data_8XCE
# 
_entry.id   8XCE 
# 
_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   8XCE         pdb_00008xce 10.2210/pdb8xce/pdb 
WWPDB D_1300043109 ?            ?                   
# 
_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       2025-06-11 
_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                        8XCE 
_pdbx_database_status.recvd_initial_deposition_date   2023-12-08 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBJ 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           N 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              min.lu@shsmu.edu.cn 
_pdbx_contact_author.name_first         Min 
_pdbx_contact_author.name_last          Lu 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-6902-3751 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Wang, Z.'   1 0000-0002-8043-7522 
'Shujun, X.' 2 ?                   
'Yigang, T.' 3 ?                   
'Derun, Z.'  4 ?                   
'Jiaqi, W.'  5 ?                   
'Kai, K.'    6 ?                   
'Lu, M.'     7 ?                   
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     'cocrystal structure of p53 in complex of B23' 
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Wang, Z.'     1  ? 
primary 'Taijie, G.'   2  ? 
primary 'Shujun, X.'   3  ? 
primary 'Huaxin, S.'   4  ? 
primary 'Yigang, T.'   5  ? 
primary 'Xueqin, C.'   6  ? 
primary 'Fangfang, S.' 7  ? 
primary 'Kai, K.'      8  ? 
primary 'Lirong, Z.'   9  ? 
primary 'Derun, Z.'    10 ? 
primary 'Jiaqi, W.'    11 ? 
primary 'Jingyi, C.'   12 ? 
primary 'Hesong, Z.'   13 ? 
primary 'Lu, M.'       14 ? 
# 
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 'Cellular tumor antigen p53'                                                                  22505.582 4  ? ? ? 
? 
2 non-polymer syn 'ZINC ION'                                                                                    65.409    4  ? ? ? 
? 
3 non-polymer syn '2-[(2~{Z})-2-(3-ethynylphenyl)imino-4-oxidanylidene-1,3-thiazolidin-5-ylidene]ethanoic acid' 272.279   1  ? ? ? 
? 
4 water       nat water                                                                                         18.015    83 ? ? ? 
? 
# 
_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       
;SSSVPSQKTYQGSYGFRLGFLHSGTAKSVTCTYSPALNKMFCQLAKTCPVQLWVDSTPPPGTRVRAMAIYKQSQHMTEVV
RRCPHHERCSDSDGLAPPQHLIRVEGNLRVEYLDDRNTFRHSVVVPYEPPEVGSDCTTIHYNYMCNSSCMGGMNRRPILT
IITLEDSSGNLLGRNSFEVRVCACPGRDRRTEEENLRKKG
;
_entity_poly.pdbx_seq_one_letter_code_can   
;SSSVPSQKTYQGSYGFRLGFLHSGTAKSVTCTYSPALNKMFCQLAKTCPVQLWVDSTPPPGTRVRAMAIYKQSQHMTEVV
RRCPHHERCSDSDGLAPPQHLIRVEGNLRVEYLDDRNTFRHSVVVPYEPPEVGSDCTTIHYNYMCNSSCMGGMNRRPILT
IITLEDSSGNLLGRNSFEVRVCACPGRDRRTEEENLRKKG
;
_entity_poly.pdbx_strand_id                 A,B,C,D 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'ZINC ION'                                                                                    ZN    
3 '2-[(2~{Z})-2-(3-ethynylphenyl)imino-4-oxidanylidene-1,3-thiazolidin-5-ylidene]ethanoic acid' A1LU0 
4 water                                                                                         HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   SER n 
1 2   SER n 
1 3   SER n 
1 4   VAL n 
1 5   PRO n 
1 6   SER n 
1 7   GLN n 
1 8   LYS n 
1 9   THR n 
1 10  TYR n 
1 11  GLN n 
1 12  GLY n 
1 13  SER n 
1 14  TYR n 
1 15  GLY n 
1 16  PHE n 
1 17  ARG n 
1 18  LEU n 
1 19  GLY n 
1 20  PHE n 
1 21  LEU n 
1 22  HIS n 
1 23  SER n 
1 24  GLY n 
1 25  THR n 
1 26  ALA n 
1 27  LYS n 
1 28  SER n 
1 29  VAL n 
1 30  THR n 
1 31  CYS n 
1 32  THR n 
1 33  TYR n 
1 34  SER n 
1 35  PRO n 
1 36  ALA n 
1 37  LEU n 
1 38  ASN n 
1 39  LYS n 
1 40  MET n 
1 41  PHE n 
1 42  CYS n 
1 43  GLN n 
1 44  LEU n 
1 45  ALA n 
1 46  LYS n 
1 47  THR n 
1 48  CYS n 
1 49  PRO n 
1 50  VAL n 
1 51  GLN n 
1 52  LEU n 
1 53  TRP n 
1 54  VAL n 
1 55  ASP n 
1 56  SER n 
1 57  THR n 
1 58  PRO n 
1 59  PRO n 
1 60  PRO n 
1 61  GLY n 
1 62  THR n 
1 63  ARG n 
1 64  VAL n 
1 65  ARG n 
1 66  ALA n 
1 67  MET n 
1 68  ALA n 
1 69  ILE n 
1 70  TYR n 
1 71  LYS n 
1 72  GLN n 
1 73  SER n 
1 74  GLN n 
1 75  HIS n 
1 76  MET n 
1 77  THR n 
1 78  GLU n 
1 79  VAL n 
1 80  VAL n 
1 81  ARG n 
1 82  ARG n 
1 83  CYS n 
1 84  PRO n 
1 85  HIS n 
1 86  HIS n 
1 87  GLU n 
1 88  ARG n 
1 89  CYS n 
1 90  SER n 
1 91  ASP n 
1 92  SER n 
1 93  ASP n 
1 94  GLY n 
1 95  LEU n 
1 96  ALA n 
1 97  PRO n 
1 98  PRO n 
1 99  GLN n 
1 100 HIS n 
1 101 LEU n 
1 102 ILE n 
1 103 ARG n 
1 104 VAL n 
1 105 GLU n 
1 106 GLY n 
1 107 ASN n 
1 108 LEU n 
1 109 ARG n 
1 110 VAL n 
1 111 GLU n 
1 112 TYR n 
1 113 LEU n 
1 114 ASP n 
1 115 ASP n 
1 116 ARG n 
1 117 ASN n 
1 118 THR n 
1 119 PHE n 
1 120 ARG n 
1 121 HIS n 
1 122 SER n 
1 123 VAL n 
1 124 VAL n 
1 125 VAL n 
1 126 PRO n 
1 127 TYR n 
1 128 GLU n 
1 129 PRO n 
1 130 PRO n 
1 131 GLU n 
1 132 VAL n 
1 133 GLY n 
1 134 SER n 
1 135 ASP n 
1 136 CYS n 
1 137 THR n 
1 138 THR n 
1 139 ILE n 
1 140 HIS n 
1 141 TYR n 
1 142 ASN n 
1 143 TYR n 
1 144 MET n 
1 145 CYS n 
1 146 ASN n 
1 147 SER n 
1 148 SER n 
1 149 CYS n 
1 150 MET n 
1 151 GLY n 
1 152 GLY n 
1 153 MET n 
1 154 ASN n 
1 155 ARG n 
1 156 ARG n 
1 157 PRO n 
1 158 ILE n 
1 159 LEU n 
1 160 THR n 
1 161 ILE n 
1 162 ILE n 
1 163 THR n 
1 164 LEU n 
1 165 GLU n 
1 166 ASP n 
1 167 SER n 
1 168 SER n 
1 169 GLY n 
1 170 ASN n 
1 171 LEU n 
1 172 LEU n 
1 173 GLY n 
1 174 ARG n 
1 175 ASN n 
1 176 SER n 
1 177 PHE n 
1 178 GLU n 
1 179 VAL n 
1 180 ARG n 
1 181 VAL n 
1 182 CYS n 
1 183 ALA n 
1 184 CYS n 
1 185 PRO n 
1 186 GLY n 
1 187 ARG n 
1 188 ASP n 
1 189 ARG n 
1 190 ARG n 
1 191 THR n 
1 192 GLU n 
1 193 GLU n 
1 194 GLU n 
1 195 ASN n 
1 196 LEU n 
1 197 ARG n 
1 198 LYS n 
1 199 LYS n 
1 200 GLY 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                   200 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 TP53 
_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      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_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 'BL21-Gold(DE3)pLysS AG'
;
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     866768 
_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 
A1LU0 non-polymer         . '2-[(2~{Z})-2-(3-ethynylphenyl)imino-4-oxidanylidene-1,3-thiazolidin-5-ylidene]ethanoic acid' ? 
'C13 H8 N2 O3 S' 272.279 
ALA   'L-peptide linking' y ALANINE                                                                                       ? 
'C3 H7 N O2'     89.093  
ARG   'L-peptide linking' y ARGININE                                                                                      ? 
'C6 H15 N4 O2 1' 175.209 
ASN   'L-peptide linking' y ASPARAGINE                                                                                    ? 
'C4 H8 N2 O3'    132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID'                                                                               ? 
'C4 H7 N O4'     133.103 
CYS   'L-peptide linking' y CYSTEINE                                                                                      ? 
'C3 H7 N O2 S'   121.158 
GLN   'L-peptide linking' y GLUTAMINE                                                                                     ? 
'C5 H10 N2 O3'   146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID'                                                                               ? 
'C5 H9 N O4'     147.129 
GLY   'peptide linking'   y GLYCINE                                                                                       ? 
'C2 H5 N O2'     75.067  
HIS   'L-peptide linking' y HISTIDINE                                                                                     ? 
'C6 H10 N3 O2 1' 156.162 
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 
PHE   'L-peptide linking' y PHENYLALANINE                                                                                 ? 
'C9 H11 N O2'    165.189 
PRO   'L-peptide linking' y PROLINE                                                                                       ? 
'C5 H9 N O2'     115.130 
SER   'L-peptide linking' y SERINE                                                                                        ? 
'C3 H7 N O3'     105.093 
THR   'L-peptide linking' y THREONINE                                                                                     ? 
'C4 H9 N O3'     119.119 
TRP   'L-peptide linking' y TRYPTOPHAN                                                                                    ? 
'C11 H12 N2 O2'  204.225 
TYR   'L-peptide linking' y TYROSINE                                                                                      ? 
'C9 H11 N O3'    181.189 
VAL   'L-peptide linking' y VALINE                                                                                        ? 
'C5 H11 N O2'    117.146 
ZN    non-polymer         . 'ZINC ION'                                                                                    ? 'Zn 2' 
65.409  
# 
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   SER 1   94  ?   ?   ?   A . n 
A 1 2   SER 2   95  ?   ?   ?   A . n 
A 1 3   SER 3   96  96  SER SER A . n 
A 1 4   VAL 4   97  97  VAL VAL A . n 
A 1 5   PRO 5   98  98  PRO PRO A . n 
A 1 6   SER 6   99  99  SER SER A . n 
A 1 7   GLN 7   100 100 GLN GLN A . n 
A 1 8   LYS 8   101 101 LYS LYS A . n 
A 1 9   THR 9   102 102 THR THR A . n 
A 1 10  TYR 10  103 103 TYR TYR A . n 
A 1 11  GLN 11  104 104 GLN GLN A . n 
A 1 12  GLY 12  105 105 GLY GLY A . n 
A 1 13  SER 13  106 106 SER SER A . n 
A 1 14  TYR 14  107 107 TYR TYR A . n 
A 1 15  GLY 15  108 108 GLY GLY A . n 
A 1 16  PHE 16  109 109 PHE PHE A . n 
A 1 17  ARG 17  110 110 ARG ARG A . n 
A 1 18  LEU 18  111 111 LEU LEU A . n 
A 1 19  GLY 19  112 112 GLY GLY A . n 
A 1 20  PHE 20  113 113 PHE PHE A . n 
A 1 21  LEU 21  114 114 LEU LEU A . n 
A 1 22  HIS 22  115 115 HIS HIS A . n 
A 1 23  SER 23  116 116 SER SER A . n 
A 1 24  GLY 24  117 117 GLY GLY A . n 
A 1 25  THR 25  118 118 THR THR A . n 
A 1 26  ALA 26  119 119 ALA ALA A . n 
A 1 27  LYS 27  120 120 LYS LYS A . n 
A 1 28  SER 28  121 121 SER SER A . n 
A 1 29  VAL 29  122 122 VAL VAL A . n 
A 1 30  THR 30  123 123 THR THR A . n 
A 1 31  CYS 31  124 124 CYS CYS A . n 
A 1 32  THR 32  125 125 THR THR A . n 
A 1 33  TYR 33  126 126 TYR TYR A . n 
A 1 34  SER 34  127 127 SER SER A . n 
A 1 35  PRO 35  128 128 PRO PRO A . n 
A 1 36  ALA 36  129 129 ALA ALA A . n 
A 1 37  LEU 37  130 130 LEU LEU A . n 
A 1 38  ASN 38  131 131 ASN ASN A . n 
A 1 39  LYS 39  132 132 LYS LYS A . n 
A 1 40  MET 40  133 133 MET MET A . n 
A 1 41  PHE 41  134 134 PHE PHE A . n 
A 1 42  CYS 42  135 135 CYS CYS A . n 
A 1 43  GLN 43  136 136 GLN GLN A . n 
A 1 44  LEU 44  137 137 LEU LEU A . n 
A 1 45  ALA 45  138 138 ALA ALA A . n 
A 1 46  LYS 46  139 139 LYS LYS A . n 
A 1 47  THR 47  140 140 THR THR A . n 
A 1 48  CYS 48  141 141 CYS CYS A . n 
A 1 49  PRO 49  142 142 PRO PRO A . n 
A 1 50  VAL 50  143 143 VAL VAL A . n 
A 1 51  GLN 51  144 144 GLN GLN A . n 
A 1 52  LEU 52  145 145 LEU LEU A . n 
A 1 53  TRP 53  146 146 TRP TRP A . n 
A 1 54  VAL 54  147 147 VAL VAL A . n 
A 1 55  ASP 55  148 148 ASP ASP A . n 
A 1 56  SER 56  149 149 SER SER A . n 
A 1 57  THR 57  150 150 THR THR A . n 
A 1 58  PRO 58  151 151 PRO PRO A . n 
A 1 59  PRO 59  152 152 PRO PRO A . n 
A 1 60  PRO 60  153 153 PRO PRO A . n 
A 1 61  GLY 61  154 154 GLY GLY A . n 
A 1 62  THR 62  155 155 THR THR A . n 
A 1 63  ARG 63  156 156 ARG ARG A . n 
A 1 64  VAL 64  157 157 VAL VAL A . n 
A 1 65  ARG 65  158 158 ARG ARG A . n 
A 1 66  ALA 66  159 159 ALA ALA A . n 
A 1 67  MET 67  160 160 MET MET A . n 
A 1 68  ALA 68  161 161 ALA ALA A . n 
A 1 69  ILE 69  162 162 ILE ILE A . n 
A 1 70  TYR 70  163 163 TYR TYR A . n 
A 1 71  LYS 71  164 164 LYS LYS A . n 
A 1 72  GLN 72  165 165 GLN GLN A . n 
A 1 73  SER 73  166 166 SER SER A . n 
A 1 74  GLN 74  167 167 GLN GLN A . n 
A 1 75  HIS 75  168 168 HIS HIS A . n 
A 1 76  MET 76  169 169 MET MET A . n 
A 1 77  THR 77  170 170 THR THR A . n 
A 1 78  GLU 78  171 171 GLU GLU A . n 
A 1 79  VAL 79  172 172 VAL VAL A . n 
A 1 80  VAL 80  173 173 VAL VAL A . n 
A 1 81  ARG 81  174 174 ARG ARG A . n 
A 1 82  ARG 82  175 175 ARG ARG A . n 
A 1 83  CYS 83  176 176 CYS CYS A . n 
A 1 84  PRO 84  177 177 PRO PRO A . n 
A 1 85  HIS 85  178 178 HIS HIS A . n 
A 1 86  HIS 86  179 179 HIS HIS A . n 
A 1 87  GLU 87  180 180 GLU GLU A . n 
A 1 88  ARG 88  181 181 ARG ARG A . n 
A 1 89  CYS 89  182 182 CYS CYS A . n 
A 1 90  SER 90  183 183 SER SER A . n 
A 1 91  ASP 91  184 184 ASP ASP A . n 
A 1 92  SER 92  185 185 SER SER A . n 
A 1 93  ASP 93  186 186 ASP ASP A . n 
A 1 94  GLY 94  187 187 GLY GLY A . n 
A 1 95  LEU 95  188 188 LEU LEU A . n 
A 1 96  ALA 96  189 189 ALA ALA A . n 
A 1 97  PRO 97  190 190 PRO PRO A . n 
A 1 98  PRO 98  191 191 PRO PRO A . n 
A 1 99  GLN 99  192 192 GLN GLN A . n 
A 1 100 HIS 100 193 193 HIS HIS A . n 
A 1 101 LEU 101 194 194 LEU LEU A . n 
A 1 102 ILE 102 195 195 ILE ILE A . n 
A 1 103 ARG 103 196 196 ARG ARG A . n 
A 1 104 VAL 104 197 197 VAL VAL A . n 
A 1 105 GLU 105 198 198 GLU GLU A . n 
A 1 106 GLY 106 199 199 GLY GLY A . n 
A 1 107 ASN 107 200 200 ASN ASN A . n 
A 1 108 LEU 108 201 201 LEU LEU A . n 
A 1 109 ARG 109 202 202 ARG ARG A . n 
A 1 110 VAL 110 203 203 VAL VAL A . n 
A 1 111 GLU 111 204 204 GLU GLU A . n 
A 1 112 TYR 112 205 205 TYR TYR A . n 
A 1 113 LEU 113 206 206 LEU LEU A . n 
A 1 114 ASP 114 207 207 ASP ASP A . n 
A 1 115 ASP 115 208 208 ASP ASP A . n 
A 1 116 ARG 116 209 209 ARG ARG A . n 
A 1 117 ASN 117 210 210 ASN ASN A . n 
A 1 118 THR 118 211 211 THR THR A . n 
A 1 119 PHE 119 212 212 PHE PHE A . n 
A 1 120 ARG 120 213 213 ARG ARG A . n 
A 1 121 HIS 121 214 214 HIS HIS A . n 
A 1 122 SER 122 215 215 SER SER A . n 
A 1 123 VAL 123 216 216 VAL VAL A . n 
A 1 124 VAL 124 217 217 VAL VAL A . n 
A 1 125 VAL 125 218 218 VAL VAL A . n 
A 1 126 PRO 126 219 219 PRO PRO A . n 
A 1 127 TYR 127 220 220 TYR TYR A . n 
A 1 128 GLU 128 221 221 GLU GLU A . n 
A 1 129 PRO 129 222 222 PRO PRO A . n 
A 1 130 PRO 130 223 223 PRO PRO A . n 
A 1 131 GLU 131 224 224 GLU GLU A . n 
A 1 132 VAL 132 225 225 VAL VAL A . n 
A 1 133 GLY 133 226 226 GLY GLY A . n 
A 1 134 SER 134 227 227 SER SER A . n 
A 1 135 ASP 135 228 228 ASP ASP A . n 
A 1 136 CYS 136 229 229 CYS CYS A . n 
A 1 137 THR 137 230 230 THR THR A . n 
A 1 138 THR 138 231 231 THR THR A . n 
A 1 139 ILE 139 232 232 ILE ILE A . n 
A 1 140 HIS 140 233 233 HIS HIS A . n 
A 1 141 TYR 141 234 234 TYR TYR A . n 
A 1 142 ASN 142 235 235 ASN ASN A . n 
A 1 143 TYR 143 236 236 TYR TYR A . n 
A 1 144 MET 144 237 237 MET MET A . n 
A 1 145 CYS 145 238 238 CYS CYS A . n 
A 1 146 ASN 146 239 239 ASN ASN A . n 
A 1 147 SER 147 240 240 SER SER A . n 
A 1 148 SER 148 241 241 SER SER A . n 
A 1 149 CYS 149 242 242 CYS CYS A . n 
A 1 150 MET 150 243 243 MET MET A . n 
A 1 151 GLY 151 244 244 GLY GLY A . n 
A 1 152 GLY 152 245 245 GLY GLY A . n 
A 1 153 MET 153 246 246 MET MET A . n 
A 1 154 ASN 154 247 247 ASN ASN A . n 
A 1 155 ARG 155 248 248 ARG ARG A . n 
A 1 156 ARG 156 249 249 ARG ARG A . n 
A 1 157 PRO 157 250 250 PRO PRO A . n 
A 1 158 ILE 158 251 251 ILE ILE A . n 
A 1 159 LEU 159 252 252 LEU LEU A . n 
A 1 160 THR 160 253 253 THR THR A . n 
A 1 161 ILE 161 254 254 ILE ILE A . n 
A 1 162 ILE 162 255 255 ILE ILE A . n 
A 1 163 THR 163 256 256 THR THR A . n 
A 1 164 LEU 164 257 257 LEU LEU A . n 
A 1 165 GLU 165 258 258 GLU GLU A . n 
A 1 166 ASP 166 259 259 ASP ASP A . n 
A 1 167 SER 167 260 260 SER SER A . n 
A 1 168 SER 168 261 261 SER SER A . n 
A 1 169 GLY 169 262 262 GLY GLY A . n 
A 1 170 ASN 170 263 263 ASN ASN A . n 
A 1 171 LEU 171 264 264 LEU LEU A . n 
A 1 172 LEU 172 265 265 LEU LEU A . n 
A 1 173 GLY 173 266 266 GLY GLY A . n 
A 1 174 ARG 174 267 267 ARG ARG A . n 
A 1 175 ASN 175 268 268 ASN ASN A . n 
A 1 176 SER 176 269 269 SER SER A . n 
A 1 177 PHE 177 270 270 PHE PHE A . n 
A 1 178 GLU 178 271 271 GLU GLU A . n 
A 1 179 VAL 179 272 272 VAL VAL A . n 
A 1 180 ARG 180 273 273 ARG ARG A . n 
A 1 181 VAL 181 274 274 VAL VAL A . n 
A 1 182 CYS 182 275 275 CYS CYS A . n 
A 1 183 ALA 183 276 276 ALA ALA A . n 
A 1 184 CYS 184 277 277 CYS CYS A . n 
A 1 185 PRO 185 278 278 PRO PRO A . n 
A 1 186 GLY 186 279 279 GLY GLY A . n 
A 1 187 ARG 187 280 280 ARG ARG A . n 
A 1 188 ASP 188 281 281 ASP ASP A . n 
A 1 189 ARG 189 282 282 ARG ARG A . n 
A 1 190 ARG 190 283 283 ARG ARG A . n 
A 1 191 THR 191 284 284 THR THR A . n 
A 1 192 GLU 192 285 285 GLU GLU A . n 
A 1 193 GLU 193 286 286 GLU GLU A . n 
A 1 194 GLU 194 287 287 GLU GLU A . n 
A 1 195 ASN 195 288 288 ASN ASN A . n 
A 1 196 LEU 196 289 ?   ?   ?   A . n 
A 1 197 ARG 197 290 ?   ?   ?   A . n 
A 1 198 LYS 198 291 ?   ?   ?   A . n 
A 1 199 LYS 199 292 ?   ?   ?   A . n 
A 1 200 GLY 200 293 ?   ?   ?   A . n 
B 1 1   SER 1   94  ?   ?   ?   B . n 
B 1 2   SER 2   95  ?   ?   ?   B . n 
B 1 3   SER 3   96  ?   ?   ?   B . n 
B 1 4   VAL 4   97  97  VAL VAL B . n 
B 1 5   PRO 5   98  98  PRO PRO B . n 
B 1 6   SER 6   99  99  SER SER B . n 
B 1 7   GLN 7   100 100 GLN GLN B . n 
B 1 8   LYS 8   101 101 LYS LYS B . n 
B 1 9   THR 9   102 102 THR THR B . n 
B 1 10  TYR 10  103 103 TYR TYR B . n 
B 1 11  GLN 11  104 104 GLN GLN B . n 
B 1 12  GLY 12  105 105 GLY GLY B . n 
B 1 13  SER 13  106 106 SER SER B . n 
B 1 14  TYR 14  107 107 TYR TYR B . n 
B 1 15  GLY 15  108 108 GLY GLY B . n 
B 1 16  PHE 16  109 109 PHE PHE B . n 
B 1 17  ARG 17  110 110 ARG ARG B . n 
B 1 18  LEU 18  111 111 LEU LEU B . n 
B 1 19  GLY 19  112 112 GLY GLY B . n 
B 1 20  PHE 20  113 113 PHE PHE B . n 
B 1 21  LEU 21  114 114 LEU LEU B . n 
B 1 22  HIS 22  115 115 HIS HIS B . n 
B 1 23  SER 23  116 116 SER SER B . n 
B 1 24  GLY 24  117 117 GLY GLY B . n 
B 1 25  THR 25  118 118 THR THR B . n 
B 1 26  ALA 26  119 119 ALA ALA B . n 
B 1 27  LYS 27  120 120 LYS LYS B . n 
B 1 28  SER 28  121 121 SER SER B . n 
B 1 29  VAL 29  122 122 VAL VAL B . n 
B 1 30  THR 30  123 123 THR THR B . n 
B 1 31  CYS 31  124 124 CYS CYS B . n 
B 1 32  THR 32  125 125 THR THR B . n 
B 1 33  TYR 33  126 126 TYR TYR B . n 
B 1 34  SER 34  127 127 SER SER B . n 
B 1 35  PRO 35  128 128 PRO PRO B . n 
B 1 36  ALA 36  129 129 ALA ALA B . n 
B 1 37  LEU 37  130 130 LEU LEU B . n 
B 1 38  ASN 38  131 131 ASN ASN B . n 
B 1 39  LYS 39  132 132 LYS LYS B . n 
B 1 40  MET 40  133 133 MET MET B . n 
B 1 41  PHE 41  134 134 PHE PHE B . n 
B 1 42  CYS 42  135 135 CYS CYS B . n 
B 1 43  GLN 43  136 136 GLN GLN B . n 
B 1 44  LEU 44  137 137 LEU LEU B . n 
B 1 45  ALA 45  138 138 ALA ALA B . n 
B 1 46  LYS 46  139 139 LYS LYS B . n 
B 1 47  THR 47  140 140 THR THR B . n 
B 1 48  CYS 48  141 141 CYS CYS B . n 
B 1 49  PRO 49  142 142 PRO PRO B . n 
B 1 50  VAL 50  143 143 VAL VAL B . n 
B 1 51  GLN 51  144 144 GLN GLN B . n 
B 1 52  LEU 52  145 145 LEU LEU B . n 
B 1 53  TRP 53  146 146 TRP TRP B . n 
B 1 54  VAL 54  147 147 VAL VAL B . n 
B 1 55  ASP 55  148 148 ASP ASP B . n 
B 1 56  SER 56  149 149 SER SER B . n 
B 1 57  THR 57  150 150 THR THR B . n 
B 1 58  PRO 58  151 151 PRO PRO B . n 
B 1 59  PRO 59  152 152 PRO PRO B . n 
B 1 60  PRO 60  153 153 PRO PRO B . n 
B 1 61  GLY 61  154 154 GLY GLY B . n 
B 1 62  THR 62  155 155 THR THR B . n 
B 1 63  ARG 63  156 156 ARG ARG B . n 
B 1 64  VAL 64  157 157 VAL VAL B . n 
B 1 65  ARG 65  158 158 ARG ARG B . n 
B 1 66  ALA 66  159 159 ALA ALA B . n 
B 1 67  MET 67  160 160 MET MET B . n 
B 1 68  ALA 68  161 161 ALA ALA B . n 
B 1 69  ILE 69  162 162 ILE ILE B . n 
B 1 70  TYR 70  163 163 TYR TYR B . n 
B 1 71  LYS 71  164 164 LYS LYS B . n 
B 1 72  GLN 72  165 165 GLN GLN B . n 
B 1 73  SER 73  166 166 SER SER B . n 
B 1 74  GLN 74  167 167 GLN GLN B . n 
B 1 75  HIS 75  168 168 HIS HIS B . n 
B 1 76  MET 76  169 169 MET MET B . n 
B 1 77  THR 77  170 170 THR THR B . n 
B 1 78  GLU 78  171 171 GLU GLU B . n 
B 1 79  VAL 79  172 172 VAL VAL B . n 
B 1 80  VAL 80  173 173 VAL VAL B . n 
B 1 81  ARG 81  174 174 ARG ARG B . n 
B 1 82  ARG 82  175 175 ARG ARG B . n 
B 1 83  CYS 83  176 176 CYS CYS B . n 
B 1 84  PRO 84  177 177 PRO PRO B . n 
B 1 85  HIS 85  178 178 HIS HIS B . n 
B 1 86  HIS 86  179 179 HIS HIS B . n 
B 1 87  GLU 87  180 180 GLU GLU B . n 
B 1 88  ARG 88  181 181 ARG ARG B . n 
B 1 89  CYS 89  182 182 CYS CYS B . n 
B 1 90  SER 90  183 183 SER SER B . n 
B 1 91  ASP 91  184 184 ASP ASP B . n 
B 1 92  SER 92  185 185 SER SER B . n 
B 1 93  ASP 93  186 186 ASP ASP B . n 
B 1 94  GLY 94  187 187 GLY GLY B . n 
B 1 95  LEU 95  188 188 LEU LEU B . n 
B 1 96  ALA 96  189 189 ALA ALA B . n 
B 1 97  PRO 97  190 190 PRO PRO B . n 
B 1 98  PRO 98  191 191 PRO PRO B . n 
B 1 99  GLN 99  192 192 GLN GLN B . n 
B 1 100 HIS 100 193 193 HIS HIS B . n 
B 1 101 LEU 101 194 194 LEU LEU B . n 
B 1 102 ILE 102 195 195 ILE ILE B . n 
B 1 103 ARG 103 196 196 ARG ARG B . n 
B 1 104 VAL 104 197 197 VAL VAL B . n 
B 1 105 GLU 105 198 198 GLU GLU B . n 
B 1 106 GLY 106 199 199 GLY GLY B . n 
B 1 107 ASN 107 200 200 ASN ASN B . n 
B 1 108 LEU 108 201 201 LEU LEU B . n 
B 1 109 ARG 109 202 202 ARG ARG B . n 
B 1 110 VAL 110 203 203 VAL VAL B . n 
B 1 111 GLU 111 204 204 GLU GLU B . n 
B 1 112 TYR 112 205 205 TYR TYR B . n 
B 1 113 LEU 113 206 206 LEU LEU B . n 
B 1 114 ASP 114 207 207 ASP ASP B . n 
B 1 115 ASP 115 208 208 ASP ASP B . n 
B 1 116 ARG 116 209 209 ARG ARG B . n 
B 1 117 ASN 117 210 210 ASN ASN B . n 
B 1 118 THR 118 211 211 THR THR B . n 
B 1 119 PHE 119 212 212 PHE PHE B . n 
B 1 120 ARG 120 213 213 ARG ARG B . n 
B 1 121 HIS 121 214 214 HIS HIS B . n 
B 1 122 SER 122 215 215 SER SER B . n 
B 1 123 VAL 123 216 216 VAL VAL B . n 
B 1 124 VAL 124 217 217 VAL VAL B . n 
B 1 125 VAL 125 218 218 VAL VAL B . n 
B 1 126 PRO 126 219 219 PRO PRO B . n 
B 1 127 TYR 127 220 220 TYR TYR B . n 
B 1 128 GLU 128 221 221 GLU GLU B . n 
B 1 129 PRO 129 222 222 PRO PRO B . n 
B 1 130 PRO 130 223 223 PRO PRO B . n 
B 1 131 GLU 131 224 224 GLU GLU B . n 
B 1 132 VAL 132 225 225 VAL VAL B . n 
B 1 133 GLY 133 226 226 GLY GLY B . n 
B 1 134 SER 134 227 227 SER SER B . n 
B 1 135 ASP 135 228 228 ASP ASP B . n 
B 1 136 CYS 136 229 229 CYS CYS B . n 
B 1 137 THR 137 230 230 THR THR B . n 
B 1 138 THR 138 231 231 THR THR B . n 
B 1 139 ILE 139 232 232 ILE ILE B . n 
B 1 140 HIS 140 233 233 HIS HIS B . n 
B 1 141 TYR 141 234 234 TYR TYR B . n 
B 1 142 ASN 142 235 235 ASN ASN B . n 
B 1 143 TYR 143 236 236 TYR TYR B . n 
B 1 144 MET 144 237 237 MET MET B . n 
B 1 145 CYS 145 238 238 CYS CYS B . n 
B 1 146 ASN 146 239 239 ASN ASN B . n 
B 1 147 SER 147 240 240 SER SER B . n 
B 1 148 SER 148 241 241 SER SER B . n 
B 1 149 CYS 149 242 242 CYS CYS B . n 
B 1 150 MET 150 243 243 MET MET B . n 
B 1 151 GLY 151 244 244 GLY GLY B . n 
B 1 152 GLY 152 245 245 GLY GLY B . n 
B 1 153 MET 153 246 246 MET MET B . n 
B 1 154 ASN 154 247 247 ASN ASN B . n 
B 1 155 ARG 155 248 248 ARG ARG B . n 
B 1 156 ARG 156 249 249 ARG ARG B . n 
B 1 157 PRO 157 250 250 PRO PRO B . n 
B 1 158 ILE 158 251 251 ILE ILE B . n 
B 1 159 LEU 159 252 252 LEU LEU B . n 
B 1 160 THR 160 253 253 THR THR B . n 
B 1 161 ILE 161 254 254 ILE ILE B . n 
B 1 162 ILE 162 255 255 ILE ILE B . n 
B 1 163 THR 163 256 256 THR THR B . n 
B 1 164 LEU 164 257 257 LEU LEU B . n 
B 1 165 GLU 165 258 258 GLU GLU B . n 
B 1 166 ASP 166 259 259 ASP ASP B . n 
B 1 167 SER 167 260 260 SER SER B . n 
B 1 168 SER 168 261 261 SER SER B . n 
B 1 169 GLY 169 262 262 GLY GLY B . n 
B 1 170 ASN 170 263 263 ASN ASN B . n 
B 1 171 LEU 171 264 264 LEU LEU B . n 
B 1 172 LEU 172 265 265 LEU LEU B . n 
B 1 173 GLY 173 266 266 GLY GLY B . n 
B 1 174 ARG 174 267 267 ARG ARG B . n 
B 1 175 ASN 175 268 268 ASN ASN B . n 
B 1 176 SER 176 269 269 SER SER B . n 
B 1 177 PHE 177 270 270 PHE PHE B . n 
B 1 178 GLU 178 271 271 GLU GLU B . n 
B 1 179 VAL 179 272 272 VAL VAL B . n 
B 1 180 ARG 180 273 273 ARG ARG B . n 
B 1 181 VAL 181 274 274 VAL VAL B . n 
B 1 182 CYS 182 275 275 CYS CYS B . n 
B 1 183 ALA 183 276 276 ALA ALA B . n 
B 1 184 CYS 184 277 277 CYS CYS B . n 
B 1 185 PRO 185 278 278 PRO PRO B . n 
B 1 186 GLY 186 279 279 GLY GLY B . n 
B 1 187 ARG 187 280 280 ARG ARG B . n 
B 1 188 ASP 188 281 281 ASP ASP B . n 
B 1 189 ARG 189 282 282 ARG ARG B . n 
B 1 190 ARG 190 283 283 ARG ARG B . n 
B 1 191 THR 191 284 284 THR THR B . n 
B 1 192 GLU 192 285 285 GLU GLU B . n 
B 1 193 GLU 193 286 286 GLU GLU B . n 
B 1 194 GLU 194 287 287 GLU GLU B . n 
B 1 195 ASN 195 288 288 ASN ASN B . n 
B 1 196 LEU 196 289 ?   ?   ?   B . n 
B 1 197 ARG 197 290 ?   ?   ?   B . n 
B 1 198 LYS 198 291 ?   ?   ?   B . n 
B 1 199 LYS 199 292 ?   ?   ?   B . n 
B 1 200 GLY 200 293 ?   ?   ?   B . n 
C 1 1   SER 1   94  ?   ?   ?   C . n 
C 1 2   SER 2   95  ?   ?   ?   C . n 
C 1 3   SER 3   96  96  SER SER C . n 
C 1 4   VAL 4   97  97  VAL VAL C . n 
C 1 5   PRO 5   98  98  PRO PRO C . n 
C 1 6   SER 6   99  99  SER SER C . n 
C 1 7   GLN 7   100 100 GLN GLN C . n 
C 1 8   LYS 8   101 101 LYS LYS C . n 
C 1 9   THR 9   102 102 THR THR C . n 
C 1 10  TYR 10  103 103 TYR TYR C . n 
C 1 11  GLN 11  104 104 GLN GLN C . n 
C 1 12  GLY 12  105 105 GLY GLY C . n 
C 1 13  SER 13  106 106 SER SER C . n 
C 1 14  TYR 14  107 107 TYR TYR C . n 
C 1 15  GLY 15  108 108 GLY GLY C . n 
C 1 16  PHE 16  109 109 PHE PHE C . n 
C 1 17  ARG 17  110 110 ARG ARG C . n 
C 1 18  LEU 18  111 111 LEU LEU C . n 
C 1 19  GLY 19  112 112 GLY GLY C . n 
C 1 20  PHE 20  113 113 PHE PHE C . n 
C 1 21  LEU 21  114 114 LEU LEU C . n 
C 1 22  HIS 22  115 115 HIS HIS C . n 
C 1 23  SER 23  116 116 SER SER C . n 
C 1 24  GLY 24  117 117 GLY GLY C . n 
C 1 25  THR 25  118 118 THR THR C . n 
C 1 26  ALA 26  119 119 ALA ALA C . n 
C 1 27  LYS 27  120 120 LYS LYS C . n 
C 1 28  SER 28  121 121 SER SER C . n 
C 1 29  VAL 29  122 122 VAL VAL C . n 
C 1 30  THR 30  123 123 THR THR C . n 
C 1 31  CYS 31  124 124 CYS CYS C . n 
C 1 32  THR 32  125 125 THR THR C . n 
C 1 33  TYR 33  126 126 TYR TYR C . n 
C 1 34  SER 34  127 127 SER SER C . n 
C 1 35  PRO 35  128 128 PRO PRO C . n 
C 1 36  ALA 36  129 129 ALA ALA C . n 
C 1 37  LEU 37  130 130 LEU LEU C . n 
C 1 38  ASN 38  131 131 ASN ASN C . n 
C 1 39  LYS 39  132 132 LYS LYS C . n 
C 1 40  MET 40  133 133 MET MET C . n 
C 1 41  PHE 41  134 134 PHE PHE C . n 
C 1 42  CYS 42  135 135 CYS CYS C . n 
C 1 43  GLN 43  136 136 GLN GLN C . n 
C 1 44  LEU 44  137 137 LEU LEU C . n 
C 1 45  ALA 45  138 138 ALA ALA C . n 
C 1 46  LYS 46  139 139 LYS LYS C . n 
C 1 47  THR 47  140 140 THR THR C . n 
C 1 48  CYS 48  141 141 CYS CYS C . n 
C 1 49  PRO 49  142 142 PRO PRO C . n 
C 1 50  VAL 50  143 143 VAL VAL C . n 
C 1 51  GLN 51  144 144 GLN GLN C . n 
C 1 52  LEU 52  145 145 LEU LEU C . n 
C 1 53  TRP 53  146 146 TRP TRP C . n 
C 1 54  VAL 54  147 147 VAL VAL C . n 
C 1 55  ASP 55  148 148 ASP ASP C . n 
C 1 56  SER 56  149 149 SER SER C . n 
C 1 57  THR 57  150 150 THR THR C . n 
C 1 58  PRO 58  151 151 PRO PRO C . n 
C 1 59  PRO 59  152 152 PRO PRO C . n 
C 1 60  PRO 60  153 153 PRO PRO C . n 
C 1 61  GLY 61  154 154 GLY GLY C . n 
C 1 62  THR 62  155 155 THR THR C . n 
C 1 63  ARG 63  156 156 ARG ARG C . n 
C 1 64  VAL 64  157 157 VAL VAL C . n 
C 1 65  ARG 65  158 158 ARG ARG C . n 
C 1 66  ALA 66  159 159 ALA ALA C . n 
C 1 67  MET 67  160 160 MET MET C . n 
C 1 68  ALA 68  161 161 ALA ALA C . n 
C 1 69  ILE 69  162 162 ILE ILE C . n 
C 1 70  TYR 70  163 163 TYR TYR C . n 
C 1 71  LYS 71  164 164 LYS LYS C . n 
C 1 72  GLN 72  165 165 GLN GLN C . n 
C 1 73  SER 73  166 166 SER SER C . n 
C 1 74  GLN 74  167 167 GLN GLN C . n 
C 1 75  HIS 75  168 168 HIS HIS C . n 
C 1 76  MET 76  169 169 MET MET C . n 
C 1 77  THR 77  170 170 THR THR C . n 
C 1 78  GLU 78  171 171 GLU GLU C . n 
C 1 79  VAL 79  172 172 VAL VAL C . n 
C 1 80  VAL 80  173 173 VAL VAL C . n 
C 1 81  ARG 81  174 174 ARG ARG C . n 
C 1 82  ARG 82  175 175 ARG ARG C . n 
C 1 83  CYS 83  176 176 CYS CYS C . n 
C 1 84  PRO 84  177 177 PRO PRO C . n 
C 1 85  HIS 85  178 178 HIS HIS C . n 
C 1 86  HIS 86  179 179 HIS HIS C . n 
C 1 87  GLU 87  180 180 GLU GLU C . n 
C 1 88  ARG 88  181 181 ARG ARG C . n 
C 1 89  CYS 89  182 ?   ?   ?   C . n 
C 1 90  SER 90  183 ?   ?   ?   C . n 
C 1 91  ASP 91  184 ?   ?   ?   C . n 
C 1 92  SER 92  185 185 SER SER C . n 
C 1 93  ASP 93  186 186 ASP ASP C . n 
C 1 94  GLY 94  187 187 GLY GLY C . n 
C 1 95  LEU 95  188 188 LEU LEU C . n 
C 1 96  ALA 96  189 189 ALA ALA C . n 
C 1 97  PRO 97  190 190 PRO PRO C . n 
C 1 98  PRO 98  191 191 PRO PRO C . n 
C 1 99  GLN 99  192 192 GLN GLN C . n 
C 1 100 HIS 100 193 193 HIS HIS C . n 
C 1 101 LEU 101 194 194 LEU LEU C . n 
C 1 102 ILE 102 195 195 ILE ILE C . n 
C 1 103 ARG 103 196 196 ARG ARG C . n 
C 1 104 VAL 104 197 197 VAL VAL C . n 
C 1 105 GLU 105 198 198 GLU GLU C . n 
C 1 106 GLY 106 199 199 GLY GLY C . n 
C 1 107 ASN 107 200 200 ASN ASN C . n 
C 1 108 LEU 108 201 201 LEU LEU C . n 
C 1 109 ARG 109 202 202 ARG ARG C . n 
C 1 110 VAL 110 203 203 VAL VAL C . n 
C 1 111 GLU 111 204 204 GLU GLU C . n 
C 1 112 TYR 112 205 205 TYR TYR C . n 
C 1 113 LEU 113 206 206 LEU LEU C . n 
C 1 114 ASP 114 207 207 ASP ASP C . n 
C 1 115 ASP 115 208 208 ASP ASP C . n 
C 1 116 ARG 116 209 209 ARG ARG C . n 
C 1 117 ASN 117 210 210 ASN ASN C . n 
C 1 118 THR 118 211 211 THR THR C . n 
C 1 119 PHE 119 212 212 PHE PHE C . n 
C 1 120 ARG 120 213 213 ARG ARG C . n 
C 1 121 HIS 121 214 214 HIS HIS C . n 
C 1 122 SER 122 215 215 SER SER C . n 
C 1 123 VAL 123 216 216 VAL VAL C . n 
C 1 124 VAL 124 217 217 VAL VAL C . n 
C 1 125 VAL 125 218 218 VAL VAL C . n 
C 1 126 PRO 126 219 219 PRO PRO C . n 
C 1 127 TYR 127 220 220 TYR TYR C . n 
C 1 128 GLU 128 221 221 GLU GLU C . n 
C 1 129 PRO 129 222 222 PRO PRO C . n 
C 1 130 PRO 130 223 223 PRO PRO C . n 
C 1 131 GLU 131 224 224 GLU GLU C . n 
C 1 132 VAL 132 225 225 VAL VAL C . n 
C 1 133 GLY 133 226 226 GLY GLY C . n 
C 1 134 SER 134 227 227 SER SER C . n 
C 1 135 ASP 135 228 228 ASP ASP C . n 
C 1 136 CYS 136 229 229 CYS CYS C . n 
C 1 137 THR 137 230 230 THR THR C . n 
C 1 138 THR 138 231 231 THR THR C . n 
C 1 139 ILE 139 232 232 ILE ILE C . n 
C 1 140 HIS 140 233 233 HIS HIS C . n 
C 1 141 TYR 141 234 234 TYR TYR C . n 
C 1 142 ASN 142 235 235 ASN ASN C . n 
C 1 143 TYR 143 236 236 TYR TYR C . n 
C 1 144 MET 144 237 237 MET MET C . n 
C 1 145 CYS 145 238 238 CYS CYS C . n 
C 1 146 ASN 146 239 239 ASN ASN C . n 
C 1 147 SER 147 240 240 SER SER C . n 
C 1 148 SER 148 241 241 SER SER C . n 
C 1 149 CYS 149 242 242 CYS CYS C . n 
C 1 150 MET 150 243 243 MET MET C . n 
C 1 151 GLY 151 244 244 GLY GLY C . n 
C 1 152 GLY 152 245 245 GLY GLY C . n 
C 1 153 MET 153 246 246 MET MET C . n 
C 1 154 ASN 154 247 247 ASN ASN C . n 
C 1 155 ARG 155 248 248 ARG ARG C . n 
C 1 156 ARG 156 249 249 ARG ARG C . n 
C 1 157 PRO 157 250 250 PRO PRO C . n 
C 1 158 ILE 158 251 251 ILE ILE C . n 
C 1 159 LEU 159 252 252 LEU LEU C . n 
C 1 160 THR 160 253 253 THR THR C . n 
C 1 161 ILE 161 254 254 ILE ILE C . n 
C 1 162 ILE 162 255 255 ILE ILE C . n 
C 1 163 THR 163 256 256 THR THR C . n 
C 1 164 LEU 164 257 257 LEU LEU C . n 
C 1 165 GLU 165 258 258 GLU GLU C . n 
C 1 166 ASP 166 259 259 ASP ASP C . n 
C 1 167 SER 167 260 260 SER SER C . n 
C 1 168 SER 168 261 261 SER SER C . n 
C 1 169 GLY 169 262 262 GLY GLY C . n 
C 1 170 ASN 170 263 263 ASN ASN C . n 
C 1 171 LEU 171 264 264 LEU LEU C . n 
C 1 172 LEU 172 265 265 LEU LEU C . n 
C 1 173 GLY 173 266 266 GLY GLY C . n 
C 1 174 ARG 174 267 267 ARG ARG C . n 
C 1 175 ASN 175 268 268 ASN ASN C . n 
C 1 176 SER 176 269 269 SER SER C . n 
C 1 177 PHE 177 270 270 PHE PHE C . n 
C 1 178 GLU 178 271 271 GLU GLU C . n 
C 1 179 VAL 179 272 272 VAL VAL C . n 
C 1 180 ARG 180 273 273 ARG ARG C . n 
C 1 181 VAL 181 274 274 VAL VAL C . n 
C 1 182 CYS 182 275 275 CYS CYS C . n 
C 1 183 ALA 183 276 276 ALA ALA C . n 
C 1 184 CYS 184 277 277 CYS CYS C . n 
C 1 185 PRO 185 278 278 PRO PRO C . n 
C 1 186 GLY 186 279 279 GLY GLY C . n 
C 1 187 ARG 187 280 280 ARG ARG C . n 
C 1 188 ASP 188 281 281 ASP ASP C . n 
C 1 189 ARG 189 282 282 ARG ARG C . n 
C 1 190 ARG 190 283 283 ARG ARG C . n 
C 1 191 THR 191 284 284 THR THR C . n 
C 1 192 GLU 192 285 285 GLU GLU C . n 
C 1 193 GLU 193 286 286 GLU GLU C . n 
C 1 194 GLU 194 287 287 GLU GLU C . n 
C 1 195 ASN 195 288 288 ASN ASN C . n 
C 1 196 LEU 196 289 ?   ?   ?   C . n 
C 1 197 ARG 197 290 ?   ?   ?   C . n 
C 1 198 LYS 198 291 ?   ?   ?   C . n 
C 1 199 LYS 199 292 ?   ?   ?   C . n 
C 1 200 GLY 200 293 ?   ?   ?   C . n 
D 1 1   SER 1   94  ?   ?   ?   D . n 
D 1 2   SER 2   95  95  SER SER D . n 
D 1 3   SER 3   96  96  SER SER D . n 
D 1 4   VAL 4   97  97  VAL VAL D . n 
D 1 5   PRO 5   98  98  PRO PRO D . n 
D 1 6   SER 6   99  99  SER SER D . n 
D 1 7   GLN 7   100 100 GLN GLN D . n 
D 1 8   LYS 8   101 101 LYS LYS D . n 
D 1 9   THR 9   102 102 THR THR D . n 
D 1 10  TYR 10  103 103 TYR TYR D . n 
D 1 11  GLN 11  104 104 GLN GLN D . n 
D 1 12  GLY 12  105 105 GLY GLY D . n 
D 1 13  SER 13  106 106 SER SER D . n 
D 1 14  TYR 14  107 107 TYR TYR D . n 
D 1 15  GLY 15  108 108 GLY GLY D . n 
D 1 16  PHE 16  109 109 PHE PHE D . n 
D 1 17  ARG 17  110 110 ARG ARG D . n 
D 1 18  LEU 18  111 111 LEU LEU D . n 
D 1 19  GLY 19  112 112 GLY GLY D . n 
D 1 20  PHE 20  113 113 PHE PHE D . n 
D 1 21  LEU 21  114 114 LEU LEU D . n 
D 1 22  HIS 22  115 115 HIS HIS D . n 
D 1 23  SER 23  116 116 SER SER D . n 
D 1 24  GLY 24  117 117 GLY GLY D . n 
D 1 25  THR 25  118 118 THR THR D . n 
D 1 26  ALA 26  119 119 ALA ALA D . n 
D 1 27  LYS 27  120 120 LYS LYS D . n 
D 1 28  SER 28  121 121 SER SER D . n 
D 1 29  VAL 29  122 122 VAL VAL D . n 
D 1 30  THR 30  123 123 THR THR D . n 
D 1 31  CYS 31  124 124 CYS CYS D . n 
D 1 32  THR 32  125 125 THR THR D . n 
D 1 33  TYR 33  126 126 TYR TYR D . n 
D 1 34  SER 34  127 127 SER SER D . n 
D 1 35  PRO 35  128 128 PRO PRO D . n 
D 1 36  ALA 36  129 129 ALA ALA D . n 
D 1 37  LEU 37  130 130 LEU LEU D . n 
D 1 38  ASN 38  131 131 ASN ASN D . n 
D 1 39  LYS 39  132 132 LYS LYS D . n 
D 1 40  MET 40  133 133 MET MET D . n 
D 1 41  PHE 41  134 134 PHE PHE D . n 
D 1 42  CYS 42  135 135 CYS CYS D . n 
D 1 43  GLN 43  136 136 GLN GLN D . n 
D 1 44  LEU 44  137 137 LEU LEU D . n 
D 1 45  ALA 45  138 138 ALA ALA D . n 
D 1 46  LYS 46  139 139 LYS LYS D . n 
D 1 47  THR 47  140 140 THR THR D . n 
D 1 48  CYS 48  141 141 CYS CYS D . n 
D 1 49  PRO 49  142 142 PRO PRO D . n 
D 1 50  VAL 50  143 143 VAL VAL D . n 
D 1 51  GLN 51  144 144 GLN GLN D . n 
D 1 52  LEU 52  145 145 LEU LEU D . n 
D 1 53  TRP 53  146 146 TRP TRP D . n 
D 1 54  VAL 54  147 147 VAL VAL D . n 
D 1 55  ASP 55  148 148 ASP ASP D . n 
D 1 56  SER 56  149 149 SER SER D . n 
D 1 57  THR 57  150 150 THR THR D . n 
D 1 58  PRO 58  151 151 PRO PRO D . n 
D 1 59  PRO 59  152 152 PRO PRO D . n 
D 1 60  PRO 60  153 153 PRO PRO D . n 
D 1 61  GLY 61  154 154 GLY GLY D . n 
D 1 62  THR 62  155 155 THR THR D . n 
D 1 63  ARG 63  156 156 ARG ARG D . n 
D 1 64  VAL 64  157 157 VAL VAL D . n 
D 1 65  ARG 65  158 158 ARG ARG D . n 
D 1 66  ALA 66  159 159 ALA ALA D . n 
D 1 67  MET 67  160 160 MET MET D . n 
D 1 68  ALA 68  161 161 ALA ALA D . n 
D 1 69  ILE 69  162 162 ILE ILE D . n 
D 1 70  TYR 70  163 163 TYR TYR D . n 
D 1 71  LYS 71  164 164 LYS LYS D . n 
D 1 72  GLN 72  165 165 GLN GLN D . n 
D 1 73  SER 73  166 166 SER SER D . n 
D 1 74  GLN 74  167 167 GLN GLN D . n 
D 1 75  HIS 75  168 168 HIS HIS D . n 
D 1 76  MET 76  169 169 MET MET D . n 
D 1 77  THR 77  170 170 THR THR D . n 
D 1 78  GLU 78  171 171 GLU GLU D . n 
D 1 79  VAL 79  172 172 VAL VAL D . n 
D 1 80  VAL 80  173 173 VAL VAL D . n 
D 1 81  ARG 81  174 174 ARG ARG D . n 
D 1 82  ARG 82  175 175 ARG ARG D . n 
D 1 83  CYS 83  176 176 CYS CYS D . n 
D 1 84  PRO 84  177 177 PRO PRO D . n 
D 1 85  HIS 85  178 178 HIS HIS D . n 
D 1 86  HIS 86  179 179 HIS HIS D . n 
D 1 87  GLU 87  180 180 GLU GLU D . n 
D 1 88  ARG 88  181 181 ARG ARG D . n 
D 1 89  CYS 89  182 182 CYS CYS D . n 
D 1 90  SER 90  183 183 SER SER D . n 
D 1 91  ASP 91  184 184 ASP ASP D . n 
D 1 92  SER 92  185 185 SER SER D . n 
D 1 93  ASP 93  186 186 ASP ASP D . n 
D 1 94  GLY 94  187 187 GLY GLY D . n 
D 1 95  LEU 95  188 188 LEU LEU D . n 
D 1 96  ALA 96  189 189 ALA ALA D . n 
D 1 97  PRO 97  190 190 PRO PRO D . n 
D 1 98  PRO 98  191 191 PRO PRO D . n 
D 1 99  GLN 99  192 192 GLN GLN D . n 
D 1 100 HIS 100 193 193 HIS HIS D . n 
D 1 101 LEU 101 194 194 LEU LEU D . n 
D 1 102 ILE 102 195 195 ILE ILE D . n 
D 1 103 ARG 103 196 196 ARG ARG D . n 
D 1 104 VAL 104 197 197 VAL VAL D . n 
D 1 105 GLU 105 198 198 GLU GLU D . n 
D 1 106 GLY 106 199 199 GLY GLY D . n 
D 1 107 ASN 107 200 200 ASN ASN D . n 
D 1 108 LEU 108 201 201 LEU LEU D . n 
D 1 109 ARG 109 202 202 ARG ARG D . n 
D 1 110 VAL 110 203 203 VAL VAL D . n 
D 1 111 GLU 111 204 204 GLU GLU D . n 
D 1 112 TYR 112 205 205 TYR TYR D . n 
D 1 113 LEU 113 206 206 LEU LEU D . n 
D 1 114 ASP 114 207 207 ASP ASP D . n 
D 1 115 ASP 115 208 208 ASP ASP D . n 
D 1 116 ARG 116 209 209 ARG ARG D . n 
D 1 117 ASN 117 210 210 ASN ASN D . n 
D 1 118 THR 118 211 211 THR THR D . n 
D 1 119 PHE 119 212 212 PHE PHE D . n 
D 1 120 ARG 120 213 213 ARG ARG D . n 
D 1 121 HIS 121 214 214 HIS HIS D . n 
D 1 122 SER 122 215 215 SER SER D . n 
D 1 123 VAL 123 216 216 VAL VAL D . n 
D 1 124 VAL 124 217 217 VAL VAL D . n 
D 1 125 VAL 125 218 218 VAL VAL D . n 
D 1 126 PRO 126 219 219 PRO PRO D . n 
D 1 127 TYR 127 220 220 TYR TYR D . n 
D 1 128 GLU 128 221 221 GLU GLU D . n 
D 1 129 PRO 129 222 222 PRO PRO D . n 
D 1 130 PRO 130 223 223 PRO PRO D . n 
D 1 131 GLU 131 224 224 GLU GLU D . n 
D 1 132 VAL 132 225 225 VAL VAL D . n 
D 1 133 GLY 133 226 226 GLY GLY D . n 
D 1 134 SER 134 227 227 SER SER D . n 
D 1 135 ASP 135 228 228 ASP ASP D . n 
D 1 136 CYS 136 229 229 CYS CYS D . n 
D 1 137 THR 137 230 230 THR THR D . n 
D 1 138 THR 138 231 231 THR THR D . n 
D 1 139 ILE 139 232 232 ILE ILE D . n 
D 1 140 HIS 140 233 233 HIS HIS D . n 
D 1 141 TYR 141 234 234 TYR TYR D . n 
D 1 142 ASN 142 235 235 ASN ASN D . n 
D 1 143 TYR 143 236 236 TYR TYR D . n 
D 1 144 MET 144 237 237 MET MET D . n 
D 1 145 CYS 145 238 238 CYS CYS D . n 
D 1 146 ASN 146 239 239 ASN ASN D . n 
D 1 147 SER 147 240 240 SER SER D . n 
D 1 148 SER 148 241 241 SER SER D . n 
D 1 149 CYS 149 242 242 CYS CYS D . n 
D 1 150 MET 150 243 243 MET MET D . n 
D 1 151 GLY 151 244 244 GLY GLY D . n 
D 1 152 GLY 152 245 245 GLY GLY D . n 
D 1 153 MET 153 246 246 MET MET D . n 
D 1 154 ASN 154 247 247 ASN ASN D . n 
D 1 155 ARG 155 248 248 ARG ARG D . n 
D 1 156 ARG 156 249 249 ARG ARG D . n 
D 1 157 PRO 157 250 250 PRO PRO D . n 
D 1 158 ILE 158 251 251 ILE ILE D . n 
D 1 159 LEU 159 252 252 LEU LEU D . n 
D 1 160 THR 160 253 253 THR THR D . n 
D 1 161 ILE 161 254 254 ILE ILE D . n 
D 1 162 ILE 162 255 255 ILE ILE D . n 
D 1 163 THR 163 256 256 THR THR D . n 
D 1 164 LEU 164 257 257 LEU LEU D . n 
D 1 165 GLU 165 258 258 GLU GLU D . n 
D 1 166 ASP 166 259 259 ASP ASP D . n 
D 1 167 SER 167 260 260 SER SER D . n 
D 1 168 SER 168 261 261 SER SER D . n 
D 1 169 GLY 169 262 262 GLY GLY D . n 
D 1 170 ASN 170 263 263 ASN ASN D . n 
D 1 171 LEU 171 264 264 LEU LEU D . n 
D 1 172 LEU 172 265 265 LEU LEU D . n 
D 1 173 GLY 173 266 266 GLY GLY D . n 
D 1 174 ARG 174 267 267 ARG ARG D . n 
D 1 175 ASN 175 268 268 ASN ASN D . n 
D 1 176 SER 176 269 269 SER SER D . n 
D 1 177 PHE 177 270 270 PHE PHE D . n 
D 1 178 GLU 178 271 271 GLU GLU D . n 
D 1 179 VAL 179 272 272 VAL VAL D . n 
D 1 180 ARG 180 273 273 ARG ARG D . n 
D 1 181 VAL 181 274 274 VAL VAL D . n 
D 1 182 CYS 182 275 275 CYS CYS D . n 
D 1 183 ALA 183 276 276 ALA ALA D . n 
D 1 184 CYS 184 277 277 CYS CYS D . n 
D 1 185 PRO 185 278 278 PRO PRO D . n 
D 1 186 GLY 186 279 279 GLY GLY D . n 
D 1 187 ARG 187 280 280 ARG ARG D . n 
D 1 188 ASP 188 281 281 ASP ASP D . n 
D 1 189 ARG 189 282 282 ARG ARG D . n 
D 1 190 ARG 190 283 283 ARG ARG D . n 
D 1 191 THR 191 284 284 THR THR D . n 
D 1 192 GLU 192 285 285 GLU GLU D . n 
D 1 193 GLU 193 286 286 GLU GLU D . n 
D 1 194 GLU 194 287 287 GLU GLU D . n 
D 1 195 ASN 195 288 288 ASN ASN D . n 
D 1 196 LEU 196 289 289 LEU LEU D . n 
D 1 197 ARG 197 290 ?   ?   ?   D . n 
D 1 198 LYS 198 291 ?   ?   ?   D . n 
D 1 199 LYS 199 292 ?   ?   ?   D . n 
D 1 200 GLY 200 293 ?   ?   ?   D . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
E 2 ZN    1  301 301 ZN    ZN  A . 
F 2 ZN    1  301 301 ZN    ZN  B . 
G 2 ZN    1  301 301 ZN    ZN  C . 
H 2 ZN    1  301 301 ZN    ZN  D . 
I 3 A1LU0 1  302 401 A1LU0 LIG D . 
J 4 HOH   1  401 48  HOH   HOH A . 
J 4 HOH   2  402 59  HOH   HOH A . 
J 4 HOH   3  403 45  HOH   HOH A . 
J 4 HOH   4  404 5   HOH   HOH A . 
J 4 HOH   5  405 74  HOH   HOH A . 
J 4 HOH   6  406 20  HOH   HOH A . 
J 4 HOH   7  407 70  HOH   HOH A . 
J 4 HOH   8  408 51  HOH   HOH A . 
J 4 HOH   9  409 19  HOH   HOH A . 
J 4 HOH   10 410 58  HOH   HOH A . 
J 4 HOH   11 411 4   HOH   HOH A . 
J 4 HOH   12 412 46  HOH   HOH A . 
J 4 HOH   13 413 72  HOH   HOH A . 
J 4 HOH   14 414 69  HOH   HOH A . 
J 4 HOH   15 415 86  HOH   HOH A . 
J 4 HOH   16 416 84  HOH   HOH A . 
K 4 HOH   1  401 9   HOH   HOH B . 
K 4 HOH   2  402 52  HOH   HOH B . 
K 4 HOH   3  403 66  HOH   HOH B . 
K 4 HOH   4  404 44  HOH   HOH B . 
K 4 HOH   5  405 43  HOH   HOH B . 
K 4 HOH   6  406 47  HOH   HOH B . 
K 4 HOH   7  407 34  HOH   HOH B . 
K 4 HOH   8  408 37  HOH   HOH B . 
K 4 HOH   9  409 79  HOH   HOH B . 
K 4 HOH   10 410 24  HOH   HOH B . 
K 4 HOH   11 411 31  HOH   HOH B . 
K 4 HOH   12 412 3   HOH   HOH B . 
K 4 HOH   13 413 71  HOH   HOH B . 
K 4 HOH   14 414 61  HOH   HOH B . 
K 4 HOH   15 415 8   HOH   HOH B . 
K 4 HOH   16 416 65  HOH   HOH B . 
K 4 HOH   17 417 29  HOH   HOH B . 
K 4 HOH   18 418 23  HOH   HOH B . 
K 4 HOH   19 419 2   HOH   HOH B . 
K 4 HOH   20 420 53  HOH   HOH B . 
K 4 HOH   21 421 68  HOH   HOH B . 
K 4 HOH   22 422 33  HOH   HOH B . 
K 4 HOH   23 423 54  HOH   HOH B . 
K 4 HOH   24 424 39  HOH   HOH B . 
K 4 HOH   25 425 73  HOH   HOH B . 
L 4 HOH   1  401 63  HOH   HOH C . 
L 4 HOH   2  402 6   HOH   HOH C . 
L 4 HOH   3  403 40  HOH   HOH C . 
L 4 HOH   4  404 22  HOH   HOH C . 
L 4 HOH   5  405 36  HOH   HOH C . 
L 4 HOH   6  406 78  HOH   HOH C . 
L 4 HOH   7  407 12  HOH   HOH C . 
L 4 HOH   8  408 14  HOH   HOH C . 
L 4 HOH   9  409 49  HOH   HOH C . 
L 4 HOH   10 410 67  HOH   HOH C . 
L 4 HOH   11 411 56  HOH   HOH C . 
L 4 HOH   12 412 26  HOH   HOH C . 
L 4 HOH   13 413 7   HOH   HOH C . 
L 4 HOH   14 414 13  HOH   HOH C . 
L 4 HOH   15 415 60  HOH   HOH C . 
L 4 HOH   16 416 15  HOH   HOH C . 
L 4 HOH   17 417 85  HOH   HOH C . 
L 4 HOH   18 418 75  HOH   HOH C . 
M 4 HOH   1  401 18  HOH   HOH D . 
M 4 HOH   2  402 55  HOH   HOH D . 
M 4 HOH   3  403 17  HOH   HOH D . 
M 4 HOH   4  404 30  HOH   HOH D . 
M 4 HOH   5  405 50  HOH   HOH D . 
M 4 HOH   6  406 82  HOH   HOH D . 
M 4 HOH   7  407 21  HOH   HOH D . 
M 4 HOH   8  408 38  HOH   HOH D . 
M 4 HOH   9  409 32  HOH   HOH D . 
M 4 HOH   10 410 1   HOH   HOH D . 
M 4 HOH   11 411 25  HOH   HOH D . 
M 4 HOH   12 412 41  HOH   HOH D . 
M 4 HOH   13 413 42  HOH   HOH D . 
M 4 HOH   14 414 57  HOH   HOH D . 
M 4 HOH   15 415 35  HOH   HOH D . 
M 4 HOH   16 416 10  HOH   HOH D . 
M 4 HOH   17 417 83  HOH   HOH D . 
M 4 HOH   18 418 62  HOH   HOH D . 
M 4 HOH   19 419 80  HOH   HOH D . 
M 4 HOH   20 420 81  HOH   HOH D . 
M 4 HOH   21 421 76  HOH   HOH D . 
M 4 HOH   22 422 16  HOH   HOH D . 
M 4 HOH   23 423 64  HOH   HOH D . 
M 4 HOH   24 424 77  HOH   HOH D . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1 1 Y 1 C ARG 110 ? NH1 ? C ARG 17 NH1 
2 1 Y 1 C ARG 110 ? NH2 ? C ARG 17 NH2 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement        ? ? ? ? ? ? ? ? ? ? ? REFMAC      ? ? ? 5.8.0267 1 
? 'data scaling'    ? ? ? ? ? ? ? ? ? ? ? XSCALE      ? ? ? .        2 
? 'data reduction'  ? ? ? ? ? ? ? ? ? ? ? XDS         ? ? ? .        3 
? phasing           ? ? ? ? ? ? ? ? ? ? ? PHASER      ? ? ? .        4 
? 'data extraction' ? ? ? ? ? ? ? ? ? ? ? PDB_EXTRACT ? ? ? .        5 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8XCE 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     68.930 
_cell.length_a_esd                 ? 
_cell.length_b                     71.800 
_cell.length_b_esd                 ? 
_cell.length_c                     84.620 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        8 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         8XCE 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                4 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 1 21 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_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                   8XCE 
_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             2.37 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          48.20 
_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, HANGING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              8.5 
_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    '0.1M Tris pH 8.5, 10% w/v PEG3350 and 0.2M Magnesium chloride' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            277 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS3 S 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2022-08-29 
_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                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.97918 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'SSRF BEAMLINE BL02U1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.97918 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL02U1 
_diffrn_source.pdbx_synchrotron_site       SSRF 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       8XCE 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.00 
_reflns.d_resolution_low                               53.44 
_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                                     54521 
_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                           97.4 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                4.6 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          6.2 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   ? 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.154 
_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                        ? 
# 
_reflns_shell.d_res_high                                    2.00 
_reflns_shell.d_res_low                                     2.05 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           1.9 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             4076 
_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                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  ? 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          98.8 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  0.929 
_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               ? 
# 
_refine.aniso_B[1][1]                            -32.31 
_refine.aniso_B[1][2]                            -0.00 
_refine.aniso_B[1][3]                            1.85 
_refine.aniso_B[2][2]                            58.43 
_refine.aniso_B[2][3]                            0.00 
_refine.aniso_B[3][3]                            -26.12 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               36.179 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.949 
_refine.correlation_coeff_Fo_to_Fc_free          0.941 
_refine.details                                  'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS' 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 8XCE 
_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                            2.00 
_refine.ls_d_res_low                             53.44 
_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                     51846 
_refine.ls_number_reflns_R_free                  2655 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    97.34 
_refine.ls_percent_reflns_R_free                 4.9 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.20172 
_refine.ls_R_factor_R_free                       0.22288 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.20056 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    MASK 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       0.043 
_refine.pdbx_overall_ESU_R_Free                  0.034 
_refine.pdbx_solvent_vdw_probe_radii             1.20 
_refine.pdbx_solvent_ion_probe_radii             0.80 
_refine.pdbx_solvent_shrinkage_radii             0.80 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             6.830 
_refine.overall_SU_ML                            0.095 
_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                         1 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       2.00 
_refine_hist.d_res_low                        53.44 
_refine_hist.number_atoms_solvent             83 
_refine_hist.number_atoms_total               6152 
_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        6046 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         23 
_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' ? 0.006  0.013  6551  ? r_bond_refined_d             ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.014  5968  ? r_bond_other_d               ? ? 
'X-RAY DIFFRACTION' ? 1.436  1.662  8953  ? r_angle_refined_deg          ? ? 
'X-RAY DIFFRACTION' ? 1.189  1.576  13801 ? r_angle_other_deg            ? ? 
'X-RAY DIFFRACTION' ? 7.368  5.000  848   ? r_dihedral_angle_1_deg       ? ? 
'X-RAY DIFFRACTION' ? 29.938 20.082 367   ? r_dihedral_angle_2_deg       ? ? 
'X-RAY DIFFRACTION' ? 15.275 15.000 1086  ? r_dihedral_angle_3_deg       ? ? 
'X-RAY DIFFRACTION' ? 15.705 15.000 71    ? r_dihedral_angle_4_deg       ? ? 
'X-RAY DIFFRACTION' ? 0.059  0.200  849   ? r_chiral_restr               ? ? 
'X-RAY DIFFRACTION' ? 0.005  0.020  8627  ? r_gen_planes_refined         ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.020  1581  ? r_gen_planes_other           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbd_refined                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbd_other                  ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbtor_refined              ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbtor_other                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_xyhbond_nbd_refined        ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_xyhbond_nbd_other          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_metal_ion_refined          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_metal_ion_other            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_vdw_refined       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_vdw_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_hbond_refined     ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_hbond_other       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_metal_ion_refined ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_metal_ion_other   ? ? 
'X-RAY DIFFRACTION' ? 0.709  2.046  3270  ? r_mcbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 0.709  2.045  3269  ? r_mcbond_other               ? ? 
'X-RAY DIFFRACTION' ? 1.183  3.062  4145  ? r_mcangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 1.182  3.062  4146  ? r_mcangle_other              ? ? 
'X-RAY DIFFRACTION' ? 0.611  2.082  3281  ? r_scbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 0.611  2.081  3280  ? r_scbond_other               ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_scangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 0.972  3.101  4803  ? r_scangle_other              ? ? 
'X-RAY DIFFRACTION' ? 2.461  23.201 6610  ? r_long_range_B_refined       ? ? 
'X-RAY DIFFRACTION' ? 2.452  23.181 6606  ? r_long_range_B_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_rigid_bond_restr           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_sphericity_free            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_sphericity_bonded          ? ? 
# 
loop_
_refine_ls_restr_ncs.pdbx_refine_id 
_refine_ls_restr_ncs.dom_id 
_refine_ls_restr_ncs.ncs_model_details 
_refine_ls_restr_ncs.rms_dev_B_iso 
_refine_ls_restr_ncs.rms_dev_position 
_refine_ls_restr_ncs.weight_B_iso 
_refine_ls_restr_ncs.weight_position 
_refine_ls_restr_ncs.pdbx_ordinal 
_refine_ls_restr_ncs.pdbx_type 
_refine_ls_restr_ncs.pdbx_asym_id 
_refine_ls_restr_ncs.pdbx_auth_asym_id 
_refine_ls_restr_ncs.pdbx_number 
_refine_ls_restr_ncs.pdbx_rms 
_refine_ls_restr_ncs.pdbx_weight 
_refine_ls_restr_ncs.pdbx_ens_id 
'X-RAY DIFFRACTION' 1 ? ? 0.09 ? 0.05 1  'interatomic distance' ? A 6239 ? ? 1 
'X-RAY DIFFRACTION' 2 ? ? 0.09 ? 0.05 2  'interatomic distance' ? B 6239 ? ? 1 
'X-RAY DIFFRACTION' 1 ? ? 0.10 ? 0.05 3  'interatomic distance' ? A 6123 ? ? 2 
'X-RAY DIFFRACTION' 2 ? ? 0.10 ? 0.05 4  'interatomic distance' ? C 6123 ? ? 2 
'X-RAY DIFFRACTION' 1 ? ? 0.10 ? 0.05 5  'interatomic distance' ? A 6196 ? ? 3 
'X-RAY DIFFRACTION' 2 ? ? 0.10 ? 0.05 6  'interatomic distance' ? D 6196 ? ? 3 
'X-RAY DIFFRACTION' 1 ? ? 0.09 ? 0.05 7  'interatomic distance' ? B 6035 ? ? 4 
'X-RAY DIFFRACTION' 2 ? ? 0.09 ? 0.05 8  'interatomic distance' ? C 6035 ? ? 4 
'X-RAY DIFFRACTION' 1 ? ? 0.10 ? 0.05 9  'interatomic distance' ? B 5984 ? ? 5 
'X-RAY DIFFRACTION' 2 ? ? 0.10 ? 0.05 10 'interatomic distance' ? D 5984 ? ? 5 
'X-RAY DIFFRACTION' 1 ? ? 0.09 ? 0.05 11 'interatomic distance' ? C 5917 ? ? 6 
'X-RAY DIFFRACTION' 2 ? ? 0.09 ? 0.05 12 'interatomic distance' ? D 5917 ? ? 6 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       2.000 
_refine_ls_shell.d_res_low                        2.052 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             201 
_refine_ls_shell.number_reflns_R_work             3868 
_refine_ls_shell.percent_reflns_obs               98.59 
_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                  0.286 
_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   20 
_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                  0.307 
# 
loop_
_struct_ncs_dom.id 
_struct_ncs_dom.details 
_struct_ncs_dom.pdbx_ens_id 
1 ? 1 
2 ? 2 
3 ? 3 
4 ? 4 
5 ? 5 
6 ? 6 
# 
loop_
_struct_ncs_ens.id 
_struct_ncs_ens.details 
1 ? 
2 ? 
3 ? 
4 ? 
5 ? 
6 ? 
# 
_struct.entry_id                     8XCE 
_struct.title                        'cocrystal structure of p53 in complex of B23' 
_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        8XCE 
_struct_keywords.text            'ANTITUMOR PROTEIN-INHIBITOR COMPLEX' 
_struct_keywords.pdbx_keywords   'ANTITUMOR PROTEIN/INHIBITOR' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 1 ? 
D N N 1 ? 
E N N 2 ? 
F N N 2 ? 
G N N 2 ? 
H N N 2 ? 
I N N 3 ? 
J N N 4 ? 
K N N 4 ? 
L N N 4 ? 
M N N 4 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    P53_HUMAN 
_struct_ref.pdbx_db_accession          P04637 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;SSSVPSQKTYQGSYGFRLGFLHSGTAKSVTCTYSPALNKMFCQLAKTCPVQLWVDSTPPPGTRVRAMAIYKQSQHMTEVV
RRCPHHERCSDSDGLAPPQHLIRVEGNLRVEYLDDRNTFRHSVVVPYEPPEVGSDCTTIHYNYMCNSSCMGGMNRRPILT
IITLEDSSGNLLGRNSFEVRVCACPGRDRRTEEENLRKKG
;
_struct_ref.pdbx_align_begin           94 
# 
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 8XCE A 1 ? 200 ? P04637 94 ? 293 ? 94 293 
2 1 8XCE B 1 ? 200 ? P04637 94 ? 293 ? 94 293 
3 1 8XCE C 1 ? 200 ? P04637 94 ? 293 ? 94 293 
4 1 8XCE D 1 ? 200 ? P04637 94 ? 293 ? 94 293 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   tetrameric 
_pdbx_struct_assembly.oligomeric_count     4 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I,J,K,L,M 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   cross-linking 
_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]         1.0 
_pdbx_struct_oper_list.matrix[1][2]         0.0 
_pdbx_struct_oper_list.matrix[1][3]         0.0 
_pdbx_struct_oper_list.vector[1]            0.0 
_pdbx_struct_oper_list.matrix[2][1]         0.0 
_pdbx_struct_oper_list.matrix[2][2]         1.0 
_pdbx_struct_oper_list.matrix[2][3]         0.0 
_pdbx_struct_oper_list.vector[2]            0.0 
_pdbx_struct_oper_list.matrix[3][1]         0.0 
_pdbx_struct_oper_list.matrix[3][2]         0.0 
_pdbx_struct_oper_list.matrix[3][3]         1.0 
_pdbx_struct_oper_list.vector[3]            0.0 
# 
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 GLN A 11  ? GLY A 15  ? GLN A 104 GLY A 108 5 ? 5  
HELX_P HELX_P2  AA2 GLN A 72  ? MET A 76  ? GLN A 165 MET A 169 5 ? 5  
HELX_P HELX_P3  AA3 CYS A 83  ? CYS A 89  ? CYS A 176 CYS A 182 1 ? 7  
HELX_P HELX_P4  AA4 CYS A 184 ? GLU A 194 ? CYS A 277 GLU A 287 1 ? 11 
HELX_P HELX_P5  AA5 GLN B 11  ? GLY B 15  ? GLN B 104 GLY B 108 5 ? 5  
HELX_P HELX_P6  AA6 GLN B 72  ? MET B 76  ? GLN B 165 MET B 169 5 ? 5  
HELX_P HELX_P7  AA7 CYS B 83  ? CYS B 89  ? CYS B 176 CYS B 182 1 ? 7  
HELX_P HELX_P8  AA8 CYS B 184 ? GLU B 194 ? CYS B 277 GLU B 287 1 ? 11 
HELX_P HELX_P9  AA9 GLN C 11  ? GLY C 15  ? GLN C 104 GLY C 108 5 ? 5  
HELX_P HELX_P10 AB1 GLN C 72  ? MET C 76  ? GLN C 165 MET C 169 5 ? 5  
HELX_P HELX_P11 AB2 CYS C 83  ? ARG C 88  ? CYS C 176 ARG C 181 1 ? 6  
HELX_P HELX_P12 AB3 CYS C 184 ? ASN C 195 ? CYS C 277 ASN C 288 1 ? 12 
HELX_P HELX_P13 AB4 GLN D 11  ? GLY D 15  ? GLN D 104 GLY D 108 5 ? 5  
HELX_P HELX_P14 AB5 GLN D 72  ? MET D 76  ? GLN D 165 MET D 169 5 ? 5  
HELX_P HELX_P15 AB6 CYS D 83  ? CYS D 89  ? CYS D 176 CYS D 182 1 ? 7  
HELX_P HELX_P16 AB7 CYS D 184 ? ASN D 195 ? CYS D 277 ASN D 288 1 ? 12 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1  metalc ? ? A CYS 83  SG  ? ? ? 1_555 E ZN . ZN ? ? A CYS 176 A ZN 301 1_555 ? ? ? ? ? ? ? 2.325 ? ? 
metalc2  metalc ? ? A HIS 86  ND1 ? ? ? 1_555 E ZN . ZN ? ? A HIS 179 A ZN 301 1_555 ? ? ? ? ? ? ? 2.061 ? ? 
metalc3  metalc ? ? A CYS 145 SG  A ? ? 1_555 E ZN . ZN ? ? A CYS 238 A ZN 301 1_555 ? ? ? ? ? ? ? 2.354 ? ? 
metalc4  metalc ? ? A CYS 145 SG  B ? ? 1_555 E ZN . ZN ? ? A CYS 238 A ZN 301 1_555 ? ? ? ? ? ? ? 2.316 ? ? 
metalc5  metalc ? ? A CYS 149 SG  ? ? ? 1_555 E ZN . ZN ? ? A CYS 242 A ZN 301 1_555 ? ? ? ? ? ? ? 2.329 ? ? 
metalc6  metalc ? ? B CYS 83  SG  ? ? ? 1_555 F ZN . ZN ? ? B CYS 176 B ZN 301 1_555 ? ? ? ? ? ? ? 2.341 ? ? 
metalc7  metalc ? ? B HIS 86  ND1 ? ? ? 1_555 F ZN . ZN ? ? B HIS 179 B ZN 301 1_555 ? ? ? ? ? ? ? 2.061 ? ? 
metalc8  metalc ? ? B CYS 145 SG  ? ? ? 1_555 F ZN . ZN ? ? B CYS 238 B ZN 301 1_555 ? ? ? ? ? ? ? 2.342 ? ? 
metalc9  metalc ? ? B CYS 149 SG  ? ? ? 1_555 F ZN . ZN ? ? B CYS 242 B ZN 301 1_555 ? ? ? ? ? ? ? 2.340 ? ? 
metalc10 metalc ? ? C CYS 83  SG  ? ? ? 1_555 G ZN . ZN ? ? C CYS 176 C ZN 301 1_555 ? ? ? ? ? ? ? 2.327 ? ? 
metalc11 metalc ? ? C HIS 86  ND1 ? ? ? 1_555 G ZN . ZN ? ? C HIS 179 C ZN 301 1_555 ? ? ? ? ? ? ? 2.039 ? ? 
metalc12 metalc ? ? C CYS 145 SG  ? ? ? 1_555 G ZN . ZN ? ? C CYS 238 C ZN 301 1_555 ? ? ? ? ? ? ? 2.354 ? ? 
metalc13 metalc ? ? C CYS 149 SG  ? ? ? 1_555 G ZN . ZN ? ? C CYS 242 C ZN 301 1_555 ? ? ? ? ? ? ? 2.314 ? ? 
metalc14 metalc ? ? D CYS 83  SG  ? ? ? 1_555 H ZN . ZN ? ? D CYS 176 D ZN 301 1_555 ? ? ? ? ? ? ? 2.345 ? ? 
metalc15 metalc ? ? D HIS 86  ND1 ? ? ? 1_555 H ZN . ZN ? ? D HIS 179 D ZN 301 1_555 ? ? ? ? ? ? ? 1.999 ? ? 
metalc16 metalc ? ? D CYS 145 SG  A ? ? 1_555 H ZN . ZN ? ? D CYS 238 D ZN 301 1_555 ? ? ? ? ? ? ? 2.339 ? ? 
metalc17 metalc ? ? D CYS 145 SG  B ? ? 1_555 H ZN . ZN ? ? D CYS 238 D ZN 301 1_555 ? ? ? ? ? ? ? 2.335 ? ? 
metalc18 metalc ? ? D CYS 149 SG  ? ? ? 1_555 H ZN . ZN ? ? D CYS 242 D ZN 301 1_555 ? ? ? ? ? ? ? 2.330 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  SG  ? A CYS 83  ? A CYS 176 ? 1_555 ZN ? E ZN . ? A ZN 301 ? 1_555 ND1 ? A HIS 86  ? A HIS 179 ? 1_555 107.3 ? 
2  SG  ? A CYS 83  ? A CYS 176 ? 1_555 ZN ? E ZN . ? A ZN 301 ? 1_555 SG  A A CYS 145 ? A CYS 238 ? 1_555 111.7 ? 
3  ND1 ? A HIS 86  ? A HIS 179 ? 1_555 ZN ? E ZN . ? A ZN 301 ? 1_555 SG  A A CYS 145 ? A CYS 238 ? 1_555 96.5  ? 
4  SG  ? A CYS 83  ? A CYS 176 ? 1_555 ZN ? E ZN . ? A ZN 301 ? 1_555 SG  B A CYS 145 ? A CYS 238 ? 1_555 113.6 ? 
5  ND1 ? A HIS 86  ? A HIS 179 ? 1_555 ZN ? E ZN . ? A ZN 301 ? 1_555 SG  B A CYS 145 ? A CYS 238 ? 1_555 121.4 ? 
6  SG  A A CYS 145 ? A CYS 238 ? 1_555 ZN ? E ZN . ? A ZN 301 ? 1_555 SG  B A CYS 145 ? A CYS 238 ? 1_555 29.9  ? 
7  SG  ? A CYS 83  ? A CYS 176 ? 1_555 ZN ? E ZN . ? A ZN 301 ? 1_555 SG  ? A CYS 149 ? A CYS 242 ? 1_555 115.6 ? 
8  ND1 ? A HIS 86  ? A HIS 179 ? 1_555 ZN ? E ZN . ? A ZN 301 ? 1_555 SG  ? A CYS 149 ? A CYS 242 ? 1_555 99.1  ? 
9  SG  A A CYS 145 ? A CYS 238 ? 1_555 ZN ? E ZN . ? A ZN 301 ? 1_555 SG  ? A CYS 149 ? A CYS 242 ? 1_555 122.3 ? 
10 SG  B A CYS 145 ? A CYS 238 ? 1_555 ZN ? E ZN . ? A ZN 301 ? 1_555 SG  ? A CYS 149 ? A CYS 242 ? 1_555 99.0  ? 
11 SG  ? B CYS 83  ? B CYS 176 ? 1_555 ZN ? F ZN . ? B ZN 301 ? 1_555 ND1 ? B HIS 86  ? B HIS 179 ? 1_555 107.1 ? 
12 SG  ? B CYS 83  ? B CYS 176 ? 1_555 ZN ? F ZN . ? B ZN 301 ? 1_555 SG  ? B CYS 145 ? B CYS 238 ? 1_555 111.8 ? 
13 ND1 ? B HIS 86  ? B HIS 179 ? 1_555 ZN ? F ZN . ? B ZN 301 ? 1_555 SG  ? B CYS 145 ? B CYS 238 ? 1_555 101.7 ? 
14 SG  ? B CYS 83  ? B CYS 176 ? 1_555 ZN ? F ZN . ? B ZN 301 ? 1_555 SG  ? B CYS 149 ? B CYS 242 ? 1_555 117.4 ? 
15 ND1 ? B HIS 86  ? B HIS 179 ? 1_555 ZN ? F ZN . ? B ZN 301 ? 1_555 SG  ? B CYS 149 ? B CYS 242 ? 1_555 97.1  ? 
16 SG  ? B CYS 145 ? B CYS 238 ? 1_555 ZN ? F ZN . ? B ZN 301 ? 1_555 SG  ? B CYS 149 ? B CYS 242 ? 1_555 118.4 ? 
17 SG  ? C CYS 83  ? C CYS 176 ? 1_555 ZN ? G ZN . ? C ZN 301 ? 1_555 ND1 ? C HIS 86  ? C HIS 179 ? 1_555 107.4 ? 
18 SG  ? C CYS 83  ? C CYS 176 ? 1_555 ZN ? G ZN . ? C ZN 301 ? 1_555 SG  ? C CYS 145 ? C CYS 238 ? 1_555 113.0 ? 
19 ND1 ? C HIS 86  ? C HIS 179 ? 1_555 ZN ? G ZN . ? C ZN 301 ? 1_555 SG  ? C CYS 145 ? C CYS 238 ? 1_555 121.9 ? 
20 SG  ? C CYS 83  ? C CYS 176 ? 1_555 ZN ? G ZN . ? C ZN 301 ? 1_555 SG  ? C CYS 149 ? C CYS 242 ? 1_555 117.5 ? 
21 ND1 ? C HIS 86  ? C HIS 179 ? 1_555 ZN ? G ZN . ? C ZN 301 ? 1_555 SG  ? C CYS 149 ? C CYS 242 ? 1_555 100.0 ? 
22 SG  ? C CYS 145 ? C CYS 238 ? 1_555 ZN ? G ZN . ? C ZN 301 ? 1_555 SG  ? C CYS 149 ? C CYS 242 ? 1_555 96.6  ? 
23 SG  ? D CYS 83  ? D CYS 176 ? 1_555 ZN ? H ZN . ? D ZN 301 ? 1_555 ND1 ? D HIS 86  ? D HIS 179 ? 1_555 107.4 ? 
24 SG  ? D CYS 83  ? D CYS 176 ? 1_555 ZN ? H ZN . ? D ZN 301 ? 1_555 SG  A D CYS 145 ? D CYS 238 ? 1_555 111.7 ? 
25 ND1 ? D HIS 86  ? D HIS 179 ? 1_555 ZN ? H ZN . ? D ZN 301 ? 1_555 SG  A D CYS 145 ? D CYS 238 ? 1_555 123.1 ? 
26 SG  ? D CYS 83  ? D CYS 176 ? 1_555 ZN ? H ZN . ? D ZN 301 ? 1_555 SG  B D CYS 145 ? D CYS 238 ? 1_555 108.4 ? 
27 ND1 ? D HIS 86  ? D HIS 179 ? 1_555 ZN ? H ZN . ? D ZN 301 ? 1_555 SG  B D CYS 145 ? D CYS 238 ? 1_555 96.3  ? 
28 SG  A D CYS 145 ? D CYS 238 ? 1_555 ZN ? H ZN . ? D ZN 301 ? 1_555 SG  B D CYS 145 ? D CYS 238 ? 1_555 32.7  ? 
29 SG  ? D CYS 83  ? D CYS 176 ? 1_555 ZN ? H ZN . ? D ZN 301 ? 1_555 SG  ? D CYS 149 ? D CYS 242 ? 1_555 115.0 ? 
30 ND1 ? D HIS 86  ? D HIS 179 ? 1_555 ZN ? H ZN . ? D ZN 301 ? 1_555 SG  ? D CYS 149 ? D CYS 242 ? 1_555 101.4 ? 
31 SG  A D CYS 145 ? D CYS 238 ? 1_555 ZN ? H ZN . ? D ZN 301 ? 1_555 SG  ? D CYS 149 ? D CYS 242 ? 1_555 97.7  ? 
32 SG  B D CYS 145 ? D CYS 238 ? 1_555 ZN ? H ZN . ? D ZN 301 ? 1_555 SG  ? D CYS 149 ? D CYS 242 ? 1_555 124.7 ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 4 ? 
AA2 ? 7 ? 
AA3 ? 4 ? 
AA4 ? 7 ? 
AA5 ? 4 ? 
AA6 ? 7 ? 
AA7 ? 4 ? 
AA8 ? 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 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? parallel      
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA2 5 6 ? anti-parallel 
AA2 6 7 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA3 3 4 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? parallel      
AA4 3 4 ? anti-parallel 
AA4 4 5 ? anti-parallel 
AA4 5 6 ? anti-parallel 
AA4 6 7 ? anti-parallel 
AA5 1 2 ? anti-parallel 
AA5 2 3 ? anti-parallel 
AA5 3 4 ? anti-parallel 
AA6 1 2 ? anti-parallel 
AA6 2 3 ? parallel      
AA6 3 4 ? anti-parallel 
AA6 4 5 ? anti-parallel 
AA6 5 6 ? anti-parallel 
AA6 6 7 ? anti-parallel 
AA7 1 2 ? anti-parallel 
AA7 2 3 ? anti-parallel 
AA7 3 4 ? anti-parallel 
AA8 1 2 ? anti-parallel 
AA8 2 3 ? parallel      
AA8 3 4 ? anti-parallel 
AA8 4 5 ? anti-parallel 
AA8 5 6 ? anti-parallel 
AA8 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 ARG A 17  ? GLY A 19  ? ARG A 110 GLY A 112 
AA1 2 CYS A 48  ? TRP A 53  ? CYS A 141 TRP A 146 
AA1 3 THR A 137 ? TYR A 143 ? THR A 230 TYR A 236 
AA1 4 ILE A 102 ? VAL A 104 ? ILE A 195 VAL A 197 
AA2 1 CYS A 31  ? SER A 34  ? CYS A 124 SER A 127 
AA2 2 LYS A 39  ? CYS A 42  ? LYS A 132 CYS A 135 
AA2 3 LEU A 171 ? VAL A 181 ? LEU A 264 VAL A 274 
AA2 4 ILE A 158 ? GLU A 165 ? ILE A 251 GLU A 258 
AA2 5 ARG A 63  ? TYR A 70  ? ARG A 156 TYR A 163 
AA2 6 HIS A 121 ? PRO A 126 ? HIS A 214 PRO A 219 
AA2 7 GLU A 111 ? ASP A 114 ? GLU A 204 ASP A 207 
AA3 1 ARG B 17  ? GLY B 19  ? ARG B 110 GLY B 112 
AA3 2 CYS B 48  ? TRP B 53  ? CYS B 141 TRP B 146 
AA3 3 THR B 137 ? TYR B 143 ? THR B 230 TYR B 236 
AA3 4 ILE B 102 ? GLU B 105 ? ILE B 195 GLU B 198 
AA4 1 CYS B 31  ? SER B 34  ? CYS B 124 SER B 127 
AA4 2 LYS B 39  ? CYS B 42  ? LYS B 132 CYS B 135 
AA4 3 LEU B 171 ? VAL B 181 ? LEU B 264 VAL B 274 
AA4 4 ILE B 158 ? GLU B 165 ? ILE B 251 GLU B 258 
AA4 5 ARG B 63  ? TYR B 70  ? ARG B 156 TYR B 163 
AA4 6 HIS B 121 ? PRO B 126 ? HIS B 214 PRO B 219 
AA4 7 GLU B 111 ? ASP B 114 ? GLU B 204 ASP B 207 
AA5 1 ARG C 17  ? GLY C 19  ? ARG C 110 GLY C 112 
AA5 2 CYS C 48  ? TRP C 53  ? CYS C 141 TRP C 146 
AA5 3 THR C 137 ? TYR C 143 ? THR C 230 TYR C 236 
AA5 4 ILE C 102 ? VAL C 104 ? ILE C 195 VAL C 197 
AA6 1 CYS C 31  ? SER C 34  ? CYS C 124 SER C 127 
AA6 2 LYS C 39  ? CYS C 42  ? LYS C 132 CYS C 135 
AA6 3 LEU C 171 ? VAL C 181 ? LEU C 264 VAL C 274 
AA6 4 ILE C 158 ? GLU C 165 ? ILE C 251 GLU C 258 
AA6 5 ARG C 63  ? TYR C 70  ? ARG C 156 TYR C 163 
AA6 6 HIS C 121 ? PRO C 126 ? HIS C 214 PRO C 219 
AA6 7 GLU C 111 ? ASP C 114 ? GLU C 204 ASP C 207 
AA7 1 ARG D 17  ? GLY D 19  ? ARG D 110 GLY D 112 
AA7 2 CYS D 48  ? TRP D 53  ? CYS D 141 TRP D 146 
AA7 3 THR D 137 ? TYR D 143 ? THR D 230 TYR D 236 
AA7 4 ILE D 102 ? VAL D 104 ? ILE D 195 VAL D 197 
AA8 1 CYS D 31  ? SER D 34  ? CYS D 124 SER D 127 
AA8 2 LYS D 39  ? CYS D 42  ? LYS D 132 CYS D 135 
AA8 3 LEU D 171 ? VAL D 181 ? LEU D 264 VAL D 274 
AA8 4 ILE D 158 ? GLU D 165 ? ILE D 251 GLU D 258 
AA8 5 ARG D 63  ? TYR D 70  ? ARG D 156 TYR D 163 
AA8 6 HIS D 121 ? PRO D 126 ? HIS D 214 PRO D 219 
AA8 7 GLU D 111 ? ASP D 114 ? GLU D 204 ASP D 207 
# 
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 ARG A 17  ? N ARG A 110 O TRP A 53  ? O TRP A 146 
AA1 2 3 N LEU A 52  ? N LEU A 145 O THR A 137 ? O THR A 230 
AA1 3 4 O ASN A 142 ? O ASN A 235 N ARG A 103 ? N ARG A 196 
AA2 1 2 N THR A 32  ? N THR A 125 O PHE A 41  ? O PHE A 134 
AA2 2 3 N MET A 40  ? N MET A 133 O GLU A 178 ? O GLU A 271 
AA2 3 4 O LEU A 172 ? O LEU A 265 N LEU A 164 ? N LEU A 257 
AA2 4 5 O GLU A 165 ? O GLU A 258 N ARG A 63  ? N ARG A 156 
AA2 5 6 N VAL A 64  ? N VAL A 157 O VAL A 125 ? O VAL A 218 
AA2 6 7 O VAL A 124 ? O VAL A 217 N GLU A 111 ? N GLU A 204 
AA3 1 2 N ARG B 17  ? N ARG B 110 O TRP B 53  ? O TRP B 146 
AA3 2 3 N LEU B 52  ? N LEU B 145 O THR B 137 ? O THR B 230 
AA3 3 4 O ASN B 142 ? O ASN B 235 N ARG B 103 ? N ARG B 196 
AA4 1 2 N THR B 32  ? N THR B 125 O PHE B 41  ? O PHE B 134 
AA4 2 3 N MET B 40  ? N MET B 133 O GLU B 178 ? O GLU B 271 
AA4 3 4 O LEU B 172 ? O LEU B 265 N LEU B 164 ? N LEU B 257 
AA4 4 5 O GLU B 165 ? O GLU B 258 N ARG B 63  ? N ARG B 156 
AA4 5 6 N VAL B 64  ? N VAL B 157 O VAL B 125 ? O VAL B 218 
AA4 6 7 O VAL B 124 ? O VAL B 217 N GLU B 111 ? N GLU B 204 
AA5 1 2 N ARG C 17  ? N ARG C 110 O TRP C 53  ? O TRP C 146 
AA5 2 3 N LEU C 52  ? N LEU C 145 O THR C 137 ? O THR C 230 
AA5 3 4 O ASN C 142 ? O ASN C 235 N ARG C 103 ? N ARG C 196 
AA6 1 2 N THR C 32  ? N THR C 125 O PHE C 41  ? O PHE C 134 
AA6 2 3 N MET C 40  ? N MET C 133 O GLU C 178 ? O GLU C 271 
AA6 3 4 O LEU C 172 ? O LEU C 265 N LEU C 164 ? N LEU C 257 
AA6 4 5 O GLU C 165 ? O GLU C 258 N ARG C 63  ? N ARG C 156 
AA6 5 6 N VAL C 64  ? N VAL C 157 O VAL C 125 ? O VAL C 218 
AA6 6 7 O VAL C 124 ? O VAL C 217 N GLU C 111 ? N GLU C 204 
AA7 1 2 N ARG D 17  ? N ARG D 110 O TRP D 53  ? O TRP D 146 
AA7 2 3 N LEU D 52  ? N LEU D 145 O THR D 137 ? O THR D 230 
AA7 3 4 O ASN D 142 ? O ASN D 235 N ARG D 103 ? N ARG D 196 
AA8 1 2 N THR D 32  ? N THR D 125 O PHE D 41  ? O PHE D 134 
AA8 2 3 N MET D 40  ? N MET D 133 O GLU D 178 ? O GLU D 271 
AA8 3 4 O LEU D 172 ? O LEU D 265 N LEU D 164 ? N LEU D 257 
AA8 4 5 O GLU D 165 ? O GLU D 258 N ARG D 63  ? N ARG D 156 
AA8 5 6 N VAL D 64  ? N VAL D 157 O VAL D 125 ? O VAL D 218 
AA8 6 7 O VAL D 124 ? O VAL D 217 N GLU D 111 ? N GLU D 204 
# 
_pdbx_entry_details.entry_id                   8XCE 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 SG  D CYS 182 ? ? C12 D A1LU0 302 ? ? 1.83 
2 1 NH1 D ARG 273 ? ? OD2 D ASP   281 ? ? 2.02 
3 1 OE2 C GLU 258 ? ? O   C HOH   401 ? ? 2.03 
# 
_pdbx_validate_rmsd_angle.id                         1 
_pdbx_validate_rmsd_angle.PDB_model_num              1 
_pdbx_validate_rmsd_angle.auth_atom_id_1             CA 
_pdbx_validate_rmsd_angle.auth_asym_id_1             C 
_pdbx_validate_rmsd_angle.auth_comp_id_1             CYS 
_pdbx_validate_rmsd_angle.auth_seq_id_1              238 
_pdbx_validate_rmsd_angle.PDB_ins_code_1             ? 
_pdbx_validate_rmsd_angle.label_alt_id_1             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_2             CB 
_pdbx_validate_rmsd_angle.auth_asym_id_2             C 
_pdbx_validate_rmsd_angle.auth_comp_id_2             CYS 
_pdbx_validate_rmsd_angle.auth_seq_id_2              238 
_pdbx_validate_rmsd_angle.PDB_ins_code_2             ? 
_pdbx_validate_rmsd_angle.label_alt_id_2             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_3             SG 
_pdbx_validate_rmsd_angle.auth_asym_id_3             C 
_pdbx_validate_rmsd_angle.auth_comp_id_3             CYS 
_pdbx_validate_rmsd_angle.auth_seq_id_3              238 
_pdbx_validate_rmsd_angle.PDB_ins_code_3             ? 
_pdbx_validate_rmsd_angle.label_alt_id_3             ? 
_pdbx_validate_rmsd_angle.angle_value                121.83 
_pdbx_validate_rmsd_angle.angle_target_value         114.20 
_pdbx_validate_rmsd_angle.angle_deviation            7.63 
_pdbx_validate_rmsd_angle.angle_standard_deviation   1.10 
_pdbx_validate_rmsd_angle.linker_flag                N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 VAL A 97  ? ? -29.58  131.64 
2  1 ALA A 138 ? ? 68.28   -0.39  
3  1 ARG A 248 ? ? 77.39   -1.17  
4  1 ALA B 138 ? ? 67.88   -0.49  
5  1 ASP B 184 ? ? -117.59 56.66  
6  1 ARG B 248 ? ? 78.49   -1.11  
7  1 ALA C 138 ? ? 68.72   -0.72  
8  1 ARG C 248 ? ? 78.36   -0.60  
9  1 VAL D 97  ? ? -30.16  130.32 
10 1 ALA D 138 ? ? 69.39   -0.28  
11 1 ASP D 184 ? ? -41.37  77.57  
# 
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 5.8290   -3.3427 9.4436  0.1687 ? -0.0025 ? 0.0132  ? 0.0003 ? 0.0010  ? 0.1884 ? 2.4732 ? 0.0905  
? 0.3054  ? 1.1532 ? 0.2232 ? 1.5177 ? -0.0033 ? -0.0044 ? -0.0393 ? -0.0380 ? 0.0043  ? -0.0276 ? 0.0559  ? 0.0180  ? -0.0010 ? 
2 'X-RAY DIFFRACTION' ? refined 2.7955   -2.6175 50.5523 0.1984 ? -0.0092 ? 0.0042  ? 0.0262 ? -0.0155 ? 0.2211 ? 2.9816 ? 0.0250  
? 0.0028  ? 0.7274 ? 0.1807 ? 1.7339 ? -0.0359 ? 0.2678  ? -0.1975 ? -0.0884 ? 0.0371  ? 0.0110  ? 0.0572  ? -0.0192 ? -0.0012 ? 
3 'X-RAY DIFFRACTION' ? refined -31.7607 5.1541  52.5069 0.1874 ? 0.0013  ? -0.0143 ? 0.0228 ? 0.0226  ? 0.2108 ? 3.3600 ? 0.0769  
? -0.3888 ? 0.7752 ? 0.1421 ? 1.4797 ? -0.0196 ? 0.0733  ? 0.1817  ? -0.0322 ? 0.0178  ? 0.0142  ? -0.0690 ? -0.0254 ? 0.0018  ? 
4 'X-RAY DIFFRACTION' ? refined -28.6620 5.0993  9.2745  0.1988 ? -0.0030 ? -0.0146 ? 0.0562 ? 0.0040  ? 0.2270 ? 2.4164 ? -0.1303 
? -0.3715 ? 1.0931 ? 0.1911 ? 1.5124 ? -0.0035 ? -0.0146 ? 0.1198  ? 0.0475  ? -0.0199 ? 0.0132  ? -0.0430 ? -0.0876 ? 0.0234  ? 
# 
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 96 ? ? ? A 301 ? ? ? 
2 'X-RAY DIFFRACTION' 2 ? ? B 97 ? ? ? B 301 ? ? ? 
3 'X-RAY DIFFRACTION' 3 ? ? C 96 ? ? ? C 301 ? ? ? 
4 'X-RAY DIFFRACTION' 4 ? ? D 95 ? ? ? D 401 ? ? ? 
# 
_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                      C 
_pdbx_distant_solvent_atoms.auth_comp_id                      HOH 
_pdbx_distant_solvent_atoms.auth_seq_id                       418 
_pdbx_distant_solvent_atoms.PDB_ins_code                      ? 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance   7.13 
_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 SER 94  ? A SER 1   
2  1 Y 1 A SER 95  ? A SER 2   
3  1 Y 1 A LEU 289 ? A LEU 196 
4  1 Y 1 A ARG 290 ? A ARG 197 
5  1 Y 1 A LYS 291 ? A LYS 198 
6  1 Y 1 A LYS 292 ? A LYS 199 
7  1 Y 1 A GLY 293 ? A GLY 200 
8  1 Y 1 B SER 94  ? B SER 1   
9  1 Y 1 B SER 95  ? B SER 2   
10 1 Y 1 B SER 96  ? B SER 3   
11 1 Y 1 B LEU 289 ? B LEU 196 
12 1 Y 1 B ARG 290 ? B ARG 197 
13 1 Y 1 B LYS 291 ? B LYS 198 
14 1 Y 1 B LYS 292 ? B LYS 199 
15 1 Y 1 B GLY 293 ? B GLY 200 
16 1 Y 1 C SER 94  ? C SER 1   
17 1 Y 1 C SER 95  ? C SER 2   
18 1 Y 1 C CYS 182 ? C CYS 89  
19 1 Y 1 C SER 183 ? C SER 90  
20 1 Y 1 C ASP 184 ? C ASP 91  
21 1 Y 1 C LEU 289 ? C LEU 196 
22 1 Y 1 C ARG 290 ? C ARG 197 
23 1 Y 1 C LYS 291 ? C LYS 198 
24 1 Y 1 C LYS 292 ? C LYS 199 
25 1 Y 1 C GLY 293 ? C GLY 200 
26 1 Y 1 D SER 94  ? D SER 1   
27 1 Y 1 D ARG 290 ? D ARG 197 
28 1 Y 1 D LYS 291 ? D LYS 198 
29 1 Y 1 D LYS 292 ? D LYS 199 
30 1 Y 1 D GLY 293 ? D GLY 200 
# 
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 
A1LU0 N1   N  N N 1   
A1LU0 C4   C  Y N 2   
A1LU0 C5   C  Y N 3   
A1LU0 C6   C  Y N 4   
A1LU0 C7   C  N N 5   
A1LU0 C8   C  N N 6   
A1LU0 C10  C  N N 7   
A1LU0 C13  C  N N 8   
A1LU0 C1   C  Y N 9   
A1LU0 C2   C  Y N 10  
A1LU0 C3   C  Y N 11  
A1LU0 C9   C  N N 12  
A1LU0 S    S  N N 13  
A1LU0 C11  C  N N 14  
A1LU0 N2   N  N N 15  
A1LU0 O1   O  N N 16  
A1LU0 C12  C  N N 17  
A1LU0 O2   O  N N 18  
A1LU0 O3   O  N N 19  
A1LU0 H2   H  N N 20  
A1LU0 H3   H  N N 21  
A1LU0 H4   H  N N 22  
A1LU0 H6   H  N N 23  
A1LU0 H7   H  N N 24  
A1LU0 H8   H  N N 25  
A1LU0 H10  H  N N 26  
A1LU0 H1   H  N N 27  
ALA   N    N  N N 28  
ALA   CA   C  N S 29  
ALA   C    C  N N 30  
ALA   O    O  N N 31  
ALA   CB   C  N N 32  
ALA   OXT  O  N N 33  
ALA   H    H  N N 34  
ALA   H2   H  N N 35  
ALA   HA   H  N N 36  
ALA   HB1  H  N N 37  
ALA   HB2  H  N N 38  
ALA   HB3  H  N N 39  
ALA   HXT  H  N N 40  
ARG   N    N  N N 41  
ARG   CA   C  N S 42  
ARG   C    C  N N 43  
ARG   O    O  N N 44  
ARG   CB   C  N N 45  
ARG   CG   C  N N 46  
ARG   CD   C  N N 47  
ARG   NE   N  N N 48  
ARG   CZ   C  N N 49  
ARG   NH1  N  N N 50  
ARG   NH2  N  N N 51  
ARG   OXT  O  N N 52  
ARG   H    H  N N 53  
ARG   H2   H  N N 54  
ARG   HA   H  N N 55  
ARG   HB2  H  N N 56  
ARG   HB3  H  N N 57  
ARG   HG2  H  N N 58  
ARG   HG3  H  N N 59  
ARG   HD2  H  N N 60  
ARG   HD3  H  N N 61  
ARG   HE   H  N N 62  
ARG   HH11 H  N N 63  
ARG   HH12 H  N N 64  
ARG   HH21 H  N N 65  
ARG   HH22 H  N N 66  
ARG   HXT  H  N N 67  
ASN   N    N  N N 68  
ASN   CA   C  N S 69  
ASN   C    C  N N 70  
ASN   O    O  N N 71  
ASN   CB   C  N N 72  
ASN   CG   C  N N 73  
ASN   OD1  O  N N 74  
ASN   ND2  N  N N 75  
ASN   OXT  O  N N 76  
ASN   H    H  N N 77  
ASN   H2   H  N N 78  
ASN   HA   H  N N 79  
ASN   HB2  H  N N 80  
ASN   HB3  H  N N 81  
ASN   HD21 H  N N 82  
ASN   HD22 H  N N 83  
ASN   HXT  H  N N 84  
ASP   N    N  N N 85  
ASP   CA   C  N S 86  
ASP   C    C  N N 87  
ASP   O    O  N N 88  
ASP   CB   C  N N 89  
ASP   CG   C  N N 90  
ASP   OD1  O  N N 91  
ASP   OD2  O  N N 92  
ASP   OXT  O  N N 93  
ASP   H    H  N N 94  
ASP   H2   H  N N 95  
ASP   HA   H  N N 96  
ASP   HB2  H  N N 97  
ASP   HB3  H  N N 98  
ASP   HD2  H  N N 99  
ASP   HXT  H  N N 100 
CYS   N    N  N N 101 
CYS   CA   C  N R 102 
CYS   C    C  N N 103 
CYS   O    O  N N 104 
CYS   CB   C  N N 105 
CYS   SG   S  N N 106 
CYS   OXT  O  N N 107 
CYS   H    H  N N 108 
CYS   H2   H  N N 109 
CYS   HA   H  N N 110 
CYS   HB2  H  N N 111 
CYS   HB3  H  N N 112 
CYS   HG   H  N N 113 
CYS   HXT  H  N N 114 
GLN   N    N  N N 115 
GLN   CA   C  N S 116 
GLN   C    C  N N 117 
GLN   O    O  N N 118 
GLN   CB   C  N N 119 
GLN   CG   C  N N 120 
GLN   CD   C  N N 121 
GLN   OE1  O  N N 122 
GLN   NE2  N  N N 123 
GLN   OXT  O  N N 124 
GLN   H    H  N N 125 
GLN   H2   H  N N 126 
GLN   HA   H  N N 127 
GLN   HB2  H  N N 128 
GLN   HB3  H  N N 129 
GLN   HG2  H  N N 130 
GLN   HG3  H  N N 131 
GLN   HE21 H  N N 132 
GLN   HE22 H  N N 133 
GLN   HXT  H  N N 134 
GLU   N    N  N N 135 
GLU   CA   C  N S 136 
GLU   C    C  N N 137 
GLU   O    O  N N 138 
GLU   CB   C  N N 139 
GLU   CG   C  N N 140 
GLU   CD   C  N N 141 
GLU   OE1  O  N N 142 
GLU   OE2  O  N N 143 
GLU   OXT  O  N N 144 
GLU   H    H  N N 145 
GLU   H2   H  N N 146 
GLU   HA   H  N N 147 
GLU   HB2  H  N N 148 
GLU   HB3  H  N N 149 
GLU   HG2  H  N N 150 
GLU   HG3  H  N N 151 
GLU   HE2  H  N N 152 
GLU   HXT  H  N N 153 
GLY   N    N  N N 154 
GLY   CA   C  N N 155 
GLY   C    C  N N 156 
GLY   O    O  N N 157 
GLY   OXT  O  N N 158 
GLY   H    H  N N 159 
GLY   H2   H  N N 160 
GLY   HA2  H  N N 161 
GLY   HA3  H  N N 162 
GLY   HXT  H  N N 163 
HIS   N    N  N N 164 
HIS   CA   C  N S 165 
HIS   C    C  N N 166 
HIS   O    O  N N 167 
HIS   CB   C  N N 168 
HIS   CG   C  Y N 169 
HIS   ND1  N  Y N 170 
HIS   CD2  C  Y N 171 
HIS   CE1  C  Y N 172 
HIS   NE2  N  Y N 173 
HIS   OXT  O  N N 174 
HIS   H    H  N N 175 
HIS   H2   H  N N 176 
HIS   HA   H  N N 177 
HIS   HB2  H  N N 178 
HIS   HB3  H  N N 179 
HIS   HD1  H  N N 180 
HIS   HD2  H  N N 181 
HIS   HE1  H  N N 182 
HIS   HE2  H  N N 183 
HIS   HXT  H  N N 184 
HOH   O    O  N N 185 
HOH   H1   H  N N 186 
HOH   H2   H  N N 187 
ILE   N    N  N N 188 
ILE   CA   C  N S 189 
ILE   C    C  N N 190 
ILE   O    O  N N 191 
ILE   CB   C  N S 192 
ILE   CG1  C  N N 193 
ILE   CG2  C  N N 194 
ILE   CD1  C  N N 195 
ILE   OXT  O  N N 196 
ILE   H    H  N N 197 
ILE   H2   H  N N 198 
ILE   HA   H  N N 199 
ILE   HB   H  N N 200 
ILE   HG12 H  N N 201 
ILE   HG13 H  N N 202 
ILE   HG21 H  N N 203 
ILE   HG22 H  N N 204 
ILE   HG23 H  N N 205 
ILE   HD11 H  N N 206 
ILE   HD12 H  N N 207 
ILE   HD13 H  N N 208 
ILE   HXT  H  N N 209 
LEU   N    N  N N 210 
LEU   CA   C  N S 211 
LEU   C    C  N N 212 
LEU   O    O  N N 213 
LEU   CB   C  N N 214 
LEU   CG   C  N N 215 
LEU   CD1  C  N N 216 
LEU   CD2  C  N N 217 
LEU   OXT  O  N N 218 
LEU   H    H  N N 219 
LEU   H2   H  N N 220 
LEU   HA   H  N N 221 
LEU   HB2  H  N N 222 
LEU   HB3  H  N N 223 
LEU   HG   H  N N 224 
LEU   HD11 H  N N 225 
LEU   HD12 H  N N 226 
LEU   HD13 H  N N 227 
LEU   HD21 H  N N 228 
LEU   HD22 H  N N 229 
LEU   HD23 H  N N 230 
LEU   HXT  H  N N 231 
LYS   N    N  N N 232 
LYS   CA   C  N S 233 
LYS   C    C  N N 234 
LYS   O    O  N N 235 
LYS   CB   C  N N 236 
LYS   CG   C  N N 237 
LYS   CD   C  N N 238 
LYS   CE   C  N N 239 
LYS   NZ   N  N N 240 
LYS   OXT  O  N N 241 
LYS   H    H  N N 242 
LYS   H2   H  N N 243 
LYS   HA   H  N N 244 
LYS   HB2  H  N N 245 
LYS   HB3  H  N N 246 
LYS   HG2  H  N N 247 
LYS   HG3  H  N N 248 
LYS   HD2  H  N N 249 
LYS   HD3  H  N N 250 
LYS   HE2  H  N N 251 
LYS   HE3  H  N N 252 
LYS   HZ1  H  N N 253 
LYS   HZ2  H  N N 254 
LYS   HZ3  H  N N 255 
LYS   HXT  H  N N 256 
MET   N    N  N N 257 
MET   CA   C  N S 258 
MET   C    C  N N 259 
MET   O    O  N N 260 
MET   CB   C  N N 261 
MET   CG   C  N N 262 
MET   SD   S  N N 263 
MET   CE   C  N N 264 
MET   OXT  O  N N 265 
MET   H    H  N N 266 
MET   H2   H  N N 267 
MET   HA   H  N N 268 
MET   HB2  H  N N 269 
MET   HB3  H  N N 270 
MET   HG2  H  N N 271 
MET   HG3  H  N N 272 
MET   HE1  H  N N 273 
MET   HE2  H  N N 274 
MET   HE3  H  N N 275 
MET   HXT  H  N N 276 
PHE   N    N  N N 277 
PHE   CA   C  N S 278 
PHE   C    C  N N 279 
PHE   O    O  N N 280 
PHE   CB   C  N N 281 
PHE   CG   C  Y N 282 
PHE   CD1  C  Y N 283 
PHE   CD2  C  Y N 284 
PHE   CE1  C  Y N 285 
PHE   CE2  C  Y N 286 
PHE   CZ   C  Y N 287 
PHE   OXT  O  N N 288 
PHE   H    H  N N 289 
PHE   H2   H  N N 290 
PHE   HA   H  N N 291 
PHE   HB2  H  N N 292 
PHE   HB3  H  N N 293 
PHE   HD1  H  N N 294 
PHE   HD2  H  N N 295 
PHE   HE1  H  N N 296 
PHE   HE2  H  N N 297 
PHE   HZ   H  N N 298 
PHE   HXT  H  N N 299 
PRO   N    N  N N 300 
PRO   CA   C  N S 301 
PRO   C    C  N N 302 
PRO   O    O  N N 303 
PRO   CB   C  N N 304 
PRO   CG   C  N N 305 
PRO   CD   C  N N 306 
PRO   OXT  O  N N 307 
PRO   H    H  N N 308 
PRO   HA   H  N N 309 
PRO   HB2  H  N N 310 
PRO   HB3  H  N N 311 
PRO   HG2  H  N N 312 
PRO   HG3  H  N N 313 
PRO   HD2  H  N N 314 
PRO   HD3  H  N N 315 
PRO   HXT  H  N N 316 
SER   N    N  N N 317 
SER   CA   C  N S 318 
SER   C    C  N N 319 
SER   O    O  N N 320 
SER   CB   C  N N 321 
SER   OG   O  N N 322 
SER   OXT  O  N N 323 
SER   H    H  N N 324 
SER   H2   H  N N 325 
SER   HA   H  N N 326 
SER   HB2  H  N N 327 
SER   HB3  H  N N 328 
SER   HG   H  N N 329 
SER   HXT  H  N N 330 
THR   N    N  N N 331 
THR   CA   C  N S 332 
THR   C    C  N N 333 
THR   O    O  N N 334 
THR   CB   C  N R 335 
THR   OG1  O  N N 336 
THR   CG2  C  N N 337 
THR   OXT  O  N N 338 
THR   H    H  N N 339 
THR   H2   H  N N 340 
THR   HA   H  N N 341 
THR   HB   H  N N 342 
THR   HG1  H  N N 343 
THR   HG21 H  N N 344 
THR   HG22 H  N N 345 
THR   HG23 H  N N 346 
THR   HXT  H  N N 347 
TRP   N    N  N N 348 
TRP   CA   C  N S 349 
TRP   C    C  N N 350 
TRP   O    O  N N 351 
TRP   CB   C  N N 352 
TRP   CG   C  Y N 353 
TRP   CD1  C  Y N 354 
TRP   CD2  C  Y N 355 
TRP   NE1  N  Y N 356 
TRP   CE2  C  Y N 357 
TRP   CE3  C  Y N 358 
TRP   CZ2  C  Y N 359 
TRP   CZ3  C  Y N 360 
TRP   CH2  C  Y N 361 
TRP   OXT  O  N N 362 
TRP   H    H  N N 363 
TRP   H2   H  N N 364 
TRP   HA   H  N N 365 
TRP   HB2  H  N N 366 
TRP   HB3  H  N N 367 
TRP   HD1  H  N N 368 
TRP   HE1  H  N N 369 
TRP   HE3  H  N N 370 
TRP   HZ2  H  N N 371 
TRP   HZ3  H  N N 372 
TRP   HH2  H  N N 373 
TRP   HXT  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 
ZN    ZN   ZN N N 418 
# 
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 
A1LU0 C6  C1   doub Y N 1   
A1LU0 C6  C5   sing Y N 2   
A1LU0 C1  C2   sing Y N 3   
A1LU0 C5  C4   doub Y N 4   
A1LU0 C2  C7   sing N N 5   
A1LU0 C2  C3   doub Y N 6   
A1LU0 C7  C8   trip N N 7   
A1LU0 C4  C3   sing Y N 8   
A1LU0 C4  N1   sing N N 9   
A1LU0 N1  C9   doub N N 10  
A1LU0 C9  S    sing N N 11  
A1LU0 C9  N2   sing N N 12  
A1LU0 S   C10  sing N N 13  
A1LU0 O3  C13  doub N N 14  
A1LU0 N2  C11  sing N N 15  
A1LU0 C13 C12  sing N N 16  
A1LU0 C13 O2   sing N N 17  
A1LU0 C11 C10  sing N N 18  
A1LU0 C11 O1   doub N N 19  
A1LU0 C10 C12  doub N Z 20  
A1LU0 C5  H2   sing N N 21  
A1LU0 C6  H3   sing N N 22  
A1LU0 C8  H4   sing N N 23  
A1LU0 C1  H6   sing N N 24  
A1LU0 C3  H7   sing N N 25  
A1LU0 C12 H8   sing N N 26  
A1LU0 O2  H10  sing N N 27  
A1LU0 N2  H1   sing N N 28  
ALA   N   CA   sing N N 29  
ALA   N   H    sing N N 30  
ALA   N   H2   sing N N 31  
ALA   CA  C    sing N N 32  
ALA   CA  CB   sing N N 33  
ALA   CA  HA   sing N N 34  
ALA   C   O    doub N N 35  
ALA   C   OXT  sing N N 36  
ALA   CB  HB1  sing N N 37  
ALA   CB  HB2  sing N N 38  
ALA   CB  HB3  sing N N 39  
ALA   OXT HXT  sing N N 40  
ARG   N   CA   sing N N 41  
ARG   N   H    sing N N 42  
ARG   N   H2   sing N N 43  
ARG   CA  C    sing N N 44  
ARG   CA  CB   sing N N 45  
ARG   CA  HA   sing N N 46  
ARG   C   O    doub N N 47  
ARG   C   OXT  sing N N 48  
ARG   CB  CG   sing N N 49  
ARG   CB  HB2  sing N N 50  
ARG   CB  HB3  sing N N 51  
ARG   CG  CD   sing N N 52  
ARG   CG  HG2  sing N N 53  
ARG   CG  HG3  sing N N 54  
ARG   CD  NE   sing N N 55  
ARG   CD  HD2  sing N N 56  
ARG   CD  HD3  sing N N 57  
ARG   NE  CZ   sing N N 58  
ARG   NE  HE   sing N N 59  
ARG   CZ  NH1  sing N N 60  
ARG   CZ  NH2  doub N N 61  
ARG   NH1 HH11 sing N N 62  
ARG   NH1 HH12 sing N N 63  
ARG   NH2 HH21 sing N N 64  
ARG   NH2 HH22 sing N N 65  
ARG   OXT HXT  sing N N 66  
ASN   N   CA   sing N N 67  
ASN   N   H    sing N N 68  
ASN   N   H2   sing N N 69  
ASN   CA  C    sing N N 70  
ASN   CA  CB   sing N N 71  
ASN   CA  HA   sing N N 72  
ASN   C   O    doub N N 73  
ASN   C   OXT  sing N N 74  
ASN   CB  CG   sing N N 75  
ASN   CB  HB2  sing N N 76  
ASN   CB  HB3  sing N N 77  
ASN   CG  OD1  doub N N 78  
ASN   CG  ND2  sing N N 79  
ASN   ND2 HD21 sing N N 80  
ASN   ND2 HD22 sing N N 81  
ASN   OXT HXT  sing N N 82  
ASP   N   CA   sing N N 83  
ASP   N   H    sing N N 84  
ASP   N   H2   sing N N 85  
ASP   CA  C    sing N N 86  
ASP   CA  CB   sing N N 87  
ASP   CA  HA   sing N N 88  
ASP   C   O    doub N N 89  
ASP   C   OXT  sing N N 90  
ASP   CB  CG   sing N N 91  
ASP   CB  HB2  sing N N 92  
ASP   CB  HB3  sing N N 93  
ASP   CG  OD1  doub N N 94  
ASP   CG  OD2  sing N N 95  
ASP   OD2 HD2  sing N N 96  
ASP   OXT HXT  sing N N 97  
CYS   N   CA   sing N N 98  
CYS   N   H    sing N N 99  
CYS   N   H2   sing N N 100 
CYS   CA  C    sing N N 101 
CYS   CA  CB   sing N N 102 
CYS   CA  HA   sing N N 103 
CYS   C   O    doub N N 104 
CYS   C   OXT  sing N N 105 
CYS   CB  SG   sing N N 106 
CYS   CB  HB2  sing N N 107 
CYS   CB  HB3  sing N N 108 
CYS   SG  HG   sing N N 109 
CYS   OXT HXT  sing N N 110 
GLN   N   CA   sing N N 111 
GLN   N   H    sing N N 112 
GLN   N   H2   sing N N 113 
GLN   CA  C    sing N N 114 
GLN   CA  CB   sing N N 115 
GLN   CA  HA   sing N N 116 
GLN   C   O    doub N N 117 
GLN   C   OXT  sing N N 118 
GLN   CB  CG   sing N N 119 
GLN   CB  HB2  sing N N 120 
GLN   CB  HB3  sing N N 121 
GLN   CG  CD   sing N N 122 
GLN   CG  HG2  sing N N 123 
GLN   CG  HG3  sing N N 124 
GLN   CD  OE1  doub N N 125 
GLN   CD  NE2  sing N N 126 
GLN   NE2 HE21 sing N N 127 
GLN   NE2 HE22 sing N N 128 
GLN   OXT HXT  sing N N 129 
GLU   N   CA   sing N N 130 
GLU   N   H    sing N N 131 
GLU   N   H2   sing N N 132 
GLU   CA  C    sing N N 133 
GLU   CA  CB   sing N N 134 
GLU   CA  HA   sing N N 135 
GLU   C   O    doub N N 136 
GLU   C   OXT  sing N N 137 
GLU   CB  CG   sing N N 138 
GLU   CB  HB2  sing N N 139 
GLU   CB  HB3  sing N N 140 
GLU   CG  CD   sing N N 141 
GLU   CG  HG2  sing N N 142 
GLU   CG  HG3  sing N N 143 
GLU   CD  OE1  doub N N 144 
GLU   CD  OE2  sing N N 145 
GLU   OE2 HE2  sing N N 146 
GLU   OXT HXT  sing N N 147 
GLY   N   CA   sing N N 148 
GLY   N   H    sing N N 149 
GLY   N   H2   sing N N 150 
GLY   CA  C    sing N N 151 
GLY   CA  HA2  sing N N 152 
GLY   CA  HA3  sing N N 153 
GLY   C   O    doub N N 154 
GLY   C   OXT  sing N N 155 
GLY   OXT HXT  sing N N 156 
HIS   N   CA   sing N N 157 
HIS   N   H    sing N N 158 
HIS   N   H2   sing N N 159 
HIS   CA  C    sing N N 160 
HIS   CA  CB   sing N N 161 
HIS   CA  HA   sing N N 162 
HIS   C   O    doub N N 163 
HIS   C   OXT  sing N N 164 
HIS   CB  CG   sing N N 165 
HIS   CB  HB2  sing N N 166 
HIS   CB  HB3  sing N N 167 
HIS   CG  ND1  sing Y N 168 
HIS   CG  CD2  doub Y N 169 
HIS   ND1 CE1  doub Y N 170 
HIS   ND1 HD1  sing N N 171 
HIS   CD2 NE2  sing Y N 172 
HIS   CD2 HD2  sing N N 173 
HIS   CE1 NE2  sing Y N 174 
HIS   CE1 HE1  sing N N 175 
HIS   NE2 HE2  sing N N 176 
HIS   OXT HXT  sing N N 177 
HOH   O   H1   sing N N 178 
HOH   O   H2   sing N N 179 
ILE   N   CA   sing N N 180 
ILE   N   H    sing N N 181 
ILE   N   H2   sing N N 182 
ILE   CA  C    sing N N 183 
ILE   CA  CB   sing N N 184 
ILE   CA  HA   sing N N 185 
ILE   C   O    doub N N 186 
ILE   C   OXT  sing N N 187 
ILE   CB  CG1  sing N N 188 
ILE   CB  CG2  sing N N 189 
ILE   CB  HB   sing N N 190 
ILE   CG1 CD1  sing N N 191 
ILE   CG1 HG12 sing N N 192 
ILE   CG1 HG13 sing N N 193 
ILE   CG2 HG21 sing N N 194 
ILE   CG2 HG22 sing N N 195 
ILE   CG2 HG23 sing N N 196 
ILE   CD1 HD11 sing N N 197 
ILE   CD1 HD12 sing N N 198 
ILE   CD1 HD13 sing N N 199 
ILE   OXT HXT  sing N N 200 
LEU   N   CA   sing N N 201 
LEU   N   H    sing N N 202 
LEU   N   H2   sing N N 203 
LEU   CA  C    sing N N 204 
LEU   CA  CB   sing N N 205 
LEU   CA  HA   sing N N 206 
LEU   C   O    doub N N 207 
LEU   C   OXT  sing N N 208 
LEU   CB  CG   sing N N 209 
LEU   CB  HB2  sing N N 210 
LEU   CB  HB3  sing N N 211 
LEU   CG  CD1  sing N N 212 
LEU   CG  CD2  sing N N 213 
LEU   CG  HG   sing N N 214 
LEU   CD1 HD11 sing N N 215 
LEU   CD1 HD12 sing N N 216 
LEU   CD1 HD13 sing N N 217 
LEU   CD2 HD21 sing N N 218 
LEU   CD2 HD22 sing N N 219 
LEU   CD2 HD23 sing N N 220 
LEU   OXT HXT  sing N N 221 
LYS   N   CA   sing N N 222 
LYS   N   H    sing N N 223 
LYS   N   H2   sing N N 224 
LYS   CA  C    sing N N 225 
LYS   CA  CB   sing N N 226 
LYS   CA  HA   sing N N 227 
LYS   C   O    doub N N 228 
LYS   C   OXT  sing N N 229 
LYS   CB  CG   sing N N 230 
LYS   CB  HB2  sing N N 231 
LYS   CB  HB3  sing N N 232 
LYS   CG  CD   sing N N 233 
LYS   CG  HG2  sing N N 234 
LYS   CG  HG3  sing N N 235 
LYS   CD  CE   sing N N 236 
LYS   CD  HD2  sing N N 237 
LYS   CD  HD3  sing N N 238 
LYS   CE  NZ   sing N N 239 
LYS   CE  HE2  sing N N 240 
LYS   CE  HE3  sing N N 241 
LYS   NZ  HZ1  sing N N 242 
LYS   NZ  HZ2  sing N N 243 
LYS   NZ  HZ3  sing N N 244 
LYS   OXT HXT  sing N N 245 
MET   N   CA   sing N N 246 
MET   N   H    sing N N 247 
MET   N   H2   sing N N 248 
MET   CA  C    sing N N 249 
MET   CA  CB   sing N N 250 
MET   CA  HA   sing N N 251 
MET   C   O    doub N N 252 
MET   C   OXT  sing N N 253 
MET   CB  CG   sing N N 254 
MET   CB  HB2  sing N N 255 
MET   CB  HB3  sing N N 256 
MET   CG  SD   sing N N 257 
MET   CG  HG2  sing N N 258 
MET   CG  HG3  sing N N 259 
MET   SD  CE   sing N N 260 
MET   CE  HE1  sing N N 261 
MET   CE  HE2  sing N N 262 
MET   CE  HE3  sing N N 263 
MET   OXT HXT  sing N N 264 
PHE   N   CA   sing N N 265 
PHE   N   H    sing N N 266 
PHE   N   H2   sing N N 267 
PHE   CA  C    sing N N 268 
PHE   CA  CB   sing N N 269 
PHE   CA  HA   sing N N 270 
PHE   C   O    doub N N 271 
PHE   C   OXT  sing N N 272 
PHE   CB  CG   sing N N 273 
PHE   CB  HB2  sing N N 274 
PHE   CB  HB3  sing N N 275 
PHE   CG  CD1  doub Y N 276 
PHE   CG  CD2  sing Y N 277 
PHE   CD1 CE1  sing Y N 278 
PHE   CD1 HD1  sing N N 279 
PHE   CD2 CE2  doub Y N 280 
PHE   CD2 HD2  sing N N 281 
PHE   CE1 CZ   doub Y N 282 
PHE   CE1 HE1  sing N N 283 
PHE   CE2 CZ   sing Y N 284 
PHE   CE2 HE2  sing N N 285 
PHE   CZ  HZ   sing N N 286 
PHE   OXT HXT  sing N N 287 
PRO   N   CA   sing N N 288 
PRO   N   CD   sing N N 289 
PRO   N   H    sing N N 290 
PRO   CA  C    sing N N 291 
PRO   CA  CB   sing N N 292 
PRO   CA  HA   sing N N 293 
PRO   C   O    doub N N 294 
PRO   C   OXT  sing N N 295 
PRO   CB  CG   sing N N 296 
PRO   CB  HB2  sing N N 297 
PRO   CB  HB3  sing N N 298 
PRO   CG  CD   sing N N 299 
PRO   CG  HG2  sing N N 300 
PRO   CG  HG3  sing N N 301 
PRO   CD  HD2  sing N N 302 
PRO   CD  HD3  sing N N 303 
PRO   OXT HXT  sing N N 304 
SER   N   CA   sing N N 305 
SER   N   H    sing N N 306 
SER   N   H2   sing N N 307 
SER   CA  C    sing N N 308 
SER   CA  CB   sing N N 309 
SER   CA  HA   sing N N 310 
SER   C   O    doub N N 311 
SER   C   OXT  sing N N 312 
SER   CB  OG   sing N N 313 
SER   CB  HB2  sing N N 314 
SER   CB  HB3  sing N N 315 
SER   OG  HG   sing N N 316 
SER   OXT HXT  sing N N 317 
THR   N   CA   sing N N 318 
THR   N   H    sing N N 319 
THR   N   H2   sing N N 320 
THR   CA  C    sing N N 321 
THR   CA  CB   sing N N 322 
THR   CA  HA   sing N N 323 
THR   C   O    doub N N 324 
THR   C   OXT  sing N N 325 
THR   CB  OG1  sing N N 326 
THR   CB  CG2  sing N N 327 
THR   CB  HB   sing N N 328 
THR   OG1 HG1  sing N N 329 
THR   CG2 HG21 sing N N 330 
THR   CG2 HG22 sing N N 331 
THR   CG2 HG23 sing N N 332 
THR   OXT HXT  sing N N 333 
TRP   N   CA   sing N N 334 
TRP   N   H    sing N N 335 
TRP   N   H2   sing N N 336 
TRP   CA  C    sing N N 337 
TRP   CA  CB   sing N N 338 
TRP   CA  HA   sing N N 339 
TRP   C   O    doub N N 340 
TRP   C   OXT  sing N N 341 
TRP   CB  CG   sing N N 342 
TRP   CB  HB2  sing N N 343 
TRP   CB  HB3  sing N N 344 
TRP   CG  CD1  doub Y N 345 
TRP   CG  CD2  sing Y N 346 
TRP   CD1 NE1  sing Y N 347 
TRP   CD1 HD1  sing N N 348 
TRP   CD2 CE2  doub Y N 349 
TRP   CD2 CE3  sing Y N 350 
TRP   NE1 CE2  sing Y N 351 
TRP   NE1 HE1  sing N N 352 
TRP   CE2 CZ2  sing Y N 353 
TRP   CE3 CZ3  doub Y N 354 
TRP   CE3 HE3  sing N N 355 
TRP   CZ2 CH2  doub Y N 356 
TRP   CZ2 HZ2  sing N N 357 
TRP   CZ3 CH2  sing Y N 358 
TRP   CZ3 HZ3  sing N N 359 
TRP   CH2 HH2  sing N N 360 
TRP   OXT HXT  sing N N 361 
TYR   N   CA   sing N N 362 
TYR   N   H    sing N N 363 
TYR   N   H2   sing N N 364 
TYR   CA  C    sing N N 365 
TYR   CA  CB   sing N N 366 
TYR   CA  HA   sing N N 367 
TYR   C   O    doub N N 368 
TYR   C   OXT  sing N N 369 
TYR   CB  CG   sing N N 370 
TYR   CB  HB2  sing N N 371 
TYR   CB  HB3  sing N N 372 
TYR   CG  CD1  doub Y N 373 
TYR   CG  CD2  sing Y N 374 
TYR   CD1 CE1  sing Y N 375 
TYR   CD1 HD1  sing N N 376 
TYR   CD2 CE2  doub Y N 377 
TYR   CD2 HD2  sing N N 378 
TYR   CE1 CZ   doub Y N 379 
TYR   CE1 HE1  sing N N 380 
TYR   CE2 CZ   sing Y N 381 
TYR   CE2 HE2  sing N N 382 
TYR   CZ  OH   sing N N 383 
TYR   OH  HH   sing N N 384 
TYR   OXT HXT  sing N N 385 
VAL   N   CA   sing N N 386 
VAL   N   H    sing N N 387 
VAL   N   H2   sing N N 388 
VAL   CA  C    sing N N 389 
VAL   CA  CB   sing N N 390 
VAL   CA  HA   sing N N 391 
VAL   C   O    doub N N 392 
VAL   C   OXT  sing N N 393 
VAL   CB  CG1  sing N N 394 
VAL   CB  CG2  sing N N 395 
VAL   CB  HB   sing N N 396 
VAL   CG1 HG11 sing N N 397 
VAL   CG1 HG12 sing N N 398 
VAL   CG1 HG13 sing N N 399 
VAL   CG2 HG21 sing N N 400 
VAL   CG2 HG22 sing N N 401 
VAL   CG2 HG23 sing N N 402 
VAL   OXT HXT  sing N N 403 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'National Natural Science Foundation of China (NSFC)' China 81622002 1 
'National Natural Science Foundation of China (NSFC)' China 81861130368 2 
'Other government'                                    China 'Shanghai Youth Talent Development Program (2017275)' 3 
'Other government'                                    China 
'Shanghai Collaborative Innovation Center for Translational Medicine (TM201902)'        4 
'Other government'                                    China 
'Foundation of National Facility for Translational Medicine (Shanghai) (TMSK-2020-003)' 5 
'Other government'                                    China 
'Shanghai Medical and Health Excellent Discipline Leader Development Plan (2018BR36)'   6 
# 
_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   6GGB 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    8XCE 
_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]   0.014507 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   -0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.013928 
_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]   0.011818 
_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  
N  
O  
S  
ZN 
# 
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   . SER   A 1 3   ? 15.896  -19.991 16.424  1.00 57.03 ? 96  SER   A N   1 
ATOM   2    C  CA  . SER   A 1 3   ? 14.969  -19.475 17.485  1.00 56.49 ? 96  SER   A CA  1 
ATOM   3    C  C   . SER   A 1 3   ? 14.213  -18.237 16.978  1.00 54.19 ? 96  SER   A C   1 
ATOM   4    O  O   . SER   A 1 3   ? 14.478  -17.130 17.480  1.00 53.79 ? 96  SER   A O   1 
ATOM   5    C  CB  . SER   A 1 3   ? 15.712  -19.178 18.767  1.00 57.36 ? 96  SER   A CB  1 
ATOM   6    O  OG  . SER   A 1 3   ? 16.603  -18.084 18.597  1.00 57.80 ? 96  SER   A OG  1 
ATOM   7    N  N   . VAL   A 1 4   ? 13.295  -18.442 16.028  1.00 51.83 ? 97  VAL   A N   1 
ATOM   8    C  CA  . VAL   A 1 4   ? 12.325  -17.439 15.480  1.00 49.23 ? 97  VAL   A CA  1 
ATOM   9    C  C   . VAL   A 1 4   ? 11.982  -16.407 16.554  1.00 47.32 ? 97  VAL   A C   1 
ATOM   10   O  O   . VAL   A 1 4   ? 11.667  -16.784 17.683  1.00 47.44 ? 97  VAL   A O   1 
ATOM   11   C  CB  . VAL   A 1 4   ? 11.042  -18.144 14.987  1.00 49.55 ? 97  VAL   A CB  1 
ATOM   12   C  CG1 . VAL   A 1 4   ? 10.010  -17.155 14.475  1.00 48.89 ? 97  VAL   A CG1 1 
ATOM   13   C  CG2 . VAL   A 1 4   ? 11.328  -19.198 13.933  1.00 51.33 ? 97  VAL   A CG2 1 
ATOM   14   N  N   . PRO   A 1 5   ? 12.030  -15.088 16.246  1.00 44.05 ? 98  PRO   A N   1 
ATOM   15   C  CA  . PRO   A 1 5   ? 11.616  -14.054 17.192  1.00 43.27 ? 98  PRO   A CA  1 
ATOM   16   C  C   . PRO   A 1 5   ? 10.122  -14.126 17.537  1.00 41.85 ? 98  PRO   A C   1 
ATOM   17   O  O   . PRO   A 1 5   ? 9.311   -14.445 16.672  1.00 39.79 ? 98  PRO   A O   1 
ATOM   18   C  CB  . PRO   A 1 5   ? 11.937  -12.718 16.502  1.00 42.09 ? 98  PRO   A CB  1 
ATOM   19   C  CG  . PRO   A 1 5   ? 12.072  -13.051 15.025  1.00 42.27 ? 98  PRO   A CG  1 
ATOM   20   C  CD  . PRO   A 1 5   ? 12.502  -14.509 14.981  1.00 43.42 ? 98  PRO   A CD  1 
ATOM   21   N  N   . SER   A 1 6   ? 9.805   -13.831 18.801  1.00 42.02 ? 99  SER   A N   1 
ATOM   22   C  CA  . SER   A 1 6   ? 8.446   -13.956 19.389  1.00 41.61 ? 99  SER   A CA  1 
ATOM   23   C  C   . SER   A 1 6   ? 7.490   -13.001 18.672  1.00 39.62 ? 99  SER   A C   1 
ATOM   24   O  O   . SER   A 1 6   ? 7.905   -11.862 18.364  1.00 39.90 ? 99  SER   A O   1 
ATOM   25   C  CB  . SER   A 1 6   ? 8.479   -13.693 20.870  1.00 42.90 ? 99  SER   A CB  1 
ATOM   26   O  OG  . SER   A 1 6   ? 7.165   -13.566 21.393  1.00 43.95 ? 99  SER   A OG  1 
ATOM   27   N  N   . GLN   A 1 7   ? 6.259   -13.450 18.429  1.00 38.14 ? 100 GLN   A N   1 
ATOM   28   C  CA  . GLN   A 1 7   ? 5.175   -12.625 17.832  1.00 36.30 ? 100 GLN   A CA  1 
ATOM   29   C  C   . GLN   A 1 7   ? 4.028   -12.478 18.837  1.00 36.81 ? 100 GLN   A C   1 
ATOM   30   O  O   . GLN   A 1 7   ? 2.997   -11.908 18.460  1.00 36.16 ? 100 GLN   A O   1 
ATOM   31   C  CB  . GLN   A 1 7   ? 4.720   -13.232 16.508  1.00 35.43 ? 100 GLN   A CB  1 
ATOM   32   C  CG  . GLN   A 1 7   ? 3.986   -14.553 16.633  1.00 36.34 ? 100 GLN   A CG  1 
ATOM   33   C  CD  . GLN   A 1 7   ? 3.709   -15.146 15.267  1.00 35.46 ? 100 GLN   A CD  1 
ATOM   34   O  OE1 . GLN   A 1 7   ? 4.572   -15.761 14.657  1.00 36.56 ? 100 GLN   A OE1 1 
ATOM   35   N  NE2 . GLN   A 1 7   ? 2.493   -14.999 14.776  1.00 35.04 ? 100 GLN   A NE2 1 
ATOM   36   N  N   . LYS   A 1 8   ? 4.203   -12.963 20.071  1.00 38.24 ? 101 LYS   A N   1 
ATOM   37   C  CA  . LYS   A 1 8   ? 3.144   -12.957 21.119  1.00 39.91 ? 101 LYS   A CA  1 
ATOM   38   C  C   . LYS   A 1 8   ? 2.818   -11.502 21.509  1.00 39.17 ? 101 LYS   A C   1 
ATOM   39   O  O   . LYS   A 1 8   ? 3.743   -10.764 21.864  1.00 39.04 ? 101 LYS   A O   1 
ATOM   40   C  CB  . LYS   A 1 8   ? 3.600   -13.792 22.319  1.00 42.15 ? 101 LYS   A CB  1 
ATOM   41   C  CG  . LYS   A 1 8   ? 2.579   -13.950 23.438  1.00 43.46 ? 101 LYS   A CG  1 
ATOM   42   C  CD  . LYS   A 1 8   ? 1.201   -14.394 22.966  1.00 44.46 ? 101 LYS   A CD  1 
ATOM   43   C  CE  . LYS   A 1 8   ? 0.077   -13.932 23.867  1.00 45.00 ? 101 LYS   A CE  1 
ATOM   44   N  NZ  . LYS   A 1 8   ? 0.172   -14.549 25.209  1.00 46.60 ? 101 LYS   A NZ  1 
ATOM   45   N  N   . THR   A 1 9   ? 1.544   -11.118 21.439  1.00 38.45 ? 102 THR   A N   1 
ATOM   46   C  CA  . THR   A 1 9   ? 1.045   -9.777  21.834  1.00 38.17 ? 102 THR   A CA  1 
ATOM   47   C  C   . THR   A 1 9   ? 1.336   -9.544  23.317  1.00 38.62 ? 102 THR   A C   1 
ATOM   48   O  O   . THR   A 1 9   ? 1.208   -10.482 24.104  1.00 39.70 ? 102 THR   A O   1 
ATOM   49   C  CB  . THR   A 1 9   ? -0.450  -9.610  21.544  1.00 37.83 ? 102 THR   A CB  1 
ATOM   50   O  OG1 . THR   A 1 9   ? -0.613  -9.849  20.153  1.00 37.87 ? 102 THR   A OG1 1 
ATOM   51   C  CG2 . THR   A 1 9   ? -0.969  -8.229  21.887  1.00 37.54 ? 102 THR   A CG2 1 
ATOM   52   N  N   . TYR   A 1 10  ? 1.715   -8.317  23.662  1.00 38.80 ? 103 TYR   A N   1 
ATOM   53   C  CA  . TYR   A 1 10  ? 2.138   -7.902  25.021  1.00 39.69 ? 103 TYR   A CA  1 
ATOM   54   C  C   . TYR   A 1 10  ? 1.933   -6.389  25.150  1.00 38.02 ? 103 TYR   A C   1 
ATOM   55   O  O   . TYR   A 1 10  ? 2.781   -5.636  24.669  1.00 36.17 ? 103 TYR   A O   1 
ATOM   56   C  CB  . TYR   A 1 10  ? 3.623   -8.213  25.231  1.00 41.13 ? 103 TYR   A CB  1 
ATOM   57   C  CG  . TYR   A 1 10  ? 4.043   -9.481  25.926  1.00 43.80 ? 103 TYR   A CG  1 
ATOM   58   C  CD1 . TYR   A 1 10  ? 3.969   -10.715 25.298  1.00 44.75 ? 103 TYR   A CD1 1 
ATOM   59   C  CD2 . TYR   A 1 10  ? 4.650   -9.431  27.174  1.00 45.56 ? 103 TYR   A CD2 1 
ATOM   60   C  CE1 . TYR   A 1 10  ? 4.398   -11.872 25.927  1.00 46.37 ? 103 TYR   A CE1 1 
ATOM   61   C  CE2 . TYR   A 1 10  ? 5.098   -10.573 27.811  1.00 47.00 ? 103 TYR   A CE2 1 
ATOM   62   C  CZ  . TYR   A 1 10  ? 4.966   -11.798 27.186  1.00 47.27 ? 103 TYR   A CZ  1 
ATOM   63   O  OH  . TYR   A 1 10  ? 5.419   -12.918 27.814  1.00 49.54 ? 103 TYR   A OH  1 
ATOM   64   N  N   . GLN   A 1 11  ? 0.823   -5.958  25.740  1.00 38.03 ? 104 GLN   A N   1 
ATOM   65   C  CA  . GLN   A 1 11  ? 0.510   -4.510  25.910  1.00 37.30 ? 104 GLN   A CA  1 
ATOM   66   C  C   . GLN   A 1 11  ? 1.461   -3.942  26.967  1.00 37.51 ? 104 GLN   A C   1 
ATOM   67   O  O   . GLN   A 1 11  ? 1.843   -2.770  26.845  1.00 37.12 ? 104 GLN   A O   1 
ATOM   68   C  CB  . GLN   A 1 11  ? -0.963  -4.332  26.272  1.00 37.92 ? 104 GLN   A CB  1 
ATOM   69   C  CG  . GLN   A 1 11  ? -1.907  -4.788  25.165  1.00 37.73 ? 104 GLN   A CG  1 
ATOM   70   C  CD  . GLN   A 1 11  ? -3.308  -4.246  25.328  1.00 38.26 ? 104 GLN   A CD  1 
ATOM   71   O  OE1 . GLN   A 1 11  ? -3.731  -3.867  26.417  1.00 39.45 ? 104 GLN   A OE1 1 
ATOM   72   N  NE2 . GLN   A 1 11  ? -4.041  -4.181  24.227  1.00 37.84 ? 104 GLN   A NE2 1 
ATOM   73   N  N   . GLY   A 1 12  ? 1.829   -4.760  27.954  1.00 38.15 ? 105 GLY   A N   1 
ATOM   74   C  CA  . GLY   A 1 12  ? 2.821   -4.430  28.996  1.00 39.50 ? 105 GLY   A CA  1 
ATOM   75   C  C   . GLY   A 1 12  ? 2.456   -3.174  29.766  1.00 39.93 ? 105 GLY   A C   1 
ATOM   76   O  O   . GLY   A 1 12  ? 1.249   -2.864  29.867  1.00 41.34 ? 105 GLY   A O   1 
ATOM   77   N  N   . SER   A 1 13  ? 3.467   -2.469  30.265  1.00 39.62 ? 106 SER   A N   1 
ATOM   78   C  CA  . SER   A 1 13  ? 3.385   -1.467  31.356  1.00 41.23 ? 106 SER   A CA  1 
ATOM   79   C  C   . SER   A 1 13  ? 2.650   -0.215  30.869  1.00 40.66 ? 106 SER   A C   1 
ATOM   80   O  O   . SER   A 1 13  ? 1.978   0.415   31.706  1.00 42.56 ? 106 SER   A O   1 
ATOM   81   C  CB  . SER   A 1 13  ? 4.778   -1.144  31.868  1.00 41.36 ? 106 SER   A CB  1 
ATOM   82   O  OG  . SER   A 1 13  ? 4.761   -0.088  32.818  1.00 43.34 ? 106 SER   A OG  1 
ATOM   83   N  N   . TYR   A 1 14  ? 2.760   0.124   29.578  1.00 38.52 ? 107 TYR   A N   1 
ATOM   84   C  CA  . TYR   A 1 14  ? 2.282   1.413   29.018  1.00 38.19 ? 107 TYR   A CA  1 
ATOM   85   C  C   . TYR   A 1 14  ? 0.976   1.231   28.240  1.00 37.64 ? 107 TYR   A C   1 
ATOM   86   O  O   . TYR   A 1 14  ? 0.520   2.212   27.669  1.00 37.23 ? 107 TYR   A O   1 
ATOM   87   C  CB  . TYR   A 1 14  ? 3.387   2.063   28.182  1.00 36.89 ? 107 TYR   A CB  1 
ATOM   88   C  CG  . TYR   A 1 14  ? 4.605   2.403   29.002  1.00 37.82 ? 107 TYR   A CG  1 
ATOM   89   C  CD1 . TYR   A 1 14  ? 4.636   3.531   29.810  1.00 38.50 ? 107 TYR   A CD1 1 
ATOM   90   C  CD2 . TYR   A 1 14  ? 5.717   1.580   28.988  1.00 37.43 ? 107 TYR   A CD2 1 
ATOM   91   C  CE1 . TYR   A 1 14  ? 5.748   3.842   30.572  1.00 39.66 ? 107 TYR   A CE1 1 
ATOM   92   C  CE2 . TYR   A 1 14  ? 6.842   1.876   29.741  1.00 37.89 ? 107 TYR   A CE2 1 
ATOM   93   C  CZ  . TYR   A 1 14  ? 6.861   3.016   30.525  1.00 38.86 ? 107 TYR   A CZ  1 
ATOM   94   O  OH  . TYR   A 1 14  ? 7.959   3.301   31.264  1.00 39.92 ? 107 TYR   A OH  1 
ATOM   95   N  N   . GLY   A 1 15  ? 0.361   0.040   28.288  1.00 38.34 ? 108 GLY   A N   1 
ATOM   96   C  CA  . GLY   A 1 15  ? -0.894  -0.281  27.574  1.00 38.23 ? 108 GLY   A CA  1 
ATOM   97   C  C   . GLY   A 1 15  ? -0.745  -0.061  26.077  1.00 36.95 ? 108 GLY   A C   1 
ATOM   98   O  O   . GLY   A 1 15  ? -1.539  0.714   25.497  1.00 36.36 ? 108 GLY   A O   1 
ATOM   99   N  N   . PHE   A 1 16  ? 0.244   -0.729  25.473  1.00 37.10 ? 109 PHE   A N   1 
ATOM   100  C  CA  . PHE   A 1 16  ? 0.704   -0.510  24.078  1.00 35.69 ? 109 PHE   A CA  1 
ATOM   101  C  C   . PHE   A 1 16  ? -0.175  -1.308  23.108  1.00 35.06 ? 109 PHE   A C   1 
ATOM   102  O  O   . PHE   A 1 16  ? -0.252  -2.550  23.224  1.00 34.31 ? 109 PHE   A O   1 
ATOM   103  C  CB  . PHE   A 1 16  ? 2.187   -0.862  23.961  1.00 35.37 ? 109 PHE   A CB  1 
ATOM   104  C  CG  . PHE   A 1 16  ? 2.727   -0.912  22.557  1.00 34.14 ? 109 PHE   A CG  1 
ATOM   105  C  CD1 . PHE   A 1 16  ? 2.861   0.245   21.805  1.00 33.30 ? 109 PHE   A CD1 1 
ATOM   106  C  CD2 . PHE   A 1 16  ? 3.128   -2.116  21.997  1.00 33.04 ? 109 PHE   A CD2 1 
ATOM   107  C  CE1 . PHE   A 1 16  ? 3.369   0.195   20.516  1.00 32.59 ? 109 PHE   A CE1 1 
ATOM   108  C  CE2 . PHE   A 1 16  ? 3.636   -2.164  20.709  1.00 32.47 ? 109 PHE   A CE2 1 
ATOM   109  C  CZ  . PHE   A 1 16  ? 3.757   -1.008  19.968  1.00 32.05 ? 109 PHE   A CZ  1 
ATOM   110  N  N   A ARG   A 1 17  ? -0.845  -0.598  22.193  0.60 34.51 ? 110 ARG   A N   1 
ATOM   111  N  N   B ARG   A 1 17  ? -0.838  -0.596  22.191  0.40 34.47 ? 110 ARG   A N   1 
ATOM   112  C  CA  A ARG   A 1 17  ? -1.664  -1.184  21.093  0.60 34.39 ? 110 ARG   A CA  1 
ATOM   113  C  CA  B ARG   A 1 17  ? -1.673  -1.162  21.099  0.40 34.20 ? 110 ARG   A CA  1 
ATOM   114  C  C   A ARG   A 1 17  ? -1.346  -0.452  19.786  0.60 32.78 ? 110 ARG   A C   1 
ATOM   115  C  C   B ARG   A 1 17  ? -1.339  -0.453  19.785  0.40 32.73 ? 110 ARG   A C   1 
ATOM   116  O  O   A ARG   A 1 17  ? -0.855  0.691   19.844  0.60 32.93 ? 110 ARG   A O   1 
ATOM   117  O  O   B ARG   A 1 17  ? -0.846  0.693   19.841  0.40 32.90 ? 110 ARG   A O   1 
ATOM   118  C  CB  A ARG   A 1 17  ? -3.170  -1.145  21.381  0.60 35.58 ? 110 ARG   A CB  1 
ATOM   119  C  CB  B ARG   A 1 17  ? -3.155  -0.924  21.379  0.40 35.29 ? 110 ARG   A CB  1 
ATOM   120  C  CG  A ARG   A 1 17  ? -3.711  0.193   21.854  0.60 36.85 ? 110 ARG   A CG  1 
ATOM   121  C  CG  B ARG   A 1 17  ? -3.710  -1.679  22.572  0.40 36.83 ? 110 ARG   A CG  1 
ATOM   122  C  CD  A ARG   A 1 17  ? -4.832  0.073   22.842  0.60 38.72 ? 110 ARG   A CD  1 
ATOM   123  C  CD  B ARG   A 1 17  ? -4.713  -0.821  23.314  0.40 38.54 ? 110 ARG   A CD  1 
ATOM   124  N  NE  A ARG   A 1 17  ? -5.491  1.361   22.999  0.60 40.39 ? 110 ARG   A NE  1 
ATOM   125  N  NE  B ARG   A 1 17  ? -4.044  0.335   23.906  0.40 39.15 ? 110 ARG   A NE  1 
ATOM   126  C  CZ  A ARG   A 1 17  ? -5.149  2.312   23.872  0.60 41.47 ? 110 ARG   A CZ  1 
ATOM   127  C  CZ  B ARG   A 1 17  ? -4.544  1.568   23.987  0.40 40.17 ? 110 ARG   A CZ  1 
ATOM   128  N  NH1 A ARG   A 1 17  ? -5.839  3.440   23.901  0.60 42.16 ? 110 ARG   A NH1 1 
ATOM   129  N  NH1 B ARG   A 1 17  ? -3.839  2.528   24.563  0.40 40.64 ? 110 ARG   A NH1 1 
ATOM   130  N  NH2 A ARG   A 1 17  ? -4.109  2.158   24.680  0.60 42.08 ? 110 ARG   A NH2 1 
ATOM   131  N  NH2 B ARG   A 1 17  ? -5.742  1.845   23.501  0.40 40.70 ? 110 ARG   A NH2 1 
ATOM   132  N  N   . LEU   A 1 18  ? -1.646  -1.097  18.653  1.00 31.78 ? 111 LEU   A N   1 
ATOM   133  C  CA  . LEU   A 1 18  ? -1.513  -0.496  17.304  1.00 30.14 ? 111 LEU   A CA  1 
ATOM   134  C  C   . LEU   A 1 18  ? -2.893  -0.007  16.884  1.00 29.77 ? 111 LEU   A C   1 
ATOM   135  O  O   . LEU   A 1 18  ? -3.882  -0.605  17.309  1.00 30.50 ? 111 LEU   A O   1 
ATOM   136  C  CB  . LEU   A 1 18  ? -0.972  -1.529  16.314  1.00 29.46 ? 111 LEU   A CB  1 
ATOM   137  C  CG  . LEU   A 1 18  ? 0.402   -2.107  16.633  1.00 28.95 ? 111 LEU   A CG  1 
ATOM   138  C  CD1 . LEU   A 1 18  ? 0.826   -3.073  15.554  1.00 28.23 ? 111 LEU   A CD1 1 
ATOM   139  C  CD2 . LEU   A 1 18  ? 1.433   -1.001  16.798  1.00 28.81 ? 111 LEU   A CD2 1 
ATOM   140  N  N   . GLY   A 1 19  ? -2.926  1.084   16.128  1.00 29.28 ? 112 GLY   A N   1 
ATOM   141  C  CA  . GLY   A 1 19  ? -4.121  1.553   15.427  1.00 29.27 ? 112 GLY   A CA  1 
ATOM   142  C  C   . GLY   A 1 19  ? -3.793  1.772   13.974  1.00 28.96 ? 112 GLY   A C   1 
ATOM   143  O  O   . GLY   A 1 19  ? -2.611  1.912   13.634  1.00 27.59 ? 112 GLY   A O   1 
ATOM   144  N  N   . PHE   A 1 20  ? -4.822  1.778   13.142  1.00 29.32 ? 113 PHE   A N   1 
ATOM   145  C  CA  . PHE   A 1 20  ? -4.706  2.023   11.690  1.00 29.11 ? 113 PHE   A CA  1 
ATOM   146  C  C   . PHE   A 1 20  ? -5.816  2.983   11.293  1.00 29.39 ? 113 PHE   A C   1 
ATOM   147  O  O   . PHE   A 1 20  ? -6.903  2.958   11.934  1.00 29.55 ? 113 PHE   A O   1 
ATOM   148  C  CB  . PHE   A 1 20  ? -4.759  0.699   10.947  1.00 29.39 ? 113 PHE   A CB  1 
ATOM   149  C  CG  . PHE   A 1 20  ? -3.766  -0.324  11.444  1.00 29.39 ? 113 PHE   A CG  1 
ATOM   150  C  CD1 . PHE   A 1 20  ? -4.081  -1.165  12.506  1.00 29.56 ? 113 PHE   A CD1 1 
ATOM   151  C  CD2 . PHE   A 1 20  ? -2.518  -0.431  10.855  1.00 29.35 ? 113 PHE   A CD2 1 
ATOM   152  C  CE1 . PHE   A 1 20  ? -3.162  -2.088  12.969  1.00 29.66 ? 113 PHE   A CE1 1 
ATOM   153  C  CE2 . PHE   A 1 20  ? -1.596  -1.361  11.316  1.00 28.98 ? 113 PHE   A CE2 1 
ATOM   154  C  CZ  . PHE   A 1 20  ? -1.928  -2.190  12.367  1.00 29.64 ? 113 PHE   A CZ  1 
ATOM   155  N  N   . LEU   A 1 21  ? -5.534  3.822   10.291  1.00 29.82 ? 114 LEU   A N   1 
ATOM   156  C  CA  . LEU   A 1 21  ? -6.540  4.710   9.683   1.00 30.95 ? 114 LEU   A CA  1 
ATOM   157  C  C   . LEU   A 1 21  ? -7.693  3.848   9.137   1.00 30.66 ? 114 LEU   A C   1 
ATOM   158  O  O   . LEU   A 1 21  ? -7.423  2.704   8.657   1.00 29.44 ? 114 LEU   A O   1 
ATOM   159  C  CB  . LEU   A 1 21  ? -5.847  5.517   8.580   1.00 32.45 ? 114 LEU   A CB  1 
ATOM   160  C  CG  . LEU   A 1 21  ? -4.903  6.619   9.051   1.00 33.36 ? 114 LEU   A CG  1 
ATOM   161  C  CD1 . LEU   A 1 21  ? -4.202  7.266   7.868   1.00 33.93 ? 114 LEU   A CD1 1 
ATOM   162  C  CD2 . LEU   A 1 21  ? -5.651  7.675   9.844   1.00 35.09 ? 114 LEU   A CD2 1 
ATOM   163  N  N   . HIS   A 1 22  ? -8.920  4.342   9.247   1.00 30.22 ? 115 HIS   A N   1 
ATOM   164  C  CA  . HIS   A 1 22  ? -10.136 3.726   8.644   1.00 30.57 ? 115 HIS   A CA  1 
ATOM   165  C  C   . HIS   A 1 22  ? -10.259 4.287   7.224   1.00 30.12 ? 115 HIS   A C   1 
ATOM   166  O  O   . HIS   A 1 22  ? -11.068 5.182   7.000   1.00 31.29 ? 115 HIS   A O   1 
ATOM   167  C  CB  . HIS   A 1 22  ? -11.359 3.983   9.535   1.00 31.83 ? 115 HIS   A CB  1 
ATOM   168  C  CG  . HIS   A 1 22  ? -11.066 3.760   10.981  1.00 32.00 ? 115 HIS   A CG  1 
ATOM   169  N  ND1 . HIS   A 1 22  ? -10.653 2.529   11.467  1.00 31.47 ? 115 HIS   A ND1 1 
ATOM   170  C  CD2 . HIS   A 1 22  ? -11.076 4.610   12.029  1.00 32.28 ? 115 HIS   A CD2 1 
ATOM   171  C  CE1 . HIS   A 1 22  ? -10.426 2.637   12.763  1.00 32.17 ? 115 HIS   A CE1 1 
ATOM   172  N  NE2 . HIS   A 1 22  ? -10.688 3.907   13.137  1.00 31.82 ? 115 HIS   A NE2 1 
ATOM   173  N  N   A SER   A 1 23  ? -9.448  3.768   6.304   0.60 29.18 ? 116 SER   A N   1 
ATOM   174  N  N   B SER   A 1 23  ? -9.445  3.772   6.304   0.40 29.51 ? 116 SER   A N   1 
ATOM   175  C  CA  A SER   A 1 23  ? -9.195  4.355   4.961   0.60 29.48 ? 116 SER   A CA  1 
ATOM   176  C  CA  B SER   A 1 23  ? -9.192  4.353   4.960   0.40 29.90 ? 116 SER   A CA  1 
ATOM   177  C  C   A SER   A 1 23  ? -10.209 3.840   3.926   0.60 30.15 ? 116 SER   A C   1 
ATOM   178  C  C   B SER   A 1 23  ? -10.208 3.838   3.928   0.40 30.43 ? 116 SER   A C   1 
ATOM   179  O  O   A SER   A 1 23  ? -10.374 4.511   2.898   0.60 30.78 ? 116 SER   A O   1 
ATOM   180  O  O   B SER   A 1 23  ? -10.384 4.515   2.912   0.40 31.10 ? 116 SER   A O   1 
ATOM   181  C  CB  A SER   A 1 23  ? -7.787  4.076   4.513   0.60 28.72 ? 116 SER   A CB  1 
ATOM   182  C  CB  B SER   A 1 23  ? -7.788  4.043   4.547   0.40 29.30 ? 116 SER   A CB  1 
ATOM   183  O  OG  A SER   A 1 23  ? -6.839  4.570   5.448   0.60 27.77 ? 116 SER   A OG  1 
ATOM   184  O  OG  B SER   A 1 23  ? -7.479  2.700   4.885   0.40 28.63 ? 116 SER   A OG  1 
ATOM   185  N  N   . GLY   A 1 24  ? -10.837 2.684   4.176   1.00 30.02 ? 117 GLY   A N   1 
ATOM   186  C  CA  . GLY   A 1 24  ? -11.753 2.038   3.219   1.00 31.62 ? 117 GLY   A CA  1 
ATOM   187  C  C   . GLY   A 1 24  ? -11.014 1.387   2.057   1.00 31.37 ? 117 GLY   A C   1 
ATOM   188  O  O   . GLY   A 1 24  ? -9.763  1.314   2.104   1.00 31.00 ? 117 GLY   A O   1 
ATOM   189  N  N   . THR   A 1 25  ? -11.749 0.953   1.029   1.00 32.80 ? 118 THR   A N   1 
ATOM   190  C  CA  . THR   A 1 25  ? -11.238 0.115   -0.094  1.00 33.18 ? 118 THR   A CA  1 
ATOM   191  C  C   . THR   A 1 25  ? -11.503 0.807   -1.437  1.00 34.93 ? 118 THR   A C   1 
ATOM   192  O  O   . THR   A 1 25  ? -11.636 0.094   -2.435  1.00 35.17 ? 118 THR   A O   1 
ATOM   193  C  CB  . THR   A 1 25  ? -11.861 -1.290  -0.054  1.00 33.14 ? 118 THR   A CB  1 
ATOM   194  O  OG1 . THR   A 1 25  ? -13.274 -1.154  -0.164  1.00 34.08 ? 118 THR   A OG1 1 
ATOM   195  C  CG2 . THR   A 1 25  ? -11.537 -2.055  1.208   1.00 32.38 ? 118 THR   A CG2 1 
ATOM   196  N  N   . ALA   A 1 26  ? -11.598 2.145   -1.458  1.00 36.76 ? 119 ALA   A N   1 
ATOM   197  C  CA  . ALA   A 1 26  ? -11.832 2.940   -2.686  1.00 38.90 ? 119 ALA   A CA  1 
ATOM   198  C  C   . ALA   A 1 26  ? -10.627 2.788   -3.624  1.00 39.77 ? 119 ALA   A C   1 
ATOM   199  O  O   . ALA   A 1 26  ? -9.495  2.645   -3.121  1.00 38.45 ? 119 ALA   A O   1 
ATOM   200  C  CB  . ALA   A 1 26  ? -12.084 4.386   -2.340  1.00 39.47 ? 119 ALA   A CB  1 
ATOM   201  N  N   . LYS   A 1 27  ? -10.880 2.832   -4.935  1.00 42.88 ? 120 LYS   A N   1 
ATOM   202  C  CA  . LYS   A 1 27  ? -9.897  2.597   -6.033  1.00 44.73 ? 120 LYS   A CA  1 
ATOM   203  C  C   . LYS   A 1 27  ? -8.561  3.291   -5.731  1.00 44.72 ? 120 LYS   A C   1 
ATOM   204  O  O   . LYS   A 1 27  ? -7.514  2.679   -5.989  1.00 44.17 ? 120 LYS   A O   1 
ATOM   205  C  CB  . LYS   A 1 27  ? -10.459 3.089   -7.375  1.00 47.51 ? 120 LYS   A CB  1 
ATOM   206  C  CG  . LYS   A 1 27  ? -11.590 2.262   -7.969  1.00 49.15 ? 120 LYS   A CG  1 
ATOM   207  C  CD  . LYS   A 1 27  ? -11.967 2.648   -9.389  1.00 51.13 ? 120 LYS   A CD  1 
ATOM   208  C  CE  . LYS   A 1 27  ? -12.242 4.130   -9.544  1.00 52.26 ? 120 LYS   A CE  1 
ATOM   209  N  NZ  . LYS   A 1 27  ? -12.679 4.475   -10.913 1.00 54.39 ? 120 LYS   A NZ  1 
ATOM   210  N  N   . SER   A 1 28  ? -8.600  4.508   -5.179  1.00 45.66 ? 121 SER   A N   1 
ATOM   211  C  CA  . SER   A 1 28  ? -7.437  5.424   -5.026  1.00 45.92 ? 121 SER   A CA  1 
ATOM   212  C  C   . SER   A 1 28  ? -6.516  5.041   -3.852  1.00 44.19 ? 121 SER   A C   1 
ATOM   213  O  O   . SER   A 1 28  ? -5.367  5.533   -3.826  1.00 44.22 ? 121 SER   A O   1 
ATOM   214  C  CB  . SER   A 1 28  ? -7.938  6.834   -4.846  1.00 47.70 ? 121 SER   A CB  1 
ATOM   215  O  OG  . SER   A 1 28  ? -8.711  6.938   -3.652  1.00 48.38 ? 121 SER   A OG  1 
ATOM   216  N  N   A VAL   A 1 29  ? -6.997  4.213   -2.913  0.60 42.30 ? 122 VAL   A N   1 
ATOM   217  N  N   B VAL   A 1 29  ? -6.995  4.212   -2.919  0.40 42.20 ? 122 VAL   A N   1 
ATOM   218  C  CA  A VAL   A 1 29  ? -6.359  4.012   -1.579  0.60 40.50 ? 122 VAL   A CA  1 
ATOM   219  C  CA  B VAL   A 1 29  ? -6.359  4.020   -1.583  0.40 40.28 ? 122 VAL   A CA  1 
ATOM   220  C  C   A VAL   A 1 29  ? -5.030  3.271   -1.771  0.60 39.53 ? 122 VAL   A C   1 
ATOM   221  C  C   B VAL   A 1 29  ? -5.033  3.273   -1.768  0.40 39.38 ? 122 VAL   A C   1 
ATOM   222  O  O   A VAL   A 1 29  ? -5.019  2.219   -2.457  0.60 39.46 ? 122 VAL   A O   1 
ATOM   223  O  O   B VAL   A 1 29  ? -5.027  2.220   -2.451  0.40 39.41 ? 122 VAL   A O   1 
ATOM   224  C  CB  A VAL   A 1 29  ? -7.295  3.274   -0.597  0.60 39.90 ? 122 VAL   A CB  1 
ATOM   225  C  CB  B VAL   A 1 29  ? -7.288  3.279   -0.601  0.40 39.45 ? 122 VAL   A CB  1 
ATOM   226  C  CG1 A VAL   A 1 29  ? -6.615  2.967   0.731   0.60 38.56 ? 122 VAL   A CG1 1 
ATOM   227  C  CG1 B VAL   A 1 29  ? -6.763  1.889   -0.298  0.40 38.41 ? 122 VAL   A CG1 1 
ATOM   228  C  CG2 A VAL   A 1 29  ? -8.577  4.055   -0.347  0.60 40.97 ? 122 VAL   A CG2 1 
ATOM   229  C  CG2 B VAL   A 1 29  ? -7.474  4.065   0.687   0.40 38.96 ? 122 VAL   A CG2 1 
ATOM   230  N  N   . THR   A 1 30  ? -3.959  3.806   -1.181  1.00 38.41 ? 123 THR   A N   1 
ATOM   231  C  CA  . THR   A 1 30  ? -2.572  3.291   -1.311  1.00 37.57 ? 123 THR   A CA  1 
ATOM   232  C  C   . THR   A 1 30  ? -2.251  2.325   -0.167  1.00 34.60 ? 123 THR   A C   1 
ATOM   233  O  O   . THR   A 1 30  ? -1.346  1.514   -0.339  1.00 35.37 ? 123 THR   A O   1 
ATOM   234  C  CB  . THR   A 1 30  ? -1.576  4.451   -1.422  1.00 38.96 ? 123 THR   A CB  1 
ATOM   235  O  OG1 . THR   A 1 30  ? -1.636  5.221   -0.221  1.00 40.40 ? 123 THR   A OG1 1 
ATOM   236  C  CG2 . THR   A 1 30  ? -1.853  5.339   -2.614  1.00 40.57 ? 123 THR   A CG2 1 
ATOM   237  N  N   A CYS   A 1 31  ? -2.973  2.418   0.954   0.70 32.84 ? 124 CYS   A N   1 
ATOM   238  N  N   B CYS   A 1 31  ? -2.977  2.415   0.950   0.30 33.47 ? 124 CYS   A N   1 
ATOM   239  C  CA  A CYS   A 1 31  ? -2.807  1.537   2.137   0.70 31.31 ? 124 CYS   A CA  1 
ATOM   240  C  CA  B CYS   A 1 31  ? -2.804  1.530   2.128   0.30 31.93 ? 124 CYS   A CA  1 
ATOM   241  C  C   A CYS   A 1 31  ? -4.145  1.445   2.885   0.70 31.07 ? 124 CYS   A C   1 
ATOM   242  C  C   B CYS   A 1 31  ? -4.126  1.441   2.901   0.30 31.36 ? 124 CYS   A C   1 
ATOM   243  O  O   A CYS   A 1 31  ? -4.789  2.497   3.118   0.70 30.74 ? 124 CYS   A O   1 
ATOM   244  O  O   B CYS   A 1 31  ? -4.739  2.491   3.168   0.30 31.46 ? 124 CYS   A O   1 
ATOM   245  C  CB  A CYS   A 1 31  ? -1.662  2.047   3.006   0.70 30.94 ? 124 CYS   A CB  1 
ATOM   246  C  CB  B CYS   A 1 31  ? -1.663  2.022   3.007   0.30 31.61 ? 124 CYS   A CB  1 
ATOM   247  S  SG  A CYS   A 1 31  ? -1.619  1.430   4.710   0.70 30.08 ? 124 CYS   A SG  1 
ATOM   248  S  SG  B CYS   A 1 31  ? -2.028  3.593   3.826   0.30 32.23 ? 124 CYS   A SG  1 
ATOM   249  N  N   . THR   A 1 32  ? -4.559  0.220   3.221   1.00 30.00 ? 125 THR   A N   1 
ATOM   250  C  CA  . THR   A 1 32  ? -5.846  -0.041  3.902   1.00 30.23 ? 125 THR   A CA  1 
ATOM   251  C  C   . THR   A 1 32  ? -5.677  -1.239  4.828   1.00 29.91 ? 125 THR   A C   1 
ATOM   252  O  O   . THR   A 1 32  ? -5.042  -2.225  4.423   1.00 31.41 ? 125 THR   A O   1 
ATOM   253  C  CB  . THR   A 1 32  ? -6.983  -0.165  2.888   1.00 30.56 ? 125 THR   A CB  1 
ATOM   254  O  OG1 . THR   A 1 32  ? -8.197  -0.213  3.640   1.00 30.61 ? 125 THR   A OG1 1 
ATOM   255  C  CG2 . THR   A 1 32  ? -6.865  -1.381  1.987   1.00 30.87 ? 125 THR   A CG2 1 
ATOM   256  N  N   . TYR   A 1 33  ? -6.218  -1.115  6.031   1.00 30.30 ? 126 TYR   A N   1 
ATOM   257  C  CA  . TYR   A 1 33  ? -6.162  -2.138  7.096   1.00 29.88 ? 126 TYR   A CA  1 
ATOM   258  C  C   . TYR   A 1 33  ? -7.525  -2.811  7.228   1.00 30.47 ? 126 TYR   A C   1 
ATOM   259  O  O   . TYR   A 1 33  ? -8.545  -2.108  7.272   1.00 30.80 ? 126 TYR   A O   1 
ATOM   260  C  CB  . TYR   A 1 33  ? -5.736  -1.503  8.414   1.00 29.20 ? 126 TYR   A CB  1 
ATOM   261  C  CG  . TYR   A 1 33  ? -5.830  -2.434  9.594   1.00 29.06 ? 126 TYR   A CG  1 
ATOM   262  C  CD1 . TYR   A 1 33  ? -4.905  -3.451  9.777   1.00 28.63 ? 126 TYR   A CD1 1 
ATOM   263  C  CD2 . TYR   A 1 33  ? -6.843  -2.290  10.527  1.00 29.47 ? 126 TYR   A CD2 1 
ATOM   264  C  CE1 . TYR   A 1 33  ? -4.988  -4.299  10.864  1.00 29.21 ? 126 TYR   A CE1 1 
ATOM   265  C  CE2 . TYR   A 1 33  ? -6.926  -3.122  11.633  1.00 30.36 ? 126 TYR   A CE2 1 
ATOM   266  C  CZ  . TYR   A 1 33  ? -5.997  -4.140  11.791  1.00 30.06 ? 126 TYR   A CZ  1 
ATOM   267  O  OH  . TYR   A 1 33  ? -6.065  -4.990  12.858  1.00 31.69 ? 126 TYR   A OH  1 
ATOM   268  N  N   . SER   A 1 34  ? -7.510  -4.149  7.288   1.00 30.69 ? 127 SER   A N   1 
ATOM   269  C  CA  . SER   A 1 34  ? -8.685  -5.001  7.568   1.00 31.24 ? 127 SER   A CA  1 
ATOM   270  C  C   . SER   A 1 34  ? -8.667  -5.403  9.041   1.00 31.12 ? 127 SER   A C   1 
ATOM   271  O  O   . SER   A 1 34  ? -7.815  -6.189  9.450   1.00 30.77 ? 127 SER   A O   1 
ATOM   272  C  CB  . SER   A 1 34  ? -8.683  -6.219  6.679   1.00 32.03 ? 127 SER   A CB  1 
ATOM   273  O  OG  . SER   A 1 34  ? -9.758  -7.091  7.025   1.00 33.34 ? 127 SER   A OG  1 
ATOM   274  N  N   . PRO   A 1 35  ? -9.600  -4.881  9.875   1.00 31.68 ? 128 PRO   A N   1 
ATOM   275  C  CA  . PRO   A 1 35  ? -9.708  -5.297  11.267  1.00 32.05 ? 128 PRO   A CA  1 
ATOM   276  C  C   . PRO   A 1 35  ? -10.124 -6.767  11.385  1.00 32.29 ? 128 PRO   A C   1 
ATOM   277  O  O   . PRO   A 1 35  ? -9.652  -7.417  12.293  1.00 32.24 ? 128 PRO   A O   1 
ATOM   278  C  CB  . PRO   A 1 35  ? -10.790 -4.401  11.902  1.00 32.82 ? 128 PRO   A CB  1 
ATOM   279  C  CG  . PRO   A 1 35  ? -11.188 -3.406  10.834  1.00 32.41 ? 128 PRO   A CG  1 
ATOM   280  C  CD  . PRO   A 1 35  ? -10.597 -3.860  9.519   1.00 31.81 ? 128 PRO   A CD  1 
ATOM   281  N  N   . ALA   A 1 36  ? -10.971 -7.254  10.471  1.00 32.42 ? 129 ALA   A N   1 
ATOM   282  C  CA  . ALA   A 1 36  ? -11.477 -8.645  10.471  1.00 33.39 ? 129 ALA   A CA  1 
ATOM   283  C  C   . ALA   A 1 36  ? -10.310 -9.621  10.290  1.00 32.65 ? 129 ALA   A C   1 
ATOM   284  O  O   . ALA   A 1 36  ? -10.342 -10.693 10.911  1.00 33.51 ? 129 ALA   A O   1 
ATOM   285  C  CB  . ALA   A 1 36  ? -12.546 -8.838  9.408   1.00 33.61 ? 129 ALA   A CB  1 
ATOM   286  N  N   . LEU   A 1 37  ? -9.323  -9.276  9.469   1.00 31.70 ? 130 LEU   A N   1 
ATOM   287  C  CA  . LEU   A 1 37  ? -8.185  -10.170 9.128   1.00 31.60 ? 130 LEU   A CA  1 
ATOM   288  C  C   . LEU   A 1 37  ? -6.915  -9.787  9.905   1.00 30.42 ? 130 LEU   A C   1 
ATOM   289  O  O   . LEU   A 1 37  ? -5.957  -10.554 9.801   1.00 29.96 ? 130 LEU   A O   1 
ATOM   290  C  CB  . LEU   A 1 37  ? -7.932  -10.079 7.620   1.00 32.05 ? 130 LEU   A CB  1 
ATOM   291  C  CG  . LEU   A 1 37  ? -9.044  -10.597 6.720   1.00 33.36 ? 130 LEU   A CG  1 
ATOM   292  C  CD1 . LEU   A 1 37  ? -8.778  -10.183 5.290   1.00 33.84 ? 130 LEU   A CD1 1 
ATOM   293  C  CD2 . LEU   A 1 37  ? -9.195  -12.115 6.817   1.00 35.05 ? 130 LEU   A CD2 1 
ATOM   294  N  N   . ASN   A 1 38  ? -6.909  -8.660  10.645  1.00 29.70 ? 131 ASN   A N   1 
ATOM   295  C  CA  . ASN   A 1 38  ? -5.702  -8.007  11.241  1.00 28.62 ? 131 ASN   A CA  1 
ATOM   296  C  C   . ASN   A 1 38  ? -4.596  -7.945  10.177  1.00 28.03 ? 131 ASN   A C   1 
ATOM   297  O  O   . ASN   A 1 38  ? -3.457  -8.420  10.423  1.00 27.15 ? 131 ASN   A O   1 
ATOM   298  C  CB  . ASN   A 1 38  ? -5.239  -8.685  12.534  1.00 29.05 ? 131 ASN   A CB  1 
ATOM   299  C  CG  . ASN   A 1 38  ? -4.113  -7.953  13.245  1.00 28.34 ? 131 ASN   A CG  1 
ATOM   300  O  OD1 . ASN   A 1 38  ? -3.998  -6.725  13.190  1.00 27.23 ? 131 ASN   A OD1 1 
ATOM   301  N  ND2 . ASN   A 1 38  ? -3.267  -8.699  13.930  1.00 28.42 ? 131 ASN   A ND2 1 
ATOM   302  N  N   . LYS   A 1 39  ? -4.926  -7.388  9.013   1.00 28.35 ? 132 LYS   A N   1 
ATOM   303  C  CA  . LYS   A 1 39  ? -4.054  -7.439  7.820   1.00 28.18 ? 132 LYS   A CA  1 
ATOM   304  C  C   . LYS   A 1 39  ? -4.031  -6.073  7.138   1.00 28.45 ? 132 LYS   A C   1 
ATOM   305  O  O   . LYS   A 1 39  ? -5.115  -5.545  6.812   1.00 29.79 ? 132 LYS   A O   1 
ATOM   306  C  CB  . LYS   A 1 39  ? -4.516  -8.539  6.867   1.00 28.66 ? 132 LYS   A CB  1 
ATOM   307  C  CG  . LYS   A 1 39  ? -3.586  -8.795  5.692   1.00 28.57 ? 132 LYS   A CG  1 
ATOM   308  C  CD  . LYS   A 1 39  ? -3.923  -10.046 4.940   1.00 29.31 ? 132 LYS   A CD  1 
ATOM   309  C  CE  . LYS   A 1 39  ? -2.950  -10.350 3.823   1.00 29.26 ? 132 LYS   A CE  1 
ATOM   310  N  NZ  . LYS   A 1 39  ? -3.053  -11.776 3.423   1.00 30.13 ? 132 LYS   A NZ  1 
ATOM   311  N  N   A MET   A 1 40  ? -2.822  -5.531  6.954   0.70 28.85 ? 133 MET   A N   1 
ATOM   312  N  N   B MET   A 1 40  ? -2.824  -5.527  6.953   0.30 27.64 ? 133 MET   A N   1 
ATOM   313  C  CA  A MET   A 1 40  ? -2.545  -4.316  6.148   0.70 29.33 ? 133 MET   A CA  1 
ATOM   314  C  CA  B MET   A 1 40  ? -2.547  -4.305  6.153   0.30 27.26 ? 133 MET   A CA  1 
ATOM   315  C  C   A MET   A 1 40  ? -2.366  -4.719  4.683   0.70 29.36 ? 133 MET   A C   1 
ATOM   316  C  C   B MET   A 1 40  ? -2.359  -4.709  4.687   0.30 28.11 ? 133 MET   A C   1 
ATOM   317  O  O   A MET   A 1 40  ? -1.560  -5.625  4.427   0.70 29.03 ? 133 MET   A O   1 
ATOM   318  O  O   B MET   A 1 40  ? -1.550  -5.619  4.433   0.30 28.12 ? 133 MET   A O   1 
ATOM   319  C  CB  A MET   A 1 40  ? -1.267  -3.625  6.634   0.70 29.56 ? 133 MET   A CB  1 
ATOM   320  C  CB  B MET   A 1 40  ? -1.284  -3.602  6.665   0.30 26.02 ? 133 MET   A CB  1 
ATOM   321  C  CG  A MET   A 1 40  ? -0.872  -2.423  5.798   0.70 30.28 ? 133 MET   A CG  1 
ATOM   322  C  CG  B MET   A 1 40  ? -0.670  -2.601  5.696   0.30 25.51 ? 133 MET   A CG  1 
ATOM   323  S  SD  A MET   A 1 40  ? -2.086  -1.105  5.905   0.70 32.30 ? 133 MET   A SD  1 
ATOM   324  S  SD  B MET   A 1 40  ? 0.705   -1.621  6.386   0.30 24.10 ? 133 MET   A SD  1 
ATOM   325  C  CE  A MET   A 1 40  ? -1.704  -0.475  7.540   0.70 31.35 ? 133 MET   A CE  1 
ATOM   326  C  CE  B MET   A 1 40  ? -0.166  -0.765  7.698   0.30 24.41 ? 133 MET   A CE  1 
ATOM   327  N  N   . PHE   A 1 41  ? -3.098  -4.075  3.773   1.00 29.04 ? 134 PHE   A N   1 
ATOM   328  C  CA  . PHE   A 1 41  ? -2.881  -4.161  2.308   1.00 29.75 ? 134 PHE   A CA  1 
ATOM   329  C  C   . PHE   A 1 41  ? -2.280  -2.829  1.868   1.00 30.26 ? 134 PHE   A C   1 
ATOM   330  O  O   . PHE   A 1 41  ? -2.927  -1.805  2.111   1.00 30.41 ? 134 PHE   A O   1 
ATOM   331  C  CB  . PHE   A 1 41  ? -4.187  -4.452  1.570   1.00 29.79 ? 134 PHE   A CB  1 
ATOM   332  C  CG  . PHE   A 1 41  ? -4.896  -5.704  2.020   1.00 30.06 ? 134 PHE   A CG  1 
ATOM   333  C  CD1 . PHE   A 1 41  ? -5.595  -5.736  3.220   1.00 29.65 ? 134 PHE   A CD1 1 
ATOM   334  C  CD2 . PHE   A 1 41  ? -4.863  -6.852  1.246   1.00 30.49 ? 134 PHE   A CD2 1 
ATOM   335  C  CE1 . PHE   A 1 41  ? -6.241  -6.892  3.638   1.00 30.19 ? 134 PHE   A CE1 1 
ATOM   336  C  CE2 . PHE   A 1 41  ? -5.519  -8.001  1.662   1.00 31.16 ? 134 PHE   A CE2 1 
ATOM   337  C  CZ  . PHE   A 1 41  ? -6.206  -8.020  2.856   1.00 30.76 ? 134 PHE   A CZ  1 
ATOM   338  N  N   . CYS   A 1 42  ? -1.092  -2.835  1.260   1.00 30.57 ? 135 CYS   A N   1 
ATOM   339  C  CA  . CYS   A 1 42  ? -0.393  -1.582  0.873   1.00 31.12 ? 135 CYS   A CA  1 
ATOM   340  C  C   . CYS   A 1 42  ? 0.331   -1.768  -0.467  1.00 31.11 ? 135 CYS   A C   1 
ATOM   341  O  O   . CYS   A 1 42  ? 0.591   -2.906  -0.865  1.00 30.95 ? 135 CYS   A O   1 
ATOM   342  C  CB  . CYS   A 1 42  ? 0.551   -1.131  1.982   1.00 31.45 ? 135 CYS   A CB  1 
ATOM   343  S  SG  . CYS   A 1 42  ? 1.850   -2.331  2.360   1.00 33.44 ? 135 CYS   A SG  1 
ATOM   344  N  N   . GLN   A 1 43  ? 0.606   -0.667  -1.152  1.00 31.70 ? 136 GLN   A N   1 
ATOM   345  C  CA  . GLN   A 1 43  ? 1.386   -0.643  -2.411  1.00 32.33 ? 136 GLN   A CA  1 
ATOM   346  C  C   . GLN   A 1 43  ? 2.870   -0.492  -2.085  1.00 32.26 ? 136 GLN   A C   1 
ATOM   347  O  O   . GLN   A 1 43  ? 3.187   0.127   -1.056  1.00 32.28 ? 136 GLN   A O   1 
ATOM   348  C  CB  . GLN   A 1 43  ? 0.960   0.533   -3.282  1.00 33.31 ? 136 GLN   A CB  1 
ATOM   349  C  CG  . GLN   A 1 43  ? -0.413  0.388   -3.888  1.00 33.97 ? 136 GLN   A CG  1 
ATOM   350  C  CD  . GLN   A 1 43  ? -0.807  1.692   -4.531  1.00 34.65 ? 136 GLN   A CD  1 
ATOM   351  O  OE1 . GLN   A 1 43  ? -1.805  2.292   -4.160  1.00 36.32 ? 136 GLN   A OE1 1 
ATOM   352  N  NE2 . GLN   A 1 43  ? 0.017   2.191   -5.434  1.00 35.15 ? 136 GLN   A NE2 1 
ATOM   353  N  N   . LEU   A 1 44  ? 3.710   -1.001  -2.987  1.00 32.70 ? 137 LEU   A N   1 
ATOM   354  C  CA  . LEU   A 1 44  ? 5.191   -0.898  -2.977  1.00 33.08 ? 137 LEU   A CA  1 
ATOM   355  C  C   . LEU   A 1 44  ? 5.626   0.560   -2.784  1.00 32.76 ? 137 LEU   A C   1 
ATOM   356  O  O   . LEU   A 1 44  ? 5.132   1.428   -3.530  1.00 32.65 ? 137 LEU   A O   1 
ATOM   357  C  CB  . LEU   A 1 44  ? 5.685   -1.414  -4.329  1.00 34.88 ? 137 LEU   A CB  1 
ATOM   358  C  CG  . LEU   A 1 44  ? 7.159   -1.776  -4.385  1.00 35.38 ? 137 LEU   A CG  1 
ATOM   359  C  CD1 . LEU   A 1 44  ? 7.404   -2.965  -3.505  1.00 35.33 ? 137 LEU   A CD1 1 
ATOM   360  C  CD2 . LEU   A 1 44  ? 7.544   -2.112  -5.814  1.00 37.02 ? 137 LEU   A CD2 1 
ATOM   361  N  N   . ALA   A 1 45  ? 6.498   0.814   -1.800  1.00 32.81 ? 138 ALA   A N   1 
ATOM   362  C  CA  . ALA   A 1 45  ? 7.194   2.102   -1.567  1.00 33.54 ? 138 ALA   A CA  1 
ATOM   363  C  C   . ALA   A 1 45  ? 6.233   3.211   -1.116  1.00 34.22 ? 138 ALA   A C   1 
ATOM   364  O  O   . ALA   A 1 45  ? 6.734   4.333   -0.866  1.00 36.16 ? 138 ALA   A O   1 
ATOM   365  C  CB  . ALA   A 1 45  ? 7.942   2.519   -2.811  1.00 34.81 ? 138 ALA   A CB  1 
ATOM   366  N  N   . LYS   A 1 46  ? 4.932   2.933   -0.990  1.00 33.61 ? 139 LYS   A N   1 
ATOM   367  C  CA  . LYS   A 1 46  ? 3.927   3.951   -0.591  1.00 34.10 ? 139 LYS   A CA  1 
ATOM   368  C  C   . LYS   A 1 46  ? 3.827   4.031   0.938   1.00 31.85 ? 139 LYS   A C   1 
ATOM   369  O  O   . LYS   A 1 46  ? 4.140   3.056   1.643   1.00 29.08 ? 139 LYS   A O   1 
ATOM   370  C  CB  . LYS   A 1 46  ? 2.565   3.674   -1.238  1.00 35.62 ? 139 LYS   A CB  1 
ATOM   371  C  CG  . LYS   A 1 46  ? 2.465   3.988   -2.728  1.00 37.63 ? 139 LYS   A CG  1 
ATOM   372  C  CD  . LYS   A 1 46  ? 2.900   5.417   -3.105  1.00 39.47 ? 139 LYS   A CD  1 
ATOM   373  C  CE  . LYS   A 1 46  ? 2.289   5.949   -4.387  1.00 41.36 ? 139 LYS   A CE  1 
ATOM   374  N  NZ  . LYS   A 1 46  ? 2.519   5.041   -5.537  1.00 42.82 ? 139 LYS   A NZ  1 
ATOM   375  N  N   . THR   A 1 47  ? 3.397   5.192   1.418   1.00 31.72 ? 140 THR   A N   1 
ATOM   376  C  CA  . THR   A 1 47  ? 3.257   5.543   2.851   1.00 31.20 ? 140 THR   A CA  1 
ATOM   377  C  C   . THR   A 1 47  ? 2.250   4.626   3.541   1.00 30.83 ? 140 THR   A C   1 
ATOM   378  O  O   . THR   A 1 47  ? 1.080   4.569   3.105   1.00 31.09 ? 140 THR   A O   1 
ATOM   379  C  CB  . THR   A 1 47  ? 2.806   6.996   3.012   1.00 31.53 ? 140 THR   A CB  1 
ATOM   380  O  OG1 . THR   A 1 47  ? 3.731   7.766   2.244   1.00 31.89 ? 140 THR   A OG1 1 
ATOM   381  C  CG2 . THR   A 1 47  ? 2.762   7.430   4.456   1.00 30.89 ? 140 THR   A CG2 1 
ATOM   382  N  N   A CYS   A 1 48  ? 2.696   3.942   4.591   0.70 31.16 ? 141 CYS   A N   1 
ATOM   383  N  N   B CYS   A 1 48  ? 2.693   3.931   4.589   0.30 30.06 ? 141 CYS   A N   1 
ATOM   384  C  CA  A CYS   A 1 48  ? 1.877   3.010   5.407   0.70 31.72 ? 141 CYS   A CA  1 
ATOM   385  C  CA  B CYS   A 1 48  ? 1.866   3.011   5.413   0.30 29.68 ? 141 CYS   A CA  1 
ATOM   386  C  C   A CYS   A 1 48  ? 1.826   3.508   6.846   0.70 30.93 ? 141 CYS   A C   1 
ATOM   387  C  C   B CYS   A 1 48  ? 1.825   3.512   6.849   0.30 29.84 ? 141 CYS   A C   1 
ATOM   388  O  O   A CYS   A 1 48  ? 2.699   3.169   7.642   0.70 30.97 ? 141 CYS   A O   1 
ATOM   389  O  O   B CYS   A 1 48  ? 2.699   3.173   7.644   0.30 29.82 ? 141 CYS   A O   1 
ATOM   390  C  CB  A CYS   A 1 48  ? 2.448   1.599   5.326   0.70 32.86 ? 141 CYS   A CB  1 
ATOM   391  C  CB  B CYS   A 1 48  ? 2.427   1.598   5.409   0.30 29.14 ? 141 CYS   A CB  1 
ATOM   392  S  SG  A CYS   A 1 48  ? 1.415   0.369   6.143   0.70 35.99 ? 141 CYS   A SG  1 
ATOM   393  S  SG  B CYS   A 1 48  ? 2.381   0.839   3.776   0.30 29.02 ? 141 CYS   A SG  1 
ATOM   394  N  N   . PRO   A 1 49  ? 0.822   4.336   7.222   1.00 30.60 ? 142 PRO   A N   1 
ATOM   395  C  CA  . PRO   A 1 49  ? 0.705   4.820   8.592   1.00 30.53 ? 142 PRO   A CA  1 
ATOM   396  C  C   . PRO   A 1 49  ? 0.389   3.674   9.560   1.00 30.32 ? 142 PRO   A C   1 
ATOM   397  O  O   . PRO   A 1 49  ? -0.512  2.911   9.327   1.00 30.56 ? 142 PRO   A O   1 
ATOM   398  C  CB  . PRO   A 1 49  ? -0.438  5.838   8.516   1.00 31.24 ? 142 PRO   A CB  1 
ATOM   399  C  CG  . PRO   A 1 49  ? -0.563  6.170   7.049   1.00 31.81 ? 142 PRO   A CG  1 
ATOM   400  C  CD  . PRO   A 1 49  ? -0.242  4.861   6.354   1.00 31.26 ? 142 PRO   A CD  1 
ATOM   401  N  N   . VAL   A 1 50  ? 1.187   3.561   10.615  1.00 29.31 ? 143 VAL   A N   1 
ATOM   402  C  CA  . VAL   A 1 50  ? 0.900   2.686   11.782  1.00 29.73 ? 143 VAL   A CA  1 
ATOM   403  C  C   . VAL   A 1 50  ? 0.849   3.598   13.001  1.00 30.38 ? 143 VAL   A C   1 
ATOM   404  O  O   . VAL   A 1 50  ? 1.814   4.342   13.219  1.00 32.15 ? 143 VAL   A O   1 
ATOM   405  C  CB  . VAL   A 1 50  ? 1.940   1.554   11.899  1.00 28.93 ? 143 VAL   A CB  1 
ATOM   406  C  CG1 . VAL   A 1 50  ? 1.750   0.746   13.165  1.00 29.72 ? 143 VAL   A CG1 1 
ATOM   407  C  CG2 . VAL   A 1 50  ? 1.913   0.657   10.668  1.00 28.47 ? 143 VAL   A CG2 1 
ATOM   408  N  N   . GLN   A 1 51  ? -0.267  3.572   13.721  1.00 31.15 ? 144 GLN   A N   1 
ATOM   409  C  CA  . GLN   A 1 51  ? -0.470  4.357   14.959  1.00 31.37 ? 144 GLN   A CA  1 
ATOM   410  C  C   . GLN   A 1 51  ? 0.002   3.538   16.162  1.00 31.64 ? 144 GLN   A C   1 
ATOM   411  O  O   . GLN   A 1 51  ? -0.323  2.323   16.234  1.00 31.37 ? 144 GLN   A O   1 
ATOM   412  C  CB  . GLN   A 1 51  ? -1.933  4.745   15.094  1.00 32.10 ? 144 GLN   A CB  1 
ATOM   413  C  CG  . GLN   A 1 51  ? -2.455  5.529   13.898  1.00 32.44 ? 144 GLN   A CG  1 
ATOM   414  C  CD  . GLN   A 1 51  ? -3.954  5.682   13.980  1.00 33.91 ? 144 GLN   A CD  1 
ATOM   415  O  OE1 . GLN   A 1 51  ? -4.632  4.986   14.732  1.00 35.16 ? 144 GLN   A OE1 1 
ATOM   416  N  NE2 . GLN   A 1 51  ? -4.496  6.598   13.207  1.00 34.86 ? 144 GLN   A NE2 1 
ATOM   417  N  N   . LEU   A 1 52  ? 0.753   4.183   17.054  1.00 31.57 ? 145 LEU   A N   1 
ATOM   418  C  CA  . LEU   A 1 52  ? 1.104   3.666   18.396  1.00 31.98 ? 145 LEU   A CA  1 
ATOM   419  C  C   . LEU   A 1 52  ? 0.161   4.304   19.415  1.00 34.04 ? 145 LEU   A C   1 
ATOM   420  O  O   . LEU   A 1 52  ? 0.105   5.571   19.491  1.00 34.52 ? 145 LEU   A O   1 
ATOM   421  C  CB  . LEU   A 1 52  ? 2.566   3.998   18.715  1.00 31.58 ? 145 LEU   A CB  1 
ATOM   422  C  CG  . LEU   A 1 52  ? 3.578   3.734   17.599  1.00 30.44 ? 145 LEU   A CG  1 
ATOM   423  C  CD1 . LEU   A 1 52  ? 4.976   4.091   18.082  1.00 30.99 ? 145 LEU   A CD1 1 
ATOM   424  C  CD2 . LEU   A 1 52  ? 3.513   2.289   17.117  1.00 29.59 ? 145 LEU   A CD2 1 
ATOM   425  N  N   . TRP   A 1 53  ? -0.586  3.474   20.148  1.00 34.45 ? 146 TRP   A N   1 
ATOM   426  C  CA  . TRP   A 1 53  ? -1.477  3.930   21.243  1.00 35.71 ? 146 TRP   A CA  1 
ATOM   427  C  C   . TRP   A 1 53  ? -0.915  3.419   22.566  1.00 36.44 ? 146 TRP   A C   1 
ATOM   428  O  O   . TRP   A 1 53  ? -0.602  2.212   22.668  1.00 35.63 ? 146 TRP   A O   1 
ATOM   429  C  CB  . TRP   A 1 53  ? -2.915  3.462   21.033  1.00 35.91 ? 146 TRP   A CB  1 
ATOM   430  C  CG  . TRP   A 1 53  ? -3.589  4.070   19.842  1.00 36.04 ? 146 TRP   A CG  1 
ATOM   431  C  CD1 . TRP   A 1 53  ? -3.302  3.806   18.538  1.00 34.73 ? 146 TRP   A CD1 1 
ATOM   432  C  CD2 . TRP   A 1 53  ? -4.670  5.019   19.836  1.00 36.86 ? 146 TRP   A CD2 1 
ATOM   433  N  NE1 . TRP   A 1 53  ? -4.125  4.526   17.722  1.00 36.18 ? 146 TRP   A NE1 1 
ATOM   434  C  CE2 . TRP   A 1 53  ? -4.979  5.277   18.482  1.00 36.65 ? 146 TRP   A CE2 1 
ATOM   435  C  CE3 . TRP   A 1 53  ? -5.393  5.693   20.825  1.00 38.01 ? 146 TRP   A CE3 1 
ATOM   436  C  CZ2 . TRP   A 1 53  ? -5.983  6.169   18.099  1.00 37.83 ? 146 TRP   A CZ2 1 
ATOM   437  C  CZ3 . TRP   A 1 53  ? -6.388  6.570   20.443  1.00 39.12 ? 146 TRP   A CZ3 1 
ATOM   438  C  CH2 . TRP   A 1 53  ? -6.671  6.810   19.101  1.00 38.52 ? 146 TRP   A CH2 1 
ATOM   439  N  N   . VAL   A 1 54  ? -0.793  4.327   23.532  1.00 38.48 ? 147 VAL   A N   1 
ATOM   440  C  CA  . VAL   A 1 54  ? -0.316  4.027   24.910  1.00 40.36 ? 147 VAL   A CA  1 
ATOM   441  C  C   . VAL   A 1 54  ? -1.310  4.630   25.905  1.00 43.03 ? 147 VAL   A C   1 
ATOM   442  O  O   . VAL   A 1 54  ? -1.910  5.695   25.599  1.00 42.44 ? 147 VAL   A O   1 
ATOM   443  C  CB  . VAL   A 1 54  ? 1.116   4.557   25.120  1.00 40.01 ? 147 VAL   A CB  1 
ATOM   444  C  CG1 . VAL   A 1 54  ? 2.131   3.714   24.367  1.00 38.52 ? 147 VAL   A CG1 1 
ATOM   445  C  CG2 . VAL   A 1 54  ? 1.250   6.029   24.743  1.00 40.36 ? 147 VAL   A CG2 1 
ATOM   446  N  N   . ASP   A 1 55  ? -1.510  3.936   27.027  1.00 45.55 ? 148 ASP   A N   1 
ATOM   447  C  CA  . ASP   A 1 55  ? -2.314  4.405   28.183  1.00 48.18 ? 148 ASP   A CA  1 
ATOM   448  C  C   . ASP   A 1 55  ? -1.485  5.419   28.972  1.00 48.76 ? 148 ASP   A C   1 
ATOM   449  O  O   . ASP   A 1 55  ? -2.073  6.334   29.568  1.00 50.08 ? 148 ASP   A O   1 
ATOM   450  C  CB  . ASP   A 1 55  ? -2.750  3.240   29.076  1.00 50.59 ? 148 ASP   A CB  1 
ATOM   451  C  CG  . ASP   A 1 55  ? -3.782  2.322   28.443  1.00 51.64 ? 148 ASP   A CG  1 
ATOM   452  O  OD1 . ASP   A 1 55  ? -4.506  2.774   27.518  1.00 53.00 ? 148 ASP   A OD1 1 
ATOM   453  O  OD2 . ASP   A 1 55  ? -3.858  1.159   28.884  1.00 54.21 ? 148 ASP   A OD2 1 
ATOM   454  N  N   A SER   A 1 56  ? -0.161  5.241   28.988  0.50 48.04 ? 149 SER   A N   1 
ATOM   455  N  N   B SER   A 1 56  ? -0.162  5.242   28.991  0.50 48.08 ? 149 SER   A N   1 
ATOM   456  C  CA  A SER   A 1 56  ? 0.806   6.127   29.686  0.50 48.99 ? 149 SER   A CA  1 
ATOM   457  C  CA  B SER   A 1 56  ? 0.800   6.137   29.683  0.50 49.04 ? 149 SER   A CA  1 
ATOM   458  C  C   A SER   A 1 56  ? 2.025   6.368   28.794  0.50 47.84 ? 149 SER   A C   1 
ATOM   459  C  C   B SER   A 1 56  ? 2.025   6.369   28.796  0.50 47.87 ? 149 SER   A C   1 
ATOM   460  O  O   A SER   A 1 56  ? 2.453   5.423   28.115  0.50 46.82 ? 149 SER   A O   1 
ATOM   461  O  O   B SER   A 1 56  ? 2.452   5.423   28.116  0.50 46.85 ? 149 SER   A O   1 
ATOM   462  C  CB  A SER   A 1 56  ? 1.204   5.543   31.007  0.50 50.14 ? 149 SER   A CB  1 
ATOM   463  C  CB  B SER   A 1 56  ? 1.182   5.584   31.026  0.50 50.26 ? 149 SER   A CB  1 
ATOM   464  O  OG  A SER   A 1 56  ? 0.063   5.073   31.714  0.50 50.76 ? 149 SER   A OG  1 
ATOM   465  O  OG  B SER   A 1 56  ? 1.627   4.244   30.908  0.50 49.16 ? 149 SER   A OG  1 
ATOM   466  N  N   . THR   A 1 57  ? 2.536   7.601   28.800  1.00 48.41 ? 150 THR   A N   1 
ATOM   467  C  CA  . THR   A 1 57  ? 3.663   8.066   27.956  1.00 48.76 ? 150 THR   A CA  1 
ATOM   468  C  C   . THR   A 1 57  ? 4.946   7.361   28.383  1.00 49.16 ? 150 THR   A C   1 
ATOM   469  O  O   . THR   A 1 57  ? 5.418   7.541   29.499  1.00 50.42 ? 150 THR   A O   1 
ATOM   470  C  CB  . THR   A 1 57  ? 3.816   9.586   28.069  1.00 49.80 ? 150 THR   A CB  1 
ATOM   471  O  OG1 . THR   A 1 57  ? 2.530   10.168  27.869  1.00 50.54 ? 150 THR   A OG1 1 
ATOM   472  C  CG2 . THR   A 1 57  ? 4.780   10.164  27.066  1.00 49.56 ? 150 THR   A CG2 1 
ATOM   473  N  N   . PRO   A 1 58  ? 5.554   6.522   27.521  1.00 48.40 ? 151 PRO   A N   1 
ATOM   474  C  CA  . PRO   A 1 58  ? 6.886   5.991   27.802  1.00 49.04 ? 151 PRO   A CA  1 
ATOM   475  C  C   . PRO   A 1 58  ? 7.927   7.095   27.950  1.00 49.95 ? 151 PRO   A C   1 
ATOM   476  O  O   . PRO   A 1 58  ? 7.748   8.194   27.437  1.00 51.29 ? 151 PRO   A O   1 
ATOM   477  C  CB  . PRO   A 1 58  ? 7.207   5.083   26.611  1.00 47.27 ? 151 PRO   A CB  1 
ATOM   478  C  CG  . PRO   A 1 58  ? 5.855   4.782   25.986  1.00 47.12 ? 151 PRO   A CG  1 
ATOM   479  C  CD  . PRO   A 1 58  ? 5.005   6.008   26.265  1.00 47.36 ? 151 PRO   A CD  1 
ATOM   480  N  N   . PRO   A 1 59  ? 9.044   6.851   28.665  1.00 50.53 ? 152 PRO   A N   1 
ATOM   481  C  CA  . PRO   A 1 59  ? 10.057  7.894   28.851  1.00 51.07 ? 152 PRO   A CA  1 
ATOM   482  C  C   . PRO   A 1 59  ? 10.770  8.245   27.544  1.00 49.86 ? 152 PRO   A C   1 
ATOM   483  O  O   . PRO   A 1 59  ? 10.799  7.449   26.615  1.00 47.60 ? 152 PRO   A O   1 
ATOM   484  C  CB  . PRO   A 1 59  ? 11.011  7.287   29.884  1.00 52.04 ? 152 PRO   A CB  1 
ATOM   485  C  CG  . PRO   A 1 59  ? 10.815  5.772   29.720  1.00 51.05 ? 152 PRO   A CG  1 
ATOM   486  C  CD  . PRO   A 1 59  ? 9.362   5.583   29.339  1.00 50.76 ? 152 PRO   A CD  1 
ATOM   487  N  N   . PRO   A 1 60  ? 11.360  9.460   27.416  1.00 50.18 ? 153 PRO   A N   1 
ATOM   488  C  CA  . PRO   A 1 60  ? 12.186  9.782   26.248  1.00 48.33 ? 153 PRO   A CA  1 
ATOM   489  C  C   . PRO   A 1 60  ? 13.317  8.748   26.106  1.00 46.15 ? 153 PRO   A C   1 
ATOM   490  O  O   . PRO   A 1 60  ? 13.834  8.304   27.119  1.00 46.76 ? 153 PRO   A O   1 
ATOM   491  C  CB  . PRO   A 1 60  ? 12.732  11.184  26.549  1.00 50.50 ? 153 PRO   A CB  1 
ATOM   492  C  CG  . PRO   A 1 60  ? 11.739  11.764  27.544  1.00 52.35 ? 153 PRO   A CG  1 
ATOM   493  C  CD  . PRO   A 1 60  ? 11.253  10.579  28.366  1.00 52.21 ? 153 PRO   A CD  1 
ATOM   494  N  N   . GLY   A 1 61  ? 13.687  8.390   24.879  1.00 42.07 ? 154 GLY   A N   1 
ATOM   495  C  CA  . GLY   A 1 61  ? 14.729  7.375   24.617  1.00 40.16 ? 154 GLY   A CA  1 
ATOM   496  C  C   . GLY   A 1 61  ? 14.122  5.988   24.446  1.00 37.72 ? 154 GLY   A C   1 
ATOM   497  O  O   . GLY   A 1 61  ? 14.837  5.091   23.993  1.00 36.40 ? 154 GLY   A O   1 
ATOM   498  N  N   . THR   A 1 62  ? 12.830  5.814   24.734  1.00 36.37 ? 155 THR   A N   1 
ATOM   499  C  CA  . THR   A 1 62  ? 12.018  4.648   24.276  1.00 34.74 ? 155 THR   A CA  1 
ATOM   500  C  C   . THR   A 1 62  ? 12.139  4.541   22.750  1.00 32.37 ? 155 THR   A C   1 
ATOM   501  O  O   . THR   A 1 62  ? 12.169  5.588   22.071  1.00 30.38 ? 155 THR   A O   1 
ATOM   502  C  CB  . THR   A 1 62  ? 10.537  4.800   24.651  1.00 35.31 ? 155 THR   A CB  1 
ATOM   503  O  OG1 . THR   A 1 62  ? 10.467  4.941   26.076  1.00 37.45 ? 155 THR   A OG1 1 
ATOM   504  C  CG2 . THR   A 1 62  ? 9.671   3.671   24.121  1.00 34.12 ? 155 THR   A CG2 1 
ATOM   505  N  N   . ARG   A 1 63  ? 12.241  3.320   22.230  1.00 31.01 ? 156 ARG   A N   1 
ATOM   506  C  CA  . ARG   A 1 63  ? 12.425  3.092   20.776  1.00 30.18 ? 156 ARG   A CA  1 
ATOM   507  C  C   . ARG   A 1 63  ? 11.335  2.159   20.242  1.00 28.90 ? 156 ARG   A C   1 
ATOM   508  O  O   . ARG   A 1 63  ? 10.763  1.384   21.030  1.00 28.79 ? 156 ARG   A O   1 
ATOM   509  C  CB  . ARG   A 1 63  ? 13.852  2.598   20.530  1.00 30.47 ? 156 ARG   A CB  1 
ATOM   510  C  CG  . ARG   A 1 63  ? 14.873  3.726   20.449  1.00 31.29 ? 156 ARG   A CG  1 
ATOM   511  C  CD  . ARG   A 1 63  ? 16.253  3.322   20.953  1.00 32.25 ? 156 ARG   A CD  1 
ATOM   512  N  NE  . ARG   A 1 63  ? 16.816  2.123   20.342  1.00 32.53 ? 156 ARG   A NE  1 
ATOM   513  C  CZ  . ARG   A 1 63  ? 17.639  2.083   19.286  1.00 33.08 ? 156 ARG   A CZ  1 
ATOM   514  N  NH1 . ARG   A 1 63  ? 17.973  3.189   18.638  1.00 32.88 ? 156 ARG   A NH1 1 
ATOM   515  N  NH2 . ARG   A 1 63  ? 18.077  0.912   18.849  1.00 32.85 ? 156 ARG   A NH2 1 
ATOM   516  N  N   . VAL   A 1 64  ? 11.043  2.298   18.946  1.00 28.81 ? 157 VAL   A N   1 
ATOM   517  C  CA  . VAL   A 1 64  ? 10.027  1.496   18.215  1.00 28.58 ? 157 VAL   A CA  1 
ATOM   518  C  C   . VAL   A 1 64  ? 10.706  0.779   17.049  1.00 28.21 ? 157 VAL   A C   1 
ATOM   519  O  O   . VAL   A 1 64  ? 11.209  1.467   16.124  1.00 27.55 ? 157 VAL   A O   1 
ATOM   520  C  CB  . VAL   A 1 64  ? 8.878   2.384   17.727  1.00 28.77 ? 157 VAL   A CB  1 
ATOM   521  C  CG1 . VAL   A 1 64  ? 7.717   1.539   17.223  1.00 28.08 ? 157 VAL   A CG1 1 
ATOM   522  C  CG2 . VAL   A 1 64  ? 8.445   3.369   18.797  1.00 29.44 ? 157 VAL   A CG2 1 
ATOM   523  N  N   . ARG   A 1 65  ? 10.738  -0.554  17.122  1.00 27.93 ? 158 ARG   A N   1 
ATOM   524  C  CA  . ARG   A 1 65  ? 11.347  -1.444  16.108  1.00 27.02 ? 158 ARG   A CA  1 
ATOM   525  C  C   . ARG   A 1 65  ? 10.226  -2.131  15.323  1.00 26.47 ? 158 ARG   A C   1 
ATOM   526  O  O   . ARG   A 1 65  ? 9.199   -2.504  15.937  1.00 26.79 ? 158 ARG   A O   1 
ATOM   527  C  CB  . ARG   A 1 65  ? 12.269  -2.453  16.802  1.00 27.66 ? 158 ARG   A CB  1 
ATOM   528  C  CG  . ARG   A 1 65  ? 12.985  -3.407  15.853  1.00 27.65 ? 158 ARG   A CG  1 
ATOM   529  C  CD  . ARG   A 1 65  ? 13.803  -4.403  16.647  1.00 28.01 ? 158 ARG   A CD  1 
ATOM   530  N  NE  . ARG   A 1 65  ? 14.689  -3.737  17.602  1.00 28.68 ? 158 ARG   A NE  1 
ATOM   531  C  CZ  . ARG   A 1 65  ? 15.914  -3.292  17.335  1.00 28.58 ? 158 ARG   A CZ  1 
ATOM   532  N  NH1 . ARG   A 1 65  ? 16.431  -3.403  16.127  1.00 28.33 ? 158 ARG   A NH1 1 
ATOM   533  N  NH2 . ARG   A 1 65  ? 16.630  -2.718  18.282  1.00 29.61 ? 158 ARG   A NH2 1 
ATOM   534  N  N   . ALA   A 1 66  ? 10.427  -2.261  14.008  1.00 25.44 ? 159 ALA   A N   1 
ATOM   535  C  CA  . ALA   A 1 66  ? 9.623   -3.062  13.064  1.00 25.20 ? 159 ALA   A CA  1 
ATOM   536  C  C   . ALA   A 1 66  ? 10.510  -4.167  12.482  1.00 25.31 ? 159 ALA   A C   1 
ATOM   537  O  O   . ALA   A 1 66  ? 11.675  -3.877  12.124  1.00 25.20 ? 159 ALA   A O   1 
ATOM   538  C  CB  . ALA   A 1 66  ? 9.058   -2.181  11.982  1.00 24.62 ? 159 ALA   A CB  1 
ATOM   539  N  N   . MET   A 1 67  ? 9.969   -5.379  12.381  1.00 26.01 ? 160 MET   A N   1 
ATOM   540  C  CA  . MET   A 1 67  ? 10.657  -6.572  11.822  1.00 26.92 ? 160 MET   A CA  1 
ATOM   541  C  C   . MET   A 1 67  ? 9.619   -7.440  11.108  1.00 26.24 ? 160 MET   A C   1 
ATOM   542  O  O   . MET   A 1 67  ? 8.519   -7.609  11.663  1.00 26.39 ? 160 MET   A O   1 
ATOM   543  C  CB  . MET   A 1 67  ? 11.333  -7.376  12.939  1.00 28.74 ? 160 MET   A CB  1 
ATOM   544  C  CG  . MET   A 1 67  ? 12.004  -8.656  12.447  1.00 30.24 ? 160 MET   A CG  1 
ATOM   545  S  SD  . MET   A 1 67  ? 12.669  -9.689  13.777  1.00 32.42 ? 160 MET   A SD  1 
ATOM   546  C  CE  . MET   A 1 67  ? 14.002  -8.673  14.405  1.00 32.55 ? 160 MET   A CE  1 
ATOM   547  N  N   . ALA   A 1 68  ? 9.953   -7.963  9.923   1.00 25.70 ? 161 ALA   A N   1 
ATOM   548  C  CA  . ALA   A 1 68  ? 9.092   -8.903  9.176   1.00 25.72 ? 161 ALA   A CA  1 
ATOM   549  C  C   . ALA   A 1 68  ? 9.540   -10.337 9.477   1.00 26.75 ? 161 ALA   A C   1 
ATOM   550  O  O   . ALA   A 1 68  ? 10.750  -10.569 9.579   1.00 27.34 ? 161 ALA   A O   1 
ATOM   551  C  CB  . ALA   A 1 68  ? 9.123   -8.622  7.711   1.00 25.72 ? 161 ALA   A CB  1 
ATOM   552  N  N   . ILE   A 1 69  ? 8.582   -11.237 9.651   1.00 27.91 ? 162 ILE   A N   1 
ATOM   553  C  CA  . ILE   A 1 69  ? 8.805   -12.712 9.633   1.00 29.62 ? 162 ILE   A CA  1 
ATOM   554  C  C   . ILE   A 1 69  ? 7.743   -13.314 8.713   1.00 30.70 ? 162 ILE   A C   1 
ATOM   555  O  O   . ILE   A 1 69  ? 6.716   -12.650 8.494   1.00 31.56 ? 162 ILE   A O   1 
ATOM   556  C  CB  . ILE   A 1 69  ? 8.761   -13.299 11.058  1.00 30.11 ? 162 ILE   A CB  1 
ATOM   557  C  CG1 . ILE   A 1 69  ? 7.390   -13.144 11.716  1.00 30.01 ? 162 ILE   A CG1 1 
ATOM   558  C  CG2 . ILE   A 1 69  ? 9.867   -12.709 11.923  1.00 29.73 ? 162 ILE   A CG2 1 
ATOM   559  C  CD1 . ILE   A 1 69  ? 7.281   -13.892 13.031  1.00 30.82 ? 162 ILE   A CD1 1 
ATOM   560  N  N   . TYR   A 1 70  ? 7.996   -14.510 8.185   1.00 31.98 ? 163 TYR   A N   1 
ATOM   561  C  CA  . TYR   A 1 70  ? 7.007   -15.341 7.452   1.00 32.72 ? 163 TYR   A CA  1 
ATOM   562  C  C   . TYR   A 1 70  ? 5.994   -15.872 8.461   1.00 33.57 ? 163 TYR   A C   1 
ATOM   563  O  O   . TYR   A 1 70  ? 6.399   -16.221 9.594   1.00 34.94 ? 163 TYR   A O   1 
ATOM   564  C  CB  . TYR   A 1 70  ? 7.709   -16.445 6.652   1.00 33.50 ? 163 TYR   A CB  1 
ATOM   565  C  CG  . TYR   A 1 70  ? 8.441   -15.890 5.455   1.00 32.88 ? 163 TYR   A CG  1 
ATOM   566  C  CD1 . TYR   A 1 70  ? 7.736   -15.288 4.421   1.00 32.50 ? 163 TYR   A CD1 1 
ATOM   567  C  CD2 . TYR   A 1 70  ? 9.824   -15.908 5.370   1.00 32.59 ? 163 TYR   A CD2 1 
ATOM   568  C  CE1 . TYR   A 1 70  ? 8.388   -14.741 3.329   1.00 31.62 ? 163 TYR   A CE1 1 
ATOM   569  C  CE2 . TYR   A 1 70  ? 10.486  -15.378 4.272   1.00 32.60 ? 163 TYR   A CE2 1 
ATOM   570  C  CZ  . TYR   A 1 70  ? 9.764   -14.784 3.258   1.00 31.87 ? 163 TYR   A CZ  1 
ATOM   571  O  OH  . TYR   A 1 70  ? 10.403  -14.252 2.184   1.00 32.31 ? 163 TYR   A OH  1 
ATOM   572  N  N   . LYS   A 1 71  ? 4.722   -15.906 8.063   1.00 33.38 ? 164 LYS   A N   1 
ATOM   573  C  CA  . LYS   A 1 71  ? 3.598   -16.289 8.946   1.00 34.52 ? 164 LYS   A CA  1 
ATOM   574  C  C   . LYS   A 1 71  ? 3.580   -17.813 9.100   1.00 35.83 ? 164 LYS   A C   1 
ATOM   575  O  O   . LYS   A 1 71  ? 3.315   -18.269 10.218  1.00 36.56 ? 164 LYS   A O   1 
ATOM   576  C  CB  . LYS   A 1 71  ? 2.281   -15.773 8.374   1.00 35.27 ? 164 LYS   A CB  1 
ATOM   577  C  CG  . LYS   A 1 71  ? 1.036   -16.056 9.216   1.00 35.97 ? 164 LYS   A CG  1 
ATOM   578  C  CD  . LYS   A 1 71  ? -0.222  -15.504 8.613   1.00 36.93 ? 164 LYS   A CD  1 
ATOM   579  C  CE  . LYS   A 1 71  ? -1.425  -16.403 8.833   1.00 38.15 ? 164 LYS   A CE  1 
ATOM   580  N  NZ  . LYS   A 1 71  ? -2.600  -15.849 8.130   1.00 38.52 ? 164 LYS   A NZ  1 
ATOM   581  N  N   . GLN   A 1 72  ? 3.858   -18.542 8.016   1.00 36.22 ? 165 GLN   A N   1 
ATOM   582  C  CA  . GLN   A 1 72  ? 3.733   -20.025 7.937   1.00 38.53 ? 165 GLN   A CA  1 
ATOM   583  C  C   . GLN   A 1 72  ? 4.871   -20.673 8.726   1.00 38.92 ? 165 GLN   A C   1 
ATOM   584  O  O   . GLN   A 1 72  ? 6.011   -20.197 8.577   1.00 38.57 ? 165 GLN   A O   1 
ATOM   585  C  CB  . GLN   A 1 72  ? 3.753   -20.460 6.470   1.00 39.80 ? 165 GLN   A CB  1 
ATOM   586  C  CG  . GLN   A 1 72  ? 2.514   -20.027 5.711   1.00 40.13 ? 165 GLN   A CG  1 
ATOM   587  C  CD  . GLN   A 1 72  ? 2.704   -20.036 4.216   1.00 41.67 ? 165 GLN   A CD  1 
ATOM   588  O  OE1 . GLN   A 1 72  ? 3.677   -19.499 3.682   1.00 41.62 ? 165 GLN   A OE1 1 
ATOM   589  N  NE2 . GLN   A 1 72  ? 1.730   -20.616 3.528   1.00 43.43 ? 165 GLN   A NE2 1 
ATOM   590  N  N   . SER   A 1 73  ? 4.583   -21.743 9.478   1.00 40.13 ? 166 SER   A N   1 
ATOM   591  C  CA  . SER   A 1 73  ? 5.547   -22.399 10.400  1.00 40.79 ? 166 SER   A CA  1 
ATOM   592  C  C   . SER   A 1 73  ? 6.711   -23.013 9.604   1.00 41.98 ? 166 SER   A C   1 
ATOM   593  O  O   . SER   A 1 73  ? 7.834   -23.029 10.140  1.00 41.26 ? 166 SER   A O   1 
ATOM   594  C  CB  . SER   A 1 73  ? 4.868   -23.420 11.272  1.00 42.12 ? 166 SER   A CB  1 
ATOM   595  O  OG  . SER   A 1 73  ? 4.194   -24.391 10.487  1.00 42.37 ? 166 SER   A OG  1 
ATOM   596  N  N   . GLN   A 1 74  ? 6.449   -23.473 8.375   1.00 43.37 ? 167 GLN   A N   1 
ATOM   597  C  CA  . GLN   A 1 74  ? 7.457   -24.154 7.518   1.00 45.17 ? 167 GLN   A CA  1 
ATOM   598  C  C   . GLN   A 1 74  ? 8.419   -23.138 6.882   1.00 43.58 ? 167 GLN   A C   1 
ATOM   599  O  O   . GLN   A 1 74  ? 9.441   -23.583 6.348   1.00 43.82 ? 167 GLN   A O   1 
ATOM   600  C  CB  . GLN   A 1 74  ? 6.787   -25.031 6.456   1.00 47.68 ? 167 GLN   A CB  1 
ATOM   601  C  CG  . GLN   A 1 74  ? 5.954   -24.271 5.433   1.00 47.33 ? 167 GLN   A CG  1 
ATOM   602  C  CD  . GLN   A 1 74  ? 4.489   -24.228 5.792   1.00 48.27 ? 167 GLN   A CD  1 
ATOM   603  O  OE1 . GLN   A 1 74  ? 4.108   -24.129 6.962   1.00 50.41 ? 167 GLN   A OE1 1 
ATOM   604  N  NE2 . GLN   A 1 74  ? 3.649   -24.218 4.772   1.00 48.59 ? 167 GLN   A NE2 1 
ATOM   605  N  N   . HIS   A 1 75  ? 8.132   -21.831 6.950   1.00 41.68 ? 168 HIS   A N   1 
ATOM   606  C  CA  . HIS   A 1 75  ? 8.961   -20.762 6.326   1.00 40.58 ? 168 HIS   A CA  1 
ATOM   607  C  C   . HIS   A 1 75  ? 9.529   -19.799 7.371   1.00 39.55 ? 168 HIS   A C   1 
ATOM   608  O  O   . HIS   A 1 75  ? 10.255  -18.845 6.964   1.00 38.84 ? 168 HIS   A O   1 
ATOM   609  C  CB  . HIS   A 1 75  ? 8.125   -19.976 5.302   1.00 39.77 ? 168 HIS   A CB  1 
ATOM   610  C  CG  . HIS   A 1 75  ? 7.707   -20.795 4.127   1.00 40.89 ? 168 HIS   A CG  1 
ATOM   611  N  ND1 . HIS   A 1 75  ? 8.617   -21.484 3.336   1.00 41.82 ? 168 HIS   A ND1 1 
ATOM   612  C  CD2 . HIS   A 1 75  ? 6.488   -21.024 3.595   1.00 41.17 ? 168 HIS   A CD2 1 
ATOM   613  C  CE1 . HIS   A 1 75  ? 7.969   -22.104 2.370   1.00 42.56 ? 168 HIS   A CE1 1 
ATOM   614  N  NE2 . HIS   A 1 75  ? 6.665   -21.840 2.505   1.00 42.65 ? 168 HIS   A NE2 1 
ATOM   615  N  N   . MET   A 1 76  ? 9.232   -20.029 8.653   1.00 39.64 ? 169 MET   A N   1 
ATOM   616  C  CA  . MET   A 1 76  ? 9.372   -19.011 9.727   1.00 38.53 ? 169 MET   A CA  1 
ATOM   617  C  C   . MET   A 1 76  ? 10.847  -18.727 10.046  1.00 37.86 ? 169 MET   A C   1 
ATOM   618  O  O   . MET   A 1 76  ? 11.146  -17.603 10.460  1.00 35.49 ? 169 MET   A O   1 
ATOM   619  C  CB  . MET   A 1 76  ? 8.661   -19.483 10.999  1.00 39.83 ? 169 MET   A CB  1 
ATOM   620  C  CG  . MET   A 1 76  ? 7.243   -19.014 11.080  1.00 40.03 ? 169 MET   A CG  1 
ATOM   621  S  SD  . MET   A 1 76  ? 6.843   -18.509 12.748  1.00 41.21 ? 169 MET   A SD  1 
ATOM   622  C  CE  . MET   A 1 76  ? 7.037   -20.099 13.561  1.00 42.79 ? 169 MET   A CE  1 
ATOM   623  N  N   A THR   A 1 77  ? 11.725  -19.721 9.860   0.50 38.56 ? 170 THR   A N   1 
ATOM   624  N  N   B THR   A 1 77  ? 11.722  -19.721 9.859   0.50 38.76 ? 170 THR   A N   1 
ATOM   625  C  CA  A THR   A 1 77  ? 13.187  -19.630 10.124  0.50 38.88 ? 170 THR   A CA  1 
ATOM   626  C  CA  B THR   A 1 77  ? 13.186  -19.646 10.117  0.50 39.23 ? 170 THR   A CA  1 
ATOM   627  C  C   A THR   A 1 77  ? 13.906  -18.935 8.961   0.50 38.41 ? 170 THR   A C   1 
ATOM   628  C  C   B THR   A 1 77  ? 13.905  -18.938 8.961   0.50 38.61 ? 170 THR   A C   1 
ATOM   629  O  O   A THR   A 1 77  ? 15.113  -18.676 9.105   0.50 39.18 ? 170 THR   A O   1 
ATOM   630  O  O   B THR   A 1 77  ? 15.112  -18.676 9.107   0.50 39.37 ? 170 THR   A O   1 
ATOM   631  C  CB  A THR   A 1 77  ? 13.813  -21.012 10.343  0.50 40.62 ? 170 THR   A CB  1 
ATOM   632  C  CB  B THR   A 1 77  ? 13.768  -21.054 10.309  0.50 41.21 ? 170 THR   A CB  1 
ATOM   633  O  OG1 A THR   A 1 77  ? 13.867  -21.649 9.067   0.50 41.56 ? 170 THR   A OG1 1 
ATOM   634  O  OG1 B THR   A 1 77  ? 15.193  -20.970 10.334  0.50 42.10 ? 170 THR   A OG1 1 
ATOM   635  C  CG2 A THR   A 1 77  ? 13.052  -21.868 11.331  0.50 41.44 ? 170 THR   A CG2 1 
ATOM   636  C  CG2 B THR   A 1 77  ? 13.342  -22.003 9.211   0.50 42.40 ? 170 THR   A CG2 1 
ATOM   637  N  N   . GLU   A 1 78  ? 13.218  -18.675 7.843   1.00 37.78 ? 171 GLU   A N   1 
ATOM   638  C  CA  . GLU   A 1 78  ? 13.805  -17.959 6.679   1.00 37.57 ? 171 GLU   A CA  1 
ATOM   639  C  C   . GLU   A 1 78  ? 13.728  -16.448 6.954   1.00 35.97 ? 171 GLU   A C   1 
ATOM   640  O  O   . GLU   A 1 78  ? 12.662  -15.995 7.385   1.00 35.09 ? 171 GLU   A O   1 
ATOM   641  C  CB  . GLU   A 1 78  ? 13.100  -18.352 5.379   1.00 38.43 ? 171 GLU   A CB  1 
ATOM   642  C  CG  . GLU   A 1 78  ? 13.718  -17.707 4.151   1.00 39.07 ? 171 GLU   A CG  1 
ATOM   643  C  CD  . GLU   A 1 78  ? 13.260  -18.255 2.811   1.00 40.75 ? 171 GLU   A CD  1 
ATOM   644  O  OE1 . GLU   A 1 78  ? 13.252  -19.483 2.632   1.00 43.07 ? 171 GLU   A OE1 1 
ATOM   645  O  OE2 . GLU   A 1 78  ? 12.905  -17.444 1.937   1.00 40.92 ? 171 GLU   A OE2 1 
ATOM   646  N  N   . VAL   A 1 79  ? 14.819  -15.712 6.732   1.00 35.58 ? 172 VAL   A N   1 
ATOM   647  C  CA  . VAL   A 1 79  ? 14.860  -14.225 6.884   1.00 34.75 ? 172 VAL   A CA  1 
ATOM   648  C  C   . VAL   A 1 79  ? 14.060  -13.590 5.741   1.00 34.47 ? 172 VAL   A C   1 
ATOM   649  O  O   . VAL   A 1 79  ? 14.289  -13.947 4.579   1.00 35.14 ? 172 VAL   A O   1 
ATOM   650  C  CB  . VAL   A 1 79  ? 16.300  -13.677 6.909   1.00 34.87 ? 172 VAL   A CB  1 
ATOM   651  C  CG1 . VAL   A 1 79  ? 16.328  -12.152 6.895   1.00 33.83 ? 172 VAL   A CG1 1 
ATOM   652  C  CG2 . VAL   A 1 79  ? 17.088  -14.203 8.087   1.00 35.51 ? 172 VAL   A CG2 1 
ATOM   653  N  N   . VAL   A 1 80  ? 13.163  -12.666 6.067   1.00 34.36 ? 173 VAL   A N   1 
ATOM   654  C  CA  . VAL   A 1 80  ? 12.390  -11.883 5.063   1.00 33.90 ? 173 VAL   A CA  1 
ATOM   655  C  C   . VAL   A 1 80  ? 13.300  -10.774 4.528   1.00 34.35 ? 173 VAL   A C   1 
ATOM   656  O  O   . VAL   A 1 80  ? 13.743  -9.933  5.342   1.00 32.80 ? 173 VAL   A O   1 
ATOM   657  C  CB  . VAL   A 1 80  ? 11.094  -11.299 5.650   1.00 32.66 ? 173 VAL   A CB  1 
ATOM   658  C  CG1 . VAL   A 1 80  ? 10.331  -10.518 4.590   1.00 32.22 ? 173 VAL   A CG1 1 
ATOM   659  C  CG2 . VAL   A 1 80  ? 10.206  -12.376 6.266   1.00 32.77 ? 173 VAL   A CG2 1 
ATOM   660  N  N   . ARG   A 1 81  ? 13.555  -10.779 3.218   1.00 34.86 ? 174 ARG   A N   1 
ATOM   661  C  CA  . ARG   A 1 81  ? 14.405  -9.778  2.513   1.00 36.34 ? 174 ARG   A CA  1 
ATOM   662  C  C   . ARG   A 1 81  ? 13.773  -9.447  1.156   1.00 36.26 ? 174 ARG   A C   1 
ATOM   663  O  O   . ARG   A 1 81  ? 12.867  -10.189 0.700   1.00 36.68 ? 174 ARG   A O   1 
ATOM   664  C  CB  . ARG   A 1 81  ? 15.836  -10.308 2.324   1.00 38.06 ? 174 ARG   A CB  1 
ATOM   665  C  CG  . ARG   A 1 81  ? 15.882  -11.715 1.733   1.00 40.47 ? 174 ARG   A CG  1 
ATOM   666  C  CD  . ARG   A 1 81  ? 17.285  -12.239 1.493   1.00 42.51 ? 174 ARG   A CD  1 
ATOM   667  N  NE  . ARG   A 1 81  ? 17.903  -12.895 2.638   1.00 43.16 ? 174 ARG   A NE  1 
ATOM   668  C  CZ  . ARG   A 1 81  ? 18.736  -12.326 3.517   1.00 44.31 ? 174 ARG   A CZ  1 
ATOM   669  N  NH1 . ARG   A 1 81  ? 19.052  -11.039 3.446   1.00 43.30 ? 174 ARG   A NH1 1 
ATOM   670  N  NH2 . ARG   A 1 81  ? 19.266  -13.068 4.480   1.00 45.06 ? 174 ARG   A NH2 1 
ATOM   671  N  N   . ARG   A 1 82  ? 14.258  -8.385  0.519   1.00 35.69 ? 175 ARG   A N   1 
ATOM   672  C  CA  . ARG   A 1 82  ? 13.855  -8.017  -0.861  1.00 35.81 ? 175 ARG   A CA  1 
ATOM   673  C  C   . ARG   A 1 82  ? 14.378  -9.064  -1.851  1.00 37.51 ? 175 ARG   A C   1 
ATOM   674  O  O   . ARG   A 1 82  ? 15.391  -9.724  -1.542  1.00 37.55 ? 175 ARG   A O   1 
ATOM   675  C  CB  . ARG   A 1 82  ? 14.394  -6.636  -1.226  1.00 35.29 ? 175 ARG   A CB  1 
ATOM   676  C  CG  . ARG   A 1 82  ? 13.883  -5.525  -0.318  1.00 33.84 ? 175 ARG   A CG  1 
ATOM   677  C  CD  . ARG   A 1 82  ? 14.535  -4.227  -0.713  1.00 34.47 ? 175 ARG   A CD  1 
ATOM   678  N  NE  . ARG   A 1 82  ? 13.823  -3.572  -1.793  1.00 34.48 ? 175 ARG   A NE  1 
ATOM   679  C  CZ  . ARG   A 1 82  ? 14.244  -2.486  -2.426  1.00 35.11 ? 175 ARG   A CZ  1 
ATOM   680  N  NH1 . ARG   A 1 82  ? 15.412  -1.944  -2.135  1.00 35.36 ? 175 ARG   A NH1 1 
ATOM   681  N  NH2 . ARG   A 1 82  ? 13.487  -1.949  -3.355  1.00 35.21 ? 175 ARG   A NH2 1 
ATOM   682  N  N   . CYS   A 1 83  ? 13.710  -9.183  -2.996  1.00 38.19 ? 176 CYS   A N   1 
ATOM   683  C  CA  . CYS   A 1 83  ? 14.143  -10.029 -4.134  1.00 40.74 ? 176 CYS   A CA  1 
ATOM   684  C  C   . CYS   A 1 83  ? 15.383  -9.397  -4.761  1.00 42.24 ? 176 CYS   A C   1 
ATOM   685  O  O   . CYS   A 1 83  ? 15.622  -8.197  -4.612  1.00 42.43 ? 176 CYS   A O   1 
ATOM   686  C  CB  . CYS   A 1 83  ? 13.006  -10.166 -5.140  1.00 41.25 ? 176 CYS   A CB  1 
ATOM   687  S  SG  . CYS   A 1 83  ? 12.614  -8.668  -6.004  1.00 41.02 ? 176 CYS   A SG  1 
ATOM   688  N  N   . PRO   A 1 84  ? 16.224  -10.179 -5.471  1.00 44.77 ? 177 PRO   A N   1 
ATOM   689  C  CA  . PRO   A 1 84  ? 17.357  -9.609  -6.204  1.00 46.00 ? 177 PRO   A CA  1 
ATOM   690  C  C   . PRO   A 1 84  ? 16.968  -8.339  -6.980  1.00 46.39 ? 177 PRO   A C   1 
ATOM   691  O  O   . PRO   A 1 84  ? 17.625  -7.335  -6.812  1.00 46.18 ? 177 PRO   A O   1 
ATOM   692  C  CB  . PRO   A 1 84  ? 17.763  -10.762 -7.127  1.00 47.91 ? 177 PRO   A CB  1 
ATOM   693  C  CG  . PRO   A 1 84  ? 17.433  -12.000 -6.317  1.00 47.40 ? 177 PRO   A CG  1 
ATOM   694  C  CD  . PRO   A 1 84  ? 16.143  -11.643 -5.602  1.00 45.64 ? 177 PRO   A CD  1 
ATOM   695  N  N   . HIS   A 1 85  ? 15.886  -8.402  -7.763  1.00 46.36 ? 178 HIS   A N   1 
ATOM   696  C  CA  . HIS   A 1 85  ? 15.436  -7.319  -8.680  1.00 46.81 ? 178 HIS   A CA  1 
ATOM   697  C  C   . HIS   A 1 85  ? 15.286  -6.001  -7.915  1.00 45.57 ? 178 HIS   A C   1 
ATOM   698  O  O   . HIS   A 1 85  ? 15.861  -4.999  -8.369  1.00 46.32 ? 178 HIS   A O   1 
ATOM   699  C  CB  . HIS   A 1 85  ? 14.127  -7.692  -9.397  1.00 47.62 ? 178 HIS   A CB  1 
ATOM   700  C  CG  . HIS   A 1 85  ? 13.469  -6.535  -10.077 1.00 47.84 ? 178 HIS   A CG  1 
ATOM   701  N  ND1 . HIS   A 1 85  ? 14.000  -5.976  -11.211 1.00 50.02 ? 178 HIS   A ND1 1 
ATOM   702  C  CD2 . HIS   A 1 85  ? 12.345  -5.833  -9.796  1.00 47.42 ? 178 HIS   A CD2 1 
ATOM   703  C  CE1 . HIS   A 1 85  ? 13.237  -4.983  -11.618 1.00 50.09 ? 178 HIS   A CE1 1 
ATOM   704  N  NE2 . HIS   A 1 85  ? 12.219  -4.869  -10.759 1.00 48.99 ? 178 HIS   A NE2 1 
ATOM   705  N  N   . HIS   A 1 86  ? 14.519  -5.991  -6.822  1.00 43.64 ? 179 HIS   A N   1 
ATOM   706  C  CA  . HIS   A 1 86  ? 14.207  -4.754  -6.054  1.00 43.23 ? 179 HIS   A CA  1 
ATOM   707  C  C   . HIS   A 1 86  ? 15.455  -4.275  -5.304  1.00 43.35 ? 179 HIS   A C   1 
ATOM   708  O  O   . HIS   A 1 86  ? 15.630  -3.054  -5.183  1.00 42.73 ? 179 HIS   A O   1 
ATOM   709  C  CB  . HIS   A 1 86  ? 12.992  -4.958  -5.144  1.00 41.13 ? 179 HIS   A CB  1 
ATOM   710  C  CG  . HIS   A 1 86  ? 11.707  -4.762  -5.871  1.00 41.09 ? 179 HIS   A CG  1 
ATOM   711  N  ND1 . HIS   A 1 86  ? 10.696  -5.701  -5.864  1.00 40.72 ? 179 HIS   A ND1 1 
ATOM   712  C  CD2 . HIS   A 1 86  ? 11.278  -3.740  -6.645  1.00 41.12 ? 179 HIS   A CD2 1 
ATOM   713  C  CE1 . HIS   A 1 86  ? 9.689   -5.251  -6.586  1.00 42.16 ? 179 HIS   A CE1 1 
ATOM   714  N  NE2 . HIS   A 1 86  ? 10.035  -4.060  -7.097  1.00 41.17 ? 179 HIS   A NE2 1 
ATOM   715  N  N   . GLU   A 1 87  ? 16.299  -5.199  -4.847  1.00 44.18 ? 180 GLU   A N   1 
ATOM   716  C  CA  . GLU   A 1 87  ? 17.573  -4.867  -4.153  1.00 45.33 ? 180 GLU   A CA  1 
ATOM   717  C  C   . GLU   A 1 87  ? 18.458  -4.011  -5.084  1.00 47.54 ? 180 GLU   A C   1 
ATOM   718  O  O   . GLU   A 1 87  ? 19.086  -3.073  -4.577  1.00 47.80 ? 180 GLU   A O   1 
ATOM   719  C  CB  . GLU   A 1 87  ? 18.248  -6.156  -3.682  1.00 45.52 ? 180 GLU   A CB  1 
ATOM   720  C  CG  . GLU   A 1 87  ? 19.569  -5.924  -2.975  1.00 45.86 ? 180 GLU   A CG  1 
ATOM   721  C  CD  . GLU   A 1 87  ? 20.346  -7.201  -2.701  0.80 46.56 ? 180 GLU   A CD  1 
ATOM   722  O  OE1 . GLU   A 1 87  ? 21.561  -7.221  -2.981  0.80 47.67 ? 180 GLU   A OE1 1 
ATOM   723  O  OE2 . GLU   A 1 87  ? 19.728  -8.174  -2.227  0.80 45.42 ? 180 GLU   A OE2 1 
ATOM   724  N  N   . ARG   A 1 88  ? 18.457  -4.271  -6.401  1.00 49.21 ? 181 ARG   A N   1 
ATOM   725  C  CA  . ARG   A 1 88  ? 19.308  -3.558  -7.398  1.00 51.57 ? 181 ARG   A CA  1 
ATOM   726  C  C   . ARG   A 1 88  ? 18.596  -2.338  -8.005  1.00 51.63 ? 181 ARG   A C   1 
ATOM   727  O  O   . ARG   A 1 88  ? 19.285  -1.579  -8.709  1.00 52.61 ? 181 ARG   A O   1 
ATOM   728  C  CB  . ARG   A 1 88  ? 19.743  -4.491  -8.532  1.00 53.66 ? 181 ARG   A CB  1 
ATOM   729  C  CG  . ARG   A 1 88  ? 20.737  -5.556  -8.090  1.00 54.72 ? 181 ARG   A CG  1 
ATOM   730  C  CD  . ARG   A 1 88  ? 20.863  -6.651  -9.123  1.00 57.00 ? 181 ARG   A CD  1 
ATOM   731  N  NE  . ARG   A 1 88  ? 21.918  -7.605  -8.817  1.00 58.50 ? 181 ARG   A NE  1 
ATOM   732  C  CZ  . ARG   A 1 88  ? 22.201  -8.671  -9.560  1.00 61.16 ? 181 ARG   A CZ  1 
ATOM   733  N  NH1 . ARG   A 1 88  ? 21.499  -8.926  -10.652 1.00 62.38 ? 181 ARG   A NH1 1 
ATOM   734  N  NH2 . ARG   A 1 88  ? 23.196  -9.475  -9.221  1.00 62.58 ? 181 ARG   A NH2 1 
ATOM   735  N  N   . CYS   A 1 89  ? 17.290  -2.136  -7.792  1.00 50.48 ? 182 CYS   A N   1 
ATOM   736  C  CA  . CYS   A 1 89  ? 16.574  -0.893  -8.227  1.00 50.46 ? 182 CYS   A CA  1 
ATOM   737  C  C   . CYS   A 1 89  ? 17.159  0.307   -7.472  1.00 50.91 ? 182 CYS   A C   1 
ATOM   738  O  O   . CYS   A 1 89  ? 17.387  0.165   -6.255  1.00 51.72 ? 182 CYS   A O   1 
ATOM   739  C  CB  . CYS   A 1 89  ? 15.075  -0.926  -7.953  1.00 49.15 ? 182 CYS   A CB  1 
ATOM   740  S  SG  . CYS   A 1 89  ? 14.078  -1.765  -9.214  1.00 49.13 ? 182 CYS   A SG  1 
ATOM   741  N  N   . SER   A 1 90  ? 17.440  1.428   -8.153  1.00 52.81 ? 183 SER   A N   1 
ATOM   742  C  CA  . SER   A 1 90  ? 18.231  2.559   -7.593  1.00 53.44 ? 183 SER   A CA  1 
ATOM   743  C  C   . SER   A 1 90  ? 17.340  3.424   -6.693  1.00 51.58 ? 183 SER   A C   1 
ATOM   744  O  O   . SER   A 1 90  ? 17.248  4.634   -6.952  1.00 52.62 ? 183 SER   A O   1 
ATOM   745  C  CB  . SER   A 1 90  ? 18.886  3.364   -8.679  1.00 56.19 ? 183 SER   A CB  1 
ATOM   746  O  OG  . SER   A 1 90  ? 19.952  2.623   -9.236  1.00 58.88 ? 183 SER   A OG  1 
ATOM   747  N  N   . ASP   A 1 91  ? 16.755  2.813   -5.655  0.80 50.07 ? 184 ASP   A N   1 
ATOM   748  C  CA  . ASP   A 1 91  ? 15.629  3.360   -4.854  0.80 47.89 ? 184 ASP   A CA  1 
ATOM   749  C  C   . ASP   A 1 91  ? 16.089  3.646   -3.424  0.80 47.06 ? 184 ASP   A C   1 
ATOM   750  O  O   . ASP   A 1 91  ? 15.274  4.229   -2.688  0.80 45.16 ? 184 ASP   A O   1 
ATOM   751  C  CB  . ASP   A 1 91  ? 14.445  2.386   -4.834  0.80 46.48 ? 184 ASP   A CB  1 
ATOM   752  C  CG  . ASP   A 1 91  ? 14.714  1.042   -4.166  0.80 45.20 ? 184 ASP   A CG  1 
ATOM   753  O  OD1 . ASP   A 1 91  ? 15.657  0.950   -3.355  0.80 45.51 ? 184 ASP   A OD1 1 
ATOM   754  O  OD2 . ASP   A 1 91  ? 13.971  0.094   -4.445  0.80 43.60 ? 184 ASP   A OD2 1 
ATOM   755  N  N   . SER   A 1 92  ? 17.317  3.247   -3.061  1.00 48.12 ? 185 SER   A N   1 
ATOM   756  C  CA  . SER   A 1 92  ? 17.937  3.579   -1.752  1.00 47.93 ? 185 SER   A CA  1 
ATOM   757  C  C   . SER   A 1 92  ? 17.709  5.071   -1.480  1.00 48.58 ? 185 SER   A C   1 
ATOM   758  O  O   . SER   A 1 92  ? 17.930  5.899   -2.394  1.00 51.11 ? 185 SER   A O   1 
ATOM   759  C  CB  . SER   A 1 92  ? 19.397  3.220   -1.705  1.00 49.43 ? 185 SER   A CB  1 
ATOM   760  O  OG  . SER   A 1 92  ? 20.102  3.792   -2.796  1.00 52.21 ? 185 SER   A OG  1 
ATOM   761  N  N   . ASP   A 1 93  ? 17.313  5.407   -0.254  1.00 47.28 ? 186 ASP   A N   1 
ATOM   762  C  CA  . ASP   A 1 93  ? 17.136  6.807   0.217   1.00 46.92 ? 186 ASP   A CA  1 
ATOM   763  C  C   . ASP   A 1 93  ? 18.416  7.291   0.919   1.00 46.74 ? 186 ASP   A C   1 
ATOM   764  O  O   . ASP   A 1 93  ? 18.386  8.371   1.522   1.00 48.07 ? 186 ASP   A O   1 
ATOM   765  C  CB  . ASP   A 1 93  ? 15.917  6.894   1.134   1.00 45.98 ? 186 ASP   A CB  1 
ATOM   766  C  CG  . ASP   A 1 93  ? 16.065  6.168   2.465   1.00 44.97 ? 186 ASP   A CG  1 
ATOM   767  O  OD1 . ASP   A 1 93  ? 17.020  5.391   2.616   1.00 45.24 ? 186 ASP   A OD1 1 
ATOM   768  O  OD2 . ASP   A 1 93  ? 15.219  6.396   3.336   1.00 45.67 ? 186 ASP   A OD2 1 
ATOM   769  N  N   . GLY   A 1 94  ? 19.495  6.510   0.872   1.00 45.74 ? 187 GLY   A N   1 
ATOM   770  C  CA  . GLY   A 1 94  ? 20.797  6.834   1.482   1.00 45.53 ? 187 GLY   A CA  1 
ATOM   771  C  C   . GLY   A 1 94  ? 20.883  6.376   2.924   1.00 43.63 ? 187 GLY   A C   1 
ATOM   772  O  O   . GLY   A 1 94  ? 22.009  6.383   3.456   1.00 44.94 ? 187 GLY   A O   1 
ATOM   773  N  N   . LEU   A 1 95  ? 19.778  5.949   3.546   1.00 41.02 ? 188 LEU   A N   1 
ATOM   774  C  CA  . LEU   A 1 95  ? 19.810  5.486   4.962   1.00 38.92 ? 188 LEU   A CA  1 
ATOM   775  C  C   . LEU   A 1 95  ? 19.551  3.972   5.048   1.00 36.66 ? 188 LEU   A C   1 
ATOM   776  O  O   . LEU   A 1 95  ? 20.256  3.328   5.821   1.00 36.20 ? 188 LEU   A O   1 
ATOM   777  C  CB  . LEU   A 1 95  ? 18.783  6.287   5.767   1.00 38.41 ? 188 LEU   A CB  1 
ATOM   778  C  CG  . LEU   A 1 95  ? 18.983  7.804   5.754   1.00 39.17 ? 188 LEU   A CG  1 
ATOM   779  C  CD1 . LEU   A 1 95  ? 17.796  8.518   6.386   1.00 39.42 ? 188 LEU   A CD1 1 
ATOM   780  C  CD2 . LEU   A 1 95  ? 20.270  8.187   6.460   1.00 40.30 ? 188 LEU   A CD2 1 
ATOM   781  N  N   . ALA   A 1 96  ? 18.599  3.435   4.280   1.00 34.95 ? 189 ALA   A N   1 
ATOM   782  C  CA  . ALA   A 1 96  ? 18.135  2.027   4.390   1.00 33.63 ? 189 ALA   A CA  1 
ATOM   783  C  C   . ALA   A 1 96  ? 19.078  1.093   3.633   1.00 33.69 ? 189 ALA   A C   1 
ATOM   784  O  O   . ALA   A 1 96  ? 19.502  1.387   2.519   1.00 33.78 ? 189 ALA   A O   1 
ATOM   785  C  CB  . ALA   A 1 96  ? 16.720  1.903   3.874   1.00 33.68 ? 189 ALA   A CB  1 
ATOM   786  N  N   . PRO   A 1 97  ? 19.456  -0.069  4.207   1.00 33.10 ? 190 PRO   A N   1 
ATOM   787  C  CA  . PRO   A 1 97  ? 20.202  -1.069  3.450   1.00 33.46 ? 190 PRO   A CA  1 
ATOM   788  C  C   . PRO   A 1 97  ? 19.333  -1.505  2.278   1.00 33.35 ? 190 PRO   A C   1 
ATOM   789  O  O   . PRO   A 1 97  ? 18.112  -1.600  2.412   1.00 32.13 ? 190 PRO   A O   1 
ATOM   790  C  CB  . PRO   A 1 97  ? 20.458  -2.206  4.447   1.00 32.77 ? 190 PRO   A CB  1 
ATOM   791  C  CG  . PRO   A 1 97  ? 20.259  -1.559  5.802   1.00 32.37 ? 190 PRO   A CG  1 
ATOM   792  C  CD  . PRO   A 1 97  ? 19.210  -0.485  5.599   1.00 31.81 ? 190 PRO   A CD  1 
ATOM   793  N  N   . PRO   A 1 98  ? 19.935  -1.791  1.105   1.00 34.55 ? 191 PRO   A N   1 
ATOM   794  C  CA  . PRO   A 1 98  ? 19.158  -2.170  -0.073  1.00 34.86 ? 191 PRO   A CA  1 
ATOM   795  C  C   . PRO   A 1 98  ? 18.360  -3.482  0.087   1.00 34.19 ? 191 PRO   A C   1 
ATOM   796  O  O   . PRO   A 1 98  ? 17.417  -3.662  -0.631  1.00 33.70 ? 191 PRO   A O   1 
ATOM   797  C  CB  . PRO   A 1 98  ? 20.209  -2.258  -1.193  1.00 36.16 ? 191 PRO   A CB  1 
ATOM   798  C  CG  . PRO   A 1 98  ? 21.532  -2.435  -0.489  1.00 37.01 ? 191 PRO   A CG  1 
ATOM   799  C  CD  . PRO   A 1 98  ? 21.386  -1.764  0.856   1.00 35.88 ? 191 PRO   A CD  1 
ATOM   800  N  N   A GLN   A 1 99  ? 18.756  -4.350  1.027   0.40 33.93 ? 192 GLN   A N   1 
ATOM   801  N  N   B GLN   A 1 99  ? 18.755  -4.345  1.029   0.60 34.54 ? 192 GLN   A N   1 
ATOM   802  C  CA  A GLN   A 1 99  ? 18.146  -5.693  1.260   0.40 33.33 ? 192 GLN   A CA  1 
ATOM   803  C  CA  B GLN   A 1 99  ? 18.160  -5.689  1.275   0.60 34.14 ? 192 GLN   A CA  1 
ATOM   804  C  C   A GLN   A 1 99  ? 16.888  -5.603  2.135   0.40 32.17 ? 192 GLN   A C   1 
ATOM   805  C  C   B GLN   A 1 99  ? 16.891  -5.602  2.136   0.60 32.65 ? 192 GLN   A C   1 
ATOM   806  O  O   A GLN   A 1 99  ? 16.086  -6.584  2.111   0.40 31.85 ? 192 GLN   A O   1 
ATOM   807  O  O   B GLN   A 1 99  ? 16.089  -6.583  2.109   0.60 32.17 ? 192 GLN   A O   1 
ATOM   808  C  CB  A GLN   A 1 99  ? 19.133  -6.633  1.948   0.40 33.67 ? 192 GLN   A CB  1 
ATOM   809  C  CB  B GLN   A 1 99  ? 19.169  -6.580  1.996   0.60 35.08 ? 192 GLN   A CB  1 
ATOM   810  C  CG  A GLN   A 1 99  ? 20.373  -6.933  1.118   0.40 35.07 ? 192 GLN   A CG  1 
ATOM   811  C  CG  B GLN   A 1 99  ? 20.343  -7.019  1.133   0.60 37.18 ? 192 GLN   A CG  1 
ATOM   812  C  CD  A GLN   A 1 99  ? 21.336  -5.774  1.174   0.40 35.14 ? 192 GLN   A CD  1 
ATOM   813  C  CD  B GLN   A 1 99  ? 20.985  -8.264  1.704   0.60 37.96 ? 192 GLN   A CD  1 
ATOM   814  O  OE1 A GLN   A 1 99  ? 21.168  -4.848  1.963   0.40 34.09 ? 192 GLN   A OE1 1 
ATOM   815  O  OE1 B GLN   A 1 99  ? 21.049  -8.445  2.919   0.60 38.15 ? 192 GLN   A OE1 1 
ATOM   816  N  NE2 A GLN   A 1 99  ? 22.350  -5.819  0.327   0.40 36.31 ? 192 GLN   A NE2 1 
ATOM   817  N  NE2 B GLN   A 1 99  ? 21.443  -9.146  0.832   0.60 39.71 ? 192 GLN   A NE2 1 
ATOM   818  N  N   . HIS   A 1 100 ? 16.706  -4.499  2.875   1.00 31.33 ? 193 HIS   A N   1 
ATOM   819  C  CA  . HIS   A 1 100 ? 15.653  -4.347  3.912   1.00 30.43 ? 193 HIS   A CA  1 
ATOM   820  C  C   . HIS   A 1 100 ? 14.281  -4.173  3.262   1.00 30.28 ? 193 HIS   A C   1 
ATOM   821  O  O   . HIS   A 1 100 ? 14.103  -3.242  2.458   1.00 30.80 ? 193 HIS   A O   1 
ATOM   822  C  CB  . HIS   A 1 100 ? 15.971  -3.200  4.882   1.00 29.70 ? 193 HIS   A CB  1 
ATOM   823  C  CG  . HIS   A 1 100 ? 16.925  -3.595  5.955   1.00 29.73 ? 193 HIS   A CG  1 
ATOM   824  N  ND1 . HIS   A 1 100 ? 16.705  -3.306  7.298   1.00 28.95 ? 193 HIS   A ND1 1 
ATOM   825  C  CD2 . HIS   A 1 100 ? 18.079  -4.288  5.893   1.00 30.23 ? 193 HIS   A CD2 1 
ATOM   826  C  CE1 . HIS   A 1 100 ? 17.701  -3.799  8.010   1.00 29.39 ? 193 HIS   A CE1 1 
ATOM   827  N  NE2 . HIS   A 1 100 ? 18.550  -4.402  7.173   1.00 30.94 ? 193 HIS   A NE2 1 
ATOM   828  N  N   . LEU   A 1 101 ? 13.331  -5.025  3.652   1.00 29.75 ? 194 LEU   A N   1 
ATOM   829  C  CA  . LEU   A 1 101 ? 11.936  -4.942  3.181   1.00 29.25 ? 194 LEU   A CA  1 
ATOM   830  C  C   . LEU   A 1 101 ? 11.280  -3.684  3.743   1.00 28.23 ? 194 LEU   A C   1 
ATOM   831  O  O   . LEU   A 1 101 ? 10.574  -3.030  2.970   1.00 29.03 ? 194 LEU   A O   1 
ATOM   832  C  CB  . LEU   A 1 101 ? 11.141  -6.180  3.600   1.00 28.71 ? 194 LEU   A CB  1 
ATOM   833  C  CG  . LEU   A 1 101 ? 9.650   -6.077  3.297   1.00 28.27 ? 194 LEU   A CG  1 
ATOM   834  C  CD1 . LEU   A 1 101 ? 9.420   -6.034  1.801   1.00 28.66 ? 194 LEU   A CD1 1 
ATOM   835  C  CD2 . LEU   A 1 101 ? 8.875   -7.207  3.937   1.00 28.02 ? 194 LEU   A CD2 1 
ATOM   836  N  N   . ILE   A 1 102 ? 11.483  -3.383  5.030   1.00 28.50 ? 195 ILE   A N   1 
ATOM   837  C  CA  . ILE   A 1 102 ? 10.690  -2.355  5.772   1.00 28.21 ? 195 ILE   A CA  1 
ATOM   838  C  C   . ILE   A 1 102 ? 11.571  -1.133  5.977   1.00 28.69 ? 195 ILE   A C   1 
ATOM   839  O  O   . ILE   A 1 102 ? 12.638  -1.266  6.603   1.00 29.46 ? 195 ILE   A O   1 
ATOM   840  C  CB  . ILE   A 1 102 ? 10.131  -2.864  7.116   1.00 27.75 ? 195 ILE   A CB  1 
ATOM   841  C  CG1 . ILE   A 1 102 ? 9.460   -4.230  6.979   1.00 28.20 ? 195 ILE   A CG1 1 
ATOM   842  C  CG2 . ILE   A 1 102 ? 9.185   -1.840  7.706   1.00 27.01 ? 195 ILE   A CG2 1 
ATOM   843  C  CD1 . ILE   A 1 102 ? 8.672   -4.647  8.200   1.00 28.37 ? 195 ILE   A CD1 1 
ATOM   844  N  N   . ARG   A 1 103 ? 11.117  0.017   5.484   1.00 28.84 ? 196 ARG   A N   1 
ATOM   845  C  CA  . ARG   A 1 103 ? 11.790  1.313   5.721   1.00 28.03 ? 196 ARG   A CA  1 
ATOM   846  C  C   . ARG   A 1 103 ? 10.859  2.207   6.536   1.00 27.73 ? 196 ARG   A C   1 
ATOM   847  O  O   . ARG   A 1 103 ? 9.643   1.946   6.546   1.00 26.48 ? 196 ARG   A O   1 
ATOM   848  C  CB  . ARG   A 1 103 ? 12.120  1.986   4.390   1.00 28.99 ? 196 ARG   A CB  1 
ATOM   849  C  CG  . ARG   A 1 103 ? 13.034  1.178   3.494   1.00 29.27 ? 196 ARG   A CG  1 
ATOM   850  C  CD  . ARG   A 1 103 ? 13.566  2.104   2.420   1.00 30.02 ? 196 ARG   A CD  1 
ATOM   851  N  NE  . ARG   A 1 103 ? 14.293  1.375   1.401   1.00 30.52 ? 196 ARG   A NE  1 
ATOM   852  C  CZ  . ARG   A 1 103 ? 14.585  1.843   0.205   1.00 31.75 ? 196 ARG   A CZ  1 
ATOM   853  N  NH1 . ARG   A 1 103 ? 14.210  3.065   -0.140  1.00 32.74 ? 196 ARG   A NH1 1 
ATOM   854  N  NH2 . ARG   A 1 103 ? 15.255  1.085   -0.638  1.00 32.68 ? 196 ARG   A NH2 1 
ATOM   855  N  N   . VAL   A 1 104 ? 11.408  3.241   7.175   1.00 27.87 ? 197 VAL   A N   1 
ATOM   856  C  CA  . VAL   A 1 104 ? 10.621  4.368   7.734   1.00 27.93 ? 197 VAL   A CA  1 
ATOM   857  C  C   . VAL   A 1 104 ? 10.938  5.591   6.881   1.00 28.83 ? 197 VAL   A C   1 
ATOM   858  O  O   . VAL   A 1 104 ? 12.134  5.789   6.532   1.00 28.42 ? 197 VAL   A O   1 
ATOM   859  C  CB  . VAL   A 1 104 ? 10.907  4.585   9.235   1.00 27.57 ? 197 VAL   A CB  1 
ATOM   860  C  CG1 . VAL   A 1 104 ? 10.276  5.859   9.751   1.00 28.34 ? 197 VAL   A CG1 1 
ATOM   861  C  CG2 . VAL   A 1 104 ? 10.467  3.399   10.078  1.00 26.57 ? 197 VAL   A CG2 1 
ATOM   862  N  N   . GLU   A 1 105 ? 9.907   6.340   6.494   1.00 30.17 ? 198 GLU   A N   1 
ATOM   863  C  CA  . GLU   A 1 105 ? 10.046  7.576   5.686   1.00 32.20 ? 198 GLU   A CA  1 
ATOM   864  C  C   . GLU   A 1 105 ? 9.813   8.770   6.615   1.00 32.69 ? 198 GLU   A C   1 
ATOM   865  O  O   . GLU   A 1 105 ? 9.108   8.609   7.630   1.00 31.42 ? 198 GLU   A O   1 
ATOM   866  C  CB  . GLU   A 1 105 ? 9.109   7.532   4.473   1.00 33.78 ? 198 GLU   A CB  1 
ATOM   867  C  CG  . GLU   A 1 105 ? 7.859   8.389   4.563   1.00 35.00 ? 198 GLU   A CG  1 
ATOM   868  C  CD  . GLU   A 1 105 ? 6.928   8.265   3.361   1.00 37.13 ? 198 GLU   A CD  1 
ATOM   869  O  OE1 . GLU   A 1 105 ? 6.685   9.276   2.674   1.00 39.15 ? 198 GLU   A OE1 1 
ATOM   870  O  OE2 . GLU   A 1 105 ? 6.442   7.150   3.099   1.00 37.17 ? 198 GLU   A OE2 1 
ATOM   871  N  N   . GLY   A 1 106 ? 10.393  9.926   6.277   1.00 34.05 ? 199 GLY   A N   1 
ATOM   872  C  CA  . GLY   A 1 106 ? 10.202  11.196  7.001   1.00 35.38 ? 199 GLY   A CA  1 
ATOM   873  C  C   . GLY   A 1 106 ? 10.850  11.210  8.379   1.00 35.79 ? 199 GLY   A C   1 
ATOM   874  O  O   . GLY   A 1 106 ? 10.410  12.045  9.193   1.00 36.32 ? 199 GLY   A O   1 
ATOM   875  N  N   . ASN   A 1 107 ? 11.853  10.355  8.653   1.00 34.34 ? 200 ASN   A N   1 
ATOM   876  C  CA  . ASN   A 1 107 ? 12.516  10.335  9.984   1.00 33.70 ? 200 ASN   A CA  1 
ATOM   877  C  C   . ASN   A 1 107 ? 14.035  10.219  9.818   1.00 34.09 ? 200 ASN   A C   1 
ATOM   878  O  O   . ASN   A 1 107 ? 14.545  9.119   9.553   1.00 33.78 ? 200 ASN   A O   1 
ATOM   879  C  CB  . ASN   A 1 107 ? 11.898  9.290   10.917  1.00 32.48 ? 200 ASN   A CB  1 
ATOM   880  C  CG  . ASN   A 1 107 ? 12.229  9.584   12.367  1.00 32.82 ? 200 ASN   A CG  1 
ATOM   881  O  OD1 . ASN   A 1 107 ? 13.317  10.070  12.662  1.00 32.35 ? 200 ASN   A OD1 1 
ATOM   882  N  ND2 . ASN   A 1 107 ? 11.324  9.283   13.281  1.00 32.33 ? 200 ASN   A ND2 1 
ATOM   883  N  N   . LEU   A 1 108 ? 14.739  11.328  10.011  1.00 34.87 ? 201 LEU   A N   1 
ATOM   884  C  CA  . LEU   A 1 108 ? 16.210  11.402  9.850   1.00 35.45 ? 201 LEU   A CA  1 
ATOM   885  C  C   . LEU   A 1 108 ? 16.928  10.665  10.987  1.00 34.72 ? 201 LEU   A C   1 
ATOM   886  O  O   . LEU   A 1 108 ? 18.138  10.505  10.851  1.00 34.95 ? 201 LEU   A O   1 
ATOM   887  C  CB  . LEU   A 1 108 ? 16.643  12.872  9.785   1.00 37.04 ? 201 LEU   A CB  1 
ATOM   888  C  CG  . LEU   A 1 108 ? 16.753  13.473  8.384   1.00 38.51 ? 201 LEU   A CG  1 
ATOM   889  C  CD1 . LEU   A 1 108 ? 15.391  13.520  7.712   1.00 38.19 ? 201 LEU   A CD1 1 
ATOM   890  C  CD2 . LEU   A 1 108 ? 17.372  14.868  8.459   1.00 40.15 ? 201 LEU   A CD2 1 
ATOM   891  N  N   . ARG   A 1 109 ? 16.231  10.253  12.053  1.00 34.30 ? 202 ARG   A N   1 
ATOM   892  C  CA  . ARG   A 1 109 ? 16.836  9.552   13.225  1.00 34.08 ? 202 ARG   A CA  1 
ATOM   893  C  C   . ARG   A 1 109 ? 16.620  8.038   13.106  1.00 32.34 ? 202 ARG   A C   1 
ATOM   894  O  O   . ARG   A 1 109 ? 16.949  7.319   14.047  1.00 33.14 ? 202 ARG   A O   1 
ATOM   895  C  CB  . ARG   A 1 109 ? 16.236  10.079  14.533  1.00 35.34 ? 202 ARG   A CB  1 
ATOM   896  C  CG  . ARG   A 1 109 ? 16.551  11.549  14.789  1.00 37.40 ? 202 ARG   A CG  1 
ATOM   897  C  CD  . ARG   A 1 109 ? 15.716  12.097  15.929  1.00 39.19 ? 202 ARG   A CD  1 
ATOM   898  N  NE  . ARG   A 1 109 ? 16.101  11.518  17.208  1.00 40.46 ? 202 ARG   A NE  1 
ATOM   899  C  CZ  . ARG   A 1 109 ? 15.414  11.656  18.344  1.00 42.25 ? 202 ARG   A CZ  1 
ATOM   900  N  NH1 . ARG   A 1 109 ? 14.281  12.343  18.365  1.00 43.41 ? 202 ARG   A NH1 1 
ATOM   901  N  NH2 . ARG   A 1 109 ? 15.864  11.100  19.456  1.00 42.84 ? 202 ARG   A NH2 1 
ATOM   902  N  N   . VAL   A 1 110 ? 16.083  7.576   11.987  1.00 31.02 ? 203 VAL   A N   1 
ATOM   903  C  CA  . VAL   A 1 110 ? 15.852  6.124   11.695  1.00 29.36 ? 203 VAL   A CA  1 
ATOM   904  C  C   . VAL   A 1 110 ? 17.182  5.364   11.765  1.00 29.64 ? 203 VAL   A C   1 
ATOM   905  O  O   . VAL   A 1 110 ? 18.215  5.902   11.360  1.00 29.87 ? 203 VAL   A O   1 
ATOM   906  C  CB  . VAL   A 1 110 ? 15.149  5.919   10.341  1.00 28.46 ? 203 VAL   A CB  1 
ATOM   907  C  CG1 . VAL   A 1 110 ? 15.967  6.419   9.160   1.00 28.89 ? 203 VAL   A CG1 1 
ATOM   908  C  CG2 . VAL   A 1 110 ? 14.761  4.460   10.141  1.00 27.46 ? 203 VAL   A CG2 1 
ATOM   909  N  N   . GLU   A 1 111 ? 17.142  4.134   12.282  1.00 29.46 ? 204 GLU   A N   1 
ATOM   910  C  CA  . GLU   A 1 111 ? 18.332  3.264   12.447  1.00 30.46 ? 204 GLU   A CA  1 
ATOM   911  C  C   . GLU   A 1 111 ? 17.957  1.877   11.921  1.00 29.24 ? 204 GLU   A C   1 
ATOM   912  O  O   . GLU   A 1 111 ? 16.813  1.457   12.150  1.00 28.13 ? 204 GLU   A O   1 
ATOM   913  C  CB  . GLU   A 1 111 ? 18.766  3.303   13.917  1.00 31.65 ? 204 GLU   A CB  1 
ATOM   914  C  CG  . GLU   A 1 111 ? 19.620  2.128   14.372  1.00 33.08 ? 204 GLU   A CG  1 
ATOM   915  C  CD  . GLU   A 1 111 ? 19.863  2.076   15.870  1.00 34.79 ? 204 GLU   A CD  1 
ATOM   916  O  OE1 . GLU   A 1 111 ? 20.060  3.165   16.470  1.00 36.06 ? 204 GLU   A OE1 1 
ATOM   917  O  OE2 . GLU   A 1 111 ? 19.840  0.953   16.444  1.00 36.62 ? 204 GLU   A OE2 1 
ATOM   918  N  N   . TYR   A 1 112 ? 18.866  1.240   11.178  1.00 29.49 ? 205 TYR   A N   1 
ATOM   919  C  CA  . TYR   A 1 112 ? 18.640  -0.090  10.557  1.00 29.26 ? 205 TYR   A CA  1 
ATOM   920  C  C   . TYR   A 1 112 ? 19.622  -1.082  11.180  1.00 30.26 ? 205 TYR   A C   1 
ATOM   921  O  O   . TYR   A 1 112 ? 20.796  -0.732  11.433  1.00 32.09 ? 205 TYR   A O   1 
ATOM   922  C  CB  . TYR   A 1 112 ? 18.757  0.003   9.027   1.00 29.02 ? 205 TYR   A CB  1 
ATOM   923  C  CG  . TYR   A 1 112 ? 17.651  0.781   8.367   1.00 28.63 ? 205 TYR   A CG  1 
ATOM   924  C  CD1 . TYR   A 1 112 ? 17.746  2.152   8.204   1.00 29.04 ? 205 TYR   A CD1 1 
ATOM   925  C  CD2 . TYR   A 1 112 ? 16.505  0.156   7.907   1.00 27.44 ? 205 TYR   A CD2 1 
ATOM   926  C  CE1 . TYR   A 1 112 ? 16.734  2.879   7.604   1.00 28.62 ? 205 TYR   A CE1 1 
ATOM   927  C  CE2 . TYR   A 1 112 ? 15.489  0.862   7.295   1.00 27.35 ? 205 TYR   A CE2 1 
ATOM   928  C  CZ  . TYR   A 1 112 ? 15.600  2.234   7.155   1.00 28.01 ? 205 TYR   A CZ  1 
ATOM   929  O  OH  . TYR   A 1 112 ? 14.581  2.928   6.584   1.00 28.75 ? 205 TYR   A OH  1 
ATOM   930  N  N   . LEU   A 1 113 ? 19.153  -2.306  11.420  1.00 31.03 ? 206 LEU   A N   1 
ATOM   931  C  CA  . LEU   A 1 113 ? 19.967  -3.376  12.042  1.00 31.51 ? 206 LEU   A CA  1 
ATOM   932  C  C   . LEU   A 1 113 ? 19.932  -4.617  11.150  1.00 31.65 ? 206 LEU   A C   1 
ATOM   933  O  O   . LEU   A 1 113 ? 18.828  -5.028  10.745  1.00 30.75 ? 206 LEU   A O   1 
ATOM   934  C  CB  . LEU   A 1 113 ? 19.423  -3.666  13.443  1.00 31.55 ? 206 LEU   A CB  1 
ATOM   935  C  CG  . LEU   A 1 113 ? 20.040  -4.875  14.146  1.00 32.12 ? 206 LEU   A CG  1 
ATOM   936  C  CD1 . LEU   A 1 113 ? 21.529  -4.667  14.367  1.00 33.46 ? 206 LEU   A CD1 1 
ATOM   937  C  CD2 . LEU   A 1 113 ? 19.339  -5.184  15.459  1.00 32.77 ? 206 LEU   A CD2 1 
ATOM   938  N  N   . ASP   A 1 114 ? 21.111  -5.121  10.793  1.00 32.94 ? 207 ASP   A N   1 
ATOM   939  C  CA  . ASP   A 1 114 ? 21.344  -6.533  10.391  1.00 34.70 ? 207 ASP   A CA  1 
ATOM   940  C  C   . ASP   A 1 114 ? 21.841  -7.246  11.649  1.00 36.10 ? 207 ASP   A C   1 
ATOM   941  O  O   . ASP   A 1 114 ? 22.970  -6.936  12.091  1.00 38.62 ? 207 ASP   A O   1 
ATOM   942  C  CB  . ASP   A 1 114 ? 22.376  -6.639  9.266   1.00 35.18 ? 207 ASP   A CB  1 
ATOM   943  C  CG  . ASP   A 1 114 ? 21.973  -6.007  7.950   1.00 34.57 ? 207 ASP   A CG  1 
ATOM   944  O  OD1 . ASP   A 1 114 ? 20.811  -5.622  7.813   1.00 34.12 ? 207 ASP   A OD1 1 
ATOM   945  O  OD2 . ASP   A 1 114 ? 22.841  -5.858  7.083   1.00 36.60 ? 207 ASP   A OD2 1 
ATOM   946  N  N   . ASP   A 1 115 ? 20.996  -8.071  12.261  1.00 36.88 ? 208 ASP   A N   1 
ATOM   947  C  CA  . ASP   A 1 115 ? 21.294  -8.726  13.559  1.00 37.83 ? 208 ASP   A CA  1 
ATOM   948  C  C   . ASP   A 1 115 ? 22.494  -9.647  13.360  1.00 39.34 ? 208 ASP   A C   1 
ATOM   949  O  O   . ASP   A 1 115 ? 22.448  -10.484 12.432  1.00 39.65 ? 208 ASP   A O   1 
ATOM   950  C  CB  . ASP   A 1 115 ? 20.057  -9.435  14.120  1.00 37.75 ? 208 ASP   A CB  1 
ATOM   951  C  CG  . ASP   A 1 115 ? 20.249  -9.979  15.520  1.00 38.88 ? 208 ASP   A CG  1 
ATOM   952  O  OD1 . ASP   A 1 115 ? 21.062  -10.908 15.677  1.00 40.13 ? 208 ASP   A OD1 1 
ATOM   953  O  OD2 . ASP   A 1 115 ? 19.584  -9.468  16.440  1.00 39.47 ? 208 ASP   A OD2 1 
ATOM   954  N  N   . ARG   A 1 116 ? 23.526  -9.480  14.187  1.00 40.13 ? 209 ARG   A N   1 
ATOM   955  C  CA  . ARG   A 1 116 ? 24.804  -10.234 14.076  1.00 42.18 ? 209 ARG   A CA  1 
ATOM   956  C  C   . ARG   A 1 116 ? 24.562  -11.748 14.187  1.00 43.43 ? 209 ARG   A C   1 
ATOM   957  O  O   . ARG   A 1 116 ? 25.350  -12.484 13.591  1.00 44.13 ? 209 ARG   A O   1 
ATOM   958  C  CB  . ARG   A 1 116 ? 25.841  -9.742  15.093  1.00 42.87 ? 209 ARG   A CB  1 
ATOM   959  C  CG  . ARG   A 1 116 ? 25.374  -9.654  16.540  1.00 42.88 ? 209 ARG   A CG  1 
ATOM   960  C  CD  . ARG   A 1 116 ? 26.531  -9.289  17.463  1.00 44.53 ? 209 ARG   A CD  1 
ATOM   961  N  NE  . ARG   A 1 116 ? 26.097  -8.490  18.604  1.00 44.46 ? 209 ARG   A NE  1 
ATOM   962  C  CZ  . ARG   A 1 116 ? 26.856  -8.178  19.647  1.00 45.64 ? 209 ARG   A CZ  1 
ATOM   963  N  NH1 . ARG   A 1 116 ? 28.107  -8.603  19.724  1.00 48.04 ? 209 ARG   A NH1 1 
ATOM   964  N  NH2 . ARG   A 1 116 ? 26.359  -7.445  20.625  1.00 45.56 ? 209 ARG   A NH2 1 
ATOM   965  N  N   . ASN   A 1 117 ? 23.528  -12.201 14.904  1.00 43.78 ? 210 ASN   A N   1 
ATOM   966  C  CA  . ASN   A 1 117 ? 23.331  -13.650 15.218  1.00 44.74 ? 210 ASN   A CA  1 
ATOM   967  C  C   . ASN   A 1 117 ? 22.129  -14.247 14.473  1.00 44.53 ? 210 ASN   A C   1 
ATOM   968  O  O   . ASN   A 1 117 ? 22.243  -15.415 14.057  1.00 46.26 ? 210 ASN   A O   1 
ATOM   969  C  CB  . ASN   A 1 117 ? 23.207  -13.895 16.721  1.00 44.90 ? 210 ASN   A CB  1 
ATOM   970  C  CG  . ASN   A 1 117 ? 24.287  -13.195 17.514  1.00 45.71 ? 210 ASN   A CG  1 
ATOM   971  O  OD1 . ASN   A 1 117 ? 25.476  -13.515 17.399  1.00 45.58 ? 210 ASN   A OD1 1 
ATOM   972  N  ND2 . ASN   A 1 117 ? 23.868  -12.243 18.331  1.00 45.18 ? 210 ASN   A ND2 1 
ATOM   973  N  N   . THR   A 1 118 ? 21.006  -13.530 14.352  1.00 43.60 ? 211 THR   A N   1 
ATOM   974  C  CA  . THR   A 1 118 ? 19.777  -14.048 13.682  1.00 42.97 ? 211 THR   A CA  1 
ATOM   975  C  C   . THR   A 1 118 ? 19.807  -13.701 12.192  1.00 41.11 ? 211 THR   A C   1 
ATOM   976  O  O   . THR   A 1 118 ? 19.045  -14.315 11.444  1.00 41.62 ? 211 THR   A O   1 
ATOM   977  C  CB  . THR   A 1 118 ? 18.483  -13.508 14.307  1.00 42.63 ? 211 THR   A CB  1 
ATOM   978  O  OG1 . THR   A 1 118 ? 18.421  -12.096 14.105  1.00 42.12 ? 211 THR   A OG1 1 
ATOM   979  C  CG2 . THR   A 1 118 ? 18.374  -13.815 15.784  1.00 44.32 ? 211 THR   A CG2 1 
ATOM   980  N  N   . PHE   A 1 119 ? 20.594  -12.698 11.797  1.00 39.22 ? 212 PHE   A N   1 
ATOM   981  C  CA  . PHE   A 1 119 ? 20.707  -12.184 10.405  1.00 37.59 ? 212 PHE   A CA  1 
ATOM   982  C  C   . PHE   A 1 119 ? 19.390  -11.516 9.985   1.00 35.14 ? 212 PHE   A C   1 
ATOM   983  O  O   . PHE   A 1 119 ? 19.250  -11.134 8.802   1.00 33.62 ? 212 PHE   A O   1 
ATOM   984  C  CB  . PHE   A 1 119 ? 21.101  -13.295 9.429   1.00 39.30 ? 212 PHE   A CB  1 
ATOM   985  C  CG  . PHE   A 1 119 ? 22.317  -14.095 9.837   1.00 41.45 ? 212 PHE   A CG  1 
ATOM   986  C  CD1 . PHE   A 1 119 ? 23.582  -13.524 9.842   1.00 42.44 ? 212 PHE   A CD1 1 
ATOM   987  C  CD2 . PHE   A 1 119 ? 22.196  -15.420 10.232  1.00 42.96 ? 212 PHE   A CD2 1 
ATOM   988  C  CE1 . PHE   A 1 119 ? 24.693  -14.258 10.232  1.00 43.93 ? 212 PHE   A CE1 1 
ATOM   989  C  CE2 . PHE   A 1 119 ? 23.310  -16.156 10.605  1.00 44.43 ? 212 PHE   A CE2 1 
ATOM   990  C  CZ  . PHE   A 1 119 ? 24.555  -15.576 10.602  1.00 44.86 ? 212 PHE   A CZ  1 
ATOM   991  N  N   . ARG   A 1 120 ? 18.447  -11.361 10.917  1.00 33.23 ? 213 ARG   A N   1 
ATOM   992  C  CA  . ARG   A 1 120 ? 17.134  -10.732 10.638  1.00 31.96 ? 213 ARG   A CA  1 
ATOM   993  C  C   . ARG   A 1 120 ? 17.350  -9.221  10.553  1.00 30.92 ? 213 ARG   A C   1 
ATOM   994  O  O   . ARG   A 1 120 ? 18.261  -8.686  11.210  1.00 31.39 ? 213 ARG   A O   1 
ATOM   995  C  CB  . ARG   A 1 120 ? 16.096  -11.129 11.694  1.00 31.55 ? 213 ARG   A CB  1 
ATOM   996  C  CG  . ARG   A 1 120 ? 15.799  -12.620 11.664  1.00 32.30 ? 213 ARG   A CG  1 
ATOM   997  C  CD  . ARG   A 1 120 ? 14.636  -13.040 12.503  1.00 31.98 ? 213 ARG   A CD  1 
ATOM   998  N  NE  . ARG   A 1 120 ? 14.393  -14.474 12.405  1.00 34.25 ? 213 ARG   A NE  1 
ATOM   999  C  CZ  . ARG   A 1 120 ? 13.640  -15.077 11.499  1.00 33.47 ? 213 ARG   A CZ  1 
ATOM   1000 N  NH1 . ARG   A 1 120 ? 13.041  -14.378 10.553  1.00 33.31 ? 213 ARG   A NH1 1 
ATOM   1001 N  NH2 . ARG   A 1 120 ? 13.497  -16.390 11.535  1.00 34.90 ? 213 ARG   A NH2 1 
ATOM   1002 N  N   . HIS   A 1 121 ? 16.542  -8.580  9.720   1.00 30.25 ? 214 HIS   A N   1 
ATOM   1003 C  CA  . HIS   A 1 121 ? 16.545  -7.119  9.466   1.00 29.22 ? 214 HIS   A CA  1 
ATOM   1004 C  C   . HIS   A 1 121 ? 15.492  -6.438  10.335  1.00 28.21 ? 214 HIS   A C   1 
ATOM   1005 O  O   . HIS   A 1 121 ? 14.390  -6.997  10.513  1.00 28.77 ? 214 HIS   A O   1 
ATOM   1006 C  CB  . HIS   A 1 121 ? 16.258  -6.861  7.987   1.00 29.31 ? 214 HIS   A CB  1 
ATOM   1007 C  CG  . HIS   A 1 121 ? 17.234  -7.492  7.053   1.00 29.76 ? 214 HIS   A CG  1 
ATOM   1008 N  ND1 . HIS   A 1 121 ? 16.946  -7.684  5.717   1.00 29.69 ? 214 HIS   A ND1 1 
ATOM   1009 C  CD2 . HIS   A 1 121 ? 18.498  -7.933  7.235   1.00 31.06 ? 214 HIS   A CD2 1 
ATOM   1010 C  CE1 . HIS   A 1 121 ? 17.987  -8.217  5.112   1.00 30.73 ? 214 HIS   A CE1 1 
ATOM   1011 N  NE2 . HIS   A 1 121 ? 18.949  -8.376  6.026   1.00 31.32 ? 214 HIS   A NE2 1 
ATOM   1012 N  N   . SER   A 1 122 ? 15.777  -5.234  10.812  1.00 27.49 ? 215 SER   A N   1 
ATOM   1013 C  CA  . SER   A 1 122 ? 14.761  -4.416  11.502  1.00 26.26 ? 215 SER   A CA  1 
ATOM   1014 C  C   . SER   A 1 122 ? 15.103  -2.931  11.361  1.00 26.03 ? 215 SER   A C   1 
ATOM   1015 O  O   . SER   A 1 122 ? 16.272  -2.605  11.042  1.00 26.06 ? 215 SER   A O   1 
ATOM   1016 C  CB  . SER   A 1 122 ? 14.596  -4.852  12.919  1.00 26.07 ? 215 SER   A CB  1 
ATOM   1017 O  OG  . SER   A 1 122 ? 15.808  -4.712  13.635  1.00 27.01 ? 215 SER   A OG  1 
ATOM   1018 N  N   . VAL   A 1 123 ? 14.092  -2.090  11.531  1.00 24.95 ? 216 VAL   A N   1 
ATOM   1019 C  CA  . VAL   A 1 123 ? 14.199  -0.605  11.435  1.00 25.40 ? 216 VAL   A CA  1 
ATOM   1020 C  C   . VAL   A 1 123 ? 13.645  -0.043  12.739  1.00 25.94 ? 216 VAL   A C   1 
ATOM   1021 O  O   . VAL   A 1 123 ? 12.584  -0.515  13.204  1.00 25.84 ? 216 VAL   A O   1 
ATOM   1022 C  CB  . VAL   A 1 123 ? 13.526  -0.047  10.161  1.00 25.04 ? 216 VAL   A CB  1 
ATOM   1023 C  CG1 . VAL   A 1 123 ? 12.071  -0.463  10.022  1.00 24.73 ? 216 VAL   A CG1 1 
ATOM   1024 C  CG2 . VAL   A 1 123 ? 13.688  1.472   10.036  1.00 25.08 ? 216 VAL   A CG2 1 
ATOM   1025 N  N   A VAL   A 1 124 ? 14.363  0.909   13.343  0.45 26.81 ? 217 VAL   A N   1 
ATOM   1026 N  N   B VAL   A 1 124 ? 14.359  0.912   13.343  0.55 26.86 ? 217 VAL   A N   1 
ATOM   1027 C  CA  A VAL   A 1 124 ? 14.037  1.444   14.696  0.45 26.96 ? 217 VAL   A CA  1 
ATOM   1028 C  CA  B VAL   A 1 124 ? 14.044  1.445   14.702  0.55 26.98 ? 217 VAL   A CA  1 
ATOM   1029 C  C   A VAL   A 1 124 ? 14.028  2.977   14.625  0.45 27.54 ? 217 VAL   A C   1 
ATOM   1030 C  C   B VAL   A 1 124 ? 14.026  2.977   14.621  0.55 27.53 ? 217 VAL   A C   1 
ATOM   1031 O  O   A VAL   A 1 124 ? 14.886  3.541   13.926  0.45 27.52 ? 217 VAL   A O   1 
ATOM   1032 O  O   B VAL   A 1 124 ? 14.884  3.547   13.921  0.55 27.41 ? 217 VAL   A O   1 
ATOM   1033 C  CB  A VAL   A 1 124 ? 14.989  0.881   15.773  0.45 27.45 ? 217 VAL   A CB  1 
ATOM   1034 C  CB  B VAL   A 1 124 ? 15.050  0.922   15.748  0.55 27.50 ? 217 VAL   A CB  1 
ATOM   1035 C  CG1 A VAL   A 1 124 ? 16.442  1.180   15.481  0.45 28.15 ? 217 VAL   A CG1 1 
ATOM   1036 C  CG1 B VAL   A 1 124 ? 14.691  1.272   17.184  0.55 27.79 ? 217 VAL   A CG1 1 
ATOM   1037 C  CG2 A VAL   A 1 124 ? 14.619  1.364   17.164  0.45 27.78 ? 217 VAL   A CG2 1 
ATOM   1038 C  CG2 B VAL   A 1 124 ? 15.296  -0.566  15.608  0.55 27.57 ? 217 VAL   A CG2 1 
ATOM   1039 N  N   . VAL   A 1 125 ? 13.031  3.606   15.258  1.00 27.66 ? 218 VAL   A N   1 
ATOM   1040 C  CA  . VAL   A 1 125 ? 12.927  5.091   15.388  1.00 28.99 ? 218 VAL   A CA  1 
ATOM   1041 C  C   . VAL   A 1 125 ? 12.717  5.396   16.865  1.00 29.53 ? 218 VAL   A C   1 
ATOM   1042 O  O   . VAL   A 1 125 ? 12.176  4.565   17.603  1.00 29.82 ? 218 VAL   A O   1 
ATOM   1043 C  CB  . VAL   A 1 125 ? 11.798  5.677   14.513  1.00 29.04 ? 218 VAL   A CB  1 
ATOM   1044 C  CG1 . VAL   A 1 125 ? 12.157  5.617   13.044  1.00 29.43 ? 218 VAL   A CG1 1 
ATOM   1045 C  CG2 . VAL   A 1 125 ? 10.451  5.000   14.749  1.00 28.56 ? 218 VAL   A CG2 1 
ATOM   1046 N  N   . PRO   A 1 126 ? 13.128  6.596   17.332  1.00 30.03 ? 219 PRO   A N   1 
ATOM   1047 C  CA  . PRO   A 1 126 ? 12.741  7.065   18.653  1.00 30.87 ? 219 PRO   A CA  1 
ATOM   1048 C  C   . PRO   A 1 126 ? 11.214  7.185   18.736  1.00 30.74 ? 219 PRO   A C   1 
ATOM   1049 O  O   . PRO   A 1 126 ? 10.581  7.549   17.771  1.00 29.40 ? 219 PRO   A O   1 
ATOM   1050 C  CB  . PRO   A 1 126 ? 13.397  8.448   18.837  1.00 31.67 ? 219 PRO   A CB  1 
ATOM   1051 C  CG  . PRO   A 1 126 ? 14.135  8.755   17.541  1.00 31.40 ? 219 PRO   A CG  1 
ATOM   1052 C  CD  . PRO   A 1 126 ? 13.967  7.566   16.613  1.00 30.74 ? 219 PRO   A CD  1 
ATOM   1053 N  N   . TYR   A 1 127 ? 10.663  6.833   19.896  1.00 31.83 ? 220 TYR   A N   1 
ATOM   1054 C  CA  . TYR   A 1 127 ? 9.253   7.109   20.255  1.00 32.37 ? 220 TYR   A CA  1 
ATOM   1055 C  C   . TYR   A 1 127 ? 9.129   8.620   20.488  1.00 34.25 ? 220 TYR   A C   1 
ATOM   1056 O  O   . TYR   A 1 127 ? 9.954   9.171   21.238  1.00 35.00 ? 220 TYR   A O   1 
ATOM   1057 C  CB  . TYR   A 1 127 ? 8.829   6.320   21.494  1.00 32.33 ? 220 TYR   A CB  1 
ATOM   1058 C  CG  . TYR   A 1 127 ? 7.446   6.714   21.946  1.00 32.66 ? 220 TYR   A CG  1 
ATOM   1059 C  CD1 . TYR   A 1 127 ? 6.334   6.136   21.368  1.00 32.08 ? 220 TYR   A CD1 1 
ATOM   1060 C  CD2 . TYR   A 1 127 ? 7.249   7.727   22.877  1.00 33.82 ? 220 TYR   A CD2 1 
ATOM   1061 C  CE1 . TYR   A 1 127 ? 5.055   6.508   21.740  1.00 32.57 ? 220 TYR   A CE1 1 
ATOM   1062 C  CE2 . TYR   A 1 127 ? 5.975   8.116   23.257  1.00 34.46 ? 220 TYR   A CE2 1 
ATOM   1063 C  CZ  . TYR   A 1 127 ? 4.875   7.507   22.673  1.00 33.65 ? 220 TYR   A CZ  1 
ATOM   1064 O  OH  . TYR   A 1 127 ? 3.609   7.868   23.020  1.00 34.62 ? 220 TYR   A OH  1 
ATOM   1065 N  N   . GLU   A 1 128 ? 8.173   9.269   19.830  1.00 34.71 ? 221 GLU   A N   1 
ATOM   1066 C  CA  . GLU   A 1 128 ? 7.757   10.662  20.152  1.00 36.99 ? 221 GLU   A CA  1 
ATOM   1067 C  C   . GLU   A 1 128 ? 6.299   10.615  20.577  1.00 36.69 ? 221 GLU   A C   1 
ATOM   1068 O  O   . GLU   A 1 128 ? 5.506   9.862   20.016  1.00 35.96 ? 221 GLU   A O   1 
ATOM   1069 C  CB  . GLU   A 1 128 ? 7.993   11.611  18.974  1.00 38.17 ? 221 GLU   A CB  1 
ATOM   1070 C  CG  . GLU   A 1 128 ? 9.474   11.903  18.775  1.00 39.21 ? 221 GLU   A CG  1 
ATOM   1071 C  CD  . GLU   A 1 128 ? 10.198  12.413  20.019  1.00 41.84 ? 221 GLU   A CD  1 
ATOM   1072 O  OE1 . GLU   A 1 128 ? 9.569   13.159  20.806  1.00 42.66 ? 221 GLU   A OE1 1 
ATOM   1073 O  OE2 . GLU   A 1 128 ? 11.398  12.076  20.212  1.00 42.37 ? 221 GLU   A OE2 1 
ATOM   1074 N  N   . PRO   A 1 129 ? 5.905   11.402  21.598  1.00 37.29 ? 222 PRO   A N   1 
ATOM   1075 C  CA  . PRO   A 1 129 ? 4.518   11.425  22.050  1.00 37.62 ? 222 PRO   A CA  1 
ATOM   1076 C  C   . PRO   A 1 129 ? 3.624   12.049  20.977  1.00 36.79 ? 222 PRO   A C   1 
ATOM   1077 O  O   . PRO   A 1 129 ? 4.126   12.687  20.058  1.00 35.99 ? 222 PRO   A O   1 
ATOM   1078 C  CB  . PRO   A 1 129 ? 4.560   12.258  23.339  1.00 39.45 ? 222 PRO   A CB  1 
ATOM   1079 C  CG  . PRO   A 1 129 ? 5.803   13.102  23.223  1.00 40.16 ? 222 PRO   A CG  1 
ATOM   1080 C  CD  . PRO   A 1 129 ? 6.761   12.316  22.364  1.00 38.68 ? 222 PRO   A CD  1 
ATOM   1081 N  N   . PRO   A 1 130 ? 2.290   11.858  21.055  1.00 36.84 ? 223 PRO   A N   1 
ATOM   1082 C  CA  . PRO   A 1 130 ? 1.364   12.337  20.029  1.00 37.07 ? 223 PRO   A CA  1 
ATOM   1083 C  C   . PRO   A 1 130 ? 1.544   13.827  19.740  1.00 39.12 ? 223 PRO   A C   1 
ATOM   1084 O  O   . PRO   A 1 130 ? 1.897   14.529  20.634  1.00 39.22 ? 223 PRO   A O   1 
ATOM   1085 C  CB  . PRO   A 1 130 ? -0.040  12.060  20.614  1.00 37.29 ? 223 PRO   A CB  1 
ATOM   1086 C  CG  . PRO   A 1 130 ? 0.216   10.882  21.544  1.00 36.87 ? 223 PRO   A CG  1 
ATOM   1087 C  CD  . PRO   A 1 130 ? 1.591   11.138  22.120  1.00 37.05 ? 223 PRO   A CD  1 
ATOM   1088 N  N   . GLU   A 1 131 ? 1.328   14.241  18.488  1.00 40.44 ? 224 GLU   A N   1 
ATOM   1089 C  CA  . GLU   A 1 131 ? 1.335   15.673  18.089  1.00 42.70 ? 224 GLU   A CA  1 
ATOM   1090 C  C   . GLU   A 1 131 ? 0.048   16.314  18.608  1.00 43.76 ? 224 GLU   A C   1 
ATOM   1091 O  O   . GLU   A 1 131 ? -0.911  15.571  18.894  1.00 43.77 ? 224 GLU   A O   1 
ATOM   1092 C  CB  . GLU   A 1 131 ? 1.475   15.808  16.568  1.00 43.21 ? 224 GLU   A CB  1 
ATOM   1093 C  CG  . GLU   A 1 131 ? 2.891   15.543  16.090  1.00 42.78 ? 224 GLU   A CG  1 
ATOM   1094 C  CD  . GLU   A 1 131 ? 3.965   16.251  16.896  1.00 44.18 ? 224 GLU   A CD  1 
ATOM   1095 O  OE1 . GLU   A 1 131 ? 4.927   15.576  17.317  1.00 43.43 ? 224 GLU   A OE1 1 
ATOM   1096 O  OE2 . GLU   A 1 131 ? 3.850   17.489  17.100  1.00 47.05 ? 224 GLU   A OE2 1 
ATOM   1097 N  N   . VAL   A 1 132 ? 0.048   17.646  18.693  1.00 44.62 ? 225 VAL   A N   1 
ATOM   1098 C  CA  . VAL   A 1 132 ? -1.141  18.485  19.018  1.00 46.33 ? 225 VAL   A CA  1 
ATOM   1099 C  C   . VAL   A 1 132 ? -2.268  18.101  18.051  1.00 45.55 ? 225 VAL   A C   1 
ATOM   1100 O  O   . VAL   A 1 132 ? -2.080  18.254  16.822  1.00 44.92 ? 225 VAL   A O   1 
ATOM   1101 C  CB  . VAL   A 1 132 ? -0.818  19.993  18.937  1.00 47.96 ? 225 VAL   A CB  1 
ATOM   1102 C  CG1 . VAL   A 1 132 ? -2.060  20.843  19.155  1.00 49.78 ? 225 VAL   A CG1 1 
ATOM   1103 C  CG2 . VAL   A 1 132 ? 0.288   20.396  19.903  1.00 48.55 ? 225 VAL   A CG2 1 
ATOM   1104 N  N   . GLY   A 1 133 ? -3.388  17.620  18.596  1.00 45.50 ? 226 GLY   A N   1 
ATOM   1105 C  CA  . GLY   A 1 133 ? -4.555  17.135  17.831  1.00 45.14 ? 226 GLY   A CA  1 
ATOM   1106 C  C   . GLY   A 1 133 ? -4.767  15.643  18.039  1.00 43.93 ? 226 GLY   A C   1 
ATOM   1107 O  O   . GLY   A 1 133 ? -5.936  15.230  18.252  1.00 45.66 ? 226 GLY   A O   1 
ATOM   1108 N  N   . SER   A 1 134 ? -3.686  14.859  17.992  1.00 42.45 ? 227 SER   A N   1 
ATOM   1109 C  CA  . SER   A 1 134 ? -3.724  13.372  17.958  1.00 40.36 ? 227 SER   A CA  1 
ATOM   1110 C  C   . SER   A 1 134 ? -3.657  12.800  19.382  1.00 40.69 ? 227 SER   A C   1 
ATOM   1111 O  O   . SER   A 1 134 ? -3.088  13.468  20.258  1.00 41.87 ? 227 SER   A O   1 
ATOM   1112 C  CB  . SER   A 1 134 ? -2.627  12.838  17.085  1.00 39.16 ? 227 SER   A CB  1 
ATOM   1113 O  OG  . SER   A 1 134 ? -2.761  11.419  16.940  1.00 37.46 ? 227 SER   A OG  1 
ATOM   1114 N  N   . ASP   A 1 135 ? -4.206  11.599  19.565  1.00 39.56 ? 228 ASP   A N   1 
ATOM   1115 C  CA  . ASP   A 1 135 ? -4.115  10.784  20.803  1.00 40.39 ? 228 ASP   A CA  1 
ATOM   1116 C  C   . ASP   A 1 135 ? -3.217  9.558   20.583  1.00 38.94 ? 228 ASP   A C   1 
ATOM   1117 O  O   . ASP   A 1 135 ? -3.181  8.674   21.453  1.00 38.96 ? 228 ASP   A O   1 
ATOM   1118 C  CB  . ASP   A 1 135 ? -5.527  10.375  21.232  1.00 41.43 ? 228 ASP   A CB  1 
ATOM   1119 C  CG  . ASP   A 1 135 ? -6.334  11.553  21.744  1.00 43.22 ? 228 ASP   A CG  1 
ATOM   1120 O  OD1 . ASP   A 1 135 ? -5.747  12.398  22.450  1.00 44.61 ? 228 ASP   A OD1 1 
ATOM   1121 O  OD2 . ASP   A 1 135 ? -7.536  11.637  21.414  1.00 43.62 ? 228 ASP   A OD2 1 
ATOM   1122 N  N   . CYS   A 1 136 ? -2.498  9.511   19.467  1.00 37.88 ? 229 CYS   A N   1 
ATOM   1123 C  CA  . CYS   A 1 136 ? -1.610  8.397   19.057  1.00 37.55 ? 229 CYS   A CA  1 
ATOM   1124 C  C   . CYS   A 1 136 ? -0.394  8.949   18.312  1.00 36.97 ? 229 CYS   A C   1 
ATOM   1125 O  O   . CYS   A 1 136 ? -0.446  10.105  17.839  1.00 39.93 ? 229 CYS   A O   1 
ATOM   1126 C  CB  . CYS   A 1 136 ? -2.364  7.429   18.154  1.00 36.26 ? 229 CYS   A CB  1 
ATOM   1127 S  SG  . CYS   A 1 136 ? -2.905  8.148   16.573  1.00 36.72 ? 229 CYS   A SG  1 
ATOM   1128 N  N   . THR   A 1 137 ? 0.657   8.140   18.206  1.00 35.34 ? 230 THR   A N   1 
ATOM   1129 C  CA  . THR   A 1 137 ? 1.875   8.460   17.421  1.00 34.32 ? 230 THR   A CA  1 
ATOM   1130 C  C   . THR   A 1 137 ? 1.832   7.672   16.115  1.00 33.07 ? 230 THR   A C   1 
ATOM   1131 O  O   . THR   A 1 137 ? 1.585   6.448   16.181  1.00 33.18 ? 230 THR   A O   1 
ATOM   1132 C  CB  . THR   A 1 137 ? 3.135   8.189   18.245  1.00 33.85 ? 230 THR   A CB  1 
ATOM   1133 O  OG1 . THR   A 1 137 ? 3.038   9.093   19.342  1.00 34.84 ? 230 THR   A OG1 1 
ATOM   1134 C  CG2 . THR   A 1 137 ? 4.426   8.425   17.485  1.00 33.03 ? 230 THR   A CG2 1 
ATOM   1135 N  N   . THR   A 1 138 ? 2.021   8.355   14.988  1.00 32.64 ? 231 THR   A N   1 
ATOM   1136 C  CA  . THR   A 1 138 ? 2.010   7.744   13.637  1.00 31.85 ? 231 THR   A CA  1 
ATOM   1137 C  C   . THR   A 1 138 ? 3.457   7.565   13.173  1.00 31.32 ? 231 THR   A C   1 
ATOM   1138 O  O   . THR   A 1 138 ? 4.224   8.551   13.241  1.00 31.83 ? 231 THR   A O   1 
ATOM   1139 C  CB  . THR   A 1 138 ? 1.155   8.540   12.646  1.00 32.17 ? 231 THR   A CB  1 
ATOM   1140 O  OG1 . THR   A 1 138 ? -0.182  8.622   13.147  1.00 32.62 ? 231 THR   A OG1 1 
ATOM   1141 C  CG2 . THR   A 1 138 ? 1.102   7.913   11.278  1.00 31.37 ? 231 THR   A CG2 1 
ATOM   1142 N  N   . ILE   A 1 139 ? 3.794   6.340   12.749  1.00 29.80 ? 232 ILE   A N   1 
ATOM   1143 C  CA  . ILE   A 1 139 ? 5.026   6.012   11.975  1.00 29.45 ? 232 ILE   A CA  1 
ATOM   1144 C  C   . ILE   A 1 139 ? 4.614   5.701   10.538  1.00 28.98 ? 232 ILE   A C   1 
ATOM   1145 O  O   . ILE   A 1 139 ? 3.610   4.982   10.340  1.00 28.55 ? 232 ILE   A O   1 
ATOM   1146 C  CB  . ILE   A 1 139 ? 5.797   4.851   12.621  1.00 29.00 ? 232 ILE   A CB  1 
ATOM   1147 C  CG1 . ILE   A 1 139 ? 6.305   5.223   14.013  1.00 29.72 ? 232 ILE   A CG1 1 
ATOM   1148 C  CG2 . ILE   A 1 139 ? 6.946   4.396   11.716  1.00 28.81 ? 232 ILE   A CG2 1 
ATOM   1149 C  CD1 . ILE   A 1 139 ? 6.764   4.038   14.811  1.00 29.56 ? 232 ILE   A CD1 1 
ATOM   1150 N  N   . HIS   A 1 140 ? 5.370   6.228   9.580   1.00 29.68 ? 233 HIS   A N   1 
ATOM   1151 C  CA  . HIS   A 1 140 ? 5.190   6.011   8.128   1.00 29.15 ? 233 HIS   A CA  1 
ATOM   1152 C  C   . HIS   A 1 140 ? 6.166   4.929   7.660   1.00 28.21 ? 233 HIS   A C   1 
ATOM   1153 O  O   . HIS   A 1 140 ? 7.340   5.237   7.459   1.00 29.81 ? 233 HIS   A O   1 
ATOM   1154 C  CB  . HIS   A 1 140 ? 5.341   7.347   7.388   1.00 30.11 ? 233 HIS   A CB  1 
ATOM   1155 C  CG  . HIS   A 1 140 ? 4.193   8.273   7.609   1.00 30.74 ? 233 HIS   A CG  1 
ATOM   1156 N  ND1 . HIS   A 1 140 ? 4.261   9.623   7.299   1.00 32.05 ? 233 HIS   A ND1 1 
ATOM   1157 C  CD2 . HIS   A 1 140 ? 2.955   8.055   8.095   1.00 31.08 ? 233 HIS   A CD2 1 
ATOM   1158 C  CE1 . HIS   A 1 140 ? 3.119   10.199  7.597   1.00 32.74 ? 233 HIS   A CE1 1 
ATOM   1159 N  NE2 . HIS   A 1 140 ? 2.303   9.261   8.096   1.00 32.20 ? 233 HIS   A NE2 1 
ATOM   1160 N  N   . TYR   A 1 141 ? 5.695   3.684   7.546   1.00 27.26 ? 234 TYR   A N   1 
ATOM   1161 C  CA  . TYR   A 1 141 ? 6.459   2.550   6.970   1.00 25.69 ? 234 TYR   A CA  1 
ATOM   1162 C  C   . TYR   A 1 141 ? 6.332   2.561   5.435   1.00 26.32 ? 234 TYR   A C   1 
ATOM   1163 O  O   . TYR   A 1 141 ? 5.273   2.971   4.897   1.00 26.02 ? 234 TYR   A O   1 
ATOM   1164 C  CB  . TYR   A 1 141 ? 6.002   1.246   7.631   1.00 24.59 ? 234 TYR   A CB  1 
ATOM   1165 C  CG  . TYR   A 1 141 ? 6.385   1.142   9.084   1.00 24.20 ? 234 TYR   A CG  1 
ATOM   1166 C  CD1 . TYR   A 1 141 ? 7.713   0.984   9.457   1.00 23.93 ? 234 TYR   A CD1 1 
ATOM   1167 C  CD2 . TYR   A 1 141 ? 5.438   1.268   10.098  1.00 23.82 ? 234 TYR   A CD2 1 
ATOM   1168 C  CE1 . TYR   A 1 141 ? 8.087   0.911   10.790  1.00 23.99 ? 234 TYR   A CE1 1 
ATOM   1169 C  CE2 . TYR   A 1 141 ? 5.799   1.205   11.438  1.00 24.06 ? 234 TYR   A CE2 1 
ATOM   1170 C  CZ  . TYR   A 1 141 ? 7.134   1.020   11.780  1.00 23.95 ? 234 TYR   A CZ  1 
ATOM   1171 O  OH  . TYR   A 1 141 ? 7.518   0.970   13.091  1.00 24.45 ? 234 TYR   A OH  1 
ATOM   1172 N  N   . ASN   A 1 142 ? 7.383   2.101   4.747   1.00 26.29 ? 235 ASN   A N   1 
ATOM   1173 C  CA  . ASN   A 1 142 ? 7.382   1.741   3.306   1.00 26.64 ? 235 ASN   A CA  1 
ATOM   1174 C  C   . ASN   A 1 142 ? 7.788   0.271   3.180   1.00 26.94 ? 235 ASN   A C   1 
ATOM   1175 O  O   . ASN   A 1 142 ? 8.804   -0.098  3.784   1.00 27.11 ? 235 ASN   A O   1 
ATOM   1176 C  CB  . ASN   A 1 142 ? 8.350   2.551   2.452   1.00 27.12 ? 235 ASN   A CB  1 
ATOM   1177 C  CG  . ASN   A 1 142 ? 8.116   4.047   2.506   1.00 27.79 ? 235 ASN   A CG  1 
ATOM   1178 O  OD1 . ASN   A 1 142 ? 9.004   4.810   2.141   1.00 28.94 ? 235 ASN   A OD1 1 
ATOM   1179 N  ND2 . ASN   A 1 142 ? 6.947   4.475   2.947   1.00 26.94 ? 235 ASN   A ND2 1 
ATOM   1180 N  N   . TYR   A 1 143 ? 7.014   -0.522  2.442   1.00 27.05 ? 236 TYR   A N   1 
ATOM   1181 C  CA  . TYR   A 1 143 ? 7.362   -1.917  2.079   1.00 28.46 ? 236 TYR   A CA  1 
ATOM   1182 C  C   . TYR   A 1 143 ? 7.918   -1.911  0.653   1.00 29.35 ? 236 TYR   A C   1 
ATOM   1183 O  O   . TYR   A 1 143 ? 7.262   -1.396  -0.270  1.00 31.03 ? 236 TYR   A O   1 
ATOM   1184 C  CB  . TYR   A 1 143 ? 6.161   -2.826  2.319   1.00 28.24 ? 236 TYR   A CB  1 
ATOM   1185 C  CG  . TYR   A 1 143 ? 5.778   -2.959  3.769   1.00 28.37 ? 236 TYR   A CG  1 
ATOM   1186 C  CD1 . TYR   A 1 143 ? 5.006   -1.997  4.405   1.00 28.47 ? 236 TYR   A CD1 1 
ATOM   1187 C  CD2 . TYR   A 1 143 ? 6.200   -4.052  4.512   1.00 28.41 ? 236 TYR   A CD2 1 
ATOM   1188 C  CE1 . TYR   A 1 143 ? 4.625   -2.151  5.731   1.00 28.76 ? 236 TYR   A CE1 1 
ATOM   1189 C  CE2 . TYR   A 1 143 ? 5.865   -4.189  5.851   1.00 28.77 ? 236 TYR   A CE2 1 
ATOM   1190 C  CZ  . TYR   A 1 143 ? 5.071   -3.239  6.462   1.00 28.48 ? 236 TYR   A CZ  1 
ATOM   1191 O  OH  . TYR   A 1 143 ? 4.730   -3.372  7.777   1.00 28.65 ? 236 TYR   A OH  1 
ATOM   1192 N  N   . MET   A 1 144 ? 9.126   -2.447  0.492   1.00 29.84 ? 237 MET   A N   1 
ATOM   1193 C  CA  . MET   A 1 144 ? 9.989   -2.199  -0.696  1.00 31.74 ? 237 MET   A CA  1 
ATOM   1194 C  C   . MET   A 1 144 ? 10.015  -3.418  -1.643  1.00 32.46 ? 237 MET   A C   1 
ATOM   1195 O  O   . MET   A 1 144 ? 10.803  -3.411  -2.598  1.00 33.60 ? 237 MET   A O   1 
ATOM   1196 C  CB  . MET   A 1 144 ? 11.404  -1.838  -0.243  1.00 31.42 ? 237 MET   A CB  1 
ATOM   1197 C  CG  . MET   A 1 144 ? 11.442  -0.594  0.652   1.00 31.11 ? 237 MET   A CG  1 
ATOM   1198 S  SD  . MET   A 1 144 ? 10.630  0.865   -0.112  1.00 31.77 ? 237 MET   A SD  1 
ATOM   1199 C  CE  . MET   A 1 144 ? 11.500  0.936   -1.673  1.00 32.46 ? 237 MET   A CE  1 
ATOM   1200 N  N   A CYS   A 1 145 ? 9.143   -4.401  -1.403  0.50 32.91 ? 238 CYS   A N   1 
ATOM   1201 N  N   B CYS   A 1 145 ? 9.143   -4.406  -1.416  0.50 32.93 ? 238 CYS   A N   1 
ATOM   1202 C  CA  A CYS   A 1 145 ? 8.953   -5.598  -2.264  0.50 34.04 ? 238 CYS   A CA  1 
ATOM   1203 C  CA  B CYS   A 1 145 ? 8.987   -5.626  -2.264  0.50 34.07 ? 238 CYS   A CA  1 
ATOM   1204 C  C   A CYS   A 1 145 ? 7.487   -6.003  -2.263  0.50 33.50 ? 238 CYS   A C   1 
ATOM   1205 C  C   B CYS   A 1 145 ? 7.504   -6.013  -2.266  0.50 33.51 ? 238 CYS   A C   1 
ATOM   1206 O  O   A CYS   A 1 145 ? 6.836   -5.817  -1.214  0.50 32.62 ? 238 CYS   A O   1 
ATOM   1207 O  O   B CYS   A 1 145 ? 6.843   -5.817  -1.217  0.50 32.64 ? 238 CYS   A O   1 
ATOM   1208 C  CB  A CYS   A 1 145 ? 9.837   -6.735  -1.784  0.50 34.93 ? 238 CYS   A CB  1 
ATOM   1209 C  CB  B CYS   A 1 145 ? 9.869   -6.734  -1.693  0.50 34.92 ? 238 CYS   A CB  1 
ATOM   1210 S  SG  A CYS   A 1 145 ? 11.189  -6.939  -2.845  0.50 37.35 ? 238 CYS   A SG  1 
ATOM   1211 S  SG  B CYS   A 1 145 ? 10.552  -7.961  -2.789  0.50 37.45 ? 238 CYS   A SG  1 
ATOM   1212 N  N   . ASN   A 1 146 ? 6.993   -6.500  -3.400  1.00 33.91 ? 239 ASN   A N   1 
ATOM   1213 C  CA  . ASN   A 1 146 ? 5.598   -7.005  -3.526  1.00 33.41 ? 239 ASN   A CA  1 
ATOM   1214 C  C   . ASN   A 1 146 ? 5.555   -8.421  -2.940  1.00 33.41 ? 239 ASN   A C   1 
ATOM   1215 O  O   . ASN   A 1 146 ? 6.560   -9.146  -3.064  1.00 34.14 ? 239 ASN   A O   1 
ATOM   1216 C  CB  . ASN   A 1 146 ? 5.092   -6.953  -4.973  1.00 34.25 ? 239 ASN   A CB  1 
ATOM   1217 C  CG  . ASN   A 1 146 ? 4.717   -5.546  -5.408  1.00 34.87 ? 239 ASN   A CG  1 
ATOM   1218 O  OD1 . ASN   A 1 146 ? 4.001   -4.830  -4.694  1.00 33.14 ? 239 ASN   A OD1 1 
ATOM   1219 N  ND2 . ASN   A 1 146 ? 5.190   -5.135  -6.579  1.00 35.74 ? 239 ASN   A ND2 1 
ATOM   1220 N  N   . SER   A 1 147 ? 4.432   -8.788  -2.313  1.00 32.56 ? 240 SER   A N   1 
ATOM   1221 C  CA  . SER   A 1 147 ? 4.163   -10.150 -1.781  1.00 32.66 ? 240 SER   A CA  1 
ATOM   1222 C  C   . SER   A 1 147 ? 4.372   -11.190 -2.893  1.00 34.87 ? 240 SER   A C   1 
ATOM   1223 O  O   . SER   A 1 147 ? 4.786   -12.320 -2.572  1.00 35.15 ? 240 SER   A O   1 
ATOM   1224 C  CB  . SER   A 1 147 ? 2.775   -10.242 -1.194  1.00 31.46 ? 240 SER   A CB  1 
ATOM   1225 O  OG  . SER   A 1 147 ? 2.631   -9.365  -0.089  1.00 29.02 ? 240 SER   A OG  1 
ATOM   1226 N  N   . SER   A 1 148 ? 4.094   -10.806 -4.145  1.00 37.41 ? 241 SER   A N   1 
ATOM   1227 C  CA  . SER   A 1 148 ? 4.141   -11.672 -5.358  1.00 39.73 ? 241 SER   A CA  1 
ATOM   1228 C  C   . SER   A 1 148 ? 5.572   -11.882 -5.874  1.00 41.20 ? 241 SER   A C   1 
ATOM   1229 O  O   . SER   A 1 148 ? 5.763   -12.809 -6.677  1.00 42.83 ? 241 SER   A O   1 
ATOM   1230 C  CB  . SER   A 1 148 ? 3.284   -11.076 -6.453  1.00 40.56 ? 241 SER   A CB  1 
ATOM   1231 O  OG  . SER   A 1 148 ? 3.772   -9.785  -6.818  1.00 40.50 ? 241 SER   A OG  1 
ATOM   1232 N  N   . CYS   A 1 149 ? 6.545   -11.062 -5.461  1.00 41.11 ? 242 CYS   A N   1 
ATOM   1233 C  CA  . CYS   A 1 149 ? 7.916   -11.030 -6.042  1.00 42.91 ? 242 CYS   A CA  1 
ATOM   1234 C  C   . CYS   A 1 149 ? 8.545   -12.428 -6.037  1.00 44.69 ? 242 CYS   A C   1 
ATOM   1235 O  O   . CYS   A 1 149 ? 8.784   -12.976 -4.936  1.00 43.38 ? 242 CYS   A O   1 
ATOM   1236 C  CB  . CYS   A 1 149 ? 8.807   -10.077 -5.262  1.00 42.19 ? 242 CYS   A CB  1 
ATOM   1237 S  SG  . CYS   A 1 149 ? 8.694   -8.380  -5.764  1.00 43.58 ? 242 CYS   A SG  1 
ATOM   1238 N  N   . MET   A 1 150 ? 8.809   -12.977 -7.226  1.00 48.10 ? 243 MET   A N   1 
ATOM   1239 C  CA  . MET   A 1 150 ? 9.619   -14.208 -7.421  1.00 51.13 ? 243 MET   A CA  1 
ATOM   1240 C  C   . MET   A 1 150 ? 11.023  -13.959 -6.858  1.00 50.39 ? 243 MET   A C   1 
ATOM   1241 O  O   . MET   A 1 150 ? 11.576  -12.872 -7.106  1.00 52.92 ? 243 MET   A O   1 
ATOM   1242 C  CB  . MET   A 1 150 ? 9.701   -14.586 -8.903  1.00 54.23 ? 243 MET   A CB  1 
ATOM   1243 C  CG  . MET   A 1 150 ? 8.482   -15.374 -9.394  1.00 56.13 ? 243 MET   A CG  1 
ATOM   1244 S  SD  . MET   A 1 150 ? 6.916   -14.431 -9.528  1.00 57.59 ? 243 MET   A SD  1 
ATOM   1245 C  CE  . MET   A 1 150 ? 5.886   -15.609 -10.405 1.00 58.70 ? 243 MET   A CE  1 
ATOM   1246 N  N   . GLY   A 1 151 ? 11.552  -14.908 -6.088  1.00 49.30 ? 244 GLY   A N   1 
ATOM   1247 C  CA  . GLY   A 1 151 ? 12.904  -14.820 -5.503  1.00 49.15 ? 244 GLY   A CA  1 
ATOM   1248 C  C   . GLY   A 1 151 ? 12.953  -13.844 -4.340  1.00 46.95 ? 244 GLY   A C   1 
ATOM   1249 O  O   . GLY   A 1 151 ? 14.061  -13.397 -3.991  1.00 47.34 ? 244 GLY   A O   1 
ATOM   1250 N  N   . GLY   A 1 152 ? 11.789  -13.510 -3.777  1.00 44.55 ? 245 GLY   A N   1 
ATOM   1251 C  CA  . GLY   A 1 152 ? 11.624  -12.771 -2.513  1.00 42.57 ? 245 GLY   A CA  1 
ATOM   1252 C  C   . GLY   A 1 152 ? 10.593  -13.489 -1.650  1.00 40.77 ? 245 GLY   A C   1 
ATOM   1253 O  O   . GLY   A 1 152 ? 10.732  -14.714 -1.442  1.00 41.38 ? 245 GLY   A O   1 
ATOM   1254 N  N   . MET   A 1 153 ? 9.549   -12.780 -1.222  1.00 38.88 ? 246 MET   A N   1 
ATOM   1255 C  CA  . MET   A 1 153 ? 8.441   -13.368 -0.423  1.00 38.18 ? 246 MET   A CA  1 
ATOM   1256 C  C   . MET   A 1 153 ? 7.697   -14.423 -1.247  1.00 39.34 ? 246 MET   A C   1 
ATOM   1257 O  O   . MET   A 1 153 ? 7.276   -15.445 -0.661  1.00 39.10 ? 246 MET   A O   1 
ATOM   1258 C  CB  . MET   A 1 153 ? 7.487   -12.276 0.056   1.00 36.46 ? 246 MET   A CB  1 
ATOM   1259 C  CG  . MET   A 1 153 ? 8.135   -11.333 1.046   1.00 35.14 ? 246 MET   A CG  1 
ATOM   1260 S  SD  . MET   A 1 153 ? 6.961   -10.126 1.685   1.00 32.53 ? 246 MET   A SD  1 
ATOM   1261 C  CE  . MET   A 1 153 ? 6.998   -8.915  0.360   1.00 33.30 ? 246 MET   A CE  1 
ATOM   1262 N  N   . ASN   A 1 154 ? 7.578   -14.199 -2.561  1.00 40.63 ? 247 ASN   A N   1 
ATOM   1263 C  CA  . ASN   A 1 154 ? 7.052   -15.171 -3.557  1.00 41.71 ? 247 ASN   A CA  1 
ATOM   1264 C  C   . ASN   A 1 154 ? 5.723   -15.736 -3.046  1.00 41.55 ? 247 ASN   A C   1 
ATOM   1265 O  O   . ASN   A 1 154 ? 5.609   -16.981 -2.913  1.00 40.76 ? 247 ASN   A O   1 
ATOM   1266 C  CB  . ASN   A 1 154 ? 8.084   -16.253 -3.875  1.00 43.62 ? 247 ASN   A CB  1 
ATOM   1267 C  CG  . ASN   A 1 154 ? 7.633   -17.221 -4.953  1.00 45.50 ? 247 ASN   A CG  1 
ATOM   1268 O  OD1 . ASN   A 1 154 ? 6.953   -16.846 -5.908  1.00 45.84 ? 247 ASN   A OD1 1 
ATOM   1269 N  ND2 . ASN   A 1 154 ? 7.981   -18.485 -4.798  1.00 46.71 ? 247 ASN   A ND2 1 
ATOM   1270 N  N   . ARG   A 1 155 ? 4.788   -14.832 -2.737  1.00 39.75 ? 248 ARG   A N   1 
ATOM   1271 C  CA  . ARG   A 1 155 ? 3.359   -15.094 -2.430  1.00 40.35 ? 248 ARG   A CA  1 
ATOM   1272 C  C   . ARG   A 1 155 ? 3.192   -15.633 -1.005  1.00 38.84 ? 248 ARG   A C   1 
ATOM   1273 O  O   . ARG   A 1 155 ? 2.026   -15.810 -0.595  1.00 38.28 ? 248 ARG   A O   1 
ATOM   1274 C  CB  . ARG   A 1 155 ? 2.741   -16.038 -3.472  1.00 42.54 ? 248 ARG   A CB  1 
ATOM   1275 C  CG  . ARG   A 1 155 ? 2.889   -15.528 -4.896  1.00 43.82 ? 248 ARG   A CG  1 
ATOM   1276 C  CD  . ARG   A 1 155 ? 1.909   -16.142 -5.878  1.00 46.11 ? 248 ARG   A CD  1 
ATOM   1277 N  NE  . ARG   A 1 155 ? 2.040   -15.530 -7.195  1.00 47.94 ? 248 ARG   A NE  1 
ATOM   1278 C  CZ  . ARG   A 1 155 ? 1.456   -14.393 -7.584  1.00 48.02 ? 248 ARG   A CZ  1 
ATOM   1279 N  NH1 . ARG   A 1 155 ? 0.666   -13.719 -6.761  1.00 47.32 ? 248 ARG   A NH1 1 
ATOM   1280 N  NH2 . ARG   A 1 155 ? 1.668   -13.937 -8.807  1.00 49.03 ? 248 ARG   A NH2 1 
ATOM   1281 N  N   . ARG   A 1 156 ? 4.279   -15.821 -0.250  1.00 37.45 ? 249 ARG   A N   1 
ATOM   1282 C  CA  . ARG   A 1 156 ? 4.212   -16.288 1.158   1.00 37.10 ? 249 ARG   A CA  1 
ATOM   1283 C  C   . ARG   A 1 156 ? 3.800   -15.124 2.052   1.00 35.68 ? 249 ARG   A C   1 
ATOM   1284 O  O   . ARG   A 1 156 ? 4.380   -14.038 1.973   1.00 34.82 ? 249 ARG   A O   1 
ATOM   1285 C  CB  . ARG   A 1 156 ? 5.555   -16.876 1.593   1.00 37.41 ? 249 ARG   A CB  1 
ATOM   1286 C  CG  . ARG   A 1 156 ? 5.971   -18.092 0.785   1.00 38.92 ? 249 ARG   A CG  1 
ATOM   1287 C  CD  . ARG   A 1 156 ? 7.368   -18.542 1.158   1.00 39.47 ? 249 ARG   A CD  1 
ATOM   1288 N  NE  . ARG   A 1 156 ? 8.375   -17.595 0.714   1.00 39.31 ? 249 ARG   A NE  1 
ATOM   1289 C  CZ  . ARG   A 1 156 ? 9.679   -17.710 0.941   1.00 39.89 ? 249 ARG   A CZ  1 
ATOM   1290 N  NH1 . ARG   A 1 156 ? 10.156  -18.756 1.605   1.00 40.23 ? 249 ARG   A NH1 1 
ATOM   1291 N  NH2 . ARG   A 1 156 ? 10.503  -16.781 0.480   1.00 39.67 ? 249 ARG   A NH2 1 
ATOM   1292 N  N   . PRO   A 1 157 ? 2.782   -15.311 2.925   1.00 35.41 ? 250 PRO   A N   1 
ATOM   1293 C  CA  . PRO   A 1 157 ? 2.312   -14.235 3.792   1.00 34.16 ? 250 PRO   A CA  1 
ATOM   1294 C  C   . PRO   A 1 157 ? 3.336   -13.905 4.891   1.00 33.05 ? 250 PRO   A C   1 
ATOM   1295 O  O   . PRO   A 1 157 ? 4.021   -14.817 5.361   1.00 32.96 ? 250 PRO   A O   1 
ATOM   1296 C  CB  . PRO   A 1 157 ? 1.014   -14.798 4.387   1.00 34.55 ? 250 PRO   A CB  1 
ATOM   1297 C  CG  . PRO   A 1 157 ? 1.196   -16.294 4.354   1.00 35.75 ? 250 PRO   A CG  1 
ATOM   1298 C  CD  . PRO   A 1 157 ? 2.036   -16.560 3.124   1.00 36.33 ? 250 PRO   A CD  1 
ATOM   1299 N  N   . ILE   A 1 158 ? 3.424   -12.622 5.255   1.00 30.89 ? 251 ILE   A N   1 
ATOM   1300 C  CA  . ILE   A 1 158 ? 4.362   -12.158 6.314   1.00 31.11 ? 251 ILE   A CA  1 
ATOM   1301 C  C   . ILE   A 1 158 ? 3.577   -11.441 7.408   1.00 30.06 ? 251 ILE   A C   1 
ATOM   1302 O  O   . ILE   A 1 158 ? 2.455   -10.952 7.134   1.00 30.46 ? 251 ILE   A O   1 
ATOM   1303 C  CB  . ILE   A 1 158 ? 5.478   -11.274 5.724   1.00 30.57 ? 251 ILE   A CB  1 
ATOM   1304 C  CG1 . ILE   A 1 158 ? 4.922   -10.032 5.032   1.00 30.12 ? 251 ILE   A CG1 1 
ATOM   1305 C  CG2 . ILE   A 1 158 ? 6.348   -12.090 4.793   1.00 30.89 ? 251 ILE   A CG2 1 
ATOM   1306 C  CD1 . ILE   A 1 158 ? 5.900   -8.882  5.020   1.00 30.08 ? 251 ILE   A CD1 1 
ATOM   1307 N  N   . LEU   A 1 159 ? 4.143   -11.446 8.611   1.00 30.59 ? 252 LEU   A N   1 
ATOM   1308 C  CA  . LEU   A 1 159 ? 3.738   -10.568 9.728   1.00 30.47 ? 252 LEU   A CA  1 
ATOM   1309 C  C   . LEU   A 1 159 ? 4.794   -9.474  9.864   1.00 29.00 ? 252 LEU   A C   1 
ATOM   1310 O  O   . LEU   A 1 159 ? 5.984   -9.767  9.636   1.00 29.93 ? 252 LEU   A O   1 
ATOM   1311 C  CB  . LEU   A 1 159 ? 3.663   -11.385 11.025  1.00 32.19 ? 252 LEU   A CB  1 
ATOM   1312 C  CG  . LEU   A 1 159 ? 2.326   -12.021 11.396  1.00 33.48 ? 252 LEU   A CG  1 
ATOM   1313 C  CD1 . LEU   A 1 159 ? 2.431   -13.541 11.353  1.00 35.21 ? 252 LEU   A CD1 1 
ATOM   1314 C  CD2 . LEU   A 1 159 ? 1.902   -11.576 12.789  1.00 33.80 ? 252 LEU   A CD2 1 
ATOM   1315 N  N   . THR   A 1 160 ? 4.358   -8.269  10.218  1.00 28.61 ? 253 THR   A N   1 
ATOM   1316 C  CA  . THR   A 1 160 ? 5.212   -7.219  10.815  1.00 26.90 ? 253 THR   A CA  1 
ATOM   1317 C  C   . THR   A 1 160 ? 5.031   -7.267  12.330  1.00 26.28 ? 253 THR   A C   1 
ATOM   1318 O  O   . THR   A 1 160 ? 3.874   -7.252  12.784  1.00 27.03 ? 253 THR   A O   1 
ATOM   1319 C  CB  . THR   A 1 160 ? 4.859   -5.815  10.321  1.00 26.29 ? 253 THR   A CB  1 
ATOM   1320 O  OG1 . THR   A 1 160 ? 5.025   -5.802  8.907   1.00 26.44 ? 253 THR   A OG1 1 
ATOM   1321 C  CG2 . THR   A 1 160 ? 5.735   -4.744  10.939  1.00 25.68 ? 253 THR   A CG2 1 
ATOM   1322 N  N   . ILE   A 1 161 ? 6.137   -7.314  13.072  1.00 25.75 ? 254 ILE   A N   1 
ATOM   1323 C  CA  . ILE   A 1 161 ? 6.150   -7.293  14.563  1.00 26.19 ? 254 ILE   A CA  1 
ATOM   1324 C  C   . ILE   A 1 161 ? 6.672   -5.923  14.980  1.00 26.18 ? 254 ILE   A C   1 
ATOM   1325 O  O   . ILE   A 1 161 ? 7.781   -5.587  14.536  1.00 26.11 ? 254 ILE   A O   1 
ATOM   1326 C  CB  . ILE   A 1 161 ? 7.016   -8.440  15.114  1.00 26.89 ? 254 ILE   A CB  1 
ATOM   1327 C  CG1 . ILE   A 1 161 ? 6.541   -9.784  14.566  1.00 27.62 ? 254 ILE   A CG1 1 
ATOM   1328 C  CG2 . ILE   A 1 161 ? 7.035   -8.405  16.645  1.00 27.42 ? 254 ILE   A CG2 1 
ATOM   1329 C  CD1 . ILE   A 1 161 ? 7.526   -10.901 14.759  1.00 28.11 ? 254 ILE   A CD1 1 
ATOM   1330 N  N   . ILE   A 1 162 ? 5.841   -5.143  15.681  1.00 26.73 ? 255 ILE   A N   1 
ATOM   1331 C  CA  . ILE   A 1 162 ? 6.186   -3.800  16.231  1.00 27.11 ? 255 ILE   A CA  1 
ATOM   1332 C  C   . ILE   A 1 162 ? 6.467   -3.983  17.718  1.00 27.68 ? 255 ILE   A C   1 
ATOM   1333 O  O   . ILE   A 1 162 ? 5.532   -4.377  18.455  1.00 30.24 ? 255 ILE   A O   1 
ATOM   1334 C  CB  . ILE   A 1 162 ? 5.077   -2.759  15.994  1.00 26.95 ? 255 ILE   A CB  1 
ATOM   1335 C  CG1 . ILE   A 1 162 ? 4.611   -2.718  14.539  1.00 26.54 ? 255 ILE   A CG1 1 
ATOM   1336 C  CG2 . ILE   A 1 162 ? 5.515   -1.383  16.490  1.00 27.24 ? 255 ILE   A CG2 1 
ATOM   1337 C  CD1 . ILE   A 1 162 ? 5.686   -2.389  13.534  1.00 26.19 ? 255 ILE   A CD1 1 
ATOM   1338 N  N   . THR   A 1 163 ? 7.710   -3.745  18.134  1.00 27.68 ? 256 THR   A N   1 
ATOM   1339 C  CA  A THR   A 1 163 ? 8.123   -3.855  19.552  0.60 28.67 ? 256 THR   A CA  1 
ATOM   1340 C  CA  B THR   A 1 163 ? 8.130   -3.857  19.551  0.40 29.03 ? 256 THR   A CA  1 
ATOM   1341 C  C   . THR   A 1 163 ? 8.450   -2.456  20.074  1.00 29.17 ? 256 THR   A C   1 
ATOM   1342 O  O   . THR   A 1 163 ? 9.057   -1.665  19.325  1.00 28.30 ? 256 THR   A O   1 
ATOM   1343 C  CB  A THR   A 1 163 ? 9.286   -4.836  19.731  0.60 28.80 ? 256 THR   A CB  1 
ATOM   1344 C  CB  B THR   A 1 163 ? 9.302   -4.830  19.731  0.40 29.62 ? 256 THR   A CB  1 
ATOM   1345 O  OG1 A THR   A 1 163 ? 10.399  -4.302  19.020  0.60 28.73 ? 256 THR   A OG1 1 
ATOM   1346 O  OG1 B THR   A 1 163 ? 9.721   -4.833  21.095  0.40 31.31 ? 256 THR   A OG1 1 
ATOM   1347 C  CG2 A THR   A 1 163 ? 8.949   -6.231  19.244  0.60 28.89 ? 256 THR   A CG2 1 
ATOM   1348 C  CG2 B THR   A 1 163 ? 10.507  -4.484  18.890  0.40 29.56 ? 256 THR   A CG2 1 
ATOM   1349 N  N   . LEU   A 1 164 ? 8.013   -2.182  21.292  1.00 30.45 ? 257 LEU   A N   1 
ATOM   1350 C  CA  . LEU   A 1 164 ? 8.365   -0.971  22.057  1.00 31.89 ? 257 LEU   A CA  1 
ATOM   1351 C  C   . LEU   A 1 164 ? 9.495   -1.372  23.013  1.00 33.37 ? 257 LEU   A C   1 
ATOM   1352 O  O   . LEU   A 1 164 ? 9.327   -2.365  23.739  1.00 34.84 ? 257 LEU   A O   1 
ATOM   1353 C  CB  . LEU   A 1 164 ? 7.093   -0.507  22.765  1.00 32.59 ? 257 LEU   A CB  1 
ATOM   1354 C  CG  . LEU   A 1 164 ? 7.131   0.909   23.340  1.00 33.29 ? 257 LEU   A CG  1 
ATOM   1355 C  CD1 . LEU   A 1 164 ? 7.029   1.946   22.242  1.00 32.82 ? 257 LEU   A CD1 1 
ATOM   1356 C  CD2 . LEU   A 1 164 ? 6.000   1.113   24.339  1.00 34.42 ? 257 LEU   A CD2 1 
ATOM   1357 N  N   . GLU   A 1 165 ? 10.646  -0.703  22.954  1.00 35.00 ? 258 GLU   A N   1 
ATOM   1358 C  CA  . GLU   A 1 165 ? 11.801  -1.004  23.848  1.00 36.18 ? 258 GLU   A CA  1 
ATOM   1359 C  C   . GLU   A 1 165 ? 12.269  0.277   24.529  1.00 37.89 ? 258 GLU   A C   1 
ATOM   1360 O  O   . GLU   A 1 165 ? 12.073  1.367   23.963  1.00 38.66 ? 258 GLU   A O   1 
ATOM   1361 C  CB  . GLU   A 1 165 ? 12.976  -1.672  23.118  1.00 35.67 ? 258 GLU   A CB  1 
ATOM   1362 C  CG  . GLU   A 1 165 ? 12.803  -1.795  21.614  1.00 34.80 ? 258 GLU   A CG  1 
ATOM   1363 C  CD  . GLU   A 1 165 ? 13.961  -2.488  20.919  0.80 34.84 ? 258 GLU   A CD  1 
ATOM   1364 O  OE1 . GLU   A 1 165 ? 15.053  -1.914  20.910  0.80 35.77 ? 258 GLU   A OE1 1 
ATOM   1365 O  OE2 . GLU   A 1 165 ? 13.764  -3.613  20.409  0.80 34.81 ? 258 GLU   A OE2 1 
ATOM   1366 N  N   . ASP   A 1 166 ? 12.889  0.148   25.699  1.00 39.45 ? 259 ASP   A N   1 
ATOM   1367 C  CA  . ASP   A 1 166 ? 13.505  1.311   26.387  1.00 40.87 ? 259 ASP   A CA  1 
ATOM   1368 C  C   . ASP   A 1 166 ? 14.885  1.533   25.761  1.00 42.08 ? 259 ASP   A C   1 
ATOM   1369 O  O   . ASP   A 1 166 ? 15.262  0.733   24.868  1.00 42.64 ? 259 ASP   A O   1 
ATOM   1370 C  CB  . ASP   A 1 166 ? 13.539  1.141   27.905  1.00 42.30 ? 259 ASP   A CB  1 
ATOM   1371 C  CG  . ASP   A 1 166 ? 14.468  0.059   28.424  1.00 43.12 ? 259 ASP   A CG  1 
ATOM   1372 O  OD1 . ASP   A 1 166 ? 15.357  -0.401  27.670  1.00 42.37 ? 259 ASP   A OD1 1 
ATOM   1373 O  OD2 . ASP   A 1 166 ? 14.268  -0.328  29.599  1.00 44.76 ? 259 ASP   A OD2 1 
ATOM   1374 N  N   . SER   A 1 167 ? 15.610  2.549   26.234  1.00 42.13 ? 260 SER   A N   1 
ATOM   1375 C  CA  . SER   A 1 167 ? 16.909  2.970   25.659  1.00 41.93 ? 260 SER   A CA  1 
ATOM   1376 C  C   . SER   A 1 167 ? 17.935  1.840   25.815  1.00 42.45 ? 260 SER   A C   1 
ATOM   1377 O  O   . SER   A 1 167 ? 18.857  1.787   24.986  1.00 43.18 ? 260 SER   A O   1 
ATOM   1378 C  CB  . SER   A 1 167 ? 17.384  4.255   26.281  1.00 42.12 ? 260 SER   A CB  1 
ATOM   1379 O  OG  . SER   A 1 167 ? 17.610  4.098   27.661  1.00 42.39 ? 260 SER   A OG  1 
ATOM   1380 N  N   . SER   A 1 168 ? 17.763  0.958   26.810  1.00 43.13 ? 261 SER   A N   1 
ATOM   1381 C  CA  . SER   A 1 168 ? 18.697  -0.158  27.127  1.00 43.87 ? 261 SER   A CA  1 
ATOM   1382 C  C   . SER   A 1 168 ? 18.337  -1.425  26.341  1.00 43.36 ? 261 SER   A C   1 
ATOM   1383 O  O   . SER   A 1 168 ? 19.104  -2.412  26.443  1.00 44.53 ? 261 SER   A O   1 
ATOM   1384 C  CB  . SER   A 1 168 ? 18.734  -0.453  28.607  1.00 45.21 ? 261 SER   A CB  1 
ATOM   1385 O  OG  . SER   A 1 168 ? 19.225  0.659   29.334  1.00 45.39 ? 261 SER   A OG  1 
ATOM   1386 N  N   . GLY   A 1 169 ? 17.227  -1.409  25.600  1.00 42.32 ? 262 GLY   A N   1 
ATOM   1387 C  CA  . GLY   A 1 169 ? 16.769  -2.532  24.764  1.00 41.34 ? 262 GLY   A CA  1 
ATOM   1388 C  C   . GLY   A 1 169 ? 15.836  -3.472  25.514  1.00 41.15 ? 262 GLY   A C   1 
ATOM   1389 O  O   . GLY   A 1 169 ? 15.576  -4.573  24.987  1.00 40.96 ? 262 GLY   A O   1 
ATOM   1390 N  N   . ASN   A 1 170 ? 15.358  -3.092  26.706  1.00 41.40 ? 263 ASN   A N   1 
ATOM   1391 C  CA  . ASN   A 1 170 ? 14.384  -3.908  27.479  1.00 41.67 ? 263 ASN   A CA  1 
ATOM   1392 C  C   . ASN   A 1 170 ? 13.035  -3.835  26.765  1.00 40.09 ? 263 ASN   A C   1 
ATOM   1393 O  O   . ASN   A 1 170 ? 12.625  -2.721  26.372  1.00 39.60 ? 263 ASN   A O   1 
ATOM   1394 C  CB  . ASN   A 1 170 ? 14.289  -3.487  28.947  1.00 42.87 ? 263 ASN   A CB  1 
ATOM   1395 C  CG  . ASN   A 1 170 ? 15.595  -3.659  29.694  1.00 44.65 ? 263 ASN   A CG  1 
ATOM   1396 O  OD1 . ASN   A 1 170 ? 16.114  -4.767  29.771  1.00 45.82 ? 263 ASN   A OD1 1 
ATOM   1397 N  ND2 . ASN   A 1 170 ? 16.120  -2.584  30.267  1.00 44.56 ? 263 ASN   A ND2 1 
ATOM   1398 N  N   . LEU   A 1 171 ? 12.397  -4.991  26.558  1.00 40.46 ? 264 LEU   A N   1 
ATOM   1399 C  CA  . LEU   A 1 171 ? 11.058  -5.108  25.922  1.00 40.77 ? 264 LEU   A CA  1 
ATOM   1400 C  C   . LEU   A 1 171 ? 10.021  -4.399  26.807  1.00 39.98 ? 264 LEU   A C   1 
ATOM   1401 O  O   . LEU   A 1 171 ? 9.957   -4.736  27.998  1.00 41.76 ? 264 LEU   A O   1 
ATOM   1402 C  CB  . LEU   A 1 171 ? 10.722  -6.598  25.774  1.00 42.81 ? 264 LEU   A CB  1 
ATOM   1403 C  CG  . LEU   A 1 171 ? 11.192  -7.280  24.491  1.00 43.14 ? 264 LEU   A CG  1 
ATOM   1404 C  CD1 . LEU   A 1 171 ? 10.283  -6.907  23.328  1.00 42.80 ? 264 LEU   A CD1 1 
ATOM   1405 C  CD2 . LEU   A 1 171 ? 12.637  -6.948  24.169  1.00 43.77 ? 264 LEU   A CD2 1 
ATOM   1406 N  N   . LEU   A 1 172 ? 9.266   -3.441  26.252  1.00 38.20 ? 265 LEU   A N   1 
ATOM   1407 C  CA  . LEU   A 1 172 ? 8.139   -2.752  26.944  1.00 37.24 ? 265 LEU   A CA  1 
ATOM   1408 C  C   . LEU   A 1 172 ? 6.794   -3.268  26.414  1.00 35.51 ? 265 LEU   A C   1 
ATOM   1409 O  O   . LEU   A 1 172 ? 5.872   -3.379  27.203  1.00 35.87 ? 265 LEU   A O   1 
ATOM   1410 C  CB  . LEU   A 1 172 ? 8.237   -1.240  26.728  1.00 36.68 ? 265 LEU   A CB  1 
ATOM   1411 C  CG  . LEU   A 1 172 ? 9.580   -0.597  27.060  1.00 37.05 ? 265 LEU   A CG  1 
ATOM   1412 C  CD1 . LEU   A 1 172 ? 9.504   0.904   26.908  1.00 36.87 ? 265 LEU   A CD1 1 
ATOM   1413 C  CD2 . LEU   A 1 172 ? 10.040  -0.962  28.460  1.00 38.34 ? 265 LEU   A CD2 1 
ATOM   1414 N  N   . GLY   A 1 173 ? 6.700   -3.571  25.122  1.00 34.04 ? 266 GLY   A N   1 
ATOM   1415 C  CA  . GLY   A 1 173 ? 5.429   -3.908  24.453  1.00 33.48 ? 266 GLY   A CA  1 
ATOM   1416 C  C   . GLY   A 1 173 ? 5.647   -4.519  23.086  1.00 32.51 ? 266 GLY   A C   1 
ATOM   1417 O  O   . GLY   A 1 173 ? 6.657   -4.198  22.457  1.00 32.74 ? 266 GLY   A O   1 
ATOM   1418 N  N   . ARG   A 1 174 ? 4.734   -5.384  22.651  1.00 32.41 ? 267 ARG   A N   1 
ATOM   1419 C  CA  . ARG   A 1 174 ? 4.789   -6.032  21.321  1.00 31.07 ? 267 ARG   A CA  1 
ATOM   1420 C  C   . ARG   A 1 174 ? 3.375   -6.227  20.773  1.00 30.27 ? 267 ARG   A C   1 
ATOM   1421 O  O   . ARG   A 1 174 ? 2.468   -6.625  21.544  1.00 29.69 ? 267 ARG   A O   1 
ATOM   1422 C  CB  . ARG   A 1 174 ? 5.523   -7.372  21.400  1.00 32.11 ? 267 ARG   A CB  1 
ATOM   1423 C  CG  . ARG   A 1 174 ? 5.777   -8.001  20.039  1.00 31.60 ? 267 ARG   A CG  1 
ATOM   1424 C  CD  . ARG   A 1 174 ? 6.159   -9.467  20.158  1.00 33.00 ? 267 ARG   A CD  1 
ATOM   1425 N  NE  . ARG   A 1 174 ? 7.421   -9.636  20.859  1.00 33.98 ? 267 ARG   A NE  1 
ATOM   1426 C  CZ  . ARG   A 1 174 ? 7.592   -10.255 22.034  1.00 34.56 ? 267 ARG   A CZ  1 
ATOM   1427 N  NH1 . ARG   A 1 174 ? 6.578   -10.792 22.694  1.00 34.79 ? 267 ARG   A NH1 1 
ATOM   1428 N  NH2 . ARG   A 1 174 ? 8.806   -10.351 22.542  1.00 35.25 ? 267 ARG   A NH2 1 
ATOM   1429 N  N   . ASN   A 1 175 ? 3.211   -5.927  19.485  1.00 28.94 ? 268 ASN   A N   1 
ATOM   1430 C  CA  . ASN   A 1 175 ? 2.002   -6.226  18.689  1.00 29.33 ? 268 ASN   A CA  1 
ATOM   1431 C  C   . ASN   A 1 175 ? 2.451   -6.682  17.302  1.00 28.61 ? 268 ASN   A C   1 
ATOM   1432 O  O   . ASN   A 1 175 ? 3.663   -6.646  17.020  1.00 29.86 ? 268 ASN   A O   1 
ATOM   1433 C  CB  . ASN   A 1 175 ? 1.073   -5.013  18.621  1.00 30.01 ? 268 ASN   A CB  1 
ATOM   1434 C  CG  . ASN   A 1 175 ? 0.300   -4.787  19.903  1.00 31.78 ? 268 ASN   A CG  1 
ATOM   1435 O  OD1 . ASN   A 1 175 ? -0.725  -5.417  20.144  1.00 32.14 ? 268 ASN   A OD1 1 
ATOM   1436 N  ND2 . ASN   A 1 175 ? 0.772   -3.862  20.721  1.00 31.89 ? 268 ASN   A ND2 1 
ATOM   1437 N  N   . SER   A 1 176 ? 1.509   -7.115  16.470  1.00 29.11 ? 269 SER   A N   1 
ATOM   1438 C  CA  . SER   A 1 176 ? 1.778   -7.693  15.138  1.00 28.56 ? 269 SER   A CA  1 
ATOM   1439 C  C   . SER   A 1 176 ? 0.544   -7.535  14.254  1.00 28.68 ? 269 SER   A C   1 
ATOM   1440 O  O   . SER   A 1 176 ? -0.571  -7.356  14.785  1.00 28.49 ? 269 SER   A O   1 
ATOM   1441 C  CB  . SER   A 1 176 ? 2.185   -9.129  15.258  1.00 29.29 ? 269 SER   A CB  1 
ATOM   1442 O  OG  . SER   A 1 176 ? 1.159   -9.870  15.900  1.00 29.99 ? 269 SER   A OG  1 
ATOM   1443 N  N   . PHE   A 1 177 ? 0.759   -7.562  12.943  1.00 28.93 ? 270 PHE   A N   1 
ATOM   1444 C  CA  . PHE   A 1 177 ? -0.305  -7.532  11.914  1.00 29.11 ? 270 PHE   A CA  1 
ATOM   1445 C  C   . PHE   A 1 177 ? 0.256   -8.195  10.661  1.00 29.68 ? 270 PHE   A C   1 
ATOM   1446 O  O   . PHE   A 1 177 ? 1.488   -8.050  10.390  1.00 30.40 ? 270 PHE   A O   1 
ATOM   1447 C  CB  . PHE   A 1 177 ? -0.778  -6.094  11.674  1.00 28.95 ? 270 PHE   A CB  1 
ATOM   1448 C  CG  . PHE   A 1 177 ? 0.295   -5.109  11.310  1.00 29.11 ? 270 PHE   A CG  1 
ATOM   1449 C  CD1 . PHE   A 1 177 ? 1.017   -4.463  12.295  1.00 28.97 ? 270 PHE   A CD1 1 
ATOM   1450 C  CD2 . PHE   A 1 177 ? 0.565   -4.797  9.983   1.00 29.07 ? 270 PHE   A CD2 1 
ATOM   1451 C  CE1 . PHE   A 1 177 ? 1.986   -3.526  11.961  1.00 29.46 ? 270 PHE   A CE1 1 
ATOM   1452 C  CE2 . PHE   A 1 177 ? 1.553   -3.883  9.654   1.00 28.61 ? 270 PHE   A CE2 1 
ATOM   1453 C  CZ  . PHE   A 1 177 ? 2.260   -3.243  10.643  1.00 29.09 ? 270 PHE   A CZ  1 
ATOM   1454 N  N   . GLU   A 1 178 ? -0.607  -8.918  9.944   1.00 29.20 ? 271 GLU   A N   1 
ATOM   1455 C  CA  A GLU   A 1 178 ? -0.276  -9.486  8.615   0.50 29.36 ? 271 GLU   A CA  1 
ATOM   1456 C  CA  B GLU   A 1 178 ? -0.272  -9.484  8.615   0.50 29.68 ? 271 GLU   A CA  1 
ATOM   1457 C  C   . GLU   A 1 178 ? -0.162  -8.321  7.629   1.00 29.05 ? 271 GLU   A C   1 
ATOM   1458 O  O   . GLU   A 1 178 ? -0.833  -7.299  7.848   1.00 29.06 ? 271 GLU   A O   1 
ATOM   1459 C  CB  A GLU   A 1 178 ? -1.326  -10.510 8.189   0.50 29.61 ? 271 GLU   A CB  1 
ATOM   1460 C  CB  B GLU   A 1 178 ? -1.320  -10.504 8.180   0.50 30.30 ? 271 GLU   A CB  1 
ATOM   1461 C  CG  A GLU   A 1 178 ? -0.887  -11.341 7.003   0.50 29.87 ? 271 GLU   A CG  1 
ATOM   1462 C  CG  B GLU   A 1 178 ? -1.437  -11.689 9.117   0.50 31.12 ? 271 GLU   A CG  1 
ATOM   1463 C  CD  A GLU   A 1 178 ? -1.730  -12.568 6.663   0.50 30.49 ? 271 GLU   A CD  1 
ATOM   1464 C  CD  B GLU   A 1 178 ? -2.680  -12.526 8.872   0.50 32.12 ? 271 GLU   A CD  1 
ATOM   1465 O  OE1 A GLU   A 1 178 ? -1.702  -12.965 5.484   0.50 30.35 ? 271 GLU   A OE1 1 
ATOM   1466 O  OE1 B GLU   A 1 178 ? -3.481  -12.141 7.985   0.50 32.65 ? 271 GLU   A OE1 1 
ATOM   1467 O  OE2 A GLU   A 1 178 ? -2.418  -13.116 7.556   0.50 31.03 ? 271 GLU   A OE2 1 
ATOM   1468 O  OE2 B GLU   A 1 178 ? -2.864  -13.528 9.583   0.50 32.56 ? 271 GLU   A OE2 1 
ATOM   1469 N  N   A VAL   A 1 179 ? 0.692   -8.465  6.618   0.50 29.42 ? 272 VAL   A N   1 
ATOM   1470 N  N   B VAL   A 1 179 ? 0.694   -8.460  6.618   0.50 29.68 ? 272 VAL   A N   1 
ATOM   1471 C  CA  A VAL   A 1 179 ? 0.918   -7.446  5.551   0.50 29.34 ? 272 VAL   A CA  1 
ATOM   1472 C  CA  B VAL   A 1 179 ? 0.910   -7.434  5.556   0.50 29.73 ? 272 VAL   A CA  1 
ATOM   1473 C  C   A VAL   A 1 179 ? 0.870   -8.142  4.192   0.50 29.77 ? 272 VAL   A C   1 
ATOM   1474 C  C   B VAL   A 1 179 ? 0.882   -8.128  4.193   0.50 29.99 ? 272 VAL   A C   1 
ATOM   1475 O  O   A VAL   A 1 179 ? 1.503   -9.215  4.042   0.50 29.74 ? 272 VAL   A O   1 
ATOM   1476 O  O   B VAL   A 1 179 ? 1.514   -9.202  4.046   0.50 29.94 ? 272 VAL   A O   1 
ATOM   1477 C  CB  A VAL   A 1 179 ? 2.258   -6.711  5.727   0.50 29.16 ? 272 VAL   A CB  1 
ATOM   1478 C  CB  B VAL   A 1 179 ? 2.214   -6.642  5.777   0.50 29.83 ? 272 VAL   A CB  1 
ATOM   1479 C  CG1 A VAL   A 1 179 ? 2.524   -5.742  4.581   0.50 28.92 ? 272 VAL   A CG1 1 
ATOM   1480 C  CG1 B VAL   A 1 179 ? 2.224   -5.988  7.146   0.50 29.54 ? 272 VAL   A CG1 1 
ATOM   1481 C  CG2 A VAL   A 1 179 ? 2.323   -5.981  7.048   0.50 28.77 ? 272 VAL   A CG2 1 
ATOM   1482 C  CG2 B VAL   A 1 179 ? 3.430   -7.507  5.611   0.50 30.07 ? 272 VAL   A CG2 1 
ATOM   1483 N  N   . ARG   A 1 180 ? 0.136   -7.552  3.251   1.00 29.60 ? 273 ARG   A N   1 
ATOM   1484 C  CA  . ARG   A 1 180 ? 0.212   -7.901  1.821   1.00 29.77 ? 273 ARG   A CA  1 
ATOM   1485 C  C   . ARG   A 1 180 ? 0.636   -6.639  1.075   1.00 29.30 ? 273 ARG   A C   1 
ATOM   1486 O  O   . ARG   A 1 180 ? -0.059  -5.629  1.222   1.00 28.39 ? 273 ARG   A O   1 
ATOM   1487 C  CB  . ARG   A 1 180 ? -1.136  -8.400  1.334   1.00 30.45 ? 273 ARG   A CB  1 
ATOM   1488 C  CG  . ARG   A 1 180 ? -1.186  -8.587  -0.165  1.00 31.34 ? 273 ARG   A CG  1 
ATOM   1489 C  CD  . ARG   A 1 180 ? -2.478  -9.258  -0.525  1.00 32.81 ? 273 ARG   A CD  1 
ATOM   1490 N  NE  . ARG   A 1 180 ? -2.502  -9.492  -1.952  1.00 34.59 ? 273 ARG   A NE  1 
ATOM   1491 C  CZ  . ARG   A 1 180 ? -3.470  -10.080 -2.627  1.00 36.83 ? 273 ARG   A CZ  1 
ATOM   1492 N  NH1 . ARG   A 1 180 ? -4.567  -10.493 -2.007  1.00 37.10 ? 273 ARG   A NH1 1 
ATOM   1493 N  NH2 . ARG   A 1 180 ? -3.351  -10.213 -3.939  1.00 38.27 ? 273 ARG   A NH2 1 
ATOM   1494 N  N   . VAL   A 1 181 ? 1.756   -6.700  0.358   1.00 29.18 ? 274 VAL   A N   1 
ATOM   1495 C  CA  . VAL   A 1 181 ? 2.210   -5.594  -0.529  1.00 29.53 ? 274 VAL   A CA  1 
ATOM   1496 C  C   . VAL   A 1 181 ? 1.750   -5.956  -1.942  1.00 30.62 ? 274 VAL   A C   1 
ATOM   1497 O  O   . VAL   A 1 181 ? 2.147   -7.018  -2.425  1.00 31.05 ? 274 VAL   A O   1 
ATOM   1498 C  CB  . VAL   A 1 181 ? 3.725   -5.363  -0.438  1.00 29.01 ? 274 VAL   A CB  1 
ATOM   1499 C  CG1 . VAL   A 1 181 ? 4.121   -4.039  -1.091  1.00 29.44 ? 274 VAL   A CG1 1 
ATOM   1500 C  CG2 . VAL   A 1 181 ? 4.207   -5.410  1.001   1.00 28.41 ? 274 VAL   A CG2 1 
ATOM   1501 N  N   . CYS   A 1 182 ? 0.860   -5.157  -2.530  1.00 31.69 ? 275 CYS   A N   1 
ATOM   1502 C  CA  . CYS   A 1 182 ? 0.155   -5.496  -3.795  1.00 34.11 ? 275 CYS   A CA  1 
ATOM   1503 C  C   . CYS   A 1 182 ? -0.172  -4.223  -4.570  1.00 34.50 ? 275 CYS   A C   1 
ATOM   1504 O  O   . CYS   A 1 182 ? -0.099  -3.128  -3.978  1.00 34.31 ? 275 CYS   A O   1 
ATOM   1505 C  CB  . CYS   A 1 182 ? -1.106  -6.312  -3.524  1.00 35.21 ? 275 CYS   A CB  1 
ATOM   1506 S  SG  . CYS   A 1 182 ? -2.223  -5.598  -2.286  1.00 36.52 ? 275 CYS   A SG  1 
ATOM   1507 N  N   . ALA   A 1 183 ? -0.515  -4.380  -5.851  1.00 36.59 ? 276 ALA   A N   1 
ATOM   1508 C  CA  . ALA   A 1 183 ? -0.820  -3.285  -6.800  1.00 37.71 ? 276 ALA   A CA  1 
ATOM   1509 C  C   . ALA   A 1 183 ? -2.113  -2.580  -6.377  1.00 37.45 ? 276 ALA   A C   1 
ATOM   1510 O  O   . ALA   A 1 183 ? -2.170  -1.329  -6.480  1.00 37.92 ? 276 ALA   A O   1 
ATOM   1511 C  CB  . ALA   A 1 183 ? -0.938  -3.826  -8.200  1.00 39.01 ? 276 ALA   A CB  1 
ATOM   1512 N  N   . CYS   A 1 184 ? -3.111  -3.347  -5.921  1.00 37.08 ? 277 CYS   A N   1 
ATOM   1513 C  CA  . CYS   A 1 184 ? -4.498  -2.863  -5.698  1.00 37.44 ? 277 CYS   A CA  1 
ATOM   1514 C  C   . CYS   A 1 184 ? -4.970  -3.249  -4.301  1.00 35.33 ? 277 CYS   A C   1 
ATOM   1515 O  O   . CYS   A 1 184 ? -5.721  -4.201  -4.149  1.00 36.05 ? 277 CYS   A O   1 
ATOM   1516 C  CB  . CYS   A 1 184 ? -5.417  -3.419  -6.781  1.00 39.91 ? 277 CYS   A CB  1 
ATOM   1517 S  SG  . CYS   A 1 184 ? -6.818  -2.331  -7.130  1.00 42.40 ? 277 CYS   A SG  1 
ATOM   1518 N  N   . PRO   A 1 185 ? -4.544  -2.529  -3.245  1.00 33.21 ? 278 PRO   A N   1 
ATOM   1519 C  CA  . PRO   A 1 185 ? -4.896  -2.875  -1.866  1.00 31.98 ? 278 PRO   A CA  1 
ATOM   1520 C  C   . PRO   A 1 185 ? -6.406  -2.878  -1.574  1.00 31.79 ? 278 PRO   A C   1 
ATOM   1521 O  O   . PRO   A 1 185 ? -6.891  -3.812  -0.931  1.00 30.62 ? 278 PRO   A O   1 
ATOM   1522 C  CB  . PRO   A 1 185 ? -4.244  -1.762  -1.020  1.00 31.76 ? 278 PRO   A CB  1 
ATOM   1523 C  CG  . PRO   A 1 185 ? -3.167  -1.188  -1.902  1.00 32.22 ? 278 PRO   A CG  1 
ATOM   1524 C  CD  . PRO   A 1 185 ? -3.696  -1.324  -3.318  1.00 33.30 ? 278 PRO   A CD  1 
ATOM   1525 N  N   . GLY   A 1 186 ? -7.117  -1.859  -2.069  1.00 31.93 ? 279 GLY   A N   1 
ATOM   1526 C  CA  . GLY   A 1 186 ? -8.584  -1.763  -1.986  1.00 32.71 ? 279 GLY   A CA  1 
ATOM   1527 C  C   . GLY   A 1 186 ? -9.266  -3.026  -2.496  1.00 33.78 ? 279 GLY   A C   1 
ATOM   1528 O  O   . GLY   A 1 186 ? -10.050 -3.642  -1.722  1.00 33.28 ? 279 GLY   A O   1 
ATOM   1529 N  N   . ARG   A 1 187 ? -8.948  -3.430  -3.729  1.00 34.93 ? 280 ARG   A N   1 
ATOM   1530 C  CA  . ARG   A 1 187 ? -9.554  -4.613  -4.397  1.00 36.74 ? 280 ARG   A CA  1 
ATOM   1531 C  C   . ARG   A 1 187 ? -9.173  -5.873  -3.617  1.00 36.03 ? 280 ARG   A C   1 
ATOM   1532 O  O   . ARG   A 1 187 ? -10.045 -6.718  -3.400  1.00 36.32 ? 280 ARG   A O   1 
ATOM   1533 C  CB  . ARG   A 1 187 ? -9.113  -4.711  -5.863  1.00 38.50 ? 280 ARG   A CB  1 
ATOM   1534 C  CG  . ARG   A 1 187 ? -9.778  -5.840  -6.641  1.00 40.66 ? 280 ARG   A CG  1 
ATOM   1535 C  CD  . ARG   A 1 187 ? -9.116  -6.104  -7.993  1.00 42.80 ? 280 ARG   A CD  1 
ATOM   1536 N  NE  . ARG   A 1 187 ? -7.710  -6.464  -7.819  1.00 42.86 ? 280 ARG   A NE  1 
ATOM   1537 C  CZ  . ARG   A 1 187 ? -6.749  -6.352  -8.736  1.00 43.64 ? 280 ARG   A CZ  1 
ATOM   1538 N  NH1 . ARG   A 1 187 ? -7.014  -5.923  -9.960  1.00 45.67 ? 280 ARG   A NH1 1 
ATOM   1539 N  NH2 . ARG   A 1 187 ? -5.505  -6.666  -8.410  1.00 43.34 ? 280 ARG   A NH2 1 
ATOM   1540 N  N   . ASP   A 1 188 ? -7.902  -6.004  -3.235  1.00 35.64 ? 281 ASP   A N   1 
ATOM   1541 C  CA  . ASP   A 1 188 ? -7.375  -7.236  -2.586  1.00 35.63 ? 281 ASP   A CA  1 
ATOM   1542 C  C   . ASP   A 1 188 ? -7.978  -7.366  -1.180  1.00 34.29 ? 281 ASP   A C   1 
ATOM   1543 O  O   . ASP   A 1 188 ? -8.311  -8.505  -0.797  1.00 35.22 ? 281 ASP   A O   1 
ATOM   1544 C  CB  . ASP   A 1 188 ? -5.845  -7.247  -2.625  1.00 35.83 ? 281 ASP   A CB  1 
ATOM   1545 C  CG  . ASP   A 1 188 ? -5.267  -7.397  -4.027  1.00 37.16 ? 281 ASP   A CG  1 
ATOM   1546 O  OD1 . ASP   A 1 188 ? -6.027  -7.644  -4.954  1.00 39.68 ? 281 ASP   A OD1 1 
ATOM   1547 O  OD2 . ASP   A 1 188 ? -4.044  -7.289  -4.175  1.00 38.93 ? 281 ASP   A OD2 1 
ATOM   1548 N  N   . ARG   A 1 189 ? -8.146  -6.265  -0.439  1.00 32.83 ? 282 ARG   A N   1 
ATOM   1549 C  CA  . ARG   A 1 189 ? -8.830  -6.301  0.882   1.00 32.84 ? 282 ARG   A CA  1 
ATOM   1550 C  C   . ARG   A 1 189 ? -10.267 -6.800  0.693   1.00 34.36 ? 282 ARG   A C   1 
ATOM   1551 O  O   . ARG   A 1 189 ? -10.664 -7.748  1.405   1.00 35.32 ? 282 ARG   A O   1 
ATOM   1552 C  CB  . ARG   A 1 189 ? -8.812  -4.939  1.593   1.00 31.69 ? 282 ARG   A CB  1 
ATOM   1553 C  CG  . ARG   A 1 189 ? -9.609  -4.944  2.891   1.00 31.46 ? 282 ARG   A CG  1 
ATOM   1554 C  CD  . ARG   A 1 189 ? -9.451  -3.705  3.746   1.00 30.26 ? 282 ARG   A CD  1 
ATOM   1555 N  NE  . ARG   A 1 189 ? -10.533 -3.649  4.709   1.00 30.30 ? 282 ARG   A NE  1 
ATOM   1556 C  CZ  . ARG   A 1 189 ? -10.985 -2.544  5.298   1.00 30.25 ? 282 ARG   A CZ  1 
ATOM   1557 N  NH1 . ARG   A 1 189 ? -10.445 -1.359  5.038   1.00 29.83 ? 282 ARG   A NH1 1 
ATOM   1558 N  NH2 . ARG   A 1 189 ? -11.998 -2.636  6.139   1.00 30.63 ? 282 ARG   A NH2 1 
ATOM   1559 N  N   . ARG   A 1 190 ? -11.019 -6.195  -0.231  1.00 35.36 ? 283 ARG   A N   1 
ATOM   1560 C  CA  . ARG   A 1 190 ? -12.441 -6.543  -0.502  1.00 37.55 ? 283 ARG   A CA  1 
ATOM   1561 C  C   . ARG   A 1 190 ? -12.546 -8.043  -0.837  1.00 38.07 ? 283 ARG   A C   1 
ATOM   1562 O  O   . ARG   A 1 190 ? -13.397 -8.738  -0.259  1.00 39.19 ? 283 ARG   A O   1 
ATOM   1563 C  CB  . ARG   A 1 190 ? -12.980 -5.696  -1.661  1.00 38.64 ? 283 ARG   A CB  1 
ATOM   1564 C  CG  . ARG   A 1 190 ? -14.229 -4.904  -1.326  1.00 40.02 ? 283 ARG   A CG  1 
ATOM   1565 C  CD  . ARG   A 1 190 ? -14.689 -4.109  -2.522  1.00 41.04 ? 283 ARG   A CD  1 
ATOM   1566 N  NE  . ARG   A 1 190 ? -14.401 -2.685  -2.420  1.00 40.75 ? 283 ARG   A NE  1 
ATOM   1567 C  CZ  . ARG   A 1 190 ? -14.696 -1.806  -3.372  1.00 41.10 ? 283 ARG   A CZ  1 
ATOM   1568 N  NH1 . ARG   A 1 190 ? -14.449 -0.524  -3.194  1.00 40.89 ? 283 ARG   A NH1 1 
ATOM   1569 N  NH2 . ARG   A 1 190 ? -15.220 -2.205  -4.514  1.00 42.66 ? 283 ARG   A NH2 1 
ATOM   1570 N  N   . THR   A 1 191 ? -11.690 -8.516  -1.737  1.00 38.33 ? 284 THR   A N   1 
ATOM   1571 C  CA  . THR   A 1 191 ? -11.653 -9.925  -2.216  1.00 40.12 ? 284 THR   A CA  1 
ATOM   1572 C  C   . THR   A 1 191 ? -11.378 -10.855 -1.027  1.00 40.29 ? 284 THR   A C   1 
ATOM   1573 O  O   . THR   A 1 191 ? -12.124 -11.827 -0.852  1.00 41.98 ? 284 THR   A O   1 
ATOM   1574 C  CB  . THR   A 1 191 ? -10.638 -10.064 -3.358  1.00 40.42 ? 284 THR   A CB  1 
ATOM   1575 O  OG1 . THR   A 1 191 ? -11.018 -9.106  -4.347  1.00 40.94 ? 284 THR   A OG1 1 
ATOM   1576 C  CG2 . THR   A 1 191 ? -10.604 -11.447 -3.971  1.00 41.58 ? 284 THR   A CG2 1 
ATOM   1577 N  N   . GLU   A 1 192 ? -10.370 -10.551 -0.210  1.00 40.04 ? 285 GLU   A N   1 
ATOM   1578 C  CA  . GLU   A 1 192 ? -9.952  -11.425 0.919   1.00 40.39 ? 285 GLU   A CA  1 
ATOM   1579 C  C   . GLU   A 1 192 ? -11.032 -11.451 2.011   1.00 40.76 ? 285 GLU   A C   1 
ATOM   1580 O  O   . GLU   A 1 192 ? -11.213 -12.526 2.623   1.00 40.86 ? 285 GLU   A O   1 
ATOM   1581 C  CB  . GLU   A 1 192 ? -8.591  -10.992 1.454   1.00 40.45 ? 285 GLU   A CB  1 
ATOM   1582 C  CG  . GLU   A 1 192 ? -7.435  -11.428 0.570   1.00 41.07 ? 285 GLU   A CG  1 
ATOM   1583 C  CD  . GLU   A 1 192 ? -6.099  -11.589 1.280   1.00 41.57 ? 285 GLU   A CD  1 
ATOM   1584 O  OE1 . GLU   A 1 192 ? -6.087  -11.838 2.518   1.00 41.35 ? 285 GLU   A OE1 1 
ATOM   1585 O  OE2 . GLU   A 1 192 ? -5.064  -11.458 0.595   1.00 42.56 ? 285 GLU   A OE2 1 
ATOM   1586 N  N   . GLU   A 1 193 ? -11.755 -10.344 2.219   1.00 40.83 ? 286 GLU   A N   1 
ATOM   1587 C  CA  . GLU   A 1 193 ? -12.843 -10.256 3.238   1.00 41.62 ? 286 GLU   A CA  1 
ATOM   1588 C  C   . GLU   A 1 193 ? -14.074 -11.064 2.789   1.00 43.92 ? 286 GLU   A C   1 
ATOM   1589 O  O   . GLU   A 1 193 ? -14.761 -11.605 3.680   1.00 42.95 ? 286 GLU   A O   1 
ATOM   1590 C  CB  . GLU   A 1 193 ? -13.186 -8.795  3.550   1.00 40.91 ? 286 GLU   A CB  1 
ATOM   1591 C  CG  . GLU   A 1 193 ? -12.242 -8.184  4.568   1.00 39.34 ? 286 GLU   A CG  1 
ATOM   1592 C  CD  . GLU   A 1 193 ? -12.314 -6.674  4.769   1.00 38.95 ? 286 GLU   A CD  1 
ATOM   1593 O  OE1 . GLU   A 1 193 ? -13.114 -6.019  4.088   1.00 39.75 ? 286 GLU   A OE1 1 
ATOM   1594 O  OE2 . GLU   A 1 193 ? -11.550 -6.154  5.614   1.00 37.65 ? 286 GLU   A OE2 1 
ATOM   1595 N  N   . GLU   A 1 194 ? -14.341 -11.169 1.482   1.00 46.21 ? 287 GLU   A N   1 
ATOM   1596 C  CA  . GLU   A 1 194 ? -15.547 -11.876 0.961   1.00 49.29 ? 287 GLU   A CA  1 
ATOM   1597 C  C   . GLU   A 1 194 ? -15.486 -13.362 1.365   1.00 50.76 ? 287 GLU   A C   1 
ATOM   1598 O  O   . GLU   A 1 194 ? -16.552 -13.989 1.382   1.00 51.78 ? 287 GLU   A O   1 
ATOM   1599 C  CB  . GLU   A 1 194 ? -15.758 -11.622 -0.537  1.00 51.08 ? 287 GLU   A CB  1 
ATOM   1600 C  CG  . GLU   A 1 194 ? -15.014 -12.564 -1.467  1.00 52.32 ? 287 GLU   A CG  1 
ATOM   1601 C  CD  . GLU   A 1 194 ? -15.170 -12.247 -2.945  1.00 53.72 ? 287 GLU   A CD  1 
ATOM   1602 O  OE1 . GLU   A 1 194 ? -14.207 -12.477 -3.693  1.00 52.45 ? 287 GLU   A OE1 1 
ATOM   1603 O  OE2 . GLU   A 1 194 ? -16.259 -11.784 -3.350  1.00 56.29 ? 287 GLU   A OE2 1 
ATOM   1604 N  N   . ASN   A 1 195 ? -14.305 -13.870 1.745   1.00 51.45 ? 288 ASN   A N   1 
ATOM   1605 C  CA  . ASN   A 1 195 ? -14.110 -15.205 2.380   1.00 53.74 ? 288 ASN   A CA  1 
ATOM   1606 C  C   . ASN   A 1 195 ? -14.572 -15.182 3.847   1.00 54.54 ? 288 ASN   A C   1 
ATOM   1607 O  O   . ASN   A 1 195 ? -15.204 -14.251 4.360   1.00 54.93 ? 288 ASN   A O   1 
ATOM   1608 C  CB  . ASN   A 1 195 ? -12.645 -15.648 2.308   1.00 53.36 ? 288 ASN   A CB  1 
ATOM   1609 C  CG  . ASN   A 1 195 ? -12.161 -15.847 0.889   1.00 54.28 ? 288 ASN   A CG  1 
ATOM   1610 O  OD1 . ASN   A 1 195 ? -12.748 -15.324 -0.058  1.00 54.59 ? 288 ASN   A OD1 1 
ATOM   1611 N  ND2 . ASN   A 1 195 ? -11.085 -16.603 0.735   1.00 55.63 ? 288 ASN   A ND2 1 
ATOM   1612 N  N   . VAL   B 1 4   ? 9.553   -19.228 52.431  1.00 46.08 ? 97  VAL   B N   1 
ATOM   1613 C  CA  . VAL   B 1 4   ? 8.603   -18.098 52.191  1.00 44.03 ? 97  VAL   B CA  1 
ATOM   1614 C  C   . VAL   B 1 4   ? 8.254   -17.446 53.528  1.00 43.11 ? 97  VAL   B C   1 
ATOM   1615 O  O   . VAL   B 1 4   ? 7.896   -18.147 54.472  1.00 44.33 ? 97  VAL   B O   1 
ATOM   1616 C  CB  . VAL   B 1 4   ? 7.337   -18.584 51.457  1.00 44.66 ? 97  VAL   B CB  1 
ATOM   1617 C  CG1 . VAL   B 1 4   ? 6.320   -17.459 51.283  1.00 43.18 ? 97  VAL   B CG1 1 
ATOM   1618 C  CG2 . VAL   B 1 4   ? 7.680   -19.228 50.116  1.00 45.86 ? 97  VAL   B CG2 1 
ATOM   1619 N  N   . PRO   B 1 5   ? 8.353   -16.099 53.650  1.00 41.06 ? 98  PRO   B N   1 
ATOM   1620 C  CA  . PRO   B 1 5   ? 7.968   -15.405 54.878  1.00 40.31 ? 98  PRO   B CA  1 
ATOM   1621 C  C   . PRO   B 1 5   ? 6.473   -15.519 55.193  1.00 40.03 ? 98  PRO   B C   1 
ATOM   1622 O  O   . PRO   B 1 5   ? 5.664   -15.533 54.276  1.00 40.21 ? 98  PRO   B O   1 
ATOM   1623 C  CB  . PRO   B 1 5   ? 8.341   -13.926 54.648  1.00 38.27 ? 98  PRO   B CB  1 
ATOM   1624 C  CG  . PRO   B 1 5   ? 8.527   -13.786 53.140  1.00 38.48 ? 98  PRO   B CG  1 
ATOM   1625 C  CD  . PRO   B 1 5   ? 8.873   -15.171 52.631  1.00 40.05 ? 98  PRO   B CD  1 
ATOM   1626 N  N   . SER   B 1 6   ? 6.156   -15.595 56.487  1.00 40.80 ? 99  SER   B N   1 
ATOM   1627 C  CA  . SER   B 1 6   ? 4.790   -15.808 57.028  1.00 41.64 ? 99  SER   B CA  1 
ATOM   1628 C  C   . SER   B 1 6   ? 3.875   -14.653 56.610  1.00 40.45 ? 99  SER   B C   1 
ATOM   1629 O  O   . SER   B 1 6   ? 4.319   -13.498 56.664  1.00 39.24 ? 99  SER   B O   1 
ATOM   1630 C  CB  . SER   B 1 6   ? 4.809   -15.961 58.524  1.00 42.25 ? 99  SER   B CB  1 
ATOM   1631 O  OG  . SER   B 1 6   ? 3.471   -15.992 59.030  1.00 44.03 ? 99  SER   B OG  1 
ATOM   1632 N  N   . GLN   B 1 7   ? 2.638   -14.975 56.228  1.00 41.38 ? 100 GLN   B N   1 
ATOM   1633 C  CA  . GLN   B 1 7   ? 1.596   -13.993 55.848  1.00 40.63 ? 100 GLN   B CA  1 
ATOM   1634 C  C   . GLN   B 1 7   ? 0.425   -14.075 56.835  1.00 41.04 ? 100 GLN   B C   1 
ATOM   1635 O  O   . GLN   B 1 7   ? -0.558  -13.353 56.624  1.00 41.24 ? 100 GLN   B O   1 
ATOM   1636 C  CB  . GLN   B 1 7   ? 1.160   -14.232 54.405  1.00 40.81 ? 100 GLN   B CB  1 
ATOM   1637 C  CG  . GLN   B 1 7   ? 0.373   -15.524 54.201  1.00 42.40 ? 100 GLN   B CG  1 
ATOM   1638 C  CD  . GLN   B 1 7   ? -0.155  -15.650 52.795  1.00 42.14 ? 100 GLN   B CD  1 
ATOM   1639 O  OE1 . GLN   B 1 7   ? 0.580   -15.946 51.856  1.00 42.32 ? 100 GLN   B OE1 1 
ATOM   1640 N  NE2 . GLN   B 1 7   ? -1.444  -15.404 52.638  1.00 41.80 ? 100 GLN   B NE2 1 
ATOM   1641 N  N   . LYS   B 1 8   ? 0.551   -14.887 57.889  1.00 41.56 ? 101 LYS   B N   1 
ATOM   1642 C  CA  . LYS   B 1 8   ? -0.534  -15.174 58.866  1.00 42.10 ? 101 LYS   B CA  1 
ATOM   1643 C  C   . LYS   B 1 8   ? -0.858  -13.897 59.649  1.00 39.96 ? 101 LYS   B C   1 
ATOM   1644 O  O   . LYS   B 1 8   ? 0.056   -13.314 60.241  1.00 38.62 ? 101 LYS   B O   1 
ATOM   1645 C  CB  . LYS   B 1 8   ? -0.086  -16.331 59.760  1.00 43.96 ? 101 LYS   B CB  1 
ATOM   1646 C  CG  . LYS   B 1 8   ? -1.012  -16.780 60.875  1.00 45.93 ? 101 LYS   B CG  1 
ATOM   1647 C  CD  . LYS   B 1 8   ? -0.281  -17.696 61.846  1.00 47.62 ? 101 LYS   B CD  1 
ATOM   1648 C  CE  . LYS   B 1 8   ? 0.658   -18.690 61.186  1.00 49.13 ? 101 LYS   B CE  1 
ATOM   1649 N  NZ  . LYS   B 1 8   ? 0.951   -19.847 62.061  1.00 51.45 ? 101 LYS   B NZ  1 
ATOM   1650 N  N   . THR   B 1 9   ? -2.126  -13.491 59.649  1.00 39.86 ? 102 THR   B N   1 
ATOM   1651 C  CA  . THR   B 1 9   ? -2.620  -12.290 60.371  1.00 38.32 ? 102 THR   B CA  1 
ATOM   1652 C  C   . THR   B 1 9   ? -2.404  -12.489 61.869  1.00 38.79 ? 102 THR   B C   1 
ATOM   1653 O  O   . THR   B 1 9   ? -2.581  -13.627 62.354  1.00 39.12 ? 102 THR   B O   1 
ATOM   1654 C  CB  . THR   B 1 9   ? -4.087  -12.000 60.064  1.00 39.18 ? 102 THR   B CB  1 
ATOM   1655 O  OG1 . THR   B 1 9   ? -4.169  -11.838 58.647  1.00 38.65 ? 102 THR   B OG1 1 
ATOM   1656 C  CG2 . THR   B 1 9   ? -4.607  -10.762 60.770  1.00 38.92 ? 102 THR   B CG2 1 
ATOM   1657 N  N   . TYR   B 1 10  ? -2.025  -11.416 62.564  1.00 37.15 ? 103 TYR   B N   1 
ATOM   1658 C  CA  . TYR   B 1 10  ? -1.659  -11.419 64.001  1.00 38.16 ? 103 TYR   B CA  1 
ATOM   1659 C  C   . TYR   B 1 10  ? -1.848  -10.006 64.548  1.00 37.22 ? 103 TYR   B C   1 
ATOM   1660 O  O   . TYR   B 1 10  ? -0.948  -9.184  64.346  1.00 37.11 ? 103 TYR   B O   1 
ATOM   1661 C  CB  . TYR   B 1 10  ? -0.209  -11.882 64.180  1.00 38.16 ? 103 TYR   B CB  1 
ATOM   1662 C  CG  . TYR   B 1 10  ? 0.321   -11.831 65.591  1.00 38.51 ? 103 TYR   B CG  1 
ATOM   1663 C  CD1 . TYR   B 1 10  ? -0.350  -12.412 66.653  1.00 39.92 ? 103 TYR   B CD1 1 
ATOM   1664 C  CD2 . TYR   B 1 10  ? 1.524   -11.209 65.856  1.00 38.30 ? 103 TYR   B CD2 1 
ATOM   1665 C  CE1 . TYR   B 1 10  ? 0.155   -12.364 67.945  1.00 40.53 ? 103 TYR   B CE1 1 
ATOM   1666 C  CE2 . TYR   B 1 10  ? 2.046   -11.142 67.138  1.00 38.73 ? 103 TYR   B CE2 1 
ATOM   1667 C  CZ  . TYR   B 1 10  ? 1.357   -11.720 68.186  1.00 40.03 ? 103 TYR   B CZ  1 
ATOM   1668 O  OH  . TYR   B 1 10  ? 1.870   -11.625 69.442  1.00 41.06 ? 103 TYR   B OH  1 
ATOM   1669 N  N   . GLN   B 1 11  ? -2.960  -9.751  65.237  1.00 37.86 ? 104 GLN   B N   1 
ATOM   1670 C  CA  . GLN   B 1 11  ? -3.223  -8.431  65.867  1.00 37.43 ? 104 GLN   B CA  1 
ATOM   1671 C  C   . GLN   B 1 11  ? -2.261  -8.260  67.044  1.00 37.25 ? 104 GLN   B C   1 
ATOM   1672 O  O   . GLN   B 1 11  ? -1.824  -7.117  67.308  1.00 35.78 ? 104 GLN   B O   1 
ATOM   1673 C  CB  . GLN   B 1 11  ? -4.690  -8.305  66.274  1.00 38.69 ? 104 GLN   B CB  1 
ATOM   1674 C  CG  . GLN   B 1 11  ? -5.628  -8.314  65.076  1.00 39.03 ? 104 GLN   B CG  1 
ATOM   1675 C  CD  . GLN   B 1 11  ? -7.041  -7.929  65.430  1.00 40.11 ? 104 GLN   B CD  1 
ATOM   1676 O  OE1 . GLN   B 1 11  ? -7.491  -8.122  66.554  1.00 42.87 ? 104 GLN   B OE1 1 
ATOM   1677 N  NE2 . GLN   B 1 11  ? -7.764  -7.401  64.455  1.00 40.47 ? 104 GLN   B NE2 1 
ATOM   1678 N  N   . GLY   B 1 12  ? -1.946  -9.367  67.720  1.00 37.60 ? 105 GLY   B N   1 
ATOM   1679 C  CA  . GLY   B 1 12  ? -1.008  -9.402  68.849  1.00 37.90 ? 105 GLY   B CA  1 
ATOM   1680 C  C   . GLY   B 1 12  ? -1.450  -8.492  69.981  1.00 37.82 ? 105 GLY   B C   1 
ATOM   1681 O  O   . GLY   B 1 12  ? -2.679  -8.183  70.097  1.00 36.93 ? 105 GLY   B O   1 
ATOM   1682 N  N   . SER   B 1 13  ? -0.466  -8.030  70.752  1.00 37.80 ? 106 SER   B N   1 
ATOM   1683 C  CA  . SER   B 1 13  ? -0.649  -7.450  72.106  1.00 39.68 ? 106 SER   B CA  1 
ATOM   1684 C  C   . SER   B 1 13  ? -1.328  -6.075  72.018  1.00 39.23 ? 106 SER   B C   1 
ATOM   1685 O  O   . SER   B 1 13  ? -2.042  -5.706  72.958  1.00 39.03 ? 106 SER   B O   1 
ATOM   1686 C  CB  . SER   B 1 13  ? 0.679   -7.405  72.820  1.00 41.17 ? 106 SER   B CB  1 
ATOM   1687 O  OG  . SER   B 1 13  ? 0.555   -6.821  74.097  1.00 43.74 ? 106 SER   B OG  1 
ATOM   1688 N  N   . TYR   B 1 14  ? -1.115  -5.344  70.921  1.00 37.71 ? 107 TYR   B N   1 
ATOM   1689 C  CA  . TYR   B 1 14  ? -1.496  -3.911  70.764  1.00 37.25 ? 107 TYR   B CA  1 
ATOM   1690 C  C   . TYR   B 1 14  ? -2.727  -3.760  69.859  1.00 36.76 ? 107 TYR   B C   1 
ATOM   1691 O  O   . TYR   B 1 14  ? -3.084  -2.599  69.554  1.00 35.74 ? 107 TYR   B O   1 
ATOM   1692 C  CB  . TYR   B 1 14  ? -0.286  -3.114  70.262  1.00 36.20 ? 107 TYR   B CB  1 
ATOM   1693 C  CG  . TYR   B 1 14  ? 0.845   -3.122  71.254  1.00 37.53 ? 107 TYR   B CG  1 
ATOM   1694 C  CD1 . TYR   B 1 14  ? 0.784   -2.357  72.408  1.00 38.72 ? 107 TYR   B CD1 1 
ATOM   1695 C  CD2 . TYR   B 1 14  ? 1.931   -3.961  71.090  1.00 37.96 ? 107 TYR   B CD2 1 
ATOM   1696 C  CE1 . TYR   B 1 14  ? 1.786   -2.410  73.363  1.00 39.90 ? 107 TYR   B CE1 1 
ATOM   1697 C  CE2 . TYR   B 1 14  ? 2.934   -4.039  72.043  1.00 39.17 ? 107 TYR   B CE2 1 
ATOM   1698 C  CZ  . TYR   B 1 14  ? 2.856   -3.260  73.183  1.00 40.04 ? 107 TYR   B CZ  1 
ATOM   1699 O  OH  . TYR   B 1 14  ? 3.843   -3.293  74.117  1.00 41.73 ? 107 TYR   B OH  1 
ATOM   1700 N  N   . GLY   B 1 15  ? -3.369  -4.873  69.479  1.00 37.03 ? 108 GLY   B N   1 
ATOM   1701 C  CA  . GLY   B 1 15  ? -4.568  -4.882  68.616  1.00 37.08 ? 108 GLY   B CA  1 
ATOM   1702 C  C   . GLY   B 1 15  ? -4.301  -4.204  67.279  1.00 35.71 ? 108 GLY   B C   1 
ATOM   1703 O  O   . GLY   B 1 15  ? -5.054  -3.262  66.925  1.00 35.55 ? 108 GLY   B O   1 
ATOM   1704 N  N   . PHE   B 1 16  ? -3.289  -4.686  66.556  1.00 35.03 ? 109 PHE   B N   1 
ATOM   1705 C  CA  . PHE   B 1 16  ? -2.772  -4.094  65.291  1.00 34.17 ? 109 PHE   B CA  1 
ATOM   1706 C  C   . PHE   B 1 16  ? -3.623  -4.552  64.101  1.00 33.40 ? 109 PHE   B C   1 
ATOM   1707 O  O   . PHE   B 1 16  ? -3.734  -5.772  63.851  1.00 34.25 ? 109 PHE   B O   1 
ATOM   1708 C  CB  . PHE   B 1 16  ? -1.294  -4.444  65.113  1.00 33.46 ? 109 PHE   B CB  1 
ATOM   1709 C  CG  . PHE   B 1 16  ? -0.701  -4.110  63.772  1.00 32.71 ? 109 PHE   B CG  1 
ATOM   1710 C  CD1 . PHE   B 1 16  ? -0.501  -2.790  63.398  1.00 32.22 ? 109 PHE   B CD1 1 
ATOM   1711 C  CD2 . PHE   B 1 16  ? -0.315  -5.111  62.890  1.00 32.51 ? 109 PHE   B CD2 1 
ATOM   1712 C  CE1 . PHE   B 1 16  ? 0.096   -2.481  62.186  1.00 31.55 ? 109 PHE   B CE1 1 
ATOM   1713 C  CE2 . PHE   B 1 16  ? 0.254   -4.793  61.664  1.00 32.45 ? 109 PHE   B CE2 1 
ATOM   1714 C  CZ  . PHE   B 1 16  ? 0.446   -3.477  61.306  1.00 31.60 ? 109 PHE   B CZ  1 
ATOM   1715 N  N   . ARG   B 1 17  ? -4.236  -3.589  63.409  1.00 32.20 ? 110 ARG   B N   1 
ATOM   1716 C  CA  . ARG   B 1 17  ? -5.055  -3.798  62.180  1.00 32.39 ? 110 ARG   B CA  1 
ATOM   1717 C  C   . ARG   B 1 17  ? -4.667  -2.742  61.138  1.00 30.64 ? 110 ARG   B C   1 
ATOM   1718 O  O   . ARG   B 1 17  ? -4.120  -1.687  61.532  1.00 29.86 ? 110 ARG   B O   1 
ATOM   1719 C  CB  . ARG   B 1 17  ? -6.551  -3.651  62.472  1.00 34.09 ? 110 ARG   B CB  1 
ATOM   1720 C  CG  . ARG   B 1 17  ? -7.143  -4.623  63.475  1.00 36.60 ? 110 ARG   B CG  1 
ATOM   1721 C  CD  . ARG   B 1 17  ? -8.205  -3.924  64.316  0.65 37.53 ? 110 ARG   B CD  1 
ATOM   1722 N  NE  . ARG   B 1 17  ? -7.524  -3.026  65.241  0.65 38.03 ? 110 ARG   B NE  1 
ATOM   1723 C  CZ  . ARG   B 1 17  ? -7.981  -1.849  65.664  0.65 37.67 ? 110 ARG   B CZ  1 
ATOM   1724 N  NH1 . ARG   B 1 17  ? -7.252  -1.140  66.508  0.65 37.64 ? 110 ARG   B NH1 1 
ATOM   1725 N  NH2 . ARG   B 1 17  ? -9.139  -1.377  65.247  0.65 37.95 ? 110 ARG   B NH2 1 
ATOM   1726 N  N   . LEU   B 1 18  ? -4.951  -3.016  59.864  1.00 30.05 ? 111 LEU   B N   1 
ATOM   1727 C  CA  . LEU   B 1 18  ? -4.761  -2.066  58.745  1.00 28.74 ? 111 LEU   B CA  1 
ATOM   1728 C  C   . LEU   B 1 18  ? -6.114  -1.430  58.446  1.00 28.62 ? 111 LEU   B C   1 
ATOM   1729 O  O   . LEU   B 1 18  ? -7.132  -2.087  58.669  1.00 28.72 ? 111 LEU   B O   1 
ATOM   1730 C  CB  . LEU   B 1 18  ? -4.221  -2.789  57.510  1.00 29.11 ? 111 LEU   B CB  1 
ATOM   1731 C  CG  . LEU   B 1 18  ? -2.856  -3.451  57.662  1.00 29.04 ? 111 LEU   B CG  1 
ATOM   1732 C  CD1 . LEU   B 1 18  ? -2.419  -4.045  56.328  1.00 28.67 ? 111 LEU   B CD1 1 
ATOM   1733 C  CD2 . LEU   B 1 18  ? -1.792  -2.497  58.200  1.00 28.76 ? 111 LEU   B CD2 1 
ATOM   1734 N  N   . GLY   B 1 19  ? -6.105  -0.165  58.027  1.00 28.02 ? 112 GLY   B N   1 
ATOM   1735 C  CA  . GLY   B 1 19  ? -7.275  0.521   57.463  1.00 27.84 ? 112 GLY   B CA  1 
ATOM   1736 C  C   . GLY   B 1 19  ? -6.914  1.136   56.129  1.00 27.03 ? 112 GLY   B C   1 
ATOM   1737 O  O   . GLY   B 1 19  ? -5.709  1.326   55.861  1.00 26.99 ? 112 GLY   B O   1 
ATOM   1738 N  N   . PHE   B 1 20  ? -7.923  1.434   55.318  1.00 27.27 ? 113 PHE   B N   1 
ATOM   1739 C  CA  . PHE   B 1 20  ? -7.766  2.024   53.968  1.00 27.78 ? 113 PHE   B CA  1 
ATOM   1740 C  C   . PHE   B 1 20  ? -8.798  3.136   53.807  1.00 28.46 ? 113 PHE   B C   1 
ATOM   1741 O  O   . PHE   B 1 20  ? -9.869  3.050   54.434  1.00 28.21 ? 113 PHE   B O   1 
ATOM   1742 C  CB  . PHE   B 1 20  ? -7.896  0.919   52.920  1.00 28.21 ? 113 PHE   B CB  1 
ATOM   1743 C  CG  . PHE   B 1 20  ? -6.904  -0.201  53.111  1.00 28.01 ? 113 PHE   B CG  1 
ATOM   1744 C  CD1 . PHE   B 1 20  ? -5.635  -0.135  52.553  1.00 28.02 ? 113 PHE   B CD1 1 
ATOM   1745 C  CD2 . PHE   B 1 20  ? -7.234  -1.312  53.866  1.00 28.92 ? 113 PHE   B CD2 1 
ATOM   1746 C  CE1 . PHE   B 1 20  ? -4.717  -1.164  52.749  1.00 28.18 ? 113 PHE   B CE1 1 
ATOM   1747 C  CE2 . PHE   B 1 20  ? -6.328  -2.342  54.055  1.00 28.39 ? 113 PHE   B CE2 1 
ATOM   1748 C  CZ  . PHE   B 1 20  ? -5.081  -2.278  53.485  1.00 28.29 ? 113 PHE   B CZ  1 
ATOM   1749 N  N   . LEU   B 1 21  ? -8.487  4.147   52.996  1.00 28.60 ? 114 LEU   B N   1 
ATOM   1750 C  CA  . LEU   B 1 21  ? -9.464  5.210   52.656  1.00 30.01 ? 114 LEU   B CA  1 
ATOM   1751 C  C   . LEU   B 1 21  ? -10.632 4.555   51.894  1.00 30.25 ? 114 LEU   B C   1 
ATOM   1752 O  O   . LEU   B 1 21  ? -10.386 3.572   51.156  1.00 29.71 ? 114 LEU   B O   1 
ATOM   1753 C  CB  . LEU   B 1 21  ? -8.778  6.291   51.818  1.00 30.80 ? 114 LEU   B CB  1 
ATOM   1754 C  CG  . LEU   B 1 21  ? -7.697  7.110   52.513  1.00 30.56 ? 114 LEU   B CG  1 
ATOM   1755 C  CD1 . LEU   B 1 21  ? -7.022  8.027   51.495  1.00 31.51 ? 114 LEU   B CD1 1 
ATOM   1756 C  CD2 . LEU   B 1 21  ? -8.275  7.929   53.673  1.00 30.98 ? 114 LEU   B CD2 1 
ATOM   1757 N  N   . HIS   B 1 22  ? -11.865 5.004   52.134  1.00 30.81 ? 115 HIS   B N   1 
ATOM   1758 C  CA  . HIS   B 1 22  ? -13.087 4.518   51.419  1.00 31.75 ? 115 HIS   B CA  1 
ATOM   1759 C  C   . HIS   B 1 22  ? -13.272 5.401   50.187  1.00 32.06 ? 115 HIS   B C   1 
ATOM   1760 O  O   . HIS   B 1 22  ? -14.126 6.292   50.210  1.00 33.15 ? 115 HIS   B O   1 
ATOM   1761 C  CB  . HIS   B 1 22  ? -14.274 4.492   52.388  1.00 32.62 ? 115 HIS   B CB  1 
ATOM   1762 C  CG  . HIS   B 1 22  ? -13.921 3.774   53.648  1.00 32.45 ? 115 HIS   B CG  1 
ATOM   1763 N  ND1 . HIS   B 1 22  ? -13.528 2.447   53.643  1.00 32.05 ? 115 HIS   B ND1 1 
ATOM   1764 C  CD2 . HIS   B 1 22  ? -13.841 4.194   54.934  1.00 32.65 ? 115 HIS   B CD2 1 
ATOM   1765 C  CE1 . HIS   B 1 22  ? -13.251 2.069   54.876  1.00 31.60 ? 115 HIS   B CE1 1 
ATOM   1766 N  NE2 . HIS   B 1 22  ? -13.429 3.132   55.690  1.00 31.91 ? 115 HIS   B NE2 1 
ATOM   1767 N  N   A SER   B 1 23  ? -12.462 5.163   49.153  0.60 32.00 ? 116 SER   B N   1 
ATOM   1768 N  N   B SER   B 1 23  ? -12.461 5.175   49.152  0.40 32.01 ? 116 SER   B N   1 
ATOM   1769 C  CA  A SER   B 1 23  ? -12.215 6.120   48.038  0.60 32.55 ? 116 SER   B CA  1 
ATOM   1770 C  CA  B SER   B 1 23  ? -12.222 6.133   48.036  0.40 32.63 ? 116 SER   B CA  1 
ATOM   1771 C  C   A SER   B 1 23  ? -13.216 5.933   46.890  0.60 33.78 ? 116 SER   B C   1 
ATOM   1772 C  C   B SER   B 1 23  ? -13.222 5.938   46.887  0.40 33.83 ? 116 SER   B C   1 
ATOM   1773 O  O   A SER   B 1 23  ? -13.389 6.883   46.109  0.60 34.65 ? 116 SER   B O   1 
ATOM   1774 O  O   B SER   B 1 23  ? -13.404 6.890   46.103  0.40 34.76 ? 116 SER   B O   1 
ATOM   1775 C  CB  A SER   B 1 23  ? -10.803 5.998   47.555  0.60 31.96 ? 116 SER   B CB  1 
ATOM   1776 C  CB  B SER   B 1 23  ? -10.812 6.009   47.552  0.40 32.03 ? 116 SER   B CB  1 
ATOM   1777 O  OG  A SER   B 1 23  ? -9.882  6.324   48.586  0.60 30.83 ? 116 SER   B OG  1 
ATOM   1778 O  OG  B SER   B 1 23  ? -10.412 4.651   47.579  0.40 31.13 ? 116 SER   B OG  1 
ATOM   1779 N  N   . GLY   B 1 24  ? -13.837 4.759   46.779  1.00 33.73 ? 117 GLY   B N   1 
ATOM   1780 C  CA  . GLY   B 1 24  ? -14.731 4.420   45.654  1.00 35.41 ? 117 GLY   B CA  1 
ATOM   1781 C  C   . GLY   B 1 24  ? -13.960 4.147   44.364  1.00 36.27 ? 117 GLY   B C   1 
ATOM   1782 O  O   . GLY   B 1 24  ? -12.701 4.065   44.400  1.00 34.72 ? 117 GLY   B O   1 
ATOM   1783 N  N   . THR   B 1 25  ? -14.690 4.044   43.250  1.00 38.74 ? 118 THR   B N   1 
ATOM   1784 C  CA  . THR   B 1 25  ? -14.171 3.582   41.936  1.00 40.77 ? 118 THR   B CA  1 
ATOM   1785 C  C   . THR   B 1 25  ? -14.417 4.646   40.862  1.00 43.65 ? 118 THR   B C   1 
ATOM   1786 O  O   . THR   B 1 25  ? -14.551 4.262   39.691  1.00 45.35 ? 118 THR   B O   1 
ATOM   1787 C  CB  . THR   B 1 25  ? -14.795 2.236   41.549  1.00 41.14 ? 118 THR   B CB  1 
ATOM   1788 O  OG1 . THR   B 1 25  ? -16.210 2.413   41.467  1.00 42.35 ? 118 THR   B OG1 1 
ATOM   1789 C  CG2 . THR   B 1 25  ? -14.486 1.128   42.536  1.00 39.76 ? 118 THR   B CG2 1 
ATOM   1790 N  N   . ALA   B 1 26  ? -14.465 5.934   41.221  1.00 45.83 ? 119 ALA   B N   1 
ATOM   1791 C  CA  . ALA   B 1 26  ? -14.600 7.047   40.244  1.00 48.66 ? 119 ALA   B CA  1 
ATOM   1792 C  C   . ALA   B 1 26  ? -13.346 7.102   39.364  1.00 50.12 ? 119 ALA   B C   1 
ATOM   1793 O  O   . ALA   B 1 26  ? -12.248 6.812   39.878  1.00 49.20 ? 119 ALA   B O   1 
ATOM   1794 C  CB  . ALA   B 1 26  ? -14.842 8.357   40.944  1.00 49.47 ? 119 ALA   B CB  1 
ATOM   1795 N  N   . LYS   B 1 27  ? -13.500 7.470   38.087  1.00 54.53 ? 120 LYS   B N   1 
ATOM   1796 C  CA  . LYS   B 1 27  ? -12.418 7.443   37.059  1.00 56.17 ? 120 LYS   B CA  1 
ATOM   1797 C  C   . LYS   B 1 27  ? -11.155 8.130   37.598  1.00 55.90 ? 120 LYS   B C   1 
ATOM   1798 O  O   . LYS   B 1 27  ? -10.058 7.652   37.288  1.00 56.00 ? 120 LYS   B O   1 
ATOM   1799 C  CB  . LYS   B 1 27  ? -12.906 8.098   35.763  1.00 59.34 ? 120 LYS   B CB  1 
ATOM   1800 C  CG  . LYS   B 1 27  ? -13.881 7.242   34.962  1.00 60.89 ? 120 LYS   B CG  1 
ATOM   1801 C  CD  . LYS   B 1 27  ? -14.349 7.855   33.662  1.00 63.57 ? 120 LYS   B CD  1 
ATOM   1802 C  CE  . LYS   B 1 27  ? -15.157 6.882   32.829  1.00 64.99 ? 120 LYS   B CE  1 
ATOM   1803 N  NZ  . LYS   B 1 27  ? -15.387 7.382   31.453  1.00 67.92 ? 120 LYS   B NZ  1 
ATOM   1804 N  N   . SER   B 1 28  ? -11.312 9.181   38.409  1.00 56.68 ? 121 SER   B N   1 
ATOM   1805 C  CA  . SER   B 1 28  ? -10.230 10.082  38.892  1.00 56.92 ? 121 SER   B CA  1 
ATOM   1806 C  C   . SER   B 1 28  ? -9.368  9.466   40.003  1.00 54.58 ? 121 SER   B C   1 
ATOM   1807 O  O   . SER   B 1 28  ? -8.253  9.979   40.246  1.00 55.55 ? 121 SER   B O   1 
ATOM   1808 C  CB  . SER   B 1 28  ? -10.823 11.378  39.365  1.00 58.61 ? 121 SER   B CB  1 
ATOM   1809 O  OG  . SER   B 1 28  ? -11.680 11.153  40.475  1.00 58.86 ? 121 SER   B OG  1 
ATOM   1810 N  N   A VAL   B 1 29  ? -9.847  8.403   40.654  0.60 52.57 ? 122 VAL   B N   1 
ATOM   1811 N  N   B VAL   B 1 29  ? -9.853  8.407   40.661  0.40 52.64 ? 122 VAL   B N   1 
ATOM   1812 C  CA  A VAL   B 1 29  ? -9.211  7.799   41.862  0.60 49.60 ? 122 VAL   B CA  1 
ATOM   1813 C  CA  B VAL   B 1 29  ? -9.214  7.806   41.871  0.40 49.80 ? 122 VAL   B CA  1 
ATOM   1814 C  C   A VAL   B 1 29  ? -7.859  7.183   41.463  0.60 48.28 ? 122 VAL   B C   1 
ATOM   1815 C  C   B VAL   B 1 29  ? -7.867  7.184   41.472  0.40 48.36 ? 122 VAL   B C   1 
ATOM   1816 O  O   A VAL   B 1 29  ? -7.812  6.409   40.487  0.60 49.11 ? 122 VAL   B O   1 
ATOM   1817 O  O   B VAL   B 1 29  ? -7.833  6.400   40.503  0.40 49.08 ? 122 VAL   B O   1 
ATOM   1818 C  CB  A VAL   B 1 29  ? -10.148 6.771   42.531  0.60 48.47 ? 122 VAL   B CB  1 
ATOM   1819 C  CB  B VAL   B 1 29  ? -10.145 6.778   42.548  0.40 48.93 ? 122 VAL   B CB  1 
ATOM   1820 C  CG1 A VAL   B 1 29  ? -9.489  6.077   43.702  0.60 46.87 ? 122 VAL   B CG1 1 
ATOM   1821 C  CG1 B VAL   B 1 29  ? -9.679  5.349   42.323  0.40 48.04 ? 122 VAL   B CG1 1 
ATOM   1822 C  CG2 A VAL   B 1 29  ? -11.467 7.402   42.964  0.60 48.85 ? 122 VAL   B CG2 1 
ATOM   1823 C  CG2 B VAL   B 1 29  ? -10.299 7.052   44.034  0.40 48.14 ? 122 VAL   B CG2 1 
ATOM   1824 N  N   . THR   B 1 30  ? -6.804  7.526   42.208  1.00 46.37 ? 123 THR   B N   1 
ATOM   1825 C  CA  . THR   B 1 30  ? -5.408  7.083   41.956  1.00 44.42 ? 123 THR   B CA  1 
ATOM   1826 C  C   . THR   B 1 30  ? -5.084  5.827   42.772  1.00 41.18 ? 123 THR   B C   1 
ATOM   1827 O  O   . THR   B 1 30  ? -4.134  5.098   42.399  1.00 40.27 ? 123 THR   B O   1 
ATOM   1828 C  CB  . THR   B 1 30  ? -4.427  8.236   42.200  1.00 44.15 ? 123 THR   B CB  1 
ATOM   1829 O  OG1 . THR   B 1 30  ? -4.520  8.629   43.567  1.00 43.08 ? 123 THR   B OG1 1 
ATOM   1830 C  CG2 . THR   B 1 30  ? -4.705  9.421   41.295  1.00 45.57 ? 123 THR   B CG2 1 
ATOM   1831 N  N   A CYS   B 1 31  ? -5.839  5.573   43.846  0.70 40.38 ? 124 CYS   B N   1 
ATOM   1832 N  N   B CYS   B 1 31  ? -5.828  5.581   43.857  0.30 39.95 ? 124 CYS   B N   1 
ATOM   1833 C  CA  A CYS   B 1 31  ? -5.687  4.371   44.710  0.70 38.57 ? 124 CYS   B CA  1 
ATOM   1834 C  CA  B CYS   B 1 31  ? -5.682  4.371   44.710  0.30 38.12 ? 124 CYS   B CA  1 
ATOM   1835 C  C   A CYS   B 1 31  ? -7.027  4.044   45.382  0.70 38.01 ? 124 CYS   B C   1 
ATOM   1836 C  C   B CYS   B 1 31  ? -7.026  4.048   45.377  0.30 37.55 ? 124 CYS   B C   1 
ATOM   1837 O  O   A CYS   B 1 31  ? -7.692  4.976   45.887  0.70 38.99 ? 124 CYS   B O   1 
ATOM   1838 O  O   B CYS   B 1 31  ? -7.684  4.983   45.877  0.30 38.17 ? 124 CYS   B O   1 
ATOM   1839 C  CB  A CYS   B 1 31  ? -4.567  4.624   45.712  0.70 37.94 ? 124 CYS   B CB  1 
ATOM   1840 C  CB  B CYS   B 1 31  ? -4.547  4.545   45.718  0.30 37.16 ? 124 CYS   B CB  1 
ATOM   1841 S  SG  A CYS   B 1 31  ? -4.399  3.406   47.031  0.70 37.08 ? 124 CYS   B SG  1 
ATOM   1842 S  SG  B CYS   B 1 31  ? -4.856  5.756   47.029  0.30 36.88 ? 124 CYS   B SG  1 
ATOM   1843 N  N   . THR   B 1 32  ? -7.438  2.777   45.343  1.00 36.45 ? 125 THR   B N   1 
ATOM   1844 C  CA  . THR   B 1 32  ? -8.744  2.321   45.879  1.00 35.60 ? 125 THR   B CA  1 
ATOM   1845 C  C   . THR   B 1 32  ? -8.598  0.895   46.408  1.00 33.82 ? 125 THR   B C   1 
ATOM   1846 O  O   . THR   B 1 32  ? -7.943  0.081   45.744  1.00 33.40 ? 125 THR   B O   1 
ATOM   1847 C  CB  . THR   B 1 32  ? -9.866  2.491   44.847  1.00 36.29 ? 125 THR   B CB  1 
ATOM   1848 O  OG1 . THR   B 1 32  ? -11.102 2.211   45.506  1.00 36.73 ? 125 THR   B OG1 1 
ATOM   1849 C  CG2 . THR   B 1 32  ? -9.713  1.612   43.631  1.00 37.04 ? 125 THR   B CG2 1 
ATOM   1850 N  N   . TYR   B 1 33  ? -9.189  0.634   47.569  1.00 32.44 ? 126 TYR   B N   1 
ATOM   1851 C  CA  . TYR   B 1 33  ? -9.140  -0.662  48.283  1.00 31.75 ? 126 TYR   B CA  1 
ATOM   1852 C  C   . TYR   B 1 33  ? -10.505 -1.345  48.179  1.00 32.02 ? 126 TYR   B C   1 
ATOM   1853 O  O   . TYR   B 1 33  ? -11.528 -0.695  48.400  1.00 31.33 ? 126 TYR   B O   1 
ATOM   1854 C  CB  . TYR   B 1 33  ? -8.713  -0.461  49.738  1.00 31.45 ? 126 TYR   B CB  1 
ATOM   1855 C  CG  . TYR   B 1 33  ? -8.851  -1.693  50.591  1.00 31.17 ? 126 TYR   B CG  1 
ATOM   1856 C  CD1 . TYR   B 1 33  ? -7.936  -2.725  50.491  1.00 30.79 ? 126 TYR   B CD1 1 
ATOM   1857 C  CD2 . TYR   B 1 33  ? -9.902  -1.829  51.490  1.00 31.61 ? 126 TYR   B CD2 1 
ATOM   1858 C  CE1 . TYR   B 1 33  ? -8.054  -3.860  51.275  1.00 30.98 ? 126 TYR   B CE1 1 
ATOM   1859 C  CE2 . TYR   B 1 33  ? -10.034 -2.956  52.278  1.00 31.62 ? 126 TYR   B CE2 1 
ATOM   1860 C  CZ  . TYR   B 1 33  ? -9.108  -3.979  52.160  1.00 31.45 ? 126 TYR   B CZ  1 
ATOM   1861 O  OH  . TYR   B 1 33  ? -9.225  -5.103  52.927  1.00 32.57 ? 126 TYR   B OH  1 
ATOM   1862 N  N   . SER   B 1 34  ? -10.491 -2.638  47.847  1.00 31.86 ? 127 SER   B N   1 
ATOM   1863 C  CA  . SER   B 1 34  ? -11.670 -3.534  47.820  1.00 32.46 ? 127 SER   B CA  1 
ATOM   1864 C  C   . SER   B 1 34  ? -11.690 -4.359  49.102  1.00 32.15 ? 127 SER   B C   1 
ATOM   1865 O  O   . SER   B 1 34  ? -10.842 -5.233  49.273  1.00 31.23 ? 127 SER   B O   1 
ATOM   1866 C  CB  . SER   B 1 34  ? -11.643 -4.429  46.601  1.00 33.44 ? 127 SER   B CB  1 
ATOM   1867 O  OG  . SER   B 1 34  ? -12.722 -5.356  46.637  1.00 34.18 ? 127 SER   B OG  1 
ATOM   1868 N  N   . PRO   B 1 35  ? -12.654 -4.117  50.025  1.00 31.95 ? 128 PRO   B N   1 
ATOM   1869 C  CA  . PRO   B 1 35  ? -12.796 -4.948  51.219  1.00 32.16 ? 128 PRO   B CA  1 
ATOM   1870 C  C   . PRO   B 1 35  ? -13.200 -6.391  50.865  1.00 33.22 ? 128 PRO   B C   1 
ATOM   1871 O  O   . PRO   B 1 35  ? -12.762 -7.288  51.534  1.00 33.39 ? 128 PRO   B O   1 
ATOM   1872 C  CB  . PRO   B 1 35  ? -13.887 -4.282  52.075  1.00 32.05 ? 128 PRO   B CB  1 
ATOM   1873 C  CG  . PRO   B 1 35  ? -14.373 -3.067  51.291  1.00 32.22 ? 128 PRO   B CG  1 
ATOM   1874 C  CD  . PRO   B 1 35  ? -13.654 -3.042  49.959  1.00 31.98 ? 128 PRO   B CD  1 
ATOM   1875 N  N   . ALA   B 1 36  ? -14.004 -6.581  49.821  1.00 34.46 ? 129 ALA   B N   1 
ATOM   1876 C  CA  . ALA   B 1 36  ? -14.510 -7.905  49.383  1.00 36.16 ? 129 ALA   B CA  1 
ATOM   1877 C  C   . ALA   B 1 36  ? -13.328 -8.780  48.938  1.00 36.63 ? 129 ALA   B C   1 
ATOM   1878 O  O   . ALA   B 1 36  ? -13.363 -9.988  49.208  1.00 37.45 ? 129 ALA   B O   1 
ATOM   1879 C  CB  . ALA   B 1 36  ? -15.540 -7.751  48.283  1.00 36.86 ? 129 ALA   B CB  1 
ATOM   1880 N  N   . LEU   B 1 37  ? -12.319 -8.193  48.292  1.00 36.33 ? 130 LEU   B N   1 
ATOM   1881 C  CA  . LEU   B 1 37  ? -11.162 -8.939  47.727  1.00 36.59 ? 130 LEU   B CA  1 
ATOM   1882 C  C   . LEU   B 1 37  ? -9.930  -8.816  48.638  1.00 35.99 ? 130 LEU   B C   1 
ATOM   1883 O  O   . LEU   B 1 37  ? -8.958  -9.519  48.343  1.00 36.76 ? 130 LEU   B O   1 
ATOM   1884 C  CB  . LEU   B 1 37  ? -10.856 -8.388  46.334  1.00 36.63 ? 130 LEU   B CB  1 
ATOM   1885 C  CG  . LEU   B 1 37  ? -11.935 -8.596  45.277  1.00 37.90 ? 130 LEU   B CG  1 
ATOM   1886 C  CD1 . LEU   B 1 37  ? -11.686 -7.730  44.050  1.00 37.98 ? 130 LEU   B CD1 1 
ATOM   1887 C  CD2 . LEU   B 1 37  ? -12.028 -10.057 44.874  1.00 39.40 ? 130 LEU   B CD2 1 
ATOM   1888 N  N   . ASN   B 1 38  ? -9.962  -7.955  49.671  1.00 34.85 ? 131 ASN   B N   1 
ATOM   1889 C  CA  . ASN   B 1 38  ? -8.790  -7.503  50.485  1.00 33.89 ? 131 ASN   B CA  1 
ATOM   1890 C  C   . ASN   B 1 38  ? -7.651  -7.124  49.532  1.00 33.45 ? 131 ASN   B C   1 
ATOM   1891 O  O   . ASN   B 1 38  ? -6.527  -7.650  49.667  1.00 33.00 ? 131 ASN   B O   1 
ATOM   1892 C  CB  . ASN   B 1 38  ? -8.381  -8.538  51.536  1.00 34.06 ? 131 ASN   B CB  1 
ATOM   1893 C  CG  . ASN   B 1 38  ? -7.299  -8.060  52.481  1.00 32.82 ? 131 ASN   B CG  1 
ATOM   1894 O  OD1 . ASN   B 1 38  ? -7.199  -6.878  52.799  1.00 32.32 ? 131 ASN   B OD1 1 
ATOM   1895 N  ND2 . ASN   B 1 38  ? -6.478  -8.973  52.956  1.00 32.89 ? 131 ASN   B ND2 1 
ATOM   1896 N  N   . LYS   B 1 39  ? -7.950  -6.247  48.572  1.00 33.70 ? 132 LYS   B N   1 
ATOM   1897 C  CA  . LYS   B 1 39  ? -7.045  -5.937  47.440  1.00 33.55 ? 132 LYS   B CA  1 
ATOM   1898 C  C   . LYS   B 1 39  ? -7.014  -4.435  47.195  1.00 33.23 ? 132 LYS   B C   1 
ATOM   1899 O  O   . LYS   B 1 39  ? -8.090  -3.831  47.012  1.00 33.53 ? 132 LYS   B O   1 
ATOM   1900 C  CB  . LYS   B 1 39  ? -7.478  -6.699  46.188  1.00 34.67 ? 132 LYS   B CB  1 
ATOM   1901 C  CG  . LYS   B 1 39  ? -6.530  -6.587  45.006  1.00 34.77 ? 132 LYS   B CG  1 
ATOM   1902 C  CD  . LYS   B 1 39  ? -6.878  -7.516  43.882  1.00 36.24 ? 132 LYS   B CD  1 
ATOM   1903 C  CE  . LYS   B 1 39  ? -5.870  -7.469  42.754  1.00 37.23 ? 132 LYS   B CE  1 
ATOM   1904 N  NZ  . LYS   B 1 39  ? -5.910  -8.696  41.926  1.00 38.91 ? 132 LYS   B NZ  1 
ATOM   1905 N  N   A MET   B 1 40  ? -5.806  -3.863  47.219  0.70 33.18 ? 133 MET   B N   1 
ATOM   1906 N  N   B MET   B 1 40  ? -5.806  -3.862  47.217  0.30 32.74 ? 133 MET   B N   1 
ATOM   1907 C  CA  A MET   B 1 40  ? -5.509  -2.458  46.835  0.70 33.76 ? 133 MET   B CA  1 
ATOM   1908 C  CA  B MET   B 1 40  ? -5.508  -2.457  46.834  0.30 32.77 ? 133 MET   B CA  1 
ATOM   1909 C  C   A MET   B 1 40  ? -5.283  -2.409  45.316  0.70 34.11 ? 133 MET   B C   1 
ATOM   1910 C  C   B MET   B 1 40  ? -5.279  -2.404  45.318  0.30 33.59 ? 133 MET   B C   1 
ATOM   1911 O  O   A MET   B 1 40  ? -4.474  -3.210  44.820  0.70 33.56 ? 133 MET   B O   1 
ATOM   1912 O  O   B MET   B 1 40  ? -4.474  -3.211  44.820  0.30 33.57 ? 133 MET   B O   1 
ATOM   1913 C  CB  A MET   B 1 40  ? -4.255  -1.955  47.559  0.70 33.74 ? 133 MET   B CB  1 
ATOM   1914 C  CB  B MET   B 1 40  ? -4.255  -1.960  47.567  0.30 32.00 ? 133 MET   B CB  1 
ATOM   1915 C  CG  A MET   B 1 40  ? -3.814  -0.577  47.113  0.70 34.61 ? 133 MET   B CG  1 
ATOM   1916 C  CG  B MET   B 1 40  ? -3.676  -0.666  47.021  0.30 32.16 ? 133 MET   B CG  1 
ATOM   1917 S  SD  A MET   B 1 40  ? -5.014  0.719   47.510  0.70 36.47 ? 133 MET   B SD  1 
ATOM   1918 S  SD  B MET   B 1 40  ? -2.206  -0.120  47.937  0.30 31.45 ? 133 MET   B SD  1 
ATOM   1919 C  CE  A MET   B 1 40  ? -4.806  0.861   49.283  0.70 35.01 ? 133 MET   B CE  1 
ATOM   1920 C  CE  B MET   B 1 40  ? -2.983  0.429   49.454  0.30 30.94 ? 133 MET   B CE  1 
ATOM   1921 N  N   . PHE   B 1 41  ? -5.990  -1.515  44.619  1.00 34.10 ? 134 PHE   B N   1 
ATOM   1922 C  CA  . PHE   B 1 41  ? -5.725  -1.145  43.210  1.00 35.21 ? 134 PHE   B CA  1 
ATOM   1923 C  C   . PHE   B 1 41  ? -5.107  0.256   43.227  1.00 34.99 ? 134 PHE   B C   1 
ATOM   1924 O  O   . PHE   B 1 41  ? -5.748  1.156   43.749  1.00 34.36 ? 134 PHE   B O   1 
ATOM   1925 C  CB  . PHE   B 1 41  ? -7.013  -1.181  42.383  1.00 36.32 ? 134 PHE   B CB  1 
ATOM   1926 C  CG  . PHE   B 1 41  ? -7.743  -2.499  42.400  1.00 37.18 ? 134 PHE   B CG  1 
ATOM   1927 C  CD1 . PHE   B 1 41  ? -8.469  -2.904  43.515  1.00 36.50 ? 134 PHE   B CD1 1 
ATOM   1928 C  CD2 . PHE   B 1 41  ? -7.712  -3.337  41.291  1.00 38.15 ? 134 PHE   B CD2 1 
ATOM   1929 C  CE1 . PHE   B 1 41  ? -9.129  -4.127  43.532  1.00 37.19 ? 134 PHE   B CE1 1 
ATOM   1930 C  CE2 . PHE   B 1 41  ? -8.385  -4.552  41.303  1.00 39.09 ? 134 PHE   B CE2 1 
ATOM   1931 C  CZ  . PHE   B 1 41  ? -9.093  -4.947  42.420  1.00 38.83 ? 134 PHE   B CZ  1 
ATOM   1932 N  N   . CYS   B 1 42  ? -3.897  0.438   42.696  1.00 36.20 ? 135 CYS   B N   1 
ATOM   1933 C  CA  . CYS   B 1 42  ? -3.186  1.747   42.721  1.00 36.58 ? 135 CYS   B CA  1 
ATOM   1934 C  C   . CYS   B 1 42  ? -2.408  1.964   41.419  1.00 37.97 ? 135 CYS   B C   1 
ATOM   1935 O  O   . CYS   B 1 42  ? -2.157  0.983   40.709  1.00 37.92 ? 135 CYS   B O   1 
ATOM   1936 C  CB  . CYS   B 1 42  ? -2.280  1.840   43.941  1.00 36.18 ? 135 CYS   B CB  1 
ATOM   1937 S  SG  . CYS   B 1 42  ? -1.007  0.545   44.022  1.00 36.74 ? 135 CYS   B SG  1 
ATOM   1938 N  N   . GLN   B 1 43  ? -2.081  3.216   41.099  1.00 39.23 ? 136 GLN   B N   1 
ATOM   1939 C  CA  . GLN   B 1 43  ? -1.265  3.590   39.915  1.00 40.56 ? 136 GLN   B CA  1 
ATOM   1940 C  C   . GLN   B 1 43  ? 0.222   3.596   40.272  1.00 39.50 ? 136 GLN   B C   1 
ATOM   1941 O  O   . GLN   B 1 43  ? 0.532   3.829   41.431  1.00 37.40 ? 136 GLN   B O   1 
ATOM   1942 C  CB  . GLN   B 1 43  ? -1.658  4.975   39.408  1.00 42.75 ? 136 GLN   B CB  1 
ATOM   1943 C  CG  . GLN   B 1 43  ? -3.040  5.044   38.785  1.00 44.47 ? 136 GLN   B CG  1 
ATOM   1944 C  CD  . GLN   B 1 43  ? -3.437  6.481   38.551  1.00 45.65 ? 136 GLN   B CD  1 
ATOM   1945 O  OE1 . GLN   B 1 43  ? -4.509  6.920   38.975  1.00 46.59 ? 136 GLN   B OE1 1 
ATOM   1946 N  NE2 . GLN   B 1 43  ? -2.548  7.242   37.935  1.00 46.34 ? 136 GLN   B NE2 1 
ATOM   1947 N  N   . LEU   B 1 44  ? 1.089   3.369   39.274  1.00 40.52 ? 137 LEU   B N   1 
ATOM   1948 C  CA  . LEU   B 1 44  ? 2.581   3.380   39.350  1.00 40.02 ? 137 LEU   B CA  1 
ATOM   1949 C  C   . LEU   B 1 44  ? 3.060   4.671   40.018  1.00 39.59 ? 137 LEU   B C   1 
ATOM   1950 O  O   . LEU   B 1 44  ? 2.642   5.756   39.550  1.00 39.28 ? 137 LEU   B O   1 
ATOM   1951 C  CB  . LEU   B 1 44  ? 3.128   3.305   37.917  1.00 41.66 ? 137 LEU   B CB  1 
ATOM   1952 C  CG  . LEU   B 1 44  ? 4.625   3.036   37.779  1.00 41.53 ? 137 LEU   B CG  1 
ATOM   1953 C  CD1 . LEU   B 1 44  ? 4.955   1.686   38.374  1.00 40.75 ? 137 LEU   B CD1 1 
ATOM   1954 C  CD2 . LEU   B 1 44  ? 5.076   3.129   36.336  1.00 43.12 ? 137 LEU   B CD2 1 
ATOM   1955 N  N   . ALA   B 1 45  ? 3.905   4.561   41.052  1.00 38.83 ? 138 ALA   B N   1 
ATOM   1956 C  CA  . ALA   B 1 45  ? 4.643   5.679   41.695  1.00 39.68 ? 138 ALA   B CA  1 
ATOM   1957 C  C   . ALA   B 1 45  ? 3.697   6.634   42.438  1.00 39.84 ? 138 ALA   B C   1 
ATOM   1958 O  O   . ALA   B 1 45  ? 4.208   7.592   43.033  1.00 41.97 ? 138 ALA   B O   1 
ATOM   1959 C  CB  . ALA   B 1 45  ? 5.461   6.416   40.660  1.00 40.85 ? 138 ALA   B CB  1 
ATOM   1960 N  N   . LYS   B 1 46  ? 2.384   6.388   42.426  1.00 39.33 ? 139 LYS   B N   1 
ATOM   1961 C  CA  . LYS   B 1 46  ? 1.387   7.274   43.084  1.00 38.57 ? 139 LYS   B CA  1 
ATOM   1962 C  C   . LYS   B 1 46  ? 1.218   6.854   44.550  1.00 36.12 ? 139 LYS   B C   1 
ATOM   1963 O  O   . LYS   B 1 46  ? 1.491   5.681   44.919  1.00 33.80 ? 139 LYS   B O   1 
ATOM   1964 C  CB  . LYS   B 1 46  ? 0.047   7.271   42.343  1.00 40.01 ? 139 LYS   B CB  1 
ATOM   1965 C  CG  . LYS   B 1 46  ? 0.018   7.974   40.990  1.00 42.40 ? 139 LYS   B CG  1 
ATOM   1966 C  CD  . LYS   B 1 46  ? 0.519   9.398   40.967  1.00 43.70 ? 139 LYS   B CD  1 
ATOM   1967 C  CE  . LYS   B 1 46  ? 0.270   10.085  39.641  1.00 45.94 ? 139 LYS   B CE  1 
ATOM   1968 N  NZ  . LYS   B 1 46  ? 0.949   9.401   38.509  1.00 47.10 ? 139 LYS   B NZ  1 
ATOM   1969 N  N   . THR   B 1 47  ? 0.792   7.816   45.367  1.00 35.46 ? 140 THR   B N   1 
ATOM   1970 C  CA  . THR   B 1 47  ? 0.569   7.684   46.823  1.00 34.26 ? 140 THR   B CA  1 
ATOM   1971 C  C   . THR   B 1 47  ? -0.466  6.598   47.127  1.00 33.45 ? 140 THR   B C   1 
ATOM   1972 O  O   . THR   B 1 47  ? -1.608  6.680   46.651  1.00 33.65 ? 140 THR   B O   1 
ATOM   1973 C  CB  . THR   B 1 47  ? 0.115   9.020   47.403  1.00 35.18 ? 140 THR   B CB  1 
ATOM   1974 O  OG1 . THR   B 1 47  ? 1.126   9.958   47.031  1.00 36.15 ? 140 THR   B OG1 1 
ATOM   1975 C  CG2 . THR   B 1 47  ? -0.052  8.974   48.900  1.00 34.31 ? 140 THR   B CG2 1 
ATOM   1976 N  N   A CYS   B 1 48  ? -0.066  5.618   47.935  0.50 32.78 ? 141 CYS   B N   1 
ATOM   1977 N  N   B CYS   B 1 48  ? -0.064  5.619   47.937  0.50 32.35 ? 141 CYS   B N   1 
ATOM   1978 C  CA  A CYS   B 1 48  ? -0.926  4.531   48.465  0.50 32.32 ? 141 CYS   B CA  1 
ATOM   1979 C  CA  B CYS   B 1 48  ? -0.926  4.540   48.479  0.50 31.62 ? 141 CYS   B CA  1 
ATOM   1980 C  C   A CYS   B 1 48  ? -0.993  4.644   49.984  0.50 31.02 ? 141 CYS   B C   1 
ATOM   1981 C  C   B CYS   B 1 48  ? -0.992  4.650   49.991  0.50 30.64 ? 141 CYS   B C   1 
ATOM   1982 O  O   A CYS   B 1 48  ? -0.146  4.092   50.684  0.50 30.32 ? 141 CYS   B O   1 
ATOM   1983 O  O   B CYS   B 1 48  ? -0.145  4.096   50.688  0.50 29.96 ? 141 CYS   B O   1 
ATOM   1984 C  CB  A CYS   B 1 48  ? -0.384  3.170   48.052  0.50 33.16 ? 141 CYS   B CB  1 
ATOM   1985 C  CB  B CYS   B 1 48  ? -0.383  3.173   48.111  0.50 31.96 ? 141 CYS   B CB  1 
ATOM   1986 S  SG  A CYS   B 1 48  ? -1.484  1.807   48.523  0.50 34.85 ? 141 CYS   B SG  1 
ATOM   1987 S  SG  B CYS   B 1 48  ? -0.335  2.948   46.327  0.50 33.53 ? 141 CYS   B SG  1 
ATOM   1988 N  N   . PRO   B 1 49  ? -1.998  5.365   50.545  1.00 30.60 ? 142 PRO   B N   1 
ATOM   1989 C  CA  . PRO   B 1 49  ? -2.154  5.454   51.990  1.00 29.98 ? 142 PRO   B CA  1 
ATOM   1990 C  C   . PRO   B 1 49  ? -2.517  4.075   52.575  1.00 29.34 ? 142 PRO   B C   1 
ATOM   1991 O  O   . PRO   B 1 49  ? -3.428  3.419   52.084  1.00 29.14 ? 142 PRO   B O   1 
ATOM   1992 C  CB  . PRO   B 1 49  ? -3.283  6.471   52.160  1.00 30.83 ? 142 PRO   B CB  1 
ATOM   1993 C  CG  . PRO   B 1 49  ? -3.317  7.208   50.833  1.00 32.00 ? 142 PRO   B CG  1 
ATOM   1994 C  CD  . PRO   B 1 49  ? -3.029  6.127   49.818  1.00 31.75 ? 142 PRO   B CD  1 
ATOM   1995 N  N   . VAL   B 1 50  ? -1.763  3.652   53.582  1.00 27.80 ? 143 VAL   B N   1 
ATOM   1996 C  CA  . VAL   B 1 50  ? -2.100  2.482   54.428  1.00 27.61 ? 143 VAL   B CA  1 
ATOM   1997 C  C   . VAL   B 1 50  ? -2.179  3.003   55.855  1.00 26.89 ? 143 VAL   B C   1 
ATOM   1998 O  O   . VAL   B 1 50  ? -1.204  3.630   56.316  1.00 26.95 ? 143 VAL   B O   1 
ATOM   1999 C  CB  . VAL   B 1 50  ? -1.072  1.349   54.252  1.00 27.51 ? 143 VAL   B CB  1 
ATOM   2000 C  CG1 . VAL   B 1 50  ? -1.300  0.213   55.240  1.00 27.32 ? 143 VAL   B CG1 1 
ATOM   2001 C  CG2 . VAL   B 1 50  ? -1.079  0.835   52.816  1.00 28.40 ? 143 VAL   B CG2 1 
ATOM   2002 N  N   . GLN   B 1 51  ? -3.317  2.787   56.508  1.00 26.97 ? 144 GLN   B N   1 
ATOM   2003 C  CA  . GLN   B 1 51  ? -3.528  3.185   57.918  1.00 27.45 ? 144 GLN   B CA  1 
ATOM   2004 C  C   . GLN   B 1 51  ? -3.106  2.049   58.847  1.00 26.95 ? 144 GLN   B C   1 
ATOM   2005 O  O   . GLN   B 1 51  ? -3.465  0.894   58.563  1.00 27.10 ? 144 GLN   B O   1 
ATOM   2006 C  CB  . GLN   B 1 51  ? -4.982  3.574   58.125  1.00 28.56 ? 144 GLN   B CB  1 
ATOM   2007 C  CG  . GLN   B 1 51  ? -5.430  4.697   57.206  1.00 29.51 ? 144 GLN   B CG  1 
ATOM   2008 C  CD  . GLN   B 1 51  ? -6.918  4.882   57.270  1.00 30.69 ? 144 GLN   B CD  1 
ATOM   2009 O  OE1 . GLN   B 1 51  ? -7.640  4.028   57.778  1.00 32.58 ? 144 GLN   B OE1 1 
ATOM   2010 N  NE2 . GLN   B 1 51  ? -7.387  6.001   56.743  1.00 31.70 ? 144 GLN   B NE2 1 
ATOM   2011 N  N   . LEU   B 1 52  ? -2.360  2.388   59.902  1.00 26.92 ? 145 LEU   B N   1 
ATOM   2012 C  CA  . LEU   B 1 52  ? -2.063  1.497   61.050  1.00 26.87 ? 145 LEU   B CA  1 
ATOM   2013 C  C   . LEU   B 1 52  ? -3.026  1.848   62.188  1.00 28.23 ? 145 LEU   B C   1 
ATOM   2014 O  O   . LEU   B 1 52  ? -3.064  3.037   62.614  1.00 29.16 ? 145 LEU   B O   1 
ATOM   2015 C  CB  . LEU   B 1 52  ? -0.608  1.679   61.493  1.00 26.21 ? 145 LEU   B CB  1 
ATOM   2016 C  CG  . LEU   B 1 52  ? 0.447   1.700   60.393  1.00 25.57 ? 145 LEU   B CG  1 
ATOM   2017 C  CD1 . LEU   B 1 52  ? 1.836   1.789   61.017  1.00 25.49 ? 145 LEU   B CD1 1 
ATOM   2018 C  CD2 . LEU   B 1 52  ? 0.349   0.478   59.486  1.00 25.12 ? 145 LEU   B CD2 1 
ATOM   2019 N  N   . TRP   B 1 53  ? -3.811  0.874   62.643  1.00 28.47 ? 146 TRP   B N   1 
ATOM   2020 C  CA  . TRP   B 1 53  ? -4.725  1.026   63.803  1.00 29.37 ? 146 TRP   B CA  1 
ATOM   2021 C  C   . TRP   B 1 53  ? -4.199  0.146   64.939  1.00 30.30 ? 146 TRP   B C   1 
ATOM   2022 O  O   . TRP   B 1 53  ? -3.951  -1.052  64.686  1.00 30.28 ? 146 TRP   B O   1 
ATOM   2023 C  CB  . TRP   B 1 53  ? -6.170  0.682   63.418  1.00 29.81 ? 146 TRP   B CB  1 
ATOM   2024 C  CG  . TRP   B 1 53  ? -6.794  1.631   62.439  1.00 30.25 ? 146 TRP   B CG  1 
ATOM   2025 C  CD1 . TRP   B 1 53  ? -6.468  1.754   61.122  1.00 29.41 ? 146 TRP   B CD1 1 
ATOM   2026 C  CD2 . TRP   B 1 53  ? -7.847  2.587   62.679  1.00 31.08 ? 146 TRP   B CD2 1 
ATOM   2027 N  NE1 . TRP   B 1 53  ? -7.244  2.708   60.528  1.00 30.18 ? 146 TRP   B NE1 1 
ATOM   2028 C  CE2 . TRP   B 1 53  ? -8.102  3.237   61.451  1.00 31.38 ? 146 TRP   B CE2 1 
ATOM   2029 C  CE3 . TRP   B 1 53  ? -8.633  2.920   63.784  1.00 32.40 ? 146 TRP   B CE3 1 
ATOM   2030 C  CZ2 . TRP   B 1 53  ? -9.080  4.227   61.310  1.00 32.45 ? 146 TRP   B CZ2 1 
ATOM   2031 C  CZ3 . TRP   B 1 53  ? -9.608  3.889   63.646  1.00 33.17 ? 146 TRP   B CZ3 1 
ATOM   2032 C  CH2 . TRP   B 1 53  ? -9.830  4.529   62.425  1.00 33.23 ? 146 TRP   B CH2 1 
ATOM   2033 N  N   . VAL   B 1 54  ? -4.074  0.716   66.136  1.00 30.59 ? 147 VAL   B N   1 
ATOM   2034 C  CA  . VAL   B 1 54  ? -3.686  -0.004  67.381  1.00 32.27 ? 147 VAL   B CA  1 
ATOM   2035 C  C   . VAL   B 1 54  ? -4.702  0.336   68.478  1.00 34.81 ? 147 VAL   B C   1 
ATOM   2036 O  O   . VAL   B 1 54  ? -5.232  1.492   68.473  1.00 34.29 ? 147 VAL   B O   1 
ATOM   2037 C  CB  . VAL   B 1 54  ? -2.249  0.340   67.809  1.00 31.79 ? 147 VAL   B CB  1 
ATOM   2038 C  CG1 . VAL   B 1 54  ? -1.233  -0.292  66.875  1.00 30.72 ? 147 VAL   B CG1 1 
ATOM   2039 C  CG2 . VAL   B 1 54  ? -2.020  1.842   67.921  1.00 31.47 ? 147 VAL   B CG2 1 
ATOM   2040 N  N   . ASP   B 1 55  ? -4.982  -0.638  69.351  1.00 36.78 ? 148 ASP   B N   1 
ATOM   2041 C  CA  . ASP   B 1 55  ? -5.832  -0.465  70.559  1.00 39.40 ? 148 ASP   B CA  1 
ATOM   2042 C  C   . ASP   B 1 55  ? -4.999  0.236   71.637  1.00 40.22 ? 148 ASP   B C   1 
ATOM   2043 O  O   . ASP   B 1 55  ? -5.573  0.978   72.440  1.00 41.20 ? 148 ASP   B O   1 
ATOM   2044 C  CB  . ASP   B 1 55  ? -6.361  -1.808  71.074  1.00 41.15 ? 148 ASP   B CB  1 
ATOM   2045 C  CG  . ASP   B 1 55  ? -7.360  -2.480  70.147  1.00 42.01 ? 148 ASP   B CG  1 
ATOM   2046 O  OD1 . ASP   B 1 55  ? -8.035  -1.754  69.381  1.00 41.06 ? 148 ASP   B OD1 1 
ATOM   2047 O  OD2 . ASP   B 1 55  ? -7.486  -3.731  70.231  1.00 44.79 ? 148 ASP   B OD2 1 
ATOM   2048 N  N   . SER   B 1 56  ? -3.688  -0.012  71.652  1.00 41.13 ? 149 SER   B N   1 
ATOM   2049 C  CA  . SER   B 1 56  ? -2.725  0.552   72.633  1.00 42.16 ? 149 SER   B CA  1 
ATOM   2050 C  C   . SER   B 1 56  ? -1.421  0.909   71.921  1.00 40.79 ? 149 SER   B C   1 
ATOM   2051 O  O   . SER   B 1 56  ? -1.025  0.177   70.990  1.00 39.77 ? 149 SER   B O   1 
ATOM   2052 C  CB  . SER   B 1 56  ? -2.498  -0.395  73.804  1.00 43.72 ? 149 SER   B CB  1 
ATOM   2053 O  OG  . SER   B 1 56  ? -2.256  -1.719  73.348  1.00 44.50 ? 149 SER   B OG  1 
ATOM   2054 N  N   . THR   B 1 57  ? -0.781  1.998   72.357  1.00 40.72 ? 150 THR   B N   1 
ATOM   2055 C  CA  . THR   B 1 57  ? 0.469   2.552   71.774  1.00 39.97 ? 150 THR   B CA  1 
ATOM   2056 C  C   . THR   B 1 57  ? 1.625   1.578   71.988  1.00 39.89 ? 150 THR   B C   1 
ATOM   2057 O  O   . THR   B 1 57  ? 2.027   1.351   73.120  1.00 40.10 ? 150 THR   B O   1 
ATOM   2058 C  CB  . THR   B 1 57  ? 0.756   3.945   72.343  1.00 41.08 ? 150 THR   B CB  1 
ATOM   2059 O  OG1 . THR   B 1 57  ? -0.412  4.707   72.030  1.00 41.54 ? 150 THR   B OG1 1 
ATOM   2060 C  CG2 . THR   B 1 57  ? 1.973   4.621   71.746  1.00 41.13 ? 150 THR   B CG2 1 
ATOM   2061 N  N   . PRO   B 1 58  ? 2.188   0.987   70.905  1.00 37.86 ? 151 PRO   B N   1 
ATOM   2062 C  CA  . PRO   B 1 58  ? 3.380   0.145   71.002  1.00 37.69 ? 151 PRO   B CA  1 
ATOM   2063 C  C   . PRO   B 1 58  ? 4.547   0.857   71.684  1.00 37.54 ? 151 PRO   B C   1 
ATOM   2064 O  O   . PRO   B 1 58  ? 4.585   2.089   71.747  1.00 37.22 ? 151 PRO   B O   1 
ATOM   2065 C  CB  . PRO   B 1 58  ? 3.733   -0.125  69.525  1.00 36.21 ? 151 PRO   B CB  1 
ATOM   2066 C  CG  . PRO   B 1 58  ? 2.420   -0.010  68.814  1.00 36.47 ? 151 PRO   B CG  1 
ATOM   2067 C  CD  . PRO   B 1 58  ? 1.693   1.107   69.523  1.00 36.70 ? 151 PRO   B CD  1 
ATOM   2068 N  N   . PRO   B 1 59  ? 5.539   0.108   72.201  1.00 38.03 ? 152 PRO   B N   1 
ATOM   2069 C  CA  . PRO   B 1 59  ? 6.663   0.694   72.932  1.00 38.84 ? 152 PRO   B CA  1 
ATOM   2070 C  C   . PRO   B 1 59  ? 7.552   1.583   72.059  1.00 38.09 ? 152 PRO   B C   1 
ATOM   2071 O  O   . PRO   B 1 59  ? 7.541   1.457   70.823  1.00 35.61 ? 152 PRO   B O   1 
ATOM   2072 C  CB  . PRO   B 1 59  ? 7.438   -0.544  73.433  1.00 40.18 ? 152 PRO   B CB  1 
ATOM   2073 C  CG  . PRO   B 1 59  ? 7.098   -1.636  72.459  1.00 39.50 ? 152 PRO   B CG  1 
ATOM   2074 C  CD  . PRO   B 1 59  ? 5.658   -1.356  72.096  1.00 38.77 ? 152 PRO   B CD  1 
ATOM   2075 N  N   . PRO   B 1 60  ? 8.348   2.496   72.664  1.00 38.78 ? 153 PRO   B N   1 
ATOM   2076 C  CA  . PRO   B 1 60  ? 9.295   3.311   71.908  1.00 38.80 ? 153 PRO   B CA  1 
ATOM   2077 C  C   . PRO   B 1 60  ? 10.231  2.434   71.066  1.00 38.18 ? 153 PRO   B C   1 
ATOM   2078 O  O   . PRO   B 1 60  ? 10.609  1.360   71.552  1.00 40.42 ? 153 PRO   B O   1 
ATOM   2079 C  CB  . PRO   B 1 60  ? 10.094  4.072   72.987  1.00 40.28 ? 153 PRO   B CB  1 
ATOM   2080 C  CG  . PRO   B 1 60  ? 9.192   4.082   74.201  1.00 41.22 ? 153 PRO   B CG  1 
ATOM   2081 C  CD  . PRO   B 1 60  ? 8.397   2.795   74.105  1.00 40.87 ? 153 PRO   B CD  1 
ATOM   2082 N  N   . GLY   B 1 61  ? 10.552  2.883   69.842  1.00 36.16 ? 154 GLY   B N   1 
ATOM   2083 C  CA  . GLY   B 1 61  ? 11.479  2.204   68.915  1.00 34.44 ? 154 GLY   B CA  1 
ATOM   2084 C  C   . GLY   B 1 61  ? 10.794  1.136   68.085  1.00 32.31 ? 154 GLY   B C   1 
ATOM   2085 O  O   . GLY   B 1 61  ? 11.505  0.453   67.337  1.00 31.64 ? 154 GLY   B O   1 
ATOM   2086 N  N   . THR   B 1 62  ? 9.478   0.974   68.242  1.00 31.04 ? 155 THR   B N   1 
ATOM   2087 C  CA  . THR   B 1 62  ? 8.647   0.112   67.367  1.00 29.87 ? 155 THR   B CA  1 
ATOM   2088 C  C   . THR   B 1 62  ? 8.862   0.505   65.901  1.00 28.66 ? 155 THR   B C   1 
ATOM   2089 O  O   . THR   B 1 62  ? 8.963   1.723   65.611  1.00 27.05 ? 155 THR   B O   1 
ATOM   2090 C  CB  . THR   B 1 62  ? 7.163   0.193   67.723  1.00 30.13 ? 155 THR   B CB  1 
ATOM   2091 O  OG1 . THR   B 1 62  ? 7.022   -0.298  69.049  1.00 31.45 ? 155 THR   B OG1 1 
ATOM   2092 C  CG2 . THR   B 1 62  ? 6.302   -0.657  66.823  1.00 29.66 ? 155 THR   B CG2 1 
ATOM   2093 N  N   . ARG   B 1 63  ? 8.929   -0.491  65.011  1.00 27.72 ? 156 ARG   B N   1 
ATOM   2094 C  CA  . ARG   B 1 63  ? 9.195   -0.260  63.573  1.00 27.09 ? 156 ARG   B CA  1 
ATOM   2095 C  C   . ARG   B 1 63  ? 8.087   -0.918  62.743  1.00 26.36 ? 156 ARG   B C   1 
ATOM   2096 O  O   . ARG   B 1 63  ? 7.453   -1.881  63.235  1.00 26.18 ? 156 ARG   B O   1 
ATOM   2097 C  CB  . ARG   B 1 63  ? 10.623  -0.713  63.245  1.00 27.28 ? 156 ARG   B CB  1 
ATOM   2098 C  CG  . ARG   B 1 63  ? 11.649  0.377   63.518  1.00 27.59 ? 156 ARG   B CG  1 
ATOM   2099 C  CD  . ARG   B 1 63  ? 13.029  -0.075  63.883  1.00 28.15 ? 156 ARG   B CD  1 
ATOM   2100 N  NE  . ARG   B 1 63  ? 13.633  -1.043  62.963  1.00 27.96 ? 156 ARG   B NE  1 
ATOM   2101 C  CZ  . ARG   B 1 63  ? 14.482  -0.766  61.981  1.00 27.66 ? 156 ARG   B CZ  1 
ATOM   2102 N  NH1 . ARG   B 1 63  ? 14.814  0.487   61.691  1.00 27.41 ? 156 ARG   B NH1 1 
ATOM   2103 N  NH2 . ARG   B 1 63  ? 14.969  -1.758  61.250  1.00 27.66 ? 156 ARG   B NH2 1 
ATOM   2104 N  N   . VAL   B 1 64  ? 7.876   -0.398  61.529  1.00 25.80 ? 157 VAL   B N   1 
ATOM   2105 C  CA  . VAL   B 1 64  ? 6.863   -0.890  60.552  1.00 25.07 ? 157 VAL   B CA  1 
ATOM   2106 C  C   . VAL   B 1 64  ? 7.576   -1.267  59.254  1.00 24.82 ? 157 VAL   B C   1 
ATOM   2107 O  O   . VAL   B 1 64  ? 8.137   -0.375  58.595  1.00 23.79 ? 157 VAL   B O   1 
ATOM   2108 C  CB  . VAL   B 1 64  ? 5.771   0.165   60.303  1.00 24.66 ? 157 VAL   B CB  1 
ATOM   2109 C  CG1 . VAL   B 1 64  ? 4.610   -0.423  59.508  1.00 24.64 ? 157 VAL   B CG1 1 
ATOM   2110 C  CG2 . VAL   B 1 64  ? 5.283   0.744   61.611  1.00 24.94 ? 157 VAL   B CG2 1 
ATOM   2111 N  N   . ARG   B 1 65  ? 7.558   -2.554  58.915  1.00 24.06 ? 158 ARG   B N   1 
ATOM   2112 C  CA  . ARG   B 1 65  ? 8.163   -3.128  57.693  1.00 24.01 ? 158 ARG   B CA  1 
ATOM   2113 C  C   . ARG   B 1 65  ? 7.048   -3.487  56.706  1.00 24.14 ? 158 ARG   B C   1 
ATOM   2114 O  O   . ARG   B 1 65  ? 5.971   -3.962  57.142  1.00 24.59 ? 158 ARG   B O   1 
ATOM   2115 C  CB  . ARG   B 1 65  ? 8.989   -4.363  58.066  1.00 24.32 ? 158 ARG   B CB  1 
ATOM   2116 C  CG  . ARG   B 1 65  ? 9.740   -4.993  56.905  1.00 24.19 ? 158 ARG   B CG  1 
ATOM   2117 C  CD  . ARG   B 1 65  ? 10.568  -6.167  57.392  1.00 24.58 ? 158 ARG   B CD  1 
ATOM   2118 N  NE  . ARG   B 1 65  ? 11.413  -5.804  58.525  1.00 24.81 ? 158 ARG   B NE  1 
ATOM   2119 C  CZ  . ARG   B 1 65  ? 12.632  -5.275  58.450  1.00 24.43 ? 158 ARG   B CZ  1 
ATOM   2120 N  NH1 . ARG   B 1 65  ? 13.165  -4.957  57.288  1.00 24.79 ? 158 ARG   B NH1 1 
ATOM   2121 N  NH2 . ARG   B 1 65  ? 13.319  -5.038  59.556  1.00 25.00 ? 158 ARG   B NH2 1 
ATOM   2122 N  N   . ALA   B 1 66  ? 7.299   -3.217  55.430  1.00 24.43 ? 159 ALA   B N   1 
ATOM   2123 C  CA  . ALA   B 1 66  ? 6.496   -3.637  54.258  1.00 25.43 ? 159 ALA   B CA  1 
ATOM   2124 C  C   . ALA   B 1 66  ? 7.368   -4.545  53.388  1.00 26.38 ? 159 ALA   B C   1 
ATOM   2125 O  O   . ALA   B 1 66  ? 8.562   -4.219  53.196  1.00 27.02 ? 159 ALA   B O   1 
ATOM   2126 C  CB  . ALA   B 1 66  ? 6.017   -2.425  53.500  1.00 24.47 ? 159 ALA   B CB  1 
ATOM   2127 N  N   . MET   B 1 67  ? 6.783   -5.632  52.876  1.00 28.27 ? 160 MET   B N   1 
ATOM   2128 C  CA  . MET   B 1 67  ? 7.478   -6.633  52.020  1.00 29.62 ? 160 MET   B CA  1 
ATOM   2129 C  C   . MET   B 1 67  ? 6.454   -7.244  51.057  1.00 29.51 ? 160 MET   B C   1 
ATOM   2130 O  O   . MET   B 1 67  ? 5.324   -7.533  51.495  1.00 28.86 ? 160 MET   B O   1 
ATOM   2131 C  CB  . MET   B 1 67  ? 8.105   -7.747  52.869  1.00 31.76 ? 160 MET   B CB  1 
ATOM   2132 C  CG  . MET   B 1 67  ? 8.781   -8.835  52.054  1.00 34.07 ? 160 MET   B CG  1 
ATOM   2133 S  SD  . MET   B 1 67  ? 9.330   -10.238 53.079  1.00 38.27 ? 160 MET   B SD  1 
ATOM   2134 C  CE  . MET   B 1 67  ? 10.570  -9.488  54.134  1.00 37.76 ? 160 MET   B CE  1 
ATOM   2135 N  N   . ALA   B 1 68  ? 6.832   -7.400  49.791  1.00 29.53 ? 161 ALA   B N   1 
ATOM   2136 C  CA  . ALA   B 1 68  ? 6.002   -8.024  48.747  1.00 30.09 ? 161 ALA   B CA  1 
ATOM   2137 C  C   . ALA   B 1 68  ? 6.412   -9.490  48.597  1.00 31.00 ? 161 ALA   B C   1 
ATOM   2138 O  O   . ALA   B 1 68  ? 7.605   -9.791  48.677  1.00 30.14 ? 161 ALA   B O   1 
ATOM   2139 C  CB  . ALA   B 1 68  ? 6.145   -7.283  47.445  1.00 30.29 ? 161 ALA   B CB  1 
ATOM   2140 N  N   . ILE   B 1 69  ? 5.425   -10.360 48.427  1.00 32.70 ? 162 ILE   B N   1 
ATOM   2141 C  CA  . ILE   B 1 69  ? 5.615   -11.762 47.957  1.00 34.82 ? 162 ILE   B CA  1 
ATOM   2142 C  C   . ILE   B 1 69  ? 4.604   -11.994 46.833  1.00 36.13 ? 162 ILE   B C   1 
ATOM   2143 O  O   . ILE   B 1 69  ? 3.602   -11.255 46.796  1.00 35.32 ? 162 ILE   B O   1 
ATOM   2144 C  CB  . ILE   B 1 69  ? 5.460   -12.771 49.111  1.00 35.57 ? 162 ILE   B CB  1 
ATOM   2145 C  CG1 . ILE   B 1 69  ? 4.047   -12.789 49.706  1.00 35.72 ? 162 ILE   B CG1 1 
ATOM   2146 C  CG2 . ILE   B 1 69  ? 6.497   -12.518 50.189  1.00 34.83 ? 162 ILE   B CG2 1 
ATOM   2147 C  CD1 . ILE   B 1 69  ? 3.816   -13.922 50.687  1.00 36.44 ? 162 ILE   B CD1 1 
ATOM   2148 N  N   . TYR   B 1 70  ? 4.883   -12.957 45.940  1.00 38.48 ? 163 TYR   B N   1 
ATOM   2149 C  CA  . TYR   B 1 70  ? 3.922   -13.444 44.919  1.00 40.09 ? 163 TYR   B CA  1 
ATOM   2150 C  C   . TYR   B 1 70  ? 2.852   -14.263 45.644  1.00 41.49 ? 163 TYR   B C   1 
ATOM   2151 O  O   . TYR   B 1 70  ? 3.175   -14.960 46.613  1.00 41.35 ? 163 TYR   B O   1 
ATOM   2152 C  CB  . TYR   B 1 70  ? 4.641   -14.229 43.822  1.00 41.82 ? 163 TYR   B CB  1 
ATOM   2153 C  CG  . TYR   B 1 70  ? 5.436   -13.343 42.903  1.00 41.22 ? 163 TYR   B CG  1 
ATOM   2154 C  CD1 . TYR   B 1 70  ? 4.792   -12.426 42.089  1.00 41.03 ? 163 TYR   B CD1 1 
ATOM   2155 C  CD2 . TYR   B 1 70  ? 6.818   -13.397 42.858  1.00 41.42 ? 163 TYR   B CD2 1 
ATOM   2156 C  CE1 . TYR   B 1 70  ? 5.499   -11.589 41.237  1.00 41.09 ? 163 TYR   B CE1 1 
ATOM   2157 C  CE2 . TYR   B 1 70  ? 7.543   -12.563 42.024  1.00 41.35 ? 163 TYR   B CE2 1 
ATOM   2158 C  CZ  . TYR   B 1 70  ? 6.882   -11.650 41.214  1.00 41.02 ? 163 TYR   B CZ  1 
ATOM   2159 O  OH  . TYR   B 1 70  ? 7.545   -10.809 40.365  1.00 41.20 ? 163 TYR   B OH  1 
ATOM   2160 N  N   . LYS   B 1 71  ? 1.602   -14.132 45.203  1.00 42.58 ? 164 LYS   B N   1 
ATOM   2161 C  CA  . LYS   B 1 71  ? 0.433   -14.746 45.868  1.00 43.77 ? 164 LYS   B CA  1 
ATOM   2162 C  C   . LYS   B 1 71  ? 0.370   -16.229 45.509  1.00 46.54 ? 164 LYS   B C   1 
ATOM   2163 O  O   . LYS   B 1 71  ? 0.051   -17.028 46.406  1.00 47.37 ? 164 LYS   B O   1 
ATOM   2164 C  CB  . LYS   B 1 71  ? -0.851  -14.015 45.476  1.00 43.61 ? 164 LYS   B CB  1 
ATOM   2165 C  CG  . LYS   B 1 71  ? -2.076  -14.460 46.256  1.00 43.75 ? 164 LYS   B CG  1 
ATOM   2166 C  CD  . LYS   B 1 71  ? -3.333  -13.783 45.816  1.00 43.53 ? 164 LYS   B CD  1 
ATOM   2167 C  CE  . LYS   B 1 71  ? -4.444  -13.980 46.820  1.00 43.95 ? 164 LYS   B CE  1 
ATOM   2168 N  NZ  . LYS   B 1 71  ? -5.641  -13.180 46.479  1.00 43.77 ? 164 LYS   B NZ  1 
ATOM   2169 N  N   . GLN   B 1 72  ? 0.669   -16.562 44.252  1.00 48.46 ? 165 GLN   B N   1 
ATOM   2170 C  CA  . GLN   B 1 72  ? 0.540   -17.937 43.692  1.00 51.04 ? 165 GLN   B CA  1 
ATOM   2171 C  C   . GLN   B 1 72  ? 1.658   -18.823 44.252  1.00 51.79 ? 165 GLN   B C   1 
ATOM   2172 O  O   . GLN   B 1 72  ? 2.808   -18.346 44.334  1.00 50.30 ? 165 GLN   B O   1 
ATOM   2173 C  CB  . GLN   B 1 72  ? 0.608   -17.893 42.164  1.00 52.61 ? 165 GLN   B CB  1 
ATOM   2174 C  CG  . GLN   B 1 72  ? -0.581  -17.198 41.515  1.00 53.07 ? 165 GLN   B CG  1 
ATOM   2175 C  CD  . GLN   B 1 72  ? -0.253  -16.698 40.128  1.00 53.63 ? 165 GLN   B CD  1 
ATOM   2176 O  OE1 . GLN   B 1 72  ? 0.759   -16.034 39.921  1.00 54.15 ? 165 GLN   B OE1 1 
ATOM   2177 N  NE2 . GLN   B 1 72  ? -1.107  -16.993 39.162  1.00 54.66 ? 165 GLN   B NE2 1 
ATOM   2178 N  N   . SER   B 1 73  ? 1.328   -20.074 44.590  1.00 53.59 ? 166 SER   B N   1 
ATOM   2179 C  CA  . SER   B 1 73  ? 2.221   -21.024 45.300  1.00 54.63 ? 166 SER   B CA  1 
ATOM   2180 C  C   . SER   B 1 73  ? 3.433   -21.367 44.426  1.00 56.10 ? 166 SER   B C   1 
ATOM   2181 O  O   . SER   B 1 73  ? 4.513   -21.597 44.996  1.00 55.53 ? 166 SER   B O   1 
ATOM   2182 C  CB  . SER   B 1 73  ? 1.478   -22.267 45.722  1.00 56.57 ? 166 SER   B CB  1 
ATOM   2183 O  OG  . SER   B 1 73  ? 0.837   -22.882 44.616  1.00 57.69 ? 166 SER   B OG  1 
ATOM   2184 N  N   . GLN   B 1 74  ? 3.263   -21.392 43.099  1.00 57.63 ? 167 GLN   B N   1 
ATOM   2185 C  CA  . GLN   B 1 74  ? 4.331   -21.798 42.144  1.00 59.34 ? 167 GLN   B CA  1 
ATOM   2186 C  C   . GLN   B 1 74  ? 5.330   -20.648 41.930  1.00 57.91 ? 167 GLN   B C   1 
ATOM   2187 O  O   . GLN   B 1 74  ? 6.385   -20.909 41.333  1.00 60.02 ? 167 GLN   B O   1 
ATOM   2188 C  CB  . GLN   B 1 74  ? 3.735   -22.292 40.824  1.00 61.52 ? 167 GLN   B CB  1 
ATOM   2189 C  CG  . GLN   B 1 74  ? 2.985   -21.236 40.027  1.00 60.74 ? 167 GLN   B CG  1 
ATOM   2190 C  CD  . GLN   B 1 74  ? 1.499   -21.226 40.278  1.00 60.93 ? 167 GLN   B CD  1 
ATOM   2191 O  OE1 . GLN   B 1 74  ? 1.033   -21.474 41.390  1.00 61.09 ? 167 GLN   B OE1 1 
ATOM   2192 N  NE2 . GLN   B 1 74  ? 0.741   -20.951 39.228  1.00 61.23 ? 167 GLN   B NE2 1 
ATOM   2193 N  N   . HIS   B 1 75  ? 5.031   -19.430 42.396  1.00 55.93 ? 168 HIS   B N   1 
ATOM   2194 C  CA  . HIS   B 1 75  ? 5.894   -18.228 42.210  1.00 54.26 ? 168 HIS   B CA  1 
ATOM   2195 C  C   . HIS   B 1 75  ? 6.398   -17.684 43.556  1.00 51.85 ? 168 HIS   B C   1 
ATOM   2196 O  O   . HIS   B 1 75  ? 7.138   -16.689 43.544  1.00 51.24 ? 168 HIS   B O   1 
ATOM   2197 C  CB  . HIS   B 1 75  ? 5.135   -17.141 41.440  1.00 54.02 ? 168 HIS   B CB  1 
ATOM   2198 C  CG  . HIS   B 1 75  ? 4.740   -17.532 40.055  1.00 56.08 ? 168 HIS   B CG  1 
ATOM   2199 N  ND1 . HIS   B 1 75  ? 5.657   -17.957 39.115  1.00 57.52 ? 168 HIS   B ND1 1 
ATOM   2200 C  CD2 . HIS   B 1 75  ? 3.537   -17.544 39.438  1.00 57.46 ? 168 HIS   B CD2 1 
ATOM   2201 C  CE1 . HIS   B 1 75  ? 5.035   -18.236 37.985  1.00 59.17 ? 168 HIS   B CE1 1 
ATOM   2202 N  NE2 . HIS   B 1 75  ? 3.731   -17.983 38.153  1.00 58.95 ? 168 HIS   B NE2 1 
ATOM   2203 N  N   . MET   B 1 76  ? 6.037   -18.326 44.665  1.00 51.32 ? 169 MET   B N   1 
ATOM   2204 C  CA  . MET   B 1 76  ? 6.100   -17.737 46.031  1.00 49.21 ? 169 MET   B CA  1 
ATOM   2205 C  C   . MET   B 1 76  ? 7.547   -17.609 46.519  1.00 48.19 ? 169 MET   B C   1 
ATOM   2206 O  O   . MET   B 1 76  ? 7.827   -16.672 47.292  1.00 45.96 ? 169 MET   B O   1 
ATOM   2207 C  CB  . MET   B 1 76  ? 5.305   -18.603 47.010  1.00 49.93 ? 169 MET   B CB  1 
ATOM   2208 C  CG  . MET   B 1 76  ? 4.805   -17.875 48.232  1.00 48.79 ? 169 MET   B CG  1 
ATOM   2209 S  SD  . MET   B 1 76  ? 3.024   -18.250 48.490  1.00 49.82 ? 169 MET   B SD  1 
ATOM   2210 C  CE  . MET   B 1 76  ? 3.098   -20.036 48.635  1.00 52.02 ? 169 MET   B CE  1 
ATOM   2211 N  N   . THR   B 1 77  ? 8.430   -18.511 46.083  1.00 48.99 ? 170 THR   B N   1 
ATOM   2212 C  CA  . THR   B 1 77  ? 9.873   -18.538 46.457  1.00 48.45 ? 170 THR   B CA  1 
ATOM   2213 C  C   . THR   B 1 77  ? 10.663  -17.540 45.607  1.00 47.50 ? 170 THR   B C   1 
ATOM   2214 O  O   . THR   B 1 77  ? 11.847  -17.370 45.899  1.00 48.40 ? 170 THR   B O   1 
ATOM   2215 C  CB  . THR   B 1 77  ? 10.496  -19.931 46.300  1.00 50.35 ? 170 THR   B CB  1 
ATOM   2216 O  OG1 . THR   B 1 77  ? 10.582  -20.188 44.900  1.00 51.27 ? 170 THR   B OG1 1 
ATOM   2217 C  CG2 . THR   B 1 77  ? 9.714   -21.007 47.015  1.00 51.17 ? 170 THR   B CG2 1 
ATOM   2218 N  N   . GLU   B 1 78  ? 10.059  -16.944 44.577  1.00 47.42 ? 171 GLU   B N   1 
ATOM   2219 C  CA  . GLU   B 1 78  ? 10.704  -15.916 43.718  1.00 47.20 ? 171 GLU   B CA  1 
ATOM   2220 C  C   . GLU   B 1 78  ? 10.622  -14.570 44.447  1.00 44.21 ? 171 GLU   B C   1 
ATOM   2221 O  O   . GLU   B 1 78  ? 9.526   -14.226 44.959  1.00 42.96 ? 171 GLU   B O   1 
ATOM   2222 C  CB  . GLU   B 1 78  ? 10.040  -15.852 42.340  1.00 49.39 ? 171 GLU   B CB  1 
ATOM   2223 C  CG  . GLU   B 1 78  ? 10.704  -14.881 41.387  1.00 50.64 ? 171 GLU   B CG  1 
ATOM   2224 C  CD  . GLU   B 1 78  ? 10.264  -14.971 39.933  1.00 53.23 ? 171 GLU   B CD  1 
ATOM   2225 O  OE1 . GLU   B 1 78  ? 10.236  -16.092 39.394  1.00 55.80 ? 171 GLU   B OE1 1 
ATOM   2226 O  OE2 . GLU   B 1 78  ? 9.993   -13.917 39.326  1.00 54.73 ? 171 GLU   B OE2 1 
ATOM   2227 N  N   . VAL   B 1 79  ? 11.743  -13.839 44.510  1.00 42.69 ? 172 VAL   B N   1 
ATOM   2228 C  CA  . VAL   B 1 79  ? 11.810  -12.486 45.135  1.00 40.50 ? 172 VAL   B CA  1 
ATOM   2229 C  C   . VAL   B 1 79  ? 11.087  -11.511 44.209  1.00 39.55 ? 172 VAL   B C   1 
ATOM   2230 O  O   . VAL   B 1 79  ? 11.372  -11.508 42.990  1.00 39.72 ? 172 VAL   B O   1 
ATOM   2231 C  CB  . VAL   B 1 79  ? 13.256  -12.029 45.398  1.00 40.15 ? 172 VAL   B CB  1 
ATOM   2232 C  CG1 . VAL   B 1 79  ? 13.319  -10.574 45.848  1.00 38.97 ? 172 VAL   B CG1 1 
ATOM   2233 C  CG2 . VAL   B 1 79  ? 13.922  -12.931 46.422  1.00 41.02 ? 172 VAL   B CG2 1 
ATOM   2234 N  N   . VAL   B 1 80  ? 10.202  -10.694 44.776  1.00 38.46 ? 173 VAL   B N   1 
ATOM   2235 C  CA  . VAL   B 1 80  ? 9.480   -9.637  44.027  1.00 38.19 ? 173 VAL   B CA  1 
ATOM   2236 C  C   . VAL   B 1 80  ? 10.436  -8.457  43.874  1.00 38.48 ? 173 VAL   B C   1 
ATOM   2237 O  O   . VAL   B 1 80  ? 10.863  -7.907  44.916  1.00 36.49 ? 173 VAL   B O   1 
ATOM   2238 C  CB  . VAL   B 1 80  ? 8.171   -9.225  44.727  1.00 37.06 ? 173 VAL   B CB  1 
ATOM   2239 C  CG1 . VAL   B 1 80  ? 7.474   -8.135  43.932  1.00 36.93 ? 173 VAL   B CG1 1 
ATOM   2240 C  CG2 . VAL   B 1 80  ? 7.220   -10.404 44.927  1.00 37.69 ? 173 VAL   B CG2 1 
ATOM   2241 N  N   . ARG   B 1 81  ? 10.740  -8.087  42.626  1.00 40.18 ? 174 ARG   B N   1 
ATOM   2242 C  CA  . ARG   B 1 81  ? 11.621  -6.939  42.287  1.00 41.37 ? 174 ARG   B CA  1 
ATOM   2243 C  C   . ARG   B 1 81  ? 11.041  -6.197  41.083  1.00 41.67 ? 174 ARG   B C   1 
ATOM   2244 O  O   . ARG   B 1 81  ? 10.153  -6.736  40.404  1.00 41.20 ? 174 ARG   B O   1 
ATOM   2245 C  CB  . ARG   B 1 81  ? 13.050  -7.416  41.995  1.00 43.60 ? 174 ARG   B CB  1 
ATOM   2246 C  CG  . ARG   B 1 81  ? 13.125  -8.570  41.000  1.00 45.95 ? 174 ARG   B CG  1 
ATOM   2247 C  CD  . ARG   B 1 81  ? 14.556  -8.967  40.655  1.00 48.63 ? 174 ARG   B CD  1 
ATOM   2248 N  NE  . ARG   B 1 81  ? 15.117  -9.931  41.606  1.00 48.95 ? 174 ARG   B NE  1 
ATOM   2249 C  CZ  . ARG   B 1 81  ? 15.908  -9.646  42.640  1.00 48.94 ? 174 ARG   B CZ  1 
ATOM   2250 N  NH1 . ARG   B 1 81  ? 16.290  -8.398  42.875  1.00 48.26 ? 174 ARG   B NH1 1 
ATOM   2251 N  NH2 . ARG   B 1 81  ? 16.347  -10.629 43.413  1.00 49.22 ? 174 ARG   B NH2 1 
ATOM   2252 N  N   . ARG   B 1 82  ? 11.563  -5.001  40.822  1.00 41.90 ? 175 ARG   B N   1 
ATOM   2253 C  CA  . ARG   B 1 82  ? 11.231  -4.214  39.615  1.00 43.05 ? 175 ARG   B CA  1 
ATOM   2254 C  C   . ARG   B 1 82  ? 11.765  -4.932  38.371  1.00 44.53 ? 175 ARG   B C   1 
ATOM   2255 O  O   . ARG   B 1 82  ? 12.745  -5.705  38.478  1.00 45.22 ? 175 ARG   B O   1 
ATOM   2256 C  CB  . ARG   B 1 82  ? 11.808  -2.802  39.710  1.00 43.23 ? 175 ARG   B CB  1 
ATOM   2257 C  CG  . ARG   B 1 82  ? 11.278  -2.017  40.895  1.00 42.48 ? 175 ARG   B CG  1 
ATOM   2258 C  CD  . ARG   B 1 82  ? 11.956  -0.669  40.977  1.00 43.01 ? 175 ARG   B CD  1 
ATOM   2259 N  NE  . ARG   B 1 82  ? 11.283  0.323   40.163  1.00 44.65 ? 175 ARG   B NE  1 
ATOM   2260 C  CZ  . ARG   B 1 82  ? 11.753  1.547   39.927  1.00 45.27 ? 175 ARG   B CZ  1 
ATOM   2261 N  NH1 . ARG   B 1 82  ? 12.914  1.935   40.440  1.00 44.40 ? 175 ARG   B NH1 1 
ATOM   2262 N  NH2 . ARG   B 1 82  ? 11.056  2.376   39.164  1.00 46.04 ? 175 ARG   B NH2 1 
ATOM   2263 N  N   . CYS   B 1 83  ? 11.140  -4.656  37.227  1.00 44.75 ? 176 CYS   B N   1 
ATOM   2264 C  CA  . CYS   B 1 83  ? 11.609  -5.105  35.892  1.00 46.10 ? 176 CYS   B CA  1 
ATOM   2265 C  C   . CYS   B 1 83  ? 12.901  -4.366  35.557  1.00 45.74 ? 176 CYS   B C   1 
ATOM   2266 O  O   . CYS   B 1 83  ? 13.158  -3.292  36.090  1.00 44.24 ? 176 CYS   B O   1 
ATOM   2267 C  CB  . CYS   B 1 83  ? 10.531  -4.831  34.848  1.00 47.09 ? 176 CYS   B CB  1 
ATOM   2268 S  SG  . CYS   B 1 83  ? 10.214  -3.138  34.546  1.00 47.73 ? 176 CYS   B SG  1 
ATOM   2269 N  N   . PRO   B 1 84  ? 13.761  -4.909  34.673  1.00 46.88 ? 177 PRO   B N   1 
ATOM   2270 C  CA  . PRO   B 1 84  ? 14.945  -4.186  34.218  1.00 47.29 ? 177 PRO   B CA  1 
ATOM   2271 C  C   . PRO   B 1 84  ? 14.625  -2.721  33.876  1.00 46.71 ? 177 PRO   B C   1 
ATOM   2272 O  O   . PRO   B 1 84  ? 15.299  -1.855  34.395  1.00 46.10 ? 177 PRO   B O   1 
ATOM   2273 C  CB  . PRO   B 1 84  ? 15.370  -4.995  32.982  1.00 49.64 ? 177 PRO   B CB  1 
ATOM   2274 C  CG  . PRO   B 1 84  ? 14.938  -6.410  33.299  1.00 49.86 ? 177 PRO   B CG  1 
ATOM   2275 C  CD  . PRO   B 1 84  ? 13.653  -6.249  34.080  1.00 48.28 ? 177 PRO   B CD  1 
ATOM   2276 N  N   . HIS   B 1 85  ? 13.582  -2.478  33.072  1.00 46.66 ? 178 HIS   B N   1 
ATOM   2277 C  CA  . HIS   B 1 85  ? 13.219  -1.136  32.543  1.00 46.99 ? 178 HIS   B CA  1 
ATOM   2278 C  C   . HIS   B 1 85  ? 13.074  -0.130  33.689  1.00 45.72 ? 178 HIS   B C   1 
ATOM   2279 O  O   . HIS   B 1 85  ? 13.724  0.932   33.614  1.00 46.46 ? 178 HIS   B O   1 
ATOM   2280 C  CB  . HIS   B 1 85  ? 11.943  -1.190  31.693  1.00 46.95 ? 178 HIS   B CB  1 
ATOM   2281 C  CG  . HIS   B 1 85  ? 11.377  0.156   31.391  1.00 46.74 ? 178 HIS   B CG  1 
ATOM   2282 N  ND1 . HIS   B 1 85  ? 12.005  1.063   30.560  1.00 48.11 ? 178 HIS   B ND1 1 
ATOM   2283 C  CD2 . HIS   B 1 85  ? 10.239  0.751   31.803  1.00 45.73 ? 178 HIS   B CD2 1 
ATOM   2284 C  CE1 . HIS   B 1 85  ? 11.273  2.157   30.469  1.00 48.09 ? 178 HIS   B CE1 1 
ATOM   2285 N  NE2 . HIS   B 1 85  ? 10.175  1.985   31.209  1.00 46.67 ? 178 HIS   B NE2 1 
ATOM   2286 N  N   . HIS   B 1 86  ? 12.241  -0.435  34.687  1.00 45.26 ? 179 HIS   B N   1 
ATOM   2287 C  CA  . HIS   B 1 86  ? 11.912  0.502   35.793  1.00 45.15 ? 179 HIS   B CA  1 
ATOM   2288 C  C   . HIS   B 1 86  ? 13.121  0.647   36.723  1.00 46.13 ? 179 HIS   B C   1 
ATOM   2289 O  O   . HIS   B 1 86  ? 13.328  1.770   37.229  1.00 46.20 ? 179 HIS   B O   1 
ATOM   2290 C  CB  . HIS   B 1 86  ? 10.626  0.090   36.514  1.00 43.85 ? 179 HIS   B CB  1 
ATOM   2291 C  CG  . HIS   B 1 86  ? 9.399   0.570   35.815  1.00 44.53 ? 179 HIS   B CG  1 
ATOM   2292 N  ND1 . HIS   B 1 86  ? 8.353   -0.267  35.475  1.00 44.26 ? 179 HIS   B ND1 1 
ATOM   2293 C  CD2 . HIS   B 1 86  ? 9.057   1.805   35.384  1.00 45.06 ? 179 HIS   B CD2 1 
ATOM   2294 C  CE1 . HIS   B 1 86  ? 7.422   0.438   34.859  1.00 45.20 ? 179 HIS   B CE1 1 
ATOM   2295 N  NE2 . HIS   B 1 86  ? 7.826   1.711   34.789  1.00 45.08 ? 179 HIS   B NE2 1 
ATOM   2296 N  N   . GLU   B 1 87  ? 13.905  -0.420  36.895  1.00 47.45 ? 180 GLU   B N   1 
ATOM   2297 C  CA  . GLU   B 1 87  ? 15.155  -0.408  37.705  1.00 48.38 ? 180 GLU   B CA  1 
ATOM   2298 C  C   . GLU   B 1 87  ? 16.115  0.662   37.170  1.00 50.39 ? 180 GLU   B C   1 
ATOM   2299 O  O   . GLU   B 1 87  ? 16.731  1.346   38.008  1.00 50.81 ? 180 GLU   B O   1 
ATOM   2300 C  CB  . GLU   B 1 87  ? 15.768  -1.812  37.729  1.00 48.25 ? 180 GLU   B CB  1 
ATOM   2301 C  CG  . GLU   B 1 87  ? 17.063  -1.929  38.497  1.00 48.34 ? 180 GLU   B CG  1 
ATOM   2302 C  CD  . GLU   B 1 87  ? 17.641  -3.338  38.462  0.70 48.91 ? 180 GLU   B CD  1 
ATOM   2303 O  OE1 . GLU   B 1 87  ? 16.912  -4.270  38.055  0.70 48.94 ? 180 GLU   B OE1 1 
ATOM   2304 O  OE2 . GLU   B 1 87  ? 18.821  -3.506  38.823  0.70 49.30 ? 180 GLU   B OE2 1 
ATOM   2305 N  N   . ARG   B 1 88  ? 16.197  0.854   35.843  1.00 53.30 ? 181 ARG   B N   1 
ATOM   2306 C  CA  . ARG   B 1 88  ? 17.158  1.801   35.199  1.00 55.02 ? 181 ARG   B CA  1 
ATOM   2307 C  C   . ARG   B 1 88  ? 16.546  3.211   35.050  1.00 55.84 ? 181 ARG   B C   1 
ATOM   2308 O  O   . ARG   B 1 88  ? 17.312  4.141   34.779  1.00 56.82 ? 181 ARG   B O   1 
ATOM   2309 C  CB  . ARG   B 1 88  ? 17.630  1.343   33.812  1.00 57.57 ? 181 ARG   B CB  1 
ATOM   2310 C  CG  . ARG   B 1 88  ? 17.814  -0.150  33.568  1.00 58.20 ? 181 ARG   B CG  1 
ATOM   2311 C  CD  . ARG   B 1 88  ? 18.611  -0.968  34.570  1.00 57.46 ? 181 ARG   B CD  1 
ATOM   2312 N  NE  . ARG   B 1 88  ? 18.274  -2.385  34.449  1.00 57.08 ? 181 ARG   B NE  1 
ATOM   2313 C  CZ  . ARG   B 1 88  ? 18.909  -3.392  35.057  1.00 57.53 ? 181 ARG   B CZ  1 
ATOM   2314 N  NH1 . ARG   B 1 88  ? 18.498  -4.637  34.872  1.00 57.76 ? 181 ARG   B NH1 1 
ATOM   2315 N  NH2 . ARG   B 1 88  ? 19.946  -3.167  35.849  1.00 57.34 ? 181 ARG   B NH2 1 
ATOM   2316 N  N   . CYS   B 1 89  ? 15.228  3.369   35.190  1.00 55.66 ? 182 CYS   B N   1 
ATOM   2317 C  CA  . CYS   B 1 89  ? 14.513  4.644   34.929  1.00 57.14 ? 182 CYS   B CA  1 
ATOM   2318 C  C   . CYS   B 1 89  ? 14.830  5.652   36.039  1.00 55.98 ? 182 CYS   B C   1 
ATOM   2319 O  O   . CYS   B 1 89  ? 14.968  5.245   37.199  1.00 55.29 ? 182 CYS   B O   1 
ATOM   2320 C  CB  . CYS   B 1 89  ? 13.012  4.409   34.783  1.00 57.71 ? 182 CYS   B CB  1 
ATOM   2321 S  SG  . CYS   B 1 89  ? 12.550  3.983   33.081  1.00 62.53 ? 182 CYS   B SG  1 
ATOM   2322 N  N   . SER   B 1 90  ? 14.870  6.939   35.690  1.00 56.94 ? 183 SER   B N   1 
ATOM   2323 C  CA  . SER   B 1 90  ? 15.043  8.095   36.613  1.00 55.89 ? 183 SER   B CA  1 
ATOM   2324 C  C   . SER   B 1 90  ? 13.757  8.350   37.411  1.00 54.03 ? 183 SER   B C   1 
ATOM   2325 O  O   . SER   B 1 90  ? 13.216  9.487   37.298  1.00 56.53 ? 183 SER   B O   1 
ATOM   2326 C  CB  . SER   B 1 90  ? 15.434  9.345   35.866  1.00 57.59 ? 183 SER   B CB  1 
ATOM   2327 O  OG  . SER   B 1 90  ? 16.628  9.165   35.126  1.00 59.30 ? 183 SER   B OG  1 
ATOM   2328 N  N   . ASP   B 1 91  ? 13.284  7.361   38.190  1.00 50.57 ? 184 ASP   B N   1 
ATOM   2329 C  CA  . ASP   B 1 91  ? 12.154  7.522   39.155  1.00 48.61 ? 184 ASP   B CA  1 
ATOM   2330 C  C   . ASP   B 1 91  ? 12.701  7.251   40.568  1.00 45.50 ? 184 ASP   B C   1 
ATOM   2331 O  O   . ASP   B 1 91  ? 12.177  6.365   41.250  1.00 44.32 ? 184 ASP   B O   1 
ATOM   2332 C  CB  . ASP   B 1 91  ? 10.953  6.636   38.780  1.00 48.36 ? 184 ASP   B CB  1 
ATOM   2333 C  CG  . ASP   B 1 91  ? 9.599   7.344   38.730  1.00 49.27 ? 184 ASP   B CG  1 
ATOM   2334 O  OD1 . ASP   B 1 91  ? 9.532   8.567   39.059  1.00 49.85 ? 184 ASP   B OD1 1 
ATOM   2335 O  OD2 . ASP   B 1 91  ? 8.609   6.672   38.341  1.00 47.59 ? 184 ASP   B OD2 1 
ATOM   2336 N  N   . SER   B 1 92  ? 13.730  7.989   40.984  1.00 44.90 ? 185 SER   B N   1 
ATOM   2337 C  CA  . SER   B 1 92  ? 14.557  7.725   42.194  1.00 43.15 ? 185 SER   B CA  1 
ATOM   2338 C  C   . SER   B 1 92  ? 14.473  8.914   43.155  1.00 42.58 ? 185 SER   B C   1 
ATOM   2339 O  O   . SER   B 1 92  ? 14.659  10.065  42.715  1.00 43.15 ? 185 SER   B O   1 
ATOM   2340 C  CB  . SER   B 1 92  ? 15.991  7.408   41.822  1.00 43.51 ? 185 SER   B CB  1 
ATOM   2341 O  OG  . SER   B 1 92  ? 16.919  8.003   42.727  1.00 42.80 ? 185 SER   B OG  1 
ATOM   2342 N  N   . ASP   B 1 93  ? 14.233  8.625   44.430  1.00 40.74 ? 186 ASP   B N   1 
ATOM   2343 C  CA  . ASP   B 1 93  ? 14.087  9.649   45.498  1.00 40.99 ? 186 ASP   B CA  1 
ATOM   2344 C  C   . ASP   B 1 93  ? 15.409  9.793   46.259  1.00 40.91 ? 186 ASP   B C   1 
ATOM   2345 O  O   . ASP   B 1 93  ? 15.408  10.516  47.274  1.00 42.14 ? 186 ASP   B O   1 
ATOM   2346 C  CB  . ASP   B 1 93  ? 12.923  9.306   46.430  1.00 39.70 ? 186 ASP   B CB  1 
ATOM   2347 C  CG  . ASP   B 1 93  ? 13.139  8.049   47.261  1.00 39.01 ? 186 ASP   B CG  1 
ATOM   2348 O  OD1 . ASP   B 1 93  ? 14.125  7.290   46.983  1.00 38.82 ? 186 ASP   B OD1 1 
ATOM   2349 O  OD2 . ASP   B 1 93  ? 12.346  7.843   48.191  1.00 38.37 ? 186 ASP   B OD2 1 
ATOM   2350 N  N   . GLY   B 1 94  ? 16.480  9.117   45.817  1.00 40.54 ? 187 GLY   B N   1 
ATOM   2351 C  CA  . GLY   B 1 94  ? 17.817  9.145   46.448  1.00 40.40 ? 187 GLY   B CA  1 
ATOM   2352 C  C   . GLY   B 1 94  ? 17.951  8.207   47.645  1.00 38.42 ? 187 GLY   B C   1 
ATOM   2353 O  O   . GLY   B 1 94  ? 19.061  8.084   48.165  1.00 38.36 ? 187 GLY   B O   1 
ATOM   2354 N  N   . LEU   B 1 95  ? 16.865  7.576   48.098  1.00 36.70 ? 188 LEU   B N   1 
ATOM   2355 C  CA  . LEU   B 1 95  ? 16.874  6.751   49.335  1.00 35.23 ? 188 LEU   B CA  1 
ATOM   2356 C  C   . LEU   B 1 95  ? 16.652  5.275   48.989  1.00 34.75 ? 188 LEU   B C   1 
ATOM   2357 O  O   . LEU   B 1 95  ? 17.343  4.434   49.579  1.00 35.70 ? 188 LEU   B O   1 
ATOM   2358 C  CB  . LEU   B 1 95  ? 15.807  7.281   50.293  1.00 33.97 ? 188 LEU   B CB  1 
ATOM   2359 C  CG  . LEU   B 1 95  ? 15.967  8.739   50.726  1.00 34.57 ? 188 LEU   B CG  1 
ATOM   2360 C  CD1 . LEU   B 1 95  ? 14.763  9.183   51.541  1.00 34.22 ? 188 LEU   B CD1 1 
ATOM   2361 C  CD2 . LEU   B 1 95  ? 17.245  8.962   51.518  1.00 35.14 ? 188 LEU   B CD2 1 
ATOM   2362 N  N   . ALA   B 1 96  ? 15.730  4.960   48.074  1.00 34.04 ? 189 ALA   B N   1 
ATOM   2363 C  CA  . ALA   B 1 96  ? 15.303  3.573   47.770  1.00 33.08 ? 189 ALA   B CA  1 
ATOM   2364 C  C   . ALA   B 1 96  ? 16.281  2.913   46.802  1.00 33.81 ? 189 ALA   B C   1 
ATOM   2365 O  O   . ALA   B 1 96  ? 16.733  3.531   45.842  1.00 34.27 ? 189 ALA   B O   1 
ATOM   2366 C  CB  . ALA   B 1 96  ? 13.911  3.587   47.215  1.00 33.56 ? 189 ALA   B CB  1 
ATOM   2367 N  N   . PRO   B 1 97  ? 16.661  1.633   47.020  1.00 33.10 ? 190 PRO   B N   1 
ATOM   2368 C  CA  . PRO   B 1 97  ? 17.439  0.901   46.025  1.00 33.72 ? 190 PRO   B CA  1 
ATOM   2369 C  C   . PRO   B 1 97  ? 16.624  0.851   44.741  1.00 34.40 ? 190 PRO   B C   1 
ATOM   2370 O  O   . PRO   B 1 97  ? 15.397  0.739   44.790  1.00 33.29 ? 190 PRO   B O   1 
ATOM   2371 C  CB  . PRO   B 1 97  ? 17.640  -0.499  46.624  1.00 32.98 ? 190 PRO   B CB  1 
ATOM   2372 C  CG  . PRO   B 1 97  ? 17.399  -0.290  48.109  1.00 32.43 ? 190 PRO   B CG  1 
ATOM   2373 C  CD  . PRO   B 1 97  ? 16.373  0.818   48.208  1.00 31.65 ? 190 PRO   B CD  1 
ATOM   2374 N  N   . PRO   B 1 98  ? 17.278  0.923   43.561  1.00 36.32 ? 191 PRO   B N   1 
ATOM   2375 C  CA  . PRO   B 1 98  ? 16.562  0.913   42.285  1.00 37.48 ? 191 PRO   B CA  1 
ATOM   2376 C  C   . PRO   B 1 98  ? 15.764  -0.378  42.034  1.00 37.82 ? 191 PRO   B C   1 
ATOM   2377 O  O   . PRO   B 1 98  ? 14.832  -0.310  41.276  1.00 37.93 ? 191 PRO   B O   1 
ATOM   2378 C  CB  . PRO   B 1 98  ? 17.658  1.115   41.223  1.00 38.88 ? 191 PRO   B CB  1 
ATOM   2379 C  CG  . PRO   B 1 98  ? 18.955  0.769   41.919  1.00 39.14 ? 191 PRO   B CG  1 
ATOM   2380 C  CD  . PRO   B 1 98  ? 18.738  1.021   43.398  1.00 37.54 ? 191 PRO   B CD  1 
ATOM   2381 N  N   . GLN   B 1 99  ? 16.123  -1.486  42.692  1.00 37.96 ? 192 GLN   B N   1 
ATOM   2382 C  CA  . GLN   B 1 99  ? 15.507  -2.833  42.516  1.00 38.10 ? 192 GLN   B CA  1 
ATOM   2383 C  C   . GLN   B 1 99  ? 14.185  -2.972  43.300  1.00 36.28 ? 192 GLN   B C   1 
ATOM   2384 O  O   . GLN   B 1 99  ? 13.382  -3.850  42.943  1.00 36.02 ? 192 GLN   B O   1 
ATOM   2385 C  CB  . GLN   B 1 99  ? 16.474  -3.910  43.017  1.00 38.78 ? 192 GLN   B CB  1 
ATOM   2386 C  CG  . GLN   B 1 99  ? 17.764  -4.019  42.229  1.00 41.19 ? 192 GLN   B CG  1 
ATOM   2387 C  CD  . GLN   B 1 99  ? 18.475  -5.308  42.547  1.00 42.19 ? 192 GLN   B CD  1 
ATOM   2388 O  OE1 . GLN   B 1 99  ? 18.445  -5.783  43.683  1.00 42.27 ? 192 GLN   B OE1 1 
ATOM   2389 N  NE2 . GLN   B 1 99  ? 19.120  -5.887  41.548  1.00 44.02 ? 192 GLN   B NE2 1 
ATOM   2390 N  N   . HIS   B 1 100 ? 13.977  -2.157  44.338  1.00 34.61 ? 193 HIS   B N   1 
ATOM   2391 C  CA  . HIS   B 1 100 ? 12.885  -2.317  45.334  1.00 33.05 ? 193 HIS   B CA  1 
ATOM   2392 C  C   . HIS   B 1 100 ? 11.542  -1.902  44.728  1.00 32.60 ? 193 HIS   B C   1 
ATOM   2393 O  O   . HIS   B 1 100 ? 11.420  -0.740  44.243  1.00 32.13 ? 193 HIS   B O   1 
ATOM   2394 C  CB  . HIS   B 1 100 ? 13.187  -1.528  46.621  1.00 32.38 ? 193 HIS   B CB  1 
ATOM   2395 C  CG  . HIS   B 1 100 ? 14.096  -2.264  47.546  1.00 32.11 ? 193 HIS   B CG  1 
ATOM   2396 N  ND1 . HIS   B 1 100 ? 13.846  -2.390  48.891  1.00 31.17 ? 193 HIS   B ND1 1 
ATOM   2397 C  CD2 . HIS   B 1 100 ? 15.250  -2.928  47.312  1.00 33.15 ? 193 HIS   B CD2 1 
ATOM   2398 C  CE1 . HIS   B 1 100 ? 14.794  -3.106  49.449  1.00 31.37 ? 193 HIS   B CE1 1 
ATOM   2399 N  NE2 . HIS   B 1 100 ? 15.672  -3.450  48.499  1.00 32.60 ? 193 HIS   B NE2 1 
ATOM   2400 N  N   . LEU   B 1 101 ? 10.556  -2.796  44.782  1.00 31.47 ? 194 LEU   B N   1 
ATOM   2401 C  CA  . LEU   B 1 101 ? 9.187   -2.501  44.287  1.00 30.96 ? 194 LEU   B CA  1 
ATOM   2402 C  C   . LEU   B 1 101 ? 8.525   -1.466  45.190  1.00 29.92 ? 194 LEU   B C   1 
ATOM   2403 O  O   . LEU   B 1 101 ? 7.867   -0.579  44.621  1.00 28.91 ? 194 LEU   B O   1 
ATOM   2404 C  CB  . LEU   B 1 101 ? 8.337   -3.770  44.222  1.00 31.14 ? 194 LEU   B CB  1 
ATOM   2405 C  CG  . LEU   B 1 101 ? 6.856   -3.520  43.946  1.00 30.96 ? 194 LEU   B CG  1 
ATOM   2406 C  CD1 . LEU   B 1 101 ? 6.644   -2.991  42.532  1.00 31.88 ? 194 LEU   B CD1 1 
ATOM   2407 C  CD2 . LEU   B 1 101 ? 6.041   -4.787  44.230  1.00 31.33 ? 194 LEU   B CD2 1 
ATOM   2408 N  N   . ILE   B 1 102 ? 8.672   -1.592  46.520  1.00 29.35 ? 195 ILE   B N   1 
ATOM   2409 C  CA  . ILE   B 1 102 ? 7.872   -0.814  47.515  1.00 28.90 ? 195 ILE   B CA  1 
ATOM   2410 C  C   . ILE   B 1 102 ? 8.749   0.276   48.115  1.00 28.65 ? 195 ILE   B C   1 
ATOM   2411 O  O   . ILE   B 1 102 ? 9.790   -0.048  48.706  1.00 28.64 ? 195 ILE   B O   1 
ATOM   2412 C  CB  . ILE   B 1 102 ? 7.258   -1.693  48.620  1.00 28.82 ? 195 ILE   B CB  1 
ATOM   2413 C  CG1 . ILE   B 1 102 ? 6.534   -2.912  48.046  1.00 29.63 ? 195 ILE   B CG1 1 
ATOM   2414 C  CG2 . ILE   B 1 102 ? 6.328   -0.870  49.506  1.00 28.17 ? 195 ILE   B CG2 1 
ATOM   2415 C  CD1 . ILE   B 1 102 ? 5.694   -3.665  49.072  1.00 29.56 ? 195 ILE   B CD1 1 
ATOM   2416 N  N   . ARG   B 1 103 ? 8.320   1.529   47.962  1.00 29.31 ? 196 ARG   B N   1 
ATOM   2417 C  CA  . ARG   B 1 103 ? 8.987   2.690   48.592  1.00 29.57 ? 196 ARG   B CA  1 
ATOM   2418 C  C   . ARG   B 1 103 ? 8.034   3.303   49.615  1.00 27.92 ? 196 ARG   B C   1 
ATOM   2419 O  O   . ARG   B 1 103 ? 6.814   3.093   49.497  1.00 26.95 ? 196 ARG   B O   1 
ATOM   2420 C  CB  . ARG   B 1 103 ? 9.373   3.741   47.552  1.00 31.73 ? 196 ARG   B CB  1 
ATOM   2421 C  CG  . ARG   B 1 103 ? 10.269  3.190   46.467  1.00 33.55 ? 196 ARG   B CG  1 
ATOM   2422 C  CD  . ARG   B 1 103 ? 11.220  4.122   45.787  1.00 35.97 ? 196 ARG   B CD  1 
ATOM   2423 N  NE  . ARG   B 1 103 ? 10.773  5.431   45.350  1.00 38.33 ? 196 ARG   B NE  1 
ATOM   2424 C  CZ  . ARG   B 1 103 ? 11.183  5.992   44.211  1.00 40.49 ? 196 ARG   B CZ  1 
ATOM   2425 N  NH1 . ARG   B 1 103 ? 10.740  7.181   43.847  1.00 40.81 ? 196 ARG   B NH1 1 
ATOM   2426 N  NH2 . ARG   B 1 103 ? 11.977  5.321   43.392  1.00 41.87 ? 196 ARG   B NH2 1 
ATOM   2427 N  N   . VAL   B 1 104 ? 8.591   4.038   50.577  1.00 27.55 ? 197 VAL   B N   1 
ATOM   2428 C  CA  . VAL   B 1 104 ? 7.813   4.977   51.420  1.00 27.50 ? 197 VAL   B CA  1 
ATOM   2429 C  C   . VAL   B 1 104 ? 8.176   6.397   50.968  1.00 28.96 ? 197 VAL   B C   1 
ATOM   2430 O  O   . VAL   B 1 104 ? 9.380   6.669   50.746  1.00 28.33 ? 197 VAL   B O   1 
ATOM   2431 C  CB  . VAL   B 1 104 ? 8.057   4.732   52.920  1.00 27.06 ? 197 VAL   B CB  1 
ATOM   2432 C  CG1 . VAL   B 1 104 ? 7.438   5.820   53.777  1.00 27.31 ? 197 VAL   B CG1 1 
ATOM   2433 C  CG2 . VAL   B 1 104 ? 7.537   3.367   53.348  1.00 26.15 ? 197 VAL   B CG2 1 
ATOM   2434 N  N   . GLU   B 1 105 ? 7.165   7.240   50.776  1.00 30.59 ? 198 GLU   B N   1 
ATOM   2435 C  CA  . GLU   B 1 105 ? 7.351   8.663   50.398  1.00 32.45 ? 198 GLU   B CA  1 
ATOM   2436 C  C   . GLU   B 1 105 ? 7.112   9.521   51.649  1.00 32.39 ? 198 GLU   B C   1 
ATOM   2437 O  O   . GLU   B 1 105 ? 6.331   9.093   52.531  1.00 30.98 ? 198 GLU   B O   1 
ATOM   2438 C  CB  . GLU   B 1 105 ? 6.448   8.985   49.195  1.00 33.96 ? 198 GLU   B CB  1 
ATOM   2439 C  CG  . GLU   B 1 105 ? 5.264   9.881   49.495  1.00 34.63 ? 198 GLU   B CG  1 
ATOM   2440 C  CD  . GLU   B 1 105 ? 4.304   10.066  48.328  1.00 35.92 ? 198 GLU   B CD  1 
ATOM   2441 O  OE1 . GLU   B 1 105 ? 4.119   11.233  47.900  1.00 38.14 ? 198 GLU   B OE1 1 
ATOM   2442 O  OE2 . GLU   B 1 105 ? 3.738   9.046   47.837  1.00 35.32 ? 198 GLU   B OE2 1 
ATOM   2443 N  N   . GLY   B 1 106 ? 7.758   10.686  51.707  1.00 33.99 ? 199 GLY   B N   1 
ATOM   2444 C  CA  . GLY   B 1 106 ? 7.570   11.701  52.759  1.00 34.48 ? 199 GLY   B CA  1 
ATOM   2445 C  C   . GLY   B 1 106 ? 8.089   11.269  54.122  1.00 34.56 ? 199 GLY   B C   1 
ATOM   2446 O  O   . GLY   B 1 106 ? 7.564   11.786  55.139  1.00 35.25 ? 199 GLY   B O   1 
ATOM   2447 N  N   . ASN   B 1 107 ? 9.069   10.356  54.186  1.00 33.65 ? 200 ASN   B N   1 
ATOM   2448 C  CA  . ASN   B 1 107 ? 9.671   9.937   55.481  1.00 32.37 ? 200 ASN   B CA  1 
ATOM   2449 C  C   . ASN   B 1 107 ? 11.192  9.822   55.337  1.00 32.80 ? 200 ASN   B C   1 
ATOM   2450 O  O   . ASN   B 1 107 ? 11.700  8.834   54.759  1.00 31.07 ? 200 ASN   B O   1 
ATOM   2451 C  CB  . ASN   B 1 107 ? 9.009   8.669   56.024  1.00 32.11 ? 200 ASN   B CB  1 
ATOM   2452 C  CG  . ASN   B 1 107 ? 9.289   8.468   57.494  1.00 31.38 ? 200 ASN   B CG  1 
ATOM   2453 O  OD1 . ASN   B 1 107 ? 10.364  8.844   57.977  1.00 31.81 ? 200 ASN   B OD1 1 
ATOM   2454 N  ND2 . ASN   B 1 107 ? 8.322   7.906   58.202  1.00 31.03 ? 200 ASN   B ND2 1 
ATOM   2455 N  N   . LEU   B 1 108 ? 11.920  10.797  55.878  1.00 33.68 ? 201 LEU   B N   1 
ATOM   2456 C  CA  . LEU   B 1 108 ? 13.397  10.850  55.737  1.00 34.38 ? 201 LEU   B CA  1 
ATOM   2457 C  C   . LEU   B 1 108 ? 14.063  9.802   56.637  1.00 33.23 ? 201 LEU   B C   1 
ATOM   2458 O  O   . LEU   B 1 108 ? 15.269  9.636   56.475  1.00 34.12 ? 201 LEU   B O   1 
ATOM   2459 C  CB  . LEU   B 1 108 ? 13.907  12.261  56.038  1.00 36.39 ? 201 LEU   B CB  1 
ATOM   2460 C  CG  . LEU   B 1 108 ? 14.003  13.196  54.834  1.00 38.04 ? 201 LEU   B CG  1 
ATOM   2461 C  CD1 . LEU   B 1 108 ? 12.627  13.454  54.215  1.00 38.51 ? 201 LEU   B CD1 1 
ATOM   2462 C  CD2 . LEU   B 1 108 ? 14.655  14.509  55.234  1.00 39.76 ? 201 LEU   B CD2 1 
ATOM   2463 N  N   . ARG   B 1 109 ? 13.318  9.125   57.522  1.00 33.00 ? 202 ARG   B N   1 
ATOM   2464 C  CA  A ARG   B 1 109 ? 13.872  8.111   58.460  0.50 33.19 ? 202 ARG   B CA  1 
ATOM   2465 C  CA  B ARG   B 1 109 ? 13.875  8.109   58.457  0.50 32.30 ? 202 ARG   B CA  1 
ATOM   2466 C  C   . ARG   B 1 109 ? 13.647  6.699   57.907  1.00 31.54 ? 202 ARG   B C   1 
ATOM   2467 O  O   . ARG   B 1 109 ? 14.019  5.744   58.604  1.00 32.36 ? 202 ARG   B O   1 
ATOM   2468 C  CB  A ARG   B 1 109 ? 13.237  8.250   59.844  0.50 34.38 ? 202 ARG   B CB  1 
ATOM   2469 C  CB  B ARG   B 1 109 ? 13.247  8.250   59.845  0.50 32.24 ? 202 ARG   B CB  1 
ATOM   2470 C  CG  A ARG   B 1 109 ? 13.500  9.585   60.526  0.50 36.47 ? 202 ARG   B CG  1 
ATOM   2471 C  CG  B ARG   B 1 109 ? 13.535  9.585   60.512  0.50 33.06 ? 202 ARG   B CG  1 
ATOM   2472 C  CD  A ARG   B 1 109 ? 12.731  9.693   61.828  0.50 37.63 ? 202 ARG   B CD  1 
ATOM   2473 C  CD  B ARG   B 1 109 ? 12.974  9.595   61.908  0.50 33.02 ? 202 ARG   B CD  1 
ATOM   2474 N  NE  A ARG   B 1 109 ? 13.161  8.686   62.794  0.50 38.38 ? 202 ARG   B NE  1 
ATOM   2475 N  NE  B ARG   B 1 109 ? 11.540  9.386   61.904  0.50 31.74 ? 202 ARG   B NE  1 
ATOM   2476 C  CZ  A ARG   B 1 109 ? 12.561  8.443   63.953  0.50 38.90 ? 202 ARG   B CZ  1 
ATOM   2477 C  CZ  B ARG   B 1 109 ? 10.829  9.208   63.005  0.50 31.67 ? 202 ARG   B CZ  1 
ATOM   2478 N  NH1 A ARG   B 1 109 ? 11.495  9.139   64.300  0.50 39.24 ? 202 ARG   B NH1 1 
ATOM   2479 N  NH1 B ARG   B 1 109 ? 11.439  9.202   64.178  0.50 32.53 ? 202 ARG   B NH1 1 
ATOM   2480 N  NH2 A ARG   B 1 109 ? 13.019  7.500   64.757  0.50 39.07 ? 202 ARG   B NH2 1 
ATOM   2481 N  NH2 B ARG   B 1 109 ? 9.526   9.025   62.931  0.50 30.93 ? 202 ARG   B NH2 1 
ATOM   2482 N  N   . VAL   B 1 110 ? 13.092  6.588   56.698  1.00 30.06 ? 203 VAL   B N   1 
ATOM   2483 C  CA  . VAL   B 1 110 ? 12.900  5.304   55.967  1.00 28.52 ? 203 VAL   B CA  1 
ATOM   2484 C  C   . VAL   B 1 110 ? 14.239  4.558   55.838  1.00 28.24 ? 203 VAL   B C   1 
ATOM   2485 O  O   . VAL   B 1 110 ? 15.276  5.193   55.624  1.00 28.26 ? 203 VAL   B O   1 
ATOM   2486 C  CB  . VAL   B 1 110 ? 12.231  5.527   54.595  1.00 28.46 ? 203 VAL   B CB  1 
ATOM   2487 C  CG1 . VAL   B 1 110 ? 13.072  6.343   53.638  1.00 29.30 ? 203 VAL   B CG1 1 
ATOM   2488 C  CG2 . VAL   B 1 110 ? 11.868  4.213   53.934  1.00 28.36 ? 203 VAL   B CG2 1 
ATOM   2489 N  N   . GLU   B 1 111 ? 14.195  3.228   55.932  1.00 27.68 ? 204 GLU   B N   1 
ATOM   2490 C  CA  . GLU   B 1 111 ? 15.375  2.338   55.829  1.00 28.46 ? 204 GLU   B CA  1 
ATOM   2491 C  C   . GLU   B 1 111 ? 15.004  1.168   54.905  1.00 28.17 ? 204 GLU   B C   1 
ATOM   2492 O  O   . GLU   B 1 111 ? 13.850  0.703   54.977  1.00 27.66 ? 204 GLU   B O   1 
ATOM   2493 C  CB  . GLU   B 1 111 ? 15.774  1.933   57.253  1.00 29.70 ? 204 GLU   B CB  1 
ATOM   2494 C  CG  . GLU   B 1 111 ? 16.630  0.679   57.362  1.00 31.08 ? 204 GLU   B CG  1 
ATOM   2495 C  CD  . GLU   B 1 111 ? 16.826  0.214   58.803  1.00 31.41 ? 204 GLU   B CD  1 
ATOM   2496 O  OE1 . GLU   B 1 111 ? 17.001  1.086   59.700  1.00 31.12 ? 204 GLU   B OE1 1 
ATOM   2497 O  OE2 . GLU   B 1 111 ? 16.821  -1.029  59.035  1.00 31.28 ? 204 GLU   B OE2 1 
ATOM   2498 N  N   . TYR   B 1 112 ? 15.914  0.747   54.028  1.00 28.27 ? 205 TYR   B N   1 
ATOM   2499 C  CA  . TYR   B 1 112 ? 15.679  -0.336  53.034  1.00 28.58 ? 205 TYR   B CA  1 
ATOM   2500 C  C   . TYR   B 1 112 ? 16.610  -1.508  53.342  1.00 29.28 ? 205 TYR   B C   1 
ATOM   2501 O  O   . TYR   B 1 112 ? 17.775  -1.293  53.724  1.00 31.01 ? 205 TYR   B O   1 
ATOM   2502 C  CB  . TYR   B 1 112 ? 15.829  0.209   51.606  1.00 28.67 ? 205 TYR   B CB  1 
ATOM   2503 C  CG  . TYR   B 1 112 ? 14.749  1.177   51.190  1.00 28.31 ? 205 TYR   B CG  1 
ATOM   2504 C  CD1 . TYR   B 1 112 ? 14.859  2.538   51.455  1.00 28.63 ? 205 TYR   B CD1 1 
ATOM   2505 C  CD2 . TYR   B 1 112 ? 13.608  0.738   50.548  1.00 27.61 ? 205 TYR   B CD2 1 
ATOM   2506 C  CE1 . TYR   B 1 112 ? 13.862  3.429   51.083  1.00 28.17 ? 205 TYR   B CE1 1 
ATOM   2507 C  CE2 . TYR   B 1 112 ? 12.611  1.612   50.158  1.00 27.65 ? 205 TYR   B CE2 1 
ATOM   2508 C  CZ  . TYR   B 1 112 ? 12.733  2.962   50.436  1.00 27.75 ? 205 TYR   B CZ  1 
ATOM   2509 O  OH  . TYR   B 1 112 ? 11.747  3.805   50.053  1.00 27.08 ? 205 TYR   B OH  1 
ATOM   2510 N  N   . LEU   B 1 113 ? 16.107  -2.736  53.190  1.00 29.51 ? 206 LEU   B N   1 
ATOM   2511 C  CA  . LEU   B 1 113 ? 16.875  -3.962  53.494  1.00 29.91 ? 206 LEU   B CA  1 
ATOM   2512 C  C   . LEU   B 1 113 ? 16.862  -4.890  52.276  1.00 31.05 ? 206 LEU   B C   1 
ATOM   2513 O  O   . LEU   B 1 113 ? 15.775  -5.134  51.718  1.00 30.61 ? 206 LEU   B O   1 
ATOM   2514 C  CB  . LEU   B 1 113 ? 16.263  -4.630  54.734  1.00 29.95 ? 206 LEU   B CB  1 
ATOM   2515 C  CG  . LEU   B 1 113 ? 16.826  -6.008  55.085  1.00 30.74 ? 206 LEU   B CG  1 
ATOM   2516 C  CD1 . LEU   B 1 113 ? 18.310  -5.915  55.401  1.00 31.61 ? 206 LEU   B CD1 1 
ATOM   2517 C  CD2 . LEU   B 1 113 ? 16.072  -6.615  56.259  1.00 30.61 ? 206 LEU   B CD2 1 
ATOM   2518 N  N   . ASP   B 1 114 ? 18.048  -5.306  51.842  1.00 32.89 ? 207 ASP   B N   1 
ATOM   2519 C  CA  . ASP   B 1 114 ? 18.271  -6.546  51.050  1.00 35.39 ? 207 ASP   B CA  1 
ATOM   2520 C  C   . ASP   B 1 114 ? 18.698  -7.604  52.065  1.00 37.23 ? 207 ASP   B C   1 
ATOM   2521 O  O   . ASP   B 1 114 ? 19.806  -7.462  52.614  1.00 38.33 ? 207 ASP   B O   1 
ATOM   2522 C  CB  . ASP   B 1 114 ? 19.331  -6.383  49.957  1.00 36.31 ? 207 ASP   B CB  1 
ATOM   2523 C  CG  . ASP   B 1 114 ? 19.021  -5.335  48.904  1.00 35.91 ? 207 ASP   B CG  1 
ATOM   2524 O  OD1 . ASP   B 1 114 ? 17.867  -4.911  48.822  1.00 35.44 ? 207 ASP   B OD1 1 
ATOM   2525 O  OD2 . ASP   B 1 114 ? 19.959  -4.924  48.207  1.00 37.66 ? 207 ASP   B OD2 1 
ATOM   2526 N  N   . ASP   B 1 115 ? 17.809  -8.542  52.391  1.00 38.92 ? 208 ASP   B N   1 
ATOM   2527 C  CA  . ASP   B 1 115 ? 18.032  -9.567  53.444  1.00 40.64 ? 208 ASP   B CA  1 
ATOM   2528 C  C   . ASP   B 1 115 ? 19.229  -10.410 53.007  1.00 42.46 ? 208 ASP   B C   1 
ATOM   2529 O  O   . ASP   B 1 115 ? 19.221  -10.914 51.865  1.00 43.11 ? 208 ASP   B O   1 
ATOM   2530 C  CB  . ASP   B 1 115 ? 16.771  -10.400 53.693  1.00 41.12 ? 208 ASP   B CB  1 
ATOM   2531 C  CG  . ASP   B 1 115 ? 16.896  -11.377 54.852  1.00 42.39 ? 208 ASP   B CG  1 
ATOM   2532 O  OD1 . ASP   B 1 115 ? 17.699  -12.323 54.744  1.00 43.87 ? 208 ASP   B OD1 1 
ATOM   2533 O  OD2 . ASP   B 1 115 ? 16.183  -11.181 55.858  1.00 42.62 ? 208 ASP   B OD2 1 
ATOM   2534 N  N   . ARG   B 1 116 ? 20.230  -10.517 53.881  1.00 43.96 ? 209 ARG   B N   1 
ATOM   2535 C  CA  . ARG   B 1 116 ? 21.508  -11.230 53.618  1.00 46.36 ? 209 ARG   B CA  1 
ATOM   2536 C  C   . ARG   B 1 116 ? 21.256  -12.689 53.202  1.00 47.39 ? 209 ARG   B C   1 
ATOM   2537 O  O   . ARG   B 1 116 ? 22.067  -13.182 52.406  1.00 48.32 ? 209 ARG   B O   1 
ATOM   2538 C  CB  . ARG   B 1 116 ? 22.437  -11.158 54.834  1.00 47.76 ? 209 ARG   B CB  1 
ATOM   2539 C  CG  . ARG   B 1 116 ? 21.784  -11.481 56.173  1.00 48.93 ? 209 ARG   B CG  1 
ATOM   2540 C  CD  . ARG   B 1 116 ? 22.615  -11.062 57.374  1.00 49.69 ? 209 ARG   B CD  1 
ATOM   2541 N  NE  . ARG   B 1 116 ? 23.965  -11.608 57.359  1.00 51.89 ? 209 ARG   B NE  1 
ATOM   2542 C  CZ  . ARG   B 1 116 ? 25.022  -11.042 57.940  1.00 52.99 ? 209 ARG   B CZ  1 
ATOM   2543 N  NH1 . ARG   B 1 116 ? 24.895  -9.896  58.591  1.00 52.57 ? 209 ARG   B NH1 1 
ATOM   2544 N  NH2 . ARG   B 1 116 ? 26.206  -11.626 57.863  1.00 54.66 ? 209 ARG   B NH2 1 
ATOM   2545 N  N   . ASN   B 1 117 ? 20.186  -13.339 53.680  1.00 46.83 ? 210 ASN   B N   1 
ATOM   2546 C  CA  . ASN   B 1 117 ? 20.000  -14.808 53.512  1.00 48.17 ? 210 ASN   B CA  1 
ATOM   2547 C  C   . ASN   B 1 117 ? 18.829  -15.127 52.569  1.00 47.57 ? 210 ASN   B C   1 
ATOM   2548 O  O   . ASN   B 1 117 ? 18.972  -16.093 51.796  1.00 48.40 ? 210 ASN   B O   1 
ATOM   2549 C  CB  . ASN   B 1 117 ? 19.796  -15.526 54.846  1.00 49.08 ? 210 ASN   B CB  1 
ATOM   2550 C  CG  . ASN   B 1 117 ? 20.707  -15.066 55.961  1.00 49.49 ? 210 ASN   B CG  1 
ATOM   2551 O  OD1 . ASN   B 1 117 ? 20.291  -15.043 57.114  1.00 49.47 ? 210 ASN   B OD1 1 
ATOM   2552 N  ND2 . ASN   B 1 117 ? 21.952  -14.743 55.661  1.00 50.59 ? 210 ASN   B ND2 1 
ATOM   2553 N  N   . THR   B 1 118 ? 17.706  -14.398 52.640  1.00 45.37 ? 211 THR   B N   1 
ATOM   2554 C  CA  . THR   B 1 118 ? 16.514  -14.660 51.787  1.00 44.96 ? 211 THR   B CA  1 
ATOM   2555 C  C   . THR   B 1 118 ? 16.607  -13.854 50.488  1.00 43.92 ? 211 THR   B C   1 
ATOM   2556 O  O   . THR   B 1 118 ? 15.873  -14.188 49.551  1.00 44.62 ? 211 THR   B O   1 
ATOM   2557 C  CB  . THR   B 1 118 ? 15.197  -14.330 52.502  1.00 44.01 ? 211 THR   B CB  1 
ATOM   2558 O  OG1 . THR   B 1 118 ? 15.163  -12.925 52.766  1.00 42.56 ? 211 THR   B OG1 1 
ATOM   2559 C  CG2 . THR   B 1 118 ? 15.015  -15.101 53.789  1.00 44.82 ? 211 THR   B CG2 1 
ATOM   2560 N  N   . PHE   B 1 119 ? 17.409  -12.783 50.472  1.00 42.56 ? 212 PHE   B N   1 
ATOM   2561 C  CA  . PHE   B 1 119 ? 17.572  -11.847 49.327  1.00 41.13 ? 212 PHE   B CA  1 
ATOM   2562 C  C   . PHE   B 1 119 ? 16.267  -11.081 49.085  1.00 38.19 ? 212 PHE   B C   1 
ATOM   2563 O  O   . PHE   B 1 119 ? 16.169  -10.369 48.063  1.00 37.33 ? 212 PHE   B O   1 
ATOM   2564 C  CB  . PHE   B 1 119 ? 18.015  -12.593 48.067  1.00 43.17 ? 212 PHE   B CB  1 
ATOM   2565 C  CG  . PHE   B 1 119 ? 19.225  -13.475 48.243  1.00 45.75 ? 212 PHE   B CG  1 
ATOM   2566 C  CD1 . PHE   B 1 119 ? 20.480  -12.924 48.454  1.00 46.48 ? 212 PHE   B CD1 1 
ATOM   2567 C  CD2 . PHE   B 1 119 ? 19.112  -14.856 48.196  1.00 47.68 ? 212 PHE   B CD2 1 
ATOM   2568 C  CE1 . PHE   B 1 119 ? 21.595  -13.732 48.617  1.00 48.14 ? 212 PHE   B CE1 1 
ATOM   2569 C  CE2 . PHE   B 1 119 ? 20.227  -15.663 48.353  1.00 49.75 ? 212 PHE   B CE2 1 
ATOM   2570 C  CZ  . PHE   B 1 119 ? 21.467  -15.101 48.561  1.00 49.94 ? 212 PHE   B CZ  1 
ATOM   2571 N  N   . ARG   B 1 120 ? 15.293  -11.208 49.988  1.00 36.41 ? 213 ARG   B N   1 
ATOM   2572 C  CA  . ARG   B 1 120 ? 13.994  -10.498 49.879  1.00 34.13 ? 213 ARG   B CA  1 
ATOM   2573 C  C   . ARG   B 1 120 ? 14.217  -9.029  50.237  1.00 32.09 ? 213 ARG   B C   1 
ATOM   2574 O  O   . ARG   B 1 120 ? 15.118  -8.730  51.079  1.00 31.71 ? 213 ARG   B O   1 
ATOM   2575 C  CB  . ARG   B 1 120 ? 12.938  -11.172 50.758  1.00 34.49 ? 213 ARG   B CB  1 
ATOM   2576 C  CG  . ARG   B 1 120 ? 12.587  -12.576 50.279  1.00 36.03 ? 213 ARG   B CG  1 
ATOM   2577 C  CD  . ARG   B 1 120 ? 11.298  -13.117 50.899  1.00 36.25 ? 213 ARG   B CD  1 
ATOM   2578 N  NE  . ARG   B 1 120 ? 10.994  -14.436 50.344  1.00 38.02 ? 213 ARG   B NE  1 
ATOM   2579 C  CZ  . ARG   B 1 120 ? 10.281  -14.672 49.239  1.00 38.32 ? 213 ARG   B CZ  1 
ATOM   2580 N  NH1 . ARG   B 1 120 ? 9.794   -13.676 48.515  1.00 37.11 ? 213 ARG   B NH1 1 
ATOM   2581 N  NH2 . ARG   B 1 120 ? 10.094  -15.921 48.836  1.00 39.49 ? 213 ARG   B NH2 1 
ATOM   2582 N  N   . HIS   B 1 121 ? 13.450  -8.150  49.601  1.00 30.88 ? 214 HIS   B N   1 
ATOM   2583 C  CA  . HIS   B 1 121 ? 13.497  -6.674  49.805  1.00 29.79 ? 214 HIS   B CA  1 
ATOM   2584 C  C   . HIS   B 1 121 ? 12.416  -6.254  50.803  1.00 28.12 ? 214 HIS   B C   1 
ATOM   2585 O  O   . HIS   B 1 121 ? 11.292  -6.800  50.765  1.00 27.92 ? 214 HIS   B O   1 
ATOM   2586 C  CB  . HIS   B 1 121 ? 13.278  -5.963  48.466  1.00 30.03 ? 214 HIS   B CB  1 
ATOM   2587 C  CG  . HIS   B 1 121 ? 14.271  -6.313  47.417  1.00 31.80 ? 214 HIS   B CG  1 
ATOM   2588 N  ND1 . HIS   B 1 121 ? 14.040  -6.064  46.067  1.00 32.51 ? 214 HIS   B ND1 1 
ATOM   2589 C  CD2 . HIS   B 1 121 ? 15.514  -6.841  47.500  1.00 33.03 ? 214 HIS   B CD2 1 
ATOM   2590 C  CE1 . HIS   B 1 121 ? 15.099  -6.413  45.371  1.00 33.63 ? 214 HIS   B CE1 1 
ATOM   2591 N  NE2 . HIS   B 1 121 ? 15.999  -6.918  46.233  1.00 33.96 ? 214 HIS   B NE2 1 
ATOM   2592 N  N   . SER   B 1 122 ? 12.690  -5.242  51.615  1.00 26.97 ? 215 SER   B N   1 
ATOM   2593 C  CA  . SER   B 1 122 ? 11.666  -4.648  52.492  1.00 25.67 ? 215 SER   B CA  1 
ATOM   2594 C  C   . SER   B 1 122 ? 12.057  -3.208  52.831  1.00 25.38 ? 215 SER   B C   1 
ATOM   2595 O  O   . SER   B 1 122 ? 13.244  -2.833  52.652  1.00 25.50 ? 215 SER   B O   1 
ATOM   2596 C  CB  . SER   B 1 122 ? 11.445  -5.480  53.724  1.00 25.09 ? 215 SER   B CB  1 
ATOM   2597 O  OG  . SER   B 1 122 ? 12.625  -5.593  54.481  1.00 24.36 ? 215 SER   B OG  1 
ATOM   2598 N  N   . VAL   B 1 123 ? 11.061  -2.427  53.224  1.00 25.14 ? 216 VAL   B N   1 
ATOM   2599 C  CA  . VAL   B 1 123 ? 11.221  -0.986  53.590  1.00 24.84 ? 216 VAL   B CA  1 
ATOM   2600 C  C   . VAL   B 1 123 ? 10.641  -0.847  54.998  1.00 24.89 ? 216 VAL   B C   1 
ATOM   2601 O  O   . VAL   B 1 123 ? 9.543   -1.401  55.268  1.00 24.54 ? 216 VAL   B O   1 
ATOM   2602 C  CB  . VAL   B 1 123 ? 10.610  -0.042  52.540  1.00 24.81 ? 216 VAL   B CB  1 
ATOM   2603 C  CG1 . VAL   B 1 123 ? 9.163   -0.367  52.195  1.00 24.98 ? 216 VAL   B CG1 1 
ATOM   2604 C  CG2 . VAL   B 1 123 ? 10.753  1.437   52.926  1.00 24.84 ? 216 VAL   B CG2 1 
ATOM   2605 N  N   A VAL   B 1 124 ? 11.371  -0.164  55.884  0.45 24.84 ? 217 VAL   B N   1 
ATOM   2606 N  N   B VAL   B 1 124 ? 11.373  -0.168  55.883  0.55 25.03 ? 217 VAL   B N   1 
ATOM   2607 C  CA  A VAL   B 1 124 ? 11.013  -0.036  57.322  0.45 24.57 ? 217 VAL   B CA  1 
ATOM   2608 C  CA  B VAL   B 1 124 ? 11.011  -0.026  57.318  0.55 24.85 ? 217 VAL   B CA  1 
ATOM   2609 C  C   A VAL   B 1 124 ? 11.011  1.451   57.708  0.45 24.83 ? 217 VAL   B C   1 
ATOM   2610 C  C   B VAL   B 1 124 ? 11.004  1.459   57.696  0.55 24.98 ? 217 VAL   B C   1 
ATOM   2611 O  O   A VAL   B 1 124 ? 11.889  2.177   57.245  0.45 25.41 ? 217 VAL   B O   1 
ATOM   2612 O  O   B VAL   B 1 124 ? 11.890  2.185   57.246  0.55 25.60 ? 217 VAL   B O   1 
ATOM   2613 C  CB  A VAL   B 1 124 ? 11.935  -0.904  58.200  0.45 24.79 ? 217 VAL   B CB  1 
ATOM   2614 C  CB  B VAL   B 1 124 ? 11.947  -0.866  58.203  0.55 25.31 ? 217 VAL   B CB  1 
ATOM   2615 C  CG1 A VAL   B 1 124 ? 13.414  -0.562  58.047  0.45 25.03 ? 217 VAL   B CG1 1 
ATOM   2616 C  CG1 B VAL   B 1 124 ? 12.321  -0.148  59.495  0.55 25.60 ? 217 VAL   B CG1 1 
ATOM   2617 C  CG2 A VAL   B 1 124 ? 11.509  -0.873  59.668  0.45 24.64 ? 217 VAL   B CG2 1 
ATOM   2618 C  CG2 B VAL   B 1 124 ? 11.328  -2.215  58.508  0.55 25.17 ? 217 VAL   B CG2 1 
ATOM   2619 N  N   . VAL   B 1 125 ? 10.003  1.878   58.471  1.00 24.92 ? 218 VAL   B N   1 
ATOM   2620 C  CA  . VAL   B 1 125 ? 9.902   3.254   59.040  1.00 25.53 ? 218 VAL   B CA  1 
ATOM   2621 C  C   . VAL   B 1 125 ? 9.669   3.110   60.535  1.00 25.80 ? 218 VAL   B C   1 
ATOM   2622 O  O   . VAL   B 1 125 ? 9.110   2.108   60.978  1.00 25.73 ? 218 VAL   B O   1 
ATOM   2623 C  CB  . VAL   B 1 125 ? 8.793   4.084   58.353  1.00 25.60 ? 218 VAL   B CB  1 
ATOM   2624 C  CG1 . VAL   B 1 125 ? 9.159   4.450   56.927  1.00 25.60 ? 218 VAL   B CG1 1 
ATOM   2625 C  CG2 . VAL   B 1 125 ? 7.448   3.399   58.351  1.00 25.70 ? 218 VAL   B CG2 1 
ATOM   2626 N  N   . PRO   B 1 126 ? 10.078  4.102   61.356  1.00 26.66 ? 219 PRO   B N   1 
ATOM   2627 C  CA  . PRO   B 1 126 ? 9.668   4.153   62.755  1.00 27.35 ? 219 PRO   B CA  1 
ATOM   2628 C  C   . PRO   B 1 126 ? 8.144   4.254   62.824  1.00 27.04 ? 219 PRO   B C   1 
ATOM   2629 O  O   . PRO   B 1 126 ? 7.533   4.923   61.978  1.00 26.08 ? 219 PRO   B O   1 
ATOM   2630 C  CB  . PRO   B 1 126 ? 10.297  5.432   63.355  1.00 28.27 ? 219 PRO   B CB  1 
ATOM   2631 C  CG  . PRO   B 1 126 ? 11.121  6.040   62.246  1.00 28.30 ? 219 PRO   B CG  1 
ATOM   2632 C  CD  . PRO   B 1 126 ? 10.946  5.222   60.981  1.00 27.15 ? 219 PRO   B CD  1 
ATOM   2633 N  N   . TYR   B 1 127 ? 7.553   3.577   63.807  1.00 27.60 ? 220 TYR   B N   1 
ATOM   2634 C  CA  . TYR   B 1 127 ? 6.138   3.762   64.181  1.00 27.82 ? 220 TYR   B CA  1 
ATOM   2635 C  C   . TYR   B 1 127 ? 6.001   5.137   64.834  1.00 29.47 ? 220 TYR   B C   1 
ATOM   2636 O  O   . TYR   B 1 127 ? 6.796   5.449   65.731  1.00 29.37 ? 220 TYR   B O   1 
ATOM   2637 C  CB  . TYR   B 1 127 ? 5.654   2.660   65.119  1.00 27.60 ? 220 TYR   B CB  1 
ATOM   2638 C  CG  . TYR   B 1 127 ? 4.254   2.916   65.595  1.00 27.67 ? 220 TYR   B CG  1 
ATOM   2639 C  CD1 . TYR   B 1 127 ? 3.166   2.543   64.829  1.00 26.83 ? 220 TYR   B CD1 1 
ATOM   2640 C  CD2 . TYR   B 1 127 ? 4.026   3.628   66.769  1.00 28.00 ? 220 TYR   B CD2 1 
ATOM   2641 C  CE1 . TYR   B 1 127 ? 1.874   2.855   65.222  1.00 27.03 ? 220 TYR   B CE1 1 
ATOM   2642 C  CE2 . TYR   B 1 127 ? 2.744   3.913   67.191  1.00 28.46 ? 220 TYR   B CE2 1 
ATOM   2643 C  CZ  . TYR   B 1 127 ? 1.667   3.526   66.412  1.00 27.78 ? 220 TYR   B CZ  1 
ATOM   2644 O  OH  . TYR   B 1 127 ? 0.411   3.818   66.827  1.00 27.28 ? 220 TYR   B OH  1 
ATOM   2645 N  N   . GLU   B 1 128 ? 5.076   5.951   64.332  1.00 30.98 ? 221 GLU   B N   1 
ATOM   2646 C  CA  . GLU   B 1 128 ? 4.664   7.214   64.968  1.00 33.66 ? 221 GLU   B CA  1 
ATOM   2647 C  C   . GLU   B 1 128 ? 3.203   7.072   65.346  1.00 33.56 ? 221 GLU   B C   1 
ATOM   2648 O  O   . GLU   B 1 128 ? 2.407   6.534   64.575  1.00 33.93 ? 221 GLU   B O   1 
ATOM   2649 C  CB  . GLU   B 1 128 ? 4.929   8.425   64.074  1.00 35.41 ? 221 GLU   B CB  1 
ATOM   2650 C  CG  . GLU   B 1 128 ? 6.404   8.745   63.979  1.00 37.05 ? 221 GLU   B CG  1 
ATOM   2651 C  CD  . GLU   B 1 128 ? 7.134   8.872   65.308  1.00 39.16 ? 221 GLU   B CD  1 
ATOM   2652 O  OE1 . GLU   B 1 128 ? 6.516   9.370   66.285  1.00 42.96 ? 221 GLU   B OE1 1 
ATOM   2653 O  OE2 . GLU   B 1 128 ? 8.320   8.476   65.371  1.00 40.43 ? 221 GLU   B OE2 1 
ATOM   2654 N  N   . PRO   B 1 129 ? 2.824   7.538   66.549  1.00 33.92 ? 222 PRO   B N   1 
ATOM   2655 C  CA  . PRO   B 1 129 ? 1.434   7.472   66.981  1.00 34.74 ? 222 PRO   B CA  1 
ATOM   2656 C  C   . PRO   B 1 129 ? 0.588   8.410   66.134  1.00 34.46 ? 222 PRO   B C   1 
ATOM   2657 O  O   . PRO   B 1 129 ? 1.120   9.289   65.458  1.00 34.14 ? 222 PRO   B O   1 
ATOM   2658 C  CB  . PRO   B 1 129 ? 1.475   7.906   68.456  1.00 35.26 ? 222 PRO   B CB  1 
ATOM   2659 C  CG  . PRO   B 1 129 ? 2.757   8.673   68.607  1.00 35.92 ? 222 PRO   B CG  1 
ATOM   2660 C  CD  . PRO   B 1 129 ? 3.703   8.159   67.550  1.00 35.00 ? 222 PRO   B CD  1 
ATOM   2661 N  N   . PRO   B 1 130 ? -0.754  8.254   66.145  1.00 34.98 ? 223 PRO   B N   1 
ATOM   2662 C  CA  . PRO   B 1 130 ? -1.626  9.137   65.376  1.00 35.88 ? 223 PRO   B CA  1 
ATOM   2663 C  C   . PRO   B 1 130 ? -1.372  10.604  65.748  1.00 37.77 ? 223 PRO   B C   1 
ATOM   2664 O  O   . PRO   B 1 130 ? -0.937  10.853  66.866  1.00 37.85 ? 223 PRO   B O   1 
ATOM   2665 C  CB  . PRO   B 1 130 ? -3.041  8.691   65.774  1.00 36.35 ? 223 PRO   B CB  1 
ATOM   2666 C  CG  . PRO   B 1 130 ? -2.864  7.250   66.234  1.00 35.53 ? 223 PRO   B CG  1 
ATOM   2667 C  CD  . PRO   B 1 130 ? -1.500  7.236   66.895  1.00 35.43 ? 223 PRO   B CD  1 
ATOM   2668 N  N   . GLU   B 1 131 ? -1.628  11.521  64.813  1.00 38.98 ? 224 GLU   B N   1 
ATOM   2669 C  CA  . GLU   B 1 131 ? -1.566  12.986  65.072  1.00 40.94 ? 224 GLU   B CA  1 
ATOM   2670 C  C   . GLU   B 1 131 ? -2.764  13.377  65.936  1.00 41.79 ? 224 GLU   B C   1 
ATOM   2671 O  O   . GLU   B 1 131 ? -3.753  12.615  65.957  1.00 41.16 ? 224 GLU   B O   1 
ATOM   2672 C  CB  . GLU   B 1 131 ? -1.530  13.779  63.761  1.00 41.60 ? 224 GLU   B CB  1 
ATOM   2673 C  CG  . GLU   B 1 131 ? -0.258  13.567  62.965  1.00 41.42 ? 224 GLU   B CG  1 
ATOM   2674 C  CD  . GLU   B 1 131 ? 0.996   13.601  63.817  1.00 41.86 ? 224 GLU   B CD  1 
ATOM   2675 O  OE1 . GLU   B 1 131 ? 1.086   14.499  64.690  1.00 44.51 ? 224 GLU   B OE1 1 
ATOM   2676 O  OE2 . GLU   B 1 131 ? 1.847   12.712  63.648  1.00 40.17 ? 224 GLU   B OE2 1 
ATOM   2677 N  N   . VAL   B 1 132 ? -2.640  14.517  66.626  1.00 43.84 ? 225 VAL   B N   1 
ATOM   2678 C  CA  . VAL   B 1 132 ? -3.714  15.168  67.430  1.00 45.43 ? 225 VAL   B CA  1 
ATOM   2679 C  C   . VAL   B 1 132 ? -4.970  15.284  66.557  1.00 45.62 ? 225 VAL   B C   1 
ATOM   2680 O  O   . VAL   B 1 132 ? -4.907  15.982  65.514  1.00 46.40 ? 225 VAL   B O   1 
ATOM   2681 C  CB  . VAL   B 1 132 ? -3.277  16.554  67.950  1.00 47.23 ? 225 VAL   B CB  1 
ATOM   2682 C  CG1 . VAL   B 1 132 ? -4.399  17.209  68.742  1.00 49.56 ? 225 VAL   B CG1 1 
ATOM   2683 C  CG2 . VAL   B 1 132 ? -1.995  16.509  68.774  1.00 47.13 ? 225 VAL   B CG2 1 
ATOM   2684 N  N   . GLY   B 1 133 ? -6.057  14.620  66.964  1.00 45.46 ? 226 GLY   B N   1 
ATOM   2685 C  CA  . GLY   B 1 133 ? -7.342  14.573  66.236  1.00 45.88 ? 226 GLY   B CA  1 
ATOM   2686 C  C   . GLY   B 1 133 ? -7.649  13.182  65.693  1.00 44.50 ? 226 GLY   B C   1 
ATOM   2687 O  O   . GLY   B 1 133 ? -8.812  12.767  65.767  1.00 46.27 ? 226 GLY   B O   1 
ATOM   2688 N  N   . SER   B 1 134 ? -6.641  12.495  65.156  1.00 42.45 ? 227 SER   B N   1 
ATOM   2689 C  CA  . SER   B 1 134 ? -6.783  11.279  64.306  1.00 40.16 ? 227 SER   B CA  1 
ATOM   2690 C  C   . SER   B 1 134 ? -6.608  10.022  65.161  1.00 38.61 ? 227 SER   B C   1 
ATOM   2691 O  O   . SER   B 1 134 ? -5.989  10.116  66.234  1.00 37.60 ? 227 SER   B O   1 
ATOM   2692 C  CB  . SER   B 1 134 ? -5.793  11.333  63.191  1.00 39.42 ? 227 SER   B CB  1 
ATOM   2693 O  OG  . SER   B 1 134 ? -4.604  11.938  63.658  1.00 40.10 ? 227 SER   B OG  1 
ATOM   2694 N  N   . ASP   B 1 135 ? -7.145  8.883   64.693  1.00 37.43 ? 228 ASP   B N   1 
ATOM   2695 C  CA  . ASP   B 1 135 ? -7.198  7.601   65.437  1.00 37.97 ? 228 ASP   B CA  1 
ATOM   2696 C  C   . ASP   B 1 135 ? -6.315  6.550   64.763  1.00 36.06 ? 228 ASP   B C   1 
ATOM   2697 O  O   . ASP   B 1 135 ? -6.304  5.398   65.258  1.00 36.12 ? 228 ASP   B O   1 
ATOM   2698 C  CB  . ASP   B 1 135 ? -8.645  7.125   65.560  1.00 39.30 ? 228 ASP   B CB  1 
ATOM   2699 C  CG  . ASP   B 1 135 ? -9.497  8.024   66.435  1.00 41.21 ? 228 ASP   B CG  1 
ATOM   2700 O  OD1 . ASP   B 1 135 ? -8.989  8.441   67.500  1.00 42.06 ? 228 ASP   B OD1 1 
ATOM   2701 O  OD2 . ASP   B 1 135 ? -10.658 8.327   66.027  1.00 42.81 ? 228 ASP   B OD2 1 
ATOM   2702 N  N   . CYS   B 1 136 ? -5.567  6.907   63.714  1.00 35.25 ? 229 CYS   B N   1 
ATOM   2703 C  CA  . CYS   B 1 136 ? -4.698  5.945   62.977  1.00 34.20 ? 229 CYS   B CA  1 
ATOM   2704 C  C   . CYS   B 1 136 ? -3.426  6.631   62.498  1.00 33.06 ? 229 CYS   B C   1 
ATOM   2705 O  O   . CYS   B 1 136 ? -3.391  7.868   62.454  1.00 32.28 ? 229 CYS   B O   1 
ATOM   2706 C  CB  . CYS   B 1 136 ? -5.428  5.306   61.800  1.00 34.60 ? 229 CYS   B CB  1 
ATOM   2707 S  SG  . CYS   B 1 136 ? -5.884  6.476   60.493  1.00 37.02 ? 229 CYS   B SG  1 
ATOM   2708 N  N   . THR   B 1 137 ? -2.413  5.840   62.151  1.00 31.57 ? 230 THR   B N   1 
ATOM   2709 C  CA  . THR   B 1 137 ? -1.153  6.331   61.544  1.00 31.01 ? 230 THR   B CA  1 
ATOM   2710 C  C   . THR   B 1 137 ? -1.193  5.971   60.065  1.00 30.56 ? 230 THR   B C   1 
ATOM   2711 O  O   . THR   B 1 137 ? -1.455  4.781   59.755  1.00 31.02 ? 230 THR   B O   1 
ATOM   2712 C  CB  . THR   B 1 137 ? 0.073   5.765   62.263  1.00 30.39 ? 230 THR   B CB  1 
ATOM   2713 O  OG1 . THR   B 1 137 ? -0.053  6.129   63.643  1.00 31.86 ? 230 THR   B OG1 1 
ATOM   2714 C  CG2 . THR   B 1 137 ? 1.369   6.253   61.656  1.00 30.16 ? 230 THR   B CG2 1 
ATOM   2715 N  N   . THR   B 1 138 ? -0.966  6.952   59.189  1.00 29.68 ? 231 THR   B N   1 
ATOM   2716 C  CA  . THR   B 1 138 ? -0.950  6.760   57.719  1.00 29.65 ? 231 THR   B CA  1 
ATOM   2717 C  C   . THR   B 1 138 ? 0.503   6.692   57.252  1.00 29.59 ? 231 THR   B C   1 
ATOM   2718 O  O   . THR   B 1 138 ? 1.294   7.593   57.643  1.00 29.03 ? 231 THR   B O   1 
ATOM   2719 C  CB  . THR   B 1 138 ? -1.749  7.844   56.985  1.00 29.91 ? 231 THR   B CB  1 
ATOM   2720 O  OG1 . THR   B 1 138 ? -3.089  7.823   57.456  1.00 30.13 ? 231 THR   B OG1 1 
ATOM   2721 C  CG2 . THR   B 1 138 ? -1.796  7.622   55.492  1.00 30.30 ? 231 THR   B CG2 1 
ATOM   2722 N  N   . ILE   B 1 139 ? 0.827   5.633   56.506  1.00 28.68 ? 232 ILE   B N   1 
ATOM   2723 C  CA  . ILE   B 1 139 ? 2.086   5.486   55.725  1.00 29.72 ? 232 ILE   B CA  1 
ATOM   2724 C  C   . ILE   B 1 139 ? 1.723   5.620   54.244  1.00 29.31 ? 232 ILE   B C   1 
ATOM   2725 O  O   . ILE   B 1 139 ? 0.696   5.029   53.813  1.00 29.94 ? 232 ILE   B O   1 
ATOM   2726 C  CB  . ILE   B 1 139 ? 2.798   4.162   56.033  1.00 29.61 ? 232 ILE   B CB  1 
ATOM   2727 C  CG1 . ILE   B 1 139 ? 3.243   4.100   57.497  1.00 30.15 ? 232 ILE   B CG1 1 
ATOM   2728 C  CG2 . ILE   B 1 139 ? 3.964   3.954   55.081  1.00 30.56 ? 232 ILE   B CG2 1 
ATOM   2729 C  CD1 . ILE   B 1 139 ? 3.723   2.732   57.956  1.00 29.91 ? 232 ILE   B CD1 1 
ATOM   2730 N  N   . HIS   B 1 140 ? 2.535   6.374   53.506  1.00 29.39 ? 233 HIS   B N   1 
ATOM   2731 C  CA  . HIS   B 1 140 ? 2.390   6.583   52.043  1.00 30.18 ? 233 HIS   B CA  1 
ATOM   2732 C  C   . HIS   B 1 140 ? 3.360   5.649   51.327  1.00 28.97 ? 233 HIS   B C   1 
ATOM   2733 O  O   . HIS   B 1 140 ? 4.553   5.945   51.296  1.00 28.62 ? 233 HIS   B O   1 
ATOM   2734 C  CB  . HIS   B 1 140 ? 2.563   8.072   51.685  1.00 31.76 ? 233 HIS   B CB  1 
ATOM   2735 C  CG  . HIS   B 1 140 ? 1.428   8.921   52.147  1.00 32.72 ? 233 HIS   B CG  1 
ATOM   2736 N  ND1 . HIS   B 1 140 ? 1.509   10.299  52.203  1.00 34.86 ? 233 HIS   B ND1 1 
ATOM   2737 C  CD2 . HIS   B 1 140 ? 0.176   8.609   52.545  1.00 32.99 ? 233 HIS   B CD2 1 
ATOM   2738 C  CE1 . HIS   B 1 140 ? 0.363   10.792  52.622  1.00 34.79 ? 233 HIS   B CE1 1 
ATOM   2739 N  NE2 . HIS   B 1 140 ? -0.466  9.779   52.843  1.00 33.39 ? 233 HIS   B NE2 1 
ATOM   2740 N  N   . TYR   B 1 141 ? 2.857   4.518   50.826  1.00 29.01 ? 234 TYR   B N   1 
ATOM   2741 C  CA  . TYR   B 1 141 ? 3.619   3.575   49.976  1.00 28.67 ? 234 TYR   B CA  1 
ATOM   2742 C  C   . TYR   B 1 141 ? 3.525   4.028   48.513  1.00 30.13 ? 234 TYR   B C   1 
ATOM   2743 O  O   . TYR   B 1 141 ? 2.497   4.600   48.088  1.00 31.96 ? 234 TYR   B O   1 
ATOM   2744 C  CB  . TYR   B 1 141 ? 3.124   2.142   50.206  1.00 27.73 ? 234 TYR   B CB  1 
ATOM   2745 C  CG  . TYR   B 1 141 ? 3.457   1.614   51.580  1.00 26.33 ? 234 TYR   B CG  1 
ATOM   2746 C  CD1 . TYR   B 1 141 ? 4.767   1.340   51.938  1.00 25.45 ? 234 TYR   B CD1 1 
ATOM   2747 C  CD2 . TYR   B 1 141 ? 2.477   1.468   52.550  1.00 25.09 ? 234 TYR   B CD2 1 
ATOM   2748 C  CE1 . TYR   B 1 141 ? 5.093   0.876   53.204  1.00 24.83 ? 234 TYR   B CE1 1 
ATOM   2749 C  CE2 . TYR   B 1 141 ? 2.787   1.021   53.822  1.00 24.69 ? 234 TYR   B CE2 1 
ATOM   2750 C  CZ  . TYR   B 1 141 ? 4.102   0.717   54.150  1.00 24.62 ? 234 TYR   B CZ  1 
ATOM   2751 O  OH  . TYR   B 1 141 ? 4.397   0.282   55.408  1.00 23.54 ? 234 TYR   B OH  1 
ATOM   2752 N  N   . ASN   B 1 142 ? 4.604   3.796   47.757  1.00 30.54 ? 235 ASN   B N   1 
ATOM   2753 C  CA  . ASN   B 1 142 ? 4.642   3.869   46.277  1.00 31.44 ? 235 ASN   B CA  1 
ATOM   2754 C  C   . ASN   B 1 142 ? 5.044   2.492   45.752  1.00 31.43 ? 235 ASN   B C   1 
ATOM   2755 O  O   . ASN   B 1 142 ? 6.042   1.950   46.247  1.00 31.60 ? 235 ASN   B O   1 
ATOM   2756 C  CB  . ASN   B 1 142 ? 5.644   4.892   45.748  1.00 32.10 ? 235 ASN   B CB  1 
ATOM   2757 C  CG  . ASN   B 1 142 ? 5.408   6.311   46.219  1.00 32.44 ? 235 ASN   B CG  1 
ATOM   2758 O  OD1 . ASN   B 1 142 ? 6.304   7.136   46.129  1.00 33.28 ? 235 ASN   B OD1 1 
ATOM   2759 N  ND2 . ASN   B 1 142 ? 4.235   6.604   46.749  1.00 32.48 ? 235 ASN   B ND2 1 
ATOM   2760 N  N   . TYR   B 1 143 ? 4.299   1.969   44.779  1.00 32.60 ? 236 TYR   B N   1 
ATOM   2761 C  CA  . TYR   B 1 143 ? 4.659   0.754   44.007  1.00 32.86 ? 236 TYR   B CA  1 
ATOM   2762 C  C   . TYR   B 1 143 ? 5.271   1.231   42.688  1.00 34.43 ? 236 TYR   B C   1 
ATOM   2763 O  O   . TYR   B 1 143 ? 4.625   2.016   41.944  1.00 36.01 ? 236 TYR   B O   1 
ATOM   2764 C  CB  . TYR   B 1 143 ? 3.442   -0.166  43.884  1.00 32.97 ? 236 TYR   B CB  1 
ATOM   2765 C  CG  . TYR   B 1 143 ? 2.971   -0.723  45.203  1.00 32.01 ? 236 TYR   B CG  1 
ATOM   2766 C  CD1 . TYR   B 1 143 ? 2.145   0.020   46.028  1.00 31.22 ? 236 TYR   B CD1 1 
ATOM   2767 C  CD2 . TYR   B 1 143 ? 3.364   -1.980  45.644  1.00 31.77 ? 236 TYR   B CD2 1 
ATOM   2768 C  CE1 . TYR   B 1 143 ? 1.732   -0.455  47.260  1.00 30.85 ? 236 TYR   B CE1 1 
ATOM   2769 C  CE2 . TYR   B 1 143 ? 2.958   -2.477  46.871  1.00 30.61 ? 236 TYR   B CE2 1 
ATOM   2770 C  CZ  . TYR   B 1 143 ? 2.138   -1.713  47.683  1.00 30.57 ? 236 TYR   B CZ  1 
ATOM   2771 O  OH  . TYR   B 1 143 ? 1.739   -2.169  48.907  1.00 29.03 ? 236 TYR   B OH  1 
ATOM   2772 N  N   . MET   B 1 144 ? 6.493   0.777   42.407  1.00 34.89 ? 237 MET   B N   1 
ATOM   2773 C  CA  . MET   B 1 144 ? 7.392   1.377   41.389  1.00 36.47 ? 237 MET   B CA  1 
ATOM   2774 C  C   . MET   B 1 144 ? 7.444   0.514   40.110  1.00 38.10 ? 237 MET   B C   1 
ATOM   2775 O  O   . MET   B 1 144 ? 8.291   0.783   39.253  1.00 39.37 ? 237 MET   B O   1 
ATOM   2776 C  CB  . MET   B 1 144 ? 8.789   1.539   41.989  1.00 36.04 ? 237 MET   B CB  1 
ATOM   2777 C  CG  . MET   B 1 144 ? 8.824   2.444   43.218  1.00 35.00 ? 237 MET   B CG  1 
ATOM   2778 S  SD  . MET   B 1 144 ? 8.020   4.050   42.956  1.00 35.26 ? 237 MET   B SD  1 
ATOM   2779 C  CE  . MET   B 1 144 ? 8.973   4.646   41.560  1.00 36.18 ? 237 MET   B CE  1 
ATOM   2780 N  N   . CYS   B 1 145 ? 6.526   -0.442  39.970  1.00 38.75 ? 238 CYS   B N   1 
ATOM   2781 C  CA  . CYS   B 1 145 ? 6.304   -1.285  38.772  1.00 40.95 ? 238 CYS   B CA  1 
ATOM   2782 C  C   . CYS   B 1 145 ? 4.806   -1.572  38.634  1.00 41.45 ? 238 CYS   B C   1 
ATOM   2783 O  O   . CYS   B 1 145 ? 4.129   -1.703  39.669  1.00 40.13 ? 238 CYS   B O   1 
ATOM   2784 C  CB  . CYS   B 1 145 ? 7.107   -2.567  38.909  1.00 41.48 ? 238 CYS   B CB  1 
ATOM   2785 S  SG  . CYS   B 1 145 ? 8.608   -2.531  38.024  1.00 43.36 ? 238 CYS   B SG  1 
ATOM   2786 N  N   . ASN   B 1 146 ? 4.305   -1.629  37.397  1.00 42.97 ? 239 ASN   B N   1 
ATOM   2787 C  CA  . ASN   B 1 146 ? 2.934   -2.078  37.055  1.00 43.50 ? 239 ASN   B CA  1 
ATOM   2788 C  C   . ASN   B 1 146 ? 2.873   -3.603  37.170  1.00 43.45 ? 239 ASN   B C   1 
ATOM   2789 O  O   . ASN   B 1 146 ? 3.883   -4.262  36.868  1.00 43.03 ? 239 ASN   B O   1 
ATOM   2790 C  CB  . ASN   B 1 146 ? 2.502   -1.576  35.677  1.00 46.03 ? 239 ASN   B CB  1 
ATOM   2791 C  CG  . ASN   B 1 146 ? 2.063   -0.125  35.685  1.00 47.34 ? 239 ASN   B CG  1 
ATOM   2792 O  OD1 . ASN   B 1 146 ? 1.291   0.298   36.544  1.00 47.51 ? 239 ASN   B OD1 1 
ATOM   2793 N  ND2 . ASN   B 1 146 ? 2.552   0.659   34.739  1.00 49.42 ? 239 ASN   B ND2 1 
ATOM   2794 N  N   . SER   B 1 147 ? 1.727   -4.143  37.596  1.00 43.41 ? 240 SER   B N   1 
ATOM   2795 C  CA  . SER   B 1 147 ? 1.438   -5.603  37.634  1.00 44.29 ? 240 SER   B CA  1 
ATOM   2796 C  C   . SER   B 1 147 ? 1.700   -6.211  36.249  1.00 45.82 ? 240 SER   B C   1 
ATOM   2797 O  O   . SER   B 1 147 ? 2.115   -7.382  36.195  1.00 46.70 ? 240 SER   B O   1 
ATOM   2798 C  CB  . SER   B 1 147 ? 0.019   -5.877  38.093  1.00 44.26 ? 240 SER   B CB  1 
ATOM   2799 O  OG  . SER   B 1 147 ? -0.183  -5.429  39.425  1.00 43.99 ? 240 SER   B OG  1 
ATOM   2800 N  N   . SER   B 1 148 ? 1.470   -5.441  35.183  1.00 46.85 ? 241 SER   B N   1 
ATOM   2801 C  CA  . SER   B 1 148 ? 1.588   -5.860  33.758  1.00 49.81 ? 241 SER   B CA  1 
ATOM   2802 C  C   . SER   B 1 148 ? 3.044   -5.879  33.265  1.00 50.55 ? 241 SER   B C   1 
ATOM   2803 O  O   . SER   B 1 148 ? 3.273   -6.501  32.220  1.00 53.08 ? 241 SER   B O   1 
ATOM   2804 C  CB  . SER   B 1 148 ? 0.749   -4.968  32.885  1.00 51.31 ? 241 SER   B CB  1 
ATOM   2805 O  OG  . SER   B 1 148 ? 1.216   -3.625  32.967  1.00 50.97 ? 241 SER   B OG  1 
ATOM   2806 N  N   . CYS   B 1 149 ? 3.989   -5.235  33.968  1.00 49.23 ? 242 CYS   B N   1 
ATOM   2807 C  CA  . CYS   B 1 149 ? 5.400   -5.044  33.517  1.00 50.30 ? 242 CYS   B CA  1 
ATOM   2808 C  C   . CYS   B 1 149 ? 6.021   -6.370  33.049  1.00 51.38 ? 242 CYS   B C   1 
ATOM   2809 O  O   . CYS   B 1 149 ? 6.208   -7.287  33.891  1.00 49.63 ? 242 CYS   B O   1 
ATOM   2810 C  CB  . CYS   B 1 149 ? 6.265   -4.468  34.633  1.00 48.67 ? 242 CYS   B CB  1 
ATOM   2811 S  SG  . CYS   B 1 149 ? 6.244   -2.711  34.776  1.00 48.86 ? 242 CYS   B SG  1 
ATOM   2812 N  N   . MET   B 1 150 ? 6.344   -6.423  31.752  1.00 54.13 ? 243 MET   B N   1 
ATOM   2813 C  CA  . MET   B 1 150 ? 7.136   -7.497  31.095  1.00 56.21 ? 243 MET   B CA  1 
ATOM   2814 C  C   . MET   B 1 150 ? 8.497   -7.573  31.797  1.00 55.70 ? 243 MET   B C   1 
ATOM   2815 O  O   . MET   B 1 150 ? 9.109   -6.498  32.010  1.00 53.75 ? 243 MET   B O   1 
ATOM   2816 C  CB  . MET   B 1 150 ? 7.387   -7.180  29.616  1.00 58.98 ? 243 MET   B CB  1 
ATOM   2817 C  CG  . MET   B 1 150 ? 6.143   -7.048  28.760  1.00 60.36 ? 243 MET   B CG  1 
ATOM   2818 S  SD  . MET   B 1 150 ? 6.550   -6.723  27.017  1.00 63.86 ? 243 MET   B SD  1 
ATOM   2819 C  CE  . MET   B 1 150 ? 7.637   -8.097  26.633  1.00 65.51 ? 243 MET   B CE  1 
ATOM   2820 N  N   . GLY   B 1 151 ? 8.945   -8.777  32.162  1.00 56.64 ? 244 GLY   B N   1 
ATOM   2821 C  CA  . GLY   B 1 151 ? 10.263  -8.992  32.789  1.00 57.18 ? 244 GLY   B CA  1 
ATOM   2822 C  C   . GLY   B 1 151 ? 10.289  -8.532  34.232  1.00 55.70 ? 244 GLY   B C   1 
ATOM   2823 O  O   . GLY   B 1 151 ? 11.396  -8.308  34.752  1.00 57.04 ? 244 GLY   B O   1 
ATOM   2824 N  N   . GLY   B 1 152 ? 9.111   -8.375  34.848  1.00 55.60 ? 245 GLY   B N   1 
ATOM   2825 C  CA  . GLY   B 1 152 ? 8.949   -8.049  36.277  1.00 53.34 ? 245 GLY   B CA  1 
ATOM   2826 C  C   . GLY   B 1 152 ? 7.905   -8.925  36.910  1.00 53.17 ? 245 GLY   B C   1 
ATOM   2827 O  O   . GLY   B 1 152 ? 8.036   -10.142 36.764  1.00 54.74 ? 245 GLY   B O   1 
ATOM   2828 N  N   . MET   B 1 153 ? 6.870   -8.344  37.520  1.00 50.89 ? 246 MET   B N   1 
ATOM   2829 C  CA  . MET   B 1 153 ? 5.717   -9.116  38.062  1.00 50.78 ? 246 MET   B CA  1 
ATOM   2830 C  C   . MET   B 1 153 ? 4.999   -9.826  36.904  1.00 52.67 ? 246 MET   B C   1 
ATOM   2831 O  O   . MET   B 1 153 ? 4.544   -10.972 37.114  1.00 53.05 ? 246 MET   B O   1 
ATOM   2832 C  CB  . MET   B 1 153 ? 4.754   -8.195  38.809  1.00 49.00 ? 246 MET   B CB  1 
ATOM   2833 C  CG  . MET   B 1 153 ? 5.369   -7.635  40.076  1.00 47.05 ? 246 MET   B CG  1 
ATOM   2834 S  SD  . MET   B 1 153 ? 4.198   -6.705  41.086  1.00 45.26 ? 246 MET   B SD  1 
ATOM   2835 C  CE  . MET   B 1 153 ? 4.152   -5.146  40.200  1.00 45.08 ? 246 MET   B CE  1 
ATOM   2836 N  N   . ASN   B 1 154 ? 4.929   -9.182  35.731  1.00 53.86 ? 247 ASN   B N   1 
ATOM   2837 C  CA  . ASN   B 1 154 ? 4.430   -9.773  34.461  1.00 55.85 ? 247 ASN   B CA  1 
ATOM   2838 C  C   . ASN   B 1 154 ? 3.085   -10.464 34.722  1.00 56.73 ? 247 ASN   B C   1 
ATOM   2839 O  O   . ASN   B 1 154 ? 2.962   -11.683 34.445  1.00 57.96 ? 247 ASN   B O   1 
ATOM   2840 C  CB  . ASN   B 1 154 ? 5.467   -10.716 33.848  1.00 57.76 ? 247 ASN   B CB  1 
ATOM   2841 C  CG  . ASN   B 1 154 ? 5.049   -11.249 32.494  1.00 60.12 ? 247 ASN   B CG  1 
ATOM   2842 O  OD1 . ASN   B 1 154 ? 4.429   -10.534 31.704  1.00 60.53 ? 247 ASN   B OD1 1 
ATOM   2843 N  ND2 . ASN   B 1 154 ? 5.381   -12.501 32.221  1.00 61.49 ? 247 ASN   B ND2 1 
ATOM   2844 N  N   . ARG   B 1 155 ? 2.135   -9.695  35.259  1.00 55.09 ? 248 ARG   B N   1 
ATOM   2845 C  CA  . ARG   B 1 155 ? 0.691   -10.031 35.409  1.00 55.88 ? 248 ARG   B CA  1 
ATOM   2846 C  C   . ARG   B 1 155 ? 0.473   -10.967 36.604  1.00 54.78 ? 248 ARG   B C   1 
ATOM   2847 O  O   . ARG   B 1 155 ? -0.691  -11.265 36.889  1.00 56.29 ? 248 ARG   B O   1 
ATOM   2848 C  CB  . ARG   B 1 155 ? 0.121   -10.582 34.096  1.00 57.88 ? 248 ARG   B CB  1 
ATOM   2849 C  CG  . ARG   B 1 155 ? 0.350   -9.656  32.907  1.00 58.95 ? 248 ARG   B CG  1 
ATOM   2850 C  CD  . ARG   B 1 155 ? -0.600  -9.849  31.735  1.00 60.77 ? 248 ARG   B CD  1 
ATOM   2851 N  NE  . ARG   B 1 155 ? -1.993  -9.679  32.114  1.00 60.19 ? 248 ARG   B NE  1 
ATOM   2852 C  CZ  . ARG   B 1 155 ? -2.627  -8.512  32.236  1.00 59.89 ? 248 ARG   B CZ  1 
ATOM   2853 N  NH1 . ARG   B 1 155 ? -2.006  -7.366  31.990  1.00 58.41 ? 248 ARG   B NH1 1 
ATOM   2854 N  NH2 . ARG   B 1 155 ? -3.905  -8.503  32.589  1.00 60.14 ? 248 ARG   B NH2 1 
ATOM   2855 N  N   . ARG   B 1 156 ? 1.529   -11.368 37.313  1.00 53.90 ? 249 ARG   B N   1 
ATOM   2856 C  CA  . ARG   B 1 156 ? 1.411   -12.233 38.517  1.00 52.60 ? 249 ARG   B CA  1 
ATOM   2857 C  C   . ARG   B 1 156 ? 0.966   -11.399 39.720  1.00 49.91 ? 249 ARG   B C   1 
ATOM   2858 O  O   . ARG   B 1 156 ? 1.543   -10.354 40.011  1.00 49.62 ? 249 ARG   B O   1 
ATOM   2859 C  CB  . ARG   B 1 156 ? 2.731   -12.951 38.789  1.00 52.86 ? 249 ARG   B CB  1 
ATOM   2860 C  CG  . ARG   B 1 156 ? 3.157   -13.874 37.653  1.00 55.02 ? 249 ARG   B CG  1 
ATOM   2861 C  CD  . ARG   B 1 156 ? 4.529   -14.464 37.885  1.00 55.14 ? 249 ARG   B CD  1 
ATOM   2862 N  NE  . ARG   B 1 156 ? 5.566   -13.444 37.831  1.00 54.37 ? 249 ARG   B NE  1 
ATOM   2863 C  CZ  . ARG   B 1 156 ? 6.855   -13.663 38.073  1.00 54.49 ? 249 ARG   B CZ  1 
ATOM   2864 N  NH1 . ARG   B 1 156 ? 7.284   -14.869 38.393  1.00 55.21 ? 249 ARG   B NH1 1 
ATOM   2865 N  NH2 . ARG   B 1 156 ? 7.719   -12.671 37.978  1.00 53.46 ? 249 ARG   B NH2 1 
ATOM   2866 N  N   . PRO   B 1 157 ? -0.079  -11.836 40.454  1.00 48.34 ? 250 PRO   B N   1 
ATOM   2867 C  CA  . PRO   B 1 157 ? -0.566  -11.099 41.617  1.00 45.67 ? 250 PRO   B CA  1 
ATOM   2868 C  C   . PRO   B 1 157 ? 0.409   -11.196 42.801  1.00 43.71 ? 250 PRO   B C   1 
ATOM   2869 O  O   . PRO   B 1 157 ? 1.051   -12.211 42.970  1.00 44.57 ? 250 PRO   B O   1 
ATOM   2870 C  CB  . PRO   B 1 157 ? -1.912  -11.768 41.935  1.00 46.55 ? 250 PRO   B CB  1 
ATOM   2871 C  CG  . PRO   B 1 157 ? -1.759  -13.180 41.423  1.00 48.85 ? 250 PRO   B CG  1 
ATOM   2872 C  CD  . PRO   B 1 157 ? -0.857  -13.063 40.208  1.00 49.87 ? 250 PRO   B CD  1 
ATOM   2873 N  N   . ILE   B 1 158 ? 0.486   -10.135 43.594  1.00 40.48 ? 251 ILE   B N   1 
ATOM   2874 C  CA  . ILE   B 1 158 ? 1.383   -10.026 44.783  1.00 38.85 ? 251 ILE   B CA  1 
ATOM   2875 C  C   . ILE   B 1 158 ? 0.554   -9.691  46.023  1.00 37.33 ? 251 ILE   B C   1 
ATOM   2876 O  O   . ILE   B 1 158 ? -0.549  -9.147  45.886  1.00 37.04 ? 251 ILE   B O   1 
ATOM   2877 C  CB  . ILE   B 1 158 ? 2.495   -8.996  44.531  1.00 38.15 ? 251 ILE   B CB  1 
ATOM   2878 C  CG1 . ILE   B 1 158 ? 1.937   -7.605  44.200  1.00 37.12 ? 251 ILE   B CG1 1 
ATOM   2879 C  CG2 . ILE   B 1 158 ? 3.429   -9.499  43.438  1.00 39.33 ? 251 ILE   B CG2 1 
ATOM   2880 C  CD1 . ILE   B 1 158 ? 2.872   -6.479  44.560  1.00 36.32 ? 251 ILE   B CD1 1 
ATOM   2881 N  N   . LEU   B 1 159 ? 1.072   -10.058 47.191  1.00 36.55 ? 252 LEU   B N   1 
ATOM   2882 C  CA  . LEU   B 1 159 ? 0.606   -9.570  48.517  1.00 34.62 ? 252 LEU   B CA  1 
ATOM   2883 C  C   . LEU   B 1 159 ? 1.665   -8.614  49.058  1.00 32.24 ? 252 LEU   B C   1 
ATOM   2884 O  O   . LEU   B 1 159 ? 2.866   -8.866  48.793  1.00 31.52 ? 252 LEU   B O   1 
ATOM   2885 C  CB  . LEU   B 1 159 ? 0.421   -10.736 49.491  1.00 35.85 ? 252 LEU   B CB  1 
ATOM   2886 C  CG  . LEU   B 1 159 ? -0.406  -11.902 48.966  1.00 38.12 ? 252 LEU   B CG  1 
ATOM   2887 C  CD1 . LEU   B 1 159 ? 0.480   -12.863 48.224  1.00 39.22 ? 252 LEU   B CD1 1 
ATOM   2888 C  CD2 . LEU   B 1 159 ? -1.110  -12.628 50.103  1.00 39.12 ? 252 LEU   B CD2 1 
ATOM   2889 N  N   . THR   B 1 160 ? 1.234   -7.560  49.758  1.00 29.65 ? 253 THR   B N   1 
ATOM   2890 C  CA  . THR   B 1 160 ? 2.078   -6.775  50.689  1.00 27.52 ? 253 THR   B CA  1 
ATOM   2891 C  C   . THR   B 1 160 ? 1.829   -7.274  52.110  1.00 26.35 ? 253 THR   B C   1 
ATOM   2892 O  O   . THR   B 1 160 ? 0.663   -7.333  52.508  1.00 26.97 ? 253 THR   B O   1 
ATOM   2893 C  CB  . THR   B 1 160 ? 1.772   -5.274  50.631  1.00 27.21 ? 253 THR   B CB  1 
ATOM   2894 O  OG1 . THR   B 1 160 ? 1.960   -4.832  49.292  1.00 28.08 ? 253 THR   B OG1 1 
ATOM   2895 C  CG2 . THR   B 1 160 ? 2.638   -4.469  51.570  1.00 26.72 ? 253 THR   B CG2 1 
ATOM   2896 N  N   . ILE   B 1 161 ? 2.881   -7.586  52.850  1.00 25.51 ? 254 ILE   B N   1 
ATOM   2897 C  CA  . ILE   B 1 161 ? 2.837   -7.983  54.288  1.00 25.53 ? 254 ILE   B CA  1 
ATOM   2898 C  C   . ILE   B 1 161 ? 3.380   -6.806  55.108  1.00 25.07 ? 254 ILE   B C   1 
ATOM   2899 O  O   . ILE   B 1 161 ? 4.511   -6.409  54.821  1.00 23.35 ? 254 ILE   B O   1 
ATOM   2900 C  CB  . ILE   B 1 161 ? 3.662   -9.265  54.506  1.00 26.37 ? 254 ILE   B CB  1 
ATOM   2901 C  CG1 . ILE   B 1 161 ? 3.173   -10.382 53.573  1.00 27.24 ? 254 ILE   B CG1 1 
ATOM   2902 C  CG2 . ILE   B 1 161 ? 3.627   -9.682  55.974  1.00 26.75 ? 254 ILE   B CG2 1 
ATOM   2903 C  CD1 . ILE   B 1 161 ? 4.113   -11.566 53.447  1.00 28.41 ? 254 ILE   B CD1 1 
ATOM   2904 N  N   . ILE   B 1 162 ? 2.549   -6.239  55.994  1.00 25.35 ? 255 ILE   B N   1 
ATOM   2905 C  CA  . ILE   B 1 162 ? 2.919   -5.145  56.940  1.00 25.63 ? 255 ILE   B CA  1 
ATOM   2906 C  C   . ILE   B 1 162 ? 3.128   -5.767  58.317  1.00 26.92 ? 255 ILE   B C   1 
ATOM   2907 O  O   . ILE   B 1 162 ? 2.150   -6.310  58.883  1.00 28.09 ? 255 ILE   B O   1 
ATOM   2908 C  CB  . ILE   B 1 162 ? 1.852   -4.026  56.998  1.00 24.79 ? 255 ILE   B CB  1 
ATOM   2909 C  CG1 . ILE   B 1 162 ? 1.426   -3.526  55.613  1.00 24.46 ? 255 ILE   B CG1 1 
ATOM   2910 C  CG2 . ILE   B 1 162 ? 2.320   -2.889  57.897  1.00 24.27 ? 255 ILE   B CG2 1 
ATOM   2911 C  CD1 . ILE   B 1 162 ? 2.536   -3.004  54.758  1.00 24.65 ? 255 ILE   B CD1 1 
ATOM   2912 N  N   . THR   B 1 163 ? 4.360   -5.740  58.824  1.00 28.56 ? 256 THR   B N   1 
ATOM   2913 C  CA  . THR   B 1 163 ? 4.712   -6.289  60.151  1.00 29.84 ? 256 THR   B CA  1 
ATOM   2914 C  C   . THR   B 1 163 ? 5.083   -5.139  61.080  1.00 29.76 ? 256 THR   B C   1 
ATOM   2915 O  O   . THR   B 1 163 ? 5.752   -4.194  60.636  1.00 29.41 ? 256 THR   B O   1 
ATOM   2916 C  CB  . THR   B 1 163 ? 5.835   -7.327  60.057  1.00 31.03 ? 256 THR   B CB  1 
ATOM   2917 O  OG1 . THR   B 1 163 ? 7.003   -6.666  59.579  1.00 31.85 ? 256 THR   B OG1 1 
ATOM   2918 C  CG2 . THR   B 1 163 ? 5.504   -8.465  59.124  1.00 31.58 ? 256 THR   B CG2 1 
ATOM   2919 N  N   . LEU   B 1 164 ? 4.600   -5.219  62.313  1.00 31.23 ? 257 LEU   B N   1 
ATOM   2920 C  CA  . LEU   B 1 164 ? 4.966   -4.308  63.419  1.00 31.94 ? 257 LEU   B CA  1 
ATOM   2921 C  C   . LEU   B 1 164 ? 6.034   -5.034  64.243  1.00 33.15 ? 257 LEU   B C   1 
ATOM   2922 O  O   . LEU   B 1 164 ? 5.793   -6.188  64.627  1.00 33.66 ? 257 LEU   B O   1 
ATOM   2923 C  CB  . LEU   B 1 164 ? 3.675   -4.022  64.189  1.00 31.98 ? 257 LEU   B CB  1 
ATOM   2924 C  CG  . LEU   B 1 164 ? 3.712   -2.878  65.180  1.00 32.37 ? 257 LEU   B CG  1 
ATOM   2925 C  CD1 . LEU   B 1 164 ? 3.667   -1.535  64.447  1.00 30.90 ? 257 LEU   B CD1 1 
ATOM   2926 C  CD2 . LEU   B 1 164 ? 2.552   -2.999  66.165  1.00 33.17 ? 257 LEU   B CD2 1 
ATOM   2927 N  N   . GLU   B 1 165 ? 7.210   -4.436  64.419  1.00 33.40 ? 258 GLU   B N   1 
ATOM   2928 C  CA  . GLU   B 1 165 ? 8.316   -5.067  65.188  1.00 34.68 ? 258 GLU   B CA  1 
ATOM   2929 C  C   . GLU   B 1 165 ? 8.813   -4.100  66.256  1.00 34.67 ? 258 GLU   B C   1 
ATOM   2930 O  O   . GLU   B 1 165 ? 8.679   -2.877  66.058  1.00 32.63 ? 258 GLU   B O   1 
ATOM   2931 C  CB  . GLU   B 1 165 ? 9.484   -5.531  64.307  1.00 35.18 ? 258 GLU   B CB  1 
ATOM   2932 C  CG  . GLU   B 1 165 ? 9.368   -5.209  62.842  1.00 35.74 ? 258 GLU   B CG  1 
ATOM   2933 C  CD  . GLU   B 1 165 ? 10.567  -5.700  62.039  1.00 36.37 ? 258 GLU   B CD  1 
ATOM   2934 O  OE1 . GLU   B 1 165 ? 11.691  -5.204  62.271  1.00 36.72 ? 258 GLU   B OE1 1 
ATOM   2935 O  OE2 . GLU   B 1 165 ? 10.386  -6.604  61.185  1.00 38.42 ? 258 GLU   B OE2 1 
ATOM   2936 N  N   . ASP   B 1 166 ? 9.390   -4.646  67.328  1.00 35.73 ? 259 ASP   B N   1 
ATOM   2937 C  CA  . ASP   B 1 166 ? 10.050  -3.834  68.377  1.00 37.58 ? 259 ASP   B CA  1 
ATOM   2938 C  C   . ASP   B 1 166 ? 11.433  -3.451  67.859  1.00 37.96 ? 259 ASP   B C   1 
ATOM   2939 O  O   . ASP   B 1 166 ? 11.783  -3.850  66.736  1.00 38.38 ? 259 ASP   B O   1 
ATOM   2940 C  CB  . ASP   B 1 166 ? 10.072  -4.549  69.727  1.00 38.86 ? 259 ASP   B CB  1 
ATOM   2941 C  CG  . ASP   B 1 166 ? 10.994  -5.753  69.826  1.00 40.00 ? 259 ASP   B CG  1 
ATOM   2942 O  OD1 . ASP   B 1 166 ? 11.841  -5.946  68.932  1.00 40.42 ? 259 ASP   B OD1 1 
ATOM   2943 O  OD2 . ASP   B 1 166 ? 10.856  -6.491  70.797  1.00 40.28 ? 259 ASP   B OD2 1 
ATOM   2944 N  N   . SER   B 1 167 ? 12.184  -2.698  68.653  1.00 39.47 ? 260 SER   B N   1 
ATOM   2945 C  CA  . SER   B 1 167 ? 13.501  -2.134  68.276  1.00 40.01 ? 260 SER   B CA  1 
ATOM   2946 C  C   . SER   B 1 167 ? 14.492  -3.270  67.989  1.00 40.36 ? 260 SER   B C   1 
ATOM   2947 O  O   . SER   B 1 167 ? 15.411  -3.040  67.192  1.00 39.61 ? 260 SER   B O   1 
ATOM   2948 C  CB  . SER   B 1 167 ? 13.980  -1.198  69.340  1.00 40.84 ? 260 SER   B CB  1 
ATOM   2949 O  OG  . SER   B 1 167 ? 14.153  -1.887  70.573  1.00 42.65 ? 260 SER   B OG  1 
ATOM   2950 N  N   . SER   B 1 168 ? 14.290  -4.458  68.579  1.00 40.89 ? 261 SER   B N   1 
ATOM   2951 C  CA  . SER   B 1 168 ? 15.180  -5.643  68.423  1.00 41.63 ? 261 SER   B CA  1 
ATOM   2952 C  C   . SER   B 1 168 ? 14.755  -6.509  67.232  1.00 40.73 ? 261 SER   B C   1 
ATOM   2953 O  O   . SER   B 1 168 ? 15.486  -7.466  66.927  1.00 41.77 ? 261 SER   B O   1 
ATOM   2954 C  CB  . SER   B 1 168 ? 15.228  -6.469  69.686  1.00 42.50 ? 261 SER   B CB  1 
ATOM   2955 O  OG  . SER   B 1 168 ? 15.797  -5.724  70.742  1.00 43.15 ? 261 SER   B OG  1 
ATOM   2956 N  N   . GLY   B 1 169 ? 13.627  -6.198  66.591  1.00 39.12 ? 262 GLY   B N   1 
ATOM   2957 C  CA  . GLY   B 1 169 ? 13.103  -6.950  65.432  1.00 38.08 ? 262 GLY   B CA  1 
ATOM   2958 C  C   . GLY   B 1 169 ? 12.146  -8.073  65.828  1.00 38.95 ? 262 GLY   B C   1 
ATOM   2959 O  O   . GLY   B 1 169 ? 11.762  -8.850  64.929  1.00 40.09 ? 262 GLY   B O   1 
ATOM   2960 N  N   . ASN   B 1 170 ? 11.713  -8.128  67.090  1.00 38.91 ? 263 ASN   B N   1 
ATOM   2961 C  CA  . ASN   B 1 170 ? 10.709  -9.123  67.559  1.00 39.36 ? 263 ASN   B CA  1 
ATOM   2962 C  C   . ASN   B 1 170 ? 9.341   -8.756  66.972  1.00 37.43 ? 263 ASN   B C   1 
ATOM   2963 O  O   . ASN   B 1 170 ? 8.981   -7.551  67.004  1.00 36.47 ? 263 ASN   B O   1 
ATOM   2964 C  CB  . ASN   B 1 170 ? 10.674  -9.245  69.085  1.00 40.77 ? 263 ASN   B CB  1 
ATOM   2965 C  CG  . ASN   B 1 170 ? 11.994  -9.710  69.670  1.00 42.92 ? 263 ASN   B CG  1 
ATOM   2966 O  OD1 . ASN   B 1 170 ? 12.516  -10.762 69.297  1.00 43.97 ? 263 ASN   B OD1 1 
ATOM   2967 N  ND2 . ASN   B 1 170 ? 12.554  -8.932  70.584  1.00 43.27 ? 263 ASN   B ND2 1 
ATOM   2968 N  N   . LEU   B 1 171 ? 8.632   -9.738  66.410  1.00 37.08 ? 264 LEU   B N   1 
ATOM   2969 C  CA  . LEU   B 1 171 ? 7.278   -9.567  65.811  1.00 36.49 ? 264 LEU   B CA  1 
ATOM   2970 C  C   . LEU   B 1 171 ? 6.291   -9.108  66.892  1.00 36.54 ? 264 LEU   B C   1 
ATOM   2971 O  O   . LEU   B 1 171 ? 6.186   -9.804  67.909  1.00 38.34 ? 264 LEU   B O   1 
ATOM   2972 C  CB  . LEU   B 1 171 ? 6.836   -10.893 65.180  1.00 37.15 ? 264 LEU   B CB  1 
ATOM   2973 C  CG  . LEU   B 1 171 ? 5.414   -10.940 64.607  1.00 36.92 ? 264 LEU   B CG  1 
ATOM   2974 C  CD1 . LEU   B 1 171 ? 5.290   -10.143 63.308  1.00 35.64 ? 264 LEU   B CD1 1 
ATOM   2975 C  CD2 . LEU   B 1 171 ? 4.983   -12.376 64.392  1.00 38.03 ? 264 LEU   B CD2 1 
ATOM   2976 N  N   . LEU   B 1 172 ? 5.598   -7.983  66.677  1.00 35.63 ? 265 LEU   B N   1 
ATOM   2977 C  CA  . LEU   B 1 172 ? 4.495   -7.476  67.543  1.00 36.35 ? 265 LEU   B CA  1 
ATOM   2978 C  C   . LEU   B 1 172 ? 3.133   -7.690  66.874  1.00 36.11 ? 265 LEU   B C   1 
ATOM   2979 O  O   . LEU   B 1 172 ? 2.145   -7.882  67.613  1.00 37.72 ? 265 LEU   B O   1 
ATOM   2980 C  CB  . LEU   B 1 172 ? 4.695   -5.979  67.808  1.00 35.82 ? 265 LEU   B CB  1 
ATOM   2981 C  CG  . LEU   B 1 172 ? 6.052   -5.575  68.366  1.00 36.13 ? 265 LEU   B CG  1 
ATOM   2982 C  CD1 . LEU   B 1 172 ? 6.044   -4.103  68.726  1.00 35.67 ? 265 LEU   B CD1 1 
ATOM   2983 C  CD2 . LEU   B 1 172 ? 6.416   -6.402  69.578  1.00 38.03 ? 265 LEU   B CD2 1 
ATOM   2984 N  N   . GLY   B 1 173 ? 3.067   -7.593  65.544  1.00 35.48 ? 266 GLY   B N   1 
ATOM   2985 C  CA  . GLY   B 1 173 ? 1.813   -7.678  64.775  1.00 35.18 ? 266 GLY   B CA  1 
ATOM   2986 C  C   . GLY   B 1 173 ? 2.065   -7.842  63.291  1.00 34.13 ? 266 GLY   B C   1 
ATOM   2987 O  O   . GLY   B 1 173 ? 3.123   -7.405  62.809  1.00 35.97 ? 266 GLY   B O   1 
ATOM   2988 N  N   . ARG   B 1 174 ? 1.136   -8.470  62.574  1.00 33.93 ? 267 ARG   B N   1 
ATOM   2989 C  CA  . ARG   B 1 174 ? 1.240   -8.691  61.111  1.00 32.83 ? 267 ARG   B CA  1 
ATOM   2990 C  C   . ARG   B 1 174 ? -0.153  -8.664  60.477  1.00 31.81 ? 267 ARG   B C   1 
ATOM   2991 O  O   . ARG   B 1 174 ? -1.098  -9.234  61.051  1.00 31.98 ? 267 ARG   B O   1 
ATOM   2992 C  CB  . ARG   B 1 174 ? 1.941   -10.016 60.801  1.00 34.36 ? 267 ARG   B CB  1 
ATOM   2993 C  CG  . ARG   B 1 174 ? 2.229   -10.234 59.324  1.00 34.62 ? 267 ARG   B CG  1 
ATOM   2994 C  CD  . ARG   B 1 174 ? 2.577   -11.678 59.039  1.00 36.37 ? 267 ARG   B CD  1 
ATOM   2995 N  NE  . ARG   B 1 174 ? 3.805   -12.093 59.705  1.00 37.12 ? 267 ARG   B NE  1 
ATOM   2996 C  CZ  . ARG   B 1 174 ? 3.912   -13.029 60.646  1.00 38.87 ? 267 ARG   B CZ  1 
ATOM   2997 N  NH1 . ARG   B 1 174 ? 2.863   -13.704 61.083  1.00 40.00 ? 267 ARG   B NH1 1 
ATOM   2998 N  NH2 . ARG   B 1 174 ? 5.095   -13.309 61.165  1.00 39.38 ? 267 ARG   B NH2 1 
ATOM   2999 N  N   A ASN   B 1 175 ? -0.255  -8.002  59.323  0.40 31.02 ? 268 ASN   B N   1 
ATOM   3000 N  N   B ASN   B 1 175 ? -0.258  -7.998  59.325  0.60 31.04 ? 268 ASN   B N   1 
ATOM   3001 C  CA  A ASN   B 1 175 ? -1.439  -8.023  58.428  0.40 31.09 ? 268 ASN   B CA  1 
ATOM   3002 C  CA  B ASN   B 1 175 ? -1.434  -8.053  58.420  0.60 31.23 ? 268 ASN   B CA  1 
ATOM   3003 C  C   A ASN   B 1 175 ? -0.933  -8.079  56.983  0.40 30.64 ? 268 ASN   B C   1 
ATOM   3004 C  C   B ASN   B 1 175 ? -0.927  -8.091  56.978  0.60 30.66 ? 268 ASN   B C   1 
ATOM   3005 O  O   A ASN   B 1 175 ? 0.292   -7.988  56.778  0.40 31.03 ? 268 ASN   B O   1 
ATOM   3006 O  O   B ASN   B 1 175 ? 0.295   -7.990  56.776  0.60 31.33 ? 268 ASN   B O   1 
ATOM   3007 C  CB  A ASN   B 1 175 ? -2.355  -6.824  58.692  0.40 30.72 ? 268 ASN   B CB  1 
ATOM   3008 C  CB  B ASN   B 1 175 ? -2.397  -6.886  58.664  0.60 30.99 ? 268 ASN   B CB  1 
ATOM   3009 C  CG  A ASN   B 1 175 ? -3.144  -6.927  59.984  0.40 31.25 ? 268 ASN   B CG  1 
ATOM   3010 C  CG  B ASN   B 1 175 ? -3.847  -7.313  58.602  0.60 31.82 ? 268 ASN   B CG  1 
ATOM   3011 O  OD1 A ASN   B 1 175 ? -4.197  -7.552  60.010  0.40 32.36 ? 268 ASN   B OD1 1 
ATOM   3012 O  OD1 B ASN   B 1 175 ? -4.416  -7.443  57.516  0.60 32.17 ? 268 ASN   B OD1 1 
ATOM   3013 N  ND2 A ASN   B 1 175 ? -2.664  -6.311  61.057  0.40 31.38 ? 268 ASN   B ND2 1 
ATOM   3014 N  ND2 B ASN   B 1 175 ? -4.452  -7.531  59.754  0.60 32.75 ? 268 ASN   B ND2 1 
ATOM   3015 N  N   . SER   B 1 176 ? -1.839  -8.214  56.020  1.00 30.60 ? 269 SER   B N   1 
ATOM   3016 C  CA  . SER   B 1 176 ? -1.513  -8.355  54.584  1.00 30.90 ? 269 SER   B CA  1 
ATOM   3017 C  C   . SER   B 1 176 ? -2.709  -7.929  53.735  1.00 30.56 ? 269 SER   B C   1 
ATOM   3018 O  O   . SER   B 1 176 ? -3.824  -7.909  54.244  1.00 31.14 ? 269 SER   B O   1 
ATOM   3019 C  CB  . SER   B 1 176 ? -1.104  -9.782  54.270  1.00 31.80 ? 269 SER   B CB  1 
ATOM   3020 O  OG  . SER   B 1 176 ? -2.154  -10.661 54.589  1.00 32.78 ? 269 SER   B OG  1 
ATOM   3021 N  N   . PHE   B 1 177 ? -2.452  -7.573  52.485  1.00 31.61 ? 270 PHE   B N   1 
ATOM   3022 C  CA  . PHE   B 1 177 ? -3.464  -7.236  51.456  1.00 32.81 ? 270 PHE   B CA  1 
ATOM   3023 C  C   . PHE   B 1 177 ? -2.852  -7.504  50.080  1.00 33.64 ? 270 PHE   B C   1 
ATOM   3024 O  O   . PHE   B 1 177 ? -1.629  -7.312  49.910  1.00 35.29 ? 270 PHE   B O   1 
ATOM   3025 C  CB  . PHE   B 1 177 ? -3.933  -5.788  51.639  1.00 31.89 ? 270 PHE   B CB  1 
ATOM   3026 C  CG  . PHE   B 1 177 ? -2.832  -4.756  51.625  1.00 30.67 ? 270 PHE   B CG  1 
ATOM   3027 C  CD1 . PHE   B 1 177 ? -2.134  -4.447  52.784  1.00 30.41 ? 270 PHE   B CD1 1 
ATOM   3028 C  CD2 . PHE   B 1 177 ? -2.510  -4.075  50.455  1.00 31.07 ? 270 PHE   B CD2 1 
ATOM   3029 C  CE1 . PHE   B 1 177 ? -1.128  -3.496  52.778  1.00 29.80 ? 270 PHE   B CE1 1 
ATOM   3030 C  CE2 . PHE   B 1 177 ? -1.496  -3.128  50.446  1.00 29.97 ? 270 PHE   B CE2 1 
ATOM   3031 C  CZ  . PHE   B 1 177 ? -0.803  -2.851  51.601  1.00 29.86 ? 270 PHE   B CZ  1 
ATOM   3032 N  N   . GLU   B 1 178 ? -3.668  -7.970  49.144  1.00 34.00 ? 271 GLU   B N   1 
ATOM   3033 C  CA  . GLU   B 1 178 ? -3.289  -8.143  47.721  1.00 34.28 ? 271 GLU   B CA  1 
ATOM   3034 C  C   . GLU   B 1 178 ? -3.156  -6.741  47.122  1.00 33.85 ? 271 GLU   B C   1 
ATOM   3035 O  O   . GLU   B 1 178 ? -3.839  -5.820  47.613  1.00 32.51 ? 271 GLU   B O   1 
ATOM   3036 C  CB  . GLU   B 1 178 ? -4.327  -8.985  46.975  1.00 34.59 ? 271 GLU   B CB  1 
ATOM   3037 C  CG  . GLU   B 1 178 ? -3.873  -9.377  45.580  0.80 35.93 ? 271 GLU   B CG  1 
ATOM   3038 C  CD  . GLU   B 1 178 ? -4.728  -10.389 44.863  0.80 37.43 ? 271 GLU   B CD  1 
ATOM   3039 O  OE1 . GLU   B 1 178 ? -4.641  -10.457 43.628  0.80 38.30 ? 271 GLU   B OE1 1 
ATOM   3040 O  OE2 . GLU   B 1 178 ? -5.474  -11.102 45.547  0.80 37.92 ? 271 GLU   B OE2 1 
ATOM   3041 N  N   . VAL   B 1 179 ? -2.272  -6.589  46.136  1.00 34.57 ? 272 VAL   B N   1 
ATOM   3042 C  CA  . VAL   B 1 179 ? -2.033  -5.308  45.407  1.00 35.76 ? 272 VAL   B CA  1 
ATOM   3043 C  C   . VAL   B 1 179 ? -2.074  -5.581  43.898  1.00 37.81 ? 272 VAL   B C   1 
ATOM   3044 O  O   . VAL   B 1 179 ? -1.504  -6.589  43.444  1.00 39.01 ? 272 VAL   B O   1 
ATOM   3045 C  CB  . VAL   B 1 179 ? -0.705  -4.657  45.843  1.00 34.88 ? 272 VAL   B CB  1 
ATOM   3046 C  CG1 . VAL   B 1 179 ? -0.384  -3.411  45.034  1.00 34.82 ? 272 VAL   B CG1 1 
ATOM   3047 C  CG2 . VAL   B 1 179 ? -0.694  -4.341  47.328  1.00 33.95 ? 272 VAL   B CG2 1 
ATOM   3048 N  N   . ARG   B 1 180 ? -2.763  -4.721  43.156  1.00 38.91 ? 273 ARG   B N   1 
ATOM   3049 C  CA  . ARG   B 1 180 ? -2.638  -4.603  41.689  1.00 40.50 ? 273 ARG   B CA  1 
ATOM   3050 C  C   . ARG   B 1 180 ? -2.181  -3.180  41.384  1.00 39.60 ? 273 ARG   B C   1 
ATOM   3051 O  O   . ARG   B 1 180 ? -2.858  -2.239  41.843  1.00 38.65 ? 273 ARG   B O   1 
ATOM   3052 C  CB  . ARG   B 1 180 ? -3.981  -4.889  41.023  1.00 43.20 ? 273 ARG   B CB  1 
ATOM   3053 C  CG  . ARG   B 1 180 ? -3.978  -4.591  39.538  1.00 45.54 ? 273 ARG   B CG  1 
ATOM   3054 C  CD  . ARG   B 1 180 ? -4.979  -5.464  38.826  1.00 48.12 ? 273 ARG   B CD  1 
ATOM   3055 N  NE  . ARG   B 1 180 ? -5.400  -4.951  37.536  1.00 50.36 ? 273 ARG   B NE  1 
ATOM   3056 C  CZ  . ARG   B 1 180 ? -4.815  -5.215  36.367  1.00 52.72 ? 273 ARG   B CZ  1 
ATOM   3057 N  NH1 . ARG   B 1 180 ? -3.709  -5.944  36.316  1.00 53.61 ? 273 ARG   B NH1 1 
ATOM   3058 N  NH2 . ARG   B 1 180 ? -5.320  -4.705  35.254  1.00 53.21 ? 273 ARG   B NH2 1 
ATOM   3059 N  N   . VAL   B 1 181 ? -1.051  -3.032  40.695  1.00 39.85 ? 274 VAL   B N   1 
ATOM   3060 C  CA  . VAL   B 1 181 ? -0.572  -1.706  40.215  1.00 40.15 ? 274 VAL   B CA  1 
ATOM   3061 C  C   . VAL   B 1 181 ? -1.010  -1.598  38.758  1.00 41.95 ? 274 VAL   B C   1 
ATOM   3062 O  O   . VAL   B 1 181 ? -0.583  -2.450  37.965  1.00 42.21 ? 274 VAL   B O   1 
ATOM   3063 C  CB  . VAL   B 1 181 ? 0.948   -1.536  40.409  1.00 39.41 ? 274 VAL   B CB  1 
ATOM   3064 C  CG1 . VAL   B 1 181 ? 1.360   -0.085  40.240  1.00 39.19 ? 274 VAL   B CG1 1 
ATOM   3065 C  CG2 . VAL   B 1 181 ? 1.411   -2.082  41.755  1.00 38.39 ? 274 VAL   B CG2 1 
ATOM   3066 N  N   . CYS   B 1 182 ? -1.884  -0.640  38.435  1.00 43.23 ? 275 CYS   B N   1 
ATOM   3067 C  CA  . CYS   B 1 182 ? -2.563  -0.555  37.114  1.00 45.68 ? 275 CYS   B CA  1 
ATOM   3068 C  C   . CYS   B 1 182 ? -2.877  0.900   36.764  1.00 46.23 ? 275 CYS   B C   1 
ATOM   3069 O  O   . CYS   B 1 182 ? -2.799  1.742   37.653  1.00 46.32 ? 275 CYS   B O   1 
ATOM   3070 C  CB  . CYS   B 1 182 ? -3.828  -1.404  37.083  1.00 46.95 ? 275 CYS   B CB  1 
ATOM   3071 S  SG  . CYS   B 1 182 ? -4.974  -1.103  38.456  1.00 47.90 ? 275 CYS   B SG  1 
ATOM   3072 N  N   . ALA   B 1 183 ? -3.182  1.159   35.493  1.00 48.24 ? 276 ALA   B N   1 
ATOM   3073 C  CA  . ALA   B 1 183 ? -3.421  2.507   34.924  1.00 49.14 ? 276 ALA   B CA  1 
ATOM   3074 C  C   . ALA   B 1 183 ? -4.726  3.088   35.474  1.00 48.81 ? 276 ALA   B C   1 
ATOM   3075 O  O   . ALA   B 1 183 ? -4.766  4.293   35.764  1.00 47.72 ? 276 ALA   B O   1 
ATOM   3076 C  CB  . ALA   B 1 183 ? -3.450  2.430   33.414  1.00 51.43 ? 276 ALA   B CB  1 
ATOM   3077 N  N   A CYS   B 1 184 ? -5.754  2.248   35.617  0.80 49.63 ? 277 CYS   B N   1 
ATOM   3078 N  N   B CYS   B 1 184 ? -5.757  2.252   35.614  0.20 48.87 ? 277 CYS   B N   1 
ATOM   3079 C  CA  A CYS   B 1 184 ? -7.138  2.662   35.988  0.80 50.65 ? 277 CYS   B CA  1 
ATOM   3080 C  CA  B CYS   B 1 184 ? -7.141  2.661   35.979  0.20 49.25 ? 277 CYS   B CA  1 
ATOM   3081 C  C   A CYS   B 1 184 ? -7.634  1.813   37.153  0.80 48.75 ? 277 CYS   B C   1 
ATOM   3082 C  C   B CYS   B 1 184 ? -7.636  1.816   37.153  0.20 47.85 ? 277 CYS   B C   1 
ATOM   3083 O  O   A CYS   B 1 184 ? -8.396  0.867   36.961  0.80 49.94 ? 277 CYS   B O   1 
ATOM   3084 O  O   B CYS   B 1 184 ? -8.395  0.865   36.967  0.20 48.53 ? 277 CYS   B O   1 
ATOM   3085 C  CB  A CYS   B 1 184 ? -8.088  2.596   34.797  0.80 53.77 ? 277 CYS   B CB  1 
ATOM   3086 C  CB  B CYS   B 1 184 ? -8.077  2.539   34.782  0.20 51.35 ? 277 CYS   B CB  1 
ATOM   3087 S  SG  A CYS   B 1 184 ? -8.206  4.184   33.930  0.80 57.77 ? 277 CYS   B SG  1 
ATOM   3088 S  SG  B CYS   B 1 184 ? -7.670  3.655   33.412  0.20 53.67 ? 277 CYS   B SG  1 
ATOM   3089 N  N   . PRO   B 1 185 ? -7.230  2.151   38.401  1.00 46.24 ? 278 PRO   B N   1 
ATOM   3090 C  CA  . PRO   B 1 185 ? -7.633  1.389   39.583  1.00 44.71 ? 278 PRO   B CA  1 
ATOM   3091 C  C   . PRO   B 1 185 ? -9.152  1.314   39.802  1.00 44.67 ? 278 PRO   B C   1 
ATOM   3092 O  O   . PRO   B 1 185 ? -9.652  0.233   40.109  1.00 43.50 ? 278 PRO   B O   1 
ATOM   3093 C  CB  . PRO   B 1 185 ? -6.998  2.162   40.750  1.00 44.21 ? 278 PRO   B CB  1 
ATOM   3094 C  CG  . PRO   B 1 185 ? -5.895  2.988   40.131  1.00 44.35 ? 278 PRO   B CG  1 
ATOM   3095 C  CD  . PRO   B 1 185 ? -6.371  3.294   38.734  1.00 45.75 ? 278 PRO   B CD  1 
ATOM   3096 N  N   . GLY   B 1 186 ? -9.847  2.449   39.634  1.00 44.83 ? 279 GLY   B N   1 
ATOM   3097 C  CA  . GLY   B 1 186 ? -11.322 2.535   39.732  1.00 45.32 ? 279 GLY   B CA  1 
ATOM   3098 C  C   . GLY   B 1 186 ? -11.983 1.507   38.830  1.00 46.54 ? 279 GLY   B C   1 
ATOM   3099 O  O   . GLY   B 1 186 ? -12.780 0.687   39.345  1.00 46.42 ? 279 GLY   B O   1 
ATOM   3100 N  N   . ARG   B 1 187 ? -11.639 1.520   37.536  1.00 47.30 ? 280 ARG   B N   1 
ATOM   3101 C  CA  . ARG   B 1 187 ? -12.234 0.625   36.513  1.00 48.68 ? 280 ARG   B CA  1 
ATOM   3102 C  C   . ARG   B 1 187 ? -11.884 -0.827  36.855  1.00 47.10 ? 280 ARG   B C   1 
ATOM   3103 O  O   . ARG   B 1 187 ? -12.782 -1.679  36.793  1.00 47.84 ? 280 ARG   B O   1 
ATOM   3104 C  CB  . ARG   B 1 187 ? -11.756 0.990   35.101  1.00 50.60 ? 280 ARG   B CB  1 
ATOM   3105 C  CG  . ARG   B 1 187 ? -12.088 2.415   34.677  1.00 52.37 ? 280 ARG   B CG  1 
ATOM   3106 C  CD  . ARG   B 1 187 ? -11.508 2.782   33.323  1.00 54.63 ? 280 ARG   B CD  1 
ATOM   3107 N  NE  . ARG   B 1 187 ? -11.684 4.207   33.052  1.00 56.45 ? 280 ARG   B NE  1 
ATOM   3108 C  CZ  . ARG   B 1 187 ? -11.127 4.888   32.051  1.00 58.00 ? 280 ARG   B CZ  1 
ATOM   3109 N  NH1 . ARG   B 1 187 ? -10.330 4.290   31.179  1.00 58.84 ? 280 ARG   B NH1 1 
ATOM   3110 N  NH2 . ARG   B 1 187 ? -11.381 6.182   31.923  1.00 58.91 ? 280 ARG   B NH2 1 
ATOM   3111 N  N   . ASP   B 1 188 ? -10.627 -1.094  37.196  1.00 45.62 ? 281 ASP   B N   1 
ATOM   3112 C  CA  . ASP   B 1 188 ? -10.131 -2.472  37.448  1.00 44.75 ? 281 ASP   B CA  1 
ATOM   3113 C  C   . ASP   B 1 188 ? -10.775 -3.035  38.727  1.00 42.68 ? 281 ASP   B C   1 
ATOM   3114 O  O   . ASP   B 1 188 ? -11.139 -4.229  38.719  1.00 42.61 ? 281 ASP   B O   1 
ATOM   3115 C  CB  . ASP   B 1 188 ? -8.603  -2.497  37.458  1.00 44.77 ? 281 ASP   B CB  1 
ATOM   3116 C  CG  . ASP   B 1 188 ? -7.968  -2.214  36.109  1.00 46.63 ? 281 ASP   B CG  1 
ATOM   3117 O  OD1 . ASP   B 1 188 ? -8.705  -2.116  35.102  1.00 48.61 ? 281 ASP   B OD1 1 
ATOM   3118 O  OD2 . ASP   B 1 188 ? -6.738  -2.111  36.073  1.00 48.65 ? 281 ASP   B OD2 1 
ATOM   3119 N  N   . ARG   B 1 189 ? -10.943 -2.224  39.777  1.00 40.66 ? 282 ARG   B N   1 
ATOM   3120 C  CA  . ARG   B 1 189 ? -11.657 -2.671  41.005  1.00 39.83 ? 282 ARG   B CA  1 
ATOM   3121 C  C   . ARG   B 1 189 ? -13.102 -3.048  40.635  1.00 41.44 ? 282 ARG   B C   1 
ATOM   3122 O  O   . ARG   B 1 189 ? -13.534 -4.160  41.003  1.00 42.34 ? 282 ARG   B O   1 
ATOM   3123 C  CB  . ARG   B 1 189 ? -11.645 -1.617  42.117  1.00 37.48 ? 282 ARG   B CB  1 
ATOM   3124 C  CG  . ARG   B 1 189 ? -12.465 -2.045  43.331  1.00 36.53 ? 282 ARG   B CG  1 
ATOM   3125 C  CD  . ARG   B 1 189 ? -12.328 -1.144  44.531  1.00 34.79 ? 282 ARG   B CD  1 
ATOM   3126 N  NE  . ARG   B 1 189 ? -13.432 -1.374  45.443  1.00 34.12 ? 282 ARG   B NE  1 
ATOM   3127 C  CZ  . ARG   B 1 189 ? -13.907 -0.502  46.314  1.00 33.57 ? 282 ARG   B CZ  1 
ATOM   3128 N  NH1 . ARG   B 1 189 ? -13.352 0.686   46.434  1.00 32.69 ? 282 ARG   B NH1 1 
ATOM   3129 N  NH2 . ARG   B 1 189 ? -14.943 -0.819  47.065  1.00 34.02 ? 282 ARG   B NH2 1 
ATOM   3130 N  N   . ARG   B 1 190 ? -13.824 -2.162  39.937  1.00 43.17 ? 283 ARG   B N   1 
ATOM   3131 C  CA  . ARG   B 1 190 ? -15.249 -2.367  39.559  1.00 45.37 ? 283 ARG   B CA  1 
ATOM   3132 C  C   . ARG   B 1 190 ? -15.378 -3.675  38.767  1.00 47.65 ? 283 ARG   B C   1 
ATOM   3133 O  O   . ARG   B 1 190 ? -16.272 -4.507  39.086  1.00 48.37 ? 283 ARG   B O   1 
ATOM   3134 C  CB  . ARG   B 1 190 ? -15.763 -1.197  38.718  1.00 46.35 ? 283 ARG   B CB  1 
ATOM   3135 C  CG  . ARG   B 1 190 ? -17.124 -0.689  39.164  1.00 46.96 ? 283 ARG   B CG  1 
ATOM   3136 C  CD  . ARG   B 1 190 ? -17.683 0.420   38.301  1.00 48.04 ? 283 ARG   B CD  1 
ATOM   3137 N  NE  . ARG   B 1 190 ? -17.331 1.737   38.806  1.00 47.15 ? 283 ARG   B NE  1 
ATOM   3138 C  CZ  . ARG   B 1 190 ? -17.806 2.879   38.333  1.00 48.24 ? 283 ARG   B CZ  1 
ATOM   3139 N  NH1 . ARG   B 1 190 ? -17.425 4.027   38.868  1.00 47.87 ? 283 ARG   B NH1 1 
ATOM   3140 N  NH2 . ARG   B 1 190 ? -18.684 2.876   37.347  1.00 50.25 ? 283 ARG   B NH2 1 
ATOM   3141 N  N   . THR   B 1 191 ? -14.509 -3.849  37.768  1.00 48.45 ? 284 THR   B N   1 
ATOM   3142 C  CA  . THR   B 1 191 ? -14.493 -5.028  36.867  1.00 50.36 ? 284 THR   B CA  1 
ATOM   3143 C  C   . THR   B 1 191 ? -14.263 -6.296  37.695  1.00 50.63 ? 284 THR   B C   1 
ATOM   3144 O  O   . THR   B 1 191 ? -15.035 -7.243  37.530  1.00 50.27 ? 284 THR   B O   1 
ATOM   3145 C  CB  . THR   B 1 191 ? -13.473 -4.814  35.743  1.00 50.56 ? 284 THR   B CB  1 
ATOM   3146 O  OG1 . THR   B 1 191 ? -13.839 -3.588  35.106  1.00 50.69 ? 284 THR   B OG1 1 
ATOM   3147 C  CG2 . THR   B 1 191 ? -13.448 -5.932  34.727  1.00 52.06 ? 284 THR   B CG2 1 
ATOM   3148 N  N   . GLU   B 1 192 ? -13.260 -6.294  38.578  1.00 51.28 ? 285 GLU   B N   1 
ATOM   3149 C  CA  . GLU   B 1 192 ? -12.870 -7.489  39.375  1.00 52.27 ? 285 GLU   B CA  1 
ATOM   3150 C  C   . GLU   B 1 192 ? -13.977 -7.849  40.379  1.00 54.00 ? 285 GLU   B C   1 
ATOM   3151 O  O   . GLU   B 1 192 ? -14.179 -9.060  40.618  1.00 55.46 ? 285 GLU   B O   1 
ATOM   3152 C  CB  . GLU   B 1 192 ? -11.533 -7.270  40.083  1.00 51.30 ? 285 GLU   B CB  1 
ATOM   3153 C  CG  . GLU   B 1 192 ? -10.964 -8.559  40.631  1.00 51.62 ? 285 GLU   B CG  1 
ATOM   3154 C  CD  . GLU   B 1 192 ? -9.469  -8.540  40.865  1.00 50.63 ? 285 GLU   B CD  1 
ATOM   3155 O  OE1 . GLU   B 1 192 ? -9.024  -9.179  41.831  1.00 49.47 ? 285 GLU   B OE1 1 
ATOM   3156 O  OE2 . GLU   B 1 192 ? -8.753  -7.952  40.031  1.00 51.99 ? 285 GLU   B OE2 1 
ATOM   3157 N  N   . GLU   B 1 193 ? -14.692 -6.856  40.921  1.00 54.73 ? 286 GLU   B N   1 
ATOM   3158 C  CA  . GLU   B 1 193 ? -15.784 -7.084  41.911  1.00 55.99 ? 286 GLU   B CA  1 
ATOM   3159 C  C   . GLU   B 1 193 ? -17.020 -7.678  41.224  1.00 59.35 ? 286 GLU   B C   1 
ATOM   3160 O  O   . GLU   B 1 193 ? -17.727 -8.444  41.887  1.00 59.96 ? 286 GLU   B O   1 
ATOM   3161 C  CB  . GLU   B 1 193 ? -16.095 -5.798  42.683  1.00 54.70 ? 286 GLU   B CB  1 
ATOM   3162 C  CG  . GLU   B 1 193 ? -15.135 -5.572  43.845  1.00 53.21 ? 286 GLU   B CG  1 
ATOM   3163 C  CD  . GLU   B 1 193 ? -15.221 -4.219  44.530  1.00 52.78 ? 286 GLU   B CD  1 
ATOM   3164 O  OE1 . GLU   B 1 193 ? -16.016 -3.363  44.064  1.00 53.73 ? 286 GLU   B OE1 1 
ATOM   3165 O  OE2 . GLU   B 1 193 ? -14.481 -4.016  45.524  1.00 50.37 ? 286 GLU   B OE2 1 
ATOM   3166 N  N   . GLU   B 1 194 ? -17.270 -7.349  39.952  1.00 62.41 ? 287 GLU   B N   1 
ATOM   3167 C  CA  . GLU   B 1 194 ? -18.388 -7.894  39.137  1.00 66.34 ? 287 GLU   B CA  1 
ATOM   3168 C  C   . GLU   B 1 194 ? -18.381 -9.428  39.134  1.00 68.61 ? 287 GLU   B C   1 
ATOM   3169 O  O   . GLU   B 1 194 ? -19.470 -10.002 38.946  1.00 70.68 ? 287 GLU   B O   1 
ATOM   3170 C  CB  . GLU   B 1 194 ? -18.281 -7.365  37.700  1.00 68.12 ? 287 GLU   B CB  1 
ATOM   3171 C  CG  . GLU   B 1 194 ? -19.067 -6.095  37.450  1.00 69.32 ? 287 GLU   B CG  1 
ATOM   3172 C  CD  . GLU   B 1 194 ? -18.569 -5.194  36.332  1.00 71.12 ? 287 GLU   B CD  1 
ATOM   3173 O  OE1 . GLU   B 1 194 ? -17.987 -5.733  35.361  1.00 73.35 ? 287 GLU   B OE1 1 
ATOM   3174 O  OE2 . GLU   B 1 194 ? -18.758 -3.958  36.444  1.00 71.61 ? 287 GLU   B OE2 1 
ATOM   3175 N  N   . ASN   B 1 195 ? -17.215 -10.060 39.324  1.00 69.63 ? 288 ASN   B N   1 
ATOM   3176 C  CA  . ASN   B 1 195 ? -17.109 -11.523 39.579  1.00 71.80 ? 288 ASN   B CA  1 
ATOM   3177 C  C   . ASN   B 1 195 ? -17.331 -11.799 41.068  1.00 71.74 ? 288 ASN   B C   1 
ATOM   3178 O  O   . ASN   B 1 195 ? -18.147 -11.156 41.720  1.00 72.46 ? 288 ASN   B O   1 
ATOM   3179 C  CB  . ASN   B 1 195 ? -15.776 -12.110 39.116  1.00 72.28 ? 288 ASN   B CB  1 
ATOM   3180 C  CG  . ASN   B 1 195 ? -15.704 -12.219 37.609  1.00 74.62 ? 288 ASN   B CG  1 
ATOM   3181 O  OD1 . ASN   B 1 195 ? -16.208 -11.347 36.908  1.00 76.77 ? 288 ASN   B OD1 1 
ATOM   3182 N  ND2 . ASN   B 1 195 ? -15.099 -13.284 37.101  1.00 75.87 ? 288 ASN   B ND2 1 
ATOM   3183 N  N   . SER   C 1 3   ? -21.433 21.432  50.351  1.00 61.49 ? 96  SER   C N   1 
ATOM   3184 C  CA  . SER   C 1 3   ? -22.133 22.216  51.418  1.00 62.34 ? 96  SER   C CA  1 
ATOM   3185 C  C   . SER   C 1 3   ? -23.381 21.450  51.877  1.00 60.77 ? 96  SER   C C   1 
ATOM   3186 O  O   . SER   C 1 3   ? -23.400 21.035  53.057  1.00 60.39 ? 96  SER   C O   1 
ATOM   3187 C  CB  . SER   C 1 3   ? -22.469 23.614  50.951  1.00 64.63 ? 96  SER   C CB  1 
ATOM   3188 O  OG  . SER   C 1 3   ? -23.448 23.582  49.922  1.00 64.80 ? 96  SER   C OG  1 
ATOM   3189 N  N   . VAL   C 1 4   ? -24.386 21.297  50.994  1.00 59.89 ? 97  VAL   C N   1 
ATOM   3190 C  CA  . VAL   C 1 4   ? -25.501 20.312  51.144  1.00 57.18 ? 97  VAL   C CA  1 
ATOM   3191 C  C   . VAL   C 1 4   ? -25.821 19.673  49.792  1.00 56.12 ? 97  VAL   C C   1 
ATOM   3192 O  O   . VAL   C 1 4   ? -26.038 20.373  48.807  1.00 58.28 ? 97  VAL   C O   1 
ATOM   3193 C  CB  . VAL   C 1 4   ? -26.755 20.951  51.771  1.00 58.50 ? 97  VAL   C CB  1 
ATOM   3194 C  CG1 . VAL   C 1 4   ? -27.918 19.973  51.842  1.00 56.36 ? 97  VAL   C CG1 1 
ATOM   3195 C  CG2 . VAL   C 1 4   ? -26.453 21.515  53.156  1.00 59.60 ? 97  VAL   C CG2 1 
ATOM   3196 N  N   . PRO   C 1 5   ? -25.867 18.321  49.699  1.00 52.69 ? 98  PRO   C N   1 
ATOM   3197 C  CA  . PRO   C 1 5   ? -26.310 17.655  48.475  1.00 50.92 ? 98  PRO   C CA  1 
ATOM   3198 C  C   . PRO   C 1 5   ? -27.807 17.880  48.221  1.00 49.97 ? 98  PRO   C C   1 
ATOM   3199 O  O   . PRO   C 1 5   ? -28.581 17.932  49.157  1.00 48.72 ? 98  PRO   C O   1 
ATOM   3200 C  CB  . PRO   C 1 5   ? -26.016 16.163  48.686  1.00 49.42 ? 98  PRO   C CB  1 
ATOM   3201 C  CG  . PRO   C 1 5   ? -25.787 16.007  50.180  1.00 49.55 ? 98  PRO   C CG  1 
ATOM   3202 C  CD  . PRO   C 1 5   ? -25.485 17.373  50.751  1.00 50.69 ? 98  PRO   C CD  1 
ATOM   3203 N  N   . SER   C 1 6   ? -28.177 17.986  46.947  1.00 50.62 ? 99  SER   C N   1 
ATOM   3204 C  CA  . SER   C 1 6   ? -29.566 18.226  46.479  1.00 51.01 ? 99  SER   C CA  1 
ATOM   3205 C  C   . SER   C 1 6   ? -30.463 17.055  46.903  1.00 48.89 ? 99  SER   C C   1 
ATOM   3206 O  O   . SER   C 1 6   ? -30.021 15.903  46.813  1.00 47.08 ? 99  SER   C O   1 
ATOM   3207 C  CB  . SER   C 1 6   ? -29.598 18.440  44.996  1.00 52.76 ? 99  SER   C CB  1 
ATOM   3208 O  OG  . SER   C 1 6   ? -30.935 18.452  44.522  1.00 54.52 ? 99  SER   C OG  1 
ATOM   3209 N  N   . GLN   C 1 7   ? -31.683 17.360  47.340  1.00 48.35 ? 100 GLN   C N   1 
ATOM   3210 C  CA  . GLN   C 1 7   ? -32.725 16.373  47.704  1.00 47.03 ? 100 GLN   C CA  1 
ATOM   3211 C  C   . GLN   C 1 7   ? -33.915 16.507  46.744  1.00 48.09 ? 100 GLN   C C   1 
ATOM   3212 O  O   . GLN   C 1 7   ? -34.902 15.801  46.962  1.00 47.40 ? 100 GLN   C O   1 
ATOM   3213 C  CB  . GLN   C 1 7   ? -33.115 16.592  49.170  1.00 46.53 ? 100 GLN   C CB  1 
ATOM   3214 C  CG  . GLN   C 1 7   ? -33.910 17.862  49.441  1.00 47.99 ? 100 GLN   C CG  1 
ATOM   3215 C  CD  . GLN   C 1 7   ? -33.651 18.437  50.815  1.00 48.31 ? 100 GLN   C CD  1 
ATOM   3216 O  OE1 . GLN   C 1 7   ? -32.622 19.068  51.055  1.00 48.58 ? 100 GLN   C OE1 1 
ATOM   3217 N  NE2 . GLN   C 1 7   ? -34.585 18.221  51.727  1.00 48.02 ? 100 GLN   C NE2 1 
ATOM   3218 N  N   . LYS   C 1 8   ? -33.808 17.355  45.712  1.00 49.74 ? 101 LYS   C N   1 
ATOM   3219 C  CA  . LYS   C 1 8   ? -34.916 17.662  44.764  1.00 51.07 ? 101 LYS   C CA  1 
ATOM   3220 C  C   . LYS   C 1 8   ? -35.235 16.402  43.948  1.00 49.87 ? 101 LYS   C C   1 
ATOM   3221 O  O   . LYS   C 1 8   ? -34.316 15.850  43.326  1.00 49.02 ? 101 LYS   C O   1 
ATOM   3222 C  CB  . LYS   C 1 8   ? -34.525 18.848  43.872  1.00 53.54 ? 101 LYS   C CB  1 
ATOM   3223 C  CG  . LYS   C 1 8   ? -35.583 19.312  42.877  1.00 55.42 ? 101 LYS   C CG  1 
ATOM   3224 C  CD  . LYS   C 1 8   ? -35.443 20.758  42.456  1.00 58.29 ? 101 LYS   C CD  1 
ATOM   3225 C  CE  . LYS   C 1 8   ? -34.035 21.120  42.020  1.00 59.49 ? 101 LYS   C CE  1 
ATOM   3226 N  NZ  . LYS   C 1 8   ? -33.609 20.367  40.815  1.00 59.34 ? 101 LYS   C NZ  1 
ATOM   3227 N  N   . THR   C 1 9   ? -36.495 15.962  43.956  1.00 49.21 ? 102 THR   C N   1 
ATOM   3228 C  CA  . THR   C 1 9   ? -36.972 14.784  43.189  1.00 48.19 ? 102 THR   C CA  1 
ATOM   3229 C  C   . THR   C 1 9   ? -36.773 15.047  41.696  1.00 49.73 ? 102 THR   C C   1 
ATOM   3230 O  O   . THR   C 1 9   ? -36.984 16.196  41.247  1.00 51.62 ? 102 THR   C O   1 
ATOM   3231 C  CB  . THR   C 1 9   ? -38.439 14.473  43.495  1.00 48.38 ? 102 THR   C CB  1 
ATOM   3232 O  OG1 . THR   C 1 9   ? -38.514 14.241  44.899  1.00 47.59 ? 102 THR   C OG1 1 
ATOM   3233 C  CG2 . THR   C 1 9   ? -38.964 13.272  42.741  1.00 48.06 ? 102 THR   C CG2 1 
ATOM   3234 N  N   . TYR   C 1 10  ? -36.384 14.009  40.960  1.00 48.34 ? 103 TYR   C N   1 
ATOM   3235 C  CA  . TYR   C 1 10  ? -36.034 14.064  39.520  1.00 49.40 ? 103 TYR   C CA  1 
ATOM   3236 C  C   . TYR   C 1 10  ? -36.230 12.669  38.933  1.00 48.29 ? 103 TYR   C C   1 
ATOM   3237 O  O   . TYR   C 1 10  ? -35.333 11.829  39.090  1.00 46.13 ? 103 TYR   C O   1 
ATOM   3238 C  CB  . TYR   C 1 10  ? -34.587 14.530  39.351  1.00 49.69 ? 103 TYR   C CB  1 
ATOM   3239 C  CG  . TYR   C 1 10  ? -34.050 14.485  37.942  1.00 51.69 ? 103 TYR   C CG  1 
ATOM   3240 C  CD1 . TYR   C 1 10  ? -34.716 15.108  36.899  1.00 54.05 ? 103 TYR   C CD1 1 
ATOM   3241 C  CD2 . TYR   C 1 10  ? -32.853 13.843  37.657  1.00 51.09 ? 103 TYR   C CD2 1 
ATOM   3242 C  CE1 . TYR   C 1 10  ? -34.221 15.075  35.604  1.00 55.37 ? 103 TYR   C CE1 1 
ATOM   3243 C  CE2 . TYR   C 1 10  ? -32.347 13.795  36.371  1.00 52.22 ? 103 TYR   C CE2 1 
ATOM   3244 C  CZ  . TYR   C 1 10  ? -33.029 14.420  35.342  1.00 54.69 ? 103 TYR   C CZ  1 
ATOM   3245 O  OH  . TYR   C 1 10  ? -32.526 14.377  34.076  1.00 55.93 ? 103 TYR   C OH  1 
ATOM   3246 N  N   . GLN   C 1 11  ? -37.362 12.431  38.274  1.00 49.24 ? 104 GLN   C N   1 
ATOM   3247 C  CA  . GLN   C 1 11  ? -37.656 11.127  37.619  1.00 48.91 ? 104 GLN   C CA  1 
ATOM   3248 C  C   . GLN   C 1 11  ? -36.721 10.984  36.413  1.00 50.01 ? 104 GLN   C C   1 
ATOM   3249 O  O   . GLN   C 1 11  ? -36.280 9.850   36.118  1.00 48.61 ? 104 GLN   C O   1 
ATOM   3250 C  CB  . GLN   C 1 11  ? -39.142 11.026  37.278  1.00 50.04 ? 104 GLN   C CB  1 
ATOM   3251 C  CG  . GLN   C 1 11  ? -40.009 11.018  38.535  1.00 49.41 ? 104 GLN   C CG  1 
ATOM   3252 C  CD  . GLN   C 1 11  ? -41.490 10.956  38.283  1.00 50.55 ? 104 GLN   C CD  1 
ATOM   3253 O  OE1 . GLN   C 1 11  ? -41.977 11.261  37.196  1.00 53.06 ? 104 GLN   C OE1 1 
ATOM   3254 N  NE2 . GLN   C 1 11  ? -42.223 10.595  39.319  1.00 49.80 ? 104 GLN   C NE2 1 
ATOM   3255 N  N   . GLY   C 1 12  ? -36.401 12.107  35.767  1.00 51.35 ? 105 GLY   C N   1 
ATOM   3256 C  CA  . GLY   C 1 12  ? -35.442 12.171  34.653  1.00 52.76 ? 105 GLY   C CA  1 
ATOM   3257 C  C   . GLY   C 1 12  ? -35.875 11.301  33.491  1.00 54.13 ? 105 GLY   C C   1 
ATOM   3258 O  O   . GLY   C 1 12  ? -37.098 11.001  33.357  1.00 55.52 ? 105 GLY   C O   1 
ATOM   3259 N  N   . SER   C 1 13  ? -34.894 10.864  32.707  1.00 53.64 ? 106 SER   C N   1 
ATOM   3260 C  CA  . SER   C 1 13  ? -35.068 10.326  31.335  1.00 55.65 ? 106 SER   C CA  1 
ATOM   3261 C  C   . SER   C 1 13  ? -35.739 8.947   31.381  1.00 54.56 ? 106 SER   C C   1 
ATOM   3262 O  O   . SER   C 1 13  ? -36.465 8.622   30.431  1.00 54.87 ? 106 SER   C O   1 
ATOM   3263 C  CB  . SER   C 1 13  ? -33.738 10.304  30.620  1.00 56.25 ? 106 SER   C CB  1 
ATOM   3264 O  OG  . SER   C 1 13  ? -33.863 9.743   29.326  1.00 58.54 ? 106 SER   C OG  1 
ATOM   3265 N  N   . TYR   C 1 14  ? -35.523 8.179   32.454  1.00 52.39 ? 107 TYR   C N   1 
ATOM   3266 C  CA  . TYR   C 1 14  ? -35.928 6.749   32.562  1.00 51.92 ? 107 TYR   C CA  1 
ATOM   3267 C  C   . TYR   C 1 14  ? -37.163 6.584   33.463  1.00 50.79 ? 107 TYR   C C   1 
ATOM   3268 O  O   . TYR   C 1 14  ? -37.542 5.428   33.719  1.00 50.14 ? 107 TYR   C O   1 
ATOM   3269 C  CB  . TYR   C 1 14  ? -34.737 5.924   33.049  1.00 51.01 ? 107 TYR   C CB  1 
ATOM   3270 C  CG  . TYR   C 1 14  ? -33.580 5.943   32.087  1.00 52.34 ? 107 TYR   C CG  1 
ATOM   3271 C  CD1 . TYR   C 1 14  ? -33.592 5.137   30.967  1.00 53.98 ? 107 TYR   C CD1 1 
ATOM   3272 C  CD2 . TYR   C 1 14  ? -32.496 6.788   32.270  1.00 52.24 ? 107 TYR   C CD2 1 
ATOM   3273 C  CE1 . TYR   C 1 14  ? -32.546 5.141   30.061  1.00 55.31 ? 107 TYR   C CE1 1 
ATOM   3274 C  CE2 . TYR   C 1 14  ? -31.444 6.815   31.369  1.00 53.44 ? 107 TYR   C CE2 1 
ATOM   3275 C  CZ  . TYR   C 1 14  ? -31.474 5.992   30.258  1.00 54.70 ? 107 TYR   C CZ  1 
ATOM   3276 O  OH  . TYR   C 1 14  ? -30.452 6.002   29.361  1.00 56.11 ? 107 TYR   C OH  1 
ATOM   3277 N  N   . GLY   C 1 15  ? -37.794 7.684   33.883  1.00 50.64 ? 108 GLY   C N   1 
ATOM   3278 C  CA  . GLY   C 1 15  ? -39.012 7.671   34.717  1.00 49.84 ? 108 GLY   C CA  1 
ATOM   3279 C  C   . GLY   C 1 15  ? -38.775 6.964   36.043  1.00 47.63 ? 108 GLY   C C   1 
ATOM   3280 O  O   . GLY   C 1 15  ? -39.526 6.018   36.361  1.00 47.21 ? 108 GLY   C O   1 
ATOM   3281 N  N   . PHE   C 1 16  ? -37.766 7.412   36.792  1.00 46.63 ? 109 PHE   C N   1 
ATOM   3282 C  CA  . PHE   C 1 16  ? -37.246 6.755   38.022  1.00 44.34 ? 109 PHE   C CA  1 
ATOM   3283 C  C   . PHE   C 1 16  ? -38.082 7.176   39.235  1.00 42.77 ? 109 PHE   C C   1 
ATOM   3284 O  O   . PHE   C 1 16  ? -38.143 8.380   39.535  1.00 43.83 ? 109 PHE   C O   1 
ATOM   3285 C  CB  . PHE   C 1 16  ? -35.758 7.070   38.190  1.00 43.84 ? 109 PHE   C CB  1 
ATOM   3286 C  CG  . PHE   C 1 16  ? -35.163 6.691   39.520  1.00 41.94 ? 109 PHE   C CG  1 
ATOM   3287 C  CD1 . PHE   C 1 16  ? -35.003 5.362   39.873  1.00 41.22 ? 109 PHE   C CD1 1 
ATOM   3288 C  CD2 . PHE   C 1 16  ? -34.737 7.668   40.410  1.00 41.84 ? 109 PHE   C CD2 1 
ATOM   3289 C  CE1 . PHE   C 1 16  ? -34.449 5.016   41.093  1.00 40.09 ? 109 PHE   C CE1 1 
ATOM   3290 C  CE2 . PHE   C 1 16  ? -34.164 7.316   41.622  1.00 41.04 ? 109 PHE   C CE2 1 
ATOM   3291 C  CZ  . PHE   C 1 16  ? -34.027 5.991   41.965  1.00 40.13 ? 109 PHE   C CZ  1 
ATOM   3292 N  N   . ARG   C 1 17  ? -38.725 6.202   39.889  1.00 41.58 ? 110 ARG   C N   1 
ATOM   3293 C  CA  . ARG   C 1 17  ? -39.526 6.384   41.135  1.00 40.35 ? 110 ARG   C CA  1 
ATOM   3294 C  C   . ARG   C 1 17  ? -39.177 5.268   42.128  1.00 37.58 ? 110 ARG   C C   1 
ATOM   3295 O  O   . ARG   C 1 17  ? -38.661 4.223   41.694  1.00 36.93 ? 110 ARG   C O   1 
ATOM   3296 C  CB  . ARG   C 1 17  ? -41.033 6.352   40.862  1.00 41.91 ? 110 ARG   C CB  1 
ATOM   3297 C  CG  . ARG   C 1 17  ? -41.559 7.509   40.029  1.00 44.83 ? 110 ARG   C CG  1 
ATOM   3298 C  CD  . ARG   C 1 17  ? -42.886 7.149   39.404  1.00 45.86 ? 110 ARG   C CD  1 
ATOM   3299 N  NE  . ARG   C 1 17  ? -43.980 7.356   40.339  1.00 46.53 ? 110 ARG   C NE  1 
ATOM   3300 C  CZ  . ARG   C 1 17  ? -45.226 7.654   39.988  1.00 47.94 ? 110 ARG   C CZ  1 
ATOM   3301 N  N   . LEU   C 1 18  ? -39.451 5.486   43.413  1.00 36.36 ? 111 LEU   C N   1 
ATOM   3302 C  CA  . LEU   C 1 18  ? -39.241 4.489   44.494  1.00 34.12 ? 111 LEU   C CA  1 
ATOM   3303 C  C   . LEU   C 1 18  ? -40.588 3.846   44.801  1.00 33.80 ? 111 LEU   C C   1 
ATOM   3304 O  O   . LEU   C 1 18  ? -41.614 4.515   44.617  1.00 34.18 ? 111 LEU   C O   1 
ATOM   3305 C  CB  . LEU   C 1 18  ? -38.671 5.172   45.741  1.00 33.46 ? 111 LEU   C CB  1 
ATOM   3306 C  CG  . LEU   C 1 18  ? -37.325 5.865   45.580  1.00 33.57 ? 111 LEU   C CG  1 
ATOM   3307 C  CD1 . LEU   C 1 18  ? -36.874 6.431   46.910  1.00 32.69 ? 111 LEU   C CD1 1 
ATOM   3308 C  CD2 . LEU   C 1 18  ? -36.267 4.920   45.026  1.00 32.95 ? 111 LEU   C CD2 1 
ATOM   3309 N  N   . GLY   C 1 19  ? -40.577 2.571   45.187  1.00 32.99 ? 112 GLY   C N   1 
ATOM   3310 C  CA  . GLY   C 1 19  ? -41.746 1.860   45.722  1.00 32.23 ? 112 GLY   C CA  1 
ATOM   3311 C  C   . GLY   C 1 19  ? -41.382 1.192   47.029  1.00 31.15 ? 112 GLY   C C   1 
ATOM   3312 O  O   . GLY   C 1 19  ? -40.173 0.984   47.290  1.00 29.75 ? 112 GLY   C O   1 
ATOM   3313 N  N   . PHE   C 1 20  ? -42.381 0.869   47.838  1.00 31.24 ? 113 PHE   C N   1 
ATOM   3314 C  CA  . PHE   C 1 20  ? -42.227 0.258   49.178  1.00 31.09 ? 113 PHE   C CA  1 
ATOM   3315 C  C   . PHE   C 1 20  ? -43.280 -0.841  49.315  1.00 32.14 ? 113 PHE   C C   1 
ATOM   3316 O  O   . PHE   C 1 20  ? -44.354 -0.730  48.691  1.00 31.90 ? 113 PHE   C O   1 
ATOM   3317 C  CB  . PHE   C 1 20  ? -42.340 1.352   50.240  1.00 30.92 ? 113 PHE   C CB  1 
ATOM   3318 C  CG  . PHE   C 1 20  ? -41.352 2.482   50.053  1.00 30.59 ? 113 PHE   C CG  1 
ATOM   3319 C  CD1 . PHE   C 1 20  ? -40.085 2.411   50.607  1.00 30.66 ? 113 PHE   C CD1 1 
ATOM   3320 C  CD2 . PHE   C 1 20  ? -41.677 3.600   49.309  1.00 31.27 ? 113 PHE   C CD2 1 
ATOM   3321 C  CE1 . PHE   C 1 20  ? -39.161 3.438   50.425  1.00 30.53 ? 113 PHE   C CE1 1 
ATOM   3322 C  CE2 . PHE   C 1 20  ? -40.764 4.629   49.126  1.00 31.13 ? 113 PHE   C CE2 1 
ATOM   3323 C  CZ  . PHE   C 1 20  ? -39.521 4.564   49.712  1.00 30.97 ? 113 PHE   C CZ  1 
ATOM   3324 N  N   . LEU   C 1 21  ? -42.986 -1.870  50.110  1.00 32.04 ? 114 LEU   C N   1 
ATOM   3325 C  CA  . LEU   C 1 21  ? -43.986 -2.913  50.448  1.00 33.79 ? 114 LEU   C CA  1 
ATOM   3326 C  C   . LEU   C 1 21  ? -45.124 -2.248  51.238  1.00 33.46 ? 114 LEU   C C   1 
ATOM   3327 O  O   . LEU   C 1 21  ? -44.847 -1.298  51.991  1.00 33.15 ? 114 LEU   C O   1 
ATOM   3328 C  CB  . LEU   C 1 21  ? -43.311 -4.039  51.240  1.00 34.73 ? 114 LEU   C CB  1 
ATOM   3329 C  CG  . LEU   C 1 21  ? -42.284 -4.857  50.446  1.00 35.64 ? 114 LEU   C CG  1 
ATOM   3330 C  CD1 . LEU   C 1 21  ? -41.525 -5.795  51.375  1.00 36.26 ? 114 LEU   C CD1 1 
ATOM   3331 C  CD2 . LEU   C 1 21  ? -42.941 -5.615  49.282  1.00 37.35 ? 114 LEU   C CD2 1 
ATOM   3332 N  N   . HIS   C 1 22  ? -46.362 -2.675  51.013  1.00 33.94 ? 115 HIS   C N   1 
ATOM   3333 C  CA  . HIS   C 1 22  ? -47.569 -2.215  51.765  1.00 33.73 ? 115 HIS   C CA  1 
ATOM   3334 C  C   . HIS   C 1 22  ? -47.723 -3.139  52.975  1.00 32.56 ? 115 HIS   C C   1 
ATOM   3335 O  O   . HIS   C 1 22  ? -48.553 -4.034  52.941  1.00 33.30 ? 115 HIS   C O   1 
ATOM   3336 C  CB  . HIS   C 1 22  ? -48.783 -2.161  50.834  1.00 35.61 ? 115 HIS   C CB  1 
ATOM   3337 C  CG  . HIS   C 1 22  ? -48.460 -1.503  49.536  1.00 36.98 ? 115 HIS   C CG  1 
ATOM   3338 N  ND1 . HIS   C 1 22  ? -48.035 -0.189  49.477  1.00 37.13 ? 115 HIS   C ND1 1 
ATOM   3339 C  CD2 . HIS   C 1 22  ? -48.430 -1.974  48.267  1.00 38.52 ? 115 HIS   C CD2 1 
ATOM   3340 C  CE1 . HIS   C 1 22  ? -47.776 0.128   48.229  1.00 37.82 ? 115 HIS   C CE1 1 
ATOM   3341 N  NE2 . HIS   C 1 22  ? -47.987 -0.960  47.468  1.00 39.00 ? 115 HIS   C NE2 1 
ATOM   3342 N  N   A SER   C 1 23  ? -46.900 -2.919  54.001  0.60 31.66 ? 116 SER   C N   1 
ATOM   3343 N  N   B SER   C 1 23  ? -46.894 -2.937  54.002  0.40 31.66 ? 116 SER   C N   1 
ATOM   3344 C  CA  A SER   C 1 23  ? -46.647 -3.881  55.110  0.60 31.50 ? 116 SER   C CA  1 
ATOM   3345 C  CA  B SER   C 1 23  ? -46.659 -3.901  55.116  0.40 31.51 ? 116 SER   C CA  1 
ATOM   3346 C  C   A SER   C 1 23  ? -47.646 -3.705  56.264  0.60 31.94 ? 116 SER   C C   1 
ATOM   3347 C  C   B SER   C 1 23  ? -47.654 -3.713  56.272  0.40 31.91 ? 116 SER   C C   1 
ATOM   3348 O  O   A SER   C 1 23  ? -47.813 -4.656  57.046  0.60 32.80 ? 116 SER   C O   1 
ATOM   3349 O  O   B SER   C 1 23  ? -47.808 -4.661  57.081  0.40 32.68 ? 116 SER   C O   1 
ATOM   3350 C  CB  A SER   C 1 23  ? -45.237 -3.751  55.583  0.60 30.78 ? 116 SER   C CB  1 
ATOM   3351 C  CB  B SER   C 1 23  ? -45.248 -3.785  55.597  0.40 30.75 ? 116 SER   C CB  1 
ATOM   3352 O  OG  A SER   C 1 23  ? -44.309 -4.039  54.536  0.60 30.17 ? 116 SER   C OG  1 
ATOM   3353 O  OG  B SER   C 1 23  ? -44.832 -2.429  55.591  0.40 29.72 ? 116 SER   C OG  1 
ATOM   3354 N  N   . GLY   C 1 24  ? -48.285 -2.540  56.379  1.00 31.38 ? 117 GLY   C N   1 
ATOM   3355 C  CA  . GLY   C 1 24  ? -49.162 -2.197  57.516  1.00 32.07 ? 117 GLY   C CA  1 
ATOM   3356 C  C   . GLY   C 1 24  ? -48.387 -1.915  58.796  1.00 31.59 ? 117 GLY   C C   1 
ATOM   3357 O  O   . GLY   C 1 24  ? -47.142 -1.829  58.741  1.00 31.31 ? 117 GLY   C O   1 
ATOM   3358 N  N   . THR   C 1 25  ? -49.091 -1.811  59.923  1.00 32.50 ? 118 THR   C N   1 
ATOM   3359 C  CA  . THR   C 1 25  ? -48.553 -1.352  61.232  1.00 32.63 ? 118 THR   C CA  1 
ATOM   3360 C  C   . THR   C 1 25  ? -48.789 -2.422  62.309  1.00 34.38 ? 118 THR   C C   1 
ATOM   3361 O  O   . THR   C 1 25  ? -48.916 -2.046  63.485  1.00 34.87 ? 118 THR   C O   1 
ATOM   3362 C  CB  . THR   C 1 25  ? -49.175 -0.009  61.634  1.00 32.29 ? 118 THR   C CB  1 
ATOM   3363 O  OG1 . THR   C 1 25  ? -50.584 -0.176  61.729  1.00 32.59 ? 118 THR   C OG1 1 
ATOM   3364 C  CG2 . THR   C 1 25  ? -48.889 1.104   60.649  1.00 31.65 ? 118 THR   C CG2 1 
ATOM   3365 N  N   . ALA   C 1 26  ? -48.864 -3.704  61.945  1.00 35.85 ? 119 ALA   C N   1 
ATOM   3366 C  CA  . ALA   C 1 26  ? -49.021 -4.822  62.911  1.00 37.86 ? 119 ALA   C CA  1 
ATOM   3367 C  C   . ALA   C 1 26  ? -47.763 -4.917  63.785  1.00 39.12 ? 119 ALA   C C   1 
ATOM   3368 O  O   . ALA   C 1 26  ? -46.667 -4.639  63.284  1.00 37.30 ? 119 ALA   C O   1 
ATOM   3369 C  CB  . ALA   C 1 26  ? -49.287 -6.119  62.186  1.00 38.45 ? 119 ALA   C CB  1 
ATOM   3370 N  N   . LYS   C 1 27  ? -47.931 -5.329  65.043  1.00 42.80 ? 120 LYS   C N   1 
ATOM   3371 C  CA  . LYS   C 1 27  ? -46.866 -5.443  66.079  1.00 44.65 ? 120 LYS   C CA  1 
ATOM   3372 C  C   . LYS   C 1 27  ? -45.609 -6.100  65.498  1.00 44.92 ? 120 LYS   C C   1 
ATOM   3373 O  O   . LYS   C 1 27  ? -44.505 -5.636  65.849  1.00 44.18 ? 120 LYS   C O   1 
ATOM   3374 C  CB  . LYS   C 1 27  ? -47.383 -6.235  67.287  1.00 47.47 ? 120 LYS   C CB  1 
ATOM   3375 C  CG  . LYS   C 1 27  ? -48.374 -5.481  68.165  1.00 48.92 ? 120 LYS   C CG  1 
ATOM   3376 C  CD  . LYS   C 1 27  ? -48.922 -6.284  69.323  1.00 51.11 ? 120 LYS   C CD  1 
ATOM   3377 C  CE  . LYS   C 1 27  ? -49.912 -5.492  70.148  1.00 52.22 ? 120 LYS   C CE  1 
ATOM   3378 N  NZ  . LYS   C 1 27  ? -50.377 -6.265  71.324  1.00 54.71 ? 120 LYS   C NZ  1 
ATOM   3379 N  N   . SER   C 1 28  ? -45.765 -7.088  64.610  1.00 45.99 ? 121 SER   C N   1 
ATOM   3380 C  CA  . SER   C 1 28  ? -44.680 -7.964  64.089  1.00 47.34 ? 121 SER   C CA  1 
ATOM   3381 C  C   . SER   C 1 28  ? -43.786 -7.273  63.044  1.00 45.92 ? 121 SER   C C   1 
ATOM   3382 O  O   . SER   C 1 28  ? -42.675 -7.767  62.787  1.00 47.45 ? 121 SER   C O   1 
ATOM   3383 C  CB  . SER   C 1 28  ? -45.276 -9.218  63.500  1.00 49.66 ? 121 SER   C CB  1 
ATOM   3384 O  OG  . SER   C 1 28  ? -46.125 -8.899  62.401  1.00 50.55 ? 121 SER   C OG  1 
ATOM   3385 N  N   A VAL   C 1 29  ? -44.256 -6.175  62.450  0.60 44.35 ? 122 VAL   C N   1 
ATOM   3386 N  N   B VAL   C 1 29  ? -44.263 -6.177  62.440  0.40 44.35 ? 122 VAL   C N   1 
ATOM   3387 C  CA  A VAL   C 1 29  ? -43.632 -5.543  61.250  0.60 42.24 ? 122 VAL   C CA  1 
ATOM   3388 C  CA  B VAL   C 1 29  ? -43.632 -5.538  61.245  0.40 42.29 ? 122 VAL   C CA  1 
ATOM   3389 C  C   A VAL   C 1 29  ? -42.285 -4.930  61.656  0.60 41.02 ? 122 VAL   C C   1 
ATOM   3390 C  C   B VAL   C 1 29  ? -42.285 -4.928  61.656  0.40 41.02 ? 122 VAL   C C   1 
ATOM   3391 O  O   A VAL   C 1 29  ? -42.242 -4.176  62.647  0.60 41.17 ? 122 VAL   C O   1 
ATOM   3392 O  O   B VAL   C 1 29  ? -42.246 -4.173  62.649  0.40 41.17 ? 122 VAL   C O   1 
ATOM   3393 C  CB  A VAL   C 1 29  ? -44.579 -4.516  60.603  0.60 41.38 ? 122 VAL   C CB  1 
ATOM   3394 C  CB  B VAL   C 1 29  ? -44.562 -4.498  60.590  0.40 41.58 ? 122 VAL   C CB  1 
ATOM   3395 C  CG1 A VAL   C 1 29  ? -43.923 -3.831  59.428  0.60 40.63 ? 122 VAL   C CG1 1 
ATOM   3396 C  CG1 B VAL   C 1 29  ? -44.222 -3.070  60.992  0.40 40.91 ? 122 VAL   C CG1 1 
ATOM   3397 C  CG2 A VAL   C 1 29  ? -45.897 -5.153  60.175  0.60 42.12 ? 122 VAL   C CG2 1 
ATOM   3398 C  CG2 B VAL   C 1 29  ? -44.552 -4.635  59.076  0.40 41.35 ? 122 VAL   C CG2 1 
ATOM   3399 N  N   . THR   C 1 30  ? -41.223 -5.260  60.916  1.00 39.58 ? 123 THR   C N   1 
ATOM   3400 C  CA  . THR   C 1 30  ? -39.827 -4.807  61.184  1.00 38.24 ? 123 THR   C CA  1 
ATOM   3401 C  C   . THR   C 1 30  ? -39.506 -3.559  60.357  1.00 35.92 ? 123 THR   C C   1 
ATOM   3402 O  O   . THR   C 1 30  ? -38.568 -2.831  60.716  1.00 34.83 ? 123 THR   C O   1 
ATOM   3403 C  CB  . THR   C 1 30  ? -38.838 -5.957  60.962  1.00 39.09 ? 123 THR   C CB  1 
ATOM   3404 O  OG1 . THR   C 1 30  ? -38.938 -6.370  59.601  1.00 39.63 ? 123 THR   C OG1 1 
ATOM   3405 C  CG2 . THR   C 1 30  ? -39.114 -7.140  61.866  1.00 39.86 ? 123 THR   C CG2 1 
ATOM   3406 N  N   A CYS   C 1 31  ? -40.261 -3.312  59.282  0.70 35.11 ? 124 CYS   C N   1 
ATOM   3407 N  N   B CYS   C 1 31  ? -40.215 -3.335  59.243  0.30 34.79 ? 124 CYS   C N   1 
ATOM   3408 C  CA  A CYS   C 1 31  ? -40.121 -2.112  58.413  0.70 33.93 ? 124 CYS   C CA  1 
ATOM   3409 C  CA  B CYS   C 1 31  ? -40.118 -2.086  58.442  0.30 33.41 ? 124 CYS   C CA  1 
ATOM   3410 C  C   A CYS   C 1 31  ? -41.471 -1.791  57.756  0.70 33.54 ? 124 CYS   C C   1 
ATOM   3411 C  C   B CYS   C 1 31  ? -41.468 -1.793  57.772  0.30 33.01 ? 124 CYS   C C   1 
ATOM   3412 O  O   A CYS   C 1 31  ? -42.132 -2.724  57.257  0.70 33.43 ? 124 CYS   C O   1 
ATOM   3413 O  O   B CYS   C 1 31  ? -42.125 -2.742  57.295  0.30 33.28 ? 124 CYS   C O   1 
ATOM   3414 C  CB  A CYS   C 1 31  ? -39.005 -2.349  57.401  0.70 33.90 ? 124 CYS   C CB  1 
ATOM   3415 C  CB  B CYS   C 1 31  ? -38.941 -2.125  57.466  0.30 32.98 ? 124 CYS   C CB  1 
ATOM   3416 S  SG  A CYS   C 1 31  ? -38.868 -1.132  56.078  0.70 33.88 ? 124 CYS   C SG  1 
ATOM   3417 S  SG  B CYS   C 1 31  ? -39.194 -3.127  55.985  0.30 33.23 ? 124 CYS   C SG  1 
ATOM   3418 N  N   . THR   C 1 32  ? -41.888 -0.525  57.807  1.00 31.63 ? 125 THR   C N   1 
ATOM   3419 C  CA  . THR   C 1 32  ? -43.198 -0.078  57.278  1.00 31.21 ? 125 THR   C CA  1 
ATOM   3420 C  C   . THR   C 1 32  ? -43.055 1.350   56.750  1.00 29.82 ? 125 THR   C C   1 
ATOM   3421 O  O   . THR   C 1 32  ? -42.395 2.169   57.419  1.00 29.54 ? 125 THR   C O   1 
ATOM   3422 C  CB  . THR   C 1 32  ? -44.316 -0.247  58.312  1.00 31.19 ? 125 THR   C CB  1 
ATOM   3423 O  OG1 . THR   C 1 32  ? -45.553 0.019   57.646  1.00 31.94 ? 125 THR   C OG1 1 
ATOM   3424 C  CG2 . THR   C 1 32  ? -44.162 0.635   59.531  1.00 31.50 ? 125 THR   C CG2 1 
ATOM   3425 N  N   . TYR   C 1 33  ? -43.646 1.603   55.588  1.00 29.27 ? 126 TYR   C N   1 
ATOM   3426 C  CA  . TYR   C 1 33  ? -43.601 2.900   54.880  1.00 29.18 ? 126 TYR   C CA  1 
ATOM   3427 C  C   . TYR   C 1 33  ? -44.964 3.579   54.992  1.00 29.43 ? 126 TYR   C C   1 
ATOM   3428 O  O   . TYR   C 1 33  ? -45.993 2.925   54.764  1.00 29.99 ? 126 TYR   C O   1 
ATOM   3429 C  CB  . TYR   C 1 33  ? -43.170 2.704   53.424  1.00 28.89 ? 126 TYR   C CB  1 
ATOM   3430 C  CG  . TYR   C 1 33  ? -43.312 3.942   52.577  1.00 28.95 ? 126 TYR   C CG  1 
ATOM   3431 C  CD1 . TYR   C 1 33  ? -42.400 4.975   52.683  1.00 28.75 ? 126 TYR   C CD1 1 
ATOM   3432 C  CD2 . TYR   C 1 33  ? -44.358 4.080   51.679  1.00 29.26 ? 126 TYR   C CD2 1 
ATOM   3433 C  CE1 . TYR   C 1 33  ? -42.521 6.114   51.902  1.00 29.34 ? 126 TYR   C CE1 1 
ATOM   3434 C  CE2 . TYR   C 1 33  ? -44.489 5.209   50.888  1.00 30.05 ? 126 TYR   C CE2 1 
ATOM   3435 C  CZ  . TYR   C 1 33  ? -43.568 6.236   51.007  1.00 30.22 ? 126 TYR   C CZ  1 
ATOM   3436 O  OH  . TYR   C 1 33  ? -43.690 7.364   50.242  1.00 31.07 ? 126 TYR   C OH  1 
ATOM   3437 N  N   . SER   C 1 34  ? -44.947 4.870   55.328  1.00 29.64 ? 127 SER   C N   1 
ATOM   3438 C  CA  . SER   C 1 34  ? -46.124 5.769   55.359  1.00 30.43 ? 127 SER   C CA  1 
ATOM   3439 C  C   . SER   C 1 34  ? -46.141 6.598   54.080  1.00 30.94 ? 127 SER   C C   1 
ATOM   3440 O  O   . SER   C 1 34  ? -45.296 7.474   53.913  1.00 29.85 ? 127 SER   C O   1 
ATOM   3441 C  CB  . SER   C 1 34  ? -46.088 6.659   56.579  1.00 30.57 ? 127 SER   C CB  1 
ATOM   3442 O  OG  . SER   C 1 34  ? -47.150 7.596   56.558  1.00 31.13 ? 127 SER   C OG  1 
ATOM   3443 N  N   . PRO   C 1 35  ? -47.100 6.357   53.152  1.00 31.76 ? 128 PRO   C N   1 
ATOM   3444 C  CA  . PRO   C 1 35  ? -47.249 7.195   51.964  1.00 32.85 ? 128 PRO   C CA  1 
ATOM   3445 C  C   . PRO   C 1 35  ? -47.656 8.628   52.329  1.00 34.18 ? 128 PRO   C C   1 
ATOM   3446 O  O   . PRO   C 1 35  ? -47.228 9.530   51.652  1.00 35.85 ? 128 PRO   C O   1 
ATOM   3447 C  CB  . PRO   C 1 35  ? -48.341 6.540   51.100  1.00 33.10 ? 128 PRO   C CB  1 
ATOM   3448 C  CG  . PRO   C 1 35  ? -48.790 5.297   51.850  1.00 32.70 ? 128 PRO   C CG  1 
ATOM   3449 C  CD  . PRO   C 1 35  ? -48.082 5.266   53.190  1.00 31.73 ? 128 PRO   C CD  1 
ATOM   3450 N  N   . ALA   C 1 36  ? -48.458 8.807   53.380  1.00 34.99 ? 129 ALA   C N   1 
ATOM   3451 C  CA  . ALA   C 1 36  ? -48.964 10.133  53.818  1.00 36.60 ? 129 ALA   C CA  1 
ATOM   3452 C  C   . ALA   C 1 36  ? -47.786 11.013  54.257  1.00 36.82 ? 129 ALA   C C   1 
ATOM   3453 O  O   . ALA   C 1 36  ? -47.824 12.215  53.991  1.00 38.74 ? 129 ALA   C O   1 
ATOM   3454 C  CB  . ALA   C 1 36  ? -49.988 9.974   54.924  1.00 36.70 ? 129 ALA   C CB  1 
ATOM   3455 N  N   . LEU   C 1 37  ? -46.770 10.429  54.898  1.00 36.63 ? 130 LEU   C N   1 
ATOM   3456 C  CA  . LEU   C 1 37  ? -45.615 11.178  55.464  1.00 36.54 ? 130 LEU   C CA  1 
ATOM   3457 C  C   . LEU   C 1 37  ? -44.387 11.063  54.554  1.00 36.33 ? 130 LEU   C C   1 
ATOM   3458 O  O   . LEU   C 1 37  ? -43.419 11.772  54.846  1.00 37.00 ? 130 LEU   C O   1 
ATOM   3459 C  CB  . LEU   C 1 37  ? -45.310 10.630  56.860  1.00 35.77 ? 130 LEU   C CB  1 
ATOM   3460 C  CG  . LEU   C 1 37  ? -46.393 10.842  57.911  1.00 36.69 ? 130 LEU   C CG  1 
ATOM   3461 C  CD1 . LEU   C 1 37  ? -46.141 9.978   59.134  1.00 36.48 ? 130 LEU   C CD1 1 
ATOM   3462 C  CD2 . LEU   C 1 37  ? -46.477 12.303  58.310  1.00 38.14 ? 130 LEU   C CD2 1 
ATOM   3463 N  N   . ASN   C 1 38  ? -44.418 10.201  53.522  1.00 35.86 ? 131 ASN   C N   1 
ATOM   3464 C  CA  . ASN   C 1 38  ? -43.249 9.751   52.710  1.00 35.04 ? 131 ASN   C CA  1 
ATOM   3465 C  C   . ASN   C 1 38  ? -42.108 9.376   53.668  1.00 33.92 ? 131 ASN   C C   1 
ATOM   3466 O  O   . ASN   C 1 38  ? -40.979 9.915   53.547  1.00 32.79 ? 131 ASN   C O   1 
ATOM   3467 C  CB  . ASN   C 1 38  ? -42.840 10.791  51.663  1.00 36.08 ? 131 ASN   C CB  1 
ATOM   3468 C  CG  . ASN   C 1 38  ? -41.744 10.316  50.734  1.00 35.37 ? 131 ASN   C CG  1 
ATOM   3469 O  OD1 . ASN   C 1 38  ? -41.645 9.138   50.416  1.00 34.57 ? 131 ASN   C OD1 1 
ATOM   3470 N  ND2 . ASN   C 1 38  ? -40.923 11.239  50.267  1.00 35.95 ? 131 ASN   C ND2 1 
ATOM   3471 N  N   . LYS   C 1 39  ? -42.409 8.489   54.617  1.00 33.28 ? 132 LYS   C N   1 
ATOM   3472 C  CA  . LYS   C 1 39  ? -41.501 8.181   55.748  1.00 32.40 ? 132 LYS   C CA  1 
ATOM   3473 C  C   . LYS   C 1 39  ? -41.467 6.677   55.983  1.00 31.25 ? 132 LYS   C C   1 
ATOM   3474 O  O   . LYS   C 1 39  ? -42.543 6.073   56.167  1.00 32.04 ? 132 LYS   C O   1 
ATOM   3475 C  CB  . LYS   C 1 39  ? -41.937 8.936   57.002  1.00 32.80 ? 132 LYS   C CB  1 
ATOM   3476 C  CG  . LYS   C 1 39  ? -40.992 8.828   58.185  1.00 32.72 ? 132 LYS   C CG  1 
ATOM   3477 C  CD  . LYS   C 1 39  ? -41.360 9.797   59.299  1.00 33.58 ? 132 LYS   C CD  1 
ATOM   3478 C  CE  . LYS   C 1 39  ? -40.375 9.770   60.453  1.00 34.02 ? 132 LYS   C CE  1 
ATOM   3479 N  NZ  . LYS   C 1 39  ? -40.508 11.016  61.247  1.00 35.73 ? 132 LYS   C NZ  1 
ATOM   3480 N  N   A MET   C 1 40  ? -40.258 6.107   55.956  0.50 30.92 ? 133 MET   C N   1 
ATOM   3481 N  N   B MET   C 1 40  ? -40.260 6.107   55.947  0.50 30.61 ? 133 MET   C N   1 
ATOM   3482 C  CA  A MET   C 1 40  ? -39.958 4.701   56.335  0.50 30.90 ? 133 MET   C CA  1 
ATOM   3483 C  CA  B MET   C 1 40  ? -39.961 4.704   56.334  0.50 30.39 ? 133 MET   C CA  1 
ATOM   3484 C  C   A MET   C 1 40  ? -39.726 4.650   57.850  0.50 30.96 ? 133 MET   C C   1 
ATOM   3485 C  C   B MET   C 1 40  ? -39.728 4.650   57.850  0.50 30.67 ? 133 MET   C C   1 
ATOM   3486 O  O   A MET   C 1 40  ? -38.914 5.455   58.357  0.50 30.70 ? 133 MET   C O   1 
ATOM   3487 O  O   B MET   C 1 40  ? -38.914 5.453   58.353  0.50 30.43 ? 133 MET   C O   1 
ATOM   3488 C  CB  A MET   C 1 40  ? -38.703 4.201   55.609  0.50 30.75 ? 133 MET   C CB  1 
ATOM   3489 C  CB  B MET   C 1 40  ? -38.706 4.193   55.619  0.50 29.84 ? 133 MET   C CB  1 
ATOM   3490 C  CG  A MET   C 1 40  ? -38.185 2.853   56.091  0.50 31.27 ? 133 MET   C CG  1 
ATOM   3491 C  CG  B MET   C 1 40  ? -38.361 2.759   55.984  0.50 30.00 ? 133 MET   C CG  1 
ATOM   3492 S  SD  A MET   C 1 40  ? -36.685 2.336   55.191  0.50 32.01 ? 133 MET   C SD  1 
ATOM   3493 S  SD  B MET   C 1 40  ? -39.625 1.595   55.426  0.50 30.92 ? 133 MET   C SD  1 
ATOM   3494 C  CE  A MET   C 1 40  ? -37.445 1.752   53.676  0.50 32.14 ? 133 MET   C CE  1 
ATOM   3495 C  CE  B MET   C 1 40  ? -39.139 1.392   53.715  0.50 30.44 ? 133 MET   C CE  1 
ATOM   3496 N  N   . PHE   C 1 41  ? -40.433 3.753   58.546  1.00 30.87 ? 134 PHE   C N   1 
ATOM   3497 C  CA  . PHE   C 1 41  ? -40.166 3.390   59.959  1.00 30.84 ? 134 PHE   C CA  1 
ATOM   3498 C  C   . PHE   C 1 41  ? -39.555 1.988   59.937  1.00 31.07 ? 134 PHE   C C   1 
ATOM   3499 O  O   . PHE   C 1 41  ? -40.209 1.086   59.415  1.00 29.57 ? 134 PHE   C O   1 
ATOM   3500 C  CB  . PHE   C 1 41  ? -41.452 3.425   60.785  1.00 31.32 ? 134 PHE   C CB  1 
ATOM   3501 C  CG  . PHE   C 1 41  ? -42.182 4.747   60.769  1.00 31.53 ? 134 PHE   C CG  1 
ATOM   3502 C  CD1 . PHE   C 1 41  ? -42.906 5.147   59.659  1.00 31.18 ? 134 PHE   C CD1 1 
ATOM   3503 C  CD2 . PHE   C 1 41  ? -42.141 5.590   61.868  1.00 31.68 ? 134 PHE   C CD2 1 
ATOM   3504 C  CE1 . PHE   C 1 41  ? -43.573 6.364   59.637  1.00 31.57 ? 134 PHE   C CE1 1 
ATOM   3505 C  CE2 . PHE   C 1 41  ? -42.820 6.804   61.857  1.00 32.51 ? 134 PHE   C CE2 1 
ATOM   3506 C  CZ  . PHE   C 1 41  ? -43.545 7.183   60.743  1.00 32.35 ? 134 PHE   C CZ  1 
ATOM   3507 N  N   . CYS   C 1 42  ? -38.339 1.810   60.458  1.00 32.52 ? 135 CYS   C N   1 
ATOM   3508 C  CA  . CYS   C 1 42  ? -37.629 0.505   60.414  1.00 33.12 ? 135 CYS   C CA  1 
ATOM   3509 C  C   . CYS   C 1 42  ? -36.852 0.284   61.716  1.00 33.44 ? 135 CYS   C C   1 
ATOM   3510 O  O   . CYS   C 1 42  ? -36.573 1.262   62.432  1.00 33.34 ? 135 CYS   C O   1 
ATOM   3511 C  CB  . CYS   C 1 42  ? -36.726 0.435   59.184  1.00 34.00 ? 135 CYS   C CB  1 
ATOM   3512 S  SG  . CYS   C 1 42  ? -35.402 1.683   59.160  1.00 36.14 ? 135 CYS   C SG  1 
ATOM   3513 N  N   . GLN   C 1 43  ? -36.532 -0.972  62.016  1.00 34.04 ? 136 GLN   C N   1 
ATOM   3514 C  CA  . GLN   C 1 43  ? -35.690 -1.363  63.168  1.00 34.63 ? 136 GLN   C CA  1 
ATOM   3515 C  C   . GLN   C 1 43  ? -34.222 -1.362  62.750  1.00 34.06 ? 136 GLN   C C   1 
ATOM   3516 O  O   . GLN   C 1 43  ? -33.945 -1.624  61.574  1.00 34.00 ? 136 GLN   C O   1 
ATOM   3517 C  CB  . GLN   C 1 43  ? -36.079 -2.755  63.677  1.00 35.56 ? 136 GLN   C CB  1 
ATOM   3518 C  CG  . GLN   C 1 43  ? -37.457 -2.799  64.325  1.00 36.33 ? 136 GLN   C CG  1 
ATOM   3519 C  CD  . GLN   C 1 43  ? -37.872 -4.213  64.635  1.00 36.97 ? 136 GLN   C CD  1 
ATOM   3520 O  OE1 . GLN   C 1 43  ? -37.390 -5.180  64.046  1.00 36.62 ? 136 GLN   C OE1 1 
ATOM   3521 N  NE2 . GLN   C 1 43  ? -38.750 -4.336  65.617  1.00 38.47 ? 136 GLN   C NE2 1 
ATOM   3522 N  N   . LEU   C 1 44  ? -33.335 -1.143  63.722  1.00 34.96 ? 137 LEU   C N   1 
ATOM   3523 C  CA  . LEU   C 1 44  ? -31.854 -1.169  63.582  1.00 34.98 ? 137 LEU   C CA  1 
ATOM   3524 C  C   . LEU   C 1 44  ? -31.408 -2.496  62.963  1.00 35.28 ? 137 LEU   C C   1 
ATOM   3525 O  O   . LEU   C 1 44  ? -31.848 -3.559  63.453  1.00 35.35 ? 137 LEU   C O   1 
ATOM   3526 C  CB  . LEU   C 1 44  ? -31.240 -0.975  64.967  1.00 36.05 ? 137 LEU   C CB  1 
ATOM   3527 C  CG  . LEU   C 1 44  ? -29.757 -0.610  64.972  1.00 36.56 ? 137 LEU   C CG  1 
ATOM   3528 C  CD1 . LEU   C 1 44  ? -29.454 0.431   66.033  1.00 37.58 ? 137 LEU   C CD1 1 
ATOM   3529 C  CD2 . LEU   C 1 44  ? -28.896 -1.843  65.163  1.00 37.14 ? 137 LEU   C CD2 1 
ATOM   3530 N  N   . ALA   C 1 45  ? -30.586 -2.424  61.907  1.00 34.62 ? 138 ALA   C N   1 
ATOM   3531 C  CA  . ALA   C 1 45  ? -29.870 -3.558  61.276  1.00 35.78 ? 138 ALA   C CA  1 
ATOM   3532 C  C   . ALA   C 1 45  ? -30.840 -4.508  60.566  1.00 35.38 ? 138 ALA   C C   1 
ATOM   3533 O  O   . ALA   C 1 45  ? -30.341 -5.473  59.972  1.00 36.91 ? 138 ALA   C O   1 
ATOM   3534 C  CB  . ALA   C 1 45  ? -29.055 -4.305  62.312  1.00 36.98 ? 138 ALA   C CB  1 
ATOM   3535 N  N   . LYS   C 1 46  ? -32.151 -4.249  60.595  1.00 34.43 ? 139 LYS   C N   1 
ATOM   3536 C  CA  . LYS   C 1 46  ? -33.163 -5.104  59.926  1.00 34.57 ? 139 LYS   C CA  1 
ATOM   3537 C  C   . LYS   C 1 46  ? -33.305 -4.697  58.450  1.00 32.62 ? 139 LYS   C C   1 
ATOM   3538 O  O   . LYS   C 1 46  ? -33.029 -3.517  58.091  1.00 30.67 ? 139 LYS   C O   1 
ATOM   3539 C  CB  . LYS   C 1 46  ? -34.498 -5.048  60.672  1.00 35.57 ? 139 LYS   C CB  1 
ATOM   3540 C  CG  . LYS   C 1 46  ? -34.546 -5.832  61.979  1.00 37.83 ? 139 LYS   C CG  1 
ATOM   3541 C  CD  . LYS   C 1 46  ? -34.989 -7.265  61.736  1.00 39.81 ? 139 LYS   C CD  1 
ATOM   3542 C  CE  . LYS   C 1 46  ? -35.091 -8.119  62.983  1.00 41.58 ? 139 LYS   C CE  1 
ATOM   3543 N  NZ  . LYS   C 1 46  ? -36.051 -7.556  63.965  1.00 43.39 ? 139 LYS   C NZ  1 
ATOM   3544 N  N   . THR   C 1 47  ? -33.727 -5.656  57.625  1.00 32.58 ? 140 THR   C N   1 
ATOM   3545 C  CA  . THR   C 1 47  ? -33.945 -5.510  56.169  1.00 32.28 ? 140 THR   C CA  1 
ATOM   3546 C  C   . THR   C 1 47  ? -34.982 -4.423  55.874  1.00 31.49 ? 140 THR   C C   1 
ATOM   3547 O  O   . THR   C 1 47  ? -36.129 -4.512  56.345  1.00 30.98 ? 140 THR   C O   1 
ATOM   3548 C  CB  . THR   C 1 47  ? -34.398 -6.835  55.553  1.00 34.15 ? 140 THR   C CB  1 
ATOM   3549 O  OG1 . THR   C 1 47  ? -33.401 -7.784  55.933  1.00 34.34 ? 140 THR   C OG1 1 
ATOM   3550 C  CG2 . THR   C 1 47  ? -34.549 -6.766  54.050  1.00 34.02 ? 140 THR   C CG2 1 
ATOM   3551 N  N   A CYS   C 1 48  ? -34.578 -3.431  55.078  0.50 30.91 ? 141 CYS   C N   1 
ATOM   3552 N  N   B CYS   C 1 48  ? -34.581 -3.437  55.071  0.50 31.25 ? 141 CYS   C N   1 
ATOM   3553 C  CA  A CYS   C 1 48  ? -35.436 -2.342  54.555  0.50 30.52 ? 141 CYS   C CA  1 
ATOM   3554 C  CA  B CYS   C 1 48  ? -35.428 -2.328  54.566  0.50 31.07 ? 141 CYS   C CA  1 
ATOM   3555 C  C   A CYS   C 1 48  ? -35.497 -2.439  53.037  0.50 30.77 ? 141 CYS   C C   1 
ATOM   3556 C  C   B CYS   C 1 48  ? -35.501 -2.430  53.044  0.50 31.09 ? 141 CYS   C C   1 
ATOM   3557 O  O   A CYS   C 1 48  ? -34.646 -1.882  52.347  0.50 30.10 ? 141 CYS   C O   1 
ATOM   3558 O  O   B CYS   C 1 48  ? -34.650 -1.871  52.354  0.50 30.39 ? 141 CYS   C O   1 
ATOM   3559 C  CB  A CYS   C 1 48  ? -34.869 -0.991  54.945  0.50 30.22 ? 141 CYS   C CB  1 
ATOM   3560 C  CB  B CYS   C 1 48  ? -34.821 -1.000  54.998  0.50 31.16 ? 141 CYS   C CB  1 
ATOM   3561 S  SG  A CYS   C 1 48  ? -34.862 -0.730  56.728  0.50 29.73 ? 141 CYS   C SG  1 
ATOM   3562 S  SG  B CYS   C 1 48  ? -36.028 0.285   55.405  0.50 31.31 ? 141 CYS   C SG  1 
ATOM   3563 N  N   . PRO   C 1 49  ? -36.496 -3.150  52.467  1.00 31.24 ? 142 PRO   C N   1 
ATOM   3564 C  CA  . PRO   C 1 49  ? -36.643 -3.219  51.015  1.00 32.01 ? 142 PRO   C CA  1 
ATOM   3565 C  C   . PRO   C 1 49  ? -37.016 -1.842  50.445  1.00 32.23 ? 142 PRO   C C   1 
ATOM   3566 O  O   . PRO   C 1 49  ? -37.925 -1.197  50.949  1.00 33.76 ? 142 PRO   C O   1 
ATOM   3567 C  CB  . PRO   C 1 49  ? -37.766 -4.251  50.820  1.00 32.63 ? 142 PRO   C CB  1 
ATOM   3568 C  CG  . PRO   C 1 49  ? -37.814 -4.998  52.133  1.00 32.79 ? 142 PRO   C CG  1 
ATOM   3569 C  CD  . PRO   C 1 49  ? -37.523 -3.931  53.170  1.00 32.33 ? 142 PRO   C CD  1 
ATOM   3570 N  N   . VAL   C 1 50  ? -36.266 -1.399  49.448  1.00 32.76 ? 143 VAL   C N   1 
ATOM   3571 C  CA  . VAL   C 1 50  ? -36.586 -0.192  48.642  1.00 33.39 ? 143 VAL   C CA  1 
ATOM   3572 C  C   . VAL   C 1 50  ? -36.655 -0.666  47.195  1.00 33.65 ? 143 VAL   C C   1 
ATOM   3573 O  O   . VAL   C 1 50  ? -35.689 -1.279  46.724  1.00 33.65 ? 143 VAL   C O   1 
ATOM   3574 C  CB  . VAL   C 1 50  ? -35.568 0.944   48.854  1.00 33.29 ? 143 VAL   C CB  1 
ATOM   3575 C  CG1 . VAL   C 1 50  ? -35.807 2.108   47.909  1.00 33.58 ? 143 VAL   C CG1 1 
ATOM   3576 C  CG2 . VAL   C 1 50  ? -35.570 1.419   50.293  1.00 32.70 ? 143 VAL   C CG2 1 
ATOM   3577 N  N   . GLN   C 1 51  ? -37.794 -0.432  46.545  1.00 33.96 ? 144 GLN   C N   1 
ATOM   3578 C  CA  . GLN   C 1 51  ? -38.019 -0.786  45.131  1.00 34.47 ? 144 GLN   C CA  1 
ATOM   3579 C  C   . GLN   C 1 51  ? -37.604 0.384   44.244  1.00 34.35 ? 144 GLN   C C   1 
ATOM   3580 O  O   . GLN   C 1 51  ? -37.957 1.534   44.565  1.00 33.35 ? 144 GLN   C O   1 
ATOM   3581 C  CB  . GLN   C 1 51  ? -39.478 -1.162  44.923  1.00 35.51 ? 144 GLN   C CB  1 
ATOM   3582 C  CG  . GLN   C 1 51  ? -39.926 -2.314  45.802  1.00 35.71 ? 144 GLN   C CG  1 
ATOM   3583 C  CD  . GLN   C 1 51  ? -41.418 -2.502  45.734  1.00 36.74 ? 144 GLN   C CD  1 
ATOM   3584 O  OE1 . GLN   C 1 51  ? -42.141 -1.622  45.278  1.00 36.95 ? 144 GLN   C OE1 1 
ATOM   3585 N  NE2 . GLN   C 1 51  ? -41.884 -3.647  46.213  1.00 37.08 ? 144 GLN   C NE2 1 
ATOM   3586 N  N   . LEU   C 1 52  ? -36.861 0.079   43.174  1.00 34.59 ? 145 LEU   C N   1 
ATOM   3587 C  CA  . LEU   C 1 52  ? -36.573 1.013   42.057  1.00 35.84 ? 145 LEU   C CA  1 
ATOM   3588 C  C   . LEU   C 1 52  ? -37.545 0.705   40.913  1.00 37.69 ? 145 LEU   C C   1 
ATOM   3589 O  O   . LEU   C 1 52  ? -37.569 -0.449  40.453  1.00 37.40 ? 145 LEU   C O   1 
ATOM   3590 C  CB  . LEU   C 1 52  ? -35.119 0.844   41.611  1.00 35.15 ? 145 LEU   C CB  1 
ATOM   3591 C  CG  . LEU   C 1 52  ? -34.071 0.792   42.722  1.00 34.22 ? 145 LEU   C CG  1 
ATOM   3592 C  CD1 . LEU   C 1 52  ? -32.690 0.740   42.129  1.00 34.25 ? 145 LEU   C CD1 1 
ATOM   3593 C  CD2 . LEU   C 1 52  ? -34.162 1.977   43.672  1.00 33.35 ? 145 LEU   C CD2 1 
ATOM   3594 N  N   . TRP   C 1 53  ? -38.333 1.696   40.496  1.00 39.66 ? 146 TRP   C N   1 
ATOM   3595 C  CA  . TRP   C 1 53  ? -39.256 1.592   39.335  1.00 42.47 ? 146 TRP   C CA  1 
ATOM   3596 C  C   . TRP   C 1 53  ? -38.745 2.521   38.229  1.00 43.98 ? 146 TRP   C C   1 
ATOM   3597 O  O   . TRP   C 1 53  ? -38.475 3.704   38.528  1.00 44.06 ? 146 TRP   C O   1 
ATOM   3598 C  CB  . TRP   C 1 53  ? -40.700 1.928   39.730  1.00 43.19 ? 146 TRP   C CB  1 
ATOM   3599 C  CG  . TRP   C 1 53  ? -41.313 0.961   40.696  1.00 43.34 ? 146 TRP   C CG  1 
ATOM   3600 C  CD1 . TRP   C 1 53  ? -40.976 0.787   42.005  1.00 41.94 ? 146 TRP   C CD1 1 
ATOM   3601 C  CD2 . TRP   C 1 53  ? -42.401 0.051   40.446  1.00 44.34 ? 146 TRP   C CD2 1 
ATOM   3602 N  NE1 . TRP   C 1 53  ? -41.754 -0.181  42.577  1.00 42.42 ? 146 TRP   C NE1 1 
ATOM   3603 C  CE2 . TRP   C 1 53  ? -42.637 -0.656  41.646  1.00 44.06 ? 146 TRP   C CE2 1 
ATOM   3604 C  CE3 . TRP   C 1 53  ? -43.222 -0.213  39.344  1.00 46.58 ? 146 TRP   C CE3 1 
ATOM   3605 C  CZ2 . TRP   C 1 53  ? -43.620 -1.638  41.760  1.00 45.00 ? 146 TRP   C CZ2 1 
ATOM   3606 C  CZ3 . TRP   C 1 53  ? -44.191 -1.191  39.451  1.00 47.47 ? 146 TRP   C CZ3 1 
ATOM   3607 C  CH2 . TRP   C 1 53  ? -44.401 -1.877  40.650  1.00 46.42 ? 146 TRP   C CH2 1 
ATOM   3608 N  N   . VAL   C 1 54  ? -38.624 1.996   37.008  1.00 45.85 ? 147 VAL   C N   1 
ATOM   3609 C  CA  . VAL   C 1 54  ? -38.205 2.765   35.795  1.00 47.59 ? 147 VAL   C CA  1 
ATOM   3610 C  C   . VAL   C 1 54  ? -39.203 2.478   34.672  1.00 49.73 ? 147 VAL   C C   1 
ATOM   3611 O  O   . VAL   C 1 54  ? -39.737 1.334   34.626  1.00 49.92 ? 147 VAL   C O   1 
ATOM   3612 C  CB  . VAL   C 1 54  ? -36.763 2.428   35.370  1.00 47.55 ? 147 VAL   C CB  1 
ATOM   3613 C  CG1 . VAL   C 1 54  ? -35.752 3.018   36.331  1.00 46.68 ? 147 VAL   C CG1 1 
ATOM   3614 C  CG2 . VAL   C 1 54  ? -36.544 0.932   35.228  1.00 47.57 ? 147 VAL   C CG2 1 
ATOM   3615 N  N   . ASP   C 1 55  ? -39.472 3.488   33.842  1.00 51.14 ? 148 ASP   C N   1 
ATOM   3616 C  CA  . ASP   C 1 55  ? -40.316 3.377   32.621  1.00 54.41 ? 148 ASP   C CA  1 
ATOM   3617 C  C   . ASP   C 1 55  ? -39.488 2.716   31.517  1.00 55.90 ? 148 ASP   C C   1 
ATOM   3618 O  O   . ASP   C 1 55  ? -40.071 1.991   30.692  1.00 57.90 ? 148 ASP   C O   1 
ATOM   3619 C  CB  . ASP   C 1 55  ? -40.830 4.746   32.165  1.00 55.40 ? 148 ASP   C CB  1 
ATOM   3620 C  CG  . ASP   C 1 55  ? -41.842 5.376   33.107  1.00 54.44 ? 148 ASP   C CG  1 
ATOM   3621 O  OD1 . ASP   C 1 55  ? -42.508 4.618   33.848  1.00 53.54 ? 148 ASP   C OD1 1 
ATOM   3622 O  OD2 . ASP   C 1 55  ? -41.969 6.619   33.080  1.00 54.69 ? 148 ASP   C OD2 1 
ATOM   3623 N  N   . SER   C 1 56  ? -38.174 2.959   31.515  1.00 56.18 ? 149 SER   C N   1 
ATOM   3624 C  CA  . SER   C 1 56  ? -37.215 2.397   30.531  1.00 57.73 ? 149 SER   C CA  1 
ATOM   3625 C  C   . SER   C 1 56  ? -35.941 1.956   31.253  1.00 56.29 ? 149 SER   C C   1 
ATOM   3626 O  O   . SER   C 1 56  ? -35.518 2.654   32.205  1.00 55.37 ? 149 SER   C O   1 
ATOM   3627 C  CB  . SER   C 1 56  ? -36.939 3.382   29.423  1.00 59.99 ? 149 SER   C CB  1 
ATOM   3628 O  OG  . SER   C 1 56  ? -38.145 3.709   28.754  1.00 62.04 ? 149 SER   C OG  1 
ATOM   3629 N  N   . THR   C 1 57  ? -35.360 0.843   30.806  1.00 56.22 ? 150 THR   C N   1 
ATOM   3630 C  CA  . THR   C 1 57  ? -34.153 0.211   31.397  1.00 54.73 ? 150 THR   C CA  1 
ATOM   3631 C  C   . THR   C 1 57  ? -32.944 1.117   31.185  1.00 54.37 ? 150 THR   C C   1 
ATOM   3632 O  O   . THR   C 1 57  ? -32.529 1.338   30.056  1.00 54.99 ? 150 THR   C O   1 
ATOM   3633 C  CB  . THR   C 1 57  ? -33.920 -1.179  30.796  1.00 55.96 ? 150 THR   C CB  1 
ATOM   3634 O  OG1 . THR   C 1 57  ? -35.152 -1.889  30.892  1.00 56.48 ? 150 THR   C OG1 1 
ATOM   3635 C  CG2 . THR   C 1 57  ? -32.825 -1.952  31.499  1.00 54.89 ? 150 THR   C CG2 1 
ATOM   3636 N  N   . PRO   C 1 58  ? -32.342 1.673   32.261  1.00 52.21 ? 151 PRO   C N   1 
ATOM   3637 C  CA  . PRO   C 1 58  ? -31.086 2.413   32.141  1.00 51.97 ? 151 PRO   C CA  1 
ATOM   3638 C  C   . PRO   C 1 58  ? -29.974 1.571   31.517  1.00 51.75 ? 151 PRO   C C   1 
ATOM   3639 O  O   . PRO   C 1 58  ? -30.030 0.342   31.534  1.00 51.87 ? 151 PRO   C O   1 
ATOM   3640 C  CB  . PRO   C 1 58  ? -30.737 2.763   33.594  1.00 49.77 ? 151 PRO   C CB  1 
ATOM   3641 C  CG  . PRO   C 1 58  ? -32.050 2.715   34.323  1.00 49.62 ? 151 PRO   C CG  1 
ATOM   3642 C  CD  . PRO   C 1 58  ? -32.845 1.626   33.644  1.00 50.64 ? 151 PRO   C CD  1 
ATOM   3643 N  N   . PRO   C 1 59  ? -28.926 2.203   30.949  1.00 51.89 ? 152 PRO   C N   1 
ATOM   3644 C  CA  . PRO   C 1 59  ? -27.859 1.462   30.275  1.00 52.63 ? 152 PRO   C CA  1 
ATOM   3645 C  C   . PRO   C 1 59  ? -27.036 0.604   31.237  1.00 50.69 ? 152 PRO   C C   1 
ATOM   3646 O  O   . PRO   C 1 59  ? -27.017 0.861   32.442  1.00 48.36 ? 152 PRO   C O   1 
ATOM   3647 C  CB  . PRO   C 1 59  ? -27.013 2.569   29.627  1.00 53.70 ? 152 PRO   C CB  1 
ATOM   3648 C  CG  . PRO   C 1 59  ? -27.260 3.784   30.489  1.00 53.00 ? 152 PRO   C CG  1 
ATOM   3649 C  CD  . PRO   C 1 59  ? -28.704 3.656   30.924  1.00 52.36 ? 152 PRO   C CD  1 
ATOM   3650 N  N   . PRO   C 1 60  ? -26.333 -0.442  30.742  1.00 51.41 ? 153 PRO   C N   1 
ATOM   3651 C  CA  . PRO   C 1 60  ? -25.415 -1.213  31.578  1.00 50.52 ? 153 PRO   C CA  1 
ATOM   3652 C  C   . PRO   C 1 60  ? -24.389 -0.286  32.253  1.00 48.88 ? 153 PRO   C C   1 
ATOM   3653 O  O   . PRO   C 1 60  ? -23.975 0.670   31.632  1.00 49.04 ? 153 PRO   C O   1 
ATOM   3654 C  CB  . PRO   C 1 60  ? -24.724 -2.179  30.600  1.00 52.49 ? 153 PRO   C CB  1 
ATOM   3655 C  CG  . PRO   C 1 60  ? -25.673 -2.279  29.420  1.00 54.54 ? 153 PRO   C CG  1 
ATOM   3656 C  CD  . PRO   C 1 60  ? -26.373 -0.936  29.357  1.00 54.35 ? 153 PRO   C CD  1 
ATOM   3657 N  N   . GLY   C 1 61  ? -24.030 -0.578  33.507  1.00 47.26 ? 154 GLY   C N   1 
ATOM   3658 C  CA  . GLY   C 1 61  ? -23.060 0.207   34.293  1.00 45.50 ? 154 GLY   C CA  1 
ATOM   3659 C  C   . GLY   C 1 61  ? -23.723 1.327   35.066  1.00 44.09 ? 154 GLY   C C   1 
ATOM   3660 O  O   . GLY   C 1 61  ? -23.004 2.006   35.817  1.00 44.43 ? 154 GLY   C O   1 
ATOM   3661 N  N   . THR   C 1 62  ? -25.039 1.502   34.916  1.00 42.89 ? 155 THR   C N   1 
ATOM   3662 C  CA  . THR   C 1 62  ? -25.863 2.374   35.792  1.00 41.49 ? 155 THR   C CA  1 
ATOM   3663 C  C   . THR   C 1 62  ? -25.653 1.960   37.249  1.00 39.62 ? 155 THR   C C   1 
ATOM   3664 O  O   . THR   C 1 62  ? -25.568 0.741   37.525  1.00 38.05 ? 155 THR   C O   1 
ATOM   3665 C  CB  . THR   C 1 62  ? -27.350 2.328   35.423  1.00 41.88 ? 155 THR   C CB  1 
ATOM   3666 O  OG1 . THR   C 1 62  ? -27.459 2.806   34.079  1.00 43.21 ? 155 THR   C OG1 1 
ATOM   3667 C  CG2 . THR   C 1 62  ? -28.204 3.185   36.334  1.00 40.63 ? 155 THR   C CG2 1 
ATOM   3668 N  N   . ARG   C 1 63  ? -25.578 2.938   38.153  1.00 38.14 ? 156 ARG   C N   1 
ATOM   3669 C  CA  . ARG   C 1 63  ? -25.320 2.683   39.590  1.00 36.70 ? 156 ARG   C CA  1 
ATOM   3670 C  C   . ARG   C 1 63  ? -26.426 3.328   40.427  1.00 35.78 ? 156 ARG   C C   1 
ATOM   3671 O  O   . ARG   C 1 63  ? -27.061 4.288   39.952  1.00 36.62 ? 156 ARG   C O   1 
ATOM   3672 C  CB  . ARG   C 1 63  ? -23.895 3.128   39.939  1.00 36.65 ? 156 ARG   C CB  1 
ATOM   3673 C  CG  . ARG   C 1 63  ? -22.849 2.070   39.623  1.00 37.12 ? 156 ARG   C CG  1 
ATOM   3674 C  CD  . ARG   C 1 63  ? -21.495 2.651   39.259  1.00 37.76 ? 156 ARG   C CD  1 
ATOM   3675 N  NE  . ARG   C 1 63  ? -20.910 3.587   40.223  1.00 37.51 ? 156 ARG   C NE  1 
ATOM   3676 C  CZ  . ARG   C 1 63  ? -20.036 3.281   41.185  1.00 36.33 ? 156 ARG   C CZ  1 
ATOM   3677 N  NH1 . ARG   C 1 63  ? -19.661 2.034   41.391  1.00 36.57 ? 156 ARG   C NH1 1 
ATOM   3678 N  NH2 . ARG   C 1 63  ? -19.550 4.227   41.965  1.00 36.37 ? 156 ARG   C NH2 1 
ATOM   3679 N  N   . VAL   C 1 64  ? -26.650 2.779   41.626  1.00 35.06 ? 157 VAL   C N   1 
ATOM   3680 C  CA  . VAL   C 1 64  ? -27.638 3.279   42.627  1.00 33.26 ? 157 VAL   C CA  1 
ATOM   3681 C  C   . VAL   C 1 64  ? -26.899 3.615   43.921  1.00 32.01 ? 157 VAL   C C   1 
ATOM   3682 O  O   . VAL   C 1 64  ? -26.355 2.696   44.551  1.00 31.74 ? 157 VAL   C O   1 
ATOM   3683 C  CB  . VAL   C 1 64  ? -28.751 2.251   42.873  1.00 33.34 ? 157 VAL   C CB  1 
ATOM   3684 C  CG1 . VAL   C 1 64  ? -29.883 2.856   43.693  1.00 32.60 ? 157 VAL   C CG1 1 
ATOM   3685 C  CG2 . VAL   C 1 64  ? -29.266 1.703   41.564  1.00 34.70 ? 157 VAL   C CG2 1 
ATOM   3686 N  N   . ARG   C 1 65  ? -26.882 4.897   44.280  1.00 30.96 ? 158 ARG   C N   1 
ATOM   3687 C  CA  . ARG   C 1 65  ? -26.275 5.432   45.516  1.00 29.73 ? 158 ARG   C CA  1 
ATOM   3688 C  C   . ARG   C 1 65  ? -27.386 5.786   46.513  1.00 28.99 ? 158 ARG   C C   1 
ATOM   3689 O  O   . ARG   C 1 65  ? -28.461 6.281   46.081  1.00 28.51 ? 158 ARG   C O   1 
ATOM   3690 C  CB  . ARG   C 1 65  ? -25.430 6.656   45.166  1.00 30.23 ? 158 ARG   C CB  1 
ATOM   3691 C  CG  . ARG   C 1 65  ? -24.694 7.273   46.343  1.00 29.69 ? 158 ARG   C CG  1 
ATOM   3692 C  CD  . ARG   C 1 65  ? -23.889 8.481   45.894  1.00 30.12 ? 158 ARG   C CD  1 
ATOM   3693 N  NE  . ARG   C 1 65  ? -23.024 8.176   44.766  1.00 31.01 ? 158 ARG   C NE  1 
ATOM   3694 C  CZ  . ARG   C 1 65  ? -21.815 7.616   44.820  1.00 30.58 ? 158 ARG   C CZ  1 
ATOM   3695 N  NH1 . ARG   C 1 65  ? -21.292 7.233   45.964  1.00 30.23 ? 158 ARG   C NH1 1 
ATOM   3696 N  NH2 . ARG   C 1 65  ? -21.131 7.415   43.707  1.00 31.75 ? 158 ARG   C NH2 1 
ATOM   3697 N  N   . ALA   C 1 66  ? -27.132 5.485   47.789  1.00 28.44 ? 159 ALA   C N   1 
ATOM   3698 C  CA  . ALA   C 1 66  ? -27.923 5.910   48.963  1.00 28.89 ? 159 ALA   C CA  1 
ATOM   3699 C  C   . ALA   C 1 66  ? -27.034 6.787   49.844  1.00 28.91 ? 159 ALA   C C   1 
ATOM   3700 O  O   . ALA   C 1 66  ? -25.849 6.435   50.053  1.00 29.39 ? 159 ALA   C O   1 
ATOM   3701 C  CB  . ALA   C 1 66  ? -28.436 4.710   49.716  1.00 27.93 ? 159 ALA   C CB  1 
ATOM   3702 N  N   . MET   C 1 67  ? -27.587 7.894   50.335  1.00 29.93 ? 160 MET   C N   1 
ATOM   3703 C  CA  . MET   C 1 67  ? -26.896 8.867   51.220  1.00 30.44 ? 160 MET   C CA  1 
ATOM   3704 C  C   . MET   C 1 67  ? -27.928 9.450   52.189  1.00 30.07 ? 160 MET   C C   1 
ATOM   3705 O  O   . MET   C 1 67  ? -29.065 9.737   51.763  1.00 30.16 ? 160 MET   C O   1 
ATOM   3706 C  CB  . MET   C 1 67  ? -26.271 9.990   50.390  1.00 32.73 ? 160 MET   C CB  1 
ATOM   3707 C  CG  . MET   C 1 67  ? -25.604 11.067  51.224  1.00 34.22 ? 160 MET   C CG  1 
ATOM   3708 S  SD  . MET   C 1 67  ? -24.982 12.492  50.270  1.00 38.84 ? 160 MET   C SD  1 
ATOM   3709 C  CE  . MET   C 1 67  ? -23.747 11.725  49.219  1.00 38.18 ? 160 MET   C CE  1 
ATOM   3710 N  N   . ALA   C 1 68  ? -27.568 9.587   53.460  1.00 29.41 ? 161 ALA   C N   1 
ATOM   3711 C  CA  . ALA   C 1 68  ? -28.414 10.203  54.499  1.00 29.71 ? 161 ALA   C CA  1 
ATOM   3712 C  C   . ALA   C 1 68  ? -27.983 11.663  54.665  1.00 31.35 ? 161 ALA   C C   1 
ATOM   3713 O  O   . ALA   C 1 68  ? -26.775 11.944  54.592  1.00 30.52 ? 161 ALA   C O   1 
ATOM   3714 C  CB  . ALA   C 1 68  ? -28.299 9.462   55.794  1.00 29.47 ? 161 ALA   C CB  1 
ATOM   3715 N  N   . ILE   C 1 69  ? -28.959 12.550  54.826  1.00 33.27 ? 162 ILE   C N   1 
ATOM   3716 C  CA  . ILE   C 1 69  ? -28.748 13.945  55.299  1.00 35.90 ? 162 ILE   C CA  1 
ATOM   3717 C  C   . ILE   C 1 69  ? -29.780 14.192  56.401  1.00 35.99 ? 162 ILE   C C   1 
ATOM   3718 O  O   . ILE   C 1 69  ? -30.791 13.467  56.427  1.00 35.71 ? 162 ILE   C O   1 
ATOM   3719 C  CB  . ILE   C 1 69  ? -28.857 14.961  54.148  1.00 37.09 ? 162 ILE   C CB  1 
ATOM   3720 C  CG1 . ILE   C 1 69  ? -30.257 15.006  53.529  1.00 38.27 ? 162 ILE   C CG1 1 
ATOM   3721 C  CG2 . ILE   C 1 69  ? -27.800 14.682  53.098  1.00 36.93 ? 162 ILE   C CG2 1 
ATOM   3722 C  CD1 . ILE   C 1 69  ? -30.437 16.131  52.541  1.00 39.78 ? 162 ILE   C CD1 1 
ATOM   3723 N  N   . TYR   C 1 70  ? -29.508 15.155  57.283  1.00 37.21 ? 163 TYR   C N   1 
ATOM   3724 C  CA  . TYR   C 1 70  ? -30.473 15.656  58.294  1.00 38.40 ? 163 TYR   C CA  1 
ATOM   3725 C  C   . TYR   C 1 70  ? -31.529 16.474  57.560  1.00 39.14 ? 163 TYR   C C   1 
ATOM   3726 O  O   . TYR   C 1 70  ? -31.181 17.176  56.590  1.00 39.34 ? 163 TYR   C O   1 
ATOM   3727 C  CB  . TYR   C 1 70  ? -29.756 16.430  59.396  1.00 39.37 ? 163 TYR   C CB  1 
ATOM   3728 C  CG  . TYR   C 1 70  ? -28.955 15.539  60.306  1.00 38.78 ? 163 TYR   C CG  1 
ATOM   3729 C  CD1 . TYR   C 1 70  ? -29.595 14.600  61.102  1.00 37.96 ? 163 TYR   C CD1 1 
ATOM   3730 C  CD2 . TYR   C 1 70  ? -27.571 15.594  60.348  1.00 38.84 ? 163 TYR   C CD2 1 
ATOM   3731 C  CE1 . TYR   C 1 70  ? -28.887 13.762  61.945  1.00 37.17 ? 163 TYR   C CE1 1 
ATOM   3732 C  CE2 . TYR   C 1 70  ? -26.845 14.755  61.176  1.00 37.99 ? 163 TYR   C CE2 1 
ATOM   3733 C  CZ  . TYR   C 1 70  ? -27.507 13.834  61.978  1.00 37.39 ? 163 TYR   C CZ  1 
ATOM   3734 O  OH  . TYR   C 1 70  ? -26.833 12.991  62.816  1.00 36.75 ? 163 TYR   C OH  1 
ATOM   3735 N  N   . LYS   C 1 71  ? -32.784 16.337  57.989  1.00 39.91 ? 164 LYS   C N   1 
ATOM   3736 C  CA  . LYS   C 1 71  ? -33.953 16.943  57.310  1.00 41.18 ? 164 LYS   C CA  1 
ATOM   3737 C  C   . LYS   C 1 71  ? -34.002 18.437  57.648  1.00 43.83 ? 164 LYS   C C   1 
ATOM   3738 O  O   . LYS   C 1 71  ? -34.325 19.225  56.751  1.00 46.02 ? 164 LYS   C O   1 
ATOM   3739 C  CB  . LYS   C 1 71  ? -35.236 16.237  57.745  1.00 40.11 ? 164 LYS   C CB  1 
ATOM   3740 C  CG  . LYS   C 1 71  ? -36.495 16.686  57.020  1.00 41.35 ? 164 LYS   C CG  1 
ATOM   3741 C  CD  . LYS   C 1 71  ? -37.738 16.166  57.667  1.00 40.57 ? 164 LYS   C CD  1 
ATOM   3742 C  CE  . LYS   C 1 71  ? -38.981 16.569  56.916  1.00 41.76 ? 164 LYS   C CE  1 
ATOM   3743 N  NZ  . LYS   C 1 71  ? -40.207 16.187  57.656  1.00 41.67 ? 164 LYS   C NZ  1 
ATOM   3744 N  N   . GLN   C 1 72  ? -33.703 18.786  58.903  1.00 45.49 ? 165 GLN   C N   1 
ATOM   3745 C  CA  . GLN   C 1 72  ? -33.830 20.158  59.463  1.00 47.79 ? 165 GLN   C CA  1 
ATOM   3746 C  C   . GLN   C 1 72  ? -32.719 21.040  58.887  1.00 49.54 ? 165 GLN   C C   1 
ATOM   3747 O  O   . GLN   C 1 72  ? -31.575 20.570  58.808  1.00 49.53 ? 165 GLN   C O   1 
ATOM   3748 C  CB  . GLN   C 1 72  ? -33.768 20.102  60.988  1.00 48.34 ? 165 GLN   C CB  1 
ATOM   3749 C  CG  . GLN   C 1 72  ? -34.966 19.404  61.620  1.00 48.39 ? 165 GLN   C CG  1 
ATOM   3750 C  CD  . GLN   C 1 72  ? -34.667 18.906  63.014  1.00 49.03 ? 165 GLN   C CD  1 
ATOM   3751 O  OE1 . GLN   C 1 72  ? -33.659 18.250  63.253  1.00 50.11 ? 165 GLN   C OE1 1 
ATOM   3752 N  NE2 . GLN   C 1 72  ? -35.551 19.200  63.952  1.00 50.68 ? 165 GLN   C NE2 1 
ATOM   3753 N  N   . SER   C 1 73  ? -33.049 22.289  58.546  1.00 52.63 ? 166 SER   C N   1 
ATOM   3754 C  CA  A SER   C 1 73  ? -32.143 23.238  57.846  0.40 54.04 ? 166 SER   C CA  1 
ATOM   3755 C  CA  B SER   C 1 73  ? -32.136 23.231  57.846  0.60 54.02 ? 166 SER   C CA  1 
ATOM   3756 C  C   . SER   C 1 73  ? -30.944 23.590  58.733  1.00 55.18 ? 166 SER   C C   1 
ATOM   3757 O  O   . SER   C 1 73  ? -29.856 23.811  58.169  1.00 55.92 ? 166 SER   C O   1 
ATOM   3758 C  CB  A SER   C 1 73  ? -32.882 24.469  57.392  0.40 55.97 ? 166 SER   C CB  1 
ATOM   3759 C  CB  B SER   C 1 73  ? -32.857 24.457  57.364  0.60 55.88 ? 166 SER   C CB  1 
ATOM   3760 O  OG  A SER   C 1 73  ? -33.538 25.095  58.486  0.40 57.19 ? 166 SER   C OG  1 
ATOM   3761 O  OG  B SER   C 1 73  ? -33.117 24.343  55.977  0.60 55.27 ? 166 SER   C OG  1 
ATOM   3762 N  N   . GLN   C 1 74  ? -31.140 23.618  60.055  1.00 55.97 ? 167 GLN   C N   1 
ATOM   3763 C  CA  . GLN   C 1 74  ? -30.080 24.012  61.025  1.00 57.06 ? 167 GLN   C CA  1 
ATOM   3764 C  C   . GLN   C 1 74  ? -29.082 22.864  61.247  1.00 55.06 ? 167 GLN   C C   1 
ATOM   3765 O  O   . GLN   C 1 74  ? -28.033 23.124  61.849  1.00 56.53 ? 167 GLN   C O   1 
ATOM   3766 C  CB  . GLN   C 1 74  ? -30.687 24.502  62.343  1.00 58.96 ? 167 GLN   C CB  1 
ATOM   3767 C  CG  . GLN   C 1 74  ? -31.460 23.445  63.119  1.00 57.83 ? 167 GLN   C CG  1 
ATOM   3768 C  CD  . GLN   C 1 74  ? -32.946 23.476  62.851  1.00 58.32 ? 167 GLN   C CD  1 
ATOM   3769 O  OE1 . GLN   C 1 74  ? -33.392 23.705  61.727  1.00 58.88 ? 167 GLN   C OE1 1 
ATOM   3770 N  NE2 . GLN   C 1 74  ? -33.728 23.267  63.901  1.00 58.37 ? 167 GLN   C NE2 1 
ATOM   3771 N  N   . HIS   C 1 75  ? -29.376 21.646  60.779  1.00 53.36 ? 168 HIS   C N   1 
ATOM   3772 C  CA  . HIS   C 1 75  ? -28.520 20.441  60.976  1.00 51.34 ? 168 HIS   C CA  1 
ATOM   3773 C  C   . HIS   C 1 75  ? -28.007 19.890  59.641  1.00 49.73 ? 168 HIS   C C   1 
ATOM   3774 O  O   . HIS   C 1 75  ? -27.261 18.891  59.668  1.00 49.54 ? 168 HIS   C O   1 
ATOM   3775 C  CB  . HIS   C 1 75  ? -29.292 19.360  61.735  1.00 50.32 ? 168 HIS   C CB  1 
ATOM   3776 C  CG  . HIS   C 1 75  ? -29.679 19.751  63.121  1.00 52.00 ? 168 HIS   C CG  1 
ATOM   3777 N  ND1 . HIS   C 1 75  ? -28.752 20.164  64.060  1.00 52.87 ? 168 HIS   C ND1 1 
ATOM   3778 C  CD2 . HIS   C 1 75  ? -30.880 19.765  63.741  1.00 52.38 ? 168 HIS   C CD2 1 
ATOM   3779 C  CE1 . HIS   C 1 75  ? -29.371 20.432  65.194  1.00 54.35 ? 168 HIS   C CE1 1 
ATOM   3780 N  NE2 . HIS   C 1 75  ? -30.677 20.190  65.024  1.00 54.00 ? 168 HIS   C NE2 1 
ATOM   3781 N  N   . MET   C 1 76  ? -28.355 20.534  58.524  1.00 49.85 ? 169 MET   C N   1 
ATOM   3782 C  CA  . MET   C 1 76  ? -28.247 19.951  57.161  1.00 48.61 ? 169 MET   C CA  1 
ATOM   3783 C  C   . MET   C 1 76  ? -26.778 19.852  56.721  1.00 47.19 ? 169 MET   C C   1 
ATOM   3784 O  O   . MET   C 1 76  ? -26.466 18.934  55.942  1.00 44.67 ? 169 MET   C O   1 
ATOM   3785 C  CB  . MET   C 1 76  ? -29.038 20.781  56.151  1.00 50.86 ? 169 MET   C CB  1 
ATOM   3786 C  CG  . MET   C 1 76  ? -29.351 20.012  54.889  1.00 50.82 ? 169 MET   C CG  1 
ATOM   3787 S  SD  . MET   C 1 76  ? -31.012 20.118  54.212  1.00 53.57 ? 169 MET   C SD  1 
ATOM   3788 C  CE  . MET   C 1 76  ? -31.553 21.764  54.664  1.00 54.59 ? 169 MET   C CE  1 
ATOM   3789 N  N   . THR   C 1 77  ? -25.918 20.757  57.195  1.00 47.73 ? 170 THR   C N   1 
ATOM   3790 C  CA  . THR   C 1 77  ? -24.466 20.804  56.865  1.00 47.67 ? 170 THR   C CA  1 
ATOM   3791 C  C   . THR   C 1 77  ? -23.688 19.785  57.710  1.00 46.15 ? 170 THR   C C   1 
ATOM   3792 O  O   . THR   C 1 77  ? -22.499 19.614  57.437  1.00 46.37 ? 170 THR   C O   1 
ATOM   3793 C  CB  . THR   C 1 77  ? -23.864 22.198  57.083  1.00 50.30 ? 170 THR   C CB  1 
ATOM   3794 O  OG1 . THR   C 1 77  ? -23.796 22.414  58.493  1.00 51.21 ? 170 THR   C OG1 1 
ATOM   3795 C  CG2 . THR   C 1 77  ? -24.652 23.297  56.406  1.00 51.76 ? 170 THR   C CG2 1 
ATOM   3796 N  N   . GLU   C 1 78  ? -24.317 19.164  58.710  1.00 44.80 ? 171 GLU   C N   1 
ATOM   3797 C  CA  . GLU   C 1 78  ? -23.685 18.109  59.546  1.00 43.46 ? 171 GLU   C CA  1 
ATOM   3798 C  C   . GLU   C 1 78  ? -23.762 16.774  58.791  1.00 40.49 ? 171 GLU   C C   1 
ATOM   3799 O  O   . GLU   C 1 78  ? -24.845 16.449  58.277  1.00 38.67 ? 171 GLU   C O   1 
ATOM   3800 C  CB  . GLU   C 1 78  ? -24.355 18.034  60.919  1.00 44.12 ? 171 GLU   C CB  1 
ATOM   3801 C  CG  . GLU   C 1 78  ? -23.680 17.049  61.854  1.00 44.43 ? 171 GLU   C CG  1 
ATOM   3802 C  CD  . GLU   C 1 78  ? -24.092 17.135  63.312  1.00 45.41 ? 171 GLU   C CD  1 
ATOM   3803 O  OE1 . GLU   C 1 78  ? -24.106 18.259  63.862  1.00 47.49 ? 171 GLU   C OE1 1 
ATOM   3804 O  OE2 . GLU   C 1 78  ? -24.386 16.074  63.904  1.00 44.44 ? 171 GLU   C OE2 1 
ATOM   3805 N  N   . VAL   C 1 79  ? -22.646 16.036  58.717  1.00 39.14 ? 172 VAL   C N   1 
ATOM   3806 C  CA  . VAL   C 1 79  ? -22.595 14.682  58.082  1.00 37.10 ? 172 VAL   C CA  1 
ATOM   3807 C  C   . VAL   C 1 79  ? -23.334 13.695  58.984  1.00 35.84 ? 172 VAL   C C   1 
ATOM   3808 O  O   . VAL   C 1 79  ? -23.038 13.670  60.192  1.00 35.68 ? 172 VAL   C O   1 
ATOM   3809 C  CB  . VAL   C 1 79  ? -21.155 14.206  57.814  1.00 36.74 ? 172 VAL   C CB  1 
ATOM   3810 C  CG1 . VAL   C 1 79  ? -21.134 12.762  57.310  1.00 34.97 ? 172 VAL   C CG1 1 
ATOM   3811 C  CG2 . VAL   C 1 79  ? -20.426 15.137  56.860  1.00 37.10 ? 172 VAL   C CG2 1 
ATOM   3812 N  N   . VAL   C 1 80  ? -24.235 12.891  58.409  1.00 35.01 ? 173 VAL   C N   1 
ATOM   3813 C  CA  . VAL   C 1 80  ? -24.946 11.821  59.162  1.00 34.18 ? 173 VAL   C CA  1 
ATOM   3814 C  C   . VAL   C 1 80  ? -23.997 10.632  59.304  1.00 33.87 ? 173 VAL   C C   1 
ATOM   3815 O  O   . VAL   C 1 80  ? -23.593 10.087  58.266  1.00 33.01 ? 173 VAL   C O   1 
ATOM   3816 C  CB  . VAL   C 1 80  ? -26.272 11.401  58.506  1.00 32.93 ? 173 VAL   C CB  1 
ATOM   3817 C  CG1 . VAL   C 1 80  ? -26.962 10.318  59.313  1.00 32.67 ? 173 VAL   C CG1 1 
ATOM   3818 C  CG2 . VAL   C 1 80  ? -27.206 12.574  58.320  1.00 33.54 ? 173 VAL   C CG2 1 
ATOM   3819 N  N   . ARG   C 1 81  ? -23.692 10.261  60.548  1.00 35.43 ? 174 ARG   C N   1 
ATOM   3820 C  CA  . ARG   C 1 81  ? -22.829 9.112   60.893  1.00 36.66 ? 174 ARG   C CA  1 
ATOM   3821 C  C   . ARG   C 1 81  ? -23.407 8.387   62.105  1.00 36.24 ? 174 ARG   C C   1 
ATOM   3822 O  O   . ARG   C 1 81  ? -24.264 8.968   62.822  1.00 35.34 ? 174 ARG   C O   1 
ATOM   3823 C  CB  . ARG   C 1 81  ? -21.394 9.565   61.170  1.00 39.45 ? 174 ARG   C CB  1 
ATOM   3824 C  CG  . ARG   C 1 81  ? -21.268 10.725  62.143  1.00 42.44 ? 174 ARG   C CG  1 
ATOM   3825 C  CD  . ARG   C 1 81  ? -19.835 11.102  62.501  1.00 45.50 ? 174 ARG   C CD  1 
ATOM   3826 N  NE  . ARG   C 1 81  ? -19.097 11.856  61.480  1.00 46.80 ? 174 ARG   C NE  1 
ATOM   3827 C  CZ  . ARG   C 1 81  ? -18.258 11.329  60.583  1.00 47.60 ? 174 ARG   C CZ  1 
ATOM   3828 N  NH1 . ARG   C 1 81  ? -18.012 10.032  60.565  1.00 47.79 ? 174 ARG   C NH1 1 
ATOM   3829 N  NH2 . ARG   C 1 81  ? -17.636 12.101  59.710  1.00 48.73 ? 174 ARG   C NH2 1 
ATOM   3830 N  N   . ARG   C 1 82  ? -22.908 7.176   62.341  1.00 35.64 ? 175 ARG   C N   1 
ATOM   3831 C  CA  . ARG   C 1 82  ? -23.238 6.369   63.539  1.00 36.07 ? 175 ARG   C CA  1 
ATOM   3832 C  C   . ARG   C 1 82  ? -22.686 7.061   64.786  1.00 37.23 ? 175 ARG   C C   1 
ATOM   3833 O  O   . ARG   C 1 82  ? -21.681 7.823   64.674  1.00 36.01 ? 175 ARG   C O   1 
ATOM   3834 C  CB  . ARG   C 1 82  ? -22.665 4.958   63.410  1.00 36.15 ? 175 ARG   C CB  1 
ATOM   3835 C  CG  . ARG   C 1 82  ? -23.204 4.196   62.207  1.00 35.47 ? 175 ARG   C CG  1 
ATOM   3836 C  CD  . ARG   C 1 82  ? -22.540 2.845   62.095  1.00 36.11 ? 175 ARG   C CD  1 
ATOM   3837 N  NE  . ARG   C 1 82  ? -23.206 1.852   62.905  1.00 37.73 ? 175 ARG   C NE  1 
ATOM   3838 C  CZ  . ARG   C 1 82  ? -22.735 0.626   63.120  1.00 38.39 ? 175 ARG   C CZ  1 
ATOM   3839 N  NH1 . ARG   C 1 82  ? -21.583 0.245   62.579  1.00 37.62 ? 175 ARG   C NH1 1 
ATOM   3840 N  NH2 . ARG   C 1 82  ? -23.423 -0.207  63.888  1.00 38.79 ? 175 ARG   C NH2 1 
ATOM   3841 N  N   . CYS   C 1 83  ? -23.290 6.772   65.936  1.00 37.75 ? 176 CYS   C N   1 
ATOM   3842 C  CA  . CYS   C 1 83  ? -22.810 7.217   67.268  1.00 39.42 ? 176 CYS   C CA  1 
ATOM   3843 C  C   . CYS   C 1 83  ? -21.521 6.460   67.589  1.00 39.48 ? 176 CYS   C C   1 
ATOM   3844 O  O   . CYS   C 1 83  ? -21.267 5.396   67.031  1.00 38.36 ? 176 CYS   C O   1 
ATOM   3845 C  CB  . CYS   C 1 83  ? -23.894 6.963   68.312  1.00 40.38 ? 176 CYS   C CB  1 
ATOM   3846 S  SG  . CYS   C 1 83  ? -24.203 5.252   68.623  1.00 41.23 ? 176 CYS   C SG  1 
ATOM   3847 N  N   . PRO   C 1 84  ? -20.657 6.981   68.482  1.00 40.23 ? 177 PRO   C N   1 
ATOM   3848 C  CA  . PRO   C 1 84  ? -19.467 6.242   68.906  1.00 40.56 ? 177 PRO   C CA  1 
ATOM   3849 C  C   . PRO   C 1 84  ? -19.781 4.770   69.226  1.00 40.31 ? 177 PRO   C C   1 
ATOM   3850 O  O   . PRO   C 1 84  ? -19.115 3.909   68.692  1.00 40.04 ? 177 PRO   C O   1 
ATOM   3851 C  CB  . PRO   C 1 84  ? -19.014 7.033   70.141  1.00 42.87 ? 177 PRO   C CB  1 
ATOM   3852 C  CG  . PRO   C 1 84  ? -19.442 8.455   69.838  1.00 42.97 ? 177 PRO   C CG  1 
ATOM   3853 C  CD  . PRO   C 1 84  ? -20.760 8.305   69.111  1.00 41.46 ? 177 PRO   C CD  1 
ATOM   3854 N  N   . HIS   C 1 85  ? -20.817 4.519   70.034  1.00 40.11 ? 178 HIS   C N   1 
ATOM   3855 C  CA  . HIS   C 1 85  ? -21.193 3.171   70.541  1.00 40.08 ? 178 HIS   C CA  1 
ATOM   3856 C  C   . HIS   C 1 85  ? -21.364 2.190   69.378  1.00 38.99 ? 178 HIS   C C   1 
ATOM   3857 O  O   . HIS   C 1 85  ? -20.729 1.117   69.422  1.00 39.31 ? 178 HIS   C O   1 
ATOM   3858 C  CB  . HIS   C 1 85  ? -22.452 3.218   71.415  1.00 39.70 ? 178 HIS   C CB  1 
ATOM   3859 C  CG  . HIS   C 1 85  ? -23.043 1.875   71.684  1.00 39.28 ? 178 HIS   C CG  1 
ATOM   3860 N  ND1 . HIS   C 1 85  ? -22.429 0.896   72.442  1.00 40.38 ? 178 HIS   C ND1 1 
ATOM   3861 C  CD2 . HIS   C 1 85  ? -24.216 1.352   71.283  1.00 38.20 ? 178 HIS   C CD2 1 
ATOM   3862 C  CE1 . HIS   C 1 85  ? -23.206 -0.171  72.493  1.00 40.51 ? 178 HIS   C CE1 1 
ATOM   3863 N  NE2 . HIS   C 1 85  ? -24.325 0.096   71.812  1.00 38.95 ? 178 HIS   C NE2 1 
ATOM   3864 N  N   . HIS   C 1 86  ? -22.201 2.526   68.400  1.00 38.77 ? 179 HIS   C N   1 
ATOM   3865 C  CA  . HIS   C 1 86  ? -22.544 1.619   67.269  1.00 38.54 ? 179 HIS   C CA  1 
ATOM   3866 C  C   . HIS   C 1 86  ? -21.340 1.479   66.328  1.00 39.12 ? 179 HIS   C C   1 
ATOM   3867 O  O   . HIS   C 1 86  ? -21.151 0.382   65.796  1.00 38.91 ? 179 HIS   C O   1 
ATOM   3868 C  CB  . HIS   C 1 86  ? -23.828 2.062   66.560  1.00 37.17 ? 179 HIS   C CB  1 
ATOM   3869 C  CG  . HIS   C 1 86  ? -25.059 1.591   67.265  1.00 37.79 ? 179 HIS   C CG  1 
ATOM   3870 N  ND1 . HIS   C 1 86  ? -26.083 2.450   67.614  1.00 37.39 ? 179 HIS   C ND1 1 
ATOM   3871 C  CD2 . HIS   C 1 86  ? -25.418 0.361   67.703  1.00 37.77 ? 179 HIS   C CD2 1 
ATOM   3872 C  CE1 . HIS   C 1 86  ? -27.027 1.767   68.232  1.00 38.17 ? 179 HIS   C CE1 1 
ATOM   3873 N  NE2 . HIS   C 1 86  ? -26.640 0.482   68.304  1.00 38.18 ? 179 HIS   C NE2 1 
ATOM   3874 N  N   . GLU   C 1 87  ? -20.541 2.531   66.182  1.00 40.85 ? 180 GLU   C N   1 
ATOM   3875 C  CA  . GLU   C 1 87  ? -19.288 2.517   65.374  1.00 43.28 ? 180 GLU   C CA  1 
ATOM   3876 C  C   . GLU   C 1 87  ? -18.355 1.407   65.883  1.00 46.85 ? 180 GLU   C C   1 
ATOM   3877 O  O   . GLU   C 1 87  ? -17.742 0.749   65.030  1.00 49.78 ? 180 GLU   C O   1 
ATOM   3878 C  CB  . GLU   C 1 87  ? -18.682 3.925   65.322  1.00 42.83 ? 180 GLU   C CB  1 
ATOM   3879 C  CG  . GLU   C 1 87  ? -17.380 4.174   66.065  1.00 44.44 ? 180 GLU   C CG  1 
ATOM   3880 C  CD  . GLU   C 1 87  ? -16.992 5.639   66.031  0.80 44.15 ? 180 GLU   C CD  1 
ATOM   3881 O  OE1 . GLU   C 1 87  ? -16.562 6.157   67.080  0.80 45.74 ? 180 GLU   C OE1 1 
ATOM   3882 O  OE2 . GLU   C 1 87  ? -17.135 6.266   64.957  0.80 43.00 ? 180 GLU   C OE2 1 
ATOM   3883 N  N   . ARG   C 1 88  ? -18.251 1.204   67.200  1.00 49.85 ? 181 ARG   C N   1 
ATOM   3884 C  CA  . ARG   C 1 88  ? -17.332 0.185   67.792  1.00 51.12 ? 181 ARG   C CA  1 
ATOM   3885 C  C   . ARG   C 1 88  ? -17.498 -1.139  67.033  1.00 51.73 ? 181 ARG   C C   1 
ATOM   3886 O  O   . ARG   C 1 88  ? -18.627 -1.669  67.052  1.00 52.40 ? 181 ARG   C O   1 
ATOM   3887 C  CB  . ARG   C 1 88  ? -17.600 -0.021  69.281  1.00 52.62 ? 181 ARG   C CB  1 
ATOM   3888 C  CG  . ARG   C 1 88  ? -17.035 1.069   70.179  1.00 53.52 ? 181 ARG   C CG  1 
ATOM   3889 C  CD  . ARG   C 1 88  ? -17.839 1.242   71.465  1.00 54.22 ? 181 ARG   C CD  1 
ATOM   3890 N  NE  . ARG   C 1 88  ? -17.707 0.210   72.504  1.00 56.24 ? 181 ARG   C NE  1 
ATOM   3891 C  CZ  . ARG   C 1 88  ? -18.584 -0.774  72.744  1.00 55.08 ? 181 ARG   C CZ  1 
ATOM   3892 N  NH1 . ARG   C 1 88  ? -18.346 -1.626  73.724  1.00 55.45 ? 181 ARG   C NH1 1 
ATOM   3893 N  NH2 . ARG   C 1 88  ? -19.668 -0.927  71.989  1.00 52.69 ? 181 ARG   C NH2 1 
ATOM   3894 N  N   . SER   C 1 92  ? -19.123 -5.782  61.678  1.00 49.80 ? 185 SER   C N   1 
ATOM   3895 C  CA  . SER   C 1 92  ? -19.466 -7.227  61.643  1.00 49.76 ? 185 SER   C CA  1 
ATOM   3896 C  C   . SER   C 1 92  ? -19.520 -7.764  60.207  1.00 47.34 ? 185 SER   C C   1 
ATOM   3897 O  O   . SER   C 1 92  ? -19.271 -8.979  60.057  1.00 49.57 ? 185 SER   C O   1 
ATOM   3898 C  CB  . SER   C 1 92  ? -20.759 -7.496  62.375  1.00 50.78 ? 185 SER   C CB  1 
ATOM   3899 O  OG  . SER   C 1 92  ? -20.863 -8.881  62.678  1.00 51.98 ? 185 SER   C OG  1 
ATOM   3900 N  N   . ASP   C 1 93  ? -19.840 -6.925  59.207  1.00 44.19 ? 186 ASP   C N   1 
ATOM   3901 C  CA  . ASP   C 1 93  ? -20.237 -7.391  57.846  1.00 42.29 ? 186 ASP   C CA  1 
ATOM   3902 C  C   . ASP   C 1 93  ? -19.002 -7.492  56.926  1.00 42.16 ? 186 ASP   C C   1 
ATOM   3903 O  O   . ASP   C 1 93  ? -19.109 -8.178  55.893  1.00 42.15 ? 186 ASP   C O   1 
ATOM   3904 C  CB  . ASP   C 1 93  ? -21.469 -6.627  57.347  1.00 40.21 ? 186 ASP   C CB  1 
ATOM   3905 C  CG  . ASP   C 1 93  ? -21.281 -5.677  56.173  1.00 38.79 ? 186 ASP   C CG  1 
ATOM   3906 O  OD1 . ASP   C 1 93  ? -20.213 -5.139  56.045  1.00 38.55 ? 186 ASP   C OD1 1 
ATOM   3907 O  OD2 . ASP   C 1 93  ? -22.248 -5.456  55.438  1.00 37.48 ? 186 ASP   C OD2 1 
ATOM   3908 N  N   . GLY   C 1 94  ? -17.875 -6.895  57.333  1.00 41.23 ? 187 GLY   C N   1 
ATOM   3909 C  CA  . GLY   C 1 94  ? -16.578 -6.987  56.636  1.00 41.02 ? 187 GLY   C CA  1 
ATOM   3910 C  C   . GLY   C 1 94  ? -16.421 -6.004  55.483  1.00 38.90 ? 187 GLY   C C   1 
ATOM   3911 O  O   . GLY   C 1 94  ? -15.298 -5.883  54.976  1.00 39.09 ? 187 GLY   C O   1 
ATOM   3912 N  N   . LEU   C 1 95  ? -17.495 -5.359  55.018  1.00 36.88 ? 188 LEU   C N   1 
ATOM   3913 C  CA  . LEU   C 1 95  ? -17.456 -4.534  53.780  1.00 35.24 ? 188 LEU   C CA  1 
ATOM   3914 C  C   . LEU   C 1 95  ? -17.694 -3.058  54.126  1.00 34.52 ? 188 LEU   C C   1 
ATOM   3915 O  O   . LEU   C 1 95  ? -17.021 -2.204  53.539  1.00 36.01 ? 188 LEU   C O   1 
ATOM   3916 C  CB  . LEU   C 1 95  ? -18.507 -5.053  52.791  1.00 34.48 ? 188 LEU   C CB  1 
ATOM   3917 C  CG  . LEU   C 1 95  ? -18.387 -6.523  52.396  1.00 35.40 ? 188 LEU   C CG  1 
ATOM   3918 C  CD1 . LEU   C 1 95  ? -19.595 -6.958  51.575  1.00 34.93 ? 188 LEU   C CD1 1 
ATOM   3919 C  CD2 . LEU   C 1 95  ? -17.113 -6.771  51.617  1.00 36.21 ? 188 LEU   C CD2 1 
ATOM   3920 N  N   . ALA   C 1 96  ? -18.647 -2.756  55.016  1.00 33.47 ? 189 ALA   C N   1 
ATOM   3921 C  CA  . ALA   C 1 96  ? -19.107 -1.379  55.330  1.00 31.96 ? 189 ALA   C CA  1 
ATOM   3922 C  C   . ALA   C 1 96  ? -18.147 -0.709  56.308  1.00 31.94 ? 189 ALA   C C   1 
ATOM   3923 O  O   . ALA   C 1 96  ? -17.721 -1.320  57.280  1.00 32.21 ? 189 ALA   C O   1 
ATOM   3924 C  CB  . ALA   C 1 96  ? -20.496 -1.429  55.888  1.00 32.16 ? 189 ALA   C CB  1 
ATOM   3925 N  N   . PRO   C 1 97  ? -17.755 0.568   56.091  1.00 30.97 ? 190 PRO   C N   1 
ATOM   3926 C  CA  . PRO   C 1 97  ? -16.973 1.290   57.086  1.00 31.32 ? 190 PRO   C CA  1 
ATOM   3927 C  C   . PRO   C 1 97  ? -17.806 1.370   58.360  1.00 30.86 ? 190 PRO   C C   1 
ATOM   3928 O  O   . PRO   C 1 97  ? -19.030 1.498   58.292  1.00 29.89 ? 190 PRO   C O   1 
ATOM   3929 C  CB  . PRO   C 1 97  ? -16.732 2.677   56.475  1.00 30.69 ? 190 PRO   C CB  1 
ATOM   3930 C  CG  . PRO   C 1 97  ? -16.989 2.473   54.992  1.00 30.42 ? 190 PRO   C CG  1 
ATOM   3931 C  CD  . PRO   C 1 97  ? -18.034 1.381   54.900  1.00 29.96 ? 190 PRO   C CD  1 
ATOM   3932 N  N   . PRO   C 1 98  ? -17.171 1.284   59.547  1.00 32.01 ? 191 PRO   C N   1 
ATOM   3933 C  CA  . PRO   C 1 98  ? -17.910 1.277   60.808  1.00 32.72 ? 191 PRO   C CA  1 
ATOM   3934 C  C   . PRO   C 1 98  ? -18.702 2.567   61.072  1.00 32.88 ? 191 PRO   C C   1 
ATOM   3935 O  O   . PRO   C 1 98  ? -19.649 2.474   61.816  1.00 33.45 ? 191 PRO   C O   1 
ATOM   3936 C  CB  . PRO   C 1 98  ? -16.824 1.039   61.873  1.00 33.78 ? 191 PRO   C CB  1 
ATOM   3937 C  CG  . PRO   C 1 98  ? -15.523 1.413   61.215  1.00 34.15 ? 191 PRO   C CG  1 
ATOM   3938 C  CD  . PRO   C 1 98  ? -15.717 1.177   59.732  1.00 33.01 ? 191 PRO   C CD  1 
ATOM   3939 N  N   . GLN   C 1 99  ? -18.332 3.696   60.444  1.00 32.92 ? 192 GLN   C N   1 
ATOM   3940 C  CA  . GLN   C 1 99  ? -18.987 5.020   60.657  1.00 32.68 ? 192 GLN   C CA  1 
ATOM   3941 C  C   . GLN   C 1 99  ? -20.285 5.170   59.840  1.00 31.23 ? 192 GLN   C C   1 
ATOM   3942 O  O   . GLN   C 1 99  ? -21.100 6.038   60.197  1.00 29.51 ? 192 GLN   C O   1 
ATOM   3943 C  CB  . GLN   C 1 99  ? -18.033 6.154   60.287  1.00 34.07 ? 192 GLN   C CB  1 
ATOM   3944 C  CG  . GLN   C 1 99  ? -16.968 6.433   61.342  1.00 36.54 ? 192 GLN   C CG  1 
ATOM   3945 C  CD  . GLN   C 1 99  ? -16.440 7.845   61.185  1.00 37.89 ? 192 GLN   C CD  1 
ATOM   3946 O  OE1 . GLN   C 1 99  ? -16.293 8.349   60.069  1.00 38.83 ? 192 GLN   C OE1 1 
ATOM   3947 N  NE2 . GLN   C 1 99  ? -16.212 8.528   62.294  1.00 40.44 ? 192 GLN   C NE2 1 
ATOM   3948 N  N   . HIS   C 1 100 ? -20.464 4.376   58.787  1.00 30.18 ? 193 HIS   C N   1 
ATOM   3949 C  CA  . HIS   C 1 100 ? -21.551 4.530   57.781  1.00 29.48 ? 193 HIS   C CA  1 
ATOM   3950 C  C   . HIS   C 1 100 ? -22.895 4.087   58.362  1.00 29.09 ? 193 HIS   C C   1 
ATOM   3951 O  O   . HIS   C 1 100 ? -23.002 2.920   58.817  1.00 29.18 ? 193 HIS   C O   1 
ATOM   3952 C  CB  . HIS   C 1 100 ? -21.231 3.745   56.493  1.00 28.99 ? 193 HIS   C CB  1 
ATOM   3953 C  CG  . HIS   C 1 100 ? -20.291 4.464   55.594  1.00 29.00 ? 193 HIS   C CG  1 
ATOM   3954 N  ND1 . HIS   C 1 100 ? -20.532 4.602   54.263  1.00 28.51 ? 193 HIS   C ND1 1 
ATOM   3955 C  CD2 . HIS   C 1 100 ? -19.132 5.116   55.848  1.00 30.17 ? 193 HIS   C CD2 1 
ATOM   3956 C  CE1 . HIS   C 1 100 ? -19.579 5.300   53.713  1.00 29.21 ? 193 HIS   C CE1 1 
ATOM   3957 N  NE2 . HIS   C 1 100 ? -18.700 5.646   54.669  1.00 30.05 ? 193 HIS   C NE2 1 
ATOM   3958 N  N   . LEU   C 1 101 ? -23.894 4.968   58.312  1.00 28.34 ? 194 LEU   C N   1 
ATOM   3959 C  CA  . LEU   C 1 101 ? -25.258 4.663   58.796  1.00 27.58 ? 194 LEU   C CA  1 
ATOM   3960 C  C   . LEU   C 1 101 ? -25.916 3.617   57.913  1.00 26.98 ? 194 LEU   C C   1 
ATOM   3961 O  O   . LEU   C 1 101 ? -26.562 2.716   58.486  1.00 27.28 ? 194 LEU   C O   1 
ATOM   3962 C  CB  . LEU   C 1 101 ? -26.113 5.931   58.851  1.00 27.78 ? 194 LEU   C CB  1 
ATOM   3963 C  CG  . LEU   C 1 101 ? -27.586 5.681   59.164  1.00 27.60 ? 194 LEU   C CG  1 
ATOM   3964 C  CD1 . LEU   C 1 101 ? -27.771 5.150   60.566  1.00 27.98 ? 194 LEU   C CD1 1 
ATOM   3965 C  CD2 . LEU   C 1 101 ? -28.399 6.954   58.965  1.00 27.59 ? 194 LEU   C CD2 1 
ATOM   3966 N  N   . ILE   C 1 102 ? -25.790 3.741   56.585  1.00 26.52 ? 195 ILE   C N   1 
ATOM   3967 C  CA  . ILE   C 1 102 ? -26.602 2.974   55.599  1.00 25.80 ? 195 ILE   C CA  1 
ATOM   3968 C  C   . ILE   C 1 102 ? -25.726 1.885   54.988  1.00 26.25 ? 195 ILE   C C   1 
ATOM   3969 O  O   . ILE   C 1 102 ? -24.688 2.221   54.386  1.00 25.96 ? 195 ILE   C O   1 
ATOM   3970 C  CB  . ILE   C 1 102 ? -27.218 3.861   54.502  1.00 25.34 ? 195 ILE   C CB  1 
ATOM   3971 C  CG1 . ILE   C 1 102 ? -27.924 5.086   55.082  1.00 25.13 ? 195 ILE   C CG1 1 
ATOM   3972 C  CG2 . ILE   C 1 102 ? -28.159 3.050   53.627  1.00 24.85 ? 195 ILE   C CG2 1 
ATOM   3973 C  CD1 . ILE   C 1 102 ? -28.756 5.852   54.082  1.00 25.10 ? 195 ILE   C CD1 1 
ATOM   3974 N  N   . ARG   C 1 103 ? -26.150 0.630   55.136  1.00 26.83 ? 196 ARG   C N   1 
ATOM   3975 C  CA  . ARG   C 1 103 ? -25.479 -0.517  54.488  1.00 27.74 ? 196 ARG   C CA  1 
ATOM   3976 C  C   . ARG   C 1 103 ? -26.431 -1.136  53.472  1.00 27.96 ? 196 ARG   C C   1 
ATOM   3977 O  O   . ARG   C 1 103 ? -27.665 -0.927  53.589  1.00 28.24 ? 196 ARG   C O   1 
ATOM   3978 C  CB  . ARG   C 1 103 ? -25.096 -1.558  55.535  1.00 29.00 ? 196 ARG   C CB  1 
ATOM   3979 C  CG  . ARG   C 1 103 ? -24.149 -1.040  56.601  1.00 30.06 ? 196 ARG   C CG  1 
ATOM   3980 C  CD  . ARG   C 1 103 ? -23.552 -2.256  57.281  1.00 31.63 ? 196 ARG   C CD  1 
ATOM   3981 N  NE  . ARG   C 1 103 ? -22.810 -1.930  58.474  1.00 32.21 ? 196 ARG   C NE  1 
ATOM   3982 C  CZ  . ARG   C 1 103 ? -22.503 -2.800  59.423  1.00 34.58 ? 196 ARG   C CZ  1 
ATOM   3983 N  NH1 . ARG   C 1 103 ? -22.886 -4.069  59.326  1.00 35.85 ? 196 ARG   C NH1 1 
ATOM   3984 N  NH2 . ARG   C 1 103 ? -21.794 -2.400  60.467  1.00 35.21 ? 196 ARG   C NH2 1 
ATOM   3985 N  N   . VAL   C 1 104 ? -25.871 -1.856  52.495  1.00 28.61 ? 197 VAL   C N   1 
ATOM   3986 C  CA  . VAL   C 1 104 ? -26.671 -2.759  51.623  1.00 29.79 ? 197 VAL   C CA  1 
ATOM   3987 C  C   . VAL   C 1 104 ? -26.314 -4.188  52.026  1.00 31.06 ? 197 VAL   C C   1 
ATOM   3988 O  O   . VAL   C 1 104 ? -25.110 -4.466  52.229  1.00 31.49 ? 197 VAL   C O   1 
ATOM   3989 C  CB  . VAL   C 1 104 ? -26.444 -2.474  50.127  1.00 30.34 ? 197 VAL   C CB  1 
ATOM   3990 C  CG1 . VAL   C 1 104 ? -27.086 -3.537  49.248  1.00 31.07 ? 197 VAL   C CG1 1 
ATOM   3991 C  CG2 . VAL   C 1 104 ? -26.955 -1.094  49.745  1.00 29.93 ? 197 VAL   C CG2 1 
ATOM   3992 N  N   . GLU   C 1 105 ? -27.330 -5.025  52.220  1.00 32.78 ? 198 GLU   C N   1 
ATOM   3993 C  CA  . GLU   C 1 105 ? -27.144 -6.453  52.597  1.00 34.29 ? 198 GLU   C CA  1 
ATOM   3994 C  C   . GLU   C 1 105 ? -27.381 -7.306  51.345  1.00 34.42 ? 198 GLU   C C   1 
ATOM   3995 O  O   . GLU   C 1 105 ? -28.128 -6.855  50.453  1.00 34.88 ? 198 GLU   C O   1 
ATOM   3996 C  CB  . GLU   C 1 105 ? -28.050 -6.783  53.795  1.00 35.74 ? 198 GLU   C CB  1 
ATOM   3997 C  CG  . GLU   C 1 105 ? -29.251 -7.652  53.472  1.00 37.37 ? 198 GLU   C CG  1 
ATOM   3998 C  CD  . GLU   C 1 105 ? -30.224 -7.853  54.624  1.00 38.69 ? 198 GLU   C CD  1 
ATOM   3999 O  OE1 . GLU   C 1 105 ? -30.435 -9.021  55.016  1.00 39.85 ? 198 GLU   C OE1 1 
ATOM   4000 O  OE2 . GLU   C 1 105 ? -30.781 -6.838  55.118  1.00 38.63 ? 198 GLU   C OE2 1 
ATOM   4001 N  N   . GLY   C 1 106 ? -26.752 -8.477  51.286  1.00 36.69 ? 199 GLY   C N   1 
ATOM   4002 C  CA  . GLY   C 1 106 ? -26.953 -9.487  50.229  1.00 37.28 ? 199 GLY   C CA  1 
ATOM   4003 C  C   . GLY   C 1 106 ? -26.390 -9.065  48.881  1.00 37.98 ? 199 GLY   C C   1 
ATOM   4004 O  O   . GLY   C 1 106 ? -26.899 -9.579  47.858  1.00 38.78 ? 199 GLY   C O   1 
ATOM   4005 N  N   . ASN   C 1 107 ? -25.398 -8.163  48.839  1.00 36.67 ? 200 ASN   C N   1 
ATOM   4006 C  CA  . ASN   C 1 107 ? -24.816 -7.691  47.554  1.00 36.47 ? 200 ASN   C CA  1 
ATOM   4007 C  C   . ASN   C 1 107 ? -23.289 -7.596  47.679  1.00 35.88 ? 200 ASN   C C   1 
ATOM   4008 O  O   . ASN   C 1 107 ? -22.768 -6.631  48.260  1.00 33.62 ? 200 ASN   C O   1 
ATOM   4009 C  CB  . ASN   C 1 107 ? -25.484 -6.401  47.067  1.00 36.35 ? 200 ASN   C CB  1 
ATOM   4010 C  CG  . ASN   C 1 107 ? -25.237 -6.169  45.592  1.00 37.34 ? 200 ASN   C CG  1 
ATOM   4011 O  OD1 . ASN   C 1 107 ? -24.172 -6.517  45.089  1.00 38.70 ? 200 ASN   C OD1 1 
ATOM   4012 N  ND2 . ASN   C 1 107 ? -26.209 -5.605  44.889  1.00 37.55 ? 200 ASN   C ND2 1 
ATOM   4013 N  N   . LEU   C 1 108 ? -22.590 -8.554  47.075  1.00 36.37 ? 201 LEU   C N   1 
ATOM   4014 C  CA  . LEU   C 1 108 ? -21.114 -8.652  47.146  1.00 37.29 ? 201 LEU   C CA  1 
ATOM   4015 C  C   . LEU   C 1 108 ? -20.463 -7.572  46.279  1.00 36.98 ? 201 LEU   C C   1 
ATOM   4016 O  O   . LEU   C 1 108 ? -19.247 -7.432  46.404  1.00 37.67 ? 201 LEU   C O   1 
ATOM   4017 C  CB  . LEU   C 1 108 ? -20.672 -10.042 46.686  1.00 39.47 ? 201 LEU   C CB  1 
ATOM   4018 C  CG  . LEU   C 1 108 ? -21.421 -11.211 47.310  1.00 40.59 ? 201 LEU   C CG  1 
ATOM   4019 C  CD1 . LEU   C 1 108 ? -21.222 -12.479 46.482  1.00 42.86 ? 201 LEU   C CD1 1 
ATOM   4020 C  CD2 . LEU   C 1 108 ? -20.967 -11.429 48.749  1.00 41.07 ? 201 LEU   C CD2 1 
ATOM   4021 N  N   . ARG   C 1 109 ? -21.220 -6.837  45.449  1.00 36.89 ? 202 ARG   C N   1 
ATOM   4022 C  CA  . ARG   C 1 109 ? -20.676 -5.791  44.538  1.00 36.97 ? 202 ARG   C CA  1 
ATOM   4023 C  C   . ARG   C 1 109 ? -20.879 -4.404  45.155  1.00 35.85 ? 202 ARG   C C   1 
ATOM   4024 O  O   . ARG   C 1 109 ? -20.573 -3.401  44.478  1.00 37.24 ? 202 ARG   C O   1 
ATOM   4025 C  CB  . ARG   C 1 109 ? -21.347 -5.874  43.167  1.00 38.12 ? 202 ARG   C CB  1 
ATOM   4026 C  CG  . ARG   C 1 109 ? -21.082 -7.171  42.420  1.00 40.09 ? 202 ARG   C CG  1 
ATOM   4027 C  CD  . ARG   C 1 109 ? -21.681 -7.196  41.025  1.00 41.95 ? 202 ARG   C CD  1 
ATOM   4028 N  NE  . ARG   C 1 109 ? -21.234 -6.104  40.161  0.80 43.00 ? 202 ARG   C NE  1 
ATOM   4029 C  CZ  . ARG   C 1 109 ? -21.787 -5.783  38.990  0.80 44.53 ? 202 ARG   C CZ  1 
ATOM   4030 N  NH1 . ARG   C 1 109 ? -22.804 -6.481  38.509  0.80 45.07 ? 202 ARG   C NH1 1 
ATOM   4031 N  NH2 . ARG   C 1 109 ? -21.319 -4.760  38.289  0.80 44.97 ? 202 ARG   C NH2 1 
ATOM   4032 N  N   . VAL   C 1 110 ? -21.373 -4.339  46.392  1.00 34.09 ? 203 VAL   C N   1 
ATOM   4033 C  CA  . VAL   C 1 110 ? -21.585 -3.064  47.141  1.00 32.00 ? 203 VAL   C CA  1 
ATOM   4034 C  C   . VAL   C 1 110 ? -20.252 -2.310  47.270  1.00 31.41 ? 203 VAL   C C   1 
ATOM   4035 O  O   . VAL   C 1 110 ? -19.216 -2.940  47.459  1.00 32.08 ? 203 VAL   C O   1 
ATOM   4036 C  CB  . VAL   C 1 110 ? -22.250 -3.312  48.510  1.00 31.31 ? 203 VAL   C CB  1 
ATOM   4037 C  CG1 . VAL   C 1 110 ? -21.388 -4.153  49.447  1.00 32.07 ? 203 VAL   C CG1 1 
ATOM   4038 C  CG2 . VAL   C 1 110 ? -22.624 -1.995  49.169  1.00 30.18 ? 203 VAL   C CG2 1 
ATOM   4039 N  N   . GLU   C 1 111 ? -20.298 -0.982  47.182  1.00 30.18 ? 204 GLU   C N   1 
ATOM   4040 C  CA  . GLU   C 1 111 ? -19.109 -0.093  47.266  1.00 30.26 ? 204 GLU   C CA  1 
ATOM   4041 C  C   . GLU   C 1 111 ? -19.472 1.061   48.213  1.00 28.96 ? 204 GLU   C C   1 
ATOM   4042 O  O   . GLU   C 1 111 ? -20.626 1.522   48.157  1.00 28.54 ? 204 GLU   C O   1 
ATOM   4043 C  CB  . GLU   C 1 111 ? -18.715 0.328   45.845  1.00 31.26 ? 204 GLU   C CB  1 
ATOM   4044 C  CG  . GLU   C 1 111 ? -17.894 1.606   45.745  1.00 31.70 ? 204 GLU   C CG  1 
ATOM   4045 C  CD  . GLU   C 1 111 ? -17.695 2.127   44.332  1.00 32.48 ? 204 GLU   C CD  1 
ATOM   4046 O  OE1 . GLU   C 1 111 ? -17.555 1.306   43.416  1.00 33.02 ? 204 GLU   C OE1 1 
ATOM   4047 O  OE2 . GLU   C 1 111 ? -17.684 3.362   44.148  1.00 32.88 ? 204 GLU   C OE2 1 
ATOM   4048 N  N   . TYR   C 1 112 ? -18.554 1.449   49.099  1.00 28.63 ? 205 TYR   C N   1 
ATOM   4049 C  CA  . TYR   C 1 112 ? -18.769 2.523   50.107  1.00 28.00 ? 205 TYR   C CA  1 
ATOM   4050 C  C   . TYR   C 1 112 ? -17.823 3.695   49.803  1.00 28.13 ? 205 TYR   C C   1 
ATOM   4051 O  O   . TYR   C 1 112 ? -16.675 3.478   49.405  1.00 28.60 ? 205 TYR   C O   1 
ATOM   4052 C  CB  . TYR   C 1 112 ? -18.611 1.962   51.525  1.00 27.51 ? 205 TYR   C CB  1 
ATOM   4053 C  CG  . TYR   C 1 112 ? -19.698 1.002   51.946  1.00 27.02 ? 205 TYR   C CG  1 
ATOM   4054 C  CD1 . TYR   C 1 112 ? -20.871 1.452   52.534  1.00 26.32 ? 205 TYR   C CD1 1 
ATOM   4055 C  CD2 . TYR   C 1 112 ? -19.549 -0.363  51.770  1.00 27.03 ? 205 TYR   C CD2 1 
ATOM   4056 C  CE1 . TYR   C 1 112 ? -21.881 0.576   52.901  1.00 25.82 ? 205 TYR   C CE1 1 
ATOM   4057 C  CE2 . TYR   C 1 112 ? -20.549 -1.252  52.121  1.00 26.92 ? 205 TYR   C CE2 1 
ATOM   4058 C  CZ  . TYR   C 1 112 ? -21.720 -0.783  52.685  1.00 26.21 ? 205 TYR   C CZ  1 
ATOM   4059 O  OH  . TYR   C 1 112 ? -22.700 -1.657  53.045  1.00 25.57 ? 205 TYR   C OH  1 
ATOM   4060 N  N   . LEU   C 1 113 ? -18.301 4.928   49.979  1.00 28.52 ? 206 LEU   C N   1 
ATOM   4061 C  CA  . LEU   C 1 113 ? -17.521 6.155   49.677  1.00 29.48 ? 206 LEU   C CA  1 
ATOM   4062 C  C   . LEU   C 1 113 ? -17.523 7.076   50.903  1.00 30.36 ? 206 LEU   C C   1 
ATOM   4063 O  O   . LEU   C 1 113 ? -18.618 7.326   51.458  1.00 31.07 ? 206 LEU   C O   1 
ATOM   4064 C  CB  . LEU   C 1 113 ? -18.134 6.837   48.444  1.00 29.83 ? 206 LEU   C CB  1 
ATOM   4065 C  CG  . LEU   C 1 113 ? -17.583 8.225   48.117  1.00 30.35 ? 206 LEU   C CG  1 
ATOM   4066 C  CD1 . LEU   C 1 113 ? -16.107 8.156   47.783  1.00 31.12 ? 206 LEU   C CD1 1 
ATOM   4067 C  CD2 . LEU   C 1 113 ? -18.372 8.866   46.981  1.00 30.84 ? 206 LEU   C CD2 1 
ATOM   4068 N  N   . ASP   C 1 114 ? -16.338 7.495   51.341  1.00 31.46 ? 207 ASP   C N   1 
ATOM   4069 C  CA  . ASP   C 1 114 ? -16.120 8.732   52.131  1.00 33.25 ? 207 ASP   C CA  1 
ATOM   4070 C  C   . ASP   C 1 114 ? -15.705 9.812   51.128  1.00 34.70 ? 207 ASP   C C   1 
ATOM   4071 O  O   . ASP   C 1 114 ? -14.605 9.682   50.568  1.00 34.76 ? 207 ASP   C O   1 
ATOM   4072 C  CB  . ASP   C 1 114 ? -15.040 8.554   53.199  1.00 33.71 ? 207 ASP   C CB  1 
ATOM   4073 C  CG  . ASP   C 1 114 ? -15.377 7.589   54.315  1.00 33.06 ? 207 ASP   C CG  1 
ATOM   4074 O  OD1 . ASP   C 1 114 ? -16.498 7.086   54.353  1.00 32.79 ? 207 ASP   C OD1 1 
ATOM   4075 O  OD2 . ASP   C 1 114 ? -14.521 7.432   55.200  1.00 34.57 ? 207 ASP   C OD2 1 
ATOM   4076 N  N   . ASP   C 1 115 ? -16.598 10.752  50.817  1.00 36.30 ? 208 ASP   C N   1 
ATOM   4077 C  CA  . ASP   C 1 115 ? -16.356 11.799  49.785  1.00 38.60 ? 208 ASP   C CA  1 
ATOM   4078 C  C   . ASP   C 1 115 ? -15.157 12.633  50.246  1.00 40.49 ? 208 ASP   C C   1 
ATOM   4079 O  O   . ASP   C 1 115 ? -15.172 13.115  51.397  1.00 40.43 ? 208 ASP   C O   1 
ATOM   4080 C  CB  . ASP   C 1 115 ? -17.607 12.648  49.534  1.00 38.85 ? 208 ASP   C CB  1 
ATOM   4081 C  CG  . ASP   C 1 115 ? -17.453 13.656  48.398  1.00 39.83 ? 208 ASP   C CG  1 
ATOM   4082 O  OD1 . ASP   C 1 115 ? -16.649 14.600  48.543  1.00 41.33 ? 208 ASP   C OD1 1 
ATOM   4083 O  OD2 . ASP   C 1 115 ? -18.135 13.489  47.371  1.00 39.60 ? 208 ASP   C OD2 1 
ATOM   4084 N  N   . ARG   C 1 116 ? -14.148 12.763  49.381  1.00 43.29 ? 209 ARG   C N   1 
ATOM   4085 C  CA  . ARG   C 1 116 ? -12.869 13.468  49.657  1.00 46.42 ? 209 ARG   C CA  1 
ATOM   4086 C  C   . ARG   C 1 116 ? -13.115 14.906  50.141  1.00 47.94 ? 209 ARG   C C   1 
ATOM   4087 O  O   . ARG   C 1 116 ? -12.301 15.384  50.944  1.00 49.52 ? 209 ARG   C O   1 
ATOM   4088 C  CB  . ARG   C 1 116 ? -12.019 13.550  48.385  1.00 48.17 ? 209 ARG   C CB  1 
ATOM   4089 C  CG  . ARG   C 1 116 ? -11.187 12.320  48.055  1.00 48.94 ? 209 ARG   C CG  1 
ATOM   4090 C  CD  . ARG   C 1 116 ? -10.279 12.581  46.862  1.00 51.39 ? 209 ARG   C CD  1 
ATOM   4091 N  NE  . ARG   C 1 116 ? -9.695  13.924  46.878  1.00 53.92 ? 209 ARG   C NE  1 
ATOM   4092 C  CZ  . ARG   C 1 116 ? -8.955  14.450  45.910  1.00 55.70 ? 209 ARG   C CZ  1 
ATOM   4093 N  NH1 . ARG   C 1 116 ? -8.489  15.680  46.039  1.00 57.90 ? 209 ARG   C NH1 1 
ATOM   4094 N  NH2 . ARG   C 1 116 ? -8.679  13.757  44.820  1.00 56.94 ? 209 ARG   C NH2 1 
ATOM   4095 N  N   . ASN   C 1 117 ? -14.171 15.577  49.664  1.00 48.80 ? 210 ASN   C N   1 
ATOM   4096 C  CA  . ASN   C 1 117 ? -14.347 17.047  49.850  1.00 50.76 ? 210 ASN   C CA  1 
ATOM   4097 C  C   . ASN   C 1 117 ? -15.531 17.358  50.773  1.00 49.31 ? 210 ASN   C C   1 
ATOM   4098 O  O   . ASN   C 1 117 ? -15.397 18.309  51.568  1.00 51.23 ? 210 ASN   C O   1 
ATOM   4099 C  CB  . ASN   C 1 117 ? -14.475 17.802  48.526  1.00 53.22 ? 210 ASN   C CB  1 
ATOM   4100 C  CG  . ASN   C 1 117 ? -15.329 17.101  47.497  1.00 53.75 ? 210 ASN   C CG  1 
ATOM   4101 O  OD1 . ASN   C 1 117 ? -14.961 16.034  47.010  1.00 55.64 ? 210 ASN   C OD1 1 
ATOM   4102 N  ND2 . ASN   C 1 117 ? -16.464 17.690  47.163  1.00 55.05 ? 210 ASN   C ND2 1 
ATOM   4103 N  N   . THR   C 1 118 ? -16.657 16.639  50.666  1.00 46.28 ? 211 THR   C N   1 
ATOM   4104 C  CA  . THR   C 1 118 ? -17.857 16.880  51.515  1.00 44.82 ? 211 THR   C CA  1 
ATOM   4105 C  C   . THR   C 1 118 ? -17.779 16.043  52.793  1.00 43.31 ? 211 THR   C C   1 
ATOM   4106 O  O   . THR   C 1 118 ? -18.513 16.365  53.725  1.00 43.71 ? 211 THR   C O   1 
ATOM   4107 C  CB  . THR   C 1 118 ? -19.170 16.570  50.782  1.00 44.35 ? 211 THR   C CB  1 
ATOM   4108 O  OG1 . THR   C 1 118 ? -19.212 15.172  50.486  1.00 42.11 ? 211 THR   C OG1 1 
ATOM   4109 C  CG2 . THR   C 1 118 ? -19.333 17.383  49.516  1.00 45.52 ? 211 THR   C CG2 1 
ATOM   4110 N  N   . PHE   C 1 119 ? -16.973 14.975  52.799  1.00 41.75 ? 212 PHE   C N   1 
ATOM   4111 C  CA  . PHE   C 1 119 ? -16.815 14.025  53.933  1.00 40.47 ? 212 PHE   C CA  1 
ATOM   4112 C  C   . PHE   C 1 119 ? -18.121 13.255  54.154  1.00 38.63 ? 212 PHE   C C   1 
ATOM   4113 O  O   . PHE   C 1 119 ? -18.243 12.538  55.171  1.00 38.89 ? 212 PHE   C O   1 
ATOM   4114 C  CB  . PHE   C 1 119 ? -16.387 14.753  55.210  1.00 41.82 ? 212 PHE   C CB  1 
ATOM   4115 C  CG  . PHE   C 1 119 ? -15.185 15.650  55.061  1.00 43.69 ? 212 PHE   C CG  1 
ATOM   4116 C  CD1 . PHE   C 1 119 ? -13.922 15.125  54.834  1.00 44.37 ? 212 PHE   C CD1 1 
ATOM   4117 C  CD2 . PHE   C 1 119 ? -15.319 17.025  55.153  1.00 45.50 ? 212 PHE   C CD2 1 
ATOM   4118 C  CE1 . PHE   C 1 119 ? -12.817 15.955  54.718  1.00 45.67 ? 212 PHE   C CE1 1 
ATOM   4119 C  CE2 . PHE   C 1 119 ? -14.214 17.855  55.032  1.00 47.31 ? 212 PHE   C CE2 1 
ATOM   4120 C  CZ  . PHE   C 1 119 ? -12.966 17.320  54.807  1.00 47.16 ? 212 PHE   C CZ  1 
ATOM   4121 N  N   . ARG   C 1 120 ? -19.073 13.379  53.227  1.00 37.48 ? 213 ARG   C N   1 
ATOM   4122 C  CA  . ARG   C 1 120 ? -20.379 12.679  53.314  1.00 36.21 ? 213 ARG   C CA  1 
ATOM   4123 C  C   . ARG   C 1 120 ? -20.162 11.213  52.953  1.00 34.61 ? 213 ARG   C C   1 
ATOM   4124 O  O   . ARG   C 1 120 ? -19.276 10.916  52.130  1.00 34.68 ? 213 ARG   C O   1 
ATOM   4125 C  CB  . ARG   C 1 120 ? -21.433 13.381  52.455  1.00 37.02 ? 213 ARG   C CB  1 
ATOM   4126 C  CG  . ARG   C 1 120 ? -21.767 14.763  52.991  1.00 38.34 ? 213 ARG   C CG  1 
ATOM   4127 C  CD  . ARG   C 1 120 ? -22.980 15.399  52.364  1.00 38.90 ? 213 ARG   C CD  1 
ATOM   4128 N  NE  . ARG   C 1 120 ? -23.263 16.705  52.952  1.00 40.48 ? 213 ARG   C NE  1 
ATOM   4129 C  CZ  . ARG   C 1 120 ? -23.979 16.931  54.057  1.00 40.46 ? 213 ARG   C CZ  1 
ATOM   4130 N  NH1 . ARG   C 1 120 ? -24.538 15.933  54.716  1.00 39.01 ? 213 ARG   C NH1 1 
ATOM   4131 N  NH2 . ARG   C 1 120 ? -24.173 18.172  54.473  1.00 42.02 ? 213 ARG   C NH2 1 
ATOM   4132 N  N   . HIS   C 1 121 ? -20.932 10.336  53.587  1.00 33.30 ? 214 HIS   C N   1 
ATOM   4133 C  CA  . HIS   C 1 121 ? -20.885 8.865   53.388  1.00 32.11 ? 214 HIS   C CA  1 
ATOM   4134 C  C   . HIS   C 1 121 ? -21.973 8.439   52.405  1.00 30.47 ? 214 HIS   C C   1 
ATOM   4135 O  O   . HIS   C 1 121 ? -23.088 8.991   52.454  1.00 30.38 ? 214 HIS   C O   1 
ATOM   4136 C  CB  . HIS   C 1 121 ? -21.100 8.161   54.722  1.00 32.18 ? 214 HIS   C CB  1 
ATOM   4137 C  CG  . HIS   C 1 121 ? -20.102 8.501   55.767  1.00 33.59 ? 214 HIS   C CG  1 
ATOM   4138 N  ND1 . HIS   C 1 121 ? -20.352 8.258   57.102  1.00 34.57 ? 214 HIS   C ND1 1 
ATOM   4139 C  CD2 . HIS   C 1 121 ? -18.860 9.019   55.698  1.00 34.76 ? 214 HIS   C CD2 1 
ATOM   4140 C  CE1 . HIS   C 1 121 ? -19.303 8.594   57.813  1.00 34.87 ? 214 HIS   C CE1 1 
ATOM   4141 N  NE2 . HIS   C 1 121 ? -18.367 9.064   56.983  1.00 35.40 ? 214 HIS   C NE2 1 
ATOM   4142 N  N   . SER   C 1 122 ? -21.698 7.439   51.577  1.00 29.30 ? 215 SER   C N   1 
ATOM   4143 C  CA  . SER   C 1 122 ? -22.737 6.836   50.719  1.00 28.12 ? 215 SER   C CA  1 
ATOM   4144 C  C   . SER   C 1 122 ? -22.362 5.397   50.367  1.00 27.96 ? 215 SER   C C   1 
ATOM   4145 O  O   . SER   C 1 122 ? -21.166 5.021   50.523  1.00 27.10 ? 215 SER   C O   1 
ATOM   4146 C  CB  . SER   C 1 122 ? -22.967 7.676   49.516  1.00 28.52 ? 215 SER   C CB  1 
ATOM   4147 O  OG  . SER   C 1 122 ? -21.777 7.802   48.748  1.00 28.18 ? 215 SER   C OG  1 
ATOM   4148 N  N   . VAL   C 1 123 ? -23.367 4.628   49.963  1.00 27.50 ? 216 VAL   C N   1 
ATOM   4149 C  CA  . VAL   C 1 123 ? -23.227 3.199   49.573  1.00 27.86 ? 216 VAL   C CA  1 
ATOM   4150 C  C   . VAL   C 1 123 ? -23.826 3.079   48.171  1.00 28.81 ? 216 VAL   C C   1 
ATOM   4151 O  O   . VAL   C 1 123 ? -24.917 3.645   47.915  1.00 28.39 ? 216 VAL   C O   1 
ATOM   4152 C  CB  . VAL   C 1 123 ? -23.861 2.243   50.607  1.00 27.21 ? 216 VAL   C CB  1 
ATOM   4153 C  CG1 . VAL   C 1 123 ? -25.316 2.559   50.917  1.00 27.06 ? 216 VAL   C CG1 1 
ATOM   4154 C  CG2 . VAL   C 1 123 ? -23.711 0.774   50.212  1.00 27.29 ? 216 VAL   C CG2 1 
ATOM   4155 N  N   A VAL   C 1 124 ? -23.109 2.402   47.271  0.45 29.55 ? 217 VAL   C N   1 
ATOM   4156 N  N   B VAL   C 1 124 ? -23.114 2.394   47.277  0.55 29.67 ? 217 VAL   C N   1 
ATOM   4157 C  CA  A VAL   C 1 124 ? -23.479 2.304   45.833  0.45 30.45 ? 217 VAL   C CA  1 
ATOM   4158 C  CA  B VAL   C 1 124 ? -23.485 2.295   45.840  0.55 30.65 ? 217 VAL   C CA  1 
ATOM   4159 C  C   A VAL   C 1 124 ? -23.486 0.825   45.425  0.45 31.07 ? 217 VAL   C C   1 
ATOM   4160 C  C   B VAL   C 1 124 ? -23.494 0.819   45.435  0.55 31.16 ? 217 VAL   C C   1 
ATOM   4161 O  O   A VAL   C 1 124 ? -22.605 0.078   45.874  0.45 32.28 ? 217 VAL   C O   1 
ATOM   4162 O  O   B VAL   C 1 124 ? -22.615 0.072   45.883  0.55 32.57 ? 217 VAL   C O   1 
ATOM   4163 C  CB  A VAL   C 1 124 ? -22.557 3.183   44.965  0.45 30.81 ? 217 VAL   C CB  1 
ATOM   4164 C  CB  B VAL   C 1 124 ? -22.552 3.133   44.947  0.55 31.14 ? 217 VAL   C CB  1 
ATOM   4165 C  CG1 A VAL   C 1 124 ? -21.091 2.827   45.096  0.45 30.97 ? 217 VAL   C CG1 1 
ATOM   4166 C  CG1 B VAL   C 1 124 ? -23.253 3.502   43.652  0.55 31.60 ? 217 VAL   C CG1 1 
ATOM   4167 C  CG2 A VAL   C 1 124 ? -22.986 3.185   43.507  0.45 31.50 ? 217 VAL   C CG2 1 
ATOM   4168 C  CG2 B VAL   C 1 124 ? -22.035 4.380   45.642  0.55 31.23 ? 217 VAL   C CG2 1 
ATOM   4169 N  N   . VAL   C 1 125 ? -24.501 0.421   44.660  1.00 32.00 ? 218 VAL   C N   1 
ATOM   4170 C  CA  . VAL   C 1 125 ? -24.623 -0.939  44.066  1.00 33.01 ? 218 VAL   C CA  1 
ATOM   4171 C  C   . VAL   C 1 125 ? -24.874 -0.746  42.575  1.00 34.37 ? 218 VAL   C C   1 
ATOM   4172 O  O   . VAL   C 1 125 ? -25.417 0.272   42.149  1.00 33.71 ? 218 VAL   C O   1 
ATOM   4173 C  CB  . VAL   C 1 125 ? -25.739 -1.765  44.741  1.00 32.87 ? 218 VAL   C CB  1 
ATOM   4174 C  CG1 . VAL   C 1 125 ? -25.338 -2.172  46.153  1.00 32.53 ? 218 VAL   C CG1 1 
ATOM   4175 C  CG2 . VAL   C 1 125 ? -27.090 -1.050  44.746  1.00 32.79 ? 218 VAL   C CG2 1 
ATOM   4176 N  N   . PRO   C 1 126 ? -24.483 -1.720  41.731  1.00 36.24 ? 219 PRO   C N   1 
ATOM   4177 C  CA  . PRO   C 1 126 ? -24.892 -1.706  40.330  1.00 38.13 ? 219 PRO   C CA  1 
ATOM   4178 C  C   . PRO   C 1 126 ? -26.417 -1.833  40.253  1.00 38.88 ? 219 PRO   C C   1 
ATOM   4179 O  O   . PRO   C 1 126 ? -27.016 -2.530  41.068  1.00 37.87 ? 219 PRO   C O   1 
ATOM   4180 C  CB  . PRO   C 1 126 ? -24.207 -2.906  39.666  1.00 39.55 ? 219 PRO   C CB  1 
ATOM   4181 C  CG  . PRO   C 1 126 ? -23.396 -3.578  40.767  1.00 38.44 ? 219 PRO   C CG  1 
ATOM   4182 C  CD  . PRO   C 1 126 ? -23.645 -2.870  42.081  1.00 36.83 ? 219 PRO   C CD  1 
ATOM   4183 N  N   . TYR   C 1 127 ? -27.013 -1.117  39.307  1.00 40.39 ? 220 TYR   C N   1 
ATOM   4184 C  CA  . TYR   C 1 127 ? -28.427 -1.287  38.926  1.00 40.77 ? 220 TYR   C CA  1 
ATOM   4185 C  C   . TYR   C 1 127 ? -28.572 -2.630  38.206  1.00 42.99 ? 220 TYR   C C   1 
ATOM   4186 O  O   . TYR   C 1 127 ? -27.787 -2.915  37.294  1.00 43.72 ? 220 TYR   C O   1 
ATOM   4187 C  CB  . TYR   C 1 127 ? -28.887 -0.135  38.037  1.00 41.38 ? 220 TYR   C CB  1 
ATOM   4188 C  CG  . TYR   C 1 127 ? -30.293 -0.344  37.561  1.00 41.84 ? 220 TYR   C CG  1 
ATOM   4189 C  CD1 . TYR   C 1 127 ? -31.368 -0.004  38.359  1.00 40.50 ? 220 TYR   C CD1 1 
ATOM   4190 C  CD2 . TYR   C 1 127 ? -30.538 -0.966  36.349  1.00 43.41 ? 220 TYR   C CD2 1 
ATOM   4191 C  CE1 . TYR   C 1 127 ? -32.669 -0.239  37.956  1.00 41.80 ? 220 TYR   C CE1 1 
ATOM   4192 C  CE2 . TYR   C 1 127 ? -31.834 -1.187  35.916  1.00 43.83 ? 220 TYR   C CE2 1 
ATOM   4193 C  CZ  . TYR   C 1 127 ? -32.899 -0.823  36.727  1.00 42.96 ? 220 TYR   C CZ  1 
ATOM   4194 O  OH  . TYR   C 1 127 ? -34.179 -1.045  36.339  1.00 43.03 ? 220 TYR   C OH  1 
ATOM   4195 N  N   . GLU   C 1 128 ? -29.510 -3.459  38.648  1.00 43.83 ? 221 GLU   C N   1 
ATOM   4196 C  CA  . GLU   C 1 128 ? -29.933 -4.682  37.916  1.00 46.47 ? 221 GLU   C CA  1 
ATOM   4197 C  C   . GLU   C 1 128 ? -31.389 -4.483  37.522  1.00 47.56 ? 221 GLU   C C   1 
ATOM   4198 O  O   . GLU   C 1 128 ? -32.180 -3.983  38.322  1.00 47.47 ? 221 GLU   C O   1 
ATOM   4199 C  CB  . GLU   C 1 128 ? -29.764 -5.964  38.736  1.00 46.61 ? 221 GLU   C CB  1 
ATOM   4200 C  CG  . GLU   C 1 128 ? -28.672 -5.955  39.808  1.00 45.43 ? 221 GLU   C CG  1 
ATOM   4201 C  CD  . GLU   C 1 128 ? -28.849 -7.012  40.886  1.00 45.53 ? 221 GLU   C CD  1 
ATOM   4202 O  OE1 . GLU   C 1 128 ? -29.418 -8.098  40.577  1.00 47.37 ? 221 GLU   C OE1 1 
ATOM   4203 O  OE2 . GLU   C 1 128 ? -28.411 -6.764  42.032  1.00 43.60 ? 221 GLU   C OE2 1 
ATOM   4204 N  N   . PRO   C 1 129 ? -31.766 -4.844  36.282  1.00 50.16 ? 222 PRO   C N   1 
ATOM   4205 C  CA  . PRO   C 1 129 ? -33.140 -4.650  35.841  1.00 51.44 ? 222 PRO   C CA  1 
ATOM   4206 C  C   . PRO   C 1 129 ? -34.051 -5.607  36.586  1.00 51.98 ? 222 PRO   C C   1 
ATOM   4207 O  O   . PRO   C 1 129 ? -33.582 -6.584  37.169  1.00 51.57 ? 222 PRO   C O   1 
ATOM   4208 C  CB  . PRO   C 1 129 ? -33.103 -4.906  34.329  1.00 53.22 ? 222 PRO   C CB  1 
ATOM   4209 C  CG  . PRO   C 1 129 ? -31.854 -5.757  34.118  1.00 53.76 ? 222 PRO   C CG  1 
ATOM   4210 C  CD  . PRO   C 1 129 ? -30.897 -5.429  35.251  1.00 51.61 ? 222 PRO   C CD  1 
ATOM   4211 N  N   . PRO   C 1 130 ? -35.382 -5.373  36.577  1.00 53.16 ? 223 PRO   C N   1 
ATOM   4212 C  CA  . PRO   C 1 130 ? -36.301 -6.346  37.166  1.00 54.55 ? 223 PRO   C CA  1 
ATOM   4213 C  C   . PRO   C 1 130 ? -36.110 -7.705  36.454  1.00 56.84 ? 223 PRO   C C   1 
ATOM   4214 O  O   . PRO   C 1 130 ? -35.630 -7.724  35.336  1.00 58.28 ? 223 PRO   C O   1 
ATOM   4215 C  CB  . PRO   C 1 130 ? -37.691 -5.734  36.914  1.00 54.81 ? 223 PRO   C CB  1 
ATOM   4216 C  CG  . PRO   C 1 130 ? -37.431 -4.260  36.632  1.00 53.92 ? 223 PRO   C CG  1 
ATOM   4217 C  CD  . PRO   C 1 130 ? -36.056 -4.200  35.990  1.00 53.21 ? 223 PRO   C CD  1 
ATOM   4218 N  N   . GLU   C 1 131 ? -36.473 -8.812  37.097  1.00 58.78 ? 224 GLU   C N   1 
ATOM   4219 C  CA  . GLU   C 1 131 ? -36.551 -10.158 36.451  1.00 61.31 ? 224 GLU   C CA  1 
ATOM   4220 C  C   . GLU   C 1 131 ? -37.731 -10.152 35.468  1.00 63.60 ? 224 GLU   C C   1 
ATOM   4221 O  O   . GLU   C 1 131 ? -38.643 -9.324  35.652  1.00 64.48 ? 224 GLU   C O   1 
ATOM   4222 C  CB  . GLU   C 1 131 ? -36.740 -11.281 37.473  1.00 61.23 ? 224 GLU   C CB  1 
ATOM   4223 C  CG  . GLU   C 1 131 ? -35.643 -11.388 38.522  1.00 59.70 ? 224 GLU   C CG  1 
ATOM   4224 C  CD  . GLU   C 1 131 ? -36.041 -12.205 39.739  1.00 59.82 ? 224 GLU   C CD  1 
ATOM   4225 O  OE1 . GLU   C 1 131 ? -36.736 -13.227 39.566  1.00 61.87 ? 224 GLU   C OE1 1 
ATOM   4226 O  OE2 . GLU   C 1 131 ? -35.677 -11.811 40.864  1.00 58.31 ? 224 GLU   C OE2 1 
ATOM   4227 N  N   . VAL   C 1 132 ? -37.716 -10.980 34.424  1.00 66.07 ? 225 VAL   C N   1 
ATOM   4228 C  CA  . VAL   C 1 132 ? -38.843 -11.001 33.439  1.00 67.52 ? 225 VAL   C CA  1 
ATOM   4229 C  C   . VAL   C 1 132 ? -40.095 -11.468 34.189  1.00 67.40 ? 225 VAL   C C   1 
ATOM   4230 O  O   . VAL   C 1 132 ? -40.034 -12.549 34.765  1.00 68.44 ? 225 VAL   C O   1 
ATOM   4231 C  CB  . VAL   C 1 132 ? -38.520 -11.863 32.208  1.00 70.46 ? 225 VAL   C CB  1 
ATOM   4232 C  CG1 . VAL   C 1 132 ? -39.730 -12.033 31.304  1.00 72.45 ? 225 VAL   C CG1 1 
ATOM   4233 C  CG2 . VAL   C 1 132 ? -37.344 -11.263 31.447  1.00 70.69 ? 225 VAL   C CG2 1 
ATOM   4234 N  N   . GLY   C 1 133 ? -41.154 -10.652 34.212  1.00 66.58 ? 226 GLY   C N   1 
ATOM   4235 C  CA  . GLY   C 1 133 ? -42.369 -10.881 35.024  1.00 65.54 ? 226 GLY   C CA  1 
ATOM   4236 C  C   . GLY   C 1 133 ? -42.542 -9.837  36.112  1.00 61.84 ? 226 GLY   C C   1 
ATOM   4237 O  O   . GLY   C 1 133 ? -43.693 -9.418  36.337  1.00 63.09 ? 226 GLY   C O   1 
ATOM   4238 N  N   . SER   C 1 134 ? -41.445 -9.393  36.736  1.00 59.13 ? 227 SER   C N   1 
ATOM   4239 C  CA  . SER   C 1 134 ? -41.415 -8.403  37.851  1.00 55.01 ? 227 SER   C CA  1 
ATOM   4240 C  C   . SER   C 1 134 ? -41.328 -6.971  37.295  1.00 53.73 ? 227 SER   C C   1 
ATOM   4241 O  O   . SER   C 1 134 ? -40.812 -6.805  36.160  1.00 53.19 ? 227 SER   C O   1 
ATOM   4242 C  CB  . SER   C 1 134 ? -40.256 -8.723  38.766  1.00 53.39 ? 227 SER   C CB  1 
ATOM   4243 O  OG  . SER   C 1 134 ? -40.063 -7.757  39.786  1.00 52.20 ? 227 SER   C OG  1 
ATOM   4244 N  N   . ASP   C 1 135 ? -41.769 -5.978  38.075  1.00 52.17 ? 228 ASP   C N   1 
ATOM   4245 C  CA  . ASP   C 1 135 ? -41.944 -4.581  37.585  1.00 51.63 ? 228 ASP   C CA  1 
ATOM   4246 C  C   . ASP   C 1 135 ? -40.894 -3.651  38.202  1.00 49.64 ? 228 ASP   C C   1 
ATOM   4247 O  O   . ASP   C 1 135 ? -40.840 -2.491  37.756  1.00 50.01 ? 228 ASP   C O   1 
ATOM   4248 C  CB  . ASP   C 1 135 ? -43.343 -4.057  37.891  1.00 52.39 ? 228 ASP   C CB  1 
ATOM   4249 C  CG  . ASP   C 1 135 ? -44.465 -4.847  37.251  1.00 53.83 ? 228 ASP   C CG  1 
ATOM   4250 O  OD1 . ASP   C 1 135 ? -44.322 -5.204  36.064  1.00 55.57 ? 228 ASP   C OD1 1 
ATOM   4251 O  OD2 . ASP   C 1 135 ? -45.478 -5.070  37.944  1.00 52.94 ? 228 ASP   C OD2 1 
ATOM   4252 N  N   . CYS   C 1 136 ? -40.122 -4.130  39.187  1.00 48.15 ? 229 CYS   C N   1 
ATOM   4253 C  CA  . CYS   C 1 136 ? -39.224 -3.270  39.994  1.00 46.17 ? 229 CYS   C CA  1 
ATOM   4254 C  C   . CYS   C 1 136 ? -37.972 -4.031  40.418  1.00 44.31 ? 229 CYS   C C   1 
ATOM   4255 O  O   . CYS   C 1 136 ? -37.970 -5.256  40.334  1.00 45.37 ? 229 CYS   C O   1 
ATOM   4256 C  CB  . CYS   C 1 136 ? -39.948 -2.707  41.207  1.00 45.40 ? 229 CYS   C CB  1 
ATOM   4257 S  SG  . CYS   C 1 136 ? -40.424 -3.946  42.430  1.00 46.01 ? 229 CYS   C SG  1 
ATOM   4258 N  N   . THR   C 1 137 ? -36.938 -3.292  40.816  1.00 42.21 ? 230 THR   C N   1 
ATOM   4259 C  CA  . THR   C 1 137 ? -35.695 -3.832  41.413  1.00 40.61 ? 230 THR   C CA  1 
ATOM   4260 C  C   . THR   C 1 137 ? -35.717 -3.516  42.906  1.00 37.99 ? 230 THR   C C   1 
ATOM   4261 O  O   . THR   C 1 137 ? -35.956 -2.326  43.250  1.00 38.73 ? 230 THR   C O   1 
ATOM   4262 C  CB  . THR   C 1 137 ? -34.464 -3.256  40.705  1.00 40.68 ? 230 THR   C CB  1 
ATOM   4263 O  OG1 . THR   C 1 137 ? -34.584 -3.595  39.322  1.00 42.29 ? 230 THR   C OG1 1 
ATOM   4264 C  CG2 . THR   C 1 137 ? -33.165 -3.774  41.273  1.00 40.27 ? 230 THR   C CG2 1 
ATOM   4265 N  N   . THR   C 1 138 ? -35.471 -4.517  43.758  1.00 35.48 ? 231 THR   C N   1 
ATOM   4266 C  CA  . THR   C 1 138 ? -35.451 -4.359  45.237  1.00 33.42 ? 231 THR   C CA  1 
ATOM   4267 C  C   . THR   C 1 138 ? -33.995 -4.314  45.710  1.00 32.37 ? 231 THR   C C   1 
ATOM   4268 O  O   . THR   C 1 138 ? -33.215 -5.185  45.286  1.00 31.64 ? 231 THR   C O   1 
ATOM   4269 C  CB  . THR   C 1 138 ? -36.257 -5.454  45.950  1.00 32.98 ? 231 THR   C CB  1 
ATOM   4270 O  OG1 . THR   C 1 138 ? -37.600 -5.399  45.488  1.00 33.12 ? 231 THR   C OG1 1 
ATOM   4271 C  CG2 . THR   C 1 138 ? -36.293 -5.291  47.452  1.00 32.12 ? 231 THR   C CG2 1 
ATOM   4272 N  N   . ILE   C 1 139 ? -33.661 -3.285  46.488  1.00 31.36 ? 232 ILE   C N   1 
ATOM   4273 C  CA  . ILE   C 1 139 ? -32.406 -3.159  47.285  1.00 30.75 ? 232 ILE   C CA  1 
ATOM   4274 C  C   . ILE   C 1 139 ? -32.770 -3.332  48.759  1.00 30.18 ? 232 ILE   C C   1 
ATOM   4275 O  O   . ILE   C 1 139 ? -33.792 -2.749  49.203  1.00 30.09 ? 232 ILE   C O   1 
ATOM   4276 C  CB  . ILE   C 1 139 ? -31.703 -1.811  47.025  1.00 31.10 ? 232 ILE   C CB  1 
ATOM   4277 C  CG1 . ILE   C 1 139 ? -31.284 -1.679  45.560  1.00 31.69 ? 232 ILE   C CG1 1 
ATOM   4278 C  CG2 . ILE   C 1 139 ? -30.525 -1.630  47.979  1.00 31.15 ? 232 ILE   C CG2 1 
ATOM   4279 C  CD1 . ILE   C 1 139 ? -30.817 -0.295  45.176  1.00 32.31 ? 232 ILE   C CD1 1 
ATOM   4280 N  N   . HIS   C 1 140 ? -31.962 -4.098  49.488  1.00 30.24 ? 233 HIS   C N   1 
ATOM   4281 C  CA  . HIS   C 1 140 ? -32.108 -4.346  50.946  1.00 30.72 ? 233 HIS   C CA  1 
ATOM   4282 C  C   . HIS   C 1 140 ? -31.141 -3.431  51.692  1.00 30.18 ? 233 HIS   C C   1 
ATOM   4283 O  O   . HIS   C 1 140 ? -29.948 -3.737  51.722  1.00 30.54 ? 233 HIS   C O   1 
ATOM   4284 C  CB  . HIS   C 1 140 ? -31.931 -5.843  51.265  1.00 31.98 ? 233 HIS   C CB  1 
ATOM   4285 C  CG  . HIS   C 1 140 ? -33.070 -6.680  50.798  1.00 33.33 ? 233 HIS   C CG  1 
ATOM   4286 N  ND1 . HIS   C 1 140 ? -33.007 -8.059  50.741  1.00 35.43 ? 233 HIS   C ND1 1 
ATOM   4287 C  CD2 . HIS   C 1 140 ? -34.312 -6.352  50.387  1.00 33.53 ? 233 HIS   C CD2 1 
ATOM   4288 C  CE1 . HIS   C 1 140 ? -34.155 -8.536  50.303  1.00 35.43 ? 233 HIS   C CE1 1 
ATOM   4289 N  NE2 . HIS   C 1 140 ? -34.965 -7.507  50.064  1.00 34.71 ? 233 HIS   C NE2 1 
ATOM   4290 N  N   . TYR   C 1 141 ? -31.648 -2.313  52.222  1.00 29.73 ? 234 TYR   C N   1 
ATOM   4291 C  CA  . TYR   C 1 141 ? -30.886 -1.389  53.096  1.00 29.18 ? 234 TYR   C CA  1 
ATOM   4292 C  C   . TYR   C 1 141 ? -30.965 -1.867  54.548  1.00 29.82 ? 234 TYR   C C   1 
ATOM   4293 O  O   . TYR   C 1 141 ? -32.002 -2.432  54.955  1.00 31.24 ? 234 TYR   C O   1 
ATOM   4294 C  CB  . TYR   C 1 141 ? -31.379 0.051   52.897  1.00 28.16 ? 234 TYR   C CB  1 
ATOM   4295 C  CG  . TYR   C 1 141 ? -31.050 0.608   51.537  1.00 27.63 ? 234 TYR   C CG  1 
ATOM   4296 C  CD1 . TYR   C 1 141 ? -29.734 0.889   51.202  1.00 26.89 ? 234 TYR   C CD1 1 
ATOM   4297 C  CD2 . TYR   C 1 141 ? -32.021 0.777   50.559  1.00 27.07 ? 234 TYR   C CD2 1 
ATOM   4298 C  CE1 . TYR   C 1 141 ? -29.395 1.395   49.957  1.00 27.51 ? 234 TYR   C CE1 1 
ATOM   4299 C  CE2 . TYR   C 1 141 ? -31.699 1.281   49.305  1.00 27.64 ? 234 TYR   C CE2 1 
ATOM   4300 C  CZ  . TYR   C 1 141 ? -30.377 1.578   49.000  1.00 27.86 ? 234 TYR   C CZ  1 
ATOM   4301 O  OH  . TYR   C 1 141 ? -30.007 2.049   47.775  1.00 28.83 ? 234 TYR   C OH  1 
ATOM   4302 N  N   . ASN   C 1 142 ? -29.884 -1.640  55.306  1.00 30.67 ? 235 ASN   C N   1 
ATOM   4303 C  CA  . ASN   C 1 142 ? -29.848 -1.717  56.788  1.00 31.22 ? 235 ASN   C CA  1 
ATOM   4304 C  C   . ASN   C 1 142 ? -29.429 -0.343  57.320  1.00 30.83 ? 235 ASN   C C   1 
ATOM   4305 O  O   . ASN   C 1 142 ? -28.421 0.183   56.847  1.00 30.89 ? 235 ASN   C O   1 
ATOM   4306 C  CB  . ASN   C 1 142 ? -28.855 -2.751  57.314  1.00 32.34 ? 235 ASN   C CB  1 
ATOM   4307 C  CG  . ASN   C 1 142 ? -29.093 -4.165  56.821  1.00 33.14 ? 235 ASN   C CG  1 
ATOM   4308 O  OD1 . ASN   C 1 142 ? -28.201 -4.999  56.904  1.00 34.43 ? 235 ASN   C OD1 1 
ATOM   4309 N  ND2 . ASN   C 1 142 ? -30.266 -4.446  56.287  1.00 33.34 ? 235 ASN   C ND2 1 
ATOM   4310 N  N   . TYR   C 1 143 ? -30.160 0.190   58.292  1.00 31.66 ? 236 TYR   C N   1 
ATOM   4311 C  CA  . TYR   C 1 143 ? -29.789 1.398   59.073  1.00 31.43 ? 236 TYR   C CA  1 
ATOM   4312 C  C   . TYR   C 1 143 ? -29.187 0.922   60.395  1.00 32.28 ? 236 TYR   C C   1 
ATOM   4313 O  O   . TYR   C 1 143 ? -29.825 0.129   61.107  1.00 33.57 ? 236 TYR   C O   1 
ATOM   4314 C  CB  . TYR   C 1 143 ? -31.002 2.323   59.213  1.00 31.10 ? 236 TYR   C CB  1 
ATOM   4315 C  CG  . TYR   C 1 143 ? -31.474 2.889   57.899  1.00 29.83 ? 236 TYR   C CG  1 
ATOM   4316 C  CD1 . TYR   C 1 143 ? -32.305 2.158   57.071  1.00 29.02 ? 236 TYR   C CD1 1 
ATOM   4317 C  CD2 . TYR   C 1 143 ? -31.095 4.157   57.486  1.00 29.56 ? 236 TYR   C CD2 1 
ATOM   4318 C  CE1 . TYR   C 1 143 ? -32.725 2.650   55.853  1.00 28.93 ? 236 TYR   C CE1 1 
ATOM   4319 C  CE2 . TYR   C 1 143 ? -31.493 4.658   56.258  1.00 28.86 ? 236 TYR   C CE2 1 
ATOM   4320 C  CZ  . TYR   C 1 143 ? -32.323 3.913   55.447  1.00 28.88 ? 236 TYR   C CZ  1 
ATOM   4321 O  OH  . TYR   C 1 143 ? -32.738 4.388   54.241  1.00 27.79 ? 236 TYR   C OH  1 
ATOM   4322 N  N   . MET   C 1 144 ? -27.970 1.372   60.689  1.00 32.59 ? 237 MET   C N   1 
ATOM   4323 C  CA  . MET   C 1 144 ? -27.084 0.769   61.713  1.00 34.01 ? 237 MET   C CA  1 
ATOM   4324 C  C   . MET   C 1 144 ? -27.034 1.635   62.988  1.00 34.48 ? 237 MET   C C   1 
ATOM   4325 O  O   . MET   C 1 144 ? -26.189 1.371   63.839  1.00 34.84 ? 237 MET   C O   1 
ATOM   4326 C  CB  . MET   C 1 144 ? -25.688 0.596   61.109  1.00 34.04 ? 237 MET   C CB  1 
ATOM   4327 C  CG  . MET   C 1 144 ? -25.652 -0.314  59.884  1.00 34.24 ? 237 MET   C CG  1 
ATOM   4328 S  SD  . MET   C 1 144 ? -26.445 -1.926  60.122  1.00 34.56 ? 237 MET   C SD  1 
ATOM   4329 C  CE  . MET   C 1 144 ? -25.537 -2.501  61.554  1.00 35.47 ? 237 MET   C CE  1 
ATOM   4330 N  N   . CYS   C 1 145 ? -27.936 2.604   63.132  1.00 35.81 ? 238 CYS   C N   1 
ATOM   4331 C  CA  . CYS   C 1 145 ? -28.089 3.488   64.329  1.00 37.68 ? 238 CYS   C CA  1 
ATOM   4332 C  C   . CYS   C 1 145 ? -29.583 3.790   64.503  1.00 38.46 ? 238 CYS   C C   1 
ATOM   4333 O  O   . CYS   C 1 145 ? -30.286 3.925   63.460  1.00 37.22 ? 238 CYS   C O   1 
ATOM   4334 C  CB  . CYS   C 1 145 ? -27.277 4.761   64.097  1.00 38.78 ? 238 CYS   C CB  1 
ATOM   4335 S  SG  . CYS   C 1 145 ? -26.430 5.599   65.436  1.00 41.46 ? 238 CYS   C SG  1 
ATOM   4336 N  N   . ASN   C 1 146 ? -30.058 3.871   65.750  1.00 38.76 ? 239 ASN   C N   1 
ATOM   4337 C  CA  . ASN   C 1 146 ? -31.437 4.310   66.082  1.00 39.53 ? 239 ASN   C CA  1 
ATOM   4338 C  C   . ASN   C 1 146 ? -31.503 5.836   65.970  1.00 39.33 ? 239 ASN   C C   1 
ATOM   4339 O  O   . ASN   C 1 146 ? -30.483 6.500   66.268  1.00 39.04 ? 239 ASN   C O   1 
ATOM   4340 C  CB  . ASN   C 1 146 ? -31.876 3.814   67.462  1.00 41.14 ? 239 ASN   C CB  1 
ATOM   4341 C  CG  . ASN   C 1 146 ? -32.325 2.369   67.456  1.00 41.90 ? 239 ASN   C CG  1 
ATOM   4342 O  OD1 . ASN   C 1 146 ? -33.082 1.937   66.583  1.00 41.96 ? 239 ASN   C OD1 1 
ATOM   4343 N  ND2 . ASN   C 1 146 ? -31.869 1.604   68.426  1.00 42.95 ? 239 ASN   C ND2 1 
ATOM   4344 N  N   . SER   C 1 147 ? -32.655 6.369   65.552  1.00 38.96 ? 240 SER   C N   1 
ATOM   4345 C  CA  . SER   C 1 147 ? -32.943 7.830   65.519  1.00 39.30 ? 240 SER   C CA  1 
ATOM   4346 C  C   . SER   C 1 147 ? -32.683 8.434   66.904  1.00 40.57 ? 240 SER   C C   1 
ATOM   4347 O  O   . SER   C 1 147 ? -32.285 9.606   66.961  1.00 42.48 ? 240 SER   C O   1 
ATOM   4348 C  CB  . SER   C 1 147 ? -34.363 8.102   65.055  1.00 38.93 ? 240 SER   C CB  1 
ATOM   4349 O  OG  . SER   C 1 147 ? -34.564 7.655   63.716  1.00 37.98 ? 240 SER   C OG  1 
ATOM   4350 N  N   . SER   C 1 148 ? -32.906 7.661   67.973  1.00 40.89 ? 241 SER   C N   1 
ATOM   4351 C  CA  . SER   C 1 148 ? -32.784 8.076   69.398  1.00 42.74 ? 241 SER   C CA  1 
ATOM   4352 C  C   . SER   C 1 148 ? -31.324 8.116   69.884  1.00 44.31 ? 241 SER   C C   1 
ATOM   4353 O  O   . SER   C 1 148 ? -31.095 8.733   70.940  1.00 46.97 ? 241 SER   C O   1 
ATOM   4354 C  CB  . SER   C 1 148 ? -33.601 7.164   70.272  1.00 43.09 ? 241 SER   C CB  1 
ATOM   4355 O  OG  . SER   C 1 148 ? -33.100 5.836   70.221  1.00 42.47 ? 241 SER   C OG  1 
ATOM   4356 N  N   . CYS   C 1 149 ? -30.377 7.482   69.179  1.00 43.04 ? 242 CYS   C N   1 
ATOM   4357 C  CA  . CYS   C 1 149 ? -28.971 7.289   69.643  1.00 44.34 ? 242 CYS   C CA  1 
ATOM   4358 C  C   . CYS   C 1 149 ? -28.350 8.610   70.121  1.00 45.74 ? 242 CYS   C C   1 
ATOM   4359 O  O   . CYS   C 1 149 ? -28.159 9.520   69.276  1.00 43.91 ? 242 CYS   C O   1 
ATOM   4360 C  CB  . CYS   C 1 149 ? -28.108 6.708   68.531  1.00 42.38 ? 242 CYS   C CB  1 
ATOM   4361 S  SG  . CYS   C 1 149 ? -28.153 4.952   68.395  1.00 42.04 ? 242 CYS   C SG  1 
ATOM   4362 N  N   . MET   C 1 150 ? -28.032 8.678   71.418  1.00 48.25 ? 243 MET   C N   1 
ATOM   4363 C  CA  . MET   C 1 150 ? -27.237 9.770   72.046  1.00 51.61 ? 243 MET   C CA  1 
ATOM   4364 C  C   . MET   C 1 150 ? -25.865 9.808   71.364  1.00 50.17 ? 243 MET   C C   1 
ATOM   4365 O  O   . MET   C 1 150 ? -25.268 8.723   71.172  1.00 48.60 ? 243 MET   C O   1 
ATOM   4366 C  CB  . MET   C 1 150 ? -27.030 9.537   73.550  1.00 55.31 ? 243 MET   C CB  1 
ATOM   4367 C  CG  . MET   C 1 150 ? -28.313 9.444   74.376  1.00 57.41 ? 243 MET   C CG  1 
ATOM   4368 S  SD  . MET   C 1 150 ? -28.050 8.908   76.114  1.00 62.29 ? 243 MET   C SD  1 
ATOM   4369 C  CE  . MET   C 1 150 ? -26.839 10.121  76.641  1.00 64.52 ? 243 MET   C CE  1 
ATOM   4370 N  N   . GLY   C 1 151 ? -25.398 10.996  70.967  1.00 50.17 ? 244 GLY   C N   1 
ATOM   4371 C  CA  . GLY   C 1 151 ? -24.078 11.180  70.334  1.00 50.10 ? 244 GLY   C CA  1 
ATOM   4372 C  C   . GLY   C 1 151 ? -24.060 10.683  68.901  1.00 48.38 ? 244 GLY   C C   1 
ATOM   4373 O  O   . GLY   C 1 151 ? -22.958 10.428  68.381  1.00 49.27 ? 244 GLY   C O   1 
ATOM   4374 N  N   . GLY   C 1 152 ? -25.240 10.541  68.293  1.00 47.86 ? 245 GLY   C N   1 
ATOM   4375 C  CA  . GLY   C 1 152 ? -25.418 10.229  66.862  1.00 46.49 ? 245 GLY   C CA  1 
ATOM   4376 C  C   . GLY   C 1 152 ? -26.477 11.115  66.263  1.00 46.01 ? 245 GLY   C C   1 
ATOM   4377 O  O   . GLY   C 1 152 ? -26.350 12.332  66.415  1.00 47.61 ? 245 GLY   C O   1 
ATOM   4378 N  N   . MET   C 1 153 ? -27.511 10.534  65.649  1.00 44.68 ? 246 MET   C N   1 
ATOM   4379 C  CA  . MET   C 1 153 ? -28.662 11.301  65.100  1.00 44.16 ? 246 MET   C CA  1 
ATOM   4380 C  C   . MET   C 1 153 ? -29.391 12.022  66.245  1.00 45.47 ? 246 MET   C C   1 
ATOM   4381 O  O   . MET   C 1 153 ? -29.851 13.162  66.017  1.00 46.19 ? 246 MET   C O   1 
ATOM   4382 C  CB  . MET   C 1 153 ? -29.620 10.373  64.354  1.00 42.93 ? 246 MET   C CB  1 
ATOM   4383 C  CG  . MET   C 1 153 ? -29.005 9.804   63.097  1.00 41.81 ? 246 MET   C CG  1 
ATOM   4384 S  SD  . MET   C 1 153 ? -30.230 8.943   62.102  1.00 40.36 ? 246 MET   C SD  1 
ATOM   4385 C  CE  . MET   C 1 153 ? -30.264 7.345   62.910  1.00 40.07 ? 246 MET   C CE  1 
ATOM   4386 N  N   . ASN   C 1 154 ? -29.461 11.389  67.423  1.00 46.64 ? 247 ASN   C N   1 
ATOM   4387 C  CA  . ASN   C 1 154 ? -29.948 11.993  68.691  1.00 49.14 ? 247 ASN   C CA  1 
ATOM   4388 C  C   . ASN   C 1 154 ? -31.289 12.684  68.434  1.00 49.55 ? 247 ASN   C C   1 
ATOM   4389 O  O   . ASN   C 1 154 ? -31.401 13.903  68.702  1.00 51.20 ? 247 ASN   C O   1 
ATOM   4390 C  CB  . ASN   C 1 154 ? -28.911 12.940  69.298  1.00 51.39 ? 247 ASN   C CB  1 
ATOM   4391 C  CG  . ASN   C 1 154 ? -29.324 13.469  70.657  1.00 53.97 ? 247 ASN   C CG  1 
ATOM   4392 O  OD1 . ASN   C 1 154 ? -29.950 12.763  71.451  1.00 55.50 ? 247 ASN   C OD1 1 
ATOM   4393 N  ND2 . ASN   C 1 154 ? -28.980 14.717  70.933  1.00 55.65 ? 247 ASN   C ND2 1 
ATOM   4394 N  N   . ARG   C 1 155 ? -32.248 11.914  67.909  1.00 48.00 ? 248 ARG   C N   1 
ATOM   4395 C  CA  . ARG   C 1 155 ? -33.694 12.258  67.780  1.00 48.41 ? 248 ARG   C CA  1 
ATOM   4396 C  C   . ARG   C 1 155 ? -33.921 13.198  66.589  1.00 46.52 ? 248 ARG   C C   1 
ATOM   4397 O  O   . ARG   C 1 155 ? -35.080 13.523  66.327  1.00 47.46 ? 248 ARG   C O   1 
ATOM   4398 C  CB  . ARG   C 1 155 ? -34.236 12.822  69.098  1.00 50.58 ? 248 ARG   C CB  1 
ATOM   4399 C  CG  . ARG   C 1 155 ? -34.021 11.871  70.268  1.00 52.43 ? 248 ARG   C CG  1 
ATOM   4400 C  CD  . ARG   C 1 155 ? -34.617 12.293  71.594  1.00 55.13 ? 248 ARG   C CD  1 
ATOM   4401 N  NE  . ARG   C 1 155 ? -35.790 11.490  71.933  1.00 56.07 ? 248 ARG   C NE  1 
ATOM   4402 C  CZ  . ARG   C 1 155 ? -37.037 11.750  71.542  1.00 56.98 ? 248 ARG   C CZ  1 
ATOM   4403 N  NH1 . ARG   C 1 155 ? -37.298 12.798  70.778  1.00 57.84 ? 248 ARG   C NH1 1 
ATOM   4404 N  NH2 . ARG   C 1 155 ? -38.029 10.959  71.917  1.00 56.96 ? 248 ARG   C NH2 1 
ATOM   4405 N  N   . ARG   C 1 156 ? -32.869 13.583  65.864  1.00 45.56 ? 249 ARG   C N   1 
ATOM   4406 C  CA  . ARG   C 1 156 ? -32.997 14.445  64.658  1.00 43.97 ? 249 ARG   C CA  1 
ATOM   4407 C  C   . ARG   C 1 156 ? -33.456 13.599  63.476  1.00 41.17 ? 249 ARG   C C   1 
ATOM   4408 O  O   . ARG   C 1 156 ? -32.872 12.548  63.195  1.00 41.20 ? 249 ARG   C O   1 
ATOM   4409 C  CB  . ARG   C 1 156 ? -31.678 15.158  64.364  1.00 44.20 ? 249 ARG   C CB  1 
ATOM   4410 C  CG  . ARG   C 1 156 ? -31.236 16.081  65.490  1.00 46.13 ? 249 ARG   C CG  1 
ATOM   4411 C  CD  . ARG   C 1 156 ? -29.873 16.660  65.227  1.00 46.14 ? 249 ARG   C CD  1 
ATOM   4412 N  NE  . ARG   C 1 156 ? -28.839 15.650  65.327  1.00 45.77 ? 249 ARG   C NE  1 
ATOM   4413 C  CZ  . ARG   C 1 156 ? -27.545 15.864  65.097  1.00 46.01 ? 249 ARG   C CZ  1 
ATOM   4414 N  NH1 . ARG   C 1 156 ? -27.116 17.069  64.749  1.00 47.19 ? 249 ARG   C NH1 1 
ATOM   4415 N  NH2 . ARG   C 1 156 ? -26.685 14.867  65.212  1.00 44.50 ? 249 ARG   C NH2 1 
ATOM   4416 N  N   . PRO   C 1 157 ? -34.506 14.034  62.743  1.00 39.15 ? 250 PRO   C N   1 
ATOM   4417 C  CA  . PRO   C 1 157 ? -34.987 13.297  61.581  1.00 36.89 ? 250 PRO   C CA  1 
ATOM   4418 C  C   . PRO   C 1 157 ? -33.999 13.402  60.410  1.00 36.50 ? 250 PRO   C C   1 
ATOM   4419 O  O   . PRO   C 1 157 ? -33.346 14.430  60.241  1.00 38.66 ? 250 PRO   C O   1 
ATOM   4420 C  CB  . PRO   C 1 157 ? -36.328 13.974  61.237  1.00 37.49 ? 250 PRO   C CB  1 
ATOM   4421 C  CG  . PRO   C 1 157 ? -36.180 15.386  61.768  1.00 39.41 ? 250 PRO   C CG  1 
ATOM   4422 C  CD  . PRO   C 1 157 ? -35.285 15.260  62.986  1.00 40.08 ? 250 PRO   C CD  1 
ATOM   4423 N  N   . ILE   C 1 158 ? -33.920 12.341  59.618  1.00 34.01 ? 251 ILE   C N   1 
ATOM   4424 C  CA  . ILE   C 1 158 ? -33.030 12.237  58.431  1.00 33.11 ? 251 ILE   C CA  1 
ATOM   4425 C  C   . ILE   C 1 158 ? -33.870 11.923  57.197  1.00 32.64 ? 251 ILE   C C   1 
ATOM   4426 O  O   . ILE   C 1 158 ? -34.996 11.391  57.333  1.00 32.81 ? 251 ILE   C O   1 
ATOM   4427 C  CB  . ILE   C 1 158 ? -31.924 11.203  58.668  1.00 32.22 ? 251 ILE   C CB  1 
ATOM   4428 C  CG1 . ILE   C 1 158 ? -32.481 9.809   58.969  1.00 31.32 ? 251 ILE   C CG1 1 
ATOM   4429 C  CG2 . ILE   C 1 158 ? -30.997 11.694  59.770  1.00 33.10 ? 251 ILE   C CG2 1 
ATOM   4430 C  CD1 . ILE   C 1 158 ? -31.531 8.684   58.620  1.00 30.64 ? 251 ILE   C CD1 1 
ATOM   4431 N  N   . LEU   C 1 159 ? -33.347 12.298  56.037  1.00 33.42 ? 252 LEU   C N   1 
ATOM   4432 C  CA  . LEU   C 1 159 ? -33.806 11.819  54.711  1.00 32.46 ? 252 LEU   C CA  1 
ATOM   4433 C  C   . LEU   C 1 159 ? -32.747 10.857  54.188  1.00 31.48 ? 252 LEU   C C   1 
ATOM   4434 O  O   . LEU   C 1 159 ? -31.543 11.092  54.454  1.00 30.17 ? 252 LEU   C O   1 
ATOM   4435 C  CB  . LEU   C 1 159 ? -33.966 12.996  53.746  1.00 33.98 ? 252 LEU   C CB  1 
ATOM   4436 C  CG  . LEU   C 1 159 ? -34.772 14.176  54.273  1.00 35.84 ? 252 LEU   C CG  1 
ATOM   4437 C  CD1 . LEU   C 1 159 ? -34.746 15.324  53.273  1.00 37.38 ? 252 LEU   C CD1 1 
ATOM   4438 C  CD2 . LEU   C 1 159 ? -36.206 13.757  54.594  1.00 35.68 ? 252 LEU   C CD2 1 
ATOM   4439 N  N   . THR   C 1 160 ? -33.185 9.818   53.480  1.00 30.87 ? 253 THR   C N   1 
ATOM   4440 C  CA  . THR   C 1 160 ? -32.343 9.017   52.560  1.00 30.42 ? 253 THR   C CA  1 
ATOM   4441 C  C   . THR   C 1 160 ? -32.574 9.534   51.145  1.00 31.16 ? 253 THR   C C   1 
ATOM   4442 O  O   . THR   C 1 160 ? -33.749 9.633   50.745  1.00 31.81 ? 253 THR   C O   1 
ATOM   4443 C  CB  . THR   C 1 160 ? -32.685 7.525   52.593  1.00 29.72 ? 253 THR   C CB  1 
ATOM   4444 O  OG1 . THR   C 1 160 ? -32.504 7.072   53.924  1.00 30.02 ? 253 THR   C OG1 1 
ATOM   4445 C  CG2 . THR   C 1 160 ? -31.819 6.716   51.655  1.00 29.31 ? 253 THR   C CG2 1 
ATOM   4446 N  N   . ILE   C 1 161 ? -31.499 9.840   50.424  1.00 31.30 ? 254 ILE   C N   1 
ATOM   4447 C  CA  . ILE   C 1 161 ? -31.532 10.287  49.005  1.00 31.97 ? 254 ILE   C CA  1 
ATOM   4448 C  C   . ILE   C 1 161 ? -31.006 9.132   48.167  1.00 32.07 ? 254 ILE   C C   1 
ATOM   4449 O  O   . ILE   C 1 161 ? -29.874 8.708   48.437  1.00 31.33 ? 254 ILE   C O   1 
ATOM   4450 C  CB  . ILE   C 1 161 ? -30.705 11.571  48.813  1.00 33.19 ? 254 ILE   C CB  1 
ATOM   4451 C  CG1 . ILE   C 1 161 ? -31.173 12.667  49.768  1.00 33.58 ? 254 ILE   C CG1 1 
ATOM   4452 C  CG2 . ILE   C 1 161 ? -30.760 12.029  47.367  1.00 34.60 ? 254 ILE   C CG2 1 
ATOM   4453 C  CD1 . ILE   C 1 161 ? -30.209 13.812  49.899  1.00 34.53 ? 254 ILE   C CD1 1 
ATOM   4454 N  N   . ILE   C 1 162 ? -31.846 8.592   47.276  1.00 32.87 ? 255 ILE   C N   1 
ATOM   4455 C  CA  . ILE   C 1 162 ? -31.497 7.503   46.318  1.00 33.12 ? 255 ILE   C CA  1 
ATOM   4456 C  C   . ILE   C 1 162 ? -31.288 8.168   44.962  1.00 35.37 ? 255 ILE   C C   1 
ATOM   4457 O  O   . ILE   C 1 162 ? -32.259 8.745   44.420  1.00 35.83 ? 255 ILE   C O   1 
ATOM   4458 C  CB  . ILE   C 1 162 ? -32.589 6.414   46.246  1.00 32.51 ? 255 ILE   C CB  1 
ATOM   4459 C  CG1 . ILE   C 1 162 ? -33.011 5.901   47.626  1.00 31.70 ? 255 ILE   C CG1 1 
ATOM   4460 C  CG2 . ILE   C 1 162 ? -32.159 5.288   45.323  1.00 31.98 ? 255 ILE   C CG2 1 
ATOM   4461 C  CD1 . ILE   C 1 162 ? -31.886 5.328   48.450  1.00 30.89 ? 255 ILE   C CD1 1 
ATOM   4462 N  N   . THR   C 1 163 ? -30.057 8.137   44.454  1.00 37.28 ? 256 THR   C N   1 
ATOM   4463 C  CA  . THR   C 1 163 ? -29.699 8.704   43.140  1.00 38.52 ? 256 THR   C CA  1 
ATOM   4464 C  C   . THR   C 1 163 ? -29.370 7.554   42.198  1.00 39.55 ? 256 THR   C C   1 
ATOM   4465 O  O   . THR   C 1 163 ? -28.712 6.589   42.621  1.00 39.23 ? 256 THR   C O   1 
ATOM   4466 C  CB  . THR   C 1 163 ? -28.564 9.725   43.249  1.00 39.90 ? 256 THR   C CB  1 
ATOM   4467 O  OG1 . THR   C 1 163 ? -27.410 9.035   43.719  1.00 39.97 ? 256 THR   C OG1 1 
ATOM   4468 C  CG2 . THR   C 1 163 ? -28.906 10.874  44.173  1.00 39.86 ? 256 THR   C CG2 1 
ATOM   4469 N  N   . LEU   C 1 164 ? -29.882 7.655   40.976  1.00 40.49 ? 257 LEU   C N   1 
ATOM   4470 C  CA  . LEU   C 1 164 ? -29.547 6.760   39.852  1.00 41.45 ? 257 LEU   C CA  1 
ATOM   4471 C  C   . LEU   C 1 164 ? -28.476 7.479   39.021  1.00 43.04 ? 257 LEU   C C   1 
ATOM   4472 O  O   . LEU   C 1 164 ? -28.693 8.643   38.674  1.00 43.20 ? 257 LEU   C O   1 
ATOM   4473 C  CB  . LEU   C 1 164 ? -30.847 6.516   39.085  1.00 42.34 ? 257 LEU   C CB  1 
ATOM   4474 C  CG  . LEU   C 1 164 ? -30.821 5.400   38.046  1.00 43.23 ? 257 LEU   C CG  1 
ATOM   4475 C  CD1 . LEU   C 1 164 ? -30.852 4.029   38.716  1.00 41.84 ? 257 LEU   C CD1 1 
ATOM   4476 C  CD2 . LEU   C 1 164 ? -31.977 5.591   37.068  1.00 45.16 ? 257 LEU   C CD2 1 
ATOM   4477 N  N   . GLU   C 1 165 ? -27.311 6.868   38.824  1.00 43.87 ? 258 GLU   C N   1 
ATOM   4478 C  CA  . GLU   C 1 165 ? -26.188 7.511   38.091  1.00 45.69 ? 258 GLU   C CA  1 
ATOM   4479 C  C   . GLU   C 1 165 ? -25.685 6.571   37.004  1.00 46.20 ? 258 GLU   C C   1 
ATOM   4480 O  O   . GLU   C 1 165 ? -25.839 5.348   37.159  1.00 44.58 ? 258 GLU   C O   1 
ATOM   4481 C  CB  . GLU   C 1 165 ? -25.027 7.908   39.005  1.00 45.02 ? 258 GLU   C CB  1 
ATOM   4482 C  CG  . GLU   C 1 165 ? -25.171 7.551   40.463  1.00 44.70 ? 258 GLU   C CG  1 
ATOM   4483 C  CD  . GLU   C 1 165 ? -23.953 7.948   41.278  0.80 44.55 ? 258 GLU   C CD  1 
ATOM   4484 O  OE1 . GLU   C 1 165 ? -22.888 7.331   41.066  0.80 44.24 ? 258 GLU   C OE1 1 
ATOM   4485 O  OE2 . GLU   C 1 165 ? -24.062 8.905   42.086  0.80 45.50 ? 258 GLU   C OE2 1 
ATOM   4486 N  N   . ASP   C 1 166 ? -25.088 7.139   35.958  1.00 48.44 ? 259 ASP   C N   1 
ATOM   4487 C  CA  . ASP   C 1 166 ? -24.434 6.361   34.883  1.00 50.09 ? 259 ASP   C CA  1 
ATOM   4488 C  C   . ASP   C 1 166 ? -23.064 5.930   35.402  1.00 49.58 ? 259 ASP   C C   1 
ATOM   4489 O  O   . ASP   C 1 166 ? -22.716 6.273   36.553  1.00 49.09 ? 259 ASP   C O   1 
ATOM   4490 C  CB  . ASP   C 1 166 ? -24.375 7.149   33.571  1.00 53.34 ? 259 ASP   C CB  1 
ATOM   4491 C  CG  . ASP   C 1 166 ? -23.431 8.344   33.547  1.00 54.76 ? 259 ASP   C CG  1 
ATOM   4492 O  OD1 . ASP   C 1 166 ? -22.592 8.471   34.461  1.00 54.11 ? 259 ASP   C OD1 1 
ATOM   4493 O  OD2 . ASP   C 1 166 ? -23.558 9.147   32.618  1.00 57.72 ? 259 ASP   C OD2 1 
ATOM   4494 N  N   . SER   C 1 167 ? -22.321 5.196   34.584  1.00 50.20 ? 260 SER   C N   1 
ATOM   4495 C  CA  . SER   C 1 167 ? -21.013 4.601   34.948  1.00 49.94 ? 260 SER   C CA  1 
ATOM   4496 C  C   . SER   C 1 167 ? -20.005 5.704   35.296  1.00 49.99 ? 260 SER   C C   1 
ATOM   4497 O  O   . SER   C 1 167 ? -19.098 5.417   36.076  1.00 49.20 ? 260 SER   C O   1 
ATOM   4498 C  CB  . SER   C 1 167 ? -20.541 3.697   33.853  1.00 51.04 ? 260 SER   C CB  1 
ATOM   4499 O  OG  . SER   C 1 167 ? -20.352 4.427   32.649  1.00 52.57 ? 260 SER   C OG  1 
ATOM   4500 N  N   . SER   C 1 168 ? -20.180 6.923   34.772  1.00 51.79 ? 261 SER   C N   1 
ATOM   4501 C  CA  . SER   C 1 168 ? -19.270 8.084   35.001  1.00 52.68 ? 261 SER   C CA  1 
ATOM   4502 C  C   . SER   C 1 168 ? -19.696 8.896   36.231  1.00 51.13 ? 261 SER   C C   1 
ATOM   4503 O  O   . SER   C 1 168 ? -18.951 9.813   36.608  1.00 51.05 ? 261 SER   C O   1 
ATOM   4504 C  CB  . SER   C 1 168 ? -19.190 8.974   33.789  1.00 54.88 ? 261 SER   C CB  1 
ATOM   4505 O  OG  . SER   C 1 168 ? -18.650 8.277   32.679  1.00 56.79 ? 261 SER   C OG  1 
ATOM   4506 N  N   . GLY   C 1 169 ? -20.841 8.577   36.836  1.00 50.19 ? 262 GLY   C N   1 
ATOM   4507 C  CA  . GLY   C 1 169 ? -21.371 9.275   38.027  1.00 48.74 ? 262 GLY   C CA  1 
ATOM   4508 C  C   . GLY   C 1 169 ? -22.313 10.424  37.678  1.00 49.89 ? 262 GLY   C C   1 
ATOM   4509 O  O   . GLY   C 1 169 ? -22.694 11.172  38.598  1.00 50.65 ? 262 GLY   C O   1 
ATOM   4510 N  N   . ASN   C 1 170 ? -22.715 10.556  36.414  1.00 51.02 ? 263 ASN   C N   1 
ATOM   4511 C  CA  . ASN   C 1 170 ? -23.678 11.603  35.975  1.00 51.56 ? 263 ASN   C CA  1 
ATOM   4512 C  C   . ASN   C 1 170 ? -25.076 11.233  36.488  1.00 49.53 ? 263 ASN   C C   1 
ATOM   4513 O  O   . ASN   C 1 170 ? -25.462 10.049  36.384  1.00 48.24 ? 263 ASN   C O   1 
ATOM   4514 C  CB  . ASN   C 1 170 ? -23.664 11.810  34.458  1.00 53.76 ? 263 ASN   C CB  1 
ATOM   4515 C  CG  . ASN   C 1 170 ? -22.319 12.269  33.933  1.00 55.42 ? 263 ASN   C CG  1 
ATOM   4516 O  OD1 . ASN   C 1 170 ? -21.778 13.284  34.382  1.00 55.54 ? 263 ASN   C OD1 1 
ATOM   4517 N  ND2 . ASN   C 1 170 ? -21.776 11.531  32.980  1.00 55.62 ? 263 ASN   C ND2 1 
ATOM   4518 N  N   . LEU   C 1 171 ? -25.774 12.204  37.073  1.00 48.77 ? 264 LEU   C N   1 
ATOM   4519 C  CA  . LEU   C 1 171 ? -27.134 12.047  37.654  1.00 47.75 ? 264 LEU   C CA  1 
ATOM   4520 C  C   . LEU   C 1 171 ? -28.122 11.651  36.549  1.00 48.06 ? 264 LEU   C C   1 
ATOM   4521 O  O   . LEU   C 1 171 ? -28.202 12.380  35.565  1.00 49.80 ? 264 LEU   C O   1 
ATOM   4522 C  CB  . LEU   C 1 171 ? -27.534 13.369  38.321  1.00 48.03 ? 264 LEU   C CB  1 
ATOM   4523 C  CG  . LEU   C 1 171 ? -28.952 13.449  38.888  1.00 48.01 ? 264 LEU   C CG  1 
ATOM   4524 C  CD1 . LEU   C 1 171 ? -29.074 12.639  40.172  1.00 46.31 ? 264 LEU   C CD1 1 
ATOM   4525 C  CD2 . LEU   C 1 171 ? -29.340 14.901  39.129  1.00 49.23 ? 264 LEU   C CD2 1 
ATOM   4526 N  N   . LEU   C 1 172 ? -28.837 10.531  36.718  1.00 47.05 ? 265 LEU   C N   1 
ATOM   4527 C  CA  . LEU   C 1 172 ? -29.945 10.079  35.819  1.00 48.89 ? 265 LEU   C CA  1 
ATOM   4528 C  C   . LEU   C 1 172 ? -31.304 10.308  36.492  1.00 48.64 ? 265 LEU   C C   1 
ATOM   4529 O  O   . LEU   C 1 172 ? -32.285 10.564  35.774  1.00 51.80 ? 265 LEU   C O   1 
ATOM   4530 C  CB  . LEU   C 1 172 ? -29.778 8.592   35.491  1.00 48.01 ? 265 LEU   C CB  1 
ATOM   4531 C  CG  . LEU   C 1 172 ? -28.417 8.177   34.938  1.00 48.88 ? 265 LEU   C CG  1 
ATOM   4532 C  CD1 . LEU   C 1 172 ? -28.438 6.706   34.529  1.00 48.93 ? 265 LEU   C CD1 1 
ATOM   4533 C  CD2 . LEU   C 1 172 ? -28.013 9.048   33.763  1.00 51.26 ? 265 LEU   C CD2 1 
ATOM   4534 N  N   . GLY   C 1 173 ? -31.374 10.154  37.816  1.00 47.20 ? 266 GLY   C N   1 
ATOM   4535 C  CA  . GLY   C 1 173 ? -32.616 10.251  38.597  1.00 46.51 ? 266 GLY   C CA  1 
ATOM   4536 C  C   . GLY   C 1 173 ? -32.337 10.394  40.078  1.00 44.95 ? 266 GLY   C C   1 
ATOM   4537 O  O   . GLY   C 1 173 ? -31.280 9.924   40.537  1.00 46.59 ? 266 GLY   C O   1 
ATOM   4538 N  N   . ARG   C 1 174 ? -33.250 11.028  40.811  1.00 43.98 ? 267 ARG   C N   1 
ATOM   4539 C  CA  . ARG   C 1 174 ? -33.145 11.203  42.278  1.00 41.89 ? 267 ARG   C CA  1 
ATOM   4540 C  C   . ARG   C 1 174 ? -34.540 11.154  42.904  1.00 41.35 ? 267 ARG   C C   1 
ATOM   4541 O  O   . ARG   C 1 174 ? -35.486 11.744  42.351  1.00 43.23 ? 267 ARG   C O   1 
ATOM   4542 C  CB  . ARG   C 1 174 ? -32.457 12.521  42.624  1.00 42.89 ? 267 ARG   C CB  1 
ATOM   4543 C  CG  . ARG   C 1 174 ? -32.180 12.704  44.107  1.00 41.63 ? 267 ARG   C CG  1 
ATOM   4544 C  CD  . ARG   C 1 174 ? -31.821 14.137  44.434  1.00 42.89 ? 267 ARG   C CD  1 
ATOM   4545 N  NE  . ARG   C 1 174 ? -30.591 14.556  43.778  1.00 43.38 ? 267 ARG   C NE  1 
ATOM   4546 C  CZ  . ARG   C 1 174 ? -30.480 15.517  42.855  1.00 45.35 ? 267 ARG   C CZ  1 
ATOM   4547 N  NH1 . ARG   C 1 174 ? -31.531 16.207  42.435  1.00 46.13 ? 267 ARG   C NH1 1 
ATOM   4548 N  NH2 . ARG   C 1 174 ? -29.288 15.794  42.358  1.00 45.73 ? 267 ARG   C NH2 1 
ATOM   4549 N  N   A ASN   C 1 175 ? -34.647 10.459  44.035  0.50 39.51 ? 268 ASN   C N   1 
ATOM   4550 N  N   B ASN   C 1 175 ? -34.676 10.439  44.023  0.50 39.41 ? 268 ASN   C N   1 
ATOM   4551 C  CA  A ASN   C 1 175 ? -35.829 10.467  44.929  0.50 38.96 ? 268 ASN   C CA  1 
ATOM   4552 C  CA  B ASN   C 1 175 ? -35.840 10.592  44.934  0.50 38.90 ? 268 ASN   C CA  1 
ATOM   4553 C  C   A ASN   C 1 175 ? -35.324 10.483  46.369  0.50 37.63 ? 268 ASN   C C   1 
ATOM   4554 C  C   B ASN   C 1 175 ? -35.333 10.473  46.369  0.50 37.51 ? 268 ASN   C C   1 
ATOM   4555 O  O   A ASN   C 1 175 ? -34.110 10.358  46.582  0.50 37.94 ? 268 ASN   C O   1 
ATOM   4556 O  O   B ASN   C 1 175 ? -34.121 10.302  46.577  0.50 37.73 ? 268 ASN   C O   1 
ATOM   4557 C  CB  A ASN   C 1 175 ? -36.739 9.272   44.656  0.50 38.77 ? 268 ASN   C CB  1 
ATOM   4558 C  CB  B ASN   C 1 175 ? -37.008 9.648   44.605  0.50 38.86 ? 268 ASN   C CB  1 
ATOM   4559 C  CG  A ASN   C 1 175 ? -37.543 9.410   43.387  0.50 39.81 ? 268 ASN   C CG  1 
ATOM   4560 C  CG  B ASN   C 1 175 ? -38.345 10.367  44.619  0.50 39.50 ? 268 ASN   C CG  1 
ATOM   4561 O  OD1 A ASN   C 1 175 ? -38.591 10.049  43.378  0.50 40.80 ? 268 ASN   C OD1 1 
ATOM   4562 O  OD1 B ASN   C 1 175 ? -38.568 11.261  45.434  0.50 39.18 ? 268 ASN   C OD1 1 
ATOM   4563 N  ND2 A ASN   C 1 175 ? -37.067 8.797   42.319  0.50 40.19 ? 268 ASN   C ND2 1 
ATOM   4564 N  ND2 B ASN   C 1 175 ? -39.223 10.023  43.694  0.50 40.31 ? 268 ASN   C ND2 1 
ATOM   4565 N  N   . SER   C 1 176 ? -36.242 10.622  47.322  1.00 36.98 ? 269 SER   C N   1 
ATOM   4566 C  CA  . SER   C 1 176 ? -35.933 10.733  48.757  1.00 35.09 ? 269 SER   C CA  1 
ATOM   4567 C  C   . SER   C 1 176 ? -37.138 10.254  49.561  1.00 33.49 ? 269 SER   C C   1 
ATOM   4568 O  O   . SER   C 1 176 ? -38.254 10.223  49.027  1.00 33.48 ? 269 SER   C O   1 
ATOM   4569 C  CB  . SER   C 1 176 ? -35.550 12.136  49.098  1.00 36.25 ? 269 SER   C CB  1 
ATOM   4570 O  OG  . SER   C 1 176 ? -36.610 13.012  48.799  1.00 37.46 ? 269 SER   C OG  1 
ATOM   4571 N  N   . PHE   C 1 177 ? -36.881 9.864   50.798  1.00 32.25 ? 270 PHE   C N   1 
ATOM   4572 C  CA  . PHE   C 1 177 ? -37.907 9.507   51.801  1.00 31.56 ? 270 PHE   C CA  1 
ATOM   4573 C  C   . PHE   C 1 177 ? -37.291 9.761   53.175  1.00 31.12 ? 270 PHE   C C   1 
ATOM   4574 O  O   . PHE   C 1 177 ? -36.053 9.564   53.347  1.00 30.57 ? 270 PHE   C O   1 
ATOM   4575 C  CB  . PHE   C 1 177 ? -38.375 8.065   51.597  1.00 30.31 ? 270 PHE   C CB  1 
ATOM   4576 C  CG  . PHE   C 1 177 ? -37.278 7.030   51.594  1.00 29.18 ? 270 PHE   C CG  1 
ATOM   4577 C  CD1 . PHE   C 1 177 ? -36.576 6.743   50.434  1.00 29.21 ? 270 PHE   C CD1 1 
ATOM   4578 C  CD2 . PHE   C 1 177 ? -36.953 6.331   52.746  1.00 28.86 ? 270 PHE   C CD2 1 
ATOM   4579 C  CE1 . PHE   C 1 177 ? -35.581 5.782   50.418  1.00 28.48 ? 270 PHE   C CE1 1 
ATOM   4580 C  CE2 . PHE   C 1 177 ? -35.952 5.369   52.736  1.00 28.09 ? 270 PHE   C CE2 1 
ATOM   4581 C  CZ  . PHE   C 1 177 ? -35.263 5.099   51.572  1.00 27.99 ? 270 PHE   C CZ  1 
ATOM   4582 N  N   . GLU   C 1 178 ? -38.116 10.248  54.101  1.00 31.20 ? 271 GLU   C N   1 
ATOM   4583 C  CA  . GLU   C 1 178 ? -37.758 10.400  55.526  1.00 31.41 ? 271 GLU   C CA  1 
ATOM   4584 C  C   . GLU   C 1 178 ? -37.616 8.994   56.111  1.00 30.59 ? 271 GLU   C C   1 
ATOM   4585 O  O   . GLU   C 1 178 ? -38.286 8.073   55.605  1.00 29.71 ? 271 GLU   C O   1 
ATOM   4586 C  CB  . GLU   C 1 178 ? -38.795 11.241  56.268  1.00 32.07 ? 271 GLU   C CB  1 
ATOM   4587 C  CG  . GLU   C 1 178 ? -38.332 11.649  57.659  1.00 33.20 ? 271 GLU   C CG  1 
ATOM   4588 C  CD  . GLU   C 1 178 ? -39.186 12.706  58.347  1.00 34.88 ? 271 GLU   C CD  1 
ATOM   4589 O  OE1 . GLU   C 1 178 ? -39.170 12.776  59.604  1.00 35.97 ? 271 GLU   C OE1 1 
ATOM   4590 O  OE2 . GLU   C 1 178 ? -39.863 13.462  57.623  1.00 35.49 ? 271 GLU   C OE2 1 
ATOM   4591 N  N   . VAL   C 1 179 ? -36.726 8.838   57.093  1.00 30.50 ? 272 VAL   C N   1 
ATOM   4592 C  CA  . VAL   C 1 179 ? -36.465 7.547   57.787  1.00 30.73 ? 272 VAL   C CA  1 
ATOM   4593 C  C   . VAL   C 1 179 ? -36.493 7.806   59.292  1.00 32.22 ? 272 VAL   C C   1 
ATOM   4594 O  O   . VAL   C 1 179 ? -35.896 8.804   59.756  1.00 32.50 ? 272 VAL   C O   1 
ATOM   4595 C  CB  . VAL   C 1 179 ? -35.142 6.898   57.335  1.00 30.51 ? 272 VAL   C CB  1 
ATOM   4596 C  CG1 . VAL   C 1 179 ? -34.826 5.635   58.116  1.00 30.34 ? 272 VAL   C CG1 1 
ATOM   4597 C  CG2 . VAL   C 1 179 ? -35.128 6.600   55.854  1.00 29.93 ? 272 VAL   C CG2 1 
ATOM   4598 N  N   . ARG   C 1 180 ? -37.200 6.950   60.023  1.00 32.44 ? 273 ARG   C N   1 
ATOM   4599 C  CA  . ARG   C 1 180 ? -37.065 6.835   61.489  1.00 33.43 ? 273 ARG   C CA  1 
ATOM   4600 C  C   . ARG   C 1 180 ? -36.604 5.412   61.785  1.00 32.83 ? 273 ARG   C C   1 
ATOM   4601 O  O   . ARG   C 1 180 ? -37.296 4.470   61.329  1.00 32.01 ? 273 ARG   C O   1 
ATOM   4602 C  CB  . ARG   C 1 180 ? -38.403 7.145   62.157  1.00 35.55 ? 273 ARG   C CB  1 
ATOM   4603 C  CG  . ARG   C 1 180 ? -38.370 6.861   63.646  1.00 37.09 ? 273 ARG   C CG  1 
ATOM   4604 C  CD  . ARG   C 1 180 ? -39.371 7.733   64.348  1.00 39.40 ? 273 ARG   C CD  1 
ATOM   4605 N  NE  . ARG   C 1 180 ? -39.774 7.210   65.642  1.00 41.05 ? 273 ARG   C NE  1 
ATOM   4606 C  CZ  . ARG   C 1 180 ? -39.259 7.570   66.809  1.00 43.18 ? 273 ARG   C CZ  1 
ATOM   4607 N  NH1 . ARG   C 1 180 ? -39.754 7.068   67.931  1.00 44.54 ? 273 ARG   C NH1 1 
ATOM   4608 N  NH2 . ARG   C 1 180 ? -38.237 8.411   66.857  1.00 44.13 ? 273 ARG   C NH2 1 
ATOM   4609 N  N   . VAL   C 1 181 ? -35.461 5.268   62.449  1.00 32.54 ? 274 VAL   C N   1 
ATOM   4610 C  CA  . VAL   C 1 181 ? -34.978 3.944   62.923  1.00 33.22 ? 274 VAL   C CA  1 
ATOM   4611 C  C   . VAL   C 1 181 ? -35.403 3.838   64.387  1.00 33.72 ? 274 VAL   C C   1 
ATOM   4612 O  O   . VAL   C 1 181 ? -34.964 4.675   65.167  1.00 33.54 ? 274 VAL   C O   1 
ATOM   4613 C  CB  . VAL   C 1 181 ? -33.461 3.768   62.714  1.00 32.82 ? 274 VAL   C CB  1 
ATOM   4614 C  CG1 . VAL   C 1 181 ? -33.046 2.323   62.896  1.00 32.66 ? 274 VAL   C CG1 1 
ATOM   4615 C  CG2 . VAL   C 1 181 ? -33.021 4.264   61.352  1.00 32.15 ? 274 VAL   C CG2 1 
ATOM   4616 N  N   . CYS   C 1 182 ? -36.274 2.878   64.716  1.00 33.87 ? 275 CYS   C N   1 
ATOM   4617 C  CA  . CYS   C 1 182 ? -36.937 2.796   66.045  1.00 35.90 ? 275 CYS   C CA  1 
ATOM   4618 C  C   . CYS   C 1 182 ? -37.238 1.336   66.382  1.00 35.35 ? 275 CYS   C C   1 
ATOM   4619 O  O   . CYS   C 1 182 ? -37.187 0.495   65.473  1.00 35.16 ? 275 CYS   C O   1 
ATOM   4620 C  CB  . CYS   C 1 182 ? -38.207 3.647   66.099  1.00 37.09 ? 275 CYS   C CB  1 
ATOM   4621 S  SG  . CYS   C 1 182 ? -39.366 3.344   64.738  1.00 38.41 ? 275 CYS   C SG  1 
ATOM   4622 N  N   . ALA   C 1 183 ? -37.530 1.069   67.651  1.00 36.80 ? 276 ALA   C N   1 
ATOM   4623 C  CA  . ALA   C 1 183 ? -37.806 -0.272  68.215  1.00 37.12 ? 276 ALA   C CA  1 
ATOM   4624 C  C   . ALA   C 1 183 ? -39.125 -0.805  67.657  1.00 36.59 ? 276 ALA   C C   1 
ATOM   4625 O  O   . ALA   C 1 183 ? -39.192 -2.023  67.380  1.00 35.76 ? 276 ALA   C O   1 
ATOM   4626 C  CB  . ALA   C 1 183 ? -37.851 -0.193  69.726  1.00 38.65 ? 276 ALA   C CB  1 
ATOM   4627 N  N   . CYS   C 1 184 ? -40.135 0.058   67.508  1.00 36.59 ? 277 CYS   C N   1 
ATOM   4628 C  CA  . CYS   C 1 184 ? -41.531 -0.349  67.186  1.00 37.72 ? 277 CYS   C CA  1 
ATOM   4629 C  C   . CYS   C 1 184 ? -42.054 0.457   66.001  1.00 35.93 ? 277 CYS   C C   1 
ATOM   4630 O  O   . CYS   C 1 184 ? -42.806 1.411   66.178  1.00 36.59 ? 277 CYS   C O   1 
ATOM   4631 C  CB  . CYS   C 1 184 ? -42.444 -0.168  68.395  1.00 40.45 ? 277 CYS   C CB  1 
ATOM   4632 S  SG  . CYS   C 1 184 ? -41.922 -1.023  69.909  1.00 44.70 ? 277 CYS   C SG  1 
ATOM   4633 N  N   . PRO   C 1 185 ? -41.666 0.100   64.753  1.00 33.89 ? 278 PRO   C N   1 
ATOM   4634 C  CA  . PRO   C 1 185 ? -42.066 0.850   63.566  1.00 32.74 ? 278 PRO   C CA  1 
ATOM   4635 C  C   . PRO   C 1 185 ? -43.588 0.933   63.359  1.00 33.26 ? 278 PRO   C C   1 
ATOM   4636 O  O   . PRO   C 1 185 ? -44.093 2.022   63.057  1.00 31.47 ? 278 PRO   C O   1 
ATOM   4637 C  CB  . PRO   C 1 185 ? -41.444 0.066   62.403  1.00 32.52 ? 278 PRO   C CB  1 
ATOM   4638 C  CG  . PRO   C 1 185 ? -40.331 -0.747  63.025  1.00 32.58 ? 278 PRO   C CG  1 
ATOM   4639 C  CD  . PRO   C 1 185 ? -40.812 -1.053  64.424  1.00 33.49 ? 278 PRO   C CD  1 
ATOM   4640 N  N   . GLY   C 1 186 ? -44.283 -0.201  63.537  1.00 33.55 ? 279 GLY   C N   1 
ATOM   4641 C  CA  . GLY   C 1 186 ? -45.755 -0.269  63.473  1.00 34.71 ? 279 GLY   C CA  1 
ATOM   4642 C  C   . GLY   C 1 186 ? -46.409 0.768   64.371  1.00 35.80 ? 279 GLY   C C   1 
ATOM   4643 O  O   . GLY   C 1 186 ? -47.207 1.584   63.853  1.00 35.06 ? 279 GLY   C O   1 
ATOM   4644 N  N   . ARG   C 1 187 ? -46.054 0.765   65.659  1.00 36.75 ? 280 ARG   C N   1 
ATOM   4645 C  CA  . ARG   C 1 187 ? -46.640 1.668   66.681  1.00 38.99 ? 280 ARG   C CA  1 
ATOM   4646 C  C   . ARG   C 1 187 ? -46.288 3.113   66.330  1.00 38.53 ? 280 ARG   C C   1 
ATOM   4647 O  O   . ARG   C 1 187 ? -47.184 3.966   66.399  1.00 38.50 ? 280 ARG   C O   1 
ATOM   4648 C  CB  . ARG   C 1 187 ? -46.154 1.311   68.089  1.00 40.24 ? 280 ARG   C CB  1 
ATOM   4649 C  CG  . ARG   C 1 187 ? -46.795 2.125   69.204  1.00 42.23 ? 280 ARG   C CG  1 
ATOM   4650 C  CD  . ARG   C 1 187 ? -46.191 1.808   70.570  1.00 44.31 ? 280 ARG   C CD  1 
ATOM   4651 N  NE  . ARG   C 1 187 ? -44.770 2.148   70.614  1.00 44.75 ? 280 ARG   C NE  1 
ATOM   4652 C  CZ  . ARG   C 1 187 ? -43.837 1.560   71.369  1.00 45.93 ? 280 ARG   C CZ  1 
ATOM   4653 N  NH1 . ARG   C 1 187 ? -44.137 0.538   72.157  1.00 48.04 ? 280 ARG   C NH1 1 
ATOM   4654 N  NH2 . ARG   C 1 187 ? -42.582 1.967   71.275  1.00 45.36 ? 280 ARG   C NH2 1 
ATOM   4655 N  N   . ASP   C 1 188 ? -45.030 3.374   65.973  1.00 38.26 ? 281 ASP   C N   1 
ATOM   4656 C  CA  . ASP   C 1 188 ? -44.536 4.753   65.719  1.00 37.96 ? 281 ASP   C CA  1 
ATOM   4657 C  C   . ASP   C 1 188 ? -45.196 5.306   64.443  1.00 36.97 ? 281 ASP   C C   1 
ATOM   4658 O  O   . ASP   C 1 188 ? -45.558 6.504   64.445  1.00 37.40 ? 281 ASP   C O   1 
ATOM   4659 C  CB  . ASP   C 1 188 ? -43.008 4.772   65.699  1.00 37.65 ? 281 ASP   C CB  1 
ATOM   4660 C  CG  . ASP   C 1 188 ? -42.366 4.488   67.052  1.00 39.15 ? 281 ASP   C CG  1 
ATOM   4661 O  OD1 . ASP   C 1 188 ? -43.098 4.379   68.070  1.00 41.21 ? 281 ASP   C OD1 1 
ATOM   4662 O  OD2 . ASP   C 1 188 ? -41.134 4.400   67.084  1.00 39.82 ? 281 ASP   C OD2 1 
ATOM   4663 N  N   . ARG   C 1 189 ? -45.368 4.488   63.396  1.00 34.91 ? 282 ARG   C N   1 
ATOM   4664 C  CA  . ARG   C 1 189 ? -46.089 4.929   62.169  1.00 34.29 ? 282 ARG   C CA  1 
ATOM   4665 C  C   . ARG   C 1 189 ? -47.531 5.310   62.543  1.00 35.32 ? 282 ARG   C C   1 
ATOM   4666 O  O   . ARG   C 1 189 ? -47.960 6.430   62.181  1.00 35.89 ? 282 ARG   C O   1 
ATOM   4667 C  CB  . ARG   C 1 189 ? -46.078 3.867   61.062  1.00 32.88 ? 282 ARG   C CB  1 
ATOM   4668 C  CG  . ARG   C 1 189 ? -46.903 4.289   59.847  1.00 32.50 ? 282 ARG   C CG  1 
ATOM   4669 C  CD  . ARG   C 1 189 ? -46.780 3.379   58.641  1.00 31.29 ? 282 ARG   C CD  1 
ATOM   4670 N  NE  . ARG   C 1 189 ? -47.885 3.617   57.735  1.00 31.11 ? 282 ARG   C NE  1 
ATOM   4671 C  CZ  . ARG   C 1 189 ? -48.379 2.746   56.868  1.00 31.03 ? 282 ARG   C CZ  1 
ATOM   4672 N  NH1 . ARG   C 1 189 ? -47.835 1.551   56.739  1.00 30.48 ? 282 ARG   C NH1 1 
ATOM   4673 N  NH2 . ARG   C 1 189 ? -49.403 3.090   56.107  1.00 31.12 ? 282 ARG   C NH2 1 
ATOM   4674 N  N   . ARG   C 1 190 ? -48.244 4.425   63.248  1.00 35.69 ? 283 ARG   C N   1 
ATOM   4675 C  CA  . ARG   C 1 190 ? -49.663 4.633   63.640  1.00 36.98 ? 283 ARG   C CA  1 
ATOM   4676 C  C   . ARG   C 1 190 ? -49.790 5.940   64.429  1.00 37.97 ? 283 ARG   C C   1 
ATOM   4677 O  O   . ARG   C 1 190 ? -50.686 6.758   64.098  1.00 36.92 ? 283 ARG   C O   1 
ATOM   4678 C  CB  . ARG   C 1 190 ? -50.182 3.468   64.483  1.00 37.55 ? 283 ARG   C CB  1 
ATOM   4679 C  CG  . ARG   C 1 190 ? -51.526 2.955   63.990  1.00 38.08 ? 283 ARG   C CG  1 
ATOM   4680 C  CD  . ARG   C 1 190 ? -52.112 1.851   64.838  1.00 38.90 ? 283 ARG   C CD  1 
ATOM   4681 N  NE  . ARG   C 1 190 ? -51.676 0.533   64.397  1.00 38.06 ? 283 ARG   C NE  1 
ATOM   4682 C  CZ  . ARG   C 1 190 ? -52.141 -0.607  64.882  1.00 39.01 ? 283 ARG   C CZ  1 
ATOM   4683 N  NH1 . ARG   C 1 190 ? -51.692 -1.757  64.422  1.00 39.38 ? 283 ARG   C NH1 1 
ATOM   4684 N  NH2 . ARG   C 1 190 ? -53.095 -0.603  65.791  1.00 40.05 ? 283 ARG   C NH2 1 
ATOM   4685 N  N   . THR   C 1 191 ? -48.922 6.120   65.424  1.00 38.59 ? 284 THR   C N   1 
ATOM   4686 C  CA  . THR   C 1 191 ? -48.911 7.307   66.320  1.00 40.35 ? 284 THR   C CA  1 
ATOM   4687 C  C   . THR   C 1 191 ? -48.687 8.569   65.479  1.00 40.65 ? 284 THR   C C   1 
ATOM   4688 O  O   . THR   C 1 191 ? -49.483 9.513   65.637  1.00 41.88 ? 284 THR   C O   1 
ATOM   4689 C  CB  . THR   C 1 191 ? -47.862 7.120   67.423  1.00 40.18 ? 284 THR   C CB  1 
ATOM   4690 O  OG1 . THR   C 1 191 ? -48.178 5.894   68.075  1.00 40.42 ? 284 THR   C OG1 1 
ATOM   4691 C  CG2 . THR   C 1 191 ? -47.845 8.239   68.441  1.00 41.41 ? 284 THR   C CG2 1 
ATOM   4692 N  N   . GLU   C 1 192 ? -47.681 8.570   64.596  1.00 40.90 ? 285 GLU   C N   1 
ATOM   4693 C  CA  . GLU   C 1 192 ? -47.296 9.765   63.794  1.00 41.85 ? 285 GLU   C CA  1 
ATOM   4694 C  C   . GLU   C 1 192 ? -48.412 10.115  62.797  1.00 42.55 ? 285 GLU   C C   1 
ATOM   4695 O  O   . GLU   C 1 192 ? -48.623 11.323  62.567  1.00 43.27 ? 285 GLU   C O   1 
ATOM   4696 C  CB  . GLU   C 1 192 ? -45.957 9.551   63.082  1.00 41.60 ? 285 GLU   C CB  1 
ATOM   4697 C  CG  . GLU   C 1 192 ? -44.760 9.680   64.004  1.00 42.32 ? 285 GLU   C CG  1 
ATOM   4698 C  CD  . GLU   C 1 192 ? -43.452 10.076  63.340  1.00 42.42 ? 285 GLU   C CD  1 
ATOM   4699 O  OE1 . GLU   C 1 192 ? -43.484 10.682  62.238  1.00 43.47 ? 285 GLU   C OE1 1 
ATOM   4700 O  OE2 . GLU   C 1 192 ? -42.394 9.786   63.925  1.00 41.41 ? 285 GLU   C OE2 1 
ATOM   4701 N  N   . GLU   C 1 193 ? -49.129 9.120   62.258  1.00 42.47 ? 286 GLU   C N   1 
ATOM   4702 C  CA  . GLU   C 1 193 ? -50.225 9.347   61.274  1.00 43.49 ? 286 GLU   C CA  1 
ATOM   4703 C  C   . GLU   C 1 193 ? -51.464 9.927   61.973  1.00 45.94 ? 286 GLU   C C   1 
ATOM   4704 O  O   . GLU   C 1 193 ? -52.162 10.751  61.336  1.00 46.46 ? 286 GLU   C O   1 
ATOM   4705 C  CB  . GLU   C 1 193 ? -50.543 8.068   60.497  1.00 42.42 ? 286 GLU   C CB  1 
ATOM   4706 C  CG  . GLU   C 1 193 ? -49.575 7.831   59.340  1.00 41.22 ? 286 GLU   C CG  1 
ATOM   4707 C  CD  . GLU   C 1 193 ? -49.651 6.473   58.663  1.00 40.46 ? 286 GLU   C CD  1 
ATOM   4708 O  OE1 . GLU   C 1 193 ? -50.430 5.625   59.128  1.00 41.13 ? 286 GLU   C OE1 1 
ATOM   4709 O  OE2 . GLU   C 1 193 ? -48.929 6.268   57.657  1.00 38.71 ? 286 GLU   C OE2 1 
ATOM   4710 N  N   . GLU   C 1 194 ? -51.724 9.561   63.234  1.00 48.48 ? 287 GLU   C N   1 
ATOM   4711 C  CA  . GLU   C 1 194 ? -52.938 10.029  63.968  1.00 51.16 ? 287 GLU   C CA  1 
ATOM   4712 C  C   . GLU   C 1 194 ? -52.860 11.548  64.159  1.00 52.72 ? 287 GLU   C C   1 
ATOM   4713 O  O   . GLU   C 1 194 ? -53.909 12.158  64.372  1.00 54.31 ? 287 GLU   C O   1 
ATOM   4714 C  CB  . GLU   C 1 194 ? -53.185 9.236   65.255  1.00 53.07 ? 287 GLU   C CB  1 
ATOM   4715 C  CG  . GLU   C 1 194 ? -52.418 9.697   66.478  1.00 54.21 ? 287 GLU   C CG  1 
ATOM   4716 C  CD  . GLU   C 1 194 ? -52.822 8.958   67.747  1.00 55.87 ? 287 GLU   C CD  1 
ATOM   4717 O  OE1 . GLU   C 1 194 ? -51.912 8.523   68.514  1.00 54.62 ? 287 GLU   C OE1 1 
ATOM   4718 O  OE2 . GLU   C 1 194 ? -54.058 8.809   67.970  1.00 56.56 ? 287 GLU   C OE2 1 
ATOM   4719 N  N   . ASN   C 1 195 ? -51.670 12.139  64.032  1.00 53.22 ? 288 ASN   C N   1 
ATOM   4720 C  CA  . ASN   C 1 195 ? -51.436 13.609  63.966  1.00 55.14 ? 288 ASN   C CA  1 
ATOM   4721 C  C   . ASN   C 1 195 ? -51.781 14.113  62.557  1.00 55.32 ? 288 ASN   C C   1 
ATOM   4722 O  O   . ASN   C 1 195 ? -52.452 13.475  61.725  1.00 55.13 ? 288 ASN   C O   1 
ATOM   4723 C  CB  . ASN   C 1 195 ? -49.982 13.964  64.302  1.00 54.82 ? 288 ASN   C CB  1 
ATOM   4724 C  CG  . ASN   C 1 195 ? -49.545 13.500  65.676  1.00 54.99 ? 288 ASN   C CG  1 
ATOM   4725 O  OD1 . ASN   C 1 195 ? -50.324 12.907  66.421  1.00 56.79 ? 288 ASN   C OD1 1 
ATOM   4726 N  ND2 . ASN   C 1 195 ? -48.313 13.803  66.044  1.00 54.73 ? 288 ASN   C ND2 1 
ATOM   4727 N  N   . SER   D 1 2   ? -22.526 23.038  -1.835  1.00 68.13 ? 95  SER   D N   1 
ATOM   4728 C  CA  . SER   D 1 2   ? -21.702 23.283  -0.603  1.00 68.42 ? 95  SER   D CA  1 
ATOM   4729 C  C   . SER   D 1 2   ? -20.879 22.034  -0.238  1.00 67.42 ? 95  SER   D C   1 
ATOM   4730 O  O   . SER   D 1 2   ? -21.059 20.983  -0.897  1.00 65.87 ? 95  SER   D O   1 
ATOM   4731 C  CB  . SER   D 1 2   ? -22.578 23.727  0.543   1.00 67.90 ? 95  SER   D CB  1 
ATOM   4732 O  OG  . SER   D 1 2   ? -23.528 22.726  0.873   1.00 67.16 ? 95  SER   D OG  1 
ATOM   4733 N  N   . SER   D 1 3   ? -19.997 22.156  0.765   1.00 68.00 ? 96  SER   D N   1 
ATOM   4734 C  CA  . SER   D 1 3   ? -19.160 21.059  1.326   1.00 66.65 ? 96  SER   D CA  1 
ATOM   4735 C  C   . SER   D 1 3   ? -20.038 19.829  1.605   1.00 64.00 ? 96  SER   D C   1 
ATOM   4736 O  O   . SER   D 1 3   ? -19.784 18.769  1.012   1.00 63.65 ? 96  SER   D O   1 
ATOM   4737 C  CB  . SER   D 1 3   ? -18.425 21.525  2.565   1.00 67.60 ? 96  SER   D CB  1 
ATOM   4738 O  OG  . SER   D 1 3   ? -19.321 21.754  3.644   1.00 68.03 ? 96  SER   D OG  1 
ATOM   4739 N  N   . VAL   D 1 4   ? -21.047 20.006  2.458   1.00 61.98 ? 97  VAL   D N   1 
ATOM   4740 C  CA  . VAL   D 1 4   ? -22.062 18.998  2.888   1.00 58.55 ? 97  VAL   D CA  1 
ATOM   4741 C  C   . VAL   D 1 4   ? -22.315 17.987  1.772   1.00 56.83 ? 97  VAL   D C   1 
ATOM   4742 O  O   . VAL   D 1 4   ? -22.572 18.370  0.635   1.00 56.13 ? 97  VAL   D O   1 
ATOM   4743 C  CB  . VAL   D 1 4   ? -23.383 19.688  3.287   1.00 59.01 ? 97  VAL   D CB  1 
ATOM   4744 C  CG1 . VAL   D 1 4   ? -24.419 18.682  3.736   1.00 57.76 ? 97  VAL   D CG1 1 
ATOM   4745 C  CG2 . VAL   D 1 4   ? -23.203 20.750  4.353   1.00 59.78 ? 97  VAL   D CG2 1 
ATOM   4746 N  N   . PRO   D 1 5   ? -22.274 16.661  2.059   1.00 54.76 ? 98  PRO   D N   1 
ATOM   4747 C  CA  . PRO   D 1 5   ? -22.706 15.658  1.085   1.00 53.69 ? 98  PRO   D CA  1 
ATOM   4748 C  C   . PRO   D 1 5   ? -24.217 15.734  0.804   1.00 53.06 ? 98  PRO   D C   1 
ATOM   4749 O  O   . PRO   D 1 5   ? -24.987 16.027  1.704   1.00 52.32 ? 98  PRO   D O   1 
ATOM   4750 C  CB  . PRO   D 1 5   ? -22.338 14.303  1.695   1.00 52.73 ? 98  PRO   D CB  1 
ATOM   4751 C  CG  . PRO   D 1 5   ? -22.093 14.577  3.158   1.00 52.60 ? 98  PRO   D CG  1 
ATOM   4752 C  CD  . PRO   D 1 5   ? -21.825 16.064  3.325   1.00 53.29 ? 98  PRO   D CD  1 
ATOM   4753 N  N   . SER   D 1 6   ? -24.588 15.457  -0.444  1.00 51.91 ? 99  SER   D N   1 
ATOM   4754 C  CA  . SER   D 1 6   ? -25.962 15.598  -0.985  1.00 51.14 ? 99  SER   D CA  1 
ATOM   4755 C  C   . SER   D 1 6   ? -26.924 14.668  -0.240  1.00 48.83 ? 99  SER   D C   1 
ATOM   4756 O  O   . SER   D 1 6   ? -26.541 13.530  0.097   1.00 47.39 ? 99  SER   D O   1 
ATOM   4757 C  CB  . SER   D 1 6   ? -25.964 15.336  -2.465  1.00 52.08 ? 99  SER   D CB  1 
ATOM   4758 O  OG  . SER   D 1 6   ? -27.289 15.198  -2.959  1.00 53.14 ? 99  SER   D OG  1 
ATOM   4759 N  N   . GLN   D 1 7   ? -28.143 15.146  -0.001  1.00 47.20 ? 100 GLN   D N   1 
ATOM   4760 C  CA  . GLN   D 1 7   ? -29.242 14.378  0.649   1.00 45.09 ? 100 GLN   D CA  1 
ATOM   4761 C  C   . GLN   D 1 7   ? -30.405 14.208  -0.338  1.00 44.74 ? 100 GLN   D C   1 
ATOM   4762 O  O   . GLN   D 1 7   ? -31.457 13.705  0.077   1.00 44.80 ? 100 GLN   D O   1 
ATOM   4763 C  CB  . GLN   D 1 7   ? -29.638 15.129  1.924   1.00 45.01 ? 100 GLN   D CB  1 
ATOM   4764 C  CG  . GLN   D 1 7   ? -28.467 15.940  2.467   1.00 44.71 ? 100 GLN   D CG  1 
ATOM   4765 C  CD  . GLN   D 1 7   ? -28.755 16.601  3.784   1.00 44.93 ? 100 GLN   D CD  1 
ATOM   4766 O  OE1 . GLN   D 1 7   ? -28.755 15.952  4.830   1.00 43.02 ? 100 GLN   D OE1 1 
ATOM   4767 N  NE2 . GLN   D 1 7   ? -28.962 17.908  3.730   1.00 45.63 ? 100 GLN   D NE2 1 
ATOM   4768 N  N   . LYS   D 1 8   ? -30.235 14.629  -1.594  1.00 45.75 ? 101 LYS   D N   1 
ATOM   4769 C  CA  . LYS   D 1 8   ? -31.309 14.615  -2.628  1.00 45.95 ? 101 LYS   D CA  1 
ATOM   4770 C  C   . LYS   D 1 8   ? -31.651 13.155  -2.966  1.00 44.13 ? 101 LYS   D C   1 
ATOM   4771 O  O   . LYS   D 1 8   ? -30.729 12.397  -3.306  1.00 42.15 ? 101 LYS   D O   1 
ATOM   4772 C  CB  . LYS   D 1 8   ? -30.857 15.421  -3.850  1.00 48.22 ? 101 LYS   D CB  1 
ATOM   4773 C  CG  . LYS   D 1 8   ? -30.402 16.838  -3.514  1.00 49.49 ? 101 LYS   D CG  1 
ATOM   4774 C  CD  . LYS   D 1 8   ? -30.349 17.804  -4.666  1.00 52.05 ? 101 LYS   D CD  1 
ATOM   4775 C  CE  . LYS   D 1 8   ? -30.437 19.246  -4.201  1.00 53.48 ? 101 LYS   D CE  1 
ATOM   4776 N  NZ  . LYS   D 1 8   ? -29.998 20.208  -5.242  1.00 55.39 ? 101 LYS   D NZ  1 
ATOM   4777 N  N   . THR   D 1 9   ? -32.929 12.781  -2.882  1.00 43.24 ? 102 THR   D N   1 
ATOM   4778 C  CA  . THR   D 1 9   ? -33.428 11.433  -3.268  1.00 42.92 ? 102 THR   D CA  1 
ATOM   4779 C  C   . THR   D 1 9   ? -33.142 11.179  -4.751  1.00 43.63 ? 102 THR   D C   1 
ATOM   4780 O  O   . THR   D 1 9   ? -33.271 12.119  -5.546  1.00 43.90 ? 102 THR   D O   1 
ATOM   4781 C  CB  . THR   D 1 9   ? -34.914 11.261  -2.945  1.00 42.95 ? 102 THR   D CB  1 
ATOM   4782 O  OG1 . THR   D 1 9   ? -35.007 11.405  -1.529  1.00 42.59 ? 102 THR   D OG1 1 
ATOM   4783 C  CG2 . THR   D 1 9   ? -35.470 9.908   -3.331  1.00 42.73 ? 102 THR   D CG2 1 
ATOM   4784 N  N   . TYR   D 1 10  ? -32.763 9.942   -5.077  1.00 43.80 ? 103 TYR   D N   1 
ATOM   4785 C  CA  . TYR   D 1 10  ? -32.426 9.477   -6.442  1.00 45.06 ? 103 TYR   D CA  1 
ATOM   4786 C  C   . TYR   D 1 10  ? -32.633 7.968   -6.532  1.00 43.89 ? 103 TYR   D C   1 
ATOM   4787 O  O   . TYR   D 1 10  ? -31.757 7.232   -6.063  1.00 42.13 ? 103 TYR   D O   1 
ATOM   4788 C  CB  . TYR   D 1 10  ? -30.971 9.823   -6.770  1.00 46.43 ? 103 TYR   D CB  1 
ATOM   4789 C  CG  . TYR   D 1 10  ? -30.727 11.280  -7.077  1.00 48.34 ? 103 TYR   D CG  1 
ATOM   4790 C  CD1 . TYR   D 1 10  ? -31.476 11.959  -8.027  1.00 50.63 ? 103 TYR   D CD1 1 
ATOM   4791 C  CD2 . TYR   D 1 10  ? -29.749 11.991  -6.402  1.00 49.06 ? 103 TYR   D CD2 1 
ATOM   4792 C  CE1 . TYR   D 1 10  ? -31.241 13.295  -8.318  1.00 52.05 ? 103 TYR   D CE1 1 
ATOM   4793 C  CE2 . TYR   D 1 10  ? -29.503 13.329  -6.674  1.00 50.17 ? 103 TYR   D CE2 1 
ATOM   4794 C  CZ  . TYR   D 1 10  ? -30.258 13.984  -7.628  1.00 52.28 ? 103 TYR   D CZ  1 
ATOM   4795 O  OH  . TYR   D 1 10  ? -30.012 15.299  -7.889  1.00 54.68 ? 103 TYR   D OH  1 
ATOM   4796 N  N   . GLN   D 1 11  ? -33.747 7.517   -7.113  1.00 44.54 ? 104 GLN   D N   1 
ATOM   4797 C  CA  . GLN   D 1 11  ? -34.008 6.072   -7.335  1.00 44.44 ? 104 GLN   D CA  1 
ATOM   4798 C  C   . GLN   D 1 11  ? -33.020 5.549   -8.385  1.00 44.29 ? 104 GLN   D C   1 
ATOM   4799 O  O   . GLN   D 1 11  ? -32.584 4.383   -8.274  1.00 43.63 ? 104 GLN   D O   1 
ATOM   4800 C  CB  . GLN   D 1 11  ? -35.468 5.843   -7.737  1.00 46.22 ? 104 GLN   D CB  1 
ATOM   4801 C  CG  . GLN   D 1 11  ? -36.475 6.121   -6.630  1.00 46.40 ? 104 GLN   D CG  1 
ATOM   4802 C  CD  . GLN   D 1 11  ? -37.747 5.303   -6.766  1.00 48.18 ? 104 GLN   D CD  1 
ATOM   4803 O  OE1 . GLN   D 1 11  ? -38.112 4.858   -7.856  1.00 49.74 ? 104 GLN   D OE1 1 
ATOM   4804 N  NE2 . GLN   D 1 11  ? -38.430 5.069   -5.651  1.00 47.58 ? 104 GLN   D NE2 1 
ATOM   4805 N  N   . GLY   D 1 12  ? -32.676 6.394   -9.358  1.00 44.60 ? 105 GLY   D N   1 
ATOM   4806 C  CA  . GLY   D 1 12  ? -31.677 6.092   -10.399 1.00 45.18 ? 105 GLY   D CA  1 
ATOM   4807 C  C   . GLY   D 1 12  ? -32.043 4.860   -11.209 1.00 45.44 ? 105 GLY   D C   1 
ATOM   4808 O  O   . GLY   D 1 12  ? -33.247 4.537   -11.302 1.00 46.49 ? 105 GLY   D O   1 
ATOM   4809 N  N   . SER   D 1 13  ? -31.030 4.181   -11.740 1.00 45.12 ? 106 SER   D N   1 
ATOM   4810 C  CA  . SER   D 1 13  ? -31.124 3.197   -12.847 1.00 46.36 ? 106 SER   D CA  1 
ATOM   4811 C  C   . SER   D 1 13  ? -31.839 1.925   -12.377 1.00 45.53 ? 106 SER   D C   1 
ATOM   4812 O  O   . SER   D 1 13  ? -32.536 1.312   -13.210 1.00 47.04 ? 106 SER   D O   1 
ATOM   4813 C  CB  . SER   D 1 13  ? -29.747 2.889   -13.397 1.00 46.25 ? 106 SER   D CB  1 
ATOM   4814 O  OG  . SER   D 1 13  ? -29.835 1.943   -14.458 1.00 48.09 ? 106 SER   D OG  1 
ATOM   4815 N  N   . TYR   D 1 14  ? -31.706 1.565   -11.098 1.00 43.16 ? 107 TYR   D N   1 
ATOM   4816 C  CA  . TYR   D 1 14  ? -32.160 0.261   -10.547 1.00 42.45 ? 107 TYR   D CA  1 
ATOM   4817 C  C   . TYR   D 1 14  ? -33.455 0.418   -9.735  1.00 42.32 ? 107 TYR   D C   1 
ATOM   4818 O  O   . TYR   D 1 14  ? -33.891 -0.578  -9.158  1.00 42.15 ? 107 TYR   D O   1 
ATOM   4819 C  CB  . TYR   D 1 14  ? -31.033 -0.371  -9.730  1.00 40.98 ? 107 TYR   D CB  1 
ATOM   4820 C  CG  . TYR   D 1 14  ? -29.816 -0.684  -10.555 1.00 41.06 ? 107 TYR   D CG  1 
ATOM   4821 C  CD1 . TYR   D 1 14  ? -29.768 -1.809  -11.359 1.00 41.88 ? 107 TYR   D CD1 1 
ATOM   4822 C  CD2 . TYR   D 1 14  ? -28.722 0.164   -10.550 1.00 40.73 ? 107 TYR   D CD2 1 
ATOM   4823 C  CE1 . TYR   D 1 14  ? -28.659 -2.093  -12.137 1.00 42.49 ? 107 TYR   D CE1 1 
ATOM   4824 C  CE2 . TYR   D 1 14  ? -27.593 -0.110  -11.305 1.00 40.89 ? 107 TYR   D CE2 1 
ATOM   4825 C  CZ  . TYR   D 1 14  ? -27.563 -1.243  -12.099 1.00 41.99 ? 107 TYR   D CZ  1 
ATOM   4826 O  OH  . TYR   D 1 14  ? -26.463 -1.504  -12.852 1.00 42.97 ? 107 TYR   D OH  1 
ATOM   4827 N  N   . GLY   D 1 15  ? -34.069 1.604   -9.738  1.00 42.78 ? 108 GLY   D N   1 
ATOM   4828 C  CA  . GLY   D 1 15  ? -35.318 1.898   -9.002  1.00 43.19 ? 108 GLY   D CA  1 
ATOM   4829 C  C   . GLY   D 1 15  ? -35.152 1.653   -7.513  1.00 41.42 ? 108 GLY   D C   1 
ATOM   4830 O  O   . GLY   D 1 15  ? -35.949 0.878   -6.940  1.00 41.50 ? 108 GLY   D O   1 
ATOM   4831 N  N   . PHE   D 1 16  ? -34.144 2.294   -6.913  1.00 41.37 ? 109 PHE   D N   1 
ATOM   4832 C  CA  . PHE   D 1 16  ? -33.676 2.066   -5.521  1.00 39.78 ? 109 PHE   D CA  1 
ATOM   4833 C  C   . PHE   D 1 16  ? -34.542 2.875   -4.549  1.00 39.40 ? 109 PHE   D C   1 
ATOM   4834 O  O   . PHE   D 1 16  ? -34.595 4.119   -4.658  1.00 39.21 ? 109 PHE   D O   1 
ATOM   4835 C  CB  . PHE   D 1 16  ? -32.186 2.398   -5.412  1.00 39.30 ? 109 PHE   D CB  1 
ATOM   4836 C  CG  . PHE   D 1 16  ? -31.644 2.473   -4.006  1.00 38.07 ? 109 PHE   D CG  1 
ATOM   4837 C  CD1 . PHE   D 1 16  ? -31.527 1.331   -3.233  1.00 37.41 ? 109 PHE   D CD1 1 
ATOM   4838 C  CD2 . PHE   D 1 16  ? -31.263 3.690   -3.452  1.00 37.57 ? 109 PHE   D CD2 1 
ATOM   4839 C  CE1 . PHE   D 1 16  ? -31.045 1.407   -1.937  1.00 36.98 ? 109 PHE   D CE1 1 
ATOM   4840 C  CE2 . PHE   D 1 16  ? -30.787 3.766   -2.156  1.00 36.72 ? 109 PHE   D CE2 1 
ATOM   4841 C  CZ  . PHE   D 1 16  ? -30.663 2.618   -1.406  1.00 36.41 ? 109 PHE   D CZ  1 
ATOM   4842 N  N   . ARG   D 1 17  ? -35.213 2.177   -3.631  1.00 39.25 ? 110 ARG   D N   1 
ATOM   4843 C  CA  A ARG   D 1 17  ? -36.050 2.770   -2.546  0.40 38.93 ? 110 ARG   D CA  1 
ATOM   4844 C  CA  B ARG   D 1 17  ? -35.966 2.829   -2.528  0.60 38.82 ? 110 ARG   D CA  1 
ATOM   4845 C  C   . ARG   D 1 17  ? -35.795 2.017   -1.241  1.00 37.51 ? 110 ARG   D C   1 
ATOM   4846 O  O   . ARG   D 1 17  ? -35.303 0.874   -1.301  1.00 37.65 ? 110 ARG   D O   1 
ATOM   4847 C  CB  A ARG   D 1 17  ? -37.557 2.757   -2.863  0.40 40.20 ? 110 ARG   D CB  1 
ATOM   4848 C  CB  B ARG   D 1 17  ? -37.426 3.022   -2.942  0.60 39.96 ? 110 ARG   D CB  1 
ATOM   4849 C  CG  A ARG   D 1 17  ? -38.125 1.461   -3.425  0.40 41.27 ? 110 ARG   D CG  1 
ATOM   4850 C  CG  B ARG   D 1 17  ? -38.191 1.726   -3.150  0.60 40.76 ? 110 ARG   D CG  1 
ATOM   4851 C  CD  A ARG   D 1 17  ? -39.174 1.813   -4.477  0.40 42.82 ? 110 ARG   D CD  1 
ATOM   4852 C  CD  B ARG   D 1 17  ? -39.022 1.758   -4.414  0.60 42.06 ? 110 ARG   D CD  1 
ATOM   4853 N  NE  A ARG   D 1 17  ? -40.111 0.740   -4.772  0.40 44.20 ? 110 ARG   D NE  1 
ATOM   4854 N  NE  B ARG   D 1 17  ? -38.410 0.954   -5.460  0.60 42.91 ? 110 ARG   D NE  1 
ATOM   4855 C  CZ  A ARG   D 1 17  ? -39.837 -0.299  -5.549  0.40 45.05 ? 110 ARG   D CZ  1 
ATOM   4856 C  CZ  B ARG   D 1 17  ? -38.533 -0.369  -5.565  0.60 43.64 ? 110 ARG   D CZ  1 
ATOM   4857 N  NH1 A ARG   D 1 17  ? -38.635 -0.417  -6.094  0.40 45.14 ? 110 ARG   D NH1 1 
ATOM   4858 N  NH1 B ARG   D 1 17  ? -39.260 -1.050  -4.691  0.60 43.27 ? 110 ARG   D NH1 1 
ATOM   4859 N  NH2 A ARG   D 1 17  ? -40.755 -1.222  -5.763  0.40 45.95 ? 110 ARG   D NH2 1 
ATOM   4860 N  NH2 B ARG   D 1 17  ? -37.943 -1.007  -6.560  0.60 44.29 ? 110 ARG   D NH2 1 
ATOM   4861 N  N   . LEU   D 1 18  ? -36.123 2.643   -0.109  1.00 36.90 ? 111 LEU   D N   1 
ATOM   4862 C  CA  . LEU   D 1 18  ? -35.982 2.049   1.242   1.00 35.61 ? 111 LEU   D CA  1 
ATOM   4863 C  C   . LEU   D 1 18  ? -37.356 1.545   1.665   1.00 35.95 ? 111 LEU   D C   1 
ATOM   4864 O  O   . LEU   D 1 18  ? -38.355 2.130   1.233   1.00 37.13 ? 111 LEU   D O   1 
ATOM   4865 C  CB  . LEU   D 1 18  ? -35.452 3.093   2.229   1.00 34.78 ? 111 LEU   D CB  1 
ATOM   4866 C  CG  . LEU   D 1 18  ? -34.079 3.683   1.909   1.00 34.62 ? 111 LEU   D CG  1 
ATOM   4867 C  CD1 . LEU   D 1 18  ? -33.658 4.653   2.998   1.00 34.10 ? 111 LEU   D CD1 1 
ATOM   4868 C  CD2 . LEU   D 1 18  ? -33.026 2.584   1.743   1.00 34.12 ? 111 LEU   D CD2 1 
ATOM   4869 N  N   . GLY   D 1 19  ? -37.385 0.452   2.422   1.00 35.48 ? 112 GLY   D N   1 
ATOM   4870 C  CA  . GLY   D 1 19  ? -38.581 -0.030  3.125   1.00 35.72 ? 112 GLY   D CA  1 
ATOM   4871 C  C   . GLY   D 1 19  ? -38.263 -0.229  4.592   1.00 34.89 ? 112 GLY   D C   1 
ATOM   4872 O  O   . GLY   D 1 19  ? -37.073 -0.358  4.931   1.00 33.80 ? 112 GLY   D O   1 
ATOM   4873 N  N   . PHE   D 1 20  ? -39.291 -0.251  5.431   1.00 35.16 ? 113 PHE   D N   1 
ATOM   4874 C  CA  . PHE   D 1 20  ? -39.163 -0.464  6.894   1.00 35.14 ? 113 PHE   D CA  1 
ATOM   4875 C  C   . PHE   D 1 20  ? -40.246 -1.452  7.320   1.00 35.88 ? 113 PHE   D C   1 
ATOM   4876 O  O   . PHE   D 1 20  ? -41.321 -1.490  6.674   1.00 37.51 ? 113 PHE   D O   1 
ATOM   4877 C  CB  . PHE   D 1 20  ? -39.244 0.874   7.626   1.00 34.50 ? 113 PHE   D CB  1 
ATOM   4878 C  CG  . PHE   D 1 20  ? -38.257 1.893   7.124   1.00 33.55 ? 113 PHE   D CG  1 
ATOM   4879 C  CD1 . PHE   D 1 20  ? -38.578 2.726   6.060   1.00 33.73 ? 113 PHE   D CD1 1 
ATOM   4880 C  CD2 . PHE   D 1 20  ? -37.002 2.007   7.701   1.00 32.65 ? 113 PHE   D CD2 1 
ATOM   4881 C  CE1 . PHE   D 1 20  ? -37.660 3.649   5.582   1.00 32.83 ? 113 PHE   D CE1 1 
ATOM   4882 C  CE2 . PHE   D 1 20  ? -36.084 2.929   7.221   1.00 31.99 ? 113 PHE   D CE2 1 
ATOM   4883 C  CZ  . PHE   D 1 20  ? -36.422 3.759   6.176   1.00 32.77 ? 113 PHE   D CZ  1 
ATOM   4884 N  N   . LEU   D 1 21  ? -39.967 -2.244  8.353   1.00 35.88 ? 114 LEU   D N   1 
ATOM   4885 C  CA  . LEU   D 1 21  ? -40.978 -3.134  8.970   1.00 36.26 ? 114 LEU   D CA  1 
ATOM   4886 C  C   . LEU   D 1 21  ? -42.114 -2.255  9.514   1.00 36.34 ? 114 LEU   D C   1 
ATOM   4887 O  O   . LEU   D 1 21  ? -41.850 -1.113  9.951   1.00 34.84 ? 114 LEU   D O   1 
ATOM   4888 C  CB  . LEU   D 1 21  ? -40.318 -3.977  10.067  1.00 36.19 ? 114 LEU   D CB  1 
ATOM   4889 C  CG  . LEU   D 1 21  ? -39.354 -5.053  9.561   1.00 35.86 ? 114 LEU   D CG  1 
ATOM   4890 C  CD1 . LEU   D 1 21  ? -38.613 -5.711  10.711  1.00 35.89 ? 114 LEU   D CD1 1 
ATOM   4891 C  CD2 . LEU   D 1 21  ? -40.074 -6.104  8.734   1.00 36.62 ? 114 LEU   D CD2 1 
ATOM   4892 N  N   . HIS   D 1 22  ? -43.350 -2.743  9.414   1.00 36.93 ? 115 HIS   D N   1 
ATOM   4893 C  CA  . HIS   D 1 22  ? -44.564 -2.131  10.013  1.00 37.47 ? 115 HIS   D CA  1 
ATOM   4894 C  C   . HIS   D 1 22  ? -44.668 -2.656  11.446  1.00 36.84 ? 115 HIS   D C   1 
ATOM   4895 O  O   . HIS   D 1 22  ? -45.491 -3.529  11.700  1.00 37.83 ? 115 HIS   D O   1 
ATOM   4896 C  CB  . HIS   D 1 22  ? -45.761 -2.413  9.099   1.00 39.29 ? 115 HIS   D CB  1 
ATOM   4897 C  CG  . HIS   D 1 22  ? -45.464 -1.996  7.697   1.00 40.03 ? 115 HIS   D CG  1 
ATOM   4898 N  ND1 . HIS   D 1 22  ? -45.255 -2.907  6.671   1.00 40.78 ? 115 HIS   D ND1 1 
ATOM   4899 C  CD2 . HIS   D 1 22  ? -45.241 -0.773  7.167   1.00 39.93 ? 115 HIS   D CD2 1 
ATOM   4900 C  CE1 . HIS   D 1 22  ? -44.938 -2.258  5.570   1.00 40.31 ? 115 HIS   D CE1 1 
ATOM   4901 N  NE2 . HIS   D 1 22  ? -44.940 -0.945  5.843   1.00 40.26 ? 115 HIS   D NE2 1 
ATOM   4902 N  N   A SER   D 1 23  ? -43.852 -2.111  12.346  0.85 35.86 ? 116 SER   D N   1 
ATOM   4903 N  N   B SER   D 1 23  ? -43.806 -2.135  12.323  0.15 36.02 ? 116 SER   D N   1 
ATOM   4904 C  CA  A SER   D 1 23  ? -43.554 -2.667  13.690  0.85 35.84 ? 116 SER   D CA  1 
ATOM   4905 C  CA  B SER   D 1 23  ? -43.540 -2.627  13.701  0.15 36.08 ? 116 SER   D CA  1 
ATOM   4906 C  C   A SER   D 1 23  ? -44.560 -2.169  14.740  0.85 36.44 ? 116 SER   D C   1 
ATOM   4907 C  C   B SER   D 1 23  ? -44.674 -2.240  14.655  0.15 36.80 ? 116 SER   D C   1 
ATOM   4908 O  O   A SER   D 1 23  ? -44.680 -2.842  15.773  0.85 37.24 ? 116 SER   D O   1 
ATOM   4909 O  O   B SER   D 1 23  ? -45.011 -3.063  15.526  0.15 37.65 ? 116 SER   D O   1 
ATOM   4910 C  CB  A SER   D 1 23  ? -42.142 -2.314  14.106  0.85 34.76 ? 116 SER   D CB  1 
ATOM   4911 C  CB  B SER   D 1 23  ? -42.239 -2.071  14.200  0.15 35.16 ? 116 SER   D CB  1 
ATOM   4912 O  OG  A SER   D 1 23  ? -41.180 -2.832  13.202  0.85 33.78 ? 116 SER   D OG  1 
ATOM   4913 O  OG  B SER   D 1 23  ? -42.375 -0.684  14.468  0.15 34.95 ? 116 SER   D OG  1 
ATOM   4914 N  N   . GLY   D 1 24  ? -45.219 -1.029  14.500  1.00 36.45 ? 117 GLY   D N   1 
ATOM   4915 C  CA  . GLY   D 1 24  ? -46.146 -0.416  15.466  1.00 37.52 ? 117 GLY   D CA  1 
ATOM   4916 C  C   . GLY   D 1 24  ? -45.416 0.268   16.609  1.00 37.52 ? 117 GLY   D C   1 
ATOM   4917 O  O   . GLY   D 1 24  ? -44.158 0.367   16.561  1.00 36.35 ? 117 GLY   D O   1 
ATOM   4918 N  N   . THR   D 1 25  ? -46.157 0.708   17.633  1.00 38.42 ? 118 THR   D N   1 
ATOM   4919 C  CA  . THR   D 1 25  ? -45.639 1.558   18.747  1.00 38.74 ? 118 THR   D CA  1 
ATOM   4920 C  C   . THR   D 1 25  ? -45.883 0.874   20.100  1.00 40.36 ? 118 THR   D C   1 
ATOM   4921 O  O   . THR   D 1 25  ? -46.018 1.597   21.096  1.00 41.74 ? 118 THR   D O   1 
ATOM   4922 C  CB  . THR   D 1 25  ? -46.271 2.955   18.704  1.00 38.57 ? 118 THR   D CB  1 
ATOM   4923 O  OG1 . THR   D 1 25  ? -47.683 2.780   18.820  1.00 39.94 ? 118 THR   D OG1 1 
ATOM   4924 C  CG2 . THR   D 1 25  ? -45.940 3.725   17.446  1.00 37.81 ? 118 THR   D CG2 1 
ATOM   4925 N  N   . ALA   D 1 26  ? -45.951 -0.463  20.135  1.00 41.54 ? 119 ALA   D N   1 
ATOM   4926 C  CA  . ALA   D 1 26  ? -46.178 -1.242  21.375  1.00 43.75 ? 119 ALA   D CA  1 
ATOM   4927 C  C   . ALA   D 1 26  ? -44.965 -1.072  22.301  1.00 44.14 ? 119 ALA   D C   1 
ATOM   4928 O  O   . ALA   D 1 26  ? -43.846 -0.930  21.788  1.00 43.63 ? 119 ALA   D O   1 
ATOM   4929 C  CB  . ALA   D 1 26  ? -46.430 -2.692  21.047  1.00 44.13 ? 119 ALA   D CB  1 
ATOM   4930 N  N   . LYS   D 1 27  ? -45.197 -1.095  23.614  1.00 46.69 ? 120 LYS   D N   1 
ATOM   4931 C  CA  . LYS   D 1 27  ? -44.194 -0.815  24.682  1.00 48.33 ? 120 LYS   D CA  1 
ATOM   4932 C  C   . LYS   D 1 27  ? -42.867 -1.526  24.396  1.00 48.43 ? 120 LYS   D C   1 
ATOM   4933 O  O   . LYS   D 1 27  ? -41.822 -0.908  24.639  1.00 49.32 ? 120 LYS   D O   1 
ATOM   4934 C  CB  . LYS   D 1 27  ? -44.751 -1.235  26.051  1.00 49.90 ? 120 LYS   D CB  1 
ATOM   4935 C  CG  . LYS   D 1 27  ? -45.797 -0.299  26.638  1.00 51.14 ? 120 LYS   D CG  1 
ATOM   4936 C  CD  . LYS   D 1 27  ? -46.042 -0.517  28.126  1.00 52.78 ? 120 LYS   D CD  1 
ATOM   4937 C  CE  . LYS   D 1 27  ? -46.619 0.692   28.827  1.00 53.66 ? 120 LYS   D CE  1 
ATOM   4938 N  NZ  . LYS   D 1 27  ? -46.904 0.384   30.246  1.00 55.45 ? 120 LYS   D NZ  1 
ATOM   4939 N  N   . SER   D 1 28  ? -42.909 -2.754  23.871  1.00 50.09 ? 121 SER   D N   1 
ATOM   4940 C  CA  . SER   D 1 28  ? -41.741 -3.665  23.710  1.00 50.13 ? 121 SER   D CA  1 
ATOM   4941 C  C   . SER   D 1 28  ? -40.832 -3.280  22.528  1.00 48.87 ? 121 SER   D C   1 
ATOM   4942 O  O   . SER   D 1 28  ? -39.682 -3.764  22.501  1.00 49.57 ? 121 SER   D O   1 
ATOM   4943 C  CB  . SER   D 1 28  ? -42.223 -5.083  23.544  1.00 51.91 ? 121 SER   D CB  1 
ATOM   4944 O  OG  . SER   D 1 28  ? -42.991 -5.217  22.351  1.00 52.10 ? 121 SER   D OG  1 
ATOM   4945 N  N   A VAL   D 1 29  ? -41.330 -2.472  21.583  0.60 47.50 ? 122 VAL   D N   1 
ATOM   4946 N  N   B VAL   D 1 29  ? -41.305 -2.417  21.618  0.40 47.24 ? 122 VAL   D N   1 
ATOM   4947 C  CA  A VAL   D 1 29  ? -40.692 -2.269  20.248  0.60 45.28 ? 122 VAL   D CA  1 
ATOM   4948 C  CA  B VAL   D 1 29  ? -40.714 -2.182  20.263  0.40 45.01 ? 122 VAL   D CA  1 
ATOM   4949 C  C   A VAL   D 1 29  ? -39.375 -1.506  20.439  0.60 43.95 ? 122 VAL   D C   1 
ATOM   4950 C  C   B VAL   D 1 29  ? -39.373 -1.445  20.392  0.40 43.68 ? 122 VAL   D C   1 
ATOM   4951 O  O   A VAL   D 1 29  ? -39.387 -0.448  21.109  0.60 43.53 ? 122 VAL   D O   1 
ATOM   4952 O  O   B VAL   D 1 29  ? -39.370 -0.315  20.932  0.40 43.14 ? 122 VAL   D O   1 
ATOM   4953 C  CB  A VAL   D 1 29  ? -41.641 -1.553  19.261  0.60 45.11 ? 122 VAL   D CB  1 
ATOM   4954 C  CB  B VAL   D 1 29  ? -41.696 -1.399  19.370  0.40 44.71 ? 122 VAL   D CB  1 
ATOM   4955 C  CG1 A VAL   D 1 29  ? -40.964 -1.269  17.925  0.60 44.05 ? 122 VAL   D CG1 1 
ATOM   4956 C  CG1 B VAL   D 1 29  ? -41.574 0.104   19.574  0.40 44.08 ? 122 VAL   D CG1 1 
ATOM   4957 C  CG2 A VAL   D 1 29  ? -42.921 -2.340  19.024  0.60 45.84 ? 122 VAL   D CG2 1 
ATOM   4958 C  CG2 B VAL   D 1 29  ? -41.529 -1.754  17.902  0.40 43.98 ? 122 VAL   D CG2 1 
ATOM   4959 N  N   . THR   D 1 30  ? -38.288 -2.037  19.872  1.00 42.32 ? 123 THR   D N   1 
ATOM   4960 C  CA  . THR   D 1 30  ? -36.908 -1.497  19.999  1.00 41.19 ? 123 THR   D CA  1 
ATOM   4961 C  C   . THR   D 1 30  ? -36.605 -0.553  18.832  1.00 38.41 ? 123 THR   D C   1 
ATOM   4962 O  O   . THR   D 1 30  ? -35.734 0.278   18.995  1.00 38.80 ? 123 THR   D O   1 
ATOM   4963 C  CB  . THR   D 1 30  ? -35.896 -2.645  20.130  1.00 41.86 ? 123 THR   D CB  1 
ATOM   4964 O  OG1 . THR   D 1 30  ? -35.920 -3.440  18.943  1.00 42.44 ? 123 THR   D OG1 1 
ATOM   4965 C  CG2 . THR   D 1 30  ? -36.185 -3.549  21.306  1.00 43.44 ? 123 THR   D CG2 1 
ATOM   4966 N  N   A CYS   D 1 31  ? -37.316 -0.687  17.707  0.50 38.06 ? 124 CYS   D N   1 
ATOM   4967 N  N   B CYS   D 1 31  ? -37.373 -0.657  17.736  0.50 37.22 ? 124 CYS   D N   1 
ATOM   4968 C  CA  A CYS   D 1 31  ? -37.185 0.214   16.533  0.50 36.72 ? 124 CYS   D CA  1 
ATOM   4969 C  CA  B CYS   D 1 31  ? -37.186 0.089   16.461  0.50 35.35 ? 124 CYS   D CA  1 
ATOM   4970 C  C   A CYS   D 1 31  ? -38.518 0.280   15.778  0.50 36.28 ? 124 CYS   D C   1 
ATOM   4971 C  C   B CYS   D 1 31  ? -38.520 0.252   15.717  0.50 35.46 ? 124 CYS   D C   1 
ATOM   4972 O  O   A CYS   D 1 31  ? -39.133 -0.778  15.550  0.50 37.01 ? 124 CYS   D O   1 
ATOM   4973 O  O   B CYS   D 1 31  ? -39.126 -0.792  15.379  0.50 36.06 ? 124 CYS   D O   1 
ATOM   4974 C  CB  A CYS   D 1 31  ? -36.013 -0.214  15.655  0.50 36.45 ? 124 CYS   D CB  1 
ATOM   4975 C  CB  B CYS   D 1 31  ? -36.213 -0.668  15.568  0.50 34.28 ? 124 CYS   D CB  1 
ATOM   4976 S  SG  A CYS   D 1 31  ? -36.329 -1.587  14.524  0.50 36.75 ? 124 CYS   D SG  1 
ATOM   4977 S  SG  B CYS   D 1 31  ? -35.746 0.253   14.082  0.50 32.12 ? 124 CYS   D SG  1 
ATOM   4978 N  N   . THR   D 1 32  ? -38.960 1.489   15.442  1.00 34.94 ? 125 THR   D N   1 
ATOM   4979 C  CA  . THR   D 1 32  ? -40.257 1.734   14.766  1.00 35.19 ? 125 THR   D CA  1 
ATOM   4980 C  C   . THR   D 1 32  ? -40.119 2.933   13.834  1.00 34.84 ? 125 THR   D C   1 
ATOM   4981 O  O   . THR   D 1 32  ? -39.477 3.926   14.225  1.00 36.10 ? 125 THR   D O   1 
ATOM   4982 C  CB  . THR   D 1 32  ? -41.391 1.865   15.785  1.00 35.83 ? 125 THR   D CB  1 
ATOM   4983 O  OG1 . THR   D 1 32  ? -42.615 1.910   15.043  1.00 36.49 ? 125 THR   D OG1 1 
ATOM   4984 C  CG2 . THR   D 1 32  ? -41.281 3.087   16.675  1.00 36.14 ? 125 THR   D CG2 1 
ATOM   4985 N  N   . TYR   D 1 33  ? -40.677 2.805   12.635  1.00 34.26 ? 126 TYR   D N   1 
ATOM   4986 C  CA  . TYR   D 1 33  ? -40.595 3.807   11.546  1.00 33.56 ? 126 TYR   D CA  1 
ATOM   4987 C  C   . TYR   D 1 33  ? -41.962 4.470   11.403  1.00 33.62 ? 126 TYR   D C   1 
ATOM   4988 O  O   . TYR   D 1 33  ? -42.981 3.761   11.371  1.00 33.01 ? 126 TYR   D O   1 
ATOM   4989 C  CB  . TYR   D 1 33  ? -40.141 3.154   10.239  1.00 33.42 ? 126 TYR   D CB  1 
ATOM   4990 C  CG  . TYR   D 1 33  ? -40.254 4.053   9.040   1.00 33.98 ? 126 TYR   D CG  1 
ATOM   4991 C  CD1 . TYR   D 1 33  ? -39.334 5.068   8.835   1.00 33.62 ? 126 TYR   D CD1 1 
ATOM   4992 C  CD2 . TYR   D 1 33  ? -41.276 3.893   8.115   1.00 34.66 ? 126 TYR   D CD2 1 
ATOM   4993 C  CE1 . TYR   D 1 33  ? -39.425 5.904   7.736   1.00 34.22 ? 126 TYR   D CE1 1 
ATOM   4994 C  CE2 . TYR   D 1 33  ? -41.368 4.707   7.000   1.00 35.23 ? 126 TYR   D CE2 1 
ATOM   4995 C  CZ  . TYR   D 1 33  ? -40.443 5.724   6.820   1.00 35.40 ? 126 TYR   D CZ  1 
ATOM   4996 O  OH  . TYR   D 1 33  ? -40.508 6.548   5.736   1.00 37.62 ? 126 TYR   D OH  1 
ATOM   4997 N  N   . SER   D 1 34  ? -41.962 5.800   11.313  1.00 33.81 ? 127 SER   D N   1 
ATOM   4998 C  CA  . SER   D 1 34  ? -43.147 6.645   11.026  1.00 35.00 ? 127 SER   D CA  1 
ATOM   4999 C  C   . SER   D 1 34  ? -43.125 7.018   9.546   1.00 35.12 ? 127 SER   D C   1 
ATOM   5000 O  O   . SER   D 1 34  ? -42.272 7.801   9.123   1.00 34.75 ? 127 SER   D O   1 
ATOM   5001 C  CB  . SER   D 1 34  ? -43.157 7.876   11.900  1.00 35.71 ? 127 SER   D CB  1 
ATOM   5002 O  OG  . SER   D 1 34  ? -44.240 8.743   11.537  1.00 37.01 ? 127 SER   D OG  1 
ATOM   5003 N  N   . PRO   D 1 35  ? -44.050 6.476   8.719   1.00 36.04 ? 128 PRO   D N   1 
ATOM   5004 C  CA  . PRO   D 1 35  ? -44.153 6.865   7.313   1.00 36.18 ? 128 PRO   D CA  1 
ATOM   5005 C  C   . PRO   D 1 35  ? -44.575 8.336   7.172   1.00 36.80 ? 128 PRO   D C   1 
ATOM   5006 O  O   . PRO   D 1 35  ? -44.119 8.972   6.256   1.00 36.95 ? 128 PRO   D O   1 
ATOM   5007 C  CB  . PRO   D 1 35  ? -45.225 5.951   6.695   1.00 37.05 ? 128 PRO   D CB  1 
ATOM   5008 C  CG  . PRO   D 1 35  ? -45.690 5.013   7.802   1.00 36.95 ? 128 PRO   D CG  1 
ATOM   5009 C  CD  . PRO   D 1 35  ? -45.041 5.454   9.094   1.00 36.43 ? 128 PRO   D CD  1 
ATOM   5010 N  N   . ALA   D 1 36  ? -45.421 8.838   8.076   1.00 37.54 ? 129 ALA   D N   1 
ATOM   5011 C  CA  . ALA   D 1 36  ? -45.939 10.223  8.042   1.00 38.73 ? 129 ALA   D CA  1 
ATOM   5012 C  C   . ALA   D 1 36  ? -44.782 11.213  8.219   1.00 38.30 ? 129 ALA   D C   1 
ATOM   5013 O  O   . ALA   D 1 36  ? -44.809 12.272  7.570   1.00 39.71 ? 129 ALA   D O   1 
ATOM   5014 C  CB  . ALA   D 1 36  ? -47.018 10.422  9.084   1.00 39.76 ? 129 ALA   D CB  1 
ATOM   5015 N  N   . LEU   D 1 37  ? -43.801 10.888  9.058   1.00 37.37 ? 130 LEU   D N   1 
ATOM   5016 C  CA  . LEU   D 1 37  ? -42.665 11.789  9.386   1.00 36.84 ? 130 LEU   D CA  1 
ATOM   5017 C  C   . LEU   D 1 37  ? -41.396 11.408  8.614   1.00 35.86 ? 130 LEU   D C   1 
ATOM   5018 O  O   . LEU   D 1 37  ? -40.445 12.191  8.706   1.00 35.51 ? 130 LEU   D O   1 
ATOM   5019 C  CB  . LEU   D 1 37  ? -42.413 11.720  10.895  1.00 36.53 ? 130 LEU   D CB  1 
ATOM   5020 C  CG  . LEU   D 1 37  ? -43.525 12.287  11.769  1.00 37.77 ? 130 LEU   D CG  1 
ATOM   5021 C  CD1 . LEU   D 1 37  ? -43.314 11.885  13.219  1.00 37.99 ? 130 LEU   D CD1 1 
ATOM   5022 C  CD2 . LEU   D 1 37  ? -43.594 13.809  11.639  1.00 38.79 ? 130 LEU   D CD2 1 
ATOM   5023 N  N   . ASN   D 1 38  ? -41.387 10.265  7.902   1.00 35.59 ? 131 ASN   D N   1 
ATOM   5024 C  CA  . ASN   D 1 38  ? -40.186 9.607   7.307   1.00 34.35 ? 131 ASN   D CA  1 
ATOM   5025 C  C   . ASN   D 1 38  ? -39.072 9.574   8.366   1.00 33.50 ? 131 ASN   D C   1 
ATOM   5026 O  O   . ASN   D 1 38  ? -37.944 10.063  8.104   1.00 32.19 ? 131 ASN   D O   1 
ATOM   5027 C  CB  . ASN   D 1 38  ? -39.749 10.276  5.998   1.00 34.75 ? 131 ASN   D CB  1 
ATOM   5028 C  CG  . ASN   D 1 38  ? -38.623 9.550   5.291   1.00 34.16 ? 131 ASN   D CG  1 
ATOM   5029 O  OD1 . ASN   D 1 38  ? -38.513 8.325   5.365   1.00 34.67 ? 131 ASN   D OD1 1 
ATOM   5030 N  ND2 . ASN   D 1 38  ? -37.789 10.290  4.580   1.00 34.18 ? 131 ASN   D ND2 1 
ATOM   5031 N  N   . LYS   D 1 39  ? -39.392 9.029   9.535   1.00 33.60 ? 132 LYS   D N   1 
ATOM   5032 C  CA  . LYS   D 1 39  ? -38.525 9.104   10.730  1.00 33.45 ? 132 LYS   D CA  1 
ATOM   5033 C  C   . LYS   D 1 39  ? -38.505 7.750   11.439  1.00 33.83 ? 132 LYS   D C   1 
ATOM   5034 O  O   . LYS   D 1 39  ? -39.592 7.229   11.778  1.00 33.94 ? 132 LYS   D O   1 
ATOM   5035 C  CB  . LYS   D 1 39  ? -39.000 10.216  11.666  1.00 33.92 ? 132 LYS   D CB  1 
ATOM   5036 C  CG  . LYS   D 1 39  ? -38.074 10.496  12.841  1.00 33.57 ? 132 LYS   D CG  1 
ATOM   5037 C  CD  . LYS   D 1 39  ? -38.451 11.760  13.580  1.00 34.45 ? 132 LYS   D CD  1 
ATOM   5038 C  CE  . LYS   D 1 39  ? -37.477 12.096  14.687  1.00 34.64 ? 132 LYS   D CE  1 
ATOM   5039 N  NZ  . LYS   D 1 39  ? -37.579 13.519  15.070  1.00 35.76 ? 132 LYS   D NZ  1 
ATOM   5040 N  N   A MET   D 1 40  ? -37.298 7.210   11.636  0.50 34.14 ? 133 MET   D N   1 
ATOM   5041 N  N   B MET   D 1 40  ? -37.306 7.197   11.652  0.50 32.96 ? 133 MET   D N   1 
ATOM   5042 C  CA  A MET   D 1 40  ? -37.019 6.004   12.453  0.50 34.90 ? 133 MET   D CA  1 
ATOM   5043 C  CA  B MET   D 1 40  ? -37.090 5.970   12.460  0.50 32.95 ? 133 MET   D CA  1 
ATOM   5044 C  C   A MET   D 1 40  ? -36.826 6.431   13.912  0.50 34.82 ? 133 MET   D C   1 
ATOM   5045 C  C   B MET   D 1 40  ? -36.798 6.375   13.909  0.50 33.65 ? 133 MET   D C   1 
ATOM   5046 O  O   A MET   D 1 40  ? -36.024 7.356   14.155  0.50 34.59 ? 133 MET   D O   1 
ATOM   5047 O  O   B MET   D 1 40  ? -35.902 7.213   14.144  0.50 33.48 ? 133 MET   D O   1 
ATOM   5048 C  CB  A MET   D 1 40  ? -35.753 5.297   11.959  0.50 35.40 ? 133 MET   D CB  1 
ATOM   5049 C  CB  B MET   D 1 40  ? -35.931 5.132   11.911  0.50 31.84 ? 133 MET   D CB  1 
ATOM   5050 C  CG  A MET   D 1 40  ? -35.364 4.112   12.808  0.50 36.22 ? 133 MET   D CG  1 
ATOM   5051 C  CG  B MET   D 1 40  ? -35.189 4.362   12.974  0.50 31.47 ? 133 MET   D CG  1 
ATOM   5052 S  SD  A MET   D 1 40  ? -36.577 2.775   12.678  0.50 39.45 ? 133 MET   D SD  1 
ATOM   5053 S  SD  B MET   D 1 40  ? -33.802 3.426   12.282  0.50 30.76 ? 133 MET   D SD  1 
ATOM   5054 C  CE  A MET   D 1 40  ? -36.227 2.115   11.044  0.50 38.12 ? 133 MET   D CE  1 
ATOM   5055 C  CE  B MET   D 1 40  ? -34.674 2.442   11.065  0.50 30.62 ? 133 MET   D CE  1 
ATOM   5056 N  N   . PHE   D 1 41  ? -37.556 5.803   14.841  1.00 34.52 ? 134 PHE   D N   1 
ATOM   5057 C  CA  . PHE   D 1 41  ? -37.328 5.912   16.303  1.00 34.65 ? 134 PHE   D CA  1 
ATOM   5058 C  C   . PHE   D 1 41  ? -36.713 4.588   16.749  1.00 34.18 ? 134 PHE   D C   1 
ATOM   5059 O  O   . PHE   D 1 41  ? -37.354 3.555   16.533  1.00 33.68 ? 134 PHE   D O   1 
ATOM   5060 C  CB  . PHE   D 1 41  ? -38.639 6.199   17.041  1.00 35.74 ? 134 PHE   D CB  1 
ATOM   5061 C  CG  . PHE   D 1 41  ? -39.358 7.439   16.577  1.00 35.95 ? 134 PHE   D CG  1 
ATOM   5062 C  CD1 . PHE   D 1 41  ? -40.056 7.455   15.375  1.00 36.40 ? 134 PHE   D CD1 1 
ATOM   5063 C  CD2 . PHE   D 1 41  ? -39.331 8.597   17.337  1.00 36.53 ? 134 PHE   D CD2 1 
ATOM   5064 C  CE1 . PHE   D 1 41  ? -40.712 8.600   14.942  1.00 36.75 ? 134 PHE   D CE1 1 
ATOM   5065 C  CE2 . PHE   D 1 41  ? -39.989 9.738   16.907  1.00 37.31 ? 134 PHE   D CE2 1 
ATOM   5066 C  CZ  . PHE   D 1 41  ? -40.681 9.738   15.718  1.00 37.66 ? 134 PHE   D CZ  1 
ATOM   5067 N  N   . CYS   D 1 42  ? -35.523 4.612   17.354  1.00 34.95 ? 135 CYS   D N   1 
ATOM   5068 C  CA  . CYS   D 1 42  ? -34.812 3.373   17.763  1.00 35.04 ? 135 CYS   D CA  1 
ATOM   5069 C  C   . CYS   D 1 42  ? -34.099 3.581   19.107  1.00 34.99 ? 135 CYS   D C   1 
ATOM   5070 O  O   . CYS   D 1 42  ? -33.855 4.724   19.496  1.00 35.20 ? 135 CYS   D O   1 
ATOM   5071 C  CB  . CYS   D 1 42  ? -33.861 2.934   16.662  1.00 35.19 ? 135 CYS   D CB  1 
ATOM   5072 S  SG  . CYS   D 1 42  ? -32.550 4.120   16.296  1.00 37.60 ? 135 CYS   D SG  1 
ATOM   5073 N  N   . GLN   D 1 43  ? -33.823 2.485   19.807  1.00 34.38 ? 136 GLN   D N   1 
ATOM   5074 C  CA  . GLN   D 1 43  ? -33.034 2.466   21.059  1.00 34.81 ? 136 GLN   D CA  1 
ATOM   5075 C  C   . GLN   D 1 43  ? -31.561 2.307   20.696  1.00 33.98 ? 136 GLN   D C   1 
ATOM   5076 O  O   . GLN   D 1 43  ? -31.273 1.664   19.660  1.00 32.56 ? 136 GLN   D O   1 
ATOM   5077 C  CB  . GLN   D 1 43  ? -33.456 1.298   21.947  1.00 36.08 ? 136 GLN   D CB  1 
ATOM   5078 C  CG  . GLN   D 1 43  ? -34.834 1.454   22.545  1.00 36.85 ? 136 GLN   D CG  1 
ATOM   5079 C  CD  . GLN   D 1 43  ? -35.264 0.214   23.290  1.00 38.49 ? 136 GLN   D CD  1 
ATOM   5080 O  OE1 . GLN   D 1 43  ? -34.855 -0.903  22.981  1.00 38.57 ? 136 GLN   D OE1 1 
ATOM   5081 N  NE2 . GLN   D 1 43  ? -36.072 0.415   24.320  1.00 39.61 ? 136 GLN   D NE2 1 
ATOM   5082 N  N   . LEU   D 1 44  ? -30.686 2.830   21.560  1.00 35.10 ? 137 LEU   D N   1 
ATOM   5083 C  CA  . LEU   D 1 44  ? -29.210 2.725   21.458  1.00 35.60 ? 137 LEU   D CA  1 
ATOM   5084 C  C   . LEU   D 1 44  ? -28.798 1.249   21.346  1.00 36.29 ? 137 LEU   D C   1 
ATOM   5085 O  O   . LEU   D 1 44  ? -29.303 0.398   22.111  1.00 36.91 ? 137 LEU   D O   1 
ATOM   5086 C  CB  . LEU   D 1 44  ? -28.629 3.471   22.667  1.00 36.50 ? 137 LEU   D CB  1 
ATOM   5087 C  CG  . LEU   D 1 44  ? -27.134 3.430   23.004  1.00 36.94 ? 137 LEU   D CG  1 
ATOM   5088 C  CD1 . LEU   D 1 44  ? -26.223 2.885   21.922  1.00 36.03 ? 137 LEU   D CD1 1 
ATOM   5089 C  CD2 . LEU   D 1 44  ? -26.661 4.823   23.415  1.00 37.74 ? 137 LEU   D CD2 1 
ATOM   5090 N  N   . ALA   D 1 45  ? -27.948 0.969   20.353  1.00 36.66 ? 138 ALA   D N   1 
ATOM   5091 C  CA  . ALA   D 1 45  ? -27.252 -0.322  20.131  1.00 37.18 ? 138 ALA   D CA  1 
ATOM   5092 C  C   . ALA   D 1 45  ? -28.222 -1.425  19.701  1.00 37.79 ? 138 ALA   D C   1 
ATOM   5093 O  O   . ALA   D 1 45  ? -27.726 -2.547  19.456  1.00 38.89 ? 138 ALA   D O   1 
ATOM   5094 C  CB  . ALA   D 1 45  ? -26.500 -0.720  21.376  1.00 38.58 ? 138 ALA   D CB  1 
ATOM   5095 N  N   . LYS   D 1 46  ? -29.526 -1.141  19.579  1.00 37.60 ? 139 LYS   D N   1 
ATOM   5096 C  CA  . LYS   D 1 46  ? -30.534 -2.170  19.201  1.00 37.89 ? 139 LYS   D CA  1 
ATOM   5097 C  C   . LYS   D 1 46  ? -30.641 -2.275  17.667  1.00 36.99 ? 139 LYS   D C   1 
ATOM   5098 O  O   . LYS   D 1 46  ? -30.343 -1.290  16.950  1.00 34.94 ? 139 LYS   D O   1 
ATOM   5099 C  CB  . LYS   D 1 46  ? -31.888 -1.881  19.861  1.00 38.88 ? 139 LYS   D CB  1 
ATOM   5100 C  CG  . LYS   D 1 46  ? -31.959 -2.160  21.360  1.00 40.24 ? 139 LYS   D CG  1 
ATOM   5101 C  CD  . LYS   D 1 46  ? -32.218 -3.607  21.718  1.00 41.10 ? 139 LYS   D CD  1 
ATOM   5102 C  CE  . LYS   D 1 46  ? -32.433 -3.818  23.203  1.00 42.78 ? 139 LYS   D CE  1 
ATOM   5103 N  NZ  . LYS   D 1 46  ? -31.221 -3.493  23.988  1.00 43.54 ? 139 LYS   D NZ  1 
ATOM   5104 N  N   . THR   D 1 47  ? -31.055 -3.449  17.191  1.00 36.76 ? 140 THR   D N   1 
ATOM   5105 C  CA  . THR   D 1 47  ? -31.189 -3.805  15.755  1.00 36.59 ? 140 THR   D CA  1 
ATOM   5106 C  C   . THR   D 1 47  ? -32.204 -2.899  15.057  1.00 36.73 ? 140 THR   D C   1 
ATOM   5107 O  O   . THR   D 1 47  ? -33.372 -2.850  15.488  1.00 36.62 ? 140 THR   D O   1 
ATOM   5108 C  CB  . THR   D 1 47  ? -31.629 -5.261  15.593  1.00 37.24 ? 140 THR   D CB  1 
ATOM   5109 O  OG1 . THR   D 1 47  ? -30.717 -6.033  16.372  1.00 36.67 ? 140 THR   D OG1 1 
ATOM   5110 C  CG2 . THR   D 1 47  ? -31.673 -5.703  14.145  1.00 36.91 ? 140 THR   D CG2 1 
ATOM   5111 N  N   A CYS   D 1 48  ? -31.766 -2.211  14.005  0.50 36.60 ? 141 CYS   D N   1 
ATOM   5112 N  N   B CYS   D 1 48  ? -31.763 -2.199  14.009  0.50 36.29 ? 141 CYS   D N   1 
ATOM   5113 C  CA  A CYS   D 1 48  ? -32.603 -1.319  13.158  0.50 36.91 ? 141 CYS   D CA  1 
ATOM   5114 C  CA  B CYS   D 1 48  ? -32.595 -1.316  13.147  0.50 36.39 ? 141 CYS   D CA  1 
ATOM   5115 C  C   A CYS   D 1 48  ? -32.622 -1.855  11.727  0.50 36.67 ? 141 CYS   D C   1 
ATOM   5116 C  C   B CYS   D 1 48  ? -32.610 -1.862  11.726  0.50 36.37 ? 141 CYS   D C   1 
ATOM   5117 O  O   A CYS   D 1 48  ? -31.746 -1.518  10.921  0.50 36.23 ? 141 CYS   D O   1 
ATOM   5118 O  O   B CYS   D 1 48  ? -31.725 -1.541  10.934  0.50 35.95 ? 141 CYS   D O   1 
ATOM   5119 C  CB  A CYS   D 1 48  ? -32.039 0.097   13.186  0.50 37.01 ? 141 CYS   D CB  1 
ATOM   5120 C  CB  B CYS   D 1 48  ? -32.049 0.103   13.123  0.50 36.15 ? 141 CYS   D CB  1 
ATOM   5121 S  SG  A CYS   D 1 48  ? -33.104 1.305   12.371  0.50 38.20 ? 141 CYS   D SG  1 
ATOM   5122 S  SG  B CYS   D 1 48  ? -31.930 0.836   14.770  0.50 36.93 ? 141 CYS   D SG  1 
ATOM   5123 N  N   . PRO   D 1 49  ? -33.604 -2.705  11.360  1.00 37.22 ? 142 PRO   D N   1 
ATOM   5124 C  CA  . PRO   D 1 49  ? -33.722 -3.198  9.993   1.00 36.74 ? 142 PRO   D CA  1 
ATOM   5125 C  C   . PRO   D 1 49  ? -34.048 -2.058  9.018   1.00 35.96 ? 142 PRO   D C   1 
ATOM   5126 O  O   . PRO   D 1 49  ? -34.961 -1.286  9.263   1.00 36.59 ? 142 PRO   D O   1 
ATOM   5127 C  CB  . PRO   D 1 49  ? -34.867 -4.218  10.069  1.00 37.31 ? 142 PRO   D CB  1 
ATOM   5128 C  CG  . PRO   D 1 49  ? -34.986 -4.549  11.534  1.00 38.79 ? 142 PRO   D CG  1 
ATOM   5129 C  CD  . PRO   D 1 49  ? -34.650 -3.250  12.228  1.00 37.93 ? 142 PRO   D CD  1 
ATOM   5130 N  N   . VAL   D 1 50  ? -33.258 -1.955  7.956   1.00 34.39 ? 143 VAL   D N   1 
ATOM   5131 C  CA  . VAL   D 1 50  ? -33.557 -1.096  6.782   1.00 34.32 ? 143 VAL   D CA  1 
ATOM   5132 C  C   . VAL   D 1 50  ? -33.603 -2.016  5.563   1.00 33.60 ? 143 VAL   D C   1 
ATOM   5133 O  O   . VAL   D 1 50  ? -32.629 -2.751  5.349   1.00 35.14 ? 143 VAL   D O   1 
ATOM   5134 C  CB  . VAL   D 1 50  ? -32.526 0.042   6.646   1.00 34.21 ? 143 VAL   D CB  1 
ATOM   5135 C  CG1 . VAL   D 1 50  ? -32.762 0.857   5.391   1.00 35.21 ? 143 VAL   D CG1 1 
ATOM   5136 C  CG2 . VAL   D 1 50  ? -32.545 0.952   7.863   1.00 34.46 ? 143 VAL   D CG2 1 
ATOM   5137 N  N   . GLN   D 1 51  ? -34.709 -1.997  4.829   1.00 34.05 ? 144 GLN   D N   1 
ATOM   5138 C  CA  . GLN   D 1 51  ? -34.896 -2.783  3.590   1.00 34.35 ? 144 GLN   D CA  1 
ATOM   5139 C  C   . GLN   D 1 51  ? -34.427 -1.965  2.388   1.00 34.23 ? 144 GLN   D C   1 
ATOM   5140 O  O   . GLN   D 1 51  ? -34.765 -0.760  2.310   1.00 33.36 ? 144 GLN   D O   1 
ATOM   5141 C  CB  . GLN   D 1 51  ? -36.357 -3.184  3.437   1.00 35.50 ? 144 GLN   D CB  1 
ATOM   5142 C  CG  . GLN   D 1 51  ? -36.883 -3.969  4.628   1.00 35.70 ? 144 GLN   D CG  1 
ATOM   5143 C  CD  . GLN   D 1 51  ? -38.377 -4.140  4.549   1.00 36.19 ? 144 GLN   D CD  1 
ATOM   5144 O  OE1 . GLN   D 1 51  ? -39.061 -3.451  3.793   1.00 37.14 ? 144 GLN   D OE1 1 
ATOM   5145 N  NE2 . GLN   D 1 51  ? -38.898 -5.063  5.337   1.00 36.63 ? 144 GLN   D NE2 1 
ATOM   5146 N  N   . LEU   D 1 52  ? -33.663 -2.608  1.503   1.00 34.36 ? 145 LEU   D N   1 
ATOM   5147 C  CA  . LEU   D 1 52  ? -33.309 -2.081  0.162   1.00 35.67 ? 145 LEU   D CA  1 
ATOM   5148 C  C   . LEU   D 1 52  ? -34.241 -2.732  -0.863  1.00 37.09 ? 145 LEU   D C   1 
ATOM   5149 O  O   . LEU   D 1 52  ? -34.284 -4.000  -0.937  1.00 37.70 ? 145 LEU   D O   1 
ATOM   5150 C  CB  . LEU   D 1 52  ? -31.840 -2.394  -0.151  1.00 35.31 ? 145 LEU   D CB  1 
ATOM   5151 C  CG  . LEU   D 1 52  ? -30.839 -2.132  0.972   1.00 34.61 ? 145 LEU   D CG  1 
ATOM   5152 C  CD1 . LEU   D 1 52  ? -29.442 -2.481  0.499   1.00 35.33 ? 145 LEU   D CD1 1 
ATOM   5153 C  CD2 . LEU   D 1 52  ? -30.916 -0.692  1.455   1.00 34.27 ? 145 LEU   D CD2 1 
ATOM   5154 N  N   . TRP   D 1 53  ? -34.982 -1.909  -1.606  1.00 38.76 ? 146 TRP   D N   1 
ATOM   5155 C  CA  . TRP   D 1 53  ? -35.857 -2.371  -2.712  1.00 40.84 ? 146 TRP   D CA  1 
ATOM   5156 C  C   . TRP   D 1 53  ? -35.285 -1.844  -4.026  1.00 41.46 ? 146 TRP   D C   1 
ATOM   5157 O  O   . TRP   D 1 53  ? -34.999 -0.632  -4.114  1.00 41.17 ? 146 TRP   D O   1 
ATOM   5158 C  CB  . TRP   D 1 53  ? -37.308 -1.928  -2.513  1.00 41.42 ? 146 TRP   D CB  1 
ATOM   5159 C  CG  . TRP   D 1 53  ? -37.985 -2.535  -1.326  1.00 41.95 ? 146 TRP   D CG  1 
ATOM   5160 C  CD1 . TRP   D 1 53  ? -37.719 -2.261  -0.015  1.00 41.20 ? 146 TRP   D CD1 1 
ATOM   5161 C  CD2 . TRP   D 1 53  ? -39.059 -3.496  -1.328  1.00 43.16 ? 146 TRP   D CD2 1 
ATOM   5162 N  NE1 . TRP   D 1 53  ? -38.554 -2.980  0.796   1.00 42.14 ? 146 TRP   D NE1 1 
ATOM   5163 C  CE2 . TRP   D 1 53  ? -39.385 -3.748  0.026   1.00 42.95 ? 146 TRP   D CE2 1 
ATOM   5164 C  CE3 . TRP   D 1 53  ? -39.752 -4.195  -2.323  1.00 44.44 ? 146 TRP   D CE3 1 
ATOM   5165 C  CZ2 . TRP   D 1 53  ? -40.380 -4.650  0.403   1.00 43.51 ? 146 TRP   D CZ2 1 
ATOM   5166 C  CZ3 . TRP   D 1 53  ? -40.762 -5.060  -1.949  1.00 45.25 ? 146 TRP   D CZ3 1 
ATOM   5167 C  CH2 . TRP   D 1 53  ? -41.049 -5.303  -0.606  1.00 44.93 ? 146 TRP   D CH2 1 
ATOM   5168 N  N   . VAL   D 1 54  ? -35.144 -2.735  -5.005  1.00 42.67 ? 147 VAL   D N   1 
ATOM   5169 C  CA  . VAL   D 1 54  ? -34.681 -2.414  -6.385  1.00 44.56 ? 147 VAL   D CA  1 
ATOM   5170 C  C   . VAL   D 1 54  ? -35.674 -3.020  -7.383  1.00 46.26 ? 147 VAL   D C   1 
ATOM   5171 O  O   . VAL   D 1 54  ? -36.252 -4.083  -7.076  1.00 46.41 ? 147 VAL   D O   1 
ATOM   5172 C  CB  . VAL   D 1 54  ? -33.244 -2.916  -6.617  1.00 43.50 ? 147 VAL   D CB  1 
ATOM   5173 C  CG1 . VAL   D 1 54  ? -32.235 -2.071  -5.864  1.00 42.34 ? 147 VAL   D CG1 1 
ATOM   5174 C  CG2 . VAL   D 1 54  ? -33.086 -4.390  -6.264  1.00 43.92 ? 147 VAL   D CG2 1 
ATOM   5175 N  N   . ASP   D 1 55  ? -35.887 -2.330  -8.507  1.00 48.46 ? 148 ASP   D N   1 
ATOM   5176 C  CA  . ASP   D 1 55  ? -36.689 -2.807  -9.662  1.00 50.95 ? 148 ASP   D CA  1 
ATOM   5177 C  C   . ASP   D 1 55  ? -35.847 -3.812  -10.452 1.00 51.70 ? 148 ASP   D C   1 
ATOM   5178 O  O   . ASP   D 1 55  ? -36.431 -4.749  -11.028 1.00 53.35 ? 148 ASP   D O   1 
ATOM   5179 C  CB  . ASP   D 1 55  ? -37.131 -1.648  -10.561 1.00 52.65 ? 148 ASP   D CB  1 
ATOM   5180 C  CG  . ASP   D 1 55  ? -38.156 -0.721  -9.935  1.00 53.53 ? 148 ASP   D CG  1 
ATOM   5181 O  OD1 . ASP   D 1 55  ? -38.883 -1.171  -9.025  1.00 53.11 ? 148 ASP   D OD1 1 
ATOM   5182 O  OD2 . ASP   D 1 55  ? -38.230 0.443   -10.379 1.00 54.92 ? 148 ASP   D OD2 1 
ATOM   5183 N  N   . SER   D 1 56  ? -34.528 -3.612  -10.478 1.00 50.48 ? 149 SER   D N   1 
ATOM   5184 C  CA  . SER   D 1 56  ? -33.561 -4.480  -11.199 1.00 51.07 ? 149 SER   D CA  1 
ATOM   5185 C  C   . SER   D 1 56  ? -32.319 -4.697  -10.329 1.00 48.72 ? 149 SER   D C   1 
ATOM   5186 O  O   . SER   D 1 56  ? -31.902 -3.749  -9.636  1.00 47.55 ? 149 SER   D O   1 
ATOM   5187 C  CB  . SER   D 1 56  ? -33.219 -3.906  -12.555 1.00 52.33 ? 149 SER   D CB  1 
ATOM   5188 O  OG  . SER   D 1 56  ? -32.791 -2.550  -12.449 1.00 51.74 ? 149 SER   D OG  1 
ATOM   5189 N  N   . THR   D 1 57  ? -31.782 -5.915  -10.367 1.00 48.61 ? 150 THR   D N   1 
ATOM   5190 C  CA  . THR   D 1 57  ? -30.634 -6.382  -9.552  1.00 47.71 ? 150 THR   D CA  1 
ATOM   5191 C  C   . THR   D 1 57  ? -29.373 -5.636  -9.972  1.00 46.98 ? 150 THR   D C   1 
ATOM   5192 O  O   . THR   D 1 57  ? -28.908 -5.779  -11.097 1.00 47.58 ? 150 THR   D O   1 
ATOM   5193 C  CB  . THR   D 1 57  ? -30.441 -7.894  -9.721  1.00 48.92 ? 150 THR   D CB  1 
ATOM   5194 O  OG1 . THR   D 1 57  ? -31.706 -8.515  -9.518  1.00 50.10 ? 150 THR   D OG1 1 
ATOM   5195 C  CG2 . THR   D 1 57  ? -29.445 -8.486  -8.755  1.00 48.43 ? 150 THR   D CG2 1 
ATOM   5196 N  N   . PRO   D 1 58  ? -28.776 -4.806  -9.091  1.00 44.92 ? 151 PRO   D N   1 
ATOM   5197 C  CA  . PRO   D 1 58  ? -27.461 -4.231  -9.375  1.00 44.23 ? 151 PRO   D CA  1 
ATOM   5198 C  C   . PRO   D 1 58  ? -26.391 -5.301  -9.578  1.00 44.47 ? 151 PRO   D C   1 
ATOM   5199 O  O   . PRO   D 1 58  ? -26.533 -6.427  -9.115  1.00 44.77 ? 151 PRO   D O   1 
ATOM   5200 C  CB  . PRO   D 1 58  ? -27.157 -3.377  -8.139  1.00 43.01 ? 151 PRO   D CB  1 
ATOM   5201 C  CG  . PRO   D 1 58  ? -28.512 -3.106  -7.513  1.00 42.63 ? 151 PRO   D CG  1 
ATOM   5202 C  CD  . PRO   D 1 58  ? -29.331 -4.352  -7.808  1.00 43.30 ? 151 PRO   D CD  1 
ATOM   5203 N  N   . PRO   D 1 59  ? -25.282 -4.991  -10.280 1.00 44.20 ? 152 PRO   D N   1 
ATOM   5204 C  CA  . PRO   D 1 59  ? -24.243 -5.990  -10.542 1.00 44.46 ? 152 PRO   D CA  1 
ATOM   5205 C  C   . PRO   D 1 59  ? -23.512 -6.421  -9.269  1.00 43.17 ? 152 PRO   D C   1 
ATOM   5206 O  O   . PRO   D 1 59  ? -23.515 -5.701  -8.269  1.00 41.53 ? 152 PRO   D O   1 
ATOM   5207 C  CB  . PRO   D 1 59  ? -23.309 -5.276  -11.527 1.00 45.11 ? 152 PRO   D CB  1 
ATOM   5208 C  CG  . PRO   D 1 59  ? -23.521 -3.797  -11.239 1.00 44.39 ? 152 PRO   D CG  1 
ATOM   5209 C  CD  . PRO   D 1 59  ? -24.982 -3.677  -10.865 1.00 44.30 ? 152 PRO   D CD  1 
ATOM   5210 N  N   . PRO   D 1 60  ? -22.860 -7.610  -9.254  1.00 43.35 ? 153 PRO   D N   1 
ATOM   5211 C  CA  . PRO   D 1 60  ? -22.017 -8.002  -8.123  1.00 42.26 ? 153 PRO   D CA  1 
ATOM   5212 C  C   . PRO   D 1 60  ? -20.951 -6.927  -7.847  1.00 40.75 ? 153 PRO   D C   1 
ATOM   5213 O  O   . PRO   D 1 60  ? -20.461 -6.344  -8.790  1.00 40.51 ? 153 PRO   D O   1 
ATOM   5214 C  CB  . PRO   D 1 60  ? -21.373 -9.326  -8.568  1.00 43.82 ? 153 PRO   D CB  1 
ATOM   5215 C  CG  . PRO   D 1 60  ? -22.298 -9.856  -9.648  1.00 45.35 ? 153 PRO   D CG  1 
ATOM   5216 C  CD  . PRO   D 1 60  ? -22.890 -8.628  -10.313 1.00 45.26 ? 153 PRO   D CD  1 
ATOM   5217 N  N   . GLY   D 1 61  ? -20.630 -6.684  -6.574  1.00 39.58 ? 154 GLY   D N   1 
ATOM   5218 C  CA  . GLY   D 1 61  ? -19.631 -5.680  -6.158  1.00 38.90 ? 154 GLY   D CA  1 
ATOM   5219 C  C   . GLY   D 1 61  ? -20.267 -4.316  -5.926  1.00 38.00 ? 154 GLY   D C   1 
ATOM   5220 O  O   . GLY   D 1 61  ? -19.557 -3.400  -5.472  1.00 38.11 ? 154 GLY   D O   1 
ATOM   5221 N  N   . THR   D 1 62  ? -21.568 -4.170  -6.193  1.00 37.59 ? 155 THR   D N   1 
ATOM   5222 C  CA  . THR   D 1 62  ? -22.382 -3.013  -5.734  1.00 36.52 ? 155 THR   D CA  1 
ATOM   5223 C  C   . THR   D 1 62  ? -22.246 -2.903  -4.212  1.00 34.84 ? 155 THR   D C   1 
ATOM   5224 O  O   . THR   D 1 62  ? -22.215 -3.954  -3.542  1.00 33.34 ? 155 THR   D O   1 
ATOM   5225 C  CB  . THR   D 1 62  ? -23.856 -3.165  -6.124  1.00 37.59 ? 155 THR   D CB  1 
ATOM   5226 O  OG1 . THR   D 1 62  ? -23.908 -3.248  -7.555  1.00 39.46 ? 155 THR   D OG1 1 
ATOM   5227 C  CG2 . THR   D 1 62  ? -24.719 -2.036  -5.594  1.00 36.81 ? 155 THR   D CG2 1 
ATOM   5228 N  N   . ARG   D 1 63  ? -22.169 -1.683  -3.680  1.00 33.47 ? 156 ARG   D N   1 
ATOM   5229 C  CA  . ARG   D 1 63  ? -21.978 -1.459  -2.224  1.00 32.71 ? 156 ARG   D CA  1 
ATOM   5230 C  C   . ARG   D 1 63  ? -23.078 -0.532  -1.695  1.00 31.39 ? 156 ARG   D C   1 
ATOM   5231 O  O   . ARG   D 1 63  ? -23.658 0.239   -2.493  1.00 30.69 ? 156 ARG   D O   1 
ATOM   5232 C  CB  . ARG   D 1 63  ? -20.549 -0.970  -1.970  1.00 32.98 ? 156 ARG   D CB  1 
ATOM   5233 C  CG  . ARG   D 1 63  ? -19.535 -2.102  -1.875  1.00 33.70 ? 156 ARG   D CG  1 
ATOM   5234 C  CD  . ARG   D 1 63  ? -18.148 -1.724  -2.361  1.00 34.44 ? 156 ARG   D CD  1 
ATOM   5235 N  NE  . ARG   D 1 63  ? -17.555 -0.534  -1.759  1.00 34.71 ? 156 ARG   D NE  1 
ATOM   5236 C  CZ  . ARG   D 1 63  ? -16.735 -0.514  -0.697  1.00 34.94 ? 156 ARG   D CZ  1 
ATOM   5237 N  NH1 . ARG   D 1 63  ? -16.418 -1.623  -0.052  1.00 35.13 ? 156 ARG   D NH1 1 
ATOM   5238 N  NH2 . ARG   D 1 63  ? -16.250 0.633   -0.266  1.00 34.77 ? 156 ARG   D NH2 1 
ATOM   5239 N  N   . VAL   D 1 64  ? -23.373 -0.662  -0.396  1.00 30.71 ? 157 VAL   D N   1 
ATOM   5240 C  CA  . VAL   D 1 64  ? -24.382 0.153   0.328   1.00 31.04 ? 157 VAL   D CA  1 
ATOM   5241 C  C   . VAL   D 1 64  ? -23.687 0.872   1.490   1.00 30.32 ? 157 VAL   D C   1 
ATOM   5242 O  O   . VAL   D 1 64  ? -23.196 0.186   2.424   1.00 30.04 ? 157 VAL   D O   1 
ATOM   5243 C  CB  . VAL   D 1 64  ? -25.538 -0.726  0.828   1.00 31.55 ? 157 VAL   D CB  1 
ATOM   5244 C  CG1 . VAL   D 1 64  ? -26.695 0.117   1.343   1.00 32.01 ? 157 VAL   D CG1 1 
ATOM   5245 C  CG2 . VAL   D 1 64  ? -25.989 -1.694  -0.239  1.00 32.28 ? 157 VAL   D CG2 1 
ATOM   5246 N  N   . ARG   D 1 65  ? -23.679 2.204   1.425   1.00 29.89 ? 158 ARG   D N   1 
ATOM   5247 C  CA  . ARG   D 1 65  ? -23.096 3.095   2.451   1.00 29.47 ? 158 ARG   D CA  1 
ATOM   5248 C  C   . ARG   D 1 65  ? -24.218 3.766   3.245   1.00 29.11 ? 158 ARG   D C   1 
ATOM   5249 O  O   . ARG   D 1 65  ? -25.258 4.130   2.635   1.00 30.13 ? 158 ARG   D O   1 
ATOM   5250 C  CB  . ARG   D 1 65  ? -22.192 4.116   1.763   1.00 29.65 ? 158 ARG   D CB  1 
ATOM   5251 C  CG  . ARG   D 1 65  ? -21.478 5.078   2.701   1.00 29.37 ? 158 ARG   D CG  1 
ATOM   5252 C  CD  . ARG   D 1 65  ? -20.598 6.014   1.904   1.00 29.70 ? 158 ARG   D CD  1 
ATOM   5253 N  NE  . ARG   D 1 65  ? -19.725 5.278   0.990   1.00 30.15 ? 158 ARG   D NE  1 
ATOM   5254 C  CZ  . ARG   D 1 65  ? -18.540 4.749   1.295   1.00 29.35 ? 158 ARG   D CZ  1 
ATOM   5255 N  NH1 . ARG   D 1 65  ? -18.042 4.855   2.512   1.00 29.22 ? 158 ARG   D NH1 1 
ATOM   5256 N  NH2 . ARG   D 1 65  ? -17.851 4.114   0.371   1.00 29.58 ? 158 ARG   D NH2 1 
ATOM   5257 N  N   . ALA   D 1 66  ? -24.003 3.895   4.556   1.00 29.07 ? 159 ALA   D N   1 
ATOM   5258 C  CA  . ALA   D 1 66  ? -24.812 4.695   5.501   1.00 29.09 ? 159 ALA   D CA  1 
ATOM   5259 C  C   . ALA   D 1 66  ? -23.927 5.798   6.079   1.00 29.24 ? 159 ALA   D C   1 
ATOM   5260 O  O   . ALA   D 1 66  ? -22.758 5.514   6.445   1.00 29.08 ? 159 ALA   D O   1 
ATOM   5261 C  CB  . ALA   D 1 66  ? -25.371 3.813   6.586   1.00 28.81 ? 159 ALA   D CB  1 
ATOM   5262 N  N   . MET   D 1 67  ? -24.482 7.000   6.204   1.00 29.75 ? 160 MET   D N   1 
ATOM   5263 C  CA  . MET   D 1 67  ? -23.810 8.193   6.773   1.00 30.26 ? 160 MET   D CA  1 
ATOM   5264 C  C   . MET   D 1 67  ? -24.875 9.061   7.456   1.00 30.09 ? 160 MET   D C   1 
ATOM   5265 O  O   . MET   D 1 67  ? -25.983 9.202   6.901   1.00 29.60 ? 160 MET   D O   1 
ATOM   5266 C  CB  . MET   D 1 67  ? -23.141 8.997   5.656   1.00 31.87 ? 160 MET   D CB  1 
ATOM   5267 C  CG  . MET   D 1 67  ? -22.492 10.285  6.121   1.00 33.37 ? 160 MET   D CG  1 
ATOM   5268 S  SD  . MET   D 1 67  ? -21.909 11.310  4.743   1.00 35.58 ? 160 MET   D SD  1 
ATOM   5269 C  CE  . MET   D 1 67  ? -20.564 10.293  4.128   1.00 35.59 ? 160 MET   D CE  1 
ATOM   5270 N  N   . ALA   D 1 68  ? -24.563 9.609   8.629   1.00 30.08 ? 161 ALA   D N   1 
ATOM   5271 C  CA  . ALA   D 1 68  ? -25.440 10.549  9.356   1.00 30.38 ? 161 ALA   D CA  1 
ATOM   5272 C  C   . ALA   D 1 68  ? -25.006 11.976  9.048   1.00 31.03 ? 161 ALA   D C   1 
ATOM   5273 O  O   . ALA   D 1 68  ? -23.808 12.227  8.920   1.00 31.86 ? 161 ALA   D O   1 
ATOM   5274 C  CB  . ALA   D 1 68  ? -25.401 10.293  10.832  1.00 30.61 ? 161 ALA   D CB  1 
ATOM   5275 N  N   A ILE   D 1 69  ? -25.968 12.871  8.855   0.60 32.04 ? 162 ILE   D N   1 
ATOM   5276 N  N   B ILE   D 1 69  ? -25.985 12.875  9.052   0.40 32.15 ? 162 ILE   D N   1 
ATOM   5277 C  CA  A ILE   D 1 69  ? -25.760 14.350  8.790   0.60 32.95 ? 162 ILE   D CA  1 
ATOM   5278 C  CA  B ILE   D 1 69  ? -25.800 14.330  8.797   0.40 33.22 ? 162 ILE   D CA  1 
ATOM   5279 C  C   A ILE   D 1 69  ? -26.799 14.983  9.715   0.60 33.68 ? 162 ILE   D C   1 
ATOM   5280 C  C   B ILE   D 1 69  ? -26.888 15.083  9.557   0.40 33.89 ? 162 ILE   D C   1 
ATOM   5281 O  O   A ILE   D 1 69  ? -27.825 14.327  9.959   0.60 33.39 ? 162 ILE   D O   1 
ATOM   5282 O  O   B ILE   D 1 69  ? -28.063 14.648  9.483   0.40 33.68 ? 162 ILE   D O   1 
ATOM   5283 C  CB  A ILE   D 1 69  ? -25.904 14.868  7.347   0.60 33.52 ? 162 ILE   D CB  1 
ATOM   5284 C  CB  B ILE   D 1 69  ? -25.882 14.605  7.292   0.40 33.73 ? 162 ILE   D CB  1 
ATOM   5285 C  CG1 A ILE   D 1 69  ? -24.858 14.287  6.391   0.60 33.35 ? 162 ILE   D CG1 1 
ATOM   5286 C  CG1 B ILE   D 1 69  ? -25.391 16.015  6.962   0.40 35.08 ? 162 ILE   D CG1 1 
ATOM   5287 C  CG2 A ILE   D 1 69  ? -25.906 16.398  7.349   0.60 34.56 ? 162 ILE   D CG2 1 
ATOM   5288 C  CG2 B ILE   D 1 69  ? -27.298 14.359  6.801   0.40 33.80 ? 162 ILE   D CG2 1 
ATOM   5289 C  CD1 A ILE   D 1 69  ? -24.901 14.884  4.998   0.60 34.17 ? 162 ILE   D CD1 1 
ATOM   5290 C  CD1 B ILE   D 1 69  ? -26.091 16.632  5.795   0.40 35.96 ? 162 ILE   D CD1 1 
ATOM   5291 N  N   . TYR   D 1 70  ? -26.530 16.185  10.225  1.00 34.71 ? 163 TYR   D N   1 
ATOM   5292 C  CA  . TYR   D 1 70  ? -27.514 17.026  10.955  1.00 35.72 ? 163 TYR   D CA  1 
ATOM   5293 C  C   . TYR   D 1 70  ? -28.537 17.552  9.952   1.00 36.43 ? 163 TYR   D C   1 
ATOM   5294 O  O   . TYR   D 1 70  ? -28.159 17.869  8.814   1.00 36.36 ? 163 TYR   D O   1 
ATOM   5295 C  CB  . TYR   D 1 70  ? -26.815 18.137  11.742  1.00 36.30 ? 163 TYR   D CB  1 
ATOM   5296 C  CG  . TYR   D 1 70  ? -26.072 17.601  12.936  1.00 35.89 ? 163 TYR   D CG  1 
ATOM   5297 C  CD1 . TYR   D 1 70  ? -26.763 17.027  13.986  1.00 35.19 ? 163 TYR   D CD1 1 
ATOM   5298 C  CD2 . TYR   D 1 70  ? -24.686 17.637  13.007  1.00 35.72 ? 163 TYR   D CD2 1 
ATOM   5299 C  CE1 . TYR   D 1 70  ? -26.100 16.506  15.083  1.00 34.76 ? 163 TYR   D CE1 1 
ATOM   5300 C  CE2 . TYR   D 1 70  ? -24.010 17.134  14.109  1.00 35.66 ? 163 TYR   D CE2 1 
ATOM   5301 C  CZ  . TYR   D 1 70  ? -24.723 16.559  15.142  1.00 35.02 ? 163 TYR   D CZ  1 
ATOM   5302 O  OH  . TYR   D 1 70  ? -24.068 16.047  16.213  1.00 34.97 ? 163 TYR   D OH  1 
ATOM   5303 N  N   . LYS   D 1 71  ? -29.799 17.599  10.367  1.00 37.57 ? 164 LYS   D N   1 
ATOM   5304 C  CA  . LYS   D 1 71  ? -30.934 17.956  9.484   1.00 38.81 ? 164 LYS   D CA  1 
ATOM   5305 C  C   . LYS   D 1 71  ? -30.966 19.475  9.307   1.00 42.00 ? 164 LYS   D C   1 
ATOM   5306 O  O   . LYS   D 1 71  ? -31.244 19.920  8.185   1.00 42.23 ? 164 LYS   D O   1 
ATOM   5307 C  CB  . LYS   D 1 71  ? -32.243 17.445  10.081  1.00 38.82 ? 164 LYS   D CB  1 
ATOM   5308 C  CG  . LYS   D 1 71  ? -33.472 17.642  9.212   1.00 38.74 ? 164 LYS   D CG  1 
ATOM   5309 C  CD  . LYS   D 1 71  ? -34.692 17.081  9.883   1.00 38.51 ? 164 LYS   D CD  1 
ATOM   5310 C  CE  . LYS   D 1 71  ? -35.965 17.307  9.099   1.00 39.09 ? 164 LYS   D CE  1 
ATOM   5311 N  NZ  . LYS   D 1 71  ? -37.144 17.311  9.997   1.00 39.79 ? 164 LYS   D NZ  1 
ATOM   5312 N  N   . GLN   D 1 72  ? -30.692 20.221  10.381  1.00 44.51 ? 165 GLN   D N   1 
ATOM   5313 C  CA  . GLN   D 1 72  ? -30.789 21.705  10.429  1.00 47.89 ? 165 GLN   D CA  1 
ATOM   5314 C  C   . GLN   D 1 72  ? -29.630 22.317  9.638   1.00 49.17 ? 165 GLN   D C   1 
ATOM   5315 O  O   . GLN   D 1 72  ? -28.496 21.824  9.772   1.00 49.15 ? 165 GLN   D O   1 
ATOM   5316 C  CB  . GLN   D 1 72  ? -30.783 22.184  11.879  1.00 50.19 ? 165 GLN   D CB  1 
ATOM   5317 C  CG  . GLN   D 1 72  ? -32.012 21.748  12.669  1.00 51.16 ? 165 GLN   D CG  1 
ATOM   5318 C  CD  . GLN   D 1 72  ? -31.778 21.757  14.161  1.00 52.65 ? 165 GLN   D CD  1 
ATOM   5319 O  OE1 . GLN   D 1 72  ? -30.799 21.215  14.663  1.00 53.40 ? 165 GLN   D OE1 1 
ATOM   5320 N  NE2 . GLN   D 1 72  ? -32.699 22.363  14.891  1.00 55.02 ? 165 GLN   D NE2 1 
ATOM   5321 N  N   . SER   D 1 73  ? -29.906 23.369  8.858   1.00 50.73 ? 166 SER   D N   1 
ATOM   5322 C  CA  . SER   D 1 73  ? -28.951 23.982  7.900   1.00 51.20 ? 166 SER   D CA  1 
ATOM   5323 C  C   . SER   D 1 73  ? -27.776 24.614  8.654   1.00 52.03 ? 166 SER   D C   1 
ATOM   5324 O  O   . SER   D 1 73  ? -26.662 24.611  8.101   1.00 51.86 ? 166 SER   D O   1 
ATOM   5325 C  CB  . SER   D 1 73  ? -29.638 24.980  7.005   1.00 53.21 ? 166 SER   D CB  1 
ATOM   5326 O  OG  . SER   D 1 73  ? -30.311 25.966  7.769   1.00 54.87 ? 166 SER   D OG  1 
ATOM   5327 N  N   . GLN   D 1 74  ? -28.010 25.112  9.871   1.00 52.56 ? 167 GLN   D N   1 
ATOM   5328 C  CA  . GLN   D 1 74  ? -26.980 25.805  10.694  1.00 52.81 ? 167 GLN   D CA  1 
ATOM   5329 C  C   . GLN   D 1 74  ? -26.021 24.789  11.343  1.00 50.60 ? 167 GLN   D C   1 
ATOM   5330 O  O   . GLN   D 1 74  ? -24.987 25.234  11.865  1.00 49.77 ? 167 GLN   D O   1 
ATOM   5331 C  CB  . GLN   D 1 74  ? -27.627 26.716  11.742  1.00 54.32 ? 167 GLN   D CB  1 
ATOM   5332 C  CG  . GLN   D 1 74  ? -28.452 25.995  12.798  1.00 53.79 ? 167 GLN   D CG  1 
ATOM   5333 C  CD  . GLN   D 1 74  ? -29.924 25.950  12.460  1.00 54.43 ? 167 GLN   D CD  1 
ATOM   5334 O  OE1 . GLN   D 1 74  ? -30.326 25.827  11.302  1.00 54.99 ? 167 GLN   D OE1 1 
ATOM   5335 N  NE2 . GLN   D 1 74  ? -30.754 25.994  13.487  1.00 54.97 ? 167 GLN   D NE2 1 
ATOM   5336 N  N   . HIS   D 1 75  ? -26.326 23.487  11.312  1.00 48.01 ? 168 HIS   D N   1 
ATOM   5337 C  CA  . HIS   D 1 75  ? -25.500 22.423  11.949  1.00 46.95 ? 168 HIS   D CA  1 
ATOM   5338 C  C   . HIS   D 1 75  ? -24.960 21.431  10.912  1.00 46.12 ? 168 HIS   D C   1 
ATOM   5339 O  O   . HIS   D 1 75  ? -24.241 20.489  11.313  1.00 44.19 ? 168 HIS   D O   1 
ATOM   5340 C  CB  . HIS   D 1 75  ? -26.318 21.671  13.006  1.00 46.48 ? 168 HIS   D CB  1 
ATOM   5341 C  CG  . HIS   D 1 75  ? -26.756 22.515  14.153  1.00 47.84 ? 168 HIS   D CG  1 
ATOM   5342 N  ND1 . HIS   D 1 75  ? -25.858 23.217  14.932  1.00 48.90 ? 168 HIS   D ND1 1 
ATOM   5343 C  CD2 . HIS   D 1 75  ? -27.978 22.742  14.678  1.00 48.17 ? 168 HIS   D CD2 1 
ATOM   5344 C  CE1 . HIS   D 1 75  ? -26.509 23.854  15.884  1.00 49.95 ? 168 HIS   D CE1 1 
ATOM   5345 N  NE2 . HIS   D 1 75  ? -27.814 23.582  15.747  1.00 49.91 ? 168 HIS   D NE2 1 
ATOM   5346 N  N   . MET   D 1 76  ? -25.273 21.636  9.630   1.00 46.49 ? 169 MET   D N   1 
ATOM   5347 C  CA  . MET   D 1 76  ? -25.149 20.616  8.558   1.00 44.73 ? 169 MET   D CA  1 
ATOM   5348 C  C   . MET   D 1 76  ? -23.673 20.342  8.237   1.00 43.64 ? 169 MET   D C   1 
ATOM   5349 O  O   . MET   D 1 76  ? -23.374 19.181  7.848   1.00 41.64 ? 169 MET   D O   1 
ATOM   5350 C  CB  . MET   D 1 76  ? -25.870 21.082  7.294   1.00 46.58 ? 169 MET   D CB  1 
ATOM   5351 C  CG  . MET   D 1 76  ? -26.207 19.949  6.355   1.00 46.46 ? 169 MET   D CG  1 
ATOM   5352 S  SD  . MET   D 1 76  ? -27.549 20.339  5.221   1.00 49.12 ? 169 MET   D SD  1 
ATOM   5353 C  CE  . MET   D 1 76  ? -27.165 22.005  4.669   1.00 50.46 ? 169 MET   D CE  1 
ATOM   5354 N  N   . THR   D 1 77  ? -22.792 21.335  8.405   1.00 43.40 ? 170 THR   D N   1 
ATOM   5355 C  CA  . THR   D 1 77  ? -21.334 21.227  8.119   1.00 42.95 ? 170 THR   D CA  1 
ATOM   5356 C  C   . THR   D 1 77  ? -20.604 20.553  9.289   1.00 41.98 ? 170 THR   D C   1 
ATOM   5357 O  O   . THR   D 1 77  ? -19.406 20.281  9.138   1.00 43.22 ? 170 THR   D O   1 
ATOM   5358 C  CB  . THR   D 1 77  ? -20.692 22.601  7.867   1.00 44.33 ? 170 THR   D CB  1 
ATOM   5359 O  OG1 . THR   D 1 77  ? -20.599 23.281  9.117   1.00 44.63 ? 170 THR   D OG1 1 
ATOM   5360 C  CG2 . THR   D 1 77  ? -21.453 23.457  6.881   1.00 45.15 ? 170 THR   D CG2 1 
ATOM   5361 N  N   . GLU   D 1 78  ? -21.272 20.331  10.422  1.00 40.90 ? 171 GLU   D N   1 
ATOM   5362 C  CA  . GLU   D 1 78  ? -20.686 19.632  11.594  1.00 40.41 ? 171 GLU   D CA  1 
ATOM   5363 C  C   . GLU   D 1 78  ? -20.776 18.115  11.357  1.00 38.49 ? 171 GLU   D C   1 
ATOM   5364 O  O   . GLU   D 1 78  ? -21.845 17.649  10.941  1.00 37.44 ? 171 GLU   D O   1 
ATOM   5365 C  CB  . GLU   D 1 78  ? -21.396 20.060  12.877  1.00 41.40 ? 171 GLU   D CB  1 
ATOM   5366 C  CG  . GLU   D 1 78  ? -20.790 19.454  14.129  1.00 41.86 ? 171 GLU   D CG  1 
ATOM   5367 C  CD  . GLU   D 1 78  ? -21.261 20.060  15.439  1.00 43.63 ? 171 GLU   D CD  1 
ATOM   5368 O  OE1 . GLU   D 1 78  ? -21.324 21.323  15.547  1.00 45.83 ? 171 GLU   D OE1 1 
ATOM   5369 O  OE2 . GLU   D 1 78  ? -21.576 19.272  16.353  1.00 43.81 ? 171 GLU   D OE2 1 
ATOM   5370 N  N   . VAL   D 1 79  ? -19.687 17.386  11.603  1.00 37.44 ? 172 VAL   D N   1 
ATOM   5371 C  CA  . VAL   D 1 79  ? -19.632 15.897  11.500  1.00 35.74 ? 172 VAL   D CA  1 
ATOM   5372 C  C   . VAL   D 1 79  ? -20.448 15.300  12.653  1.00 35.22 ? 172 VAL   D C   1 
ATOM   5373 O  O   . VAL   D 1 79  ? -20.217 15.681  13.826  1.00 35.58 ? 172 VAL   D O   1 
ATOM   5374 C  CB  . VAL   D 1 79  ? -18.189 15.361  11.558  1.00 35.86 ? 172 VAL   D CB  1 
ATOM   5375 C  CG1 . VAL   D 1 79  ? -18.165 13.842  11.545  1.00 34.53 ? 172 VAL   D CG1 1 
ATOM   5376 C  CG2 . VAL   D 1 79  ? -17.317 15.910  10.453  1.00 36.69 ? 172 VAL   D CG2 1 
ATOM   5377 N  N   . VAL   D 1 80  ? -21.341 14.364  12.347  1.00 34.57 ? 173 VAL   D N   1 
ATOM   5378 C  CA  . VAL   D 1 80  ? -22.109 13.609  13.378  1.00 34.26 ? 173 VAL   D CA  1 
ATOM   5379 C  C   . VAL   D 1 80  ? -21.197 12.496  13.900  1.00 34.48 ? 173 VAL   D C   1 
ATOM   5380 O  O   . VAL   D 1 80  ? -20.767 11.652  13.083  1.00 34.03 ? 173 VAL   D O   1 
ATOM   5381 C  CB  . VAL   D 1 80  ? -23.421 13.025  12.821  1.00 33.39 ? 173 VAL   D CB  1 
ATOM   5382 C  CG1 . VAL   D 1 80  ? -24.171 12.279  13.916  1.00 33.20 ? 173 VAL   D CG1 1 
ATOM   5383 C  CG2 . VAL   D 1 80  ? -24.312 14.092  12.178  1.00 34.14 ? 173 VAL   D CG2 1 
ATOM   5384 N  N   . ARG   D 1 81  ? -20.919 12.497  15.202  1.00 35.92 ? 174 ARG   D N   1 
ATOM   5385 C  CA  . ARG   D 1 81  ? -20.098 11.469  15.904  1.00 37.42 ? 174 ARG   D CA  1 
ATOM   5386 C  C   . ARG   D 1 81  ? -20.704 11.173  17.276  1.00 37.83 ? 174 ARG   D C   1 
ATOM   5387 O  O   . ARG   D 1 81  ? -21.582 11.943  17.726  1.00 39.10 ? 174 ARG   D O   1 
ATOM   5388 C  CB  . ARG   D 1 81  ? -18.655 11.954  16.080  1.00 38.88 ? 174 ARG   D CB  1 
ATOM   5389 C  CG  . ARG   D 1 81  ? -18.513 13.372  16.607  1.00 40.74 ? 174 ARG   D CG  1 
ATOM   5390 C  CD  . ARG   D 1 81  ? -17.086 13.756  16.971  1.00 42.62 ? 174 ARG   D CD  1 
ATOM   5391 N  NE  . ARG   D 1 81  ? -16.242 14.074  15.818  1.00 43.13 ? 174 ARG   D NE  1 
ATOM   5392 C  CZ  . ARG   D 1 81  ? -15.349 13.257  15.255  1.00 43.15 ? 174 ARG   D CZ  1 
ATOM   5393 N  NH1 . ARG   D 1 81  ? -15.168 12.022  15.708  1.00 42.55 ? 174 ARG   D NH1 1 
ATOM   5394 N  NH2 . ARG   D 1 81  ? -14.669 13.672  14.199  1.00 43.52 ? 174 ARG   D NH2 1 
ATOM   5395 N  N   . ARG   D 1 82  ? -20.229 10.114  17.932  1.00 38.31 ? 175 ARG   D N   1 
ATOM   5396 C  CA  . ARG   D 1 82  ? -20.619 9.773   19.321  1.00 39.23 ? 175 ARG   D CA  1 
ATOM   5397 C  C   . ARG   D 1 82  ? -20.077 10.839  20.279  1.00 40.81 ? 175 ARG   D C   1 
ATOM   5398 O  O   . ARG   D 1 82  ? -19.069 11.498  19.947  1.00 40.97 ? 175 ARG   D O   1 
ATOM   5399 C  CB  . ARG   D 1 82  ? -20.079 8.400   19.719  1.00 39.25 ? 175 ARG   D CB  1 
ATOM   5400 C  CG  . ARG   D 1 82  ? -20.572 7.268   18.833  1.00 38.63 ? 175 ARG   D CG  1 
ATOM   5401 C  CD  . ARG   D 1 82  ? -19.918 5.975   19.244  1.00 39.27 ? 175 ARG   D CD  1 
ATOM   5402 N  NE  . ARG   D 1 82  ? -20.645 5.331   20.328  1.00 39.79 ? 175 ARG   D NE  1 
ATOM   5403 C  CZ  . ARG   D 1 82  ? -20.227 4.252   20.980  1.00 40.55 ? 175 ARG   D CZ  1 
ATOM   5404 N  NH1 . ARG   D 1 82  ? -19.062 3.700   20.689  1.00 40.79 ? 175 ARG   D NH1 1 
ATOM   5405 N  NH2 . ARG   D 1 82  ? -20.978 3.737   21.936  1.00 41.17 ? 175 ARG   D NH2 1 
ATOM   5406 N  N   . CYS   D 1 83  ? -20.729 10.996  21.428  1.00 41.65 ? 176 CYS   D N   1 
ATOM   5407 C  CA  . CYS   D 1 83  ? -20.268 11.857  22.543  1.00 43.86 ? 176 CYS   D CA  1 
ATOM   5408 C  C   . CYS   D 1 83  ? -19.020 11.224  23.160  1.00 44.69 ? 176 CYS   D C   1 
ATOM   5409 O  O   . CYS   D 1 83  ? -18.788 10.022  23.027  1.00 44.54 ? 176 CYS   D O   1 
ATOM   5410 C  CB  . CYS   D 1 83  ? -21.394 12.019  23.556  1.00 44.31 ? 176 CYS   D CB  1 
ATOM   5411 S  SG  . CYS   D 1 83  ? -21.771 10.541  24.441  1.00 45.20 ? 176 CYS   D SG  1 
ATOM   5412 N  N   . PRO   D 1 84  ? -18.164 12.012  23.843  1.00 47.44 ? 177 PRO   D N   1 
ATOM   5413 C  CA  . PRO   D 1 84  ? -17.015 11.442  24.550  1.00 48.23 ? 177 PRO   D CA  1 
ATOM   5414 C  C   . PRO   D 1 84  ? -17.391 10.193  25.366  1.00 48.85 ? 177 PRO   D C   1 
ATOM   5415 O  O   . PRO   D 1 84  ? -16.735 9.175   25.205  1.00 49.10 ? 177 PRO   D O   1 
ATOM   5416 C  CB  . PRO   D 1 84  ? -16.567 12.612  25.431  1.00 50.40 ? 177 PRO   D CB  1 
ATOM   5417 C  CG  . PRO   D 1 84  ? -16.922 13.836  24.607  1.00 49.67 ? 177 PRO   D CG  1 
ATOM   5418 C  CD  . PRO   D 1 84  ? -18.243 13.479  23.957  1.00 48.06 ? 177 PRO   D CD  1 
ATOM   5419 N  N   . HIS   D 1 85  ? -18.463 10.276  26.164  1.00 49.16 ? 178 HIS   D N   1 
ATOM   5420 C  CA  . HIS   D 1 85  ? -18.900 9.210   27.106  1.00 49.38 ? 178 HIS   D CA  1 
ATOM   5421 C  C   . HIS   D 1 85  ? -19.063 7.876   26.368  1.00 48.45 ? 178 HIS   D C   1 
ATOM   5422 O  O   . HIS   D 1 85  ? -18.470 6.871   26.832  1.00 48.20 ? 178 HIS   D O   1 
ATOM   5423 C  CB  . HIS   D 1 85  ? -20.203 9.585   27.831  1.00 50.12 ? 178 HIS   D CB  1 
ATOM   5424 C  CG  . HIS   D 1 85  ? -20.828 8.440   28.558  1.00 49.79 ? 178 HIS   D CG  1 
ATOM   5425 N  ND1 . HIS   D 1 85  ? -20.260 7.912   29.698  1.00 51.83 ? 178 HIS   D ND1 1 
ATOM   5426 C  CD2 . HIS   D 1 85  ? -21.950 7.716   28.326  1.00 49.22 ? 178 HIS   D CD2 1 
ATOM   5427 C  CE1 . HIS   D 1 85  ? -20.999 6.915   30.140  1.00 51.54 ? 178 HIS   D CE1 1 
ATOM   5428 N  NE2 . HIS   D 1 85  ? -22.031 6.769   29.314  1.00 49.48 ? 178 HIS   D NE2 1 
ATOM   5429 N  N   . HIS   D 1 86  ? -19.855 7.854   25.290  1.00 46.50 ? 179 HIS   D N   1 
ATOM   5430 C  CA  . HIS   D 1 86  ? -20.195 6.609   24.551  1.00 46.53 ? 179 HIS   D CA  1 
ATOM   5431 C  C   . HIS   D 1 86  ? -18.963 6.106   23.792  1.00 47.08 ? 179 HIS   D C   1 
ATOM   5432 O  O   . HIS   D 1 86  ? -18.804 4.879   23.693  1.00 46.06 ? 179 HIS   D O   1 
ATOM   5433 C  CB  . HIS   D 1 86  ? -21.424 6.806   23.650  1.00 44.71 ? 179 HIS   D CB  1 
ATOM   5434 C  CG  . HIS   D 1 86  ? -22.702 6.646   24.402  1.00 44.78 ? 179 HIS   D CG  1 
ATOM   5435 N  ND1 . HIS   D 1 86  ? -23.697 7.610   24.410  1.00 44.06 ? 179 HIS   D ND1 1 
ATOM   5436 C  CD2 . HIS   D 1 86  ? -23.129 5.649   25.207  1.00 44.56 ? 179 HIS   D CD2 1 
ATOM   5437 C  CE1 . HIS   D 1 86  ? -24.674 7.215   25.200  1.00 44.84 ? 179 HIS   D CE1 1 
ATOM   5438 N  NE2 . HIS   D 1 86  ? -24.359 6.002   25.688  1.00 44.36 ? 179 HIS   D NE2 1 
ATOM   5439 N  N   . GLU   D 1 87  ? -18.121 7.017   23.301  1.00 49.24 ? 180 GLU   D N   1 
ATOM   5440 C  CA  . GLU   D 1 87  ? -16.864 6.672   22.587  1.00 50.67 ? 180 GLU   D CA  1 
ATOM   5441 C  C   . GLU   D 1 87  ? -15.972 5.811   23.500  1.00 53.15 ? 180 GLU   D C   1 
ATOM   5442 O  O   . GLU   D 1 87  ? -15.367 4.861   22.969  1.00 53.88 ? 180 GLU   D O   1 
ATOM   5443 C  CB  . GLU   D 1 87  ? -16.180 7.951   22.098  1.00 51.81 ? 180 GLU   D CB  1 
ATOM   5444 C  CG  . GLU   D 1 87  ? -14.847 7.719   21.410  1.00 51.93 ? 180 GLU   D CG  1 
ATOM   5445 C  CD  . GLU   D 1 87  ? -14.051 8.994   21.194  1.00 54.06 ? 180 GLU   D CD  1 
ATOM   5446 O  OE1 . GLU   D 1 87  ? -14.611 10.099  21.445  1.00 54.60 ? 180 GLU   D OE1 1 
ATOM   5447 O  OE2 . GLU   D 1 87  ? -12.881 8.885   20.773  1.00 54.28 ? 180 GLU   D OE2 1 
ATOM   5448 N  N   . ARG   D 1 88  ? -15.945 6.073   24.817  1.00 56.17 ? 181 ARG   D N   1 
ATOM   5449 C  CA  . ARG   D 1 88  ? -15.078 5.369   25.804  1.00 58.79 ? 181 ARG   D CA  1 
ATOM   5450 C  C   . ARG   D 1 88  ? -15.756 4.106   26.373  1.00 58.60 ? 181 ARG   D C   1 
ATOM   5451 O  O   . ARG   D 1 88  ? -15.031 3.314   27.008  1.00 59.08 ? 181 ARG   D O   1 
ATOM   5452 C  CB  . ARG   D 1 88  ? -14.716 6.260   27.003  1.00 62.11 ? 181 ARG   D CB  1 
ATOM   5453 C  CG  . ARG   D 1 88  ? -14.338 7.703   26.689  1.00 63.90 ? 181 ARG   D CG  1 
ATOM   5454 C  CD  . ARG   D 1 88  ? -13.003 7.806   25.989  1.00 65.83 ? 181 ARG   D CD  1 
ATOM   5455 N  NE  . ARG   D 1 88  ? -12.747 9.161   25.507  1.00 67.54 ? 181 ARG   D NE  1 
ATOM   5456 C  CZ  . ARG   D 1 88  ? -11.695 9.538   24.779  1.00 68.59 ? 181 ARG   D CZ  1 
ATOM   5457 N  NH1 . ARG   D 1 88  ? -11.572 10.803  24.407  1.00 69.20 ? 181 ARG   D NH1 1 
ATOM   5458 N  NH2 . ARG   D 1 88  ? -10.773 8.660   24.414  1.00 69.16 ? 181 ARG   D NH2 1 
ATOM   5459 N  N   . CYS   D 1 89  ? -17.073 3.903   26.198  1.00 57.46 ? 182 CYS   D N   1 
ATOM   5460 C  CA  . CYS   D 1 89  ? -17.772 2.666   26.666  1.00 58.21 ? 182 CYS   D CA  1 
ATOM   5461 C  C   . CYS   D 1 89  ? -17.264 1.449   25.872  1.00 58.27 ? 182 CYS   D C   1 
ATOM   5462 O  O   . CYS   D 1 89  ? -17.053 1.592   24.657  1.00 58.19 ? 182 CYS   D O   1 
ATOM   5463 C  CB  . CYS   D 1 89  ? -19.288 2.805   26.562  1.00 57.25 ? 182 CYS   D CB  1 
ATOM   5464 S  SG  . CYS   D 1 89  ? -20.070 3.512   27.986  1.00 58.85 ? 182 CYS   D SG  1 
ATOM   5465 N  N   . SER   D 1 90  ? -17.081 0.312   26.550  1.00 60.11 ? 183 SER   D N   1 
ATOM   5466 C  CA  . SER   D 1 90  ? -16.291 -0.861  26.086  1.00 61.12 ? 183 SER   D CA  1 
ATOM   5467 C  C   . SER   D 1 90  ? -17.014 -1.658  24.991  1.00 61.11 ? 183 SER   D C   1 
ATOM   5468 O  O   . SER   D 1 90  ? -16.330 -2.010  24.013  1.00 61.20 ? 183 SER   D O   1 
ATOM   5469 C  CB  . SER   D 1 90  ? -15.879 -1.743  27.254  1.00 63.28 ? 183 SER   D CB  1 
ATOM   5470 O  OG  . SER   D 1 90  ? -16.999 -2.244  27.974  1.00 63.94 ? 183 SER   D OG  1 
ATOM   5471 N  N   . ASP   D 1 91  ? -18.322 -1.909  25.128  1.00 62.12 ? 184 ASP   D N   1 
ATOM   5472 C  CA  . ASP   D 1 91  ? -19.152 -2.738  24.204  1.00 61.30 ? 184 ASP   D CA  1 
ATOM   5473 C  C   . ASP   D 1 91  ? -18.796 -2.454  22.732  1.00 59.10 ? 184 ASP   D C   1 
ATOM   5474 O  O   . ASP   D 1 91  ? -19.568 -1.778  22.017  1.00 58.82 ? 184 ASP   D O   1 
ATOM   5475 C  CB  . ASP   D 1 91  ? -20.647 -2.542  24.491  1.00 61.86 ? 184 ASP   D CB  1 
ATOM   5476 C  CG  . ASP   D 1 91  ? -21.098 -2.960  25.887  1.00 63.39 ? 184 ASP   D CG  1 
ATOM   5477 O  OD1 . ASP   D 1 91  ? -20.237 -3.032  26.790  1.00 64.30 ? 184 ASP   D OD1 1 
ATOM   5478 O  OD2 . ASP   D 1 91  ? -22.317 -3.197  26.070  1.00 63.91 ? 184 ASP   D OD2 1 
ATOM   5479 N  N   . SER   D 1 92  ? -17.675 -3.018  22.275  1.00 58.81 ? 185 SER   D N   1 
ATOM   5480 C  CA  . SER   D 1 92  ? -17.089 -2.858  20.916  1.00 57.61 ? 185 SER   D CA  1 
ATOM   5481 C  C   . SER   D 1 92  ? -16.995 -4.231  20.237  1.00 56.31 ? 185 SER   D C   1 
ATOM   5482 O  O   . SER   D 1 92  ? -16.638 -5.201  20.941  1.00 57.57 ? 185 SER   D O   1 
ATOM   5483 C  CB  . SER   D 1 92  ? -15.731 -2.189  20.995  1.00 58.78 ? 185 SER   D CB  1 
ATOM   5484 O  OG  . SER   D 1 92  ? -14.861 -2.887  21.888  1.00 61.98 ? 185 SER   D OG  1 
ATOM   5485 N  N   . ASP   D 1 93  ? -17.280 -4.304  18.930  1.00 53.61 ? 186 ASP   D N   1 
ATOM   5486 C  CA  . ASP   D 1 93  ? -17.377 -5.581  18.178  1.00 52.29 ? 186 ASP   D CA  1 
ATOM   5487 C  C   . ASP   D 1 93  ? -16.046 -5.893  17.480  1.00 51.11 ? 186 ASP   D C   1 
ATOM   5488 O  O   . ASP   D 1 93  ? -16.018 -6.880  16.730  1.00 53.55 ? 186 ASP   D O   1 
ATOM   5489 C  CB  . ASP   D 1 93  ? -18.540 -5.530  17.184  1.00 51.67 ? 186 ASP   D CB  1 
ATOM   5490 C  CG  . ASP   D 1 93  ? -18.346 -4.572  16.018  1.00 50.48 ? 186 ASP   D CG  1 
ATOM   5491 O  OD1 . ASP   D 1 93  ? -17.388 -3.736  16.060  1.00 49.48 ? 186 ASP   D OD1 1 
ATOM   5492 O  OD2 . ASP   D 1 93  ? -19.127 -4.682  15.054  1.00 50.35 ? 186 ASP   D OD2 1 
ATOM   5493 N  N   . GLY   D 1 94  ? -15.001 -5.082  17.695  1.00 48.42 ? 187 GLY   D N   1 
ATOM   5494 C  CA  . GLY   D 1 94  ? -13.660 -5.255  17.111  1.00 47.16 ? 187 GLY   D CA  1 
ATOM   5495 C  C   . GLY   D 1 94  ? -13.537 -4.696  15.703  1.00 44.52 ? 187 GLY   D C   1 
ATOM   5496 O  O   . GLY   D 1 94  ? -12.422 -4.708  15.167  1.00 45.68 ? 187 GLY   D O   1 
ATOM   5497 N  N   . LEU   D 1 95  ? -14.631 -4.244  15.089  1.00 41.75 ? 188 LEU   D N   1 
ATOM   5498 C  CA  . LEU   D 1 95  ? -14.629 -3.810  13.668  1.00 40.05 ? 188 LEU   D CA  1 
ATOM   5499 C  C   . LEU   D 1 95  ? -14.886 -2.300  13.579  1.00 39.01 ? 188 LEU   D C   1 
ATOM   5500 O  O   . LEU   D 1 95  ? -14.184 -1.659  12.797  1.00 39.38 ? 188 LEU   D O   1 
ATOM   5501 C  CB  . LEU   D 1 95  ? -15.672 -4.615  12.892  1.00 39.13 ? 188 LEU   D CB  1 
ATOM   5502 C  CG  . LEU   D 1 95  ? -15.501 -6.134  12.927  1.00 39.45 ? 188 LEU   D CG  1 
ATOM   5503 C  CD1 . LEU   D 1 95  ? -16.720 -6.819  12.311  1.00 39.30 ? 188 LEU   D CD1 1 
ATOM   5504 C  CD2 . LEU   D 1 95  ? -14.221 -6.551  12.218  1.00 39.64 ? 188 LEU   D CD2 1 
ATOM   5505 N  N   . ALA   D 1 96  ? -15.838 -1.759  14.345  1.00 38.31 ? 189 ALA   D N   1 
ATOM   5506 C  CA  . ALA   D 1 96  ? -16.325 -0.359  14.211  1.00 36.71 ? 189 ALA   D CA  1 
ATOM   5507 C  C   . ALA   D 1 96  ? -15.395 0.592   14.957  1.00 36.33 ? 189 ALA   D C   1 
ATOM   5508 O  O   . ALA   D 1 96  ? -14.994 0.319   16.079  1.00 36.47 ? 189 ALA   D O   1 
ATOM   5509 C  CB  . ALA   D 1 96  ? -17.741 -0.247  14.722  1.00 37.14 ? 189 ALA   D CB  1 
ATOM   5510 N  N   . PRO   D 1 97  ? -15.011 1.745   14.368  1.00 35.77 ? 190 PRO   D N   1 
ATOM   5511 C  CA  . PRO   D 1 97  ? -14.265 2.753   15.112  1.00 35.75 ? 190 PRO   D CA  1 
ATOM   5512 C  C   . PRO   D 1 97  ? -15.135 3.212   16.276  1.00 35.89 ? 190 PRO   D C   1 
ATOM   5513 O  O   . PRO   D 1 97  ? -16.355 3.305   16.143  1.00 35.54 ? 190 PRO   D O   1 
ATOM   5514 C  CB  . PRO   D 1 97  ? -14.000 3.879   14.106  1.00 34.96 ? 190 PRO   D CB  1 
ATOM   5515 C  CG  . PRO   D 1 97  ? -14.200 3.224   12.759  1.00 34.46 ? 190 PRO   D CG  1 
ATOM   5516 C  CD  . PRO   D 1 97  ? -15.258 2.153   12.975  1.00 34.09 ? 190 PRO   D CD  1 
ATOM   5517 N  N   . PRO   D 1 98  ? -14.531 3.510   17.446  1.00 37.51 ? 191 PRO   D N   1 
ATOM   5518 C  CA  . PRO   D 1 98  ? -15.304 3.897   18.625  1.00 38.15 ? 191 PRO   D CA  1 
ATOM   5519 C  C   . PRO   D 1 98  ? -16.102 5.205   18.450  1.00 38.15 ? 191 PRO   D C   1 
ATOM   5520 O  O   . PRO   D 1 98  ? -17.043 5.387   19.164  1.00 38.20 ? 191 PRO   D O   1 
ATOM   5521 C  CB  . PRO   D 1 98  ? -14.249 3.985   19.737  1.00 39.19 ? 191 PRO   D CB  1 
ATOM   5522 C  CG  . PRO   D 1 98  ? -12.925 4.170   19.026  1.00 39.97 ? 191 PRO   D CG  1 
ATOM   5523 C  CD  . PRO   D 1 98  ? -13.081 3.466   17.695  1.00 38.86 ? 191 PRO   D CD  1 
ATOM   5524 N  N   . GLN   D 1 99  ? -15.708 6.060   17.502  1.00 38.65 ? 192 GLN   D N   1 
ATOM   5525 C  CA  . GLN   D 1 99  ? -16.286 7.409   17.246  1.00 38.67 ? 192 GLN   D CA  1 
ATOM   5526 C  C   . GLN   D 1 99  ? -17.559 7.319   16.389  1.00 37.00 ? 192 GLN   D C   1 
ATOM   5527 O  O   . GLN   D 1 99  ? -18.353 8.299   16.413  1.00 37.81 ? 192 GLN   D O   1 
ATOM   5528 C  CB  . GLN   D 1 99  ? -15.271 8.292   16.521  1.00 39.76 ? 192 GLN   D CB  1 
ATOM   5529 C  CG  . GLN   D 1 99  ? -14.093 8.688   17.385  1.00 42.42 ? 192 GLN   D CG  1 
ATOM   5530 C  CD  . GLN   D 1 99  ? -13.195 9.700   16.723  1.00 43.46 ? 192 GLN   D CD  1 
ATOM   5531 O  OE1 . GLN   D 1 99  ? -13.459 10.203  15.635  1.00 44.11 ? 192 GLN   D OE1 1 
ATOM   5532 N  NE2 . GLN   D 1 99  ? -12.117 10.032  17.403  1.00 45.08 ? 192 GLN   D NE2 1 
ATOM   5533 N  N   . HIS   D 1 100 ? -17.751 6.219   15.648  1.00 34.63 ? 193 HIS   D N   1 
ATOM   5534 C  CA  . HIS   D 1 100 ? -18.804 6.074   14.609  1.00 32.92 ? 193 HIS   D CA  1 
ATOM   5535 C  C   . HIS   D 1 100 ? -20.180 5.917   15.256  1.00 32.29 ? 193 HIS   D C   1 
ATOM   5536 O  O   . HIS   D 1 100 ? -20.364 4.991   16.063  1.00 32.79 ? 193 HIS   D O   1 
ATOM   5537 C  CB  . HIS   D 1 100 ? -18.488 4.917   13.647  1.00 31.67 ? 193 HIS   D CB  1 
ATOM   5538 C  CG  . HIS   D 1 100 ? -17.513 5.296   12.586  1.00 31.71 ? 193 HIS   D CG  1 
ATOM   5539 N  ND1 . HIS   D 1 100 ? -17.721 5.015   11.256  1.00 31.20 ? 193 HIS   D ND1 1 
ATOM   5540 C  CD2 . HIS   D 1 100 ? -16.353 5.981   12.650  1.00 32.56 ? 193 HIS   D CD2 1 
ATOM   5541 C  CE1 . HIS   D 1 100 ? -16.721 5.495   10.547  1.00 31.33 ? 193 HIS   D CE1 1 
ATOM   5542 N  NE2 . HIS   D 1 100 ? -15.874 6.098   11.376  1.00 32.82 ? 193 HIS   D NE2 1 
ATOM   5543 N  N   . LEU   D 1 101 ? -21.124 6.775   14.870  1.00 31.37 ? 194 LEU   D N   1 
ATOM   5544 C  CA  . LEU   D 1 101 ? -22.524 6.696   15.349  1.00 30.77 ? 194 LEU   D CA  1 
ATOM   5545 C  C   . LEU   D 1 101 ? -23.187 5.437   14.788  1.00 29.64 ? 194 LEU   D C   1 
ATOM   5546 O  O   . LEU   D 1 101 ? -23.881 4.785   15.578  1.00 28.86 ? 194 LEU   D O   1 
ATOM   5547 C  CB  . LEU   D 1 101 ? -23.317 7.933   14.944  1.00 30.80 ? 194 LEU   D CB  1 
ATOM   5548 C  CG  . LEU   D 1 101 ? -24.811 7.836   15.242  1.00 30.80 ? 194 LEU   D CG  1 
ATOM   5549 C  CD1 . LEU   D 1 101 ? -25.064 7.768   16.735  1.00 31.45 ? 194 LEU   D CD1 1 
ATOM   5550 C  CD2 . LEU   D 1 101 ? -25.580 8.985   14.641  1.00 30.56 ? 194 LEU   D CD2 1 
ATOM   5551 N  N   . ILE   D 1 102 ? -22.983 5.133   13.499  1.00 28.74 ? 195 ILE   D N   1 
ATOM   5552 C  CA  . ILE   D 1 102 ? -23.750 4.079   12.773  1.00 28.61 ? 195 ILE   D CA  1 
ATOM   5553 C  C   . ILE   D 1 102 ? -22.869 2.852   12.585  1.00 28.61 ? 195 ILE   D C   1 
ATOM   5554 O  O   . ILE   D 1 102 ? -21.789 2.974   11.957  1.00 29.06 ? 195 ILE   D O   1 
ATOM   5555 C  CB  . ILE   D 1 102 ? -24.299 4.572   11.418  1.00 27.96 ? 195 ILE   D CB  1 
ATOM   5556 C  CG1 . ILE   D 1 102 ? -25.010 5.924   11.548  1.00 28.64 ? 195 ILE   D CG1 1 
ATOM   5557 C  CG2 . ILE   D 1 102 ? -25.218 3.521   10.805  1.00 27.64 ? 195 ILE   D CG2 1 
ATOM   5558 C  CD1 . ILE   D 1 102 ? -25.854 6.297   10.354  1.00 28.07 ? 195 ILE   D CD1 1 
ATOM   5559 N  N   . ARG   D 1 103 ? -23.326 1.713   13.090  1.00 29.16 ? 196 ARG   D N   1 
ATOM   5560 C  CA  . ARG   D 1 103 ? -22.667 0.407   12.869  1.00 29.44 ? 196 ARG   D CA  1 
ATOM   5561 C  C   . ARG   D 1 103 ? -23.591 -0.491  12.042  1.00 29.73 ? 196 ARG   D C   1 
ATOM   5562 O  O   . ARG   D 1 103 ? -24.809 -0.238  12.035  1.00 29.90 ? 196 ARG   D O   1 
ATOM   5563 C  CB  . ARG   D 1 103 ? -22.359 -0.250  14.209  1.00 30.43 ? 196 ARG   D CB  1 
ATOM   5564 C  CG  . ARG   D 1 103 ? -21.434 0.566   15.102  1.00 30.93 ? 196 ARG   D CG  1 
ATOM   5565 C  CD  . ARG   D 1 103 ? -20.891 -0.348  16.169  1.00 31.84 ? 196 ARG   D CD  1 
ATOM   5566 N  NE  . ARG   D 1 103 ? -20.154 0.381   17.186  1.00 32.83 ? 196 ARG   D NE  1 
ATOM   5567 C  CZ  . ARG   D 1 103 ? -19.874 -0.089  18.393  1.00 33.44 ? 196 ARG   D CZ  1 
ATOM   5568 N  NH1 . ARG   D 1 103 ? -20.251 -1.309  18.739  1.00 34.51 ? 196 ARG   D NH1 1 
ATOM   5569 N  NH2 . ARG   D 1 103 ? -19.193 0.659   19.234  1.00 33.98 ? 196 ARG   D NH2 1 
ATOM   5570 N  N   . VAL   D 1 104 ? -23.035 -1.522  11.401  1.00 29.83 ? 197 VAL   D N   1 
ATOM   5571 C  CA  . VAL   D 1 104 ? -23.823 -2.651  10.840  1.00 30.13 ? 197 VAL   D CA  1 
ATOM   5572 C  C   . VAL   D 1 104 ? -23.492 -3.873  11.690  1.00 31.02 ? 197 VAL   D C   1 
ATOM   5573 O  O   . VAL   D 1 104 ? -22.306 -4.073  12.002  1.00 30.75 ? 197 VAL   D O   1 
ATOM   5574 C  CB  . VAL   D 1 104 ? -23.544 -2.882  9.337   1.00 29.69 ? 197 VAL   D CB  1 
ATOM   5575 C  CG1 . VAL   D 1 104 ? -24.184 -4.163  8.830   1.00 30.58 ? 197 VAL   D CG1 1 
ATOM   5576 C  CG2 . VAL   D 1 104 ? -23.989 -1.710  8.496   1.00 28.98 ? 197 VAL   D CG2 1 
ATOM   5577 N  N   . GLU   D 1 105 ? -24.519 -4.623  12.092  1.00 32.55 ? 198 GLU   D N   1 
ATOM   5578 C  CA  . GLU   D 1 105 ? -24.374 -5.839  12.927  1.00 34.17 ? 198 GLU   D CA  1 
ATOM   5579 C  C   . GLU   D 1 105 ? -24.574 -7.058  12.021  1.00 34.34 ? 198 GLU   D C   1 
ATOM   5580 O  O   . GLU   D 1 105 ? -25.281 -6.926  11.003  1.00 33.60 ? 198 GLU   D O   1 
ATOM   5581 C  CB  . GLU   D 1 105 ? -25.326 -5.768  14.127  1.00 35.54 ? 198 GLU   D CB  1 
ATOM   5582 C  CG  . GLU   D 1 105 ? -26.556 -6.655  14.040  1.00 36.76 ? 198 GLU   D CG  1 
ATOM   5583 C  CD  . GLU   D 1 105 ? -27.530 -6.522  15.197  1.00 38.44 ? 198 GLU   D CD  1 
ATOM   5584 O  OE1 . GLU   D 1 105 ? -27.806 -7.549  15.844  1.00 41.56 ? 198 GLU   D OE1 1 
ATOM   5585 O  OE2 . GLU   D 1 105 ? -28.007 -5.405  15.459  1.00 38.58 ? 198 GLU   D OE2 1 
ATOM   5586 N  N   . GLY   D 1 106 ? -23.973 -8.195  12.396  1.00 35.37 ? 199 GLY   D N   1 
ATOM   5587 C  CA  . GLY   D 1 106 ? -24.151 -9.496  11.725  1.00 35.64 ? 199 GLY   D CA  1 
ATOM   5588 C  C   . GLY   D 1 106 ? -23.552 -9.541  10.325  1.00 35.64 ? 199 GLY   D C   1 
ATOM   5589 O  O   . GLY   D 1 106 ? -24.025 -10.366 9.507   1.00 36.55 ? 199 GLY   D O   1 
ATOM   5590 N  N   . ASN   D 1 107 ? -22.532 -8.725  10.042  1.00 34.13 ? 200 ASN   D N   1 
ATOM   5591 C  CA  . ASN   D 1 107 ? -21.902 -8.676  8.700   1.00 33.63 ? 200 ASN   D CA  1 
ATOM   5592 C  C   . ASN   D 1 107 ? -20.383 -8.550  8.844   1.00 33.45 ? 200 ASN   D C   1 
ATOM   5593 O  O   . ASN   D 1 107 ? -19.870 -7.458  9.094   1.00 32.15 ? 200 ASN   D O   1 
ATOM   5594 C  CB  . ASN   D 1 107 ? -22.531 -7.610  7.798   1.00 32.43 ? 200 ASN   D CB  1 
ATOM   5595 C  CG  . ASN   D 1 107 ? -22.249 -7.895  6.340   1.00 32.85 ? 200 ASN   D CG  1 
ATOM   5596 O  OD1 . ASN   D 1 107 ? -21.168 -8.381  6.011   1.00 33.02 ? 200 ASN   D OD1 1 
ATOM   5597 N  ND2 . ASN   D 1 107 ? -23.193 -7.592  5.460   1.00 32.43 ? 200 ASN   D ND2 1 
ATOM   5598 N  N   . LEU   D 1 108 ? -19.674 -9.651  8.621   1.00 34.58 ? 201 LEU   D N   1 
ATOM   5599 C  CA  . LEU   D 1 108 ? -18.203 -9.706  8.799   1.00 35.11 ? 201 LEU   D CA  1 
ATOM   5600 C  C   . LEU   D 1 108 ? -17.508 -9.016  7.623   1.00 34.25 ? 201 LEU   D C   1 
ATOM   5601 O  O   . LEU   D 1 108 ? -16.299 -8.851  7.733   1.00 34.24 ? 201 LEU   D O   1 
ATOM   5602 C  CB  . LEU   D 1 108 ? -17.734 -11.160 8.936   1.00 36.89 ? 201 LEU   D CB  1 
ATOM   5603 C  CG  . LEU   D 1 108 ? -18.600 -12.041 9.832   1.00 38.24 ? 201 LEU   D CG  1 
ATOM   5604 C  CD1 . LEU   D 1 108 ? -19.563 -12.856 8.982   1.00 39.38 ? 201 LEU   D CD1 1 
ATOM   5605 C  CD2 . LEU   D 1 108 ? -17.764 -12.962 10.723  1.00 40.20 ? 201 LEU   D CD2 1 
ATOM   5606 N  N   . ARG   D 1 109 ? -18.229 -8.603  6.574   1.00 33.48 ? 202 ARG   D N   1 
ATOM   5607 C  CA  . ARG   D 1 109 ? -17.650 -7.904  5.391   1.00 33.71 ? 202 ARG   D CA  1 
ATOM   5608 C  C   . ARG   D 1 109 ? -17.848 -6.384  5.517   1.00 31.93 ? 202 ARG   D C   1 
ATOM   5609 O  O   . ARG   D 1 109 ? -17.478 -5.679  4.596   1.00 32.09 ? 202 ARG   D O   1 
ATOM   5610 C  CB  . ARG   D 1 109 ? -18.276 -8.420  4.091   1.00 34.48 ? 202 ARG   D CB  1 
ATOM   5611 C  CG  . ARG   D 1 109 ? -18.047 -9.903  3.841   1.00 36.55 ? 202 ARG   D CG  1 
ATOM   5612 C  CD  . ARG   D 1 109 ? -18.956 -10.401 2.728   1.00 37.80 ? 202 ARG   D CD  1 
ATOM   5613 N  NE  . ARG   D 1 109 ? -18.497 -9.895  1.440   1.00 38.60 ? 202 ARG   D NE  1 
ATOM   5614 C  CZ  . ARG   D 1 109 ? -19.155 -10.020 0.286   1.00 39.78 ? 202 ARG   D CZ  1 
ATOM   5615 N  NH1 . ARG   D 1 109 ? -20.342 -10.618 0.247   1.00 40.08 ? 202 ARG   D NH1 1 
ATOM   5616 N  NH2 . ARG   D 1 109 ? -18.617 -9.529  -0.820  1.00 39.94 ? 202 ARG   D NH2 1 
ATOM   5617 N  N   . VAL   D 1 110 ? -18.378 -5.915  6.639   1.00 31.04 ? 203 VAL   D N   1 
ATOM   5618 C  CA  . VAL   D 1 110 ? -18.604 -4.467  6.931   1.00 29.52 ? 203 VAL   D CA  1 
ATOM   5619 C  C   . VAL   D 1 110 ? -17.265 -3.718  6.874   1.00 29.32 ? 203 VAL   D C   1 
ATOM   5620 O  O   . VAL   D 1 110 ? -16.242 -4.265  7.305   1.00 29.78 ? 203 VAL   D O   1 
ATOM   5621 C  CB  . VAL   D 1 110 ? -19.317 -4.250  8.283   1.00 29.11 ? 203 VAL   D CB  1 
ATOM   5622 C  CG1 . VAL   D 1 110 ? -18.511 -4.742  9.475   1.00 29.91 ? 203 VAL   D CG1 1 
ATOM   5623 C  CG2 . VAL   D 1 110 ? -19.682 -2.783  8.467   1.00 28.51 ? 203 VAL   D CG2 1 
ATOM   5624 N  N   . GLU   D 1 111 ? -17.289 -2.486  6.356   1.00 28.78 ? 204 GLU   D N   1 
ATOM   5625 C  CA  . GLU   D 1 111 ? -16.089 -1.637  6.182   1.00 29.04 ? 204 GLU   D CA  1 
ATOM   5626 C  C   . GLU   D 1 111 ? -16.453 -0.231  6.667   1.00 28.33 ? 204 GLU   D C   1 
ATOM   5627 O  O   . GLU   D 1 111 ? -17.589 0.195   6.420   1.00 27.33 ? 204 GLU   D O   1 
ATOM   5628 C  CB  . GLU   D 1 111 ? -15.636 -1.720  4.717   1.00 29.86 ? 204 GLU   D CB  1 
ATOM   5629 C  CG  . GLU   D 1 111 ? -14.760 -0.572  4.244   1.00 30.23 ? 204 GLU   D CG  1 
ATOM   5630 C  CD  . GLU   D 1 111 ? -14.526 -0.539  2.739   1.00 31.00 ? 204 GLU   D CD  1 
ATOM   5631 O  OE1 . GLU   D 1 111 ? -14.355 -1.617  2.148   1.00 32.05 ? 204 GLU   D OE1 1 
ATOM   5632 O  OE2 . GLU   D 1 111 ? -14.508 0.570   2.164   1.00 30.75 ? 204 GLU   D OE2 1 
ATOM   5633 N  N   . TYR   D 1 112 ? -15.546 0.421   7.405   1.00 28.44 ? 205 TYR   D N   1 
ATOM   5634 C  CA  . TYR   D 1 112 ? -15.771 1.753   8.015   1.00 28.28 ? 205 TYR   D CA  1 
ATOM   5635 C  C   . TYR   D 1 112 ? -14.794 2.748   7.383   1.00 28.99 ? 205 TYR   D C   1 
ATOM   5636 O  O   . TYR   D 1 112 ? -13.627 2.400   7.110   1.00 29.97 ? 205 TYR   D O   1 
ATOM   5637 C  CB  . TYR   D 1 112 ? -15.668 1.670   9.544   1.00 28.38 ? 205 TYR   D CB  1 
ATOM   5638 C  CG  . TYR   D 1 112 ? -16.790 0.908   10.207  1.00 28.07 ? 205 TYR   D CG  1 
ATOM   5639 C  CD1 . TYR   D 1 112 ? -17.968 1.529   10.572  1.00 27.73 ? 205 TYR   D CD1 1 
ATOM   5640 C  CD2 . TYR   D 1 112 ? -16.660 -0.440  10.494  1.00 28.82 ? 205 TYR   D CD2 1 
ATOM   5641 C  CE1 . TYR   D 1 112 ? -18.992 0.840   11.199  1.00 27.81 ? 205 TYR   D CE1 1 
ATOM   5642 C  CE2 . TYR   D 1 112 ? -17.689 -1.158  11.081  1.00 28.60 ? 205 TYR   D CE2 1 
ATOM   5643 C  CZ  . TYR   D 1 112 ? -18.862 -0.518  11.426  1.00 28.18 ? 205 TYR   D CZ  1 
ATOM   5644 O  OH  . TYR   D 1 112 ? -19.879 -1.203  12.012  1.00 28.14 ? 205 TYR   D OH  1 
ATOM   5645 N  N   . LEU   D 1 113 ? -15.257 3.976   7.156   1.00 29.25 ? 206 LEU   D N   1 
ATOM   5646 C  CA  . LEU   D 1 113 ? -14.459 5.040   6.509   1.00 29.86 ? 206 LEU   D CA  1 
ATOM   5647 C  C   . LEU   D 1 113 ? -14.483 6.283   7.400   1.00 30.03 ? 206 LEU   D C   1 
ATOM   5648 O  O   . LEU   D 1 113 ? -15.576 6.698   7.815   1.00 29.65 ? 206 LEU   D O   1 
ATOM   5649 C  CB  . LEU   D 1 113 ? -15.022 5.333   5.117   1.00 30.17 ? 206 LEU   D CB  1 
ATOM   5650 C  CG  . LEU   D 1 113 ? -14.431 6.540   4.386   1.00 30.90 ? 206 LEU   D CG  1 
ATOM   5651 C  CD1 . LEU   D 1 113 ? -12.949 6.335   4.139   1.00 32.00 ? 206 LEU   D CD1 1 
ATOM   5652 C  CD2 . LEU   D 1 113 ? -15.145 6.763   3.046   1.00 30.96 ? 206 LEU   D CD2 1 
ATOM   5653 N  N   . ASP   D 1 114 ? -13.296 6.777   7.740   1.00 30.74 ? 207 ASP   D N   1 
ATOM   5654 C  CA  . ASP   D 1 114 ? -13.043 8.186   8.138   1.00 32.21 ? 207 ASP   D CA  1 
ATOM   5655 C  C   . ASP   D 1 114 ? -12.553 8.882   6.869   1.00 32.97 ? 207 ASP   D C   1 
ATOM   5656 O  O   . ASP   D 1 114 ? -11.441 8.548   6.409   1.00 34.49 ? 207 ASP   D O   1 
ATOM   5657 C  CB  . ASP   D 1 114 ? -11.997 8.275   9.247   1.00 32.32 ? 207 ASP   D CB  1 
ATOM   5658 C  CG  . ASP   D 1 114 ? -12.441 7.732   10.588  1.00 32.35 ? 207 ASP   D CG  1 
ATOM   5659 O  OD1 . ASP   D 1 114 ? -13.618 7.330   10.727  1.00 32.22 ? 207 ASP   D OD1 1 
ATOM   5660 O  OD2 . ASP   D 1 114 ? -11.601 7.711   11.488  1.00 32.66 ? 207 ASP   D OD2 1 
ATOM   5661 N  N   . ASP   D 1 115 ? -13.387 9.717   6.262   1.00 33.50 ? 208 ASP   D N   1 
ATOM   5662 C  CA  . ASP   D 1 115 ? -13.061 10.397  4.983   1.00 34.80 ? 208 ASP   D CA  1 
ATOM   5663 C  C   . ASP   D 1 115 ? -11.866 11.307  5.259   1.00 36.48 ? 208 ASP   D C   1 
ATOM   5664 O  O   . ASP   D 1 115 ? -11.946 12.119  6.216   1.00 36.85 ? 208 ASP   D O   1 
ATOM   5665 C  CB  . ASP   D 1 115 ? -14.272 11.146  4.411   1.00 34.79 ? 208 ASP   D CB  1 
ATOM   5666 C  CG  . ASP   D 1 115 ? -14.011 11.737  3.031   1.00 35.39 ? 208 ASP   D CG  1 
ATOM   5667 O  OD1 . ASP   D 1 115 ? -13.170 12.654  2.925   1.00 36.43 ? 208 ASP   D OD1 1 
ATOM   5668 O  OD2 . ASP   D 1 115 ? -14.636 11.274  2.071   1.00 34.96 ? 208 ASP   D OD2 1 
ATOM   5669 N  N   . ARG   D 1 116 ? -10.792 11.166  4.474   1.00 37.77 ? 209 ARG   D N   1 
ATOM   5670 C  CA  . ARG   D 1 116 ? -9.521  11.879  4.717   1.00 40.16 ? 209 ARG   D CA  1 
ATOM   5671 C  C   . ARG   D 1 116 ? -9.736  13.398  4.639   1.00 41.11 ? 209 ARG   D C   1 
ATOM   5672 O  O   . ARG   D 1 116 ? -8.971  14.114  5.311   1.00 42.65 ? 209 ARG   D O   1 
ATOM   5673 C  CB  . ARG   D 1 116 ? -8.431  11.421  3.744   1.00 41.11 ? 209 ARG   D CB  1 
ATOM   5674 C  CG  . ARG   D 1 116 ? -7.213  12.322  3.769   0.70 42.92 ? 209 ARG   D CG  1 
ATOM   5675 C  CD  . ARG   D 1 116 ? -6.506  12.261  5.111   0.70 43.87 ? 209 ARG   D CD  1 
ATOM   5676 N  NE  . ARG   D 1 116 ? -5.499  11.219  5.071   0.70 44.30 ? 209 ARG   D NE  1 
ATOM   5677 C  CZ  . ARG   D 1 116 ? -4.405  11.260  4.316   0.70 45.42 ? 209 ARG   D CZ  1 
ATOM   5678 N  NH1 . ARG   D 1 116 ? -4.165  12.305  3.538   0.70 46.60 ? 209 ARG   D NH1 1 
ATOM   5679 N  NH2 . ARG   D 1 116 ? -3.542  10.259  4.350   0.70 45.42 ? 209 ARG   D NH2 1 
ATOM   5680 N  N   . ASN   D 1 117 ? -10.718 13.880  3.864   1.00 40.89 ? 210 ASN   D N   1 
ATOM   5681 C  CA  . ASN   D 1 117 ? -10.865 15.330  3.543   1.00 42.19 ? 210 ASN   D CA  1 
ATOM   5682 C  C   . ASN   D 1 117 ? -12.093 15.948  4.227   1.00 41.76 ? 210 ASN   D C   1 
ATOM   5683 O  O   . ASN   D 1 117 ? -11.969 17.100  4.658   1.00 42.97 ? 210 ASN   D O   1 
ATOM   5684 C  CB  . ASN   D 1 117 ? -10.856 15.552  2.029   1.00 42.34 ? 210 ASN   D CB  1 
ATOM   5685 C  CG  . ASN   D 1 117 ? -9.565  15.023  1.437   1.00 42.95 ? 210 ASN   D CG  1 
ATOM   5686 O  OD1 . ASN   D 1 117 ? -9.554  14.095  0.631   1.00 42.56 ? 210 ASN   D OD1 1 
ATOM   5687 N  ND2 . ASN   D 1 117 ? -8.450  15.523  1.933   1.00 43.94 ? 210 ASN   D ND2 1 
ATOM   5688 N  N   . THR   D 1 118 ? -13.229 15.251  4.297   1.00 40.30 ? 211 THR   D N   1 
ATOM   5689 C  CA  . THR   D 1 118 ? -14.470 15.770  4.942   1.00 40.05 ? 211 THR   D CA  1 
ATOM   5690 C  C   . THR   D 1 118 ? -14.495 15.397  6.426   1.00 39.44 ? 211 THR   D C   1 
ATOM   5691 O  O   . THR   D 1 118 ? -15.287 16.017  7.165   1.00 38.84 ? 211 THR   D O   1 
ATOM   5692 C  CB  . THR   D 1 118 ? -15.750 15.265  4.271   1.00 39.32 ? 211 THR   D CB  1 
ATOM   5693 O  OG1 . THR   D 1 118 ? -15.824 13.850  4.448   1.00 38.03 ? 211 THR   D OG1 1 
ATOM   5694 C  CG2 . THR   D 1 118 ? -15.817 15.617  2.800   1.00 40.25 ? 211 THR   D CG2 1 
ATOM   5695 N  N   . PHE   D 1 119 ? -13.730 14.375  6.830   1.00 37.86 ? 212 PHE   D N   1 
ATOM   5696 C  CA  . PHE   D 1 119 ? -13.686 13.849  8.221   1.00 36.90 ? 212 PHE   D CA  1 
ATOM   5697 C  C   . PHE   D 1 119 ? -15.027 13.197  8.583   1.00 34.86 ? 212 PHE   D C   1 
ATOM   5698 O  O   . PHE   D 1 119 ? -15.200 12.816  9.751   1.00 34.11 ? 212 PHE   D O   1 
ATOM   5699 C  CB  . PHE   D 1 119 ? -13.327 14.952  9.227   1.00 38.26 ? 212 PHE   D CB  1 
ATOM   5700 C  CG  . PHE   D 1 119 ? -12.069 15.711  8.887   1.00 40.54 ? 212 PHE   D CG  1 
ATOM   5701 C  CD1 . PHE   D 1 119 ? -10.830 15.100  9.011   1.00 41.05 ? 212 PHE   D CD1 1 
ATOM   5702 C  CD2 . PHE   D 1 119 ? -12.114 17.029  8.460   1.00 42.05 ? 212 PHE   D CD2 1 
ATOM   5703 C  CE1 . PHE   D 1 119 ? -9.664  15.783  8.705   1.00 42.66 ? 212 PHE   D CE1 1 
ATOM   5704 C  CE2 . PHE   D 1 119 ? -10.947 17.706  8.144   1.00 43.63 ? 212 PHE   D CE2 1 
ATOM   5705 C  CZ  . PHE   D 1 119 ? -9.727  17.086  8.267   1.00 44.08 ? 212 PHE   D CZ  1 
ATOM   5706 N  N   . ARG   D 1 120 ? -15.933 13.052  7.617   1.00 33.87 ? 213 ARG   D N   1 
ATOM   5707 C  CA  . ARG   D 1 120 ? -17.245 12.407  7.840   1.00 32.59 ? 213 ARG   D CA  1 
ATOM   5708 C  C   . ARG   D 1 120 ? -17.038 10.894  7.952   1.00 31.12 ? 213 ARG   D C   1 
ATOM   5709 O  O   . ARG   D 1 120 ? -16.115 10.355  7.322   1.00 30.66 ? 213 ARG   D O   1 
ATOM   5710 C  CB  . ARG   D 1 120 ? -18.235 12.796  6.735   1.00 33.03 ? 213 ARG   D CB  1 
ATOM   5711 C  CG  . ARG   D 1 120 ? -18.559 14.287  6.745   1.00 34.33 ? 213 ARG   D CG  1 
ATOM   5712 C  CD  . ARG   D 1 120 ? -19.747 14.632  5.884   1.00 34.61 ? 213 ARG   D CD  1 
ATOM   5713 N  NE  . ARG   D 1 120 ? -20.068 16.051  5.985   1.00 36.50 ? 213 ARG   D NE  1 
ATOM   5714 C  CZ  . ARG   D 1 120 ? -20.883 16.606  6.876   1.00 36.48 ? 213 ARG   D CZ  1 
ATOM   5715 N  NH1 . ARG   D 1 120 ? -21.468 15.886  7.819   1.00 36.06 ? 213 ARG   D NH1 1 
ATOM   5716 N  NH2 . ARG   D 1 120 ? -21.080 17.908  6.843   1.00 37.97 ? 213 ARG   D NH2 1 
ATOM   5717 N  N   . HIS   D 1 121 ? -17.864 10.260  8.779   1.00 30.67 ? 214 HIS   D N   1 
ATOM   5718 C  CA  . HIS   D 1 121 ? -17.868 8.801   9.052   1.00 29.68 ? 214 HIS   D CA  1 
ATOM   5719 C  C   . HIS   D 1 121 ? -18.917 8.118   8.183   1.00 28.82 ? 214 HIS   D C   1 
ATOM   5720 O  O   . HIS   D 1 121 ? -20.017 8.676   7.998   1.00 30.00 ? 214 HIS   D O   1 
ATOM   5721 C  CB  . HIS   D 1 121 ? -18.174 8.554   10.529  1.00 29.62 ? 214 HIS   D CB  1 
ATOM   5722 C  CG  . HIS   D 1 121 ? -17.209 9.181   11.468  1.00 30.17 ? 214 HIS   D CG  1 
ATOM   5723 N  ND1 . HIS   D 1 121 ? -17.510 9.381   12.797  1.00 30.19 ? 214 HIS   D ND1 1 
ATOM   5724 C  CD2 . HIS   D 1 121 ? -15.944 9.628   11.298  1.00 31.34 ? 214 HIS   D CD2 1 
ATOM   5725 C  CE1 . HIS   D 1 121 ? -16.457 9.893   13.398  1.00 31.06 ? 214 HIS   D CE1 1 
ATOM   5726 N  NE2 . HIS   D 1 121 ? -15.500 10.067  12.514  1.00 31.54 ? 214 HIS   D NE2 1 
ATOM   5727 N  N   . SER   D 1 122 ? -18.639 6.902   7.725   1.00 28.41 ? 215 SER   D N   1 
ATOM   5728 C  CA  . SER   D 1 122 ? -19.670 6.074   7.071   1.00 26.88 ? 215 SER   D CA  1 
ATOM   5729 C  C   . SER   D 1 122 ? -19.318 4.592   7.225   1.00 26.60 ? 215 SER   D C   1 
ATOM   5730 O  O   . SER   D 1 122 ? -18.143 4.272   7.531   1.00 26.36 ? 215 SER   D O   1 
ATOM   5731 C  CB  . SER   D 1 122 ? -19.846 6.489   5.638   1.00 26.73 ? 215 SER   D CB  1 
ATOM   5732 O  OG  . SER   D 1 122 ? -18.643 6.323   4.922   1.00 26.36 ? 215 SER   D OG  1 
ATOM   5733 N  N   . VAL   D 1 123 ? -20.321 3.742   7.033   1.00 26.29 ? 216 VAL   D N   1 
ATOM   5734 C  CA  . VAL   D 1 123 ? -20.204 2.260   7.124   1.00 26.91 ? 216 VAL   D CA  1 
ATOM   5735 C  C   . VAL   D 1 123 ? -20.750 1.705   5.809   1.00 27.09 ? 216 VAL   D C   1 
ATOM   5736 O  O   . VAL   D 1 123 ? -21.813 2.176   5.338   1.00 27.69 ? 216 VAL   D O   1 
ATOM   5737 C  CB  . VAL   D 1 123 ? -20.888 1.695   8.389   1.00 27.04 ? 216 VAL   D CB  1 
ATOM   5738 C  CG1 . VAL   D 1 123 ? -22.342 2.110   8.528   1.00 27.15 ? 216 VAL   D CG1 1 
ATOM   5739 C  CG2 . VAL   D 1 123 ? -20.749 0.186   8.504   1.00 27.44 ? 216 VAL   D CG2 1 
ATOM   5740 N  N   A VAL   D 1 124 ? -20.030 0.756   5.210   0.45 27.48 ? 217 VAL   D N   1 
ATOM   5741 N  N   B VAL   D 1 124 ? -20.028 0.736   5.244   0.55 27.56 ? 217 VAL   D N   1 
ATOM   5742 C  CA  A VAL   D 1 124 ? -20.363 0.197   3.869   0.45 27.61 ? 217 VAL   D CA  1 
ATOM   5743 C  CA  B VAL   D 1 124 ? -20.291 0.149   3.901   0.55 27.75 ? 217 VAL   D CA  1 
ATOM   5744 C  C   A VAL   D 1 124 ? -20.392 -1.334  3.972   0.45 27.89 ? 217 VAL   D C   1 
ATOM   5745 C  C   B VAL   D 1 124 ? -20.438 -1.365  4.062   0.55 27.88 ? 217 VAL   D C   1 
ATOM   5746 O  O   A VAL   D 1 124 ? -19.528 -1.905  4.674   0.45 27.66 ? 217 VAL   D O   1 
ATOM   5747 O  O   B VAL   D 1 124 ? -19.673 -1.955  4.861   0.55 27.37 ? 217 VAL   D O   1 
ATOM   5748 C  CB  A VAL   D 1 124 ? -19.389 0.721   2.795   0.45 27.93 ? 217 VAL   D CB  1 
ATOM   5749 C  CB  B VAL   D 1 124 ? -19.160 0.487   2.916   0.55 28.27 ? 217 VAL   D CB  1 
ATOM   5750 C  CG1 A VAL   D 1 124 ? -17.927 0.420   3.093   0.45 28.32 ? 217 VAL   D CG1 1 
ATOM   5751 C  CG1 B VAL   D 1 124 ? -19.527 0.094   1.490   0.55 28.55 ? 217 VAL   D CG1 1 
ATOM   5752 C  CG2 A VAL   D 1 124 ? -19.765 0.243   1.403   0.45 28.26 ? 217 VAL   D CG2 1 
ATOM   5753 C  CG2 B VAL   D 1 124 ? -18.755 1.946   2.991   0.55 28.42 ? 217 VAL   D CG2 1 
ATOM   5754 N  N   . VAL   D 1 125 ? -21.397 -1.953  3.344   1.00 28.18 ? 218 VAL   D N   1 
ATOM   5755 C  CA  . VAL   D 1 125 ? -21.506 -3.432  3.199   1.00 29.17 ? 218 VAL   D CA  1 
ATOM   5756 C  C   . VAL   D 1 125 ? -21.703 -3.724  1.718   1.00 30.02 ? 218 VAL   D C   1 
ATOM   5757 O  O   . VAL   D 1 125 ? -22.246 -2.902  0.978   1.00 30.34 ? 218 VAL   D O   1 
ATOM   5758 C  CB  . VAL   D 1 125 ? -22.630 -4.024  4.066   1.00 29.05 ? 218 VAL   D CB  1 
ATOM   5759 C  CG1 . VAL   D 1 125 ? -22.275 -3.951  5.546   1.00 28.85 ? 218 VAL   D CG1 1 
ATOM   5760 C  CG2 . VAL   D 1 125 ? -23.979 -3.358  3.804   1.00 29.31 ? 218 VAL   D CG2 1 
ATOM   5761 N  N   . PRO   D 1 126 ? -21.266 -4.908  1.240   1.00 31.20 ? 219 PRO   D N   1 
ATOM   5762 C  CA  . PRO   D 1 126 ? -21.635 -5.358  -0.095  1.00 32.64 ? 219 PRO   D CA  1 
ATOM   5763 C  C   . PRO   D 1 126 ? -23.156 -5.528  -0.177  1.00 33.11 ? 219 PRO   D C   1 
ATOM   5764 O  O   . PRO   D 1 126 ? -23.775 -5.942  0.792   1.00 31.83 ? 219 PRO   D O   1 
ATOM   5765 C  CB  . PRO   D 1 126 ? -20.904 -6.685  -0.318  1.00 33.59 ? 219 PRO   D CB  1 
ATOM   5766 C  CG  . PRO   D 1 126 ? -20.181 -6.997  0.982   1.00 33.21 ? 219 PRO   D CG  1 
ATOM   5767 C  CD  . PRO   D 1 126 ? -20.398 -5.856  1.946   1.00 32.22 ? 219 PRO   D CD  1 
ATOM   5768 N  N   . TYR   D 1 127 ? -23.716 -5.153  -1.326  1.00 34.32 ? 220 TYR   D N   1 
ATOM   5769 C  CA  . TYR   D 1 127 ? -25.121 -5.423  -1.691  1.00 35.56 ? 220 TYR   D CA  1 
ATOM   5770 C  C   . TYR   D 1 127 ? -25.237 -6.924  -1.961  1.00 37.28 ? 220 TYR   D C   1 
ATOM   5771 O  O   . TYR   D 1 127 ? -24.406 -7.471  -2.702  1.00 37.96 ? 220 TYR   D O   1 
ATOM   5772 C  CB  . TYR   D 1 127 ? -25.541 -4.620  -2.923  1.00 35.69 ? 220 TYR   D CB  1 
ATOM   5773 C  CG  . TYR   D 1 127 ? -26.917 -4.996  -3.393  1.00 36.45 ? 220 TYR   D CG  1 
ATOM   5774 C  CD1 . TYR   D 1 127 ? -28.033 -4.428  -2.808  1.00 36.20 ? 220 TYR   D CD1 1 
ATOM   5775 C  CD2 . TYR   D 1 127 ? -27.104 -5.992  -4.342  1.00 37.60 ? 220 TYR   D CD2 1 
ATOM   5776 C  CE1 . TYR   D 1 127 ? -29.311 -4.799  -3.190  1.00 36.59 ? 220 TYR   D CE1 1 
ATOM   5777 C  CE2 . TYR   D 1 127 ? -28.373 -6.372  -4.740  1.00 38.06 ? 220 TYR   D CE2 1 
ATOM   5778 C  CZ  . TYR   D 1 127 ? -29.480 -5.775  -4.153  1.00 37.40 ? 220 TYR   D CZ  1 
ATOM   5779 O  OH  . TYR   D 1 127 ? -30.740 -6.135  -4.513  1.00 36.86 ? 220 TYR   D OH  1 
ATOM   5780 N  N   . GLU   D 1 128 ? -26.197 -7.578  -1.315  1.00 38.73 ? 221 GLU   D N   1 
ATOM   5781 C  CA  . GLU   D 1 128 ? -26.600 -8.967  -1.630  1.00 42.21 ? 221 GLU   D CA  1 
ATOM   5782 C  C   . GLU   D 1 128 ? -28.050 -8.909  -2.085  1.00 42.94 ? 221 GLU   D C   1 
ATOM   5783 O  O   . GLU   D 1 128 ? -28.859 -8.173  -1.523  1.00 42.63 ? 221 GLU   D O   1 
ATOM   5784 C  CB  . GLU   D 1 128 ? -26.410 -9.903  -0.437  1.00 43.39 ? 221 GLU   D CB  1 
ATOM   5785 C  CG  . GLU   D 1 128 ? -24.956 -10.102 -0.078  1.00 44.36 ? 221 GLU   D CG  1 
ATOM   5786 C  CD  . GLU   D 1 128 ? -24.678 -10.861 1.204   1.00 45.53 ? 221 GLU   D CD  1 
ATOM   5787 O  OE1 . GLU   D 1 128 ? -25.626 -11.406 1.822   1.00 47.85 ? 221 GLU   D OE1 1 
ATOM   5788 O  OE2 . GLU   D 1 128 ? -23.499 -10.909 1.576   1.00 47.24 ? 221 GLU   D OE2 1 
ATOM   5789 N  N   . PRO   D 1 129 ? -28.417 -9.677  -3.130  1.00 44.83 ? 222 PRO   D N   1 
ATOM   5790 C  CA  . PRO   D 1 129 ? -29.795 -9.698  -3.605  1.00 45.79 ? 222 PRO   D CA  1 
ATOM   5791 C  C   . PRO   D 1 129 ? -30.680 -10.356 -2.555  1.00 46.35 ? 222 PRO   D C   1 
ATOM   5792 O  O   . PRO   D 1 129 ? -30.186 -11.027 -1.650  1.00 47.27 ? 222 PRO   D O   1 
ATOM   5793 C  CB  . PRO   D 1 129 ? -29.735 -10.511 -4.906  1.00 47.32 ? 222 PRO   D CB  1 
ATOM   5794 C  CG  . PRO   D 1 129 ? -28.466 -11.334 -4.800  1.00 47.53 ? 222 PRO   D CG  1 
ATOM   5795 C  CD  . PRO   D 1 129 ? -27.528 -10.563 -3.898  1.00 45.84 ? 222 PRO   D CD  1 
ATOM   5796 N  N   . PRO   D 1 130 ? -32.017 -10.201 -2.635  1.00 47.59 ? 223 PRO   D N   1 
ATOM   5797 C  CA  . PRO   D 1 130 ? -32.904 -10.854 -1.669  1.00 47.95 ? 223 PRO   D CA  1 
ATOM   5798 C  C   . PRO   D 1 130 ? -32.671 -12.377 -1.702  1.00 49.76 ? 223 PRO   D C   1 
ATOM   5799 O  O   . PRO   D 1 130 ? -32.210 -12.882 -2.705  1.00 50.05 ? 223 PRO   D O   1 
ATOM   5800 C  CB  . PRO   D 1 130 ? -34.305 -10.469 -2.153  1.00 48.61 ? 223 PRO   D CB  1 
ATOM   5801 C  CG  . PRO   D 1 130 ? -34.113 -9.252  -3.052  1.00 47.76 ? 223 PRO   D CG  1 
ATOM   5802 C  CD  . PRO   D 1 130 ? -32.733 -9.412  -3.655  1.00 47.69 ? 223 PRO   D CD  1 
ATOM   5803 N  N   . GLU   D 1 131 ? -32.946 -13.062 -0.591  1.00 51.20 ? 224 GLU   D N   1 
ATOM   5804 C  CA  . GLU   D 1 131 ? -32.883 -14.543 -0.473  1.00 52.90 ? 224 GLU   D CA  1 
ATOM   5805 C  C   . GLU   D 1 131 ? -34.049 -15.132 -1.270  1.00 54.55 ? 224 GLU   D C   1 
ATOM   5806 O  O   . GLU   D 1 131 ? -35.020 -14.387 -1.531  1.00 54.42 ? 224 GLU   D O   1 
ATOM   5807 C  CB  . GLU   D 1 131 ? -32.936 -14.943 1.008   1.00 53.14 ? 224 GLU   D CB  1 
ATOM   5808 C  CG  . GLU   D 1 131 ? -33.202 -16.418 1.283   1.00 55.12 ? 224 GLU   D CG  1 
ATOM   5809 C  CD  . GLU   D 1 131 ? -33.995 -16.680 2.555   1.00 55.58 ? 224 GLU   D CD  1 
ATOM   5810 O  OE1 . GLU   D 1 131 ? -35.121 -17.236 2.464   1.00 56.93 ? 224 GLU   D OE1 1 
ATOM   5811 O  OE2 . GLU   D 1 131 ? -33.492 -16.315 3.632   1.00 55.11 ? 224 GLU   D OE2 1 
ATOM   5812 N  N   . VAL   D 1 132 ? -33.971 -16.420 -1.619  1.00 56.30 ? 225 VAL   D N   1 
ATOM   5813 C  CA  . VAL   D 1 132 ? -35.113 -17.216 -2.165  1.00 58.87 ? 225 VAL   D CA  1 
ATOM   5814 C  C   . VAL   D 1 132 ? -36.305 -17.072 -1.207  1.00 59.33 ? 225 VAL   D C   1 
ATOM   5815 O  O   . VAL   D 1 132 ? -36.161 -17.479 -0.033  1.00 60.05 ? 225 VAL   D O   1 
ATOM   5816 C  CB  . VAL   D 1 132 ? -34.742 -18.700 -2.365  1.00 60.39 ? 225 VAL   D CB  1 
ATOM   5817 C  CG1 . VAL   D 1 132 ? -35.938 -19.508 -2.851  1.00 62.43 ? 225 VAL   D CG1 1 
ATOM   5818 C  CG2 . VAL   D 1 132 ? -33.554 -18.877 -3.298  1.00 60.23 ? 225 VAL   D CG2 1 
ATOM   5819 N  N   . GLY   D 1 133 ? -37.418 -16.498 -1.687  1.00 59.77 ? 226 GLY   D N   1 
ATOM   5820 C  CA  . GLY   D 1 133 ? -38.623 -16.202 -0.888  1.00 60.43 ? 226 GLY   D CA  1 
ATOM   5821 C  C   . GLY   D 1 133 ? -38.851 -14.705 -0.698  1.00 58.94 ? 226 GLY   D C   1 
ATOM   5822 O  O   . GLY   D 1 133 ? -40.010 -14.270 -0.786  1.00 59.89 ? 226 GLY   D O   1 
ATOM   5823 N  N   . SER   D 1 134 ? -37.780 -13.951 -0.435  1.00 58.06 ? 227 SER   D N   1 
ATOM   5824 C  CA  . SER   D 1 134 ? -37.798 -12.541 0.040   1.00 55.98 ? 227 SER   D CA  1 
ATOM   5825 C  C   . SER   D 1 134 ? -37.747 -11.573 -1.147  1.00 55.14 ? 227 SER   D C   1 
ATOM   5826 O  O   . SER   D 1 134 ? -37.255 -11.972 -2.222  1.00 55.31 ? 227 SER   D O   1 
ATOM   5827 C  CB  . SER   D 1 134 ? -36.663 -12.303 0.989   1.00 56.05 ? 227 SER   D CB  1 
ATOM   5828 O  OG  . SER   D 1 134 ? -36.712 -13.236 2.064   1.00 56.96 ? 227 SER   D OG  1 
ATOM   5829 N  N   . ASP   D 1 135 ? -38.277 -10.358 -0.980  1.00 53.13 ? 228 ASP   D N   1 
ATOM   5830 C  CA  . ASP   D 1 135 ? -38.530 -9.392  -2.090  1.00 52.38 ? 228 ASP   D CA  1 
ATOM   5831 C  C   . ASP   D 1 135 ? -37.625 -8.161  -1.940  1.00 50.24 ? 228 ASP   D C   1 
ATOM   5832 O  O   . ASP   D 1 135 ? -37.645 -7.295  -2.831  1.00 50.75 ? 228 ASP   D O   1 
ATOM   5833 C  CB  . ASP   D 1 135 ? -40.004 -8.978  -2.146  1.00 53.85 ? 228 ASP   D CB  1 
ATOM   5834 C  CG  . ASP   D 1 135 ? -40.952 -10.145 -2.398  1.00 56.05 ? 228 ASP   D CG  1 
ATOM   5835 O  OD1 . ASP   D 1 135 ? -40.645 -10.969 -3.291  1.00 57.71 ? 228 ASP   D OD1 1 
ATOM   5836 O  OD2 . ASP   D 1 135 ? -41.984 -10.246 -1.678  1.00 56.70 ? 228 ASP   D OD2 1 
ATOM   5837 N  N   . CYS   D 1 136 ? -36.844 -8.082  -0.862  1.00 47.05 ? 229 CYS   D N   1 
ATOM   5838 C  CA  . CYS   D 1 136 ? -35.993 -6.903  -0.511  1.00 44.12 ? 229 CYS   D CA  1 
ATOM   5839 C  C   . CYS   D 1 136 ? -34.752 -7.407  0.229   1.00 42.69 ? 229 CYS   D C   1 
ATOM   5840 O  O   . CYS   D 1 136 ? -34.762 -8.583  0.687   1.00 43.04 ? 229 CYS   D O   1 
ATOM   5841 C  CB  . CYS   D 1 136 ? -36.747 -5.894  0.353   1.00 43.11 ? 229 CYS   D CB  1 
ATOM   5842 S  SG  . CYS   D 1 136 ? -37.267 -6.569  1.951   1.00 42.81 ? 229 CYS   D SG  1 
ATOM   5843 N  N   . THR   D 1 137 ? -33.717 -6.569  0.343   1.00 40.65 ? 230 THR   D N   1 
ATOM   5844 C  CA  . THR   D 1 137 ? -32.507 -6.883  1.141   1.00 39.10 ? 230 THR   D CA  1 
ATOM   5845 C  C   . THR   D 1 137 ? -32.562 -6.091  2.446   1.00 37.33 ? 230 THR   D C   1 
ATOM   5846 O  O   . THR   D 1 137 ? -32.792 -4.867  2.375   1.00 37.47 ? 230 THR   D O   1 
ATOM   5847 C  CB  . THR   D 1 137 ? -31.234 -6.629  0.331   1.00 39.39 ? 230 THR   D CB  1 
ATOM   5848 O  OG1 . THR   D 1 137 ? -31.324 -7.453  -0.834  1.00 40.46 ? 230 THR   D OG1 1 
ATOM   5849 C  CG2 . THR   D 1 137 ? -29.978 -6.950  1.109   1.00 39.06 ? 230 THR   D CG2 1 
ATOM   5850 N  N   . THR   D 1 138 ? -32.394 -6.766  3.584   1.00 36.20 ? 231 THR   D N   1 
ATOM   5851 C  CA  . THR   D 1 138 ? -32.409 -6.149  4.933   1.00 35.54 ? 231 THR   D CA  1 
ATOM   5852 C  C   . THR   D 1 138 ? -30.965 -5.971  5.411   1.00 34.68 ? 231 THR   D C   1 
ATOM   5853 O  O   . THR   D 1 138 ? -30.191 -6.947  5.333   1.00 34.30 ? 231 THR   D O   1 
ATOM   5854 C  CB  . THR   D 1 138 ? -33.263 -6.947  5.928   1.00 35.91 ? 231 THR   D CB  1 
ATOM   5855 O  OG1 . THR   D 1 138 ? -34.597 -7.009  5.423   1.00 35.44 ? 231 THR   D OG1 1 
ATOM   5856 C  CG2 . THR   D 1 138 ? -33.309 -6.325  7.309   1.00 35.71 ? 231 THR   D CG2 1 
ATOM   5857 N  N   . ILE   D 1 139 ? -30.637 -4.750  5.839   1.00 33.67 ? 232 ILE   D N   1 
ATOM   5858 C  CA  . ILE   D 1 139 ? -29.405 -4.399  6.603   1.00 33.63 ? 232 ILE   D CA  1 
ATOM   5859 C  C   . ILE   D 1 139 ? -29.816 -4.081  8.041   1.00 32.83 ? 232 ILE   D C   1 
ATOM   5860 O  O   . ILE   D 1 139 ? -30.828 -3.371  8.233   1.00 33.00 ? 232 ILE   D O   1 
ATOM   5861 C  CB  . ILE   D 1 139 ? -28.660 -3.219  5.949   1.00 32.83 ? 232 ILE   D CB  1 
ATOM   5862 C  CG1 . ILE   D 1 139 ? -28.178 -3.583  4.542   1.00 33.80 ? 232 ILE   D CG1 1 
ATOM   5863 C  CG2 . ILE   D 1 139 ? -27.510 -2.742  6.837   1.00 32.96 ? 232 ILE   D CG2 1 
ATOM   5864 C  CD1 . ILE   D 1 139 ? -27.663 -2.401  3.754   1.00 33.61 ? 232 ILE   D CD1 1 
ATOM   5865 N  N   . HIS   D 1 140 ? -29.037 -4.575  9.004   1.00 33.41 ? 233 HIS   D N   1 
ATOM   5866 C  CA  . HIS   D 1 140 ? -29.226 -4.338  10.456  1.00 33.41 ? 233 HIS   D CA  1 
ATOM   5867 C  C   . HIS   D 1 140 ? -28.264 -3.240  10.911  1.00 32.62 ? 233 HIS   D C   1 
ATOM   5868 O  O   . HIS   D 1 140 ? -27.096 -3.537  11.116  1.00 32.42 ? 233 HIS   D O   1 
ATOM   5869 C  CB  . HIS   D 1 140 ? -29.075 -5.661  11.221  1.00 34.36 ? 233 HIS   D CB  1 
ATOM   5870 C  CG  . HIS   D 1 140 ? -30.217 -6.595  11.012  1.00 35.29 ? 233 HIS   D CG  1 
ATOM   5871 N  ND1 . HIS   D 1 140 ? -30.152 -7.934  11.346  1.00 36.36 ? 233 HIS   D ND1 1 
ATOM   5872 C  CD2 . HIS   D 1 140 ? -31.455 -6.393  10.518  1.00 35.45 ? 233 HIS   D CD2 1 
ATOM   5873 C  CE1 . HIS   D 1 140 ? -31.309 -8.504  11.074  1.00 37.11 ? 233 HIS   D CE1 1 
ATOM   5874 N  NE2 . HIS   D 1 140 ? -32.116 -7.586  10.555  1.00 36.05 ? 233 HIS   D NE2 1 
ATOM   5875 N  N   . TYR   D 1 141 ? -28.749 -2.003  11.023  1.00 32.66 ? 234 TYR   D N   1 
ATOM   5876 C  CA  . TYR   D 1 141 ? -27.994 -0.853  11.590  1.00 32.27 ? 234 TYR   D CA  1 
ATOM   5877 C  C   . TYR   D 1 141 ? -28.138 -0.831  13.124  1.00 33.23 ? 234 TYR   D C   1 
ATOM   5878 O  O   . TYR   D 1 141 ? -29.190 -1.254  13.657  1.00 33.05 ? 234 TYR   D O   1 
ATOM   5879 C  CB  . TYR   D 1 141 ? -28.454 0.441   10.915  1.00 31.06 ? 234 TYR   D CB  1 
ATOM   5880 C  CG  . TYR   D 1 141 ? -28.072 0.522   9.458   1.00 30.53 ? 234 TYR   D CG  1 
ATOM   5881 C  CD1 . TYR   D 1 141 ? -26.746 0.682   9.088   1.00 30.35 ? 234 TYR   D CD1 1 
ATOM   5882 C  CD2 . TYR   D 1 141 ? -29.021 0.390   8.448   1.00 30.01 ? 234 TYR   D CD2 1 
ATOM   5883 C  CE1 . TYR   D 1 141 ? -26.370 0.733   7.754   1.00 30.55 ? 234 TYR   D CE1 1 
ATOM   5884 C  CE2 . TYR   D 1 141 ? -28.661 0.454   7.109   1.00 30.30 ? 234 TYR   D CE2 1 
ATOM   5885 C  CZ  . TYR   D 1 141 ? -27.329 0.626   6.762   1.00 30.37 ? 234 TYR   D CZ  1 
ATOM   5886 O  OH  . TYR   D 1 141 ? -26.942 0.692   5.455   1.00 30.86 ? 234 TYR   D OH  1 
ATOM   5887 N  N   . ASN   D 1 142 ? -27.088 -0.370  13.814  1.00 34.09 ? 235 ASN   D N   1 
ATOM   5888 C  CA  . ASN   D 1 142 ? -27.102 0.010   15.254  1.00 34.11 ? 235 ASN   D CA  1 
ATOM   5889 C  C   . ASN   D 1 142 ? -26.681 1.474   15.375  1.00 33.56 ? 235 ASN   D C   1 
ATOM   5890 O  O   . ASN   D 1 142 ? -25.658 1.840   14.772  1.00 33.43 ? 235 ASN   D O   1 
ATOM   5891 C  CB  . ASN   D 1 142 ? -26.130 -0.796  16.120  1.00 34.85 ? 235 ASN   D CB  1 
ATOM   5892 C  CG  . ASN   D 1 142 ? -26.361 -2.291  16.078  1.00 35.34 ? 235 ASN   D CG  1 
ATOM   5893 O  OD1 . ASN   D 1 142 ? -25.474 -3.046  16.450  1.00 36.36 ? 235 ASN   D OD1 1 
ATOM   5894 N  ND2 . ASN   D 1 142 ? -27.529 -2.726  15.633  1.00 34.61 ? 235 ASN   D ND2 1 
ATOM   5895 N  N   . TYR   D 1 143 ? -27.446 2.278   16.115  1.00 32.74 ? 236 TYR   D N   1 
ATOM   5896 C  CA  . TYR   D 1 143 ? -27.090 3.679   16.460  1.00 32.90 ? 236 TYR   D CA  1 
ATOM   5897 C  C   . TYR   D 1 143 ? -26.541 3.690   17.889  1.00 34.31 ? 236 TYR   D C   1 
ATOM   5898 O  O   . TYR   D 1 143 ? -27.197 3.165   18.792  1.00 35.55 ? 236 TYR   D O   1 
ATOM   5899 C  CB  . TYR   D 1 143 ? -28.285 4.605   16.225  1.00 32.15 ? 236 TYR   D CB  1 
ATOM   5900 C  CG  . TYR   D 1 143 ? -28.702 4.697   14.785  1.00 31.08 ? 236 TYR   D CG  1 
ATOM   5901 C  CD1 . TYR   D 1 143 ? -29.497 3.720   14.192  1.00 30.79 ? 236 TYR   D CD1 1 
ATOM   5902 C  CD2 . TYR   D 1 143 ? -28.278 5.749   13.994  1.00 30.82 ? 236 TYR   D CD2 1 
ATOM   5903 C  CE1 . TYR   D 1 143 ? -29.906 3.829   12.872  1.00 30.18 ? 236 TYR   D CE1 1 
ATOM   5904 C  CE2 . TYR   D 1 143 ? -28.641 5.846   12.663  1.00 30.26 ? 236 TYR   D CE2 1 
ATOM   5905 C  CZ  . TYR   D 1 143 ? -29.464 4.891   12.099  1.00 29.97 ? 236 TYR   D CZ  1 
ATOM   5906 O  OH  . TYR   D 1 143 ? -29.809 4.997   10.783  1.00 29.51 ? 236 TYR   D OH  1 
ATOM   5907 N  N   . MET   D 1 144 ? -25.336 4.225   18.065  1.00 34.77 ? 237 MET   D N   1 
ATOM   5908 C  CA  . MET   D 1 144 ? -24.486 3.986   19.258  1.00 35.61 ? 237 MET   D CA  1 
ATOM   5909 C  C   . MET   D 1 144 ? -24.468 5.193   20.218  1.00 36.58 ? 237 MET   D C   1 
ATOM   5910 O  O   . MET   D 1 144 ? -23.664 5.193   21.175  1.00 37.02 ? 237 MET   D O   1 
ATOM   5911 C  CB  . MET   D 1 144 ? -23.065 3.643   18.799  1.00 35.63 ? 237 MET   D CB  1 
ATOM   5912 C  CG  . MET   D 1 144 ? -23.002 2.384   17.910  1.00 34.93 ? 237 MET   D CG  1 
ATOM   5913 S  SD  . MET   D 1 144 ? -23.834 0.929   18.626  1.00 35.62 ? 237 MET   D SD  1 
ATOM   5914 C  CE  . MET   D 1 144 ? -22.978 0.863   20.203  1.00 35.79 ? 237 MET   D CE  1 
ATOM   5915 N  N   A CYS   D 1 145 ? -25.338 6.184   19.989  0.50 36.81 ? 238 CYS   D N   1 
ATOM   5916 N  N   B CYS   D 1 145 ? -25.270 6.222   19.952  0.50 36.95 ? 238 CYS   D N   1 
ATOM   5917 C  CA  A CYS   D 1 145 ? -25.458 7.428   20.817  0.50 37.94 ? 238 CYS   D CA  1 
ATOM   5918 C  CA  B CYS   D 1 145 ? -25.486 7.363   20.880  0.50 38.24 ? 238 CYS   D CA  1 
ATOM   5919 C  C   A CYS   D 1 145 ? -26.931 7.856   20.817  0.50 38.00 ? 238 CYS   D C   1 
ATOM   5920 C  C   B CYS   D 1 145 ? -26.961 7.748   20.864  0.50 38.14 ? 238 CYS   D C   1 
ATOM   5921 O  O   A CYS   D 1 145 ? -27.601 7.645   19.783  0.50 37.31 ? 238 CYS   D O   1 
ATOM   5922 O  O   B CYS   D 1 145 ? -27.648 7.394   19.882  0.50 37.25 ? 238 CYS   D O   1 
ATOM   5923 C  CB  A CYS   D 1 145 ? -24.563 8.515   20.221  0.50 38.52 ? 238 CYS   D CB  1 
ATOM   5924 C  CB  B CYS   D 1 145 ? -24.621 8.553   20.492  0.50 39.12 ? 238 CYS   D CB  1 
ATOM   5925 S  SG  A CYS   D 1 145 ? -23.881 9.786   21.279  0.50 40.27 ? 238 CYS   D SG  1 
ATOM   5926 S  SG  B CYS   D 1 145 ? -23.143 8.704   21.415  0.50 41.27 ? 238 CYS   D SG  1 
ATOM   5927 N  N   . ASN   D 1 146 ? -27.422 8.392   21.939  1.00 38.90 ? 239 ASN   D N   1 
ATOM   5928 C  CA  . ASN   D 1 146 ? -28.815 8.891   22.062  1.00 39.25 ? 239 ASN   D CA  1 
ATOM   5929 C  C   . ASN   D 1 146 ? -28.868 10.294  21.449  1.00 39.92 ? 239 ASN   D C   1 
ATOM   5930 O  O   . ASN   D 1 146 ? -27.852 11.030  21.549  1.00 40.62 ? 239 ASN   D O   1 
ATOM   5931 C  CB  . ASN   D 1 146 ? -29.308 8.876   23.512  1.00 40.85 ? 239 ASN   D CB  1 
ATOM   5932 C  CG  . ASN   D 1 146 ? -29.702 7.492   23.980  1.00 40.97 ? 239 ASN   D CG  1 
ATOM   5933 O  OD1 . ASN   D 1 146 ? -30.425 6.777   23.287  1.00 39.50 ? 239 ASN   D OD1 1 
ATOM   5934 N  ND2 . ASN   D 1 146 ? -29.247 7.122   25.168  1.00 42.49 ? 239 ASN   D ND2 1 
ATOM   5935 N  N   . SER   D 1 147 ? -30.000 10.642  20.825  1.00 39.51 ? 240 SER   D N   1 
ATOM   5936 C  CA  . SER   D 1 147 ? -30.269 11.998  20.277  1.00 40.07 ? 240 SER   D CA  1 
ATOM   5937 C  C   . SER   D 1 147 ? -30.060 13.053  21.375  1.00 42.22 ? 240 SER   D C   1 
ATOM   5938 O  O   . SER   D 1 147 ? -29.658 14.188  21.035  1.00 42.80 ? 240 SER   D O   1 
ATOM   5939 C  CB  . SER   D 1 147 ? -31.660 12.078  19.691  1.00 39.86 ? 240 SER   D CB  1 
ATOM   5940 O  OG  . SER   D 1 147 ? -31.812 11.182  18.596  1.00 38.05 ? 240 SER   D OG  1 
ATOM   5941 N  N   . SER   D 1 148 ? -30.315 12.684  22.638  1.00 43.05 ? 241 SER   D N   1 
ATOM   5942 C  CA  . SER   D 1 148 ? -30.258 13.562  23.838  1.00 45.41 ? 241 SER   D CA  1 
ATOM   5943 C  C   . SER   D 1 148 ? -28.820 13.805  24.331  1.00 46.52 ? 241 SER   D C   1 
ATOM   5944 O  O   . SER   D 1 148 ? -28.633 14.747  25.114  1.00 48.22 ? 241 SER   D O   1 
ATOM   5945 C  CB  . SER   D 1 148 ? -31.099 12.974  24.940  1.00 45.77 ? 241 SER   D CB  1 
ATOM   5946 O  OG  . SER   D 1 148 ? -30.592 11.719  25.359  1.00 45.57 ? 241 SER   D OG  1 
ATOM   5947 N  N   . CYS   D 1 149 ? -27.848 12.980  23.927  1.00 46.04 ? 242 CYS   D N   1 
ATOM   5948 C  CA  . CYS   D 1 149 ? -26.473 12.956  24.503  1.00 47.13 ? 242 CYS   D CA  1 
ATOM   5949 C  C   . CYS   D 1 149 ? -25.840 14.353  24.467  1.00 48.95 ? 242 CYS   D C   1 
ATOM   5950 O  O   . CYS   D 1 149 ? -25.611 14.877  23.357  1.00 46.83 ? 242 CYS   D O   1 
ATOM   5951 C  CB  . CYS   D 1 149 ? -25.590 11.985  23.726  1.00 45.60 ? 242 CYS   D CB  1 
ATOM   5952 S  SG  . CYS   D 1 149 ? -25.701 10.299  24.243  1.00 45.69 ? 242 CYS   D SG  1 
ATOM   5953 N  N   . MET   D 1 150 ? -25.563 14.932  25.640  1.00 52.68 ? 243 MET   D N   1 
ATOM   5954 C  CA  . MET   D 1 150 ? -24.717 16.147  25.807  1.00 55.29 ? 243 MET   D CA  1 
ATOM   5955 C  C   . MET   D 1 150 ? -23.327 15.867  25.223  1.00 55.17 ? 243 MET   D C   1 
ATOM   5956 O  O   . MET   D 1 150 ? -22.779 14.780  25.485  1.00 55.80 ? 243 MET   D O   1 
ATOM   5957 C  CB  . MET   D 1 150 ? -24.573 16.534  27.285  1.00 58.27 ? 243 MET   D CB  1 
ATOM   5958 C  CG  . MET   D 1 150 ? -25.850 17.083  27.890  1.00 59.86 ? 243 MET   D CG  1 
ATOM   5959 S  SD  . MET   D 1 150 ? -25.554 18.149  29.332  1.00 63.40 ? 243 MET   D SD  1 
ATOM   5960 C  CE  . MET   D 1 150 ? -24.516 19.407  28.590  1.00 63.93 ? 243 MET   D CE  1 
ATOM   5961 N  N   . GLY   D 1 151 ? -22.799 16.797  24.428  1.00 55.31 ? 244 GLY   D N   1 
ATOM   5962 C  CA  . GLY   D 1 151 ? -21.458 16.686  23.823  1.00 55.43 ? 244 GLY   D CA  1 
ATOM   5963 C  C   . GLY   D 1 151 ? -21.433 15.682  22.685  1.00 53.73 ? 244 GLY   D C   1 
ATOM   5964 O  O   . GLY   D 1 151 ? -20.337 15.217  22.330  1.00 53.76 ? 244 GLY   D O   1 
ATOM   5965 N  N   . GLY   D 1 152 ? -22.612 15.346  22.149  1.00 51.93 ? 245 GLY   D N   1 
ATOM   5966 C  CA  . GLY   D 1 152 ? -22.808 14.591  20.903  1.00 49.76 ? 245 GLY   D CA  1 
ATOM   5967 C  C   . GLY   D 1 152 ? -23.846 15.317  20.050  1.00 48.63 ? 245 GLY   D C   1 
ATOM   5968 O  O   . GLY   D 1 152 ? -23.701 16.534  19.824  1.00 49.23 ? 245 GLY   D O   1 
ATOM   5969 N  N   . MET   D 1 153 ? -24.893 14.607  19.634  1.00 47.06 ? 246 MET   D N   1 
ATOM   5970 C  CA  . MET   D 1 153 ? -26.005 15.184  18.840  1.00 45.89 ? 246 MET   D CA  1 
ATOM   5971 C  C   . MET   D 1 153 ? -26.744 16.251  19.655  1.00 46.62 ? 246 MET   D C   1 
ATOM   5972 O  O   . MET   D 1 153 ? -27.177 17.256  19.055  1.00 46.48 ? 246 MET   D O   1 
ATOM   5973 C  CB  . MET   D 1 153 ? -26.963 14.083  18.387  1.00 44.54 ? 246 MET   D CB  1 
ATOM   5974 C  CG  . MET   D 1 153 ? -26.324 13.130  17.398  1.00 43.50 ? 246 MET   D CG  1 
ATOM   5975 S  SD  . MET   D 1 153 ? -27.506 11.918  16.815  1.00 41.73 ? 246 MET   D SD  1 
ATOM   5976 C  CE  . MET   D 1 153 ? -27.435 10.717  18.146  1.00 41.87 ? 246 MET   D CE  1 
ATOM   5977 N  N   . ASN   D 1 154 ? -26.854 16.046  20.970  1.00 47.28 ? 247 ASN   D N   1 
ATOM   5978 C  CA  . ASN   D 1 154 ? -27.367 17.039  21.954  1.00 49.18 ? 247 ASN   D CA  1 
ATOM   5979 C  C   . ASN   D 1 154 ? -28.706 17.595  21.456  1.00 49.18 ? 247 ASN   D C   1 
ATOM   5980 O  O   . ASN   D 1 154 ? -28.826 18.824  21.303  1.00 50.14 ? 247 ASN   D O   1 
ATOM   5981 C  CB  . ASN   D 1 154 ? -26.325 18.126  22.232  1.00 50.43 ? 247 ASN   D CB  1 
ATOM   5982 C  CG  . ASN   D 1 154 ? -26.754 19.125  23.281  1.00 52.69 ? 247 ASN   D CG  1 
ATOM   5983 O  OD1 . ASN   D 1 154 ? -27.402 18.773  24.264  1.00 53.62 ? 247 ASN   D OD1 1 
ATOM   5984 N  ND2 . ASN   D 1 154 ? -26.392 20.378  23.078  1.00 54.02 ? 247 ASN   D ND2 1 
ATOM   5985 N  N   . ARG   D 1 155 ? -29.647 16.688  21.178  1.00 48.53 ? 248 ARG   D N   1 
ATOM   5986 C  CA  . ARG   D 1 155 ? -31.083 16.950  20.883  1.00 48.87 ? 248 ARG   D CA  1 
ATOM   5987 C  C   . ARG   D 1 155 ? -31.266 17.480  19.454  1.00 47.80 ? 248 ARG   D C   1 
ATOM   5988 O  O   . ARG   D 1 155 ? -32.427 17.694  19.058  1.00 48.81 ? 248 ARG   D O   1 
ATOM   5989 C  CB  . ARG   D 1 155 ? -31.682 17.897  21.930  1.00 51.27 ? 248 ARG   D CB  1 
ATOM   5990 C  CG  . ARG   D 1 155 ? -31.509 17.401  23.357  1.00 52.53 ? 248 ARG   D CG  1 
ATOM   5991 C  CD  . ARG   D 1 155 ? -32.520 17.976  24.328  1.00 54.84 ? 248 ARG   D CD  1 
ATOM   5992 N  NE  . ARG   D 1 155 ? -32.447 17.329  25.633  1.00 56.38 ? 248 ARG   D NE  1 
ATOM   5993 C  CZ  . ARG   D 1 155 ? -33.060 16.194  25.965  1.00 56.08 ? 248 ARG   D CZ  1 
ATOM   5994 N  NH1 . ARG   D 1 155 ? -33.798 15.537  25.081  1.00 54.71 ? 248 ARG   D NH1 1 
ATOM   5995 N  NH2 . ARG   D 1 155 ? -32.925 15.715  27.191  1.00 56.74 ? 248 ARG   D NH2 1 
ATOM   5996 N  N   . ARG   D 1 156 ? -30.187 17.619  18.677  1.00 46.42 ? 249 ARG   D N   1 
ATOM   5997 C  CA  . ARG   D 1 156 ? -30.266 18.063  17.261  1.00 45.24 ? 249 ARG   D CA  1 
ATOM   5998 C  C   . ARG   D 1 156 ? -30.699 16.880  16.400  1.00 43.47 ? 249 ARG   D C   1 
ATOM   5999 O  O   . ARG   D 1 156 ? -30.125 15.792  16.497  1.00 42.66 ? 249 ARG   D O   1 
ATOM   6000 C  CB  . ARG   D 1 156 ? -28.925 18.640  16.806  1.00 45.74 ? 249 ARG   D CB  1 
ATOM   6001 C  CG  . ARG   D 1 156 ? -28.501 19.879  17.581  1.00 47.59 ? 249 ARG   D CG  1 
ATOM   6002 C  CD  . ARG   D 1 156 ? -27.107 20.336  17.198  1.00 48.09 ? 249 ARG   D CD  1 
ATOM   6003 N  NE  . ARG   D 1 156 ? -26.098 19.398  17.657  1.00 47.92 ? 249 ARG   D NE  1 
ATOM   6004 C  CZ  . ARG   D 1 156 ? -24.791 19.505  17.420  1.00 48.09 ? 249 ARG   D CZ  1 
ATOM   6005 N  NH1 . ARG   D 1 156 ? -24.330 20.520  16.714  1.00 48.85 ? 249 ARG   D NH1 1 
ATOM   6006 N  NH2 . ARG   D 1 156 ? -23.953 18.591  17.886  1.00 47.56 ? 249 ARG   D NH2 1 
ATOM   6007 N  N   . PRO   D 1 157 ? -31.720 17.053  15.530  1.00 42.44 ? 250 PRO   D N   1 
ATOM   6008 C  CA  . PRO   D 1 157 ? -32.191 15.965  14.672  1.00 41.20 ? 250 PRO   D CA  1 
ATOM   6009 C  C   . PRO   D 1 157 ? -31.167 15.634  13.576  1.00 39.23 ? 250 PRO   D C   1 
ATOM   6010 O  O   . PRO   D 1 157 ? -30.477 16.545  13.093  1.00 39.91 ? 250 PRO   D O   1 
ATOM   6011 C  CB  . PRO   D 1 157 ? -33.493 16.507  14.065  1.00 41.91 ? 250 PRO   D CB  1 
ATOM   6012 C  CG  . PRO   D 1 157 ? -33.320 18.024  14.097  1.00 43.10 ? 250 PRO   D CG  1 
ATOM   6013 C  CD  . PRO   D 1 157 ? -32.465 18.304  15.316  1.00 43.96 ? 250 PRO   D CD  1 
ATOM   6014 N  N   . ILE   D 1 158 ? -31.078 14.354  13.213  1.00 36.56 ? 251 ILE   D N   1 
ATOM   6015 C  CA  . ILE   D 1 158 ? -30.146 13.874  12.156  1.00 35.44 ? 251 ILE   D CA  1 
ATOM   6016 C  C   . ILE   D 1 158 ? -30.939 13.148  11.073  1.00 34.18 ? 251 ILE   D C   1 
ATOM   6017 O  O   . ILE   D 1 158 ? -32.057 12.665  11.357  1.00 34.77 ? 251 ILE   D O   1 
ATOM   6018 C  CB  . ILE   D 1 158 ? -29.036 12.991  12.760  1.00 34.93 ? 251 ILE   D CB  1 
ATOM   6019 C  CG1 . ILE   D 1 158 ? -29.593 11.755  13.466  1.00 34.47 ? 251 ILE   D CG1 1 
ATOM   6020 C  CG2 . ILE   D 1 158 ? -28.161 13.816  13.684  1.00 35.42 ? 251 ILE   D CG2 1 
ATOM   6021 C  CD1 . ILE   D 1 158 ? -28.602 10.607  13.514  1.00 33.97 ? 251 ILE   D CD1 1 
ATOM   6022 N  N   . LEU   D 1 159 ? -30.376 13.112  9.868   1.00 33.36 ? 252 LEU   D N   1 
ATOM   6023 C  CA  . LEU   D 1 159 ? -30.806 12.221  8.763   1.00 32.71 ? 252 LEU   D CA  1 
ATOM   6024 C  C   . LEU   D 1 159 ? -29.747 11.129  8.626   1.00 31.71 ? 252 LEU   D C   1 
ATOM   6025 O  O   . LEU   D 1 159 ? -28.554 11.424  8.850   1.00 31.90 ? 252 LEU   D O   1 
ATOM   6026 C  CB  . LEU   D 1 159 ? -30.928 13.019  7.461   1.00 32.69 ? 252 LEU   D CB  1 
ATOM   6027 C  CG  . LEU   D 1 159 ? -31.739 14.312  7.551   1.00 33.64 ? 252 LEU   D CG  1 
ATOM   6028 C  CD1 . LEU   D 1 159 ? -31.683 15.086  6.242   1.00 34.34 ? 252 LEU   D CD1 1 
ATOM   6029 C  CD2 . LEU   D 1 159 ? -33.193 14.048  7.951   1.00 33.51 ? 252 LEU   D CD2 1 
ATOM   6030 N  N   . THR   D 1 160 ? -30.169 9.916   8.286   1.00 31.53 ? 253 THR   D N   1 
ATOM   6031 C  CA  . THR   D 1 160 ? -29.310 8.851   7.722   1.00 30.69 ? 253 THR   D CA  1 
ATOM   6032 C  C   . THR   D 1 160 ? -29.474 8.875   6.207   1.00 30.76 ? 253 THR   D C   1 
ATOM   6033 O  O   . THR   D 1 160 ? -30.631 8.843   5.740   1.00 31.65 ? 253 THR   D O   1 
ATOM   6034 C  CB  . THR   D 1 160 ? -29.665 7.454   8.237   1.00 30.57 ? 253 THR   D CB  1 
ATOM   6035 O  OG1 . THR   D 1 160 ? -29.516 7.465   9.654   1.00 30.89 ? 253 THR   D OG1 1 
ATOM   6036 C  CG2 . THR   D 1 160 ? -28.796 6.372   7.631   1.00 29.95 ? 253 THR   D CG2 1 
ATOM   6037 N  N   . ILE   D 1 161 ? -28.357 8.937   5.476   1.00 30.32 ? 254 ILE   D N   1 
ATOM   6038 C  CA  . ILE   D 1 161 ? -28.323 8.918   3.988   1.00 30.48 ? 254 ILE   D CA  1 
ATOM   6039 C  C   . ILE   D 1 161 ? -27.787 7.548   3.578   1.00 30.37 ? 254 ILE   D C   1 
ATOM   6040 O  O   . ILE   D 1 161 ? -26.675 7.221   4.024   1.00 28.61 ? 254 ILE   D O   1 
ATOM   6041 C  CB  . ILE   D 1 161 ? -27.463 10.064  3.444   1.00 30.96 ? 254 ILE   D CB  1 
ATOM   6042 C  CG1 . ILE   D 1 161 ? -27.926 11.408  4.009   1.00 31.92 ? 254 ILE   D CG1 1 
ATOM   6043 C  CG2 . ILE   D 1 161 ? -27.439 10.040  1.912   1.00 31.77 ? 254 ILE   D CG2 1 
ATOM   6044 C  CD1 . ILE   D 1 161 ? -27.005 12.553  3.693   1.00 32.92 ? 254 ILE   D CD1 1 
ATOM   6045 N  N   . ILE   D 1 162 ? -28.612 6.766   2.869   1.00 31.20 ? 255 ILE   D N   1 
ATOM   6046 C  CA  . ILE   D 1 162 ? -28.267 5.417   2.334   1.00 31.86 ? 255 ILE   D CA  1 
ATOM   6047 C  C   . ILE   D 1 162 ? -27.992 5.603   0.845   1.00 33.08 ? 255 ILE   D C   1 
ATOM   6048 O  O   . ILE   D 1 162 ? -28.933 5.992   0.106   1.00 34.46 ? 255 ILE   D O   1 
ATOM   6049 C  CB  . ILE   D 1 162 ? -29.384 4.383   2.572   1.00 31.85 ? 255 ILE   D CB  1 
ATOM   6050 C  CG1 . ILE   D 1 162 ? -29.855 4.350   4.028   1.00 31.58 ? 255 ILE   D CG1 1 
ATOM   6051 C  CG2 . ILE   D 1 162 ? -28.948 3.004   2.082   1.00 31.73 ? 255 ILE   D CG2 1 
ATOM   6052 C  CD1 . ILE   D 1 162 ? -28.759 4.039   5.033   1.00 31.16 ? 255 ILE   D CD1 1 
ATOM   6053 N  N   A THR   D 1 163 ? -26.743 5.380   0.427   0.60 33.40 ? 256 THR   D N   1 
ATOM   6054 N  N   B THR   D 1 163 ? -26.742 5.383   0.429   0.40 33.19 ? 256 THR   D N   1 
ATOM   6055 C  CA  A THR   D 1 163 ? -26.324 5.499   -0.987  0.60 34.47 ? 256 THR   D CA  1 
ATOM   6056 C  CA  B THR   D 1 163 ? -26.277 5.528   -0.973  0.40 34.02 ? 256 THR   D CA  1 
ATOM   6057 C  C   A THR   D 1 163 ? -25.983 4.106   -1.513  0.60 34.72 ? 256 THR   D C   1 
ATOM   6058 C  C   B THR   D 1 163 ? -25.958 4.130   -1.521  0.40 34.47 ? 256 THR   D C   1 
ATOM   6059 O  O   A THR   D 1 163 ? -25.372 3.311   -0.773  0.60 34.17 ? 256 THR   D O   1 
ATOM   6060 O  O   B THR   D 1 163 ? -25.360 3.329   -0.784  0.40 34.02 ? 256 THR   D O   1 
ATOM   6061 C  CB  A THR   D 1 163 ? -25.167 6.485   -1.157  0.60 34.96 ? 256 THR   D CB  1 
ATOM   6062 C  CB  B THR   D 1 163 ? -25.118 6.531   -1.034  0.40 34.11 ? 256 THR   D CB  1 
ATOM   6063 O  OG1 A THR   D 1 163 ? -24.047 5.964   -0.445  0.60 35.08 ? 256 THR   D OG1 1 
ATOM   6064 O  OG1 B THR   D 1 163 ? -24.588 6.550   -2.356  0.40 34.78 ? 256 THR   D OG1 1 
ATOM   6065 C  CG2 A THR   D 1 163 ? -25.513 7.875   -0.667  0.60 35.52 ? 256 THR   D CG2 1 
ATOM   6066 C  CG2 B THR   D 1 163 ? -24.001 6.211   -0.070  0.40 33.64 ? 256 THR   D CG2 1 
ATOM   6067 N  N   . LEU   D 1 164 ? -26.427 3.828   -2.735  1.00 35.47 ? 257 LEU   D N   1 
ATOM   6068 C  CA  . LEU   D 1 164 ? -26.070 2.600   -3.486  1.00 36.64 ? 257 LEU   D CA  1 
ATOM   6069 C  C   . LEU   D 1 164 ? -24.944 3.004   -4.448  1.00 36.65 ? 257 LEU   D C   1 
ATOM   6070 O  O   . LEU   D 1 164 ? -25.126 3.992   -5.161  1.00 37.95 ? 257 LEU   D O   1 
ATOM   6071 C  CB  . LEU   D 1 164 ? -27.337 2.116   -4.192  1.00 38.01 ? 257 LEU   D CB  1 
ATOM   6072 C  CG  . LEU   D 1 164 ? -27.283 0.720   -4.810  1.00 39.20 ? 257 LEU   D CG  1 
ATOM   6073 C  CD1 . LEU   D 1 164 ? -27.380 -0.350  -3.743  1.00 39.50 ? 257 LEU   D CD1 1 
ATOM   6074 C  CD2 . LEU   D 1 164 ? -28.409 0.543   -5.823  1.00 41.12 ? 257 LEU   D CD2 1 
ATOM   6075 N  N   . GLU   D 1 165 ? -23.788 2.339   -4.395  1.00 36.54 ? 258 GLU   D N   1 
ATOM   6076 C  CA  . GLU   D 1 165 ? -22.638 2.652   -5.285  1.00 37.03 ? 258 GLU   D CA  1 
ATOM   6077 C  C   . GLU   D 1 165 ? -22.170 1.376   -5.982  1.00 37.12 ? 258 GLU   D C   1 
ATOM   6078 O  O   . GLU   D 1 165 ? -22.348 0.271   -5.415  1.00 35.55 ? 258 GLU   D O   1 
ATOM   6079 C  CB  . GLU   D 1 165 ? -21.458 3.304   -4.549  1.00 37.29 ? 258 GLU   D CB  1 
ATOM   6080 C  CG  . GLU   D 1 165 ? -21.629 3.420   -3.051  1.00 37.58 ? 258 GLU   D CG  1 
ATOM   6081 C  CD  . GLU   D 1 165 ? -20.454 4.063   -2.340  1.00 38.42 ? 258 GLU   D CD  1 
ATOM   6082 O  OE1 . GLU   D 1 165 ? -19.364 3.450   -2.331  1.00 39.65 ? 258 GLU   D OE1 1 
ATOM   6083 O  OE2 . GLU   D 1 165 ? -20.631 5.186   -1.820  1.00 38.93 ? 258 GLU   D OE2 1 
ATOM   6084 N  N   . ASP   D 1 166 ? -21.564 1.528   -7.159  1.00 37.82 ? 259 ASP   D N   1 
ATOM   6085 C  CA  . ASP   D 1 166 ? -20.948 0.383   -7.873  1.00 38.49 ? 259 ASP   D CA  1 
ATOM   6086 C  C   . ASP   D 1 166 ? -19.569 0.148   -7.257  1.00 38.91 ? 259 ASP   D C   1 
ATOM   6087 O  O   . ASP   D 1 166 ? -19.188 0.915   -6.343  1.00 37.44 ? 259 ASP   D O   1 
ATOM   6088 C  CB  . ASP   D 1 166 ? -20.909 0.587   -9.388  1.00 40.07 ? 259 ASP   D CB  1 
ATOM   6089 C  CG  . ASP   D 1 166 ? -19.984 1.686   -9.880  1.00 40.26 ? 259 ASP   D CG  1 
ATOM   6090 O  OD1 . ASP   D 1 166 ? -19.107 2.128   -9.108  1.00 39.51 ? 259 ASP   D OD1 1 
ATOM   6091 O  OD2 . ASP   D 1 166 ? -20.157 2.090   -11.040 1.00 41.20 ? 259 ASP   D OD2 1 
ATOM   6092 N  N   . SER   D 1 167 ? -18.856 -0.862  -7.752  1.00 40.03 ? 260 SER   D N   1 
ATOM   6093 C  CA  . SER   D 1 167 ? -17.550 -1.300  -7.209  1.00 40.36 ? 260 SER   D CA  1 
ATOM   6094 C  C   . SER   D 1 167 ? -16.523 -0.171  -7.342  1.00 41.25 ? 260 SER   D C   1 
ATOM   6095 O  O   . SER   D 1 167 ? -15.590 -0.146  -6.517  1.00 41.42 ? 260 SER   D O   1 
ATOM   6096 C  CB  . SER   D 1 167 ? -17.092 -2.565  -7.877  1.00 41.55 ? 260 SER   D CB  1 
ATOM   6097 O  OG  . SER   D 1 167 ? -16.918 -2.359  -9.265  1.00 42.79 ? 260 SER   D OG  1 
ATOM   6098 N  N   . SER   D 1 168 ? -16.700 0.740   -8.310  1.00 42.05 ? 261 SER   D N   1 
ATOM   6099 C  CA  . SER   D 1 168 ? -15.763 1.858   -8.604  1.00 42.70 ? 261 SER   D CA  1 
ATOM   6100 C  C   . SER   D 1 168 ? -16.115 3.104   -7.782  1.00 41.74 ? 261 SER   D C   1 
ATOM   6101 O  O   . SER   D 1 168 ? -15.361 4.094   -7.882  1.00 42.47 ? 261 SER   D O   1 
ATOM   6102 C  CB  . SER   D 1 168 ? -15.746 2.189   -10.079 1.00 44.18 ? 261 SER   D CB  1 
ATOM   6103 O  OG  . SER   D 1 168 ? -15.247 1.104   -10.845 1.00 44.75 ? 261 SER   D OG  1 
ATOM   6104 N  N   . GLY   D 1 169 ? -17.219 3.074   -7.028  1.00 41.51 ? 262 GLY   D N   1 
ATOM   6105 C  CA  . GLY   D 1 169 ? -17.676 4.180   -6.165  1.00 40.64 ? 262 GLY   D CA  1 
ATOM   6106 C  C   . GLY   D 1 169 ? -18.615 5.138   -6.884  1.00 41.83 ? 262 GLY   D C   1 
ATOM   6107 O  O   . GLY   D 1 169 ? -18.886 6.224   -6.330  1.00 43.14 ? 262 GLY   D O   1 
ATOM   6108 N  N   . ASN   D 1 170 ? -19.098 4.787   -8.081  1.00 42.03 ? 263 ASN   D N   1 
ATOM   6109 C  CA  . ASN   D 1 170 ? -20.067 5.627   -8.838  1.00 42.08 ? 263 ASN   D CA  1 
ATOM   6110 C  C   . ASN   D 1 170 ? -21.419 5.539   -8.130  1.00 41.04 ? 263 ASN   D C   1 
ATOM   6111 O  O   . ASN   D 1 170 ? -21.829 4.415   -7.762  1.00 40.92 ? 263 ASN   D O   1 
ATOM   6112 C  CB  . ASN   D 1 170 ? -20.158 5.245   -10.316 1.00 43.19 ? 263 ASN   D CB  1 
ATOM   6113 C  CG  . ASN   D 1 170 ? -18.849 5.436   -11.050 1.00 43.79 ? 263 ASN   D CG  1 
ATOM   6114 O  OD1 . ASN   D 1 170 ? -18.307 6.539   -11.070 1.00 43.74 ? 263 ASN   D OD1 1 
ATOM   6115 N  ND2 . ASN   D 1 170 ? -18.341 4.378   -11.665 1.00 43.99 ? 263 ASN   D ND2 1 
ATOM   6116 N  N   . LEU   D 1 171 ? -22.060 6.688   -7.900  1.00 40.60 ? 264 LEU   D N   1 
ATOM   6117 C  CA  . LEU   D 1 171 ? -23.387 6.735   -7.237  1.00 40.27 ? 264 LEU   D CA  1 
ATOM   6118 C  C   . LEU   D 1 171 ? -24.437 6.098   -8.154  1.00 40.72 ? 264 LEU   D C   1 
ATOM   6119 O  O   . LEU   D 1 171 ? -24.493 6.489   -9.309  1.00 41.95 ? 264 LEU   D O   1 
ATOM   6120 C  CB  . LEU   D 1 171 ? -23.764 8.173   -6.878  1.00 40.49 ? 264 LEU   D CB  1 
ATOM   6121 C  CG  . LEU   D 1 171 ? -24.954 8.279   -5.922  1.00 39.63 ? 264 LEU   D CG  1 
ATOM   6122 C  CD1 . LEU   D 1 171 ? -25.047 7.078   -4.997  1.00 39.25 ? 264 LEU   D CD1 1 
ATOM   6123 C  CD2 . LEU   D 1 171 ? -24.872 9.527   -5.072  1.00 39.61 ? 264 LEU   D CD2 1 
ATOM   6124 N  N   . LEU   D 1 172 ? -25.197 5.114   -7.652  1.00 39.92 ? 265 LEU   D N   1 
ATOM   6125 C  CA  . LEU   D 1 172 ? -26.312 4.441   -8.372  1.00 40.04 ? 265 LEU   D CA  1 
ATOM   6126 C  C   . LEU   D 1 172 ? -27.664 4.932   -7.842  1.00 39.80 ? 265 LEU   D C   1 
ATOM   6127 O  O   . LEU   D 1 172 ? -28.591 5.053   -8.649  1.00 41.19 ? 265 LEU   D O   1 
ATOM   6128 C  CB  . LEU   D 1 172 ? -26.204 2.928   -8.183  1.00 39.70 ? 265 LEU   D CB  1 
ATOM   6129 C  CG  . LEU   D 1 172 ? -24.855 2.293   -8.512  1.00 39.62 ? 265 LEU   D CG  1 
ATOM   6130 C  CD1 . LEU   D 1 172 ? -24.941 0.781   -8.365  1.00 39.65 ? 265 LEU   D CD1 1 
ATOM   6131 C  CD2 . LEU   D 1 172 ? -24.399 2.701   -9.906  1.00 40.72 ? 265 LEU   D CD2 1 
ATOM   6132 N  N   . GLY   D 1 173 ? -27.776 5.187   -6.541  1.00 38.86 ? 266 GLY   D N   1 
ATOM   6133 C  CA  . GLY   D 1 173 ? -29.051 5.566   -5.901  1.00 38.60 ? 266 GLY   D CA  1 
ATOM   6134 C  C   . GLY   D 1 173 ? -28.836 6.160   -4.526  1.00 37.47 ? 266 GLY   D C   1 
ATOM   6135 O  O   . GLY   D 1 173 ? -27.802 5.828   -3.890  1.00 37.00 ? 266 GLY   D O   1 
ATOM   6136 N  N   . ARG   D 1 174 ? -29.754 7.030   -4.095  1.00 37.35 ? 267 ARG   D N   1 
ATOM   6137 C  CA  . ARG   D 1 174 ? -29.693 7.655   -2.753  1.00 36.42 ? 267 ARG   D CA  1 
ATOM   6138 C  C   . ARG   D 1 174 ? -31.108 7.834   -2.197  1.00 36.51 ? 267 ARG   D C   1 
ATOM   6139 O  O   . ARG   D 1 174 ? -32.016 8.261   -2.954  1.00 36.61 ? 267 ARG   D O   1 
ATOM   6140 C  CB  . ARG   D 1 174 ? -28.965 8.996   -2.818  1.00 37.41 ? 267 ARG   D CB  1 
ATOM   6141 C  CG  . ARG   D 1 174 ? -28.724 9.639   -1.461  1.00 37.05 ? 267 ARG   D CG  1 
ATOM   6142 C  CD  . ARG   D 1 174 ? -28.335 11.103  -1.593  1.00 38.14 ? 267 ARG   D CD  1 
ATOM   6143 N  NE  . ARG   D 1 174 ? -27.070 11.253  -2.300  1.00 39.46 ? 267 ARG   D NE  1 
ATOM   6144 C  CZ  . ARG   D 1 174 ? -26.884 11.859  -3.477  1.00 40.32 ? 267 ARG   D CZ  1 
ATOM   6145 N  NH1 . ARG   D 1 174 ? -27.884 12.386  -4.152  1.00 40.98 ? 267 ARG   D NH1 1 
ATOM   6146 N  NH2 . ARG   D 1 174 ? -25.666 11.933  -3.974  1.00 41.50 ? 267 ARG   D NH2 1 
ATOM   6147 N  N   . ASN   D 1 175 ? -31.263 7.529   -0.910  1.00 35.47 ? 268 ASN   D N   1 
ATOM   6148 C  CA  . ASN   D 1 175 ? -32.473 7.844   -0.121  1.00 36.23 ? 268 ASN   D CA  1 
ATOM   6149 C  C   . ASN   D 1 175 ? -32.033 8.296   1.267   1.00 35.51 ? 268 ASN   D C   1 
ATOM   6150 O  O   . ASN   D 1 175 ? -30.811 8.247   1.559   1.00 36.71 ? 268 ASN   D O   1 
ATOM   6151 C  CB  . ASN   D 1 175 ? -33.436 6.653   -0.047  1.00 37.07 ? 268 ASN   D CB  1 
ATOM   6152 C  CG  . ASN   D 1 175 ? -34.852 7.051   -0.400  1.00 38.70 ? 268 ASN   D CG  1 
ATOM   6153 O  OD1 . ASN   D 1 175 ? -35.204 7.046   -1.578  1.00 40.74 ? 268 ASN   D OD1 1 
ATOM   6154 N  ND2 . ASN   D 1 175 ? -35.663 7.435   0.582   1.00 39.35 ? 268 ASN   D ND2 1 
ATOM   6155 N  N   . SER   D 1 176 ? -32.990 8.736   2.079   1.00 34.53 ? 269 SER   D N   1 
ATOM   6156 C  CA  . SER   D 1 176 ? -32.734 9.299   3.419   1.00 33.29 ? 269 SER   D CA  1 
ATOM   6157 C  C   . SER   D 1 176 ? -33.972 9.108   4.298   1.00 33.05 ? 269 SER   D C   1 
ATOM   6158 O  O   . SER   D 1 176 ? -35.087 8.907   3.765   1.00 33.09 ? 269 SER   D O   1 
ATOM   6159 C  CB  . SER   D 1 176 ? -32.364 10.740  3.305   1.00 33.95 ? 269 SER   D CB  1 
ATOM   6160 O  OG  . SER   D 1 176 ? -33.419 11.467  2.683   1.00 35.41 ? 269 SER   D OG  1 
ATOM   6161 N  N   . PHE   D 1 177 ? -33.757 9.143   5.607   1.00 32.37 ? 270 PHE   D N   1 
ATOM   6162 C  CA  . PHE   D 1 177 ? -34.820 9.127   6.639   1.00 32.61 ? 270 PHE   D CA  1 
ATOM   6163 C  C   . PHE   D 1 177 ? -34.250 9.801   7.882   1.00 32.84 ? 270 PHE   D C   1 
ATOM   6164 O  O   . PHE   D 1 177 ? -33.032 9.659   8.143   1.00 33.45 ? 270 PHE   D O   1 
ATOM   6165 C  CB  . PHE   D 1 177 ? -35.299 7.693   6.894   1.00 31.34 ? 270 PHE   D CB  1 
ATOM   6166 C  CG  . PHE   D 1 177 ? -34.220 6.710   7.256   1.00 30.20 ? 270 PHE   D CG  1 
ATOM   6167 C  CD1 . PHE   D 1 177 ? -33.492 6.060   6.267   1.00 30.19 ? 270 PHE   D CD1 1 
ATOM   6168 C  CD2 . PHE   D 1 177 ? -33.940 6.416   8.580   1.00 29.53 ? 270 PHE   D CD2 1 
ATOM   6169 C  CE1 . PHE   D 1 177 ? -32.522 5.126   6.601   1.00 29.71 ? 270 PHE   D CE1 1 
ATOM   6170 C  CE2 . PHE   D 1 177 ? -32.958 5.495   8.908   1.00 29.07 ? 270 PHE   D CE2 1 
ATOM   6171 C  CZ  . PHE   D 1 177 ? -32.250 4.855   7.924   1.00 28.84 ? 270 PHE   D CZ  1 
ATOM   6172 N  N   . GLU   D 1 178 ? -35.095 10.550  8.590   1.00 34.57 ? 271 GLU   D N   1 
ATOM   6173 C  CA  . GLU   D 1 178 ? -34.763 11.146  9.906   1.00 34.88 ? 271 GLU   D CA  1 
ATOM   6174 C  C   . GLU   D 1 178 ? -34.648 9.995   10.907  1.00 34.53 ? 271 GLU   D C   1 
ATOM   6175 O  O   . GLU   D 1 178 ? -35.316 8.966   10.706  1.00 33.59 ? 271 GLU   D O   1 
ATOM   6176 C  CB  . GLU   D 1 178 ? -35.817 12.179  10.308  1.00 36.07 ? 271 GLU   D CB  1 
ATOM   6177 C  CG  . GLU   D 1 178 ? -35.398 13.013  11.500  1.00 36.82 ? 271 GLU   D CG  1 
ATOM   6178 C  CD  . GLU   D 1 178 ? -36.278 14.221  11.800  0.80 37.77 ? 271 GLU   D CD  1 
ATOM   6179 O  OE1 . GLU   D 1 178 ? -36.256 14.698  12.957  0.80 38.06 ? 271 GLU   D OE1 1 
ATOM   6180 O  OE2 . GLU   D 1 178 ? -36.972 14.699  10.883  0.80 38.83 ? 271 GLU   D OE2 1 
ATOM   6181 N  N   A VAL   D 1 179 ? -33.797 10.163  11.921  0.50 34.81 ? 272 VAL   D N   1 
ATOM   6182 N  N   B VAL   D 1 179 ? -33.816 10.140  11.942  0.50 34.87 ? 272 VAL   D N   1 
ATOM   6183 C  CA  A VAL   D 1 179 ? -33.559 9.163   13.002  0.50 34.91 ? 272 VAL   D CA  1 
ATOM   6184 C  CA  B VAL   D 1 179 ? -33.649 9.104   13.004  0.50 35.06 ? 272 VAL   D CA  1 
ATOM   6185 C  C   A VAL   D 1 179 ? -33.609 9.885   14.349  0.50 35.92 ? 272 VAL   D C   1 
ATOM   6186 C  C   B VAL   D 1 179 ? -33.538 9.791   14.362  0.50 35.96 ? 272 VAL   D C   1 
ATOM   6187 O  O   A VAL   D 1 179 ? -33.024 10.987  14.472  0.50 36.07 ? 272 VAL   D O   1 
ATOM   6188 O  O   B VAL   D 1 179 ? -32.758 10.745  14.508  0.50 36.14 ? 272 VAL   D O   1 
ATOM   6189 C  CB  A VAL   D 1 179 ? -32.229 8.404   12.817  0.50 34.48 ? 272 VAL   D CB  1 
ATOM   6190 C  CB  B VAL   D 1 179 ? -32.445 8.173   12.765  0.50 34.67 ? 272 VAL   D CB  1 
ATOM   6191 C  CG1 A VAL   D 1 179 ? -31.936 7.474   13.989  0.50 34.24 ? 272 VAL   D CG1 1 
ATOM   6192 C  CG1 B VAL   D 1 179 ? -32.568 7.416   11.457  0.50 34.37 ? 272 VAL   D CG1 1 
ATOM   6193 C  CG2 A VAL   D 1 179 ? -32.204 7.623   11.516  0.50 34.11 ? 272 VAL   D CG2 1 
ATOM   6194 C  CG2 B VAL   D 1 179 ? -31.126 8.917   12.824  0.50 34.57 ? 272 VAL   D CG2 1 
ATOM   6195 N  N   . ARG   D 1 180 ? -34.321 9.294   15.310  1.00 35.97 ? 273 ARG   D N   1 
ATOM   6196 C  CA  . ARG   D 1 180 ? -34.254 9.682   16.731  1.00 37.17 ? 273 ARG   D CA  1 
ATOM   6197 C  C   . ARG   D 1 180 ? -33.821 8.436   17.493  1.00 36.70 ? 273 ARG   D C   1 
ATOM   6198 O  O   . ARG   D 1 180 ? -34.523 7.415   17.367  1.00 36.04 ? 273 ARG   D O   1 
ATOM   6199 C  CB  . ARG   D 1 180 ? -35.624 10.186  17.188  1.00 39.18 ? 273 ARG   D CB  1 
ATOM   6200 C  CG  . ARG   D 1 180 ? -35.621 11.404  18.096  1.00 41.20 ? 273 ARG   D CG  1 
ATOM   6201 C  CD  . ARG   D 1 180 ? -35.962 10.974  19.490  1.00 43.03 ? 273 ARG   D CD  1 
ATOM   6202 N  NE  . ARG   D 1 180 ? -36.819 11.956  20.126  1.00 44.77 ? 273 ARG   D NE  1 
ATOM   6203 C  CZ  . ARG   D 1 180 ? -37.700 11.670  21.065  1.00 46.72 ? 273 ARG   D CZ  1 
ATOM   6204 N  NH1 . ARG   D 1 180 ? -37.829 10.426  21.486  1.00 46.99 ? 273 ARG   D NH1 1 
ATOM   6205 N  NH2 . ARG   D 1 180 ? -38.439 12.626  21.597  1.00 48.28 ? 273 ARG   D NH2 1 
ATOM   6206 N  N   . VAL   D 1 181 ? -32.705 8.510   18.216  1.00 35.95 ? 274 VAL   D N   1 
ATOM   6207 C  CA  . VAL   D 1 181 ? -32.251 7.419   19.120  1.00 36.63 ? 274 VAL   D CA  1 
ATOM   6208 C  C   . VAL   D 1 181 ? -32.711 7.808   20.524  1.00 38.39 ? 274 VAL   D C   1 
ATOM   6209 O  O   . VAL   D 1 181 ? -32.301 8.888   20.990  1.00 39.19 ? 274 VAL   D O   1 
ATOM   6210 C  CB  . VAL   D 1 181 ? -30.731 7.190   19.030  1.00 35.91 ? 274 VAL   D CB  1 
ATOM   6211 C  CG1 . VAL   D 1 181 ? -30.332 5.882   19.705  1.00 36.10 ? 274 VAL   D CG1 1 
ATOM   6212 C  CG2 . VAL   D 1 181 ? -30.240 7.209   17.583  1.00 34.78 ? 274 VAL   D CG2 1 
ATOM   6213 N  N   . CYS   D 1 182 ? -33.589 7.003   21.131  1.00 39.27 ? 275 CYS   D N   1 
ATOM   6214 C  CA  . CYS   D 1 182 ? -34.286 7.348   22.396  1.00 41.65 ? 275 CYS   D CA  1 
ATOM   6215 C  C   . CYS   D 1 182 ? -34.605 6.084   23.194  1.00 41.64 ? 275 CYS   D C   1 
ATOM   6216 O  O   . CYS   D 1 182 ? -34.527 4.974   22.607  1.00 41.44 ? 275 CYS   D O   1 
ATOM   6217 C  CB  . CYS   D 1 182 ? -35.557 8.147   22.118  1.00 42.76 ? 275 CYS   D CB  1 
ATOM   6218 S  SG  . CYS   D 1 182 ? -36.682 7.393   20.916  1.00 43.91 ? 275 CYS   D SG  1 
ATOM   6219 N  N   . ALA   D 1 183 ? -34.967 6.259   24.471  1.00 43.46 ? 276 ALA   D N   1 
ATOM   6220 C  CA  . ALA   D 1 183 ? -35.265 5.170   25.429  1.00 43.96 ? 276 ALA   D CA  1 
ATOM   6221 C  C   . ALA   D 1 183 ? -36.548 4.442   25.018  1.00 43.81 ? 276 ALA   D C   1 
ATOM   6222 O  O   . ALA   D 1 183 ? -36.587 3.201   25.147  1.00 45.28 ? 276 ALA   D O   1 
ATOM   6223 C  CB  . ALA   D 1 183 ? -35.380 5.725   26.824  1.00 45.73 ? 276 ALA   D CB  1 
ATOM   6224 N  N   . CYS   D 1 184 ? -37.561 5.182   24.558  1.00 43.12 ? 277 CYS   D N   1 
ATOM   6225 C  CA  . CYS   D 1 184 ? -38.939 4.661   24.340  1.00 42.92 ? 277 CYS   D CA  1 
ATOM   6226 C  C   . CYS   D 1 184 ? -39.419 5.035   22.938  1.00 41.65 ? 277 CYS   D C   1 
ATOM   6227 O  O   . CYS   D 1 184 ? -40.176 5.987   22.777  1.00 42.05 ? 277 CYS   D O   1 
ATOM   6228 C  CB  . CYS   D 1 184 ? -39.890 5.192   25.411  1.00 44.24 ? 277 CYS   D CB  1 
ATOM   6229 S  SG  . CYS   D 1 184 ? -41.280 4.077   25.727  1.00 44.99 ? 277 CYS   D SG  1 
ATOM   6230 N  N   . PRO   D 1 185 ? -38.983 4.311   21.888  1.00 39.51 ? 278 PRO   D N   1 
ATOM   6231 C  CA  . PRO   D 1 185 ? -39.336 4.650   20.506  1.00 39.03 ? 278 PRO   D CA  1 
ATOM   6232 C  C   . PRO   D 1 185 ? -40.847 4.642   20.216  1.00 39.56 ? 278 PRO   D C   1 
ATOM   6233 O  O   . PRO   D 1 185 ? -41.331 5.560   19.563  1.00 39.16 ? 278 PRO   D O   1 
ATOM   6234 C  CB  . PRO   D 1 185 ? -38.665 3.545   19.668  1.00 37.99 ? 278 PRO   D CB  1 
ATOM   6235 C  CG  . PRO   D 1 185 ? -37.591 2.981   20.551  1.00 37.89 ? 278 PRO   D CG  1 
ATOM   6236 C  CD  . PRO   D 1 185 ? -38.117 3.124   21.970  1.00 39.17 ? 278 PRO   D CD  1 
ATOM   6237 N  N   . GLY   D 1 186 ? -41.553 3.624   20.713  1.00 40.47 ? 279 GLY   D N   1 
ATOM   6238 C  CA  . GLY   D 1 186 ? -43.021 3.519   20.622  1.00 41.60 ? 279 GLY   D CA  1 
ATOM   6239 C  C   . GLY   D 1 186 ? -43.715 4.780   21.122  1.00 43.13 ? 279 GLY   D C   1 
ATOM   6240 O  O   . GLY   D 1 186 ? -44.504 5.387   20.347  1.00 41.81 ? 279 GLY   D O   1 
ATOM   6241 N  N   . ARG   D 1 187 ? -43.404 5.192   22.356  1.00 44.53 ? 280 ARG   D N   1 
ATOM   6242 C  CA  . ARG   D 1 187 ? -44.018 6.377   23.010  1.00 46.39 ? 280 ARG   D CA  1 
ATOM   6243 C  C   . ARG   D 1 187 ? -43.633 7.637   22.227  1.00 44.92 ? 280 ARG   D C   1 
ATOM   6244 O  O   . ARG   D 1 187 ? -44.489 8.487   22.004  1.00 45.45 ? 280 ARG   D O   1 
ATOM   6245 C  CB  . ARG   D 1 187 ? -43.570 6.508   24.477  1.00 48.87 ? 280 ARG   D CB  1 
ATOM   6246 C  CG  . ARG   D 1 187 ? -44.269 7.627   25.250  1.00 51.39 ? 280 ARG   D CG  1 
ATOM   6247 C  CD  . ARG   D 1 187 ? -43.348 8.527   26.081  1.00 53.76 ? 280 ARG   D CD  1 
ATOM   6248 N  NE  . ARG   D 1 187 ? -42.468 7.767   26.965  1.00 54.79 ? 280 ARG   D NE  1 
ATOM   6249 C  CZ  . ARG   D 1 187 ? -41.257 8.150   27.375  1.00 56.05 ? 280 ARG   D CZ  1 
ATOM   6250 N  NH1 . ARG   D 1 187 ? -40.742 9.314   27.006  1.00 56.25 ? 280 ARG   D NH1 1 
ATOM   6251 N  NH2 . ARG   D 1 187 ? -40.567 7.370   28.190  1.00 56.77 ? 280 ARG   D NH2 1 
ATOM   6252 N  N   . ASP   D 1 188 ? -42.365 7.768   21.846  1.00 43.66 ? 281 ASP   D N   1 
ATOM   6253 C  CA  . ASP   D 1 188 ? -41.835 8.990   21.185  1.00 42.66 ? 281 ASP   D CA  1 
ATOM   6254 C  C   . ASP   D 1 188 ? -42.431 9.107   19.775  1.00 41.13 ? 281 ASP   D C   1 
ATOM   6255 O  O   . ASP   D 1 188 ? -42.760 10.239  19.374  1.00 40.81 ? 281 ASP   D O   1 
ATOM   6256 C  CB  . ASP   D 1 188 ? -40.310 9.005   21.232  1.00 42.68 ? 281 ASP   D CB  1 
ATOM   6257 C  CG  . ASP   D 1 188 ? -39.749 9.185   22.647  1.00 44.24 ? 281 ASP   D CG  1 
ATOM   6258 O  OD1 . ASP   D 1 188 ? -40.531 9.429   23.581  1.00 45.54 ? 281 ASP   D OD1 1 
ATOM   6259 O  OD2 . ASP   D 1 188 ? -38.517 9.069   22.818  1.00 45.62 ? 281 ASP   D OD2 1 
ATOM   6260 N  N   . ARG   D 1 189 ? -42.598 7.997   19.046  1.00 39.29 ? 282 ARG   D N   1 
ATOM   6261 C  CA  . ARG   D 1 189 ? -43.288 8.022   17.726  1.00 38.91 ? 282 ARG   D CA  1 
ATOM   6262 C  C   . ARG   D 1 189 ? -44.729 8.522   17.917  1.00 40.20 ? 282 ARG   D C   1 
ATOM   6263 O  O   . ARG   D 1 189 ? -45.129 9.460   17.200  1.00 40.62 ? 282 ARG   D O   1 
ATOM   6264 C  CB  . ARG   D 1 189 ? -43.263 6.653   17.031  1.00 37.36 ? 282 ARG   D CB  1 
ATOM   6265 C  CG  . ARG   D 1 189 ? -44.057 6.643   15.733  1.00 37.12 ? 282 ARG   D CG  1 
ATOM   6266 C  CD  . ARG   D 1 189 ? -43.876 5.399   14.883  1.00 36.48 ? 282 ARG   D CD  1 
ATOM   6267 N  NE  . ARG   D 1 189 ? -44.961 5.321   13.924  1.00 36.83 ? 282 ARG   D NE  1 
ATOM   6268 C  CZ  . ARG   D 1 189 ? -45.409 4.206   13.352  1.00 36.71 ? 282 ARG   D CZ  1 
ATOM   6269 N  NH1 . ARG   D 1 189 ? -44.865 3.026   13.626  1.00 36.42 ? 282 ARG   D NH1 1 
ATOM   6270 N  NH2 . ARG   D 1 189 ? -46.419 4.290   12.503  1.00 37.40 ? 282 ARG   D NH2 1 
ATOM   6271 N  N   . ARG   D 1 190 ? -45.480 7.926   18.845  1.00 41.00 ? 283 ARG   D N   1 
ATOM   6272 C  CA  . ARG   D 1 190 ? -46.897 8.290   19.134  1.00 42.53 ? 283 ARG   D CA  1 
ATOM   6273 C  C   . ARG   D 1 190 ? -47.000 9.788   19.447  1.00 44.03 ? 283 ARG   D C   1 
ATOM   6274 O  O   . ARG   D 1 190 ? -47.861 10.478  18.860  1.00 44.52 ? 283 ARG   D O   1 
ATOM   6275 C  CB  . ARG   D 1 190 ? -47.434 7.500   20.332  1.00 43.19 ? 283 ARG   D CB  1 
ATOM   6276 C  CG  . ARG   D 1 190 ? -48.410 6.408   19.961  1.00 43.16 ? 283 ARG   D CG  1 
ATOM   6277 C  CD  . ARG   D 1 190 ? -48.973 5.735   21.196  1.00 44.23 ? 283 ARG   D CD  1 
ATOM   6278 N  NE  . ARG   D 1 190 ? -48.801 4.298   21.089  1.00 43.80 ? 283 ARG   D NE  1 
ATOM   6279 C  CZ  . ARG   D 1 190 ? -49.101 3.419   22.035  1.00 44.53 ? 283 ARG   D CZ  1 
ATOM   6280 N  NH1 . ARG   D 1 190 ? -48.886 2.131   21.828  1.00 44.36 ? 283 ARG   D NH1 1 
ATOM   6281 N  NH2 . ARG   D 1 190 ? -49.582 3.831   23.189  1.00 46.52 ? 283 ARG   D NH2 1 
ATOM   6282 N  N   . THR   D 1 191 ? -46.132 10.277  20.334  1.00 44.45 ? 284 THR   D N   1 
ATOM   6283 C  CA  . THR   D 1 191 ? -46.092 11.690  20.797  1.00 45.94 ? 284 THR   D CA  1 
ATOM   6284 C  C   . THR   D 1 191 ? -45.830 12.598  19.588  1.00 45.77 ? 284 THR   D C   1 
ATOM   6285 O  O   . THR   D 1 191 ? -46.578 13.560  19.409  1.00 46.97 ? 284 THR   D O   1 
ATOM   6286 C  CB  . THR   D 1 191 ? -45.054 11.837  21.918  1.00 45.91 ? 284 THR   D CB  1 
ATOM   6287 O  OG1 . THR   D 1 191 ? -45.432 10.905  22.931  1.00 46.80 ? 284 THR   D OG1 1 
ATOM   6288 C  CG2 . THR   D 1 191 ? -44.956 13.232  22.494  1.00 47.02 ? 284 THR   D CG2 1 
ATOM   6289 N  N   . GLU   D 1 192 ? -44.829 12.276  18.765  1.00 45.71 ? 285 GLU   D N   1 
ATOM   6290 C  CA  . GLU   D 1 192 ? -44.410 13.134  17.629  1.00 46.60 ? 285 GLU   D CA  1 
ATOM   6291 C  C   . GLU   D 1 192 ? -45.486 13.146  16.539  1.00 47.66 ? 285 GLU   D C   1 
ATOM   6292 O  O   . GLU   D 1 192 ? -45.657 14.214  15.917  1.00 48.73 ? 285 GLU   D O   1 
ATOM   6293 C  CB  . GLU   D 1 192 ? -43.052 12.695  17.097  1.00 45.58 ? 285 GLU   D CB  1 
ATOM   6294 C  CG  . GLU   D 1 192 ? -41.900 13.150  17.987  1.00 45.97 ? 285 GLU   D CG  1 
ATOM   6295 C  CD  . GLU   D 1 192 ? -40.568 13.324  17.284  1.00 45.47 ? 285 GLU   D CD  1 
ATOM   6296 O  OE1 . GLU   D 1 192 ? -40.574 13.569  16.058  1.00 45.04 ? 285 GLU   D OE1 1 
ATOM   6297 O  OE2 . GLU   D 1 192 ? -39.524 13.211  17.967  1.00 46.15 ? 285 GLU   D OE2 1 
ATOM   6298 N  N   . GLU   D 1 193 ? -46.217 12.041  16.347  1.00 48.48 ? 286 GLU   D N   1 
ATOM   6299 C  CA  . GLU   D 1 193 ? -47.309 11.942  15.332  1.00 49.27 ? 286 GLU   D CA  1 
ATOM   6300 C  C   . GLU   D 1 193 ? -48.530 12.769  15.776  1.00 51.64 ? 286 GLU   D C   1 
ATOM   6301 O  O   . GLU   D 1 193 ? -49.206 13.344  14.892  1.00 52.03 ? 286 GLU   D O   1 
ATOM   6302 C  CB  . GLU   D 1 193 ? -47.655 10.476  15.041  1.00 48.59 ? 286 GLU   D CB  1 
ATOM   6303 C  CG  . GLU   D 1 193 ? -46.711 9.846   14.031  1.00 47.28 ? 286 GLU   D CG  1 
ATOM   6304 C  CD  . GLU   D 1 193 ? -46.769 8.336   13.849  1.00 47.48 ? 286 GLU   D CD  1 
ATOM   6305 O  OE1 . GLU   D 1 193 ? -47.564 7.684   14.541  1.00 49.15 ? 286 GLU   D OE1 1 
ATOM   6306 O  OE2 . GLU   D 1 193 ? -46.008 7.810   13.003  1.00 47.04 ? 286 GLU   D OE2 1 
ATOM   6307 N  N   . GLU   D 1 194 ? -48.803 12.864  17.081  1.00 53.45 ? 287 GLU   D N   1 
ATOM   6308 C  CA  . GLU   D 1 194 ? -50.006 13.583  17.590  1.00 55.74 ? 287 GLU   D CA  1 
ATOM   6309 C  C   . GLU   D 1 194 ? -49.871 15.078  17.266  1.00 56.24 ? 287 GLU   D C   1 
ATOM   6310 O  O   . GLU   D 1 194 ? -50.906 15.753  17.245  1.00 56.32 ? 287 GLU   D O   1 
ATOM   6311 C  CB  . GLU   D 1 194 ? -50.291 13.271  19.063  1.00 57.82 ? 287 GLU   D CB  1 
ATOM   6312 C  CG  . GLU   D 1 194 ? -49.525 14.102  20.077  1.00 58.87 ? 287 GLU   D CG  1 
ATOM   6313 C  CD  . GLU   D 1 194 ? -49.947 13.829  21.510  1.00 60.21 ? 287 GLU   D CD  1 
ATOM   6314 O  OE1 . GLU   D 1 194 ? -49.055 13.683  22.383  1.00 60.69 ? 287 GLU   D OE1 1 
ATOM   6315 O  OE2 . GLU   D 1 194 ? -51.168 13.750  21.751  1.00 62.80 ? 287 GLU   D OE2 1 
ATOM   6316 N  N   . ASN   D 1 195 ? -48.654 15.553  16.973  1.00 55.42 ? 288 ASN   D N   1 
ATOM   6317 C  CA  . ASN   D 1 195 ? -48.375 16.916  16.442  1.00 56.67 ? 288 ASN   D CA  1 
ATOM   6318 C  C   . ASN   D 1 195 ? -48.747 16.981  14.951  1.00 56.42 ? 288 ASN   D C   1 
ATOM   6319 O  O   . ASN   D 1 195 ? -47.828 16.947  14.119  1.00 55.20 ? 288 ASN   D O   1 
ATOM   6320 C  CB  . ASN   D 1 195 ? -46.911 17.323  16.660  1.00 55.87 ? 288 ASN   D CB  1 
ATOM   6321 C  CG  . ASN   D 1 195 ? -46.487 17.280  18.112  1.00 56.25 ? 288 ASN   D CG  1 
ATOM   6322 O  OD1 . ASN   D 1 195 ? -47.307 17.050  18.999  1.00 58.48 ? 288 ASN   D OD1 1 
ATOM   6323 N  ND2 . ASN   D 1 195 ? -45.203 17.468  18.366  1.00 55.38 ? 288 ASN   D ND2 1 
ATOM   6324 N  N   . LEU   D 1 196 ? -50.051 17.087  14.660  1.00 58.05 ? 289 LEU   D N   1 
ATOM   6325 C  CA  . LEU   D 1 196 ? -50.698 17.177  13.315  1.00 58.67 ? 289 LEU   D CA  1 
ATOM   6326 C  C   . LEU   D 1 196 ? -51.644 15.984  13.132  1.00 58.23 ? 289 LEU   D C   1 
ATOM   6327 O  O   . LEU   D 1 196 ? -52.790 16.024  13.573  1.00 59.61 ? 289 LEU   D O   1 
ATOM   6328 C  CB  . LEU   D 1 196 ? -49.664 17.229  12.182  1.00 57.46 ? 289 LEU   D CB  1 
ATOM   6329 C  CG  . LEU   D 1 196 ? -49.049 18.601  11.900  1.00 58.16 ? 289 LEU   D CG  1 
ATOM   6330 C  CD1 . LEU   D 1 196 ? -47.969 18.505  10.829  1.00 57.24 ? 289 LEU   D CD1 1 
ATOM   6331 C  CD2 . LEU   D 1 196 ? -50.114 19.611  11.488  1.00 60.06 ? 289 LEU   D CD2 1 
HETATM 6332 ZN ZN  . ZN    E 2 .   ? 10.774  -7.600  -5.066  1.00 40.39 ? 301 ZN    A ZN  1 
HETATM 6333 ZN ZN  . ZN    F 2 .   ? 8.354   -2.315  35.706  1.00 45.63 ? 301 ZN    B ZN  1 
HETATM 6334 ZN ZN  . ZN    G 2 .   ? -26.079 4.485   67.480  1.00 39.31 ? 301 ZN    C ZN  1 
HETATM 6335 ZN ZN  . ZN    H 2 .   ? -23.645 9.427   23.578  1.00 43.71 ? 301 ZN    D ZN  1 
HETATM 6336 N  N1  . A1LU0 I 3 .   ? -24.566 2.409   26.303  1.00 49.66 ? 302 A1LU0 D N1  1 
HETATM 6337 C  C4  . A1LU0 I 3 .   ? -24.649 1.214   25.533  1.00 48.28 ? 302 A1LU0 D C4  1 
HETATM 6338 C  C5  . A1LU0 I 3 .   ? -23.617 0.879   24.662  1.00 47.46 ? 302 A1LU0 D C5  1 
HETATM 6339 C  C6  . A1LU0 I 3 .   ? -23.643 -0.318  23.967  1.00 46.79 ? 302 A1LU0 D C6  1 
HETATM 6340 C  C7  . A1LU0 I 3 .   ? -26.859 -1.771  25.153  1.00 48.13 ? 302 A1LU0 D C7  1 
HETATM 6341 C  C8  . A1LU0 I 3 .   ? -27.879 -2.370  25.252  1.00 48.55 ? 302 A1LU0 D C8  1 
HETATM 6342 C  C10 . A1LU0 I 3 .   ? -21.991 2.020   29.070  1.00 57.45 ? 302 A1LU0 D C10 1 
HETATM 6343 C  C13 . A1LU0 I 3 .   ? -19.972 0.676   28.907  1.00 61.20 ? 302 A1LU0 D C13 1 
HETATM 6344 C  C1  . A1LU0 I 3 .   ? -24.701 -1.188  24.124  1.00 46.91 ? 302 A1LU0 D C1  1 
HETATM 6345 C  C2  . A1LU0 I 3 .   ? -25.735 -0.876  25.006  1.00 47.49 ? 302 A1LU0 D C2  1 
HETATM 6346 C  C3  . A1LU0 I 3 .   ? -25.697 0.324   25.720  1.00 48.00 ? 302 A1LU0 D C3  1 
HETATM 6347 C  C9  . A1LU0 I 3 .   ? -23.706 2.409   27.245  1.00 52.57 ? 302 A1LU0 D C9  1 
HETATM 6348 S  S   . A1LU0 I 3 .   ? -22.507 1.163   27.562  1.00 54.07 ? 302 A1LU0 D S   1 
HETATM 6349 C  C11 . A1LU0 I 3 .   ? -22.622 3.369   29.052  1.00 56.64 ? 302 A1LU0 D C11 1 
HETATM 6350 N  N2  . A1LU0 I 3 .   ? -23.657 3.414   28.151  1.00 54.62 ? 302 A1LU0 D N2  1 
HETATM 6351 O  O1  . A1LU0 I 3 .   ? -22.236 4.277   29.774  1.00 59.07 ? 302 A1LU0 D O1  1 
HETATM 6352 C  C12 . A1LU0 I 3 .   ? -20.481 2.115   29.091  1.00 59.79 ? 302 A1LU0 D C12 1 
HETATM 6353 O  O2  . A1LU0 I 3 .   ? -19.660 0.081   29.953  1.00 63.32 ? 302 A1LU0 D O2  1 
HETATM 6354 O  O3  . A1LU0 I 3 .   ? -19.962 0.160   27.767  1.00 61.37 ? 302 A1LU0 D O3  1 
HETATM 6355 O  O   . HOH   J 4 .   ? 4.647   0.751   1.447   1.00 25.70 ? 401 HOH   A O   1 
HETATM 6356 O  O   . HOH   J 4 .   ? -0.672  10.011  15.005  1.00 28.54 ? 402 HOH   A O   1 
HETATM 6357 O  O   . HOH   J 4 .   ? 13.198  7.875   7.015   1.00 27.69 ? 403 HOH   A O   1 
HETATM 6358 O  O   . HOH   J 4 .   ? 12.938  -11.829 9.153   1.00 31.60 ? 404 HOH   A O   1 
HETATM 6359 O  O   . HOH   J 4 .   ? 17.358  -6.759  13.203  1.00 28.35 ? 405 HOH   A O   1 
HETATM 6360 O  O   . HOH   J 4 .   ? 10.692  -15.421 9.067   1.00 29.26 ? 406 HOH   A O   1 
HETATM 6361 O  O   . HOH   J 4 .   ? -7.208  7.182   5.232   1.00 30.40 ? 407 HOH   A O   1 
HETATM 6362 O  O   . HOH   J 4 .   ? 10.015  -5.598  16.083  1.00 22.45 ? 408 HOH   A O   1 
HETATM 6363 O  O   . HOH   J 4 .   ? 14.012  -7.224  5.204   1.00 25.88 ? 409 HOH   A O   1 
HETATM 6364 O  O   . HOH   J 4 .   ? 18.973  -1.626  16.230  1.00 27.24 ? 410 HOH   A O   1 
HETATM 6365 O  O   . HOH   J 4 .   ? 14.125  -9.673  8.110   1.00 25.44 ? 411 HOH   A O   1 
HETATM 6366 O  O   . HOH   J 4 .   ? 23.128  0.729   12.141  1.00 24.31 ? 412 HOH   A O   1 
HETATM 6367 O  O   . HOH   J 4 .   ? -1.134  -7.742  18.174  1.00 35.37 ? 413 HOH   A O   1 
HETATM 6368 O  O   . HOH   J 4 .   ? -7.390  0.847   14.492  1.00 40.53 ? 414 HOH   A O   1 
HETATM 6369 O  O   . HOH   J 4 .   ? 16.649  -22.593 7.748   1.00 40.39 ? 415 HOH   A O   1 
HETATM 6370 O  O   . HOH   J 4 .   ? 21.148  3.129   27.075  1.00 36.78 ? 416 HOH   A O   1 
HETATM 6371 O  O   . HOH   K 4 .   ? 7.711   -14.436 46.414  1.00 34.15 ? 401 HOH   B O   1 
HETATM 6372 O  O   . HOH   K 4 .   ? 4.132   -17.151 53.442  1.00 34.52 ? 402 HOH   B O   1 
HETATM 6373 O  O   . HOH   K 4 .   ? -5.477  0.089   34.442  1.00 41.80 ? 403 HOH   B O   1 
HETATM 6374 O  O   . HOH   K 4 .   ? 11.176  -5.176  45.469  1.00 29.25 ? 404 HOH   B O   1 
HETATM 6375 O  O   . HOH   K 4 .   ? 9.536   -6.614  48.888  1.00 27.07 ? 405 HOH   B O   1 
HETATM 6376 O  O   . HOH   K 4 .   ? 9.818   -11.169 47.805  1.00 28.53 ? 406 HOH   B O   1 
HETATM 6377 O  O   . HOH   K 4 .   ? 14.172  -7.711  53.309  1.00 30.14 ? 407 HOH   B O   1 
HETATM 6378 O  O   . HOH   K 4 .   ? -11.928 7.014   53.872  1.00 22.27 ? 408 HOH   B O   1 
HETATM 6379 O  O   . HOH   K 4 .   ? -5.660  -5.850  55.783  1.00 34.59 ? 409 HOH   B O   1 
HETATM 6380 O  O   . HOH   K 4 .   ? 14.747  3.603   43.994  1.00 43.59 ? 410 HOH   B O   1 
HETATM 6381 O  O   . HOH   K 4 .   ? 20.045  -0.253  54.796  1.00 24.51 ? 411 HOH   B O   1 
HETATM 6382 O  O   . HOH   K 4 .   ? -18.636 -4.845  40.434  1.00 32.81 ? 412 HOH   B O   1 
HETATM 6383 O  O   . HOH   K 4 .   ? 15.347  -5.395  40.019  1.00 35.56 ? 413 HOH   B O   1 
HETATM 6384 O  O   . HOH   K 4 .   ? -10.272 0.165   56.002  1.00 31.53 ? 414 HOH   B O   1 
HETATM 6385 O  O   . HOH   K 4 .   ? 11.102  -2.376  49.407  1.00 22.20 ? 415 HOH   B O   1 
HETATM 6386 O  O   . HOH   K 4 .   ? 9.494   10.927  49.551  1.00 31.72 ? 416 HOH   B O   1 
HETATM 6387 O  O   . HOH   K 4 .   ? 6.247   -11.470 58.514  1.00 37.16 ? 417 HOH   B O   1 
HETATM 6388 O  O   . HOH   K 4 .   ? 12.932  1.687   43.862  1.00 38.95 ? 418 HOH   B O   1 
HETATM 6389 O  O   . HOH   K 4 .   ? 4.598   8.100   54.538  1.00 27.91 ? 419 HOH   B O   1 
HETATM 6390 O  O   . HOH   K 4 .   ? -16.297 -0.437  49.611  1.00 28.27 ? 420 HOH   B O   1 
HETATM 6391 O  O   . HOH   K 4 .   ? 9.491   5.614   69.688  1.00 34.00 ? 421 HOH   B O   1 
HETATM 6392 O  O   . HOH   K 4 .   ? 11.077  -8.844  47.821  1.00 21.00 ? 422 HOH   B O   1 
HETATM 6393 O  O   . HOH   K 4 .   ? 6.874   -7.282  56.546  1.00 28.49 ? 423 HOH   B O   1 
HETATM 6394 O  O   . HOH   K 4 .   ? -16.217 0.717   34.970  1.00 37.89 ? 424 HOH   B O   1 
HETATM 6395 O  O   . HOH   K 4 .   ? -9.136  -5.969  31.323  1.00 43.47 ? 425 HOH   B O   1 
HETATM 6396 O  O   . HOH   L 4 .   ? -24.805 10.759  42.463  1.00 35.28 ? 401 HOH   C O   1 
HETATM 6397 O  O   . HOH   L 4 .   ? -22.365 -4.086  52.999  1.00 29.20 ? 402 HOH   C O   1 
HETATM 6398 O  O   . HOH   L 4 .   ? -20.676 9.972   49.500  1.00 23.95 ? 403 HOH   C O   1 
HETATM 6399 O  O   . HOH   L 4 .   ? -32.460 -1.222  59.189  1.00 24.62 ? 404 HOH   C O   1 
HETATM 6400 O  O   . HOH   L 4 .   ? -24.968 -5.261  58.303  1.00 37.67 ? 405 HOH   C O   1 
HETATM 6401 O  O   . HOH   L 4 .   ? -28.605 -5.271  46.218  1.00 37.63 ? 406 HOH   C O   1 
HETATM 6402 O  O   . HOH   L 4 .   ? -23.335 4.464   53.450  1.00 31.49 ? 407 HOH   C O   1 
HETATM 6403 O  O   . HOH   L 4 .   ? -23.087 7.448   57.324  1.00 35.45 ? 408 HOH   C O   1 
HETATM 6404 O  O   . HOH   L 4 .   ? -27.327 1.675   47.014  1.00 26.39 ? 409 HOH   C O   1 
HETATM 6405 O  O   . HOH   L 4 .   ? -50.440 2.026   53.712  1.00 27.89 ? 410 HOH   C O   1 
HETATM 6406 O  O   . HOH   L 4 .   ? -15.903 4.247   59.018  1.00 29.34 ? 411 HOH   C O   1 
HETATM 6407 O  O   . HOH   L 4 .   ? -20.497 0.626   36.269  1.00 28.42 ? 412 HOH   C O   1 
HETATM 6408 O  O   . HOH   L 4 .   ? -30.148 -6.048  48.150  1.00 41.28 ? 413 HOH   C O   1 
HETATM 6409 O  O   . HOH   L 4 .   ? -24.451 6.216   55.437  1.00 22.18 ? 414 HOH   C O   1 
HETATM 6410 O  O   . HOH   L 4 .   ? -44.871 2.827   47.301  1.00 40.56 ? 415 HOH   C O   1 
HETATM 6411 O  O   . HOH   L 4 .   ? -44.076 -3.131  68.019  1.00 34.62 ? 416 HOH   C O   1 
HETATM 6412 O  O   . HOH   L 4 .   ? -20.635 12.081  43.849  1.00 40.05 ? 417 HOH   C O   1 
HETATM 6413 O  O   . HOH   L 4 .   ? -27.581 -15.532 55.595  1.00 41.60 ? 418 HOH   C O   1 
HETATM 6414 O  O   . HOH   M 4 .   ? -19.812 -3.528  12.769  1.00 26.09 ? 401 HOH   D O   1 
HETATM 6415 O  O   . HOH   M 4 .   ? -48.537 5.988   13.052  1.00 35.95 ? 402 HOH   D O   1 
HETATM 6416 O  O   . HOH   M 4 .   ? -20.633 -6.792  11.340  1.00 37.42 ? 403 HOH   D O   1 
HETATM 6417 O  O   . HOH   M 4 .   ? -17.153 -3.961  -4.640  1.00 29.64 ? 404 HOH   D O   1 
HETATM 6418 O  O   . HOH   M 4 .   ? -18.661 -6.196  22.268  1.00 43.87 ? 405 HOH   D O   1 
HETATM 6419 O  O   . HOH   M 4 .   ? -25.752 -4.223  18.987  1.00 48.58 ? 406 HOH   D O   1 
HETATM 6420 O  O   . HOH   M 4 .   ? -18.893 3.040   17.041  1.00 26.82 ? 407 HOH   D O   1 
HETATM 6421 O  O   . HOH   M 4 .   ? -5.929  14.614  1.825   1.00 36.82 ? 408 HOH   D O   1 
HETATM 6422 O  O   . HOH   M 4 .   ? -20.350 11.428  10.427  1.00 27.81 ? 409 HOH   D O   1 
HETATM 6423 O  O   . HOH   M 4 .   ? -24.303 0.389   4.957   1.00 22.42 ? 410 HOH   D O   1 
HETATM 6424 O  O   . HOH   M 4 .   ? -22.056 9.084   9.745   1.00 23.93 ? 411 HOH   D O   1 
HETATM 6425 O  O   . HOH   M 4 .   ? -20.469 4.880   10.497  1.00 23.77 ? 412 HOH   D O   1 
HETATM 6426 O  O   . HOH   M 4 .   ? -43.450 -5.164  8.002   1.00 28.51 ? 413 HOH   D O   1 
HETATM 6427 O  O   . HOH   M 4 .   ? -13.220 -0.986  8.106   1.00 24.44 ? 414 HOH   D O   1 
HETATM 6428 O  O   . HOH   M 4 .   ? -40.965 1.413   25.990  1.00 36.41 ? 415 HOH   D O   1 
HETATM 6429 O  O   . HOH   M 4 .   ? -13.187 6.138   16.177  1.00 41.70 ? 416 HOH   D O   1 
HETATM 6430 O  O   . HOH   M 4 .   ? -24.069 -11.747 6.920   1.00 46.24 ? 417 HOH   D O   1 
HETATM 6431 O  O   . HOH   M 4 .   ? -48.079 3.712   9.949   1.00 32.81 ? 418 HOH   D O   1 
HETATM 6432 O  O   . HOH   M 4 .   ? -25.651 -9.570  14.781  1.00 38.88 ? 419 HOH   D O   1 
HETATM 6433 O  O   . HOH   M 4 .   ? -20.810 9.577   -8.789  1.00 35.99 ? 420 HOH   D O   1 
HETATM 6434 O  O   . HOH   M 4 .   ? -42.204 14.716  6.542   1.00 46.83 ? 421 HOH   D O   1 
HETATM 6435 O  O   . HOH   M 4 .   ? -27.873 -9.485  8.796   1.00 38.05 ? 422 HOH   D O   1 
HETATM 6436 O  O   . HOH   M 4 .   ? -35.955 14.076  3.970   1.00 40.72 ? 423 HOH   D O   1 
HETATM 6437 O  O   . HOH   M 4 .   ? -21.334 -6.098  19.115  1.00 43.69 ? 424 HOH   D 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   . SER   A 3   ? 0.7733 0.4985 0.8949 0.0836  -0.0478 0.0730  96  SER   A N   
2    C  CA  . SER   A 3   ? 0.7709 0.5016 0.8736 0.0719  -0.0475 0.0872  96  SER   A CA  
3    C  C   . SER   A 3   ? 0.7413 0.4860 0.8314 0.0614  -0.0386 0.0763  96  SER   A C   
4    O  O   . SER   A 3   ? 0.7320 0.4987 0.8131 0.0591  -0.0376 0.0759  96  SER   A O   
5    C  CB  . SER   A 3   ? 0.7779 0.5256 0.8756 0.0758  -0.0544 0.1002  96  SER   A CB  
6    O  OG  . SER   A 3   ? 0.7747 0.5480 0.8734 0.0791  -0.0528 0.0890  96  SER   A OG  
7    N  N   . VAL   A 4   ? 0.7157 0.4474 0.8060 0.0554  -0.0332 0.0679  97  VAL   A N   
8    C  CA  . VAL   A 4   ? 0.6836 0.4242 0.7628 0.0451  -0.0256 0.0593  97  VAL   A CA  
9    C  C   . VAL   A 4   ? 0.6582 0.4169 0.7227 0.0387  -0.0248 0.0673  97  VAL   A C   
10   O  O   . VAL   A 4   ? 0.6624 0.4192 0.7209 0.0359  -0.0284 0.0822  97  VAL   A O   
11   C  CB  . VAL   A 4   ? 0.6941 0.4154 0.7732 0.0371  -0.0234 0.0589  97  VAL   A CB  
12   C  CG1 . VAL   A 4   ? 0.6857 0.4172 0.7546 0.0275  -0.0168 0.0514  97  VAL   A CG1 
13   C  CG2 . VAL   A 4   ? 0.7181 0.4204 0.8117 0.0432  -0.0246 0.0488  97  VAL   A CG2 
14   N  N   . PRO   A 5   ? 0.6129 0.3894 0.6713 0.0360  -0.0202 0.0579  98  PRO   A N   
15   C  CA  . PRO   A 5   ? 0.6018 0.3946 0.6474 0.0299  -0.0191 0.0622  98  PRO   A CA  
16   C  C   . PRO   A 5   ? 0.5885 0.3765 0.6248 0.0200  -0.0159 0.0680  98  PRO   A C   
17   O  O   . PRO   A 5   ? 0.5652 0.3420 0.6044 0.0160  -0.0126 0.0631  98  PRO   A O   
18   C  CB  . PRO   A 5   ? 0.5823 0.3895 0.6272 0.0292  -0.0148 0.0491  98  PRO   A CB  
19   C  CG  . PRO   A 5   ? 0.5848 0.3828 0.6385 0.0319  -0.0115 0.0384  98  PRO   A CG  
20   C  CD  . PRO   A 5   ? 0.6012 0.3833 0.6650 0.0386  -0.0159 0.0426  98  PRO   A CD  
21   N  N   . SER   A 6   ? 0.5906 0.3895 0.6162 0.0162  -0.0170 0.0778  99  SER   A N   
22   C  CA  . SER   A 6   ? 0.5884 0.3873 0.6053 0.0068  -0.0138 0.0855  99  SER   A CA  
23   C  C   . SER   A 6   ? 0.5618 0.3667 0.5767 0.0012  -0.0073 0.0737  99  SER   A C   
24   O  O   . SER   A 6   ? 0.5620 0.3781 0.5759 0.0036  -0.0059 0.0633  99  SER   A O   
25   C  CB  . SER   A 6   ? 0.6035 0.4180 0.6082 0.0050  -0.0158 0.0962  99  SER   A CB  
26   O  OG  . SER   A 6   ? 0.6177 0.4383 0.6137 -0.0042 -0.0108 0.1008  99  SER   A OG  
27   N  N   . GLN   A 7   ? 0.5453 0.3430 0.5608 -0.0060 -0.0040 0.0759  100 GLN   A N   
28   C  CA  . GLN   A 7   ? 0.5201 0.3247 0.5345 -0.0114 0.0012  0.0665  100 GLN   A CA  
29   C  C   . GLN   A 7   ? 0.5250 0.3415 0.5320 -0.0192 0.0047  0.0737  100 GLN   A C   
30   O  O   . GLN   A 7   ? 0.5143 0.3375 0.5221 -0.0237 0.0089  0.0672  100 GLN   A O   
31   C  CB  . GLN   A 7   ? 0.5110 0.3005 0.5346 -0.0129 0.0019  0.0600  100 GLN   A CB  
32   C  CG  . GLN   A 7   ? 0.5257 0.3007 0.5542 -0.0191 0.0011  0.0689  100 GLN   A CG  
33   C  CD  . GLN   A 7   ? 0.5164 0.2765 0.5544 -0.0197 0.0006  0.0595  100 GLN   A CD  
34   O  OE1 . GLN   A 7   ? 0.5325 0.2796 0.5769 -0.0135 -0.0024 0.0555  100 GLN   A OE1 
35   N  NE2 . GLN   A 7   ? 0.5094 0.2727 0.5491 -0.0270 0.0034  0.0550  100 GLN   A NE2 
36   N  N   . LYS   A 8   ? 0.5439 0.3647 0.5440 -0.0206 0.0030  0.0869  101 LYS   A N   
37   C  CA  . LYS   A 8   ? 0.5633 0.3978 0.5552 -0.0287 0.0072  0.0955  101 LYS   A CA  
38   C  C   . LYS   A 8   ? 0.5488 0.4058 0.5335 -0.0282 0.0112  0.0849  101 LYS   A C   
39   O  O   . LYS   A 8   ? 0.5461 0.4112 0.5259 -0.0222 0.0086  0.0801  101 LYS   A O   
40   C  CB  . LYS   A 8   ? 0.5942 0.4286 0.5785 -0.0294 0.0037  0.1131  101 LYS   A CB  
41   C  CG  . LYS   A 8   ? 0.6090 0.4585 0.5836 -0.0386 0.0084  0.1247  101 LYS   A CG  
42   C  CD  . LYS   A 8   ? 0.6204 0.4658 0.6028 -0.0485 0.0140  0.1256  101 LYS   A CD  
43   C  CE  . LYS   A 8   ? 0.6217 0.4921 0.5959 -0.0565 0.0215  0.1283  101 LYS   A CE  
44   N  NZ  . LYS   A 8   ? 0.6433 0.5221 0.6050 -0.0610 0.0213  0.1475  101 LYS   A NZ  
45   N  N   . THR   A 9   ? 0.5360 0.4028 0.5219 -0.0341 0.0170  0.0808  102 THR   A N   
46   C  CA  . THR   A 9   ? 0.5269 0.4147 0.5083 -0.0333 0.0211  0.0701  102 THR   A CA  
47   C  C   . THR   A 9   ? 0.5312 0.4373 0.4988 -0.0334 0.0216  0.0756  102 THR   A C   
48   O  O   . THR   A 9   ? 0.5464 0.4540 0.5078 -0.0382 0.0217  0.0905  102 THR   A O   
49   C  CB  . THR   A 9   ? 0.5179 0.4140 0.5053 -0.0394 0.0270  0.0663  102 THR   A CB  
50   O  OG1 . THR   A 9   ? 0.5201 0.3999 0.5189 -0.0389 0.0252  0.0610  102 THR   A OG1 
51   C  CG2 . THR   A 9   ? 0.5081 0.4244 0.4936 -0.0369 0.0309  0.0539  102 THR   A CG2 
52   N  N   . TYR   A 10  ? 0.5306 0.4499 0.4937 -0.0286 0.0215  0.0638  103 TYR   A N   
53   C  CA  . TYR   A 10  ? 0.5400 0.4787 0.4891 -0.0275 0.0208  0.0648  103 TYR   A CA  
54   C  C   . TYR   A 10  ? 0.5139 0.4672 0.4631 -0.0241 0.0232  0.0467  103 TYR   A C   
55   O  O   . TYR   A 10  ? 0.4911 0.4379 0.4450 -0.0187 0.0192  0.0368  103 TYR   A O   
56   C  CB  . TYR   A 10  ? 0.5618 0.4934 0.5075 -0.0223 0.0129  0.0699  103 TYR   A CB  
57   C  CG  . TYR   A 10  ? 0.5991 0.5271 0.5377 -0.0240 0.0091  0.0891  103 TYR   A CG  
58   C  CD1 . TYR   A 10  ? 0.6156 0.5223 0.5624 -0.0259 0.0076  0.1008  103 TYR   A CD1 
59   C  CD2 . TYR   A 10  ? 0.6207 0.5651 0.5450 -0.0227 0.0055  0.0950  103 TYR   A CD2 
60   C  CE1 . TYR   A 10  ? 0.6398 0.5401 0.5817 -0.0267 0.0031  0.1193  103 TYR   A CE1 
61   C  CE2 . TYR   A 10  ? 0.6426 0.5830 0.5603 -0.0234 0.0007  0.1143  103 TYR   A CE2 
62   C  CZ  . TYR   A 10  ? 0.6505 0.5677 0.5777 -0.0253 -0.0004 0.1270  103 TYR   A CZ  
63   O  OH  . TYR   A 10  ? 0.6831 0.5939 0.6053 -0.0253 -0.0060 0.1469  103 TYR   A OH  
64   N  N   . GLN   A 11  ? 0.5089 0.4810 0.4549 -0.0272 0.0298  0.0421  104 GLN   A N   
65   C  CA  . GLN   A 11  ? 0.4946 0.4801 0.4425 -0.0231 0.0323  0.0235  104 GLN   A CA  
66   C  C   . GLN   A 11  ? 0.4969 0.4955 0.4327 -0.0200 0.0286  0.0181  104 GLN   A C   
67   O  O   . GLN   A 11  ? 0.4903 0.4896 0.4304 -0.0152 0.0265  0.0024  104 GLN   A O   
68   C  CB  . GLN   A 11  ? 0.4957 0.4998 0.4450 -0.0267 0.0406  0.0200  104 GLN   A CB  
69   C  CG  . GLN   A 11  ? 0.4924 0.4852 0.4558 -0.0298 0.0432  0.0232  104 GLN   A CG  
70   C  CD  . GLN   A 11  ? 0.4903 0.5027 0.4603 -0.0309 0.0505  0.0146  104 GLN   A CD  
71   O  OE1 . GLN   A 11  ? 0.5000 0.5367 0.4622 -0.0314 0.0557  0.0099  104 GLN   A OE1 
72   N  NE2 . GLN   A 11  ? 0.4830 0.4867 0.4678 -0.0307 0.0509  0.0115  104 GLN   A NE2 
73   N  N   . GLY   A 12  ? 0.5065 0.5147 0.4281 -0.0229 0.0271  0.0312  105 GLY   A N   
74   C  CA  . GLY   A 12  ? 0.5234 0.5454 0.4317 -0.0204 0.0220  0.0288  105 GLY   A CA  
75   C  C   . GLY   A 12  ? 0.5232 0.5677 0.4262 -0.0185 0.0252  0.0098  105 GLY   A C   
76   O  O   . GLY   A 12  ? 0.5366 0.5925 0.4416 -0.0202 0.0332  0.0037  105 GLY   A O   
77   N  N   . SER   A 13  ? 0.5187 0.5696 0.4168 -0.0148 0.0191  -0.0002 106 SER   A N   
78   C  CA  . SER   A 13  ? 0.5342 0.6101 0.4220 -0.0134 0.0202  -0.0172 106 SER   A CA  
79   C  C   . SER   A 13  ? 0.5230 0.5970 0.4247 -0.0101 0.0248  -0.0382 106 SER   A C   
80   O  O   . SER   A 13  ? 0.5418 0.6383 0.4369 -0.0094 0.0298  -0.0514 106 SER   A O   
81   C  CB  . SER   A 13  ? 0.5365 0.6165 0.4182 -0.0109 0.0106  -0.0218 106 SER   A CB  
82   O  OG  . SER   A 13  ? 0.5569 0.6591 0.4306 -0.0094 0.0107  -0.0415 106 SER   A OG  
83   N  N   . TYR   A 14  ? 0.4981 0.5472 0.4180 -0.0078 0.0231  -0.0411 107 TYR   A N   
84   C  CA  . TYR   A 14  ? 0.4911 0.5338 0.4261 -0.0036 0.0249  -0.0601 107 TYR   A CA  
85   C  C   . TYR   A 14  ? 0.4822 0.5195 0.4280 -0.0037 0.0316  -0.0570 107 TYR   A C   
86   O  O   . TYR   A 14  ? 0.4749 0.5051 0.4345 0.0003  0.0325  -0.0700 107 TYR   A O   
87   C  CB  . TYR   A 14  ? 0.4777 0.4988 0.4248 -0.0012 0.0175  -0.0655 107 TYR   A CB  
88   C  CG  . TYR   A 14  ? 0.4891 0.5191 0.4284 -0.0013 0.0106  -0.0720 107 TYR   A CG  
89   C  CD1 . TYR   A 14  ? 0.4938 0.5374 0.4314 0.0006  0.0097  -0.0925 107 TYR   A CD1 
90   C  CD2 . TYR   A 14  ? 0.4872 0.5132 0.4216 -0.0029 0.0046  -0.0586 107 TYR   A CD2 
91   C  CE1 . TYR   A 14  ? 0.5076 0.5610 0.4383 0.0000  0.0026  -0.0995 107 TYR   A CE1 
92   C  CE2 . TYR   A 14  ? 0.4915 0.5281 0.4198 -0.0029 -0.0026 -0.0644 107 TYR   A CE2 
93   C  CZ  . TYR   A 14  ? 0.4998 0.5504 0.4261 -0.0019 -0.0037 -0.0850 107 TYR   A CZ  
94   O  OH  . TYR   A 14  ? 0.5112 0.5736 0.4319 -0.0025 -0.0116 -0.0917 107 TYR   A OH  
95   N  N   . GLY   A 15  ? 0.4915 0.5334 0.4317 -0.0086 0.0359  -0.0404 108 GLY   A N   
96   C  CA  . GLY   A 15  ? 0.4874 0.5266 0.4383 -0.0102 0.0419  -0.0364 108 GLY   A CA  
97   C  C   . GLY   A 15  ? 0.4747 0.4873 0.4418 -0.0076 0.0381  -0.0363 108 GLY   A C   
98   O  O   . GLY   A 15  ? 0.4635 0.4741 0.4436 -0.0040 0.0401  -0.0464 108 GLY   A O   
99   N  N   . PHE   A 16  ? 0.4831 0.4770 0.4494 -0.0091 0.0326  -0.0252 109 PHE   A N   
100  C  CA  . PHE   A 16  ? 0.4691 0.4389 0.4477 -0.0068 0.0283  -0.0251 109 PHE   A CA  
101  C  C   . PHE   A 16  ? 0.4616 0.4226 0.4476 -0.0096 0.0309  -0.0160 109 PHE   A C   
102  O  O   . PHE   A 16  ? 0.4542 0.4142 0.4351 -0.0144 0.0318  -0.0025 109 PHE   A O   
103  C  CB  . PHE   A 16  ? 0.4702 0.4287 0.4450 -0.0067 0.0220  -0.0192 109 PHE   A CB  
104  C  CG  . PHE   A 16  ? 0.4585 0.3951 0.4435 -0.0055 0.0188  -0.0164 109 PHE   A CG  
105  C  CD1 . PHE   A 16  ? 0.4475 0.3750 0.4426 -0.0024 0.0173  -0.0265 109 PHE   A CD1 
106  C  CD2 . PHE   A 16  ? 0.4484 0.3738 0.4328 -0.0074 0.0172  -0.0036 109 PHE   A CD2 
107  C  CE1 . PHE   A 16  ? 0.4419 0.3519 0.4444 -0.0020 0.0149  -0.0229 109 PHE   A CE1 
108  C  CE2 . PHE   A 16  ? 0.4443 0.3525 0.4369 -0.0062 0.0150  -0.0024 109 PHE   A CE2 
109  C  CZ  . PHE   A 16  ? 0.4383 0.3401 0.4391 -0.0038 0.0141  -0.0116 109 PHE   A CZ  
110  N  N   A ARG   A 17  ? 0.4527 0.4074 0.4510 -0.0066 0.0314  -0.0233 110 ARG   A N   
111  N  N   B ARG   A 17  ? 0.4522 0.4068 0.4505 -0.0066 0.0313  -0.0233 110 ARG   A N   
112  C  CA  A ARG   A 17  ? 0.4510 0.3974 0.4580 -0.0087 0.0323  -0.0172 110 ARG   A CA  
113  C  CA  B ARG   A 17  ? 0.4486 0.3951 0.4556 -0.0086 0.0323  -0.0174 110 ARG   A CA  
114  C  C   A ARG   A 17  ? 0.4334 0.3623 0.4497 -0.0046 0.0280  -0.0215 110 ARG   A C   
115  C  C   B ARG   A 17  ? 0.4327 0.3616 0.4491 -0.0046 0.0280  -0.0214 110 ARG   A C   
116  O  O   A ARG   A 17  ? 0.4354 0.3613 0.4544 -0.0001 0.0258  -0.0306 110 ARG   A O   
117  O  O   B ARG   A 17  ? 0.4350 0.3609 0.4540 -0.0001 0.0257  -0.0306 110 ARG   A O   
118  C  CB  A ARG   A 17  ? 0.4584 0.4224 0.4710 -0.0099 0.0380  -0.0202 110 ARG   A CB  
119  C  CB  B ARG   A 17  ? 0.4544 0.4185 0.4678 -0.0088 0.0378  -0.0224 110 ARG   A CB  
120  C  CG  A ARG   A 17  ? 0.4682 0.4453 0.4865 -0.0038 0.0400  -0.0355 110 ARG   A CG  
121  C  CG  B ARG   A 17  ? 0.4699 0.4546 0.4749 -0.0144 0.0437  -0.0168 110 ARG   A CG  
122  C  CD  A ARG   A 17  ? 0.4832 0.4868 0.5009 -0.0057 0.0473  -0.0386 110 ARG   A CD  
123  C  CD  B ARG   A 17  ? 0.4823 0.4906 0.4913 -0.0113 0.0493  -0.0291 110 ARG   A CD  
124  N  NE  A ARG   A 17  ? 0.4975 0.5114 0.5255 0.0018  0.0489  -0.0550 110 ARG   A NE  
125  N  NE  B ARG   A 17  ? 0.4904 0.5012 0.4959 -0.0050 0.0474  -0.0425 110 ARG   A NE  
126  C  CZ  A ARG   A 17  ? 0.5095 0.5318 0.5341 0.0067  0.0494  -0.0683 110 ARG   A CZ  
127  C  CZ  B ARG   A 17  ? 0.4979 0.5155 0.5128 0.0019  0.0483  -0.0585 110 ARG   A CZ  
128  N  NH1 A ARG   A 17  ? 0.5118 0.5412 0.5489 0.0144  0.0504  -0.0837 110 ARG   A NH1 
129  N  NH1 B ARG   A 17  ? 0.5048 0.5227 0.5165 0.0065  0.0459  -0.0707 110 ARG   A NH1 
130  N  NH2 A ARG   A 17  ? 0.5219 0.5451 0.5318 0.0045  0.0479  -0.0672 110 ARG   A NH2 
131  N  NH2 B ARG   A 17  ? 0.4977 0.5221 0.5266 0.0045  0.0510  -0.0628 110 ARG   A NH2 
132  N  N   . LEU   A 18  ? 0.4227 0.3409 0.4438 -0.0065 0.0268  -0.0150 111 LEU   A N   
133  C  CA  . LEU   A 18  ? 0.4042 0.3082 0.4327 -0.0033 0.0231  -0.0172 111 LEU   A CA  
134  C  C   . LEU   A 18  ? 0.3937 0.3051 0.4323 -0.0012 0.0241  -0.0217 111 LEU   A C   
135  O  O   . LEU   A 18  ? 0.3979 0.3226 0.4382 -0.0043 0.0277  -0.0201 111 LEU   A O   
136  C  CB  . LEU   A 18  ? 0.4009 0.2912 0.4272 -0.0063 0.0209  -0.0088 111 LEU   A CB  
137  C  CG  . LEU   A 18  ? 0.3992 0.2826 0.4181 -0.0073 0.0194  -0.0041 111 LEU   A CG  
138  C  CD1 . LEU   A 18  ? 0.3943 0.2648 0.4135 -0.0089 0.0176  0.0016  111 LEU   A CD1 
139  C  CD2 . LEU   A 18  ? 0.3982 0.2790 0.4171 -0.0038 0.0172  -0.0099 111 LEU   A CD2 
140  N  N   . GLY   A 19  ? 0.3876 0.2915 0.4334 0.0039  0.0208  -0.0267 112 GLY   A N   
141  C  CA  . GLY   A 19  ? 0.3825 0.2904 0.4392 0.0073  0.0196  -0.0293 112 GLY   A CA  
142  C  C   . GLY   A 19  ? 0.3832 0.2757 0.4414 0.0085  0.0145  -0.0249 112 GLY   A C   
143  O  O   . GLY   A 19  ? 0.3720 0.2516 0.4245 0.0078  0.0128  -0.0223 112 GLY   A O   
144  N  N   . PHE   A 20  ? 0.3840 0.2802 0.4496 0.0099  0.0123  -0.0240 113 PHE   A N   
145  C  CA  . PHE   A 20  ? 0.3851 0.2699 0.4511 0.0113  0.0070  -0.0194 113 PHE   A CA  
146  C  C   . PHE   A 20  ? 0.3825 0.2731 0.4609 0.0180  0.0034  -0.0226 113 PHE   A C   
147  O  O   . PHE   A 20  ? 0.3763 0.2830 0.4635 0.0196  0.0057  -0.0278 113 PHE   A O   
148  C  CB  . PHE   A 20  ? 0.3907 0.2747 0.4510 0.0053  0.0065  -0.0139 113 PHE   A CB  
149  C  CG  . PHE   A 20  ? 0.3957 0.2745 0.4465 0.0000  0.0098  -0.0110 113 PHE   A CG  
150  C  CD1 . PHE   A 20  ? 0.3951 0.2828 0.4453 -0.0041 0.0139  -0.0107 113 PHE   A CD1 
151  C  CD2 . PHE   A 20  ? 0.4018 0.2678 0.4452 -0.0005 0.0086  -0.0079 113 PHE   A CD2 
152  C  CE1 . PHE   A 20  ? 0.4010 0.2828 0.4431 -0.0080 0.0158  -0.0066 113 PHE   A CE1 
153  C  CE2 . PHE   A 20  ? 0.4008 0.2626 0.4376 -0.0039 0.0109  -0.0055 113 PHE   A CE2 
154  C  CZ  . PHE   A 20  ? 0.4070 0.2757 0.4433 -0.0073 0.0139  -0.0045 113 PHE   A CZ  
155  N  N   . LEU   A 21  ? 0.3916 0.2702 0.4710 0.0218  -0.0018 -0.0191 114 LEU   A N   
156  C  CA  . LEU   A 21  ? 0.4011 0.2826 0.4922 0.0290  -0.0071 -0.0195 114 LEU   A CA  
157  C  C   . LEU   A 21  ? 0.3913 0.2876 0.4860 0.0270  -0.0088 -0.0182 114 LEU   A C   
158  O  O   . LEU   A 21  ? 0.3791 0.2749 0.4644 0.0199  -0.0081 -0.0143 114 LEU   A O   
159  C  CB  . LEU   A 21  ? 0.4269 0.2914 0.5145 0.0310  -0.0125 -0.0120 114 LEU   A CB  
160  C  CG  . LEU   A 21  ? 0.4427 0.2925 0.5320 0.0332  -0.0122 -0.0138 114 LEU   A CG  
161  C  CD1 . LEU   A 21  ? 0.4567 0.2906 0.5416 0.0328  -0.0168 -0.0037 114 LEU   A CD1 
162  C  CD2 . LEU   A 21  ? 0.4585 0.3114 0.5632 0.0415  -0.0132 -0.0227 114 LEU   A CD2 
163  N  N   . HIS   A 22  ? 0.3764 0.2860 0.4858 0.0331  -0.0110 -0.0225 115 HIS   A N   
164  C  CA  . HIS   A 22  ? 0.3728 0.2989 0.4895 0.0321  -0.0142 -0.0218 115 HIS   A CA  
165  C  C   . HIS   A 22  ? 0.3697 0.2886 0.4860 0.0366  -0.0235 -0.0149 115 HIS   A C   
166  O  O   . HIS   A 22  ? 0.3782 0.3025 0.5078 0.0453  -0.0288 -0.0157 115 HIS   A O   
167  C  CB  . HIS   A 22  ? 0.3759 0.3233 0.5099 0.0366  -0.0115 -0.0303 115 HIS   A CB  
168  C  CG  . HIS   A 22  ? 0.3769 0.3300 0.5087 0.0337  -0.0024 -0.0364 115 HIS   A CG  
169  N  ND1 . HIS   A 22  ? 0.3733 0.3281 0.4941 0.0233  0.0032  -0.0339 115 HIS   A ND1 
170  C  CD2 . HIS   A 22  ? 0.3771 0.3339 0.5152 0.0398  0.0012  -0.0449 115 HIS   A CD2 
171  C  CE1 . HIS   A 22  ? 0.3807 0.3415 0.5000 0.0230  0.0101  -0.0391 115 HIS   A CE1 
172  N  NE2 . HIS   A 22  ? 0.3721 0.3353 0.5016 0.0329  0.0092  -0.0470 115 HIS   A NE2 
173  N  N   A SER   A 23  ? 0.3666 0.2744 0.4677 0.0311  -0.0252 -0.0081 116 SER   A N   
174  N  N   B SER   A 23  ? 0.3708 0.2785 0.4719 0.0311  -0.0252 -0.0081 116 SER   A N   
175  C  CA  A SER   A 23  ? 0.3755 0.2739 0.4704 0.0341  -0.0329 0.0004  116 SER   A CA  
176  C  CA  B SER   A 23  ? 0.3809 0.2792 0.4757 0.0341  -0.0329 0.0004  116 SER   A CA  
177  C  C   A SER   A 23  ? 0.3786 0.2914 0.4753 0.0336  -0.0399 0.0021  116 SER   A C   
178  C  C   B SER   A 23  ? 0.3822 0.2950 0.4789 0.0336  -0.0398 0.0021  116 SER   A C   
179  O  O   A SER   A 23  ? 0.3880 0.2984 0.4831 0.0384  -0.0477 0.0093  116 SER   A O   
180  O  O   B SER   A 23  ? 0.3918 0.3024 0.4871 0.0385  -0.0477 0.0092  116 SER   A O   
181  C  CB  A SER   A 23  ? 0.3769 0.2597 0.4545 0.0284  -0.0303 0.0056  116 SER   A CB  
182  C  CB  B SER   A 23  ? 0.3842 0.2672 0.4618 0.0282  -0.0301 0.0054  116 SER   A CB  
183  O  OG  A SER   A 23  ? 0.3689 0.2400 0.4459 0.0285  -0.0249 0.0037  116 SER   A OG  
184  O  OG  B SER   A 23  ? 0.3769 0.2635 0.4474 0.0202  -0.0246 0.0014  116 SER   A OG  
185  N  N   . GLY   A 24  ? 0.3712 0.2984 0.4709 0.0273  -0.0375 -0.0034 117 GLY   A N   
186  C  CA  . GLY   A 24  ? 0.3859 0.3279 0.4875 0.0248  -0.0441 -0.0036 117 GLY   A CA  
187  C  C   . GLY   A 24  ? 0.3915 0.3257 0.4745 0.0191  -0.0467 0.0001  117 GLY   A C   
188  O  O   . GLY   A 24  ? 0.3966 0.3147 0.4664 0.0165  -0.0419 0.0026  117 GLY   A O   
189  N  N   . THR   A 25  ? 0.4056 0.3524 0.4879 0.0175  -0.0544 -0.0002 118 THR   A N   
190  C  CA  . THR   A 25  ? 0.4170 0.3615 0.4822 0.0113  -0.0569 -0.0002 118 THR   A CA  
191  C  C   . THR   A 25  ? 0.4398 0.3898 0.4975 0.0164  -0.0672 0.0068  118 THR   A C   
192  O  O   . THR   A 25  ? 0.4435 0.4014 0.4913 0.0120  -0.0720 0.0043  118 THR   A O   
193  C  CB  . THR   A 25  ? 0.4112 0.3667 0.4812 0.0022  -0.0564 -0.0094 118 THR   A CB  
194  O  OG1 . THR   A 25  ? 0.4107 0.3869 0.4971 0.0042  -0.0632 -0.0118 118 THR   A OG1 
195  C  CG2 . THR   A 25  ? 0.4020 0.3509 0.4772 -0.0037 -0.0466 -0.0138 118 THR   A CG2 
196  N  N   . ALA   A 26  ? 0.4627 0.4087 0.5251 0.0256  -0.0710 0.0154  119 ALA   A N   
197  C  CA  . ALA   A 26  ? 0.4909 0.4406 0.5462 0.0314  -0.0815 0.0255  119 ALA   A CA  
198  C  C   . ALA   A 26  ? 0.5136 0.4530 0.5443 0.0269  -0.0797 0.0315  119 ALA   A C   
199  O  O   . ALA   A 26  ? 0.5040 0.4285 0.5281 0.0231  -0.0704 0.0307  119 ALA   A O   
200  C  CB  . ALA   A 26  ? 0.4962 0.4391 0.5641 0.0421  -0.0849 0.0336  119 ALA   A CB  
201  N  N   . LYS   A 27  ? 0.5537 0.5033 0.5719 0.0274  -0.0886 0.0370  120 LYS   A N   
202  C  CA  . LYS   A 27  ? 0.5864 0.5334 0.5795 0.0228  -0.0877 0.0417  120 LYS   A CA  
203  C  C   . LYS   A 27  ? 0.5956 0.5223 0.5813 0.0226  -0.0793 0.0502  120 LYS   A C   
204  O  O   . LYS   A 27  ? 0.5949 0.5174 0.5660 0.0165  -0.0722 0.0472  120 LYS   A O   
205  C  CB  . LYS   A 27  ? 0.6207 0.5813 0.6030 0.0265  -0.0999 0.0516  120 LYS   A CB  
206  C  CG  . LYS   A 27  ? 0.6331 0.6168 0.6174 0.0247  -0.1090 0.0423  120 LYS   A CG  
207  C  CD  . LYS   A 27  ? 0.6583 0.6572 0.6269 0.0275  -0.1212 0.0520  120 LYS   A CD  
208  C  CE  . LYS   A 27  ? 0.6726 0.6663 0.6465 0.0376  -0.1287 0.0706  120 LYS   A CE  
209  N  NZ  . LYS   A 27  ? 0.6994 0.7095 0.6577 0.0405  -0.1418 0.0816  120 LYS   A NZ  
210  N  N   . SER   A 28  ? 0.6074 0.5225 0.6049 0.0291  -0.0803 0.0592  121 SER   A N   
211  C  CA  . SER   A 28  ? 0.6187 0.5147 0.6113 0.0291  -0.0749 0.0696  121 SER   A CA  
212  C  C   . SER   A 28  ? 0.5991 0.4830 0.5966 0.0248  -0.0632 0.0608  121 SER   A C   
213  O  O   . SER   A 28  ? 0.6060 0.4769 0.5970 0.0222  -0.0577 0.0672  121 SER   A O   
214  C  CB  . SER   A 28  ? 0.6396 0.5268 0.6459 0.0379  -0.0817 0.0807  121 SER   A CB  
215  O  OG  . SER   A 28  ? 0.6406 0.5278 0.6696 0.0431  -0.0811 0.0709  121 SER   A OG  
216  N  N   A VAL   A 29  ? 0.5698 0.4586 0.5785 0.0236  -0.0598 0.0475  122 VAL   A N   
217  N  N   B VAL   A 29  ? 0.5686 0.4574 0.5772 0.0236  -0.0598 0.0476  122 VAL   A N   
218  C  CA  A VAL   A 29  ? 0.5478 0.4263 0.5646 0.0215  -0.0504 0.0402  122 VAL   A CA  
219  C  CA  B VAL   A 29  ? 0.5451 0.4235 0.5618 0.0215  -0.0504 0.0403  122 VAL   A CA  
220  C  C   A VAL   A 29  ? 0.5423 0.4155 0.5443 0.0144  -0.0426 0.0382  122 VAL   A C   
221  C  C   B VAL   A 29  ? 0.5403 0.4135 0.5424 0.0145  -0.0426 0.0382  122 VAL   A C   
222  O  O   A VAL   A 29  ? 0.5418 0.4238 0.5334 0.0102  -0.0426 0.0331  122 VAL   A O   
223  O  O   B VAL   A 29  ? 0.5412 0.4232 0.5329 0.0102  -0.0426 0.0331  122 VAL   A O   
224  C  CB  A VAL   A 29  ? 0.5324 0.4201 0.5635 0.0214  -0.0490 0.0286  122 VAL   A CB  
225  C  CB  B VAL   A 29  ? 0.5266 0.4143 0.5577 0.0214  -0.0490 0.0287  122 VAL   A CB  
226  C  CG1 A VAL   A 29  ? 0.5166 0.3958 0.5525 0.0187  -0.0397 0.0222  122 VAL   A CG1 
227  C  CG1 B VAL   A 29  ? 0.5154 0.4039 0.5401 0.0137  -0.0422 0.0199  122 VAL   A CG1 
228  C  CG2 A VAL   A 29  ? 0.5375 0.4331 0.5858 0.0293  -0.0558 0.0294  122 VAL   A CG2 
229  C  CG2 B VAL   A 29  ? 0.5170 0.3986 0.5644 0.0263  -0.0462 0.0264  122 VAL   A CG2 
230  N  N   . THR   A 30  ? 0.5322 0.3923 0.5349 0.0135  -0.0366 0.0410  123 THR   A N   
231  C  CA  . THR   A 30  ? 0.5267 0.3824 0.5182 0.0079  -0.0290 0.0400  123 THR   A CA  
232  C  C   . THR   A 30  ? 0.4877 0.3416 0.4851 0.0054  -0.0226 0.0291  123 THR   A C   
233  O  O   . THR   A 30  ? 0.5001 0.3540 0.4895 0.0015  -0.0175 0.0255  123 THR   A O   
234  C  CB  . THR   A 30  ? 0.5486 0.3930 0.5384 0.0074  -0.0269 0.0505  123 THR   A CB  
235  O  OG1 . THR   A 30  ? 0.5652 0.3993 0.5703 0.0104  -0.0262 0.0489  123 THR   A OG1 
236  C  CG2 . THR   A 30  ? 0.5712 0.4165 0.5535 0.0090  -0.0334 0.0639  123 THR   A CG2 
237  N  N   A CYS   A 31  ? 0.4610 0.3146 0.4720 0.0079  -0.0229 0.0244  124 CYS   A N   
238  N  N   B CYS   A 31  ? 0.4689 0.3226 0.4799 0.0079  -0.0229 0.0244  124 CYS   A N   
239  C  CA  A CYS   A 31  ? 0.4400 0.2933 0.4564 0.0055  -0.0174 0.0159  124 CYS   A CA  
240  C  CA  B CYS   A 31  ? 0.4478 0.3011 0.4641 0.0055  -0.0174 0.0159  124 CYS   A CA  
241  C  C   A CYS   A 31  ? 0.4300 0.2913 0.4591 0.0078  -0.0196 0.0112  124 CYS   A C   
242  C  C   B CYS   A 31  ? 0.4338 0.2949 0.4628 0.0078  -0.0195 0.0112  124 CYS   A C   
243  O  O   A CYS   A 31  ? 0.4225 0.2844 0.4608 0.0131  -0.0230 0.0133  124 CYS   A O   
244  O  O   B CYS   A 31  ? 0.4318 0.2932 0.4700 0.0130  -0.0227 0.0132  124 CYS   A O   
245  C  CB  A CYS   A 31  ? 0.4379 0.2813 0.4561 0.0052  -0.0122 0.0167  124 CYS   A CB  
246  C  CB  B CYS   A 31  ? 0.4464 0.2899 0.4645 0.0051  -0.0122 0.0166  124 CYS   A CB  
247  S  SG  A CYS   A 31  ? 0.4243 0.2680 0.4504 0.0042  -0.0072 0.0089  124 CYS   A SG  
248  S  SG  B CYS   A 31  ? 0.4520 0.2894 0.4830 0.0106  -0.0143 0.0185  124 CYS   A SG  
249  N  N   . THR   A 32  ? 0.4140 0.2813 0.4445 0.0038  -0.0178 0.0050  125 THR   A N   
250  C  CA  . THR   A 32  ? 0.4091 0.2874 0.4520 0.0040  -0.0188 0.0006  125 THR   A CA  
251  C  C   . THR   A 32  ? 0.4047 0.2829 0.4487 -0.0016 -0.0132 -0.0037 125 THR   A C   
252  O  O   . THR   A 32  ? 0.4281 0.3009 0.4642 -0.0059 -0.0119 -0.0050 125 THR   A O   
253  C  CB  . THR   A 32  ? 0.4085 0.2986 0.4539 0.0045  -0.0260 0.0004  125 THR   A CB  
254  O  OG1 . THR   A 32  ? 0.3999 0.3026 0.4603 0.0053  -0.0264 -0.0035 125 THR   A OG1 
255  C  CG2 . THR   A 32  ? 0.4149 0.3068 0.4512 -0.0014 -0.0274 -0.0027 125 THR   A CG2 
256  N  N   . TYR   A 33  ? 0.4045 0.2886 0.4581 -0.0011 -0.0101 -0.0059 126 TYR   A N   
257  C  CA  . TYR   A 33  ? 0.3983 0.2836 0.4534 -0.0066 -0.0047 -0.0078 126 TYR   A CA  
258  C  C   . TYR   A 33  ? 0.3975 0.2971 0.4630 -0.0109 -0.0055 -0.0104 126 TYR   A C   
259  O  O   . TYR   A 33  ? 0.3941 0.3064 0.4697 -0.0072 -0.0077 -0.0121 126 TYR   A O   
260  C  CB  . TYR   A 33  ? 0.3893 0.2739 0.4460 -0.0040 0.0000  -0.0081 126 TYR   A CB  
261  C  CG  . TYR   A 33  ? 0.3857 0.2748 0.4435 -0.0093 0.0051  -0.0083 126 TYR   A CG  
262  C  CD1 . TYR   A 33  ? 0.3862 0.2653 0.4363 -0.0136 0.0072  -0.0056 126 TYR   A CD1 
263  C  CD2 . TYR   A 33  ? 0.3829 0.2871 0.4497 -0.0096 0.0080  -0.0106 126 TYR   A CD2 
264  C  CE1 . TYR   A 33  ? 0.3924 0.2746 0.4429 -0.0185 0.0113  -0.0033 126 TYR   A CE1 
265  C  CE2 . TYR   A 33  ? 0.3926 0.3023 0.4587 -0.0153 0.0132  -0.0088 126 TYR   A CE2 
266  C  CZ  . TYR   A 33  ? 0.3956 0.2932 0.4532 -0.0200 0.0145  -0.0042 126 TYR   A CZ  
267  O  OH  . TYR   A 33  ? 0.4153 0.3169 0.4716 -0.0257 0.0189  -0.0001 126 TYR   A OH  
268  N  N   . SER   A 34  ? 0.4015 0.2987 0.4657 -0.0184 -0.0039 -0.0108 127 SER   A N   
269  C  CA  . SER   A 34  ? 0.4009 0.3103 0.4758 -0.0254 -0.0035 -0.0125 127 SER   A CA  
270  C  C   . SER   A 34  ? 0.3975 0.3097 0.4750 -0.0293 0.0034  -0.0097 127 SER   A C   
271  O  O   . SER   A 34  ? 0.3995 0.2994 0.4700 -0.0328 0.0061  -0.0065 127 SER   A O   
272  C  CB  . SER   A 34  ? 0.4136 0.3166 0.4865 -0.0321 -0.0067 -0.0147 127 SER   A CB  
273  O  OG  . SER   A 34  ? 0.4229 0.3362 0.5076 -0.0405 -0.0061 -0.0158 127 SER   A OG  
274  N  N   . PRO   A 35  ? 0.3954 0.3252 0.4828 -0.0284 0.0065  -0.0108 128 PRO   A N   
275  C  CA  . PRO   A 35  ? 0.3974 0.3341 0.4860 -0.0331 0.0136  -0.0078 128 PRO   A CA  
276  C  C   . PRO   A 35  ? 0.3993 0.3357 0.4918 -0.0447 0.0151  -0.0040 128 PRO   A C   
277  O  O   . PRO   A 35  ? 0.4021 0.3333 0.4894 -0.0493 0.0196  0.0017  128 PRO   A O   
278  C  CB  . PRO   A 35  ? 0.3956 0.3552 0.4959 -0.0293 0.0163  -0.0120 128 PRO   A CB  
279  C  CG  . PRO   A 35  ? 0.3878 0.3497 0.4939 -0.0210 0.0096  -0.0166 128 PRO   A CG  
280  C  CD  . PRO   A 35  ? 0.3884 0.3337 0.4865 -0.0223 0.0032  -0.0149 128 PRO   A CD  
281  N  N   . ALA   A 36  ? 0.3962 0.3377 0.4979 -0.0494 0.0107  -0.0070 129 ALA   A N   
282  C  CA  . ALA   A 36  ? 0.4065 0.3469 0.5150 -0.0617 0.0111  -0.0045 129 ALA   A CA  
283  C  C   . ALA   A 36  ? 0.4092 0.3240 0.5072 -0.0644 0.0102  -0.0011 129 ALA   A C   
284  O  O   . ALA   A 36  ? 0.4211 0.3301 0.5217 -0.0733 0.0131  0.0047  129 ALA   A O   
285  C  CB  . ALA   A 36  ? 0.4016 0.3529 0.5222 -0.0652 0.0050  -0.0106 129 ALA   A CB  
286  N  N   . LEU   A 37  ? 0.4054 0.3059 0.4930 -0.0569 0.0063  -0.0043 130 LEU   A N   
287  C  CA  . LEU   A 37  ? 0.4145 0.2922 0.4938 -0.0577 0.0049  -0.0033 130 LEU   A CA  
288  C  C   . LEU   A 37  ? 0.4063 0.2747 0.4747 -0.0514 0.0084  0.0016  130 LEU   A C   
289  O  O   . LEU   A 37  ? 0.4079 0.2592 0.4713 -0.0514 0.0078  0.0031  130 LEU   A O   
290  C  CB  . LEU   A 37  ? 0.4234 0.2955 0.4987 -0.0541 -0.0011 -0.0113 130 LEU   A CB  
291  C  CG  . LEU   A 37  ? 0.4342 0.3143 0.5189 -0.0605 -0.0063 -0.0177 130 LEU   A CG  
292  C  CD1 . LEU   A 37  ? 0.4430 0.3225 0.5200 -0.0550 -0.0123 -0.0249 130 LEU   A CD1 
293  C  CD2 . LEU   A 37  ? 0.4571 0.3256 0.5488 -0.0710 -0.0065 -0.0181 130 LEU   A CD2 
294  N  N   . ASN   A 38  ? 0.3942 0.2737 0.4603 -0.0460 0.0115  0.0030  131 ASN   A N   
295  C  CA  . ASN   A 38  ? 0.3859 0.2593 0.4420 -0.0391 0.0135  0.0053  131 ASN   A CA  
296  C  C   . ASN   A 38  ? 0.3856 0.2444 0.4346 -0.0341 0.0099  0.0021  131 ASN   A C   
297  O  O   . ASN   A 38  ? 0.3805 0.2272 0.4238 -0.0327 0.0106  0.0048  131 ASN   A O   
298  C  CB  . ASN   A 38  ? 0.3936 0.2638 0.4461 -0.0426 0.0175  0.0131  131 ASN   A CB  
299  C  CG  . ASN   A 38  ? 0.3883 0.2566 0.4317 -0.0359 0.0188  0.0145  131 ASN   A CG  
300  O  OD1 . ASN   A 38  ? 0.3726 0.2471 0.4146 -0.0299 0.0187  0.0097  131 ASN   A OD1 
301  N  ND2 . ASN   A 38  ? 0.3940 0.2535 0.4321 -0.0371 0.0195  0.0211  131 ASN   A ND2 
302  N  N   . LYS   A 39  ? 0.3885 0.2502 0.4381 -0.0313 0.0062  -0.0030 132 LYS   A N   
303  C  CA  . LYS   A 39  ? 0.3922 0.2436 0.4348 -0.0281 0.0033  -0.0063 132 LYS   A CA  
304  C  C   . LYS   A 39  ? 0.3948 0.2518 0.4342 -0.0219 0.0011  -0.0077 132 LYS   A C   
305  O  O   . LYS   A 39  ? 0.4063 0.2742 0.4512 -0.0216 -0.0014 -0.0091 132 LYS   A O   
306  C  CB  . LYS   A 39  ? 0.3986 0.2463 0.4439 -0.0332 0.0000  -0.0110 132 LYS   A CB  
307  C  CG  . LYS   A 39  ? 0.4031 0.2417 0.4404 -0.0302 -0.0021 -0.0160 132 LYS   A CG  
308  C  CD  . LYS   A 39  ? 0.4135 0.2465 0.4537 -0.0354 -0.0051 -0.0226 132 LYS   A CD  
309  C  CE  . LYS   A 39  ? 0.4179 0.2438 0.4499 -0.0318 -0.0062 -0.0293 132 LYS   A CE  
310  N  NZ  . LYS   A 39  ? 0.4307 0.2465 0.4674 -0.0365 -0.0083 -0.0368 132 LYS   A NZ  
311  N  N   A MET   A 40  ? 0.4048 0.2546 0.4368 -0.0174 0.0021  -0.0066 133 MET   A N   
312  N  N   B MET   A 40  ? 0.3894 0.2393 0.4214 -0.0174 0.0021  -0.0066 133 MET   A N   
313  C  CA  A MET   A 40  ? 0.4118 0.2630 0.4396 -0.0126 0.0001  -0.0061 133 MET   A CA  
314  C  CA  B MET   A 40  ? 0.3856 0.2368 0.4134 -0.0126 0.0001  -0.0061 133 MET   A CA  
315  C  C   A MET   A 40  ? 0.4149 0.2645 0.4360 -0.0132 -0.0028 -0.0088 133 MET   A C   
316  C  C   B MET   A 40  ? 0.3991 0.2487 0.4202 -0.0131 -0.0028 -0.0087 133 MET   A C   
317  O  O   A MET   A 40  ? 0.4144 0.2571 0.4315 -0.0145 -0.0012 -0.0113 133 MET   A O   
318  O  O   B MET   A 40  ? 0.4029 0.2455 0.4199 -0.0144 -0.0012 -0.0113 133 MET   A O   
319  C  CB  A MET   A 40  ? 0.4180 0.2632 0.4419 -0.0093 0.0029  -0.0035 133 MET   A CB  
320  C  CB  B MET   A 40  ? 0.3730 0.2184 0.3971 -0.0093 0.0030  -0.0035 133 MET   A CB  
321  C  CG  A MET   A 40  ? 0.4285 0.2730 0.4487 -0.0059 0.0012  -0.0014 133 MET   A CG  
322  C  CG  B MET   A 40  ? 0.3689 0.2124 0.3878 -0.0062 0.0016  -0.0016 133 MET   A CG  
323  S  SD  A MET   A 40  ? 0.4495 0.3006 0.4771 -0.0023 -0.0021 0.0000  133 MET   A SD  
324  S  SD  B MET   A 40  ? 0.3531 0.1912 0.3713 -0.0040 0.0046  0.0009  133 MET   A SD  
325  C  CE  A MET   A 40  ? 0.4359 0.2860 0.4690 -0.0006 0.0015  -0.0012 133 MET   A CE  
326  C  CE  B MET   A 40  ? 0.3526 0.1951 0.3794 -0.0019 0.0044  0.0000  133 MET   A CE  
327  N  N   . PHE   A 41  ? 0.4087 0.2655 0.4289 -0.0117 -0.0072 -0.0085 134 PHE   A N   
328  C  CA  . PHE   A 41  ? 0.4203 0.2788 0.4310 -0.0115 -0.0103 -0.0102 134 PHE   A CA  
329  C  C   . PHE   A 41  ? 0.4290 0.2867 0.4338 -0.0073 -0.0105 -0.0037 134 PHE   A C   
330  O  O   . PHE   A 41  ? 0.4281 0.2888 0.4384 -0.0044 -0.0131 0.0004  134 PHE   A O   
331  C  CB  . PHE   A 41  ? 0.4165 0.2853 0.4298 -0.0136 -0.0164 -0.0136 134 PHE   A CB  
332  C  CG  . PHE   A 41  ? 0.4168 0.2864 0.4386 -0.0193 -0.0165 -0.0194 134 PHE   A CG  
333  C  CD1 . PHE   A 41  ? 0.4068 0.2794 0.4402 -0.0211 -0.0145 -0.0176 134 PHE   A CD1 
334  C  CD2 . PHE   A 41  ? 0.4241 0.2918 0.4425 -0.0234 -0.0184 -0.0269 134 PHE   A CD2 
335  C  CE1 . PHE   A 41  ? 0.4107 0.2840 0.4524 -0.0279 -0.0141 -0.0211 134 PHE   A CE1 
336  C  CE2 . PHE   A 41  ? 0.4299 0.2961 0.4579 -0.0298 -0.0188 -0.0316 134 PHE   A CE2 
337  C  CZ  . PHE   A 41  ? 0.4199 0.2888 0.4597 -0.0325 -0.0166 -0.0277 134 PHE   A CZ  
338  N  N   . CYS   A 42  ? 0.4373 0.2913 0.4328 -0.0072 -0.0077 -0.0029 135 CYS   A N   
339  C  CA  . CYS   A 42  ? 0.4464 0.2989 0.4370 -0.0049 -0.0070 0.0047  135 CYS   A CA  
340  C  C   . CYS   A 42  ? 0.4494 0.3060 0.4267 -0.0060 -0.0061 0.0049  135 CYS   A C   
341  O  O   . CYS   A 42  ? 0.4480 0.3066 0.4211 -0.0077 -0.0046 -0.0028 135 CYS   A O   
342  C  CB  . CYS   A 42  ? 0.4513 0.2963 0.4473 -0.0042 -0.0023 0.0066  135 CYS   A CB  
343  S  SG  . CYS   A 42  ? 0.4782 0.3196 0.4727 -0.0058 0.0034  0.0011  135 CYS   A SG  
344  N  N   . GLN   A 43  ? 0.4583 0.3164 0.4296 -0.0053 -0.0071 0.0136  136 GLN   A N   
345  C  CA  . GLN   A 43  ? 0.4689 0.3335 0.4261 -0.0069 -0.0050 0.0161  136 GLN   A CA  
346  C  C   . GLN   A 43  ? 0.4689 0.3300 0.4268 -0.0082 0.0024  0.0174  136 GLN   A C   
347  O  O   . GLN   A 43  ? 0.4685 0.3215 0.4365 -0.0078 0.0038  0.0206  136 GLN   A O   
348  C  CB  . GLN   A 43  ? 0.4823 0.3504 0.4328 -0.0062 -0.0098 0.0278  136 GLN   A CB  
349  C  CG  . GLN   A 43  ? 0.4889 0.3649 0.4369 -0.0046 -0.0181 0.0270  136 GLN   A CG  
350  C  CD  . GLN   A 43  ? 0.4985 0.3754 0.4427 -0.0025 -0.0238 0.0410  136 GLN   A CD  
351  O  OE1 . GLN   A 43  ? 0.5170 0.3916 0.4712 0.0012  -0.0300 0.0445  136 GLN   A OE1 
352  N  NE2 . GLN   A 43  ? 0.5081 0.3880 0.4392 -0.0048 -0.0214 0.0499  136 GLN   A NE2 
353  N  N   . LEU   A 44  ? 0.4751 0.3443 0.4228 -0.0098 0.0067  0.0143  137 LEU   A N   
354  C  CA  . LEU   A 44  ? 0.4792 0.3506 0.4268 -0.0113 0.0143  0.0152  137 LEU   A CA  
355  C  C   . LEU   A 44  ? 0.4755 0.3426 0.4265 -0.0135 0.0151  0.0282  137 LEU   A C   
356  O  O   . LEU   A 44  ? 0.4759 0.3444 0.4199 -0.0146 0.0115  0.0382  137 LEU   A O   
357  C  CB  . LEU   A 44  ? 0.5021 0.3876 0.4354 -0.0124 0.0178  0.0114  137 LEU   A CB  
358  C  CG  . LEU   A 44  ? 0.5058 0.3978 0.4404 -0.0130 0.0264  0.0071  137 LEU   A CG  
359  C  CD1 . LEU   A 44  ? 0.5036 0.3894 0.4491 -0.0095 0.0275  -0.0050 137 LEU   A CD1 
360  C  CD2 . LEU   A 44  ? 0.5262 0.4352 0.4450 -0.0141 0.0303  0.0036  137 LEU   A CD2 
361  N  N   . ALA   A 45  ? 0.4743 0.3359 0.4364 -0.0142 0.0188  0.0280  138 ALA   A N   
362  C  CA  . ALA   A 45  ? 0.4830 0.3403 0.4507 -0.0176 0.0205  0.0381  138 ALA   A CA  
363  C  C   . ALA   A 45  ? 0.4937 0.3391 0.4674 -0.0165 0.0140  0.0454  138 ALA   A C   
364  O  O   . ALA   A 45  ? 0.5183 0.3570 0.4986 -0.0194 0.0145  0.0531  138 ALA   A O   
365  C  CB  . ALA   A 45  ? 0.4992 0.3670 0.4564 -0.0221 0.0250  0.0461  138 ALA   A CB  
366  N  N   . LYS   A 46  ? 0.4867 0.3298 0.4602 -0.0125 0.0082  0.0424  139 LYS   A N   
367  C  CA  . LYS   A 46  ? 0.4935 0.3273 0.4745 -0.0098 0.0018  0.0478  139 LYS   A CA  
368  C  C   . LYS   A 46  ? 0.4629 0.2892 0.4578 -0.0077 0.0018  0.0408  139 LYS   A C   
369  O  O   . LYS   A 46  ? 0.4263 0.2553 0.4230 -0.0075 0.0050  0.0320  139 LYS   A O   
370  C  CB  . LYS   A 46  ? 0.5130 0.3518 0.4885 -0.0064 -0.0045 0.0479  139 LYS   A CB  
371  C  CG  . LYS   A 46  ? 0.5408 0.3868 0.5022 -0.0078 -0.0069 0.0576  139 LYS   A CG  
372  C  CD  . LYS   A 46  ? 0.5665 0.4048 0.5283 -0.0099 -0.0078 0.0728  139 LYS   A CD  
373  C  CE  . LYS   A 46  ? 0.5927 0.4359 0.5426 -0.0093 -0.0138 0.0853  139 LYS   A CE  
374  N  NZ  . LYS   A 46  ? 0.6117 0.4719 0.5431 -0.0119 -0.0114 0.0830  139 LYS   A NZ  
375  N  N   . THR   A 47  ? 0.4613 0.2782 0.4654 -0.0058 -0.0018 0.0448  140 THR   A N   
376  C  CA  . THR   A 47  ? 0.4527 0.2632 0.4696 -0.0035 -0.0021 0.0380  140 THR   A CA  
377  C  C   . THR   A 47  ? 0.4453 0.2617 0.4643 0.0000  -0.0032 0.0291  140 THR   A C   
378  O  O   . THR   A 47  ? 0.4475 0.2674 0.4661 0.0032  -0.0075 0.0300  140 THR   A O   
379  C  CB  . THR   A 47  ? 0.4574 0.2565 0.4841 -0.0010 -0.0068 0.0431  140 THR   A CB  
380  O  OG1 . THR   A 47  ? 0.4646 0.2580 0.4888 -0.0060 -0.0057 0.0535  140 THR   A OG1 
381  C  CG2 . THR   A 47  ? 0.4469 0.2407 0.4861 0.0011  -0.0067 0.0341  140 THR   A CG2 
382  N  N   A CYS   A 48  ? 0.4479 0.2664 0.4694 -0.0008 0.0003  0.0216  141 CYS   A N   
383  N  N   B CYS   A 48  ? 0.4340 0.2526 0.4555 -0.0008 0.0003  0.0215  141 CYS   A N   
384  C  CA  A CYS   A 48  ? 0.4524 0.2766 0.4760 0.0010  0.0004  0.0144  141 CYS   A CA  
385  C  CA  B CYS   A 48  ? 0.4266 0.2508 0.4503 0.0010  0.0004  0.0143  141 CYS   A CA  
386  C  C   A CYS   A 48  ? 0.4399 0.2626 0.4723 0.0026  0.0011  0.0090  141 CYS   A C   
387  C  C   B CYS   A 48  ? 0.4262 0.2489 0.4586 0.0026  0.0011  0.0090  141 CYS   A C   
388  O  O   A CYS   A 48  ? 0.4404 0.2637 0.4727 0.0008  0.0040  0.0059  141 CYS   A O   
389  O  O   B CYS   A 48  ? 0.4257 0.2490 0.4580 0.0008  0.0040  0.0059  141 CYS   A O   
390  C  CB  A CYS   A 48  ? 0.4676 0.2961 0.4848 -0.0015 0.0038  0.0114  141 CYS   A CB  
391  C  CB  B CYS   A 48  ? 0.4203 0.2488 0.4379 -0.0014 0.0038  0.0111  141 CYS   A CB  
392  S  SG  A CYS   A 48  ? 0.5046 0.3384 0.5241 -0.0012 0.0038  0.0055  141 CYS   A SG  
393  S  SG  B CYS   A 48  ? 0.4209 0.2536 0.4278 -0.0029 0.0033  0.0133  141 CYS   A SG  
394  N  N   . PRO   A 49  ? 0.4334 0.2554 0.4738 0.0067  -0.0018 0.0071  142 PRO   A N   
395  C  CA  . PRO   A 49  ? 0.4297 0.2526 0.4777 0.0088  -0.0009 -0.0001 142 PRO   A CA  
396  C  C   . PRO   A 49  ? 0.4243 0.2575 0.4699 0.0077  0.0023  -0.0052 142 PRO   A C   
397  O  O   . PRO   A 49  ? 0.4254 0.2654 0.4701 0.0076  0.0021  -0.0048 142 PRO   A O   
398  C  CB  . PRO   A 49  ? 0.4359 0.2574 0.4936 0.0146  -0.0049 -0.0012 142 PRO   A CB  
399  C  CG  . PRO   A 49  ? 0.4459 0.2619 0.5007 0.0148  -0.0088 0.0083  142 PRO   A CG  
400  C  CD  . PRO   A 49  ? 0.4408 0.2629 0.4838 0.0103  -0.0066 0.0112  142 PRO   A CD  
401  N  N   . VAL   A 50  ? 0.4115 0.2460 0.4561 0.0061  0.0047  -0.0090 143 VAL   A N   
402  C  CA  . VAL   A 50  ? 0.4142 0.2586 0.4565 0.0052  0.0075  -0.0128 143 VAL   A CA  
403  C  C   . VAL   A 50  ? 0.4196 0.2678 0.4668 0.0077  0.0079  -0.0206 143 VAL   A C   
404  O  O   . VAL   A 50  ? 0.4434 0.2857 0.4922 0.0072  0.0069  -0.0229 143 VAL   A O   
405  C  CB  . VAL   A 50  ? 0.4066 0.2507 0.4415 0.0016  0.0093  -0.0095 143 VAL   A CB  
406  C  CG1 . VAL   A 50  ? 0.4148 0.2677 0.4467 0.0004  0.0115  -0.0109 143 VAL   A CG1 
407  C  CG2 . VAL   A 50  ? 0.4034 0.2440 0.4343 0.0000  0.0091  -0.0044 143 VAL   A CG2 
408  N  N   . GLN   A 51  ? 0.4247 0.2836 0.4751 0.0099  0.0094  -0.0255 144 GLN   A N   
409  C  CA  . GLN   A 51  ? 0.4238 0.2900 0.4781 0.0128  0.0105  -0.0354 144 GLN   A CA  
410  C  C   . GLN   A 51  ? 0.4266 0.3034 0.4719 0.0095  0.0136  -0.0363 144 GLN   A C   
411  O  O   . GLN   A 51  ? 0.4231 0.3061 0.4627 0.0062  0.0159  -0.0302 144 GLN   A O   
412  C  CB  . GLN   A 51  ? 0.4269 0.3026 0.4900 0.0175  0.0112  -0.0406 144 GLN   A CB  
413  C  CG  . GLN   A 51  ? 0.4315 0.2974 0.5037 0.0218  0.0069  -0.0382 144 GLN   A CG  
414  C  CD  . GLN   A 51  ? 0.4426 0.3210 0.5246 0.0268  0.0072  -0.0425 144 GLN   A CD  
415  O  OE1 . GLN   A 51  ? 0.4531 0.3483 0.5342 0.0252  0.0116  -0.0453 144 GLN   A OE1 
416  N  NE2 . GLN   A 51  ? 0.4534 0.3252 0.5459 0.0327  0.0026  -0.0423 144 GLN   A NE2 
417  N  N   . LEU   A 52  ? 0.4255 0.3039 0.4699 0.0100  0.0131  -0.0434 145 LEU   A N   
418  C  CA  . LEU   A 52  ? 0.4292 0.3211 0.4647 0.0079  0.0152  -0.0460 145 LEU   A CA  
419  C  C   . LEU   A 52  ? 0.4496 0.3560 0.4876 0.0114  0.0178  -0.0574 145 LEU   A C   
420  O  O   . LEU   A 52  ? 0.4541 0.3563 0.5010 0.0157  0.0159  -0.0683 145 LEU   A O   
421  C  CB  . LEU   A 52  ? 0.4266 0.3137 0.4595 0.0062  0.0121  -0.0480 145 LEU   A CB  
422  C  CG  . LEU   A 52  ? 0.4163 0.2896 0.4504 0.0038  0.0097  -0.0396 145 LEU   A CG  
423  C  CD1 . LEU   A 52  ? 0.4234 0.2967 0.4573 0.0018  0.0069  -0.0428 145 LEU   A CD1 
424  C  CD2 . LEU   A 52  ? 0.4077 0.2809 0.4357 0.0017  0.0113  -0.0286 145 LEU   A CD2 
425  N  N   . TRP   A 53  ? 0.4513 0.3744 0.4831 0.0097  0.0223  -0.0553 146 TRP   A N   
426  C  CA  . TRP   A 53  ? 0.4605 0.4032 0.4929 0.0125  0.0264  -0.0664 146 TRP   A CA  
427  C  C   . TRP   A 53  ? 0.4696 0.4272 0.4875 0.0091  0.0282  -0.0665 146 TRP   A C   
428  O  O   . TRP   A 53  ? 0.4621 0.4211 0.4704 0.0040  0.0289  -0.0536 146 TRP   A O   
429  C  CB  . TRP   A 53  ? 0.4575 0.4116 0.4953 0.0126  0.0309  -0.0637 146 TRP   A CB  
430  C  CG  . TRP   A 53  ? 0.4578 0.4012 0.5101 0.0172  0.0282  -0.0649 146 TRP   A CG  
431  C  CD1 . TRP   A 53  ? 0.4463 0.3721 0.5010 0.0159  0.0242  -0.0555 146 TRP   A CD1 
432  C  CD2 . TRP   A 53  ? 0.4612 0.4121 0.5272 0.0243  0.0291  -0.0757 146 TRP   A CD2 
433  N  NE1 . TRP   A 53  ? 0.4617 0.3836 0.5293 0.0212  0.0219  -0.0584 146 TRP   A NE1 
434  C  CE2 . TRP   A 53  ? 0.4600 0.3963 0.5360 0.0269  0.0245  -0.0705 146 TRP   A CE2 
435  C  CE3 . TRP   A 53  ? 0.4678 0.4371 0.5391 0.0294  0.0330  -0.0898 146 TRP   A CE3 
436  C  CZ2 . TRP   A 53  ? 0.4690 0.4076 0.5607 0.0347  0.0229  -0.0775 146 TRP   A CZ2 
437  C  CZ3 . TRP   A 53  ? 0.4755 0.4471 0.5638 0.0376  0.0322  -0.0984 146 TRP   A CZ3 
438  C  CH2 . TRP   A 53  ? 0.4696 0.4254 0.5684 0.0404  0.0267  -0.0916 146 TRP   A CH2 
439  N  N   . VAL   A 54  ? 0.4923 0.4606 0.5091 0.0122  0.0285  -0.0810 147 VAL   A N   
440  C  CA  . VAL   A 54  ? 0.5149 0.5017 0.5166 0.0097  0.0297  -0.0837 147 VAL   A CA  
441  C  C   . VAL   A 54  ? 0.5411 0.5511 0.5426 0.0133  0.0353  -0.0985 147 VAL   A C   
442  O  O   . VAL   A 54  ? 0.5301 0.5364 0.5459 0.0195  0.0354  -0.1119 147 VAL   A O   
443  C  CB  . VAL   A 54  ? 0.5142 0.4924 0.5133 0.0095  0.0232  -0.0887 147 VAL   A CB  
444  C  CG1 . VAL   A 54  ? 0.5013 0.4639 0.4982 0.0056  0.0191  -0.0732 147 VAL   A CG1 
445  C  CG2 . VAL   A 54  ? 0.5182 0.4836 0.5318 0.0141  0.0198  -0.1042 147 VAL   A CG2 
446  N  N   . ASP   A 55  ? 0.5703 0.6038 0.5566 0.0097  0.0398  -0.0954 148 ASP   A N   
447  C  CA  . ASP   A 55  ? 0.5956 0.6573 0.5775 0.0122  0.0461  -0.1100 148 ASP   A CA  
448  C  C   . ASP   A 55  ? 0.6031 0.6686 0.5807 0.0155  0.0419  -0.1280 148 ASP   A C   
449  O  O   . ASP   A 55  ? 0.6136 0.6934 0.5956 0.0209  0.0451  -0.1477 148 ASP   A O   
450  C  CB  . ASP   A 55  ? 0.6236 0.7097 0.5887 0.0057  0.0526  -0.0975 148 ASP   A CB  
451  C  CG  . ASP   A 55  ? 0.6347 0.7211 0.6062 0.0017  0.0578  -0.0830 148 ASP   A CG  
452  O  OD1 . ASP   A 55  ? 0.6491 0.7262 0.6385 0.0057  0.0582  -0.0877 148 ASP   A OD1 
453  O  OD2 . ASP   A 55  ? 0.6681 0.7641 0.6273 -0.0056 0.0609  -0.0667 148 ASP   A OD2 
454  N  N   A SER   A 56  ? 0.6002 0.6545 0.5706 0.0125  0.0348  -0.1225 149 SER   A N   
455  N  N   B SER   A 56  ? 0.6006 0.6549 0.5710 0.0125  0.0348  -0.1226 149 SER   A N   
456  C  CA  A SER   A 56  ? 0.6125 0.6694 0.5794 0.0139  0.0291  -0.1387 149 SER   A CA  
457  C  CA  B SER   A 56  ? 0.6131 0.6700 0.5802 0.0140  0.0291  -0.1389 149 SER   A CA  
458  C  C   A SER   A 56  ? 0.6039 0.6337 0.5798 0.0126  0.0207  -0.1341 149 SER   A C   
459  C  C   B SER   A 56  ? 0.6043 0.6341 0.5802 0.0126  0.0207  -0.1342 149 SER   A C   
460  O  O   A SER   A 56  ? 0.5955 0.6137 0.5696 0.0090  0.0190  -0.1151 149 SER   A O   
461  O  O   B SER   A 56  ? 0.5959 0.6141 0.5700 0.0090  0.0190  -0.1151 149 SER   A O   
462  C  CB  A SER   A 56  ? 0.6259 0.7088 0.5704 0.0103  0.0295  -0.1368 149 SER   A CB  
463  C  CB  B SER   A 56  ? 0.6272 0.7106 0.5719 0.0105  0.0296  -0.1377 149 SER   A CB  
464  O  OG  A SER   A 56  ? 0.6283 0.7371 0.5631 0.0097  0.0386  -0.1354 149 SER   A OG  
465  O  OG  B SER   A 56  ? 0.6175 0.6989 0.5511 0.0049  0.0284  -0.1138 149 SER   A OG  
466  N  N   . THR   A 57  ? 0.6108 0.6313 0.5972 0.0151  0.0158  -0.1517 150 THR   A N   
467  C  CA  . THR   A 57  ? 0.6195 0.6154 0.6175 0.0132  0.0084  -0.1498 150 THR   A CA  
468  C  C   . THR   A 57  ? 0.6265 0.6288 0.6124 0.0080  0.0032  -0.1409 150 THR   A C   
469  O  O   . THR   A 57  ? 0.6398 0.6604 0.6153 0.0071  0.0003  -0.1512 150 THR   A O   
470  C  CB  . THR   A 57  ? 0.6309 0.6179 0.6433 0.0163  0.0048  -0.1722 150 THR   A CB  
471  O  OG1 . THR   A 57  ? 0.6373 0.6228 0.6601 0.0228  0.0097  -0.1812 150 THR   A OG1 
472  C  CG2 . THR   A 57  ? 0.6317 0.5919 0.6591 0.0135  -0.0014 -0.1691 150 THR   A CG2 
473  N  N   . PRO   A 58  ? 0.6209 0.6100 0.6080 0.0050  0.0013  -0.1221 151 PRO   A N   
474  C  CA  . PRO   A 58  ? 0.6298 0.6229 0.6104 0.0015  -0.0048 -0.1149 151 PRO   A CA  
475  C  C   . PRO   A 58  ? 0.6395 0.6286 0.6298 -0.0001 -0.0117 -0.1300 151 PRO   A C   
476  O  O   . PRO   A 58  ? 0.6563 0.6305 0.6618 0.0007  -0.0119 -0.1413 151 PRO   A O   
477  C  CB  . PRO   A 58  ? 0.6114 0.5875 0.5969 0.0001  -0.0046 -0.0954 151 PRO   A CB  
478  C  CG  . PRO   A 58  ? 0.6109 0.5807 0.5987 0.0021  0.0023  -0.0895 151 PRO   A CG  
479  C  CD  . PRO   A 58  ? 0.6109 0.5828 0.6057 0.0055  0.0047  -0.1078 151 PRO   A CD  
480  N  N   . PRO   A 59  ? 0.6447 0.6471 0.6278 -0.0028 -0.0180 -0.1305 152 PRO   A N   
481  C  CA  . PRO   A 59  ? 0.6486 0.6492 0.6424 -0.0057 -0.0251 -0.1458 152 PRO   A CA  
482  C  C   . PRO   A 59  ? 0.6347 0.6117 0.6479 -0.0087 -0.0269 -0.1398 152 PRO   A C   
483  O  O   . PRO   A 59  ? 0.6090 0.5757 0.6238 -0.0085 -0.0242 -0.1225 152 PRO   A O   
484  C  CB  . PRO   A 59  ? 0.6577 0.6816 0.6378 -0.0075 -0.0316 -0.1437 152 PRO   A CB  
485  C  CG  . PRO   A 59  ? 0.6482 0.6755 0.6160 -0.0060 -0.0287 -0.1202 152 PRO   A CG  
486  C  CD  . PRO   A 59  ? 0.6476 0.6675 0.6133 -0.0033 -0.0194 -0.1161 152 PRO   A CD  
487  N  N   . PRO   A 60  ? 0.6366 0.6044 0.6653 -0.0121 -0.0313 -0.1543 153 PRO   A N   
488  C  CA  . PRO   A 60  ? 0.6137 0.5626 0.6600 -0.0166 -0.0330 -0.1473 153 PRO   A CA  
489  C  C   . PRO   A 60  ? 0.5839 0.5426 0.6270 -0.0189 -0.0360 -0.1329 153 PRO   A C   
490  O  O   . PRO   A 60  ? 0.5880 0.5678 0.6208 -0.0188 -0.0407 -0.1354 153 PRO   A O   
491  C  CB  . PRO   A 60  ? 0.6380 0.5816 0.6991 -0.0212 -0.0385 -0.1669 153 PRO   A CB  
492  C  CG  . PRO   A 60  ? 0.6612 0.6125 0.7153 -0.0166 -0.0374 -0.1854 153 PRO   A CG  
493  C  CD  . PRO   A 60  ? 0.6593 0.6342 0.6901 -0.0122 -0.0345 -0.1782 153 PRO   A CD  
494  N  N   . GLY   A 61  ? 0.5336 0.4787 0.5858 -0.0204 -0.0336 -0.1188 154 GLY   A N   
495  C  CA  . GLY   A 61  ? 0.5068 0.4605 0.5587 -0.0212 -0.0358 -0.1055 154 GLY   A CA  
496  C  C   . GLY   A 61  ? 0.4799 0.4351 0.5182 -0.0157 -0.0315 -0.0897 154 GLY   A C   
497  O  O   . GLY   A 61  ? 0.4618 0.4191 0.5018 -0.0149 -0.0322 -0.0778 154 GLY   A O   
498  N  N   . THR   A 62  ? 0.4670 0.4205 0.4940 -0.0122 -0.0270 -0.0898 155 THR   A N   
499  C  CA  . THR   A 62  ? 0.4510 0.3998 0.4691 -0.0085 -0.0217 -0.0748 155 THR   A CA  
500  C  C   . THR   A 62  ? 0.4234 0.3536 0.4529 -0.0094 -0.0183 -0.0659 155 THR   A C   
501  O  O   . THR   A 62  ? 0.3983 0.3163 0.4396 -0.0120 -0.0176 -0.0718 155 THR   A O   
502  C  CB  . THR   A 62  ? 0.4609 0.4099 0.4706 -0.0060 -0.0166 -0.0789 155 THR   A CB  
503  O  OG1 . THR   A 62  ? 0.4852 0.4543 0.4832 -0.0056 -0.0191 -0.0882 155 THR   A OG1 
504  C  CG2 . THR   A 62  ? 0.4497 0.3934 0.4530 -0.0039 -0.0113 -0.0643 155 THR   A CG2 
505  N  N   . ARG   A 63  ? 0.4080 0.3361 0.4339 -0.0073 -0.0166 -0.0521 156 ARG   A N   
506  C  CA  . ARG   A 63  ? 0.3994 0.3131 0.4340 -0.0078 -0.0133 -0.0442 156 ARG   A CA  
507  C  C   . ARG   A 63  ? 0.3882 0.2939 0.4156 -0.0050 -0.0085 -0.0349 156 ARG   A C   
508  O  O   . ARG   A 63  ? 0.3881 0.3009 0.4047 -0.0030 -0.0083 -0.0310 156 ARG   A O   
509  C  CB  . ARG   A 63  ? 0.3986 0.3186 0.4403 -0.0082 -0.0165 -0.0397 156 ARG   A CB  
510  C  CG  . ARG   A 63  ? 0.4037 0.3265 0.4586 -0.0132 -0.0195 -0.0483 156 ARG   A CG  
511  C  CD  . ARG   A 63  ? 0.4087 0.3480 0.4687 -0.0133 -0.0251 -0.0480 156 ARG   A CD  
512  N  NE  . ARG   A 63  ? 0.4109 0.3518 0.4730 -0.0093 -0.0241 -0.0372 156 ARG   A NE  
513  C  CZ  . ARG   A 63  ? 0.4142 0.3539 0.4888 -0.0107 -0.0216 -0.0343 156 ARG   A CZ  
514  N  NH1 . ARG   A 63  ? 0.4093 0.3447 0.4950 -0.0172 -0.0195 -0.0391 156 ARG   A NH1 
515  N  NH2 . ARG   A 63  ? 0.4099 0.3520 0.4859 -0.0055 -0.0208 -0.0263 156 ARG   A NH2 
516  N  N   . VAL   A 64  ? 0.3896 0.2818 0.4230 -0.0055 -0.0050 -0.0315 157 VAL   A N   
517  C  CA  . VAL   A 64  ? 0.3910 0.2749 0.4198 -0.0037 -0.0010 -0.0240 157 VAL   A CA  
518  C  C   . VAL   A 64  ? 0.3870 0.2647 0.4200 -0.0034 0.0002  -0.0169 157 VAL   A C   
519  O  O   . VAL   A 64  ? 0.3778 0.2504 0.4185 -0.0055 0.0012  -0.0181 157 VAL   A O   
520  C  CB  . VAL   A 64  ? 0.3955 0.2710 0.4267 -0.0040 0.0015  -0.0281 157 VAL   A CB  
521  C  CG1 . VAL   A 64  ? 0.3898 0.2610 0.4160 -0.0025 0.0047  -0.0218 157 VAL   A CG1 
522  C  CG2 . VAL   A 64  ? 0.4020 0.2837 0.4328 -0.0037 0.0002  -0.0388 157 VAL   A CG2 
523  N  N   . ARG   A 65  ? 0.3846 0.2633 0.4130 -0.0009 0.0001  -0.0099 158 ARG   A N   
524  C  CA  . ARG   A 65  ? 0.3734 0.2472 0.4057 0.0008  0.0013  -0.0047 158 ARG   A CA  
525  C  C   . ARG   A 65  ? 0.3712 0.2349 0.3994 0.0012  0.0045  -0.0009 158 ARG   A C   
526  O  O   . ARG   A 65  ? 0.3774 0.2409 0.3994 0.0009  0.0048  0.0010  158 ARG   A O   
527  C  CB  . ARG   A 65  ? 0.3791 0.2600 0.4116 0.0042  -0.0022 -0.0005 158 ARG   A CB  
528  C  CG  . ARG   A 65  ? 0.3783 0.2554 0.4169 0.0075  -0.0012 0.0027  158 ARG   A CG  
529  C  CD  . ARG   A 65  ? 0.3802 0.2634 0.4204 0.0122  -0.0060 0.0074  158 ARG   A CD  
530  N  NE  . ARG   A 65  ? 0.3831 0.2807 0.4259 0.0117  -0.0105 0.0045  158 ARG   A NE  
531  C  CZ  . ARG   A 65  ? 0.3750 0.2820 0.4288 0.0119  -0.0118 0.0004  158 ARG   A CZ  
532  N  NH1 . ARG   A 65  ? 0.3697 0.2744 0.4322 0.0126  -0.0079 -0.0008 158 ARG   A NH1 
533  N  NH2 . ARG   A 65  ? 0.3826 0.3034 0.4388 0.0107  -0.0168 -0.0028 158 ARG   A NH2 
534  N  N   . ALA   A 66  ? 0.3590 0.2167 0.3907 0.0013  0.0069  -0.0005 159 ALA   A N   
535  C  CA  . ALA   A 66  ? 0.3597 0.2090 0.3885 0.0018  0.0092  0.0017  159 ALA   A CA  
536  C  C   . ALA   A 66  ? 0.3605 0.2084 0.3928 0.0050  0.0094  0.0030  159 ALA   A C   
537  O  O   . ALA   A 66  ? 0.3552 0.2089 0.3933 0.0059  0.0100  0.0011  159 ALA   A O   
538  C  CB  . ALA   A 66  ? 0.3538 0.1991 0.3826 -0.0004 0.0113  0.0000  159 ALA   A CB  
539  N  N   . MET   A 67  ? 0.3722 0.2132 0.4025 0.0065  0.0092  0.0056  160 MET   A N   
540  C  CA  . MET   A 67  ? 0.3837 0.2206 0.4183 0.0107  0.0091  0.0054  160 MET   A CA  
541  C  C   . MET   A 67  ? 0.3795 0.2058 0.4115 0.0096  0.0100  0.0049  160 MET   A C   
542  O  O   . MET   A 67  ? 0.3838 0.2066 0.4120 0.0064  0.0092  0.0082  160 MET   A O   
543  C  CB  . MET   A 67  ? 0.4053 0.2435 0.4430 0.0145  0.0051  0.0101  160 MET   A CB  
544  C  CG  . MET   A 67  ? 0.4240 0.2561 0.4686 0.0203  0.0042  0.0097  160 MET   A CG  
545  S  SD  . MET   A 67  ? 0.4506 0.2818 0.4991 0.0257  -0.0019 0.0180  160 MET   A SD  
546  C  CE  . MET   A 67  ? 0.4445 0.2946 0.4974 0.0276  -0.0041 0.0164  160 MET   A CE  
547  N  N   . ALA   A 68  ? 0.3729 0.1962 0.4073 0.0118  0.0118  0.0000  161 ALA   A N   
548  C  CA  . ALA   A 68  ? 0.3769 0.1903 0.4100 0.0108  0.0119  -0.0026 161 ALA   A CA  
549  C  C   . ALA   A 68  ? 0.3909 0.1949 0.4306 0.0153  0.0095  -0.0020 161 ALA   A C   
550  O  O   . ALA   A 68  ? 0.3951 0.2027 0.4410 0.0210  0.0091  -0.0030 161 ALA   A O   
551  C  CB  . ALA   A 68  ? 0.3766 0.1931 0.4072 0.0106  0.0149  -0.0095 161 ALA   A CB  
552  N  N   . ILE   A 69  ? 0.4092 0.2019 0.4490 0.0126  0.0077  0.0001  162 ILE   A N   
553  C  CA  . ILE   A 69  ? 0.4331 0.2117 0.4804 0.0161  0.0051  -0.0003 162 ILE   A CA  
554  C  C   . ILE   A 69  ? 0.4500 0.2194 0.4968 0.0118  0.0053  -0.0065 162 ILE   A C   
555  O  O   . ILE   A 69  ? 0.4613 0.2359 0.5020 0.0057  0.0065  -0.0065 162 ILE   A O   
556  C  CB  . ILE   A 69  ? 0.4407 0.2132 0.4899 0.0159  0.0014  0.0114  162 ILE   A CB  
557  C  CG1 . ILE   A 69  ? 0.4416 0.2135 0.4849 0.0075  0.0017  0.0184  162 ILE   A CG1 
558  C  CG2 . ILE   A 69  ? 0.4320 0.2160 0.4815 0.0205  0.0001  0.0161  162 ILE   A CG2 
559  C  CD1 . ILE   A 69  ? 0.4537 0.2195 0.4977 0.0063  -0.0014 0.0311  162 ILE   A CD1 
560  N  N   . TYR   A 70  ? 0.4679 0.2248 0.5222 0.0152  0.0037  -0.0124 163 TYR   A N   
561  C  CA  . TYR   A 70  ? 0.4805 0.2259 0.5368 0.0106  0.0025  -0.0190 163 TYR   A CA  
562  C  C   . TYR   A 70  ? 0.4938 0.2292 0.5523 0.0035  0.0000  -0.0082 163 TYR   A C   
563  O  O   . TYR   A 70  ? 0.5119 0.2422 0.5734 0.0053  -0.0019 0.0027  163 TYR   A O   
564  C  CB  . TYR   A 70  ? 0.4910 0.2255 0.5560 0.0173  0.0015  -0.0303 163 TYR   A CB  
565  C  CG  . TYR   A 70  ? 0.4800 0.2284 0.5409 0.0221  0.0055  -0.0425 163 TYR   A CG  
566  C  CD1 . TYR   A 70  ? 0.4752 0.2330 0.5265 0.0172  0.0075  -0.0495 163 TYR   A CD1 
567  C  CD2 . TYR   A 70  ? 0.4725 0.2271 0.5388 0.0312  0.0073  -0.0460 163 TYR   A CD2 
568  C  CE1 . TYR   A 70  ? 0.4612 0.2335 0.5067 0.0206  0.0116  -0.0586 163 TYR   A CE1 
569  C  CE2 . TYR   A 70  ? 0.4687 0.2389 0.5310 0.0344  0.0121  -0.0563 163 TYR   A CE2 
570  C  CZ  . TYR   A 70  ? 0.4603 0.2391 0.5112 0.0288  0.0145  -0.0620 163 TYR   A CZ  
571  O  OH  . TYR   A 70  ? 0.4623 0.2575 0.5074 0.0311  0.0195  -0.0702 163 TYR   A OH  
572  N  N   . LYS   A 71  ? 0.4922 0.2270 0.5490 -0.0045 -0.0001 -0.0107 164 LYS   A N   
573  C  CA  . LYS   A 71  ? 0.5075 0.2373 0.5666 -0.0133 -0.0013 -0.0006 164 LYS   A CA  
574  C  C   . LYS   A 71  ? 0.5278 0.2354 0.5981 -0.0146 -0.0049 0.0010  164 LYS   A C   
575  O  O   . LYS   A 71  ? 0.5384 0.2394 0.6113 -0.0186 -0.0060 0.0145  164 LYS   A O   
576  C  CB  . LYS   A 71  ? 0.5148 0.2543 0.5708 -0.0210 -0.0004 -0.0051 164 LYS   A CB  
577  C  CG  . LYS   A 71  ? 0.5225 0.2620 0.5820 -0.0310 -0.0005 0.0041  164 LYS   A CG  
578  C  CD  . LYS   A 71  ? 0.5307 0.2828 0.5894 -0.0374 -0.0001 -0.0012 164 LYS   A CD  
579  C  CE  . LYS   A 71  ? 0.5449 0.2915 0.6131 -0.0482 -0.0015 0.0015  164 LYS   A CE  
580  N  NZ  . LYS   A 71  ? 0.5444 0.3058 0.6133 -0.0534 -0.0020 -0.0053 164 LYS   A NZ  
581  N  N   . GLN   A 72  ? 0.5343 0.2311 0.6106 -0.0115 -0.0066 -0.0124 165 GLN   A N   
582  C  CA  . GLN   A 72  ? 0.5674 0.2400 0.6566 -0.0131 -0.0107 -0.0144 165 GLN   A CA  
583  C  C   . GLN   A 72  ? 0.5744 0.2339 0.6705 -0.0045 -0.0130 -0.0059 165 GLN   A C   
584  O  O   . GLN   A 72  ? 0.5678 0.2363 0.6613 0.0056  -0.0117 -0.0096 165 GLN   A O   
585  C  CB  . GLN   A 72  ? 0.5837 0.2520 0.6762 -0.0110 -0.0116 -0.0347 165 GLN   A CB  
586  C  CG  . GLN   A 72  ? 0.5859 0.2655 0.6732 -0.0202 -0.0112 -0.0421 165 GLN   A CG  
587  C  CD  . GLN   A 72  ? 0.6048 0.2896 0.6887 -0.0166 -0.0113 -0.0621 165 GLN   A CD  
588  O  OE1 . GLN   A 72  ? 0.6028 0.2982 0.6801 -0.0077 -0.0085 -0.0684 165 GLN   A OE1 
589  N  NE2 . GLN   A 72  ? 0.6273 0.3071 0.7156 -0.0243 -0.0146 -0.0722 165 GLN   A NE2 
590  N  N   . SER   A 73  ? 0.5934 0.2324 0.6990 -0.0085 -0.0168 0.0050  166 SER   A N   
591  C  CA  . SER   A 73  ? 0.6039 0.2297 0.7162 -0.0008 -0.0204 0.0173  166 SER   A CA  
592  C  C   . SER   A 73  ? 0.6190 0.2340 0.7417 0.0123  -0.0227 0.0032  166 SER   A C   
593  O  O   . SER   A 73  ? 0.6086 0.2248 0.7341 0.0228  -0.0246 0.0091  166 SER   A O   
594  C  CB  . SER   A 73  ? 0.6250 0.2303 0.7450 -0.0094 -0.0240 0.0331  166 SER   A CB  
595  O  OG  . SER   A 73  ? 0.6309 0.2161 0.7628 -0.0154 -0.0264 0.0229  166 SER   A OG  
596  N  N   . GLN   A 74  ? 0.6372 0.2447 0.7657 0.0120  -0.0227 -0.0157 167 GLN   A N   
597  C  CA  . GLN   A 74  ? 0.6596 0.2573 0.7992 0.0244  -0.0243 -0.0325 167 GLN   A CA  
598  C  C   . GLN   A 74  ? 0.6337 0.2572 0.7649 0.0337  -0.0192 -0.0431 167 GLN   A C   
599  O  O   . GLN   A 74  ? 0.6345 0.2554 0.7748 0.0456  -0.0195 -0.0551 167 GLN   A O   
600  C  CB  . GLN   A 74  ? 0.6941 0.2754 0.8422 0.0200  -0.0262 -0.0504 167 GLN   A CB  
601  C  CG  . GLN   A 74  ? 0.6873 0.2877 0.8231 0.0122  -0.0223 -0.0636 167 GLN   A CG  
602  C  CD  . GLN   A 74  ? 0.7007 0.2993 0.8339 -0.0035 -0.0233 -0.0546 167 GLN   A CD  
603  O  OE1 . GLN   A 74  ? 0.7288 0.3254 0.8611 -0.0095 -0.0237 -0.0346 167 GLN   A OE1 
604  N  NE2 . GLN   A 74  ? 0.7039 0.3074 0.8348 -0.0105 -0.0234 -0.0697 167 GLN   A NE2 
605  N  N   . HIS   A 75  ? 0.6067 0.2543 0.7224 0.0286  -0.0147 -0.0387 168 HIS   A N   
606  C  CA  . HIS   A 75  ? 0.5874 0.2597 0.6946 0.0349  -0.0095 -0.0470 168 HIS   A CA  
607  C  C   . HIS   A 75  ? 0.5713 0.2589 0.6723 0.0367  -0.0083 -0.0320 168 HIS   A C   
608  O  O   . HIS   A 75  ? 0.5573 0.2655 0.6527 0.0407  -0.0041 -0.0369 168 HIS   A O   
609  C  CB  . HIS   A 75  ? 0.5764 0.2634 0.6710 0.0273  -0.0056 -0.0568 168 HIS   A CB  
610  C  CG  . HIS   A 75  ? 0.5924 0.2699 0.6911 0.0264  -0.0067 -0.0749 168 HIS   A CG  
611  N  ND1 . HIS   A 75  ? 0.6028 0.2764 0.7098 0.0366  -0.0062 -0.0912 168 HIS   A ND1 
612  C  CD2 . HIS   A 75  ? 0.5983 0.2714 0.6945 0.0167  -0.0084 -0.0808 168 HIS   A CD2 
613  C  CE1 . HIS   A 75  ? 0.6142 0.2804 0.7224 0.0330  -0.0077 -0.1071 168 HIS   A CE1 
614  N  NE2 . HIS   A 75  ? 0.6176 0.2834 0.7194 0.0205  -0.0094 -0.1007 168 HIS   A NE2 
615  N  N   . MET   A 76  ? 0.5750 0.2541 0.6770 0.0332  -0.0119 -0.0147 169 MET   A N   
616  C  CA  . MET   A 76  ? 0.5587 0.2539 0.6514 0.0312  -0.0110 -0.0006 169 MET   A CA  
617  C  C   . MET   A 76  ? 0.5451 0.2512 0.6421 0.0423  -0.0117 0.0002  169 MET   A C   
618  O  O   . MET   A 76  ? 0.5115 0.2366 0.6003 0.0413  -0.0095 0.0043  169 MET   A O   
619  C  CB  . MET   A 76  ? 0.5790 0.2632 0.6710 0.0246  -0.0145 0.0172  169 MET   A CB  
620  C  CG  . MET   A 76  ? 0.5829 0.2718 0.6660 0.0119  -0.0118 0.0203  169 MET   A CG  
621  S  SD  . MET   A 76  ? 0.5978 0.2964 0.6715 0.0061  -0.0121 0.0406  169 MET   A SD  
622  C  CE  . MET   A 76  ? 0.6226 0.2958 0.7072 0.0073  -0.0184 0.0550  169 MET   A CE  
623  N  N   A THR   A 77  ? 0.5531 0.2478 0.6641 0.0526  -0.0149 -0.0041 170 THR   A N   
624  N  N   B THR   A 77  ? 0.5557 0.2503 0.6667 0.0526  -0.0149 -0.0041 170 THR   A N   
625  C  CA  A THR   A 77  ? 0.5507 0.2563 0.6701 0.0646  -0.0164 -0.0043 170 THR   A CA  
626  C  CA  B THR   A 77  ? 0.5552 0.2605 0.6748 0.0646  -0.0164 -0.0044 170 THR   A CA  
627  C  C   A THR   A 77  ? 0.5383 0.2634 0.6576 0.0689  -0.0101 -0.0208 170 THR   A C   
628  C  C   B THR   A 77  ? 0.5407 0.2658 0.6601 0.0689  -0.0101 -0.0208 170 THR   A C   
629  O  O   A THR   A 77  ? 0.5408 0.2803 0.6673 0.0774  -0.0101 -0.0220 170 THR   A O   
630  O  O   B THR   A 77  ? 0.5432 0.2827 0.6697 0.0774  -0.0101 -0.0220 170 THR   A O   
631  C  CB  A THR   A 77  ? 0.5736 0.2590 0.7105 0.0752  -0.0228 -0.0031 170 THR   A CB  
632  C  CB  B THR   A 77  ? 0.5815 0.2658 0.7185 0.0749  -0.0227 -0.0034 170 THR   A CB  
633  O  OG1 A THR   A 77  ? 0.5855 0.2623 0.7310 0.0795  -0.0204 -0.0220 170 THR   A OG1 
634  O  OG1 B THR   A 77  ? 0.5846 0.2825 0.7322 0.0877  -0.0237 -0.0072 170 THR   A OG1 
635  C  CG2 A THR   A 77  ? 0.5913 0.2537 0.7293 0.0700  -0.0289 0.0137  170 THR   A CG2 
636  C  CG2 B THR   A 77  ? 0.6000 0.2656 0.7453 0.0757  -0.0221 -0.0186 170 THR   A CG2 
637  N  N   . GLU   A 78  ? 0.5320 0.2591 0.6441 0.0631  -0.0052 -0.0327 171 GLU   A N   
638  C  CA  . GLU   A 78  ? 0.5237 0.2710 0.6326 0.0654  0.0014  -0.0467 171 GLU   A CA  
639  C  C   . GLU   A 78  ? 0.5010 0.2683 0.5972 0.0584  0.0049  -0.0394 171 GLU   A C   
640  O  O   . GLU   A 78  ? 0.4944 0.2580 0.5805 0.0492  0.0041  -0.0313 171 GLU   A O   
641  C  CB  . GLU   A 78  ? 0.5378 0.2794 0.6430 0.0624  0.0042  -0.0618 171 GLU   A CB  
642  C  CG  . GLU   A 78  ? 0.5401 0.3036 0.6407 0.0648  0.0114  -0.0754 171 GLU   A CG  
643  C  CD  . GLU   A 78  ? 0.5634 0.3238 0.6611 0.0644  0.0137  -0.0930 171 GLU   A CD  
644  O  OE1 . GLU   A 78  ? 0.5949 0.3376 0.7038 0.0698  0.0104  -0.1022 171 GLU   A OE1 
645  O  OE2 . GLU   A 78  ? 0.5650 0.3405 0.6489 0.0586  0.0183  -0.0976 171 GLU   A OE2 
646  N  N   . VAL   A 79  ? 0.4884 0.2762 0.5870 0.0624  0.0086  -0.0425 172 VAL   A N   
647  C  CA  . VAL   A 79  ? 0.4752 0.2811 0.5639 0.0557  0.0120  -0.0371 172 VAL   A CA  
648  C  C   . VAL   A 79  ? 0.4744 0.2848 0.5505 0.0483  0.0171  -0.0434 172 VAL   A C   
649  O  O   . VAL   A 79  ? 0.4813 0.2956 0.5580 0.0512  0.0209  -0.0555 172 VAL   A O   
650  C  CB  . VAL   A 79  ? 0.4669 0.2936 0.5642 0.0611  0.0145  -0.0389 172 VAL   A CB  
651  C  CG1 . VAL   A 79  ? 0.4513 0.2942 0.5398 0.0530  0.0182  -0.0348 172 VAL   A CG1 
652  C  CG2 . VAL   A 79  ? 0.4715 0.2966 0.5809 0.0685  0.0082  -0.0316 172 VAL   A CG2 
653  N  N   . VAL   A 80  ? 0.4764 0.2875 0.5415 0.0397  0.0169  -0.0357 173 VAL   A N   
654  C  CA  . VAL   A 80  ? 0.4727 0.2896 0.5257 0.0329  0.0205  -0.0391 173 VAL   A CA  
655  C  C   . VAL   A 80  ? 0.4724 0.3087 0.5237 0.0324  0.0258  -0.0400 173 VAL   A C   
656  O  O   . VAL   A 80  ? 0.4499 0.2929 0.5032 0.0307  0.0252  -0.0324 173 VAL   A O   
657  C  CB  . VAL   A 80  ? 0.4618 0.2727 0.5064 0.0250  0.0179  -0.0305 173 VAL   A CB  
658  C  CG1 . VAL   A 80  ? 0.4578 0.2749 0.4916 0.0195  0.0204  -0.0334 173 VAL   A CG1 
659  C  CG2 . VAL   A 80  ? 0.4679 0.2616 0.5154 0.0239  0.0133  -0.0279 173 VAL   A CG2 
660  N  N   . ARG   A 81  ? 0.4771 0.3227 0.5246 0.0331  0.0307  -0.0490 174 ARG   A N   
661  C  CA  . ARG   A 81  ? 0.4900 0.3555 0.5352 0.0313  0.0369  -0.0494 174 ARG   A CA  
662  C  C   . ARG   A 81  ? 0.4917 0.3628 0.5230 0.0268  0.0404  -0.0537 174 ARG   A C   
663  O  O   . ARG   A 81  ? 0.5021 0.3634 0.5280 0.0269  0.0379  -0.0598 174 ARG   A O   
664  C  CB  . ARG   A 81  ? 0.5034 0.3814 0.5613 0.0391  0.0406  -0.0569 174 ARG   A CB  
665  C  CG  . ARG   A 81  ? 0.5344 0.4060 0.5971 0.0469  0.0406  -0.0700 174 ARG   A CG  
666  C  CD  . ARG   A 81  ? 0.5508 0.4365 0.6279 0.0562  0.0446  -0.0790 174 ARG   A CD  
667  N  NE  . ARG   A 81  ? 0.5560 0.4344 0.6494 0.0639  0.0392  -0.0759 174 ARG   A NE  
668  C  CZ  . ARG   A 81  ? 0.5641 0.4528 0.6665 0.0645  0.0379  -0.0679 174 ARG   A CZ  
669  N  NH1 . ARG   A 81  ? 0.5474 0.4524 0.6453 0.0570  0.0418  -0.0621 174 ARG   A NH1 
670  N  NH2 . ARG   A 81  ? 0.5710 0.4533 0.6875 0.0727  0.0319  -0.0655 174 ARG   A NH2 
671  N  N   . ARG   A 82  ? 0.4809 0.3680 0.5068 0.0226  0.0457  -0.0503 175 ARG   A N   
672  C  CA  . ARG   A 82  ? 0.4842 0.3808 0.4956 0.0187  0.0494  -0.0529 175 ARG   A CA  
673  C  C   . ARG   A 82  ? 0.5025 0.4083 0.5140 0.0247  0.0538  -0.0680 175 ARG   A C   
674  O  O   . ARG   A 82  ? 0.4972 0.4071 0.5223 0.0316  0.0559  -0.0745 175 ARG   A O   
675  C  CB  . ARG   A 82  ? 0.4742 0.3854 0.4813 0.0124  0.0542  -0.0435 175 ARG   A CB  
676  C  CG  . ARG   A 82  ? 0.4588 0.3603 0.4666 0.0069  0.0499  -0.0305 175 ARG   A CG  
677  C  CD  . ARG   A 82  ? 0.4631 0.3772 0.4694 0.0004  0.0546  -0.0218 175 ARG   A CD  
678  N  NE  . ARG   A 82  ? 0.4673 0.3842 0.4582 -0.0045 0.0554  -0.0164 175 ARG   A NE  
679  C  CZ  . ARG   A 82  ? 0.4734 0.4007 0.4598 -0.0110 0.0596  -0.0072 175 ARG   A CZ  
680  N  NH1 . ARG   A 82  ? 0.4697 0.4068 0.4668 -0.0140 0.0643  -0.0038 175 ARG   A NH1 
681  N  NH2 . ARG   A 82  ? 0.4794 0.4075 0.4509 -0.0149 0.0588  -0.0008 175 ARG   A NH2 
682  N  N   . CYS   A 83  ? 0.5146 0.4246 0.5118 0.0225  0.0547  -0.0738 176 CYS   A N   
683  C  CA  . CYS   A 83  ? 0.5439 0.4663 0.5376 0.0273  0.0597  -0.0899 176 CYS   A CA  
684  C  C   . CYS   A 83  ? 0.5544 0.5025 0.5477 0.0268  0.0693  -0.0893 176 CYS   A C   
685  O  O   . CYS   A 83  ? 0.5553 0.5105 0.5460 0.0202  0.0714  -0.0753 176 CYS   A O   
686  C  CB  . CYS   A 83  ? 0.5562 0.4782 0.5327 0.0236  0.0571  -0.0950 176 CYS   A CB  
687  S  SG  . CYS   A 83  ? 0.5548 0.4922 0.5112 0.0144  0.0593  -0.0812 176 CYS   A SG  
688  N  N   . PRO   A 84  ? 0.5802 0.5434 0.5773 0.0335  0.0756  -0.1047 177 PRO   A N   
689  C  CA  . PRO   A 84  ? 0.5866 0.5786 0.5824 0.0321  0.0861  -0.1049 177 PRO   A CA  
690  C  C   . PRO   A 84  ? 0.5941 0.5981 0.5702 0.0212  0.0891  -0.0914 177 PRO   A C   
691  O  O   . PRO   A 84  ? 0.5868 0.6016 0.5661 0.0156  0.0934  -0.0789 177 PRO   A O   
692  C  CB  . PRO   A 84  ? 0.6066 0.6110 0.6027 0.0406  0.0911  -0.1269 177 PRO   A CB  
693  C  CG  . PRO   A 84  ? 0.6037 0.5824 0.6146 0.0493  0.0830  -0.1365 177 PRO   A CG  
694  C  CD  . PRO   A 84  ? 0.5920 0.5458 0.5964 0.0426  0.0733  -0.1232 177 PRO   A CD  
695  N  N   . HIS   A 85  ? 0.6012 0.6018 0.5584 0.0183  0.0857  -0.0933 178 HIS   A N   
696  C  CA  . HIS   A 85  ? 0.6099 0.6226 0.5460 0.0092  0.0875  -0.0809 178 HIS   A CA  
697  C  C   . HIS   A 85  ? 0.5963 0.5990 0.5358 0.0017  0.0845  -0.0593 178 HIS   A C   
698  O  O   . HIS   A 85  ? 0.6023 0.6207 0.5367 -0.0050 0.0907  -0.0476 178 HIS   A O   
699  C  CB  . HIS   A 85  ? 0.6281 0.6346 0.5464 0.0083  0.0809  -0.0864 178 HIS   A CB  
700  C  CG  . HIS   A 85  ? 0.6352 0.6482 0.5340 -0.0001 0.0793  -0.0701 178 HIS   A CG  
701  N  ND1 . HIS   A 85  ? 0.6595 0.6985 0.5423 -0.0046 0.0873  -0.0659 178 HIS   A ND1 
702  C  CD2 . HIS   A 85  ? 0.6369 0.6347 0.5300 -0.0046 0.0705  -0.0565 178 HIS   A CD2 
703  C  CE1 . HIS   A 85  ? 0.6658 0.7039 0.5333 -0.0115 0.0830  -0.0492 178 HIS   A CE1 
704  N  NE2 . HIS   A 85  ? 0.6580 0.6708 0.5325 -0.0110 0.0725  -0.0438 178 HIS   A NE2 
705  N  N   . HIS   A 86  ? 0.5774 0.5554 0.5251 0.0024  0.0755  -0.0544 179 HIS   A N   
706  C  CA  . HIS   A 86  ? 0.5751 0.5415 0.5259 -0.0038 0.0715  -0.0362 179 HIS   A CA  
707  C  C   . HIS   A 86  ? 0.5690 0.5412 0.5366 -0.0049 0.0762  -0.0313 179 HIS   A C   
708  O  O   . HIS   A 86  ? 0.5608 0.5339 0.5286 -0.0122 0.0771  -0.0170 179 HIS   A O   
709  C  CB  . HIS   A 86  ? 0.5555 0.4975 0.5096 -0.0023 0.0613  -0.0347 179 HIS   A CB  
710  C  CG  . HIS   A 86  ? 0.5615 0.5004 0.4994 -0.0050 0.0559  -0.0319 179 HIS   A CG  
711  N  ND1 . HIS   A 86  ? 0.5609 0.4896 0.4967 -0.0018 0.0497  -0.0417 179 HIS   A ND1 
712  C  CD2 . HIS   A 86  ? 0.5643 0.5096 0.4882 -0.0106 0.0553  -0.0200 179 HIS   A CD2 
713  C  CE1 . HIS   A 86  ? 0.5831 0.5138 0.5047 -0.0052 0.0452  -0.0366 179 HIS   A CE1 
714  N  NE2 . HIS   A 86  ? 0.5700 0.5108 0.4834 -0.0101 0.0484  -0.0230 179 HIS   A NE2 
715  N  N   . GLU   A 87  ? 0.5734 0.5494 0.5555 0.0020  0.0787  -0.0430 180 GLU   A N   
716  C  CA  . GLU   A 87  ? 0.5789 0.5644 0.5790 0.0019  0.0828  -0.0404 180 GLU   A CA  
717  C  C   . GLU   A 87  ? 0.5999 0.6105 0.5959 -0.0053 0.0927  -0.0341 180 GLU   A C   
718  O  O   . GLU   A 87  ? 0.5987 0.6127 0.6047 -0.0115 0.0941  -0.0237 180 GLU   A O   
719  C  CB  . GLU   A 87  ? 0.5757 0.5624 0.5912 0.0125  0.0830  -0.0550 180 GLU   A CB  
720  C  CG  . GLU   A 87  ? 0.5693 0.5684 0.6047 0.0136  0.0861  -0.0536 180 GLU   A CG  
721  C  CD  . GLU   A 87  ? 0.5711 0.5753 0.6224 0.0254  0.0868  -0.0681 180 GLU   A CD  
722  O  OE1 . GLU   A 87  ? 0.5733 0.6013 0.6364 0.0275  0.0942  -0.0729 180 GLU   A OE1 
723  O  OE2 . GLU   A 87  ? 0.5627 0.5474 0.6156 0.0325  0.0800  -0.0743 180 GLU   A OE2 
724  N  N   . ARG   A 88  ? 0.6202 0.6480 0.6012 -0.0057 0.0990  -0.0395 181 ARG   A N   
725  C  CA  . ARG   A 88  ? 0.6430 0.6984 0.6180 -0.0130 0.1099  -0.0334 181 ARG   A CA  
726  C  C   . ARG   A 88  ? 0.6509 0.7030 0.6078 -0.0237 0.1085  -0.0150 181 ARG   A C   
727  O  O   . ARG   A 88  ? 0.6579 0.7304 0.6106 -0.0319 0.1170  -0.0055 181 ARG   A O   
728  C  CB  . ARG   A 88  ? 0.6639 0.7435 0.6311 -0.0075 0.1183  -0.0496 181 ARG   A CB  
729  C  CG  . ARG   A 88  ? 0.6674 0.7561 0.6555 0.0030  0.1218  -0.0669 181 ARG   A CG  
730  C  CD  . ARG   A 88  ? 0.6933 0.7987 0.6735 0.0109  0.1276  -0.0868 181 ARG   A CD  
731  N  NE  . ARG   A 88  ? 0.7012 0.8181 0.7031 0.0219  0.1318  -0.1034 181 ARG   A NE  
732  C  CZ  . ARG   A 88  ? 0.7305 0.8614 0.7317 0.0312  0.1369  -0.1243 181 ARG   A CZ  
733  N  NH1 . ARG   A 88  ? 0.7519 0.8880 0.7303 0.0302  0.1383  -0.1318 181 ARG   A NH1 
734  N  NH2 . ARG   A 88  ? 0.7376 0.8785 0.7617 0.0421  0.1402  -0.1385 181 ARG   A NH2 
735  N  N   . CYS   A 89  ? 0.6472 0.6763 0.5944 -0.0239 0.0986  -0.0094 182 CYS   A N   
736  C  CA  . CYS   A 89  ? 0.6537 0.6763 0.5870 -0.0328 0.0954  0.0096  182 CYS   A CA  
737  C  C   . CYS   A 89  ? 0.6566 0.6729 0.6046 -0.0405 0.0959  0.0243  182 CYS   A C   
738  O  O   . CYS   A 89  ? 0.6650 0.6689 0.6312 -0.0373 0.0921  0.0200  182 CYS   A O   
739  C  CB  . CYS   A 89  ? 0.6476 0.6467 0.5730 -0.0300 0.0839  0.0114  182 CYS   A CB  
740  S  SG  . CYS   A 89  ? 0.6527 0.6598 0.5541 -0.0262 0.0814  0.0017  182 CYS   A SG  
741  N  N   . SER   A 90  ? 0.6801 0.7051 0.6211 -0.0508 0.1002  0.0410  183 SER   A N   
742  C  CA  . SER   A 90  ? 0.6835 0.7065 0.6404 -0.0600 0.1025  0.0539  183 SER   A CA  
743  C  C   . SER   A 90  ? 0.6681 0.6607 0.6306 -0.0614 0.0916  0.0636  183 SER   A C   
744  O  O   . SER   A 90  ? 0.6842 0.6703 0.6449 -0.0704 0.0907  0.0810  183 SER   A O   
745  C  CB  . SER   A 90  ? 0.7143 0.7579 0.6626 -0.0711 0.1118  0.0684  183 SER   A CB  
746  O  OG  . SER   A 90  ? 0.7375 0.8119 0.6875 -0.0699 0.1233  0.0573  183 SER   A OG  
747  N  N   . ASP   A 91  ? 0.6522 0.6277 0.6225 -0.0529 0.0839  0.0527  184 ASP   A N   
748  C  CA  . ASP   A 91  ? 0.6329 0.5814 0.6053 -0.0513 0.0731  0.0576  184 ASP   A CA  
749  C  C   . ASP   A 91  ? 0.6190 0.5566 0.6124 -0.0514 0.0701  0.0542  184 ASP   A C   
750  O  O   . ASP   A 91  ? 0.6005 0.5176 0.5975 -0.0506 0.0622  0.0578  184 ASP   A O   
751  C  CB  . ASP   A 91  ? 0.6211 0.5610 0.5836 -0.0421 0.0668  0.0477  184 ASP   A CB  
752  C  CG  . ASP   A 91  ? 0.6015 0.5436 0.5722 -0.0338 0.0671  0.0303  184 ASP   A CG  
753  O  OD1 . ASP   A 91  ? 0.5991 0.5442 0.5857 -0.0336 0.0695  0.0262  184 ASP   A OD1 
754  O  OD2 . ASP   A 91  ? 0.5848 0.5249 0.5468 -0.0278 0.0643  0.0213  184 ASP   A OD2 
755  N  N   . SER   A 92  ? 0.6230 0.5754 0.6296 -0.0517 0.0758  0.0469  185 SER   A N   
756  C  CA  . SER   A 92  ? 0.6158 0.5626 0.6426 -0.0529 0.0730  0.0441  185 SER   A CA  
757  C  C   . SER   A 92  ? 0.6275 0.5590 0.6593 -0.0618 0.0692  0.0570  185 SER   A C   
758  O  O   . SER   A 92  ? 0.6596 0.5956 0.6866 -0.0706 0.0735  0.0699  185 SER   A O   
759  C  CB  . SER   A 92  ? 0.6225 0.5923 0.6630 -0.0544 0.0804  0.0382  185 SER   A CB  
760  O  OG  . SER   A 92  ? 0.6527 0.6405 0.6903 -0.0636 0.0894  0.0472  185 SER   A OG  
761  N  N   . ASP   A 93  ? 0.6136 0.5277 0.6551 -0.0598 0.0616  0.0538  186 ASP   A N   
762  C  CA  . ASP   A 93  ? 0.6117 0.5089 0.6619 -0.0670 0.0570  0.0624  186 ASP   A CA  
763  C  C   . ASP   A 93  ? 0.6001 0.5056 0.6701 -0.0742 0.0589  0.0601  186 ASP   A C   
764  O  O   . ASP   A 93  ? 0.6182 0.5094 0.6988 -0.0800 0.0544  0.0635  186 ASP   A O   
765  C  CB  . ASP   A 93  ? 0.6073 0.4833 0.6564 -0.0601 0.0478  0.0579  186 ASP   A CB  
766  C  CG  . ASP   A 93  ? 0.5914 0.4681 0.6488 -0.0537 0.0444  0.0444  186 ASP   A CG  
767  O  OD1 . ASP   A 93  ? 0.5876 0.4806 0.6504 -0.0524 0.0482  0.0379  186 ASP   A OD1 
768  O  OD2 . ASP   A 93  ? 0.6048 0.4668 0.6635 -0.0499 0.0378  0.0408  186 ASP   A OD2 
769  N  N   . GLY   A 94  ? 0.5778 0.5058 0.6541 -0.0734 0.0649  0.0532  187 GLY   A N   
770  C  CA  . GLY   A 94  ? 0.5640 0.5054 0.6606 -0.0799 0.0669  0.0500  187 GLY   A CA  
771  C  C   . GLY   A 94  ? 0.5376 0.4757 0.6442 -0.0730 0.0598  0.0375  187 GLY   A C   
772  O  O   . GLY   A 94  ? 0.5435 0.4971 0.6667 -0.0762 0.0607  0.0326  187 GLY   A O   
773  N  N   . LEU   A 95  ? 0.5131 0.4348 0.6105 -0.0641 0.0530  0.0327  188 LEU   A N   
774  C  CA  . LEU   A 95  ? 0.4849 0.4046 0.5893 -0.0577 0.0463  0.0221  188 LEU   A CA  
775  C  C   . LEU   A 95  ? 0.4572 0.3821 0.5535 -0.0459 0.0462  0.0152  188 LEU   A C   
776  O  O   . LEU   A 95  ? 0.4447 0.3804 0.5502 -0.0416 0.0443  0.0081  188 LEU   A O   
777  C  CB  . LEU   A 95  ? 0.4865 0.3838 0.5889 -0.0579 0.0387  0.0220  188 LEU   A CB  
778  C  CG  . LEU   A 95  ? 0.4961 0.3837 0.6085 -0.0689 0.0375  0.0278  188 LEU   A CG  
779  C  CD1 . LEU   A 95  ? 0.5079 0.3725 0.6172 -0.0666 0.0305  0.0266  188 LEU   A CD1 
780  C  CD2 . LEU   A 95  ? 0.4997 0.4004 0.6310 -0.0757 0.0368  0.0227  188 LEU   A CD2 
781  N  N   . ALA   A 96  ? 0.4432 0.3607 0.5240 -0.0413 0.0476  0.0172  189 ALA   A N   
782  C  CA  . ALA   A 96  ? 0.4291 0.3462 0.5023 -0.0308 0.0464  0.0105  189 ALA   A CA  
783  C  C   . ALA   A 96  ? 0.4225 0.3589 0.4986 -0.0274 0.0531  0.0062  189 ALA   A C   
784  O  O   . ALA   A 96  ? 0.4206 0.3683 0.4943 -0.0322 0.0600  0.0099  189 ALA   A O   
785  C  CB  . ALA   A 96  ? 0.4399 0.3422 0.4973 -0.0283 0.0447  0.0133  189 ALA   A CB  
786  N  N   . PRO   A 97  ? 0.4114 0.3531 0.4931 -0.0187 0.0512  -0.0016 190 PRO   A N   
787  C  CA  . PRO   A 97  ? 0.4095 0.3675 0.4942 -0.0131 0.0571  -0.0077 190 PRO   A CA  
788  C  C   . PRO   A 97  ? 0.4154 0.3680 0.4835 -0.0115 0.0605  -0.0081 190 PRO   A C   
789  O  O   . PRO   A 97  ? 0.4096 0.3446 0.4665 -0.0102 0.0558  -0.0065 190 PRO   A O   
790  C  CB  . PRO   A 97  ? 0.3984 0.3552 0.4913 -0.0030 0.0517  -0.0146 190 PRO   A CB  
791  C  CG  . PRO   A 97  ? 0.3950 0.3428 0.4919 -0.0058 0.0441  -0.0113 190 PRO   A CG  
792  C  CD  . PRO   A 97  ? 0.3967 0.3296 0.4823 -0.0134 0.0434  -0.0048 190 PRO   A CD  
793  N  N   . PRO   A 98  ? 0.4254 0.3955 0.4917 -0.0115 0.0687  -0.0111 191 PRO   A N   
794  C  CA  . PRO   A 98  ? 0.4356 0.4038 0.4848 -0.0104 0.0717  -0.0126 191 PRO   A CA  
795  C  C   . PRO   A 98  ? 0.4332 0.3883 0.4772 -0.0008 0.0671  -0.0216 191 PRO   A C   
796  O  O   . PRO   A 98  ? 0.4342 0.3825 0.4636 -0.0011 0.0665  -0.0221 191 PRO   A O   
797  C  CB  . PRO   A 98  ? 0.4428 0.4373 0.4937 -0.0119 0.0821  -0.0158 191 PRO   A CB  
798  C  CG  . PRO   A 98  ? 0.4414 0.4510 0.5137 -0.0094 0.0838  -0.0203 191 PRO   A CG  
799  C  CD  . PRO   A 98  ? 0.4290 0.4242 0.5099 -0.0126 0.0755  -0.0141 191 PRO   A CD  
800  N  N   A GLN   A 99  ? 0.4269 0.3789 0.4833 0.0068  0.0633  -0.0278 192 GLN   A N   
801  N  N   B GLN   A 99  ? 0.4346 0.3865 0.4910 0.0067  0.0633  -0.0278 192 GLN   A N   
802  C  CA  A GLN   A 99  ? 0.4243 0.3628 0.4792 0.0156  0.0588  -0.0358 192 GLN   A CA  
803  C  CA  B GLN   A 99  ? 0.4345 0.3730 0.4896 0.0156  0.0588  -0.0358 192 GLN   A CA  
804  C  C   A GLN   A 99  ? 0.4190 0.3353 0.4677 0.0141  0.0508  -0.0302 192 GLN   A C   
805  C  C   B GLN   A 99  ? 0.4252 0.3415 0.4738 0.0141  0.0508  -0.0302 192 GLN   A C   
806  O  O   A GLN   A 99  ? 0.4208 0.3243 0.4650 0.0185  0.0475  -0.0349 192 GLN   A O   
807  O  O   B GLN   A 99  ? 0.4248 0.3283 0.4690 0.0185  0.0475  -0.0350 192 GLN   A O   
808  C  CB  A GLN   A 99  ? 0.4212 0.3649 0.4932 0.0247  0.0575  -0.0426 192 GLN   A CB  
809  C  CB  B GLN   A 99  ? 0.4387 0.3829 0.5113 0.0245  0.0574  -0.0421 192 GLN   A CB  
810  C  CG  A GLN   A 99  ? 0.4278 0.3954 0.5090 0.0285  0.0656  -0.0509 192 GLN   A CG  
811  C  CG  B GLN   A 99  ? 0.4548 0.4215 0.5361 0.0291  0.0653  -0.0514 192 GLN   A CG  
812  C  CD  A GLN   A 99  ? 0.4196 0.4065 0.5089 0.0210  0.0700  -0.0445 192 GLN   A CD  
813  C  CD  B GLN   A 99  ? 0.4596 0.4257 0.5567 0.0412  0.0621  -0.0598 192 GLN   A CD  
814  O  OE1 A GLN   A 99  ? 0.4083 0.3886 0.4984 0.0143  0.0658  -0.0352 192 GLN   A OE1 
815  O  OE1 B GLN   A 99  ? 0.4624 0.4191 0.5679 0.0441  0.0547  -0.0553 192 GLN   A OE1 
816  N  NE2 A GLN   A 99  ? 0.4240 0.4355 0.5199 0.0217  0.0788  -0.0501 192 GLN   A NE2 
817  N  NE2 B GLN   A 99  ? 0.4772 0.4533 0.5783 0.0487  0.0672  -0.0723 192 GLN   A NE2 
818  N  N   . HIS   A 100 ? 0.4096 0.3218 0.4589 0.0081  0.0479  -0.0213 193 HIS   A N   
819  C  CA  . HIS   A 100 ? 0.4051 0.3000 0.4511 0.0072  0.0409  -0.0168 193 HIS   A CA  
820  C  C   . HIS   A 100 ? 0.4113 0.2959 0.4434 0.0043  0.0397  -0.0148 193 HIS   A C   
821  O  O   . HIS   A 100 ? 0.4188 0.3074 0.4441 -0.0010 0.0423  -0.0102 193 HIS   A O   
822  C  CB  . HIS   A 100 ? 0.3934 0.2893 0.4455 0.0023  0.0384  -0.0107 193 HIS   A CB  
823  C  CG  . HIS   A 100 ? 0.3875 0.2895 0.4524 0.0063  0.0356  -0.0128 193 HIS   A CG  
824  N  ND1 . HIS   A 100 ? 0.3788 0.2750 0.4460 0.0059  0.0296  -0.0101 193 HIS   A ND1 
825  C  CD2 . HIS   A 100 ? 0.3859 0.3007 0.4618 0.0116  0.0375  -0.0175 193 HIS   A CD2 
826  C  CE1 . HIS   A 100 ? 0.3778 0.2830 0.4560 0.0104  0.0273  -0.0121 193 HIS   A CE1 
827  N  NE2 . HIS   A 100 ? 0.3915 0.3078 0.4763 0.0143  0.0319  -0.0165 193 HIS   A NE2 
828  N  N   . LEU   A 101 ? 0.4097 0.2818 0.4388 0.0074  0.0354  -0.0171 194 LEU   A N   
829  C  CA  . LEU   A 101 ? 0.4098 0.2732 0.4281 0.0049  0.0331  -0.0158 194 LEU   A CA  
830  C  C   . LEU   A 101 ? 0.3991 0.2578 0.4157 0.0002  0.0304  -0.0079 194 LEU   A C   
831  O  O   . LEU   A 101 ? 0.4120 0.2703 0.4207 -0.0029 0.0302  -0.0046 194 LEU   A O   
832  C  CB  . LEU   A 101 ? 0.4067 0.2585 0.4254 0.0082  0.0292  -0.0199 194 LEU   A CB  
833  C  CG  . LEU   A 101 ? 0.4063 0.2510 0.4168 0.0050  0.0261  -0.0186 194 LEU   A CG  
834  C  CD1 . LEU   A 101 ? 0.4122 0.2635 0.4131 0.0037  0.0282  -0.0224 194 LEU   A CD1 
835  C  CD2 . LEU   A 101 ? 0.4058 0.2392 0.4194 0.0064  0.0223  -0.0210 194 LEU   A CD2 
836  N  N   . ILE   A 102 ? 0.4011 0.2569 0.4247 0.0003  0.0278  -0.0056 195 ILE   A N   
837  C  CA  . ILE   A 102 ? 0.3995 0.2494 0.4227 -0.0026 0.0245  -0.0010 195 ILE   A CA  
838  C  C   . ILE   A 102 ? 0.4021 0.2569 0.4310 -0.0062 0.0257  0.0020  195 ILE   A C   
839  O  O   . ILE   A 102 ? 0.4070 0.2682 0.4439 -0.0054 0.0261  0.0002  195 ILE   A O   
840  C  CB  . ILE   A 102 ? 0.3949 0.2390 0.4203 -0.0006 0.0207  -0.0015 195 ILE   A CB  
841  C  CG1 . ILE   A 102 ? 0.4034 0.2420 0.4260 0.0019  0.0197  -0.0040 195 ILE   A CG1 
842  C  CG2 . ILE   A 102 ? 0.3872 0.2273 0.4116 -0.0029 0.0183  0.0008  195 ILE   A CG2 
843  C  CD1 . ILE   A 102 ? 0.4071 0.2405 0.4303 0.0021  0.0166  -0.0022 195 ILE   A CD1 
844  N  N   . ARG   A 103 ? 0.4059 0.2576 0.4322 -0.0101 0.0256  0.0066  196 ARG   A N   
845  C  CA  . ARG   A 103 ? 0.3930 0.2456 0.4262 -0.0149 0.0259  0.0101  196 ARG   A CA  
846  C  C   . ARG   A 103 ? 0.3919 0.2346 0.4269 -0.0153 0.0214  0.0106  196 ARG   A C   
847  O  O   . ARG   A 103 ? 0.3796 0.2168 0.4093 -0.0125 0.0191  0.0103  196 ARG   A O   
848  C  CB  . ARG   A 103 ? 0.4052 0.2613 0.4350 -0.0195 0.0296  0.0163  196 ARG   A CB  
849  C  CG  . ARG   A 103 ? 0.4051 0.2743 0.4327 -0.0190 0.0352  0.0144  196 ARG   A CG  
850  C  CD  . ARG   A 103 ? 0.4132 0.2885 0.4390 -0.0256 0.0396  0.0221  196 ARG   A CD  
851  N  NE  . ARG   A 103 ? 0.4158 0.3064 0.4373 -0.0251 0.0460  0.0198  196 ARG   A NE  
852  C  CZ  . ARG   A 103 ? 0.4307 0.3301 0.4453 -0.0300 0.0509  0.0262  196 ARG   A CZ  
853  N  NH1 . ARG   A 103 ? 0.4466 0.3387 0.4584 -0.0361 0.0494  0.0373  196 ARG   A NH1 
854  N  NH2 . ARG   A 103 ? 0.4383 0.3540 0.4491 -0.0287 0.0572  0.0216  196 ARG   A NH2 
855  N  N   . VAL   A 104 ? 0.3912 0.2326 0.4348 -0.0187 0.0202  0.0105  197 VAL   A N   
856  C  CA  . VAL   A 104 ? 0.3943 0.2254 0.4413 -0.0193 0.0163  0.0103  197 VAL   A CA  
857  C  C   . VAL   A 104 ? 0.4063 0.2318 0.4571 -0.0249 0.0170  0.0173  197 VAL   A C   
858  O  O   . VAL   A 104 ? 0.3973 0.2294 0.4529 -0.0301 0.0202  0.0198  197 VAL   A O   
859  C  CB  . VAL   A 104 ? 0.3869 0.2197 0.4407 -0.0188 0.0135  0.0029  197 VAL   A CB  
860  C  CG1 . VAL   A 104 ? 0.3981 0.2211 0.4575 -0.0195 0.0101  0.0004  197 VAL   A CG1 
861  C  CG2 . VAL   A 104 ? 0.3744 0.2122 0.4229 -0.0138 0.0126  -0.0012 197 VAL   A CG2 
862  N  N   . GLU   A 105 ? 0.4274 0.2423 0.4767 -0.0238 0.0143  0.0215  198 GLU   A N   
863  C  CA  . GLU   A 105 ? 0.4548 0.2609 0.5078 -0.0288 0.0138  0.0306  198 GLU   A CA  
864  C  C   . GLU   A 105 ? 0.4611 0.2548 0.5261 -0.0292 0.0093  0.0266  198 GLU   A C   
865  O  O   . GLU   A 105 ? 0.4448 0.2375 0.5113 -0.0238 0.0066  0.0175  198 GLU   A O   
866  C  CB  . GLU   A 105 ? 0.4791 0.2825 0.5219 -0.0266 0.0129  0.0392  198 GLU   A CB  
867  C  CG  . GLU   A 105 ? 0.4977 0.2881 0.5437 -0.0224 0.0071  0.0413  198 GLU   A CG  
868  C  CD  . GLU   A 105 ? 0.5281 0.3188 0.5638 -0.0197 0.0051  0.0499  198 GLU   A CD  
869  O  OE1 . GLU   A 105 ? 0.5563 0.3377 0.5935 -0.0210 0.0021  0.0604  198 GLU   A OE1 
870  O  OE2 . GLU   A 105 ? 0.5285 0.3287 0.5550 -0.0165 0.0059  0.0463  198 GLU   A OE2 
871  N  N   . GLY   A 106 ? 0.4783 0.2632 0.5519 -0.0357 0.0088  0.0328  199 GLY   A N   
872  C  CA  . GLY   A 106 ? 0.4958 0.2656 0.5828 -0.0366 0.0041  0.0288  199 GLY   A CA  
873  C  C   . GLY   A 106 ? 0.4966 0.2712 0.5921 -0.0378 0.0031  0.0152  199 GLY   A C   
874  O  O   . GLY   A 106 ? 0.5037 0.2678 0.6082 -0.0358 -0.0012 0.0071  199 GLY   A O   
875  N  N   . ASN   A 107 ? 0.4735 0.2641 0.5670 -0.0404 0.0065  0.0120  200 ASN   A N   
876  C  CA  . ASN   A 107 ? 0.4605 0.2584 0.5613 -0.0415 0.0045  -0.0003 200 ASN   A CA  
877  C  C   . ASN   A 107 ? 0.4592 0.2692 0.5668 -0.0494 0.0074  0.0014  200 ASN   A C   
878  O  O   . ASN   A 107 ? 0.4523 0.2772 0.5538 -0.0478 0.0110  0.0032  200 ASN   A O   
879  C  CB  . ASN   A 107 ? 0.4450 0.2522 0.5368 -0.0334 0.0037  -0.0087 200 ASN   A CB  
880  C  CG  . ASN   A 107 ? 0.4457 0.2577 0.5436 -0.0335 0.0000  -0.0216 200 ASN   A CG  
881  O  OD1 . ASN   A 107 ? 0.4352 0.2508 0.5429 -0.0399 -0.0011 -0.0248 200 ASN   A OD1 
882  N  ND2 . ASN   A 107 ? 0.4407 0.2549 0.5327 -0.0270 -0.0017 -0.0294 200 ASN   A ND2 
883  N  N   . LEU   A 108 ? 0.4662 0.2704 0.5881 -0.0576 0.0055  0.0000  201 LEU   A N   
884  C  CA  . LEU   A 108 ? 0.4659 0.2828 0.5982 -0.0668 0.0081  0.0016  201 LEU   A CA  
885  C  C   . LEU   A 108 ? 0.4499 0.2850 0.5844 -0.0645 0.0061  -0.0098 201 LEU   A C   
886  O  O   . LEU   A 108 ? 0.4449 0.2950 0.5880 -0.0704 0.0083  -0.0089 201 LEU   A O   
887  C  CB  . LEU   A 108 ? 0.4851 0.2883 0.6338 -0.0772 0.0058  0.0032  201 LEU   A CB  
888  C  CG  . LEU   A 108 ? 0.5063 0.3007 0.6562 -0.0846 0.0100  0.0200  201 LEU   A CG  
889  C  CD1 . LEU   A 108 ? 0.5115 0.2906 0.6489 -0.0771 0.0092  0.0279  201 LEU   A CD1 
890  C  CD2 . LEU   A 108 ? 0.5250 0.3063 0.6941 -0.0966 0.0075  0.0215  201 LEU   A CD2 
891  N  N   . ARG   A 109 ? 0.4466 0.2822 0.5741 -0.0566 0.0021  -0.0194 202 ARG   A N   
892  C  CA  . ARG   A 109 ? 0.4380 0.2911 0.5656 -0.0539 -0.0009 -0.0290 202 ARG   A CA  
893  C  C   . ARG   A 109 ? 0.4169 0.2805 0.5312 -0.0455 0.0016  -0.0252 202 ARG   A C   
894  O  O   . ARG   A 109 ? 0.4235 0.3000 0.5354 -0.0416 -0.0012 -0.0306 202 ARG   A O   
895  C  CB  . ARG   A 109 ? 0.4556 0.3041 0.5828 -0.0511 -0.0068 -0.0419 202 ARG   A CB  
896  C  CG  . ARG   A 109 ? 0.4803 0.3179 0.6229 -0.0592 -0.0105 -0.0488 202 ARG   A CG  
897  C  CD  . ARG   A 109 ? 0.5056 0.3367 0.6465 -0.0548 -0.0155 -0.0628 202 ARG   A CD  
898  N  NE  . ARG   A 109 ? 0.5170 0.3673 0.6530 -0.0521 -0.0193 -0.0735 202 ARG   A NE  
899  C  CZ  . ARG   A 109 ? 0.5409 0.3936 0.6705 -0.0470 -0.0227 -0.0860 202 ARG   A CZ  
900  N  NH1 . ARG   A 109 ? 0.5609 0.3980 0.6902 -0.0432 -0.0226 -0.0907 202 ARG   A NH1 
901  N  NH2 . ARG   A 109 ? 0.5438 0.4162 0.6674 -0.0453 -0.0264 -0.0937 202 ARG   A NH2 
902  N  N   . VAL   A 110 ? 0.4047 0.2629 0.5110 -0.0431 0.0064  -0.0160 203 VAL   A N   
903  C  CA  . VAL   A 110 ? 0.3850 0.2504 0.4801 -0.0358 0.0091  -0.0125 203 VAL   A CA  
904  C  C   . VAL   A 110 ? 0.3803 0.2640 0.4818 -0.0359 0.0102  -0.0132 203 VAL   A C   
905  O  O   . VAL   A 110 ? 0.3769 0.2680 0.4900 -0.0427 0.0120  -0.0120 203 VAL   A O   
906  C  CB  . VAL   A 110 ? 0.3790 0.2363 0.4659 -0.0347 0.0137  -0.0039 203 VAL   A CB  
907  C  CG1 . VAL   A 110 ? 0.3815 0.2417 0.4742 -0.0418 0.0184  0.0032  203 VAL   A CG1 
908  C  CG2 . VAL   A 110 ? 0.3683 0.2303 0.4445 -0.0274 0.0155  -0.0028 203 VAL   A CG2 
909  N  N   . GLU   A 111 ? 0.3776 0.2686 0.4730 -0.0285 0.0088  -0.0146 204 GLU   A N   
910  C  CA  . GLU   A 111 ? 0.3822 0.2905 0.4844 -0.0259 0.0086  -0.0155 204 GLU   A CA  
911  C  C   . GLU   A 111 ? 0.3701 0.2772 0.4635 -0.0181 0.0114  -0.0118 204 GLU   A C   
912  O  O   . GLU   A 111 ? 0.3635 0.2596 0.4455 -0.0142 0.0103  -0.0108 204 GLU   A O   
913  C  CB  . GLU   A 111 ? 0.3929 0.3105 0.4988 -0.0249 0.0015  -0.0218 204 GLU   A CB  
914  C  CG  . GLU   A 111 ? 0.4048 0.3379 0.5140 -0.0184 -0.0010 -0.0217 204 GLU   A CG  
915  C  CD  . GLU   A 111 ? 0.4235 0.3660 0.5322 -0.0165 -0.0090 -0.0264 204 GLU   A CD  
916  O  OE1 . GLU   A 111 ? 0.4370 0.3822 0.5507 -0.0227 -0.0125 -0.0328 204 GLU   A OE1 
917  O  OE2 . GLU   A 111 ? 0.4472 0.3941 0.5500 -0.0089 -0.0123 -0.0235 204 GLU   A OE2 
918  N  N   . TYR   A 112 ? 0.3674 0.2856 0.4671 -0.0163 0.0152  -0.0107 205 TYR   A N   
919  C  CA  . TYR   A 112 ? 0.3669 0.2838 0.4608 -0.0088 0.0179  -0.0093 205 TYR   A CA  
920  C  C   . TYR   A 112 ? 0.3723 0.3024 0.4749 -0.0019 0.0147  -0.0116 205 TYR   A C   
921  O  O   . TYR   A 112 ? 0.3856 0.3319 0.5018 -0.0040 0.0137  -0.0139 205 TYR   A O   
922  C  CB  . TYR   A 112 ? 0.3637 0.2823 0.4566 -0.0114 0.0255  -0.0072 205 TYR   A CB  
923  C  CG  . TYR   A 112 ? 0.3669 0.2713 0.4493 -0.0162 0.0274  -0.0031 205 TYR   A CG  
924  C  CD1 . TYR   A 112 ? 0.3716 0.2737 0.4579 -0.0246 0.0281  -0.0002 205 TYR   A CD1 
925  C  CD2 . TYR   A 112 ? 0.3598 0.2530 0.4297 -0.0122 0.0278  -0.0020 205 TYR   A CD2 
926  C  CE1 . TYR   A 112 ? 0.3736 0.2621 0.4516 -0.0279 0.0288  0.0045  205 TYR   A CE1 
927  C  CE2 . TYR   A 112 ? 0.3652 0.2473 0.4266 -0.0157 0.0286  0.0019  205 TYR   A CE2 
928  C  CZ  . TYR   A 112 ? 0.3731 0.2526 0.4384 -0.0230 0.0288  0.0056  205 TYR   A CZ  
929  O  OH  . TYR   A 112 ? 0.3888 0.2566 0.4468 -0.0252 0.0284  0.0104  205 TYR   A OH  
930  N  N   . LEU   A 113 ? 0.3862 0.3097 0.4828 0.0059  0.0126  -0.0106 206 LEU   A N   
931  C  CA  . LEU   A 113 ? 0.3866 0.3191 0.4912 0.0142  0.0083  -0.0111 206 LEU   A CA  
932  C  C   . LEU   A 113 ? 0.3899 0.3180 0.4947 0.0215  0.0119  -0.0119 206 LEU   A C   
933  O  O   . LEU   A 113 ? 0.3875 0.2999 0.4809 0.0219  0.0135  -0.0106 206 LEU   A O   
934  C  CB  . LEU   A 113 ? 0.3915 0.3184 0.4888 0.0166  0.0008  -0.0080 206 LEU   A CB  
935  C  CG  . LEU   A 113 ? 0.3950 0.3273 0.4979 0.0258  -0.0049 -0.0055 206 LEU   A CG  
936  C  CD1 . LEU   A 113 ? 0.3993 0.3531 0.5187 0.0275  -0.0076 -0.0086 206 LEU   A CD1 
937  C  CD2 . LEU   A 113 ? 0.4089 0.3351 0.5008 0.0271  -0.0115 -0.0001 206 LEU   A CD2 
938  N  N   . ASP   A 114 ? 0.3967 0.3395 0.5153 0.0268  0.0133  -0.0154 207 ASP   A N   
939  C  CA  . ASP   A 114 ? 0.4182 0.3585 0.5418 0.0373  0.0136  -0.0178 207 ASP   A CA  
940  C  C   . ASP   A 114 ? 0.4325 0.3755 0.5633 0.0450  0.0046  -0.0145 207 ASP   A C   
941  O  O   . ASP   A 114 ? 0.4536 0.4158 0.5979 0.0462  0.0018  -0.0158 207 ASP   A O   
942  C  CB  . ASP   A 114 ? 0.4144 0.3719 0.5503 0.0397  0.0207  -0.0246 207 ASP   A CB  
943  C  CG  . ASP   A 114 ? 0.4095 0.3669 0.5369 0.0324  0.0297  -0.0267 207 ASP   A CG  
944  O  OD1 . ASP   A 114 ? 0.4140 0.3557 0.5265 0.0270  0.0299  -0.0232 207 ASP   A OD1 
945  O  OD2 . ASP   A 114 ? 0.4263 0.4016 0.5625 0.0320  0.0365  -0.0312 207 ASP   A OD2 
946  N  N   . ASP   A 115 ? 0.4512 0.3767 0.5732 0.0488  -0.0002 -0.0092 208 ASP   A N   
947  C  CA  . ASP   A 115 ? 0.4621 0.3881 0.5871 0.0551  -0.0096 -0.0028 208 ASP   A CA  
948  C  C   . ASP   A 115 ? 0.4717 0.4079 0.6151 0.0665  -0.0118 -0.0056 208 ASP   A C   
949  O  O   . ASP   A 115 ? 0.4768 0.4048 0.6247 0.0724  -0.0077 -0.0103 208 ASP   A O   
950  C  CB  . ASP   A 115 ? 0.4728 0.3774 0.5840 0.0553  -0.0128 0.0047  208 ASP   A CB  
951  C  CG  . ASP   A 115 ? 0.4870 0.3925 0.5975 0.0599  -0.0223 0.0140  208 ASP   A CG  
952  O  OD1 . ASP   A 115 ? 0.4979 0.4059 0.6206 0.0698  -0.0271 0.0160  208 ASP   A OD1 
953  O  OD2 . ASP   A 115 ? 0.4990 0.4038 0.5967 0.0539  -0.0249 0.0191  208 ASP   A OD2 
954  N  N   . ARG   A 116 ? 0.4718 0.4264 0.6264 0.0699  -0.0182 -0.0041 209 ARG   A N   
955  C  CA  . ARG   A 116 ? 0.4857 0.4551 0.6615 0.0817  -0.0212 -0.0072 209 ARG   A CA  
956  C  C   . ARG   A 116 ? 0.5070 0.4576 0.6853 0.0936  -0.0258 -0.0029 209 ARG   A C   
957  O  O   . ARG   A 116 ? 0.5082 0.4646 0.7037 0.1040  -0.0248 -0.0090 209 ARG   A O   
958  C  CB  . ARG   A 116 ? 0.4831 0.4762 0.6694 0.0824  -0.0292 -0.0053 209 ARG   A CB  
959  C  CG  . ARG   A 116 ? 0.4891 0.4777 0.6622 0.0804  -0.0390 0.0046  209 ARG   A CG  
960  C  CD  . ARG   A 116 ? 0.4970 0.5122 0.6824 0.0826  -0.0479 0.0048  209 ARG   A CD  
961  N  NE  . ARG   A 116 ? 0.5002 0.5185 0.6705 0.0743  -0.0536 0.0087  209 ARG   A NE  
962  C  CZ  . ARG   A 116 ? 0.5066 0.5459 0.6817 0.0750  -0.0633 0.0099  209 ARG   A CZ  
963  N  NH1 . ARG   A 116 ? 0.5231 0.5828 0.7192 0.0841  -0.0692 0.0087  209 ARG   A NH1 
964  N  NH2 . ARG   A 116 ? 0.5101 0.5515 0.6695 0.0671  -0.0675 0.0114  209 ARG   A NH2 
965  N  N   . ASN   A 117 ? 0.5234 0.4529 0.6868 0.0920  -0.0305 0.0069  210 ASN   A N   
966  C  CA  . ASN   A 117 ? 0.5410 0.4510 0.7079 0.1024  -0.0368 0.0140  210 ASN   A CA  
967  C  C   . ASN   A 117 ? 0.5504 0.4338 0.7076 0.0994  -0.0314 0.0127  210 ASN   A C   
968  O  O   . ASN   A 117 ? 0.5735 0.4428 0.7411 0.1089  -0.0327 0.0108  210 ASN   A O   
969  C  CB  . ASN   A 117 ? 0.5461 0.4543 0.7056 0.1035  -0.0477 0.0288  210 ASN   A CB  
970  C  CG  . ASN   A 117 ? 0.5446 0.4808 0.7114 0.1047  -0.0539 0.0294  210 ASN   A CG  
971  O  OD1 . ASN   A 117 ? 0.5311 0.4829 0.7178 0.1147  -0.0575 0.0258  210 ASN   A OD1 
972  N  ND2 . ASN   A 117 ? 0.5405 0.4842 0.6919 0.0947  -0.0555 0.0330  210 ASN   A ND2 
973  N  N   . THR   A 118 ? 0.5471 0.4231 0.6864 0.0874  -0.0263 0.0133  211 THR   A N   
974  C  CA  . THR   A 118 ? 0.5499 0.4027 0.6799 0.0834  -0.0219 0.0120  211 THR   A CA  
975  C  C   . THR   A 118 ? 0.5243 0.3813 0.6564 0.0814  -0.0125 -0.0019 211 THR   A C   
976  O  O   . THR   A 118 ? 0.5375 0.3777 0.6662 0.0808  -0.0094 -0.0061 211 THR   A O   
977  C  CB  . THR   A 118 ? 0.5547 0.3992 0.6655 0.0721  -0.0216 0.0199  211 THR   A CB  
978  O  OG1 . THR   A 118 ? 0.5456 0.4051 0.6495 0.0637  -0.0166 0.0149  211 THR   A OG1 
979  C  CG2 . THR   A 118 ? 0.5786 0.4214 0.6840 0.0727  -0.0300 0.0342  211 THR   A CG2 
980  N  N   . PHE   A 119 ? 0.4915 0.3707 0.6279 0.0792  -0.0080 -0.0082 212 PHE   A N   
981  C  CA  . PHE   A 119 ? 0.4679 0.3558 0.6043 0.0759  0.0015  -0.0195 212 PHE   A CA  
982  C  C   . PHE   A 119 ? 0.4466 0.3238 0.5648 0.0647  0.0058  -0.0185 212 PHE   A C   
983  O  O   . PHE   A 119 ? 0.4271 0.3086 0.5416 0.0612  0.0131  -0.0261 212 PHE   A O   
984  C  CB  . PHE   A 119 ? 0.4872 0.3710 0.6349 0.0858  0.0042  -0.0298 212 PHE   A CB  
985  C  CG  . PHE   A 119 ? 0.5048 0.3969 0.6729 0.0990  -0.0008 -0.0310 212 PHE   A CG  
986  C  CD1 . PHE   A 119 ? 0.5037 0.4231 0.6854 0.1017  0.0006  -0.0346 212 PHE   A CD1 
987  C  CD2 . PHE   A 119 ? 0.5281 0.4006 0.7036 0.1087  -0.0076 -0.0281 212 PHE   A CD2 
988  C  CE1 . PHE   A 119 ? 0.5125 0.4416 0.7148 0.1148  -0.0047 -0.0358 212 PHE   A CE1 
989  C  CE2 . PHE   A 119 ? 0.5376 0.4170 0.7332 0.1222  -0.0132 -0.0287 212 PHE   A CE2 
990  C  CZ  . PHE   A 119 ? 0.5288 0.4375 0.7379 0.1258  -0.0119 -0.0329 212 PHE   A CZ  
991  N  N   . ARG   A 120 ? 0.4299 0.2957 0.5369 0.0594  0.0014  -0.0094 213 ARG   A N   
992  C  CA  . ARG   A 120 ? 0.4219 0.2787 0.5135 0.0497  0.0046  -0.0081 213 ARG   A CA  
993  C  C   . ARG   A 120 ? 0.4050 0.2766 0.4930 0.0423  0.0080  -0.0089 213 ARG   A C   
994  O  O   . ARG   A 120 ? 0.4040 0.2897 0.4988 0.0428  0.0056  -0.0075 213 ARG   A O   
995  C  CB  . ARG   A 120 ? 0.4245 0.2667 0.5075 0.0470  -0.0004 0.0013  213 ARG   A CB  
996  C  CG  . ARG   A 120 ? 0.4385 0.2627 0.5259 0.0526  -0.0035 0.0030  213 ARG   A CG  
997  C  CD  . ARG   A 120 ? 0.4422 0.2520 0.5208 0.0478  -0.0068 0.0128  213 ARG   A CD  
998  N  NE  . ARG   A 120 ? 0.4752 0.2658 0.5601 0.0522  -0.0099 0.0147  213 ARG   A NE  
999  C  CZ  . ARG   A 120 ? 0.4700 0.2467 0.5550 0.0502  -0.0074 0.0084  213 ARG   A CZ  
1000 N  NH1 . ARG   A 120 ? 0.4688 0.2501 0.5465 0.0443  -0.0019 0.0004  213 ARG   A NH1 
1001 N  NH2 . ARG   A 120 ? 0.4918 0.2494 0.5846 0.0540  -0.0112 0.0103  213 ARG   A NH2 
1002 N  N   . HIS   A 121 ? 0.4009 0.2691 0.4794 0.0356  0.0129  -0.0112 214 HIS   A N   
1003 C  CA  . HIS   A 121 ? 0.3860 0.2635 0.4606 0.0279  0.0162  -0.0112 214 HIS   A CA  
1004 C  C   . HIS   A 121 ? 0.3788 0.2489 0.4438 0.0221  0.0132  -0.0059 214 HIS   A C   
1005 O  O   . HIS   A 121 ? 0.3927 0.2501 0.4504 0.0218  0.0118  -0.0035 214 HIS   A O   
1006 C  CB  . HIS   A 121 ? 0.3886 0.2666 0.4581 0.0249  0.0227  -0.0158 214 HIS   A CB  
1007 C  CG  . HIS   A 121 ? 0.3882 0.2762 0.4660 0.0304  0.0271  -0.0228 214 HIS   A CG  
1008 N  ND1 . HIS   A 121 ? 0.3893 0.2778 0.4611 0.0298  0.0325  -0.0285 214 HIS   A ND1 
1009 C  CD2 . HIS   A 121 ? 0.3959 0.2963 0.4876 0.0368  0.0270  -0.0261 214 HIS   A CD2 
1010 C  CE1 . HIS   A 121 ? 0.3952 0.2960 0.4764 0.0356  0.0363  -0.0356 214 HIS   A CE1 
1011 N  NE2 . HIS   A 121 ? 0.3957 0.3039 0.4903 0.0402  0.0331  -0.0342 214 HIS   A NE2 
1012 N  N   . SER   A 122 ? 0.3668 0.2449 0.4326 0.0173  0.0127  -0.0050 215 SER   A N   
1013 C  CA  . SER   A 122 ? 0.3559 0.2284 0.4134 0.0122  0.0108  -0.0025 215 SER   A CA  
1014 C  C   . SER   A 122 ? 0.3499 0.2289 0.4102 0.0061  0.0124  -0.0042 215 SER   A C   
1015 O  O   . SER   A 122 ? 0.3433 0.2336 0.4130 0.0053  0.0139  -0.0061 215 SER   A O   
1016 C  CB  . SER   A 122 ? 0.3543 0.2266 0.4096 0.0144  0.0054  0.0009  215 SER   A CB  
1017 O  OG  . SER   A 122 ? 0.3592 0.2442 0.4226 0.0164  0.0019  0.0004  215 SER   A OG  
1018 N  N   . VAL   A 123 ? 0.3406 0.2126 0.3944 0.0020  0.0121  -0.0036 216 VAL   A N   
1019 C  CA  . VAL   A 123 ? 0.3449 0.2182 0.4017 -0.0039 0.0128  -0.0049 216 VAL   A CA  
1020 C  C   . VAL   A 123 ? 0.3530 0.2251 0.4074 -0.0048 0.0086  -0.0070 216 VAL   A C   
1021 O  O   . VAL   A 123 ? 0.3561 0.2228 0.4027 -0.0027 0.0076  -0.0059 216 VAL   A O   
1022 C  CB  . VAL   A 123 ? 0.3442 0.2100 0.3969 -0.0070 0.0166  -0.0028 216 VAL   A CB  
1023 C  CG1 . VAL   A 123 ? 0.3468 0.2026 0.3901 -0.0051 0.0161  -0.0015 216 VAL   A CG1 
1024 C  CG2 . VAL   A 123 ? 0.3436 0.2079 0.4011 -0.0131 0.0167  -0.0024 216 VAL   A CG2 
1025 N  N   A VAL   A 124 ? 0.3595 0.2380 0.4208 -0.0083 0.0063  -0.0106 217 VAL   A N   
1026 N  N   B VAL   A 124 ? 0.3602 0.2387 0.4215 -0.0083 0.0063  -0.0106 217 VAL   A N   
1027 C  CA  A VAL   A 124 ? 0.3614 0.2423 0.4206 -0.0089 0.0020  -0.0152 217 VAL   A CA  
1028 C  CA  B VAL   A 124 ? 0.3615 0.2425 0.4208 -0.0089 0.0019  -0.0152 217 VAL   A CA  
1029 C  C   A VAL   A 124 ? 0.3679 0.2447 0.4335 -0.0145 0.0016  -0.0199 217 VAL   A C   
1030 C  C   B VAL   A 124 ? 0.3679 0.2446 0.4334 -0.0145 0.0016  -0.0199 217 VAL   A C   
1031 O  O   A VAL   A 124 ? 0.3643 0.2424 0.4389 -0.0189 0.0031  -0.0192 217 VAL   A O   
1032 O  O   B VAL   A 124 ? 0.3629 0.2409 0.4376 -0.0189 0.0032  -0.0192 217 VAL   A O   
1033 C  CB  A VAL   A 124 ? 0.3623 0.2567 0.4237 -0.0065 -0.0026 -0.0165 217 VAL   A CB  
1034 C  CB  B VAL   A 124 ? 0.3626 0.2574 0.4247 -0.0067 -0.0025 -0.0166 217 VAL   A CB  
1035 C  CG1 A VAL   A 124 ? 0.3633 0.2684 0.4377 -0.0090 -0.0032 -0.0182 217 VAL   A CG1 
1036 C  CG1 B VAL   A 124 ? 0.3663 0.2666 0.4228 -0.0067 -0.0071 -0.0214 217 VAL   A CG1 
1037 C  CG2 A VAL   A 124 ? 0.3664 0.2659 0.4229 -0.0070 -0.0069 -0.0218 217 VAL   A CG2 
1038 C  CG2 B VAL   A 124 ? 0.3636 0.2603 0.4235 -0.0009 -0.0025 -0.0108 217 VAL   A CG2 
1039 N  N   . VAL   A 125 ? 0.3727 0.2440 0.4342 -0.0142 0.0002  -0.0244 218 VAL   A N   
1040 C  CA  . VAL   A 125 ? 0.3892 0.2541 0.4581 -0.0184 -0.0012 -0.0307 218 VAL   A CA  
1041 C  C   . VAL   A 125 ? 0.3946 0.2666 0.4609 -0.0173 -0.0053 -0.0403 218 VAL   A C   
1042 O  O   . VAL   A 125 ? 0.3994 0.2781 0.4556 -0.0131 -0.0056 -0.0399 218 VAL   A O   
1043 C  CB  . VAL   A 125 ? 0.3950 0.2453 0.4628 -0.0180 0.0010  -0.0278 218 VAL   A CB  
1044 C  CG1 . VAL   A 125 ? 0.4011 0.2462 0.4710 -0.0206 0.0045  -0.0189 218 VAL   A CG1 
1045 C  CG2 . VAL   A 125 ? 0.3927 0.2419 0.4505 -0.0126 0.0021  -0.0270 218 VAL   A CG2 
1046 N  N   . PRO   A 126 ? 0.3981 0.2693 0.4734 -0.0214 -0.0084 -0.0494 219 PRO   A N   
1047 C  CA  . PRO   A 126 ? 0.4078 0.2850 0.4800 -0.0200 -0.0119 -0.0611 219 PRO   A CA  
1048 C  C   . PRO   A 126 ? 0.4107 0.2808 0.4763 -0.0153 -0.0094 -0.0629 219 PRO   A C   
1049 O  O   . PRO   A 126 ? 0.3971 0.2537 0.4663 -0.0148 -0.0070 -0.0585 219 PRO   A O   
1050 C  CB  . PRO   A 126 ? 0.4148 0.2876 0.5008 -0.0260 -0.0155 -0.0712 219 PRO   A CB  
1051 C  CG  . PRO   A 126 ? 0.4107 0.2745 0.5077 -0.0316 -0.0133 -0.0624 219 PRO   A CG  
1052 C  CD  . PRO   A 126 ? 0.4047 0.2694 0.4937 -0.0281 -0.0086 -0.0492 219 PRO   A CD  
1053 N  N   . TYR   A 127 ? 0.4238 0.3058 0.4797 -0.0119 -0.0101 -0.0688 220 TYR   A N   
1054 C  CA  . TYR   A 127 ? 0.4325 0.3130 0.4841 -0.0076 -0.0077 -0.0743 220 TYR   A CA  
1055 C  C   . TYR   A 127 ? 0.4553 0.3278 0.5182 -0.0083 -0.0102 -0.0883 220 TYR   A C   
1056 O  O   . TYR   A 127 ? 0.4616 0.3401 0.5281 -0.0114 -0.0143 -0.0985 220 TYR   A O   
1057 C  CB  . TYR   A 127 ? 0.4305 0.3292 0.4683 -0.0050 -0.0072 -0.0764 220 TYR   A CB  
1058 C  CG  . TYR   A 127 ? 0.4346 0.3361 0.4700 -0.0011 -0.0041 -0.0842 220 TYR   A CG  
1059 C  CD1 . TYR   A 127 ? 0.4293 0.3274 0.4622 0.0014  0.0003  -0.0762 220 TYR   A CD1 
1060 C  CD2 . TYR   A 127 ? 0.4465 0.3541 0.4842 0.0001  -0.0057 -0.1009 220 TYR   A CD2 
1061 C  CE1 . TYR   A 127 ? 0.4337 0.3367 0.4669 0.0053  0.0034  -0.0835 220 TYR   A CE1 
1062 C  CE2 . TYR   A 127 ? 0.4534 0.3651 0.4908 0.0047  -0.0022 -0.1095 220 TYR   A CE2 
1063 C  CZ  . TYR   A 127 ? 0.4442 0.3542 0.4800 0.0074  0.0024  -0.1002 220 TYR   A CZ  
1064 O  OH  . TYR   A 127 ? 0.4536 0.3704 0.4913 0.0122  0.0061  -0.1085 220 TYR   A OH  
1065 N  N   . GLU   A 128 ? 0.4635 0.3223 0.5331 -0.0055 -0.0085 -0.0887 221 GLU   A N   
1066 C  CA  . GLU   A 128 ? 0.4916 0.3413 0.5725 -0.0038 -0.0107 -0.1031 221 GLU   A CA  
1067 C  C   . GLU   A 128 ? 0.4871 0.3428 0.5641 0.0034  -0.0076 -0.1088 221 GLU   A C   
1068 O  O   . GLU   A 128 ? 0.4791 0.3359 0.5509 0.0061  -0.0041 -0.0984 221 GLU   A O   
1069 C  CB  . GLU   A 128 ? 0.5092 0.3363 0.6047 -0.0065 -0.0124 -0.0979 221 GLU   A CB  
1070 C  CG  . GLU   A 128 ? 0.5210 0.3452 0.6234 -0.0149 -0.0153 -0.0961 221 GLU   A CG  
1071 C  CD  . GLU   A 128 ? 0.5501 0.3839 0.6557 -0.0179 -0.0197 -0.1125 221 GLU   A CD  
1072 O  OE1 . GLU   A 128 ? 0.5596 0.3927 0.6685 -0.0142 -0.0213 -0.1281 221 GLU   A OE1 
1073 O  OE2 . GLU   A 128 ? 0.5535 0.3972 0.6590 -0.0237 -0.0216 -0.1109 221 GLU   A OE2 
1074 N  N   . PRO   A 129 ? 0.4917 0.3532 0.5718 0.0067  -0.0087 -0.1267 222 PRO   A N   
1075 C  CA  . PRO   A 129 ? 0.4935 0.3640 0.5718 0.0140  -0.0050 -0.1340 222 PRO   A CA  
1076 C  C   . PRO   A 129 ? 0.4845 0.3369 0.5763 0.0189  -0.0049 -0.1300 222 PRO   A C   
1077 O  O   . PRO   A 129 ? 0.4777 0.3096 0.5800 0.0163  -0.0084 -0.1242 222 PRO   A O   
1078 C  CB  . PRO   A 129 ? 0.5127 0.3932 0.5928 0.0160  -0.0068 -0.1563 222 PRO   A CB  
1079 C  CG  . PRO   A 129 ? 0.5231 0.3894 0.6134 0.0102  -0.0129 -0.1616 222 PRO   A CG  
1080 C  CD  . PRO   A 129 ? 0.5071 0.3685 0.5937 0.0035  -0.0135 -0.1422 222 PRO   A CD  
1081 N  N   . PRO   A 130 ? 0.4822 0.3433 0.5740 0.0256  -0.0012 -0.1318 223 PRO   A N   
1082 C  CA  . PRO   A 130 ? 0.4857 0.3328 0.5899 0.0311  -0.0019 -0.1268 223 PRO   A CA  
1083 C  C   . PRO   A 130 ? 0.5130 0.3378 0.6353 0.0338  -0.0073 -0.1354 223 PRO   A C   
1084 O  O   . PRO   A 130 ? 0.5125 0.3384 0.6392 0.0342  -0.0090 -0.1518 223 PRO   A O   
1085 C  CB  . PRO   A 130 ? 0.4822 0.3488 0.5857 0.0383  0.0028  -0.1342 223 PRO   A CB  
1086 C  CG  . PRO   A 130 ? 0.4754 0.3651 0.5604 0.0334  0.0074  -0.1324 223 PRO   A CG  
1087 C  CD  . PRO   A 130 ? 0.4802 0.3671 0.5602 0.0279  0.0039  -0.1377 223 PRO   A CD  
1088 N  N   . GLU   A 131 ? 0.5331 0.3381 0.6651 0.0352  -0.0103 -0.1234 224 GLU   A N   
1089 C  CA  . GLU   A 131 ? 0.5636 0.3441 0.7146 0.0384  -0.0160 -0.1284 224 GLU   A CA  
1090 C  C   . GLU   A 131 ? 0.5715 0.3564 0.7347 0.0503  -0.0159 -0.1437 224 GLU   A C   
1091 O  O   . GLU   A 131 ? 0.5667 0.3727 0.7235 0.0550  -0.0112 -0.1447 224 GLU   A O   
1092 C  CB  . GLU   A 131 ? 0.5754 0.3362 0.7302 0.0359  -0.0190 -0.1079 224 GLU   A CB  
1093 C  CG  . GLU   A 131 ? 0.5743 0.3284 0.7224 0.0244  -0.0193 -0.0965 224 GLU   A CG  
1094 C  CD  . GLU   A 131 ? 0.5919 0.3405 0.7464 0.0185  -0.0217 -0.1093 224 GLU   A CD  
1095 O  OE1 . GLU   A 131 ? 0.5816 0.3426 0.7257 0.0113  -0.0198 -0.1090 224 GLU   A OE1 
1096 O  OE2 . GLU   A 131 ? 0.6282 0.3598 0.7993 0.0213  -0.0261 -0.1198 224 GLU   A OE2 
1097 N  N   . VAL   A 132 ? 0.5829 0.3481 0.7645 0.0547  -0.0210 -0.1550 225 VAL   A N   
1098 C  CA  . VAL   A 132 ? 0.5992 0.3631 0.7979 0.0678  -0.0224 -0.1702 225 VAL   A CA  
1099 C  C   . VAL   A 132 ? 0.5875 0.3542 0.7888 0.0747  -0.0222 -0.1556 225 VAL   A C   
1100 O  O   . VAL   A 132 ? 0.5851 0.3325 0.7892 0.0723  -0.0266 -0.1367 225 VAL   A O   
1101 C  CB  . VAL   A 132 ? 0.6226 0.3564 0.8431 0.0705  -0.0296 -0.1797 225 VAL   A CB  
1102 C  CG1 . VAL   A 132 ? 0.6400 0.3707 0.8805 0.0858  -0.0317 -0.1945 225 VAL   A CG1 
1103 C  CG2 . VAL   A 132 ? 0.6310 0.3632 0.8504 0.0630  -0.0306 -0.1961 225 VAL   A CG2 
1104 N  N   . GLY   A 133 ? 0.5788 0.3707 0.7790 0.0823  -0.0172 -0.1641 226 GLY   A N   
1105 C  CA  . GLY   A 133 ? 0.5702 0.3716 0.7732 0.0885  -0.0167 -0.1528 226 GLY   A CA  
1106 C  C   . GLY   A 133 ? 0.5521 0.3810 0.7357 0.0823  -0.0094 -0.1454 226 GLY   A C   
1107 O  O   . GLY   A 133 ? 0.5657 0.4165 0.7526 0.0884  -0.0056 -0.1491 226 GLY   A O   
1108 N  N   . SER   A 134 ? 0.5396 0.3678 0.7053 0.0706  -0.0077 -0.1354 227 SER   A N   
1109 C  CA  . SER   A 134 ? 0.5127 0.3603 0.6603 0.0636  -0.0022 -0.1241 227 SER   A CA  
1110 C  C   . SER   A 134 ? 0.5126 0.3847 0.6487 0.0611  0.0043  -0.1364 227 SER   A C   
1111 O  O   . SER   A 134 ? 0.5276 0.3983 0.6649 0.0614  0.0037  -0.1510 227 SER   A O   
1112 C  CB  . SER   A 134 ? 0.5060 0.3396 0.6423 0.0539  -0.0043 -0.1067 227 SER   A CB  
1113 O  OG  . SER   A 134 ? 0.4841 0.3332 0.6057 0.0485  0.0000  -0.0962 227 SER   A OG  
1114 N  N   . ASP   A 135 ? 0.4947 0.3882 0.6201 0.0580  0.0099  -0.1298 228 ASP   A N   
1115 C  CA  . ASP   A 135 ? 0.5020 0.4200 0.6125 0.0535  0.0165  -0.1352 228 ASP   A CA  
1116 C  C   . ASP   A 135 ? 0.4900 0.4066 0.5828 0.0432  0.0172  -0.1190 228 ASP   A C   
1117 O  O   . ASP   A 135 ? 0.4883 0.4241 0.5678 0.0387  0.0221  -0.1181 228 ASP   A O   
1118 C  CB  . ASP   A 135 ? 0.5052 0.4493 0.6194 0.0578  0.0227  -0.1397 228 ASP   A CB  
1119 C  CG  . ASP   A 135 ? 0.5200 0.4707 0.6513 0.0691  0.0232  -0.1597 228 ASP   A CG  
1120 O  OD1 . ASP   A 135 ? 0.5389 0.4845 0.6715 0.0714  0.0216  -0.1747 228 ASP   A OD1 
1121 O  OD2 . ASP   A 135 ? 0.5172 0.4780 0.6618 0.0758  0.0245  -0.1610 228 ASP   A OD2 
1122 N  N   . CYS   A 136 ? 0.4835 0.3789 0.5765 0.0397  0.0125  -0.1064 229 CYS   A N   
1123 C  CA  . CYS   A 136 ? 0.4852 0.3769 0.5645 0.0313  0.0126  -0.0915 229 CYS   A CA  
1124 C  C   . CYS   A 136 ? 0.4845 0.3541 0.5661 0.0283  0.0074  -0.0867 229 CYS   A C   
1125 O  O   . CYS   A 136 ? 0.5228 0.3772 0.6171 0.0323  0.0034  -0.0907 229 CYS   A O   
1126 C  CB  . CYS   A 136 ? 0.4684 0.3628 0.5464 0.0299  0.0139  -0.0785 229 CYS   A CB  
1127 S  SG  . CYS   A 136 ? 0.4757 0.3522 0.5672 0.0347  0.0085  -0.0721 229 CYS   A SG  
1128 N  N   . THR   A 137 ? 0.4679 0.3361 0.5387 0.0216  0.0074  -0.0778 230 THR   A N   
1129 C  CA  . THR   A 137 ? 0.4601 0.3111 0.5325 0.0174  0.0037  -0.0713 230 THR   A CA  
1130 C  C   . THR   A 137 ? 0.4477 0.2923 0.5165 0.0152  0.0039  -0.0562 230 THR   A C   
1131 O  O   . THR   A 137 ? 0.4487 0.3033 0.5085 0.0133  0.0068  -0.0503 230 THR   A O   
1132 C  CB  . THR   A 137 ? 0.4547 0.3114 0.5198 0.0125  0.0033  -0.0741 230 THR   A CB  
1133 O  OG1 . THR   A 137 ? 0.4640 0.3261 0.5333 0.0151  0.0024  -0.0902 230 THR   A OG1 
1134 C  CG2 . THR   A 137 ? 0.4478 0.2912 0.5157 0.0074  0.0004  -0.0675 230 THR   A CG2 
1135 N  N   . THR   A 138 ? 0.4452 0.2740 0.5208 0.0152  0.0009  -0.0503 231 THR   A N   
1136 C  CA  . THR   A 138 ? 0.4384 0.2618 0.5098 0.0132  0.0007  -0.0370 231 THR   A CA  
1137 C  C   . THR   A 138 ? 0.4351 0.2524 0.5025 0.0070  0.0007  -0.0307 231 THR   A C   
1138 O  O   . THR   A 138 ? 0.4422 0.2505 0.5165 0.0049  -0.0012 -0.0333 231 THR   A O   
1139 C  CB  . THR   A 138 ? 0.4430 0.2565 0.5227 0.0175  -0.0025 -0.0330 231 THR   A CB  
1140 O  OG1 . THR   A 138 ? 0.4437 0.2666 0.5290 0.0239  -0.0022 -0.0400 231 THR   A OG1 
1141 C  CG2 . THR   A 138 ? 0.4359 0.2467 0.5092 0.0154  -0.0030 -0.0204 231 THR   A CG2 
1142 N  N   . ILE   A 139 ? 0.4171 0.2398 0.4752 0.0042  0.0030  -0.0237 232 ILE   A N   
1143 C  CA  . ILE   A 139 ? 0.4150 0.2342 0.4698 -0.0004 0.0037  -0.0165 232 ILE   A CA  
1144 C  C   . ILE   A 139 ? 0.4116 0.2267 0.4627 -0.0004 0.0038  -0.0074 232 ILE   A C   
1145 O  O   . ILE   A 139 ? 0.4058 0.2256 0.4531 0.0019  0.0041  -0.0065 232 ILE   A O   
1146 C  CB  . ILE   A 139 ? 0.4082 0.2371 0.4564 -0.0023 0.0057  -0.0171 232 ILE   A CB  
1147 C  CG1 . ILE   A 139 ? 0.4146 0.2495 0.4650 -0.0027 0.0047  -0.0256 232 ILE   A CG1 
1148 C  CG2 . ILE   A 139 ? 0.4069 0.2345 0.4531 -0.0058 0.0071  -0.0106 232 ILE   A CG2 
1149 C  CD1 . ILE   A 139 ? 0.4114 0.2572 0.4545 -0.0030 0.0056  -0.0251 232 ILE   A CD1 
1150 N  N   . HIS   A 140 ? 0.4224 0.2305 0.4745 -0.0037 0.0036  -0.0010 233 HIS   A N   
1151 C  CA  . HIS   A 140 ? 0.4183 0.2244 0.4647 -0.0045 0.0038  0.0081  233 HIS   A CA  
1152 C  C   . HIS   A 140 ? 0.4065 0.2196 0.4457 -0.0077 0.0075  0.0104  233 HIS   A C   
1153 O  O   . HIS   A 140 ? 0.4260 0.2392 0.4673 -0.0118 0.0094  0.0125  233 HIS   A O   
1154 C  CB  . HIS   A 140 ? 0.4324 0.2273 0.4842 -0.0062 0.0014  0.0148  233 HIS   A CB  
1155 C  CG  . HIS   A 140 ? 0.4403 0.2276 0.4999 -0.0010 -0.0029 0.0131  233 HIS   A CG  
1156 N  ND1 . HIS   A 140 ? 0.4586 0.2322 0.5270 -0.0014 -0.0063 0.0176  233 HIS   A ND1 
1157 C  CD2 . HIS   A 140 ? 0.4425 0.2342 0.5040 0.0049  -0.0046 0.0074  233 HIS   A CD2 
1158 C  CE1 . HIS   A 140 ? 0.4662 0.2355 0.5421 0.0052  -0.0102 0.0139  233 HIS   A CE1 
1159 N  NE2 . HIS   A 140 ? 0.4565 0.2384 0.5285 0.0092  -0.0089 0.0073  233 HIS   A NE2 
1160 N  N   . TYR   A 141 ? 0.3947 0.2139 0.4272 -0.0059 0.0086  0.0090  234 TYR   A N   
1161 C  CA  . TYR   A 141 ? 0.3749 0.1997 0.4013 -0.0073 0.0117  0.0100  234 TYR   A CA  
1162 C  C   . TYR   A 141 ? 0.3850 0.2102 0.4045 -0.0085 0.0122  0.0157  234 TYR   A C   
1163 O  O   . TYR   A 141 ? 0.3828 0.2053 0.4003 -0.0070 0.0091  0.0187  234 TYR   A O   
1164 C  CB  . TYR   A 141 ? 0.3606 0.1891 0.3845 -0.0052 0.0119  0.0056  234 TYR   A CB  
1165 C  CG  . TYR   A 141 ? 0.3535 0.1844 0.3814 -0.0046 0.0118  0.0017  234 TYR   A CG  
1166 C  CD1 . TYR   A 141 ? 0.3481 0.1824 0.3784 -0.0057 0.0130  0.0009  234 TYR   A CD1 
1167 C  CD2 . TYR   A 141 ? 0.3477 0.1799 0.3772 -0.0031 0.0105  -0.0013 234 TYR   A CD2 
1168 C  CE1 . TYR   A 141 ? 0.3468 0.1850 0.3796 -0.0051 0.0119  -0.0023 234 TYR   A CE1 
1169 C  CE2 . TYR   A 141 ? 0.3488 0.1855 0.3797 -0.0028 0.0103  -0.0048 234 TYR   A CE2 
1170 C  CZ  . TYR   A 141 ? 0.3462 0.1856 0.3781 -0.0038 0.0105  -0.0050 234 TYR   A CZ  
1171 O  OH  . TYR   A 141 ? 0.3504 0.1960 0.3826 -0.0035 0.0094  -0.0082 234 TYR   A OH  
1172 N  N   . ASN   A 142 ? 0.3842 0.2146 0.4001 -0.0106 0.0159  0.0168  235 ASN   A N   
1173 C  CA  . ASN   A 142 ? 0.3902 0.2254 0.3966 -0.0115 0.0175  0.0200  235 ASN   A CA  
1174 C  C   . ASN   A 142 ? 0.3929 0.2343 0.3962 -0.0098 0.0203  0.0133  235 ASN   A C   
1175 O  O   . ASN   A 142 ? 0.3924 0.2365 0.4012 -0.0095 0.0228  0.0102  235 ASN   A O   
1176 C  CB  . ASN   A 142 ? 0.3956 0.2342 0.4006 -0.0160 0.0208  0.0269  235 ASN   A CB  
1177 C  CG  . ASN   A 142 ? 0.4053 0.2350 0.4152 -0.0184 0.0179  0.0348  235 ASN   A CG  
1178 O  OD1 . ASN   A 142 ? 0.4189 0.2492 0.4313 -0.0234 0.0205  0.0409  235 ASN   A OD1 
1179 N  ND2 . ASN   A 142 ? 0.3963 0.2180 0.4090 -0.0151 0.0128  0.0345  235 ASN   A ND2 
1180 N  N   . TYR   A 143 ? 0.3963 0.2393 0.3922 -0.0084 0.0190  0.0106  236 TYR   A N   
1181 C  CA  . TYR   A 143 ? 0.4137 0.2608 0.4068 -0.0066 0.0213  0.0032  236 TYR   A CA  
1182 C  C   . TYR   A 143 ? 0.4248 0.2813 0.4088 -0.0079 0.0248  0.0035  236 TYR   A C   
1183 O  O   . TYR   A 143 ? 0.4482 0.3072 0.4234 -0.0095 0.0229  0.0079  236 TYR   A O   
1184 C  CB  . TYR   A 143 ? 0.4126 0.2551 0.4052 -0.0052 0.0175  -0.0012 236 TYR   A CB  
1185 C  CG  . TYR   A 143 ? 0.4135 0.2500 0.4143 -0.0044 0.0157  -0.0013 236 TYR   A CG  
1186 C  CD1 . TYR   A 143 ? 0.4144 0.2487 0.4184 -0.0048 0.0131  0.0025  236 TYR   A CD1 
1187 C  CD2 . TYR   A 143 ? 0.4135 0.2471 0.4187 -0.0028 0.0165  -0.0051 236 TYR   A CD2 
1188 C  CE1 . TYR   A 143 ? 0.4170 0.2488 0.4269 -0.0043 0.0122  0.0016  236 TYR   A CE1 
1189 C  CE2 . TYR   A 143 ? 0.4175 0.2474 0.4280 -0.0027 0.0150  -0.0037 236 TYR   A CE2 
1190 C  CZ  . TYR   A 143 ? 0.4132 0.2434 0.4253 -0.0037 0.0133  -0.0007 236 TYR   A CZ  
1191 O  OH  . TYR   A 143 ? 0.4143 0.2440 0.4301 -0.0037 0.0126  -0.0001 236 TYR   A OH  
1192 N  N   . MET   A 144 ? 0.4280 0.2915 0.4142 -0.0070 0.0299  -0.0007 237 MET   A N   
1193 C  CA  . MET   A 144 ? 0.4500 0.3265 0.4294 -0.0090 0.0354  0.0003  237 MET   A CA  
1194 C  C   . MET   A 144 ? 0.4591 0.3430 0.4311 -0.0061 0.0376  -0.0101 237 MET   A C   
1195 O  O   . MET   A 144 ? 0.4708 0.3686 0.4372 -0.0070 0.0433  -0.0117 237 MET   A O   
1196 C  CB  . MET   A 144 ? 0.4406 0.3234 0.4298 -0.0102 0.0404  0.0018  237 MET   A CB  
1197 C  CG  . MET   A 144 ? 0.4364 0.3119 0.4334 -0.0138 0.0380  0.0103  237 MET   A CG  
1198 S  SD  . MET   A 144 ? 0.4491 0.3201 0.4378 -0.0190 0.0355  0.0229  237 MET   A SD  
1199 C  CE  . MET   A 144 ? 0.4555 0.3439 0.4338 -0.0230 0.0429  0.0266  237 MET   A CE  
1200 N  N   A CYS   A 145 ? 0.4674 0.3430 0.4398 -0.0033 0.0332  -0.0174 238 CYS   A N   
1201 N  N   B CYS   A 145 ? 0.4677 0.3434 0.4400 -0.0033 0.0332  -0.0174 238 CYS   A N   
1202 C  CA  A CYS   A 145 ? 0.4824 0.3619 0.4490 -0.0008 0.0336  -0.0294 238 CYS   A CA  
1203 C  CA  B CYS   A 145 ? 0.4826 0.3622 0.4494 -0.0006 0.0337  -0.0297 238 CYS   A CA  
1204 C  C   A CYS   A 145 ? 0.4793 0.3504 0.4429 -0.0017 0.0267  -0.0316 238 CYS   A C   
1205 C  C   B CYS   A 145 ? 0.4795 0.3506 0.4431 -0.0016 0.0268  -0.0317 238 CYS   A C   
1206 O  O   A CYS   A 145 ? 0.4692 0.3298 0.4403 -0.0023 0.0228  -0.0267 238 CYS   A O   
1207 O  O   B CYS   A 145 ? 0.4694 0.3300 0.4404 -0.0023 0.0228  -0.0267 238 CYS   A O   
1208 C  CB  A CYS   A 145 ? 0.4908 0.3680 0.4681 0.0043  0.0362  -0.0391 238 CYS   A CB  
1209 C  CB  B CYS   A 145 ? 0.4906 0.3673 0.4689 0.0044  0.0362  -0.0388 238 CYS   A CB  
1210 S  SG  A CYS   A 145 ? 0.5163 0.4123 0.4906 0.0066  0.0446  -0.0465 238 CYS   A SG  
1211 S  SG  B CYS   A 145 ? 0.5203 0.4067 0.4959 0.0092  0.0407  -0.0552 238 CYS   A SG  
1212 N  N   . ASN   A 146 ? 0.4858 0.3636 0.4388 -0.0021 0.0254  -0.0391 239 ASN   A N   
1213 C  CA  . ASN   A 146 ? 0.4818 0.3543 0.4332 -0.0036 0.0185  -0.0432 239 ASN   A CA  
1214 C  C   . ASN   A 146 ? 0.4821 0.3429 0.4442 -0.0015 0.0174  -0.0542 239 ASN   A C   
1215 O  O   . ASN   A 146 ? 0.4901 0.3515 0.4556 0.0021  0.0217  -0.0626 239 ASN   A O   
1216 C  CB  . ASN   A 146 ? 0.4933 0.3789 0.4289 -0.0053 0.0164  -0.0472 239 ASN   A CB  
1217 C  CG  . ASN   A 146 ? 0.5018 0.3948 0.4281 -0.0078 0.0145  -0.0330 239 ASN   A CG  
1218 O  OD1 . ASN   A 146 ? 0.4802 0.3658 0.4128 -0.0087 0.0103  -0.0235 239 ASN   A OD1 
1219 N  ND2 . ASN   A 146 ? 0.5127 0.4206 0.4242 -0.0088 0.0175  -0.0311 239 ASN   A ND2 
1220 N  N   . SER   A 147 ? 0.4724 0.3236 0.4411 -0.0039 0.0119  -0.0537 240 SER   A N   
1221 C  CA  . SER   A 147 ? 0.4745 0.3126 0.4537 -0.0037 0.0097  -0.0622 240 SER   A CA  
1222 C  C   . SER   A 147 ? 0.5030 0.3436 0.4781 -0.0023 0.0098  -0.0782 240 SER   A C   
1223 O  O   . SER   A 147 ? 0.5071 0.3364 0.4919 0.0003  0.0103  -0.0866 240 SER   A O   
1224 C  CB  . SER   A 147 ? 0.4594 0.2916 0.4442 -0.0085 0.0041  -0.0585 240 SER   A CB  
1225 O  OG  . SER   A 147 ? 0.4276 0.2579 0.4170 -0.0089 0.0047  -0.0461 240 SER   A OG  
1226 N  N   . SER   A 148 ? 0.5351 0.3902 0.4962 -0.0036 0.0091  -0.0823 241 SER   A N   
1227 C  CA  . SER   A 148 ? 0.5646 0.4265 0.5184 -0.0028 0.0086  -0.0994 241 SER   A CA  
1228 C  C   . SER   A 148 ? 0.5816 0.4514 0.5322 0.0028  0.0163  -0.1071 241 SER   A C   
1229 O  O   . SER   A 148 ? 0.6020 0.4748 0.5502 0.0051  0.0168  -0.1242 241 SER   A O   
1230 C  CB  . SER   A 148 ? 0.5751 0.4526 0.5133 -0.0065 0.0044  -0.0992 241 SER   A CB  
1231 O  OG  . SER   A 148 ? 0.5737 0.4645 0.5003 -0.0060 0.0081  -0.0865 241 SER   A OG  
1232 N  N   . CYS   A 149 ? 0.5786 0.4532 0.5302 0.0050  0.0221  -0.0962 242 CYS   A N   
1233 C  CA  . CYS   A 149 ? 0.5979 0.4861 0.5461 0.0096  0.0304  -0.1016 242 CYS   A CA  
1234 C  C   . CYS   A 149 ? 0.6191 0.5003 0.5785 0.0160  0.0321  -0.1191 242 CYS   A C   
1235 O  O   . CYS   A 149 ? 0.6027 0.4671 0.5784 0.0189  0.0306  -0.1172 242 CYS   A O   
1236 C  CB  . CYS   A 149 ? 0.5862 0.4764 0.5403 0.0101  0.0350  -0.0871 242 CYS   A CB  
1237 S  SG  . CYS   A 149 ? 0.6038 0.5084 0.5434 0.0043  0.0367  -0.0701 242 CYS   A SG  
1238 N  N   . MET   A 150 ? 0.6609 0.5549 0.6117 0.0184  0.0348  -0.1356 243 MET   A N   
1239 C  CA  . MET   A 150 ? 0.6967 0.5877 0.6580 0.0262  0.0380  -0.1547 243 MET   A CA  
1240 C  C   . MET   A 150 ? 0.6819 0.5784 0.6543 0.0322  0.0452  -0.1495 243 MET   A C   
1241 O  O   . MET   A 150 ? 0.7106 0.6253 0.6746 0.0299  0.0509  -0.1389 243 MET   A O   
1242 C  CB  . MET   A 150 ? 0.7346 0.6446 0.6814 0.0275  0.0409  -0.1735 243 MET   A CB  
1243 C  CG  . MET   A 150 ? 0.7630 0.6640 0.7057 0.0240  0.0326  -0.1868 243 MET   A CG  
1244 S  SD  . MET   A 150 ? 0.7854 0.6888 0.7136 0.0133  0.0242  -0.1715 243 MET   A SD  
1245 C  CE  . MET   A 150 ? 0.8017 0.7021 0.7265 0.0108  0.0163  -0.1952 243 MET   A CE  
1246 N  N   . GLY   A 151 ? 0.6668 0.5477 0.6585 0.0392  0.0441  -0.1555 244 GLY   A N   
1247 C  CA  . GLY   A 151 ? 0.6585 0.5450 0.6637 0.0461  0.0496  -0.1521 244 GLY   A CA  
1248 C  C   . GLY   A 151 ? 0.6309 0.5129 0.6401 0.0420  0.0481  -0.1305 244 GLY   A C   
1249 O  O   . GLY   A 151 ? 0.6294 0.5228 0.6462 0.0452  0.0530  -0.1253 244 GLY   A O   
1250 N  N   . GLY   A 152 ? 0.6066 0.4744 0.6114 0.0351  0.0415  -0.1193 245 GLY   A N   
1251 C  CA  . GLY   A 152 ? 0.5828 0.4421 0.5925 0.0316  0.0386  -0.1012 245 GLY   A CA  
1252 C  C   . GLY   A 152 ? 0.5656 0.4015 0.5819 0.0297  0.0309  -0.0986 245 GLY   A C   
1253 O  O   . GLY   A 152 ? 0.5740 0.3962 0.6018 0.0348  0.0285  -0.1076 245 GLY   A O   
1254 N  N   . MET   A 153 ? 0.5450 0.3768 0.5551 0.0224  0.0272  -0.0871 246 MET   A N   
1255 C  CA  . MET   A 153 ? 0.5406 0.3537 0.5562 0.0187  0.0207  -0.0834 246 MET   A CA  
1256 C  C   . MET   A 153 ? 0.5579 0.3638 0.5728 0.0174  0.0174  -0.0976 246 MET   A C   
1257 O  O   . MET   A 153 ? 0.5573 0.3449 0.5831 0.0170  0.0132  -0.0994 246 MET   A O   
1258 C  CB  . MET   A 153 ? 0.5202 0.3356 0.5293 0.0118  0.0185  -0.0701 246 MET   A CB  
1259 C  CG  . MET   A 153 ? 0.5013 0.3204 0.5133 0.0126  0.0205  -0.0575 246 MET   A CG  
1260 S  SD  . MET   A 153 ? 0.4697 0.2896 0.4765 0.0059  0.0176  -0.0446 246 MET   A SD  
1261 C  CE  . MET   A 153 ? 0.4784 0.3148 0.4717 0.0039  0.0203  -0.0440 246 MET   A CE  
1262 N  N   . ASN   A 154 ? 0.5735 0.3937 0.5762 0.0165  0.0192  -0.1073 247 ASN   A N   
1263 C  CA  . ASN   A 154 ? 0.5888 0.4067 0.5892 0.0159  0.0165  -0.1249 247 ASN   A CA  
1264 C  C   . ASN   A 154 ? 0.5902 0.3915 0.5969 0.0092  0.0092  -0.1231 247 ASN   A C   
1265 O  O   . ASN   A 154 ? 0.5820 0.3663 0.6004 0.0102  0.0061  -0.1330 247 ASN   A O   
1266 C  CB  . ASN   A 154 ? 0.6113 0.4250 0.6210 0.0245  0.0194  -0.1408 247 ASN   A CB  
1267 C  CG  . ASN   A 154 ? 0.6365 0.4486 0.6437 0.0244  0.0169  -0.1618 247 ASN   A CG  
1268 O  OD1 . ASN   A 154 ? 0.6412 0.4668 0.6335 0.0194  0.0156  -0.1667 247 ASN   A OD1 
1269 N  ND2 . ASN   A 154 ? 0.6524 0.4474 0.6747 0.0299  0.0152  -0.1745 247 ASN   A ND2 
1270 N  N   . ARG   A 155 ? 0.5677 0.3740 0.5686 0.0027  0.0067  -0.1104 248 ARG   A N   
1271 C  CA  . ARG   A 155 ? 0.5764 0.3751 0.5813 -0.0050 0.0004  -0.1080 248 ARG   A CA  
1272 C  C   . ARG   A 155 ? 0.5585 0.3386 0.5784 -0.0067 -0.0010 -0.0984 248 ARG   A C   
1273 O  O   . ARG   A 155 ? 0.5515 0.3267 0.5762 -0.0140 -0.0051 -0.0944 248 ARG   A O   
1274 C  CB  . ARG   A 155 ? 0.6049 0.4025 0.6089 -0.0079 -0.0039 -0.1260 248 ARG   A CB  
1275 C  CG  . ARG   A 155 ? 0.6199 0.4386 0.6064 -0.0065 -0.0027 -0.1354 248 ARG   A CG  
1276 C  CD  . ARG   A 155 ? 0.6488 0.4715 0.6314 -0.0116 -0.0090 -0.1506 248 ARG   A CD  
1277 N  NE  . ARG   A 155 ? 0.6708 0.5167 0.6337 -0.0103 -0.0080 -0.1568 248 ARG   A NE  
1278 C  CZ  . ARG   A 155 ? 0.6706 0.5334 0.6204 -0.0133 -0.0101 -0.1459 248 ARG   A CZ  
1279 N  NH1 . ARG   A 155 ? 0.6609 0.5204 0.6164 -0.0170 -0.0131 -0.1300 248 ARG   A NH1 
1280 N  NH2 . ARG   A 155 ? 0.6828 0.5662 0.6137 -0.0120 -0.0091 -0.1510 248 ARG   A NH2 
1281 N  N   . ARG   A 156 ? 0.5413 0.3138 0.5679 -0.0006 0.0022  -0.0936 249 ARG   A N   
1282 C  CA  . ARG   A 156 ? 0.5381 0.2946 0.5768 -0.0017 0.0007  -0.0822 249 ARG   A CA  
1283 C  C   . ARG   A 156 ? 0.5187 0.2839 0.5530 -0.0051 0.0017  -0.0662 249 ARG   A C   
1284 O  O   . ARG   A 156 ? 0.5060 0.2841 0.5326 -0.0020 0.0050  -0.0618 249 ARG   A O   
1285 C  CB  . ARG   A 156 ? 0.5422 0.2898 0.5893 0.0070  0.0027  -0.0830 249 ARG   A CB  
1286 C  CG  . ARG   A 156 ? 0.5624 0.2996 0.6166 0.0118  0.0016  -0.1003 249 ARG   A CG  
1287 C  CD  . ARG   A 156 ? 0.5679 0.2999 0.6316 0.0224  0.0037  -0.1012 249 ARG   A CD  
1288 N  NE  . ARG   A 156 ? 0.5615 0.3147 0.6173 0.0280  0.0095  -0.1023 249 ARG   A NE  
1289 C  CZ  . ARG   A 156 ? 0.5652 0.3218 0.6285 0.0373  0.0123  -0.1032 249 ARG   A CZ  
1290 N  NH1 . ARG   A 156 ? 0.5703 0.3092 0.6490 0.0436  0.0090  -0.1030 249 ARG   A NH1 
1291 N  NH2 . ARG   A 156 ? 0.5576 0.3357 0.6139 0.0403  0.0181  -0.1038 249 ARG   A NH2 
1292 N  N   . PRO   A 157 ? 0.5155 0.2743 0.5553 -0.0119 -0.0008 -0.0577 250 PRO   A N   
1293 C  CA  . PRO   A 157 ? 0.4977 0.2659 0.5341 -0.0147 0.0003  -0.0448 250 PRO   A CA  
1294 C  C   . PRO   A 157 ? 0.4838 0.2505 0.5213 -0.0096 0.0029  -0.0350 250 PRO   A C   
1295 O  O   . PRO   A 157 ? 0.4844 0.2388 0.5291 -0.0063 0.0022  -0.0341 250 PRO   A O   
1296 C  CB  . PRO   A 157 ? 0.5021 0.2645 0.5460 -0.0234 -0.0025 -0.0405 250 PRO   A CB  
1297 C  CG  . PRO   A 157 ? 0.5204 0.2636 0.5743 -0.0243 -0.0048 -0.0460 250 PRO   A CG  
1298 C  CD  . PRO   A 157 ? 0.5290 0.2719 0.5794 -0.0177 -0.0046 -0.0605 250 PRO   A CD  
1299 N  N   . ILE   A 158 ? 0.4543 0.2334 0.4857 -0.0089 0.0050  -0.0283 251 ILE   A N   
1300 C  CA  . ILE   A 158 ? 0.4564 0.2371 0.4883 -0.0049 0.0068  -0.0199 251 ILE   A CA  
1301 C  C   . ILE   A 158 ? 0.4416 0.2280 0.4724 -0.0090 0.0069  -0.0105 251 ILE   A C   
1302 O  O   . ILE   A 158 ? 0.4451 0.2379 0.4741 -0.0135 0.0064  -0.0111 251 ILE   A O   
1303 C  CB  . ILE   A 158 ? 0.4478 0.2385 0.4750 0.0003  0.0097  -0.0228 251 ILE   A CB  
1304 C  CG1 . ILE   A 158 ? 0.4409 0.2431 0.4601 -0.0021 0.0106  -0.0230 251 ILE   A CG1 
1305 C  CG2 . ILE   A 158 ? 0.4523 0.2397 0.4818 0.0052  0.0106  -0.0327 251 ILE   A CG2 
1306 C  CD1 . ILE   A 158 ? 0.4384 0.2498 0.4545 0.0006  0.0135  -0.0201 251 ILE   A CD1 
1307 N  N   . LEU   A 159 ? 0.4482 0.2336 0.4805 -0.0072 0.0073  -0.0028 252 LEU   A N   
1308 C  CA  . LEU   A 159 ? 0.4446 0.2389 0.4740 -0.0094 0.0082  0.0045  252 LEU   A CA  
1309 C  C   . LEU   A 159 ? 0.4244 0.2269 0.4506 -0.0046 0.0095  0.0042  252 LEU   A C   
1310 O  O   . LEU   A 159 ? 0.4361 0.2363 0.4644 0.0000  0.0095  0.0024  252 LEU   A O   
1311 C  CB  . LEU   A 159 ? 0.4672 0.2563 0.4992 -0.0113 0.0073  0.0136  252 LEU   A CB  
1312 C  CG  . LEU   A 159 ? 0.4834 0.2702 0.5182 -0.0190 0.0072  0.0178  252 LEU   A CG  
1313 C  CD1 . LEU   A 159 ? 0.5089 0.2786 0.5504 -0.0206 0.0048  0.0202  252 LEU   A CD1 
1314 C  CD2 . LEU   A 159 ? 0.4852 0.2823 0.5165 -0.0219 0.0090  0.0265  252 LEU   A CD2 
1315 N  N   . THR   A 160 ? 0.4172 0.2292 0.4404 -0.0060 0.0105  0.0053  253 THR   A N   
1316 C  CA  . THR   A 160 ? 0.3937 0.2128 0.4154 -0.0033 0.0111  0.0064  253 THR   A CA  
1317 C  C   . THR   A 160 ? 0.3848 0.2080 0.4054 -0.0045 0.0107  0.0120  253 THR   A C   
1318 O  O   . THR   A 160 ? 0.3936 0.2200 0.4133 -0.0081 0.0114  0.0138  253 THR   A O   
1319 C  CB  . THR   A 160 ? 0.3845 0.2098 0.4044 -0.0039 0.0120  0.0036  253 THR   A CB  
1320 O  OG1 . THR   A 160 ? 0.3875 0.2107 0.4062 -0.0033 0.0124  0.0000  253 THR   A OG1 
1321 C  CG2 . THR   A 160 ? 0.3748 0.2056 0.3951 -0.0022 0.0122  0.0036  253 THR   A CG2 
1322 N  N   . ILE   A 161 ? 0.3775 0.2028 0.3981 -0.0014 0.0094  0.0144  254 ILE   A N   
1323 C  CA  . ILE   A 161 ? 0.3820 0.2140 0.3992 -0.0021 0.0084  0.0198  254 ILE   A CA  
1324 C  C   . ILE   A 161 ? 0.3788 0.2209 0.3948 -0.0009 0.0083  0.0155  254 ILE   A C   
1325 O  O   . ILE   A 161 ? 0.3767 0.2192 0.3961 0.0017  0.0075  0.0126  254 ILE   A O   
1326 C  CB  . ILE   A 161 ? 0.3920 0.2192 0.4105 0.0007  0.0054  0.0264  254 ILE   A CB  
1327 C  CG1 . ILE   A 161 ? 0.4046 0.2181 0.4268 -0.0004 0.0051  0.0293  254 ILE   A CG1 
1328 C  CG2 . ILE   A 161 ? 0.3976 0.2339 0.4102 -0.0001 0.0038  0.0332  254 ILE   A CG2 
1329 C  CD1 . ILE   A 161 ? 0.4120 0.2170 0.4390 0.0043  0.0016  0.0341  254 ILE   A CD1 
1330 N  N   . ILE   A 162 ? 0.3843 0.2342 0.3970 -0.0031 0.0096  0.0138  255 ILE   A N   
1331 C  CA  . ILE   A 162 ? 0.3863 0.2449 0.3986 -0.0023 0.0092  0.0079  255 ILE   A CA  
1332 C  C   . ILE   A 162 ? 0.3921 0.2609 0.3985 -0.0023 0.0075  0.0106  255 ILE   A C   
1333 O  O   . ILE   A 162 ? 0.4244 0.2986 0.4257 -0.0046 0.0093  0.0142  255 ILE   A O   
1334 C  CB  . ILE   A 162 ? 0.3831 0.2439 0.3969 -0.0034 0.0112  0.0023  255 ILE   A CB  
1335 C  CG1 . ILE   A 162 ? 0.3795 0.2316 0.3971 -0.0036 0.0120  0.0017  255 ILE   A CG1 
1336 C  CG2 . ILE   A 162 ? 0.3844 0.2506 0.3999 -0.0023 0.0102  -0.0048 255 ILE   A CG2 
1337 C  CD1 . ILE   A 162 ? 0.3761 0.2224 0.3965 -0.0024 0.0113  0.0007  255 ILE   A CD1 
1338 N  N   . THR   A 163 ? 0.3904 0.2637 0.3975 -0.0002 0.0043  0.0095  256 THR   A N   
1339 C  CA  A THR   A 163 ? 0.4011 0.2865 0.4015 0.0001  0.0014  0.0117  256 THR   A CA  
1340 C  CA  B THR   A 163 ? 0.4056 0.2910 0.4061 0.0001  0.0014  0.0117  256 THR   A CA  
1341 C  C   . THR   A 163 ? 0.4040 0.2991 0.4050 -0.0001 0.0003  0.0013  256 THR   A C   
1342 O  O   . THR   A 163 ? 0.3918 0.2824 0.4008 0.0000  -0.0001 -0.0045 256 THR   A O   
1343 C  CB  A THR   A 163 ? 0.4026 0.2871 0.4043 0.0032  -0.0028 0.0190  256 THR   A CB  
1344 C  CB  B THR   A 163 ? 0.4130 0.2975 0.4147 0.0032  -0.0029 0.0190  256 THR   A CB  
1345 O  OG1 A THR   A 163 ? 0.3991 0.2826 0.4098 0.0052  -0.0043 0.0134  256 THR   A OG1 
1346 O  OG1 B THR   A 163 ? 0.4323 0.3305 0.4266 0.0037  -0.0067 0.0214  256 THR   A OG1 
1347 C  CG2 A THR   A 163 ? 0.4076 0.2797 0.4104 0.0037  -0.0022 0.0282  256 THR   A CG2 
1348 C  CG2 B THR   A 163 ? 0.4098 0.2918 0.4214 0.0057  -0.0045 0.0144  256 THR   A CG2 
1349 N  N   . LEU   A 164 ? 0.4187 0.3266 0.4114 -0.0011 0.0002  -0.0009 257 LEU   A N   
1350 C  CA  . LEU   A 164 ? 0.4336 0.3525 0.4256 -0.0012 -0.0018 -0.0123 257 LEU   A CA  
1351 C  C   . LEU   A 164 ? 0.4501 0.3808 0.4369 -0.0002 -0.0075 -0.0092 257 LEU   A C   
1352 O  O   . LEU   A 164 ? 0.4699 0.4068 0.4470 0.0000  -0.0084 0.0006  257 LEU   A O   
1353 C  CB  . LEU   A 164 ? 0.4414 0.3694 0.4271 -0.0022 0.0021  -0.0180 257 LEU   A CB  
1354 C  CG  . LEU   A 164 ? 0.4470 0.3831 0.4346 -0.0018 0.0011  -0.0335 257 LEU   A CG  
1355 C  CD1 . LEU   A 164 ? 0.4415 0.3631 0.4424 -0.0013 0.0019  -0.0408 257 LEU   A CD1 
1356 C  CD2 . LEU   A 164 ? 0.4591 0.4102 0.4382 -0.0018 0.0050  -0.0390 257 LEU   A CD2 
1357 N  N   . GLU   A 165 ? 0.4674 0.4008 0.4614 0.0000  -0.0118 -0.0159 258 GLU   A N   
1358 C  CA  . GLU   A 165 ? 0.4788 0.4260 0.4697 0.0013  -0.0187 -0.0140 258 GLU   A CA  
1359 C  C   . GLU   A 165 ? 0.4959 0.4549 0.4885 -0.0006 -0.0222 -0.0286 258 GLU   A C   
1360 O  O   . GLU   A 165 ? 0.5053 0.4565 0.5068 -0.0027 -0.0198 -0.0389 258 GLU   A O   
1361 C  CB  . GLU   A 165 ? 0.4706 0.4127 0.4719 0.0039  -0.0218 -0.0073 258 GLU   A CB  
1362 C  CG  . GLU   A 165 ? 0.4621 0.3868 0.4733 0.0039  -0.0168 -0.0056 258 GLU   A CG  
1363 C  CD  . GLU   A 165 ? 0.4599 0.3824 0.4813 0.0071  -0.0190 -0.0006 258 GLU   A CD  
1364 O  OE1 . GLU   A 165 ? 0.4658 0.3968 0.4963 0.0066  -0.0222 -0.0061 258 GLU   A OE1 
1365 O  OE2 . GLU   A 165 ? 0.4626 0.3758 0.4840 0.0101  -0.0176 0.0079  258 GLU   A OE2 
1366 N  N   . ASP   A 166 ? 0.5123 0.4893 0.4970 0.0000  -0.0283 -0.0295 259 ASP   A N   
1367 C  CA  . ASP   A 166 ? 0.5252 0.5150 0.5124 -0.0024 -0.0331 -0.0450 259 ASP   A CA  
1368 C  C   . ASP   A 166 ? 0.5356 0.5239 0.5391 -0.0032 -0.0377 -0.0464 259 ASP   A C   
1369 O  O   . ASP   A 166 ? 0.5435 0.5224 0.5541 -0.0010 -0.0364 -0.0354 259 ASP   A O   
1370 C  CB  . ASP   A 166 ? 0.5413 0.5539 0.5119 -0.0018 -0.0379 -0.0467 259 ASP   A CB  
1371 C  CG  . ASP   A 166 ? 0.5495 0.5736 0.5149 0.0010  -0.0452 -0.0335 259 ASP   A CG  
1372 O  OD1 . ASP   A 166 ? 0.5382 0.5551 0.5165 0.0030  -0.0478 -0.0268 259 ASP   A OD1 
1373 O  OD2 . ASP   A 166 ? 0.5704 0.6117 0.5186 0.0017  -0.0482 -0.0297 259 ASP   A OD2 
1374 N  N   . SER   A 167 ? 0.5307 0.5293 0.5405 -0.0065 -0.0429 -0.0600 260 SER   A N   
1375 C  CA  . SER   A 167 ? 0.5219 0.5214 0.5499 -0.0092 -0.0467 -0.0634 260 SER   A CA  
1376 C  C   . SER   A 167 ? 0.5240 0.5353 0.5533 -0.0051 -0.0523 -0.0519 260 SER   A C   
1377 O  O   . SER   A 167 ? 0.5285 0.5379 0.5740 -0.0056 -0.0526 -0.0497 260 SER   A O   
1378 C  CB  . SER   A 167 ? 0.5190 0.5279 0.5533 -0.0145 -0.0517 -0.0810 260 SER   A CB  
1379 O  OG  . SER   A 167 ? 0.5193 0.5504 0.5408 -0.0133 -0.0589 -0.0857 260 SER   A OG  
1380 N  N   . SER   A 168 ? 0.5339 0.5573 0.5475 -0.0008 -0.0563 -0.0440 261 SER   A N   
1381 C  CA  . SER   A 168 ? 0.5391 0.5742 0.5532 0.0046  -0.0634 -0.0319 261 SER   A CA  
1382 C  C   . SER   A 168 ? 0.5381 0.5569 0.5523 0.0098  -0.0587 -0.0157 261 SER   A C   
1383 O  O   . SER   A 168 ? 0.5499 0.5742 0.5676 0.0156  -0.0642 -0.0052 261 SER   A O   
1384 C  CB  . SER   A 168 ? 0.5549 0.6110 0.5516 0.0063  -0.0711 -0.0300 261 SER   A CB  
1385 O  OG  . SER   A 168 ? 0.5511 0.6243 0.5491 0.0018  -0.0769 -0.0467 261 SER   A OG  
1386 N  N   . GLY   A 169 ? 0.5323 0.5320 0.5436 0.0082  -0.0497 -0.0144 262 GLY   A N   
1387 C  CA  . GLY   A 169 ? 0.5254 0.5080 0.5374 0.0119  -0.0449 -0.0016 262 GLY   A CA  
1388 C  C   . GLY   A 169 ? 0.5291 0.5105 0.5240 0.0137  -0.0445 0.0101  262 GLY   A C   
1389 O  O   . GLY   A 169 ? 0.5307 0.4986 0.5267 0.0169  -0.0424 0.0218  262 GLY   A O   
1390 N  N   . ASN   A 170 ? 0.5326 0.5280 0.5123 0.0113  -0.0463 0.0072  263 ASN   A N   
1391 C  CA  . ASN   A 170 ? 0.5414 0.5384 0.5034 0.0112  -0.0446 0.0190  263 ASN   A CA  
1392 C  C   . ASN   A 170 ? 0.5270 0.5080 0.4883 0.0081  -0.0346 0.0181  263 ASN   A C   
1393 O  O   . ASN   A 170 ? 0.5199 0.4985 0.4859 0.0051  -0.0303 0.0043  263 ASN   A O   
1394 C  CB  . ASN   A 170 ? 0.5544 0.5749 0.4993 0.0094  -0.0486 0.0152  263 ASN   A CB  
1395 C  CG  . ASN   A 170 ? 0.5712 0.6096 0.5158 0.0128  -0.0599 0.0174  263 ASN   A CG  
1396 O  OD1 . ASN   A 170 ? 0.5863 0.6230 0.5315 0.0176  -0.0651 0.0330  263 ASN   A OD1 
1397 N  ND2 . ASN   A 170 ? 0.5643 0.6200 0.5088 0.0106  -0.0644 0.0017  263 ASN   A ND2 
1398 N  N   . LEU   A 171 ? 0.5367 0.5063 0.4943 0.0087  -0.0318 0.0326  264 LEU   A N   
1399 C  CA  . LEU   A 171 ? 0.5451 0.5013 0.5023 0.0053  -0.0231 0.0334  264 LEU   A CA  
1400 C  C   . LEU   A 171 ? 0.5346 0.5053 0.4791 0.0012  -0.0188 0.0267  264 LEU   A C   
1401 O  O   . LEU   A 171 ? 0.5567 0.5433 0.4866 0.0004  -0.0211 0.0332  264 LEU   A O   
1402 C  CB  . LEU   A 171 ? 0.5757 0.5195 0.5314 0.0060  -0.0228 0.0510  264 LEU   A CB  
1403 C  CG  . LEU   A 171 ? 0.5816 0.5053 0.5523 0.0095  -0.0231 0.0540  264 LEU   A CG  
1404 C  CD1 . LEU   A 171 ? 0.5793 0.4899 0.5568 0.0064  -0.0157 0.0465  264 LEU   A CD1 
1405 C  CD2 . LEU   A 171 ? 0.5846 0.5120 0.5663 0.0145  -0.0287 0.0480  264 LEU   A CD2 
1406 N  N   . LEU   A 172 ? 0.5116 0.4782 0.4616 -0.0006 -0.0129 0.0141  265 LEU   A N   
1407 C  CA  . LEU   A 172 ? 0.4980 0.4775 0.4392 -0.0034 -0.0075 0.0057  265 LEU   A CA  
1408 C  C   . LEU   A 172 ? 0.4786 0.4495 0.4212 -0.0060 0.0000  0.0119  265 LEU   A C   
1409 O  O   . LEU   A 172 ? 0.4819 0.4664 0.4144 -0.0087 0.0043  0.0136  265 LEU   A O   
1410 C  CB  . LEU   A 172 ? 0.4879 0.4687 0.4371 -0.0028 -0.0073 -0.0137 265 LEU   A CB  
1411 C  CG  . LEU   A 172 ? 0.4892 0.4767 0.4416 -0.0016 -0.0147 -0.0221 265 LEU   A CG  
1412 C  CD1 . LEU   A 172 ? 0.4843 0.4711 0.4453 -0.0022 -0.0140 -0.0413 265 LEU   A CD1 
1413 C  CD2 . LEU   A 172 ? 0.5035 0.5128 0.4403 -0.0014 -0.0199 -0.0187 265 LEU   A CD2 
1414 N  N   . GLY   A 173 ? 0.4625 0.4136 0.4172 -0.0055 0.0013  0.0146  266 GLY   A N   
1415 C  CA  . GLY   A 173 ? 0.4568 0.3997 0.4155 -0.0081 0.0075  0.0175  266 GLY   A CA  
1416 C  C   . GLY   A 173 ? 0.4478 0.3697 0.4176 -0.0073 0.0068  0.0224  266 GLY   A C   
1417 O  O   . GLY   A 173 ? 0.4509 0.3652 0.4277 -0.0042 0.0033  0.0184  266 GLY   A O   
1418 N  N   . ARG   A 174 ? 0.4485 0.3628 0.4201 -0.0104 0.0102  0.0303  267 ARG   A N   
1419 C  CA  . ARG   A 174 ? 0.4346 0.3298 0.4160 -0.0100 0.0098  0.0333  267 ARG   A CA  
1420 C  C   . ARG   A 174 ? 0.4240 0.3165 0.4093 -0.0141 0.0147  0.0332  267 ARG   A C   
1421 O  O   . ARG   A 174 ? 0.4151 0.3174 0.3954 -0.0186 0.0182  0.0388  267 ARG   A O   
1422 C  CB  . ARG   A 174 ? 0.4512 0.3366 0.4320 -0.0091 0.0059  0.0457  267 ARG   A CB  
1423 C  CG  . ARG   A 174 ? 0.4476 0.3143 0.4388 -0.0074 0.0050  0.0457  267 ARG   A CG  
1424 C  CD  . ARG   A 174 ? 0.4688 0.3238 0.4613 -0.0068 0.0018  0.0580  267 ARG   A CD  
1425 N  NE  . ARG   A 174 ? 0.4804 0.3398 0.4706 -0.0018 -0.0037 0.0626  267 ARG   A NE  
1426 C  CZ  . ARG   A 174 ? 0.4886 0.3536 0.4709 -0.0022 -0.0068 0.0747  267 ARG   A CZ  
1427 N  NH1 . ARG   A 174 ? 0.4931 0.3602 0.4684 -0.0083 -0.0041 0.0846  267 ARG   A NH1 
1428 N  NH2 . ARG   A 174 ? 0.4959 0.3657 0.4776 0.0034  -0.0130 0.0778  267 ARG   A NH2 
1429 N  N   . ASN   A 175 ? 0.4078 0.2896 0.4019 -0.0129 0.0150  0.0272  268 ASN   A N   
1430 C  CA  . ASN   A 175 ? 0.4122 0.2897 0.4121 -0.0163 0.0179  0.0270  268 ASN   A CA  
1431 C  C   . ASN   A 175 ? 0.4066 0.2675 0.4129 -0.0148 0.0156  0.0262  268 ASN   A C   
1432 O  O   . ASN   A 175 ? 0.4243 0.2792 0.4309 -0.0108 0.0127  0.0253  268 ASN   A O   
1433 C  CB  . ASN   A 175 ? 0.4164 0.3045 0.4194 -0.0157 0.0208  0.0173  268 ASN   A CB  
1434 C  CG  . ASN   A 175 ? 0.4342 0.3409 0.4321 -0.0180 0.0247  0.0171  268 ASN   A CG  
1435 O  OD1 . ASN   A 175 ? 0.4364 0.3496 0.4351 -0.0230 0.0283  0.0221  268 ASN   A OD1 
1436 N  ND2 . ASN   A 175 ? 0.4339 0.3507 0.4269 -0.0148 0.0244  0.0105  268 ASN   A ND2 
1437 N  N   . SER   A 176 ? 0.4128 0.2687 0.4243 -0.0179 0.0168  0.0258  269 SER   A N   
1438 C  CA  . SER   A 176 ? 0.4090 0.2508 0.4254 -0.0172 0.0147  0.0241  269 SER   A CA  
1439 C  C   . SER   A 176 ? 0.4082 0.2516 0.4296 -0.0201 0.0157  0.0197  269 SER   A C   
1440 O  O   . SER   A 176 ? 0.4018 0.2558 0.4248 -0.0237 0.0182  0.0203  269 SER   A O   
1441 C  CB  . SER   A 176 ? 0.4217 0.2519 0.4390 -0.0186 0.0130  0.0315  269 SER   A CB  
1442 O  OG  . SER   A 176 ? 0.4296 0.2622 0.4476 -0.0253 0.0147  0.0385  269 SER   A OG  
1443 N  N   . PHE   A 177 ? 0.4134 0.2486 0.4371 -0.0184 0.0139  0.0150  270 PHE   A N   
1444 C  CA  . PHE   A 177 ? 0.4138 0.2502 0.4418 -0.0208 0.0132  0.0107  270 PHE   A CA  
1445 C  C   . PHE   A 177 ? 0.4249 0.2499 0.4530 -0.0197 0.0109  0.0073  270 PHE   A C   
1446 O  O   . PHE   A 177 ? 0.4366 0.2567 0.4617 -0.0152 0.0106  0.0062  270 PHE   A O   
1447 C  CB  . PHE   A 177 ? 0.4084 0.2544 0.4371 -0.0178 0.0133  0.0062  270 PHE   A CB  
1448 C  CG  . PHE   A 177 ? 0.4125 0.2555 0.4378 -0.0126 0.0126  0.0039  270 PHE   A CG  
1449 C  CD1 . PHE   A 177 ? 0.4105 0.2566 0.4336 -0.0103 0.0136  0.0043  270 PHE   A CD1 
1450 C  CD2 . PHE   A 177 ? 0.4138 0.2525 0.4380 -0.0108 0.0107  0.0012  270 PHE   A CD2 
1451 C  CE1 . PHE   A 177 ? 0.4178 0.2615 0.4399 -0.0070 0.0128  0.0021  270 PHE   A CE1 
1452 C  CE2 . PHE   A 177 ? 0.4094 0.2461 0.4313 -0.0075 0.0107  0.0005  270 PHE   A CE2 
1453 C  CZ  . PHE   A 177 ? 0.4148 0.2535 0.4368 -0.0059 0.0117  0.0009  270 PHE   A CZ  
1454 N  N   . GLU   A 178 ? 0.4183 0.2408 0.4504 -0.0239 0.0095  0.0048  271 GLU   A N   
1455 C  CA  A GLU   A 178 ? 0.4231 0.2375 0.4547 -0.0231 0.0071  -0.0013 271 GLU   A CA  
1456 C  CA  B GLU   A 178 ? 0.4272 0.2415 0.4588 -0.0231 0.0071  -0.0013 271 GLU   A CA  
1457 C  C   . GLU   A 178 ? 0.4186 0.2397 0.4454 -0.0192 0.0064  -0.0055 271 GLU   A C   
1458 O  O   . GLU   A 178 ? 0.4153 0.2458 0.4428 -0.0188 0.0064  -0.0042 271 GLU   A O   
1459 C  CB  A GLU   A 178 ? 0.4252 0.2366 0.4630 -0.0296 0.0051  -0.0039 271 GLU   A CB  
1460 C  CB  B GLU   A 178 ? 0.4340 0.2454 0.4717 -0.0296 0.0051  -0.0039 271 GLU   A CB  
1461 C  CG  A GLU   A 178 ? 0.4319 0.2334 0.4693 -0.0288 0.0027  -0.0118 271 GLU   A CG  
1462 C  CG  B GLU   A 178 ? 0.4456 0.2480 0.4888 -0.0345 0.0057  0.0021  271 GLU   A CG  
1463 C  CD  A GLU   A 178 ? 0.4396 0.2341 0.4847 -0.0359 0.0000  -0.0156 271 GLU   A CD  
1464 C  CD  B GLU   A 178 ? 0.4555 0.2574 0.5072 -0.0432 0.0041  0.0005  271 GLU   A CD  
1465 O  OE1 A GLU   A 178 ? 0.4391 0.2307 0.4833 -0.0356 -0.0026 -0.0253 271 GLU   A OE1 
1466 O  OE1 B GLU   A 178 ? 0.4588 0.2696 0.5119 -0.0447 0.0020  -0.0060 271 GLU   A OE1 
1467 O  OE2 A GLU   A 178 ? 0.4446 0.2375 0.4966 -0.0422 0.0006  -0.0094 271 GLU   A OE2 
1468 O  OE2 B GLU   A 178 ? 0.4620 0.2555 0.5193 -0.0488 0.0045  0.0067  271 GLU   A OE2 
1469 N  N   A VAL   A 179 ? 0.4261 0.2429 0.4488 -0.0162 0.0060  -0.0099 272 VAL   A N   
1470 N  N   B VAL   A 179 ? 0.4294 0.2462 0.4521 -0.0162 0.0060  -0.0099 272 VAL   A N   
1471 C  CA  A VAL   A 179 ? 0.4251 0.2479 0.4416 -0.0134 0.0055  -0.0122 272 VAL   A CA  
1472 C  CA  B VAL   A 179 ? 0.4300 0.2529 0.4465 -0.0134 0.0055  -0.0121 272 VAL   A CA  
1473 C  C   A VAL   A 179 ? 0.4321 0.2539 0.4450 -0.0141 0.0036  -0.0195 272 VAL   A C   
1474 C  C   B VAL   A 179 ? 0.4349 0.2566 0.4477 -0.0140 0.0036  -0.0194 272 VAL   A C   
1475 O  O   A VAL   A 179 ? 0.4340 0.2478 0.4482 -0.0135 0.0043  -0.0240 272 VAL   A O   
1476 O  O   B VAL   A 179 ? 0.4364 0.2503 0.4506 -0.0135 0.0043  -0.0239 272 VAL   A O   
1477 C  CB  A VAL   A 179 ? 0.4239 0.2467 0.4373 -0.0092 0.0081  -0.0098 272 VAL   A CB  
1478 C  CB  B VAL   A 179 ? 0.4323 0.2553 0.4457 -0.0092 0.0081  -0.0094 272 VAL   A CB  
1479 C  CG1 A VAL   A 179 ? 0.4212 0.2494 0.4282 -0.0077 0.0081  -0.0102 272 VAL   A CG1 
1480 C  CG1 B VAL   A 179 ? 0.4268 0.2518 0.4435 -0.0088 0.0092  -0.0044 272 VAL   A CG1 
1481 C  CG2 A VAL   A 179 ? 0.4174 0.2421 0.4336 -0.0086 0.0093  -0.0046 272 VAL   A CG2 
1482 C  CG2 B VAL   A 179 ? 0.4372 0.2545 0.4506 -0.0069 0.0098  -0.0123 272 VAL   A CG2 
1483 N  N   . ARG   A 180 ? 0.4286 0.2584 0.4374 -0.0148 0.0008  -0.0210 273 ARG   A N   
1484 C  CA  . ARG   A 180 ? 0.4321 0.2651 0.4336 -0.0148 -0.0009 -0.0281 273 ARG   A CA  
1485 C  C   . ARG   A 180 ? 0.4267 0.2675 0.4192 -0.0119 -0.0004 -0.0238 273 ARG   A C   
1486 O  O   . ARG   A 180 ? 0.4131 0.2587 0.4067 -0.0116 -0.0027 -0.0178 273 ARG   A O   
1487 C  CB  . ARG   A 180 ? 0.4384 0.2758 0.4427 -0.0191 -0.0060 -0.0329 273 ARG   A CB  
1488 C  CG  . ARG   A 180 ? 0.4505 0.2947 0.4453 -0.0192 -0.0089 -0.0406 273 ARG   A CG  
1489 C  CD  . ARG   A 180 ? 0.4661 0.3145 0.4659 -0.0243 -0.0146 -0.0469 273 ARG   A CD  
1490 N  NE  . ARG   A 180 ? 0.4894 0.3456 0.4789 -0.0244 -0.0180 -0.0557 273 ARG   A NE  
1491 C  CZ  . ARG   A 180 ? 0.5153 0.3778 0.5061 -0.0288 -0.0240 -0.0641 273 ARG   A CZ  
1492 N  NH1 . ARG   A 180 ? 0.5144 0.3766 0.5186 -0.0341 -0.0271 -0.0642 273 ARG   A NH1 
1493 N  NH2 . ARG   A 180 ? 0.5347 0.4061 0.5132 -0.0282 -0.0268 -0.0725 273 ARG   A NH2 
1494 N  N   . VAL   A 181 ? 0.4272 0.2691 0.4124 -0.0098 0.0027  -0.0264 274 VAL   A N   
1495 C  CA  . VAL   A 181 ? 0.4321 0.2823 0.4075 -0.0085 0.0037  -0.0214 274 VAL   A CA  
1496 C  C   . VAL   A 181 ? 0.4464 0.3055 0.4113 -0.0097 0.0006  -0.0275 274 VAL   A C   
1497 O  O   . VAL   A 181 ? 0.4527 0.3117 0.4153 -0.0095 0.0021  -0.0378 274 VAL   A O   
1498 C  CB  . VAL   A 181 ? 0.4259 0.2759 0.4002 -0.0065 0.0097  -0.0198 274 VAL   A CB  
1499 C  CG1 . VAL   A 181 ? 0.4316 0.2886 0.3984 -0.0070 0.0110  -0.0111 274 VAL   A CG1 
1500 C  CG2 . VAL   A 181 ? 0.4175 0.2592 0.4025 -0.0054 0.0117  -0.0171 274 VAL   A CG2 
1501 N  N   . CYS   A 182 ? 0.4592 0.3258 0.4188 -0.0103 -0.0042 -0.0222 275 CYS   A N   
1502 C  CA  . CYS   A 182 ? 0.4896 0.3669 0.4393 -0.0118 -0.0093 -0.0278 275 CYS   A CA  
1503 C  C   . CYS   A 182 ? 0.4947 0.3813 0.4348 -0.0108 -0.0129 -0.0169 275 CYS   A C   
1504 O  O   . CYS   A 182 ? 0.4922 0.3740 0.4372 -0.0093 -0.0124 -0.0058 275 CYS   A O   
1505 C  CB  . CYS   A 182 ? 0.5009 0.3774 0.4595 -0.0144 -0.0149 -0.0349 275 CYS   A CB  
1506 S  SG  . CYS   A 182 ? 0.5133 0.3871 0.4869 -0.0144 -0.0180 -0.0262 275 CYS   A SG  
1507 N  N   . ALA   A 183 ? 0.5214 0.4206 0.4481 -0.0117 -0.0169 -0.0202 276 ALA   A N   
1508 C  CA  . ALA   A 183 ? 0.5361 0.4459 0.4506 -0.0109 -0.0213 -0.0089 276 ALA   A CA  
1509 C  C   . ALA   A 183 ? 0.5296 0.4388 0.4542 -0.0092 -0.0294 -0.0015 276 ALA   A C   
1510 O  O   . ALA   A 183 ? 0.5364 0.4449 0.4595 -0.0068 -0.0316 0.0124  276 ALA   A O   
1511 C  CB  . ALA   A 183 ? 0.5531 0.4785 0.4503 -0.0124 -0.0242 -0.0164 276 ALA   A CB  
1512 N  N   . CYS   A 184 ? 0.5212 0.4307 0.4570 -0.0104 -0.0335 -0.0104 277 CYS   A N   
1513 C  CA  . CYS   A 184 ? 0.5204 0.4353 0.4666 -0.0087 -0.0418 -0.0064 277 CYS   A CA  
1514 C  C   . CYS   A 184 ? 0.4899 0.3967 0.4555 -0.0096 -0.0396 -0.0104 277 CYS   A C   
1515 O  O   . CYS   A 184 ? 0.4953 0.4058 0.4685 -0.0131 -0.0421 -0.0198 277 CYS   A O   
1516 C  CB  . CYS   A 184 ? 0.5486 0.4795 0.4880 -0.0107 -0.0504 -0.0135 277 CYS   A CB  
1517 S  SG  . CYS   A 184 ? 0.5742 0.5179 0.5187 -0.0062 -0.0623 -0.0029 277 CYS   A SG  
1518 N  N   . PRO   A 185 ? 0.4639 0.3600 0.4377 -0.0070 -0.0347 -0.0035 278 PRO   A N   
1519 C  CA  . PRO   A 185 ? 0.4449 0.3352 0.4346 -0.0080 -0.0316 -0.0068 278 PRO   A CA  
1520 C  C   . PRO   A 185 ? 0.4347 0.3353 0.4378 -0.0080 -0.0375 -0.0086 278 PRO   A C   
1521 O  O   . PRO   A 185 ? 0.4163 0.3177 0.4291 -0.0124 -0.0360 -0.0154 278 PRO   A O   
1522 C  CB  . PRO   A 185 ? 0.4441 0.3249 0.4376 -0.0042 -0.0273 0.0015  278 PRO   A CB  
1523 C  CG  . PRO   A 185 ? 0.4555 0.3336 0.4350 -0.0033 -0.0256 0.0077  278 PRO   A CG  
1524 C  CD  . PRO   A 185 ? 0.4690 0.3590 0.4371 -0.0038 -0.0321 0.0077  278 PRO   A CD  
1525 N  N   . GLY   A 186 ? 0.4332 0.3422 0.4377 -0.0033 -0.0442 -0.0020 279 GLY   A N   
1526 C  CA  . GLY   A 186 ? 0.4338 0.3569 0.4520 -0.0020 -0.0510 -0.0037 279 GLY   A CA  
1527 C  C   . GLY   A 186 ? 0.4435 0.3772 0.4628 -0.0086 -0.0548 -0.0139 279 GLY   A C   
1528 O  O   . GLY   A 186 ? 0.4305 0.3691 0.4649 -0.0126 -0.0538 -0.0195 279 GLY   A O   
1529 N  N   . ARG   A 187 ? 0.4620 0.3993 0.4658 -0.0106 -0.0585 -0.0169 280 ARG   A N   
1530 C  CA  . ARG   A 187 ? 0.4817 0.4291 0.4851 -0.0171 -0.0634 -0.0286 280 ARG   A CA  
1531 C  C   . ARG   A 187 ? 0.4744 0.4101 0.4843 -0.0239 -0.0563 -0.0376 280 ARG   A C   
1532 O  O   . ARG   A 187 ? 0.4720 0.4135 0.4942 -0.0300 -0.0588 -0.0453 280 ARG   A O   
1533 C  CB  . ARG   A 187 ? 0.5088 0.4625 0.4914 -0.0170 -0.0678 -0.0308 280 ARG   A CB  
1534 C  CG  . ARG   A 187 ? 0.5325 0.4981 0.5141 -0.0233 -0.0743 -0.0447 280 ARG   A CG  
1535 C  CD  . ARG   A 187 ? 0.5655 0.5365 0.5242 -0.0237 -0.0763 -0.0498 280 ARG   A CD  
1536 N  NE  . ARG   A 187 ? 0.5745 0.5299 0.5240 -0.0238 -0.0660 -0.0520 280 ARG   A NE  
1537 C  CZ  . ARG   A 187 ? 0.5904 0.5480 0.5195 -0.0221 -0.0633 -0.0522 280 ARG   A CZ  
1538 N  NH1 . ARG   A 187 ? 0.6159 0.5907 0.5286 -0.0208 -0.0704 -0.0499 280 ARG   A NH1 
1539 N  NH2 . ARG   A 187 ? 0.5922 0.5367 0.5177 -0.0217 -0.0535 -0.0543 280 ARG   A NH2 
1540 N  N   . ASP   A 188 ? 0.4773 0.3970 0.4797 -0.0230 -0.0481 -0.0363 281 ASP   A N   
1541 C  CA  . ASP   A 188 ? 0.4800 0.3865 0.4871 -0.0283 -0.0420 -0.0437 281 ASP   A CA  
1542 C  C   . ASP   A 188 ? 0.4580 0.3619 0.4827 -0.0309 -0.0387 -0.0406 281 ASP   A C   
1543 O  O   . ASP   A 188 ? 0.4681 0.3681 0.5019 -0.0378 -0.0379 -0.0470 281 ASP   A O   
1544 C  CB  . ASP   A 188 ? 0.4908 0.3843 0.4860 -0.0253 -0.0350 -0.0425 281 ASP   A CB  
1545 C  CG  . ASP   A 188 ? 0.5117 0.4104 0.4897 -0.0243 -0.0369 -0.0481 281 ASP   A CG  
1546 O  OD1 . ASP   A 188 ? 0.5408 0.4517 0.5151 -0.0265 -0.0440 -0.0542 281 ASP   A OD1 
1547 O  OD2 . ASP   A 188 ? 0.5394 0.4316 0.5079 -0.0216 -0.0311 -0.0469 281 ASP   A OD2 
1548 N  N   . ARG   A 189 ? 0.4370 0.3434 0.4669 -0.0259 -0.0369 -0.0317 282 ARG   A N   
1549 C  CA  . ARG   A 189 ? 0.4310 0.3398 0.4768 -0.0281 -0.0335 -0.0295 282 ARG   A CA  
1550 C  C   . ARG   A 189 ? 0.4405 0.3653 0.4997 -0.0336 -0.0391 -0.0346 282 ARG   A C   
1551 O  O   . ARG   A 189 ? 0.4495 0.3731 0.5194 -0.0413 -0.0361 -0.0374 282 ARG   A O   
1552 C  CB  . ARG   A 189 ? 0.4148 0.3255 0.4638 -0.0208 -0.0313 -0.0216 282 ARG   A CB  
1553 C  CG  . ARG   A 189 ? 0.4042 0.3221 0.4688 -0.0226 -0.0276 -0.0210 282 ARG   A CG  
1554 C  CD  . ARG   A 189 ? 0.3879 0.3058 0.4558 -0.0153 -0.0243 -0.0160 282 ARG   A CD  
1555 N  NE  . ARG   A 189 ? 0.3784 0.3106 0.4620 -0.0164 -0.0222 -0.0174 282 ARG   A NE  
1556 C  CZ  . ARG   A 189 ? 0.3723 0.3126 0.4645 -0.0095 -0.0215 -0.0164 282 ARG   A CZ  
1557 N  NH1 . ARG   A 189 ? 0.3711 0.3037 0.4584 -0.0010 -0.0235 -0.0131 282 ARG   A NH1 
1558 N  NH2 . ARG   A 189 ? 0.3667 0.3234 0.4736 -0.0112 -0.0187 -0.0191 282 ARG   A NH2 
1559 N  N   . ARG   A 190 ? 0.4481 0.3878 0.5074 -0.0304 -0.0472 -0.0350 283 ARG   A N   
1560 C  CA  . ARG   A 190 ? 0.4646 0.4237 0.5382 -0.0350 -0.0539 -0.0401 283 ARG   A CA  
1561 C  C   . ARG   A 190 ? 0.4719 0.4274 0.5472 -0.0457 -0.0550 -0.0501 283 ARG   A C   
1562 O  O   . ARG   A 190 ? 0.4783 0.4406 0.5701 -0.0538 -0.0544 -0.0532 283 ARG   A O   
1563 C  CB  . ARG   A 190 ? 0.4749 0.4489 0.5440 -0.0287 -0.0640 -0.0386 283 ARG   A CB  
1564 C  CG  . ARG   A 190 ? 0.4799 0.4735 0.5669 -0.0243 -0.0683 -0.0356 283 ARG   A CG  
1565 C  CD  . ARG   A 190 ? 0.4901 0.4971 0.5719 -0.0175 -0.0796 -0.0325 283 ARG   A CD  
1566 N  NE  . ARG   A 190 ? 0.4888 0.4913 0.5678 -0.0061 -0.0800 -0.0219 283 ARG   A NE  
1567 C  CZ  . ARG   A 190 ? 0.4922 0.5031 0.5661 0.0014  -0.0896 -0.0155 283 ARG   A CZ  
1568 N  NH1 . ARG   A 190 ? 0.4919 0.4957 0.5659 0.0113  -0.0899 -0.0054 283 ARG   A NH1 
1569 N  NH2 . ARG   A 190 ? 0.5089 0.5346 0.5772 -0.0010 -0.0994 -0.0190 283 ARG   A NH2 
1570 N  N   . THR   A 191 ? 0.4838 0.4290 0.5433 -0.0460 -0.0563 -0.0553 284 THR   A N   
1571 C  CA  . THR   A 191 ? 0.5085 0.4474 0.5683 -0.0549 -0.0582 -0.0671 284 THR   A CA  
1572 C  C   . THR   A 191 ? 0.5126 0.4352 0.5829 -0.0615 -0.0504 -0.0664 284 THR   A C   
1573 O  O   . THR   A 191 ? 0.5287 0.4531 0.6129 -0.0713 -0.0522 -0.0722 284 THR   A O   
1574 C  CB  . THR   A 191 ? 0.5214 0.4534 0.5607 -0.0514 -0.0596 -0.0729 284 THR   A CB  
1575 O  OG1 . THR   A 191 ? 0.5255 0.4747 0.5553 -0.0458 -0.0670 -0.0702 284 THR   A OG1 
1576 C  CG2 . THR   A 191 ? 0.5379 0.4642 0.5775 -0.0591 -0.0624 -0.0879 284 THR   A CG2 
1577 N  N   . GLU   A 192 ? 0.5161 0.4243 0.5808 -0.0567 -0.0425 -0.0587 285 GLU   A N   
1578 C  CA  . GLU   A 192 ? 0.5236 0.4154 0.5954 -0.0618 -0.0356 -0.0560 285 GLU   A CA  
1579 C  C   . GLU   A 192 ? 0.5190 0.4214 0.6082 -0.0679 -0.0332 -0.0505 285 GLU   A C   
1580 O  O   . GLU   A 192 ? 0.5199 0.4136 0.6189 -0.0770 -0.0307 -0.0506 285 GLU   A O   
1581 C  CB  . GLU   A 192 ? 0.5329 0.4103 0.5935 -0.0544 -0.0289 -0.0493 285 GLU   A CB  
1582 C  CG  . GLU   A 192 ? 0.5493 0.4142 0.5967 -0.0511 -0.0291 -0.0560 285 GLU   A CG  
1583 C  CD  . GLU   A 192 ? 0.5628 0.4109 0.6055 -0.0470 -0.0224 -0.0514 285 GLU   A CD  
1584 O  OE1 . GLU   A 192 ? 0.5597 0.4012 0.6102 -0.0493 -0.0182 -0.0443 285 GLU   A OE1 
1585 O  OE2 . GLU   A 192 ? 0.5809 0.4244 0.6118 -0.0415 -0.0214 -0.0547 285 GLU   A OE2 
1586 N  N   . GLU   A 193 ? 0.5122 0.4330 0.6060 -0.0633 -0.0341 -0.0460 286 GLU   A N   
1587 C  CA  . GLU   A 193 ? 0.5114 0.4474 0.6224 -0.0682 -0.0311 -0.0418 286 GLU   A CA  
1588 C  C   . GLU   A 193 ? 0.5306 0.4805 0.6573 -0.0788 -0.0367 -0.0488 286 GLU   A C   
1589 O  O   . GLU   A 193 ? 0.5114 0.4676 0.6530 -0.0877 -0.0325 -0.0460 286 GLU   A O   
1590 C  CB  . GLU   A 193 ? 0.4968 0.4480 0.6093 -0.0583 -0.0305 -0.0369 286 GLU   A CB  
1591 C  CG  . GLU   A 193 ? 0.4833 0.4234 0.5879 -0.0521 -0.0227 -0.0297 286 GLU   A CG  
1592 C  CD  . GLU   A 193 ? 0.4756 0.4246 0.5797 -0.0410 -0.0227 -0.0264 286 GLU   A CD  
1593 O  OE1 . GLU   A 193 ? 0.4788 0.4426 0.5888 -0.0368 -0.0291 -0.0284 286 GLU   A OE1 
1594 O  OE2 . GLU   A 193 ? 0.4639 0.4044 0.5622 -0.0365 -0.0168 -0.0221 286 GLU   A OE2 
1595 N  N   . GLU   A 194 ? 0.5589 0.5146 0.6823 -0.0787 -0.0457 -0.0575 287 GLU   A N   
1596 C  CA  . GLU   A 194 ? 0.5873 0.5589 0.7264 -0.0890 -0.0526 -0.0658 287 GLU   A CA  
1597 C  C   . GLU   A 194 ? 0.6084 0.5639 0.7561 -0.1024 -0.0497 -0.0691 287 GLU   A C   
1598 O  O   . GLU   A 194 ? 0.6110 0.5793 0.7769 -0.1137 -0.0527 -0.0732 287 GLU   A O   
1599 C  CB  . GLU   A 194 ? 0.6093 0.5914 0.7402 -0.0852 -0.0636 -0.0746 287 GLU   A CB  
1600 C  CG  . GLU   A 194 ? 0.6348 0.5999 0.7532 -0.0886 -0.0669 -0.0850 287 GLU   A CG  
1601 C  CD  . GLU   A 194 ? 0.6520 0.6302 0.7586 -0.0845 -0.0774 -0.0934 287 GLU   A CD  
1602 O  OE1 . GLU   A 194 ? 0.6462 0.6117 0.7347 -0.0812 -0.0778 -0.0989 287 GLU   A OE1 
1603 O  OE2 . GLU   A 194 ? 0.6734 0.6763 0.7890 -0.0845 -0.0852 -0.0945 287 GLU   A OE2 
1604 N  N   . ASN   A 195 ? 0.6295 0.5587 0.7667 -0.1013 -0.0441 -0.0662 288 ASN   A N   
1605 C  CA  . ASN   A 195 ? 0.6623 0.5717 0.8079 -0.1124 -0.0403 -0.0654 288 ASN   A CA  
1606 C  C   . ASN   A 195 ? 0.6665 0.5818 0.8239 -0.1179 -0.0320 -0.0526 288 ASN   A C   
1607 O  O   . ASN   A 195 ? 0.6625 0.5996 0.8247 -0.1145 -0.0293 -0.0473 288 ASN   A O   
1608 C  CB  . ASN   A 195 ? 0.6718 0.5529 0.8025 -0.1069 -0.0376 -0.0658 288 ASN   A CB  
1609 C  CG  . ASN   A 195 ? 0.6890 0.5649 0.8084 -0.1028 -0.0444 -0.0797 288 ASN   A CG  
1610 O  OD1 . ASN   A 195 ? 0.6875 0.5821 0.8043 -0.1008 -0.0511 -0.0865 288 ASN   A OD1 
1611 N  ND2 . ASN   A 195 ? 0.7164 0.5684 0.8289 -0.1009 -0.0429 -0.0839 288 ASN   A ND2 
1612 N  N   . VAL   B 4   ? 0.6251 0.2808 0.8449 0.0543  0.0155  -0.0653 97  VAL   B N   
1613 C  CA  . VAL   B 4   ? 0.6006 0.2736 0.7985 0.0414  0.0153  -0.0648 97  VAL   B CA  
1614 C  C   . VAL   B 4   ? 0.5914 0.2681 0.7784 0.0386  0.0135  -0.0396 97  VAL   B C   
1615 O  O   . VAL   B 4   ? 0.6093 0.2683 0.8067 0.0384  0.0127  -0.0240 97  VAL   B O   
1616 C  CB  . VAL   B 4   ? 0.6104 0.2729 0.8132 0.0296  0.0158  -0.0780 97  VAL   B CB  
1617 C  CG1 . VAL   B 4   ? 0.5925 0.2732 0.7748 0.0180  0.0150  -0.0755 97  VAL   B CG1 
1618 C  CG2 . VAL   B 4   ? 0.6224 0.2844 0.8354 0.0322  0.0175  -0.1058 97  VAL   B CG2 
1619 N  N   . PRO   B 5   ? 0.5644 0.2645 0.7309 0.0361  0.0131  -0.0352 98  PRO   B N   
1620 C  CA  . PRO   B 5   ? 0.5565 0.2627 0.7121 0.0331  0.0116  -0.0149 98  PRO   B CA  
1621 C  C   . PRO   B 5   ? 0.5562 0.2541 0.7106 0.0218  0.0115  -0.0085 98  PRO   B C   
1622 O  O   . PRO   B 5   ? 0.5588 0.2561 0.7126 0.0140  0.0122  -0.0216 98  PRO   B O   
1623 C  CB  . PRO   B 5   ? 0.5289 0.2598 0.6651 0.0319  0.0114  -0.0174 98  PRO   B CB  
1624 C  CG  . PRO   B 5   ? 0.5297 0.2681 0.6640 0.0306  0.0131  -0.0380 98  PRO   B CG  
1625 C  CD  . PRO   B 5   ? 0.5486 0.2707 0.7023 0.0362  0.0142  -0.0493 98  PRO   B CD  
1626 N  N   . SER   B 6   ? 0.5669 0.2621 0.7211 0.0211  0.0108  0.0115  99  SER   B N   
1627 C  CA  . SER   B 6   ? 0.5791 0.2683 0.7344 0.0108  0.0114  0.0212  99  SER   B CA  
1628 C  C   . SER   B 6   ? 0.5637 0.2701 0.7030 0.0024  0.0114  0.0146  99  SER   B C   
1629 O  O   . SER   B 6   ? 0.5475 0.2713 0.6720 0.0053  0.0107  0.0140  99  SER   B O   
1630 C  CB  . SER   B 6   ? 0.5868 0.2767 0.7418 0.0129  0.0109  0.0447  99  SER   B CB  
1631 O  OG  . SER   B 6   ? 0.6096 0.2998 0.7635 0.0022  0.0121  0.0537  99  SER   B OG  
1632 N  N   . GLN   B 7   ? 0.5755 0.2770 0.7195 -0.0076 0.0121  0.0101  100 GLN   B N   
1633 C  CA  . GLN   B 7   ? 0.5647 0.2824 0.6963 -0.0152 0.0118  0.0050  100 GLN   B CA  
1634 C  C   . GLN   B 7   ? 0.5687 0.2887 0.7019 -0.0229 0.0128  0.0191  100 GLN   B C   
1635 O  O   . GLN   B 7   ? 0.5690 0.3029 0.6947 -0.0288 0.0126  0.0159  100 GLN   B O   
1636 C  CB  . GLN   B 7   ? 0.5659 0.2830 0.7014 -0.0203 0.0114  -0.0149 100 GLN   B CB  
1637 C  CG  . GLN   B 7   ? 0.5856 0.2856 0.7398 -0.0284 0.0121  -0.0192 100 GLN   B CG  
1638 C  CD  . GLN   B 7   ? 0.5799 0.2848 0.7361 -0.0344 0.0111  -0.0406 100 GLN   B CD  
1639 O  OE1 . GLN   B 7   ? 0.5821 0.2847 0.7409 -0.0300 0.0110  -0.0562 100 GLN   B OE1 
1640 N  NE2 . GLN   B 7   ? 0.5726 0.2879 0.7274 -0.0442 0.0104  -0.0420 100 GLN   B NE2 
1641 N  N   . LYS   B 8   ? 0.5758 0.2849 0.7182 -0.0221 0.0139  0.0353  101 LYS   B N   
1642 C  CA  . LYS   B 8   ? 0.5806 0.2921 0.7267 -0.0303 0.0157  0.0507  101 LYS   B CA  
1643 C  C   . LYS   B 8   ? 0.5512 0.2874 0.6797 -0.0293 0.0158  0.0578  101 LYS   B C   
1644 O  O   . LYS   B 8   ? 0.5349 0.2791 0.6534 -0.0209 0.0149  0.0632  101 LYS   B O   
1645 C  CB  . LYS   B 8   ? 0.6056 0.2997 0.7650 -0.0280 0.0167  0.0681  101 LYS   B CB  
1646 C  CG  . LYS   B 8   ? 0.6282 0.3245 0.7925 -0.0361 0.0192  0.0881  101 LYS   B CG  
1647 C  CD  . LYS   B 8   ? 0.6510 0.3338 0.8244 -0.0304 0.0195  0.1089  101 LYS   B CD  
1648 C  CE  . LYS   B 8   ? 0.6738 0.3292 0.8637 -0.0235 0.0180  0.1023  101 LYS   B CE  
1649 N  NZ  . LYS   B 8   ? 0.7043 0.3410 0.9095 -0.0212 0.0186  0.1246  101 LYS   B NZ  
1650 N  N   . THR   B 9   ? 0.5464 0.2952 0.6726 -0.0376 0.0169  0.0565  102 THR   B N   
1651 C  CA  . THR   B 9   ? 0.5238 0.2964 0.6358 -0.0367 0.0174  0.0610  102 THR   B CA  
1652 C  C   . THR   B 9   ? 0.5283 0.3075 0.6378 -0.0347 0.0192  0.0804  102 THR   B C   
1653 O  O   . THR   B 9   ? 0.5322 0.3004 0.6537 -0.0391 0.0210  0.0933  102 THR   B O   
1654 C  CB  . THR   B 9   ? 0.5299 0.3149 0.6436 -0.0455 0.0184  0.0560  102 THR   B CB  
1655 O  OG1 . THR   B 9   ? 0.5242 0.3051 0.6391 -0.0465 0.0159  0.0387  102 THR   B OG1 
1656 C  CG2 . THR   B 9   ? 0.5228 0.3319 0.6240 -0.0431 0.0190  0.0586  102 THR   B CG2 
1657 N  N   . TYR   B 10  ? 0.5063 0.3035 0.6014 -0.0284 0.0187  0.0823  103 TYR   B N   
1658 C  CA  . TYR   B 10  ? 0.5169 0.3267 0.6061 -0.0249 0.0197  0.0987  103 TYR   B CA  
1659 C  C   . TYR   B 10  ? 0.5019 0.3362 0.5760 -0.0217 0.0196  0.0936  103 TYR   B C   
1660 O  O   . TYR   B 10  ? 0.5026 0.3388 0.5685 -0.0149 0.0171  0.0850  103 TYR   B O   
1661 C  CB  . TYR   B 10  ? 0.5201 0.3192 0.6106 -0.0164 0.0173  0.1040  103 TYR   B CB  
1662 C  CG  . TYR   B 10  ? 0.5215 0.3369 0.6046 -0.0115 0.0172  0.1201  103 TYR   B CG  
1663 C  CD1 . TYR   B 10  ? 0.5356 0.3605 0.6206 -0.0162 0.0200  0.1386  103 TYR   B CD1 
1664 C  CD2 . TYR   B 10  ? 0.5189 0.3428 0.5933 -0.0025 0.0142  0.1171  103 TYR   B CD2 
1665 C  CE1 . TYR   B 10  ? 0.5398 0.3836 0.6165 -0.0115 0.0196  0.1539  103 TYR   B CE1 
1666 C  CE2 . TYR   B 10  ? 0.5206 0.3632 0.5876 0.0020  0.0133  0.1306  103 TYR   B CE2 
1667 C  CZ  . TYR   B 10  ? 0.5333 0.3867 0.6007 -0.0020 0.0159  0.1492  103 TYR   B CZ  
1668 O  OH  . TYR   B 10  ? 0.5417 0.4178 0.6003 0.0026  0.0148  0.1625  103 TYR   B OH  
1669 N  N   . GLN   B 11  ? 0.5046 0.3573 0.5765 -0.0267 0.0226  0.0983  104 GLN   B N   
1670 C  CA  . GLN   B 11  ? 0.4952 0.3722 0.5545 -0.0230 0.0230  0.0923  104 GLN   B CA  
1671 C  C   . GLN   B 11  ? 0.4917 0.3817 0.5417 -0.0169 0.0223  0.1008  104 GLN   B C   
1672 O  O   . GLN   B 11  ? 0.4724 0.3746 0.5122 -0.0114 0.0207  0.0910  104 GLN   B O   
1673 C  CB  . GLN   B 11  ? 0.5043 0.3999 0.5657 -0.0294 0.0268  0.0944  104 GLN   B CB  
1674 C  CG  . GLN   B 11  ? 0.5084 0.3958 0.5786 -0.0347 0.0265  0.0839  104 GLN   B CG  
1675 C  CD  . GLN   B 11  ? 0.5138 0.4242 0.5859 -0.0392 0.0298  0.0829  104 GLN   B CD  
1676 O  OE1 . GLN   B 11  ? 0.5428 0.4726 0.6135 -0.0419 0.0336  0.0938  104 GLN   B OE1 
1677 N  NE2 . GLN   B 11  ? 0.5170 0.4277 0.5926 -0.0399 0.0282  0.0703  104 GLN   B NE2 
1678 N  N   . GLY   B 12  ? 0.4955 0.3831 0.5499 -0.0180 0.0231  0.1187  105 GLY   B N   
1679 C  CA  . GLY   B 12  ? 0.4972 0.3991 0.5435 -0.0120 0.0218  0.1298  105 GLY   B CA  
1680 C  C   . GLY   B 12  ? 0.4893 0.4246 0.5229 -0.0113 0.0237  0.1289  105 GLY   B C   
1681 O  O   . GLY   B 12  ? 0.4738 0.4217 0.5075 -0.0166 0.0274  0.1259  105 GLY   B O   
1682 N  N   . SER   B 13  ? 0.4871 0.4382 0.5107 -0.0046 0.0210  0.1292  106 SER   B N   
1683 C  CA  . SER   B 13  ? 0.5031 0.4902 0.5142 -0.0033 0.0225  0.1319  106 SER   B CA  
1684 C  C   . SER   B 13  ? 0.4950 0.4952 0.5002 -0.0031 0.0239  0.1109  106 SER   B C   
1685 O  O   . SER   B 13  ? 0.4851 0.5142 0.4836 -0.0042 0.0272  0.1113  106 SER   B O   
1686 C  CB  . SER   B 13  ? 0.5204 0.5197 0.5241 0.0036  0.0183  0.1365  106 SER   B CB  
1687 O  OG  . SER   B 13  ? 0.5447 0.5814 0.5355 0.0049  0.0192  0.1367  106 SER   B OG  
1688 N  N   . TYR   B 14  ? 0.4812 0.4617 0.4897 -0.0013 0.0215  0.0936  107 TYR   B N   
1689 C  CA  . TYR   B 14  ? 0.4742 0.4624 0.4786 0.0009  0.0215  0.0730  107 TYR   B CA  
1690 C  C   . TYR   B 14  ? 0.4690 0.4464 0.4811 -0.0025 0.0239  0.0669  107 TYR   B C   
1691 O  O   . TYR   B 14  ? 0.4557 0.4349 0.4670 0.0002  0.0235  0.0509  107 TYR   B O   
1692 C  CB  . TYR   B 14  ? 0.4657 0.4418 0.4678 0.0055  0.0170  0.0601  107 TYR   B CB  
1693 C  CG  . TYR   B 14  ? 0.4792 0.4728 0.4739 0.0090  0.0144  0.0637  107 TYR   B CG  
1694 C  CD1 . TYR   B 14  ? 0.4873 0.5109 0.4727 0.0109  0.0149  0.0566  107 TYR   B CD1 
1695 C  CD2 . TYR   B 14  ? 0.4872 0.4703 0.4845 0.0108  0.0114  0.0744  107 TYR   B CD2 
1696 C  CE1 . TYR   B 14  ? 0.4978 0.5422 0.4758 0.0137  0.0120  0.0602  107 TYR   B CE1 
1697 C  CE2 . TYR   B 14  ? 0.4980 0.5010 0.4890 0.0145  0.0085  0.0796  107 TYR   B CE2 
1698 C  CZ  . TYR   B 14  ? 0.5020 0.5366 0.4827 0.0156  0.0086  0.0727  107 TYR   B CZ  
1699 O  OH  . TYR   B 14  ? 0.5178 0.5758 0.4917 0.0191  0.0051  0.0764  107 TYR   B OH  
1700 N  N   . GLY   B 15  ? 0.4729 0.4406 0.4935 -0.0085 0.0260  0.0791  108 GLY   B N   
1701 C  CA  . GLY   B 15  ? 0.4729 0.4337 0.5022 -0.0129 0.0277  0.0743  108 GLY   B CA  
1702 C  C   . GLY   B 15  ? 0.4618 0.4012 0.4937 -0.0101 0.0241  0.0599  108 GLY   B C   
1703 O  O   . GLY   B 15  ? 0.4578 0.4025 0.4903 -0.0082 0.0243  0.0484  108 GLY   B O   
1704 N  N   . PHE   B 16  ? 0.4599 0.3771 0.4938 -0.0095 0.0211  0.0613  109 PHE   B N   
1705 C  CA  . PHE   B 16  ? 0.4550 0.3534 0.4896 -0.0070 0.0178  0.0495  109 PHE   B CA  
1706 C  C   . PHE   B 16  ? 0.4464 0.3329 0.4897 -0.0117 0.0178  0.0473  109 PHE   B C   
1707 O  O   . PHE   B 16  ? 0.4578 0.3346 0.5086 -0.0168 0.0186  0.0550  109 PHE   B O   
1708 C  CB  . PHE   B 16  ? 0.4509 0.3364 0.4840 -0.0042 0.0152  0.0516  109 PHE   B CB  
1709 C  CG  . PHE   B 16  ? 0.4468 0.3144 0.4815 -0.0030 0.0126  0.0423  109 PHE   B CG  
1710 C  CD1 . PHE   B 16  ? 0.4420 0.3101 0.4721 0.0000  0.0111  0.0312  109 PHE   B CD1 
1711 C  CD2 . PHE   B 16  ? 0.4476 0.2983 0.4891 -0.0048 0.0119  0.0446  109 PHE   B CD2 
1712 C  CE1 . PHE   B 16  ? 0.4379 0.2920 0.4688 0.0003  0.0091  0.0249  109 PHE   B CE1 
1713 C  CE2 . PHE   B 16  ? 0.4508 0.2895 0.4926 -0.0037 0.0101  0.0357  109 PHE   B CE2 
1714 C  CZ  . PHE   B 16  ? 0.4411 0.2824 0.4770 -0.0014 0.0088  0.0270  109 PHE   B CZ  
1715 N  N   . ARG   B 17  ? 0.4308 0.3187 0.4739 -0.0100 0.0167  0.0369  110 ARG   B N   
1716 C  CA  . ARG   B 17  ? 0.4331 0.3143 0.4831 -0.0135 0.0156  0.0327  110 ARG   B CA  
1717 C  C   . ARG   B 17  ? 0.4151 0.2877 0.4613 -0.0089 0.0123  0.0229  110 ARG   B C   
1718 O  O   . ARG   B 17  ? 0.4066 0.2810 0.4468 -0.0035 0.0116  0.0188  110 ARG   B O   
1719 C  CB  . ARG   B 17  ? 0.4469 0.3462 0.5019 -0.0160 0.0178  0.0325  110 ARG   B CB  
1720 C  CG  . ARG   B 17  ? 0.4731 0.3848 0.5327 -0.0222 0.0219  0.0434  110 ARG   B CG  
1721 C  CD  . ARG   B 17  ? 0.4763 0.4140 0.5354 -0.0204 0.0248  0.0417  110 ARG   B CD  
1722 N  NE  . ARG   B 17  ? 0.4833 0.4291 0.5325 -0.0131 0.0251  0.0385  110 ARG   B NE  
1723 C  CZ  . ARG   B 17  ? 0.4744 0.4357 0.5209 -0.0067 0.0257  0.0292  110 ARG   B CZ  
1724 N  NH1 . ARG   B 17  ? 0.4748 0.4422 0.5130 -0.0013 0.0257  0.0249  110 ARG   B NH1 
1725 N  NH2 . ARG   B 17  ? 0.4725 0.4437 0.5256 -0.0054 0.0260  0.0232  110 ARG   B NH2 
1726 N  N   . LEU   B 18  ? 0.4089 0.2737 0.4590 -0.0114 0.0104  0.0194  111 LEU   B N   
1727 C  CA  . LEU   B 18  ? 0.3953 0.2547 0.4420 -0.0078 0.0073  0.0126  111 LEU   B CA  
1728 C  C   . LEU   B 18  ? 0.3884 0.2602 0.4386 -0.0064 0.0063  0.0098  111 LEU   B C   
1729 O  O   . LEU   B 18  ? 0.3839 0.2664 0.4408 -0.0107 0.0077  0.0116  111 LEU   B O   
1730 C  CB  . LEU   B 18  ? 0.4035 0.2513 0.4513 -0.0111 0.0057  0.0104  111 LEU   B CB  
1731 C  CG  . LEU   B 18  ? 0.4069 0.2430 0.4533 -0.0111 0.0064  0.0122  111 LEU   B CG  
1732 C  CD1 . LEU   B 18  ? 0.4045 0.2321 0.4525 -0.0133 0.0051  0.0070  111 LEU   B CD1 
1733 C  CD2 . LEU   B 18  ? 0.4062 0.2409 0.4455 -0.0060 0.0062  0.0122  111 LEU   B CD2 
1734 N  N   . GLY   B 19  ? 0.3821 0.2531 0.4291 -0.0003 0.0041  0.0061  112 GLY   B N   
1735 C  CA  . GLY   B 19  ? 0.3751 0.2563 0.4262 0.0031  0.0019  0.0039  112 GLY   B CA  
1736 C  C   . GLY   B 19  ? 0.3688 0.2418 0.4164 0.0054  -0.0018 0.0031  112 GLY   B C   
1737 O  O   . GLY   B 19  ? 0.3747 0.2345 0.4163 0.0054  -0.0019 0.0035  112 GLY   B O   
1738 N  N   . PHE   B 20  ? 0.3672 0.2503 0.4184 0.0074  -0.0047 0.0027  113 PHE   B N   
1739 C  CA  . PHE   B 20  ? 0.3759 0.2560 0.4233 0.0099  -0.0088 0.0041  113 PHE   B CA  
1740 C  C   . PHE   B 20  ? 0.3798 0.2694 0.4320 0.0183  -0.0117 0.0056  113 PHE   B C   
1741 O  O   . PHE   B 20  ? 0.3694 0.2733 0.4291 0.0200  -0.0109 0.0036  113 PHE   B O   
1742 C  CB  . PHE   B 20  ? 0.3796 0.2654 0.4267 0.0028  -0.0103 0.0022  113 PHE   B CB  
1743 C  CG  . PHE   B 20  ? 0.3813 0.2562 0.4265 -0.0038 -0.0074 0.0001  113 PHE   B CG  
1744 C  CD1 . PHE   B 20  ? 0.3876 0.2511 0.4257 -0.0041 -0.0072 0.0000  113 PHE   B CD1 
1745 C  CD2 . PHE   B 20  ? 0.3901 0.2668 0.4417 -0.0095 -0.0047 -0.0009 113 PHE   B CD2 
1746 C  CE1 . PHE   B 20  ? 0.3926 0.2470 0.4307 -0.0086 -0.0047 -0.0022 113 PHE   B CE1 
1747 C  CE2 . PHE   B 20  ? 0.3872 0.2523 0.4389 -0.0142 -0.0023 -0.0017 113 PHE   B CE2 
1748 C  CZ  . PHE   B 20  ? 0.3918 0.2459 0.4370 -0.0131 -0.0025 -0.0030 113 PHE   B CZ  
1749 N  N   . LEU   B 21  ? 0.3851 0.2677 0.4339 0.0236  -0.0148 0.0098  114 LEU   B N   
1750 C  CA  . LEU   B 21  ? 0.3984 0.2888 0.4529 0.0330  -0.0185 0.0130  114 LEU   B CA  
1751 C  C   . LEU   B 21  ? 0.3925 0.3056 0.4510 0.0313  -0.0218 0.0127  114 LEU   B C   
1752 O  O   . LEU   B 21  ? 0.3857 0.3032 0.4397 0.0231  -0.0224 0.0112  114 LEU   B O   
1753 C  CB  . LEU   B 21  ? 0.4145 0.2912 0.4643 0.0374  -0.0211 0.0204  114 LEU   B CB  
1754 C  CG  . LEU   B 21  ? 0.4192 0.2742 0.4676 0.0388  -0.0184 0.0201  114 LEU   B CG  
1755 C  CD1 . LEU   B 21  ? 0.4368 0.2793 0.4810 0.0404  -0.0209 0.0295  114 LEU   B CD1 
1756 C  CD2 . LEU   B 21  ? 0.4221 0.2752 0.4798 0.0469  -0.0172 0.0149  114 LEU   B CD2 
1757 N  N   . HIS   B 22  ? 0.3911 0.3200 0.4593 0.0384  -0.0236 0.0123  115 HIS   B N   
1758 C  CA  . HIS   B 22  ? 0.3924 0.3472 0.4665 0.0375  -0.0276 0.0117  115 HIS   B CA  
1759 C  C   . HIS   B 22  ? 0.3957 0.3547 0.4675 0.0453  -0.0339 0.0198  115 HIS   B C   
1760 O  O   . HIS   B 22  ? 0.4037 0.3719 0.4839 0.0563  -0.0370 0.0232  115 HIS   B O   
1761 C  CB  . HIS   B 22  ? 0.3932 0.3662 0.4797 0.0408  -0.0257 0.0072  115 HIS   B CB  
1762 C  CG  . HIS   B 22  ? 0.3930 0.3602 0.4795 0.0336  -0.0191 0.0024  115 HIS   B CG  
1763 N  ND1 . HIS   B 22  ? 0.3897 0.3548 0.4731 0.0209  -0.0166 0.0004  115 HIS   B ND1 
1764 C  CD2 . HIS   B 22  ? 0.3960 0.3594 0.4850 0.0377  -0.0146 -0.0004 115 HIS   B CD2 
1765 C  CE1 . HIS   B 22  ? 0.3854 0.3458 0.4693 0.0176  -0.0111 -0.0011 115 HIS   B CE1 
1766 N  NE2 . HIS   B 22  ? 0.3882 0.3493 0.4747 0.0275  -0.0097 -0.0020 115 HIS   B NE2 
1767 N  N   A SER   B 23  ? 0.4004 0.3539 0.4614 0.0402  -0.0356 0.0234  116 SER   B N   
1768 N  N   B SER   B 23  ? 0.4006 0.3539 0.4616 0.0403  -0.0357 0.0234  116 SER   B N   
1769 C  CA  A SER   B 23  ? 0.4100 0.3616 0.4651 0.0467  -0.0405 0.0344  116 SER   B CA  
1770 C  CA  B SER   B 23  ? 0.4109 0.3626 0.4661 0.0469  -0.0405 0.0345  116 SER   B CA  
1771 C  C   A SER   B 23  ? 0.4154 0.3964 0.4714 0.0483  -0.0471 0.0372  116 SER   B C   
1772 C  C   B SER   B 23  ? 0.4160 0.3971 0.4720 0.0484  -0.0472 0.0372  116 SER   B C   
1773 O  O   A SER   B 23  ? 0.4256 0.4106 0.4801 0.0571  -0.0521 0.0487  116 SER   B O   
1774 O  O   B SER   B 23  ? 0.4270 0.4122 0.4815 0.0572  -0.0522 0.0488  116 SER   B O   
1775 C  CB  A SER   B 23  ? 0.4123 0.3470 0.4550 0.0402  -0.0382 0.0370  116 SER   B CB  
1776 C  CB  B SER   B 23  ? 0.4131 0.3479 0.4559 0.0404  -0.0383 0.0371  116 SER   B CB  
1777 O  OG  A SER   B 23  ? 0.4062 0.3161 0.4489 0.0398  -0.0330 0.0352  116 SER   B OG  
1778 O  OG  B SER   B 23  ? 0.4020 0.3397 0.4409 0.0290  -0.0353 0.0273  116 SER   B OG  
1779 N  N   . GLY   B 24  ? 0.4070 0.4083 0.4660 0.0399  -0.0475 0.0275  117 GLY   B N   
1780 C  CA  . GLY   B 24  ? 0.4176 0.4505 0.4772 0.0390  -0.0541 0.0272  117 GLY   B CA  
1781 C  C   . GLY   B 24  ? 0.4319 0.4689 0.4772 0.0336  -0.0564 0.0292  117 GLY   B C   
1782 O  O   . GLY   B 24  ? 0.4228 0.4374 0.4587 0.0293  -0.0520 0.0296  117 GLY   B O   
1783 N  N   . THR   B 25  ? 0.4535 0.5212 0.4970 0.0343  -0.0632 0.0304  118 THR   B N   
1784 C  CA  . THR   B 25  ? 0.4789 0.5610 0.5089 0.0279  -0.0659 0.0288  118 THR   B CA  
1785 C  C   . THR   B 25  ? 0.5119 0.6116 0.5349 0.0381  -0.0730 0.0453  118 THR   B C   
1786 O  O   . THR   B 25  ? 0.5270 0.6546 0.5414 0.0343  -0.0777 0.0434  118 THR   B O   
1787 C  CB  . THR   B 25  ? 0.4738 0.5811 0.5079 0.0165  -0.0677 0.0117  118 THR   B CB  
1788 O  OG1 . THR   B 25  ? 0.4758 0.6121 0.5210 0.0212  -0.0737 0.0122  118 THR   B OG1 
1789 C  CG2 . THR   B 25  ? 0.4604 0.5484 0.5017 0.0058  -0.0607 -0.0022 118 THR   B CG2 
1790 N  N   . ALA   B 26  ? 0.5434 0.6278 0.5701 0.0506  -0.0738 0.0610  119 ALA   B N   
1791 C  CA  . ALA   B 26  ? 0.5774 0.6730 0.5984 0.0612  -0.0802 0.0808  119 ALA   B CA  
1792 C  C   . ALA   B 26  ? 0.6039 0.6934 0.6071 0.0554  -0.0782 0.0878  119 ALA   B C   
1793 O  O   . ALA   B 26  ? 0.6023 0.6653 0.6015 0.0481  -0.0709 0.0819  119 ALA   B O   
1794 C  CB  . ALA   B 26  ? 0.5913 0.6652 0.6230 0.0753  -0.0805 0.0942  119 ALA   B CB  
1795 N  N   . LYS   B 27  ? 0.6542 0.7702 0.6472 0.0587  -0.0845 0.1005  120 LYS   B N   
1796 C  CA  . LYS   B 27  ? 0.6795 0.8006 0.6540 0.0523  -0.0829 0.1071  120 LYS   B CA  
1797 C  C   . LYS   B 27  ? 0.6901 0.7713 0.6624 0.0516  -0.0757 0.1164  120 LYS   B C   
1798 O  O   . LYS   B 27  ? 0.6963 0.7735 0.6576 0.0421  -0.0705 0.1112  120 LYS   B O   
1799 C  CB  . LYS   B 27  ? 0.7115 0.8658 0.6771 0.0596  -0.0913 0.1261  120 LYS   B CB  
1800 C  CG  . LYS   B 27  ? 0.7163 0.9178 0.6794 0.0567  -0.0983 0.1141  120 LYS   B CG  
1801 C  CD  . LYS   B 27  ? 0.7410 0.9803 0.6939 0.0640  -0.1072 0.1332  120 LYS   B CD  
1802 C  CE  . LYS   B 27  ? 0.7438 1.0328 0.6924 0.0585  -0.1138 0.1172  120 LYS   B CE  
1803 N  NZ  . LYS   B 27  ? 0.7721 1.1023 0.7061 0.0638  -0.1220 0.1353  120 LYS   B NZ  
1804 N  N   . SER   B 28  ? 0.7053 0.7590 0.6893 0.0612  -0.0753 0.1275  121 SER   B N   
1805 C  CA  . SER   B 28  ? 0.7206 0.7368 0.7052 0.0617  -0.0698 0.1385  121 SER   B CA  
1806 C  C   . SER   B 28  ? 0.6989 0.6883 0.6865 0.0529  -0.0614 0.1212  121 SER   B C   
1807 O  O   . SER   B 28  ? 0.7203 0.6844 0.7055 0.0496  -0.0564 0.1272  121 SER   B O   
1808 C  CB  . SER   B 28  ? 0.7434 0.7413 0.7419 0.0755  -0.0730 0.1534  121 SER   B CB  
1809 O  OG  . SER   B 28  ? 0.7432 0.7361 0.7568 0.0805  -0.0728 0.1392  121 SER   B OG  
1810 N  N   A VAL   B 29  ? 0.6695 0.6652 0.6626 0.0488  -0.0601 0.1014  122 VAL   B N   
1811 N  N   B VAL   B 29  ? 0.6704 0.6659 0.6636 0.0489  -0.0601 0.1014  122 VAL   B N   
1812 C  CA  A VAL   B 29  ? 0.6383 0.6099 0.6362 0.0423  -0.0530 0.0862  122 VAL   B CA  
1813 C  CA  B VAL   B 29  ? 0.6408 0.6122 0.6388 0.0424  -0.0530 0.0862  122 VAL   B CA  
1814 C  C   A VAL   B 29  ? 0.6270 0.5945 0.6130 0.0316  -0.0478 0.0814  122 VAL   B C   
1815 C  C   B VAL   B 29  ? 0.6279 0.5953 0.6140 0.0316  -0.0478 0.0813  122 VAL   B C   
1816 O  O   A VAL   B 29  ? 0.6325 0.6243 0.6090 0.0259  -0.0492 0.0761  122 VAL   B O   
1817 O  O   B VAL   B 29  ? 0.6321 0.6239 0.6088 0.0260  -0.0492 0.0759  122 VAL   B O   
1818 C  CB  A VAL   B 29  ? 0.6171 0.6003 0.6241 0.0401  -0.0533 0.0692  122 VAL   B CB  
1819 C  CB  B VAL   B 29  ? 0.6231 0.6058 0.6301 0.0401  -0.0532 0.0692  122 VAL   B CB  
1820 C  CG1 A VAL   B 29  ? 0.6028 0.5645 0.6135 0.0333  -0.0463 0.0561  122 VAL   B CG1 
1821 C  CG1 B VAL   B 29  ? 0.6109 0.6023 0.6120 0.0280  -0.0501 0.0534  122 VAL   B CG1 
1822 C  CG2 A VAL   B 29  ? 0.6152 0.6055 0.6353 0.0511  -0.0578 0.0733  122 VAL   B CG2 
1823 C  CG2 B VAL   B 29  ? 0.6165 0.5765 0.6360 0.0438  -0.0495 0.0643  122 VAL   B CG2 
1824 N  N   . THR   B 30  ? 0.6116 0.5511 0.5989 0.0291  -0.0421 0.0819  123 THR   B N   
1825 C  CA  . THR   B 30  ? 0.5918 0.5256 0.5700 0.0201  -0.0366 0.0782  123 THR   B CA  
1826 C  C   . THR   B 30  ? 0.5515 0.4796 0.5332 0.0138  -0.0323 0.0591  123 THR   B C   
1827 O  O   . THR   B 30  ? 0.5412 0.4727 0.5162 0.0068  -0.0286 0.0519  123 THR   B O   
1828 C  CB  . THR   B 30  ? 0.5963 0.5061 0.5750 0.0206  -0.0335 0.0911  123 THR   B CB  
1829 O  OG1 . THR   B 30  ? 0.5869 0.4721 0.5776 0.0241  -0.0317 0.0866  123 THR   B OG1 
1830 C  CG2 . THR   B 30  ? 0.6137 0.5282 0.5895 0.0262  -0.0377 0.1124  123 THR   B CG2 
1831 N  N   A CYS   B 31  ? 0.5404 0.4611 0.5328 0.0165  -0.0325 0.0516  124 CYS   B N   
1832 N  N   B CYS   B 31  ? 0.5350 0.4553 0.5274 0.0165  -0.0324 0.0516  124 CYS   B N   
1833 C  CA  A CYS   B 31  ? 0.5177 0.4329 0.5149 0.0109  -0.0288 0.0361  124 CYS   B CA  
1834 C  CA  B CYS   B 31  ? 0.5120 0.4271 0.5091 0.0109  -0.0287 0.0361  124 CYS   B CA  
1835 C  C   A CYS   B 31  ? 0.5048 0.4269 0.5123 0.0137  -0.0311 0.0307  124 CYS   B C   
1836 C  C   B CYS   B 31  ? 0.4990 0.4212 0.5065 0.0137  -0.0311 0.0307  124 CYS   B C   
1837 O  O   A CYS   B 31  ? 0.5165 0.4343 0.5305 0.0214  -0.0329 0.0373  124 CYS   B O   
1838 O  O   B CYS   B 31  ? 0.5061 0.4240 0.5200 0.0214  -0.0330 0.0374  124 CYS   B O   
1839 C  CB  A CYS   B 31  ? 0.5172 0.4079 0.5161 0.0096  -0.0235 0.0356  124 CYS   B CB  
1840 C  CB  B CYS   B 31  ? 0.5074 0.3983 0.5062 0.0092  -0.0234 0.0349  124 CYS   B CB  
1841 S  SG  A CYS   B 31  ? 0.5072 0.3883 0.5133 0.0053  -0.0193 0.0219  124 CYS   B SG  
1842 S  SG  B CYS   B 31  ? 0.5072 0.3781 0.5157 0.0166  -0.0231 0.0403  124 CYS   B SG  
1843 N  N   . THR   B 32  ? 0.4803 0.4138 0.4905 0.0075  -0.0309 0.0187  125 THR   B N   
1844 C  CA  . THR   B 32  ? 0.4623 0.4068 0.4832 0.0078  -0.0327 0.0132  125 THR   B CA  
1845 C  C   . THR   B 32  ? 0.4395 0.3801 0.4653 -0.0011 -0.0290 0.0006  125 THR   B C   
1846 O  O   . THR   B 32  ? 0.4353 0.3773 0.4564 -0.0072 -0.0280 -0.0064 125 THR   B O   
1847 C  CB  . THR   B 32  ? 0.4618 0.4340 0.4828 0.0104  -0.0393 0.0153  125 THR   B CB  
1848 O  OG1 . THR   B 32  ? 0.4598 0.4426 0.4930 0.0111  -0.0405 0.0109  125 THR   B OG1 
1849 C  CG2 . THR   B 32  ? 0.4675 0.4582 0.4814 0.0032  -0.0412 0.0073  125 THR   B CG2 
1850 N  N   . TYR   B 33  ? 0.4202 0.3565 0.4559 -0.0014 -0.0269 -0.0014 126 TYR   B N   
1851 C  CA  . TYR   B 33  ? 0.4112 0.3413 0.4537 -0.0095 -0.0231 -0.0097 126 TYR   B CA  
1852 C  C   . TYR   B 33  ? 0.4045 0.3547 0.4573 -0.0144 -0.0254 -0.0155 126 TYR   B C   
1853 O  O   . TYR   B 33  ? 0.3895 0.3533 0.4475 -0.0094 -0.0278 -0.0116 126 TYR   B O   
1854 C  CB  . TYR   B 33  ? 0.4123 0.3250 0.4575 -0.0074 -0.0184 -0.0061 126 TYR   B CB  
1855 C  CG  . TYR   B 33  ? 0.4074 0.3158 0.4608 -0.0148 -0.0147 -0.0107 126 TYR   B CG  
1856 C  CD1 . TYR   B 33  ? 0.4070 0.3030 0.4597 -0.0206 -0.0123 -0.0153 126 TYR   B CD1 
1857 C  CD2 . TYR   B 33  ? 0.4069 0.3244 0.4695 -0.0158 -0.0135 -0.0097 126 TYR   B CD2 
1858 C  CE1 . TYR   B 33  ? 0.4086 0.2983 0.4701 -0.0271 -0.0091 -0.0172 126 TYR   B CE1 
1859 C  CE2 . TYR   B 33  ? 0.4057 0.3196 0.4761 -0.0234 -0.0098 -0.0112 126 TYR   B CE2 
1860 C  CZ  . TYR   B 33  ? 0.4088 0.3073 0.4788 -0.0291 -0.0078 -0.0142 126 TYR   B CZ  
1861 O  OH  . TYR   B 33  ? 0.4220 0.3144 0.5009 -0.0364 -0.0044 -0.0136 126 TYR   B OH  
1862 N  N   . SER   B 34  ? 0.4005 0.3524 0.4577 -0.0241 -0.0247 -0.0255 127 SER   B N   
1863 C  CA  . SER   B 34  ? 0.3984 0.3667 0.4679 -0.0323 -0.0260 -0.0329 127 SER   B CA  
1864 C  C   . SER   B 34  ? 0.3960 0.3500 0.4754 -0.0382 -0.0205 -0.0325 127 SER   B C   
1865 O  O   . SER   B 34  ? 0.3901 0.3260 0.4703 -0.0432 -0.0173 -0.0361 127 SER   B O   
1866 C  CB  . SER   B 34  ? 0.4075 0.3860 0.4769 -0.0400 -0.0288 -0.0454 127 SER   B CB  
1867 O  OG  . SER   B 34  ? 0.4077 0.3998 0.4911 -0.0498 -0.0298 -0.0538 127 SER   B OG  
1868 N  N   . PRO   B 35  ? 0.3874 0.3510 0.4752 -0.0376 -0.0193 -0.0277 128 PRO   B N   
1869 C  CA  . PRO   B 35  ? 0.3898 0.3449 0.4871 -0.0444 -0.0140 -0.0256 128 PRO   B CA  
1870 C  C   . PRO   B 35  ? 0.3986 0.3552 0.5080 -0.0582 -0.0136 -0.0343 128 PRO   B C   
1871 O  O   . PRO   B 35  ? 0.4049 0.3441 0.5196 -0.0642 -0.0094 -0.0327 128 PRO   B O   
1872 C  CB  . PRO   B 35  ? 0.3804 0.3534 0.4839 -0.0405 -0.0130 -0.0200 128 PRO   B CB  
1873 C  CG  . PRO   B 35  ? 0.3784 0.3681 0.4774 -0.0303 -0.0186 -0.0195 128 PRO   B CG  
1874 C  CD  . PRO   B 35  ? 0.3803 0.3651 0.4695 -0.0296 -0.0227 -0.0235 128 PRO   B CD  
1875 N  N   . ALA   B 36  ? 0.4060 0.3831 0.5200 -0.0627 -0.0184 -0.0433 129 ALA   B N   
1876 C  CA  . ALA   B 36  ? 0.4216 0.4028 0.5493 -0.0769 -0.0189 -0.0545 129 ALA   B CA  
1877 C  C   . ALA   B 36  ? 0.4367 0.3932 0.5619 -0.0805 -0.0174 -0.0621 129 ALA   B C   
1878 O  O   . ALA   B 36  ? 0.4469 0.3908 0.5852 -0.0912 -0.0147 -0.0668 129 ALA   B O   
1879 C  CB  . ALA   B 36  ? 0.4189 0.4314 0.5501 -0.0795 -0.0253 -0.0637 129 ALA   B CB  
1880 N  N   . LEU   B 37  ? 0.4399 0.3900 0.5502 -0.0717 -0.0190 -0.0629 130 LEU   B N   
1881 C  CA  . LEU   B 37  ? 0.4504 0.3818 0.5579 -0.0733 -0.0178 -0.0719 130 LEU   B CA  
1882 C  C   . LEU   B 37  ? 0.4534 0.3584 0.5553 -0.0667 -0.0130 -0.0619 130 LEU   B C   
1883 O  O   . LEU   B 37  ? 0.4686 0.3571 0.5709 -0.0675 -0.0113 -0.0686 130 LEU   B O   
1884 C  CB  . LEU   B 37  ? 0.4498 0.3973 0.5445 -0.0687 -0.0224 -0.0797 130 LEU   B CB  
1885 C  CG  . LEU   B 37  ? 0.4546 0.4316 0.5537 -0.0750 -0.0280 -0.0916 130 LEU   B CG  
1886 C  CD1 . LEU   B 37  ? 0.4542 0.4517 0.5371 -0.0678 -0.0328 -0.0930 130 LEU   B CD1 
1887 C  CD2 . LEU   B 37  ? 0.4707 0.4426 0.5836 -0.0875 -0.0275 -0.1096 130 LEU   B CD2 
1888 N  N   . ASN   B 38  ? 0.4411 0.3443 0.5384 -0.0602 -0.0111 -0.0480 131 ASN   B N   
1889 C  CA  . ASN   B 38  ? 0.4380 0.3226 0.5270 -0.0523 -0.0077 -0.0384 131 ASN   B CA  
1890 C  C   . ASN   B 38  ? 0.4377 0.3181 0.5149 -0.0467 -0.0091 -0.0431 131 ASN   B C   
1891 O  O   . ASN   B 38  ? 0.4380 0.3011 0.5147 -0.0456 -0.0065 -0.0445 131 ASN   B O   
1892 C  CB  . ASN   B 38  ? 0.4436 0.3084 0.5418 -0.0566 -0.0032 -0.0339 131 ASN   B CB  
1893 C  CG  . ASN   B 38  ? 0.4351 0.2864 0.5254 -0.0487 -0.0004 -0.0236 131 ASN   B CG  
1894 O  OD1 . ASN   B 38  ? 0.4299 0.2875 0.5105 -0.0415 -0.0009 -0.0179 131 ASN   B OD1 
1895 N  ND2 . ASN   B 38  ? 0.4404 0.2731 0.5358 -0.0499 0.0022  -0.0216 131 ASN   B ND2 
1896 N  N   . LYS   B 39  ? 0.4381 0.3357 0.5066 -0.0431 -0.0130 -0.0447 132 LYS   B N   
1897 C  CA  . LYS   B 39  ? 0.4390 0.3393 0.4963 -0.0397 -0.0144 -0.0495 132 LYS   B CA  
1898 C  C   . LYS   B 39  ? 0.4359 0.3451 0.4814 -0.0315 -0.0167 -0.0395 132 LYS   B C   
1899 O  O   . LYS   B 39  ? 0.4339 0.3596 0.4802 -0.0299 -0.0202 -0.0361 132 LYS   B O   
1900 C  CB  . LYS   B 39  ? 0.4471 0.3629 0.5071 -0.0462 -0.0175 -0.0643 132 LYS   B CB  
1901 C  CG  . LYS   B 39  ? 0.4501 0.3720 0.4990 -0.0438 -0.0180 -0.0712 132 LYS   B CG  
1902 C  CD  . LYS   B 39  ? 0.4623 0.3994 0.5150 -0.0508 -0.0204 -0.0891 132 LYS   B CD  
1903 C  CE  . LYS   B 39  ? 0.4757 0.4215 0.5171 -0.0483 -0.0201 -0.0971 132 LYS   B CE  
1904 N  NZ  . LYS   B 39  ? 0.4923 0.4451 0.5408 -0.0552 -0.0205 -0.1189 132 LYS   B NZ  
1905 N  N   A MET   B 40  ? 0.4418 0.3401 0.4785 -0.0266 -0.0146 -0.0346 133 MET   B N   
1906 N  N   B MET   B 40  ? 0.4363 0.3346 0.4729 -0.0266 -0.0146 -0.0346 133 MET   B N   
1907 C  CA  A MET   B 40  ? 0.4512 0.3540 0.4771 -0.0198 -0.0163 -0.0250 133 MET   B CA  
1908 C  CA  B MET   B 40  ? 0.4388 0.3416 0.4647 -0.0198 -0.0163 -0.0250 133 MET   B CA  
1909 C  C   A MET   B 40  ? 0.4531 0.3727 0.4701 -0.0208 -0.0188 -0.0294 133 MET   B C   
1910 C  C   B MET   B 40  ? 0.4466 0.3660 0.4635 -0.0208 -0.0188 -0.0293 133 MET   B C   
1911 O  O   A MET   B 40  ? 0.4471 0.3651 0.4627 -0.0242 -0.0167 -0.0388 133 MET   B O   
1912 O  O   B MET   B 40  ? 0.4472 0.3653 0.4629 -0.0242 -0.0167 -0.0388 133 MET   B O   
1913 C  CB  A MET   B 40  ? 0.4584 0.3429 0.4804 -0.0162 -0.0125 -0.0187 133 MET   B CB  
1914 C  CB  B MET   B 40  ? 0.4364 0.3209 0.4585 -0.0163 -0.0125 -0.0187 133 MET   B CB  
1915 C  CG  A MET   B 40  ? 0.4720 0.3580 0.4848 -0.0112 -0.0137 -0.0092 133 MET   B CG  
1916 C  CG  B MET   B 40  ? 0.4412 0.3272 0.4534 -0.0116 -0.0134 -0.0100 133 MET   B CG  
1917 S  SD  A MET   B 40  ? 0.4933 0.3837 0.5084 -0.0047 -0.0172 0.0008  133 MET   B SD  
1918 S  SD  B MET   B 40  ? 0.4393 0.3057 0.4496 -0.0094 -0.0091 -0.0048 133 MET   B SD  
1919 C  CE  A MET   B 40  ? 0.4786 0.3512 0.5003 -0.0027 -0.0134 0.0023  133 MET   B CE  
1920 C  CE  B MET   B 40  ? 0.4335 0.2913 0.4507 -0.0057 -0.0091 0.0000  133 MET   B CE  
1921 N  N   . PHE   B 41  ? 0.4491 0.3857 0.4608 -0.0174 -0.0232 -0.0228 134 PHE   B N   
1922 C  CA  . PHE   B 41  ? 0.4607 0.4161 0.4609 -0.0169 -0.0258 -0.0219 134 PHE   B CA  
1923 C  C   . PHE   B 41  ? 0.4631 0.4109 0.4553 -0.0107 -0.0253 -0.0059 134 PHE   B C   
1924 O  O   . PHE   B 41  ? 0.4554 0.3990 0.4510 -0.0053 -0.0274 0.0041  134 PHE   B O   
1925 C  CB  . PHE   B 41  ? 0.4655 0.4481 0.4661 -0.0176 -0.0319 -0.0243 134 PHE   B CB  
1926 C  CG  . PHE   B 41  ? 0.4705 0.4607 0.4814 -0.0252 -0.0327 -0.0405 134 PHE   B CG  
1927 C  CD1 . PHE   B 41  ? 0.4608 0.4408 0.4850 -0.0272 -0.0317 -0.0417 134 PHE   B CD1 
1928 C  CD2 . PHE   B 41  ? 0.4775 0.4864 0.4855 -0.0310 -0.0344 -0.0551 134 PHE   B CD2 
1929 C  CE1 . PHE   B 41  ? 0.4640 0.4495 0.4994 -0.0358 -0.0320 -0.0555 134 PHE   B CE1 
1930 C  CE2 . PHE   B 41  ? 0.4837 0.4977 0.5035 -0.0391 -0.0352 -0.0712 134 PHE   B CE2 
1931 C  CZ  . PHE   B 41  ? 0.4800 0.4812 0.5141 -0.0420 -0.0340 -0.0706 134 PHE   B CZ  
1932 N  N   . CYS   B 42  ? 0.4819 0.4279 0.4655 -0.0116 -0.0224 -0.0040 135 CYS   B N   
1933 C  CA  . CYS   B 42  ? 0.4917 0.4284 0.4695 -0.0078 -0.0212 0.0113  135 CYS   B CA  
1934 C  C   . CYS   B 42  ? 0.5079 0.4614 0.4733 -0.0099 -0.0205 0.0147  135 CYS   B C   
1935 O  O   . CYS   B 42  ? 0.5033 0.4720 0.4653 -0.0141 -0.0195 0.0019  135 CYS   B O   
1936 C  CB  . CYS   B 42  ? 0.4934 0.4048 0.4766 -0.0077 -0.0165 0.0115  135 CYS   B CB  
1937 S  SG  . CYS   B 42  ? 0.5017 0.4086 0.4857 -0.0128 -0.0111 -0.0025 135 CYS   B SG  
1938 N  N   . GLN   B 43  ? 0.5263 0.4781 0.4860 -0.0073 -0.0208 0.0315  136 GLN   B N   
1939 C  CA  . GLN   B 43  ? 0.5417 0.5100 0.4892 -0.0099 -0.0193 0.0389  136 GLN   B CA  
1940 C  C   . GLN   B 43  ? 0.5327 0.4876 0.4802 -0.0137 -0.0127 0.0376  136 GLN   B C   
1941 O  O   . GLN   B 43  ? 0.5113 0.4421 0.4675 -0.0127 -0.0107 0.0379  136 GLN   B O   
1942 C  CB  . GLN   B 43  ? 0.5698 0.5415 0.5127 -0.0057 -0.0229 0.0606  136 GLN   B CB  
1943 C  CG  . GLN   B 43  ? 0.5852 0.5779 0.5263 -0.0012 -0.0300 0.0641  136 GLN   B CG  
1944 C  CD  . GLN   B 43  ? 0.6016 0.5905 0.5422 0.0051  -0.0338 0.0874  136 GLN   B CD  
1945 O  OE1 . GLN   B 43  ? 0.6123 0.5965 0.5611 0.0122  -0.0385 0.0920  136 GLN   B OE1 
1946 N  NE2 . GLN   B 43  ? 0.6128 0.6022 0.5456 0.0028  -0.0312 0.1025  136 GLN   B NE2 
1947 N  N   . LEU   B 44  ? 0.5424 0.5165 0.4805 -0.0178 -0.0095 0.0360  137 LEU   B N   
1948 C  CA  . LEU   B 44  ? 0.5377 0.5076 0.4751 -0.0218 -0.0030 0.0351  137 LEU   B CA  
1949 C  C   . LEU   B 44  ? 0.5382 0.4861 0.4798 -0.0220 -0.0017 0.0518  137 LEU   B C   
1950 O  O   . LEU   B 44  ? 0.5351 0.4846 0.4727 -0.0208 -0.0044 0.0695  137 LEU   B O   
1951 C  CB  . LEU   B 44  ? 0.5523 0.5538 0.4767 -0.0255 -0.0008 0.0363  137 LEU   B CB  
1952 C  CG  . LEU   B 44  ? 0.5491 0.5560 0.4727 -0.0298 0.0063  0.0309  137 LEU   B CG  
1953 C  CD1 . LEU   B 44  ? 0.5385 0.5386 0.4711 -0.0286 0.0085  0.0083  137 LEU   B CD1 
1954 C  CD2 . LEU   B 44  ? 0.5622 0.6042 0.4718 -0.0334 0.0087  0.0345  137 LEU   B CD2 
1955 N  N   . ALA   B 45  ? 0.5320 0.4609 0.4821 -0.0233 0.0019  0.0463  138 ALA   B N   
1956 C  CA  . ALA   B 45  ? 0.5474 0.4573 0.5027 -0.0255 0.0041  0.0579  138 ALA   B CA  
1957 C  C   . ALA   B 45  ? 0.5543 0.4430 0.5161 -0.0209 -0.0001 0.0672  138 ALA   B C   
1958 O  O   . ALA   B 45  ? 0.5852 0.4560 0.5531 -0.0226 0.0012  0.0749  138 ALA   B O   
1959 C  CB  . ALA   B 45  ? 0.5601 0.4842 0.5078 -0.0311 0.0073  0.0714  138 ALA   B CB  
1960 N  N   . LYS   B 46  ? 0.5469 0.4385 0.5089 -0.0153 -0.0050 0.0653  139 LYS   B N   
1961 C  CA  . LYS   B 46  ? 0.5404 0.4153 0.5096 -0.0093 -0.0091 0.0730  139 LYS   B CA  
1962 C  C   . LYS   B 46  ? 0.5117 0.3695 0.4908 -0.0071 -0.0085 0.0607  139 LYS   B C   
1963 O  O   . LYS   B 46  ? 0.4809 0.3426 0.4607 -0.0090 -0.0065 0.0471  139 LYS   B O   
1964 C  CB  . LYS   B 46  ? 0.5546 0.4451 0.5201 -0.0040 -0.0147 0.0777  139 LYS   B CB  
1965 C  CG  . LYS   B 46  ? 0.5826 0.4898 0.5385 -0.0044 -0.0166 0.0946  139 LYS   B CG  
1966 C  CD  . LYS   B 46  ? 0.6037 0.4940 0.5624 -0.0048 -0.0157 0.1136  139 LYS   B CD  
1967 C  CE  . LYS   B 46  ? 0.6294 0.5372 0.5789 -0.0039 -0.0185 0.1336  139 LYS   B CE  
1968 N  NZ  . LYS   B 46  ? 0.6388 0.5765 0.5742 -0.0106 -0.0155 0.1318  139 LYS   B NZ  
1969 N  N   . THR   B 47  ? 0.5067 0.3464 0.4939 -0.0029 -0.0101 0.0657  140 THR   B N   
1970 C  CA  . THR   B 47  ? 0.4935 0.3186 0.4896 -0.0003 -0.0096 0.0559  140 THR   B CA  
1971 C  C   . THR   B 47  ? 0.4794 0.3146 0.4767 0.0026  -0.0114 0.0461  140 THR   B C   
1972 O  O   . THR   B 47  ? 0.4787 0.3235 0.4760 0.0069  -0.0153 0.0494  140 THR   B O   
1973 C  CB  . THR   B 47  ? 0.5082 0.3158 0.5126 0.0048  -0.0115 0.0627  140 THR   B CB  
1974 O  OG1 . THR   B 47  ? 0.5237 0.3214 0.5281 0.0001  -0.0095 0.0723  140 THR   B OG1 
1975 C  CG2 . THR   B 47  ? 0.4982 0.2945 0.5109 0.0073  -0.0106 0.0518  140 THR   B CG2 
1976 N  N   A CYS   B 48  ? 0.4708 0.3042 0.4703 0.0001  -0.0088 0.0350  141 CYS   B N   
1977 N  N   B CYS   B 48  ? 0.4653 0.2987 0.4649 0.0001  -0.0088 0.0350  141 CYS   B N   
1978 C  CA  A CYS   B 48  ? 0.4618 0.3011 0.4648 0.0012  -0.0095 0.0260  141 CYS   B CA  
1979 C  CA  B CYS   B 48  ? 0.4530 0.2922 0.4561 0.0012  -0.0095 0.0260  141 CYS   B CA  
1980 C  C   A CYS   B 48  ? 0.4469 0.2748 0.4569 0.0033  -0.0081 0.0219  141 CYS   B C   
1981 C  C   B CYS   B 48  ? 0.4421 0.2699 0.4521 0.0033  -0.0081 0.0219  141 CYS   B C   
1982 O  O   A CYS   B 48  ? 0.4393 0.2625 0.4501 0.0006  -0.0053 0.0170  141 CYS   B O   
1983 O  O   B CYS   B 48  ? 0.4347 0.2580 0.4456 0.0006  -0.0053 0.0170  141 CYS   B O   
1984 C  CB  A CYS   B 48  ? 0.4707 0.3182 0.4709 -0.0035 -0.0075 0.0177  141 CYS   B CB  
1985 C  CB  B CYS   B 48  ? 0.4555 0.3025 0.4560 -0.0034 -0.0075 0.0176  141 CYS   B CB  
1986 S  SG  A CYS   B 48  ? 0.4881 0.3415 0.4945 -0.0041 -0.0085 0.0082  141 CYS   B SG  
1987 S  SG  B CYS   B 48  ? 0.4721 0.3381 0.4635 -0.0060 -0.0088 0.0189  141 CYS   B SG  
1988 N  N   . PRO   B 49  ? 0.4406 0.2661 0.4560 0.0088  -0.0101 0.0237  142 PRO   B N   
1989 C  CA  . PRO   B 49  ? 0.4328 0.2523 0.4540 0.0110  -0.0086 0.0185  142 PRO   B CA  
1990 C  C   . PRO   B 49  ? 0.4214 0.2491 0.4441 0.0084  -0.0071 0.0123  142 PRO   B C   
1991 O  O   . PRO   B 49  ? 0.4149 0.2533 0.4388 0.0078  -0.0086 0.0115  142 PRO   B O   
1992 C  CB  . PRO   B 49  ? 0.4416 0.2609 0.4687 0.0184  -0.0111 0.0211  142 PRO   B CB  
1993 C  CG  . PRO   B 49  ? 0.4575 0.2764 0.4816 0.0199  -0.0140 0.0308  142 PRO   B CG  
1994 C  CD  . PRO   B 49  ? 0.4529 0.2839 0.4694 0.0140  -0.0140 0.0307  142 PRO   B CD  
1995 N  N   . VAL   B 50  ? 0.4033 0.2264 0.4265 0.0064  -0.0044 0.0087  143 VAL   B N   
1996 C  CA  . VAL   B 50  ? 0.3981 0.2266 0.4241 0.0045  -0.0027 0.0055  143 VAL   B CA  
1997 C  C   . VAL   B 50  ? 0.3882 0.2164 0.4167 0.0075  -0.0013 0.0037  143 VAL   B C   
1998 O  O   . VAL   B 50  ? 0.3919 0.2134 0.4187 0.0079  -0.0006 0.0024  143 VAL   B O   
1999 C  CB  . VAL   B 50  ? 0.3983 0.2241 0.4227 0.0001  -0.0010 0.0041  143 VAL   B CB  
2000 C  CG1 . VAL   B 50  ? 0.3938 0.2219 0.4223 -0.0014 0.0008  0.0035  143 VAL   B CG1 
2001 C  CG2 . VAL   B 50  ? 0.4092 0.2384 0.4313 -0.0024 -0.0021 0.0030  143 VAL   B CG2 
2002 N  N   . GLN   B 51  ? 0.3848 0.2225 0.4174 0.0092  -0.0008 0.0028  144 GLN   B N   
2003 C  CA  . GLN   B 51  ? 0.3885 0.2313 0.4229 0.0122  0.0009  -0.0001 144 GLN   B CA  
2004 C  C   . GLN   B 51  ? 0.3810 0.2287 0.4142 0.0083  0.0034  0.0014  144 GLN   B C   
2005 O  O   . GLN   B 51  ? 0.3813 0.2316 0.4166 0.0042  0.0040  0.0046  144 GLN   B O   
2006 C  CB  . GLN   B 51  ? 0.3969 0.2512 0.4369 0.0165  0.0006  -0.0016 144 GLN   B CB  
2007 C  CG  . GLN   B 51  ? 0.4097 0.2593 0.4522 0.0219  -0.0024 -0.0012 144 GLN   B CG  
2008 C  CD  . GLN   B 51  ? 0.4175 0.2815 0.4669 0.0267  -0.0032 -0.0022 144 GLN   B CD  
2009 O  OE1 . GLN   B 51  ? 0.4358 0.3141 0.4880 0.0239  -0.0012 -0.0027 144 GLN   B OE1 
2010 N  NE2 . GLN   B 51  ? 0.4299 0.2908 0.4834 0.0340  -0.0060 -0.0017 144 GLN   B NE2 
2011 N  N   . LEU   B 52  ? 0.3811 0.2299 0.4118 0.0095  0.0046  -0.0007 145 LEU   B N   
2012 C  CA  . LEU   B 52  ? 0.3780 0.2356 0.4072 0.0076  0.0067  0.0022  145 LEU   B CA  
2013 C  C   . LEU   B 52  ? 0.3895 0.2634 0.4197 0.0103  0.0087  -0.0001 145 LEU   B C   
2014 O  O   . LEU   B 52  ? 0.4005 0.2767 0.4305 0.0147  0.0084  -0.0079 145 LEU   B O   
2015 C  CB  . LEU   B 52  ? 0.3722 0.2262 0.3974 0.0075  0.0062  0.0009  145 LEU   B CB  
2016 C  CG  . LEU   B 52  ? 0.3687 0.2093 0.3932 0.0058  0.0047  0.0011  145 LEU   B CG  
2017 C  CD1 . LEU   B 52  ? 0.3680 0.2102 0.3903 0.0055  0.0044  -0.0001 145 LEU   B CD1 
2018 C  CD2 . LEU   B 52  ? 0.3640 0.1996 0.3905 0.0029  0.0049  0.0058  145 LEU   B CD2 
2019 N  N   . TRP   B 53  ? 0.3880 0.2732 0.4204 0.0074  0.0109  0.0055  146 TRP   B N   
2020 C  CA  . TRP   B 53  ? 0.3923 0.2983 0.4254 0.0090  0.0138  0.0045  146 TRP   B CA  
2021 C  C   . TRP   B 53  ? 0.4020 0.3184 0.4308 0.0061  0.0160  0.0121  146 TRP   B C   
2022 O  O   . TRP   B 53  ? 0.4035 0.3129 0.4341 0.0014  0.0162  0.0217  146 TRP   B O   
2023 C  CB  . TRP   B 53  ? 0.3924 0.3075 0.4326 0.0073  0.0151  0.0064  146 TRP   B CB  
2024 C  CG  . TRP   B 53  ? 0.3983 0.3084 0.4427 0.0119  0.0125  0.0000  146 TRP   B CG  
2025 C  CD1 . TRP   B 53  ? 0.3929 0.2867 0.4376 0.0116  0.0091  0.0001  146 TRP   B CD1 
2026 C  CD2 . TRP   B 53  ? 0.4027 0.3258 0.4521 0.0184  0.0129  -0.0068 146 TRP   B CD2 
2027 N  NE1 . TRP   B 53  ? 0.4007 0.2961 0.4498 0.0172  0.0070  -0.0040 146 TRP   B NE1 
2028 C  CE2 . TRP   B 53  ? 0.4091 0.3211 0.4620 0.0220  0.0092  -0.0087 146 TRP   B CE2 
2029 C  CE3 . TRP   B 53  ? 0.4114 0.3564 0.4631 0.0219  0.0163  -0.0112 146 TRP   B CE3 
2030 C  CZ2 . TRP   B 53  ? 0.4178 0.3374 0.4776 0.0300  0.0081  -0.0141 146 TRP   B CZ2 
2031 C  CZ3 . TRP   B 53  ? 0.4160 0.3694 0.4748 0.0297  0.0158  -0.0187 146 TRP   B CZ3 
2032 C  CH2 . TRP   B 53  ? 0.4197 0.3595 0.4832 0.0340  0.0115  -0.0197 146 TRP   B CH2 
2033 N  N   . VAL   B 54  ? 0.4016 0.3348 0.4257 0.0092  0.0174  0.0077  147 VAL   B N   
2034 C  CA  . VAL   B 54  ? 0.4191 0.3692 0.4377 0.0074  0.0194  0.0159  147 VAL   B CA  
2035 C  C   . VAL   B 54  ? 0.4423 0.4205 0.4595 0.0090  0.0232  0.0129  147 VAL   B C   
2036 O  O   . VAL   B 54  ? 0.4335 0.4167 0.4527 0.0140  0.0234  -0.0006 147 VAL   B O   
2037 C  CB  . VAL   B 54  ? 0.4158 0.3639 0.4280 0.0095  0.0168  0.0127  147 VAL   B CB  
2038 C  CG1 . VAL   B 54  ? 0.4090 0.3349 0.4232 0.0076  0.0140  0.0184  147 VAL   B CG1 
2039 C  CG2 . VAL   B 54  ? 0.4119 0.3606 0.4229 0.0141  0.0153  -0.0038 147 VAL   B CG2 
2040 N  N   . ASP   B 55  ? 0.4621 0.4582 0.4771 0.0050  0.0264  0.0255  148 ASP   B N   
2041 C  CA  . ASP   B 55  ? 0.4852 0.5146 0.4970 0.0056  0.0310  0.0247  148 ASP   B CA  
2042 C  C   . ASP   B 55  ? 0.4932 0.5398 0.4950 0.0101  0.0301  0.0164  148 ASP   B C   
2043 O  O   . ASP   B 55  ? 0.4981 0.5697 0.4974 0.0137  0.0328  0.0056  148 ASP   B O   
2044 C  CB  . ASP   B 55  ? 0.5027 0.5450 0.5157 -0.0015 0.0349  0.0440  148 ASP   B CB  
2045 C  CG  . ASP   B 55  ? 0.5135 0.5444 0.5380 -0.0074 0.0362  0.0498  148 ASP   B CG  
2046 O  OD1 . ASP   B 55  ? 0.5012 0.5272 0.5316 -0.0047 0.0354  0.0379  148 ASP   B OD1 
2047 O  OD2 . ASP   B 55  ? 0.5484 0.5767 0.5768 -0.0149 0.0381  0.0665  148 ASP   B OD2 
2048 N  N   . SER   B 56  ? 0.5099 0.5457 0.5070 0.0101  0.0264  0.0204  149 SER   B N   
2049 C  CA  . SER   B 56  ? 0.5203 0.5733 0.5082 0.0133  0.0246  0.0129  149 SER   B CA  
2050 C  C   . SER   B 56  ? 0.5107 0.5393 0.4997 0.0144  0.0193  0.0073  149 SER   B C   
2051 O  O   . SER   B 56  ? 0.5042 0.5090 0.4979 0.0121  0.0177  0.0173  149 SER   B O   
2052 C  CB  . SER   B 56  ? 0.5339 0.6134 0.5137 0.0112  0.0261  0.0291  149 SER   B CB  
2053 O  OG  . SER   B 56  ? 0.5481 0.6106 0.5318 0.0072  0.0256  0.0497  149 SER   B OG  
2054 N  N   . THR   B 57  ? 0.5084 0.5445 0.4941 0.0174  0.0172  -0.0090 150 THR   B N   
2055 C  CA  . THR   B 57  ? 0.5046 0.5215 0.4922 0.0175  0.0126  -0.0169 150 THR   B CA  
2056 C  C   . THR   B 57  ? 0.5040 0.5237 0.4880 0.0161  0.0099  -0.0031 150 THR   B C   
2057 O  O   . THR   B 57  ? 0.5002 0.5467 0.4766 0.0169  0.0093  -0.0001 150 THR   B O   
2058 C  CB  . THR   B 57  ? 0.5157 0.5428 0.5023 0.0198  0.0114  -0.0387 150 THR   B CB  
2059 O  OG1 . THR   B 57  ? 0.5214 0.5428 0.5139 0.0226  0.0140  -0.0490 150 THR   B OG1 
2060 C  CG2 . THR   B 57  ? 0.5213 0.5294 0.5118 0.0182  0.0072  -0.0475 150 THR   B CG2 
2061 N  N   . PRO   B 58  ? 0.4850 0.4788 0.4745 0.0147  0.0081  0.0051  151 PRO   B N   
2062 C  CA  . PRO   B 58  ? 0.4830 0.4774 0.4716 0.0150  0.0052  0.0162  151 PRO   B CA  
2063 C  C   . PRO   B 58  ? 0.4769 0.4880 0.4614 0.0161  0.0015  0.0058  151 PRO   B C   
2064 O  O   . PRO   B 58  ? 0.4722 0.4848 0.4570 0.0154  0.0010  -0.0121 151 PRO   B O   
2065 C  CB  . PRO   B 58  ? 0.4721 0.4350 0.4688 0.0137  0.0043  0.0180  151 PRO   B CB  
2066 C  CG  . PRO   B 58  ? 0.4785 0.4282 0.4789 0.0121  0.0073  0.0165  151 PRO   B CG  
2067 C  CD  . PRO   B 58  ? 0.4772 0.4427 0.4743 0.0134  0.0088  0.0036  151 PRO   B CD  
2068 N  N   . PRO   B 59  ? 0.4795 0.5036 0.4617 0.0178  -0.0013 0.0165  152 PRO   B N   
2069 C  CA  . PRO   B 59  ? 0.4837 0.5294 0.4623 0.0185  -0.0054 0.0070  152 PRO   B CA  
2070 C  C   . PRO   B 59  ? 0.4778 0.5061 0.4633 0.0159  -0.0077 -0.0073 152 PRO   B C   
2071 O  O   . PRO   B 59  ? 0.4535 0.4535 0.4460 0.0147  -0.0066 -0.0052 152 PRO   B O   
2072 C  CB  . PRO   B 59  ? 0.4968 0.5560 0.4737 0.0220  -0.0081 0.0265  152 PRO   B CB  
2073 C  CG  . PRO   B 59  ? 0.4952 0.5259 0.4795 0.0226  -0.0060 0.0419  152 PRO   B CG  
2074 C  CD  . PRO   B 59  ? 0.4900 0.5086 0.4744 0.0194  -0.0012 0.0380  152 PRO   B CD  
2075 N  N   . PRO   B 60  ? 0.4809 0.5272 0.4652 0.0143  -0.0108 -0.0225 153 PRO   B N   
2076 C  CA  . PRO   B 60  ? 0.4832 0.5154 0.4754 0.0103  -0.0129 -0.0347 153 PRO   B CA  
2077 C  C   . PRO   B 60  ? 0.4775 0.4977 0.4754 0.0114  -0.0143 -0.0220 153 PRO   B C   
2078 O  O   . PRO   B 60  ? 0.5018 0.5364 0.4974 0.0160  -0.0161 -0.0076 153 PRO   B O   
2079 C  CB  . PRO   B 60  ? 0.4929 0.5550 0.4824 0.0084  -0.0167 -0.0497 153 PRO   B CB  
2080 C  CG  . PRO   B 60  ? 0.4995 0.5874 0.4790 0.0111  -0.0154 -0.0518 153 PRO   B CG  
2081 C  CD  . PRO   B 60  ? 0.4981 0.5812 0.4735 0.0153  -0.0125 -0.0292 153 PRO   B CD  
2082 N  N   . GLY   B 61  ? 0.4575 0.4531 0.4633 0.0079  -0.0134 -0.0269 154 GLY   B N   
2083 C  CA  . GLY   B 61  ? 0.4369 0.4221 0.4493 0.0086  -0.0141 -0.0187 154 GLY   B CA  
2084 C  C   . GLY   B 61  ? 0.4164 0.3810 0.4300 0.0119  -0.0112 -0.0050 154 GLY   B C   
2085 O  O   . GLY   B 61  ? 0.4086 0.3656 0.4280 0.0137  -0.0115 0.0010  154 GLY   B O   
2086 N  N   . THR   B 62  ? 0.4040 0.3622 0.4132 0.0127  -0.0086 -0.0014 155 THR   B N   
2087 C  CA  . THR   B 62  ? 0.3953 0.3325 0.4069 0.0138  -0.0057 0.0085  155 THR   B CA  
2088 C  C   . THR   B 62  ? 0.3855 0.3005 0.4026 0.0108  -0.0046 0.0031  155 THR   B C   
2089 O  O   . THR   B 62  ? 0.3664 0.2773 0.3841 0.0068  -0.0046 -0.0081 155 THR   B O   
2090 C  CB  . THR   B 62  ? 0.4003 0.3368 0.4076 0.0134  -0.0030 0.0096  155 THR   B CB  
2091 O  OG1 . THR   B 62  ? 0.4111 0.3710 0.4127 0.0159  -0.0035 0.0169  155 THR   B OG1 
2092 C  CG2 . THR   B 62  ? 0.3996 0.3167 0.4105 0.0131  -0.0004 0.0182  155 THR   B CG2 
2093 N  N   . ARG   B 63  ? 0.3767 0.2784 0.3982 0.0124  -0.0035 0.0108  156 ARG   B N   
2094 C  CA  . ARG   B 63  ? 0.3728 0.2578 0.3984 0.0099  -0.0022 0.0066  156 ARG   B CA  
2095 C  C   . ARG   B 63  ? 0.3686 0.2374 0.3952 0.0098  0.0000  0.0110  156 ARG   B C   
2096 O  O   . ARG   B 63  ? 0.3662 0.2355 0.3930 0.0120  0.0005  0.0193  156 ARG   B O   
2097 C  CB  . ARG   B 63  ? 0.3715 0.2620 0.4028 0.0118  -0.0034 0.0073  156 ARG   B CB  
2098 C  CG  . ARG   B 63  ? 0.3711 0.2739 0.4032 0.0082  -0.0051 -0.0013 156 ARG   B CG  
2099 C  CD  . ARG   B 63  ? 0.3707 0.2907 0.4078 0.0112  -0.0075 0.0000  156 ARG   B CD  
2100 N  NE  . ARG   B 63  ? 0.3680 0.2824 0.4119 0.0151  -0.0063 0.0042  156 ARG   B NE  
2101 C  CZ  . ARG   B 63  ? 0.3625 0.2767 0.4115 0.0125  -0.0049 -0.0009 156 ARG   B CZ  
2102 N  NH1 . ARG   B 63  ? 0.3588 0.2750 0.4075 0.0047  -0.0043 -0.0089 156 ARG   B NH1 
2103 N  NH2 . ARG   B 63  ? 0.3612 0.2729 0.4167 0.0176  -0.0036 0.0017  156 ARG   B NH2 
2104 N  N   . VAL   B 64  ? 0.3655 0.2219 0.3927 0.0068  0.0012  0.0062  157 VAL   B N   
2105 C  CA  . VAL   B 64  ? 0.3602 0.2038 0.3882 0.0059  0.0028  0.0080  157 VAL   B CA  
2106 C  C   . VAL   B 64  ? 0.3581 0.1952 0.3894 0.0054  0.0036  0.0060  157 VAL   B C   
2107 O  O   . VAL   B 64  ? 0.3455 0.1826 0.3758 0.0026  0.0039  0.0015  157 VAL   B O   
2108 C  CB  . VAL   B 64  ? 0.3576 0.1968 0.3824 0.0036  0.0032  0.0042  157 VAL   B CB  
2109 C  CG1 . VAL   B 64  ? 0.3596 0.1909 0.3854 0.0029  0.0041  0.0065  157 VAL   B CG1 
2110 C  CG2 . VAL   B 64  ? 0.3589 0.2078 0.3808 0.0046  0.0027  0.0027  157 VAL   B CG2 
2111 N  N   . ARG   B 65  ? 0.3485 0.1809 0.3845 0.0077  0.0043  0.0090  158 ARG   B N   
2112 C  CA  . ARG   B 65  ? 0.3480 0.1761 0.3881 0.0082  0.0055  0.0051  158 ARG   B CA  
2113 C  C   . ARG   B 65  ? 0.3527 0.1719 0.3924 0.0056  0.0064  0.0028  158 ARG   B C   
2114 O  O   . ARG   B 65  ? 0.3595 0.1744 0.4003 0.0049  0.0062  0.0064  158 ARG   B O   
2115 C  CB  . ARG   B 65  ? 0.3490 0.1780 0.3969 0.0137  0.0052  0.0082  158 ARG   B CB  
2116 C  CG  . ARG   B 65  ? 0.3460 0.1731 0.3997 0.0158  0.0067  0.0020  158 ARG   B CG  
2117 C  CD  . ARG   B 65  ? 0.3475 0.1749 0.4113 0.0231  0.0061  0.0054  158 ARG   B CD  
2118 N  NE  . ARG   B 65  ? 0.3462 0.1866 0.4097 0.0262  0.0040  0.0108  158 ARG   B NE  
2119 C  CZ  . ARG   B 65  ? 0.3363 0.1906 0.4011 0.0273  0.0036  0.0070  158 ARG   B CZ  
2120 N  NH1 . ARG   B 65  ? 0.3397 0.1969 0.4052 0.0252  0.0059  -0.0012 158 ARG   B NH1 
2121 N  NH2 . ARG   B 65  ? 0.3388 0.2069 0.4039 0.0299  0.0010  0.0115  158 ARG   B NH2 
2122 N  N   . ALA   B 66  ? 0.3568 0.1763 0.3949 0.0037  0.0074  -0.0027 159 ALA   B N   
2123 C  CA  . ALA   B 66  ? 0.3708 0.1866 0.4086 0.0015  0.0079  -0.0071 159 ALA   B CA  
2124 C  C   . ALA   B 66  ? 0.3806 0.1978 0.4236 0.0036  0.0095  -0.0138 159 ALA   B C   
2125 O  O   . ALA   B 66  ? 0.3862 0.2110 0.4292 0.0050  0.0106  -0.0155 159 ALA   B O   
2126 C  CB  . ALA   B 66  ? 0.3602 0.1793 0.3903 -0.0020 0.0075  -0.0075 159 ALA   B CB  
2127 N  N   . MET   B 67  ? 0.4049 0.2160 0.4532 0.0035  0.0098  -0.0186 160 MET   B N   
2128 C  CA  . MET   B 67  ? 0.4195 0.2309 0.4748 0.0062  0.0115  -0.0281 160 MET   B CA  
2129 C  C   . MET   B 67  ? 0.4186 0.2273 0.4752 0.0025  0.0113  -0.0364 160 MET   B C   
2130 O  O   . MET   B 67  ? 0.4122 0.2133 0.4710 -0.0004 0.0100  -0.0330 160 MET   B O   
2131 C  CB  . MET   B 67  ? 0.4455 0.2484 0.5127 0.0123  0.0116  -0.0257 160 MET   B CB  
2132 C  CG  . MET   B 67  ? 0.4720 0.2730 0.5492 0.0167  0.0133  -0.0368 160 MET   B CG  
2133 S  SD  . MET   B 67  ? 0.5245 0.3110 0.6186 0.0251  0.0127  -0.0315 160 MET   B SD  
2134 C  CE  . MET   B 67  ? 0.5147 0.3142 0.6057 0.0304  0.0117  -0.0212 160 MET   B CE  
2135 N  N   . ALA   B 68  ? 0.4164 0.2341 0.4715 0.0022  0.0128  -0.0474 161 ALA   B N   
2136 C  CA  . ALA   B 68  ? 0.4224 0.2419 0.4788 -0.0012 0.0124  -0.0586 161 ALA   B CA  
2137 C  C   . ALA   B 68  ? 0.4323 0.2423 0.5031 0.0023  0.0138  -0.0697 161 ALA   B C   
2138 O  O   . ALA   B 68  ? 0.4193 0.2302 0.4954 0.0085  0.0157  -0.0722 161 ALA   B O   
2139 C  CB  . ALA   B 68  ? 0.4223 0.2608 0.4675 -0.0037 0.0131  -0.0641 161 ALA   B CB  
2140 N  N   . ILE   B 69  ? 0.4543 0.2551 0.5328 -0.0014 0.0127  -0.0761 162 ILE   B N   
2141 C  CA  . ILE   B 69  ? 0.4794 0.2706 0.5729 0.0004  0.0139  -0.0911 162 ILE   B CA  
2142 C  C   . ILE   B 69  ? 0.4937 0.2935 0.5854 -0.0067 0.0127  -0.1052 162 ILE   B C   
2143 O  O   . ILE   B 69  ? 0.4840 0.2918 0.5662 -0.0126 0.0104  -0.0988 162 ILE   B O   
2144 C  CB  . ILE   B 69  ? 0.4916 0.2587 0.6009 0.0022  0.0135  -0.0834 162 ILE   B CB  
2145 C  CG1 . ILE   B 69  ? 0.4958 0.2554 0.6059 -0.0057 0.0116  -0.0746 162 ILE   B CG1 
2146 C  CG2 . ILE   B 69  ? 0.4832 0.2470 0.5931 0.0099  0.0140  -0.0695 162 ILE   B CG2 
2147 C  CD1 . ILE   B 69  ? 0.5070 0.2436 0.6339 -0.0057 0.0118  -0.0672 162 ILE   B CD1 
2148 N  N   . TYR   B 70  ? 0.5203 0.3207 0.6211 -0.0057 0.0140  -0.1247 163 TYR   B N   
2149 C  CA  . TYR   B 70  ? 0.5375 0.3455 0.6401 -0.0129 0.0125  -0.1417 163 TYR   B CA  
2150 C  C   . TYR   B 70  ? 0.5575 0.3440 0.6747 -0.0191 0.0107  -0.1387 163 TYR   B C   
2151 O  O   . TYR   B 70  ? 0.5590 0.3222 0.6898 -0.0156 0.0118  -0.1311 163 TYR   B O   
2152 C  CB  . TYR   B 70  ? 0.5546 0.3705 0.6637 -0.0094 0.0148  -0.1654 163 TYR   B CB  
2153 C  CG  . TYR   B 70  ? 0.5430 0.3877 0.6354 -0.0064 0.0167  -0.1688 163 TYR   B CG  
2154 C  CD1 . TYR   B 70  ? 0.5381 0.4077 0.6130 -0.0123 0.0148  -0.1675 163 TYR   B CD1 
2155 C  CD2 . TYR   B 70  ? 0.5433 0.3921 0.6380 0.0022  0.0204  -0.1715 163 TYR   B CD2 
2156 C  CE1 . TYR   B 70  ? 0.5349 0.4316 0.5944 -0.0105 0.0168  -0.1678 163 TYR   B CE1 
2157 C  CE2 . TYR   B 70  ? 0.5380 0.4152 0.6179 0.0035  0.0228  -0.1731 163 TYR   B CE2 
2158 C  CZ  . TYR   B 70  ? 0.5320 0.4325 0.5938 -0.0032 0.0211  -0.1704 163 TYR   B CZ  
2159 O  OH  . TYR   B 70  ? 0.5297 0.4589 0.5766 -0.0030 0.0236  -0.1694 163 TYR   B OH  
2160 N  N   . LYS   B 71  ? 0.5691 0.3654 0.6831 -0.0281 0.0080  -0.1428 164 LYS   B N   
2161 C  CA  . LYS   B 71  ? 0.5851 0.3661 0.7118 -0.0362 0.0064  -0.1385 164 LYS   B CA  
2162 C  C   . LYS   B 71  ? 0.6187 0.3828 0.7666 -0.0395 0.0072  -0.1574 164 LYS   B C   
2163 O  O   . LYS   B 71  ? 0.6319 0.3715 0.7963 -0.0423 0.0078  -0.1498 164 LYS   B O   
2164 C  CB  . LYS   B 71  ? 0.5795 0.3813 0.6962 -0.0442 0.0030  -0.1369 164 LYS   B CB  
2165 C  CG  . LYS   B 71  ? 0.5808 0.3719 0.7093 -0.0529 0.0018  -0.1296 164 LYS   B CG  
2166 C  CD  . LYS   B 71  ? 0.5729 0.3874 0.6936 -0.0597 -0.0017 -0.1297 164 LYS   B CD  
2167 C  CE  . LYS   B 71  ? 0.5773 0.3844 0.7080 -0.0670 -0.0020 -0.1177 164 LYS   B CE  
2168 N  NZ  . LYS   B 71  ? 0.5691 0.4017 0.6921 -0.0716 -0.0056 -0.1158 164 LYS   B NZ  
2169 N  N   . GLN   B 72  ? 0.6386 0.4161 0.7864 -0.0391 0.0073  -0.1808 165 GLN   B N   
2170 C  CA  . GLN   B 72  ? 0.6688 0.4332 0.8373 -0.0429 0.0077  -0.2048 165 GLN   B CA  
2171 C  C   . GLN   B 72  ? 0.6821 0.4182 0.8675 -0.0333 0.0110  -0.2049 165 GLN   B C   
2172 O  O   . GLN   B 72  ? 0.6641 0.4061 0.8409 -0.0224 0.0130  -0.1992 165 GLN   B O   
2173 C  CB  . GLN   B 72  ? 0.6818 0.4748 0.8421 -0.0442 0.0070  -0.2307 165 GLN   B CB  
2174 C  CG  . GLN   B 72  ? 0.6826 0.5045 0.8292 -0.0538 0.0028  -0.2325 165 GLN   B CG  
2175 C  CD  . GLN   B 72  ? 0.6833 0.5413 0.8129 -0.0518 0.0022  -0.2487 165 GLN   B CD  
2176 O  OE1 . GLN   B 72  ? 0.6906 0.5600 0.8066 -0.0432 0.0047  -0.2430 165 GLN   B OE1 
2177 N  NE2 . GLN   B 72  ? 0.6892 0.5682 0.8191 -0.0604 -0.0009 -0.2684 165 GLN   B NE2 
2178 N  N   . SER   B 73  ? 0.7062 0.4135 0.9161 -0.0373 0.0113  -0.2111 166 SER   B N   
2179 C  CA  . SER   B 73  ? 0.7235 0.3986 0.9536 -0.0281 0.0138  -0.2070 166 SER   B CA  
2180 C  C   . SER   B 73  ? 0.7388 0.4201 0.9725 -0.0167 0.0161  -0.2290 166 SER   B C   
2181 O  O   . SER   B 73  ? 0.7338 0.4015 0.9745 -0.0043 0.0180  -0.2205 166 SER   B O   
2182 C  CB  . SER   B 73  ? 0.7498 0.3929 1.0064 -0.0366 0.0135  -0.2093 166 SER   B CB  
2183 O  OG  . SER   B 73  ? 0.7591 0.4075 1.0252 -0.0459 0.0124  -0.2387 166 SER   B OG  
2184 N  N   . GLN   B 74  ? 0.7521 0.4563 0.9809 -0.0203 0.0159  -0.2563 167 GLN   B N   
2185 C  CA  . GLN   B 74  ? 0.7690 0.4834 1.0020 -0.0103 0.0187  -0.2818 167 GLN   B CA  
2186 C  C   . GLN   B 74  ? 0.7488 0.4928 0.9586 -0.0011 0.0206  -0.2729 167 GLN   B C   
2187 O  O   . GLN   B 74  ? 0.7711 0.5248 0.9844 0.0088  0.0237  -0.2893 167 GLN   B O   
2188 C  CB  . GLN   B 74  ? 0.7900 0.5210 1.0264 -0.0185 0.0178  -0.3155 167 GLN   B CB  
2189 C  CG  . GLN   B 74  ? 0.7755 0.5465 0.9857 -0.0275 0.0151  -0.3169 167 GLN   B CG  
2190 C  CD  . GLN   B 74  ? 0.7785 0.5459 0.9905 -0.0424 0.0110  -0.3106 167 GLN   B CD  
2191 O  OE1 . GLN   B 74  ? 0.7862 0.5254 1.0095 -0.0461 0.0104  -0.2909 167 GLN   B OE1 
2192 N  NE2 . GLN   B 74  ? 0.7754 0.5745 0.9763 -0.0512 0.0081  -0.3274 167 GLN   B NE2 
2193 N  N   . HIS   B 75  ? 0.7261 0.4841 0.9146 -0.0045 0.0190  -0.2486 168 HIS   B N   
2194 C  CA  . HIS   B 75  ? 0.7032 0.4885 0.8698 0.0017  0.0206  -0.2383 168 HIS   B CA  
2195 C  C   . HIS   B 75  ? 0.6781 0.4494 0.8424 0.0074  0.0207  -0.2091 168 HIS   B C   
2196 O  O   . HIS   B 75  ? 0.6691 0.4598 0.8178 0.0117  0.0220  -0.1991 168 HIS   B O   
2197 C  CB  . HIS   B 75  ? 0.6973 0.5147 0.8402 -0.0070 0.0185  -0.2370 168 HIS   B CB  
2198 C  CG  . HIS   B 75  ? 0.7164 0.5564 0.8577 -0.0121 0.0181  -0.2652 168 HIS   B CG  
2199 N  ND1 . HIS   B 75  ? 0.7285 0.5847 0.8723 -0.0055 0.0216  -0.2885 168 HIS   B ND1 
2200 C  CD2 . HIS   B 75  ? 0.7310 0.5839 0.8681 -0.0230 0.0145  -0.2748 168 HIS   B CD2 
2201 C  CE1 . HIS   B 75  ? 0.7432 0.6210 0.8838 -0.0123 0.0203  -0.3120 168 HIS   B CE1 
2202 N  NE2 . HIS   B 75  ? 0.7423 0.6188 0.8787 -0.0232 0.0155  -0.3038 168 HIS   B NE2 
2203 N  N   . MET   B 76  ? 0.6766 0.4170 0.8563 0.0069  0.0195  -0.1961 169 MET   B N   
2204 C  CA  . MET   B 76  ? 0.6548 0.3852 0.8295 0.0087  0.0184  -0.1667 169 MET   B CA  
2205 C  C   . MET   B 76  ? 0.6411 0.3722 0.8176 0.0218  0.0204  -0.1589 169 MET   B C   
2206 O  O   . MET   B 76  ? 0.6147 0.3529 0.7787 0.0233  0.0197  -0.1389 169 MET   B O   
2207 C  CB  . MET   B 76  ? 0.6685 0.3681 0.8602 0.0040  0.0170  -0.1559 169 MET   B CB  
2208 C  CG  . MET   B 76  ? 0.6581 0.3554 0.8402 0.0006  0.0155  -0.1285 169 MET   B CG  
2209 S  SD  . MET   B 76  ? 0.6726 0.3594 0.8610 -0.0149 0.0135  -0.1250 169 MET   B SD  
2210 C  CE  . MET   B 76  ? 0.7018 0.3526 0.9221 -0.0144 0.0146  -0.1340 169 MET   B CE  
2211 N  N   . THR   B 77  ? 0.6478 0.3731 0.8403 0.0312  0.0226  -0.1754 170 THR   B N   
2212 C  CA  . THR   B 77  ? 0.6381 0.3664 0.8361 0.0451  0.0244  -0.1710 170 THR   B CA  
2213 C  C   . THR   B 77  ? 0.6202 0.3840 0.8006 0.0471  0.0269  -0.1783 170 THR   B C   
2214 O  O   . THR   B 77  ? 0.6279 0.4001 0.8107 0.0570  0.0285  -0.1738 170 THR   B O   
2215 C  CB  . THR   B 77  ? 0.6600 0.3683 0.8846 0.0558  0.0259  -0.1867 170 THR   B CB  
2216 O  OG1 . THR   B 77  ? 0.6660 0.3909 0.8911 0.0551  0.0284  -0.2162 170 THR   B OG1 
2217 C  CG2 . THR   B 77  ? 0.6761 0.3472 0.9208 0.0528  0.0239  -0.1802 170 THR   B CG2 
2218 N  N   . GLU   B 78  ? 0.6173 0.4025 0.7817 0.0380  0.0273  -0.1889 171 GLU   B N   
2219 C  CA  . GLU   B 78  ? 0.6089 0.4295 0.7549 0.0378  0.0298  -0.1929 171 GLU   B CA  
2220 C  C   . GLU   B 78  ? 0.5745 0.4021 0.7030 0.0333  0.0282  -0.1677 171 GLU   B C   
2221 O  O   . GLU   B 78  ? 0.5644 0.3810 0.6868 0.0255  0.0249  -0.1553 171 GLU   B O   
2222 C  CB  . GLU   B 78  ? 0.6329 0.4745 0.7690 0.0300  0.0303  -0.2126 171 GLU   B CB  
2223 C  CG  . GLU   B 78  ? 0.6423 0.5216 0.7601 0.0296  0.0335  -0.2158 171 GLU   B CG  
2224 C  CD  . GLU   B 78  ? 0.6693 0.5749 0.7781 0.0242  0.0345  -0.2377 171 GLU   B CD  
2225 O  OE1 . GLU   B 78  ? 0.6984 0.5998 0.8216 0.0270  0.0355  -0.2622 171 GLU   B OE1 
2226 O  OE2 . GLU   B 78  ? 0.6867 0.6180 0.7747 0.0175  0.0342  -0.2305 171 GLU   B OE2 
2227 N  N   . VAL   B 79  ? 0.5514 0.3971 0.6735 0.0381  0.0305  -0.1612 172 VAL   B N   
2228 C  CA  . VAL   B 79  ? 0.5261 0.3797 0.6327 0.0337  0.0292  -0.1397 172 VAL   B CA  
2229 C  C   . VAL   B 79  ? 0.5142 0.3869 0.6015 0.0238  0.0291  -0.1399 172 VAL   B C   
2230 O  O   . VAL   B 79  ? 0.5105 0.4061 0.5924 0.0230  0.0319  -0.1545 172 VAL   B O   
2231 C  CB  . VAL   B 79  ? 0.5162 0.3852 0.6240 0.0403  0.0318  -0.1348 172 VAL   B CB  
2232 C  CG1 . VAL   B 79  ? 0.5031 0.3820 0.5954 0.0340  0.0309  -0.1164 172 VAL   B CG1 
2233 C  CG2 . VAL   B 79  ? 0.5268 0.3781 0.6535 0.0511  0.0309  -0.1313 172 VAL   B CG2 
2234 N  N   . VAL   B 80  ? 0.5061 0.3716 0.5833 0.0171  0.0259  -0.1238 173 VAL   B N   
2235 C  CA  . VAL   B 80  ? 0.5031 0.3853 0.5625 0.0089  0.0249  -0.1196 173 VAL   B CA  
2236 C  C   . VAL   B 80  ? 0.5042 0.4049 0.5530 0.0084  0.0273  -0.1099 173 VAL   B C   
2237 O  O   . VAL   B 80  ? 0.4814 0.3734 0.5315 0.0097  0.0267  -0.0960 173 VAL   B O   
2238 C  CB  . VAL   B 80  ? 0.4951 0.3625 0.5505 0.0033  0.0206  -0.1068 173 VAL   B CB  
2239 C  CG1 . VAL   B 80  ? 0.4932 0.3780 0.5319 -0.0031 0.0191  -0.1018 173 VAL   B CG1 
2240 C  CG2 . VAL   B 80  ? 0.5050 0.3544 0.5725 0.0020  0.0185  -0.1153 173 VAL   B CG2 
2241 N  N   . ARG   B 81  ? 0.5202 0.4470 0.5591 0.0058  0.0301  -0.1170 174 ARG   B N   
2242 C  CA  . ARG   B 81  ? 0.5319 0.4792 0.5606 0.0032  0.0331  -0.1073 174 ARG   B CA  
2243 C  C   . ARG   B 81  ? 0.5340 0.5031 0.5462 -0.0036 0.0332  -0.1055 174 ARG   B C   
2244 O  O   . ARG   B 81  ? 0.5275 0.5009 0.5370 -0.0050 0.0312  -0.1161 174 ARG   B O   
2245 C  CB  . ARG   B 81  ? 0.5520 0.5153 0.5890 0.0091  0.0383  -0.1180 174 ARG   B CB  
2246 C  CG  . ARG   B 81  ? 0.5759 0.5515 0.6185 0.0133  0.0407  -0.1414 174 ARG   B CG  
2247 C  CD  . ARG   B 81  ? 0.6003 0.5957 0.6514 0.0201  0.0464  -0.1527 174 ARG   B CD  
2248 N  NE  . ARG   B 81  ? 0.6044 0.5797 0.6755 0.0302  0.0458  -0.1574 174 ARG   B NE  
2249 C  CZ  . ARG   B 81  ? 0.6042 0.5728 0.6824 0.0339  0.0454  -0.1452 174 ARG   B CZ  
2250 N  NH1 . ARG   B 81  ? 0.5953 0.5748 0.6636 0.0276  0.0460  -0.1291 174 ARG   B NH1 
2251 N  NH2 . ARG   B 81  ? 0.6071 0.5592 0.7036 0.0442  0.0444  -0.1494 174 ARG   B NH2 
2252 N  N   . ARG   B 82  ? 0.5354 0.5189 0.5376 -0.0080 0.0352  -0.0919 175 ARG   B N   
2253 C  CA  . ARG   B 82  ? 0.5472 0.5552 0.5331 -0.0141 0.0359  -0.0867 175 ARG   B CA  
2254 C  C   . ARG   B 82  ? 0.5567 0.5951 0.5402 -0.0127 0.0403  -0.1051 175 ARG   B C   
2255 O  O   . ARG   B 82  ? 0.5604 0.6027 0.5550 -0.0071 0.0443  -0.1184 175 ARG   B O   
2256 C  CB  . ARG   B 82  ? 0.5500 0.5634 0.5290 -0.0194 0.0377  -0.0667 175 ARG   B CB  
2257 C  CG  . ARG   B 82  ? 0.5490 0.5342 0.5305 -0.0207 0.0334  -0.0509 175 ARG   B CG  
2258 C  CD  . ARG   B 82  ? 0.5559 0.5448 0.5334 -0.0265 0.0355  -0.0338 175 ARG   B CD  
2259 N  NE  . ARG   B 82  ? 0.5781 0.5756 0.5427 -0.0318 0.0342  -0.0200 175 ARG   B NE  
2260 C  CZ  . ARG   B 82  ? 0.5857 0.5885 0.5458 -0.0382 0.0362  -0.0035 175 ARG   B CZ  
2261 N  NH1 . ARG   B 82  ? 0.5724 0.5744 0.5400 -0.0412 0.0399  -0.0003 175 ARG   B NH1 
2262 N  NH2 . ARG   B 82  ? 0.5969 0.6064 0.5459 -0.0417 0.0344  0.0102  175 ARG   B NH2 
2263 N  N   . CYS   B 83  ? 0.5565 0.6179 0.5259 -0.0170 0.0396  -0.1058 176 CYS   B N   
2264 C  CA  . CYS   B 83  ? 0.5634 0.6618 0.5260 -0.0170 0.0441  -0.1219 176 CYS   B CA  
2265 C  C   . CYS   B 83  ? 0.5527 0.6741 0.5110 -0.0195 0.0507  -0.1126 176 CYS   B C   
2266 O  O   . CYS   B 83  ? 0.5376 0.6492 0.4939 -0.0236 0.0507  -0.0913 176 CYS   B O   
2267 C  CB  . CYS   B 83  ? 0.5744 0.6934 0.5211 -0.0217 0.0407  -0.1209 176 CYS   B CB  
2268 S  SG  . CYS   B 83  ? 0.5852 0.7133 0.5148 -0.0288 0.0390  -0.0895 176 CYS   B SG  
2269 N  N   . PRO   B 84  ? 0.5565 0.7101 0.5145 -0.0174 0.0569  -0.1292 177 PRO   B N   
2270 C  CA  . PRO   B 84  ? 0.5538 0.7358 0.5069 -0.0212 0.0638  -0.1201 177 PRO   B CA  
2271 C  C   . PRO   B 84  ? 0.5494 0.7390 0.4863 -0.0310 0.0629  -0.0921 177 PRO   B C   
2272 O  O   . PRO   B 84  ? 0.5430 0.7257 0.4829 -0.0352 0.0651  -0.0749 177 PRO   B O   
2273 C  CB  . PRO   B 84  ? 0.5715 0.7937 0.5207 -0.0185 0.0692  -0.1439 177 PRO   B CB  
2274 C  CG  . PRO   B 84  ? 0.5761 0.7785 0.5396 -0.0097 0.0662  -0.1699 177 PRO   B CG  
2275 C  CD  . PRO   B 84  ? 0.5685 0.7335 0.5322 -0.0116 0.0578  -0.1587 177 PRO   B CD  
2276 N  N   . HIS   B 85  ? 0.5498 0.7515 0.4716 -0.0341 0.0592  -0.0879 178 HIS   B N   
2277 C  CA  . HIS   B 85  ? 0.5555 0.7685 0.4614 -0.0422 0.0581  -0.0607 178 HIS   B CA  
2278 C  C   . HIS   B 85  ? 0.5498 0.7249 0.4622 -0.0448 0.0548  -0.0378 178 HIS   B C   
2279 O  O   . HIS   B 85  ? 0.5583 0.7391 0.4677 -0.0515 0.0583  -0.0179 178 HIS   B O   
2280 C  CB  . HIS   B 85  ? 0.5550 0.7824 0.4464 -0.0427 0.0525  -0.0613 178 HIS   B CB  
2281 C  CG  . HIS   B 85  ? 0.5561 0.7851 0.4346 -0.0485 0.0494  -0.0313 178 HIS   B CG  
2282 N  ND1 . HIS   B 85  ? 0.5677 0.8263 0.4340 -0.0553 0.0544  -0.0125 178 HIS   B ND1 
2283 C  CD2 . HIS   B 85  ? 0.5519 0.7568 0.4288 -0.0481 0.0418  -0.0160 178 HIS   B CD2 
2284 C  CE1 . HIS   B 85  ? 0.5729 0.8231 0.4312 -0.0586 0.0497  0.0138  178 HIS   B CE1 
2285 N  NE2 . HIS   B 85  ? 0.5634 0.7816 0.4281 -0.0536 0.0418  0.0112  178 HIS   B NE2 
2286 N  N   . HIS   B 86  ? 0.5531 0.6922 0.4743 -0.0403 0.0484  -0.0408 179 HIS   B N   
2287 C  CA  . HIS   B 86  ? 0.5616 0.6655 0.4884 -0.0419 0.0445  -0.0216 179 HIS   B CA  
2288 C  C   . HIS   B 86  ? 0.5738 0.6652 0.5138 -0.0425 0.0486  -0.0207 179 HIS   B C   
2289 O  O   . HIS   B 86  ? 0.5789 0.6560 0.5204 -0.0477 0.0484  -0.0019 179 HIS   B O   
2290 C  CB  . HIS   B 86  ? 0.5529 0.6287 0.4843 -0.0371 0.0371  -0.0261 179 HIS   B CB  
2291 C  CG  . HIS   B 86  ? 0.5629 0.6468 0.4820 -0.0384 0.0319  -0.0162 179 HIS   B CG  
2292 N  ND1 . HIS   B 86  ? 0.5585 0.6474 0.4755 -0.0353 0.0274  -0.0303 179 HIS   B ND1 
2293 C  CD2 . HIS   B 86  ? 0.5714 0.6601 0.4807 -0.0424 0.0303  0.0067  179 HIS   B CD2 
2294 C  CE1 . HIS   B 86  ? 0.5706 0.6701 0.4765 -0.0369 0.0229  -0.0165 179 HIS   B CE1 
2295 N  NE2 . HIS   B 86  ? 0.5711 0.6697 0.4719 -0.0406 0.0245  0.0070  179 HIS   B NE2 
2296 N  N   . GLU   B 87  ? 0.5849 0.6829 0.5347 -0.0374 0.0521  -0.0403 180 GLU   B N   
2297 C  CA  . GLU   B 87  ? 0.5940 0.6870 0.5571 -0.0369 0.0559  -0.0415 180 GLU   B CA  
2298 C  C   . GLU   B 87  ? 0.6134 0.7292 0.5719 -0.0461 0.0617  -0.0264 180 GLU   B C   
2299 O  O   . GLU   B 87  ? 0.6204 0.7225 0.5875 -0.0499 0.0622  -0.0163 180 GLU   B O   
2300 C  CB  . GLU   B 87  ? 0.5857 0.6874 0.5598 -0.0282 0.0586  -0.0657 180 GLU   B CB  
2301 C  CG  . GLU   B 87  ? 0.5820 0.6836 0.5707 -0.0258 0.0620  -0.0683 180 GLU   B CG  
2302 C  CD  . GLU   B 87  ? 0.5823 0.6923 0.5834 -0.0153 0.0644  -0.0918 180 GLU   B CD  
2303 O  OE1 . GLU   B 87  ? 0.5841 0.6911 0.5842 -0.0101 0.0625  -0.1068 180 GLU   B OE1 
2304 O  OE2 . GLU   B 87  ? 0.5801 0.7001 0.5930 -0.0123 0.0681  -0.0958 180 GLU   B OE2 
2305 N  N   . ARG   B 88  ? 0.6433 0.7930 0.5887 -0.0505 0.0657  -0.0238 181 ARG   B N   
2306 C  CA  . ARG   B 88  ? 0.6576 0.8343 0.5984 -0.0604 0.0725  -0.0087 181 ARG   B CA  
2307 C  C   . ARG   B 88  ? 0.6750 0.8398 0.6066 -0.0692 0.0698  0.0192  181 ARG   B C   
2308 O  O   . ARG   B 88  ? 0.6835 0.8606 0.6146 -0.0789 0.0747  0.0356  181 ARG   B O   
2309 C  CB  . ARG   B 88  ? 0.6775 0.9017 0.6080 -0.0612 0.0792  -0.0183 181 ARG   B CB  
2310 C  CG  . ARG   B 88  ? 0.6789 0.9178 0.6146 -0.0508 0.0808  -0.0488 181 ARG   B CG  
2311 C  CD  . ARG   B 88  ? 0.6676 0.8919 0.6235 -0.0428 0.0817  -0.0651 181 ARG   B CD  
2312 N  NE  . ARG   B 88  ? 0.6614 0.8848 0.6226 -0.0317 0.0802  -0.0919 181 ARG   B NE  
2313 C  CZ  . ARG   B 88  ? 0.6637 0.8797 0.6423 -0.0220 0.0812  -0.1103 181 ARG   B CZ  
2314 N  NH1 . ARG   B 88  ? 0.6661 0.8784 0.6500 -0.0128 0.0796  -0.1336 181 ARG   B NH1 
2315 N  NH2 . ARG   B 88  ? 0.6581 0.8704 0.6500 -0.0215 0.0835  -0.1056 181 ARG   B NH2 
2316 N  N   . CYS   B 89  ? 0.6822 0.8248 0.6078 -0.0660 0.0624  0.0248  182 CYS   B N   
2317 C  CA  . CYS   B 89  ? 0.7071 0.8395 0.6242 -0.0719 0.0592  0.0509  182 CYS   B CA  
2318 C  C   . CYS   B 89  ? 0.6993 0.7986 0.6288 -0.0767 0.0581  0.0648  182 CYS   B C   
2319 O  O   . CYS   B 89  ? 0.6942 0.7700 0.6364 -0.0723 0.0560  0.0531  182 CYS   B O   
2320 C  CB  . CYS   B 89  ? 0.7205 0.8422 0.6298 -0.0655 0.0514  0.0499  182 CYS   B CB  
2321 S  SG  . CYS   B 89  ? 0.7727 0.9411 0.6619 -0.0653 0.0522  0.0468  182 CYS   B SG  
2322 N  N   . SER   B 90  ? 0.7134 0.8105 0.6396 -0.0855 0.0591  0.0895  183 SER   B N   
2323 C  CA  . SER   B 90  ? 0.7070 0.7712 0.6450 -0.0914 0.0577  0.1045  183 SER   B CA  
2324 C  C   . SER   B 90  ? 0.6948 0.7225 0.6356 -0.0841 0.0492  0.1064  183 SER   B C   
2325 O  O   . SER   B 90  ? 0.7323 0.7435 0.6721 -0.0873 0.0466  0.1272  183 SER   B O   
2326 C  CB  . SER   B 90  ? 0.7268 0.8000 0.6612 -0.1031 0.0616  0.1308  183 SER   B CB  
2327 O  OG  . SER   B 90  ? 0.7368 0.8471 0.6689 -0.1109 0.0702  0.1302  183 SER   B OG  
2328 N  N   . ASP   B 91  ? 0.6536 0.6689 0.5986 -0.0748 0.0454  0.0866  184 ASP   B N   
2329 C  CA  . ASP   B 91  ? 0.6383 0.6202 0.5882 -0.0680 0.0382  0.0857  184 ASP   B CA  
2330 C  C   . ASP   B 91  ? 0.6010 0.5626 0.5652 -0.0666 0.0380  0.0730  184 ASP   B C   
2331 O  O   . ASP   B 91  ? 0.5882 0.5402 0.5552 -0.0587 0.0347  0.0586  184 ASP   B O   
2332 C  CB  . ASP   B 91  ? 0.6360 0.6238 0.5774 -0.0592 0.0334  0.0763  184 ASP   B CB  
2333 C  CG  . ASP   B 91  ? 0.6539 0.6263 0.5918 -0.0555 0.0269  0.0896  184 ASP   B CG  
2334 O  OD1 . ASP   B 91  ? 0.6662 0.6185 0.6092 -0.0585 0.0258  0.1064  184 ASP   B OD1 
2335 O  OD2 . ASP   B 91  ? 0.6318 0.6131 0.5631 -0.0495 0.0229  0.0826  184 ASP   B OD2 
2336 N  N   . SER   B 92  ? 0.5918 0.5490 0.5649 -0.0747 0.0415  0.0786  185 SER   B N   
2337 C  CA  . SER   B 92  ? 0.5683 0.5165 0.5546 -0.0749 0.0422  0.0664  185 SER   B CA  
2338 C  C   . SER   B 92  ? 0.5673 0.4868 0.5635 -0.0794 0.0396  0.0745  185 SER   B C   
2339 O  O   . SER   B 92  ? 0.5756 0.4907 0.5730 -0.0882 0.0413  0.0908  185 SER   B O   
2340 C  CB  . SER   B 92  ? 0.5626 0.5381 0.5525 -0.0806 0.0488  0.0616  185 SER   B CB  
2341 O  OG  . SER   B 92  ? 0.5517 0.5192 0.5550 -0.0873 0.0500  0.0615  185 SER   B OG  
2342 N  N   . ASP   B 93  ? 0.5475 0.4491 0.5511 -0.0739 0.0358  0.0632  186 ASP   B N   
2343 C  CA  . ASP   B 93  ? 0.5562 0.4313 0.5698 -0.0768 0.0329  0.0658  186 ASP   B CA  
2344 C  C   . ASP   B 93  ? 0.5494 0.4301 0.5748 -0.0837 0.0354  0.0586  186 ASP   B C   
2345 O  O   . ASP   B 93  ? 0.5681 0.4299 0.6028 -0.0862 0.0328  0.0563  186 ASP   B O   
2346 C  CB  . ASP   B 93  ? 0.5462 0.4023 0.5597 -0.0666 0.0272  0.0580  186 ASP   B CB  
2347 C  CG  . ASP   B 93  ? 0.5346 0.3975 0.5500 -0.0597 0.0263  0.0419  186 ASP   B CG  
2348 O  OD1 . ASP   B 93  ? 0.5251 0.4084 0.5413 -0.0607 0.0297  0.0357  186 ASP   B OD1 
2349 O  OD2 . ASP   B 93  ? 0.5307 0.3793 0.5476 -0.0532 0.0223  0.0362  186 ASP   B OD2 
2350 N  N   . GLY   B 94  ? 0.5357 0.4431 0.5615 -0.0862 0.0399  0.0536  187 GLY   B N   
2351 C  CA  . GLY   B 94  ? 0.5259 0.4454 0.5635 -0.0923 0.0423  0.0464  187 GLY   B CA  
2352 C  C   . GLY   B 94  ? 0.4993 0.4186 0.5418 -0.0833 0.0389  0.0307  187 GLY   B C   
2353 O  O   . GLY   B 94  ? 0.4905 0.4242 0.5427 -0.0865 0.0402  0.0239  187 GLY   B O   
2354 N  N   . LEU   B 95  ? 0.4840 0.3892 0.5209 -0.0725 0.0345  0.0259  188 LEU   B N   
2355 C  CA  . LEU   B 95  ? 0.4647 0.3675 0.5061 -0.0641 0.0309  0.0141  188 LEU   B CA  
2356 C  C   . LEU   B 95  ? 0.4569 0.3699 0.4935 -0.0537 0.0311  0.0073  188 LEU   B C   
2357 O  O   . LEU   B 95  ? 0.4632 0.3870 0.5061 -0.0485 0.0308  -0.0010 188 LEU   B O   
2358 C  CB  . LEU   B 95  ? 0.4572 0.3352 0.4982 -0.0614 0.0259  0.0142  188 LEU   B CB  
2359 C  CG  . LEU   B 95  ? 0.4670 0.3313 0.5150 -0.0709 0.0253  0.0181  188 LEU   B CG  
2360 C  CD1 . LEU   B 95  ? 0.4706 0.3119 0.5176 -0.0659 0.0208  0.0168  188 LEU   B CD1 
2361 C  CD2 . LEU   B 95  ? 0.4664 0.3429 0.5256 -0.0772 0.0257  0.0109  188 LEU   B CD2 
2362 N  N   . ALA   B 96  ? 0.4521 0.3622 0.4791 -0.0505 0.0314  0.0104  189 ALA   B N   
2363 C  CA  . ALA   B 96  ? 0.4394 0.3545 0.4629 -0.0410 0.0310  0.0023  189 ALA   B CA  
2364 C  C   . ALA   B 96  ? 0.4398 0.3805 0.4641 -0.0409 0.0360  -0.0030 189 ALA   B C   
2365 O  O   . ALA   B 96  ? 0.4421 0.3972 0.4629 -0.0483 0.0400  0.0028  189 ALA   B O   
2366 C  CB  . ALA   B 96  ? 0.4523 0.3564 0.4663 -0.0388 0.0287  0.0063  189 ALA   B CB  
2367 N  N   . PRO   B 97  ? 0.4265 0.3747 0.4564 -0.0323 0.0363  -0.0143 190 PRO   B N   
2368 C  CA  . PRO   B 97  ? 0.4258 0.3984 0.4569 -0.0302 0.0411  -0.0222 190 PRO   B CA  
2369 C  C   . PRO   B 97  ? 0.4367 0.4143 0.4557 -0.0316 0.0426  -0.0213 190 PRO   B C   
2370 O  O   . PRO   B 97  ? 0.4303 0.3912 0.4433 -0.0294 0.0387  -0.0197 190 PRO   B O   
2371 C  CB  . PRO   B 97  ? 0.4141 0.3846 0.4544 -0.0186 0.0396  -0.0340 190 PRO   B CB  
2372 C  CG  . PRO   B 97  ? 0.4119 0.3632 0.4569 -0.0169 0.0345  -0.0296 190 PRO   B CG  
2373 C  CD  . PRO   B 97  ? 0.4107 0.3451 0.4467 -0.0239 0.0321  -0.0196 190 PRO   B CD  
2374 N  N   . PRO   B 98  ? 0.4535 0.4577 0.4688 -0.0355 0.0481  -0.0225 191 PRO   B N   
2375 C  CA  . PRO   B 98  ? 0.4689 0.4838 0.4712 -0.0372 0.0493  -0.0214 191 PRO   B CA  
2376 C  C   . PRO   B 98  ? 0.4749 0.4860 0.4760 -0.0283 0.0471  -0.0357 191 PRO   B C   
2377 O  O   . PRO   B 98  ? 0.4791 0.4922 0.4696 -0.0297 0.0457  -0.0340 191 PRO   B O   
2378 C  CB  . PRO   B 98  ? 0.4758 0.5251 0.4761 -0.0426 0.0565  -0.0216 191 PRO   B CB  
2379 C  CG  . PRO   B 98  ? 0.4713 0.5292 0.4863 -0.0401 0.0591  -0.0290 191 PRO   B CG  
2380 C  CD  . PRO   B 98  ? 0.4581 0.4870 0.4811 -0.0385 0.0534  -0.0249 191 PRO   B CD  
2381 N  N   . GLN   B 99  ? 0.4748 0.4800 0.4876 -0.0197 0.0465  -0.0486 192 GLN   B N   
2382 C  CA  . GLN   B 99  ? 0.4774 0.4767 0.4933 -0.0114 0.0449  -0.0639 192 GLN   B CA  
2383 C  C   . GLN   B 99  ? 0.4644 0.4343 0.4796 -0.0100 0.0387  -0.0598 192 GLN   B C   
2384 O  O   . GLN   B 99  ? 0.4628 0.4280 0.4778 -0.0067 0.0370  -0.0698 192 GLN   B O   
2385 C  CB  . GLN   B 99  ? 0.4802 0.4816 0.5116 -0.0023 0.0465  -0.0765 192 GLN   B CB  
2386 C  CG  . GLN   B 99  ? 0.4988 0.5323 0.5336 -0.0016 0.0530  -0.0846 192 GLN   B CG  
2387 C  CD  . GLN   B 99  ? 0.5056 0.5404 0.5569 0.0102  0.0541  -0.1002 192 GLN   B CD  
2388 O  OE1 . GLN   B 99  ? 0.5103 0.5234 0.5721 0.0165  0.0501  -0.0985 192 GLN   B OE1 
2389 N  NE2 . GLN   B 99  ? 0.5191 0.5802 0.5730 0.0140  0.0594  -0.1152 192 GLN   B NE2 
2390 N  N   . HIS   B 100 ? 0.4489 0.4013 0.4648 -0.0126 0.0356  -0.0470 193 HIS   B N   
2391 C  CA  . HIS   B 100 ? 0.4371 0.3638 0.4548 -0.0103 0.0304  -0.0433 193 HIS   B CA  
2392 C  C   . HIS   B 100 ? 0.4362 0.3592 0.4432 -0.0140 0.0277  -0.0388 193 HIS   B C   
2393 O  O   . HIS   B 100 ? 0.4312 0.3601 0.4295 -0.0198 0.0280  -0.0279 193 HIS   B O   
2394 C  CB  . HIS   B 100 ? 0.4314 0.3457 0.4530 -0.0118 0.0284  -0.0332 193 HIS   B CB  
2395 C  CG  . HIS   B 100 ? 0.4243 0.3377 0.4579 -0.0056 0.0285  -0.0380 193 HIS   B CG  
2396 N  ND1 . HIS   B 100 ? 0.4159 0.3136 0.4546 -0.0025 0.0250  -0.0340 193 HIS   B ND1 
2397 C  CD2 . HIS   B 100 ? 0.4297 0.3582 0.4715 -0.0012 0.0317  -0.0461 193 HIS   B CD2 
2398 C  CE1 . HIS   B 100 ? 0.4134 0.3160 0.4624 0.0035  0.0254  -0.0381 193 HIS   B CE1 
2399 N  NE2 . HIS   B 100 ? 0.4219 0.3427 0.4739 0.0049  0.0294  -0.0459 193 HIS   B NE2 
2400 N  N   . LEU   B 101 ? 0.4244 0.3377 0.4334 -0.0108 0.0250  -0.0459 194 LEU   B N   
2401 C  CA  . LEU   B 101 ? 0.4214 0.3329 0.4220 -0.0136 0.0217  -0.0426 194 LEU   B CA  
2402 C  C   . LEU   B 101 ? 0.4140 0.3096 0.4130 -0.0153 0.0184  -0.0288 194 LEU   B C   
2403 O  O   . LEU   B 101 ? 0.4026 0.3025 0.3931 -0.0184 0.0168  -0.0204 194 LEU   B O   
2404 C  CB  . LEU   B 101 ? 0.4239 0.3293 0.4300 -0.0109 0.0197  -0.0549 194 LEU   B CB  
2405 C  CG  . LEU   B 101 ? 0.4240 0.3277 0.4243 -0.0137 0.0155  -0.0517 194 LEU   B CG  
2406 C  CD1 . LEU   B 101 ? 0.4321 0.3592 0.4199 -0.0171 0.0156  -0.0512 194 LEU   B CD1 
2407 C  CD2 . LEU   B 101 ? 0.4293 0.3223 0.4388 -0.0124 0.0135  -0.0627 194 LEU   B CD2 
2408 N  N   . ILE   B 102 ? 0.4095 0.2891 0.4164 -0.0127 0.0174  -0.0268 195 ILE   B N   
2409 C  CA  . ILE   B 102 ? 0.4088 0.2735 0.4155 -0.0131 0.0142  -0.0174 195 ILE   B CA  
2410 C  C   . ILE   B 102 ? 0.4061 0.2686 0.4136 -0.0153 0.0152  -0.0099 195 ILE   B C   
2411 O  O   . ILE   B 102 ? 0.4035 0.2675 0.4171 -0.0139 0.0169  -0.0129 195 ILE   B O   
2412 C  CB  . ILE   B 102 ? 0.4098 0.2611 0.4240 -0.0095 0.0122  -0.0203 195 ILE   B CB  
2413 C  CG1 . ILE   B 102 ? 0.4189 0.2710 0.4357 -0.0087 0.0116  -0.0295 195 ILE   B CG1 
2414 C  CG2 . ILE   B 102 ? 0.4054 0.2465 0.4184 -0.0099 0.0095  -0.0123 195 ILE   B CG2 
2415 C  CD1 . ILE   B 102 ? 0.4200 0.2586 0.4442 -0.0072 0.0098  -0.0293 195 ILE   B CD1 
2416 N  N   . ARG   B 103 ? 0.4173 0.2764 0.4199 -0.0185 0.0140  -0.0007 196 ARG   B N   
2417 C  CA  . ARG   B 103 ? 0.4217 0.2751 0.4267 -0.0218 0.0145  0.0057  196 ARG   B CA  
2418 C  C   . ARG   B 103 ? 0.4052 0.2432 0.4122 -0.0198 0.0112  0.0089  196 ARG   B C   
2419 O  O   . ARG   B 103 ? 0.3948 0.2294 0.3996 -0.0170 0.0088  0.0094  196 ARG   B O   
2420 C  CB  . ARG   B 103 ? 0.4482 0.3088 0.4483 -0.0276 0.0164  0.0143  196 ARG   B CB  
2421 C  CG  . ARG   B 103 ? 0.4656 0.3462 0.4627 -0.0297 0.0203  0.0108  196 ARG   B CG  
2422 C  CD  . ARG   B 103 ? 0.4933 0.3844 0.4887 -0.0370 0.0239  0.0189  196 ARG   B CD  
2423 N  NE  . ARG   B 103 ? 0.5267 0.4113 0.5181 -0.0416 0.0230  0.0331  196 ARG   B NE  
2424 C  CZ  . ARG   B 103 ? 0.5513 0.4502 0.5369 -0.0474 0.0260  0.0426  196 ARG   B CZ  
2425 N  NH1 . ARG   B 103 ? 0.5589 0.4493 0.5420 -0.0509 0.0247  0.0577  196 ARG   B NH1 
2426 N  NH2 . ARG   B 103 ? 0.5619 0.4846 0.5441 -0.0490 0.0302  0.0373  196 ARG   B NH2 
2427 N  N   . VAL   B 104 ? 0.4011 0.2326 0.4129 -0.0215 0.0111  0.0098  197 VAL   B N   
2428 C  CA  . VAL   B 104 ? 0.4042 0.2225 0.4180 -0.0204 0.0086  0.0123  197 VAL   B CA  
2429 C  C   . VAL   B 104 ? 0.4242 0.2368 0.4390 -0.0257 0.0092  0.0195  197 VAL   B C   
2430 O  O   . VAL   B 104 ? 0.4137 0.2320 0.4307 -0.0315 0.0118  0.0202  197 VAL   B O   
2431 C  CB  . VAL   B 104 ? 0.3977 0.2137 0.4165 -0.0182 0.0077  0.0063  197 VAL   B CB  
2432 C  CG1 . VAL   B 104 ? 0.4036 0.2088 0.4251 -0.0175 0.0058  0.0062  197 VAL   B CG1 
2433 C  CG2 . VAL   B 104 ? 0.3852 0.2045 0.4038 -0.0132 0.0071  0.0026  197 VAL   B CG2 
2434 N  N   . GLU   B 105 ? 0.4485 0.2508 0.4628 -0.0239 0.0071  0.0254  198 GLU   B N   
2435 C  CA  . GLU   B 105 ? 0.4746 0.2664 0.4919 -0.0282 0.0072  0.0341  198 GLU   B CA  
2436 C  C   . GLU   B 105 ? 0.4761 0.2527 0.5017 -0.0268 0.0055  0.0291  198 GLU   B C   
2437 O  O   . GLU   B 105 ? 0.4583 0.2341 0.4844 -0.0207 0.0037  0.0220  198 GLU   B O   
2438 C  CB  . GLU   B 105 ? 0.4953 0.2878 0.5070 -0.0260 0.0057  0.0452  198 GLU   B CB  
2439 C  CG  . GLU   B 105 ? 0.5073 0.2851 0.5232 -0.0203 0.0023  0.0493  198 GLU   B CG  
2440 C  CD  . GLU   B 105 ? 0.5239 0.3066 0.5343 -0.0166 -0.0001 0.0606  198 GLU   B CD  
2441 O  OE1 . GLU   B 105 ? 0.5546 0.3262 0.5683 -0.0165 -0.0012 0.0724  198 GLU   B OE1 
2442 O  OE2 . GLU   B 105 ? 0.5135 0.3113 0.5171 -0.0138 -0.0010 0.0577  198 GLU   B OE2 
2443 N  N   . GLY   B 106 ? 0.4977 0.2637 0.5301 -0.0328 0.0063  0.0321  199 GLY   B N   
2444 C  CA  . GLY   B 106 ? 0.5060 0.2560 0.5480 -0.0323 0.0048  0.0260  199 GLY   B CA  
2445 C  C   . GLY   B 106 ? 0.5039 0.2607 0.5486 -0.0325 0.0047  0.0118  199 GLY   B C   
2446 O  O   . GLY   B 106 ? 0.5134 0.2622 0.5634 -0.0289 0.0029  0.0034  199 GLY   B O   
2447 N  N   . ASN   B 107 ? 0.4879 0.2609 0.5297 -0.0357 0.0063  0.0087  200 ASN   B N   
2448 C  CA  . ASN   B 107 ? 0.4676 0.2502 0.5120 -0.0357 0.0057  -0.0028 200 ASN   B CA  
2449 C  C   . ASN   B 107 ? 0.4679 0.2627 0.5156 -0.0436 0.0077  -0.0040 200 ASN   B C   
2450 O  O   . ASN   B 107 ? 0.4428 0.2512 0.4863 -0.0430 0.0093  -0.0011 200 ASN   B O   
2451 C  CB  . ASN   B 107 ? 0.4632 0.2555 0.5012 -0.0276 0.0047  -0.0059 200 ASN   B CB  
2452 C  CG  . ASN   B 107 ? 0.4503 0.2513 0.4905 -0.0260 0.0033  -0.0158 200 ASN   B CG  
2453 O  OD1 . ASN   B 107 ? 0.4521 0.2593 0.4972 -0.0314 0.0032  -0.0213 200 ASN   B OD1 
2454 N  ND2 . ASN   B 107 ? 0.4462 0.2500 0.4827 -0.0191 0.0021  -0.0180 200 ASN   B ND2 
2455 N  N   . LEU   B 108 ? 0.4772 0.2686 0.5338 -0.0509 0.0075  -0.0095 201 LEU   B N   
2456 C  CA  . LEU   B 108 ? 0.4798 0.2845 0.5419 -0.0600 0.0094  -0.0108 201 LEU   B CA  
2457 C  C   . LEU   B 108 ? 0.4583 0.2845 0.5194 -0.0564 0.0082  -0.0189 201 LEU   B C   
2458 O  O   . LEU   B 108 ? 0.4630 0.3047 0.5287 -0.0619 0.0096  -0.0199 201 LEU   B O   
2459 C  CB  . LEU   B 108 ? 0.5050 0.2986 0.5789 -0.0702 0.0094  -0.0147 201 LEU   B CB  
2460 C  CG  . LEU   B 108 ? 0.5293 0.3087 0.6071 -0.0783 0.0121  -0.0022 201 LEU   B CG  
2461 C  CD1 . LEU   B 108 ? 0.5434 0.3040 0.6156 -0.0708 0.0113  0.0073  201 LEU   B CD1 
2462 C  CD2 . LEU   B 108 ? 0.5501 0.3181 0.6425 -0.0899 0.0122  -0.0071 201 LEU   B CD2 
2463 N  N   . ARG   B 109 ? 0.4564 0.2849 0.5124 -0.0474 0.0057  -0.0233 202 ARG   B N   
2464 C  CA  A ARG   B 109 ? 0.4525 0.3010 0.5075 -0.0428 0.0040  -0.0285 202 ARG   B CA  
2465 C  CA  B ARG   B 109 ? 0.4412 0.2897 0.4962 -0.0428 0.0040  -0.0285 202 ARG   B CA  
2466 C  C   . ARG   B 109 ? 0.4318 0.2858 0.4805 -0.0352 0.0050  -0.0218 202 ARG   B C   
2467 O  O   . ARG   B 109 ? 0.4377 0.3056 0.4861 -0.0299 0.0036  -0.0234 202 ARG   B O   
2468 C  CB  A ARG   B 109 ? 0.4676 0.3174 0.5211 -0.0384 0.0009  -0.0365 202 ARG   B CB  
2469 C  CB  B ARG   B 109 ? 0.4404 0.2903 0.4939 -0.0385 0.0009  -0.0365 202 ARG   B CB  
2470 C  CG  A ARG   B 109 ? 0.4929 0.3389 0.5539 -0.0454 -0.0004 -0.0471 202 ARG   B CG  
2471 C  CG  B ARG   B 109 ? 0.4496 0.2958 0.5108 -0.0456 -0.0003 -0.0471 202 ARG   B CG  
2472 C  CD  A ARG   B 109 ? 0.5073 0.3570 0.5655 -0.0400 -0.0029 -0.0562 202 ARG   B CD  
2473 C  CD  B ARG   B 109 ? 0.4474 0.3012 0.5059 -0.0406 -0.0031 -0.0567 202 ARG   B CD  
2474 N  NE  A ARG   B 109 ? 0.5102 0.3841 0.5640 -0.0354 -0.0050 -0.0579 202 ARG   B NE  
2475 N  NE  B ARG   B 109 ? 0.4370 0.2795 0.4892 -0.0328 -0.0026 -0.0532 202 ARG   B NE  
2476 C  CZ  A ARG   B 109 ? 0.5148 0.3994 0.5635 -0.0297 -0.0068 -0.0629 202 ARG   B CZ  
2477 C  CZ  B ARG   B 109 ? 0.4348 0.2856 0.4828 -0.0270 -0.0040 -0.0591 202 ARG   B CZ  
2478 N  NH1 A ARG   B 109 ? 0.5230 0.3967 0.5709 -0.0278 -0.0065 -0.0689 202 ARG   B NH1 
2479 N  NH1 B ARG   B 109 ? 0.4388 0.3098 0.4871 -0.0280 -0.0063 -0.0684 202 ARG   B NH1 
2480 N  NH2 A ARG   B 109 ? 0.5107 0.4182 0.5554 -0.0255 -0.0088 -0.0611 202 ARG   B NH2 
2481 N  NH2 B ARG   B 109 ? 0.4297 0.2720 0.4733 -0.0206 -0.0032 -0.0555 202 ARG   B NH2 
2482 N  N   . VAL   B 110 ? 0.4177 0.2618 0.4625 -0.0348 0.0072  -0.0148 203 VAL   B N   
2483 C  CA  . VAL   B 110 ? 0.3983 0.2468 0.4385 -0.0290 0.0086  -0.0106 203 VAL   B CA  
2484 C  C   . VAL   B 110 ? 0.3871 0.2537 0.4320 -0.0288 0.0098  -0.0125 203 VAL   B C   
2485 O  O   . VAL   B 110 ? 0.3827 0.2579 0.4329 -0.0358 0.0112  -0.0138 203 VAL   B O   
2486 C  CB  . VAL   B 110 ? 0.4021 0.2414 0.4376 -0.0304 0.0105  -0.0042 203 VAL   B CB  
2487 C  CG1 . VAL   B 110 ? 0.4109 0.2533 0.4488 -0.0389 0.0134  -0.0004 203 VAL   B CG1 
2488 C  CG2 . VAL   B 110 ? 0.4009 0.2443 0.4322 -0.0246 0.0114  -0.0031 203 VAL   B CG2 
2489 N  N   . GLU   B 111 ? 0.3784 0.2504 0.4226 -0.0210 0.0095  -0.0124 204 GLU   B N   
2490 C  CA  . GLU   B 111 ? 0.3808 0.2696 0.4309 -0.0177 0.0105  -0.0144 204 GLU   B CA  
2491 C  C   . GLU   B 111 ? 0.3787 0.2645 0.4270 -0.0118 0.0124  -0.0136 204 GLU   B C   
2492 O  O   . GLU   B 111 ? 0.3779 0.2510 0.4218 -0.0082 0.0113  -0.0117 204 GLU   B O   
2493 C  CB  . GLU   B 111 ? 0.3921 0.2904 0.4460 -0.0129 0.0069  -0.0160 204 GLU   B CB  
2494 C  CG  . GLU   B 111 ? 0.4028 0.3148 0.4631 -0.0048 0.0066  -0.0160 204 GLU   B CG  
2495 C  CD  . GLU   B 111 ? 0.4032 0.3245 0.4657 0.0011  0.0024  -0.0143 204 GLU   B CD  
2496 O  OE1 . GLU   B 111 ? 0.3973 0.3261 0.4590 -0.0033 0.0000  -0.0169 204 GLU   B OE1 
2497 O  OE2 . GLU   B 111 ? 0.4004 0.3221 0.4659 0.0103  0.0014  -0.0103 204 GLU   B OE2 
2498 N  N   . TYR   B 112 ? 0.3745 0.2729 0.4268 -0.0114 0.0154  -0.0162 205 TYR   B N   
2499 C  CA  . TYR   B 112 ? 0.3787 0.2766 0.4306 -0.0062 0.0177  -0.0188 205 TYR   B CA  
2500 C  C   . TYR   B 112 ? 0.3805 0.2896 0.4422 0.0024  0.0177  -0.0229 205 TYR   B C   
2501 O  O   . TYR   B 112 ? 0.3946 0.3201 0.4632 0.0022  0.0177  -0.0241 205 TYR   B O   
2502 C  CB  . TYR   B 112 ? 0.3791 0.2838 0.4264 -0.0126 0.0218  -0.0192 205 TYR   B CB  
2503 C  CG  . TYR   B 112 ? 0.3818 0.2737 0.4200 -0.0187 0.0212  -0.0135 205 TYR   B CG  
2504 C  CD1 . TYR   B 112 ? 0.3873 0.2756 0.4247 -0.0265 0.0208  -0.0084 205 TYR   B CD1 
2505 C  CD2 . TYR   B 112 ? 0.3780 0.2612 0.4098 -0.0164 0.0208  -0.0134 205 TYR   B CD2 
2506 C  CE1 . TYR   B 112 ? 0.3881 0.2632 0.4190 -0.0304 0.0200  -0.0023 205 TYR   B CE1 
2507 C  CE2 . TYR   B 112 ? 0.3841 0.2577 0.4085 -0.0206 0.0198  -0.0074 205 TYR   B CE2 
2508 C  CZ  . TYR   B 112 ? 0.3871 0.2558 0.4112 -0.0269 0.0194  -0.0012 205 TYR   B CZ  
2509 O  OH  . TYR   B 112 ? 0.3841 0.2422 0.4025 -0.0293 0.0181  0.0053  205 TYR   B OH  
2510 N  N   . LEU   B 113 ? 0.3855 0.2860 0.4496 0.0101  0.0174  -0.0250 206 LEU   B N   
2511 C  CA  . LEU   B 113 ? 0.3848 0.2913 0.4604 0.0203  0.0170  -0.0280 206 LEU   B CA  
2512 C  C   . LEU   B 113 ? 0.3981 0.3045 0.4771 0.0244  0.0204  -0.0367 206 LEU   B C   
2513 O  O   . LEU   B 113 ? 0.3988 0.2919 0.4721 0.0224  0.0207  -0.0384 206 LEU   B O   
2514 C  CB  . LEU   B 113 ? 0.3889 0.2822 0.4666 0.0261  0.0129  -0.0214 206 LEU   B CB  
2515 C  CG  . LEU   B 113 ? 0.3947 0.2882 0.4851 0.0379  0.0119  -0.0215 206 LEU   B CG  
2516 C  CD1 . LEU   B 113 ? 0.3953 0.3114 0.4944 0.0423  0.0114  -0.0227 206 LEU   B CD1 
2517 C  CD2 . LEU   B 113 ? 0.3974 0.2770 0.4885 0.0419  0.0083  -0.0118 206 LEU   B CD2 
2518 N  N   . ASP   B 114 ? 0.4125 0.3364 0.5007 0.0294  0.0229  -0.0433 207 ASP   B N   
2519 C  CA  . ASP   B 114 ? 0.4408 0.3656 0.5380 0.0380  0.0254  -0.0538 207 ASP   B CA  
2520 C  C   . ASP   B 114 ? 0.4615 0.3804 0.5726 0.0501  0.0222  -0.0511 207 ASP   B C   
2521 O  O   . ASP   B 114 ? 0.4673 0.4033 0.5858 0.0542  0.0213  -0.0490 207 ASP   B O   
2522 C  CB  . ASP   B 114 ? 0.4429 0.3933 0.5430 0.0376  0.0306  -0.0634 207 ASP   B CB  
2523 C  CG  . ASP   B 114 ? 0.4394 0.3988 0.5259 0.0257  0.0340  -0.0635 207 ASP   B CG  
2524 O  OD1 . ASP   B 114 ? 0.4424 0.3862 0.5179 0.0196  0.0324  -0.0585 207 ASP   B OD1 
2525 O  OD2 . ASP   B 114 ? 0.4533 0.4369 0.5407 0.0228  0.0384  -0.0672 207 ASP   B OD2 
2526 N  N   . ASP   B 115 ? 0.4895 0.3855 0.6038 0.0546  0.0201  -0.0492 208 ASP   B N   
2527 C  CA  . ASP   B 115 ? 0.5102 0.3964 0.6374 0.0656  0.0166  -0.0424 208 ASP   B CA  
2528 C  C   . ASP   B 115 ? 0.5238 0.4222 0.6674 0.0775  0.0185  -0.0517 208 ASP   B C   
2529 O  O   . ASP   B 115 ? 0.5308 0.4289 0.6783 0.0792  0.0223  -0.0656 208 ASP   B O   
2530 C  CB  . ASP   B 115 ? 0.5252 0.3837 0.6535 0.0659  0.0151  -0.0386 208 ASP   B CB  
2531 C  CG  . ASP   B 115 ? 0.5410 0.3879 0.6814 0.0758  0.0115  -0.0274 208 ASP   B CG  
2532 O  OD1 . ASP   B 115 ? 0.5544 0.4017 0.7107 0.0874  0.0116  -0.0312 208 ASP   B OD1 
2533 O  OD2 . ASP   B 115 ? 0.5488 0.3875 0.6828 0.0722  0.0086  -0.0143 208 ASP   B OD2 
2534 N  N   . ARG   B 116 ? 0.5352 0.4469 0.6880 0.0856  0.0158  -0.0451 209 ARG   B N   
2535 C  CA  . ARG   B 116 ? 0.5543 0.4824 0.7247 0.0986  0.0170  -0.0526 209 ARG   B CA  
2536 C  C   . ARG   B 116 ? 0.5693 0.4763 0.7548 0.1100  0.0179  -0.0600 209 ARG   B C   
2537 O  O   . ARG   B 116 ? 0.5729 0.4925 0.7706 0.1183  0.0213  -0.0739 209 ARG   B O   
2538 C  CB  . ARG   B 116 ? 0.5641 0.5086 0.7420 0.1060  0.0122  -0.0413 209 ARG   B CB  
2539 C  CG  . ARG   B 116 ? 0.5853 0.5125 0.7613 0.1084  0.0065  -0.0241 209 ARG   B CG  
2540 C  CD  . ARG   B 116 ? 0.5867 0.5369 0.7643 0.1118  0.0015  -0.0131 209 ARG   B CD  
2541 N  NE  . ARG   B 116 ? 0.6013 0.5732 0.7968 0.1256  0.0006  -0.0163 209 ARG   B NE  
2542 C  CZ  . ARG   B 116 ? 0.6037 0.6074 0.8023 0.1270  -0.0022 -0.0138 209 ARG   B CZ  
2543 N  NH1 . ARG   B 116 ? 0.5990 0.6147 0.7837 0.1148  -0.0044 -0.0091 209 ARG   B NH1 
2544 N  NH2 . ARG   B 116 ? 0.6119 0.6360 0.8287 0.1408  -0.0029 -0.0172 209 ARG   B NH2 
2545 N  N   . ASN   B 117 ? 0.5721 0.4492 0.7580 0.1099  0.0154  -0.0523 210 ASN   B N   
2546 C  CA  . ASN   B 117 ? 0.5909 0.4441 0.7952 0.1211  0.0154  -0.0570 210 ASN   B CA  
2547 C  C   . ASN   B 117 ? 0.5916 0.4242 0.7915 0.1128  0.0183  -0.0688 210 ASN   B C   
2548 O  O   . ASN   B 117 ? 0.6001 0.4239 0.8146 0.1202  0.0208  -0.0842 210 ASN   B O   
2549 C  CB  . ASN   B 117 ? 0.6056 0.4404 0.8187 0.1286  0.0102  -0.0375 210 ASN   B CB  
2550 C  CG  . ASN   B 117 ? 0.6034 0.4606 0.8164 0.1342  0.0060  -0.0229 210 ASN   B CG  
2551 O  OD1 . ASN   B 117 ? 0.6068 0.4575 0.8152 0.1332  0.0018  -0.0047 210 ASN   B OD1 
2552 N  ND2 . ASN   B 117 ? 0.6059 0.4918 0.8245 0.1401  0.0070  -0.0307 210 ASN   B ND2 
2553 N  N   . THR   B 118 ? 0.5720 0.3976 0.7541 0.0988  0.0178  -0.0631 211 THR   B N   
2554 C  CA  . THR   B 118 ? 0.5738 0.3828 0.7514 0.0901  0.0198  -0.0735 211 THR   B CA  
2555 C  C   . THR   B 118 ? 0.5577 0.3884 0.7227 0.0826  0.0238  -0.0887 211 THR   B C   
2556 O  O   . THR   B 118 ? 0.5693 0.3932 0.7327 0.0779  0.0257  -0.1019 211 THR   B O   
2557 C  CB  . THR   B 118 ? 0.5710 0.3637 0.7374 0.0797  0.0171  -0.0594 211 THR   B CB  
2558 O  OG1 . THR   B 118 ? 0.5528 0.3634 0.7007 0.0712  0.0166  -0.0518 211 THR   B OG1 
2559 C  CG2 . THR   B 118 ? 0.5840 0.3577 0.7611 0.0855  0.0136  -0.0421 211 THR   B CG2 
2560 N  N   . PHE   B 119 ? 0.5349 0.3914 0.6905 0.0802  0.0248  -0.0856 212 PHE   B N   
2561 C  CA  . PHE   B 119 ? 0.5136 0.3934 0.6558 0.0719  0.0288  -0.0952 212 PHE   B CA  
2562 C  C   . PHE   B 119 ? 0.4848 0.3568 0.6094 0.0586  0.0279  -0.0906 212 PHE   B C   
2563 O  O   . PHE   B 119 ? 0.4724 0.3606 0.5851 0.0512  0.0308  -0.0969 212 PHE   B O   
2564 C  CB  . PHE   B 119 ? 0.5330 0.4231 0.6839 0.0775  0.0333  -0.1165 212 PHE   B CB  
2565 C  CG  . PHE   B 119 ? 0.5568 0.4532 0.7282 0.0927  0.0343  -0.1232 212 PHE   B CG  
2566 C  CD1 . PHE   B 119 ? 0.5563 0.4794 0.7301 0.0965  0.0355  -0.1200 212 PHE   B CD1 
2567 C  CD2 . PHE   B 119 ? 0.5818 0.4576 0.7719 0.1033  0.0339  -0.1330 212 PHE   B CD2 
2568 C  CE1 . PHE   B 119 ? 0.5678 0.4994 0.7617 0.1117  0.0361  -0.1261 212 PHE   B CE1 
2569 C  CE2 . PHE   B 119 ? 0.5994 0.4804 0.8101 0.1190  0.0346  -0.1389 212 PHE   B CE2 
2570 C  CZ  . PHE   B 119 ? 0.5916 0.5018 0.8040 0.1237  0.0356  -0.1354 212 PHE   B CZ  
2571 N  N   . ARG   B 120 ? 0.4701 0.3202 0.5931 0.0559  0.0242  -0.0790 213 ARG   B N   
2572 C  CA  . ARG   B 120 ? 0.4485 0.2916 0.5567 0.0446  0.0229  -0.0739 213 ARG   B CA  
2573 C  C   . ARG   B 120 ? 0.4225 0.2793 0.5171 0.0381  0.0223  -0.0632 213 ARG   B C   
2574 O  O   . ARG   B 120 ? 0.4140 0.2784 0.5122 0.0418  0.0213  -0.0559 213 ARG   B O   
2575 C  CB  . ARG   B 120 ? 0.4597 0.2779 0.5728 0.0442  0.0197  -0.0656 213 ARG   B CB  
2576 C  CG  . ARG   B 120 ? 0.4799 0.2816 0.6075 0.0482  0.0204  -0.0773 213 ARG   B CG  
2577 C  CD  . ARG   B 120 ? 0.4892 0.2679 0.6200 0.0435  0.0180  -0.0697 213 ARG   B CD  
2578 N  NE  . ARG   B 120 ? 0.5119 0.2740 0.6584 0.0458  0.0189  -0.0829 213 ARG   B NE  
2579 C  CZ  . ARG   B 120 ? 0.5159 0.2787 0.6612 0.0396  0.0200  -0.0989 213 ARG   B CZ  
2580 N  NH1 . ARG   B 120 ? 0.5004 0.2809 0.6284 0.0315  0.0202  -0.1022 213 ARG   B NH1 
2581 N  NH2 . ARG   B 120 ? 0.5306 0.2769 0.6928 0.0420  0.0206  -0.1123 213 ARG   B NH2 
2582 N  N   . HIS   B 121 ? 0.4106 0.2712 0.4915 0.0289  0.0228  -0.0628 214 HIS   B N   
2583 C  CA  . HIS   B 121 ? 0.3978 0.2676 0.4665 0.0216  0.0224  -0.0533 214 HIS   B CA  
2584 C  C   . HIS   B 121 ? 0.3834 0.2378 0.4470 0.0181  0.0188  -0.0423 214 HIS   B C   
2585 O  O   . HIS   B 121 ? 0.3853 0.2265 0.4490 0.0170  0.0175  -0.0431 214 HIS   B O   
2586 C  CB  . HIS   B 121 ? 0.4000 0.2832 0.4577 0.0147  0.0249  -0.0578 214 HIS   B CB  
2587 C  CG  . HIS   B 121 ? 0.4148 0.3176 0.4757 0.0173  0.0292  -0.0693 214 HIS   B CG  
2588 N  ND1 . HIS   B 121 ? 0.4218 0.3395 0.4737 0.0127  0.0319  -0.0759 214 HIS   B ND1 
2589 C  CD2 . HIS   B 121 ? 0.4231 0.3370 0.4950 0.0243  0.0315  -0.0752 214 HIS   B CD2 
2590 C  CE1 . HIS   B 121 ? 0.4279 0.3654 0.4845 0.0161  0.0361  -0.0860 214 HIS   B CE1 
2591 N  NE2 . HIS   B 121 ? 0.4286 0.3633 0.4984 0.0237  0.0359  -0.0862 214 HIS   B NE2 
2592 N  N   . SER   B 122 ? 0.3692 0.2270 0.4284 0.0154  0.0174  -0.0334 215 SER   B N   
2593 C  CA  . SER   B 122 ? 0.3582 0.2054 0.4115 0.0118  0.0146  -0.0248 215 SER   B CA  
2594 C  C   . SER   B 122 ? 0.3542 0.2089 0.4012 0.0067  0.0143  -0.0199 215 SER   B C   
2595 O  O   . SER   B 122 ? 0.3505 0.2184 0.4000 0.0061  0.0158  -0.0216 215 SER   B O   
2596 C  CB  . SER   B 122 ? 0.3519 0.1894 0.4120 0.0170  0.0123  -0.0193 215 SER   B CB  
2597 O  OG  . SER   B 122 ? 0.3376 0.1839 0.4038 0.0220  0.0116  -0.0168 215 SER   B OG  
2598 N  N   . VAL   B 123 ? 0.3558 0.2028 0.3963 0.0028  0.0125  -0.0149 216 VAL   B N   
2599 C  CA  . VAL   B 123 ? 0.3528 0.2021 0.3887 -0.0022 0.0119  -0.0112 216 VAL   B CA  
2600 C  C   . VAL   B 123 ? 0.3554 0.1989 0.3913 -0.0006 0.0091  -0.0073 216 VAL   B C   
2601 O  O   . VAL   B 123 ? 0.3540 0.1893 0.3890 0.0011  0.0082  -0.0055 216 VAL   B O   
2602 C  CB  . VAL   B 123 ? 0.3555 0.2028 0.3843 -0.0078 0.0127  -0.0096 216 VAL   B CB  
2603 C  CG1 . VAL   B 123 ? 0.3618 0.2006 0.3867 -0.0070 0.0114  -0.0090 216 VAL   B CG1 
2604 C  CG2 . VAL   B 123 ? 0.3571 0.2025 0.3839 -0.0129 0.0121  -0.0057 216 VAL   B CG2 
2605 N  N   A VAL   B 124 ? 0.3520 0.2022 0.3893 -0.0018 0.0081  -0.0069 217 VAL   B N   
2606 N  N   B VAL   B 124 ? 0.3544 0.2046 0.3918 -0.0018 0.0081  -0.0069 217 VAL   B N   
2607 C  CA  A VAL   B 124 ? 0.3487 0.1992 0.3854 0.0000  0.0055  -0.0047 217 VAL   B CA  
2608 C  CA  B VAL   B 124 ? 0.3522 0.2027 0.3890 0.0000  0.0056  -0.0047 217 VAL   B CA  
2609 C  C   A VAL   B 124 ? 0.3526 0.2035 0.3870 -0.0053 0.0048  -0.0069 217 VAL   B C   
2610 C  C   B VAL   B 124 ? 0.3547 0.2054 0.3890 -0.0053 0.0048  -0.0069 217 VAL   B C   
2611 O  O   A VAL   B 124 ? 0.3579 0.2130 0.3943 -0.0099 0.0057  -0.0092 217 VAL   B O   
2612 O  O   B VAL   B 124 ? 0.3603 0.2155 0.3968 -0.0100 0.0057  -0.0092 217 VAL   B O   
2613 C  CB  A VAL   B 124 ? 0.3461 0.2074 0.3884 0.0053  0.0042  -0.0031 217 VAL   B CB  
2614 C  CB  B VAL   B 124 ? 0.3526 0.2140 0.3948 0.0052  0.0042  -0.0032 217 VAL   B CB  
2615 C  CG1 A VAL   B 124 ? 0.3428 0.2181 0.3900 0.0040  0.0044  -0.0067 217 VAL   B CG1 
2616 C  CG1 B VAL   B 124 ? 0.3530 0.2253 0.3944 0.0041  0.0017  -0.0038 217 VAL   B CG1 
2617 C  CG2 A VAL   B 124 ? 0.3434 0.2090 0.3835 0.0074  0.0017  0.0002  217 VAL   B CG2 
2618 C  CG2 B VAL   B 124 ? 0.3522 0.2074 0.3967 0.0110  0.0038  0.0017  217 VAL   B CG2 
2619 N  N   . VAL   B 125 ? 0.3565 0.2025 0.3876 -0.0048 0.0035  -0.0067 218 VAL   B N   
2620 C  CA  . VAL   B 125 ? 0.3648 0.2098 0.3954 -0.0085 0.0025  -0.0110 218 VAL   B CA  
2621 C  C   . VAL   B 125 ? 0.3654 0.2198 0.3949 -0.0054 0.0006  -0.0128 218 VAL   B C   
2622 O  O   . VAL   B 125 ? 0.3643 0.2213 0.3919 -0.0009 0.0005  -0.0080 218 VAL   B O   
2623 C  CB  . VAL   B 125 ? 0.3711 0.2021 0.3995 -0.0101 0.0031  -0.0103 218 VAL   B CB  
2624 C  CG1 . VAL   B 125 ? 0.3728 0.1984 0.4014 -0.0141 0.0047  -0.0075 218 VAL   B CG1 
2625 C  CG2 . VAL   B 125 ? 0.3746 0.2017 0.4000 -0.0058 0.0030  -0.0070 218 VAL   B CG2 
2626 N  N   . PRO   B 126 ? 0.3738 0.2347 0.4045 -0.0082 -0.0007 -0.0199 219 PRO   B N   
2627 C  CA  . PRO   B 126 ? 0.3797 0.2519 0.4076 -0.0055 -0.0023 -0.0233 219 PRO   B CA  
2628 C  C   . PRO   B 126 ? 0.3796 0.2434 0.4041 -0.0028 -0.0012 -0.0222 219 PRO   B C   
2629 O  O   . PRO   B 126 ? 0.3719 0.2210 0.3978 -0.0042 -0.0002 -0.0230 219 PRO   B O   
2630 C  CB  . PRO   B 126 ? 0.3883 0.2662 0.4195 -0.0104 -0.0038 -0.0346 219 PRO   B CB  
2631 C  CG  . PRO   B 126 ? 0.3900 0.2582 0.4269 -0.0167 -0.0028 -0.0352 219 PRO   B CG  
2632 C  CD  . PRO   B 126 ? 0.3790 0.2379 0.4144 -0.0149 -0.0007 -0.0255 219 PRO   B CD  
2633 N  N   . TYR   B 127 ? 0.3842 0.2595 0.4050 0.0011  -0.0014 -0.0193 220 TYR   B N   
2634 C  CA  . TYR   B 127 ? 0.3881 0.2625 0.4064 0.0035  -0.0001 -0.0201 220 TYR   B CA  
2635 C  C   . TYR   B 127 ? 0.4076 0.2852 0.4270 0.0027  -0.0007 -0.0329 220 TYR   B C   
2636 O  O   . TYR   B 127 ? 0.4018 0.2936 0.4205 0.0014  -0.0023 -0.0397 220 TYR   B O   
2637 C  CB  . TYR   B 127 ? 0.3817 0.2706 0.3960 0.0067  0.0003  -0.0124 220 TYR   B CB  
2638 C  CG  . TYR   B 127 ? 0.3819 0.2750 0.3944 0.0085  0.0021  -0.0142 220 TYR   B CG  
2639 C  CD1 . TYR   B 127 ? 0.3742 0.2567 0.3886 0.0088  0.0038  -0.0092 220 TYR   B CD1 
2640 C  CD2 . TYR   B 127 ? 0.3814 0.2912 0.3910 0.0098  0.0021  -0.0231 220 TYR   B CD2 
2641 C  CE1 . TYR   B 127 ? 0.3746 0.2634 0.3890 0.0107  0.0056  -0.0117 220 TYR   B CE1 
2642 C  CE2 . TYR   B 127 ? 0.3853 0.3016 0.3943 0.0122  0.0043  -0.0262 220 TYR   B CE2 
2643 C  CZ  . TYR   B 127 ? 0.3792 0.2850 0.3910 0.0127  0.0061  -0.0200 220 TYR   B CZ  
2644 O  OH  . TYR   B 127 ? 0.3696 0.2846 0.3821 0.0153  0.0082  -0.0234 220 TYR   B OH  
2645 N  N   . GLU   B 128 ? 0.4301 0.2945 0.4522 0.0035  0.0001  -0.0367 221 GLU   B N   
2646 C  CA  . GLU   B 128 ? 0.4629 0.3279 0.4880 0.0046  0.0000  -0.0497 221 GLU   B CA  
2647 C  C   . GLU   B 128 ? 0.4602 0.3310 0.4839 0.0099  0.0017  -0.0496 221 GLU   B C   
2648 O  O   . GLU   B 128 ? 0.4672 0.3308 0.4911 0.0115  0.0026  -0.0407 221 GLU   B O   
2649 C  CB  . GLU   B 128 ? 0.4897 0.3334 0.5222 0.0017  -0.0006 -0.0543 221 GLU   B CB  
2650 C  CG  . GLU   B 128 ? 0.5097 0.3530 0.5451 -0.0049 -0.0019 -0.0573 221 GLU   B CG  
2651 C  CD  . GLU   B 128 ? 0.5299 0.3937 0.5643 -0.0065 -0.0034 -0.0683 221 GLU   B CD  
2652 O  OE1 . GLU   B 128 ? 0.5751 0.4479 0.6092 -0.0034 -0.0034 -0.0792 221 GLU   B OE1 
2653 O  OE2 . GLU   B 128 ? 0.5429 0.4162 0.5770 -0.0104 -0.0047 -0.0665 221 GLU   B OE2 
2654 N  N   . PRO   B 129 ? 0.4596 0.3466 0.4823 0.0126  0.0022  -0.0604 222 PRO   B N   
2655 C  CA  . PRO   B 129 ? 0.4669 0.3637 0.4892 0.0178  0.0045  -0.0616 222 PRO   B CA  
2656 C  C   . PRO   B 129 ? 0.4670 0.3448 0.4975 0.0213  0.0046  -0.0653 222 PRO   B C   
2657 O  O   . PRO   B 129 ? 0.4675 0.3256 0.5037 0.0197  0.0029  -0.0688 222 PRO   B O   
2658 C  CB  . PRO   B 129 ? 0.4664 0.3874 0.4858 0.0195  0.0050  -0.0751 222 PRO   B CB  
2659 C  CG  . PRO   B 129 ? 0.4755 0.3918 0.4974 0.0154  0.0023  -0.0856 222 PRO   B CG  
2660 C  CD  . PRO   B 129 ? 0.4692 0.3691 0.4916 0.0105  0.0007  -0.0734 222 PRO   B CD  
2661 N  N   . PRO   B 130 ? 0.4709 0.3551 0.5030 0.0263  0.0064  -0.0636 223 PRO   B N   
2662 C  CA  . PRO   B 130 ? 0.4844 0.3534 0.5252 0.0315  0.0060  -0.0663 223 PRO   B CA  
2663 C  C   . PRO   B 130 ? 0.5089 0.3684 0.5575 0.0344  0.0050  -0.0824 223 PRO   B C   
2664 O  O   . PRO   B 130 ? 0.5060 0.3796 0.5525 0.0337  0.0056  -0.0946 223 PRO   B O   
2665 C  CB  . PRO   B 130 ? 0.4840 0.3716 0.5254 0.0364  0.0085  -0.0651 223 PRO   B CB  
2666 C  CG  . PRO   B 130 ? 0.4709 0.3756 0.5034 0.0312  0.0102  -0.0545 223 PRO   B CG  
2667 C  CD  . PRO   B 130 ? 0.4706 0.3783 0.4973 0.0272  0.0091  -0.0580 223 PRO   B CD  
2668 N  N   . GLU   B 131 ? 0.5289 0.3653 0.5865 0.0374  0.0034  -0.0820 224 GLU   B N   
2669 C  CA  . GLU   B 131 ? 0.5548 0.3770 0.6236 0.0411  0.0026  -0.0969 224 GLU   B CA  
2670 C  C   . GLU   B 131 ? 0.5584 0.3965 0.6325 0.0508  0.0046  -0.1098 224 GLU   B C   
2671 O  O   . GLU   B 131 ? 0.5459 0.4012 0.6166 0.0544  0.0063  -0.1031 224 GLU   B O   
2672 C  CB  . GLU   B 131 ? 0.5702 0.3626 0.6477 0.0419  0.0003  -0.0886 224 GLU   B CB  
2673 C  CG  . GLU   B 131 ? 0.5737 0.3528 0.6471 0.0319  -0.0009 -0.0783 224 GLU   B CG  
2674 C  CD  . GLU   B 131 ? 0.5780 0.3637 0.6488 0.0242  -0.0007 -0.0885 224 GLU   B CD  
2675 O  OE1 . GLU   B 131 ? 0.6092 0.3945 0.6872 0.0256  -0.0007 -0.1057 224 GLU   B OE1 
2676 O  OE2 . GLU   B 131 ? 0.5568 0.3501 0.6191 0.0175  -0.0007 -0.0805 224 GLU   B OE2 
2677 N  N   . VAL   B 132 ? 0.5830 0.4164 0.6661 0.0542  0.0046  -0.1288 225 VAL   B N   
2678 C  CA  . VAL   B 132 ? 0.5961 0.4422 0.6876 0.0649  0.0066  -0.1457 225 VAL   B CA  
2679 C  C   . VAL   B 132 ? 0.5983 0.4371 0.6979 0.0742  0.0062  -0.1360 225 VAL   B C   
2680 O  O   . VAL   B 132 ? 0.6148 0.4244 0.7235 0.0762  0.0034  -0.1288 225 VAL   B O   
2681 C  CB  . VAL   B 132 ? 0.6196 0.4510 0.7238 0.0669  0.0058  -0.1677 225 VAL   B CB  
2682 C  CG1 . VAL   B 132 ? 0.6413 0.4865 0.7553 0.0793  0.0081  -0.1868 225 VAL   B CG1 
2683 C  CG2 . VAL   B 132 ? 0.6175 0.4580 0.7150 0.0569  0.0053  -0.1786 225 VAL   B CG2 
2684 N  N   . GLY   B 133 ? 0.5881 0.4543 0.6846 0.0794  0.0089  -0.1349 226 GLY   B N   
2685 C  CA  . GLY   B 133 ? 0.5905 0.4583 0.6943 0.0880  0.0086  -0.1261 226 GLY   B CA  
2686 C  C   . GLY   B 133 ? 0.5720 0.4533 0.6652 0.0818  0.0090  -0.1070 226 GLY   B C   
2687 O  O   . GLY   B 133 ? 0.5866 0.4889 0.6825 0.0867  0.0108  -0.1048 226 GLY   B O   
2688 N  N   . SER   B 134 ? 0.5531 0.4234 0.6363 0.0713  0.0074  -0.0947 227 SER   B N   
2689 C  CA  . SER   B 134 ? 0.5255 0.3990 0.6012 0.0651  0.0068  -0.0764 227 SER   B CA  
2690 C  C   . SER   B 134 ? 0.5017 0.3990 0.5664 0.0579  0.0100  -0.0734 227 SER   B C   
2691 O  O   . SER   B 134 ? 0.4871 0.3942 0.5471 0.0560  0.0117  -0.0827 227 SER   B O   
2692 C  CB  . SER   B 134 ? 0.5256 0.3734 0.5985 0.0592  0.0035  -0.0660 227 SER   B CB  
2693 O  OG  . SER   B 134 ? 0.5385 0.3744 0.6105 0.0553  0.0033  -0.0744 227 SER   B OG  
2694 N  N   . ASP   B 135 ? 0.4846 0.3913 0.5460 0.0539  0.0106  -0.0606 228 ASP   B N   
2695 C  CA  . ASP   B 135 ? 0.4868 0.4152 0.5403 0.0473  0.0138  -0.0545 228 ASP   B CA  
2696 C  C   . ASP   B 135 ? 0.4693 0.3852 0.5157 0.0384  0.0123  -0.0414 228 ASP   B C   
2697 O  O   . ASP   B 135 ? 0.4672 0.3965 0.5085 0.0327  0.0146  -0.0339 228 ASP   B O   
2698 C  CB  . ASP   B 135 ? 0.4944 0.4454 0.5531 0.0495  0.0165  -0.0519 228 ASP   B CB  
2699 C  CG  . ASP   B 135 ? 0.5101 0.4801 0.5757 0.0588  0.0191  -0.0661 228 ASP   B CG  
2700 O  OD1 . ASP   B 135 ? 0.5192 0.4978 0.5809 0.0601  0.0210  -0.0769 228 ASP   B OD1 
2701 O  OD2 . ASP   B 135 ? 0.5245 0.5020 0.6000 0.0653  0.0190  -0.0674 228 ASP   B OD2 
2702 N  N   . CYS   B 136 ? 0.4669 0.3589 0.5135 0.0371  0.0089  -0.0386 229 CYS   B N   
2703 C  CA  . CYS   B 136 ? 0.4592 0.3401 0.5000 0.0296  0.0077  -0.0280 229 CYS   B CA  
2704 C  C   . CYS   B 136 ? 0.4519 0.3131 0.4911 0.0281  0.0053  -0.0300 229 CYS   B C   
2705 O  O   . CYS   B 136 ? 0.4435 0.2951 0.4876 0.0325  0.0042  -0.0373 229 CYS   B O   
2706 C  CB  . CYS   B 136 ? 0.4644 0.3425 0.5078 0.0279  0.0064  -0.0195 229 CYS   B CB  
2707 S  SG  . CYS   B 136 ? 0.4978 0.3614 0.5474 0.0340  0.0026  -0.0198 229 CYS   B SG  
2708 N  N   . THR   B 137 ? 0.4366 0.2920 0.4706 0.0221  0.0049  -0.0235 230 THR   B N   
2709 C  CA  . THR   B 137 ? 0.4354 0.2747 0.4682 0.0192  0.0031  -0.0236 230 THR   B CA  
2710 C  C   . THR   B 137 ? 0.4332 0.2619 0.4658 0.0171  0.0017  -0.0152 230 THR   B C   
2711 O  O   . THR   B 137 ? 0.4379 0.2720 0.4684 0.0146  0.0023  -0.0094 230 THR   B O   
2712 C  CB  . THR   B 137 ? 0.4272 0.2721 0.4552 0.0151  0.0036  -0.0239 230 THR   B CB  
2713 O  OG1 . THR   B 137 ? 0.4412 0.3006 0.4685 0.0174  0.0047  -0.0323 230 THR   B OG1 
2714 C  CG2 . THR   B 137 ? 0.4285 0.2605 0.4567 0.0114  0.0022  -0.0244 230 THR   B CG2 
2715 N  N   . THR   B 138 ? 0.4259 0.2408 0.4610 0.0179  0.0000  -0.0145 231 THR   B N   
2716 C  CA  . THR   B 138 ? 0.4284 0.2362 0.4618 0.0160  -0.0014 -0.0064 231 THR   B CA  
2717 C  C   . THR   B 138 ? 0.4311 0.2319 0.4612 0.0102  -0.0010 -0.0044 231 THR   B C   
2718 O  O   . THR   B 138 ? 0.4256 0.2191 0.4580 0.0089  -0.0009 -0.0082 231 THR   B O   
2719 C  CB  . THR   B 138 ? 0.4325 0.2329 0.4707 0.0211  -0.0036 -0.0038 231 THR   B CB  
2720 O  OG1 . THR   B 138 ? 0.4304 0.2412 0.4730 0.0271  -0.0037 -0.0066 231 THR   B OG1 
2721 C  CG2 . THR   B 138 ? 0.4392 0.2377 0.4742 0.0193  -0.0053 0.0051  231 THR   B CG2 
2722 N  N   . ILE   B 139 ? 0.4198 0.2240 0.4458 0.0068  -0.0006 0.0000  232 ILE   B N   
2723 C  CA  . ILE   B 139 ? 0.4351 0.2357 0.4582 0.0020  0.0000  0.0025  232 ILE   B CA  
2724 C  C   . ILE   B 139 ? 0.4311 0.2305 0.4518 0.0015  -0.0011 0.0087  232 ILE   B C   
2725 O  O   . ILE   B 139 ? 0.4373 0.2429 0.4573 0.0034  -0.0022 0.0099  232 ILE   B O   
2726 C  CB  . ILE   B 139 ? 0.4320 0.2395 0.4534 -0.0001 0.0014  0.0013  232 ILE   B CB  
2727 C  CG1 . ILE   B 139 ? 0.4369 0.2489 0.4596 0.0005  0.0019  -0.0027 232 ILE   B CG1 
2728 C  CG2 . ILE   B 139 ? 0.4448 0.2519 0.4643 -0.0039 0.0023  0.0030  232 ILE   B CG2 
2729 C  CD1 . ILE   B 139 ? 0.4317 0.2506 0.4540 0.0003  0.0028  -0.0015 232 ILE   B CD1 
2730 N  N   . HIS   B 140 ? 0.4344 0.2281 0.4541 -0.0015 -0.0008 0.0127  233 HIS   B N   
2731 C  CA  . HIS   B 140 ? 0.4450 0.2406 0.4608 -0.0027 -0.0017 0.0204  233 HIS   B CA  
2732 C  C   . HIS   B 140 ? 0.4284 0.2328 0.4394 -0.0073 0.0003  0.0196  233 HIS   B C   
2733 O  O   . HIS   B 140 ? 0.4243 0.2274 0.4357 -0.0115 0.0024  0.0199  233 HIS   B O   
2734 C  CB  . HIS   B 140 ? 0.4679 0.2521 0.4865 -0.0031 -0.0024 0.0275  233 HIS   B CB  
2735 C  CG  . HIS   B 140 ? 0.4808 0.2570 0.5052 0.0035  -0.0049 0.0280  233 HIS   B CG  
2736 N  ND1 . HIS   B 140 ? 0.5108 0.2719 0.5417 0.0045  -0.0056 0.0319  233 HIS   B ND1 
2737 C  CD2 . HIS   B 140 ? 0.4817 0.2635 0.5081 0.0096  -0.0066 0.0248  233 HIS   B CD2 
2738 C  CE1 . HIS   B 140 ? 0.5092 0.2666 0.5459 0.0124  -0.0078 0.0303  233 HIS   B CE1 
2739 N  NE2 . HIS   B 140 ? 0.4877 0.2594 0.5215 0.0155  -0.0083 0.0260  233 HIS   B NE2 
2740 N  N   . TYR   B 141 ? 0.4267 0.2404 0.4349 -0.0066 0.0000  0.0170  234 TYR   B N   
2741 C  CA  . TYR   B 141 ? 0.4205 0.2437 0.4251 -0.0097 0.0019  0.0141  234 TYR   B CA  
2742 C  C   . TYR   B 141 ? 0.4383 0.2700 0.4364 -0.0115 0.0013  0.0203  234 TYR   B C   
2743 O  O   . TYR   B 141 ? 0.4616 0.2943 0.4581 -0.0091 -0.0015 0.0261  234 TYR   B O   
2744 C  CB  . TYR   B 141 ? 0.4065 0.2338 0.4132 -0.0085 0.0018  0.0068  234 TYR   B CB  
2745 C  CG  . TYR   B 141 ? 0.3889 0.2103 0.4010 -0.0072 0.0028  0.0034  234 TYR   B CG  
2746 C  CD1 . TYR   B 141 ? 0.3772 0.1987 0.3910 -0.0081 0.0049  0.0013  234 TYR   B CD1 
2747 C  CD2 . TYR   B 141 ? 0.3730 0.1916 0.3885 -0.0049 0.0017  0.0032  234 TYR   B CD2 
2748 C  CE1 . TYR   B 141 ? 0.3687 0.1876 0.3868 -0.0063 0.0053  -0.0001 234 TYR   B CE1 
2749 C  CE2 . TYR   B 141 ? 0.3676 0.1839 0.3866 -0.0038 0.0027  0.0019  234 TYR   B CE2 
2750 C  CZ  . TYR   B 141 ? 0.3664 0.1827 0.3864 -0.0043 0.0041  0.0006  234 TYR   B CZ  
2751 O  OH  . TYR   B 141 ? 0.3515 0.1682 0.3744 -0.0026 0.0044  0.0008  234 TYR   B OH  
2752 N  N   . ASN   B 142 ? 0.4418 0.2821 0.4363 -0.0153 0.0041  0.0197  235 ASN   B N   
2753 C  CA  . ASN   B 142 ? 0.4508 0.3062 0.4374 -0.0175 0.0044  0.0238  235 ASN   B CA  
2754 C  C   . ASN   B 142 ? 0.4468 0.3154 0.4319 -0.0182 0.0064  0.0122  235 ASN   B C   
2755 O  O   . ASN   B 142 ? 0.4481 0.3149 0.4377 -0.0186 0.0093  0.0060  235 ASN   B O   
2756 C  CB  . ASN   B 142 ? 0.4594 0.3168 0.4433 -0.0222 0.0070  0.0333  235 ASN   B CB  
2757 C  CG  . ASN   B 142 ? 0.4679 0.3091 0.4556 -0.0222 0.0054  0.0442  235 ASN   B CG  
2758 O  OD1 . ASN   B 142 ? 0.4791 0.3168 0.4684 -0.0271 0.0077  0.0509  235 ASN   B OD1 
2759 N  ND2 . ASN   B 142 ? 0.4706 0.3020 0.4615 -0.0169 0.0017  0.0452  235 ASN   B ND2 
2760 N  N   . TYR   B 143 ? 0.4587 0.3409 0.4387 -0.0179 0.0047  0.0089  236 TYR   B N   
2761 C  CA  . TYR   B 143 ? 0.4575 0.3547 0.4360 -0.0188 0.0066  -0.0037 236 TYR   B CA  
2762 C  C   . TYR   B 143 ? 0.4739 0.3917 0.4425 -0.0220 0.0087  0.0007  236 TYR   B C   
2763 O  O   . TYR   B 143 ? 0.4935 0.4203 0.4543 -0.0227 0.0062  0.0112  236 TYR   B O   
2764 C  CB  . TYR   B 143 ? 0.4573 0.3572 0.4379 -0.0176 0.0033  -0.0126 236 TYR   B CB  
2765 C  CG  . TYR   B 143 ? 0.4479 0.3295 0.4387 -0.0156 0.0024  -0.0159 236 TYR   B CG  
2766 C  CD1 . TYR   B 143 ? 0.4406 0.3118 0.4337 -0.0138 0.0000  -0.0074 236 TYR   B CD1 
2767 C  CD2 . TYR   B 143 ? 0.4442 0.3198 0.4430 -0.0152 0.0043  -0.0269 236 TYR   B CD2 
2768 C  CE1 . TYR   B 143 ? 0.4375 0.2957 0.4388 -0.0124 -0.0003 -0.0095 236 TYR   B CE1 
2769 C  CE2 . TYR   B 143 ? 0.4316 0.2919 0.4392 -0.0138 0.0038  -0.0271 236 TYR   B CE2 
2770 C  CZ  . TYR   B 143 ? 0.4333 0.2866 0.4414 -0.0128 0.0016  -0.0183 236 TYR   B CZ  
2771 O  OH  . TYR   B 143 ? 0.4151 0.2571 0.4307 -0.0118 0.0015  -0.0177 236 TYR   B OH  
2772 N  N   . MET   B 144 ? 0.4765 0.4034 0.4456 -0.0235 0.0134  -0.0060 237 MET   B N   
2773 C  CA  . MET   B 144 ? 0.4926 0.4392 0.4537 -0.0276 0.0171  0.0003  237 MET   B CA  
2774 C  C   . MET   B 144 ? 0.5065 0.4804 0.4604 -0.0280 0.0187  -0.0117 237 MET   B C   
2775 O  O   . MET   B 144 ? 0.5177 0.5129 0.4652 -0.0312 0.0229  -0.0094 237 MET   B O   
2776 C  CB  . MET   B 144 ? 0.4864 0.4286 0.4541 -0.0293 0.0217  0.0004  237 MET   B CB  
2777 C  CG  . MET   B 144 ? 0.4790 0.3974 0.4533 -0.0298 0.0202  0.0102  237 MET   B CG  
2778 S  SD  . MET   B 144 ? 0.4868 0.3971 0.4555 -0.0325 0.0170  0.0302  237 MET   B SD  
2779 C  CE  . MET   B 144 ? 0.4932 0.4285 0.4530 -0.0394 0.0218  0.0401  237 MET   B CE  
2780 N  N   . CYS   B 145 ? 0.5138 0.4891 0.4693 -0.0255 0.0156  -0.0244 238 CYS   B N   
2781 C  CA  . CYS   B 145 ? 0.5350 0.5362 0.4844 -0.0260 0.0158  -0.0389 238 CYS   B CA  
2782 C  C   . CYS   B 145 ? 0.5417 0.5427 0.4903 -0.0255 0.0097  -0.0421 238 CYS   B C   
2783 O  O   . CYS   B 145 ? 0.5298 0.5075 0.4873 -0.0237 0.0068  -0.0407 238 CYS   B O   
2784 C  CB  . CYS   B 145 ? 0.5386 0.5396 0.4976 -0.0236 0.0197  -0.0591 238 CYS   B CB  
2785 S  SG  . CYS   B 145 ? 0.5550 0.5832 0.5090 -0.0248 0.0268  -0.0635 238 CYS   B SG  
2786 N  N   . ASN   B 146 ? 0.5551 0.5844 0.4929 -0.0273 0.0077  -0.0456 239 ASN   B N   
2787 C  CA  . ASN   B 146 ? 0.5593 0.5968 0.4967 -0.0276 0.0018  -0.0529 239 ASN   B CA  
2788 C  C   . ASN   B 146 ? 0.5563 0.5898 0.5047 -0.0278 0.0026  -0.0782 239 ASN   B C   
2789 O  O   . ASN   B 146 ? 0.5482 0.5880 0.4987 -0.0273 0.0076  -0.0916 239 ASN   B O   
2790 C  CB  . ASN   B 146 ? 0.5847 0.6577 0.5063 -0.0294 -0.0008 -0.0475 239 ASN   B CB  
2791 C  CG  . ASN   B 146 ? 0.6043 0.6755 0.5188 -0.0282 -0.0040 -0.0208 239 ASN   B CG  
2792 O  OD1 . ASN   B 146 ? 0.6114 0.6607 0.5330 -0.0256 -0.0077 -0.0120 239 ASN   B OD1 
2793 N  ND2 . ASN   B 146 ? 0.6275 0.7215 0.5285 -0.0298 -0.0024 -0.0074 239 ASN   B ND2 
2794 N  N   . SER   B 147 ? 0.5563 0.5798 0.5131 -0.0286 -0.0018 -0.0844 240 SER   B N   
2795 C  CA  . SER   B 147 ? 0.5649 0.5837 0.5339 -0.0304 -0.0019 -0.1080 240 SER   B CA  
2796 C  C   . SER   B 147 ? 0.5759 0.6268 0.5380 -0.0324 -0.0009 -0.1274 240 SER   B C   
2797 O  O   . SER   B 147 ? 0.5852 0.6312 0.5578 -0.0324 0.0018  -0.1488 240 SER   B O   
2798 C  CB  . SER   B 147 ? 0.5646 0.5753 0.5416 -0.0329 -0.0073 -0.1088 240 SER   B CB  
2799 O  OG  . SER   B 147 ? 0.5681 0.5510 0.5523 -0.0308 -0.0074 -0.0936 240 SER   B OG  
2800 N  N   . SER   B 148 ? 0.5838 0.6668 0.5293 -0.0336 -0.0030 -0.1201 241 SER   B N   
2801 C  CA  . SER   B 148 ? 0.6117 0.7339 0.5467 -0.0359 -0.0027 -0.1370 241 SER   B CA  
2802 C  C   . SER   B 148 ? 0.6186 0.7539 0.5480 -0.0341 0.0045  -0.1417 241 SER   B C   
2803 O  O   . SER   B 148 ? 0.6424 0.8077 0.5666 -0.0353 0.0061  -0.1618 241 SER   B O   
2804 C  CB  . SER   B 148 ? 0.6258 0.7791 0.5447 -0.0374 -0.0083 -0.1236 241 SER   B CB  
2805 O  OG  . SER   B 148 ? 0.6253 0.7774 0.5337 -0.0351 -0.0069 -0.0957 241 SER   B OG  
2806 N  N   . CYS   B 149 ? 0.6078 0.7243 0.5385 -0.0315 0.0089  -0.1253 242 CYS   B N   
2807 C  CA  . CYS   B 149 ? 0.6179 0.7502 0.5431 -0.0304 0.0162  -0.1255 242 CYS   B CA  
2808 C  C   . CYS   B 149 ? 0.6252 0.7688 0.5583 -0.0285 0.0204  -0.1561 242 CYS   B C   
2809 O  O   . CYS   B 149 ? 0.6067 0.7212 0.5578 -0.0253 0.0213  -0.1687 242 CYS   B O   
2810 C  CB  . CYS   B 149 ? 0.6044 0.7078 0.5369 -0.0281 0.0197  -0.1091 242 CYS   B CB  
2811 S  SG  . CYS   B 149 ? 0.6113 0.7129 0.5322 -0.0306 0.0186  -0.0750 242 CYS   B SG  
2812 N  N   . MET   B 150 ? 0.6504 0.8357 0.5705 -0.0300 0.0229  -0.1666 243 MET   B N   
2813 C  CA  . MET   B 150 ? 0.6685 0.8735 0.5936 -0.0275 0.0283  -0.1961 243 MET   B CA  
2814 C  C   . MET   B 150 ? 0.6641 0.8519 0.6003 -0.0226 0.0352  -0.1941 243 MET   B C   
2815 O  O   . MET   B 150 ? 0.6413 0.8306 0.5701 -0.0238 0.0378  -0.1702 243 MET   B O   
2816 C  CB  . MET   B 150 ? 0.6923 0.9509 0.5974 -0.0303 0.0308  -0.2007 243 MET   B CB  
2817 C  CG  . MET   B 150 ? 0.7054 0.9910 0.5969 -0.0348 0.0239  -0.2024 243 MET   B CG  
2818 S  SD  . MET   B 150 ? 0.7352 1.0894 0.6017 -0.0376 0.0274  -0.2075 243 MET   B SD  
2819 C  CE  . MET   B 150 ? 0.7477 1.1152 0.6263 -0.0332 0.0355  -0.2480 243 MET   B CE  
2820 N  N   . GLY   B 151 ? 0.6752 0.8467 0.6300 -0.0172 0.0376  -0.2176 244 GLY   B N   
2821 C  CA  . GLY   B 151 ? 0.6821 0.8408 0.6495 -0.0109 0.0437  -0.2184 244 GLY   B CA  
2822 C  C   . GLY   B 151 ? 0.6739 0.7920 0.6504 -0.0097 0.0415  -0.1961 244 GLY   B C   
2823 O  O   . GLY   B 151 ? 0.6904 0.8036 0.6730 -0.0061 0.0459  -0.1890 244 GLY   B O   
2824 N  N   . GLY   B 152 ? 0.6805 0.7740 0.6579 -0.0128 0.0350  -0.1858 245 GLY   B N   
2825 C  CA  . GLY   B 152 ? 0.6616 0.7169 0.6481 -0.0117 0.0324  -0.1673 245 GLY   B CA  
2826 C  C   . GLY   B 152 ? 0.6645 0.6919 0.6637 -0.0117 0.0275  -0.1755 245 GLY   B C   
2827 O  O   . GLY   B 152 ? 0.6816 0.7039 0.6941 -0.0085 0.0287  -0.1980 245 GLY   B O   
2828 N  N   . MET   B 153 ? 0.6419 0.6536 0.6380 -0.0154 0.0224  -0.1590 246 MET   B N   
2829 C  CA  . MET   B 153 ? 0.6441 0.6336 0.6516 -0.0174 0.0178  -0.1653 246 MET   B CA  
2830 C  C   . MET   B 153 ? 0.6613 0.6726 0.6670 -0.0214 0.0158  -0.1875 246 MET   B C   
2831 O  O   . MET   B 153 ? 0.6663 0.6616 0.6876 -0.0222 0.0145  -0.2043 246 MET   B O   
2832 C  CB  . MET   B 153 ? 0.6275 0.6040 0.6301 -0.0205 0.0133  -0.1432 246 MET   B CB  
2833 C  CG  . MET   B 153 ? 0.6093 0.5624 0.6160 -0.0171 0.0148  -0.1250 246 MET   B CG  
2834 S  SD  . MET   B 153 ? 0.5931 0.5292 0.5974 -0.0195 0.0099  -0.1035 246 MET   B SD  
2835 C  CE  . MET   B 153 ? 0.5891 0.5499 0.5738 -0.0216 0.0089  -0.0878 246 MET   B CE  
2836 N  N   . ASN   B 154 ? 0.6702 0.7176 0.6582 -0.0240 0.0155  -0.1875 247 ASN   B N   
2837 C  CA  . ASN   B 154 ? 0.6869 0.7651 0.6700 -0.0276 0.0139  -0.2104 247 ASN   B CA  
2838 C  C   . ASN   B 154 ? 0.6990 0.7635 0.6929 -0.0325 0.0081  -0.2197 247 ASN   B C   
2839 O  O   . ASN   B 154 ? 0.7111 0.7724 0.7183 -0.0338 0.0084  -0.2461 247 ASN   B O   
2840 C  CB  . ASN   B 154 ? 0.7048 0.7950 0.6946 -0.0235 0.0196  -0.2363 247 ASN   B CB  
2841 C  CG  . ASN   B 154 ? 0.7248 0.8515 0.7079 -0.0271 0.0185  -0.2617 247 ASN   B CG  
2842 O  OD1 . ASN   B 154 ? 0.7257 0.8834 0.6907 -0.0316 0.0150  -0.2544 247 ASN   B OD1 
2843 N  ND2 . ASN   B 154 ? 0.7380 0.8619 0.7361 -0.0248 0.0210  -0.2918 247 ASN   B ND2 
2844 N  N   . ARG   B 155 ? 0.6824 0.7386 0.6720 -0.0353 0.0033  -0.1990 248 ARG   B N   
2845 C  CA  . ARG   B 155 ? 0.6915 0.7438 0.6878 -0.0412 -0.0028 -0.2028 248 ARG   B CA  
2846 C  C   . ARG   B 155 ? 0.6834 0.6958 0.7020 -0.0419 -0.0022 -0.2068 248 ARG   B C   
2847 O  O   . ARG   B 155 ? 0.7019 0.7084 0.7285 -0.0476 -0.0066 -0.2082 248 ARG   B O   
2848 C  CB  . ARG   B 155 ? 0.7067 0.7940 0.6985 -0.0462 -0.0058 -0.2267 248 ARG   B CB  
2849 C  CG  . ARG   B 155 ? 0.7137 0.8441 0.6821 -0.0454 -0.0064 -0.2203 248 ARG   B CG  
2850 C  CD  . ARG   B 155 ? 0.7263 0.8963 0.6863 -0.0510 -0.0120 -0.2355 248 ARG   B CD  
2851 N  NE  . ARG   B 155 ? 0.7188 0.8846 0.6836 -0.0553 -0.0191 -0.2276 248 ARG   B NE  
2852 C  CZ  . ARG   B 155 ? 0.7159 0.8896 0.6699 -0.0538 -0.0235 -0.2014 248 ARG   B CZ  
2853 N  NH1 . ARG   B 155 ? 0.6992 0.8834 0.6365 -0.0489 -0.0217 -0.1790 248 ARG   B NH1 
2854 N  NH2 . ARG   B 155 ? 0.7173 0.8888 0.6787 -0.0573 -0.0297 -0.1979 248 ARG   B NH2 
2855 N  N   . ARG   B 156 ? 0.6773 0.6649 0.7057 -0.0364 0.0027  -0.2063 249 ARG   B N   
2856 C  CA  . ARG   B 156 ? 0.6666 0.6159 0.7159 -0.0362 0.0034  -0.2060 249 ARG   B CA  
2857 C  C   . ARG   B 156 ? 0.6392 0.5706 0.6865 -0.0359 0.0017  -0.1790 249 ARG   B C   
2858 O  O   . ARG   B 156 ? 0.6385 0.5722 0.6744 -0.0316 0.0031  -0.1611 249 ARG   B O   
2859 C  CB  . ARG   B 156 ? 0.6716 0.6045 0.7320 -0.0289 0.0088  -0.2146 249 ARG   B CB  
2860 C  CG  . ARG   B 156 ? 0.6919 0.6412 0.7572 -0.0283 0.0109  -0.2447 249 ARG   B CG  
2861 C  CD  . ARG   B 156 ? 0.6941 0.6306 0.7704 -0.0190 0.0163  -0.2523 249 ARG   B CD  
2862 N  NE  . ARG   B 156 ? 0.6839 0.6364 0.7453 -0.0134 0.0196  -0.2375 249 ARG   B NE  
2863 C  CZ  . ARG   B 156 ? 0.6848 0.6325 0.7529 -0.0049 0.0244  -0.2393 249 ARG   B CZ  
2864 N  NH1 . ARG   B 156 ? 0.6941 0.6200 0.7836 0.0007  0.0262  -0.2545 249 ARG   B NH1 
2865 N  NH2 . ARG   B 156 ? 0.6704 0.6356 0.7251 -0.0020 0.0273  -0.2257 249 ARG   B NH2 
2866 N  N   . PRO   B 157 ? 0.6210 0.5353 0.6802 -0.0411 -0.0009 -0.1762 250 PRO   B N   
2867 C  CA  . PRO   B 157 ? 0.5923 0.4925 0.6504 -0.0407 -0.0021 -0.1528 250 PRO   B CA  
2868 C  C   . PRO   B 157 ? 0.5741 0.4476 0.6388 -0.0345 0.0017  -0.1412 250 PRO   B C   
2869 O  O   . PRO   B 157 ? 0.5860 0.4438 0.6637 -0.0323 0.0043  -0.1514 250 PRO   B O   
2870 C  CB  . PRO   B 157 ? 0.6012 0.4950 0.6723 -0.0489 -0.0052 -0.1573 250 PRO   B CB  
2871 C  CG  . PRO   B 157 ? 0.6275 0.5143 0.7140 -0.0525 -0.0040 -0.1816 250 PRO   B CG  
2872 C  CD  . PRO   B 157 ? 0.6368 0.5457 0.7122 -0.0483 -0.0026 -0.1960 250 PRO   B CD  
2873 N  N   . ILE   B 158 ? 0.5372 0.4071 0.5936 -0.0315 0.0016  -0.1207 251 ILE   B N   
2874 C  CA  . ILE   B 158 ? 0.5220 0.3717 0.5823 -0.0257 0.0044  -0.1079 251 ILE   B CA  
2875 C  C   . ILE   B 158 ? 0.5059 0.3433 0.5691 -0.0275 0.0029  -0.0919 251 ILE   B C   
2876 O  O   . ILE   B 158 ? 0.5003 0.3482 0.5588 -0.0314 0.0000  -0.0879 251 ILE   B O   
2877 C  CB  . ILE   B 158 ? 0.5138 0.3745 0.5610 -0.0204 0.0064  -0.1007 251 ILE   B CB  
2878 C  CG1 . ILE   B 158 ? 0.5005 0.3772 0.5325 -0.0220 0.0039  -0.0888 251 ILE   B CG1 
2879 C  CG2 . ILE   B 158 ? 0.5247 0.3983 0.5713 -0.0182 0.0090  -0.1171 251 ILE   B CG2 
2880 C  CD1 . ILE   B 158 ? 0.4932 0.3701 0.5166 -0.0181 0.0057  -0.0752 251 ILE   B CD1 
2881 N  N   . LEU   B 159 ? 0.4997 0.3178 0.5710 -0.0242 0.0049  -0.0835 252 LEU   B N   
2882 C  CA  . LEU   B 159 ? 0.4782 0.2878 0.5494 -0.0241 0.0045  -0.0665 252 LEU   B CA  
2883 C  C   . LEU   B 159 ? 0.4508 0.2610 0.5131 -0.0177 0.0058  -0.0560 252 LEU   B C   
2884 O  O   . LEU   B 159 ? 0.4418 0.2508 0.5050 -0.0132 0.0078  -0.0607 252 LEU   B O   
2885 C  CB  . LEU   B 159 ? 0.4951 0.2849 0.5820 -0.0257 0.0057  -0.0635 252 LEU   B CB  
2886 C  CG  . LEU   B 159 ? 0.5211 0.3057 0.6213 -0.0329 0.0051  -0.0760 252 LEU   B CG  
2887 C  CD1 . LEU   B 159 ? 0.5347 0.3119 0.6435 -0.0301 0.0066  -0.0917 252 LEU   B CD1 
2888 C  CD2 . LEU   B 159 ? 0.5346 0.3036 0.6478 -0.0375 0.0058  -0.0660 252 LEU   B CD2 
2889 N  N   . THR   B 160 ? 0.4194 0.2326 0.4745 -0.0174 0.0048  -0.0439 253 THR   B N   
2890 C  CA  . THR   B 160 ? 0.3949 0.2051 0.4453 -0.0127 0.0058  -0.0334 253 THR   B CA  
2891 C  C   . THR   B 160 ? 0.3813 0.1806 0.4391 -0.0122 0.0063  -0.0246 253 THR   B C   
2892 O  O   . THR   B 160 ? 0.3882 0.1880 0.4483 -0.0160 0.0055  -0.0212 253 THR   B O   
2893 C  CB  . THR   B 160 ? 0.3917 0.2112 0.4309 -0.0124 0.0044  -0.0268 253 THR   B CB  
2894 O  OG1 . THR   B 160 ? 0.4012 0.2323 0.4332 -0.0133 0.0039  -0.0321 253 THR   B OG1 
2895 C  CG2 . THR   B 160 ? 0.3876 0.2042 0.4235 -0.0088 0.0053  -0.0188 253 THR   B CG2 
2896 N  N   . ILE   B 161 ? 0.3717 0.1645 0.4328 -0.0076 0.0076  -0.0204 254 ILE   B N   
2897 C  CA  . ILE   B 161 ? 0.3726 0.1585 0.4388 -0.0062 0.0080  -0.0095 254 ILE   B CA  
2898 C  C   . ILE   B 161 ? 0.3672 0.1608 0.4244 -0.0029 0.0076  -0.0024 254 ILE   B C   
2899 O  O   . ILE   B 161 ? 0.3453 0.1424 0.3995 0.0003  0.0078  -0.0050 254 ILE   B O   
2900 C  CB  . ILE   B 161 ? 0.3833 0.1574 0.4612 -0.0024 0.0090  -0.0096 254 ILE   B CB  
2901 C  CG1 . ILE   B 161 ? 0.3938 0.1589 0.4822 -0.0060 0.0094  -0.0203 254 ILE   B CG1 
2902 C  CG2 . ILE   B 161 ? 0.3883 0.1574 0.4705 -0.0007 0.0091  0.0044  254 ILE   B CG2 
2903 C  CD1 . ILE   B 161 ? 0.4085 0.1610 0.5098 -0.0008 0.0104  -0.0247 254 ILE   B CD1 
2904 N  N   . ILE   B 162 ? 0.3705 0.1685 0.4241 -0.0045 0.0072  0.0044  255 ILE   B N   
2905 C  CA  . ILE   B 162 ? 0.3739 0.1794 0.4203 -0.0019 0.0068  0.0093  255 ILE   B CA  
2906 C  C   . ILE   B 162 ? 0.3890 0.1952 0.4387 0.0001  0.0073  0.0185  255 ILE   B C   
2907 O  O   . ILE   B 162 ? 0.4026 0.2086 0.4558 -0.0025 0.0081  0.0242  255 ILE   B O   
2908 C  CB  . ILE   B 162 ? 0.3629 0.1752 0.4035 -0.0037 0.0062  0.0089  255 ILE   B CB  
2909 C  CG1 . ILE   B 162 ? 0.3595 0.1724 0.3974 -0.0056 0.0051  0.0026  255 ILE   B CG1 
2910 C  CG2 . ILE   B 162 ? 0.3562 0.1747 0.3910 -0.0010 0.0058  0.0106  255 ILE   B CG2 
2911 C  CD1 . ILE   B 162 ? 0.3633 0.1761 0.3970 -0.0044 0.0050  -0.0011 255 ILE   B CD1 
2912 N  N   . THR   B 163 ? 0.4089 0.2179 0.4581 0.0045  0.0067  0.0208  256 THR   B N   
2913 C  CA  . THR   B 163 ? 0.4230 0.2363 0.4744 0.0077  0.0064  0.0311  256 THR   B CA  
2914 C  C   . THR   B 163 ? 0.4199 0.2478 0.4628 0.0091  0.0054  0.0314  256 THR   B C   
2915 O  O   . THR   B 163 ? 0.4158 0.2467 0.4549 0.0093  0.0046  0.0241  256 THR   B O   
2916 C  CB  . THR   B 163 ? 0.4373 0.2444 0.4970 0.0127  0.0060  0.0335  256 THR   B CB  
2917 O  OG1 . THR   B 163 ? 0.4466 0.2596 0.5038 0.0155  0.0052  0.0263  256 THR   B OG1 
2918 C  CG2 . THR   B 163 ? 0.4462 0.2375 0.5160 0.0114  0.0071  0.0302  256 THR   B CG2 
2919 N  N   . LEU   B 164 ? 0.4362 0.2737 0.4766 0.0092  0.0056  0.0394  257 LEU   B N   
2920 C  CA  . LEU   B 164 ? 0.4419 0.2965 0.4749 0.0109  0.0045  0.0392  257 LEU   B CA  
2921 C  C   . LEU   B 164 ? 0.4539 0.3164 0.4889 0.0157  0.0027  0.0480  257 LEU   B C   
2922 O  O   . LEU   B 164 ? 0.4600 0.3189 0.5000 0.0169  0.0033  0.0597  257 LEU   B O   
2923 C  CB  . LEU   B 164 ? 0.4406 0.3046 0.4696 0.0084  0.0061  0.0418  257 LEU   B CB  
2924 C  CG  . LEU   B 164 ? 0.4422 0.3242 0.4634 0.0094  0.0055  0.0366  257 LEU   B CG  
2925 C  CD1 . LEU   B 164 ? 0.4261 0.3024 0.4455 0.0084  0.0050  0.0232  257 LEU   B CD1 
2926 C  CD2 . LEU   B 164 ? 0.4486 0.3447 0.4669 0.0081  0.0078  0.0420  257 LEU   B CD2 
2927 N  N   . GLU   B 165 ? 0.4546 0.3266 0.4876 0.0183  0.0005  0.0431  258 GLU   B N   
2928 C  CA  . GLU   B 165 ? 0.4662 0.3497 0.5018 0.0240  -0.0019 0.0513  258 GLU   B CA  
2929 C  C   . GLU   B 165 ? 0.4607 0.3678 0.4886 0.0243  -0.0041 0.0475  258 GLU   B C   
2930 O  O   . GLU   B 165 ? 0.4357 0.3447 0.4593 0.0203  -0.0039 0.0352  258 GLU   B O   
2931 C  CB  . GLU   B 165 ? 0.4722 0.3481 0.5162 0.0278  -0.0028 0.0484  258 GLU   B CB  
2932 C  CG  . GLU   B 165 ? 0.4837 0.3443 0.5299 0.0244  -0.0008 0.0375  258 GLU   B CG  
2933 C  CD  . GLU   B 165 ? 0.4898 0.3477 0.5443 0.0286  -0.0011 0.0339  258 GLU   B CD  
2934 O  OE1 . GLU   B 165 ? 0.4893 0.3617 0.5441 0.0305  -0.0028 0.0308  258 GLU   B OE1 
2935 O  OE2 . GLU   B 165 ? 0.5182 0.3613 0.5799 0.0301  0.0004  0.0333  258 GLU   B OE2 
2936 N  N   . ASP   B 166 ? 0.4686 0.3930 0.4958 0.0290  -0.0066 0.0577  259 ASP   B N   
2937 C  CA  . ASP   B 166 ? 0.4853 0.4368 0.5058 0.0296  -0.0097 0.0531  259 ASP   B CA  
2938 C  C   . ASP   B 166 ? 0.4872 0.4420 0.5130 0.0309  -0.0122 0.0446  259 ASP   B C   
2939 O  O   . ASP   B 166 ? 0.4957 0.4329 0.5293 0.0318  -0.0110 0.0432  259 ASP   B O   
2940 C  CB  . ASP   B 166 ? 0.4957 0.4688 0.5120 0.0341  -0.0116 0.0684  259 ASP   B CB  
2941 C  CG  . ASP   B 166 ? 0.5071 0.4809 0.5316 0.0418  -0.0144 0.0831  259 ASP   B CG  
2942 O  OD1 . ASP   B 166 ? 0.5133 0.4757 0.5468 0.0445  -0.0152 0.0785  259 ASP   B OD1 
2943 O  OD2 . ASP   B 166 ? 0.5071 0.4939 0.5292 0.0456  -0.0156 0.0996  259 ASP   B OD2 
2944 N  N   . SER   B 167 ? 0.4994 0.4785 0.5216 0.0304  -0.0154 0.0380  260 SER   B N   
2945 C  CA  . SER   B 167 ? 0.5016 0.4890 0.5293 0.0295  -0.0178 0.0280  260 SER   B CA  
2946 C  C   . SER   B 167 ? 0.5025 0.4912 0.5397 0.0373  -0.0196 0.0380  260 SER   B C   
2947 O  O   . SER   B 167 ? 0.4910 0.4783 0.5356 0.0367  -0.0197 0.0306  260 SER   B O   
2948 C  CB  . SER   B 167 ? 0.5045 0.5200 0.5269 0.0268  -0.0212 0.0189  260 SER   B CB  
2949 O  OG  . SER   B 167 ? 0.5206 0.5612 0.5387 0.0329  -0.0246 0.0306  260 SER   B OG  
2950 N  N   . SER   B 168 ? 0.5082 0.4988 0.5463 0.0447  -0.0208 0.0547  261 SER   B N   
2951 C  CA  . SER   B 168 ? 0.5138 0.5045 0.5631 0.0544  -0.0229 0.0660  261 SER   B CA  
2952 C  C   . SER   B 168 ? 0.5103 0.4689 0.5683 0.0560  -0.0190 0.0683  261 SER   B C   
2953 O  O   . SER   B 168 ? 0.5209 0.4756 0.5904 0.0645  -0.0201 0.0745  261 SER   B O   
2954 C  CB  . SER   B 168 ? 0.5197 0.5283 0.5669 0.0618  -0.0265 0.0843  261 SER   B CB  
2955 O  OG  . SER   B 168 ? 0.5188 0.5620 0.5585 0.0610  -0.0308 0.0805  261 SER   B OG  
2956 N  N   . GLY   B 169 ? 0.4981 0.4363 0.5519 0.0488  -0.0149 0.0628  262 GLY   B N   
2957 C  CA  . GLY   B 169 ? 0.4919 0.4018 0.5530 0.0488  -0.0113 0.0625  262 GLY   B CA  
2958 C  C   . GLY   B 169 ? 0.5066 0.4029 0.5702 0.0507  -0.0102 0.0773  262 GLY   B C   
2959 O  O   . GLY   B 169 ? 0.5260 0.3991 0.5980 0.0509  -0.0077 0.0768  262 GLY   B O   
2960 N  N   . ASN   B 170 ? 0.5036 0.4144 0.5602 0.0508  -0.0116 0.0892  263 ASN   B N   
2961 C  CA  . ASN   B 170 ? 0.5123 0.4122 0.5708 0.0504  -0.0099 0.1054  263 ASN   B CA  
2962 C  C   . ASN   B 170 ? 0.4942 0.3791 0.5487 0.0411  -0.0056 0.0980  263 ASN   B C   
2963 O  O   . ASN   B 170 ? 0.4821 0.3770 0.5266 0.0358  -0.0049 0.0863  263 ASN   B O   
2964 C  CB  . ASN   B 170 ? 0.5244 0.4493 0.5753 0.0529  -0.0122 0.1213  263 ASN   B CB  
2965 C  CG  . ASN   B 170 ? 0.5443 0.4859 0.6002 0.0632  -0.0172 0.1308  263 ASN   B CG  
2966 O  OD1 . ASN   B 170 ? 0.5581 0.4848 0.6275 0.0706  -0.0182 0.1393  263 ASN   B OD1 
2967 N  ND2 . ASN   B 170 ? 0.5414 0.5151 0.5874 0.0640  -0.0207 0.1286  263 ASN   B ND2 
2968 N  N   . LEU   B 171 ? 0.4945 0.3561 0.5580 0.0394  -0.0031 0.1033  264 LEU   B N   
2969 C  CA  . LEU   B 171 ? 0.4919 0.3404 0.5540 0.0307  0.0005  0.0973  264 LEU   B CA  
2970 C  C   . LEU   B 171 ? 0.4902 0.3562 0.5420 0.0259  0.0019  0.1042  264 LEU   B C   
2971 O  O   . LEU   B 171 ? 0.5100 0.3843 0.5622 0.0275  0.0017  0.1215  264 LEU   B O   
2972 C  CB  . LEU   B 171 ? 0.5041 0.3270 0.5803 0.0298  0.0023  0.1030  264 LEU   B CB  
2973 C  CG  . LEU   B 171 ? 0.5047 0.3159 0.5821 0.0204  0.0056  0.0984  264 LEU   B CG  
2974 C  CD1 . LEU   B 171 ? 0.4912 0.2969 0.5658 0.0173  0.0062  0.0787  264 LEU   B CD1 
2975 C  CD2 . LEU   B 171 ? 0.5210 0.3101 0.6137 0.0187  0.0071  0.1077  264 LEU   B CD2 
2976 N  N   . LEU   B 172 ? 0.4794 0.3515 0.5228 0.0207  0.0033  0.0916  265 LEU   B N   
2977 C  CA  . LEU   B 172 ? 0.4857 0.3744 0.5207 0.0161  0.0055  0.0942  265 LEU   B CA  
2978 C  C   . LEU   B 172 ? 0.4856 0.3611 0.5251 0.0093  0.0089  0.0920  265 LEU   B C   
2979 O  O   . LEU   B 172 ? 0.5030 0.3895 0.5406 0.0053  0.0116  0.1006  265 LEU   B O   
2980 C  CB  . LEU   B 172 ? 0.4768 0.3826 0.5014 0.0164  0.0044  0.0797  265 LEU   B CB  
2981 C  CG  . LEU   B 172 ? 0.4770 0.3981 0.4976 0.0215  0.0006  0.0776  265 LEU   B CG  
2982 C  CD1 . LEU   B 172 ? 0.4688 0.4057 0.4807 0.0199  0.0000  0.0624  265 LEU   B CD1 
2983 C  CD2 . LEU   B 172 ? 0.4958 0.4343 0.5148 0.0255  -0.0008 0.0951  265 LEU   B CD2 
2984 N  N   . GLY   B 173 ? 0.4821 0.3389 0.5267 0.0076  0.0089  0.0805  266 GLY   B N   
2985 C  CA  . GLY   B 173 ? 0.4802 0.3274 0.5291 0.0012  0.0112  0.0757  266 GLY   B CA  
2986 C  C   . GLY   B 173 ? 0.4712 0.2993 0.5263 0.0007  0.0104  0.0648  266 GLY   B C   
2987 O  O   . GLY   B 173 ? 0.4959 0.3218 0.5487 0.0049  0.0085  0.0574  266 GLY   B O   
2988 N  N   . ARG   B 174 ? 0.4697 0.2866 0.5326 -0.0049 0.0119  0.0633  267 ARG   B N   
2989 C  CA  . ARG   B 174 ? 0.4590 0.2609 0.5273 -0.0061 0.0111  0.0515  267 ARG   B CA  
2990 C  C   . ARG   B 174 ? 0.4451 0.2470 0.5163 -0.0133 0.0122  0.0462  267 ARG   B C   
2991 O  O   . ARG   B 174 ? 0.4447 0.2491 0.5212 -0.0186 0.0141  0.0543  267 ARG   B O   
2992 C  CB  . ARG   B 174 ? 0.4802 0.2649 0.5604 -0.0041 0.0110  0.0546  267 ARG   B CB  
2993 C  CG  . ARG   B 174 ? 0.4857 0.2587 0.5706 -0.0043 0.0104  0.0401  267 ARG   B CG  
2994 C  CD  . ARG   B 174 ? 0.5090 0.2634 0.6092 -0.0034 0.0108  0.0413  267 ARG   B CD  
2995 N  NE  . ARG   B 174 ? 0.5183 0.2703 0.6217 0.0051  0.0099  0.0498  267 ARG   B NE  
2996 C  CZ  . ARG   B 174 ? 0.5400 0.2848 0.6519 0.0071  0.0101  0.0653  267 ARG   B CZ  
2997 N  NH1 . ARG   B 174 ? 0.5542 0.2923 0.6730 0.0000  0.0118  0.0750  267 ARG   B NH1 
2998 N  NH2 . ARG   B 174 ? 0.5453 0.2909 0.6598 0.0163  0.0085  0.0725  267 ARG   B NH2 
2999 N  N   A ASN   B 175 ? 0.4364 0.2378 0.5043 -0.0136 0.0109  0.0338  268 ASN   B N   
3000 N  N   B ASN   B 175 ? 0.4367 0.2382 0.5046 -0.0136 0.0109  0.0338  268 ASN   B N   
3001 C  CA  A ASN   B 175 ? 0.4357 0.2383 0.5072 -0.0196 0.0107  0.0266  268 ASN   B CA  
3002 C  CA  B ASN   B 175 ? 0.4375 0.2397 0.5092 -0.0197 0.0107  0.0266  268 ASN   B CA  
3003 C  C   A ASN   B 175 ? 0.4323 0.2276 0.5041 -0.0189 0.0091  0.0146  268 ASN   B C   
3004 C  C   B ASN   B 175 ? 0.4326 0.2278 0.5046 -0.0189 0.0091  0.0145  268 ASN   B C   
3005 O  O   A ASN   B 175 ? 0.4396 0.2305 0.5087 -0.0138 0.0087  0.0124  268 ASN   B O   
3006 O  O   B ASN   B 175 ? 0.4435 0.2343 0.5126 -0.0138 0.0087  0.0124  268 ASN   B O   
3007 C  CB  A ASN   B 175 ? 0.4281 0.2465 0.4924 -0.0196 0.0105  0.0256  268 ASN   B CB  
3008 C  CB  B ASN   B 175 ? 0.4315 0.2496 0.4964 -0.0200 0.0106  0.0256  268 ASN   B CB  
3009 C  CG  A ASN   B 175 ? 0.4307 0.2603 0.4962 -0.0218 0.0129  0.0354  268 ASN   B CG  
3010 C  CG  B ASN   B 175 ? 0.4373 0.2619 0.5096 -0.0271 0.0116  0.0262  268 ASN   B CG  
3011 O  OD1 A ASN   B 175 ? 0.4410 0.2738 0.5144 -0.0283 0.0144  0.0379  268 ASN   B OD1 
3012 O  OD1 B ASN   B 175 ? 0.4407 0.2649 0.5167 -0.0307 0.0101  0.0181  268 ASN   B OD1 
3013 N  ND2 A ASN   B 175 ? 0.4318 0.2703 0.4899 -0.0172 0.0135  0.0402  268 ASN   B ND2 
3014 N  ND2 B ASN   B 175 ? 0.4453 0.2788 0.5199 -0.0295 0.0141  0.0358  268 ASN   B ND2 
3015 N  N   . SER   B 176 ? 0.4299 0.2274 0.5050 -0.0241 0.0082  0.0067  269 SER   B N   
3016 C  CA  . SER   B 176 ? 0.4346 0.2297 0.5097 -0.0244 0.0068  -0.0056 269 SER   B CA  
3017 C  C   . SER   B 176 ? 0.4268 0.2340 0.5004 -0.0289 0.0048  -0.0120 269 SER   B C   
3018 O  O   . SER   B 176 ? 0.4306 0.2448 0.5078 -0.0328 0.0050  -0.0078 269 SER   B O   
3019 C  CB  . SER   B 176 ? 0.4469 0.2272 0.5341 -0.0264 0.0077  -0.0102 269 SER   B CB  
3020 O  OG  . SER   B 176 ? 0.4568 0.2330 0.5555 -0.0339 0.0085  -0.0078 269 SER   B OG  
3021 N  N   . PHE   B 177 ? 0.4401 0.2525 0.5082 -0.0279 0.0030  -0.0213 270 PHE   B N   
3022 C  CA  . PHE   B 177 ? 0.4512 0.2778 0.5174 -0.0314 0.0003  -0.0281 270 PHE   B CA  
3023 C  C   . PHE   B 177 ? 0.4618 0.2912 0.5251 -0.0315 -0.0007 -0.0399 270 PHE   B C   
3024 O  O   . PHE   B 177 ? 0.4860 0.3107 0.5441 -0.0268 0.0006  -0.0404 270 PHE   B O   
3025 C  CB  . PHE   B 177 ? 0.4388 0.2770 0.4959 -0.0272 -0.0012 -0.0214 270 PHE   B CB  
3026 C  CG  . PHE   B 177 ? 0.4276 0.2631 0.4744 -0.0208 -0.0009 -0.0177 270 PHE   B CG  
3027 C  CD1 . PHE   B 177 ? 0.4275 0.2550 0.4729 -0.0173 0.0010  -0.0107 270 PHE   B CD1 
3028 C  CD2 . PHE   B 177 ? 0.4330 0.2758 0.4716 -0.0191 -0.0027 -0.0207 270 PHE   B CD2 
3029 C  CE1 . PHE   B 177 ? 0.4229 0.2486 0.4606 -0.0129 0.0012  -0.0084 270 PHE   B CE1 
3030 C  CE2 . PHE   B 177 ? 0.4226 0.2626 0.4534 -0.0149 -0.0020 -0.0164 270 PHE   B CE2 
3031 C  CZ  . PHE   B 177 ? 0.4242 0.2549 0.4553 -0.0122 -0.0001 -0.0110 270 PHE   B CZ  
3032 N  N   . GLU   B 178 ? 0.4617 0.3011 0.5288 -0.0370 -0.0028 -0.0500 271 GLU   B N   
3033 C  CA  . GLU   B 178 ? 0.4635 0.3127 0.5262 -0.0376 -0.0042 -0.0630 271 GLU   B CA  
3034 C  C   . GLU   B 178 ? 0.4580 0.3224 0.5056 -0.0328 -0.0062 -0.0572 271 GLU   B C   
3035 O  O   . GLU   B 178 ? 0.4405 0.3096 0.4849 -0.0308 -0.0077 -0.0469 271 GLU   B O   
3036 C  CB  . GLU   B 178 ? 0.4614 0.3203 0.5326 -0.0456 -0.0066 -0.0760 271 GLU   B CB  
3037 C  CG  . GLU   B 178 ? 0.4757 0.3456 0.5436 -0.0466 -0.0075 -0.0924 271 GLU   B CG  
3038 C  CD  . GLU   B 178 ? 0.4885 0.3665 0.5670 -0.0553 -0.0097 -0.1092 271 GLU   B CD  
3039 O  OE1 . GLU   B 178 ? 0.4955 0.3915 0.5682 -0.0563 -0.0116 -0.1229 271 GLU   B OE1 
3040 O  OE2 . GLU   B 178 ? 0.4934 0.3611 0.5860 -0.0616 -0.0094 -0.1088 271 GLU   B OE2 
3041 N  N   . VAL   B 179 ? 0.4674 0.3389 0.5070 -0.0307 -0.0057 -0.0630 272 VAL   B N   
3042 C  CA  . VAL   B 179 ? 0.4824 0.3685 0.5077 -0.0271 -0.0072 -0.0562 272 VAL   B CA  
3043 C  C   . VAL   B 179 ? 0.5033 0.4106 0.5226 -0.0297 -0.0090 -0.0679 272 VAL   B C   
3044 O  O   . VAL   B 179 ? 0.5173 0.4238 0.5410 -0.0315 -0.0070 -0.0820 272 VAL   B O   
3045 C  CB  . VAL   B 179 ? 0.4763 0.3525 0.4962 -0.0224 -0.0040 -0.0481 272 VAL   B CB  
3046 C  CG1 . VAL   B 179 ? 0.4754 0.3648 0.4825 -0.0202 -0.0049 -0.0404 272 VAL   B CG1 
3047 C  CG2 . VAL   B 179 ? 0.4686 0.3281 0.4932 -0.0200 -0.0028 -0.0379 272 VAL   B CG2 
3048 N  N   . ARG   B 180 ? 0.5136 0.4405 0.5240 -0.0292 -0.0128 -0.0626 273 ARG   B N   
3049 C  CA  . ARG   B 180 ? 0.5289 0.4812 0.5286 -0.0302 -0.0146 -0.0689 273 ARG   B CA  
3050 C  C   . ARG   B 180 ? 0.5197 0.4783 0.5063 -0.0256 -0.0147 -0.0520 273 ARG   B C   
3051 O  O   . ARG   B 180 ? 0.5089 0.4643 0.4951 -0.0225 -0.0174 -0.0383 273 ARG   B O   
3052 C  CB  . ARG   B 180 ? 0.5554 0.5291 0.5567 -0.0341 -0.0199 -0.0760 273 ARG   B CB  
3053 C  CG  . ARG   B 180 ? 0.5790 0.5841 0.5670 -0.0345 -0.0227 -0.0798 273 ARG   B CG  
3054 C  CD  . ARG   B 180 ? 0.6030 0.6294 0.5959 -0.0405 -0.0270 -0.0969 273 ARG   B CD  
3055 N  NE  . ARG   B 180 ? 0.6238 0.6861 0.6034 -0.0402 -0.0318 -0.0962 273 ARG   B NE  
3056 C  CZ  . ARG   B 180 ? 0.6494 0.7351 0.6186 -0.0417 -0.0312 -0.1072 273 ARG   B CZ  
3057 N  NH1 . ARG   B 180 ? 0.6634 0.7388 0.6346 -0.0427 -0.0255 -0.1203 273 ARG   B NH1 
3058 N  NH2 . ARG   B 180 ? 0.6479 0.7693 0.6045 -0.0413 -0.0363 -0.1042 273 ARG   B NH2 
3059 N  N   . VAL   B 181 ? 0.5232 0.4893 0.5013 -0.0252 -0.0116 -0.0530 274 VAL   B N   
3060 C  CA  . VAL   B 181 ? 0.5284 0.5029 0.4942 -0.0227 -0.0114 -0.0364 274 VAL   B CA  
3061 C  C   . VAL   B 181 ? 0.5440 0.5515 0.4983 -0.0242 -0.0147 -0.0383 274 VAL   B C   
3062 O  O   . VAL   B 181 ? 0.5428 0.5666 0.4944 -0.0271 -0.0129 -0.0542 274 VAL   B O   
3063 C  CB  . VAL   B 181 ? 0.5226 0.4880 0.4867 -0.0223 -0.0055 -0.0342 274 VAL   B CB  
3064 C  CG1 . VAL   B 181 ? 0.5223 0.4886 0.4779 -0.0210 -0.0051 -0.0145 274 VAL   B CG1 
3065 C  CG2 . VAL   B 181 ? 0.5146 0.4530 0.4910 -0.0211 -0.0027 -0.0381 274 VAL   B CG2 
3066 N  N   . CYS   B 182 ? 0.5584 0.5768 0.5072 -0.0217 -0.0197 -0.0238 275 CYS   B N   
3067 C  CA  . CYS   B 182 ? 0.5812 0.6346 0.5195 -0.0225 -0.0246 -0.0244 275 CYS   B CA  
3068 C  C   . CYS   B 182 ? 0.5887 0.6492 0.5185 -0.0179 -0.0281 0.0000  275 CYS   B C   
3069 O  O   . CYS   B 182 ? 0.5963 0.6318 0.5316 -0.0142 -0.0273 0.0140  275 CYS   B O   
3070 C  CB  . CYS   B 182 ? 0.5911 0.6552 0.5373 -0.0248 -0.0296 -0.0387 275 CYS   B CB  
3071 S  SG  . CYS   B 182 ? 0.6060 0.6468 0.5670 -0.0216 -0.0326 -0.0308 275 CYS   B SG  
3072 N  N   . ALA   B 183 ? 0.6070 0.7013 0.5243 -0.0180 -0.0318 0.0046  276 ALA   B N   
3073 C  CA  . ALA   B 183 ? 0.6178 0.7233 0.5258 -0.0133 -0.0353 0.0300  276 ALA   B CA  
3074 C  C   . ALA   B 183 ? 0.6132 0.7111 0.5301 -0.0069 -0.0419 0.0400  276 ALA   B C   
3075 O  O   . ALA   B 183 ? 0.6039 0.6870 0.5221 -0.0012 -0.0429 0.0613  276 ALA   B O   
3076 C  CB  . ALA   B 183 ? 0.6379 0.7865 0.5297 -0.0153 -0.0378 0.0304  276 ALA   B CB  
3077 N  N   A CYS   B 184 ? 0.6177 0.7256 0.5423 -0.0079 -0.0459 0.0244  277 CYS   B N   
3078 N  N   B CYS   B 184 ? 0.6081 0.7161 0.5326 -0.0078 -0.0459 0.0244  277 CYS   B N   
3079 C  CA  A CYS   B 184 ? 0.6267 0.7373 0.5603 -0.0019 -0.0526 0.0311  277 CYS   B CA  
3080 C  CA  B CYS   B 184 ? 0.6090 0.7198 0.5425 -0.0019 -0.0526 0.0311  277 CYS   B CA  
3081 C  C   A CYS   B 184 ? 0.6037 0.6949 0.5534 -0.0045 -0.0511 0.0149  277 CYS   B C   
3082 C  C   B CYS   B 184 ? 0.5923 0.6835 0.5420 -0.0045 -0.0511 0.0150  277 CYS   B C   
3083 O  O   A CYS   B 184 ? 0.6113 0.7199 0.5662 -0.0090 -0.0539 -0.0013 277 CYS   B O   
3084 O  O   B CYS   B 184 ? 0.5934 0.7018 0.5484 -0.0090 -0.0539 -0.0013 277 CYS   B O   
3085 C  CB  A CYS   B 184 ? 0.6544 0.8080 0.5806 -0.0009 -0.0605 0.0311  277 CYS   B CB  
3086 C  CB  B CYS   B 184 ? 0.6235 0.7777 0.5497 -0.0013 -0.0604 0.0301  277 CYS   B CB  
3087 S  SG  A CYS   B 184 ? 0.7038 0.8732 0.6181 0.0082  -0.0655 0.0637  277 CYS   B SG  
3088 S  SG  B CYS   B 184 ? 0.6504 0.8318 0.5569 0.0028  -0.0632 0.0546  277 CYS   B SG  
3089 N  N   . PRO   B 185 ? 0.5808 0.6368 0.5391 -0.0023 -0.0465 0.0196  278 PRO   B N   
3090 C  CA  . PRO   B 185 ? 0.5627 0.6007 0.5353 -0.0048 -0.0443 0.0071  278 PRO   B CA  
3091 C  C   . PRO   B 185 ? 0.5538 0.6065 0.5367 -0.0025 -0.0500 0.0053  278 PRO   B C   
3092 O  O   . PRO   B 185 ? 0.5349 0.5911 0.5268 -0.0089 -0.0497 -0.0103 278 PRO   B O   
3093 C  CB  . PRO   B 185 ? 0.5660 0.5706 0.5431 -0.0006 -0.0398 0.0175  278 PRO   B CB  
3094 C  CG  . PRO   B 185 ? 0.5726 0.5741 0.5381 0.0005  -0.0377 0.0301  278 PRO   B CG  
3095 C  CD  . PRO   B 185 ? 0.5832 0.6169 0.5381 0.0020  -0.0433 0.0371  278 PRO   B CD  
3096 N  N   . GLY   B 186 ? 0.5530 0.6143 0.5358 0.0064  -0.0549 0.0214  279 GLY   B N   
3097 C  CA  . GLY   B 186 ? 0.5495 0.6301 0.5424 0.0105  -0.0610 0.0215  279 GLY   B CA  
3098 C  C   . GLY   B 186 ? 0.5538 0.6683 0.5459 0.0031  -0.0654 0.0064  279 GLY   B C   
3099 O  O   . GLY   B 186 ? 0.5465 0.6658 0.5513 -0.0021 -0.0657 -0.0066 279 GLY   B O   
3100 N  N   . ARG   B 187 ? 0.5602 0.6986 0.5382 0.0017  -0.0683 0.0074  280 ARG   B N   
3101 C  CA  . ARG   B 187 ? 0.5659 0.7420 0.5414 -0.0052 -0.0734 -0.0081 280 ARG   B CA  
3102 C  C   . ARG   B 187 ? 0.5473 0.7122 0.5298 -0.0172 -0.0683 -0.0325 280 ARG   B C   
3103 O  O   . ARG   B 187 ? 0.5476 0.7298 0.5402 -0.0239 -0.0714 -0.0481 280 ARG   B O   
3104 C  CB  . ARG   B 187 ? 0.5873 0.7912 0.5439 -0.0039 -0.0765 -0.0014 280 ARG   B CB  
3105 C  CG  . ARG   B 187 ? 0.6083 0.8231 0.5584 0.0079  -0.0819 0.0253  280 ARG   B CG  
3106 C  CD  . ARG   B 187 ? 0.6345 0.8764 0.5647 0.0083  -0.0840 0.0349  280 ARG   B CD  
3107 N  NE  . ARG   B 187 ? 0.6585 0.9021 0.5841 0.0200  -0.0881 0.0645  280 ARG   B NE  
3108 C  CZ  . ARG   B 187 ? 0.6781 0.9381 0.5872 0.0224  -0.0892 0.0824  280 ARG   B CZ  
3109 N  NH1 . ARG   B 187 ? 0.6871 0.9673 0.5812 0.0142  -0.0863 0.0727  280 ARG   B NH1 
3110 N  NH2 . ARG   B 187 ? 0.6910 0.9477 0.5996 0.0334  -0.0932 0.1106  280 ARG   B NH2 
3111 N  N   . ASP   B 188 ? 0.5391 0.6765 0.5177 -0.0198 -0.0609 -0.0354 281 ASP   B N   
3112 C  CA  . ASP   B 188 ? 0.5301 0.6546 0.5155 -0.0297 -0.0559 -0.0575 281 ASP   B CA  
3113 C  C   . ASP   B 188 ? 0.5046 0.6083 0.5085 -0.0331 -0.0539 -0.0625 281 ASP   B C   
3114 O  O   . ASP   B 188 ? 0.4992 0.6064 0.5134 -0.0425 -0.0537 -0.0812 281 ASP   B O   
3115 C  CB  . ASP   B 188 ? 0.5402 0.6438 0.5170 -0.0296 -0.0491 -0.0570 281 ASP   B CB  
3116 C  CG  . ASP   B 188 ? 0.5608 0.6905 0.5201 -0.0289 -0.0501 -0.0560 281 ASP   B CG  
3117 O  OD1 . ASP   B 188 ? 0.5761 0.7419 0.5289 -0.0292 -0.0565 -0.0575 281 ASP   B OD1 
3118 O  OD2 . ASP   B 188 ? 0.5931 0.7099 0.5455 -0.0284 -0.0444 -0.0539 281 ASP   B OD2 
3119 N  N   . ARG   B 189 ? 0.4841 0.5680 0.4927 -0.0264 -0.0524 -0.0470 282 ARG   B N   
3120 C  CA  . ARG   B 189 ? 0.4726 0.5425 0.4979 -0.0293 -0.0504 -0.0498 282 ARG   B CA  
3121 C  C   . ARG   B 189 ? 0.4794 0.5803 0.5145 -0.0335 -0.0564 -0.0576 282 ARG   B C   
3122 O  O   . ARG   B 189 ? 0.4872 0.5862 0.5353 -0.0436 -0.0549 -0.0715 282 ARG   B O   
3123 C  CB  . ARG   B 189 ? 0.4489 0.4986 0.4765 -0.0202 -0.0481 -0.0331 282 ARG   B CB  
3124 C  CG  . ARG   B 189 ? 0.4340 0.4764 0.4774 -0.0231 -0.0459 -0.0357 282 ARG   B CG  
3125 C  CD  . ARG   B 189 ? 0.4180 0.4401 0.4637 -0.0149 -0.0426 -0.0230 282 ARG   B CD  
3126 N  NE  . ARG   B 189 ? 0.4026 0.4312 0.4625 -0.0165 -0.0420 -0.0245 282 ARG   B NE  
3127 C  CZ  . ARG   B 189 ? 0.3948 0.4208 0.4597 -0.0081 -0.0413 -0.0157 282 ARG   B CZ  
3128 N  NH1 . ARG   B 189 ? 0.3904 0.4035 0.4480 0.0022  -0.0412 -0.0049 282 ARG   B NH1 
3129 N  NH2 . ARG   B 189 ? 0.3924 0.4296 0.4705 -0.0106 -0.0404 -0.0184 282 ARG   B NH2 
3130 N  N   . ARG   B 190 ? 0.4938 0.6225 0.5239 -0.0263 -0.0632 -0.0482 283 ARG   B N   
3131 C  CA  . ARG   B 190 ? 0.5067 0.6703 0.5465 -0.0287 -0.0700 -0.0540 283 ARG   B CA  
3132 C  C   . ARG   B 190 ? 0.5287 0.7106 0.5712 -0.0421 -0.0717 -0.0767 283 ARG   B C   
3133 O  O   . ARG   B 190 ? 0.5293 0.7204 0.5879 -0.0514 -0.0725 -0.0890 283 ARG   B O   
3134 C  CB  . ARG   B 190 ? 0.5127 0.7047 0.5437 -0.0174 -0.0777 -0.0392 283 ARG   B CB  
3135 C  CG  . ARG   B 190 ? 0.5097 0.7199 0.5543 -0.0112 -0.0824 -0.0325 283 ARG   B CG  
3136 C  CD  . ARG   B 190 ? 0.5159 0.7554 0.5539 0.0012  -0.0908 -0.0172 283 ARG   B CD  
3137 N  NE  . ARG   B 190 ? 0.5133 0.7296 0.5484 0.0153  -0.0893 0.0037  283 ARG   B NE  
3138 C  CZ  . ARG   B 190 ? 0.5226 0.7547 0.5555 0.0289  -0.0957 0.0213  283 ARG   B CZ  
3139 N  NH1 . ARG   B 190 ? 0.5269 0.7321 0.5595 0.0407  -0.0936 0.0385  283 ARG   B NH1 
3140 N  NH2 . ARG   B 190 ? 0.5340 0.8089 0.5663 0.0308  -0.1046 0.0215  283 ARG   B NH2 
3141 N  N   . THR   B 191 ? 0.5415 0.7295 0.5696 -0.0435 -0.0719 -0.0827 284 THR   B N   
3142 C  CA  . THR   B 191 ? 0.5591 0.7661 0.5881 -0.0551 -0.0735 -0.1069 284 THR   B CA  
3143 C  C   . THR   B 191 ? 0.5671 0.7444 0.6120 -0.0661 -0.0671 -0.1228 284 THR   B C   
3144 O  O   . THR   B 191 ? 0.5533 0.7447 0.6118 -0.0771 -0.0694 -0.1404 284 THR   B O   
3145 C  CB  . THR   B 191 ? 0.5646 0.7827 0.5736 -0.0523 -0.0735 -0.1081 284 THR   B CB  
3146 O  OG1 . THR   B 191 ? 0.5616 0.8061 0.5581 -0.0420 -0.0797 -0.0889 284 THR   B OG1 
3147 C  CG2 . THR   B 191 ? 0.5758 0.8179 0.5843 -0.0628 -0.0754 -0.1348 284 THR   B CG2 
3148 N  N   . GLU   B 192 ? 0.5885 0.7267 0.6329 -0.0633 -0.0596 -0.1158 285 GLU   B N   
3149 C  CA  . GLU   B 192 ? 0.6067 0.7139 0.6654 -0.0723 -0.0533 -0.1278 285 GLU   B CA  
3150 C  C   . GLU   B 192 ? 0.6236 0.7267 0.7013 -0.0783 -0.0530 -0.1262 285 GLU   B C   
3151 O  O   . GLU   B 192 ? 0.6401 0.7335 0.7335 -0.0901 -0.0508 -0.1410 285 GLU   B O   
3152 C  CB  . GLU   B 192 ? 0.6085 0.6796 0.6610 -0.0661 -0.0462 -0.1180 285 GLU   B CB  
3153 C  CG  . GLU   B 192 ? 0.6177 0.6602 0.6831 -0.0739 -0.0406 -0.1310 285 GLU   B CG  
3154 C  CD  . GLU   B 192 ? 0.6165 0.6329 0.6742 -0.0682 -0.0348 -0.1277 285 GLU   B CD  
3155 O  OE1 . GLU   B 192 ? 0.6082 0.5949 0.6763 -0.0701 -0.0298 -0.1271 285 GLU   B OE1 
3156 O  OE2 . GLU   B 192 ? 0.6350 0.6632 0.6770 -0.0625 -0.0355 -0.1262 285 GLU   B OE2 
3157 N  N   . GLU   B 193 ? 0.6301 0.7414 0.7080 -0.0709 -0.0549 -0.1093 286 GLU   B N   
3158 C  CA  . GLU   B 193 ? 0.6397 0.7522 0.7353 -0.0758 -0.0541 -0.1064 286 GLU   B CA  
3159 C  C   . GLU   B 193 ? 0.6664 0.8144 0.7739 -0.0859 -0.0601 -0.1210 286 GLU   B C   
3160 O  O   . GLU   B 193 ? 0.6689 0.8145 0.7947 -0.0966 -0.0580 -0.1264 286 GLU   B O   
3161 C  CB  . GLU   B 193 ? 0.6248 0.7364 0.7172 -0.0631 -0.0539 -0.0860 286 GLU   B CB  
3162 C  CG  . GLU   B 193 ? 0.6193 0.6934 0.7087 -0.0583 -0.0465 -0.0751 286 GLU   B CG  
3163 C  CD  . GLU   B 193 ? 0.6168 0.6871 0.7013 -0.0449 -0.0461 -0.0574 286 GLU   B CD  
3164 O  OE1 . GLU   B 193 ? 0.6209 0.7163 0.7041 -0.0375 -0.0518 -0.0516 286 GLU   B OE1 
3165 O  OE2 . GLU   B 193 ? 0.5961 0.6389 0.6786 -0.0415 -0.0404 -0.0499 286 GLU   B OE2 
3166 N  N   . GLU   B 194 ? 0.6973 0.8787 0.7952 -0.0835 -0.0674 -0.1267 287 GLU   B N   
3167 C  CA  . GLU   B 194 ? 0.7306 0.9516 0.8382 -0.0933 -0.0744 -0.1427 287 GLU   B CA  
3168 C  C   . GLU   B 194 ? 0.7577 0.9677 0.8812 -0.1109 -0.0716 -0.1658 287 GLU   B C   
3169 O  O   . GLU   B 194 ? 0.7703 1.0055 0.9097 -0.1222 -0.0754 -0.1781 287 GLU   B O   
3170 C  CB  . GLU   B 194 ? 0.7476 1.0030 0.8377 -0.0873 -0.0819 -0.1455 287 GLU   B CB  
3171 C  CG  . GLU   B 194 ? 0.7545 1.0406 0.8386 -0.0745 -0.0888 -0.1277 287 GLU   B CG  
3172 C  CD  . GLU   B 194 ? 0.7781 1.0841 0.8399 -0.0633 -0.0939 -0.1182 287 GLU   B CD  
3173 O  OE1 . GLU   B 194 ? 0.8061 1.1229 0.8578 -0.0689 -0.0949 -0.1327 287 GLU   B OE1 
3174 O  OE2 . GLU   B 194 ? 0.7850 1.0956 0.8403 -0.0491 -0.0965 -0.0963 287 GLU   B OE2 
3175 N  N   . ASN   B 195 ? 0.7834 0.9577 0.9044 -0.1131 -0.0652 -0.1716 288 ASN   B N   
3176 C  CA  . ASN   B 195 ? 0.8120 0.9645 0.9515 -0.1284 -0.0611 -0.1903 288 ASN   B CA  
3177 C  C   . ASN   B 195 ? 0.8160 0.9389 0.9709 -0.1321 -0.0546 -0.1773 288 ASN   B C   
3178 O  O   . ASN   B 195 ? 0.8198 0.9546 0.9784 -0.1290 -0.0552 -0.1629 288 ASN   B O   
3179 C  CB  . ASN   B 195 ? 0.8284 0.9573 0.9605 -0.1278 -0.0574 -0.2026 288 ASN   B CB  
3180 C  CG  . ASN   B 195 ? 0.8502 1.0127 0.9719 -0.1292 -0.0634 -0.2223 288 ASN   B CG  
3181 O  OD1 . ASN   B 195 ? 0.8694 1.0690 0.9785 -0.1231 -0.0699 -0.2165 288 ASN   B OD1 
3182 N  ND2 . ASN   B 195 ? 0.8679 1.0194 0.9953 -0.1366 -0.0613 -0.2456 288 ASN   B ND2 
3183 N  N   . SER   C 3   ? 0.7925 0.5066 1.0373 -0.0780 0.0279  0.0582  96  SER   C N   
3184 C  CA  . SER   C 3   ? 0.8034 0.4982 1.0670 -0.0757 0.0280  0.0404  96  SER   C CA  
3185 C  C   . SER   C 3   ? 0.7884 0.4882 1.0324 -0.0625 0.0225  0.0342  96  SER   C C   
3186 O  O   . SER   C 3   ? 0.7826 0.4914 1.0203 -0.0620 0.0193  0.0112  96  SER   C O   
3187 C  CB  . SER   C 3   ? 0.8317 0.4980 1.1258 -0.0773 0.0341  0.0535  96  SER   C CB  
3188 O  OG  . SER   C 3   ? 0.8379 0.4994 1.1247 -0.0667 0.0336  0.0791  96  SER   C OG  
3189 N  N   . VAL   C 4   ? 0.7812 0.4775 1.0167 -0.0527 0.0214  0.0542  97  VAL   C N   
3190 C  CA  . VAL   C 4   ? 0.7509 0.4580 0.9635 -0.0411 0.0160  0.0525  97  VAL   C CA  
3191 C  C   . VAL   C 4   ? 0.7397 0.4583 0.9341 -0.0362 0.0145  0.0763  97  VAL   C C   
3192 O  O   . VAL   C 4   ? 0.7665 0.4767 0.9710 -0.0350 0.0171  0.0975  97  VAL   C O   
3193 C  CB  . VAL   C 4   ? 0.7683 0.4597 0.9946 -0.0326 0.0159  0.0450  97  VAL   C CB  
3194 C  CG1 . VAL   C 4   ? 0.7443 0.4481 0.9490 -0.0218 0.0109  0.0452  97  VAL   C CG1 
3195 C  CG2 . VAL   C 4   ? 0.7791 0.4636 1.0217 -0.0376 0.0176  0.0176  97  VAL   C CG2 
3196 N  N   . PRO   C 5   ? 0.6982 0.4373 0.8662 -0.0332 0.0103  0.0734  98  PRO   C N   
3197 C  CA  . PRO   C 5   ? 0.6772 0.4296 0.8277 -0.0284 0.0085  0.0915  98  PRO   C CA  
3198 C  C   . PRO   C 5   ? 0.6665 0.4137 0.8182 -0.0179 0.0061  0.1001  98  PRO   C C   
3199 O  O   . PRO   C 5   ? 0.6516 0.3918 0.8075 -0.0130 0.0044  0.0869  98  PRO   C O   
3200 C  CB  . PRO   C 5   ? 0.6596 0.4317 0.7863 -0.0280 0.0051  0.0807  98  PRO   C CB  
3201 C  CG  . PRO   C 5   ? 0.6612 0.4303 0.7911 -0.0295 0.0038  0.0584  98  PRO   C CG  
3202 C  CD  . PRO   C 5   ? 0.6731 0.4245 0.8282 -0.0345 0.0073  0.0529  98  PRO   C CD  
3203 N  N   . SER   C 6   ? 0.6737 0.4280 0.8213 -0.0148 0.0060  0.1221  99  SER   C N   
3204 C  CA  . SER   C 6   ? 0.6781 0.4326 0.8273 -0.0044 0.0032  0.1345  99  SER   C CA  
3205 C  C   . SER   C 6   ? 0.6530 0.4207 0.7839 0.0012  -0.0018 0.1213  99  SER   C C   
3206 O  O   . SER   C 6   ? 0.6313 0.4146 0.7428 -0.0021 -0.0033 0.1139  99  SER   C O   
3207 C  CB  . SER   C 6   ? 0.6976 0.4643 0.8426 -0.0034 0.0037  0.1609  99  SER   C CB  
3208 O  OG  . SER   C 6   ? 0.7180 0.4922 0.8610 0.0068  -0.0003 0.1718  99  SER   C OG  
3209 N  N   . GLN   C 7   ? 0.6453 0.4070 0.7844 0.0096  -0.0038 0.1189  100 GLN   C N   
3210 C  CA  . GLN   C 7   ? 0.6290 0.4034 0.7543 0.0152  -0.0081 0.1089  100 GLN   C CA  
3211 C  C   . GLN   C 7   ? 0.6387 0.4243 0.7639 0.0237  -0.0114 0.1259  100 GLN   C C   
3212 O  O   . GLN   C 7   ? 0.6289 0.4260 0.7460 0.0282  -0.0149 0.1190  100 GLN   C O   
3213 C  CB  . GLN   C 7   ? 0.6233 0.3855 0.7588 0.0172  -0.0073 0.0890  100 GLN   C CB  
3214 C  CG  . GLN   C 7   ? 0.6390 0.3850 0.7993 0.0245  -0.0055 0.0922  100 GLN   C CG  
3215 C  CD  . GLN   C 7   ? 0.6432 0.3739 0.8184 0.0224  -0.0022 0.0713  100 GLN   C CD  
3216 O  OE1 . GLN   C 7   ? 0.6471 0.3652 0.8335 0.0153  0.0012  0.0673  100 GLN   C OE1 
3217 N  NE2 . GLN   C 7   ? 0.6381 0.3724 0.8138 0.0279  -0.0031 0.0570  100 GLN   C NE2 
3218 N  N   . LYS   C 8   ? 0.6569 0.4418 0.7911 0.0253  -0.0103 0.1482  101 LYS   C N   
3219 C  CA  . LYS   C 8   ? 0.6686 0.4664 0.8053 0.0345  -0.0139 0.1679  101 LYS   C CA  
3220 C  C   . LYS   C 8   ? 0.6516 0.4801 0.7629 0.0334  -0.0185 0.1683  101 LYS   C C   
3221 O  O   . LYS   C 8   ? 0.6420 0.4819 0.7384 0.0261  -0.0175 0.1700  101 LYS   C O   
3222 C  CB  . LYS   C 8   ? 0.6973 0.4876 0.8493 0.0354  -0.0109 0.1939  101 LYS   C CB  
3223 C  CG  . LYS   C 8   ? 0.7146 0.5193 0.8719 0.0458  -0.0146 0.2184  101 LYS   C CG  
3224 C  CD  . LYS   C 8   ? 0.7483 0.5349 0.9315 0.0498  -0.0107 0.2430  101 LYS   C CD  
3225 C  CE  . LYS   C 8   ? 0.7656 0.5448 0.9496 0.0389  -0.0051 0.2528  101 LYS   C CE  
3226 N  NZ  . LYS   C 8   ? 0.7616 0.5733 0.9196 0.0341  -0.0070 0.2653  101 LYS   C NZ  
3227 N  N   . THR   C 9   ? 0.6397 0.4822 0.7477 0.0402  -0.0232 0.1654  102 THR   C N   
3228 C  CA  . THR   C 9   ? 0.6236 0.4964 0.7107 0.0390  -0.0279 0.1636  102 THR   C CA  
3229 C  C   . THR   C 9   ? 0.6383 0.5326 0.7184 0.0392  -0.0293 0.1864  102 THR   C C   
3230 O  O   . THR   C 9   ? 0.6588 0.5487 0.7538 0.0454  -0.0290 0.2081  102 THR   C O   
3231 C  CB  . THR   C 9   ? 0.6214 0.5051 0.7114 0.0462  -0.0323 0.1577  102 THR   C CB  
3232 O  OG1 . THR   C 9   ? 0.6158 0.4813 0.7110 0.0452  -0.0300 0.1374  102 THR   C OG1 
3233 C  CG2 . THR   C 9   ? 0.6132 0.5281 0.6845 0.0437  -0.0370 0.1533  102 THR   C CG2 
3234 N  N   . TYR   C 10  ? 0.6199 0.5377 0.6790 0.0330  -0.0305 0.1816  103 TYR   C N   
3235 C  CA  . TYR   C 10  ? 0.6282 0.5729 0.6759 0.0312  -0.0313 0.1997  103 TYR   C CA  
3236 C  C   . TYR   C 10  ? 0.6111 0.5860 0.6374 0.0266  -0.0344 0.1853  103 TYR   C C   
3237 O  O   . TYR   C 10  ? 0.5880 0.5607 0.6037 0.0190  -0.0313 0.1697  103 TYR   C O   
3238 C  CB  . TYR   C 10  ? 0.6355 0.5681 0.6844 0.0243  -0.0250 0.2069  103 TYR   C CB  
3239 C  CG  . TYR   C 10  ? 0.6555 0.6176 0.6906 0.0208  -0.0243 0.2234  103 TYR   C CG  
3240 C  CD1 . TYR   C 10  ? 0.6776 0.6626 0.7133 0.0270  -0.0276 0.2488  103 TYR   C CD1 
3241 C  CD2 . TYR   C 10  ? 0.6498 0.6193 0.6719 0.0118  -0.0201 0.2145  103 TYR   C CD2 
3242 C  CE1 . TYR   C 10  ? 0.6885 0.7051 0.7101 0.0235  -0.0267 0.2647  103 TYR   C CE1 
3243 C  CE2 . TYR   C 10  ? 0.6584 0.6583 0.6674 0.0084  -0.0187 0.2284  103 TYR   C CE2 
3244 C  CZ  . TYR   C 10  ? 0.6819 0.7061 0.6899 0.0139  -0.0219 0.2538  103 TYR   C CZ  
3245 O  OH  . TYR   C 10  ? 0.6911 0.7494 0.6847 0.0102  -0.0203 0.2681  103 TYR   C OH  
3246 N  N   . GLN   C 11  ? 0.6154 0.6183 0.6370 0.0313  -0.0404 0.1898  104 GLN   C N   
3247 C  CA  . GLN   C 11  ? 0.6067 0.6415 0.6101 0.0263  -0.0436 0.1747  104 GLN   C CA  
3248 C  C   . GLN   C 11  ? 0.6175 0.6768 0.6056 0.0208  -0.0415 0.1827  104 GLN   C C   
3249 O  O   . GLN   C 11  ? 0.5998 0.6731 0.5739 0.0137  -0.0402 0.1639  104 GLN   C O   
3250 C  CB  . GLN   C 11  ? 0.6120 0.6721 0.6172 0.0324  -0.0508 0.1773  104 GLN   C CB  
3251 C  CG  . GLN   C 11  ? 0.6066 0.6443 0.6262 0.0366  -0.0517 0.1660  104 GLN   C CG  
3252 C  CD  . GLN   C 11  ? 0.6111 0.6739 0.6355 0.0427  -0.0585 0.1681  104 GLN   C CD  
3253 O  OE1 . GLN   C 11  ? 0.6332 0.7287 0.6540 0.0467  -0.0635 0.1840  104 GLN   C OE1 
3254 N  NE2 . GLN   C 11  ? 0.6029 0.6528 0.6362 0.0437  -0.0587 0.1529  104 GLN   C NE2 
3255 N  N   . GLY   C 12  ? 0.6317 0.6953 0.6240 0.0241  -0.0404 0.2096  105 GLY   C N   
3256 C  CA  . GLY   C 12  ? 0.6461 0.7331 0.6253 0.0190  -0.0371 0.2214  105 GLY   C CA  
3257 C  C   . GLY   C 12  ? 0.6539 0.7891 0.6134 0.0167  -0.0414 0.2155  105 GLY   C C   
3258 O  O   . GLY   C 12  ? 0.6654 0.8197 0.6244 0.0209  -0.0483 0.2117  105 GLY   C O   
3259 N  N   . SER   C 13  ? 0.6457 0.8018 0.5903 0.0096  -0.0373 0.2123  106 SER   C N   
3260 C  CA  . SER   C 13  ? 0.6600 0.8692 0.5850 0.0069  -0.0400 0.2125  106 SER   C CA  
3261 C  C   . SER   C 13  ? 0.6437 0.8687 0.5605 0.0034  -0.0438 0.1805  106 SER   C C   
3262 O  O   . SER   C 13  ? 0.6366 0.9057 0.5424 0.0035  -0.0493 0.1800  106 SER   C O   
3263 C  CB  . SER   C 13  ? 0.6666 0.8902 0.5803 0.0002  -0.0329 0.2165  106 SER   C CB  
3264 O  OG  . SER   C 13  ? 0.6842 0.9616 0.5781 -0.0028 -0.0348 0.2134  106 SER   C OG  
3265 N  N   . TYR   C 14  ? 0.6250 0.8167 0.5486 0.0002  -0.0411 0.1556  107 TYR   C N   
3266 C  CA  . TYR   C 14  ? 0.6178 0.8185 0.5363 -0.0049 -0.0425 0.1235  107 TYR   C CA  
3267 C  C   . TYR   C 14  ? 0.6050 0.7888 0.5357 -0.0013 -0.0476 0.1162  107 TYR   C C   
3268 O  O   . TYR   C 14  ? 0.5965 0.7815 0.5269 -0.0061 -0.0481 0.0906  107 TYR   C O   
3269 C  CB  . TYR   C 14  ? 0.6139 0.7923 0.5318 -0.0110 -0.0351 0.1026  107 TYR   C CB  
3270 C  CG  . TYR   C 14  ? 0.6271 0.8284 0.5329 -0.0150 -0.0298 0.1062  107 TYR   C CG  
3271 C  CD1 . TYR   C 14  ? 0.6384 0.8826 0.5297 -0.0197 -0.0299 0.0917  107 TYR   C CD1 
3272 C  CD2 . TYR   C 14  ? 0.6307 0.8140 0.5402 -0.0147 -0.0243 0.1233  107 TYR   C CD2 
3273 C  CE1 . TYR   C 14  ? 0.6508 0.9203 0.5305 -0.0234 -0.0244 0.0940  107 TYR   C CE1 
3274 C  CE2 . TYR   C 14  ? 0.6413 0.8487 0.5404 -0.0189 -0.0188 0.1273  107 TYR   C CE2 
3275 C  CZ  . TYR   C 14  ? 0.6478 0.8992 0.5313 -0.0229 -0.0188 0.1129  107 TYR   C CZ  
3276 O  OH  . TYR   C 14  ? 0.6601 0.9389 0.5327 -0.0270 -0.0128 0.1158  107 TYR   C OH  
3277 N  N   . GLY   C 15  ? 0.6037 0.7742 0.5461 0.0067  -0.0508 0.1376  108 GLY   C N   
3278 C  CA  . GLY   C 15  ? 0.5934 0.7514 0.5486 0.0112  -0.0552 0.1329  108 GLY   C CA  
3279 C  C   . GLY   C 15  ? 0.5756 0.6953 0.5386 0.0076  -0.0511 0.1116  108 GLY   C C   
3280 O  O   . GLY   C 15  ? 0.5683 0.6922 0.5330 0.0044  -0.0531 0.0924  108 GLY   C O   
3281 N  N   . PHE   C 16  ? 0.5726 0.6581 0.5409 0.0078  -0.0455 0.1155  109 PHE   C N   
3282 C  CA  . PHE   C 16  ? 0.5531 0.6047 0.5267 0.0043  -0.0409 0.0974  109 PHE   C CA  
3283 C  C   . PHE   C 16  ? 0.5365 0.5641 0.5245 0.0095  -0.0424 0.0982  109 PHE   C C   
3284 O  O   . PHE   C 16  ? 0.5511 0.5652 0.5490 0.0158  -0.0425 0.1150  109 PHE   C O   
3285 C  CB  . PHE   C 16  ? 0.5535 0.5865 0.5258 0.0019  -0.0348 0.1011  109 PHE   C CB  
3286 C  CG  . PHE   C 16  ? 0.5383 0.5374 0.5177 0.0002  -0.0308 0.0882  109 PHE   C CG  
3287 C  CD1 . PHE   C 16  ? 0.5313 0.5271 0.5076 -0.0043 -0.0291 0.0670  109 PHE   C CD1 
3288 C  CD2 . PHE   C 16  ? 0.5426 0.5142 0.5326 0.0032  -0.0287 0.0974  109 PHE   C CD2 
3289 C  CE1 . PHE   C 16  ? 0.5243 0.4920 0.5067 -0.0050 -0.0257 0.0580  109 PHE   C CE1 
3290 C  CE2 . PHE   C 16  ? 0.5394 0.4853 0.5345 0.0015  -0.0255 0.0855  109 PHE   C CE2 
3291 C  CZ  . PHE   C 16  ? 0.5297 0.4746 0.5204 -0.0021 -0.0243 0.0672  109 PHE   C CZ  
3292 N  N   . ARG   C 17  ? 0.5219 0.5454 0.5123 0.0068  -0.0429 0.0802  110 ARG   C N   
3293 C  CA  . ARG   C 17  ? 0.5087 0.5124 0.5118 0.0105  -0.0433 0.0772  110 ARG   C CA  
3294 C  C   . ARG   C 17  ? 0.4800 0.4643 0.4834 0.0048  -0.0393 0.0584  110 ARG   C C   
3295 O  O   . ARG   C 17  ? 0.4721 0.4630 0.4678 -0.0014 -0.0375 0.0462  110 ARG   C O   
3296 C  CB  . ARG   C 17  ? 0.5191 0.5458 0.5272 0.0135  -0.0489 0.0780  110 ARG   C CB  
3297 C  CG  . ARG   C 17  ? 0.5487 0.5948 0.5598 0.0215  -0.0537 0.0993  110 ARG   C CG  
3298 C  CD  . ARG   C 17  ? 0.5499 0.6306 0.5617 0.0224  -0.0600 0.0972  110 ARG   C CD  
3299 N  NE  . ARG   C 17  ? 0.5561 0.6291 0.5826 0.0273  -0.0613 0.0950  110 ARG   C NE  
3300 C  CZ  . ARG   C 17  ? 0.5628 0.6616 0.5969 0.0329  -0.0671 0.1013  110 ARG   C CZ  
3301 N  N   . LEU   C 18  ? 0.4687 0.4312 0.4814 0.0073  -0.0376 0.0564  111 LEU   C N   
3302 C  CA  . LEU   C 18  ? 0.4457 0.3910 0.4597 0.0029  -0.0340 0.0421  111 LEU   C CA  
3303 C  C   . LEU   C 18  ? 0.4363 0.3918 0.4560 0.0014  -0.0358 0.0343  111 LEU   C C   
3304 O  O   . LEU   C 18  ? 0.4349 0.4033 0.4604 0.0062  -0.0394 0.0412  111 LEU   C O   
3305 C  CB  . LEU   C 18  ? 0.4438 0.3637 0.4636 0.0062  -0.0309 0.0451  111 LEU   C CB  
3306 C  CG  . LEU   C 18  ? 0.4498 0.3585 0.4670 0.0067  -0.0287 0.0520  111 LEU   C CG  
3307 C  CD1 . LEU   C 18  ? 0.4437 0.3305 0.4678 0.0086  -0.0260 0.0509  111 LEU   C CD1 
3308 C  CD2 . LEU   C 18  ? 0.4439 0.3560 0.4520 0.0012  -0.0264 0.0452  111 LEU   C CD2 
3309 N  N   . GLY   C 19  ? 0.4276 0.3786 0.4470 -0.0049 -0.0331 0.0210  112 GLY   C N   
3310 C  CA  . GLY   C 19  ? 0.4138 0.3700 0.4408 -0.0081 -0.0331 0.0131  112 GLY   C CA  
3311 C  C   . GLY   C 19  ? 0.4063 0.3403 0.4366 -0.0106 -0.0280 0.0080  112 GLY   C C   
3312 O  O   . GLY   C 19  ? 0.3955 0.3136 0.4213 -0.0109 -0.0250 0.0076  112 GLY   C O   
3313 N  N   . PHE   C 20  ? 0.4045 0.3395 0.4427 -0.0121 -0.0269 0.0052  113 PHE   C N   
3314 C  CA  . PHE   C 20  ? 0.4072 0.3254 0.4487 -0.0142 -0.0219 0.0030  113 PHE   C CA  
3315 C  C   . PHE   C 20  ? 0.4149 0.3415 0.4647 -0.0216 -0.0203 -0.0044 113 PHE   C C   
3316 O  O   . PHE   C 20  ? 0.4035 0.3504 0.4580 -0.0229 -0.0236 -0.0068 113 PHE   C O   
3317 C  CB  . PHE   C 20  ? 0.4065 0.3181 0.4500 -0.0073 -0.0214 0.0099  113 PHE   C CB  
3318 C  CG  . PHE   C 20  ? 0.4069 0.3098 0.4455 -0.0013 -0.0227 0.0164  113 PHE   C CG  
3319 C  CD1 . PHE   C 20  ? 0.4147 0.3017 0.4485 -0.0014 -0.0201 0.0167  113 PHE   C CD1 
3320 C  CD2 . PHE   C 20  ? 0.4119 0.3236 0.4524 0.0040  -0.0265 0.0230  113 PHE   C CD2 
3321 C  CE1 . PHE   C 20  ? 0.4162 0.2960 0.4475 0.0025  -0.0210 0.0218  113 PHE   C CE1 
3322 C  CE2 . PHE   C 20  ? 0.4139 0.3162 0.4525 0.0084  -0.0269 0.0299  113 PHE   C CE2 
3323 C  CZ  . PHE   C 20  ? 0.4187 0.3048 0.4530 0.0070  -0.0239 0.0285  113 PHE   C CZ  
3324 N  N   . LEU   C 21  ? 0.4171 0.3298 0.4702 -0.0263 -0.0152 -0.0070 114 LEU   C N   
3325 C  CA  . LEU   C 21  ? 0.4342 0.3516 0.4980 -0.0343 -0.0122 -0.0123 114 LEU   C CA  
3326 C  C   . LEU   C 21  ? 0.4245 0.3533 0.4934 -0.0317 -0.0123 -0.0078 114 LEU   C C   
3327 O  O   . LEU   C 21  ? 0.4237 0.3475 0.4881 -0.0243 -0.0123 -0.0010 114 LEU   C O   
3328 C  CB  . LEU   C 21  ? 0.4517 0.3490 0.5188 -0.0383 -0.0062 -0.0118 114 LEU   C CB  
3329 C  CG  . LEU   C 21  ? 0.4670 0.3538 0.5333 -0.0409 -0.0052 -0.0186 114 LEU   C CG  
3330 C  CD1 . LEU   C 21  ? 0.4804 0.3460 0.5512 -0.0417 0.0005  -0.0143 114 LEU   C CD1 
3331 C  CD2 . LEU   C 21  ? 0.4818 0.3815 0.5556 -0.0491 -0.0061 -0.0322 114 LEU   C CD2 
3332 N  N   . HIS   C 22  ? 0.4217 0.3674 0.5004 -0.0375 -0.0126 -0.0128 115 HIS   C N   
3333 C  CA  . HIS   C 22  ? 0.4116 0.3717 0.4981 -0.0360 -0.0117 -0.0100 115 HIS   C CA  
3334 C  C   . HIS   C 22  ? 0.3980 0.3488 0.4902 -0.0423 -0.0045 -0.0079 115 HIS   C C   
3335 O  O   . HIS   C 22  ? 0.4009 0.3598 0.5043 -0.0516 -0.0019 -0.0124 115 HIS   C O   
3336 C  CB  . HIS   C 22  ? 0.4237 0.4107 0.5185 -0.0389 -0.0162 -0.0158 115 HIS   C CB  
3337 C  CG  . HIS   C 22  ? 0.4402 0.4368 0.5280 -0.0340 -0.0231 -0.0161 115 HIS   C CG  
3338 N  ND1 . HIS   C 22  ? 0.4453 0.4391 0.5264 -0.0226 -0.0263 -0.0073 115 HIS   C ND1 
3339 C  CD2 . HIS   C 22  ? 0.4560 0.4653 0.5424 -0.0390 -0.0268 -0.0238 115 HIS   C CD2 
3340 C  CE1 . HIS   C 22  ? 0.4522 0.4568 0.5278 -0.0207 -0.0316 -0.0068 115 HIS   C CE1 
3341 N  NE2 . HIS   C 22  ? 0.4630 0.4786 0.5403 -0.0305 -0.0322 -0.0175 115 HIS   C NE2 
3342 N  N   A SER   C 23  ? 0.3941 0.3295 0.4791 -0.0377 -0.0013 -0.0008 116 SER   C N   
3343 N  N   B SER   C 23  ? 0.3941 0.3294 0.4792 -0.0378 -0.0013 -0.0008 116 SER   C N   
3344 C  CA  A SER   C 23  ? 0.3952 0.3190 0.4825 -0.0427 0.0054  0.0045  116 SER   C CA  
3345 C  CA  B SER   C 23  ? 0.3953 0.3192 0.4828 -0.0429 0.0055  0.0045  116 SER   C CA  
3346 C  C   A SER   C 23  ? 0.3943 0.3322 0.4867 -0.0434 0.0097  0.0088  116 SER   C C   
3347 C  C   B SER   C 23  ? 0.3940 0.3319 0.4864 -0.0435 0.0097  0.0088  116 SER   C C   
3348 O  O   A SER   C 23  ? 0.4046 0.3392 0.5023 -0.0501 0.0158  0.0141  116 SER   C O   
3349 O  O   B SER   C 23  ? 0.4031 0.3376 0.5007 -0.0500 0.0159  0.0144  116 SER   C O   
3350 C  CB  A SER   C 23  ? 0.3957 0.3015 0.4723 -0.0372 0.0059  0.0101  116 SER   C CB  
3351 C  CB  B SER   C 23  ? 0.3952 0.3009 0.4721 -0.0375 0.0060  0.0102  116 SER   C CB  
3352 O  OG  A SER   C 23  ? 0.3929 0.2871 0.4662 -0.0373 0.0031  0.0058  116 SER   C OG  
3353 O  OG  B SER   C 23  ? 0.3845 0.2923 0.4524 -0.0281 0.0020  0.0105  116 SER   C OG  
3354 N  N   . GLY   C 24  ? 0.3822 0.3357 0.4742 -0.0365 0.0071  0.0071  117 GLY   C N   
3355 C  CA  . GLY   C 24  ? 0.3843 0.3537 0.4804 -0.0354 0.0115  0.0095  117 GLY   C CA  
3356 C  C   . GLY   C 24  ? 0.3838 0.3465 0.4699 -0.0308 0.0151  0.0153  117 GLY   C C   
3357 O  O   . GLY   C 24  ? 0.3891 0.3348 0.4655 -0.0275 0.0132  0.0174  117 GLY   C O   
3358 N  N   . THR   C 25  ? 0.3891 0.3679 0.4777 -0.0312 0.0204  0.0175  118 THR   C N   
3359 C  CA  . THR   C 25  ? 0.3931 0.3748 0.4718 -0.0263 0.0238  0.0207  118 THR   C CA  
3360 C  C   . THR   C 25  ? 0.4126 0.4018 0.4918 -0.0339 0.0314  0.0308  118 THR   C C   
3361 O  O   . THR   C 25  ? 0.4152 0.4202 0.4892 -0.0313 0.0355  0.0324  118 THR   C O   
3362 C  CB  . THR   C 25  ? 0.3824 0.3811 0.4633 -0.0178 0.0235  0.0126  118 THR   C CB  
3363 O  OG1 . THR   C 25  ? 0.3749 0.3951 0.4680 -0.0212 0.0269  0.0107  118 THR   C OG1 
3364 C  CG2 . THR   C 25  ? 0.3769 0.3667 0.4589 -0.0095 0.0166  0.0059  118 THR   C CG2 
3365 N  N   . ALA   C 26  ? 0.4321 0.4116 0.5183 -0.0433 0.0337  0.0372  119 ALA   C N   
3366 C  CA  . ALA   C 26  ? 0.4554 0.4383 0.5445 -0.0511 0.0415  0.0503  119 ALA   C CA  
3367 C  C   . ALA   C 26  ? 0.4785 0.4535 0.5541 -0.0465 0.0421  0.0602  119 ALA   C C   
3368 O  O   . ALA   C 26  ? 0.4636 0.4216 0.5320 -0.0410 0.0367  0.0573  119 ALA   C O   
3369 C  CB  . ALA   C 26  ? 0.4628 0.4323 0.5659 -0.0619 0.0435  0.0533  119 ALA   C CB  
3370 N  N   . LYS   C 27  ? 0.5213 0.5110 0.5939 -0.0490 0.0487  0.0722  120 LYS   C N   
3371 C  CA  . LYS   C 27  ? 0.5486 0.5397 0.6078 -0.0446 0.0497  0.0837  120 LYS   C CA  
3372 C  C   . LYS   C 27  ? 0.5616 0.5247 0.6202 -0.0432 0.0461  0.0895  120 LYS   C C   
3373 O  O   . LYS   C 27  ? 0.5568 0.5185 0.6032 -0.0358 0.0423  0.0900  120 LYS   C O   
3374 C  CB  . LYS   C 27  ? 0.5778 0.5876 0.6382 -0.0506 0.0584  0.1007  120 LYS   C CB  
3375 C  CG  . LYS   C 27  ? 0.5861 0.6298 0.6429 -0.0501 0.0627  0.0954  120 LYS   C CG  
3376 C  CD  . LYS   C 27  ? 0.6062 0.6717 0.6639 -0.0569 0.0721  0.1134  120 LYS   C CD  
3377 C  CE  . LYS   C 27  ? 0.6092 0.7114 0.6635 -0.0560 0.0768  0.1056  120 LYS   C CE  
3378 N  NZ  . LYS   C 27  ? 0.6327 0.7598 0.6859 -0.0629 0.0864  0.1250  120 LYS   C NZ  
3379 N  N   . SER   C 28  ? 0.5772 0.5203 0.6497 -0.0498 0.0471  0.0913  121 SER   C N   
3380 C  CA  . SER   C 28  ? 0.6019 0.5184 0.6783 -0.0494 0.0456  0.0973  121 SER   C CA  
3381 C  C   . SER   C 28  ? 0.5906 0.4931 0.6610 -0.0427 0.0377  0.0837  121 SER   C C   
3382 O  O   . SER   C 28  ? 0.6158 0.5008 0.6861 -0.0397 0.0361  0.0879  121 SER   C O   
3383 C  CB  . SER   C 28  ? 0.6297 0.5314 0.7257 -0.0597 0.0504  0.1004  121 SER   C CB  
3384 O  OG  . SER   C 28  ? 0.6379 0.5410 0.7415 -0.0641 0.0477  0.0833  121 SER   C OG  
3385 N  N   A VAL   C 29  ? 0.5691 0.4798 0.6360 -0.0403 0.0333  0.0688  122 VAL   C N   
3386 N  N   B VAL   C 29  ? 0.5692 0.4798 0.6361 -0.0404 0.0333  0.0688  122 VAL   C N   
3387 C  CA  A VAL   C 29  ? 0.5475 0.4461 0.6113 -0.0358 0.0265  0.0566  122 VAL   C CA  
3388 C  CA  B VAL   C 29  ? 0.5482 0.4468 0.6119 -0.0358 0.0265  0.0565  122 VAL   C CA  
3389 C  C   A VAL   C 29  ? 0.5375 0.4326 0.5884 -0.0275 0.0230  0.0584  122 VAL   C C   
3390 C  C   B VAL   C 29  ? 0.5375 0.4326 0.5884 -0.0275 0.0230  0.0583  122 VAL   C C   
3391 O  O   A VAL   C 29  ? 0.5371 0.4476 0.5792 -0.0234 0.0232  0.0594  122 VAL   C O   
3392 O  O   B VAL   C 29  ? 0.5372 0.4477 0.5792 -0.0234 0.0232  0.0593  122 VAL   C O   
3393 C  CB  A VAL   C 29  ? 0.5321 0.4427 0.5972 -0.0348 0.0232  0.0440  122 VAL   C CB  
3394 C  CB  B VAL   C 29  ? 0.5347 0.4452 0.5997 -0.0347 0.0230  0.0438  122 VAL   C CB  
3395 C  CG1 A VAL   C 29  ? 0.5273 0.4279 0.5885 -0.0301 0.0166  0.0348  122 VAL   C CG1 
3396 C  CG1 B VAL   C 29  ? 0.5269 0.4461 0.5812 -0.0260 0.0196  0.0386  122 VAL   C CG1 
3397 C  CG2 A VAL   C 29  ? 0.5345 0.4522 0.6135 -0.0436 0.0261  0.0414  122 VAL   C CG2 
3398 C  CG2 B VAL   C 29  ? 0.5335 0.4335 0.6040 -0.0368 0.0188  0.0347  122 VAL   C CG2 
3399 N  N   . THR   C 30  ? 0.5251 0.4026 0.5760 -0.0255 0.0201  0.0574  123 THR   C N   
3400 C  CA  . THR   C 30  ? 0.5126 0.3865 0.5538 -0.0185 0.0167  0.0590  123 THR   C CA  
3401 C  C   . THR   C 30  ? 0.4853 0.3583 0.5211 -0.0145 0.0112  0.0466  123 THR   C C   
3402 O  O   . THR   C 30  ? 0.4733 0.3485 0.5013 -0.0094 0.0084  0.0455  123 THR   C O   
3403 C  CB  . THR   C 30  ? 0.5271 0.3843 0.5736 -0.0181 0.0179  0.0667  123 THR   C CB  
3404 O  OG1 . THR   C 30  ? 0.5359 0.3790 0.5909 -0.0215 0.0171  0.0577  123 THR   C OG1 
3405 C  CG2 . THR   C 30  ? 0.5345 0.3916 0.5882 -0.0213 0.0238  0.0823  123 THR   C CG2 
3406 N  N   A CYS   C 31  ? 0.4739 0.3453 0.5148 -0.0170 0.0096  0.0383  124 CYS   C N   
3407 N  N   B CYS   C 31  ? 0.4700 0.3407 0.5109 -0.0169 0.0095  0.0383  124 CYS   C N   
3408 C  CA  A CYS   C 31  ? 0.4599 0.3315 0.4975 -0.0132 0.0047  0.0294  124 CYS   C CA  
3409 C  CA  B CYS   C 31  ? 0.4534 0.3253 0.4908 -0.0131 0.0047  0.0294  124 CYS   C CA  
3410 C  C   A CYS   C 31  ? 0.4500 0.3304 0.4938 -0.0155 0.0039  0.0237  124 CYS   C C   
3411 C  C   B CYS   C 31  ? 0.4433 0.3238 0.4872 -0.0155 0.0039  0.0238  124 CYS   C C   
3412 O  O   A CYS   C 31  ? 0.4461 0.3262 0.4976 -0.0216 0.0056  0.0231  124 CYS   C O   
3413 O  O   B CYS   C 31  ? 0.4442 0.3243 0.4956 -0.0216 0.0057  0.0233  124 CYS   C O   
3414 C  CB  A CYS   C 31  ? 0.4644 0.3228 0.5006 -0.0123 0.0021  0.0275  124 CYS   C CB  
3415 C  CB  B CYS   C 31  ? 0.4529 0.3122 0.4879 -0.0114 0.0017  0.0272  124 CYS   C CB  
3416 S  SG  A CYS   C 31  ? 0.4648 0.3236 0.4986 -0.0094 -0.0029 0.0200  124 CYS   C SG  
3417 S  SG  B CYS   C 31  ? 0.4560 0.3078 0.4985 -0.0168 0.0016  0.0222  124 CYS   C SG  
3418 N  N   . THR   C 32  ? 0.4233 0.3122 0.4661 -0.0109 0.0017  0.0196  125 THR   C N   
3419 C  CA  . THR   C 32  ? 0.4116 0.3124 0.4617 -0.0110 0.0005  0.0154  125 THR   C CA  
3420 C  C   . THR   C 32  ? 0.3942 0.2951 0.4437 -0.0039 -0.0036 0.0121  125 THR   C C   
3421 O  O   . THR   C 32  ? 0.3931 0.2904 0.4389 0.0005  -0.0035 0.0112  125 THR   C O   
3422 C  CB  . THR   C 32  ? 0.4048 0.3204 0.4598 -0.0129 0.0049  0.0162  125 THR   C CB  
3423 O  OG1 . THR   C 32  ? 0.4071 0.3353 0.4711 -0.0135 0.0034  0.0122  125 THR   C OG1 
3424 C  CG2 . THR   C 32  ? 0.4078 0.3306 0.4584 -0.0076 0.0068  0.0151  125 THR   C CG2 
3425 N  N   . TYR   C 33  ? 0.3839 0.2899 0.4381 -0.0034 -0.0071 0.0107  126 TYR   C N   
3426 C  CA  . TYR   C 33  ? 0.3821 0.2882 0.4381 0.0033  -0.0112 0.0110  126 TYR   C CA  
3427 C  C   . TYR   C 33  ? 0.3767 0.2982 0.4431 0.0076  -0.0116 0.0095  126 TYR   C C   
3428 O  O   . TYR   C 33  ? 0.3774 0.3126 0.4492 0.0037  -0.0114 0.0083  126 TYR   C O   
3429 C  CB  . TYR   C 33  ? 0.3802 0.2843 0.4331 0.0017  -0.0152 0.0128  126 TYR   C CB  
3430 C  CG  . TYR   C 33  ? 0.3787 0.2864 0.4348 0.0083  -0.0193 0.0166  126 TYR   C CG  
3431 C  CD1 . TYR   C 33  ? 0.3806 0.2762 0.4355 0.0132  -0.0196 0.0196  126 TYR   C CD1 
3432 C  CD2 . TYR   C 33  ? 0.3750 0.2995 0.4369 0.0096  -0.0229 0.0181  126 TYR   C CD2 
3433 C  CE1 . TYR   C 33  ? 0.3859 0.2829 0.4459 0.0192  -0.0227 0.0256  126 TYR   C CE1 
3434 C  CE2 . TYR   C 33  ? 0.3823 0.3111 0.4481 0.0167  -0.0267 0.0249  126 TYR   C CE2 
3435 C  CZ  . TYR   C 33  ? 0.3897 0.3033 0.4550 0.0216  -0.0263 0.0295  126 TYR   C CZ  
3436 O  OH  . TYR   C 33  ? 0.3977 0.3135 0.4691 0.0286  -0.0294 0.0386  126 TYR   C OH  
3437 N  N   . SER   C 34  ? 0.3785 0.2979 0.4495 0.0155  -0.0119 0.0089  127 SER   C N   
3438 C  CA  . SER   C 34  ? 0.3801 0.3123 0.4638 0.0225  -0.0125 0.0076  127 SER   C CA  
3439 C  C   . SER   C 34  ? 0.3852 0.3166 0.4738 0.0283  -0.0178 0.0140  127 SER   C C   
3440 O  O   . SER   C 34  ? 0.3761 0.2934 0.4645 0.0324  -0.0185 0.0168  127 SER   C O   
3441 C  CB  . SER   C 34  ? 0.3811 0.3110 0.4695 0.0279  -0.0086 0.0015  127 SER   C CB  
3442 O  OG  . SER   C 34  ? 0.3797 0.3201 0.4830 0.0362  -0.0088 -0.0002 127 SER   C OG  
3443 N  N   . PRO   C 35  ? 0.3880 0.3367 0.4817 0.0285  -0.0215 0.0173  128 PRO   C N   
3444 C  CA  . PRO   C 35  ? 0.3986 0.3520 0.4974 0.0352  -0.0268 0.0259  128 PRO   C CA  
3445 C  C   . PRO   C 35  ? 0.4114 0.3619 0.5253 0.0469  -0.0262 0.0282  128 PRO   C C   
3446 O  O   . PRO   C 35  ? 0.4340 0.3764 0.5515 0.0528  -0.0287 0.0369  128 PRO   C O   
3447 C  CB  . PRO   C 35  ? 0.3922 0.3710 0.4942 0.0325  -0.0308 0.0267  128 PRO   C CB  
3448 C  CG  . PRO   C 35  ? 0.3858 0.3706 0.4860 0.0230  -0.0268 0.0176  128 PRO   C CG  
3449 C  CD  . PRO   C 35  ? 0.3812 0.3476 0.4768 0.0217  -0.0208 0.0134  128 PRO   C CD  
3450 N  N   . ALA   C 36  ? 0.4162 0.3734 0.5397 0.0500  -0.0223 0.0206  129 ALA   C N   
3451 C  CA  . ALA   C 36  ? 0.4312 0.3868 0.5724 0.0618  -0.0208 0.0196  129 ALA   C CA  
3452 C  C   . ALA   C 36  ? 0.4426 0.3725 0.5839 0.0641  -0.0182 0.0178  129 ALA   C C   
3453 O  O   . ALA   C 36  ? 0.4648 0.3862 0.6208 0.0735  -0.0187 0.0223  129 ALA   C O   
3454 C  CB  . ALA   C 36  ? 0.4245 0.3955 0.5742 0.0631  -0.0161 0.0092  129 ALA   C CB  
3455 N  N   . LEU   C 37  ? 0.4487 0.3674 0.5756 0.0557  -0.0154 0.0117  130 LEU   C N   
3456 C  CA  . LEU   C 37  ? 0.4546 0.3524 0.5814 0.0561  -0.0128 0.0071  130 LEU   C CA  
3457 C  C   . LEU   C 37  ? 0.4600 0.3438 0.5764 0.0514  -0.0158 0.0161  130 LEU   C C   
3458 O  O   . LEU   C 37  ? 0.4733 0.3405 0.5920 0.0514  -0.0141 0.0136  130 LEU   C O   
3459 C  CB  . LEU   C 37  ? 0.4468 0.3470 0.5650 0.0505  -0.0080 -0.0053 130 LEU   C CB  
3460 C  CG  . LEU   C 37  ? 0.4501 0.3659 0.5780 0.0547  -0.0037 -0.0159 130 LEU   C CG  
3461 C  CD1 . LEU   C 37  ? 0.4489 0.3734 0.5637 0.0474  0.0004  -0.0239 130 LEU   C CD1 
3462 C  CD2 . LEU   C 37  ? 0.4650 0.3724 0.6114 0.0639  -0.0011 -0.0239 130 LEU   C CD2 
3463 N  N   . ASN   C 38  ? 0.4547 0.3467 0.5610 0.0470  -0.0196 0.0244  131 ASN   C N   
3464 C  CA  . ASN   C 38  ? 0.4514 0.3351 0.5446 0.0408  -0.0216 0.0305  131 ASN   C CA  
3465 C  C   . ASN   C 38  ? 0.4443 0.3159 0.5284 0.0349  -0.0182 0.0224  131 ASN   C C   
3466 O  O   . ASN   C 38  ? 0.4350 0.2927 0.5182 0.0339  -0.0178 0.0241  131 ASN   C O   
3467 C  CB  . ASN   C 38  ? 0.4649 0.3411 0.5646 0.0456  -0.0241 0.0427  131 ASN   C CB  
3468 C  CG  . ASN   C 38  ? 0.4614 0.3345 0.5477 0.0394  -0.0257 0.0491  131 ASN   C CG  
3469 O  OD1 . ASN   C 38  ? 0.4524 0.3345 0.5263 0.0331  -0.0267 0.0464  131 ASN   C OD1 
3470 N  ND2 . ASN   C 38  ? 0.4714 0.3323 0.5621 0.0410  -0.0254 0.0574  131 ASN   C ND2 
3471 N  N   . LYS   C 39  ? 0.4357 0.3143 0.5142 0.0310  -0.0157 0.0146  132 LYS   C N   
3472 C  CA  . LYS   C 39  ? 0.4292 0.3015 0.5004 0.0270  -0.0126 0.0074  132 LYS   C CA  
3473 C  C   . LYS   C 39  ? 0.4161 0.2949 0.4761 0.0202  -0.0117 0.0076  132 LYS   C C   
3474 O  O   . LYS   C 39  ? 0.4215 0.3125 0.4835 0.0191  -0.0107 0.0069  132 LYS   C O   
3475 C  CB  . LYS   C 39  ? 0.4303 0.3059 0.5098 0.0310  -0.0091 -0.0024 132 LYS   C CB  
3476 C  CG  . LYS   C 39  ? 0.4323 0.3060 0.5047 0.0275  -0.0064 -0.0104 132 LYS   C CG  
3477 C  CD  . LYS   C 39  ? 0.4383 0.3168 0.5204 0.0318  -0.0030 -0.0228 132 LYS   C CD  
3478 C  CE  . LYS   C 39  ? 0.4455 0.3266 0.5202 0.0280  -0.0010 -0.0319 132 LYS   C CE  
3479 N  NZ  . LYS   C 39  ? 0.4628 0.3448 0.5500 0.0320  0.0018  -0.0466 132 LYS   C NZ  
3480 N  N   A MET   C 40  ? 0.4178 0.2884 0.4685 0.0159  -0.0118 0.0090  133 MET   C N   
3481 N  N   B MET   C 40  ? 0.4139 0.2844 0.4646 0.0159  -0.0118 0.0090  133 MET   C N   
3482 C  CA  A MET   C 40  ? 0.4198 0.2922 0.4620 0.0102  -0.0102 0.0098  133 MET   C CA  
3483 C  CA  B MET   C 40  ? 0.4133 0.2858 0.4556 0.0103  -0.0102 0.0098  133 MET   C CA  
3484 C  C   A MET   C 40  ? 0.4201 0.2968 0.4594 0.0101  -0.0070 0.0057  133 MET   C C   
3485 C  C   B MET   C 40  ? 0.4163 0.2930 0.4557 0.0101  -0.0070 0.0057  133 MET   C C   
3486 O  O   A MET   C 40  ? 0.4182 0.2910 0.4572 0.0120  -0.0071 0.0016  133 MET   C O   
3487 O  O   B MET   C 40  ? 0.4148 0.2876 0.4538 0.0120  -0.0071 0.0016  133 MET   C O   
3488 C  CB  A MET   C 40  ? 0.4232 0.2861 0.4588 0.0074  -0.0116 0.0130  133 MET   C CB  
3489 C  CB  B MET   C 40  ? 0.4117 0.2747 0.4473 0.0074  -0.0116 0.0130  133 MET   C CB  
3490 C  CG  A MET   C 40  ? 0.4321 0.2937 0.4620 0.0033  -0.0096 0.0144  133 MET   C CG  
3491 C  CG  B MET   C 40  ? 0.4157 0.2781 0.4461 0.0030  -0.0096 0.0145  133 MET   C CG  
3492 S  SD  A MET   C 40  ? 0.4463 0.2983 0.4714 0.0016  -0.0108 0.0165  133 MET   C SD  
3493 S  SD  B MET   C 40  ? 0.4237 0.2930 0.4579 -0.0014 -0.0087 0.0150  133 MET   C SD  
3494 C  CE  A MET   C 40  ? 0.4462 0.3017 0.4731 -0.0011 -0.0122 0.0163  133 MET   C CE  
3495 C  CE  B MET   C 40  ? 0.4192 0.2853 0.4518 -0.0030 -0.0118 0.0147  133 MET   C CE  
3496 N  N   . PHE   C 41  ? 0.4161 0.3025 0.4541 0.0074  -0.0042 0.0067  134 PHE   C N   
3497 C  CA  . PHE   C 41  ? 0.4149 0.3095 0.4474 0.0063  -0.0010 0.0061  134 PHE   C CA  
3498 C  C   . PHE   C 41  ? 0.4212 0.3110 0.4482 0.0019  -0.0002 0.0142  134 PHE   C C   
3499 O  O   . PHE   C 41  ? 0.4013 0.2902 0.4317 -0.0016 0.0007  0.0180  134 PHE   C O   
3500 C  CB  . PHE   C 41  ? 0.4141 0.3251 0.4505 0.0066  0.0026  0.0035  134 PHE   C CB  
3501 C  CG  . PHE   C 41  ? 0.4122 0.3279 0.4576 0.0122  0.0024  -0.0050 134 PHE   C CG  
3502 C  CD1 . PHE   C 41  ? 0.4060 0.3184 0.4602 0.0147  0.0000  -0.0042 134 PHE   C CD1 
3503 C  CD2 . PHE   C 41  ? 0.4108 0.3358 0.4571 0.0153  0.0048  -0.0142 134 PHE   C CD2 
3504 C  CE1 . PHE   C 41  ? 0.4061 0.3219 0.4713 0.0212  0.0000  -0.0103 134 PHE   C CE1 
3505 C  CE2 . PHE   C 41  ? 0.4167 0.3441 0.4745 0.0213  0.0054  -0.0232 134 PHE   C CE2 
3506 C  CZ  . PHE   C 41  ? 0.4130 0.3348 0.4812 0.0247  0.0031  -0.0202 134 PHE   C CZ  
3507 N  N   . CYS   C 42  ? 0.4424 0.3299 0.4633 0.0024  -0.0007 0.0164  135 CYS   C N   
3508 C  CA  . CYS   C 42  ? 0.4529 0.3342 0.4711 0.0000  0.0000  0.0250  135 CYS   C CA  
3509 C  C   . CYS   C 42  ? 0.4558 0.3470 0.4676 0.0014  0.0008  0.0293  135 CYS   C C   
3510 O  O   . CYS   C 42  ? 0.4524 0.3537 0.4607 0.0036  -0.0001 0.0226  135 CYS   C O   
3511 C  CB  . CYS   C 42  ? 0.4685 0.3357 0.4876 0.0002  -0.0029 0.0243  135 CYS   C CB  
3512 S  SG  . CYS   C 42  ? 0.4972 0.3623 0.5133 0.0034  -0.0062 0.0190  135 CYS   C SG  
3513 N  N   . GLN   C 43  ? 0.4641 0.3536 0.4756 0.0001  0.0027  0.0400  136 GLN   C N   
3514 C  CA  . GLN   C 43  ? 0.4697 0.3704 0.4754 0.0023  0.0029  0.0479  136 GLN   C CA  
3515 C  C   . GLN   C 43  ? 0.4653 0.3584 0.4703 0.0051  -0.0006 0.0480  136 GLN   C C   
3516 O  O   . GLN   C 43  ? 0.4683 0.3451 0.4783 0.0046  -0.0014 0.0462  136 GLN   C O   
3517 C  CB  . GLN   C 43  ? 0.4803 0.3819 0.4888 0.0003  0.0071  0.0626  136 GLN   C CB  
3518 C  CG  . GLN   C 43  ? 0.4856 0.4002 0.4945 -0.0031 0.0115  0.0643  136 GLN   C CG  
3519 C  CD  . GLN   C 43  ? 0.4926 0.4043 0.5076 -0.0065 0.0164  0.0799  136 GLN   C CD  
3520 O  OE1 . GLN   C 43  ? 0.4916 0.3856 0.5143 -0.0070 0.0169  0.0865  136 GLN   C OE1 
3521 N  NE2 . GLN   C 43  ? 0.5063 0.4362 0.5192 -0.0090 0.0208  0.0860  136 GLN   C NE2 
3522 N  N   . LEU   C 44  ? 0.4737 0.3816 0.4728 0.0079  -0.0024 0.0499  137 LEU   C N   
3523 C  CA  . LEU   C 44  ? 0.4744 0.3814 0.4733 0.0109  -0.0058 0.0509  137 LEU   C CA  
3524 C  C   . LEU   C 44  ? 0.4808 0.3730 0.4866 0.0125  -0.0045 0.0617  137 LEU   C C   
3525 O  O   . LEU   C 44  ? 0.4807 0.3731 0.4891 0.0127  -0.0013 0.0742  137 LEU   C O   
3526 C  CB  . LEU   C 44  ? 0.4820 0.4142 0.4735 0.0132  -0.0076 0.0537  137 LEU   C CB  
3527 C  CG  . LEU   C 44  ? 0.4863 0.4248 0.4777 0.0156  -0.0120 0.0504  137 LEU   C CG  
3528 C  CD1 . LEU   C 44  ? 0.4931 0.4567 0.4778 0.0148  -0.0145 0.0401  137 LEU   C CD1 
3529 C  CD2 . LEU   C 44  ? 0.4923 0.4325 0.4864 0.0203  -0.0126 0.0661  137 LEU   C CD2 
3530 N  N   . ALA   C 45  ? 0.4750 0.3549 0.4852 0.0135  -0.0063 0.0569  138 ALA   C N   
3531 C  CA  . ALA   C 45  ? 0.4912 0.3585 0.5095 0.0162  -0.0052 0.0634  138 ALA   C CA  
3532 C  C   . ALA   C 45  ? 0.4891 0.3398 0.5151 0.0132  -0.0010 0.0652  138 ALA   C C   
3533 O  O   . ALA   C 45  ? 0.5096 0.3481 0.5447 0.0151  0.0006  0.0680  138 ALA   C O   
3534 C  CB  . ALA   C 45  ? 0.5023 0.3810 0.5217 0.0216  -0.0057 0.0768  138 ALA   C CB  
3535 N  N   . LYS   C 46  ? 0.4775 0.3287 0.5017 0.0085  0.0005  0.0623  139 LYS   C N   
3536 C  CA  . LYS   C 46  ? 0.4807 0.3192 0.5133 0.0040  0.0043  0.0621  139 LYS   C CA  
3537 C  C   . LYS   C 46  ? 0.4584 0.2882 0.4925 0.0015  0.0029  0.0493  139 LYS   C C   
3538 O  O   . LYS   C 46  ? 0.4343 0.2692 0.4619 0.0023  -0.0004 0.0421  139 LYS   C O   
3539 C  CB  . LYS   C 46  ? 0.4911 0.3382 0.5220 0.0001  0.0068  0.0654  139 LYS   C CB  
3540 C  CG  . LYS   C 46  ? 0.5169 0.3721 0.5484 0.0012  0.0099  0.0811  139 LYS   C CG  
3541 C  CD  . LYS   C 46  ? 0.5423 0.3825 0.5877 -0.0020 0.0151  0.0897  139 LYS   C CD  
3542 C  CE  . LYS   C 46  ? 0.5615 0.4085 0.6096 -0.0012 0.0191  0.1090  139 LYS   C CE  
3543 N  NZ  . LYS   C 46  ? 0.5805 0.4485 0.6196 -0.0042 0.0205  0.1118  139 LYS   C NZ  
3544 N  N   . THR   C 47  ? 0.4586 0.2769 0.5021 -0.0018 0.0057  0.0467  140 THR   C N   
3545 C  CA  . THR   C 47  ? 0.4557 0.2697 0.5010 -0.0049 0.0048  0.0347  140 THR   C CA  
3546 C  C   . THR   C 47  ? 0.4446 0.2679 0.4838 -0.0076 0.0022  0.0291  140 THR   C C   
3547 O  O   . THR   C 47  ? 0.4359 0.2639 0.4771 -0.0109 0.0037  0.0310  140 THR   C O   
3548 C  CB  . THR   C 47  ? 0.4788 0.2817 0.5370 -0.0093 0.0088  0.0314  140 THR   C CB  
3549 O  OG1 . THR   C 47  ? 0.4819 0.2748 0.5480 -0.0050 0.0114  0.0382  140 THR   C OG1 
3550 C  CG2 . THR   C 47  ? 0.4767 0.2798 0.5359 -0.0126 0.0078  0.0176  140 THR   C CG2 
3551 N  N   A CYS   C 48  ? 0.4380 0.2648 0.4714 -0.0061 -0.0010 0.0234  141 CYS   C N   
3552 N  N   B CYS   C 48  ? 0.4424 0.2691 0.4758 -0.0062 -0.0010 0.0233  141 CYS   C N   
3553 C  CA  A CYS   C 48  ? 0.4316 0.2663 0.4614 -0.0072 -0.0038 0.0191  141 CYS   C CA  
3554 C  CA  B CYS   C 48  ? 0.4386 0.2734 0.4683 -0.0072 -0.0038 0.0192  141 CYS   C CA  
3555 C  C   A CYS   C 48  ? 0.4341 0.2701 0.4647 -0.0096 -0.0050 0.0123  141 CYS   C C   
3556 C  C   B CYS   C 48  ? 0.4382 0.2741 0.4687 -0.0096 -0.0050 0.0123  141 CYS   C C   
3557 O  O   A CYS   C 48  ? 0.4268 0.2635 0.4532 -0.0077 -0.0066 0.0109  141 CYS   C O   
3558 O  O   B CYS   C 48  ? 0.4304 0.2672 0.4568 -0.0076 -0.0067 0.0110  141 CYS   C O   
3559 C  CB  A CYS   C 48  ? 0.4286 0.2670 0.4525 -0.0033 -0.0064 0.0203  141 CYS   C CB  
3560 C  CB  B CYS   C 48  ? 0.4406 0.2788 0.4643 -0.0032 -0.0063 0.0205  141 CYS   C CB  
3561 S  SG  A CYS   C 48  ? 0.4215 0.2652 0.4429 -0.0010 -0.0054 0.0250  141 CYS   C SG  
3562 S  SG  B CYS   C 48  ? 0.4398 0.2866 0.4631 -0.0022 -0.0078 0.0192  141 CYS   C SG  
3563 N  N   . PRO   C 49  ? 0.4374 0.2761 0.4734 -0.0144 -0.0040 0.0074  142 PRO   C N   
3564 C  CA  . PRO   C 49  ? 0.4449 0.2907 0.4806 -0.0171 -0.0056 -0.0005 142 PRO   C CA  
3565 C  C   . PRO   C 49  ? 0.4460 0.3034 0.4752 -0.0147 -0.0099 0.0015  142 PRO   C C   
3566 O  O   . PRO   C 49  ? 0.4633 0.3257 0.4936 -0.0135 -0.0113 0.0049  142 PRO   C O   
3567 C  CB  . PRO   C 49  ? 0.4489 0.2971 0.4936 -0.0237 -0.0036 -0.0066 142 PRO   C CB  
3568 C  CG  . PRO   C 49  ? 0.4526 0.2894 0.5038 -0.0242 0.0004  -0.0002 142 PRO   C CG  
3569 C  CD  . PRO   C 49  ? 0.4489 0.2870 0.4922 -0.0184 -0.0011 0.0088  142 PRO   C CD  
3570 N  N   . VAL   C 50  ? 0.4530 0.3147 0.4769 -0.0134 -0.0115 0.0005  143 VAL   C N   
3571 C  CA  . VAL   C 50  ? 0.4585 0.3321 0.4778 -0.0113 -0.0154 0.0045  143 VAL   C CA  
3572 C  C   . VAL   C 50  ? 0.4579 0.3458 0.4746 -0.0148 -0.0163 -0.0021 143 VAL   C C   
3573 O  O   . VAL   C 50  ? 0.4591 0.3450 0.4742 -0.0161 -0.0140 -0.0074 143 VAL   C O   
3574 C  CB  . VAL   C 50  ? 0.4605 0.3283 0.4761 -0.0071 -0.0159 0.0118  143 VAL   C CB  
3575 C  CG1 . VAL   C 50  ? 0.4615 0.3398 0.4746 -0.0050 -0.0190 0.0183  143 VAL   C CG1 
3576 C  CG2 . VAL   C 50  ? 0.4554 0.3131 0.4738 -0.0043 -0.0151 0.0152  143 VAL   C CG2 
3577 N  N   . GLN   C 51  ? 0.4561 0.3606 0.4732 -0.0162 -0.0196 -0.0028 144 GLN   C N   
3578 C  CA  . GLN   C 51  ? 0.4570 0.3821 0.4705 -0.0198 -0.0215 -0.0097 144 GLN   C CA  
3579 C  C   . GLN   C 51  ? 0.4540 0.3917 0.4593 -0.0159 -0.0244 0.0003  144 GLN   C C   
3580 O  O   . GLN   C 51  ? 0.4414 0.3776 0.4479 -0.0108 -0.0268 0.0122  144 GLN   C O   
3581 C  CB  . GLN   C 51  ? 0.4632 0.4037 0.4823 -0.0236 -0.0240 -0.0153 144 GLN   C CB  
3582 C  CG  . GLN   C 51  ? 0.4666 0.3945 0.4957 -0.0286 -0.0202 -0.0235 144 GLN   C CG  
3583 C  CD  . GLN   C 51  ? 0.4719 0.4157 0.5081 -0.0326 -0.0226 -0.0273 144 GLN   C CD  
3584 O  OE1 . GLN   C 51  ? 0.4691 0.4314 0.5032 -0.0294 -0.0274 -0.0216 144 GLN   C OE1 
3585 N  NE2 . GLN   C 51  ? 0.4750 0.4120 0.5216 -0.0394 -0.0189 -0.0361 144 GLN   C NE2 
3586 N  N   . LEU   C 52  ? 0.4552 0.4048 0.4539 -0.0181 -0.0235 -0.0044 145 LEU   C N   
3587 C  CA  . LEU   C 52  ? 0.4676 0.4365 0.4577 -0.0160 -0.0260 0.0052  145 LEU   C CA  
3588 C  C   . LEU   C 52  ? 0.4818 0.4820 0.4683 -0.0192 -0.0299 -0.0004 145 LEU   C C   
3589 O  O   . LEU   C 52  ? 0.4750 0.4842 0.4616 -0.0251 -0.0282 -0.0175 145 LEU   C O   
3590 C  CB  . LEU   C 52  ? 0.4611 0.4284 0.4457 -0.0169 -0.0220 0.0031  145 LEU   C CB  
3591 C  CG  . LEU   C 52  ? 0.4569 0.3971 0.4460 -0.0151 -0.0180 0.0040  145 LEU   C CG  
3592 C  CD1 . LEU   C 52  ? 0.4574 0.4018 0.4420 -0.0156 -0.0144 0.0029  145 LEU   C CD1 
3593 C  CD2 . LEU   C 52  ? 0.4497 0.3745 0.4427 -0.0106 -0.0194 0.0177  145 LEU   C CD2 
3594 N  N   . TRP   C 53  ? 0.5016 0.5184 0.4867 -0.0152 -0.0349 0.0128  146 TRP   C N   
3595 C  CA  . TRP   C 53  ? 0.5265 0.5797 0.5072 -0.0172 -0.0400 0.0105  146 TRP   C CA  
3596 C  C   . TRP   C 53  ? 0.5420 0.6166 0.5122 -0.0139 -0.0418 0.0259  146 TRP   C C   
3597 O  O   . TRP   C 53  ? 0.5464 0.6085 0.5188 -0.0076 -0.0420 0.0452  146 TRP   C O   
3598 C  CB  . TRP   C 53  ? 0.5305 0.5904 0.5198 -0.0144 -0.0448 0.0150  146 TRP   C CB  
3599 C  CG  . TRP   C 53  ? 0.5341 0.5790 0.5335 -0.0190 -0.0427 0.0005  146 TRP   C CG  
3600 C  CD1 . TRP   C 53  ? 0.5249 0.5374 0.5309 -0.0183 -0.0382 -0.0002 146 TRP   C CD1 
3601 C  CD2 . TRP   C 53  ? 0.5385 0.6024 0.5436 -0.0256 -0.0448 -0.0140 146 TRP   C CD2 
3602 N  NE1 . TRP   C 53  ? 0.5291 0.5384 0.5440 -0.0238 -0.0369 -0.0125 146 TRP   C NE1 
3603 C  CE2 . TRP   C 53  ? 0.5397 0.5788 0.5554 -0.0288 -0.0406 -0.0218 146 TRP   C CE2 
3604 C  CE3 . TRP   C 53  ? 0.5549 0.6567 0.5579 -0.0295 -0.0499 -0.0211 146 TRP   C CE3 
3605 C  CZ2 . TRP   C 53  ? 0.5455 0.5932 0.5709 -0.0365 -0.0405 -0.0360 146 TRP   C CZ2 
3606 C  CZ3 . TRP   C 53  ? 0.5597 0.6715 0.5724 -0.0374 -0.0503 -0.0377 146 TRP   C CZ3 
3607 C  CH2 . TRP   C 53  ? 0.5518 0.6354 0.5764 -0.0410 -0.0454 -0.0445 146 TRP   C CH2 
3608 N  N   . VAL   C 54  ? 0.5584 0.6650 0.5187 -0.0185 -0.0426 0.0173  147 VAL   C N   
3609 C  CA  . VAL   C 54  ? 0.5747 0.7105 0.5230 -0.0164 -0.0443 0.0323  147 VAL   C CA  
3610 C  C   . VAL   C 54  ? 0.5886 0.7704 0.5304 -0.0189 -0.0504 0.0272  147 VAL   C C   
3611 O  O   . VAL   C 54  ? 0.5871 0.7779 0.5317 -0.0256 -0.0508 0.0036  147 VAL   C O   
3612 C  CB  . VAL   C 54  ? 0.5773 0.7117 0.5174 -0.0199 -0.0380 0.0263  147 VAL   C CB  
3613 C  CG1 . VAL   C 54  ? 0.5770 0.6737 0.5229 -0.0166 -0.0332 0.0366  147 VAL   C CG1 
3614 C  CG2 . VAL   C 54  ? 0.5764 0.7143 0.5166 -0.0272 -0.0345 -0.0028 147 VAL   C CG2 
3615 N  N   . ASP   C 55  ? 0.5994 0.8091 0.5345 -0.0137 -0.0550 0.0492  148 ASP   C N   
3616 C  CA  . ASP   C 55  ? 0.6262 0.8883 0.5526 -0.0151 -0.0617 0.0485  148 ASP   C CA  
3617 C  C   . ASP   C 55  ? 0.6402 0.9324 0.5513 -0.0220 -0.0585 0.0347  148 ASP   C C   
3618 O  O   . ASP   C 55  ? 0.6543 0.9862 0.5592 -0.0276 -0.0620 0.0175  148 ASP   C O   
3619 C  CB  . ASP   C 55  ? 0.6327 0.9135 0.5584 -0.0056 -0.0674 0.0808  148 ASP   C CB  
3620 C  CG  . ASP   C 55  ? 0.6221 0.8817 0.5644 0.0020  -0.0712 0.0920  148 ASP   C CG  
3621 O  OD1 . ASP   C 55  ? 0.6117 0.8591 0.5632 -0.0014 -0.0716 0.0728  148 ASP   C OD1 
3622 O  OD2 . ASP   C 55  ? 0.6247 0.8811 0.5720 0.0114  -0.0733 0.1199  148 ASP   C OD2 
3623 N  N   . SER   C 56  ? 0.6509 0.9266 0.5570 -0.0219 -0.0518 0.0406  149 SER   C N   
3624 C  CA  . SER   C 56  ? 0.6662 0.9685 0.5587 -0.0277 -0.0471 0.0279  149 SER   C CA  
3625 C  C   . SER   C 56  ? 0.6593 0.9224 0.5569 -0.0297 -0.0383 0.0172  149 SER   C C   
3626 O  O   . SER   C 56  ? 0.6577 0.8821 0.5639 -0.0251 -0.0361 0.0328  149 SER   C O   
3627 C  CB  . SER   C 56  ? 0.6871 1.0265 0.5656 -0.0246 -0.0487 0.0536  149 SER   C CB  
3628 O  OG  . SER   C 56  ? 0.7012 1.0804 0.5755 -0.0220 -0.0576 0.0633  149 SER   C OG  
3629 N  N   . THR   C 57  ? 0.6557 0.9307 0.5494 -0.0361 -0.0334 -0.0094 150 THR   C N   
3630 C  CA  . THR   C 57  ? 0.6454 0.8885 0.5453 -0.0377 -0.0251 -0.0234 150 THR   C CA  
3631 C  C   . THR   C 57  ? 0.6435 0.8849 0.5372 -0.0348 -0.0205 -0.0028 150 THR   C C   
3632 O  O   . THR   C 57  ? 0.6431 0.9226 0.5234 -0.0366 -0.0190 0.0014  150 THR   C O   
3633 C  CB  . THR   C 57  ? 0.6551 0.9169 0.5542 -0.0445 -0.0210 -0.0575 150 THR   C CB  
3634 O  OG1 . THR   C 57  ? 0.6575 0.9250 0.5634 -0.0484 -0.0257 -0.0743 150 THR   C OG1 
3635 C  CG2 . THR   C 57  ? 0.6495 0.8765 0.5594 -0.0447 -0.0129 -0.0728 150 THR   C CG2 
3636 N  N   . PRO   C 58  ? 0.6268 0.8265 0.5303 -0.0311 -0.0179 0.0103  151 PRO   C N   
3637 C  CA  . PRO   C 58  ? 0.6260 0.8216 0.5268 -0.0301 -0.0125 0.0261  151 PRO   C CA  
3638 C  C   . PRO   C 58  ? 0.6192 0.8319 0.5149 -0.0341 -0.0053 0.0068  151 PRO   C C   
3639 O  O   . PRO   C 58  ? 0.6195 0.8324 0.5188 -0.0366 -0.0034 -0.0208 151 PRO   C O   
3640 C  CB  . PRO   C 58  ? 0.6098 0.7561 0.5251 -0.0268 -0.0113 0.0326  151 PRO   C CB  
3641 C  CG  . PRO   C 58  ? 0.6107 0.7411 0.5334 -0.0243 -0.0175 0.0318  151 PRO   C CG  
3642 C  CD  . PRO   C 58  ? 0.6162 0.7738 0.5340 -0.0283 -0.0199 0.0100  151 PRO   C CD  
3643 N  N   . PRO   C 59  ? 0.6183 0.8458 0.5075 -0.0347 -0.0003 0.0204  152 PRO   C N   
3644 C  CA  . PRO   C 59  ? 0.6220 0.8711 0.5064 -0.0381 0.0071  0.0022  152 PRO   C CA  
3645 C  C   . PRO   C 59  ? 0.6043 0.8185 0.5032 -0.0370 0.0122  -0.0169 152 PRO   C C   
3646 O  O   . PRO   C 59  ? 0.5842 0.7582 0.4950 -0.0339 0.0107  -0.0095 152 PRO   C O   
3647 C  CB  . PRO   C 59  ? 0.6316 0.9005 0.5080 -0.0389 0.0109  0.0278  152 PRO   C CB  
3648 C  CG  . PRO   C 59  ? 0.6310 0.8664 0.5163 -0.0355 0.0073  0.0560  152 PRO   C CG  
3649 C  CD  . PRO   C 59  ? 0.6255 0.8499 0.5137 -0.0326 -0.0009 0.0537  152 PRO   C CD  
3650 N  N   . PRO   C 60  ? 0.6080 0.8380 0.5073 -0.0388 0.0185  -0.0422 153 PRO   C N   
3651 C  CA  . PRO   C 60  ? 0.6017 0.8016 0.5161 -0.0364 0.0239  -0.0574 153 PRO   C CA  
3652 C  C   . PRO   C 60  ? 0.5859 0.7652 0.5058 -0.0342 0.0264  -0.0361 153 PRO   C C   
3653 O  O   . PRO   C 60  ? 0.5840 0.7841 0.4951 -0.0362 0.0280  -0.0172 153 PRO   C O   
3654 C  CB  . PRO   C 60  ? 0.6169 0.8485 0.5288 -0.0384 0.0312  -0.0833 153 PRO   C CB  
3655 C  CG  . PRO   C 60  ? 0.6338 0.9078 0.5305 -0.0428 0.0279  -0.0906 153 PRO   C CG  
3656 C  CD  . PRO   C 60  ? 0.6332 0.9126 0.5192 -0.0428 0.0209  -0.0579 153 PRO   C CD  
3657 N  N   . GLY   C 61  ? 0.5733 0.7139 0.5082 -0.0306 0.0266  -0.0389 154 GLY   C N   
3658 C  CA  . GLY   C 61  ? 0.5553 0.6755 0.4978 -0.0291 0.0284  -0.0225 154 GLY   C CA  
3659 C  C   . GLY   C 61  ? 0.5448 0.6418 0.4885 -0.0286 0.0223  0.0000  154 GLY   C C   
3660 O  O   . GLY   C 61  ? 0.5526 0.6311 0.5043 -0.0281 0.0233  0.0117  154 GLY   C O   
3661 N  N   . THR   C 62  ? 0.5309 0.6299 0.4688 -0.0288 0.0164  0.0042  155 THR   C N   
3662 C  CA  . THR   C 62  ? 0.5201 0.5938 0.4623 -0.0268 0.0104  0.0209  155 THR   C CA  
3663 C  C   . THR   C 62  ? 0.5042 0.5414 0.4596 -0.0238 0.0100  0.0137  155 THR   C C   
3664 O  O   . THR   C 62  ? 0.4848 0.5157 0.4451 -0.0226 0.0116  -0.0055 155 THR   C O   
3665 C  CB  . THR   C 62  ? 0.5237 0.6077 0.4596 -0.0266 0.0043  0.0213  155 THR   C CB  
3666 O  OG1 . THR   C 62  ? 0.5323 0.6541 0.4551 -0.0289 0.0043  0.0310  155 THR   C OG1 
3667 C  CG2 . THR   C 62  ? 0.5141 0.5733 0.4563 -0.0236 -0.0011 0.0366  155 THR   C CG2 
3668 N  N   . ARG   C 63  ? 0.4907 0.5055 0.4528 -0.0227 0.0081  0.0288  156 ARG   C N   
3669 C  CA  . ARG   C 63  ? 0.4788 0.4633 0.4522 -0.0200 0.0074  0.0240  156 ARG   C CA  
3670 C  C   . ARG   C 63  ? 0.4725 0.4378 0.4490 -0.0182 0.0020  0.0328  156 ARG   C C   
3671 O  O   . ARG   C 63  ? 0.4821 0.4541 0.4552 -0.0186 -0.0003 0.0469  156 ARG   C O   
3672 C  CB  . ARG   C 63  ? 0.4773 0.4579 0.4573 -0.0210 0.0114  0.0284  156 ARG   C CB  
3673 C  CG  . ARG   C 63  ? 0.4788 0.4707 0.4609 -0.0203 0.0166  0.0134  156 ARG   C CG  
3674 C  CD  . ARG   C 63  ? 0.4817 0.4865 0.4663 -0.0231 0.0216  0.0198  156 ARG   C CD  
3675 N  NE  . ARG   C 63  ? 0.4809 0.4690 0.4750 -0.0243 0.0208  0.0305  156 ARG   C NE  
3676 C  CZ  . ARG   C 63  ? 0.4661 0.4436 0.4707 -0.0223 0.0214  0.0246  156 ARG   C CZ  
3677 N  NH1 . ARG   C 63  ? 0.4677 0.4458 0.4760 -0.0177 0.0229  0.0099  156 ARG   C NH1 
3678 N  NH2 . ARG   C 63  ? 0.4675 0.4341 0.4802 -0.0249 0.0205  0.0332  156 ARG   C NH2 
3679 N  N   . VAL   C 64  ? 0.4682 0.4119 0.4517 -0.0157 0.0006  0.0251  157 VAL   C N   
3680 C  CA  . VAL   C 64  ? 0.4501 0.3754 0.4379 -0.0137 -0.0036 0.0306  157 VAL   C CA  
3681 C  C   . VAL   C 64  ? 0.4379 0.3439 0.4343 -0.0125 -0.0030 0.0318  157 VAL   C C   
3682 O  O   . VAL   C 64  ? 0.4354 0.3351 0.4352 -0.0111 -0.0015 0.0224  157 VAL   C O   
3683 C  CB  . VAL   C 64  ? 0.4522 0.3746 0.4398 -0.0126 -0.0057 0.0198  157 VAL   C CB  
3684 C  CG1 . VAL   C 64  ? 0.4458 0.3559 0.4368 -0.0107 -0.0097 0.0262  157 VAL   C CG1 
3685 C  CG2 . VAL   C 64  ? 0.4642 0.4100 0.4442 -0.0149 -0.0059 0.0136  157 VAL   C CG2 
3686 N  N   . ARG   C 65  ? 0.4259 0.3240 0.4265 -0.0130 -0.0040 0.0429  158 ARG   C N   
3687 C  CA  . ARG   C 65  ? 0.4126 0.2952 0.4218 -0.0130 -0.0039 0.0431  158 ARG   C CA  
3688 C  C   . ARG   C 65  ? 0.4066 0.2753 0.4193 -0.0103 -0.0073 0.0432  158 ARG   C C   
3689 O  O   . ARG   C 65  ? 0.4004 0.2706 0.4121 -0.0090 -0.0093 0.0494  158 ARG   C O   
3690 C  CB  . ARG   C 65  ? 0.4166 0.3008 0.4311 -0.0166 -0.0017 0.0533  158 ARG   C CB  
3691 C  CG  . ARG   C 65  ? 0.4104 0.2822 0.4353 -0.0182 -0.0014 0.0512  158 ARG   C CG  
3692 C  CD  . ARG   C 65  ? 0.4128 0.2858 0.4455 -0.0234 0.0014  0.0611  158 ARG   C CD  
3693 N  NE  . ARG   C 65  ? 0.4197 0.3106 0.4478 -0.0263 0.0051  0.0644  158 ARG   C NE  
3694 C  CZ  . ARG   C 65  ? 0.4106 0.3109 0.4402 -0.0280 0.0078  0.0577  158 ARG   C CZ  
3695 N  NH1 . ARG   C 65  ? 0.4064 0.3006 0.4414 -0.0268 0.0064  0.0480  158 ARG   C NH1 
3696 N  NH2 . ARG   C 65  ? 0.4206 0.3394 0.4462 -0.0305 0.0119  0.0608  158 ARG   C NH2 
3697 N  N   . ALA   C 66  ? 0.4015 0.2606 0.4183 -0.0091 -0.0078 0.0366  159 ALA   C N   
3698 C  CA  . ALA   C 66  ? 0.4095 0.2576 0.4305 -0.0071 -0.0099 0.0351  159 ALA   C CA  
3699 C  C   . ALA   C 66  ? 0.4091 0.2513 0.4379 -0.0090 -0.0094 0.0340  159 ALA   C C   
3700 O  O   . ALA   C 66  ? 0.4133 0.2600 0.4432 -0.0106 -0.0082 0.0308  159 ALA   C O   
3701 C  CB  . ALA   C 66  ? 0.3988 0.2453 0.4168 -0.0047 -0.0107 0.0281  159 ALA   C CB  
3702 N  N   . MET   C 67  ? 0.4225 0.2563 0.4584 -0.0088 -0.0101 0.0355  160 MET   C N   
3703 C  CA  . MET   C 67  ? 0.4276 0.2554 0.4736 -0.0116 -0.0095 0.0316  160 MET   C CA  
3704 C  C   . MET   C 67  ? 0.4237 0.2438 0.4749 -0.0089 -0.0106 0.0267  160 MET   C C   
3705 O  O   . MET   C 67  ? 0.4257 0.2422 0.4777 -0.0056 -0.0112 0.0317  160 MET   C O   
3706 C  CB  . MET   C 67  ? 0.4547 0.2796 0.5094 -0.0159 -0.0071 0.0396  160 MET   C CB  
3707 C  CG  . MET   C 67  ? 0.4713 0.2890 0.5397 -0.0202 -0.0059 0.0341  160 MET   C CG  
3708 S  SD  . MET   C 67  ? 0.5274 0.3377 0.6105 -0.0263 -0.0020 0.0457  160 MET   C SD  
3709 C  CE  . MET   C 67  ? 0.5163 0.3434 0.5909 -0.0301 0.0000  0.0516  160 MET   C CE  
3710 N  N   . ALA   C 68  ? 0.4140 0.2347 0.4685 -0.0098 -0.0110 0.0168  161 ALA   C N   
3711 C  CA  . ALA   C 68  ? 0.4173 0.2338 0.4775 -0.0077 -0.0114 0.0091  161 ALA   C CA  
3712 C  C   . ALA   C 68  ? 0.4358 0.2433 0.5120 -0.0114 -0.0096 0.0052  161 ALA   C C   
3713 O  O   . ALA   C 68  ? 0.4232 0.2324 0.5041 -0.0169 -0.0087 0.0039  161 ALA   C O   
3714 C  CB  . ALA   C 68  ? 0.4130 0.2397 0.4668 -0.0069 -0.0126 0.0001  161 ALA   C CB  
3715 N  N   . ILE   C 69  ? 0.4600 0.2579 0.5461 -0.0084 -0.0086 0.0037  162 ILE   C N   
3716 C  CA  . ILE   C 69  ? 0.4906 0.2776 0.5957 -0.0112 -0.0063 -0.0043 162 ILE   C CA  
3717 C  C   . ILE   C 69  ? 0.4902 0.2783 0.5989 -0.0067 -0.0061 -0.0169 162 ILE   C C   
3718 O  O   . ILE   C 69  ? 0.4880 0.2820 0.5866 -0.0013 -0.0075 -0.0137 162 ILE   C O   
3719 C  CB  . ILE   C 69  ? 0.5060 0.2780 0.6249 -0.0113 -0.0040 0.0090  162 ILE   C CB  
3720 C  CG1 . ILE   C 69  ? 0.5223 0.2905 0.6409 -0.0032 -0.0048 0.0193  162 ILE   C CG1 
3721 C  CG2 . ILE   C 69  ? 0.5046 0.2801 0.6185 -0.0164 -0.0035 0.0209  162 ILE   C CG2 
3722 C  CD1 . ILE   C 69  ? 0.5408 0.2950 0.6755 -0.0019 -0.0027 0.0339  162 ILE   C CD1 
3723 N  N   . TYR   C 70  ? 0.5020 0.2863 0.6252 -0.0097 -0.0042 -0.0319 163 TYR   C N   
3724 C  CA  . TYR   C 70  ? 0.5143 0.2994 0.6452 -0.0055 -0.0027 -0.0464 163 TYR   C CA  
3725 C  C   . TYR   C 70  ? 0.5244 0.2927 0.6701 0.0008  -0.0008 -0.0378 163 TYR   C C   
3726 O  O   . TYR   C 70  ? 0.5279 0.2809 0.6857 -0.0006 0.0005  -0.0261 163 TYR   C O   
3727 C  CB  . TYR   C 70  ? 0.5215 0.3100 0.6642 -0.0115 -0.0011 -0.0674 163 TYR   C CB  
3728 C  CG  . TYR   C 70  ? 0.5117 0.3235 0.6383 -0.0155 -0.0039 -0.0758 163 TYR   C CG  
3729 C  CD1 . TYR   C 70  ? 0.5007 0.3306 0.6107 -0.0112 -0.0055 -0.0784 163 TYR   C CD1 
3730 C  CD2 . TYR   C 70  ? 0.5100 0.3274 0.6383 -0.0234 -0.0049 -0.0790 163 TYR   C CD2 
3731 C  CE1 . TYR   C 70  ? 0.4880 0.3405 0.5837 -0.0138 -0.0082 -0.0829 163 TYR   C CE1 
3732 C  CE2 . TYR   C 70  ? 0.4959 0.3372 0.6101 -0.0257 -0.0081 -0.0848 163 TYR   C CE2 
3733 C  CZ  . TYR   C 70  ? 0.4880 0.3467 0.5858 -0.0205 -0.0098 -0.0858 163 TYR   C CZ  
3734 O  OH  . TYR   C 70  ? 0.4761 0.3595 0.5605 -0.0216 -0.0130 -0.0885 163 TYR   C OH  
3735 N  N   . LYS   C 71  ? 0.5328 0.3061 0.6775 0.0080  -0.0006 -0.0417 164 LYS   C N   
3736 C  CA  . LYS   C 71  ? 0.5482 0.3104 0.7059 0.0162  0.0003  -0.0323 164 LYS   C CA  
3737 C  C   . LYS   C 71  ? 0.5782 0.3230 0.7641 0.0174  0.0046  -0.0429 164 LYS   C C   
3738 O  O   . LYS   C 71  ? 0.6059 0.3342 0.8083 0.0216  0.0058  -0.0295 164 LYS   C O   
3739 C  CB  . LYS   C 71  ? 0.5330 0.3097 0.6812 0.0228  -0.0005 -0.0347 164 LYS   C CB  
3740 C  CG  . LYS   C 71  ? 0.5467 0.3177 0.7066 0.0321  -0.0005 -0.0239 164 LYS   C CG  
3741 C  CD  . LYS   C 71  ? 0.5332 0.3200 0.6883 0.0377  -0.0003 -0.0306 164 LYS   C CD  
3742 C  CE  . LYS   C 71  ? 0.5448 0.3297 0.7122 0.0472  -0.0009 -0.0195 164 LYS   C CE  
3743 N  NZ  . LYS   C 71  ? 0.5384 0.3401 0.7048 0.0524  0.0000  -0.0285 164 LYS   C NZ  
3744 N  N   . GLN   C 72  ? 0.5956 0.3455 0.7872 0.0139  0.0069  -0.0662 165 GLN   C N   
3745 C  CA  . GLN   C 72  ? 0.6200 0.3553 0.8402 0.0148  0.0117  -0.0833 165 GLN   C CA  
3746 C  C   . GLN   C 72  ? 0.6430 0.3579 0.8812 0.0073  0.0138  -0.0792 165 GLN   C C   
3747 O  O   . GLN   C 72  ? 0.6446 0.3666 0.8707 -0.0016 0.0118  -0.0774 165 GLN   C O   
3748 C  CB  . GLN   C 72  ? 0.6219 0.3756 0.8390 0.0119  0.0132  -0.1114 165 GLN   C CB  
3749 C  CG  . GLN   C 72  ? 0.6203 0.3940 0.8241 0.0194  0.0128  -0.1158 165 GLN   C CG  
3750 C  CD  . GLN   C 72  ? 0.6243 0.4248 0.8137 0.0147  0.0127  -0.1365 165 GLN   C CD  
3751 O  OE1 . GLN   C 72  ? 0.6393 0.4521 0.8124 0.0073  0.0097  -0.1359 165 GLN   C OE1 
3752 N  NE2 . GLN   C 72  ? 0.6391 0.4520 0.8344 0.0195  0.0162  -0.1545 165 GLN   C NE2 
3753 N  N   . SER   C 73  ? 0.6802 0.3711 0.9484 0.0108  0.0181  -0.0778 166 SER   C N   
3754 C  CA  A SER   C 73  ? 0.6985 0.3661 0.9886 0.0041  0.0212  -0.0691 166 SER   C CA  
3755 C  CA  B SER   C 73  ? 0.6983 0.3660 0.9882 0.0041  0.0211  -0.0691 166 SER   C CA  
3756 C  C   . SER   C 73  ? 0.7096 0.3797 1.0070 -0.0085 0.0231  -0.0930 166 SER   C C   
3757 O  O   . SER   C 73  ? 0.7200 0.3824 1.0224 -0.0178 0.0238  -0.0842 166 SER   C O   
3758 C  CB  A SER   C 73  ? 0.7209 0.3619 1.0439 0.0121  0.0257  -0.0621 166 SER   C CB  
3759 C  CB  B SER   C 73  ? 0.7198 0.3608 1.0424 0.0120  0.0257  -0.0614 166 SER   C CB  
3760 O  OG  A SER   C 73  ? 0.7310 0.3695 1.0725 0.0167  0.0295  -0.0885 166 SER   C OG  
3761 O  OG  B SER   C 73  ? 0.7155 0.3500 1.0345 0.0170  0.0237  -0.0287 166 SER   C OG  
3762 N  N   . GLN   C 74  ? 0.7149 0.3990 1.0126 -0.0091 0.0240  -0.1218 167 GLN   C N   
3763 C  CA  . GLN   C 74  ? 0.7233 0.4150 1.0293 -0.0211 0.0255  -0.1487 167 GLN   C CA  
3764 C  C   . GLN   C 74  ? 0.6990 0.4178 0.9750 -0.0288 0.0200  -0.1470 167 GLN   C C   
3765 O  O   . GLN   C 74  ? 0.7128 0.4404 0.9946 -0.0397 0.0202  -0.1646 167 GLN   C O   
3766 C  CB  . GLN   C 74  ? 0.7407 0.4414 1.0581 -0.0187 0.0286  -0.1812 167 GLN   C CB  
3767 C  CG  . GLN   C 74  ? 0.7256 0.4570 1.0144 -0.0119 0.0252  -0.1870 167 GLN   C CG  
3768 C  CD  . GLN   C 74  ? 0.7328 0.4574 1.0253 0.0019  0.0268  -0.1782 167 GLN   C CD  
3769 O  OE1 . GLN   C 74  ? 0.7442 0.4474 1.0456 0.0082  0.0271  -0.1544 167 GLN   C OE1 
3770 N  NE2 . GLN   C 74  ? 0.7286 0.4744 1.0147 0.0067  0.0280  -0.1975 167 GLN   C NE2 
3771 N  N   . HIS   C 75  ? 0.6827 0.4147 0.9300 -0.0234 0.0153  -0.1272 168 HIS   C N   
3772 C  CA  . HIS   C 75  ? 0.6579 0.4151 0.8777 -0.0284 0.0102  -0.1238 168 HIS   C CA  
3773 C  C   . HIS   C 75  ? 0.6431 0.3935 0.8529 -0.0294 0.0083  -0.0963 168 HIS   C C   
3774 O  O   . HIS   C 75  ? 0.6413 0.4100 0.8309 -0.0326 0.0045  -0.0919 168 HIS   C O   
3775 C  CB  . HIS   C 75  ? 0.6451 0.4264 0.8401 -0.0216 0.0071  -0.1272 168 HIS   C CB  
3776 C  CG  . HIS   C 75  ? 0.6597 0.4562 0.8599 -0.0215 0.0089  -0.1548 168 HIS   C CG  
3777 N  ND1 . HIS   C 75  ? 0.6638 0.4747 0.8703 -0.0306 0.0091  -0.1781 168 HIS   C ND1 
3778 C  CD2 . HIS   C 75  ? 0.6625 0.4659 0.8618 -0.0137 0.0108  -0.1639 168 HIS   C CD2 
3779 C  CE1 . HIS   C 75  ? 0.6766 0.5030 0.8853 -0.0283 0.0110  -0.2010 168 HIS   C CE1 
3780 N  NE2 . HIS   C 75  ? 0.6752 0.4970 0.8796 -0.0178 0.0124  -0.1924 168 HIS   C NE2 
3781 N  N   . MET   C 76  ? 0.6476 0.3743 0.8718 -0.0265 0.0109  -0.0787 169 MET   C N   
3782 C  CA  . MET   C 76  ? 0.6370 0.3608 0.8489 -0.0247 0.0092  -0.0510 169 MET   C CA  
3783 C  C   . MET   C 76  ? 0.6181 0.3458 0.8289 -0.0352 0.0092  -0.0460 169 MET   C C   
3784 O  O   . MET   C 76  ? 0.5892 0.3265 0.7813 -0.0347 0.0068  -0.0300 169 MET   C O   
3785 C  CB  . MET   C 76  ? 0.6674 0.3686 0.8965 -0.0184 0.0120  -0.0331 169 MET   C CB  
3786 C  CG  . MET   C 76  ? 0.6712 0.3773 0.8824 -0.0136 0.0092  -0.0072 169 MET   C CG  
3787 S  SD  . MET   C 76  ? 0.7072 0.4076 0.9204 0.0000  0.0082  0.0086  169 MET   C SD  
3788 C  CE  . MET   C 76  ? 0.7162 0.3908 0.9671 0.0039  0.0136  -0.0001 169 MET   C CE  
3789 N  N   . THR   C 77  ? 0.6200 0.3417 0.8516 -0.0448 0.0123  -0.0604 170 THR   C N   
3790 C  CA  . THR   C 77  ? 0.6163 0.3433 0.8515 -0.0562 0.0130  -0.0581 170 THR   C CA  
3791 C  C   . THR   C 77  ? 0.5939 0.3502 0.8094 -0.0596 0.0083  -0.0712 170 THR   C C   
3792 O  O   . THR   C 77  ? 0.5935 0.3593 0.8089 -0.0676 0.0081  -0.0686 170 THR   C O   
3793 C  CB  . THR   C 77  ? 0.6443 0.3541 0.9126 -0.0664 0.0184  -0.0699 170 THR   C CB  
3794 O  OG1 . THR   C 77  ? 0.6503 0.3713 0.9241 -0.0696 0.0175  -0.1002 170 THR   C OG1 
3795 C  CG2 . THR   C 77  ? 0.6650 0.3439 0.9576 -0.0623 0.0235  -0.0577 170 THR   C CG2 
3796 N  N   . GLU   C 78  ? 0.5765 0.3480 0.7774 -0.0535 0.0050  -0.0838 171 GLU   C N   
3797 C  CA  . GLU   C 78  ? 0.5563 0.3574 0.7374 -0.0547 0.0002  -0.0926 171 GLU   C CA  
3798 C  C   . GLU   C 78  ? 0.5241 0.3327 0.6814 -0.0483 -0.0027 -0.0720 171 GLU   C C   
3799 O  O   . GLU   C 78  ? 0.5069 0.3061 0.6563 -0.0402 -0.0026 -0.0602 171 GLU   C O   
3800 C  CB  . GLU   C 78  ? 0.5616 0.3772 0.7376 -0.0512 -0.0012 -0.1128 171 GLU   C CB  
3801 C  CG  . GLU   C 78  ? 0.5608 0.4089 0.7184 -0.0523 -0.0062 -0.1203 171 GLU   C CG  
3802 C  CD  . GLU   C 78  ? 0.5673 0.4362 0.7216 -0.0514 -0.0073 -0.1424 171 GLU   C CD  
3803 O  OE1 . GLU   C 78  ? 0.5885 0.4533 0.7623 -0.0567 -0.0044 -0.1634 171 GLU   C OE1 
3804 O  OE2 . GLU   C 78  ? 0.5552 0.4451 0.6882 -0.0457 -0.0107 -0.1389 171 GLU   C OE2 
3805 N  N   . VAL   C 79  ? 0.5043 0.3302 0.6525 -0.0519 -0.0051 -0.0689 172 VAL   C N   
3806 C  CA  . VAL   C 79  ? 0.4824 0.3169 0.6101 -0.0460 -0.0076 -0.0526 172 VAL   C CA  
3807 C  C   . VAL   C 79  ? 0.4679 0.3158 0.5780 -0.0384 -0.0109 -0.0563 172 VAL   C C   
3808 O  O   . VAL   C 79  ? 0.4602 0.3260 0.5692 -0.0401 -0.0131 -0.0708 172 VAL   C O   
3809 C  CB  . VAL   C 79  ? 0.4732 0.3233 0.5994 -0.0511 -0.0087 -0.0497 172 VAL   C CB  
3810 C  CG1 . VAL   C 79  ? 0.4541 0.3131 0.5613 -0.0440 -0.0108 -0.0365 172 VAL   C CG1 
3811 C  CG2 . VAL   C 79  ? 0.4759 0.3144 0.6193 -0.0595 -0.0045 -0.0439 172 VAL   C CG2 
3812 N  N   . VAL   C 80  ? 0.4635 0.3056 0.5609 -0.0310 -0.0113 -0.0433 173 VAL   C N   
3813 C  CA  . VAL   C 80  ? 0.4544 0.3085 0.5358 -0.0244 -0.0137 -0.0436 173 VAL   C CA  
3814 C  C   . VAL   C 80  ? 0.4483 0.3196 0.5188 -0.0235 -0.0165 -0.0386 173 VAL   C C   
3815 O  O   . VAL   C 80  ? 0.4398 0.3067 0.5075 -0.0228 -0.0159 -0.0272 173 VAL   C O   
3816 C  CB  . VAL   C 80  ? 0.4447 0.2869 0.5193 -0.0179 -0.0128 -0.0329 173 VAL   C CB  
3817 C  CG1 . VAL   C 80  ? 0.4419 0.2965 0.5026 -0.0127 -0.0145 -0.0328 173 VAL   C CG1 
3818 C  CG2 . VAL   C 80  ? 0.4535 0.2798 0.5410 -0.0170 -0.0103 -0.0360 173 VAL   C CG2 
3819 N  N   . ARG   C 81  ? 0.4630 0.3549 0.5282 -0.0230 -0.0191 -0.0468 174 ARG   C N   
3820 C  CA  . ARG   C 81  ? 0.4752 0.3860 0.5316 -0.0204 -0.0222 -0.0413 174 ARG   C CA  
3821 C  C   . ARG   C 81  ? 0.4681 0.3956 0.5131 -0.0155 -0.0242 -0.0421 174 ARG   C C   
3822 O  O   . ARG   C 81  ? 0.4562 0.3853 0.5011 -0.0159 -0.0233 -0.0516 174 ARG   C O   
3823 C  CB  . ARG   C 81  ? 0.5023 0.4289 0.5677 -0.0265 -0.0240 -0.0492 174 ARG   C CB  
3824 C  CG  . ARG   C 81  ? 0.5338 0.4701 0.6085 -0.0330 -0.0245 -0.0680 174 ARG   C CG  
3825 C  CD  . ARG   C 81  ? 0.5627 0.5191 0.6469 -0.0400 -0.0268 -0.0774 174 ARG   C CD  
3826 N  NE  . ARG   C 81  ? 0.5787 0.5214 0.6781 -0.0474 -0.0239 -0.0767 174 ARG   C NE  
3827 C  CZ  . ARG   C 81  ? 0.5883 0.5317 0.6883 -0.0472 -0.0234 -0.0651 174 ARG   C CZ  
3828 N  NH1 . ARG   C 81  ? 0.5908 0.5459 0.6788 -0.0394 -0.0259 -0.0543 174 ARG   C NH1 
3829 N  NH2 . ARG   C 81  ? 0.6014 0.5347 0.7155 -0.0548 -0.0200 -0.0644 174 ARG   C NH2 
3830 N  N   . ARG   C 82  ? 0.4588 0.3994 0.4957 -0.0109 -0.0264 -0.0323 175 ARG   C N   
3831 C  CA  . ARG   C 82  ? 0.4612 0.4216 0.4875 -0.0062 -0.0285 -0.0291 175 ARG   C CA  
3832 C  C   . ARG   C 82  ? 0.4664 0.4542 0.4938 -0.0100 -0.0314 -0.0434 175 ARG   C C   
3833 O  O   . ARG   C 82  ? 0.4457 0.4393 0.4830 -0.0158 -0.0328 -0.0533 175 ARG   C O   
3834 C  CB  . ARG   C 82  ? 0.4617 0.4281 0.4835 0.0000  -0.0299 -0.0136 175 ARG   C CB  
3835 C  CG  . ARG   C 82  ? 0.4614 0.4032 0.4829 0.0030  -0.0267 -0.0025 175 ARG   C CG  
3836 C  CD  . ARG   C 82  ? 0.4682 0.4146 0.4892 0.0093  -0.0275 0.0102  175 ARG   C CD  
3837 N  NE  . ARG   C 82  ? 0.4891 0.4412 0.5033 0.0144  -0.0274 0.0203  175 ARG   C NE  
3838 C  CZ  . ARG   C 82  ? 0.4952 0.4529 0.5103 0.0209  -0.0279 0.0333  175 ARG   C CZ  
3839 N  NH1 . ARG   C 82  ? 0.4824 0.4418 0.5051 0.0238  -0.0289 0.0359  175 ARG   C NH1 
3840 N  NH2 . ARG   C 82  ? 0.5004 0.4626 0.5105 0.0247  -0.0271 0.0442  175 ARG   C NH2 
3841 N  N   . CYS   C 83  ? 0.4698 0.4766 0.4876 -0.0074 -0.0322 -0.0446 176 CYS   C N   
3842 C  CA  . CYS   C 83  ? 0.4804 0.5215 0.4958 -0.0102 -0.0355 -0.0578 176 CYS   C CA  
3843 C  C   . CYS   C 83  ? 0.4736 0.5391 0.4872 -0.0076 -0.0405 -0.0490 176 CYS   C C   
3844 O  O   . CYS   C 83  ? 0.4629 0.5197 0.4748 -0.0016 -0.0406 -0.0311 176 CYS   C O   
3845 C  CB  . CYS   C 83  ? 0.4914 0.5478 0.4951 -0.0073 -0.0343 -0.0581 176 CYS   C CB  
3846 S  SG  . CYS   C 83  ? 0.5038 0.5684 0.4943 0.0014  -0.0347 -0.0318 176 CYS   C SG  
3847 N  N   . PRO   C 84  ? 0.4718 0.5696 0.4871 -0.0117 -0.0447 -0.0622 177 PRO   C N   
3848 C  CA  . PRO   C 84  ? 0.4668 0.5938 0.4806 -0.0080 -0.0502 -0.0531 177 PRO   C CA  
3849 C  C   . PRO   C 84  ? 0.4652 0.5986 0.4676 0.0025  -0.0509 -0.0286 177 PRO   C C   
3850 O  O   . PRO   C 84  ? 0.4622 0.5906 0.4684 0.0083  -0.0520 -0.0135 177 PRO   C O   
3851 C  CB  . PRO   C 84  ? 0.4829 0.6498 0.4959 -0.0139 -0.0543 -0.0730 177 PRO   C CB  
3852 C  CG  . PRO   C 84  ? 0.4870 0.6343 0.5110 -0.0236 -0.0503 -0.0965 177 PRO   C CG  
3853 C  CD  . PRO   C 84  ? 0.4816 0.5908 0.5027 -0.0200 -0.0444 -0.0877 177 PRO   C CD  
3854 N  N   . HIS   C 85  ? 0.4637 0.6059 0.4542 0.0048  -0.0493 -0.0253 178 HIS   C N   
3855 C  CA  . HIS   C 85  ? 0.4636 0.6153 0.4440 0.0137  -0.0494 -0.0013 178 HIS   C CA  
3856 C  C   . HIS   C 85  ? 0.4601 0.5753 0.4461 0.0192  -0.0460 0.0166  178 HIS   C C   
3857 O  O   . HIS   C 85  ? 0.4611 0.5833 0.4489 0.0268  -0.0480 0.0349  178 HIS   C O   
3858 C  CB  . HIS   C 85  ? 0.4592 0.6213 0.4275 0.0132  -0.0464 -0.0024 178 HIS   C CB  
3859 C  CG  . HIS   C 85  ? 0.4567 0.6179 0.4176 0.0208  -0.0443 0.0235  178 HIS   C CG  
3860 N  ND1 . HIS   C 85  ? 0.4629 0.6524 0.4190 0.0279  -0.0480 0.0434  178 HIS   C ND1 
3861 C  CD2 . HIS   C 85  ? 0.4523 0.5873 0.4118 0.0220  -0.0386 0.0333  178 HIS   C CD2 
3862 C  CE1 . HIS   C 85  ? 0.4694 0.6474 0.4222 0.0328  -0.0440 0.0651  178 HIS   C CE1 
3863 N  NE2 . HIS   C 85  ? 0.4598 0.6055 0.4144 0.0287  -0.0382 0.0581  178 HIS   C NE2 
3864 N  N   . HIS   C 86  ? 0.4678 0.5476 0.4574 0.0159  -0.0411 0.0114  179 HIS   C N   
3865 C  CA  . HIS   C 86  ? 0.4745 0.5210 0.4688 0.0199  -0.0374 0.0254  179 HIS   C CA  
3866 C  C   . HIS   C 86  ? 0.4811 0.5192 0.4861 0.0211  -0.0389 0.0263  179 HIS   C C   
3867 O  O   . HIS   C 86  ? 0.4811 0.5070 0.4903 0.0273  -0.0375 0.0407  179 HIS   C O   
3868 C  CB  . HIS   C 86  ? 0.4667 0.4846 0.4609 0.0159  -0.0324 0.0191  179 HIS   C CB  
3869 C  CG  . HIS   C 86  ? 0.4761 0.4979 0.4618 0.0174  -0.0296 0.0263  179 HIS   C CG  
3870 N  ND1 . HIS   C 86  ? 0.4718 0.4947 0.4538 0.0132  -0.0273 0.0138  179 HIS   C ND1 
3871 C  CD2 . HIS   C 86  ? 0.4759 0.5016 0.4576 0.0225  -0.0282 0.0451  179 HIS   C CD2 
3872 C  CE1 . HIS   C 86  ? 0.4818 0.5113 0.4569 0.0153  -0.0246 0.0242  179 HIS   C CE1 
3873 N  NE2 . HIS   C 86  ? 0.4817 0.5124 0.4565 0.0205  -0.0250 0.0442  179 HIS   C NE2 
3874 N  N   . GLU   C 87  ? 0.4983 0.5446 0.5090 0.0153  -0.0411 0.0110  180 GLU   C N   
3875 C  CA  . GLU   C 87  ? 0.5261 0.5707 0.5476 0.0154  -0.0424 0.0105  180 GLU   C CA  
3876 C  C   . GLU   C 87  ? 0.5631 0.6302 0.5864 0.0243  -0.0460 0.0252  180 GLU   C C   
3877 O  O   . GLU   C 87  ? 0.6012 0.6570 0.6330 0.0289  -0.0447 0.0327  180 GLU   C O   
3878 C  CB  . GLU   C 87  ? 0.5155 0.5679 0.5438 0.0058  -0.0437 -0.0087 180 GLU   C CB  
3879 C  CG  . GLU   C 87  ? 0.5224 0.6105 0.5555 0.0044  -0.0493 -0.0147 180 GLU   C CG  
3880 C  CD  . GLU   C 87  ? 0.5146 0.6064 0.5565 -0.0070 -0.0495 -0.0361 180 GLU   C CD  
3881 O  OE1 . GLU   C 87  ? 0.5242 0.6475 0.5660 -0.0110 -0.0537 -0.0481 180 GLU   C OE1 
3882 O  OE2 . GLU   C 87  ? 0.5066 0.5708 0.5562 -0.0124 -0.0452 -0.0406 180 GLU   C OE2 
3883 N  N   . ARG   C 88  ? 0.5929 0.6919 0.6091 0.0273  -0.0502 0.0296  181 ARG   C N   
3884 C  CA  . ARG   C 88  ? 0.5995 0.7245 0.6183 0.0370  -0.0545 0.0461  181 ARG   C CA  
3885 C  C   . ARG   C 88  ? 0.6141 0.7123 0.6392 0.0461  -0.0505 0.0647  181 ARG   C C   
3886 O  O   . ARG   C 88  ? 0.6306 0.7100 0.6501 0.0474  -0.0465 0.0732  181 ARG   C O   
3887 C  CB  . ARG   C 88  ? 0.6108 0.7707 0.6179 0.0399  -0.0583 0.0532  181 ARG   C CB  
3888 C  CG  . ARG   C 88  ? 0.6105 0.8089 0.6140 0.0329  -0.0638 0.0349  181 ARG   C CG  
3889 C  CD  . ARG   C 88  ? 0.6156 0.8404 0.6038 0.0315  -0.0649 0.0337  181 ARG   C CD  
3890 N  NE  . ARG   C 88  ? 0.6331 0.8901 0.6135 0.0410  -0.0683 0.0563  181 ARG   C NE  
3891 C  CZ  . ARG   C 88  ? 0.6240 0.8706 0.5980 0.0473  -0.0646 0.0779  181 ARG   C CZ  
3892 N  NH1 . ARG   C 88  ? 0.6197 0.8989 0.5880 0.0558  -0.0680 0.0997  181 ARG   C NH1 
3893 N  NH2 . ARG   C 88  ? 0.6074 0.8124 0.5821 0.0452  -0.0576 0.0787  181 ARG   C NH2 
3894 N  N   . SER   C 92  ? 0.6277 0.5681 0.6963 0.0644  -0.0223 0.0908  185 SER   C N   
3895 C  CA  . SER   C 92  ? 0.6293 0.5520 0.7093 0.0719  -0.0181 0.1042  185 SER   C CA  
3896 C  C   . SER   C 92  ? 0.6034 0.5007 0.6944 0.0716  -0.0123 0.0944  185 SER   C C   
3897 O  O   . SER   C 92  ? 0.6302 0.5160 0.7371 0.0798  -0.0088 0.1026  185 SER   C O   
3898 C  CB  . SER   C 92  ? 0.6471 0.5630 0.7193 0.0688  -0.0165 0.1135  185 SER   C CB  
3899 O  OG  . SER   C 92  ? 0.6615 0.5665 0.7469 0.0768  -0.0132 0.1310  185 SER   C OG  
3900 N  N   . ASP   C 93  ? 0.5684 0.4582 0.6522 0.0628  -0.0111 0.0781  186 ASP   C N   
3901 C  CA  . ASP   C 93  ? 0.5496 0.4175 0.6397 0.0604  -0.0055 0.0677  186 ASP   C CA  
3902 C  C   . ASP   C 93  ? 0.5427 0.4160 0.6431 0.0645  -0.0039 0.0594  186 ASP   C C   
3903 O  O   . ASP   C 93  ? 0.5444 0.4032 0.6538 0.0653  0.0012  0.0515  186 ASP   C O   
3904 C  CB  . ASP   C 93  ? 0.5308 0.3890 0.6079 0.0498  -0.0048 0.0585  186 ASP   C CB  
3905 C  CG  . ASP   C 93  ? 0.5141 0.3739 0.5856 0.0434  -0.0044 0.0443  186 ASP   C CG  
3906 O  OD1 . ASP   C 93  ? 0.5061 0.3797 0.5789 0.0445  -0.0061 0.0414  186 ASP   C OD1 
3907 O  OD2 . ASP   C 93  ? 0.5030 0.3520 0.5691 0.0372  -0.0026 0.0375  186 ASP   C OD2 
3908 N  N   . GLY   C 94  ? 0.5233 0.4192 0.6239 0.0670  -0.0080 0.0605  187 GLY   C N   
3909 C  CA  . GLY   C 94  ? 0.5133 0.4200 0.6252 0.0716  -0.0067 0.0543  187 GLY   C CA  
3910 C  C   . GLY   C 94  ? 0.4878 0.3971 0.5930 0.0626  -0.0049 0.0397  187 GLY   C C   
3911 O  O   . GLY   C 94  ? 0.4829 0.4061 0.5960 0.0649  -0.0039 0.0346  187 GLY   C O   
3912 N  N   . LEU   C 95  ? 0.4704 0.3679 0.5628 0.0532  -0.0042 0.0339  188 LEU   C N   
3913 C  CA  . LEU   C 95  ? 0.4511 0.3498 0.5379 0.0453  -0.0017 0.0227  188 LEU   C CA  
3914 C  C   . LEU   C 95  ? 0.4437 0.3492 0.5186 0.0363  -0.0056 0.0222  188 LEU   C C   
3915 O  O   . LEU   C 95  ? 0.4591 0.3750 0.5339 0.0313  -0.0050 0.0173  188 LEU   C O   
3916 C  CB  . LEU   C 95  ? 0.4483 0.3291 0.5326 0.0424  0.0025  0.0163  188 LEU   C CB  
3917 C  CG  . LEU   C 95  ? 0.4586 0.3293 0.5571 0.0501  0.0073  0.0136  188 LEU   C CG  
3918 C  CD1 . LEU   C 95  ? 0.4590 0.3136 0.5543 0.0452  0.0107  0.0058  188 LEU   C CD1 
3919 C  CD2 . LEU   C 95  ? 0.4610 0.3445 0.5703 0.0547  0.0107  0.0062  188 LEU   C CD2 
3920 N  N   . ALA   C 96  ? 0.4351 0.3346 0.5018 0.0340  -0.0086 0.0267  189 ALA   C N   
3921 C  CA  . ALA   C 96  ? 0.4183 0.3202 0.4756 0.0258  -0.0114 0.0243  189 ALA   C CA  
3922 C  C   . ALA   C 96  ? 0.4107 0.3324 0.4704 0.0253  -0.0156 0.0246  189 ALA   C C   
3923 O  O   . ALA   C 96  ? 0.4093 0.3421 0.4724 0.0316  -0.0183 0.0306  189 ALA   C O   
3924 C  CB  . ALA   C 96  ? 0.4274 0.3176 0.4768 0.0244  -0.0122 0.0272  189 ALA   C CB  
3925 N  N   . PRO   C 97  ? 0.3963 0.3247 0.4557 0.0175  -0.0163 0.0185  190 PRO   C N   
3926 C  CA  . PRO   C 97  ? 0.3932 0.3411 0.4556 0.0150  -0.0205 0.0159  190 PRO   C CA  
3927 C  C   . PRO   C 97  ? 0.3893 0.3388 0.4442 0.0158  -0.0239 0.0176  190 PRO   C C   
3928 O  O   . PRO   C 97  ? 0.3848 0.3184 0.4324 0.0140  -0.0226 0.0178  190 PRO   C O   
3929 C  CB  . PRO   C 97  ? 0.3848 0.3318 0.4495 0.0048  -0.0191 0.0087  190 PRO   C CB  
3930 C  CG  . PRO   C 97  ? 0.3862 0.3195 0.4500 0.0040  -0.0140 0.0100  190 PRO   C CG  
3931 C  CD  . PRO   C 97  ? 0.3873 0.3063 0.4447 0.0103  -0.0131 0.0143  190 PRO   C CD  
3932 N  N   . PRO   C 98  ? 0.3960 0.3679 0.4523 0.0185  -0.0284 0.0189  191 PRO   C N   
3933 C  CA  . PRO   C 98  ? 0.4053 0.3843 0.4533 0.0197  -0.0314 0.0211  191 PRO   C CA  
3934 C  C   . PRO   C 98  ? 0.4108 0.3848 0.4536 0.0110  -0.0314 0.0103  191 PRO   C C   
3935 O  O   . PRO   C 98  ? 0.4208 0.3942 0.4558 0.0120  -0.0319 0.0119  191 PRO   C O   
3936 C  CB  . PRO   C 98  ? 0.4071 0.4175 0.4586 0.0238  -0.0366 0.0237  191 PRO   C CB  
3937 C  CG  . PRO   C 98  ? 0.4047 0.4251 0.4675 0.0213  -0.0367 0.0180  191 PRO   C CG  
3938 C  CD  . PRO   C 98  ? 0.3976 0.3930 0.4636 0.0209  -0.0309 0.0186  191 PRO   C CD  
3939 N  N   . GLN   C 99  ? 0.4106 0.3804 0.4594 0.0030  -0.0302 0.0006  192 GLN   C N   
3940 C  CA  . GLN   C 99  ? 0.4099 0.3730 0.4585 -0.0049 -0.0297 -0.0103 192 GLN   C CA  
3941 C  C   . GLN   C 99  ? 0.4019 0.3383 0.4464 -0.0054 -0.0259 -0.0077 192 GLN   C C   
3942 O  O   . GLN   C 99  ? 0.3824 0.3127 0.4261 -0.0090 -0.0254 -0.0147 192 GLN   C O   
3943 C  CB  . GLN   C 99  ? 0.4221 0.3899 0.4822 -0.0136 -0.0293 -0.0198 192 GLN   C CB  
3944 C  CG  . GLN   C 99  ? 0.4417 0.4396 0.5070 -0.0162 -0.0338 -0.0281 192 GLN   C CG  
3945 C  CD  . GLN   C 99  ? 0.4544 0.4526 0.5324 -0.0276 -0.0327 -0.0416 192 GLN   C CD  
3946 O  OE1 . GLN   C 99  ? 0.4695 0.4507 0.5549 -0.0323 -0.0286 -0.0398 192 GLN   C OE1 
3947 N  NE2 . GLN   C 99  ? 0.4791 0.4967 0.5604 -0.0327 -0.0359 -0.0553 192 GLN   C NE2 
3948 N  N   . HIS   C 100 ? 0.3935 0.3164 0.4365 -0.0018 -0.0232 0.0006  193 HIS   C N   
3949 C  CA  . HIS   C 100 ? 0.3928 0.2943 0.4329 -0.0028 -0.0200 0.0030  193 HIS   C CA  
3950 C  C   . HIS   C 100 ? 0.3924 0.2878 0.4249 0.0004  -0.0201 0.0054  193 HIS   C C   
3951 O  O   . HIS   C 100 ? 0.3935 0.2930 0.4221 0.0058  -0.0206 0.0119  193 HIS   C O   
3952 C  CB  . HIS   C 100 ? 0.3885 0.2833 0.4294 -0.0005 -0.0173 0.0088  193 HIS   C CB  
3953 C  CG  . HIS   C 100 ? 0.3856 0.2829 0.4334 -0.0056 -0.0155 0.0069  193 HIS   C CG  
3954 N  ND1 . HIS   C 100 ? 0.3827 0.2706 0.4297 -0.0076 -0.0122 0.0098  193 HIS   C ND1 
3955 C  CD2 . HIS   C 100 ? 0.3934 0.3036 0.4492 -0.0099 -0.0163 0.0026  193 HIS   C CD2 
3956 C  CE1 . HIS   C 100 ? 0.3872 0.2812 0.4411 -0.0127 -0.0106 0.0090  193 HIS   C CE1 
3957 N  NE2 . HIS   C 100 ? 0.3915 0.2982 0.4519 -0.0146 -0.0129 0.0041  193 HIS   C NE2 
3958 N  N   . LEU   C 101 ? 0.3863 0.2720 0.4182 -0.0024 -0.0192 0.0014  194 LEU   C N   
3959 C  CA  . LEU   C 101 ? 0.3802 0.2615 0.4062 0.0000  -0.0187 0.0028  194 LEU   C CA  
3960 C  C   . LEU   C 101 ? 0.3773 0.2476 0.4000 0.0028  -0.0168 0.0106  194 LEU   C C   
3961 O  O   . LEU   C 101 ? 0.3820 0.2538 0.4006 0.0058  -0.0165 0.0150  194 LEU   C O   
3962 C  CB  . LEU   C 101 ? 0.3839 0.2581 0.4133 -0.0029 -0.0179 -0.0042 194 LEU   C CB  
3963 C  CG  . LEU   C 101 ? 0.3844 0.2548 0.4093 -0.0003 -0.0168 -0.0029 194 LEU   C CG  
3964 C  CD1 . LEU   C 101 ? 0.3859 0.2722 0.4048 0.0016  -0.0176 -0.0040 194 LEU   C CD1 
3965 C  CD2 . LEU   C 101 ? 0.3851 0.2466 0.4166 -0.0018 -0.0157 -0.0091 194 LEU   C CD2 
3966 N  N   . ILE   C 102 ? 0.3737 0.2349 0.3987 0.0013  -0.0154 0.0120  195 ILE   C N   
3967 C  CA  . ILE   C 102 ? 0.3685 0.2207 0.3909 0.0024  -0.0136 0.0159  195 ILE   C CA  
3968 C  C   . ILE   C 102 ? 0.3733 0.2269 0.3971 0.0045  -0.0123 0.0182  195 ILE   C C   
3969 O  O   . ILE   C 102 ? 0.3673 0.2249 0.3942 0.0032  -0.0119 0.0171  195 ILE   C O   
3970 C  CB  . ILE   C 102 ? 0.3648 0.2100 0.3880 -0.0001 -0.0130 0.0159  195 ILE   C CB  
3971 C  CG1 . ILE   C 102 ? 0.3620 0.2047 0.3880 -0.0012 -0.0138 0.0130  195 ILE   C CG1 
3972 C  CG2 . ILE   C 102 ? 0.3608 0.2021 0.3809 0.0006  -0.0120 0.0181  195 ILE   C CG2 
3973 C  CD1 . ILE   C 102 ? 0.3631 0.1989 0.3914 -0.0019 -0.0134 0.0159  195 ILE   C CD1 
3974 N  N   . ARG   C 103 ? 0.3818 0.2322 0.4052 0.0075  -0.0112 0.0210  196 ARG   C N   
3975 C  CA  . ARG   C 103 ? 0.3924 0.2414 0.4202 0.0103  -0.0091 0.0215  196 ARG   C CA  
3976 C  C   . ARG   C 103 ? 0.3980 0.2388 0.4253 0.0087  -0.0068 0.0190  196 ARG   C C   
3977 O  O   . ARG   C 103 ? 0.4039 0.2410 0.4280 0.0065  -0.0073 0.0192  196 ARG   C O   
3978 C  CB  . ARG   C 103 ? 0.4063 0.2576 0.4379 0.0155  -0.0091 0.0271  196 ARG   C CB  
3979 C  CG  . ARG   C 103 ? 0.4152 0.2801 0.4467 0.0172  -0.0121 0.0293  196 ARG   C CG  
3980 C  CD  . ARG   C 103 ? 0.4318 0.3007 0.4691 0.0240  -0.0119 0.0370  196 ARG   C CD  
3981 N  NE  . ARG   C 103 ? 0.4336 0.3201 0.4700 0.0263  -0.0155 0.0406  196 ARG   C NE  
3982 C  CZ  . ARG   C 103 ? 0.4600 0.3546 0.4992 0.0325  -0.0165 0.0506  196 ARG   C CZ  
3983 N  NH1 . ARG   C 103 ? 0.4781 0.3607 0.5232 0.0368  -0.0134 0.0587  196 ARG   C NH1 
3984 N  NH2 . ARG   C 103 ? 0.4615 0.3773 0.4987 0.0341  -0.0205 0.0529  196 ARG   C NH2 
3985 N  N   . VAL   C 104 ? 0.4051 0.2456 0.4362 0.0096  -0.0043 0.0152  197 VAL   C N   
3986 C  CA  . VAL   C 104 ? 0.4213 0.2561 0.4543 0.0082  -0.0018 0.0102  197 VAL   C CA  
3987 C  C   . VAL   C 104 ? 0.4364 0.2642 0.4795 0.0125  0.0009  0.0107  197 VAL   C C   
3988 O  O   . VAL   C 104 ? 0.4389 0.2700 0.4875 0.0172  0.0016  0.0121  197 VAL   C O   
3989 C  CB  . VAL   C 104 ? 0.4269 0.2689 0.4571 0.0054  -0.0005 0.0035  197 VAL   C CB  
3990 C  CG1 . VAL   C 104 ? 0.4356 0.2755 0.4691 0.0037  0.0022  -0.0050 197 VAL   C CG1 
3991 C  CG2 . VAL   C 104 ? 0.4225 0.2698 0.4447 0.0016  -0.0030 0.0065  197 VAL   C CG2 
3992 N  N   . GLU   C 105 ? 0.4599 0.2784 0.5071 0.0111  0.0026  0.0106  198 GLU   C N   
3993 C  CA  . GLU   C 105 ? 0.4782 0.2862 0.5384 0.0149  0.0061  0.0126  198 GLU   C CA  
3994 C  C   . GLU   C 105 ? 0.4789 0.2819 0.5468 0.0123  0.0100  -0.0002 198 GLU   C C   
3995 O  O   . GLU   C 105 ? 0.4851 0.2938 0.5461 0.0065  0.0092  -0.0081 198 GLU   C O   
3996 C  CB  . GLU   C 105 ? 0.4982 0.3002 0.5594 0.0143  0.0060  0.0226  198 GLU   C CB  
3997 C  CG  . GLU   C 105 ? 0.5198 0.3115 0.5883 0.0092  0.0093  0.0186  198 GLU   C CG  
3998 C  CD  . GLU   C 105 ? 0.5373 0.3263 0.6061 0.0073  0.0097  0.0293  198 GLU   C CD  
3999 O  OE1 . GLU   C 105 ? 0.5516 0.3292 0.6332 0.0077  0.0137  0.0347  198 GLU   C OE1 
4000 O  OE2 . GLU   C 105 ? 0.5372 0.3358 0.5947 0.0054  0.0065  0.0321  198 GLU   C OE2 
4001 N  N   . GLY   C 106 ? 0.5057 0.3000 0.5883 0.0169  0.0141  -0.0025 199 GLY   C N   
4002 C  CA  . GLY   C 106 ? 0.5115 0.2993 0.6056 0.0147  0.0190  -0.0173 199 GLY   C CA  
4003 C  C   . GLY   C 106 ? 0.5175 0.3196 0.6058 0.0133  0.0195  -0.0310 199 GLY   C C   
4004 O  O   . GLY   C 106 ? 0.5260 0.3296 0.6179 0.0085  0.0223  -0.0460 199 GLY   C O   
4005 N  N   . ASN   C 107 ? 0.4996 0.3143 0.5795 0.0164  0.0173  -0.0268 200 ASN   C N   
4006 C  CA  . ASN   C 107 ? 0.4935 0.3248 0.5672 0.0146  0.0184  -0.0375 200 ASN   C CA  
4007 C  C   . ASN   C 107 ? 0.4820 0.3206 0.5606 0.0213  0.0197  -0.0350 200 ASN   C C   
4008 O  O   . ASN   C 107 ? 0.4536 0.2988 0.5251 0.0222  0.0161  -0.0246 200 ASN   C O   
4009 C  CB  . ASN   C 107 ? 0.4937 0.3373 0.5500 0.0081  0.0144  -0.0349 200 ASN   C CB  
4010 C  CG  . ASN   C 107 ? 0.5022 0.3641 0.5525 0.0048  0.0163  -0.0460 200 ASN   C CG  
4011 O  OD1 . ASN   C 107 ? 0.5151 0.3845 0.5707 0.0080  0.0201  -0.0528 200 ASN   C OD1 
4012 N  ND2 . ASN   C 107 ? 0.5051 0.3769 0.5446 -0.0010 0.0139  -0.0477 200 ASN   C ND2 
4013 N  N   . LEU   C 108 ? 0.4836 0.3227 0.5753 0.0256  0.0249  -0.0464 201 LEU   C N   
4014 C  CA  . LEU   C 108 ? 0.4897 0.3372 0.5899 0.0332  0.0269  -0.0456 201 LEU   C CA  
4015 C  C   . LEU   C 108 ? 0.4822 0.3524 0.5703 0.0294  0.0266  -0.0483 201 LEU   C C   
4016 O  O   . LEU   C 108 ? 0.4856 0.3661 0.5794 0.0343  0.0277  -0.0462 201 LEU   C O   
4017 C  CB  . LEU   C 108 ? 0.5127 0.3536 0.6332 0.0393  0.0335  -0.0589 201 LEU   C CB  
4018 C  CG  . LEU   C 108 ? 0.5300 0.3465 0.6656 0.0414  0.0354  -0.0576 201 LEU   C CG  
4019 C  CD1 . LEU   C 108 ? 0.5543 0.3641 0.7100 0.0444  0.0429  -0.0768 201 LEU   C CD1 
4020 C  CD2 . LEU   C 108 ? 0.5365 0.3431 0.6806 0.0497  0.0328  -0.0383 201 LEU   C CD2 
4021 N  N   . ARG   C 109 ? 0.4830 0.3623 0.5562 0.0212  0.0254  -0.0515 202 ARG   C N   
4022 C  CA  . ARG   C 109 ? 0.4804 0.3818 0.5422 0.0169  0.0258  -0.0515 202 ARG   C CA  
4023 C  C   . ARG   C 109 ? 0.4700 0.3712 0.5207 0.0129  0.0204  -0.0359 202 ARG   C C   
4024 O  O   . ARG   C 109 ? 0.4854 0.4019 0.5273 0.0084  0.0205  -0.0325 202 ARG   C O   
4025 C  CB  . ARG   C 109 ? 0.4934 0.4081 0.5467 0.0110  0.0281  -0.0636 202 ARG   C CB  
4026 C  CG  . ARG   C 109 ? 0.5132 0.4316 0.5783 0.0139  0.0344  -0.0833 202 ARG   C CG  
4027 C  CD  . ARG   C 109 ? 0.5334 0.4718 0.5887 0.0074  0.0364  -0.0971 202 ARG   C CD  
4028 N  NE  . ARG   C 109 ? 0.5428 0.5077 0.5831 0.0033  0.0365  -0.0916 202 ARG   C NE  
4029 C  CZ  . ARG   C 109 ? 0.5590 0.5469 0.5860 -0.0028 0.0367  -0.0972 202 ARG   C CZ  
4030 N  NH1 . ARG   C 109 ? 0.5655 0.5548 0.5921 -0.0061 0.0365  -0.1111 202 ARG   C NH1 
4031 N  NH2 . ARG   C 109 ? 0.5609 0.5723 0.5755 -0.0061 0.0372  -0.0881 202 ARG   C NH2 
4032 N  N   . VAL   C 110 ? 0.4527 0.3379 0.5046 0.0145  0.0163  -0.0269 203 VAL   C N   
4033 C  CA  . VAL   C 110 ? 0.4293 0.3130 0.4734 0.0113  0.0114  -0.0147 203 VAL   C CA  
4034 C  C   . VAL   C 110 ? 0.4170 0.3129 0.4635 0.0115  0.0116  -0.0105 203 VAL   C C   
4035 O  O   . VAL   C 110 ? 0.4204 0.3214 0.4771 0.0169  0.0137  -0.0133 203 VAL   C O   
4036 C  CB  . VAL   C 110 ? 0.4251 0.2931 0.4713 0.0137  0.0079  -0.0081 203 VAL   C CB  
4037 C  CG1 . VAL   C 110 ? 0.4319 0.2967 0.4899 0.0212  0.0084  -0.0056 203 VAL   C CG1 
4038 C  CG2 . VAL   C 110 ? 0.4135 0.2810 0.4520 0.0099  0.0036  0.0004  203 VAL   C CG2 
4039 N  N   . GLU   C 111 ? 0.4021 0.3027 0.4417 0.0058  0.0097  -0.0038 204 GLU   C N   
4040 C  CA  . GLU   C 111 ? 0.3980 0.3103 0.4411 0.0034  0.0101  0.0001  204 GLU   C CA  
4041 C  C   . GLU   C 111 ? 0.3848 0.2894 0.4260 -0.0002 0.0057  0.0077  204 GLU   C C   
4042 O  O   . GLU   C 111 ? 0.3849 0.2801 0.4192 -0.0027 0.0038  0.0107  204 GLU   C O   
4043 C  CB  . GLU   C 111 ? 0.4067 0.3350 0.4459 -0.0011 0.0144  -0.0009 204 GLU   C CB  
4044 C  CG  . GLU   C 111 ? 0.4083 0.3465 0.4495 -0.0071 0.0152  0.0063  204 GLU   C CG  
4045 C  CD  . GLU   C 111 ? 0.4145 0.3690 0.4502 -0.0125 0.0196  0.0091  204 GLU   C CD  
4046 O  OE1 . GLU   C 111 ? 0.4182 0.3851 0.4514 -0.0104 0.0235  0.0014  204 GLU   C OE1 
4047 O  OE2 . GLU   C 111 ? 0.4196 0.3752 0.4542 -0.0190 0.0196  0.0191  204 GLU   C OE2 
4048 N  N   . TYR   C 112 ? 0.3767 0.2862 0.4249 -0.0001 0.0040  0.0092  205 TYR   C N   
4049 C  CA  . TYR   C 112 ? 0.3703 0.2746 0.4188 -0.0038 0.0002  0.0127  205 TYR   C CA  
4050 C  C   . TYR   C 112 ? 0.3667 0.2809 0.4211 -0.0109 0.0017  0.0144  205 TYR   C C   
4051 O  O   . TYR   C 112 ? 0.3658 0.2945 0.4263 -0.0110 0.0044  0.0127  205 TYR   C O   
4052 C  CB  . TYR   C 112 ? 0.3630 0.2672 0.4149 0.0013  -0.0034 0.0119  205 TYR   C CB  
4053 C  CG  . TYR   C 112 ? 0.3624 0.2546 0.4096 0.0065  -0.0045 0.0127  205 TYR   C CG  
4054 C  CD1 . TYR   C 112 ? 0.3590 0.2409 0.4002 0.0047  -0.0069 0.0144  205 TYR   C CD1 
4055 C  CD2 . TYR   C 112 ? 0.3616 0.2527 0.4125 0.0131  -0.0026 0.0115  205 TYR   C CD2 
4056 C  CE1 . TYR   C 112 ? 0.3568 0.2294 0.3947 0.0084  -0.0073 0.0157  205 TYR   C CE1 
4057 C  CE2 . TYR   C 112 ? 0.3649 0.2438 0.4138 0.0166  -0.0028 0.0129  205 TYR   C CE2 
4058 C  CZ  . TYR   C 112 ? 0.3611 0.2316 0.4031 0.0137  -0.0052 0.0154  205 TYR   C CZ  
4059 O  OH  . TYR   C 112 ? 0.3566 0.2168 0.3978 0.0161  -0.0049 0.0172  205 TYR   C OH  
4060 N  N   . LEU   C 113 ? 0.3742 0.2805 0.4287 -0.0169 0.0006  0.0176  206 LEU   C N   
4061 C  CA  . LEU   C 113 ? 0.3817 0.2936 0.4445 -0.0252 0.0028  0.0203  206 LEU   C CA  
4062 C  C   . LEU   C 113 ? 0.3923 0.2988 0.4622 -0.0290 -0.0004 0.0167  206 LEU   C C   
4063 O  O   . LEU   C 113 ? 0.4071 0.3003 0.4731 -0.0274 -0.0029 0.0161  206 LEU   C O   
4064 C  CB  . LEU   C 113 ? 0.3892 0.2960 0.4478 -0.0293 0.0059  0.0287  206 LEU   C CB  
4065 C  CG  . LEU   C 113 ? 0.3923 0.2997 0.4610 -0.0384 0.0088  0.0349  206 LEU   C CG  
4066 C  CD1 . LEU   C 113 ? 0.3931 0.3194 0.4696 -0.0425 0.0124  0.0336  206 LEU   C CD1 
4067 C  CD2 . LEU   C 113 ? 0.4019 0.3037 0.4659 -0.0406 0.0112  0.0467  206 LEU   C CD2 
4068 N  N   . ASP   C 114 ? 0.3984 0.3175 0.4791 -0.0337 -0.0004 0.0127  207 ASP   C N   
4069 C  CA  . ASP   C 114 ? 0.4183 0.3349 0.5099 -0.0415 -0.0016 0.0079  207 ASP   C CA  
4070 C  C   . ASP   C 114 ? 0.4345 0.3485 0.5355 -0.0508 0.0035  0.0144  207 ASP   C C   
4071 O  O   . ASP   C 114 ? 0.4280 0.3579 0.5345 -0.0541 0.0066  0.0159  207 ASP   C O   
4072 C  CB  . ASP   C 114 ? 0.4153 0.3508 0.5146 -0.0422 -0.0048 -0.0009 207 ASP   C CB  
4073 C  CG  . ASP   C 114 ? 0.4079 0.3486 0.4993 -0.0334 -0.0100 -0.0047 207 ASP   C CG  
4074 O  OD1 . ASP   C 114 ? 0.4124 0.3400 0.4932 -0.0275 -0.0108 -0.0016 207 ASP   C OD1 
4075 O  OD2 . ASP   C 114 ? 0.4189 0.3785 0.5158 -0.0332 -0.0133 -0.0105 207 ASP   C OD2 
4076 N  N   . ASP   C 115 ? 0.4601 0.3559 0.5629 -0.0538 0.0049  0.0199  208 ASP   C N   
4077 C  CA  . ASP   C 115 ? 0.4878 0.3788 0.5999 -0.0620 0.0103  0.0305  208 ASP   C CA  
4078 C  C   . ASP   C 115 ? 0.5030 0.4016 0.6337 -0.0725 0.0121  0.0244  208 ASP   C C   
4079 O  O   . ASP   C 115 ? 0.5008 0.3952 0.6401 -0.0751 0.0091  0.0127  208 ASP   C O   
4080 C  CB  . ASP   C 115 ? 0.4980 0.3671 0.6110 -0.0615 0.0107  0.0382  208 ASP   C CB  
4081 C  CG  . ASP   C 115 ? 0.5089 0.3731 0.6311 -0.0684 0.0164  0.0535  208 ASP   C CG  
4082 O  OD1 . ASP   C 115 ? 0.5225 0.3851 0.6626 -0.0781 0.0196  0.0531  208 ASP   C OD1 
4083 O  OD2 . ASP   C 115 ? 0.5096 0.3731 0.6217 -0.0645 0.0176  0.0664  208 ASP   C OD2 
4084 N  N   . ARG   C 116 ? 0.5318 0.4441 0.6687 -0.0787 0.0170  0.0310  209 ARG   C N   
4085 C  CA  . ARG   C 116 ? 0.5612 0.4852 0.7173 -0.0901 0.0196  0.0259  209 ARG   C CA  
4086 C  C   . ARG   C 116 ? 0.5807 0.4853 0.7553 -0.0996 0.0209  0.0233  209 ARG   C C   
4087 O  O   . ARG   C 116 ? 0.5928 0.5054 0.7831 -0.1078 0.0202  0.0108  209 ARG   C O   
4088 C  CB  . ARG   C 116 ? 0.5773 0.5159 0.7369 -0.0959 0.0265  0.0378  209 ARG   C CB  
4089 C  CG  . ARG   C 116 ? 0.5810 0.5461 0.7324 -0.0902 0.0268  0.0348  209 ARG   C CG  
4090 C  CD  . ARG   C 116 ? 0.6041 0.5866 0.7617 -0.0978 0.0346  0.0451  209 ARG   C CD  
4091 N  NE  . ARG   C 116 ? 0.6303 0.6091 0.8091 -0.1125 0.0390  0.0491  209 ARG   C NE  
4092 C  CZ  . ARG   C 116 ? 0.6457 0.6368 0.8337 -0.1221 0.0469  0.0606  209 ARG   C CZ  
4093 N  NH1 . ARG   C 116 ? 0.6685 0.6527 0.8786 -0.1361 0.0509  0.0637  209 ARG   C NH1 
4094 N  NH2 . ARG   C 116 ? 0.6587 0.6696 0.8351 -0.1184 0.0512  0.0684  209 ARG   C NH2 
4095 N  N   . ASN   C 117 ? 0.5994 0.4806 0.7741 -0.0985 0.0228  0.0340  210 ASN   C N   
4096 C  CA  . ASN   C 117 ? 0.6238 0.4838 0.8209 -0.1078 0.0262  0.0349  210 ASN   C CA  
4097 C  C   . ASN   C 117 ? 0.6122 0.4518 0.8093 -0.1020 0.0221  0.0252  210 ASN   C C   
4098 O  O   . ASN   C 117 ? 0.6333 0.4626 0.8503 -0.1094 0.0228  0.0130  210 ASN   C O   
4099 C  CB  . ASN   C 117 ? 0.6560 0.5058 0.8600 -0.1124 0.0331  0.0576  210 ASN   C CB  
4100 C  CG  . ASN   C 117 ? 0.6696 0.5213 0.8514 -0.1019 0.0326  0.0735  210 ASN   C CG  
4101 O  OD1 . ASN   C 117 ? 0.6920 0.5647 0.8572 -0.0976 0.0320  0.0744  210 ASN   C OD1 
4102 N  ND2 . ASN   C 117 ? 0.6924 0.5237 0.8753 -0.0977 0.0329  0.0850  210 ASN   C ND2 
4103 N  N   . THR   C 118 ? 0.5820 0.4166 0.7597 -0.0899 0.0186  0.0294  211 THR   C N   
4104 C  CA  . THR   C 118 ? 0.5693 0.3872 0.7464 -0.0836 0.0152  0.0207  211 THR   C CA  
4105 C  C   . THR   C 118 ? 0.5488 0.3811 0.7156 -0.0793 0.0093  0.0021  211 THR   C C   
4106 O  O   . THR   C 118 ? 0.5558 0.3794 0.7254 -0.0767 0.0070  -0.0094 211 THR   C O   
4107 C  CB  . THR   C 118 ? 0.5715 0.3789 0.7346 -0.0733 0.0143  0.0348  211 THR   C CB  
4108 O  OG1 . THR   C 118 ? 0.5451 0.3694 0.6855 -0.0661 0.0113  0.0367  211 THR   C OG1 
4109 C  CG2 . THR   C 118 ? 0.5871 0.3836 0.7588 -0.0761 0.0195  0.0561  211 THR   C CG2 
4110 N  N   . PHE   C 119 ? 0.5254 0.3801 0.6808 -0.0775 0.0071  0.0005  212 PHE   C N   
4111 C  CA  . PHE   C 119 ? 0.5070 0.3787 0.6517 -0.0722 0.0014  -0.0125 212 PHE   C CA  
4112 C  C   . PHE   C 119 ? 0.4920 0.3563 0.6192 -0.0609 -0.0017 -0.0103 212 PHE   C C   
4113 O  O   . PHE   C 119 ? 0.4946 0.3700 0.6131 -0.0558 -0.0060 -0.0192 212 PHE   C O   
4114 C  CB  . PHE   C 119 ? 0.5174 0.3951 0.6762 -0.0791 -0.0004 -0.0312 212 PHE   C CB  
4115 C  CG  . PHE   C 119 ? 0.5322 0.4157 0.7122 -0.0922 0.0029  -0.0356 212 PHE   C CG  
4116 C  CD1 . PHE   C 119 ? 0.5326 0.4396 0.7135 -0.0954 0.0027  -0.0346 212 PHE   C CD1 
4117 C  CD2 . PHE   C 119 ? 0.5539 0.4193 0.7553 -0.1014 0.0067  -0.0411 212 PHE   C CD2 
4118 C  CE1 . PHE   C 119 ? 0.5396 0.4540 0.7414 -0.1086 0.0061  -0.0391 212 PHE   C CE1 
4119 C  CE2 . PHE   C 119 ? 0.5680 0.4380 0.7915 -0.1150 0.0104  -0.0455 212 PHE   C CE2 
4120 C  CZ  . PHE   C 119 ? 0.5577 0.4532 0.7809 -0.1190 0.0101  -0.0444 212 PHE   C CZ  
4121 N  N   . ARG   C 120 ? 0.4843 0.3328 0.6068 -0.0572 0.0004  0.0020  213 ARG   C N   
4122 C  CA  . ARG   C 120 ? 0.4753 0.3174 0.5829 -0.0474 -0.0021 0.0047  213 ARG   C CA  
4123 C  C   . ARG   C 120 ? 0.4559 0.3115 0.5475 -0.0414 -0.0037 0.0088  213 ARG   C C   
4124 O  O   . ARG   C 120 ? 0.4536 0.3187 0.5453 -0.0437 -0.0014 0.0145  213 ARG   C O   
4125 C  CB  . ARG   C 120 ? 0.4906 0.3145 0.6011 -0.0457 0.0002  0.0161  213 ARG   C CB  
4126 C  CG  . ARG   C 120 ? 0.5065 0.3143 0.6356 -0.0497 0.0018  0.0101  213 ARG   C CG  
4127 C  CD  . ARG   C 120 ? 0.5181 0.3083 0.6513 -0.0452 0.0033  0.0211  213 ARG   C CD  
4128 N  NE  . ARG   C 120 ? 0.5367 0.3101 0.6911 -0.0482 0.0055  0.0136  213 ARG   C NE  
4129 C  CZ  . ARG   C 120 ? 0.5367 0.3057 0.6947 -0.0448 0.0040  -0.0013 213 ARG   C CZ  
4130 N  NH1 . ARG   C 120 ? 0.5202 0.3009 0.6610 -0.0385 0.0001  -0.0081 213 ARG   C NH1 
4131 N  NH2 . ARG   C 120 ? 0.5544 0.3072 0.7348 -0.0477 0.0069  -0.0091 213 ARG   C NH2 
4132 N  N   . HIS   C 121 ? 0.4427 0.2994 0.5230 -0.0342 -0.0069 0.0055  214 HIS   C N   
4133 C  CA  . HIS   C 121 ? 0.4288 0.2947 0.4965 -0.0277 -0.0081 0.0084  214 HIS   C CA  
4134 C  C   . HIS   C 121 ? 0.4139 0.2709 0.4726 -0.0235 -0.0071 0.0167  214 HIS   C C   
4135 O  O   . HIS   C 121 ? 0.4166 0.2623 0.4754 -0.0224 -0.0075 0.0182  214 HIS   C O   
4136 C  CB  . HIS   C 121 ? 0.4291 0.3018 0.4915 -0.0230 -0.0118 0.0014  214 HIS   C CB  
4137 C  CG  . HIS   C 121 ? 0.4398 0.3267 0.5094 -0.0266 -0.0139 -0.0075 214 HIS   C CG  
4138 N  ND1 . HIS   C 121 ? 0.4505 0.3463 0.5165 -0.0239 -0.0172 -0.0144 214 HIS   C ND1 
4139 C  CD2 . HIS   C 121 ? 0.4478 0.3450 0.5278 -0.0328 -0.0132 -0.0109 214 HIS   C CD2 
4140 C  CE1 . HIS   C 121 ? 0.4464 0.3589 0.5195 -0.0279 -0.0192 -0.0222 214 HIS   C CE1 
4141 N  NE2 . HIS   C 121 ? 0.4497 0.3628 0.5323 -0.0337 -0.0168 -0.0208 214 HIS   C NE2 
4142 N  N   . SER   C 122 ? 0.3992 0.2631 0.4510 -0.0209 -0.0059 0.0204  215 SER   C N   
4143 C  CA  . SER   C 122 ? 0.3886 0.2484 0.4313 -0.0172 -0.0055 0.0252  215 SER   C CA  
4144 C  C   . SER   C 122 ? 0.3857 0.2538 0.4226 -0.0132 -0.0048 0.0230  215 SER   C C   
4145 O  O   . SER   C 122 ? 0.3702 0.2481 0.4113 -0.0132 -0.0038 0.0202  215 SER   C O   
4146 C  CB  . SER   C 122 ? 0.3939 0.2518 0.4376 -0.0205 -0.0033 0.0339  215 SER   C CB  
4147 O  OG  . SER   C 122 ? 0.3850 0.2537 0.4317 -0.0246 0.0000  0.0369  215 SER   C OG  
4148 N  N   . VAL   C 123 ? 0.3834 0.2481 0.4133 -0.0099 -0.0051 0.0232  216 VAL   C N   
4149 C  CA  . VAL   C 123 ? 0.3875 0.2567 0.4143 -0.0061 -0.0037 0.0193  216 VAL   C CA  
4150 C  C   . VAL   C 123 ? 0.4001 0.2735 0.4209 -0.0075 -0.0020 0.0206  216 VAL   C C   
4151 O  O   . VAL   C 123 ? 0.3972 0.2666 0.4146 -0.0086 -0.0036 0.0246  216 VAL   C O   
4152 C  CB  . VAL   C 123 ? 0.3818 0.2440 0.4080 -0.0017 -0.0055 0.0166  216 VAL   C CB  
4153 C  CG1 . VAL   C 123 ? 0.3840 0.2378 0.4064 -0.0020 -0.0075 0.0182  216 VAL   C CG1 
4154 C  CG2 . VAL   C 123 ? 0.3822 0.2454 0.4093 0.0019  -0.0033 0.0126  216 VAL   C CG2 
4155 N  N   A VAL   C 124 ? 0.4060 0.2903 0.4263 -0.0073 0.0011  0.0170  217 VAL   C N   
4156 N  N   B VAL   C 124 ? 0.4076 0.2918 0.4279 -0.0072 0.0011  0.0169  217 VAL   C N   
4157 C  CA  A VAL   C 124 ? 0.4159 0.3113 0.4296 -0.0093 0.0031  0.0168  217 VAL   C CA  
4158 C  CA  B VAL   C 124 ? 0.4185 0.3138 0.4322 -0.0092 0.0031  0.0167  217 VAL   C CA  
4159 C  C   A VAL   C 124 ? 0.4225 0.3218 0.4362 -0.0063 0.0054  0.0057  217 VAL   C C   
4160 C  C   B VAL   C 124 ? 0.4236 0.3228 0.4373 -0.0063 0.0054  0.0056  217 VAL   C C   
4161 O  O   A VAL   C 124 ? 0.4358 0.3341 0.4565 -0.0029 0.0072  0.0005  217 VAL   C O   
4162 O  O   B VAL   C 124 ? 0.4395 0.3377 0.4602 -0.0029 0.0072  0.0005  217 VAL   C O   
4163 C  CB  A VAL   C 124 ? 0.4160 0.3249 0.4295 -0.0134 0.0061  0.0230  217 VAL   C CB  
4164 C  CB  B VAL   C 124 ? 0.4201 0.3293 0.4336 -0.0133 0.0062  0.0226  217 VAL   C CB  
4165 C  CG1 A VAL   C 124 ? 0.4131 0.3301 0.4334 -0.0129 0.0093  0.0186  217 VAL   C CG1 
4166 C  CG1 B VAL   C 124 ? 0.4249 0.3460 0.4297 -0.0159 0.0067  0.0279  217 VAL   C CG1 
4167 C  CG2 A VAL   C 124 ? 0.4224 0.3472 0.4272 -0.0156 0.0079  0.0248  217 VAL   C CG2 
4168 C  CG2 B VAL   C 124 ? 0.4213 0.3239 0.4415 -0.0164 0.0053  0.0304  217 VAL   C CG2 
4169 N  N   . VAL   C 125 ? 0.4348 0.3383 0.4427 -0.0074 0.0050  0.0018  218 VAL   C N   
4170 C  CA  . VAL   C 125 ? 0.4454 0.3537 0.4548 -0.0062 0.0078  -0.0115 218 VAL   C CA  
4171 C  C   . VAL   C 125 ? 0.4585 0.3884 0.4589 -0.0099 0.0091  -0.0142 218 VAL   C C   
4172 O  O   . VAL   C 125 ? 0.4502 0.3873 0.4433 -0.0126 0.0066  -0.0039 218 VAL   C O   
4173 C  CB  . VAL   C 125 ? 0.4475 0.3412 0.4603 -0.0051 0.0059  -0.0160 218 VAL   C CB  
4174 C  CG1 . VAL   C 125 ? 0.4458 0.3228 0.4672 -0.0008 0.0055  -0.0132 218 VAL   C CG1 
4175 C  CG2 . VAL   C 125 ? 0.4488 0.3416 0.4553 -0.0077 0.0017  -0.0097 218 VAL   C CG2 
4176 N  N   . PRO   C 126 ? 0.4775 0.4203 0.4790 -0.0098 0.0133  -0.0281 219 PRO   C N   
4177 C  CA  . PRO   C 126 ? 0.4964 0.4639 0.4883 -0.0137 0.0143  -0.0334 219 PRO   C CA  
4178 C  C   . PRO   C 126 ? 0.5077 0.4737 0.4956 -0.0158 0.0099  -0.0349 219 PRO   C C   
4179 O  O   . PRO   C 126 ? 0.4987 0.4461 0.4942 -0.0146 0.0086  -0.0402 219 PRO   C O   
4180 C  CB  . PRO   C 126 ? 0.5089 0.4877 0.5060 -0.0126 0.0201  -0.0525 219 PRO   C CB  
4181 C  CG  . PRO   C 126 ? 0.4972 0.4544 0.5089 -0.0069 0.0222  -0.0553 219 PRO   C CG  
4182 C  CD  . PRO   C 126 ? 0.4833 0.4193 0.4965 -0.0055 0.0174  -0.0396 219 PRO   C CD  
4183 N  N   . TYR   C 127 ? 0.5235 0.5106 0.5003 -0.0189 0.0075  -0.0285 220 TYR   C N   
4184 C  CA  . TYR   C 127 ? 0.5269 0.5227 0.4994 -0.0213 0.0033  -0.0320 220 TYR   C CA  
4185 C  C   . TYR   C 127 ? 0.5498 0.5588 0.5246 -0.0240 0.0063  -0.0554 220 TYR   C C   
4186 O  O   . TYR   C 127 ? 0.5536 0.5830 0.5246 -0.0251 0.0106  -0.0645 220 TYR   C O   
4187 C  CB  . TYR   C 127 ? 0.5307 0.5498 0.4915 -0.0228 0.0000  -0.0169 220 TYR   C CB  
4188 C  CG  . TYR   C 127 ? 0.5330 0.5669 0.4898 -0.0249 -0.0047 -0.0212 220 TYR   C CG  
4189 C  CD1 . TYR   C 127 ? 0.5196 0.5380 0.4810 -0.0233 -0.0095 -0.0138 220 TYR   C CD1 
4190 C  CD2 . TYR   C 127 ? 0.5448 0.6102 0.4944 -0.0287 -0.0042 -0.0352 220 TYR   C CD2 
4191 C  CE1 . TYR   C 127 ? 0.5315 0.5654 0.4912 -0.0253 -0.0140 -0.0185 220 TYR   C CE1 
4192 C  CE2 . TYR   C 127 ? 0.5453 0.6278 0.4922 -0.0313 -0.0091 -0.0406 220 TYR   C CE2 
4193 C  CZ  . TYR   C 127 ? 0.5378 0.6041 0.4903 -0.0295 -0.0141 -0.0317 220 TYR   C CZ  
4194 O  OH  . TYR   C 127 ? 0.5329 0.6176 0.4845 -0.0321 -0.0190 -0.0371 220 TYR   C OH  
4195 N  N   . GLU   C 128 ? 0.5619 0.5589 0.5443 -0.0255 0.0048  -0.0659 221 GLU   C N   
4196 C  CA  . GLU   C 128 ? 0.5896 0.5996 0.5762 -0.0298 0.0071  -0.0897 221 GLU   C CA  
4197 C  C   . GLU   C 128 ? 0.5998 0.6258 0.5812 -0.0341 0.0013  -0.0898 221 GLU   C C   
4198 O  O   . GLU   C 128 ? 0.6030 0.6146 0.5861 -0.0330 -0.0029 -0.0770 221 GLU   C O   
4199 C  CB  . GLU   C 128 ? 0.5947 0.5770 0.5991 -0.0287 0.0113  -0.1034 221 GLU   C CB  
4200 C  CG  . GLU   C 128 ? 0.5858 0.5420 0.5984 -0.0223 0.0141  -0.0938 221 GLU   C CG  
4201 C  CD  . GLU   C 128 ? 0.5912 0.5176 0.6210 -0.0205 0.0162  -0.0986 221 GLU   C CD  
4202 O  OE1 . GLU   C 128 ? 0.6116 0.5364 0.6517 -0.0244 0.0187  -0.1162 221 GLU   C OE1 
4203 O  OE2 . GLU   C 128 ? 0.5722 0.4783 0.6061 -0.0157 0.0157  -0.0847 221 GLU   C OE2 
4204 N  N   . PRO   C 129 ? 0.6239 0.6829 0.5988 -0.0391 0.0010  -0.1048 222 PRO   C N   
4205 C  CA  . PRO   C 129 ? 0.6347 0.7147 0.6049 -0.0432 -0.0051 -0.1051 222 PRO   C CA  
4206 C  C   . PRO   C 129 ? 0.6432 0.7026 0.6289 -0.0468 -0.0053 -0.1177 222 PRO   C C   
4207 O  O   . PRO   C 129 ? 0.6419 0.6759 0.6415 -0.0469 0.0001  -0.1295 222 PRO   C O   
4208 C  CB  . PRO   C 129 ? 0.6462 0.7700 0.6058 -0.0478 -0.0047 -0.1205 222 PRO   C CB  
4209 C  CG  . PRO   C 129 ? 0.6529 0.7714 0.6184 -0.0474 0.0035  -0.1384 222 PRO   C CG  
4210 C  CD  . PRO   C 129 ? 0.6357 0.7171 0.6079 -0.0408 0.0065  -0.1227 222 PRO   C CD  
4211 N  N   . PRO   C 130 ? 0.6545 0.7253 0.6398 -0.0498 -0.0112 -0.1147 223 PRO   C N   
4212 C  CA  . PRO   C 130 ? 0.6718 0.7277 0.6729 -0.0552 -0.0107 -0.1282 223 PRO   C CA  
4213 C  C   . PRO   C 130 ? 0.6949 0.7594 0.7054 -0.0623 -0.0055 -0.1588 223 PRO   C C   
4214 O  O   . PRO   C 130 ? 0.7065 0.8000 0.7076 -0.0636 -0.0046 -0.1697 223 PRO   C O   
4215 C  CB  . PRO   C 130 ? 0.6688 0.7484 0.6652 -0.0574 -0.0184 -0.1210 223 PRO   C CB  
4216 C  CG  . PRO   C 130 ? 0.6583 0.7513 0.6389 -0.0501 -0.0228 -0.0961 223 PRO   C CG  
4217 C  CD  . PRO   C 130 ? 0.6502 0.7494 0.6219 -0.0481 -0.0183 -0.0978 223 PRO   C CD  
4218 N  N   . GLU   C 131 ? 0.7210 0.7612 0.7509 -0.0668 -0.0017 -0.1724 224 GLU   C N   
4219 C  CA  . GLU   C 131 ? 0.7462 0.7929 0.7904 -0.0750 0.0032  -0.2042 224 GLU   C CA  
4220 C  C   . GLU   C 131 ? 0.7631 0.8508 0.8024 -0.0838 -0.0023 -0.2182 224 GLU   C C   
4221 O  O   . GLU   C 131 ? 0.7729 0.8725 0.8044 -0.0832 -0.0094 -0.2014 224 GLU   C O   
4222 C  CB  . GLU   C 131 ? 0.7500 0.7574 0.8190 -0.0780 0.0089  -0.2112 224 GLU   C CB  
4223 C  CG  . GLU   C 131 ? 0.7411 0.7102 0.8168 -0.0690 0.0140  -0.1969 224 GLU   C CG  
4224 C  CD  . GLU   C 131 ? 0.7478 0.6800 0.8448 -0.0707 0.0178  -0.1931 224 GLU   C CD  
4225 O  OE1 . GLU   C 131 ? 0.7688 0.6980 0.8839 -0.0798 0.0209  -0.2123 224 GLU   C OE1 
4226 O  OE2 . GLU   C 131 ? 0.7371 0.6453 0.8330 -0.0636 0.0177  -0.1707 224 GLU   C OE2 
4227 N  N   . VAL   C 132 ? 0.7848 0.8971 0.8284 -0.0913 0.0002  -0.2480 225 VAL   C N   
4228 C  CA  . VAL   C 132 ? 0.7896 0.9474 0.8282 -0.1005 -0.0057 -0.2635 225 VAL   C CA  
4229 C  C   . VAL   C 132 ? 0.7872 0.9297 0.8440 -0.1077 -0.0075 -0.2657 225 VAL   C C   
4230 O  O   . VAL   C 132 ? 0.8036 0.9137 0.8831 -0.1124 -0.0005 -0.2798 225 VAL   C O   
4231 C  CB  . VAL   C 132 ? 0.8159 1.0043 0.8568 -0.1078 -0.0018 -0.2988 225 VAL   C CB  
4232 C  CG1 . VAL   C 132 ? 0.8262 1.0614 0.8652 -0.1186 -0.0080 -0.3179 225 VAL   C CG1 
4233 C  CG2 . VAL   C 132 ? 0.8186 1.0282 0.8391 -0.1005 -0.0003 -0.2934 225 VAL   C CG2 
4234 N  N   . GLY   C 133 ? 0.7723 0.9368 0.8206 -0.1079 -0.0160 -0.2503 226 GLY   C N   
4235 C  CA  . GLY   C 133 ? 0.7580 0.9102 0.8219 -0.1134 -0.0180 -0.2471 226 GLY   C CA  
4236 C  C   . GLY   C 133 ? 0.7205 0.8509 0.7782 -0.1036 -0.0211 -0.2132 226 GLY   C C   
4237 O  O   . GLY   C 133 ? 0.7309 0.8756 0.7905 -0.1054 -0.0269 -0.2048 226 GLY   C O   
4238 N  N   . SER   C 134 ? 0.6984 0.7988 0.7495 -0.0936 -0.0177 -0.1953 227 SER   C N   
4239 C  CA  . SER   C 134 ? 0.6557 0.7323 0.7017 -0.0840 -0.0196 -0.1651 227 SER   C CA  
4240 C  C   . SER   C 134 ? 0.6379 0.7404 0.6629 -0.0757 -0.0265 -0.1451 227 SER   C C   
4241 O  O   . SER   C 134 ? 0.6259 0.7564 0.6384 -0.0755 -0.0277 -0.1513 227 SER   C O   
4242 C  CB  . SER   C 134 ? 0.6475 0.6821 0.6988 -0.0786 -0.0124 -0.1587 227 SER   C CB  
4243 O  OG  . SER   C 134 ? 0.6412 0.6558 0.6863 -0.0697 -0.0140 -0.1326 227 SER   C OG  
4244 N  N   . ASP   C 135 ? 0.6222 0.7154 0.6447 -0.0688 -0.0301 -0.1217 228 ASP   C N   
4245 C  CA  . ASP   C 135 ? 0.6123 0.7294 0.6198 -0.0610 -0.0370 -0.1010 228 ASP   C CA  
4246 C  C   . ASP   C 135 ? 0.5984 0.6892 0.5985 -0.0512 -0.0349 -0.0797 228 ASP   C C   
4247 O  O   . ASP   C 135 ? 0.6013 0.7079 0.5906 -0.0447 -0.0392 -0.0619 228 ASP   C O   
4248 C  CB  . ASP   C 135 ? 0.6155 0.7464 0.6284 -0.0600 -0.0431 -0.0919 228 ASP   C CB  
4249 C  CG  . ASP   C 135 ? 0.6206 0.7832 0.6415 -0.0702 -0.0463 -0.1119 228 ASP   C CG  
4250 O  OD1 . ASP   C 135 ? 0.6343 0.8286 0.6482 -0.0751 -0.0480 -0.1267 228 ASP   C OD1 
4251 O  OD2 . ASP   C 135 ? 0.6065 0.7644 0.6406 -0.0734 -0.0470 -0.1129 228 ASP   C OD2 
4252 N  N   . CYS   C 136 ? 0.5895 0.6432 0.5966 -0.0504 -0.0286 -0.0809 229 CYS   C N   
4253 C  CA  . CYS   C 136 ? 0.5744 0.6023 0.5773 -0.0420 -0.0269 -0.0620 229 CYS   C CA  
4254 C  C   . CYS   C 136 ? 0.5582 0.5604 0.5648 -0.0422 -0.0200 -0.0694 229 CYS   C C   
4255 O  O   . CYS   C 136 ? 0.5701 0.5676 0.5861 -0.0481 -0.0161 -0.0876 229 CYS   C O   
4256 C  CB  . CYS   C 136 ? 0.5684 0.5786 0.5779 -0.0382 -0.0284 -0.0486 229 CYS   C CB  
4257 S  SG  . CYS   C 136 ? 0.5791 0.5636 0.6051 -0.0438 -0.0235 -0.0591 229 CYS   C SG  
4258 N  N   . THR   C 137 ? 0.5384 0.5259 0.5394 -0.0358 -0.0185 -0.0557 230 THR   C N   
4259 C  CA  . THR   C 137 ? 0.5248 0.4877 0.5302 -0.0339 -0.0127 -0.0585 230 THR   C CA  
4260 C  C   . THR   C 137 ? 0.4990 0.4345 0.5100 -0.0298 -0.0123 -0.0460 230 THR   C C   
4261 O  O   . THR   C 137 ? 0.5098 0.4456 0.5159 -0.0256 -0.0157 -0.0309 230 THR   C O   
4262 C  CB  . THR   C 137 ? 0.5260 0.4982 0.5212 -0.0307 -0.0114 -0.0538 230 THR   C CB  
4263 O  OG1 . THR   C 137 ? 0.5384 0.5410 0.5274 -0.0350 -0.0118 -0.0664 230 THR   C OG1 
4264 C  CG2 . THR   C 137 ? 0.5261 0.4771 0.5268 -0.0281 -0.0059 -0.0567 230 THR   C CG2 
4265 N  N   . THR   C 138 ? 0.4708 0.3846 0.4925 -0.0308 -0.0080 -0.0517 231 THR   C N   
4266 C  CA  . THR   C 138 ? 0.4507 0.3419 0.4772 -0.0273 -0.0071 -0.0404 231 THR   C CA  
4267 C  C   . THR   C 138 ? 0.4423 0.3195 0.4681 -0.0222 -0.0042 -0.0356 231 THR   C C   
4268 O  O   . THR   C 138 ? 0.4322 0.3069 0.4627 -0.0226 -0.0004 -0.0453 231 THR   C O   
4269 C  CB  . THR   C 138 ? 0.4447 0.3242 0.4840 -0.0317 -0.0044 -0.0459 231 THR   C CB  
4270 O  OG1 . THR   C 138 ? 0.4405 0.3366 0.4811 -0.0368 -0.0074 -0.0506 231 THR   C OG1 
4271 C  CG2 . THR   C 138 ? 0.4385 0.3005 0.4811 -0.0283 -0.0034 -0.0335 231 THR   C CG2 
4272 N  N   . ILE   C 139 ? 0.4330 0.3042 0.4541 -0.0176 -0.0060 -0.0223 232 ILE   C N   
4273 C  CA  . ILE   C 139 ? 0.4292 0.2877 0.4511 -0.0130 -0.0042 -0.0163 232 ILE   C CA  
4274 C  C   . ILE   C 139 ? 0.4250 0.2698 0.4518 -0.0114 -0.0038 -0.0096 232 ILE   C C   
4275 O  O   . ILE   C 139 ? 0.4235 0.2706 0.4488 -0.0122 -0.0061 -0.0051 232 ILE   C O   
4276 C  CB  . ILE   C 139 ? 0.4342 0.2992 0.4480 -0.0104 -0.0063 -0.0080 232 ILE   C CB  
4277 C  CG1 . ILE   C 139 ? 0.4380 0.3198 0.4462 -0.0122 -0.0059 -0.0125 232 ILE   C CG1 
4278 C  CG2 . ILE   C 139 ? 0.4377 0.2922 0.4536 -0.0067 -0.0050 -0.0027 232 ILE   C CG2 
4279 C  CD1 . ILE   C 139 ? 0.4455 0.3349 0.4470 -0.0110 -0.0076 -0.0018 232 ILE   C CD1 
4280 N  N   . HIS   C 140 ? 0.4275 0.2609 0.4605 -0.0088 -0.0009 -0.0084 233 HIS   C N   
4281 C  CA  . HIS   C 140 ? 0.4356 0.2592 0.4724 -0.0067 -0.0002 -0.0001 233 HIS   C CA  
4282 C  C   . HIS   C 140 ? 0.4302 0.2548 0.4616 -0.0022 -0.0021 0.0074  233 HIS   C C   
4283 O  O   . HIS   C 140 ? 0.4345 0.2574 0.4684 0.0010  -0.0009 0.0077  233 HIS   C O   
4284 C  CB  . HIS   C 140 ? 0.4515 0.2632 0.5003 -0.0066 0.0040  -0.0017 233 HIS   C CB  
4285 C  CG  . HIS   C 140 ? 0.4666 0.2764 0.5232 -0.0128 0.0061  -0.0093 233 HIS   C CG  
4286 N  ND1 . HIS   C 140 ? 0.4924 0.2902 0.5633 -0.0143 0.0109  -0.0142 233 HIS   C ND1 
4287 C  CD2 . HIS   C 140 ? 0.4670 0.2856 0.5211 -0.0181 0.0042  -0.0133 233 HIS   C CD2 
4288 C  CE1 . HIS   C 140 ? 0.4899 0.2893 0.5668 -0.0215 0.0119  -0.0221 233 HIS   C CE1 
4289 N  NE2 . HIS   C 140 ? 0.4795 0.2934 0.5456 -0.0237 0.0076  -0.0217 233 HIS   C NE2 
4290 N  N   . TYR   C 141 ? 0.4249 0.2537 0.4507 -0.0022 -0.0049 0.0118  234 TYR   C N   
4291 C  CA  . TYR   C 141 ? 0.4185 0.2491 0.4409 0.0007  -0.0066 0.0166  234 TYR   C CA  
4292 C  C   . TYR   C 141 ? 0.4266 0.2557 0.4507 0.0027  -0.0058 0.0222  234 TYR   C C   
4293 O  O   . TYR   C 141 ? 0.4443 0.2718 0.4706 0.0010  -0.0044 0.0239  234 TYR   C O   
4294 C  CB  . TYR   C 141 ? 0.4054 0.2405 0.4238 0.0000  -0.0091 0.0169  234 TYR   C CB  
4295 C  CG  . TYR   C 141 ? 0.3981 0.2371 0.4144 -0.0013 -0.0098 0.0154  234 TYR   C CG  
4296 C  CD1 . TYR   C 141 ? 0.3883 0.2288 0.4043 -0.0007 -0.0093 0.0157  234 TYR   C CD1 
4297 C  CD2 . TYR   C 141 ? 0.3898 0.2340 0.4047 -0.0031 -0.0109 0.0143  234 TYR   C CD2 
4298 C  CE1 . TYR   C 141 ? 0.3948 0.2415 0.4085 -0.0024 -0.0092 0.0160  234 TYR   C CE1 
4299 C  CE2 . TYR   C 141 ? 0.3956 0.2472 0.4074 -0.0041 -0.0115 0.0150  234 TYR   C CE2 
4300 C  CZ  . TYR   C 141 ? 0.3984 0.2509 0.4093 -0.0039 -0.0103 0.0162  234 TYR   C CZ  
4301 O  OH  . TYR   C 141 ? 0.4085 0.2706 0.4160 -0.0054 -0.0101 0.0183  234 TYR   C OH  
4302 N  N   . ASN   C 142 ? 0.4364 0.2690 0.4597 0.0059  -0.0067 0.0254  235 ASN   C N   
4303 C  CA  . ASN   C 142 ? 0.4420 0.2803 0.4639 0.0080  -0.0072 0.0313  235 ASN   C CA  
4304 C  C   . ASN   C 142 ? 0.4355 0.2826 0.4530 0.0080  -0.0099 0.0282  235 ASN   C C   
4305 O  O   . ASN   C 142 ? 0.4356 0.2840 0.4539 0.0081  -0.0112 0.0254  235 ASN   C O   
4306 C  CB  . ASN   C 142 ? 0.4545 0.2933 0.4808 0.0123  -0.0063 0.0379  235 ASN   C CB  
4307 C  CG  . ASN   C 142 ? 0.4656 0.2929 0.5006 0.0128  -0.0027 0.0402  235 ASN   C CG  
4308 O  OD1 . ASN   C 142 ? 0.4805 0.3052 0.5224 0.0171  -0.0015 0.0444  235 ASN   C OD1 
4309 N  ND2 . ASN   C 142 ? 0.4698 0.2905 0.5064 0.0083  -0.0008 0.0367  235 ASN   C ND2 
4310 N  N   . TYR   C 143 ? 0.4450 0.2987 0.4593 0.0075  -0.0104 0.0278  236 TYR   C N   
4311 C  CA  . TYR   C 143 ? 0.4395 0.3030 0.4515 0.0073  -0.0124 0.0226  236 TYR   C CA  
4312 C  C   . TYR   C 143 ? 0.4465 0.3243 0.4556 0.0097  -0.0132 0.0270  236 TYR   C C   
4313 O  O   . TYR   C 143 ? 0.4621 0.3443 0.4691 0.0108  -0.0115 0.0339  236 TYR   C O   
4314 C  CB  . TYR   C 143 ? 0.4354 0.2989 0.4474 0.0058  -0.0119 0.0172  236 TYR   C CB  
4315 C  CG  . TYR   C 143 ? 0.4217 0.2745 0.4372 0.0045  -0.0120 0.0151  236 TYR   C CG  
4316 C  CD1 . TYR   C 143 ? 0.4130 0.2603 0.4291 0.0038  -0.0109 0.0181  236 TYR   C CD1 
4317 C  CD2 . TYR   C 143 ? 0.4181 0.2678 0.4373 0.0037  -0.0131 0.0105  236 TYR   C CD2 
4318 C  CE1 . TYR   C 143 ? 0.4128 0.2552 0.4309 0.0030  -0.0116 0.0171  236 TYR   C CE1 
4319 C  CE2 . TYR   C 143 ? 0.4107 0.2528 0.4329 0.0032  -0.0133 0.0119  236 TYR   C CE2 
4320 C  CZ  . TYR   C 143 ? 0.4121 0.2524 0.4328 0.0031  -0.0129 0.0154  236 TYR   C CZ  
4321 O  OH  . TYR   C 143 ? 0.3986 0.2362 0.4211 0.0029  -0.0136 0.0175  236 TYR   C OH  
4322 N  N   . MET   C 144 ? 0.4472 0.3341 0.4569 0.0103  -0.0157 0.0242  237 MET   C N   
4323 C  CA  . MET   C 144 ? 0.4603 0.3635 0.4681 0.0136  -0.0174 0.0302  237 MET   C CA  
4324 C  C   . MET   C 144 ? 0.4609 0.3850 0.4639 0.0123  -0.0195 0.0234  237 MET   C C   
4325 O  O   . MET   C 144 ? 0.4598 0.4030 0.4608 0.0146  -0.0220 0.0267  237 MET   C O   
4326 C  CB  . MET   C 144 ? 0.4590 0.3621 0.4721 0.0152  -0.0190 0.0308  237 MET   C CB  
4327 C  CG  . MET   C 144 ? 0.4655 0.3515 0.4838 0.0168  -0.0164 0.0351  237 MET   C CG  
4328 S  SD  . MET   C 144 ? 0.4718 0.3493 0.4920 0.0204  -0.0132 0.0472  237 MET   C SD  
4329 C  CE  . MET   C 144 ? 0.4765 0.3746 0.4965 0.0265  -0.0157 0.0585  237 MET   C CE  
4330 N  N   . CYS   C 145 ? 0.4786 0.4013 0.4807 0.0092  -0.0184 0.0137  238 CYS   C N   
4331 C  CA  . CYS   C 145 ? 0.4968 0.4394 0.4955 0.0075  -0.0193 0.0032  238 CYS   C CA  
4332 C  C   . CYS   C 145 ? 0.5083 0.4473 0.5057 0.0069  -0.0160 -0.0003 238 CYS   C C   
4333 O  O   . CYS   C 145 ? 0.4977 0.4165 0.4999 0.0064  -0.0143 0.0001  238 CYS   C O   
4334 C  CB  . CYS   C 145 ? 0.5084 0.4509 0.5139 0.0037  -0.0212 -0.0107 238 CYS   C CB  
4335 S  SG  . CYS   C 145 ? 0.5327 0.5049 0.5375 0.0008  -0.0242 -0.0251 238 CYS   C SG  
4336 N  N   . ASN   C 146 ? 0.5070 0.4675 0.4982 0.0071  -0.0152 -0.0034 239 ASN   C N   
4337 C  CA  . ASN   C 146 ? 0.5161 0.4786 0.5072 0.0067  -0.0116 -0.0097 239 ASN   C CA  
4338 C  C   . ASN   C 146 ? 0.5122 0.4706 0.5115 0.0048  -0.0116 -0.0286 239 ASN   C C   
4339 O  O   . ASN   C 146 ? 0.5051 0.4712 0.5069 0.0026  -0.0141 -0.0385 239 ASN   C O   
4340 C  CB  . ASN   C 146 ? 0.5304 0.5208 0.5119 0.0075  -0.0100 -0.0060 239 ASN   C CB  
4341 C  CG  . ASN   C 146 ? 0.5421 0.5302 0.5197 0.0091  -0.0078 0.0139  239 ASN   C CG  
4342 O  OD1 . ASN   C 146 ? 0.5478 0.5157 0.5305 0.0086  -0.0056 0.0195  239 ASN   C OD1 
4343 N  ND2 . ASN   C 146 ? 0.5507 0.5605 0.5206 0.0107  -0.0085 0.0253  239 ASN   C ND2 
4344 N  N   . SER   C 147 ? 0.5092 0.4560 0.5148 0.0055  -0.0087 -0.0333 240 SER   C N   
4345 C  CA  . SER   C 147 ? 0.5117 0.4531 0.5284 0.0050  -0.0075 -0.0506 240 SER   C CA  
4346 C  C   . SER   C 147 ? 0.5198 0.4871 0.5344 0.0036  -0.0071 -0.0669 240 SER   C C   
4347 O  O   . SER   C 147 ? 0.5416 0.5055 0.5668 0.0015  -0.0071 -0.0831 240 SER   C O   
4348 C  CB  . SER   C 147 ? 0.5081 0.4393 0.5315 0.0079  -0.0044 -0.0507 240 SER   C CB  
4349 O  OG  . SER   C 147 ? 0.5022 0.4127 0.5280 0.0086  -0.0055 -0.0379 240 SER   C OG  
4350 N  N   . SER   C 148 ? 0.5193 0.5128 0.5215 0.0042  -0.0063 -0.0627 241 SER   C N   
4351 C  CA  . SER   C 148 ? 0.5335 0.5600 0.5301 0.0029  -0.0056 -0.0775 241 SER   C CA  
4352 C  C   . SER   C 148 ? 0.5492 0.5923 0.5418 0.0000  -0.0103 -0.0815 241 SER   C C   
4353 O  O   . SER   C 148 ? 0.5744 0.6448 0.5651 -0.0021 -0.0104 -0.0990 241 SER   C O   
4354 C  CB  . SER   C 148 ? 0.5342 0.5845 0.5183 0.0046  -0.0028 -0.0676 241 SER   C CB  
4355 O  OG  . SER   C 148 ? 0.5288 0.5815 0.5032 0.0053  -0.0050 -0.0452 241 SER   C OG  
4356 N  N   . CYS   C 149 ? 0.5375 0.5683 0.5293 0.0000  -0.0140 -0.0673 242 CYS   C N   
4357 C  CA  . CYS   C 149 ? 0.5488 0.5992 0.5365 -0.0017 -0.0189 -0.0671 242 CYS   C CA  
4358 C  C   . CYS   C 149 ? 0.5597 0.6221 0.5558 -0.0069 -0.0201 -0.0926 242 CYS   C C   
4359 O  O   . CYS   C 149 ? 0.5402 0.5772 0.5510 -0.0098 -0.0193 -0.1019 242 CYS   C O   
4360 C  CB  . CYS   C 149 ? 0.5300 0.5586 0.5215 -0.0009 -0.0215 -0.0526 242 CYS   C CB  
4361 S  SG  . CYS   C 149 ? 0.5291 0.5569 0.5110 0.0045  -0.0219 -0.0249 242 CYS   C SG  
4362 N  N   . MET   C 150 ? 0.5814 0.6826 0.5692 -0.0084 -0.0218 -0.1026 243 MET   C N   
4363 C  CA  . MET   C 150 ? 0.6148 0.7360 0.6098 -0.0145 -0.0239 -0.1283 243 MET   C CA  
4364 C  C   . MET   C 150 ? 0.5972 0.7089 0.6001 -0.0177 -0.0285 -0.1248 243 MET   C C   
4365 O  O   . MET   C 150 ? 0.5784 0.6948 0.5733 -0.0139 -0.0319 -0.1037 243 MET   C O   
4366 C  CB  . MET   C 150 ? 0.6495 0.8216 0.6302 -0.0150 -0.0262 -0.1353 243 MET   C CB  
4367 C  CG  . MET   C 150 ? 0.6733 0.8636 0.6443 -0.0123 -0.0213 -0.1387 243 MET   C CG  
4368 S  SD  . MET   C 150 ? 0.7202 0.9765 0.6698 -0.0121 -0.0241 -0.1394 243 MET   C SD  
4369 C  CE  . MET   C 150 ? 0.7369 1.0183 0.6961 -0.0203 -0.0286 -0.1728 243 MET   C CE  
4370 N  N   . GLY   C 151 ? 0.5961 0.6937 0.6164 -0.0241 -0.0278 -0.1440 244 GLY   C N   
4371 C  CA  . GLY   C 151 ? 0.5941 0.6849 0.6243 -0.0287 -0.0313 -0.1431 244 GLY   C CA  
4372 C  C   . GLY   C 151 ? 0.5834 0.6375 0.6171 -0.0255 -0.0302 -0.1219 244 GLY   C C   
4373 O  O   . GLY   C 151 ? 0.5937 0.6470 0.6312 -0.0272 -0.0331 -0.1147 244 GLY   C O   
4374 N  N   . GLY   C 152 ? 0.5858 0.6139 0.6185 -0.0211 -0.0261 -0.1130 245 GLY   C N   
4375 C  CA  . GLY   C 152 ? 0.5786 0.5722 0.6154 -0.0187 -0.0244 -0.0962 245 GLY   C CA  
4376 C  C   . GLY   C 152 ? 0.5779 0.5444 0.6255 -0.0186 -0.0198 -0.1020 245 GLY   C C   
4377 O  O   . GLY   C 152 ? 0.5949 0.5570 0.6570 -0.0235 -0.0181 -0.1201 245 GLY   C O   
4378 N  N   . MET   C 153 ? 0.5682 0.5185 0.6106 -0.0131 -0.0177 -0.0879 246 MET   C N   
4379 C  CA  . MET   C 153 ? 0.5657 0.4937 0.6182 -0.0112 -0.0138 -0.0913 246 MET   C CA  
4380 C  C   . MET   C 153 ? 0.5762 0.5190 0.6321 -0.0110 -0.0113 -0.1108 246 MET   C C   
4381 O  O   . MET   C 153 ? 0.5851 0.5121 0.6574 -0.0114 -0.0081 -0.1226 246 MET   C O   
4382 C  CB  . MET   C 153 ? 0.5570 0.4726 0.6015 -0.0057 -0.0129 -0.0731 246 MET   C CB  
4383 C  CG  . MET   C 153 ? 0.5484 0.4482 0.5920 -0.0060 -0.0144 -0.0573 246 MET   C CG  
4384 S  SD  . MET   C 153 ? 0.5367 0.4216 0.5750 -0.0010 -0.0131 -0.0410 246 MET   C SD  
4385 C  CE  . MET   C 153 ? 0.5321 0.4357 0.5546 0.0012  -0.0141 -0.0314 246 MET   C CE  
4386 N  N   . ASN   C 154 ? 0.5856 0.5588 0.6276 -0.0101 -0.0123 -0.1137 247 ASN   C N   
4387 C  CA  . ASN   C 154 ? 0.6092 0.6065 0.6515 -0.0108 -0.0100 -0.1347 247 ASN   C CA  
4388 C  C   . ASN   C 154 ? 0.6162 0.5967 0.6698 -0.0069 -0.0050 -0.1414 247 ASN   C C   
4389 O  O   . ASN   C 154 ? 0.6329 0.6094 0.7028 -0.0087 -0.0022 -0.1629 247 ASN   C O   
4390 C  CB  . ASN   C 154 ? 0.6298 0.6408 0.6817 -0.0177 -0.0115 -0.1571 247 ASN   C CB  
4391 C  CG  . ASN   C 154 ? 0.6527 0.6943 0.7034 -0.0189 -0.0093 -0.1811 247 ASN   C CG  
4392 O  OD1 . ASN   C 154 ? 0.6689 0.7358 0.7037 -0.0153 -0.0087 -0.1767 247 ASN   C OD1 
4393 N  ND2 . ASN   C 154 ? 0.6684 0.7089 0.7368 -0.0243 -0.0077 -0.2070 247 ASN   C ND2 
4394 N  N   . ARG   C 155 ? 0.6019 0.5729 0.6489 -0.0017 -0.0038 -0.1238 248 ARG   C N   
4395 C  CA  . ARG   C 155 ? 0.6072 0.5704 0.6615 0.0033  0.0006  -0.1265 248 ARG   C CA  
4396 C  C   . ARG   C 155 ? 0.5880 0.5175 0.6620 0.0051  0.0017  -0.1259 248 ARG   C C   
4397 O  O   . ARG   C 155 ? 0.5998 0.5211 0.6822 0.0103  0.0047  -0.1262 248 ARG   C O   
4398 C  CB  . ARG   C 155 ? 0.6255 0.6151 0.6810 0.0037  0.0043  -0.1487 248 ARG   C CB  
4399 C  CG  . ARG   C 155 ? 0.6434 0.6704 0.6780 0.0021  0.0032  -0.1459 248 ARG   C CG  
4400 C  CD  . ARG   C 155 ? 0.6675 0.7274 0.6998 0.0025  0.0073  -0.1666 248 ARG   C CD  
4401 N  NE  . ARG   C 155 ? 0.6781 0.7525 0.6999 0.0063  0.0108  -0.1552 248 ARG   C NE  
4402 C  CZ  . ARG   C 155 ? 0.6902 0.7525 0.7221 0.0109  0.0152  -0.1558 248 ARG   C CZ  
4403 N  NH1 . ARG   C 155 ? 0.7035 0.7376 0.7562 0.0136  0.0164  -0.1656 248 ARG   C NH1 
4404 N  NH2 . ARG   C 155 ? 0.6875 0.7668 0.7098 0.0130  0.0185  -0.1453 248 ARG   C NH2 
4405 N  N   . ARG   C 156 ? 0.5792 0.4914 0.6604 0.0011  -0.0006 -0.1232 249 ARG   C N   
4406 C  CA  . ARG   C 156 ? 0.5633 0.4443 0.6628 0.0025  0.0004  -0.1183 249 ARG   C CA  
4407 C  C   . ARG   C 156 ? 0.5347 0.4031 0.6264 0.0061  -0.0013 -0.0946 249 ARG   C C   
4408 O  O   . ARG   C 156 ? 0.5383 0.4115 0.6153 0.0040  -0.0042 -0.0817 249 ARG   C O   
4409 C  CB  . ARG   C 156 ? 0.5661 0.4364 0.6765 -0.0042 -0.0006 -0.1237 249 ARG   C CB  
4410 C  CG  . ARG   C 156 ? 0.5827 0.4656 0.7041 -0.0090 0.0012  -0.1505 249 ARG   C CG  
4411 C  CD  . ARG   C 156 ? 0.5818 0.4573 0.7140 -0.0174 0.0000  -0.1555 249 ARG   C CD  
4412 N  NE  . ARG   C 156 ? 0.5772 0.4705 0.6914 -0.0211 -0.0047 -0.1463 249 ARG   C NE  
4413 C  CZ  . ARG   C 156 ? 0.5783 0.4715 0.6980 -0.0285 -0.0066 -0.1477 249 ARG   C CZ  
4414 N  NH1 . ARG   C 156 ? 0.5918 0.4666 0.7346 -0.0342 -0.0039 -0.1577 249 ARG   C NH1 
4415 N  NH2 . ARG   C 156 ? 0.5584 0.4699 0.6622 -0.0300 -0.0109 -0.1384 249 ARG   C NH2 
4416 N  N   . PRO   C 157 ? 0.5105 0.3639 0.6130 0.0117  0.0004  -0.0888 250 PRO   C N   
4417 C  CA  . PRO   C 157 ? 0.4870 0.3317 0.5828 0.0146  -0.0015 -0.0685 250 PRO   C CA  
4418 C  C   . PRO   C 157 ? 0.4869 0.3153 0.5846 0.0111  -0.0037 -0.0564 250 PRO   C C   
4419 O  O   . PRO   C 157 ? 0.5135 0.3297 0.6256 0.0085  -0.0026 -0.0617 250 PRO   C O   
4420 C  CB  . PRO   C 157 ? 0.4923 0.3296 0.6025 0.0219  0.0006  -0.0684 250 PRO   C CB  
4421 C  CG  . PRO   C 157 ? 0.5124 0.3414 0.6433 0.0225  0.0039  -0.0859 250 PRO   C CG  
4422 C  CD  . PRO   C 157 ? 0.5180 0.3637 0.6411 0.0162  0.0042  -0.1023 250 PRO   C CD  
4423 N  N   . ILE   C 158 ? 0.4594 0.2887 0.5441 0.0108  -0.0061 -0.0412 251 ILE   C N   
4424 C  CA  . ILE   C 158 ? 0.4519 0.2705 0.5354 0.0077  -0.0078 -0.0289 251 ILE   C CA  
4425 C  C   . ILE   C 158 ? 0.4483 0.2616 0.5301 0.0116  -0.0089 -0.0142 251 ILE   C C   
4426 O  O   . ILE   C 158 ? 0.4493 0.2700 0.5270 0.0154  -0.0091 -0.0130 251 ILE   C O   
4427 C  CB  . ILE   C 158 ? 0.4420 0.2706 0.5115 0.0033  -0.0097 -0.0272 251 ILE   C CB  
4428 C  CG1 . ILE   C 158 ? 0.4316 0.2720 0.4864 0.0052  -0.0106 -0.0222 251 ILE   C CG1 
4429 C  CG2 . ILE   C 158 ? 0.4494 0.2859 0.5224 -0.0008 -0.0094 -0.0414 251 ILE   C CG2 
4430 C  CD1 . ILE   C 158 ? 0.4252 0.2692 0.4695 0.0028  -0.0123 -0.0145 251 ILE   C CD1 
4431 N  N   . LEU   C 159 ? 0.4601 0.2635 0.5460 0.0102  -0.0095 -0.0037 252 LEU   C N   
4432 C  CA  . LEU   C 159 ? 0.4496 0.2535 0.5299 0.0122  -0.0113 0.0109  252 LEU   C CA  
4433 C  C   . LEU   C 159 ? 0.4400 0.2485 0.5075 0.0073  -0.0123 0.0155  252 LEU   C C   
4434 O  O   . LEU   C 159 ? 0.4235 0.2299 0.4926 0.0029  -0.0115 0.0119  252 LEU   C O   
4435 C  CB  . LEU   C 159 ? 0.4680 0.2605 0.5624 0.0147  -0.0107 0.0211  252 LEU   C CB  
4436 C  CG  . LEU   C 159 ? 0.4883 0.2721 0.6013 0.0201  -0.0088 0.0157  252 LEU   C CG  
4437 C  CD1 . LEU   C 159 ? 0.5069 0.2773 0.6359 0.0225  -0.0079 0.0291  252 LEU   C CD1 
4438 C  CD2 . LEU   C 159 ? 0.4835 0.2774 0.5947 0.0264  -0.0097 0.0132  252 LEU   C CD2 
4439 N  N   . THR   C 160 ? 0.4332 0.2492 0.4902 0.0080  -0.0138 0.0218  253 THR   C N   
4440 C  CA  . THR   C 160 ? 0.4293 0.2493 0.4770 0.0047  -0.0143 0.0275  253 THR   C CA  
4441 C  C   . THR   C 160 ? 0.4378 0.2582 0.4877 0.0056  -0.0150 0.0392  253 THR   C C   
4442 O  O   . THR   C 160 ? 0.4442 0.2685 0.4957 0.0095  -0.0165 0.0434  253 THR   C O   
4443 C  CB  . THR   C 160 ? 0.4214 0.2496 0.4582 0.0044  -0.0151 0.0255  253 THR   C CB  
4444 O  OG1 . THR   C 160 ? 0.4254 0.2549 0.4603 0.0042  -0.0144 0.0180  253 THR   C OG1 
4445 C  CG2 . THR   C 160 ? 0.4171 0.2494 0.4469 0.0016  -0.0148 0.0286  253 THR   C CG2 
4446 N  N   . ILE   C 161 ? 0.4398 0.2593 0.4899 0.0021  -0.0138 0.0449  254 ILE   C N   
4447 C  CA  . ILE   C 161 ? 0.4469 0.2708 0.4970 0.0022  -0.0140 0.0584  254 ILE   C CA  
4448 C  C   . ILE   C 161 ? 0.4481 0.2852 0.4850 -0.0005 -0.0140 0.0584  254 ILE   C C   
4449 O  O   . ILE   C 161 ? 0.4396 0.2765 0.4741 -0.0040 -0.0123 0.0531  254 ILE   C O   
4450 C  CB  . ILE   C 161 ? 0.4615 0.2756 0.5238 -0.0002 -0.0115 0.0655  254 ILE   C CB  
4451 C  CG1 . ILE   C 161 ? 0.4661 0.2653 0.5443 0.0023  -0.0106 0.0611  254 ILE   C CG1 
4452 C  CG2 . ILE   C 161 ? 0.4773 0.2983 0.5391 0.0000  -0.0113 0.0825  254 ILE   C CG2 
4453 C  CD1 . ILE   C 161 ? 0.4773 0.2640 0.5704 -0.0021 -0.0074 0.0627  254 ILE   C CD1 
4454 N  N   . ILE   C 162 ? 0.4565 0.3060 0.4864 0.0011  -0.0160 0.0620  255 ILE   C N   
4455 C  CA  . ILE   C 162 ? 0.4585 0.3229 0.4769 -0.0015 -0.0158 0.0598  255 ILE   C CA  
4456 C  C   . ILE   C 162 ? 0.4836 0.3602 0.4999 -0.0022 -0.0155 0.0732  255 ILE   C C   
4457 O  O   . ILE   C 162 ? 0.4866 0.3696 0.5049 0.0011  -0.0181 0.0829  255 ILE   C O   
4458 C  CB  . ILE   C 162 ? 0.4496 0.3227 0.4626 -0.0005 -0.0180 0.0525  255 ILE   C CB  
4459 C  CG1 . ILE   C 162 ? 0.4420 0.3041 0.4583 0.0005  -0.0180 0.0432  255 ILE   C CG1 
4460 C  CG2 . ILE   C 162 ? 0.4414 0.3284 0.4452 -0.0037 -0.0170 0.0466  255 ILE   C CG2 
4461 C  CD1 . ILE   C 162 ? 0.4346 0.2885 0.4503 -0.0013 -0.0155 0.0364  255 ILE   C CD1 
4462 N  N   . THR   C 163 ? 0.5072 0.3885 0.5206 -0.0062 -0.0125 0.0749  256 THR   C N   
4463 C  CA  . THR   C 163 ? 0.5190 0.4153 0.5291 -0.0079 -0.0112 0.0887  256 THR   C CA  
4464 C  C   . THR   C 163 ? 0.5292 0.4472 0.5264 -0.0104 -0.0102 0.0814  256 THR   C C   
4465 O  O   . THR   C 163 ? 0.5267 0.4419 0.5220 -0.0120 -0.0083 0.0677  256 THR   C O   
4466 C  CB  . THR   C 163 ? 0.5366 0.4234 0.5557 -0.0114 -0.0074 0.0973  256 THR   C CB  
4467 O  OG1 . THR   C 163 ? 0.5385 0.4238 0.5562 -0.0149 -0.0047 0.0853  256 THR   C OG1 
4468 C  CG2 . THR   C 163 ? 0.5383 0.4032 0.5728 -0.0094 -0.0078 0.1014  256 THR   C CG2 
4469 N  N   . LEU   C 164 ? 0.5362 0.4762 0.5258 -0.0101 -0.0116 0.0901  257 LEU   C N   
4470 C  CA  . LEU   C 164 ? 0.5437 0.5102 0.5210 -0.0130 -0.0102 0.0836  257 LEU   C CA  
4471 C  C   . LEU   C 164 ? 0.5603 0.5390 0.5357 -0.0163 -0.0059 0.0970  257 LEU   C C   
4472 O  O   . LEU   C 164 ? 0.5609 0.5402 0.5402 -0.0153 -0.0065 0.1167  257 LEU   C O   
4473 C  CB  . LEU   C 164 ? 0.5503 0.5377 0.5206 -0.0111 -0.0148 0.0848  257 LEU   C CB  
4474 C  CG  . LEU   C 164 ? 0.5560 0.5722 0.5142 -0.0143 -0.0143 0.0717  257 LEU   C CG  
4475 C  CD1 . LEU   C 164 ? 0.5413 0.5463 0.5018 -0.0156 -0.0133 0.0485  257 LEU   C CD1 
4476 C  CD2 . LEU   C 164 ? 0.5734 0.6179 0.5245 -0.0129 -0.0193 0.0791  257 LEU   C CD2 
4477 N  N   . GLU   C 165 ? 0.5697 0.5552 0.5420 -0.0199 -0.0013 0.0877  258 GLU   C N   
4478 C  CA  . GLU   C 165 ? 0.5886 0.5872 0.5602 -0.0240 0.0037  0.0997  258 GLU   C CA  
4479 C  C   . GLU   C 165 ? 0.5888 0.6184 0.5482 -0.0264 0.0070  0.0894  258 GLU   C C   
4480 O  O   . GLU   C 165 ? 0.5687 0.5999 0.5250 -0.0253 0.0065  0.0690  258 GLU   C O   
4481 C  CB  . GLU   C 165 ? 0.5829 0.5609 0.5666 -0.0265 0.0073  0.0987  258 GLU   C CB  
4482 C  CG  . GLU   C 165 ? 0.5851 0.5360 0.5771 -0.0239 0.0049  0.0859  258 GLU   C CG  
4483 C  CD  . GLU   C 165 ? 0.5839 0.5215 0.5872 -0.0270 0.0080  0.0844  258 GLU   C CD  
4484 O  OE1 . GLU   C 165 ? 0.5766 0.5255 0.5787 -0.0290 0.0118  0.0765  258 GLU   C OE1 
4485 O  OE2 . GLU   C 165 ? 0.5988 0.5168 0.6131 -0.0275 0.0069  0.0904  258 GLU   C OE2 
4486 N  N   . ASP   C 166 ? 0.6110 0.6644 0.5649 -0.0299 0.0109  0.1032  259 ASP   C N   
4487 C  CA  . ASP   C 166 ? 0.6245 0.7114 0.5671 -0.0328 0.0155  0.0933  259 ASP   C CA  
4488 C  C   . ASP   C 166 ? 0.6183 0.6965 0.5689 -0.0347 0.0212  0.0813  259 ASP   C C   
4489 O  O   . ASP   C 166 ? 0.6178 0.6663 0.5810 -0.0341 0.0206  0.0822  259 ASP   C O   
4490 C  CB  . ASP   C 166 ? 0.6579 0.7778 0.5908 -0.0356 0.0176  0.1143  259 ASP   C CB  
4491 C  CG  . ASP   C 166 ? 0.6749 0.7894 0.6162 -0.0397 0.0227  0.1364  259 ASP   C CG  
4492 O  OD1 . ASP   C 166 ? 0.6705 0.7606 0.6247 -0.0414 0.0254  0.1316  259 ASP   C OD1 
4493 O  OD2 . ASP   C 166 ? 0.7070 0.8431 0.6429 -0.0414 0.0238  0.1591  259 ASP   C OD2 
4494 N  N   . SER   C 167 ? 0.6192 0.7248 0.5631 -0.0366 0.0264  0.0697  260 SER   C N   
4495 C  CA  . SER   C 167 ? 0.6141 0.7173 0.5660 -0.0372 0.0321  0.0558  260 SER   C CA  
4496 C  C   . SER   C 167 ? 0.6140 0.7090 0.5761 -0.0413 0.0356  0.0727  260 SER   C C   
4497 O  O   . SER   C 167 ? 0.6045 0.6868 0.5778 -0.0408 0.0378  0.0636  260 SER   C O   
4498 C  CB  . SER   C 167 ? 0.6192 0.7575 0.5623 -0.0380 0.0375  0.0404  260 SER   C CB  
4499 O  OG  . SER   C 167 ? 0.6310 0.8030 0.5631 -0.0427 0.0409  0.0566  260 SER   C OG  
4500 N  N   . SER   C 168 ? 0.6353 0.7369 0.5954 -0.0452 0.0361  0.0968  261 SER   C N   
4501 C  CA  . SER   C 168 ? 0.6451 0.7390 0.6174 -0.0509 0.0403  0.1146  261 SER   C CA  
4502 C  C   . SER   C 168 ? 0.6337 0.6888 0.6200 -0.0500 0.0355  0.1216  261 SER   C C   
4503 O  O   . SER   C 168 ? 0.6319 0.6761 0.6317 -0.0552 0.0387  0.1322  261 SER   C O   
4504 C  CB  . SER   C 168 ? 0.6663 0.7868 0.6320 -0.0559 0.0443  0.1384  261 SER   C CB  
4505 O  OG  . SER   C 168 ? 0.6815 0.8418 0.6344 -0.0576 0.0498  0.1307  261 SER   C OG  
4506 N  N   . GLY   C 169 ? 0.6286 0.6652 0.6129 -0.0442 0.0288  0.1148  262 GLY   C N   
4507 C  CA  . GLY   C 169 ? 0.6176 0.6199 0.6143 -0.0424 0.0243  0.1186  262 GLY   C CA  
4508 C  C   . GLY   C 169 ? 0.6334 0.6299 0.6321 -0.0418 0.0220  0.1406  262 GLY   C C   
4509 O  O   . GLY   C 169 ? 0.6479 0.6167 0.6595 -0.0406 0.0195  0.1445  262 GLY   C O   
4510 N  N   . ASN   C 170 ? 0.6427 0.6658 0.6298 -0.0417 0.0226  0.1542  263 ASN   C N   
4511 C  CA  . ASN   C 170 ? 0.6494 0.6708 0.6386 -0.0394 0.0199  0.1779  263 ASN   C CA  
4512 C  C   . ASN   C 170 ? 0.6285 0.6380 0.6153 -0.0319 0.0123  0.1696  263 ASN   C C   
4513 O  O   . ASN   C 170 ? 0.6119 0.6339 0.5868 -0.0296 0.0097  0.1512  263 ASN   C O   
4514 C  CB  . ASN   C 170 ? 0.6691 0.7282 0.6454 -0.0412 0.0225  0.1963  263 ASN   C CB  
4515 C  CG  . ASN   C 170 ? 0.6844 0.7570 0.6642 -0.0493 0.0309  0.2072  263 ASN   C CG  
4516 O  OD1 . ASN   C 170 ? 0.6872 0.7384 0.6845 -0.0536 0.0343  0.2203  263 ASN   C OD1 
4517 N  ND2 . ASN   C 170 ? 0.6798 0.7889 0.6444 -0.0519 0.0347  0.2008  263 ASN   C ND2 
4518 N  N   . LEU   C 171 ? 0.6226 0.6078 0.6227 -0.0285 0.0095  0.1815  264 LEU   C N   
4519 C  CA  . LEU   C 171 ? 0.6133 0.5861 0.6147 -0.0212 0.0028  0.1756  264 LEU   C CA  
4520 C  C   . LEU   C 171 ? 0.6118 0.6160 0.5981 -0.0174 -0.0013 0.1818  264 LEU   C C   
4521 O  O   . LEU   C 171 ? 0.6284 0.6508 0.6127 -0.0172 -0.0005 0.2048  264 LEU   C O   
4522 C  CB  . LEU   C 171 ? 0.6198 0.5638 0.6411 -0.0185 0.0023  0.1898  264 LEU   C CB  
4523 C  CG  . LEU   C 171 ? 0.6219 0.5541 0.6479 -0.0104 -0.0036 0.1872  264 LEU   C CG  
4524 C  CD1 . LEU   C 171 ? 0.6060 0.5207 0.6326 -0.0097 -0.0054 0.1615  264 LEU   C CD1 
4525 C  CD2 . LEU   C 171 ? 0.6376 0.5484 0.6843 -0.0068 -0.0030 0.2064  264 LEU   C CD2 
4526 N  N   . LEU   C 172 ? 0.5997 0.6110 0.5767 -0.0150 -0.0055 0.1622  265 LEU   C N   
4527 C  CA  . LEU   C 172 ? 0.6172 0.6586 0.5817 -0.0117 -0.0107 0.1634  265 LEU   C CA  
4528 C  C   . LEU   C 172 ? 0.6162 0.6429 0.5890 -0.0050 -0.0169 0.1638  265 LEU   C C   
4529 O  O   . LEU   C 172 ? 0.6502 0.6986 0.6193 -0.0007 -0.0216 0.1758  265 LEU   C O   
4530 C  CB  . LEU   C 172 ? 0.6041 0.6652 0.5548 -0.0150 -0.0104 0.1384  265 LEU   C CB  
4531 C  CG  . LEU   C 172 ? 0.6125 0.6882 0.5562 -0.0208 -0.0037 0.1325  265 LEU   C CG  
4532 C  CD1 . LEU   C 172 ? 0.6101 0.7064 0.5427 -0.0229 -0.0035 0.1066  265 LEU   C CD1 
4533 C  CD2 . LEU   C 172 ? 0.6356 0.7384 0.5735 -0.0229 -0.0010 0.1566  265 LEU   C CD2 
4534 N  N   . GLY   C 173 ? 0.6050 0.6001 0.5883 -0.0040 -0.0169 0.1502  266 GLY   C N   
4535 C  CA  . GLY   C 173 ? 0.5979 0.5794 0.5896 0.0018  -0.0217 0.1467  266 GLY   C CA  
4536 C  C   . GLY   C 173 ? 0.5857 0.5323 0.5898 0.0019  -0.0197 0.1360  266 GLY   C C   
4537 O  O   . GLY   C 173 ? 0.6102 0.5472 0.6128 -0.0028 -0.0159 0.1245  266 GLY   C O   
4538 N  N   . ARG   C 174 ? 0.5745 0.5052 0.5911 0.0076  -0.0222 0.1392  267 ARG   C N   
4539 C  CA  . ARG   C 174 ? 0.5540 0.4555 0.5821 0.0082  -0.0207 0.1276  267 ARG   C CA  
4540 C  C   . ARG   C 174 ? 0.5462 0.4446 0.5803 0.0143  -0.0246 0.1226  267 ARG   C C   
4541 O  O   . ARG   C 174 ? 0.5650 0.4735 0.6039 0.0202  -0.0278 0.1359  267 ARG   C O   
4542 C  CB  . ARG   C 174 ? 0.5685 0.4489 0.6122 0.0079  -0.0170 0.1387  267 ARG   C CB  
4543 C  CG  . ARG   C 174 ? 0.5574 0.4123 0.6119 0.0071  -0.0151 0.1243  267 ARG   C CG  
4544 C  CD  . ARG   C 174 ? 0.5737 0.4079 0.6480 0.0074  -0.0119 0.1339  267 ARG   C CD  
4545 N  NE  . ARG   C 174 ? 0.5791 0.4146 0.6545 0.0009  -0.0079 0.1443  267 ARG   C NE  
4546 C  CZ  . ARG   C 174 ? 0.6008 0.4380 0.6841 0.0011  -0.0059 0.1665  267 ARG   C CZ  
4547 N  NH1 . ARG   C 174 ? 0.6077 0.4454 0.6995 0.0089  -0.0083 0.1821  267 ARG   C NH1 
4548 N  NH2 . ARG   C 174 ? 0.6045 0.4442 0.6885 -0.0061 -0.0014 0.1742  267 ARG   C NH2 
4549 N  N   A ASN   C 175 ? 0.5267 0.4135 0.5608 0.0131  -0.0241 0.1050  268 ASN   C N   
4550 N  N   B ASN   C 175 ? 0.5253 0.4126 0.5593 0.0132  -0.0242 0.1049  268 ASN   C N   
4551 C  CA  A ASN   C 175 ? 0.5192 0.4001 0.5611 0.0181  -0.0262 0.0983  268 ASN   C CA  
4552 C  CA  B ASN   C 175 ? 0.5183 0.3982 0.5614 0.0185  -0.0262 0.0994  268 ASN   C CA  
4553 C  C   A ASN   C 175 ? 0.5074 0.3669 0.5551 0.0164  -0.0232 0.0855  268 ASN   C C   
4554 C  C   B ASN   C 175 ? 0.5060 0.3656 0.5536 0.0164  -0.0232 0.0854  268 ASN   C C   
4555 O  O   A ASN   C 175 ? 0.5148 0.3668 0.5597 0.0115  -0.0203 0.0817  268 ASN   C O   
4556 O  O   B ASN   C 175 ? 0.5122 0.3647 0.5564 0.0114  -0.0204 0.0813  268 ASN   C O   
4557 C  CB  A ASN   C 175 ? 0.5137 0.4133 0.5461 0.0173  -0.0294 0.0894  268 ASN   C CB  
4558 C  CB  B ASN   C 175 ? 0.5134 0.4132 0.5496 0.0196  -0.0301 0.0937  268 ASN   C CB  
4559 C  CG  A ASN   C 175 ? 0.5195 0.4444 0.5487 0.0202  -0.0336 0.1009  268 ASN   C CG  
4560 C  CG  B ASN   C 175 ? 0.5161 0.4211 0.5636 0.0275  -0.0334 0.1015  268 ASN   C CG  
4561 O  OD1 A ASN   C 175 ? 0.5273 0.4568 0.5658 0.0268  -0.0366 0.1088  268 ASN   C OD1 
4562 O  OD1 B ASN   C 175 ? 0.5130 0.4010 0.5745 0.0323  -0.0319 0.1029  268 ASN   C OD1 
4563 N  ND2 A ASN   C 175 ? 0.5223 0.4662 0.5386 0.0156  -0.0340 0.1013  268 ASN   C ND2 
4564 N  ND2 B ASN   C 175 ? 0.5194 0.4498 0.5621 0.0291  -0.0378 0.1061  268 ASN   C ND2 
4565 N  N   . SER   C 176 ? 0.4986 0.3521 0.5542 0.0205  -0.0238 0.0788  269 SER   C N   
4566 C  CA  . SER   C 176 ? 0.4781 0.3159 0.5392 0.0196  -0.0211 0.0665  269 SER   C CA  
4567 C  C   . SER   C 176 ? 0.4558 0.2985 0.5182 0.0227  -0.0221 0.0576  269 SER   C C   
4568 O  O   . SER   C 176 ? 0.4509 0.3057 0.5154 0.0267  -0.0248 0.0625  269 SER   C O   
4569 C  CB  . SER   C 176 ? 0.4931 0.3145 0.5697 0.0217  -0.0188 0.0705  269 SER   C CB  
4570 O  OG  . SER   C 176 ? 0.5041 0.3255 0.5936 0.0292  -0.0201 0.0794  269 SER   C OG  
4571 N  N   . PHE   C 177 ? 0.4425 0.2791 0.5037 0.0205  -0.0200 0.0455  270 PHE   C N   
4572 C  CA  . PHE   C 177 ? 0.4315 0.2725 0.4949 0.0227  -0.0195 0.0368  270 PHE   C CA  
4573 C  C   . PHE   C 177 ? 0.4282 0.2604 0.4939 0.0213  -0.0166 0.0263  270 PHE   C C   
4574 O  O   . PHE   C 177 ? 0.4246 0.2516 0.4850 0.0168  -0.0157 0.0243  270 PHE   C O   
4575 C  CB  . PHE   C 177 ? 0.4152 0.2685 0.4679 0.0191  -0.0206 0.0342  270 PHE   C CB  
4576 C  CG  . PHE   C 177 ? 0.4053 0.2562 0.4471 0.0132  -0.0196 0.0311  270 PHE   C CG  
4577 C  CD1 . PHE   C 177 ? 0.4069 0.2604 0.4425 0.0106  -0.0205 0.0360  270 PHE   C CD1 
4578 C  CD2 . PHE   C 177 ? 0.4033 0.2514 0.4417 0.0108  -0.0174 0.0239  270 PHE   C CD2 
4579 C  CE1 . PHE   C 177 ? 0.4006 0.2525 0.4287 0.0062  -0.0191 0.0322  270 PHE   C CE1 
4580 C  CE2 . PHE   C 177 ? 0.3968 0.2428 0.4276 0.0069  -0.0164 0.0225  270 PHE   C CE2 
4581 C  CZ  . PHE   C 177 ? 0.3967 0.2436 0.4232 0.0049  -0.0172 0.0259  270 PHE   C CZ  
4582 N  N   . GLU   C 178 ? 0.4259 0.2592 0.5003 0.0253  -0.0151 0.0193  271 GLU   C N   
4583 C  CA  . GLU   C 178 ? 0.4287 0.2605 0.5041 0.0241  -0.0123 0.0069  271 GLU   C CA  
4584 C  C   . GLU   C 178 ? 0.4199 0.2613 0.4811 0.0196  -0.0120 0.0041  271 GLU   C C   
4585 O  O   . GLU   C 178 ? 0.4080 0.2566 0.4640 0.0188  -0.0131 0.0089  271 GLU   C O   
4586 C  CB  . GLU   C 178 ? 0.4319 0.2659 0.5205 0.0300  -0.0102 -0.0007 271 GLU   C CB  
4587 C  CG  . GLU   C 178 ? 0.4453 0.2797 0.5363 0.0286  -0.0072 -0.0154 271 GLU   C CG  
4588 C  CD  . GLU   C 178 ? 0.4609 0.2959 0.5684 0.0347  -0.0042 -0.0261 271 GLU   C CD  
4589 O  OE1 . GLU   C 178 ? 0.4720 0.3159 0.5788 0.0338  -0.0014 -0.0404 271 GLU   C OE1 
4590 O  OE2 . GLU   C 178 ? 0.4662 0.2944 0.5878 0.0409  -0.0046 -0.0201 271 GLU   C OE2 
4591 N  N   . VAL   C 179 ? 0.4200 0.2620 0.4765 0.0166  -0.0107 -0.0026 272 VAL   C N   
4592 C  CA  . VAL   C 179 ? 0.4241 0.2749 0.4687 0.0133  -0.0101 -0.0029 272 VAL   C CA  
4593 C  C   . VAL   C 179 ? 0.4396 0.3002 0.4841 0.0136  -0.0079 -0.0128 272 VAL   C C   
4594 O  O   . VAL   C 179 ? 0.4422 0.3003 0.4924 0.0137  -0.0075 -0.0213 272 VAL   C O   
4595 C  CB  . VAL   C 179 ? 0.4251 0.2714 0.4624 0.0097  -0.0115 0.0016  272 VAL   C CB  
4596 C  CG1 . VAL   C 179 ? 0.4234 0.2774 0.4518 0.0077  -0.0107 0.0028  272 VAL   C CG1 
4597 C  CG2 . VAL   C 179 ? 0.4200 0.2608 0.4564 0.0090  -0.0131 0.0096  272 VAL   C CG2 
4598 N  N   . ARG   C 180 ? 0.4403 0.3132 0.4790 0.0132  -0.0062 -0.0123 273 ARG   C N   
4599 C  CA  . ARG   C 180 ? 0.4494 0.3376 0.4831 0.0125  -0.0041 -0.0190 273 ARG   C CA  
4600 C  C   . ARG   C 180 ? 0.4436 0.3372 0.4664 0.0096  -0.0042 -0.0095 273 ARG   C C   
4601 O  O   . ARG   C 180 ? 0.4341 0.3262 0.4559 0.0084  -0.0033 -0.0014 273 ARG   C O   
4602 C  CB  . ARG   C 180 ? 0.4705 0.3711 0.5089 0.0152  -0.0009 -0.0251 273 ARG   C CB  
4603 C  CG  . ARG   C 180 ? 0.4856 0.4070 0.5163 0.0140  0.0017  -0.0304 273 ARG   C CG  
4604 C  CD  . ARG   C 180 ? 0.5081 0.4419 0.5467 0.0173  0.0053  -0.0431 273 ARG   C CD  
4605 N  NE  . ARG   C 180 ? 0.5235 0.4825 0.5536 0.0160  0.0089  -0.0451 273 ARG   C NE  
4606 C  CZ  . ARG   C 180 ? 0.5462 0.5233 0.5711 0.0153  0.0101  -0.0557 273 ARG   C CZ  
4607 N  NH1 . ARG   C 180 ? 0.5574 0.5610 0.5739 0.0143  0.0138  -0.0557 273 ARG   C NH1 
4608 N  NH2 . ARG   C 180 ? 0.5592 0.5302 0.5872 0.0150  0.0077  -0.0662 273 ARG   C NH2 
4609 N  N   . VAL   C 181 ? 0.4400 0.3395 0.4569 0.0084  -0.0052 -0.0103 274 VAL   C N   
4610 C  CA  . VAL   C 181 ? 0.4490 0.3556 0.4573 0.0071  -0.0051 0.0000  274 VAL   C CA  
4611 C  C   . VAL   C 181 ? 0.4497 0.3792 0.4523 0.0073  -0.0026 -0.0019 274 VAL   C C   
4612 O  O   . VAL   C 181 ? 0.4436 0.3854 0.4451 0.0077  -0.0032 -0.0126 274 VAL   C O   
4613 C  CB  . VAL   C 181 ? 0.4460 0.3488 0.4521 0.0068  -0.0081 0.0025  274 VAL   C CB  
4614 C  CG1 . VAL   C 181 ? 0.4448 0.3497 0.4462 0.0071  -0.0078 0.0156  274 VAL   C CG1 
4615 C  CG2 . VAL   C 181 ? 0.4416 0.3262 0.4537 0.0063  -0.0099 0.0013  274 VAL   C CG2 
4616 N  N   . CYS   C 182 ? 0.4501 0.3863 0.4502 0.0064  0.0004  0.0072  275 CYS   C N   
4617 C  CA  . CYS   C 182 ? 0.4695 0.4302 0.4643 0.0062  0.0040  0.0064  275 CYS   C CA  
4618 C  C   . CYS   C 182 ? 0.4622 0.4277 0.4533 0.0043  0.0068  0.0238  275 CYS   C C   
4619 O  O   . CYS   C 182 ? 0.4644 0.4112 0.4600 0.0030  0.0064  0.0329  275 CYS   C O   
4620 C  CB  . CYS   C 182 ? 0.4806 0.4465 0.4818 0.0071  0.0068  -0.0046 275 CYS   C CB  
4621 S  SG  . CYS   C 182 ? 0.5002 0.4476 0.5116 0.0065  0.0075  0.0000  275 CYS   C SG  
4622 N  N   . ALA   C 183 ? 0.4745 0.4651 0.4585 0.0038  0.0099  0.0279  276 ALA   C N   
4623 C  CA  . ALA   C 183 ? 0.4768 0.4757 0.4578 0.0018  0.0135  0.0470  276 ALA   C CA  
4624 C  C   . ALA   C 183 ? 0.4703 0.4598 0.4601 -0.0018 0.0178  0.0512  276 ALA   C C   
4625 O  O   . ALA   C 183 ? 0.4621 0.4404 0.4562 -0.0045 0.0198  0.0662  276 ALA   C O   
4626 C  CB  . ALA   C 183 ? 0.4882 0.5216 0.4585 0.0022  0.0159  0.0491  276 ALA   C CB  
4627 N  N   . CYS   C 184 ? 0.4673 0.4616 0.4613 -0.0019 0.0194  0.0380  277 CYS   C N   
4628 C  CA  . CYS   C 184 ? 0.4786 0.4730 0.4813 -0.0057 0.0237  0.0405  277 CYS   C CA  
4629 C  C   . CYS   C 184 ? 0.4578 0.4371 0.4699 -0.0041 0.0210  0.0279  277 CYS   C C   
4630 O  O   . CYS   C 184 ? 0.4613 0.4516 0.4772 -0.0016 0.0221  0.0161  277 CYS   C O   
4631 C  CB  . CYS   C 184 ? 0.5042 0.5290 0.5034 -0.0067 0.0295  0.0392  277 CYS   C CB  
4632 S  SG  . CYS   C 184 ? 0.5537 0.6046 0.5399 -0.0081 0.0330  0.0562  277 CYS   C SG  
4633 N  N   . PRO   C 185 ? 0.4384 0.3939 0.4553 -0.0050 0.0174  0.0303  278 PRO   C N   
4634 C  CA  . PRO   C 185 ? 0.4251 0.3688 0.4497 -0.0031 0.0141  0.0210  278 PRO   C CA  
4635 C  C   . PRO   C 185 ? 0.4252 0.3791 0.4592 -0.0046 0.0168  0.0179  278 PRO   C C   
4636 O  O   . PRO   C 185 ? 0.3996 0.3565 0.4393 0.0000  0.0153  0.0081  278 PRO   C O   
4637 C  CB  . PRO   C 185 ? 0.4287 0.3514 0.4552 -0.0055 0.0112  0.0267  278 PRO   C CB  
4638 C  CG  . PRO   C 185 ? 0.4327 0.3527 0.4524 -0.0060 0.0118  0.0362  278 PRO   C CG  
4639 C  CD  . PRO   C 185 ? 0.4387 0.3794 0.4544 -0.0073 0.0166  0.0423  278 PRO   C CD  
4640 N  N   . GLY   C 186 ? 0.4259 0.3852 0.4633 -0.0108 0.0209  0.0267  279 GLY   C N   
4641 C  CA  . GLY   C 186 ? 0.4327 0.4061 0.4800 -0.0137 0.0241  0.0245  279 GLY   C CA  
4642 C  C   . GLY   C 186 ? 0.4391 0.4342 0.4868 -0.0088 0.0269  0.0157  279 GLY   C C   
4643 O  O   . GLY   C 186 ? 0.4252 0.4248 0.4821 -0.0049 0.0254  0.0068  279 GLY   C O   
4644 N  N   . ARG   C 187 ? 0.4493 0.4591 0.4878 -0.0084 0.0305  0.0176  280 ARG   C N   
4645 C  CA  . ARG   C 187 ? 0.4694 0.5044 0.5075 -0.0044 0.0344  0.0072  280 ARG   C CA  
4646 C  C   . ARG   C 187 ? 0.4651 0.4921 0.5065 0.0037  0.0302  -0.0083 280 ARG   C C   
4647 O  O   . ARG   C 187 ? 0.4577 0.4961 0.5088 0.0083  0.0320  -0.0192 280 ARG   C O   
4648 C  CB  . ARG   C 187 ? 0.4829 0.5376 0.5082 -0.0061 0.0385  0.0127  280 ARG   C CB  
4649 C  CG  . ARG   C 187 ? 0.4983 0.5838 0.5223 -0.0029 0.0436  0.0006  280 ARG   C CG  
4650 C  CD  . ARG   C 187 ? 0.5218 0.6309 0.5306 -0.0045 0.0468  0.0060  280 ARG   C CD  
4651 N  NE  . ARG   C 187 ? 0.5342 0.6323 0.5337 -0.0016 0.0410  0.0031  280 ARG   C NE  
4652 C  CZ  . ARG   C 187 ? 0.5502 0.6582 0.5366 -0.0031 0.0405  0.0141  280 ARG   C CZ  
4653 N  NH1 . ARG   C 187 ? 0.5725 0.6998 0.5527 -0.0076 0.0456  0.0315  280 ARG   C NH1 
4654 N  NH2 . ARG   C 187 ? 0.5482 0.6462 0.5290 -0.0003 0.0347  0.0093  280 ARG   C NH2 
4655 N  N   . ASP   C 188 ? 0.4698 0.4783 0.5053 0.0054  0.0252  -0.0087 281 ASP   C N   
4656 C  CA  . ASP   C 188 ? 0.4677 0.4670 0.5075 0.0120  0.0219  -0.0224 281 ASP   C CA  
4657 C  C   . ASP   C 188 ? 0.4552 0.4408 0.5086 0.0157  0.0188  -0.0245 281 ASP   C C   
4658 O  O   . ASP   C 188 ? 0.4568 0.4436 0.5204 0.0223  0.0190  -0.0361 281 ASP   C O   
4659 C  CB  . ASP   C 188 ? 0.4714 0.4572 0.5019 0.0114  0.0179  -0.0209 281 ASP   C CB  
4660 C  CG  . ASP   C 188 ? 0.4880 0.4932 0.5061 0.0095  0.0201  -0.0208 281 ASP   C CG  
4661 O  OD1 . ASP   C 188 ? 0.5065 0.5371 0.5220 0.0089  0.0252  -0.0230 281 ASP   C OD1 
4662 O  OD2 . ASP   C 188 ? 0.5013 0.4993 0.5124 0.0089  0.0166  -0.0185 281 ASP   C OD2 
4663 N  N   . ARG   C 189 ? 0.4324 0.4068 0.4871 0.0120  0.0162  -0.0141 282 ARG   C N   
4664 C  CA  . ARG   C 189 ? 0.4227 0.3906 0.4893 0.0153  0.0128  -0.0146 282 ARG   C CA  
4665 C  C   . ARG   C 189 ? 0.4250 0.4136 0.5033 0.0186  0.0165  -0.0204 282 ARG   C C   
4666 O  O   . ARG   C 189 ? 0.4285 0.4165 0.5187 0.0265  0.0150  -0.0271 282 ARG   C O   
4667 C  CB  . ARG   C 189 ? 0.4086 0.3668 0.4739 0.0095  0.0098  -0.0048 282 ARG   C CB  
4668 C  CG  . ARG   C 189 ? 0.3998 0.3587 0.4762 0.0127  0.0060  -0.0051 282 ARG   C CG  
4669 C  CD  . ARG   C 189 ? 0.3875 0.3388 0.4623 0.0069  0.0024  0.0010  282 ARG   C CD  
4670 N  NE  . ARG   C 189 ? 0.3778 0.3406 0.4634 0.0089  -0.0004 0.0005  282 ARG   C NE  
4671 C  CZ  . ARG   C 189 ? 0.3740 0.3425 0.4624 0.0027  -0.0023 0.0026  282 ARG   C CZ  
4672 N  NH1 . ARG   C 189 ? 0.3720 0.3316 0.4542 -0.0058 -0.0012 0.0049  282 ARG   C NH1 
4673 N  NH2 . ARG   C 189 ? 0.3666 0.3504 0.4653 0.0053  -0.0056 0.0017  282 ARG   C NH2 
4674 N  N   . ARG   C 190 ? 0.4241 0.4310 0.5009 0.0129  0.0215  -0.0171 283 ARG   C N   
4675 C  CA  . ARG   C 190 ? 0.4285 0.4593 0.5169 0.0148  0.0259  -0.0221 283 ARG   C CA  
4676 C  C   . ARG   C 190 ? 0.4360 0.4765 0.5299 0.0237  0.0286  -0.0362 283 ARG   C C   
4677 O  O   . ARG   C 190 ? 0.4152 0.4627 0.5248 0.0311  0.0285  -0.0429 283 ARG   C O   
4678 C  CB  . ARG   C 190 ? 0.4312 0.4804 0.5152 0.0060  0.0322  -0.0153 283 ARG   C CB  
4679 C  CG  . ARG   C 190 ? 0.4287 0.4922 0.5258 0.0020  0.0336  -0.0126 283 ARG   C CG  
4680 C  CD  . ARG   C 190 ? 0.4333 0.5156 0.5291 -0.0075 0.0410  -0.0051 283 ARG   C CD  
4681 N  NE  . ARG   C 190 ? 0.4291 0.4959 0.5210 -0.0175 0.0403  0.0071  283 ARG   C NE  
4682 C  CZ  . ARG   C 190 ? 0.4371 0.5136 0.5311 -0.0276 0.0463  0.0168  283 ARG   C CZ  
4683 N  NH1 . ARG   C 190 ? 0.4480 0.5066 0.5415 -0.0359 0.0457  0.0267  283 ARG   C NH1 
4684 N  NH2 . ARG   C 190 ? 0.4394 0.5440 0.5381 -0.0296 0.0535  0.0164  283 ARG   C NH2 
4685 N  N   . THR   C 191 ? 0.4471 0.4892 0.5299 0.0233  0.0309  -0.0411 284 THR   C N   
4686 C  CA  . THR   C 191 ? 0.4643 0.5171 0.5516 0.0303  0.0342  -0.0580 284 THR   C CA  
4687 C  C   . THR   C 191 ? 0.4705 0.5023 0.5715 0.0390  0.0298  -0.0655 284 THR   C C   
4688 O  O   . THR   C 191 ? 0.4779 0.5183 0.5949 0.0470  0.0325  -0.0770 284 THR   C O   
4689 C  CB  . THR   C 191 ? 0.4654 0.5249 0.5362 0.0264  0.0360  -0.0608 284 THR   C CB  
4690 O  OG1 . THR   C 191 ? 0.4656 0.5440 0.5259 0.0189  0.0402  -0.0492 284 THR   C OG1 
4691 C  CG2 . THR   C 191 ? 0.4745 0.5497 0.5491 0.0319  0.0400  -0.0811 284 THR   C CG2 
4692 N  N   . GLU   C 192 ? 0.4838 0.4898 0.5803 0.0377  0.0238  -0.0582 285 GLU   C N   
4693 C  CA  . GLU   C 192 ? 0.4988 0.4832 0.6077 0.0449  0.0200  -0.0623 285 GLU   C CA  
4694 C  C   . GLU   C 192 ? 0.5022 0.4867 0.6278 0.0515  0.0180  -0.0575 285 GLU   C C   
4695 O  O   . GLU   C 192 ? 0.5080 0.4850 0.6507 0.0607  0.0179  -0.0642 285 GLU   C O   
4696 C  CB  . GLU   C 192 ? 0.5069 0.4678 0.6057 0.0407  0.0148  -0.0538 285 GLU   C CB  
4697 C  CG  . GLU   C 192 ? 0.5200 0.4796 0.6082 0.0372  0.0159  -0.0615 285 GLU   C CG  
4698 C  CD  . GLU   C 192 ? 0.5297 0.4658 0.6162 0.0360  0.0114  -0.0588 285 GLU   C CD  
4699 O  OE1 . GLU   C 192 ? 0.5452 0.4641 0.6424 0.0398  0.0084  -0.0539 285 GLU   C OE1 
4700 O  OE2 . GLU   C 192 ? 0.5204 0.4575 0.5953 0.0312  0.0111  -0.0607 285 GLU   C OE2 
4701 N  N   . GLU   C 193 ? 0.4988 0.4930 0.6217 0.0472  0.0166  -0.0468 286 GLU   C N   
4702 C  CA  . GLU   C 193 ? 0.5046 0.5049 0.6428 0.0528  0.0137  -0.0417 286 GLU   C CA  
4703 C  C   . GLU   C 193 ? 0.5227 0.5455 0.6772 0.0601  0.0188  -0.0521 286 GLU   C C   
4704 O  O   . GLU   C 193 ? 0.5228 0.5467 0.6957 0.0700  0.0167  -0.0518 286 GLU   C O   
4705 C  CB  . GLU   C 193 ? 0.4918 0.4973 0.6226 0.0443  0.0106  -0.0299 286 GLU   C CB  
4706 C  CG  . GLU   C 193 ? 0.4864 0.4707 0.6087 0.0413  0.0043  -0.0203 286 GLU   C CG  
4707 C  CD  . GLU   C 193 ? 0.4788 0.4660 0.5926 0.0314  0.0020  -0.0122 286 GLU   C CD  
4708 O  OE1 . GLU   C 193 ? 0.4813 0.4851 0.5960 0.0255  0.0055  -0.0127 286 GLU   C OE1 
4709 O  OE2 . GLU   C 193 ? 0.4633 0.4366 0.5709 0.0293  -0.0027 -0.0059 286 GLU   C OE2 
4710 N  N   . GLU   C 194 ? 0.5503 0.5923 0.6993 0.0563  0.0256  -0.0604 287 GLU   C N   
4711 C  CA  . GLU   C 194 ? 0.5705 0.6387 0.7346 0.0627  0.0317  -0.0716 287 GLU   C CA  
4712 C  C   . GLU   C 194 ? 0.5874 0.6467 0.7687 0.0753  0.0331  -0.0856 287 GLU   C C   
4713 O  O   . GLU   C 194 ? 0.5957 0.6716 0.7961 0.0842  0.0366  -0.0939 287 GLU   C O   
4714 C  CB  . GLU   C 194 ? 0.5900 0.6835 0.7426 0.0548  0.0391  -0.0758 287 GLU   C CB  
4715 C  CG  . GLU   C 194 ? 0.6064 0.7031 0.7501 0.0550  0.0438  -0.0892 287 GLU   C CG  
4716 C  CD  . GLU   C 194 ? 0.6205 0.7488 0.7534 0.0481  0.0515  -0.0915 287 GLU   C CD  
4717 O  OE1 . GLU   C 194 ? 0.6101 0.7403 0.7245 0.0417  0.0529  -0.0905 287 GLU   C OE1 
4718 O  OE2 . GLU   C 194 ? 0.6172 0.7710 0.7608 0.0493  0.0564  -0.0933 287 GLU   C OE2 
4719 N  N   . ASN   C 195 ? 0.6036 0.6372 0.7810 0.0759  0.0305  -0.0879 288 ASN   C N   
4720 C  CA  . ASN   C 195 ? 0.6271 0.6438 0.8240 0.0868  0.0310  -0.0989 288 ASN   C CA  
4721 C  C   . ASN   C 195 ? 0.6292 0.6306 0.8421 0.0950  0.0249  -0.0852 288 ASN   C C   
4722 O  O   . ASN   C 195 ? 0.6239 0.6346 0.8361 0.0941  0.0208  -0.0713 288 ASN   C O   
4723 C  CB  . ASN   C 195 ? 0.6334 0.6291 0.8203 0.0823  0.0304  -0.1052 288 ASN   C CB  
4724 C  CG  . ASN   C 195 ? 0.6351 0.6491 0.8051 0.0746  0.0355  -0.1176 288 ASN   C CG  
4725 O  OD1 . ASN   C 195 ? 0.6502 0.6923 0.8151 0.0725  0.0402  -0.1208 288 ASN   C OD1 
4726 N  ND2 . ASN   C 195 ? 0.6387 0.6397 0.8007 0.0705  0.0348  -0.1246 288 ASN   C ND2 
4727 N  N   . SER   D 2   ? 0.9154 0.6201 1.0528 -0.0042 0.0427  0.1620  95  SER   D N   
4728 C  CA  . SER   D 2   ? 0.9176 0.6106 1.0715 -0.0157 0.0436  0.1430  95  SER   D CA  
4729 C  C   . SER   D 2   ? 0.8997 0.6156 1.0462 -0.0234 0.0400  0.1285  95  SER   D C   
4730 O  O   . SER   D 2   ? 0.8786 0.6164 1.0077 -0.0192 0.0370  0.1319  95  SER   D O   
4731 C  CB  . SER   D 2   ? 0.9132 0.5911 1.0756 -0.0104 0.0396  0.1289  95  SER   D CB  
4732 O  OG  . SER   D 2   ? 0.9028 0.5981 1.0505 -0.0021 0.0316  0.1198  95  SER   D OG  
4733 N  N   . SER   D 3   ? 0.9041 0.6154 1.0639 -0.0340 0.0401  0.1126  96  SER   D N   
4734 C  CA  . SER   D 3   ? 0.8816 0.6130 1.0378 -0.0408 0.0360  0.0976  96  SER   D CA  
4735 C  C   . SER   D 3   ? 0.8486 0.5963 0.9868 -0.0320 0.0280  0.0898  96  SER   D C   
4736 O  O   . SER   D 3   ? 0.8417 0.6089 0.9676 -0.0311 0.0268  0.0922  96  SER   D O   
4737 C  CB  . SER   D 3   ? 0.8907 0.6136 1.0640 -0.0508 0.0352  0.0802  96  SER   D CB  
4738 O  OG  . SER   D 3   ? 0.8993 0.6120 1.0735 -0.0458 0.0302  0.0670  96  SER   D OG  
4739 N  N   . VAL   D 4   ? 0.8259 0.5650 0.9640 -0.0259 0.0236  0.0808  97  VAL   D N   
4740 C  CA  . VAL   D 4   ? 0.7831 0.5344 0.9071 -0.0179 0.0167  0.0728  97  VAL   D CA  
4741 C  C   . VAL   D 4   ? 0.7604 0.5303 0.8682 -0.0132 0.0156  0.0826  97  VAL   D C   
4742 O  O   . VAL   D 4   ? 0.7529 0.5224 0.8572 -0.0091 0.0188  0.0984  97  VAL   D O   
4743 C  CB  . VAL   D 4   ? 0.7924 0.5306 0.9190 -0.0089 0.0153  0.0719  97  VAL   D CB  
4744 C  CG1 . VAL   D 4   ? 0.7761 0.5281 0.8903 -0.0020 0.0093  0.0640  97  VAL   D CG1 
4745 C  CG2 . VAL   D 4   ? 0.8033 0.5217 0.9461 -0.0130 0.0171  0.0607  97  VAL   D CG2 
4746 N  N   . PRO   D 5   ? 0.7321 0.5190 0.8295 -0.0132 0.0111  0.0734  98  PRO   D N   
4747 C  CA  . PRO   D 5   ? 0.7179 0.5215 0.8003 -0.0083 0.0095  0.0793  98  PRO   D CA  
4748 C  C   . PRO   D 5   ? 0.7119 0.5163 0.7876 0.0013  0.0064  0.0836  98  PRO   D C   
4749 O  O   . PRO   D 5   ? 0.7036 0.5004 0.7837 0.0046  0.0039  0.0764  98  PRO   D O   
4750 C  CB  . PRO   D 5   ? 0.7034 0.5199 0.7799 -0.0109 0.0058  0.0666  98  PRO   D CB  
4751 C  CG  . PRO   D 5   ? 0.7017 0.5096 0.7873 -0.0146 0.0035  0.0540  98  PRO   D CG  
4752 C  CD  . PRO   D 5   ? 0.7116 0.5021 0.8111 -0.0178 0.0073  0.0572  98  PRO   D CD  
4753 N  N   . SER   D 6   ? 0.6969 0.5131 0.7623 0.0059  0.0067  0.0946  99  SER   D N   
4754 C  CA  . SER   D 6   ? 0.6874 0.5088 0.7469 0.0156  0.0035  0.1015  99  SER   D CA  
4755 C  C   . SER   D 6   ? 0.6565 0.4865 0.7121 0.0182  -0.0022 0.0883  99  SER   D C   
4756 O  O   . SER   D 6   ? 0.6371 0.4758 0.6876 0.0136  -0.0037 0.0780  99  SER   D O   
4757 C  CB  . SER   D 6   ? 0.6982 0.5349 0.7456 0.0184  0.0044  0.1141  99  SER   D CB  
4758 O  OG  . SER   D 6   ? 0.7101 0.5583 0.7506 0.0274  -0.0004 0.1179  99  SER   D OG  
4759 N  N   . GLN   D 7   ? 0.6355 0.4632 0.6945 0.0258  -0.0048 0.0893  100 GLN   D N   
4760 C  CA  . GLN   D 7   ? 0.6062 0.4436 0.6631 0.0288  -0.0094 0.0785  100 GLN   D CA  
4761 C  C   . GLN   D 7   ? 0.5982 0.4523 0.6491 0.0368  -0.0132 0.0858  100 GLN   D C   
4762 O  O   . GLN   D 7   ? 0.5957 0.4594 0.6471 0.0397  -0.0168 0.0784  100 GLN   D O   
4763 C  CB  . GLN   D 7   ? 0.6063 0.4290 0.6747 0.0305  -0.0088 0.0710  100 GLN   D CB  
4764 C  CG  . GLN   D 7   ? 0.6059 0.4099 0.6828 0.0244  -0.0045 0.0697  100 GLN   D CG  
4765 C  CD  . GLN   D 7   ? 0.6098 0.4005 0.6969 0.0250  -0.0039 0.0590  100 GLN   D CD  
4766 O  OE1 . GLN   D 7   ? 0.5850 0.3797 0.6699 0.0216  -0.0055 0.0460  100 GLN   D OE1 
4767 N  NE2 . GLN   D 7   ? 0.6203 0.3947 0.7185 0.0294  -0.0009 0.0647  100 GLN   D NE2 
4768 N  N   . LYS   D 8   ? 0.6112 0.4703 0.6569 0.0401  -0.0124 0.1002  101 LYS   D N   
4769 C  CA  . LYS   D 8   ? 0.6096 0.4871 0.6492 0.0487  -0.0167 0.1090  101 LYS   D CA  
4770 C  C   . LYS   D 8   ? 0.5826 0.4825 0.6116 0.0453  -0.0210 0.0986  101 LYS   D C   
4771 O  O   . LYS   D 8   ? 0.5589 0.4625 0.5799 0.0384  -0.0190 0.0948  101 LYS   D O   
4772 C  CB  . LYS   D 8   ? 0.6401 0.5171 0.6747 0.0524  -0.0140 0.1279  101 LYS   D CB  
4773 C  CG  . LYS   D 8   ? 0.6607 0.5118 0.7077 0.0540  -0.0086 0.1381  101 LYS   D CG  
4774 C  CD  . LYS   D 8   ? 0.6945 0.5439 0.7389 0.0606  -0.0061 0.1603  101 LYS   D CD  
4775 C  CE  . LYS   D 8   ? 0.7162 0.5389 0.7769 0.0655  -0.0020 0.1692  101 LYS   D CE  
4776 N  NZ  . LYS   D 8   ? 0.7433 0.5583 0.8028 0.0688  0.0030  0.1923  101 LYS   D NZ  
4777 N  N   . THR   D 9   ? 0.5659 0.4804 0.5965 0.0499  -0.0262 0.0935  102 THR   D N   
4778 C  CA  . THR   D 9   ? 0.5572 0.4937 0.5799 0.0464  -0.0304 0.0831  102 THR   D CA  
4779 C  C   . THR   D 9   ? 0.5648 0.5187 0.5739 0.0473  -0.0318 0.0905  102 THR   D C   
4780 O  O   . THR   D 9   ? 0.5682 0.5251 0.5747 0.0547  -0.0323 0.1059  102 THR   D O   
4781 C  CB  . THR   D 9   ? 0.5505 0.5010 0.5803 0.0512  -0.0354 0.0777  102 THR   D CB  
4782 O  OG1 . THR   D 9   ? 0.5478 0.4824 0.5881 0.0492  -0.0327 0.0697  102 THR   D OG1 
4783 C  CG2 . THR   D 9   ? 0.5422 0.5148 0.5666 0.0462  -0.0395 0.0661  102 THR   D CG2 
4784 N  N   . TYR   D 10  ? 0.5663 0.5307 0.5670 0.0401  -0.0320 0.0797  103 TYR   D N   
4785 C  CA  . TYR   D 10  ? 0.5809 0.5639 0.5670 0.0396  -0.0328 0.0822  103 TYR   D CA  
4786 C  C   . TYR   D 10  ? 0.5630 0.5595 0.5450 0.0328  -0.0350 0.0645  103 TYR   D C   
4787 O  O   . TYR   D 10  ? 0.5443 0.5296 0.5268 0.0257  -0.0309 0.0555  103 TYR   D O   
4788 C  CB  . TYR   D 10  ? 0.6038 0.5751 0.5848 0.0364  -0.0260 0.0898  103 TYR   D CB  
4789 C  CG  . TYR   D 10  ? 0.6308 0.5921 0.6138 0.0425  -0.0231 0.1092  103 TYR   D CG  
4790 C  CD1 . TYR   D 10  ? 0.6570 0.6324 0.6341 0.0515  -0.0267 0.1234  103 TYR   D CD1 
4791 C  CD2 . TYR   D 10  ? 0.6450 0.5824 0.6366 0.0392  -0.0169 0.1138  103 TYR   D CD2 
4792 C  CE1 . TYR   D 10  ? 0.6781 0.6417 0.6578 0.0574  -0.0233 0.1430  103 TYR   D CE1 
4793 C  CE2 . TYR   D 10  ? 0.6618 0.5871 0.6572 0.0436  -0.0134 0.1314  103 TYR   D CE2 
4794 C  CZ  . TYR   D 10  ? 0.6866 0.6235 0.6762 0.0530  -0.0162 0.1467  103 TYR   D CZ  
4795 O  OH  . TYR   D 10  ? 0.7203 0.6427 0.7146 0.0576  -0.0119 0.1656  103 TYR   D OH  
4796 N  N   . GLN   D 11  ? 0.5644 0.5842 0.5438 0.0348  -0.0414 0.0595  104 GLN   D N   
4797 C  CA  . GLN   D 11  ? 0.5594 0.5929 0.5358 0.0275  -0.0435 0.0417  104 GLN   D CA  
4798 C  C   . GLN   D 11  ? 0.5599 0.6010 0.5220 0.0246  -0.0406 0.0394  104 GLN   D C   
4799 O  O   . GLN   D 11  ? 0.5524 0.5911 0.5140 0.0173  -0.0382 0.0247  104 GLN   D O   
4800 C  CB  . GLN   D 11  ? 0.5727 0.6317 0.5515 0.0300  -0.0514 0.0368  104 GLN   D CB  
4801 C  CG  . GLN   D 11  ? 0.5714 0.6252 0.5662 0.0317  -0.0533 0.0354  104 GLN   D CG  
4802 C  CD  . GLN   D 11  ? 0.5841 0.6617 0.5849 0.0286  -0.0593 0.0226  104 GLN   D CD  
4803 O  OE1 . GLN   D 11  ? 0.5980 0.7009 0.5910 0.0281  -0.0644 0.0177  104 GLN   D OE1 
4804 N  NE2 . GLN   D 11  ? 0.5739 0.6451 0.5889 0.0256  -0.0584 0.0161  104 GLN   D NE2 
4805 N  N   . GLY   D 12  ? 0.5644 0.6142 0.5158 0.0305  -0.0401 0.0540  105 GLY   D N   
4806 C  CA  . GLY   D 12  ? 0.5737 0.6324 0.5105 0.0287  -0.0361 0.0544  105 GLY   D CA  
4807 C  C   . GLY   D 12  ? 0.5721 0.6544 0.4999 0.0247  -0.0395 0.0372  105 GLY   D C   
4808 O  O   . GLY   D 12  ? 0.5790 0.6778 0.5095 0.0252  -0.0469 0.0299  105 GLY   D O   
4809 N  N   . SER   D 13  ? 0.5704 0.6543 0.4896 0.0206  -0.0341 0.0296  106 SER   D N   
4810 C  CA  . SER   D 13  ? 0.5821 0.6909 0.4883 0.0179  -0.0358 0.0148  106 SER   D CA  
4811 C  C   . SER   D 13  ? 0.5683 0.6775 0.4841 0.0108  -0.0393 -0.0073 106 SER   D C   
4812 O  O   . SER   D 13  ? 0.5813 0.7157 0.4901 0.0092  -0.0446 -0.0196 106 SER   D O   
4813 C  CB  . SER   D 13  ? 0.5844 0.6913 0.4813 0.0159  -0.0273 0.0129  106 SER   D CB  
4814 O  OG  . SER   D 13  ? 0.6039 0.7350 0.4882 0.0136  -0.0284 -0.0032 106 SER   D OG  
4815 N  N   . TYR   D 14  ? 0.5415 0.6251 0.4730 0.0066  -0.0365 -0.0120 107 TYR   D N   
4816 C  CA  . TYR   D 14  ? 0.5309 0.6091 0.4728 -0.0011 -0.0372 -0.0319 107 TYR   D CA  
4817 C  C   . TYR   D 14  ? 0.5250 0.6030 0.4799 -0.0018 -0.0428 -0.0316 107 TYR   D C   
4818 O  O   . TYR   D 14  ? 0.5215 0.5932 0.4868 -0.0089 -0.0426 -0.0457 107 TYR   D O   
4819 C  CB  . TYR   D 14  ? 0.5188 0.5701 0.4679 -0.0049 -0.0294 -0.0367 107 TYR   D CB  
4820 C  CG  . TYR   D 14  ? 0.5222 0.5768 0.4609 -0.0044 -0.0234 -0.0400 107 TYR   D CG  
4821 C  CD1 . TYR   D 14  ? 0.5303 0.5971 0.4637 -0.0082 -0.0225 -0.0587 107 TYR   D CD1 
4822 C  CD2 . TYR   D 14  ? 0.5219 0.5685 0.4570 -0.0003 -0.0182 -0.0254 107 TYR   D CD2 
4823 C  CE1 . TYR   D 14  ? 0.5395 0.6112 0.4635 -0.0071 -0.0163 -0.0627 107 TYR   D CE1 
4824 C  CE2 . TYR   D 14  ? 0.5250 0.5768 0.4517 0.0000  -0.0119 -0.0283 107 TYR   D CE2 
4825 C  CZ  . TYR   D 14  ? 0.5366 0.6013 0.4573 -0.0027 -0.0108 -0.0470 107 TYR   D CZ  
4826 O  OH  . TYR   D 14  ? 0.5495 0.6209 0.4621 -0.0016 -0.0038 -0.0506 107 TYR   D OH  
4827 N  N   . GLY   D 15  ? 0.5284 0.6139 0.4832 0.0052  -0.0472 -0.0162 108 GLY   D N   
4828 C  CA  . GLY   D 15  ? 0.5282 0.6164 0.4960 0.0062  -0.0521 -0.0148 108 GLY   D CA  
4829 C  C   . GLY   D 15  ? 0.5105 0.5711 0.4922 0.0020  -0.0473 -0.0168 108 GLY   D C   
4830 O  O   . GLY   D 15  ? 0.5075 0.5691 0.5001 -0.0039 -0.0485 -0.0281 108 GLY   D O   
4831 N  N   . PHE   D 16  ? 0.5174 0.5556 0.4989 0.0047  -0.0419 -0.0060 109 PHE   D N   
4832 C  CA  . PHE   D 16  ? 0.5027 0.5146 0.4941 0.0012  -0.0369 -0.0072 109 PHE   D CA  
4833 C  C   . PHE   D 16  ? 0.4960 0.5032 0.4977 0.0047  -0.0387 -0.0003 109 PHE   D C   
4834 O  O   . PHE   D 16  ? 0.4938 0.5012 0.4946 0.0122  -0.0400 0.0128  109 PHE   D O   
4835 C  CB  . PHE   D 16  ? 0.5040 0.4987 0.4906 0.0023  -0.0311 -0.0003 109 PHE   D CB  
4836 C  CG  . PHE   D 16  ? 0.4934 0.4642 0.4888 0.0007  -0.0272 0.0015  109 PHE   D CG  
4837 C  CD1 . PHE   D 16  ? 0.4867 0.4467 0.4877 -0.0050 -0.0248 -0.0088 109 PHE   D CD1 
4838 C  CD2 . PHE   D 16  ? 0.4900 0.4492 0.4880 0.0050  -0.0259 0.0136  109 PHE   D CD2 
4839 C  CE1 . PHE   D 16  ? 0.4855 0.4265 0.4928 -0.0058 -0.0219 -0.0062 109 PHE   D CE1 
4840 C  CE2 . PHE   D 16  ? 0.4833 0.4235 0.4883 0.0033  -0.0231 0.0138  109 PHE   D CE2 
4841 C  CZ  . PHE   D 16  ? 0.4807 0.4131 0.4894 -0.0017 -0.0213 0.0042  109 PHE   D CZ  
4842 N  N   . ARG   D 17  ? 0.4921 0.4952 0.5040 -0.0004 -0.0382 -0.0090 110 ARG   D N   
4843 C  CA  A ARG   D 17  ? 0.4859 0.4848 0.5085 0.0019  -0.0386 -0.0051 110 ARG   D CA  
4844 C  CA  B ARG   D 17  ? 0.4849 0.4826 0.5072 0.0022  -0.0383 -0.0043 110 ARG   D CA  
4845 C  C   . ARG   D 17  ? 0.4719 0.4522 0.5008 -0.0044 -0.0335 -0.0109 110 ARG   D C   
4846 O  O   . ARG   D 17  ? 0.4762 0.4507 0.5035 -0.0109 -0.0310 -0.0192 110 ARG   D O   
4847 C  CB  A ARG   D 17  ? 0.4914 0.5145 0.5213 0.0028  -0.0441 -0.0089 110 ARG   D CB  
4848 C  CB  B ARG   D 17  ? 0.4892 0.5113 0.5176 0.0047  -0.0442 -0.0060 110 ARG   D CB  
4849 C  CG  A ARG   D 17  ? 0.4991 0.5382 0.5308 -0.0055 -0.0462 -0.0235 110 ARG   D CG  
4850 C  CG  B ARG   D 17  ? 0.4929 0.5292 0.5264 -0.0039 -0.0458 -0.0208 110 ARG   D CG  
4851 C  CD  A ARG   D 17  ? 0.5082 0.5786 0.5400 -0.0013 -0.0541 -0.0237 110 ARG   D CD  
4852 C  CD  B ARG   D 17  ? 0.4999 0.5669 0.5311 -0.0018 -0.0533 -0.0238 110 ARG   D CD  
4853 N  NE  A ARG   D 17  ? 0.5167 0.6065 0.5560 -0.0098 -0.0571 -0.0389 110 ARG   D NE  
4854 N  NE  B ARG   D 17  ? 0.5122 0.5855 0.5326 -0.0063 -0.0538 -0.0322 110 ARG   D NE  
4855 C  CZ  A ARG   D 17  ? 0.5271 0.6233 0.5611 -0.0171 -0.0576 -0.0516 110 ARG   D CZ  
4856 C  CZ  B ARG   D 17  ? 0.5196 0.5949 0.5434 -0.0165 -0.0526 -0.0483 110 ARG   D CZ  
4857 N  NH1 A ARG   D 17  ? 0.5363 0.6217 0.5568 -0.0162 -0.0549 -0.0505 110 ARG   D NH1 
4858 N  NH1 B ARG   D 17  ? 0.5116 0.5831 0.5494 -0.0238 -0.0507 -0.0562 110 ARG   D NH1 
4859 N  NH2 A ARG   D 17  ? 0.5297 0.6432 0.5730 -0.0257 -0.0603 -0.0664 110 ARG   D NH2 
4860 N  NH2 B ARG   D 17  ? 0.5293 0.6105 0.5429 -0.0193 -0.0529 -0.0567 110 ARG   D NH2 
4861 N  N   . LEU   D 18  ? 0.4649 0.4365 0.5005 -0.0019 -0.0318 -0.0064 111 LEU   D N   
4862 C  CA  . LEU   D 18  ? 0.4522 0.4083 0.4924 -0.0069 -0.0271 -0.0099 111 LEU   D CA  
4863 C  C   . LEU   D 18  ? 0.4490 0.4175 0.4993 -0.0108 -0.0273 -0.0161 111 LEU   D C   
4864 O  O   . LEU   D 18  ? 0.4563 0.4427 0.5115 -0.0068 -0.0312 -0.0151 111 LEU   D O   
4865 C  CB  . LEU   D 18  ? 0.4466 0.3877 0.4869 -0.0020 -0.0248 -0.0024 111 LEU   D CB  
4866 C  CG  . LEU   D 18  ? 0.4509 0.3801 0.4841 0.0007  -0.0241 0.0038  111 LEU   D CG  
4867 C  CD1 . LEU   D 18  ? 0.4482 0.3635 0.4837 0.0038  -0.0220 0.0084  111 LEU   D CD1 
4868 C  CD2 . LEU   D 18  ? 0.4488 0.3704 0.4770 -0.0044 -0.0218 -0.0005 111 LEU   D CD2 
4869 N  N   . GLY   D 19  ? 0.4448 0.4049 0.4984 -0.0185 -0.0230 -0.0219 112 GLY   D N   
4870 C  CA  . GLY   D 19  ? 0.4414 0.4098 0.5057 -0.0236 -0.0209 -0.0264 112 GLY   D CA  
4871 C  C   . GLY   D 19  ? 0.4366 0.3880 0.5008 -0.0255 -0.0149 -0.0234 112 GLY   D C   
4872 O  O   . GLY   D 19  ? 0.4312 0.3650 0.4877 -0.0247 -0.0130 -0.0200 112 GLY   D O   
4873 N  N   . PHE   D 20  ? 0.4348 0.3936 0.5074 -0.0276 -0.0119 -0.0244 113 PHE   D N   
4874 C  CA  . PHE   D 20  ? 0.4389 0.3855 0.5105 -0.0296 -0.0057 -0.0213 113 PHE   D CA  
4875 C  C   . PHE   D 20  ? 0.4421 0.3971 0.5240 -0.0387 -0.0010 -0.0257 113 PHE   D C   
4876 O  O   . PHE   D 20  ? 0.4526 0.4276 0.5450 -0.0410 -0.0034 -0.0311 113 PHE   D O   
4877 C  CB  . PHE   D 20  ? 0.4311 0.3783 0.5012 -0.0213 -0.0056 -0.0168 113 PHE   D CB  
4878 C  CG  . PHE   D 20  ? 0.4243 0.3633 0.4871 -0.0136 -0.0097 -0.0126 113 PHE   D CG  
4879 C  CD1 . PHE   D 20  ? 0.4221 0.3720 0.4874 -0.0077 -0.0148 -0.0114 113 PHE   D CD1 
4880 C  CD2 . PHE   D 20  ? 0.4217 0.3432 0.4756 -0.0126 -0.0085 -0.0092 113 PHE   D CD2 
4881 C  CE1 . PHE   D 20  ? 0.4156 0.3569 0.4748 -0.0015 -0.0175 -0.0061 113 PHE   D CE1 
4882 C  CE2 . PHE   D 20  ? 0.4172 0.3318 0.4664 -0.0070 -0.0116 -0.0056 113 PHE   D CE2 
4883 C  CZ  . PHE   D 20  ? 0.4232 0.3466 0.4752 -0.0018 -0.0155 -0.0037 113 PHE   D CZ  
4884 N  N   . LEU   D 21  ? 0.4473 0.3888 0.5270 -0.0438 0.0052  -0.0229 114 LEU   D N   
4885 C  CA  . LEU   D 21  ? 0.4468 0.3943 0.5365 -0.0530 0.0116  -0.0248 114 LEU   D CA  
4886 C  C   . LEU   D 21  ? 0.4389 0.4057 0.5359 -0.0497 0.0131  -0.0251 114 LEU   D C   
4887 O  O   . LEU   D 21  ? 0.4222 0.3884 0.5131 -0.0405 0.0117  -0.0217 114 LEU   D O   
4888 C  CB  . LEU   D 21  ? 0.4546 0.3823 0.5378 -0.0568 0.0184  -0.0183 114 LEU   D CB  
4889 C  CG  . LEU   D 21  ? 0.4577 0.3668 0.5378 -0.0604 0.0182  -0.0187 114 LEU   D CG  
4890 C  CD1 . LEU   D 21  ? 0.4671 0.3570 0.5396 -0.0610 0.0239  -0.0097 114 LEU   D CD1 
4891 C  CD2 . LEU   D 21  ? 0.4614 0.3755 0.5544 -0.0706 0.0194  -0.0273 114 LEU   D CD2 
4892 N  N   . HIS   D 22  ? 0.4357 0.4201 0.5472 -0.0570 0.0157  -0.0301 115 HIS   D N   
4893 C  CA  . HIS   D 22  ? 0.4321 0.4375 0.5540 -0.0553 0.0189  -0.0310 115 HIS   D CA  
4894 C  C   . HIS   D 22  ? 0.4274 0.4253 0.5468 -0.0605 0.0291  -0.0258 115 HIS   D C   
4895 O  O   . HIS   D 22  ? 0.4335 0.4394 0.5642 -0.0709 0.0353  -0.0274 115 HIS   D O   
4896 C  CB  . HIS   D 22  ? 0.4408 0.4715 0.5802 -0.0607 0.0159  -0.0392 115 HIS   D CB  
4897 C  CG  . HIS   D 22  ? 0.4491 0.4855 0.5864 -0.0553 0.0057  -0.0428 115 HIS   D CG  
4898 N  ND1 . HIS   D 22  ? 0.4585 0.4938 0.5972 -0.0628 0.0021  -0.0491 115 HIS   D ND1 
4899 C  CD2 . HIS   D 22  ? 0.4479 0.4891 0.5802 -0.0429 -0.0010 -0.0401 115 HIS   D CD2 
4900 C  CE1 . HIS   D 22  ? 0.4521 0.4940 0.5854 -0.0551 -0.0065 -0.0501 115 HIS   D CE1 
4901 N  NE2 . HIS   D 22  ? 0.4515 0.4967 0.5813 -0.0430 -0.0085 -0.0436 115 HIS   D NE2 
4902 N  N   A SER   D 23  ? 0.4244 0.4085 0.5293 -0.0538 0.0308  -0.0197 116 SER   D N   
4903 N  N   B SER   D 23  ? 0.4268 0.4101 0.5314 -0.0538 0.0306  -0.0196 116 SER   D N   
4904 C  CA  A SER   D 23  ? 0.4309 0.4038 0.5270 -0.0574 0.0392  -0.0126 116 SER   D CA  
4905 C  CA  B SER   D 23  ? 0.4341 0.4070 0.5298 -0.0570 0.0391  -0.0126 116 SER   D CA  
4906 C  C   A SER   D 23  ? 0.4313 0.4217 0.5315 -0.0563 0.0465  -0.0126 116 SER   D C   
4907 C  C   B SER   D 23  ? 0.4345 0.4266 0.5368 -0.0572 0.0466  -0.0132 116 SER   D C   
4908 O  O   A SER   D 23  ? 0.4437 0.4310 0.5400 -0.0621 0.0552  -0.0068 116 SER   D O   
4909 O  O   B SER   D 23  ? 0.4455 0.4370 0.5479 -0.0651 0.0556  -0.0083 116 SER   D O   
4910 C  CB  A SER   D 23  ? 0.4298 0.3829 0.5079 -0.0504 0.0363  -0.0073 116 SER   D CB  
4911 C  CB  B SER   D 23  ? 0.4340 0.3897 0.5121 -0.0489 0.0363  -0.0078 116 SER   D CB  
4912 O  OG  A SER   D 23  ? 0.4236 0.3613 0.4984 -0.0513 0.0309  -0.0071 116 SER   D OG  
4913 O  OG  B SER   D 23  ? 0.4290 0.3935 0.5050 -0.0392 0.0340  -0.0107 116 SER   D OG  
4914 N  N   . GLY   D 24  ? 0.4231 0.4309 0.5306 -0.0485 0.0435  -0.0183 117 GLY   D N   
4915 C  CA  . GLY   D 24  ? 0.4291 0.4549 0.5413 -0.0454 0.0504  -0.0200 117 GLY   D CA  
4916 C  C   . GLY   D 24  ? 0.4382 0.4539 0.5332 -0.0382 0.0529  -0.0173 117 GLY   D C   
4917 O  O   . GLY   D 24  ? 0.4348 0.4304 0.5156 -0.0350 0.0479  -0.0141 117 GLY   D O   
4918 N  N   . THR   D 25  ? 0.4442 0.4750 0.5406 -0.0359 0.0607  -0.0192 118 THR   D N   
4919 C  CA  . THR   D 25  ? 0.4547 0.4813 0.5359 -0.0280 0.0631  -0.0202 118 THR   D CA  
4920 C  C   . THR   D 25  ? 0.4765 0.5085 0.5484 -0.0341 0.0743  -0.0150 118 THR   D C   
4921 O  O   . THR   D 25  ? 0.4937 0.5340 0.5581 -0.0284 0.0791  -0.0187 118 THR   D O   
4922 C  CB  . THR   D 25  ? 0.4449 0.4852 0.5354 -0.0170 0.0620  -0.0293 118 THR   D CB  
4923 O  OG1 . THR   D 25  ? 0.4482 0.5135 0.5557 -0.0197 0.0690  -0.0322 118 THR   D OG1 
4924 C  CG2 . THR   D 25  ? 0.4354 0.4686 0.5326 -0.0097 0.0513  -0.0319 118 THR   D CG2 
4925 N  N   . ALA   D 26  ? 0.4927 0.5202 0.5653 -0.0453 0.0789  -0.0067 119 ALA   D N   
4926 C  CA  . ALA   D 26  ? 0.5224 0.5539 0.5860 -0.0520 0.0903  0.0015  119 ALA   D CA  
4927 C  C   . ALA   D 26  ? 0.5404 0.5577 0.5790 -0.0468 0.0889  0.0067  119 ALA   D C   
4928 O  O   . ALA   D 26  ? 0.5423 0.5416 0.5736 -0.0428 0.0794  0.0071  119 ALA   D O   
4929 C  CB  . ALA   D 26  ? 0.5265 0.5517 0.5984 -0.0650 0.0947  0.0097  119 ALA   D CB  
4930 N  N   . LYS   D 27  ? 0.5732 0.6011 0.5996 -0.0469 0.0981  0.0103  120 LYS   D N   
4931 C  CA  . LYS   D 27  ? 0.6043 0.6263 0.6058 -0.0413 0.0972  0.0136  120 LYS   D CA  
4932 C  C   . LYS   D 27  ? 0.6170 0.6150 0.6078 -0.0422 0.0897  0.0232  120 LYS   D C   
4933 O  O   . LYS   D 27  ? 0.6353 0.6261 0.6124 -0.0350 0.0824  0.0203  120 LYS   D O   
4934 C  CB  . LYS   D 27  ? 0.6228 0.6603 0.6128 -0.0448 0.1102  0.0207  120 LYS   D CB  
4935 C  CG  . LYS   D 27  ? 0.6285 0.6915 0.6231 -0.0407 0.1176  0.0093  120 LYS   D CG  
4936 C  CD  . LYS   D 27  ? 0.6501 0.7288 0.6263 -0.0419 0.1294  0.0151  120 LYS   D CD  
4937 C  CE  . LYS   D 27  ? 0.6547 0.7553 0.6286 -0.0338 0.1340  0.0003  120 LYS   D CE  
4938 N  NZ  . LYS   D 27  ? 0.6778 0.7962 0.6327 -0.0357 0.1464  0.0064  120 LYS   D NZ  
4939 N  N   . SER   D 28  ? 0.6393 0.6259 0.6380 -0.0507 0.0916  0.0328  121 SER   D N   
4940 C  CA  . SER   D 28  ? 0.6503 0.6141 0.6401 -0.0519 0.0870  0.0438  121 SER   D CA  
4941 C  C   . SER   D 28  ? 0.6376 0.5868 0.6322 -0.0473 0.0745  0.0372  121 SER   D C   
4942 O  O   . SER   D 28  ? 0.6550 0.5878 0.6405 -0.0453 0.0695  0.0442  121 SER   D O   
4943 C  CB  . SER   D 28  ? 0.6723 0.6283 0.6718 -0.0628 0.0947  0.0548  121 SER   D CB  
4944 O  OG  . SER   D 28  ? 0.6664 0.6244 0.6886 -0.0687 0.0935  0.0465  121 SER   D OG  
4945 N  N   A VAL   D 29  ? 0.6134 0.5691 0.6222 -0.0453 0.0700  0.0252  122 VAL   D N   
4946 N  N   B VAL   D 29  ? 0.6102 0.5663 0.6184 -0.0448 0.0698  0.0249  122 VAL   D N   
4947 C  CA  A VAL   D 29  ? 0.5867 0.5302 0.6031 -0.0429 0.0598  0.0201  122 VAL   D CA  
4948 C  CA  B VAL   D 29  ? 0.5831 0.5275 0.5995 -0.0425 0.0597  0.0195  122 VAL   D CA  
4949 C  C   A VAL   D 29  ? 0.5776 0.5121 0.5802 -0.0345 0.0518  0.0185  122 VAL   D C   
4950 C  C   B VAL   D 29  ? 0.5739 0.5086 0.5770 -0.0342 0.0514  0.0180  122 VAL   D C   
4951 O  O   A VAL   D 29  ? 0.5714 0.5152 0.5672 -0.0286 0.0515  0.0124  122 VAL   D O   
4952 O  O   B VAL   D 29  ? 0.5661 0.5094 0.5636 -0.0280 0.0503  0.0110  122 VAL   D O   
4953 C  CB  A VAL   D 29  ? 0.5747 0.5306 0.6086 -0.0421 0.0574  0.0094  122 VAL   D CB  
4954 C  CB  B VAL   D 29  ? 0.5691 0.5270 0.6025 -0.0412 0.0577  0.0087  122 VAL   D CB  
4955 C  CG1 A VAL   D 29  ? 0.5632 0.5085 0.6020 -0.0390 0.0474  0.0053  122 VAL   D CG1 
4956 C  CG1 B VAL   D 29  ? 0.5601 0.5246 0.5899 -0.0313 0.0537  0.0001  122 VAL   D CG1 
4957 C  CG2 A VAL   D 29  ? 0.5748 0.5423 0.6247 -0.0514 0.0646  0.0098  122 VAL   D CG2 
4958 C  CG2 B VAL   D 29  ? 0.5588 0.5085 0.6036 -0.0437 0.0510  0.0062  122 VAL   D CG2 
4959 N  N   . THR   D 30  ? 0.5632 0.4812 0.5633 -0.0342 0.0459  0.0229  123 THR   D N   
4960 C  CA  . THR   D 30  ? 0.5555 0.4650 0.5444 -0.0276 0.0382  0.0224  123 THR   D CA  
4961 C  C   . THR   D 30  ? 0.5183 0.4252 0.5158 -0.0237 0.0305  0.0134  123 THR   D C   
4962 O  O   . THR   D 30  ? 0.5262 0.4306 0.5174 -0.0185 0.0251  0.0100  123 THR   D O   
4963 C  CB  . THR   D 30  ? 0.5711 0.4662 0.5532 -0.0287 0.0371  0.0334  123 THR   D CB  
4964 O  OG1 . THR   D 30  ? 0.5780 0.4621 0.5723 -0.0329 0.0362  0.0339  123 THR   D OG1 
4965 C  CG2 . THR   D 30  ? 0.5936 0.4905 0.5664 -0.0317 0.0450  0.0448  123 THR   D CG2 
4966 N  N   A CYS   D 31  ? 0.5088 0.4172 0.5202 -0.0267 0.0302  0.0100  124 CYS   D N   
4967 N  N   B CYS   D 31  ? 0.4978 0.4070 0.5094 -0.0267 0.0304  0.0098  124 CYS   D N   
4968 C  CA  A CYS   D 31  ? 0.4893 0.3973 0.5086 -0.0228 0.0236  0.0032  124 CYS   D CA  
4969 C  CA  B CYS   D 31  ? 0.4719 0.3792 0.4917 -0.0234 0.0236  0.0036  124 CYS   D CA  
4970 C  C   A CYS   D 31  ? 0.4748 0.3950 0.5086 -0.0252 0.0253  -0.0012 124 CYS   D C   
4971 C  C   B CYS   D 31  ? 0.4643 0.3844 0.4985 -0.0253 0.0252  -0.0012 124 CYS   D C   
4972 O  O   A CYS   D 31  ? 0.4812 0.4035 0.5215 -0.0323 0.0291  0.0008  124 CYS   D O   
4973 O  O   B CYS   D 31  ? 0.4688 0.3909 0.5102 -0.0324 0.0285  0.0004  124 CYS   D O   
4974 C  CB  A CYS   D 31  ? 0.4908 0.3850 0.5089 -0.0227 0.0179  0.0057  124 CYS   D CB  
4975 C  CB  B CYS   D 31  ? 0.4628 0.3566 0.4828 -0.0251 0.0194  0.0069  124 CYS   D CB  
4976 S  SG  A CYS   D 31  ? 0.4931 0.3823 0.5208 -0.0298 0.0190  0.0071  124 CYS   D SG  
4977 S  SG  B CYS   D 31  ? 0.4341 0.3261 0.4601 -0.0207 0.0116  0.0015  124 CYS   D SG  
4978 N  N   . THR   D 32  ? 0.4531 0.3815 0.4927 -0.0193 0.0227  -0.0072 125 THR   D N   
4979 C  CA  . THR   D 32  ? 0.4464 0.3902 0.5005 -0.0194 0.0234  -0.0115 125 THR   D CA  
4980 C  C   . THR   D 32  ? 0.4402 0.3843 0.4991 -0.0115 0.0167  -0.0147 125 THR   D C   
4981 O  O   . THR   D 32  ? 0.4604 0.3973 0.5137 -0.0054 0.0150  -0.0160 125 THR   D O   
4982 C  CB  . THR   D 32  ? 0.4480 0.4073 0.5060 -0.0199 0.0310  -0.0137 125 THR   D CB  
4983 O  OG1 . THR   D 32  ? 0.4452 0.4214 0.5196 -0.0208 0.0311  -0.0174 125 THR   D OG1 
4984 C  CG2 . THR   D 32  ? 0.4531 0.4143 0.5056 -0.0120 0.0321  -0.0179 125 THR   D CG2 
4985 N  N   . TYR   D 33  ? 0.4267 0.3790 0.4957 -0.0121 0.0132  -0.0157 126 TYR   D N   
4986 C  CA  . TYR   D 33  ? 0.4160 0.3696 0.4895 -0.0048 0.0067  -0.0162 126 TYR   D CA  
4987 C  C   . TYR   D 33  ? 0.4057 0.3788 0.4928 0.0002  0.0072  -0.0194 126 TYR   D C   
4988 O  O   . TYR   D 33  ? 0.3896 0.3786 0.4858 -0.0050 0.0098  -0.0217 126 TYR   D O   
4989 C  CB  . TYR   D 33  ? 0.4153 0.3662 0.4881 -0.0083 0.0015  -0.0145 126 TYR   D CB  
4990 C  CG  . TYR   D 33  ? 0.4191 0.3758 0.4962 -0.0013 -0.0045 -0.0134 126 TYR   D CG  
4991 C  CD1 . TYR   D 33  ? 0.4205 0.3647 0.4921 0.0051  -0.0073 -0.0100 126 TYR   D CD1 
4992 C  CD2 . TYR   D 33  ? 0.4181 0.3938 0.5050 -0.0013 -0.0076 -0.0154 126 TYR   D CD2 
4993 C  CE1 . TYR   D 33  ? 0.4256 0.3740 0.5005 0.0119  -0.0122 -0.0066 126 TYR   D CE1 
4994 C  CE2 . TYR   D 33  ? 0.4223 0.4047 0.5116 0.0060  -0.0137 -0.0125 126 TYR   D CE2 
4995 C  CZ  . TYR   D 33  ? 0.4313 0.3992 0.5142 0.0129  -0.0155 -0.0072 126 TYR   D CZ  
4996 O  OH  . TYR   D 33  ? 0.4573 0.4303 0.5418 0.0205  -0.0207 -0.0020 126 TYR   D OH  
4997 N  N   . SER   D 34  ? 0.4077 0.3793 0.4976 0.0101  0.0051  -0.0197 127 SER   D N   
4998 C  CA  . SER   D 34  ? 0.4122 0.4009 0.5164 0.0183  0.0044  -0.0216 127 SER   D CA  
4999 C  C   . SER   D 34  ? 0.4113 0.4036 0.5193 0.0231  -0.0033 -0.0172 127 SER   D C   
5000 O  O   . SER   D 34  ? 0.4134 0.3909 0.5160 0.0284  -0.0065 -0.0130 127 SER   D O   
5001 C  CB  . SER   D 34  ? 0.4229 0.4057 0.5283 0.0271  0.0076  -0.0246 127 SER   D CB  
5002 O  OG  . SER   D 34  ? 0.4292 0.4269 0.5498 0.0369  0.0067  -0.0258 127 SER   D OG  
5003 N  N   . PRO   D 35  ? 0.4129 0.4260 0.5302 0.0211  -0.0063 -0.0179 128 PRO   D N   
5004 C  CA  . PRO   D 35  ? 0.4110 0.4325 0.5312 0.0267  -0.0142 -0.0135 128 PRO   D CA  
5005 C  C   . PRO   D 35  ? 0.4152 0.4391 0.5437 0.0410  -0.0160 -0.0096 128 PRO   D C   
5006 O  O   . PRO   D 35  ? 0.4201 0.4384 0.5453 0.0473  -0.0211 -0.0027 128 PRO   D O   
5007 C  CB  . PRO   D 35  ? 0.4098 0.4576 0.5401 0.0209  -0.0166 -0.0177 128 PRO   D CB  
5008 C  CG  . PRO   D 35  ? 0.4060 0.4574 0.5402 0.0109  -0.0089 -0.0239 128 PRO   D CG  
5009 C  CD  . PRO   D 35  ? 0.4090 0.4403 0.5348 0.0127  -0.0024 -0.0231 128 PRO   D CD  
5010 N  N   . ALA   D 36  ? 0.4183 0.4502 0.5576 0.0462  -0.0112 -0.0138 129 ALA   D N   
5011 C  CA  . ALA   D 36  ? 0.4291 0.4631 0.5793 0.0609  -0.0119 -0.0113 129 ALA   D CA  
5012 C  C   . ALA   D 36  ? 0.4363 0.4410 0.5779 0.0658  -0.0112 -0.0074 129 ALA   D C   
5013 O  O   . ALA   D 36  ? 0.4538 0.4541 0.6009 0.0770  -0.0145 -0.0006 129 ALA   D O   
5014 C  CB  . ALA   D 36  ? 0.4328 0.4814 0.5962 0.0642  -0.0054 -0.0187 129 ALA   D CB  
5015 N  N   . LEU   D 37  ? 0.4348 0.4208 0.5642 0.0579  -0.0071 -0.0111 130 LEU   D N   
5016 C  CA  . LEU   D 37  ? 0.4391 0.3986 0.5617 0.0606  -0.0059 -0.0098 130 LEU   D CA  
5017 C  C   . LEU   D 37  ? 0.4356 0.3812 0.5456 0.0543  -0.0099 -0.0034 130 LEU   D C   
5018 O  O   . LEU   D 37  ? 0.4391 0.3645 0.5455 0.0561  -0.0094 -0.0014 130 LEU   D O   
5019 C  CB  . LEU   D 37  ? 0.4394 0.3912 0.5571 0.0564  0.0007  -0.0191 130 LEU   D CB  
5020 C  CG  . LEU   D 37  ? 0.4474 0.4107 0.5769 0.0636  0.0062  -0.0267 130 LEU   D CG  
5021 C  CD1 . LEU   D 37  ? 0.4537 0.4151 0.5744 0.0572  0.0129  -0.0357 130 LEU   D CD1 
5022 C  CD2 . LEU   D 37  ? 0.4607 0.4124 0.6006 0.0765  0.0062  -0.0264 130 LEU   D CD2 
5023 N  N   . ASN   D 38  ? 0.4304 0.3867 0.5351 0.0469  -0.0130 -0.0015 131 ASN   D N   
5024 C  CA  . ASN   D 38  ? 0.4224 0.3680 0.5146 0.0394  -0.0154 0.0020  131 ASN   D CA  
5025 C  C   . ASN   D 38  ? 0.4209 0.3472 0.5046 0.0343  -0.0116 -0.0015 131 ASN   D C   
5026 O  O   . ASN   D 38  ? 0.4114 0.3218 0.4898 0.0344  -0.0127 0.0022  131 ASN   D O   
5027 C  CB  . ASN   D 38  ? 0.4292 0.3713 0.5199 0.0450  -0.0202 0.0115  131 ASN   D CB  
5028 C  CG  . ASN   D 38  ? 0.4278 0.3634 0.5067 0.0377  -0.0221 0.0143  131 ASN   D CG  
5029 O  OD1 . ASN   D 38  ? 0.4343 0.3747 0.5082 0.0293  -0.0217 0.0096  131 ASN   D OD1 
5030 N  ND2 . ASN   D 38  ? 0.4329 0.3575 0.5082 0.0410  -0.0235 0.0223  131 ASN   D ND2 
5031 N  N   . LYS   D 39  ? 0.4216 0.3510 0.5041 0.0301  -0.0072 -0.0082 132 LYS   D N   
5032 C  CA  . LYS   D 39  ? 0.4269 0.3424 0.5015 0.0268  -0.0038 -0.0124 132 LYS   D CA  
5033 C  C   . LYS   D 39  ? 0.4325 0.3526 0.4999 0.0181  -0.0009 -0.0147 132 LYS   D C   
5034 O  O   . LYS   D 39  ? 0.4274 0.3620 0.4999 0.0165  0.0021  -0.0172 132 LYS   D O   
5035 C  CB  . LYS   D 39  ? 0.4314 0.3453 0.5122 0.0336  -0.0001 -0.0183 132 LYS   D CB  
5036 C  CG  . LYS   D 39  ? 0.4339 0.3350 0.5065 0.0310  0.0022  -0.0241 132 LYS   D CG  
5037 C  CD  . LYS   D 39  ? 0.4440 0.3413 0.5235 0.0383  0.0055  -0.0317 132 LYS   D CD  
5038 C  CE  . LYS   D 39  ? 0.4529 0.3391 0.5240 0.0352  0.0070  -0.0392 132 LYS   D CE  
5039 N  NZ  . LYS   D 39  ? 0.4674 0.3442 0.5471 0.0422  0.0091  -0.0470 132 LYS   D NZ  
5040 N  N   A MET   D 40  ? 0.4439 0.3523 0.5011 0.0128  -0.0017 -0.0131 133 MET   D N   
5041 N  N   B MET   D 40  ? 0.4288 0.3373 0.4859 0.0128  -0.0017 -0.0131 133 MET   D N   
5042 C  CA  A MET   D 40  ? 0.4563 0.3644 0.5053 0.0057  0.0010  -0.0134 133 MET   D CA  
5043 C  CA  B MET   D 40  ? 0.4311 0.3400 0.4805 0.0056  0.0012  -0.0135 133 MET   D CA  
5044 C  C   A MET   D 40  ? 0.4579 0.3636 0.5011 0.0067  0.0045  -0.0179 133 MET   D C   
5045 C  C   B MET   D 40  ? 0.4433 0.3489 0.4861 0.0064  0.0045  -0.0177 133 MET   D C   
5046 O  O   A MET   D 40  ? 0.4589 0.3552 0.4999 0.0098  0.0027  -0.0203 133 MET   D O   
5047 O  O   B MET   D 40  ? 0.4455 0.3411 0.4853 0.0090  0.0025  -0.0196 133 MET   D O   
5048 C  CB  A MET   D 40  ? 0.4685 0.3660 0.5103 0.0016  -0.0019 -0.0094 133 MET   D CB  
5049 C  CB  B MET   D 40  ? 0.4226 0.3219 0.4651 0.0009  -0.0015 -0.0093 133 MET   D CB  
5050 C  CG  A MET   D 40  ? 0.4825 0.3773 0.5164 -0.0040 0.0008  -0.0080 133 MET   D CG  
5051 C  CG  B MET   D 40  ? 0.4231 0.3164 0.4560 -0.0030 0.0005  -0.0085 133 MET   D CG  
5052 S  SD  A MET   D 40  ? 0.5182 0.4234 0.5572 -0.0102 0.0048  -0.0073 133 MET   D SD  
5053 S  SD  B MET   D 40  ? 0.4194 0.3020 0.4471 -0.0065 -0.0026 -0.0039 133 MET   D SD  
5054 C  CE  A MET   D 40  ? 0.5011 0.4039 0.5434 -0.0128 0.0005  -0.0061 133 MET   D CE  
5055 C  CE  B MET   D 40  ? 0.4132 0.3025 0.4476 -0.0103 -0.0024 -0.0035 133 MET   D CE  
5056 N  N   . PHE   D 41  ? 0.4518 0.3668 0.4928 0.0039  0.0098  -0.0193 134 PHE   D N   
5057 C  CA  . PHE   D 41  ? 0.4565 0.3721 0.4880 0.0037  0.0135  -0.0228 134 PHE   D CA  
5058 C  C   . PHE   D 41  ? 0.4551 0.3674 0.4761 -0.0026 0.0145  -0.0166 134 PHE   D C   
5059 O  O   . PHE   D 41  ? 0.4460 0.3633 0.4700 -0.0074 0.0175  -0.0125 134 PHE   D O   
5060 C  CB  . PHE   D 41  ? 0.4637 0.3941 0.5000 0.0059  0.0199  -0.0278 134 PHE   D CB  
5061 C  CG  . PHE   D 41  ? 0.4609 0.3950 0.5100 0.0136  0.0194  -0.0332 134 PHE   D CG  
5062 C  CD1 . PHE   D 41  ? 0.4605 0.4003 0.5220 0.0155  0.0168  -0.0303 134 PHE   D CD1 
5063 C  CD2 . PHE   D 41  ? 0.4688 0.4011 0.5178 0.0196  0.0212  -0.0415 134 PHE   D CD2 
5064 C  CE1 . PHE   D 41  ? 0.4597 0.4032 0.5334 0.0242  0.0159  -0.0334 134 PHE   D CE1 
5065 C  CE2 . PHE   D 41  ? 0.4739 0.4074 0.5362 0.0278  0.0211  -0.0458 134 PHE   D CE2 
5066 C  CZ  . PHE   D 41  ? 0.4723 0.4114 0.5470 0.0306  0.0185  -0.0407 134 PHE   D CZ  
5067 N  N   . CYS   D 42  ? 0.4708 0.3755 0.4813 -0.0026 0.0120  -0.0159 135 CYS   D N   
5068 C  CA  . CYS   D 42  ? 0.4766 0.3772 0.4774 -0.0068 0.0122  -0.0085 135 CYS   D CA  
5069 C  C   . CYS   D 42  ? 0.4798 0.3824 0.4673 -0.0054 0.0120  -0.0098 135 CYS   D C   
5070 O  O   . CYS   D 42  ? 0.4823 0.3864 0.4688 -0.0020 0.0102  -0.0180 135 CYS   D O   
5071 C  CB  . CYS   D 42  ? 0.4811 0.3709 0.4847 -0.0079 0.0070  -0.0043 135 CYS   D CB  
5072 S  SG  . CYS   D 42  ? 0.5141 0.3962 0.5182 -0.0042 0.0004  -0.0085 135 CYS   D SG  
5073 N  N   . GLN   D 43  ? 0.4750 0.3783 0.4527 -0.0080 0.0141  -0.0019 136 GLN   D N   
5074 C  CA  . GLN   D 43  ? 0.4841 0.3915 0.4469 -0.0064 0.0128  -0.0008 136 GLN   D CA  
5075 C  C   . GLN   D 43  ? 0.4769 0.3758 0.4383 -0.0052 0.0054  0.0020  136 GLN   D C   
5076 O  O   . GLN   D 43  ? 0.4595 0.3490 0.4286 -0.0066 0.0039  0.0071  136 GLN   D O   
5077 C  CB  . GLN   D 43  ? 0.5016 0.4141 0.4548 -0.0089 0.0189  0.0093  136 GLN   D CB  
5078 C  CG  . GLN   D 43  ? 0.5074 0.4321 0.4604 -0.0104 0.0273  0.0066  136 GLN   D CG  
5079 C  CD  . GLN   D 43  ? 0.5297 0.4578 0.4748 -0.0142 0.0345  0.0188  136 GLN   D CD  
5080 O  OE1 . GLN   D 43  ? 0.5340 0.4516 0.4797 -0.0167 0.0343  0.0296  136 GLN   D OE1 
5081 N  NE2 . GLN   D 43  ? 0.5415 0.4843 0.4791 -0.0144 0.0416  0.0173  136 GLN   D NE2 
5082 N  N   . LEU   D 44  ? 0.4923 0.3966 0.4445 -0.0028 0.0012  -0.0018 137 LEU   D N   
5083 C  CA  . LEU   D 44  ? 0.5002 0.4013 0.4509 -0.0015 -0.0060 0.0001  137 LEU   D CA  
5084 C  C   . LEU   D 44  ? 0.5117 0.4075 0.4597 -0.0015 -0.0057 0.0138  137 LEU   D C   
5085 O  O   . LEU   D 44  ? 0.5213 0.4205 0.4604 -0.0018 -0.0010 0.0222  137 LEU   D O   
5086 C  CB  . LEU   D 44  ? 0.5113 0.4243 0.4513 0.0002  -0.0097 -0.0075 137 LEU   D CB  
5087 C  CG  . LEU   D 44  ? 0.5167 0.4340 0.4528 0.0018  -0.0177 -0.0069 137 LEU   D CG  
5088 C  CD1 . LEU   D 44  ? 0.5050 0.4124 0.4515 0.0019  -0.0215 -0.0003 137 LEU   D CD1 
5089 C  CD2 . LEU   D 44  ? 0.5242 0.4480 0.4615 0.0012  -0.0221 -0.0224 137 LEU   D CD2 
5090 N  N   . ALA   D 45  ? 0.5163 0.4033 0.4731 -0.0011 -0.0097 0.0160  138 ALA   D N   
5091 C  CA  . ALA   D 45  ? 0.5251 0.4053 0.4821 0.0002  -0.0105 0.0272  138 ALA   D CA  
5092 C  C   . ALA   D 45  ? 0.5346 0.4058 0.4951 -0.0026 -0.0036 0.0343  138 ALA   D C   
5093 O  O   . ALA   D 45  ? 0.5508 0.4135 0.5134 -0.0015 -0.0032 0.0430  138 ALA   D O   
5094 C  CB  . ALA   D 45  ? 0.5441 0.4330 0.4885 0.0041  -0.0136 0.0337  138 ALA   D CB  
5095 N  N   . LYS   D 46  ? 0.5307 0.4039 0.4939 -0.0063 0.0017  0.0304  139 LYS   D N   
5096 C  CA  . LYS   D 46  ? 0.5347 0.4017 0.5033 -0.0108 0.0085  0.0357  139 LYS   D CA  
5097 C  C   . LYS   D 46  ? 0.5213 0.3804 0.5035 -0.0130 0.0074  0.0311  139 LYS   D C   
5098 O  O   . LYS   D 46  ? 0.4932 0.3541 0.4800 -0.0115 0.0031  0.0235  139 LYS   D O   
5099 C  CB  . LYS   D 46  ? 0.5448 0.4215 0.5109 -0.0138 0.0149  0.0337  139 LYS   D CB  
5100 C  CG  . LYS   D 46  ? 0.5642 0.4491 0.5155 -0.0127 0.0184  0.0409  139 LYS   D CG  
5101 C  CD  . LYS   D 46  ? 0.5781 0.4559 0.5273 -0.0156 0.0247  0.0547  139 LYS   D CD  
5102 C  CE  . LYS   D 46  ? 0.6014 0.4894 0.5345 -0.0145 0.0293  0.0631  139 LYS   D CE  
5103 N  NZ  . LYS   D 46  ? 0.6135 0.5077 0.5328 -0.0078 0.0221  0.0651  139 LYS   D NZ  
5104 N  N   . THR   D 47  ? 0.5194 0.3699 0.5075 -0.0169 0.0117  0.0357  140 THR   D N   
5105 C  CA  . THR   D 47  ? 0.5155 0.3594 0.5152 -0.0197 0.0112  0.0310  140 THR   D CA  
5106 C  C   . THR   D 47  ? 0.5119 0.3652 0.5182 -0.0219 0.0110  0.0221  140 THR   D C   
5107 O  O   . THR   D 47  ? 0.5074 0.3683 0.5153 -0.0252 0.0155  0.0214  140 THR   D O   
5108 C  CB  . THR   D 47  ? 0.5253 0.3588 0.5305 -0.0246 0.0170  0.0361  140 THR   D CB  
5109 O  OG1 . THR   D 47  ? 0.5231 0.3480 0.5219 -0.0209 0.0173  0.0463  140 THR   D OG1 
5110 C  CG2 . THR   D 47  ? 0.5194 0.3471 0.5356 -0.0276 0.0162  0.0293  140 THR   D CG2 
5111 N  N   A CYS   D 48  ? 0.5088 0.3627 0.5192 -0.0197 0.0061  0.0165  141 CYS   D N   
5112 N  N   B CYS   D 48  ? 0.5048 0.3587 0.5151 -0.0196 0.0061  0.0165  141 CYS   D N   
5113 C  CA  A CYS   D 48  ? 0.5076 0.3701 0.5245 -0.0201 0.0048  0.0097  141 CYS   D CA  
5114 C  CA  B CYS   D 48  ? 0.5010 0.3634 0.5179 -0.0200 0.0048  0.0097  141 CYS   D CA  
5115 C  C   A CYS   D 48  ? 0.5029 0.3632 0.5269 -0.0224 0.0035  0.0065  141 CYS   D C   
5116 C  C   B CYS   D 48  ? 0.4992 0.3594 0.5232 -0.0224 0.0035  0.0065  141 CYS   D C   
5117 O  O   A CYS   D 48  ? 0.4983 0.3560 0.5221 -0.0196 -0.0002 0.0052  141 CYS   D O   
5118 O  O   B CYS   D 48  ? 0.4949 0.3524 0.5186 -0.0196 -0.0002 0.0053  141 CYS   D O   
5119 C  CB  A CYS   D 48  ? 0.5088 0.3741 0.5233 -0.0149 0.0004  0.0068  141 CYS   D CB  
5120 C  CB  B CYS   D 48  ? 0.4978 0.3632 0.5126 -0.0150 0.0004  0.0067  141 CYS   D CB  
5121 S  SG  A CYS   D 48  ? 0.5180 0.3929 0.5402 -0.0132 -0.0007 0.0012  141 CYS   D SG  
5122 S  SG  B CYS   D 48  ? 0.5092 0.3786 0.5152 -0.0122 0.0012  0.0068  141 CYS   D SG  
5123 N  N   . PRO   D 49  ? 0.5069 0.3694 0.5376 -0.0281 0.0069  0.0044  142 PRO   D N   
5124 C  CA  . PRO   D 49  ? 0.4985 0.3617 0.5355 -0.0309 0.0053  -0.0009 142 PRO   D CA  
5125 C  C   . PRO   D 49  ? 0.4840 0.3592 0.5229 -0.0277 0.0007  -0.0051 142 PRO   D C   
5126 O  O   . PRO   D 49  ? 0.4876 0.3733 0.5292 -0.0265 0.0005  -0.0060 142 PRO   D O   
5127 C  CB  . PRO   D 49  ? 0.5023 0.3678 0.5473 -0.0388 0.0102  -0.0031 142 PRO   D CB  
5128 C  CG  . PRO   D 49  ? 0.5240 0.3844 0.5650 -0.0399 0.0154  0.0043  142 PRO   D CG  
5129 C  CD  . PRO   D 49  ? 0.5140 0.3799 0.5470 -0.0330 0.0126  0.0065  142 PRO   D CD  
5130 N  N   . VAL   D 50  ? 0.4652 0.3387 0.5026 -0.0255 -0.0025 -0.0069 143 VAL   D N   
5131 C  CA  . VAL   D 50  ? 0.4601 0.3450 0.4987 -0.0228 -0.0067 -0.0095 143 VAL   D CA  
5132 C  C   . VAL   D 50  ? 0.4492 0.3373 0.4900 -0.0266 -0.0073 -0.0157 143 VAL   D C   
5133 O  O   . VAL   D 50  ? 0.4728 0.3508 0.5114 -0.0272 -0.0061 -0.0165 143 VAL   D O   
5134 C  CB  . VAL   D 50  ? 0.4616 0.3431 0.4951 -0.0167 -0.0094 -0.0054 143 VAL   D CB  
5135 C  CG1 . VAL   D 50  ? 0.4706 0.3624 0.5046 -0.0136 -0.0129 -0.0056 143 VAL   D CG1 
5136 C  CG2 . VAL   D 50  ? 0.4661 0.3449 0.4983 -0.0137 -0.0088 -0.0021 143 VAL   D CG2 
5137 N  N   . GLN   D 51  ? 0.4482 0.3512 0.4941 -0.0290 -0.0092 -0.0207 144 GLN   D N   
5138 C  CA  . GLN   D 51  ? 0.4490 0.3594 0.4968 -0.0331 -0.0106 -0.0290 144 GLN   D CA  
5139 C  C   . GLN   D 51  ? 0.4465 0.3661 0.4877 -0.0275 -0.0151 -0.0280 144 GLN   D C   
5140 O  O   . GLN   D 51  ? 0.4331 0.3612 0.4732 -0.0220 -0.0181 -0.0225 144 GLN   D O   
5141 C  CB  . GLN   D 51  ? 0.4554 0.3806 0.5125 -0.0391 -0.0110 -0.0355 144 GLN   D CB  
5142 C  CG  . GLN   D 51  ? 0.4584 0.3754 0.5225 -0.0454 -0.0052 -0.0350 144 GLN   D CG  
5143 C  CD  . GLN   D 51  ? 0.4549 0.3899 0.5303 -0.0512 -0.0053 -0.0407 144 GLN   D CD  
5144 O  OE1 . GLN   D 51  ? 0.4595 0.4144 0.5373 -0.0484 -0.0105 -0.0433 144 GLN   D OE1 
5145 N  NE2 . GLN   D 51  ? 0.4597 0.3888 0.5429 -0.0592 0.0005  -0.0418 144 GLN   D NE2 
5146 N  N   . LEU   D 52  ? 0.4502 0.3676 0.4875 -0.0286 -0.0149 -0.0330 145 LEU   D N   
5147 C  CA  . LEU   D 52  ? 0.4651 0.3948 0.4953 -0.0249 -0.0183 -0.0335 145 LEU   D CA  
5148 C  C   . LEU   D 52  ? 0.4765 0.4239 0.5088 -0.0296 -0.0210 -0.0444 145 LEU   D C   
5149 O  O   . LEU   D 52  ? 0.4844 0.4266 0.5212 -0.0363 -0.0184 -0.0548 145 LEU   D O   
5150 C  CB  . LEU   D 52  ? 0.4660 0.3848 0.4905 -0.0230 -0.0156 -0.0332 145 LEU   D CB  
5151 C  CG  . LEU   D 52  ? 0.4630 0.3643 0.4878 -0.0203 -0.0128 -0.0254 145 LEU   D CG  
5152 C  CD1 . LEU   D 52  ? 0.4752 0.3705 0.4965 -0.0183 -0.0104 -0.0262 145 LEU   D CD1 
5153 C  CD2 . LEU   D 52  ? 0.4586 0.3613 0.4821 -0.0156 -0.0148 -0.0156 145 LEU   D CD2 
5154 N  N   . TRP   D 53  ? 0.4916 0.4593 0.5217 -0.0262 -0.0263 -0.0424 146 TRP   D N   
5155 C  CA  . TRP   D 53  ? 0.5101 0.5004 0.5409 -0.0297 -0.0306 -0.0529 146 TRP   D CA  
5156 C  C   . TRP   D 53  ? 0.5179 0.5212 0.5359 -0.0243 -0.0337 -0.0506 146 TRP   D C   
5157 O  O   . TRP   D 53  ? 0.5158 0.5203 0.5283 -0.0165 -0.0351 -0.0376 146 TRP   D O   
5158 C  CB  . TRP   D 53  ? 0.5086 0.5169 0.5482 -0.0298 -0.0349 -0.0523 146 TRP   D CB  
5159 C  CG  . TRP   D 53  ? 0.5139 0.5137 0.5662 -0.0363 -0.0310 -0.0555 146 TRP   D CG  
5160 C  CD1 . TRP   D 53  ? 0.5097 0.4911 0.5644 -0.0349 -0.0264 -0.0475 146 TRP   D CD1 
5161 C  CD2 . TRP   D 53  ? 0.5215 0.5324 0.5856 -0.0459 -0.0311 -0.0673 146 TRP   D CD2 
5162 N  NE1 . TRP   D 53  ? 0.5181 0.4985 0.5842 -0.0423 -0.0231 -0.0521 146 TRP   D NE1 
5163 C  CE2 . TRP   D 53  ? 0.5204 0.5178 0.5936 -0.0496 -0.0255 -0.0641 146 TRP   D CE2 
5164 C  CE3 . TRP   D 53  ? 0.5296 0.5609 0.5979 -0.0524 -0.0349 -0.0810 146 TRP   D CE3 
5165 C  CZ2 . TRP   D 53  ? 0.5211 0.5239 0.6081 -0.0598 -0.0229 -0.0725 146 TRP   D CZ2 
5166 C  CZ3 . TRP   D 53  ? 0.5329 0.5701 0.6163 -0.0628 -0.0332 -0.0908 146 TRP   D CZ3 
5167 C  CH2 . TRP   D 53  ? 0.5307 0.5527 0.6236 -0.0667 -0.0267 -0.0860 146 TRP   D CH2 
5168 N  N   . VAL   D 54  ? 0.5316 0.5442 0.5455 -0.0286 -0.0341 -0.0632 147 VAL   D N   
5169 C  CA  . VAL   D 54  ? 0.5544 0.5840 0.5544 -0.0244 -0.0366 -0.0634 147 VAL   D CA  
5170 C  C   . VAL   D 54  ? 0.5672 0.6236 0.5668 -0.0291 -0.0422 -0.0778 147 VAL   D C   
5171 O  O   . VAL   D 54  ? 0.5662 0.6204 0.5768 -0.0379 -0.0414 -0.0918 147 VAL   D O   
5172 C  CB  . VAL   D 54  ? 0.5481 0.5629 0.5415 -0.0243 -0.0305 -0.0662 147 VAL   D CB  
5173 C  CG1 . VAL   D 54  ? 0.5400 0.5359 0.5325 -0.0188 -0.0267 -0.0509 147 VAL   D CG1 
5174 C  CG2 . VAL   D 54  ? 0.5553 0.5559 0.5573 -0.0321 -0.0261 -0.0815 147 VAL   D CG2 
5175 N  N   . ASP   D 55  ? 0.5905 0.6720 0.5785 -0.0235 -0.0478 -0.0738 148 ASP   D N   
5176 C  CA  . ASP   D 55  ? 0.6131 0.7259 0.5969 -0.0267 -0.0543 -0.0876 148 ASP   D CA  
5177 C  C   . ASP   D 55  ? 0.6257 0.7376 0.6010 -0.0312 -0.0504 -0.1031 148 ASP   D C   
5178 O  O   . ASP   D 55  ? 0.6405 0.7679 0.6184 -0.0387 -0.0532 -0.1225 148 ASP   D O   
5179 C  CB  . ASP   D 55  ? 0.6292 0.7696 0.6016 -0.0173 -0.0617 -0.0750 148 ASP   D CB  
5180 C  CG  . ASP   D 55  ? 0.6350 0.7811 0.6177 -0.0121 -0.0664 -0.0625 148 ASP   D CG  
5181 O  OD1 . ASP   D 55  ? 0.6263 0.7661 0.6253 -0.0180 -0.0660 -0.0690 148 ASP   D OD1 
5182 O  OD2 . ASP   D 55  ? 0.6515 0.8088 0.6262 -0.0019 -0.0701 -0.0461 148 ASP   D OD2 
5183 N  N   . SER   D 56  ? 0.6185 0.7139 0.5853 -0.0270 -0.0440 -0.0959 149 SER   D N   
5184 C  CA  . SER   D 56  ? 0.6293 0.7228 0.5882 -0.0294 -0.0387 -0.1095 149 SER   D CA  
5185 C  C   . SER   D 56  ? 0.6085 0.6697 0.5727 -0.0284 -0.0299 -0.1043 149 SER   D C   
5186 O  O   . SER   D 56  ? 0.5976 0.6462 0.5626 -0.0230 -0.0285 -0.0861 149 SER   D O   
5187 C  CB  . SER   D 56  ? 0.6432 0.7628 0.5822 -0.0235 -0.0409 -0.1060 149 SER   D CB  
5188 O  OG  . SER   D 56  ? 0.6388 0.7560 0.5709 -0.0147 -0.0405 -0.0821 149 SER   D OG  
5189 N  N   . THR   D 57  ? 0.6096 0.6588 0.5784 -0.0333 -0.0245 -0.1206 150 THR   D N   
5190 C  CA  . THR   D 57  ? 0.6056 0.6254 0.5817 -0.0323 -0.0165 -0.1185 150 THR   D CA  
5191 C  C   . THR   D 57  ? 0.5995 0.6209 0.5644 -0.0247 -0.0126 -0.1070 150 THR   D C   
5192 O  O   . THR   D 57  ? 0.6056 0.6432 0.5589 -0.0231 -0.0108 -0.1144 150 THR   D O   
5193 C  CB  . THR   D 57  ? 0.6218 0.6315 0.6055 -0.0383 -0.0119 -0.1401 150 THR   D CB  
5194 O  OG1 . THR   D 57  ? 0.6323 0.6450 0.6262 -0.0468 -0.0157 -0.1513 150 THR   D OG1 
5195 C  CG2 . THR   D 57  ? 0.6223 0.6012 0.6164 -0.0369 -0.0046 -0.1375 150 THR   D CG2 
5196 N  N   . PRO   D 58  ? 0.5774 0.5835 0.5455 -0.0204 -0.0108 -0.0892 151 PRO   D N   
5197 C  CA  . PRO   D 58  ? 0.5713 0.5764 0.5328 -0.0148 -0.0057 -0.0797 151 PRO   D CA  
5198 C  C   . PRO   D 58  ? 0.5760 0.5727 0.5406 -0.0149 0.0014  -0.0924 151 PRO   D C   
5199 O  O   . PRO   D 58  ? 0.5812 0.5635 0.5562 -0.0185 0.0030  -0.1049 151 PRO   D O   
5200 C  CB  . PRO   D 58  ? 0.5593 0.5462 0.5287 -0.0124 -0.0055 -0.0625 151 PRO   D CB  
5201 C  CG  . PRO   D 58  ? 0.5528 0.5393 0.5273 -0.0148 -0.0117 -0.0598 151 PRO   D CG  
5202 C  CD  . PRO   D 58  ? 0.5585 0.5498 0.5368 -0.0210 -0.0132 -0.0784 151 PRO   D CD  
5203 N  N   . PRO   D 59  ? 0.5724 0.5776 0.5292 -0.0106 0.0065  -0.0894 152 PRO   D N   
5204 C  CA  . PRO   D 59  ? 0.5763 0.5760 0.5369 -0.0094 0.0139  -0.1022 152 PRO   D CA  
5205 C  C   . PRO   D 59  ? 0.5634 0.5366 0.5401 -0.0079 0.0171  -0.0986 152 PRO   D C   
5206 O  O   . PRO   D 59  ? 0.5445 0.5067 0.5266 -0.0072 0.0147  -0.0838 152 PRO   D O   
5207 C  CB  . PRO   D 59  ? 0.5824 0.6009 0.5306 -0.0050 0.0185  -0.0956 152 PRO   D CB  
5208 C  CG  . PRO   D 59  ? 0.5737 0.5950 0.5177 -0.0036 0.0147  -0.0734 152 PRO   D CG  
5209 C  CD  . PRO   D 59  ? 0.5726 0.5931 0.5176 -0.0067 0.0063  -0.0731 152 PRO   D CD  
5210 N  N   . PRO   D 60  ? 0.5664 0.5290 0.5515 -0.0067 0.0227  -0.1123 153 PRO   D N   
5211 C  CA  . PRO   D 60  ? 0.5552 0.4956 0.5548 -0.0034 0.0258  -0.1071 153 PRO   D CA  
5212 C  C   . PRO   D 60  ? 0.5347 0.4792 0.5341 0.0010  0.0274  -0.0906 153 PRO   D C   
5213 O  O   . PRO   D 60  ? 0.5287 0.4917 0.5188 0.0026  0.0303  -0.0886 153 PRO   D O   
5214 C  CB  . PRO   D 60  ? 0.5746 0.5093 0.5809 -0.0010 0.0325  -0.1249 153 PRO   D CB  
5215 C  CG  . PRO   D 60  ? 0.5925 0.5402 0.5902 -0.0062 0.0314  -0.1429 153 PRO   D CG  
5216 C  CD  . PRO   D 60  ? 0.5888 0.5605 0.5702 -0.0079 0.0262  -0.1335 153 PRO   D CD  
5217 N  N   . GLY   D 61  ? 0.5218 0.4505 0.5313 0.0025  0.0258  -0.0792 154 GLY   D N   
5218 C  CA  . GLY   D 61  ? 0.5113 0.4429 0.5235 0.0055  0.0267  -0.0648 154 GLY   D CA  
5219 C  C   . GLY   D 61  ? 0.5008 0.4367 0.5064 0.0026  0.0216  -0.0509 154 GLY   D C   
5220 O  O   . GLY   D 61  ? 0.5009 0.4369 0.5100 0.0036  0.0218  -0.0391 154 GLY   D O   
5221 N  N   . THR   D 62  ? 0.4970 0.4363 0.4949 -0.0009 0.0170  -0.0526 155 THR   D N   
5222 C  CA  . THR   D 62  ? 0.4845 0.4236 0.4792 -0.0026 0.0116  -0.0402 155 THR   D CA  
5223 C  C   . THR   D 62  ? 0.4657 0.3867 0.4711 -0.0025 0.0095  -0.0335 155 THR   D C   
5224 O  O   . THR   D 62  ? 0.4485 0.3569 0.4612 -0.0025 0.0101  -0.0399 155 THR   D O   
5225 C  CB  . THR   D 62  ? 0.4980 0.4436 0.4866 -0.0058 0.0067  -0.0456 155 THR   D CB  
5226 O  OG1 . THR   D 62  ? 0.5189 0.4843 0.4960 -0.0055 0.0081  -0.0521 155 THR   D OG1 
5227 C  CG2 . THR   D 62  ? 0.4887 0.4337 0.4762 -0.0063 0.0015  -0.0335 155 THR   D CG2 
5228 N  N   . ARG   D 63  ? 0.4487 0.3684 0.4547 -0.0024 0.0074  -0.0210 156 ARG   D N   
5229 C  CA  . ARG   D 63  ? 0.4409 0.3463 0.4554 -0.0023 0.0052  -0.0153 156 ARG   D CA  
5230 C  C   . ARG   D 63  ? 0.4257 0.3286 0.4381 -0.0039 0.0006  -0.0087 156 ARG   D C   
5231 O  O   . ARG   D 63  ? 0.4158 0.3285 0.4216 -0.0040 -0.0005 -0.0048 156 ARG   D O   
5232 C  CB  . ARG   D 63  ? 0.4420 0.3482 0.4627 -0.0004 0.0079  -0.0096 156 ARG   D CB  
5233 C  CG  . ARG   D 63  ? 0.4495 0.3535 0.4773 0.0025  0.0114  -0.0164 156 ARG   D CG  
5234 C  CD  . ARG   D 63  ? 0.4538 0.3683 0.4862 0.0043  0.0159  -0.0138 156 ARG   D CD  
5235 N  NE  . ARG   D 63  ? 0.4552 0.3705 0.4929 0.0026  0.0146  -0.0040 156 ARG   D NE  
5236 C  CZ  . ARG   D 63  ? 0.4559 0.3674 0.5042 0.0038  0.0129  -0.0018 156 ARG   D CZ  
5237 N  NH1 . ARG   D 63  ? 0.4583 0.3638 0.5124 0.0078  0.0121  -0.0065 156 ARG   D NH1 
5238 N  NH2 . ARG   D 63  ? 0.4513 0.3650 0.5046 0.0010  0.0118  0.0051  156 ARG   D NH2 
5239 N  N   . VAL   D 64  ? 0.4193 0.3105 0.4370 -0.0045 -0.0016 -0.0074 157 VAL   D N   
5240 C  CA  . VAL   D 64  ? 0.4246 0.3125 0.4420 -0.0055 -0.0053 -0.0025 157 VAL   D CA  
5241 C  C   . VAL   D 64  ? 0.4164 0.2965 0.4390 -0.0048 -0.0061 0.0033  157 VAL   D C   
5242 O  O   . VAL   D 64  ? 0.4139 0.2868 0.4405 -0.0044 -0.0060 0.0017  157 VAL   D O   
5243 C  CB  . VAL   D 64  ? 0.4322 0.3159 0.4505 -0.0077 -0.0067 -0.0081 157 VAL   D CB  
5244 C  CG1 . VAL   D 64  ? 0.4377 0.3225 0.4558 -0.0082 -0.0098 -0.0042 157 VAL   D CG1 
5245 C  CG2 . VAL   D 64  ? 0.4401 0.3307 0.4556 -0.0095 -0.0057 -0.0172 157 VAL   D CG2 
5246 N  N   . ARG   D 65  ? 0.4103 0.2921 0.4330 -0.0046 -0.0069 0.0099  158 ARG   D N   
5247 C  CA  . ARG   D 65  ? 0.4053 0.2807 0.4335 -0.0050 -0.0078 0.0138  158 ARG   D CA  
5248 C  C   . ARG   D 65  ? 0.4025 0.2731 0.4305 -0.0049 -0.0105 0.0149  158 ARG   D C   
5249 O  O   . ARG   D 65  ? 0.4151 0.2895 0.4400 -0.0039 -0.0112 0.0165  158 ARG   D O   
5250 C  CB  . ARG   D 65  ? 0.4055 0.2847 0.4363 -0.0057 -0.0055 0.0196  158 ARG   D CB  
5251 C  CG  . ARG   D 65  ? 0.4013 0.2748 0.4398 -0.0075 -0.0063 0.0219  158 ARG   D CG  
5252 C  CD  . ARG   D 65  ? 0.4029 0.2799 0.4456 -0.0095 -0.0027 0.0279  158 ARG   D CD  
5253 N  NE  . ARG   D 65  ? 0.4056 0.2924 0.4475 -0.0092 0.0008  0.0272  158 ARG   D NE  
5254 C  CZ  . ARG   D 65  ? 0.3918 0.2828 0.4405 -0.0097 0.0019  0.0240  158 ARG   D CZ  
5255 N  NH1 . ARG   D 65  ? 0.3888 0.2762 0.4449 -0.0107 -0.0011 0.0215  158 ARG   D NH1 
5256 N  NH2 . ARG   D 65  ? 0.3916 0.2923 0.4399 -0.0086 0.0060  0.0227  158 ARG   D NH2 
5257 N  N   . ALA   D 66  ? 0.4030 0.2674 0.4340 -0.0054 -0.0120 0.0137  159 ALA   D N   
5258 C  CA  . ALA   D 66  ? 0.4045 0.2644 0.4363 -0.0051 -0.0137 0.0136  159 ALA   D CA  
5259 C  C   . ALA   D 66  ? 0.4058 0.2619 0.4432 -0.0063 -0.0141 0.0146  159 ALA   D C   
5260 O  O   . ALA   D 66  ? 0.4024 0.2597 0.4427 -0.0076 -0.0145 0.0134  159 ALA   D O   
5261 C  CB  . ALA   D 66  ? 0.4024 0.2603 0.4317 -0.0053 -0.0145 0.0100  159 ALA   D CB  
5262 N  N   . MET   D 67  ? 0.4127 0.2646 0.4528 -0.0057 -0.0142 0.0159  160 MET   D N   
5263 C  CA  . MET   D 67  ? 0.4188 0.2649 0.4658 -0.0077 -0.0143 0.0152  160 MET   D CA  
5264 C  C   . MET   D 67  ? 0.4181 0.2584 0.4665 -0.0056 -0.0147 0.0126  160 MET   D C   
5265 O  O   . MET   D 67  ? 0.4123 0.2533 0.4590 -0.0021 -0.0142 0.0156  160 MET   D O   
5266 C  CB  . MET   D 67  ? 0.4379 0.2829 0.4900 -0.0091 -0.0116 0.0217  160 MET   D CB  
5267 C  CG  . MET   D 67  ? 0.4563 0.2935 0.5181 -0.0124 -0.0108 0.0209  160 MET   D CG  
5268 S  SD  . MET   D 67  ? 0.4832 0.3171 0.5514 -0.0144 -0.0060 0.0315  160 MET   D SD  
5269 C  CE  . MET   D 67  ? 0.4793 0.3260 0.5468 -0.0174 -0.0044 0.0323  160 MET   D CE  
5270 N  N   . ALA   D 68  ? 0.4183 0.2547 0.4699 -0.0073 -0.0158 0.0064  161 ALA   D N   
5271 C  CA  . ALA   D 68  ? 0.4232 0.2537 0.4774 -0.0052 -0.0154 0.0019  161 ALA   D CA  
5272 C  C   . ALA   D 68  ? 0.4314 0.2516 0.4959 -0.0066 -0.0137 0.0030  161 ALA   D C   
5273 O  O   . ALA   D 68  ? 0.4405 0.2596 0.5103 -0.0114 -0.0135 0.0032  161 ALA   D O   
5274 C  CB  . ALA   D 68  ? 0.4264 0.2597 0.4768 -0.0062 -0.0173 -0.0068 161 ALA   D CB  
5275 N  N   A ILE   D 69  ? 0.4453 0.2582 0.5140 -0.0023 -0.0119 0.0045  162 ILE   D N   
5276 N  N   B ILE   D 69  ? 0.4467 0.2596 0.5153 -0.0025 -0.0121 0.0030  162 ILE   D N   
5277 C  CA  A ILE   D 69  ? 0.4575 0.2564 0.5378 -0.0028 -0.0095 0.0046  162 ILE   D CA  
5278 C  CA  B ILE   D 69  ? 0.4609 0.2600 0.5410 -0.0026 -0.0095 0.0046  162 ILE   D CA  
5279 C  C   A ILE   D 69  ? 0.4676 0.2613 0.5506 0.0016  -0.0089 -0.0035 162 ILE   D C   
5280 C  C   B ILE   D 69  ? 0.4704 0.2630 0.5542 0.0023  -0.0086 -0.0020 162 ILE   D C   
5281 O  O   A ILE   D 69  ? 0.4634 0.2657 0.5396 0.0060  -0.0097 -0.0047 162 ILE   D O   
5282 O  O   B ILE   D 69  ? 0.4670 0.2664 0.5460 0.0082  -0.0089 -0.0005 162 ILE   D O   
5283 C  CB  A ILE   D 69  ? 0.4652 0.2594 0.5490 0.0000  -0.0069 0.0181  162 ILE   D CB  
5284 C  CB  B ILE   D 69  ? 0.4677 0.2646 0.5493 -0.0002 -0.0074 0.0184  162 ILE   D CB  
5285 C  CG1 A ILE   D 69  ? 0.4618 0.2626 0.5426 -0.0044 -0.0064 0.0256  162 ILE   D CG1 
5286 C  CG1 B ILE   D 69  ? 0.4858 0.2669 0.5800 -0.0019 -0.0038 0.0227  162 ILE   D CG1 
5287 C  CG2 A ILE   D 69  ? 0.4799 0.2566 0.5766 0.0006  -0.0037 0.0194  162 ILE   D CG2 
5288 C  CG2 B ILE   D 69  ? 0.4682 0.2707 0.5452 0.0076  -0.0081 0.0232  162 ILE   D CG2 
5289 C  CD1 A ILE   D 69  ? 0.4727 0.2701 0.5555 -0.0020 -0.0032 0.0397  162 ILE   D CD1 
5290 C  CD1 B ILE   D 69  ? 0.4980 0.2742 0.5941 0.0045  -0.0015 0.0364  162 ILE   D CD1 
5291 N  N   . TYR   D 70  ? 0.4815 0.2622 0.5750 0.0001  -0.0071 -0.0099 163 TYR   D N   
5292 C  CA  . TYR   D 70  ? 0.4951 0.2681 0.5940 0.0055  -0.0052 -0.0181 163 TYR   D CA  
5293 C  C   . TYR   D 70  ? 0.5042 0.2715 0.6082 0.0140  -0.0030 -0.0068 163 TYR   D C   
5294 O  O   . TYR   D 70  ? 0.5040 0.2656 0.6117 0.0139  -0.0019 0.0056  163 TYR   D O   
5295 C  CB  . TYR   D 70  ? 0.5032 0.2630 0.6129 0.0005  -0.0038 -0.0298 163 TYR   D CB  
5296 C  CG  . TYR   D 70  ? 0.4967 0.2671 0.5998 -0.0059 -0.0071 -0.0430 163 TYR   D CG  
5297 C  CD1 . TYR   D 70  ? 0.4874 0.2693 0.5801 -0.0029 -0.0084 -0.0519 163 TYR   D CD1 
5298 C  CD2 . TYR   D 70  ? 0.4929 0.2643 0.5999 -0.0147 -0.0089 -0.0456 163 TYR   D CD2 
5299 C  CE1 . TYR   D 70  ? 0.4808 0.2744 0.5656 -0.0079 -0.0118 -0.0621 163 TYR   D CE1 
5300 C  CE2 . TYR   D 70  ? 0.4899 0.2740 0.5907 -0.0196 -0.0131 -0.0569 163 TYR   D CE2 
5301 C  CZ  . TYR   D 70  ? 0.4823 0.2773 0.5709 -0.0158 -0.0147 -0.0646 163 TYR   D CZ  
5302 O  OH  . TYR   D 70  ? 0.4796 0.2885 0.5603 -0.0197 -0.0190 -0.0739 163 TYR   D OH  
5303 N  N   . LYS   D 71  ? 0.5174 0.2886 0.6213 0.0216  -0.0025 -0.0108 164 LYS   D N   
5304 C  CA  . LYS   D 71  ? 0.5315 0.3028 0.6401 0.0314  -0.0016 -0.0004 164 LYS   D CA  
5305 C  C   . LYS   D 71  ? 0.5740 0.3241 0.6978 0.0358  0.0020  0.0016  164 LYS   D C   
5306 O  O   . LYS   D 71  ? 0.5770 0.3224 0.7052 0.0415  0.0027  0.0162  164 LYS   D O   
5307 C  CB  . LYS   D 71  ? 0.5280 0.3134 0.6333 0.0374  -0.0019 -0.0065 164 LYS   D CB  
5308 C  CG  . LYS   D 71  ? 0.5233 0.3148 0.6335 0.0476  -0.0022 0.0033  164 LYS   D CG  
5309 C  CD  . LYS   D 71  ? 0.5155 0.3234 0.6241 0.0519  -0.0020 -0.0040 164 LYS   D CD  
5310 C  CE  . LYS   D 71  ? 0.5171 0.3347 0.6331 0.0625  -0.0029 0.0042  164 LYS   D CE  
5311 N  NZ  . LYS   D 71  ? 0.5207 0.3491 0.6419 0.0681  -0.0005 -0.0057 164 LYS   D NZ  
5312 N  N   . GLN   D 72  ? 0.6072 0.3453 0.7384 0.0334  0.0044  -0.0127 165 GLN   D N   
5313 C  CA  . GLN   D 72  ? 0.6521 0.3670 0.8002 0.0376  0.0088  -0.0145 165 GLN   D CA  
5314 C  C   . GLN   D 72  ? 0.6714 0.3700 0.8268 0.0308  0.0106  -0.0046 165 GLN   D C   
5315 O  O   . GLN   D 72  ? 0.6712 0.3747 0.8215 0.0200  0.0090  -0.0076 165 GLN   D O   
5316 C  CB  . GLN   D 72  ? 0.6817 0.3912 0.8342 0.0355  0.0107  -0.0361 165 GLN   D CB  
5317 C  CG  . GLN   D 72  ? 0.6906 0.4155 0.8377 0.0430  0.0108  -0.0453 165 GLN   D CG  
5318 C  CD  . GLN   D 72  ? 0.7095 0.4381 0.8527 0.0381  0.0115  -0.0668 165 GLN   D CD  
5319 O  OE1 . GLN   D 72  ? 0.7198 0.4550 0.8540 0.0281  0.0086  -0.0728 165 GLN   D OE1 
5320 N  NE2 . GLN   D 72  ? 0.7380 0.4645 0.8878 0.0458  0.0153  -0.0787 165 GLN   D NE2 
5321 N  N   . SER   D 73  ? 0.6930 0.3735 0.8611 0.0373  0.0143  0.0073  166 SER   D N   
5322 C  CA  . SER   D 73  ? 0.7016 0.3667 0.8769 0.0319  0.0174  0.0215  166 SER   D CA  
5323 C  C   . SER   D 73  ? 0.7137 0.3634 0.8998 0.0197  0.0201  0.0079  166 SER   D C   
5324 O  O   . SER   D 73  ? 0.7118 0.3590 0.8994 0.0101  0.0213  0.0152  166 SER   D O   
5325 C  CB  . SER   D 73  ? 0.7288 0.3776 0.9151 0.0431  0.0210  0.0381  166 SER   D CB  
5326 O  OG  . SER   D 73  ? 0.7508 0.3821 0.9518 0.0501  0.0243  0.0273  166 SER   D OG  
5327 N  N   . GLN   D 74  ? 0.7205 0.3625 0.9138 0.0195  0.0211  -0.0121 167 GLN   D N   
5328 C  CA  . GLN   D 74  ? 0.7244 0.3526 0.9295 0.0078  0.0232  -0.0288 167 GLN   D CA  
5329 C  C   . GLN   D 74  ? 0.6933 0.3430 0.8861 -0.0035 0.0179  -0.0398 167 GLN   D C   
5330 O  O   . GLN   D 74  ? 0.6818 0.3252 0.8838 -0.0149 0.0184  -0.0517 167 GLN   D O   
5331 C  CB  . GLN   D 74  ? 0.7446 0.3580 0.9611 0.0125  0.0262  -0.0478 167 GLN   D CB  
5332 C  CG  . GLN   D 74  ? 0.7355 0.3694 0.9387 0.0179  0.0227  -0.0632 167 GLN   D CG  
5333 C  CD  . GLN   D 74  ? 0.7428 0.3804 0.9446 0.0336  0.0237  -0.0547 167 GLN   D CD  
5334 O  OE1 . GLN   D 74  ? 0.7500 0.3881 0.9511 0.0404  0.0236  -0.0338 167 GLN   D OE1 
5335 N  NE2 . GLN   D 74  ? 0.7480 0.3919 0.9487 0.0396  0.0246  -0.0714 167 GLN   D NE2 
5336 N  N   . HIS   D 75  ? 0.6585 0.3327 0.8328 -0.0008 0.0130  -0.0361 168 HIS   D N   
5337 C  CA  . HIS   D 75  ? 0.6422 0.3373 0.8042 -0.0093 0.0077  -0.0448 168 HIS   D CA  
5338 C  C   . HIS   D 75  ? 0.6304 0.3391 0.7829 -0.0117 0.0057  -0.0283 168 HIS   D C   
5339 O  O   . HIS   D 75  ? 0.6032 0.3289 0.7466 -0.0176 0.0015  -0.0331 168 HIS   D O   
5340 C  CB  . HIS   D 75  ? 0.6352 0.3471 0.7836 -0.0043 0.0045  -0.0568 168 HIS   D CB  
5341 C  CG  . HIS   D 75  ? 0.6530 0.3563 0.8082 -0.0026 0.0065  -0.0760 168 HIS   D CG  
5342 N  ND1 . HIS   D 75  ? 0.6659 0.3618 0.8302 -0.0118 0.0066  -0.0926 168 HIS   D ND1 
5343 C  CD2 . HIS   D 75  ? 0.6575 0.3606 0.8119 0.0069  0.0087  -0.0829 168 HIS   D CD2 
5344 C  CE1 . HIS   D 75  ? 0.6798 0.3702 0.8478 -0.0079 0.0088  -0.1096 168 HIS   D CE1 
5345 N  NE2 . HIS   D 75  ? 0.6798 0.3744 0.8419 0.0039  0.0105  -0.1037 168 HIS   D NE2 
5346 N  N   . MET   D 76  ? 0.6365 0.3386 0.7911 -0.0067 0.0085  -0.0097 169 MET   D N   
5347 C  CA  . MET   D 76  ? 0.6132 0.3305 0.7558 -0.0057 0.0067  0.0055  169 MET   D CA  
5348 C  C   . MET   D 76  ? 0.5970 0.3193 0.7416 -0.0166 0.0069  0.0078  169 MET   D C   
5349 O  O   . MET   D 76  ? 0.5698 0.3098 0.7024 -0.0174 0.0041  0.0124  169 MET   D O   
5350 C  CB  . MET   D 76  ? 0.6384 0.3481 0.7829 0.0027  0.0097  0.0241  169 MET   D CB  
5351 C  CG  . MET   D 76  ? 0.6357 0.3646 0.7651 0.0066  0.0069  0.0358  169 MET   D CG  
5352 S  SD  . MET   D 76  ? 0.6701 0.3979 0.7984 0.0201  0.0076  0.0530  169 MET   D SD  
5353 C  CE  . MET   D 76  ? 0.6904 0.3904 0.8362 0.0206  0.0143  0.0650  169 MET   D CE  
5354 N  N   . THR   D 77  ? 0.5935 0.3015 0.7536 -0.0249 0.0103  0.0039  170 THR   D N   
5355 C  CA  . THR   D 77  ? 0.5840 0.2975 0.7502 -0.0363 0.0113  0.0053  170 THR   D CA  
5356 C  C   . THR   D 77  ? 0.5674 0.2969 0.7306 -0.0428 0.0057  -0.0119 170 THR   D C   
5357 O  O   . THR   D 77  ? 0.5784 0.3176 0.7461 -0.0512 0.0053  -0.0119 170 THR   D O   
5358 C  CB  . THR   D 77  ? 0.6018 0.2937 0.7886 -0.0439 0.0177  0.0075  170 THR   D CB  
5359 O  OG1 . THR   D 77  ? 0.6052 0.2879 0.8026 -0.0485 0.0166  -0.0124 170 THR   D OG1 
5360 C  CG2 . THR   D 77  ? 0.6171 0.2897 0.8087 -0.0364 0.0236  0.0247  170 THR   D CG2 
5361 N  N   . GLU   D 78  ? 0.5547 0.2881 0.7110 -0.0389 0.0017  -0.0258 171 GLU   D N   
5362 C  CA  . GLU   D 78  ? 0.5447 0.2955 0.6949 -0.0433 -0.0043 -0.0409 171 GLU   D CA  
5363 C  C   . GLU   D 78  ? 0.5196 0.2901 0.6527 -0.0388 -0.0081 -0.0335 171 GLU   D C   
5364 O  O   . GLU   D 78  ? 0.5096 0.2804 0.6326 -0.0304 -0.0075 -0.0257 171 GLU   D O   
5365 C  CB  . GLU   D 78  ? 0.5590 0.3062 0.7077 -0.0407 -0.0059 -0.0579 171 GLU   D CB  
5366 C  CG  . GLU   D 78  ? 0.5609 0.3270 0.7025 -0.0451 -0.0123 -0.0730 171 GLU   D CG  
5367 C  CD  . GLU   D 78  ? 0.5842 0.3479 0.7255 -0.0447 -0.0133 -0.0925 171 GLU   D CD  
5368 O  OE1 . GLU   D 78  ? 0.6132 0.3583 0.7697 -0.0476 -0.0094 -0.1010 171 GLU   D OE1 
5369 O  OE2 . GLU   D 78  ? 0.5860 0.3662 0.7122 -0.0414 -0.0175 -0.0991 171 GLU   D OE2 
5370 N  N   . VAL   D 79  ? 0.5014 0.2880 0.6331 -0.0442 -0.0118 -0.0362 172 VAL   D N   
5371 C  CA  . VAL   D 79  ? 0.4788 0.2830 0.5962 -0.0402 -0.0153 -0.0308 172 VAL   D CA  
5372 C  C   . VAL   D 79  ? 0.4743 0.2854 0.5784 -0.0349 -0.0193 -0.0393 172 VAL   D C   
5373 O  O   . VAL   D 79  ? 0.4773 0.2917 0.5827 -0.0380 -0.0223 -0.0530 172 VAL   D O   
5374 C  CB  . VAL   D 79  ? 0.4736 0.2932 0.5956 -0.0464 -0.0182 -0.0322 172 VAL   D CB  
5375 C  CG1 . VAL   D 79  ? 0.4561 0.2910 0.5646 -0.0411 -0.0215 -0.0274 172 VAL   D CG1 
5376 C  CG2 . VAL   D 79  ? 0.4809 0.2965 0.6166 -0.0524 -0.0133 -0.0239 172 VAL   D CG2 
5377 N  N   . VAL   D 80  ? 0.4690 0.2839 0.5605 -0.0280 -0.0192 -0.0318 173 VAL   D N   
5378 C  CA  . VAL   D 80  ? 0.4668 0.2900 0.5450 -0.0235 -0.0219 -0.0373 173 VAL   D CA  
5379 C  C   . VAL   D 80  ? 0.4664 0.3054 0.5381 -0.0250 -0.0266 -0.0379 173 VAL   D C   
5380 O  O   . VAL   D 80  ? 0.4596 0.3031 0.5301 -0.0243 -0.0264 -0.0287 173 VAL   D O   
5381 C  CB  . VAL   D 80  ? 0.4589 0.2806 0.5288 -0.0165 -0.0195 -0.0292 173 VAL   D CB  
5382 C  CG1 . VAL   D 80  ? 0.4577 0.2881 0.5155 -0.0132 -0.0211 -0.0343 173 VAL   D CG1 
5383 C  CG2 . VAL   D 80  ? 0.4706 0.2786 0.5479 -0.0132 -0.0155 -0.0263 173 VAL   D CG2 
5384 N  N   . ARG   D 81  ? 0.4831 0.3310 0.5506 -0.0264 -0.0305 -0.0484 174 ARG   D N   
5385 C  CA  . ARG   D 81  ? 0.4988 0.3634 0.5593 -0.0264 -0.0359 -0.0487 174 ARG   D CA  
5386 C  C   . ARG   D 81  ? 0.5059 0.3787 0.5527 -0.0235 -0.0383 -0.0557 174 ARG   D C   
5387 O  O   . ARG   D 81  ? 0.5245 0.3909 0.5701 -0.0228 -0.0357 -0.0634 174 ARG   D O   
5388 C  CB  . ARG   D 81  ? 0.5107 0.3834 0.5831 -0.0330 -0.0397 -0.0550 174 ARG   D CB  
5389 C  CG  . ARG   D 81  ? 0.5328 0.3998 0.6152 -0.0391 -0.0397 -0.0688 174 ARG   D CG  
5390 C  CD  . ARG   D 81  ? 0.5486 0.4277 0.6430 -0.0468 -0.0444 -0.0772 174 ARG   D CD  
5391 N  NE  . ARG   D 81  ? 0.5511 0.4260 0.6617 -0.0520 -0.0413 -0.0706 174 ARG   D NE  
5392 C  CZ  . ARG   D 81  ? 0.5463 0.4330 0.6600 -0.0517 -0.0426 -0.0622 174 ARG   D CZ  
5393 N  NH1 . ARG   D 81  ? 0.5375 0.4392 0.6399 -0.0457 -0.0473 -0.0584 174 ARG   D NH1 
5394 N  NH2 . ARG   D 81  ? 0.5474 0.4301 0.6757 -0.0568 -0.0383 -0.0566 174 ARG   D NH2 
5395 N  N   . ARG   D 82  ? 0.5103 0.3974 0.5477 -0.0213 -0.0426 -0.0527 175 ARG   D N   
5396 C  CA  . ARG   D 82  ? 0.5231 0.4216 0.5458 -0.0187 -0.0452 -0.0579 175 ARG   D CA  
5397 C  C   . ARG   D 82  ? 0.5395 0.4457 0.5654 -0.0233 -0.0492 -0.0740 175 ARG   D C   
5398 O  O   . ARG   D 82  ? 0.5366 0.4434 0.5766 -0.0290 -0.0516 -0.0793 175 ARG   D O   
5399 C  CB  . ARG   D 82  ? 0.5223 0.4336 0.5354 -0.0148 -0.0491 -0.0486 175 ARG   D CB  
5400 C  CG  . ARG   D 82  ? 0.5179 0.4210 0.5287 -0.0108 -0.0450 -0.0345 175 ARG   D CG  
5401 C  CD  . ARG   D 82  ? 0.5248 0.4384 0.5289 -0.0065 -0.0487 -0.0256 175 ARG   D CD  
5402 N  NE  . ARG   D 82  ? 0.5349 0.4539 0.5228 -0.0029 -0.0482 -0.0224 175 ARG   D NE  
5403 C  CZ  . ARG   D 82  ? 0.5444 0.4727 0.5235 0.0016  -0.0512 -0.0138 175 ARG   D CZ  
5404 N  NH1 . ARG   D 82  ? 0.5433 0.4773 0.5292 0.0039  -0.0556 -0.0086 175 ARG   D NH1 
5405 N  NH2 . ARG   D 82  ? 0.5559 0.4883 0.5198 0.0043  -0.0494 -0.0097 175 ARG   D NH2 
5406 N  N   . CYS   D 83  ? 0.5519 0.4649 0.5654 -0.0216 -0.0493 -0.0824 176 CYS   D N   
5407 C  CA  . CYS   D 83  ? 0.5764 0.5008 0.5891 -0.0255 -0.0538 -0.1000 176 CYS   D CA  
5408 C  C   . CYS   D 83  ? 0.5809 0.5272 0.5897 -0.0262 -0.0624 -0.0993 176 CYS   D C   
5409 O  O   . CYS   D 83  ? 0.5792 0.5318 0.5811 -0.0214 -0.0642 -0.0849 176 CYS   D O   
5410 C  CB  . CYS   D 83  ? 0.5859 0.5138 0.5839 -0.0221 -0.0506 -0.1077 176 CYS   D CB  
5411 S  SG  . CYS   D 83  ? 0.5993 0.5443 0.5736 -0.0156 -0.0518 -0.0957 176 CYS   D SG  
5412 N  N   . PRO   D 84  ? 0.6097 0.5686 0.6241 -0.0320 -0.0684 -0.1151 177 PRO   D N   
5413 C  CA  . PRO   D 84  ? 0.6127 0.5969 0.6228 -0.0318 -0.0779 -0.1153 177 PRO   D CA  
5414 C  C   . PRO   D 84  ? 0.6235 0.6218 0.6107 -0.0231 -0.0799 -0.1038 177 PRO   D C   
5415 O  O   . PRO   D 84  ? 0.6240 0.6313 0.6100 -0.0189 -0.0838 -0.0904 177 PRO   D O   
5416 C  CB  . PRO   D 84  ? 0.6349 0.6304 0.6494 -0.0390 -0.0826 -0.1384 177 PRO   D CB  
5417 C  CG  . PRO   D 84  ? 0.6280 0.5982 0.6610 -0.0454 -0.0755 -0.1467 177 PRO   D CG  
5418 C  CD  . PRO   D 84  ? 0.6167 0.5663 0.6431 -0.0389 -0.0665 -0.1338 177 PRO   D CD  
5419 N  N   . HIS   D 85  ? 0.6327 0.6315 0.6034 -0.0204 -0.0762 -0.1081 178 HIS   D N   
5420 C  CA  . HIS   D 85  ? 0.6386 0.6517 0.5859 -0.0131 -0.0770 -0.0979 178 HIS   D CA  
5421 C  C   . HIS   D 85  ? 0.6304 0.6340 0.5763 -0.0073 -0.0739 -0.0750 178 HIS   D C   
5422 O  O   . HIS   D 85  ? 0.6254 0.6436 0.5623 -0.0021 -0.0792 -0.0635 178 HIS   D O   
5423 C  CB  . HIS   D 85  ? 0.6533 0.6645 0.5862 -0.0119 -0.0704 -0.1055 178 HIS   D CB  
5424 C  CG  . HIS   D 85  ? 0.6533 0.6743 0.5640 -0.0050 -0.0682 -0.0911 178 HIS   D CG  
5425 N  ND1 . HIS   D 85  ? 0.6764 0.7230 0.5697 -0.0017 -0.0752 -0.0889 178 HIS   D ND1 
5426 C  CD2 . HIS   D 85  ? 0.6522 0.6619 0.5558 -0.0013 -0.0597 -0.0778 178 HIS   D CD2 
5427 C  CE1 . HIS   D 85  ? 0.6778 0.7267 0.5537 0.0039  -0.0705 -0.0735 178 HIS   D CE1 
5428 N  NE2 . HIS   D 85  ? 0.6569 0.6833 0.5397 0.0036  -0.0608 -0.0670 178 HIS   D NE2 
5429 N  N   . HIS   D 86  ? 0.6106 0.5912 0.5650 -0.0077 -0.0659 -0.0688 179 HIS   D N   
5430 C  CA  . HIS   D 86  ? 0.6149 0.5846 0.5683 -0.0031 -0.0617 -0.0496 179 HIS   D CA  
5431 C  C   . HIS   D 86  ? 0.6172 0.5881 0.5833 -0.0025 -0.0665 -0.0422 179 HIS   D C   
5432 O  O   . HIS   D 86  ? 0.6056 0.5770 0.5673 0.0030  -0.0666 -0.0273 179 HIS   D O   
5433 C  CB  . HIS   D 86  ? 0.5971 0.5458 0.5559 -0.0041 -0.0526 -0.0476 179 HIS   D CB  
5434 C  CG  . HIS   D 86  ? 0.6023 0.5524 0.5464 -0.0020 -0.0468 -0.0474 179 HIS   D CG  
5435 N  ND1 . HIS   D 86  ? 0.5948 0.5380 0.5413 -0.0038 -0.0414 -0.0583 179 HIS   D ND1 
5436 C  CD2 . HIS   D 86  ? 0.6022 0.5608 0.5298 0.0019  -0.0452 -0.0373 179 HIS   D CD2 
5437 C  CE1 . HIS   D 86  ? 0.6072 0.5567 0.5394 -0.0012 -0.0366 -0.0560 179 HIS   D CE1 
5438 N  NE2 . HIS   D 86  ? 0.6023 0.5608 0.5223 0.0017  -0.0385 -0.0425 179 HIS   D NE2 
5439 N  N   . GLU   D 87  ? 0.6389 0.6105 0.6213 -0.0079 -0.0696 -0.0522 180 GLU   D N   
5440 C  CA  . GLU   D 87  ? 0.6507 0.6268 0.6475 -0.0080 -0.0737 -0.0471 180 GLU   D CA  
5441 C  C   . GLU   D 87  ? 0.6773 0.6760 0.6661 -0.0022 -0.0820 -0.0413 180 GLU   D C   
5442 O  O   . GLU   D 87  ? 0.6845 0.6837 0.6789 0.0025  -0.0829 -0.0292 180 GLU   D O   
5443 C  CB  . GLU   D 87  ? 0.6594 0.6344 0.6746 -0.0163 -0.0750 -0.0604 180 GLU   D CB  
5444 C  CG  . GLU   D 87  ? 0.6528 0.6358 0.6844 -0.0175 -0.0786 -0.0568 180 GLU   D CG  
5445 C  CD  . GLU   D 87  ? 0.6724 0.6590 0.7223 -0.0271 -0.0805 -0.0708 180 GLU   D CD  
5446 O  OE1 . GLU   D 87  ? 0.6819 0.6598 0.7327 -0.0328 -0.0781 -0.0831 180 GLU   D OE1 
5447 O  OE2 . GLU   D 87  ? 0.6666 0.6644 0.7312 -0.0290 -0.0838 -0.0695 180 GLU   D OE2 
5448 N  N   . ARG   D 88  ? 0.7137 0.7309 0.6892 -0.0018 -0.0875 -0.0489 181 ARG   D N   
5449 C  CA  . ARG   D 88  ? 0.7414 0.7844 0.7079 0.0041  -0.0968 -0.0437 181 ARG   D CA  
5450 C  C   . ARG   D 88  ? 0.7460 0.7878 0.6925 0.0131  -0.0942 -0.0262 181 ARG   D C   
5451 O  O   . ARG   D 88  ? 0.7482 0.8082 0.6883 0.0203  -0.1012 -0.0166 181 ARG   D O   
5452 C  CB  . ARG   D 88  ? 0.7778 0.8445 0.7374 0.0002  -0.1046 -0.0609 181 ARG   D CB  
5453 C  CG  . ARG   D 88  ? 0.7952 0.8602 0.7722 -0.0105 -0.1055 -0.0816 181 ARG   D CG  
5454 C  CD  . ARG   D 88  ? 0.8095 0.8825 0.8092 -0.0137 -0.1106 -0.0825 181 ARG   D CD  
5455 N  NE  . ARG   D 88  ? 0.8273 0.8928 0.8460 -0.0251 -0.1089 -0.0997 181 ARG   D NE  
5456 C  CZ  . ARG   D 88  ? 0.8318 0.9008 0.8735 -0.0310 -0.1108 -0.1030 181 ARG   D CZ  
5457 N  NH1 . ARG   D 88  ? 0.8371 0.8967 0.8953 -0.0419 -0.1081 -0.1180 181 ARG   D NH1 
5458 N  NH2 . ARG   D 88  ? 0.8322 0.9137 0.8816 -0.0259 -0.1147 -0.0913 181 ARG   D NH2 
5459 N  N   . CYS   D 89  ? 0.7408 0.7638 0.6786 0.0130  -0.0848 -0.0214 182 CYS   D N   
5460 C  CA  . CYS   D 89  ? 0.7570 0.7765 0.6781 0.0201  -0.0806 -0.0037 182 CYS   D CA  
5461 C  C   . CYS   D 89  ? 0.7580 0.7675 0.6884 0.0260  -0.0799 0.0130  182 CYS   D C   
5462 O  O   . CYS   D 89  ? 0.7558 0.7513 0.7037 0.0231  -0.0772 0.0108  182 CYS   D O   
5463 C  CB  . CYS   D 89  ? 0.7528 0.7557 0.6666 0.0171  -0.0703 -0.0044 182 CYS   D CB  
5464 S  SG  . CYS   D 89  ? 0.7747 0.7936 0.6677 0.0156  -0.0694 -0.0154 182 CYS   D SG  
5465 N  N   . SER   D 90  ? 0.7828 0.7993 0.7016 0.0344  -0.0818 0.0292  183 SER   D N   
5466 C  CA  . SER   D 90  ? 0.7940 0.8067 0.7217 0.0424  -0.0836 0.0446  183 SER   D CA  
5467 C  C   . SER   D 90  ? 0.8007 0.7847 0.7362 0.0421  -0.0735 0.0535  183 SER   D C   
5468 O  O   . SER   D 90  ? 0.7988 0.7755 0.7508 0.0440  -0.0737 0.0552  183 SER   D O   
5469 C  CB  . SER   D 90  ? 0.8207 0.8503 0.7331 0.0522  -0.0892 0.0596  183 SER   D CB  
5470 O  OG  . SER   D 90  ? 0.8377 0.8611 0.7306 0.0532  -0.0825 0.0697  183 SER   D OG  
5471 N  N   . ASP   D 91  ? 0.8217 0.7918 0.7467 0.0394  -0.0650 0.0577  184 ASP   D N   
5472 C  CA  . ASP   D 91  ? 0.8177 0.7623 0.7489 0.0382  -0.0553 0.0656  184 ASP   D CA  
5473 C  C   . ASP   D 91  ? 0.7872 0.7200 0.7382 0.0349  -0.0541 0.0575  184 ASP   D C   
5474 O  O   . ASP   D 91  ? 0.7853 0.7084 0.7410 0.0279  -0.0493 0.0481  184 ASP   D O   
5475 C  CB  . ASP   D 91  ? 0.8308 0.7678 0.7515 0.0326  -0.0470 0.0641  184 ASP   D CB  
5476 C  CG  . ASP   D 91  ? 0.8535 0.8013 0.7536 0.0357  -0.0459 0.0741  184 ASP   D CG  
5477 O  OD1 . ASP   D 91  ? 0.8618 0.8282 0.7528 0.0416  -0.0536 0.0784  184 ASP   D OD1 
5478 O  OD2 . ASP   D 91  ? 0.8652 0.8048 0.7583 0.0321  -0.0372 0.0777  184 ASP   D OD2 
5479 N  N   . SER   D 92  ? 0.7791 0.7136 0.7415 0.0406  -0.0579 0.0622  185 SER   D N   
5480 C  CA  . SER   D 92  ? 0.7602 0.6876 0.7411 0.0389  -0.0571 0.0558  185 SER   D CA  
5481 C  C   . SER   D 92  ? 0.7466 0.6578 0.7349 0.0447  -0.0523 0.0668  185 SER   D C   
5482 O  O   . SER   D 92  ? 0.7635 0.6765 0.7473 0.0531  -0.0541 0.0798  185 SER   D O   
5483 C  CB  . SER   D 92  ? 0.7652 0.7128 0.7555 0.0401  -0.0656 0.0489  185 SER   D CB  
5484 O  OG  . SER   D 92  ? 0.8017 0.7645 0.7886 0.0494  -0.0725 0.0587  185 SER   D OG  
5485 N  N   . ASP   D 93  ? 0.7137 0.6102 0.7128 0.0409  -0.0465 0.0618  186 ASP   D N   
5486 C  CA  . ASP   D 93  ? 0.7007 0.5791 0.7070 0.0449  -0.0406 0.0688  186 ASP   D CA  
5487 C  C   . ASP   D 93  ? 0.6789 0.5625 0.7004 0.0511  -0.0432 0.0678  186 ASP   D C   
5488 O  O   . ASP   D 93  ? 0.7120 0.5810 0.7416 0.0546  -0.0381 0.0708  186 ASP   D O   
5489 C  CB  . ASP   D 93  ? 0.6977 0.5597 0.7056 0.0371  -0.0329 0.0627  186 ASP   D CB  
5490 C  CG  . ASP   D 93  ? 0.6787 0.5437 0.6955 0.0317  -0.0328 0.0505  186 ASP   D CG  
5491 O  OD1 . ASP   D 93  ? 0.6594 0.5393 0.6810 0.0320  -0.0382 0.0455  186 ASP   D OD1 
5492 O  OD2 . ASP   D 93  ? 0.6800 0.5335 0.6995 0.0271  -0.0272 0.0462  186 ASP   D OD2 
5493 N  N   . GLY   D 94  ? 0.6364 0.5404 0.6630 0.0520  -0.0504 0.0627  187 GLY   D N   
5494 C  CA  . GLY   D 94  ? 0.6116 0.5258 0.6542 0.0576  -0.0531 0.0611  187 GLY   D CA  
5495 C  C   . GLY   D 94  ? 0.5755 0.4865 0.6295 0.0515  -0.0486 0.0504  187 GLY   D C   
5496 O  O   . GLY   D 94  ? 0.5820 0.5038 0.6499 0.0549  -0.0500 0.0478  187 GLY   D O   
5497 N  N   . LEU   D 95  ? 0.5465 0.4446 0.5951 0.0431  -0.0432 0.0449  188 LEU   D N   
5498 C  CA  . LEU   D 95  ? 0.5235 0.4176 0.5805 0.0379  -0.0382 0.0367  188 LEU   D CA  
5499 C  C   . LEU   D 95  ? 0.5087 0.4095 0.5638 0.0288  -0.0397 0.0288  188 LEU   D C   
5500 O  O   . LEU   D 95  ? 0.5074 0.4160 0.5726 0.0260  -0.0391 0.0236  188 LEU   D O   
5501 C  CB  . LEU   D 95  ? 0.5195 0.3937 0.5733 0.0367  -0.0308 0.0371  188 LEU   D CB  
5502 C  CG  . LEU   D 95  ? 0.5261 0.3891 0.5835 0.0449  -0.0280 0.0441  188 LEU   D CG  
5503 C  CD1 . LEU   D 95  ? 0.5320 0.3753 0.5857 0.0410  -0.0210 0.0427  188 LEU   D CD1 
5504 C  CD2 . LEU   D 95  ? 0.5213 0.3913 0.5933 0.0517  -0.0276 0.0421  188 LEU   D CD2 
5505 N  N   . ALA   D 96  ? 0.5047 0.4025 0.5482 0.0246  -0.0408 0.0282  189 ALA   D N   
5506 C  CA  . ALA   D 96  ? 0.4846 0.3837 0.5265 0.0165  -0.0408 0.0205  189 ALA   D CA  
5507 C  C   . ALA   D 96  ? 0.4727 0.3885 0.5189 0.0146  -0.0473 0.0156  189 ALA   D C   
5508 O  O   . ALA   D 96  ? 0.4724 0.3988 0.5142 0.0185  -0.0529 0.0180  189 ALA   D O   
5509 C  CB  . ALA   D 96  ? 0.4973 0.3869 0.5267 0.0138  -0.0386 0.0209  189 ALA   D CB  
5510 N  N   . PRO   D 97  ? 0.4613 0.3810 0.5166 0.0082  -0.0469 0.0086  190 PRO   D N   
5511 C  CA  . PRO   D 97  ? 0.4545 0.3888 0.5150 0.0042  -0.0528 0.0017  190 PRO   D CA  
5512 C  C   . PRO   D 97  ? 0.4611 0.3942 0.5083 0.0026  -0.0553 -0.0017 190 PRO   D C   
5513 O  O   . PRO   D 97  ? 0.4640 0.3836 0.5027 0.0014  -0.0509 -0.0012 190 PRO   D O   
5514 C  CB  . PRO   D 97  ? 0.4413 0.3733 0.5135 -0.0033 -0.0492 -0.0036 190 PRO   D CB  
5515 C  CG  . PRO   D 97  ? 0.4375 0.3598 0.5118 -0.0010 -0.0425 0.0018  190 PRO   D CG  
5516 C  CD  . PRO   D 97  ? 0.4410 0.3518 0.5022 0.0042  -0.0408 0.0072  190 PRO   D CD  
5517 N  N   . PRO   D 98  ? 0.4766 0.4262 0.5221 0.0027  -0.0626 -0.0061 191 PRO   D N   
5518 C  CA  . PRO   D 98  ? 0.4889 0.4402 0.5202 0.0018  -0.0648 -0.0104 191 PRO   D CA  
5519 C  C   . PRO   D 98  ? 0.4921 0.4332 0.5242 -0.0055 -0.0612 -0.0203 191 PRO   D C   
5520 O  O   . PRO   D 98  ? 0.4977 0.4357 0.5178 -0.0054 -0.0602 -0.0228 191 PRO   D O   
5521 C  CB  . PRO   D 98  ? 0.4940 0.4690 0.5256 0.0033  -0.0741 -0.0143 191 PRO   D CB  
5522 C  CG  . PRO   D 98  ? 0.4941 0.4793 0.5451 0.0014  -0.0764 -0.0164 191 PRO   D CG  
5523 C  CD  . PRO   D 98  ? 0.4833 0.4531 0.5402 0.0041  -0.0690 -0.0077 191 PRO   D CD  
5524 N  N   . GLN   D 99  ? 0.4952 0.4313 0.5418 -0.0113 -0.0588 -0.0248 192 GLN   D N   
5525 C  CA  . GLN   D 99  ? 0.4977 0.4228 0.5488 -0.0180 -0.0553 -0.0335 192 GLN   D CA  
5526 C  C   . GLN   D 99  ? 0.4842 0.3908 0.5307 -0.0165 -0.0481 -0.0277 192 GLN   D C   
5527 O  O   . GLN   D 99  ? 0.4977 0.3946 0.5443 -0.0193 -0.0452 -0.0336 192 GLN   D O   
5528 C  CB  . GLN   D 99  ? 0.5047 0.4318 0.5743 -0.0248 -0.0550 -0.0380 192 GLN   D CB  
5529 C  CG  . GLN   D 99  ? 0.5292 0.4758 0.6066 -0.0286 -0.0624 -0.0472 192 GLN   D CG  
5530 C  CD  . GLN   D 99  ? 0.5353 0.4828 0.6329 -0.0374 -0.0610 -0.0528 192 GLN   D CD  
5531 O  OE1 . GLN   D 99  ? 0.5462 0.4786 0.6510 -0.0406 -0.0541 -0.0490 192 GLN   D OE1 
5532 N  NE2 . GLN   D 99  ? 0.5463 0.5130 0.6535 -0.0419 -0.0675 -0.0617 192 GLN   D NE2 
5533 N  N   . HIS   D 100 ? 0.4565 0.3588 0.5003 -0.0120 -0.0452 -0.0176 193 HIS   D N   
5534 C  CA  . HIS   D 100 ? 0.4403 0.3283 0.4821 -0.0112 -0.0390 -0.0126 193 HIS   D CA  
5535 C  C   . HIS   D 100 ? 0.4381 0.3208 0.4679 -0.0092 -0.0372 -0.0128 193 HIS   D C   
5536 O  O   . HIS   D 100 ? 0.4461 0.3334 0.4663 -0.0057 -0.0386 -0.0094 193 HIS   D O   
5537 C  CB  . HIS   D 100 ? 0.4242 0.3111 0.4678 -0.0078 -0.0367 -0.0044 193 HIS   D CB  
5538 C  CG  . HIS   D 100 ? 0.4198 0.3091 0.4759 -0.0105 -0.0353 -0.0039 193 HIS   D CG  
5539 N  ND1 . HIS   D 100 ? 0.4146 0.2980 0.4727 -0.0100 -0.0304 0.0005  193 HIS   D ND1 
5540 C  CD2 . HIS   D 100 ? 0.4237 0.3221 0.4910 -0.0143 -0.0376 -0.0078 193 HIS   D CD2 
5541 C  CE1 . HIS   D 100 ? 0.4108 0.2994 0.4798 -0.0130 -0.0291 0.0004  193 HIS   D CE1 
5542 N  NE2 . HIS   D 100 ? 0.4245 0.3219 0.5005 -0.0160 -0.0333 -0.0045 193 HIS   D NE2 
5543 N  N   . LEU   D 101 ? 0.4290 0.3026 0.4603 -0.0108 -0.0336 -0.0157 194 LEU   D N   
5544 C  CA  . LEU   D 101 ? 0.4255 0.2954 0.4479 -0.0088 -0.0309 -0.0163 194 LEU   D CA  
5545 C  C   . LEU   D 101 ? 0.4139 0.2807 0.4315 -0.0062 -0.0279 -0.0080 194 LEU   D C   
5546 O  O   . LEU   D 101 ? 0.4063 0.2753 0.4149 -0.0046 -0.0269 -0.0063 194 LEU   D O   
5547 C  CB  . LEU   D 101 ? 0.4269 0.2884 0.4549 -0.0100 -0.0279 -0.0209 194 LEU   D CB  
5548 C  CG  . LEU   D 101 ? 0.4297 0.2892 0.4513 -0.0073 -0.0244 -0.0212 194 LEU   D CG  
5549 C  CD1 . LEU   D 101 ? 0.4385 0.3058 0.4505 -0.0066 -0.0254 -0.0271 194 LEU   D CD1 
5550 C  CD2 . LEU   D 101 ? 0.4269 0.2781 0.4562 -0.0066 -0.0216 -0.0238 194 LEU   D CD2 
5551 N  N   . ILE   D 102 ? 0.4020 0.2646 0.4254 -0.0064 -0.0262 -0.0035 195 ILE   D N   
5552 C  CA  . ILE   D 102 ? 0.4024 0.2614 0.4232 -0.0050 -0.0230 0.0017  195 ILE   D CA  
5553 C  C   . ILE   D 102 ? 0.4019 0.2622 0.4229 -0.0033 -0.0238 0.0062  195 ILE   D C   
5554 O  O   . ILE   D 102 ? 0.4046 0.2672 0.4322 -0.0034 -0.0248 0.0064  195 ILE   D O   
5555 C  CB  . ILE   D 102 ? 0.3939 0.2487 0.4196 -0.0057 -0.0206 0.0025  195 ILE   D CB  
5556 C  CG1 . ILE   D 102 ? 0.4024 0.2548 0.4307 -0.0060 -0.0200 -0.0010 195 ILE   D CG1 
5557 C  CG2 . ILE   D 102 ? 0.3912 0.2448 0.4141 -0.0052 -0.0180 0.0052  195 ILE   D CG2 
5558 C  CD1 . ILE   D 102 ? 0.3950 0.2451 0.4263 -0.0050 -0.0179 0.0016  195 ILE   D CD1 
5559 N  N   . ARG   D 103 ? 0.4114 0.2700 0.4265 -0.0017 -0.0225 0.0100  196 ARG   D N   
5560 C  CA  . ARG   D 103 ? 0.4152 0.2717 0.4315 0.0009  -0.0221 0.0148  196 ARG   D CA  
5561 C  C   . ARG   D 103 ? 0.4212 0.2702 0.4380 -0.0002 -0.0176 0.0160  196 ARG   D C   
5562 O  O   . ARG   D 103 ? 0.4246 0.2725 0.4389 -0.0027 -0.0155 0.0143  196 ARG   D O   
5563 C  CB  . ARG   D 103 ? 0.4290 0.2883 0.4389 0.0039  -0.0241 0.0195  196 ARG   D CB  
5564 C  CG  . ARG   D 103 ? 0.4319 0.3021 0.4410 0.0048  -0.0296 0.0168  196 ARG   D CG  
5565 C  CD  . ARG   D 103 ? 0.4438 0.3187 0.4470 0.0096  -0.0323 0.0236  196 ARG   D CD  
5566 N  NE  . ARG   D 103 ? 0.4528 0.3414 0.4531 0.0102  -0.0383 0.0202  196 ARG   D NE  
5567 C  CZ  . ARG   D 103 ? 0.4606 0.3578 0.4520 0.0141  -0.0417 0.0252  196 ARG   D CZ  
5568 N  NH1 . ARG   D 103 ? 0.4782 0.3694 0.4633 0.0180  -0.0389 0.0356  196 ARG   D NH1 
5569 N  NH2 . ARG   D 103 ? 0.4633 0.3754 0.4524 0.0140  -0.0478 0.0198  196 ARG   D NH2 
5570 N  N   . VAL   D 104 ? 0.4225 0.2675 0.4433 0.0016  -0.0162 0.0177  197 VAL   D N   
5571 C  CA  . VAL   D 104 ? 0.4287 0.2655 0.4504 0.0002  -0.0119 0.0178  197 VAL   D CA  
5572 C  C   . VAL   D 104 ? 0.4425 0.2727 0.4631 0.0034  -0.0109 0.0242  197 VAL   D C   
5573 O  O   . VAL   D 104 ? 0.4377 0.2701 0.4604 0.0084  -0.0135 0.0274  197 VAL   D O   
5574 C  CB  . VAL   D 104 ? 0.4214 0.2578 0.4487 -0.0001 -0.0102 0.0132  197 VAL   D CB  
5575 C  CG1 . VAL   D 104 ? 0.4348 0.2627 0.4642 -0.0018 -0.0062 0.0112  197 VAL   D CG1 
5576 C  CG2 . VAL   D 104 ? 0.4104 0.2533 0.4373 -0.0028 -0.0110 0.0094  197 VAL   D CG2 
5577 N  N   . GLU   D 105 ? 0.4651 0.2882 0.4833 0.0008  -0.0072 0.0269  198 GLU   D N   
5578 C  CA  . GLU   D 105 ? 0.4890 0.3031 0.5060 0.0035  -0.0049 0.0354  198 GLU   D CA  
5579 C  C   . GLU   D 105 ? 0.4928 0.2941 0.5178 0.0021  -0.0001 0.0332  198 GLU   D C   
5580 O  O   . GLU   D 105 ? 0.4821 0.2839 0.5105 -0.0028 0.0015  0.0250  198 GLU   D O   
5581 C  CB  . GLU   D 105 ? 0.5086 0.3242 0.5174 0.0010  -0.0031 0.0407  198 GLU   D CB  
5582 C  CG  . GLU   D 105 ? 0.5263 0.3327 0.5375 -0.0046 0.0033  0.0419  198 GLU   D CG  
5583 C  CD  . GLU   D 105 ? 0.5488 0.3594 0.5523 -0.0076 0.0063  0.0472  198 GLU   D CD  
5584 O  OE1 . GLU   D 105 ? 0.5916 0.3935 0.5940 -0.0084 0.0110  0.0562  198 GLU   D OE1 
5585 O  OE2 . GLU   D 105 ? 0.5482 0.3703 0.5473 -0.0090 0.0045  0.0426  198 GLU   D OE2 
5586 N  N   . GLY   D 106 ? 0.5083 0.2988 0.5364 0.0069  0.0016  0.0401  199 GLY   D N   
5587 C  CA  . GLY   D 106 ? 0.5141 0.2888 0.5510 0.0058  0.0071  0.0381  199 GLY   D CA  
5588 C  C   . GLY   D 106 ? 0.5113 0.2870 0.5557 0.0070  0.0070  0.0274  199 GLY   D C   
5589 O  O   . GLY   D 106 ? 0.5240 0.2897 0.5750 0.0033  0.0115  0.0204  199 GLY   D O   
5590 N  N   . ASN   D 107 ? 0.4883 0.2761 0.5322 0.0115  0.0025  0.0255  200 ASN   D N   
5591 C  CA  . ASN   D 107 ? 0.4786 0.2704 0.5285 0.0128  0.0032  0.0160  200 ASN   D CA  
5592 C  C   . ASN   D 107 ? 0.4726 0.2713 0.5268 0.0212  0.0003  0.0192  200 ASN   D C   
5593 O  O   . ASN   D 107 ? 0.4525 0.2649 0.5039 0.0217  -0.0041 0.0206  200 ASN   D O   
5594 C  CB  . ASN   D 107 ? 0.4609 0.2642 0.5068 0.0067  0.0020  0.0081  200 ASN   D CB  
5595 C  CG  . ASN   D 107 ? 0.4640 0.2695 0.5144 0.0064  0.0045  -0.0019 200 ASN   D CG  
5596 O  OD1 . ASN   D 107 ? 0.4646 0.2691 0.5208 0.0122  0.0058  -0.0033 200 ASN   D OD1 
5597 N  ND2 . ASN   D 107 ? 0.4580 0.2684 0.5055 0.0004  0.0052  -0.0093 200 ASN   D ND2 
5598 N  N   . LEU   D 108 ? 0.4871 0.2768 0.5499 0.0275  0.0032  0.0193  201 LEU   D N   
5599 C  CA  . LEU   D 108 ? 0.4889 0.2863 0.5586 0.0369  0.0007  0.0228  201 LEU   D CA  
5600 C  C   . LEU   D 108 ? 0.4720 0.2836 0.5455 0.0364  0.0010  0.0136  201 LEU   D C   
5601 O  O   . LEU   D 108 ? 0.4662 0.2884 0.5463 0.0428  -0.0011 0.0156  201 LEU   D O   
5602 C  CB  . LEU   D 108 ? 0.5135 0.2953 0.5926 0.0450  0.0045  0.0263  201 LEU   D CB  
5603 C  CG  . LEU   D 108 ? 0.5378 0.3011 0.6141 0.0439  0.0069  0.0352  201 LEU   D CG  
5604 C  CD1 . LEU   D 108 ? 0.5565 0.3030 0.6367 0.0373  0.0139  0.0259  201 LEU   D CD1 
5605 C  CD2 . LEU   D 108 ? 0.5632 0.3186 0.6455 0.0554  0.0064  0.0478  201 LEU   D CD2 
5606 N  N   . ARG   D 109 ? 0.4629 0.2766 0.5325 0.0293  0.0034  0.0047  202 ARG   D N   
5607 C  CA  . ARG   D 109 ? 0.4605 0.2885 0.5316 0.0283  0.0045  -0.0025 202 ARG   D CA  
5608 C  C   . ARG   D 109 ? 0.4361 0.2766 0.5004 0.0229  0.0005  0.0000  202 ARG   D C   
5609 O  O   . ARG   D 109 ? 0.4343 0.2860 0.4988 0.0211  0.0017  -0.0036 202 ARG   D O   
5610 C  CB  . ARG   D 109 ? 0.4719 0.2961 0.5419 0.0247  0.0096  -0.0136 202 ARG   D CB  
5611 C  CG  . ARG   D 109 ? 0.4999 0.3101 0.5784 0.0296  0.0146  -0.0190 202 ARG   D CG  
5612 C  CD  . ARG   D 109 ? 0.5180 0.3239 0.5941 0.0237  0.0187  -0.0316 202 ARG   D CD  
5613 N  NE  . ARG   D 109 ? 0.5235 0.3457 0.5972 0.0234  0.0206  -0.0401 202 ARG   D NE  
5614 C  CZ  . ARG   D 109 ? 0.5387 0.3654 0.6074 0.0183  0.0231  -0.0518 202 ARG   D CZ  
5615 N  NH1 . ARG   D 109 ? 0.5464 0.3627 0.6136 0.0123  0.0235  -0.0575 202 ARG   D NH1 
5616 N  NH2 . ARG   D 109 ? 0.5363 0.3797 0.6014 0.0191  0.0252  -0.0574 202 ARG   D NH2 
5617 N  N   . VAL   D 110 ? 0.4273 0.2657 0.4863 0.0207  -0.0035 0.0064  203 VAL   D N   
5618 C  CA  . VAL   D 110 ? 0.4067 0.2543 0.4605 0.0161  -0.0072 0.0083  203 VAL   D CA  
5619 C  C   . VAL   D 110 ? 0.3975 0.2586 0.4579 0.0181  -0.0092 0.0091  203 VAL   D C   
5620 O  O   . VAL   D 110 ? 0.3997 0.2643 0.4675 0.0241  -0.0103 0.0114  203 VAL   D O   
5621 C  CB  . VAL   D 110 ? 0.4050 0.2483 0.4524 0.0146  -0.0106 0.0138  203 VAL   D CB  
5622 C  CG1 . VAL   D 110 ? 0.4142 0.2582 0.4638 0.0206  -0.0137 0.0204  203 VAL   D CG1 
5623 C  CG2 . VAL   D 110 ? 0.3965 0.2470 0.4395 0.0099  -0.0134 0.0134  203 VAL   D CG2 
5624 N  N   . GLU   D 111 ? 0.3885 0.2574 0.4477 0.0133  -0.0094 0.0078  204 GLU   D N   
5625 C  CA  . GLU   D 111 ? 0.3848 0.2668 0.4518 0.0129  -0.0102 0.0082  204 GLU   D CA  
5626 C  C   . GLU   D 111 ? 0.3762 0.2599 0.4403 0.0072  -0.0133 0.0097  204 GLU   D C   
5627 O  O   . GLU   D 111 ? 0.3681 0.2454 0.4248 0.0039  -0.0125 0.0095  204 GLU   D O   
5628 C  CB  . GLU   D 111 ? 0.3919 0.2803 0.4623 0.0128  -0.0045 0.0047  204 GLU   D CB  
5629 C  CG  . GLU   D 111 ? 0.3902 0.2913 0.4669 0.0093  -0.0033 0.0059  204 GLU   D CG  
5630 C  CD  . GLU   D 111 ? 0.3977 0.3058 0.4741 0.0084  0.0031  0.0037  204 GLU   D CD  
5631 O  OE1 . GLU   D 111 ? 0.4108 0.3192 0.4878 0.0129  0.0066  -0.0008 204 GLU   D OE1 
5632 O  OE2 . GLU   D 111 ? 0.3932 0.3065 0.4686 0.0035  0.0050  0.0066  204 GLU   D OE2 
5633 N  N   . TYR   D 112 ? 0.3723 0.2649 0.4433 0.0065  -0.0169 0.0104  205 TYR   D N   
5634 C  CA  . TYR   D 112 ? 0.3703 0.2636 0.4406 0.0010  -0.0199 0.0099  205 TYR   D CA  
5635 C  C   . TYR   D 112 ? 0.3726 0.2754 0.4535 -0.0033 -0.0181 0.0092  205 TYR   D C   
5636 O  O   . TYR   D 112 ? 0.3779 0.2919 0.4686 -0.0014 -0.0171 0.0090  205 TYR   D O   
5637 C  CB  . TYR   D 112 ? 0.3714 0.2670 0.4397 0.0027  -0.0260 0.0098  205 TYR   D CB  
5638 C  CG  . TYR   D 112 ? 0.3747 0.2602 0.4316 0.0054  -0.0266 0.0119  205 TYR   D CG  
5639 C  CD1 . TYR   D 112 ? 0.3753 0.2539 0.4242 0.0021  -0.0266 0.0108  205 TYR   D CD1 
5640 C  CD2 . TYR   D 112 ? 0.3854 0.2684 0.4410 0.0114  -0.0266 0.0154  205 TYR   D CD2 
5641 C  CE1 . TYR   D 112 ? 0.3818 0.2533 0.4215 0.0037  -0.0263 0.0128  205 TYR   D CE1 
5642 C  CE2 . TYR   D 112 ? 0.3890 0.2621 0.4353 0.0128  -0.0260 0.0184  205 TYR   D CE2 
5643 C  CZ  . TYR   D 112 ? 0.3880 0.2563 0.4264 0.0085  -0.0257 0.0170  205 TYR   D CZ  
5644 O  OH  . TYR   D 112 ? 0.3927 0.2533 0.4231 0.0091  -0.0242 0.0200  205 TYR   D OH  
5645 N  N   . LEU   D 113 ? 0.3776 0.2760 0.4578 -0.0089 -0.0170 0.0094  206 LEU   D N   
5646 C  CA  . LEU   D 113 ? 0.3798 0.2841 0.4703 -0.0145 -0.0139 0.0103  206 LEU   D CA  
5647 C  C   . LEU   D 113 ? 0.3814 0.2830 0.4766 -0.0202 -0.0172 0.0074  206 LEU   D C   
5648 O  O   . LEU   D 113 ? 0.3829 0.2735 0.4701 -0.0203 -0.0185 0.0066  206 LEU   D O   
5649 C  CB  . LEU   D 113 ? 0.3869 0.2867 0.4726 -0.0156 -0.0078 0.0147  206 LEU   D CB  
5650 C  CG  . LEU   D 113 ? 0.3922 0.2950 0.4866 -0.0218 -0.0032 0.0184  206 LEU   D CG  
5651 C  CD1 . LEU   D 113 ? 0.3967 0.3148 0.5041 -0.0233 -0.0009 0.0176  206 LEU   D CD1 
5652 C  CD2 . LEU   D 113 ? 0.3971 0.2961 0.4831 -0.0213 0.0020  0.0246  206 LEU   D CD2 
5653 N  N   . ASP   D 114 ? 0.3823 0.2947 0.4907 -0.0244 -0.0186 0.0045  207 ASP   D N   
5654 C  CA  . ASP   D 114 ? 0.3984 0.3088 0.5164 -0.0324 -0.0192 0.0010  207 ASP   D CA  
5655 C  C   . ASP   D 114 ? 0.4049 0.3156 0.5319 -0.0377 -0.0118 0.0064  207 ASP   D C   
5656 O  O   . ASP   D 114 ? 0.4160 0.3410 0.5531 -0.0386 -0.0095 0.0073  207 ASP   D O   
5657 C  CB  . ASP   D 114 ? 0.3915 0.3164 0.5200 -0.0350 -0.0255 -0.0062 207 ASP   D CB  
5658 C  CG  . ASP   D 114 ? 0.3949 0.3211 0.5131 -0.0302 -0.0329 -0.0106 207 ASP   D CG  
5659 O  OD1 . ASP   D 114 ? 0.4019 0.3164 0.5057 -0.0257 -0.0326 -0.0084 207 ASP   D OD1 
5660 O  OD2 . ASP   D 114 ? 0.3917 0.3326 0.5166 -0.0312 -0.0388 -0.0161 207 ASP   D OD2 
5661 N  N   . ASP   D 115 ? 0.4178 0.3143 0.5407 -0.0397 -0.0077 0.0111  208 ASP   D N   
5662 C  CA  . ASP   D 115 ? 0.4326 0.3281 0.5614 -0.0440 0.0002  0.0192  208 ASP   D CA  
5663 C  C   . ASP   D 115 ? 0.4452 0.3471 0.5935 -0.0534 0.0015  0.0163  208 ASP   D C   
5664 O  O   . ASP   D 115 ? 0.4501 0.3451 0.6048 -0.0581 -0.0021 0.0095  208 ASP   D O   
5665 C  CB  . ASP   D 115 ? 0.4409 0.3196 0.5613 -0.0430 0.0032  0.0260  208 ASP   D CB  
5666 C  CG  . ASP   D 115 ? 0.4477 0.3263 0.5707 -0.0459 0.0114  0.0370  208 ASP   D CG  
5667 O  OD1 . ASP   D 115 ? 0.4559 0.3346 0.5936 -0.0538 0.0155  0.0390  208 ASP   D OD1 
5668 O  OD2 . ASP   D 115 ? 0.4460 0.3255 0.5566 -0.0407 0.0140  0.0435  208 ASP   D OD2 
5669 N  N   . ARG   D 116 ? 0.4536 0.3695 0.6118 -0.0565 0.0068  0.0199  209 ARG   D N   
5670 C  CA  . ARG   D 116 ? 0.4732 0.3998 0.6527 -0.0662 0.0083  0.0164  209 ARG   D CA  
5671 C  C   . ARG   D 116 ? 0.4877 0.3978 0.6762 -0.0754 0.0124  0.0190  209 ARG   D C   
5672 O  O   . ARG   D 116 ? 0.5001 0.4140 0.7061 -0.0845 0.0108  0.0116  209 ARG   D O   
5673 C  CB  . ARG   D 116 ? 0.4761 0.4216 0.6642 -0.0672 0.0150  0.0211  209 ARG   D CB  
5674 C  CG  . ARG   D 116 ? 0.4876 0.4437 0.6994 -0.0790 0.0187  0.0195  209 ARG   D CG  
5675 C  CD  . ARG   D 116 ? 0.4909 0.4598 0.7159 -0.0819 0.0096  0.0067  209 ARG   D CD  
5676 N  NE  . ARG   D 116 ? 0.4856 0.4798 0.7178 -0.0771 0.0083  0.0042  209 ARG   D NE  
5677 C  CZ  . ARG   D 116 ? 0.4884 0.5008 0.7365 -0.0818 0.0155  0.0072  209 ARG   D CZ  
5678 N  NH1 . ARG   D 116 ? 0.5016 0.5091 0.7596 -0.0922 0.0249  0.0137  209 ARG   D NH1 
5679 N  NH2 . ARG   D 116 ? 0.4782 0.5140 0.7335 -0.0756 0.0137  0.0041  209 ARG   D NH2 
5680 N  N   . ASN   D 117 ? 0.4943 0.3869 0.6723 -0.0732 0.0172  0.0288  210 ASN   D N   
5681 C  CA  . ASN   D 117 ? 0.5132 0.3885 0.7010 -0.0809 0.0232  0.0349  210 ASN   D CA  
5682 C  C   . ASN   D 117 ? 0.5173 0.3708 0.6985 -0.0778 0.0192  0.0316  210 ASN   D C   
5683 O  O   . ASN   D 117 ? 0.5324 0.3728 0.7275 -0.0855 0.0207  0.0281  210 ASN   D O   
5684 C  CB  . ASN   D 117 ? 0.5166 0.3911 0.7007 -0.0809 0.0332  0.0512  210 ASN   D CB  
5685 C  CG  . ASN   D 117 ? 0.5137 0.4113 0.7067 -0.0847 0.0382  0.0528  210 ASN   D CG  
5686 O  OD1 . ASN   D 117 ? 0.5085 0.4185 0.6899 -0.0781 0.0406  0.0573  210 ASN   D OD1 
5687 N  ND2 . ASN   D 117 ? 0.5162 0.4220 0.7310 -0.0950 0.0390  0.0465  210 ASN   D ND2 
5688 N  N   . THR   D 118 ? 0.5063 0.3559 0.6687 -0.0676 0.0150  0.0321  211 THR   D N   
5689 C  CA  . THR   D 118 ? 0.5113 0.3429 0.6675 -0.0634 0.0116  0.0286  211 THR   D CA  
5690 C  C   . THR   D 118 ? 0.5022 0.3384 0.6576 -0.0630 0.0032  0.0130  211 THR   D C   
5691 O  O   . THR   D 118 ? 0.4994 0.3221 0.6539 -0.0618 0.0010  0.0068  211 THR   D O   
5692 C  CB  . THR   D 118 ? 0.5096 0.3367 0.6474 -0.0532 0.0116  0.0370  211 THR   D CB  
5693 O  OG1 . THR   D 118 ? 0.4924 0.3340 0.6183 -0.0475 0.0070  0.0327  211 THR   D OG1 
5694 C  CG2 . THR   D 118 ? 0.5230 0.3480 0.6584 -0.0524 0.0191  0.0530  211 THR   D CG2 
5695 N  N   . PHE   D 119 ? 0.4763 0.3315 0.6307 -0.0624 -0.0010 0.0075  212 PHE   D N   
5696 C  CA  . PHE   D 119 ? 0.4624 0.3260 0.6135 -0.0607 -0.0094 -0.0051 212 PHE   D CA  
5697 C  C   . PHE   D 119 ? 0.4448 0.3020 0.5774 -0.0514 -0.0126 -0.0051 212 PHE   D C   
5698 O  O   . PHE   D 119 ? 0.4355 0.2976 0.5627 -0.0493 -0.0187 -0.0140 212 PHE   D O   
5699 C  CB  . PHE   D 119 ? 0.4767 0.3358 0.6412 -0.0690 -0.0118 -0.0172 212 PHE   D CB  
5700 C  CG  . PHE   D 119 ? 0.4967 0.3610 0.6824 -0.0801 -0.0081 -0.0180 212 PHE   D CG  
5701 C  CD1 . PHE   D 119 ? 0.4926 0.3798 0.6870 -0.0831 -0.0107 -0.0210 212 PHE   D CD1 
5702 C  CD2 . PHE   D 119 ? 0.5175 0.3640 0.7160 -0.0875 -0.0016 -0.0154 212 PHE   D CD2 
5703 C  CE1 . PHE   D 119 ? 0.5034 0.3980 0.7193 -0.0942 -0.0068 -0.0222 212 PHE   D CE1 
5704 C  CE2 . PHE   D 119 ? 0.5289 0.3802 0.7484 -0.0991 0.0027  -0.0157 212 PHE   D CE2 
5705 C  CZ  . PHE   D 119 ? 0.5234 0.3997 0.7518 -0.1028 0.0001  -0.0195 212 PHE   D CZ  
5706 N  N   . ARG   D 120 ? 0.4382 0.2870 0.5615 -0.0462 -0.0086 0.0047  213 ARG   D N   
5707 C  CA  . ARG   D 120 ? 0.4286 0.2731 0.5363 -0.0381 -0.0110 0.0051  213 ARG   D CA  
5708 C  C   . ARG   D 120 ? 0.4086 0.2664 0.5073 -0.0334 -0.0140 0.0048  213 ARG   D C   
5709 O  O   . ARG   D 120 ? 0.3981 0.2661 0.5006 -0.0343 -0.0123 0.0081  213 ARG   D O   
5710 C  CB  . ARG   D 120 ? 0.4394 0.2734 0.5420 -0.0343 -0.0064 0.0152  213 ARG   D CB  
5711 C  CG  . ARG   D 120 ? 0.4581 0.2760 0.5702 -0.0371 -0.0034 0.0162  213 ARG   D CG  
5712 C  CD  . ARG   D 120 ? 0.4669 0.2754 0.5727 -0.0309 -0.0006 0.0261  213 ARG   D CD  
5713 N  NE  . ARG   D 120 ? 0.4932 0.2842 0.6095 -0.0322 0.0023  0.0272  213 ARG   D NE  
5714 C  CZ  . ARG   D 120 ? 0.4956 0.2765 0.6136 -0.0295 0.0005  0.0193  213 ARG   D CZ  
5715 N  NH1 . ARG   D 120 ? 0.4911 0.2788 0.6001 -0.0260 -0.0041 0.0098  213 ARG   D NH1 
5716 N  NH2 . ARG   D 120 ? 0.5166 0.2799 0.6461 -0.0304 0.0041  0.0208  213 ARG   D NH2 
5717 N  N   . HIS   D 121 ? 0.4066 0.2638 0.4946 -0.0287 -0.0179 0.0008  214 HIS   D N   
5718 C  CA  . HIS   D 121 ? 0.3942 0.2600 0.4733 -0.0238 -0.0205 0.0010  214 HIS   D CA  
5719 C  C   . HIS   D 121 ? 0.3881 0.2496 0.4573 -0.0191 -0.0178 0.0068  214 HIS   D C   
5720 O  O   . HIS   D 121 ? 0.4069 0.2601 0.4725 -0.0179 -0.0166 0.0082  214 HIS   D O   
5721 C  CB  . HIS   D 121 ? 0.3946 0.2626 0.4679 -0.0223 -0.0256 -0.0057 214 HIS   D CB  
5722 C  CG  . HIS   D 121 ? 0.3964 0.2716 0.4780 -0.0268 -0.0295 -0.0134 214 HIS   D CG  
5723 N  ND1 . HIS   D 121 ? 0.3978 0.2751 0.4743 -0.0267 -0.0338 -0.0213 214 HIS   D ND1 
5724 C  CD2 . HIS   D 121 ? 0.4042 0.2872 0.4991 -0.0321 -0.0300 -0.0154 214 HIS   D CD2 
5725 C  CE1 . HIS   D 121 ? 0.4026 0.2893 0.4883 -0.0316 -0.0375 -0.0284 214 HIS   D CE1 
5726 N  NE2 . HIS   D 121 ? 0.4034 0.2936 0.5014 -0.0352 -0.0353 -0.0251 214 HIS   D NE2 
5727 N  N   . SER   D 122 ? 0.3821 0.2498 0.4476 -0.0161 -0.0173 0.0091  215 SER   D N   
5728 C  CA  . SER   D 122 ? 0.3667 0.2317 0.4229 -0.0124 -0.0156 0.0118  215 SER   D CA  
5729 C  C   . SER   D 122 ? 0.3626 0.2321 0.4159 -0.0090 -0.0164 0.0109  215 SER   D C   
5730 O  O   . SER   D 122 ? 0.3552 0.2316 0.4147 -0.0087 -0.0176 0.0100  215 SER   D O   
5731 C  CB  . SER   D 122 ? 0.3647 0.2297 0.4210 -0.0128 -0.0115 0.0169  215 SER   D CB  
5732 O  OG  . SER   D 122 ? 0.3556 0.2283 0.4175 -0.0142 -0.0088 0.0187  215 SER   D OG  
5733 N  N   . VAL   D 123 ? 0.3623 0.2282 0.4081 -0.0067 -0.0157 0.0110  216 VAL   D N   
5734 C  CA  . VAL   D 123 ? 0.3709 0.2369 0.4144 -0.0035 -0.0154 0.0103  216 VAL   D CA  
5735 C  C   . VAL   D 123 ? 0.3744 0.2402 0.4148 -0.0032 -0.0119 0.0099  216 VAL   D C   
5736 O  O   . VAL   D 123 ? 0.3837 0.2482 0.4200 -0.0045 -0.0114 0.0102  216 VAL   D O   
5737 C  CB  . VAL   D 123 ? 0.3759 0.2373 0.4141 -0.0023 -0.0176 0.0101  216 VAL   D CB  
5738 C  CG1 . VAL   D 123 ? 0.3805 0.2376 0.4133 -0.0039 -0.0171 0.0094  216 VAL   D CG1 
5739 C  CG2 . VAL   D 123 ? 0.3823 0.2407 0.4195 0.0009  -0.0166 0.0110  216 VAL   D CG2 
5740 N  N   A VAL   D 124 ? 0.3775 0.2461 0.4204 -0.0010 -0.0096 0.0084  217 VAL   D N   
5741 N  N   B VAL   D 124 ? 0.3786 0.2470 0.4214 -0.0010 -0.0097 0.0084  217 VAL   D N   
5742 C  CA  A VAL   D 124 ? 0.3794 0.2504 0.4192 -0.0008 -0.0061 0.0056  217 VAL   D CA  
5743 C  CA  B VAL   D 124 ? 0.3810 0.2519 0.4212 -0.0007 -0.0061 0.0056  217 VAL   D CA  
5744 C  C   A VAL   D 124 ? 0.3845 0.2502 0.4250 0.0016  -0.0047 0.0016  217 VAL   D C   
5745 C  C   B VAL   D 124 ? 0.3846 0.2496 0.4249 0.0016  -0.0049 0.0017  217 VAL   D C   
5746 O  O   A VAL   D 124 ? 0.3804 0.2443 0.4261 0.0049  -0.0053 0.0026  217 VAL   D O   
5747 O  O   B VAL   D 124 ? 0.3775 0.2399 0.4226 0.0048  -0.0058 0.0029  217 VAL   D O   
5748 C  CB  A VAL   D 124 ? 0.3792 0.2597 0.4221 -0.0011 -0.0030 0.0067  217 VAL   D CB  
5749 C  CB  B VAL   D 124 ? 0.3830 0.2634 0.4274 -0.0004 -0.0029 0.0061  217 VAL   D CB  
5750 C  CG1 A VAL   D 124 ? 0.3794 0.2649 0.4314 0.0010  -0.0021 0.0065  217 VAL   D CG1 
5751 C  CG1 B VAL   D 124 ? 0.3867 0.2724 0.4256 -0.0003 0.0007  0.0029  217 VAL   D CG1 
5752 C  CG2 A VAL   D 124 ? 0.3835 0.2692 0.4208 -0.0009 0.0004  0.0033  217 VAL   D CG2 
5753 C  CG2 B VAL   D 124 ? 0.3827 0.2665 0.4303 -0.0033 -0.0034 0.0111  217 VAL   D CG2 
5754 N  N   . VAL   D 125 ? 0.3904 0.2537 0.4265 0.0002  -0.0033 -0.0026 218 VAL   D N   
5755 C  CA  . VAL   D 125 ? 0.4046 0.2610 0.4426 0.0015  -0.0007 -0.0082 218 VAL   D CA  
5756 C  C   . VAL   D 125 ? 0.4139 0.2773 0.4492 0.0003  0.0021  -0.0155 218 VAL   D C   
5757 O  O   . VAL   D 125 ? 0.4170 0.2892 0.4466 -0.0019 0.0013  -0.0151 218 VAL   D O   
5758 C  CB  . VAL   D 125 ? 0.4068 0.2532 0.4435 -0.0007 -0.0016 -0.0078 218 VAL   D CB  
5759 C  CG1 . VAL   D 125 ? 0.4057 0.2466 0.4437 0.0014  -0.0039 -0.0007 218 VAL   D CG1 
5760 C  CG2 . VAL   D 125 ? 0.4103 0.2612 0.4420 -0.0051 -0.0032 -0.0087 218 VAL   D CG2 
5761 N  N   . PRO   D 126 ? 0.4287 0.2887 0.4677 0.0025  0.0057  -0.0226 219 PRO   D N   
5762 C  CA  . PRO   D 126 ? 0.4460 0.3127 0.4813 0.0008  0.0084  -0.0324 219 PRO   D CA  
5763 C  C   . PRO   D 126 ? 0.4537 0.3190 0.4850 -0.0045 0.0064  -0.0363 219 PRO   D C   
5764 O  O   . PRO   D 126 ? 0.4402 0.2944 0.4748 -0.0064 0.0053  -0.0343 219 PRO   D O   
5765 C  CB  . PRO   D 126 ? 0.4581 0.3176 0.5005 0.0045  0.0130  -0.0404 219 PRO   D CB  
5766 C  CG  . PRO   D 126 ? 0.4543 0.3027 0.5048 0.0090  0.0122  -0.0327 219 PRO   D CG  
5767 C  CD  . PRO   D 126 ? 0.4421 0.2925 0.4893 0.0073  0.0073  -0.0220 219 PRO   D CD  
5768 N  N   . TYR   D 127 ? 0.4669 0.3456 0.4912 -0.0068 0.0057  -0.0410 220 TYR   D N   
5769 C  CA  . TYR   D 127 ? 0.4822 0.3650 0.5038 -0.0119 0.0036  -0.0476 220 TYR   D CA  
5770 C  C   . TYR   D 127 ? 0.5048 0.3794 0.5320 -0.0142 0.0070  -0.0607 220 TYR   D C   
5771 O  O   . TYR   D 127 ? 0.5127 0.3891 0.5402 -0.0116 0.0108  -0.0683 220 TYR   D O   
5772 C  CB  . TYR   D 127 ? 0.4805 0.3831 0.4925 -0.0124 0.0014  -0.0485 220 TYR   D CB  
5773 C  CG  . TYR   D 127 ? 0.4879 0.3987 0.4984 -0.0174 -0.0013 -0.0570 220 TYR   D CG  
5774 C  CD1 . TYR   D 127 ? 0.4836 0.3962 0.4955 -0.0195 -0.0055 -0.0516 220 TYR   D CD1 
5775 C  CD2 . TYR   D 127 ? 0.5008 0.4177 0.5102 -0.0202 0.0002  -0.0720 220 TYR   D CD2 
5776 C  CE1 . TYR   D 127 ? 0.4850 0.4074 0.4978 -0.0243 -0.0083 -0.0597 220 TYR   D CE1 
5777 C  CE2 . TYR   D 127 ? 0.5033 0.4296 0.5132 -0.0258 -0.0029 -0.0813 220 TYR   D CE2 
5778 C  CZ  . TYR   D 127 ? 0.4931 0.4227 0.5052 -0.0280 -0.0074 -0.0747 220 TYR   D CZ  
5779 O  OH  . TYR   D 127 ? 0.4814 0.4228 0.4961 -0.0337 -0.0107 -0.0839 220 TYR   D OH  
5780 N  N   . GLU   D 128 ? 0.5247 0.3894 0.5574 -0.0190 0.0066  -0.0633 221 GLU   D N   
5781 C  CA  . GLU   D 128 ? 0.5693 0.4256 0.6088 -0.0235 0.0099  -0.0770 221 GLU   D CA  
5782 C  C   . GLU   D 128 ? 0.5749 0.4432 0.6131 -0.0309 0.0066  -0.0841 221 GLU   D C   
5783 O  O   . GLU   D 128 ? 0.5696 0.4430 0.6068 -0.0327 0.0030  -0.0760 221 GLU   D O   
5784 C  CB  . GLU   D 128 ? 0.5886 0.4215 0.6382 -0.0233 0.0133  -0.0730 221 GLU   D CB  
5785 C  CG  . GLU   D 128 ? 0.6031 0.4266 0.6555 -0.0150 0.0161  -0.0674 221 GLU   D CG  
5786 C  CD  . GLU   D 128 ? 0.6223 0.4246 0.6829 -0.0126 0.0184  -0.0593 221 GLU   D CD  
5787 O  OE1 . GLU   D 128 ? 0.6538 0.4456 0.7186 -0.0183 0.0195  -0.0584 221 GLU   D OE1 
5788 O  OE2 . GLU   D 128 ? 0.6445 0.4424 0.7076 -0.0049 0.0194  -0.0532 221 GLU   D OE2 
5789 N  N   . PRO   D 129 ? 0.5964 0.4715 0.6353 -0.0353 0.0075  -0.1005 222 PRO   D N   
5790 C  CA  . PRO   D 129 ? 0.6035 0.4934 0.6429 -0.0429 0.0036  -0.1089 222 PRO   D CA  
5791 C  C   . PRO   D 129 ? 0.6113 0.4866 0.6629 -0.0498 0.0052  -0.1081 222 PRO   D C   
5792 O  O   . PRO   D 129 ? 0.6282 0.4806 0.6871 -0.0489 0.0100  -0.1034 222 PRO   D O   
5793 C  CB  . PRO   D 129 ? 0.6203 0.5192 0.6582 -0.0459 0.0050  -0.1286 222 PRO   D CB  
5794 C  CG  . PRO   D 129 ? 0.6279 0.5073 0.6704 -0.0412 0.0118  -0.1320 222 PRO   D CG  
5795 C  CD  . PRO   D 129 ? 0.6101 0.4808 0.6504 -0.0331 0.0123  -0.1129 222 PRO   D CD  
5796 N  N   . PRO   D 130 ? 0.6214 0.5105 0.6762 -0.0567 0.0016  -0.1119 223 PRO   D N   
5797 C  CA  . PRO   D 130 ? 0.6258 0.5028 0.6932 -0.0645 0.0042  -0.1113 223 PRO   D CA  
5798 C  C   . PRO   D 130 ? 0.6520 0.5080 0.7306 -0.0702 0.0108  -0.1234 223 PRO   D C   
5799 O  O   . PRO   D 130 ? 0.6554 0.5138 0.7325 -0.0700 0.0116  -0.1372 223 PRO   D O   
5800 C  CB  . PRO   D 130 ? 0.6251 0.5272 0.6946 -0.0709 -0.0011 -0.1177 223 PRO   D CB  
5801 C  CG  . PRO   D 130 ? 0.6111 0.5367 0.6666 -0.0634 -0.0076 -0.1141 223 PRO   D CG  
5802 C  CD  . PRO   D 130 ? 0.6155 0.5338 0.6625 -0.0571 -0.0050 -0.1161 223 PRO   D CD  
5803 N  N   . GLU   D 131 ? 0.6736 0.5088 0.7630 -0.0745 0.0159  -0.1174 224 GLU   D N   
5804 C  CA  . GLU   D 131 ? 0.6984 0.5098 0.8015 -0.0807 0.0231  -0.1267 224 GLU   D CA  
5805 C  C   . GLU   D 131 ? 0.7120 0.5357 0.8248 -0.0935 0.0222  -0.1461 224 GLU   D C   
5806 O  O   . GLU   D 131 ? 0.7027 0.5520 0.8130 -0.0972 0.0163  -0.1473 224 GLU   D O   
5807 C  CB  . GLU   D 131 ? 0.7068 0.4950 0.8170 -0.0815 0.0286  -0.1109 224 GLU   D CB  
5808 C  CG  . GLU   D 131 ? 0.7348 0.4977 0.8615 -0.0900 0.0366  -0.1174 224 GLU   D CG  
5809 C  CD  . GLU   D 131 ? 0.7416 0.4937 0.8763 -0.0965 0.0412  -0.1043 224 GLU   D CD  
5810 O  OE1 . GLU   D 131 ? 0.7537 0.5080 0.9013 -0.1096 0.0438  -0.1134 224 GLU   D OE1 
5811 O  OE2 . GLU   D 131 ? 0.7408 0.4841 0.8689 -0.0889 0.0422  -0.0854 224 GLU   D OE2 
5812 N  N   . VAL   D 132 ? 0.7360 0.5423 0.8608 -0.0998 0.0279  -0.1611 225 VAL   D N   
5813 C  CA  . VAL   D 132 ? 0.7617 0.5744 0.9006 -0.1147 0.0286  -0.1808 225 VAL   D CA  
5814 C  C   . VAL   D 132 ? 0.7633 0.5793 0.9117 -0.1234 0.0293  -0.1710 225 VAL   D C   
5815 O  O   . VAL   D 132 ? 0.7786 0.5697 0.9333 -0.1235 0.0360  -0.1563 225 VAL   D O   
5816 C  CB  . VAL   D 132 ? 0.7856 0.5696 0.9390 -0.1200 0.0369  -0.1954 225 VAL   D CB  
5817 C  CG1 . VAL   D 132 ? 0.8040 0.5939 0.9741 -0.1369 0.0379  -0.2163 225 VAL   D CG1 
5818 C  CG2 . VAL   D 132 ? 0.7873 0.5689 0.9323 -0.1106 0.0372  -0.2062 225 VAL   D CG2 
5819 N  N   . GLY   D 133 ? 0.7582 0.6055 0.9073 -0.1298 0.0227  -0.1781 226 GLY   D N   
5820 C  CA  . GLY   D 133 ? 0.7600 0.6179 0.9182 -0.1374 0.0227  -0.1699 226 GLY   D CA  
5821 C  C   . GLY   D 133 ? 0.7372 0.6201 0.8820 -0.1282 0.0153  -0.1560 226 GLY   D C   
5822 O  O   . GLY   D 133 ? 0.7387 0.6473 0.8895 -0.1338 0.0111  -0.1589 226 GLY   D O   
5823 N  N   . SER   D 134 ? 0.7337 0.6094 0.8627 -0.1145 0.0140  -0.1418 227 SER   D N   
5824 C  CA  . SER   D 134 ? 0.7066 0.5965 0.8238 -0.1048 0.0092  -0.1254 227 SER   D CA  
5825 C  C   . SER   D 134 ? 0.6908 0.6083 0.7959 -0.0983 0.0002  -0.1304 227 SER   D C   
5826 O  O   . SER   D 134 ? 0.6933 0.6141 0.7941 -0.0981 -0.0012 -0.1433 227 SER   D O   
5827 C  CB  . SER   D 134 ? 0.7180 0.5849 0.8267 -0.0951 0.0129  -0.1085 227 SER   D CB  
5828 O  OG  . SER   D 134 ? 0.7343 0.5766 0.8530 -0.1004 0.0211  -0.1024 227 SER   D OG  
5829 N  N   . ASP   D 135 ? 0.6604 0.5978 0.7603 -0.0929 -0.0051 -0.1206 228 ASP   D N   
5830 C  CA  . ASP   D 135 ? 0.6441 0.6112 0.7346 -0.0873 -0.0139 -0.1235 228 ASP   D CA  
5831 C  C   . ASP   D 135 ? 0.6230 0.5873 0.6984 -0.0740 -0.0160 -0.1075 228 ASP   D C   
5832 O  O   . ASP   D 135 ? 0.6258 0.6107 0.6916 -0.0678 -0.0223 -0.1063 228 ASP   D O   
5833 C  CB  . ASP   D 135 ? 0.6504 0.6452 0.7503 -0.0917 -0.0189 -0.1261 228 ASP   D CB  
5834 C  CG  . ASP   D 135 ? 0.6703 0.6721 0.7871 -0.1064 -0.0175 -0.1436 228 ASP   D CG  
5835 O  OD1 . ASP   D 135 ? 0.6917 0.6927 0.8083 -0.1115 -0.0176 -0.1594 228 ASP   D OD1 
5836 O  OD2 . ASP   D 135 ? 0.6718 0.6797 0.8029 -0.1132 -0.0155 -0.1422 228 ASP   D OD2 
5837 N  N   . CYS   D 136 ? 0.5913 0.5316 0.6647 -0.0700 -0.0108 -0.0953 229 CYS   D N   
5838 C  CA  . CYS   D 136 ? 0.5595 0.4954 0.6214 -0.0589 -0.0122 -0.0804 229 CYS   D CA  
5839 C  C   . CYS   D 136 ? 0.5510 0.4598 0.6109 -0.0564 -0.0064 -0.0747 229 CYS   D C   
5840 O  O   . CYS   D 136 ? 0.5582 0.4508 0.6264 -0.0626 -0.0011 -0.0793 229 CYS   D O   
5841 C  CB  . CYS   D 136 ? 0.5436 0.4867 0.6078 -0.0558 -0.0138 -0.0695 229 CYS   D CB  
5842 S  SG  . CYS   D 136 ? 0.5414 0.4683 0.6166 -0.0624 -0.0067 -0.0652 229 CYS   D SG  
5843 N  N   . THR   D 137 ? 0.5300 0.4342 0.5803 -0.0476 -0.0072 -0.0648 230 THR   D N   
5844 C  CA  . THR   D 137 ? 0.5182 0.4004 0.5669 -0.0439 -0.0029 -0.0579 230 THR   D CA  
5845 C  C   . THR   D 137 ? 0.4978 0.3748 0.5455 -0.0405 -0.0028 -0.0449 230 THR   D C   
5846 O  O   . THR   D 137 ? 0.4973 0.3859 0.5405 -0.0363 -0.0066 -0.0395 230 THR   D O   
5847 C  CB  . THR   D 137 ? 0.5245 0.4069 0.5652 -0.0377 -0.0034 -0.0581 230 THR   D CB  
5848 O  OG1 . THR   D 137 ? 0.5356 0.4243 0.5772 -0.0414 -0.0030 -0.0723 230 THR   D OG1 
5849 C  CG2 . THR   D 137 ? 0.5264 0.3899 0.5675 -0.0332 0.0001  -0.0515 230 THR   D CG2 
5850 N  N   . THR   D 138 ? 0.4878 0.3482 0.5393 -0.0422 0.0015  -0.0402 231 THR   D N   
5851 C  CA  . THR   D 138 ? 0.4817 0.3376 0.5309 -0.0393 0.0022  -0.0290 231 THR   D CA  
5852 C  C   . THR   D 138 ? 0.4765 0.3210 0.5200 -0.0325 0.0023  -0.0218 231 THR   D C   
5853 O  O   . THR   D 138 ? 0.4751 0.3071 0.5207 -0.0320 0.0050  -0.0232 231 THR   D O   
5854 C  CB  . THR   D 138 ? 0.4865 0.3354 0.5424 -0.0457 0.0070  -0.0272 231 THR   D CB  
5855 O  OG1 . THR   D 138 ? 0.4733 0.3366 0.5364 -0.0524 0.0064  -0.0347 231 THR   D OG1 
5856 C  CG2 . THR   D 138 ? 0.4860 0.3330 0.5376 -0.0427 0.0081  -0.0166 231 THR   D CG2 
5857 N  N   . ILE   D 139 ? 0.4640 0.3135 0.5019 -0.0275 -0.0005 -0.0154 232 ILE   D N   
5858 C  CA  . ILE   D 139 ? 0.4673 0.3093 0.5009 -0.0219 -0.0011 -0.0081 232 ILE   D CA  
5859 C  C   . ILE   D 139 ? 0.4586 0.2987 0.4900 -0.0218 -0.0003 -0.0016 232 ILE   D C   
5860 O  O   . ILE   D 139 ? 0.4578 0.3068 0.4894 -0.0233 -0.0009 -0.0022 232 ILE   D O   
5861 C  CB  . ILE   D 139 ? 0.4560 0.3054 0.4859 -0.0174 -0.0046 -0.0072 232 ILE   D CB  
5862 C  CG1 . ILE   D 139 ? 0.4669 0.3200 0.4973 -0.0172 -0.0045 -0.0132 232 ILE   D CG1 
5863 C  CG2 . ILE   D 139 ? 0.4600 0.3047 0.4875 -0.0130 -0.0057 -0.0010 232 ILE   D CG2 
5864 C  CD1 . ILE   D 139 ? 0.4627 0.3250 0.4893 -0.0139 -0.0070 -0.0112 232 ILE   D CD1 
5865 N  N   . HIS   D 140 ? 0.4699 0.3005 0.4991 -0.0193 0.0009  0.0043  233 HIS   D N   
5866 C  CA  . HIS   D 140 ? 0.4716 0.3017 0.4960 -0.0185 0.0016  0.0111  233 HIS   D CA  
5867 C  C   . HIS   D 140 ? 0.4619 0.2963 0.4812 -0.0133 -0.0025 0.0133  233 HIS   D C   
5868 O  O   . HIS   D 140 ? 0.4609 0.2913 0.4794 -0.0095 -0.0040 0.0165  233 HIS   D O   
5869 C  CB  . HIS   D 140 ? 0.4874 0.3056 0.5122 -0.0192 0.0057  0.0172  233 HIS   D CB  
5870 C  CG  . HIS   D 140 ? 0.4985 0.3126 0.5297 -0.0263 0.0108  0.0150  233 HIS   D CG  
5871 N  ND1 . HIS   D 140 ? 0.5156 0.3154 0.5505 -0.0283 0.0157  0.0195  233 HIS   D ND1 
5872 C  CD2 . HIS   D 140 ? 0.4960 0.3187 0.5319 -0.0321 0.0119  0.0087  233 HIS   D CD2 
5873 C  CE1 . HIS   D 140 ? 0.5229 0.3221 0.5650 -0.0363 0.0200  0.0154  233 HIS   D CE1 
5874 N  NE2 . HIS   D 140 ? 0.5041 0.3187 0.5470 -0.0387 0.0174  0.0084  233 HIS   D NE2 
5875 N  N   . TYR   D 141 ? 0.4600 0.3029 0.4778 -0.0130 -0.0044 0.0111  234 TYR   D N   
5876 C  CA  . TYR   D 141 ? 0.4551 0.3015 0.4694 -0.0095 -0.0079 0.0116  234 TYR   D CA  
5877 C  C   . TYR   D 141 ? 0.4690 0.3170 0.4766 -0.0088 -0.0072 0.0149  234 TYR   D C   
5878 O  O   . TYR   D 141 ? 0.4669 0.3159 0.4728 -0.0113 -0.0034 0.0162  234 TYR   D O   
5879 C  CB  . TYR   D 141 ? 0.4369 0.2891 0.4539 -0.0093 -0.0095 0.0076  234 TYR   D CB  
5880 C  CG  . TYR   D 141 ? 0.4287 0.2814 0.4496 -0.0091 -0.0106 0.0061  234 TYR   D CG  
5881 C  CD1 . TYR   D 141 ? 0.4267 0.2778 0.4484 -0.0073 -0.0123 0.0071  234 TYR   D CD1 
5882 C  CD2 . TYR   D 141 ? 0.4198 0.2769 0.4434 -0.0108 -0.0098 0.0035  234 TYR   D CD2 
5883 C  CE1 . TYR   D 141 ? 0.4278 0.2810 0.4519 -0.0072 -0.0122 0.0060  234 TYR   D CE1 
5884 C  CE2 . TYR   D 141 ? 0.4221 0.2821 0.4470 -0.0104 -0.0108 0.0023  234 TYR   D CE2 
5885 C  CZ  . TYR   D 141 ? 0.4239 0.2815 0.4484 -0.0086 -0.0115 0.0038  234 TYR   D CZ  
5886 O  OH  . TYR   D 141 ? 0.4286 0.2905 0.4533 -0.0081 -0.0115 0.0029  234 TYR   D OH  
5887 N  N   . ASN   D 142 ? 0.4804 0.3304 0.4843 -0.0058 -0.0107 0.0159  235 ASN   D N   
5888 C  CA  . ASN   D 142 ? 0.4815 0.3371 0.4773 -0.0046 -0.0115 0.0167  235 ASN   D CA  
5889 C  C   . ASN   D 142 ? 0.4725 0.3332 0.4693 -0.0037 -0.0151 0.0100  235 ASN   D C   
5890 O  O   . ASN   D 142 ? 0.4694 0.3293 0.4713 -0.0031 -0.0183 0.0087  235 ASN   D O   
5891 C  CB  . ASN   D 142 ? 0.4927 0.3484 0.4827 -0.0015 -0.0134 0.0234  235 ASN   D CB  
5892 C  CG  . ASN   D 142 ? 0.5018 0.3490 0.4919 -0.0017 -0.0094 0.0314  235 ASN   D CG  
5893 O  OD1 . ASN   D 142 ? 0.5160 0.3608 0.5045 0.0020  -0.0110 0.0379  235 ASN   D OD1 
5894 N  ND2 . ASN   D 142 ? 0.4928 0.3357 0.4862 -0.0059 -0.0043 0.0308  235 ASN   D ND2 
5895 N  N   . TYR   D 143 ? 0.4616 0.3272 0.4549 -0.0040 -0.0139 0.0055  236 TYR   D N   
5896 C  CA  . TYR   D 143 ? 0.4622 0.3310 0.4567 -0.0035 -0.0167 -0.0023 236 TYR   D CA  
5897 C  C   . TYR   D 143 ? 0.4806 0.3575 0.4654 -0.0024 -0.0192 -0.0037 236 TYR   D C   
5898 O  O   . TYR   D 143 ? 0.4977 0.3794 0.4734 -0.0019 -0.0163 -0.0011 236 TYR   D O   
5899 C  CB  . TYR   D 143 ? 0.4514 0.3200 0.4501 -0.0034 -0.0137 -0.0076 236 TYR   D CB  
5900 C  CG  . TYR   D 143 ? 0.4365 0.3002 0.4442 -0.0037 -0.0128 -0.0058 236 TYR   D CG  
5901 C  CD1 . TYR   D 143 ? 0.4325 0.2963 0.4411 -0.0049 -0.0101 -0.0015 236 TYR   D CD1 
5902 C  CD2 . TYR   D 143 ? 0.4322 0.2916 0.4472 -0.0031 -0.0147 -0.0081 236 TYR   D CD2 
5903 C  CE1 . TYR   D 143 ? 0.4228 0.2854 0.4384 -0.0050 -0.0101 -0.0008 236 TYR   D CE1 
5904 C  CE2 . TYR   D 143 ? 0.4238 0.2808 0.4449 -0.0026 -0.0142 -0.0051 236 TYR   D CE2 
5905 C  CZ  . TYR   D 143 ? 0.4193 0.2791 0.4401 -0.0033 -0.0123 -0.0019 236 TYR   D CZ  
5906 O  OH  . TYR   D 143 ? 0.4117 0.2721 0.4373 -0.0027 -0.0126 0.0000  236 TYR   D OH  
5907 N  N   . MET   D 144 ? 0.4847 0.3647 0.4714 -0.0023 -0.0243 -0.0074 237 MET   D N   
5908 C  CA  . MET   D 144 ? 0.4947 0.3853 0.4727 -0.0009 -0.0287 -0.0074 237 MET   D CA  
5909 C  C   . MET   D 144 ? 0.5056 0.4043 0.4800 -0.0020 -0.0308 -0.0193 237 MET   D C   
5910 O  O   . MET   D 144 ? 0.5095 0.4200 0.4771 -0.0012 -0.0358 -0.0218 237 MET   D O   
5911 C  CB  . MET   D 144 ? 0.4924 0.3844 0.4768 -0.0001 -0.0337 -0.0041 237 MET   D CB  
5912 C  CG  . MET   D 144 ? 0.4851 0.3691 0.4729 0.0016  -0.0313 0.0061  237 MET   D CG  
5913 S  SD  . MET   D 144 ? 0.4984 0.3802 0.4749 0.0041  -0.0271 0.0169  237 MET   D SD  
5914 C  CE  . MET   D 144 ? 0.4993 0.3965 0.4639 0.0078  -0.0329 0.0189  237 MET   D CE  
5915 N  N   A CYS   D 145 ? 0.5086 0.4021 0.4878 -0.0032 -0.0273 -0.0271 238 CYS   D N   
5916 N  N   B CYS   D 145 ? 0.5102 0.4035 0.4900 -0.0033 -0.0276 -0.0274 238 CYS   D N   
5917 C  CA  A CYS   D 145 ? 0.5217 0.4199 0.4997 -0.0042 -0.0279 -0.0409 238 CYS   D CA  
5918 C  CA  B CYS   D 145 ? 0.5256 0.4245 0.5026 -0.0040 -0.0278 -0.0406 238 CYS   D CA  
5919 C  C   A CYS   D 145 ? 0.5236 0.4181 0.5020 -0.0027 -0.0213 -0.0444 238 CYS   D C   
5920 C  C   B CYS   D 145 ? 0.5255 0.4206 0.5028 -0.0026 -0.0212 -0.0436 238 CYS   D C   
5921 O  O   A CYS   D 145 ? 0.5152 0.4012 0.5010 -0.0021 -0.0180 -0.0383 238 CYS   D O   
5922 O  O   B CYS   D 145 ? 0.5148 0.4021 0.4984 -0.0020 -0.0178 -0.0366 238 CYS   D O   
5923 C  CB  A CYS   D 145 ? 0.5265 0.4188 0.5181 -0.0073 -0.0313 -0.0485 238 CYS   D CB  
5924 C  CB  B CYS   D 145 ? 0.5342 0.4286 0.5235 -0.0071 -0.0314 -0.0501 238 CYS   D CB  
5925 S  SG  A CYS   D 145 ? 0.5458 0.4458 0.5384 -0.0105 -0.0355 -0.0662 238 CYS   D SG  
5926 S  SG  B CYS   D 145 ? 0.5576 0.4664 0.5440 -0.0094 -0.0394 -0.0570 238 CYS   D SG  
5927 N  N   . ASN   D 146 ? 0.5348 0.4377 0.5055 -0.0018 -0.0196 -0.0542 239 ASN   D N   
5928 C  CA  . ASN   D 146 ? 0.5389 0.4409 0.5112 0.0003  -0.0129 -0.0593 239 ASN   D CA  
5929 C  C   . ASN   D 146 ? 0.5464 0.4367 0.5337 0.0006  -0.0126 -0.0692 239 ASN   D C   
5930 O  O   . ASN   D 146 ? 0.5547 0.4421 0.5466 -0.0019 -0.0171 -0.0771 239 ASN   D O   
5931 C  CB  . ASN   D 146 ? 0.5591 0.4760 0.5167 0.0017  -0.0101 -0.0661 239 ASN   D CB  
5932 C  CG  . ASN   D 146 ? 0.5621 0.4878 0.5066 0.0020  -0.0072 -0.0532 239 ASN   D CG  
5933 O  OD1 . ASN   D 146 ? 0.5436 0.4642 0.4928 0.0019  -0.0032 -0.0432 239 ASN   D OD1 
5934 N  ND2 . ASN   D 146 ? 0.5821 0.5217 0.5103 0.0023  -0.0091 -0.0533 239 ASN   D ND2 
5935 N  N   . SER   D 147 ? 0.5403 0.4246 0.5362 0.0037  -0.0077 -0.0683 240 SER   D N   
5936 C  CA  . SER   D 147 ? 0.5464 0.4186 0.5572 0.0058  -0.0063 -0.0760 240 SER   D CA  
5937 C  C   . SER   D 147 ? 0.5735 0.4475 0.5832 0.0057  -0.0060 -0.0934 240 SER   D C   
5938 O  O   . SER   D 147 ? 0.5808 0.4420 0.6030 0.0051  -0.0068 -0.1009 240 SER   D O   
5939 C  CB  . SER   D 147 ? 0.5418 0.4127 0.5598 0.0108  -0.0011 -0.0722 240 SER   D CB  
5940 O  OG  . SER   D 147 ? 0.5186 0.3883 0.5387 0.0101  -0.0020 -0.0584 240 SER   D OG  
5941 N  N   . SER   D 148 ? 0.5837 0.4729 0.5788 0.0061  -0.0045 -0.0996 241 SER   D N   
5942 C  CA  . SER   D 148 ? 0.6130 0.5086 0.6036 0.0062  -0.0036 -0.1182 241 SER   D CA  
5943 C  C   . SER   D 148 ? 0.6272 0.5259 0.6143 0.0007  -0.0109 -0.1260 241 SER   D C   
5944 O  O   . SER   D 148 ? 0.6479 0.5487 0.6355 -0.0002 -0.0111 -0.1441 241 SER   D O   
5945 C  CB  . SER   D 148 ? 0.6168 0.5306 0.5913 0.0087  0.0011  -0.1200 241 SER   D CB  
5946 O  OG  . SER   D 148 ? 0.6156 0.5416 0.5742 0.0062  -0.0020 -0.1086 241 SER   D OG  
5947 N  N   . CYS   D 149 ? 0.6214 0.5220 0.6058 -0.0025 -0.0167 -0.1142 242 CYS   D N   
5948 C  CA  . CYS   D 149 ? 0.6336 0.5437 0.6132 -0.0073 -0.0244 -0.1198 242 CYS   D CA  
5949 C  C   . CYS   D 149 ? 0.6549 0.5556 0.6491 -0.0116 -0.0263 -0.1366 242 CYS   D C   
5950 O  O   . CYS   D 149 ? 0.6282 0.5113 0.6396 -0.0133 -0.0256 -0.1326 242 CYS   D O   
5951 C  CB  . CYS   D 149 ? 0.6140 0.5234 0.5951 -0.0090 -0.0291 -0.1036 242 CYS   D CB  
5952 S  SG  . CYS   D 149 ? 0.6166 0.5409 0.5785 -0.0060 -0.0298 -0.0876 242 CYS   D SG  
5953 N  N   . MET   D 150 ? 0.7004 0.6128 0.6881 -0.0136 -0.0285 -0.1548 243 MET   D N   
5954 C  CA  . MET   D 150 ? 0.7309 0.6378 0.7320 -0.0199 -0.0318 -0.1732 243 MET   D CA  
5955 C  C   . MET   D 150 ? 0.7262 0.6342 0.7355 -0.0259 -0.0390 -0.1660 243 MET   D C   
5956 O  O   . MET   D 150 ? 0.7327 0.6575 0.7298 -0.0252 -0.0443 -0.1556 243 MET   D O   
5957 C  CB  . MET   D 150 ? 0.7666 0.6925 0.7548 -0.0214 -0.0343 -0.1942 243 MET   D CB  
5958 C  CG  . MET   D 150 ? 0.7887 0.7131 0.7722 -0.0161 -0.0262 -0.2064 243 MET   D CG  
5959 S  SD  . MET   D 150 ? 0.8308 0.7688 0.8091 -0.0198 -0.0281 -0.2392 243 MET   D SD  
5960 C  CE  . MET   D 150 ? 0.8355 0.7508 0.8427 -0.0289 -0.0312 -0.2512 243 MET   D CE  
5961 N  N   . GLY   D 151 ? 0.7268 0.6174 0.7572 -0.0312 -0.0385 -0.1700 244 GLY   D N   
5962 C  CA  . GLY   D 151 ? 0.7241 0.6160 0.7658 -0.0379 -0.0441 -0.1646 244 GLY   D CA  
5963 C  C   . GLY   D 151 ? 0.7040 0.5914 0.7458 -0.0346 -0.0432 -0.1412 244 GLY   D C   
5964 O  O   . GLY   D 151 ? 0.7003 0.5955 0.7466 -0.0381 -0.0481 -0.1346 244 GLY   D O   
5965 N  N   . GLY   D 152 ? 0.6861 0.5631 0.7237 -0.0279 -0.0370 -0.1303 245 GLY   D N   
5966 C  CA  . GLY   D 152 ? 0.6605 0.5294 0.7005 -0.0249 -0.0348 -0.1105 245 GLY   D CA  
5967 C  C   . GLY   D 152 ? 0.6496 0.4985 0.6996 -0.0216 -0.0278 -0.1075 245 GLY   D C   
5968 O  O   . GLY   D 152 ? 0.6570 0.4918 0.7217 -0.0246 -0.0257 -0.1159 245 GLY   D O   
5969 N  N   . MET   D 153 ? 0.6323 0.4804 0.6752 -0.0154 -0.0243 -0.0961 246 MET   D N   
5970 C  CA  . MET   D 153 ? 0.6195 0.4529 0.6708 -0.0104 -0.0185 -0.0920 246 MET   D CA  
5971 C  C   . MET   D 153 ? 0.6293 0.4579 0.6839 -0.0078 -0.0148 -0.1077 246 MET   D C   
5972 O  O   . MET   D 153 ? 0.6285 0.4405 0.6971 -0.0054 -0.0110 -0.1087 246 MET   D O   
5973 C  CB  . MET   D 153 ? 0.6036 0.4425 0.6462 -0.0052 -0.0164 -0.0788 246 MET   D CB  
5974 C  CG  . MET   D 153 ? 0.5902 0.4303 0.6320 -0.0071 -0.0189 -0.0644 246 MET   D CG  
5975 S  SD  . MET   D 153 ? 0.5687 0.4137 0.6030 -0.0023 -0.0161 -0.0518 246 MET   D SD  
5976 C  CE  . MET   D 153 ? 0.5707 0.4319 0.5880 -0.0029 -0.0177 -0.0530 246 MET   D CE  
5977 N  N   . ASN   D 154 ? 0.6369 0.4800 0.6792 -0.0079 -0.0159 -0.1193 247 ASN   D N   
5978 C  CA  . ASN   D 154 ? 0.6608 0.5030 0.7045 -0.0062 -0.0127 -0.1385 247 ASN   D CA  
5979 C  C   . ASN   D 154 ? 0.6619 0.4921 0.7146 0.0015  -0.0058 -0.1366 247 ASN   D C   
5980 O  O   . ASN   D 154 ? 0.6745 0.4883 0.7423 0.0026  -0.0028 -0.1459 247 ASN   D O   
5981 C  CB  . ASN   D 154 ? 0.6755 0.5098 0.7307 -0.0132 -0.0154 -0.1538 247 ASN   D CB  
5982 C  CG  . ASN   D 154 ? 0.7039 0.5374 0.7606 -0.0122 -0.0123 -0.1763 247 ASN   D CG  
5983 O  OD1 . ASN   D 154 ? 0.7154 0.5645 0.7572 -0.0084 -0.0108 -0.1835 247 ASN   D OD1 
5984 N  ND2 . ASN   D 154 ? 0.7208 0.5358 0.7958 -0.0157 -0.0107 -0.1877 247 ASN   D ND2 
5985 N  N   . ARG   D 155 ? 0.6534 0.4918 0.6986 0.0066  -0.0034 -0.1244 248 ARG   D N   
5986 C  CA  . ARG   D 155 ? 0.6565 0.4922 0.7078 0.0149  0.0026  -0.1223 248 ARG   D CA  
5987 C  C   . ARG   D 155 ? 0.6435 0.4615 0.7112 0.0181  0.0034  -0.1108 248 ARG   D C   
5988 O  O   . ARG   D 155 ? 0.6544 0.4712 0.7289 0.0258  0.0074  -0.1072 248 ARG   D O   
5989 C  CB  . ARG   D 155 ? 0.6860 0.5223 0.7394 0.0187  0.0074  -0.1418 248 ARG   D CB  
5990 C  CG  . ARG   D 155 ? 0.7015 0.5580 0.7363 0.0159  0.0068  -0.1531 248 ARG   D CG  
5991 C  CD  . ARG   D 155 ? 0.7288 0.5926 0.7621 0.0218  0.0135  -0.1693 248 ARG   D CD  
5992 N  NE  . ARG   D 155 ? 0.7478 0.6344 0.7598 0.0195  0.0135  -0.1765 248 ARG   D NE  
5993 C  CZ  . ARG   D 155 ? 0.7429 0.6473 0.7404 0.0207  0.0159  -0.1660 248 ARG   D CZ  
5994 N  NH1 . ARG   D 155 ? 0.7243 0.6271 0.7272 0.0234  0.0181  -0.1492 248 ARG   D NH1 
5995 N  NH2 . ARG   D 155 ? 0.7512 0.6758 0.7288 0.0189  0.0161  -0.1723 248 ARG   D NH2 
5996 N  N   . ARG   D 156 ? 0.6276 0.4350 0.7011 0.0127  -0.0002 -0.1040 249 ARG   D N   
5997 C  CA  . ARG   D 156 ? 0.6132 0.4055 0.6999 0.0153  0.0004  -0.0907 249 ARG   D CA  
5998 C  C   . ARG   D 156 ? 0.5898 0.3924 0.6692 0.0172  -0.0009 -0.0741 249 ARG   D C   
5999 O  O   . ARG   D 156 ? 0.5797 0.3932 0.6478 0.0122  -0.0042 -0.0697 249 ARG   D O   
6000 C  CB  . ARG   D 156 ? 0.6211 0.4002 0.7164 0.0079  -0.0018 -0.0900 249 ARG   D CB  
6001 C  CG  . ARG   D 156 ? 0.6452 0.4121 0.7508 0.0048  -0.0001 -0.1077 249 ARG   D CG  
6002 C  CD  . ARG   D 156 ? 0.6517 0.4086 0.7666 -0.0045 -0.0024 -0.1074 249 ARG   D CD  
6003 N  NE  . ARG   D 156 ? 0.6476 0.4220 0.7509 -0.0119 -0.0081 -0.1088 249 ARG   D NE  
6004 C  CZ  . ARG   D 156 ? 0.6480 0.4214 0.7575 -0.0207 -0.0110 -0.1085 249 ARG   D CZ  
6005 N  NH1 . ARG   D 156 ? 0.6581 0.4126 0.7852 -0.0245 -0.0081 -0.1065 249 ARG   D NH1 
6006 N  NH2 . ARG   D 156 ? 0.6387 0.4305 0.7379 -0.0255 -0.0166 -0.1095 249 ARG   D NH2 
6007 N  N   . PRO   D 157 ? 0.5753 0.3755 0.6617 0.0245  0.0012  -0.0651 250 PRO   D N   
6008 C  CA  . PRO   D 157 ? 0.5578 0.3690 0.6384 0.0257  -0.0003 -0.0515 250 PRO   D CA  
6009 C  C   . PRO   D 157 ? 0.5347 0.3411 0.6148 0.0208  -0.0036 -0.0398 250 PRO   D C   
6010 O  O   . PRO   D 157 ? 0.5451 0.3370 0.6342 0.0195  -0.0033 -0.0380 250 PRO   D O   
6011 C  CB  . PRO   D 157 ? 0.5636 0.3743 0.6545 0.0354  0.0022  -0.0470 250 PRO   D CB  
6012 C  CG  . PRO   D 157 ? 0.5805 0.3717 0.6854 0.0391  0.0047  -0.0523 250 PRO   D CG  
6013 C  CD  . PRO   D 157 ? 0.5938 0.3812 0.6951 0.0325  0.0050  -0.0678 250 PRO   D CD  
6014 N  N   . ILE   D 158 ? 0.5002 0.3181 0.5706 0.0180  -0.0058 -0.0326 251 ILE   D N   
6015 C  CA  . ILE   D 158 ? 0.4872 0.3035 0.5558 0.0139  -0.0084 -0.0224 251 ILE   D CA  
6016 C  C   . ILE   D 158 ? 0.4691 0.2939 0.5356 0.0171  -0.0089 -0.0122 251 ILE   D C   
6017 O  O   . ILE   D 158 ? 0.4738 0.3088 0.5383 0.0203  -0.0081 -0.0139 251 ILE   D O   
6018 C  CB  . ILE   D 158 ? 0.4818 0.3037 0.5416 0.0069  -0.0109 -0.0254 251 ILE   D CB  
6019 C  CG1 . ILE   D 158 ? 0.4753 0.3102 0.5242 0.0068  -0.0110 -0.0269 251 ILE   D CG1 
6020 C  CG2 . ILE   D 158 ? 0.4890 0.3046 0.5523 0.0032  -0.0114 -0.0359 251 ILE   D CG2 
6021 C  CD1 . ILE   D 158 ? 0.4698 0.3099 0.5107 0.0020  -0.0137 -0.0234 251 ILE   D CD1 
6022 N  N   . LEU   D 159 ? 0.4592 0.2814 0.5267 0.0160  -0.0101 -0.0026 252 LEU   D N   
6023 C  CA  . LEU   D 159 ? 0.4491 0.2816 0.5120 0.0171  -0.0116 0.0057  252 LEU   D CA  
6024 C  C   . LEU   D 159 ? 0.4378 0.2738 0.4929 0.0107  -0.0129 0.0065  252 LEU   D C   
6025 O  O   . LEU   D 159 ? 0.4420 0.2714 0.4984 0.0066  -0.0130 0.0052  252 LEU   D O   
6026 C  CB  . LEU   D 159 ? 0.4484 0.2770 0.5166 0.0215  -0.0115 0.0161  252 LEU   D CB  
6027 C  CG  . LEU   D 159 ? 0.4596 0.2804 0.5382 0.0291  -0.0099 0.0170  252 LEU   D CG  
6028 C  CD1 . LEU   D 159 ? 0.4687 0.2843 0.5516 0.0336  -0.0097 0.0303  252 LEU   D CD1 
6029 C  CD2 . LEU   D 159 ? 0.4535 0.2861 0.5336 0.0348  -0.0101 0.0129  252 LEU   D CD2 
6030 N  N   . THR   D 160 ? 0.4341 0.2805 0.4832 0.0097  -0.0139 0.0078  253 THR   D N   
6031 C  CA  . THR   D 160 ? 0.4243 0.2740 0.4677 0.0055  -0.0147 0.0102  253 THR   D CA  
6032 C  C   . THR   D 160 ? 0.4237 0.2782 0.4669 0.0074  -0.0152 0.0175  253 THR   D C   
6033 O  O   . THR   D 160 ? 0.4322 0.2944 0.4760 0.0109  -0.0161 0.0190  253 THR   D O   
6034 C  CB  . THR   D 160 ? 0.4225 0.2789 0.4602 0.0030  -0.0148 0.0067  253 THR   D CB  
6035 O  OG1 . THR   D 160 ? 0.4280 0.2818 0.4639 0.0019  -0.0142 0.0014  253 THR   D OG1 
6036 C  CG2 . THR   D 160 ? 0.4154 0.2733 0.4491 0.0000  -0.0152 0.0085  253 THR   D CG2 
6037 N  N   . ILE   D 161 ? 0.4192 0.2713 0.4614 0.0053  -0.0147 0.0218  254 ILE   D N   
6038 C  CA  . ILE   D 161 ? 0.4199 0.2784 0.4594 0.0067  -0.0147 0.0291  254 ILE   D CA  
6039 C  C   . ILE   D 161 ? 0.4183 0.2837 0.4517 0.0032  -0.0147 0.0261  254 ILE   D C   
6040 O  O   . ILE   D 161 ? 0.3971 0.2585 0.4311 0.0000  -0.0137 0.0238  254 ILE   D O   
6041 C  CB  . ILE   D 161 ? 0.4271 0.2781 0.4707 0.0068  -0.0126 0.0366  254 ILE   D CB  
6042 C  CG1 . ILE   D 161 ? 0.4402 0.2803 0.4921 0.0100  -0.0119 0.0380  254 ILE   D CG1 
6043 C  CG2 . ILE   D 161 ? 0.4363 0.2960 0.4747 0.0086  -0.0120 0.0454  254 ILE   D CG2 
6044 C  CD1 . ILE   D 161 ? 0.4544 0.2833 0.5131 0.0084  -0.0089 0.0444  254 ILE   D CD1 
6045 N  N   . ILE   D 162 ? 0.4267 0.3028 0.4558 0.0041  -0.0160 0.0248  255 ILE   D N   
6046 C  CA  . ILE   D 162 ? 0.4347 0.3169 0.4588 0.0011  -0.0156 0.0204  255 ILE   D CA  
6047 C  C   . ILE   D 162 ? 0.4487 0.3400 0.4680 0.0024  -0.0151 0.0252  255 ILE   D C   
6048 O  O   . ILE   D 162 ? 0.4639 0.3644 0.4810 0.0056  -0.0172 0.0286  255 ILE   D O   
6049 C  CB  . ILE   D 162 ? 0.4327 0.3209 0.4564 -0.0003 -0.0168 0.0138  255 ILE   D CB  
6050 C  CG1 . ILE   D 162 ? 0.4302 0.3118 0.4576 -0.0011 -0.0165 0.0109  255 ILE   D CG1 
6051 C  CG2 . ILE   D 162 ? 0.4314 0.3221 0.4518 -0.0037 -0.0157 0.0081  255 ILE   D CG2 
6052 C  CD1 . ILE   D 162 ? 0.4283 0.2998 0.4555 -0.0031 -0.0151 0.0097  255 ILE   D CD1 
6053 N  N   A THR   D 163 ? 0.4537 0.3440 0.4713 0.0006  -0.0125 0.0261  256 THR   D N   
6054 N  N   B THR   D 163 ? 0.4510 0.3413 0.4686 0.0006  -0.0125 0.0261  256 THR   D N   
6055 C  CA  A THR   D 163 ? 0.4659 0.3663 0.4774 0.0015  -0.0108 0.0306  256 THR   D CA  
6056 C  CA  B THR   D 163 ? 0.4603 0.3603 0.4720 0.0015  -0.0107 0.0308  256 THR   D CA  
6057 C  C   A THR   D 163 ? 0.4681 0.3757 0.4752 -0.0005 -0.0096 0.0219  256 THR   D C   
6058 C  C   B THR   D 163 ? 0.4650 0.3725 0.4721 -0.0004 -0.0095 0.0221  256 THR   D C   
6059 O  O   A THR   D 163 ? 0.4622 0.3626 0.4732 -0.0025 -0.0084 0.0160  256 THR   D O   
6060 O  O   B THR   D 163 ? 0.4603 0.3607 0.4713 -0.0025 -0.0084 0.0162  256 THR   D O   
6061 C  CB  A THR   D 163 ? 0.4727 0.3680 0.4873 0.0010  -0.0073 0.0389  256 THR   D CB  
6062 C  CB  B THR   D 163 ? 0.4621 0.3560 0.4776 0.0008  -0.0072 0.0388  256 THR   D CB  
6063 O  OG1 A THR   D 163 ? 0.4745 0.3640 0.4941 -0.0021 -0.0054 0.0338  256 THR   D OG1 
6064 O  OG1 B THR   D 163 ? 0.4692 0.3738 0.4782 0.0012  -0.0042 0.0436  256 THR   D OG1 
6065 C  CG2 A THR   D 163 ? 0.4811 0.3667 0.5018 0.0029  -0.0078 0.0464  256 THR   D CG2 
6066 C  CG2 B THR   D 163 ? 0.4567 0.3424 0.4788 -0.0024 -0.0057 0.0343  256 THR   D CG2 
6067 N  N   . LEU   D 164 ? 0.4756 0.3972 0.4748 0.0005  -0.0102 0.0209  257 LEU   D N   
6068 C  CA  . LEU   D 164 ? 0.4892 0.4192 0.4836 -0.0012 -0.0084 0.0114  257 LEU   D CA  
6069 C  C   . LEU   D 164 ? 0.4887 0.4257 0.4781 -0.0002 -0.0039 0.0169  257 LEU   D C   
6070 O  O   . LEU   D 164 ? 0.5044 0.4488 0.4886 0.0020  -0.0040 0.0271  257 LEU   D O   
6071 C  CB  . LEU   D 164 ? 0.5038 0.4475 0.4927 -0.0012 -0.0122 0.0053  257 LEU   D CB  
6072 C  CG  . LEU   D 164 ? 0.5176 0.4683 0.5033 -0.0041 -0.0110 -0.0084 257 LEU   D CG  
6073 C  CD1 . LEU   D 164 ? 0.5232 0.4596 0.5177 -0.0076 -0.0103 -0.0172 257 LEU   D CD1 
6074 C  CD2 . LEU   D 164 ? 0.5377 0.5080 0.5164 -0.0042 -0.0152 -0.0134 257 LEU   D CD2 
6075 N  N   . GLU   D 165 ? 0.4871 0.4215 0.4794 -0.0015 0.0003  0.0119  258 GLU   D N   
6076 C  CA  . GLU   D 165 ? 0.4916 0.4347 0.4807 -0.0010 0.0058  0.0164  258 GLU   D CA  
6077 C  C   . GLU   D 165 ? 0.4911 0.4428 0.4766 -0.0010 0.0091  0.0041  258 GLU   D C   
6078 O  O   . GLU   D 165 ? 0.4721 0.4162 0.4624 -0.0017 0.0080  -0.0066 258 GLU   D O   
6079 C  CB  . GLU   D 165 ? 0.4946 0.4283 0.4939 -0.0022 0.0089  0.0229  258 GLU   D CB  
6080 C  CG  . GLU   D 165 ? 0.5002 0.4183 0.5092 -0.0032 0.0052  0.0221  258 GLU   D CG  
6081 C  CD  . GLU   D 165 ? 0.5095 0.4214 0.5289 -0.0050 0.0073  0.0267  258 GLU   D CD  
6082 O  OE1 . GLU   D 165 ? 0.5222 0.4377 0.5466 -0.0052 0.0104  0.0226  258 GLU   D OE1 
6083 O  OE2 . GLU   D 165 ? 0.5170 0.4215 0.5405 -0.0062 0.0059  0.0336  258 GLU   D OE2 
6084 N  N   . ASP   D 166 ? 0.4975 0.4641 0.4752 -0.0001 0.0139  0.0059  259 ASP   D N   
6085 C  CA  . ASP   D 166 ? 0.5038 0.4796 0.4788 0.0004  0.0185  -0.0067 259 ASP   D CA  
6086 C  C   . ASP   D 166 ? 0.5075 0.4760 0.4949 0.0008  0.0233  -0.0073 259 ASP   D C   
6087 O  O   . ASP   D 166 ? 0.4893 0.4476 0.4857 -0.0001 0.0222  0.0019  259 ASP   D O   
6088 C  CB  . ASP   D 166 ? 0.5215 0.5191 0.4816 0.0015  0.0219  -0.0057 259 ASP   D CB  
6089 C  CG  . ASP   D 166 ? 0.5221 0.5273 0.4802 0.0018  0.0277  0.0089  259 ASP   D CG  
6090 O  OD1 . ASP   D 166 ? 0.5120 0.5066 0.4827 0.0006  0.0303  0.0150  259 ASP   D OD1 
6091 O  OD2 . ASP   D 166 ? 0.5328 0.5556 0.4769 0.0030  0.0297  0.0142  259 ASP   D OD2 
6092 N  N   . SER   D 167 ? 0.5193 0.4940 0.5076 0.0026  0.0283  -0.0185 260 SER   D N   
6093 C  CA  . SER   D 167 ? 0.5204 0.4907 0.5221 0.0045  0.0327  -0.0210 260 SER   D CA  
6094 C  C   . SER   D 167 ? 0.5277 0.5059 0.5336 0.0033  0.0371  -0.0085 260 SER   D C   
6095 O  O   . SER   D 167 ? 0.5269 0.4999 0.5468 0.0037  0.0379  -0.0067 260 SER   D O   
6096 C  CB  . SER   D 167 ? 0.5334 0.5102 0.5351 0.0075  0.0378  -0.0360 260 SER   D CB  
6097 O  OG  . SER   D 167 ? 0.5463 0.5436 0.5357 0.0077  0.0431  -0.0377 260 SER   D OG  
6098 N  N   . SER   D 168 ? 0.5373 0.5280 0.5321 0.0017  0.0396  0.0004  261 SER   D N   
6099 C  CA  . SER   D 168 ? 0.5418 0.5403 0.5402 -0.0005 0.0453  0.0135  261 SER   D CA  
6100 C  C   . SER   D 168 ? 0.5323 0.5174 0.5362 -0.0038 0.0409  0.0267  261 SER   D C   
6101 O  O   . SER   D 168 ? 0.5385 0.5265 0.5484 -0.0070 0.0455  0.0377  261 SER   D O   
6102 C  CB  . SER   D 168 ? 0.5590 0.5774 0.5422 -0.0003 0.0513  0.0179  261 SER   D CB  
6103 O  OG  . SER   D 168 ? 0.5628 0.5952 0.5420 0.0025  0.0569  0.0043  261 SER   D OG  
6104 N  N   . GLY   D 169 ? 0.5344 0.5057 0.5371 -0.0034 0.0330  0.0253  262 GLY   D N   
6105 C  CA  . GLY   D 169 ? 0.5261 0.4836 0.5342 -0.0056 0.0286  0.0352  262 GLY   D CA  
6106 C  C   . GLY   D 169 ? 0.5440 0.5041 0.5410 -0.0050 0.0274  0.0463  262 GLY   D C   
6107 O  O   . GLY   D 169 ? 0.5626 0.5114 0.5651 -0.0064 0.0254  0.0558  262 GLY   D O   
6108 N  N   . ASN   D 170 ? 0.5465 0.5217 0.5288 -0.0026 0.0285  0.0452  263 ASN   D N   
6109 C  CA  . ASN   D 170 ? 0.5492 0.5301 0.5195 -0.0005 0.0263  0.0566  263 ASN   D CA  
6110 C  C   . ASN   D 170 ? 0.5389 0.5103 0.5098 0.0012  0.0176  0.0529  263 ASN   D C   
6111 O  O   . ASN   D 170 ? 0.5376 0.5080 0.5090 0.0012  0.0142  0.0388  263 ASN   D O   
6112 C  CB  . ASN   D 170 ? 0.5613 0.5650 0.5145 0.0017  0.0294  0.0557  263 ASN   D CB  
6113 C  CG  . ASN   D 170 ? 0.5654 0.5805 0.5176 0.0000  0.0393  0.0608  263 ASN   D CG  
6114 O  OD1 . ASN   D 170 ? 0.5645 0.5756 0.5217 -0.0021 0.0438  0.0759  263 ASN   D OD1 
6115 N  ND2 . ASN   D 170 ? 0.5650 0.5944 0.5119 0.0006  0.0433  0.0478  263 ASN   D ND2 
6116 N  N   . LEU   D 171 ? 0.5355 0.4990 0.5080 0.0027  0.0149  0.0653  264 LEU   D N   
6117 C  CA  . LEU   D 171 ? 0.5330 0.4894 0.5073 0.0050  0.0073  0.0628  264 LEU   D CA  
6118 C  C   . LEU   D 171 ? 0.5371 0.5116 0.4983 0.0081  0.0030  0.0575  264 LEU   D C   
6119 O  O   . LEU   D 171 ? 0.5515 0.5411 0.5010 0.0107  0.0044  0.0660  264 LEU   D O   
6120 C  CB  . LEU   D 171 ? 0.5379 0.4825 0.5180 0.0070  0.0064  0.0772  264 LEU   D CB  
6121 C  CG  . LEU   D 171 ? 0.5282 0.4633 0.5142 0.0093  -0.0001 0.0734  264 LEU   D CG  
6122 C  CD1 . LEU   D 171 ? 0.5233 0.4544 0.5136 0.0063  -0.0026 0.0573  264 LEU   D CD1 
6123 C  CD2 . LEU   D 171 ? 0.5302 0.4467 0.5279 0.0094  0.0007  0.0819  264 LEU   D CD2 
6124 N  N   . LEU   D 172 ? 0.5264 0.5004 0.4897 0.0072  -0.0018 0.0438  265 LEU   D N   
6125 C  CA  . LEU   D 172 ? 0.5253 0.5166 0.4793 0.0086  -0.0069 0.0357  265 LEU   D CA  
6126 C  C   . LEU   D 172 ? 0.5214 0.5107 0.4802 0.0112  -0.0136 0.0391  265 LEU   D C   
6127 O  O   . LEU   D 172 ? 0.5357 0.5428 0.4865 0.0145  -0.0183 0.0409  265 LEU   D O   
6128 C  CB  . LEU   D 172 ? 0.5203 0.5116 0.4763 0.0045  -0.0066 0.0169  265 LEU   D CB  
6129 C  CG  . LEU   D 172 ? 0.5196 0.5110 0.4746 0.0028  0.0003  0.0110  265 LEU   D CG  
6130 C  CD1 . LEU   D 172 ? 0.5196 0.5095 0.4774 0.0000  0.0003  -0.0076 265 LEU   D CD1 
6131 C  CD2 . LEU   D 172 ? 0.5316 0.5425 0.4729 0.0049  0.0040  0.0174  265 LEU   D CD2 
6132 N  N   . GLY   D 173 ? 0.5116 0.4822 0.4826 0.0102  -0.0142 0.0392  266 GLY   D N   
6133 C  CA  . GLY   D 173 ? 0.5068 0.4754 0.4841 0.0126  -0.0196 0.0403  266 GLY   D CA  
6134 C  C   . GLY   D 173 ? 0.4957 0.4430 0.4849 0.0121  -0.0182 0.0431  266 GLY   D C   
6135 O  O   . GLY   D 173 ? 0.4925 0.4275 0.4856 0.0082  -0.0144 0.0393  266 GLY   D O   
6136 N  N   . ARG   D 174 ? 0.4932 0.4376 0.4880 0.0164  -0.0211 0.0492  267 ARG   D N   
6137 C  CA  . ARG   D 174 ? 0.4842 0.4097 0.4898 0.0162  -0.0200 0.0500  267 ARG   D CA  
6138 C  C   . ARG   D 174 ? 0.4822 0.4111 0.4939 0.0197  -0.0241 0.0478  267 ARG   D C   
6139 O  O   . ARG   D 174 ? 0.4796 0.4221 0.4894 0.0254  -0.0276 0.0535  267 ARG   D O   
6140 C  CB  . ARG   D 174 ? 0.4996 0.4133 0.5084 0.0185  -0.0166 0.0627  267 ARG   D CB  
6141 C  CG  . ARG   D 174 ? 0.4977 0.3922 0.5175 0.0172  -0.0150 0.0611  267 ARG   D CG  
6142 C  CD  . ARG   D 174 ? 0.5137 0.3962 0.5390 0.0199  -0.0121 0.0733  267 ARG   D CD  
6143 N  NE  . ARG   D 174 ? 0.5317 0.4135 0.5539 0.0162  -0.0076 0.0797  267 ARG   D NE  
6144 C  CZ  . ARG   D 174 ? 0.5425 0.4298 0.5596 0.0189  -0.0053 0.0930  267 ARG   D CZ  
6145 N  NH1 . ARG   D 174 ? 0.5497 0.4439 0.5631 0.0263  -0.0080 0.1025  267 ARG   D NH1 
6146 N  NH2 . ARG   D 174 ? 0.5580 0.4450 0.5735 0.0144  0.0000  0.0975  267 ARG   D NH2 
6147 N  N   . ASN   D 175 ? 0.4701 0.3888 0.4888 0.0169  -0.0234 0.0401  268 ASN   D N   
6148 C  CA  . ASN   D 175 ? 0.4767 0.3963 0.5033 0.0200  -0.0255 0.0379  268 ASN   D CA  
6149 C  C   . ASN   D 175 ? 0.4715 0.3731 0.5045 0.0186  -0.0225 0.0357  268 ASN   D C   
6150 O  O   . ASN   D 175 ? 0.4909 0.3815 0.5224 0.0148  -0.0198 0.0354  268 ASN   D O   
6151 C  CB  . ASN   D 175 ? 0.4828 0.4159 0.5098 0.0167  -0.0278 0.0278  268 ASN   D CB  
6152 C  CG  . ASN   D 175 ? 0.4964 0.4459 0.5282 0.0222  -0.0320 0.0296  268 ASN   D CG  
6153 O  OD1 . ASN   D 175 ? 0.5182 0.4842 0.5452 0.0250  -0.0356 0.0329  268 ASN   D OD1 
6154 N  ND2 . ASN   D 175 ? 0.5022 0.4494 0.5433 0.0246  -0.0316 0.0278  268 ASN   D ND2 
6155 N  N   . SER   D 176 ? 0.4569 0.3577 0.4971 0.0219  -0.0230 0.0335  269 SER   D N   
6156 C  CA  . SER   D 176 ? 0.4443 0.3304 0.4900 0.0215  -0.0204 0.0302  269 SER   D CA  
6157 C  C   . SER   D 176 ? 0.4373 0.3299 0.4885 0.0231  -0.0206 0.0237  269 SER   D C   
6158 O  O   . SER   D 176 ? 0.4319 0.3397 0.4856 0.0261  -0.0230 0.0240  269 SER   D O   
6159 C  CB  . SER   D 176 ? 0.4550 0.3291 0.5057 0.0262  -0.0191 0.0377  269 SER   D CB  
6160 O  OG  . SER   D 176 ? 0.4696 0.3510 0.5249 0.0344  -0.0210 0.0443  269 SER   D OG  
6161 N  N   . PHE   D 177 ? 0.4312 0.3146 0.4839 0.0208  -0.0180 0.0177  270 PHE   D N   
6162 C  CA  . PHE   D 177 ? 0.4309 0.3193 0.4886 0.0223  -0.0165 0.0115  270 PHE   D CA  
6163 C  C   . PHE   D 177 ? 0.4381 0.3130 0.4967 0.0221  -0.0138 0.0071  270 PHE   D C   
6164 O  O   . PHE   D 177 ? 0.4506 0.3160 0.5043 0.0176  -0.0135 0.0066  270 PHE   D O   
6165 C  CB  . PHE   D 177 ? 0.4124 0.3113 0.4671 0.0163  -0.0160 0.0065  270 PHE   D CB  
6166 C  CG  . PHE   D 177 ? 0.4031 0.2942 0.4501 0.0095  -0.0150 0.0047  270 PHE   D CG  
6167 C  CD1 . PHE   D 177 ? 0.4045 0.2956 0.4468 0.0066  -0.0165 0.0071  270 PHE   D CD1 
6168 C  CD2 . PHE   D 177 ? 0.3975 0.2828 0.4417 0.0066  -0.0123 0.0008  270 PHE   D CD2 
6169 C  CE1 . PHE   D 177 ? 0.4025 0.2868 0.4395 0.0016  -0.0154 0.0054  270 PHE   D CE1 
6170 C  CE2 . PHE   D 177 ? 0.3959 0.2750 0.4336 0.0018  -0.0118 0.0005  270 PHE   D CE2 
6171 C  CZ  . PHE   D 177 ? 0.3941 0.2722 0.4293 -0.0003 -0.0133 0.0028  270 PHE   D CZ  
6172 N  N   . GLU   D 178 ? 0.4573 0.3331 0.5228 0.0271  -0.0119 0.0033  271 GLU   D N   
6173 C  CA  . GLU   D 178 ? 0.4642 0.3305 0.5302 0.0269  -0.0090 -0.0041 271 GLU   D CA  
6174 C  C   . GLU   D 178 ? 0.4608 0.3325 0.5184 0.0206  -0.0075 -0.0094 271 GLU   D C   
6175 O  O   . GLU   D 178 ? 0.4457 0.3288 0.5017 0.0182  -0.0073 -0.0083 271 GLU   D O   
6176 C  CB  . GLU   D 178 ? 0.4755 0.3431 0.5516 0.0349  -0.0068 -0.0077 271 GLU   D CB  
6177 C  CG  . GLU   D 178 ? 0.4884 0.3446 0.5657 0.0353  -0.0038 -0.0167 271 GLU   D CG  
6178 C  CD  . GLU   D 178 ? 0.4974 0.3508 0.5866 0.0444  -0.0010 -0.0210 271 GLU   D CD  
6179 O  OE1 . GLU   D 178 ? 0.5023 0.3516 0.5920 0.0447  0.0021  -0.0319 271 GLU   D OE1 
6180 O  OE2 . GLU   D 178 ? 0.5072 0.3629 0.6052 0.0517  -0.0021 -0.0139 271 GLU   D OE2 
6181 N  N   A VAL   D 179 ? 0.4686 0.3327 0.5213 0.0177  -0.0066 -0.0146 272 VAL   D N   
6182 N  N   B VAL   D 179 ? 0.4693 0.3337 0.5219 0.0177  -0.0066 -0.0147 272 VAL   D N   
6183 C  CA  A VAL   D 179 ? 0.4715 0.3402 0.5147 0.0127  -0.0053 -0.0181 272 VAL   D CA  
6184 C  CA  B VAL   D 179 ? 0.4730 0.3426 0.5163 0.0127  -0.0051 -0.0180 272 VAL   D CA  
6185 C  C   A VAL   D 179 ? 0.4851 0.3529 0.5268 0.0142  -0.0029 -0.0272 272 VAL   D C   
6186 C  C   B VAL   D 179 ? 0.4859 0.3537 0.5267 0.0137  -0.0030 -0.0269 272 VAL   D C   
6187 O  O   A VAL   D 179 ? 0.4889 0.3469 0.5346 0.0158  -0.0037 -0.0314 272 VAL   D O   
6188 O  O   B VAL   D 179 ? 0.4905 0.3486 0.5338 0.0143  -0.0043 -0.0307 272 VAL   D O   
6189 C  CB  A VAL   D 179 ? 0.4700 0.3336 0.5063 0.0075  -0.0080 -0.0144 272 VAL   D CB  
6190 C  CB  B VAL   D 179 ? 0.4718 0.3375 0.5078 0.0073  -0.0076 -0.0138 272 VAL   D CB  
6191 C  CG1 A VAL   D 179 ? 0.4688 0.3364 0.4954 0.0040  -0.0069 -0.0163 272 VAL   D CG1 
6192 C  CG1 B VAL   D 179 ? 0.4666 0.3351 0.5040 0.0061  -0.0091 -0.0073 272 VAL   D CG1 
6193 C  CG2 A VAL   D 179 ? 0.4644 0.3300 0.5014 0.0060  -0.0096 -0.0075 272 VAL   D CG2 
6194 C  CG2 B VAL   D 179 ? 0.4738 0.3296 0.5101 0.0064  -0.0100 -0.0151 272 VAL   D CG2 
6195 N  N   . ARG   D 180 ? 0.4841 0.3621 0.5205 0.0134  0.0005  -0.0304 273 ARG   D N   
6196 C  CA  . ARG   D 180 ? 0.5004 0.3811 0.5306 0.0137  0.0030  -0.0394 273 ARG   D CA  
6197 C  C   . ARG   D 180 ? 0.4969 0.3835 0.5140 0.0086  0.0033  -0.0360 273 ARG   D C   
6198 O  O   . ARG   D 180 ? 0.4865 0.3802 0.5024 0.0065  0.0059  -0.0303 273 ARG   D O   
6199 C  CB  . ARG   D 180 ? 0.5209 0.4107 0.5570 0.0187  0.0082  -0.0453 273 ARG   D CB  
6200 C  CG  . ARG   D 180 ? 0.5469 0.4339 0.5847 0.0227  0.0104  -0.0576 273 ARG   D CG  
6201 C  CD  . ARG   D 180 ? 0.5694 0.4694 0.5958 0.0212  0.0149  -0.0638 273 ARG   D CD  
6202 N  NE  . ARG   D 180 ? 0.5880 0.4926 0.6204 0.0273  0.0200  -0.0754 273 ARG   D NE  
6203 C  CZ  . ARG   D 180 ? 0.6090 0.5293 0.6365 0.0283  0.0264  -0.0799 273 ARG   D CZ  
6204 N  NH1 . ARG   D 180 ? 0.6126 0.5440 0.6288 0.0230  0.0284  -0.0726 273 ARG   D NH1 
6205 N  NH2 . ARG   D 180 ? 0.6252 0.5497 0.6594 0.0347  0.0314  -0.0918 273 ARG   D NH2 
6206 N  N   . VAL   D 181 ? 0.4909 0.3750 0.4997 0.0066  0.0006  -0.0390 274 VAL   D N   
6207 C  CA  . VAL   D 181 ? 0.5019 0.3926 0.4971 0.0034  0.0005  -0.0351 274 VAL   D CA  
6208 C  C   . VAL   D 181 ? 0.5236 0.4248 0.5102 0.0049  0.0042  -0.0436 274 VAL   D C   
6209 O  O   . VAL   D 181 ? 0.5339 0.4336 0.5212 0.0064  0.0026  -0.0544 274 VAL   D O   
6210 C  CB  . VAL   D 181 ? 0.4958 0.3813 0.4873 0.0012  -0.0054 -0.0324 274 VAL   D CB  
6211 C  CG1 . VAL   D 181 ? 0.5003 0.3915 0.4798 -0.0005 -0.0056 -0.0246 274 VAL   D CG1 
6212 C  CG2 . VAL   D 181 ? 0.4814 0.3569 0.4830 0.0005  -0.0083 -0.0272 274 VAL   D CG2 
6213 N  N   . CYS   D 182 ? 0.5335 0.4451 0.5135 0.0041  0.0097  -0.0396 275 CYS   D N   
6214 C  CA  . CYS   D 182 ? 0.5620 0.4865 0.5340 0.0059  0.0153  -0.0474 275 CYS   D CA  
6215 C  C   . CYS   D 182 ? 0.5627 0.4976 0.5218 0.0029  0.0199  -0.0380 275 CYS   D C   
6216 O  O   . CYS   D 182 ? 0.5613 0.4911 0.5218 -0.0002 0.0196  -0.0260 275 CYS   D O   
6217 C  CB  . CYS   D 182 ? 0.5707 0.4985 0.5553 0.0097  0.0204  -0.0545 275 CYS   D CB  
6218 S  SG  . CYS   D 182 ? 0.5804 0.5093 0.5785 0.0085  0.0232  -0.0446 275 CYS   D SG  
6219 N  N   . ALA   D 183 ? 0.5851 0.5337 0.5323 0.0041  0.0245  -0.0434 276 ALA   D N   
6220 C  CA  . ALA   D 183 ? 0.5926 0.5528 0.5249 0.0016  0.0300  -0.0338 276 ALA   D CA  
6221 C  C   . ALA   D 183 ? 0.5866 0.5500 0.5280 -0.0012 0.0380  -0.0263 276 ALA   D C   
6222 O  O   . ALA   D 183 ? 0.6070 0.5701 0.5431 -0.0053 0.0409  -0.0128 276 ALA   D O   
6223 C  CB  . ALA   D 183 ? 0.6146 0.5907 0.5319 0.0040  0.0334  -0.0434 276 ALA   D CB  
6224 N  N   . CYS   D 184 ? 0.5719 0.5388 0.5277 0.0009  0.0415  -0.0347 277 CYS   D N   
6225 C  CA  . CYS   D 184 ? 0.5628 0.5392 0.5287 -0.0016 0.0497  -0.0308 277 CYS   D CA  
6226 C  C   . CYS   D 184 ? 0.5419 0.5118 0.5285 -0.0003 0.0465  -0.0330 277 CYS   D C   
6227 O  O   . CYS   D 184 ? 0.5413 0.5174 0.5389 0.0046  0.0484  -0.0423 277 CYS   D O   
6228 C  CB  . CYS   D 184 ? 0.5744 0.5696 0.5366 0.0010  0.0586  -0.0393 277 CYS   D CB  
6229 S  SG  . CYS   D 184 ? 0.5772 0.5888 0.5433 -0.0051 0.0708  -0.0297 277 CYS   D SG  
6230 N  N   . PRO   D 185 ? 0.5170 0.4749 0.5090 -0.0039 0.0415  -0.0246 278 PRO   D N   
6231 C  CA  . PRO   D 185 ? 0.5068 0.4601 0.5158 -0.0025 0.0375  -0.0261 278 PRO   D CA  
6232 C  C   . PRO   D 185 ? 0.5036 0.4721 0.5274 -0.0027 0.0432  -0.0282 278 PRO   D C   
6233 O  O   . PRO   D 185 ? 0.4934 0.4645 0.5299 0.0030  0.0410  -0.0342 278 PRO   D O   
6234 C  CB  . PRO   D 185 ? 0.4976 0.4391 0.5064 -0.0079 0.0333  -0.0164 278 PRO   D CB  
6235 C  CG  . PRO   D 185 ? 0.5041 0.4394 0.4962 -0.0096 0.0325  -0.0109 278 PRO   D CG  
6236 C  CD  . PRO   D 185 ? 0.5191 0.4680 0.5010 -0.0089 0.0396  -0.0132 278 PRO   D CD  
6237 N  N   . GLY   D 186 ? 0.5119 0.4907 0.5349 -0.0091 0.0505  -0.0228 279 GLY   D N   
6238 C  CA  . GLY   D 186 ? 0.5151 0.5125 0.5530 -0.0106 0.0572  -0.0250 279 GLY   D CA  
6239 C  C   . GLY   D 186 ? 0.5283 0.5387 0.5716 -0.0021 0.0606  -0.0359 279 GLY   D C   
6240 O  O   . GLY   D 186 ? 0.5032 0.5215 0.5638 0.0025  0.0590  -0.0406 279 GLY   D O   
6241 N  N   . ARG   D 187 ? 0.5500 0.5629 0.5789 0.0005  0.0647  -0.0402 280 ARG   D N   
6242 C  CA  . ARG   D 187 ? 0.5684 0.5933 0.6009 0.0087  0.0693  -0.0527 280 ARG   D CA  
6243 C  C   . ARG   D 187 ? 0.5508 0.5631 0.5926 0.0175  0.0614  -0.0602 280 ARG   D C   
6244 O  O   . ARG   D 187 ? 0.5497 0.5706 0.6065 0.0249  0.0634  -0.0677 280 ARG   D O   
6245 C  CB  . ARG   D 187 ? 0.6052 0.6344 0.6172 0.0092  0.0742  -0.0567 280 ARG   D CB  
6246 C  CG  . ARG   D 187 ? 0.6314 0.6747 0.6464 0.0172  0.0807  -0.0713 280 ARG   D CG  
6247 C  CD  . ARG   D 187 ? 0.6687 0.7051 0.6686 0.0219  0.0782  -0.0825 280 ARG   D CD  
6248 N  NE  . ARG   D 187 ? 0.6897 0.7259 0.6658 0.0161  0.0778  -0.0760 280 ARG   D NE  
6249 C  CZ  . ARG   D 187 ? 0.7138 0.7400 0.6756 0.0171  0.0711  -0.0806 280 ARG   D CZ  
6250 N  NH1 . ARG   D 187 ? 0.7181 0.7318 0.6872 0.0224  0.0649  -0.0925 280 ARG   D NH1 
6251 N  NH2 . ARG   D 187 ? 0.7288 0.7586 0.6694 0.0126  0.0709  -0.0730 280 ARG   D NH2 
6252 N  N   . ASP   D 188 ? 0.5441 0.5368 0.5777 0.0170  0.0531  -0.0579 281 ASP   D N   
6253 C  CA  . ASP   D 188 ? 0.5339 0.5121 0.5749 0.0242  0.0464  -0.0640 281 ASP   D CA  
6254 C  C   . ASP   D 188 ? 0.5085 0.4864 0.5676 0.0270  0.0424  -0.0594 281 ASP   D C   
6255 O  O   . ASP   D 188 ? 0.5012 0.4766 0.5726 0.0357  0.0411  -0.0650 281 ASP   D O   
6256 C  CB  . ASP   D 188 ? 0.5444 0.5048 0.5721 0.0215  0.0396  -0.0624 281 ASP   D CB  
6257 C  CG  . ASP   D 188 ? 0.5689 0.5324 0.5796 0.0208  0.0422  -0.0697 281 ASP   D CG  
6258 O  OD1 . ASP   D 188 ? 0.5811 0.5594 0.5897 0.0233  0.0497  -0.0772 281 ASP   D OD1 
6259 O  OD2 . ASP   D 188 ? 0.5934 0.5468 0.5930 0.0180  0.0367  -0.0682 281 ASP   D OD2 
6260 N  N   . ARG   D 189 ? 0.4834 0.4644 0.5449 0.0203  0.0407  -0.0498 282 ARG   D N   
6261 C  CA  . ARG   D 189 ? 0.4714 0.4576 0.5494 0.0225  0.0368  -0.0463 282 ARG   D CA  
6262 C  C   . ARG   D 189 ? 0.4754 0.4825 0.5692 0.0286  0.0423  -0.0521 282 ARG   D C   
6263 O  O   . ARG   D 189 ? 0.4760 0.4840 0.5832 0.0378  0.0389  -0.0540 282 ARG   D O   
6264 C  CB  . ARG   D 189 ? 0.4514 0.4393 0.5288 0.0129  0.0348  -0.0378 282 ARG   D CB  
6265 C  CG  . ARG   D 189 ? 0.4394 0.4377 0.5331 0.0147  0.0305  -0.0360 282 ARG   D CG  
6266 C  CD  . ARG   D 189 ? 0.4318 0.4290 0.5250 0.0054  0.0273  -0.0301 282 ARG   D CD  
6267 N  NE  . ARG   D 189 ? 0.4246 0.4402 0.5343 0.0062  0.0249  -0.0309 282 ARG   D NE  
6268 C  CZ  . ARG   D 189 ? 0.4181 0.4430 0.5337 -0.0027 0.0245  -0.0295 282 ARG   D CZ  
6269 N  NH1 . ARG   D 189 ? 0.4208 0.4354 0.5275 -0.0130 0.0271  -0.0264 282 ARG   D NH1 
6270 N  NH2 . ARG   D 189 ? 0.4149 0.4599 0.5462 -0.0010 0.0214  -0.0317 282 ARG   D NH2 
6271 N  N   . ARG   D 190 ? 0.4803 0.5041 0.5732 0.0242  0.0509  -0.0540 283 ARG   D N   
6272 C  CA  . ARG   D 190 ? 0.4864 0.5340 0.5953 0.0293  0.0577  -0.0600 283 ARG   D CA  
6273 C  C   . ARG   D 190 ? 0.5046 0.5491 0.6192 0.0424  0.0585  -0.0698 283 ARG   D C   
6274 O  O   . ARG   D 190 ? 0.5010 0.5558 0.6344 0.0515  0.0575  -0.0723 283 ARG   D O   
6275 C  CB  . ARG   D 190 ? 0.4915 0.5551 0.5942 0.0221  0.0685  -0.0606 283 ARG   D CB  
6276 C  CG  . ARG   D 190 ? 0.4808 0.5631 0.5957 0.0133  0.0720  -0.0553 283 ARG   D CG  
6277 C  CD  . ARG   D 190 ? 0.4909 0.5890 0.6004 0.0064  0.0843  -0.0549 283 ARG   D CD  
6278 N  NE  . ARG   D 190 ? 0.4883 0.5827 0.5929 -0.0071 0.0858  -0.0447 283 ARG   D NE  
6279 C  CZ  . ARG   D 190 ? 0.4970 0.6000 0.5948 -0.0160 0.0961  -0.0397 283 ARG   D CZ  
6280 N  NH1 . ARG   D 190 ? 0.4982 0.5935 0.5935 -0.0279 0.0970  -0.0298 283 ARG   D NH1 
6281 N  NH2 . ARG   D 190 ? 0.5186 0.6369 0.6117 -0.0127 0.1059  -0.0445 283 ARG   D NH2 
6282 N  N   . THR   D 191 ? 0.5195 0.5503 0.6190 0.0436  0.0598  -0.0756 284 THR   D N   
6283 C  CA  . THR   D 191 ? 0.5392 0.5636 0.6426 0.0547  0.0615  -0.0875 284 THR   D CA  
6284 C  C   . THR   D 191 ? 0.5382 0.5466 0.6542 0.0628  0.0533  -0.0849 284 THR   D C   
6285 O  O   . THR   D 191 ? 0.5463 0.5593 0.6789 0.0740  0.0550  -0.0903 284 THR   D O   
6286 C  CB  . THR   D 191 ? 0.5495 0.5626 0.6322 0.0514  0.0631  -0.0941 284 THR   D CB  
6287 O  OG1 . THR   D 191 ? 0.5587 0.5895 0.6298 0.0444  0.0710  -0.0933 284 THR   D OG1 
6288 C  CG2 . THR   D 191 ? 0.5649 0.5707 0.6508 0.0611  0.0654  -0.1090 284 THR   D CG2 
6289 N  N   . GLU   D 192 ? 0.5454 0.5367 0.6544 0.0577  0.0451  -0.0760 285 GLU   D N   
6290 C  CA  . GLU   D 192 ? 0.5592 0.5338 0.6772 0.0644  0.0377  -0.0717 285 GLU   D CA  
6291 C  C   . GLU   D 192 ? 0.5618 0.5512 0.6978 0.0705  0.0351  -0.0652 285 GLU   D C   
6292 O  O   . GLU   D 192 ? 0.5736 0.5557 0.7222 0.0814  0.0323  -0.0644 285 GLU   D O   
6293 C  CB  . GLU   D 192 ? 0.5569 0.5128 0.6618 0.0566  0.0309  -0.0641 285 GLU   D CB  
6294 C  CG  . GLU   D 192 ? 0.5718 0.5111 0.6638 0.0541  0.0314  -0.0714 285 GLU   D CG  
6295 C  CD  . GLU   D 192 ? 0.5741 0.4924 0.6609 0.0508  0.0244  -0.0657 285 GLU   D CD  
6296 O  OE1 . GLU   D 192 ? 0.5677 0.4802 0.6631 0.0540  0.0197  -0.0572 285 GLU   D OE1 
6297 O  OE2 . GLU   D 192 ? 0.5899 0.4996 0.6638 0.0451  0.0236  -0.0695 285 GLU   D OE2 
6298 N  N   . GLU   D 193 ? 0.5645 0.5745 0.7029 0.0640  0.0361  -0.0611 286 GLU   D N   
6299 C  CA  . GLU   D 193 ? 0.5620 0.5918 0.7182 0.0686  0.0329  -0.0563 286 GLU   D CA  
6300 C  C   . GLU   D 193 ? 0.5801 0.6275 0.7544 0.0804  0.0386  -0.0638 286 GLU   D C   
6301 O  O   . GLU   D 193 ? 0.5764 0.6329 0.7675 0.0907  0.0343  -0.0602 286 GLU   D O   
6302 C  CB  . GLU   D 193 ? 0.5487 0.5945 0.7029 0.0562  0.0325  -0.0517 286 GLU   D CB  
6303 C  CG  . GLU   D 193 ? 0.5400 0.5720 0.6843 0.0492  0.0245  -0.0432 286 GLU   D CG  
6304 C  CD  . GLU   D 193 ? 0.5412 0.5815 0.6810 0.0355  0.0247  -0.0401 286 GLU   D CD  
6305 O  OE1 . GLU   D 193 ? 0.5553 0.6123 0.6996 0.0298  0.0316  -0.0432 286 GLU   D OE1 
6306 O  OE2 . GLU   D 193 ? 0.5418 0.5712 0.6740 0.0303  0.0186  -0.0346 286 GLU   D OE2 
6307 N  N   . GLU   D 194 ? 0.6019 0.6554 0.7733 0.0801  0.0479  -0.0738 287 GLU   D N   
6308 C  CA  . GLU   D 194 ? 0.6185 0.6915 0.8078 0.0914  0.0550  -0.0826 287 GLU   D CA  
6309 C  C   . GLU   D 194 ? 0.6270 0.6830 0.8268 0.1070  0.0524  -0.0854 287 GLU   D C   
6310 O  O   . GLU   D 194 ? 0.6163 0.6875 0.8360 0.1194  0.0554  -0.0896 287 GLU   D O   
6311 C  CB  . GLU   D 194 ? 0.6436 0.7283 0.8249 0.0867  0.0664  -0.0926 287 GLU   D CB  
6312 C  CG  . GLU   D 194 ? 0.6673 0.7331 0.8362 0.0903  0.0704  -0.1033 287 GLU   D CG  
6313 C  CD  . GLU   D 194 ? 0.6813 0.7640 0.8421 0.0870  0.0821  -0.1135 287 GLU   D CD  
6314 O  OE1 . GLU   D 194 ? 0.6983 0.7696 0.8379 0.0808  0.0840  -0.1176 287 GLU   D OE1 
6315 O  OE2 . GLU   D 194 ? 0.7003 0.8098 0.8759 0.0908  0.0892  -0.1170 287 GLU   D OE2 
6316 N  N   . ASN   D 195 ? 0.6302 0.6564 0.8191 0.1063  0.0471  -0.0826 288 ASN   D N   
6317 C  CA  . ASN   D 195 ? 0.6496 0.6545 0.8487 0.1193  0.0438  -0.0818 288 ASN   D CA  
6318 C  C   . ASN   D 195 ? 0.6406 0.6509 0.8519 0.1255  0.0352  -0.0676 288 ASN   D C   
6319 O  O   . ASN   D 195 ? 0.6342 0.6264 0.8367 0.1217  0.0282  -0.0578 288 ASN   D O   
6320 C  CB  . ASN   D 195 ? 0.6553 0.6282 0.8390 0.1141  0.0417  -0.0835 288 ASN   D CB  
6321 C  CG  . ASN   D 195 ? 0.6657 0.6355 0.8360 0.1082  0.0488  -0.0979 288 ASN   D CG  
6322 O  OD1 . ASN   D 195 ? 0.6865 0.6767 0.8586 0.1091  0.0565  -0.1068 288 ASN   D OD1 
6323 N  ND2 . ASN   D 195 ? 0.6669 0.6138 0.8233 0.1017  0.0464  -0.1002 288 ASN   D ND2 
6324 N  N   . LEU   D 196 ? 0.6462 0.6824 0.8768 0.1350  0.0359  -0.0670 289 LEU   D N   
6325 C  CA  . LEU   D 196 ? 0.6445 0.6950 0.8895 0.1433  0.0277  -0.0547 289 LEU   D CA  
6326 C  C   . LEU   D 196 ? 0.6253 0.7117 0.8754 0.1356  0.0269  -0.0540 289 LEU   D C   
6327 O  O   . LEU   D 196 ? 0.6286 0.7410 0.8951 0.1413  0.0321  -0.0605 289 LEU   D O   
6328 C  CB  . LEU   D 196 ? 0.6400 0.6691 0.8740 0.1405  0.0185  -0.0414 289 LEU   D CB  
6329 C  CG  . LEU   D 196 ? 0.6577 0.6563 0.8956 0.1521  0.0176  -0.0373 289 LEU   D CG  
6330 C  CD1 . LEU   D 196 ? 0.6565 0.6365 0.8816 0.1467  0.0099  -0.0238 289 LEU   D CD1 
6331 C  CD2 . LEU   D 196 ? 0.6704 0.6790 0.9324 0.1718  0.0171  -0.0338 289 LEU   D CD2 
6332 ZN ZN  . ZN    E .   ? 0.5560 0.4702 0.5082 0.0065  0.0474  -0.0612 301 ZN    A ZN  
6333 ZN ZN  . ZN    F .   ? 0.5726 0.6576 0.5035 -0.0295 0.0280  -0.0672 301 ZN    B ZN  
6334 ZN ZN  . ZN    G .   ? 0.4946 0.5153 0.4837 0.0052  -0.0275 -0.0160 301 ZN    C ZN  
6335 ZN ZN  . ZN    H .   ? 0.5882 0.5162 0.5563 -0.0089 -0.0404 -0.0755 301 ZN    D ZN  
6336 N  N1  . A1LU0 I .   ? 0.6767 0.6377 0.5723 0.0107  -0.0339 0.0033  302 A1LU0 D N1  
6337 C  C4  . A1LU0 I .   ? 0.6619 0.6086 0.5637 0.0120  -0.0307 0.0187  302 A1LU0 D C4  
6338 C  C5  . A1LU0 I .   ? 0.6498 0.5894 0.5640 0.0134  -0.0356 0.0223  302 A1LU0 D C5  
6339 C  C6  . A1LU0 I .   ? 0.6439 0.5697 0.5640 0.0151  -0.0324 0.0357  302 A1LU0 D C6  
6340 C  C7  . A1LU0 I .   ? 0.6701 0.5893 0.5691 0.0103  -0.0097 0.0542  302 A1LU0 D C7  
6341 C  C8  . A1LU0 I .   ? 0.6777 0.5919 0.5751 0.0074  -0.0014 0.0610  302 A1LU0 D C8  
6342 C  C10 . A1LU0 I .   ? 0.7682 0.7840 0.6304 0.0212  -0.0557 0.0077  302 A1LU0 D C10 
6343 C  C13 . A1LU0 I .   ? 0.8106 0.8352 0.6793 0.0308  -0.0685 0.0277  302 A1LU0 D C13 
6344 C  C1  . A1LU0 I .   ? 0.6498 0.5678 0.5645 0.0143  -0.0243 0.0458  302 A1LU0 D C1  
6345 C  C2  . A1LU0 I .   ? 0.6585 0.5846 0.5611 0.0123  -0.0191 0.0436  302 A1LU0 D C2  
6346 C  C3  . A1LU0 I .   ? 0.6623 0.6034 0.5579 0.0117  -0.0223 0.0300  302 A1LU0 D C3  
6347 C  C9  . A1LU0 I .   ? 0.7113 0.6897 0.5961 0.0136  -0.0409 0.0029  302 A1LU0 D C9  
6348 S  S   . A1LU0 I .   ? 0.7296 0.7153 0.6093 0.0202  -0.0478 0.0204  302 A1LU0 D S   
6349 C  C11 . A1LU0 I .   ? 0.7570 0.7720 0.6228 0.0153  -0.0528 -0.0128 302 A1LU0 D C11 
6350 N  N2  . A1LU0 I .   ? 0.7349 0.7293 0.6110 0.0123  -0.0439 -0.0120 302 A1LU0 D N2  
6351 O  O1  . A1LU0 I .   ? 0.7841 0.8155 0.6447 0.0137  -0.0581 -0.0284 302 A1LU0 D O1  
6352 C  C12 . A1LU0 I .   ? 0.7913 0.8202 0.6599 0.0235  -0.0674 0.0054  302 A1LU0 D C12 
6353 O  O2  . A1LU0 I .   ? 0.8373 0.8791 0.6894 0.0370  -0.0725 0.0382  302 A1LU0 D O2  
6354 O  O3  . A1LU0 I .   ? 0.8144 0.8186 0.6986 0.0306  -0.0648 0.0344  302 A1LU0 D O3  
# 
