data_7HAJ
# 
_entry.id   7HAJ 
# 
_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   7HAJ         pdb_00007haj 10.2210/pdb7haj/pdb 
WWPDB D_1001407230 ?            ?                   
# 
_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       2025-03-26 
_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.entry_id                        7HAJ 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.recvd_initial_deposition_date   2024-07-10 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.pdb_format_compatible           N 
_pdbx_database_status.methods_development_category    ? 
# 
_pdbx_contact_author.id                 1 
_pdbx_contact_author.name_last          Yu 
_pdbx_contact_author.name_first         Feng 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.email              yufeng@sari.ac.cn 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-9502-3277 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Huang, L.' 1  ? 
'Wang, W.'  2  ? 
'Zhu, Z.'   3  ? 
'Li, Q.'    4  ? 
'Li, M.'    5  ? 
'Zhou, H.'  6  ? 
'Xu, Q.'    7  ? 
'Wen, W.'   8  ? 
'Wang, Q.'  9  ? 
'Yu, F.'    10 ? 
# 
_citation.id                        primary 
_citation.title                     
;Novel starting points for fragment-based drug design against human heat-shock protein 90 identified using crystallographic fragment screening.
;
_citation.journal_abbrev            Iucrj 
_citation.journal_volume            12 
_citation.page_first                177 
_citation.page_last                 187 
_citation.year                      2025 
_citation.journal_id_ASTM           ? 
_citation.country                   UK 
_citation.journal_id_ISSN           2052-2525 
_citation.journal_id_CSD            ? 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   39819741 
_citation.pdbx_database_id_DOI      10.1107/S2052252524012247 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.identifier_ORCID 
_citation_author.ordinal 
primary 'Huang, L.' 0009-0001-8431-0182 1  
primary 'Wang, W.'  ?                   2  
primary 'Zhu, Z.'   ?                   3  
primary 'Li, Q.'    ?                   4  
primary 'Li, M.'    ?                   5  
primary 'Zhou, H.'  ?                   6  
primary 'Xu, Q.'    0000-0002-7137-0768 7  
primary 'Wen, W.'   ?                   8  
primary 'Wang, Q.'  ?                   9  
primary 'Yu, F.'    0000-0002-9502-3277 10 
# 
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 'Heat shock protein HSP 90-alpha'      26859.117 1   3.6.4.10 ? ? ? 
2 non-polymer syn '1-methyl-1H-indole-6-carboxylic acid' 175.184   1   ?        ? ? ? 
3 water       nat water                                  18.015    386 ?        ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        
;Heat shock 86 kDa,HSP 86,HSP86,Heat shock protein family C member 1,Lipopolysaccharide-associated protein 2,LAP-2,LPS-associated protein 2,Renal carcinoma antigen NY-REN-38
;
# 
_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       
;MDQPMEEEEVETFAFQAEIAQLMSLIINTFYSNKEIFLRELISNSSDALDKIRYESLTDPSKLDSGKELHINLIPNKQDR
TLTIVDTGIGMTKADLINNLGTIAKSGTKAFMEALQAGADISMIGQFGVGFYSAYLVAEKVTVITKHNDDEQYAWESSAG
GSFTVRTDTGEPMGRGTKVILHLKEDQTEYLEERRIKEIVKKHSQFIGYPITLFVEKERDKEVSDDEAELEHHHHHH
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MDQPMEEEEVETFAFQAEIAQLMSLIINTFYSNKEIFLRELISNSSDALDKIRYESLTDPSKLDSGKELHINLIPNKQDR
TLTIVDTGIGMTKADLINNLGTIAKSGTKAFMEALQAGADISMIGQFGVGFYSAYLVAEKVTVITKHNDDEQYAWESSAG
GSFTVRTDTGEPMGRGTKVILHLKEDQTEYLEERRIKEIVKKHSQFIGYPITLFVEKERDKEVSDDEAELEHHHHHH
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 '1-methyl-1H-indole-6-carboxylic acid' A1AXE 
3 water                                  HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   ASP n 
1 3   GLN n 
1 4   PRO n 
1 5   MET n 
1 6   GLU n 
1 7   GLU n 
1 8   GLU n 
1 9   GLU n 
1 10  VAL n 
1 11  GLU n 
1 12  THR n 
1 13  PHE n 
1 14  ALA n 
1 15  PHE n 
1 16  GLN n 
1 17  ALA n 
1 18  GLU n 
1 19  ILE n 
1 20  ALA n 
1 21  GLN n 
1 22  LEU n 
1 23  MET n 
1 24  SER n 
1 25  LEU n 
1 26  ILE n 
1 27  ILE n 
1 28  ASN n 
1 29  THR n 
1 30  PHE n 
1 31  TYR n 
1 32  SER n 
1 33  ASN n 
1 34  LYS n 
1 35  GLU n 
1 36  ILE n 
1 37  PHE n 
1 38  LEU n 
1 39  ARG n 
1 40  GLU n 
1 41  LEU n 
1 42  ILE n 
1 43  SER n 
1 44  ASN n 
1 45  SER n 
1 46  SER n 
1 47  ASP n 
1 48  ALA n 
1 49  LEU n 
1 50  ASP n 
1 51  LYS n 
1 52  ILE n 
1 53  ARG n 
1 54  TYR n 
1 55  GLU n 
1 56  SER n 
1 57  LEU n 
1 58  THR n 
1 59  ASP n 
1 60  PRO n 
1 61  SER n 
1 62  LYS n 
1 63  LEU n 
1 64  ASP n 
1 65  SER n 
1 66  GLY n 
1 67  LYS n 
1 68  GLU n 
1 69  LEU n 
1 70  HIS n 
1 71  ILE n 
1 72  ASN n 
1 73  LEU n 
1 74  ILE n 
1 75  PRO n 
1 76  ASN n 
1 77  LYS n 
1 78  GLN n 
1 79  ASP n 
1 80  ARG n 
1 81  THR n 
1 82  LEU n 
1 83  THR n 
1 84  ILE n 
1 85  VAL n 
1 86  ASP n 
1 87  THR n 
1 88  GLY n 
1 89  ILE n 
1 90  GLY n 
1 91  MET n 
1 92  THR n 
1 93  LYS n 
1 94  ALA n 
1 95  ASP n 
1 96  LEU n 
1 97  ILE n 
1 98  ASN n 
1 99  ASN n 
1 100 LEU n 
1 101 GLY n 
1 102 THR n 
1 103 ILE n 
1 104 ALA n 
1 105 LYS n 
1 106 SER n 
1 107 GLY n 
1 108 THR n 
1 109 LYS n 
1 110 ALA n 
1 111 PHE n 
1 112 MET n 
1 113 GLU n 
1 114 ALA n 
1 115 LEU n 
1 116 GLN n 
1 117 ALA n 
1 118 GLY n 
1 119 ALA n 
1 120 ASP n 
1 121 ILE n 
1 122 SER n 
1 123 MET n 
1 124 ILE n 
1 125 GLY n 
1 126 GLN n 
1 127 PHE n 
1 128 GLY n 
1 129 VAL n 
1 130 GLY n 
1 131 PHE n 
1 132 TYR n 
1 133 SER n 
1 134 ALA n 
1 135 TYR n 
1 136 LEU n 
1 137 VAL n 
1 138 ALA n 
1 139 GLU n 
1 140 LYS n 
1 141 VAL n 
1 142 THR n 
1 143 VAL n 
1 144 ILE n 
1 145 THR n 
1 146 LYS n 
1 147 HIS n 
1 148 ASN n 
1 149 ASP n 
1 150 ASP n 
1 151 GLU n 
1 152 GLN n 
1 153 TYR n 
1 154 ALA n 
1 155 TRP n 
1 156 GLU n 
1 157 SER n 
1 158 SER n 
1 159 ALA n 
1 160 GLY n 
1 161 GLY n 
1 162 SER n 
1 163 PHE n 
1 164 THR n 
1 165 VAL n 
1 166 ARG n 
1 167 THR n 
1 168 ASP n 
1 169 THR n 
1 170 GLY n 
1 171 GLU n 
1 172 PRO n 
1 173 MET n 
1 174 GLY n 
1 175 ARG n 
1 176 GLY n 
1 177 THR n 
1 178 LYS n 
1 179 VAL n 
1 180 ILE n 
1 181 LEU n 
1 182 HIS n 
1 183 LEU n 
1 184 LYS n 
1 185 GLU n 
1 186 ASP n 
1 187 GLN n 
1 188 THR n 
1 189 GLU n 
1 190 TYR n 
1 191 LEU n 
1 192 GLU n 
1 193 GLU n 
1 194 ARG n 
1 195 ARG n 
1 196 ILE n 
1 197 LYS n 
1 198 GLU n 
1 199 ILE n 
1 200 VAL n 
1 201 LYS n 
1 202 LYS n 
1 203 HIS n 
1 204 SER n 
1 205 GLN n 
1 206 PHE n 
1 207 ILE n 
1 208 GLY n 
1 209 TYR n 
1 210 PRO n 
1 211 ILE n 
1 212 THR n 
1 213 LEU n 
1 214 PHE n 
1 215 VAL n 
1 216 GLU n 
1 217 LYS n 
1 218 GLU n 
1 219 ARG n 
1 220 ASP n 
1 221 LYS n 
1 222 GLU n 
1 223 VAL n 
1 224 SER n 
1 225 ASP n 
1 226 ASP n 
1 227 GLU n 
1 228 ALA n 
1 229 GLU n 
1 230 LEU n 
1 231 GLU n 
1 232 HIS n 
1 233 HIS n 
1 234 HIS n 
1 235 HIS n 
1 236 HIS n 
1 237 HIS 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                   237 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'HSP90AA1, HSP90A, HSPC1, HSPCA' 
_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(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_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          plasmid 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       pET28 
_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 
A1AXE non-polymer         . '1-methyl-1H-indole-6-carboxylic acid' ? 'C10 H9 N O2'    175.184 
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 
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 
# 
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   MET 1   8   ?   ?   ?   A . n 
A 1 2   ASP 2   9   ?   ?   ?   A . n 
A 1 3   GLN 3   10  ?   ?   ?   A . n 
A 1 4   PRO 4   11  ?   ?   ?   A . n 
A 1 5   MET 5   12  ?   ?   ?   A . n 
A 1 6   GLU 6   13  ?   ?   ?   A . n 
A 1 7   GLU 7   14  ?   ?   ?   A . n 
A 1 8   GLU 8   15  ?   ?   ?   A . n 
A 1 9   GLU 9   16  16  GLU GLU A . n 
A 1 10  VAL 10  17  17  VAL VAL A . n 
A 1 11  GLU 11  18  18  GLU GLU A . n 
A 1 12  THR 12  19  19  THR THR A . n 
A 1 13  PHE 13  20  20  PHE PHE A . n 
A 1 14  ALA 14  21  21  ALA ALA A . n 
A 1 15  PHE 15  22  22  PHE PHE A . n 
A 1 16  GLN 16  23  23  GLN GLN A . n 
A 1 17  ALA 17  24  24  ALA ALA A . n 
A 1 18  GLU 18  25  25  GLU GLU A . n 
A 1 19  ILE 19  26  26  ILE ILE A . n 
A 1 20  ALA 20  27  27  ALA ALA A . n 
A 1 21  GLN 21  28  28  GLN GLN A . n 
A 1 22  LEU 22  29  29  LEU LEU A . n 
A 1 23  MET 23  30  30  MET MET A . n 
A 1 24  SER 24  31  31  SER SER A . n 
A 1 25  LEU 25  32  32  LEU LEU A . n 
A 1 26  ILE 26  33  33  ILE ILE A . n 
A 1 27  ILE 27  34  34  ILE ILE A . n 
A 1 28  ASN 28  35  35  ASN ASN A . n 
A 1 29  THR 29  36  36  THR THR A . n 
A 1 30  PHE 30  37  37  PHE PHE A . n 
A 1 31  TYR 31  38  38  TYR TYR A . n 
A 1 32  SER 32  39  39  SER SER A . n 
A 1 33  ASN 33  40  40  ASN ASN A . n 
A 1 34  LYS 34  41  41  LYS LYS A . n 
A 1 35  GLU 35  42  42  GLU GLU A . n 
A 1 36  ILE 36  43  43  ILE ILE A . n 
A 1 37  PHE 37  44  44  PHE PHE A . n 
A 1 38  LEU 38  45  45  LEU LEU A . n 
A 1 39  ARG 39  46  46  ARG ARG A . n 
A 1 40  GLU 40  47  47  GLU GLU A . n 
A 1 41  LEU 41  48  48  LEU LEU A . n 
A 1 42  ILE 42  49  49  ILE ILE A . n 
A 1 43  SER 43  50  50  SER SER A . n 
A 1 44  ASN 44  51  51  ASN ASN A . n 
A 1 45  SER 45  52  52  SER SER A . n 
A 1 46  SER 46  53  53  SER SER A . n 
A 1 47  ASP 47  54  54  ASP ASP A . n 
A 1 48  ALA 48  55  55  ALA ALA A . n 
A 1 49  LEU 49  56  56  LEU LEU A . n 
A 1 50  ASP 50  57  57  ASP ASP A . n 
A 1 51  LYS 51  58  58  LYS LYS A . n 
A 1 52  ILE 52  59  59  ILE ILE A . n 
A 1 53  ARG 53  60  60  ARG ARG A . n 
A 1 54  TYR 54  61  61  TYR TYR A . n 
A 1 55  GLU 55  62  62  GLU GLU A . n 
A 1 56  SER 56  63  63  SER SER A . n 
A 1 57  LEU 57  64  64  LEU LEU A . n 
A 1 58  THR 58  65  65  THR THR A . n 
A 1 59  ASP 59  66  66  ASP ASP A . n 
A 1 60  PRO 60  67  67  PRO PRO A . n 
A 1 61  SER 61  68  68  SER SER A . n 
A 1 62  LYS 62  69  69  LYS LYS A . n 
A 1 63  LEU 63  70  70  LEU LEU A . n 
A 1 64  ASP 64  71  71  ASP ASP A . n 
A 1 65  SER 65  72  72  SER SER A . n 
A 1 66  GLY 66  73  73  GLY GLY A . n 
A 1 67  LYS 67  74  74  LYS LYS A . n 
A 1 68  GLU 68  75  75  GLU GLU A . n 
A 1 69  LEU 69  76  76  LEU LEU A . n 
A 1 70  HIS 70  77  77  HIS HIS A . n 
A 1 71  ILE 71  78  78  ILE ILE A . n 
A 1 72  ASN 72  79  79  ASN ASN A . n 
A 1 73  LEU 73  80  80  LEU LEU A . n 
A 1 74  ILE 74  81  81  ILE ILE A . n 
A 1 75  PRO 75  82  82  PRO PRO A . n 
A 1 76  ASN 76  83  83  ASN ASN A . n 
A 1 77  LYS 77  84  84  LYS LYS A . n 
A 1 78  GLN 78  85  85  GLN GLN A . n 
A 1 79  ASP 79  86  86  ASP ASP A . n 
A 1 80  ARG 80  87  87  ARG ARG A . n 
A 1 81  THR 81  88  88  THR THR A . n 
A 1 82  LEU 82  89  89  LEU LEU A . n 
A 1 83  THR 83  90  90  THR THR A . n 
A 1 84  ILE 84  91  91  ILE ILE A . n 
A 1 85  VAL 85  92  92  VAL VAL A . n 
A 1 86  ASP 86  93  93  ASP ASP A . n 
A 1 87  THR 87  94  94  THR THR A . n 
A 1 88  GLY 88  95  95  GLY GLY A . n 
A 1 89  ILE 89  96  96  ILE ILE A . n 
A 1 90  GLY 90  97  97  GLY GLY A . n 
A 1 91  MET 91  98  98  MET MET A . n 
A 1 92  THR 92  99  99  THR THR A . n 
A 1 93  LYS 93  100 100 LYS LYS A . n 
A 1 94  ALA 94  101 101 ALA ALA A . n 
A 1 95  ASP 95  102 102 ASP ASP A . n 
A 1 96  LEU 96  103 103 LEU LEU A . n 
A 1 97  ILE 97  104 104 ILE ILE A . n 
A 1 98  ASN 98  105 105 ASN ASN A . n 
A 1 99  ASN 99  106 106 ASN ASN A . n 
A 1 100 LEU 100 107 107 LEU LEU A . n 
A 1 101 GLY 101 108 108 GLY GLY A . n 
A 1 102 THR 102 109 109 THR THR A . n 
A 1 103 ILE 103 110 110 ILE ILE A . n 
A 1 104 ALA 104 111 111 ALA ALA A . n 
A 1 105 LYS 105 112 112 LYS LYS A . n 
A 1 106 SER 106 113 113 SER SER A . n 
A 1 107 GLY 107 114 114 GLY GLY A . n 
A 1 108 THR 108 115 115 THR THR A . n 
A 1 109 LYS 109 116 116 LYS LYS A . n 
A 1 110 ALA 110 117 117 ALA ALA A . n 
A 1 111 PHE 111 118 118 PHE PHE A . n 
A 1 112 MET 112 119 119 MET MET A . n 
A 1 113 GLU 113 120 120 GLU GLU A . n 
A 1 114 ALA 114 121 121 ALA ALA A . n 
A 1 115 LEU 115 122 122 LEU LEU A . n 
A 1 116 GLN 116 123 123 GLN GLN A . n 
A 1 117 ALA 117 124 124 ALA ALA A . n 
A 1 118 GLY 118 125 125 GLY GLY A . n 
A 1 119 ALA 119 126 126 ALA ALA A . n 
A 1 120 ASP 120 127 127 ASP ASP A . n 
A 1 121 ILE 121 128 128 ILE ILE A . n 
A 1 122 SER 122 129 129 SER SER A . n 
A 1 123 MET 123 130 130 MET MET A . n 
A 1 124 ILE 124 131 131 ILE ILE A . n 
A 1 125 GLY 125 132 132 GLY GLY A . n 
A 1 126 GLN 126 133 133 GLN GLN A . n 
A 1 127 PHE 127 134 134 PHE PHE A . n 
A 1 128 GLY 128 135 135 GLY GLY A . n 
A 1 129 VAL 129 136 136 VAL VAL A . n 
A 1 130 GLY 130 137 137 GLY GLY A . n 
A 1 131 PHE 131 138 138 PHE PHE A . n 
A 1 132 TYR 132 139 139 TYR TYR A . n 
A 1 133 SER 133 140 140 SER SER A . n 
A 1 134 ALA 134 141 141 ALA ALA A . n 
A 1 135 TYR 135 142 142 TYR TYR A . n 
A 1 136 LEU 136 143 143 LEU LEU A . n 
A 1 137 VAL 137 144 144 VAL VAL A . n 
A 1 138 ALA 138 145 145 ALA ALA A . n 
A 1 139 GLU 139 146 146 GLU GLU A . n 
A 1 140 LYS 140 147 147 LYS LYS A . n 
A 1 141 VAL 141 148 148 VAL VAL A . n 
A 1 142 THR 142 149 149 THR THR A . n 
A 1 143 VAL 143 150 150 VAL VAL A . n 
A 1 144 ILE 144 151 151 ILE ILE A . n 
A 1 145 THR 145 152 152 THR THR A . n 
A 1 146 LYS 146 153 153 LYS LYS A . n 
A 1 147 HIS 147 154 154 HIS HIS A . n 
A 1 148 ASN 148 155 155 ASN ASN A . n 
A 1 149 ASP 149 156 156 ASP ASP A . n 
A 1 150 ASP 150 157 157 ASP ASP A . n 
A 1 151 GLU 151 158 158 GLU GLU A . n 
A 1 152 GLN 152 159 159 GLN GLN A . n 
A 1 153 TYR 153 160 160 TYR TYR A . n 
A 1 154 ALA 154 161 161 ALA ALA A . n 
A 1 155 TRP 155 162 162 TRP TRP A . n 
A 1 156 GLU 156 163 163 GLU GLU A . n 
A 1 157 SER 157 164 164 SER SER A . n 
A 1 158 SER 158 165 165 SER SER A . n 
A 1 159 ALA 159 166 166 ALA ALA A . n 
A 1 160 GLY 160 167 167 GLY GLY A . n 
A 1 161 GLY 161 168 168 GLY GLY A . n 
A 1 162 SER 162 169 169 SER SER A . n 
A 1 163 PHE 163 170 170 PHE PHE A . n 
A 1 164 THR 164 171 171 THR THR A . n 
A 1 165 VAL 165 172 172 VAL VAL A . n 
A 1 166 ARG 166 173 173 ARG ARG A . n 
A 1 167 THR 167 174 174 THR THR A . n 
A 1 168 ASP 168 175 175 ASP ASP A . n 
A 1 169 THR 169 176 176 THR THR A . n 
A 1 170 GLY 170 177 177 GLY GLY A . n 
A 1 171 GLU 171 178 178 GLU GLU A . n 
A 1 172 PRO 172 179 179 PRO PRO A . n 
A 1 173 MET 173 180 180 MET MET A . n 
A 1 174 GLY 174 181 181 GLY GLY A . n 
A 1 175 ARG 175 182 182 ARG ARG A . n 
A 1 176 GLY 176 183 183 GLY GLY A . n 
A 1 177 THR 177 184 184 THR THR A . n 
A 1 178 LYS 178 185 185 LYS LYS A . n 
A 1 179 VAL 179 186 186 VAL VAL A . n 
A 1 180 ILE 180 187 187 ILE ILE A . n 
A 1 181 LEU 181 188 188 LEU LEU A . n 
A 1 182 HIS 182 189 189 HIS HIS A . n 
A 1 183 LEU 183 190 190 LEU LEU A . n 
A 1 184 LYS 184 191 191 LYS LYS A . n 
A 1 185 GLU 185 192 192 GLU GLU A . n 
A 1 186 ASP 186 193 193 ASP ASP A . n 
A 1 187 GLN 187 194 194 GLN GLN A . n 
A 1 188 THR 188 195 195 THR THR A . n 
A 1 189 GLU 189 196 196 GLU GLU A . n 
A 1 190 TYR 190 197 197 TYR TYR A . n 
A 1 191 LEU 191 198 198 LEU LEU A . n 
A 1 192 GLU 192 199 199 GLU GLU A . n 
A 1 193 GLU 193 200 200 GLU GLU A . n 
A 1 194 ARG 194 201 201 ARG ARG A . n 
A 1 195 ARG 195 202 202 ARG ARG A . n 
A 1 196 ILE 196 203 203 ILE ILE A . n 
A 1 197 LYS 197 204 204 LYS LYS A . n 
A 1 198 GLU 198 205 205 GLU GLU A . n 
A 1 199 ILE 199 206 206 ILE ILE A . n 
A 1 200 VAL 200 207 207 VAL VAL A . n 
A 1 201 LYS 201 208 208 LYS LYS A . n 
A 1 202 LYS 202 209 209 LYS LYS A . n 
A 1 203 HIS 203 210 210 HIS HIS A . n 
A 1 204 SER 204 211 211 SER SER A . n 
A 1 205 GLN 205 212 212 GLN GLN A . n 
A 1 206 PHE 206 213 213 PHE PHE A . n 
A 1 207 ILE 207 214 214 ILE ILE A . n 
A 1 208 GLY 208 215 215 GLY GLY A . n 
A 1 209 TYR 209 216 216 TYR TYR A . n 
A 1 210 PRO 210 217 217 PRO PRO A . n 
A 1 211 ILE 211 218 218 ILE ILE A . n 
A 1 212 THR 212 219 219 THR THR A . n 
A 1 213 LEU 213 220 220 LEU LEU A . n 
A 1 214 PHE 214 221 221 PHE PHE A . n 
A 1 215 VAL 215 222 222 VAL VAL A . n 
A 1 216 GLU 216 223 223 GLU GLU A . n 
A 1 217 LYS 217 224 224 LYS LYS A . n 
A 1 218 GLU 218 225 ?   ?   ?   A . n 
A 1 219 ARG 219 226 ?   ?   ?   A . n 
A 1 220 ASP 220 227 ?   ?   ?   A . n 
A 1 221 LYS 221 228 ?   ?   ?   A . n 
A 1 222 GLU 222 229 ?   ?   ?   A . n 
A 1 223 VAL 223 230 ?   ?   ?   A . n 
A 1 224 SER 224 231 ?   ?   ?   A . n 
A 1 225 ASP 225 232 ?   ?   ?   A . n 
A 1 226 ASP 226 233 ?   ?   ?   A . n 
A 1 227 GLU 227 234 ?   ?   ?   A . n 
A 1 228 ALA 228 235 ?   ?   ?   A . n 
A 1 229 GLU 229 236 ?   ?   ?   A . n 
A 1 230 LEU 230 237 ?   ?   ?   A . n 
A 1 231 GLU 231 238 ?   ?   ?   A . n 
A 1 232 HIS 232 239 ?   ?   ?   A . n 
A 1 233 HIS 233 240 ?   ?   ?   A . n 
A 1 234 HIS 234 241 ?   ?   ?   A . n 
A 1 235 HIS 235 242 ?   ?   ?   A . n 
A 1 236 HIS 236 243 ?   ?   ?   A . n 
A 1 237 HIS 237 244 ?   ?   ?   A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1AXE 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1AXE 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
B 2 A1AXE 1   301 301 A1AXE E5I A . 
C 3 HOH   1   401 272 HOH   HOH A . 
C 3 HOH   2   402 212 HOH   HOH A . 
C 3 HOH   3   403 293 HOH   HOH A . 
C 3 HOH   4   404 345 HOH   HOH A . 
C 3 HOH   5   405 63  HOH   HOH A . 
C 3 HOH   6   406 236 HOH   HOH A . 
C 3 HOH   7   407 247 HOH   HOH A . 
C 3 HOH   8   408 319 HOH   HOH A . 
C 3 HOH   9   409 200 HOH   HOH A . 
C 3 HOH   10  410 188 HOH   HOH A . 
C 3 HOH   11  411 343 HOH   HOH A . 
C 3 HOH   12  412 180 HOH   HOH A . 
C 3 HOH   13  413 309 HOH   HOH A . 
C 3 HOH   14  414 385 HOH   HOH A . 
C 3 HOH   15  415 367 HOH   HOH A . 
C 3 HOH   16  416 357 HOH   HOH A . 
C 3 HOH   17  417 116 HOH   HOH A . 
C 3 HOH   18  418 169 HOH   HOH A . 
C 3 HOH   19  419 95  HOH   HOH A . 
C 3 HOH   20  420 147 HOH   HOH A . 
C 3 HOH   21  421 220 HOH   HOH A . 
C 3 HOH   22  422 174 HOH   HOH A . 
C 3 HOH   23  423 255 HOH   HOH A . 
C 3 HOH   24  424 81  HOH   HOH A . 
C 3 HOH   25  425 223 HOH   HOH A . 
C 3 HOH   26  426 73  HOH   HOH A . 
C 3 HOH   27  427 213 HOH   HOH A . 
C 3 HOH   28  428 42  HOH   HOH A . 
C 3 HOH   29  429 224 HOH   HOH A . 
C 3 HOH   30  430 307 HOH   HOH A . 
C 3 HOH   31  431 105 HOH   HOH A . 
C 3 HOH   32  432 239 HOH   HOH A . 
C 3 HOH   33  433 84  HOH   HOH A . 
C 3 HOH   34  434 115 HOH   HOH A . 
C 3 HOH   35  435 127 HOH   HOH A . 
C 3 HOH   36  436 253 HOH   HOH A . 
C 3 HOH   37  437 59  HOH   HOH A . 
C 3 HOH   38  438 366 HOH   HOH A . 
C 3 HOH   39  439 28  HOH   HOH A . 
C 3 HOH   40  440 205 HOH   HOH A . 
C 3 HOH   41  441 14  HOH   HOH A . 
C 3 HOH   42  442 111 HOH   HOH A . 
C 3 HOH   43  443 308 HOH   HOH A . 
C 3 HOH   44  444 364 HOH   HOH A . 
C 3 HOH   45  445 304 HOH   HOH A . 
C 3 HOH   46  446 237 HOH   HOH A . 
C 3 HOH   47  447 80  HOH   HOH A . 
C 3 HOH   48  448 341 HOH   HOH A . 
C 3 HOH   49  449 22  HOH   HOH A . 
C 3 HOH   50  450 25  HOH   HOH A . 
C 3 HOH   51  451 17  HOH   HOH A . 
C 3 HOH   52  452 55  HOH   HOH A . 
C 3 HOH   53  453 53  HOH   HOH A . 
C 3 HOH   54  454 353 HOH   HOH A . 
C 3 HOH   55  455 23  HOH   HOH A . 
C 3 HOH   56  456 288 HOH   HOH A . 
C 3 HOH   57  457 70  HOH   HOH A . 
C 3 HOH   58  458 61  HOH   HOH A . 
C 3 HOH   59  459 264 HOH   HOH A . 
C 3 HOH   60  460 99  HOH   HOH A . 
C 3 HOH   61  461 359 HOH   HOH A . 
C 3 HOH   62  462 62  HOH   HOH A . 
C 3 HOH   63  463 281 HOH   HOH A . 
C 3 HOH   64  464 44  HOH   HOH A . 
C 3 HOH   65  465 88  HOH   HOH A . 
C 3 HOH   66  466 31  HOH   HOH A . 
C 3 HOH   67  467 179 HOH   HOH A . 
C 3 HOH   68  468 154 HOH   HOH A . 
C 3 HOH   69  469 46  HOH   HOH A . 
C 3 HOH   70  470 30  HOH   HOH A . 
C 3 HOH   71  471 12  HOH   HOH A . 
C 3 HOH   72  472 86  HOH   HOH A . 
C 3 HOH   73  473 121 HOH   HOH A . 
C 3 HOH   74  474 27  HOH   HOH A . 
C 3 HOH   75  475 123 HOH   HOH A . 
C 3 HOH   76  476 64  HOH   HOH A . 
C 3 HOH   77  477 7   HOH   HOH A . 
C 3 HOH   78  478 48  HOH   HOH A . 
C 3 HOH   79  479 39  HOH   HOH A . 
C 3 HOH   80  480 148 HOH   HOH A . 
C 3 HOH   81  481 113 HOH   HOH A . 
C 3 HOH   82  482 136 HOH   HOH A . 
C 3 HOH   83  483 15  HOH   HOH A . 
C 3 HOH   84  484 325 HOH   HOH A . 
C 3 HOH   85  485 8   HOH   HOH A . 
C 3 HOH   86  486 29  HOH   HOH A . 
C 3 HOH   87  487 33  HOH   HOH A . 
C 3 HOH   88  488 13  HOH   HOH A . 
C 3 HOH   89  489 254 HOH   HOH A . 
C 3 HOH   90  490 66  HOH   HOH A . 
C 3 HOH   91  491 89  HOH   HOH A . 
C 3 HOH   92  492 197 HOH   HOH A . 
C 3 HOH   93  493 5   HOH   HOH A . 
C 3 HOH   94  494 3   HOH   HOH A . 
C 3 HOH   95  495 47  HOH   HOH A . 
C 3 HOH   96  496 60  HOH   HOH A . 
C 3 HOH   97  497 371 HOH   HOH A . 
C 3 HOH   98  498 19  HOH   HOH A . 
C 3 HOH   99  499 1   HOH   HOH A . 
C 3 HOH   100 500 110 HOH   HOH A . 
C 3 HOH   101 501 233 HOH   HOH A . 
C 3 HOH   102 502 94  HOH   HOH A . 
C 3 HOH   103 503 137 HOH   HOH A . 
C 3 HOH   104 504 41  HOH   HOH A . 
C 3 HOH   105 505 159 HOH   HOH A . 
C 3 HOH   106 506 87  HOH   HOH A . 
C 3 HOH   107 507 11  HOH   HOH A . 
C 3 HOH   108 508 54  HOH   HOH A . 
C 3 HOH   109 509 83  HOH   HOH A . 
C 3 HOH   110 510 187 HOH   HOH A . 
C 3 HOH   111 511 206 HOH   HOH A . 
C 3 HOH   112 512 384 HOH   HOH A . 
C 3 HOH   113 513 38  HOH   HOH A . 
C 3 HOH   114 514 52  HOH   HOH A . 
C 3 HOH   115 515 300 HOH   HOH A . 
C 3 HOH   116 516 273 HOH   HOH A . 
C 3 HOH   117 517 92  HOH   HOH A . 
C 3 HOH   118 518 333 HOH   HOH A . 
C 3 HOH   119 519 256 HOH   HOH A . 
C 3 HOH   120 520 157 HOH   HOH A . 
C 3 HOH   121 521 195 HOH   HOH A . 
C 3 HOH   122 522 97  HOH   HOH A . 
C 3 HOH   123 523 162 HOH   HOH A . 
C 3 HOH   124 524 96  HOH   HOH A . 
C 3 HOH   125 525 65  HOH   HOH A . 
C 3 HOH   126 526 166 HOH   HOH A . 
C 3 HOH   127 527 18  HOH   HOH A . 
C 3 HOH   128 528 301 HOH   HOH A . 
C 3 HOH   129 529 128 HOH   HOH A . 
C 3 HOH   130 530 16  HOH   HOH A . 
C 3 HOH   131 531 26  HOH   HOH A . 
C 3 HOH   132 532 210 HOH   HOH A . 
C 3 HOH   133 533 129 HOH   HOH A . 
C 3 HOH   134 534 72  HOH   HOH A . 
C 3 HOH   135 535 271 HOH   HOH A . 
C 3 HOH   136 536 194 HOH   HOH A . 
C 3 HOH   137 537 196 HOH   HOH A . 
C 3 HOH   138 538 297 HOH   HOH A . 
C 3 HOH   139 539 149 HOH   HOH A . 
C 3 HOH   140 540 20  HOH   HOH A . 
C 3 HOH   141 541 36  HOH   HOH A . 
C 3 HOH   142 542 381 HOH   HOH A . 
C 3 HOH   143 543 24  HOH   HOH A . 
C 3 HOH   144 544 198 HOH   HOH A . 
C 3 HOH   145 545 150 HOH   HOH A . 
C 3 HOH   146 546 276 HOH   HOH A . 
C 3 HOH   147 547 299 HOH   HOH A . 
C 3 HOH   148 548 21  HOH   HOH A . 
C 3 HOH   149 549 75  HOH   HOH A . 
C 3 HOH   150 550 306 HOH   HOH A . 
C 3 HOH   151 551 77  HOH   HOH A . 
C 3 HOH   152 552 6   HOH   HOH A . 
C 3 HOH   153 553 104 HOH   HOH A . 
C 3 HOH   154 554 355 HOH   HOH A . 
C 3 HOH   155 555 9   HOH   HOH A . 
C 3 HOH   156 556 238 HOH   HOH A . 
C 3 HOH   157 557 168 HOH   HOH A . 
C 3 HOH   158 558 170 HOH   HOH A . 
C 3 HOH   159 559 119 HOH   HOH A . 
C 3 HOH   160 560 251 HOH   HOH A . 
C 3 HOH   161 561 120 HOH   HOH A . 
C 3 HOH   162 562 103 HOH   HOH A . 
C 3 HOH   163 563 91  HOH   HOH A . 
C 3 HOH   164 564 144 HOH   HOH A . 
C 3 HOH   165 565 139 HOH   HOH A . 
C 3 HOH   166 566 4   HOH   HOH A . 
C 3 HOH   167 567 315 HOH   HOH A . 
C 3 HOH   168 568 98  HOH   HOH A . 
C 3 HOH   169 569 379 HOH   HOH A . 
C 3 HOH   170 570 352 HOH   HOH A . 
C 3 HOH   171 571 278 HOH   HOH A . 
C 3 HOH   172 572 260 HOH   HOH A . 
C 3 HOH   173 573 181 HOH   HOH A . 
C 3 HOH   174 574 219 HOH   HOH A . 
C 3 HOH   175 575 263 HOH   HOH A . 
C 3 HOH   176 576 167 HOH   HOH A . 
C 3 HOH   177 577 368 HOH   HOH A . 
C 3 HOH   178 578 108 HOH   HOH A . 
C 3 HOH   179 579 184 HOH   HOH A . 
C 3 HOH   180 580 106 HOH   HOH A . 
C 3 HOH   181 581 245 HOH   HOH A . 
C 3 HOH   182 582 386 HOH   HOH A . 
C 3 HOH   183 583 295 HOH   HOH A . 
C 3 HOH   184 584 160 HOH   HOH A . 
C 3 HOH   185 585 71  HOH   HOH A . 
C 3 HOH   186 586 43  HOH   HOH A . 
C 3 HOH   187 587 10  HOH   HOH A . 
C 3 HOH   188 588 141 HOH   HOH A . 
C 3 HOH   189 589 173 HOH   HOH A . 
C 3 HOH   190 590 56  HOH   HOH A . 
C 3 HOH   191 591 50  HOH   HOH A . 
C 3 HOH   192 592 274 HOH   HOH A . 
C 3 HOH   193 593 131 HOH   HOH A . 
C 3 HOH   194 594 102 HOH   HOH A . 
C 3 HOH   195 595 204 HOH   HOH A . 
C 3 HOH   196 596 100 HOH   HOH A . 
C 3 HOH   197 597 138 HOH   HOH A . 
C 3 HOH   198 598 74  HOH   HOH A . 
C 3 HOH   199 599 292 HOH   HOH A . 
C 3 HOH   200 600 313 HOH   HOH A . 
C 3 HOH   201 601 85  HOH   HOH A . 
C 3 HOH   202 602 107 HOH   HOH A . 
C 3 HOH   203 603 109 HOH   HOH A . 
C 3 HOH   204 604 126 HOH   HOH A . 
C 3 HOH   205 605 153 HOH   HOH A . 
C 3 HOH   206 606 82  HOH   HOH A . 
C 3 HOH   207 607 314 HOH   HOH A . 
C 3 HOH   208 608 289 HOH   HOH A . 
C 3 HOH   209 609 158 HOH   HOH A . 
C 3 HOH   210 610 298 HOH   HOH A . 
C 3 HOH   211 611 37  HOH   HOH A . 
C 3 HOH   212 612 186 HOH   HOH A . 
C 3 HOH   213 613 317 HOH   HOH A . 
C 3 HOH   214 614 282 HOH   HOH A . 
C 3 HOH   215 615 117 HOH   HOH A . 
C 3 HOH   216 616 32  HOH   HOH A . 
C 3 HOH   217 617 45  HOH   HOH A . 
C 3 HOH   218 618 118 HOH   HOH A . 
C 3 HOH   219 619 261 HOH   HOH A . 
C 3 HOH   220 620 152 HOH   HOH A . 
C 3 HOH   221 621 69  HOH   HOH A . 
C 3 HOH   222 622 146 HOH   HOH A . 
C 3 HOH   223 623 248 HOH   HOH A . 
C 3 HOH   224 624 112 HOH   HOH A . 
C 3 HOH   225 625 192 HOH   HOH A . 
C 3 HOH   226 626 250 HOH   HOH A . 
C 3 HOH   227 627 222 HOH   HOH A . 
C 3 HOH   228 628 303 HOH   HOH A . 
C 3 HOH   229 629 34  HOH   HOH A . 
C 3 HOH   230 630 363 HOH   HOH A . 
C 3 HOH   231 631 348 HOH   HOH A . 
C 3 HOH   232 632 134 HOH   HOH A . 
C 3 HOH   233 633 35  HOH   HOH A . 
C 3 HOH   234 634 269 HOH   HOH A . 
C 3 HOH   235 635 225 HOH   HOH A . 
C 3 HOH   236 636 49  HOH   HOH A . 
C 3 HOH   237 637 171 HOH   HOH A . 
C 3 HOH   238 638 142 HOH   HOH A . 
C 3 HOH   239 639 101 HOH   HOH A . 
C 3 HOH   240 640 228 HOH   HOH A . 
C 3 HOH   241 641 322 HOH   HOH A . 
C 3 HOH   242 642 90  HOH   HOH A . 
C 3 HOH   243 643 235 HOH   HOH A . 
C 3 HOH   244 644 380 HOH   HOH A . 
C 3 HOH   245 645 190 HOH   HOH A . 
C 3 HOH   246 646 285 HOH   HOH A . 
C 3 HOH   247 647 339 HOH   HOH A . 
C 3 HOH   248 648 51  HOH   HOH A . 
C 3 HOH   249 649 262 HOH   HOH A . 
C 3 HOH   250 650 258 HOH   HOH A . 
C 3 HOH   251 651 241 HOH   HOH A . 
C 3 HOH   252 652 165 HOH   HOH A . 
C 3 HOH   253 653 340 HOH   HOH A . 
C 3 HOH   254 654 40  HOH   HOH A . 
C 3 HOH   255 655 327 HOH   HOH A . 
C 3 HOH   256 656 2   HOH   HOH A . 
C 3 HOH   257 657 266 HOH   HOH A . 
C 3 HOH   258 658 382 HOH   HOH A . 
C 3 HOH   259 659 362 HOH   HOH A . 
C 3 HOH   260 660 365 HOH   HOH A . 
C 3 HOH   261 661 143 HOH   HOH A . 
C 3 HOH   262 662 242 HOH   HOH A . 
C 3 HOH   263 663 268 HOH   HOH A . 
C 3 HOH   264 664 296 HOH   HOH A . 
C 3 HOH   265 665 122 HOH   HOH A . 
C 3 HOH   266 666 354 HOH   HOH A . 
C 3 HOH   267 667 265 HOH   HOH A . 
C 3 HOH   268 668 185 HOH   HOH A . 
C 3 HOH   269 669 332 HOH   HOH A . 
C 3 HOH   270 670 155 HOH   HOH A . 
C 3 HOH   271 671 164 HOH   HOH A . 
C 3 HOH   272 672 183 HOH   HOH A . 
C 3 HOH   273 673 79  HOH   HOH A . 
C 3 HOH   274 674 243 HOH   HOH A . 
C 3 HOH   275 675 310 HOH   HOH A . 
C 3 HOH   276 676 349 HOH   HOH A . 
C 3 HOH   277 677 311 HOH   HOH A . 
C 3 HOH   278 678 370 HOH   HOH A . 
C 3 HOH   279 679 132 HOH   HOH A . 
C 3 HOH   280 680 124 HOH   HOH A . 
C 3 HOH   281 681 346 HOH   HOH A . 
C 3 HOH   282 682 193 HOH   HOH A . 
C 3 HOH   283 683 376 HOH   HOH A . 
C 3 HOH   284 684 267 HOH   HOH A . 
C 3 HOH   285 685 130 HOH   HOH A . 
C 3 HOH   286 686 369 HOH   HOH A . 
C 3 HOH   287 687 378 HOH   HOH A . 
C 3 HOH   288 688 231 HOH   HOH A . 
C 3 HOH   289 689 125 HOH   HOH A . 
C 3 HOH   290 690 226 HOH   HOH A . 
C 3 HOH   291 691 209 HOH   HOH A . 
C 3 HOH   292 692 338 HOH   HOH A . 
C 3 HOH   293 693 291 HOH   HOH A . 
C 3 HOH   294 694 351 HOH   HOH A . 
C 3 HOH   295 695 290 HOH   HOH A . 
C 3 HOH   296 696 377 HOH   HOH A . 
C 3 HOH   297 697 312 HOH   HOH A . 
C 3 HOH   298 698 78  HOH   HOH A . 
C 3 HOH   299 699 218 HOH   HOH A . 
C 3 HOH   300 700 211 HOH   HOH A . 
C 3 HOH   301 701 249 HOH   HOH A . 
C 3 HOH   302 702 361 HOH   HOH A . 
C 3 HOH   303 703 259 HOH   HOH A . 
C 3 HOH   304 704 328 HOH   HOH A . 
C 3 HOH   305 705 350 HOH   HOH A . 
C 3 HOH   306 706 257 HOH   HOH A . 
C 3 HOH   307 707 280 HOH   HOH A . 
C 3 HOH   308 708 229 HOH   HOH A . 
C 3 HOH   309 709 330 HOH   HOH A . 
C 3 HOH   310 710 93  HOH   HOH A . 
C 3 HOH   311 711 216 HOH   HOH A . 
C 3 HOH   312 712 217 HOH   HOH A . 
C 3 HOH   313 713 58  HOH   HOH A . 
C 3 HOH   314 714 342 HOH   HOH A . 
C 3 HOH   315 715 277 HOH   HOH A . 
C 3 HOH   316 716 199 HOH   HOH A . 
C 3 HOH   317 717 227 HOH   HOH A . 
C 3 HOH   318 718 68  HOH   HOH A . 
C 3 HOH   319 719 336 HOH   HOH A . 
C 3 HOH   320 720 331 HOH   HOH A . 
C 3 HOH   321 721 177 HOH   HOH A . 
C 3 HOH   322 722 176 HOH   HOH A . 
C 3 HOH   323 723 375 HOH   HOH A . 
C 3 HOH   324 724 140 HOH   HOH A . 
C 3 HOH   325 725 230 HOH   HOH A . 
C 3 HOH   326 726 215 HOH   HOH A . 
C 3 HOH   327 727 156 HOH   HOH A . 
C 3 HOH   328 728 208 HOH   HOH A . 
C 3 HOH   329 729 145 HOH   HOH A . 
C 3 HOH   330 730 214 HOH   HOH A . 
C 3 HOH   331 731 320 HOH   HOH A . 
C 3 HOH   332 732 175 HOH   HOH A . 
C 3 HOH   333 733 294 HOH   HOH A . 
C 3 HOH   334 734 114 HOH   HOH A . 
C 3 HOH   335 735 334 HOH   HOH A . 
C 3 HOH   336 736 316 HOH   HOH A . 
C 3 HOH   337 737 356 HOH   HOH A . 
C 3 HOH   338 738 240 HOH   HOH A . 
C 3 HOH   339 739 207 HOH   HOH A . 
C 3 HOH   340 740 172 HOH   HOH A . 
C 3 HOH   341 741 232 HOH   HOH A . 
C 3 HOH   342 742 203 HOH   HOH A . 
C 3 HOH   343 743 305 HOH   HOH A . 
C 3 HOH   344 744 221 HOH   HOH A . 
C 3 HOH   345 745 67  HOH   HOH A . 
C 3 HOH   346 746 373 HOH   HOH A . 
C 3 HOH   347 747 275 HOH   HOH A . 
C 3 HOH   348 748 360 HOH   HOH A . 
C 3 HOH   349 749 234 HOH   HOH A . 
C 3 HOH   350 750 372 HOH   HOH A . 
C 3 HOH   351 751 302 HOH   HOH A . 
C 3 HOH   352 752 374 HOH   HOH A . 
C 3 HOH   353 753 182 HOH   HOH A . 
C 3 HOH   354 754 244 HOH   HOH A . 
C 3 HOH   355 755 335 HOH   HOH A . 
C 3 HOH   356 756 178 HOH   HOH A . 
C 3 HOH   357 757 202 HOH   HOH A . 
C 3 HOH   358 758 283 HOH   HOH A . 
C 3 HOH   359 759 286 HOH   HOH A . 
C 3 HOH   360 760 329 HOH   HOH A . 
C 3 HOH   361 761 326 HOH   HOH A . 
C 3 HOH   362 762 324 HOH   HOH A . 
C 3 HOH   363 763 246 HOH   HOH A . 
C 3 HOH   364 764 161 HOH   HOH A . 
C 3 HOH   365 765 383 HOH   HOH A . 
C 3 HOH   366 766 358 HOH   HOH A . 
C 3 HOH   367 767 57  HOH   HOH A . 
C 3 HOH   368 768 287 HOH   HOH A . 
C 3 HOH   369 769 135 HOH   HOH A . 
C 3 HOH   370 770 151 HOH   HOH A . 
C 3 HOH   371 771 76  HOH   HOH A . 
C 3 HOH   372 772 318 HOH   HOH A . 
C 3 HOH   373 773 133 HOH   HOH A . 
C 3 HOH   374 774 163 HOH   HOH A . 
C 3 HOH   375 775 252 HOH   HOH A . 
C 3 HOH   376 776 201 HOH   HOH A . 
C 3 HOH   377 777 347 HOH   HOH A . 
C 3 HOH   378 778 189 HOH   HOH A . 
C 3 HOH   379 779 344 HOH   HOH A . 
C 3 HOH   380 780 337 HOH   HOH A . 
C 3 HOH   381 781 279 HOH   HOH A . 
C 3 HOH   382 782 284 HOH   HOH A . 
C 3 HOH   383 783 321 HOH   HOH A . 
C 3 HOH   384 784 191 HOH   HOH A . 
C 3 HOH   385 785 270 HOH   HOH A . 
C 3 HOH   386 786 323 HOH   HOH A . 
# 
loop_
_software.pdbx_ordinal 
_software.name 
_software.version 
_software.date 
_software.type 
_software.contact_author 
_software.contact_author_email 
_software.classification 
_software.location 
_software.language 
_software.citation_id 
1 XDS         .           ?               package 'Wolfgang Kabsch' Wolfgang.Kabsch@mpimf-heidelberg.mpg.de 'data reduction'  
http://www.mpimf-heidelberg.mpg.de/~kabsch/xds/     ?   ? 
2 Aimless     0.7.7       23/04/21        program 'Phil Evans'      ?                                       'data scaling'    
http://www.mrc-lmb.cam.ac.uk/harry/pre/aimless.html ?   ? 
3 DIMPLE      .           ?               program 'Marcin Wojdyr'   wojdyr@gmail.com                        phasing           
http://ccp4.github.io/dimple/                       ?   ? 
4 PHENIX      1.20.1_4487 ?               package 'Paul D. Adams'   PDAdams@lbl.gov                         refinement        
http://www.phenix-online.org/                       C++ ? 
5 PDB_EXTRACT 3.28        'Apr. 15, 2021' package PDB               deposit@deposit.rcsb.org                'data extraction' 
http://sw-tools.pdb.org/apps/PDB_EXTRACT/           C++ ? 
# 
_cell.volume             591929.668 
_cell.length_a           65.998 
_cell.length_b           89.786 
_cell.length_c           99.892 
_cell.angle_beta         90.000 
_cell.angle_gamma        90.000 
_cell.angle_alpha        90.000 
_cell.entry_id           7HAJ 
_cell.Z_PDB              8 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.Int_Tables_number                23 
_symmetry.space_group_name_H-M             'I 2 2 2' 
_symmetry.space_group_name_Hall            'I 2 2' 
_symmetry.entry_id                         7HAJ 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
# 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
_exptl.entry_id          7HAJ 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_Matthews      2.88 
_exptl_crystal.density_percent_sol   57.23 
_exptl_crystal.density_meas          ? 
_exptl_crystal.description           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.pH              8.5 
_exptl_crystal_grow.temp            277 
_exptl_crystal_grow.pdbx_details    '100mM Tris-HCl pH 8.5, 22% PEG4000, 200mM MgCl2' 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_diffrn.id                     1 
_diffrn.crystal_id             1 
_diffrn.ambient_temp           100 
_diffrn.ambient_temp_details   ? 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               PIXEL 
_diffrn_detector.type                   'DECTRIS EIGER2 S 9M' 
_diffrn_detector.pdbx_collection_date   2023-07-04 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.pdbx_scattering_type             x-ray 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.monochromator                    Si111 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.97918 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.pdbx_synchrotron_beamline   BL02U1 
_diffrn_source.type                        'SSRF BEAMLINE BL02U1' 
_diffrn_source.pdbx_wavelength_list        0.97918 
_diffrn_source.pdbx_synchrotron_site       SSRF 
_diffrn_source.pdbx_wavelength             ? 
# 
_reflns.entry_id                     7HAJ 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             33.390 
_reflns.d_resolution_high            1.570 
_reflns.number_obs                   37638 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         91.600 
_reflns.pdbx_Rmerge_I_obs            0.068 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        17.200 
_reflns.B_iso_Wilson_estimate        ? 
_reflns.pdbx_redundancy              7.900 
_reflns.pdbx_Rrim_I_all              0.073 
_reflns.pdbx_Rpim_I_all              0.025 
_reflns.pdbx_CC_half                 0.998 
_reflns.pdbx_netI_over_av_sigmaI     ? 
_reflns.pdbx_number_measured_all     296077 
_reflns.pdbx_scaling_rejects         421 
_reflns.pdbx_chi_squared             ? 
_reflns.Rmerge_F_all                 ? 
_reflns.Rmerge_F_obs                 ? 
_reflns.observed_criterion_F_max     ? 
_reflns.observed_criterion_F_min     ? 
_reflns.observed_criterion_I_max     ? 
_reflns.observed_criterion_I_min     ? 
_reflns.pdbx_d_res_high_opt          ? 
_reflns.pdbx_d_res_low_opt           ? 
_reflns.details                      ? 
# 
loop_
_reflns_shell.pdbx_diffrn_id 
_reflns_shell.pdbx_ordinal 
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_reflns_shell.number_measured_obs 
_reflns_shell.number_measured_all 
_reflns_shell.number_unique_obs 
_reflns_shell.pdbx_rejects 
_reflns_shell.Rmerge_I_obs 
_reflns_shell.meanI_over_sigI_obs 
_reflns_shell.pdbx_Rsym_value 
_reflns_shell.pdbx_chi_squared 
_reflns_shell.pdbx_redundancy 
_reflns_shell.percent_possible_obs 
_reflns_shell.pdbx_netI_over_sigmaI_obs 
_reflns_shell.number_possible 
_reflns_shell.number_unique_all 
_reflns_shell.Rmerge_F_all 
_reflns_shell.Rmerge_F_obs 
_reflns_shell.Rmerge_I_all 
_reflns_shell.meanI_over_sigI_all 
_reflns_shell.percent_possible_all 
_reflns_shell.pdbx_Rrim_I_all 
_reflns_shell.pdbx_Rpim_I_all 
_reflns_shell.pdbx_CC_half 
1 1 1.570 1.660  ? 32077 5484 ? 0.593 ? ? ? 5.800 ? 2.500  ? ? ? ? ? ? 91.600 0.646 0.246 0.819 
1 2 4.980 33.390 ? 9907  1171 ? 0.032 ? ? ? 8.500 ? 46.200 ? ? ? ? ? ? 84.600 0.034 0.011 0.999 
# 
_refine.entry_id                                 7HAJ 
_refine.pdbx_method_to_determine_struct          'FOURIER SYNTHESIS' 
_refine.ls_percent_reflns_R_free                 5.04 
_refine.pdbx_overall_phase_error                 18.5010 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_R_factor_obs                          0.1632 
_refine.B_iso_mean                               24.21 
_refine.ls_number_reflns_R_free                  1898 
_refine.ls_percent_reflns_obs                    90.88 
_refine.ls_R_factor_R_work                       0.1618 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_refine.ls_d_res_high                            1.57 
_refine.ls_number_reflns_obs                     37623 
_refine.pdbx_ls_sigma_F                          1.35 
_refine.ls_number_reflns_R_work                  35725 
_refine.ls_d_res_low                             29.73 
_refine.pdbx_stereochemistry_target_values       'GeoStd + Monomer Library + CDL v1.2' 
_refine.ls_R_factor_R_free                       0.1893 
_refine.overall_SU_ML                            0.1822 
_refine.pdbx_solvent_vdw_probe_radii             1.1000 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.solvent_model_param_ksol                 ? 
_refine.solvent_model_param_bsol                 ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.details                                  ? 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.overall_SU_B                             ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        1644 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         13 
_refine_hist.number_atoms_solvent             386 
_refine_hist.number_atoms_total               2043 
_refine_hist.d_res_high                       1.57 
_refine_hist.d_res_low                        29.73 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.type 
_refine_ls_restr.number 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
_refine_ls_restr.dev_ideal_target 
'X-RAY DIFFRACTION' f_bond_d           1684 0.0166 ? ? ? 
'X-RAY DIFFRACTION' f_angle_d          2271 1.4899 ? ? ? 
'X-RAY DIFFRACTION' f_chiral_restr     259  0.0870 ? ? ? 
'X-RAY DIFFRACTION' f_plane_restr      290  0.0118 ? ? ? 
'X-RAY DIFFRACTION' f_dihedral_angle_d 223  5.9812 ? ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.R_factor_R_free 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.R_factor_all 
'X-RAY DIFFRACTION' 1.57 1.61  2470 0.2481 89.08 0.2741 132 . . . . . 
'X-RAY DIFFRACTION' 1.61 1.66  2606 0.2269 93.08 0.2556 123 . . . . . 
'X-RAY DIFFRACTION' 1.66 1.71  2568 0.2116 93.66 0.2455 150 . . . . . 
'X-RAY DIFFRACTION' 1.71 1.76  2590 0.2043 93.34 0.2619 144 . . . . . 
'X-RAY DIFFRACTION' 1.76 1.82  2578 0.1832 92.70 0.2196 139 . . . . . 
'X-RAY DIFFRACTION' 1.82 1.90  2552 0.1738 92.58 0.2041 145 . . . . . 
'X-RAY DIFFRACTION' 1.90 1.98  2584 0.1714 92.07 0.1956 120 . . . . . 
'X-RAY DIFFRACTION' 1.98 2.09  2562 0.1726 91.81 0.2055 141 . . . . . 
'X-RAY DIFFRACTION' 2.09 2.22  2540 0.1500 90.86 0.1795 143 . . . . . 
'X-RAY DIFFRACTION' 2.22 2.39  2538 0.1571 90.84 0.1816 139 . . . . . 
'X-RAY DIFFRACTION' 2.39 2.63  2561 0.1608 90.56 0.1913 126 . . . . . 
'X-RAY DIFFRACTION' 2.63 3.01  2548 0.1564 89.41 0.1866 127 . . . . . 
'X-RAY DIFFRACTION' 3.01 3.79  2497 0.1426 88.16 0.1547 140 . . . . . 
'X-RAY DIFFRACTION' 3.79 29.73 2531 0.1477 84.77 0.1772 129 . . . . . 
# 
_struct.entry_id                  7HAJ 
_struct.title                     'PanDDA analysis group deposition -- Crystal structure of HSP90N in complex with PS-4122' 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_details        ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HAJ 
_struct_keywords.pdbx_keywords   CHAPERONE 
_struct_keywords.text            
'Crystallographic Fragment Screening; Fragment-Based Drug Discovery (FBDD); Heat shock protein 90 (HSP90), CHAPERONE' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    HS90A_HUMAN 
_struct_ref.pdbx_db_accession          P07900 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;DQPMEEEEVETFAFQAEIAQLMSLIINTFYSNKEIFLRELISNSSDALDKIRYESLTDPSKLDSGKELHINLIPNKQDRT
LTIVDTGIGMTKADLINNLGTIAKSGTKAFMEALQAGADISMIGQFGVGFYSAYLVAEKVTVITKHNDDEQYAWESSAGG
SFTVRTDTGEPMGRGTKVILHLKEDQTEYLEERRIKEIVKKHSQFIGYPITLFVEKERDKEVSDDEAE
;
_struct_ref.pdbx_align_begin           9 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              7HAJ 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 2 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 229 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             P07900 
_struct_ref_seq.db_align_beg                  9 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  236 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       9 
_struct_ref_seq.pdbx_auth_seq_align_end       236 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 7HAJ MET A 1   ? UNP P07900 ? ? 'initiating methionine' 8   1 
1 7HAJ LEU A 230 ? UNP P07900 ? ? 'expression tag'        237 2 
1 7HAJ GLU A 231 ? UNP P07900 ? ? 'expression tag'        238 3 
1 7HAJ HIS A 232 ? UNP P07900 ? ? 'expression tag'        239 4 
1 7HAJ HIS A 233 ? UNP P07900 ? ? 'expression tag'        240 5 
1 7HAJ HIS A 234 ? UNP P07900 ? ? 'expression tag'        241 6 
1 7HAJ HIS A 235 ? UNP P07900 ? ? 'expression tag'        242 7 
1 7HAJ HIS A 236 ? UNP P07900 ? ? 'expression tag'        243 8 
1 7HAJ HIS A 237 ? UNP P07900 ? ? 'expression tag'        244 9 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 AA1 GLN A 16  ? THR A 29  ? GLN A 23  THR A 36  1 ? 14 
HELX_P HELX_P2 AA2 GLU A 35  ? LEU A 57  ? GLU A 42  LEU A 64  1 ? 23 
HELX_P HELX_P3 AA3 THR A 58  ? ASP A 64  ? THR A 65  ASP A 71  5 ? 7  
HELX_P HELX_P4 AA4 THR A 92  ? ASN A 98  ? THR A 99  ASN A 105 1 ? 7  
HELX_P HELX_P5 AA5 ILE A 103 ? ALA A 117 ? ILE A 110 ALA A 124 1 ? 15 
HELX_P HELX_P6 AA6 ASP A 120 ? GLY A 128 ? ASP A 127 GLY A 135 5 ? 9  
HELX_P HELX_P7 AA7 VAL A 129 ? LEU A 136 ? VAL A 136 LEU A 143 5 ? 8  
HELX_P HELX_P8 AA8 GLU A 185 ? LEU A 191 ? GLU A 192 LEU A 198 5 ? 7  
HELX_P HELX_P9 AA9 GLU A 192 ? SER A 204 ? GLU A 199 SER A 211 1 ? 13 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
_struct_sheet.id               AA1 
_struct_sheet.type             ? 
_struct_sheet.number_strands   8 
_struct_sheet.details          ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA1 5 6 ? anti-parallel 
AA1 6 7 ? anti-parallel 
AA1 7 8 ? 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 GLU A 11  ? ALA A 14  ? GLU A 18  ALA A 21  
AA1 2 SER A 162 ? THR A 167 ? SER A 169 THR A 174 
AA1 3 TYR A 153 ? SER A 157 ? TYR A 160 SER A 164 
AA1 4 ALA A 138 ? LYS A 146 ? ALA A 145 LYS A 153 
AA1 5 GLY A 176 ? LEU A 183 ? GLY A 183 LEU A 190 
AA1 6 THR A 81  ? ASP A 86  ? THR A 88  ASP A 93  
AA1 7 ILE A 71  ? ASN A 76  ? ILE A 78  ASN A 83  
AA1 8 ILE A 211 ? LEU A 213 ? ILE A 218 LEU A 220 
# 
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 PHE A 13  ? N PHE A 20  O PHE A 163 ? O PHE A 170 
AA1 2 3 O ARG A 166 ? O ARG A 173 N ALA A 154 ? N ALA A 161 
AA1 3 4 O TRP A 155 ? O TRP A 162 N VAL A 143 ? N VAL A 150 
AA1 4 5 N THR A 142 ? N THR A 149 O ILE A 180 ? O ILE A 187 
AA1 5 6 O LEU A 181 ? O LEU A 188 N LEU A 82  ? N LEU A 89  
AA1 6 7 O THR A 83  ? O THR A 90  N ILE A 74  ? N ILE A 81  
AA1 7 8 N LEU A 73  ? N LEU A 80  O THR A 212 ? O THR A 219 
# 
_pdbx_entry_details.entry_id                   7HAJ 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1  1 O A HOH 577 ? ? O A HOH 737 ? ? 1.88 
2  1 O A HOH 519 ? ? O A HOH 583 ? ? 1.93 
3  1 O A HOH 631 ? ? O A HOH 647 ? ? 1.97 
4  1 O A HOH 448 ? ? O A HOH 694 ? ? 1.98 
5  1 O A HOH 429 ? ? O A HOH 595 ? ? 1.98 
6  1 O A HOH 489 ? ? O A HOH 634 ? ? 2.01 
7  1 O A HOH 639 ? ? O A HOH 730 ? ? 2.02 
8  1 O A HOH 564 ? ? O A HOH 581 ? ? 2.09 
9  1 O A HOH 413 ? ? O A HOH 664 ? ? 2.09 
10 1 O A HOH 569 ? ? O A HOH 696 ? ? 2.10 
11 1 O A HOH 619 ? ? O A HOH 733 ? ? 2.11 
12 1 O A HOH 521 ? ? O A HOH 700 ? ? 2.11 
13 1 O A HOH 556 ? ? O A HOH 731 ? ? 2.12 
14 1 O A HOH 538 ? ? O A HOH 689 ? ? 2.13 
15 1 O A HOH 714 ? ? O A HOH 777 ? ? 2.13 
16 1 O A HOH 575 ? ? O A HOH 631 ? ? 2.14 
17 1 O A HOH 438 ? ? O A HOH 679 ? ? 2.15 
18 1 O A HOH 436 ? ? O A HOH 672 ? ? 2.18 
19 1 O A HOH 722 ? ? O A HOH 742 ? ? 2.19 
# 
loop_
_pdbx_validate_symm_contact.id 
_pdbx_validate_symm_contact.PDB_model_num 
_pdbx_validate_symm_contact.auth_atom_id_1 
_pdbx_validate_symm_contact.auth_asym_id_1 
_pdbx_validate_symm_contact.auth_comp_id_1 
_pdbx_validate_symm_contact.auth_seq_id_1 
_pdbx_validate_symm_contact.PDB_ins_code_1 
_pdbx_validate_symm_contact.label_alt_id_1 
_pdbx_validate_symm_contact.site_symmetry_1 
_pdbx_validate_symm_contact.auth_atom_id_2 
_pdbx_validate_symm_contact.auth_asym_id_2 
_pdbx_validate_symm_contact.auth_comp_id_2 
_pdbx_validate_symm_contact.auth_seq_id_2 
_pdbx_validate_symm_contact.PDB_ins_code_2 
_pdbx_validate_symm_contact.label_alt_id_2 
_pdbx_validate_symm_contact.site_symmetry_2 
_pdbx_validate_symm_contact.dist 
1 1 O A HOH 647 ? ? 1_555 O A HOH 687 ? ? 8_444 1.93 
2 1 O A HOH 759 ? ? 1_555 O A HOH 768 ? ? 3_555 2.06 
3 1 O A HOH 676 ? ? 1_555 O A HOH 723 ? ? 8_444 2.11 
4 1 O A HOH 666 ? ? 1_555 O A HOH 686 ? ? 8_544 2.12 
5 1 O A HOH 682 ? ? 1_555 O A HOH 754 ? ? 2_555 2.18 
# 
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 TYR A 38  ? ? -163.55 114.23  
2 1 ASP A 66  ? ? -150.06 86.62   
3 1 THR A 94  ? ? -106.07 40.32   
4 1 ALA A 166 ? ? 65.63   -142.48 
5 1 ARG A 182 ? ? -170.80 138.79  
# 
_pdbx_struct_special_symmetry.id              1 
_pdbx_struct_special_symmetry.PDB_model_num   1 
_pdbx_struct_special_symmetry.auth_asym_id    A 
_pdbx_struct_special_symmetry.auth_comp_id    HOH 
_pdbx_struct_special_symmetry.auth_seq_id     745 
_pdbx_struct_special_symmetry.PDB_ins_code    ? 
_pdbx_struct_special_symmetry.label_asym_id   C 
_pdbx_struct_special_symmetry.label_comp_id   HOH 
_pdbx_struct_special_symmetry.label_seq_id    . 
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z               
2 x,-y,-z             
3 -x,y,-z             
4 -x,-y,z             
5 x+1/2,y+1/2,z+1/2   
6 x+1/2,-y+1/2,-z+1/2 
7 -x+1/2,y+1/2,-z+1/2 
8 -x+1/2,-y+1/2,z+1/2 
# 
loop_
_pdbx_refine_tls.id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.pdbx_refine_id 
_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[2][2] 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][3] 
1  ? 'X-RAY DIFFRACTION' refined 12.362142703   -17.8707444437 -18.6559395031 0.116045568986 0.117049319055  0.149165093802 
0.00864825498209   -0.0197108383515  -0.014211480805   2.4786916775  1.14111985896 7.28252292948  -1.1465327767   -2.52463018859  
0.657739349132  0.0480639314482  -0.121329566848  -0.0102005344479 0.0671484162033  -0.0494867377495 -0.0476334467536 
0.218477715881   0.101565102027   -0.055315524981   
2  ? 'X-RAY DIFFRACTION' refined -5.20616831658 -6.40931119292 -20.7744108199 0.123955275288 0.118938549766  0.159674893295 
-0.00540342222212  -0.0075580245277  -0.0303888895986  1.91560354727 6.14377446901 7.67032597828  -2.53268215979  2.76418380881   
-5.93597876329  0.00539051811769 0.0310349748786  0.0795752317325  0.0532963590559  -0.0420203805477 0.110317513459   
-0.206233229822  0.0732911790547  0.0449109197319   
3  ? 'X-RAY DIFFRACTION' refined -13.6228949071 -10.904871375  -27.7898264952 0.135921831211 0.155705344608  0.20288114299  
-9.34696846519e-05 -0.0731665210402  -0.016112467892   1.43085549978 5.01246863759 7.74346801677  -1.15133873591  1.00865985933   
-5.43516641123  0.044598008197   0.147923633346   0.0651179034692  -0.299251615901  0.200862360355   0.525663729836   
-0.0441928144803 -0.3310671426    -0.314317195778   
4  ? 'X-RAY DIFFRACTION' refined -5.97450624412 -19.8615519921 -21.8738179017 0.130394523147 0.0915765939721 0.162792046893 
-0.00702968271686  -0.02599926647    -0.0292746553609  1.56415570867 3.87873314205 5.52156623663  0.0166732765532 -0.70354791057  
-3.62169309642  -0.0378169697592 -0.0137383270229 -0.158141702311  -0.120046986354  0.0881599963893  0.143567432522   
0.273072313983   -0.0578596408132 -0.0678437273719  
5  ? 'X-RAY DIFFRACTION' refined 6.96717850906  -10.9291167853 -29.6066466531 0.136374247774 0.132117280497  0.17416290155  
0.00215614985062   0.0121274117733   0.00138888069439  4.98160066383 6.00315653644 9.97404325304  3.92086412175   6.19498441902   
6.14444464986   -0.0367976406456 0.110327127539   0.205704432073   -0.172552911863  0.00286654737375 0.00695386097397 
-0.154510743731  0.248396163529   0.0526980083679   
6  ? 'X-RAY DIFFRACTION' refined 12.2873162522  -6.01538253504 -12.4321864189 0.170699207445 0.261722556267  0.230255198658 
-0.045009796773    -0.0211982638027  -0.0475368801987  2.81539268376 6.33326141252 6.61116186574  -0.399448777968 0.434679127408  
-1.2950651185   0.151875165442   -0.642283771238  0.365690565336   0.386557628698   -0.250778813996  -0.414833854811  
-0.311685951233  0.801763127552   0.107012631208    
7  ? 'X-RAY DIFFRACTION' refined 2.19871226308  -18.3963785264 -25.7754394314 0.113409781744 0.0894702883741 0.122989385227 
-0.00465854053682  0.00955533749333  -0.0136180716508  3.65112093836 1.64118835684 3.49886091023  -0.859408358048 1.81699325079   
-0.521140120037 0.0769040384142  0.159741612896   -0.0460922763554 -0.106503284     0.0047440153198  0.00783970217248 
0.0687605543633  0.183668617119   -0.0842627548271  
8  ? 'X-RAY DIFFRACTION' refined -1.89598078258 -21.0372453225 -32.529096578  0.19513485907  0.220166414452  0.243298995788 
-0.00523265738972  -0.0319526373895  -0.0544789280957  3.15092848718 1.23402765763 0.116402097598 -1.44321769588  -0.44135597305  
0.113984084097  -0.0765633208059 0.323864155784   -0.515811003713  -0.0942257503198 0.00860324759388 0.330463564303   
0.120190329023   -0.102185803025  -0.00720304693393 
9  ? 'X-RAY DIFFRACTION' refined -5.52172942879 -20.3323071832 -10.3983764123 0.113628263644 0.138756309861  0.142800419713 
-0.0269529142529   -0.0180191290998  0.0129985144449   2.34978984502 2.19335470208 3.46532281103  -0.698321044981 -0.423400890292 
-0.340294161148 -0.0674827953683 -0.293966378167  -0.158126939113  0.168087274218   0.0546847920617  0.0645318964437  
0.31463773714    -0.028876215732  0.0191776770951   
10 ? 'X-RAY DIFFRACTION' refined -13.9574910917 -13.5733666609 -14.7148040232 0.106990861591 0.139292941173  0.111823384346 
-0.00122626446121  -0.00607036846962 -0.00795871738487 4.50241959644 1.5336712232  3.65052878669  1.53071109343   -0.17536585304  
-0.373634194411 0.189100541272   -0.322683971009  0.00849368871675 0.447188863068   -0.219612394685  0.0445524269713  
-0.0469488544006 -0.16521964301   0.041757284897    
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
1  1  'X-RAY DIFFRACTION' A 16  A 1   A 40  A 25  . 
;chain 'A' and (resid 16 through 40 )
;
2  2  'X-RAY DIFFRACTION' A 41  A 26  A 65  A 50  . 
;chain 'A' and (resid 41 through 65 )
;
3  3  'X-RAY DIFFRACTION' A 66  A 51  A 83  A 68  . 
;chain 'A' and (resid 66 through 83 )
;
4  4  'X-RAY DIFFRACTION' A 84  A 69  A 99  A 84  . 
;chain 'A' and (resid 84 through 99 )
;
5  5  'X-RAY DIFFRACTION' A 100 A 85  A 110 A 95  . 
;chain 'A' and (resid 100 through 110 )
;
6  6  'X-RAY DIFFRACTION' A 111 A 96  A 136 A 121 . 
;chain 'A' and (resid 111 through 136 )
;
7  7  'X-RAY DIFFRACTION' A 137 A 122 A 168 A 153 . 
;chain 'A' and (resid 137 through 168 )
;
8  8  'X-RAY DIFFRACTION' A 169 A 154 A 182 A 167 . 
;chain 'A' and (resid 169 through 182 )
;
9  9  'X-RAY DIFFRACTION' A 183 A 168 A 210 A 195 . 
;chain 'A' and (resid 183 through 210 )
;
10 10 'X-RAY DIFFRACTION' A 211 A 196 A 224 A 209 . 
;chain 'A' and (resid 211 through 224 )
;
# 
_pdbx_distant_solvent_atoms.id                                1 
_pdbx_distant_solvent_atoms.PDB_model_num                     1 
_pdbx_distant_solvent_atoms.auth_atom_id                      O 
_pdbx_distant_solvent_atoms.label_alt_id                      ? 
_pdbx_distant_solvent_atoms.auth_asym_id                      A 
_pdbx_distant_solvent_atoms.auth_comp_id                      HOH 
_pdbx_distant_solvent_atoms.auth_seq_id                       786 
_pdbx_distant_solvent_atoms.PDB_ins_code                      ? 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance   6.65 
_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 MET 8   ? A MET 1   
2  1 Y 1 A ASP 9   ? A ASP 2   
3  1 Y 1 A GLN 10  ? A GLN 3   
4  1 Y 1 A PRO 11  ? A PRO 4   
5  1 Y 1 A MET 12  ? A MET 5   
6  1 Y 1 A GLU 13  ? A GLU 6   
7  1 Y 1 A GLU 14  ? A GLU 7   
8  1 Y 1 A GLU 15  ? A GLU 8   
9  1 Y 1 A GLU 225 ? A GLU 218 
10 1 Y 1 A ARG 226 ? A ARG 219 
11 1 Y 1 A ASP 227 ? A ASP 220 
12 1 Y 1 A LYS 228 ? A LYS 221 
13 1 Y 1 A GLU 229 ? A GLU 222 
14 1 Y 1 A VAL 230 ? A VAL 223 
15 1 Y 1 A SER 231 ? A SER 224 
16 1 Y 1 A ASP 232 ? A ASP 225 
17 1 Y 1 A ASP 233 ? A ASP 226 
18 1 Y 1 A GLU 234 ? A GLU 227 
19 1 Y 1 A ALA 235 ? A ALA 228 
20 1 Y 1 A GLU 236 ? A GLU 229 
21 1 Y 1 A LEU 237 ? A LEU 230 
22 1 Y 1 A GLU 238 ? A GLU 231 
23 1 Y 1 A HIS 239 ? A HIS 232 
24 1 Y 1 A HIS 240 ? A HIS 233 
25 1 Y 1 A HIS 241 ? A HIS 234 
26 1 Y 1 A HIS 242 ? A HIS 235 
27 1 Y 1 A HIS 243 ? A HIS 236 
28 1 Y 1 A HIS 244 ? A HIS 237 
# 
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 
A1AXE C1   C N N 1   
A1AXE C10  C N N 2   
A1AXE C2   C Y N 3   
A1AXE C4   C Y N 4   
A1AXE C5   C Y N 5   
A1AXE C6   C Y N 6   
A1AXE C7   C Y N 7   
A1AXE C3   C Y N 8   
A1AXE C8   C Y N 9   
A1AXE C9   C Y N 10  
A1AXE N1   N Y N 11  
A1AXE O1   O N N 12  
A1AXE O2   O N N 13  
A1AXE H1   H N N 14  
A1AXE H2   H N N 15  
A1AXE H3   H N N 16  
A1AXE H4   H N N 17  
A1AXE H6   H N N 18  
A1AXE H7   H N N 19  
A1AXE H5   H N N 20  
A1AXE H8   H N N 21  
A1AXE H9   H N N 22  
ALA   N    N N N 23  
ALA   CA   C N S 24  
ALA   C    C N N 25  
ALA   O    O N N 26  
ALA   CB   C N N 27  
ALA   OXT  O N N 28  
ALA   H    H N N 29  
ALA   H2   H N N 30  
ALA   HA   H N N 31  
ALA   HB1  H N N 32  
ALA   HB2  H N N 33  
ALA   HB3  H N N 34  
ALA   HXT  H N N 35  
ARG   N    N N N 36  
ARG   CA   C N S 37  
ARG   C    C N N 38  
ARG   O    O N N 39  
ARG   CB   C N N 40  
ARG   CG   C N N 41  
ARG   CD   C N N 42  
ARG   NE   N N N 43  
ARG   CZ   C N N 44  
ARG   NH1  N N N 45  
ARG   NH2  N N N 46  
ARG   OXT  O N N 47  
ARG   H    H N N 48  
ARG   H2   H N N 49  
ARG   HA   H N N 50  
ARG   HB2  H N N 51  
ARG   HB3  H N N 52  
ARG   HG2  H N N 53  
ARG   HG3  H N N 54  
ARG   HD2  H N N 55  
ARG   HD3  H N N 56  
ARG   HE   H N N 57  
ARG   HH11 H N N 58  
ARG   HH12 H N N 59  
ARG   HH21 H N N 60  
ARG   HH22 H N N 61  
ARG   HXT  H N N 62  
ASN   N    N N N 63  
ASN   CA   C N S 64  
ASN   C    C N N 65  
ASN   O    O N N 66  
ASN   CB   C N N 67  
ASN   CG   C N N 68  
ASN   OD1  O N N 69  
ASN   ND2  N N N 70  
ASN   OXT  O N N 71  
ASN   H    H N N 72  
ASN   H2   H N N 73  
ASN   HA   H N N 74  
ASN   HB2  H N N 75  
ASN   HB3  H N N 76  
ASN   HD21 H N N 77  
ASN   HD22 H N N 78  
ASN   HXT  H N N 79  
ASP   N    N N N 80  
ASP   CA   C N S 81  
ASP   C    C N N 82  
ASP   O    O N N 83  
ASP   CB   C N N 84  
ASP   CG   C N N 85  
ASP   OD1  O N N 86  
ASP   OD2  O N N 87  
ASP   OXT  O N N 88  
ASP   H    H N N 89  
ASP   H2   H N N 90  
ASP   HA   H N N 91  
ASP   HB2  H N N 92  
ASP   HB3  H N N 93  
ASP   HD2  H N N 94  
ASP   HXT  H N N 95  
GLN   N    N N N 96  
GLN   CA   C N S 97  
GLN   C    C N N 98  
GLN   O    O N N 99  
GLN   CB   C N N 100 
GLN   CG   C N N 101 
GLN   CD   C N N 102 
GLN   OE1  O N N 103 
GLN   NE2  N N N 104 
GLN   OXT  O N N 105 
GLN   H    H N N 106 
GLN   H2   H N N 107 
GLN   HA   H N N 108 
GLN   HB2  H N N 109 
GLN   HB3  H N N 110 
GLN   HG2  H N N 111 
GLN   HG3  H N N 112 
GLN   HE21 H N N 113 
GLN   HE22 H N N 114 
GLN   HXT  H N N 115 
GLU   N    N N N 116 
GLU   CA   C N S 117 
GLU   C    C N N 118 
GLU   O    O N N 119 
GLU   CB   C N N 120 
GLU   CG   C N N 121 
GLU   CD   C N N 122 
GLU   OE1  O N N 123 
GLU   OE2  O N N 124 
GLU   OXT  O N N 125 
GLU   H    H N N 126 
GLU   H2   H N N 127 
GLU   HA   H N N 128 
GLU   HB2  H N N 129 
GLU   HB3  H N N 130 
GLU   HG2  H N N 131 
GLU   HG3  H N N 132 
GLU   HE2  H N N 133 
GLU   HXT  H N N 134 
GLY   N    N N N 135 
GLY   CA   C N N 136 
GLY   C    C N N 137 
GLY   O    O N N 138 
GLY   OXT  O N N 139 
GLY   H    H N N 140 
GLY   H2   H N N 141 
GLY   HA2  H N N 142 
GLY   HA3  H N N 143 
GLY   HXT  H N N 144 
HIS   N    N N N 145 
HIS   CA   C N S 146 
HIS   C    C N N 147 
HIS   O    O N N 148 
HIS   CB   C N N 149 
HIS   CG   C Y N 150 
HIS   ND1  N Y N 151 
HIS   CD2  C Y N 152 
HIS   CE1  C Y N 153 
HIS   NE2  N Y N 154 
HIS   OXT  O N N 155 
HIS   H    H N N 156 
HIS   H2   H N N 157 
HIS   HA   H N N 158 
HIS   HB2  H N N 159 
HIS   HB3  H N N 160 
HIS   HD1  H N N 161 
HIS   HD2  H N N 162 
HIS   HE1  H N N 163 
HIS   HE2  H N N 164 
HIS   HXT  H N N 165 
HOH   O    O N N 166 
HOH   H1   H N N 167 
HOH   H2   H N N 168 
ILE   N    N N N 169 
ILE   CA   C N S 170 
ILE   C    C N N 171 
ILE   O    O N N 172 
ILE   CB   C N S 173 
ILE   CG1  C N N 174 
ILE   CG2  C N N 175 
ILE   CD1  C N N 176 
ILE   OXT  O N N 177 
ILE   H    H N N 178 
ILE   H2   H N N 179 
ILE   HA   H N N 180 
ILE   HB   H N N 181 
ILE   HG12 H N N 182 
ILE   HG13 H N N 183 
ILE   HG21 H N N 184 
ILE   HG22 H N N 185 
ILE   HG23 H N N 186 
ILE   HD11 H N N 187 
ILE   HD12 H N N 188 
ILE   HD13 H N N 189 
ILE   HXT  H N N 190 
LEU   N    N N N 191 
LEU   CA   C N S 192 
LEU   C    C N N 193 
LEU   O    O N N 194 
LEU   CB   C N N 195 
LEU   CG   C N N 196 
LEU   CD1  C N N 197 
LEU   CD2  C N N 198 
LEU   OXT  O N N 199 
LEU   H    H N N 200 
LEU   H2   H N N 201 
LEU   HA   H N N 202 
LEU   HB2  H N N 203 
LEU   HB3  H N N 204 
LEU   HG   H N N 205 
LEU   HD11 H N N 206 
LEU   HD12 H N N 207 
LEU   HD13 H N N 208 
LEU   HD21 H N N 209 
LEU   HD22 H N N 210 
LEU   HD23 H N N 211 
LEU   HXT  H N N 212 
LYS   N    N N N 213 
LYS   CA   C N S 214 
LYS   C    C N N 215 
LYS   O    O N N 216 
LYS   CB   C N N 217 
LYS   CG   C N N 218 
LYS   CD   C N N 219 
LYS   CE   C N N 220 
LYS   NZ   N N N 221 
LYS   OXT  O N N 222 
LYS   H    H N N 223 
LYS   H2   H N N 224 
LYS   HA   H N N 225 
LYS   HB2  H N N 226 
LYS   HB3  H N N 227 
LYS   HG2  H N N 228 
LYS   HG3  H N N 229 
LYS   HD2  H N N 230 
LYS   HD3  H N N 231 
LYS   HE2  H N N 232 
LYS   HE3  H N N 233 
LYS   HZ1  H N N 234 
LYS   HZ2  H N N 235 
LYS   HZ3  H N N 236 
LYS   HXT  H N N 237 
MET   N    N N N 238 
MET   CA   C N S 239 
MET   C    C N N 240 
MET   O    O N N 241 
MET   CB   C N N 242 
MET   CG   C N N 243 
MET   SD   S N N 244 
MET   CE   C N N 245 
MET   OXT  O N N 246 
MET   H    H N N 247 
MET   H2   H N N 248 
MET   HA   H N N 249 
MET   HB2  H N N 250 
MET   HB3  H N N 251 
MET   HG2  H N N 252 
MET   HG3  H N N 253 
MET   HE1  H N N 254 
MET   HE2  H N N 255 
MET   HE3  H N N 256 
MET   HXT  H N N 257 
PHE   N    N N N 258 
PHE   CA   C N S 259 
PHE   C    C N N 260 
PHE   O    O N N 261 
PHE   CB   C N N 262 
PHE   CG   C Y N 263 
PHE   CD1  C Y N 264 
PHE   CD2  C Y N 265 
PHE   CE1  C Y N 266 
PHE   CE2  C Y N 267 
PHE   CZ   C Y N 268 
PHE   OXT  O N N 269 
PHE   H    H N N 270 
PHE   H2   H N N 271 
PHE   HA   H N N 272 
PHE   HB2  H N N 273 
PHE   HB3  H N N 274 
PHE   HD1  H N N 275 
PHE   HD2  H N N 276 
PHE   HE1  H N N 277 
PHE   HE2  H N N 278 
PHE   HZ   H N N 279 
PHE   HXT  H N N 280 
PRO   N    N N N 281 
PRO   CA   C N S 282 
PRO   C    C N N 283 
PRO   O    O N N 284 
PRO   CB   C N N 285 
PRO   CG   C N N 286 
PRO   CD   C N N 287 
PRO   OXT  O N N 288 
PRO   H    H N N 289 
PRO   HA   H N N 290 
PRO   HB2  H N N 291 
PRO   HB3  H N N 292 
PRO   HG2  H N N 293 
PRO   HG3  H N N 294 
PRO   HD2  H N N 295 
PRO   HD3  H N N 296 
PRO   HXT  H N N 297 
SER   N    N N N 298 
SER   CA   C N S 299 
SER   C    C N N 300 
SER   O    O N N 301 
SER   CB   C N N 302 
SER   OG   O N N 303 
SER   OXT  O N N 304 
SER   H    H N N 305 
SER   H2   H N N 306 
SER   HA   H N N 307 
SER   HB2  H N N 308 
SER   HB3  H N N 309 
SER   HG   H N N 310 
SER   HXT  H N N 311 
THR   N    N N N 312 
THR   CA   C N S 313 
THR   C    C N N 314 
THR   O    O N N 315 
THR   CB   C N R 316 
THR   OG1  O N N 317 
THR   CG2  C N N 318 
THR   OXT  O N N 319 
THR   H    H N N 320 
THR   H2   H N N 321 
THR   HA   H N N 322 
THR   HB   H N N 323 
THR   HG1  H N N 324 
THR   HG21 H N N 325 
THR   HG22 H N N 326 
THR   HG23 H N N 327 
THR   HXT  H N N 328 
TRP   N    N N N 329 
TRP   CA   C N S 330 
TRP   C    C N N 331 
TRP   O    O N N 332 
TRP   CB   C N N 333 
TRP   CG   C Y N 334 
TRP   CD1  C Y N 335 
TRP   CD2  C Y N 336 
TRP   NE1  N Y N 337 
TRP   CE2  C Y N 338 
TRP   CE3  C Y N 339 
TRP   CZ2  C Y N 340 
TRP   CZ3  C Y N 341 
TRP   CH2  C Y N 342 
TRP   OXT  O N N 343 
TRP   H    H N N 344 
TRP   H2   H N N 345 
TRP   HA   H N N 346 
TRP   HB2  H N N 347 
TRP   HB3  H N N 348 
TRP   HD1  H N N 349 
TRP   HE1  H N N 350 
TRP   HE3  H N N 351 
TRP   HZ2  H N N 352 
TRP   HZ3  H N N 353 
TRP   HH2  H N N 354 
TRP   HXT  H N N 355 
TYR   N    N N N 356 
TYR   CA   C N S 357 
TYR   C    C N N 358 
TYR   O    O N N 359 
TYR   CB   C N N 360 
TYR   CG   C Y N 361 
TYR   CD1  C Y N 362 
TYR   CD2  C Y N 363 
TYR   CE1  C Y N 364 
TYR   CE2  C Y N 365 
TYR   CZ   C Y N 366 
TYR   OH   O N N 367 
TYR   OXT  O N N 368 
TYR   H    H N N 369 
TYR   H2   H N N 370 
TYR   HA   H N N 371 
TYR   HB2  H N N 372 
TYR   HB3  H N N 373 
TYR   HD1  H N N 374 
TYR   HD2  H N N 375 
TYR   HE1  H N N 376 
TYR   HE2  H N N 377 
TYR   HH   H N N 378 
TYR   HXT  H N N 379 
VAL   N    N N N 380 
VAL   CA   C N S 381 
VAL   C    C N N 382 
VAL   O    O N N 383 
VAL   CB   C N N 384 
VAL   CG1  C N N 385 
VAL   CG2  C N N 386 
VAL   OXT  O N N 387 
VAL   H    H N N 388 
VAL   H2   H N N 389 
VAL   HA   H N N 390 
VAL   HB   H N N 391 
VAL   HG11 H N N 392 
VAL   HG12 H N N 393 
VAL   HG13 H N N 394 
VAL   HG21 H N N 395 
VAL   HG22 H N N 396 
VAL   HG23 H N N 397 
VAL   HXT  H N N 398 
# 
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 
A1AXE C1  N1   sing N N 1   
A1AXE N1  C2   sing Y N 2   
A1AXE C2  C3   doub Y N 3   
A1AXE C3  C4   sing Y N 4   
A1AXE C4  C5   doub Y N 5   
A1AXE C5  C6   sing Y N 6   
A1AXE C6  C7   doub Y N 7   
A1AXE C7  C8   sing Y N 8   
A1AXE C8  C9   doub Y N 9   
A1AXE C7  C10  sing N N 10  
A1AXE C10 O1   sing N N 11  
A1AXE C10 O2   doub N N 12  
A1AXE N1  C9   sing Y N 13  
A1AXE C4  C9   sing Y N 14  
A1AXE C1  H1   sing N N 15  
A1AXE C1  H2   sing N N 16  
A1AXE C1  H3   sing N N 17  
A1AXE C2  H4   sing N N 18  
A1AXE C5  H6   sing N N 19  
A1AXE C6  H7   sing N N 20  
A1AXE C3  H5   sing N N 21  
A1AXE C8  H8   sing N N 22  
A1AXE O1  H9   sing N N 23  
ALA   N   CA   sing N N 24  
ALA   N   H    sing N N 25  
ALA   N   H2   sing N N 26  
ALA   CA  C    sing N N 27  
ALA   CA  CB   sing N N 28  
ALA   CA  HA   sing N N 29  
ALA   C   O    doub N N 30  
ALA   C   OXT  sing N N 31  
ALA   CB  HB1  sing N N 32  
ALA   CB  HB2  sing N N 33  
ALA   CB  HB3  sing N N 34  
ALA   OXT HXT  sing N N 35  
ARG   N   CA   sing N N 36  
ARG   N   H    sing N N 37  
ARG   N   H2   sing N N 38  
ARG   CA  C    sing N N 39  
ARG   CA  CB   sing N N 40  
ARG   CA  HA   sing N N 41  
ARG   C   O    doub N N 42  
ARG   C   OXT  sing N N 43  
ARG   CB  CG   sing N N 44  
ARG   CB  HB2  sing N N 45  
ARG   CB  HB3  sing N N 46  
ARG   CG  CD   sing N N 47  
ARG   CG  HG2  sing N N 48  
ARG   CG  HG3  sing N N 49  
ARG   CD  NE   sing N N 50  
ARG   CD  HD2  sing N N 51  
ARG   CD  HD3  sing N N 52  
ARG   NE  CZ   sing N N 53  
ARG   NE  HE   sing N N 54  
ARG   CZ  NH1  sing N N 55  
ARG   CZ  NH2  doub N N 56  
ARG   NH1 HH11 sing N N 57  
ARG   NH1 HH12 sing N N 58  
ARG   NH2 HH21 sing N N 59  
ARG   NH2 HH22 sing N N 60  
ARG   OXT HXT  sing N N 61  
ASN   N   CA   sing N N 62  
ASN   N   H    sing N N 63  
ASN   N   H2   sing N N 64  
ASN   CA  C    sing N N 65  
ASN   CA  CB   sing N N 66  
ASN   CA  HA   sing N N 67  
ASN   C   O    doub N N 68  
ASN   C   OXT  sing N N 69  
ASN   CB  CG   sing N N 70  
ASN   CB  HB2  sing N N 71  
ASN   CB  HB3  sing N N 72  
ASN   CG  OD1  doub N N 73  
ASN   CG  ND2  sing N N 74  
ASN   ND2 HD21 sing N N 75  
ASN   ND2 HD22 sing N N 76  
ASN   OXT HXT  sing N N 77  
ASP   N   CA   sing N N 78  
ASP   N   H    sing N N 79  
ASP   N   H2   sing N N 80  
ASP   CA  C    sing N N 81  
ASP   CA  CB   sing N N 82  
ASP   CA  HA   sing N N 83  
ASP   C   O    doub N N 84  
ASP   C   OXT  sing N N 85  
ASP   CB  CG   sing N N 86  
ASP   CB  HB2  sing N N 87  
ASP   CB  HB3  sing N N 88  
ASP   CG  OD1  doub N N 89  
ASP   CG  OD2  sing N N 90  
ASP   OD2 HD2  sing N N 91  
ASP   OXT HXT  sing N N 92  
GLN   N   CA   sing N N 93  
GLN   N   H    sing N N 94  
GLN   N   H2   sing N N 95  
GLN   CA  C    sing N N 96  
GLN   CA  CB   sing N N 97  
GLN   CA  HA   sing N N 98  
GLN   C   O    doub N N 99  
GLN   C   OXT  sing N N 100 
GLN   CB  CG   sing N N 101 
GLN   CB  HB2  sing N N 102 
GLN   CB  HB3  sing N N 103 
GLN   CG  CD   sing N N 104 
GLN   CG  HG2  sing N N 105 
GLN   CG  HG3  sing N N 106 
GLN   CD  OE1  doub N N 107 
GLN   CD  NE2  sing N N 108 
GLN   NE2 HE21 sing N N 109 
GLN   NE2 HE22 sing N N 110 
GLN   OXT HXT  sing N N 111 
GLU   N   CA   sing N N 112 
GLU   N   H    sing N N 113 
GLU   N   H2   sing N N 114 
GLU   CA  C    sing N N 115 
GLU   CA  CB   sing N N 116 
GLU   CA  HA   sing N N 117 
GLU   C   O    doub N N 118 
GLU   C   OXT  sing N N 119 
GLU   CB  CG   sing N N 120 
GLU   CB  HB2  sing N N 121 
GLU   CB  HB3  sing N N 122 
GLU   CG  CD   sing N N 123 
GLU   CG  HG2  sing N N 124 
GLU   CG  HG3  sing N N 125 
GLU   CD  OE1  doub N N 126 
GLU   CD  OE2  sing N N 127 
GLU   OE2 HE2  sing N N 128 
GLU   OXT HXT  sing N N 129 
GLY   N   CA   sing N N 130 
GLY   N   H    sing N N 131 
GLY   N   H2   sing N N 132 
GLY   CA  C    sing N N 133 
GLY   CA  HA2  sing N N 134 
GLY   CA  HA3  sing N N 135 
GLY   C   O    doub N N 136 
GLY   C   OXT  sing N N 137 
GLY   OXT HXT  sing N N 138 
HIS   N   CA   sing N N 139 
HIS   N   H    sing N N 140 
HIS   N   H2   sing N N 141 
HIS   CA  C    sing N N 142 
HIS   CA  CB   sing N N 143 
HIS   CA  HA   sing N N 144 
HIS   C   O    doub N N 145 
HIS   C   OXT  sing N N 146 
HIS   CB  CG   sing N N 147 
HIS   CB  HB2  sing N N 148 
HIS   CB  HB3  sing N N 149 
HIS   CG  ND1  sing Y N 150 
HIS   CG  CD2  doub Y N 151 
HIS   ND1 CE1  doub Y N 152 
HIS   ND1 HD1  sing N N 153 
HIS   CD2 NE2  sing Y N 154 
HIS   CD2 HD2  sing N N 155 
HIS   CE1 NE2  sing Y N 156 
HIS   CE1 HE1  sing N N 157 
HIS   NE2 HE2  sing N N 158 
HIS   OXT HXT  sing N N 159 
HOH   O   H1   sing N N 160 
HOH   O   H2   sing N N 161 
ILE   N   CA   sing N N 162 
ILE   N   H    sing N N 163 
ILE   N   H2   sing N N 164 
ILE   CA  C    sing N N 165 
ILE   CA  CB   sing N N 166 
ILE   CA  HA   sing N N 167 
ILE   C   O    doub N N 168 
ILE   C   OXT  sing N N 169 
ILE   CB  CG1  sing N N 170 
ILE   CB  CG2  sing N N 171 
ILE   CB  HB   sing N N 172 
ILE   CG1 CD1  sing N N 173 
ILE   CG1 HG12 sing N N 174 
ILE   CG1 HG13 sing N N 175 
ILE   CG2 HG21 sing N N 176 
ILE   CG2 HG22 sing N N 177 
ILE   CG2 HG23 sing N N 178 
ILE   CD1 HD11 sing N N 179 
ILE   CD1 HD12 sing N N 180 
ILE   CD1 HD13 sing N N 181 
ILE   OXT HXT  sing N N 182 
LEU   N   CA   sing N N 183 
LEU   N   H    sing N N 184 
LEU   N   H2   sing N N 185 
LEU   CA  C    sing N N 186 
LEU   CA  CB   sing N N 187 
LEU   CA  HA   sing N N 188 
LEU   C   O    doub N N 189 
LEU   C   OXT  sing N N 190 
LEU   CB  CG   sing N N 191 
LEU   CB  HB2  sing N N 192 
LEU   CB  HB3  sing N N 193 
LEU   CG  CD1  sing N N 194 
LEU   CG  CD2  sing N N 195 
LEU   CG  HG   sing N N 196 
LEU   CD1 HD11 sing N N 197 
LEU   CD1 HD12 sing N N 198 
LEU   CD1 HD13 sing N N 199 
LEU   CD2 HD21 sing N N 200 
LEU   CD2 HD22 sing N N 201 
LEU   CD2 HD23 sing N N 202 
LEU   OXT HXT  sing N N 203 
LYS   N   CA   sing N N 204 
LYS   N   H    sing N N 205 
LYS   N   H2   sing N N 206 
LYS   CA  C    sing N N 207 
LYS   CA  CB   sing N N 208 
LYS   CA  HA   sing N N 209 
LYS   C   O    doub N N 210 
LYS   C   OXT  sing N N 211 
LYS   CB  CG   sing N N 212 
LYS   CB  HB2  sing N N 213 
LYS   CB  HB3  sing N N 214 
LYS   CG  CD   sing N N 215 
LYS   CG  HG2  sing N N 216 
LYS   CG  HG3  sing N N 217 
LYS   CD  CE   sing N N 218 
LYS   CD  HD2  sing N N 219 
LYS   CD  HD3  sing N N 220 
LYS   CE  NZ   sing N N 221 
LYS   CE  HE2  sing N N 222 
LYS   CE  HE3  sing N N 223 
LYS   NZ  HZ1  sing N N 224 
LYS   NZ  HZ2  sing N N 225 
LYS   NZ  HZ3  sing N N 226 
LYS   OXT HXT  sing N N 227 
MET   N   CA   sing N N 228 
MET   N   H    sing N N 229 
MET   N   H2   sing N N 230 
MET   CA  C    sing N N 231 
MET   CA  CB   sing N N 232 
MET   CA  HA   sing N N 233 
MET   C   O    doub N N 234 
MET   C   OXT  sing N N 235 
MET   CB  CG   sing N N 236 
MET   CB  HB2  sing N N 237 
MET   CB  HB3  sing N N 238 
MET   CG  SD   sing N N 239 
MET   CG  HG2  sing N N 240 
MET   CG  HG3  sing N N 241 
MET   SD  CE   sing N N 242 
MET   CE  HE1  sing N N 243 
MET   CE  HE2  sing N N 244 
MET   CE  HE3  sing N N 245 
MET   OXT HXT  sing N N 246 
PHE   N   CA   sing N N 247 
PHE   N   H    sing N N 248 
PHE   N   H2   sing N N 249 
PHE   CA  C    sing N N 250 
PHE   CA  CB   sing N N 251 
PHE   CA  HA   sing N N 252 
PHE   C   O    doub N N 253 
PHE   C   OXT  sing N N 254 
PHE   CB  CG   sing N N 255 
PHE   CB  HB2  sing N N 256 
PHE   CB  HB3  sing N N 257 
PHE   CG  CD1  doub Y N 258 
PHE   CG  CD2  sing Y N 259 
PHE   CD1 CE1  sing Y N 260 
PHE   CD1 HD1  sing N N 261 
PHE   CD2 CE2  doub Y N 262 
PHE   CD2 HD2  sing N N 263 
PHE   CE1 CZ   doub Y N 264 
PHE   CE1 HE1  sing N N 265 
PHE   CE2 CZ   sing Y N 266 
PHE   CE2 HE2  sing N N 267 
PHE   CZ  HZ   sing N N 268 
PHE   OXT HXT  sing N N 269 
PRO   N   CA   sing N N 270 
PRO   N   CD   sing N N 271 
PRO   N   H    sing N N 272 
PRO   CA  C    sing N N 273 
PRO   CA  CB   sing N N 274 
PRO   CA  HA   sing N N 275 
PRO   C   O    doub N N 276 
PRO   C   OXT  sing N N 277 
PRO   CB  CG   sing N N 278 
PRO   CB  HB2  sing N N 279 
PRO   CB  HB3  sing N N 280 
PRO   CG  CD   sing N N 281 
PRO   CG  HG2  sing N N 282 
PRO   CG  HG3  sing N N 283 
PRO   CD  HD2  sing N N 284 
PRO   CD  HD3  sing N N 285 
PRO   OXT HXT  sing N N 286 
SER   N   CA   sing N N 287 
SER   N   H    sing N N 288 
SER   N   H2   sing N N 289 
SER   CA  C    sing N N 290 
SER   CA  CB   sing N N 291 
SER   CA  HA   sing N N 292 
SER   C   O    doub N N 293 
SER   C   OXT  sing N N 294 
SER   CB  OG   sing N N 295 
SER   CB  HB2  sing N N 296 
SER   CB  HB3  sing N N 297 
SER   OG  HG   sing N N 298 
SER   OXT HXT  sing N N 299 
THR   N   CA   sing N N 300 
THR   N   H    sing N N 301 
THR   N   H2   sing N N 302 
THR   CA  C    sing N N 303 
THR   CA  CB   sing N N 304 
THR   CA  HA   sing N N 305 
THR   C   O    doub N N 306 
THR   C   OXT  sing N N 307 
THR   CB  OG1  sing N N 308 
THR   CB  CG2  sing N N 309 
THR   CB  HB   sing N N 310 
THR   OG1 HG1  sing N N 311 
THR   CG2 HG21 sing N N 312 
THR   CG2 HG22 sing N N 313 
THR   CG2 HG23 sing N N 314 
THR   OXT HXT  sing N N 315 
TRP   N   CA   sing N N 316 
TRP   N   H    sing N N 317 
TRP   N   H2   sing N N 318 
TRP   CA  C    sing N N 319 
TRP   CA  CB   sing N N 320 
TRP   CA  HA   sing N N 321 
TRP   C   O    doub N N 322 
TRP   C   OXT  sing N N 323 
TRP   CB  CG   sing N N 324 
TRP   CB  HB2  sing N N 325 
TRP   CB  HB3  sing N N 326 
TRP   CG  CD1  doub Y N 327 
TRP   CG  CD2  sing Y N 328 
TRP   CD1 NE1  sing Y N 329 
TRP   CD1 HD1  sing N N 330 
TRP   CD2 CE2  doub Y N 331 
TRP   CD2 CE3  sing Y N 332 
TRP   NE1 CE2  sing Y N 333 
TRP   NE1 HE1  sing N N 334 
TRP   CE2 CZ2  sing Y N 335 
TRP   CE3 CZ3  doub Y N 336 
TRP   CE3 HE3  sing N N 337 
TRP   CZ2 CH2  doub Y N 338 
TRP   CZ2 HZ2  sing N N 339 
TRP   CZ3 CH2  sing Y N 340 
TRP   CZ3 HZ3  sing N N 341 
TRP   CH2 HH2  sing N N 342 
TRP   OXT HXT  sing N N 343 
TYR   N   CA   sing N N 344 
TYR   N   H    sing N N 345 
TYR   N   H2   sing N N 346 
TYR   CA  C    sing N N 347 
TYR   CA  CB   sing N N 348 
TYR   CA  HA   sing N N 349 
TYR   C   O    doub N N 350 
TYR   C   OXT  sing N N 351 
TYR   CB  CG   sing N N 352 
TYR   CB  HB2  sing N N 353 
TYR   CB  HB3  sing N N 354 
TYR   CG  CD1  doub Y N 355 
TYR   CG  CD2  sing Y N 356 
TYR   CD1 CE1  sing Y N 357 
TYR   CD1 HD1  sing N N 358 
TYR   CD2 CE2  doub Y N 359 
TYR   CD2 HD2  sing N N 360 
TYR   CE1 CZ   doub Y N 361 
TYR   CE1 HE1  sing N N 362 
TYR   CE2 CZ   sing Y N 363 
TYR   CE2 HE2  sing N N 364 
TYR   CZ  OH   sing N N 365 
TYR   OH  HH   sing N N 366 
TYR   OXT HXT  sing N N 367 
VAL   N   CA   sing N N 368 
VAL   N   H    sing N N 369 
VAL   N   H2   sing N N 370 
VAL   CA  C    sing N N 371 
VAL   CA  CB   sing N N 372 
VAL   CA  HA   sing N N 373 
VAL   C   O    doub N N 374 
VAL   C   OXT  sing N N 375 
VAL   CB  CG1  sing N N 376 
VAL   CB  CG2  sing N N 377 
VAL   CB  HB   sing N N 378 
VAL   CG1 HG11 sing N N 379 
VAL   CG1 HG12 sing N N 380 
VAL   CG1 HG13 sing N N 381 
VAL   CG2 HG21 sing N N 382 
VAL   CG2 HG22 sing N N 383 
VAL   CG2 HG23 sing N N 384 
VAL   OXT HXT  sing N N 385 
# 
_pdbx_audit_support.funding_organization   'National Natural Science Foundation of China (NSFC)' 
_pdbx_audit_support.country                China 
_pdbx_audit_support.grant_number           2021YFC2301405 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_deposit_group.group_title         'Crystallographic fragment screening of Human heat shock protein 90' 
_pdbx_deposit_group.group_description   
;Heat shock protein 90 (HSP90) is one of the most active molecular chaperones in cells. It plays a vital role in the cell maturation process and serves as a molecular chaperone involved in many oncogenic proteins folding, assembly and stabilization. Many HSP90 client proteins are kinases or transcription factors involved in signal transduction pathways and are key regulatory factors in tumor growth and maintenance. Therefore, HSP90 inhibitors can be used as drugs for cancer treatment.
;
_pdbx_deposit_group.group_type          'changed state' 
_pdbx_deposit_group.group_id            G_1002298 
# 
_space_group.name_H-M_alt     'I 2 2 2' 
_space_group.name_Hall        'I 2 2' 
_space_group.IT_number        23 
_space_group.crystal_system   orthorhombic 
_space_group.id               1 
# 
_atom_sites.entry_id                    7HAJ 
_atom_sites.fract_transf_matrix[1][1]   0.015152 
_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]   0.011138 
_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]   0.010011 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
_atom_type.scat_dispersion_real 
_atom_type.scat_dispersion_imag 
_atom_type.scat_Cromer_Mann_a1 
_atom_type.scat_Cromer_Mann_a2 
_atom_type.scat_Cromer_Mann_a3 
_atom_type.scat_Cromer_Mann_a4 
_atom_type.scat_Cromer_Mann_b1 
_atom_type.scat_Cromer_Mann_b2 
_atom_type.scat_Cromer_Mann_b3 
_atom_type.scat_Cromer_Mann_b4 
_atom_type.scat_Cromer_Mann_c 
_atom_type.scat_source 
_atom_type.scat_dispersion_source 
C   ? ? 3.54356 2.42580 ? ? 25.62398 1.50364  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
N   ? ? 4.01032 2.96436 ? ? 19.97189 1.75589  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O   ? ? 4.49882 3.47563 ? ? 15.80542 1.70748  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O1- ? ? 5.12366 3.84317 ? ? 3.49406  27.47979 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
S   ? ? 9.55732 6.39887 ? ? 1.23737  29.19336 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
# 
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   . GLU   A 1 9   ? 4.50384   -28.16823 -38.98537 1.000 51.12362 ?  16  GLU   A N   1 
ATOM   2    C CA  . GLU   A 1 9   ? 5.75466   -27.42388 -39.17470 1.000 51.20789 ?  16  GLU   A CA  1 
ATOM   3    C C   . GLU   A 1 9   ? 6.04532   -26.53366 -37.95110 1.000 42.33730 ?  16  GLU   A C   1 
ATOM   4    O O   . GLU   A 1 9   ? 5.47761   -25.44183 -37.81159 1.000 41.34453 ?  16  GLU   A O   1 
ATOM   5    C CB  . GLU   A 1 9   ? 5.68352   -26.57728 -40.45533 1.000 64.05707 ?  16  GLU   A CB  1 
ATOM   6    C CG  . GLU   A 1 9   ? 7.01366   -26.37559 -41.23010 1.000 71.94176 ?  16  GLU   A CG  1 
ATOM   7    C CD  . GLU   A 1 9   ? 7.89815   -25.25611 -40.64915 1.000 69.35570 ?  16  GLU   A CD  1 
ATOM   8    O OE1 . GLU   A 1 9   ? 7.36155   -24.36502 -39.94681 1.000 76.40995 ?  16  GLU   A OE1 1 
ATOM   9    O OE2 . GLU   A 1 9   ? 9.12220   -25.24410 -40.91966 1.000 69.11108 ?  16  GLU   A OE2 1 
ATOM   10   N N   . VAL   A 1 10  ? 6.92854   -27.00060 -37.07135 1.000 37.45540 ?  17  VAL   A N   1 
ATOM   11   C CA  . VAL   A 1 10  ? 7.18640   -26.36373 -35.78865 1.000 29.20565 ?  17  VAL   A CA  1 
ATOM   12   C C   . VAL   A 1 10  ? 8.56740   -25.72813 -35.84793 1.000 30.93470 ?  17  VAL   A C   1 
ATOM   13   O O   . VAL   A 1 10  ? 9.54867   -26.40359 -36.18170 1.000 28.23210 ?  17  VAL   A O   1 
ATOM   14   C CB  . VAL   A 1 10  ? 7.13342   -27.37936 -34.64835 1.000 31.82594 ?  17  VAL   A CB  1 
ATOM   15   C CG1 . VAL   A 1 10  ? 7.43093   -26.68419 -33.32306 1.000 30.19642 ?  17  VAL   A CG1 1 
ATOM   16   C CG2 . VAL   A 1 10  ? 5.79522   -28.12447 -34.65789 1.000 42.57982 ?  17  VAL   A CG2 1 
ATOM   17   N N   . GLU   A 1 11  ? 8.64234   -24.44133 -35.55199 1.000 22.67678 ?  18  GLU   A N   1 
ATOM   18   C CA  . GLU   A 1 11  ? 9.91514   -23.73102 -35.47980 1.000 22.15994 ?  18  GLU   A CA  1 
ATOM   19   C C   . GLU   A 1 11  ? 10.30723  -23.62449 -34.01447 1.000 19.62393 ?  18  GLU   A C   1 
ATOM   20   O O   . GLU   A 1 11  ? 9.48414   -23.24897 -33.15890 1.000 18.61421 ?  18  GLU   A O   1 
ATOM   21   C CB  . GLU   A 1 11  ? 9.82006   -22.34042 -36.11553 1.000 19.90773 ?  18  GLU   A CB  1 
ATOM   22   C CG  . GLU   A 1 11  ? 9.64913   -22.36500 -37.65222 1.000 21.55455 ?  18  GLU   A CG  1 
ATOM   23   C CD  . GLU   A 1 11  ? 9.48289   -20.95300 -38.21549 1.000 31.78055 ?  18  GLU   A CD  1 
ATOM   24   O OE1 . GLU   A 1 11  ? 8.45130   -20.33013 -37.92712 1.000 31.86492 ?  18  GLU   A OE1 1 
ATOM   25   O OE2 . GLU   A 1 11  ? 10.32357  -20.50413 -39.01720 1.000 37.39009 ?  18  GLU   A OE2 1 
ATOM   26   N N   . THR   A 1 12  ? 11.55998  -23.93991 -33.71626 1.000 17.99161 ?  19  THR   A N   1 
ATOM   27   C CA  . THR   A 1 12  ? 12.10220  -23.79046 -32.37113 1.000 16.66682 ?  19  THR   A CA  1 
ATOM   28   C C   . THR   A 1 12  ? 13.09054  -22.64110 -32.34963 1.000 15.71923 ?  19  THR   A C   1 
ATOM   29   O O   . THR   A 1 12  ? 14.00247  -22.59378 -33.17671 1.000 16.12476 ?  19  THR   A O   1 
ATOM   30   C CB  . THR   A 1 12  ? 12.80423  -25.09378 -31.94367 1.000 17.49995 ?  19  THR   A CB  1 
ATOM   31   O OG1 . THR   A 1 12  ? 11.91371  -26.19307 -32.05845 1.000 19.45986 ?  19  THR   A OG1 1 
ATOM   32   C CG2 . THR   A 1 12  ? 13.29848  -24.99656 -30.51508 1.000 16.53424 ?  19  THR   A CG2 1 
ATOM   33   N N   . PHE   A 1 13  ? 12.95299  -21.76225 -31.37427 1.000 14.67107 ?  20  PHE   A N   1 
ATOM   34   C CA  . PHE   A 1 13  ? 13.75782  -20.56035 -31.19992 1.000 15.46649 ?  20  PHE   A CA  1 
ATOM   35   C C   . PHE   A 1 13  ? 14.39263  -20.54985 -29.82556 1.000 16.06188 ?  20  PHE   A C   1 
ATOM   36   O O   . PHE   A 1 13  ? 13.81444  -21.05505 -28.84524 1.000 15.65924 ?  20  PHE   A O   1 
ATOM   37   C CB  . PHE   A 1 13  ? 12.89944  -19.27959 -31.23787 1.000 13.92934 ?  20  PHE   A CB  1 
ATOM   38   C CG  . PHE   A 1 13  ? 12.15059  -19.08635 -32.53937 1.000 14.96112 ?  20  PHE   A CG  1 
ATOM   39   C CD1 . PHE   A 1 13  ? 10.94559  -19.71969 -32.77167 1.000 18.22604 ?  20  PHE   A CD1 1 
ATOM   40   C CD2 . PHE   A 1 13  ? 12.68034  -18.24371 -33.51849 1.000 17.54569 ?  20  PHE   A CD2 1 
ATOM   41   C CE1 . PHE   A 1 13  ? 10.30253  -19.52960 -33.98337 1.000 18.28049 ?  20  PHE   A CE1 1 
ATOM   42   C CE2 . PHE   A 1 13  ? 12.01232  -18.00975 -34.74522 1.000 19.27742 ?  20  PHE   A CE2 1 
ATOM   43   C CZ  . PHE   A 1 13  ? 10.84285  -18.66034 -34.96629 1.000 21.10460 ?  20  PHE   A CZ  1 
ATOM   44   N N   . ALA   A 1 14  ? 15.58300  -19.94505 -29.73493 1.000 14.45684 ?  21  ALA   A N   1 
ATOM   45   C CA  . ALA   A 1 14  ? 16.19068  -19.67492 -28.42724 1.000 13.98586 ?  21  ALA   A CA  1 
ATOM   46   C C   . ALA   A 1 14  ? 15.65327  -18.36607 -27.86352 1.000 14.99557 ?  21  ALA   A C   1 
ATOM   47   O O   . ALA   A 1 14  ? 15.57491  -17.36311 -28.55429 1.000 15.19166 ?  21  ALA   A O   1 
ATOM   48   C CB  . ALA   A 1 14  ? 17.71948  -19.60257 -28.54183 1.000 16.49330 ?  21  ALA   A CB  1 
ATOM   49   N N   . PHE   A 1 15  ? 15.26975  -18.36864 -26.57024 1.000 14.55445 ?  22  PHE   A N   1 
ATOM   50   C CA  . PHE   A 1 15  ? 15.06840  -17.06103 -25.94518 1.000 15.25120 ?  22  PHE   A CA  1 
ATOM   51   C C   . PHE   A 1 15  ? 16.35754  -16.24993 -25.97934 1.000 12.57507 ?  22  PHE   A C   1 
ATOM   52   O O   . PHE   A 1 15  ? 17.46185  -16.80021 -25.87484 1.000 15.97131 ?  22  PHE   A O   1 
ATOM   53   C CB  . PHE   A 1 15  ? 14.69685  -17.22179 -24.44945 1.000 13.29481 ?  22  PHE   A CB  1 
ATOM   54   C CG  . PHE   A 1 15  ? 13.33471  -17.78849 -24.21616 1.000 12.08539 ?  22  PHE   A CG  1 
ATOM   55   C CD1 . PHE   A 1 15  ? 12.19548  -17.03548 -24.50305 1.000 13.82377 ?  22  PHE   A CD1 1 
ATOM   56   C CD2 . PHE   A 1 15  ? 13.19386  -19.06594 -23.73246 1.000 12.75435 ?  22  PHE   A CD2 1 
ATOM   57   C CE1 . PHE   A 1 15  ? 10.90326  -17.57349 -24.28273 1.000 12.78788 ?  22  PHE   A CE1 1 
ATOM   58   C CE2 . PHE   A 1 15  ? 11.92382  -19.64048 -23.52366 1.000 12.69383 ?  22  PHE   A CE2 1 
ATOM   59   C CZ  . PHE   A 1 15  ? 10.76682  -18.87816 -23.80032 1.000 12.70521 ?  22  PHE   A CZ  1 
ATOM   60   N N   . GLN   A 1 16  ? 16.19144  -14.94052 -26.05757 1.000 14.48437 ?  23  GLN   A N   1 
ATOM   61   C CA  . GLN   A 1 16  ? 17.28799  -14.03601 -25.72856 1.000 17.57278 ?  23  GLN   A CA  1 
ATOM   62   C C   . GLN   A 1 16  ? 17.80454  -14.35524 -24.34192 1.000 17.36641 ?  23  GLN   A C   1 
ATOM   63   O O   . GLN   A 1 16  ? 17.03707  -14.70638 -23.45164 1.000 16.01738 ?  23  GLN   A O   1 
ATOM   64   C CB  . GLN   A 1 16  ? 16.80652  -12.59117 -25.78286 1.000 18.60490 ?  23  GLN   A CB  1 
ATOM   65   C CG  . GLN   A 1 16  ? 16.42561  -12.12422 -27.19041 1.000 21.62253 ?  23  GLN   A CG  1 
ATOM   66   C CD  . GLN   A 1 16  ? 15.88829  -10.68274 -27.08704 1.000 32.91793 ?  23  GLN   A CD  1 
ATOM   67   O OE1 . GLN   A 1 16  ? 14.70338  -10.46782 -26.98160 1.000 33.09850 ?  23  GLN   A OE1 1 
ATOM   68   N NE2 . GLN   A 1 16  ? 16.79786  -9.68920  -27.14071 1.000 36.40773 ?  23  GLN   A NE2 1 
ATOM   69   N N   . ALA   A 1 17  ? 19.11728  -14.27149 -24.17182 1.000 17.72611 ?  24  ALA   A N   1 
ATOM   70   C CA  . ALA   A 1 17  ? 19.71456  -14.64831 -22.89625 1.000 15.53007 ?  24  ALA   A CA  1 
ATOM   71   C C   . ALA   A 1 17  ? 19.05554  -13.96150 -21.72132 1.000 17.06556 ?  24  ALA   A C   1 
ATOM   72   O O   . ALA   A 1 17  ? 18.80465  -14.60279 -20.69817 1.000 17.92298 ?  24  ALA   A O   1 
ATOM   73   C CB  . ALA   A 1 17  ? 21.19575  -14.30966 -22.93824 1.000 21.76029 ?  24  ALA   A CB  1 
ATOM   74   N N   . GLU   A 1 18  ? 18.76252  -12.67222 -21.84306 1.000 18.72802 ?  25  GLU   A N   1 
ATOM   75   C CA  . GLU   A 1 18  ? 18.14656  -11.96634 -20.72201 1.000 18.96749 ?  25  GLU   A CA  1 
ATOM   76   C C   . GLU   A 1 18  ? 16.79527  -12.57259 -20.35092 1.000 17.35096 ?  25  GLU   A C   1 
ATOM   77   O O   . GLU   A 1 18  ? 16.41737  -12.60774 -19.16110 1.000 19.14345 ?  25  GLU   A O   1 
ATOM   78   C CB  . GLU   A 1 18  ? 18.01631  -10.48336 -21.07221 1.000 24.00976 ?  25  GLU   A CB  1 
ATOM   79   C CG  . GLU   A 1 18  ? 19.37530  -9.81635  -21.25220 1.000 25.58313 ?  25  GLU   A CG  1 
ATOM   80   C CD  . GLU   A 1 18  ? 19.94758  -9.96420  -22.65786 1.000 30.57426 ?  25  GLU   A CD  1 
ATOM   81   O OE1 . GLU   A 1 18  ? 19.33402  -10.63301 -23.52055 1.000 26.68449 ?  25  GLU   A OE1 1 
ATOM   82   O OE2 . GLU   A 1 18  ? 21.02948  -9.38249  -22.92116 1.000 37.28363 ?  25  GLU   A OE2 1 
ATOM   83   N N   . ILE   A 1 19  ? 16.02991  -13.03652 -21.34281 1.000 16.97791 ?  26  ILE   A N   1 
ATOM   84   C CA  . ILE   A 1 19  ? 14.70827  -13.56412 -21.03794 1.000 14.56518 ?  26  ILE   A CA  1 
ATOM   85   C C   . ILE   A 1 19  ? 14.82495  -14.96892 -20.45027 1.000 16.16234 ?  26  ILE   A C   1 
ATOM   86   O O   . ILE   A 1 19  ? 14.11303  -15.33411 -19.51566 1.000 16.86595 ?  26  ILE   A O   1 
ATOM   87   C CB  . ILE   A 1 19  ? 13.81833  -13.52869 -22.30974 1.000 17.04306 ?  26  ILE   A CB  1 
ATOM   88   C CG1 . ILE   A 1 19  ? 13.29634  -12.10838 -22.61616 1.000 17.95206 ?  26  ILE   A CG1 1 
ATOM   89   C CG2 . ILE   A 1 19  ? 12.58562  -14.44787 -22.12371 1.000 16.18058 ?  26  ILE   A CG2 1 
ATOM   90   C CD1 . ILE   A 1 19  ? 14.35587  -11.03931 -22.86739 1.000 23.13544 ?  26  ILE   A CD1 1 
ATOM   91   N N   . ALA   A 1 20  ? 15.77247  -15.76617 -20.94508 1.000 13.61322 ?  27  ALA   A N   1 
ATOM   92   C CA  . ALA   A 1 20  ? 16.02539  -17.03518 -20.30015 1.000 13.70779 ?  27  ALA   A CA  1 
ATOM   93   C C   . ALA   A 1 20  ? 16.43372  -16.81438 -18.84717 1.000 15.02786 ?  27  ALA   A C   1 
ATOM   94   O O   . ALA   A 1 20  ? 16.05822  -17.59097 -17.95827 1.000 15.13531 ?  27  ALA   A O   1 
ATOM   95   C CB  . ALA   A 1 20  ? 17.15362  -17.76740 -21.04619 1.000 14.39119 ?  27  ALA   A CB  1 
ATOM   96   N N   . GLN   A 1 21  ? 17.16610  -15.73504 -18.58319 1.000 13.24655 ?  28  GLN   A N   1 
ATOM   97   C CA  . GLN   A 1 21  ? 17.58856  -15.49953 -17.20917 1.000 14.06286 ?  28  GLN   A CA  1 
ATOM   98   C C   . GLN   A 1 21  ? 16.41236  -15.08114 -16.34703 1.000 17.97485 ?  28  GLN   A C   1 
ATOM   99   O O   . GLN   A 1 21  ? 16.29633  -15.52162 -15.19453 1.000 18.27259 ?  28  GLN   A O   1 
ATOM   100  C CB  . GLN   A 1 21  ? 18.70535  -14.44702 -17.18337 1.000 16.44385 ?  28  GLN   A CB  1 
ATOM   101  C CG  . GLN   A 1 21  ? 19.38789  -14.32430 -15.79069 1.000 25.82496 ?  28  GLN   A CG  1 
ATOM   102  C CD  . GLN   A 1 21  ? 20.52283  -13.27608 -15.82097 1.000 28.17794 ?  28  GLN   A CD  1 
ATOM   103  O OE1 . GLN   A 1 21  ? 20.74440  -12.66859 -16.86734 1.000 35.21567 ?  28  GLN   A OE1 1 
ATOM   104  N NE2 . GLN   A 1 21  ? 21.24485  -13.09625 -14.70707 1.000 39.21251 ?  28  GLN   A NE2 1 
ATOM   105  N N   . LEU   A 1 22  ? 15.54960  -14.21622 -16.89177 1.000 16.33415 ?  29  LEU   A N   1 
ATOM   106  C CA  . LEU   A 1 22  ? 14.29479  -13.87862 -16.19683 1.000 16.11034 ?  29  LEU   A CA  1 
ATOM   107  C C   . LEU   A 1 22  ? 13.50495  -15.12795 -15.83864 1.000 16.72353 ?  29  LEU   A C   1 
ATOM   108  O O   . LEU   A 1 22  ? 13.00181  -15.28292 -14.70717 1.000 16.32048 ?  29  LEU   A O   1 
ATOM   109  C CB  . LEU   A 1 22  ? 13.43463  -12.97597 -17.10953 1.000 19.59300 ?  29  LEU   A CB  1 
ATOM   110  C CG  . LEU   A 1 22  ? 12.02770  -12.64974 -16.57554 1.000 20.46147 ?  29  LEU   A CG  1 
ATOM   111  C CD1 . LEU   A 1 22  ? 12.22043  -11.73224 -15.42472 1.000 22.43854 ?  29  LEU   A CD1 1 
ATOM   112  C CD2 . LEU   A 1 22  ? 11.14894  -11.98121 -17.64345 1.000 19.03008 ?  29  LEU   A CD2 1 
ATOM   113  N N   . MET   A 1 23  ? 13.32421  -16.01130 -16.82402 1.000 13.82617 ?  30  MET   A N   1 
ATOM   114  C CA  . MET   A 1 23  ? 12.53907  -17.19010 -16.58305 1.000 14.44685 ?  30  MET   A CA  1 
ATOM   115  C C   . MET   A 1 23  ? 13.16775  -18.07928 -15.53594 1.000 14.44809 ?  30  MET   A C   1 
ATOM   116  O O   . MET   A 1 23  ? 12.45105  -18.66472 -14.69648 1.000 15.83543 ?  30  MET   A O   1 
ATOM   117  C CB  . MET   A 1 23  ? 12.30611  -17.94643 -17.90432 1.000 12.48966 ?  30  MET   A CB  1 
ATOM   118  C CG  . MET   A 1 23  ? 11.37615  -17.16404 -18.84644 1.000 14.85346 ?  30  MET   A CG  1 
ATOM   119  S SD  . MET   A 1 23  ? 11.31303  -17.93648 -20.48625 1.000 15.47759 ?  30  MET   A SD  1 
ATOM   120  C CE  . MET   A 1 23  ? 10.07673  -19.17262 -20.17905 1.000 16.76752 ?  30  MET   A CE  1 
ATOM   121  N N   . SER   A 1 24  ? 14.49835  -18.24383 -15.57797 1.000 15.58905 ?  31  SER   A N   1 
ATOM   122  C CA  . SER   A 1 24  ? 15.14845  -19.06968 -14.56414 1.000 16.32407 ?  31  SER   A CA  1 
ATOM   123  C C   . SER   A 1 24  ? 14.98743  -18.44054 -13.17362 1.000 21.18216 ?  31  SER   A C   1 
ATOM   124  O O   . SER   A 1 24  ? 14.74218  -19.14212 -12.18250 1.000 21.10060 ?  31  SER   A O   1 
ATOM   125  C CB  . SER   A 1 24  ? 16.62395  -19.27051 -15.02300 1.000 18.93442 ?  31  SER   A CB  1 
ATOM   126  O OG  . SER   A 1 24  ? 17.41413  -19.83568 -13.99854 1.000 25.69607 ?  31  SER   A OG  1 
ATOM   127  N N   . LEU   A 1 25  ? 15.04174  -17.11468 -13.07855 1.000 17.14310 ?  32  LEU   A N   1 
ATOM   128  C CA  . LEU   A 1 25  ? 14.83563  -16.47397 -11.77552 1.000 16.68165 ?  32  LEU   A CA  1 
ATOM   129  C C   . LEU   A 1 25  ? 13.43778  -16.73970 -11.26879 1.000 18.78158 ?  32  LEU   A C   1 
ATOM   130  O O   . LEU   A 1 25  ? 13.23262  -17.03419 -10.08288 1.000 20.10079 ?  32  LEU   A O   1 
ATOM   131  C CB  . LEU   A 1 25  ? 15.09423  -14.97509 -11.91360 1.000 21.32240 ?  32  LEU   A CB  1 
ATOM   132  C CG  . LEU   A 1 25  ? 14.90497  -14.16093 -10.63579 1.000 27.23696 ?  32  LEU   A CG  1 
ATOM   133  C CD1 . LEU   A 1 25  ? 15.81969  -12.97599 -10.72494 1.000 29.09007 ?  32  LEU   A CD1 1 
ATOM   134  C CD2 . LEU   A 1 25  ? 13.44419  -13.69459 -10.45039 1.000 27.98169 ?  32  LEU   A CD2 1 
ATOM   135  N N   . ILE   A 1 26  ? 12.44922  -16.63967 -12.16407 1.000 14.08572 ?  33  ILE   A N   1 
ATOM   136  C CA  . ILE   A 1 26  ? 11.07289  -16.83976 -11.70156 1.000 15.08649 ?  33  ILE   A CA  1 
ATOM   137  C C   . ILE   A 1 26  ? 10.87618  -18.27872 -11.25308 1.000 17.55350 ?  33  ILE   A C   1 
ATOM   138  O O   . ILE   A 1 26  ? 10.13484  -18.55862 -10.29491 1.000 19.48037 ?  33  ILE   A O   1 
ATOM   139  C CB  . ILE   A 1 26  ? 10.11495  -16.44118 -12.83757 1.000 13.54804 ?  33  ILE   A CB  1 
ATOM   140  C CG1 . ILE   A 1 26  ? 10.13941  -14.91136 -12.99531 1.000 16.46212 ?  33  ILE   A CG1 1 
ATOM   141  C CG2 . ILE   A 1 26  ? 8.69104   -17.00777 -12.59689 1.000 15.75346 ?  33  ILE   A CG2 1 
ATOM   142  C CD1 . ILE   A 1 26  ? 9.55904   -14.45779 -14.37111 1.000 20.08167 ?  33  ILE   A CD1 1 
ATOM   143  N N   . ILE   A 1 27  ? 11.51538  -19.22410 -11.94462 1.000 17.35265 ?  34  ILE   A N   1 
ATOM   144  C CA  . ILE   A 1 27  ? 11.29981  -20.63350 -11.61083 1.000 18.60164 ?  34  ILE   A CA  1 
ATOM   145  C C   . ILE   A 1 27  ? 12.06010  -21.05176 -10.37124 1.000 23.23501 ?  34  ILE   A C   1 
ATOM   146  O O   . ILE   A 1 27  ? 11.58703  -21.91051 -9.60866  1.000 24.40761 ?  34  ILE   A O   1 
ATOM   147  C CB  . ILE   A 1 27  ? 11.70580  -21.47669 -12.82265 1.000 19.53275 ?  34  ILE   A CB  1 
ATOM   148  C CG1 . ILE   A 1 27  ? 10.65729  -21.27070 -13.92355 1.000 16.57050 ?  34  ILE   A CG1 1 
ATOM   149  C CG2 . ILE   A 1 27  ? 11.90849  -22.93665 -12.40914 1.000 20.15624 ?  34  ILE   A CG2 1 
ATOM   150  C CD1 . ILE   A 1 27  ? 11.17736  -21.85775 -15.31623 1.000 17.52291 ?  34  ILE   A CD1 1 
ATOM   151  N N   . ASN   A 1 28  ? 13.22618  -20.43953 -10.11475 1.000 18.76020 ?  35  ASN   A N   1 
ATOM   152  C CA  . ASN   A 1 28  ? 14.12568  -20.93747 -9.07133  1.000 22.97789 ?  35  ASN   A CA  1 
ATOM   153  C C   . ASN   A 1 28  ? 14.14048  -20.11895 -7.78793  1.000 27.06470 ?  35  ASN   A C   1 
ATOM   154  O O   . ASN   A 1 28  ? 14.59085  -20.63662 -6.75502  1.000 28.52947 ?  35  ASN   A O   1 
ATOM   155  C CB  . ASN   A 1 28  ? 15.52408  -21.01975 -9.64708  1.000 23.98122 ?  35  ASN   A CB  1 
ATOM   156  C CG  . ASN   A 1 28  ? 15.58222  -22.09915 -10.66887 1.000 30.29443 ?  35  ASN   A CG  1 
ATOM   157  O OD1 . ASN   A 1 28  ? 15.13511  -23.21092 -10.40097 1.000 32.38930 ?  35  ASN   A OD1 1 
ATOM   158  N ND2 . ASN   A 1 28  ? 15.95500  -21.75834 -11.88228 1.000 35.66751 ?  35  ASN   A ND2 1 
ATOM   159  N N   . THR   A 1 29  ? 13.62565  -18.89993 -7.80042  1.000 18.74046 ?  36  THR   A N   1 
ATOM   160  C CA  . THR   A 1 29  ? 13.64393  -18.10604 -6.56633  1.000 18.60827 ?  36  THR   A CA  1 
ATOM   161  C C   . THR   A 1 29  ? 12.58722  -18.62477 -5.60835  1.000 20.68110 ?  36  THR   A C   1 
ATOM   162  O O   . THR   A 1 29  ? 11.42334  -18.85189 -5.99946  1.000 22.30856 ?  36  THR   A O   1 
ATOM   163  C CB  . THR   A 1 29  ? 13.37369  -16.62940 -6.91375  1.000 22.06790 ?  36  THR   A CB  1 
ATOM   164  O OG1 . THR   A 1 29  ? 14.41746  -16.16074 -7.77520  1.000 25.26463 ?  36  THR   A OG1 1 
ATOM   165  C CG2 . THR   A 1 29  ? 13.36824  -15.72560 -5.67931  1.000 22.51146 ?  36  THR   A CG2 1 
ATOM   166  N N   . PHE   A 1 30  ? 12.97096  -18.77390 -4.34190  1.000 20.44588 ?  37  PHE   A N   1 
ATOM   167  C CA  . PHE   A 1 30  ? 11.94097  -19.04816 -3.37146  1.000 21.71537 ?  37  PHE   A CA  1 
ATOM   168  C C   . PHE   A 1 30  ? 11.07741  -17.81878 -3.19001  1.000 22.39096 ?  37  PHE   A C   1 
ATOM   169  O O   . PHE   A 1 30  ? 11.55267  -16.76068 -2.74818  1.000 21.21015 ?  37  PHE   A O   1 
ATOM   170  C CB  . PHE   A 1 30  ? 12.55383  -19.48490 -2.05005  1.000 22.16704 ?  37  PHE   A CB  1 
ATOM   171  C CG  . PHE   A 1 30  ? 11.50701  -19.81758 -1.02304  1.000 23.71066 ?  37  PHE   A CG  1 
ATOM   172  C CD1 . PHE   A 1 30  ? 10.77166  -20.98260 -1.13967  1.000 30.88558 ?  37  PHE   A CD1 1 
ATOM   173  C CD2 . PHE   A 1 30  ? 11.22905  -18.95331 0.03187   1.000 24.06128 ?  37  PHE   A CD2 1 
ATOM   174  C CE1 . PHE   A 1 30  ? 9.77519   -21.30276 -0.21188  1.000 27.40672 ?  37  PHE   A CE1 1 
ATOM   175  C CE2 . PHE   A 1 30  ? 10.23528  -19.27164 0.95321   1.000 24.70633 ?  37  PHE   A CE2 1 
ATOM   176  C CZ  . PHE   A 1 30  ? 9.52438   -20.44926 0.84149   1.000 27.44137 ?  37  PHE   A CZ  1 
ATOM   177  N N   . TYR   A 1 31  ? 9.76952   -17.97678 -3.41933  1.000 18.52473 ?  38  TYR   A N   1 
ATOM   178  C CA  . TYR   A 1 31  ? 8.90258   -16.82234 -3.33476  1.000 17.59469 ?  38  TYR   A CA  1 
ATOM   179  C C   . TYR   A 1 31  ? 7.46454   -17.34427 -3.22522  1.000 17.56064 ?  38  TYR   A C   1 
ATOM   180  O O   . TYR   A 1 31  ? 6.93830   -17.94084 -4.18113  1.000 18.23834 ?  38  TYR   A O   1 
ATOM   181  C CB  . TYR   A 1 31  ? 9.11906   -15.93263 -4.58325  1.000 18.35614 ?  38  TYR   A CB  1 
ATOM   182  C CG  . TYR   A 1 31  ? 8.05019   -14.92072 -4.75602  1.000 18.70385 ?  38  TYR   A CG  1 
ATOM   183  C CD1 . TYR   A 1 31  ? 8.02272   -13.74211 -4.02748  1.000 23.01860 ?  38  TYR   A CD1 1 
ATOM   184  C CD2 . TYR   A 1 31  ? 7.07742   -15.14965 -5.73590  1.000 22.78909 ?  38  TYR   A CD2 1 
ATOM   185  C CE1 . TYR   A 1 31  ? 6.95590   -12.82358 -4.23149  1.000 29.49397 ?  38  TYR   A CE1 1 
ATOM   186  C CE2 . TYR   A 1 31  ? 6.09590   -14.28694 -5.92157  1.000 25.32705 ?  38  TYR   A CE2 1 
ATOM   187  C CZ  . TYR   A 1 31  ? 6.02609   -13.14586 -5.21614  1.000 21.01105 ?  38  TYR   A CZ  1 
ATOM   188  O OH  . TYR   A 1 31  ? 4.91885   -12.35495 -5.54855  1.000 29.65675 ?  38  TYR   A OH  1 
ATOM   189  N N   . SER   A 1 32  ? 6.80664   -17.11325 -2.08976  1.000 18.41761 ?  39  SER   A N   1 
ATOM   190  C CA  . SER   A 1 32  ? 5.56232   -17.82647 -1.80969  1.000 18.99523 ?  39  SER   A CA  1 
ATOM   191  C C   . SER   A 1 32  ? 4.32983   -17.18814 -2.44807  1.000 18.66153 ?  39  SER   A C   1 
ATOM   192  O O   . SER   A 1 32  ? 3.32906   -17.87630 -2.62137  1.000 20.64039 ?  39  SER   A O   1 
ATOM   193  C CB  . SER   A 1 32  ? 5.34667   -17.92806 -0.31038  1.000 20.43819 ?  39  SER   A CB  1 
ATOM   194  O OG  . SER   A 1 32  ? 6.36942   -18.74358 0.27151   1.000 21.56569 ?  39  SER   A OG  1 
ATOM   195  N N   . ASN   A 1 33  ? 4.39389   -15.91762 -2.80478  1.000 17.70615 ?  40  ASN   A N   1 
ATOM   196  C CA  . ASN   A 1 33  ? 3.21638   -15.15634 -3.23683  1.000 19.57359 ?  40  ASN   A CA  1 
ATOM   197  C C   . ASN   A 1 33  ? 2.94453   -15.39537 -4.72542  1.000 19.16004 ?  40  ASN   A C   1 
ATOM   198  O O   . ASN   A 1 33  ? 2.89999   -14.47487 -5.53490  1.000 19.08865 ?  40  ASN   A O   1 
ATOM   199  C CB  . ASN   A 1 33  ? 3.45000   -13.68838 -2.94167  1.000 20.08409 ?  40  ASN   A CB  1 
ATOM   200  C CG  . ASN   A 1 33  ? 2.22049   -12.82592 -3.25344  1.000 23.89763 ?  40  ASN   A CG  1 
ATOM   201  O OD1 . ASN   A 1 33  ? 1.08644   -13.27247 -3.09924  1.000 22.55860 ?  40  ASN   A OD1 1 
ATOM   202  N ND2 . ASN   A 1 33  ? 2.46323   -11.57041 -3.60027  1.000 25.63483 ?  40  ASN   A ND2 1 
ATOM   203  N N   . LYS   A 1 34  ? 2.72273   -16.66780 -5.06221  1.000 15.03931 ?  41  LYS   A N   1 
ATOM   204  C CA  . LYS   A 1 34  ? 2.65667   -16.99082 -6.49425  1.000 15.13468 ?  41  LYS   A CA  1 
ATOM   205  C C   . LYS   A 1 34  ? 1.35860   -16.51879 -7.13281  1.000 14.89527 ?  41  LYS   A C   1 
ATOM   206  O O   . LYS   A 1 34  ? 1.31580   -16.41721 -8.35471  1.000 14.51851 ?  41  LYS   A O   1 
ATOM   207  C CB  . LYS   A 1 34  ? 2.75339   -18.50119 -6.67536  1.000 18.14362 ?  41  LYS   A CB  1 
ATOM   208  C CG  . LYS   A 1 34  ? 4.11003   -19.11426 -6.35059  1.000 16.76314 ?  41  LYS   A CG  1 
ATOM   209  C CD  . LYS   A 1 34  ? 4.05334   -20.64503 -6.53018  1.000 19.61893 ?  41  LYS   A CD  1 
ATOM   210  C CE  . LYS   A 1 34  ? 5.42198   -21.35416 -6.27779  1.000 18.34459 ?  41  LYS   A CE  1 
ATOM   211  N NZ  . LYS   A 1 34  ? 6.39150   -21.14629 -7.43246  1.000 19.23427 ?  41  LYS   A NZ  1 
ATOM   212  N N   . GLU   A 1 35  ? 0.32159   -16.24813 -6.33829  1.000 14.79153 ?  42  GLU   A N   1 
ATOM   213  C CA  . GLU   A 1 35  ? -0.99363  -16.00520 -6.94577  1.000 13.01019 ?  42  GLU   A CA  1 
ATOM   214  C C   . GLU   A 1 35  ? -0.99742  -14.79137 -7.85885  1.000 16.20423 ?  42  GLU   A C   1 
ATOM   215  O O   . GLU   A 1 35  ? -1.96675  -14.63120 -8.63796  1.000 15.73328 ?  42  GLU   A O   1 
ATOM   216  C CB  . GLU   A 1 35  ? -2.01522  -15.82143 -5.80446  1.000 16.79422 ?  42  GLU   A CB  1 
ATOM   217  C CG  . GLU   A 1 35  ? -1.85899  -14.51135 -5.04104  1.000 17.13158 ?  42  GLU   A CG  1 
ATOM   218  C CD  . GLU   A 1 35  ? -2.74866  -14.43317 -3.78866  1.000 22.49381 ?  42  GLU   A CD  1 
ATOM   219  O OE1 . GLU   A 1 35  ? -2.82893  -15.41053 -3.06097  1.000 26.38997 ?  42  GLU   A OE1 1 
ATOM   220  O OE2 . GLU   A 1 35  ? -3.31025  -13.38325 -3.54408  1.000 28.86009 ?  42  GLU   A OE2 1 
ATOM   221  N N   . ILE   A 1 36  ? -0.00773  -13.88557 -7.71503  1.000 14.36319 ?  43  ILE   A N   1 
ATOM   222  C CA  . ILE   A 1 36  ? 0.01702   -12.69251 -8.58772  1.000 14.79528 ?  43  ILE   A CA  1 
ATOM   223  C C   . ILE   A 1 36  ? 0.12828   -13.01260 -10.06959 1.000 14.55572 ?  43  ILE   A C   1 
ATOM   224  O O   . ILE   A 1 36  ? -0.13941  -12.10383 -10.88728 1.000 14.51920 ?  43  ILE   A O   1 
ATOM   225  C CB  . ILE   A 1 36  ? 1.15473   -11.72048 -8.19127  1.000 17.93735 ?  43  ILE   A CB  1 
ATOM   226  C CG1 . ILE   A 1 36  ? 2.53667   -12.37931 -8.35384  1.000 18.60376 ?  43  ILE   A CG1 1 
ATOM   227  C CG2 . ILE   A 1 36  ? 0.90208   -11.24419 -6.71557  1.000 20.52952 ?  43  ILE   A CG2 1 
ATOM   228  C CD1 . ILE   A 1 36  ? 3.17407   -12.09357 -9.68820  1.000 21.32374 ?  43  ILE   A CD1 1 
ATOM   229  N N   . PHE   A 1 37  ? 0.48225   -14.24764 -10.44247 1.000 12.04038 ?  44  PHE   A N   1 
ATOM   230  C CA  . PHE   A 1 37  ? 0.49104   -14.55698 -11.88026 1.000 12.79161 ?  44  PHE   A CA  1 
ATOM   231  C C   . PHE   A 1 37  ? -0.85076  -14.21859 -12.51128 1.000 13.65671 ?  44  PHE   A C   1 
ATOM   232  O O   . PHE   A 1 37  ? -0.90829  -13.75965 -13.67646 1.000 13.31528 ?  44  PHE   A O   1 
ATOM   233  C CB  . PHE   A 1 37  ? 0.82255   -16.03615 -12.14166 1.000 14.45398 ?  44  PHE   A CB  1 
ATOM   234  C CG  . PHE   A 1 37  ? -0.35220  -16.94763 -11.94080 1.000 13.22937 ?  44  PHE   A CG  1 
ATOM   235  C CD1 . PHE   A 1 37  ? -0.64693  -17.45083 -10.68476 1.000 15.30463 ?  44  PHE   A CD1 1 
ATOM   236  C CD2 . PHE   A 1 37  ? -1.18294  -17.30773 -13.01350 1.000 15.41643 ?  44  PHE   A CD2 1 
ATOM   237  C CE1 . PHE   A 1 37  ? -1.75420  -18.29257 -10.51090 1.000 14.02108 ?  44  PHE   A CE1 1 
ATOM   238  C CE2 . PHE   A 1 37  ? -2.30231  -18.12023 -12.83685 1.000 15.82837 ?  44  PHE   A CE2 1 
ATOM   239  C CZ  . PHE   A 1 37  ? -2.60178  -18.60339 -11.57221 1.000 14.38858 ?  44  PHE   A CZ  1 
ATOM   240  N N   . LEU   A 1 38  ? -1.96404  -14.47983 -11.78241 1.000 12.39996 ?  45  LEU   A N   1 
ATOM   241  C CA  . LEU   A 1 38  ? -3.26729  -14.33240 -12.44278 1.000 12.14960 ?  45  LEU   A CA  1 
ATOM   242  C C   . LEU   A 1 38  ? -3.57666  -12.85861 -12.64565 1.000 16.01807 ?  45  LEU   A C   1 
ATOM   243  O O   . LEU   A 1 38  ? -4.10803  -12.45043 -13.69727 1.000 13.47842 ?  45  LEU   A O   1 
ATOM   244  C CB  . LEU   A 1 38  ? -4.31894  -15.03369 -11.60630 1.000 12.88003 ?  45  LEU   A CB  1 
ATOM   245  C CG  . LEU   A 1 38  ? -5.73248  -15.07705 -12.21424 1.000 14.22912 ?  45  LEU   A CG  1 
ATOM   246  C CD1 . LEU   A 1 38  ? -5.64975  -15.73945 -13.59902 1.000 14.61104 ?  45  LEU   A CD1 1 
ATOM   247  C CD2 . LEU   A 1 38  ? -6.73961  -15.83685 -11.34355 1.000 16.96155 ?  45  LEU   A CD2 1 
ATOM   248  N N   . ARG   A 1 39  ? -3.20979  -12.03312 -11.66168 1.000 13.85488 ?  46  ARG   A N   1 
ATOM   249  C CA  . ARG   A 1 39  ? -3.36163  -10.59333 -11.82181 1.000 13.25504 ?  46  ARG   A CA  1 
ATOM   250  C C   . ARG   A 1 39  ? -2.58380  -10.12959 -13.04407 1.000 15.43758 ?  46  ARG   A C   1 
ATOM   251  O O   . ARG   A 1 39  ? -3.06637  -9.31280  -13.85102 1.000 16.21047 ?  46  ARG   A O   1 
ATOM   252  C CB  . ARG   A 1 39  ? -2.84816  -9.90658  -10.57126 1.000 15.11783 ?  46  ARG   A CB  1 
ATOM   253  C CG  . ARG   A 1 39  ? -2.78290  -8.40022  -10.77938 1.000 20.25911 ?  46  ARG   A CG  1 
ATOM   254  C CD  . ARG   A 1 39  ? -2.10138  -7.74933  -9.53110  1.000 25.14102 ?  46  ARG   A CD  1 
ATOM   255  N NE  . ARG   A 1 39  ? -0.65574  -7.97742  -9.56302  1.000 28.31758 ?  46  ARG   A NE  1 
ATOM   256  C CZ  . ARG   A 1 39  ? 0.14924   -7.84925  -8.51790  1.000 27.28541 ?  46  ARG   A CZ  1 
ATOM   257  N NH1 . ARG   A 1 39  ? -0.28712  -7.40071  -7.34182  1.000 29.35532 ?  46  ARG   A NH1 1 
ATOM   258  N NH2 . ARG   A 1 39  ? 1.42871   -8.16836  -8.65249  1.000 30.05056 ?  46  ARG   A NH2 1 
ATOM   259  N N   . GLU   A 1 40  ? -1.36458  -10.64997 -13.21026 1.000 13.07814 ?  47  GLU   A N   1 
ATOM   260  C CA  . GLU   A 1 40  ? -0.53856  -10.14169 -14.30466 1.000 11.68314 ?  47  GLU   A CA  1 
ATOM   261  C C   . GLU   A 1 40  ? -1.11560  -10.55182 -15.65418 1.000 14.33862 ?  47  GLU   A C   1 
ATOM   262  O O   . GLU   A 1 40  ? -1.05999  -9.75797  -16.62038 1.000 15.72805 ?  47  GLU   A O   1 
ATOM   263  C CB  . GLU   A 1 40  ? 0.90931   -10.66829 -14.16182 1.000 12.48548 ?  47  GLU   A CB  1 
ATOM   264  C CG  . GLU   A 1 40  ? 1.54678   -10.18692 -12.88967 1.000 13.74435 ?  47  GLU   A CG  1 
ATOM   265  C CD  . GLU   A 1 40  ? 1.51352   -8.67209  -12.75633 1.000 19.39400 ?  47  GLU   A CD  1 
ATOM   266  O OE1 . GLU   A 1 40  ? 1.66152   -7.92373  -13.75417 1.000 19.55746 ?  47  GLU   A OE1 1 
ATOM   267  O OE2 . GLU   A 1 40  ? 1.40150   -8.21413  -11.57235 1.000 24.17761 ?  47  GLU   A OE2 1 
ATOM   268  N N   . LEU   A 1 41  ? -1.63924  -11.78408 -15.76344 1.000 12.40485 ?  48  LEU   A N   1 
ATOM   269  C CA  . LEU   A 1 41  ? -2.20437  -12.19938 -17.06074 1.000 14.18436 ?  48  LEU   A CA  1 
ATOM   270  C C   . LEU   A 1 41  ? -3.49139  -11.47729 -17.34921 1.000 15.49689 ?  48  LEU   A C   1 
ATOM   271  O O   . LEU   A 1 41  ? -3.77657  -11.13252 -18.51047 1.000 14.35449 ?  48  LEU   A O   1 
ATOM   272  C CB  . LEU   A 1 41  ? -2.41927  -13.71189 -17.10273 1.000 13.48453 ?  48  LEU   A CB  1 
ATOM   273  C CG  . LEU   A 1 41  ? -1.07247  -14.47323 -17.00770 1.000 13.55122 ?  48  LEU   A CG  1 
ATOM   274  C CD1 . LEU   A 1 41  ? -1.35625  -15.96973 -16.88602 1.000 15.06253 ?  48  LEU   A CD1 1 
ATOM   275  C CD2 . LEU   A 1 41  ? -0.07152  -14.24603 -18.21897 1.000 14.86278 ?  48  LEU   A CD2 1 
ATOM   276  N N   . ILE   A 1 42  ? -4.31688  -11.27774 -16.32710 1.000 12.54480 ?  49  ILE   A N   1 
ATOM   277  C CA  . ILE   A 1 42  ? -5.54304  -10.52290 -16.54035 1.000 13.16880 ?  49  ILE   A CA  1 
ATOM   278  C C   . ILE   A 1 42  ? -5.22632  -9.09038  -16.96244 1.000 13.89806 ?  49  ILE   A C   1 
ATOM   279  O O   . ILE   A 1 42  ? -5.91511  -8.52640  -17.83474 1.000 14.15845 ?  49  ILE   A O   1 
ATOM   280  C CB  . ILE   A 1 42  ? -6.43528  -10.60127 -15.28903 1.000 12.06813 ?  49  ILE   A CB  1 
ATOM   281  C CG1 . ILE   A 1 42  ? -6.99231  -12.01388 -15.21430 1.000 12.19430 ?  49  ILE   A CG1 1 
ATOM   282  C CG2 . ILE   A 1 42  ? -7.58327  -9.56382  -15.36999 1.000 14.34549 ?  49  ILE   A CG2 1 
ATOM   283  C CD1 . ILE   A 1 42  ? -7.78356  -12.28630 -13.81945 1.000 14.24399 ?  49  ILE   A CD1 1 
ATOM   284  N N   . SER   A 1 43  ? -4.18421  -8.47428  -16.35612 1.000 13.57185 ?  50  SER   A N   1 
ATOM   285  C CA  . SER   A 1 43  ? -3.77278  -7.14092  -16.74748 1.000 12.37417 ?  50  SER   A CA  1 
ATOM   286  C C   . SER   A 1 43  ? -3.29404  -7.14001  -18.19803 1.000 12.97837 ?  50  SER   A C   1 
ATOM   287  O O   . SER   A 1 43  ? -3.64590  -6.22937  -18.96691 1.000 13.56736 ?  50  SER   A O   1 
ATOM   288  C CB  . SER   A 1 43  ? -2.66446  -6.68937  -15.78646 1.000 18.50133 ?  50  SER   A CB  1 
ATOM   289  O OG  . SER   A 1 43  ? -2.12119  -5.45526  -16.24909 1.000 25.02955 ?  50  SER   A OG  1 
ATOM   290  N N   . ASN   A 1 44  ? -2.57424  -8.16848  -18.61695 1.000 12.22005 ?  51  ASN   A N   1 
ATOM   291  C CA  . ASN   A 1 44  ? -2.16228  -8.22300  -20.01765 1.000 12.72835 ?  51  ASN   A CA  1 
ATOM   292  C C   . ASN   A 1 44  ? -3.36327  -8.34644  -20.93497 1.000 14.74183 ?  51  ASN   A C   1 
ATOM   293  O O   . ASN   A 1 44  ? -3.43220  -7.67013  -21.99165 1.000 13.79384 ?  51  ASN   A O   1 
ATOM   294  C CB  . ASN   A 1 44  ? -1.23862  -9.43027  -20.26400 1.000 15.10297 ?  51  ASN   A CB  1 
ATOM   295  C CG  . ASN   A 1 44  ? 0.12176   -9.21377  -19.72898 1.000 19.08018 ?  51  ASN   A CG  1 
ATOM   296  O OD1 . ASN   A 1 44  ? 0.44434   -8.11037  -19.24143 1.000 18.75370 ?  51  ASN   A OD1 1 
ATOM   297  N ND2 . ASN   A 1 44  ? 0.95576   -10.24573 -19.81995 1.000 19.32206 ?  51  ASN   A ND2 1 
ATOM   298  N N   . SER   A 1 45  ? -4.35395  -9.13493  -20.50810 1.000 12.29380 ?  52  SER   A N   1 
ATOM   299  C CA  . SER   A 1 45  ? -5.56199  -9.25155  -21.33236 1.000 14.81501 ?  52  SER   A CA  1 
ATOM   300  C C   . SER   A 1 45  ? -6.27209  -7.90879  -21.42235 1.000 13.51683 ?  52  SER   A C   1 
ATOM   301  O O   . SER   A 1 45  ? -6.78209  -7.53671  -22.47887 1.000 12.36107 ?  52  SER   A O   1 
ATOM   302  C CB  . SER   A 1 45  ? -6.50445  -10.31528 -20.73057 1.000 13.81616 ?  52  SER   A CB  1 
ATOM   303  O OG  . SER   A 1 45  ? -5.95954  -11.61972 -20.88698 1.000 15.48724 ?  52  SER   A OG  1 
ATOM   304  N N   . SER   A 1 46  ? -6.40134  -7.19892  -20.28469 1.000 12.74628 ?  53  SER   A N   1 
ATOM   305  C CA  . SER   A 1 46  ? -7.03607  -5.88254  -20.30298 1.000 14.15758 ?  53  SER   A CA  1 
ATOM   306  C C   . SER   A 1 46  ? -6.28895  -4.93697  -21.23840 1.000 15.15858 ?  53  SER   A C   1 
ATOM   307  O O   . SER   A 1 46  ? -6.90753  -4.21919  -22.03238 1.000 14.32641 ?  53  SER   A O   1 
ATOM   308  C CB  . SER   A 1 46  ? -7.08740  -5.34159  -18.86078 1.000 15.67949 ?  53  SER   A CB  1 
ATOM   309  O OG  . SER   A 1 46  ? -7.68925  -4.02077  -18.84886 1.000 15.06460 ?  53  SER   A OG  1 
ATOM   310  N N   . ASP   A 1 47  ? -4.94885  -4.97886  -21.22740 1.000 14.35340 ?  54  ASP   A N   1 
ATOM   311  C CA  . ASP   A 1 47  ? -4.20956  -4.10496  -22.11919 1.000 13.04253 ?  54  ASP   A CA  1 
ATOM   312  C C   . ASP   A 1 47  ? -4.49517  -4.45441  -23.57734 1.000 15.76245 ?  54  ASP   A C   1 
ATOM   313  O O   . ASP   A 1 47  ? -4.60815  -3.53664  -24.42793 1.000 15.33345 ?  54  ASP   A O   1 
ATOM   314  C CB  . ASP   A 1 47  ? -2.71783  -4.24194  -21.85414 1.000 13.33939 ?  54  ASP   A CB  1 
ATOM   315  C CG  . ASP   A 1 47  ? -2.29591  -3.59241  -20.54280 1.000 20.84704 ?  54  ASP   A CG  1 
ATOM   316  O OD1 . ASP   A 1 47  ? -3.11108  -2.83472  -19.91022 1.000 18.21774 ?  54  ASP   A OD1 1 
ATOM   317  O OD2 . ASP   A 1 47  ? -1.12946  -3.81915  -20.12199 1.000 19.59187 ?  54  ASP   A OD2 1 
ATOM   318  N N   . ALA   A 1 48  ? -4.61941  -5.77382  -23.88176 1.000 13.94145 ?  55  ALA   A N   1 
ATOM   319  C CA  . ALA   A 1 48  ? -4.88972  -6.18060  -25.25995 1.000 12.50095 ?  55  ALA   A CA  1 
ATOM   320  C C   . ALA   A 1 48  ? -6.28346  -5.75971  -25.69588 1.000 12.79119 ?  55  ALA   A C   1 
ATOM   321  O O   . ALA   A 1 48  ? -6.51841  -5.44209  -26.86358 1.000 12.71202 ?  55  ALA   A O   1 
ATOM   322  C CB  . ALA   A 1 48  ? -4.70759  -7.71407  -25.38898 1.000 13.51906 ?  55  ALA   A CB  1 
ATOM   323  N N   . LEU   A 1 49  ? -7.23969  -5.86712  -24.77745 1.000 11.87935 ?  56  LEU   A N   1 
ATOM   324  C CA  . LEU   A 1 49  ? -8.60293  -5.43612  -25.08110 1.000 12.49638 ?  56  LEU   A CA  1 
ATOM   325  C C   . LEU   A 1 49  ? -8.66240  -3.93317  -25.29520 1.000 12.55716 ?  56  LEU   A C   1 
ATOM   326  O O   . LEU   A 1 49  ? -9.33358  -3.46225  -26.21149 1.000 14.20126 ?  56  LEU   A O   1 
ATOM   327  C CB  . LEU   A 1 49  ? -9.52930  -5.86652  -23.93472 1.000 15.00713 ?  56  LEU   A CB  1 
ATOM   328  C CG  . LEU   A 1 49  ? -9.79451  -7.38465  -23.93618 1.000 13.56409 ?  56  LEU   A CG  1 
ATOM   329  C CD1 . LEU   A 1 49  ? -10.25088 -7.84201  -22.51080 1.000 14.57597 ?  56  LEU   A CD1 1 
ATOM   330  C CD2 . LEU   A 1 49  ? -10.86558 -7.74972  -24.93248 1.000 15.19938 ?  56  LEU   A CD2 1 
ATOM   331  N N   . ASP   A 1 50  ? -7.93139  -3.16962  -24.47688 1.000 12.82371 ?  57  ASP   A N   1 
ATOM   332  C CA  . ASP   A 1 50  ? -7.89585  -1.72232  -24.67979 1.000 15.28083 ?  57  ASP   A CA  1 
ATOM   333  C C   . ASP   A 1 50  ? -7.39714  -1.39332  -26.08032 1.000 16.61194 ?  57  ASP   A C   1 
ATOM   334  O O   . ASP   A 1 50  ? -7.89379  -0.45990  -26.70908 1.000 14.99962 ?  57  ASP   A O   1 
ATOM   335  C CB  . ASP   A 1 50  ? -6.95796  -1.04003  -23.68565 1.000 13.35532 ?  57  ASP   A CB  1 
ATOM   336  C CG  . ASP   A 1 50  ? -7.48073  -1.04104  -22.26836 1.000 14.90869 ?  57  ASP   A CG  1 
ATOM   337  O OD1 . ASP   A 1 50  ? -8.61475  -1.46216  -21.98404 1.000 17.97517 ?  57  ASP   A OD1 1 
ATOM   338  O OD2 . ASP   A 1 50  ? -6.70198  -0.55339  -21.41588 1.000 16.71276 ?  57  ASP   A OD2 1 
ATOM   339  N N   . LYS   A 1 51  ? -6.42433  -2.16394  -26.57930 1.000 12.74101 ?  58  LYS   A N   1 
ATOM   340  C CA  . LYS   A 1 51  ? -5.86960  -1.86474  -27.90276 1.000 13.70784 ?  58  LYS   A CA  1 
ATOM   341  C C   . LYS   A 1 51  ? -6.89403  -2.08633  -29.01173 1.000 15.42732 ?  58  LYS   A C   1 
ATOM   342  O O   . LYS   A 1 51  ? -6.98184  -1.27178  -29.95894 1.000 16.13343 ?  58  LYS   A O   1 
ATOM   343  C CB  . LYS   A 1 51  ? -4.61963  -2.73205  -28.13116 1.000 16.44642 ?  58  LYS   A CB  1 
ATOM   344  C CG  . LYS   A 1 51  ? -3.36725  -2.27352  -27.30479 1.000 16.58306 ?  58  LYS   A CG  1 
ATOM   345  C CD  . LYS   A 1 51  ? -2.21868  -3.31571  -27.48670 1.000 15.34207 ?  58  LYS   A CD  1 
ATOM   346  C CE  . LYS   A 1 51  ? -1.22130  -3.08983  -26.38111 1.000 19.07206 ?  58  LYS   A CE  1 
ATOM   347  N NZ  . LYS   A 1 51  ? -0.15522  -4.13276  -26.48492 1.000 24.85233 ?  58  LYS   A NZ  1 
ATOM   348  N N   . ILE   A 1 52  ? -7.61904  -3.21776  -28.98758 1.000 14.67148 ?  59  ILE   A N   1 
ATOM   349  C CA  . ILE   A 1 52  ? -8.57455  -3.39162  -30.07236 1.000 14.83813 ?  59  ILE   A CA  1 
ATOM   350  C C   . ILE   A 1 52  ? -9.73647  -2.44864  -29.90676 1.000 14.71546 ?  59  ILE   A C   1 
ATOM   351  O O   . ILE   A 1 52  ? -10.26220 -1.93155  -30.90477 1.000 16.64389 ?  59  ILE   A O   1 
ATOM   352  C CB  . ILE   A 1 52  ? -9.04409  -4.84591  -30.19913 1.000 15.89911 ?  59  ILE   A CB  1 
ATOM   353  C CG1 . ILE   A 1 52  ? -9.87865  -5.07137  -31.46940 1.000 17.25286 ?  59  ILE   A CG1 1 
ATOM   354  C CG2 . ILE   A 1 52  ? -9.81691  -5.26704  -28.94174 1.000 15.52398 ?  59  ILE   A CG2 1 
ATOM   355  C CD1 . ILE   A 1 52  ? -9.08779  -4.85262  -32.78408 1.000 20.76293 ?  59  ILE   A CD1 1 
ATOM   356  N N   . ARG   A 1 53  ? -10.10708 -2.10479  -28.66603 1.000 15.33561 ?  60  ARG   A N   1 
ATOM   357  C CA  . ARG   A 1 53  ? -11.15687 -1.10286  -28.50634 1.000 15.00531 ?  60  ARG   A CA  1 
ATOM   358  C C   . ARG   A 1 53  ? -10.72928 0.23267   -29.12290 1.000 15.06803 ?  60  ARG   A C   1 
ATOM   359  O O   . ARG   A 1 53  ? -11.49602 0.86375   -29.86188 1.000 16.79991 ?  60  ARG   A O   1 
ATOM   360  C CB  . ARG   A 1 53  ? -11.49379 -0.88300  -27.02329 1.000 16.97461 ?  60  ARG   A CB  1 
ATOM   361  C CG  . ARG   A 1 53  ? -12.59322 0.22669   -26.93317 1.000 22.81151 ?  60  ARG   A CG  1 
ATOM   362  C CD  . ARG   A 1 53  ? -13.10774 0.36685   -25.55449 1.000 30.13051 ?  60  ARG   A CD  1 
ATOM   363  N NE  . ARG   A 1 53  ? -14.10159 -0.63439  -25.17677 1.000 38.29301 ?  60  ARG   A NE  1 
ATOM   364  C CZ  . ARG   A 1 53  ? -14.24509 -1.02765  -23.91778 1.000 42.23109 ?  60  ARG   A CZ  1 
ATOM   365  N NH1 . ARG   A 1 53  ? -13.38520 -0.65370  -22.98553 1.000 31.50174 ?  60  ARG   A NH1 1 
ATOM   366  N NH2 . ARG   A 1 53  ? -15.24448 -1.84494  -23.59430 1.000 38.05905 ?  60  ARG   A NH2 1 
ATOM   367  N N   . TYR   A 1 54  ? -9.47417  0.66428   -28.87034 1.000 14.57243 ?  61  TYR   A N   1 
ATOM   368  C CA  . TYR   A 1 54  ? -9.00388  1.93084   -29.43151 1.000 15.15783 ?  61  TYR   A CA  1 
ATOM   369  C C   . TYR   A 1 54  ? -9.04112  1.90391   -30.95181 1.000 16.93136 ?  61  TYR   A C   1 
ATOM   370  O O   . TYR   A 1 54  ? -9.50999  2.86292   -31.58482 1.000 18.41574 ?  61  TYR   A O   1 
ATOM   371  C CB  . TYR   A 1 54  ? -7.59551  2.22402   -28.95376 1.000 15.28489 ?  61  TYR   A CB  1 
ATOM   372  C CG  . TYR   A 1 54  ? -7.15312  3.60045   -29.45419 1.000 18.91505 ?  61  TYR   A CG  1 
ATOM   373  C CD1 . TYR   A 1 54  ? -7.65101  4.74679   -28.91191 1.000 17.56735 ?  61  TYR   A CD1 1 
ATOM   374  C CD2 . TYR   A 1 54  ? -6.27925  3.69205   -30.49717 1.000 18.63332 ?  61  TYR   A CD2 1 
ATOM   375  C CE1 . TYR   A 1 54  ? -7.27983  5.96983   -29.37242 1.000 19.05768 ?  61  TYR   A CE1 1 
ATOM   376  C CE2 . TYR   A 1 54  ? -5.87856  4.92360   -30.99846 1.000 21.31640 ?  61  TYR   A CE2 1 
ATOM   377  C CZ  . TYR   A 1 54  ? -6.38354  6.06524   -30.42951 1.000 19.53611 ?  61  TYR   A CZ  1 
ATOM   378  O OH  . TYR   A 1 54  ? -6.01486  7.30121   -30.87834 1.000 21.38444 ?  61  TYR   A OH  1 
ATOM   379  N N   . GLU   A 1 55  ? -8.54696  0.81941   -31.54268 1.000 16.62191 ?  62  GLU   A N   1 
ATOM   380  C CA  . GLU   A 1 55  ? -8.58942  0.75159   -33.00924 1.000 18.74185 ?  62  GLU   A CA  1 
ATOM   381  C C   . GLU   A 1 55  ? -10.00723 0.77370   -33.53248 1.000 21.60729 ?  62  GLU   A C   1 
ATOM   382  O O   . GLU   A 1 55  ? -10.26678 1.35420   -34.59931 1.000 21.68139 ?  62  GLU   A O   1 
ATOM   383  C CB  . GLU   A 1 55  ? -7.88226  -0.49270  -33.51930 1.000 19.55325 ?  62  GLU   A CB  1 
ATOM   384  C CG  . GLU   A 1 55  ? -6.38170  -0.38263  -33.32143 1.000 22.24894 ?  62  GLU   A CG  1 
ATOM   385  C CD  . GLU   A 1 55  ? -5.63709  -1.50846  -34.02022 1.000 38.60069 ?  62  GLU   A CD  1 
ATOM   386  O OE1 . GLU   A 1 55  ? -4.39063  -1.41814  -34.11495 1.000 42.96287 ?  62  GLU   A OE1 1 
ATOM   387  O OE2 . GLU   A 1 55  ? -6.27921  -2.47547  -34.48570 1.000 35.11511 ?  62  GLU   A OE2 1 
ATOM   388  N N   . SER   A 1 56  ? -10.93864 0.15498   -32.82466 1.000 18.47637 ?  63  SER   A N   1 
ATOM   389  C CA  . SER   A 1 56  ? -12.32107 0.14325   -33.29614 1.000 19.45775 ?  63  SER   A CA  1 
ATOM   390  C C   . SER   A 1 56  ? -12.95156 1.53330   -33.26362 1.000 20.64471 ?  63  SER   A C   1 
ATOM   391  O O   . SER   A 1 56  ? -13.97680 1.76377   -33.92586 1.000 24.66192 ?  63  SER   A O   1 
ATOM   392  C CB  . SER   A 1 56  ? -13.12420 -0.85658  -32.45857 1.000 20.93138 ?  63  SER   A CB  1 
ATOM   393  O OG  . SER   A 1 56  ? -13.52477 -0.30117  -31.18814 1.000 24.02631 ?  63  SER   A OG  1 
ATOM   394  N N   . LEU   A 1 57  ? -12.39773 2.47562   -32.48738 1.000 20.54888 ?  64  LEU   A N   1 
ATOM   395  C CA  . LEU   A 1 57  ? -13.03665 3.79244   -32.39868 1.000 25.99613 ?  64  LEU   A CA  1 
ATOM   396  C C   . LEU   A 1 57  ? -13.06762 4.48716   -33.73871 1.000 25.04992 ?  64  LEU   A C   1 
ATOM   397  O O   . LEU   A 1 57  ? -13.92475 5.33936   -33.97238 1.000 31.93480 ?  64  LEU   A O   1 
ATOM   398  C CB  . LEU   A 1 57  ? -12.29136 4.70117   -31.40767 1.000 21.40194 ?  64  LEU   A CB  1 
ATOM   399  C CG  . LEU   A 1 57  ? -12.38256 4.18322   -29.97372 1.000 24.94203 ?  64  LEU   A CG  1 
ATOM   400  C CD1 . LEU   A 1 57  ? -11.72391 5.17150   -28.99037 1.000 21.33926 ?  64  LEU   A CD1 1 
ATOM   401  C CD2 . LEU   A 1 57  ? -13.81084 3.93006   -29.52655 1.000 26.56062 ?  64  LEU   A CD2 1 
ATOM   402  N N   . THR   A 1 58  ? -12.07956 4.23897   -34.57687 1.000 22.30076 ?  65  THR   A N   1 
ATOM   403  C CA  . THR   A 1 58  ? -12.01119 4.87747   -35.88610 1.000 26.87532 ?  65  THR   A CA  1 
ATOM   404  C C   . THR   A 1 58  ? -12.23962 3.89267   -37.01626 1.000 26.08953 ?  65  THR   A C   1 
ATOM   405  O O   . THR   A 1 58  ? -12.31947 4.29835   -38.18377 1.000 30.62761 ?  65  THR   A O   1 
ATOM   406  C CB  . THR   A 1 58  ? -10.64258 5.54921   -36.06505 1.000 31.69964 ?  65  THR   A CB  1 
ATOM   407  O OG1 . THR   A 1 58  ? -9.61554  4.56227   -35.97181 1.000 31.85688 ?  65  THR   A OG1 1 
ATOM   408  C CG2 . THR   A 1 58  ? -10.41724 6.66801   -35.04520 1.000 29.31832 ?  65  THR   A CG2 1 
ATOM   409  N N   . ASP   A 1 59  ? -12.37813 2.60985   -36.71838 1.000 28.53689 ?  66  ASP   A N   1 
ATOM   410  C CA  . ASP   A 1 59  ? -12.54862 1.60677   -37.77117 1.000 26.63573 ?  66  ASP   A CA  1 
ATOM   411  C C   . ASP   A 1 59  ? -13.38235 0.48616   -37.18672 1.000 26.88532 ?  66  ASP   A C   1 
ATOM   412  O O   . ASP   A 1 59  ? -12.85544 -0.49567  -36.64225 1.000 26.13944 ?  66  ASP   A O   1 
ATOM   413  C CB  . ASP   A 1 59  ? -11.19496 1.10994   -38.27446 1.000 28.07340 ?  66  ASP   A CB  1 
ATOM   414  C CG  . ASP   A 1 59  ? -11.33744 0.10863   -39.41224 1.000 35.22353 ?  66  ASP   A CG  1 
ATOM   415  O OD1 . ASP   A 1 59  ? -12.47157 -0.15856  -39.80751 1.000 30.70415 ?  66  ASP   A OD1 1 
ATOM   416  O OD2 . ASP   A 1 59  ? -10.31051 -0.42110  -39.87612 1.000 32.72088 ?  66  ASP   A OD2 1 
ATOM   417  N N   . PRO   A 1 60  ? -14.70960 0.61054   -37.24845 1.000 30.60375 ?  67  PRO   A N   1 
ATOM   418  C CA  . PRO   A 1 60  ? -15.56015 -0.40842  -36.63063 1.000 29.59618 ?  67  PRO   A CA  1 
ATOM   419  C C   . PRO   A 1 60  ? -15.32315 -1.80434  -37.19769 1.000 27.52837 ?  67  PRO   A C   1 
ATOM   420  O O   . PRO   A 1 60  ? -15.57557 -2.77983  -36.48672 1.000 28.09493 ?  67  PRO   A O   1 
ATOM   421  C CB  . PRO   A 1 60  ? -16.98172 0.05964   -36.95807 1.000 37.47762 ?  67  PRO   A CB  1 
ATOM   422  C CG  . PRO   A 1 60  ? -16.88147 1.41480   -37.49778 1.000 42.23626 ?  67  PRO   A CG  1 
ATOM   423  C CD  . PRO   A 1 60  ? -15.45024 1.84184   -37.55856 1.000 34.78533 ?  67  PRO   A CD  1 
ATOM   424  N N   . SER   A 1 61  ? -14.90584 -1.93449  -38.47309 1.000 28.42200 ?  68  SER   A N   1 
ATOM   425  C CA  . SER   A 1 61  ? -14.65598 -3.26441  -39.02577 1.000 27.60968 ?  68  SER   A CA  1 
ATOM   426  C C   . SER   A 1 61  ? -13.55926 -4.02709  -38.27997 1.000 26.63584 ?  68  SER   A C   1 
ATOM   427  O O   . SER   A 1 61  ? -13.43624 -5.23825  -38.46789 1.000 25.53187 ?  68  SER   A O   1 
ATOM   428  C CB  . SER   A 1 61  ? -14.26391 -3.17113  -40.50675 1.000 27.03192 ?  68  SER   A CB  1 
ATOM   429  O OG  . SER   A 1 61  ? -12.90492 -2.76426  -40.62893 1.000 31.04710 ?  68  SER   A OG  1 
ATOM   430  N N   . LYS   A 1 62  ? -12.77281 -3.37320  -37.40608 1.000 21.75777 ?  69  LYS   A N   1 
ATOM   431  C CA  . LYS   A 1 62  ? -11.80009 -4.12390  -36.64589 1.000 23.71141 ?  69  LYS   A CA  1 
ATOM   432  C C   . LYS   A 1 62  ? -12.48032 -5.11326  -35.70413 1.000 23.84230 ?  69  LYS   A C   1 
ATOM   433  O O   . LYS   A 1 62  ? -11.84569 -6.04378  -35.20006 1.000 21.99279 ?  69  LYS   A O   1 
ATOM   434  C CB  . LYS   A 1 62  ? -10.92288 -3.14842  -35.87092 1.000 26.66308 ?  69  LYS   A CB  1 
ATOM   435  C CG  . LYS   A 1 62  ? -10.13080 -2.34543  -36.85695 1.000 30.98338 ?  69  LYS   A CG  1 
ATOM   436  C CD  . LYS   A 1 62  ? -8.70299  -2.54764  -36.68535 1.000 27.61126 ?  69  LYS   A CD  1 
ATOM   437  C CE  . LYS   A 1 62  ? -7.89682  -1.81178  -37.73383 1.000 31.85839 ?  69  LYS   A CE  1 
ATOM   438  N NZ  . LYS   A 1 62  ? -6.62555  -2.56486  -37.69579 1.000 33.02480 ?  69  LYS   A NZ  1 
ATOM   439  N N   . LEU   A 1 63  ? -13.77280 -4.93041  -35.44737 1.000 21.91751 ?  70  LEU   A N   1 
ATOM   440  C CA  . LEU   A 1 63  ? -14.46367 -5.85941  -34.58485 1.000 21.59302 ?  70  LEU   A CA  1 
ATOM   441  C C   . LEU   A 1 63  ? -15.26192 -6.87991  -35.38102 1.000 21.34908 ?  70  LEU   A C   1 
ATOM   442  O O   . LEU   A 1 63  ? -15.98670 -7.66034  -34.77266 1.000 27.35099 ?  70  LEU   A O   1 
ATOM   443  C CB  . LEU   A 1 63  ? -15.36995 -5.10933  -33.60409 1.000 25.76755 ?  70  LEU   A CB  1 
ATOM   444  C CG  . LEU   A 1 63  ? -14.65902 -4.16674  -32.61253 1.000 26.86965 ?  70  LEU   A CG  1 
ATOM   445  C CD1 . LEU   A 1 63  ? -15.68147 -3.39704  -31.74432 1.000 26.71515 ?  70  LEU   A CD1 1 
ATOM   446  C CD2 . LEU   A 1 63  ? -13.73455 -4.92084  -31.71576 1.000 25.22691 ?  70  LEU   A CD2 1 
ATOM   447  N N   . ASP   A 1 64  ? -15.03517 -6.97044  -36.69024 1.000 23.96044 ?  71  ASP   A N   1 
ATOM   448  C CA  . ASP   A 1 64  ? -15.73580 -7.98732  -37.46382 1.000 28.21299 ?  71  ASP   A CA  1 
ATOM   449  C C   . ASP   A 1 64  ? -15.38682 -9.37929  -36.98925 1.000 22.76092 ?  71  ASP   A C   1 
ATOM   450  O O   . ASP   A 1 64  ? -16.17824 -10.30829 -37.18525 1.000 29.53316 ?  71  ASP   A O   1 
ATOM   451  C CB  . ASP   A 1 64  ? -15.42103 -7.85207  -38.95355 1.000 30.09474 ?  71  ASP   A CB  1 
ATOM   452  C CG  . ASP   A 1 64  ? -16.13312 -6.64596  -39.59659 1.000 33.54297 ?  71  ASP   A CG  1 
ATOM   453  O OD1 . ASP   A 1 64  ? -16.96716 -6.01350  -38.89910 1.000 33.61295 ?  71  ASP   A OD1 1 
ATOM   454  O OD2 . ASP   A 1 64  ? -15.88356 -6.34152  -40.78468 1.000 34.36849 ?  71  ASP   A OD2 1 
ATOM   455  N N   . SER   A 1 65  ? -14.20178 -9.54718  -36.38716 1.000 24.25722 ?  72  SER   A N   1 
ATOM   456  C CA  . SER   A 1 65  ? -13.71492 -10.81384 -35.84947 1.000 24.25437 ?  72  SER   A CA  1 
ATOM   457  C C   . SER   A 1 65  ? -14.24231 -11.07921 -34.45464 1.000 28.50291 ?  72  SER   A C   1 
ATOM   458  O O   . SER   A 1 65  ? -13.80150 -12.02796 -33.79986 1.000 29.92805 ?  72  SER   A O   1 
ATOM   459  C CB  . SER   A 1 65  ? -12.18043 -10.81022 -35.85100 1.000 23.67964 ?  72  SER   A CB  1 
ATOM   460  O OG  . SER   A 1 65  ? -11.74853 -9.54770  -35.33115 1.000 21.46503 ?  72  SER   A OG  1 
ATOM   461  N N   . GLY   A 1 66  ? -15.15109 -10.23809 -33.96799 1.000 22.82964 ?  73  GLY   A N   1 
ATOM   462  C CA  . GLY   A 1 66  ? -15.71861 -10.50233 -32.65978 1.000 24.47613 ?  73  GLY   A CA  1 
ATOM   463  C C   . GLY   A 1 66  ? -16.02536 -9.18878  -31.95737 1.000 26.09337 ?  73  GLY   A C   1 
ATOM   464  O O   . GLY   A 1 66  ? -15.09700 -8.43645  -31.67415 1.000 22.91596 ?  73  GLY   A O   1 
ATOM   465  N N   . LYS   A 1 67  ? -17.30219 -8.88778  -31.66201 1.000 24.75631 ?  74  LYS   A N   1 
ATOM   466  C CA  . LYS   A 1 67  ? -17.59924 -7.60334  -31.02283 1.000 22.95644 ?  74  LYS   A CA  1 
ATOM   467  C C   . LYS   A 1 67  ? -17.40868 -7.62882  -29.51111 1.000 20.63462 ?  74  LYS   A C   1 
ATOM   468  O O   . LYS   A 1 67  ? -17.16698 -6.57805  -28.90445 1.000 26.69851 ?  74  LYS   A O   1 
ATOM   469  C CB  . LYS   A 1 67  ? -19.06851 -7.18968  -31.32430 1.000 27.61285 ?  74  LYS   A CB  1 
ATOM   470  C CG  . LYS   A 1 67  ? -19.29393 -6.76461  -32.77112 1.000 40.25310 ?  74  LYS   A CG  1 
ATOM   471  C CD  . LYS   A 1 67  ? -20.33641 -5.65260  -32.88937 1.000 54.51036 ?  74  LYS   A CD  1 
ATOM   472  C CE  . LYS   A 1 67  ? -20.88643 -5.59143  -34.30017 1.000 60.11807 ?  74  LYS   A CE  1 
ATOM   473  N NZ  . LYS   A 1 67  ? -19.81081 -5.63730  -35.31112 1.000 53.42811 ?  74  LYS   A NZ  1 
ATOM   474  N N   . GLU   A 1 68  ? -17.50971 -8.78394  -28.87369 1.000 21.61323 ?  75  GLU   A N   1 
ATOM   475  C CA  . GLU   A 1 68  ? -17.52093 -8.77747  -27.40614 1.000 20.28608 ?  75  GLU   A CA  1 
ATOM   476  C C   . GLU   A 1 68  ? -16.10434 -8.71391  -26.88290 1.000 21.61229 ?  75  GLU   A C   1 
ATOM   477  O O   . GLU   A 1 68  ? -15.25890 -9.46603  -27.34978 1.000 21.41394 ?  75  GLU   A O   1 
ATOM   478  C CB  . GLU   A 1 68  ? -18.25005 -10.00320 -26.87140 1.000 32.57107 ?  75  GLU   A CB  1 
ATOM   479  C CG  . GLU   A 1 68  ? -18.64199 -9.82855  -25.41044 1.000 48.07763 ?  75  GLU   A CG  1 
ATOM   480  C CD  . GLU   A 1 68  ? -19.02245 -11.13505 -24.73526 1.000 58.96391 ?  75  GLU   A CD  1 
ATOM   481  O OE1 . GLU   A 1 68  ? -19.40040 -12.09545 -25.46957 1.000 63.91021 ?  75  GLU   A OE1 1 
ATOM   482  O OE2 . GLU   A 1 68  ? -18.91990 -11.19527 -23.48329 1.000 53.59461 ?  75  GLU   A OE2 1 
ATOM   483  N N   . LEU   A 1 69  ? -15.86591 -7.81890  -25.93097 1.000 16.41034 ?  76  LEU   A N   1 
ATOM   484  C CA  . LEU   A 1 69  ? -14.53860 -7.61166  -25.33180 1.000 15.18901 ?  76  LEU   A CA  1 
ATOM   485  C C   . LEU   A 1 69  ? -14.63169 -8.15154  -23.91082 1.000 15.12427 ?  76  LEU   A C   1 
ATOM   486  O O   . LEU   A 1 69  ? -15.27808 -7.55341  -23.05449 1.000 16.63170 ?  76  LEU   A O   1 
ATOM   487  C CB  . LEU   A 1 69  ? -14.20079 -6.11952  -25.35788 1.000 16.73209 ?  76  LEU   A CB  1 
ATOM   488  C CG  . LEU   A 1 69  ? -14.16331 -5.53052  -26.77796 1.000 21.02695 ?  76  LEU   A CG  1 
ATOM   489  C CD1 . LEU   A 1 69  ? -13.61066 -4.13346  -26.62851 1.000 24.98572 ?  76  LEU   A CD1 1 
ATOM   490  C CD2 . LEU   A 1 69  ? -13.24383 -6.34004  -27.68140 1.000 18.95090 ?  76  LEU   A CD2 1 
ATOM   491  N N   . HIS   A 1 70  ? -13.99608 -9.29457  -23.66491 1.000 13.71811 ?  77  HIS   A N   1 
ATOM   492  C CA  . HIS   A 1 70  ? -14.13791 -9.93971  -22.37199 1.000 15.50698 ?  77  HIS   A CA  1 
ATOM   493  C C   . HIS   A 1 70  ? -12.95918 -10.86784 -22.10818 1.000 14.16164 ?  77  HIS   A C   1 
ATOM   494  O O   . HIS   A 1 70  ? -12.12911 -11.12614 -22.98215 1.000 13.25382 ?  77  HIS   A O   1 
ATOM   495  C CB  . HIS   A 1 70  ? -15.42456 -10.73924 -22.30779 1.000 17.67955 ?  77  HIS   A CB  1 
ATOM   496  C CG  . HIS   A 1 70  ? -15.47571 -11.87533 -23.27885 1.000 21.99059 ?  77  HIS   A CG  1 
ATOM   497  N ND1 . HIS   A 1 70  ? -16.62765 -12.21280 -23.93047 1.000 44.51010 ?  77  HIS   A ND1 1 
ATOM   498  C CD2 . HIS   A 1 70  ? -14.56609 -12.81483 -23.63753 1.000 25.95022 ?  77  HIS   A CD2 1 
ATOM   499  C CE1 . HIS   A 1 70  ? -16.40822 -13.24353 -24.72030 1.000 26.71081 ?  77  HIS   A CE1 1 
ATOM   500  N NE2 . HIS   A 1 70  ? -15.16938 -13.63176 -24.56389 1.000 26.83134 ?  77  HIS   A NE2 1 
ATOM   501  N N   . ILE   A 1 71  ? -12.93961 -11.38657 -20.88159 1.000 12.54087 ?  78  ILE   A N   1 
ATOM   502  C CA  . ILE   A 1 71  ? -11.93599 -12.33135 -20.39003 1.000 12.72343 ?  78  ILE   A CA  1 
ATOM   503  C C   . ILE   A 1 71  ? -12.65673 -13.53937 -19.77901 1.000 12.37093 ?  78  ILE   A C   1 
ATOM   504  O O   . ILE   A 1 71  ? -13.53705 -13.35739 -18.94293 1.000 14.37881 ?  78  ILE   A O   1 
ATOM   505  C CB  . ILE   A 1 71  ? -11.06809 -11.65095 -19.30215 1.000 13.45368 ?  78  ILE   A CB  1 
ATOM   506  C CG1 . ILE   A 1 71  ? -10.40997 -10.39086 -19.89381 1.000 14.03266 ?  78  ILE   A CG1 1 
ATOM   507  C CG2 . ILE   A 1 71  ? -10.07218 -12.66873 -18.73841 1.000 13.73435 ?  78  ILE   A CG2 1 
ATOM   508  C CD1 . ILE   A 1 71  ? -9.73170  -9.54686  -18.81373 1.000 16.61934 ?  78  ILE   A CD1 1 
ATOM   509  N N   . ASN   A 1 72  ? -12.25696 -14.75048 -20.17913 1.000 11.96513 ?  79  ASN   A N   1 
ATOM   510  C CA  . ASN   A 1 72  ? -12.77824 -15.98463 -19.58903 1.000 10.89843 ?  79  ASN   A CA  1 
ATOM   511  C C   . ASN   A 1 72  ? -11.64552 -16.66849 -18.85386 1.000 15.31246 ?  79  ASN   A C   1 
ATOM   512  O O   . ASN   A 1 72  ? -10.50960 -16.72076 -19.32871 1.000 13.50113 ?  79  ASN   A O   1 
ATOM   513  C CB  . ASN   A 1 72  ? -13.32394 -16.92377 -20.65031 1.000 11.69430 ?  79  ASN   A CB  1 
ATOM   514  C CG  . ASN   A 1 72  ? -14.54181 -16.36837 -21.32695 1.000 13.49450 ?  79  ASN   A CG  1 
ATOM   515  O OD1 . ASN   A 1 72  ? -15.29612 -15.55879 -20.75300 1.000 15.67025 ?  79  ASN   A OD1 1 
ATOM   516  N ND2 . ASN   A 1 72  ? -14.78602 -16.85408 -22.56633 1.000 15.73863 ?  79  ASN   A ND2 1 
ATOM   517  N N   . LEU   A 1 73  ? -11.97872 -17.21585 -17.68614 1.000 12.18347 ?  80  LEU   A N   1 
ATOM   518  C CA  . LEU   A 1 73  ? -11.02022 -18.00735 -16.93393 1.000 10.19480 ?  80  LEU   A CA  1 
ATOM   519  C C   . LEU   A 1 73  ? -11.54881 -19.43088 -16.90092 1.000 10.72864 ?  80  LEU   A C   1 
ATOM   520  O O   . LEU   A 1 73  ? -12.69452 -19.65348 -16.44237 1.000 11.41430 ?  80  LEU   A O   1 
ATOM   521  C CB  . LEU   A 1 73  ? -10.86387 -17.46603 -15.51918 1.000 12.45691 ?  80  LEU   A CB  1 
ATOM   522  C CG  . LEU   A 1 73  ? -10.47221 -15.98499 -15.39517 1.000 12.83233 ?  80  LEU   A CG  1 
ATOM   523  C CD1 . LEU   A 1 73  ? -10.41158 -15.63805 -13.91079 1.000 11.25154 ?  80  LEU   A CD1 1 
ATOM   524  C CD2 . LEU   A 1 73  ? -9.13855  -15.77997 -16.04577 1.000 13.83630 ?  80  LEU   A CD2 1 
ATOM   525  N N   . ILE   A 1 74  ? -10.79704 -20.36411 -17.44493 1.000 12.42091 ?  81  ILE   A N   1 
ATOM   526  C CA  . ILE   A 1 74  ? -11.32316 -21.71999 -17.66090 1.000 14.61571 ?  81  ILE   A CA  1 
ATOM   527  C C   . ILE   A 1 74  ? -10.40512 -22.72234 -16.97288 1.000 13.54984 ?  81  ILE   A C   1 
ATOM   528  O O   . ILE   A 1 74  ? -9.39261  -23.11566 -17.54059 1.000 14.79146 ?  81  ILE   A O   1 
ATOM   529  C CB  . ILE   A 1 74  ? -11.43875 -22.06136 -19.14825 1.000 15.48410 ?  81  ILE   A CB  1 
ATOM   530  C CG1 . ILE   A 1 74  ? -12.19804 -20.94820 -19.86754 1.000 14.68601 ?  81  ILE   A CG1 1 
ATOM   531  C CG2 . ILE   A 1 74  ? -12.14266 -23.42695 -19.32404 1.000 15.23218 ?  81  ILE   A CG2 1 
ATOM   532  C CD1 . ILE   A 1 74  ? -12.28423 -21.15871 -21.37947 1.000 14.38335 ?  81  ILE   A CD1 1 
ATOM   533  N N   . PRO   A 1 75  ? -10.80587 -23.24870 -15.82196 1.000 14.74979 ?  82  PRO   A N   1 
ATOM   534  C CA  . PRO   A 1 75  ? -10.03956 -24.32011 -15.18049 1.000 14.69508 ?  82  PRO   A CA  1 
ATOM   535  C C   . PRO   A 1 75  ? -10.50483 -25.66646 -15.67993 1.000 17.89758 ?  82  PRO   A C   1 
ATOM   536  O O   . PRO   A 1 75  ? -11.66685 -25.88151 -16.01501 1.000 17.52414 ?  82  PRO   A O   1 
ATOM   537  C CB  . PRO   A 1 75  ? -10.38231 -24.15925 -13.69037 1.000 14.93003 ?  82  PRO   A CB  1 
ATOM   538  C CG  . PRO   A 1 75  ? -11.76934 -23.67587 -13.68322 1.000 15.92509 ?  82  PRO   A CG  1 
ATOM   539  C CD  . PRO   A 1 75  ? -11.95005 -22.83719 -15.00311 1.000 17.29478 ?  82  PRO   A CD  1 
ATOM   540  N N   . ASN   A 1 76  ? -9.54936  -26.56019 -15.79782 1.000 16.13342 ?  83  ASN   A N   1 
ATOM   541  C CA  . ASN   A 1 76  ? -9.82334  -27.92816 -16.23888 1.000 16.76164 ?  83  ASN   A CA  1 
ATOM   542  C C   . ASN   A 1 76  ? -8.96367  -28.83933 -15.34825 1.000 21.41460 ?  83  ASN   A C   1 
ATOM   543  O O   . ASN   A 1 76  ? -7.76560  -28.97815 -15.56747 1.000 21.30209 ?  83  ASN   A O   1 
ATOM   544  C CB  . ASN   A 1 76  ? -9.54721  -28.14149 -17.72992 1.000 22.61669 ?  83  ASN   A CB  1 
ATOM   545  C CG  . ASN   A 1 76  ? -10.03603 -29.51819 -18.19036 1.000 28.19337 ?  83  ASN   A CG  1 
ATOM   546  O OD1 . ASN   A 1 76  ? -9.70452  -30.51404 -17.56311 1.000 28.29412 ?  83  ASN   A OD1 1 
ATOM   547  N ND2 . ASN   A 1 76  ? -10.87330 -29.57155 -19.22270 1.000 28.97783 ?  83  ASN   A ND2 1 
ATOM   548  N N   . LYS   A 1 77  ? -9.59559  -29.49829 -14.38717 1.000 18.49273 ?  84  LYS   A N   1 
ATOM   549  C CA  . LYS   A 1 77  ? -8.82604  -30.33395 -13.48079 1.000 18.76862 ?  84  LYS   A CA  1 
ATOM   550  C C   . LYS   A 1 77  ? -8.36837  -31.63602 -14.13086 1.000 22.64542 ?  84  LYS   A C   1 
ATOM   551  O O   . LYS   A 1 77  ? -7.41740  -32.25130 -13.63215 1.000 27.30356 ?  84  LYS   A O   1 
ATOM   552  C CB  . LYS   A 1 77  ? -9.64790  -30.66354 -12.23106 1.000 20.97366 ?  84  LYS   A CB  1 
ATOM   553  C CG  . LYS   A 1 77  ? -9.81344  -29.43713 -11.32222 1.000 24.54810 ?  84  LYS   A CG  1 
ATOM   554  C CD  . LYS   A 1 77  ? -10.70144 -29.79910 -10.15534 1.000 25.78584 ?  84  LYS   A CD  1 
ATOM   555  C CE  . LYS   A 1 77  ? -11.00584 -28.60192 -9.26213  1.000 26.47834 ?  84  LYS   A CE  1 
ATOM   556  N NZ  . LYS   A 1 77  ? -12.06270 -27.75990 -9.85697  1.000 31.93718 ?  84  LYS   A NZ  1 
ATOM   557  N N   . GLN   A 1 78  ? -9.04826  -32.10781 -15.18536 1.000 24.65037 ?  85  GLN   A N   1 
ATOM   558  C CA  . GLN   A 1 78  ? -8.60548  -33.35967 -15.79330 1.000 28.14965 ?  85  GLN   A CA  1 
ATOM   559  C C   . GLN   A 1 78  ? -7.32018  -33.15839 -16.56727 1.000 27.44758 ?  85  GLN   A C   1 
ATOM   560  O O   . GLN   A 1 78  ? -6.46674  -34.06290 -16.59210 1.000 30.73143 ?  85  GLN   A O   1 
ATOM   561  C CB  . GLN   A 1 78  ? -9.67305  -33.98904 -16.70228 1.000 35.29122 ?  85  GLN   A CB  1 
ATOM   562  C CG  . GLN   A 1 78  ? -10.98251 -34.43882 -16.01335 1.000 50.75634 ?  85  GLN   A CG  1 
ATOM   563  C CD  . GLN   A 1 78  ? -11.61042 -33.40281 -15.09144 1.000 64.36778 ?  85  GLN   A CD  1 
ATOM   564  O OE1 . GLN   A 1 78  ? -12.12059 -33.74758 -14.00848 1.000 55.87817 ?  85  GLN   A OE1 1 
ATOM   565  N NE2 . GLN   A 1 78  ? -11.70886 -32.14643 -15.58179 1.000 50.11211 ?  85  GLN   A NE2 1 
ATOM   566  N N   . ASP   A 1 79  ? -7.19051  -32.03026 -17.22517 1.000 23.01738 ?  86  ASP   A N   1 
ATOM   567  C CA  . ASP   A 1 79  ? -5.99392  -31.69758 -17.99780 1.000 22.09488 ?  86  ASP   A CA  1 
ATOM   568  C C   . ASP   A 1 79  ? -4.96952  -30.96804 -17.14944 1.000 21.73191 ?  86  ASP   A C   1 
ATOM   569  O O   . ASP   A 1 79  ? -3.85862  -30.71422 -17.62648 1.000 23.55561 ?  86  ASP   A O   1 
ATOM   570  C CB  . ASP   A 1 79  ? -6.30529  -30.78535 -19.19812 1.000 27.74488 ?  86  ASP   A CB  1 
ATOM   571  C CG  . ASP   A 1 79  ? -7.25510  -31.40414 -20.19545 1.000 33.78654 ?  86  ASP   A CG  1 
ATOM   572  O OD1 . ASP   A 1 79  ? -7.52574  -32.60779 -20.10101 1.000 35.66157 ?  86  ASP   A OD1 1 
ATOM   573  O OD2 . ASP   A 1 79  ? -7.76658  -30.61965 -21.03088 1.000 40.89504 ?  86  ASP   A OD2 1 
ATOM   574  N N   . ARG   A 1 80  ? -5.35368  -30.57790 -15.94209 1.000 20.09405 ?  87  ARG   A N   1 
ATOM   575  C CA  . ARG   A 1 80  ? -4.51919  -29.74456 -15.05399 1.000 17.29664 ?  87  ARG   A CA  1 
ATOM   576  C C   . ARG   A 1 80  ? -4.09822  -28.42359 -15.72146 1.000 18.76287 ?  87  ARG   A C   1 
ATOM   577  O O   . ARG   A 1 80  ? -2.94079  -27.99727 -15.64471 1.000 17.95512 ?  87  ARG   A O   1 
ATOM   578  C CB  . ARG   A 1 80  ? -3.29397  -30.50803 -14.53370 1.000 19.58030 ?  87  ARG   A CB  1 
ATOM   579  C CG  . ARG   A 1 80  ? -2.91764  -29.90197 -13.17732 1.000 18.68521 ?  87  ARG   A CG  1 
ATOM   580  C CD  . ARG   A 1 80  ? -1.51411  -30.14343 -12.79615 1.000 32.56772 ?  87  ARG   A CD  1 
ATOM   581  N NE  . ARG   A 1 80  ? -1.26099  -31.54146 -12.66081 1.000 33.42807 ?  87  ARG   A NE  1 
ATOM   582  C CZ  . ARG   A 1 80  ? -0.05101  -32.08105 -12.70612 1.000 48.25929 ?  87  ARG   A CZ  1 
ATOM   583  N NH1 . ARG   A 1 80  ? 1.02101   -31.36613 -13.01214 1.000 34.05042 ?  87  ARG   A NH1 1 
ATOM   584  N NH2 . ARG   A 1 80  ? 0.08727   -33.36480 -12.42049 1.000 38.57530 ?  87  ARG   A NH2 1 
ATOM   585  N N   . THR   A 1 81  ? -5.05356  -27.72536 -16.33333 1.000 15.24720 ?  88  THR   A N   1 
ATOM   586  C CA  . THR   A 1 81  ? -4.79936  -26.45908 -17.00540 1.000 15.28509 ?  88  THR   A CA  1 
ATOM   587  C C   . THR   A 1 81  ? -5.71595  -25.36656 -16.49518 1.000 16.73172 ?  88  THR   A C   1 
ATOM   588  O O   . THR   A 1 81  ? -6.88991  -25.61756 -16.15815 1.000 15.63870 ?  88  THR   A O   1 
ATOM   589  C CB  . THR   A 1 81  ? -4.98486  -26.55638 -18.53536 1.000 16.03805 ?  88  THR   A CB  1 
ATOM   590  O OG1 . THR   A 1 81  ? -6.32467  -27.00688 -18.82019 1.000 19.64151 ?  88  THR   A OG1 1 
ATOM   591  C CG2 . THR   A 1 81  ? -3.94166  -27.52503 -19.10704 1.000 15.96649 ?  88  THR   A CG2 1 
ATOM   592  N N   . LEU   A 1 82  ? -5.16271  -24.15841 -16.41603 1.000 12.75473 ?  89  LEU   A N   1 
ATOM   593  C CA  . LEU   A 1 82  ? -5.95175  -22.95359 -16.21274 1.000 13.17133 ?  89  LEU   A CA  1 
ATOM   594  C C   . LEU   A 1 82  ? -5.75907  -22.11121 -17.46170 1.000 13.44133 ?  89  LEU   A C   1 
ATOM   595  O O   . LEU   A 1 82  ? -4.61977  -21.83228 -17.83563 1.000 13.33035 ?  89  LEU   A O   1 
ATOM   596  C CB  . LEU   A 1 82  ? -5.48914  -22.18537 -14.97342 1.000 13.74956 ?  89  LEU   A CB  1 
ATOM   597  C CG  . LEU   A 1 82  ? -6.24942  -20.85160 -14.76923 1.000 11.95983 ?  89  LEU   A CG  1 
ATOM   598  C CD1 . LEU   A 1 82  ? -7.78580  -21.10171 -14.59122 1.000 14.18916 ?  89  LEU   A CD1 1 
ATOM   599  C CD2 . LEU   A 1 82  ? -5.72051  -20.11135 -13.55242 1.000 14.17573 ?  89  LEU   A CD2 1 
ATOM   600  N N   . THR   A 1 83  ? -6.83810  -21.82366 -18.16882 1.000 12.66239 ?  90  THR   A N   1 
ATOM   601  C CA  . THR   A 1 83  ? -6.76530  -21.07650 -19.41514 1.000 13.79345 ?  90  THR   A CA  1 
ATOM   602  C C   . THR   A 1 83  ? -7.34637  -19.69520 -19.19942 1.000 13.82879 ?  90  THR   A C   1 
ATOM   603  O O   . THR   A 1 83  ? -8.44949  -19.55858 -18.65223 1.000 16.39786 ?  90  THR   A O   1 
ATOM   604  C CB  . THR   A 1 83  ? -7.50138  -21.79870 -20.52908 1.000 14.59788 ?  90  THR   A CB  1 
ATOM   605  O OG1 . THR   A 1 83  ? -6.90454  -23.09367 -20.72845 1.000 15.88444 ?  90  THR   A OG1 1 
ATOM   606  C CG2 . THR   A 1 83  ? -7.39496  -21.00125 -21.81896 1.000 15.96579 ?  90  THR   A CG2 1 
ATOM   607  N N   . ILE   A 1 84  ? -6.61028  -18.67613 -19.62374 1.000 11.37795 ?  91  ILE   A N   1 
ATOM   608  C CA  . ILE   A 1 84  ? -7.06948  -17.27024 -19.58734 1.000 12.25930 ?  91  ILE   A CA  1 
ATOM   609  C C   . ILE   A 1 84  ? -7.31039  -16.86089 -21.03755 1.000 15.15305 ?  91  ILE   A C   1 
ATOM   610  O O   . ILE   A 1 84  ? -6.33857  -16.73752 -21.80585 1.000 14.83331 ?  91  ILE   A O   1 
ATOM   611  C CB  . ILE   A 1 84  ? -6.03502  -16.35091 -18.92424 1.000 13.13150 ?  91  ILE   A CB  1 
ATOM   612  C CG1 . ILE   A 1 84  ? -5.76725  -16.77976 -17.46103 1.000 16.58706 ?  91  ILE   A CG1 1 
ATOM   613  C CG2 . ILE   A 1 84  ? -6.50301  -14.89044 -18.94202 1.000 14.24797 ?  91  ILE   A CG2 1 
ATOM   614  C CD1 . ILE   A 1 84  ? -4.65861  -17.76730 -17.19452 1.000 21.03835 ?  91  ILE   A CD1 1 
ATOM   615  N N   . VAL   A 1 85  ? -8.55217  -16.59305 -21.40960 1.000 11.50128 ?  92  VAL   A N   1 
ATOM   616  C CA  . VAL   A 1 85  ? -8.88475  -16.27155 -22.79863 1.000 10.87121 ?  92  VAL   A CA  1 
ATOM   617  C C   . VAL   A 1 85  ? -9.31130  -14.82660 -22.84449 1.000 15.55356 ?  92  VAL   A C   1 
ATOM   618  O O   . VAL   A 1 85  ? -10.15233 -14.40921 -22.03233 1.000 14.57214 ?  92  VAL   A O   1 
ATOM   619  C CB  . VAL   A 1 85  ? -10.04912 -17.12445 -23.32437 1.000 13.49230 ?  92  VAL   A CB  1 
ATOM   620  C CG1 . VAL   A 1 85  ? -10.22183 -16.81891 -24.82992 1.000 16.40249 ?  92  VAL   A CG1 1 
ATOM   621  C CG2 . VAL   A 1 85  ? -9.74658  -18.57447 -23.10891 1.000 18.88685 ?  92  VAL   A CG2 1 
ATOM   622  N N   . ASP   A 1 86  ? -8.82456  -14.07186 -23.82289 1.000 12.92564 ?  93  ASP   A N   1 
ATOM   623  C CA  . ASP   A 1 86  ? -9.36511  -12.71664 -24.00314 1.000 13.41478 ?  93  ASP   A CA  1 
ATOM   624  C C   . ASP   A 1 86  ? -9.62213  -12.49103 -25.48109 1.000 13.58373 ?  93  ASP   A C   1 
ATOM   625  O O   . ASP   A 1 86  ? -9.08225  -13.21169 -26.33502 1.000 14.63136 ?  93  ASP   A O   1 
ATOM   626  C CB  . ASP   A 1 86  ? -8.41242  -11.61317 -23.45553 1.000 12.94948 ?  93  ASP   A CB  1 
ATOM   627  C CG  . ASP   A 1 86  ? -7.11311  -11.52049 -24.23497 1.000 16.36073 ?  93  ASP   A CG  1 
ATOM   628  O OD1 . ASP   A 1 86  ? -7.17222  -11.12357 -25.42576 1.000 15.74789 ?  93  ASP   A OD1 1 
ATOM   629  O OD2 . ASP   A 1 86  ? -6.01209  -11.85091 -23.65873 1.000 15.82349 ?  93  ASP   A OD2 1 
ATOM   630  N N   . THR   A 1 87  ? -10.49703 -11.53248 -25.77545 1.000 12.91226 ?  94  THR   A N   1 
ATOM   631  C CA  . THR   A 1 87  ? -10.81970 -11.19011 -27.15809 1.000 13.25310 ?  94  THR   A CA  1 
ATOM   632  C C   . THR   A 1 87  ? -10.17066 -9.86788  -27.52863 1.000 15.73489 ?  94  THR   A C   1 
ATOM   633  O O   . THR   A 1 87  ? -10.72479 -9.03112  -28.23657 1.000 14.28582 ?  94  THR   A O   1 
ATOM   634  C CB  . THR   A 1 87  ? -12.31684 -11.14841 -27.38216 1.000 16.09422 ?  94  THR   A CB  1 
ATOM   635  O OG1 . THR   A 1 87  ? -12.93209 -10.32610 -26.36827 1.000 16.57584 ?  94  THR   A OG1 1 
ATOM   636  C CG2 . THR   A 1 87  ? -12.94223 -12.59064 -27.26793 1.000 17.32402 ?  94  THR   A CG2 1 
ATOM   637  N N   . GLY   A 1 88  ? -8.95481  -9.68531  -27.07911 1.000 13.79948 ?  95  GLY   A N   1 
ATOM   638  C CA  . GLY   A 1 88  ? -8.24406  -8.45653  -27.38762 1.000 13.96717 ?  95  GLY   A CA  1 
ATOM   639  C C   . GLY   A 1 88  ? -7.62498  -8.47506  -28.76294 1.000 15.08439 ?  95  GLY   A C   1 
ATOM   640  O O   . GLY   A 1 88  ? -8.04235  -9.22599  -29.66108 1.000 14.33393 ?  95  GLY   A O   1 
ATOM   641  N N   . ILE   A 1 89  ? -6.62290  -7.58940  -28.94150 1.000 13.48201 ?  96  ILE   A N   1 
ATOM   642  C CA  . ILE   A 1 89  ? -6.08112  -7.35920  -30.29457 1.000 12.13787 ?  96  ILE   A CA  1 
ATOM   643  C C   . ILE   A 1 89  ? -5.32315  -8.57435  -30.82978 1.000 13.38348 ?  96  ILE   A C   1 
ATOM   644  O O   . ILE   A 1 89  ? -5.20011  -8.72536  -32.04532 1.000 15.11895 ?  96  ILE   A O   1 
ATOM   645  C CB  . ILE   A 1 89  ? -5.21338  -6.08041  -30.29397 1.000 13.93091 ?  96  ILE   A CB  1 
ATOM   646  C CG1 . ILE   A 1 89  ? -4.95853  -5.58701  -31.73053 1.000 15.77138 ?  96  ILE   A CG1 1 
ATOM   647  C CG2 . ILE   A 1 89  ? -3.91346  -6.28497  -29.49951 1.000 13.81990 ?  96  ILE   A CG2 1 
ATOM   648  C CD1 . ILE   A 1 89  ? -4.51782  -4.16227  -31.73216 1.000 17.50353 ?  96  ILE   A CD1 1 
ATOM   649  N N   . GLY   A 1 90  ? -4.83270  -9.48426  -29.97051 1.000 13.41087 ?  97  GLY   A N   1 
ATOM   650  C CA  . GLY   A 1 90  ? -4.12104  -10.66053 -30.45672 1.000 14.44701 ?  97  GLY   A CA  1 
ATOM   651  C C   . GLY   A 1 90  ? -2.67644  -10.27523 -30.79571 1.000 15.18511 ?  97  GLY   A C   1 
ATOM   652  O O   . GLY   A 1 90  ? -2.25974  -9.13742  -30.61248 1.000 16.44570 ?  97  GLY   A O   1 
ATOM   653  N N   . MET   A 1 91  ? -1.93311  -11.24803 -31.30713 1.000 13.63145 ?  98  MET   A N   1 
ATOM   654  C CA  . MET   A 1 91  ? -0.50142  -11.05467 -31.60760 1.000 14.54252 ?  98  MET   A CA  1 
ATOM   655  C C   . MET   A 1 91  ? -0.23282  -11.63118 -32.96866 1.000 14.17340 ?  98  MET   A C   1 
ATOM   656  O O   . MET   A 1 91  ? -0.77141  -12.67951 -33.32870 1.000 16.83347 ?  98  MET   A O   1 
ATOM   657  C CB  . MET   A 1 91  ? 0.40717   -11.79421 -30.58525 1.000 13.09844 ?  98  MET   A CB  1 
ATOM   658  C CG  . MET   A 1 91  ? 0.38712   -11.04134 -29.26966 1.000 13.24124 ?  98  MET   A CG  1 
ATOM   659  S SD  . MET   A 1 91  ? 1.44315   -11.78733 -28.00857 1.000 15.79621 ?  98  MET   A SD  1 
ATOM   660  C CE  . MET   A 1 91  ? 0.33964   -13.11441 -27.50246 1.000 16.62725 ?  98  MET   A CE  1 
ATOM   661  N N   . THR   A 1 92  ? 0.58441   -10.91920 -33.72960 1.000 13.76959 ?  99  THR   A N   1 
ATOM   662  C CA  . THR   A 1 92  ? 1.12203   -11.49159 -34.96750 1.000 16.23535 ?  99  THR   A CA  1 
ATOM   663  C C   . THR   A 1 92  ? 2.22699   -12.49562 -34.65209 1.000 15.80186 ?  99  THR   A C   1 
ATOM   664  O O   . THR   A 1 92  ? 2.69780   -12.62298 -33.52639 1.000 15.95306 ?  99  THR   A O   1 
ATOM   665  C CB  . THR   A 1 92  ? 1.71280   -10.38767 -35.84533 1.000 18.17458 ?  99  THR   A CB  1 
ATOM   666  O OG1 . THR   A 1 92  ? 2.85393   -9.83362  -35.13368 1.000 19.68484 ?  99  THR   A OG1 1 
ATOM   667  C CG2 . THR   A 1 92  ? 0.64076   -9.33235  -36.11737 1.000 19.59212 ?  99  THR   A CG2 1 
ATOM   668  N N   . LYS   A 1 93  ? 2.64050   -13.24523 -35.67172 1.000 14.94262 ?  100 LYS   A N   1 
ATOM   669  C CA  . LYS   A 1 93  ? 3.77507   -14.15473 -35.49458 1.000 13.90499 ?  100 LYS   A CA  1 
ATOM   670  C C   . LYS   A 1 93  ? 5.00769   -13.39543 -35.02840 1.000 16.23908 ?  100 LYS   A C   1 
ATOM   671  O O   . LYS   A 1 93  ? 5.71182   -13.86494 -34.13375 1.000 15.66519 ?  100 LYS   A O   1 
ATOM   672  C CB  . LYS   A 1 93  ? 4.09955   -14.88255 -36.80512 1.000 18.26313 ?  100 LYS   A CB  1 
ATOM   673  C CG  . LYS   A 1 93  ? 5.09103   -16.04245 -36.56647 1.000 16.40710 ?  100 LYS   A CG  1 
ATOM   674  C CD  . LYS   A 1 93  ? 5.46625   -16.67946 -37.94257 1.000 20.99261 ?  100 LYS   A CD  1 
ATOM   675  C CE  . LYS   A 1 93  ? 6.37328   -17.89875 -37.66750 1.000 22.23101 ?  100 LYS   A CE  1 
ATOM   676  N NZ  . LYS   A 1 93  ? 7.06661   -18.31008 -38.93862 1.000 27.23095 ?  100 LYS   A NZ  1 
ATOM   677  N N   . ALA   A 1 94  ? 5.27800   -12.21413 -35.62535 1.000 17.10656 ?  101 ALA   A N   1 
ATOM   678  C CA  . ALA   A 1 94  ? 6.42197   -11.42689 -35.18728 1.000 18.46788 ?  101 ALA   A CA  1 
ATOM   679  C C   . ALA   A 1 94  ? 6.27301   -11.01522 -33.75037 1.000 18.34648 ?  101 ALA   A C   1 
ATOM   680  O O   . ALA   A 1 94  ? 7.26736   -10.98768 -33.00750 1.000 19.54013 ?  101 ALA   A O   1 
ATOM   681  C CB  . ALA   A 1 94  ? 6.62649   -10.18314 -36.05578 1.000 19.83284 ?  101 ALA   A CB  1 
ATOM   682  N N   . ASP   A 1 95  ? 5.04754   -10.63462 -33.33552 1.000 14.66077 ?  102 ASP   A N   1 
ATOM   683  C CA  . ASP   A 1 95  ? 4.88326   -10.27597 -31.92980 1.000 14.83909 ?  102 ASP   A CA  1 
ATOM   684  C C   . ASP   A 1 95  ? 5.22682   -11.44866 -31.03255 1.000 15.08486 ?  102 ASP   A C   1 
ATOM   685  O O   . ASP   A 1 95  ? 5.84776   -11.28090 -29.96254 1.000 15.55745 ?  102 ASP   A O   1 
ATOM   686  C CB  . ASP   A 1 95  ? 3.41633   -9.88064  -31.64723 1.000 19.74132 ?  102 ASP   A CB  1 
ATOM   687  C CG  . ASP   A 1 95  ? 3.00988   -8.55840  -32.22822 1.000 21.59387 ?  102 ASP   A CG  1 
ATOM   688  O OD1 . ASP   A 1 95  ? 3.84272   -7.64943  -32.38533 1.000 23.65691 ?  102 ASP   A OD1 1 
ATOM   689  O OD2 . ASP   A 1 95  ? 1.78633   -8.41975  -32.52223 1.000 22.93567 ?  102 ASP   A OD2 1 
ATOM   690  N N   . LEU   A 1 96  ? 4.75772   -12.64398 -31.38709 1.000 14.46030 ?  103 LEU   A N   1 
ATOM   691  C CA  . LEU   A 1 96  ? 5.02151   -13.79112 -30.53333 1.000 15.37738 ?  103 LEU   A CA  1 
ATOM   692  C C   . LEU   A 1 96  ? 6.50645   -13.98674 -30.39739 1.000 15.89894 ?  103 LEU   A C   1 
ATOM   693  O O   . LEU   A 1 96  ? 7.01313   -14.20518 -29.29539 1.000 15.40467 ?  103 LEU   A O   1 
ATOM   694  C CB  . LEU   A 1 96  ? 4.41868   -15.08637 -31.11427 1.000 16.55997 ?  103 LEU   A CB  1 
ATOM   695  C CG  . LEU   A 1 96  ? 2.93269   -15.29023 -30.99221 1.000 15.01475 ?  103 LEU   A CG  1 
ATOM   696  C CD1 . LEU   A 1 96  ? 2.60741   -16.57151 -31.71945 1.000 15.21116 ?  103 LEU   A CD1 1 
ATOM   697  C CD2 . LEU   A 1 96  ? 2.46879   -15.33853 -29.50926 1.000 13.56347 ?  103 LEU   A CD2 1 
ATOM   698  N N   . ILE   A 1 97  ? 7.20740   -13.93281 -31.53034 1.000 14.31336 ?  104 ILE   A N   1 
ATOM   699  C CA  . ILE   A 1 97  ? 8.63578   -14.19759 -31.50026 1.000 15.37483 ?  104 ILE   A CA  1 
ATOM   700  C C   . ILE   A 1 97  ? 9.35833   -13.11843 -30.72489 1.000 15.13633 ?  104 ILE   A C   1 
ATOM   701  O O   . ILE   A 1 97  ? 10.30920  -13.39786 -29.96070 1.000 17.46692 ?  104 ILE   A O   1 
ATOM   702  C CB  . ILE   A 1 97  ? 9.16848   -14.34027 -32.92443 1.000 17.11774 ?  104 ILE   A CB  1 
ATOM   703  C CG1 . ILE   A 1 97  ? 8.63334   -15.63167 -33.54746 1.000 16.96340 ?  104 ILE   A CG1 1 
ATOM   704  C CG2 . ILE   A 1 97  ? 10.68616  -14.35456 -32.96405 1.000 19.59061 ?  104 ILE   A CG2 1 
ATOM   705  C CD1 . ILE   A 1 97  ? 8.80362   -15.62722 -35.11641 1.000 19.56249 ?  104 ILE   A CD1 1 
ATOM   706  N N   . ASN   A 1 98  ? 8.89110   -11.87499 -30.85790 1.000 16.69552 ?  105 ASN   A N   1 
ATOM   707  C CA  . ASN   A 1 98  ? 9.50766   -10.74609 -30.15571 1.000 17.06191 ?  105 ASN   A CA  1 
ATOM   708  C C   . ASN   A 1 98  ? 8.93081   -10.63448 -28.72882 1.000 16.20975 ?  105 ASN   A C   1 
ATOM   709  O O   . ASN   A 1 98  ? 8.34265   -9.63907  -28.30579 1.000 16.97522 ?  105 ASN   A O   1 
ATOM   710  C CB  . ASN   A 1 98  ? 9.29747   -9.46850  -30.97733 1.000 18.50936 ?  105 ASN   A CB  1 
ATOM   711  C CG  . ASN   A 1 98  ? 10.35980  -9.29909  -32.03064 1.000 26.20429 ?  105 ASN   A CG  1 
ATOM   712  O OD1 . ASN   A 1 98  ? 11.41381  -8.72309  -31.79015 1.000 35.27952 ?  105 ASN   A OD1 1 
ATOM   713  N ND2 . ASN   A 1 98  ? 10.04546  -9.74710  -33.24989 1.000 38.45002 ?  105 ASN   A ND2 1 
ATOM   714  N N   . ASN   A 1 99  ? 9.07427   -11.72835 -27.97076 1.000 15.17446 ?  106 ASN   A N   1 
ATOM   715  C CA  . ASN   A 1 99  ? 8.72863   -11.76528 -26.54355 1.000 14.53144 ?  106 ASN   A CA  1 
ATOM   716  C C   . ASN   A 1 99  ? 7.27605   -11.39053 -26.27760 1.000 17.27938 ?  106 ASN   A C   1 
ATOM   717  O O   . ASN   A 1 99  ? 6.95422   -10.62365 -25.36120 1.000 17.13347 ?  106 ASN   A O   1 
ATOM   718  C CB  . ASN   A 1 99  ? 9.70032   -10.89003 -25.74645 1.000 13.23081 ?  106 ASN   A CB  1 
ATOM   719  C CG  . ASN   A 1 99  ? 11.12101  -11.39186 -25.89322 1.000 15.21231 ?  106 ASN   A CG  1 
ATOM   720  O OD1 . ASN   A 1 99  ? 11.36421  -12.55806 -25.70015 1.000 16.92765 ?  106 ASN   A OD1 1 
ATOM   721  N ND2 . ASN   A 1 99  ? 12.04895  -10.49052 -26.17899 1.000 17.69585 ?  106 ASN   A ND2 1 
ATOM   722  N N   . LEU   A 1 100 ? 6.40603   -11.97575 -27.09549 1.000 15.04516 ?  107 LEU   A N   1 
ATOM   723  C CA  . LEU   A 1 100 ? 4.95025   -11.81015 -26.93007 1.000 14.92503 ?  107 LEU   A CA  1 
ATOM   724  C C   . LEU   A 1 100 ? 4.56784   -10.33612 -26.86575 1.000 15.96263 ?  107 LEU   A C   1 
ATOM   725  O O   . LEU   A 1 100 ? 3.79843   -9.92331  -25.99425 1.000 16.93585 ?  107 LEU   A O   1 
ATOM   726  C CB  . LEU   A 1 100 ? 4.46874   -12.54480 -25.68668 1.000 17.05555 ?  107 LEU   A CB  1 
ATOM   727  C CG  . LEU   A 1 100 ? 4.82554   -14.06359 -25.89361 1.000 22.49936 ?  107 LEU   A CG  1 
ATOM   728  C CD1 . LEU   A 1 100 ? 6.06828   -14.49034 -25.05415 1.000 20.23154 ?  107 LEU   A CD1 1 
ATOM   729  C CD2 . LEU   A 1 100 ? 3.67230   -14.99245 -25.71182 1.000 32.04600 ?  107 LEU   A CD2 1 
ATOM   730  N N   . GLY   A 1 101 ? 5.13713   -9.54066  -27.76802 1.000 16.33167 ?  108 GLY   A N   1 
ATOM   731  C CA  . GLY   A 1 101 ? 4.77258   -8.13353  -27.88178 1.000 17.34703 ?  108 GLY   A CA  1 
ATOM   732  C C   . GLY   A 1 101 ? 5.26096   -7.22486  -26.78532 1.000 20.07422 ?  108 GLY   A C   1 
ATOM   733  O O   . GLY   A 1 101 ? 4.65898   -6.15000  -26.56086 1.000 22.53838 ?  108 GLY   A O   1 
ATOM   734  N N   . THR   A 1 102 ? 6.33775   -7.61061  -26.08566 1.000 18.43064 ?  109 THR   A N   1 
ATOM   735  C CA  . THR   A 1 102 ? 6.89667   -6.84138  -24.97951 1.000 18.22589 ?  109 THR   A CA  1 
ATOM   736  C C   . THR   A 1 102 ? 8.27036   -6.33865  -25.36198 1.000 16.69895 ?  109 THR   A C   1 
ATOM   737  O O   . THR   A 1 102 ? 8.89537   -6.85352  -26.30074 1.000 20.53001 ?  109 THR   A O   1 
ATOM   738  C CB  . THR   A 1 102 ? 7.04927   -7.67858  -23.69354 1.000 16.07909 ?  109 THR   A CB  1 
ATOM   739  O OG1 . THR   A 1 102 ? 8.05094   -8.69024  -23.87450 1.000 17.26061 ?  109 THR   A OG1 1 
ATOM   740  C CG2 . THR   A 1 102 ? 5.72750   -8.30949  -23.28440 1.000 24.58319 ?  109 THR   A CG2 1 
ATOM   741  N N   . ILE   A 1 103 ? 8.75045   -5.35655  -24.60632 1.000 15.13133 ?  110 ILE   A N   1 
ATOM   742  C CA  . ILE   A 1 103 ? 10.15243  -4.95897  -24.69001 1.000 15.42712 ?  110 ILE   A CA  1 
ATOM   743  C C   . ILE   A 1 103 ? 10.88999  -5.65878  -23.56898 1.000 15.07968 ?  110 ILE   A C   1 
ATOM   744  O O   . ILE   A 1 103 ? 11.46971  -5.03157  -22.66999 1.000 15.41130 ?  110 ILE   A O   1 
ATOM   745  C CB  . ILE   A 1 103 ? 10.29968  -3.44861  -24.68124 1.000 18.31335 ?  110 ILE   A CB  1 
ATOM   746  C CG1 . ILE   A 1 103 ? 9.57690   -2.76090  -23.49581 1.000 17.98476 ?  110 ILE   A CG1 1 
ATOM   747  C CG2 . ILE   A 1 103 ? 9.67656   -2.90454  -26.01846 1.000 18.85069 ?  110 ILE   A CG2 1 
ATOM   748  C CD1 . ILE   A 1 103 ? 10.03185  -1.25067  -23.34181 1.000 21.58188 ?  110 ILE   A CD1 1 
ATOM   749  N N   . ALA   A 1 104 ? 10.90070  -6.98424  -23.64133 1.000 17.32420 ?  111 ALA   A N   1 
ATOM   750  C CA  . ALA   A 1 104 ? 11.30019  -7.73950  -22.48195 1.000 16.62649 ?  111 ALA   A CA  1 
ATOM   751  C C   . ALA   A 1 104 ? 12.78784  -7.65095  -22.17530 1.000 17.31988 ?  111 ALA   A C   1 
ATOM   752  O O   . ALA   A 1 104 ? 13.13170  -7.88767  -21.03162 1.000 17.87283 ?  111 ALA   A O   1 
ATOM   753  C CB  . ALA   A 1 104 ? 10.90291  -9.21040  -22.64678 1.000 16.70674 ?  111 ALA   A CB  1 
ATOM   754  N N   . LYS   A 1 105 ? 13.67229  -7.36862  -23.13477 1.000 18.30769 ?  112 LYS   A N   1 
ATOM   755  C CA  . LYS   A 1 105 ? 15.08725  -7.23427  -22.76346 1.000 21.48911 ?  112 LYS   A CA  1 
ATOM   756  C C   . LYS   A 1 105 ? 15.27416  -6.06009  -21.79733 1.000 22.88139 ?  112 LYS   A C   1 
ATOM   757  O O   . LYS   A 1 105 ? 15.83351  -6.21745  -20.69594 1.000 20.26983 ?  112 LYS   A O   1 
ATOM   758  C CB  . LYS   A 1 105 ? 15.99342  -7.06359  -24.01932 1.000 22.11218 ?  112 LYS   A CB  1 
ATOM   759  C CG  . LYS   A 1 105 ? 17.49049  -7.12015  -23.73966 1.000 26.84298 ?  112 LYS   A CG  1 
ATOM   760  C CD  . LYS   A 1 105 ? 18.29373  -6.76578  -24.98380 1.000 29.68626 ?  112 LYS   A CD  1 
ATOM   761  C CE  . LYS   A 1 105 ? 19.75007  -6.39294  -24.67746 1.000 42.69724 ?  112 LYS   A CE  1 
ATOM   762  N NZ  . LYS   A 1 105 ? 20.67767  -7.17837  -25.59417 1.000 51.87759 ?  112 LYS   A NZ  1 
ATOM   763  N N   . SER   A 1 106 ? 14.77267  -4.88168  -22.16713 1.000 19.98868 ?  113 SER   A N   1 
ATOM   764  C CA  . SER   A 1 106 ? 14.96894  -3.76048  -21.25744 1.000 21.61904 ?  113 SER   A CA  1 
ATOM   765  C C   . SER   A 1 106 ? 14.08049  -3.89306  -20.02020 1.000 22.92824 ?  113 SER   A C   1 
ATOM   766  O O   . SER   A 1 106 ? 14.46018  -3.44007  -18.93243 1.000 23.40037 ?  113 SER   A O   1 
ATOM   767  C CB  . SER   A 1 106 ? 14.69910  -2.40961  -21.96951 1.000 26.64413 ?  113 SER   A CB  1 
ATOM   768  O OG  . SER   A 1 106 ? 13.32322  -2.30805  -22.33819 1.000 27.23098 ?  113 SER   A OG  1 
ATOM   769  N N   . GLY   A 1 107 ? 12.91797  -4.52900  -20.13818 1.000 19.32384 ?  114 GLY   A N   1 
ATOM   770  C CA  . GLY   A 1 107 ? 12.08524  -4.73317  -18.94199 1.000 17.33198 ?  114 GLY   A CA  1 
ATOM   771  C C   . GLY   A 1 107 ? 12.77223  -5.65759  -17.95976 1.000 16.90777 ?  114 GLY   A C   1 
ATOM   772  O O   . GLY   A 1 107 ? 12.71531  -5.44641  -16.74109 1.000 17.75467 ?  114 GLY   A O   1 
ATOM   773  N N   . THR   A 1 108 ? 13.38960  -6.71277  -18.45887 1.000 15.74875 ?  115 THR   A N   1 
ATOM   774  C CA  . THR   A 1 108 ? 14.07859  -7.62923  -17.55358 1.000 16.74838 ?  115 THR   A CA  1 
ATOM   775  C C   . THR   A 1 108 ? 15.24348  -6.95237  -16.86857 1.000 22.07922 ?  115 THR   A C   1 
ATOM   776  O O   . THR   A 1 108 ? 15.46846  -7.17815  -15.66714 1.000 21.70531 ?  115 THR   A O   1 
ATOM   777  C CB  . THR   A 1 108 ? 14.59870  -8.83153  -18.33827 1.000 23.81300 ?  115 THR   A CB  1 
ATOM   778  O OG1 . THR   A 1 108 ? 13.46573  -9.55836  -18.84078 1.000 20.03694 ?  115 THR   A OG1 1 
ATOM   779  C CG2 . THR   A 1 108 ? 15.40625  -9.70741  -17.46281 1.000 23.06081 ?  115 THR   A CG2 1 
ATOM   780  N N   . LYS   A 1 109 ? 15.99683  -6.14741  -17.62405 1.000 21.52446 ?  116 LYS   A N   1 
ATOM   781  C CA  . LYS   A 1 109 ? 17.11557  -5.41863  -17.03979 1.000 24.32457 ?  116 LYS   A CA  1 
ATOM   782  C C   . LYS   A 1 109 ? 16.64538  -4.58851  -15.86043 1.000 25.16171 ?  116 LYS   A C   1 
ATOM   783  O O   . LYS   A 1 109 ? 17.24587  -4.62338  -14.77895 1.000 29.55322 ?  116 LYS   A O   1 
ATOM   784  C CB  . LYS   A 1 109 ? 17.77736  -4.52140  -18.08154 1.000 26.56780 ?  116 LYS   A CB  1 
ATOM   785  C CG  . LYS   A 1 109 ? 18.55204  -3.31838  -17.51860 1.000 45.62215 ?  116 LYS   A CG  1 
ATOM   786  C CD  . LYS   A 1 109 ? 19.56688  -2.83554  -18.57357 1.000 35.92755 ?  116 LYS   A CD  1 
ATOM   787  C CE  . LYS   A 1 109 ? 20.55038  -1.79429  -18.01683 1.000 51.00209 ?  116 LYS   A CE  1 
ATOM   788  N NZ  . LYS   A 1 109 ? 21.23972  -2.24292  -16.77742 1.000 64.36094 ?  116 LYS   A NZ  1 
ATOM   789  N N   . ALA   A 1 110 ? 15.61503  -3.78418  -16.07071 1.000 21.82019 ?  117 ALA   A N   1 
ATOM   790  C CA  . ALA   A 1 110 ? 15.11336  -2.95460  -14.97826 1.000 27.38456 ?  117 ALA   A CA  1 
ATOM   791  C C   . ALA   A 1 110 ? 14.60012  -3.81934  -13.83986 1.000 21.36867 ?  117 ALA   A C   1 
ATOM   792  O O   . ALA   A 1 110 ? 14.80587  -3.49278  -12.66814 1.000 25.07249 ?  117 ALA   A O   1 
ATOM   793  C CB  . ALA   A 1 110 ? 14.01766  -2.02075  -15.48834 1.000 24.27000 ?  117 ALA   A CB  1 
ATOM   794  N N   . PHE   A 1 111 ? 13.87618  -4.89318  -14.15850 1.000 20.71505 ?  118 PHE   A N   1 
ATOM   795  C CA  . PHE   A 1 111 ? 13.28041  -5.70241  -13.09069 1.000 20.24345 ?  118 PHE   A CA  1 
ATOM   796  C C   . PHE   A 1 111 ? 14.36093  -6.30128  -12.22084 1.000 22.80164 ?  118 PHE   A C   1 
ATOM   797  O O   . PHE   A 1 111 ? 14.29314  -6.24020  -10.99412 1.000 22.74618 ?  118 PHE   A O   1 
ATOM   798  C CB  . PHE   A 1 111 ? 12.45284  -6.81118  -13.73121 1.000 16.66493 ?  118 PHE   A CB  1 
ATOM   799  C CG  . PHE   A 1 111 ? 11.76261  -7.69778  -12.77624 1.000 17.11503 ?  118 PHE   A CG  1 
ATOM   800  C CD1 . PHE   A 1 111 ? 11.10384  -7.21690  -11.62099 1.000 18.93363 ?  118 PHE   A CD1 1 
ATOM   801  C CD2 . PHE   A 1 111 ? 11.67459  -9.02038  -13.05588 1.000 20.87174 ?  118 PHE   A CD2 1 
ATOM   802  C CE1 . PHE   A 1 111 ? 10.41453  -8.09667  -10.78614 1.000 18.66196 ?  118 PHE   A CE1 1 
ATOM   803  C CE2 . PHE   A 1 111 ? 10.95265  -9.90717  -12.25209 1.000 19.60471 ?  118 PHE   A CE2 1 
ATOM   804  C CZ  . PHE   A 1 111 ? 10.35257  -9.43275  -11.09087 1.000 19.69817 ?  118 PHE   A CZ  1 
ATOM   805  N N   . MET   A 1 112 ? 15.40543  -6.82878  -12.83511 1.000 23.16459 ?  119 MET   A N   1 
ATOM   806  C CA  . MET   A 1 112 ? 16.46273  -7.43653  -12.01330 1.000 26.23845 ?  119 MET   A CA  1 
ATOM   807  C C   . MET   A 1 112 ? 17.22405  -6.40691  -11.19633 1.000 32.24742 ?  119 MET   A C   1 
ATOM   808  O O   . MET   A 1 112 ? 17.65294  -6.70777  -10.07213 1.000 33.21473 ?  119 MET   A O   1 
ATOM   809  C CB  . MET   A 1 112 ? 17.38838  -8.24750  -12.91257 1.000 32.93532 ?  119 MET   A CB  1 
ATOM   810  C CG  . MET   A 1 112 ? 16.72219  -9.55604  -13.22764 1.000 27.92696 ?  119 MET   A CG  1 
ATOM   811  S SD  . MET   A 1 112 ? 17.77001  -10.44376 -14.40184 1.000 46.21047 ?  119 MET   A SD  1 
ATOM   812  C CE  . MET   A 1 112 ? 16.91266  -11.98347 -14.46005 1.000 28.78517 ?  119 MET   A CE  1 
ATOM   813  N N   . GLU   A 1 113 ? 17.42076  -5.20057  -11.72654 1.000 28.12592 ?  120 GLU   A N   1 
ATOM   814  C CA  . GLU   A 1 113 ? 17.99132  -4.16422  -10.88779 1.000 31.44897 ?  120 GLU   A CA  1 
ATOM   815  C C   . GLU   A 1 113 ? 17.07630  -3.82978  -9.72843  1.000 32.73752 ?  120 GLU   A C   1 
ATOM   816  O O   . GLU   A 1 113 ? 17.53790  -3.63375  -8.59247  1.000 37.94695 ?  120 GLU   A O   1 
ATOM   817  C CB  . GLU   A 1 113 ? 18.30121  -2.91102  -11.70013 1.000 39.40004 ?  120 GLU   A CB  1 
ATOM   818  C CG  . GLU   A 1 113 ? 19.32273  -3.16369  -12.77743 1.000 50.29313 ?  120 GLU   A CG  1 
ATOM   819  C CD  . GLU   A 1 113 ? 19.58289  -1.95251  -13.65011 1.000 61.76571 ?  120 GLU   A CD  1 
ATOM   820  O OE1 . GLU   A 1 113 ? 18.69707  -1.07481  -13.76328 1.000 55.05532 ?  120 GLU   A OE1 1 
ATOM   821  O OE2 . GLU   A 1 113 ? 20.68203  -1.90746  -14.24887 1.000 66.62224 ?  120 GLU   A OE2 1 
ATOM   822  N N   . ALA   A 1 114 ? 15.78369  -3.72366  -9.98569  1.000 28.24345 ?  121 ALA   A N   1 
ATOM   823  C CA  . ALA   A 1 114 ? 14.86765  -3.45122  -8.89603  1.000 27.78584 ?  121 ALA   A CA  1 
ATOM   824  C C   . ALA   A 1 114 ? 14.93528  -4.53934  -7.82558  1.000 28.78249 ?  121 ALA   A C   1 
ATOM   825  O O   . ALA   A 1 114 ? 14.96959  -4.22629  -6.62770  1.000 33.19819 ?  121 ALA   A O   1 
ATOM   826  C CB  . ALA   A 1 114 ? 13.45872  -3.30769  -9.44197  1.000 25.02864 ?  121 ALA   A CB  1 
ATOM   827  N N   . LEU   A 1 115 ? 15.01976  -5.81434  -8.23625  1.000 27.22192 ?  122 LEU   A N   1 
ATOM   828  C CA  . LEU   A 1 115 ? 15.03589  -6.91750  -7.25405  1.000 27.69677 ?  122 LEU   A CA  1 
ATOM   829  C C   . LEU   A 1 115 ? 16.26629  -6.81828  -6.37280  1.000 39.50726 ?  122 LEU   A C   1 
ATOM   830  O O   . LEU   A 1 115 ? 16.19617  -7.01346  -5.15022  1.000 36.04892 ?  122 LEU   A O   1 
ATOM   831  C CB  . LEU   A 1 115 ? 15.02306  -8.25684  -7.97696  1.000 25.84624 ?  122 LEU   A CB  1 
ATOM   832  C CG  . LEU   A 1 115 ? 13.71237  -8.59969  -8.68663  1.000 24.09823 ?  122 LEU   A CG  1 
ATOM   833  C CD1 . LEU   A 1 115 ? 13.87179  -9.82393  -9.55969  1.000 29.48983 ?  122 LEU   A CD1 1 
ATOM   834  C CD2 . LEU   A 1 115 ? 12.59007  -8.80587  -7.61320  1.000 22.85487 ?  122 LEU   A CD2 1 
ATOM   835  N N   . GLN   A 1 116 ? 17.40746  -6.49855  -6.97763  1.000 35.38495 ?  123 GLN   A N   1 
ATOM   836  C CA  . GLN   A 1 116 ? 18.62800  -6.43103  -6.19406  1.000 37.10939 ?  123 GLN   A CA  1 
ATOM   837  C C   . GLN   A 1 116 ? 18.59629  -5.25272  -5.23741  1.000 39.81808 ?  123 GLN   A C   1 
ATOM   838  O O   . GLN   A 1 116 ? 19.32432  -5.26259  -4.23388  1.000 45.55510 ?  123 GLN   A O   1 
ATOM   839  C CB  . GLN   A 1 116 ? 19.84587  -6.41698  -7.14681  1.000 38.53382 ?  123 GLN   A CB  1 
ATOM   840  C CG  . GLN   A 1 116 ? 20.10781  -5.21743  -8.12437  1.000 55.50478 ?  123 GLN   A CG  1 
ATOM   841  C CD  . GLN   A 1 116 ? 20.35779  -3.82736  -7.48940  1.000 63.78206 ?  123 GLN   A CD  1 
ATOM   842  O OE1 . GLN   A 1 116 ? 20.93111  -3.71198  -6.39529  1.000 73.29021 ?  123 GLN   A OE1 1 
ATOM   843  N NE2 . GLN   A 1 116 ? 19.99049  -2.76222  -8.22274  1.000 40.82863 ?  123 GLN   A NE2 1 
ATOM   844  N N   . ALA   A 1 117 ? 17.73396  -4.26448  -5.50276  1.000 43.48867 ?  124 ALA   A N   1 
ATOM   845  C CA  . ALA   A 1 117 ? 17.57599  -3.06376  -4.68148  1.000 43.68403 ?  124 ALA   A CA  1 
ATOM   846  C C   . ALA   A 1 117 ? 16.46755  -3.20967  -3.64152  1.000 56.67320 ?  124 ALA   A C   1 
ATOM   847  O O   . ALA   A 1 117 ? 16.21362  -2.26273  -2.89149  1.000 52.60720 ?  124 ALA   A O   1 
ATOM   848  C CB  . ALA   A 1 117 ? 17.28987  -1.84403  -5.57376  1.000 45.63493 ?  124 ALA   A CB  1 
ATOM   849  N N   . GLY   A 1 118 ? 15.78889  -4.36025  -3.59579  1.000 43.86273 ?  125 GLY   A N   1 
ATOM   850  C CA  . GLY   A 1 118 ? 14.79135  -4.62352  -2.58266  1.000 38.71415 ?  125 GLY   A CA  1 
ATOM   851  C C   . GLY   A 1 118 ? 13.39613  -4.87796  -3.10617  1.000 37.59406 ?  125 GLY   A C   1 
ATOM   852  O O   . GLY   A 1 118 ? 12.51335  -5.20409  -2.30390  1.000 40.36441 ?  125 GLY   A O   1 
ATOM   853  N N   . ALA   A 1 119 ? 13.14142  -4.74615  -4.40612  1.000 33.11248 ?  126 ALA   A N   1 
ATOM   854  C CA  . ALA   A 1 119 ? 11.83014  -5.09409  -4.91671  1.000 29.25128 ?  126 ALA   A CA  1 
ATOM   855  C C   . ALA   A 1 119 ? 11.60427  -6.58877  -4.75951  1.000 31.74310 ?  126 ALA   A C   1 
ATOM   856  O O   . ALA   A 1 119 ? 12.52555  -7.35047  -4.48698  1.000 31.59296 ?  126 ALA   A O   1 
ATOM   857  C CB  . ALA   A 1 119 ? 11.69715  -4.72234  -6.39673  1.000 28.58405 ?  126 ALA   A CB  1 
ATOM   858  N N   . ASP   A 1 120 ? 10.37942  -7.03454  -5.01517  1.000 27.39910 ?  127 ASP   A N   1 
ATOM   859  C CA  . ASP   A 1 120 ? 10.09683  -8.45783  -4.99727  1.000 25.57710 ?  127 ASP   A CA  1 
ATOM   860  C C   . ASP   A 1 120 ? 9.34755   -8.82187  -6.26455  1.000 26.00114 ?  127 ASP   A C   1 
ATOM   861  O O   . ASP   A 1 120 ? 8.93515   -7.94976  -7.05196  1.000 23.59955 ?  127 ASP   A O   1 
ATOM   862  C CB  . ASP   A 1 120 ? 9.26444   -8.85291  -3.79121  1.000 27.47582 ?  127 ASP   A CB  1 
ATOM   863  C CG  . ASP   A 1 120 ? 7.90188   -8.20998  -3.83506  1.000 40.24542 ?  127 ASP   A CG  1 
ATOM   864  O OD1 . ASP   A 1 120 ? 7.79904   -7.01162  -3.50571  1.000 46.22457 ?  127 ASP   A OD1 1 
ATOM   865  O OD2 . ASP   A 1 120 ? 6.94331   -8.89265  -4.25127  1.000 31.64449 ?  127 ASP   A OD2 1 
ATOM   866  N N   . ILE   A 1 121 ? 9.21079   -10.13828 -6.48566  1.000 23.32731 ?  128 ILE   A N   1 
ATOM   867  C CA  . ILE   A 1 121 ? 8.69120   -10.61994 -7.75451  1.000 19.60048 ?  128 ILE   A CA  1 
ATOM   868  C C   . ILE   A 1 121 ? 7.28276   -10.11057 -8.04067  1.000 22.57830 ?  128 ILE   A C   1 
ATOM   869  O O   . ILE   A 1 121 ? 6.89880   -9.99119  -9.21681  1.000 21.91999 ?  128 ILE   A O   1 
ATOM   870  C CB  . ILE   A 1 121 ? 8.79374   -12.16547 -7.78388  1.000 20.37938 ?  128 ILE   A CB  1 
ATOM   871  C CG1 . ILE   A 1 121 ? 10.28000  -12.54115 -8.06166  1.000 27.15085 ?  128 ILE   A CG1 1 
ATOM   872  C CG2 . ILE   A 1 121 ? 7.82703   -12.78547 -8.81591  1.000 21.74233 ?  128 ILE   A CG2 1 
ATOM   873  C CD1 . ILE   A 1 121 ? 10.67286  -13.98857 -7.70530  1.000 28.48282 ?  128 ILE   A CD1 1 
ATOM   874  N N   . SER   A 1 122 ? 6.50064   -9.78780  -6.99560  1.000 21.33332 ?  129 SER   A N   1 
ATOM   875  C CA  . SER   A 1 122 ? 5.14766   -9.31099  -7.26166  1.000 25.77212 ?  129 SER   A CA  1 
ATOM   876  C C   . SER   A 1 122 ? 5.15820   -8.02621  -8.07760  1.000 24.08945 ?  129 SER   A C   1 
ATOM   877  O O   . SER   A 1 122 ? 4.10804   -7.64654  -8.61598  1.000 25.28108 ?  129 SER   A O   1 
ATOM   878  C CB  . SER   A 1 122 ? 4.37336   -9.08262  -5.96102  1.000 23.43647 ?  129 SER   A CB  1 
ATOM   879  O OG  . SER   A 1 122 ? 4.74770   -7.86200  -5.35407  1.000 26.78199 ?  129 SER   A OG  1 
ATOM   880  N N   . MET   A 1 123 ? 6.28775   -7.33974  -8.14784  1.000 19.59260 ?  130 MET   A N   1 
ATOM   881  C CA  . MET   A 1 123 ? 6.35562   -6.05817  -8.85518  1.000 19.46908 ?  130 MET   A CA  1 
ATOM   882  C C   . MET   A 1 123 ? 6.65915   -6.21849  -10.35169 1.000 20.16554 ?  130 MET   A C   1 
ATOM   883  O O   . MET   A 1 123 ? 6.75743   -5.21358  -11.05931 1.000 19.51112 ?  130 MET   A O   1 
ATOM   884  C CB  . MET   A 1 123 ? 7.39931   -5.15232  -8.19648  1.000 21.41937 ?  130 MET   A CB  1 
ATOM   885  C CG  . MET   A 1 123 ? 6.97963   -4.88932  -6.74049  1.000 26.61369 ?  130 MET   A CG  1 
ATOM   886  S SD  . MET   A 1 123 ? 8.24710   -4.16012  -5.74703  1.000 32.01232 ?  130 MET   A SD  1 
ATOM   887  C CE  . MET   A 1 123 ? 8.42523   -2.63192  -6.69907  1.000 35.83012 ?  130 MET   A CE  1 
ATOM   888  N N   . ILE   A 1 124 ? 6.64584   -7.44446  -10.85762 1.000 15.94958 ?  131 ILE   A N   1 
ATOM   889  C CA  . ILE   A 1 124 ? 7.10400   -7.71734  -12.22207 1.000 14.76876 ?  131 ILE   A CA  1 
ATOM   890  C C   . ILE   A 1 124 ? 6.32463   -6.92070  -13.27189 1.000 16.98674 ?  131 ILE   A C   1 
ATOM   891  O O   . ILE   A 1 124 ? 6.87840   -6.54342  -14.30632 1.000 15.28014 ?  131 ILE   A O   1 
ATOM   892  C CB  . ILE   A 1 124 ? 6.98806   -9.23845  -12.47203 1.000 17.06899 ?  131 ILE   A CB  1 
ATOM   893  C CG1 . ILE   A 1 124 ? 7.57860   -9.60341  -13.86145 1.000 15.55181 ?  131 ILE   A CG1 1 
ATOM   894  C CG2 . ILE   A 1 124 ? 5.53649   -9.74696  -12.31626 1.000 15.33516 ?  131 ILE   A CG2 1 
ATOM   895  C CD1 . ILE   A 1 124 ? 7.71543   -11.10398 -14.01668 1.000 17.32886 ?  131 ILE   A CD1 1 
ATOM   896  N N   . GLY   A 1 125 ? 5.03088   -6.73604  -13.07768 1.000 17.32763 ?  132 GLY   A N   1 
ATOM   897  C CA  . GLY   A 1 125 ? 4.21901   -6.02375  -14.07965 1.000 19.58929 ?  132 GLY   A CA  1 
ATOM   898  C C   . GLY   A 1 125 ? 4.62804   -4.57444  -14.26490 1.000 20.13962 ?  132 GLY   A C   1 
ATOM   899  O O   . GLY   A 1 125 ? 4.34567   -3.98820  -15.31669 1.000 22.42284 ?  132 GLY   A O   1 
ATOM   900  N N   . GLN   A 1 126 ? 5.26870   -3.96742  -13.26043 1.000 18.05936 ?  133 GLN   A N   1 
ATOM   901  C CA  . GLN   A 1 126 ? 5.75096   -2.60875  -13.38690 1.000 19.30297 ?  133 GLN   A CA  1 
ATOM   902  C C   . GLN   A 1 126 ? 6.87539   -2.52112  -14.40963 1.000 17.94857 ?  133 GLN   A C   1 
ATOM   903  O O   . GLN   A 1 126 ? 7.22222   -1.41313  -14.82926 1.000 21.95902 ?  133 GLN   A O   1 
ATOM   904  C CB  . GLN   A 1 126 ? 6.23457   -2.08610  -12.04814 1.000 23.33828 ?  133 GLN   A CB  1 
ATOM   905  C CG  . GLN   A 1 126 ? 5.04108   -1.90750  -11.08893 1.000 24.35914 ?  133 GLN   A CG  1 
ATOM   906  C CD  . GLN   A 1 126 ? 5.42320   -1.30729  -9.77287  1.000 32.78180 ?  133 GLN   A CD  1 
ATOM   907  O OE1 . GLN   A 1 126 ? 6.17160   -0.31661  -9.71518  1.000 34.37450 ?  133 GLN   A OE1 1 
ATOM   908  N NE2 . GLN   A 1 126 ? 4.99499   -1.96307  -8.68819  1.000 37.29203 ?  133 GLN   A NE2 1 
ATOM   909  N N   . PHE   A 1 127 ? 7.43163   -3.66362  -14.80566 1.000 16.63120 ?  134 PHE   A N   1 
ATOM   910  C CA  . PHE   A 1 127 ? 8.54021   -3.72549  -15.75058 1.000 16.82832 ?  134 PHE   A CA  1 
ATOM   911  C C   . PHE   A 1 127 ? 8.10491   -4.30001  -17.08596 1.000 18.69043 ?  134 PHE   A C   1 
ATOM   912  O O   . PHE   A 1 127 ? 8.95059   -4.53739  -17.95308 1.000 18.39767 ?  134 PHE   A O   1 
ATOM   913  C CB  . PHE   A 1 127 ? 9.68463   -4.52160  -15.11323 1.000 15.79750 ?  134 PHE   A CB  1 
ATOM   914  C CG  . PHE   A 1 127 ? 10.10696  -3.91704  -13.80444 1.000 17.56531 ?  134 PHE   A CG  1 
ATOM   915  C CD1 . PHE   A 1 127 ? 10.99363  -2.85100  -13.79467 1.000 20.67899 ?  134 PHE   A CD1 1 
ATOM   916  C CD2 . PHE   A 1 127 ? 9.52990   -4.34577  -12.61866 1.000 19.11482 ?  134 PHE   A CD2 1 
ATOM   917  C CE1 . PHE   A 1 127 ? 11.35164  -2.22716  -12.60310 1.000 21.92294 ?  134 PHE   A CE1 1 
ATOM   918  C CE2 . PHE   A 1 127 ? 9.87830   -3.75746  -11.39303 1.000 21.35350 ?  134 PHE   A CE2 1 
ATOM   919  C CZ  . PHE   A 1 127 ? 10.77333  -2.67656  -11.38595 1.000 23.07684 ?  134 PHE   A CZ  1 
ATOM   920  N N   . GLY   A 1 128 ? 6.80343   -4.49399  -17.26330 1.000 15.69588 ?  135 GLY   A N   1 
ATOM   921  C CA  . GLY   A 1 128 ? 6.28980   -4.84466  -18.59089 1.000 15.33725 ?  135 GLY   A CA  1 
ATOM   922  C C   . GLY   A 1 128 ? 6.54379   -6.28159  -19.00439 1.000 18.89000 ?  135 GLY   A C   1 
ATOM   923  O O   . GLY   A 1 128 ? 6.40358   -6.60912  -20.18424 1.000 19.42502 ?  135 GLY   A O   1 
ATOM   924  N N   . VAL   A 1 129 ? 6.90907   -7.16946  -18.06381 1.000 14.78778 ?  136 VAL   A N   1 
ATOM   925  C CA  . VAL   A 1 129 ? 7.24445   -8.55232  -18.37224 1.000 13.82846 ?  136 VAL   A CA  1 
ATOM   926  C C   . VAL   A 1 129 ? 6.40595   -9.49041  -17.48902 1.000 15.32514 ?  136 VAL   A C   1 
ATOM   927  O O   . VAL   A 1 129 ? 6.78988   -10.63254 -17.21991 1.000 14.62903 ?  136 VAL   A O   1 
ATOM   928  C CB  . VAL   A 1 129 ? 8.77135   -8.78449  -18.24100 1.000 14.72191 ?  136 VAL   A CB  1 
ATOM   929  C CG1 . VAL   A 1 129 ? 9.48758   -8.01538  -19.39428 1.000 16.33692 ?  136 VAL   A CG1 1 
ATOM   930  C CG2 . VAL   A 1 129 ? 9.32857   -8.36397  -16.85911 1.000 16.24490 ?  136 VAL   A CG2 1 
ATOM   931  N N   . GLY   A 1 130 ? 5.18631   -9.01731  -17.13259 1.000 16.73243 ?  137 GLY   A N   1 
ATOM   932  C CA  . GLY   A 1 130 ? 4.30254   -9.81913  -16.25922 1.000 17.30454 ?  137 GLY   A CA  1 
ATOM   933  C C   . GLY   A 1 130 ? 3.90118   -11.16637 -16.81546 1.000 15.29626 ?  137 GLY   A C   1 
ATOM   934  O O   . GLY   A 1 130 ? 3.61437   -12.08880 -16.03787 1.000 15.23224 ?  137 GLY   A O   1 
ATOM   935  N N   . PHE   A 1 131 ? 3.87873   -11.31115 -18.14698 1.000 14.00892 ?  138 PHE   A N   1 
ATOM   936  C CA  . PHE   A 1 131 ? 3.53869   -12.59716 -18.75306 1.000 14.21021 ?  138 PHE   A CA  1 
ATOM   937  C C   . PHE   A 1 131 ? 4.38890   -13.71586 -18.12712 1.000 12.43400 ?  138 PHE   A C   1 
ATOM   938  O O   . PHE   A 1 131 ? 3.89076   -14.82309 -17.86638 1.000 12.79600 ?  138 PHE   A O   1 
ATOM   939  C CB  . PHE   A 1 131 ? 3.77094   -12.56124 -20.28341 1.000 15.08267 ?  138 PHE   A CB  1 
ATOM   940  C CG  . PHE   A 1 131 ? 3.74405   -13.91819 -20.88729 1.000 13.36355 ?  138 PHE   A CG  1 
ATOM   941  C CD1 . PHE   A 1 131 ? 2.53628   -14.57654 -21.08268 1.000 14.56056 ?  138 PHE   A CD1 1 
ATOM   942  C CD2 . PHE   A 1 131 ? 4.97523   -14.58795 -21.20167 1.000 12.92505 ?  138 PHE   A CD2 1 
ATOM   943  C CE1 . PHE   A 1 131 ? 2.48350   -15.87795 -21.61252 1.000 13.76168 ?  138 PHE   A CE1 1 
ATOM   944  C CE2 . PHE   A 1 131 ? 4.91337   -15.91665 -21.76120 1.000 12.30328 ?  138 PHE   A CE2 1 
ATOM   945  C CZ  . PHE   A 1 131 ? 3.67767   -16.55890 -21.93328 1.000 13.18210 ?  138 PHE   A CZ  1 
ATOM   946  N N   . TYR   A 1 132 ? 5.68246   -13.45840 -17.92409 1.000 13.86605 ?  139 TYR   A N   1 
ATOM   947  C CA  . TYR   A 1 132 ? 6.56327   -14.56460 -17.53361 1.000 12.01395 ?  139 TYR   A CA  1 
ATOM   948  C C   . TYR   A 1 132 ? 6.31756   -15.02089 -16.10436 1.000 14.69914 ?  139 TYR   A C   1 
ATOM   949  O O   . TYR   A 1 132 ? 6.77906   -16.11648 -15.75482 1.000 14.82276 ?  139 TYR   A O   1 
ATOM   950  C CB  . TYR   A 1 132 ? 8.04042   -14.13954 -17.70924 1.000 12.61884 ?  139 TYR   A CB  1 
ATOM   951  C CG  . TYR   A 1 132 ? 8.31108   -13.85020 -19.18847 1.000 13.95150 ?  139 TYR   A CG  1 
ATOM   952  C CD1 . TYR   A 1 132 ? 8.68182   -14.87234 -20.03835 1.000 14.25769 ?  139 TYR   A CD1 1 
ATOM   953  C CD2 . TYR   A 1 132 ? 8.17043   -12.55054 -19.67700 1.000 15.88958 ?  139 TYR   A CD2 1 
ATOM   954  C CE1 . TYR   A 1 132 ? 8.91040   -14.59815 -21.43802 1.000 14.31052 ?  139 TYR   A CE1 1 
ATOM   955  C CE2 . TYR   A 1 132 ? 8.38467   -12.26051 -21.01740 1.000 15.80832 ?  139 TYR   A CE2 1 
ATOM   956  C CZ  . TYR   A 1 132 ? 8.73395   -13.29224 -21.87932 1.000 16.89633 ?  139 TYR   A CZ  1 
ATOM   957  O OH  . TYR   A 1 132 ? 8.91355   -12.97903 -23.20757 1.000 17.18417 ?  139 TYR   A OH  1 
ATOM   958  N N   . SER   A 1 133 ? 5.53109   -14.26385 -15.32259 1.000 13.07942 ?  140 SER   A N   1 
ATOM   959  C CA  . SER   A 1 133 ? 5.10155   -14.76294 -14.00656 1.000 13.10341 ?  140 SER   A CA  1 
ATOM   960  C C   . SER   A 1 133 ? 4.24848   -16.01865 -14.13255 1.000 11.91161 ?  140 SER   A C   1 
ATOM   961  O O   . SER   A 1 133 ? 4.01255   -16.70427 -13.10854 1.000 14.39292 ?  140 SER   A O   1 
ATOM   962  C CB  . SER   A 1 133 ? 4.30472   -13.68376 -13.20796 1.000 17.07718 ?  140 SER   A CB  1 
ATOM   963  O OG  . SER   A 1 133 ? 3.07607   -13.42686 -13.82211 1.000 17.13444 ?  140 SER   A OG  1 
ATOM   964  N N   . ALA   A 1 134 ? 3.75722   -16.33151 -15.32830 1.000 12.12044 ?  141 ALA   A N   1 
ATOM   965  C CA  . ALA   A 1 134 ? 3.03976   -17.60260 -15.52377 1.000 12.93537 ?  141 ALA   A CA  1 
ATOM   966  C C   . ALA   A 1 134 ? 3.89072   -18.75123 -15.02134 1.000 13.47326 ?  141 ALA   A C   1 
ATOM   967  O O   . ALA   A 1 134 ? 3.34538   -19.74977 -14.55192 1.000 14.25325 ?  141 ALA   A O   1 
ATOM   968  C CB  . ALA   A 1 134 ? 2.74936   -17.80896 -17.02866 1.000 11.38559 ?  141 ALA   A CB  1 
ATOM   969  N N   . TYR   A 1 135 ? 5.25948   -18.61009 -15.13190 1.000 12.23013 ?  142 TYR   A N   1 
ATOM   970  C CA  . TYR   A 1 135 ? 6.14658   -19.72962 -14.75894 1.000 13.62092 ?  142 TYR   A CA  1 
ATOM   971  C C   . TYR   A 1 135 ? 6.30371   -19.87577 -13.24017 1.000 14.11911 ?  142 TYR   A C   1 
ATOM   972  O O   . TYR   A 1 135 ? 6.94460   -20.83413 -12.78280 1.000 15.94775 ?  142 TYR   A O   1 
ATOM   973  C CB  . TYR   A 1 135 ? 7.50899   -19.62979 -15.46934 1.000 12.84813 ?  142 TYR   A CB  1 
ATOM   974  C CG  . TYR   A 1 135 ? 7.28732   -19.93152 -16.96241 1.000 13.78986 ?  142 TYR   A CG  1 
ATOM   975  C CD1 . TYR   A 1 135 ? 7.26633   -21.25435 -17.42038 1.000 15.36623 ?  142 TYR   A CD1 1 
ATOM   976  C CD2 . TYR   A 1 135 ? 7.01466   -18.89666 -17.84847 1.000 12.19656 ?  142 TYR   A CD2 1 
ATOM   977  C CE1 . TYR   A 1 135 ? 6.98696   -21.56296 -18.77894 1.000 16.04711 ?  142 TYR   A CE1 1 
ATOM   978  C CE2 . TYR   A 1 135 ? 6.77526   -19.17451 -19.19130 1.000 13.18732 ?  142 TYR   A CE2 1 
ATOM   979  C CZ  . TYR   A 1 135 ? 6.74916   -20.49680 -19.63372 1.000 16.52839 ?  142 TYR   A CZ  1 
ATOM   980  O OH  . TYR   A 1 135 ? 6.50834   -20.74105 -20.95047 1.000 13.41383 ?  142 TYR   A OH  1 
ATOM   981  N N   . LEU   A 1 136 ? 5.64973   -19.01049 -12.45741 1.000 14.02411 ?  143 LEU   A N   1 
ATOM   982  C CA  . LEU   A 1 136 ? 5.49725   -19.27872 -11.03024 1.000 14.48416 ?  143 LEU   A CA  1 
ATOM   983  C C   . LEU   A 1 136 ? 4.65214   -20.52495 -10.79051 1.000 15.20772 ?  143 LEU   A C   1 
ATOM   984  O O   . LEU   A 1 136 ? 4.83438   -21.21471 -9.78495  1.000 17.66564 ?  143 LEU   A O   1 
ATOM   985  C CB  . LEU   A 1 136 ? 4.79616   -18.08142 -10.34707 1.000 16.41937 ?  143 LEU   A CB  1 
ATOM   986  C CG  . LEU   A 1 136 ? 5.64517   -16.78540 -10.26774 1.000 16.67097 ?  143 LEU   A CG  1 
ATOM   987  C CD1 . LEU   A 1 136 ? 4.78412   -15.61298 -9.81331  1.000 16.14111 ?  143 LEU   A CD1 1 
ATOM   988  C CD2 . LEU   A 1 136 ? 6.99581   -16.98454 -9.39291  1.000 17.31633 ?  143 LEU   A CD2 1 
ATOM   989  N N   . VAL   A 1 137 ? 3.68207   -20.80788 -11.67895 1.000 15.31283 ?  144 VAL   A N   1 
ATOM   990  C CA  . VAL   A 1 137 ? 2.72257   -21.86474 -11.35411 1.000 15.91333 ?  144 VAL   A CA  1 
ATOM   991  C C   . VAL   A 1 137 ? 2.62714   -22.90714 -12.46697 1.000 14.11158 ?  144 VAL   A C   1 
ATOM   992  O O   . VAL   A 1 137 ? 2.11701   -24.00673 -12.22043 1.000 17.13006 ?  144 VAL   A O   1 
ATOM   993  C CB  . VAL   A 1 137 ? 1.30755   -21.32732 -11.04660 1.000 15.17729 ?  144 VAL   A CB  1 
ATOM   994  C CG1 . VAL   A 1 137 ? 1.34684   -20.41392 -9.78271  1.000 16.78806 ?  144 VAL   A CG1 1 
ATOM   995  C CG2 . VAL   A 1 137 ? 0.69610   -20.52109 -12.30064 1.000 16.85816 ?  144 VAL   A CG2 1 
ATOM   996  N N   . ALA   A 1 138 ? 3.18410   -22.61328 -13.62802 1.000 15.34246 ?  145 ALA   A N   1 
ATOM   997  C CA  . ALA   A 1 138 ? 3.05148   -23.49113 -14.80252 1.000 14.90908 ?  145 ALA   A CA  1 
ATOM   998  C C   . ALA   A 1 138 ? 4.37649   -24.12832 -15.15520 1.000 15.77510 ?  145 ALA   A C   1 
ATOM   999  O O   . ALA   A 1 138 ? 5.37839   -23.40577 -15.25528 1.000 16.85644 ?  145 ALA   A O   1 
ATOM   1000 C CB  . ALA   A 1 138 ? 2.52785   -22.69703 -16.02120 1.000 15.08855 ?  145 ALA   A CB  1 
ATOM   1001 N N   . GLU   A 1 139 ? 4.33761   -25.43473 -15.46700 1.000 15.67873 ?  146 GLU   A N   1 
ATOM   1002 C CA  . GLU   A 1 139 ? 5.53009   -26.11408 -16.01028 1.000 15.32151 ?  146 GLU   A CA  1 
ATOM   1003 C C   . GLU   A 1 139 ? 5.63663   -25.88337 -17.50767 1.000 15.84861 ?  146 GLU   A C   1 
ATOM   1004 O O   . GLU   A 1 139 ? 6.74541   -25.94810 -18.06412 1.000 17.80857 ?  146 GLU   A O   1 
ATOM   1005 C CB  . GLU   A 1 139 ? 5.49308   -27.62669 -15.72533 1.000 19.26038 ?  146 GLU   A CB  1 
ATOM   1006 C CG  . GLU   A 1 139 ? 4.30898   -28.31591 -16.37712 1.000 22.74615 ?  146 GLU   A CG  1 
ATOM   1007 C CD  . GLU   A 1 139 ? 4.05235   -29.73347 -15.90031 1.000 44.46956 ?  146 GLU   A CD  1 
ATOM   1008 O OE1 . GLU   A 1 139 ? 4.73506   -30.14848 -14.93374 1.000 39.49702 ?  146 GLU   A OE1 1 
ATOM   1009 O OE2 . GLU   A 1 139 ? 3.14662   -30.40736 -16.48851 1.000 36.11600 ?  146 GLU   A OE2 1 
ATOM   1010 N N   . LYS   A 1 140 ? 4.51001   -25.63479 -18.18050 1.000 15.12021 ?  147 LYS   A N   1 
ATOM   1011 C CA  . LYS   A 1 140 ? 4.49884   -25.39550 -19.62001 1.000 14.00202 ?  147 LYS   A CA  1 
ATOM   1012 C C   . LYS   A 1 140 ? 3.43323   -24.34164 -19.85783 1.000 14.78311 ?  147 LYS   A C   1 
ATOM   1013 O O   . LYS   A 1 140 ? 2.41026   -24.35629 -19.17667 1.000 14.47572 ?  147 LYS   A O   1 
ATOM   1014 C CB  . LYS   A 1 140 ? 4.21632   -26.65512 -20.40798 1.000 13.98527 ?  147 LYS   A CB  1 
ATOM   1015 C CG  . LYS   A 1 140 ? 4.20731   -26.42083 -21.91497 1.000 14.47454 ?  147 LYS   A CG  1 
ATOM   1016 C CD  . LYS   A 1 140 ? 4.22454   -27.74714 -22.62354 1.000 20.53415 ?  147 LYS   A CD  1 
ATOM   1017 C CE  . LYS   A 1 140 ? 2.83801   -28.23713 -22.78074 1.000 25.92472 ?  147 LYS   A CE  1 
ATOM   1018 N NZ  . LYS   A 1 140 ? 2.87814   -29.66457 -23.28626 1.000 34.09112 ?  147 LYS   A NZ  1 
ATOM   1019 N N   . VAL   A 1 141 ? 3.69321   -23.41228 -20.75293 1.000 12.79023 ?  148 VAL   A N   1 
ATOM   1020 C CA  . VAL   A 1 141 ? 2.68100   -22.43093 -21.12691 1.000 10.44097 ?  148 VAL   A CA  1 
ATOM   1021 C C   . VAL   A 1 141 ? 2.49383   -22.49617 -22.63020 1.000 14.04554 ?  148 VAL   A C   1 
ATOM   1022 O O   . VAL   A 1 141 ? 3.47880   -22.49153 -23.38803 1.000 13.23761 ?  148 VAL   A O   1 
ATOM   1023 C CB  . VAL   A 1 141 ? 3.10445   -21.01945 -20.72996 1.000 13.05242 ?  148 VAL   A CB  1 
ATOM   1024 C CG1 . VAL   A 1 141 ? 2.02714   -19.98195 -21.18705 1.000 12.82931 ?  148 VAL   A CG1 1 
ATOM   1025 C CG2 . VAL   A 1 141 ? 3.34569   -20.95736 -19.17672 1.000 13.19281 ?  148 VAL   A CG2 1 
ATOM   1026 N N   . THR   A 1 142 ? 1.22180   -22.56985 -23.06634 1.000 12.89761 ?  149 THR   A N   1 
ATOM   1027 C CA  . THR   A 1 142 ? 0.87127   -22.55678 -24.49058 1.000 13.45285 ?  149 THR   A CA  1 
ATOM   1028 C C   . THR   A 1 142 ? 0.05219   -21.30972 -24.76500 1.000 13.35745 ?  149 THR   A C   1 
ATOM   1029 O O   . THR   A 1 142 ? -0.86411  -21.00421 -24.00931 1.000 15.61892 ?  149 THR   A O   1 
ATOM   1030 C CB  . THR   A 1 142 ? 0.04607   -23.78902 -24.87006 1.000 13.93278 ?  149 THR   A CB  1 
ATOM   1031 O OG1 . THR   A 1 142 ? 0.69944   -24.97635 -24.42174 1.000 17.31476 ?  149 THR   A OG1 1 
ATOM   1032 C CG2 . THR   A 1 142 ? -0.18769  -23.80034 -26.39099 1.000 15.06349 ?  149 THR   A CG2 1 
ATOM   1033 N N   . VAL   A 1 143 ? 0.41264   -20.53362 -25.78166 1.000 12.16868 ?  150 VAL   A N   1 
ATOM   1034 C CA  . VAL   A 1 143 ? -0.28696  -19.28076 -26.07135 1.000 10.92328 ?  150 VAL   A CA  1 
ATOM   1035 C C   . VAL   A 1 143 ? -0.84816  -19.42731 -27.47011 1.000 14.44679 ?  150 VAL   A C   1 
ATOM   1036 O O   . VAL   A 1 143 ? -0.06938  -19.56424 -28.43607 1.000 14.05819 ?  150 VAL   A O   1 
ATOM   1037 C CB  . VAL   A 1 143 ? 0.62134   -18.06065 -25.97648 1.000 11.22032 ?  150 VAL   A CB  1 
ATOM   1038 C CG1 . VAL   A 1 143 ? -0.13367  -16.77207 -26.37221 1.000 16.27311 ?  150 VAL   A CG1 1 
ATOM   1039 C CG2 . VAL   A 1 143 ? 1.19645   -17.96907 -24.55930 1.000 12.20690 ?  150 VAL   A CG2 1 
ATOM   1040 N N   . ILE   A 1 144 ? -2.17416  -19.41110 -27.60027 1.000 12.58577 ?  151 ILE   A N   1 
ATOM   1041 C CA  . ILE   A 1 144 ? -2.80508  -19.41891 -28.93042 1.000 13.08103 ?  151 ILE   A CA  1 
ATOM   1042 C C   . ILE   A 1 144 ? -3.25785  -18.01146 -29.20870 1.000 12.89613 ?  151 ILE   A C   1 
ATOM   1043 O O   . ILE   A 1 144 ? -3.86525  -17.37040 -28.32799 1.000 13.33107 ?  151 ILE   A O   1 
ATOM   1044 C CB  . ILE   A 1 144 ? -4.01808  -20.34845 -28.97295 1.000 14.37058 ?  151 ILE   A CB  1 
ATOM   1045 C CG1 . ILE   A 1 144 ? -3.78294  -21.69569 -28.30116 1.000 18.25413 ?  151 ILE   A CG1 1 
ATOM   1046 C CG2 . ILE   A 1 144 ? -4.49374  -20.51958 -30.44366 1.000 16.76172 ?  151 ILE   A CG2 1 
ATOM   1047 C CD1 . ILE   A 1 144 ? -2.72859  -22.53928 -28.96355 1.000 21.36491 ?  151 ILE   A CD1 1 
ATOM   1048 N N   . THR   A 1 145 ? -2.98530  -17.49062 -30.40749 1.000 11.56791 ?  152 THR   A N   1 
ATOM   1049 C CA  . THR   A 1 145 ? -3.36570  -16.10258 -30.60815 1.000 12.69456 ?  152 THR   A CA  1 
ATOM   1050 C C   . THR   A 1 145 ? -3.77941  -15.88171 -32.05224 1.000 14.35885 ?  152 THR   A C   1 
ATOM   1051 O O   . THR   A 1 145 ? -3.34652  -16.60244 -32.95521 1.000 15.20617 ?  152 THR   A O   1 
ATOM   1052 C CB  . THR   A 1 145 ? -2.16628  -15.17813 -30.22597 1.000 12.79277 ?  152 THR   A CB  1 
ATOM   1053 O OG1 . THR   A 1 145 ? -2.57959  -13.79318 -30.18066 1.000 14.25578 ?  152 THR   A OG1 1 
ATOM   1054 C CG2 . THR   A 1 145 ? -1.00957  -15.36331 -31.23196 1.000 14.29320 ?  152 THR   A CG2 1 
ATOM   1055 N N   . LYS   A 1 146 ? -4.60002  -14.83866 -32.23989 1.000 12.72248 ?  153 LYS   A N   1 
ATOM   1056 C CA  . LYS   A 1 146 ? -5.11555  -14.51398 -33.56617 1.000 13.09785 ?  153 LYS   A CA  1 
ATOM   1057 C C   . LYS   A 1 146 ? -5.29483  -13.01596 -33.61869 1.000 14.40065 ?  153 LYS   A C   1 
ATOM   1058 O O   . LYS   A 1 146 ? -6.09728  -12.46995 -32.85179 1.000 16.28313 ?  153 LYS   A O   1 
ATOM   1059 C CB  . LYS   A 1 146 ? -6.47134  -15.20595 -33.81145 1.000 13.66461 ?  153 LYS   A CB  1 
ATOM   1060 C CG  . LYS   A 1 146 ? -7.14663  -14.82069 -35.15421 1.000 18.44005 ?  153 LYS   A CG  1 
ATOM   1061 C CD  . LYS   A 1 146 ? -6.32447  -15.26302 -36.33603 1.000 17.96514 ?  153 LYS   A CD  1 
ATOM   1062 C CE  . LYS   A 1 146 ? -7.13003  -14.94810 -37.65498 1.000 20.55404 ?  153 LYS   A CE  1 
ATOM   1063 N NZ  . LYS   A 1 146 ? -7.19106  -13.50678 -38.01323 1.000 19.56607 ?  153 LYS   A NZ  1 
ATOM   1064 N N   . HIS   A 1 147 ? -4.55945  -12.37012 -34.49784 1.000 14.10874 ?  154 HIS   A N   1 
ATOM   1065 C CA  . HIS   A 1 147 ? -4.62677  -10.95221 -34.76230 1.000 14.61425 ?  154 HIS   A CA  1 
ATOM   1066 C C   . HIS   A 1 147 ? -5.33015  -10.74449 -36.09241 1.000 18.95259 ?  154 HIS   A C   1 
ATOM   1067 O O   . HIS   A 1 147 ? -5.20167  -11.57792 -36.99378 1.000 20.29354 ?  154 HIS   A O   1 
ATOM   1068 C CB  . HIS   A 1 147 ? -3.16875  -10.40234 -34.80299 1.000 17.33219 ?  154 HIS   A CB  1 
ATOM   1069 C CG  . HIS   A 1 147 ? -3.04617  -8.89914  -34.86120 1.000 18.28670 ?  154 HIS   A CG  1 
ATOM   1070 N ND1 . HIS   A 1 147 ? -3.31180  -8.17259  -35.99872 1.000 21.74676 ?  154 HIS   A ND1 1 
ATOM   1071 C CD2 . HIS   A 1 147 ? -2.56695  -8.01689  -33.95089 1.000 18.26380 ?  154 HIS   A CD2 1 
ATOM   1072 C CE1 . HIS   A 1 147 ? -3.08492  -6.89337  -35.75567 1.000 25.00270 ?  154 HIS   A CE1 1 
ATOM   1073 N NE2 . HIS   A 1 147 ? -2.64309  -6.78114  -34.51441 1.000 19.40237 ?  154 HIS   A NE2 1 
ATOM   1074 N N   . ASN   A 1 148 ? -6.09038  -9.64435  -36.21342 1.000 17.84108 ?  155 ASN   A N   1 
ATOM   1075 C CA  . ASN   A 1 148 ? -6.76846  -9.37788  -37.47220 1.000 18.01730 ?  155 ASN   A CA  1 
ATOM   1076 C C   . ASN   A 1 148 ? -5.81325  -9.44748  -38.66306 1.000 20.79984 ?  155 ASN   A C   1 
ATOM   1077 O O   . ASN   A 1 148 ? -6.24297  -9.79153  -39.78295 1.000 24.49204 ?  155 ASN   A O   1 
ATOM   1078 C CB  . ASN   A 1 148 ? -7.44956  -7.96815  -37.45075 1.000 19.46471 ?  155 ASN   A CB  1 
ATOM   1079 C CG  . ASN   A 1 148 ? -8.71913  -7.95981  -36.61342 1.000 20.68763 ?  155 ASN   A CG  1 
ATOM   1080 O OD1 . ASN   A 1 148 ? -9.35543  -8.99292  -36.45067 1.000 23.11210 ?  155 ASN   A OD1 1 
ATOM   1081 N ND2 . ASN   A 1 148 ? -9.09997  -6.77447  -36.08404 1.000 21.54702 ?  155 ASN   A ND2 1 
ATOM   1082 N N   . ASP   A 1 149 ? -4.54452  -9.05743  -38.47535 1.000 20.89181 ?  156 ASP   A N   1 
ATOM   1083 C CA  . ASP   A 1 149 ? -3.60084  -8.94023  -39.59901 1.000 37.17920 ?  156 ASP   A CA  1 
ATOM   1084 C C   . ASP   A 1 149 ? -2.80091  -10.22245 -39.90566 1.000 50.48601 ?  156 ASP   A C   1 
ATOM   1085 O O   . ASP   A 1 149 ? -1.92577  -10.18247 -40.78375 1.000 44.31097 ?  156 ASP   A O   1 
ATOM   1086 C CB  . ASP   A 1 149 ? -2.64113  -7.75189  -39.35757 1.000 36.34188 ?  156 ASP   A CB  1 
ATOM   1087 C CG  . ASP   A 1 149 ? -3.36942  -6.40183  -39.41773 1.000 37.11508 ?  156 ASP   A CG  1 
ATOM   1088 O OD1 . ASP   A 1 149 ? -4.48447  -6.35787  -39.98319 1.000 38.54093 ?  156 ASP   A OD1 1 
ATOM   1089 O OD2 . ASP   A 1 149 ? -2.84840  -5.39720  -38.89906 1.000 45.77639 ?  156 ASP   A OD2 1 
ATOM   1090 N N   . ASP   A 1 150 ? -3.09782  -11.36003 -39.25446 1.000 34.10210 ?  157 ASP   A N   1 
ATOM   1091 C CA  . ASP   A 1 150 ? -2.28431  -12.55712 -39.40171 1.000 30.57778 ?  157 ASP   A CA  1 
ATOM   1092 C C   . ASP   A 1 150 ? -3.15854  -13.83387 -39.25195 1.000 26.75409 ?  157 ASP   A C   1 
ATOM   1093 O O   . ASP   A 1 150 ? -4.37920  -13.78883 -39.05684 1.000 26.79828 ?  157 ASP   A O   1 
ATOM   1094 C CB  . ASP   A 1 150 ? -1.10495  -12.44328 -38.40817 1.000 32.55974 ?  157 ASP   A CB  1 
ATOM   1095 C CG  . ASP   A 1 150 ? 0.17666   -13.09135 -38.92004 1.000 39.20621 ?  157 ASP   A CG  1 
ATOM   1096 O OD1 . ASP   A 1 150 ? -0.01176  -13.92620 -39.82314 1.000 33.47767 ?  157 ASP   A OD1 1 
ATOM   1097 O OD2 . ASP   A 1 150 ? 1.34254   -12.86266 -38.39357 1.000 27.35143 ?  157 ASP   A OD2 1 
ATOM   1098 N N   . GLU   A 1 151 ? -2.52581  -14.98648 -39.39393 1.000 22.92784 ?  158 GLU   A N   1 
ATOM   1099 C CA  . GLU   A 1 151 ? -3.11358  -16.28395 -39.13683 1.000 22.92646 ?  158 GLU   A CA  1 
ATOM   1100 C C   . GLU   A 1 151 ? -3.09750  -16.59145 -37.66010 1.000 23.60069 ?  158 GLU   A C   1 
ATOM   1101 O O   . GLU   A 1 151 ? -2.45379  -15.91337 -36.86547 1.000 22.29979 ?  158 GLU   A O   1 
ATOM   1102 C CB  . GLU   A 1 151 ? -2.35504  -17.39525 -39.85381 1.000 25.18261 ?  158 GLU   A CB  1 
ATOM   1103 C CG  . GLU   A 1 151 ? -1.58761  -16.90448 -41.05802 1.000 48.20450 ?  158 GLU   A CG  1 
ATOM   1104 C CD  . GLU   A 1 151 ? -1.05136  -18.03917 -41.92830 1.000 56.27165 ?  158 GLU   A CD  1 
ATOM   1105 O OE1 . GLU   A 1 151 ? -0.32203  -17.73109 -42.89501 1.000 65.06475 ?  158 GLU   A OE1 1 
ATOM   1106 O OE2 . GLU   A 1 151 ? -1.38791  -19.22167 -41.68026 1.000 65.69369 ?  158 GLU   A OE2 1 
ATOM   1107 N N   . GLN   A 1 152 ? -3.73505  -17.68927 -37.30645 1.000 17.87337 ?  159 GLN   A N   1 
ATOM   1108 C CA  . GLN   A 1 152 ? -3.72238  -18.13631 -35.90677 1.000 16.82281 ?  159 GLN   A CA  1 
ATOM   1109 C C   . GLN   A 1 152 ? -2.44301  -18.90919 -35.61106 1.000 17.70639 ?  159 GLN   A C   1 
ATOM   1110 O O   . GLN   A 1 152 ? -2.06095  -19.77947 -36.39083 1.000 19.80557 ?  159 GLN   A O   1 
ATOM   1111 C CB  . GLN   A 1 152 ? -4.92428  -19.02074 -35.64416 1.000 16.52144 ?  159 GLN   A CB  1 
ATOM   1112 C CG  . GLN   A 1 152 ? -5.11781  -19.37264 -34.14383 1.000 15.89543 ?  159 GLN   A CG  1 
ATOM   1113 C CD  . GLN   A 1 152 ? -6.53523  -19.88084 -33.88530 1.000 17.22180 ?  159 GLN   A CD  1 
ATOM   1114 O OE1 . GLN   A 1 152 ? -7.49829  -19.22532 -34.23671 1.000 21.20092 ?  159 GLN   A OE1 1 
ATOM   1115 N NE2 . GLN   A 1 152 ? -6.64335  -21.05505 -33.29184 1.000 18.94844 ?  159 GLN   A NE2 1 
ATOM   1116 N N   . TYR   A 1 153 ? -1.76663  -18.58843 -34.49728 1.000 15.20479 ?  160 TYR   A N   1 
ATOM   1117 C CA  . TYR   A 1 153 ? -0.50816  -19.23758 -34.14794 1.000 16.95315 ?  160 TYR   A CA  1 
ATOM   1118 C C   . TYR   A 1 153 ? -0.55737  -19.80676 -32.74019 1.000 14.97230 ?  160 TYR   A C   1 
ATOM   1119 O O   . TYR   A 1 153 ? -1.29745  -19.30444 -31.89427 1.000 15.07489 ?  160 TYR   A O   1 
ATOM   1120 C CB  . TYR   A 1 153 ? 0.66796   -18.24177 -34.19374 1.000 15.10674 ?  160 TYR   A CB  1 
ATOM   1121 C CG  . TYR   A 1 153 ? 0.91340   -17.71466 -35.55458 1.000 20.67310 ?  160 TYR   A CG  1 
ATOM   1122 C CD1 . TYR   A 1 153 ? 1.65576   -18.44189 -36.43783 1.000 21.86453 ?  160 TYR   A CD1 1 
ATOM   1123 C CD2 . TYR   A 1 153 ? 0.34951   -16.48619 -35.95227 1.000 24.24661 ?  160 TYR   A CD2 1 
ATOM   1124 C CE1 . TYR   A 1 153 ? 1.85580   -17.97485 -37.74611 1.000 27.18464 ?  160 TYR   A CE1 1 
ATOM   1125 C CE2 . TYR   A 1 153 ? 0.52156   -16.01843 -37.19900 1.000 24.89954 ?  160 TYR   A CE2 1 
ATOM   1126 C CZ  . TYR   A 1 153 ? 1.28315   -16.75782 -38.09590 1.000 24.39005 ?  160 TYR   A CZ  1 
ATOM   1127 O OH  . TYR   A 1 153 ? 1.48682   -16.25520 -39.35990 1.000 36.36789 ?  160 TYR   A OH  1 
ATOM   1128 N N   . ALA   A 1 154 ? 0.27894   -20.82430 -32.49146 1.000 15.50700 ?  161 ALA   A N   1 
ATOM   1129 C CA  . ALA   A 1 154 ? 0.52501   -21.37191 -31.15556 1.000 15.82369 ?  161 ALA   A CA  1 
ATOM   1130 C C   . ALA   A 1 154 ? 1.99388   -21.15568 -30.79900 1.000 14.77089 ?  161 ALA   A C   1 
ATOM   1131 O O   . ALA   A 1 154 ? 2.87678   -21.63281 -31.53210 1.000 15.25883 ?  161 ALA   A O   1 
ATOM   1132 C CB  . ALA   A 1 154 ? 0.21414   -22.88709 -31.10073 1.000 18.19645 ?  161 ALA   A CB  1 
ATOM   1133 N N   . TRP   A 1 155 ? 2.22612   -20.48073 -29.67547 1.000 13.35375 ?  162 TRP   A N   1 
ATOM   1134 C CA  . TRP   A 1 155 ? 3.54625   -20.37256 -29.06024 1.000 12.53414 ?  162 TRP   A CA  1 
ATOM   1135 C C   . TRP   A 1 155 ? 3.59479   -21.32851 -27.87717 1.000 13.64559 ?  162 TRP   A C   1 
ATOM   1136 O O   . TRP   A 1 155 ? 2.58385   -21.55053 -27.21523 1.000 14.19549 ?  162 TRP   A O   1 
ATOM   1137 C CB  . TRP   A 1 155 ? 3.73606   -18.91957 -28.60522 1.000 14.37413 ?  162 TRP   A CB  1 
ATOM   1138 C CG  . TRP   A 1 155 ? 4.96842   -18.54959 -27.82018 1.000 14.17415 ?  162 TRP   A CG  1 
ATOM   1139 C CD1 . TRP   A 1 155 ? 6.04639   -17.85253 -28.30145 1.000 11.94709 ?  162 TRP   A CD1 1 
ATOM   1140 C CD2 . TRP   A 1 155 ? 5.21168   -18.77540 -26.41799 1.000 14.37488 ?  162 TRP   A CD2 1 
ATOM   1141 N NE1 . TRP   A 1 155 ? 6.96613   -17.62612 -27.27399 1.000 13.27269 ?  162 TRP   A NE1 1 
ATOM   1142 C CE2 . TRP   A 1 155 ? 6.47524   -18.19672 -26.12903 1.000 12.76129 ?  162 TRP   A CE2 1 
ATOM   1143 C CE3 . TRP   A 1 155 ? 4.51459   -19.44041 -25.39599 1.000 11.82158 ?  162 TRP   A CE3 1 
ATOM   1144 C CZ2 . TRP   A 1 155 ? 7.03729   -18.21902 -24.83660 1.000 14.69809 ?  162 TRP   A CZ2 1 
ATOM   1145 C CZ3 . TRP   A 1 155 ? 5.06819   -19.43833 -24.10467 1.000 13.53656 ?  162 TRP   A CZ3 1 
ATOM   1146 C CH2 . TRP   A 1 155 ? 6.33579   -18.85903 -23.86244 1.000 14.08439 ?  162 TRP   A CH2 1 
ATOM   1147 N N   . GLU   A 1 156 ? 4.75918   -21.92685 -27.59890 1.000 12.83870 ?  163 GLU   A N   1 
ATOM   1148 C CA  . GLU   A 1 156 ? 4.80108   -22.79043 -26.40990 1.000 12.18219 ?  163 GLU   A CA  1 
ATOM   1149 C C   . GLU   A 1 156 ? 6.19841   -22.84114 -25.82965 1.000 14.13274 ?  163 GLU   A C   1 
ATOM   1150 O O   . GLU   A 1 156 ? 7.18075   -22.78998 -26.58045 1.000 14.06863 ?  163 GLU   A O   1 
ATOM   1151 C CB  . GLU   A 1 156 ? 4.37760   -24.21531 -26.78991 1.000 15.41548 ?  163 GLU   A CB  1 
ATOM   1152 C CG  . GLU   A 1 156 ? 4.02898   -25.11604 -25.62121 1.000 19.11156 ?  163 GLU   A CG  1 
ATOM   1153 C CD  . GLU   A 1 156 ? 3.41373   -26.37876 -26.13603 1.000 27.17528 ?  163 GLU   A CD  1 
ATOM   1154 O OE1 . GLU   A 1 156 ? 2.21587   -26.61849 -25.79494 1.000 26.22827 ?  163 GLU   A OE1 1 
ATOM   1155 O OE2 . GLU   A 1 156 ? 4.10959   -27.12318 -26.93867 1.000 25.74543 ?  163 GLU   A OE2 1 
ATOM   1156 N N   . SER   A 1 157 ? 6.27415   -22.93093 -24.50171 1.000 13.60343 ?  164 SER   A N   1 
ATOM   1157 C CA  . SER   A 1 157 ? 7.57682   -23.09930 -23.89002 1.000 13.47369 ?  164 SER   A CA  1 
ATOM   1158 C C   . SER   A 1 157 ? 7.41379   -23.80365 -22.56056 1.000 11.66684 ?  164 SER   A C   1 
ATOM   1159 O O   . SER   A 1 157 ? 6.56260   -23.40879 -21.75105 1.000 13.12443 ?  164 SER   A O   1 
ATOM   1160 C CB  . SER   A 1 157 ? 8.29673   -21.75765 -23.71248 1.000 14.40660 ?  164 SER   A CB  1 
ATOM   1161 O OG  . SER   A 1 157 ? 9.58109   -21.98165 -23.10962 1.000 14.01323 ?  164 SER   A OG  1 
ATOM   1162 N N   . SER   A 1 158 ? 8.31503   -24.77145 -22.29555 1.000 13.51425 ?  165 SER   A N   1 
ATOM   1163 C CA  . SER   A 1 158 ? 8.50805   -25.27277 -20.93261 1.000 15.57325 ?  165 SER   A CA  1 
ATOM   1164 C C   . SER   A 1 158 ? 9.74911   -24.67011 -20.28097 1.000 15.64947 ?  165 SER   A C   1 
ATOM   1165 O O   . SER   A 1 158 ? 10.39793  -25.33018 -19.43000 1.000 18.65463 ?  165 SER   A O   1 
ATOM   1166 C CB  . SER   A 1 158 ? 8.61429   -26.79723 -20.96946 1.000 15.47368 ?  165 SER   A CB  1 
ATOM   1167 O OG  . SER   A 1 158 ? 7.39540   -27.30193 -21.50830 1.000 20.88150 ?  165 SER   A OG  1 
ATOM   1168 N N   . ALA   A 1 159 ? 10.13878  -23.45897 -20.70797 1.000 14.94763 ?  166 ALA   A N   1 
ATOM   1169 C CA  . ALA   A 1 159 ? 11.37383  -22.78530 -20.28795 1.000 15.53811 ?  166 ALA   A CA  1 
ATOM   1170 C C   . ALA   A 1 159 ? 12.55931  -23.59885 -20.80832 1.000 18.85369 ?  166 ALA   A C   1 
ATOM   1171 O O   . ALA   A 1 159 ? 12.51027  -24.07087 -21.95179 1.000 21.72744 ?  166 ALA   A O   1 
ATOM   1172 C CB  . ALA   A 1 159 ? 11.34480  -22.56232 -18.76093 1.000 18.39258 ?  166 ALA   A CB  1 
ATOM   1173 N N   . GLY   A 1 160 ? 13.64514  -23.71736 -20.05342 1.000 19.26794 ?  167 GLY   A N   1 
ATOM   1174 C CA  . GLY   A 1 160 ? 14.81817  -24.43151 -20.57363 1.000 20.50120 ?  167 GLY   A CA  1 
ATOM   1175 C C   . GLY   A 1 160 ? 15.46638  -23.78144 -21.78276 1.000 22.71784 ?  167 GLY   A C   1 
ATOM   1176 O O   . GLY   A 1 160 ? 16.27666  -24.42925 -22.46006 1.000 24.50086 ?  167 GLY   A O   1 
ATOM   1177 N N   . GLY   A 1 161 ? 15.14102  -22.51861 -22.04403 1.000 16.70275 ?  168 GLY   A N   1 
ATOM   1178 C CA  . GLY   A 1 161 ? 15.87474  -21.70054 -22.98293 1.000 18.33981 ?  168 GLY   A CA  1 
ATOM   1179 C C   . GLY   A 1 161 ? 15.30336  -21.64057 -24.37783 1.000 17.55025 ?  168 GLY   A C   1 
ATOM   1180 O O   . GLY   A 1 161 ? 15.90240  -20.98998 -25.23071 1.000 18.59905 ?  168 GLY   A O   1 
ATOM   1181 N N   . SER   A 1 162 ? 14.21225  -22.34502 -24.64146 1.000 14.46824 ?  169 SER   A N   1 
ATOM   1182 C CA  . SER   A 1 162 ? 13.64560  -22.34817 -26.00313 1.000 14.08548 ?  169 SER   A CA  1 
ATOM   1183 C C   . SER   A 1 162 ? 12.12198  -22.24797 -25.97049 1.000 15.27101 ?  169 SER   A C   1 
ATOM   1184 O O   . SER   A 1 162 ? 11.48371  -22.53667 -24.95923 1.000 14.71029 ?  169 SER   A O   1 
ATOM   1185 C CB  . SER   A 1 162 ? 14.03888  -23.59665 -26.78417 1.000 16.84365 ?  169 SER   A CB  1 
ATOM   1186 O OG  . SER   A 1 162 ? 13.41105  -24.74041 -26.19025 1.000 16.87116 ?  169 SER   A OG  1 
ATOM   1187 N N   . PHE   A 1 163 ? 11.56153  -21.84118 -27.10839 1.000 15.44314 ?  170 PHE   A N   1 
ATOM   1188 C CA  . PHE   A 1 163 ? 10.12152  -21.80812 -27.29851 1.000 14.02781 ?  170 PHE   A CA  1 
ATOM   1189 C C   . PHE   A 1 163 ? 9.86694   -22.21203 -28.75085 1.000 16.00121 ?  170 PHE   A C   1 
ATOM   1190 O O   . PHE   A 1 163 ? 10.78087  -22.22679 -29.60145 1.000 15.91303 ?  170 PHE   A O   1 
ATOM   1191 C CB  . PHE   A 1 163 ? 9.49718   -20.42770 -27.03249 1.000 14.16113 ?  170 PHE   A CB  1 
ATOM   1192 C CG  . PHE   A 1 163 ? 10.00762  -19.31616 -27.96934 1.000 13.28238 ?  170 PHE   A CG  1 
ATOM   1193 C CD1 . PHE   A 1 163 ? 11.14800  -18.56578 -27.60147 1.000 13.41181 ?  170 PHE   A CD1 1 
ATOM   1194 C CD2 . PHE   A 1 163 ? 9.31558   -18.97798 -29.12542 1.000 15.29861 ?  170 PHE   A CD2 1 
ATOM   1195 C CE1 . PHE   A 1 163 ? 11.57298  -17.51018 -28.44252 1.000 14.37770 ?  170 PHE   A CE1 1 
ATOM   1196 C CE2 . PHE   A 1 163 ? 9.73632   -17.97228 -29.97022 1.000 14.50842 ?  170 PHE   A CE2 1 
ATOM   1197 C CZ  . PHE   A 1 163 ? 10.88536  -17.20000 -29.60386 1.000 13.68186 ?  170 PHE   A CZ  1 
ATOM   1198 N N   . THR   A 1 164 ? 8.65340   -22.66775 -29.00271 1.000 14.57686 ?  171 THR   A N   1 
ATOM   1199 C CA  . THR   A 1 164 ? 8.26739   -23.05233 -30.35662 1.000 14.96854 ?  171 THR   A CA  1 
ATOM   1200 C C   . THR   A 1 164 ? 7.14307   -22.15695 -30.85379 1.000 14.89476 ?  171 THR   A C   1 
ATOM   1201 O O   . THR   A 1 164 ? 6.36754   -21.60965 -30.07180 1.000 15.13825 ?  171 THR   A O   1 
ATOM   1202 C CB  . THR   A 1 164 ? 7.80281   -24.50258 -30.43521 1.000 15.81616 ?  171 THR   A CB  1 
ATOM   1203 O OG1 . THR   A 1 164 ? 6.66494   -24.71682 -29.58931 1.000 16.81208 ?  171 THR   A OG1 1 
ATOM   1204 C CG2 . THR   A 1 164 ? 8.91656   -25.50368 -29.96932 1.000 16.03100 ?  171 THR   A CG2 1 
ATOM   1205 N N   . VAL   A 1 165 ? 7.05353   -22.05191 -32.18669 1.000 15.19889 ?  172 VAL   A N   1 
ATOM   1206 C CA  . VAL   A 1 165 ? 5.91778   -21.35650 -32.78707 1.000 15.62441 ?  172 VAL   A CA  1 
ATOM   1207 C C   . VAL   A 1 165 ? 5.46225   -22.22363 -33.93443 1.000 17.83888 ?  172 VAL   A C   1 
ATOM   1208 O O   . VAL   A 1 165 ? 6.29267   -22.70640 -34.69838 1.000 17.20424 ?  172 VAL   A O   1 
ATOM   1209 C CB  . VAL   A 1 165 ? 6.29961   -19.93480 -33.28070 1.000 15.09974 ?  172 VAL   A CB  1 
ATOM   1210 C CG1 . VAL   A 1 165 ? 5.11008   -19.24503 -34.00437 1.000 15.90634 ?  172 VAL   A CG1 1 
ATOM   1211 C CG2 . VAL   A 1 165 ? 6.81458   -19.02908 -32.13226 1.000 15.83537 ?  172 VAL   A CG2 1 
ATOM   1212 N N   . ARG   A 1 166 ? 4.15304   -22.35873 -34.09977 1.000 16.82805 ?  173 ARG   A N   1 
ATOM   1213 C CA  . ARG   A 1 166 ? 3.58560   -23.09033 -35.22237 1.000 17.95536 ?  173 ARG   A CA  1 
ATOM   1214 C C   . ARG   A 1 166 ? 2.30353   -22.41173 -35.63144 1.000 18.40648 ?  173 ARG   A C   1 
ATOM   1215 O O   . ARG   A 1 166 ? 1.67004   -21.75995 -34.81247 1.000 18.25889 ?  173 ARG   A O   1 
ATOM   1216 C CB  . ARG   A 1 166 ? 3.30448   -24.55888 -34.90180 1.000 19.70946 ?  173 ARG   A CB  1 
ATOM   1217 C CG  . ARG   A 1 166 ? 2.44573   -24.79440 -33.68276 1.000 23.41380 ?  173 ARG   A CG  1 
ATOM   1218 C CD  . ARG   A 1 166 ? 1.89971   -26.21574 -33.60321 1.000 29.47079 ?  173 ARG   A CD  1 
ATOM   1219 N NE  . ARG   A 1 166 ? 1.24539   -26.37913 -32.30189 1.000 35.96799 ?  173 ARG   A NE  1 
ATOM   1220 C CZ  . ARG   A 1 166 ? -0.04388  -26.17220 -32.05912 1.000 48.81589 ?  173 ARG   A CZ  1 
ATOM   1221 N NH1 . ARG   A 1 166 ? -0.88754  -25.87145 -33.02961 1.000 35.57133 ?  173 ARG   A NH1 1 
ATOM   1222 N NH2 . ARG   A 1 166 ? -0.49709  -26.27059 -30.80554 1.000 50.22220 ?  173 ARG   A NH2 1 
ATOM   1223 N N   . THR   A 1 167 ? 1.91865   -22.57266 -36.89700 1.000 19.49029 ?  174 THR   A N   1 
ATOM   1224 C CA  . THR   A 1 167 ? 0.57822   -22.19160 -37.29119 1.000 19.84341 ?  174 THR   A CA  1 
ATOM   1225 C C   . THR   A 1 167 ? -0.38823  -23.15285 -36.63631 1.000 27.40303 ?  174 THR   A C   1 
ATOM   1226 O O   . THR   A 1 167 ? -0.15176  -24.35970 -36.60053 1.000 33.30891 ?  174 THR   A O   1 
ATOM   1227 C CB  . THR   A 1 167 ? 0.45340   -22.21332 -38.83044 1.000 23.17624 ?  174 THR   A CB  1 
ATOM   1228 O OG1 . THR   A 1 167 ? 1.39837   -21.28961 -39.33896 1.000 28.24061 ?  174 THR   A OG1 1 
ATOM   1229 C CG2 . THR   A 1 167 ? -0.88678  -21.75844 -39.22603 1.000 31.26260 ?  174 THR   A CG2 1 
ATOM   1230 N N   . ASP   A 1 168 ? -1.47274  -22.62338 -36.08238 1.000 20.93479 ?  175 ASP   A N   1 
ATOM   1231 C CA  . ASP   A 1 168 ? -2.43433  -23.44322 -35.36996 1.000 20.76210 ?  175 ASP   A CA  1 
ATOM   1232 C C   . ASP   A 1 168 ? -3.64234  -23.70702 -36.25819 1.000 30.07021 ?  175 ASP   A C   1 
ATOM   1233 O O   . ASP   A 1 168 ? -4.35840  -22.76709 -36.62316 1.000 30.13318 ?  175 ASP   A O   1 
ATOM   1234 C CB  . ASP   A 1 168 ? -2.84639  -22.72084 -34.08034 1.000 19.75298 ?  175 ASP   A CB  1 
ATOM   1235 C CG  . ASP   A 1 168 ? -3.80690  -23.53542 -33.26183 1.000 35.71685 ?  175 ASP   A CG  1 
ATOM   1236 O OD1 . ASP   A 1 168 ? -3.67782  -24.76338 -33.28822 1.000 42.61641 ?  175 ASP   A OD1 1 
ATOM   1237 O OD2 . ASP   A 1 168 ? -4.64546  -22.95742 -32.55743 1.000 26.17910 ?  175 ASP   A OD2 1 
ATOM   1238 N N   . THR   A 1 169 ? -3.89170  -24.97388 -36.55156 1.000 33.21514 ?  176 THR   A N   1 
ATOM   1239 C CA  . THR   A 1 169 ? -5.02069  -25.35941 -37.39867 1.000 41.29440 ?  176 THR   A CA  1 
ATOM   1240 C C   . THR   A 1 169 ? -6.17194  -25.89497 -36.56274 1.000 41.92328 ?  176 THR   A C   1 
ATOM   1241 O O   . THR   A 1 169 ? -7.09567  -26.50346 -37.11281 1.000 40.52184 ?  176 THR   A O   1 
ATOM   1242 C CB  . THR   A 1 169 ? -4.60165  -26.41035 -38.44541 1.000 43.55174 ?  176 THR   A CB  1 
ATOM   1243 O OG1 . THR   A 1 169 ? -3.86016  -27.46731 -37.81644 1.000 44.15917 ?  176 THR   A OG1 1 
ATOM   1244 C CG2 . THR   A 1 169 ? -3.68350  -25.74007 -39.44590 1.000 40.66433 ?  176 THR   A CG2 1 
ATOM   1245 N N   . GLY   A 1 170 ? -6.10936  -25.70335 -35.24446 1.000 37.34889 ?  177 GLY   A N   1 
ATOM   1246 C CA  . GLY   A 1 170 ? -7.13039  -26.18473 -34.33876 1.000 49.58055 ?  177 GLY   A CA  1 
ATOM   1247 C C   . GLY   A 1 170 ? -8.28498  -25.22039 -34.20868 1.000 30.74725 ?  177 GLY   A C   1 
ATOM   1248 O O   . GLY   A 1 170 ? -8.61686  -24.46485 -35.13363 1.000 33.89951 ?  177 GLY   A O   1 
ATOM   1249 N N   . GLU   A 1 171 ? -8.93134  -25.27049 -33.05177 1.000 28.35912 ?  178 GLU   A N   1 
ATOM   1250 C CA  . GLU   A 1 171 ? -10.15168 -24.51651 -32.81234 1.000 25.87818 ?  178 GLU   A CA  1 
ATOM   1251 C C   . GLU   A 1 171 ? -9.98409  -23.05772 -33.18332 1.000 28.36761 ?  178 GLU   A C   1 
ATOM   1252 O O   . GLU   A 1 171 ? -9.19652  -22.37518 -32.54828 1.000 22.12618 ?  178 GLU   A O   1 
ATOM   1253 C CB  . GLU   A 1 171 ? -10.51113 -24.61741 -31.33602 1.000 27.63900 ?  178 GLU   A CB  1 
ATOM   1254 C CG  . GLU   A 1 171 ? -11.77435 -23.92672 -30.89405 1.000 36.59147 ?  178 GLU   A CG  1 
ATOM   1255 C CD  . GLU   A 1 171 ? -12.01443 -24.16056 -29.39462 1.000 44.40642 ?  178 GLU   A CD  1 
ATOM   1256 O OE1 . GLU   A 1 171 ? -11.06969 -24.69032 -28.75759 1.000 33.47029 ?  178 GLU   A OE1 1 
ATOM   1257 O OE2 . GLU   A 1 171 ? -13.13103 -23.88456 -28.88158 1.000 40.89951 ?  178 GLU   A OE2 1 
ATOM   1258 N N   . PRO   A 1 172 ? -10.70031 -22.52454 -34.15628 1.000 28.15112 ?  179 PRO   A N   1 
ATOM   1259 C CA  . PRO   A 1 172 ? -10.48721 -21.11386 -34.50309 1.000 26.10598 ?  179 PRO   A CA  1 
ATOM   1260 C C   . PRO   A 1 172 ? -10.90206 -20.17476 -33.37231 1.000 27.41212 ?  179 PRO   A C   1 
ATOM   1261 O O   . PRO   A 1 172 ? -11.91162 -20.38866 -32.70150 1.000 29.56355 ?  179 PRO   A O   1 
ATOM   1262 C CB  . PRO   A 1 172 ? -11.36760 -20.91725 -35.75351 1.000 26.54224 ?  179 PRO   A CB  1 
ATOM   1263 C CG  . PRO   A 1 172 ? -11.51798 -22.32762 -36.30967 1.000 35.97551 ?  179 PRO   A CG  1 
ATOM   1264 C CD  . PRO   A 1 172 ? -11.62828 -23.20341 -35.09817 1.000 31.46571 ?  179 PRO   A CD  1 
ATOM   1265 N N   . MET   A 1 173 ? -10.12468 -19.10567 -33.16906 1.000 23.66633 ?  180 MET   A N   1 
ATOM   1266 C CA  . MET   A 1 173 ? -10.35332 -18.17161 -32.05565 1.000 20.98871 ?  180 MET   A CA  1 
ATOM   1267 C C   . MET   A 1 173 ? -11.06695 -16.84935 -32.38004 1.000 32.97520 ?  180 MET   A C   1 
ATOM   1268 O O   . MET   A 1 173 ? -11.38463 -16.09163 -31.44725 1.000 31.72645 ?  180 MET   A O   1 
ATOM   1269 C CB  . MET   A 1 173 ? -8.99659  -17.82786 -31.46680 1.000 19.77635 ?  180 MET   A CB  1 
ATOM   1270 C CG  . MET   A 1 173 ? -8.65008  -18.72350 -30.33166 1.000 47.16141 ?  180 MET   A CG  1 
ATOM   1271 S SD  . MET   A 1 173 ? -7.10776  -18.02889 -29.87637 1.000 40.56402 ?  180 MET   A SD  1 
ATOM   1272 C CE  . MET   A 1 173 ? -7.67991  -16.54250 -29.08713 1.000 28.94888 ?  180 MET   A CE  1 
ATOM   1273 N N   . GLY   A 1 174 ? -11.23630 -16.49874 -33.62576 1.000 23.18671 ?  181 GLY   A N   1 
ATOM   1274 C CA  . GLY   A 1 174 ? -11.89744 -15.23833 -33.98927 1.000 20.35380 ?  181 GLY   A CA  1 
ATOM   1275 C C   . GLY   A 1 174 ? -10.88814 -14.10005 -33.95114 1.000 20.43804 ?  181 GLY   A C   1 
ATOM   1276 O O   . GLY   A 1 174 ? -10.40048 -13.59785 -34.98597 1.000 20.55315 ?  181 GLY   A O   1 
ATOM   1277 N N   . ARG   A 1 175 ? -10.51209 -13.75106 -32.72356 1.000 17.58384 ?  182 ARG   A N   1 
ATOM   1278 C CA  . ARG   A 1 175 ? -9.51277  -12.73155 -32.46844 1.000 16.70267 ?  182 ARG   A CA  1 
ATOM   1279 C C   . ARG   A 1 175 ? -9.18184  -12.76858 -30.98624 1.000 17.25984 ?  182 ARG   A C   1 
ATOM   1280 O O   . ARG   A 1 175 ? -10.09841 -12.88287 -30.17773 1.000 16.37305 ?  182 ARG   A O   1 
ATOM   1281 C CB  . ARG   A 1 175 ? -10.04107 -11.32749 -32.84391 1.000 16.65433 ?  182 ARG   A CB  1 
ATOM   1282 C CG  . ARG   A 1 175 ? -8.89063  -10.24018 -32.68551 1.000 15.96338 ?  182 ARG   A CG  1 
ATOM   1283 C CD  . ARG   A 1 175 ? -9.48765  -8.78022  -32.55033 1.000 16.71044 ?  182 ARG   A CD  1 
ATOM   1284 N NE  . ARG   A 1 175 ? -10.39261 -8.69829  -31.38443 1.000 15.60736 ?  182 ARG   A NE  1 
ATOM   1285 C CZ  . ARG   A 1 175 ? -11.71937 -8.62688  -31.47779 1.000 16.03373 ?  182 ARG   A CZ  1 
ATOM   1286 N NH1 . ARG   A 1 175 ? -12.36371 -8.63202  -32.64773 1.000 16.76668 ?  182 ARG   A NH1 1 
ATOM   1287 N NH2 . ARG   A 1 175 ? -12.43253 -8.53721  -30.37090 1.000 17.19030 ?  182 ARG   A NH2 1 
ATOM   1288 N N   . GLY   A 1 176 ? -7.89312  -12.63740 -30.64308 1.000 16.13446 ?  183 GLY   A N   1 
ATOM   1289 C CA  . GLY   A 1 176 ? -7.49891  -12.48263 -29.23946 1.000 14.66592 ?  183 GLY   A CA  1 
ATOM   1290 C C   . GLY   A 1 176 ? -6.40983  -13.45769 -28.85977 1.000 14.41114 ?  183 GLY   A C   1 
ATOM   1291 O O   . GLY   A 1 176 ? -5.67951  -13.97789 -29.71867 1.000 16.58498 ?  183 GLY   A O   1 
ATOM   1292 N N   . THR   A 1 177 ? -6.30216  -13.72263 -27.55629 1.000 12.76590 ?  184 THR   A N   1 
ATOM   1293 C CA  . THR   A 1 177 ? -5.22658  -14.57300 -27.07460 1.000 12.18697 ?  184 THR   A CA  1 
ATOM   1294 C C   . THR   A 1 177 ? -5.70857  -15.51823 -26.01103 1.000 17.04104 ?  184 THR   A C   1 
ATOM   1295 O O   . THR   A 1 177 ? -6.55553  -15.13962 -25.18544 1.000 14.17997 ?  184 THR   A O   1 
ATOM   1296 C CB  . THR   A 1 177 ? -4.10240  -13.67359 -26.50800 1.000 13.64517 ?  184 THR   A CB  1 
ATOM   1297 O OG1 . THR   A 1 177 ? -3.56816  -12.93062 -27.58493 1.000 16.61817 ?  184 THR   A OG1 1 
ATOM   1298 C CG2 . THR   A 1 177 ? -2.97747  -14.51492 -25.78894 1.000 16.01913 ?  184 THR   A CG2 1 
ATOM   1299 N N   . LYS   A 1 178 ? -5.17480  -16.74369 -26.03599 1.000 13.00876 ?  185 LYS   A N   1 
ATOM   1300 C CA  . LYS   A 1 178 ? -5.55568  -17.74194 -25.02934 1.000 13.93787 ?  185 LYS   A CA  1 
ATOM   1301 C C   . LYS   A 1 178 ? -4.25613  -18.22686 -24.41568 1.000 15.36318 ?  185 LYS   A C   1 
ATOM   1302 O O   . LYS   A 1 178 ? -3.40341  -18.71445 -25.15476 1.000 15.17809 ?  185 LYS   A O   1 
ATOM   1303 C CB  . LYS   A 1 178 ? -6.32781  -18.88036 -25.73436 1.000 15.05563 ?  185 LYS   A CB  1 
ATOM   1304 C CG  . LYS   A 1 178 ? -6.33965  -20.14872 -25.05300 1.000 21.08686 ?  185 LYS   A CG  1 
ATOM   1305 C CD  . LYS   A 1 178 ? -7.41837  -21.11407 -25.68244 1.000 27.42231 ?  185 LYS   A CD  1 
ATOM   1306 C CE  . LYS   A 1 178 ? -7.37340  -21.16057 -27.19626 1.000 29.55857 ?  185 LYS   A CE  1 
ATOM   1307 N NZ  . LYS   A 1 178 ? -8.48466  -22.05771 -27.76705 1.000 35.26047 ?  185 LYS   A NZ  1 
ATOM   1308 N N   . VAL   A 1 179 ? -4.08229  -18.04585 -23.10872 1.000 12.13868 ?  186 VAL   A N   1 
ATOM   1309 C CA  . VAL   A 1 179 ? -2.89202  -18.49102 -22.38971 1.000 10.98402 ?  186 VAL   A CA  1 
ATOM   1310 C C   . VAL   A 1 179 ? -3.30315  -19.74489 -21.63106 1.000 16.48220 ?  186 VAL   A C   1 
ATOM   1311 O O   . VAL   A 1 179 ? -4.15854  -19.68622 -20.73392 1.000 15.53377 ?  186 VAL   A O   1 
ATOM   1312 C CB  . VAL   A 1 179 ? -2.36212  -17.41454 -21.42561 1.000 9.67054  ?  186 VAL   A CB  1 
ATOM   1313 C CG1 . VAL   A 1 179 ? -1.17419  -17.96974 -20.59870 1.000 13.04915 ?  186 VAL   A CG1 1 
ATOM   1314 C CG2 . VAL   A 1 179 ? -1.95494  -16.17037 -22.19495 1.000 12.99659 ?  186 VAL   A CG2 1 
ATOM   1315 N N   . ILE   A 1 180 ? -2.72469  -20.87135 -21.99527 1.000 12.48637 ?  187 ILE   A N   1 
ATOM   1316 C CA  . ILE   A 1 180 ? -3.04369  -22.16062 -21.38977 1.000 11.53138 ?  187 ILE   A CA  1 
ATOM   1317 C C   . ILE   A 1 180 ? -1.89527  -22.47331 -20.43147 1.000 12.13624 ?  187 ILE   A C   1 
ATOM   1318 O O   . ILE   A 1 180 ? -0.76216  -22.70112 -20.85845 1.000 14.06641 ?  187 ILE   A O   1 
ATOM   1319 C CB  . ILE   A 1 180 ? -3.21003  -23.26007 -22.44774 1.000 13.00724 ?  187 ILE   A CB  1 
ATOM   1320 C CG1 . ILE   A 1 180 ? -4.24107  -22.81303 -23.48072 1.000 12.68860 ?  187 ILE   A CG1 1 
ATOM   1321 C CG2 . ILE   A 1 180 ? -3.59173  -24.58978 -21.71181 1.000 17.23871 ?  187 ILE   A CG2 1 
ATOM   1322 C CD1 . ILE   A 1 180 ? -4.32747  -23.74140 -24.66715 1.000 18.32098 ?  187 ILE   A CD1 1 
ATOM   1323 N N   . LEU   A 1 181 ? -2.17551  -22.46651 -19.12534 1.000 10.90959 ?  188 LEU   A N   1 
ATOM   1324 C CA  . LEU   A 1 181 ? -1.18829  -22.74790 -18.08914 1.000 12.69475 ?  188 LEU   A CA  1 
ATOM   1325 C C   . LEU   A 1 181 ? -1.26794  -24.21144 -17.74108 1.000 15.63284 ?  188 LEU   A C   1 
ATOM   1326 O O   . LEU   A 1 181 ? -2.27194  -24.65912 -17.16752 1.000 15.32651 ?  188 LEU   A O   1 
ATOM   1327 C CB  . LEU   A 1 181 ? -1.46578  -21.89099 -16.83725 1.000 12.26917 ?  188 LEU   A CB  1 
ATOM   1328 C CG  . LEU   A 1 181 ? -1.50721  -20.39200 -17.12036 1.000 12.56934 ?  188 LEU   A CG  1 
ATOM   1329 C CD1 . LEU   A 1 181 ? -1.82184  -19.76049 -15.74321 1.000 16.19482 ?  188 LEU   A CD1 1 
ATOM   1330 C CD2 . LEU   A 1 181 ? -0.18626  -19.89826 -17.61088 1.000 16.92136 ?  188 LEU   A CD2 1 
ATOM   1331 N N   . HIS   A 1 182 ? -0.22234  -24.98642 -18.08466 1.000 14.60386 ?  189 HIS   A N   1 
ATOM   1332 C CA  . HIS   A 1 182 ? -0.12955  -26.39325 -17.67042 1.000 16.00028 ?  189 HIS   A CA  1 
ATOM   1333 C C   . HIS   A 1 182 ? 0.48698   -26.35850 -16.28121 1.000 16.13640 ?  189 HIS   A C   1 
ATOM   1334 O O   . HIS   A 1 182 ? 1.69339   -26.17817 -16.13559 1.000 16.18389 ?  189 HIS   A O   1 
ATOM   1335 C CB  . HIS   A 1 182 ? 0.72939   -27.17933 -18.67395 1.000 15.62981 ?  189 HIS   A CB  1 
ATOM   1336 C CG  . HIS   A 1 182 ? 0.19379   -27.12201 -20.09233 1.000 20.14250 ?  189 HIS   A CG  1 
ATOM   1337 N ND1 . HIS   A 1 182 ? -0.67628  -28.07490 -20.59547 1.000 27.48427 ?  189 HIS   A ND1 1 
ATOM   1338 C CD2 . HIS   A 1 182 ? 0.31417   -26.17280 -21.06696 1.000 22.67404 ?  189 HIS   A CD2 1 
ATOM   1339 C CE1 . HIS   A 1 182 ? -0.99721  -27.76124 -21.84304 1.000 20.66627 ?  189 HIS   A CE1 1 
ATOM   1340 N NE2 . HIS   A 1 182 ? -0.40652  -26.60955 -22.15062 1.000 26.25223 ?  189 HIS   A NE2 1 
ATOM   1341 N N   . LEU   A 1 183 ? -0.34809  -26.52452 -15.25040 1.000 14.55128 ?  190 LEU   A N   1 
ATOM   1342 C CA  . LEU   A 1 183 ? 0.13716   -26.21543 -13.89476 1.000 14.43150 ?  190 LEU   A CA  1 
ATOM   1343 C C   . LEU   A 1 183 ? 1.09845   -27.24946 -13.36332 1.000 17.59384 ?  190 LEU   A C   1 
ATOM   1344 O O   . LEU   A 1 183 ? 0.99756   -28.44671 -13.64515 1.000 19.07775 ?  190 LEU   A O   1 
ATOM   1345 C CB  . LEU   A 1 183 ? -1.05130  -26.13041 -12.93995 1.000 15.19263 ?  190 LEU   A CB  1 
ATOM   1346 C CG  . LEU   A 1 183 ? -1.99057  -24.95816 -13.27225 1.000 15.16835 ?  190 LEU   A CG  1 
ATOM   1347 C CD1 . LEU   A 1 183 ? -3.17547  -24.96067 -12.24848 1.000 17.03999 ?  190 LEU   A CD1 1 
ATOM   1348 C CD2 . LEU   A 1 183 ? -1.29094  -23.61849 -13.16916 1.000 18.90334 ?  190 LEU   A CD2 1 
ATOM   1349 N N   . LYS   A 1 184 ? 2.01998   -26.77752 -12.51636 1.000 18.00749 ?  191 LYS   A N   1 
ATOM   1350 C CA  . LYS   A 1 184 ? 2.84710   -27.69782 -11.74324 1.000 18.18175 ?  191 LYS   A CA  1 
ATOM   1351 C C   . LYS   A 1 184 ? 1.99119   -28.53862 -10.77978 1.000 18.98053 ?  191 LYS   A C   1 
ATOM   1352 O O   . LYS   A 1 184 ? 0.92681   -28.09872 -10.34383 1.000 21.37627 ?  191 LYS   A O   1 
ATOM   1353 C CB  . LYS   A 1 184 ? 3.87453   -26.89848 -10.92844 1.000 21.68879 ?  191 LYS   A CB  1 
ATOM   1354 C CG  . LYS   A 1 184 ? 4.96075   -26.15281 -11.79681 1.000 21.16367 ?  191 LYS   A CG  1 
ATOM   1355 C CD  . LYS   A 1 184 ? 5.58111   -25.03811 -10.88951 1.000 26.95235 ?  191 LYS   A CD  1 
ATOM   1356 C CE  . LYS   A 1 184 ? 6.60583   -24.10095 -11.55326 1.000 43.44464 ?  191 LYS   A CE  1 
ATOM   1357 N NZ  . LYS   A 1 184 ? 7.20243   -22.89881 -10.70852 1.000 35.63979 ?  191 LYS   A NZ  1 
ATOM   1358 N N   . GLU   A 1 185 ? 2.46893   -29.74969 -10.43212 1.000 23.71069 ?  192 GLU   A N   1 
ATOM   1359 C CA  . GLU   A 1 185 ? 1.60718   -30.68067 -9.69389  1.000 27.82957 ?  192 GLU   A CA  1 
ATOM   1360 C C   . GLU   A 1 185 ? 1.22425   -30.12776 -8.33600  1.000 28.46007 ?  192 GLU   A C   1 
ATOM   1361 O O   . GLU   A 1 185 ? 0.16108   -30.47100 -7.80764  1.000 29.68620 ?  192 GLU   A O   1 
ATOM   1362 C CB  . GLU   A 1 185 ? 2.25703   -32.06714 -9.52925  1.000 32.27058 ?  192 GLU   A CB  1 
ATOM   1363 C CG  . GLU   A 1 185 ? 3.71665   -32.06537 -9.14972  1.000 50.13317 ?  192 GLU   A CG  1 
ATOM   1364 C CD  . GLU   A 1 185 ? 4.25183   -33.48165 -8.89898  1.000 70.47193 ?  192 GLU   A CD  1 
ATOM   1365 O OE1 . GLU   A 1 185 ? 5.47065   -33.63397 -8.65323  1.000 74.28426 ?  192 GLU   A OE1 1 
ATOM   1366 O OE2 . GLU   A 1 185 ? 3.44975   -34.44329 -8.95298  1.000 71.23172 ?  192 GLU   A OE2 1 
ATOM   1367 N N   . ASP   A 1 186 ? 2.04381   -29.24473 -7.77453  1.000 23.19848 ?  193 ASP   A N   1 
ATOM   1368 C CA  . ASP   A 1 186 ? 1.75430   -28.72658 -6.45197  1.000 21.08657 ?  193 ASP   A CA  1 
ATOM   1369 C C   . ASP   A 1 186 ? 1.05974   -27.37219 -6.48159  1.000 20.76986 ?  193 ASP   A C   1 
ATOM   1370 O O   . ASP   A 1 186 ? 0.89320   -26.75665 -5.42159  1.000 21.61212 ?  193 ASP   A O   1 
ATOM   1371 C CB  . ASP   A 1 186 ? 3.03684   -28.67360 -5.61159  1.000 27.05881 ?  193 ASP   A CB  1 
ATOM   1372 C CG  . ASP   A 1 186 ? 4.04461   -27.69637 -6.13784  1.000 29.23520 ?  193 ASP   A CG  1 
ATOM   1373 O OD1 . ASP   A 1 186 ? 3.98526   -27.28470 -7.32388  1.000 34.78660 ?  193 ASP   A OD1 1 
ATOM   1374 O OD2 . ASP   A 1 186 ? 4.95065   -27.36416 -5.36194  1.000 42.29453 ?  193 ASP   A OD2 1 
ATOM   1375 N N   . GLN   A 1 187 ? 0.57744   -26.93416 -7.64801  1.000 17.72209 ?  194 GLN   A N   1 
ATOM   1376 C CA  . GLN   A 1 187 ? -0.07561  -25.64326 -7.82416  1.000 17.07045 ?  194 GLN   A CA  1 
ATOM   1377 C C   . GLN   A 1 187 ? -1.52427  -25.82520 -8.26097  1.000 15.64761 ?  194 GLN   A C   1 
ATOM   1378 O O   . GLN   A 1 187 ? -2.09769  -24.92825 -8.87052  1.000 16.39497 ?  194 GLN   A O   1 
ATOM   1379 C CB  . GLN   A 1 187 ? 0.68503   -24.76813 -8.83700  1.000 15.77718 ?  194 GLN   A CB  1 
ATOM   1380 C CG  . GLN   A 1 187 ? 2.12540   -24.51357 -8.34742  1.000 16.98973 ?  194 GLN   A CG  1 
ATOM   1381 C CD  . GLN   A 1 187 ? 2.20211   -23.84937 -6.96758  1.000 19.69657 ?  194 GLN   A CD  1 
ATOM   1382 O OE1 . GLN   A 1 187 ? 1.39809   -22.96750 -6.65759  1.000 21.99305 ?  194 GLN   A OE1 1 
ATOM   1383 N NE2 . GLN   A 1 187 ? 3.23059   -24.20175 -6.17081  1.000 22.42357 ?  194 GLN   A NE2 1 
ATOM   1384 N N   . THR   A 1 188 ? -2.12701  -26.95515 -7.93088  1.000 21.13878 ?  195 THR   A N   1 
ATOM   1385 C CA  . THR   A 1 188 ? -3.49130  -27.14020 -8.42446  1.000 20.75927 ?  195 THR   A CA  1 
ATOM   1386 C C   . THR   A 1 188 ? -4.54767  -26.36304 -7.63965  1.000 20.95707 ?  195 THR   A C   1 
ATOM   1387 O O   . THR   A 1 188 ? -5.73332  -26.43565 -8.00667  1.000 19.52572 ?  195 THR   A O   1 
ATOM   1388 C CB  . THR   A 1 188 ? -3.86621  -28.62487 -8.43120  1.000 21.93870 ?  195 THR   A CB  1 
ATOM   1389 O OG1 . THR   A 1 188 ? -3.82016  -29.17024 -7.11532  1.000 26.59355 ?  195 THR   A OG1 1 
ATOM   1390 C CG2 . THR   A 1 188 ? -2.91779  -29.40376 -9.39083  1.000 24.72676 ?  195 THR   A CG2 1 
ATOM   1391 N N   . GLU   A 1 189 ? -4.17054  -25.64426 -6.56832  1.000 19.11056 ?  196 GLU   A N   1 
ATOM   1392 C CA  . GLU   A 1 189 ? -5.11702  -24.75015 -5.92307  1.000 19.34016 ?  196 GLU   A CA  1 
ATOM   1393 C C   . GLU   A 1 189 ? -5.67850  -23.74080 -6.88887  1.000 20.15836 ?  196 GLU   A C   1 
ATOM   1394 O O   . GLU   A 1 189 ? -6.79130  -23.27090 -6.67466  1.000 18.16063 ?  196 GLU   A O   1 
ATOM   1395 C CB  . GLU   A 1 189 ? -4.47816  -24.01943 -4.72305  1.000 17.78969 ?  196 GLU   A CB  1 
ATOM   1396 C CG  . GLU   A 1 189 ? -3.45589  -22.99374 -5.11529  1.000 19.05786 ?  196 GLU   A CG  1 
ATOM   1397 C CD  . GLU   A 1 189 ? -2.68720  -22.50466 -3.90541  1.000 22.53010 ?  196 GLU   A CD  1 
ATOM   1398 O OE1 . GLU   A 1 189 ? -1.80383  -23.26986 -3.44991  1.000 25.68204 ?  196 GLU   A OE1 1 
ATOM   1399 O OE2 . GLU   A 1 189 ? -3.03510  -21.42109 -3.36986  1.000 23.11952 ?  196 GLU   A OE2 1 
ATOM   1400 N N   . TYR   A 1 190 ? -4.95081  -23.41391 -7.96009  1.000 16.46272 ?  197 TYR   A N   1 
ATOM   1401 C CA  . TYR   A 1 190 ? -5.41859  -22.39347 -8.89669  1.000 14.20082 ?  197 TYR   A CA  1 
ATOM   1402 C C   . TYR   A 1 190 ? -6.42426  -22.94373 -9.89670  1.000 16.62651 ?  197 TYR   A C   1 
ATOM   1403 O O   . TYR   A 1 190 ? -6.80502  -22.19926 -10.82792 1.000 18.15693 ?  197 TYR   A O   1 
ATOM   1404 C CB  . TYR   A 1 190 ? -4.19081  -21.74814 -9.59836  1.000 15.64260 ?  197 TYR   A CB  1 
ATOM   1405 C CG  . TYR   A 1 190 ? -3.27941  -21.11539 -8.56288  1.000 15.11031 ?  197 TYR   A CG  1 
ATOM   1406 C CD1 . TYR   A 1 190 ? -3.71045  -20.00573 -7.83617  1.000 16.61765 ?  197 TYR   A CD1 1 
ATOM   1407 C CD2 . TYR   A 1 190 ? -2.05255  -21.68142 -8.24069  1.000 15.46114 ?  197 TYR   A CD2 1 
ATOM   1408 C CE1 . TYR   A 1 190 ? -2.92799  -19.45118 -6.86666  1.000 15.47051 ?  197 TYR   A CE1 1 
ATOM   1409 C CE2 . TYR   A 1 190 ? -1.23425  -21.12358 -7.25365  1.000 18.25402 ?  197 TYR   A CE2 1 
ATOM   1410 C CZ  . TYR   A 1 190 ? -1.72543  -19.99424 -6.54161  1.000 16.70023 ?  197 TYR   A CZ  1 
ATOM   1411 O OH  . TYR   A 1 190 ? -0.96233  -19.41475 -5.56752  1.000 18.88572 ?  197 TYR   A OH  1 
ATOM   1412 N N   . LEU   A 1 191 ? -6.85950  -24.20962 -9.72335  1.000 16.96306 ?  198 LEU   A N   1 
ATOM   1413 C CA  . LEU   A 1 191 ? -8.01284  -24.74182 -10.45544 1.000 15.70437 ?  198 LEU   A CA  1 
ATOM   1414 C C   . LEU   A 1 191 ? -9.28967  -24.67327 -9.63215  1.000 19.42688 ?  198 LEU   A C   1 
ATOM   1415 O O   . LEU   A 1 191 ? -10.34299 -25.11913 -10.11462 1.000 20.24447 ?  198 LEU   A O   1 
ATOM   1416 C CB  . LEU   A 1 191 ? -7.77574  -26.20105 -10.84611 1.000 16.41902 ?  198 LEU   A CB  1 
ATOM   1417 C CG  . LEU   A 1 191 ? -6.54740  -26.31140 -11.71453 1.000 17.01970 ?  198 LEU   A CG  1 
ATOM   1418 C CD1 . LEU   A 1 191 ? -6.25954  -27.78587 -12.05810 1.000 21.47871 ?  198 LEU   A CD1 1 
ATOM   1419 C CD2 . LEU   A 1 191 ? -6.71972  -25.44807 -12.99527 1.000 20.44381 ?  198 LEU   A CD2 1 
ATOM   1420 N N   . GLU   A 1 192 ? -9.18835  -24.31455 -8.34696  1.000 15.13698 ?  199 GLU   A N   1 
ATOM   1421 C CA  . GLU   A 1 192 ? -10.34113 -24.34513 -7.44842  1.000 17.53088 ?  199 GLU   A CA  1 
ATOM   1422 C C   . GLU   A 1 192 ? -11.12856 -23.04366 -7.54459  1.000 19.96515 ?  199 GLU   A C   1 
ATOM   1423 O O   . GLU   A 1 192 ? -10.53406 -21.95061 -7.50509  1.000 19.01522 ?  199 GLU   A O   1 
ATOM   1424 C CB  . GLU   A 1 192 ? -9.89382  -24.59619 -6.01057  1.000 21.05969 ?  199 GLU   A CB  1 
ATOM   1425 C CG  . GLU   A 1 192 ? -9.21398  -25.95822 -5.88406  1.000 24.55127 ?  199 GLU   A CG  1 
ATOM   1426 C CD  . GLU   A 1 192 ? -8.51352  -26.18943 -4.53814  1.000 49.76834 ?  199 GLU   A CD  1 
ATOM   1427 O OE1 . GLU   A 1 192 ? -7.68038  -27.12553 -4.46060  1.000 50.30353 ?  199 GLU   A OE1 1 
ATOM   1428 O OE2 . GLU   A 1 192 ? -8.77959  -25.43841 -3.57118  1.000 55.85325 ?  199 GLU   A OE2 1 
ATOM   1429 N N   . GLU   A 1 193 ? -12.44326 -23.17169 -7.76728  1.000 20.21416 ?  200 GLU   A N   1 
ATOM   1430 C CA  . GLU   A 1 193 ? -13.30929 -21.99904 -7.94728  1.000 18.21449 ?  200 GLU   A CA  1 
ATOM   1431 C C   . GLU   A 1 193 ? -13.09674 -20.97087 -6.83379  1.000 18.06321 ?  200 GLU   A C   1 
ATOM   1432 O O   . GLU   A 1 193 ? -12.90708 -19.77829 -7.10055  1.000 17.94538 ?  200 GLU   A O   1 
ATOM   1433 C CB  . GLU   A 1 193 ? -14.80608 -22.41622 -7.98464  1.000 21.01187 ?  200 GLU   A CB  1 
ATOM   1434 C CG  . GLU   A 1 193 ? -15.65630 -21.28053 -8.54663  1.000 25.64127 ?  200 GLU   A CG  1 
ATOM   1435 C CD  . GLU   A 1 193 ? -17.15704 -21.51254 -8.45209  1.000 39.95896 ?  200 GLU   A CD  1 
ATOM   1436 O OE1 . GLU   A 1 193 ? -17.58339 -22.55692 -7.90590  1.000 34.15288 ?  200 GLU   A OE1 1 
ATOM   1437 O OE2 . GLU   A 1 193 ? -17.90089 -20.64297 -8.97446  1.000 38.48882 ?  200 GLU   A OE2 1 
ATOM   1438 N N   . ARG   A 1 194 ? -13.18283 -21.40626 -5.58033  1.000 21.61792 ?  201 ARG   A N   1 
ATOM   1439 C CA  . ARG   A 1 194 ? -13.11987 -20.40713 -4.50674  1.000 20.05561 ?  201 ARG   A CA  1 
ATOM   1440 C C   . ARG   A 1 194 ? -11.78418 -19.69726 -4.50048  1.000 20.22663 ?  201 ARG   A C   1 
ATOM   1441 O O   . ARG   A 1 194 ? -11.71483 -18.51313 -4.15648  1.000 19.00697 ?  201 ARG   A O   1 
ATOM   1442 C CB  . ARG   A 1 194 ? -13.42946 -21.03825 -3.13472  1.000 24.38082 ?  201 ARG   A CB  1 
ATOM   1443 C CG  . ARG   A 1 194 ? -12.34668 -21.88299 -2.61462  1.000 29.28748 ?  201 ARG   A CG  1 
ATOM   1444 C CD  . ARG   A 1 194 ? -12.94489 -22.66827 -1.40772  1.000 33.58571 ?  201 ARG   A CD  1 
ATOM   1445 N NE  . ARG   A 1 194 ? -11.95519 -23.52158 -0.79358  1.000 41.60779 ?  201 ARG   A NE  1 
ATOM   1446 C CZ  . ARG   A 1 194 ? -12.08867 -23.99979 0.43579   1.000 32.59877 ?  201 ARG   A CZ  1 
ATOM   1447 N NH1 . ARG   A 1 194 ? -13.15139 -23.70559 1.17293   1.000 37.94772 ?  201 ARG   A NH1 1 
ATOM   1448 N NH2 . ARG   A 1 194 ? -11.14487 -24.80017 0.91699   1.000 45.87335 ?  201 ARG   A NH2 1 
ATOM   1449 N N   . ARG   A 1 195 ? -10.70453 -20.40955 -4.85230  1.000 18.05239 ?  202 ARG   A N   1 
ATOM   1450 C CA  . ARG   A 1 195 ? -9.38686  -19.79894 -4.85736  1.000 16.99613 ?  202 ARG   A CA  1 
ATOM   1451 C C   . ARG   A 1 195 ? -9.27501  -18.79052 -5.99519  1.000 17.41662 ?  202 ARG   A C   1 
ATOM   1452 O O   . ARG   A 1 195 ? -8.71212  -17.69719 -5.80652  1.000 14.75065 ?  202 ARG   A O   1 
ATOM   1453 C CB  . ARG   A 1 195 ? -8.29725  -20.87682 -5.00887  1.000 17.57218 ?  202 ARG   A CB  1 
ATOM   1454 C CG  . ARG   A 1 195 ? -6.86820  -20.32586 -4.95899  1.000 18.30016 ?  202 ARG   A CG  1 
ATOM   1455 C CD  . ARG   A 1 195 ? -6.51677  -19.77244 -3.57225  1.000 18.84347 ?  202 ARG   A CD  1 
ATOM   1456 N NE  . ARG   A 1 195 ? -5.07111  -19.52523 -3.49996  1.000 17.76917 ?  202 ARG   A NE  1 
ATOM   1457 C CZ  . ARG   A 1 195 ? -4.47107  -18.34863 -3.31911  1.000 19.66448 ?  202 ARG   A CZ  1 
ATOM   1458 N NH1 . ARG   A 1 195 ? -5.15483  -17.24959 -3.06595  1.000 19.75305 ?  202 ARG   A NH1 1 
ATOM   1459 N NH2 . ARG   A 1 195 ? -3.13632  -18.28306 -3.39962  1.000 17.56797 ?  202 ARG   A NH2 1 
ATOM   1460 N N   . ILE   A 1 196 ? -9.78571  -19.14709 -7.20181  1.000 15.20382 ?  203 ILE   A N   1 
ATOM   1461 C CA  . ILE   A 1 196 ? -9.70384  -18.20618 -8.30770  1.000 12.51495 ?  203 ILE   A CA  1 
ATOM   1462 C C   . ILE   A 1 196 ? -10.54136 -16.97950 -8.00685  1.000 14.07231 ?  203 ILE   A C   1 
ATOM   1463 O O   . ILE   A 1 196 ? -10.09439 -15.85278 -8.26275  1.000 14.84654 ?  203 ILE   A O   1 
ATOM   1464 C CB  . ILE   A 1 196 ? -10.13500 -18.88237 -9.61977  1.000 13.04770 ?  203 ILE   A CB  1 
ATOM   1465 C CG1 . ILE   A 1 196 ? -9.19339  -20.04338 -9.92396  1.000 16.18137 ?  203 ILE   A CG1 1 
ATOM   1466 C CG2 . ILE   A 1 196 ? -10.16445 -17.86950 -10.77132 1.000 14.17682 ?  203 ILE   A CG2 1 
ATOM   1467 C CD1 . ILE   A 1 196 ? -9.79548  -21.03355 -10.94108 1.000 18.47563 ?  203 ILE   A CD1 1 
ATOM   1468 N N   . LYS   A 1 197 ? -11.76135 -17.18170 -7.48728  1.000 15.52051 ?  204 LYS   A N   1 
ATOM   1469 C CA  . LYS   A 1 197 ? -12.61999 -16.04856 -7.16043  1.000 15.85048 ?  204 LYS   A CA  1 
ATOM   1470 C C   . LYS   A 1 197 ? -11.92229 -15.11127 -6.18832  1.000 18.56505 ?  204 LYS   A C   1 
ATOM   1471 O O   . LYS   A 1 197 ? -11.99861 -13.88229 -6.33928  1.000 17.90344 ?  204 LYS   A O   1 
ATOM   1472 C CB  . LYS   A 1 197 ? -13.95242 -16.51508 -6.55765  1.000 17.18811 ?  204 LYS   A CB  1 
ATOM   1473 C CG  . LYS   A 1 197 ? -14.92328 -17.14458 -7.52175  1.000 26.04949 ?  204 LYS   A CG  1 
ATOM   1474 C CD  . LYS   A 1 197 ? -16.10368 -17.64309 -6.67264  1.000 24.64165 ?  204 LYS   A CD  1 
ATOM   1475 C CE  . LYS   A 1 197 ? -17.37168 -17.87016 -7.48150  1.000 36.39504 ?  204 LYS   A CE  1 
ATOM   1476 N NZ  . LYS   A 1 197 ? -18.36006 -18.69331 -6.63723  1.000 47.44057 ?  204 LYS   A NZ  1 
ATOM   1477 N N   . GLU   A 1 198 ? -11.28789 -15.67957 -5.14703  1.000 15.99714 ?  205 GLU   A N   1 
ATOM   1478 C CA  . GLU   A 1 198 ? -10.56092 -14.86966 -4.17280  1.000 15.40341 ?  205 GLU   A CA  1 
ATOM   1479 C C   . GLU   A 1 198 ? -9.48070  -14.02351 -4.83819  1.000 14.18797 ?  205 GLU   A C   1 
ATOM   1480 O O   . GLU   A 1 198 ? -9.33745  -12.83764 -4.50441  1.000 16.57504 ?  205 GLU   A O   1 
ATOM   1481 C CB  . GLU   A 1 198 ? -9.93514  -15.79127 -3.11849  1.000 16.06235 ?  205 GLU   A CB  1 
ATOM   1482 C CG  . GLU   A 1 198 ? -9.06501  -15.05361 -2.09449  1.000 18.94596 ?  205 GLU   A CG  1 
ATOM   1483 C CD  . GLU   A 1 198 ? -8.34100  -16.01730 -1.19799  1.000 19.77026 ?  205 GLU   A CD  1 
ATOM   1484 O OE1 . GLU   A 1 198 ? -7.76174  -17.00777 -1.74233  1.000 19.28038 ?  205 GLU   A OE1 1 
ATOM   1485 O OE2 . GLU   A 1 198 ? -8.33628  -15.77885 0.01966   1.000 19.32306 ?  205 GLU   A OE2 1 
ATOM   1486 N N   . ILE   A 1 199 ? -8.70554  -14.61632 -5.75071  1.000 13.46153 ?  206 ILE   A N   1 
ATOM   1487 C CA  . ILE   A 1 199 ? -7.60919  -13.85955 -6.34705  1.000 15.39840 ?  206 ILE   A CA  1 
ATOM   1488 C C   . ILE   A 1 199 ? -8.14267  -12.76115 -7.26181  1.000 15.39264 ?  206 ILE   A C   1 
ATOM   1489 O O   . ILE   A 1 199 ? -7.58313  -11.66531 -7.30767  1.000 17.37687 ?  206 ILE   A O   1 
ATOM   1490 C CB  . ILE   A 1 199 ? -6.68117  -14.82965 -7.11159  1.000 16.76251 ?  206 ILE   A CB  1 
ATOM   1491 C CG1 . ILE   A 1 199 ? -6.06571  -15.82630 -6.11006  1.000 16.15373 ?  206 ILE   A CG1 1 
ATOM   1492 C CG2 . ILE   A 1 199 ? -5.68543  -14.08612 -7.97128  1.000 18.13543 ?  206 ILE   A CG2 1 
ATOM   1493 C CD1 . ILE   A 1 199 ? -5.57917  -17.04404 -6.88378  1.000 18.39917 ?  206 ILE   A CD1 1 
ATOM   1494 N N   . VAL   A 1 200 ? -9.19299  -13.05163 -8.04666  1.000 13.49885 ?  207 VAL   A N   1 
ATOM   1495 C CA  . VAL   A 1 200 ? -9.74159  -12.03402 -8.92342  1.000 13.79624 ?  207 VAL   A CA  1 
ATOM   1496 C C   . VAL   A 1 200 ? -10.31831 -10.88518 -8.11451  1.000 15.85340 ?  207 VAL   A C   1 
ATOM   1497 O O   . VAL   A 1 200 ? -10.14398 -9.70769  -8.43871  1.000 17.83417 ?  207 VAL   A O   1 
ATOM   1498 C CB  . VAL   A 1 200 ? -10.83097 -12.66214 -9.80554  1.000 16.47697 ?  207 VAL   A CB  1 
ATOM   1499 C CG1 . VAL   A 1 200 ? -11.60954 -11.56280 -10.54863 1.000 18.01716 ?  207 VAL   A CG1 1 
ATOM   1500 C CG2 . VAL   A 1 200 ? -10.24468 -13.70393 -10.79649 1.000 15.90978 ?  207 VAL   A CG2 1 
ATOM   1501 N N   . LYS   A 1 201 ? -10.97458 -11.20745 -7.00017  1.000 14.69454 ?  208 LYS   A N   1 
ATOM   1502 C CA  . LYS   A 1 201 ? -11.54607 -10.15020 -6.16509  1.000 17.27449 ?  208 LYS   A CA  1 
ATOM   1503 C C   . LYS   A 1 201 ? -10.44902 -9.31493  -5.54194  1.000 19.12715 ?  208 LYS   A C   1 
ATOM   1504 O O   . LYS   A 1 201 ? -10.58655 -8.10201  -5.44931  1.000 21.02722 ?  208 LYS   A O   1 
ATOM   1505 C CB  . LYS   A 1 201 ? -12.43247 -10.77479 -5.06932  1.000 17.04426 ?  208 LYS   A CB  1 
ATOM   1506 C CG  . LYS   A 1 201 ? -13.12537 -9.74278  -4.14995  1.000 21.74949 ?  208 LYS   A CG  1 
ATOM   1507 C CD  . LYS   A 1 201 ? -13.98797 -10.43522 -3.09114  1.000 26.88271 ?  208 LYS   A CD  1 
ATOM   1508 C CE  . LYS   A 1 201 ? -14.70274 -9.45806  -2.20710  1.000 33.63641 ?  208 LYS   A CE  1 
ATOM   1509 N NZ  . LYS   A 1 201 ? -15.62491 -10.24729 -1.33082  1.000 41.39070 ?  208 LYS   A NZ  1 
ATOM   1510 N N   . LYS   A 1 202 ? -9.33762  -9.95200  -5.12979  1.000 17.31482 ?  209 LYS   A N   1 
ATOM   1511 C CA  . LYS   A 1 202 ? -8.25097  -9.25175  -4.42485  1.000 17.74778 ?  209 LYS   A CA  1 
ATOM   1512 C C   . LYS   A 1 202 ? -7.45783  -8.32534  -5.35138  1.000 18.35367 ?  209 LYS   A C   1 
ATOM   1513 O O   . LYS   A 1 202 ? -7.12339  -7.18833  -4.98307  1.000 20.51305 ?  209 LYS   A O   1 
ATOM   1514 C CB  . LYS   A 1 202 ? -7.32145  -10.29451 -3.81466  1.000 18.81382 ?  209 LYS   A CB  1 
ATOM   1515 C CG  . LYS   A 1 202 ? -6.10633  -9.67571  -3.11918  1.000 21.39328 ?  209 LYS   A CG  1 
ATOM   1516 C CD  . LYS   A 1 202 ? -5.52479  -10.72400 -2.20048  1.000 33.81256 ?  209 LYS   A CD  1 
ATOM   1517 C CE  . LYS   A 1 202 ? -4.22063  -10.24213 -1.52196  1.000 42.63217 ?  209 LYS   A CE  1 
ATOM   1518 N NZ  . LYS   A 1 202 ? -3.31805  -11.39176 -1.08804  1.000 43.80007 ?  209 LYS   A NZ  1 
ATOM   1519 N N   . HIS   A 1 203 ? -7.17439  -8.79509  -6.57755  1.000 19.53976 ?  210 HIS   A N   1 
ATOM   1520 C CA  . HIS   A 1 203 ? -6.18609  -8.14246  -7.40799  1.000 22.55001 ?  210 HIS   A CA  1 
ATOM   1521 C C   . HIS   A 1 203 ? -6.71795  -7.52685  -8.69160  1.000 21.50789 ?  210 HIS   A C   1 
ATOM   1522 O O   . HIS   A 1 203 ? -5.96291  -6.76488  -9.32691  1.000 22.90253 ?  210 HIS   A O   1 
ATOM   1523 C CB  . HIS   A 1 203 ? -5.07845  -9.13480  -7.81187  1.000 24.53186 ?  210 HIS   A CB  1 
ATOM   1524 C CG  . HIS   A 1 203 ? -4.27114  -9.64879  -6.66343  1.000 25.81126 ?  210 HIS   A CG  1 
ATOM   1525 N ND1 . HIS   A 1 203 ? -3.43837  -8.83858  -5.93483  1.000 25.06856 ?  210 HIS   A ND1 1 
ATOM   1526 C CD2 . HIS   A 1 203 ? -4.15272  -10.89168 -6.13033  1.000 26.48401 ?  210 HIS   A CD2 1 
ATOM   1527 C CE1 . HIS   A 1 203 ? -2.85634  -9.54569  -4.97974  1.000 25.16057 ?  210 HIS   A CE1 1 
ATOM   1528 N NE2 . HIS   A 1 203 ? -3.27201  -10.79871 -5.08149  1.000 27.15297 ?  210 HIS   A NE2 1 
ATOM   1529 N N   . SER   A 1 204 ? -7.94368  -7.84391  -9.11502  1.000 19.38037 ?  211 SER   A N   1 
ATOM   1530 C CA  . SER   A 1 204 ? -8.42464  -7.43753  -10.41897 1.000 19.04663 ?  211 SER   A CA  1 
ATOM   1531 C C   . SER   A 1 204 ? -9.75720  -6.69292  -10.32025 1.000 18.36390 ?  211 SER   A C   1 
ATOM   1532 O O   . SER   A 1 204 ? -10.55828 -6.72533  -11.28209 1.000 21.77021 ?  211 SER   A O   1 
ATOM   1533 C CB  . SER   A 1 204 ? -8.55357  -8.66241  -11.35870 1.000 21.96816 ?  211 SER   A CB  1 
ATOM   1534 O OG  . SER   A 1 204 ? -7.26133  -9.29840  -11.45844 1.000 22.62817 ?  211 SER   A OG  1 
ATOM   1535 N N   . GLN   A 1 205 ? -9.95904  -5.96560  -9.22617  1.000 21.71266 ?  212 GLN   A N   1 
ATOM   1536 C CA  . GLN   A 1 205 ? -11.24673 -5.32732  -8.97820  1.000 29.84802 ?  212 GLN   A CA  1 
ATOM   1537 C C   . GLN   A 1 205 ? -11.57075 -4.22821  -9.99124  1.000 31.46664 ?  212 GLN   A C   1 
ATOM   1538 O O   . GLN   A 1 205 ? -12.75434 -3.95544  -10.24899 1.000 31.81894 ?  212 GLN   A O   1 
ATOM   1539 C CB  . GLN   A 1 205 ? -11.26069 -4.76408  -7.53754  1.000 32.71665 ?  212 GLN   A CB  1 
ATOM   1540 C CG  . GLN   A 1 205 ? -12.66347 -4.76395  -6.93502  1.000 55.32525 ?  212 GLN   A CG  1 
ATOM   1541 C CD  . GLN   A 1 205 ? -13.23303 -6.20656  -6.73437  1.000 52.10952 ?  212 GLN   A CD  1 
ATOM   1542 O OE1 . GLN   A 1 205 ? -13.09046 -6.80260  -5.66962  1.000 61.30240 ?  212 GLN   A OE1 1 
ATOM   1543 N NE2 . GLN   A 1 205 ? -13.90799 -6.73460  -7.75767  1.000 60.88781 ?  212 GLN   A NE2 1 
ATOM   1544 N N   . PHE   A 1 206 ? -10.54516 -3.59305  -10.57281 1.000 23.09793 ?  213 PHE   A N   1 
ATOM   1545 C CA  . PHE   A 1 206 ? -10.71616 -2.45301  -11.47457 1.000 25.39666 ?  213 PHE   A CA  1 
ATOM   1546 C C   . PHE   A 1 206 ? -10.33853 -2.78217  -12.90681 1.000 23.99484 ?  213 PHE   A C   1 
ATOM   1547 O O   . PHE   A 1 206 ? -9.92813  -1.90734  -13.68524 1.000 26.72562 ?  213 PHE   A O   1 
ATOM   1548 C CB  . PHE   A 1 206 ? -9.91129  -1.27503  -10.94658 1.000 23.69561 ?  213 PHE   A CB  1 
ATOM   1549 C CG  . PHE   A 1 206 ? -10.40271 -0.83022  -9.58233  1.000 29.48682 ?  213 PHE   A CG  1 
ATOM   1550 C CD1 . PHE   A 1 206 ? -9.55389  -0.83365  -8.50360  1.000 32.89820 ?  213 PHE   A CD1 1 
ATOM   1551 C CD2 . PHE   A 1 206 ? -11.72085 -0.42147  -9.38734  1.000 29.00131 ?  213 PHE   A CD2 1 
ATOM   1552 C CE1 . PHE   A 1 206 ? -10.00118 -0.44873  -7.24778  1.000 37.84821 ?  213 PHE   A CE1 1 
ATOM   1553 C CE2 . PHE   A 1 206 ? -12.17066 -0.01002  -8.11037  1.000 36.89330 ?  213 PHE   A CE2 1 
ATOM   1554 C CZ  . PHE   A 1 206 ? -11.31098 -0.03054  -7.05793  1.000 36.30137 ?  213 PHE   A CZ  1 
ATOM   1555 N N   . ILE   A 1 207 ? -10.52109 -4.02374  -13.28717 1.000 17.31678 ?  214 ILE   A N   1 
ATOM   1556 C CA  . ILE   A 1 207 ? -10.40383 -4.39944  -14.69226 1.000 16.12994 ?  214 ILE   A CA  1 
ATOM   1557 C C   . ILE   A 1 207 ? -11.73091 -4.12658  -15.37402 1.000 19.27884 ?  214 ILE   A C   1 
ATOM   1558 O O   . ILE   A 1 207 ? -12.76512 -4.63870  -14.93374 1.000 20.92071 ?  214 ILE   A O   1 
ATOM   1559 C CB  . ILE   A 1 207 ? -9.99435  -5.87543  -14.82851 1.000 16.00007 ?  214 ILE   A CB  1 
ATOM   1560 C CG1 . ILE   A 1 207 ? -8.61988  -6.06841  -14.19043 1.000 17.47781 ?  214 ILE   A CG1 1 
ATOM   1561 C CG2 . ILE   A 1 207 ? -9.96688  -6.36456  -16.31422 1.000 16.77315 ?  214 ILE   A CG2 1 
ATOM   1562 C CD1 . ILE   A 1 207 ? -7.43463  -5.30667  -14.91040 1.000 21.28556 ?  214 ILE   A CD1 1 
ATOM   1563 N N   . GLY   A 1 208 ? -11.70556 -3.34907  -16.44726 1.000 17.61109 ?  215 GLY   A N   1 
ATOM   1564 C CA  . GLY   A 1 208 ? -12.93262 -2.84332  -17.04160 1.000 18.59072 ?  215 GLY   A CA  1 
ATOM   1565 C C   . GLY   A 1 208 ? -13.55855 -3.70362  -18.11871 1.000 17.15846 ?  215 GLY   A C   1 
ATOM   1566 O O   . GLY   A 1 208 ? -14.15406 -3.18126  -19.05989 1.000 19.21304 ?  215 GLY   A O   1 
ATOM   1567 N N   . TYR   A 1 209 ? -13.50311 -5.01299  -17.95557 1.000 16.33748 ?  216 TYR   A N   1 
ATOM   1568 C CA  . TYR   A 1 209 ? -14.07473 -5.98162  -18.89751 1.000 18.17083 ?  216 TYR   A CA  1 
ATOM   1569 C C   . TYR   A 1 209 ? -14.67211 -7.05973  -18.03326 1.000 16.94875 ?  216 TYR   A C   1 
ATOM   1570 O O   . TYR   A 1 209 ? -14.12988 -7.35600  -16.95033 1.000 19.40161 ?  216 TYR   A O   1 
ATOM   1571 C CB  . TYR   A 1 209 ? -12.96377 -6.59241  -19.81844 1.000 15.42253 ?  216 TYR   A CB  1 
ATOM   1572 C CG  . TYR   A 1 209 ? -12.35482 -5.49255  -20.68682 1.000 14.39971 ?  216 TYR   A CG  1 
ATOM   1573 C CD1 . TYR   A 1 209 ? -13.02638 -5.02713  -21.85343 1.000 16.94794 ?  216 TYR   A CD1 1 
ATOM   1574 C CD2 . TYR   A 1 209 ? -11.13012 -4.89484  -20.35365 1.000 14.70633 ?  216 TYR   A CD2 1 
ATOM   1575 C CE1 . TYR   A 1 209 ? -12.50136 -4.00814  -22.61844 1.000 17.19516 ?  216 TYR   A CE1 1 
ATOM   1576 C CE2 . TYR   A 1 209 ? -10.60947 -3.86297  -21.12051 1.000 14.38403 ?  216 TYR   A CE2 1 
ATOM   1577 C CZ  . TYR   A 1 209 ? -11.28804 -3.43013  -22.24598 1.000 13.43125 ?  216 TYR   A CZ  1 
ATOM   1578 O OH  . TYR   A 1 209 ? -10.83069 -2.40280  -23.03861 1.000 17.14422 ?  216 TYR   A OH  1 
ATOM   1579 N N   . PRO   A 1 210 ? -15.71167 -7.74700  -18.50926 1.000 16.07046 ?  217 PRO   A N   1 
ATOM   1580 C CA  . PRO   A 1 210 ? -16.25396 -8.90713  -17.79559 1.000 14.81994 ?  217 PRO   A CA  1 
ATOM   1581 C C   . PRO   A 1 210 ? -15.21542 -9.99061  -17.69462 1.000 16.71163 ?  217 PRO   A C   1 
ATOM   1582 O O   . PRO   A 1 210 ? -14.53060 -10.29615 -18.68570 1.000 18.97327 ?  217 PRO   A O   1 
ATOM   1583 C CB  . PRO   A 1 210 ? -17.41554 -9.37013  -18.68908 1.000 21.22899 ?  217 PRO   A CB  1 
ATOM   1584 C CG  . PRO   A 1 210 ? -17.74033 -8.22985  -19.53642 1.000 23.69934 ?  217 PRO   A CG  1 
ATOM   1585 C CD  . PRO   A 1 210 ? -16.52404 -7.39128  -19.70633 1.000 18.43663 ?  217 PRO   A CD  1 
ATOM   1586 N N   . ILE   A 1 211 ? -15.10831 -10.59167 -16.50656 1.000 15.55667 ?  218 ILE   A N   1 
ATOM   1587 C CA  . ILE   A 1 211 ? -14.21736 -11.72608 -16.25701 1.000 13.66683 ?  218 ILE   A CA  1 
ATOM   1588 C C   . ILE   A 1 211 ? -15.11671 -12.86061 -15.82257 1.000 13.30879 ?  218 ILE   A C   1 
ATOM   1589 O O   . ILE   A 1 211 ? -15.72267 -12.80142 -14.73682 1.000 20.36208 ?  218 ILE   A O   1 
ATOM   1590 C CB  . ILE   A 1 211 ? -13.14964 -11.44865 -15.17546 1.000 14.64452 ?  218 ILE   A CB  1 
ATOM   1591 C CG1 . ILE   A 1 211 ? -12.25937 -10.22904 -15.53751 1.000 14.60050 ?  218 ILE   A CG1 1 
ATOM   1592 C CG2 . ILE   A 1 211 ? -12.34341 -12.74052 -14.88163 1.000 16.99696 ?  218 ILE   A CG2 1 
ATOM   1593 C CD1 . ILE   A 1 211 ? -11.48020 -9.75466  -14.31764 1.000 14.61378 ?  218 ILE   A CD1 1 
ATOM   1594 N N   . THR   A 1 212 ? -15.27597 -13.85628 -16.69975 1.000 13.84579 ?  219 THR   A N   1 
ATOM   1595 C CA  . THR   A 1 212 ? -16.17614 -14.95598 -16.38052 1.000 13.81291 ?  219 THR   A CA  1 
ATOM   1596 C C   . THR   A 1 212 ? -15.36808 -16.16639 -15.95715 1.000 13.05604 ?  219 THR   A C   1 
ATOM   1597 O O   . THR   A 1 212 ? -14.57187 -16.65466 -16.74687 1.000 13.83865 ?  219 THR   A O   1 
ATOM   1598 C CB  . THR   A 1 212 ? -17.01157 -15.29597 -17.61958 1.000 14.60318 ?  219 THR   A CB  1 
ATOM   1599 O OG1 . THR   A 1 212 ? -17.77442 -14.11732 -17.98492 1.000 15.40745 ?  219 THR   A OG1 1 
ATOM   1600 C CG2 . THR   A 1 212 ? -17.96982 -16.48285 -17.26237 1.000 18.60094 ?  219 THR   A CG2 1 
ATOM   1601 N N   . LEU   A 1 213 ? -15.58225 -16.65478 -14.75041 1.000 13.82265 ?  220 LEU   A N   1 
ATOM   1602 C CA  . LEU   A 1 213 ? -14.94549 -17.86672 -14.25425 1.000 12.63385 ?  220 LEU   A CA  1 
ATOM   1603 C C   . LEU   A 1 213 ? -15.87760 -19.04106 -14.58538 1.000 13.91792 ?  220 LEU   A C   1 
ATOM   1604 O O   . LEU   A 1 213 ? -16.98939 -19.16312 -14.03524 1.000 16.42206 ?  220 LEU   A O   1 
ATOM   1605 C CB  . LEU   A 1 213 ? -14.69930 -17.71484 -12.75101 1.000 13.61796 ?  220 LEU   A CB  1 
ATOM   1606 C CG  . LEU   A 1 213 ? -14.16996 -18.95045 -12.08996 1.000 18.03196 ?  220 LEU   A CG  1 
ATOM   1607 C CD1 . LEU   A 1 213 ? -12.90904 -19.49798 -12.75920 1.000 17.62802 ?  220 LEU   A CD1 1 
ATOM   1608 C CD2 . LEU   A 1 213 ? -13.88944 -18.65150 -10.59143 1.000 17.04757 ?  220 LEU   A CD2 1 
ATOM   1609 N N   . PHE   A 1 214 ? -15.42700 -19.89464 -15.50005 1.000 14.86077 ?  221 PHE   A N   1 
ATOM   1610 C CA  . PHE   A 1 214 ? -16.18388 -21.08561 -15.85410 1.000 13.12824 ?  221 PHE   A CA  1 
ATOM   1611 C C   . PHE   A 1 214 ? -16.13959 -22.08243 -14.73046 1.000 14.12743 ?  221 PHE   A C   1 
ATOM   1612 O O   . PHE   A 1 214 ? -15.14647 -22.18505 -13.98793 1.000 18.25923 ?  221 PHE   A O   1 
ATOM   1613 C CB  . PHE   A 1 214 ? -15.57877 -21.75620 -17.10742 1.000 12.44463 ?  221 PHE   A CB  1 
ATOM   1614 C CG  . PHE   A 1 214 ? -15.84548 -21.05472 -18.42021 1.000 12.02325 ?  221 PHE   A CG  1 
ATOM   1615 C CD1 . PHE   A 1 214 ? -15.95523 -19.66503 -18.53139 1.000 12.02862 ?  221 PHE   A CD1 1 
ATOM   1616 C CD2 . PHE   A 1 214 ? -15.92426 -21.83247 -19.56812 1.000 14.68731 ?  221 PHE   A CD2 1 
ATOM   1617 C CE1 . PHE   A 1 214 ? -16.15535 -19.06518 -19.78671 1.000 14.15790 ?  221 PHE   A CE1 1 
ATOM   1618 C CE2 . PHE   A 1 214 ? -16.13299 -21.24899 -20.81452 1.000 14.29878 ?  221 PHE   A CE2 1 
ATOM   1619 C CZ  . PHE   A 1 214 ? -16.25382 -19.87649 -20.91182 1.000 13.73495 ?  221 PHE   A CZ  1 
ATOM   1620 N N   . VAL   A 1 215 ? -17.21988 -22.86255 -14.62200 1.000 15.72676 ?  222 VAL   A N   1 
ATOM   1621 C CA  . VAL   A 1 215 ? -17.23699 -23.92768 -13.62897 1.000 18.23180 ?  222 VAL   A CA  1 
ATOM   1622 C C   . VAL   A 1 215 ? -17.10063 -25.25365 -14.34670 1.000 19.33792 ?  222 VAL   A C   1 
ATOM   1623 O O   . VAL   A 1 215 ? -17.16643 -25.32921 -15.58772 1.000 19.15929 ?  222 VAL   A O   1 
ATOM   1624 C CB  . VAL   A 1 215 ? -18.48378 -23.90053 -12.74624 1.000 30.70762 ?  222 VAL   A CB  1 
ATOM   1625 C CG1 . VAL   A 1 215 ? -18.34614 -22.72245 -11.71438 1.000 27.23983 ?  222 VAL   A CG1 1 
ATOM   1626 C CG2 . VAL   A 1 215 ? -19.66642 -23.80843 -13.59122 1.000 22.61566 ?  222 VAL   A CG2 1 
ATOM   1627 N N   . GLU   A 1 216 ? -16.77021 -26.28338 -13.58020 1.000 20.35032 ?  223 GLU   A N   1 
ATOM   1628 C CA  . GLU   A 1 216 ? -16.53984 -27.60797 -14.14099 1.000 23.89140 ?  223 GLU   A CA  1 
ATOM   1629 C C   . GLU   A 1 216 ? -17.65533 -28.56365 -13.75751 1.000 30.41860 ?  223 GLU   A C   1 
ATOM   1630 O O   . GLU   A 1 216 ? -18.18801 -28.48935 -12.64628 1.000 29.61756 ?  223 GLU   A O   1 
ATOM   1631 C CB  . GLU   A 1 216 ? -15.19682 -28.17802 -13.67815 1.000 23.42297 ?  223 GLU   A CB  1 
ATOM   1632 C CG  . GLU   A 1 216 ? -14.03577 -27.28566 -14.13671 1.000 23.94128 ?  223 GLU   A CG  1 
ATOM   1633 C CD  . GLU   A 1 216 ? -12.72494 -27.83958 -13.62438 1.000 26.01169 ?  223 GLU   A CD  1 
ATOM   1634 O OE1 . GLU   A 1 216 ? -12.34641 -28.94215 -14.07754 1.000 28.32088 ?  223 GLU   A OE1 1 
ATOM   1635 O OE2 . GLU   A 1 216 ? -12.11946 -27.15659 -12.73954 1.000 32.12782 ?  223 GLU   A OE2 1 
ATOM   1636 N N   . LYS   A 1 217 ? -17.95151 -29.51825 -14.65602 1.000 33.10755 ?  224 LYS   A N   1 
ATOM   1637 C CA  . LYS   A 1 217 ? -18.68825 -30.71270 -14.22339 1.000 37.27186 ?  224 LYS   A CA  1 
ATOM   1638 C C   . LYS   A 1 217 ? -17.87309 -31.47683 -13.15450 1.000 37.70061 ?  224 LYS   A C   1 
ATOM   1639 O O   . LYS   A 1 217 ? -18.41455 -31.83258 -12.11622 1.000 50.66355 ?  224 LYS   A O   1 
ATOM   1640 C CB  . LYS   A 1 217 ? -19.00839 -31.64785 -15.38678 1.000 38.41021 ?  224 LYS   A CB  1 
ATOM   1641 C CG  . LYS   A 1 217 ? -17.90485 -31.83534 -16.37332 1.000 47.18229 ?  224 LYS   A CG  1 
ATOM   1642 C CD  . LYS   A 1 217 ? -18.40329 -32.56928 -17.61088 1.000 47.79361 ?  224 LYS   A CD  1 
ATOM   1643 C CE  . LYS   A 1 217 ? -18.51921 -34.04148 -17.44706 1.000 53.65486 ?  224 LYS   A CE  1 
ATOM   1644 N NZ  . LYS   A 1 217 ? -17.17957 -34.68118 -17.50754 1.000 63.56428 ?  224 LYS   A NZ  1 
HETATM 1645 C C1  . A1AXE B 2 .   ? -11.77956 -28.27539 -30.03339 1.000 31.03308 ?  301 A1AXE A C1  1 
HETATM 1646 C C10 . A1AXE B 2 .   ? -9.42841  -28.96148 -35.05944 1.000 58.24030 ?  301 A1AXE A C10 1 
HETATM 1647 C C2  . A1AXE B 2 .   ? -13.40586 -26.73360 -31.13969 1.000 35.57054 ?  301 A1AXE A C2  1 
HETATM 1648 C C4  . A1AXE B 2 .   ? -12.68666 -26.82227 -33.25891 1.000 30.78519 ?  301 A1AXE A C4  1 
HETATM 1649 C C5  . A1AXE B 2 .   ? -12.43954 -26.71229 -34.63056 1.000 29.82493 ?  301 A1AXE A C5  1 
HETATM 1650 C C6  . A1AXE B 2 .   ? -11.39123 -27.42664 -35.15786 1.000 32.65722 ?  301 A1AXE A C6  1 
HETATM 1651 C C7  . A1AXE B 2 .   ? -10.57217 -28.24916 -34.35595 1.000 41.10771 ?  301 A1AXE A C7  1 
HETATM 1652 C C3  . A1AXE B 2 .   ? -13.64630 -26.24085 -32.37687 1.000 25.96920 ?  301 A1AXE A C3  1 
HETATM 1653 C C8  . A1AXE B 2 .   ? -10.80260 -28.38468 -32.99408 0.696 23.65479 ?  301 A1AXE A C8  1 
HETATM 1654 C C9  . A1AXE B 2 .   ? -11.87269 -27.66746 -32.47271 1.000 26.13211 ?  301 A1AXE A C9  1 
HETATM 1655 N N1  . A1AXE B 2 .   ? -12.32882 -27.58797 -31.17295 0.582 25.51845 ?  301 A1AXE A N1  1 
HETATM 1656 O O1  . A1AXE B 2 .   ? -9.32023  -28.73176 -36.29797 1.000 51.86713 -1 301 A1AXE A O1  1 
HETATM 1657 O O2  . A1AXE B 2 .   ? -8.63246  -29.68480 -34.38142 1.000 51.20013 ?  301 A1AXE A O2  1 
HETATM 1658 O O   . HOH   C 3 .   ? 18.01857  -0.32337  -15.74781 1.000 51.91418 ?  401 HOH   A O   1 
HETATM 1659 O O   . HOH   C 3 .   ? -9.53939  -23.62355 -2.48894  1.000 37.96143 ?  402 HOH   A O   1 
HETATM 1660 O O   . HOH   C 3 .   ? -17.52250 -5.22197  -36.71139 1.000 65.98327 ?  403 HOH   A O   1 
HETATM 1661 O O   . HOH   C 3 .   ? -2.47631  -27.31596 -35.86827 1.000 52.86992 ?  404 HOH   A O   1 
HETATM 1662 O O   . HOH   C 3 .   ? 12.39968  -8.68096  -29.56843 1.000 26.38302 ?  405 HOH   A O   1 
HETATM 1663 O O   . HOH   C 3 .   ? 5.76324   -25.60840 -7.25045  1.000 40.02384 ?  406 HOH   A O   1 
HETATM 1664 O O   . HOH   C 3 .   ? 10.19173  -23.86484 -9.10758  1.000 41.99932 ?  407 HOH   A O   1 
HETATM 1665 O O   . HOH   C 3 .   ? 11.990    -21.237   -40.666   1.000 48.57021 ?  408 HOH   A O   1 
HETATM 1666 O O   . HOH   C 3 .   ? 13.78778  -10.91866 -29.22545 1.000 32.15728 ?  409 HOH   A O   1 
HETATM 1667 O O   . HOH   C 3 .   ? 0.49504   -30.30725 -23.07286 1.000 49.98411 ?  410 HOH   A O   1 
HETATM 1668 O O   . HOH   C 3 .   ? -13.86811 -7.33273  -41.85704 1.000 46.11055 ?  411 HOH   A O   1 
HETATM 1669 O O   . HOH   C 3 .   ? -15.73042 0.05069   -30.09003 1.000 35.33382 ?  412 HOH   A O   1 
HETATM 1670 O O   . HOH   C 3 .   ? 17.636    -26.211   -21.360   1.000 46.77041 ?  413 HOH   A O   1 
HETATM 1671 O O   . HOH   C 3 .   ? -9.60715  -23.79104 -26.36175 1.000 56.04524 ?  414 HOH   A O   1 
HETATM 1672 O O   . HOH   C 3 .   ? 3.10389   -16.91212 -41.16957 1.000 47.65288 ?  415 HOH   A O   1 
HETATM 1673 O O   . HOH   C 3 .   ? 0.49778   -28.48468 -25.64930 1.000 48.58896 ?  416 HOH   A O   1 
HETATM 1674 O O   . HOH   C 3 .   ? 0.72505   -29.72839 -16.10747 1.000 28.15686 ?  417 HOH   A O   1 
HETATM 1675 O O   . HOH   C 3 .   ? -2.81802  -3.05451  -35.26404 1.000 42.17539 ?  418 HOH   A O   1 
HETATM 1676 O O   . HOH   C 3 .   ? 3.51955   -24.09127 -38.76298 1.000 28.89033 ?  419 HOH   A O   1 
HETATM 1677 O O   . HOH   C 3 .   ? 0.33140   -15.04735 -1.39645  1.000 34.40827 ?  420 HOH   A O   1 
HETATM 1678 O O   . HOH   C 3 .   ? -12.88720 -8.50066  -9.33650  1.000 38.76642 ?  421 HOH   A O   1 
HETATM 1679 O O   . HOH   C 3 .   ? -7.25322  -28.09380 -21.15429 1.000 35.92321 ?  422 HOH   A O   1 
HETATM 1680 O O   . HOH   C 3 .   ? -5.64883  -28.66320 -4.89614  1.000 39.16754 ?  423 HOH   A O   1 
HETATM 1681 O O   . HOH   C 3 .   ? 6.49975   -26.72656 -27.84301 1.000 27.45831 ?  424 HOH   A O   1 
HETATM 1682 O O   . HOH   C 3 .   ? -18.62246 -12.05229 -21.05520 1.000 40.51100 ?  425 HOH   A O   1 
HETATM 1683 O O   . HOH   C 3 .   ? 6.01157   -21.28632 -0.09339  1.000 24.22561 ?  426 HOH   A O   1 
HETATM 1684 O O   . HOH   C 3 .   ? 0.17751   -22.19146 -2.15874  1.000 37.40990 ?  427 HOH   A O   1 
HETATM 1685 O O   . HOH   C 3 .   ? 12.85794  -13.66047 -29.45389 1.000 20.74162 ?  428 HOH   A O   1 
HETATM 1686 O O   . HOH   C 3 .   ? 0.45298   -5.01650  -16.18113 1.000 36.30257 ?  429 HOH   A O   1 
HETATM 1687 O O   . HOH   C 3 .   ? 13.30450  -8.49575  -33.57840 1.000 45.44587 ?  430 HOH   A O   1 
HETATM 1688 O O   . HOH   C 3 .   ? -7.440    -1.349    -14.253   1.000 30.71227 ?  431 HOH   A O   1 
HETATM 1689 O O   . HOH   C 3 .   ? -20.43554 -21.11844 -9.41142  1.000 35.30405 ?  432 HOH   A O   1 
HETATM 1690 O O   . HOH   C 3 .   ? 9.05433   -3.17103  -20.18473 1.000 20.59668 ?  433 HOH   A O   1 
HETATM 1691 O O   . HOH   C 3 .   ? -7.75963  -22.58481 -30.23142 1.000 28.13762 ?  434 HOH   A O   1 
HETATM 1692 O O   . HOH   C 3 .   ? 7.84117   -27.72280 -24.06181 1.000 27.82824 ?  435 HOH   A O   1 
HETATM 1693 O O   . HOH   C 3 .   ? -15.61434 -15.25028 -26.58480 1.000 40.33308 ?  436 HOH   A O   1 
HETATM 1694 O O   . HOH   C 3 .   ? -15.21425 -23.37897 -30.40046 1.000 26.55035 ?  437 HOH   A O   1 
HETATM 1695 O O   . HOH   C 3 .   ? -1.29706  -20.64618 -1.55681  1.000 50.17687 ?  438 HOH   A O   1 
HETATM 1696 O O   . HOH   C 3 .   ? 10.85696  -25.15966 -23.68082 1.000 19.07843 ?  439 HOH   A O   1 
HETATM 1697 O O   . HOH   C 3 .   ? -13.98968 -21.96191 -33.08424 1.000 36.67034 ?  440 HOH   A O   1 
HETATM 1698 O O   . HOH   C 3 .   ? -1.56000  -6.30019  -25.95204 1.000 18.18055 ?  441 HOH   A O   1 
HETATM 1699 O O   . HOH   C 3 .   ? -2.83179  -6.30663  -6.37490  1.000 30.68808 ?  442 HOH   A O   1 
HETATM 1700 O O   . HOH   C 3 .   ? 3.08249   -29.97237 -19.09396 1.000 42.02977 ?  443 HOH   A O   1 
HETATM 1701 O O   . HOH   C 3 .   ? -16.83676 -4.67550  -42.60175 1.000 46.10546 ?  444 HOH   A O   1 
HETATM 1702 O O   . HOH   C 3 .   ? -7.85859  -12.92139 -40.50305 1.000 46.71510 ?  445 HOH   A O   1 
HETATM 1703 O O   . HOH   C 3 .   ? 18.13265  -7.35018  -20.02325 1.000 32.45036 ?  446 HOH   A O   1 
HETATM 1704 O O   . HOH   C 3 .   ? 7.84101   -23.27504 -14.27602 1.000 24.63538 ?  447 HOH   A O   1 
HETATM 1705 O O   . HOH   C 3 .   ? -8.81259  -10.37463 -40.10151 1.000 39.78682 ?  448 HOH   A O   1 
HETATM 1706 O O   . HOH   C 3 .   ? 9.85284   -14.64833 -25.06907 1.000 16.21626 ?  449 HOH   A O   1 
HETATM 1707 O O   . HOH   C 3 .   ? -16.25828 -12.82443 -19.74524 1.000 17.88223 ?  450 HOH   A O   1 
HETATM 1708 O O   . HOH   C 3 .   ? -6.50718  -7.84120  -34.18697 1.000 18.24293 ?  451 HOH   A O   1 
HETATM 1709 O O   . HOH   C 3 .   ? -4.40947  0.54963   -22.19395 1.000 23.49333 ?  452 HOH   A O   1 
HETATM 1710 O O   . HOH   C 3 .   ? -13.30003 -0.97322  -20.27514 1.000 25.48228 ?  453 HOH   A O   1 
HETATM 1711 O O   . HOH   C 3 .   ? -13.08204 -7.25664  -11.95285 1.000 36.02738 ?  454 HOH   A O   1 
HETATM 1712 O O   . HOH   C 3 .   ? 7.72424   -18.95361 -6.52345  1.000 20.90344 ?  455 HOH   A O   1 
HETATM 1713 O O   . HOH   C 3 .   ? 1.25847   -7.03542  -5.19294  1.000 45.81253 ?  456 HOH   A O   1 
HETATM 1714 O O   . HOH   C 3 .   ? 9.19608   -26.45037 -17.11979 1.000 25.57361 ?  457 HOH   A O   1 
HETATM 1715 O O   . HOH   C 3 .   ? -16.02785 -26.07665 -17.88989 1.000 20.00429 ?  458 HOH   A O   1 
HETATM 1716 O O   . HOH   C 3 .   ? -13.58176 -14.84804 -30.54760 1.000 46.33572 ?  459 HOH   A O   1 
HETATM 1717 O O   . HOH   C 3 .   ? 6.80806   -29.59515 -20.25014 1.000 28.19801 ?  460 HOH   A O   1 
HETATM 1718 O O   . HOH   C 3 .   ? 20.08228  -10.27431 -26.07332 1.000 38.45500 ?  461 HOH   A O   1 
HETATM 1719 O O   . HOH   C 3 .   ? -1.39017  -29.14891 -5.97501  1.000 28.18636 ?  462 HOH   A O   1 
HETATM 1720 O O   . HOH   C 3 .   ? 16.51751  -14.61903 -7.12448  1.000 46.81087 ?  463 HOH   A O   1 
HETATM 1721 O O   . HOH   C 3 .   ? 0.90025   -21.21960 -4.68049  1.000 20.65734 ?  464 HOH   A O   1 
HETATM 1722 O O   . HOH   C 3 .   ? -0.31610  -5.55644  -18.24224 1.000 24.97005 ?  465 HOH   A O   1 
HETATM 1723 O O   . HOH   C 3 .   ? 1.35502   -7.86613  -16.42397 1.000 17.96966 ?  466 HOH   A O   1 
HETATM 1724 O O   . HOH   C 3 .   ? 6.09836   1.49475   -11.70191 1.000 41.00763 ?  467 HOH   A O   1 
HETATM 1725 O O   . HOH   C 3 .   ? -11.11594 -14.41892 -37.44658 1.000 28.61591 ?  468 HOH   A O   1 
HETATM 1726 O O   . HOH   C 3 .   ? 3.18409   -6.30310  -10.90490 1.000 19.36449 ?  469 HOH   A O   1 
HETATM 1727 O O   . HOH   C 3 .   ? -10.628   -14.701   0.955     1.000 21.21662 ?  470 HOH   A O   1 
HETATM 1728 O O   . HOH   C 3 .   ? -3.47643  -10.95736 -23.90850 1.000 23.50646 ?  471 HOH   A O   1 
HETATM 1729 O O   . HOH   C 3 .   ? -8.47901  4.61586   -33.36194 1.000 23.09418 ?  472 HOH   A O   1 
HETATM 1730 O O   . HOH   C 3 .   ? -1.42936  -4.72601  -33.24846 1.000 35.85536 ?  473 HOH   A O   1 
HETATM 1731 O O   . HOH   C 3 .   ? -8.73529  -11.83899 -36.18366 1.000 20.08440 ?  474 HOH   A O   1 
HETATM 1732 O O   . HOH   C 3 .   ? 3.05431   -20.55308 -2.88322  1.000 29.81722 ?  475 HOH   A O   1 
HETATM 1733 O O   . HOH   C 3 .   ? -7.86531  -3.96935  -10.65333 1.000 27.76286 ?  476 HOH   A O   1 
HETATM 1734 O O   . HOH   C 3 .   ? 15.53209  -20.15941 -18.63692 1.000 19.78062 ?  477 HOH   A O   1 
HETATM 1735 O O   . HOH   C 3 .   ? -2.54297  -10.57644 -26.71553 1.000 22.97779 ?  478 HOH   A O   1 
HETATM 1736 O O   . HOH   C 3 .   ? -1.18974  -7.54153  -23.50985 1.000 19.37301 ?  479 HOH   A O   1 
HETATM 1737 O O   . HOH   C 3 .   ? 10.29167  -21.15144 -6.88388  1.000 31.55800 ?  480 HOH   A O   1 
HETATM 1738 O O   . HOH   C 3 .   ? 7.93150   -23.36525 -7.18885  1.000 30.90837 ?  481 HOH   A O   1 
HETATM 1739 O O   . HOH   C 3 .   ? -14.18663 -11.79887 0.36690   1.000 30.28022 ?  482 HOH   A O   1 
HETATM 1740 O O   . HOH   C 3 .   ? -9.30801  -2.30132  -17.51361 1.000 19.26870 ?  483 HOH   A O   1 
HETATM 1741 O O   . HOH   C 3 .   ? -0.35888  -5.79671  -37.89311 1.000 52.51513 ?  484 HOH   A O   1 
HETATM 1742 O O   . HOH   C 3 .   ? -2.17612  -13.53374 -35.58724 1.000 16.03506 ?  485 HOH   A O   1 
HETATM 1743 O O   . HOH   C 3 .   ? -5.67536  -31.34343 -11.75722 1.000 26.52913 ?  486 HOH   A O   1 
HETATM 1744 O O   . HOH   C 3 .   ? 11.24969  -7.91119  -27.14624 1.000 19.72313 ?  487 HOH   A O   1 
HETATM 1745 O O   . HOH   C 3 .   ? 9.77921   -17.55263 -7.72826  1.000 18.04075 ?  488 HOH   A O   1 
HETATM 1746 O O   . HOH   C 3 .   ? 2.99245   -5.53498  -33.86899 1.000 45.19052 ?  489 HOH   A O   1 
HETATM 1747 O O   . HOH   C 3 .   ? -17.02591 -5.51237  -22.62457 1.000 26.51579 ?  490 HOH   A O   1 
HETATM 1748 O O   . HOH   C 3 .   ? -7.58874  -28.42697 -8.04568  1.000 27.41923 ?  491 HOH   A O   1 
HETATM 1749 O O   . HOH   C 3 .   ? 15.08432  -0.86170  -12.01593 1.000 32.12774 ?  492 HOH   A O   1 
HETATM 1750 O O   . HOH   C 3 .   ? 4.26806   -24.08106 -30.72391 1.000 16.00772 ?  493 HOH   A O   1 
HETATM 1751 O O   . HOH   C 3 .   ? -8.13418  -24.98498 -19.09791 1.000 15.31204 ?  494 HOH   A O   1 
HETATM 1752 O O   . HOH   C 3 .   ? 11.65614  -27.23141 -34.56833 1.000 20.88401 ?  495 HOH   A O   1 
HETATM 1753 O O   . HOH   C 3 .   ? -12.93001 -25.21332 -10.97772 1.000 24.97937 ?  496 HOH   A O   1 
HETATM 1754 O O   . HOH   C 3 .   ? -8.53180  4.01404   -38.41574 1.000 44.12690 ?  497 HOH   A O   1 
HETATM 1755 O O   . HOH   C 3 .   ? -5.72596  -2.19052  -19.34291 1.000 17.59326 ?  498 HOH   A O   1 
HETATM 1756 O O   . HOH   C 3 .   ? -5.30119  -10.44436 -27.29862 1.000 14.58802 ?  499 HOH   A O   1 
HETATM 1757 O O   . HOH   C 3 .   ? 19.56726  -16.49036 -27.59556 1.000 30.38564 ?  500 HOH   A O   1 
HETATM 1758 O O   . HOH   C 3 .   ? -4.26597  -4.83540  -8.38215  1.000 36.57509 ?  501 HOH   A O   1 
HETATM 1759 O O   . HOH   C 3 .   ? 18.19611  -19.06388 -24.51703 1.000 28.56470 ?  502 HOH   A O   1 
HETATM 1760 O O   . HOH   C 3 .   ? -5.44756  -5.53093  -11.72386 1.000 31.90770 ?  503 HOH   A O   1 
HETATM 1761 O O   . HOH   C 3 .   ? -13.68921 -17.26990 -2.70962  1.000 22.84905 ?  504 HOH   A O   1 
HETATM 1762 O O   . HOH   C 3 .   ? -14.70670 -7.37295  -14.26623 1.000 31.94998 ?  505 HOH   A O   1 
HETATM 1763 O O   . HOH   C 3 .   ? 6.13408   -21.73612 -37.26399 1.000 26.34048 ?  506 HOH   A O   1 
HETATM 1764 O O   . HOH   C 3 .   ? -19.67258 -19.73221 -14.20171 1.000 17.34943 ?  507 HOH   A O   1 
HETATM 1765 O O   . HOH   C 3 .   ? -10.28768 -0.73256  -19.92380 1.000 20.74321 ?  508 HOH   A O   1 
HETATM 1766 O O   . HOH   C 3 .   ? -7.26647  1.22649   -19.38921 1.000 23.26941 ?  509 HOH   A O   1 
HETATM 1767 O O   . HOH   C 3 .   ? 19.82812  -5.54154  -14.45758 1.000 34.96215 ?  510 HOH   A O   1 
HETATM 1768 O O   . HOH   C 3 .   ? -8.79243  -26.25293 -28.79866 1.000 37.05125 ?  511 HOH   A O   1 
HETATM 1769 O O   . HOH   C 3 .   ? -20.11464 -22.81644 -6.82772  1.000 56.14206 ?  512 HOH   A O   1 
HETATM 1770 O O   . HOH   C 3 .   ? -14.12059 -12.93614 -7.83630  1.000 21.34702 ?  513 HOH   A O   1 
HETATM 1771 O O   . HOH   C 3 .   ? -14.37182 -22.85881 -11.41929 1.000 24.29068 ?  514 HOH   A O   1 
HETATM 1772 O O   . HOH   C 3 .   ? -2.62740  -2.86710  -17.18664 1.000 40.32816 ?  515 HOH   A O   1 
HETATM 1773 O O   . HOH   C 3 .   ? -5.86830  -14.04407 -2.72381  1.000 45.02607 ?  516 HOH   A O   1 
HETATM 1774 O O   . HOH   C 3 .   ? 8.58781   -20.53964 -9.13914  1.000 24.79705 ?  517 HOH   A O   1 
HETATM 1775 O O   . HOH   C 3 .   ? 3.31695   -4.80043  -28.57235 1.000 50.42506 ?  518 HOH   A O   1 
HETATM 1776 O O   . HOH   C 3 .   ? -2.76153  -31.68172 -19.97874 1.000 40.16845 ?  519 HOH   A O   1 
HETATM 1777 O O   . HOH   C 3 .   ? -4.20186  -13.99811 -0.76693  1.000 37.10474 ?  520 HOH   A O   1 
HETATM 1778 O O   . HOH   C 3 .   ? 4.19793   -29.67976 -25.87384 1.000 33.96870 ?  521 HOH   A O   1 
HETATM 1779 O O   . HOH   C 3 .   ? 11.49658  -28.28503 -30.28465 1.000 30.41354 ?  522 HOH   A O   1 
HETATM 1780 O O   . HOH   C 3 .   ? -1.00820  -11.45039 -3.06557  1.000 34.42639 ?  523 HOH   A O   1 
HETATM 1781 O O   . HOH   C 3 .   ? 14.08446  -15.83839 -2.07391  1.000 29.12421 ?  524 HOH   A O   1 
HETATM 1782 O O   . HOH   C 3 .   ? -15.98080 -3.12762  -21.15225 1.000 25.53491 ?  525 HOH   A O   1 
HETATM 1783 O O   . HOH   C 3 .   ? -3.24496  -21.15189 -0.60895  1.000 29.03787 ?  526 HOH   A O   1 
HETATM 1784 O O   . HOH   C 3 .   ? -6.42970  -5.05749  -35.51187 1.000 18.31834 ?  527 HOH   A O   1 
HETATM 1785 O O   . HOH   C 3 .   ? -4.32014  -4.28657  -36.81221 1.000 42.59823 ?  528 HOH   A O   1 
HETATM 1786 O O   . HOH   C 3 .   ? 1.99934   -6.16949  -25.73320 1.000 31.32948 ?  529 HOH   A O   1 
HETATM 1787 O O   . HOH   C 3 .   ? -10.35817 -11.80978 -2.12492  1.000 18.71547 ?  530 HOH   A O   1 
HETATM 1788 O O   . HOH   C 3 .   ? 3.58078   -6.80526  -17.67690 1.000 20.47329 ?  531 HOH   A O   1 
HETATM 1789 O O   . HOH   C 3 .   ? 0.41223   -1.52386  -19.76823 1.000 39.54906 ?  532 HOH   A O   1 
HETATM 1790 O O   . HOH   C 3 .   ? -6.26682  -11.48688 -10.03500 1.000 23.37691 ?  533 HOH   A O   1 
HETATM 1791 O O   . HOH   C 3 .   ? -11.74280 -0.44414  -15.23204 1.000 24.68042 ?  534 HOH   A O   1 
HETATM 1792 O O   . HOH   C 3 .   ? -19.49867 -10.17349 -32.82355 1.000 42.51762 ?  535 HOH   A O   1 
HETATM 1793 O O   . HOH   C 3 .   ? -5.95746  -24.38593 -30.53769 1.000 32.39538 ?  536 HOH   A O   1 
HETATM 1794 O O   . HOH   C 3 .   ? -7.34284  -22.43856 -36.59731 1.000 33.66212 ?  537 HOH   A O   1 
HETATM 1795 O O   . HOH   C 3 .   ? 14.24465  -24.08370 -17.33560 1.000 41.47962 ?  538 HOH   A O   1 
HETATM 1796 O O   . HOH   C 3 .   ? -7.64005  -24.36343 -23.12362 1.000 27.16334 ?  539 HOH   A O   1 
HETATM 1797 O O   . HOH   C 3 .   ? -5.46115  -7.81917  -13.03920 1.000 17.75538 ?  540 HOH   A O   1 
HETATM 1798 O O   . HOH   C 3 .   ? -1.70490  -25.75312 -4.77643  1.000 19.48748 ?  541 HOH   A O   1 
HETATM 1799 O O   . HOH   C 3 .   ? -8.53800  -28.40770 -2.10006  1.000 48.58350 ?  542 HOH   A O   1 
HETATM 1800 O O   . HOH   C 3 .   ? 13.51044  -14.12924 -26.63693 1.000 17.88908 ?  543 HOH   A O   1 
HETATM 1801 O O   . HOH   C 3 .   ? -8.68071  -18.13141 -36.55328 1.000 33.87822 ?  544 HOH   A O   1 
HETATM 1802 O O   . HOH   C 3 .   ? 4.74195   -19.01203 -40.37649 1.000 30.90265 ?  545 HOH   A O   1 
HETATM 1803 O O   . HOH   C 3 .   ? -1.56907  -32.65226 -8.28830  1.000 49.95554 ?  546 HOH   A O   1 
HETATM 1804 O O   . HOH   C 3 .   ? -8.39091  -5.26429  -6.97948  1.000 28.74048 ?  547 HOH   A O   1 
HETATM 1805 O O   . HOH   C 3 .   ? -13.46625 -26.64562 -18.06202 1.000 21.41253 ?  548 HOH   A O   1 
HETATM 1806 O O   . HOH   C 3 .   ? -6.18838  -14.12419 0.83337   1.000 22.19634 ?  549 HOH   A O   1 
HETATM 1807 O O   . HOH   C 3 .   ? -6.92723  -29.22871 -32.16683 1.000 52.01619 ?  550 HOH   A O   1 
HETATM 1808 O O   . HOH   C 3 .   ? 14.24131  -15.84030 -30.53534 1.000 27.42147 ?  551 HOH   A O   1 
HETATM 1809 O O   . HOH   C 3 .   ? 8.91614   -15.43746 -27.58864 1.000 13.92865 ?  552 HOH   A O   1 
HETATM 1810 O O   . HOH   C 3 .   ? -7.48160  7.30445   -33.30912 1.000 27.92551 ?  553 HOH   A O   1 
HETATM 1811 O O   . HOH   C 3 .   ? -15.863   6.235     -32.101   1.000 39.64035 ?  554 HOH   A O   1 
HETATM 1812 O O   . HOH   C 3 .   ? 13.75991  -20.45656 -20.66348 1.000 17.90785 ?  555 HOH   A O   1 
HETATM 1813 O O   . HOH   C 3 .   ? -2.443    -24.885   -1.199    1.000 41.81622 ?  556 HOH   A O   1 
HETATM 1814 O O   . HOH   C 3 .   ? -15.06989 -12.35465 -12.00569 1.000 26.61540 ?  557 HOH   A O   1 
HETATM 1815 O O   . HOH   C 3 .   ? -17.86575 -19.00101 -11.29566 1.000 26.64392 ?  558 HOH   A O   1 
HETATM 1816 O O   . HOH   C 3 .   ? 0.52964   -5.31494  -13.72388 1.000 36.09713 ?  559 HOH   A O   1 
HETATM 1817 O O   . HOH   C 3 .   ? 18.44796  -18.54979 -11.68193 1.000 43.63821 ?  560 HOH   A O   1 
HETATM 1818 O O   . HOH   C 3 .   ? -7.55693  -26.69347 -31.00791 1.000 33.47308 ?  561 HOH   A O   1 
HETATM 1819 O O   . HOH   C 3 .   ? -3.84878  -3.41353  -15.26944 1.000 31.61975 ?  562 HOH   A O   1 
HETATM 1820 O O   . HOH   C 3 .   ? 8.85150   -20.55065 -4.22525  1.000 23.98135 ?  563 HOH   A O   1 
HETATM 1821 O O   . HOH   C 3 .   ? -4.93599  -19.21978 -39.38933 1.000 35.39634 ?  564 HOH   A O   1 
HETATM 1822 O O   . HOH   C 3 .   ? 15.67355  -18.33652 -3.54477  1.000 27.69599 ?  565 HOH   A O   1 
HETATM 1823 O O   . HOH   C 3 .   ? -5.02121  -14.31599 -22.53844 1.000 14.58403 ?  566 HOH   A O   1 
HETATM 1824 O O   . HOH   C 3 .   ? -6.40578  -7.39880  -41.82097 1.000 39.80784 ?  567 HOH   A O   1 
HETATM 1825 O O   . HOH   C 3 .   ? 8.43242   -0.36007  -17.19442 1.000 22.69675 ?  568 HOH   A O   1 
HETATM 1826 O O   . HOH   C 3 .   ? 17.03989  -17.22944 -7.38140  1.000 53.48737 ?  569 HOH   A O   1 
HETATM 1827 O O   . HOH   C 3 .   ? -17.99536 -2.86395  -34.95345 1.000 49.21165 ?  570 HOH   A O   1 
HETATM 1828 O O   . HOH   C 3 .   ? -18.22153 -25.17401 -8.88611  1.000 46.65538 ?  571 HOH   A O   1 
HETATM 1829 O O   . HOH   C 3 .   ? -19.04709 -12.37844 -16.09363 1.000 46.88975 ?  572 HOH   A O   1 
HETATM 1830 O O   . HOH   C 3 .   ? 14.16715  -9.65155  -3.99224  1.000 38.98627 ?  573 HOH   A O   1 
HETATM 1831 O O   . HOH   C 3 .   ? 2.93370   -5.73414  -6.00044  1.000 40.36950 ?  574 HOH   A O   1 
HETATM 1832 O O   . HOH   C 3 .   ? -20.605   -14.353   -18.411   1.000 41.82879 ?  575 HOH   A O   1 
HETATM 1833 O O   . HOH   C 3 .   ? -8.02853  1.70049   -36.36562 1.000 30.17250 ?  576 HOH   A O   1 
HETATM 1834 O O   . HOH   C 3 .   ? 4.04554   -26.67265 -31.72466 1.000 53.22562 ?  577 HOH   A O   1 
HETATM 1835 O O   . HOH   C 3 .   ? 9.83731   -5.88636  -1.49289  1.000 42.47672 ?  578 HOH   A O   1 
HETATM 1836 O O   . HOH   C 3 .   ? 3.91090   -7.40747  -36.26701 1.000 29.05359 ?  579 HOH   A O   1 
HETATM 1837 O O   . HOH   C 3 .   ? -17.03496 -29.06079 -17.34659 1.000 27.70041 ?  580 HOH   A O   1 
HETATM 1838 O O   . HOH   C 3 .   ? -3.49993  -20.59319 -38.74948 1.000 43.53184 ?  581 HOH   A O   1 
HETATM 1839 O O   . HOH   C 3 .   ? -20.20893 -28.11510 -10.61908 1.000 56.67879 ?  582 HOH   A O   1 
HETATM 1840 O O   . HOH   C 3 .   ? -2.53256  -30.20373 -21.19565 1.000 55.37842 ?  583 HOH   A O   1 
HETATM 1841 O O   . HOH   C 3 .   ? -17.69670 -3.75910  -28.55366 1.000 38.58310 ?  584 HOH   A O   1 
HETATM 1842 O O   . HOH   C 3 .   ? -15.22372 -11.32207 -29.57043 1.000 24.80056 ?  585 HOH   A O   1 
HETATM 1843 O O   . HOH   C 3 .   ? 3.98456   -9.26401  -20.19794 1.000 18.74201 ?  586 HOH   A O   1 
HETATM 1844 O O   . HOH   C 3 .   ? -13.56384 -18.73899 -24.40152 1.000 18.52786 ?  587 HOH   A O   1 
HETATM 1845 O O   . HOH   C 3 .   ? -16.52801 -9.45723  -14.24484 1.000 30.78974 ?  588 HOH   A O   1 
HETATM 1846 O O   . HOH   C 3 .   ? 17.23681  -22.45705 -15.23322 1.000 38.50222 ?  589 HOH   A O   1 
HETATM 1847 O O   . HOH   C 3 .   ? -3.00752  -1.19234  -23.81070 1.000 21.31251 ?  590 HOH   A O   1 
HETATM 1848 O O   . HOH   C 3 .   ? 11.39864  -1.80532  -20.22029 1.000 25.16209 ?  591 HOH   A O   1 
HETATM 1849 O O   . HOH   C 3 .   ? -15.77578 -1.31801  -27.45217 1.000 50.35170 ?  592 HOH   A O   1 
HETATM 1850 O O   . HOH   C 3 .   ? -1.14625  -29.70534 -17.95922 1.000 32.39459 ?  593 HOH   A O   1 
HETATM 1851 O O   . HOH   C 3 .   ? -4.60199  0.39014   -30.21502 1.000 26.49952 ?  594 HOH   A O   1 
HETATM 1852 O O   . HOH   C 3 .   ? 1.95296   -4.00281  -16.98353 1.000 34.82799 ?  595 HOH   A O   1 
HETATM 1853 O O   . HOH   C 3 .   ? 1.43602   -3.04450  -24.29680 1.000 27.18146 ?  596 HOH   A O   1 
HETATM 1854 O O   . HOH   C 3 .   ? 4.99399   -10.05041 -2.41213  1.000 32.01331 ?  597 HOH   A O   1 
HETATM 1855 O O   . HOH   C 3 .   ? 10.64547  -25.50776 -26.72551 1.000 22.66544 ?  598 HOH   A O   1 
HETATM 1856 O O   . HOH   C 3 .   ? 6.52301   1.05549   -7.16100  1.000 50.49747 ?  599 HOH   A O   1 
HETATM 1857 O O   . HOH   C 3 .   ? -10.61790 -20.06059 -27.77961 1.000 42.85265 ?  600 HOH   A O   1 
HETATM 1858 O O   . HOH   C 3 .   ? 7.40058   -4.56631  -22.02171 1.000 22.72707 ?  601 HOH   A O   1 
HETATM 1859 O O   . HOH   C 3 .   ? 10.99411  -11.66090 -4.73909  1.000 25.85350 ?  602 HOH   A O   1 
HETATM 1860 O O   . HOH   C 3 .   ? -0.33774  -6.95530  -30.93316 1.000 33.46744 ?  603 HOH   A O   1 
HETATM 1861 O O   . HOH   C 3 .   ? -2.00716  -0.34170  -18.83147 1.000 36.16524 ?  604 HOH   A O   1 
HETATM 1862 O O   . HOH   C 3 .   ? -17.38988 -16.48542 -23.87129 1.000 33.17636 ?  605 HOH   A O   1 
HETATM 1863 O O   . HOH   C 3 .   ? -10.27840 -15.10782 -28.23268 1.000 22.15692 ?  606 HOH   A O   1 
HETATM 1864 O O   . HOH   C 3 .   ? 4.98382   -30.67747 -11.63834 1.000 43.35837 ?  607 HOH   A O   1 
HETATM 1865 O O   . HOH   C 3 .   ? -13.52092 -31.23308 -12.64522 1.000 43.23205 ?  608 HOH   A O   1 
HETATM 1866 O O   . HOH   C 3 .   ? 14.77554  -0.52082  -18.66316 1.000 35.27060 ?  609 HOH   A O   1 
HETATM 1867 O O   . HOH   C 3 .   ? 18.55309  -9.41953  -29.50107 1.000 53.66185 ?  610 HOH   A O   1 
HETATM 1868 O O   . HOH   C 3 .   ? -3.36997  -13.17974 -20.60398 1.000 18.60843 ?  611 HOH   A O   1 
HETATM 1869 O O   . HOH   C 3 .   ? -18.51499 -12.65047 -13.77439 1.000 44.31326 ?  612 HOH   A O   1 
HETATM 1870 O O   . HOH   C 3 .   ? 10.89730  -10.34670 -36.01840 1.000 34.44702 ?  613 HOH   A O   1 
HETATM 1871 O O   . HOH   C 3 .   ? 18.52555  -15.98784 -13.29919 1.000 35.76191 ?  614 HOH   A O   1 
HETATM 1872 O O   . HOH   C 3 .   ? 17.39667  -24.59624 -25.19866 1.000 24.93985 ?  615 HOH   A O   1 
HETATM 1873 O O   . HOH   C 3 .   ? -13.48894 -26.10286 -7.85544  1.000 22.63479 ?  616 HOH   A O   1 
HETATM 1874 O O   . HOH   C 3 .   ? 13.30081  -6.61334  -25.98096 1.000 20.42002 ?  617 HOH   A O   1 
HETATM 1875 O O   . HOH   C 3 .   ? -17.64245 -15.35064 -13.05788 1.000 24.54751 ?  618 HOH   A O   1 
HETATM 1876 O O   . HOH   C 3 .   ? -9.441    -30.594   -23.492   1.000 38.51874 ?  619 HOH   A O   1 
HETATM 1877 O O   . HOH   C 3 .   ? -2.24762  -15.89670 -0.17975  1.000 30.34494 ?  620 HOH   A O   1 
HETATM 1878 O O   . HOH   C 3 .   ? 4.15521   -11.44926 -38.27709 1.000 25.49460 ?  621 HOH   A O   1 
HETATM 1879 O O   . HOH   C 3 .   ? 20.87118  -14.08253 -26.57561 1.000 31.33795 ?  622 HOH   A O   1 
HETATM 1880 O O   . HOH   C 3 .   ? -16.77518 -20.59695 -4.97196  1.000 34.53864 ?  623 HOH   A O   1 
HETATM 1881 O O   . HOH   C 3 .   ? -15.75125 -25.63437 -10.85013 1.000 28.85620 ?  624 HOH   A O   1 
HETATM 1882 O O   . HOH   C 3 .   ? -12.79021 -26.45778 -27.06837 1.000 36.12630 ?  625 HOH   A O   1 
HETATM 1883 O O   . HOH   C 3 .   ? 12.43716  -27.47089 -19.87558 1.000 38.98809 ?  626 HOH   A O   1 
HETATM 1884 O O   . HOH   C 3 .   ? 8.54310   -19.65269 -41.26355 1.000 47.01899 ?  627 HOH   A O   1 
HETATM 1885 O O   . HOH   C 3 .   ? -5.01945  -31.90403 -7.32332  1.000 40.10318 ?  628 HOH   A O   1 
HETATM 1886 O O   . HOH   C 3 .   ? -0.05238  -16.83775 -3.42563  1.000 20.59800 ?  629 HOH   A O   1 
HETATM 1887 O O   . HOH   C 3 .   ? 4.83107   -1.23822  -5.78241  1.000 46.64319 ?  630 HOH   A O   1 
HETATM 1888 O O   . HOH   C 3 .   ? -19.624   -14.676   -20.280   1.000 50.44117 ?  631 HOH   A O   1 
HETATM 1889 O O   . HOH   C 3 .   ? -18.01904 -5.80609  -25.31007 1.000 28.41264 ?  632 HOH   A O   1 
HETATM 1890 O O   . HOH   C 3 .   ? -12.98415 -12.29775 -30.85201 1.000 22.05096 ?  633 HOH   A O   1 
HETATM 1891 O O   . HOH   C 3 .   ? 1.02293   -5.90251  -34.00779 1.000 45.78101 ?  634 HOH   A O   1 
HETATM 1892 O O   . HOH   C 3 .   ? -14.01272 -24.23778 -4.91561  1.000 25.99297 ?  635 HOH   A O   1 
HETATM 1893 O O   . HOH   C 3 .   ? -12.21187 -27.10580 -20.37193 1.000 23.61024 ?  636 HOH   A O   1 
HETATM 1894 O O   . HOH   C 3 .   ? 8.91413   -15.94356 -39.37344 1.000 38.95396 ?  637 HOH   A O   1 
HETATM 1895 O O   . HOH   C 3 .   ? -14.45323 -3.39746  -12.70049 1.000 33.44461 ?  638 HOH   A O   1 
HETATM 1896 O O   . HOH   C 3 .   ? -0.47174  -12.55827 -21.19844 1.000 27.58865 ?  639 HOH   A O   1 
HETATM 1897 O O   . HOH   C 3 .   ? 2.99248   -6.80664  -20.31939 1.000 32.81733 ?  640 HOH   A O   1 
HETATM 1898 O O   . HOH   C 3 .   ? -2.24959  -26.52070 -28.29744 1.000 53.56805 ?  641 HOH   A O   1 
HETATM 1899 O O   . HOH   C 3 .   ? 15.60079  -6.88196  -27.50660 1.000 26.23167 ?  642 HOH   A O   1 
HETATM 1900 O O   . HOH   C 3 .   ? -5.793    -11.571   0.727     1.000 45.62982 ?  643 HOH   A O   1 
HETATM 1901 O O   . HOH   C 3 .   ? -12.56187 -32.13704 -19.02355 1.000 55.06465 ?  644 HOH   A O   1 
HETATM 1902 O O   . HOH   C 3 .   ? -1.99583  -26.96694 -24.76396 1.000 34.25867 ?  645 HOH   A O   1 
HETATM 1903 O O   . HOH   C 3 .   ? 1.01159   -8.87989  -3.99155  1.000 28.34508 ?  646 HOH   A O   1 
HETATM 1904 O O   . HOH   C 3 .   ? -18.33730 -15.80346 -21.24828 1.000 31.48075 ?  647 HOH   A O   1 
HETATM 1905 O O   . HOH   C 3 .   ? -1.46583  -8.57420  -27.67177 1.000 22.58028 ?  648 HOH   A O   1 
HETATM 1906 O O   . HOH   C 3 .   ? 0.99419   -9.24150  -40.26710 1.000 47.01999 ?  649 HOH   A O   1 
HETATM 1907 O O   . HOH   C 3 .   ? -15.64614 -14.48706 -33.28299 1.000 41.66687 ?  650 HOH   A O   1 
HETATM 1908 O O   . HOH   C 3 .   ? 3.04400   -4.39865  -8.77669  1.000 45.86862 ?  651 HOH   A O   1 
HETATM 1909 O O   . HOH   C 3 .   ? 4.33372   -4.88470  -21.77031 1.000 38.00109 ?  652 HOH   A O   1 
HETATM 1910 O O   . HOH   C 3 .   ? 2.22719   -25.80796 -29.34018 1.000 34.17605 ?  653 HOH   A O   1 
HETATM 1911 O O   . HOH   C 3 .   ? 2.64421   -10.06393 -23.07336 1.000 26.21391 ?  654 HOH   A O   1 
HETATM 1912 O O   . HOH   C 3 .   ? 5.632     -3.192    -26.107   1.000 32.09012 ?  655 HOH   A O   1 
HETATM 1913 O O   . HOH   C 3 .   ? 13.83948  -3.86084  -25.03905 1.000 15.80776 ?  656 HOH   A O   1 
HETATM 1914 O O   . HOH   C 3 .   ? 17.76771  -15.30387 -29.55212 1.000 43.19309 ?  657 HOH   A O   1 
HETATM 1915 O O   . HOH   C 3 .   ? -17.15392 -3.18837  -25.76273 1.000 48.44074 ?  658 HOH   A O   1 
HETATM 1916 O O   . HOH   C 3 .   ? -10.69356 -33.00418 -20.17384 1.000 49.53454 ?  659 HOH   A O   1 
HETATM 1917 O O   . HOH   C 3 .   ? -11.635   7.200     -39.332   1.000 47.67830 ?  660 HOH   A O   1 
HETATM 1918 O O   . HOH   C 3 .   ? 4.29463   -23.01326 -3.40205  1.000 31.18954 ?  661 HOH   A O   1 
HETATM 1919 O O   . HOH   C 3 .   ? -3.65851  -33.23202 -11.38885 1.000 45.95656 ?  662 HOH   A O   1 
HETATM 1920 O O   . HOH   C 3 .   ? -12.60582 -20.78569 -29.56077 1.000 41.82652 ?  663 HOH   A O   1 
HETATM 1921 O O   . HOH   C 3 .   ? 16.465    -27.642   -22.330   1.000 45.15762 ?  664 HOH   A O   1 
HETATM 1922 O O   . HOH   C 3 .   ? 1.76534   -18.67990 0.07939   1.000 27.65340 ?  665 HOH   A O   1 
HETATM 1923 O O   . HOH   C 3 .   ? 10.57963  -17.31709 -38.59379 1.000 43.28290 ?  666 HOH   A O   1 
HETATM 1924 O O   . HOH   C 3 .   ? 4.50980   -30.95884 -20.78287 1.000 46.48512 ?  667 HOH   A O   1 
HETATM 1925 O O   . HOH   C 3 .   ? 1.01456   -8.43935  -26.89764 1.000 29.49195 ?  668 HOH   A O   1 
HETATM 1926 O O   . HOH   C 3 .   ? -15.64973 0.26601   -40.81176 1.000 43.39955 ?  669 HOH   A O   1 
HETATM 1927 O O   . HOH   C 3 .   ? 8.32388   -25.82112 -25.82582 1.000 28.83467 ?  670 HOH   A O   1 
HETATM 1928 O O   . HOH   C 3 .   ? -12.18900 -16.80800 -28.27755 1.000 39.07860 ?  671 HOH   A O   1 
HETATM 1929 O O   . HOH   C 3 .   ? -13.73712 -16.25987 -26.11440 1.000 35.12989 ?  672 HOH   A O   1 
HETATM 1930 O O   . HOH   C 3 .   ? 4.92701   -1.87016  -18.27515 1.000 27.33063 ?  673 HOH   A O   1 
HETATM 1931 O O   . HOH   C 3 .   ? -1.33864  -6.03172  -12.26335 1.000 39.72385 ?  674 HOH   A O   1 
HETATM 1932 O O   . HOH   C 3 .   ? -13.92009 -29.25813 -17.08853 1.000 46.39082 ?  675 HOH   A O   1 
HETATM 1933 O O   . HOH   C 3 .   ? -10.09247 -25.23766 -38.17174 1.000 52.25373 ?  676 HOH   A O   1 
HETATM 1934 O O   . HOH   C 3 .   ? -15.693   -37.291   -15.846   1.000 50.03432 ?  677 HOH   A O   1 
HETATM 1935 O O   . HOH   C 3 .   ? 18.31146  -10.07941 -9.83819  1.000 49.01733 ?  678 HOH   A O   1 
HETATM 1936 O O   . HOH   C 3 .   ? 0.16131   -19.10759 -1.93841  1.000 29.06153 ?  679 HOH   A O   1 
HETATM 1937 O O   . HOH   C 3 .   ? -14.36109 -10.13495 -8.33103  1.000 33.21208 ?  680 HOH   A O   1 
HETATM 1938 O O   . HOH   C 3 .   ? 3.24597   -7.90776  -2.20532  1.000 46.12208 ?  681 HOH   A O   1 
HETATM 1939 O O   . HOH   C 3 .   ? -6.51257  3.68527   -34.52424 1.000 36.83355 ?  682 HOH   A O   1 
HETATM 1940 O O   . HOH   C 3 .   ? 11.92000  -23.99392 -6.75400  1.000 50.59171 ?  683 HOH   A O   1 
HETATM 1941 O O   . HOH   C 3 .   ? -12.30655 -25.86634 -3.54213  1.000 43.02288 ?  684 HOH   A O   1 
HETATM 1942 O O   . HOH   C 3 .   ? -13.94912 -14.54549 -3.01738  1.000 25.68568 ?  685 HOH   A O   1 
HETATM 1943 O O   . HOH   C 3 .   ? -21.64264 -29.40272 -12.09484 1.000 47.90373 ?  686 HOH   A O   1 
HETATM 1944 O O   . HOH   C 3 .   ? 13.620    -28.154   -27.363   1.000 52.42451 ?  687 HOH   A O   1 
HETATM 1945 O O   . HOH   C 3 .   ? -6.599    -23.197   -1.746    1.000 39.01200 ?  688 HOH   A O   1 
HETATM 1946 O O   . HOH   C 3 .   ? 14.47555  -22.00397 -16.94878 1.000 30.62702 ?  689 HOH   A O   1 
HETATM 1947 O O   . HOH   C 3 .   ? 12.278    -25.210   -38.281   1.000 26.77259 ?  690 HOH   A O   1 
HETATM 1948 O O   . HOH   C 3 .   ? -18.131   -37.182   -19.987   1.000 35.65477 ?  691 HOH   A O   1 
HETATM 1949 O O   . HOH   C 3 .   ? 1.07286   -4.91411  -29.88728 1.000 40.13951 ?  692 HOH   A O   1 
HETATM 1950 O O   . HOH   C 3 .   ? 21.96423  -5.53129  -18.37745 1.000 50.11796 ?  693 HOH   A O   1 
HETATM 1951 O O   . HOH   C 3 .   ? -10.07700 -11.83982 -39.70671 1.000 54.81974 ?  694 HOH   A O   1 
HETATM 1952 O O   . HOH   C 3 .   ? -0.77147  -29.48961 -3.48568  1.000 50.37450 ?  695 HOH   A O   1 
HETATM 1953 O O   . HOH   C 3 .   ? 17.40762  -17.77775 -9.37432  1.000 50.95814 ?  696 HOH   A O   1 
HETATM 1954 O O   . HOH   C 3 .   ? 7.85470   -13.49158 -38.05150 1.000 29.26757 ?  697 HOH   A O   1 
HETATM 1955 O O   . HOH   C 3 .   ? -0.54536  -1.33871  -22.89153 1.000 26.29231 ?  698 HOH   A O   1 
HETATM 1956 O O   . HOH   C 3 .   ? 15.32505  -12.57735 -7.02238  1.000 36.42872 ?  699 HOH   A O   1 
HETATM 1957 O O   . HOH   C 3 .   ? 6.17287   -29.71785 -25.12315 1.000 37.31583 ?  700 HOH   A O   1 
HETATM 1958 O O   . HOH   C 3 .   ? -8.27024  -20.72761 -37.61710 1.000 47.63006 ?  701 HOH   A O   1 
HETATM 1959 O O   . HOH   C 3 .   ? -11.73298 -9.35271  -39.41052 1.000 48.97046 ?  702 HOH   A O   1 
HETATM 1960 O O   . HOH   C 3 .   ? 1.57360   -3.40779  -12.49862 1.000 42.31745 ?  703 HOH   A O   1 
HETATM 1961 O O   . HOH   C 3 .   ? 12.19773  -27.67823 -23.16817 1.000 41.17608 ?  704 HOH   A O   1 
HETATM 1962 O O   . HOH   C 3 .   ? 10.422    -20.947   -42.835   1.000 52.48438 ?  705 HOH   A O   1 
HETATM 1963 O O   . HOH   C 3 .   ? -3.05791  -27.55977 -3.42097  1.000 40.13099 ?  706 HOH   A O   1 
HETATM 1964 O O   . HOH   C 3 .   ? 2.21372   -0.94271  -14.20226 1.000 50.03035 ?  707 HOH   A O   1 
HETATM 1965 O O   . HOH   C 3 .   ? 3.63718   -8.80849  -38.80412 1.000 40.61825 ?  708 HOH   A O   1 
HETATM 1966 O O   . HOH   C 3 .   ? -16.293   -0.745    -16.859   1.000 41.79338 ?  709 HOH   A O   1 
HETATM 1967 O O   . HOH   C 3 .   ? 10.93996  -1.25426  -17.15319 1.000 25.34451 ?  710 HOH   A O   1 
HETATM 1968 O O   . HOH   C 3 .   ? 5.34641   1.58422   -16.52740 1.000 31.53244 ?  711 HOH   A O   1 
HETATM 1969 O O   . HOH   C 3 .   ? -13.736   -0.944    -13.412   1.000 32.52795 ?  712 HOH   A O   1 
HETATM 1970 O O   . HOH   C 3 .   ? -9.74374  -26.18374 -20.88678 1.000 22.83673 ?  713 HOH   A O   1 
HETATM 1971 O O   . HOH   C 3 .   ? -7.987    7.495     -38.047   1.000 38.32791 ?  714 HOH   A O   1 
HETATM 1972 O O   . HOH   C 3 .   ? 0.935     -0.754    -28.211   1.000 58.66264 ?  715 HOH   A O   1 
HETATM 1973 O O   . HOH   C 3 .   ? -10.76751 -9.06490  -1.55423  1.000 31.61367 ?  716 HOH   A O   1 
HETATM 1974 O O   . HOH   C 3 .   ? 19.23843  -8.40365  -17.39538 1.000 36.50653 ?  717 HOH   A O   1 
HETATM 1975 O O   . HOH   C 3 .   ? 3.85919   -0.20956  -16.53499 1.000 39.68100 ?  718 HOH   A O   1 
HETATM 1976 O O   . HOH   C 3 .   ? 10.11461  -29.17878 -23.72099 1.000 48.38193 ?  719 HOH   A O   1 
HETATM 1977 O O   . HOH   C 3 .   ? -16.553   -18.189   -3.121    1.000 45.56381 ?  720 HOH   A O   1 
HETATM 1978 O O   . HOH   C 3 .   ? 6.75776   -21.63966 -2.68315  1.000 29.84281 ?  721 HOH   A O   1 
HETATM 1979 O O   . HOH   C 3 .   ? 0.97623   -11.96390 -23.45119 1.000 34.10546 ?  722 HOH   A O   1 
HETATM 1980 O O   . HOH   C 3 .   ? 20.805    -19.501   -11.868   1.000 51.43713 ?  723 HOH   A O   1 
HETATM 1981 O O   . HOH   C 3 .   ? -6.267    6.823     -35.673   1.000 34.08115 ?  724 HOH   A O   1 
HETATM 1982 O O   . HOH   C 3 .   ? -10.537   -22.797   4.419     1.000 39.56960 ?  725 HOH   A O   1 
HETATM 1983 O O   . HOH   C 3 .   ? -16.19375 -13.53544 -3.69971  1.000 39.43120 ?  726 HOH   A O   1 
HETATM 1984 O O   . HOH   C 3 .   ? 5.65014   -2.93301  -23.43015 1.000 29.57986 ?  727 HOH   A O   1 
HETATM 1985 O O   . HOH   C 3 .   ? -2.16725  -1.07629  -30.63547 1.000 35.66344 ?  728 HOH   A O   1 
HETATM 1986 O O   . HOH   C 3 .   ? 5.93673   -12.74553 -39.70451 1.000 32.65862 ?  729 HOH   A O   1 
HETATM 1987 O O   . HOH   C 3 .   ? -2.05226  -12.12344 -22.37964 1.000 42.72569 ?  730 HOH   A O   1 
HETATM 1988 O O   . HOH   C 3 .   ? -4.516    -25.208   -0.920    1.000 47.84028 ?  731 HOH   A O   1 
HETATM 1989 O O   . HOH   C 3 .   ? 2.285     -0.804    -25.783   1.000 30.80267 ?  732 HOH   A O   1 
HETATM 1990 O O   . HOH   C 3 .   ? -9.397    -32.494   -24.408   1.000 49.17061 ?  733 HOH   A O   1 
HETATM 1991 O O   . HOH   C 3 .   ? -6.99613  -30.92683 -9.23408  1.000 30.52143 ?  734 HOH   A O   1 
HETATM 1992 O O   . HOH   C 3 .   ? 9.99700   -30.60452 -21.40918 1.000 53.29852 ?  735 HOH   A O   1 
HETATM 1993 O O   . HOH   C 3 .   ? -22.426   -32.095   -13.368   1.000 41.86935 ?  736 HOH   A O   1 
HETATM 1994 O O   . HOH   C 3 .   ? 4.89713   -28.22795 -31.11204 1.000 45.99967 ?  737 HOH   A O   1 
HETATM 1995 O O   . HOH   C 3 .   ? 20.52403  -5.75985  -20.77784 1.000 41.33651 ?  738 HOH   A O   1 
HETATM 1996 O O   . HOH   C 3 .   ? 10.88635  -27.80714 -27.74781 1.000 35.31602 ?  739 HOH   A O   1 
HETATM 1997 O O   . HOH   C 3 .   ? -11.69646 -20.60259 -25.36032 1.000 28.92829 ?  740 HOH   A O   1 
HETATM 1998 O O   . HOH   C 3 .   ? 12.70730  -25.09434 -15.83814 1.000 36.55086 ?  741 HOH   A O   1 
HETATM 1999 O O   . HOH   C 3 .   ? -0.79250  -10.69127 -23.70579 1.000 39.80883 ?  742 HOH   A O   1 
HETATM 2000 O O   . HOH   C 3 .   ? -20.65143 -11.29475 -19.44191 1.000 42.78774 ?  743 HOH   A O   1 
HETATM 2001 O O   . HOH   C 3 .   ? -21.363   -14.896   -15.711   1.000 39.23502 ?  744 HOH   A O   1 
HETATM 2002 O O   . HOH   C 3 .   ? -0.00000  -0.00000  -18.44473 0.50  22.15222 ?  745 HOH   A O   1 
HETATM 2003 O O   . HOH   C 3 .   ? -18.150   -15.925   -3.278    1.000 47.20505 ?  746 HOH   A O   1 
HETATM 2004 O O   . HOH   C 3 .   ? 20.18951  -7.79157  -15.38908 1.000 49.70693 ?  747 HOH   A O   1 
HETATM 2005 O O   . HOH   C 3 .   ? 5.04270   -14.60745 -41.31795 1.000 40.25434 ?  748 HOH   A O   1 
HETATM 2006 O O   . HOH   C 3 .   ? -16.29364 -12.92371 -6.32032  1.000 37.44417 ?  749 HOH   A O   1 
HETATM 2007 O O   . HOH   C 3 .   ? -17.344   4.366     -31.375   1.000 48.40034 ?  750 HOH   A O   1 
HETATM 2008 O O   . HOH   C 3 .   ? -16.273   3.130     -25.943   1.000 39.60574 ?  751 HOH   A O   1 
HETATM 2009 O O   . HOH   C 3 .   ? 9.11736   -29.48621 -31.08504 1.000 49.51843 ?  752 HOH   A O   1 
HETATM 2010 O O   . HOH   C 3 .   ? -2.127    -22.941   0.990     1.000 41.72619 ?  753 HOH   A O   1 
HETATM 2011 O O   . HOH   C 3 .   ? 4.400     -3.511    -33.995   1.000 38.59237 ?  754 HOH   A O   1 
HETATM 2012 O O   . HOH   C 3 .   ? -16.56463 -13.56280 -28.81670 1.000 40.72220 ?  755 HOH   A O   1 
HETATM 2013 O O   . HOH   C 3 .   ? 2.931     -1.963    -20.484   1.000 40.60406 ?  756 HOH   A O   1 
HETATM 2014 O O   . HOH   C 3 .   ? -4.16888  1.81212   -27.72687 1.000 35.44223 ?  757 HOH   A O   1 
HETATM 2015 O O   . HOH   C 3 .   ? -9.12261  -28.43757 -24.72077 1.000 38.60629 ?  758 HOH   A O   1 
HETATM 2016 O O   . HOH   C 3 .   ? -15.125   -18.886   -1.232    1.000 43.90515 ?  759 HOH   A O   1 
HETATM 2017 O O   . HOH   C 3 .   ? 8.16352   -28.93578 -27.74512 1.000 43.98724 ?  760 HOH   A O   1 
HETATM 2018 O O   . HOH   C 3 .   ? 0.65227   -1.42590  -16.73445 1.000 36.98854 ?  761 HOH   A O   1 
HETATM 2019 O O   . HOH   C 3 .   ? -19.35693 -2.94940  -30.46923 1.000 49.94236 ?  762 HOH   A O   1 
HETATM 2020 O O   . HOH   C 3 .   ? -11.18715 -27.00819 -24.86773 1.000 38.31332 ?  763 HOH   A O   1 
HETATM 2021 O O   . HOH   C 3 .   ? 14.50012  -13.29338 -2.91248  1.000 31.53530 ?  764 HOH   A O   1 
HETATM 2022 O O   . HOH   C 3 .   ? 10.88606  -29.83823 -18.98286 1.000 52.33716 ?  765 HOH   A O   1 
HETATM 2023 O O   . HOH   C 3 .   ? 9.89404   -25.07903 -14.87584 1.000 39.37982 ?  766 HOH   A O   1 
HETATM 2024 O O   . HOH   C 3 .   ? -12.24462 -13.40579 -0.96230  1.000 22.22784 ?  767 HOH   A O   1 
HETATM 2025 O O   . HOH   C 3 .   ? 14.952    -17.021   0.368     1.000 34.41665 ?  768 HOH   A O   1 
HETATM 2026 O O   . HOH   C 3 .   ? -16.87491 -15.88103 -10.38373 1.000 28.66848 ?  769 HOH   A O   1 
HETATM 2027 O O   . HOH   C 3 .   ? -14.43348 -14.38875 -10.24711 1.000 27.26217 ?  770 HOH   A O   1 
HETATM 2028 O O   . HOH   C 3 .   ? 13.62372  -11.82756 -5.07097  1.000 26.43491 ?  771 HOH   A O   1 
HETATM 2029 O O   . HOH   C 3 .   ? -20.61919 -10.58692 -16.93993 1.000 47.87980 ?  772 HOH   A O   1 
HETATM 2030 O O   . HOH   C 3 .   ? -10.355   -12.026   2.013     1.000 25.80870 ?  773 HOH   A O   1 
HETATM 2031 O O   . HOH   C 3 .   ? -14.67027 -9.54888  -11.49608 1.000 35.34598 ?  774 HOH   A O   1 
HETATM 2032 O O   . HOH   C 3 .   ? -19.03390 -8.38289  -15.12176 1.000 48.78746 ?  775 HOH   A O   1 
HETATM 2033 O O   . HOH   C 3 .   ? 17.34294  -4.62628  -27.78650 1.000 40.45663 ?  776 HOH   A O   1 
HETATM 2034 O O   . HOH   C 3 .   ? -9.621    8.860     -37.991   1.000 42.74295 ?  777 HOH   A O   1 
HETATM 2035 O O   . HOH   C 3 .   ? -8.74914  -11.03061 -0.02711  1.000 34.13501 ?  778 HOH   A O   1 
HETATM 2036 O O   . HOH   C 3 .   ? -8.79760  -32.93754 -8.88886  1.000 39.86148 ?  779 HOH   A O   1 
HETATM 2037 O O   . HOH   C 3 .   ? -17.40089 2.47802   -41.04492 1.000 51.70387 ?  780 HOH   A O   1 
HETATM 2038 O O   . HOH   C 3 .   ? -8.54804  -28.81618 -27.41995 1.000 44.61094 ?  781 HOH   A O   1 
HETATM 2039 O O   . HOH   C 3 .   ? 16.21968  -19.50292 -0.57483  1.000 51.07147 ?  782 HOH   A O   1 
HETATM 2040 O O   . HOH   C 3 .   ? 17.13568  -11.52080 -7.74492  1.000 46.27325 ?  783 HOH   A O   1 
HETATM 2041 O O   . HOH   C 3 .   ? 5.89476   -8.31973  -39.40062 1.000 43.59845 ?  784 HOH   A O   1 
HETATM 2042 O O   . HOH   C 3 .   ? -9.94199  -20.76873 -39.33584 1.000 45.95454 ?  785 HOH   A O   1 
HETATM 2043 O O   . HOH   C 3 .   ? -22.75380 -10.74787 -15.15229 1.000 48.88798 ?  786 HOH   A 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   . GLU A 9   ? 0.61216 0.82311 0.50719 -0.10505 -0.02207 -0.22887 16  GLU A N   
2    C CA  . GLU A 9   ? 0.62446 0.80871 0.51250 -0.06686 -0.02780 -0.21032 16  GLU A CA  
3    C C   . GLU A 9   ? 0.50834 0.68667 0.41361 -0.05354 -0.02908 -0.19101 16  GLU A C   
4    O O   . GLU A 9   ? 0.46598 0.70625 0.39866 -0.03704 -0.03474 -0.18163 16  GLU A O   
5    C CB  . GLU A 9   ? 0.76103 1.01150 0.66135 -0.03544 -0.03661 -0.20701 16  GLU A CB  
6    C CG  . GLU A 9   ? 0.87946 1.09405 0.75995 -0.00324 -0.03783 -0.19611 16  GLU A CG  
7    C CD  . GLU A 9   ? 0.84678 1.05047 0.73795 0.03010  -0.03910 -0.17081 16  GLU A CD  
8    O OE1 . GLU A 9   ? 0.91639 1.15548 0.83136 0.03621  -0.04175 -0.16072 16  GLU A OE1 
9    O OE2 . GLU A 9   ? 0.86315 1.02432 0.73844 0.05178  -0.03610 -0.16049 16  GLU A OE2 
10   N N   . VAL A 10  ? 0.47780 0.58064 0.36469 -0.05783 -0.02236 -0.18499 17  VAL A N   
11   C CA  . VAL A 10  ? 0.37254 0.46381 0.27334 -0.05188 -0.02214 -0.17047 17  VAL A CA  
12   C C   . VAL A 10  ? 0.40451 0.46951 0.30137 -0.01636 -0.02377 -0.15460 17  VAL A C   
13   O O   . VAL A 10  ? 0.39644 0.40620 0.27005 -0.00823 -0.01735 -0.15195 17  VAL A O   
14   C CB  . VAL A 10  ? 0.43149 0.46021 0.31754 -0.08019 -0.01057 -0.17272 17  VAL A CB  
15   C CG1 . VAL A 10  ? 0.40917 0.42849 0.30967 -0.07282 -0.01072 -0.15773 17  VAL A CG1 
16   C CG2 . VAL A 10  ? 0.55768 0.61196 0.44820 -0.11527 -0.00519 -0.18796 17  VAL A CG2 
17   N N   . GLU A 11  ? 0.28025 0.37839 0.20297 0.00758  -0.02917 -0.13395 18  GLU A N   
18   C CA  . GLU A 11  ? 0.28069 0.35176 0.20953 0.03782  -0.02709 -0.10802 18  GLU A CA  
19   C C   . GLU A 11  ? 0.25676 0.29354 0.19533 0.03168  -0.02322 -0.09427 18  GLU A C   
20   O O   . GLU A 11  ? 0.23227 0.28999 0.18500 0.01940  -0.02506 -0.09500 18  GLU A O   
21   C CB  . GLU A 11  ? 0.23139 0.35004 0.17497 0.06674  -0.03090 -0.09457 18  GLU A CB  
22   C CG  . GLU A 11  ? 0.24500 0.39822 0.17576 0.08226  -0.03415 -0.10380 18  GLU A CG  
23   C CD  . GLU A 11  ? 0.35837 0.55265 0.29650 0.11528  -0.03413 -0.08740 18  GLU A CD  
24   O OE1 . GLU A 11  ? 0.34168 0.58036 0.28867 0.11793  -0.03728 -0.08848 18  GLU A OE1 
25   O OE2 . GLU A 11  ? 0.43555 0.61882 0.36628 0.14018  -0.02928 -0.07401 18  GLU A OE2 
26   N N   . THR A 12  ? 0.25413 0.24486 0.18460 0.04253  -0.01801 -0.08186 19  THR A N   
27   C CA  . THR A 12  ? 0.24281 0.20888 0.18157 0.04206  -0.01516 -0.06809 19  THR A CA  
28   C C   . THR A 12  ? 0.22027 0.19951 0.17747 0.06416  -0.01561 -0.04917 19  THR A C   
29   O O   . THR A 12  ? 0.22782 0.20440 0.18044 0.08131  -0.01348 -0.04338 19  THR A O   
30   C CB  . THR A 12  ? 0.28181 0.19023 0.19288 0.03952  -0.00706 -0.06889 19  THR A CB  
31   O OG1 . THR A 12  ? 0.32267 0.20719 0.20953 0.01439  -0.00185 -0.08860 19  THR A OG1 
32   C CG2 . THR A 12  ? 0.27343 0.16437 0.19042 0.04175  -0.00469 -0.05537 19  THR A CG2 
33   N N   . PHE A 13  ? 0.19704 0.18777 0.17262 0.06148  -0.01649 -0.04076 20  PHE A N   
34   C CA  . PHE A 13  ? 0.19846 0.19915 0.19004 0.07392  -0.01399 -0.02637 20  PHE A CA  
35   C C   . PHE A 13  ? 0.20784 0.19565 0.20679 0.06824  -0.01312 -0.02004 20  PHE A C   
36   O O   . PHE A 13  ? 0.20727 0.18460 0.20311 0.05578  -0.01485 -0.02419 20  PHE A O   
37   C CB  . PHE A 13  ? 0.16715 0.19296 0.16915 0.07660  -0.01349 -0.02349 20  PHE A CB  
38   C CG  . PHE A 13  ? 0.17428 0.22564 0.16854 0.08799  -0.01464 -0.02827 20  PHE A CG  
39   C CD1 . PHE A 13  ? 0.20964 0.28409 0.19877 0.07827  -0.02073 -0.04317 20  PHE A CD1 
40   C CD2 . PHE A 13  ? 0.20659 0.26255 0.19751 0.10786  -0.00824 -0.01822 20  PHE A CD2 
41   C CE1 . PHE A 13  ? 0.20094 0.31077 0.18286 0.09107  -0.02296 -0.04896 20  PHE A CE1 
42   C CE2 . PHE A 13  ? 0.22482 0.30456 0.20307 0.11893  -0.00872 -0.01999 20  PHE A CE2 
43   C CZ  . PHE A 13  ? 0.23708 0.35123 0.21357 0.11733  -0.01741 -0.03656 20  PHE A CZ  
44   N N   . ALA A 14  ? 0.18243 0.17588 0.19098 0.07634  -0.00962 -0.01076 21  ALA A N   
45   C CA  . ALA A 14  ? 0.17223 0.16829 0.19088 0.07070  -0.00958 -0.00660 21  ALA A CA  
46   C C   . ALA A 14  ? 0.17795 0.18267 0.20914 0.06140  -0.00751 -0.00565 21  ALA A C   
47   O O   . ALA A 14  ? 0.17824 0.18710 0.21187 0.06495  -0.00150 -0.00262 21  ALA A O   
48   C CB  . ALA A 14  ? 0.19725 0.20757 0.22185 0.07992  -0.00630 -0.00059 21  ALA A CB  
49   N N   . PHE A 15  ? 0.17210 0.17455 0.20635 0.05154  -0.01042 -0.00750 22  PHE A N   
50   C CA  . PHE A 15  ? 0.17663 0.18335 0.21950 0.04423  -0.00630 -0.00663 22  PHE A CA  
51   C C   . PHE A 15  ? 0.13697 0.15232 0.18851 0.04111  0.00065  -0.00439 22  PHE A C   
52   O O   . PHE A 15  ? 0.17344 0.20370 0.22970 0.04314  -0.00134 -0.00395 22  PHE A O   
53   C CB  . PHE A 15  ? 0.15163 0.15742 0.19609 0.03481  -0.01046 -0.00924 22  PHE A CB  
54   C CG  . PHE A 15  ? 0.14021 0.14095 0.17802 0.03157  -0.01410 -0.01253 22  PHE A CG  
55   C CD1 . PHE A 15  ? 0.15995 0.16766 0.19762 0.03269  -0.01210 -0.01372 22  PHE A CD1 
56   C CD2 . PHE A 15  ? 0.15531 0.14535 0.18395 0.02828  -0.01719 -0.01433 22  PHE A CD2 
57   C CE1 . PHE A 15  ? 0.14479 0.16163 0.17946 0.02709  -0.01537 -0.01884 22  PHE A CE1 
58   C CE2 . PHE A 15  ? 0.15784 0.14445 0.18001 0.01876  -0.01778 -0.01960 22  PHE A CE2 
59   C CZ  . PHE A 15  ? 0.14911 0.15592 0.17771 0.01645  -0.01794 -0.02294 22  PHE A CZ  
60   N N   . GLN A 16  ? 0.16437 0.17082 0.21515 0.03590  0.01062  -0.00362 23  GLN A N   
61   C CA  . GLN A 16  ? 0.19953 0.21100 0.25715 0.02212  0.02019  -0.00596 23  GLN A CA  
62   C C   . GLN A 16  ? 0.18675 0.21896 0.25413 0.01087  0.01258  -0.01258 23  GLN A C   
63   O O   . GLN A 16  ? 0.17218 0.19989 0.23652 0.01142  0.00513  -0.01408 23  GLN A O   
64   C CB  . GLN A 16  ? 0.22638 0.20881 0.27171 0.01665  0.03559  -0.00524 23  GLN A CB  
65   C CG  . GLN A 16  ? 0.27600 0.23915 0.30641 0.03289  0.04656  0.00359  23  GLN A CG  
66   C CD  . GLN A 16  ? 0.43934 0.36363 0.44777 0.03296  0.06533  0.00636  23  GLN A CD  
67   O OE1 . GLN A 16  ? 0.44935 0.36352 0.44472 0.04788  0.06441  0.00963  23  GLN A OE1 
68   N NE2 . GLN A 16  ? 0.49340 0.39526 0.49466 0.01599  0.08488  0.00460  23  GLN A NE2 
69   N N   . ALA A 17  ? 0.17771 0.23930 0.25651 0.00191  0.01461  -0.01665 24  ALA A N   
70   C CA  . ALA A 17  ? 0.13618 0.23059 0.22331 -0.00383 0.00616  -0.02310 24  ALA A CA  
71   C C   . ALA A 17  ? 0.16115 0.24285 0.24442 -0.01720 0.00649  -0.02997 24  ALA A C   
72   O O   . ALA A 17  ? 0.16905 0.26113 0.25081 -0.01185 -0.00357 -0.03064 24  ALA A O   
73   C CB  . ALA A 17  ? 0.19516 0.33469 0.29695 -0.01592 0.01093  -0.02977 24  ALA A CB  
74   N N   . GLU A 18  ? 0.19348 0.24784 0.27027 -0.03234 0.02000  -0.03426 25  GLU A N   
75   C CA  . GLU A 18  ? 0.20469 0.24268 0.27330 -0.04353 0.02210  -0.04153 25  GLU A CA  
76   C C   . GLU A 18  ? 0.19248 0.21374 0.25303 -0.02665 0.01286  -0.03439 25  GLU A C   
77   O O   . GLU A 18  ? 0.21454 0.24003 0.27279 -0.02998 0.00746  -0.03883 25  GLU A O   
78   C CB  . GLU A 18  ? 0.28741 0.28430 0.34055 -0.05840 0.04301  -0.04554 25  GLU A CB  
79   C CG  . GLU A 18  ? 0.29926 0.31320 0.35958 -0.08499 0.05563  -0.05665 25  GLU A CG  
80   C CD  . GLU A 18  ? 0.36006 0.37680 0.42482 -0.07883 0.06286  -0.04809 25  GLU A CD  
81   O OE1 . GLU A 18  ? 0.31510 0.32180 0.37699 -0.05271 0.05654  -0.03433 25  GLU A OE1 
82   O OE2 . GLU A 18  ? 0.43829 0.46955 0.50877 -0.10250 0.07623  -0.05663 25  GLU A OE2 
83   N N   . ILE A 19  ? 0.19430 0.20067 0.25011 -0.01016 0.01165  -0.02475 26  ILE A N   
84   C CA  . ILE A 19  ? 0.16847 0.16680 0.21813 0.00035  0.00484  -0.02085 26  ILE A CA  
85   C C   . ILE A 19  ? 0.18144 0.19712 0.23553 0.00434  -0.00748 -0.01972 26  ILE A C   
86   O O   . ILE A 19  ? 0.19205 0.20662 0.24216 0.00407  -0.01186 -0.02004 26  ILE A O   
87   C CB  . ILE A 19  ? 0.20639 0.19254 0.24863 0.01450  0.00831  -0.01421 26  ILE A CB  
88   C CG1 . ILE A 19  ? 0.23159 0.19219 0.25832 0.01908  0.02305  -0.01208 26  ILE A CG1 
89   C CG2 . ILE A 19  ? 0.19313 0.18755 0.23411 0.02081  -0.00072 -0.01324 26  ILE A CG2 
90   C CD1 . ILE A 19  ? 0.30596 0.24624 0.32684 0.00773  0.03860  -0.01427 26  ILE A CD1 
91   N N   . ALA A 20  ? 0.14332 0.17231 0.20160 0.00987  -0.01085 -0.01753 27  ALA A N   
92   C CA  . ALA A 20  ? 0.14355 0.18031 0.19698 0.01794  -0.01823 -0.01492 27  ALA A CA  
93   C C   . ALA A 20  ? 0.15325 0.20942 0.20831 0.01310  -0.02140 -0.01907 27  ALA A C   
94   O O   . ALA A 20  ? 0.15940 0.21134 0.20433 0.01930  -0.02509 -0.01598 27  ALA A O   
95   C CB  . ALA A 20  ? 0.14779 0.19756 0.20145 0.02960  -0.01908 -0.01139 27  ALA A CB  
96   N N   . GLN A 21  ? 0.12071 0.19685 0.18575 0.00025  -0.01828 -0.02721 28  GLN A N   
97   C CA  . GLN A 21  ? 0.12192 0.22425 0.18815 -0.00597 -0.02213 -0.03457 28  GLN A CA  
98   C C   . GLN A 21  ? 0.18201 0.26128 0.23967 -0.01107 -0.02136 -0.03621 28  GLN A C   
99   O O   . GLN A 21  ? 0.18407 0.27466 0.23555 -0.00625 -0.02676 -0.03618 28  GLN A O   
100  C CB  . GLN A 21  ? 0.13783 0.27075 0.21621 -0.02517 -0.01722 -0.04740 28  GLN A CB  
101  C CG  . GLN A 21  ? 0.24054 0.41890 0.32179 -0.03191 -0.02332 -0.05872 28  GLN A CG  
102  C CD  . GLN A 21  ? 0.25366 0.46898 0.34799 -0.05896 -0.01673 -0.07628 28  GLN A CD  
103  O OE1 . GLN A 21  ? 0.34725 0.54495 0.44583 -0.07142 -0.00570 -0.07734 28  GLN A OE1 
104  N NE2 . GLN A 21  ? 0.37972 0.63701 0.47316 -0.06548 -0.02032 -0.08724 28  GLN A NE2 
105  N N   . LEU A 22  ? 0.17241 0.22133 0.22689 -0.01726 -0.01354 -0.03663 29  LEU A N   
106  C CA  . LEU A 22  ? 0.17925 0.20884 0.22404 -0.01685 -0.01205 -0.03626 29  LEU A CA  
107  C C   . LEU A 22  ? 0.18877 0.21756 0.22909 -0.00613 -0.01856 -0.02813 29  LEU A C   
108  O O   . LEU A 22  ? 0.18511 0.21597 0.21902 -0.00580 -0.02060 -0.02837 29  LEU A O   
109  C CB  . LEU A 22  ? 0.23512 0.23614 0.27319 -0.01487 -0.00201 -0.03391 29  LEU A CB  
110  C CG  . LEU A 22  ? 0.25388 0.24227 0.28130 -0.00853 0.00026  -0.03183 29  LEU A CG  
111  C CD1 . LEU A 22  ? 0.28422 0.26560 0.30274 -0.01804 0.00480  -0.04091 29  LEU A CD1 
112  C CD2 . LEU A 22  ? 0.24465 0.21542 0.26299 0.00324  0.00925  -0.02645 29  LEU A CD2 
113  N N   . MET A 23  ? 0.15426 0.17615 0.19492 0.00084  -0.01963 -0.02172 30  MET A N   
114  C CA  . MET A 23  ? 0.16809 0.18075 0.20008 0.00481  -0.02133 -0.01642 30  MET A CA  
115  C C   . MET A 23  ? 0.16995 0.18703 0.19198 0.01155  -0.02407 -0.01289 30  MET A C   
116  O O   . MET A 23  ? 0.19470 0.20174 0.20524 0.01177  -0.02231 -0.00944 30  MET A O   
117  C CB  . MET A 23  ? 0.14742 0.14921 0.17792 0.00751  -0.02029 -0.01391 30  MET A CB  
118  C CG  . MET A 23  ? 0.17480 0.17864 0.21092 0.00566  -0.01760 -0.01624 30  MET A CG  
119  S SD  . MET A 23  ? 0.18449 0.18461 0.21898 0.00919  -0.01771 -0.01637 30  MET A SD  
120  C CE  . MET A 23  ? 0.20575 0.20076 0.23058 -0.00178 -0.01683 -0.01980 30  MET A CE  
121  N N   . SER A 24  ? 0.17787 0.21275 0.20169 0.01949  -0.02701 -0.01271 31  SER A N   
122  C CA  . SER A 24  ? 0.18814 0.23404 0.19806 0.03375  -0.02917 -0.00773 31  SER A CA  
123  C C   . SER A 24  ? 0.24371 0.30774 0.25338 0.02944  -0.03177 -0.01259 31  SER A C   
124  O O   . SER A 24  ? 0.25033 0.30878 0.24262 0.03972  -0.03076 -0.00623 31  SER A O   
125  C CB  . SER A 24  ? 0.20995 0.28536 0.22412 0.04605  -0.03216 -0.00743 31  SER A CB  
126  O OG  . SER A 24  ? 0.29093 0.39308 0.29233 0.06482  -0.03511 -0.00352 31  SER A OG  
127  N N   . LEU A 25  ? 0.18286 0.26169 0.20681 0.01415  -0.03269 -0.02384 32  LEU A N   
128  C CA  . LEU A 25  ? 0.17383 0.26583 0.19417 0.00878  -0.03427 -0.03083 32  LEU A CA  
129  C C   . LEU A 25  ? 0.21303 0.27798 0.22261 0.00969  -0.03064 -0.02459 32  LEU A C   
130  O O   . LEU A 25  ? 0.23167 0.30278 0.22929 0.01592  -0.03159 -0.02242 32  LEU A O   
131  C CB  . LEU A 25  ? 0.22707 0.32523 0.25785 -0.01054 -0.03135 -0.04547 32  LEU A CB  
132  C CG  . LEU A 25  ? 0.30144 0.40823 0.32522 -0.01914 -0.03134 -0.05652 32  LEU A CG  
133  C CD1 . LEU A 25  ? 0.31750 0.43982 0.34797 -0.04028 -0.02765 -0.07439 32  LEU A CD1 
134  C CD2 . LEU A 25  ? 0.32594 0.39688 0.34036 -0.01968 -0.02514 -0.05332 32  LEU A CD2 
135  N N   . ILE A 26  ? 0.16030 0.20118 0.17371 0.00419  -0.02601 -0.02190 33  ILE A N   
136  C CA  . ILE A 26  ? 0.17978 0.20734 0.18610 0.00259  -0.02198 -0.01790 33  ILE A CA  
137  C C   . ILE A 26  ? 0.22019 0.23555 0.21121 0.00901  -0.01933 -0.00814 33  ILE A C   
138  O O   . ILE A 26  ? 0.24956 0.26073 0.22988 0.00885  -0.01546 -0.00457 33  ILE A O   
139  C CB  . ILE A 26  ? 0.16064 0.17927 0.17486 -0.00243 -0.01818 -0.01845 33  ILE A CB  
140  C CG1 . ILE A 26  ? 0.19653 0.21488 0.21408 -0.00433 -0.01546 -0.02563 33  ILE A CG1 
141  C CG2 . ILE A 26  ? 0.19055 0.20766 0.20035 -0.00582 -0.01390 -0.01467 33  ILE A CG2 
142  C CD1 . ILE A 26  ? 0.24322 0.25487 0.26493 -0.00140 -0.01110 -0.02423 33  ILE A CD1 
143  N N   . ILE A 27  ? 0.22341 0.22728 0.20863 0.01543  -0.01861 -0.00309 34  ILE A N   
144  C CA  . ILE A 27  ? 0.25661 0.23258 0.21758 0.02179  -0.01071 0.00678  34  ILE A CA  
145  C C   . ILE A 27  ? 0.31954 0.30219 0.26109 0.04064  -0.01079 0.01375  34  ILE A C   
146  O O   . ILE A 27  ? 0.35103 0.30864 0.26770 0.04579  -0.00123 0.02278  34  ILE A O   
147  C CB  . ILE A 27  ? 0.27788 0.23174 0.23254 0.02465  -0.00758 0.00919  34  ILE A CB  
148  C CG1 . ILE A 27  ? 0.23739 0.18644 0.20577 0.00584  -0.00594 0.00224  34  ILE A CG1 
149  C CG2 . ILE A 27  ? 0.31070 0.22567 0.22947 0.03756  0.00374  0.02030  34  ILE A CG2 
150  C CD1 . ILE A 27  ? 0.25549 0.18917 0.22113 0.00838  -0.00515 0.00130  34  ILE A CD1 
151  N N   . ASN A 28  ? 0.24737 0.26730 0.19813 0.05071  -0.02019 0.00906  35  ASN A N   
152  C CA  . ASN A 28  ? 0.30075 0.34043 0.23187 0.07456  -0.02170 0.01538  35  ASN A CA  
153  C C   . ASN A 28  ? 0.33981 0.41439 0.27413 0.07369  -0.02776 0.00820  35  ASN A C   
154  O O   . ASN A 28  ? 0.36056 0.45024 0.27319 0.09556  -0.02754 0.01508  35  ASN A O   
155  C CB  . ASN A 28  ? 0.30115 0.37208 0.23795 0.08891  -0.02783 0.01400  35  ASN A CB  
156  C CG  . ASN A 28  ? 0.39973 0.43036 0.32096 0.09843  -0.01969 0.02394  35  ASN A CG  
157  O OD1 . ASN A 28  ? 0.45234 0.43716 0.34114 0.10977  -0.00777 0.03617  35  ASN A OD1 
158  N ND2 . ASN A 28  ? 0.45885 0.49644 0.39992 0.08984  -0.02316 0.01796  35  ASN A ND2 
159  N N   . THR A 29  ? 0.22437 0.30836 0.17932 0.05219  -0.03137 -0.00465 36  THR A N   
160  C CA  . THR A 29  ? 0.21370 0.32609 0.16724 0.05038  -0.03587 -0.01378 36  THR A CA  
161  C C   . THR A 29  ? 0.25430 0.34381 0.18768 0.05662  -0.02862 -0.00357 36  THR A C   
162  O O   . THR A 29  ? 0.28601 0.34197 0.21965 0.04633  -0.02054 0.00193  36  THR A O   
163  C CB  . THR A 29  ? 0.24996 0.36536 0.22315 0.02685  -0.03743 -0.03018 36  THR A CB  
164  O OG1 . THR A 29  ? 0.27855 0.41343 0.26796 0.01865  -0.04109 -0.03948 36  THR A OG1 
165  C CG2 . THR A 29  ? 0.25009 0.38744 0.21780 0.02182  -0.04022 -0.04299 36  THR A CG2 
166  N N   . PHE A 30  ? 0.24887 0.36294 0.16504 0.07267  -0.03106 -0.00214 37  PHE A N   
167  C CA  . PHE A 30  ? 0.27742 0.37225 0.17542 0.07615  -0.02319 0.00605  37  PHE A CA  
168  C C   . PHE A 30  ? 0.28032 0.37730 0.19313 0.05641  -0.02441 -0.00666 37  PHE A C   
169  O O   . PHE A 30  ? 0.25355 0.37933 0.17301 0.05072  -0.03201 -0.02273 37  PHE A O   
170  C CB  . PHE A 30  ? 0.28283 0.40442 0.15500 0.10221  -0.02486 0.01169  37  PHE A CB  
171  C CG  . PHE A 30  ? 0.31707 0.41650 0.16733 0.10709  -0.01447 0.02205  37  PHE A CG  
172  C CD1 . PHE A 30  ? 0.43194 0.48116 0.26041 0.11079  0.00222  0.04066  37  PHE A CD1 
173  C CD2 . PHE A 30  ? 0.31288 0.43882 0.16252 0.10500  -0.01923 0.01187  37  PHE A CD2 
174  C CE1 . PHE A 30  ? 0.40130 0.43041 0.20961 0.11170  0.01472  0.05033  37  PHE A CE1 
175  C CE2 . PHE A 30  ? 0.33404 0.44110 0.16359 0.11009  -0.00846 0.02247  37  PHE A CE2 
176  C CZ  . PHE A 30  ? 0.39063 0.45154 0.20048 0.11332  0.00868  0.04224  37  PHE A CZ  
177  N N   . TYR A 31  ? 0.24082 0.30872 0.15432 0.04681  -0.01507 -0.00012 38  TYR A N   
178  C CA  . TYR A 31  ? 0.22473 0.29511 0.14867 0.03457  -0.01461 -0.01000 38  TYR A CA  
179  C C   . TYR A 31  ? 0.23150 0.28497 0.15076 0.03026  -0.00324 0.00051  38  TYR A C   
180  O O   . TYR A 31  ? 0.24266 0.28074 0.16957 0.02083  0.00228  0.00569  38  TYR A O   
181  C CB  . TYR A 31  ? 0.22848 0.29580 0.17317 0.02188  -0.01806 -0.02062 38  TYR A CB  
182  C CG  . TYR A 31  ? 0.23411 0.29352 0.18304 0.01546  -0.01315 -0.02579 38  TYR A CG  
183  C CD1 . TYR A 31  ? 0.29053 0.35301 0.23106 0.01519  -0.01293 -0.03763 38  TYR A CD1 
184  C CD2 . TYR A 31  ? 0.28570 0.33576 0.24442 0.01116  -0.00777 -0.01960 38  TYR A CD2 
185  C CE1 . TYR A 31  ? 0.37767 0.42761 0.31536 0.01611  -0.00545 -0.03974 38  TYR A CE1 
186  C CE2 . TYR A 31  ? 0.31729 0.36774 0.27729 0.01209  -0.00286 -0.02229 38  TYR A CE2 
187  C CZ  . TYR A 31  ? 0.26742 0.31501 0.21589 0.01683  -0.00102 -0.03068 38  TYR A CZ  
188  O OH  . TYR A 31  ? 0.37853 0.42433 0.32396 0.02410  0.00644  -0.03021 38  TYR A OH  
189  N N   . SER A 32  ? 0.24391 0.30482 0.15106 0.03501  0.00085  0.00192  39  SER A N   
190  C CA  . SER A 32  ? 0.25672 0.30813 0.15688 0.03022  0.01379  0.01306  39  SER A CA  
191  C C   . SER A 32  ? 0.24319 0.30490 0.16096 0.01853  0.01743  0.00850  39  SER A C   
192  O O   . SER A 32  ? 0.26752 0.32974 0.18699 0.00765  0.02793  0.01490  39  SER A O   
193  C CB  . SER A 32  ? 0.28008 0.33839 0.15809 0.04244  0.01840  0.01852  39  SER A CB  
194  O OG  . SER A 32  ? 0.30377 0.35553 0.16009 0.05861  0.01770  0.02655  39  SER A OG  
195  N N   . ASN A 33  ? 0.22487 0.29540 0.15248 0.02098  0.01095  -0.00262 40  ASN A N   
196  C CA  . ASN A 33  ? 0.24091 0.32530 0.17750 0.02037  0.01549  -0.00536 40  ASN A CA  
197  C C   . ASN A 33  ? 0.22872 0.31582 0.18346 0.01132  0.01536  -0.00540 40  ASN A C   
198  O O   . ASN A 33  ? 0.22530 0.31355 0.18643 0.01648  0.01326  -0.01098 40  ASN A O   
199  C CB  . ASN A 33  ? 0.25160 0.33156 0.17995 0.03082  0.01279  -0.01615 40  ASN A CB  
200  C CG  . ASN A 33  ? 0.29594 0.38784 0.22422 0.04011  0.01996  -0.01654 40  ASN A CG  
201  O OD1 . ASN A 33  ? 0.26869 0.38682 0.20161 0.04040  0.02618  -0.00955 40  ASN A OD1 
202  N ND2 . ASN A 33  ? 0.32744 0.40033 0.24624 0.04881  0.02121  -0.02491 40  ASN A ND2 
203  N N   . LYS A 34  ? 0.20752 0.20653 0.15738 -0.01430 -0.02942 -0.00375 41  LYS A N   
204  C CA  . LYS A 34  ? 0.18891 0.21571 0.17043 -0.01052 -0.01900 -0.00188 41  LYS A CA  
205  C C   . LYS A 34  ? 0.19070 0.20524 0.17001 -0.00681 -0.00914 -0.01237 41  LYS A C   
206  O O   . LYS A 34  ? 0.17627 0.20321 0.17216 -0.00597 -0.00627 -0.01211 41  LYS A O   
207  C CB  . LYS A 34  ? 0.22000 0.25881 0.21056 0.00152  -0.00880 0.00083  41  LYS A CB  
208  C CG  . LYS A 34  ? 0.19187 0.25380 0.19125 0.00516  -0.01352 0.01602  41  LYS A CG  
209  C CD  . LYS A 34  ? 0.23253 0.28845 0.22445 0.02298  -0.00367 0.01544  41  LYS A CD  
210  C CE  . LYS A 34  ? 0.20520 0.28772 0.20409 0.03570  -0.00344 0.03403  41  LYS A CE  
211  N NZ  . LYS A 34  ? 0.19823 0.31774 0.21484 0.05199  0.00366  0.05367  41  LYS A NZ  
212  N N   . GLU A 35  ? 0.20340 0.19693 0.16168 -0.00069 -0.00247 -0.01741 42  GLU A N   
213  C CA  . GLU A 35  ? 0.17693 0.17286 0.14454 0.00518  0.00929  -0.01847 42  GLU A CA  
214  C C   . GLU A 35  ? 0.21928 0.20970 0.18670 0.00116  0.00439  -0.02353 42  GLU A C   
215  O O   . GLU A 35  ? 0.20576 0.20401 0.18802 0.00417  0.01192  -0.02281 42  GLU A O   
216  C CB  . GLU A 35  ? 0.23641 0.22052 0.18117 0.02082  0.02245  -0.01341 42  GLU A CB  
217  C CG  . GLU A 35  ? 0.27264 0.21448 0.16380 0.03167  0.01759  -0.02086 42  GLU A CG  
218  C CD  . GLU A 35  ? 0.35996 0.28366 0.21104 0.06038  0.03571  -0.01331 42  GLU A CD  
219  O OE1 . GLU A 35  ? 0.40173 0.34091 0.26006 0.06457  0.04392  -0.00385 42  GLU A OE1 
220  O OE2 . GLU A 35  ? 0.46603 0.35728 0.27324 0.08213  0.04218  -0.01521 42  GLU A OE2 
221  N N   . ILE A 36  ? 0.20648 0.18178 0.15747 -0.00794 -0.01169 -0.02470 43  ILE A N   
222  C CA  . ILE A 36  ? 0.21454 0.18218 0.16543 -0.01456 -0.01948 -0.02628 43  ILE A CA  
223  C C   . ILE A 36  ? 0.18794 0.18908 0.17604 -0.01708 -0.01367 -0.02252 43  ILE A C   
224  O O   . ILE A 36  ? 0.18798 0.18537 0.17831 -0.01970 -0.01558 -0.02392 43  ILE A O   
225  C CB  . ILE A 36  ? 0.26890 0.21294 0.19970 -0.03183 -0.04725 -0.02005 43  ILE A CB  
226  C CG1 . ILE A 36  ? 0.25144 0.23695 0.21847 -0.04522 -0.05679 -0.00169 43  ILE A CG1 
227  C CG2 . ILE A 36  ? 0.34340 0.22662 0.21001 -0.02386 -0.05809 -0.02814 43  ILE A CG2 
228  C CD1 . ILE A 36  ? 0.25888 0.28532 0.26600 -0.05240 -0.05723 0.01461  43  ILE A CD1 
229  N N   . PHE A 37  ? 0.14236 0.16637 0.14876 -0.01233 -0.00730 -0.01830 44  PHE A N   
230  C CA  . PHE A 37  ? 0.14279 0.18041 0.16282 -0.00600 -0.00218 -0.01654 44  PHE A CA  
231  C C   . PHE A 37  ? 0.15814 0.18281 0.17794 -0.00519 0.00114  -0.02457 44  PHE A C   
232  O O   . PHE A 37  ? 0.15154 0.17888 0.17551 -0.00375 0.00091  -0.02462 44  PHE A O   
233  C CB  . PHE A 37  ? 0.16450 0.20410 0.18059 0.00708  0.00233  -0.01412 44  PHE A CB  
234  C CG  . PHE A 37  ? 0.15920 0.17597 0.16749 0.00710  0.00124  -0.02093 44  PHE A CG  
235  C CD1 . PHE A 37  ? 0.18633 0.20077 0.19441 0.00314  0.00188  -0.01941 44  PHE A CD1 
236  C CD2 . PHE A 37  ? 0.19576 0.19267 0.19732 0.00887  -0.00432 -0.02393 44  PHE A CD2 
237  C CE1 . PHE A 37  ? 0.17290 0.17568 0.18416 -0.00077 -0.00147 -0.01550 44  PHE A CE1 
238  C CE2 . PHE A 37  ? 0.20663 0.18545 0.20933 0.00067  -0.01400 -0.02070 44  PHE A CE2 
239  C CZ  . PHE A 37  ? 0.18224 0.16938 0.19508 -0.00508 -0.01167 -0.01369 44  PHE A CZ  
240  N N   . LEU A 38  ? 0.14541 0.16190 0.16384 -0.00449 0.00504  -0.02597 45  LEU A N   
241  C CA  . LEU A 38  ? 0.13835 0.15503 0.16824 -0.00449 0.00662  -0.02367 45  LEU A CA  
242  C C   . LEU A 38  ? 0.19039 0.20324 0.21499 -0.00231 0.00973  -0.02661 45  LEU A C   
243  O O   . LEU A 38  ? 0.15438 0.16940 0.18834 -0.00340 0.00805  -0.02644 45  LEU A O   
244  C CB  . LEU A 38  ? 0.14123 0.16562 0.18253 -0.00371 0.01096  -0.01173 45  LEU A CB  
245  C CG  . LEU A 38  ? 0.14532 0.18280 0.21251 -0.00796 0.00830  0.00342  45  LEU A CG  
246  C CD1 . LEU A 38  ? 0.15727 0.17538 0.22250 -0.01837 -0.01142 -0.00066 45  LEU A CD1 
247  C CD2 . LEU A 38  ? 0.16413 0.22446 0.25587 -0.00950 0.01185  0.02876  45  LEU A CD2 
248  N N   . ARG A 39  ? 0.17632 0.17323 0.17688 0.00132  0.01036  -0.02973 46  ARG A N   
249  C CA  . ARG A 39  ? 0.18300 0.15794 0.16269 0.00437  0.00745  -0.03379 46  ARG A CA  
250  C C   . ARG A 39  ? 0.20360 0.18595 0.19701 -0.00845 -0.00285 -0.03418 46  ARG A C   
251  O O   . ARG A 39  ? 0.21443 0.19243 0.20906 -0.00734 -0.00272 -0.03529 46  ARG A O   
252  C CB  . ARG A 39  ? 0.23527 0.17029 0.16885 0.00817  -0.00108 -0.03785 46  ARG A CB  
253  C CG  . ARG A 39  ? 0.32617 0.21923 0.22436 0.00794  -0.01407 -0.04254 46  ARG A CG  
254  C CD  . ARG A 39  ? 0.42980 0.26049 0.26495 0.00727  -0.03576 -0.04668 46  ARG A CD  
255  N NE  . ARG A 39  ? 0.45886 0.30218 0.31490 -0.02246 -0.06043 -0.03823 46  ARG A NE  
256  C CZ  . ARG A 39  ? 0.47076 0.27571 0.29025 -0.03261 -0.08518 -0.03581 46  ARG A CZ  
257  N NH1 . ARG A 39  ? 0.54117 0.28253 0.29167 -0.01221 -0.08837 -0.04359 46  ARG A NH1 
258  N NH2 . ARG A 39  ? 0.48278 0.31976 0.33924 -0.05981 -0.10500 -0.01890 46  ARG A NH2 
259  N N   . GLU A 40  ? 0.16417 0.16308 0.16966 -0.01741 -0.00958 -0.02865 47  GLU A N   
260  C CA  . GLU A 40  ? 0.13586 0.15152 0.15653 -0.02472 -0.01552 -0.01947 47  GLU A CA  
261  C C   . GLU A 40  ? 0.16215 0.18902 0.19364 -0.01498 -0.00589 -0.02192 47  GLU A C   
262  O O   . GLU A 40  ? 0.17705 0.20756 0.21298 -0.01658 -0.00743 -0.01806 47  GLU A O   
263  C CB  . GLU A 40  ? 0.13114 0.17539 0.16786 -0.02968 -0.02032 -0.00256 47  GLU A CB  
264  C CG  . GLU A 40  ? 0.15690 0.18433 0.18099 -0.04519 -0.03916 0.00316  47  GLU A CG  
265  C CD  . GLU A 40  ? 0.24804 0.23851 0.25033 -0.06091 -0.06079 0.00434  47  GLU A CD  
266  O OE1 . GLU A 40  ? 0.24145 0.24287 0.25878 -0.06780 -0.06476 0.01400  47  GLU A OE1 
267  O OE2 . GLU A 40  ? 0.33917 0.27997 0.29949 -0.06523 -0.07716 -0.00339 47  GLU A OE2 
268  N N   . LEU A 41  ? 0.13856 0.16380 0.16898 -0.00634 -0.00063 -0.02657 48  LEU A N   
269  C CA  . LEU A 41  ? 0.16517 0.18253 0.19125 0.00111  -0.00112 -0.02896 48  LEU A CA  
270  C C   . LEU A 41  ? 0.18179 0.19219 0.21483 -0.00381 -0.00331 -0.03194 48  LEU A C   
271  O O   . LEU A 41  ? 0.16997 0.17521 0.20023 -0.00151 -0.00634 -0.03238 48  LEU A O   
272  C CB  . LEU A 41  ? 0.16691 0.16670 0.17874 0.00774  -0.00567 -0.03096 48  LEU A CB  
273  C CG  . LEU A 41  ? 0.17024 0.17611 0.16854 0.02202  0.00006  -0.02577 48  LEU A CG  
274  C CD1 . LEU A 41  ? 0.20883 0.18186 0.18162 0.02904  -0.00818 -0.02973 48  LEU A CD1 
275  C CD2 . LEU A 41  ? 0.18735 0.20438 0.17299 0.04249  0.00880  -0.01578 48  LEU A CD2 
276  N N   . ILE A 42  ? 0.14157 0.15342 0.18165 -0.00606 0.00001  -0.03061 49  ILE A N   
277  C CA  . ILE A 42  ? 0.14554 0.15983 0.19499 -0.00393 0.00250  -0.02632 49  ILE A CA  
278  C C   . ILE A 42  ? 0.16189 0.16648 0.19970 -0.00244 0.00314  -0.03109 49  ILE A C   
279  O O   . ILE A 42  ? 0.16285 0.16819 0.20692 -0.00089 0.00213  -0.02918 49  ILE A O   
280  C CB  . ILE A 42  ? 0.12628 0.15038 0.18188 0.00385  0.01268  -0.01628 49  ILE A CB  
281  C CG1 . ILE A 42  ? 0.11568 0.15374 0.19391 -0.00423 0.00594  -0.00356 49  ILE A CG1 
282  C CG2 . ILE A 42  ? 0.15109 0.18242 0.21155 0.01660  0.02204  -0.00648 49  ILE A CG2 
283  C CD1 . ILE A 42  ? 0.12974 0.19049 0.22098 0.00556  0.02005  0.01568  49  ILE A CD1 
284  N N   . SER A 43  ? 0.16770 0.15988 0.18808 -0.00595 -0.00006 -0.03429 50  SER A N   
285  C CA  . SER A 43  ? 0.16232 0.13798 0.16986 -0.01092 -0.00782 -0.03431 50  SER A CA  
286  C C   . SER A 43  ? 0.15779 0.15260 0.18272 -0.01559 -0.00967 -0.02901 50  SER A C   
287  O O   . SER A 43  ? 0.16815 0.15599 0.19135 -0.01571 -0.01169 -0.02839 50  SER A O   
288  C CB  . SER A 43  ? 0.25345 0.20884 0.24068 -0.02156 -0.02159 -0.03186 50  SER A CB  
289  O OG  . SER A 43  ? 0.34523 0.28253 0.32325 -0.03416 -0.03778 -0.02553 50  SER A OG  
290  N N   . ASN A 44  ? 0.13813 0.15328 0.17289 -0.01347 -0.00683 -0.02426 51  ASN A N   
291  C CA  . ASN A 44  ? 0.13938 0.16729 0.17694 -0.00665 -0.00398 -0.01712 51  ASN A CA  
292  C C   . ASN A 44  ? 0.17231 0.18493 0.20289 -0.00027 -0.00492 -0.02550 51  ASN A C   
293  O O   . ASN A 44  ? 0.16135 0.17335 0.18941 0.00240  -0.00530 -0.02237 51  ASN A O   
294  C CB  . ASN A 44  ? 0.16609 0.20876 0.19900 0.00700  0.00277  -0.00958 51  ASN A CB  
295  C CG  . ASN A 44  ? 0.20032 0.27381 0.25082 0.00136  0.00326  0.01012  51  ASN A CG  
296  O OD1 . ASN A 44  ? 0.19074 0.26757 0.25425 -0.01842 -0.00819 0.01880  51  ASN A OD1 
297  N ND2 . ASN A 44  ? 0.19820 0.29025 0.24570 0.01875  0.01281  0.02102  51  ASN A ND2 
298  N N   . SER A 45  ? 0.14446 0.14695 0.17570 -0.00074 -0.00827 -0.03146 52  SER A N   
299  C CA  . SER A 45  ? 0.17992 0.17105 0.21193 -0.00117 -0.01698 -0.03164 52  SER A CA  
300  C C   . SER A 45  ? 0.15747 0.15462 0.20149 -0.00295 -0.01382 -0.02946 52  SER A C   
301  O O   . SER A 45  ? 0.14508 0.13678 0.18780 -0.00203 -0.01955 -0.02800 52  SER A O   
302  C CB  . SER A 45  ? 0.16451 0.15317 0.20727 -0.00766 -0.02591 -0.02689 52  SER A CB  
303  O OG  . SER A 45  ? 0.20090 0.16740 0.22014 -0.00475 -0.03480 -0.03017 52  SER A OG  
304  N N   . SER A 46  ? 0.14576 0.14589 0.19265 -0.00178 -0.00591 -0.02908 53  SER A N   
305  C CA  . SER A 46  ? 0.16761 0.16017 0.21015 0.00431  -0.00230 -0.02751 53  SER A CA  
306  C C   . SER A 46  ? 0.18724 0.16924 0.21948 -0.00060 -0.00760 -0.02964 53  SER A C   
307  O O   . SER A 46  ? 0.17757 0.15601 0.21076 0.00270  -0.00877 -0.02774 53  SER A O   
308  C CB  . SER A 46  ? 0.19912 0.17554 0.22109 0.01417  0.00513  -0.02876 53  SER A CB  
309  O OG  . SER A 46  ? 0.20631 0.15980 0.20627 0.02812  0.00848  -0.02802 53  SER A OG  
310  N N   . ASP A 47  ? 0.17758 0.16190 0.20589 -0.00882 -0.01112 -0.02773 54  ASP A N   
311  C CA  . ASP A 47  ? 0.16050 0.14645 0.18861 -0.01498 -0.01606 -0.01933 54  ASP A CA  
312  C C   . ASP A 47  ? 0.19052 0.18680 0.22158 -0.00634 -0.01246 -0.01764 54  ASP A C   
313  O O   . ASP A 47  ? 0.18689 0.17948 0.21623 -0.00681 -0.01458 -0.01303 54  ASP A O   
314  C CB  . ASP A 47  ? 0.15547 0.15937 0.19199 -0.02505 -0.02001 -0.00512 54  ASP A CB  
315  C CG  . ASP A 47  ? 0.26306 0.24221 0.28682 -0.03946 -0.03462 -0.00387 54  ASP A CG  
316  O OD1 . ASP A 47  ? 0.25329 0.19057 0.24833 -0.03583 -0.03986 -0.01573 54  ASP A OD1 
317  O OD2 . ASP A 47  ? 0.23715 0.23402 0.27324 -0.05166 -0.04253 0.01161  54  ASP A OD2 
318  N N   . ALA A 48  ? 0.16833 0.16703 0.19435 0.00246  -0.01051 -0.02143 55  ALA A N   
319  C CA  . ALA A 48  ? 0.15974 0.14739 0.16784 0.01393  -0.01334 -0.02167 55  ALA A CA  
320  C C   . ALA A 48  ? 0.16602 0.14122 0.17876 0.00976  -0.02293 -0.02540 55  ALA A C   
321  O O   . ALA A 48  ? 0.17304 0.13756 0.17240 0.01529  -0.02749 -0.02389 55  ALA A O   
322  C CB  . ALA A 48  ? 0.18672 0.15723 0.16972 0.02547  -0.01679 -0.02584 55  ALA A CB  
323  N N   . LEU A 49  ? 0.14641 0.12655 0.17840 0.00293  -0.02548 -0.02579 56  LEU A N   
324  C CA  . LEU A 49  ? 0.14789 0.13124 0.19568 0.00119  -0.03219 -0.01930 56  LEU A CA  
325  C C   . LEU A 49  ? 0.14898 0.13203 0.19611 0.00570  -0.02469 -0.01864 56  LEU A C   
326  O O   . LEU A 49  ? 0.16986 0.15066 0.21907 0.00734  -0.03075 -0.01431 56  LEU A O   
327  C CB  . LEU A 49  ? 0.16446 0.16709 0.23866 -0.00088 -0.03017 -0.00936 56  LEU A CB  
328  C CG  . LEU A 49  ? 0.14631 0.14439 0.22467 -0.01140 -0.04727 -0.00398 56  LEU A CG  
329  C CD1 . LEU A 49  ? 0.14134 0.16588 0.24660 -0.01228 -0.03854 0.00821  56  LEU A CD1 
330  C CD2 . LEU A 49  ? 0.16646 0.15744 0.25362 -0.02212 -0.07314 0.00979  56  LEU A CD2 
331  N N   . ASP A 50  ? 0.15724 0.13439 0.19562 0.00619  -0.01642 -0.02202 57  ASP A N   
332  C CA  . ASP A 50  ? 0.19815 0.15845 0.22400 0.00833  -0.01637 -0.02107 57  ASP A CA  
333  C C   . ASP A 50  ? 0.21537 0.17710 0.23871 0.00442  -0.02101 -0.01732 57  ASP A C   
334  O O   . ASP A 50  ? 0.19938 0.15177 0.21876 0.00753  -0.02323 -0.01472 57  ASP A O   
335  C CB  . ASP A 50  ? 0.18823 0.12548 0.19373 0.00258  -0.01921 -0.02303 57  ASP A CB  
336  C CG  . ASP A 50  ? 0.21924 0.13931 0.20791 0.01451  -0.01360 -0.02740 57  ASP A CG  
337  O OD1 . ASP A 50  ? 0.24835 0.18533 0.24930 0.02957  -0.00263 -0.02359 57  ASP A OD1 
338  O OD2 . ASP A 50  ? 0.26247 0.14991 0.22263 0.00891  -0.02253 -0.03026 57  ASP A OD2 
339  N N   . LYS A 51  ? 0.16295 0.13651 0.18465 0.00290  -0.01996 -0.01445 58  LYS A N   
340  C CA  . LYS A 51  ? 0.17643 0.15450 0.18990 0.00749  -0.01894 -0.00543 58  LYS A CA  
341  C C   . LYS A 51  ? 0.20663 0.17138 0.20816 0.01623  -0.02529 -0.00986 58  LYS A C   
342  O O   . LYS A 51  ? 0.21901 0.17973 0.21426 0.01919  -0.02624 -0.00432 58  LYS A O   
343  C CB  . LYS A 51  ? 0.20697 0.20324 0.21467 0.01561  -0.01061 0.00418  58  LYS A CB  
344  C CG  . LYS A 51  ? 0.19386 0.21391 0.22231 0.00219  -0.00894 0.02099  58  LYS A CG  
345  C CD  . LYS A 51  ? 0.16850 0.21794 0.19649 0.01738  0.00383  0.03622  58  LYS A CD  
346  C CE  . LYS A 51  ? 0.19855 0.27213 0.25397 -0.00128 -0.00089 0.05261  58  LYS A CE  
347  N NZ  . LYS A 51  ? 0.25855 0.36796 0.31776 0.01773  0.01436  0.07136  58  LYS A NZ  
348  N N   . ILE A 52  ? 0.20240 0.15676 0.19829 0.01813  -0.03438 -0.01652 59  ILE A N   
349  C CA  . ILE A 52  ? 0.21575 0.15037 0.19766 0.02075  -0.05023 -0.01630 59  ILE A CA  
350  C C   . ILE A 52  ? 0.20058 0.14736 0.21117 0.01440  -0.05337 -0.01059 59  ILE A C   
351  O O   . ILE A 52  ? 0.23009 0.16822 0.23408 0.01671  -0.06161 -0.00672 59  ILE A O   
352  C CB  . ILE A 52  ? 0.24452 0.15285 0.20672 0.01895  -0.07052 -0.01945 59  ILE A CB  
353  C CG1 . ILE A 52  ? 0.28337 0.15535 0.21682 0.01900  -0.09722 -0.01722 59  ILE A CG1 
354  C CG2 . ILE A 52  ? 0.21930 0.14934 0.22120 0.00431  -0.07447 -0.01436 59  ILE A CG2 
355  C CD1 . ILE A 52  ? 0.35613 0.19821 0.23456 0.04187  -0.09185 -0.02109 59  ILE A CD1 
356  N N   . ARG A 53  ? 0.19374 0.15876 0.23019 0.01206  -0.04417 -0.00817 60  ARG A N   
357  C CA  . ARG A 53  ? 0.18024 0.15541 0.23448 0.01779  -0.04087 0.00094  60  ARG A CA  
358  C C   . ARG A 53  ? 0.19240 0.15132 0.22880 0.02231  -0.03644 -0.00172 60  ARG A C   
359  O O   . ARG A 53  ? 0.21330 0.17183 0.25319 0.02705  -0.04097 0.00502  60  ARG A O   
360  C CB  . ARG A 53  ? 0.19741 0.18436 0.26318 0.02652  -0.02653 0.00472  60  ARG A CB  
361  C CG  . ARG A 53  ? 0.26699 0.26037 0.33938 0.04492  -0.01822 0.01776  60  ARG A CG  
362  C CD  . ARG A 53  ? 0.35629 0.35905 0.42949 0.06549  -0.00065 0.02665  60  ARG A CD  
363  N NE  . ARG A 53  ? 0.42823 0.47984 0.54689 0.06563  0.00022  0.05109  60  ARG A NE  
364  C CZ  . ARG A 53  ? 0.47202 0.53822 0.59436 0.07851  0.01531  0.05921  60  ARG A CZ  
365  N NH1 . ARG A 53  ? 0.36412 0.39143 0.44137 0.08885  0.02586  0.03937  60  ARG A NH1 
366  N NH2 . ARG A 53  ? 0.38448 0.50463 0.55696 0.07839  0.01612  0.09152  60  ARG A NH2 
367  N N   . TYR A 54  ? 0.19546 0.14258 0.21564 0.01802  -0.03106 -0.00690 61  TYR A N   
368  C CA  . TYR A 54  ? 0.21274 0.14384 0.21935 0.01634  -0.03236 -0.00288 61  TYR A CA  
369  C C   . TYR A 54  ? 0.23544 0.17045 0.23742 0.01877  -0.03643 0.00199  61  TYR A C   
370  O O   . TYR A 54  ? 0.25902 0.18409 0.25660 0.02205  -0.03940 0.00623  61  TYR A O   
371  C CB  . TYR A 54  ? 0.21805 0.14433 0.21838 0.00394  -0.03335 0.00145  61  TYR A CB  
372  C CG  . TYR A 54  ? 0.27401 0.18096 0.26371 -0.00407 -0.04164 0.01252  61  TYR A CG  
373  C CD1 . TYR A 54  ? 0.27872 0.14378 0.24498 -0.00174 -0.04971 0.00907  61  TYR A CD1 
374  C CD2 . TYR A 54  ? 0.26054 0.18881 0.25864 -0.00972 -0.04086 0.02933  61  TYR A CD2 
375  C CE1 . TYR A 54  ? 0.31174 0.14928 0.26308 -0.01151 -0.06280 0.01992  61  TYR A CE1 
376  C CE2 . TYR A 54  ? 0.29993 0.21549 0.29450 -0.02056 -0.05064 0.04574  61  TYR A CE2 
377  C CZ  . TYR A 54  ? 0.30146 0.16805 0.27277 -0.02487 -0.06468 0.03981  61  TYR A CZ  
378  O OH  . TYR A 54  ? 0.33633 0.17833 0.29785 -0.03842 -0.08038 0.05634  61  TYR A OH  
379  N N   . GLU A 55  ? 0.23224 0.17390 0.22542 0.02158  -0.03673 0.00141  62  GLU A N   
380  C CA  . GLU A 55  ? 0.26978 0.20184 0.24048 0.03121  -0.04112 0.00532  62  GLU A CA  
381  C C   . GLU A 55  ? 0.30935 0.22982 0.28181 0.03148  -0.05659 0.00349  62  GLU A C   
382  O O   . GLU A 55  ? 0.31836 0.22837 0.27706 0.03669  -0.06154 0.00795  62  GLU A O   
383  C CB  . GLU A 55  ? 0.29300 0.21705 0.23289 0.04435  -0.03933 0.00415  62  GLU A CB  
384  C CG  . GLU A 55  ? 0.31728 0.26703 0.26105 0.04917  -0.02095 0.01797  62  GLU A CG  
385  C CD  . GLU A 55  ? 0.54128 0.48236 0.44302 0.07615  -0.01234 0.02210  62  GLU A CD  
386  O OE1 . GLU A 55  ? 0.58394 0.55760 0.49085 0.08772  0.00667  0.04384  62  GLU A OE1 
387  O OE2 . GLU A 55  ? 0.52518 0.42414 0.38489 0.08766  -0.02642 0.00796  62  GLU A OE2 
388  N N   . SER A 56  ? 0.26043 0.18777 0.25382 0.02524  -0.06550 0.00263  63  SER A N   
389  C CA  . SER A 56  ? 0.26729 0.19646 0.27555 0.02190  -0.08391 0.01221  63  SER A CA  
390  C C   . SER A 56  ? 0.27157 0.21403 0.29881 0.02829  -0.07512 0.02056  63  SER A C   
391  O O   . SER A 56  ? 0.31672 0.26450 0.35582 0.02844  -0.08875 0.03273  63  SER A O   
392  C CB  . SER A 56  ? 0.27024 0.21683 0.30822 0.01180  -0.09527 0.02081  63  SER A CB  
393  O OG  . SER A 56  ? 0.28687 0.26624 0.35977 0.01753  -0.07579 0.02859  63  SER A OG  
394  N N   . LEU A 57  ? 0.27138 0.21267 0.29671 0.03401  -0.05655 0.01628  64  LEU A N   
395  C CA  . LEU A 57  ? 0.34098 0.27834 0.36841 0.04581  -0.05026 0.02312  64  LEU A CA  
396  C C   . LEU A 57  ? 0.33795 0.26228 0.35155 0.04626  -0.05798 0.02615  64  LEU A C   
397  O O   . LEU A 57  ? 0.42326 0.34794 0.44217 0.05696  -0.05799 0.03524  64  LEU A O   
398  C CB  . LEU A 57  ? 0.29866 0.21045 0.30406 0.05014  -0.03895 0.01597  64  LEU A CB  
399  C CG  . LEU A 57  ? 0.33993 0.25777 0.34998 0.05597  -0.02977 0.01332  64  LEU A CG  
400  C CD1 . LEU A 57  ? 0.32274 0.19473 0.29333 0.06154  -0.02688 0.00581  64  LEU A CD1 
401  C CD2 . LEU A 57  ? 0.34089 0.29018 0.37811 0.07418  -0.02231 0.02923  64  LEU A CD2 
402  N N   . THR A 58  ? 0.31388 0.22709 0.30636 0.03983  -0.06084 0.02148  65  THR A N   
403  C CA  . THR A 58  ? 0.38195 0.28282 0.35637 0.04324  -0.06573 0.02662  65  THR A CA  
404  C C   . THR A 58  ? 0.38215 0.27336 0.33577 0.04554  -0.08095 0.02604  65  THR A C   
405  O O   . THR A 58  ? 0.45198 0.32849 0.38324 0.05182  -0.08706 0.03042  65  THR A O   
406  C CB  . THR A 58  ? 0.44971 0.34478 0.40996 0.03952  -0.05582 0.03113  65  THR A CB  
407  O OG1 . THR A 58  ? 0.45006 0.35636 0.40400 0.03866  -0.04935 0.03063  65  THR A OG1 
408  C CG2 . THR A 58  ? 0.42301 0.30377 0.38718 0.03317  -0.05329 0.03261  65  THR A CG2 
409  N N   . ASP A 59  ? 0.45104 0.28067 0.35256 0.02229  -0.10484 0.08346  66  ASP A N   
410  C CA  . ASP A 59  ? 0.40270 0.28294 0.32640 0.02677  -0.10597 0.08340  66  ASP A CA  
411  C C   . ASP A 59  ? 0.39111 0.29447 0.33594 0.03527  -0.10387 0.07049  66  ASP A C   
412  O O   . ASP A 59  ? 0.37461 0.29232 0.32624 0.02689  -0.10151 0.06082  66  ASP A O   
413  C CB  . ASP A 59  ? 0.41327 0.31731 0.33609 0.01205  -0.10546 0.09047  66  ASP A CB  
414  C CG  . ASP A 59  ? 0.49423 0.42823 0.41588 0.02273  -0.10560 0.08922  66  ASP A CG  
415  O OD1 . ASP A 59  ? 0.43567 0.37138 0.35957 0.03303  -0.11255 0.08346  66  ASP A OD1 
416  O OD2 . ASP A 59  ? 0.45882 0.41173 0.37269 0.02164  -0.09938 0.09699  66  ASP A OD2 
417  N N   . PRO A 60  ? 0.43095 0.34230 0.38955 0.05190  -0.10484 0.07481  67  PRO A N   
418  C CA  . PRO A 60  ? 0.39981 0.33954 0.38518 0.05645  -0.10505 0.07053  67  PRO A CA  
419  C C   . PRO A 60  ? 0.36416 0.32843 0.35336 0.04289  -0.11651 0.06306  67  PRO A C   
420  O O   . PRO A 60  ? 0.36173 0.33990 0.36585 0.03876  -0.11719 0.05624  67  PRO A O   
421  C CB  . PRO A 60  ? 0.48663 0.44516 0.49220 0.07533  -0.10704 0.08916  67  PRO A CB  
422  C CG  . PRO A 60  ? 0.56472 0.49268 0.54739 0.08575  -0.10341 0.09839  67  PRO A CG  
423  C CD  . PRO A 60  ? 0.49317 0.38466 0.44386 0.06892  -0.10275 0.08852  67  PRO A CD  
424  N N   . SER A 61  ? 0.38296 0.34576 0.35119 0.03863  -0.12546 0.06533  68  SER A N   
425  C CA  . SER A 61  ? 0.37826 0.34306 0.32773 0.03151  -0.13545 0.05712  68  SER A CA  
426  C C   . SER A 61  ? 0.36995 0.33066 0.31142 0.02749  -0.12319 0.04489  68  SER A C   
427  O O   . SER A 61  ? 0.36488 0.31889 0.28633 0.02559  -0.12882 0.03665  68  SER A O   
428  C CB  . SER A 61  ? 0.38750 0.33969 0.29990 0.03510  -0.14216 0.06247  68  SER A CB  
429  O OG  . SER A 61  ? 0.44476 0.39267 0.34222 0.03855  -0.12531 0.06534  68  SER A OG  
430  N N   . LYS A 62  ? 0.30525 0.26465 0.25680 0.02515  -0.10897 0.04524  69  LYS A N   
431  C CA  . LYS A 62  ? 0.32883 0.29289 0.27921 0.02016  -0.09945 0.03840  69  LYS A CA  
432  C C   . LYS A 62  ? 0.32376 0.29255 0.28959 0.01815  -0.10187 0.02628  69  LYS A C   
433  O O   . LYS A 62  ? 0.30083 0.27260 0.26220 0.01603  -0.09608 0.01922  69  LYS A O   
434  C CB  . LYS A 62  ? 0.36584 0.32476 0.32248 0.01097  -0.09180 0.04554  69  LYS A CB  
435  C CG  . LYS A 62  ? 0.42387 0.38490 0.36846 0.00885  -0.09122 0.06339  69  LYS A CG  
436  C CD  . LYS A 62  ? 0.37342 0.35555 0.32013 0.00052  -0.08341 0.07771  69  LYS A CD  
437  C CE  . LYS A 62  ? 0.42464 0.42052 0.36532 -0.00074 -0.08142 0.10373  69  LYS A CE  
438  N NZ  . LYS A 62  ? 0.42456 0.45881 0.37142 0.00182  -0.06846 0.12149  69  LYS A NZ  
439  N N   . LEU A 63  ? 0.29048 0.26500 0.27729 0.02038  -0.10915 0.02848  70  LEU A N   
440  C CA  . LEU A 63  ? 0.27536 0.26244 0.28263 0.01738  -0.11185 0.02399  70  LEU A CA  
441  C C   . LEU A 63  ? 0.27260 0.26379 0.27478 0.00951  -0.13333 0.02705  70  LEU A C   
442  O O   . LEU A 63  ? 0.33691 0.34215 0.36015 0.00234  -0.14095 0.02959  70  LEU A O   
443  C CB  . LEU A 63  ? 0.31562 0.31237 0.35107 0.02745  -0.10354 0.03213  70  LEU A CB  
444  C CG  . LEU A 63  ? 0.34280 0.31328 0.36484 0.03285  -0.08734 0.02688  70  LEU A CG  
445  C CD1 . LEU A 63  ? 0.34003 0.30442 0.37061 0.05343  -0.07594 0.03615  70  LEU A CD1 
446  C CD2 . LEU A 63  ? 0.32460 0.29198 0.34192 0.02290  -0.08180 0.01457  70  LEU A CD2 
447  N N   . ASP A 64  ? 0.32341 0.29642 0.29056 0.00877  -0.14475 0.02761  71  ASP A N   
448  C CA  . ASP A 64  ? 0.38905 0.34808 0.33484 -0.00310 -0.16497 0.02830  71  ASP A CA  
449  C C   . ASP A 64  ? 0.33419 0.27170 0.25892 -0.00971 -0.16480 0.01581  71  ASP A C   
450  O O   . ASP A 64  ? 0.42593 0.35142 0.34478 -0.02453 -0.17840 0.01842  71  ASP A O   
451  C CB  . ASP A 64  ? 0.43832 0.36893 0.33622 0.00121  -0.17098 0.02807  71  ASP A CB  
452  C CG  . ASP A 64  ? 0.46784 0.41933 0.38731 0.00355  -0.17594 0.04341  71  ASP A CG  
453  O OD1 . ASP A 64  ? 0.44077 0.42666 0.40971 0.00398  -0.17428 0.05570  71  ASP A OD1 
454  O OD2 . ASP A 64  ? 0.49596 0.42902 0.38087 0.00857  -0.17916 0.04505  71  ASP A OD2 
455  N N   . SER A 65  ? 0.35999 0.29047 0.27120 0.00070  -0.15057 0.00531  72  SER A N   
456  C CA  . SER A 65  ? 0.37418 0.28409 0.26329 -0.00011 -0.14622 -0.00585 72  SER A CA  
457  C C   . SER A 65  ? 0.40208 0.34050 0.34040 -0.00981 -0.14343 -0.00535 72  SER A C   
458  O O   . SER A 65  ? 0.42738 0.35447 0.35528 -0.01016 -0.13772 -0.01375 72  SER A O   
459  C CB  . SER A 65  ? 0.37759 0.28163 0.24050 0.01884  -0.12132 -0.01005 72  SER A CB  
460  O OG  . SER A 65  ? 0.32316 0.26382 0.22860 0.01994  -0.10530 -0.00262 72  SER A OG  
461  N N   . GLY A 66  ? 0.30150 0.27599 0.28993 -0.01289 -0.14434 0.00652  73  GLY A N   
462  C CA  . GLY A 66  ? 0.29926 0.30098 0.32974 -0.01640 -0.13833 0.01095  73  GLY A CA  
463  C C   . GLY A 66  ? 0.29904 0.32717 0.36522 -0.00265 -0.12212 0.01966  73  GLY A C   
464  O O   . GLY A 66  ? 0.26756 0.28258 0.32056 0.00616  -0.10523 0.01081  73  GLY A O   
465  N N   . LYS A 67  ? 0.25757 0.31939 0.36367 0.00062  -0.12567 0.04070  74  LYS A N   
466  C CA  . LYS A 67  ? 0.22638 0.29757 0.34830 0.02330  -0.10438 0.04935  74  LYS A CA  
467  C C   . LYS A 67  ? 0.19572 0.26504 0.32326 0.03483  -0.08288 0.04388  74  LYS A C   
468  O O   . LYS A 67  ? 0.28620 0.33203 0.39620 0.05319  -0.06470 0.04073  74  LYS A O   
469  C CB  . LYS A 67  ? 0.25863 0.37157 0.41897 0.03197  -0.10992 0.08110  74  LYS A CB  
470  C CG  . LYS A 67  ? 0.42507 0.53313 0.57124 0.02498  -0.12500 0.08598  74  LYS A CG  
471  C CD  . LYS A 67  ? 0.58995 0.72344 0.75776 0.04651  -0.11349 0.11030  74  LYS A CD  
472  C CE  . LYS A 67  ? 0.65977 0.80085 0.82359 0.03250  -0.13252 0.11979  74  LYS A CE  
473  N NZ  . LYS A 67  ? 0.60244 0.70356 0.72402 0.02115  -0.14678 0.09940  74  LYS A NZ  
474  N N   . GLU A 68  ? 0.19793 0.28240 0.34088 0.02438  -0.08603 0.04288  75  GLU A N   
475  C CA  . GLU A 68  ? 0.17806 0.26486 0.32786 0.03859  -0.06490 0.04209  75  GLU A CA  
476  C C   . GLU A 68  ? 0.22070 0.26768 0.33279 0.03440  -0.05645 0.01629  75  GLU A C   
477  O O   . GLU A 68  ? 0.22553 0.26389 0.32422 0.01769  -0.06625 0.00353  75  GLU A O   
478  C CB  . GLU A 68  ? 0.30900 0.43326 0.49529 0.02862  -0.07149 0.05651  75  GLU A CB  
479  C CG  . GLU A 68  ? 0.49622 0.63428 0.69623 0.05177  -0.04618 0.06618  75  GLU A CG  
480  C CD  . GLU A 68  ? 0.62070 0.78099 0.83868 0.03654  -0.04837 0.07194  75  GLU A CD  
481  O OE1 . GLU A 68  ? 0.68010 0.84621 0.90198 0.00953  -0.06953 0.07674  75  GLU A OE1 
482  O OE2 . GLU A 68  ? 0.55354 0.71297 0.76984 0.05167  -0.02867 0.07055  75  GLU A OE2 
483  N N   . LEU A 69  ? 0.17117 0.19114 0.26121 0.05074  -0.03932 0.01238  76  LEU A N   
484  C CA  . LEU A 69  ? 0.18011 0.16277 0.23424 0.04179  -0.03647 -0.00555 76  LEU A CA  
485  C C   . LEU A 69  ? 0.17905 0.16187 0.23373 0.04876  -0.02441 -0.00801 76  LEU A C   
486  O O   . LEU A 69  ? 0.20809 0.17461 0.24923 0.07227  -0.00927 -0.00129 76  LEU A O   
487  C CB  . LEU A 69  ? 0.22925 0.16382 0.24268 0.04914  -0.03404 -0.00690 76  LEU A CB  
488  C CG  . LEU A 69  ? 0.28247 0.21932 0.29714 0.04392  -0.04464 -0.00176 76  LEU A CG  
489  C CD1 . LEU A 69  ? 0.36736 0.24702 0.33496 0.04486  -0.04517 -0.00345 76  LEU A CD1 
490  C CD2 . LEU A 69  ? 0.24581 0.20425 0.26999 0.02229  -0.05659 -0.00686 76  LEU A CD2 
491  N N   . HIS A 70  ? 0.15277 0.15078 0.21768 0.03272  -0.02890 -0.01605 77  HIS A N   
492  C CA  . HIS A 70  ? 0.17190 0.17556 0.24174 0.03835  -0.01830 -0.01678 77  HIS A CA  
493  C C   . HIS A 70  ? 0.15612 0.16099 0.22097 0.02019  -0.02326 -0.02832 77  HIS A C   
494  O O   . HIS A 70  ? 0.14512 0.15242 0.20604 0.00726  -0.03244 -0.03225 77  HIS A O   
495  C CB  . HIS A 70  ? 0.17045 0.21763 0.28366 0.04508  -0.01619 0.00047  77  HIS A CB  
496  C CG  . HIS A 70  ? 0.21008 0.27990 0.34556 0.02342  -0.03534 0.00176  77  HIS A CG  
497  N ND1 . HIS A 70  ? 0.47358 0.57534 0.64226 0.01879  -0.04763 0.02195  77  HIS A ND1 
498  C CD2 . HIS A 70  ? 0.26843 0.32734 0.39022 0.00677  -0.04501 -0.01156 77  HIS A CD2 
499  C CE1 . HIS A 70  ? 0.25175 0.34769 0.41545 -0.00320 -0.06829 0.01703  77  HIS A CE1 
500  N NE2 . HIS A 70  ? 0.27301 0.34086 0.40560 -0.00660 -0.06402 -0.00393 77  HIS A NE2 
501  N N   . ILE A 71  ? 0.13545 0.14118 0.19987 0.02411  -0.01422 -0.03006 78  ILE A N   
502  C CA  . ILE A 71  ? 0.13668 0.14771 0.19903 0.01151  -0.01569 -0.03715 78  ILE A CA  
503  C C   . ILE A 71  ? 0.11497 0.15091 0.20415 0.01500  -0.01030 -0.03230 78  ILE A C   
504  O O   . ILE A 71  ? 0.13619 0.17731 0.23283 0.02982  0.00098  -0.02403 78  ILE A O   
505  C CB  . ILE A 71  ? 0.16836 0.14773 0.19509 0.00869  -0.01363 -0.04221 78  ILE A CB  
506  C CG1 . ILE A 71  ? 0.19477 0.14501 0.19340 -0.00085 -0.02432 -0.04186 78  ILE A CG1 
507  C CG2 . ILE A 71  ? 0.16490 0.16032 0.19662 -0.00295 -0.01457 -0.04398 78  ILE A CG2 
508  C CD1 . ILE A 71  ? 0.25983 0.16160 0.21004 -0.00906 -0.03054 -0.04399 78  ILE A CD1 
509  N N   . ASN A 72  ? 0.10328 0.15027 0.20107 0.00389  -0.01713 -0.03475 79  ASN A N   
510  C CA  . ASN A 72  ? 0.07822 0.14052 0.19535 0.00171  -0.01602 -0.02954 79  ASN A CA  
511  C C   . ASN A 72  ? 0.14094 0.19740 0.24347 -0.00074 -0.01029 -0.03733 79  ASN A C   
512  O O   . ASN A 72  ? 0.12637 0.17557 0.21103 -0.00394 -0.01210 -0.04230 79  ASN A O   
513  C CB  . ASN A 72  ? 0.08518 0.14864 0.21051 -0.01025 -0.03291 -0.02452 79  ASN A CB  
514  C CG  . ASN A 72  ? 0.09509 0.17465 0.24299 -0.01154 -0.04236 -0.00999 79  ASN A CG  
515  O OD1 . ASN A 72  ? 0.10869 0.20933 0.27738 0.00193  -0.03099 0.00234  79  ASN A OD1 
516  N ND2 . ASN A 72  ? 0.13207 0.19762 0.26831 -0.02516 -0.06250 -0.00818 79  ASN A ND2 
517  N N   . LEU A 73  ? 0.09460 0.16047 0.20785 0.00291  -0.00189 -0.03344 80  LEU A N   
518  C CA  . LEU A 73  ? 0.07328 0.13765 0.17643 0.00093  0.00308  -0.03783 80  LEU A CA  
519  C C   . LEU A 73  ? 0.07371 0.14305 0.19088 -0.00388 -0.00058 -0.03242 80  LEU A C   
520  O O   . LEU A 73  ? 0.06844 0.15419 0.21106 -0.00404 0.00016  -0.02032 80  LEU A O   
521  C CB  . LEU A 73  ? 0.10666 0.16743 0.19922 0.00805  0.01389  -0.03823 80  LEU A CB  
522  C CG  . LEU A 73  ? 0.12944 0.16555 0.19258 0.00956  0.01231  -0.04259 80  LEU A CG  
523  C CD1 . LEU A 73  ? 0.12593 0.14068 0.16090 0.01737  0.02025  -0.04372 80  LEU A CD1 
524  C CD2 . LEU A 73  ? 0.14588 0.18151 0.19833 -0.00454 0.00188  -0.04392 80  LEU A CD2 
525  N N   . ILE A 74  ? 0.10674 0.16019 0.20501 -0.00660 -0.00494 -0.03690 81  ILE A N   
526  C CA  . ILE A 74  ? 0.14147 0.17793 0.23593 -0.01431 -0.01489 -0.03277 81  ILE A CA  
527  C C   . ILE A 74  ? 0.13671 0.16392 0.21420 -0.00753 -0.00521 -0.03501 81  ILE A C   
528  O O   . ILE A 74  ? 0.16953 0.17707 0.21541 0.00249  -0.00146 -0.03914 81  ILE A O   
529  C CB  . ILE A 74  ? 0.17401 0.17524 0.23908 -0.01988 -0.03186 -0.03594 81  ILE A CB  
530  C CG1 . ILE A 74  ? 0.15315 0.16873 0.23612 -0.02499 -0.04052 -0.03246 81  ILE A CG1 
531  C CG2 . ILE A 74  ? 0.18737 0.15452 0.23687 -0.03496 -0.05060 -0.02985 81  ILE A CG2 
532  C CD1 . ILE A 74  ? 0.17368 0.15144 0.22138 -0.03051 -0.05890 -0.03591 81  ILE A CD1 
533  N N   . PRO A 75  ? 0.14099 0.18198 0.23746 -0.00990 -0.00005 -0.02851 82  PRO A N   
534  C CA  . PRO A 75  ? 0.14923 0.17958 0.22954 -0.00361 0.00795  -0.02862 82  PRO A CA  
535  C C   . PRO A 75  ? 0.21162 0.19978 0.26864 -0.01221 -0.00621 -0.02565 82  PRO A C   
536  O O   . PRO A 75  ? 0.20518 0.18613 0.27453 -0.03062 -0.02447 -0.01728 82  PRO A O   
537  C CB  . PRO A 75  ? 0.13244 0.19393 0.24090 -0.00276 0.01893  -0.02198 82  PRO A CB  
538  C CG  . PRO A 75  ? 0.12902 0.20835 0.26771 -0.00986 0.01362  -0.01179 82  PRO A CG  
539  C CD  . PRO A 75  ? 0.15103 0.22188 0.28421 -0.01333 0.00263  -0.01698 82  PRO A CD  
540  N N   . ASN A 76  ? 0.21320 0.16917 0.23063 0.00131  0.00041  -0.02932 83  ASN A N   
541  C CA  . ASN A 76  ? 0.25745 0.14968 0.22974 -0.00360 -0.01353 -0.02845 83  ASN A CA  
542  C C   . ASN A 76  ? 0.32353 0.20972 0.28040 0.01347  0.00379  -0.02566 83  ASN A C   
543  O O   . ASN A 76  ? 0.33420 0.21366 0.26153 0.03999  0.02113  -0.02684 83  ASN A O   
544  C CB  . ASN A 76  ? 0.37362 0.20298 0.28272 0.00464  -0.02361 -0.03668 83  ASN A CB  
545  C CG  . ASN A 76  ? 0.49500 0.23584 0.34038 -0.00634 -0.04641 -0.03643 83  ASN A CG  
546  O OD1 . ASN A 76  ? 0.51323 0.22653 0.33529 0.00143  -0.03993 -0.03372 83  ASN A OD1 
547  N ND2 . ASN A 76  ? 0.52008 0.23469 0.34626 -0.02569 -0.07208 -0.03356 83  ASN A ND2 
548  N N   . LYS A 77  ? 0.25924 0.14475 0.29865 -0.03117 -0.00386 0.04368  84  LYS A N   
549  C CA  . LYS A 77  ? 0.27198 0.14152 0.29963 -0.01809 0.00516  0.04762  84  LYS A CA  
550  C C   . LYS A 77  ? 0.34793 0.16527 0.34722 -0.02103 0.00587  0.04433  84  LYS A C   
551  O O   . LYS A 77  ? 0.41619 0.21830 0.40292 -0.00371 0.01563  0.04699  84  LYS A O   
552  C CB  . LYS A 77  ? 0.28933 0.17552 0.33205 -0.02005 0.01066  0.06464  84  LYS A CB  
553  C CG  . LYS A 77  ? 0.31760 0.24218 0.37293 -0.00785 0.01675  0.06774  84  LYS A CG  
554  C CD  . LYS A 77  ? 0.32475 0.26335 0.39165 -0.00747 0.02549  0.08667  84  LYS A CD  
555  C CE  . LYS A 77  ? 0.32437 0.28926 0.39243 0.00675  0.03542  0.09050  84  LYS A CE  
556  N NZ  . LYS A 77  ? 0.37900 0.36698 0.46749 0.00184  0.03591  0.09594  84  LYS A NZ  
557  N N   . GLN A 78  ? 0.38871 0.17462 0.37327 -0.04264 -0.00387 0.04083  85  GLN A N   
558  C CA  . GLN A 78  ? 0.46916 0.18875 0.41166 -0.04451 -0.00087 0.03616  85  GLN A CA  
559  C C   . GLN A 78  ? 0.47441 0.17479 0.39368 -0.02244 0.00780  0.02356  85  GLN A C   
560  O O   . GLN A 78  ? 0.53358 0.20436 0.42971 -0.00491 0.02005  0.02368  85  GLN A O   
561  C CB  . GLN A 78  ? 0.57258 0.26789 0.50044 -0.07483 -0.01475 0.03437  85  GLN A CB  
562  C CG  . GLN A 78  ? 0.75436 0.46869 0.70546 -0.09838 -0.02224 0.05178  85  GLN A CG  
563  C CD  . GLN A 78  ? 0.89098 0.66498 0.88972 -0.09940 -0.02397 0.06857  85  GLN A CD  
564  O OE1 . GLN A 78  ? 0.76988 0.56370 0.78954 -0.10017 -0.01847 0.08580  85  GLN A OE1 
565  N NE2 . GLN A 78  ? 0.69071 0.50441 0.70891 -0.09525 -0.02807 0.06273  85  GLN A NE2 
566  N N   . ASP A 79  ? 0.40436 0.13430 0.33589 -0.02153 0.00224  0.01480  86  ASP A N   
567  C CA  . ASP A 79  ? 0.40073 0.12220 0.31657 -0.00110 0.01071  0.00612  86  ASP A CA  
568  C C   . ASP A 79  ? 0.36982 0.14146 0.31443 0.02160  0.01839  0.01253  86  ASP A C   
569  O O   . ASP A 79  ? 0.39315 0.16872 0.33314 0.03993  0.02643  0.01180  86  ASP A O   
570  C CB  . ASP A 79  ? 0.47057 0.19933 0.38428 -0.01263 0.00011  -0.00520 86  ASP A CB  
571  C CG  . ASP A 79  ? 0.56422 0.26492 0.45460 -0.03692 -0.01132 -0.01039 86  ASP A CG  
572  O OD1 . ASP A 79  ? 0.60538 0.27451 0.47509 -0.04345 -0.00997 -0.00768 86  ASP A OD1 
573  O OD2 . ASP A 79  ? 0.64675 0.36461 0.54246 -0.04957 -0.02256 -0.01544 86  ASP A OD2 
574  N N   . ARG A 80  ? 0.32719 0.13719 0.29911 0.01872  0.01510  0.02032  87  ARG A N   
575  C CA  . ARG A 80  ? 0.26972 0.12506 0.26242 0.03237  0.01671  0.02598  87  ARG A CA  
576  C C   . ARG A 80  ? 0.27647 0.15809 0.27835 0.03218  0.01100  0.01771  87  ARG A C   
577  O O   . ARG A 80  ? 0.25698 0.16029 0.26495 0.04424  0.01302  0.02222  87  ARG A O   
578  C CB  . ARG A 80  ? 0.30106 0.15393 0.28897 0.05390  0.02781  0.03844  87  ARG A CB  
579  C CG  . ARG A 80  ? 0.26893 0.16573 0.27529 0.05715  0.02361  0.04837  87  ARG A CG  
580  C CD  . ARG A 80  ? 0.43603 0.35343 0.44797 0.07586  0.02878  0.06392  87  ARG A CD  
581  N NE  . ARG A 80  ? 0.46087 0.34834 0.46090 0.09122  0.04253  0.07536  87  ARG A NE  
582  C CZ  . ARG A 80  ? 0.64561 0.54024 0.64779 0.11443  0.05383  0.09251  87  ARG A CZ  
583  N NH1 . ARG A 80  ? 0.44652 0.38115 0.46609 0.12260  0.05174  0.10116  87  ARG A NH1 
584  N NH2 . ARG A 80  ? 0.53638 0.40476 0.52454 0.12547  0.06658  0.10074  87  ARG A NH2 
585  N N   . THR A 81  ? 0.22972 0.11405 0.23556 0.01733  0.00309  0.00895  88  THR A N   
586  C CA  . THR A 81  ? 0.22128 0.12566 0.23383 0.01610  -0.00182 0.00142  88  THR A CA  
587  C C   . THR A 81  ? 0.22716 0.15514 0.25343 0.00753  -0.00691 0.00076  88  THR A C   
588  O O   . THR A 81  ? 0.21117 0.13903 0.24400 -0.00084 -0.00755 0.00554  88  THR A O   
589  C CB  . THR A 81  ? 0.24379 0.12388 0.24170 0.01050  -0.00413 -0.00768 88  THR A CB  
590  O OG1 . THR A 81  ? 0.29627 0.15976 0.29026 -0.00760 -0.01131 -0.00830 88  THR A OG1 
591  C CG2 . THR A 81  ? 0.26090 0.10982 0.23594 0.02551  0.00654  -0.00669 88  THR A CG2 
592  N N   . LEU A 82  ? 0.16959 0.11636 0.19866 0.01035  -0.00911 -0.00247 89  LEU A N   
593  C CA  . LEU A 82  ? 0.16984 0.12794 0.20267 0.00597  -0.01056 -0.00461 89  LEU A CA  
594  C C   . LEU A 82  ? 0.17234 0.13239 0.20598 0.00322  -0.01454 -0.01219 89  LEU A C   
595  O O   . LEU A 82  ? 0.17086 0.13434 0.20129 0.00639  -0.01620 -0.01451 89  LEU A O   
596  C CB  . LEU A 82  ? 0.17838 0.14321 0.20084 0.00951  -0.00984 -0.00269 89  LEU A CB  
597  C CG  . LEU A 82  ? 0.15900 0.12205 0.17336 0.00923  -0.00681 -0.00540 89  LEU A CG  
598  C CD1 . LEU A 82  ? 0.18200 0.14884 0.20828 0.01154  0.00157  0.00288  89  LEU A CD1 
599  C CD2 . LEU A 82  ? 0.19901 0.15283 0.18677 0.01009  -0.00710 -0.00577 89  LEU A CD2 
600  N N   . THR A 83  ? 0.15980 0.12109 0.20022 -0.00281 -0.01625 -0.01258 90  THR A N   
601  C CA  . THR A 83  ? 0.17372 0.13646 0.21391 -0.00548 -0.02022 -0.01839 90  THR A CA  
602  C C   . THR A 83  ? 0.16932 0.14287 0.21323 -0.00322 -0.01754 -0.01672 90  THR A C   
603  O O   . THR A 83  ? 0.19648 0.17785 0.24871 -0.00164 -0.01277 -0.00806 90  THR A O   
604  C CB  . THR A 83  ? 0.18721 0.14050 0.22694 -0.01547 -0.02630 -0.01824 90  THR A CB  
605  O OG1 . THR A 83  ? 0.21712 0.14539 0.24103 -0.01530 -0.02562 -0.02102 90  THR A OG1 
606  C CG2 . THR A 83  ? 0.20525 0.16001 0.24136 -0.01745 -0.03050 -0.02351 90  THR A CG2 
607  N N   . ILE A 84  ? 0.14103 0.11355 0.17772 -0.00167 -0.01860 -0.02248 91  ILE A N   
608  C CA  . ILE A 84  ? 0.15406 0.12572 0.18602 0.00163  -0.01444 -0.02184 91  ILE A CA  
609  C C   . ILE A 84  ? 0.18615 0.16388 0.22571 -0.00109 -0.01836 -0.02283 91  ILE A C   
610  O O   . ILE A 84  ? 0.18443 0.15977 0.21940 -0.00357 -0.02253 -0.02867 91  ILE A O   
611  C CB  . ILE A 84  ? 0.17634 0.13510 0.18750 0.00100  -0.01483 -0.02671 91  ILE A CB  
612  C CG1 . ILE A 84  ? 0.22698 0.17848 0.22477 0.00168  -0.01351 -0.02490 91  ILE A CG1 
613  C CG2 . ILE A 84  ? 0.20083 0.14418 0.19636 0.00488  -0.00857 -0.02718 91  ILE A CG2 
614  C CD1 . ILE A 84  ? 0.27829 0.23974 0.28134 -0.00199 -0.02039 -0.02336 91  ILE A CD1 
615  N N   . VAL A 85  ? 0.13209 0.12099 0.18392 0.00017  -0.01652 -0.01414 92  VAL A N   
616  C CA  . VAL A 85  ? 0.11908 0.11649 0.17748 -0.00400 -0.02254 -0.01247 92  VAL A CA  
617  C C   . VAL A 85  ? 0.17810 0.17708 0.23579 0.00574  -0.01421 -0.00687 92  VAL A C   
618  O O   . VAL A 85  ? 0.16329 0.16567 0.22472 0.01598  -0.00324 0.00363  92  VAL A O   
619  C CB  . VAL A 85  ? 0.14136 0.15523 0.21606 -0.01380 -0.03067 -0.00146 92  VAL A CB  
620  C CG1 . VAL A 85  ? 0.17704 0.19583 0.25035 -0.02093 -0.04028 -0.00088 92  VAL A CG1 
621  C CG2 . VAL A 85  ? 0.21629 0.21717 0.28415 -0.02306 -0.03652 -0.00635 92  VAL A CG2 
622  N N   . ASP A 86  ? 0.14823 0.14314 0.19974 0.00497  -0.01682 -0.01125 93  ASP A N   
623  C CA  . ASP A 86  ? 0.15565 0.14878 0.20528 0.01536  -0.00782 -0.00351 93  ASP A CA  
624  C C   . ASP A 86  ? 0.14970 0.15779 0.20863 0.01143  -0.01545 0.00099  93  ASP A C   
625  O O   . ASP A 86  ? 0.16349 0.17274 0.21970 0.00079  -0.02649 -0.00638 93  ASP A O   
626  C CB  . ASP A 86  ? 0.16944 0.13102 0.19156 0.01855  -0.00112 -0.01262 93  ASP A CB  
627  C CG  . ASP A 86  ? 0.21584 0.17364 0.23214 0.00798  -0.01037 -0.02218 93  ASP A CG  
628  O OD1 . ASP A 86  ? 0.20358 0.16928 0.22548 0.00777  -0.01277 -0.01964 93  ASP A OD1 
629  O OD2 . ASP A 86  ? 0.21429 0.16497 0.22196 0.00044  -0.01487 -0.02915 93  ASP A OD2 
630  N N   . THR A 87  ? 0.13537 0.15311 0.20213 0.02203  -0.00802 0.01510  94  THR A N   
631  C CA  . THR A 87  ? 0.13142 0.16577 0.20637 0.01912  -0.01551 0.02264  94  THR A CA  
632  C C   . THR A 87  ? 0.17594 0.18840 0.23351 0.02693  -0.00743 0.01832  94  THR A C   
633  O O   . THR A 87  ? 0.15280 0.17422 0.21578 0.03503  -0.00369 0.03096  94  THR A O   
634  C CB  . THR A 87  ? 0.14602 0.21679 0.24870 0.02397  -0.01547 0.04803  94  THR A CB  
635  O OG1 . THR A 87  ? 0.15227 0.21962 0.25791 0.04573  0.00576  0.06105  94  THR A OG1 
636  C CG2 . THR A 87  ? 0.14793 0.24218 0.26812 0.00725  -0.02991 0.05423  94  THR A CG2 
637  N N   . GLY A 88  ? 0.16735 0.15243 0.20453 0.02271  -0.00601 0.00274  95  GLY A N   
638  C CA  . GLY A 88  ? 0.18353 0.14483 0.20233 0.02460  -0.00075 -0.00049 95  GLY A CA  
639  C C   . GLY A 88  ? 0.19322 0.16510 0.21482 0.01709  -0.00954 -0.00256 95  GLY A C   
640  O O   . GLY A 88  ? 0.17254 0.16674 0.20535 0.01340  -0.01846 0.00065  95  GLY A O   
641  N N   . ILE A 89  ? 0.18454 0.13652 0.19119 0.01340  -0.00718 -0.00664 96  ILE A N   
642  C CA  . ILE A 89  ? 0.16408 0.12512 0.17199 0.01003  -0.01122 -0.00479 96  ILE A CA  
643  C C   . ILE A 89  ? 0.17348 0.14954 0.18549 0.00311  -0.01904 -0.01125 96  ILE A C   
644  O O   . ILE A 89  ? 0.19359 0.17789 0.20297 0.00348  -0.02163 -0.00915 96  ILE A O   
645  C CB  . ILE A 89  ? 0.20010 0.13662 0.19259 0.00594  -0.00638 -0.00401 96  ILE A CB  
646  C CG1 . ILE A 89  ? 0.21968 0.16552 0.21404 0.00687  -0.00666 0.00266  96  ILE A CG1 
647  C CG2 . ILE A 89  ? 0.20320 0.13184 0.19005 -0.00810 -0.01114 -0.01062 96  ILE A CG2 
648  C CD1 . ILE A 89  ? 0.25626 0.17394 0.23485 0.00414  -0.00044 0.00734  96  ILE A CD1 
649  N N   . GLY A 90  ? 0.17313 0.14938 0.18704 -0.00097 -0.02112 -0.01798 97  GLY A N   
650  C CA  . GLY A 90  ? 0.18396 0.16790 0.19706 -0.00236 -0.02389 -0.02197 97  GLY A CA  
651  C C   . GLY A 90  ? 0.19189 0.17983 0.20525 -0.00404 -0.02020 -0.01834 97  GLY A C   
652  O O   . GLY A 90  ? 0.20899 0.19288 0.22299 -0.00921 -0.01919 -0.01377 97  GLY A O   
653  N N   . MET A 91  ? 0.17105 0.16501 0.18187 0.00066  -0.01716 -0.01807 98  MET A N   
654  C CA  . MET A 91  ? 0.17546 0.18352 0.19358 0.00214  -0.01104 -0.00819 98  MET A CA  
655  C C   . MET A 91  ? 0.17680 0.18193 0.17980 0.01399  -0.00278 -0.00632 98  MET A C   
656  O O   . MET A 91  ? 0.22289 0.21077 0.20594 0.01970  -0.00240 -0.01444 98  MET A O   
657  C CB  . MET A 91  ? 0.14853 0.16980 0.17935 0.00179  -0.01021 -0.00358 98  MET A CB  
658  C CG  . MET A 91  ? 0.14838 0.16867 0.18606 -0.01283 -0.01925 -0.00372 98  MET A CG  
659  S SD  . MET A 91  ? 0.16899 0.20965 0.22154 -0.01712 -0.02265 0.00516  98  MET A SD  
660  C CE  . MET A 91  ? 0.18873 0.21190 0.23113 -0.00697 -0.02084 -0.00892 98  MET A CE  
661  N N   . THR A 92  ? 0.16621 0.18336 0.17361 0.01634  0.00376  0.00501  99  THR A N   
662  C CA  . THR A 92  ? 0.20472 0.21819 0.19396 0.03168  0.01661  0.01000  99  THR A CA  
663  C C   . THR A 92  ? 0.19341 0.21808 0.18892 0.04475  0.02910  0.01944  99  THR A C   
664  O O   . THR A 92  ? 0.18086 0.22454 0.20075 0.03928  0.02550  0.02506  99  THR A O   
665  C CB  . THR A 92  ? 0.22246 0.25000 0.21810 0.03183  0.02229  0.02342  99  THR A CB  
666  O OG1 . THR A 92  ? 0.22043 0.27865 0.24886 0.02387  0.02299  0.04016  99  THR A OG1 
667  C CG2 . THR A 92  ? 0.24592 0.26221 0.23628 0.02172  0.01196  0.01723  99  THR A CG2 
668  N N   . LYS A 93  ? 0.21397 0.15419 0.19959 0.02091  -0.02136 0.01026  100 LYS A N   
669  C CA  . LYS A 93  ? 0.19456 0.15595 0.17781 0.01900  -0.00627 0.00857  100 LYS A CA  
670  C C   . LYS A 93  ? 0.21967 0.19394 0.20340 0.00971  0.00272  0.00937  100 LYS A C   
671  O O   . LYS A 93  ? 0.20166 0.19305 0.20049 0.01518  0.00754  0.00193  100 LYS A O   
672  C CB  . LYS A 93  ? 0.25444 0.22101 0.21847 0.01805  -0.00454 0.00554  100 LYS A CB  
673  C CG  . LYS A 93  ? 0.21858 0.21064 0.19417 0.02916  -0.00081 -0.01138 100 LYS A CG  
674  C CD  . LYS A 93  ? 0.27392 0.28653 0.23717 0.03002  0.00182  -0.02630 100 LYS A CD  
675  C CE  . LYS A 93  ? 0.27440 0.31058 0.25970 0.05319  -0.00761 -0.05580 100 LYS A CE  
676  N NZ  . LYS A 93  ? 0.32129 0.40619 0.30717 0.05389  0.00019  -0.08630 100 LYS A NZ  
677  N N   . ALA A 94  ? 0.24406 0.20197 0.20394 -0.00812 -0.00051 0.01877  101 ALA A N   
678  C CA  . ALA A 94  ? 0.25812 0.22907 0.21450 -0.02516 0.00822  0.01954  101 ALA A CA  
679  C C   . ALA A 94  ? 0.24860 0.21637 0.23211 -0.01310 0.00490  0.01783  101 ALA A C   
680  O O   . ALA A 94  ? 0.25099 0.24353 0.24792 -0.01605 0.01476  0.01193  101 ALA A O   
681  C CB  . ALA A 94  ? 0.30437 0.23855 0.21064 -0.05849 -0.00189 0.03502  101 ALA A CB  
682  N N   . ASP A 95  ? 0.20580 0.15069 0.20054 -0.00009 -0.01009 0.01655  102 ASP A N   
683  C CA  . ASP A 95  ? 0.19599 0.15137 0.21646 0.00722  -0.00925 0.00725  102 ASP A CA  
684  C C   . ASP A 95  ? 0.18697 0.16849 0.21769 0.00898  0.00488  0.00244  102 ASP A C   
685  O O   . ASP A 95  ? 0.18830 0.17782 0.22499 0.00609  0.00907  0.00007  102 ASP A O   
686  C CB  . ASP A 95  ? 0.25134 0.20452 0.29422 0.02164  -0.02496 -0.00992 102 ASP A CB  
687  C CG  . ASP A 95  ? 0.29257 0.20147 0.32643 0.02872  -0.05760 -0.01197 102 ASP A CG  
688  O OD1 . ASP A 95  ? 0.34027 0.21290 0.34568 0.01540  -0.06791 0.00258  102 ASP A OD1 
689  O OD2 . ASP A 95  ? 0.30384 0.21017 0.35744 0.04704  -0.07950 -0.03175 102 ASP A OD2 
690  N N   . LEU A 96  ? 0.18013 0.16359 0.20570 0.01214  0.00537  0.00136  103 LEU A N   
691  C CA  . LEU A 96  ? 0.19514 0.17691 0.21223 0.00960  0.00452  -0.00030 103 LEU A CA  
692  C C   . LEU A 96  ? 0.19982 0.18606 0.21821 0.01632  0.00163  -0.00288 103 LEU A C   
693  O O   . LEU A 96  ? 0.19783 0.17581 0.21167 0.01489  -0.00543 -0.00474 103 LEU A O   
694  C CB  . LEU A 96  ? 0.21981 0.18809 0.22130 0.01012  -0.00292 0.00033  103 LEU A CB  
695  C CG  . LEU A 96  ? 0.19869 0.17256 0.19924 -0.00290 -0.00077 -0.00398 103 LEU A CG  
696  C CD1 . LEU A 96  ? 0.21487 0.16814 0.19495 -0.00342 -0.01094 -0.00050 103 LEU A CD1 
697  C CD2 . LEU A 96  ? 0.18072 0.16390 0.17073 -0.02844 0.00476  -0.01021 103 LEU A CD2 
698  N N   . ILE A 97  ? 0.17175 0.17659 0.19550 0.02101  0.00570  -0.00815 104 ILE A N   
699  C CA  . ILE A 97  ? 0.17062 0.20432 0.20924 0.02857  0.00376  -0.02587 104 ILE A CA  
700  C C   . ILE A 97  ? 0.15949 0.20702 0.20860 0.01845  0.01087  -0.02500 104 ILE A C   
701  O O   . ILE A 97  ? 0.17965 0.24003 0.24399 0.02795  0.00146  -0.03950 104 ILE A O   
702  C CB  . ILE A 97  ? 0.17866 0.25056 0.22118 0.02607  0.01343  -0.04121 104 ILE A CB  
703  C CG1 . ILE A 97  ? 0.18353 0.24109 0.21991 0.04326  0.00022  -0.04856 104 ILE A CG1 
704  C CG2 . ILE A 97  ? 0.18043 0.31264 0.25129 0.02823  0.01773  -0.07343 104 ILE A CG2 
705  C CD1 . ILE A 97  ? 0.20635 0.30022 0.23671 0.03362  0.01441  -0.06084 104 ILE A CD1 
706  N N   . ASN A 98  ? 0.18619 0.22256 0.22561 0.00159  0.01966  -0.00993 105 ASN A N   
707  C CA  . ASN A 98  ? 0.18816 0.22805 0.23206 -0.01044 0.02272  -0.00763 105 ASN A CA  
708  C C   . ASN A 98  ? 0.18297 0.20173 0.23119 -0.00277 0.01586  -0.00459 105 ASN A C   
709  O O   . ASN A 98  ? 0.19809 0.20132 0.24557 -0.00714 0.01375  -0.00065 105 ASN A O   
710  C CB  . ASN A 98  ? 0.22166 0.24075 0.24086 -0.03375 0.02297  0.00587  105 ASN A CB  
711  C CG  . ASN A 98  ? 0.31323 0.36565 0.31677 -0.06241 0.03569  0.00014  105 ASN A CG  
712  O OD1 . ASN A 98  ? 0.41810 0.49818 0.42418 -0.08367 0.04371  -0.00690 105 ASN A OD1 
713  N ND2 . ASN A 98  ? 0.47428 0.52904 0.45761 -0.06982 0.03904  0.00068  105 ASN A ND2 
714  N N   . ASN A 99  ? 0.17160 0.18628 0.21868 0.00698  0.00744  -0.01027 106 ASN A N   
715  C CA  . ASN A 99  ? 0.17327 0.16988 0.20897 0.00169  0.00183  -0.00852 106 ASN A CA  
716  C C   . ASN A 99  ? 0.21024 0.20494 0.24135 -0.00815 0.00965  -0.00817 106 ASN A C   
717  O O   . ASN A 99  ? 0.20432 0.20669 0.23999 -0.01536 0.01369  -0.01531 106 ASN A O   
718  C CB  . ASN A 99  ? 0.14971 0.15613 0.19687 -0.00080 0.00186  -0.01232 106 ASN A CB  
719  C CG  . ASN A 99  ? 0.16345 0.18861 0.22594 0.01053  -0.00860 -0.02547 106 ASN A CG  
720  O OD1 . ASN A 99  ? 0.19357 0.20199 0.24761 0.02374  -0.02957 -0.03292 106 ASN A OD1 
721  N ND2 . ASN A 99  ? 0.17654 0.23554 0.26028 0.00356  0.00106  -0.03292 106 ASN A ND2 
722  N N   . LEU A 100 ? 0.18374 0.17686 0.21105 -0.00697 0.01050  -0.00712 107 LEU A N   
723  C CA  . LEU A 100 ? 0.17534 0.18348 0.20826 -0.01524 0.01638  -0.01814 107 LEU A CA  
724  C C   . LEU A 100 ? 0.17405 0.19673 0.23573 -0.00594 0.01514  -0.03239 107 LEU A C   
725  O O   . LEU A 100 ? 0.17211 0.22298 0.24840 -0.01163 0.01918  -0.05536 107 LEU A O   
726  C CB  . LEU A 100 ? 0.21070 0.22152 0.21581 -0.04229 0.02005  -0.02330 107 LEU A CB  
727  C CG  . LEU A 100 ? 0.30760 0.27598 0.27130 -0.04962 0.00466  -0.00689 107 LEU A CG  
728  C CD1 . LEU A 100 ? 0.30147 0.23074 0.23649 -0.04956 -0.01545 0.00194  107 LEU A CD1 
729  C CD2 . LEU A 100 ? 0.44073 0.40557 0.37130 -0.08133 0.00616  -0.00857 107 LEU A CD2 
730  N N   . GLY A 101 ? 0.18473 0.18664 0.24916 0.00455  0.00593  -0.02249 108 GLY A N   
731  C CA  . GLY A 101 ? 0.19784 0.18553 0.27574 0.01425  -0.01127 -0.03304 108 GLY A CA  
732  C C   . GLY A 101 ? 0.22924 0.21831 0.31518 0.01306  -0.01368 -0.04152 108 GLY A C   
733  O O   . GLY A 101 ? 0.25691 0.23841 0.36103 0.02652  -0.03386 -0.06287 108 GLY A O   
734  N N   . THR A 102 ? 0.20971 0.20574 0.28483 0.00135  -0.00012 -0.03026 109 THR A N   
735  C CA  . THR A 102 ? 0.20494 0.20270 0.28486 -0.00179 -0.00145 -0.03704 109 THR A CA  
736  C C   . THR A 102 ? 0.19579 0.17489 0.26380 -0.01089 -0.00451 -0.01916 109 THR A C   
737  O O   . THR A 102 ? 0.24695 0.22842 0.30468 -0.01800 0.00110  -0.00655 109 THR A O   
738  C CB  . THR A 102 ? 0.17383 0.19276 0.24434 -0.01346 0.01171  -0.04163 109 THR A CB  
739  O OG1 . THR A 102 ? 0.19829 0.20651 0.25102 -0.01727 0.01237  -0.02397 109 THR A OG1 
740  C CG2 . THR A 102 ? 0.27220 0.31976 0.34209 -0.02277 0.02101  -0.06044 109 THR A CG2 
741  N N   . ILE A 103 ? 0.17795 0.14815 0.24882 -0.01413 -0.01180 -0.02370 110 ILE A N   
742  C CA  . ILE A 103 ? 0.18555 0.15317 0.24744 -0.03086 -0.01030 -0.01198 110 ILE A CA  
743  C C   . ILE A 103 ? 0.16873 0.16392 0.24032 -0.02907 -0.00086 -0.01780 110 ILE A C   
744  O O   . ILE A 103 ? 0.17213 0.16638 0.24704 -0.03324 -0.00494 -0.02233 110 ILE A O   
745  C CB  . ILE A 103 ? 0.23982 0.16696 0.28905 -0.04032 -0.03142 -0.01013 110 ILE A CB  
746  C CG1 . ILE A 103 ? 0.23185 0.15246 0.29904 -0.02139 -0.04491 -0.03262 110 ILE A CG1 
747  C CG2 . ILE A 103 ? 0.27262 0.15011 0.29351 -0.04636 -0.05339 0.00063  110 ILE A CG2 
748  C CD1 . ILE A 103 ? 0.29964 0.16959 0.35078 -0.03037 -0.07377 -0.03149 110 ILE A CD1 
749  N N   . ALA A 104 ? 0.29176 0.12735 0.23913 0.05647  0.03253  0.01446  111 ALA A N   
750  C CA  . ALA A 104 ? 0.26663 0.13052 0.23458 0.06235  0.03432  0.01445  111 ALA A CA  
751  C C   . ALA A 104 ? 0.24781 0.16578 0.24448 0.06086  0.05189  0.02296  111 ALA A C   
752  O O   . ALA A 104 ? 0.23021 0.19282 0.25606 0.05421  0.04584  0.02064  111 ALA A O   
753  C CB  . ALA A 104 ? 0.27495 0.13730 0.22253 0.06921  0.02079  0.01408  111 ALA A CB  
754  N N   . LYS A 105 ? 0.26217 0.18107 0.25236 0.06708  0.07303  0.03429  112 LYS A N   
755  C CA  . LYS A 105 ? 0.26533 0.25190 0.29926 0.06236  0.08901  0.04452  112 LYS A CA  
756  C C   . LYS A 105 ? 0.25670 0.27926 0.33343 0.02721  0.08038  0.03751  112 LYS A C   
757  O O   . LYS A 105 ? 0.19332 0.27052 0.30632 0.01814  0.07113  0.03611  112 LYS A O   
758  C CB  . LYS A 105 ? 0.27694 0.26302 0.30021 0.07364  0.11948  0.06050  112 LYS A CB  
759  C CG  . LYS A 105 ? 0.29104 0.35954 0.36933 0.07361  0.13864  0.07514  112 LYS A CG  
760  C CD  . LYS A 105 ? 0.32883 0.39931 0.39980 0.08026  0.17446  0.09237  112 LYS A CD  
761  C CE  . LYS A 105 ? 0.43809 0.60219 0.58203 0.06559  0.19110  0.10791  112 LYS A CE  
762  N NZ  . LYS A 105 ? 0.55602 0.72932 0.68577 0.09691  0.21149  0.11861  112 LYS A NZ  
763  N N   . SER A 106 ? 0.23623 0.22099 0.30226 0.00796  0.08030  0.03228  113 SER A N   
764  C CA  . SER A 106 ? 0.23976 0.24527 0.33639 -0.02513 0.07171  0.02346  113 SER A CA  
765  C C   . SER A 106 ? 0.25777 0.26017 0.35323 -0.02856 0.04972  0.00529  113 SER A C   
766  O O   . SER A 106 ? 0.24581 0.27942 0.36388 -0.04996 0.03979  -0.00298 113 SER A O   
767  C CB  . SER A 106 ? 0.32567 0.28110 0.40559 -0.04349 0.07832  0.02337  113 SER A CB  
768  O OG  . SER A 106 ? 0.36680 0.25907 0.40878 -0.02952 0.06789  0.01413  113 SER A OG  
769  N N   . GLY A 107 ? 0.23303 0.19978 0.30141 -0.00935 0.04182  -0.00047 114 GLY A N   
770  C CA  . GLY A 107 ? 0.20593 0.17684 0.27576 -0.01205 0.02685  -0.01461 114 GLY A CA  
771  C C   . GLY A 107 ? 0.17884 0.19994 0.26364 -0.00964 0.02121  -0.01117 114 GLY A C   
772  O O   . GLY A 107 ? 0.18096 0.22155 0.27208 -0.02285 0.01135  -0.02137 114 GLY A O   
773  N N   . THR A 108 ? 0.15933 0.19598 0.24306 0.01025  0.02690  0.00305  115 THR A N   
774  C CA  . THR A 108 ? 0.15248 0.23449 0.24939 0.01755  0.01979  0.00908  115 THR A CA  
775  C C   . THR A 108 ? 0.18842 0.32770 0.32279 -0.00311 0.01588  0.01044  115 THR A C   
776  O O   . THR A 108 ? 0.17123 0.34126 0.31221 -0.01003 0.00036  0.00709  115 THR A O   
777  C CB  . THR A 108 ? 0.24557 0.32710 0.33212 0.04827  0.02920  0.02448  115 THR A CB  
778  O OG1 . THR A 108 ? 0.23065 0.25359 0.27707 0.06259  0.02577  0.02172  115 THR A OG1 
779  C CG2 . THR A 108 ? 0.21525 0.34334 0.31761 0.05996  0.02152  0.03329  115 THR A CG2 
780  N N   . LYS A 109 ? 0.16920 0.32248 0.32614 -0.01490 0.02851  0.01684  116 LYS A N   
781  C CA  . LYS A 109 ? 0.17164 0.38171 0.37088 -0.04205 0.02221  0.01929  116 LYS A CA  
782  C C   . LYS A 109 ? 0.19040 0.38663 0.37900 -0.07044 0.00224  -0.00072 116 LYS A C   
783  O O   . LYS A 109 ? 0.22645 0.46552 0.43092 -0.08404 -0.01651 -0.00307 116 LYS A O   
784  C CB  . LYS A 109 ? 0.19128 0.40615 0.41203 -0.05760 0.04138  0.02927  116 LYS A CB  
785  C CG  . LYS A 109 ? 0.40986 0.65739 0.66618 -0.10121 0.03137  0.02629  116 LYS A CG  
786  C CD  . LYS A 109 ? 0.26464 0.54316 0.55729 -0.11292 0.05525  0.04660  116 LYS A CD  
787  C CE  . LYS A 109 ? 0.43107 0.74396 0.76281 -0.15543 0.04317  0.04451  116 LYS A CE  
788  N NZ  . LYS A 109 ? 0.57482 0.93928 0.93132 -0.15495 0.01630  0.03920  116 LYS A NZ  
789  N N   . ALA A 110 ? 0.17821 0.31332 0.33754 -0.07840 0.00552  -0.01523 117 ALA A N   
790  C CA  . ALA A 110 ? 0.26238 0.37479 0.40331 -0.10015 -0.00882 -0.03650 117 ALA A CA  
791  C C   . ALA A 110 ? 0.18987 0.31140 0.31064 -0.08754 -0.02057 -0.04322 117 ALA A C   
792  O O   . ALA A 110 ? 0.23647 0.36895 0.34722 -0.10498 -0.03628 -0.05501 117 ALA A O   
793  C CB  . ALA A 110 ? 0.25484 0.29847 0.36884 -0.10116 -0.00020 -0.04904 117 ALA A CB  
794  N N   . PHE A 111 ? 0.19000 0.29948 0.29760 -0.05963 -0.01372 -0.03617 118 PHE A N   
795  C CA  . PHE A 111 ? 0.19112 0.30231 0.27572 -0.05051 -0.02169 -0.04009 118 PHE A CA  
796  C C   . PHE A 111 ? 0.20324 0.36567 0.29745 -0.05276 -0.03760 -0.03141 118 PHE A C   
797  O O   . PHE A 111 ? 0.20797 0.37569 0.28060 -0.06290 -0.05071 -0.04050 118 PHE A O   
798  C CB  . PHE A 111 ? 0.15702 0.24595 0.23022 -0.02495 -0.01339 -0.03018 118 PHE A CB  
799  C CG  . PHE A 111 ? 0.17143 0.25722 0.22164 -0.01795 -0.01786 -0.02998 118 PHE A CG  
800  C CD1 . PHE A 111 ? 0.20362 0.28207 0.23371 -0.02999 -0.01898 -0.04477 118 PHE A CD1 
801  C CD2 . PHE A 111 ? 0.22317 0.30475 0.26511 0.00119  -0.01821 -0.01487 118 PHE A CD2 
802  C CE1 . PHE A 111 ? 0.20923 0.28413 0.21571 -0.02402 -0.01815 -0.04093 118 PHE A CE1 
803  C CE2 . PHE A 111 ? 0.21849 0.28977 0.23663 0.00499  -0.02060 -0.01118 118 PHE A CE2 
804  C CZ  . PHE A 111 ? 0.22451 0.29694 0.22699 -0.00877 -0.01961 -0.02300 118 PHE A CZ  
805  N N   . MET A 112 ? 0.18435 0.38604 0.30976 -0.04209 -0.03677 -0.01345 119 MET A N   
806  C CA  . MET A 112 ? 0.19911 0.45705 0.34078 -0.03958 -0.05494 -0.00241 119 MET A CA  
807  C C   . MET A 112 ? 0.25915 0.54953 0.41658 -0.07346 -0.07478 -0.01188 119 MET A C   
808  O O   . MET A 112 ? 0.26484 0.58361 0.41357 -0.07815 -0.09796 -0.01137 119 MET A O   
809  C CB  . MET A 112 ? 0.25987 0.55558 0.43594 -0.01408 -0.04577 0.01982  119 MET A CB  
810  C CG  . MET A 112 ? 0.21937 0.47833 0.36339 0.01946  -0.03764 0.02799  119 MET A CG  
811  S SD  . MET A 112 ? 0.43188 0.71981 0.60410 0.05576  -0.02127 0.05062  119 MET A SD  
812  C CE  . MET A 112 ? 0.24933 0.47651 0.36786 0.08899  -0.02044 0.05608  119 MET A CE  
813  N N   . GLU A 113 ? 0.20372 0.48563 0.37930 -0.09901 -0.06898 -0.01983 120 GLU A N   
814  C CA  . GLU A 113 ? 0.24340 0.53163 0.41989 -0.13336 -0.08945 -0.03209 120 GLU A CA  
815  C C   . GLU A 113 ? 0.29559 0.53534 0.41295 -0.14151 -0.09976 -0.05513 120 GLU A C   
816  O O   . GLU A 113 ? 0.36663 0.60977 0.46541 -0.15223 -0.12151 -0.06109 120 GLU A O   
817  C CB  . GLU A 113 ? 0.34410 0.61170 0.54123 -0.15682 -0.07874 -0.03486 120 GLU A CB  
818  C CG  . GLU A 113 ? 0.44665 0.76441 0.69986 -0.15033 -0.06448 -0.01153 120 GLU A CG  
819  C CD  . GLU A 113 ? 0.59480 0.88840 0.86361 -0.17445 -0.05052 -0.01131 120 GLU A CD  
820  O OE1 . GLU A 113 ? 0.54414 0.77123 0.77648 -0.18690 -0.04659 -0.02691 120 GLU A OE1 
821  O OE2 . GLU A 113 ? 0.62532 0.96458 0.94145 -0.17791 -0.04141 0.00539  120 GLU A OE2 
822  N N   . ALA A 114 ? 0.26714 0.45386 0.35212 -0.13133 -0.08142 -0.06747 121 ALA A N   
823  C CA  . ALA A 114 ? 0.29401 0.43811 0.32362 -0.13398 -0.08403 -0.08849 121 ALA A CA  
824  C C   . ALA A 114 ? 0.30694 0.47554 0.31112 -0.12164 -0.09724 -0.08136 121 ALA A C   
825  O O   . ALA A 114 ? 0.38136 0.53622 0.34381 -0.13322 -0.11188 -0.09412 121 ALA A O   
826  C CB  . ALA A 114 ? 0.28208 0.37423 0.29466 -0.11590 -0.05821 -0.09623 121 ALA A CB  
827  N N   . LEU A 115 ? 0.27214 0.46729 0.29488 -0.09555 -0.09227 -0.05900 122 LEU A N   
828  C CA  . LEU A 115 ? 0.28361 0.49236 0.27638 -0.08171 -0.10409 -0.04877 122 LEU A CA  
829  C C   . LEU A 115 ? 0.41765 0.66978 0.41366 -0.09658 -0.13672 -0.04564 122 LEU A C   
830  O O   . LEU A 115 ? 0.39461 0.63186 0.34323 -0.09755 -0.14998 -0.04949 122 LEU A O   
831  C CB  . LEU A 115 ? 0.25014 0.47022 0.26169 -0.05120 -0.09453 -0.02493 122 LEU A CB  
832  C CG  . LEU A 115 ? 0.24689 0.42118 0.24755 -0.03718 -0.06887 -0.02581 122 LEU A CG  
833  C CD1 . LEU A 115 ? 0.30924 0.48612 0.32512 -0.01061 -0.06320 -0.00449 122 LEU A CD1 
834  C CD2 . LEU A 115 ? 0.25841 0.40113 0.20884 -0.03930 -0.06259 -0.03389 122 LEU A CD2 
835  N N   . GLN A 116 ? 0.33392 0.62426 0.38629 -0.10249 -0.14362 -0.03586 123 GLN A N   
836  C CA  . GLN A 116 ? 0.34036 0.66282 0.40680 -0.11011 -0.17065 -0.03011 123 GLN A CA  
837  C C   . GLN A 116 ? 0.39901 0.68569 0.42821 -0.13851 -0.18582 -0.05383 123 GLN A C   
838  O O   . GLN A 116 ? 0.47096 0.77144 0.48849 -0.14450 -0.21301 -0.05444 123 GLN A O   
839  C CB  . GLN A 116 ? 0.31502 0.69253 0.45656 -0.10793 -0.16899 -0.01299 123 GLN A CB  
840  C CG  . GLN A 116 ? 0.51799 0.89306 0.69788 -0.13157 -0.15518 -0.01931 123 GLN A CG  
841  C CD  . GLN A 116 ? 0.63631 0.98463 0.80249 -0.16759 -0.17137 -0.03947 123 GLN A CD  
842  O OE1 . GLN A 116 ? 0.75772 1.11614 0.91083 -0.17789 -0.19904 -0.04481 123 GLN A OE1 
843  N NE2 . GLN A 116 ? 0.35702 0.66844 0.52585 -0.18541 -0.15513 -0.04980 123 GLN A NE2 
844  N N   . ALA A 117 ? 0.47038 0.70594 0.47606 -0.15239 -0.16916 -0.07408 124 ALA A N   
845  C CA  . ALA A 117 ? 0.50318 0.69021 0.46641 -0.17372 -0.17854 -0.09878 124 ALA A CA  
846  C C   . ALA A 117 ? 0.70975 0.84752 0.59606 -0.16393 -0.17173 -0.11452 124 ALA A C   
847  O O   . ALA A 117 ? 0.68867 0.77999 0.53018 -0.17483 -0.17568 -0.13659 124 ALA A O   
848  C CB  . ALA A 117 ? 0.53459 0.68559 0.51374 -0.18857 -0.16192 -0.11049 124 ALA A CB  
849  N N   . GLY A 118 ? 0.55071 0.69610 0.41978 -0.14239 -0.15894 -0.10329 125 GLY A N   
850  C CA  . GLY A 118 ? 0.52219 0.62802 0.32074 -0.13236 -0.14829 -0.11347 125 GLY A CA  
851  C C   . GLY A 118 ? 0.51973 0.60149 0.30719 -0.11893 -0.11298 -0.11737 125 GLY A C   
852  O O   . GLY A 118 ? 0.58108 0.63664 0.31595 -0.10884 -0.09771 -0.12185 125 GLY A O   
853  N N   . ALA A 119 ? 0.44406 0.53438 0.27969 -0.11758 -0.09807 -0.11547 126 ALA A N   
854  C CA  . ALA A 119 ? 0.40145 0.47037 0.23960 -0.09824 -0.06584 -0.11412 126 ALA A CA  
855  C C   . ALA A 119 ? 0.42728 0.51597 0.26285 -0.07933 -0.06222 -0.08960 126 ALA A C   
856  O O   . ALA A 119 ? 0.41422 0.53411 0.25206 -0.07729 -0.08404 -0.07298 126 ALA A O   
857  C CB  . ALA A 119 ? 0.37485 0.44224 0.26897 -0.09390 -0.05372 -0.11038 126 ALA A CB  
858  N N   . ASP A 120 ? 0.37802 0.44894 0.21408 -0.06513 -0.03565 -0.08520 127 ASP A N   
859  C CA  . ASP A 120 ? 0.35261 0.43233 0.18687 -0.05119 -0.03178 -0.06082 127 ASP A CA  
860  C C   . ASP A 120 ? 0.34534 0.41892 0.22366 -0.04022 -0.01583 -0.05183 127 ASP A C   
861  O O   . ASP A 120 ? 0.30909 0.37243 0.21516 -0.04132 -0.00632 -0.06424 127 ASP A O   
862  C CB  . ASP A 120 ? 0.40052 0.46338 0.18006 -0.05072 -0.01706 -0.06038 127 ASP A CB  
863  C CG  . ASP A 120 ? 0.56782 0.61142 0.34990 -0.04887 0.01471  -0.07494 127 ASP A CG  
864  O OD1 . ASP A 120 ? 0.65508 0.68182 0.41942 -0.05407 0.02001  -0.09969 127 ASP A OD1 
865  O OD2 . ASP A 120 ? 0.45073 0.49580 0.25581 -0.04186 0.03301  -0.06130 127 ASP A OD2 
866  N N   . ILE A 121 ? 0.31085 0.38483 0.19066 -0.02964 -0.01628 -0.02938 128 ILE A N   
867  C CA  . ILE A 121 ? 0.25541 0.31899 0.17034 -0.02079 -0.00933 -0.01991 128 ILE A CA  
868  C C   . ILE A 121 ? 0.29205 0.34277 0.22306 -0.02398 0.01127  -0.02951 128 ILE A C   
869  O O   . ILE A 121 ? 0.27557 0.31798 0.23931 -0.01940 0.01264  -0.02901 128 ILE A O   
870  C CB  . ILE A 121 ? 0.27333 0.32710 0.17390 -0.01063 -0.01565 0.00457  128 ILE A CB  
871  C CG1 . ILE A 121 ? 0.35115 0.42272 0.25774 0.00214  -0.03574 0.01432  128 ILE A CG1 
872  C CG2 . ILE A 121 ? 0.29214 0.32160 0.21237 -0.00752 -0.00743 0.01286  128 ILE A CG2 
873  C CD1 . ILE A 121 ? 0.38125 0.44107 0.25990 0.01694  -0.04609 0.03780  128 ILE A CD1 
874  N N   . SER A 122 ? 0.28413 0.33439 0.19204 -0.02962 0.02769  -0.03775 129 SER A N   
875  C CA  . SER A 122 ? 0.33236 0.38093 0.26593 -0.02822 0.04906  -0.04484 129 SER A CA  
876  C C   . SER A 122 ? 0.30435 0.34562 0.26532 -0.02417 0.04828  -0.06306 129 SER A C   
877  O O   . SER A 122 ? 0.30903 0.34990 0.30163 -0.01812 0.06021  -0.06623 129 SER A O   
878  C CB  . SER A 122 ? 0.31189 0.36410 0.21448 -0.03073 0.07290  -0.05158 129 SER A CB  
879  O OG  . SER A 122 ? 0.36726 0.40892 0.24142 -0.03052 0.07532  -0.07606 129 SER A OG  
880  N N   . MET A 123 ? 0.25244 0.28877 0.20322 -0.02833 0.03395  -0.07341 130 MET A N   
881  C CA  . MET A 123 ? 0.25025 0.27054 0.21894 -0.02789 0.03374  -0.08946 130 MET A CA  
882  C C   . MET A 123 ? 0.24883 0.26562 0.25175 -0.02338 0.02371  -0.07845 130 MET A C   
883  O O   . MET A 123 ? 0.24233 0.24153 0.25747 -0.02350 0.02309  -0.08758 130 MET A O   
884  C CB  . MET A 123 ? 0.28708 0.29972 0.22704 -0.04093 0.02297  -0.10583 130 MET A CB  
885  C CG  . MET A 123 ? 0.37195 0.37540 0.26385 -0.04315 0.03413  -0.12038 130 MET A CG  
886  S SD  . MET A 123 ? 0.45981 0.45267 0.30384 -0.06314 0.01247  -0.13756 130 MET A SD  
887  C CE  . MET A 123 ? 0.51182 0.47144 0.37812 -0.07002 0.01047  -0.15542 130 MET A CE  
888  N N   . ILE A 124 ? 0.18997 0.21416 0.20188 -0.01812 0.01810  -0.05936 131 ILE A N   
889  C CA  . ILE A 124 ? 0.17224 0.18739 0.20152 -0.01185 0.00896  -0.04923 131 ILE A CA  
890  C C   . ILE A 124 ? 0.20060 0.19437 0.25044 -0.00666 0.01228  -0.05494 131 ILE A C   
891  O O   . ILE A 124 ? 0.18200 0.16179 0.23678 -0.00422 0.00753  -0.05283 131 ILE A O   
892  C CB  . ILE A 124 ? 0.20405 0.21695 0.22755 -0.00526 0.00333  -0.03029 131 ILE A CB  
893  C CG1 . ILE A 124 ? 0.18892 0.18515 0.21683 0.00511  -0.00438 -0.02116 131 ILE A CG1 
894  C CG2 . ILE A 124 ? 0.18107 0.18906 0.21254 -0.00736 0.00984  -0.02587 131 ILE A CG2 
895  C CD1 . ILE A 124 ? 0.22172 0.20499 0.23170 0.01387  -0.01115 -0.00475 131 ILE A CD1 
896  N N   . GLY A 125 ? 0.20083 0.19379 0.26375 -0.00318 0.02054  -0.05913 132 GLY A N   
897  C CA  . GLY A 125 ? 0.22792 0.20318 0.31321 0.00553  0.01948  -0.06211 132 GLY A CA  
898  C C   . GLY A 125 ? 0.24402 0.19738 0.32381 0.00612  0.02240  -0.07650 132 GLY A C   
899  O O   . GLY A 125 ? 0.27800 0.20948 0.36448 0.01330  0.01697  -0.07319 132 GLY A O   
900  N N   . GLN A 126 ? 0.22392 0.17867 0.28359 -0.00315 0.02815  -0.08977 133 GLN A N   
901  C CA  . GLN A 126 ? 0.25324 0.17835 0.30184 -0.00835 0.02857  -0.10359 133 GLN A CA  
902  C C   . GLN A 126 ? 0.23832 0.15565 0.28800 -0.01700 0.01873  -0.09268 133 GLN A C   
903  O O   . GLN A 126 ? 0.30068 0.19399 0.33967 -0.02167 0.01687  -0.09185 133 GLN A O   
904  C CB  . GLN A 126 ? 0.31426 0.23852 0.33396 -0.02074 0.03213  -0.12068 133 GLN A CB  
905  C CG  . GLN A 126 ? 0.33031 0.25400 0.34122 -0.00776 0.04928  -0.13292 133 GLN A CG  
906  C CD  . GLN A 126 ? 0.45584 0.36659 0.42313 -0.01680 0.05226  -0.14975 133 GLN A CD  
907  O OE1 . GLN A 126 ? 0.49235 0.37505 0.43868 -0.02776 0.04101  -0.15560 133 GLN A OE1 
908  N NE2 . GLN A 126 ? 0.51264 0.44317 0.46112 -0.01436 0.06495  -0.15399 133 GLN A NE2 
909  N N   . PHE A 127 ? 0.21211 0.15213 0.26767 -0.01643 0.01314  -0.07721 134 PHE A N   
910  C CA  . PHE A 127 ? 0.21369 0.15393 0.27177 -0.02064 0.00985  -0.06549 134 PHE A CA  
911  C C   . PHE A 127 ? 0.24367 0.16467 0.30181 -0.00521 0.00816  -0.05216 134 PHE A C   
912  O O   . PHE A 127 ? 0.24197 0.16117 0.29588 -0.00345 0.00976  -0.04074 134 PHE A O   
913  C CB  . PHE A 127 ? 0.18659 0.16735 0.24629 -0.02749 0.00542  -0.05831 134 PHE A CB  
914  C CG  . PHE A 127 ? 0.20675 0.20184 0.25881 -0.04499 0.00119  -0.07223 134 PHE A CG  
915  C CD1 . PHE A 127 ? 0.24589 0.23827 0.30154 -0.06547 -0.00227 -0.07861 134 PHE A CD1 
916  C CD2 . PHE A 127 ? 0.22890 0.23269 0.26469 -0.04303 0.00079  -0.07930 134 PHE A CD2 
917  C CE1 . PHE A 127 ? 0.26581 0.26121 0.30595 -0.08474 -0.01088 -0.09421 134 PHE A CE1 
918  C CE2 . PHE A 127 ? 0.26300 0.27039 0.27795 -0.05842 -0.00437 -0.09432 134 PHE A CE2 
919  C CZ  . PHE A 127 ? 0.28708 0.28740 0.30233 -0.07945 -0.01232 -0.10345 134 PHE A CZ  
920  N N   . GLY A 128 ? 0.20886 0.11955 0.26796 0.00551  0.00474  -0.05120 135 GLY A N   
921  C CA  . GLY A 128 ? 0.21532 0.11012 0.25730 0.01536  -0.00168 -0.03584 135 GLY A CA  
922  C C   . GLY A 128 ? 0.26317 0.15858 0.29598 0.02081  -0.00603 -0.02587 135 GLY A C   
923  O O   . GLY A 128 ? 0.28148 0.16221 0.29436 0.02560  -0.00588 -0.01609 135 GLY A O   
924  N N   . VAL A 129 ? 0.20190 0.11312 0.24685 0.02025  -0.00705 -0.02851 136 VAL A N   
925  C CA  . VAL A 129 ? 0.19789 0.10297 0.22456 0.02838  -0.01204 -0.01681 136 VAL A CA  
926  C C   . VAL A 129 ? 0.21213 0.12741 0.24275 0.02370  -0.01730 -0.01454 136 VAL A C   
927  O O   . VAL A 129 ? 0.20940 0.12302 0.22342 0.02737  -0.02002 -0.00565 136 VAL A O   
928  C CB  . VAL A 129 ? 0.20397 0.13006 0.22534 0.03226  -0.00420 -0.01099 136 VAL A CB  
929  C CG1 . VAL A 129 ? 0.23075 0.14267 0.24730 0.03591  0.00421  -0.00825 136 VAL A CG1 
930  C CG2 . VAL A 129 ? 0.20364 0.17174 0.24185 0.01966  -0.00136 -0.01715 136 VAL A CG2 
931  N N   . GLY A 130 ? 0.23949 0.14833 0.24794 -0.01157 -0.04502 -0.06501 137 GLY A N   
932  C CA  . GLY A 130 ? 0.24544 0.17156 0.24049 0.00486  -0.03646 -0.07055 137 GLY A CA  
933  C C   . GLY A 130 ? 0.21223 0.15898 0.20998 0.00426  -0.02152 -0.05759 137 GLY A C   
934  O O   . GLY A 130 ? 0.20752 0.17272 0.19852 0.01167  -0.01544 -0.05699 137 GLY A O   
935  N N   . PHE A 131 ? 0.19401 0.13745 0.20081 -0.00453 -0.01690 -0.04669 138 PHE A N   
936  C CA  . PHE A 131 ? 0.19088 0.14932 0.19973 -0.00481 -0.00616 -0.03699 138 PHE A CA  
937  C C   . PHE A 131 ? 0.16278 0.13758 0.17207 -0.00512 -0.00387 -0.03548 138 PHE A C   
938  O O   . PHE A 131 ? 0.16505 0.14979 0.17134 -0.00059 0.00156  -0.03098 138 PHE A O   
939  C CB  . PHE A 131 ? 0.20050 0.15552 0.21705 -0.01391 -0.00363 -0.02773 138 PHE A CB  
940  C CG  . PHE A 131 ? 0.17397 0.14209 0.19169 -0.01352 0.00378  -0.02164 138 PHE A CG  
941  C CD1 . PHE A 131 ? 0.18976 0.15904 0.20443 -0.00835 0.00763  -0.01932 138 PHE A CD1 
942  C CD2 . PHE A 131 ? 0.16257 0.14305 0.18548 -0.01746 0.00527  -0.01913 138 PHE A CD2 
943  C CE1 . PHE A 131 ? 0.17723 0.15272 0.19292 -0.00825 0.01066  -0.01524 138 PHE A CE1 
944  C CE2 . PHE A 131 ? 0.15252 0.14042 0.17452 -0.01358 0.00949  -0.01660 138 PHE A CE2 
945  C CZ  . PHE A 131 ? 0.16695 0.14900 0.18491 -0.00964 0.01093  -0.01512 138 PHE A CZ  
946  N N   . TYR A 132 ? 0.17810 0.15585 0.19290 -0.01128 -0.00928 -0.03762 139 TYR A N   
947  C CA  . TYR A 132 ? 0.14837 0.14269 0.16541 -0.01036 -0.00763 -0.03515 139 TYR A CA  
948  C C   . TYR A 132 ? 0.18364 0.18498 0.18988 -0.00130 -0.00910 -0.03898 139 TYR A C   
949  O O   . TYR A 132 ? 0.18152 0.19403 0.18765 0.00143  -0.00771 -0.03442 139 TYR A O   
950  C CB  . TYR A 132 ? 0.14935 0.15192 0.17818 -0.01940 -0.01323 -0.03541 139 TYR A CB  
951  C CG  . TYR A 132 ? 0.16230 0.16650 0.20128 -0.02827 -0.00942 -0.02739 139 TYR A CG  
952  C CD1 . TYR A 132 ? 0.15986 0.17940 0.20246 -0.02585 -0.00224 -0.02186 139 TYR A CD1 
953  C CD2 . TYR A 132 ? 0.19031 0.18008 0.23334 -0.03743 -0.01433 -0.02562 139 TYR A CD2 
954  C CE1 . TYR A 132 ? 0.15604 0.18288 0.20481 -0.03199 0.00224  -0.01434 139 TYR A CE1 
955  C CE2 . TYR A 132 ? 0.18526 0.17953 0.23585 -0.04594 -0.01054 -0.01510 139 TYR A CE2 
956  C CZ  . TYR A 132 ? 0.19134 0.20686 0.24378 -0.04270 -0.00129 -0.00965 139 TYR A CZ  
957  O OH  . TYR A 132 ? 0.19049 0.21514 0.24730 -0.04928 0.00310  0.00073  139 TYR A OH  
958  N N   . SER A 133 ? 0.16826 0.16443 0.16427 0.00523  -0.01175 -0.04649 140 SER A N   
959  C CA  . SER A 133 ? 0.16836 0.17820 0.15130 0.01562  -0.01064 -0.04772 140 SER A CA  
960  C C   . SER A 133 ? 0.15018 0.16969 0.13272 0.01734  -0.00154 -0.03439 140 SER A C   
961  O O   . SER A 133 ? 0.17944 0.21411 0.15332 0.02309  0.00017  -0.02908 140 SER A O   
962  C CB  . SER A 133 ? 0.22385 0.23102 0.19398 0.02628  -0.01437 -0.06015 140 SER A CB  
963  O OG  . SER A 133 ? 0.22563 0.22854 0.19686 0.02938  -0.00858 -0.05775 140 SER A OG  
964  N N   . ALA A 134 ? 0.15254 0.16413 0.14385 0.01193  0.00294  -0.02789 141 ALA A N   
965  C CA  . ALA A 134 ? 0.16039 0.17700 0.15409 0.01083  0.00782  -0.01525 141 ALA A CA  
966  C C   . ALA A 134 ? 0.16591 0.18677 0.15924 0.01088  0.00512  -0.00890 141 ALA A C   
967  O O   . ALA A 134 ? 0.17447 0.20092 0.16617 0.01110  0.00625  0.00278  141 ALA A O   
968  C CB  . ALA A 134 ? 0.14172 0.14630 0.14459 0.00487  0.00941  -0.01252 141 ALA A CB  
969  N N   . TYR A 135 ? 0.14959 0.16894 0.14616 0.01022  0.00050  -0.01514 142 TYR A N   
970  C CA  . TYR A 135 ? 0.16559 0.18884 0.16310 0.01283  -0.00333 -0.00991 142 TYR A CA  
971  C C   . TYR A 135 ? 0.17120 0.20749 0.15777 0.01840  -0.00631 -0.00738 142 TYR A C   
972  O O   . TYR A 135 ? 0.19361 0.23293 0.17941 0.02169  -0.01058 -0.00086 142 TYR A O   
973  C CB  . TYR A 135 ? 0.15204 0.17695 0.15918 0.01175  -0.00641 -0.01611 142 TYR A CB  
974  C CG  . TYR A 135 ? 0.16462 0.18054 0.17879 0.00932  -0.00297 -0.01539 142 TYR A CG  
975  C CD1 . TYR A 135 ? 0.18675 0.19503 0.20206 0.01384  -0.00493 -0.01097 142 TYR A CD1 
976  C CD2 . TYR A 135 ? 0.14432 0.15725 0.16185 0.00350  0.00040  -0.01913 142 TYR A CD2 
977  C CE1 . TYR A 135 ? 0.19719 0.19701 0.21551 0.01382  -0.00344 -0.01292 142 TYR A CE1 
978  C CE2 . TYR A 135 ? 0.15750 0.16529 0.17827 0.00256  0.00332  -0.01823 142 TYR A CE2 
979  C CZ  . TYR A 135 ? 0.20177 0.20417 0.22206 0.00829  0.00152  -0.01637 142 TYR A CZ  
980  O OH  . TYR A 135 ? 0.16371 0.16157 0.18439 0.00925  0.00287  -0.01828 142 TYR A OH  
981  N N   . LEU A 136 ? 0.17061 0.21518 0.14706 0.02155  -0.00462 -0.01204 143 LEU A N   
982  C CA  . LEU A 136 ? 0.17543 0.23729 0.13761 0.02866  -0.00562 -0.00734 143 LEU A CA  
983  C C   . LEU A 136 ? 0.18307 0.25040 0.14435 0.02710  -0.00143 0.01272  143 LEU A C   
984  O O   . LEU A 136 ? 0.21303 0.29265 0.16553 0.03062  -0.00365 0.02349  143 LEU A O   
985  C CB  . LEU A 136 ? 0.20080 0.27252 0.15054 0.03579  -0.00413 -0.01862 143 LEU A CB  
986  C CG  . LEU A 136 ? 0.20727 0.27051 0.15564 0.03717  -0.01304 -0.03867 143 LEU A CG  
987  C CD1 . LEU A 136 ? 0.20405 0.26878 0.14045 0.04649  -0.01345 -0.05209 143 LEU A CD1 
988  C CD2 . LEU A 136 ? 0.21396 0.28611 0.15787 0.03931  -0.02290 -0.04263 143 LEU A CD2 
989  N N   . VAL A 137 ? 0.18405 0.24309 0.15467 0.02080  0.00336  0.01947  144 VAL A N   
990  C CA  . VAL A 137 ? 0.18869 0.25530 0.16064 0.01642  0.00585  0.04021  144 VAL A CA  
991  C C   . VAL A 137 ? 0.16911 0.21205 0.15501 0.00785  0.00160  0.04810  144 VAL A C   
992  O O   . VAL A 137 ? 0.20670 0.24791 0.19625 0.00185  -0.00130 0.06689  144 VAL A O   
993  C CB  . VAL A 137 ? 0.17277 0.26146 0.14244 0.01732  0.01450  0.04442  144 VAL A CB  
994  C CG1 . VAL A 137 ? 0.19066 0.30505 0.14216 0.03007  0.01731  0.03543  144 VAL A CG1 
995  C CG2 . VAL A 137 ? 0.19475 0.27130 0.17448 0.01488  0.01734  0.03283  144 VAL A CG2 
996  N N   . ALA A 138 ? 0.18835 0.21348 0.18111 0.00755  -0.00038 0.03460  145 ALA A N   
997  C CA  . ALA A 138 ? 0.18680 0.18993 0.18975 0.00260  -0.00518 0.03716  145 ALA A CA  
998  C C   . ALA A 138 ? 0.20193 0.19128 0.20616 0.00842  -0.01263 0.03115  145 ALA A C   
999  O O   . ALA A 138 ? 0.21365 0.21002 0.21679 0.01344  -0.01124 0.01873  145 ALA A O   
1000 C CB  . ALA A 138 ? 0.18896 0.18710 0.19723 -0.00007 -0.00103 0.02679  145 ALA A CB  
1001 N N   . GLU A 139 ? 0.20596 0.17545 0.21432 0.00769  -0.02159 0.03914  146 GLU A N   
1002 C CA  . GLU A 139 ? 0.20559 0.16099 0.21556 0.01727  -0.02969 0.03053  146 GLU A CA  
1003 C C   . GLU A 139 ? 0.21352 0.16118 0.22748 0.01961  -0.02859 0.01601  146 GLU A C   
1004 O O   . GLU A 139 ? 0.23725 0.18734 0.25205 0.02966  -0.03023 0.00454  146 GLU A O   
1005 C CB  . GLU A 139 ? 0.26297 0.19472 0.27412 0.01848  -0.04308 0.04316  146 GLU A CB  
1006 C CG  . GLU A 139 ? 0.31232 0.22224 0.32969 0.00852  -0.04933 0.05072  146 GLU A CG  
1007 C CD  . GLU A 139 ? 0.59510 0.47915 0.61539 0.00453  -0.06467 0.06856  146 GLU A CD  
1008 O OE1 . GLU A 139 ? 0.53317 0.41877 0.54877 0.01006  -0.06887 0.07755  146 GLU A OE1 
1009 O OE2 . GLU A 139 ? 0.49423 0.35596 0.52205 -0.00514 -0.07389 0.07453  146 GLU A OE2 
1010 N N   . LYS A 140 ? 0.20517 0.14775 0.22158 0.01147  -0.02587 0.01696  147 LYS A N   
1011 C CA  . LYS A 140 ? 0.19243 0.12963 0.20995 0.01377  -0.02505 0.00449  147 LYS A CA  
1012 C C   . LYS A 140 ? 0.19858 0.14577 0.21734 0.00479  -0.01663 0.00610  147 LYS A C   
1013 O O   . LYS A 140 ? 0.19277 0.14341 0.21383 -0.00286 -0.01550 0.01744  147 LYS A O   
1014 C CB  . LYS A 140 ? 0.20074 0.11131 0.21933 0.01652  -0.03773 0.00252  147 LYS A CB  
1015 C CG  . LYS A 140 ? 0.20848 0.11703 0.22446 0.02132  -0.03724 -0.01177 147 LYS A CG  
1016 C CD  . LYS A 140 ? 0.29533 0.17563 0.30925 0.02924  -0.05299 -0.01893 147 LYS A CD  
1017 C CE  . LYS A 140 ? 0.36836 0.22928 0.38738 0.01632  -0.06192 -0.01075 147 LYS A CE  
1018 N NZ  . LYS A 140 ? 0.48197 0.31429 0.49904 0.02217  -0.07996 -0.01682 147 LYS A NZ  
1019 N N   . VAL A 141 ? 0.17113 0.12610 0.18875 0.00635  -0.01075 -0.00356 148 VAL A N   
1020 C CA  . VAL A 141 ? 0.13925 0.09968 0.15779 -0.00001 -0.00499 -0.00262 148 VAL A CA  
1021 C C   . VAL A 141 ? 0.18760 0.14117 0.20489 0.00147  -0.00701 -0.00952 148 VAL A C   
1022 O O   . VAL A 141 ? 0.17730 0.13439 0.19128 0.00818  -0.00649 -0.01761 148 VAL A O   
1023 C CB  . VAL A 141 ? 0.16816 0.14263 0.18514 -0.00037 0.00242  -0.00590 148 VAL A CB  
1024 C CG1 . VAL A 141 ? 0.16464 0.14069 0.18213 -0.00424 0.00634  -0.00564 148 VAL A CG1 
1025 C CG2 . VAL A 141 ? 0.16780 0.15087 0.18260 0.00059  0.00298  -0.00178 148 VAL A CG2 
1026 N N   . THR A 142 ? 0.17396 0.12217 0.19392 -0.00413 -0.00944 -0.00593 149 THR A N   
1027 C CA  . THR A 142 ? 0.18369 0.12689 0.20056 -0.00268 -0.01245 -0.01245 149 THR A CA  
1028 C C   . THR A 142 ? 0.17875 0.13201 0.19677 -0.00685 -0.00619 -0.00966 149 THR A C   
1029 O O   . THR A 142 ? 0.20348 0.16247 0.22749 -0.01159 -0.00423 -0.00240 149 THR A O   
1030 C CB  . THR A 142 ? 0.19448 0.12027 0.21463 -0.00565 -0.02493 -0.01158 149 THR A CB  
1031 O OG1 . THR A 142 ? 0.24242 0.15301 0.26245 -0.00171 -0.03344 -0.01236 149 THR A OG1 
1032 C CG2 . THR A 142 ? 0.21251 0.13394 0.22589 -0.00146 -0.02973 -0.02162 149 THR A CG2 
1033 N N   . VAL A 143 ? 0.16406 0.12207 0.17622 -0.00401 -0.00282 -0.01429 150 VAL A N   
1034 C CA  . VAL A 143 ? 0.14632 0.10978 0.15893 -0.00673 0.00123  -0.01086 150 VAL A CA  
1035 C C   . VAL A 143 ? 0.19327 0.15472 0.20092 -0.00532 -0.00332 -0.01334 150 VAL A C   
1036 O O   . VAL A 143 ? 0.19030 0.15466 0.18918 -0.00049 -0.00326 -0.01835 150 VAL A O   
1037 C CB  . VAL A 143 ? 0.14882 0.11818 0.15932 -0.00689 0.00741  -0.01037 150 VAL A CB  
1038 C CG1 . VAL A 143 ? 0.21332 0.18140 0.22359 -0.00854 0.00833  -0.00657 150 VAL A CG1 
1039 C CG2 . VAL A 143 ? 0.15945 0.13081 0.17354 -0.00744 0.00948  -0.01027 150 VAL A CG2 
1040 N N   . ILE A 144 ? 0.16815 0.12903 0.18102 -0.00845 -0.00738 -0.00998 151 ILE A N   
1041 C CA  . ILE A 144 ? 0.17627 0.13682 0.18392 -0.00698 -0.01314 -0.01238 151 ILE A CA  
1042 C C   . ILE A 144 ? 0.17207 0.13892 0.17900 -0.00650 -0.00876 -0.00695 151 ILE A C   
1043 O O   . ILE A 144 ? 0.17369 0.14383 0.18900 -0.00758 -0.00587 -0.00241 151 ILE A O   
1044 C CB  . ILE A 144 ? 0.19085 0.14771 0.20746 -0.01179 -0.02345 -0.01155 151 ILE A CB  
1045 C CG1 . ILE A 144 ? 0.24197 0.18753 0.26408 -0.01523 -0.02993 -0.01245 151 ILE A CG1 
1046 C CG2 . ILE A 144 ? 0.22441 0.17968 0.23278 -0.00892 -0.03236 -0.01743 151 ILE A CG2 
1047 C CD1 . ILE A 144 ? 0.28965 0.22232 0.29979 -0.00756 -0.03556 -0.02395 151 ILE A CD1 
1048 N N   . THR A 145 ? 0.15805 0.12731 0.15417 -0.00346 -0.00882 -0.00696 152 THR A N   
1049 C CA  . THR A 145 ? 0.17206 0.14238 0.16790 -0.00329 -0.00653 0.00042  152 THR A CA  
1050 C C   . THR A 145 ? 0.19524 0.16962 0.18071 -0.00035 -0.01120 0.00244  152 THR A C   
1051 O O   . THR A 145 ? 0.20808 0.18716 0.18253 0.00263  -0.01350 -0.00275 152 THR A O   
1052 C CB  . THR A 145 ? 0.17450 0.14300 0.16857 -0.00546 0.00027  0.00445  152 THR A CB  
1053 O OG1 . THR A 145 ? 0.19482 0.15625 0.19059 -0.00564 -0.00064 0.01137  152 THR A OG1 
1054 C CG2 . THR A 145 ? 0.19382 0.17201 0.17724 -0.00513 0.00327  0.00536  152 THR A CG2 
1055 N N   . LYS A 146 ? 0.17423 0.14727 0.16190 0.00093  -0.01324 0.00938  153 LYS A N   
1056 C CA  . LYS A 146 ? 0.18084 0.15845 0.15837 0.00430  -0.01877 0.01347  153 LYS A CA  
1057 C C   . LYS A 146 ? 0.19966 0.17016 0.17734 0.00537  -0.01852 0.02452  153 LYS A C   
1058 O O   . LYS A 146 ? 0.22157 0.18673 0.21038 0.00828  -0.02044 0.02471  153 LYS A O   
1059 C CB  . LYS A 146 ? 0.18409 0.16698 0.16812 0.00597  -0.02819 0.00878  153 LYS A CB  
1060 C CG  . LYS A 146 ? 0.24601 0.23510 0.21954 0.01064  -0.03602 0.01262  153 LYS A CG  
1061 C CD  . LYS A 146 ? 0.24508 0.23976 0.19775 0.01343  -0.03659 0.00946  153 LYS A CD  
1062 C CE  . LYS A 146 ? 0.27906 0.28248 0.21942 0.01902  -0.04602 0.01306  153 LYS A CE  
1063 N NZ  . LYS A 146 ? 0.26844 0.27075 0.20423 0.02059  -0.04377 0.02938  153 LYS A NZ  
1064 N N   . HIS A 147 ? 0.19968 0.17108 0.16530 0.00377  -0.01687 0.03409  154 HIS A N   
1065 C CA  . HIS A 147 ? 0.21033 0.17057 0.17438 0.00314  -0.01952 0.04782  154 HIS A CA  
1066 C C   . HIS A 147 ? 0.26681 0.23440 0.21890 0.00801  -0.02610 0.05535  154 HIS A C   
1067 O O   . HIS A 147 ? 0.28240 0.26648 0.22218 0.00994  -0.02607 0.05163  154 HIS A O   
1068 C CB  . HIS A 147 ? 0.24609 0.20547 0.20698 -0.00593 -0.01343 0.05790  154 HIS A CB  
1069 C CG  . HIS A 147 ? 0.26386 0.20435 0.22660 -0.01058 -0.01841 0.07375  154 HIS A CG  
1070 N ND1 . HIS A 147 ? 0.31120 0.25124 0.26384 -0.01056 -0.02351 0.09011  154 HIS A ND1 
1071 C CD2 . HIS A 147 ? 0.26718 0.18691 0.23986 -0.01629 -0.02074 0.07633  154 HIS A CD2 
1072 C CE1 . HIS A 147 ? 0.35864 0.27477 0.31659 -0.01636 -0.02970 0.10306  154 HIS A CE1 
1073 N NE2 . HIS A 147 ? 0.28818 0.19066 0.25837 -0.01966 -0.02882 0.09345  154 HIS A NE2 
1074 N N   . ASN A 148 ? 0.25620 0.21105 0.21063 0.01203  -0.03328 0.06459  155 ASN A N   
1075 C CA  . ASN A 148 ? 0.26002 0.22214 0.20242 0.01737  -0.04076 0.07351  155 ASN A CA  
1076 C C   . ASN A 148 ? 0.29677 0.27396 0.21956 0.01294  -0.03671 0.08479  155 ASN A C   
1077 O O   . ASN A 148 ? 0.34320 0.33636 0.25103 0.01857  -0.04125 0.08604  155 ASN A O   
1078 C CB  . ASN A 148 ? 0.28381 0.22547 0.23029 0.02269  -0.04978 0.08562  155 ASN A CB  
1079 C CG  . ASN A 148 ? 0.29476 0.23381 0.25747 0.03324  -0.05508 0.07390  155 ASN A CG  
1080 O OD1 . ASN A 148 ? 0.31709 0.27463 0.28644 0.03527  -0.05444 0.06185  155 ASN A OD1 
1081 N ND2 . ASN A 148 ? 0.31065 0.22760 0.28044 0.04048  -0.06148 0.07787  155 ASN A ND2 
1082 N N   . ASP A 149 ? 0.29847 0.27443 0.22090 0.00341  -0.02891 0.09422  156 ASP A N   
1083 C CA  . ASP A 149 ? 0.50320 0.50076 0.40868 -0.00112 -0.02359 0.10975  156 ASP A CA  
1084 C C   . ASP A 149 ? 0.66542 0.69145 0.56136 0.00162  -0.01463 0.09665  156 ASP A C   
1085 O O   . ASP A 149 ? 0.58327 0.63524 0.46511 -0.00002 -0.00807 0.10828  156 ASP A O   
1086 C CB  . ASP A 149 ? 0.49407 0.48018 0.40657 -0.01474 -0.02139 0.13122  156 ASP A CB  
1087 C CG  . ASP A 149 ? 0.51273 0.46875 0.42872 -0.01533 -0.03364 0.14731  156 ASP A CG  
1088 O OD1 . ASP A 149 ? 0.53384 0.48827 0.44227 -0.00452 -0.04163 0.14652  156 ASP A OD1 
1089 O OD2 . ASP A 149 ? 0.62662 0.55928 0.55339 -0.02575 -0.03718 0.15969  156 ASP A OD2 
1090 N N   . ASP A 150 ? 0.45655 0.48004 0.35913 0.00686  -0.01501 0.07376  157 ASP A N   
1091 C CA  . ASP A 150 ? 0.40788 0.45093 0.30301 0.01118  -0.00891 0.05966  157 ASP A CA  
1092 C C   . ASP A 150 ? 0.36128 0.39819 0.25707 0.01936  -0.01726 0.03685  157 ASP A C   
1093 O O   . ASP A 150 ? 0.36358 0.38742 0.26722 0.02015  -0.02633 0.03374  157 ASP A O   
1094 C CB  . ASP A 150 ? 0.42870 0.47059 0.33783 0.00269  0.00049  0.06136  157 ASP A CB  
1095 C CG  . ASP A 150 ? 0.50586 0.57898 0.40482 0.00631  0.00977  0.05896  157 ASP A CG  
1096 O OD1 . ASP A 150 ? 0.43400 0.52302 0.31498 0.01856  0.00732  0.04790  157 ASP A OD1 
1097 O OD2 . ASP A 150 ? 0.34898 0.43212 0.25814 -0.00116 0.01823  0.06528  157 ASP A OD2 
1098 N N   . GLU A 151 ? 0.31173 0.35946 0.19996 0.02570  -0.01554 0.02149  158 GLU A N   
1099 C CA  . GLU A 151 ? 0.31433 0.35125 0.20552 0.03083  -0.02509 0.00061  158 GLU A CA  
1100 C C   . GLU A 151 ? 0.32151 0.34007 0.23515 0.02347  -0.02306 -0.00362 158 GLU A C   
1101 O O   . GLU A 151 ? 0.30239 0.31861 0.22629 0.01684  -0.01390 0.00556  158 GLU A O   
1102 C CB  . GLU A 151 ? 0.34427 0.39559 0.21696 0.04317  -0.02626 -0.01563 158 GLU A CB  
1103 C CG  . GLU A 151 ? 0.63298 0.71583 0.48274 0.05062  -0.01874 -0.00668 158 GLU A CG  
1104 C CD  . GLU A 151 ? 0.73687 0.83756 0.56364 0.06865  -0.02233 -0.02701 158 GLU A CD  
1105 O OE1 . GLU A 151 ? 0.84357 0.97846 0.65013 0.07710  -0.01420 -0.02028 158 GLU A OE1 
1106 O OE2 . GLU A 151 ? 0.86224 0.94343 0.69040 0.07499  -0.03437 -0.04916 158 GLU A OE2 
1107 N N   . GLN A 152 ? 0.25076 0.25715 0.17120 0.02438  -0.03278 -0.01755 159 GLN A N   
1108 C CA  . GLN A 152 ? 0.23569 0.22782 0.17568 0.01769  -0.03121 -0.02018 159 GLN A CA  
1109 C C   . GLN A 152 ? 0.24790 0.24102 0.18384 0.02213  -0.02651 -0.02878 159 GLN A C   
1110 O O   . GLN A 152 ? 0.27812 0.27485 0.19955 0.03220  -0.03209 -0.04162 159 GLN A O   
1111 C CB  . GLN A 152 ? 0.23186 0.21261 0.18327 0.01423  -0.04444 -0.02730 159 GLN A CB  
1112 C CG  . GLN A 152 ? 0.22014 0.19104 0.19278 0.00575  -0.04230 -0.02470 159 GLN A CG  
1113 C CD  . GLN A 152 ? 0.23227 0.20084 0.22124 -0.00135 -0.05374 -0.02376 159 GLN A CD  
1114 O OE1 . GLN A 152 ? 0.27810 0.25599 0.27145 -0.00195 -0.05643 -0.01802 159 GLN A OE1 
1115 N NE2 . GLN A 152 ? 0.25448 0.21191 0.25357 -0.00704 -0.06137 -0.02795 159 GLN A NE2 
1116 N N   . TYR A 153 ? 0.21302 0.20388 0.16081 0.01672  -0.01741 -0.02319 160 TYR A N   
1117 C CA  . TYR A 153 ? 0.23437 0.22927 0.18051 0.02156  -0.01288 -0.02996 160 TYR A CA  
1118 C C   . TYR A 153 ? 0.20925 0.18850 0.17113 0.01627  -0.01431 -0.03159 160 TYR A C   
1119 O O   . TYR A 153 ? 0.20864 0.18110 0.18304 0.00786  -0.01340 -0.02388 160 TYR A O   
1120 C CB  . TYR A 153 ? 0.20495 0.21922 0.14981 0.01965  -0.00009 -0.01934 160 TYR A CB  
1121 C CG  . TYR A 153 ? 0.27367 0.30932 0.20249 0.02421  0.00306  -0.01374 160 TYR A CG  
1122 C CD1 . TYR A 153 ? 0.28730 0.34294 0.20052 0.03735  0.00393  -0.02350 160 TYR A CD1 
1123 C CD2 . TYR A 153 ? 0.31896 0.35516 0.24714 0.01695  0.00423  0.00159  160 TYR A CD2 
1124 C CE1 . TYR A 153 ? 0.35186 0.43371 0.24732 0.04288  0.00764  -0.01708 160 TYR A CE1 
1125 C CE2 . TYR A 153 ? 0.32571 0.38224 0.23812 0.02043  0.00649  0.00979  160 TYR A CE2 
1126 C CZ  . TYR A 153 ? 0.31640 0.39831 0.21200 0.03288  0.00910  0.00122  160 TYR A CZ  
1127 O OH  . TYR A 153 ? 0.46505 0.57410 0.34266 0.03703  0.01278  0.01155  160 TYR A OH  
1128 N N   . ALA A 154 ? 0.21764 0.19386 0.17769 0.02310  -0.01637 -0.04124 161 ALA A N   
1129 C CA  . ALA A 154 ? 0.22142 0.18583 0.19397 0.01935  -0.01691 -0.04068 161 ALA A CA  
1130 C C   . ALA A 154 ? 0.20317 0.18247 0.17559 0.02378  -0.00760 -0.04041 161 ALA A C   
1131 O O   . ALA A 154 ? 0.20863 0.19999 0.17115 0.03573  -0.00730 -0.04914 161 ALA A O   
1132 C CB  . ALA A 154 ? 0.25853 0.20176 0.23110 0.02355  -0.03141 -0.05124 161 ALA A CB  
1133 N N   . TRP A 155 ? 0.18109 0.16179 0.16450 0.01553  -0.00117 -0.03165 162 TRP A N   
1134 C CA  . TRP A 155 ? 0.16510 0.15837 0.15277 0.01739  0.00492  -0.03105 162 TRP A CA  
1135 C C   . TRP A 155 ? 0.18185 0.16064 0.17598 0.01846  -0.00051 -0.03363 162 TRP A C   
1136 O O   . TRP A 155 ? 0.19223 0.15586 0.19128 0.01217  -0.00488 -0.02971 162 TRP A O   
1137 C CB  . TRP A 155 ? 0.18341 0.18481 0.17793 0.00689  0.01234  -0.02025 162 TRP A CB  
1138 C CG  . TRP A 155 ? 0.17397 0.18810 0.17649 0.00435  0.01680  -0.01775 162 TRP A CG  
1139 C CD1 . TRP A 155 ? 0.13711 0.17440 0.14243 0.00162  0.02259  -0.01235 162 TRP A CD1 
1140 C CD2 . TRP A 155 ? 0.17632 0.18382 0.18605 0.00275  0.01503  -0.01869 162 TRP A CD2 
1141 N NE1 . TRP A 155 ? 0.14798 0.19248 0.16385 -0.00235 0.02331  -0.01107 162 TRP A NE1 
1142 C CE2 . TRP A 155 ? 0.14741 0.17325 0.16421 -0.00040 0.01863  -0.01594 162 TRP A CE2 
1143 C CE3 . TRP A 155 ? 0.14887 0.14037 0.15992 0.00325  0.01047  -0.01999 162 TRP A CE3 
1144 C CZ2 . TRP A 155 ? 0.16959 0.19573 0.19314 -0.00192 0.01670  -0.01685 162 TRP A CZ2 
1145 C CZ3 . TRP A 155 ? 0.16832 0.16175 0.18426 0.00221  0.01017  -0.01917 162 TRP A CZ3 
1146 C CH2 . TRP A 155 ? 0.16808 0.17777 0.18929 0.00063  0.01269  -0.01904 162 TRP A CH2 
1147 N N   . GLU A 156 ? 0.16894 0.15520 0.16367 0.02684  -0.00052 -0.03869 163 GLU A N   
1148 C CA  . GLU A 156 ? 0.16381 0.13501 0.16405 0.02745  -0.00663 -0.03823 163 GLU A CA  
1149 C C   . GLU A 156 ? 0.18180 0.16909 0.18609 0.03357  -0.00338 -0.03960 163 GLU A C   
1150 O O   . GLU A 156 ? 0.17462 0.18316 0.17676 0.04251  0.00042  -0.04509 163 GLU A O   
1151 C CB  . GLU A 156 ? 0.21402 0.16215 0.20955 0.03529  -0.01980 -0.04619 163 GLU A CB  
1152 C CG  . GLU A 156 ? 0.26577 0.19263 0.26775 0.03138  -0.02853 -0.04018 163 GLU A CG  
1153 C CD  . GLU A 156 ? 0.37821 0.27689 0.37744 0.03488  -0.04459 -0.04622 163 GLU A CD  
1154 O OE1 . GLU A 156 ? 0.36873 0.25310 0.37473 0.02198  -0.05061 -0.03684 163 GLU A OE1 
1155 O OE2 . GLU A 156 ? 0.36511 0.25743 0.35567 0.05117  -0.05225 -0.06112 163 GLU A OE2 
1156 N N   . SER A 157 ? 0.17495 0.15675 0.18516 0.02926  -0.00477 -0.03391 164 SER A N   
1157 C CA  . SER A 157 ? 0.16683 0.16360 0.18151 0.03587  -0.00418 -0.03552 164 SER A CA  
1158 C C   . SER A 157 ? 0.14842 0.13008 0.16479 0.03536  -0.01081 -0.03032 164 SER A C   
1159 O O   . SER A 157 ? 0.16894 0.14387 0.18586 0.02518  -0.00959 -0.02218 164 SER A O   
1160 C CB  . SER A 157 ? 0.16809 0.18982 0.18947 0.02796  0.00440  -0.03155 164 SER A CB  
1161 O OG  . SER A 157 ? 0.15484 0.19466 0.18294 0.03399  0.00347  -0.03312 164 SER A OG  
1162 N N   . SER A 158 ? 0.17185 0.15281 0.18881 0.04781  -0.01738 -0.03436 165 SER A N   
1163 C CA  . SER A 158 ? 0.19964 0.17379 0.21828 0.04796  -0.02292 -0.02706 165 SER A CA  
1164 C C   . SER A 158 ? 0.18958 0.19109 0.21393 0.05032  -0.01900 -0.02776 165 SER A C   
1165 O O   . SER A 158 ? 0.22727 0.22890 0.25262 0.05794  -0.02560 -0.02569 165 SER A O   
1166 C CB  . SER A 158 ? 0.20747 0.15704 0.22342 0.06017  -0.03646 -0.02931 165 SER A CB  
1167 O OG  . SER A 158 ? 0.28584 0.20883 0.29873 0.05429  -0.04253 -0.02772 165 SER A OG  
1168 N N   . ALA A 159 ? 0.17138 0.19598 0.20058 0.04370  -0.01021 -0.02987 166 ALA A N   
1169 C CA  . ALA A 159 ? 0.16607 0.21976 0.20455 0.04299  -0.00792 -0.03059 166 ALA A CA  
1170 C C   . ALA A 159 ? 0.20001 0.27268 0.24367 0.05963  -0.01029 -0.03727 166 ALA A C   
1171 O O   . ALA A 159 ? 0.23761 0.31025 0.27768 0.06901  -0.00902 -0.04361 166 ALA A O   
1172 C CB  . ALA A 159 ? 0.20364 0.25435 0.24085 0.03797  -0.01199 -0.02548 166 ALA A CB  
1173 N N   . GLY A 160 ? 0.19588 0.28860 0.24761 0.06517  -0.01388 -0.03730 167 GLY A N   
1174 C CA  . GLY A 160 ? 0.20093 0.31853 0.25949 0.08374  -0.01564 -0.04443 167 GLY A CA  
1175 C C   . GLY A 160 ? 0.21347 0.36890 0.28080 0.08351  -0.00570 -0.04698 167 GLY A C   
1176 O O   . GLY A 160 ? 0.22698 0.40652 0.29742 0.10232  -0.00528 -0.05452 167 GLY A O   
1177 N N   . GLY A 161 ? 0.13363 0.29620 0.20480 0.06372  0.00166  -0.04010 168 GLY A N   
1178 C CA  . GLY A 161 ? 0.13670 0.34045 0.21968 0.05786  0.01067  -0.03626 168 GLY A CA  
1179 C C   . GLY A 161 ? 0.12993 0.33380 0.20310 0.06011  0.01808  -0.03732 168 GLY A C   
1180 O O   . GLY A 161 ? 0.12765 0.36968 0.20934 0.05541  0.02648  -0.03132 168 GLY A O   
1181 N N   . SER A 162 ? 0.20303 0.18081 0.16588 0.07185  -0.00040 -0.02631 169 SER A N   
1182 C CA  . SER A 162 ? 0.19901 0.17084 0.16533 0.05885  -0.00029 -0.02906 169 SER A CA  
1183 C C   . SER A 162 ? 0.21277 0.18635 0.18110 0.05554  0.00052  -0.02509 169 SER A C   
1184 O O   . SER A 162 ? 0.20453 0.18104 0.17336 0.06236  0.00402  -0.01810 169 SER A O   
1185 C CB  . SER A 162 ? 0.23538 0.19842 0.20619 0.05328  0.00536  -0.03018 169 SER A CB  
1186 O OG  . SER A 162 ? 0.23448 0.19431 0.21224 0.05589  0.01284  -0.02313 169 SER A OG  
1187 N N   . PHE A 163 ? 0.21467 0.18775 0.18435 0.04604  -0.00232 -0.02900 170 PHE A N   
1188 C CA  . PHE A 163 ? 0.19493 0.16963 0.16844 0.04146  -0.00217 -0.02683 170 PHE A CA  
1189 C C   . PHE A 163 ? 0.21956 0.19226 0.19615 0.03187  -0.00290 -0.03314 170 PHE A C   
1190 O O   . PHE A 163 ? 0.21996 0.19171 0.19295 0.02965  -0.00397 -0.03824 170 PHE A O   
1191 C CB  . PHE A 163 ? 0.19512 0.17731 0.16564 0.04268  -0.00777 -0.02593 170 PHE A CB  
1192 C CG  . PHE A 163 ? 0.18347 0.16891 0.15229 0.03883  -0.01316 -0.03044 170 PHE A CG  
1193 C CD1 . PHE A 163 ? 0.18422 0.17171 0.15366 0.04399  -0.01589 -0.03282 170 PHE A CD1 
1194 C CD2 . PHE A 163 ? 0.20796 0.19617 0.17715 0.03168  -0.01513 -0.03155 170 PHE A CD2 
1195 C CE1 . PHE A 163 ? 0.19400 0.18457 0.16771 0.04102  -0.01883 -0.03452 170 PHE A CE1 
1196 C CE2 . PHE A 163 ? 0.19649 0.18922 0.16554 0.03003  -0.01793 -0.03217 170 PHE A CE2 
1197 C CZ  . PHE A 163 ? 0.18453 0.17772 0.15759 0.03458  -0.01905 -0.03269 170 PHE A CZ  
1198 N N   . THR A 164 ? 0.19872 0.17173 0.18340 0.02737  -0.00185 -0.03341 171 THR A N   
1199 C CA  . THR A 164 ? 0.20184 0.17666 0.19024 0.01988  -0.00417 -0.04212 171 THR A CA  
1200 C C   . THR A 164 ? 0.19873 0.18182 0.18538 0.01659  -0.00965 -0.04269 171 THR A C   
1201 O O   . THR A 164 ? 0.20072 0.18547 0.18899 0.01845  -0.00988 -0.03634 171 THR A O   
1202 C CB  . THR A 164 ? 0.20854 0.17808 0.21432 0.01684  0.00082  -0.04588 171 THR A CB  
1203 O OG1 . THR A 164 ? 0.21728 0.18596 0.23554 0.01778  0.00438  -0.03893 171 THR A OG1 
1204 C CG2 . THR A 164 ? 0.21259 0.17371 0.22280 0.02038  0.00749  -0.04424 171 THR A CG2 
1205 N N   . VAL A 165 ? 0.20155 0.19132 0.18462 0.01277  -0.01388 -0.05043 172 VAL A N   
1206 C CA  . VAL A 165 ? 0.20389 0.20345 0.18632 0.01024  -0.01914 -0.05149 172 VAL A CA  
1207 C C   . VAL A 165 ? 0.22799 0.23342 0.21639 0.00659  -0.02192 -0.06397 172 VAL A C   
1208 O O   . VAL A 165 ? 0.22104 0.22775 0.20490 0.00719  -0.02180 -0.07112 172 VAL A O   
1209 C CB  . VAL A 165 ? 0.19878 0.20618 0.16876 0.01263  -0.02243 -0.04657 172 VAL A CB  
1210 C CG1 . VAL A 165 ? 0.20528 0.22460 0.17448 0.01098  -0.02754 -0.04668 172 VAL A CG1 
1211 C CG2 . VAL A 165 ? 0.20999 0.21282 0.17887 0.01667  -0.02090 -0.03780 172 VAL A CG2 
1212 N N   . ARG A 166 ? 0.20987 0.22063 0.20889 0.00352  -0.02511 -0.06783 173 ARG A N   
1213 C CA  . ARG A 166 ? 0.21827 0.23829 0.22565 0.00093  -0.03000 -0.08300 173 ARG A CA  
1214 C C   . ARG A 166 ? 0.21959 0.25171 0.22806 -0.00008 -0.03640 -0.08403 173 ARG A C   
1215 O O   . ARG A 166 ? 0.21804 0.24702 0.22869 -0.00056 -0.03512 -0.07353 173 ARG A O   
1216 C CB  . ARG A 166 ? 0.23469 0.24649 0.26769 -0.00256 -0.02621 -0.09143 173 ARG A CB  
1217 C CG  . ARG A 166 ? 0.27831 0.28124 0.33007 -0.00413 -0.02068 -0.08202 173 ARG A CG  
1218 C CD  . ARG A 166 ? 0.34554 0.34344 0.43078 -0.00779 -0.01683 -0.09089 173 ARG A CD  
1219 N NE  . ARG A 166 ? 0.42529 0.41436 0.52697 -0.00703 -0.00848 -0.07661 173 ARG A NE  
1220 C CZ  . ARG A 166 ? 0.58199 0.57449 0.69830 -0.00902 -0.00930 -0.07426 173 ARG A CZ  
1221 N NH1 . ARG A 166 ? 0.40919 0.41374 0.52861 -0.01254 -0.01889 -0.08675 173 ARG A NH1 
1222 N NH2 . ARG A 166 ? 0.59842 0.58354 0.72626 -0.00621 -0.00002 -0.05858 173 ARG A NH2 
1223 N N   . THR A 167 ? 0.22873 0.27629 0.23552 0.00065  -0.04357 -0.09736 174 THR A N   
1224 C CA  . THR A 167 ? 0.22701 0.28717 0.23979 -0.00026 -0.05035 -0.10124 174 THR A CA  
1225 C C   . THR A 167 ? 0.31528 0.36769 0.35821 -0.00580 -0.04883 -0.10712 174 THR A C   
1226 O O   . THR A 167 ? 0.38605 0.43199 0.44755 -0.00812 -0.04618 -0.11729 174 THR A O   
1227 C CB  . THR A 167 ? 0.26514 0.34723 0.26823 0.00428  -0.05907 -0.11585 174 THR A CB  
1228 O OG1 . THR A 167 ? 0.33577 0.42413 0.31311 0.01051  -0.05752 -0.10585 174 THR A OG1 
1229 C CG2 . THR A 167 ? 0.36096 0.45777 0.36911 0.00450  -0.06664 -0.11940 174 THR A CG2 
1230 N N   . ASP A 168 ? 0.23062 0.28324 0.28156 -0.00769 -0.04935 -0.09966 175 ASP A N   
1231 C CA  . ASP A 168 ? 0.22051 0.26555 0.30281 -0.01224 -0.04591 -0.10163 175 ASP A CA  
1232 C C   . ASP A 168 ? 0.32732 0.38769 0.42753 -0.01436 -0.05530 -0.11810 175 ASP A C   
1233 O O   . ASP A 168 ? 0.32749 0.39997 0.41747 -0.01295 -0.06160 -0.11568 175 ASP A O   
1234 C CB  . ASP A 168 ? 0.21130 0.24701 0.29222 -0.01183 -0.03948 -0.08235 175 ASP A CB  
1235 C CG  . ASP A 168 ? 0.40518 0.43315 0.51874 -0.01492 -0.03335 -0.08032 175 ASP A CG  
1236 O OD1 . ASP A 168 ? 0.48645 0.50881 0.62397 -0.01706 -0.02952 -0.08853 175 ASP A OD1 
1237 O OD2 . ASP A 168 ? 0.28344 0.31061 0.40064 -0.01466 -0.03117 -0.06949 175 ASP A OD2 
1238 N N   . THR A 169 ? 0.35726 0.41744 0.48733 -0.01743 -0.05613 -0.13493 176 THR A N   
1239 C CA  . THR A 169 ? 0.44653 0.52269 0.59977 -0.01909 -0.06627 -0.15503 176 THR A CA  
1240 C C   . THR A 169 ? 0.44395 0.51150 0.63745 -0.02448 -0.06120 -0.15250 176 THR A C   
1241 O O   . THR A 169 ? 0.41226 0.48996 0.63743 -0.02701 -0.06812 -0.17132 176 THR A O   
1242 C CB  . THR A 169 ? 0.46788 0.55363 0.63326 -0.01813 -0.07258 -0.18067 176 THR A CB  
1243 O OG1 . THR A 169 ? 0.47513 0.54273 0.65999 -0.02105 -0.06231 -0.17949 176 THR A OG1 
1244 C CG2 . THR A 169 ? 0.44027 0.54024 0.56456 -0.01086 -0.07861 -0.18308 176 THR A CG2 
1245 N N   . GLY A 170 ? 0.39142 0.44179 0.58588 -0.02519 -0.04903 -0.13011 177 GLY A N   
1246 C CA  . GLY A 170 ? 0.53684 0.57859 0.76841 -0.02852 -0.04117 -0.12297 177 GLY A CA  
1247 C C   . GLY A 170 ? 0.29671 0.34629 0.52526 -0.02887 -0.04544 -0.11634 177 GLY A C   
1248 O O   . GLY A 170 ? 0.33714 0.40312 0.54777 -0.02774 -0.05751 -0.12519 177 GLY A O   
1249 N N   . GLU A 171 ? 0.26369 0.30267 0.51116 -0.02942 -0.03477 -0.09986 178 GLU A N   
1250 C CA  . GLU A 171 ? 0.22858 0.27347 0.48120 -0.03021 -0.03707 -0.09345 178 GLU A CA  
1251 C C   . GLU A 171 ? 0.27112 0.32571 0.48100 -0.02716 -0.04538 -0.08823 178 GLU A C   
1252 O O   . GLU A 171 ? 0.20405 0.25153 0.38512 -0.02331 -0.04018 -0.07303 178 GLU A O   
1253 C CB  . GLU A 171 ? 0.25070 0.28182 0.51764 -0.02817 -0.02167 -0.07101 178 GLU A CB  
1254 C CG  . GLU A 171 ? 0.35989 0.39498 0.63544 -0.02844 -0.02122 -0.06192 178 GLU A CG  
1255 C CD  . GLU A 171 ? 0.45843 0.48114 0.74767 -0.02396 -0.00400 -0.03886 178 GLU A CD  
1256 O OE1 . GLU A 171 ? 0.32500 0.33775 0.60897 -0.01967 0.00595  -0.02967 178 GLU A OE1 
1257 O OE2 . GLU A 171 ? 0.40781 0.43195 0.71424 -0.02377 -0.00004 -0.03007 178 GLU A OE2 
1258 N N   . PRO A 172 ? 0.26379 0.33526 0.47057 -0.02790 -0.05776 -0.09973 179 PRO A N   
1259 C CA  . PRO A 172 ? 0.24752 0.32816 0.41623 -0.02407 -0.06369 -0.09184 179 PRO A CA  
1260 C C   . PRO A 172 ? 0.26912 0.34191 0.43051 -0.02289 -0.05651 -0.07094 179 PRO A C   
1261 O O   . PRO A 172 ? 0.28929 0.35816 0.47583 -0.02502 -0.05182 -0.06600 179 PRO A O   
1262 C CB  . PRO A 172 ? 0.24397 0.34658 0.41794 -0.02396 -0.07778 -0.10866 179 PRO A CB  
1263 C CG  . PRO A 172 ? 0.35140 0.45734 0.55817 -0.02689 -0.08149 -0.13133 179 PRO A CG  
1264 C CD  . PRO A 172 ? 0.29062 0.37603 0.52890 -0.03106 -0.06779 -0.12239 179 PRO A CD  
1265 N N   . MET A 173 ? 0.23292 0.30438 0.36191 -0.01891 -0.05553 -0.05919 180 MET A N   
1266 C CA  . MET A 173 ? 0.20392 0.26874 0.32481 -0.01652 -0.04919 -0.04155 180 MET A CA  
1267 C C   . MET A 173 ? 0.35534 0.43151 0.46605 -0.01554 -0.05547 -0.03672 180 MET A C   
1268 O O   . MET A 173 ? 0.34196 0.41354 0.44996 -0.01361 -0.05063 -0.02405 180 MET A O   
1269 C CB  . MET A 173 ? 0.19944 0.25504 0.29693 -0.01224 -0.04367 -0.03277 180 MET A CB  
1270 C CG  . MET A 173 ? 0.54728 0.58911 0.65553 -0.01053 -0.03270 -0.02645 180 MET A CG  
1271 S SD  . MET A 173 ? 0.47551 0.51207 0.55367 -0.00476 -0.03045 -0.01941 180 MET A SD  
1272 C CE  . MET A 173 ? 0.33025 0.37029 0.39939 -0.00087 -0.03045 -0.00784 180 MET A CE  
1273 N N   . GLY A 174 ? 0.22865 0.32030 0.33204 -0.01531 -0.06545 -0.04543 181 GLY A N   
1274 C CA  . GLY A 174 ? 0.19157 0.29525 0.28653 -0.01340 -0.07071 -0.03918 181 GLY A CA  
1275 C C   . GLY A 174 ? 0.20128 0.30399 0.27128 -0.00897 -0.06861 -0.02796 181 GLY A C   
1276 O O   . GLY A 174 ? 0.20385 0.31860 0.25848 -0.00538 -0.07345 -0.02900 181 GLY A O   
1277 N N   . ARG A 175 ? 0.17038 0.25939 0.23834 -0.00811 -0.06067 -0.01748 182 ARG A N   
1278 C CA  . ARG A 175 ? 0.16568 0.25176 0.21719 -0.00415 -0.05805 -0.00867 182 ARG A CA  
1279 C C   . ARG A 175 ? 0.17682 0.24888 0.23009 -0.00240 -0.05018 -0.00245 182 ARG A C   
1280 O O   . ARG A 175 ? 0.16265 0.23170 0.22775 -0.00285 -0.04701 0.00102  182 ARG A O   
1281 C CB  . ARG A 175 ? 0.16220 0.25909 0.21150 -0.00212 -0.06135 -0.00073 182 ARG A CB  
1282 C CG  . ARG A 175 ? 0.15779 0.25211 0.19664 0.00207  -0.05821 0.00749  182 ARG A CG  
1283 C CD  . ARG A 175 ? 0.16312 0.26357 0.20823 0.00401  -0.05846 0.01744  182 ARG A CD  
1284 N NE  . ARG A 175 ? 0.14769 0.24191 0.20341 0.00271  -0.05617 0.01908  182 ARG A NE  
1285 C CZ  . ARG A 175 ? 0.14776 0.24820 0.21325 0.00055  -0.05873 0.02002  182 ARG A CZ  
1286 N NH1 . ARG A 175 ? 0.15222 0.26625 0.21859 -0.00039 -0.06478 0.01825  182 ARG A NH1 
1287 N NH2 . ARG A 175 ? 0.16128 0.25592 0.23595 0.00047  -0.05524 0.02265  182 ARG A NH2 
1288 N N   . GLY A 176 ? 0.21755 0.24827 0.14722 0.04230  -0.03406 0.02361  183 GLY A N   
1289 C CA  . GLY A 176 ? 0.19160 0.21842 0.14722 0.03308  -0.02831 0.02252  183 GLY A CA  
1290 C C   . GLY A 176 ? 0.19064 0.20877 0.14815 0.02589  -0.02307 0.01565  183 GLY A C   
1291 O O   . GLY A 176 ? 0.22634 0.23795 0.16586 0.03017  -0.01883 0.01455  183 GLY A O   
1292 N N   . THR A 177 ? 0.16284 0.18147 0.14073 0.01682  -0.02297 0.01136  184 THR A N   
1293 C CA  . THR A 177 ? 0.15661 0.16839 0.13804 0.01227  -0.01792 0.00679  184 THR A CA  
1294 C C   . THR A 177 ? 0.21413 0.22724 0.20611 0.00335  -0.02468 -0.00135 184 THR A C   
1295 O O   . THR A 177 ? 0.17063 0.19180 0.17635 -0.00104 -0.02876 -0.00118 184 THR A O   
1296 C CB  . THR A 177 ? 0.17079 0.18086 0.16681 0.01128  -0.00682 0.01397  184 THR A CB  
1297 O OG1 . THR A 177 ? 0.21311 0.22003 0.19827 0.01832  0.00158  0.02289  184 THR A OG1 
1298 C CG2 . THR A 177 ? 0.19801 0.20769 0.20295 0.00750  -0.00293 0.00999  184 THR A CG2 
1299 N N   . LYS A 178 ? 0.16871 0.17261 0.15295 0.00192  -0.02458 -0.00765 185 LYS A N   
1300 C CA  . LYS A 178 ? 0.17913 0.17956 0.17089 -0.00656 -0.02942 -0.01361 185 LYS A CA  
1301 C C   . LYS A 178 ? 0.19827 0.19158 0.19388 -0.00420 -0.02204 -0.01269 185 LYS A C   
1302 O O   . LYS A 178 ? 0.20290 0.18806 0.18575 0.00305  -0.01717 -0.01381 185 LYS A O   
1303 C CB  . LYS A 178 ? 0.20149 0.19347 0.17709 -0.01049 -0.03809 -0.02266 185 LYS A CB  
1304 C CG  . LYS A 178 ? 0.28254 0.26067 0.25799 -0.01765 -0.03980 -0.02833 185 LYS A CG  
1305 C CD  . LYS A 178 ? 0.36941 0.33999 0.33253 -0.02677 -0.05056 -0.03832 185 LYS A CD  
1306 C CE  . LYS A 178 ? 0.40628 0.37185 0.34496 -0.01997 -0.05416 -0.04418 185 LYS A CE  
1307 N NZ  . LYS A 178 ? 0.48391 0.44432 0.41150 -0.03155 -0.06738 -0.05606 185 LYS A NZ  
1308 N N   . VAL A 179 ? 0.15017 0.14878 0.16226 -0.00846 -0.02102 -0.01038 186 VAL A N   
1309 C CA  . VAL A 179 ? 0.13421 0.13123 0.15190 -0.00556 -0.01612 -0.00886 186 VAL A CA  
1310 C C   . VAL A 179 ? 0.20880 0.19457 0.22288 -0.00953 -0.02004 -0.01227 186 VAL A C   
1311 O O   . VAL A 179 ? 0.19289 0.18268 0.21465 -0.01706 -0.02377 -0.01198 186 VAL A O   
1312 C CB  . VAL A 179 ? 0.10702 0.11758 0.14284 -0.00775 -0.01353 -0.00443 186 VAL A CB  
1313 C CG1 . VAL A 179 ? 0.14621 0.16066 0.18893 -0.00464 -0.01116 -0.00313 186 VAL A CG1 
1314 C CG2 . VAL A 179 ? 0.14603 0.16254 0.18525 -0.00580 -0.00835 -0.00002 186 VAL A CG2 
1315 N N   . ILE A 180 ? 0.16766 0.13779 0.16897 -0.00384 -0.01799 -0.01486 187 ILE A N   
1316 C CA  . ILE A 180 ? 0.16404 0.11581 0.15829 -0.00699 -0.02028 -0.01714 187 ILE A CA  
1317 C C   . ILE A 180 ? 0.16895 0.12283 0.16934 0.00110  -0.01582 -0.01163 187 ILE A C   
1318 O O   . ILE A 180 ? 0.19460 0.14818 0.19168 0.01283  -0.01056 -0.01054 187 ILE A O   
1319 C CB  . ILE A 180 ? 0.19846 0.12517 0.17059 -0.00506 -0.02136 -0.02482 187 ILE A CB  
1320 C CG1 . ILE A 180 ? 0.19486 0.12631 0.16093 -0.01175 -0.02762 -0.03040 187 ILE A CG1 
1321 C CG2 . ILE A 180 ? 0.26258 0.16457 0.22785 -0.01067 -0.02293 -0.02618 187 ILE A CG2 
1322 C CD1 . ILE A 180 ? 0.28238 0.19062 0.22311 -0.00944 -0.02986 -0.04028 187 ILE A CD1 
1323 N N   . LEU A 181 ? 0.14866 0.10787 0.15798 -0.00390 -0.01780 -0.00762 188 LEU A N   
1324 C CA  . LEU A 181 ? 0.16793 0.13240 0.18201 0.00392  -0.01586 -0.00191 188 LEU A CA  
1325 C C   . LEU A 181 ? 0.21889 0.15669 0.21840 0.00725  -0.01487 -0.00021 188 LEU A C   
1326 O O   . LEU A 181 ? 0.21999 0.14640 0.21595 -0.00263 -0.01677 0.00076  188 LEU A O   
1327 C CB  . LEU A 181 ? 0.15186 0.13545 0.17886 -0.00229 -0.01870 0.00115  188 LEU A CB  
1328 C CG  . LEU A 181 ? 0.14498 0.14799 0.18461 -0.00666 -0.01931 -0.00103 188 LEU A CG  
1329 C CD1 . LEU A 181 ? 0.18444 0.19964 0.23125 -0.01146 -0.02201 0.00015  188 LEU A CD1 
1330 C CD2 . LEU A 181 ? 0.19313 0.20900 0.24080 0.00020  -0.01624 0.00004  188 LEU A CD2 
1331 N N   . HIS A 182 ? 0.21246 0.13903 0.20339 0.02163  -0.01075 0.00094  189 HIS A N   
1332 C CA  . HIS A 182 ? 0.24548 0.14183 0.22063 0.02823  -0.00859 0.00411  189 HIS A CA  
1333 C C   . HIS A 182 ? 0.23933 0.15132 0.22246 0.03514  -0.00932 0.01385  189 HIS A C   
1334 O O   . HIS A 182 ? 0.23091 0.16217 0.22183 0.04898  -0.00815 0.01752  189 HIS A O   
1335 C CB  . HIS A 182 ? 0.25199 0.12918 0.21269 0.04408  -0.00309 0.00074  189 HIS A CB  
1336 C CG  . HIS A 182 ? 0.31715 0.18172 0.26645 0.03855  -0.00321 -0.01003 189 HIS A CG  
1337 N ND1 . HIS A 182 ? 0.42908 0.25682 0.35838 0.03067  -0.00503 -0.01769 189 HIS A ND1 
1338 C CD2 . HIS A 182 ? 0.34083 0.22544 0.29524 0.03801  -0.00270 -0.01418 189 HIS A CD2 
1339 C CE1 . HIS A 182 ? 0.34563 0.17293 0.26666 0.02749  -0.00666 -0.02716 189 HIS A CE1 
1340 N NE2 . HIS A 182 ? 0.40037 0.26156 0.33553 0.03291  -0.00458 -0.02413 189 HIS A NE2 
1341 N N   . LEU A 183 ? 0.22156 0.12834 0.20298 0.02554  -0.01134 0.01834  190 LEU A N   
1342 C CA  . LEU A 183 ? 0.21085 0.13878 0.19869 0.03084  -0.01356 0.02650  190 LEU A CA  
1343 C C   . LEU A 183 ? 0.25830 0.17461 0.23558 0.04919  -0.01142 0.03541  190 LEU A C   
1344 O O   . LEU A 183 ? 0.29485 0.17496 0.25506 0.05471  -0.00692 0.03778  190 LEU A O   
1345 C CB  . LEU A 183 ? 0.22189 0.14760 0.20776 0.01727  -0.01439 0.02975  190 LEU A CB  
1346 C CG  . LEU A 183 ? 0.21132 0.15505 0.20996 0.00232  -0.01673 0.02226  190 LEU A CG  
1347 C CD1 . LEU A 183 ? 0.23533 0.17960 0.23251 -0.00881 -0.01553 0.02669  190 LEU A CD1 
1348 C CD2 . LEU A 183 ? 0.24313 0.21868 0.25643 0.00507  -0.02022 0.01874  190 LEU A CD2 
1349 N N   . LYS A 184 ? 0.25018 0.19707 0.23696 0.05886  -0.01533 0.04050  191 LYS A N   
1350 C CA  . LYS A 184 ? 0.25743 0.19911 0.23428 0.07777  -0.01497 0.05147  191 LYS A CA  
1351 C C   . LYS A 184 ? 0.28360 0.19646 0.24111 0.07436  -0.01267 0.06073  191 LYS A C   
1352 O O   . LYS A 184 ? 0.31342 0.22740 0.27138 0.05755  -0.01317 0.05928  191 LYS A O   
1353 C CB  . LYS A 184 ? 0.28158 0.26849 0.27401 0.08546  -0.02244 0.05403  191 LYS A CB  
1354 C CG  . LYS A 184 ? 0.25662 0.27597 0.27154 0.08999  -0.02343 0.04789  191 LYS A CG  
1355 C CD  . LYS A 184 ? 0.30860 0.37357 0.34190 0.08607  -0.03313 0.04669  191 LYS A CD  
1356 C CE  . LYS A 184 ? 0.49607 0.59832 0.55631 0.08470  -0.03462 0.04129  191 LYS A CE  
1357 N NZ  . LYS A 184 ? 0.37617 0.52169 0.45629 0.07577  -0.04540 0.03727  191 LYS A NZ  
1358 N N   . GLU A 185 ? 0.35780 0.24494 0.29816 0.09153  -0.00895 0.07154  192 GLU A N   
1359 C CA  . GLU A 185 ? 0.42893 0.27974 0.34873 0.08688  -0.00399 0.08176  192 GLU A CA  
1360 C C   . GLU A 185 ? 0.42914 0.30368 0.34853 0.08138  -0.00753 0.08876  192 GLU A C   
1361 O O   . GLU A 185 ? 0.45483 0.30941 0.36371 0.06878  -0.00259 0.09446  192 GLU A O   
1362 C CB  . GLU A 185 ? 0.50422 0.31885 0.40307 0.10884  0.00146  0.09383  192 GLU A CB  
1363 C CG  . GLU A 185 ? 0.71644 0.56504 0.62335 0.13114  -0.00315 0.09744  192 GLU A CG  
1364 C CD  . GLU A 185 ? 0.98815 0.80963 0.87984 0.14546  0.00231  0.10478  192 GLU A CD  
1365 O OE1 . GLU A 185 ? 1.02613 0.87271 0.92362 0.16417  -0.00031 0.10782  192 GLU A OE1 
1366 O OE2 . GLU A 185 ? 1.01850 0.79444 0.89354 0.13709  0.00921  0.10738  192 GLU A OE2 
1367 N N   . ASP A 186 ? 0.34419 0.26220 0.27504 0.08929  -0.01583 0.08758  193 ASP A N   
1368 C CA  . ASP A 186 ? 0.31202 0.25148 0.23769 0.08627  -0.01988 0.09261  193 ASP A CA  
1369 C C   . ASP A 186 ? 0.29450 0.25939 0.23526 0.06705  -0.02321 0.07984  193 ASP A C   
1370 O O   . ASP A 186 ? 0.29961 0.28550 0.23605 0.06523  -0.02717 0.08068  193 ASP A O   
1371 C CB  . ASP A 186 ? 0.37808 0.34782 0.30221 0.10718  -0.02855 0.09941  193 ASP A CB  
1372 C CG  . ASP A 186 ? 0.38357 0.39414 0.33309 0.10900  -0.03723 0.08791  193 ASP A CG  
1373 O OD1 . ASP A 186 ? 0.44885 0.45835 0.41454 0.09981  -0.03460 0.07718  193 ASP A OD1 
1374 O OD2 . ASP A 186 ? 0.53622 0.58142 0.48937 0.11998  -0.04691 0.09032  193 ASP A OD2 
1375 N N   . GLN A 187 ? 0.25275 0.21302 0.20760 0.05379  -0.02111 0.06848  194 GLN A N   
1376 C CA  . GLN A 187 ? 0.23285 0.21377 0.20197 0.03802  -0.02348 0.05698  194 GLN A CA  
1377 C C   . GLN A 187 ? 0.22214 0.18218 0.19022 0.02157  -0.01669 0.05523  194 GLN A C   
1378 O O   . GLN A 187 ? 0.22359 0.19450 0.20484 0.01026  -0.01755 0.04545  194 GLN A O   
1379 C CB  . GLN A 187 ? 0.20319 0.20415 0.19213 0.03770  -0.02786 0.04597  194 GLN A CB  
1380 C CG  . GLN A 187 ? 0.20672 0.23653 0.20228 0.05143  -0.03537 0.04751  194 GLN A CG  
1381 C CD  . GLN A 187 ? 0.23454 0.28814 0.22570 0.05099  -0.04261 0.04755  194 GLN A CD  
1382 O OE1 . GLN A 187 ? 0.26186 0.32011 0.25367 0.03851  -0.04283 0.04065  194 GLN A OE1 
1383 N NE2 . GLN A 187 ? 0.26471 0.33593 0.25135 0.06600  -0.04931 0.05427  194 GLN A NE2 
1384 N N   . THR A 188 ? 0.30608 0.23760 0.25950 0.01988  -0.01005 0.06532  195 THR A N   
1385 C CA  . THR A 188 ? 0.30507 0.22149 0.26220 0.00171  -0.00462 0.06287  195 THR A CA  
1386 C C   . THR A 188 ? 0.29905 0.23619 0.26103 -0.00907 -0.00228 0.06303  195 THR A C   
1387 O O   . THR A 188 ? 0.27993 0.21264 0.24932 -0.02430 0.00196  0.06146  195 THR A O   
1388 C CB  . THR A 188 ? 0.33861 0.21434 0.28062 -0.00077 0.00255  0.07280  195 THR A CB  
1389 O OG1 . THR A 188 ? 0.40516 0.27451 0.33076 0.00627  0.00714  0.08798  195 THR A OG1 
1390 C CG2 . THR A 188 ? 0.38457 0.23479 0.32014 0.01098  0.00144  0.07015  195 THR A CG2 
1391 N N   . GLU A 189 ? 0.26928 0.22993 0.22691 -0.00126 -0.00497 0.06441  196 GLU A N   
1392 C CA  . GLU A 189 ? 0.26419 0.24515 0.22549 -0.00890 -0.00228 0.06173  196 GLU A CA  
1393 C C   . GLU A 189 ? 0.26370 0.25766 0.24456 -0.01839 -0.00448 0.04890  196 GLU A C   
1394 O O   . GLU A 189 ? 0.23279 0.23758 0.21965 -0.02655 0.00023  0.04780  196 GLU A O   
1395 C CB  . GLU A 189 ? 0.24085 0.24357 0.19151 0.00202  -0.00688 0.06114  196 GLU A CB  
1396 C CG  . GLU A 189 ? 0.24721 0.26833 0.20857 0.00674  -0.01722 0.04862  196 GLU A CG  
1397 C CD  . GLU A 189 ? 0.28906 0.32919 0.23779 0.01674  -0.02403 0.04780  196 GLU A CD  
1398 O OE1 . GLU A 189 ? 0.33329 0.37162 0.27090 0.02855  -0.02766 0.05649  196 GLU A OE1 
1399 O OE2 . GLU A 189 ? 0.29187 0.34715 0.23942 0.01368  -0.02549 0.03891  196 GLU A OE2 
1400 N N   . TYR A 190 ? 0.21366 0.20761 0.20424 -0.01623 -0.01055 0.04046  197 TYR A N   
1401 C CA  . TYR A 190 ? 0.17593 0.18123 0.18241 -0.02314 -0.01262 0.02985  197 TYR A CA  
1402 C C   . TYR A 190 ? 0.20834 0.20173 0.22167 -0.03437 -0.00993 0.02926  197 TYR A C   
1403 O O   . TYR A 190 ? 0.22093 0.22300 0.24596 -0.03851 -0.01246 0.02150  197 TYR A O   
1404 C CB  . TYR A 190 ? 0.18968 0.20173 0.20294 -0.01649 -0.01906 0.02251  197 TYR A CB  
1405 C CG  . TYR A 190 ? 0.17870 0.20721 0.18822 -0.00879 -0.02362 0.02134  197 TYR A CG  
1406 C CD1 . TYR A 190 ? 0.19296 0.23579 0.20265 -0.01120 -0.02423 0.01575  197 TYR A CD1 
1407 C CD2 . TYR A 190 ? 0.18446 0.21429 0.18871 0.00155  -0.02754 0.02568  197 TYR A CD2 
1408 C CE1 . TYR A 190 ? 0.17595 0.23226 0.17960 -0.00585 -0.02980 0.01256  197 TYR A CE1 
1409 C CE2 . TYR A 190 ? 0.21438 0.26353 0.21566 0.00751  -0.03399 0.02386  197 TYR A CE2 
1410 C CZ  . TYR A 190 ? 0.19117 0.25243 0.19093 0.00241  -0.03546 0.01641  197 TYR A CZ  
1411 O OH  . TYR A 190 ? 0.21479 0.29355 0.20923 0.00654  -0.04322 0.01205  197 TYR A OH  
1412 N N   . LEU A 191 ? 0.22191 0.19512 0.22749 -0.03976 -0.00534 0.03731  198 LEU A N   
1413 C CA  . LEU A 191 ? 0.20618 0.17115 0.21937 -0.05462 -0.00338 0.03630  198 LEU A CA  
1414 C C   . LEU A 191 ? 0.24622 0.22590 0.26601 -0.06461 0.00335  0.04250  198 LEU A C   
1415 O O   . LEU A 191 ? 0.25342 0.23236 0.28342 -0.07926 0.00492  0.04256  198 LEU A O   
1416 C CB  . LEU A 191 ? 0.23090 0.16060 0.23235 -0.05761 -0.00185 0.04025  198 LEU A CB  
1417 C CG  . LEU A 191 ? 0.24496 0.16184 0.23987 -0.04566 -0.00672 0.03419  198 LEU A CG  
1418 C CD1 . LEU A 191 ? 0.32010 0.19663 0.29937 -0.04524 -0.00413 0.03743  198 LEU A CD1 
1419 C CD2 . LEU A 191 ? 0.27973 0.21073 0.28631 -0.04872 -0.01243 0.02214  198 LEU A CD2 
1420 N N   . GLU A 192 ? 0.19043 0.18194 0.20276 -0.05741 0.00792  0.04873  199 GLU A N   
1421 C CA  . GLU A 192 ? 0.21493 0.22053 0.23064 -0.06471 0.01715  0.05666  199 GLU A CA  
1422 C C   . GLU A 192 ? 0.23012 0.26695 0.26151 -0.06468 0.01715  0.04912  199 GLU A C   
1423 O O   . GLU A 192 ? 0.21554 0.26204 0.24491 -0.05380 0.01239  0.04095  199 GLU A O   
1424 C CB  . GLU A 192 ? 0.26728 0.27010 0.26280 -0.05494 0.02293  0.06723  199 GLU A CB  
1425 C CG  . GLU A 192 ? 0.32797 0.29779 0.30708 -0.05303 0.02425  0.07748  199 GLU A CG  
1426 C CD  . GLU A 192 ? 0.65615 0.62318 0.61163 -0.03879 0.02719  0.08838  199 GLU A CD  
1427 O OE1 . GLU A 192 ? 0.67634 0.61807 0.61690 -0.03102 0.02610  0.09601  199 GLU A OE1 
1428 O OE2 . GLU A 192 ? 0.72750 0.71722 0.67745 -0.03370 0.03030  0.08906  199 GLU A OE2 
1429 N N   . GLU A 193 ? 0.22265 0.27437 0.27102 -0.07720 0.02199  0.05154  200 GLU A N   
1430 C CA  . GLU A 193 ? 0.18139 0.26413 0.24655 -0.07525 0.02256  0.04560  200 GLU A CA  
1431 C C   . GLU A 193 ? 0.17886 0.27453 0.23293 -0.06058 0.02719  0.04435  200 GLU A C   
1432 O O   . GLU A 193 ? 0.17372 0.27797 0.23015 -0.05128 0.02293  0.03471  200 GLU A O   
1433 C CB  . GLU A 193 ? 0.20272 0.30687 0.28876 -0.09005 0.02945  0.05195  200 GLU A CB  
1434 C CG  . GLU A 193 ? 0.24386 0.38009 0.35030 -0.08638 0.02716  0.04504  200 GLU A CG  
1435 C CD  . GLU A 193 ? 0.41143 0.56991 0.53692 -0.09282 0.03336  0.04804  200 GLU A CD  
1436 O OE1 . GLU A 193 ? 0.34026 0.49177 0.46562 -0.10340 0.04080  0.05608  200 GLU A OE1 
1437 O OE2 . GLU A 193 ? 0.38033 0.56142 0.52066 -0.08634 0.03048  0.04224  200 GLU A OE2 
1438 N N   . ARG A 194 ? 0.22853 0.32415 0.26871 -0.05855 0.03645  0.05398  201 ARG A N   
1439 C CA  . ARG A 194 ? 0.20867 0.31766 0.23569 -0.04467 0.04096  0.05095  201 ARG A CA  
1440 C C   . ARG A 194 ? 0.21979 0.31644 0.23229 -0.03350 0.03045  0.04035  201 ARG A C   
1441 O O   . ARG A 194 ? 0.20304 0.30834 0.21080 -0.02401 0.02964  0.03094  201 ARG A O   
1442 C CB  . ARG A 194 ? 0.26818 0.37969 0.27849 -0.04330 0.05330  0.06410  201 ARG A CB  
1443 C CG  . ARG A 194 ? 0.34602 0.43352 0.33325 -0.03984 0.05022  0.07083  201 ARG A CG  
1444 C CD  . ARG A 194 ? 0.40439 0.49425 0.37746 -0.04121 0.06512  0.08793  201 ARG A CD  
1445 N NE  . ARG A 194 ? 0.52228 0.58883 0.46980 -0.03509 0.06313  0.09729  201 ARG A NE  
1446 C CZ  . ARG A 194 ? 0.41602 0.48190 0.34068 -0.02972 0.07381  0.11146  201 ARG A CZ  
1447 N NH1 . ARG A 194 ? 0.47648 0.56423 0.40113 -0.03038 0.08821  0.11725  201 ARG A NH1 
1448 N NH2 . ARG A 194 ? 0.59935 0.64327 0.50036 -0.02212 0.07072  0.12102  201 ARG A NH2 
1449 N N   . ARG A 195 ? 0.20134 0.27770 0.20687 -0.03447 0.02280  0.04164  202 ARG A N   
1450 C CA  . ARG A 195 ? 0.19320 0.26322 0.18936 -0.02555 0.01274  0.03263  202 ARG A CA  
1451 C C   . ARG A 195 ? 0.19232 0.26512 0.20431 -0.02633 0.00629  0.02085  202 ARG A C   
1452 O O   . ARG A 195 ? 0.15893 0.23452 0.16701 -0.02004 0.00180  0.01108  202 ARG A O   
1453 C CB  . ARG A 195 ? 0.20946 0.26103 0.19717 -0.02446 0.00746  0.03858  202 ARG A CB  
1454 C CG  . ARG A 195 ? 0.22056 0.27244 0.20232 -0.01569 -0.00306 0.03068  202 ARG A CG  
1455 C CD  . ARG A 195 ? 0.23016 0.29283 0.19298 -0.00687 -0.00437 0.02858  202 ARG A CD  
1456 N NE  . ARG A 195 ? 0.21688 0.28217 0.17609 -0.00066 -0.01592 0.02289  202 ARG A NE  
1457 C CZ  . ARG A 195 ? 0.23726 0.31263 0.19726 0.00079  -0.02357 0.00980  202 ARG A CZ  
1458 N NH1 . ARG A 195 ? 0.23737 0.31689 0.19627 -0.00070 -0.02065 0.00027  202 ARG A NH1 
1459 N NH2 . ARG A 195 ? 0.20786 0.28909 0.17055 0.00378  -0.03418 0.00620  202 ARG A NH2 
1460 N N   . ILE A 196 ? 0.15963 0.23001 0.18803 -0.03452 0.00544  0.02158  203 ILE A N   
1461 C CA  . ILE A 196 ? 0.12081 0.19342 0.16128 -0.03374 0.00003  0.01256  203 ILE A CA  
1462 C C   . ILE A 196 ? 0.13393 0.22169 0.17906 -0.02854 0.00421  0.00766  203 ILE A C   
1463 O O   . ILE A 196 ? 0.14479 0.22971 0.18961 -0.02288 0.00073  -0.00071 203 ILE A O   
1464 C CB  . ILE A 196 ? 0.12486 0.19310 0.17780 -0.04248 -0.00252 0.01411  203 ILE A CB  
1465 C CG1 . ILE A 196 ? 0.17416 0.22192 0.21874 -0.04463 -0.00586 0.01732  203 ILE A CG1 
1466 C CG2 . ILE A 196 ? 0.13453 0.20674 0.19738 -0.03996 -0.00726 0.00673  203 ILE A CG2 
1467 C CD1 . ILE A 196 ? 0.20405 0.24270 0.25524 -0.05532 -0.00699 0.01896  203 ILE A CD1 
1468 N N   . LYS A 197 ? 0.14546 0.24871 0.19553 -0.03017 0.01265  0.01330  204 LYS A N   
1469 C CA  . LYS A 197 ? 0.14300 0.26207 0.19718 -0.02195 0.01837  0.00925  204 LYS A CA  
1470 C C   . LYS A 197 ? 0.18642 0.29765 0.22132 -0.01149 0.01849  0.00106  204 LYS A C   
1471 O O   . LYS A 197 ? 0.17870 0.28798 0.21357 -0.00366 0.01821  -0.00757 204 LYS A O   
1472 C CB  . LYS A 197 ? 0.14975 0.29114 0.21218 -0.02456 0.02942  0.01809  204 LYS A CB  
1473 C CG  . LYS A 197 ? 0.24903 0.40538 0.33534 -0.03582 0.02887  0.02367  204 LYS A CG  
1474 C CD  . LYS A 197 ? 0.22028 0.40097 0.31502 -0.03998 0.04155  0.03371  204 LYS A CD  
1475 C CE  . LYS A 197 ? 0.34990 0.55866 0.47428 -0.04930 0.04195  0.03761  204 LYS A CE  
1476 N NZ  . LYS A 197 ? 0.48237 0.70642 0.61374 -0.05762 0.05392  0.04838  204 LYS A NZ  
1477 N N   . GLU A 198 ? 0.16177 0.26756 0.17849 -0.01090 0.01890  0.00369  205 GLU A N   
1478 C CA  . GLU A 198 ? 0.16323 0.26280 0.15924 -0.00243 0.01655  -0.00565 205 GLU A CA  
1479 C C   . GLU A 198 ? 0.15162 0.23751 0.14995 -0.00296 0.00599  -0.01671 205 GLU A C   
1480 O O   . GLU A 198 ? 0.18653 0.26649 0.17676 0.00265  0.00515  -0.02804 205 GLU A O   
1481 C CB  . GLU A 198 ? 0.17875 0.27637 0.15518 -0.00188 0.01594  0.00079  205 GLU A CB  
1482 C CG  . GLU A 198 ? 0.22439 0.31800 0.17747 0.00576  0.01020  -0.00998 205 GLU A CG  
1483 C CD  . GLU A 198 ? 0.24114 0.33477 0.17527 0.00777  0.00712  -0.00219 205 GLU A CD  
1484 O OE1 . GLU A 198 ? 0.23414 0.32230 0.17613 0.00298  0.00267  0.00647  205 GLU A OE1 
1485 O OE2 . GLU A 198 ? 0.24216 0.34016 0.15187 0.01564  0.00909  -0.00480 205 GLU A OE2 
1486 N N   . ILE A 199 ? 0.14124 0.22070 0.14953 -0.00973 -0.00112 -0.01364 206 ILE A N   
1487 C CA  . ILE A 199 ? 0.16781 0.23747 0.17980 -0.01127 -0.00953 -0.02228 206 ILE A CA  
1488 C C   . ILE A 199 ? 0.16559 0.23046 0.18880 -0.01001 -0.00751 -0.02725 206 ILE A C   
1489 O O   . ILE A 199 ? 0.19500 0.24943 0.21581 -0.00922 -0.01054 -0.03651 206 ILE A O   
1490 C CB  . ILE A 199 ? 0.18367 0.25008 0.20315 -0.01644 -0.01536 -0.01649 206 ILE A CB  
1491 C CG1 . ILE A 199 ? 0.17960 0.24875 0.18541 -0.01428 -0.01759 -0.01088 206 ILE A CG1 
1492 C CG2 . ILE A 199 ? 0.19998 0.26042 0.22866 -0.01911 -0.02138 -0.02286 206 ILE A CG2 
1493 C CD1 . ILE A 199 ? 0.20779 0.27126 0.22003 -0.01676 -0.01941 -0.00234 206 ILE A CD1 
1494 N N   . VAL A 200 ? 0.13507 0.20696 0.17087 -0.01035 -0.00307 -0.02076 207 VAL A N   
1495 C CA  . VAL A 200 ? 0.13672 0.20579 0.18169 -0.00631 -0.00154 -0.02350 207 VAL A CA  
1496 C C   . VAL A 200 ? 0.16653 0.23331 0.20252 0.00363  0.00433  -0.03055 207 VAL A C   
1497 O O   . VAL A 200 ? 0.19711 0.24912 0.23138 0.00811  0.00413  -0.03715 207 VAL A O   
1498 C CB  . VAL A 200 ? 0.16097 0.24421 0.22087 -0.00818 0.00042  -0.01525 207 VAL A CB  
1499 C CG1 . VAL A 200 ? 0.17712 0.26249 0.24497 0.00015  0.00251  -0.01648 207 VAL A CG1 
1500 C CG2 . VAL A 200 ? 0.15330 0.23245 0.21875 -0.01717 -0.00568 -0.01082 207 VAL A CG2 
1501 N N   . LYS A 201 ? 0.15070 0.22931 0.17832 0.00785  0.01070  -0.02921 208 LYS A N   
1502 C CA  . LYS A 201 ? 0.18832 0.26416 0.20387 0.01977  0.01776  -0.03691 208 LYS A CA  
1503 C C   . LYS A 201 ? 0.22532 0.27911 0.22231 0.01980  0.01236  -0.05021 208 LYS A C   
1504 O O   . LYS A 201 ? 0.25730 0.29494 0.24670 0.02734  0.01486  -0.05974 208 LYS A O   
1505 C CB  . LYS A 201 ? 0.18097 0.27674 0.18990 0.02429  0.02726  -0.03143 208 LYS A CB  
1506 C CG  . LYS A 201 ? 0.24578 0.34087 0.23973 0.03964  0.03697  -0.03941 208 LYS A CG  
1507 C CD  . LYS A 201 ? 0.30512 0.42345 0.29285 0.04402  0.04845  -0.03179 208 LYS A CD  
1508 C CE  . LYS A 201 ? 0.39572 0.51502 0.36729 0.06154  0.05980  -0.03962 208 LYS A CE  
1509 N NZ  . LYS A 201 ? 0.48493 0.63257 0.45516 0.06473  0.07314  -0.02858 208 LYS A NZ  
1510 N N   . LYS A 202 ? 0.20513 0.25769 0.19507 0.01131  0.00437  -0.05118 209 LYS A N   
1511 C CA  . LYS A 202 ? 0.22095 0.25880 0.19458 0.00905  -0.00303 -0.06461 209 LYS A CA  
1512 C C   . LYS A 202 ? 0.23159 0.25062 0.21515 0.00238  -0.00884 -0.07117 209 LYS A C   
1513 O O   . LYS A 202 ? 0.26908 0.26872 0.24160 0.00260  -0.01052 -0.08445 209 LYS A O   
1514 C CB  . LYS A 202 ? 0.23311 0.28160 0.20013 0.00326  -0.01066 -0.06113 209 LYS A CB  
1515 C CG  . LYS A 202 ? 0.27292 0.31350 0.22643 -0.00099 -0.02140 -0.07494 209 LYS A CG  
1516 C CD  . LYS A 202 ? 0.42922 0.48532 0.37018 -0.00048 -0.02707 -0.07004 209 LYS A CD  
1517 C CE  . LYS A 202 ? 0.54450 0.60062 0.47470 -0.00564 -0.04097 -0.08331 209 LYS A CE  
1518 N NZ  . LYS A 202 ? 0.55385 0.62878 0.48157 -0.00571 -0.04967 -0.07477 209 LYS A NZ  
1519 N N   . HIS A 203 ? 0.23891 0.26151 0.24201 -0.00387 -0.01105 -0.06191 210 HIS A N   
1520 C CA  . HIS A 203 ? 0.27849 0.28728 0.29103 -0.01213 -0.01620 -0.06538 210 HIS A CA  
1521 C C   . HIS A 203 ? 0.26506 0.26303 0.28911 -0.00925 -0.01108 -0.06020 210 HIS A C   
1522 O O   . HIS A 203 ? 0.28628 0.26838 0.31553 -0.01552 -0.01294 -0.06284 210 HIS A O   
1523 C CB  . HIS A 203 ? 0.29576 0.31725 0.31909 -0.02103 -0.02337 -0.05923 210 HIS A CB  
1524 C CG  . HIS A 203 ? 0.31172 0.34410 0.32488 -0.02350 -0.03072 -0.06354 210 HIS A CG  
1525 N ND1 . HIS A 203 ? 0.30681 0.33353 0.31215 -0.02882 -0.03778 -0.07652 210 HIS A ND1 
1526 C CD2 . HIS A 203 ? 0.31653 0.36464 0.32510 -0.02115 -0.03278 -0.05622 210 HIS A CD2 
1527 C CE1 . HIS A 203 ? 0.30586 0.34826 0.30187 -0.02846 -0.04491 -0.07722 210 HIS A CE1 
1528 N NE2 . HIS A 203 ? 0.32674 0.38099 0.32396 -0.02286 -0.04126 -0.06395 210 HIS A NE2 
1529 N N   . SER A 204 ? 0.29080 0.28306 0.16251 -0.08806 -0.03574 -0.04083 211 SER A N   
1530 C CA  . SER A 204 ? 0.28263 0.25970 0.18135 -0.06918 -0.02960 -0.04240 211 SER A CA  
1531 C C   . SER A 204 ? 0.28079 0.23802 0.17893 -0.06103 -0.01168 -0.06142 211 SER A C   
1532 O O   . SER A 204 ? 0.31720 0.27100 0.23897 -0.04271 -0.00561 -0.05892 211 SER A O   
1533 C CB  . SER A 204 ? 0.30619 0.29872 0.22978 -0.05314 -0.03456 -0.02477 211 SER A CB  
1534 O OG  . SER A 204 ? 0.30674 0.31756 0.23547 -0.05762 -0.04995 -0.00864 211 SER A OG  
1535 N N   . GLN A 205 ? 0.33510 0.28152 0.20837 -0.07432 -0.00311 -0.08100 212 GLN A N   
1536 C CA  . GLN A 205 ? 0.44285 0.37429 0.31695 -0.06509 0.01594  -0.10140 212 GLN A CA  
1537 C C   . GLN A 205 ? 0.46448 0.36773 0.36338 -0.04878 0.02228  -0.10670 212 GLN A C   
1538 O O   . GLN A 205 ? 0.46536 0.36313 0.38049 -0.03141 0.03578  -0.11439 212 GLN A O   
1539 C CB  . GLN A 205 ? 0.48945 0.41905 0.33458 -0.08226 0.02381  -0.12077 212 GLN A CB  
1540 C CG  . GLN A 205 ? 0.77332 0.70967 0.61911 -0.07320 0.04155  -0.13419 212 GLN A CG  
1541 C CD  . GLN A 205 ? 0.72348 0.69123 0.56522 -0.07409 0.04033  -0.12086 212 GLN A CD  
1542 O OE1 . GLN A 205 ? 0.83940 0.82835 0.66146 -0.08957 0.03714  -0.11523 212 GLN A OE1 
1543 N NE2 . GLN A 205 ? 0.82552 0.79707 0.69087 -0.05670 0.04237  -0.11240 212 GLN A NE2 
1544 N N   . PHE A 206 ? 0.36199 0.25006 0.26557 -0.05448 0.01226  -0.10048 213 PHE A N   
1545 C CA  . PHE A 206 ? 0.39417 0.25206 0.31873 -0.04303 0.01633  -0.10217 213 PHE A CA  
1546 C C   . PHE A 206 ? 0.36369 0.23386 0.31414 -0.03271 0.00478  -0.07751 213 PHE A C   
1547 O O   . PHE A 206 ? 0.40064 0.25149 0.36331 -0.03211 0.00115  -0.07143 213 PHE A O   
1548 C CB  . PHE A 206 ? 0.38915 0.21552 0.29566 -0.06213 0.01622  -0.11736 213 PHE A CB  
1549 C CG  . PHE A 206 ? 0.46971 0.29313 0.35753 -0.06699 0.02765  -0.13883 213 PHE A CG  
1550 C CD1 . PHE A 206 ? 0.51718 0.35379 0.37902 -0.08926 0.02185  -0.14335 213 PHE A CD1 
1551 C CD2 . PHE A 206 ? 0.46287 0.27695 0.36210 -0.04816 0.04369  -0.15154 213 PHE A CD2 
1552 C CE1 . PHE A 206 ? 0.58532 0.42287 0.42987 -0.09516 0.03278  -0.16210 213 PHE A CE1 
1553 C CE2 . PHE A 206 ? 0.56815 0.38337 0.45026 -0.05345 0.05446  -0.17130 213 PHE A CE2 
1554 C CZ  . PHE A 206 ? 0.56650 0.39225 0.42054 -0.07771 0.04942  -0.17726 213 PHE A CZ  
1555 N N   . ILE A 207 ? 0.26581 0.16743 0.22472 -0.02542 -0.00015 -0.06377 214 ILE A N   
1556 C CA  . ILE A 207 ? 0.23728 0.15437 0.22121 -0.01412 -0.00755 -0.04467 214 ILE A CA  
1557 C C   . ILE A 207 ? 0.27056 0.18533 0.27661 0.00580  0.00234  -0.04405 214 ILE A C   
1558 O O   . ILE A 207 ? 0.28787 0.21288 0.29414 0.01339  0.01144  -0.05089 214 ILE A O   
1559 C CB  . ILE A 207 ? 0.22477 0.17382 0.20934 -0.01530 -0.01629 -0.03285 214 ILE A CB  
1560 C CG1 . ILE A 207 ? 0.24687 0.20251 0.21469 -0.03290 -0.02757 -0.02999 214 ILE A CG1 
1561 C CG2 . ILE A 207 ? 0.21975 0.18835 0.22920 -0.00414 -0.02140 -0.01779 214 ILE A CG2 
1562 C CD1 . ILE A 207 ? 0.29362 0.24719 0.26794 -0.04109 -0.03690 -0.02243 214 ILE A CD1 
1563 N N   . GLY A 208 ? 0.24601 0.15182 0.27131 0.01316  -0.00017 -0.03363 215 GLY A N   
1564 C CA  . GLY A 208 ? 0.25185 0.15423 0.30028 0.03233  0.00819  -0.03091 215 GLY A CA  
1565 C C   . GLY A 208 ? 0.21516 0.15361 0.28317 0.04336  0.00521  -0.01605 215 GLY A C   
1566 O O   . GLY A 208 ? 0.23230 0.17498 0.32272 0.05568  0.00540  -0.00426 215 GLY A O   
1567 N N   . TYR A 209 ? 0.19883 0.16297 0.25895 0.03863  0.00278  -0.01653 216 TYR A N   
1568 C CA  . TYR A 209 ? 0.20590 0.20364 0.28086 0.04507  0.00075  -0.00678 216 TYR A CA  
1569 C C   . TYR A 209 ? 0.19031 0.19900 0.25467 0.04274  0.00657  -0.01621 216 TYR A C   
1570 O O   . TYR A 209 ? 0.23202 0.22961 0.27554 0.03235  0.00627  -0.02409 216 TYR A O   
1571 C CB  . TYR A 209 ? 0.16483 0.18017 0.24099 0.03712  -0.01090 0.00406  216 TYR A CB  
1572 C CG  . TYR A 209 ? 0.15126 0.15949 0.23637 0.03600  -0.01687 0.01574  216 TYR A CG  
1573 C CD1 . TYR A 209 ? 0.17187 0.19483 0.27724 0.04498  -0.01758 0.02928  216 TYR A CD1 
1574 C CD2 . TYR A 209 ? 0.16523 0.15483 0.23871 0.02402  -0.02264 0.01563  216 TYR A CD2 
1575 C CE1 . TYR A 209 ? 0.17493 0.19060 0.28781 0.04228  -0.02368 0.04352  216 TYR A CE1 
1576 C CE2 . TYR A 209 ? 0.16135 0.14286 0.24231 0.02020  -0.02795 0.02777  216 TYR A CE2 
1577 C CZ  . TYR A 209 ? 0.13899 0.13205 0.23928 0.02937  -0.02850 0.04245  216 TYR A CZ  
1578 O OH  . TYR A 209 ? 0.18601 0.17130 0.29409 0.02458  -0.03453 0.05865  216 TYR A OH  
1579 N N   . PRO A 210 ? 0.16658 0.20038 0.24364 0.04915  0.01036  -0.01355 217 PRO A N   
1580 C CA  . PRO A 210 ? 0.15012 0.19567 0.21730 0.04354  0.01475  -0.01962 217 PRO A CA  
1581 C C   . PRO A 210 ? 0.17831 0.22329 0.23336 0.03241  0.00582  -0.01638 217 PRO A C   
1582 O O   . PRO A 210 ? 0.20131 0.25469 0.26490 0.03219  -0.00196 -0.00928 217 PRO A O   
1583 C CB  . PRO A 210 ? 0.21467 0.29051 0.30143 0.05020  0.01785  -0.01468 217 PRO A CB  
1584 C CG  . PRO A 210 ? 0.24133 0.31499 0.34414 0.05766  0.01595  -0.00873 217 PRO A CG  
1585 C CD  . PRO A 210 ? 0.18205 0.23612 0.28234 0.06010  0.01043  -0.00348 217 PRO A CD  
1586 N N   . ILE A 211 ? 0.17230 0.21006 0.20873 0.02347  0.00718  -0.02089 218 ILE A N   
1587 C CA  . ILE A 211 ? 0.15165 0.18825 0.17938 0.01485  -0.00141 -0.01514 218 ILE A CA  
1588 C C   . ILE A 211 ? 0.14553 0.19052 0.16963 0.00992  0.00324  -0.01499 218 ILE A C   
1589 O O   . ILE A 211 ? 0.23992 0.28405 0.24969 0.00411  0.00999  -0.01954 218 ILE A O   
1590 C CB  . ILE A 211 ? 0.17542 0.19767 0.18334 0.00561  -0.00709 -0.01518 218 ILE A CB  
1591 C CG1 . ILE A 211 ? 0.17749 0.18996 0.18730 0.00657  -0.01139 -0.01611 218 ILE A CG1 
1592 C CG2 . ILE A 211 ? 0.20578 0.23028 0.20975 -0.00043 -0.01655 -0.00529 218 ILE A CG2 
1593 C CD1 . ILE A 211 ? 0.18922 0.18976 0.17628 -0.00586 -0.01458 -0.02014 218 ILE A CD1 
1594 N N   . THR A 212 ? 0.14492 0.19947 0.18168 0.01062  0.00089  -0.01120 219 THR A N   
1595 C CA  . THR A 212 ? 0.14341 0.20374 0.17767 0.00324  0.00522  -0.01065 219 THR A CA  
1596 C C   . THR A 212 ? 0.14090 0.18657 0.16861 -0.00384 -0.00258 -0.00290 219 THR A C   
1597 O O   . THR A 212 ? 0.14820 0.19023 0.18737 0.00038  -0.00876 -0.00105 219 THR A O   
1598 C CB  . THR A 212 ? 0.14087 0.22074 0.19325 0.00597  0.00849  -0.01310 219 THR A CB  
1599 O OG1 . THR A 212 ? 0.14248 0.23837 0.20457 0.01485  0.01445  -0.01615 219 THR A OG1 
1600 C CG2 . THR A 212 ? 0.19095 0.27599 0.23981 -0.00572 0.01302  -0.01290 219 THR A CG2 
1601 N N   . LEU A 213 ? 0.15830 0.19754 0.16936 -0.01411 -0.00198 0.00222  220 LEU A N   
1602 C CA  . LEU A 213 ? 0.14975 0.17396 0.15632 -0.02074 -0.01009 0.01422  220 LEU A CA  
1603 C C   . LEU A 213 ? 0.16435 0.18713 0.17733 -0.02796 -0.00593 0.01515  220 LEU A C   
1604 O O   . LEU A 213 ? 0.19591 0.22845 0.19960 -0.03833 0.00158  0.01458  220 LEU A O   
1605 C CB  . LEU A 213 ? 0.17103 0.19258 0.15381 -0.03118 -0.01276 0.02221  220 LEU A CB  
1606 C CG  . LEU A 213 ? 0.23302 0.24123 0.21088 -0.03895 -0.02216 0.04005  220 LEU A CG  
1607 C CD1 . LEU A 213 ? 0.22564 0.22161 0.22253 -0.02761 -0.03291 0.04700  220 LEU A CD1 
1608 C CD2 . LEU A 213 ? 0.22763 0.24145 0.17865 -0.05180 -0.02593 0.04919  220 LEU A CD2 
1609 N N   . PHE A 214 ? 0.17447 0.18654 0.20363 -0.02366 -0.00986 0.01482  221 PHE A N   
1610 C CA  . PHE A 214 ? 0.15306 0.15772 0.18803 -0.03289 -0.00646 0.01391  221 PHE A CA  
1611 C C   . PHE A 214 ? 0.17652 0.16018 0.20008 -0.04452 -0.01080 0.02982  221 PHE A C   
1612 O O   . PHE A 214 ? 0.23477 0.20580 0.25320 -0.04147 -0.01978 0.04304  221 PHE A O   
1613 C CB  . PHE A 214 ? 0.14100 0.13606 0.19578 -0.02534 -0.00854 0.00595  221 PHE A CB  
1614 C CG  . PHE A 214 ? 0.12358 0.14372 0.18953 -0.01921 -0.00388 -0.00862 221 PHE A CG  
1615 C CD1 . PHE A 214 ? 0.11701 0.15927 0.18075 -0.01236 -0.00243 -0.01033 221 PHE A CD1 
1616 C CD2 . PHE A 214 ? 0.15305 0.17297 0.23202 -0.02108 -0.00133 -0.02026 221 PHE A CD2 
1617 C CE1 . PHE A 214 ? 0.13224 0.19820 0.20750 -0.00726 -0.00004 -0.01897 221 PHE A CE1 
1618 C CE2 . PHE A 214 ? 0.13586 0.18395 0.22348 -0.01799 0.00180  -0.03170 221 PHE A CE2 
1619 C CZ  . PHE A 214 ? 0.12132 0.19317 0.20737 -0.01102 0.00163  -0.02868 221 PHE A CZ  
1620 N N   . VAL A 215 ? 0.19844 0.18043 0.21867 -0.05962 -0.00535 0.03073  222 VAL A N   
1621 C CA  . VAL A 215 ? 0.24107 0.20052 0.25114 -0.07345 -0.01001 0.04905  222 VAL A CA  
1622 C C   . VAL A 215 ? 0.26006 0.18828 0.28641 -0.07549 -0.01194 0.04857  222 VAL A C   
1623 O O   . VAL A 215 ? 0.25188 0.18217 0.29391 -0.06944 -0.00768 0.03076  222 VAL A O   
1624 C CB  . VAL A 215 ? 0.39904 0.37718 0.39052 -0.09303 -0.00274 0.05371  222 VAL A CB  
1625 C CG1 . VAL A 215 ? 0.35389 0.35478 0.32632 -0.09130 -0.00155 0.05552  222 VAL A CG1 
1626 C CG2 . VAL A 215 ? 0.28650 0.28644 0.28636 -0.09830 0.00761  0.03796  222 VAL A CG2 
1627 N N   . GLU A 216 ? 0.28401 0.18169 0.30752 -0.08289 -0.01909 0.06846  223 GLU A N   
1628 C CA  . GLU A 216 ? 0.33629 0.19435 0.37713 -0.08353 -0.02098 0.06890  223 GLU A CA  
1629 C C   . GLU A 216 ? 0.42703 0.27011 0.45864 -0.10915 -0.01730 0.07681  223 GLU A C   
1630 O O   . GLU A 216 ? 0.41967 0.27459 0.43108 -0.12474 -0.01822 0.09393  223 GLU A O   
1631 C CB  . GLU A 216 ? 0.33666 0.16434 0.38897 -0.06939 -0.03314 0.08810  223 GLU A CB  
1632 C CG  . GLU A 216 ? 0.33338 0.17912 0.39716 -0.04575 -0.03672 0.07963  223 GLU A CG  
1633 C CD  . GLU A 216 ? 0.36176 0.18815 0.43841 -0.03100 -0.04853 0.09919  223 GLU A CD  
1634 O OE1 . GLU A 216 ? 0.39427 0.19432 0.48747 -0.02210 -0.04668 0.09485  223 GLU A OE1 
1635 O OE2 . GLU A 216 ? 0.43613 0.28355 0.50103 -0.02838 -0.05669 0.11390  223 GLU A OE2 
1636 N N   . LYS A 217 ? 0.46524 0.28167 0.51102 -0.11509 -0.01298 0.06399  224 LYS A N   
1637 C CA  . LYS A 217 ? 0.52742 0.32214 0.56660 -0.13295 -0.00908 0.07185  224 LYS A CA  
1638 C C   . LYS A 217 ? 0.54363 0.30909 0.57973 -0.12509 -0.01759 0.09773  224 LYS A C   
1639 O O   . LYS A 217 ? 0.71152 0.48114 0.73232 -0.13957 -0.01879 0.11583  224 LYS A O   
1640 C CB  . LYS A 217 ? 0.54541 0.31485 0.59916 -0.13866 -0.00099 0.04983  224 LYS A CB  
1641 C CG  . LYS A 217 ? 0.65934 0.40467 0.72870 -0.11739 -0.00268 0.03385  224 LYS A CG  
1642 C CD  . LYS A 217 ? 0.67135 0.40246 0.74213 -0.12807 0.00293  0.00764  224 LYS A CD  
1643 C CE  . LYS A 217 ? 0.76534 0.44555 0.82774 -0.13847 0.00379  0.01199  224 LYS A CE  
1644 N NZ  . LYS A 217 ? 0.89802 0.54187 0.97526 -0.11171 0.00037  0.01477  224 LYS A NZ  
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