data_7HC2
# 
_entry.id   7HC2 
# 
_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   7HC2         pdb_00007hc2 10.2210/pdb7hc2/pdb 
WWPDB D_1001407284 ?            ?                   
# 
_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                        7HC2 
_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 'N-(pyridin-4-yl)cyclopropanecarboxamide' 162.188   1   ?        ? ? ? 
3 water       nat water                                     18.015    297 ?        ? ? ? 
# 
_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 'N-(pyridin-4-yl)cyclopropanecarboxamide' A1AW4 
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 
A1AW4 non-polymer         . 'N-(pyridin-4-yl)cyclopropanecarboxamide' ? 'C9 H10 N2 O'    162.188 
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        A1AW4 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1AW4 
_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 A1AW4 1   301 301 A1AW4 FCT A . 
C 3 HOH   1   401 185 HOH   HOH A . 
C 3 HOH   2   402 264 HOH   HOH A . 
C 3 HOH   3   403 260 HOH   HOH A . 
C 3 HOH   4   404 251 HOH   HOH A . 
C 3 HOH   5   405 281 HOH   HOH A . 
C 3 HOH   6   406 263 HOH   HOH A . 
C 3 HOH   7   407 79  HOH   HOH A . 
C 3 HOH   8   408 197 HOH   HOH A . 
C 3 HOH   9   409 131 HOH   HOH A . 
C 3 HOH   10  410 90  HOH   HOH A . 
C 3 HOH   11  411 103 HOH   HOH A . 
C 3 HOH   12  412 138 HOH   HOH A . 
C 3 HOH   13  413 193 HOH   HOH A . 
C 3 HOH   14  414 196 HOH   HOH A . 
C 3 HOH   15  415 295 HOH   HOH A . 
C 3 HOH   16  416 201 HOH   HOH A . 
C 3 HOH   17  417 289 HOH   HOH A . 
C 3 HOH   18  418 113 HOH   HOH A . 
C 3 HOH   19  419 235 HOH   HOH A . 
C 3 HOH   20  420 249 HOH   HOH A . 
C 3 HOH   21  421 272 HOH   HOH A . 
C 3 HOH   22  422 171 HOH   HOH A . 
C 3 HOH   23  423 47  HOH   HOH A . 
C 3 HOH   24  424 36  HOH   HOH A . 
C 3 HOH   25  425 211 HOH   HOH A . 
C 3 HOH   26  426 70  HOH   HOH A . 
C 3 HOH   27  427 2   HOH   HOH A . 
C 3 HOH   28  428 4   HOH   HOH A . 
C 3 HOH   29  429 150 HOH   HOH A . 
C 3 HOH   30  430 42  HOH   HOH A . 
C 3 HOH   31  431 65  HOH   HOH A . 
C 3 HOH   32  432 92  HOH   HOH A . 
C 3 HOH   33  433 149 HOH   HOH A . 
C 3 HOH   34  434 72  HOH   HOH A . 
C 3 HOH   35  435 67  HOH   HOH A . 
C 3 HOH   36  436 122 HOH   HOH A . 
C 3 HOH   37  437 95  HOH   HOH A . 
C 3 HOH   38  438 29  HOH   HOH A . 
C 3 HOH   39  439 114 HOH   HOH A . 
C 3 HOH   40  440 40  HOH   HOH A . 
C 3 HOH   41  441 45  HOH   HOH A . 
C 3 HOH   42  442 38  HOH   HOH A . 
C 3 HOH   43  443 26  HOH   HOH A . 
C 3 HOH   44  444 13  HOH   HOH A . 
C 3 HOH   45  445 155 HOH   HOH A . 
C 3 HOH   46  446 20  HOH   HOH A . 
C 3 HOH   47  447 212 HOH   HOH A . 
C 3 HOH   48  448 283 HOH   HOH A . 
C 3 HOH   49  449 64  HOH   HOH A . 
C 3 HOH   50  450 241 HOH   HOH A . 
C 3 HOH   51  451 49  HOH   HOH A . 
C 3 HOH   52  452 34  HOH   HOH A . 
C 3 HOH   53  453 9   HOH   HOH A . 
C 3 HOH   54  454 168 HOH   HOH A . 
C 3 HOH   55  455 53  HOH   HOH A . 
C 3 HOH   56  456 104 HOH   HOH A . 
C 3 HOH   57  457 81  HOH   HOH A . 
C 3 HOH   58  458 199 HOH   HOH A . 
C 3 HOH   59  459 87  HOH   HOH A . 
C 3 HOH   60  460 52  HOH   HOH A . 
C 3 HOH   61  461 15  HOH   HOH A . 
C 3 HOH   62  462 28  HOH   HOH A . 
C 3 HOH   63  463 180 HOH   HOH A . 
C 3 HOH   64  464 256 HOH   HOH A . 
C 3 HOH   65  465 194 HOH   HOH A . 
C 3 HOH   66  466 23  HOH   HOH A . 
C 3 HOH   67  467 74  HOH   HOH A . 
C 3 HOH   68  468 6   HOH   HOH A . 
C 3 HOH   69  469 156 HOH   HOH A . 
C 3 HOH   70  470 33  HOH   HOH A . 
C 3 HOH   71  471 18  HOH   HOH A . 
C 3 HOH   72  472 233 HOH   HOH A . 
C 3 HOH   73  473 11  HOH   HOH A . 
C 3 HOH   74  474 85  HOH   HOH A . 
C 3 HOH   75  475 59  HOH   HOH A . 
C 3 HOH   76  476 273 HOH   HOH A . 
C 3 HOH   77  477 60  HOH   HOH A . 
C 3 HOH   78  478 14  HOH   HOH A . 
C 3 HOH   79  479 94  HOH   HOH A . 
C 3 HOH   80  480 142 HOH   HOH A . 
C 3 HOH   81  481 136 HOH   HOH A . 
C 3 HOH   82  482 97  HOH   HOH A . 
C 3 HOH   83  483 30  HOH   HOH A . 
C 3 HOH   84  484 132 HOH   HOH A . 
C 3 HOH   85  485 19  HOH   HOH A . 
C 3 HOH   86  486 242 HOH   HOH A . 
C 3 HOH   87  487 61  HOH   HOH A . 
C 3 HOH   88  488 247 HOH   HOH A . 
C 3 HOH   89  489 83  HOH   HOH A . 
C 3 HOH   90  490 63  HOH   HOH A . 
C 3 HOH   91  491 175 HOH   HOH A . 
C 3 HOH   92  492 77  HOH   HOH A . 
C 3 HOH   93  493 99  HOH   HOH A . 
C 3 HOH   94  494 112 HOH   HOH A . 
C 3 HOH   95  495 10  HOH   HOH A . 
C 3 HOH   96  496 7   HOH   HOH A . 
C 3 HOH   97  497 220 HOH   HOH A . 
C 3 HOH   98  498 209 HOH   HOH A . 
C 3 HOH   99  499 121 HOH   HOH A . 
C 3 HOH   100 500 88  HOH   HOH A . 
C 3 HOH   101 501 68  HOH   HOH A . 
C 3 HOH   102 502 46  HOH   HOH A . 
C 3 HOH   103 503 134 HOH   HOH A . 
C 3 HOH   104 504 12  HOH   HOH A . 
C 3 HOH   105 505 107 HOH   HOH A . 
C 3 HOH   106 506 32  HOH   HOH A . 
C 3 HOH   107 507 102 HOH   HOH A . 
C 3 HOH   108 508 100 HOH   HOH A . 
C 3 HOH   109 509 73  HOH   HOH A . 
C 3 HOH   110 510 75  HOH   HOH A . 
C 3 HOH   111 511 119 HOH   HOH A . 
C 3 HOH   112 512 24  HOH   HOH A . 
C 3 HOH   113 513 244 HOH   HOH A . 
C 3 HOH   114 514 257 HOH   HOH A . 
C 3 HOH   115 515 25  HOH   HOH A . 
C 3 HOH   116 516 237 HOH   HOH A . 
C 3 HOH   117 517 174 HOH   HOH A . 
C 3 HOH   118 518 161 HOH   HOH A . 
C 3 HOH   119 519 80  HOH   HOH A . 
C 3 HOH   120 520 261 HOH   HOH A . 
C 3 HOH   121 521 41  HOH   HOH A . 
C 3 HOH   122 522 141 HOH   HOH A . 
C 3 HOH   123 523 44  HOH   HOH A . 
C 3 HOH   124 524 93  HOH   HOH A . 
C 3 HOH   125 525 162 HOH   HOH A . 
C 3 HOH   126 526 232 HOH   HOH A . 
C 3 HOH   127 527 124 HOH   HOH A . 
C 3 HOH   128 528 37  HOH   HOH A . 
C 3 HOH   129 529 8   HOH   HOH A . 
C 3 HOH   130 530 223 HOH   HOH A . 
C 3 HOH   131 531 221 HOH   HOH A . 
C 3 HOH   132 532 139 HOH   HOH A . 
C 3 HOH   133 533 78  HOH   HOH A . 
C 3 HOH   134 534 123 HOH   HOH A . 
C 3 HOH   135 535 3   HOH   HOH A . 
C 3 HOH   136 536 16  HOH   HOH A . 
C 3 HOH   137 537 255 HOH   HOH A . 
C 3 HOH   138 538 35  HOH   HOH A . 
C 3 HOH   139 539 222 HOH   HOH A . 
C 3 HOH   140 540 57  HOH   HOH A . 
C 3 HOH   141 541 5   HOH   HOH A . 
C 3 HOH   142 542 166 HOH   HOH A . 
C 3 HOH   143 543 71  HOH   HOH A . 
C 3 HOH   144 544 135 HOH   HOH A . 
C 3 HOH   145 545 126 HOH   HOH A . 
C 3 HOH   146 546 117 HOH   HOH A . 
C 3 HOH   147 547 133 HOH   HOH A . 
C 3 HOH   148 548 143 HOH   HOH A . 
C 3 HOH   149 549 224 HOH   HOH A . 
C 3 HOH   150 550 145 HOH   HOH A . 
C 3 HOH   151 551 109 HOH   HOH A . 
C 3 HOH   152 552 227 HOH   HOH A . 
C 3 HOH   153 553 31  HOH   HOH A . 
C 3 HOH   154 554 280 HOH   HOH A . 
C 3 HOH   155 555 48  HOH   HOH A . 
C 3 HOH   156 556 89  HOH   HOH A . 
C 3 HOH   157 557 246 HOH   HOH A . 
C 3 HOH   158 558 39  HOH   HOH A . 
C 3 HOH   159 559 163 HOH   HOH A . 
C 3 HOH   160 560 43  HOH   HOH A . 
C 3 HOH   161 561 172 HOH   HOH A . 
C 3 HOH   162 562 108 HOH   HOH A . 
C 3 HOH   163 563 137 HOH   HOH A . 
C 3 HOH   164 564 101 HOH   HOH A . 
C 3 HOH   165 565 82  HOH   HOH A . 
C 3 HOH   166 566 200 HOH   HOH A . 
C 3 HOH   167 567 66  HOH   HOH A . 
C 3 HOH   168 568 17  HOH   HOH A . 
C 3 HOH   169 569 297 HOH   HOH A . 
C 3 HOH   170 570 234 HOH   HOH A . 
C 3 HOH   171 571 187 HOH   HOH A . 
C 3 HOH   172 572 22  HOH   HOH A . 
C 3 HOH   173 573 294 HOH   HOH A . 
C 3 HOH   174 574 110 HOH   HOH A . 
C 3 HOH   175 575 278 HOH   HOH A . 
C 3 HOH   176 576 21  HOH   HOH A . 
C 3 HOH   177 577 291 HOH   HOH A . 
C 3 HOH   178 578 203 HOH   HOH A . 
C 3 HOH   179 579 248 HOH   HOH A . 
C 3 HOH   180 580 190 HOH   HOH A . 
C 3 HOH   181 581 182 HOH   HOH A . 
C 3 HOH   182 582 228 HOH   HOH A . 
C 3 HOH   183 583 91  HOH   HOH A . 
C 3 HOH   184 584 144 HOH   HOH A . 
C 3 HOH   185 585 176 HOH   HOH A . 
C 3 HOH   186 586 160 HOH   HOH A . 
C 3 HOH   187 587 1   HOH   HOH A . 
C 3 HOH   188 588 96  HOH   HOH A . 
C 3 HOH   189 589 120 HOH   HOH A . 
C 3 HOH   190 590 214 HOH   HOH A . 
C 3 HOH   191 591 188 HOH   HOH A . 
C 3 HOH   192 592 164 HOH   HOH A . 
C 3 HOH   193 593 69  HOH   HOH A . 
C 3 HOH   194 594 56  HOH   HOH A . 
C 3 HOH   195 595 51  HOH   HOH A . 
C 3 HOH   196 596 279 HOH   HOH A . 
C 3 HOH   197 597 147 HOH   HOH A . 
C 3 HOH   198 598 27  HOH   HOH A . 
C 3 HOH   199 599 98  HOH   HOH A . 
C 3 HOH   200 600 165 HOH   HOH A . 
C 3 HOH   201 601 239 HOH   HOH A . 
C 3 HOH   202 602 170 HOH   HOH A . 
C 3 HOH   203 603 179 HOH   HOH A . 
C 3 HOH   204 604 258 HOH   HOH A . 
C 3 HOH   205 605 177 HOH   HOH A . 
C 3 HOH   206 606 205 HOH   HOH A . 
C 3 HOH   207 607 265 HOH   HOH A . 
C 3 HOH   208 608 282 HOH   HOH A . 
C 3 HOH   209 609 207 HOH   HOH A . 
C 3 HOH   210 610 277 HOH   HOH A . 
C 3 HOH   211 611 148 HOH   HOH A . 
C 3 HOH   212 612 286 HOH   HOH A . 
C 3 HOH   213 613 267 HOH   HOH A . 
C 3 HOH   214 614 238 HOH   HOH A . 
C 3 HOH   215 615 275 HOH   HOH A . 
C 3 HOH   216 616 296 HOH   HOH A . 
C 3 HOH   217 617 202 HOH   HOH A . 
C 3 HOH   218 618 76  HOH   HOH A . 
C 3 HOH   219 619 292 HOH   HOH A . 
C 3 HOH   220 620 195 HOH   HOH A . 
C 3 HOH   221 621 106 HOH   HOH A . 
C 3 HOH   222 622 250 HOH   HOH A . 
C 3 HOH   223 623 50  HOH   HOH A . 
C 3 HOH   224 624 274 HOH   HOH A . 
C 3 HOH   225 625 215 HOH   HOH A . 
C 3 HOH   226 626 216 HOH   HOH A . 
C 3 HOH   227 627 271 HOH   HOH A . 
C 3 HOH   228 628 86  HOH   HOH A . 
C 3 HOH   229 629 167 HOH   HOH A . 
C 3 HOH   230 630 129 HOH   HOH A . 
C 3 HOH   231 631 178 HOH   HOH A . 
C 3 HOH   232 632 191 HOH   HOH A . 
C 3 HOH   233 633 284 HOH   HOH A . 
C 3 HOH   234 634 54  HOH   HOH A . 
C 3 HOH   235 635 154 HOH   HOH A . 
C 3 HOH   236 636 269 HOH   HOH A . 
C 3 HOH   237 637 217 HOH   HOH A . 
C 3 HOH   238 638 152 HOH   HOH A . 
C 3 HOH   239 639 58  HOH   HOH A . 
C 3 HOH   240 640 158 HOH   HOH A . 
C 3 HOH   241 641 181 HOH   HOH A . 
C 3 HOH   242 642 290 HOH   HOH A . 
C 3 HOH   243 643 204 HOH   HOH A . 
C 3 HOH   244 644 268 HOH   HOH A . 
C 3 HOH   245 645 210 HOH   HOH A . 
C 3 HOH   246 646 125 HOH   HOH A . 
C 3 HOH   247 647 262 HOH   HOH A . 
C 3 HOH   248 648 62  HOH   HOH A . 
C 3 HOH   249 649 276 HOH   HOH A . 
C 3 HOH   250 650 198 HOH   HOH A . 
C 3 HOH   251 651 226 HOH   HOH A . 
C 3 HOH   252 652 140 HOH   HOH A . 
C 3 HOH   253 653 285 HOH   HOH A . 
C 3 HOH   254 654 189 HOH   HOH A . 
C 3 HOH   255 655 146 HOH   HOH A . 
C 3 HOH   256 656 105 HOH   HOH A . 
C 3 HOH   257 657 245 HOH   HOH A . 
C 3 HOH   258 658 206 HOH   HOH A . 
C 3 HOH   259 659 159 HOH   HOH A . 
C 3 HOH   260 660 219 HOH   HOH A . 
C 3 HOH   261 661 130 HOH   HOH A . 
C 3 HOH   262 662 127 HOH   HOH A . 
C 3 HOH   263 663 116 HOH   HOH A . 
C 3 HOH   264 664 229 HOH   HOH A . 
C 3 HOH   265 665 231 HOH   HOH A . 
C 3 HOH   266 666 55  HOH   HOH A . 
C 3 HOH   267 667 288 HOH   HOH A . 
C 3 HOH   268 668 157 HOH   HOH A . 
C 3 HOH   269 669 169 HOH   HOH A . 
C 3 HOH   270 670 259 HOH   HOH A . 
C 3 HOH   271 671 151 HOH   HOH A . 
C 3 HOH   272 672 173 HOH   HOH A . 
C 3 HOH   273 673 213 HOH   HOH A . 
C 3 HOH   274 674 293 HOH   HOH A . 
C 3 HOH   275 675 240 HOH   HOH A . 
C 3 HOH   276 676 208 HOH   HOH A . 
C 3 HOH   277 677 115 HOH   HOH A . 
C 3 HOH   278 678 236 HOH   HOH A . 
C 3 HOH   279 679 118 HOH   HOH A . 
C 3 HOH   280 680 184 HOH   HOH A . 
C 3 HOH   281 681 287 HOH   HOH A . 
C 3 HOH   282 682 254 HOH   HOH A . 
C 3 HOH   283 683 183 HOH   HOH A . 
C 3 HOH   284 684 218 HOH   HOH A . 
C 3 HOH   285 685 153 HOH   HOH A . 
C 3 HOH   286 686 111 HOH   HOH A . 
C 3 HOH   287 687 253 HOH   HOH A . 
C 3 HOH   288 688 243 HOH   HOH A . 
C 3 HOH   289 689 186 HOH   HOH A . 
C 3 HOH   290 690 84  HOH   HOH A . 
C 3 HOH   291 691 266 HOH   HOH A . 
C 3 HOH   292 692 128 HOH   HOH A . 
C 3 HOH   293 693 192 HOH   HOH A . 
C 3 HOH   294 694 270 HOH   HOH A . 
C 3 HOH   295 695 225 HOH   HOH A . 
C 3 HOH   296 696 230 HOH   HOH A . 
C 3 HOH   297 697 252 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             592212.783 
_cell.length_a           66.300 
_cell.length_b           89.350 
_cell.length_c           99.970 
_cell.angle_beta         90.000 
_cell.angle_gamma        90.000 
_cell.angle_alpha        90.000 
_cell.entry_id           7HC2 
_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                         7HC2 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
# 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
_exptl.entry_id          7HC2 
# 
_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 EIGER X 16M' 
_diffrn_detector.pdbx_collection_date   2024-01-13 
_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   0.97919 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.pdbx_synchrotron_beamline   BL10U2 
_diffrn_source.type                        'SSRF BEAMLINE BL10U2' 
_diffrn_source.pdbx_wavelength_list        0.97919 
_diffrn_source.pdbx_synchrotron_site       SSRF 
_diffrn_source.pdbx_wavelength             ? 
# 
_reflns.entry_id                     7HC2 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             29.680 
_reflns.d_resolution_high            1.600 
_reflns.number_obs                   39453 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         99.900 
_reflns.pdbx_Rmerge_I_obs            0.075 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        17.200 
_reflns.B_iso_Wilson_estimate        ? 
_reflns.pdbx_redundancy              12.400 
_reflns.pdbx_Rrim_I_all              0.078 
_reflns.pdbx_Rpim_I_all              0.022 
_reflns.pdbx_CC_half                 0.999 
_reflns.pdbx_netI_over_av_sigmaI     ? 
_reflns.pdbx_number_measured_all     487661 
_reflns.pdbx_scaling_rejects         53 
_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 1.600 1.640  ? 29297 2881 ? 1.461 ? ? ? 10.200 ? 1.600  ? ? ? ? ? ? 100.000 1.539 0.476 0.670 
1 2 7.160 29.680 ? 4907  496  ? 0.038 ? ? ? 9.900  ? 42.300 ? ? ? ? ? ? 97.900  0.040 0.012 0.999 
# 
_refine.entry_id                                 7HC2 
_refine.pdbx_method_to_determine_struct          'FOURIER SYNTHESIS' 
_refine.ls_percent_reflns_R_free                 4.86 
_refine.pdbx_overall_phase_error                 21.1773 
_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                          0.1669 
_refine.B_iso_mean                               32.11 
_refine.ls_number_reflns_R_free                  1917 
_refine.ls_percent_reflns_obs                    99.87 
_refine.ls_R_factor_R_work                       0.1656 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_refine.ls_d_res_high                            1.60 
_refine.ls_number_reflns_obs                     39430 
_refine.pdbx_ls_sigma_F                          1.34 
_refine.ls_number_reflns_R_work                  37513 
_refine.ls_d_res_low                             24.78 
_refine.pdbx_stereochemistry_target_values       'GeoStd + Monomer Library + CDL v1.2' 
_refine.ls_R_factor_R_free                       0.1933 
_refine.overall_SU_ML                            0.1821 
_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         12 
_refine_hist.number_atoms_solvent             297 
_refine_hist.number_atoms_total               1953 
_refine_hist.d_res_high                       1.60 
_refine_hist.d_res_low                        24.78 
# 
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           1683 0.0158 ? ? ? 
'X-RAY DIFFRACTION' f_angle_d          2268 1.3866 ? ? ? 
'X-RAY DIFFRACTION' f_chiral_restr     260  0.0969 ? ? ? 
'X-RAY DIFFRACTION' f_plane_restr      289  0.0105 ? ? ? 
'X-RAY DIFFRACTION' f_dihedral_angle_d 226  6.9299 ? ? ? 
# 
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' 1.60 1.64  2630 0.2605 99.86  0.2949 131 . . . . . 
'X-RAY DIFFRACTION' 1.64 1.68  2666 0.2504 99.96  0.3220 126 . . . . . 
'X-RAY DIFFRACTION' 1.68 1.73  2638 0.2507 99.96  0.3042 139 . . . . . 
'X-RAY DIFFRACTION' 1.73 1.79  2655 0.2148 99.96  0.2423 145 . . . . . 
'X-RAY DIFFRACTION' 1.79 1.85  2651 0.1907 100.00 0.2192 141 . . . . . 
'X-RAY DIFFRACTION' 1.85 1.93  2664 0.2188 99.86  0.2465 123 . . . . . 
'X-RAY DIFFRACTION' 1.93 2.02  2653 0.1728 99.89  0.2224 138 . . . . . 
'X-RAY DIFFRACTION' 2.02 2.12  2659 0.1741 100.00 0.2073 144 . . . . . 
'X-RAY DIFFRACTION' 2.12 2.25  2671 0.1769 99.68  0.1878 127 . . . . . 
'X-RAY DIFFRACTION' 2.25 2.43  2671 0.1711 99.57  0.2043 129 . . . . . 
'X-RAY DIFFRACTION' 2.43 2.67  2710 0.1668 100.00 0.1861 147 . . . . . 
'X-RAY DIFFRACTION' 2.67 3.06  2681 0.1651 100.00 0.1947 142 . . . . . 
'X-RAY DIFFRACTION' 3.06 3.85  2734 0.1459 99.83  0.1653 134 . . . . . 
'X-RAY DIFFRACTION' 3.85 24.78 2830 0.1427 99.60  0.1706 151 . . . . . 
# 
_struct.entry_id                  7HC2 
_struct.title                     'PanDDA analysis group deposition -- Crystal structure of HSP90N in complex with 2X-5009' 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_details        ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HC2 
_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              7HC2 
_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 7HC2 MET A 1   ? UNP P07900 ? ? 'initiating methionine' 8   1 
1 7HC2 LEU A 230 ? UNP P07900 ? ? 'expression tag'        237 2 
1 7HC2 GLU A 231 ? UNP P07900 ? ? 'expression tag'        238 3 
1 7HC2 HIS A 232 ? UNP P07900 ? ? 'expression tag'        239 4 
1 7HC2 HIS A 233 ? UNP P07900 ? ? 'expression tag'        240 5 
1 7HC2 HIS A 234 ? UNP P07900 ? ? 'expression tag'        241 6 
1 7HC2 HIS A 235 ? UNP P07900 ? ? 'expression tag'        242 7 
1 7HC2 HIS A 236 ? UNP P07900 ? ? 'expression tag'        243 8 
1 7HC2 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  ? ASP A 59  ? GLU A 42  ASP A 66  1 ? 25 
HELX_P HELX_P3 AA3 PRO A 60  ? ASP A 64  ? PRO A 67  ASP A 71  5 ? 5  
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 VAL A 10  ? ALA A 14  ? VAL A 17  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                   7HC2 
_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 526 ? ? O A HOH 618 ? ? 1.92 
2 1 O   A HOH 608 ? ? O A HOH 624 ? ? 1.93 
3 1 O   A HOH 401 ? ? O A HOH 652 ? ? 2.05 
4 1 O   A HOH 640 ? ? O A HOH 678 ? ? 2.12 
5 1 O   A HOH 579 ? ? O A HOH 637 ? ? 2.13 
6 1 OE1 A GLU 199 ? ? O A HOH 401 ? ? 2.18 
7 1 OE2 A GLU 192 ? ? O A HOH 402 ? ? 2.18 
8 1 O   A HOH 623 ? ? O A HOH 649 ? ? 2.18 
9 1 O   A HOH 582 ? ? O A HOH 601 ? ? 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 569 ? ? 1_555 O A HOH 607 ? ? 8_444 1.90 
2 1 O A HOH 642 ? ? 1_555 O A HOH 642 ? ? 2_555 2.14 
3 1 O A HOH 669 ? ? 1_555 O A HOH 677 ? ? 3_555 2.15 
# 
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  ? ? -163.69 105.18  
2 1 THR A 94  ? ? -104.46 43.78   
3 1 ILE A 110 ? ? -96.94  59.93   
4 1 ALA A 166 ? ? 59.51   -142.86 
# 
_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     666 
_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 12.5174813428  -17.8861678865 -18.6663793212 0.187266564447 0.215576179546 0.235821777879 
0.0514966978188    -0.0338716346055  -0.0457385983707 2.01121989206 1.3071805917  4.1584118684  -0.567859351336  -1.58956907275   
0.315205610404  0.077113606292   0.045838697569   -0.189539876267 -0.0699251771024 -0.10828353012   -0.0503670931941 
0.0737537282707 0.235545873369   -0.0219695575191  
2 ? 'X-RAY DIFFRACTION' refined -5.12654889478 -6.30512887569 -20.9328020018 0.199554584916 0.206884967334 0.232727324909 
-0.00149077522032  -0.00254064280434 -0.0400301987343 1.75598805823 3.52651919785 3.96587274243 -1.43627875495   1.35835192173    
-2.42232377849  -0.0288015601201 0.187978929543   0.0616760317746 0.0815588589017  -0.093551998068  -0.0410075938526 
-0.243084053838 0.186070258879   0.00714768727448  
3 ? 'X-RAY DIFFRACTION' refined -10.0363065322 -15.0237392389 -25.2322130679 0.221603197727 0.241640026253 0.257829963896 
0.00898308860696   -0.0499544538398  -0.0749849719785 1.45936842221 2.51853814413 2.5519698919  -0.407843537047  -0.332640464781  
-0.748596006391 0.102075324085   0.273194357712   -0.196686229169 -0.150902549849  -0.0297500374899 0.293131129807   
0.129741889863  -0.19745087866   -0.0768841472009  
4 ? 'X-RAY DIFFRACTION' refined 10.5874005971  -6.69112253483 -18.1315225138 0.211996752253 0.192920382598 0.252297797082 
0.0159672599745    -0.00302191426236 -0.0027928782196 2.46936758309 2.34117267357 6.85553469225 0.797056123514   1.878369298      
2.45909171349   0.00823971966933 0.0503911171917  0.0636611238511 0.0336147627041  -0.0822814205843 -0.0905856780316 
-0.132813249359 0.265651044303   0.0570665073369   
5 ? 'X-RAY DIFFRACTION' refined 0.99432442768  -19.2481833105 -27.9000938443 0.22898100617  0.243022154079 0.257333310085 
0.0175049511514    -0.0229005173646  -0.0792999323759 2.49144429689 1.81178931827 2.59016324148 -0.938128320805  -0.0253759134104 
-0.119229052341 0.157426467845   0.406854896004   -0.375931026904 -0.191495946997  -0.104416462847  0.208698404479   
0.255390776445  -0.0822804012508 -0.0663575402473  
6 ? 'X-RAY DIFFRACTION' refined -5.52951050602 -20.2185833428 -10.3673525553 0.182482909017 0.161621492084 0.238090787056 
-0.0272565353637   -0.0252690903228  -0.0184056667967 2.44184012147 2.55124033529 3.50206744082 -0.752293912471  -0.663422993221  
-0.458339143538 -0.0682227472223 -0.111052623281  -0.260606643533 0.206286560483   -0.0016500678879 0.0549945601937  
0.318802888796  -0.0186908466223 0.0737649561017   
7 ? 'X-RAY DIFFRACTION' refined -13.9337828794 -13.5063392451 -14.6539281513 0.194441042617 0.203828443847 0.225166235345 
-3.70285458725e-05 0.000292106874993 -0.033147715616  2.86055089113 3.14906811004 2.99931121614 -0.0700589458527 -0.244530682237  
-0.446252405855 0.0718809700926  0.00759062795135 -0.225093397112 0.299854974527   -0.0467672807782 0.0439210694556  
0.097784091897  -0.186907317384  -0.00557796476031 
# 
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 99  A 84  . 
;chain 'A' and (resid 66 through 99 )
;
4 4 'X-RAY DIFFRACTION' A 100 A 85  A 136 A 121 . 
;chain 'A' and (resid 100 through 136 )
;
5 5 'X-RAY DIFFRACTION' A 137 A 122 A 182 A 167 . 
;chain 'A' and (resid 137 through 182 )
;
6 6 'X-RAY DIFFRACTION' A 183 A 168 A 210 A 195 . 
;chain 'A' and (resid 183 through 210 )
;
7 7 '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                       697 
_pdbx_distant_solvent_atoms.PDB_ins_code                      ? 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance   6.10 
_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 
A1AW4 C1   C N N 1   
A1AW4 C2   C Y N 2   
A1AW4 C3   C Y N 3   
A1AW4 C4   C Y N 4   
A1AW4 C5   C Y N 5   
A1AW4 C6   C Y N 6   
A1AW4 C7   C N N 7   
A1AW4 C8   C N N 8   
A1AW4 C9   C N N 9   
A1AW4 N1   N N N 10  
A1AW4 N2   N Y N 11  
A1AW4 O1   O N N 12  
A1AW4 H3   H N N 13  
A1AW4 H4   H N N 14  
A1AW4 H5   H N N 15  
A1AW4 H6   H N N 16  
A1AW4 H7   H N N 17  
A1AW4 H83  H N N 18  
A1AW4 H82  H N N 19  
A1AW4 H92  H N N 20  
A1AW4 H93  H N N 21  
A1AW4 H1   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 
A1AW4 O1  C1   doub N N 1   
A1AW4 C1  N1   sing N N 2   
A1AW4 C1  C7   sing N N 3   
A1AW4 N1  C2   sing N N 4   
A1AW4 C2  C3   doub Y N 5   
A1AW4 C2  C6   sing Y N 6   
A1AW4 C3  C4   sing Y N 7   
A1AW4 C4  N2   doub Y N 8   
A1AW4 N2  C5   sing Y N 9   
A1AW4 C5  C6   doub Y N 10  
A1AW4 C7  C8   sing N N 11  
A1AW4 C7  C9   sing N N 12  
A1AW4 C8  C9   sing N N 13  
A1AW4 C3  H3   sing N N 14  
A1AW4 C4  H4   sing N N 15  
A1AW4 C5  H5   sing N N 16  
A1AW4 C6  H6   sing N N 17  
A1AW4 C7  H7   sing N N 18  
A1AW4 C8  H83  sing N N 19  
A1AW4 C8  H82  sing N N 20  
A1AW4 C9  H92  sing N N 21  
A1AW4 C9  H93  sing N N 22  
A1AW4 N1  H1   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                    7HC2 
_atom_sites.fract_transf_matrix[1][1]   0.015083 
_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]   0.011192 
_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]   0.010003 
_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.
;
? 
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   ? 4.69705   -28.36069 -39.08502 1.000 54.06481 ? 16  GLU   A N   1 
ATOM   2    C CA  . GLU   A 1 9   ? 5.94203   -27.60012 -39.22893 1.000 65.97577 ? 16  GLU   A CA  1 
ATOM   3    C C   . GLU   A 1 9   ? 6.12480   -26.72021 -37.99679 1.000 56.80928 ? 16  GLU   A C   1 
ATOM   4    O O   . GLU   A 1 9   ? 5.37342   -25.75199 -37.77737 1.000 52.88248 ? 16  GLU   A O   1 
ATOM   5    C CB  . GLU   A 1 9   ? 5.94293   -26.73561 -40.50501 1.000 66.28208 ? 16  GLU   A CB  1 
ATOM   6    C CG  . GLU   A 1 9   ? 6.87196   -25.48397 -40.46001 1.000 74.19047 ? 16  GLU   A CG  1 
ATOM   7    C CD  . GLU   A 1 9   ? 8.34727   -25.76655 -40.80232 1.000 89.40899 ? 16  GLU   A CD  1 
ATOM   8    O OE1 . GLU   A 1 9   ? 8.65879   -26.90989 -41.23046 1.000 92.11751 ? 16  GLU   A OE1 1 
ATOM   9    O OE2 . GLU   A 1 9   ? 9.19509   -24.83754 -40.64787 1.000 79.04748 ? 16  GLU   A OE2 1 
ATOM   10   N N   . VAL   A 1 10  ? 7.10413   -27.07166 -37.17021 1.000 43.90753 ? 17  VAL   A N   1 
ATOM   11   C CA  . VAL   A 1 10  ? 7.31092   -26.43916 -35.87905 1.000 35.74923 ? 17  VAL   A CA  1 
ATOM   12   C C   . VAL   A 1 10  ? 8.66223   -25.75173 -35.92136 1.000 41.61079 ? 17  VAL   A C   1 
ATOM   13   O O   . VAL   A 1 10  ? 9.66104   -26.39147 -36.24698 1.000 42.72855 ? 17  VAL   A O   1 
ATOM   14   C CB  . VAL   A 1 10  ? 7.29907   -27.48566 -34.75328 1.000 43.96148 ? 17  VAL   A CB  1 
ATOM   15   C CG1 . VAL   A 1 10  ? 7.41778   -26.81835 -33.40433 1.000 40.51776 ? 17  VAL   A CG1 1 
ATOM   16   C CG2 . VAL   A 1 10  ? 6.10233   -28.40488 -34.88524 1.000 46.28049 ? 17  VAL   A CG2 1 
ATOM   17   N N   . GLU   A 1 11  ? 8.71665   -24.47491 -35.59361 1.000 33.33844 ? 18  GLU   A N   1 
ATOM   18   C CA  . GLU   A 1 11  ? 9.99213   -23.76533 -35.53629 1.000 32.30903 ? 18  GLU   A CA  1 
ATOM   19   C C   . GLU   A 1 11  ? 10.40968  -23.63044 -34.07087 1.000 28.01676 ? 18  GLU   A C   1 
ATOM   20   O O   . GLU   A 1 11  ? 9.59971   -23.28917 -33.19691 1.000 27.95862 ? 18  GLU   A O   1 
ATOM   21   C CB  . GLU   A 1 11  ? 9.85053   -22.39621 -36.18157 1.000 35.16948 ? 18  GLU   A CB  1 
ATOM   22   C CG  . GLU   A 1 11  ? 9.62371   -22.47726 -37.69755 1.000 35.64629 ? 18  GLU   A CG  1 
ATOM   23   C CD  . GLU   A 1 11  ? 9.40202   -21.09724 -38.30920 1.000 49.00446 ? 18  GLU   A CD  1 
ATOM   24   O OE1 . GLU   A 1 11  ? 8.32451   -20.50807 -38.07499 1.000 48.13047 ? 18  GLU   A OE1 1 
ATOM   25   O OE2 . GLU   A 1 11  ? 10.27427  -20.61245 -39.05518 1.000 55.76939 ? 18  GLU   A OE2 1 
ATOM   26   N N   . THR   A 1 12  ? 11.68682  -23.91543 -33.77632 1.000 27.68140 ? 19  THR   A N   1 
ATOM   27   C CA  . THR   A 1 12  ? 12.18997  -23.80978 -32.41782 1.000 26.11040 ? 19  THR   A CA  1 
ATOM   28   C C   . THR   A 1 12  ? 13.19263  -22.66735 -32.34762 1.000 26.87408 ? 19  THR   A C   1 
ATOM   29   O O   . THR   A 1 12  ? 14.06193  -22.56960 -33.20737 1.000 27.29896 ? 19  THR   A O   1 
ATOM   30   C CB  . THR   A 1 12  ? 12.87888  -25.11521 -31.98102 1.000 27.66625 ? 19  THR   A CB  1 
ATOM   31   O OG1 . THR   A 1 12  ? 11.98529  -26.21523 -32.16904 1.000 32.62081 ? 19  THR   A OG1 1 
ATOM   32   C CG2 . THR   A 1 12  ? 13.35880  -25.10243 -30.54027 1.000 28.90716 ? 19  THR   A CG2 1 
ATOM   33   N N   . PHE   A 1 13  ? 13.02617  -21.79167 -31.36925 1.000 26.14931 ? 20  PHE   A N   1 
ATOM   34   C CA  . PHE   A 1 13  ? 13.80894  -20.56867 -31.20159 1.000 27.89672 ? 20  PHE   A CA  1 
ATOM   35   C C   . PHE   A 1 13  ? 14.46272  -20.54146 -29.83548 1.000 25.92746 ? 20  PHE   A C   1 
ATOM   36   O O   . PHE   A 1 13  ? 13.91814  -21.04816 -28.86038 1.000 25.92620 ? 20  PHE   A O   1 
ATOM   37   C CB  . PHE   A 1 13  ? 12.90626  -19.32704 -31.25549 1.000 25.30301 ? 20  PHE   A CB  1 
ATOM   38   C CG  . PHE   A 1 13  ? 12.21350  -19.13820 -32.55587 1.000 28.39769 ? 20  PHE   A CG  1 
ATOM   39   C CD1 . PHE   A 1 13  ? 10.98611  -19.76677 -32.80807 1.000 30.46888 ? 20  PHE   A CD1 1 
ATOM   40   C CD2 . PHE   A 1 13  ? 12.76623  -18.32244 -33.55283 1.000 28.73697 ? 20  PHE   A CD2 1 
ATOM   41   C CE1 . PHE   A 1 13  ? 10.34965  -19.61641 -34.04010 1.000 30.69885 ? 20  PHE   A CE1 1 
ATOM   42   C CE2 . PHE   A 1 13  ? 12.09523  -18.10744 -34.76296 1.000 31.48198 ? 20  PHE   A CE2 1 
ATOM   43   C CZ  . PHE   A 1 13  ? 10.90083  -18.77631 -35.02874 1.000 33.18167 ? 20  PHE   A CZ  1 
ATOM   44   N N   . ALA   A 1 14  ? 15.65595  -19.94699 -29.73696 1.000 25.30450 ? 21  ALA   A N   1 
ATOM   45   C CA  . ALA   A 1 14  ? 16.26780  -19.68118 -28.44217 1.000 21.88575 ? 21  ALA   A CA  1 
ATOM   46   C C   . ALA   A 1 14  ? 15.73160  -18.37282 -27.89019 1.000 23.25241 ? 21  ALA   A C   1 
ATOM   47   O O   . ALA   A 1 14  ? 15.61940  -17.38591 -28.62953 1.000 26.17782 ? 21  ALA   A O   1 
ATOM   48   C CB  . ALA   A 1 14  ? 17.78121  -19.58093 -28.57518 1.000 24.55556 ? 21  ALA   A CB  1 
ATOM   49   N N   . PHE   A 1 15  ? 15.38548  -18.35229 -26.59776 1.000 24.05292 ? 22  PHE   A N   1 
ATOM   50   C CA  . PHE   A 1 15  ? 15.17425  -17.06342 -25.92899 1.000 23.18505 ? 22  PHE   A CA  1 
ATOM   51   C C   . PHE   A 1 15  ? 16.44587  -16.23911 -25.96410 1.000 24.43676 ? 22  PHE   A C   1 
ATOM   52   O O   . PHE   A 1 15  ? 17.55561  -16.76922 -25.82587 1.000 27.01443 ? 22  PHE   A O   1 
ATOM   53   C CB  . PHE   A 1 15  ? 14.78799  -17.25243 -24.45792 1.000 23.02378 ? 22  PHE   A CB  1 
ATOM   54   C CG  . PHE   A 1 15  ? 13.39493  -17.78571 -24.27319 1.000 20.55021 ? 22  PHE   A CG  1 
ATOM   55   C CD1 . PHE   A 1 15  ? 12.27742  -16.98361 -24.52644 1.000 22.97417 ? 22  PHE   A CD1 1 
ATOM   56   C CD2 . PHE   A 1 15  ? 13.22588  -19.06877 -23.76129 1.000 24.16970 ? 22  PHE   A CD2 1 
ATOM   57   C CE1 . PHE   A 1 15  ? 10.94678  -17.48054 -24.32208 1.000 24.37047 ? 22  PHE   A CE1 1 
ATOM   58   C CE2 . PHE   A 1 15  ? 11.94120  -19.58516 -23.53259 1.000 23.07924 ? 22  PHE   A CE2 1 
ATOM   59   C CZ  . PHE   A 1 15  ? 10.78757  -18.78404 -23.79709 1.000 22.87561 ? 22  PHE   A CZ  1 
ATOM   60   N N   . GLN   A 1 16  ? 16.27574  -14.92863 -26.10126 1.000 26.44012 ? 23  GLN   A N   1 
ATOM   61   C CA  . GLN   A 1 16  ? 17.42264  -14.07423 -25.78898 1.000 29.37743 ? 23  GLN   A CA  1 
ATOM   62   C C   . GLN   A 1 16  ? 17.93498  -14.33382 -24.37244 1.000 26.51171 ? 23  GLN   A C   1 
ATOM   63   O O   . GLN   A 1 16  ? 17.18244  -14.67613 -23.46220 1.000 26.80210 ? 23  GLN   A O   1 
ATOM   64   C CB  . GLN   A 1 16  ? 17.05975  -12.60492 -25.91396 1.000 30.24876 ? 23  GLN   A CB  1 
ATOM   65   C CG  . GLN   A 1 16  ? 16.65014  -12.19071 -27.26842 1.000 35.60982 ? 23  GLN   A CG  1 
ATOM   66   C CD  . GLN   A 1 16  ? 16.08623  -10.78308 -27.23153 1.000 44.23037 ? 23  GLN   A CD  1 
ATOM   67   O OE1 . GLN   A 1 16  ? 14.92004  -10.57700 -26.94777 1.000 44.81184 ? 23  GLN   A OE1 1 
ATOM   68   N NE2 . GLN   A 1 16  ? 16.94092  -9.79646  -27.50541 1.000 45.67520 ? 23  GLN   A NE2 1 
ATOM   69   N N   . ALA   A 1 17  ? 19.24430  -14.18400 -24.20266 1.000 23.94378 ? 24  ALA   A N   1 
ATOM   70   C CA  . ALA   A 1 17  ? 19.86369  -14.53213 -22.92596 1.000 25.45396 ? 24  ALA   A CA  1 
ATOM   71   C C   . ALA   A 1 17  ? 19.20764  -13.84050 -21.73966 1.000 27.52512 ? 24  ALA   A C   1 
ATOM   72   O O   . ALA   A 1 17  ? 19.02220  -14.44910 -20.67956 1.000 28.33010 ? 24  ALA   A O   1 
ATOM   73   C CB  . ALA   A 1 17  ? 21.33912  -14.16492 -22.99043 1.000 28.08895 ? 24  ALA   A CB  1 
ATOM   74   N N   . GLU   A 1 18  ? 18.88781  -12.56042 -21.88770 1.000 28.14598 ? 25  GLU   A N   1 
ATOM   75   C CA  . GLU   A 1 18  ? 18.36114  -11.79218 -20.76934 1.000 24.83640 ? 25  GLU   A CA  1 
ATOM   76   C C   . GLU   A 1 18  ? 16.99595  -12.31576 -20.33249 1.000 23.47074 ? 25  GLU   A C   1 
ATOM   77   O O   . GLU   A 1 18  ? 16.68513  -12.28465 -19.13197 1.000 25.33688 ? 25  GLU   A O   1 
ATOM   78   C CB  . GLU   A 1 18  ? 18.26464  -10.32142 -21.17337 1.000 30.41661 ? 25  GLU   A CB  1 
ATOM   79   C CG  . GLU   A 1 18  ? 19.58134  -9.67568  -21.50401 1.000 34.85908 ? 25  GLU   A CG  1 
ATOM   80   C CD  . GLU   A 1 18  ? 20.06210  -9.88025  -22.94586 1.000 46.74306 ? 25  GLU   A CD  1 
ATOM   81   O OE1 . GLU   A 1 18  ? 19.43821  -10.62103 -23.73930 1.000 36.72551 ? 25  GLU   A OE1 1 
ATOM   82   O OE2 . GLU   A 1 18  ? 21.07524  -9.24343  -23.31526 1.000 49.55810 ? 25  GLU   A OE2 1 
ATOM   83   N N   . ILE   A 1 19  ? 16.17388  -12.74338 -21.29972 1.000 27.09892 ? 26  ILE   A N   1 
ATOM   84   C CA  . ILE   A 1 19  ? 14.83695  -13.28684 -21.00829 1.000 25.17238 ? 26  ILE   A CA  1 
ATOM   85   C C   . ILE   A 1 19  ? 14.95244  -14.66147 -20.36990 1.000 26.06280 ? 26  ILE   A C   1 
ATOM   86   O O   . ILE   A 1 19  ? 14.25418  -14.96862 -19.39322 1.000 27.25510 ? 26  ILE   A O   1 
ATOM   87   C CB  . ILE   A 1 19  ? 13.98035  -13.34750 -22.29625 1.000 25.49949 ? 26  ILE   A CB  1 
ATOM   88   C CG1 . ILE   A 1 19  ? 13.44329  -11.97947 -22.61423 1.000 35.72383 ? 26  ILE   A CG1 1 
ATOM   89   C CG2 . ILE   A 1 19  ? 12.72097  -14.23310 -22.04460 1.000 31.25403 ? 26  ILE   A CG2 1 
ATOM   90   C CD1 . ILE   A 1 19  ? 14.41837  -11.01949 -23.07589 1.000 40.41980 ? 26  ILE   A CD1 1 
ATOM   91   N N   . ALA   A 1 20  ? 15.87018  -15.48573 -20.87844 1.000 23.44705 ? 27  ALA   A N   1 
ATOM   92   C CA  . ALA   A 1 20  ? 16.09760  -16.79497 -20.29724 1.000 23.38087 ? 27  ALA   A CA  1 
ATOM   93   C C   . ALA   A 1 20  ? 16.51548  -16.63091 -18.84366 1.000 24.04593 ? 27  ALA   A C   1 
ATOM   94   O O   . ALA   A 1 20  ? 16.10797  -17.42017 -17.97541 1.000 26.47021 ? 27  ALA   A O   1 
ATOM   95   C CB  . ALA   A 1 20  ? 17.18987  -17.56986 -21.05992 1.000 25.69874 ? 27  ALA   A CB  1 
ATOM   96   N N   . GLN   A 1 21  ? 17.34861  -15.61644 -18.56476 1.000 25.32594 ? 28  GLN   A N   1 
ATOM   97   C CA  . GLN   A 1 21  ? 17.80319  -15.40959 -17.18631 1.000 27.14479 ? 28  GLN   A CA  1 
ATOM   98   C C   . GLN   A 1 21  ? 16.64871  -15.00106 -16.29565 1.000 30.14699 ? 28  GLN   A C   1 
ATOM   99   O O   . GLN   A 1 21  ? 16.53464  -15.50072 -15.17327 1.000 28.77386 ? 28  GLN   A O   1 
ATOM   100  C CB  . GLN   A 1 21  ? 18.92083  -14.36603 -17.16396 1.000 27.86533 ? 28  GLN   A CB  1 
ATOM   101  C CG  . GLN   A 1 21  ? 19.51138  -14.04512 -15.77577 1.000 38.35260 ? 28  GLN   A CG  1 
ATOM   102  C CD  . GLN   A 1 21  ? 19.93929  -15.28615 -14.96313 1.000 59.79366 ? 28  GLN   A CD  1 
ATOM   103  O OE1 . GLN   A 1 21  ? 20.28073  -16.34018 -15.51803 1.000 60.20664 ? 28  GLN   A OE1 1 
ATOM   104  N NE2 . GLN   A 1 21  ? 19.92107  -15.14937 -13.62713 1.000 62.44912 ? 28  GLN   A NE2 1 
ATOM   105  N N   . LEU   A 1 22  ? 15.77475  -14.09578 -16.76142 1.000 22.77019 ? 29  LEU   A N   1 
ATOM   106  C CA  . LEU   A 1 22  ? 14.59805  -13.75148 -15.94312 1.000 23.91778 ? 29  LEU   A CA  1 
ATOM   107  C C   . LEU   A 1 22  ? 13.72114  -14.97259 -15.68789 1.000 24.35783 ? 29  LEU   A C   1 
ATOM   108  O O   . LEU   A 1 22  ? 13.25220  -15.19842 -14.55227 1.000 24.62140 ? 29  LEU   A O   1 
ATOM   109  C CB  . LEU   A 1 22  ? 13.80000  -12.63263 -16.63491 1.000 22.23334 ? 29  LEU   A CB  1 
ATOM   110  C CG  . LEU   A 1 22  ? 12.42525  -12.42261 -15.99125 1.000 25.20489 ? 29  LEU   A CG  1 
ATOM   111  C CD1 . LEU   A 1 22  ? 12.68814  -11.73571 -14.66714 1.000 27.23840 ? 29  LEU   A CD1 1 
ATOM   112  C CD2 . LEU   A 1 22  ? 11.61569  -11.57021 -16.92477 1.000 27.90372 ? 29  LEU   A CD2 1 
ATOM   113  N N   . MET   A 1 23  ? 13.49244  -15.79909 -16.72152 1.000 22.28426 ? 30  MET   A N   1 
ATOM   114  C CA  . MET   A 1 23  ? 12.67754  -16.98356 -16.52588 1.000 22.00389 ? 30  MET   A CA  1 
ATOM   115  C C   . MET   A 1 23  ? 13.29503  -17.91275 -15.48675 1.000 26.28879 ? 30  MET   A C   1 
ATOM   116  O O   . MET   A 1 23  ? 12.56747  -18.52998 -14.69338 1.000 24.55145 ? 30  MET   A O   1 
ATOM   117  C CB  . MET   A 1 23  ? 12.50578  -17.70019 -17.87833 1.000 22.03751 ? 30  MET   A CB  1 
ATOM   118  C CG  . MET   A 1 23  ? 11.56447  -16.93620 -18.80636 1.000 23.34233 ? 30  MET   A CG  1 
ATOM   119  S SD  . MET   A 1 23  ? 11.44713  -17.67622 -20.44792 1.000 26.23029 ? 30  MET   A SD  1 
ATOM   120  C CE  . MET   A 1 23  ? 10.37530  -19.02760 -20.03416 1.000 25.92212 ? 30  MET   A CE  1 
ATOM   121  N N   . SER   A 1 24  ? 14.61640  -18.09480 -15.52087 1.000 25.16477 ? 31  SER   A N   1 
ATOM   122  C CA  . SER   A 1 24  ? 15.27055  -18.97140 -14.54913 1.000 24.15782 ? 31  SER   A CA  1 
ATOM   123  C C   . SER   A 1 24  ? 15.12722  -18.39773 -13.14446 1.000 26.74344 ? 31  SER   A C   1 
ATOM   124  O O   . SER   A 1 24  ? 14.93022  -19.14636 -12.18769 1.000 29.97772 ? 31  SER   A O   1 
ATOM   125  C CB  . SER   A 1 24  ? 16.73960  -19.18321 -14.99513 1.000 29.67767 ? 31  SER   A CB  1 
ATOM   126  O OG  . SER   A 1 24  ? 17.53934  -19.52551 -13.92610 1.000 41.22540 ? 31  SER   A OG  1 
ATOM   127  N N   . LEU   A 1 25  ? 15.17821  -17.06485 -12.99046 1.000 24.79606 ? 32  LEU   A N   1 
ATOM   128  C CA  . LEU   A 1 25  ? 14.94911  -16.47605 -11.66161 1.000 24.69579 ? 32  LEU   A CA  1 
ATOM   129  C C   . LEU   A 1 25  ? 13.52187  -16.71031 -11.18743 1.000 28.08076 ? 32  LEU   A C   1 
ATOM   130  O O   . LEU   A 1 25  ? 13.28615  -16.98759 -10.00643 1.000 26.15821 ? 32  LEU   A O   1 
ATOM   131  C CB  . LEU   A 1 25  ? 15.25119  -14.98398 -11.70212 1.000 29.43698 ? 32  LEU   A CB  1 
ATOM   132  C CG  . LEU   A 1 25  ? 16.76229  -14.70803 -11.83308 1.000 27.42023 ? 32  LEU   A CG  1 
ATOM   133  C CD1 . LEU   A 1 25  ? 16.95508  -13.22742 -11.96952 1.000 31.57453 ? 32  LEU   A CD1 1 
ATOM   134  C CD2 . LEU   A 1 25  ? 17.43559  -15.11166 -10.55664 1.000 29.67900 ? 32  LEU   A CD2 1 
ATOM   135  N N   . ILE   A 1 26  ? 12.54846  -16.57317 -12.08677 1.000 23.61185 ? 33  ILE   A N   1 
ATOM   136  C CA  . ILE   A 1 26  ? 11.16108  -16.79786 -11.70522 1.000 24.29727 ? 33  ILE   A CA  1 
ATOM   137  C C   . ILE   A 1 26  ? 10.94943  -18.24831 -11.28222 1.000 29.15492 ? 33  ILE   A C   1 
ATOM   138  O O   . ILE   A 1 26  ? 10.20172  -18.55062 -10.33309 1.000 28.60063 ? 33  ILE   A O   1 
ATOM   139  C CB  . ILE   A 1 26  ? 10.26050  -16.41442 -12.87950 1.000 21.37393 ? 33  ILE   A CB  1 
ATOM   140  C CG1 . ILE   A 1 26  ? 10.31811  -14.89002 -13.06870 1.000 23.66582 ? 33  ILE   A CG1 1 
ATOM   141  C CG2 . ILE   A 1 26  ? 8.83529   -17.00276 -12.68295 1.000 22.74426 ? 33  ILE   A CG2 1 
ATOM   142  C CD1 . ILE   A 1 26  ? 9.63252   -14.40179 -14.39054 1.000 23.03964 ? 33  ILE   A CD1 1 
ATOM   143  N N   . ILE   A 1 27  ? 11.59024  -19.16695 -11.97609 1.000 24.06881 ? 34  ILE   A N   1 
ATOM   144  C CA  . ILE   A 1 27  ? 11.32585  -20.57069 -11.71791 1.000 26.82822 ? 34  ILE   A CA  1 
ATOM   145  C C   . ILE   A 1 27  ? 12.04893  -21.04325 -10.45040 1.000 28.02352 ? 34  ILE   A C   1 
ATOM   146  O O   . ILE   A 1 27  ? 11.52708  -21.85919 -9.69520  1.000 33.18950 ? 34  ILE   A O   1 
ATOM   147  C CB  . ILE   A 1 27  ? 11.73355  -21.38705 -12.96134 1.000 26.73523 ? 34  ILE   A CB  1 
ATOM   148  C CG1 . ILE   A 1 27  ? 10.73672  -21.13085 -14.11353 1.000 27.15340 ? 34  ILE   A CG1 1 
ATOM   149  C CG2 . ILE   A 1 27  ? 11.90801  -22.87672 -12.60976 1.000 30.76020 ? 34  ILE   A CG2 1 
ATOM   150  C CD1 . ILE   A 1 27  ? 11.30932  -21.63797 -15.48021 1.000 27.36221 ? 34  ILE   A CD1 1 
ATOM   151  N N   . ASN   A 1 28  ? 13.26475  -20.54672 -10.20441 1.000 26.69281 ? 35  ASN   A N   1 
ATOM   152  C CA  . ASN   A 1 28  ? 14.12624  -21.07313 -9.15340  1.000 28.77082 ? 35  ASN   A CA  1 
ATOM   153  C C   . ASN   A 1 28  ? 14.11915  -20.28070 -7.85924  1.000 33.42290 ? 35  ASN   A C   1 
ATOM   154  O O   . ASN   A 1 28  ? 14.54876  -20.82878 -6.83970  1.000 33.99286 ? 35  ASN   A O   1 
ATOM   155  C CB  . ASN   A 1 28  ? 15.53955  -21.11975 -9.67217  1.000 32.47763 ? 35  ASN   A CB  1 
ATOM   156  C CG  . ASN   A 1 28  ? 15.68830  -22.14755 -10.72619 1.000 42.06084 ? 35  ASN   A CG  1 
ATOM   157  O OD1 . ASN   A 1 28  ? 15.10242  -23.22661 -10.62949 1.000 39.10604 ? 35  ASN   A OD1 1 
ATOM   158  N ND2 . ASN   A 1 28  ? 16.31237  -21.77188 -11.82086 1.000 49.10029 ? 35  ASN   A ND2 1 
ATOM   159  N N   . THR   A 1 29  ? 13.69629  -19.01336 -7.85907  1.000 25.06737 ? 36  THR   A N   1 
ATOM   160  C CA  . THR   A 1 29  ? 13.75003  -18.25683 -6.60808  1.000 27.56987 ? 36  THR   A CA  1 
ATOM   161  C C   . THR   A 1 29  ? 12.62304  -18.69483 -5.67603  1.000 24.03814 ? 36  THR   A C   1 
ATOM   162  O O   . THR   A 1 29  ? 11.46921  -18.79718 -6.10226  1.000 27.04169 ? 36  THR   A O   1 
ATOM   163  C CB  . THR   A 1 29  ? 13.64531  -16.74773 -6.89145  1.000 28.90479 ? 36  THR   A CB  1 
ATOM   164  O OG1 . THR   A 1 29  ? 14.72566  -16.34587 -7.73603  1.000 30.41431 ? 36  THR   A OG1 1 
ATOM   165  C CG2 . THR   A 1 29  ? 13.69094  -15.93577 -5.57146  1.000 28.92660 ? 36  THR   A CG2 1 
ATOM   166  N N   . PHE   A 1 30  ? 12.95859  -18.91089 -4.39020  1.000 26.57118 ? 37  PHE   A N   1 
ATOM   167  C CA  . PHE   A 1 30  ? 11.92146  -19.19232 -3.41342  1.000 29.86022 ? 37  PHE   A CA  1 
ATOM   168  C C   . PHE   A 1 30  ? 11.07140  -17.93924 -3.17936  1.000 28.25617 ? 37  PHE   A C   1 
ATOM   169  O O   . PHE   A 1 30  ? 11.59079  -16.87546 -2.80030  1.000 29.28073 ? 37  PHE   A O   1 
ATOM   170  C CB  . PHE   A 1 30  ? 12.54616  -19.69015 -2.11381  1.000 28.16715 ? 37  PHE   A CB  1 
ATOM   171  C CG  . PHE   A 1 30  ? 11.52304  -19.95035 -1.06723  1.000 26.79527 ? 37  PHE   A CG  1 
ATOM   172  C CD1 . PHE   A 1 30  ? 10.70414  -21.06944 -1.17562  1.000 30.67269 ? 37  PHE   A CD1 1 
ATOM   173  C CD2 . PHE   A 1 30  ? 11.30711  -19.03718 -0.02011  1.000 29.45136 ? 37  PHE   A CD2 1 
ATOM   174  C CE1 . PHE   A 1 30  ? 9.69151   -21.29916 -0.23955  1.000 30.48464 ? 37  PHE   A CE1 1 
ATOM   175  C CE2 . PHE   A 1 30  ? 10.31180  -19.26131 0.90116   1.000 34.83735 ? 37  PHE   A CE2 1 
ATOM   176  C CZ  . PHE   A 1 30  ? 9.52442   -20.39232 0.81898   1.000 31.83025 ? 37  PHE   A CZ  1 
ATOM   177  N N   . TYR   A 1 31  ? 9.76127   -18.06136 -3.39525  1.000 23.03437 ? 38  TYR   A N   1 
ATOM   178  C CA  . TYR   A 1 31  ? 8.90192   -16.87045 -3.42364  1.000 24.08502 ? 38  TYR   A CA  1 
ATOM   179  C C   . TYR   A 1 31  ? 7.46761   -17.33848 -3.27733  1.000 26.79181 ? 38  TYR   A C   1 
ATOM   180  O O   . TYR   A 1 31  ? 6.91935   -17.90196 -4.21679  1.000 24.65147 ? 38  TYR   A O   1 
ATOM   181  C CB  . TYR   A 1 31  ? 9.08608   -16.09319 -4.73993  1.000 24.96037 ? 38  TYR   A CB  1 
ATOM   182  C CG  . TYR   A 1 31  ? 8.29232   -14.81167 -4.80720  1.000 24.92417 ? 38  TYR   A CG  1 
ATOM   183  C CD1 . TYR   A 1 31  ? 8.67304   -13.72328 -4.05242  1.000 27.66334 ? 38  TYR   A CD1 1 
ATOM   184  C CD2 . TYR   A 1 31  ? 7.12991   -14.71180 -5.59674  1.000 25.64610 ? 38  TYR   A CD2 1 
ATOM   185  C CE1 . TYR   A 1 31  ? 7.93552   -12.54521 -4.07719  1.000 30.02952 ? 38  TYR   A CE1 1 
ATOM   186  C CE2 . TYR   A 1 31  ? 6.41258   -13.53878 -5.62907  1.000 25.66628 ? 38  TYR   A CE2 1 
ATOM   187  C CZ  . TYR   A 1 31  ? 6.81956   -12.47164 -4.88694  1.000 31.09141 ? 38  TYR   A CZ  1 
ATOM   188  O OH  . TYR   A 1 31  ? 6.10387   -11.29607 -4.87777  1.000 31.17885 ? 38  TYR   A OH  1 
ATOM   189  N N   . SER   A 1 32  ? 6.87151   -17.14356 -2.09039  1.000 23.05173 ? 39  SER   A N   1 
ATOM   190  C CA  . SER   A 1 32  ? 5.59407   -17.80100 -1.83740  1.000 23.23678 ? 39  SER   A CA  1 
ATOM   191  C C   . SER   A 1 32  ? 4.40971   -17.09716 -2.47482  1.000 24.41323 ? 39  SER   A C   1 
ATOM   192  O O   . SER   A 1 32  ? 3.37613   -17.73839 -2.62824  1.000 26.65454 ? 39  SER   A O   1 
ATOM   193  C CB  . SER   A 1 32  ? 5.35869   -17.91860 -0.33568  1.000 26.76363 ? 39  SER   A CB  1 
ATOM   194  O OG  . SER   A 1 32  ? 6.39741   -18.71166 0.25421   1.000 26.95953 ? 39  SER   A OG  1 
ATOM   195  N N   . ASN   A 1 33  ? 4.53892   -15.83713 -2.85538  1.000 23.68859 ? 40  ASN   A N   1 
ATOM   196  C CA  . ASN   A 1 33  ? 3.40023   -15.04526 -3.34879  1.000 22.31067 ? 40  ASN   A CA  1 
ATOM   197  C C   . ASN   A 1 33  ? 3.12237   -15.33529 -4.83477  1.000 25.90297 ? 40  ASN   A C   1 
ATOM   198  O O   . ASN   A 1 33  ? 3.15276   -14.44256 -5.68536  1.000 25.99001 ? 40  ASN   A O   1 
ATOM   199  C CB  . ASN   A 1 33  ? 3.76262   -13.57832 -3.11366  1.000 26.23168 ? 40  ASN   A CB  1 
ATOM   200  C CG  . ASN   A 1 33  ? 2.68003   -12.59925 -3.53415  1.000 27.10833 ? 40  ASN   A CG  1 
ATOM   201  O OD1 . ASN   A 1 33  ? 1.49067   -12.84486 -3.34305  1.000 30.78460 ? 40  ASN   A OD1 1 
ATOM   202  N ND2 . ASN   A 1 33  ? 3.10995   -11.44775 -4.02742  1.000 29.04914 ? 40  ASN   A ND2 1 
ATOM   203  N N   . LYS   A 1 34  ? 2.83184   -16.60628 -5.13838  1.000 23.30575 ? 41  LYS   A N   1 
ATOM   204  C CA  . LYS   A 1 34  ? 2.71958   -16.99430 -6.53928  1.000 24.18411 ? 41  LYS   A CA  1 
ATOM   205  C C   . LYS   A 1 34  ? 1.41851   -16.52290 -7.17627  1.000 23.20607 ? 41  LYS   A C   1 
ATOM   206  O O   . LYS   A 1 34  ? 1.35980   -16.44309 -8.40097  1.000 22.03415 ? 41  LYS   A O   1 
ATOM   207  C CB  . LYS   A 1 34  ? 2.81456   -18.52088 -6.64512  1.000 22.30326 ? 41  LYS   A CB  1 
ATOM   208  C CG  . LYS   A 1 34  ? 4.22235   -19.06594 -6.36771  1.000 22.79901 ? 41  LYS   A CG  1 
ATOM   209  C CD  . LYS   A 1 34  ? 4.15774   -20.57631 -6.51823  1.000 25.98210 ? 41  LYS   A CD  1 
ATOM   210  C CE  . LYS   A 1 34  ? 5.51842   -21.23474 -6.23726  1.000 27.62324 ? 41  LYS   A CE  1 
ATOM   211  N NZ  . LYS   A 1 34  ? 6.39202   -21.07786 -7.39196  1.000 28.96781 ? 41  LYS   A NZ  1 
ATOM   212  N N   . GLU   A 1 35  ? 0.42906   -16.11364 -6.38127  1.000 22.16772 ? 42  GLU   A N   1 
ATOM   213  C CA  . GLU   A 1 35  ? -0.89551  -15.86305 -6.94444  1.000 20.49459 ? 42  GLU   A CA  1 
ATOM   214  C C   . GLU   A 1 35  ? -0.93568  -14.64787 -7.85825  1.000 24.96999 ? 42  GLU   A C   1 
ATOM   215  O O   . GLU   A 1 35  ? -1.90064  -14.49845 -8.61462  1.000 24.32502 ? 42  GLU   A O   1 
ATOM   216  C CB  . GLU   A 1 35  ? -1.90349  -15.63701 -5.80327  1.000 23.18374 ? 42  GLU   A CB  1 
ATOM   217  C CG  . GLU   A 1 35  ? -1.70343  -14.34641 -5.02226  1.000 23.65839 ? 42  GLU   A CG  1 
ATOM   218  C CD  . GLU   A 1 35  ? -2.55305  -14.26484 -3.73954  1.000 30.04623 ? 42  GLU   A CD  1 
ATOM   219  O OE1 . GLU   A 1 35  ? -2.66969  -15.27440 -3.01068  1.000 39.04125 ? 42  GLU   A OE1 1 
ATOM   220  O OE2 . GLU   A 1 35  ? -2.97832  -13.16402 -3.37432  1.000 38.39385 ? 42  GLU   A OE2 1 
ATOM   221  N N   . ILE   A 1 36  ? 0.09187   -13.79267 -7.82692  1.000 20.07397 ? 43  ILE   A N   1 
ATOM   222  C CA  . ILE   A 1 36  ? 0.10278   -12.59356 -8.66006  1.000 19.63550 ? 43  ILE   A CA  1 
ATOM   223  C C   . ILE   A 1 36  ? 0.24072   -12.91583 -10.13277 1.000 20.58509 ? 43  ILE   A C   1 
ATOM   224  O O   . ILE   A 1 36  ? 0.00207   -12.02516 -10.95881 1.000 21.22698 ? 43  ILE   A O   1 
ATOM   225  C CB  . ILE   A 1 36  ? 1.21699   -11.59562 -8.28409  1.000 22.70197 ? 43  ILE   A CB  1 
ATOM   226  C CG1 . ILE   A 1 36  ? 2.60356   -12.23354 -8.47863  1.000 24.79386 ? 43  ILE   A CG1 1 
ATOM   227  C CG2 . ILE   A 1 36  ? 0.99449   -11.16354 -6.82470  1.000 25.83457 ? 43  ILE   A CG2 1 
ATOM   228  C CD1 . ILE   A 1 36  ? 3.73498   -11.24530 -8.15569  1.000 30.19226 ? 43  ILE   A CD1 1 
ATOM   229  N N   . PHE   A 1 37  ? 0.50954   -14.17078 -10.49280 1.000 19.92380 ? 44  PHE   A N   1 
ATOM   230  C CA  . PHE   A 1 37  ? 0.54206   -14.49258 -11.93516 1.000 19.35031 ? 44  PHE   A CA  1 
ATOM   231  C C   . PHE   A 1 37  ? -0.78853  -14.11973 -12.58982 1.000 23.78779 ? 44  PHE   A C   1 
ATOM   232  O O   . PHE   A 1 37  ? -0.81867  -13.69628 -13.77241 1.000 22.23779 ? 44  PHE   A O   1 
ATOM   233  C CB  . PHE   A 1 37  ? 0.85531   -16.00079 -12.16726 1.000 21.28789 ? 44  PHE   A CB  1 
ATOM   234  C CG  . PHE   A 1 37  ? -0.35099  -16.88518 -11.97147 1.000 20.98232 ? 44  PHE   A CG  1 
ATOM   235  C CD1 . PHE   A 1 37  ? -0.68236  -17.35535 -10.69929 1.000 22.67617 ? 44  PHE   A CD1 1 
ATOM   236  C CD2 . PHE   A 1 37  ? -1.16076  -17.21460 -13.04503 1.000 21.63315 ? 44  PHE   A CD2 1 
ATOM   237  C CE1 . PHE   A 1 37  ? -1.83429  -18.12417 -10.49555 1.000 23.31548 ? 44  PHE   A CE1 1 
ATOM   238  C CE2 . PHE   A 1 37  ? -2.32800  -17.95305 -12.86038 1.000 21.54034 ? 44  PHE   A CE2 1 
ATOM   239  C CZ  . PHE   A 1 37  ? -2.67841  -18.41627 -11.59092 1.000 21.07070 ? 44  PHE   A CZ  1 
ATOM   240  N N   . LEU   A 1 38  ? -1.89924  -14.30139 -11.85794 1.000 20.79032 ? 45  LEU   A N   1 
ATOM   241  C CA  . LEU   A 1 38  ? -3.18667  -14.15222 -12.53494 1.000 18.96770 ? 45  LEU   A CA  1 
ATOM   242  C C   . LEU   A 1 38  ? -3.47877  -12.68402 -12.74713 1.000 21.13519 ? 45  LEU   A C   1 
ATOM   243  O O   . LEU   A 1 38  ? -3.98516  -12.28422 -13.80967 1.000 22.26561 ? 45  LEU   A O   1 
ATOM   244  C CB  . LEU   A 1 38  ? -4.28151  -14.79141 -11.71853 1.000 21.29076 ? 45  LEU   A CB  1 
ATOM   245  C CG  . LEU   A 1 38  ? -5.65942  -14.81359 -12.41344 1.000 23.50908 ? 45  LEU   A CG  1 
ATOM   246  C CD1 . LEU   A 1 38  ? -5.63104  -15.64242 -13.67331 1.000 22.00260 ? 45  LEU   A CD1 1 
ATOM   247  C CD2 . LEU   A 1 38  ? -6.66225  -15.36945 -11.43346 1.000 26.55445 ? 45  LEU   A CD2 1 
ATOM   248  N N   . ARG   A 1 39  ? -3.11764  -11.85596 -11.76935 1.000 22.50433 ? 46  ARG   A N   1 
ATOM   249  C CA  . ARG   A 1 39  ? -3.24411  -10.41274 -11.94413 1.000 20.79076 ? 46  ARG   A CA  1 
ATOM   250  C C   . ARG   A 1 39  ? -2.48215  -9.96327  -13.16752 1.000 22.86460 ? 46  ARG   A C   1 
ATOM   251  O O   . ARG   A 1 39  ? -2.93791  -9.10903  -13.94909 1.000 22.23486 ? 46  ARG   A O   1 
ATOM   252  C CB  . ARG   A 1 39  ? -2.66223  -9.72419  -10.71472 1.000 24.01627 ? 46  ARG   A CB  1 
ATOM   253  C CG  . ARG   A 1 39  ? -2.61243  -8.26020  -10.74453 1.000 28.76953 ? 46  ARG   A CG  1 
ATOM   254  C CD  . ARG   A 1 39  ? -1.89329  -7.68294  -9.51240  1.000 28.35177 ? 46  ARG   A CD  1 
ATOM   255  N NE  . ARG   A 1 39  ? -0.44073  -7.90628  -9.52830  1.000 30.33666 ? 46  ARG   A NE  1 
ATOM   256  C CZ  . ARG   A 1 39  ? 0.33019   -7.71089  -8.47865  1.000 34.80264 ? 46  ARG   A CZ  1 
ATOM   257  N NH1 . ARG   A 1 39  ? -0.17593  -7.33653  -7.30597  1.000 30.88405 ? 46  ARG   A NH1 1 
ATOM   258  N NH2 . ARG   A 1 39  ? 1.65960   -7.83186  -8.61658  1.000 30.95062 ? 46  ARG   A NH2 1 
ATOM   259  N N   . GLU   A 1 40  ? -1.28066  -10.50503 -13.34129 1.000 19.53364 ? 47  GLU   A N   1 
ATOM   260  C CA  . GLU   A 1 40  ? -0.45901  -10.03412 -14.44400 1.000 19.62981 ? 47  GLU   A CA  1 
ATOM   261  C C   . GLU   A 1 40  ? -1.04930  -10.42754 -15.78156 1.000 21.35973 ? 47  GLU   A C   1 
ATOM   262  O O   . GLU   A 1 40  ? -0.99877  -9.63692  -16.73765 1.000 21.77775 ? 47  GLU   A O   1 
ATOM   263  C CB  . GLU   A 1 40  ? 0.98507   -10.60985 -14.31098 1.000 19.21529 ? 47  GLU   A CB  1 
ATOM   264  C CG  . GLU   A 1 40  ? 1.75712   -10.09178 -13.09828 1.000 25.69954 ? 47  GLU   A CG  1 
ATOM   265  C CD  . GLU   A 1 40  ? 1.65090   -8.58011  -12.88696 1.000 26.02799 ? 47  GLU   A CD  1 
ATOM   266  O OE1 . GLU   A 1 40  ? 1.77459   -7.83196  -13.86455 1.000 29.91929 ? 47  GLU   A OE1 1 
ATOM   267  O OE2 . GLU   A 1 40  ? 1.54647   -8.11255  -11.71075 1.000 29.48802 ? 47  GLU   A OE2 1 
ATOM   268  N N   . LEU   A 1 41  ? -1.54917  -11.66101 -15.89055 1.000 20.27199 ? 48  LEU   A N   1 
ATOM   269  C CA  . LEU   A 1 41  ? -2.11268  -12.11381 -17.16497 1.000 21.23438 ? 48  LEU   A CA  1 
ATOM   270  C C   . LEU   A 1 41  ? -3.43553  -11.41486 -17.45253 1.000 21.20305 ? 48  LEU   A C   1 
ATOM   271  O O   . LEU   A 1 41  ? -3.70656  -11.04646 -18.61181 1.000 22.52461 ? 48  LEU   A O   1 
ATOM   272  C CB  . LEU   A 1 41  ? -2.33486  -13.61847 -17.14946 1.000 20.76202 ? 48  LEU   A CB  1 
ATOM   273  C CG  . LEU   A 1 41  ? -1.01170  -14.38340 -17.06782 1.000 24.65502 ? 48  LEU   A CG  1 
ATOM   274  C CD1 . LEU   A 1 41  ? -1.33677  -15.90710 -16.89033 1.000 24.67368 ? 48  LEU   A CD1 1 
ATOM   275  C CD2 . LEU   A 1 41  ? -0.10581  -14.11790 -18.27270 1.000 23.31163 ? 48  LEU   A CD2 1 
ATOM   276  N N   . ILE   A 1 42  ? -4.24050  -11.14500 -16.41296 1.000 19.67287 ? 49  ILE   A N   1 
ATOM   277  C CA  . ILE   A 1 42  ? -5.47248  -10.38495 -16.63180 1.000 19.37540 ? 49  ILE   A CA  1 
ATOM   278  C C   . ILE   A 1 42  ? -5.14840  -8.96572  -17.06185 1.000 22.30500 ? 49  ILE   A C   1 
ATOM   279  O O   . ILE   A 1 42  ? -5.82611  -8.38734  -17.93679 1.000 20.80699 ? 49  ILE   A O   1 
ATOM   280  C CB  . ILE   A 1 42  ? -6.34108  -10.44614 -15.37687 1.000 20.79407 ? 49  ILE   A CB  1 
ATOM   281  C CG1 . ILE   A 1 42  ? -6.89150  -11.87941 -15.25478 1.000 21.82931 ? 49  ILE   A CG1 1 
ATOM   282  C CG2 . ILE   A 1 42  ? -7.47959  -9.33100  -15.41918 1.000 21.26329 ? 49  ILE   A CG2 1 
ATOM   283  C CD1 . ILE   A 1 42  ? -7.66996  -12.10769 -13.91657 1.000 23.51003 ? 49  ILE   A CD1 1 
ATOM   284  N N   . SER   A 1 43  ? -4.13178  -8.36080  -16.43465 1.000 20.52981 ? 50  SER   A N   1 
ATOM   285  C CA  . SER   A 1 43  ? -3.75199  -7.02765  -16.83864 1.000 19.96697 ? 50  SER   A CA  1 
ATOM   286  C C   . SER   A 1 43  ? -3.30867  -7.01631  -18.30403 1.000 21.62745 ? 50  SER   A C   1 
ATOM   287  O O   . SER   A 1 43  ? -3.61807  -6.07454  -19.05653 1.000 20.97104 ? 50  SER   A O   1 
ATOM   288  C CB  . SER   A 1 43  ? -2.59752  -6.56036  -15.94113 1.000 26.97577 ? 50  SER   A CB  1 
ATOM   289  O OG  . SER   A 1 43  ? -2.13399  -5.30244  -16.34666 1.000 30.47489 ? 50  SER   A OG  1 
ATOM   290  N N   . ASN   A 1 44  ? -2.52051  -8.02373  -18.70901 1.000 19.95703 ? 51  ASN   A N   1 
ATOM   291  C CA  . ASN   A 1 44  ? -2.10787  -8.08199  -20.11531 1.000 20.75583 ? 51  ASN   A CA  1 
ATOM   292  C C   . ASN   A 1 44  ? -3.33047  -8.19592  -21.03085 1.000 21.40750 ? 51  ASN   A C   1 
ATOM   293  O O   . ASN   A 1 44  ? -3.36228  -7.57841  -22.11553 1.000 22.43017 ? 51  ASN   A O   1 
ATOM   294  C CB  . ASN   A 1 44  ? -1.19299  -9.27806  -20.35856 1.000 21.87761 ? 51  ASN   A CB  1 
ATOM   295  C CG  . ASN   A 1 44  ? 0.17941   -9.04179  -19.87094 1.000 30.48083 ? 51  ASN   A CG  1 
ATOM   296  O OD1 . ASN   A 1 44  ? 0.50579   -7.97837  -19.31602 1.000 29.40474 ? 51  ASN   A OD1 1 
ATOM   297  N ND2 . ASN   A 1 44  ? 1.00554   -10.04327 -20.05363 1.000 30.76716 ? 51  ASN   A ND2 1 
ATOM   298  N N   . SER   A 1 45  ? -4.31870  -9.00268  -20.63046 1.000 18.69191 ? 52  SER   A N   1 
ATOM   299  C CA  . SER   A 1 45  ? -5.53439  -9.12548  -21.45634 1.000 21.44014 ? 52  SER   A CA  1 
ATOM   300  C C   . SER   A 1 45  ? -6.25672  -7.79100  -21.54574 1.000 22.94183 ? 52  SER   A C   1 
ATOM   301  O O   . SER   A 1 45  ? -6.74063  -7.38723  -22.63553 1.000 21.06382 ? 52  SER   A O   1 
ATOM   302  C CB  . SER   A 1 45  ? -6.47073  -10.18744 -20.85222 1.000 20.70196 ? 52  SER   A CB  1 
ATOM   303  O OG  . SER   A 1 45  ? -5.93686  -11.49821 -21.01261 1.000 22.81725 ? 52  SER   A OG  1 
ATOM   304  N N   . SER   A 1 46  ? -6.37616  -7.09658  -20.39737 1.000 21.04127 ? 53  SER   A N   1 
ATOM   305  C CA  . SER   A 1 46  ? -7.04163  -5.79657  -20.42779 1.000 21.34262 ? 53  SER   A CA  1 
ATOM   306  C C   . SER   A 1 46  ? -6.31501  -4.83252  -21.38244 1.000 23.18050 ? 53  SER   A C   1 
ATOM   307  O O   . SER   A 1 46  ? -6.96424  -4.10146  -22.14412 1.000 23.23268 ? 53  SER   A O   1 
ATOM   308  C CB  . SER   A 1 46  ? -7.13583  -5.24623  -18.98493 1.000 20.87985 ? 53  SER   A CB  1 
ATOM   309  O OG  . SER   A 1 46  ? -7.64620  -3.92476  -19.00181 1.000 22.43496 ? 53  SER   A OG  1 
ATOM   310  N N   . ASP   A 1 47  ? -4.96906  -4.81426  -21.37556 1.000 20.42674 ? 54  ASP   A N   1 
ATOM   311  C CA  . ASP   A 1 47  ? -4.20683  -3.99256  -22.30405 1.000 21.57354 ? 54  ASP   A CA  1 
ATOM   312  C C   . ASP   A 1 47  ? -4.48647  -4.34898  -23.76293 1.000 22.73875 ? 54  ASP   A C   1 
ATOM   313  O O   . ASP   A 1 47  ? -4.61224  -3.45621  -24.60937 1.000 22.91439 ? 54  ASP   A O   1 
ATOM   314  C CB  . ASP   A 1 47  ? -2.70035  -4.19027  -22.04114 1.000 20.41130 ? 54  ASP   A CB  1 
ATOM   315  C CG  . ASP   A 1 47  ? -2.21683  -3.42585  -20.77584 1.000 28.62019 ? 54  ASP   A CG  1 
ATOM   316  O OD1 . ASP   A 1 47  ? -3.03564  -2.71660  -20.10738 1.000 30.66456 ? 54  ASP   A OD1 1 
ATOM   317  O OD2 . ASP   A 1 47  ? -1.03299  -3.63485  -20.33192 1.000 28.99148 ? 54  ASP   A OD2 1 
ATOM   318  N N   . ALA   A 1 48  ? -4.62362  -5.64830  -24.06132 1.000 20.23585 ? 55  ALA   A N   1 
ATOM   319  C CA  . ALA   A 1 48  ? -4.86799  -6.09114  -25.44362 1.000 21.04694 ? 55  ALA   A CA  1 
ATOM   320  C C   . ALA   A 1 48  ? -6.27397  -5.70748  -25.88743 1.000 21.06064 ? 55  ALA   A C   1 
ATOM   321  O O   . ALA   A 1 48  ? -6.49701  -5.36971  -27.04703 1.000 20.82617 ? 55  ALA   A O   1 
ATOM   322  C CB  . ALA   A 1 48  ? -4.71991  -7.60996  -25.54184 1.000 22.04972 ? 55  ALA   A CB  1 
ATOM   323  N N   . LEU   A 1 49  ? -7.24000  -5.83725  -24.96964 1.000 21.37128 ? 56  LEU   A N   1 
ATOM   324  C CA  . LEU   A 1 49  ? -8.59452  -5.35311  -25.24526 1.000 21.35107 ? 56  LEU   A CA  1 
ATOM   325  C C   . LEU   A 1 49  ? -8.62886  -3.84831  -25.46625 1.000 21.80499 ? 56  LEU   A C   1 
ATOM   326  O O   . LEU   A 1 49  ? -9.34624  -3.35955  -26.35913 1.000 23.16309 ? 56  LEU   A O   1 
ATOM   327  C CB  . LEU   A 1 49  ? -9.51058  -5.75434  -24.08307 1.000 20.14158 ? 56  LEU   A CB  1 
ATOM   328  C CG  . LEU   A 1 49  ? -9.72761  -7.27299  -24.07444 1.000 20.35889 ? 56  LEU   A CG  1 
ATOM   329  C CD1 . LEU   A 1 49  ? -10.14059 -7.73908  -22.68727 1.000 23.52071 ? 56  LEU   A CD1 1 
ATOM   330  C CD2 . LEU   A 1 49  ? -10.81495 -7.68429  -25.14171 1.000 20.94327 ? 56  LEU   A CD2 1 
ATOM   331  N N   . ASP   A 1 50  ? -7.88563  -3.07484  -24.66205 1.000 21.92865 ? 57  ASP   A N   1 
ATOM   332  C CA  . ASP   A 1 50  ? -7.85682  -1.63134  -24.89749 1.000 21.14912 ? 57  ASP   A CA  1 
ATOM   333  C C   . ASP   A 1 50  ? -7.35019  -1.32516  -26.31238 1.000 22.78658 ? 57  ASP   A C   1 
ATOM   334  O O   . ASP   A 1 50  ? -7.82211  -0.38465  -26.95809 1.000 23.23896 ? 57  ASP   A O   1 
ATOM   335  C CB  . ASP   A 1 50  ? -6.93983  -0.90495  -23.90910 1.000 21.91601 ? 57  ASP   A CB  1 
ATOM   336  C CG  . ASP   A 1 50  ? -7.44351  -0.88583  -22.45548 1.000 30.01001 ? 57  ASP   A CG  1 
ATOM   337  O OD1 . ASP   A 1 50  ? -8.61770  -1.19171  -22.13490 1.000 28.70539 ? 57  ASP   A OD1 1 
ATOM   338  O OD2 . ASP   A 1 50  ? -6.60560  -0.50615  -21.59876 1.000 30.99737 ? 57  ASP   A OD2 1 
ATOM   339  N N   . LYS   A 1 51  ? -6.35405  -2.08845  -26.78953 1.000 21.30221 ? 58  LYS   A N   1 
ATOM   340  C CA  . LYS   A 1 51  ? -5.76124  -1.79416  -28.09829 1.000 22.66706 ? 58  LYS   A CA  1 
ATOM   341  C C   . LYS   A 1 51  ? -6.76182  -2.01134  -29.22419 1.000 22.60416 ? 58  LYS   A C   1 
ATOM   342  O O   . LYS   A 1 51  ? -6.84565  -1.18531  -30.14356 1.000 25.29055 ? 58  LYS   A O   1 
ATOM   343  C CB  . LYS   A 1 51  ? -4.52257  -2.66008  -28.33920 1.000 24.92839 ? 58  LYS   A CB  1 
ATOM   344  C CG  . LYS   A 1 51  ? -3.33577  -2.27350  -27.43899 1.000 26.53592 ? 58  LYS   A CG  1 
ATOM   345  C CD  . LYS   A 1 51  ? -2.16314  -3.25987  -27.71828 1.000 27.46133 ? 58  LYS   A CD  1 
ATOM   346  C CE  . LYS   A 1 51  ? -1.05826  -3.11953  -26.66765 1.000 36.86910 ? 58  LYS   A CE  1 
ATOM   347  N NZ  . LYS   A 1 51  ? 0.10256   -4.04454  -27.04785 1.000 38.75388 ? 58  LYS   A NZ  1 
ATOM   348  N N   . ILE   A 1 52  ? -7.52592  -3.09859  -29.18733 1.000 22.66933 ? 59  ILE   A N   1 
ATOM   349  C CA  . ILE   A 1 52  ? -8.48503  -3.30502  -30.29224 1.000 20.91863 ? 59  ILE   A CA  1 
ATOM   350  C C   . ILE   A 1 52  ? -9.65631  -2.34691  -30.12637 1.000 26.03880 ? 59  ILE   A C   1 
ATOM   351  O O   . ILE   A 1 52  ? -10.20757 -1.84461  -31.13164 1.000 26.34591 ? 59  ILE   A O   1 
ATOM   352  C CB  . ILE   A 1 52  ? -8.94660  -4.77305  -30.40253 1.000 22.56770 ? 59  ILE   A CB  1 
ATOM   353  C CG1 . ILE   A 1 52  ? -9.77176  -5.03544  -31.71017 1.000 25.38613 ? 59  ILE   A CG1 1 
ATOM   354  C CG2 . ILE   A 1 52  ? -9.76824  -5.21192  -29.18046 1.000 24.38485 ? 59  ILE   A CG2 1 
ATOM   355  C CD1 . ILE   A 1 52  ? -8.96697  -4.82962  -32.98225 1.000 30.04151 ? 59  ILE   A CD1 1 
ATOM   356  N N   . ARG   A 1 53  ? -10.01288 -2.00876  -28.89024 1.000 22.41535 ? 60  ARG   A N   1 
ATOM   357  C CA  . ARG   A 1 53  ? -11.06134 -0.99265  -28.74748 1.000 25.43411 ? 60  ARG   A CA  1 
ATOM   358  C C   . ARG   A 1 53  ? -10.62030 0.31348   -29.38652 1.000 24.57574 ? 60  ARG   A C   1 
ATOM   359  O O   . ARG   A 1 53  ? -11.39047 0.93280   -30.14361 1.000 27.73266 ? 60  ARG   A O   1 
ATOM   360  C CB  . ARG   A 1 53  ? -11.47384 -0.76967  -27.29483 1.000 26.78637 ? 60  ARG   A CB  1 
ATOM   361  C CG  . ARG   A 1 53  ? -12.89146 -0.08316  -27.34863 1.000 40.90466 ? 60  ARG   A CG  1 
ATOM   362  C CD  . ARG   A 1 53  ? -13.25697 0.43254   -26.05321 1.000 57.27988 ? 60  ARG   A CD  1 
ATOM   363  N NE  . ARG   A 1 53  ? -14.27769 -0.41233  -25.43797 1.000 58.39221 ? 60  ARG   A NE  1 
ATOM   364  C CZ  . ARG   A 1 53  ? -14.15600 -0.85985  -24.19640 1.000 57.42814 ? 60  ARG   A CZ  1 
ATOM   365  N NH1 . ARG   A 1 53  ? -13.04450 -0.63639  -23.49622 1.000 37.87355 ? 60  ARG   A NH1 1 
ATOM   366  N NH2 . ARG   A 1 53  ? -15.16314 -1.54518  -23.64209 1.000 40.17407 ? 60  ARG   A NH2 1 
ATOM   367  N N   . TYR   A 1 54  ? -9.36944  0.73285   -29.14767 1.000 24.58213 ? 61  TYR   A N   1 
ATOM   368  C CA  . TYR   A 1 54  ? -8.91551  2.00378   -29.69699 1.000 25.11776 ? 61  TYR   A CA  1 
ATOM   369  C C   . TYR   A 1 54  ? -8.91633  1.94041   -31.21137 1.000 29.57241 ? 61  TYR   A C   1 
ATOM   370  O O   . TYR   A 1 54  ? -9.37921  2.87572   -31.87307 1.000 29.22550 ? 61  TYR   A O   1 
ATOM   371  C CB  . TYR   A 1 54  ? -7.50954  2.35759   -29.20663 1.000 26.46341 ? 61  TYR   A CB  1 
ATOM   372  C CG  . TYR   A 1 54  ? -7.08374  3.74134   -29.70929 1.000 29.24477 ? 61  TYR   A CG  1 
ATOM   373  C CD1 . TYR   A 1 54  ? -7.65990  4.89833   -29.19732 1.000 28.05534 ? 61  TYR   A CD1 1 
ATOM   374  C CD2 . TYR   A 1 54  ? -6.18760  3.87232   -30.76146 1.000 26.88497 ? 61  TYR   A CD2 1 
ATOM   375  C CE1 . TYR   A 1 54  ? -7.29657  6.18883   -29.70578 1.000 30.19390 ? 61  TYR   A CE1 1 
ATOM   376  C CE2 . TYR   A 1 54  ? -5.83672  5.11525   -31.27951 1.000 30.84479 ? 61  TYR   A CE2 1 
ATOM   377  C CZ  . TYR   A 1 54  ? -6.37385  6.26798   -30.74815 1.000 36.52377 ? 61  TYR   A CZ  1 
ATOM   378  O OH  . TYR   A 1 54  ? -6.00584  7.51682   -31.25947 1.000 37.76313 ? 61  TYR   A OH  1 
ATOM   379  N N   . GLU   A 1 55  ? -8.46225  0.81502   -31.77857 1.000 27.33088 ? 62  GLU   A N   1 
ATOM   380  C CA  . GLU   A 1 55  ? -8.41174  0.72109   -33.24561 1.000 26.78744 ? 62  GLU   A CA  1 
ATOM   381  C C   . GLU   A 1 55  ? -9.81805  0.75948   -33.82618 1.000 29.17768 ? 62  GLU   A C   1 
ATOM   382  O O   . GLU   A 1 55  ? -10.04448 1.35701   -34.89288 1.000 33.06459 ? 62  GLU   A O   1 
ATOM   383  C CB  . GLU   A 1 55  ? -7.69115  -0.56361  -33.65271 1.000 31.10356 ? 62  GLU   A CB  1 
ATOM   384  C CG  . GLU   A 1 55  ? -6.21649  -0.36430  -33.73667 1.000 36.44380 ? 62  GLU   A CG  1 
ATOM   385  C CD  . GLU   A 1 55  ? -5.47115  -1.56745  -34.32801 1.000 47.58012 ? 62  GLU   A CD  1 
ATOM   386  O OE1 . GLU   A 1 55  ? -4.20954  -1.56527  -34.31152 1.000 51.51630 ? 62  GLU   A OE1 1 
ATOM   387  O OE2 . GLU   A 1 55  ? -6.12898  -2.52641  -34.79432 1.000 48.34992 ? 62  GLU   A OE2 1 
ATOM   388  N N   . SER   A 1 56  ? -10.79036 0.20790   -33.10465 1.000 27.38445 ? 63  SER   A N   1 
ATOM   389  C CA  . SER   A 1 56  ? -12.16462 0.19322   -33.61162 1.000 28.59965 ? 63  SER   A CA  1 
ATOM   390  C C   . SER   A 1 56  ? -12.81405 1.56569   -33.58091 1.000 33.27634 ? 63  SER   A C   1 
ATOM   391  O O   . SER   A 1 56  ? -13.86811 1.75696   -34.21314 1.000 33.17952 ? 63  SER   A O   1 
ATOM   392  C CB  . SER   A 1 56  ? -13.03031 -0.78189  -32.80988 1.000 26.84663 ? 63  SER   A CB  1 
ATOM   393  O OG  . SER   A 1 56  ? -13.43755 -0.22381  -31.52470 1.000 30.86455 ? 63  SER   A OG  1 
ATOM   394  N N   . LEU   A 1 57  ? -12.21150 2.54205   -32.90465 1.000 28.87546 ? 64  LEU   A N   1 
ATOM   395  C CA  . LEU   A 1 57  ? -12.88028 3.83718   -32.80618 1.000 33.81421 ? 64  LEU   A CA  1 
ATOM   396  C C   . LEU   A 1 57  ? -12.87976 4.55806   -34.13176 1.000 37.80801 ? 64  LEU   A C   1 
ATOM   397  O O   . LEU   A 1 57  ? -13.80258 5.31863   -34.42401 1.000 40.60692 ? 64  LEU   A O   1 
ATOM   398  C CB  . LEU   A 1 57  ? -12.19480 4.69519   -31.75750 1.000 31.93868 ? 64  LEU   A CB  1 
ATOM   399  C CG  . LEU   A 1 57  ? -12.40880 4.16423   -30.34487 1.000 31.11525 ? 64  LEU   A CG  1 
ATOM   400  C CD1 . LEU   A 1 57  ? -11.79857 5.20501   -29.42626 1.000 30.29860 ? 64  LEU   A CD1 1 
ATOM   401  C CD2 . LEU   A 1 57  ? -13.85175 3.91565   -29.96090 1.000 32.29605 ? 64  LEU   A CD2 1 
ATOM   402  N N   . THR   A 1 58  ? -11.87624 4.33128   -34.94689 1.000 39.87851 ? 65  THR   A N   1 
ATOM   403  C CA  . THR   A 1 58  ? -11.81317 4.94057   -36.26024 1.000 41.65315 ? 65  THR   A CA  1 
ATOM   404  C C   . THR   A 1 58  ? -12.02795 3.94805   -37.39537 1.000 44.40731 ? 65  THR   A C   1 
ATOM   405  O O   . THR   A 1 58  ? -12.15925 4.37288   -38.53675 1.000 47.64862 ? 65  THR   A O   1 
ATOM   406  C CB  . THR   A 1 58  ? -10.46249 5.64461   -36.43473 1.000 49.72384 ? 65  THR   A CB  1 
ATOM   407  O OG1 . THR   A 1 58  ? -9.41464  4.67295   -36.29174 1.000 49.06666 ? 65  THR   A OG1 1 
ATOM   408  C CG2 . THR   A 1 58  ? -10.29112 6.75585   -35.39987 1.000 43.35501 ? 65  THR   A CG2 1 
ATOM   409  N N   . ASP   A 1 59  ? -12.08798 2.65092   -37.11230 1.000 45.70350 ? 66  ASP   A N   1 
ATOM   410  C CA  . ASP   A 1 59  ? -12.29843 1.62260   -38.12789 1.000 39.15413 ? 66  ASP   A CA  1 
ATOM   411  C C   . ASP   A 1 59  ? -13.16148 0.51726   -37.53098 1.000 39.20005 ? 66  ASP   A C   1 
ATOM   412  O O   . ASP   A 1 59  ? -12.64989 -0.44325  -36.94730 1.000 38.91272 ? 66  ASP   A O   1 
ATOM   413  C CB  . ASP   A 1 59  ? -10.96832 1.05631   -38.60756 1.000 41.31194 ? 66  ASP   A CB  1 
ATOM   414  C CG  . ASP   A 1 59  ? -11.13885 0.11196   -39.78118 1.000 47.70021 ? 66  ASP   A CG  1 
ATOM   415  O OD1 . ASP   A 1 59  ? -12.31018 -0.17189  -40.14350 1.000 50.05434 ? 66  ASP   A OD1 1 
ATOM   416  O OD2 . ASP   A 1 59  ? -10.11301 -0.35732  -40.32615 1.000 48.70953 ? 66  ASP   A OD2 1 
ATOM   417  N N   . PRO   A 1 60  ? -14.48653 0.62748   -37.64496 1.000 41.56236 ? 67  PRO   A N   1 
ATOM   418  C CA  . PRO   A 1 60  ? -15.34063 -0.37148  -36.98593 1.000 36.37624 ? 67  PRO   A CA  1 
ATOM   419  C C   . PRO   A 1 60  ? -15.13319 -1.76368  -37.53274 1.000 38.86863 ? 67  PRO   A C   1 
ATOM   420  O O   . PRO   A 1 60  ? -15.43125 -2.73185  -36.82602 1.000 38.19305 ? 67  PRO   A O   1 
ATOM   421  C CB  . PRO   A 1 60  ? -16.76330 0.10866   -37.30224 1.000 43.66126 ? 67  PRO   A CB  1 
ATOM   422  C CG  . PRO   A 1 60  ? -16.63981 1.50284   -37.65199 1.000 50.78603 ? 67  PRO   A CG  1 
ATOM   423  C CD  . PRO   A 1 60  ? -15.23389 1.81808   -38.05643 1.000 42.56123 ? 67  PRO   A CD  1 
ATOM   424  N N   . SER   A 1 61  ? -14.67114 -1.90379  -38.78766 1.000 39.11967 ? 68  SER   A N   1 
ATOM   425  C CA  . SER   A 1 61  ? -14.48811 -3.24149  -39.32285 1.000 41.02485 ? 68  SER   A CA  1 
ATOM   426  C C   . SER   A 1 61  ? -13.42435 -4.03193  -38.56443 1.000 39.10397 ? 68  SER   A C   1 
ATOM   427  O O   . SER   A 1 61  ? -13.34111 -5.25316  -38.71866 1.000 36.76437 ? 68  SER   A O   1 
ATOM   428  C CB  . SER   A 1 61  ? -14.11830 -3.16423  -40.80391 1.000 39.13539 ? 68  SER   A CB  1 
ATOM   429  O OG  . SER   A 1 61  ? -12.80619 -2.64416  -40.96921 1.000 42.27762 ? 68  SER   A OG  1 
ATOM   430  N N   . LYS   A 1 62  ? -12.62962 -3.39092  -37.69909 1.000 34.14153 ? 69  LYS   A N   1 
ATOM   431  C CA  . LYS   A 1 62  ? -11.68324 -4.16752  -36.92310 1.000 31.56456 ? 69  LYS   A CA  1 
ATOM   432  C C   . LYS   A 1 62  ? -12.36121 -5.12158  -35.96243 1.000 32.37002 ? 69  LYS   A C   1 
ATOM   433  O O   . LYS   A 1 62  ? -11.70285 -6.02481  -35.45523 1.000 33.68539 ? 69  LYS   A O   1 
ATOM   434  C CB  . LYS   A 1 62  ? -10.77416 -3.24328  -36.14814 1.000 35.79753 ? 69  LYS   A CB  1 
ATOM   435  C CG  . LYS   A 1 62  ? -9.99120  -2.34686  -37.06855 1.000 42.14867 ? 69  LYS   A CG  1 
ATOM   436  C CD  . LYS   A 1 62  ? -8.51053  -2.47733  -36.86734 1.000 37.91597 ? 69  LYS   A CD  1 
ATOM   437  C CE  . LYS   A 1 62  ? -7.74685  -1.77093  -37.93419 1.000 39.13854 ? 69  LYS   A CE  1 
ATOM   438  N NZ  . LYS   A 1 62  ? -6.37062  -2.32616  -37.84801 1.000 40.03028 ? 69  LYS   A NZ  1 
ATOM   439  N N   . LEU   A 1 63  ? -13.66066 -4.92929  -35.67789 1.000 32.56689 ? 70  LEU   A N   1 
ATOM   440  C CA  . LEU   A 1 63  ? -14.40102 -5.82858  -34.81417 1.000 34.01054 ? 70  LEU   A CA  1 
ATOM   441  C C   . LEU   A 1 63  ? -15.20657 -6.83905  -35.60028 1.000 33.27908 ? 70  LEU   A C   1 
ATOM   442  O O   . LEU   A 1 63  ? -16.00393 -7.57067  -35.00210 1.000 36.10435 ? 70  LEU   A O   1 
ATOM   443  C CB  . LEU   A 1 63  ? -15.30061 -5.03143  -33.86222 1.000 31.59459 ? 70  LEU   A CB  1 
ATOM   444  C CG  . LEU   A 1 63  ? -14.49681 -4.13140  -32.90520 1.000 30.78227 ? 70  LEU   A CG  1 
ATOM   445  C CD1 . LEU   A 1 63  ? -15.51076 -3.44811  -31.97405 1.000 32.41990 ? 70  LEU   A CD1 1 
ATOM   446  C CD2 . LEU   A 1 63  ? -13.52457 -4.97826  -32.05887 1.000 29.22211 ? 70  LEU   A CD2 1 
ATOM   447  N N   . ASP   A 1 64  ? -14.97284 -6.93963  -36.91253 1.000 32.81604 ? 71  ASP   A N   1 
ATOM   448  C CA  . ASP   A 1 64  ? -15.68015 -7.95084  -37.70833 1.000 38.32973 ? 71  ASP   A CA  1 
ATOM   449  C C   . ASP   A 1 64  ? -15.31692 -9.35597  -37.25482 1.000 41.02463 ? 71  ASP   A C   1 
ATOM   450  O O   . ASP   A 1 64  ? -16.12587 -10.27866 -37.39857 1.000 41.01017 ? 71  ASP   A O   1 
ATOM   451  C CB  . ASP   A 1 64  ? -15.38030 -7.80006  -39.20201 1.000 37.99984 ? 71  ASP   A CB  1 
ATOM   452  C CG  . ASP   A 1 64  ? -16.04312 -6.57301  -39.82425 1.000 47.50396 ? 71  ASP   A CG  1 
ATOM   453  O OD1 . ASP   A 1 64  ? -16.94067 -5.99368  -39.17425 1.000 50.36360 ? 71  ASP   A OD1 1 
ATOM   454  O OD2 . ASP   A 1 64  ? -15.70083 -6.22580  -40.98942 1.000 51.06533 ? 71  ASP   A OD2 1 
ATOM   455  N N   . SER   A 1 65  ? -14.11337 -9.52166  -36.69756 1.000 34.23368 ? 72  SER   A N   1 
ATOM   456  C CA  . SER   A 1 65  ? -13.61157 -10.75596 -36.10595 1.000 33.93185 ? 72  SER   A CA  1 
ATOM   457  C C   . SER   A 1 65  ? -14.19576 -11.02761 -34.71102 1.000 40.11413 ? 72  SER   A C   1 
ATOM   458  O O   . SER   A 1 65  ? -13.77408 -11.98561 -34.04607 1.000 36.81021 ? 72  SER   A O   1 
ATOM   459  C CB  . SER   A 1 65  ? -12.07978 -10.69279 -36.03872 1.000 33.46736 ? 72  SER   A CB  1 
ATOM   460  O OG  . SER   A 1 65  ? -11.65907 -9.40594  -35.53939 1.000 32.29944 ? 72  SER   A OG  1 
ATOM   461  N N   . GLY   A 1 66  ? -15.12652 -10.18232 -34.22586 1.000 36.07195 ? 73  GLY   A N   1 
ATOM   462  C CA  . GLY   A 1 66  ? -15.75769 -10.39800 -32.93925 1.000 34.68529 ? 73  GLY   A CA  1 
ATOM   463  C C   . GLY   A 1 66  ? -15.99567 -9.08804  -32.19713 1.000 34.07620 ? 73  GLY   A C   1 
ATOM   464  O O   . GLY   A 1 66  ? -15.04423 -8.34966  -31.90856 1.000 30.88718 ? 73  GLY   A O   1 
ATOM   465  N N   . LYS   A 1 67  ? -17.25184 -8.76061  -31.90444 1.000 33.15551 ? 74  LYS   A N   1 
ATOM   466  C CA  . LYS   A 1 67  ? -17.53698 -7.48794  -31.25552 1.000 31.35589 ? 74  LYS   A CA  1 
ATOM   467  C C   . LYS   A 1 67  ? -17.40748 -7.50854  -29.74829 1.000 31.97389 ? 74  LYS   A C   1 
ATOM   468  O O   . LYS   A 1 67  ? -17.31258 -6.43795  -29.15139 1.000 34.15062 ? 74  LYS   A O   1 
ATOM   469  C CB  . LYS   A 1 67  ? -18.96691 -7.03470  -31.58835 1.000 31.24968 ? 74  LYS   A CB  1 
ATOM   470  C CG  . LYS   A 1 67  ? -19.02891 -6.26995  -32.91346 1.000 51.22716 ? 74  LYS   A CG  1 
ATOM   471  C CD  . LYS   A 1 67  ? -20.43575 -6.28621  -33.49369 1.000 66.39082 ? 74  LYS   A CD  1 
ATOM   472  C CE  . LYS   A 1 67  ? -20.41562 -6.40639  -35.01456 1.000 69.91175 ? 74  LYS   A CE  1 
ATOM   473  N NZ  . LYS   A 1 67  ? -20.97986 -7.72079  -35.47343 1.000 79.51123 ? 74  LYS   A NZ  1 
ATOM   474  N N   . GLU   A 1 68  ? -17.43402 -8.67025  -29.11336 1.000 30.98656 ? 75  GLU   A N   1 
ATOM   475  C CA  . GLU   A 1 68  ? -17.46554 -8.72207  -27.65900 1.000 28.31830 ? 75  GLU   A CA  1 
ATOM   476  C C   . GLU   A 1 68  ? -16.05687 -8.64013  -27.12786 1.000 27.33708 ? 75  GLU   A C   1 
ATOM   477  O O   . GLU   A 1 68  ? -15.18117 -9.34655  -27.61661 1.000 30.27463 ? 75  GLU   A O   1 
ATOM   478  C CB  . GLU   A 1 68  ? -18.08570 -10.02356 -27.15680 1.000 36.49466 ? 75  GLU   A CB  1 
ATOM   479  C CG  . GLU   A 1 68  ? -19.59886 -10.11821 -27.30432 1.000 42.00274 ? 75  GLU   A CG  1 
ATOM   480  C CD  . GLU   A 1 68  ? -20.06759 -10.26201 -28.73349 1.000 74.01053 ? 75  GLU   A CD  1 
ATOM   481  O OE1 . GLU   A 1 68  ? -21.01939 -9.54659  -29.13961 1.000 87.03772 ? 75  GLU   A OE1 1 
ATOM   482  O OE2 . GLU   A 1 68  ? -19.46823 -11.08710 -29.45398 1.000 75.35456 ? 75  GLU   A OE2 1 
ATOM   483  N N   . LEU   A 1 69  ? -15.86410 -7.80282  -26.13161 1.000 25.81725 ? 76  LEU   A N   1 
ATOM   484  C CA  . LEU   A 1 69  ? -14.55872 -7.56990  -25.51184 1.000 23.77443 ? 76  LEU   A CA  1 
ATOM   485  C C   . LEU   A 1 69  ? -14.62529 -8.08629  -24.08227 1.000 22.69646 ? 76  LEU   A C   1 
ATOM   486  O O   . LEU   A 1 69  ? -15.28705 -7.46662  -23.21036 1.000 24.49287 ? 76  LEU   A O   1 
ATOM   487  C CB  . LEU   A 1 69  ? -14.24534 -6.07729  -25.55431 1.000 26.34452 ? 76  LEU   A CB  1 
ATOM   488  C CG  . LEU   A 1 69  ? -14.19555 -5.46679  -26.97364 1.000 31.78158 ? 76  LEU   A CG  1 
ATOM   489  C CD1 . LEU   A 1 69  ? -13.81695 -4.01789  -26.88023 1.000 37.45470 ? 76  LEU   A CD1 1 
ATOM   490  C CD2 . LEU   A 1 69  ? -13.14523 -6.21489  -27.80407 1.000 31.08329 ? 76  LEU   A CD2 1 
ATOM   491  N N   . HIS   A 1 70  ? -13.95924 -9.21952  -23.81860 1.000 24.07588 ? 77  HIS   A N   1 
ATOM   492  C CA  . HIS   A 1 70  ? -14.12379 -9.89415  -22.53145 1.000 22.69261 ? 77  HIS   A CA  1 
ATOM   493  C C   . HIS   A 1 70  ? -12.94147 -10.78901 -22.23730 1.000 22.46001 ? 77  HIS   A C   1 
ATOM   494  O O   . HIS   A 1 70  ? -12.05900 -10.99868 -23.08298 1.000 21.63145 ? 77  HIS   A O   1 
ATOM   495  C CB  . HIS   A 1 70  ? -15.41814 -10.73928 -22.47538 1.000 24.33386 ? 77  HIS   A CB  1 
ATOM   496  C CG  . HIS   A 1 70  ? -15.44608 -11.84971 -23.48347 1.000 24.49536 ? 77  HIS   A CG  1 
ATOM   497  N ND1 . HIS   A 1 70  ? -16.41700 -11.94173 -24.45298 1.000 36.16903 ? 77  HIS   A ND1 1 
ATOM   498  C CD2 . HIS   A 1 70  ? -14.61310 -12.89614 -23.68655 1.000 27.67893 ? 77  HIS   A CD2 1 
ATOM   499  C CE1 . HIS   A 1 70  ? -16.19145 -13.00187 -25.20245 1.000 30.19980 ? 77  HIS   A CE1 1 
ATOM   500  N NE2 . HIS   A 1 70  ? -15.10361 -13.59538 -24.77421 1.000 29.75924 ? 77  HIS   A NE2 1 
ATOM   501  N N   . ILE   A 1 71  ? -12.92229 -11.25770 -20.98447 1.000 19.93268 ? 78  ILE   A N   1 
ATOM   502  C CA  . ILE   A 1 71  ? -11.89979 -12.16197 -20.45609 1.000 20.75466 ? 78  ILE   A CA  1 
ATOM   503  C C   . ILE   A 1 71  ? -12.60242 -13.36734 -19.82439 1.000 24.25378 ? 78  ILE   A C   1 
ATOM   504  O O   . ILE   A 1 71  ? -13.50060 -13.20385 -18.98581 1.000 23.40742 ? 78  ILE   A O   1 
ATOM   505  C CB  . ILE   A 1 71  ? -11.04792 -11.43257 -19.39705 1.000 21.40550 ? 78  ILE   A CB  1 
ATOM   506  C CG1 . ILE   A 1 71  ? -10.36484 -10.20801 -20.03482 1.000 22.88821 ? 78  ILE   A CG1 1 
ATOM   507  C CG2 . ILE   A 1 71  ? -10.04673 -12.46363 -18.82470 1.000 22.79185 ? 78  ILE   A CG2 1 
ATOM   508  C CD1 . ILE   A 1 71  ? -9.65618  -9.27461  -18.92527 1.000 24.04028 ? 78  ILE   A CD1 1 
ATOM   509  N N   . ASN   A 1 72  ? -12.20171 -14.58543 -20.21958 1.000 21.92686 ? 79  ASN   A N   1 
ATOM   510  C CA  . ASN   A 1 72  ? -12.74880 -15.80617 -19.62822 1.000 21.84829 ? 79  ASN   A CA  1 
ATOM   511  C C   . ASN   A 1 72  ? -11.62675 -16.54197 -18.90306 1.000 23.45856 ? 79  ASN   A C   1 
ATOM   512  O O   . ASN   A 1 72  ? -10.50013 -16.63148 -19.40672 1.000 21.94788 ? 79  ASN   A O   1 
ATOM   513  C CB  . ASN   A 1 72  ? -13.36888 -16.72918 -20.71157 1.000 22.57953 ? 79  ASN   A CB  1 
ATOM   514  C CG  . ASN   A 1 72  ? -14.58414 -16.13427 -21.35885 1.000 24.02459 ? 79  ASN   A CG  1 
ATOM   515  O OD1 . ASN   A 1 72  ? -15.30579 -15.30866 -20.76070 1.000 25.93046 ? 79  ASN   A OD1 1 
ATOM   516  N ND2 . ASN   A 1 72  ? -14.84599 -16.54488 -22.59375 1.000 26.19365 ? 79  ASN   A ND2 1 
ATOM   517  N N   . LEU   A 1 73  ? -11.93561 -17.09741 -17.73372 1.000 22.29704 ? 80  LEU   A N   1 
ATOM   518  C CA  . LEU   A 1 73  ? -11.01056 -17.92243 -16.95515 1.000 20.27009 ? 80  LEU   A CA  1 
ATOM   519  C C   . LEU   A 1 73  ? -11.56411 -19.33607 -16.93690 1.000 21.94148 ? 80  LEU   A C   1 
ATOM   520  O O   . LEU   A 1 73  ? -12.69891 -19.56854 -16.46946 1.000 22.61427 ? 80  LEU   A O   1 
ATOM   521  C CB  . LEU   A 1 73  ? -10.84421 -17.39920 -15.53265 1.000 20.30606 ? 80  LEU   A CB  1 
ATOM   522  C CG  . LEU   A 1 73  ? -10.45539 -15.91842 -15.41563 1.000 21.04326 ? 80  LEU   A CG  1 
ATOM   523  C CD1 . LEU   A 1 73  ? -10.42135 -15.52985 -13.93817 1.000 21.13539 ? 80  LEU   A CD1 1 
ATOM   524  C CD2 . LEU   A 1 73  ? -9.10226  -15.59622 -16.09533 1.000 22.43974 ? 80  LEU   A CD2 1 
ATOM   525  N N   . ILE   A 1 74  ? -10.82110 -20.28138 -17.51447 1.000 21.13811 ? 81  ILE   A N   1 
ATOM   526  C CA  . ILE   A 1 74  ? -11.34827 -21.62244 -17.71506 1.000 23.41236 ? 81  ILE   A CA  1 
ATOM   527  C C   . ILE   A 1 74  ? -10.41935 -22.62813 -17.04345 1.000 25.26523 ? 81  ILE   A C   1 
ATOM   528  O O   . ILE   A 1 74  ? -9.40108  -23.01994 -17.60807 1.000 23.32199 ? 81  ILE   A O   1 
ATOM   529  C CB  . ILE   A 1 74  ? -11.49221 -21.95311 -19.21559 1.000 21.67164 ? 81  ILE   A CB  1 
ATOM   530  C CG1 . ILE   A 1 74  ? -12.24282 -20.80822 -19.92613 1.000 24.05723 ? 81  ILE   A CG1 1 
ATOM   531  C CG2 . ILE   A 1 74  ? -12.14269 -23.28584 -19.36769 1.000 23.55866 ? 81  ILE   A CG2 1 
ATOM   532  C CD1 . ILE   A 1 74  ? -12.41787 -21.00405 -21.45191 1.000 27.18558 ? 81  ILE   A CD1 1 
ATOM   533  N N   . PRO   A 1 75  ? -10.75398 -23.07730 -15.83866 1.000 24.16723 ? 82  PRO   A N   1 
ATOM   534  C CA  . PRO   A 1 75  ? -10.02700 -24.19702 -15.22579 1.000 24.63025 ? 82  PRO   A CA  1 
ATOM   535  C C   . PRO   A 1 75  ? -10.46589 -25.55042 -15.76175 1.000 27.05562 ? 82  PRO   A C   1 
ATOM   536  O O   . PRO   A 1 75  ? -11.64185 -25.79337 -16.04314 1.000 29.92539 ? 82  PRO   A O   1 
ATOM   537  C CB  . PRO   A 1 75  ? -10.38395 -24.05708 -13.73785 1.000 23.92390 ? 82  PRO   A CB  1 
ATOM   538  C CG  . PRO   A 1 75  ? -11.76808 -23.49129 -13.75033 1.000 29.94601 ? 82  PRO   A CG  1 
ATOM   539  C CD  . PRO   A 1 75  ? -11.91751 -22.65256 -15.03965 1.000 26.81154 ? 82  PRO   A CD  1 
ATOM   540  N N   . ASN   A 1 76  ? -9.49922  -26.46028 -15.86530 1.000 25.67650 ? 83  ASN   A N   1 
ATOM   541  C CA  . ASN   A 1 76  ? -9.78340  -27.81913 -16.28787 1.000 25.65271 ? 83  ASN   A CA  1 
ATOM   542  C C   . ASN   A 1 76  ? -8.96181  -28.72570 -15.40140 1.000 31.52759 ? 83  ASN   A C   1 
ATOM   543  O O   . ASN   A 1 76  ? -7.74931  -28.82526 -15.56649 1.000 30.49282 ? 83  ASN   A O   1 
ATOM   544  C CB  . ASN   A 1 76  ? -9.47363  -28.02666 -17.76938 1.000 27.94654 ? 83  ASN   A CB  1 
ATOM   545  C CG  . ASN   A 1 76  ? -9.94956  -29.37183 -18.26087 1.000 37.06743 ? 83  ASN   A CG  1 
ATOM   546  O OD1 . ASN   A 1 76  ? -9.67847  -30.40252 -17.63597 1.000 36.26901 ? 83  ASN   A OD1 1 
ATOM   547  N ND2 . ASN   A 1 76  ? -10.74058 -29.37170 -19.33363 1.000 44.46139 ? 83  ASN   A ND2 1 
ATOM   548  N N   . LYS   A 1 77  ? -9.61423  -29.37835 -14.45509 1.000 30.63824 ? 84  LYS   A N   1 
ATOM   549  C CA  . LYS   A 1 77  ? -8.87977  -30.21712 -13.51756 1.000 33.57154 ? 84  LYS   A CA  1 
ATOM   550  C C   . LYS   A 1 77  ? -8.42090  -31.51925 -14.14821 1.000 36.09112 ? 84  LYS   A C   1 
ATOM   551  O O   . LYS   A 1 77  ? -7.44995  -32.09538 -13.67687 1.000 37.54951 ? 84  LYS   A O   1 
ATOM   552  C CB  . LYS   A 1 77  ? -9.72721  -30.54370 -12.28879 1.000 33.70584 ? 84  LYS   A CB  1 
ATOM   553  C CG  . LYS   A 1 77  ? -9.98631  -29.30977 -11.41455 1.000 35.80034 ? 84  LYS   A CG  1 
ATOM   554  C CD  . LYS   A 1 77  ? -10.63330 -29.76503 -10.09621 1.000 36.17213 ? 84  LYS   A CD  1 
ATOM   555  C CE  . LYS   A 1 77  ? -11.01464 -28.63660 -9.14379  1.000 41.85287 ? 84  LYS   A CE  1 
ATOM   556  N NZ  . LYS   A 1 77  ? -11.96617 -27.70314 -9.82381  1.000 53.17567 ? 84  LYS   A NZ  1 
ATOM   557  N N   . GLN   A 1 78  ? -9.10794  -32.00894 -15.19077 1.000 40.42569 ? 85  GLN   A N   1 
ATOM   558  C CA  . GLN   A 1 78  ? -8.69369  -33.26211 -15.80844 1.000 42.55285 ? 85  GLN   A CA  1 
ATOM   559  C C   . GLN   A 1 78  ? -7.39945  -33.08164 -16.58118 1.000 44.22147 ? 85  GLN   A C   1 
ATOM   560  O O   . GLN   A 1 78  ? -6.50914  -33.93586 -16.49987 1.000 44.18335 ? 85  GLN   A O   1 
ATOM   561  C CB  . GLN   A 1 78  ? -9.79792  -33.81647 -16.70336 1.000 39.08588 ? 85  GLN   A CB  1 
ATOM   562  C CG  . GLN   A 1 78  ? -10.98863 -34.39393 -15.92889 1.000 60.01851 ? 85  GLN   A CG  1 
ATOM   563  C CD  . GLN   A 1 78  ? -11.74481 -33.36927 -15.07104 1.000 74.58292 ? 85  GLN   A CD  1 
ATOM   564  O OE1 . GLN   A 1 78  ? -12.21246 -33.70051 -13.97188 1.000 70.82712 ? 85  GLN   A OE1 1 
ATOM   565  N NE2 . GLN   A 1 78  ? -11.91494 -32.14043 -15.59174 1.000 58.81373 ? 85  GLN   A NE2 1 
ATOM   566  N N   . ASP   A 1 79  ? -7.25485  -31.94592 -17.27449 1.000 36.41813 ? 86  ASP   A N   1 
ATOM   567  C CA  . ASP   A 1 79  ? -6.04525  -31.61210 -18.02397 1.000 35.27529 ? 86  ASP   A CA  1 
ATOM   568  C C   . ASP   A 1 79  ? -5.01514  -30.90271 -17.15165 1.000 33.49518 ? 86  ASP   A C   1 
ATOM   569  O O   . ASP   A 1 79  ? -3.86435  -30.76133 -17.57374 1.000 35.11082 ? 86  ASP   A O   1 
ATOM   570  C CB  . ASP   A 1 79  ? -6.37286  -30.70989 -19.22265 1.000 41.29926 ? 86  ASP   A CB  1 
ATOM   571  C CG  . ASP   A 1 79  ? -7.30068  -31.39068 -20.22492 1.000 50.79977 ? 86  ASP   A CG  1 
ATOM   572  O OD1 . ASP   A 1 79  ? -7.34868  -32.64323 -20.25812 1.000 52.26642 ? 86  ASP   A OD1 1 
ATOM   573  O OD2 . ASP   A 1 79  ? -7.97252  -30.66381 -20.98430 1.000 47.75718 ? 86  ASP   A OD2 1 
ATOM   574  N N   . ARG   A 1 80  ? -5.40628  -30.51362 -15.94150 1.000 31.55002 ? 87  ARG   A N   1 
ATOM   575  C CA  . ARG   A 1 80  ? -4.60860  -29.67164 -15.03068 1.000 26.34832 ? 87  ARG   A CA  1 
ATOM   576  C C   . ARG   A 1 80  ? -4.12563  -28.40067 -15.72755 1.000 27.85067 ? 87  ARG   A C   1 
ATOM   577  O O   . ARG   A 1 80  ? -2.93534  -28.05007 -15.70181 1.000 30.06542 ? 87  ARG   A O   1 
ATOM   578  C CB  . ARG   A 1 80  ? -3.45655  -30.47259 -14.42626 1.000 32.03781 ? 87  ARG   A CB  1 
ATOM   579  C CG  . ARG   A 1 80  ? -2.95177  -29.87816 -13.15484 1.000 30.88043 ? 87  ARG   A CG  1 
ATOM   580  C CD  . ARG   A 1 80  ? -2.03464  -30.81443 -12.40964 1.000 42.58052 ? 87  ARG   A CD  1 
ATOM   581  N NE  . ARG   A 1 80  ? -0.66807  -30.77192 -12.87182 1.000 48.64503 ? 87  ARG   A NE  1 
ATOM   582  C CZ  . ARG   A 1 80  ? 0.18191   -31.78179 -12.79761 1.000 50.22617 ? 87  ARG   A CZ  1 
ATOM   583  N NH1 . ARG   A 1 80  ? -0.17483  -32.95056 -12.28287 1.000 52.33089 ? 87  ARG   A NH1 1 
ATOM   584  N NH2 . ARG   A 1 80  ? 1.44042   -31.58723 -13.17479 1.000 47.86640 ? 87  ARG   A NH2 1 
ATOM   585  N N   . THR   A 1 81  ? -5.07180  -27.65476 -16.31882 1.000 26.65222 ? 88  THR   A N   1 
ATOM   586  C CA  . THR   A 1 81  ? -4.77198  -26.42272 -17.01775 1.000 25.67149 ? 88  THR   A CA  1 
ATOM   587  C C   . THR   A 1 81  ? -5.68621  -25.31038 -16.54688 1.000 25.11719 ? 88  THR   A C   1 
ATOM   588  O O   . THR   A 1 81  ? -6.85522  -25.53950 -16.27938 1.000 26.19942 ? 88  THR   A O   1 
ATOM   589  C CB  . THR   A 1 81  ? -4.91354  -26.53133 -18.54583 1.000 27.00170 ? 88  THR   A CB  1 
ATOM   590  O OG1 . THR   A 1 81  ? -6.25512  -26.95690 -18.88039 1.000 27.91064 ? 88  THR   A OG1 1 
ATOM   591  C CG2 . THR   A 1 81  ? -3.83864  -27.45511 -19.18467 1.000 27.46493 ? 88  THR   A CG2 1 
ATOM   592  N N   . LEU   A 1 82  ? -5.14817  -24.10166 -16.46830 1.000 21.39806 ? 89  LEU   A N   1 
ATOM   593  C CA  . LEU   A 1 82  ? -5.93495  -22.87690 -16.29728 1.000 23.43038 ? 89  LEU   A CA  1 
ATOM   594  C C   . LEU   A 1 82  ? -5.73199  -22.04094 -17.56268 1.000 26.15105 ? 89  LEU   A C   1 
ATOM   595  O O   . LEU   A 1 82  ? -4.58821  -21.74371 -17.93583 1.000 24.89086 ? 89  LEU   A O   1 
ATOM   596  C CB  . LEU   A 1 82  ? -5.47182  -22.10228 -15.06213 1.000 23.40959 ? 89  LEU   A CB  1 
ATOM   597  C CG  . LEU   A 1 82  ? -6.20792  -20.75656 -14.86850 1.000 22.19748 ? 89  LEU   A CG  1 
ATOM   598  C CD1 . LEU   A 1 82  ? -7.72001  -21.00370 -14.66561 1.000 24.66508 ? 89  LEU   A CD1 1 
ATOM   599  C CD2 . LEU   A 1 82  ? -5.64332  -20.12171 -13.64168 1.000 25.38227 ? 89  LEU   A CD2 1 
ATOM   600  N N   . THR   A 1 83  ? -6.80604  -21.71442 -18.24734 1.000 23.59212 ? 90  THR   A N   1 
ATOM   601  C CA  . THR   A 1 83  ? -6.72493  -20.98953 -19.50248 1.000 23.02085 ? 90  THR   A CA  1 
ATOM   602  C C   . THR   A 1 83  ? -7.28812  -19.60089 -19.28261 1.000 24.42920 ? 90  THR   A C   1 
ATOM   603  O O   . THR   A 1 83  ? -8.37495  -19.45688 -18.70851 1.000 25.40617 ? 90  THR   A O   1 
ATOM   604  C CB  . THR   A 1 83  ? -7.47921  -21.72421 -20.61647 1.000 23.82051 ? 90  THR   A CB  1 
ATOM   605  O OG1 . THR   A 1 83  ? -6.91561  -23.03362 -20.83263 1.000 27.33586 ? 90  THR   A OG1 1 
ATOM   606  C CG2 . THR   A 1 83  ? -7.39897  -20.93773 -21.88904 1.000 26.51725 ? 90  THR   A CG2 1 
ATOM   607  N N   . ILE   A 1 84  ? -6.56980  -18.57684 -19.73706 1.000 21.80694 ? 91  ILE   A N   1 
ATOM   608  C CA  . ILE   A 1 84  ? -7.03453  -17.18704 -19.69267 1.000 22.34328 ? 91  ILE   A CA  1 
ATOM   609  C C   . ILE   A 1 84  ? -7.27757  -16.76925 -21.13805 1.000 26.14659 ? 91  ILE   A C   1 
ATOM   610  O O   . ILE   A 1 84  ? -6.32586  -16.68344 -21.93949 1.000 24.95245 ? 91  ILE   A O   1 
ATOM   611  C CB  . ILE   A 1 84  ? -6.02850  -16.26194 -18.98493 1.000 23.37185 ? 91  ILE   A CB  1 
ATOM   612  C CG1 . ILE   A 1 84  ? -5.78483  -16.69659 -17.51707 1.000 27.70099 ? 91  ILE   A CG1 1 
ATOM   613  C CG2 . ILE   A 1 84  ? -6.53722  -14.83148 -18.96578 1.000 26.84360 ? 91  ILE   A CG2 1 
ATOM   614  C CD1 . ILE   A 1 84  ? -4.53369  -17.54200 -17.28704 1.000 30.51519 ? 91  ILE   A CD1 1 
ATOM   615  N N   . VAL   A 1 85  ? -8.54422  -16.51193 -21.48909 1.000 21.56317 ? 92  VAL   A N   1 
ATOM   616  C CA  . VAL   A 1 85  ? -8.94730  -16.18360 -22.86155 1.000 23.14730 ? 92  VAL   A CA  1 
ATOM   617  C C   . VAL   A 1 85  ? -9.31134  -14.71836 -22.92549 1.000 26.91792 ? 92  VAL   A C   1 
ATOM   618  O O   . VAL   A 1 85  ? -10.12851 -14.24923 -22.11759 1.000 26.15743 ? 92  VAL   A O   1 
ATOM   619  C CB  . VAL   A 1 85  ? -10.16569 -16.99910 -23.33246 1.000 24.33868 ? 92  VAL   A CB  1 
ATOM   620  C CG1 . VAL   A 1 85  ? -10.39678 -16.69566 -24.82803 1.000 30.56970 ? 92  VAL   A CG1 1 
ATOM   621  C CG2 . VAL   A 1 85  ? -9.91354  -18.46650 -23.10540 1.000 29.43057 ? 92  VAL   A CG2 1 
ATOM   622  N N   . ASP   A 1 86  ? -8.78538  -13.98575 -23.92637 1.000 23.22626 ? 93  ASP   A N   1 
ATOM   623  C CA  . ASP   A 1 86  ? -9.34681  -12.63994 -24.10581 1.000 22.79849 ? 93  ASP   A CA  1 
ATOM   624  C C   . ASP   A 1 86  ? -9.60906  -12.42347 -25.58950 1.000 25.28539 ? 93  ASP   A C   1 
ATOM   625  O O   . ASP   A 1 86  ? -9.01044  -13.07473 -26.45295 1.000 24.37134 ? 93  ASP   A O   1 
ATOM   626  C CB  . ASP   A 1 86  ? -8.43319  -11.47549 -23.61630 1.000 23.62980 ? 93  ASP   A CB  1 
ATOM   627  C CG  . ASP   A 1 86  ? -7.08728  -11.41109 -24.36147 1.000 25.13976 ? 93  ASP   A CG  1 
ATOM   628  O OD1 . ASP   A 1 86  ? -6.00507  -11.75802 -23.75768 1.000 27.29326 ? 93  ASP   A OD1 1 
ATOM   629  O OD2 . ASP   A 1 86  ? -7.13110  -11.02042 -25.54859 1.000 26.33364 ? 93  ASP   A OD2 1 
ATOM   630  N N   . THR   A 1 87  ? -10.51368 -11.49228 -25.89693 1.000 22.54608 ? 94  THR   A N   1 
ATOM   631  C CA  . THR   A 1 87  ? -10.78682 -11.15616 -27.28611 1.000 21.46597 ? 94  THR   A CA  1 
ATOM   632  C C   . THR   A 1 87  ? -10.14645 -9.82612  -27.65105 1.000 24.83486 ? 94  THR   A C   1 
ATOM   633  O O   . THR   A 1 87  ? -10.73095 -9.00087  -28.34684 1.000 24.10693 ? 94  THR   A O   1 
ATOM   634  C CB  . THR   A 1 87  ? -12.28483 -11.12271 -27.53505 1.000 22.16890 ? 94  THR   A CB  1 
ATOM   635  O OG1 . THR   A 1 87  ? -12.88726 -10.27689 -26.55160 1.000 25.22207 ? 94  THR   A OG1 1 
ATOM   636  C CG2 . THR   A 1 87  ? -12.89077 -12.54108 -27.41571 1.000 26.84225 ? 94  THR   A CG2 1 
ATOM   637  N N   . GLY   A 1 88  ? -8.90338  -9.62636  -27.22664 1.000 23.83860 ? 95  GLY   A N   1 
ATOM   638  C CA  . GLY   A 1 88  ? -8.18375  -8.41041  -27.53839 1.000 24.04253 ? 95  GLY   A CA  1 
ATOM   639  C C   . GLY   A 1 88  ? -7.58347  -8.40719  -28.93371 1.000 22.86727 ? 95  GLY   A C   1 
ATOM   640  O O   . GLY   A 1 88  ? -7.98398  -9.15937  -29.82560 1.000 22.83918 ? 95  GLY   A O   1 
ATOM   641  N N   . ILE   A 1 89  ? -6.55444  -7.57430  -29.09166 1.000 22.61165 ? 96  ILE   A N   1 
ATOM   642  C CA  . ILE   A 1 89  ? -6.01471  -7.36085  -30.45087 1.000 24.36534 ? 96  ILE   A CA  1 
ATOM   643  C C   . ILE   A 1 89  ? -5.25036  -8.57862  -30.96048 1.000 23.25382 ? 96  ILE   A C   1 
ATOM   644  O O   . ILE   A 1 89  ? -5.08028  -8.70733  -32.17588 1.000 25.01476 ? 96  ILE   A O   1 
ATOM   645  C CB  . ILE   A 1 89  ? -5.15197  -6.08408  -30.47362 1.000 23.67762 ? 96  ILE   A CB  1 
ATOM   646  C CG1 . ILE   A 1 89  ? -4.83775  -5.64677  -31.92802 1.000 27.33668 ? 96  ILE   A CG1 1 
ATOM   647  C CG2 . ILE   A 1 89  ? -3.90306  -6.28633  -29.65677 1.000 23.47922 ? 96  ILE   A CG2 1 
ATOM   648  C CD1 . ILE   A 1 89  ? -4.46768  -4.21186  -31.99865 1.000 32.05269 ? 96  ILE   A CD1 1 
ATOM   649  N N   . GLY   A 1 90  ? -4.82196  -9.49855  -30.06404 1.000 23.25472 ? 97  GLY   A N   1 
ATOM   650  C CA  . GLY   A 1 90  ? -4.07182  -10.67325 -30.51912 1.000 23.89407 ? 97  GLY   A CA  1 
ATOM   651  C C   . GLY   A 1 90  ? -2.65459  -10.28492 -30.94605 1.000 24.86390 ? 97  GLY   A C   1 
ATOM   652  O O   . GLY   A 1 90  ? -2.19142  -9.15821  -30.74483 1.000 25.71605 ? 97  GLY   A O   1 
ATOM   653  N N   . MET   A 1 91  ? -1.95614  -11.28017 -31.46014 1.000 24.53281 ? 98  MET   A N   1 
ATOM   654  C CA  . MET   A 1 91  ? -0.53620  -11.11836 -31.79029 1.000 24.62025 ? 98  MET   A CA  1 
ATOM   655  C C   . MET   A 1 91  ? -0.28376  -11.72883 -33.15766 1.000 24.72687 ? 98  MET   A C   1 
ATOM   656  O O   . MET   A 1 91  ? -0.79253  -12.81454 -33.46736 1.000 26.39405 ? 98  MET   A O   1 
ATOM   657  C CB  . MET   A 1 91  ? 0.35099   -11.82562 -30.73237 1.000 23.82274 ? 98  MET   A CB  1 
ATOM   658  C CG  . MET   A 1 91  ? 0.40989   -11.06160 -29.40552 1.000 25.84883 ? 98  MET   A CG  1 
ATOM   659  S SD  . MET   A 1 91  ? 1.42074   -11.88136 -28.16934 1.000 27.07102 ? 98  MET   A SD  1 
ATOM   660  C CE  . MET   A 1 91  ? 0.30466   -13.16764 -27.65979 1.000 29.42612 ? 98  MET   A CE  1 
ATOM   661  N N   . THR   A 1 92  ? 0.54982   -11.07115 -33.96400 1.000 25.27607 ? 99  THR   A N   1 
ATOM   662  C CA  . THR   A 1 92  ? 1.03310   -11.68048 -35.21711 1.000 25.87381 ? 99  THR   A CA  1 
ATOM   663  C C   . THR   A 1 92  ? 2.16002   -12.67566 -34.92023 1.000 27.11249 ? 99  THR   A C   1 
ATOM   664  O O   . THR   A 1 92  ? 2.63004   -12.78247 -33.79149 1.000 26.35640 ? 99  THR   A O   1 
ATOM   665  C CB  . THR   A 1 92  ? 1.58397   -10.62627 -36.16026 1.000 30.90299 ? 99  THR   A CB  1 
ATOM   666  O OG1 . THR   A 1 92  ? 2.74991   -10.03494 -35.54196 1.000 31.25076 ? 99  THR   A OG1 1 
ATOM   667  C CG2 . THR   A 1 92  ? 0.54664   -9.56759  -36.42111 1.000 32.09641 ? 99  THR   A CG2 1 
ATOM   668  N N   . LYS   A 1 93  ? 2.54576   -13.44567 -35.93185 1.000 25.55701 ? 100 LYS   A N   1 
ATOM   669  C CA  . LYS   A 1 93  ? 3.66779   -14.38119 -35.77903 1.000 26.17773 ? 100 LYS   A CA  1 
ATOM   670  C C   . LYS   A 1 93  ? 4.90653   -13.63103 -35.36759 1.000 25.41295 ? 100 LYS   A C   1 
ATOM   671  O O   . LYS   A 1 93  ? 5.63600   -14.05716 -34.45501 1.000 25.22703 ? 100 LYS   A O   1 
ATOM   672  C CB  . LYS   A 1 93  ? 3.92647   -15.13734 -37.08745 1.000 27.39650 ? 100 LYS   A CB  1 
ATOM   673  C CG  . LYS   A 1 93  ? 5.07241   -16.19408 -36.88436 1.000 31.67568 ? 100 LYS   A CG  1 
ATOM   674  C CD  . LYS   A 1 93  ? 5.28389   -16.99114 -38.19093 1.000 29.77062 ? 100 LYS   A CD  1 
ATOM   675  C CE  . LYS   A 1 93  ? 6.17425   -18.20928 -37.96614 1.000 35.94520 ? 100 LYS   A CE  1 
ATOM   676  N NZ  . LYS   A 1 93  ? 6.98184   -18.50316 -39.19225 1.000 37.97457 ? 100 LYS   A NZ  1 
ATOM   677  N N   . ALA   A 1 94  ? 5.14798   -12.48727 -36.02577 1.000 26.27183 ? 101 ALA   A N   1 
ATOM   678  C CA  . ALA   A 1 94  ? 6.29554   -11.66931 -35.65246 1.000 28.62088 ? 101 ALA   A CA  1 
ATOM   679  C C   . ALA   A 1 94  ? 6.22416   -11.21767 -34.19745 1.000 27.17018 ? 101 ALA   A C   1 
ATOM   680  O O   . ALA   A 1 94  ? 7.25274   -11.18231 -33.52181 1.000 28.52087 ? 101 ALA   A O   1 
ATOM   681  C CB  . ALA   A 1 94  ? 6.41729   -10.46662 -36.59784 1.000 30.95826 ? 101 ALA   A CB  1 
ATOM   682  N N   . ASP   A 1 95  ? 5.03288   -10.84259 -33.70617 1.000 26.20632 ? 102 ASP   A N   1 
ATOM   683  C CA  . ASP   A 1 95  ? 4.90523   -10.48475 -32.29138 1.000 28.29359 ? 102 ASP   A CA  1 
ATOM   684  C C   . ASP   A 1 95  ? 5.27749   -11.65003 -31.38306 1.000 23.68562 ? 102 ASP   A C   1 
ATOM   685  O O   . ASP   A 1 95  ? 5.94776   -11.47372 -30.34958 1.000 26.38378 ? 102 ASP   A O   1 
ATOM   686  C CB  . ASP   A 1 95  ? 3.45451   -10.07123 -31.97234 1.000 26.81388 ? 102 ASP   A CB  1 
ATOM   687  C CG  . ASP   A 1 95  ? 3.07717   -8.72426  -32.55823 1.000 33.57407 ? 102 ASP   A CG  1 
ATOM   688  O OD1 . ASP   A 1 95  ? 3.97532   -7.88415  -32.78826 1.000 36.96750 ? 102 ASP   A OD1 1 
ATOM   689  O OD2 . ASP   A 1 95  ? 1.86901   -8.53206  -32.84004 1.000 34.79219 ? 102 ASP   A OD2 1 
ATOM   690  N N   . LEU   A 1 96  ? 4.78731   -12.85867 -31.70885 1.000 26.26102 ? 103 LEU   A N   1 
ATOM   691  C CA  . LEU   A 1 96  ? 5.04601   -14.00943 -30.84303 1.000 24.89328 ? 103 LEU   A CA  1 
ATOM   692  C C   . LEU   A 1 96  ? 6.52712   -14.23364 -30.70950 1.000 24.54098 ? 103 LEU   A C   1 
ATOM   693  O O   . LEU   A 1 96  ? 7.03222   -14.42225 -29.58802 1.000 26.06851 ? 103 LEU   A O   1 
ATOM   694  C CB  . LEU   A 1 96  ? 4.43884   -15.27975 -31.40590 1.000 23.82968 ? 103 LEU   A CB  1 
ATOM   695  C CG  . LEU   A 1 96  ? 2.95144   -15.31970 -31.22163 1.000 23.54860 ? 103 LEU   A CG  1 
ATOM   696  C CD1 . LEU   A 1 96  ? 2.56321   -16.61401 -31.99212 1.000 24.22724 ? 103 LEU   A CD1 1 
ATOM   697  C CD2 . LEU   A 1 96  ? 2.49034   -15.36611 -29.73667 1.000 23.48062 ? 103 LEU   A CD2 1 
ATOM   698  N N   . ILE   A 1 97  ? 7.24486   -14.16059 -31.83561 1.000 23.56954 ? 104 ILE   A N   1 
ATOM   699  C CA  . ILE   A 1 97  ? 8.69098   -14.40486 -31.83636 1.000 24.36367 ? 104 ILE   A CA  1 
ATOM   700  C C   . ILE   A 1 97  ? 9.42450   -13.31962 -31.06012 1.000 25.60956 ? 104 ILE   A C   1 
ATOM   701  O O   . ILE   A 1 97  ? 10.41233  -13.59936 -30.34940 1.000 27.78124 ? 104 ILE   A O   1 
ATOM   702  C CB  . ILE   A 1 97  ? 9.19005   -14.51697 -33.28500 1.000 28.19050 ? 104 ILE   A CB  1 
ATOM   703  C CG1 . ILE   A 1 97  ? 8.56090   -15.76028 -33.88572 1.000 29.27393 ? 104 ILE   A CG1 1 
ATOM   704  C CG2 . ILE   A 1 97  ? 10.71805  -14.61409 -33.35894 1.000 28.99976 ? 104 ILE   A CG2 1 
ATOM   705  C CD1 . ILE   A 1 97  ? 8.68598   -15.87309 -35.41080 1.000 30.90628 ? 104 ILE   A CD1 1 
ATOM   706  N N   . ASN   A 1 98  ? 8.96135   -12.07294 -31.18639 1.000 25.32437 ? 105 ASN   A N   1 
ATOM   707  C CA  . ASN   A 1 98  ? 9.54577   -10.91575 -30.52001 1.000 29.34086 ? 105 ASN   A CA  1 
ATOM   708  C C   . ASN   A 1 98  ? 8.99356   -10.79706 -29.09218 1.000 26.59593 ? 105 ASN   A C   1 
ATOM   709  O O   . ASN   A 1 98  ? 8.42923   -9.78727  -28.67260 1.000 25.57286 ? 105 ASN   A O   1 
ATOM   710  C CB  . ASN   A 1 98  ? 9.30144   -9.63081  -31.32834 1.000 29.50236 ? 105 ASN   A CB  1 
ATOM   711  C CG  . ASN   A 1 98  ? 10.22916  -9.51103  -32.51199 1.000 51.53913 ? 105 ASN   A CG  1 
ATOM   712  O OD1 . ASN   A 1 98  ? 11.23587  -8.79599  -32.43660 1.000 54.84764 ? 105 ASN   A OD1 1 
ATOM   713  N ND2 . ASN   A 1 98  ? 9.85858   -10.14131 -33.65606 1.000 56.98168 ? 105 ASN   A ND2 1 
ATOM   714  N N   . ASN   A 1 99  ? 9.17809   -11.87697 -28.33662 1.000 27.15522 ? 106 ASN   A N   1 
ATOM   715  C CA  . ASN   A 1 99  ? 8.81367   -11.92327 -26.92689 1.000 25.27098 ? 106 ASN   A CA  1 
ATOM   716  C C   . ASN   A 1 99  ? 7.36670   -11.54065 -26.67366 1.000 26.59049 ? 106 ASN   A C   1 
ATOM   717  O O   . ASN   A 1 99  ? 7.05120   -10.76305 -25.76892 1.000 24.58363 ? 106 ASN   A O   1 
ATOM   718  C CB  . ASN   A 1 99  ? 9.77041   -11.06553 -26.08335 1.000 23.31454 ? 106 ASN   A CB  1 
ATOM   719  C CG  . ASN   A 1 99  ? 11.22899  -11.50268 -26.25661 1.000 23.48137 ? 106 ASN   A CG  1 
ATOM   720  O OD1 . ASN   A 1 99  ? 11.55338  -12.65294 -25.95750 1.000 28.05070 ? 106 ASN   A OD1 1 
ATOM   721  N ND2 . ASN   A 1 99  ? 12.10232  -10.59229 -26.66940 1.000 29.04065 ? 106 ASN   A ND2 1 
ATOM   722  N N   . LEU   A 1 100 ? 6.47340   -12.15982 -27.44522 1.000 24.09234 ? 107 LEU   A N   1 
ATOM   723  C CA  . LEU   A 1 100 ? 5.03048   -11.98510 -27.23354 1.000 23.87404 ? 107 LEU   A CA  1 
ATOM   724  C C   . LEU   A 1 100 ? 4.62997   -10.50965 -27.18631 1.000 25.41830 ? 107 LEU   A C   1 
ATOM   725  O O   . LEU   A 1 100 ? 3.82715   -10.07150 -26.34816 1.000 27.67383 ? 107 LEU   A O   1 
ATOM   726  C CB  . LEU   A 1 100 ? 4.56401   -12.72031 -25.97251 1.000 21.80531 ? 107 LEU   A CB  1 
ATOM   727  C CG  . LEU   A 1 100 ? 4.99630   -14.18364 -26.11441 1.000 28.21894 ? 107 LEU   A CG  1 
ATOM   728  C CD1 . LEU   A 1 100 ? 6.16712   -14.60387 -25.15226 1.000 29.67423 ? 107 LEU   A CD1 1 
ATOM   729  C CD2 . LEU   A 1 100 ? 3.90858   -15.21084 -26.26630 1.000 33.22963 ? 107 LEU   A CD2 1 
ATOM   730  N N   . GLY   A 1 101 ? 5.14226   -9.75420  -28.15372 1.000 23.50170 ? 108 GLY   A N   1 
ATOM   731  C CA  . GLY   A 1 101 ? 4.77367   -8.35767  -28.31529 1.000 26.65809 ? 108 GLY   A CA  1 
ATOM   732  C C   . GLY   A 1 101 ? 5.30006   -7.40326  -27.25916 1.000 28.26519 ? 108 GLY   A C   1 
ATOM   733  O O   . GLY   A 1 101 ? 4.79091   -6.28189  -27.16360 1.000 32.43648 ? 108 GLY   A O   1 
ATOM   734  N N   . THR   A 1 102 ? 6.30885   -7.80688  -26.46509 1.000 26.76314 ? 109 THR   A N   1 
ATOM   735  C CA  . THR   A 1 102 ? 6.85062   -7.03496  -25.35416 1.000 25.92929 ? 109 THR   A CA  1 
ATOM   736  C C   . THR   A 1 102 ? 8.23710   -6.52003  -25.69004 1.000 30.19917 ? 109 THR   A C   1 
ATOM   737  O O   . THR   A 1 102 ? 8.89781   -7.04222  -26.58289 1.000 30.43562 ? 109 THR   A O   1 
ATOM   738  C CB  . THR   A 1 102 ? 6.94334   -7.86921  -24.06621 1.000 28.54045 ? 109 THR   A CB  1 
ATOM   739  O OG1 . THR   A 1 102 ? 8.04730   -8.78409  -24.16906 1.000 27.68218 ? 109 THR   A OG1 1 
ATOM   740  C CG2 . THR   A 1 102 ? 5.62981   -8.59646  -23.75067 1.000 31.46821 ? 109 THR   A CG2 1 
ATOM   741  N N   . ILE   A 1 103 ? 8.67682   -5.51707  -24.91814 1.000 24.65093 ? 110 ILE   A N   1 
ATOM   742  C CA  . ILE   A 1 103 ? 10.06383  -5.04433  -25.03862 1.000 23.82952 ? 110 ILE   A CA  1 
ATOM   743  C C   . ILE   A 1 103 ? 10.84564  -5.74632  -23.93877 1.000 24.92262 ? 110 ILE   A C   1 
ATOM   744  O O   . ILE   A 1 103 ? 11.45081  -5.12650  -23.04195 1.000 26.16469 ? 110 ILE   A O   1 
ATOM   745  C CB  . ILE   A 1 103 ? 10.15995  -3.51278  -24.96750 1.000 30.16129 ? 110 ILE   A CB  1 
ATOM   746  C CG1 . ILE   A 1 103 ? 9.38758   -2.99614  -23.77906 1.000 32.55398 ? 110 ILE   A CG1 1 
ATOM   747  C CG2 . ILE   A 1 103 ? 9.66314   -2.85422  -26.25786 1.000 29.63076 ? 110 ILE   A CG2 1 
ATOM   748  C CD1 . ILE   A 1 103 ? 9.74594   -1.56410  -23.43281 1.000 41.45607 ? 110 ILE   A CD1 1 
ATOM   749  N N   . ALA   A 1 104 ? 10.84567  -7.06873  -24.00211 1.000 24.97581 ? 111 ALA   A N   1 
ATOM   750  C CA  . ALA   A 1 104 ? 11.31355  -7.84124  -22.85385 1.000 25.35985 ? 111 ALA   A CA  1 
ATOM   751  C C   . ALA   A 1 104 ? 12.77750  -7.59931  -22.51112 1.000 25.38813 ? 111 ALA   A C   1 
ATOM   752  O O   . ALA   A 1 104 ? 13.11909  -7.64675  -21.32857 1.000 25.19505 ? 111 ALA   A O   1 
ATOM   753  C CB  . ALA   A 1 104 ? 11.04385  -9.33522  -23.10670 1.000 27.00795 ? 111 ALA   A CB  1 
ATOM   754  N N   . LYS   A 1 105 ? 13.64977  -7.32426  -23.48233 1.000 25.95277 ? 112 LYS   A N   1 
ATOM   755  C CA  . LYS   A 1 105 ? 15.05372  -7.11020  -23.11953 1.000 25.25901 ? 112 LYS   A CA  1 
ATOM   756  C C   . LYS   A 1 105 ? 15.23425  -5.82726  -22.28589 1.000 29.43330 ? 112 LYS   A C   1 
ATOM   757  O O   . LYS   A 1 105 ? 15.80989  -5.85669  -21.19366 1.000 27.42534 ? 112 LYS   A O   1 
ATOM   758  C CB  . LYS   A 1 105 ? 15.94367  -7.09114  -24.39021 1.000 25.42447 ? 112 LYS   A CB  1 
ATOM   759  C CG  . LYS   A 1 105 ? 17.36283  -6.76052  -24.09889 1.000 32.82559 ? 112 LYS   A CG  1 
ATOM   760  C CD  . LYS   A 1 105 ? 18.20943  -6.75640  -25.40744 1.000 37.56976 ? 112 LYS   A CD  1 
ATOM   761  C CE  . LYS   A 1 105 ? 19.70502  -6.72148  -25.03414 1.000 49.68201 ? 112 LYS   A CE  1 
ATOM   762  N NZ  . LYS   A 1 105 ? 20.58798  -7.10531  -26.20075 1.000 55.44003 ? 112 LYS   A NZ  1 
ATOM   763  N N   . SER   A 1 106 ? 14.71942  -4.69727  -22.76121 1.000 26.18326 ? 113 SER   A N   1 
ATOM   764  C CA  . SER   A 1 106 ? 14.85740  -3.46975  -21.99768 1.000 25.49237 ? 113 SER   A CA  1 
ATOM   765  C C   . SER   A 1 106 ? 13.95851  -3.49216  -20.77199 1.000 23.58034 ? 113 SER   A C   1 
ATOM   766  O O   . SER   A 1 106 ? 14.31494  -2.90519  -19.73894 1.000 26.52239 ? 113 SER   A O   1 
ATOM   767  C CB  . SER   A 1 106 ? 14.58175  -2.25920  -22.89758 1.000 34.48757 ? 113 SER   A CB  1 
ATOM   768  O OG  . SER   A 1 106 ? 13.21758  -2.28159  -23.24990 1.000 32.44155 ? 113 SER   A OG  1 
ATOM   769  N N   . GLY   A 1 107 ? 12.80479  -4.16905  -20.86389 1.000 22.41523 ? 114 GLY   A N   1 
ATOM   770  C CA  . GLY   A 1 107 ? 11.95176  -4.31841  -19.68127 1.000 23.66712 ? 114 GLY   A CA  1 
ATOM   771  C C   . GLY   A 1 107 ? 12.63242  -5.09599  -18.57121 1.000 22.73477 ? 114 GLY   A C   1 
ATOM   772  O O   . GLY   A 1 107 ? 12.56905  -4.69196  -17.41466 1.000 23.46517 ? 114 GLY   A O   1 
ATOM   773  N N   . THR   A 1 108 ? 13.26821  -6.22795  -18.91336 1.000 21.83143 ? 115 THR   A N   1 
ATOM   774  C CA  . THR   A 1 108 ? 13.99546  -7.00960  -17.90778 1.000 22.81727 ? 115 THR   A CA  1 
ATOM   775  C C   . THR   A 1 108 ? 15.10544  -6.19017  -17.28571 1.000 24.62003 ? 115 THR   A C   1 
ATOM   776  O O   . THR   A 1 108 ? 15.33324  -6.26682  -16.06348 1.000 25.33097 ? 115 THR   A O   1 
ATOM   777  C CB  . THR   A 1 108 ? 14.56470  -8.29265  -18.53858 1.000 25.11749 ? 115 THR   A CB  1 
ATOM   778  O OG1 . THR   A 1 108 ? 13.46203  -9.07901  -19.04787 1.000 26.03775 ? 115 THR   A OG1 1 
ATOM   779  C CG2 . THR   A 1 108 ? 15.26033  -9.11727  -17.51428 1.000 26.07595 ? 115 THR   A CG2 1 
ATOM   780  N N   . LYS   A 1 109 ? 15.83198  -5.43213  -18.10934 1.000 23.25317 ? 116 LYS   A N   1 
ATOM   781  C CA  . LYS   A 1 109 ? 16.90635  -4.58870  -17.60091 1.000 23.52807 ? 116 LYS   A CA  1 
ATOM   782  C C   . LYS   A 1 109 ? 16.35601  -3.55868  -16.61169 1.000 23.17368 ? 116 LYS   A C   1 
ATOM   783  O O   . LYS   A 1 109 ? 16.91799  -3.34699  -15.52739 1.000 26.82520 ? 116 LYS   A O   1 
ATOM   784  C CB  . LYS   A 1 109 ? 17.62154  -3.90190  -18.76755 1.000 26.24328 ? 116 LYS   A CB  1 
ATOM   785  C CG  . LYS   A 1 109 ? 18.74023  -2.90059  -18.37404 1.000 32.41288 ? 116 LYS   A CG  1 
ATOM   786  C CD  . LYS   A 1 109 ? 19.31882  -2.13058  -19.59365 1.000 42.66233 ? 116 LYS   A CD  1 
ATOM   787  C CE  . LYS   A 1 109 ? 20.63037  -1.43517  -19.22797 1.000 48.50435 ? 116 LYS   A CE  1 
ATOM   788  N NZ  . LYS   A 1 109 ? 21.30394  -2.11938  -18.07741 1.000 57.08037 ? 116 LYS   A NZ  1 
ATOM   789  N N   . ALA   A 1 110 ? 15.22205  -2.92861  -16.95717 1.000 23.48772 ? 117 ALA   A N   1 
ATOM   790  C CA  . ALA   A 1 110 ? 14.68445  -1.93123  -16.04075 1.000 24.25182 ? 117 ALA   A CA  1 
ATOM   791  C C   . ALA   A 1 110 ? 14.16304  -2.56817  -14.74854 1.000 21.50778 ? 117 ALA   A C   1 
ATOM   792  O O   . ALA   A 1 110 ? 14.25503  -1.95568  -13.67729 1.000 25.72567 ? 117 ALA   A O   1 
ATOM   793  C CB  . ALA   A 1 110 ? 13.55271  -1.17219  -16.75878 1.000 23.82326 ? 117 ALA   A CB  1 
ATOM   794  N N   . PHE   A 1 111 ? 13.54657  -3.76464  -14.84783 1.000 22.98215 ? 118 PHE   A N   1 
ATOM   795  C CA  . PHE   A 1 111 ? 13.08293  -4.49470  -13.66698 1.000 21.39461 ? 118 PHE   A CA  1 
ATOM   796  C C   . PHE   A 1 111 ? 14.26941  -4.82605  -12.75476 1.000 23.99327 ? 118 PHE   A C   1 
ATOM   797  O O   . PHE   A 1 111 ? 14.21858  -4.58122  -11.54591 1.000 22.98502 ? 118 PHE   A O   1 
ATOM   798  C CB  . PHE   A 1 111 ? 12.36421  -5.76398  -14.13711 1.000 22.36492 ? 118 PHE   A CB  1 
ATOM   799  C CG  . PHE   A 1 111 ? 11.75199  -6.60800  -13.08153 1.000 19.67500 ? 118 PHE   A CG  1 
ATOM   800  C CD1 . PHE   A 1 111 ? 11.21440  -6.06724  -11.88528 1.000 22.49035 ? 118 PHE   A CD1 1 
ATOM   801  C CD2 . PHE   A 1 111 ? 11.65882  -7.97882  -13.28667 1.000 22.00223 ? 118 PHE   A CD2 1 
ATOM   802  C CE1 . PHE   A 1 111 ? 10.62865  -6.87888  -10.92937 1.000 21.40532 ? 118 PHE   A CE1 1 
ATOM   803  C CE2 . PHE   A 1 111 ? 11.03767  -8.82497  -12.33616 1.000 24.05516 ? 118 PHE   A CE2 1 
ATOM   804  C CZ  . PHE   A 1 111 ? 10.53873  -8.25106  -11.10782 1.000 23.12009 ? 118 PHE   A CZ  1 
ATOM   805  N N   . MET   A 1 112 ? 15.36124  -5.36735  -13.32969 1.000 25.78622 ? 119 MET   A N   1 
ATOM   806  C CA  . MET   A 1 112 ? 16.50822  -5.70618  -12.49025 1.000 27.44179 ? 119 MET   A CA  1 
ATOM   807  C C   . MET   A 1 112 ? 17.10348  -4.47392  -11.82954 1.000 28.98033 ? 119 MET   A C   1 
ATOM   808  O O   . MET   A 1 112 ? 17.50140  -4.52194  -10.64938 1.000 28.12568 ? 119 MET   A O   1 
ATOM   809  C CB  . MET   A 1 112 ? 17.55714  -6.44100  -13.33517 1.000 24.61006 ? 119 MET   A CB  1 
ATOM   810  C CG  . MET   A 1 112 ? 17.13566  -7.79390  -13.95479 1.000 26.91126 ? 119 MET   A CG  1 
ATOM   811  S SD  . MET   A 1 112 ? 16.29548  -8.93661  -12.77613 1.000 31.46391 ? 119 MET   A SD  1 
ATOM   812  C CE  . MET   A 1 112 ? 17.61695  -9.21996  -11.65861 1.000 36.72559 ? 119 MET   A CE  1 
ATOM   813  N N   . GLU   A 1 113 ? 17.19511  -3.35268  -12.57126 1.000 25.13010 ? 120 GLU   A N   1 
ATOM   814  C CA  . GLU   A 1 113 ? 17.68661  -2.10425  -11.97115 1.000 25.98498 ? 120 GLU   A CA  1 
ATOM   815  C C   . GLU   A 1 113 ? 16.75988  -1.64080  -10.84725 1.000 28.37086 ? 120 GLU   A C   1 
ATOM   816  O O   . GLU   A 1 113 ? 17.22459  -1.19381  -9.78754  1.000 30.44708 ? 120 GLU   A O   1 
ATOM   817  C CB  . GLU   A 1 113 ? 17.78705  -1.02076  -13.05595 1.000 33.12132 ? 120 GLU   A CB  1 
ATOM   818  C CG  . GLU   A 1 113 ? 19.02151  -1.14461  -13.96876 1.000 33.71713 ? 120 GLU   A CG  1 
ATOM   819  C CD  . GLU   A 1 113 ? 18.91106  -0.32231  -15.27766 1.000 53.45949 ? 120 GLU   A CD  1 
ATOM   820  O OE1 . GLU   A 1 113 ? 17.81754  0.19396   -15.59813 1.000 52.72077 ? 120 GLU   A OE1 1 
ATOM   821  O OE2 . GLU   A 1 113 ? 19.92114  -0.20536  -16.00263 1.000 48.49927 ? 120 GLU   A OE2 1 
ATOM   822  N N   . ALA   A 1 114 ? 15.44717  -1.76912  -11.05718 1.000 24.74349 ? 121 ALA   A N   1 
ATOM   823  C CA  . ALA   A 1 114 ? 14.50961  -1.38119  -10.00724 1.000 22.27500 ? 121 ALA   A CA  1 
ATOM   824  C C   . ALA   A 1 114 ? 14.70094  -2.23161  -8.76481  1.000 26.70216 ? 121 ALA   A C   1 
ATOM   825  O O   . ALA   A 1 114 ? 14.59667  -1.71726  -7.63837  1.000 27.48507 ? 121 ALA   A O   1 
ATOM   826  C CB  . ALA   A 1 114 ? 13.07349  -1.52325  -10.52169 1.000 23.45919 ? 121 ALA   A CB  1 
ATOM   827  N N   . LEU   A 1 115 ? 14.87765  -3.54930  -8.93693  1.000 24.97778 ? 122 LEU   A N   1 
ATOM   828  C CA  . LEU   A 1 115 ? 15.07716  -4.40634  -7.75980  1.000 24.96165 ? 122 LEU   A CA  1 
ATOM   829  C C   . LEU   A 1 115 ? 16.33400  -4.01602  -7.00184  1.000 26.68403 ? 122 LEU   A C   1 
ATOM   830  O O   . LEU   A 1 115 ? 16.34994  -4.03271  -5.76597  1.000 30.75429 ? 122 LEU   A O   1 
ATOM   831  C CB  . LEU   A 1 115 ? 15.14670  -5.88093  -8.17480  1.000 23.33797 ? 122 LEU   A CB  1 
ATOM   832  C CG  . LEU   A 1 115 ? 13.82630  -6.47597  -8.73124  1.000 24.64537 ? 122 LEU   A CG  1 
ATOM   833  C CD1 . LEU   A 1 115 ? 14.05040  -7.89627  -9.27339  1.000 27.79572 ? 122 LEU   A CD1 1 
ATOM   834  C CD2 . LEU   A 1 115 ? 12.73166  -6.49895  -7.65942  1.000 24.22164 ? 122 LEU   A CD2 1 
ATOM   835  N N   . GLN   A 1 116 ? 17.39253  -3.63802  -7.72154  1.000 27.84340 ? 123 GLN   A N   1 
ATOM   836  C CA  . GLN   A 1 116 ? 18.57324  -3.11350  -7.04470  1.000 33.27504 ? 123 GLN   A CA  1 
ATOM   837  C C   . GLN   A 1 116 ? 18.27062  -1.84269  -6.26557  1.000 32.83859 ? 123 GLN   A C   1 
ATOM   838  O O   . GLN   A 1 116 ? 18.85980  -1.62164  -5.20359  1.000 35.55076 ? 123 GLN   A O   1 
ATOM   839  C CB  . GLN   A 1 116 ? 19.67842  -2.88754  -8.08497  1.000 34.34090 ? 123 GLN   A CB  1 
ATOM   840  C CG  . GLN   A 1 116 ? 20.29954  -4.17151  -8.60277  1.000 53.54737 ? 123 GLN   A CG  1 
ATOM   841  C CD  . GLN   A 1 116 ? 20.75440  -5.08911  -7.46559  1.000 62.55977 ? 123 GLN   A CD  1 
ATOM   842  O OE1 . GLN   A 1 116 ? 20.17077  -6.15885  -7.23331  1.000 63.01376 ? 123 GLN   A OE1 1 
ATOM   843  N NE2 . GLN   A 1 116 ? 21.79665  -4.66749  -6.74925  1.000 55.30787 ? 123 GLN   A NE2 1 
ATOM   844  N N   . ALA   A 1 117 ? 17.37978  -0.98710  -6.76924  1.000 30.77850 ? 124 ALA   A N   1 
ATOM   845  C CA  . ALA   A 1 117 ? 17.00364  0.25639   -6.09208  1.000 32.81063 ? 124 ALA   A CA  1 
ATOM   846  C C   . ALA   A 1 117 ? 15.88931  0.07734   -5.05036  1.000 33.49607 ? 124 ALA   A C   1 
ATOM   847  O O   . ALA   A 1 117 ? 15.37883  1.07778   -4.52923  1.000 35.71642 ? 124 ALA   A O   1 
ATOM   848  C CB  . ALA   A 1 117 ? 16.57150  1.30453   -7.11808  1.000 36.16462 ? 124 ALA   A CB  1 
ATOM   849  N N   . GLY   A 1 118 ? 15.47012  -1.14336  -4.75249  1.000 29.48354 ? 125 GLY   A N   1 
ATOM   850  C CA  . GLY   A 1 118 ? 14.50144  -1.33764  -3.68771  1.000 31.08627 ? 125 GLY   A CA  1 
ATOM   851  C C   . GLY   A 1 118 ? 13.08371  -1.67355  -4.12531  1.000 30.92500 ? 125 GLY   A C   1 
ATOM   852  O O   . GLY   A 1 118 ? 12.19363  -1.71614  -3.27425  1.000 31.20696 ? 125 GLY   A O   1 
ATOM   853  N N   . ALA   A 1 119 ? 12.84570  -1.89683  -5.41950  1.000 25.68269 ? 126 ALA   A N   1 
ATOM   854  C CA  . ALA   A 1 119 ? 11.50114  -2.28316  -5.84780  1.000 24.02954 ? 126 ALA   A CA  1 
ATOM   855  C C   . ALA   A 1 119 ? 11.19547  -3.69469  -5.36261  1.000 27.70864 ? 126 ALA   A C   1 
ATOM   856  O O   . ALA   A 1 119 ? 12.08799  -4.44516  -4.97720  1.000 31.93907 ? 126 ALA   A O   1 
ATOM   857  C CB  . ALA   A 1 119 ? 11.36725  -2.21474  -7.36562  1.000 24.04448 ? 126 ALA   A CB  1 
ATOM   858  N N   . ASP   A 1 120 ? 9.92227   -4.04378  -5.36516  1.000 26.51068 ? 127 ASP   A N   1 
ATOM   859  C CA  . ASP   A 1 120 ? 9.50869   -5.41801  -5.03776  1.000 27.03602 ? 127 ASP   A CA  1 
ATOM   860  C C   . ASP   A 1 120 ? 9.40628   -6.28902  -6.28569  1.000 23.91188 ? 127 ASP   A C   1 
ATOM   861  O O   . ASP   A 1 120 ? 9.05630   -5.80351  -7.35076  1.000 24.69497 ? 127 ASP   A O   1 
ATOM   862  C CB  . ASP   A 1 120 ? 8.14058   -5.43913  -4.33911  1.000 27.93306 ? 127 ASP   A CB  1 
ATOM   863  C CG  . ASP   A 1 120 ? 8.03133   -4.44683  -3.19330  1.000 54.67652 ? 127 ASP   A CG  1 
ATOM   864  O OD1 . ASP   A 1 120 ? 7.05961   -3.65039  -3.16823  1.000 54.59989 ? 127 ASP   A OD1 1 
ATOM   865  O OD2 . ASP   A 1 120 ? 8.90453   -4.49728  -2.30099  1.000 49.38116 ? 127 ASP   A OD2 1 
ATOM   866  N N   . ILE   A 1 121 ? 9.62783   -7.60254  -6.10623  1.000 24.94238 ? 128 ILE   A N   1 
ATOM   867  C CA  . ILE   A 1 121 ? 9.43359   -8.58619  -7.17885  1.000 23.76823 ? 128 ILE   A CA  1 
ATOM   868  C C   . ILE   A 1 121 ? 8.02347   -8.52817  -7.73423  1.000 23.79386 ? 128 ILE   A C   1 
ATOM   869  O O   . ILE   A 1 121 ? 7.80771   -8.71414  -8.95071  1.000 25.54010 ? 128 ILE   A O   1 
ATOM   870  C CB  . ILE   A 1 121 ? 9.76589   -9.99634  -6.65450  1.000 26.60442 ? 128 ILE   A CB  1 
ATOM   871  C CG1 . ILE   A 1 121 ? 11.30214  -10.17040 -6.63897  1.000 28.64059 ? 128 ILE   A CG1 1 
ATOM   872  C CG2 . ILE   A 1 121 ? 9.05650   -11.09570 -7.43095  1.000 30.98119 ? 128 ILE   A CG2 1 
ATOM   873  C CD1 . ILE   A 1 121 ? 11.68096  -11.40457 -5.74768  1.000 31.66981 ? 128 ILE   A CD1 1 
ATOM   874  N N   . SER   A 1 122 ? 7.05052   -8.27587  -6.86193  1.000 25.95919 ? 129 SER   A N   1 
ATOM   875  C CA  . SER   A 1 122 ? 5.67861   -8.19627  -7.35215  1.000 23.81925 ? 129 SER   A CA  1 
ATOM   876  C C   . SER   A 1 122 ? 5.43156   -7.05103  -8.33278  1.000 27.29604 ? 129 SER   A C   1 
ATOM   877  O O   . SER   A 1 122 ? 4.33400   -7.02797  -8.92667  1.000 28.17512 ? 129 SER   A O   1 
ATOM   878  C CB  . SER   A 1 122 ? 4.75437   -8.11360  -6.14756  1.000 26.91943 ? 129 SER   A CB  1 
ATOM   879  O OG  . SER   A 1 122 ? 4.91902   -6.88734  -5.48720  1.000 33.78549 ? 129 SER   A OG  1 
ATOM   880  N N   . MET   A 1 123 ? 6.33604   -6.07425  -8.44215  1.000 23.58935 ? 130 MET   A N   1 
ATOM   881  C CA  . MET   A 1 123 ? 6.21715   -4.99329  -9.44070  1.000 24.97878 ? 130 MET   A CA  1 
ATOM   882  C C   . MET   A 1 123 ? 6.56351   -5.37463  -10.85401 1.000 25.16077 ? 130 MET   A C   1 
ATOM   883  O O   . MET   A 1 123 ? 6.58006   -4.47047  -11.70181 1.000 25.41583 ? 130 MET   A O   1 
ATOM   884  C CB  . MET   A 1 123 ? 6.98697   -3.72139  -9.02316  1.000 24.40150 ? 130 MET   A CB  1 
ATOM   885  C CG  . MET   A 1 123 ? 6.44429   -3.23980  -7.61867  1.000 27.03412 ? 130 MET   A CG  1 
ATOM   886  S SD  . MET   A 1 123 ? 7.61695   -2.06033  -6.88058  1.000 33.00263 ? 130 MET   A SD  1 
ATOM   887  C CE  . MET   A 1 123 ? 7.67197   -0.78664  -8.08321  1.000 41.37656 ? 130 MET   A CE  1 
ATOM   888  N N   . ILE   A 1 124 ? 6.75370   -6.66420  -11.14745 1.000 22.12193 ? 131 ILE   A N   1 
ATOM   889  C CA  . ILE   A 1 124 ? 7.22380   -7.08870  -12.46594 1.000 22.48636 ? 131 ILE   A CA  1 
ATOM   890  C C   . ILE   A 1 124 ? 6.37350   -6.47707  -13.59453 1.000 21.57543 ? 131 ILE   A C   1 
ATOM   891  O O   . ILE   A 1 124 ? 6.90776   -6.12110  -14.65168 1.000 22.29466 ? 131 ILE   A O   1 
ATOM   892  C CB  . ILE   A 1 124 ? 7.21463   -8.62405  -12.54263 1.000 22.05910 ? 131 ILE   A CB  1 
ATOM   893  C CG1 . ILE   A 1 124 ? 7.75011   -9.07162  -13.92518 1.000 21.36784 ? 131 ILE   A CG1 1 
ATOM   894  C CG2 . ILE   A 1 124 ? 5.74894   -9.18910  -12.29447 1.000 21.51961 ? 131 ILE   A CG2 1 
ATOM   895  C CD1 . ILE   A 1 124 ? 7.95798   -10.60880 -14.03748 1.000 24.11727 ? 131 ILE   A CD1 1 
ATOM   896  N N   . GLY   A 1 125 ? 5.06280   -6.35277  -13.40315 1.000 24.82399 ? 132 GLY   A N   1 
ATOM   897  C CA  . GLY   A 1 125 ? 4.21642   -5.90517  -14.51894 1.000 25.03396 ? 132 GLY   A CA  1 
ATOM   898  C C   . GLY   A 1 125 ? 4.44472   -4.44957  -14.93407 1.000 26.24441 ? 132 GLY   A C   1 
ATOM   899  O O   . GLY   A 1 125 ? 4.09159   -4.06869  -16.06559 1.000 29.11517 ? 132 GLY   A O   1 
ATOM   900  N N   . GLN   A 1 126 ? 5.00552   -3.63657  -14.03944 1.000 25.55508 ? 133 GLN   A N   1 
ATOM   901  C CA  . GLN   A 1 126 ? 5.33422   -2.25451  -14.36785 1.000 29.46375 ? 133 GLN   A CA  1 
ATOM   902  C C   . GLN   A 1 126 ? 6.45488   -2.16469  -15.38282 1.000 26.15708 ? 133 GLN   A C   1 
ATOM   903  O O   . GLN   A 1 126 ? 6.68322   -1.06976  -15.92021 1.000 29.83293 ? 133 GLN   A O   1 
ATOM   904  C CB  . GLN   A 1 126 ? 5.78102   -1.48741  -13.12427 1.000 28.42662 ? 133 GLN   A CB  1 
ATOM   905  C CG  . GLN   A 1 126 ? 4.67597   -1.42420  -12.08945 1.000 38.65161 ? 133 GLN   A CG  1 
ATOM   906  C CD  . GLN   A 1 126 ? 5.20267   -0.82341  -10.79778 1.000 45.47941 ? 133 GLN   A CD  1 
ATOM   907  O OE1 . GLN   A 1 126 ? 6.21591   -0.08286  -10.77992 1.000 39.01802 ? 133 GLN   A OE1 1 
ATOM   908  N NE2 . GLN   A 1 126 ? 4.52764   -1.13770  -9.70878  1.000 43.76536 ? 133 GLN   A NE2 1 
ATOM   909  N N   . PHE   A 1 127 ? 7.14330   -3.27045  -15.64465 1.000 23.77949 ? 134 PHE   A N   1 
ATOM   910  C CA  . PHE   A 1 127 ? 8.27070   -3.26530  -16.56984 1.000 24.57475 ? 134 PHE   A CA  1 
ATOM   911  C C   . PHE   A 1 127 ? 7.96119   -4.03759  -17.83221 1.000 29.49649 ? 134 PHE   A C   1 
ATOM   912  O O   . PHE   A 1 127 ? 8.84126   -4.27857  -18.66465 1.000 25.86219 ? 134 PHE   A O   1 
ATOM   913  C CB  . PHE   A 1 127 ? 9.54935   -3.76973  -15.85094 1.000 23.37988 ? 134 PHE   A CB  1 
ATOM   914  C CG  . PHE   A 1 127 ? 9.78971   -3.02589  -14.59066 1.000 26.58502 ? 134 PHE   A CG  1 
ATOM   915  C CD1 . PHE   A 1 127 ? 10.30015  -1.70744  -14.63955 1.000 27.72867 ? 134 PHE   A CD1 1 
ATOM   916  C CD2 . PHE   A 1 127 ? 9.41182   -3.55788  -13.37201 1.000 21.49486 ? 134 PHE   A CD2 1 
ATOM   917  C CE1 . PHE   A 1 127 ? 10.44507  -0.95225  -13.44385 1.000 23.33084 ? 134 PHE   A CE1 1 
ATOM   918  C CE2 . PHE   A 1 127 ? 9.56807   -2.80878  -12.20721 1.000 25.83521 ? 134 PHE   A CE2 1 
ATOM   919  C CZ  . PHE   A 1 127 ? 10.07278  -1.52113  -12.25358 1.000 28.78564 ? 134 PHE   A CZ  1 
ATOM   920  N N   . GLY   A 1 128 ? 6.69708   -4.34351  -18.05543 1.000 23.04769 ? 135 GLY   A N   1 
ATOM   921  C CA  . GLY   A 1 128 ? 6.33583   -4.89502  -19.33659 1.000 24.10635 ? 135 GLY   A CA  1 
ATOM   922  C C   . GLY   A 1 128 ? 6.56968   -6.37874  -19.51879 1.000 23.80902 ? 135 GLY   A C   1 
ATOM   923  O O   . GLY   A 1 128 ? 6.32664   -6.86791  -20.63243 1.000 28.97172 ? 135 GLY   A O   1 
ATOM   924  N N   . VAL   A 1 129 ? 7.01378   -7.11273  -18.48505 1.000 19.99424 ? 136 VAL   A N   1 
ATOM   925  C CA  . VAL   A 1 129 ? 7.38916   -8.52323  -18.59507 1.000 20.69807 ? 136 VAL   A CA  1 
ATOM   926  C C   . VAL   A 1 129 ? 6.57127   -9.36982  -17.64214 1.000 22.34843 ? 136 VAL   A C   1 
ATOM   927  O O   . VAL   A 1 129 ? 6.95061   -10.50719 -17.29976 1.000 21.66478 ? 136 VAL   A O   1 
ATOM   928  C CB  . VAL   A 1 129 ? 8.89443   -8.75080  -18.37638 1.000 19.79632 ? 136 VAL   A CB  1 
ATOM   929  C CG1 . VAL   A 1 129 ? 9.68058   -8.24731  -19.64920 1.000 24.79090 ? 136 VAL   A CG1 1 
ATOM   930  C CG2 . VAL   A 1 129 ? 9.40026   -7.99807  -17.15338 1.000 23.06268 ? 136 VAL   A CG2 1 
ATOM   931  N N   . GLY   A 1 130 ? 5.37538   -8.86187  -17.29840 1.000 21.69814 ? 137 GLY   A N   1 
ATOM   932  C CA  . GLY   A 1 130 ? 4.50734   -9.61135  -16.40751 1.000 21.05081 ? 137 GLY   A CA  1 
ATOM   933  C C   . GLY   A 1 130 ? 4.08280   -10.97628 -16.92448 1.000 23.05573 ? 137 GLY   A C   1 
ATOM   934  O O   . GLY   A 1 130 ? 3.77926   -11.86306 -16.12311 1.000 21.23267 ? 137 GLY   A O   1 
ATOM   935  N N   . PHE   A 1 131 ? 4.03137   -11.15595 -18.24396 1.000 21.66996 ? 138 PHE   A N   1 
ATOM   936  C CA  . PHE   A 1 131 ? 3.66641   -12.46381 -18.79670 1.000 20.79277 ? 138 PHE   A CA  1 
ATOM   937  C C   . PHE   A 1 131 ? 4.48588   -13.58970 -18.16898 1.000 19.82450 ? 138 PHE   A C   1 
ATOM   938  O O   . PHE   A 1 131 ? 3.95871   -14.66456 -17.85941 1.000 21.72439 ? 138 PHE   A O   1 
ATOM   939  C CB  . PHE   A 1 131 ? 3.86580   -12.46448 -20.30373 1.000 22.77149 ? 138 PHE   A CB  1 
ATOM   940  C CG  . PHE   A 1 131 ? 3.82695   -13.84284 -20.89860 1.000 22.74220 ? 138 PHE   A CG  1 
ATOM   941  C CD1 . PHE   A 1 131 ? 2.63014   -14.48363 -21.07118 1.000 24.57333 ? 138 PHE   A CD1 1 
ATOM   942  C CD2 . PHE   A 1 131 ? 5.01731   -14.51540 -21.21735 1.000 23.18569 ? 138 PHE   A CD2 1 
ATOM   943  C CE1 . PHE   A 1 131 ? 2.56905   -15.76724 -21.59108 1.000 23.09746 ? 138 PHE   A CE1 1 
ATOM   944  C CE2 . PHE   A 1 131 ? 4.94581   -15.80667 -21.73487 1.000 23.26192 ? 138 PHE   A CE2 1 
ATOM   945  C CZ  . PHE   A 1 131 ? 3.73465   -16.42673 -21.93468 1.000 27.62882 ? 138 PHE   A CZ  1 
ATOM   946  N N   . TYR   A 1 132 ? 5.78083   -13.36279 -17.97493 1.000 20.46495 ? 139 TYR   A N   1 
ATOM   947  C CA  . TYR   A 1 132 ? 6.65326   -14.45682 -17.56780 1.000 21.17213 ? 139 TYR   A CA  1 
ATOM   948  C C   . TYR   A 1 132 ? 6.38176   -14.91801 -16.13620 1.000 21.02428 ? 139 TYR   A C   1 
ATOM   949  O O   . TYR   A 1 132 ? 6.88122   -15.98534 -15.74175 1.000 22.07511 ? 139 TYR   A O   1 
ATOM   950  C CB  . TYR   A 1 132 ? 8.14923   -14.04624 -17.75137 1.000 21.21794 ? 139 TYR   A CB  1 
ATOM   951  C CG  . TYR   A 1 132 ? 8.40830   -13.76337 -19.22476 1.000 22.47866 ? 139 TYR   A CG  1 
ATOM   952  C CD1 . TYR   A 1 132 ? 8.63615   -14.82485 -20.14025 1.000 22.47427 ? 139 TYR   A CD1 1 
ATOM   953  C CD2 . TYR   A 1 132 ? 8.37529   -12.45622 -19.72018 1.000 22.53492 ? 139 TYR   A CD2 1 
ATOM   954  C CE1 . TYR   A 1 132 ? 8.85039   -14.55766 -21.50357 1.000 22.88480 ? 139 TYR   A CE1 1 
ATOM   955  C CE2 . TYR   A 1 132 ? 8.54183   -12.18118 -21.09314 1.000 26.39532 ? 139 TYR   A CE2 1 
ATOM   956  C CZ  . TYR   A 1 132 ? 8.79476   -13.22926 -21.96030 1.000 27.11789 ? 139 TYR   A CZ  1 
ATOM   957  O OH  . TYR   A 1 132 ? 8.98488   -12.92046 -23.29584 1.000 27.31039 ? 139 TYR   A OH  1 
ATOM   958  N N   . SER   A 1 133 ? 5.60410   -14.15358 -15.35240 1.000 20.77906 ? 140 SER   A N   1 
ATOM   959  C CA  . SER   A 1 133 ? 5.16869   -14.62307 -14.05381 1.000 20.27456 ? 140 SER   A CA  1 
ATOM   960  C C   . SER   A 1 133 ? 4.28959   -15.85901 -14.15232 1.000 19.14349 ? 140 SER   A C   1 
ATOM   961  O O   . SER   A 1 133 ? 4.10658   -16.56148 -13.14976 1.000 21.83795 ? 140 SER   A O   1 
ATOM   962  C CB  . SER   A 1 133 ? 4.43469   -13.50207 -13.28187 1.000 23.29442 ? 140 SER   A CB  1 
ATOM   963  O OG  . SER   A 1 133 ? 3.12923   -13.27932 -13.87573 1.000 22.28352 ? 140 SER   A OG  1 
ATOM   964  N N   . ALA   A 1 134 ? 3.78507   -16.17699 -15.35938 1.000 20.66111 ? 141 ALA   A N   1 
ATOM   965  C CA  . ALA   A 1 134 ? 3.11803   -17.46864 -15.54681 1.000 21.94157 ? 141 ALA   A CA  1 
ATOM   966  C C   . ALA   A 1 134 ? 3.95271   -18.62615 -15.02311 1.000 22.67702 ? 141 ALA   A C   1 
ATOM   967  O O   . ALA   A 1 134 ? 3.40834   -19.62667 -14.53775 1.000 22.66442 ? 141 ALA   A O   1 
ATOM   968  C CB  . ALA   A 1 134 ? 2.81972   -17.67288 -17.04886 1.000 21.74167 ? 141 ALA   A CB  1 
ATOM   969  N N   . TYR   A 1 135 ? 5.29030   -18.52469 -15.12281 1.000 21.93513 ? 142 TYR   A N   1 
ATOM   970  C CA  . TYR   A 1 135 ? 6.13685   -19.63990 -14.71477 1.000 22.11849 ? 142 TYR   A CA  1 
ATOM   971  C C   . TYR   A 1 135 ? 6.28118   -19.73818 -13.17505 1.000 24.01657 ? 142 TYR   A C   1 
ATOM   972  O O   . TYR   A 1 135 ? 6.99043   -20.60636 -12.69744 1.000 25.10492 ? 142 TYR   A O   1 
ATOM   973  C CB  . TYR   A 1 135 ? 7.49410   -19.53109 -15.43786 1.000 19.76183 ? 142 TYR   A CB  1 
ATOM   974  C CG  . TYR   A 1 135 ? 7.30725   -19.82790 -16.91268 1.000 23.42327 ? 142 TYR   A CG  1 
ATOM   975  C CD1 . TYR   A 1 135 ? 7.30704   -21.14696 -17.36861 1.000 23.27084 ? 142 TYR   A CD1 1 
ATOM   976  C CD2 . TYR   A 1 135 ? 7.05882   -18.80414 -17.82976 1.000 21.37085 ? 142 TYR   A CD2 1 
ATOM   977  C CE1 . TYR   A 1 135 ? 7.06660   -21.44780 -18.72174 1.000 24.02183 ? 142 TYR   A CE1 1 
ATOM   978  C CE2 . TYR   A 1 135 ? 6.84094   -19.09552 -19.21144 1.000 21.05635 ? 142 TYR   A CE2 1 
ATOM   979  C CZ  . TYR   A 1 135 ? 6.84053   -20.40458 -19.61379 1.000 23.47061 ? 142 TYR   A CZ  1 
ATOM   980  O OH  . TYR   A 1 135 ? 6.60488   -20.65608 -20.96935 1.000 22.46489 ? 142 TYR   A OH  1 
ATOM   981  N N   . LEU   A 1 136 ? 5.60175   -18.88396 -12.41264 1.000 23.19934 ? 143 LEU   A N   1 
ATOM   982  C CA  . LEU   A 1 136 ? 5.46976   -19.12632 -10.98287 1.000 25.37550 ? 143 LEU   A CA  1 
ATOM   983  C C   . LEU   A 1 136 ? 4.65076   -20.38176 -10.73846 1.000 25.84323 ? 143 LEU   A C   1 
ATOM   984  O O   . LEU   A 1 136 ? 4.85011   -21.07073 -9.74290  1.000 27.34047 ? 143 LEU   A O   1 
ATOM   985  C CB  . LEU   A 1 136 ? 4.78061   -17.93278 -10.33095 1.000 22.31651 ? 143 LEU   A CB  1 
ATOM   986  C CG  . LEU   A 1 136 ? 5.56841   -16.62821 -10.25355 1.000 23.54257 ? 143 LEU   A CG  1 
ATOM   987  C CD1 . LEU   A 1 136 ? 4.68247   -15.50390 -9.83542  1.000 24.76801 ? 143 LEU   A CD1 1 
ATOM   988  C CD2 . LEU   A 1 136 ? 6.77719   -16.79404 -9.30158  1.000 24.70357 ? 143 LEU   A CD2 1 
ATOM   989  N N   . VAL   A 1 137 ? 3.70103   -20.67705 -11.64444 1.000 23.53430 ? 144 VAL   A N   1 
ATOM   990  C CA  . VAL   A 1 137 ? 2.76106   -21.76022 -11.39636 1.000 22.27247 ? 144 VAL   A CA  1 
ATOM   991  C C   . VAL   A 1 137 ? 2.72430   -22.79373 -12.50330 1.000 25.19731 ? 144 VAL   A C   1 
ATOM   992  O O   . VAL   A 1 137 ? 2.20623   -23.88881 -12.26106 1.000 26.41037 ? 144 VAL   A O   1 
ATOM   993  C CB  . VAL   A 1 137 ? 1.31737   -21.23674 -11.12698 1.000 24.12397 ? 144 VAL   A CB  1 
ATOM   994  C CG1 . VAL   A 1 137 ? 1.28066   -20.37289 -9.85145  1.000 25.72029 ? 144 VAL   A CG1 1 
ATOM   995  C CG2 . VAL   A 1 137 ? 0.73966   -20.46947 -12.34906 1.000 23.60507 ? 144 VAL   A CG2 1 
ATOM   996  N N   . ALA   A 1 138 ? 3.24748   -22.50492 -13.67543 1.000 25.39334 ? 145 ALA   A N   1 
ATOM   997  C CA  . ALA   A 1 138 ? 3.10542   -23.37704 -14.84303 1.000 23.70691 ? 145 ALA   A CA  1 
ATOM   998  C C   . ALA   A 1 138 ? 4.42658   -24.04034 -15.17546 1.000 23.80358 ? 145 ALA   A C   1 
ATOM   999  O O   . ALA   A 1 138 ? 5.46421   -23.37279 -15.20294 1.000 27.61697 ? 145 ALA   A O   1 
ATOM   1000 C CB  . ALA   A 1 138 ? 2.64382   -22.57499 -16.04549 1.000 25.45424 ? 145 ALA   A CB  1 
ATOM   1001 N N   . GLU   A 1 139 ? 4.36998   -25.33334 -15.46870 1.000 23.71840 ? 146 GLU   A N   1 
ATOM   1002 C CA  . GLU   A 1 139 ? 5.57256   -25.98658 -16.00706 1.000 24.62170 ? 146 GLU   A CA  1 
ATOM   1003 C C   . GLU   A 1 139 ? 5.69134   -25.78007 -17.51685 1.000 31.54105 ? 146 GLU   A C   1 
ATOM   1004 O O   . GLU   A 1 139 ? 6.78173   -25.93333 -18.06945 1.000 29.94550 ? 146 GLU   A O   1 
ATOM   1005 C CB  . GLU   A 1 139 ? 5.55597   -27.48310 -15.70974 1.000 32.41100 ? 146 GLU   A CB  1 
ATOM   1006 C CG  . GLU   A 1 139 ? 4.30254   -28.19565 -16.07216 1.000 41.54006 ? 146 GLU   A CG  1 
ATOM   1007 C CD  . GLU   A 1 139 ? 4.31149   -29.68922 -15.71936 1.000 69.58290 ? 146 GLU   A CD  1 
ATOM   1008 O OE1 . GLU   A 1 139 ? 3.71004   -30.47273 -16.49839 1.000 66.98601 ? 146 GLU   A OE1 1 
ATOM   1009 O OE2 . GLU   A 1 139 ? 4.87511   -30.07117 -14.65791 1.000 62.02631 ? 146 GLU   A OE2 1 
ATOM   1010 N N   . LYS   A 1 140 ? 4.59240   -25.46969 -18.19613 1.000 26.21861 ? 147 LYS   A N   1 
ATOM   1011 C CA  . LYS   A 1 140 ? 4.58208   -25.25361 -19.63223 1.000 25.29497 ? 147 LYS   A CA  1 
ATOM   1012 C C   . LYS   A 1 140 ? 3.50917   -24.21139 -19.87386 1.000 25.43604 ? 147 LYS   A C   1 
ATOM   1013 O O   . LYS   A 1 140 ? 2.48120   -24.24381 -19.19623 1.000 22.75213 ? 147 LYS   A O   1 
ATOM   1014 C CB  . LYS   A 1 140 ? 4.28801   -26.55549 -20.40226 1.000 26.08582 ? 147 LYS   A CB  1 
ATOM   1015 C CG  . LYS   A 1 140 ? 4.15098   -26.39766 -21.89512 1.000 28.32133 ? 147 LYS   A CG  1 
ATOM   1016 C CD  . LYS   A 1 140 ? 4.09521   -27.80916 -22.46500 1.000 30.36027 ? 147 LYS   A CD  1 
ATOM   1017 C CE  . LYS   A 1 140 ? 2.81938   -28.05708 -23.19382 1.000 41.48785 ? 147 LYS   A CE  1 
ATOM   1018 N NZ  . LYS   A 1 140 ? 2.68789   -29.55577 -23.34602 1.000 47.44097 ? 147 LYS   A NZ  1 
ATOM   1019 N N   . VAL   A 1 141 ? 3.76559   -23.27918 -20.77931 1.000 22.65727 ? 148 VAL   A N   1 
ATOM   1020 C CA  . VAL   A 1 141 ? 2.73895   -22.31032 -21.18274 1.000 21.82615 ? 148 VAL   A CA  1 
ATOM   1021 C C   . VAL   A 1 141 ? 2.55934   -22.43306 -22.69566 1.000 24.20786 ? 148 VAL   A C   1 
ATOM   1022 O O   . VAL   A 1 141 ? 3.54788   -22.47055 -23.44285 1.000 23.15609 ? 148 VAL   A O   1 
ATOM   1023 C CB  . VAL   A 1 141 ? 3.12427   -20.89372 -20.78191 1.000 19.99865 ? 148 VAL   A CB  1 
ATOM   1024 C CG1 . VAL   A 1 141 ? 2.04373   -19.90511 -21.25033 1.000 21.52909 ? 148 VAL   A CG1 1 
ATOM   1025 C CG2 . VAL   A 1 141 ? 3.33507   -20.80505 -19.24136 1.000 21.08930 ? 148 VAL   A CG2 1 
ATOM   1026 N N   . THR   A 1 142 ? 1.28837   -22.47083 -23.14744 1.000 22.71951 ? 149 THR   A N   1 
ATOM   1027 C CA  . THR   A 1 142 ? 0.92955   -22.46961 -24.56100 1.000 22.14136 ? 149 THR   A CA  1 
ATOM   1028 C C   . THR   A 1 142 ? 0.09980   -21.21346 -24.80341 1.000 27.21158 ? 149 THR   A C   1 
ATOM   1029 O O   . THR   A 1 142 ? -0.84328  -20.95807 -24.05554 1.000 28.54485 ? 149 THR   A O   1 
ATOM   1030 C CB  . THR   A 1 142 ? 0.07922   -23.69429 -24.92380 1.000 26.94188 ? 149 THR   A CB  1 
ATOM   1031 O OG1 . THR   A 1 142 ? 0.73893   -24.89497 -24.50331 1.000 30.37635 ? 149 THR   A OG1 1 
ATOM   1032 C CG2 . THR   A 1 142 ? -0.18882  -23.75339 -26.46218 1.000 26.20562 ? 149 THR   A CG2 1 
ATOM   1033 N N   . VAL   A 1 143 ? 0.48135   -20.41074 -25.79222 1.000 22.44967 ? 150 VAL   A N   1 
ATOM   1034 C CA  . VAL   A 1 143 ? -0.20885  -19.16836 -26.13555 1.000 23.65536 ? 150 VAL   A CA  1 
ATOM   1035 C C   . VAL   A 1 143 ? -0.77464  -19.35165 -27.54585 1.000 28.04687 ? 150 VAL   A C   1 
ATOM   1036 O O   . VAL   A 1 143 ? -0.01870  -19.54901 -28.50689 1.000 26.71200 ? 150 VAL   A O   1 
ATOM   1037 C CB  . VAL   A 1 143 ? 0.72854   -17.95193 -26.05436 1.000 25.44060 ? 150 VAL   A CB  1 
ATOM   1038 C CG1 . VAL   A 1 143 ? -0.04689  -16.66473 -26.50150 1.000 26.39590 ? 150 VAL   A CG1 1 
ATOM   1039 C CG2 . VAL   A 1 143 ? 1.30654   -17.76509 -24.63200 1.000 24.12850 ? 150 VAL   A CG2 1 
ATOM   1040 N N   . ILE   A 1 144 ? -2.09772  -19.33325 -27.68024 1.000 23.27907 ? 151 ILE   A N   1 
ATOM   1041 C CA  . ILE   A 1 144 ? -2.73740  -19.42154 -28.99820 1.000 23.47007 ? 151 ILE   A CA  1 
ATOM   1042 C C   . ILE   A 1 144 ? -3.24164  -18.03070 -29.31056 1.000 24.69997 ? 151 ILE   A C   1 
ATOM   1043 O O   . ILE   A 1 144 ? -3.86978  -17.41171 -28.43944 1.000 25.14763 ? 151 ILE   A O   1 
ATOM   1044 C CB  . ILE   A 1 144 ? -3.92435  -20.39394 -28.99463 1.000 27.62609 ? 151 ILE   A CB  1 
ATOM   1045 C CG1 . ILE   A 1 144 ? -3.60021  -21.70562 -28.28744 1.000 35.68408 ? 151 ILE   A CG1 1 
ATOM   1046 C CG2 . ILE   A 1 144 ? -4.48654  -20.60208 -30.44068 1.000 32.30234 ? 151 ILE   A CG2 1 
ATOM   1047 C CD1 . ILE   A 1 144 ? -2.63652  -22.44595 -29.00275 1.000 35.50328 ? 151 ILE   A CD1 1 
ATOM   1048 N N   . THR   A 1 145 ? -3.00930  -17.53430 -30.52536 1.000 23.61225 ? 152 THR   A N   1 
ATOM   1049 C CA  . THR   A 1 145 ? -3.34652  -16.13412 -30.78349 1.000 26.69652 ? 152 THR   A CA  1 
ATOM   1050 C C   . THR   A 1 145 ? -3.77419  -15.94232 -32.23484 1.000 29.18076 ? 152 THR   A C   1 
ATOM   1051 O O   . THR   A 1 145 ? -3.33883  -16.68072 -33.13662 1.000 27.54803 ? 152 THR   A O   1 
ATOM   1052 C CB  . THR   A 1 145 ? -2.15743  -15.21865 -30.41496 1.000 25.04565 ? 152 THR   A CB  1 
ATOM   1053 O OG1 . THR   A 1 145 ? -2.55684  -13.83001 -30.35152 1.000 27.36024 ? 152 THR   A OG1 1 
ATOM   1054 C CG2 . THR   A 1 145 ? -0.93045  -15.38526 -31.39905 1.000 23.41482 ? 152 THR   A CG2 1 
ATOM   1055 N N   . LYS   A 1 146 ? -4.65782  -14.94996 -32.43726 1.000 25.44270 ? 153 LYS   A N   1 
ATOM   1056 C CA  . LYS   A 1 146 ? -5.15497  -14.55847 -33.75537 1.000 24.60593 ? 153 LYS   A CA  1 
ATOM   1057 C C   . LYS   A 1 146 ? -5.25243  -13.04455 -33.79964 1.000 28.55532 ? 153 LYS   A C   1 
ATOM   1058 O O   . LYS   A 1 146 ? -6.04619  -12.45130 -33.05784 1.000 27.75068 ? 153 LYS   A O   1 
ATOM   1059 C CB  . LYS   A 1 146 ? -6.53119  -15.19468 -34.02950 1.000 26.98678 ? 153 LYS   A CB  1 
ATOM   1060 C CG  . LYS   A 1 146 ? -7.21267  -14.83108 -35.36887 1.000 28.74028 ? 153 LYS   A CG  1 
ATOM   1061 C CD  . LYS   A 1 146 ? -6.36954  -15.33605 -36.56703 1.000 30.12816 ? 153 LYS   A CD  1 
ATOM   1062 C CE  . LYS   A 1 146 ? -7.09276  -15.01574 -37.85572 1.000 33.38478 ? 153 LYS   A CE  1 
ATOM   1063 N NZ  . LYS   A 1 146 ? -7.05202  -13.55899 -38.25485 1.000 32.44029 ? 153 LYS   A NZ  1 
ATOM   1064 N N   . HIS   A 1 147 ? -4.48609  -12.42657 -34.68873 1.000 29.19210 ? 154 HIS   A N   1 
ATOM   1065 C CA  . HIS   A 1 147 ? -4.51439  -10.98781 -34.93409 1.000 26.04524 ? 154 HIS   A CA  1 
ATOM   1066 C C   . HIS   A 1 147 ? -5.16595  -10.77025 -36.28117 1.000 29.43833 ? 154 HIS   A C   1 
ATOM   1067 O O   . HIS   A 1 147 ? -5.06622  -11.63868 -37.15279 1.000 31.99209 ? 154 HIS   A O   1 
ATOM   1068 C CB  . HIS   A 1 147 ? -3.06378  -10.44886 -34.88622 1.000 25.04915 ? 154 HIS   A CB  1 
ATOM   1069 C CG  . HIS   A 1 147 ? -2.92719  -8.96853  -35.04598 1.000 27.85197 ? 154 HIS   A CG  1 
ATOM   1070 N ND1 . HIS   A 1 147 ? -3.12534  -8.32555  -36.24541 1.000 31.05996 ? 154 HIS   A ND1 1 
ATOM   1071 C CD2 . HIS   A 1 147 ? -2.55605  -8.00263  -34.15708 1.000 26.58472 ? 154 HIS   A CD2 1 
ATOM   1072 C CE1 . HIS   A 1 147 ? -2.88422  -7.03609  -36.10349 1.000 32.95462 ? 154 HIS   A CE1 1 
ATOM   1073 N NE2 . HIS   A 1 147 ? -2.54604  -6.80798  -34.85094 1.000 29.46742 ? 154 HIS   A NE2 1 
ATOM   1074 N N   . ASN   A 1 148 ? -5.92892  -9.67077  -36.43012 1.000 28.84991 ? 155 ASN   A N   1 
ATOM   1075 C CA  . ASN   A 1 148 ? -6.64760  -9.46963  -37.67757 1.000 29.07198 ? 155 ASN   A CA  1 
ATOM   1076 C C   . ASN   A 1 148 ? -5.73408  -9.57004  -38.90285 1.000 36.31556 ? 155 ASN   A C   1 
ATOM   1077 O O   . ASN   A 1 148 ? -6.21055  -9.91252  -39.99593 1.000 36.28301 ? 155 ASN   A O   1 
ATOM   1078 C CB  . ASN   A 1 148 ? -7.33888  -8.09467  -37.71024 1.000 33.07504 ? 155 ASN   A CB  1 
ATOM   1079 C CG  . ASN   A 1 148 ? -8.58905  -8.02696  -36.86329 1.000 37.16425 ? 155 ASN   A CG  1 
ATOM   1080 O OD1 . ASN   A 1 148 ? -9.27558  -9.01692  -36.65180 1.000 37.35982 ? 155 ASN   A OD1 1 
ATOM   1081 N ND2 . ASN   A 1 148 ? -8.88109  -6.83380  -36.33803 1.000 35.92008 ? 155 ASN   A ND2 1 
ATOM   1082 N N   . ASP   A 1 149 ? -4.46304  -9.19831  -38.76555 1.000 34.07111 ? 156 ASP   A N   1 
ATOM   1083 C CA  . ASP   A 1 149 ? -3.53126  -9.11606  -39.89011 1.000 37.54565 ? 156 ASP   A CA  1 
ATOM   1084 C C   . ASP   A 1 149 ? -2.73224  -10.39741 -40.11654 1.000 42.78764 ? 156 ASP   A C   1 
ATOM   1085 O O   . ASP   A 1 149 ? -1.77701  -10.37454 -40.90583 1.000 41.19551 ? 156 ASP   A O   1 
ATOM   1086 C CB  . ASP   A 1 149 ? -2.53542  -7.96769  -39.66774 1.000 36.65441 ? 156 ASP   A CB  1 
ATOM   1087 C CG  . ASP   A 1 149 ? -3.19530  -6.59208  -39.66888 1.000 45.11471 ? 156 ASP   A CG  1 
ATOM   1088 O OD1 . ASP   A 1 149 ? -4.31766  -6.47485  -40.18434 1.000 42.91197 ? 156 ASP   A OD1 1 
ATOM   1089 O OD2 . ASP   A 1 149 ? -2.58283  -5.62509  -39.14621 1.000 41.94226 ? 156 ASP   A OD2 1 
ATOM   1090 N N   . ASP   A 1 150 ? -3.04090  -11.50151 -39.42619 1.000 33.41865 ? 157 ASP   A N   1 
ATOM   1091 C CA  . ASP   A 1 150 ? -2.20775  -12.71099 -39.56485 1.000 31.82462 ? 157 ASP   A CA  1 
ATOM   1092 C C   . ASP   A 1 150 ? -3.07643  -13.94632 -39.32345 1.000 39.86860 ? 157 ASP   A C   1 
ATOM   1093 O O   . ASP   A 1 150 ? -4.27987  -13.84470 -39.07311 1.000 36.80527 ? 157 ASP   A O   1 
ATOM   1094 C CB  . ASP   A 1 150 ? -0.98730  -12.67540 -38.60517 1.000 33.54549 ? 157 ASP   A CB  1 
ATOM   1095 C CG  . ASP   A 1 150 ? 0.22555   -13.43430 -39.13652 1.000 39.66012 ? 157 ASP   A CG  1 
ATOM   1096 O OD1 . ASP   A 1 150 ? 0.09475   -14.22839 -40.09851 1.000 39.31041 ? 157 ASP   A OD1 1 
ATOM   1097 O OD2 . ASP   A 1 150 ? 1.32720   -13.23823 -38.54182 1.000 36.70964 ? 157 ASP   A OD2 1 
ATOM   1098 N N   . GLU   A 1 151 ? -2.45578  -15.12479 -39.41382 1.000 34.07144 ? 158 GLU   A N   1 
ATOM   1099 C CA  . GLU   A 1 151 ? -3.13949  -16.39010 -39.24289 1.000 36.63929 ? 158 GLU   A CA  1 
ATOM   1100 C C   . GLU   A 1 151 ? -3.06958  -16.76371 -37.76369 1.000 30.17284 ? 158 GLU   A C   1 
ATOM   1101 O O   . GLU   A 1 151 ? -2.40187  -16.10174 -36.95355 1.000 30.93128 ? 158 GLU   A O   1 
ATOM   1102 C CB  . GLU   A 1 151 ? -2.50577  -17.47755 -40.11323 1.000 42.16650 ? 158 GLU   A CB  1 
ATOM   1103 C CG  . GLU   A 1 151 ? -2.90022  -17.45511 -41.58649 1.000 50.11530 ? 158 GLU   A CG  1 
ATOM   1104 C CD  . GLU   A 1 151 ? -4.23257  -16.73744 -41.87706 1.000 81.64579 ? 158 GLU   A CD  1 
ATOM   1105 O OE1 . GLU   A 1 151 ? -4.22400  -15.79840 -42.70946 1.000 80.13068 ? 158 GLU   A OE1 1 
ATOM   1106 O OE2 . GLU   A 1 151 ? -5.29193  -17.11188 -41.30919 1.000 74.15170 ? 158 GLU   A OE2 1 
ATOM   1107 N N   . GLN   A 1 152 ? -3.70611  -17.87307 -37.40425 1.000 32.28564 ? 159 GLN   A N   1 
ATOM   1108 C CA  . GLN   A 1 152 ? -3.74586  -18.30096 -36.01104 1.000 28.87741 ? 159 GLN   A CA  1 
ATOM   1109 C C   . GLN   A 1 152 ? -2.48553  -19.11503 -35.70563 1.000 28.09370 ? 159 GLN   A C   1 
ATOM   1110 O O   . GLN   A 1 152 ? -2.15447  -20.03853 -36.45410 1.000 32.52812 ? 159 GLN   A O   1 
ATOM   1111 C CB  . GLN   A 1 152 ? -5.00855  -19.12201 -35.72205 1.000 31.29064 ? 159 GLN   A CB  1 
ATOM   1112 C CG  . GLN   A 1 152 ? -5.20857  -19.46338 -34.18227 1.000 30.64164 ? 159 GLN   A CG  1 
ATOM   1113 C CD  . GLN   A 1 152 ? -6.63340  -19.92339 -33.90320 1.000 35.36296 ? 159 GLN   A CD  1 
ATOM   1114 O OE1 . GLN   A 1 152 ? -7.55234  -19.23095 -34.28571 1.000 41.26041 ? 159 GLN   A OE1 1 
ATOM   1115 N NE2 . GLN   A 1 152 ? -6.81929  -21.11306 -33.31360 1.000 37.15752 ? 159 GLN   A NE2 1 
ATOM   1116 N N   . TYR   A 1 153 ? -1.81017  -18.77912 -34.62555 1.000 26.19494 ? 160 TYR   A N   1 
ATOM   1117 C CA  . TYR   A 1 153 ? -0.52205  -19.38913 -34.30225 1.000 26.40172 ? 160 TYR   A CA  1 
ATOM   1118 C C   . TYR   A 1 153 ? -0.54023  -19.88066 -32.86205 1.000 29.32911 ? 160 TYR   A C   1 
ATOM   1119 O O   . TYR   A 1 153 ? -1.27385  -19.34251 -32.02098 1.000 26.81219 ? 160 TYR   A O   1 
ATOM   1120 C CB  . TYR   A 1 153 ? 0.62637   -18.37848 -34.47627 1.000 27.98133 ? 160 TYR   A CB  1 
ATOM   1121 C CG  . TYR   A 1 153 ? 1.04397   -18.23496 -35.91238 1.000 32.31000 ? 160 TYR   A CG  1 
ATOM   1122 C CD1 . TYR   A 1 153 ? 1.95840   -19.12074 -36.45921 1.000 34.06234 ? 160 TYR   A CD1 1 
ATOM   1123 C CD2 . TYR   A 1 153 ? 0.52789   -17.21395 -36.74159 1.000 33.45165 ? 160 TYR   A CD2 1 
ATOM   1124 C CE1 . TYR   A 1 153 ? 2.35449   -19.01763 -37.77436 1.000 36.19403 ? 160 TYR   A CE1 1 
ATOM   1125 C CE2 . TYR   A 1 153 ? 0.92177   -17.12224 -38.09518 1.000 37.42374 ? 160 TYR   A CE2 1 
ATOM   1126 C CZ  . TYR   A 1 153 ? 1.82222   -18.04072 -38.57704 1.000 39.72261 ? 160 TYR   A CZ  1 
ATOM   1127 O OH  . TYR   A 1 153 ? 2.28119   -18.00391 -39.84475 1.000 46.59515 ? 160 TYR   A OH  1 
ATOM   1128 N N   . ALA   A 1 154 ? 0.33389   -20.85324 -32.57241 1.000 27.95339 ? 161 ALA   A N   1 
ATOM   1129 C CA  . ALA   A 1 154 ? 0.55974   -21.35782 -31.22120 1.000 22.95713 ? 161 ALA   A CA  1 
ATOM   1130 C C   . ALA   A 1 154 ? 2.02406   -21.16268 -30.87349 1.000 23.29445 ? 161 ALA   A C   1 
ATOM   1131 O O   . ALA   A 1 154 ? 2.90081   -21.65164 -31.60986 1.000 27.00461 ? 161 ALA   A O   1 
ATOM   1132 C CB  . ALA   A 1 154 ? 0.21653   -22.85100 -31.12917 1.000 27.77196 ? 161 ALA   A CB  1 
ATOM   1133 N N   . TRP   A 1 155 ? 2.26453   -20.49363 -29.76199 1.000 23.98286 ? 162 TRP   A N   1 
ATOM   1134 C CA  . TRP   A 1 155 ? 3.57352   -20.40361 -29.11799 1.000 25.57427 ? 162 TRP   A CA  1 
ATOM   1135 C C   . TRP   A 1 155 ? 3.59714   -21.34806 -27.92032 1.000 26.89629 ? 162 TRP   A C   1 
ATOM   1136 O O   . TRP   A 1 155 ? 2.59330   -21.50484 -27.22019 1.000 24.83830 ? 162 TRP   A O   1 
ATOM   1137 C CB  . TRP   A 1 155 ? 3.81927   -18.94426 -28.69375 1.000 24.10809 ? 162 TRP   A CB  1 
ATOM   1138 C CG  . TRP   A 1 155 ? 5.04531   -18.54008 -27.89723 1.000 22.73360 ? 162 TRP   A CG  1 
ATOM   1139 C CD1 . TRP   A 1 155 ? 6.12241   -17.84143 -28.37701 1.000 21.70841 ? 162 TRP   A CD1 1 
ATOM   1140 C CD2 . TRP   A 1 155 ? 5.30123   -18.76393 -26.50539 1.000 22.93837 ? 162 TRP   A CD2 1 
ATOM   1141 N NE1 . TRP   A 1 155 ? 7.00399   -17.60334 -27.37097 1.000 22.22193 ? 162 TRP   A NE1 1 
ATOM   1142 C CE2 . TRP   A 1 155 ? 6.53211   -18.14795 -26.20970 1.000 22.69551 ? 162 TRP   A CE2 1 
ATOM   1143 C CE3 . TRP   A 1 155 ? 4.57901   -19.37725 -25.45858 1.000 22.94095 ? 162 TRP   A CE3 1 
ATOM   1144 C CZ2 . TRP   A 1 155 ? 7.10528   -18.16424 -24.93667 1.000 24.51505 ? 162 TRP   A CZ2 1 
ATOM   1145 C CZ3 . TRP   A 1 155 ? 5.14507   -19.36402 -24.16748 1.000 21.41791 ? 162 TRP   A CZ3 1 
ATOM   1146 C CH2 . TRP   A 1 155 ? 6.38884   -18.75170 -23.91872 1.000 22.98951 ? 162 TRP   A CH2 1 
ATOM   1147 N N   . GLU   A 1 156 ? 4.75176   -21.94461 -27.64231 1.000 22.82148 ? 163 GLU   A N   1 
ATOM   1148 C CA  . GLU   A 1 156 ? 4.81143   -22.80090 -26.47223 1.000 23.91026 ? 163 GLU   A CA  1 
ATOM   1149 C C   . GLU   A 1 156 ? 6.21381   -22.79936 -25.87375 1.000 22.40953 ? 163 GLU   A C   1 
ATOM   1150 O O   . GLU   A 1 156 ? 7.20998   -22.79866 -26.60650 1.000 24.54435 ? 163 GLU   A O   1 
ATOM   1151 C CB  . GLU   A 1 156 ? 4.42156   -24.21043 -26.84602 1.000 27.29861 ? 163 GLU   A CB  1 
ATOM   1152 C CG  . GLU   A 1 156 ? 4.11942   -25.13756 -25.71078 1.000 32.57832 ? 163 GLU   A CG  1 
ATOM   1153 C CD  . GLU   A 1 156 ? 3.42929   -26.39771 -26.22808 1.000 46.16150 ? 163 GLU   A CD  1 
ATOM   1154 O OE1 . GLU   A 1 156 ? 4.12879   -27.23608 -26.84910 1.000 40.19973 ? 163 GLU   A OE1 1 
ATOM   1155 O OE2 . GLU   A 1 156 ? 2.18484   -26.55565 -26.01702 1.000 45.29082 ? 163 GLU   A OE2 1 
ATOM   1156 N N   . SER   A 1 157 ? 6.27380   -22.83690 -24.54106 1.000 22.65833 ? 164 SER   A N   1 
ATOM   1157 C CA  . SER   A 1 157 ? 7.58212   -23.02834 -23.90987 1.000 22.32055 ? 164 SER   A CA  1 
ATOM   1158 C C   . SER   A 1 157 ? 7.45529   -23.70855 -22.55521 1.000 22.92011 ? 164 SER   A C   1 
ATOM   1159 O O   . SER   A 1 157 ? 6.55630   -23.39713 -21.75363 1.000 22.65840 ? 164 SER   A O   1 
ATOM   1160 C CB  . SER   A 1 157 ? 8.32161   -21.70802 -23.72389 1.000 23.91607 ? 164 SER   A CB  1 
ATOM   1161 O OG  . SER   A 1 157 ? 9.61316   -21.97442 -23.12818 1.000 25.19039 ? 164 SER   A OG  1 
ATOM   1162 N N   . SER   A 1 158 ? 8.40031   -24.60572 -22.28931 1.000 23.96129 ? 165 SER   A N   1 
ATOM   1163 C CA  . SER   A 1 158 ? 8.59411   -25.16136 -20.95576 1.000 25.42563 ? 165 SER   A CA  1 
ATOM   1164 C C   . SER   A 1 158 ? 9.85259   -24.57770 -20.32002 1.000 26.53794 ? 165 SER   A C   1 
ATOM   1165 O O   . SER   A 1 158 ? 10.45849  -25.22332 -19.45971 1.000 31.40198 ? 165 SER   A O   1 
ATOM   1166 C CB  . SER   A 1 158 ? 8.70711   -26.68267 -21.00736 1.000 27.81590 ? 165 SER   A CB  1 
ATOM   1167 O OG  . SER   A 1 158 ? 7.50043   -27.33160 -21.43098 1.000 30.93445 ? 165 SER   A OG  1 
ATOM   1168 N N   . ALA   A 1 159 ? 10.21321  -23.35599 -20.71499 1.000 24.63695 ? 166 ALA   A N   1 
ATOM   1169 C CA  . ALA   A 1 159 ? 11.46564  -22.66282 -20.31553 1.000 29.25275 ? 166 ALA   A CA  1 
ATOM   1170 C C   . ALA   A 1 159 ? 12.63579  -23.54085 -20.78276 1.000 28.09781 ? 166 ALA   A C   1 
ATOM   1171 O O   . ALA   A 1 159 ? 12.60654  -24.10393 -21.89253 1.000 32.18719 ? 166 ALA   A O   1 
ATOM   1172 C CB  . ALA   A 1 159 ? 11.39885  -22.34611 -18.84297 1.000 29.64714 ? 166 ALA   A CB  1 
ATOM   1173 N N   . GLY   A 1 160 ? 13.72242  -23.64263 -20.02943 1.000 32.82914 ? 167 GLY   A N   1 
ATOM   1174 C CA  . GLY   A 1 160 ? 14.84746  -24.36749 -20.59549 1.000 34.49141 ? 167 GLY   A CA  1 
ATOM   1175 C C   . GLY   A 1 160 ? 15.53243  -23.68397 -21.77037 1.000 34.35516 ? 167 GLY   A C   1 
ATOM   1176 O O   . GLY   A 1 160 ? 16.36673  -24.30322 -22.43359 1.000 32.47204 ? 167 GLY   A O   1 
ATOM   1177 N N   . GLY   A 1 161 ? 15.25245  -22.40996 -22.01294 1.000 27.79139 ? 168 GLY   A N   1 
ATOM   1178 C CA  . GLY   A 1 161 ? 15.99573  -21.68373 -23.02249 1.000 27.96931 ? 168 GLY   A CA  1 
ATOM   1179 C C   . GLY   A 1 161 ? 15.37654  -21.63935 -24.40524 1.000 25.01629 ? 168 GLY   A C   1 
ATOM   1180 O O   . GLY   A 1 161 ? 15.94308  -20.98152 -25.29221 1.000 26.59131 ? 168 GLY   A O   1 
ATOM   1181 N N   . SER   A 1 162 ? 14.25353  -22.30666 -24.63868 1.000 23.74899 ? 169 SER   A N   1 
ATOM   1182 C CA  . SER   A 1 162 ? 13.71096  -22.32381 -25.99962 1.000 23.99712 ? 169 SER   A CA  1 
ATOM   1183 C C   . SER   A 1 162 ? 12.19568  -22.24709 -25.98598 1.000 24.85703 ? 169 SER   A C   1 
ATOM   1184 O O   . SER   A 1 162 ? 11.55330  -22.56140 -24.98835 1.000 25.43690 ? 169 SER   A O   1 
ATOM   1185 C CB  . SER   A 1 162 ? 14.12463  -23.57002 -26.79133 1.000 30.21309 ? 169 SER   A CB  1 
ATOM   1186 O OG  . SER   A 1 162 ? 13.49075  -24.72210 -26.24716 1.000 28.27827 ? 169 SER   A OG  1 
ATOM   1187 N N   . PHE   A 1 163 ? 11.65841  -21.82334 -27.12391 1.000 23.70139 ? 170 PHE   A N   1 
ATOM   1188 C CA  . PHE   A 1 163 ? 10.21071  -21.78004 -27.34325 1.000 20.81201 ? 170 PHE   A CA  1 
ATOM   1189 C C   . PHE   A 1 163 ? 9.95001   -22.22687 -28.76752 1.000 22.47259 ? 170 PHE   A C   1 
ATOM   1190 O O   . PHE   A 1 163 ? 10.84889  -22.23152 -29.61884 1.000 26.18448 ? 170 PHE   A O   1 
ATOM   1191 C CB  . PHE   A 1 163 ? 9.57561   -20.37441 -27.09622 1.000 22.93252 ? 170 PHE   A CB  1 
ATOM   1192 C CG  . PHE   A 1 163 ? 10.06295  -19.27397 -28.03269 1.000 22.62212 ? 170 PHE   A CG  1 
ATOM   1193 C CD1 . PHE   A 1 163 ? 9.39175   -18.98181 -29.21132 1.000 22.61916 ? 170 PHE   A CD1 1 
ATOM   1194 C CD2 . PHE   A 1 163 ? 11.17792  -18.48907 -27.66363 1.000 25.97727 ? 170 PHE   A CD2 1 
ATOM   1195 C CE1 . PHE   A 1 163 ? 9.84205   -17.94971 -30.03764 1.000 23.88026 ? 170 PHE   A CE1 1 
ATOM   1196 C CE2 . PHE   A 1 163 ? 11.64192  -17.44266 -28.49333 1.000 25.72101 ? 170 PHE   A CE2 1 
ATOM   1197 C CZ  . PHE   A 1 163 ? 10.93872  -17.16286 -29.68802 1.000 26.75566 ? 170 PHE   A CZ  1 
ATOM   1198 N N   . THR   A 1 164 ? 8.69783   -22.64203 -29.02738 1.000 23.36081 ? 171 THR   A N   1 
ATOM   1199 C CA  . THR   A 1 164 ? 8.33285   -23.06602 -30.36393 1.000 23.09543 ? 171 THR   A CA  1 
ATOM   1200 C C   . THR   A 1 164 ? 7.17136   -22.22825 -30.85883 1.000 22.77075 ? 171 THR   A C   1 
ATOM   1201 O O   . THR   A 1 164 ? 6.39131   -21.68265 -30.05349 1.000 24.66456 ? 171 THR   A O   1 
ATOM   1202 C CB  . THR   A 1 164 ? 7.94663   -24.57575 -30.45302 1.000 27.65562 ? 171 THR   A CB  1 
ATOM   1203 O OG1 . THR   A 1 164 ? 6.80203   -24.78799 -29.63285 1.000 28.55978 ? 171 THR   A OG1 1 
ATOM   1204 C CG2 . THR   A 1 164 ? 9.05386   -25.52047 -30.00835 1.000 27.87763 ? 171 THR   A CG2 1 
ATOM   1205 N N   . VAL   A 1 165 ? 7.10997   -22.09153 -32.17944 1.000 25.26033 ? 172 VAL   A N   1 
ATOM   1206 C CA  . VAL   A 1 165 ? 5.97660   -21.43239 -32.83670 1.000 27.33404 ? 172 VAL   A CA  1 
ATOM   1207 C C   . VAL   A 1 165 ? 5.51810   -22.32057 -33.98726 1.000 29.84683 ? 172 VAL   A C   1 
ATOM   1208 O O   . VAL   A 1 165 ? 6.33963   -22.82445 -34.76453 1.000 29.09650 ? 172 VAL   A O   1 
ATOM   1209 C CB  . VAL   A 1 165 ? 6.34581   -20.01777 -33.33657 1.000 28.16989 ? 172 VAL   A CB  1 
ATOM   1210 C CG1 . VAL   A 1 165 ? 5.14237   -19.36649 -34.05816 1.000 27.91986 ? 172 VAL   A CG1 1 
ATOM   1211 C CG2 . VAL   A 1 165 ? 6.74878   -19.14719 -32.19138 1.000 28.44176 ? 172 VAL   A CG2 1 
ATOM   1212 N N   . ARG   A 1 166 ? 4.20290   -22.52790 -34.10222 1.000 29.70176 ? 173 ARG   A N   1 
ATOM   1213 C CA  . ARG   A 1 166 ? 3.64768   -23.30339 -35.19807 1.000 29.62235 ? 173 ARG   A CA  1 
ATOM   1214 C C   . ARG   A 1 166 ? 2.29393   -22.71517 -35.58651 1.000 29.00190 ? 173 ARG   A C   1 
ATOM   1215 O O   . ARG   A 1 166 ? 1.64908   -22.06947 -34.75808 1.000 29.32009 ? 173 ARG   A O   1 
ATOM   1216 C CB  . ARG   A 1 166 ? 3.46790   -24.80733 -34.86391 1.000 33.79435 ? 173 ARG   A CB  1 
ATOM   1217 C CG  . ARG   A 1 166 ? 2.44988   -25.11203 -33.73478 1.000 36.18462 ? 173 ARG   A CG  1 
ATOM   1218 C CD  . ARG   A 1 166 ? 2.61788   -26.54861 -33.29996 1.000 45.64942 ? 173 ARG   A CD  1 
ATOM   1219 N NE  . ARG   A 1 166 ? 3.73529   -26.58533 -32.34566 1.000 51.42031 ? 173 ARG   A NE  1 
ATOM   1220 C CZ  . ARG   A 1 166 ? 4.21545   -27.67714 -31.75419 1.000 58.33782 ? 173 ARG   A CZ  1 
ATOM   1221 N NH1 . ARG   A 1 166 ? 3.71010   -28.87508 -31.99501 1.000 55.04972 ? 173 ARG   A NH1 1 
ATOM   1222 N NH2 . ARG   A 1 166 ? 5.27380   -27.56951 -30.94686 1.000 47.69192 ? 173 ARG   A NH2 1 
ATOM   1223 N N   . THR   A 1 167 ? 1.88138   -22.95870 -36.84133 1.000 30.96096 ? 174 THR   A N   1 
ATOM   1224 C CA  . THR   A 1 167 ? 0.48155   -22.67929 -37.19400 1.000 31.55747 ? 174 THR   A CA  1 
ATOM   1225 C C   . THR   A 1 167 ? -0.44901  -23.51900 -36.33389 1.000 38.91458 ? 174 THR   A C   1 
ATOM   1226 O O   . THR   A 1 167 ? -0.18651  -24.68948 -36.07334 1.000 42.20812 ? 174 THR   A O   1 
ATOM   1227 C CB  . THR   A 1 167 ? 0.22983   -22.94958 -38.68249 1.000 42.23144 ? 174 THR   A CB  1 
ATOM   1228 O OG1 . THR   A 1 167 ? 1.05915   -22.07305 -39.42839 1.000 44.88157 ? 174 THR   A OG1 1 
ATOM   1229 C CG2 . THR   A 1 167 ? -1.17421  -22.58741 -39.01348 1.000 46.80909 ? 174 THR   A CG2 1 
ATOM   1230 N N   . ASP   A 1 168 ? -1.56095  -22.92685 -35.89476 1.000 33.07324 ? 175 ASP   A N   1 
ATOM   1231 C CA  . ASP   A 1 168 ? -2.49238  -23.65219 -35.05788 1.000 36.38526 ? 175 ASP   A CA  1 
ATOM   1232 C C   . ASP   A 1 168 ? -3.66380  -24.13047 -35.90363 1.000 45.87677 ? 175 ASP   A C   1 
ATOM   1233 O O   . ASP   A 1 168 ? -4.38805  -23.30934 -36.47271 1.000 49.79193 ? 175 ASP   A O   1 
ATOM   1234 C CB  . ASP   A 1 168 ? -2.99372  -22.75843 -33.93383 1.000 33.38131 ? 175 ASP   A CB  1 
ATOM   1235 C CG  . ASP   A 1 168 ? -3.87363  -23.50949 -32.94592 1.000 52.13646 ? 175 ASP   A CG  1 
ATOM   1236 O OD1 . ASP   A 1 168 ? -3.50954  -24.64083 -32.54739 1.000 54.32628 ? 175 ASP   A OD1 1 
ATOM   1237 O OD2 . ASP   A 1 168 ? -4.97361  -23.00060 -32.63623 1.000 44.31581 ? 175 ASP   A OD2 1 
ATOM   1238 N N   . THR   A 1 169 ? -3.83761  -25.45145 -35.97214 1.000 53.36326 ? 176 THR   A N   1 
ATOM   1239 C CA  . THR   A 1 169 ? -4.95418  -26.13041 -36.61787 1.000 77.24621 ? 176 THR   A CA  1 
ATOM   1240 C C   . THR   A 1 169 ? -6.15082  -26.31931 -35.69985 1.000 62.45437 ? 176 THR   A C   1 
ATOM   1241 O O   . THR   A 1 169 ? -7.18946  -26.80535 -36.16070 1.000 58.01581 ? 176 THR   A O   1 
ATOM   1242 C CB  . THR   A 1 169 ? -4.50241  -27.50265 -37.13377 1.000 71.74197 ? 176 THR   A CB  1 
ATOM   1243 O OG1 . THR   A 1 169 ? -3.87492  -28.22755 -36.05856 1.000 70.42983 ? 176 THR   A OG1 1 
ATOM   1244 C CG2 . THR   A 1 169 ? -3.55330  -27.34950 -38.31643 1.000 64.73557 ? 176 THR   A CG2 1 
ATOM   1245 N N   . GLY   A 1 170 ? -6.02213  -25.95528 -34.42585 1.000 63.35669 ? 177 GLY   A N   1 
ATOM   1246 C CA  . GLY   A 1 170 ? -7.09500  -26.07346 -33.46222 1.000 61.49414 ? 177 GLY   A CA  1 
ATOM   1247 C C   . GLY   A 1 170 ? -8.33084  -25.24968 -33.76469 1.000 54.23467 ? 177 GLY   A C   1 
ATOM   1248 O O   . GLY   A 1 170 ? -8.48277  -24.67658 -34.84869 1.000 57.33293 ? 177 GLY   A O   1 
ATOM   1249 N N   . GLU   A 1 171 ? -9.23409  -25.21914 -32.79767 1.000 60.23839 ? 178 GLU   A N   1 
ATOM   1250 C CA  . GLU   A 1 171 ? -10.46175 -24.44754 -32.88196 1.000 60.05180 ? 178 GLU   A CA  1 
ATOM   1251 C C   . GLU   A 1 171 ? -10.17130 -23.00273 -33.27453 1.000 52.24537 ? 178 GLU   A C   1 
ATOM   1252 O O   . GLU   A 1 171 ? -9.46285  -22.31327 -32.53277 1.000 44.75401 ? 178 GLU   A O   1 
ATOM   1253 C CB  . GLU   A 1 171 ? -11.13916 -24.50088 -31.51448 1.000 62.51683 ? 178 GLU   A CB  1 
ATOM   1254 C CG  . GLU   A 1 171 ? -12.59054 -24.14876 -31.54396 1.000 61.48499 ? 178 GLU   A CG  1 
ATOM   1255 C CD  . GLU   A 1 171 ? -13.33726 -25.07494 -32.47235 1.000 69.26149 ? 178 GLU   A CD  1 
ATOM   1256 O OE1 . GLU   A 1 171 ? -13.42515 -26.27748 -32.12683 1.000 53.22754 ? 178 GLU   A OE1 1 
ATOM   1257 O OE2 . GLU   A 1 171 ? -13.79471 -24.61131 -33.55229 1.000 66.25111 ? 178 GLU   A OE2 1 
ATOM   1258 N N   . PRO   A 1 172 ? -10.66589 -22.51373 -34.41031 1.000 49.30041 ? 179 PRO   A N   1 
ATOM   1259 C CA  . PRO   A 1 172 ? -10.43686 -21.10040 -34.76710 1.000 48.25116 ? 179 PRO   A CA  1 
ATOM   1260 C C   . PRO   A 1 172 ? -10.99244 -20.15090 -33.71230 1.000 49.81816 ? 179 PRO   A C   1 
ATOM   1261 O O   . PRO   A 1 172 ? -12.07708 -20.37538 -33.16831 1.000 57.76396 ? 179 PRO   A O   1 
ATOM   1262 C CB  . PRO   A 1 172 ? -11.17007 -20.93161 -36.10422 1.000 52.25705 ? 179 PRO   A CB  1 
ATOM   1263 C CG  . PRO   A 1 172 ? -11.72095 -22.27697 -36.48432 1.000 53.97945 ? 179 PRO   A CG  1 
ATOM   1264 C CD  . PRO   A 1 172 ? -11.32516 -23.29406 -35.47248 1.000 57.00372 ? 179 PRO   A CD  1 
ATOM   1265 N N   . MET   A 1 173 ? -10.25606 -19.05801 -33.44648 1.000 40.14625 ? 180 MET   A N   1 
ATOM   1266 C CA  . MET   A 1 173 ? -10.58315 -18.18866 -32.32256 1.000 39.95721 ? 180 MET   A CA  1 
ATOM   1267 C C   . MET   A 1 173 ? -11.27943 -16.88745 -32.69389 1.000 48.28639 ? 180 MET   A C   1 
ATOM   1268 O O   . MET   A 1 173 ? -11.78767 -16.20929 -31.79756 1.000 56.89047 ? 180 MET   A O   1 
ATOM   1269 C CB  . MET   A 1 173 ? -9.34998  -17.76255 -31.52079 1.000 38.61019 ? 180 MET   A CB  1 
ATOM   1270 C CG  . MET   A 1 173 ? -8.60953  -18.81144 -30.79425 1.000 52.09064 ? 180 MET   A CG  1 
ATOM   1271 S SD  . MET   A 1 173 ? -7.03850  -18.04322 -30.32437 1.000 46.78682 ? 180 MET   A SD  1 
ATOM   1272 C CE  . MET   A 1 173 ? -7.61113  -16.55878 -29.54486 1.000 40.29321 ? 180 MET   A CE  1 
ATOM   1273 N N   . GLY   A 1 174 ? -11.18243 -16.44094 -33.92215 1.000 42.09545 ? 181 GLY   A N   1 
ATOM   1274 C CA  . GLY   A 1 174 ? -11.80630 -15.17967 -34.27443 1.000 33.56422 ? 181 GLY   A CA  1 
ATOM   1275 C C   . GLY   A 1 174 ? -10.81176 -14.04680 -34.15228 1.000 36.72853 ? 181 GLY   A C   1 
ATOM   1276 O O   . GLY   A 1 174 ? -10.32059 -13.53131 -35.16541 1.000 37.15307 ? 181 GLY   A O   1 
ATOM   1277 N N   . ARG   A 1 175 ? -10.48744 -13.68100 -32.90949 1.000 29.96709 ? 182 ARG   A N   1 
ATOM   1278 C CA  . ARG   A 1 175 ? -9.45969  -12.68097 -32.63534 1.000 26.51658 ? 182 ARG   A CA  1 
ATOM   1279 C C   . ARG   A 1 175 ? -9.15081  -12.71952 -31.14090 1.000 25.88288 ? 182 ARG   A C   1 
ATOM   1280 O O   . ARG   A 1 175 ? -10.08031 -12.84408 -30.32950 1.000 30.09801 ? 182 ARG   A O   1 
ATOM   1281 C CB  . ARG   A 1 175 ? -9.93836  -11.25819 -33.04268 1.000 28.93679 ? 182 ARG   A CB  1 
ATOM   1282 C CG  . ARG   A 1 175 ? -8.84157  -10.14608 -32.79200 1.000 27.00701 ? 182 ARG   A CG  1 
ATOM   1283 C CD  . ARG   A 1 175 ? -9.49633  -8.75281  -32.72905 1.000 28.41309 ? 182 ARG   A CD  1 
ATOM   1284 N NE  . ARG   A 1 175 ? -10.38091 -8.66274  -31.56063 1.000 29.27447 ? 182 ARG   A NE  1 
ATOM   1285 C CZ  . ARG   A 1 175 ? -11.69636 -8.55464  -31.63067 1.000 27.87791 ? 182 ARG   A CZ  1 
ATOM   1286 N NH1 . ARG   A 1 175 ? -12.34187 -8.51757  -32.80905 1.000 29.06206 ? 182 ARG   A NH1 1 
ATOM   1287 N NH2 . ARG   A 1 175 ? -12.41437 -8.45302  -30.49430 1.000 28.77895 ? 182 ARG   A NH2 1 
ATOM   1288 N N   . GLY   A 1 176 ? -7.86978  -12.61229 -30.78299 1.000 24.69553 ? 183 GLY   A N   1 
ATOM   1289 C CA  . GLY   A 1 176 ? -7.52000  -12.51758 -29.38139 1.000 24.01488 ? 183 GLY   A CA  1 
ATOM   1290 C C   . GLY   A 1 176 ? -6.41779  -13.49341 -29.00941 1.000 26.57640 ? 183 GLY   A C   1 
ATOM   1291 O O   . GLY   A 1 176 ? -5.66995  -13.96120 -29.87546 1.000 26.23352 ? 183 GLY   A O   1 
ATOM   1292 N N   . THR   A 1 177 ? -6.32329  -13.77858 -27.71884 1.000 23.34621 ? 184 THR   A N   1 
ATOM   1293 C CA  . THR   A 1 177 ? -5.23612  -14.58508 -27.20799 1.000 21.99940 ? 184 THR   A CA  1 
ATOM   1294 C C   . THR   A 1 177 ? -5.75316  -15.53654 -26.15447 1.000 28.75652 ? 184 THR   A C   1 
ATOM   1295 O O   . THR   A 1 177 ? -6.62489  -15.18746 -25.34280 1.000 25.52391 ? 184 THR   A O   1 
ATOM   1296 C CB  . THR   A 1 177 ? -4.09648  -13.66861 -26.64033 1.000 24.78173 ? 184 THR   A CB  1 
ATOM   1297 O OG1 . THR   A 1 177 ? -3.58461  -12.87696 -27.70686 1.000 26.62309 ? 184 THR   A OG1 1 
ATOM   1298 C CG2 . THR   A 1 177 ? -2.94321  -14.44269 -25.95544 1.000 25.81189 ? 184 THR   A CG2 1 
ATOM   1299 N N   . LYS   A 1 178 ? -5.21387  -16.74672 -26.16415 1.000 24.12743 ? 185 LYS   A N   1 
ATOM   1300 C CA  . LYS   A 1 178 ? -5.52350  -17.72929 -25.12286 1.000 24.25725 ? 185 LYS   A CA  1 
ATOM   1301 C C   . LYS   A 1 178 ? -4.22751  -18.17435 -24.48227 1.000 25.00500 ? 185 LYS   A C   1 
ATOM   1302 O O   . LYS   A 1 178 ? -3.35670  -18.65954 -25.20079 1.000 25.97211 ? 185 LYS   A O   1 
ATOM   1303 C CB  . LYS   A 1 178 ? -6.20539  -18.92208 -25.79942 1.000 30.03503 ? 185 LYS   A CB  1 
ATOM   1304 C CG  . LYS   A 1 178 ? -6.61477  -20.05919 -24.98958 1.000 38.12950 ? 185 LYS   A CG  1 
ATOM   1305 C CD  . LYS   A 1 178 ? -7.64081  -20.97346 -25.73341 1.000 41.04364 ? 185 LYS   A CD  1 
ATOM   1306 C CE  . LYS   A 1 178 ? -8.35398  -20.21891 -26.82976 1.000 47.91749 ? 185 LYS   A CE  1 
ATOM   1307 N NZ  . LYS   A 1 178 ? -9.34293  -21.05468 -27.61821 1.000 62.87056 ? 185 LYS   A NZ  1 
ATOM   1308 N N   . VAL   A 1 179 ? -4.07248  -17.95187 -23.18009 1.000 23.26423 ? 186 VAL   A N   1 
ATOM   1309 C CA  . VAL   A 1 179 ? -2.86882  -18.38923 -22.46110 1.000 20.55602 ? 186 VAL   A CA  1 
ATOM   1310 C C   . VAL   A 1 179 ? -3.25732  -19.62491 -21.68207 1.000 26.42585 ? 186 VAL   A C   1 
ATOM   1311 O O   . VAL   A 1 179 ? -4.09847  -19.55802 -20.77326 1.000 26.15833 ? 186 VAL   A O   1 
ATOM   1312 C CB  . VAL   A 1 179 ? -2.35000  -17.30510 -21.50165 1.000 21.26185 ? 186 VAL   A CB  1 
ATOM   1313 C CG1 . VAL   A 1 179 ? -1.12731  -17.82099 -20.70828 1.000 22.56856 ? 186 VAL   A CG1 1 
ATOM   1314 C CG2 . VAL   A 1 179 ? -1.92342  -16.05925 -22.26201 1.000 23.48717 ? 186 VAL   A CG2 1 
ATOM   1315 N N   . ILE   A 1 180 ? -2.62676  -20.74127 -22.00174 1.000 23.50804 ? 187 ILE   A N   1 
ATOM   1316 C CA  . ILE   A 1 180 ? -2.94533  -22.04563 -21.41432 1.000 23.70666 ? 187 ILE   A CA  1 
ATOM   1317 C C   . ILE   A 1 180 ? -1.81925  -22.37600 -20.44658 1.000 22.13075 ? 187 ILE   A C   1 
ATOM   1318 O O   . ILE   A 1 180 ? -0.68061  -22.61547 -20.87003 1.000 23.92045 ? 187 ILE   A O   1 
ATOM   1319 C CB  . ILE   A 1 180 ? -3.10809  -23.16108 -22.46063 1.000 25.63497 ? 187 ILE   A CB  1 
ATOM   1320 C CG1 . ILE   A 1 180 ? -4.18632  -22.79764 -23.49192 1.000 23.90285 ? 187 ILE   A CG1 1 
ATOM   1321 C CG2 . ILE   A 1 180 ? -3.44916  -24.52498 -21.75257 1.000 25.41168 ? 187 ILE   A CG2 1 
ATOM   1322 C CD1 . ILE   A 1 180 ? -4.21045  -23.70777 -24.68428 1.000 27.87162 ? 187 ILE   A CD1 1 
ATOM   1323 N N   . LEU   A 1 181 ? -2.12149  -22.36552 -19.15649 1.000 22.01757 ? 188 LEU   A N   1 
ATOM   1324 C CA  . LEU   A 1 181 ? -1.13423  -22.66227 -18.12025 1.000 19.07708 ? 188 LEU   A CA  1 
ATOM   1325 C C   . LEU   A 1 181 ? -1.24177  -24.14485 -17.76329 1.000 23.04455 ? 188 LEU   A C   1 
ATOM   1326 O O   . LEU   A 1 181 ? -2.25337  -24.57697 -17.17784 1.000 24.87704 ? 188 LEU   A O   1 
ATOM   1327 C CB  . LEU   A 1 181 ? -1.37736  -21.80136 -16.88486 1.000 23.05476 ? 188 LEU   A CB  1 
ATOM   1328 C CG  . LEU   A 1 181 ? -1.45598  -20.30495 -17.14986 1.000 24.70933 ? 188 LEU   A CG  1 
ATOM   1329 C CD1 . LEU   A 1 181 ? -1.85824  -19.66138 -15.78815 1.000 24.91752 ? 188 LEU   A CD1 1 
ATOM   1330 C CD2 . LEU   A 1 181 ? -0.12987  -19.80246 -17.63982 1.000 25.30517 ? 188 LEU   A CD2 1 
ATOM   1331 N N   . HIS   A 1 182 ? -0.18279  -24.92335 -18.07546 1.000 23.90225 ? 189 HIS   A N   1 
ATOM   1332 C CA  . HIS   A 1 182 ? -0.09738  -26.34104 -17.68029 1.000 25.25466 ? 189 HIS   A CA  1 
ATOM   1333 C C   . HIS   A 1 182 ? 0.52038   -26.34038 -16.28912 1.000 26.66323 ? 189 HIS   A C   1 
ATOM   1334 O O   . HIS   A 1 182 ? 1.72033   -26.11652 -16.13232 1.000 26.99085 ? 189 HIS   A O   1 
ATOM   1335 C CB  . HIS   A 1 182 ? 0.71675   -27.15951 -18.69899 1.000 24.76006 ? 189 HIS   A CB  1 
ATOM   1336 C CG  . HIS   A 1 182 ? 0.23105   -27.01430 -20.10799 1.000 28.19679 ? 189 HIS   A CG  1 
ATOM   1337 N ND1 . HIS   A 1 182 ? -0.54817  -27.97307 -20.73606 1.000 36.86719 ? 189 HIS   A ND1 1 
ATOM   1338 C CD2 . HIS   A 1 182 ? 0.35987   -25.99248 -20.99728 1.000 28.06865 ? 189 HIS   A CD2 1 
ATOM   1339 C CE1 . HIS   A 1 182 ? -0.83067  -27.56657 -21.96247 1.000 35.79580 ? 189 HIS   A CE1 1 
ATOM   1340 N NE2 . HIS   A 1 182 ? -0.28791  -26.37373 -22.14919 1.000 32.24593 ? 189 HIS   A NE2 1 
ATOM   1341 N N   . LEU   A 1 183 ? -0.31173  -26.46843 -15.26929 1.000 25.33574 ? 190 LEU   A N   1 
ATOM   1342 C CA  . LEU   A 1 183 ? 0.11168   -26.15589 -13.90306 1.000 25.95602 ? 190 LEU   A CA  1 
ATOM   1343 C C   . LEU   A 1 183 ? 1.04492   -27.21292 -13.34079 1.000 26.43854 ? 190 LEU   A C   1 
ATOM   1344 O O   . LEU   A 1 183 ? 0.96526   -28.39943 -13.67105 1.000 29.14923 ? 190 LEU   A O   1 
ATOM   1345 C CB  . LEU   A 1 183 ? -1.12372  -26.05856 -13.00705 1.000 26.16130 ? 190 LEU   A CB  1 
ATOM   1346 C CG  . LEU   A 1 183 ? -2.06761  -24.88158 -13.25389 1.000 23.89366 ? 190 LEU   A CG  1 
ATOM   1347 C CD1 . LEU   A 1 183 ? -3.17022  -24.86136 -12.18005 1.000 26.11506 ? 190 LEU   A CD1 1 
ATOM   1348 C CD2 . LEU   A 1 183 ? -1.32096  -23.59014 -13.13066 1.000 28.85909 ? 190 LEU   A CD2 1 
ATOM   1349 N N   . LYS   A 1 184 ? 1.96450   -26.76100 -12.48935 1.000 27.74490 ? 191 LYS   A N   1 
ATOM   1350 C CA  . LYS   A 1 184 ? 2.81763   -27.66604 -11.74337 1.000 28.53543 ? 191 LYS   A CA  1 
ATOM   1351 C C   . LYS   A 1 184 ? 1.97351   -28.49487 -10.77658 1.000 31.13924 ? 191 LYS   A C   1 
ATOM   1352 O O   . LYS   A 1 184 ? 0.93873   -28.03500 -10.28341 1.000 32.73542 ? 191 LYS   A O   1 
ATOM   1353 C CB  . LYS   A 1 184 ? 3.88237   -26.88382 -10.96462 1.000 30.40393 ? 191 LYS   A CB  1 
ATOM   1354 C CG  . LYS   A 1 184 ? 4.88258   -26.08703 -11.81783 1.000 32.78782 ? 191 LYS   A CG  1 
ATOM   1355 C CD  . LYS   A 1 184 ? 5.57599   -25.02741 -10.91475 1.000 40.37773 ? 191 LYS   A CD  1 
ATOM   1356 C CE  . LYS   A 1 184 ? 6.43996   -24.05739 -11.66546 1.000 42.39109 ? 191 LYS   A CE  1 
ATOM   1357 N NZ  . LYS   A 1 184 ? 7.24806   -23.16315 -10.74932 1.000 50.42098 ? 191 LYS   A NZ  1 
ATOM   1358 N N   . GLU   A 1 185 ? 2.45657   -29.70628 -10.46638 1.000 32.67600 ? 192 GLU   A N   1 
ATOM   1359 C CA  . GLU   A 1 185 ? 1.71035   -30.64440 -9.62944  1.000 37.52128 ? 192 GLU   A CA  1 
ATOM   1360 C C   . GLU   A 1 185 ? 1.26438   -30.03516 -8.30961  1.000 39.19461 ? 192 GLU   A C   1 
ATOM   1361 O O   . GLU   A 1 185 ? 0.17190   -30.34863 -7.81358  1.000 35.84459 ? 192 GLU   A O   1 
ATOM   1362 C CB  . GLU   A 1 185 ? 2.56247   -31.89599 -9.37262  1.000 45.30749 ? 192 GLU   A CB  1 
ATOM   1363 C CG  . GLU   A 1 185 ? 2.11309   -32.78214 -8.20601  1.000 70.07520 ? 192 GLU   A CG  1 
ATOM   1364 C CD  . GLU   A 1 185 ? 2.89689   -32.52068 -6.88879  1.000 83.10254 ? 192 GLU   A CD  1 
ATOM   1365 O OE1 . GLU   A 1 185 ? 4.10976   -32.20768 -6.95484  1.000 81.06241 ? 192 GLU   A OE1 1 
ATOM   1366 O OE2 . GLU   A 1 185 ? 2.30979   -32.63894 -5.78257  1.000 72.19669 ? 192 GLU   A OE2 1 
ATOM   1367 N N   . ASP   A 1 186 ? 2.08238   -29.17554 -7.71106  1.000 34.78159 ? 193 ASP   A N   1 
ATOM   1368 C CA  . ASP   A 1 186 ? 1.74011   -28.65300 -6.39243  1.000 34.20261 ? 193 ASP   A CA  1 
ATOM   1369 C C   . ASP   A 1 186 ? 1.02838   -27.30394 -6.45279  1.000 31.73638 ? 193 ASP   A C   1 
ATOM   1370 O O   . ASP   A 1 186 ? 0.82347   -26.69117 -5.40977  1.000 29.77018 ? 193 ASP   A O   1 
ATOM   1371 C CB  . ASP   A 1 186 ? 2.98102   -28.57147 -5.51572  1.000 35.54318 ? 193 ASP   A CB  1 
ATOM   1372 C CG  . ASP   A 1 186 ? 4.01184   -27.58856 -6.02994  1.000 45.01789 ? 193 ASP   A CG  1 
ATOM   1373 O OD1 . ASP   A 1 186 ? 4.09390   -27.35191 -7.25916  1.000 50.88544 ? 193 ASP   A OD1 1 
ATOM   1374 O OD2 . ASP   A 1 186 ? 4.84727   -27.14682 -5.21098  1.000 53.27701 ? 193 ASP   A OD2 1 
ATOM   1375 N N   . GLN   A 1 187 ? 0.56194   -26.87286 -7.63482  1.000 26.54774 ? 194 GLN   A N   1 
ATOM   1376 C CA  . GLN   A 1 187 ? -0.07760  -25.58394 -7.79466  1.000 22.44081 ? 194 GLN   A CA  1 
ATOM   1377 C C   . GLN   A 1 187 ? -1.52427  -25.74780 -8.25159  1.000 23.87323 ? 194 GLN   A C   1 
ATOM   1378 O O   . GLN   A 1 187 ? -2.09727  -24.84415 -8.86221  1.000 27.10102 ? 194 GLN   A O   1 
ATOM   1379 C CB  . GLN   A 1 187 ? 0.72243   -24.71450 -8.77760  1.000 26.35812 ? 194 GLN   A CB  1 
ATOM   1380 C CG  . GLN   A 1 187 ? 2.14364   -24.48820 -8.30228  1.000 26.62268 ? 194 GLN   A CG  1 
ATOM   1381 C CD  . GLN   A 1 187 ? 2.22839   -23.80526 -6.95107  1.000 27.61445 ? 194 GLN   A CD  1 
ATOM   1382 O OE1 . GLN   A 1 187 ? 1.43867   -22.87953 -6.66912  1.000 28.95480 ? 194 GLN   A OE1 1 
ATOM   1383 N NE2 . GLN   A 1 187 ? 3.23467   -24.15023 -6.16869  1.000 31.36692 ? 194 GLN   A NE2 1 
ATOM   1384 N N   . THR   A 1 188 ? -2.14343  -26.88985 -7.93728  1.000 26.86784 ? 195 THR   A N   1 
ATOM   1385 C CA  . THR   A 1 188 ? -3.52190  -27.08600 -8.41180  1.000 30.68768 ? 195 THR   A CA  1 
ATOM   1386 C C   . THR   A 1 188 ? -4.57327  -26.33074 -7.60708  1.000 30.41460 ? 195 THR   A C   1 
ATOM   1387 O O   . THR   A 1 188 ? -5.75379  -26.36964 -8.00329  1.000 29.19538 ? 195 THR   A O   1 
ATOM   1388 C CB  . THR   A 1 188 ? -3.91144  -28.56178 -8.42315  1.000 32.80626 ? 195 THR   A CB  1 
ATOM   1389 O OG1 . THR   A 1 188 ? -3.84615  -29.10057 -7.08924  1.000 34.76187 ? 195 THR   A OG1 1 
ATOM   1390 C CG2 . THR   A 1 188 ? -3.01364  -29.32462 -9.37557  1.000 30.24980 ? 195 THR   A CG2 1 
ATOM   1391 N N   . GLU   A 1 189 ? -4.19654  -25.63873 -6.52048  1.000 27.44017 ? 196 GLU   A N   1 
ATOM   1392 C CA  . GLU   A 1 189 ? -5.15266  -24.70608 -5.88252  1.000 28.58629 ? 196 GLU   A CA  1 
ATOM   1393 C C   . GLU   A 1 189 ? -5.69889  -23.67847 -6.87023  1.000 26.93344 ? 196 GLU   A C   1 
ATOM   1394 O O   . GLU   A 1 189 ? -6.82633  -23.18939 -6.69232  1.000 25.96655 ? 196 GLU   A O   1 
ATOM   1395 C CB  . GLU   A 1 189 ? -4.52137  -23.97982 -4.69251  1.000 29.05197 ? 196 GLU   A CB  1 
ATOM   1396 C CG  . GLU   A 1 189 ? -3.49381  -22.91623 -5.06935  1.000 26.03461 ? 196 GLU   A CG  1 
ATOM   1397 C CD  . GLU   A 1 189 ? -2.71940  -22.48534 -3.84477  1.000 31.39170 ? 196 GLU   A CD  1 
ATOM   1398 O OE1 . GLU   A 1 189 ? -1.81907  -23.25261 -3.39421  1.000 34.42343 ? 196 GLU   A OE1 1 
ATOM   1399 O OE2 . GLU   A 1 189 ? -3.05230  -21.41446 -3.27820  1.000 32.36196 ? 196 GLU   A OE2 1 
ATOM   1400 N N   . TYR   A 1 190 ? -4.94927  -23.32283 -7.90903  1.000 25.37214 ? 197 TYR   A N   1 
ATOM   1401 C CA  . TYR   A 1 190 ? -5.42503  -22.31293 -8.85333  1.000 24.07478 ? 197 TYR   A CA  1 
ATOM   1402 C C   . TYR   A 1 190 ? -6.42539  -22.86359 -9.86278  1.000 29.05972 ? 197 TYR   A C   1 
ATOM   1403 O O   . TYR   A 1 190 ? -6.78038  -22.14900 -10.81321 1.000 28.07897 ? 197 TYR   A O   1 
ATOM   1404 C CB  . TYR   A 1 190 ? -4.21694  -21.67128 -9.57621  1.000 24.43579 ? 197 TYR   A CB  1 
ATOM   1405 C CG  . TYR   A 1 190 ? -3.31104  -21.03861 -8.54476  1.000 23.38297 ? 197 TYR   A CG  1 
ATOM   1406 C CD1 . TYR   A 1 190 ? -3.75289  -19.94856 -7.78676  1.000 25.90047 ? 197 TYR   A CD1 1 
ATOM   1407 C CD2 . TYR   A 1 190 ? -2.05503  -21.57953 -8.23664  1.000 24.53125 ? 197 TYR   A CD2 1 
ATOM   1408 C CE1 . TYR   A 1 190 ? -2.96047  -19.39175 -6.78730  1.000 26.06209 ? 197 TYR   A CE1 1 
ATOM   1409 C CE2 . TYR   A 1 190 ? -1.26548  -21.03002 -7.25125  1.000 27.93760 ? 197 TYR   A CE2 1 
ATOM   1410 C CZ  . TYR   A 1 190 ? -1.73400  -19.92388 -6.52311  1.000 26.57749 ? 197 TYR   A CZ  1 
ATOM   1411 O OH  . TYR   A 1 190 ? -0.99628  -19.37575 -5.50355  1.000 26.85946 ? 197 TYR   A OH  1 
ATOM   1412 N N   . LEU   A 1 191 ? -6.85682  -24.11885 -9.71581  1.000 23.48329 ? 198 LEU   A N   1 
ATOM   1413 C CA  . LEU   A 1 191 ? -8.00850  -24.62106 -10.47416 1.000 25.75552 ? 198 LEU   A CA  1 
ATOM   1414 C C   . LEU   A 1 191 ? -9.29755  -24.58968 -9.65364  1.000 25.14927 ? 198 LEU   A C   1 
ATOM   1415 O O   . LEU   A 1 191 ? -10.37393 -24.95366 -10.17107 1.000 29.10844 ? 198 LEU   A O   1 
ATOM   1416 C CB  . LEU   A 1 191 ? -7.72837  -26.05047 -10.90201 1.000 26.41085 ? 198 LEU   A CB  1 
ATOM   1417 C CG  . LEU   A 1 191 ? -6.52007  -26.16903 -11.79738 1.000 28.18084 ? 198 LEU   A CG  1 
ATOM   1418 C CD1 . LEU   A 1 191 ? -6.31007  -27.61826 -12.13431 1.000 31.11972 ? 198 LEU   A CD1 1 
ATOM   1419 C CD2 . LEU   A 1 191 ? -6.67743  -25.29417 -13.07085 1.000 31.62629 ? 198 LEU   A CD2 1 
ATOM   1420 N N   . GLU   A 1 192 ? -9.20803  -24.25166 -8.37650  1.000 26.15828 ? 199 GLU   A N   1 
ATOM   1421 C CA  . GLU   A 1 192 ? -10.37764 -24.26898 -7.49150  1.000 25.16966 ? 199 GLU   A CA  1 
ATOM   1422 C C   . GLU   A 1 192 ? -11.15169 -22.95944 -7.60985  1.000 25.88262 ? 199 GLU   A C   1 
ATOM   1423 O O   . GLU   A 1 192 ? -10.57464 -21.87426 -7.55256  1.000 25.23455 ? 199 GLU   A O   1 
ATOM   1424 C CB  . GLU   A 1 192 ? -10.00050 -24.53707 -6.04079  1.000 30.27499 ? 199 GLU   A CB  1 
ATOM   1425 C CG  . GLU   A 1 192 ? -9.22582  -25.86791 -5.88094  1.000 33.19007 ? 199 GLU   A CG  1 
ATOM   1426 C CD  . GLU   A 1 192 ? -8.74477  -26.12874 -4.46313  1.000 66.07426 ? 199 GLU   A CD  1 
ATOM   1427 O OE1 . GLU   A 1 192 ? -9.33964  -25.55278 -3.52231  1.000 78.95393 ? 199 GLU   A OE1 1 
ATOM   1428 O OE2 . GLU   A 1 192 ? -7.78135  -26.91627 -4.29119  1.000 75.20461 ? 199 GLU   A OE2 1 
ATOM   1429 N N   . GLU   A 1 193 ? -12.46894 -23.07614 -7.79010  1.000 26.97122 ? 200 GLU   A N   1 
ATOM   1430 C CA  . GLU   A 1 193 ? -13.28539 -21.87792 -8.01643  1.000 25.80586 ? 200 GLU   A CA  1 
ATOM   1431 C C   . GLU   A 1 193 ? -13.08286 -20.84088 -6.90156  1.000 25.62017 ? 200 GLU   A C   1 
ATOM   1432 O O   . GLU   A 1 193 ? -12.87579 -19.64482 -7.16794  1.000 26.49493 ? 200 GLU   A O   1 
ATOM   1433 C CB  . GLU   A 1 193 ? -14.76999 -22.28665 -8.10616  1.000 30.48379 ? 200 GLU   A CB  1 
ATOM   1434 C CG  . GLU   A 1 193 ? -15.64664 -21.12270 -8.45818  1.000 37.84233 ? 200 GLU   A CG  1 
ATOM   1435 C CD  . GLU   A 1 193 ? -17.13339 -21.45714 -8.42515  1.000 57.78774 ? 200 GLU   A CD  1 
ATOM   1436 O OE1 . GLU   A 1 193 ? -17.50189 -22.55227 -7.94206  1.000 54.39668 ? 200 GLU   A OE1 1 
ATOM   1437 O OE2 . GLU   A 1 193 ? -17.92242 -20.62926 -8.92831  1.000 61.71482 ? 200 GLU   A OE2 1 
ATOM   1438 N N   . ARG   A 1 194 ? -13.13887 -21.27775 -5.64466  1.000 26.87646 ? 201 ARG   A N   1 
ATOM   1439 C CA  . ARG   A 1 194 ? -13.08842 -20.30153 -4.55633  1.000 24.45220 ? 201 ARG   A CA  1 
ATOM   1440 C C   . ARG   A 1 194 ? -11.73930 -19.60152 -4.49847  1.000 27.47668 ? 201 ARG   A C   1 
ATOM   1441 O O   . ARG   A 1 194 ? -11.67340 -18.41558 -4.13945  1.000 24.99264 ? 201 ARG   A O   1 
ATOM   1442 C CB  . ARG   A 1 194 ? -13.42052 -20.96568 -3.23543  1.000 31.16398 ? 201 ARG   A CB  1 
ATOM   1443 C CG  . ARG   A 1 194 ? -12.50306 -22.03521 -2.80934  1.000 36.39896 ? 201 ARG   A CG  1 
ATOM   1444 C CD  . ARG   A 1 194 ? -12.91667 -22.44288 -1.38841  1.000 38.97328 ? 201 ARG   A CD  1 
ATOM   1445 N NE  . ARG   A 1 194 ? -11.97904 -23.40354 -0.84324  1.000 45.83160 ? 201 ARG   A NE  1 
ATOM   1446 C CZ  . ARG   A 1 194 ? -12.16110 -23.96553 0.33860   1.000 42.51456 ? 201 ARG   A CZ  1 
ATOM   1447 N NH1 . ARG   A 1 194 ? -13.26385 -23.72257 1.04860   1.000 44.03736 ? 201 ARG   A NH1 1 
ATOM   1448 N NH2 . ARG   A 1 194 ? -11.22140 -24.78066 0.81845   1.000 50.70046 ? 201 ARG   A NH2 1 
ATOM   1449 N N   . ARG   A 1 195 ? -10.66073 -20.29749 -4.86289  1.000 26.18279 ? 202 ARG   A N   1 
ATOM   1450 C CA  . ARG   A 1 195 ? -9.34917  -19.65874 -4.87591  1.000 25.18365 ? 202 ARG   A CA  1 
ATOM   1451 C C   . ARG   A 1 195 ? -9.24312  -18.66536 -6.01994  1.000 23.53463 ? 202 ARG   A C   1 
ATOM   1452 O O   . ARG   A 1 195 ? -8.68199  -17.57157 -5.85201  1.000 22.83735 ? 202 ARG   A O   1 
ATOM   1453 C CB  . ARG   A 1 195 ? -8.24473  -20.73635 -5.00057  1.000 25.52283 ? 202 ARG   A CB  1 
ATOM   1454 C CG  . ARG   A 1 195 ? -6.78337  -20.18330 -4.98362  1.000 23.57747 ? 202 ARG   A CG  1 
ATOM   1455 C CD  . ARG   A 1 195 ? -6.43604  -19.67915 -3.60833  1.000 25.09956 ? 202 ARG   A CD  1 
ATOM   1456 N NE  . ARG   A 1 195 ? -4.99629  -19.41438 -3.52743  1.000 25.03147 ? 202 ARG   A NE  1 
ATOM   1457 C CZ  . ARG   A 1 195 ? -4.45540  -18.22099 -3.29201  1.000 26.45249 ? 202 ARG   A CZ  1 
ATOM   1458 N NH1 . ARG   A 1 195 ? -5.17896  -17.16202 -3.01704  1.000 26.98775 ? 202 ARG   A NH1 1 
ATOM   1459 N NH2 . ARG   A 1 195 ? -3.13691  -18.09209 -3.33325  1.000 27.53271 ? 202 ARG   A NH2 1 
ATOM   1460 N N   . ILE   A 1 196 ? -9.68967  -19.05601 -7.22933  1.000 24.16929 ? 203 ILE   A N   1 
ATOM   1461 C CA  . ILE   A 1 196 ? -9.64371  -18.09980 -8.34291  1.000 24.25356 ? 203 ILE   A CA  1 
ATOM   1462 C C   . ILE   A 1 196 ? -10.48411 -16.87413 -8.03972  1.000 20.64090 ? 203 ILE   A C   1 
ATOM   1463 O O   . ILE   A 1 196 ? -10.03509 -15.74417 -8.26729  1.000 23.60878 ? 203 ILE   A O   1 
ATOM   1464 C CB  . ILE   A 1 196 ? -10.09759 -18.74244 -9.66491  1.000 23.53409 ? 203 ILE   A CB  1 
ATOM   1465 C CG1 . ILE   A 1 196 ? -9.12250  -19.87623 -10.01768 1.000 25.85137 ? 203 ILE   A CG1 1 
ATOM   1466 C CG2 . ILE   A 1 196 ? -10.08010 -17.65298 -10.76815 1.000 22.59209 ? 203 ILE   A CG2 1 
ATOM   1467 C CD1 . ILE   A 1 196 ? -9.78767  -20.87476 -11.02706 1.000 28.39022 ? 203 ILE   A CD1 1 
ATOM   1468 N N   . LYS   A 1 197 ? -11.70235 -17.06412 -7.50896  1.000 22.08056 ? 204 LYS   A N   1 
ATOM   1469 C CA  . LYS   A 1 197 ? -12.56437 -15.91711 -7.19165  1.000 24.25286 ? 204 LYS   A CA  1 
ATOM   1470 C C   . LYS   A 1 197 ? -11.86570 -14.98100 -6.21598  1.000 22.10031 ? 204 LYS   A C   1 
ATOM   1471 O O   . LYS   A 1 197 ? -11.94683 -13.73689 -6.33507  1.000 23.68346 ? 204 LYS   A O   1 
ATOM   1472 C CB  . LYS   A 1 197 ? -13.88126 -16.38279 -6.54923  1.000 27.91372 ? 204 LYS   A CB  1 
ATOM   1473 C CG  . LYS   A 1 197 ? -14.94218 -16.77490 -7.48482  1.000 35.09425 ? 204 LYS   A CG  1 
ATOM   1474 C CD  . LYS   A 1 197 ? -16.24459 -17.14809 -6.67716  1.000 35.90080 ? 204 LYS   A CD  1 
ATOM   1475 C CE  . LYS   A 1 197 ? -17.29074 -17.79099 -7.57354  1.000 60.47229 ? 204 LYS   A CE  1 
ATOM   1476 N NZ  . LYS   A 1 197 ? -18.18756 -18.69771 -6.75859  1.000 63.65821 ? 204 LYS   A NZ  1 
ATOM   1477 N N   . GLU   A 1 198 ? -11.22601 -15.56132 -5.18791  1.000 22.66942 ? 205 GLU   A N   1 
ATOM   1478 C CA  . GLU   A 1 198 ? -10.52833 -14.74668 -4.19249  1.000 22.44100 ? 205 GLU   A CA  1 
ATOM   1479 C C   . GLU   A 1 198 ? -9.42157  -13.90342 -4.81358  1.000 22.31679 ? 205 GLU   A C   1 
ATOM   1480 O O   . GLU   A 1 198 ? -9.23907  -12.72971 -4.44657  1.000 23.35955 ? 205 GLU   A O   1 
ATOM   1481 C CB  . GLU   A 1 198 ? -9.96274  -15.66464 -3.10957  1.000 20.70715 ? 205 GLU   A CB  1 
ATOM   1482 C CG  . GLU   A 1 198 ? -8.99085  -14.98813 -2.10004  1.000 23.87579 ? 205 GLU   A CG  1 
ATOM   1483 C CD  . GLU   A 1 198 ? -8.37244  -15.99809 -1.13793  1.000 26.09460 ? 205 GLU   A CD  1 
ATOM   1484 O OE1 . GLU   A 1 198 ? -7.80658  -16.99251 -1.67677  1.000 27.48082 ? 205 GLU   A OE1 1 
ATOM   1485 O OE2 . GLU   A 1 198 ? -8.38616  -15.77056 0.11811   1.000 26.46055 ? 205 GLU   A OE2 1 
ATOM   1486 N N   . ILE   A 1 199 ? -8.64346  -14.49410 -5.72703  1.000 20.61949 ? 206 ILE   A N   1 
ATOM   1487 C CA  . ILE   A 1 199 ? -7.52166  -13.74774 -6.30758  1.000 19.33458 ? 206 ILE   A CA  1 
ATOM   1488 C C   . ILE   A 1 199 ? -8.01923  -12.66299 -7.26060  1.000 21.59102 ? 206 ILE   A C   1 
ATOM   1489 O O   . ILE   A 1 199 ? -7.43017  -11.57921 -7.30090  1.000 22.83790 ? 206 ILE   A O   1 
ATOM   1490 C CB  . ILE   A 1 199 ? -6.58112  -14.73044 -7.03373  1.000 21.96414 ? 206 ILE   A CB  1 
ATOM   1491 C CG1 . ILE   A 1 199 ? -5.91523  -15.68127 -6.02871  1.000 25.24201 ? 206 ILE   A CG1 1 
ATOM   1492 C CG2 . ILE   A 1 199 ? -5.59056  -14.00435 -7.89583  1.000 25.45128 ? 206 ILE   A CG2 1 
ATOM   1493 C CD1 . ILE   A 1 199 ? -5.41930  -16.95368 -6.82915  1.000 27.09311 ? 206 ILE   A CD1 1 
ATOM   1494 N N   . VAL   A 1 200 ? -9.09048  -12.93687 -8.03722  1.000 20.31534 ? 207 VAL   A N   1 
ATOM   1495 C CA  . VAL   A 1 200 ? -9.63651  -11.89577 -8.90775  1.000 20.93666 ? 207 VAL   A CA  1 
ATOM   1496 C C   . VAL   A 1 200 ? -10.15815 -10.73360 -8.07491  1.000 23.16984 ? 207 VAL   A C   1 
ATOM   1497 O O   . VAL   A 1 200 ? -9.89975  -9.54888  -8.37308  1.000 22.78748 ? 207 VAL   A O   1 
ATOM   1498 C CB  . VAL   A 1 200 ? -10.74903 -12.48818 -9.79370  1.000 22.95655 ? 207 VAL   A CB  1 
ATOM   1499 C CG1 . VAL   A 1 200 ? -11.50495 -11.38182 -10.50154 1.000 24.44470 ? 207 VAL   A CG1 1 
ATOM   1500 C CG2 . VAL   A 1 200 ? -10.11582 -13.45369 -10.77305 1.000 22.02073 ? 207 VAL   A CG2 1 
ATOM   1501 N N   . LYS   A 1 201 ? -10.86969 -11.03508 -6.97638  1.000 21.44322 ? 208 LYS   A N   1 
ATOM   1502 C CA  . LYS   A 1 201 ? -11.38490 -9.94833  -6.14811  1.000 21.66737 ? 208 LYS   A CA  1 
ATOM   1503 C C   . LYS   A 1 201 ? -10.28098 -9.15471  -5.47464  1.000 22.32860 ? 208 LYS   A C   1 
ATOM   1504 O O   . LYS   A 1 201 ? -10.40747 -7.94705  -5.27644  1.000 25.81856 ? 208 LYS   A O   1 
ATOM   1505 C CB  . LYS   A 1 201 ? -12.34646 -10.50898 -5.06832  1.000 24.16734 ? 208 LYS   A CB  1 
ATOM   1506 C CG  . LYS   A 1 201 ? -13.10789 -9.41995  -4.28420  1.000 31.85685 ? 208 LYS   A CG  1 
ATOM   1507 C CD  . LYS   A 1 201 ? -14.21984 -10.07857 -3.52301  1.000 43.07097 ? 208 LYS   A CD  1 
ATOM   1508 C CE  . LYS   A 1 201 ? -14.76941 -9.18257  -2.42600  1.000 50.61899 ? 208 LYS   A CE  1 
ATOM   1509 N NZ  . LYS   A 1 201 ? -15.63515 -10.01540 -1.53500  1.000 60.52559 ? 208 LYS   A NZ  1 
ATOM   1510 N N   . LYS   A 1 202 ? -9.18179  -9.82741  -5.10184  1.000 21.20300 ? 209 LYS   A N   1 
ATOM   1511 C CA  . LYS   A 1 202 ? -8.09027  -9.12196  -4.42845  1.000 22.77906 ? 209 LYS   A CA  1 
ATOM   1512 C C   . LYS   A 1 202 ? -7.29118  -8.20527  -5.34786  1.000 20.86125 ? 209 LYS   A C   1 
ATOM   1513 O O   . LYS   A 1 202 ? -6.91070  -7.09108  -4.92766  1.000 23.52300 ? 209 LYS   A O   1 
ATOM   1514 C CB  . LYS   A 1 202 ? -7.12825  -10.15436 -3.82795  1.000 22.36297 ? 209 LYS   A CB  1 
ATOM   1515 C CG  . LYS   A 1 202 ? -6.05888  -9.51255  -2.94835  1.000 25.34442 ? 209 LYS   A CG  1 
ATOM   1516 C CD  . LYS   A 1 202 ? -5.36238  -10.60886 -2.12210  1.000 43.71916 ? 209 LYS   A CD  1 
ATOM   1517 C CE  . LYS   A 1 202 ? -4.27398  -10.07187 -1.15635  1.000 66.63105 ? 209 LYS   A CE  1 
ATOM   1518 N NZ  . LYS   A 1 202 ? -3.42331  -11.21334 -0.61601  1.000 50.09493 ? 209 LYS   A NZ  1 
ATOM   1519 N N   . HIS   A 1 203 ? -7.00405  -8.67554  -6.56609  1.000 22.26112 ? 210 HIS   A N   1 
ATOM   1520 C CA  . HIS   A 1 203 ? -6.00698  -8.05461  -7.42003  1.000 23.90129 ? 210 HIS   A CA  1 
ATOM   1521 C C   . HIS   A 1 203 ? -6.56416  -7.47128  -8.70853  1.000 23.64331 ? 210 HIS   A C   1 
ATOM   1522 O O   . HIS   A 1 203 ? -5.85778  -6.68540  -9.36013  1.000 25.31775 ? 210 HIS   A O   1 
ATOM   1523 C CB  . HIS   A 1 203 ? -4.93298  -9.09811  -7.79252  1.000 25.90395 ? 210 HIS   A CB  1 
ATOM   1524 C CG  . HIS   A 1 203 ? -4.09513  -9.56574  -6.63784  1.000 26.97477 ? 210 HIS   A CG  1 
ATOM   1525 N ND1 . HIS   A 1 203 ? -3.31218  -8.71595  -5.89144  1.000 33.15444 ? 210 HIS   A ND1 1 
ATOM   1526 C CD2 . HIS   A 1 203 ? -3.93646  -10.79975 -6.09800  1.000 30.80208 ? 210 HIS   A CD2 1 
ATOM   1527 C CE1 . HIS   A 1 203 ? -2.67981  -9.40870  -4.95646  1.000 31.31170 ? 210 HIS   A CE1 1 
ATOM   1528 N NE2 . HIS   A 1 203 ? -3.04670  -10.67472 -5.05887  1.000 32.36257 ? 210 HIS   A NE2 1 
ATOM   1529 N N   . SER   A 1 204 ? -7.78609  -7.83324  -9.11203  1.000 21.91083 ? 211 SER   A N   1 
ATOM   1530 C CA  . SER   A 1 204 ? -8.26714  -7.52722  -10.44200 1.000 19.73592 ? 211 SER   A CA  1 
ATOM   1531 C C   . SER   A 1 204 ? -9.71481  -7.05784  -10.36768 1.000 19.60370 ? 211 SER   A C   1 
ATOM   1532 O O   . SER   A 1 204 ? -10.45316 -7.17497  -11.34818 1.000 24.30156 ? 211 SER   A O   1 
ATOM   1533 C CB  . SER   A 1 204 ? -8.19602  -8.77289  -11.40307 1.000 23.26504 ? 211 SER   A CB  1 
ATOM   1534 O OG  . SER   A 1 204 ? -6.81513  -9.24128  -11.43766 1.000 24.11713 ? 211 SER   A OG  1 
ATOM   1535 N N   . GLN   A 1 205 ? -10.07583 -6.48051  -9.20717  1.000 23.36981 ? 212 GLN   A N   1 
ATOM   1536 C CA  . GLN   A 1 205 ? -11.51852 -6.22838  -9.00018  1.000 26.08327 ? 212 GLN   A CA  1 
ATOM   1537 C C   . GLN   A 1 205 ? -12.03705 -5.05504  -9.81345  1.000 29.11494 ? 212 GLN   A C   1 
ATOM   1538 O O   . GLN   A 1 205 ? -13.26374 -4.91755  -9.95432  1.000 29.04465 ? 212 GLN   A O   1 
ATOM   1539 C CB  . GLN   A 1 205 ? -11.87034 -5.92787  -7.54196  1.000 30.32780 ? 212 GLN   A CB  1 
ATOM   1540 C CG  . GLN   A 1 205 ? -11.03434 -4.88081  -6.98374  1.000 33.93242 ? 212 GLN   A CG  1 
ATOM   1541 C CD  . GLN   A 1 205 ? -11.18066 -4.74087  -5.48131  1.000 53.78103 ? 212 GLN   A CD  1 
ATOM   1542 O OE1 . GLN   A 1 205 ? -10.19013 -4.52930  -4.76129  1.000 42.19553 ? 212 GLN   A OE1 1 
ATOM   1543 N NE2 . GLN   A 1 205 ? -12.43142 -4.77430  -5.01405  1.000 34.02011 ? 212 GLN   A NE2 1 
ATOM   1544 N N   . PHE   A 1 206 ? -11.16908 -4.19605  -10.35075 1.000 25.56227 ? 213 PHE   A N   1 
ATOM   1545 C CA  . PHE   A 1 206 ? -11.62967 -3.02580  -11.08004 1.000 20.90211 ? 213 PHE   A CA  1 
ATOM   1546 C C   . PHE   A 1 206 ? -11.36751 -3.09801  -12.57818 1.000 24.44837 ? 213 PHE   A C   1 
ATOM   1547 O O   . PHE   A 1 206 ? -11.64403 -2.11011  -13.27633 1.000 23.92517 ? 213 PHE   A O   1 
ATOM   1548 C CB  . PHE   A 1 206 ? -10.98434 -1.76986  -10.49745 1.000 23.66607 ? 213 PHE   A CB  1 
ATOM   1549 C CG  . PHE   A 1 206 ? -11.19999 -1.64281  -9.03011  1.000 26.75596 ? 213 PHE   A CG  1 
ATOM   1550 C CD1 . PHE   A 1 206 ? -12.50181 -1.66695  -8.48651  1.000 26.72164 ? 213 PHE   A CD1 1 
ATOM   1551 C CD2 . PHE   A 1 206 ? -10.13463 -1.48266  -8.18030  1.000 27.42409 ? 213 PHE   A CD2 1 
ATOM   1552 C CE1 . PHE   A 1 206 ? -12.69727 -1.53357  -7.10531  1.000 30.26968 ? 213 PHE   A CE1 1 
ATOM   1553 C CE2 . PHE   A 1 206 ? -10.31887 -1.38493  -6.79380  1.000 30.36749 ? 213 PHE   A CE2 1 
ATOM   1554 C CZ  . PHE   A 1 206 ? -11.60362 -1.40141  -6.25182  1.000 31.18718 ? 213 PHE   A CZ  1 
ATOM   1555 N N   . ILE   A 1 207 ? -10.94050 -4.25346  -13.10791 1.000 22.18720 ? 214 ILE   A N   1 
ATOM   1556 C CA  . ILE   A 1 207 ? -10.68814 -4.37374  -14.54589 1.000 22.05296 ? 214 ILE   A CA  1 
ATOM   1557 C C   . ILE   A 1 207 ? -11.93348 -3.98324  -15.32202 1.000 24.21117 ? 214 ILE   A C   1 
ATOM   1558 O O   . ILE   A 1 207 ? -13.05775 -4.34902  -14.94119 1.000 25.14611 ? 214 ILE   A O   1 
ATOM   1559 C CB  . ILE   A 1 207 ? -10.20157 -5.80327  -14.86440 1.000 21.32139 ? 214 ILE   A CB  1 
ATOM   1560 C CG1 . ILE   A 1 207 ? -8.81695  -6.03785  -14.24407 1.000 24.21264 ? 214 ILE   A CG1 1 
ATOM   1561 C CG2 . ILE   A 1 207 ? -10.20984 -6.12036  -16.41106 1.000 21.34667 ? 214 ILE   A CG2 1 
ATOM   1562 C CD1 . ILE   A 1 207 ? -7.69601  -5.23889  -14.91107 1.000 26.32847 ? 214 ILE   A CD1 1 
ATOM   1563 N N   . GLY   A 1 208 ? -11.74845 -3.19574  -16.37939 1.000 22.56092 ? 215 GLY   A N   1 
ATOM   1564 C CA  . GLY   A 1 208 ? -12.88928 -2.65609  -17.11504 1.000 22.89413 ? 215 GLY   A CA  1 
ATOM   1565 C C   . GLY   A 1 208 ? -13.47305 -3.51318  -18.22337 1.000 26.01746 ? 215 GLY   A C   1 
ATOM   1566 O O   . GLY   A 1 208 ? -14.04772 -2.99178  -19.18459 1.000 28.78954 ? 215 GLY   A O   1 
ATOM   1567 N N   . TYR   A 1 209 ? -13.32767 -4.81730  -18.11247 1.000 23.33974 ? 216 TYR   A N   1 
ATOM   1568 C CA  . TYR   A 1 209 ? -13.92558 -5.76836  -19.05108 1.000 23.77887 ? 216 TYR   A CA  1 
ATOM   1569 C C   . TYR   A 1 209 ? -14.51243 -6.87544  -18.20066 1.000 25.01625 ? 216 TYR   A C   1 
ATOM   1570 O O   . TYR   A 1 209 ? -13.98627 -7.16195  -17.12139 1.000 23.52936 ? 216 TYR   A O   1 
ATOM   1571 C CB  . TYR   A 1 209 ? -12.85633 -6.33860  -19.98599 1.000 21.22311 ? 216 TYR   A CB  1 
ATOM   1572 C CG  . TYR   A 1 209 ? -12.23946 -5.26342  -20.83697 1.000 20.77636 ? 216 TYR   A CG  1 
ATOM   1573 C CD1 . TYR   A 1 209 ? -12.89016 -4.81779  -21.99626 1.000 22.52890 ? 216 TYR   A CD1 1 
ATOM   1574 C CD2 . TYR   A 1 209 ? -11.00743 -4.66792  -20.50531 1.000 22.90143 ? 216 TYR   A CD2 1 
ATOM   1575 C CE1 . TYR   A 1 209 ? -12.36790 -3.78376  -22.77374 1.000 22.48086 ? 216 TYR   A CE1 1 
ATOM   1576 C CE2 . TYR   A 1 209 ? -10.50992 -3.60863  -21.27424 1.000 23.48717 ? 216 TYR   A CE2 1 
ATOM   1577 C CZ  . TYR   A 1 209 ? -11.19253 -3.19486  -22.40937 1.000 23.92095 ? 216 TYR   A CZ  1 
ATOM   1578 O OH  . TYR   A 1 209 ? -10.73400 -2.19081  -23.19032 1.000 27.91018 ? 216 TYR   A OH  1 
ATOM   1579 N N   . PRO   A 1 210 ? -15.58736 -7.50930  -18.63468 1.000 22.86364 ? 217 PRO   A N   1 
ATOM   1580 C CA  . PRO   A 1 210 ? -16.15870 -8.61006  -17.83106 1.000 21.45957 ? 217 PRO   A CA  1 
ATOM   1581 C C   . PRO   A 1 210 ? -15.21691 -9.81507  -17.76866 1.000 25.69155 ? 217 PRO   A C   1 
ATOM   1582 O O   . PRO   A 1 210 ? -14.70500 -10.27596 -18.80078 1.000 26.79997 ? 217 PRO   A O   1 
ATOM   1583 C CB  . PRO   A 1 210 ? -17.46054 -8.94226  -18.57479 1.000 24.78832 ? 217 PRO   A CB  1 
ATOM   1584 C CG  . PRO   A 1 210 ? -17.33356 -8.40784  -19.87492 1.000 27.70572 ? 217 PRO   A CG  1 
ATOM   1585 C CD  . PRO   A 1 210 ? -16.35987 -7.23144  -19.85086 1.000 26.83942 ? 217 PRO   A CD  1 
ATOM   1586 N N   . ILE   A 1 211 ? -15.02450 -10.33916 -16.55176 1.000 23.20737 ? 218 ILE   A N   1 
ATOM   1587 C CA  . ILE   A 1 211 ? -14.19665 -11.51993 -16.29732 1.000 22.05369 ? 218 ILE   A CA  1 
ATOM   1588 C C   . ILE   A 1 211 ? -15.13872 -12.63366 -15.87178 1.000 23.52145 ? 218 ILE   A C   1 
ATOM   1589 O O   . ILE   A 1 211 ? -15.78873 -12.52041 -14.82499 1.000 27.61929 ? 218 ILE   A O   1 
ATOM   1590 C CB  . ILE   A 1 211 ? -13.13164 -11.27277 -15.22181 1.000 22.88540 ? 218 ILE   A CB  1 
ATOM   1591 C CG1 . ILE   A 1 211 ? -12.18771 -10.15463 -15.67636 1.000 23.52644 ? 218 ILE   A CG1 1 
ATOM   1592 C CG2 . ILE   A 1 211 ? -12.42984 -12.57954 -14.90779 1.000 23.09644 ? 218 ILE   A CG2 1 
ATOM   1593 C CD1 . ILE   A 1 211 ? -11.27049 -9.60642  -14.51657 1.000 23.60635 ? 218 ILE   A CD1 1 
ATOM   1594 N N   . THR   A 1 212 ? -15.24959 -13.67974 -16.70204 1.000 22.13481 ? 219 THR   A N   1 
ATOM   1595 C CA  . THR   A 1 212 ? -16.17292 -14.77327 -16.39630 1.000 21.83234 ? 219 THR   A CA  1 
ATOM   1596 C C   . THR   A 1 212 ? -15.35211 -15.96787 -15.96617 1.000 22.42865 ? 219 THR   A C   1 
ATOM   1597 O O   . THR   A 1 212 ? -14.53295 -16.44640 -16.74672 1.000 22.40714 ? 219 THR   A O   1 
ATOM   1598 C CB  . THR   A 1 212 ? -17.03639 -15.13097 -17.60582 1.000 23.82373 ? 219 THR   A CB  1 
ATOM   1599 O OG1 . THR   A 1 212 ? -17.81709 -13.97359 -17.99687 1.000 27.33606 ? 219 THR   A OG1 1 
ATOM   1600 C CG2 . THR   A 1 212 ? -18.01056 -16.31108 -17.26287 1.000 24.10320 ? 219 THR   A CG2 1 
ATOM   1601 N N   . LEU   A 1 213 ? -15.57941 -16.45118 -14.74358 1.000 21.99231 ? 220 LEU   A N   1 
ATOM   1602 C CA  . LEU   A 1 213 ? -14.94899 -17.67746 -14.27788 1.000 22.12329 ? 220 LEU   A CA  1 
ATOM   1603 C C   . LEU   A 1 213 ? -15.88321 -18.84067 -14.61203 1.000 22.93694 ? 220 LEU   A C   1 
ATOM   1604 O O   . LEU   A 1 213 ? -16.99096 -18.94270 -14.04314 1.000 26.40549 ? 220 LEU   A O   1 
ATOM   1605 C CB  . LEU   A 1 213 ? -14.67557 -17.58375 -12.77247 1.000 22.46584 ? 220 LEU   A CB  1 
ATOM   1606 C CG  . LEU   A 1 213 ? -14.18081 -18.83830 -12.07511 1.000 26.30019 ? 220 LEU   A CG  1 
ATOM   1607 C CD1 . LEU   A 1 213 ? -12.92485 -19.41250 -12.71257 1.000 23.30664 ? 220 LEU   A CD1 1 
ATOM   1608 C CD2 . LEU   A 1 213 ? -13.89981 -18.48020 -10.58702 1.000 29.31433 ? 220 LEU   A CD2 1 
ATOM   1609 N N   . PHE   A 1 214 ? -15.41878 -19.72329 -15.48019 1.000 21.50940 ? 221 PHE   A N   1 
ATOM   1610 C CA  . PHE   A 1 214 ? -16.17587 -20.90672 -15.86441 1.000 21.82605 ? 221 PHE   A CA  1 
ATOM   1611 C C   . PHE   A 1 214 ? -16.15053 -21.92496 -14.74343 1.000 24.59670 ? 221 PHE   A C   1 
ATOM   1612 O O   . PHE   A 1 214 ? -15.15989 -22.03100 -14.01541 1.000 28.12021 ? 221 PHE   A O   1 
ATOM   1613 C CB  . PHE   A 1 214 ? -15.60738 -21.60185 -17.11608 1.000 24.81474 ? 221 PHE   A CB  1 
ATOM   1614 C CG  . PHE   A 1 214 ? -15.85118 -20.88516 -18.42041 1.000 21.82327 ? 221 PHE   A CG  1 
ATOM   1615 C CD1 . PHE   A 1 214 ? -15.97523 -19.49846 -18.50135 1.000 23.26469 ? 221 PHE   A CD1 1 
ATOM   1616 C CD2 . PHE   A 1 214 ? -15.97617 -21.65580 -19.57755 1.000 23.83881 ? 221 PHE   A CD2 1 
ATOM   1617 C CE1 . PHE   A 1 214 ? -16.17725 -18.84830 -19.71576 1.000 22.20686 ? 221 PHE   A CE1 1 
ATOM   1618 C CE2 . PHE   A 1 214 ? -16.20520 -21.02715 -20.85197 1.000 23.56473 ? 221 PHE   A CE2 1 
ATOM   1619 C CZ  . PHE   A 1 214 ? -16.31148 -19.60934 -20.89656 1.000 22.21060 ? 221 PHE   A CZ  1 
ATOM   1620 N N   . VAL   A 1 215 ? -17.23323 -22.68676 -14.60851 1.000 24.42616 ? 222 VAL   A N   1 
ATOM   1621 C CA  . VAL   A 1 215 ? -17.23530 -23.78995 -13.65044 1.000 29.36807 ? 222 VAL   A CA  1 
ATOM   1622 C C   . VAL   A 1 215 ? -17.14633 -25.11579 -14.37833 1.000 32.76098 ? 222 VAL   A C   1 
ATOM   1623 O O   . VAL   A 1 215 ? -17.25404 -25.20052 -15.60704 1.000 30.89219 ? 222 VAL   A O   1 
ATOM   1624 C CB  . VAL   A 1 215 ? -18.43731 -23.74938 -12.71654 1.000 39.39253 ? 222 VAL   A CB  1 
ATOM   1625 C CG1 . VAL   A 1 215 ? -18.23763 -22.60294 -11.69465 1.000 42.70487 ? 222 VAL   A CG1 1 
ATOM   1626 C CG2 . VAL   A 1 215 ? -19.66737 -23.60759 -13.49078 1.000 32.24785 ? 222 VAL   A CG2 1 
ATOM   1627 N N   . GLU   A 1 216 ? -16.86714 -26.15236 -13.62009 1.000 32.76038 ? 223 GLU   A N   1 
ATOM   1628 C CA  . GLU   A 1 216 ? -16.67892 -27.48079 -14.17955 1.000 37.31713 ? 223 GLU   A CA  1 
ATOM   1629 C C   . GLU   A 1 216 ? -17.73781 -28.45321 -13.69043 1.000 43.22632 ? 223 GLU   A C   1 
ATOM   1630 O O   . GLU   A 1 216 ? -18.18501 -28.36835 -12.54642 1.000 45.45225 ? 223 GLU   A O   1 
ATOM   1631 C CB  . GLU   A 1 216 ? -15.28718 -28.06874 -13.85029 1.000 42.58903 ? 223 GLU   A CB  1 
ATOM   1632 C CG  . GLU   A 1 216 ? -14.11953 -27.11204 -14.05421 1.000 39.67493 ? 223 GLU   A CG  1 
ATOM   1633 C CD  . GLU   A 1 216 ? -12.77823 -27.74644 -13.65118 1.000 44.91948 ? 223 GLU   A CD  1 
ATOM   1634 O OE1 . GLU   A 1 216 ? -12.40114 -28.81596 -14.19937 1.000 42.49197 ? 223 GLU   A OE1 1 
ATOM   1635 O OE2 . GLU   A 1 216 ? -12.09756 -27.14574 -12.78302 1.000 48.13329 ? 223 GLU   A OE2 1 
ATOM   1636 N N   . LYS   A 1 217 ? -18.09724 -29.39816 -14.57544 1.000 43.44838 ? 224 LYS   A N   1 
ATOM   1637 C CA  . LYS   A 1 217 ? -19.01062 -30.49912 -14.25301 1.000 48.20106 ? 224 LYS   A CA  1 
ATOM   1638 C C   . LYS   A 1 217 ? -18.64912 -31.16238 -12.90949 1.000 56.86313 ? 224 LYS   A C   1 
ATOM   1639 O O   . LYS   A 1 217 ? -17.47683 -31.43557 -12.65250 1.000 57.46014 ? 224 LYS   A O   1 
ATOM   1640 C CB  . LYS   A 1 217 ? -19.00811 -31.58751 -15.33728 1.000 55.12846 ? 224 LYS   A CB  1 
ATOM   1641 C CG  . LYS   A 1 217 ? -17.70563 -31.72205 -16.11247 1.000 76.35091 ? 224 LYS   A CG  1 
ATOM   1642 C CD  . LYS   A 1 217 ? -17.64859 -33.05059 -16.90817 1.000 82.43846 ? 224 LYS   A CD  1 
ATOM   1643 C CE  . LYS   A 1 217 ? -16.23661 -33.30981 -17.46235 1.000 78.74154 ? 224 LYS   A CE  1 
ATOM   1644 N NZ  . LYS   A 1 217 ? -16.24550 -34.21936 -18.63989 1.000 68.22652 ? 224 LYS   A NZ  1 
HETATM 1645 C C1  . A1AW4 B 2 .   ? 9.85831   -12.63953 -10.43573 0.959 24.54607 ? 301 A1AW4 A C1  1 
HETATM 1646 C C2  . A1AW4 B 2 .   ? 12.20461  -12.68249 -9.67049  0.959 22.73554 ? 301 A1AW4 A C2  1 
HETATM 1647 C C3  . A1AW4 B 2 .   ? 13.02117  -13.26786 -8.70997  0.959 27.73477 ? 301 A1AW4 A C3  1 
HETATM 1648 C C4  . A1AW4 B 2 .   ? 14.30963  -12.82180 -8.58882  0.959 27.88980 ? 301 A1AW4 A C4  1 
HETATM 1649 C C5  . A1AW4 B 2 .   ? 14.04068  -11.29903 -10.27613 0.959 24.06265 ? 301 A1AW4 A C5  1 
HETATM 1650 C C6  . A1AW4 B 2 .   ? 12.72876  -11.66457 -10.45748 0.959 24.93498 ? 301 A1AW4 A C6  1 
HETATM 1651 C C7  . A1AW4 B 2 .   ? 8.54827   -13.25617 -10.14110 0.959 23.89475 ? 301 A1AW4 A C7  1 
HETATM 1652 C C8  . A1AW4 B 2 .   ? 7.37019   -12.31314 -10.11725 0.959 25.01087 ? 301 A1AW4 A C8  1 
HETATM 1653 C C9  . A1AW4 B 2 .   ? 7.55851   -13.19731 -11.27440 0.959 23.61011 ? 301 A1AW4 A C9  1 
HETATM 1654 N N1  . A1AW4 B 2 .   ? 10.88259  -13.18711 -9.73631  0.959 20.39819 ? 301 A1AW4 A N1  1 
HETATM 1655 N N2  . A1AW4 B 2 .   ? 14.83396  -11.84902 -9.34306  0.959 28.71274 ? 301 A1AW4 A N2  1 
HETATM 1656 O O1  . A1AW4 B 2 .   ? 10.00982  -11.72991 -11.24898 0.959 25.42192 ? 301 A1AW4 A O1  1 
HETATM 1657 O O   . HOH   C 3 .   ? -8.49499  -23.75816 -2.62720  1.000 53.66307 ? 401 HOH   A O   1 
HETATM 1658 O O   . HOH   C 3 .   ? 1.21826   -31.77344 -4.10784  1.000 60.12755 ? 402 HOH   A O   1 
HETATM 1659 O O   . HOH   C 3 .   ? 21.69424  -2.53243  -15.94637 1.000 49.34383 ? 403 HOH   A O   1 
HETATM 1660 O O   . HOH   C 3 .   ? 9.88517   -6.39569  -1.63345  1.000 47.70835 ? 404 HOH   A O   1 
HETATM 1661 O O   . HOH   C 3 .   ? -20.292   -20.584   -9.013    1.000 58.41638 ? 405 HOH   A O   1 
HETATM 1662 O O   . HOH   C 3 .   ? -7.67073  -17.02151 -41.21466 1.000 56.05771 ? 406 HOH   A O   1 
HETATM 1663 O O   . HOH   C 3 .   ? 16.02165  1.73185   -15.11379 1.000 37.26294 ? 407 HOH   A O   1 
HETATM 1664 O O   . HOH   C 3 .   ? 5.88057   -25.71429 -7.08243  1.000 48.33597 ? 408 HOH   A O   1 
HETATM 1665 O O   . HOH   C 3 .   ? 2.24569   -15.86558 -41.09442 1.000 49.08930 ? 409 HOH   A O   1 
HETATM 1666 O O   . HOH   C 3 .   ? 3.60199   -24.26728 -38.72896 1.000 37.60892 ? 410 HOH   A O   1 
HETATM 1667 O O   . HOH   C 3 .   ? -2.66432  -6.36064  -6.44844  1.000 41.70475 ? 411 HOH   A O   1 
HETATM 1668 O O   . HOH   C 3 .   ? -17.94624 -4.00971  -29.12067 1.000 48.44561 ? 412 HOH   A O   1 
HETATM 1669 O O   . HOH   C 3 .   ? 9.48537   -23.70723 -9.71599  1.000 48.33698 ? 413 HOH   A O   1 
HETATM 1670 O O   . HOH   C 3 .   ? -0.11320  -5.41351  -38.55432 1.000 47.08282 ? 414 HOH   A O   1 
HETATM 1671 O O   . HOH   C 3 .   ? -14.49194 -11.75897 -0.04998  1.000 54.15250 ? 415 HOH   A O   1 
HETATM 1672 O O   . HOH   C 3 .   ? 11.93641  -21.66277 -40.69874 1.000 52.17675 ? 416 HOH   A O   1 
HETATM 1673 O O   . HOH   C 3 .   ? -2.84791  -3.35026  -35.55131 1.000 49.55865 ? 417 HOH   A O   1 
HETATM 1674 O O   . HOH   C 3 .   ? -12.83495 -25.05548 -10.91970 1.000 37.69397 ? 418 HOH   A O   1 
HETATM 1675 O O   . HOH   C 3 .   ? 0.21638   -28.22381 -25.89517 1.000 61.14120 ? 419 HOH   A O   1 
HETATM 1676 O O   . HOH   C 3 .   ? 0.27291   -22.54901 -2.02736  1.000 52.49428 ? 420 HOH   A O   1 
HETATM 1677 O O   . HOH   C 3 .   ? 12.30868  -8.80049  -30.06844 1.000 41.94421 ? 421 HOH   A O   1 
HETATM 1678 O O   . HOH   C 3 .   ? 6.89820   -29.51294 -20.13849 1.000 44.18504 ? 422 HOH   A O   1 
HETATM 1679 O O   . HOH   C 3 .   ? 7.73935   -18.97432 -6.63595  1.000 30.03972 ? 423 HOH   A O   1 
HETATM 1680 O O   . HOH   C 3 .   ? 5.99477   -21.26927 -0.07918  1.000 32.34350 ? 424 HOH   A O   1 
HETATM 1681 O O   . HOH   C 3 .   ? 15.12664  -26.36702 -25.03944 1.000 52.26818 ? 425 HOH   A O   1 
HETATM 1682 O O   . HOH   C 3 .   ? -1.44975  -29.19143 -6.03060  1.000 41.57953 ? 426 HOH   A O   1 
HETATM 1683 O O   . HOH   C 3 .   ? -5.31575  -10.42813 -27.34916 1.000 23.74848 ? 427 HOH   A O   1 
HETATM 1684 O O   . HOH   C 3 .   ? 9.88407   -17.55049 -7.78871  1.000 24.85188 ? 428 HOH   A O   1 
HETATM 1685 O O   . HOH   C 3 .   ? -19.28929 -9.86122  -33.17072 1.000 47.76832 ? 429 HOH   A O   1 
HETATM 1686 O O   . HOH   C 3 .   ? -16.12067 -25.76258 -17.92415 1.000 32.44659 ? 430 HOH   A O   1 
HETATM 1687 O O   . HOH   C 3 .   ? 7.89320   -23.14887 -14.18407 1.000 34.80243 ? 431 HOH   A O   1 
HETATM 1688 O O   . HOH   C 3 .   ? -7.49908  -28.35771 -8.04569  1.000 36.69410 ? 432 HOH   A O   1 
HETATM 1689 O O   . HOH   C 3 .   ? 14.56589  -5.17478  -4.16599  1.000 38.91802 ? 433 HOH   A O   1 
HETATM 1690 O O   . HOH   C 3 .   ? -10.76979 -14.90056 0.90219   1.000 31.73167 ? 434 HOH   A O   1 
HETATM 1691 O O   . HOH   C 3 .   ? -8.64036  -11.82400 -36.31673 1.000 33.35677 ? 435 HOH   A O   1 
HETATM 1692 O O   . HOH   C 3 .   ? 7.78386   -27.68907 -24.04972 1.000 39.12807 ? 436 HOH   A O   1 
HETATM 1693 O O   . HOH   C 3 .   ? 9.23926   -26.23575 -17.10219 1.000 36.77814 ? 437 HOH   A O   1 
HETATM 1694 O O   . HOH   C 3 .   ? 1.54081   -7.83947  -16.51365 1.000 25.92769 ? 438 HOH   A O   1 
HETATM 1695 O O   . HOH   C 3 .   ? 0.48522   -1.53050  -19.73807 1.000 40.86709 ? 439 HOH   A O   1 
HETATM 1696 O O   . HOH   C 3 .   ? 11.77208  -27.30812 -34.58801 1.000 31.45974 ? 440 HOH   A O   1 
HETATM 1697 O O   . HOH   C 3 .   ? -16.96064 -5.43098  -22.81350 1.000 30.99928 ? 441 HOH   A O   1 
HETATM 1698 O O   . HOH   C 3 .   ? -6.24238  -5.02586  -35.71746 1.000 29.23552 ? 442 HOH   A O   1 
HETATM 1699 O O   . HOH   C 3 .   ? 9.81140   -14.62496 -25.17390 1.000 26.89749 ? 443 HOH   A O   1 
HETATM 1700 O O   . HOH   C 3 .   ? 3.25267   -6.12354  -11.20160 1.000 24.26478 ? 444 HOH   A O   1 
HETATM 1701 O O   . HOH   C 3 .   ? -15.83734 0.24682   -30.44743 1.000 40.66314 ? 445 HOH   A O   1 
HETATM 1702 O O   . HOH   C 3 .   ? -5.65725  -2.16164  -19.28075 1.000 30.35988 ? 446 HOH   A O   1 
HETATM 1703 O O   . HOH   C 3 .   ? 20.20982  -10.51250 -26.29922 1.000 47.71626 ? 447 HOH   A O   1 
HETATM 1704 O O   . HOH   C 3 .   ? 3.84294   -29.81595 -26.19470 1.000 57.76412 ? 448 HOH   A O   1 
HETATM 1705 O O   . HOH   C 3 .   ? -6.42840  -14.16118 0.99824   1.000 35.99636 ? 449 HOH   A O   1 
HETATM 1706 O O   . HOH   C 3 .   ? -0.60298  -11.18183 -3.09122  1.000 37.22509 ? 450 HOH   A O   1 
HETATM 1707 O O   . HOH   C 3 .   ? -3.45339  -10.94720 -23.97016 1.000 35.21178 ? 451 HOH   A O   1 
HETATM 1708 O O   . HOH   C 3 .   ? -0.29913  -5.33867  -18.38015 1.000 30.55995 ? 452 HOH   A O   1 
HETATM 1709 O O   . HOH   C 3 .   ? -2.15234  -13.74034 -35.67991 1.000 25.03042 ? 453 HOH   A O   1 
HETATM 1710 O O   . HOH   C 3 .   ? 6.15747   -21.92327 -37.29941 1.000 39.42391 ? 454 HOH   A O   1 
HETATM 1711 O O   . HOH   C 3 .   ? 7.53571   1.39036   -15.21656 1.000 33.16249 ? 455 HOH   A O   1 
HETATM 1712 O O   . HOH   C 3 .   ? 10.97644  -25.50344 -26.83389 1.000 36.67846 ? 456 HOH   A O   1 
HETATM 1713 O O   . HOH   C 3 .   ? 7.83122   -23.36572 -7.35717  1.000 42.19152 ? 457 HOH   A O   1 
HETATM 1714 O O   . HOH   C 3 .   ? -8.00788  1.62281   -36.65158 1.000 40.93803 ? 458 HOH   A O   1 
HETATM 1715 O O   . HOH   C 3 .   ? 13.03327  -13.72062 -29.69564 1.000 32.67399 ? 459 HOH   A O   1 
HETATM 1716 O O   . HOH   C 3 .   ? -6.06071  -11.42374 -10.02039 1.000 27.36651 ? 460 HOH   A O   1 
HETATM 1717 O O   . HOH   C 3 .   ? -9.16527  -2.39498  -17.36021 1.000 26.21199 ? 461 HOH   A O   1 
HETATM 1718 O O   . HOH   C 3 .   ? -13.05583 -7.42837  -12.08481 1.000 28.94272 ? 462 HOH   A O   1 
HETATM 1719 O O   . HOH   C 3 .   ? 0.81416   -29.69441 -16.05752 1.000 41.44716 ? 463 HOH   A O   1 
HETATM 1720 O O   . HOH   C 3 .   ? -8.83257  -10.48338 -40.43667 1.000 50.03002 ? 464 HOH   A O   1 
HETATM 1721 O O   . HOH   C 3 .   ? -4.14640  -4.94475  -8.15746  1.000 43.25368 ? 465 HOH   A O   1 
HETATM 1722 O O   . HOH   C 3 .   ? -16.25203 -12.67799 -19.80939 1.000 25.22870 ? 466 HOH   A O   1 
HETATM 1723 O O   . HOH   C 3 .   ? -1.14564  -7.31862  -23.67889 1.000 31.84202 ? 467 HOH   A O   1 
HETATM 1724 O O   . HOH   C 3 .   ? -8.08773  -24.85102 -19.17140 1.000 25.25377 ? 468 HOH   A O   1 
HETATM 1725 O O   . HOH   C 3 .   ? 6.75321   -26.71685 -27.70508 1.000 40.03201 ? 469 HOH   A O   1 
HETATM 1726 O O   . HOH   C 3 .   ? 0.96678   -21.14621 -4.61586  1.000 30.83935 ? 470 HOH   A O   1 
HETATM 1727 O O   . HOH   C 3 .   ? 13.72139  -14.04266 -26.86210 1.000 26.78364 ? 471 HOH   A O   1 
HETATM 1728 O O   . HOH   C 3 .   ? -13.50218 -29.27975 -16.65389 1.000 56.14686 ? 472 HOH   A O   1 
HETATM 1729 O O   . HOH   C 3 .   ? 11.17862  -8.14564  -27.61310 1.000 27.51525 ? 473 HOH   A O   1 
HETATM 1730 O O   . HOH   C 3 .   ? 11.47927  -28.21008 -30.36730 1.000 44.28758 ? 474 HOH   A O   1 
HETATM 1731 O O   . HOH   C 3 .   ? 18.17081  -6.94974  -20.34119 1.000 29.38650 ? 475 HOH   A O   1 
HETATM 1732 O O   . HOH   C 3 .   ? -2.02127  -0.55529  -18.75660 1.000 43.39607 ? 476 HOH   A O   1 
HETATM 1733 O O   . HOH   C 3 .   ? 2.97419   -20.44463 -2.83342  1.000 36.24086 ? 477 HOH   A O   1 
HETATM 1734 O O   . HOH   C 3 .   ? -6.37479  -7.77302  -34.40902 1.000 26.93907 ? 478 HOH   A O   1 
HETATM 1735 O O   . HOH   C 3 .   ? 3.61810   -7.74598  -36.79104 1.000 41.64774 ? 479 HOH   A O   1 
HETATM 1736 O O   . HOH   C 3 .   ? 14.07865  -16.02663 -1.99773  1.000 40.98050 ? 480 HOH   A O   1 
HETATM 1737 O O   . HOH   C 3 .   ? 19.44593  0.42209   -9.63302  1.000 36.15193 ? 481 HOH   A O   1 
HETATM 1738 O O   . HOH   C 3 .   ? -14.50408 -22.71474 -11.43183 1.000 36.47326 ? 482 HOH   A O   1 
HETATM 1739 O O   . HOH   C 3 .   ? -19.677   -19.523   -14.213   1.000 27.96714 ? 483 HOH   A O   1 
HETATM 1740 O O   . HOH   C 3 .   ? -18.88804 -11.00837 -23.67404 1.000 39.88805 ? 484 HOH   A O   1 
HETATM 1741 O O   . HOH   C 3 .   ? -14.090   -0.864    -13.513   1.000 27.60009 ? 485 HOH   A O   1 
HETATM 1742 O O   . HOH   C 3 .   ? 1.46990   -3.88875  -16.89404 1.000 47.75648 ? 486 HOH   A O   1 
HETATM 1743 O O   . HOH   C 3 .   ? 14.62083  -15.83721 -30.67924 1.000 38.16712 ? 487 HOH   A O   1 
HETATM 1744 O O   . HOH   C 3 .   ? 1.52487   -26.35023 -2.76099  1.000 50.60554 ? 488 HOH   A O   1 
HETATM 1745 O O   . HOH   C 3 .   ? 15.76323  -0.55479  -19.86542 1.000 32.19152 ? 489 HOH   A O   1 
HETATM 1746 O O   . HOH   C 3 .   ? -5.72605  -31.31353 -11.66308 1.000 38.29108 ? 490 HOH   A O   1 
HETATM 1747 O O   . HOH   C 3 .   ? 1.16177   -6.13832  -34.03657 1.000 48.91408 ? 491 HOH   A O   1 
HETATM 1748 O O   . HOH   C 3 .   ? -8.33319  4.68500   -33.73998 1.000 38.59243 ? 492 HOH   A O   1 
HETATM 1749 O O   . HOH   C 3 .   ? -3.34568  -12.15681 -8.96727  1.000 34.11090 ? 493 HOH   A O   1 
HETATM 1750 O O   . HOH   C 3 .   ? -14.65645 -7.48364  -14.44821 1.000 33.74761 ? 494 HOH   A O   1 
HETATM 1751 O O   . HOH   C 3 .   ? -10.27476 -11.66153 -2.10078  1.000 26.15507 ? 495 HOH   A O   1 
HETATM 1752 O O   . HOH   C 3 .   ? -5.34277  -7.61699  -13.14537 1.000 21.49238 ? 496 HOH   A O   1 
HETATM 1753 O O   . HOH   C 3 .   ? -6.55756  -5.17877  -39.17042 1.000 49.94470 ? 497 HOH   A O   1 
HETATM 1754 O O   . HOH   C 3 .   ? 0.11639   -30.49850 -23.82966 1.000 50.76027 ? 498 HOH   A O   1 
HETATM 1755 O O   . HOH   C 3 .   ? 17.43138  -11.14376 -8.64207  1.000 36.09564 ? 499 HOH   A O   1 
HETATM 1756 O O   . HOH   C 3 .   ? 4.48025   -19.49172 -40.67368 1.000 39.89084 ? 500 HOH   A O   1 
HETATM 1757 O O   . HOH   C 3 .   ? -15.16160 -11.07529 -29.79781 1.000 35.76666 ? 501 HOH   A O   1 
HETATM 1758 O O   . HOH   C 3 .   ? 3.80185   -11.96381 -38.62901 1.000 31.08616 ? 502 HOH   A O   1 
HETATM 1759 O O   . HOH   C 3 .   ? -3.91641  0.08160   -22.02512 1.000 40.80274 ? 503 HOH   A O   1 
HETATM 1760 O O   . HOH   C 3 .   ? 8.93069   -15.38218 -27.78921 1.000 24.74459 ? 504 HOH   A O   1 
HETATM 1761 O O   . HOH   C 3 .   ? -13.32385 -0.73439  -20.65313 1.000 39.47866 ? 505 HOH   A O   1 
HETATM 1762 O O   . HOH   C 3 .   ? 15.57648  -20.05743 -18.70980 1.000 31.68416 ? 506 HOH   A O   1 
HETATM 1763 O O   . HOH   C 3 .   ? 20.67458  -16.61026 -20.02799 1.000 37.65226 ? 507 HOH   A O   1 
HETATM 1764 O O   . HOH   C 3 .   ? -5.26503  -5.38866  -11.76762 1.000 43.25341 ? 508 HOH   A O   1 
HETATM 1765 O O   . HOH   C 3 .   ? -7.72264  -24.27458 -23.21083 1.000 36.90633 ? 509 HOH   A O   1 
HETATM 1766 O O   . HOH   C 3 .   ? 18.60953  -6.82487  -9.49887  1.000 36.04340 ? 510 HOH   A O   1 
HETATM 1767 O O   . HOH   C 3 .   ? -2.53349  -15.84171 -0.26819  1.000 44.84344 ? 511 HOH   A O   1 
HETATM 1768 O O   . HOH   C 3 .   ? 10.76572  -25.20794 -23.70001 1.000 32.48107 ? 512 HOH   A O   1 
HETATM 1769 O O   . HOH   C 3 .   ? -20.60300 -14.18962 -18.28236 1.000 44.45507 ? 513 HOH   A O   1 
HETATM 1770 O O   . HOH   C 3 .   ? -2.34165  -10.62974 -26.56837 1.000 37.64007 ? 514 HOH   A O   1 
HETATM 1771 O O   . HOH   C 3 .   ? -14.04250 -12.58765 -7.81341  1.000 28.83490 ? 515 HOH   A O   1 
HETATM 1772 O O   . HOH   C 3 .   ? 0.87012   -27.01413 -37.25162 1.000 51.74335 ? 516 HOH   A O   1 
HETATM 1773 O O   . HOH   C 3 .   ? 18.11456  -19.19499 -24.50951 1.000 40.53541 ? 517 HOH   A O   1 
HETATM 1774 O O   . HOH   C 3 .   ? 8.63000   -16.24174 -39.55726 1.000 41.98646 ? 518 HOH   A O   1 
HETATM 1775 O O   . HOH   C 3 .   ? -13.34821 -26.51825 -18.17167 1.000 33.34707 ? 519 HOH   A O   1 
HETATM 1776 O O   . HOH   C 3 .   ? 18.40554  -18.64980 -11.38139 1.000 49.69420 ? 520 HOH   A O   1 
HETATM 1777 O O   . HOH   C 3 .   ? 10.05707  -14.97855 -7.71029  1.000 30.42406 ? 521 HOH   A O   1 
HETATM 1778 O O   . HOH   C 3 .   ? -10.98009 -14.20898 -37.83301 1.000 41.15848 ? 522 HOH   A O   1 
HETATM 1779 O O   . HOH   C 3 .   ? -13.70224 -17.06441 -2.69944  1.000 31.58350 ? 523 HOH   A O   1 
HETATM 1780 O O   . HOH   C 3 .   ? -3.38653  -21.19716 -0.47268  1.000 40.30923 ? 524 HOH   A O   1 
HETATM 1781 O O   . HOH   C 3 .   ? 0.57698   -5.27612  -14.14628 1.000 42.70709 ? 525 HOH   A O   1 
HETATM 1782 O O   . HOH   C 3 .   ? 14.31667  -24.13435 -17.29745 1.000 47.26536 ? 526 HOH   A O   1 
HETATM 1783 O O   . HOH   C 3 .   ? -16.05002 -3.17330  -21.18909 1.000 37.26028 ? 527 HOH   A O   1 
HETATM 1784 O O   . HOH   C 3 .   ? -1.83336  -25.75471 -4.73610  1.000 29.28511 ? 528 HOH   A O   1 
HETATM 1785 O O   . HOH   C 3 .   ? -5.09437  -14.21819 -22.66381 1.000 24.00683 ? 529 HOH   A O   1 
HETATM 1786 O O   . HOH   C 3 .   ? -12.16926 -25.81019 -3.43197  1.000 50.98357 ? 530 HOH   A O   1 
HETATM 1787 O O   . HOH   C 3 .   ? -0.34206  -6.99971  -30.94789 1.000 47.16681 ? 531 HOH   A O   1 
HETATM 1788 O O   . HOH   C 3 .   ? -5.81062  -18.95806 -39.20036 1.000 40.46330 ? 532 HOH   A O   1 
HETATM 1789 O O   . HOH   C 3 .   ? -10.03287 -14.96161 -28.41579 1.000 35.12103 ? 533 HOH   A O   1 
HETATM 1790 O O   . HOH   C 3 .   ? -14.57189 -4.78911  -12.55207 1.000 32.62052 ? 534 HOH   A O   1 
HETATM 1791 O O   . HOH   C 3 .   ? 7.24607   -8.93838  -3.71797  1.000 26.58139 ? 535 HOH   A O   1 
HETATM 1792 O O   . HOH   C 3 .   ? 13.85217  -20.28433 -20.69390 1.000 26.16278 ? 536 HOH   A O   1 
HETATM 1793 O O   . HOH   C 3 .   ? -16.86475 -20.36202 -4.83170  1.000 46.92415 ? 537 HOH   A O   1 
HETATM 1794 O O   . HOH   C 3 .   ? 4.14537   -9.15456  -20.31203 1.000 25.72940 ? 538 HOH   A O   1 
HETATM 1795 O O   . HOH   C 3 .   ? 12.53820  -27.21593 -19.50357 1.000 47.99094 ? 539 HOH   A O   1 
HETATM 1796 O O   . HOH   C 3 .   ? -3.40132  -13.05139 -20.65984 1.000 30.42100 ? 540 HOH   A O   1 
HETATM 1797 O O   . HOH   C 3 .   ? 4.18293   -24.10136 -30.62233 1.000 28.21727 ? 541 HOH   A O   1 
HETATM 1798 O O   . HOH   C 3 .   ? 1.38057   -8.60916  -26.78912 1.000 43.15697 ? 542 HOH   A O   1 
HETATM 1799 O O   . HOH   C 3 .   ? 18.34835  -10.77368 -17.32223 1.000 31.21220 ? 543 HOH   A O   1 
HETATM 1800 O O   . HOH   C 3 .   ? 0.54551   -5.46253  -21.91530 1.000 40.95735 ? 544 HOH   A O   1 
HETATM 1801 O O   . HOH   C 3 .   ? 0.61407   -14.61323 -1.22944  1.000 42.59840 ? 545 HOH   A O   1 
HETATM 1802 O O   . HOH   C 3 .   ? -17.67881 -18.51515 -11.26437 1.000 38.97897 ? 546 HOH   A O   1 
HETATM 1803 O O   . HOH   C 3 .   ? -4.46026  0.39689   -30.59957 1.000 36.39094 ? 547 HOH   A O   1 
HETATM 1804 O O   . HOH   C 3 .   ? 10.53747  -21.54577 -6.98241  1.000 44.88154 ? 548 HOH   A O   1 
HETATM 1805 O O   . HOH   C 3 .   ? -2.30642  -24.87715 -1.03262  1.000 54.17739 ? 549 HOH   A O   1 
HETATM 1806 O O   . HOH   C 3 .   ? -10.46419 -6.74780  -2.62795  1.000 42.86457 ? 550 HOH   A O   1 
HETATM 1807 O O   . HOH   C 3 .   ? 15.74158  -18.73780 -3.56070  1.000 32.48939 ? 551 HOH   A O   1 
HETATM 1808 O O   . HOH   C 3 .   ? -11.83864 -7.73331  -38.40227 1.000 42.63765 ? 552 HOH   A O   1 
HETATM 1809 O O   . HOH   C 3 .   ? 3.59416   -6.63686  -17.92075 1.000 25.93053 ? 553 HOH   A O   1 
HETATM 1810 O O   . HOH   C 3 .   ? -0.86713  -25.88443 -32.63721 1.000 47.07933 ? 554 HOH   A O   1 
HETATM 1811 O O   . HOH   C 3 .   ? 8.29909   -20.67003 -9.63570  1.000 34.42446 ? 555 HOH   A O   1 
HETATM 1812 O O   . HOH   C 3 .   ? -3.09379  -1.02401  -24.02657 1.000 34.40983 ? 556 HOH   A O   1 
HETATM 1813 O O   . HOH   C 3 .   ? -9.08876  -18.03875 -36.47190 1.000 52.11416 ? 557 HOH   A O   1 
HETATM 1814 O O   . HOH   C 3 .   ? -17.67233 -15.18736 -13.12890 1.000 30.54900 ? 558 HOH   A O   1 
HETATM 1815 O O   . HOH   C 3 .   ? 17.26164  -24.58837 -25.20939 1.000 43.03981 ? 559 HOH   A O   1 
HETATM 1816 O O   . HOH   C 3 .   ? -1.50505  -6.31896  -26.12072 1.000 30.12846 ? 560 HOH   A O   1 
HETATM 1817 O O   . HOH   C 3 .   ? -1.62063  -32.66182 -8.06289  1.000 51.16940 ? 561 HOH   A O   1 
HETATM 1818 O O   . HOH   C 3 .   ? -15.20048 -12.04349 -11.96640 1.000 38.43712 ? 562 HOH   A O   1 
HETATM 1819 O O   . HOH   C 3 .   ? -1.03216  -29.92167 -17.39022 1.000 41.44818 ? 563 HOH   A O   1 
HETATM 1820 O O   . HOH   C 3 .   ? 20.96854  -14.15733 -26.62298 1.000 35.79090 ? 564 HOH   A O   1 
HETATM 1821 O O   . HOH   C 3 .   ? 8.77329   -20.72240 -4.27779  1.000 32.28675 ? 565 HOH   A O   1 
HETATM 1822 O O   . HOH   C 3 .   ? 8.91764   -19.97979 -41.63061 1.000 52.52534 ? 566 HOH   A O   1 
HETATM 1823 O O   . HOH   C 3 .   ? -13.47440 -25.88021 -7.82467  1.000 33.82638 ? 567 HOH   A O   1 
HETATM 1824 O O   . HOH   C 3 .   ? -8.22424  -3.99529  -10.75576 1.000 28.62617 ? 568 HOH   A O   1 
HETATM 1825 O O   . HOH   C 3 .   ? -20.770   -27.957   -11.122   1.000 62.27715 ? 569 HOH   A O   1 
HETATM 1826 O O   . HOH   C 3 .   ? -5.19633  -31.73649 -7.48044  1.000 47.70367 ? 570 HOH   A O   1 
HETATM 1827 O O   . HOH   C 3 .   ? -17.003   -28.872   -17.306   1.000 43.45758 ? 571 HOH   A O   1 
HETATM 1828 O O   . HOH   C 3 .   ? 13.33745  -6.85102  -26.41970 1.000 28.69120 ? 572 HOH   A O   1 
HETATM 1829 O O   . HOH   C 3 .   ? -14.36649 -29.46220 -9.51268  1.000 52.25185 ? 573 HOH   A O   1 
HETATM 1830 O O   . HOH   C 3 .   ? 10.98495  -8.40547  -3.56157  1.000 37.43150 ? 574 HOH   A O   1 
HETATM 1831 O O   . HOH   C 3 .   ? -0.36023  -12.26007 -21.53531 1.000 45.98690 ? 575 HOH   A O   1 
HETATM 1832 O O   . HOH   C 3 .   ? -13.67975 -18.54480 -24.50126 1.000 28.91542 ? 576 HOH   A O   1 
HETATM 1833 O O   . HOH   C 3 .   ? -7.67583  -5.45401  -2.52493  1.000 52.04836 ? 577 HOH   A O   1 
HETATM 1834 O O   . HOH   C 3 .   ? 2.47793   -29.71560 -34.61037 1.000 54.89961 ? 578 HOH   A O   1 
HETATM 1835 O O   . HOH   C 3 .   ? 3.01861   -4.81610  -6.56606  1.000 45.63791 ? 579 HOH   A O   1 
HETATM 1836 O O   . HOH   C 3 .   ? -1.11018  -4.49301  -33.56088 1.000 49.43113 ? 580 HOH   A O   1 
HETATM 1837 O O   . HOH   C 3 .   ? 19.78111  -4.19911  -15.10581 1.000 39.93522 ? 581 HOH   A O   1 
HETATM 1838 O O   . HOH   C 3 .   ? -16.61373 -9.23132  -14.23652 1.000 42.56166 ? 582 HOH   A O   1 
HETATM 1839 O O   . HOH   C 3 .   ? -15.97230 -4.34974  -15.73156 1.000 39.91780 ? 583 HOH   A O   1 
HETATM 1840 O O   . HOH   C 3 .   ? -17.87173 -5.59202  -25.56687 1.000 39.98179 ? 584 HOH   A O   1 
HETATM 1841 O O   . HOH   C 3 .   ? 2.63443   -3.33026  -10.65150 1.000 48.94540 ? 585 HOH   A O   1 
HETATM 1842 O O   . HOH   C 3 .   ? -15.94734 -25.56078 -10.77158 1.000 41.74195 ? 586 HOH   A O   1 
HETATM 1843 O O   . HOH   C 3 .   ? 13.60374  -3.99783  -25.74417 1.000 22.82134 ? 587 HOH   A O   1 
HETATM 1844 O O   . HOH   C 3 .   ? -1.54033  -8.62509  -27.81051 1.000 36.82651 ? 588 HOH   A O   1 
HETATM 1845 O O   . HOH   C 3 .   ? 5.16099   -30.55201 -11.65595 1.000 49.18109 ? 589 HOH   A O   1 
HETATM 1846 O O   . HOH   C 3 .   ? -3.02585  -31.27649 -20.46688 1.000 54.49152 ? 590 HOH   A O   1 
HETATM 1847 O O   . HOH   C 3 .   ? -7.00167  1.09444   -19.01491 1.000 44.24763 ? 591 HOH   A O   1 
HETATM 1848 O O   . HOH   C 3 .   ? 19.95811  -16.23311 -27.65954 1.000 45.72559 ? 592 HOH   A O   1 
HETATM 1849 O O   . HOH   C 3 .   ? -14.16354 -24.08315 -4.92066  1.000 32.68807 ? 593 HOH   A O   1 
HETATM 1850 O O   . HOH   C 3 .   ? -13.02268 -12.22784 -31.03501 1.000 31.73163 ? 594 HOH   A O   1 
HETATM 1851 O O   . HOH   C 3 .   ? -12.15787 -26.86632 -20.45243 1.000 34.02617 ? 595 HOH   A O   1 
HETATM 1852 O O   . HOH   C 3 .   ? 6.12039   -4.92108  -23.03131 1.000 39.71214 ? 596 HOH   A O   1 
HETATM 1853 O O   . HOH   C 3 .   ? -7.54444  7.56325   -33.94863 1.000 47.64725 ? 597 HOH   A O   1 
HETATM 1854 O O   . HOH   C 3 .   ? 0.19184   -16.95119 -3.40625  1.000 29.59125 ? 598 HOH   A O   1 
HETATM 1855 O O   . HOH   C 3 .   ? 7.68077   1.92362   -12.64765 1.000 34.83095 ? 599 HOH   A O   1 
HETATM 1856 O O   . HOH   C 3 .   ? 4.02524   -22.85776 -3.45397  1.000 43.50799 ? 600 HOH   A O   1 
HETATM 1857 O O   . HOH   C 3 .   ? -18.22508 -10.58809 -14.82243 1.000 55.41545 ? 601 HOH   A O   1 
HETATM 1858 O O   . HOH   C 3 .   ? 14.05065  -11.22488 -29.86949 1.000 48.15328 ? 602 HOH   A O   1 
HETATM 1859 O O   . HOH   C 3 .   ? 17.88241  -15.42109 -29.54823 1.000 53.26778 ? 603 HOH   A O   1 
HETATM 1860 O O   . HOH   C 3 .   ? 15.48046  -7.06820  -28.00973 1.000 41.13802 ? 604 HOH   A O   1 
HETATM 1861 O O   . HOH   C 3 .   ? 8.34986   -25.65301 -25.97769 1.000 39.95159 ? 605 HOH   A O   1 
HETATM 1862 O O   . HOH   C 3 .   ? -5.61775  -12.35613 -41.90957 1.000 52.13056 ? 606 HOH   A O   1 
HETATM 1863 O O   . HOH   C 3 .   ? 10.64770  -17.48849 -38.74950 1.000 54.20073 ? 607 HOH   A O   1 
HETATM 1864 O O   . HOH   C 3 .   ? -18.37312 -15.60509 -21.47257 1.000 46.57252 ? 608 HOH   A O   1 
HETATM 1865 O O   . HOH   C 3 .   ? 4.40295   -1.79611  -18.29670 1.000 42.93519 ? 609 HOH   A O   1 
HETATM 1866 O O   . HOH   C 3 .   ? 5.46492   1.82220   -16.56092 1.000 46.90929 ? 610 HOH   A O   1 
HETATM 1867 O O   . HOH   C 3 .   ? 1.77875   -18.50617 0.06129   1.000 37.76538 ? 611 HOH   A O   1 
HETATM 1868 O O   . HOH   C 3 .   ? 2.37638   -26.00886 -29.25752 1.000 47.11032 ? 612 HOH   A O   1 
HETATM 1869 O O   . HOH   C 3 .   ? 9.17023   -0.59035  -3.25556  1.000 49.04423 ? 613 HOH   A O   1 
HETATM 1870 O O   . HOH   C 3 .   ? -16.36566 -28.37437 -9.83063  1.000 56.78531 ? 614 HOH   A O   1 
HETATM 1871 O O   . HOH   C 3 .   ? 1.57354   -3.02021  -24.30853 1.000 48.86769 ? 615 HOH   A O   1 
HETATM 1872 O O   . HOH   C 3 .   ? 16.77950  -27.55818 -22.38284 1.000 54.11655 ? 616 HOH   A O   1 
HETATM 1873 O O   . HOH   C 3 .   ? -4.82571  -14.32513 -0.65769  1.000 53.30476 ? 617 HOH   A O   1 
HETATM 1874 O O   . HOH   C 3 .   ? 14.65207  -22.24981 -17.13727 1.000 40.19284 ? 618 HOH   A O   1 
HETATM 1875 O O   . HOH   C 3 .   ? -2.11263  -26.89537 -24.91196 1.000 50.33762 ? 619 HOH   A O   1 
HETATM 1876 O O   . HOH   C 3 .   ? 5.439     -3.134    -26.195   1.000 45.28670 ? 620 HOH   A O   1 
HETATM 1877 O O   . HOH   C 3 .   ? -6.07267  -11.24550 1.45950   1.000 41.49456 ? 621 HOH   A O   1 
HETATM 1878 O O   . HOH   C 3 .   ? 12.91614  -22.82310 -4.66115  1.000 54.05433 ? 622 HOH   A O   1 
HETATM 1879 O O   . HOH   C 3 .   ? 2.74329   -10.20558 -23.12641 1.000 38.60723 ? 623 HOH   A O   1 
HETATM 1880 O O   . HOH   C 3 .   ? -18.117   -15.865   -23.370   1.000 39.47412 ? 624 HOH   A O   1 
HETATM 1881 O O   . HOH   C 3 .   ? 20.48379  -4.48768  -12.62308 1.000 47.14594 ? 625 HOH   A O   1 
HETATM 1882 O O   . HOH   C 3 .   ? -11.83915 -20.52113 -25.23859 1.000 48.21523 ? 626 HOH   A O   1 
HETATM 1883 O O   . HOH   C 3 .   ? -18.295   -36.881   -19.593   1.000 47.53369 ? 627 HOH   A O   1 
HETATM 1884 O O   . HOH   C 3 .   ? -12.17835 -16.22799 -28.27819 1.000 38.54046 ? 628 HOH   A O   1 
HETATM 1885 O O   . HOH   C 3 .   ? 0.02674   -19.21635 -2.05658  1.000 44.05048 ? 629 HOH   A O   1 
HETATM 1886 O O   . HOH   C 3 .   ? 2.85125   -5.49856  -20.43498 1.000 44.55396 ? 630 HOH   A O   1 
HETATM 1887 O O   . HOH   C 3 .   ? -15.181   -2.123    -11.150   1.000 34.72403 ? 631 HOH   A O   1 
HETATM 1888 O O   . HOH   C 3 .   ? -3.56367  -33.04452 -10.99536 1.000 57.17336 ? 632 HOH   A O   1 
HETATM 1889 O O   . HOH   C 3 .   ? -17.43671 -4.51529  -17.62889 1.000 49.48456 ? 633 HOH   A O   1 
HETATM 1890 O O   . HOH   C 3 .   ? -13.98410 -9.62791  -8.32756  1.000 34.69748 ? 634 HOH   A O   1 
HETATM 1891 O O   . HOH   C 3 .   ? 17.81770  -8.97762  -7.46331  1.000 49.33305 ? 635 HOH   A O   1 
HETATM 1892 O O   . HOH   C 3 .   ? -0.42029  -29.65317 -3.58816  1.000 56.36025 ? 636 HOH   A O   1 
HETATM 1893 O O   . HOH   C 3 .   ? 2.41583   -3.87003  -8.37564  1.000 51.35486 ? 637 HOH   A O   1 
HETATM 1894 O O   . HOH   C 3 .   ? 12.46167  -25.23571 -38.38238 1.000 36.53784 ? 638 HOH   A O   1 
HETATM 1895 O O   . HOH   C 3 .   ? -9.75275  -26.18083 -20.99177 1.000 33.75822 ? 639 HOH   A O   1 
HETATM 1896 O O   . HOH   C 3 .   ? -14.11908 -14.35607 -3.15724  1.000 44.43394 ? 640 HOH   A O   1 
HETATM 1897 O O   . HOH   C 3 .   ? -15.181   -23.600   -30.202   1.000 47.37846 ? 641 HOH   A O   1 
HETATM 1898 O O   . HOH   C 3 .   ? -0.42145  -0.98487  -22.91573 1.000 52.86876 ? 642 HOH   A O   1 
HETATM 1899 O O   . HOH   C 3 .   ? 7.74473   -13.93101 -38.31659 1.000 39.61492 ? 643 HOH   A O   1 
HETATM 1900 O O   . HOH   C 3 .   ? 7.81075   -28.94475 -28.52143 1.000 53.25506 ? 644 HOH   A O   1 
HETATM 1901 O O   . HOH   C 3 .   ? -3.43386  -27.31182 -3.20914  1.000 52.98249 ? 645 HOH   A O   1 
HETATM 1902 O O   . HOH   C 3 .   ? -18.57012 -11.83691 -21.05267 1.000 34.82491 ? 646 HOH   A O   1 
HETATM 1903 O O   . HOH   C 3 .   ? -8.67168  -5.56631  -39.92598 1.000 51.28316 ? 647 HOH   A O   1 
HETATM 1904 O O   . HOH   C 3 .   ? 18.69427  -7.96518  -17.71665 1.000 36.23137 ? 648 HOH   A O   1 
HETATM 1905 O O   . HOH   C 3 .   ? 1.11564   -11.58378 -23.58065 1.000 43.36012 ? 649 HOH   A O   1 
HETATM 1906 O O   . HOH   C 3 .   ? 3.53185   -9.27041  -39.25573 1.000 43.94136 ? 650 HOH   A O   1 
HETATM 1907 O O   . HOH   C 3 .   ? 17.48074  -11.17523 -14.82134 1.000 38.59801 ? 651 HOH   A O   1 
HETATM 1908 O O   . HOH   C 3 .   ? -6.833    -23.308   -1.509    1.000 44.50950 ? 652 HOH   A O   1 
HETATM 1909 O O   . HOH   C 3 .   ? -6.18384  6.91258   -36.29939 1.000 54.09654 ? 653 HOH   A O   1 
HETATM 1910 O O   . HOH   C 3 .   ? 19.82505  -11.20319 -13.56753 1.000 49.34421 ? 654 HOH   A O   1 
HETATM 1911 O O   . HOH   C 3 .   ? 1.26952   -2.86522  -12.98293 1.000 44.21120 ? 655 HOH   A O   1 
HETATM 1912 O O   . HOH   C 3 .   ? 5.82766   -13.08599 -39.90052 1.000 39.13953 ? 656 HOH   A O   1 
HETATM 1913 O O   . HOH   C 3 .   ? -16.51145 -5.69867  -13.45364 1.000 46.24728 ? 657 HOH   A O   1 
HETATM 1914 O O   . HOH   C 3 .   ? 6.39843   -30.00599 -24.76991 1.000 54.00820 ? 658 HOH   A O   1 
HETATM 1915 O O   . HOH   C 3 .   ? 17.74856  2.65477   -10.78891 1.000 48.79347 ? 659 HOH   A O   1 
HETATM 1916 O O   . HOH   C 3 .   ? 22.64240  -15.32531 -19.15342 1.000 51.82659 ? 660 HOH   A O   1 
HETATM 1917 O O   . HOH   C 3 .   ? -10.38502 -8.91324  -1.35557  1.000 42.13804 ? 661 HOH   A O   1 
HETATM 1918 O O   . HOH   C 3 .   ? 6.61287   -21.66530 -2.69586  1.000 42.28142 ? 662 HOH   A O   1 
HETATM 1919 O O   . HOH   C 3 .   ? -6.92043  -30.74333 -9.19615  1.000 39.35949 ? 663 HOH   A O   1 
HETATM 1920 O O   . HOH   C 3 .   ? -10.713   -22.803   4.357     1.000 52.88689 ? 664 HOH   A O   1 
HETATM 1921 O O   . HOH   C 3 .   ? -16.270   3.081     -26.421   1.000 43.19406 ? 665 HOH   A O   1 
HETATM 1922 O O   . HOH   C 3 .   ? -0.00000  -0.00000  -18.55151 0.50  26.67656 ? 666 HOH   A O   1 
HETATM 1923 O O   . HOH   C 3 .   ? -16.40037 -18.54357 -2.98197  1.000 52.98205 ? 667 HOH   A O   1 
HETATM 1924 O O   . HOH   C 3 .   ? 2.95753   -2.36816  -20.66240 1.000 46.44577 ? 668 HOH   A O   1 
HETATM 1925 O O   . HOH   C 3 .   ? 13.085    -15.036   0.678     1.000 48.78651 ? 669 HOH   A O   1 
HETATM 1926 O O   . HOH   C 3 .   ? 20.39016  -5.65798  -21.15407 1.000 44.74806 ? 670 HOH   A O   1 
HETATM 1927 O O   . HOH   C 3 .   ? -16.04515 -12.62880 -6.14373  1.000 42.70220 ? 671 HOH   A O   1 
HETATM 1928 O O   . HOH   C 3 .   ? 11.10456  -27.93155 -27.75427 1.000 46.53888 ? 672 HOH   A O   1 
HETATM 1929 O O   . HOH   C 3 .   ? 9.69440   -12.50816 -37.25167 1.000 45.66679 ? 673 HOH   A O   1 
HETATM 1930 O O   . HOH   C 3 .   ? 15.63405  -9.29170  -5.95746  1.000 51.39998 ? 674 HOH   A O   1 
HETATM 1931 O O   . HOH   C 3 .   ? 11.51342  -30.05464 -34.09411 1.000 49.86792 ? 675 HOH   A O   1 
HETATM 1932 O O   . HOH   C 3 .   ? 14.14432  -8.23660  -4.20261  1.000 50.81582 ? 676 HOH   A O   1 
HETATM 1933 O O   . HOH   C 3 .   ? -12.48622 -13.06598 -1.29819  1.000 38.90176 ? 677 HOH   A O   1 
HETATM 1934 O O   . HOH   C 3 .   ? -15.98098 -13.69143 -3.91206  1.000 55.99164 ? 678 HOH   A O   1 
HETATM 1935 O O   . HOH   C 3 .   ? 0.56862   -1.39522  -16.86655 1.000 38.50857 ? 679 HOH   A O   1 
HETATM 1936 O O   . HOH   C 3 .   ? 9.74246   -25.13178 -14.86845 1.000 45.82648 ? 680 HOH   A O   1 
HETATM 1937 O O   . HOH   C 3 .   ? -1.217    1.518     -33.151   1.000 55.57289 ? 681 HOH   A O   1 
HETATM 1938 O O   . HOH   C 3 .   ? -18.365   -16.247   -26.247   1.000 51.62854 ? 682 HOH   A O   1 
HETATM 1939 O O   . HOH   C 3 .   ? 4.91394   -14.80628 -41.58906 1.000 44.47354 ? 683 HOH   A O   1 
HETATM 1940 O O   . HOH   C 3 .   ? -8.87528  -11.26986 0.19809   1.000 47.73775 ? 684 HOH   A O   1 
HETATM 1941 O O   . HOH   C 3 .   ? 3.937     -2.023    -28.526   1.000 46.90166 ? 685 HOH   A O   1 
HETATM 1942 O O   . HOH   C 3 .   ? -14.41044 -14.07484 -10.20376 1.000 32.09080 ? 686 HOH   A O   1 
HETATM 1943 O O   . HOH   C 3 .   ? -0.74056  -2.63262  -31.35356 1.000 48.86639 ? 687 HOH   A O   1 
HETATM 1944 O O   . HOH   C 3 .   ? 19.28740  -20.16531 -22.21130 1.000 40.47861 ? 688 HOH   A O   1 
HETATM 1945 O O   . HOH   C 3 .   ? -16.79062 -15.71307 -10.34397 1.000 40.88567 ? 689 HOH   A O   1 
HETATM 1946 O O   . HOH   C 3 .   ? -14.58033 -9.37503  -11.10898 1.000 34.33578 ? 690 HOH   A O   1 
HETATM 1947 O O   . HOH   C 3 .   ? -21.04900 -12.59604 -24.88564 1.000 56.92227 ? 691 HOH   A O   1 
HETATM 1948 O O   . HOH   C 3 .   ? 20.32167  -6.61974  -16.10361 1.000 43.56175 ? 692 HOH   A O   1 
HETATM 1949 O O   . HOH   C 3 .   ? -19.57756 -5.93989  -21.74657 1.000 43.33895 ? 693 HOH   A O   1 
HETATM 1950 O O   . HOH   C 3 .   ? -15.73911 -8.08229  -6.90552  1.000 53.35506 ? 694 HOH   A O   1 
HETATM 1951 O O   . HOH   C 3 .   ? 10.66822  -10.47174 -2.03339  1.000 49.23971 ? 695 HOH   A O   1 
HETATM 1952 O O   . HOH   C 3 .   ? -21.00872 -7.51544  -20.70959 1.000 52.90480 ? 696 HOH   A O   1 
HETATM 1953 O O   . HOH   C 3 .   ? 21.07250  -8.17865  -13.97151 1.000 53.33325 ? 697 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   ? 0.67511 0.80225 0.57686 0.02721  -0.06366 -0.29892 16  GLU A N   
2    C CA  . GLU A 9   ? 0.83335 0.94880 0.72463 0.05206  -0.06056 -0.28169 16  GLU A CA  
3    C C   . GLU A 9   ? 0.71211 0.82682 0.61956 0.05961  -0.06166 -0.26381 16  GLU A C   
4    O O   . GLU A 9   ? 0.64722 0.79749 0.56458 0.06447  -0.07084 -0.25648 16  GLU A O   
5    C CB  . GLU A 9   ? 0.82988 0.98182 0.70672 0.07094  -0.06787 -0.27739 16  GLU A CB  
6    C CG  . GLU A 9   ? 0.93170 1.08474 0.80246 0.09658  -0.06662 -0.25446 16  GLU A CG  
7    C CD  . GLU A 9   ? 1.14103 1.25951 0.99660 0.10774  -0.05483 -0.24877 16  GLU A CD  
8    O OE1 . GLU A 9   ? 1.18663 1.28068 1.03274 0.09910  -0.04795 -0.26264 16  GLU A OE1 
9    O OE2 . GLU A 9   ? 1.01187 1.12737 0.86421 0.12509  -0.05109 -0.23007 16  GLU A OE2 
10   N N   . VAL A 10  ? 0.56159 0.63565 0.47105 0.06156  -0.05165 -0.25663 17  VAL A N   
11   C CA  . VAL A 10  ? 0.45522 0.52293 0.38016 0.06545  -0.05152 -0.24206 17  VAL A CA  
12   C C   . VAL A 10  ? 0.53596 0.59220 0.45286 0.08711  -0.04618 -0.22531 17  VAL A C   
13   O O   . VAL A 10  ? 0.56196 0.59215 0.46939 0.09280  -0.03655 -0.22540 17  VAL A O   
14   C CB  . VAL A 10  ? 0.56792 0.59850 0.50391 0.04920  -0.04302 -0.24654 17  VAL A CB  
15   C CG1 . VAL A 10  ? 0.51984 0.54736 0.47229 0.05268  -0.04399 -0.23223 17  VAL A CG1 
16   C CG2 . VAL A 10  ? 0.59487 0.62918 0.53439 0.02468  -0.04380 -0.26470 17  VAL A CG2 
17   N N   . GLU A 11  ? 0.42394 0.49829 0.34447 0.09848  -0.05040 -0.20923 18  GLU A N   
18   C CA  . GLU A 11  ? 0.41542 0.47927 0.33291 0.11349  -0.04280 -0.18833 18  GLU A CA  
19   C C   . GLU A 11  ? 0.36026 0.40665 0.29760 0.10823  -0.03860 -0.17254 18  GLU A C   
20   O O   . GLU A 11  ? 0.35278 0.40619 0.30333 0.09958  -0.04381 -0.16911 18  GLU A O   
21   C CB  . GLU A 11  ? 0.44692 0.53640 0.35296 0.12735  -0.04661 -0.17676 18  GLU A CB  
22   C CG  . GLU A 11  ? 0.45443 0.56268 0.33729 0.13668  -0.04985 -0.18906 18  GLU A CG  
23   C CD  . GLU A 11  ? 0.62098 0.75207 0.48890 0.15325  -0.05225 -0.17521 18  GLU A CD  
24   O OE1 . GLU A 11  ? 0.60132 0.75479 0.47262 0.15371  -0.06075 -0.17384 18  GLU A OE1 
25   O OE2 . GLU A 11  ? 0.71355 0.83993 0.56551 0.16645  -0.04448 -0.16484 18  GLU A OE2 
26   N N   . THR A 12  ? 0.36189 0.38859 0.30129 0.11435  -0.02911 -0.16305 19  THR A N   
27   C CA  . THR A 12  ? 0.34019 0.35524 0.29665 0.11117  -0.02564 -0.14840 19  THR A CA  
28   C C   . THR A 12  ? 0.34595 0.37138 0.30376 0.12020  -0.02173 -0.13014 19  THR A C   
29   O O   . THR A 12  ? 0.35364 0.38227 0.30133 0.13040  -0.01587 -0.12839 19  THR A O   
30   C CB  . THR A 12  ? 0.36838 0.35567 0.32715 0.11167  -0.01720 -0.15157 19  THR A CB  
31   O OG1 . THR A 12  ? 0.43819 0.40947 0.39178 0.10090  -0.01763 -0.17068 19  THR A OG1 
32   C CG2 . THR A 12  ? 0.38169 0.36031 0.35634 0.11030  -0.01441 -0.13664 19  THR A CG2 
33   N N   . PHE A 13  ? 0.33132 0.36196 0.30027 0.11510  -0.02403 -0.11799 20  PHE A N   
34   C CA  . PHE A 13  ? 0.35042 0.38938 0.32014 0.11848  -0.01965 -0.10249 20  PHE A CA  
35   C C   . PHE A 13  ? 0.32107 0.35642 0.30764 0.11273  -0.01737 -0.09235 20  PHE A C   
36   O O   . PHE A 13  ? 0.32035 0.34794 0.31679 0.10589  -0.02121 -0.09390 20  PHE A O   
37   C CB  . PHE A 13  ? 0.31689 0.36440 0.28011 0.11753  -0.02372 -0.09760 20  PHE A CB  
38   C CG  . PHE A 13  ? 0.35877 0.41661 0.30361 0.12607  -0.02693 -0.10501 20  PHE A CG  
39   C CD1 . PHE A 13  ? 0.38240 0.44885 0.32644 0.12316  -0.03605 -0.11941 20  PHE A CD1 
40   C CD2 . PHE A 13  ? 0.36762 0.42936 0.29490 0.13675  -0.02040 -0.09802 20  PHE A CD2 
41   C CE1 . PHE A 13  ? 0.38555 0.46889 0.31197 0.13202  -0.04045 -0.12759 20  PHE A CE1 
42   C CE2 . PHE A 13  ? 0.40515 0.47888 0.31215 0.14758  -0.02370 -0.10361 20  PHE A CE2 
43   C CZ  . PHE A 13  ? 0.42235 0.50946 0.32894 0.14600  -0.03471 -0.11896 20  PHE A CZ  
44   N N   . ALA A 14  ? 0.30932 0.35294 0.29919 0.11484  -0.01064 -0.08215 21  ALA A N   
45   C CA  . ALA A 14  ? 0.25938 0.30778 0.26440 0.10838  -0.00966 -0.07289 21  ALA A CA  
46   C C   . ALA A 14  ? 0.27684 0.32575 0.28090 0.09916  -0.01124 -0.06667 21  ALA A C   
47   O O   . ALA A 14  ? 0.31808 0.36708 0.30947 0.10032  -0.00749 -0.06402 21  ALA A O   
48   C CB  . ALA A 14  ? 0.28607 0.35019 0.29674 0.11245  -0.00170 -0.06667 21  ALA A CB  
49   N N   . PHE A 15  ? 0.28437 0.33071 0.29882 0.09137  -0.01538 -0.06384 22  PHE A N   
50   C CA  . PHE A 15  ? 0.27402 0.31974 0.28716 0.08243  -0.01433 -0.05738 22  PHE A CA  
51   C C   . PHE A 15  ? 0.28607 0.34225 0.30016 0.07748  -0.00591 -0.05129 22  PHE A C   
52   O O   . PHE A 15  ? 0.31001 0.38170 0.33472 0.07870  -0.00364 -0.05029 22  PHE A O   
53   C CB  . PHE A 15  ? 0.26907 0.31258 0.29315 0.07505  -0.01930 -0.05553 22  PHE A CB  
54   C CG  . PHE A 15  ? 0.24107 0.27497 0.26478 0.07548  -0.02572 -0.06099 22  PHE A CG  
55   C CD1 . PHE A 15  ? 0.27584 0.30633 0.29075 0.07535  -0.02756 -0.06189 22  PHE A CD1 
56   C CD2 . PHE A 15  ? 0.28583 0.31473 0.31779 0.07604  -0.02848 -0.06452 22  PHE A CD2 
57   C CE1 . PHE A 15  ? 0.29284 0.32246 0.31067 0.07441  -0.03361 -0.06801 22  PHE A CE1 
58   C CE2 . PHE A 15  ? 0.27413 0.29538 0.30740 0.07261  -0.03271 -0.07065 22  PHE A CE2 
59   C CZ  . PHE A 15  ? 0.27186 0.29722 0.30009 0.07077  -0.03598 -0.07304 22  PHE A CZ  
60   N N   . GLN A 16  ? 0.31802 0.36598 0.32060 0.07168  -0.00015 -0.04725 23  GLN A N   
61   C CA  . GLN A 16  ? 0.35144 0.40781 0.35696 0.06007  0.00887  -0.04300 23  GLN A CA  
62   C C   . GLN A 16  ? 0.30425 0.37580 0.32728 0.05043  0.00438  -0.04296 23  GLN A C   
63   O O   . GLN A 16  ? 0.30852 0.37424 0.33559 0.05014  -0.00339 -0.04372 23  GLN A O   
64   C CB  . GLN A 16  ? 0.37527 0.41127 0.36278 0.05316  0.01782  -0.03889 23  GLN A CB  
65   C CG  . GLN A 16  ? 0.45468 0.47698 0.42134 0.06453  0.02390  -0.03645 23  GLN A CG  
66   C CD  . GLN A 16  ? 0.57999 0.57540 0.52516 0.06171  0.03327  -0.03064 23  GLN A CD  
67   O OE1 . GLN A 16  ? 0.59392 0.57729 0.53144 0.06836  0.02815  -0.02997 23  GLN A OE1 
68   N NE2 . GLN A 16  ? 0.60525 0.59037 0.53983 0.05159  0.04885  -0.02638 23  GLN A NE2 
69   N N   . ALA A 17  ? 0.26043 0.35546 0.29387 0.04295  0.00958  -0.04212 24  ALA A N   
70   C CA  . ALA A 17  ? 0.26607 0.38479 0.31627 0.03679  0.00427  -0.04221 24  ALA A CA  
71   C C   . ALA A 17  ? 0.29740 0.40424 0.34419 0.02482  0.00110  -0.04261 24  ALA A C   
72   O O   . ALA A 17  ? 0.30229 0.41673 0.35739 0.02673  -0.00713 -0.04220 24  ALA A O   
73   C CB  . ALA A 17  ? 0.28474 0.43655 0.34596 0.02733  0.01151  -0.04251 24  ALA A CB  
74   N N   . GLU A 18  ? 0.31697 0.40319 0.34926 0.01338  0.00914  -0.04289 25  GLU A N   
75   C CA  . GLU A 18  ? 0.28137 0.35445 0.30784 0.00145  0.00851  -0.04414 25  GLU A CA  
76   C C   . GLU A 18  ? 0.27091 0.32667 0.29420 0.01241  -0.00048 -0.04292 25  GLU A C   
77   O O   . GLU A 18  ? 0.29339 0.34992 0.31938 0.00688  -0.00523 -0.04369 25  GLU A O   
78   C CB  . GLU A 18  ? 0.36769 0.41373 0.37428 -0.01028 0.02231  -0.04410 25  GLU A CB  
79   C CG  . GLU A 18  ? 0.41822 0.47902 0.42725 -0.02670 0.03405  -0.04650 25  GLU A CG  
80   C CD  . GLU A 18  ? 0.56830 0.63265 0.57508 -0.01771 0.04114  -0.04326 25  GLU A CD  
81   O OE1 . GLU A 18  ? 0.44463 0.50254 0.44823 0.00219  0.03560  -0.04016 25  GLU A OE1 
82   O OE2 . GLU A 18  ? 0.60084 0.67440 0.60774 -0.03229 0.05365  -0.04472 25  GLU A OE2 
83   N N   . ILE A 19  ? 0.32343 0.36583 0.34037 0.02659  -0.00218 -0.04186 26  ILE A N   
84   C CA  . ILE A 19  ? 0.30308 0.33420 0.31915 0.03528  -0.01000 -0.04230 26  ILE A CA  
85   C C   . ILE A 19  ? 0.30449 0.34958 0.33620 0.03970  -0.01843 -0.04316 26  ILE A C   
86   O O   . ILE A 19  ? 0.31992 0.36093 0.35473 0.03867  -0.02330 -0.04281 26  ILE A O   
87   C CB  . ILE A 19  ? 0.31452 0.33463 0.31971 0.04780  -0.00968 -0.04296 26  ILE A CB  
88   C CG1 . ILE A 19  ? 0.45730 0.45733 0.44271 0.04789  -0.00163 -0.03963 26  ILE A CG1 
89   C CG2 . ILE A 19  ? 0.38596 0.40506 0.39649 0.05461  -0.01878 -0.04618 26  ILE A CG2 
90   C CD1 . ILE A 19  ? 0.52261 0.51561 0.49755 0.04067  0.01049  -0.03687 26  ILE A CD1 
91   N N   . ALA A 20  ? 0.26368 0.32366 0.30355 0.04561  -0.01848 -0.04342 27  ALA A N   
92   C CA  . ALA A 20  ? 0.25638 0.32487 0.30712 0.05271  -0.02361 -0.04257 27  ALA A CA  
93   C C   . ALA A 20  ? 0.25825 0.34004 0.31534 0.04574  -0.02626 -0.03930 27  ALA A C   
94   O O   . ALA A 20  ? 0.28913 0.36737 0.34925 0.05001  -0.03050 -0.03702 27  ALA A O   
95   C CB  . ALA A 20  ? 0.27892 0.36223 0.33528 0.06237  -0.02104 -0.04244 27  ALA A CB  
96   N N   . GLN A 21  ? 0.26896 0.36648 0.32684 0.03410  -0.02293 -0.03960 28  GLN A N   
97   C CA  . GLN A 21  ? 0.28423 0.39999 0.34716 0.02610  -0.02626 -0.03862 28  GLN A CA  
98   C C   . GLN A 21  ? 0.33206 0.42684 0.38655 0.02079  -0.02851 -0.03883 28  GLN A C   
99   O O   . GLN A 21  ? 0.31152 0.41298 0.36878 0.02284  -0.03348 -0.03622 28  GLN A O   
100  C CB  . GLN A 21  ? 0.28501 0.42335 0.35040 0.01061  -0.02114 -0.04212 28  GLN A CB  
101  C CG  . GLN A 21  ? 0.40734 0.57224 0.47764 -0.00066 -0.02504 -0.04408 28  GLN A CG  
102  C CD  . GLN A 21  ? 0.66647 0.85823 0.74718 0.01428  -0.03347 -0.03863 28  GLN A CD  
103  O OE1 . GLN A 21  ? 0.66718 0.86600 0.75440 0.03145  -0.03419 -0.03400 28  GLN A OE1 
104  N NE2 . GLN A 21  ? 0.69629 0.90092 0.77557 0.00910  -0.03874 -0.03884 28  GLN A NE2 
105  N N   . LEU A 22  ? 0.25088 0.32075 0.29353 0.01603  -0.02411 -0.04097 29  LEU A N   
106  C CA  . LEU A 22  ? 0.27416 0.32558 0.30903 0.01384  -0.02551 -0.04082 29  LEU A CA  
107  C C   . LEU A 22  ? 0.27954 0.32587 0.32008 0.02466  -0.03117 -0.03840 29  LEU A C   
108  O O   . LEU A 22  ? 0.28333 0.32827 0.32391 0.02344  -0.03387 -0.03650 29  LEU A O   
109  C CB  . LEU A 22  ? 0.26607 0.29274 0.28595 0.01224  -0.01875 -0.04210 29  LEU A CB  
110  C CG  . LEU A 22  ? 0.31147 0.32163 0.32457 0.01504  -0.01998 -0.04141 29  LEU A CG  
111  C CD1 . LEU A 22  ? 0.33912 0.34896 0.34686 0.00308  -0.01836 -0.04287 29  LEU A CD1 
112  C CD2 . LEU A 22  ? 0.35700 0.34736 0.35586 0.02100  -0.01395 -0.04091 29  LEU A CD2 
113  N N   . MET A 23  ? 0.25339 0.29584 0.29748 0.03417  -0.03187 -0.03915 30  MET A N   
114  C CA  . MET A 23  ? 0.25104 0.28548 0.29953 0.04077  -0.03490 -0.03886 30  MET A CA  
115  C C   . MET A 23  ? 0.30075 0.34337 0.35473 0.04437  -0.03671 -0.03377 30  MET A C   
116  O O   . MET A 23  ? 0.28200 0.31496 0.33588 0.04538  -0.03726 -0.03144 30  MET A O   
117  C CB  . MET A 23  ? 0.25280 0.28226 0.30226 0.04821  -0.03443 -0.04310 30  MET A CB  
118  C CG  . MET A 23  ? 0.27395 0.29687 0.31608 0.04804  -0.03383 -0.04735 30  MET A CG  
119  S SD  . MET A 23  ? 0.31125 0.33365 0.35174 0.05622  -0.03414 -0.05417 30  MET A SD  
120  C CE  . MET A 23  ? 0.30772 0.32203 0.35516 0.05461  -0.03677 -0.05948 30  MET A CE  
121  N N   . SER A 24  ? 0.27876 0.34035 0.33704 0.04810  -0.03678 -0.03134 31  SER A N   
122  C CA  . SER A 24  ? 0.26099 0.33447 0.32243 0.05615  -0.03846 -0.02479 31  SER A CA  
123  C C   . SER A 24  ? 0.29223 0.37358 0.35032 0.04881  -0.04120 -0.02230 31  SER A C   
124  O O   . SER A 24  ? 0.33503 0.41331 0.39068 0.05539  -0.04197 -0.01623 31  SER A O   
125  C CB  . SER A 24  ? 0.31980 0.42001 0.38780 0.06345  -0.03805 -0.02318 31  SER A CB  
126  O OG  . SER A 24  ? 0.45717 0.58146 0.52775 0.06973  -0.04085 -0.01694 31  SER A OG  
127  N N   . LEU A 25  ? 0.26652 0.35413 0.32149 0.03518  -0.04124 -0.02704 32  LEU A N   
128  C CA  . LEU A 25  ? 0.26593 0.35764 0.31476 0.02716  -0.04313 -0.02675 32  LEU A CA  
129  C C   . LEU A 25  ? 0.31914 0.38551 0.36229 0.02840  -0.04201 -0.02497 32  LEU A C   
130  O O   . LEU A 25  ? 0.29564 0.36362 0.33463 0.02974  -0.04337 -0.02081 32  LEU A O   
131  C CB  . LEU A 25  ? 0.32648 0.42211 0.36989 0.01093  -0.04057 -0.03396 32  LEU A CB  
132  C CG  . LEU A 25  ? 0.28725 0.41669 0.33791 0.00504  -0.04127 -0.03684 32  LEU A CG  
133  C CD1 . LEU A 25  ? 0.34421 0.46847 0.38701 -0.01430 -0.03534 -0.04521 32  LEU A CD1 
134  C CD2 . LEU A 25  ? 0.30460 0.46524 0.35783 0.00721  -0.04751 -0.03433 32  LEU A CD2 
135  N N   . ILE A 26  ? 0.26935 0.31578 0.31202 0.02812  -0.03930 -0.02819 33  ILE A N   
136  C CA  . ILE A 26  ? 0.28449 0.31384 0.32486 0.02843  -0.03789 -0.02761 33  ILE A CA  
137  C C   . ILE A 26  ? 0.34667 0.37027 0.39082 0.03597  -0.03738 -0.02229 33  ILE A C   
138  O O   . ILE A 26  ? 0.34319 0.35913 0.38437 0.03517  -0.03555 -0.01887 33  ILE A O   
139  C CB  . ILE A 26  ? 0.25110 0.26938 0.29163 0.02844  -0.03608 -0.03275 33  ILE A CB  
140  C CG1 . ILE A 26  ? 0.28434 0.29976 0.31510 0.02270  -0.03336 -0.03560 33  ILE A CG1 
141  C CG2 . ILE A 26  ? 0.27055 0.27944 0.31419 0.02940  -0.03499 -0.03335 33  ILE A CG2 
142  C CD1 . ILE A 26  ? 0.28031 0.28747 0.30762 0.02712  -0.03111 -0.03875 33  ILE A CD1 
143  N N   . ILE A 27  ? 0.28063 0.30460 0.32927 0.04371  -0.03705 -0.02122 34  ILE A N   
144  C CA  . ILE A 27  ? 0.32069 0.32955 0.36911 0.05105  -0.03327 -0.01663 34  ILE A CA  
145  C C   . ILE A 27  ? 0.33511 0.35177 0.37788 0.05928  -0.03321 -0.00641 34  ILE A C   
146  O O   . ILE A 27  ? 0.40774 0.40827 0.44504 0.06287  -0.02843 -0.00028 34  ILE A O   
147  C CB  . ILE A 27  ? 0.32082 0.32254 0.37246 0.05781  -0.03122 -0.01995 34  ILE A CB  
148  C CG1 . ILE A 27  ? 0.32773 0.32131 0.38267 0.05045  -0.03121 -0.03026 34  ILE A CG1 
149  C CG2 . ILE A 27  ? 0.37962 0.36257 0.42656 0.06840  -0.02489 -0.01353 34  ILE A CG2 
150  C CD1 . ILE A 27  ? 0.33070 0.32227 0.38667 0.05649  -0.03030 -0.03549 34  ILE A CD1 
151  N N   . ASN A 28  ? 0.30908 0.35270 0.35243 0.06243  -0.03792 -0.00445 35  ASN A N   
152  C CA  . ASN A 28  ? 0.33159 0.39174 0.36983 0.07419  -0.03925 0.00526  35  ASN A CA  
153  C C   . ASN A 28  ? 0.38693 0.46416 0.41883 0.06769  -0.04335 0.00647  35  ASN A C   
154  O O   . ASN A 28  ? 0.39298 0.48119 0.41740 0.07886  -0.04408 0.01564  35  ASN A O   
155  C CB  . ASN A 28  ? 0.36690 0.45570 0.41141 0.08264  -0.04235 0.00575  35  ASN A CB  
156  C CG  . ASN A 28  ? 0.49344 0.56466 0.54002 0.09423  -0.03708 0.00679  35  ASN A CG  
157  O OD1 . ASN A 28  ? 0.46855 0.50919 0.50812 0.10221  -0.03043 0.01161  35  ASN A OD1 
158  N ND2 . ASN A 28  ? 0.57549 0.65997 0.63012 0.09236  -0.03822 0.00059  35  ASN A ND2 
159  N N   . THR A 29  ? 0.28036 0.35975 0.31234 0.05169  -0.04532 -0.00225 36  THR A N   
160  C CA  . THR A 29  ? 0.31006 0.40416 0.33331 0.04491  -0.04839 -0.00290 36  THR A CA  
161  C C   . THR A 29  ? 0.27553 0.34823 0.28958 0.04744  -0.04423 0.00308  36  THR A C   
162  O O   . THR A 29  ? 0.32136 0.36851 0.33759 0.04361  -0.03921 0.00127  36  THR A O   
163  C CB  . THR A 29  ? 0.32685 0.42240 0.34900 0.02731  -0.04879 -0.01438 36  THR A CB  
164  O OG1 . THR A 29  ? 0.33682 0.45184 0.36694 0.02316  -0.05060 -0.01958 36  THR A OG1 
165  C CG2 . THR A 29  ? 0.32714 0.43462 0.33732 0.01849  -0.05086 -0.01755 36  THR A CG2 
166  N N   . PHE A 30  ? 0.30626 0.39348 0.30985 0.05360  -0.04622 0.00982  37  PHE A N   
167  C CA  . PHE A 30  ? 0.35776 0.42619 0.35061 0.05478  -0.04109 0.01559  37  PHE A CA  
168  C C   . PHE A 30  ? 0.34095 0.40249 0.33017 0.03938  -0.04022 0.00607  37  PHE A C   
169  O O   . PHE A 30  ? 0.34984 0.42909 0.33360 0.03036  -0.04465 -0.00161 37  PHE A O   
170  C CB  . PHE A 30  ? 0.33457 0.42176 0.31389 0.06735  -0.04329 0.02588  37  PHE A CB  
171  C CG  . PHE A 30  ? 0.32800 0.39598 0.29412 0.06864  -0.03670 0.03260  37  PHE A CG  
172  C CD1 . PHE A 30  ? 0.38830 0.42374 0.35339 0.07517  -0.02629 0.04165  37  PHE A CD1 
173  C CD2 . PHE A 30  ? 0.36165 0.44149 0.31588 0.06094  -0.03919 0.02832  37  PHE A CD2 
174  C CE1 . PHE A 30  ? 0.39562 0.41307 0.34959 0.07423  -0.01808 0.04771  37  PHE A CE1 
175  C CE2 . PHE A 30  ? 0.43985 0.50185 0.38196 0.06227  -0.03182 0.03454  37  PHE A CE2 
176  C CZ  . PHE A 30  ? 0.41145 0.44404 0.35392 0.06912  -0.02123 0.04494  37  PHE A CZ  
177  N N   . TYR A 31  ? 0.28245 0.31881 0.27394 0.03624  -0.03352 0.00589  38  TYR A N   
178  C CA  . TYR A 31  ? 0.29914 0.32783 0.28815 0.02540  -0.03146 -0.00273 38  TYR A CA  
179  C C   . TYR A 31  ? 0.33880 0.34901 0.33015 0.02588  -0.02376 0.00049  38  TYR A C   
180  O O   . TYR A 31  ? 0.31093 0.31141 0.31430 0.02595  -0.02116 -0.00050 38  TYR A O   
181  C CB  . TYR A 31  ? 0.30790 0.33528 0.30520 0.01931  -0.03319 -0.01177 38  TYR A CB  
182  C CG  . TYR A 31  ? 0.31330 0.32975 0.30396 0.01200  -0.02947 -0.01912 38  TYR A CG  
183  C CD1 . TYR A 31  ? 0.35174 0.37130 0.32804 0.00451  -0.02937 -0.02464 38  TYR A CD1 
184  C CD2 . TYR A 31  ? 0.32456 0.32815 0.32172 0.01358  -0.02529 -0.02082 38  TYR A CD2 
185  C CE1 . TYR A 31  ? 0.39068 0.39366 0.35665 0.00010  -0.02340 -0.03070 38  TYR A CE1 
186  C CE2 . TYR A 31  ? 0.33094 0.32474 0.31952 0.01151  -0.02081 -0.02567 38  TYR A CE2 
187  C CZ  . TYR A 31  ? 0.40642 0.39641 0.37851 0.00557  -0.01901 -0.03000 38  TYR A CZ  
188  O OH  . TYR A 31  ? 0.41715 0.39096 0.37654 0.00547  -0.01207 -0.03432 38  TYR A OH  
189  N N   . SER A 32  ? 0.29595 0.30403 0.27588 0.02543  -0.01974 0.00357  39  SER A N   
190  C CA  . SER A 32  ? 0.30158 0.29623 0.28508 0.02564  -0.01095 0.00811  39  SER A CA  
191  C C   . SER A 32  ? 0.31467 0.30599 0.30692 0.02009  -0.00762 0.00039  39  SER A C   
192  O O   . SER A 32  ? 0.34147 0.32795 0.34333 0.01821  -0.00116 0.00173  39  SER A O   
193  C CB  . SER A 32  ? 0.35164 0.34620 0.31906 0.02862  -0.00637 0.01548  39  SER A CB  
194  O OG  . SER A 32  ? 0.35545 0.35545 0.31344 0.03776  -0.00901 0.02485  39  SER A OG  
195  N N   . ASN A 33  ? 0.30578 0.30004 0.29424 0.01779  -0.01077 -0.00744 40  ASN A N   
196  C CA  . ASN A 33  ? 0.28781 0.27986 0.28003 0.01743  -0.00668 -0.01293 40  ASN A CA  
197  C C   . ASN A 33  ? 0.32691 0.32169 0.33559 0.01805  -0.00896 -0.01682 40  ASN A C   
198  O O   . ASN A 33  ? 0.32866 0.32282 0.33602 0.01996  -0.01063 -0.02200 40  ASN A O   
199  C CB  . ASN A 33  ? 0.34471 0.33167 0.32031 0.01629  -0.00678 -0.01874 40  ASN A CB  
200  C CG  . ASN A 33  ? 0.35849 0.33974 0.33176 0.02059  -0.00096 -0.02277 40  ASN A CG  
201  O OD1 . ASN A 33  ? 0.40089 0.38779 0.38099 0.02440  0.00413  -0.02071 40  ASN A OD1 
202  N ND2 . ASN A 33  ? 0.39065 0.36078 0.35231 0.02048  -0.00027 -0.02815 40  ASN A ND2 
203  N N   . LYS A 34  ? 0.32533 0.27302 0.28716 0.02846  -0.04526 -0.01599 41  LYS A N   
204  C CA  . LYS A 34  ? 0.31856 0.29032 0.31000 0.02864  -0.03521 -0.01742 41  LYS A CA  
205  C C   . LYS A 34  ? 0.30956 0.27316 0.29900 0.02737  -0.02382 -0.02397 41  LYS A C   
206  O O   . LYS A 34  ? 0.28307 0.26283 0.29130 0.02535  -0.01974 -0.02611 41  LYS A O   
207  C CB  . LYS A 34  ? 0.28930 0.26692 0.29120 0.03891  -0.02753 -0.01545 41  LYS A CB  
208  C CG  . LYS A 34  ? 0.28625 0.28159 0.29842 0.04338  -0.03692 -0.00737 41  LYS A CG  
209  C CD  . LYS A 34  ? 0.32650 0.31847 0.34223 0.05628  -0.02869 -0.00712 41  LYS A CD  
210  C CE  . LYS A 34  ? 0.33789 0.34825 0.36341 0.06549  -0.03584 0.00205  41  LYS A CE  
211  N NZ  . LYS A 34  ? 0.33568 0.37966 0.38530 0.07024  -0.03443 0.00658  41  LYS A NZ  
212  N N   . GLU A 35  ? 0.31209 0.25241 0.27777 0.03011  -0.01898 -0.02574 42  GLU A N   
213  C CA  . GLU A 35  ? 0.29032 0.22868 0.25970 0.03126  -0.00640 -0.02840 42  GLU A CA  
214  C C   . GLU A 35  ? 0.34411 0.28700 0.31764 0.02451  -0.00999 -0.03282 42  GLU A C   
215  O O   . GLU A 35  ? 0.33108 0.27868 0.31448 0.02475  -0.00114 -0.03467 42  GLU A O   
216  C CB  . GLU A 35  ? 0.34047 0.25746 0.28295 0.04013  0.00221  -0.02538 42  GLU A CB  
217  C CG  . GLU A 35  ? 0.36734 0.25869 0.27288 0.04300  -0.00656 -0.02878 42  GLU A CG  
218  C CD  . GLU A 35  ? 0.46839 0.33558 0.33765 0.05881  0.00373  -0.02470 42  GLU A CD  
219  O OE1 . GLU A 35  ? 0.58242 0.45085 0.45011 0.06511  0.01080  -0.01744 42  GLU A OE1 
220  O OE2 . GLU A 35  ? 0.59297 0.43623 0.42960 0.06685  0.00351  -0.02811 42  GLU A OE2 
221  N N   . ILE A 36  ? 0.28405 0.22625 0.25242 0.01716  -0.02450 -0.03254 43  ILE A N   
222  C CA  . ILE A 36  ? 0.27682 0.22081 0.24843 0.00921  -0.02945 -0.03439 43  ILE A CA  
223  C C   . ILE A 36  ? 0.26882 0.24198 0.27133 0.00658  -0.02341 -0.03372 43  ILE A C   
224  O O   . ILE A 36  ? 0.27484 0.25063 0.28106 0.00167  -0.02377 -0.03480 43  ILE A O   
225  C CB  . ILE A 36  ? 0.32188 0.25716 0.28353 -0.00187 -0.05040 -0.03060 43  ILE A CB  
226  C CG1 . ILE A 36  ? 0.32898 0.29501 0.31807 -0.00747 -0.05866 -0.02125 43  ILE A CG1 
227  C CG2 . ILE A 36  ? 0.38957 0.28424 0.30778 0.00330  -0.05914 -0.03387 43  ILE A CG2 
228  C CD1 . ILE A 36  ? 0.39854 0.36192 0.38671 -0.02283 -0.08308 -0.01254 43  ILE A CD1 
229  N N   . PHE A 37  ? 0.24937 0.23916 0.26848 0.01219  -0.01745 -0.03256 44  PHE A N   
230  C CA  . PHE A 37  ? 0.22918 0.23882 0.26722 0.01425  -0.01150 -0.03362 44  PHE A CA  
231  C C   . PHE A 37  ? 0.28894 0.28994 0.32494 0.01378  -0.00468 -0.03940 44  PHE A C   
232  O O   . PHE A 37  ? 0.26295 0.27495 0.30703 0.01238  -0.00339 -0.04042 44  PHE A O   
233  C CB  . PHE A 37  ? 0.24905 0.26528 0.29451 0.02454  -0.00700 -0.03381 44  PHE A CB  
234  C CG  . PHE A 37  ? 0.25328 0.25060 0.29336 0.02785  -0.00137 -0.03848 44  PHE A CG  
235  C CD1 . PHE A 37  ? 0.28267 0.26545 0.31347 0.02877  -0.00071 -0.03571 44  PHE A CD1 
236  C CD2 . PHE A 37  ? 0.26107 0.25528 0.30562 0.02900  0.00167  -0.04332 44  PHE A CD2 
237  C CE1 . PHE A 37  ? 0.29476 0.26476 0.32636 0.02940  0.00445  -0.03479 44  PHE A CE1 
238  C CE2 . PHE A 37  ? 0.26476 0.24363 0.31004 0.02765  0.00321  -0.04369 44  PHE A CE2 
239  C CZ  . PHE A 37  ? 0.26324 0.23236 0.30499 0.02721  0.00536  -0.03793 44  PHE A CZ  
240  N N   . LEU A 38  ? 0.25954 0.24408 0.28632 0.01610  0.00034  -0.04086 45  LEU A N   
241  C CA  . LEU A 38  ? 0.23493 0.21833 0.26743 0.01623  0.00647  -0.04291 45  LEU A CA  
242  C C   . LEU A 38  ? 0.26666 0.24569 0.29069 0.01344  0.00536  -0.04388 45  LEU A C   
243  O O   . LEU A 38  ? 0.27610 0.26170 0.30819 0.01186  0.00665  -0.04565 45  LEU A O   
244  C CB  . LEU A 38  ? 0.26723 0.24239 0.29933 0.01978  0.01339  -0.03863 45  LEU A CB  
245  C CG  . LEU A 38  ? 0.28876 0.26914 0.33534 0.01841  0.01786  -0.03628 45  LEU A CG  
246  C CD1 . LEU A 38  ? 0.26379 0.24839 0.32382 0.01479  0.01165  -0.04038 45  LEU A CD1 
247  C CD2 . LEU A 38  ? 0.32637 0.30533 0.37724 0.02153  0.02583  -0.02584 45  LEU A CD2 
248  N N   . ARG A 39  ? 0.29593 0.25939 0.29974 0.01324  0.00064  -0.04302 46  ARG A N   
249  C CA  . ARG A 39  ? 0.28321 0.23386 0.27288 0.01063  -0.00412 -0.04433 46  ARG A CA  
250  C C   . ARG A 39  ? 0.29879 0.26597 0.30399 0.00156  -0.01024 -0.04306 46  ARG A C   
251  O O   . ARG A 39  ? 0.29126 0.25713 0.29643 -0.00019 -0.00983 -0.04372 46  ARG A O   
252  C CB  . ARG A 39  ? 0.34291 0.26674 0.30285 0.01043  -0.01473 -0.04430 46  ARG A CB  
253  C CG  . ARG A 39  ? 0.41851 0.31814 0.35646 0.00689  -0.02501 -0.04586 46  ARG A CG  
254  C CD  . ARG A 39  ? 0.43628 0.30150 0.33946 0.00505  -0.04196 -0.04653 46  ARG A CD  
255  N NE  . ARG A 39  ? 0.45084 0.33090 0.37092 -0.01008 -0.05809 -0.04042 46  ARG A NE  
256  C CZ  . ARG A 39  ? 0.52257 0.37962 0.42016 -0.01441 -0.07602 -0.03906 46  ARG A CZ  
257  N NH1 . ARG A 39  ? 0.50331 0.31643 0.35372 -0.00273 -0.07961 -0.04545 46  ARG A NH1 
258  N NH2 . ARG A 39  ? 0.45893 0.33700 0.38005 -0.02981 -0.09186 -0.02954 46  ARG A NH2 
259  N N   . GLU A 40  ? 0.24621 0.23109 0.26489 -0.00276 -0.01516 -0.03898 47  GLU A N   
260  C CA  . GLU A 40  ? 0.23529 0.24098 0.26957 -0.00943 -0.01885 -0.03310 47  GLU A CA  
261  C C   . GLU A 40  ? 0.24902 0.26854 0.29401 -0.00359 -0.00906 -0.03625 47  GLU A C   
262  O O   . GLU A 40  ? 0.25059 0.27751 0.29935 -0.00717 -0.00956 -0.03314 47  GLU A O   
263  C CB  . GLU A 40  ? 0.21709 0.24600 0.26701 -0.01161 -0.02388 -0.02403 47  GLU A CB  
264  C CG  . GLU A 40  ? 0.30635 0.32278 0.34734 -0.02098 -0.03961 -0.01850 47  GLU A CG  
265  C CD  . GLU A 40  ? 0.32452 0.31569 0.34874 -0.03281 -0.05328 -0.01717 47  GLU A CD  
266  O OE1 . GLU A 40  ? 0.36654 0.36848 0.40177 -0.03967 -0.05426 -0.01143 47  GLU A OE1 
267  O OE2 . GLU A 40  ? 0.38909 0.34599 0.38533 -0.03488 -0.06514 -0.02088 47  GLU A OE2 
268  N N   . LEU A 41  ? 0.23386 0.25445 0.28193 0.00481  -0.00241 -0.04148 48  LEU A N   
269  C CA  . LEU A 41  ? 0.24276 0.26896 0.29508 0.01025  0.00213  -0.04559 48  LEU A CA  
270  C C   . LEU A 41  ? 0.24691 0.26259 0.29612 0.00803  0.00307  -0.04870 48  LEU A C   
271  O O   . LEU A 41  ? 0.26159 0.28243 0.31181 0.00876  0.00323  -0.04959 48  LEU A O   
272  C CB  . LEU A 41  ? 0.23837 0.25946 0.29103 0.01782  0.00377  -0.05009 48  LEU A CB  
273  C CG  . LEU A 41  ? 0.28322 0.31593 0.33763 0.02496  0.00425  -0.04671 48  LEU A CG  
274  C CD1 . LEU A 41  ? 0.29040 0.30755 0.33954 0.03279  0.00373  -0.05200 48  LEU A CD1 
275  C CD2 . LEU A 41  ? 0.25834 0.31206 0.31533 0.03160  0.00745  -0.04196 48  LEU A CD2 
276  N N   . ILE A 42  ? 0.23379 0.23602 0.27767 0.00747  0.00447  -0.04868 49  ILE A N   
277  C CA  . ILE A 42  ? 0.23244 0.22886 0.27489 0.00859  0.00698  -0.04864 49  ILE A CA  
278  C C   . ILE A 42  ? 0.27405 0.26603 0.30741 0.00515  0.00336  -0.04744 49  ILE A C   
279  O O   . ILE A 42  ? 0.25386 0.24758 0.28913 0.00599  0.00392  -0.04751 49  ILE A O   
280  C CB  . ILE A 42  ? 0.25558 0.24184 0.29266 0.01372  0.01264  -0.04575 49  ILE A CB  
281  C CG1 . ILE A 42  ? 0.26098 0.25456 0.31387 0.01420  0.01511  -0.04340 49  ILE A CG1 
282  C CG2 . ILE A 42  ? 0.26541 0.24584 0.29666 0.01946  0.01704  -0.04313 49  ILE A CG2 
283  C CD1 . ILE A 42  ? 0.28437 0.27384 0.33507 0.02025  0.02353  -0.03574 49  ILE A CD1 
284  N N   . SER A 43  ? 0.25762 0.24165 0.28077 0.00008  -0.00275 -0.04500 50  SER A N   
285  C CA  . SER A 43  ? 0.25575 0.23193 0.27097 -0.00645 -0.00976 -0.04152 50  SER A CA  
286  C C   . SER A 43  ? 0.26421 0.26311 0.29442 -0.00958 -0.00870 -0.03753 50  SER A C   
287  O O   . SER A 43  ? 0.25822 0.25354 0.28504 -0.01155 -0.01015 -0.03526 50  SER A O   
288  C CB  . SER A 43  ? 0.35159 0.31619 0.35717 -0.01519 -0.02159 -0.03710 50  SER A CB  
289  O OG  . SER A 43  ? 0.40081 0.35604 0.40105 -0.02527 -0.03211 -0.03102 50  SER A OG  
290  N N   . ASN A 44  ? 0.23146 0.25219 0.27463 -0.00776 -0.00578 -0.03558 51  ASN A N   
291  C CA  . ASN A 44  ? 0.23219 0.27344 0.28300 -0.00510 -0.00210 -0.03116 51  ASN A CA  
292  C C   . ASN A 44  ? 0.24406 0.27947 0.28986 0.00145  0.00110  -0.03841 51  ASN A C   
293  O O   . ASN A 44  ? 0.25576 0.29703 0.29945 0.00198  0.00172  -0.03481 51  ASN A O   
294  C CB  . ASN A 44  ? 0.23715 0.29834 0.29575 0.00273  0.00258  -0.02908 51  ASN A CB  
295  C CG  . ASN A 44  ? 0.33616 0.41516 0.40681 -0.00364 -0.00080 -0.01630 51  ASN A CG  
296  O OD1 . ASN A 44  ? 0.32400 0.39689 0.39636 -0.01709 -0.01010 -0.00906 51  ASN A OD1 
297  N ND2 . ASN A 44  ? 0.33061 0.42973 0.40867 0.00633  0.00474  -0.01247 51  ASN A ND2 
298  N N   . SER A 45  ? 0.21303 0.23860 0.25858 0.00566  0.00190  -0.04625 52  SER A N   
299  C CA  . SER A 45  ? 0.24924 0.27086 0.29453 0.00917  0.00084  -0.05054 52  SER A CA  
300  C C   . SER A 45  ? 0.27142 0.28654 0.31373 0.00682  0.00013  -0.04766 52  SER A C   
301  O O   . SER A 45  ? 0.24761 0.26484 0.28788 0.00869  -0.00170 -0.04737 52  SER A O   
302  C CB  . SER A 45  ? 0.23962 0.25492 0.29204 0.01038  -0.00028 -0.05421 52  SER A CB  
303  O OG  . SER A 45  ? 0.26726 0.28169 0.31800 0.01394  -0.00214 -0.05806 52  SER A OG  
304  N N   . SER A 46  ? 0.25304 0.25608 0.29035 0.00503  0.00086  -0.04583 53  SER A N   
305  C CA  . SER A 46  ? 0.26422 0.25445 0.29225 0.00652  0.00002  -0.04353 53  SER A CA  
306  C C   . SER A 46  ? 0.28906 0.27992 0.31177 0.00081  -0.00430 -0.03875 53  SER A C   
307  O O   . SER A 46  ? 0.29197 0.27958 0.31118 0.00331  -0.00512 -0.03715 53  SER A O   
308  C CB  . SER A 46  ? 0.27068 0.23932 0.28333 0.00937  0.00054  -0.04352 53  SER A CB  
309  O OG  . SER A 46  ? 0.30260 0.25126 0.29857 0.01366  -0.00132 -0.04192 53  SER A OG  
310  N N   . ASP A 47  ? 0.25109 0.24923 0.27581 -0.00692 -0.00711 -0.03357 54  ASP A N   
311  C CA  . ASP A 47  ? 0.26275 0.26861 0.28833 -0.01348 -0.01001 -0.02375 54  ASP A CA  
312  C C   . ASP A 47  ? 0.27098 0.29372 0.29927 -0.00632 -0.00473 -0.02358 54  ASP A C   
313  O O   . ASP A 47  ? 0.27531 0.29665 0.29869 -0.00756 -0.00598 -0.01756 54  ASP A O   
314  C CB  . ASP A 47  ? 0.23896 0.26126 0.27531 -0.02205 -0.01250 -0.01386 54  ASP A CB  
315  C CG  . ASP A 47  ? 0.35305 0.35253 0.38186 -0.03362 -0.02469 -0.01052 54  ASP A CG  
316  O OD1 . ASP A 47  ? 0.39676 0.36301 0.40534 -0.03176 -0.02959 -0.01728 54  ASP A OD1 
317  O OD2 . ASP A 47  ? 0.34949 0.36213 0.38992 -0.04241 -0.03020 -0.00154 54  ASP A OD2 
318  N N   . ALA A 48  ? 0.23471 0.26801 0.26614 0.00197  -0.00058 -0.03050 55  ALA A N   
319  C CA  . ALA A 48  ? 0.24464 0.28572 0.26933 0.01111  0.00137  -0.03240 55  ALA A CA  
320  C C   . ALA A 48  ? 0.25026 0.27927 0.27068 0.01318  -0.00339 -0.03728 55  ALA A C   
321  O O   . ALA A 48  ? 0.24981 0.28039 0.26110 0.01755  -0.00460 -0.03530 55  ALA A O   
322  C CB  . ALA A 48  ? 0.25734 0.30111 0.27935 0.02004  0.00269  -0.04031 55  ALA A CB  
323  N N   . LEU A 49  ? 0.25486 0.27454 0.28261 0.01177  -0.00558 -0.04195 56  LEU A N   
324  C CA  . LEU A 49  ? 0.25563 0.27002 0.28559 0.01440  -0.00924 -0.04217 56  LEU A CA  
325  C C   . LEU A 49  ? 0.26697 0.27310 0.28842 0.01358  -0.00912 -0.03579 56  LEU A C   
326  O O   . LEU A 49  ? 0.28534 0.29111 0.30364 0.01737  -0.01244 -0.03390 56  LEU A O   
327  C CB  . LEU A 49  ? 0.23674 0.24920 0.27935 0.01523  -0.00792 -0.04328 56  LEU A CB  
328  C CG  . LEU A 49  ? 0.23436 0.25225 0.28694 0.01425  -0.01172 -0.04765 56  LEU A CG  
329  C CD1 . LEU A 49  ? 0.27001 0.28869 0.33498 0.01363  -0.00707 -0.04541 56  LEU A CD1 
330  C CD2 . LEU A 49  ? 0.23890 0.25945 0.29740 0.01489  -0.02263 -0.04792 56  LEU A CD2 
331  N N   . ASP A 50  ? 0.27406 0.26950 0.28963 0.00821  -0.00799 -0.03194 57  ASP A N   
332  C CA  . ASP A 50  ? 0.27342 0.25318 0.27697 0.00603  -0.01129 -0.02532 57  ASP A CA  
333  C C   . ASP A 50  ? 0.29112 0.28241 0.29226 0.00398  -0.01188 -0.01812 57  ASP A C   
334  O O   . ASP A 50  ? 0.30259 0.28492 0.29546 0.00595  -0.01458 -0.01354 57  ASP A O   
335  C CB  . ASP A 50  ? 0.29246 0.25341 0.28685 -0.00290 -0.01568 -0.02133 57  ASP A CB  
336  C CG  . ASP A 50  ? 0.40535 0.34498 0.38992 0.00263  -0.01552 -0.02771 57  ASP A CG  
337  O OD1 . ASP A 50  ? 0.38784 0.32838 0.37445 0.01463  -0.00967 -0.03206 57  ASP A OD1 
338  O OD2 . ASP A 50  ? 0.42755 0.34900 0.40121 -0.00506 -0.02221 -0.02616 57  ASP A OD2 
339  N N   . LYS A 51  ? 0.26409 0.27511 0.27019 0.00238  -0.00818 -0.01548 58  LYS A N   
340  C CA  . LYS A 51  ? 0.27862 0.30312 0.27950 0.00384  -0.00546 -0.00550 58  LYS A CA  
341  C C   . LYS A 51  ? 0.28171 0.30519 0.27196 0.01470  -0.00704 -0.01100 58  LYS A C   
342  O O   . LYS A 51  ? 0.31937 0.34139 0.30017 0.01614  -0.00774 -0.00296 58  LYS A O   
343  C CB  . LYS A 51  ? 0.29749 0.34585 0.30382 0.00595  0.00178  -0.00024 58  LYS A CB  
344  C CG  . LYS A 51  ? 0.31058 0.36630 0.33136 -0.00729 0.00087  0.01143  58  LYS A CG  
345  C CD  . LYS A 51  ? 0.30918 0.39547 0.33875 -0.00075 0.01021  0.01850  58  LYS A CD  
346  C CE  . LYS A 51  ? 0.41828 0.51523 0.46735 -0.01423 0.00666  0.02948  58  LYS A CE  
347  N NZ  . LYS A 51  ? 0.42634 0.55954 0.48660 -0.00415 0.01799  0.04013  58  LYS A NZ  
348  N N   . ILE A 52  ? 0.28245 0.30511 0.27378 0.02114  -0.00995 -0.02311 59  ILE A N   
349  C CA  . ILE A 52  ? 0.26506 0.28411 0.24565 0.02928  -0.01675 -0.02735 59  ILE A CA  
350  C C   . ILE A 52  ? 0.33084 0.34117 0.31735 0.02812  -0.02202 -0.02525 59  ILE A C   
351  O O   . ILE A 52  ? 0.33890 0.34664 0.31549 0.03293  -0.02705 -0.02223 59  ILE A O   
352  C CB  . ILE A 52  ? 0.28731 0.30383 0.26633 0.03405  -0.02353 -0.03893 59  ILE A CB  
353  C CG1 . ILE A 52  ? 0.33167 0.33970 0.29319 0.04161  -0.03567 -0.04287 59  ILE A CG1 
354  C CG2 . ILE A 52  ? 0.30342 0.31845 0.30464 0.02789  -0.02685 -0.04318 59  ILE A CG2 
355  C CD1 . ILE A 52  ? 0.40035 0.40841 0.33268 0.05249  -0.03099 -0.03889 59  ILE A CD1 
356  N N   . ARG A 53  ? 0.28270 0.28737 0.28161 0.02451  -0.02018 -0.02557 60  ARG A N   
357  C CA  . ARG A 53  ? 0.32352 0.31915 0.32371 0.02867  -0.02259 -0.02169 60  ARG A CA  
358  C C   . ARG A 53  ? 0.32174 0.30590 0.30612 0.02765  -0.02284 -0.01308 60  ARG A C   
359  O O   . ARG A 53  ? 0.36459 0.34548 0.34365 0.03372  -0.02716 -0.00936 60  ARG A O   
360  C CB  . ARG A 53  ? 0.34095 0.32832 0.34849 0.03044  -0.01828 -0.02258 60  ARG A CB  
361  C CG  . ARG A 53  ? 0.51871 0.50473 0.53076 0.04159  -0.01973 -0.01792 60  ARG A CG  
362  C CD  . ARG A 53  ? 0.73160 0.70446 0.74031 0.04956  -0.01307 -0.01670 60  ARG A CD  
363  N NE  . ARG A 53  ? 0.73089 0.72450 0.76325 0.05591  -0.00909 -0.01469 60  ARG A NE  
364  C CZ  . ARG A 53  ? 0.71854 0.71049 0.75298 0.05778  -0.00159 -0.01625 60  ARG A CZ  
365  N NH1 . ARG A 53  ? 0.48500 0.45495 0.49907 0.05270  -0.00001 -0.02193 60  ARG A NH1 
366  N NH2 . ARG A 53  ? 0.48454 0.49867 0.54322 0.06422  0.00344  -0.00975 60  ARG A NH2 
367  N N   . TYR A 54  ? 0.32535 0.30469 0.30397 0.01890  -0.01980 -0.00748 61  TYR A N   
368  C CA  . TYR A 54  ? 0.34025 0.30742 0.30669 0.01451  -0.02194 0.00438  61  TYR A CA  
369  C C   . TYR A 54  ? 0.39480 0.37533 0.35349 0.01959  -0.02138 0.00977  61  TYR A C   
370  O O   . TYR A 54  ? 0.39741 0.36734 0.34568 0.02274  -0.02498 0.01640  61  TYR A O   
371  C CB  . TYR A 54  ? 0.35745 0.32238 0.32566 0.00052  -0.02172 0.01368  61  TYR A CB  
372  C CG  . TYR A 54  ? 0.40136 0.35037 0.35944 -0.00760 -0.02711 0.02934  61  TYR A CG  
373  C CD1 . TYR A 54  ? 0.40361 0.31578 0.34658 -0.00738 -0.03555 0.02944  61  TYR A CD1 
374  C CD2 . TYR A 54  ? 0.36359 0.33326 0.32466 -0.01271 -0.02317 0.04525  61  TYR A CD2 
375  C CE1 . TYR A 54  ? 0.44154 0.33290 0.37279 -0.01592 -0.04321 0.04478  61  TYR A CE1 
376  C CE2 . TYR A 54  ? 0.42029 0.37706 0.37461 -0.02155 -0.02843 0.06291  61  TYR A CE2 
377  C CZ  . TYR A 54  ? 0.51068 0.42651 0.45055 -0.02494 -0.03991 0.06240  61  TYR A CZ  
378  O OH  . TYR A 54  ? 0.53537 0.43262 0.46684 -0.03540 -0.04775 0.08104  61  TYR A OH  
379  N N   . GLU A 55  ? 0.35985 0.35992 0.31868 0.02330  -0.01734 0.00630  62  GLU A N   
380  C CA  . GLU A 55  ? 0.35591 0.36397 0.29792 0.03211  -0.01659 0.01089  62  GLU A CA  
381  C C   . GLU A 55  ? 0.39136 0.39058 0.32667 0.04049  -0.02660 0.00413  62  GLU A C   
382  O O   . GLU A 55  ? 0.44700 0.44295 0.36635 0.04614  -0.02920 0.01104  62  GLU A O   
383  C CB  . GLU A 55  ? 0.40773 0.43101 0.34305 0.03941  -0.01080 0.00639  62  GLU A CB  
384  C CG  . GLU A 55  ? 0.46829 0.50968 0.40673 0.03609  0.00096  0.02192  62  GLU A CG  
385  C CD  . GLU A 55  ? 0.60850 0.66551 0.53381 0.05053  0.00976  0.01997  62  GLU A CD  
386  O OE1 . GLU A 55  ? 0.64797 0.72799 0.58142 0.05022  0.02165  0.03508  62  GLU A OE1 
387  O OE2 . GLU A 55  ? 0.62848 0.67379 0.53480 0.06287  0.00371  0.00462  62  GLU A OE2 
388  N N   . SER A 56  ? 0.36440 0.36174 0.31434 0.04086  -0.03265 -0.00625 63  SER A N   
389  C CA  . SER A 56  ? 0.37977 0.37541 0.33148 0.04724  -0.04413 -0.00893 63  SER A CA  
390  C C   . SER A 56  ? 0.44192 0.42826 0.39416 0.05001  -0.04519 -0.00028 63  SER A C   
391  O O   . SER A 56  ? 0.44011 0.42782 0.39274 0.05676  -0.05462 0.00148  63  SER A O   
392  C CB  . SER A 56  ? 0.34772 0.35026 0.32207 0.04557  -0.04991 -0.01686 63  SER A CB  
393  O OG  . SER A 56  ? 0.39277 0.39464 0.38531 0.04452  -0.04356 -0.01400 63  SER A OG  
394  N N   . LEU A 57  ? 0.39118 0.36496 0.34100 0.04538  -0.03814 0.00583  64  LEU A N   
395  C CA  . LEU A 57  ? 0.46129 0.41776 0.40574 0.05081  -0.04051 0.01277  64  LEU A CA  
396  C C   . LEU A 57  ? 0.51926 0.47125 0.44601 0.05417  -0.04460 0.02203  64  LEU A C   
397  O O   . LEU A 57  ? 0.55879 0.50218 0.48191 0.06302  -0.04982 0.02642  64  LEU A O   
398  C CB  . LEU A 57  ? 0.44732 0.38063 0.38557 0.04448  -0.03654 0.01599  64  LEU A CB  
399  C CG  . LEU A 57  ? 0.43331 0.36564 0.38329 0.04556  -0.03267 0.00731  64  LEU A CG  
400  C CD1 . LEU A 57  ? 0.43988 0.33832 0.37301 0.04111  -0.03359 0.01030  64  LEU A CD1 
401  C CD2 . LEU A 57  ? 0.44057 0.38225 0.40428 0.05963  -0.03229 0.00451  64  LEU A CD2 
402  N N   . THR A 58  ? 0.54698 0.50622 0.46200 0.04962  -0.04120 0.02678  65  THR A N   
403  C CA  . THR A 58  ? 0.57691 0.53368 0.47204 0.05436  -0.04325 0.03740  65  THR A CA  
404  C C   . THR A 58  ? 0.61192 0.58176 0.49360 0.06348  -0.04747 0.03177  65  THR A C   
405  O O   . THR A 58  ? 0.66105 0.62755 0.52183 0.07074  -0.05062 0.03926  65  THR A O   
406  C CB  . THR A 58  ? 0.68235 0.63669 0.57024 0.04434  -0.03522 0.05328  65  THR A CB  
407  O OG1 . THR A 58  ? 0.66522 0.63977 0.55932 0.04012  -0.02652 0.05183  65  THR A OG1 
408  C CG2 . THR A 58  ? 0.60829 0.53764 0.50136 0.03410  -0.03770 0.05909  65  THR A CG2 
409  N N   . ASP A 59  ? 0.64164 0.62217 0.47271 0.15402  -0.01503 0.06498  66  ASP A N   
410  C CA  . ASP A 59  ? 0.55256 0.55735 0.37777 0.15593  -0.03026 0.05859  66  ASP A CA  
411  C C   . ASP A 59  ? 0.53523 0.56569 0.38850 0.15091  -0.04400 0.04656  66  ASP A C   
412  O O   . ASP A 59  ? 0.52657 0.56054 0.39139 0.13727  -0.04443 0.03381  66  ASP A O   
413  C CB  . ASP A 59  ? 0.58709 0.58603 0.39654 0.14589  -0.02512 0.05224  66  ASP A CB  
414  C CG  . ASP A 59  ? 0.66726 0.68379 0.46134 0.15005  -0.03915 0.04593  66  ASP A CG  
415  O OD1 . ASP A 59  ? 0.68924 0.72454 0.48806 0.15791  -0.05547 0.04517  66  ASP A OD1 
416  O OD2 . ASP A 59  ? 0.68710 0.69900 0.46464 0.14543  -0.03407 0.04157  66  ASP A OD2 
417  N N   . PRO A 60  ? 0.55433 0.60396 0.42089 0.16178  -0.05508 0.05141  67  PRO A N   
418  C CA  . PRO A 60  ? 0.46990 0.54461 0.36762 0.15532  -0.06642 0.04158  67  PRO A CA  
419  C C   . PRO A 60  ? 0.49726 0.58678 0.39279 0.14501  -0.08055 0.02729  67  PRO A C   
420  O O   . PRO A 60  ? 0.47675 0.57860 0.39582 0.13423  -0.08591 0.01677  67  PRO A O   
421  C CB  . PRO A 60  ? 0.55056 0.64694 0.46142 0.17089  -0.07655 0.05248  67  PRO A CB  
422  C CG  . PRO A 60  ? 0.65457 0.73003 0.54503 0.18566  -0.06544 0.06815  67  PRO A CG  
423  C CD  . PRO A 60  ? 0.57047 0.61680 0.42987 0.17993  -0.05359 0.06792  67  PRO A CD  
424  N N   . SER A 61  ? 0.51128 0.59799 0.37709 0.14868  -0.08637 0.02680  68  SER A N   
425  C CA  . SER A 61  ? 0.53443 0.63052 0.39381 0.13989  -0.09938 0.01198  68  SER A CA  
426  C C   . SER A 61  ? 0.51242 0.59614 0.37721 0.12545  -0.08934 0.00010  68  SER A C   
427  O O   . SER A 61  ? 0.48074 0.57010 0.34605 0.11709  -0.09870 -0.01343 68  SER A O   
428  C CB  . SER A 61  ? 0.52524 0.61608 0.34564 0.14841  -0.10480 0.01405  68  SER A CB  
429  O OG  . SER A 61  ? 0.58047 0.64745 0.37843 0.14880  -0.08597 0.01849  68  SER A OG  
430  N N   . LYS A 62  ? 0.45380 0.52019 0.32323 0.12197  -0.07135 0.00466  69  LYS A N   
431  C CA  . LYS A 62  ? 0.42103 0.47967 0.29860 0.10891  -0.06404 -0.00567 69  LYS A CA  
432  C C   . LYS A 62  ? 0.41753 0.48858 0.32380 0.09981  -0.07159 -0.01518 69  LYS A C   
433  O O   . LYS A 62  ? 0.43382 0.50063 0.34545 0.08982  -0.06927 -0.02500 69  LYS A O   
434  C CB  . LYS A 62  ? 0.48088 0.52033 0.35893 0.10578  -0.04605 0.00143  69  LYS A CB  
435  C CG  . LYS A 62  ? 0.57473 0.60059 0.42613 0.11229  -0.03660 0.01151  69  LYS A CG  
436  C CD  . LYS A 62  ? 0.52633 0.54109 0.37321 0.10322  -0.02393 0.00945  69  LYS A CD  
437  C CE  . LYS A 62  ? 0.55373 0.55860 0.37476 0.10921  -0.01447 0.01947  69  LYS A CE  
438  N NZ  . LYS A 62  ? 0.56521 0.56879 0.38697 0.10044  -0.00509 0.01483  69  LYS A NZ  
439  N N   . LEU A 63  ? 0.40812 0.49500 0.33427 0.10364  -0.07949 -0.01114 70  LEU A N   
440  C CA  . LEU A 63  ? 0.41210 0.51288 0.36727 0.09483  -0.08590 -0.01841 70  LEU A CA  
441  C C   . LEU A 63  ? 0.39485 0.51544 0.35417 0.09196  -0.10585 -0.02626 70  LEU A C   
442  O O   . LEU A 63  ? 0.41676 0.55211 0.40293 0.08415  -0.11288 -0.03080 70  LEU A O   
443  C CB  . LEU A 63  ? 0.37172 0.47857 0.35016 0.09988  -0.07958 -0.00871 70  LEU A CB  
444  C CG  . LEU A 63  ? 0.37159 0.45375 0.34424 0.09982  -0.06058 -0.00371 70  LEU A CG  
445  C CD1 . LEU A 63  ? 0.38408 0.47059 0.37713 0.10639  -0.05422 0.00450  70  LEU A CD1 
446  C CD2 . LEU A 63  ? 0.35482 0.42561 0.32987 0.08596  -0.05502 -0.01408 70  LEU A CD2 
447  N N   . ASP A 64  ? 0.39857 0.51797 0.33032 0.09693  -0.11489 -0.02845 71  ASP A N   
448  C CA  . ASP A 64  ? 0.46384 0.59824 0.39427 0.09254  -0.13600 -0.03811 71  ASP A CA  
449  C C   . ASP A 64  ? 0.49806 0.62549 0.43519 0.07787  -0.13828 -0.05351 71  ASP A C   
450  O O   . ASP A 64  ? 0.48932 0.62966 0.43922 0.06935  -0.15459 -0.06176 71  ASP A O   
451  C CB  . ASP A 64  ? 0.47436 0.60340 0.36606 0.10137  -0.14416 -0.03852 71  ASP A CB  
452  C CG  . ASP A 64  ? 0.59328 0.73312 0.47854 0.11650  -0.14782 -0.02302 71  ASP A CG  
453  O OD1 . ASP A 64  ? 0.61437 0.77028 0.52893 0.11997  -0.14771 -0.01346 71  ASP A OD1 
454  O OD2 . ASP A 64  ? 0.65275 0.78491 0.50259 0.12601  -0.15076 -0.02001 71  ASP A OD2 
455  N N   . SER A 65  ? 0.42126 0.52848 0.35098 0.07459  -0.12244 -0.05678 72  SER A N   
456  C CA  . SER A 65  ? 0.41873 0.51583 0.35470 0.06300  -0.12075 -0.06905 72  SER A CA  
457  C C   . SER A 65  ? 0.48263 0.58721 0.45432 0.05408  -0.11737 -0.06781 72  SER A C   
458  O O   . SER A 65  ? 0.44185 0.53654 0.42023 0.04495  -0.11407 -0.07583 72  SER A O   
459  C CB  . SER A 65  ? 0.42611 0.50278 0.34272 0.06524  -0.10465 -0.07000 72  SER A CB  
460  O OG  . SER A 65  ? 0.41132 0.48502 0.33089 0.07072  -0.09022 -0.05719 72  SER A OG  
461  N N   . GLY A 66  ? 0.41893 0.53933 0.41231 0.05801  -0.11635 -0.05692 73  GLY A N   
462  C CA  . GLY A 66  ? 0.38808 0.51625 0.41355 0.05121  -0.11157 -0.05462 73  GLY A CA  
463  C C   . GLY A 66  ? 0.37672 0.50628 0.41174 0.06022  -0.09829 -0.04126 73  GLY A C   
464  O O   . GLY A 66  ? 0.34792 0.45879 0.36686 0.06441  -0.08497 -0.03760 73  GLY A O   
465  N N   . LYS A 67  ? 0.34929 0.50034 0.41013 0.06350  -0.10149 -0.03362 74  LYS A N   
466  C CA  . LYS A 67  ? 0.32511 0.47443 0.39184 0.07457  -0.08797 -0.02103 74  LYS A CA  
467  C C   . LYS A 67  ? 0.33249 0.47062 0.41175 0.07003  -0.07256 -0.02022 74  LYS A C   
468  O O   . LYS A 67  ? 0.36588 0.49171 0.43998 0.07849  -0.05902 -0.01227 74  LYS A O   
469  C CB  . LYS A 67  ? 0.30620 0.48511 0.39604 0.08360  -0.09618 -0.01114 74  LYS A CB  
470  C CG  . LYS A 67  ? 0.56444 0.74781 0.63414 0.09605  -0.10522 -0.00520 74  LYS A CG  
471  C CD  . LYS A 67  ? 0.73624 0.95583 0.83048 0.10139  -0.12150 0.00133  74  LYS A CD  
472  C CE  . LYS A 67  ? 0.78610 1.01263 0.85760 0.10449  -0.14061 -0.00128 74  LYS A CE  
473  N NZ  . LYS A 67  ? 0.89636 1.14324 0.98147 0.09011  -0.16201 -0.01246 74  LYS A NZ  
474  N N   . GLU A 68  ? 0.31481 0.45454 0.40800 0.05742  -0.07411 -0.02788 75  GLU A N   
475  C CA  . GLU A 68  ? 0.28013 0.41103 0.38481 0.05402  -0.05999 -0.02586 75  GLU A CA  
476  C C   . GLU A 68  ? 0.28553 0.38724 0.36592 0.05066  -0.05044 -0.03046 75  GLU A C   
477  O O   . GLU A 68  ? 0.32980 0.42353 0.39697 0.04437  -0.05623 -0.03879 75  GLU A O   
478  C CB  . GLU A 68  ? 0.37110 0.51474 0.50080 0.04161  -0.06476 -0.03056 75  GLU A CB  
479  C CG  . GLU A 68  ? 0.41858 0.59523 0.58210 0.04251  -0.07161 -0.02394 75  GLU A CG  
480  C CD  . GLU A 68  ? 0.81658 1.01363 0.98186 0.04307  -0.09148 -0.02601 75  GLU A CD  
481  O OE1 . GLU A 68  ? 0.96831 1.18952 1.14920 0.05302  -0.09571 -0.01634 75  GLU A OE1 
482  O OE2 . GLU A 68  ? 0.84205 1.02995 0.99112 0.03459  -0.10286 -0.03721 75  GLU A OE2 
483  N N   . LEU A 69  ? 0.27324 0.35962 0.34808 0.05502  -0.03626 -0.02507 76  LEU A N   
484  C CA  . LEU A 69  ? 0.26332 0.32336 0.31664 0.05121  -0.02800 -0.02819 76  LEU A CA  
485  C C   . LEU A 69  ? 0.24992 0.30192 0.31052 0.04516  -0.01985 -0.02941 76  LEU A C   
486  O O   . LEU A 69  ? 0.27236 0.32078 0.33748 0.05071  -0.00935 -0.02327 76  LEU A O   
487  C CB  . LEU A 69  ? 0.30713 0.35118 0.34266 0.06029  -0.01944 -0.02134 76  LEU A CB  
488  C CG  . LEU A 69  ? 0.37736 0.42730 0.40290 0.06782  -0.02590 -0.01783 76  LEU A CG  
489  C CD1 . LEU A 69  ? 0.46251 0.49109 0.46952 0.07524  -0.01561 -0.01059 76  LEU A CD1 
490  C CD2 . LEU A 69  ? 0.37258 0.42192 0.38652 0.06080  -0.03370 -0.02544 76  LEU A CD2 
491  N N   . HIS A 70  ? 0.26909 0.31668 0.32900 0.03523  -0.02355 -0.03668 77  HIS A N   
492  C CA  . HIS A 70  ? 0.25115 0.29269 0.31838 0.02951  -0.01709 -0.03707 77  HIS A CA  
493  C C   . HIS A 70  ? 0.25604 0.28468 0.31266 0.02148  -0.01967 -0.04374 77  HIS A C   
494  O O   . HIS A 70  ? 0.24917 0.27648 0.29625 0.02035  -0.02628 -0.04846 77  HIS A O   
495  C CB  . HIS A 70  ? 0.25581 0.31798 0.35078 0.02627  -0.01995 -0.03556 77  HIS A CB  
496  C CG  . HIS A 70  ? 0.25122 0.32494 0.35455 0.01897  -0.03409 -0.04271 77  HIS A CG  
497  N ND1 . HIS A 70  ? 0.38587 0.48248 0.50591 0.01962  -0.04443 -0.04205 77  HIS A ND1 
498  C CD2 . HIS A 70  ? 0.29765 0.36133 0.39269 0.01154  -0.03993 -0.05095 77  HIS A CD2 
499  C CE1 . HIS A 70  ? 0.31018 0.40788 0.42940 0.01165  -0.05647 -0.05077 77  HIS A CE1 
500  N NE2 . HIS A 70  ? 0.31660 0.39361 0.42051 0.00749  -0.05305 -0.05625 77  HIS A NE2 
501  N N   . ILE A 71  ? 0.22716 0.24586 0.28433 0.01752  -0.01303 -0.04289 78  ILE A N   
502  C CA  . ILE A 71  ? 0.24452 0.25091 0.29316 0.01126  -0.01454 -0.04720 78  ILE A CA  
503  C C   . ILE A 71  ? 0.28303 0.29182 0.34669 0.00563  -0.01322 -0.04694 78  ILE A C   
504  O O   . ILE A 71  ? 0.26918 0.27927 0.34093 0.00657  -0.00462 -0.04128 78  ILE A O   
505  C CB  . ILE A 71  ? 0.26569 0.25309 0.29453 0.01192  -0.00777 -0.04506 78  ILE A CB  
506  C CG1 . ILE A 71  ? 0.29020 0.27370 0.30574 0.01532  -0.00866 -0.04467 78  ILE A CG1 
507  C CG2 . ILE A 71  ? 0.28818 0.26669 0.31111 0.00651  -0.01072 -0.04806 78  ILE A CG2 
508  C CD1 . ILE A 71  ? 0.31888 0.28094 0.31360 0.01417  -0.00268 -0.04281 78  ILE A CD1 
509  N N   . ASN A 72  ? 0.25287 0.26060 0.31965 0.00017  -0.02039 -0.05254 79  ASN A N   
510  C CA  . ASN A 72  ? 0.24854 0.25384 0.32775 -0.00659 -0.01902 -0.05216 79  ASN A CA  
511  C C   . ASN A 72  ? 0.27994 0.26663 0.34475 -0.00804 -0.01778 -0.05346 79  ASN A C   
512  O O   . ASN A 72  ? 0.26625 0.24827 0.31939 -0.00581 -0.02294 -0.05784 79  ASN A O   
513  C CB  . ASN A 72  ? 0.24892 0.26515 0.34385 -0.01250 -0.02928 -0.05787 79  ASN A CB  
514  C CG  . ASN A 72  ? 0.25380 0.29229 0.36673 -0.01166 -0.03247 -0.05530 79  ASN A CG  
515  O OD1 . ASN A 72  ? 0.27238 0.31923 0.39363 -0.00740 -0.02392 -0.04740 79  ASN A OD1 
516  N ND2 . ASN A 72  ? 0.27628 0.32451 0.39445 -0.01474 -0.04495 -0.06171 79  ASN A ND2 
517  N N   . LEU A 73  ? 0.26789 0.24514 0.33416 -0.01097 -0.01051 -0.04861 80  LEU A N   
518  C CA  . LEU A 73  ? 0.25230 0.21200 0.30588 -0.01167 -0.00962 -0.04807 80  LEU A CA  
519  C C   . LEU A 73  ? 0.27092 0.22545 0.33731 -0.01848 -0.01012 -0.04859 80  LEU A C   
520  O O   . LEU A 73  ? 0.27322 0.23173 0.35429 -0.02338 -0.00379 -0.04360 80  LEU A O   
521  C CB  . LEU A 73  ? 0.26161 0.20974 0.30018 -0.00903 -0.00068 -0.04124 80  LEU A CB  
522  C CG  . LEU A 73  ? 0.27554 0.22411 0.29990 -0.00413 0.00068  -0.04082 80  LEU A CG  
523  C CD1 . LEU A 73  ? 0.28824 0.22091 0.29390 -0.00235 0.00930  -0.03525 80  LEU A CD1 
524  C CD2 . LEU A 73  ? 0.29603 0.24564 0.31093 -0.00253 -0.00823 -0.04553 80  LEU A CD2 
525  N N   . ILE A 74  ? 0.26504 0.21078 0.32734 -0.01898 -0.01699 -0.05446 81  ILE A N   
526  C CA  . ILE A 74  ? 0.29322 0.23021 0.36614 -0.02646 -0.01887 -0.05688 81  ILE A CA  
527  C C   . ILE A 74  ? 0.32860 0.24317 0.38819 -0.02384 -0.01688 -0.05504 81  ILE A C   
528  O O   . ILE A 74  ? 0.30968 0.21722 0.35923 -0.01843 -0.02212 -0.06031 81  ILE A O   
529  C CB  . ILE A 74  ? 0.26738 0.21026 0.34578 -0.02916 -0.02963 -0.06721 81  ILE A CB  
530  C CG1 . ILE A 74  ? 0.28630 0.25302 0.37474 -0.02880 -0.03295 -0.06780 81  ILE A CG1 
531  C CG2 . ILE A 74  ? 0.29181 0.22280 0.38051 -0.03928 -0.03220 -0.07036 81  ILE A CG2 
532  C CD1 . ILE A 74  ? 0.32313 0.29685 0.41295 -0.03067 -0.04500 -0.07773 81  ILE A CD1 
533  N N   . PRO A 75  ? 0.31876 0.22181 0.37768 -0.02634 -0.00848 -0.04661 82  PRO A N   
534  C CA  . PRO A 75  ? 0.33622 0.21610 0.38352 -0.02385 -0.00678 -0.04358 82  PRO A CA  
535  C C   . PRO A 75  ? 0.36908 0.23368 0.42523 -0.03140 -0.00897 -0.04794 82  PRO A C   
536  O O   . PRO A 75  ? 0.39765 0.26749 0.47189 -0.04247 -0.00853 -0.04894 82  PRO A O   
537  C CB  . PRO A 75  ? 0.33161 0.20464 0.37275 -0.02398 0.00396  -0.03198 82  PRO A CB  
538  C CG  . PRO A 75  ? 0.39645 0.28543 0.45594 -0.03117 0.00971  -0.02977 82  PRO A CG  
539  C CD  . PRO A 75  ? 0.34618 0.25669 0.41584 -0.03102 0.00101  -0.03867 82  PRO A CD  
540  N N   . ASN A 76  ? 0.36247 0.20714 0.40598 -0.02538 -0.01133 -0.05007 83  ASN A N   
541  C CA  . ASN A 76  ? 0.36889 0.19067 0.41512 -0.03158 -0.01267 -0.05454 83  ASN A CA  
542  C C   . ASN A 76  ? 0.45696 0.25292 0.48803 -0.02373 -0.00752 -0.04704 83  ASN A C   
543  O O   . ASN A 76  ? 0.44966 0.24134 0.46759 -0.01102 -0.01038 -0.04836 83  ASN A O   
544  C CB  . ASN A 76  ? 0.39888 0.22024 0.44272 -0.03024 -0.02224 -0.06835 83  ASN A CB  
545  C CG  . ASN A 76  ? 0.52285 0.31758 0.56796 -0.03930 -0.02463 -0.07501 83  ASN A CG  
546  O OD1 . ASN A 76  ? 0.52452 0.29147 0.56206 -0.03802 -0.01931 -0.07032 83  ASN A OD1 
547  N ND2 . ASN A 76  ? 0.61113 0.41275 0.66545 -0.04964 -0.03305 -0.08540 83  ASN A ND2 
548  N N   . LYS A 77  ? 0.45011 0.23018 0.48383 -0.03055 0.00059  -0.03789 84  LYS A N   
549  C CA  . LYS A 77  ? 0.50125 0.25574 0.51858 -0.02206 0.00589  -0.02855 84  LYS A CA  
550  C C   . LYS A 77  ? 0.54532 0.27008 0.55590 -0.01929 0.00342  -0.03444 84  LYS A C   
551  O O   . LYS A 77  ? 0.57478 0.28193 0.56999 -0.00649 0.00519  -0.02866 84  LYS A O   
552  C CB  . LYS A 77  ? 0.50593 0.24950 0.52524 -0.02960 0.01723  -0.01547 84  LYS A CB  
553  C CG  . LYS A 77  ? 0.52567 0.29159 0.54300 -0.02781 0.02222  -0.00797 84  LYS A CG  
554  C CD  . LYS A 77  ? 0.53720 0.28734 0.54984 -0.03170 0.03570  0.00663  84  LYS A CD  
555  C CE  . LYS A 77  ? 0.60581 0.37213 0.61228 -0.02958 0.04337  0.01425  84  LYS A CE  
556  N NZ  . LYS A 77  ? 0.73225 0.52678 0.76140 -0.03748 0.04299  0.00780  84  LYS A NZ  
557  N N   . GLN A 78  ? 0.59938 0.31677 0.61984 -0.03061 -0.00097 -0.04574 85  GLN A N   
558  C CA  . GLN A 78  ? 0.64138 0.32446 0.65097 -0.02791 -0.00278 -0.05287 85  GLN A CA  
559  C C   . GLN A 78  ? 0.66587 0.35266 0.66169 -0.01024 -0.00791 -0.06033 85  GLN A C   
560  O O   . GLN A 78  ? 0.67877 0.34016 0.65984 0.00274  -0.00521 -0.05862 85  GLN A O   
561  C CB  . GLN A 78  ? 0.59712 0.26954 0.61843 -0.04657 -0.00773 -0.06402 85  GLN A CB  
562  C CG  . GLN A 78  ? 0.86111 0.52177 0.89754 -0.06464 -0.00083 -0.05515 85  GLN A CG  
563  C CD  . GLN A 78  ? 1.02857 0.72275 1.08249 -0.07018 0.00512  -0.04379 85  GLN A CD  
564  O OE1 . GLN A 78  ? 0.98281 0.66775 1.04054 -0.07516 0.01608  -0.03027 85  GLN A OE1 
565  N NE2 . GLN A 78  ? 0.81346 0.54436 0.87683 -0.06904 -0.00093 -0.04896 85  GLN A NE2 
566  N N   . ASP A 79  ? 0.55453 0.27367 0.55552 -0.00829 -0.01393 -0.06677 86  ASP A N   
567  C CA  . ASP A 79  ? 0.54021 0.26891 0.53119 0.00775  -0.01729 -0.07238 86  ASP A CA  
568  C C   . ASP A 79  ? 0.51194 0.26023 0.50050 0.02088  -0.01518 -0.06086 86  ASP A C   
569  O O   . ASP A 79  ? 0.53167 0.28790 0.51449 0.03533  -0.01646 -0.06208 86  ASP A O   
570  C CB  . ASP A 79  ? 0.60656 0.35961 0.60302 0.00309  -0.02445 -0.08382 86  ASP A CB  
571  C CG  . ASP A 79  ? 0.73279 0.46812 0.72925 -0.00964 -0.02992 -0.09689 86  ASP A CG  
572  O OD1 . ASP A 79  ? 0.76629 0.46576 0.75383 -0.01138 -0.02817 -0.10017 86  ASP A OD1 
573  O OD2 . ASP A 79  ? 0.68466 0.44092 0.68898 -0.01795 -0.03672 -0.10382 86  ASP A OD2 
574  N N   . ARG A 80  ? 0.48388 0.23884 0.47604 0.01596  -0.01183 -0.04960 87  ARG A N   
575  C CA  . ARG A 80  ? 0.41269 0.18733 0.40109 0.02457  -0.01210 -0.03952 87  ARG A CA  
576  C C   . ARG A 80  ? 0.41948 0.22590 0.41283 0.02716  -0.01762 -0.04501 87  ARG A C   
577  O O   . ARG A 80  ? 0.44408 0.26382 0.43445 0.03858  -0.02035 -0.04200 87  ARG A O   
578  C CB  . ARG A 80  ? 0.49357 0.25315 0.47057 0.04001  -0.01081 -0.03089 87  ARG A CB  
579  C CG  . ARG A 80  ? 0.47682 0.24878 0.44772 0.04464  -0.01172 -0.01839 87  ARG A CG  
580  C CD  . ARG A 80  ? 0.63449 0.38915 0.59422 0.05895  -0.01083 -0.00754 87  ARG A CD  
581  N NE  . ARG A 80  ? 0.70552 0.47528 0.66749 0.07447  -0.01586 -0.00750 87  ARG A NE  
582  C CZ  . ARG A 80  ? 0.73238 0.48677 0.68921 0.09023  -0.01452 -0.00179 87  ARG A CZ  
583  N NH1 . ARG A 80  ? 0.77431 0.49334 0.72068 0.09240  -0.00855 0.00408  87  ARG A NH1 
584  N NH2 . ARG A 80  ? 0.69328 0.46907 0.65635 0.10467  -0.01866 -0.00021 87  ARG A NH2 
585  N N   . THR A 81  ? 0.39659 0.21697 0.39911 0.01612  -0.01922 -0.05178 88  THR A N   
586  C CA  . THR A 81  ? 0.37393 0.22123 0.38024 0.01738  -0.02345 -0.05640 88  THR A CA  
587  C C   . THR A 81  ? 0.35962 0.22253 0.37218 0.00800  -0.02233 -0.05358 88  THR A C   
588  O O   . THR A 81  ? 0.37298 0.23000 0.39248 -0.00164 -0.01910 -0.05274 88  THR A O   
589  C CB  . THR A 81  ? 0.38956 0.23870 0.39769 0.01691  -0.02714 -0.06880 88  THR A CB  
590  O OG1 . THR A 81  ? 0.40199 0.24164 0.41685 0.00410  -0.02811 -0.07434 88  THR A OG1 
591  C CG2 . THR A 81  ? 0.40323 0.23824 0.40207 0.02977  -0.02672 -0.07277 88  THR A CG2 
592  N N   . LEU A 82  ? 0.30656 0.18908 0.31739 0.01093  -0.02439 -0.05183 89  LEU A N   
593  C CA  . LEU A 82  ? 0.32619 0.22306 0.34100 0.00436  -0.02315 -0.05107 89  LEU A CA  
594  C C   . LEU A 82  ? 0.35356 0.26779 0.37228 0.00561  -0.02750 -0.05821 89  LEU A C   
595  O O   . LEU A 82  ? 0.33628 0.25840 0.35106 0.01235  -0.03021 -0.05869 89  LEU A O   
596  C CB  . LEU A 82  ? 0.32861 0.22783 0.33301 0.00620  -0.02167 -0.04296 89  LEU A CB  
597  C CG  . LEU A 82  ? 0.30968 0.21945 0.31427 0.00143  -0.01902 -0.04254 89  LEU A CG  
598  C CD1 . LEU A 82  ? 0.33902 0.24503 0.35311 -0.00523 -0.01214 -0.04127 89  LEU A CD1 
599  C CD2 . LEU A 82  ? 0.35659 0.26251 0.34531 0.00317  -0.01859 -0.03616 89  LEU A CD2 
600  N N   . THR A 83  ? 0.31602 0.23713 0.34324 -0.00038 -0.02812 -0.06277 90  THR A N   
601  C CA  . THR A 83  ? 0.30357 0.23901 0.33210 0.00131  -0.03228 -0.06888 90  THR A CA  
602  C C   . THR A 83  ? 0.31608 0.26494 0.34718 -0.00105 -0.03038 -0.06536 90  THR A C   
603  O O   . THR A 83  ? 0.32597 0.27515 0.36420 -0.00607 -0.02675 -0.06208 90  THR A O   
604  C CB  . THR A 83  ? 0.31310 0.24527 0.34671 -0.00253 -0.03676 -0.07748 90  THR A CB  
605  O OG1 . THR A 83  ? 0.36585 0.27962 0.39316 0.00060  -0.03756 -0.08168 90  THR A OG1 
606  C CG2 . THR A 83  ? 0.34346 0.28968 0.37439 0.00039  -0.04111 -0.08281 90  THR A CG2 
607  N N   . ILE A 84  ? 0.28124 0.24038 0.30694 0.00291  -0.03163 -0.06534 91  ILE A N   
608  C CA  . ILE A 84  ? 0.28511 0.25331 0.31052 0.00186  -0.02961 -0.06254 91  ILE A CA  
609  C C   . ILE A 84  ? 0.32882 0.30815 0.35649 0.00377  -0.03343 -0.06731 91  ILE A C   
610  O O   . ILE A 84  ? 0.31446 0.29738 0.33623 0.00799  -0.03540 -0.06968 91  ILE A O   
611  C CB  . ILE A 84  ? 0.30180 0.26924 0.31698 0.00320  -0.02817 -0.05793 91  ILE A CB  
612  C CG1 . ILE A 84  ? 0.36281 0.31824 0.37147 0.00185  -0.02603 -0.05313 91  ILE A CG1 
613  C CG2 . ILE A 84  ? 0.34578 0.31653 0.35763 0.00238  -0.02522 -0.05569 91  ILE A CG2 
614  C CD1 . ILE A 84  ? 0.40013 0.35315 0.40616 0.00516  -0.02973 -0.05204 91  ILE A CD1 
615  N N   . VAL A 85  ? 0.26558 0.25178 0.30195 0.00138  -0.03427 -0.06782 92  VAL A N   
616  C CA  . VAL A 85  ? 0.28171 0.27871 0.31908 0.00337  -0.03970 -0.07189 92  VAL A CA  
617  C C   . VAL A 85  ? 0.32709 0.33231 0.36336 0.00641  -0.03673 -0.06657 92  VAL A C   
618  O O   . VAL A 85  ? 0.31490 0.32104 0.35792 0.00536  -0.03191 -0.06156 92  VAL A O   
619  C CB  . VAL A 85  ? 0.29117 0.29252 0.34107 -0.00180 -0.04560 -0.07611 92  VAL A CB  
620  C CG1 . VAL A 85  ? 0.36823 0.37960 0.41368 0.00113  -0.05358 -0.08101 92  VAL A CG1 
621  C CG2 . VAL A 85  ? 0.36031 0.34756 0.41036 -0.00592 -0.04722 -0.08092 92  VAL A CG2 
622  N N   . ASP A 86  ? 0.28176 0.29185 0.30888 0.01108  -0.03843 -0.06706 93  ASP A N   
623  C CA  . ASP A 86  ? 0.27476 0.29051 0.30098 0.01460  -0.03585 -0.06161 93  ASP A CA  
624  C C   . ASP A 86  ? 0.30424 0.32987 0.32663 0.01901  -0.04208 -0.06377 93  ASP A C   
625  O O   . ASP A 86  ? 0.29535 0.32057 0.31008 0.01999  -0.04638 -0.06939 93  ASP A O   
626  C CB  . ASP A 86  ? 0.29192 0.29936 0.30654 0.01585  -0.02939 -0.05657 93  ASP A CB  
627  C CG  . ASP A 86  ? 0.31408 0.32189 0.31923 0.01702  -0.03020 -0.05778 93  ASP A CG  
628  O OD1 . ASP A 86  ? 0.34339 0.34679 0.34683 0.01417  -0.02893 -0.05785 93  ASP A OD1 
629  O OD2 . ASP A 86  ? 0.32886 0.34282 0.32887 0.02139  -0.03190 -0.05772 93  ASP A OD2 
630  N N   . THR A 87  ? 0.26577 0.29941 0.29147 0.02313  -0.04217 -0.05885 94  THR A N   
631  C CA  . THR A 87  ? 0.25119 0.29406 0.27036 0.02857  -0.04868 -0.05927 94  THR A CA  
632  C C   . THR A 87  ? 0.30048 0.33805 0.30507 0.03460  -0.04257 -0.05281 94  THR A C   
633  O O   . THR A 87  ? 0.29043 0.33387 0.29166 0.04120  -0.04409 -0.04784 94  THR A O   
634  C CB  . THR A 87  ? 0.24970 0.30827 0.28435 0.02984  -0.05510 -0.05723 94  THR A CB  
635  O OG1 . THR A 87  ? 0.28513 0.34381 0.32938 0.03243  -0.04650 -0.04922 94  THR A OG1 
636  C CG2 . THR A 87  ? 0.30216 0.36618 0.35155 0.02133  -0.06295 -0.06431 94  THR A CG2 
637  N N   . GLY A 88  ? 0.29429 0.32100 0.29047 0.03208  -0.03612 -0.05220 95  GLY A N   
638  C CA  . GLY A 88  ? 0.30324 0.32335 0.28691 0.03493  -0.02993 -0.04589 95  GLY A CA  
639  C C   . GLY A 88  ? 0.29117 0.31562 0.26207 0.03949  -0.03155 -0.04622 95  GLY A C   
640  O O   . GLY A 88  ? 0.28914 0.32130 0.25734 0.04255  -0.03888 -0.05143 95  GLY A O   
641  N N   . ILE A 89  ? 0.29307 0.31118 0.25489 0.03908  -0.02426 -0.04071 96  ILE A N   
642  C CA  . ILE A 89  ? 0.31893 0.34036 0.26648 0.04477  -0.02274 -0.03840 96  ILE A CA  
643  C C   . ILE A 89  ? 0.30385 0.33075 0.24894 0.04530  -0.02424 -0.04556 96  ILE A C   
644  O O   . ILE A 89  ? 0.33008 0.35976 0.26061 0.05190  -0.02445 -0.04618 96  ILE A O   
645  C CB  . ILE A 89  ? 0.31536 0.32833 0.25595 0.04297  -0.01309 -0.02896 96  ILE A CB  
646  C CG1 . ILE A 89  ? 0.36666 0.38168 0.29033 0.05045  -0.00968 -0.02366 96  ILE A CG1 
647  C CG2 . ILE A 89  ? 0.31035 0.32228 0.25947 0.03404  -0.00870 -0.02936 96  ILE A CG2 
648  C CD1 . ILE A 89  ? 0.43258 0.43628 0.34900 0.04931  -0.00088 -0.01262 96  ILE A CD1 
649  N N   . GLY A 90  ? 0.30008 0.32677 0.25672 0.03990  -0.02495 -0.05082 97  GLY A N   
650  C CA  . GLY A 90  ? 0.30832 0.33755 0.26199 0.04247  -0.02500 -0.05720 97  GLY A CA  
651  C C   . GLY A 90  ? 0.32056 0.35374 0.27041 0.04440  -0.01530 -0.05133 97  GLY A C   
652  O O   . GLY A 90  ? 0.33064 0.36398 0.28248 0.04079  -0.00945 -0.04265 97  GLY A O   
653  N N   . MET A 91  ? 0.31689 0.35255 0.26270 0.04965  -0.01312 -0.05608 98  MET A N   
654  C CA  . MET A 91  ? 0.31477 0.35850 0.26219 0.05235  -0.00253 -0.04999 98  MET A CA  
655  C C   . MET A 91  ? 0.32280 0.36585 0.25085 0.06375  0.00153  -0.05408 98  MET A C   
656  O O   . MET A 91  ? 0.34979 0.38490 0.26817 0.06823  -0.00452 -0.06463 98  MET A O   
657  C CB  . MET A 91  ? 0.29673 0.34575 0.26267 0.04892  -0.00152 -0.05018 98  MET A CB  
658  C CG  . MET A 91  ? 0.31719 0.36670 0.29825 0.03750  -0.00408 -0.04472 98  MET A CG  
659  S SD  . MET A 91  ? 0.32388 0.38069 0.32401 0.03421  -0.00549 -0.04403 98  MET A SD  
660  C CE  . MET A 91  ? 0.35951 0.40256 0.35599 0.03637  -0.01370 -0.05459 98  MET A CE  
661  N N   . THR A 92  ? 0.32988 0.37951 0.25098 0.06819  0.01253  -0.04584 99  THR A N   
662  C CA  . THR A 92  ? 0.34453 0.39326 0.24530 0.08075  0.01993  -0.04878 99  THR A CA  
663  C C   . THR A 92  ? 0.35400 0.40946 0.26668 0.08563  0.02725  -0.05030 99  THR A C   
664  O O   . THR A 92  ? 0.33358 0.39696 0.27089 0.07878  0.02603  -0.04739 99  THR A O   
665  C CB  . THR A 92  ? 0.41014 0.46424 0.29978 0.08453  0.03183  -0.03741 99  THR A CB  
666  O OG1 . THR A 92  ? 0.40145 0.47015 0.31578 0.07774  0.04166  -0.02603 99  THR A OG1 
667  C CG2 . THR A 92  ? 0.43139 0.47833 0.30980 0.08135  0.02556  -0.03370 99  THR A CG2 
668  N N   . LYS A 93  ? 0.31590 0.37423 0.28091 0.07971  -0.02071 -0.08394 100 LYS A N   
669  C CA  . LYS A 93  ? 0.32335 0.37974 0.29155 0.07793  -0.01034 -0.08668 100 LYS A CA  
670  C C   . LYS A 93  ? 0.31429 0.37082 0.28046 0.07587  -0.00328 -0.07306 100 LYS A C   
671  O O   . LYS A 93  ? 0.30886 0.36182 0.28783 0.07587  0.00198  -0.07296 100 LYS A O   
672  C CB  . LYS A 93  ? 0.33983 0.40681 0.29431 0.08198  -0.00929 -0.09815 100 LYS A CB  
673  C CG  . LYS A 93  ? 0.39261 0.45873 0.35219 0.08705  -0.00213 -0.10710 100 LYS A CG  
674  C CD  . LYS A 93  ? 0.36861 0.44763 0.31491 0.09385  -0.00186 -0.12343 100 LYS A CD  
675  C CE  . LYS A 93  ? 0.44735 0.51999 0.39842 0.10556  -0.00064 -0.13903 100 LYS A CE  
676  N NZ  . LYS A 93  ? 0.46643 0.56934 0.40710 0.11496  0.00427  -0.15368 100 LYS A NZ  
677  N N   . ALA A 94  ? 0.33141 0.38937 0.27743 0.07239  -0.00472 -0.06136 101 ALA A N   
678  C CA  . ALA A 94  ? 0.36262 0.42152 0.30332 0.06376  0.00229  -0.04834 101 ALA A CA  
679  C C   . ALA A 94  ? 0.34341 0.38775 0.30118 0.06266  0.00087  -0.04147 101 ALA A C   
680  O O   . ALA A 94  ? 0.35518 0.40630 0.32218 0.05804  0.00828  -0.03803 101 ALA A O   
681  C CB  . ALA A 94  ? 0.40710 0.45720 0.31197 0.05422  -0.00140 -0.03474 101 ALA A CB  
682  N N   . ASP A 95  ? 0.33431 0.36442 0.29699 0.06745  -0.00896 -0.04184 102 ASP A N   
683  C CA  . ASP A 95  ? 0.35839 0.37933 0.33731 0.06641  -0.00937 -0.03862 102 ASP A CA  
684  C C   . ASP A 95  ? 0.29180 0.31764 0.29051 0.06489  -0.00183 -0.04532 102 ASP A C   
685  O O   . ASP A 95  ? 0.32475 0.34634 0.33136 0.06151  0.00180  -0.03970 102 ASP A O   
686  C CB  . ASP A 95  ? 0.33862 0.35664 0.32355 0.07390  -0.02060 -0.04539 102 ASP A CB  
687  C CG  . ASP A 95  ? 0.43807 0.43832 0.39926 0.08112  -0.03455 -0.03831 102 ASP A CG  
688  O OD1 . ASP A 95  ? 0.49552 0.47565 0.43343 0.07395  -0.03437 -0.02346 102 ASP A OD1 
689  O OD2 . ASP A 95  ? 0.45123 0.45689 0.41383 0.09346  -0.04733 -0.04884 102 ASP A OD2 
690  N N   . LEU A 96  ? 0.32211 0.35101 0.32468 0.06690  -0.00187 -0.05756 103 LEU A N   
691  C CA  . LEU A 96  ? 0.30587 0.32396 0.31601 0.06490  0.00082  -0.06290 103 LEU A CA  
692  C C   . LEU A 96  ? 0.30041 0.32102 0.31102 0.07039  0.00491  -0.06032 103 LEU A C   
693  O O   . LEU A 96  ? 0.32141 0.33159 0.33748 0.07008  0.00490  -0.05704 103 LEU A O   
694  C CB  . LEU A 96  ? 0.29617 0.30801 0.30124 0.06432  -0.00174 -0.07642 103 LEU A CB  
695  C CG  . LEU A 96  ? 0.28965 0.30596 0.29912 0.05466  -0.00504 -0.08334 103 LEU A CG  
696  C CD1 . LEU A 96  ? 0.30412 0.31240 0.30400 0.05156  -0.00762 -0.09714 103 LEU A CD1 
697  C CD2 . LEU A 96  ? 0.28921 0.29761 0.30534 0.04190  -0.00297 -0.08145 103 LEU A CD2 
698  N N   . ILE A 97  ? 0.28371 0.32354 0.28828 0.07514  0.00815  -0.06322 104 ILE A N   
699  C CA  . ILE A 97  ? 0.28593 0.34444 0.29533 0.08159  0.01266  -0.06706 104 ILE A CA  
700  C C   . ILE A 97  ? 0.29666 0.36422 0.31216 0.07344  0.01643  -0.05485 104 ILE A C   
701  O O   . ILE A 97  ? 0.31725 0.39464 0.34367 0.07883  0.01690  -0.05807 104 ILE A O   
702  C CB  . ILE A 97  ? 0.32771 0.41498 0.32842 0.08456  0.01758  -0.07592 104 ILE A CB  
703  C CG1 . ILE A 97  ? 0.34748 0.42188 0.34291 0.09463  0.01212  -0.09108 104 ILE A CG1 
704  C CG2 . ILE A 97  ? 0.32253 0.44707 0.33226 0.08986  0.02409  -0.08433 104 ILE A CG2 
705  C CD1 . ILE A 97  ? 0.36386 0.46363 0.34681 0.09669  0.01589  -0.10094 104 ILE A CD1 
706  N N   . ASN A 98  ? 0.29812 0.35985 0.30424 0.06176  0.01666  -0.04213 105 ASN A N   
707  C CA  . ASN A 98  ? 0.34917 0.41098 0.35466 0.05070  0.01862  -0.03012 105 ASN A CA  
708  C C   . ASN A 98  ? 0.31836 0.35791 0.33425 0.05202  0.01368  -0.02634 105 ASN A C   
709  O O   . ASN A 98  ? 0.31278 0.33586 0.32302 0.04676  0.00969  -0.01838 105 ASN A O   
710  C CB  . ASN A 98  ? 0.36273 0.41496 0.34326 0.03816  0.01718  -0.01836 105 ASN A CB  
711  C CG  . ASN A 98  ? 0.63791 0.71734 0.60300 0.02733  0.02554  -0.01904 105 ASN A CG  
712  O OD1 . ASN A 98  ? 0.67718 0.77117 0.63561 0.01027  0.03200  -0.01298 105 ASN A OD1 
713  N ND2 . ASN A 98  ? 0.70675 0.79539 0.66291 0.03354  0.02592  -0.02707 105 ASN A ND2 
714  N N   . ASN A 99  ? 0.32259 0.35930 0.34988 0.05991  0.01257  -0.03348 106 ASN A N   
715  C CA  . ASN A 99  ? 0.30319 0.32123 0.33577 0.05809  0.00927  -0.03034 106 ASN A CA  
716  C C   . ASN A 99  ? 0.32516 0.32973 0.35542 0.05339  0.00662  -0.02967 106 ASN A C   
717  O O   . ASN A 99  ? 0.30084 0.29970 0.33352 0.04890  0.00539  -0.02550 106 ASN A O   
718  C CB  . ASN A 99  ? 0.27417 0.29970 0.31197 0.05266  0.01059  -0.02308 106 ASN A CB  
719  C CG  . ASN A 99  ? 0.26458 0.31721 0.31040 0.05851  0.01262  -0.02899 106 ASN A CG  
720  O OD1 . ASN A 99  ? 0.32251 0.37165 0.37164 0.07192  0.00770  -0.03763 106 ASN A OD1 
721  N ND2 . ASN A 99  ? 0.32605 0.40470 0.37266 0.04804  0.01824  -0.02590 106 ASN A ND2 
722  N N   . LEU A 100 ? 0.29472 0.29890 0.32178 0.05537  0.00518  -0.03729 107 LEU A N   
723  C CA  . LEU A 100 ? 0.29113 0.29526 0.32072 0.05168  0.00234  -0.04276 107 LEU A CA  
724  C C   . LEU A 100 ? 0.30983 0.31670 0.33925 0.05457  -0.00220 -0.03882 107 LEU A C   
725  O O   . LEU A 100 ? 0.33493 0.34519 0.37135 0.05368  -0.00447 -0.04365 107 LEU A O   
726  C CB  . LEU A 100 ? 0.26727 0.26231 0.29892 0.04193  0.00403  -0.04631 107 LEU A CB  
727  C CG  . LEU A 100 ? 0.35824 0.33453 0.37942 0.04098  0.00343  -0.04937 107 LEU A CG  
728  C CD1 . LEU A 100 ? 0.38519 0.34208 0.40022 0.04402  0.00149  -0.04289 107 LEU A CD1 
729  C CD2 . LEU A 100 ? 0.42710 0.39525 0.44023 0.02926  0.00271  -0.05927 107 LEU A CD2 
730  N N   . GLY A 101 ? 0.29068 0.29449 0.30779 0.05785  -0.00480 -0.03172 108 GLY A N   
731  C CA  . GLY A 101 ? 0.33891 0.33002 0.34395 0.06191  -0.01403 -0.02697 108 GLY A CA  
732  C C   . GLY A 101 ? 0.36438 0.34143 0.36814 0.05773  -0.01498 -0.01966 108 GLY A C   
733  O O   . GLY A 101 ? 0.42679 0.38610 0.41955 0.06403  -0.02592 -0.01925 108 GLY A O   
734  N N   . THR A 102 ? 0.34061 0.32294 0.35333 0.04942  -0.00636 -0.01551 109 THR A N   
735  C CA  . THR A 102 ? 0.33296 0.30579 0.34644 0.04392  -0.00677 -0.01031 109 THR A CA  
736  C C   . THR A 102 ? 0.39092 0.36286 0.39366 0.03210  -0.00319 0.00026  109 THR A C   
737  O O   . THR A 102 ? 0.38911 0.37738 0.38993 0.02868  0.00265  0.00111  109 THR A O   
738  C CB  . THR A 102 ? 0.35767 0.33960 0.38714 0.04194  -0.00145 -0.01468 109 THR A CB  
739  O OG1 . THR A 102 ? 0.34213 0.33403 0.37563 0.03986  0.00402  -0.01243 109 THR A OG1 
740  C CG2 . THR A 102 ? 0.38961 0.37901 0.42704 0.04477  -0.00131 -0.02605 109 THR A CG2 
741  N N   . ILE A 103 ? 0.32758 0.28501 0.32403 0.02433  -0.00617 0.00569  110 ILE A N   
742  C CA  . ILE A 103 ? 0.31748 0.28176 0.30618 0.00688  -0.00122 0.01364  110 ILE A CA  
743  C C   . ILE A 103 ? 0.31526 0.30431 0.32737 0.00720  0.00433  0.00905  110 ILE A C   
744  O O   . ILE A 103 ? 0.33147 0.31828 0.34439 -0.00178 0.00321  0.01136  110 ILE A O   
745  C CB  . ILE A 103 ? 0.41926 0.34675 0.37998 -0.00573 -0.00977 0.02257  110 ILE A CB  
746  C CG1 . ILE A 103 ? 0.45527 0.36122 0.42041 0.00519  -0.01866 0.01719  110 ILE A CG1 
747  C CG2 . ILE A 103 ? 0.43421 0.33091 0.36071 -0.00768 -0.01805 0.02970  110 ILE A CG2 
748  C CD1 . ILE A 103 ? 0.59006 0.45682 0.52826 -0.00750 -0.02809 0.02384  110 ILE A CD1 
749  N N   . ALA A 104 ? 0.30429 0.31282 0.33186 0.01836  0.00801  0.00196  111 ALA A N   
750  C CA  . ALA A 104 ? 0.30110 0.31920 0.34326 0.02395  0.00772  -0.00237 111 ALA A CA  
751  C C   . ALA A 104 ? 0.29008 0.33435 0.34020 0.01661  0.00950  -0.00280 111 ALA A C   
752  O O   . ALA A 104 ? 0.28573 0.32965 0.34191 0.01784  0.00582  -0.00362 111 ALA A O   
753  C CB  . ALA A 104 ? 0.31922 0.34033 0.36663 0.03737  0.00752  -0.00964 111 ALA A CB  
754  N N   . LYS A 105 ? 0.28830 0.35994 0.33784 0.00702  0.01520  -0.00371 112 LYS A N   
755  C CA  . LYS A 105 ? 0.26278 0.37258 0.32436 -0.00219 0.01762  -0.00843 112 LYS A CA  
756  C C   . LYS A 105 ? 0.32422 0.41734 0.37677 -0.02133 0.01530  -0.00060 112 LYS A C   
757  O O   . LYS A 105 ? 0.29098 0.39579 0.35527 -0.01999 0.01145  -0.00431 112 LYS A O   
758  C CB  . LYS A 105 ? 0.24978 0.40380 0.31243 -0.01342 0.02701  -0.01432 112 LYS A CB  
759  C CG  . LYS A 105 ? 0.32148 0.52719 0.39856 -0.02770 0.03110  -0.02252 112 LYS A CG  
760  C CD  . LYS A 105 ? 0.36299 0.62378 0.44071 -0.04299 0.04337  -0.03160 112 LYS A CD  
761  C CE  . LYS A 105 ? 0.48366 0.81731 0.58672 -0.05214 0.04730  -0.04814 112 LYS A CE  
762  N NZ  . LYS A 105 ? 0.52825 0.93589 0.64232 -0.05824 0.05950  -0.06630 112 LYS A NZ  
763  N N   . SER A 106 ? 0.30243 0.36225 0.33016 -0.03756 0.01488  0.00960  113 SER A N   
764  C CA  . SER A 106 ? 0.30692 0.34106 0.32062 -0.05461 0.01000  0.01556  113 SER A CA  
765  C C   . SER A 106 ? 0.29093 0.29619 0.30883 -0.03822 0.00202  0.01400  113 SER A C   
766  O O   . SER A 106 ? 0.33012 0.32970 0.34791 -0.04576 -0.00185 0.01328  113 SER A O   
767  C CB  . SER A 106 ? 0.44638 0.44110 0.42290 -0.07514 0.00755  0.02674  113 SER A CB  
768  O OG  . SER A 106 ? 0.43716 0.39350 0.40197 -0.05607 0.00015  0.02911  113 SER A OG  
769  N N   . GLY A 107 ? 0.27964 0.27133 0.30071 -0.01852 0.00030  0.01174  114 GLY A N   
770  C CA  . GLY A 107 ? 0.29909 0.27534 0.32481 -0.00678 -0.00428 0.00745  114 GLY A CA  
771  C C   . GLY A 107 ? 0.27546 0.27265 0.31571 -0.00341 -0.00390 0.00372  114 GLY A C   
772  O O   . GLY A 107 ? 0.28834 0.27667 0.32656 -0.00554 -0.00760 0.00217  114 GLY A O   
773  N N   . THR A 108 ? 0.25176 0.27413 0.30360 0.00432  -0.00168 0.00089  115 THR A N   
774  C CA  . THR A 108 ? 0.25681 0.29322 0.31692 0.01198  -0.00644 -0.00311 115 THR A CA  
775  C C   . THR A 108 ? 0.27114 0.32755 0.33677 0.00004  -0.00866 -0.00435 115 THR A C   
776  O O   . THR A 108 ? 0.28123 0.33504 0.34619 0.00234  -0.01494 -0.00577 115 THR A O   
777  C CB  . THR A 108 ? 0.27613 0.33307 0.34516 0.02724  -0.00780 -0.00928 115 THR A CB  
778  O OG1 . THR A 108 ? 0.29860 0.33161 0.35911 0.03523  -0.00651 -0.00844 115 THR A OG1 
779  C CG2 . THR A 108 ? 0.28613 0.34760 0.35704 0.04030  -0.01823 -0.01388 115 THR A CG2 
780  N N   . LYS A 109 ? 0.24589 0.32358 0.31404 -0.01575 -0.00362 -0.00422 116 LYS A N   
781  C CA  . LYS A 109 ? 0.24052 0.34074 0.31270 -0.03393 -0.00468 -0.00663 116 LYS A CA  
782  C C   . LYS A 109 ? 0.25411 0.31574 0.31064 -0.04333 -0.00958 -0.00203 116 LYS A C   
783  O O   . LYS A 109 ? 0.29573 0.36701 0.35649 -0.04685 -0.01488 -0.00593 116 LYS A O   
784  C CB  . LYS A 109 ? 0.26784 0.39248 0.33681 -0.05770 0.00366  -0.00603 116 LYS A CB  
785  C CG  . LYS A 109 ? 0.33773 0.48708 0.40673 -0.08668 0.00434  -0.00884 116 LYS A CG  
786  C CD  . LYS A 109 ? 0.46704 0.63255 0.52139 -0.12016 0.01434  -0.00574 116 LYS A CD  
787  C CE  . LYS A 109 ? 0.52418 0.73403 0.58473 -0.15202 0.01697  -0.01324 116 LYS A CE  
788  N NZ  . LYS A 109 ? 0.60677 0.86161 0.70041 -0.13189 0.00974  -0.02763 116 LYS A NZ  
789  N N   . ALA A 110 ? 0.27854 0.29729 0.31660 -0.04422 -0.00977 0.00374  117 ALA A N   
790  C CA  . ALA A 110 ? 0.30480 0.28853 0.32813 -0.04858 -0.01625 0.00343  117 ALA A CA  
791  C C   . ALA A 110 ? 0.26793 0.25168 0.29759 -0.03331 -0.01913 -0.00187 117 ALA A C   
792  O O   . ALA A 110 ? 0.32624 0.30110 0.35013 -0.03831 -0.02400 -0.00561 117 ALA A O   
793  C CB  . ALA A 110 ? 0.32082 0.26115 0.32320 -0.04591 -0.01950 0.00669  117 ALA A CB  
794  N N   . PHE A 111 ? 0.28263 0.27190 0.31868 -0.01757 -0.01632 -0.00227 118 PHE A N   
795  C CA  . PHE A 111 ? 0.26433 0.25077 0.29779 -0.00938 -0.01829 -0.00521 118 PHE A CA  
796  C C   . PHE A 111 ? 0.28974 0.29494 0.32696 -0.01050 -0.02435 -0.00604 118 PHE A C   
797  O O   . PHE A 111 ? 0.28195 0.28084 0.31054 -0.01330 -0.02848 -0.00849 118 PHE A O   
798  C CB  . PHE A 111 ? 0.27735 0.26159 0.31082 0.00136  -0.01486 -0.00405 118 PHE A CB  
799  C CG  . PHE A 111 ? 0.25070 0.22494 0.27191 0.00316  -0.01581 -0.00500 118 PHE A CG  
800  C CD1 . PHE A 111 ? 0.29169 0.26011 0.30273 -0.00337 -0.01576 -0.00952 118 PHE A CD1 
801  C CD2 . PHE A 111 ? 0.28483 0.25202 0.29913 0.00930  -0.01703 -0.00208 118 PHE A CD2 
802  C CE1 . PHE A 111 ? 0.28643 0.24708 0.27980 -0.00777 -0.01478 -0.00976 118 PHE A CE1 
803  C CE2 . PHE A 111 ? 0.32438 0.27309 0.31651 0.00439  -0.01819 -0.00065 118 PHE A CE2 
804  C CZ  . PHE A 111 ? 0.31658 0.26451 0.29737 -0.00645 -0.01606 -0.00390 118 PHE A CZ  
805  N N   . MET A 112 ? 0.29872 0.33182 0.34921 -0.00681 -0.02601 -0.00661 119 MET A N   
806  C CA  . MET A 112 ? 0.30963 0.36688 0.36616 -0.00294 -0.03520 -0.01103 119 MET A CA  
807  C C   . MET A 112 ? 0.32572 0.39221 0.38319 -0.02043 -0.03724 -0.01415 119 MET A C   
808  O O   . MET A 112 ? 0.31508 0.38542 0.36814 -0.01881 -0.04581 -0.01721 119 MET A O   
809  C CB  . MET A 112 ? 0.25459 0.35068 0.32980 0.00758  -0.03726 -0.01706 119 MET A CB  
810  C CG  . MET A 112 ? 0.28887 0.37287 0.36076 0.02800  -0.03893 -0.01668 119 MET A CG  
811  S SD  . MET A 112 ? 0.37318 0.40738 0.41492 0.04051  -0.04947 -0.01042 119 MET A SD  
812  C CE  . MET A 112 ? 0.43324 0.48697 0.47520 0.05284  -0.06788 -0.01686 119 MET A CE  
813  N N   . GLU A 113 ? 0.27721 0.34250 0.33512 -0.03904 -0.03107 -0.01313 120 GLU A N   
814  C CA  . GLU A 113 ? 0.29102 0.35353 0.34276 -0.05978 -0.03417 -0.01599 120 GLU A CA  
815  C C   . GLU A 113 ? 0.33941 0.36483 0.37372 -0.05652 -0.03834 -0.01706 120 GLU A C   
816  O O   . GLU A 113 ? 0.36559 0.39505 0.39621 -0.06346 -0.04474 -0.02230 120 GLU A O   
817  C CB  . GLU A 113 ? 0.38873 0.43865 0.43108 -0.08270 -0.02867 -0.01205 120 GLU A CB  
818  C CG  . GLU A 113 ? 0.37422 0.47482 0.43206 -0.09826 -0.02291 -0.01489 120 GLU A CG  
819  C CD  . GLU A 113 ? 0.63729 0.71785 0.67608 -0.12185 -0.01576 -0.00712 120 GLU A CD  
820  O OE1 . GLU A 113 ? 0.65468 0.67889 0.66958 -0.11853 -0.01784 0.00083  120 GLU A OE1 
821  O OE2 . GLU A 113 ? 0.55791 0.68128 0.60356 -0.14384 -0.00885 -0.01017 120 GLU A OE2 
822  N N   . ALA A 114 ? 0.30646 0.30239 0.33128 -0.04572 -0.03472 -0.01491 121 ALA A N   
823  C CA  . ALA A 114 ? 0.28747 0.26031 0.29857 -0.04154 -0.03705 -0.02077 121 ALA A CA  
824  C C   . ALA A 114 ? 0.33992 0.32657 0.34807 -0.03589 -0.04034 -0.02230 121 ALA A C   
825  O O   . ALA A 114 ? 0.35558 0.33610 0.35263 -0.03997 -0.04422 -0.02881 121 ALA A O   
826  C CB  . ALA A 114 ? 0.31004 0.26440 0.31690 -0.03000 -0.03205 -0.02219 121 ALA A CB  
827  N N   . LEU A 115 ? 0.31291 0.31135 0.32478 -0.02567 -0.04035 -0.01677 122 LEU A N   
828  C CA  . LEU A 115 ? 0.31708 0.31624 0.31510 -0.02052 -0.04744 -0.01581 122 LEU A CA  
829  C C   . LEU A 115 ? 0.33089 0.35034 0.33264 -0.02457 -0.05802 -0.01994 122 LEU A C   
830  O O   . LEU A 115 ? 0.38996 0.40400 0.37456 -0.02618 -0.06441 -0.02201 122 LEU A O   
831  C CB  . LEU A 115 ? 0.29861 0.29490 0.29323 -0.00725 -0.05039 -0.00921 122 LEU A CB  
832  C CG  . LEU A 115 ? 0.32483 0.30067 0.31091 -0.00634 -0.04076 -0.00580 122 LEU A CG  
833  C CD1 . LEU A 115 ? 0.36968 0.33630 0.35013 0.00607  -0.04610 -0.00014 122 LEU A CD1 
834  C CD2 . LEU A 115 ? 0.33260 0.29294 0.29477 -0.01595 -0.03630 -0.00768 122 LEU A CD2 
835  N N   . GLN A 116 ? 0.32917 0.37654 0.35222 -0.02886 -0.05955 -0.02262 123 GLN A N   
836  C CA  . GLN A 116 ? 0.38630 0.46153 0.41647 -0.03714 -0.06878 -0.02994 123 GLN A CA  
837  C C   . GLN A 116 ? 0.39131 0.44775 0.40866 -0.05384 -0.06845 -0.03480 123 GLN A C   
838  O O   . GLN A 116 ? 0.42361 0.49140 0.43576 -0.05768 -0.07778 -0.04073 123 GLN A O   
839  C CB  . GLN A 116 ? 0.37715 0.49433 0.43331 -0.04505 -0.06684 -0.03450 123 GLN A CB  
840  C CG  . GLN A 116 ? 0.60466 0.75336 0.67653 -0.02337 -0.07215 -0.03691 123 GLN A CG  
841  C CD  . GLN A 116 ? 0.72037 0.87332 0.78329 -0.00251 -0.09014 -0.04013 123 GLN A CD  
842  O OE1 . GLN A 116 ? 0.74357 0.86394 0.78673 0.01613  -0.09590 -0.03317 123 GLN A OE1 
843  N NE2 . GLN A 116 ? 0.61307 0.80258 0.68581 -0.00745 -0.10067 -0.05057 123 GLN A NE2 
844  N N   . ALA A 117 ? 0.37758 0.40395 0.38791 -0.06153 -0.06042 -0.03427 124 ALA A N   
845  C CA  . ALA A 117 ? 0.41705 0.41770 0.41190 -0.07270 -0.06281 -0.04205 124 ALA A CA  
846  C C   . ALA A 117 ? 0.43732 0.42066 0.41472 -0.06225 -0.06188 -0.04719 124 ALA A C   
847  O O   . ALA A 117 ? 0.47666 0.43897 0.44142 -0.06602 -0.06373 -0.05756 124 ALA A O   
848  C CB  . ALA A 117 ? 0.47174 0.44131 0.46105 -0.08199 -0.05949 -0.04136 124 ALA A CB  
849  N N   . GLY A 118 ? 0.38571 0.37590 0.35863 -0.05084 -0.05930 -0.04179 125 GLY A N   
850  C CA  . GLY A 118 ? 0.41578 0.39726 0.36810 -0.04857 -0.05655 -0.04738 125 GLY A CA  
851  C C   . GLY A 118 ? 0.41738 0.39049 0.36714 -0.04260 -0.04529 -0.04901 125 GLY A C   
852  O O   . GLY A 118 ? 0.42555 0.40048 0.35969 -0.04441 -0.04042 -0.05771 125 GLY A O   
853  N N   . ALA A 119 ? 0.34712 0.31690 0.31181 -0.03705 -0.04067 -0.04304 126 ALA A N   
854  C CA  . ALA A 119 ? 0.32680 0.29508 0.29113 -0.03165 -0.03100 -0.04640 126 ALA A CA  
855  C C   . ALA A 119 ? 0.37744 0.34949 0.32587 -0.03519 -0.02703 -0.03882 126 ALA A C   
856  O O   . ALA A 119 ? 0.43560 0.40405 0.37388 -0.03607 -0.03454 -0.02853 126 ALA A O   
857  C CB  . ALA A 119 ? 0.32346 0.28583 0.30429 -0.02517 -0.02878 -0.04136 126 ALA A CB  
858  N N   . ASP A 120 ? 0.36207 0.34012 0.30510 -0.03785 -0.01692 -0.04529 127 ASP A N   
859  C CA  . ASP A 120 ? 0.37775 0.35125 0.29824 -0.04792 -0.01239 -0.03679 127 ASP A CA  
860  C C   . ASP A 120 ? 0.33807 0.30264 0.26784 -0.04271 -0.01083 -0.02712 127 ASP A C   
861  O O   . ASP A 120 ? 0.33763 0.30964 0.29102 -0.03390 -0.00756 -0.03191 127 ASP A O   
862  C CB  . ASP A 120 ? 0.38699 0.38012 0.29422 -0.06115 0.00024  -0.05111 127 ASP A CB  
863  C CG  . ASP A 120 ? 0.72254 0.73131 0.62361 -0.06373 0.00047  -0.06706 127 ASP A CG  
864  O OD1 . ASP A 120 ? 0.70862 0.74285 0.62308 -0.05906 0.00727  -0.08887 127 ASP A OD1 
865  O OD2 . ASP A 120 ? 0.66586 0.66275 0.54765 -0.06853 -0.00767 -0.05987 127 ASP A OD2 
866  N N   . ILE A 121 ? 0.36639 0.30999 0.27132 -0.04843 -0.01468 -0.01432 128 ILE A N   
867  C CA  . ILE A 121 ? 0.35535 0.28557 0.26216 -0.04491 -0.01393 -0.00698 128 ILE A CA  
868  C C   . ILE A 121 ? 0.34649 0.29446 0.26310 -0.05298 0.00012  -0.01729 128 ILE A C   
869  O O   . ILE A 121 ? 0.36185 0.31171 0.29685 -0.04467 0.00198  -0.01715 128 ILE A O   
870  C CB  . ILE A 121 ? 0.41739 0.31006 0.28340 -0.05136 -0.02359 0.00660  128 ILE A CB  
871  C CG1 . ILE A 121 ? 0.44594 0.32756 0.31471 -0.03132 -0.04197 0.01359  128 ILE A CG1 
872  C CG2 . ILE A 121 ? 0.48355 0.35630 0.33729 -0.05809 -0.01979 0.01085  128 ILE A CG2 
873  C CD1 . ILE A 121 ? 0.51670 0.35245 0.33416 -0.03400 -0.05823 0.02564  128 ILE A CD1 
874  N N   . SER A 122 ? 0.37133 0.33845 0.27656 -0.06891 0.00991  -0.02877 129 SER A N   
875  C CA  . SER A 122 ? 0.32957 0.32672 0.24873 -0.07527 0.02258  -0.04395 129 SER A CA  
876  C C   . SER A 122 ? 0.35402 0.37159 0.31151 -0.05294 0.02141  -0.05653 129 SER A C   
877  O O   . SER A 122 ? 0.35163 0.39509 0.32381 -0.05238 0.02829  -0.07011 129 SER A O   
878  C CB  . SER A 122 ? 0.36561 0.39079 0.26641 -0.09716 0.03386  -0.05816 129 SER A CB  
879  O OG  . SER A 122 ? 0.44245 0.48620 0.35505 -0.08621 0.03186  -0.07145 129 SER A OG  
880  N N   . MET A 123 ? 0.30656 0.31350 0.27622 -0.03710 0.01209  -0.05415 130 MET A N   
881  C CA  . MET A 123 ? 0.31528 0.32471 0.30908 -0.01836 0.00731  -0.06175 130 MET A CA  
882  C C   . MET A 123 ? 0.31848 0.31478 0.32273 -0.01056 0.00457  -0.05018 130 MET A C   
883  O O   . MET A 123 ? 0.31984 0.31018 0.33566 0.00222  -0.00103 -0.05303 130 MET A O   
884  C CB  . MET A 123 ? 0.31169 0.30870 0.30676 -0.01075 -0.00182 -0.06426 130 MET A CB  
885  C CG  . MET A 123 ? 0.34222 0.35739 0.32756 -0.01588 0.00117  -0.08165 130 MET A CG  
886  S SD  . MET A 123 ? 0.42717 0.42098 0.40580 -0.01362 -0.01048 -0.08111 130 MET A SD  
887  C CE  . MET A 123 ? 0.53800 0.50635 0.52776 0.00291  -0.02152 -0.08468 130 MET A CE  
888  N N   . ILE A 124 ? 0.28543 0.27372 0.28138 -0.01788 0.00722  -0.03870 131 ILE A N   
889  C CA  . ILE A 124 ? 0.29050 0.26845 0.29542 -0.00949 0.00441  -0.02926 131 ILE A CA  
890  C C   . ILE A 124 ? 0.27005 0.25872 0.29100 0.00070  0.00520  -0.03833 131 ILE A C   
891  O O   . ILE A 124 ? 0.27989 0.25954 0.30767 0.00934  0.00084  -0.03214 131 ILE A O   
892  C CB  . ILE A 124 ? 0.29471 0.25949 0.28395 -0.01758 0.00591  -0.02115 131 ILE A CB  
893  C CG1 . ILE A 124 ? 0.28494 0.24258 0.28435 -0.00613 0.00262  -0.01483 131 ILE A CG1 
894  C CG2 . ILE A 124 ? 0.28631 0.26450 0.26684 -0.03347 0.01554  -0.03119 131 ILE A CG2 
895  C CD1 . ILE A 124 ? 0.33408 0.26811 0.31416 -0.00906 -0.00074 -0.00780 131 ILE A CD1 
896  N N   . GLY A 125 ? 0.30228 0.31320 0.32772 -0.00044 0.00991  -0.05430 132 GLY A N   
897  C CA  . GLY A 125 ? 0.29649 0.31867 0.33601 0.01306  0.00710  -0.06449 132 GLY A CA  
898  C C   . GLY A 125 ? 0.31634 0.32245 0.35838 0.03042  -0.00449 -0.06744 132 GLY A C   
899  O O   . GLY A 125 ? 0.35371 0.35358 0.39896 0.04319  -0.01130 -0.06919 132 GLY A O   
900  N N   . GLN A 126 ? 0.31386 0.30796 0.34915 0.02986  -0.00851 -0.06793 133 GLN A N   
901  C CA  . GLN A 126 ? 0.37533 0.34065 0.40351 0.04160  -0.02155 -0.06877 133 GLN A CA  
902  C C   . GLN A 126 ? 0.34509 0.28346 0.36531 0.03606  -0.02476 -0.04875 133 GLN A C   
903  O O   . GLN A 126 ? 0.40686 0.31357 0.41309 0.04075  -0.03603 -0.04638 133 GLN A O   
904  C CB  . GLN A 126 ? 0.36767 0.32447 0.38794 0.03810  -0.02483 -0.07395 133 GLN A CB  
905  C CG  . GLN A 126 ? 0.48439 0.47338 0.51081 0.04331  -0.02115 -0.09760 133 GLN A CG  
906  C CD  . GLN A 126 ? 0.57623 0.55892 0.59286 0.03762  -0.02295 -0.10223 133 GLN A CD  
907  O OE1 . GLN A 126 ? 0.50949 0.45807 0.51494 0.03478  -0.03158 -0.09227 133 GLN A OE1 
908  N NE2 . GLN A 126 ? 0.54213 0.55996 0.56079 0.03254  -0.01426 -0.11814 133 GLN A NE2 
909  N N   . PHE A 127 ? 0.30981 0.25877 0.33493 0.02571  -0.01621 -0.03605 134 PHE A N   
910  C CA  . PHE A 127 ? 0.32488 0.26281 0.34603 0.01932  -0.01685 -0.02130 134 PHE A CA  
911  C C   . PHE A 127 ? 0.38343 0.32861 0.40869 0.02368  -0.01350 -0.01790 134 PHE A C   
912  O O   . PHE A 127 ? 0.33747 0.28381 0.36136 0.01836  -0.01139 -0.00834 134 PHE A O   
913  C CB  . PHE A 127 ? 0.30518 0.25357 0.32958 0.00833  -0.01322 -0.01372 134 PHE A CB  
914  C CG  . PHE A 127 ? 0.34944 0.29203 0.36864 0.00360  -0.01707 -0.01828 134 PHE A CG  
915  C CD1 . PHE A 127 ? 0.37481 0.29573 0.38302 -0.00276 -0.02444 -0.01729 134 PHE A CD1 
916  C CD2 . PHE A 127 ? 0.28129 0.23484 0.30057 0.00318  -0.01422 -0.02425 134 PHE A CD2 
917  C CE1 . PHE A 127 ? 0.32416 0.23660 0.32570 -0.00645 -0.02939 -0.02422 134 PHE A CE1 
918  C CE2 . PHE A 127 ? 0.33979 0.28933 0.35250 -0.00065 -0.01795 -0.03055 134 PHE A CE2 
919  C CZ  . PHE A 127 ? 0.38592 0.31594 0.39187 -0.00381 -0.02570 -0.03149 134 PHE A CZ  
920  N N   . GLY A 128 ? 0.29696 0.25141 0.32734 0.03293  -0.01330 -0.02820 135 GLY A N   
921  C CA  . GLY A 128 ? 0.30844 0.26711 0.34039 0.03759  -0.01243 -0.02651 135 GLY A CA  
922  C C   . GLY A 128 ? 0.29778 0.27063 0.33622 0.03210  -0.00391 -0.02307 135 GLY A C   
923  O O   . GLY A 128 ? 0.36191 0.33804 0.40084 0.03576  -0.00331 -0.02271 135 GLY A O   
924  N N   . VAL A 129 ? 0.24838 0.22423 0.28708 0.02462  0.00028  -0.02103 136 VAL A N   
925  C CA  . VAL A 129 ? 0.25838 0.23343 0.29462 0.02192  0.00331  -0.01720 136 VAL A CA  
926  C C   . VAL A 129 ? 0.28248 0.25614 0.31053 0.01218  0.00667  -0.02207 136 VAL A C   
927  O O   . VAL A 129 ? 0.28325 0.24164 0.29827 0.00754  0.00563  -0.01731 136 VAL A O   
928  C CB  . VAL A 129 ? 0.24789 0.22079 0.28349 0.02313  0.00074  -0.00938 136 VAL A CB  
929  C CG1 . VAL A 129 ? 0.30584 0.28873 0.34737 0.02656  0.00096  -0.00620 136 VAL A CG1 
930  C CG2 . VAL A 129 ? 0.29014 0.26207 0.32407 0.01816  -0.00167 -0.00776 136 VAL A CG2 
931  N N   . GLY A 130 ? 0.29238 0.25275 0.27930 -0.00282 0.01059  -0.02855 137 GLY A N   
932  C CA  . GLY A 130 ? 0.28617 0.24603 0.26763 0.00319  0.01165  -0.02772 137 GLY A CA  
933  C C   . GLY A 130 ? 0.30602 0.27483 0.29516 0.00533  0.01273  -0.02422 137 GLY A C   
934  O O   . GLY A 130 ? 0.28339 0.25273 0.27063 0.00825  0.01315  -0.02235 137 GLY A O   
935  N N   . PHE A 131 ? 0.28401 0.25858 0.28077 0.00412  0.01324  -0.02329 138 PHE A N   
936  C CA  . PHE A 131 ? 0.26846 0.24923 0.27234 0.00557  0.01273  -0.02270 138 PHE A CA  
937  C C   . PHE A 131 ? 0.25550 0.23729 0.26045 0.00654  0.01004  -0.02335 138 PHE A C   
938  O O   . PHE A 131 ? 0.27953 0.25878 0.28712 0.00807  0.01050  -0.02143 138 PHE A O   
939  C CB  . PHE A 131 ? 0.28964 0.27755 0.29802 0.00526  0.01216  -0.02391 138 PHE A CB  
940  C CG  . PHE A 131 ? 0.28579 0.27824 0.30007 0.00681  0.00983  -0.02665 138 PHE A CG  
941  C CD1 . PHE A 131 ? 0.30745 0.29959 0.32663 0.00695  0.00937  -0.02704 138 PHE A CD1 
942  C CD2 . PHE A 131 ? 0.28935 0.28625 0.30535 0.00821  0.00788  -0.02948 138 PHE A CD2 
943  C CE1 . PHE A 131 ? 0.28677 0.27908 0.31175 0.00721  0.00626  -0.03123 138 PHE A CE1 
944  C CE2 . PHE A 131 ? 0.28911 0.28582 0.30892 0.01097  0.00549  -0.03347 138 PHE A CE2 
945  C CZ  . PHE A 131 ? 0.34446 0.33699 0.36832 0.00985  0.00430  -0.03490 138 PHE A CZ  
946  N N   . TYR A 132 ? 0.26255 0.24833 0.26670 0.00568  0.00720  -0.02539 139 TYR A N   
947  C CA  . TYR A 132 ? 0.26968 0.25908 0.27568 0.00900  0.00402  -0.02573 139 TYR A CA  
948  C C   . TYR A 132 ? 0.27261 0.25538 0.27084 0.01242  0.00362  -0.02243 139 TYR A C   
949  O O   . TYR A 132 ? 0.28594 0.26854 0.28427 0.01705  0.00159  -0.02053 139 TYR A O   
950  C CB  . TYR A 132 ? 0.26492 0.26614 0.27513 0.00751  0.00078  -0.02860 139 TYR A CB  
951  C CG  . TYR A 132 ? 0.27599 0.28517 0.29292 0.00550  0.00328  -0.02959 139 TYR A CG  
952  C CD1 . TYR A 132 ? 0.27267 0.28740 0.29385 0.01058  0.00354  -0.03126 139 TYR A CD1 
953  C CD2 . TYR A 132 ? 0.27665 0.28588 0.29370 -0.00028 0.00585  -0.02861 139 TYR A CD2 
954  C CE1 . TYR A 132 ? 0.27402 0.29763 0.29786 0.01059  0.00641  -0.03215 139 TYR A CE1 
955  C CE2 . TYR A 132 ? 0.32193 0.33856 0.34242 -0.00089 0.00942  -0.02722 139 TYR A CE2 
956  C CZ  . TYR A 132 ? 0.32723 0.35273 0.35040 0.00485  0.00970  -0.02912 139 TYR A CZ  
957  O OH  . TYR A 132 ? 0.32658 0.36110 0.34999 0.00577  0.01366  -0.02768 139 TYR A OH  
958  N N   . SER A 133 ? 0.27415 0.25117 0.26419 0.01189  0.00608  -0.02111 140 SER A N   
959  C CA  . SER A 133 ? 0.27259 0.24459 0.25317 0.01644  0.00774  -0.01650 140 SER A CA  
960  C C   . SER A 133 ? 0.25788 0.22528 0.24420 0.01743  0.01200  -0.01007 140 SER A C   
961  O O   . SER A 133 ? 0.29561 0.25860 0.27553 0.02143  0.01419  -0.00356 140 SER A O   
962  C CB  . SER A 133 ? 0.31592 0.28362 0.28555 0.01728  0.01073  -0.01734 140 SER A CB  
963  O OG  . SER A 133 ? 0.30162 0.26790 0.27715 0.01592  0.01661  -0.01500 140 SER A OG  
964  N N   . ALA A 134 ? 0.27288 0.24102 0.27113 0.01366  0.01283  -0.01172 141 ALA A N   
965  C CA  . ALA A 134 ? 0.28819 0.25059 0.29489 0.01258  0.01486  -0.00775 141 ALA A CA  
966  C C   . ALA A 134 ? 0.30079 0.25601 0.30482 0.01722  0.01280  -0.00440 141 ALA A C   
967  O O   . ALA A 134 ? 0.30312 0.24872 0.30931 0.01727  0.01613  0.00269  141 ALA A O   
968  C CB  . ALA A 134 ? 0.28085 0.24624 0.29899 0.00884  0.01261  -0.01381 141 ALA A CB  
969  N N   . TYR A 135 ? 0.29087 0.25110 0.29147 0.02144  0.00761  -0.00853 142 TYR A N   
970  C CA  . TYR A 135 ? 0.29568 0.25050 0.29422 0.02846  0.00500  -0.00544 142 TYR A CA  
971  C C   . TYR A 135 ? 0.32504 0.27732 0.31016 0.03431  0.00580  0.00284  142 TYR A C   
972  O O   . TYR A 135 ? 0.34156 0.28966 0.32265 0.04213  0.00343  0.00717  142 TYR A O   
973  C CB  . TYR A 135 ? 0.26082 0.22692 0.26312 0.03204  -0.00045 -0.01263 142 TYR A CB  
974  C CG  . TYR A 135 ? 0.30405 0.26990 0.31603 0.02952  -0.00023 -0.01917 142 TYR A CG  
975  C CD1 . TYR A 135 ? 0.30477 0.25862 0.32079 0.03368  -0.00093 -0.02030 142 TYR A CD1 
976  C CD2 . TYR A 135 ? 0.27383 0.24918 0.28898 0.02376  0.00060  -0.02416 142 TYR A CD2 
977  C CE1 . TYR A 135 ? 0.31247 0.26551 0.33474 0.03221  -0.00172 -0.02841 142 TYR A CE1 
978  C CE2 . TYR A 135 ? 0.26756 0.24412 0.28837 0.02309  0.00040  -0.03025 142 TYR A CE2 
979  C CZ  . TYR A 135 ? 0.30059 0.26681 0.32437 0.02731  -0.00117 -0.03318 142 TYR A CZ  
980  O OH  . TYR A 135 ? 0.28634 0.25415 0.31307 0.02744  -0.00244 -0.04129 142 TYR A OH  
981  N N   . LEU A 136 ? 0.31673 0.27135 0.29339 0.03237  0.00919  0.00512  143 LEU A N   
982  C CA  . LEU A 136 ? 0.35047 0.30163 0.31205 0.03891  0.01173  0.01410  143 LEU A CA  
983  C C   . LEU A 136 ? 0.35986 0.29717 0.32490 0.03905  0.01876  0.02588  143 LEU A C   
984  O O   . LEU A 136 ? 0.38463 0.31571 0.33847 0.04657  0.02053  0.03605  143 LEU A O   
985  C CB  . LEU A 136 ? 0.31352 0.26954 0.26486 0.03767  0.01510  0.01265  143 LEU A CB  
986  C CG  . LEU A 136 ? 0.32817 0.29323 0.27311 0.03726  0.00814  0.00170  143 LEU A CG  
987  C CD1 . LEU A 136 ? 0.34675 0.31113 0.28319 0.03618  0.01249  -0.00086 143 LEU A CD1 
988  C CD2 . LEU A 136 ? 0.34505 0.31614 0.27743 0.04520  0.00031  0.00107  143 LEU A CD2 
989  N N   . VAL A 137 ? 0.32690 0.25947 0.30783 0.03038  0.02262  0.02499  144 VAL A N   
990  C CA  . VAL A 137 ? 0.31278 0.23263 0.30084 0.02695  0.02986  0.03601  144 VAL A CA  
991  C C   . VAL A 137 ? 0.34843 0.25605 0.35291 0.02180  0.02716  0.03207  144 VAL A C   
992  O O   . VAL A 137 ? 0.36689 0.25888 0.37771 0.01898  0.03172  0.04121  144 VAL A O   
993  C CB  . VAL A 137 ? 0.33213 0.25914 0.32534 0.02040  0.03857  0.04070  144 VAL A CB  
994  C CG1 . VAL A 137 ? 0.35617 0.29175 0.32933 0.02800  0.04264  0.04533  144 VAL A CG1 
995  C CG2 . VAL A 137 ? 0.31742 0.25466 0.32480 0.01270  0.03602  0.02938  144 VAL A CG2 
996  N N   . ALA A 138 ? 0.34704 0.26004 0.35775 0.02067  0.02038  0.01917  145 ALA A N   
997  C CA  . ALA A 138 ? 0.32454 0.22726 0.34895 0.01633  0.01719  0.01221  145 ALA A CA  
998  C C   . ALA A 138 ? 0.32959 0.22520 0.34964 0.02590  0.01142  0.00759  145 ALA A C   
999  O O   . ALA A 138 ? 0.37570 0.28509 0.38853 0.03244  0.00758  0.00313  145 ALA A O   
1000 C CB  . ALA A 138 ? 0.33934 0.25555 0.37226 0.00999  0.01434  0.00082  145 ALA A CB  
1001 N N   . GLU A 139 ? 0.33351 0.20807 0.35961 0.02643  0.01080  0.00808  146 GLU A N   
1002 C CA  . GLU A 139 ? 0.34809 0.21616 0.37127 0.03729  0.00529  0.00125  146 GLU A CA  
1003 C C   . GLU A 139 ? 0.43087 0.30688 0.46067 0.03538  0.00054  -0.01477 146 GLU A C   
1004 O O   . GLU A 139 ? 0.41018 0.29093 0.43668 0.04536  -0.00317 -0.02194 146 GLU A O   
1005 C CB  . GLU A 139 ? 0.45642 0.29413 0.48092 0.04116  0.00639  0.00764  146 GLU A CB  
1006 C CG  . GLU A 139 ? 0.57386 0.39245 0.61202 0.02808  0.00872  0.00750  146 GLU A CG  
1007 C CD  . GLU A 139 ? 0.94028 0.72339 0.98017 0.03087  0.01035  0.01510  146 GLU A CD  
1008 O OE1 . GLU A 139 ? 0.90973 0.67329 0.96215 0.02245  0.00805  0.00702  146 GLU A OE1 
1009 O OE2 . GLU A 139 ? 0.85144 0.62528 0.88000 0.04124  0.01358  0.02917  146 GLU A OE2 
1010 N N   . LYS A 140 ? 0.35934 0.23873 0.39812 0.02403  0.00072  -0.02010 147 LYS A N   
1011 C CA  . LYS A 140 ? 0.34360 0.23156 0.38593 0.02293  -0.00397 -0.03464 147 LYS A CA  
1012 C C   . LYS A 140 ? 0.33820 0.24253 0.38572 0.01274  -0.00260 -0.03483 147 LYS A C   
1013 O O   . LYS A 140 ? 0.30309 0.20400 0.35739 0.00456  0.00117  -0.02689 147 LYS A O   
1014 C CB  . LYS A 140 ? 0.35895 0.22445 0.40775 0.02201  -0.00811 -0.04393 147 LYS A CB  
1015 C CG  . LYS A 140 ? 0.38391 0.25841 0.43376 0.02162  -0.01371 -0.06013 147 LYS A CG  
1016 C CD  . LYS A 140 ? 0.41765 0.26513 0.47077 0.02333  -0.01866 -0.07060 147 LYS A CD  
1017 C CE  . LYS A 140 ? 0.55588 0.39990 0.62056 0.01050  -0.02372 -0.08008 147 LYS A CE  
1018 N NZ  . LYS A 140 ? 0.64101 0.45032 0.71121 0.00922  -0.02790 -0.08743 147 LYS A NZ  
1019 N N   . VAL A 141 ? 0.29798 0.22072 0.34217 0.01434  -0.00466 -0.04221 148 VAL A N   
1020 C CA  . VAL A 141 ? 0.28122 0.21848 0.32959 0.00703  -0.00417 -0.04299 148 VAL A CA  
1021 C C   . VAL A 141 ? 0.30910 0.25200 0.35869 0.00763  -0.00991 -0.05598 148 VAL A C   
1022 O O   . VAL A 141 ? 0.29710 0.24386 0.33887 0.01576  -0.01176 -0.06270 148 VAL A O   
1023 C CB  . VAL A 141 ? 0.25548 0.20824 0.29613 0.00889  -0.00077 -0.03762 148 VAL A CB  
1024 C CG1 . VAL A 141 ? 0.26956 0.23485 0.31360 0.00381  -0.00016 -0.03803 148 VAL A CG1 
1025 C CG2 . VAL A 141 ? 0.27251 0.22008 0.30871 0.00980  0.00356  -0.02678 148 VAL A CG2 
1026 N N   . THR A 142 ? 0.28581 0.23224 0.34519 -0.00026 -0.01272 -0.05950 149 THR A N   
1027 C CA  . THR A 142 ? 0.27561 0.23092 0.33474 0.00044  -0.01952 -0.07210 149 THR A CA  
1028 C C   . THR A 142 ? 0.33261 0.30839 0.39292 -0.00196 -0.01859 -0.06831 149 THR A C   
1029 O O   . THR A 142 ? 0.34503 0.32399 0.41555 -0.00866 -0.01563 -0.06076 149 THR A O   
1030 C CB  . THR A 142 ? 0.33644 0.27891 0.40832 -0.00704 -0.02616 -0.08134 149 THR A CB  
1031 O OG1 . THR A 142 ? 0.38833 0.30589 0.45994 -0.00493 -0.02597 -0.08254 149 THR A OG1 
1032 C CG2 . THR A 142 ? 0.32506 0.27749 0.39314 -0.00431 -0.03541 -0.09751 149 THR A CG2 
1033 N N   . VAL A 143 ? 0.27141 0.26093 0.32065 0.00477  -0.01992 -0.07201 150 VAL A N   
1034 C CA  . VAL A 143 ? 0.28151 0.28819 0.32910 0.00523  -0.01907 -0.06768 150 VAL A CA  
1035 C C   . VAL A 143 ? 0.33394 0.35196 0.37975 0.00777  -0.02755 -0.07898 150 VAL A C   
1036 O O   . VAL A 143 ? 0.32061 0.34025 0.35407 0.01517  -0.03000 -0.08661 150 VAL A O   
1037 C CB  . VAL A 143 ? 0.30666 0.31840 0.34157 0.01099  -0.01269 -0.05989 150 VAL A CB  
1038 C CG1 . VAL A 143 ? 0.31524 0.34050 0.34718 0.01289  -0.01188 -0.05498 150 VAL A CG1 
1039 C CG2 . VAL A 143 ? 0.29302 0.29504 0.32871 0.00870  -0.00645 -0.05102 150 VAL A CG2 
1040 N N   . ILE A 144 ? 0.26611 0.29416 0.32422 0.00243  -0.03238 -0.08068 151 ILE A N   
1041 C CA  . ILE A 144 ? 0.26424 0.30697 0.32054 0.00532  -0.04235 -0.09190 151 ILE A CA  
1042 C C   . ILE A 144 ? 0.27554 0.33682 0.32613 0.01125  -0.04033 -0.08342 151 ILE A C   
1043 O O   . ILE A 144 ? 0.27689 0.34150 0.33710 0.00797  -0.03519 -0.07323 151 ILE A O   
1044 C CB  . ILE A 144 ? 0.30924 0.35372 0.38671 -0.00537 -0.05106 -0.10069 151 ILE A CB  
1045 C CG1 . ILE A 144 ? 0.41612 0.43624 0.50347 -0.01367 -0.05031 -0.10397 151 ILE A CG1 
1046 C CG2 . ILE A 144 ? 0.36434 0.42471 0.43829 -0.00180 -0.06437 -0.11606 151 ILE A CG2 
1047 C CD1 . ILE A 144 ? 0.42292 0.42956 0.49648 -0.00722 -0.05436 -0.11593 151 ILE A CD1 
1048 N N   . THR A 145 ? 0.26341 0.33621 0.29753 0.02115  -0.04379 -0.08690 152 THR A N   
1049 C CA  . THR A 145 ? 0.30086 0.38659 0.32690 0.02846  -0.04025 -0.07597 152 THR A CA  
1050 C C   . THR A 145 ? 0.33010 0.43446 0.34418 0.03797  -0.04914 -0.08263 152 THR A C   
1051 O O   . THR A 145 ? 0.31253 0.41789 0.31629 0.04170  -0.05525 -0.09483 152 THR A O   
1052 C CB  . THR A 145 ? 0.28799 0.36311 0.30052 0.03235  -0.02869 -0.06413 152 THR A CB  
1053 O OG1 . THR A 145 ? 0.31723 0.39733 0.32500 0.03734  -0.02388 -0.05190 152 THR A OG1 
1054 C CG2 . THR A 145 ? 0.27342 0.34850 0.26773 0.03969  -0.02736 -0.06803 152 THR A CG2 
1055 N N   . LYS A 146 ? 0.27765 0.39705 0.29201 0.04349  -0.05009 -0.07480 153 LYS A N   
1056 C CA  . LYS A 146 ? 0.26473 0.40438 0.26580 0.05504  -0.05836 -0.07779 153 LYS A CA  
1057 C C   . LYS A 146 ? 0.31749 0.45999 0.30749 0.06500  -0.05066 -0.06060 153 LYS A C   
1058 O O   . LYS A 146 ? 0.30215 0.44705 0.30520 0.06377  -0.04818 -0.05279 153 LYS A O   
1059 C CB  . LYS A 146 ? 0.28198 0.44187 0.30153 0.05111  -0.07261 -0.08952 153 LYS A CB  
1060 C CG  . LYS A 146 ? 0.29970 0.48548 0.30681 0.06397  -0.08425 -0.09405 153 LYS A CG  
1061 C CD  . LYS A 146 ? 0.32606 0.51099 0.30767 0.07205  -0.08908 -0.10531 153 LYS A CD  
1062 C CE  . LYS A 146 ? 0.36302 0.57516 0.33029 0.08576  -0.10166 -0.11021 153 LYS A CE  
1063 N NZ  . LYS A 146 ? 0.35535 0.57437 0.30286 0.10132  -0.09385 -0.09046 153 LYS A NZ  
1064 N N   . HIS A 147 ? 0.33371 0.47580 0.29965 0.07557  -0.04647 -0.05443 154 HIS A N   
1065 C CA  . HIS A 147 ? 0.29858 0.44013 0.25089 0.08604  -0.03920 -0.03726 154 HIS A CA  
1066 C C   . HIS A 147 ? 0.33920 0.50325 0.27606 0.10048  -0.04862 -0.03866 154 HIS A C   
1067 O O   . HIS A 147 ? 0.37035 0.54619 0.29902 0.10306  -0.05762 -0.05231 154 HIS A O   
1068 C CB  . HIS A 147 ? 0.29670 0.42027 0.23478 0.08555  -0.02578 -0.02687 154 HIS A CB  
1069 C CG  . HIS A 147 ? 0.33905 0.45482 0.26438 0.09339  -0.01647 -0.00810 154 HIS A CG  
1070 N ND1 . HIS A 147 ? 0.38282 0.50963 0.28769 0.10783  -0.01732 0.00013  154 HIS A ND1 
1071 C CD2 . HIS A 147 ? 0.32864 0.42390 0.25756 0.08885  -0.00598 0.00413  154 HIS A CD2 
1072 C CE1 . HIS A 147 ? 0.41441 0.52603 0.31168 0.11147  -0.00695 0.01796  154 HIS A CE1 
1073 N NE2 . HIS A 147 ? 0.37192 0.46374 0.28397 0.09969  -0.00044 0.01964  154 HIS A NE2 
1074 N N   . ASN A 148 ? 0.33078 0.50156 0.26382 0.11098  -0.04806 -0.02609 155 ASN A N   
1075 C CA  . ASN A 148 ? 0.33035 0.52554 0.24870 0.12647  -0.05860 -0.02696 155 ASN A CA  
1076 C C   . ASN A 148 ? 0.43091 0.62903 0.31988 0.13580  -0.05726 -0.02700 155 ASN A C   
1077 O O   . ASN A 148 ? 0.42731 0.64823 0.30305 0.14666  -0.06946 -0.03563 155 ASN A O   
1078 C CB  . ASN A 148 ? 0.38231 0.57924 0.29516 0.13992  -0.05503 -0.00902 155 ASN A CB  
1079 C CG  . ASN A 148 ? 0.42176 0.62912 0.36120 0.13733  -0.06015 -0.01107 155 ASN A CG  
1080 O OD1 . ASN A 148 ? 0.41124 0.63616 0.37210 0.12864  -0.07092 -0.02637 155 ASN A OD1 
1081 N ND2 . ASN A 148 ? 0.41007 0.60557 0.34916 0.14474  -0.05146 0.00481  155 ASN A ND2 
1082 N N   . ASP A 149 ? 0.41281 0.59090 0.29083 0.13297  -0.04255 -0.01669 156 ASP A N   
1083 C CA  . ASP A 149 ? 0.46481 0.64690 0.31485 0.14291  -0.03726 -0.01229 156 ASP A CA  
1084 C C   . ASP A 149 ? 0.53103 0.71512 0.37958 0.13729  -0.03977 -0.03014 156 ASP A C   
1085 O O   . ASP A 149 ? 0.51712 0.70389 0.34423 0.14466  -0.03236 -0.02635 156 ASP A O   
1086 C CB  . ASP A 149 ? 0.46322 0.62481 0.30467 0.14226  -0.01869 0.01006  156 ASP A CB  
1087 C CG  . ASP A 149 ? 0.57439 0.72948 0.41028 0.15157  -0.01477 0.02959  156 ASP A CG  
1088 O OD1 . ASP A 149 ? 0.54219 0.71489 0.37338 0.16381  -0.02593 0.02802  156 ASP A OD1 
1089 O OD2 . ASP A 149 ? 0.54161 0.67352 0.37848 0.14683  -0.00100 0.04606  156 ASP A OD2 
1090 N N   . ASP A 150 ? 0.40587 0.58742 0.27646 0.12495  -0.04847 -0.04823 157 ASP A N   
1091 C CA  . ASP A 150 ? 0.38742 0.56529 0.25648 0.12056  -0.04981 -0.06455 157 ASP A CA  
1092 C C   . ASP A 150 ? 0.48175 0.66365 0.36943 0.11228  -0.06600 -0.08681 157 ASP A C   
1093 O O   . ASP A 150 ? 0.43467 0.62607 0.33769 0.10930  -0.07539 -0.08876 157 ASP A O   
1094 C CB  . ASP A 150 ? 0.41291 0.56989 0.29177 0.10983  -0.03517 -0.05706 157 ASP A CB  
1095 C CG  . ASP A 150 ? 0.49445 0.65181 0.36065 0.11358  -0.03072 -0.06526 157 ASP A CG  
1096 O OD1 . ASP A 150 ? 0.49089 0.66015 0.34257 0.12261  -0.04010 -0.08110 157 ASP A OD1 
1097 O OD2 . ASP A 150 ? 0.45891 0.60520 0.33068 0.10766  -0.01804 -0.05661 157 ASP A OD2 
1098 N N   . GLU A 151 ? 0.41081 0.58556 0.29819 0.10870  -0.06893 -0.10344 158 GLU A N   
1099 C CA  . GLU A 151 ? 0.43810 0.61152 0.34250 0.09966  -0.08366 -0.12522 158 GLU A CA  
1100 C C   . GLU A 151 ? 0.35363 0.50635 0.28645 0.08254  -0.07799 -0.12220 158 GLU A C   
1101 O O   . GLU A 151 ? 0.36614 0.50684 0.30227 0.07922  -0.06404 -0.10607 158 GLU A O   
1102 C CB  . GLU A 151 ? 0.51433 0.68633 0.40147 0.10639  -0.08974 -0.14531 158 GLU A CB  
1103 C CG  . GLU A 151 ? 0.61629 0.81120 0.47666 0.12256  -0.10131 -0.15586 158 GLU A CG  
1104 C CD  . GLU A 151 ? 1.00680 1.22401 0.87136 0.12549  -0.11183 -0.15102 158 GLU A CD  
1105 O OE1 . GLU A 151 ? 0.99039 1.22391 0.83030 0.14134  -0.10892 -0.13884 158 GLU A OE1 
1106 O OE2 . GLU A 151 ? 0.90164 1.12177 0.79401 0.11297  -0.12272 -0.15856 158 GLU A OE2 
1107 N N   . GLN A 152 ? 0.37545 0.52298 0.32827 0.07135  -0.08885 -0.13811 159 GLN A N   
1108 C CA  . GLN A 152 ? 0.32987 0.45873 0.30861 0.05581  -0.08366 -0.13435 159 GLN A CA  
1109 C C   . GLN A 152 ? 0.32902 0.43557 0.30285 0.05465  -0.07715 -0.13922 159 GLN A C   
1110 O O   . GLN A 152 ? 0.38991 0.49266 0.35335 0.05934  -0.08437 -0.15635 159 GLN A O   
1111 C CB  . GLN A 152 ? 0.35026 0.48335 0.35529 0.04306  -0.09660 -0.14647 159 GLN A CB  
1112 C CG  . GLN A 152 ? 0.33850 0.45466 0.37107 0.02706  -0.08925 -0.13839 159 GLN A CG  
1113 C CD  . GLN A 152 ? 0.38455 0.51303 0.44604 0.01451  -0.09935 -0.14441 159 GLN A CD  
1114 O OE1 . GLN A 152 ? 0.44948 0.60315 0.51507 0.01840  -0.10475 -0.14160 159 GLN A OE1 
1115 N NE2 . GLN A 152 ? 0.40597 0.51794 0.48791 0.00000  -0.10232 -0.15272 159 GLN A NE2 
1116 N N   . TYR A 153 ? 0.30728 0.40003 0.28798 0.04972  -0.06451 -0.12531 160 TYR A N   
1117 C CA  . TYR A 153 ? 0.31720 0.39284 0.29310 0.05099  -0.05743 -0.12704 160 TYR A CA  
1118 C C   . TYR A 153 ? 0.35356 0.41020 0.35061 0.03840  -0.05356 -0.12220 160 TYR A C   
1119 O O   . TYR A 153 ? 0.31636 0.37474 0.32765 0.03043  -0.05112 -0.11182 160 TYR A O   
1120 C CB  . TYR A 153 ? 0.34071 0.42191 0.30054 0.05973  -0.04457 -0.11295 160 TYR A CB  
1121 C CG  . TYR A 153 ? 0.39869 0.49492 0.33402 0.07418  -0.04565 -0.11836 160 TYR A CG  
1122 C CD1 . TYR A 153 ? 0.42594 0.51853 0.34975 0.08225  -0.04553 -0.13047 160 TYR A CD1 
1123 C CD2 . TYR A 153 ? 0.41162 0.52606 0.33333 0.08183  -0.04626 -0.11080 160 TYR A CD2 
1124 C CE1 . TYR A 153 ? 0.45607 0.56405 0.35509 0.09715  -0.04542 -0.13560 160 TYR A CE1 
1125 C CE2 . TYR A 153 ? 0.46559 0.59498 0.36137 0.09679  -0.04664 -0.11492 160 TYR A CE2 
1126 C CZ  . TYR A 153 ? 0.49933 0.62582 0.38413 0.10393  -0.04605 -0.12771 160 TYR A CZ  
1127 O OH  . TYR A 153 ? 0.59023 0.73193 0.44825 0.11980  -0.04485 -0.13196 160 TYR A OH  
1128 N N   . ALA A 154 ? 0.34205 0.38114 0.33891 0.03884  -0.05189 -0.12851 161 ALA A N   
1129 C CA  . ALA A 154 ? 0.28010 0.29998 0.29219 0.03004  -0.04700 -0.12219 161 ALA A CA  
1130 C C   . ALA A 154 ? 0.28877 0.30445 0.29186 0.03708  -0.03716 -0.11487 161 ALA A C   
1131 O O   . ALA A 154 ? 0.33996 0.35539 0.33071 0.04724  -0.03730 -0.12358 161 ALA A O   
1132 C CB  . ALA A 154 ? 0.34422 0.34424 0.36676 0.02421  -0.05521 -0.13631 161 ALA A CB  
1133 N N   . TRP A 155 ? 0.29588 0.30973 0.30563 0.03219  -0.02930 -0.10023 162 TRP A N   
1134 C CA  . TRP A 155 ? 0.31819 0.32803 0.32548 0.03579  -0.02151 -0.09309 162 TRP A CA  
1135 C C   . TRP A 155 ? 0.33784 0.32770 0.35641 0.03050  -0.02174 -0.09174 162 TRP A C   
1136 O O   . TRP A 155 ? 0.31050 0.29294 0.34030 0.02124  -0.02336 -0.08845 162 TRP A O   
1137 C CB  . TRP A 155 ? 0.29644 0.31738 0.30219 0.03375  -0.01396 -0.07871 162 TRP A CB  
1138 C CG  . TRP A 155 ? 0.27865 0.29990 0.28522 0.03430  -0.00686 -0.07005 162 TRP A CG  
1139 C CD1 . TRP A 155 ? 0.26325 0.29793 0.26364 0.03903  -0.00104 -0.06573 162 TRP A CD1 
1140 C CD2 . TRP A 155 ? 0.28220 0.29260 0.29676 0.02971  -0.00523 -0.06442 162 TRP A CD2 
1141 N NE1 . TRP A 155 ? 0.26800 0.30187 0.27447 0.03639  0.00281  -0.05909 162 TRP A NE1 
1142 C CE2 . TRP A 155 ? 0.27664 0.29572 0.28997 0.03170  -0.00010 -0.05845 162 TRP A CE2 
1143 C CE3 . TRP A 155 ? 0.28441 0.28017 0.30707 0.02389  -0.00722 -0.06277 162 TRP A CE3 
1144 C CZ2 . TRP A 155 ? 0.29961 0.31388 0.31797 0.02936  0.00116  -0.05298 162 TRP A CZ2 
1145 C CZ3 . TRP A 155 ? 0.26630 0.25606 0.29142 0.02258  -0.00427 -0.05538 162 TRP A CZ3 
1146 C CH2 . TRP A 155 ? 0.28398 0.28326 0.30625 0.02569  -0.00106 -0.05141 162 TRP A CH2 
1147 N N   . GLU A 156 ? 0.28950 0.27226 0.30535 0.03719  -0.01922 -0.09254 163 GLU A N   
1148 C CA  . GLU A 156 ? 0.30707 0.27015 0.33126 0.03402  -0.01896 -0.08881 163 GLU A CA  
1149 C C   . GLU A 156 ? 0.28836 0.25360 0.30950 0.04188  -0.01413 -0.08297 163 GLU A C   
1150 O O   . GLU A 156 ? 0.31401 0.29016 0.32841 0.05183  -0.01268 -0.08769 163 GLU A O   
1151 C CB  . GLU A 156 ? 0.35586 0.29840 0.38296 0.03448  -0.02552 -0.10105 163 GLU A CB  
1152 C CG  . GLU A 156 ? 0.42741 0.34589 0.46453 0.02871  -0.02527 -0.09562 163 GLU A CG  
1153 C CD  . GLU A 156 ? 0.60478 0.50138 0.64777 0.02493  -0.03273 -0.10865 163 GLU A CD  
1154 O OE1 . GLU A 156 ? 0.53594 0.42017 0.57129 0.03522  -0.03595 -0.12033 163 GLU A OE1 
1155 O OE2 . GLU A 156 ? 0.59084 0.48291 0.64710 0.01161  -0.03548 -0.10785 163 GLU A OE2 
1156 N N   . SER A 157 ? 0.29257 0.24952 0.31883 0.03816  -0.01176 -0.07277 164 SER A N   
1157 C CA  . SER A 157 ? 0.28812 0.24731 0.31265 0.04657  -0.00941 -0.06835 164 SER A CA  
1158 C C   . SER A 157 ? 0.30073 0.24169 0.32844 0.04530  -0.00927 -0.06014 164 SER A C   
1159 O O   . SER A 157 ? 0.29809 0.23399 0.32883 0.03621  -0.00777 -0.05256 164 SER A O   
1160 C CB  . SER A 157 ? 0.30103 0.28312 0.32454 0.04572  -0.00549 -0.06165 164 SER A CB  
1161 O OG  . SER A 157 ? 0.31477 0.30292 0.33943 0.05385  -0.00480 -0.05862 164 SER A OG  
1162 N N   . SER A 158 ? 0.31721 0.25001 0.34320 0.05621  -0.01007 -0.06065 165 SER A N   
1163 C CA  . SER A 158 ? 0.34040 0.25946 0.36620 0.05879  -0.00941 -0.05038 165 SER A CA  
1164 C C   . SER A 158 ? 0.34841 0.28789 0.37202 0.06624  -0.00884 -0.04478 165 SER A C   
1165 O O   . SER A 158 ? 0.41316 0.34545 0.43452 0.07500  -0.00982 -0.03872 165 SER A O   
1166 C CB  . SER A 158 ? 0.37999 0.27149 0.40540 0.06699  -0.01151 -0.05364 165 SER A CB  
1167 O OG  . SER A 158 ? 0.42517 0.29478 0.45542 0.05766  -0.01315 -0.05881 165 SER A OG  
1168 N N   . ALA A 159 ? 0.31555 0.28008 0.34046 0.06232  -0.00762 -0.04620 166 ALA A N   
1169 C CA  . ALA A 159 ? 0.36521 0.35405 0.39221 0.06658  -0.00786 -0.04317 166 ALA A CA  
1170 C C   . ALA A 159 ? 0.34775 0.34296 0.37688 0.08184  -0.00887 -0.04782 166 ALA A C   
1171 O O   . ALA A 159 ? 0.40141 0.39211 0.42944 0.08733  -0.00798 -0.05641 166 ALA A O   
1172 C CB  . ALA A 159 ? 0.37192 0.35869 0.39585 0.06371  -0.00926 -0.03399 166 ALA A CB  
1173 N N   . GLY A 160 ? 0.40228 0.41089 0.43419 0.09042  -0.01106 -0.04351 167 GLY A N   
1174 C CA  . GLY A 160 ? 0.41836 0.43813 0.45402 0.10634  -0.01118 -0.04831 167 GLY A CA  
1175 C C   . GLY A 160 ? 0.40460 0.45363 0.44712 0.10652  -0.00719 -0.05419 167 GLY A C   
1176 O O   . GLY A 160 ? 0.37645 0.43596 0.42138 0.12080  -0.00564 -0.05940 167 GLY A O   
1177 N N   . GLY A 161 ? 0.31582 0.37881 0.36132 0.09218  -0.00471 -0.05246 168 GLY A N   
1178 C CA  . GLY A 161 ? 0.30585 0.39822 0.35864 0.09164  0.00044  -0.05457 168 GLY A CA  
1179 C C   . GLY A 161 ? 0.27252 0.36027 0.31772 0.09107  0.00506  -0.06069 168 GLY A C   
1180 O O   . GLY A 161 ? 0.28294 0.39528 0.33213 0.09074  0.01094  -0.06048 168 GLY A O   
1181 N N   . SER A 162 ? 0.26947 0.32857 0.30432 0.09085  0.00259  -0.06581 169 SER A N   
1182 C CA  . SER A 162 ? 0.27596 0.33345 0.30236 0.09215  0.00505  -0.07356 169 SER A CA  
1183 C C   . SER A 162 ? 0.29665 0.33081 0.31699 0.08120  0.00159  -0.07494 169 SER A C   
1184 O O   . SER A 162 ? 0.30996 0.32449 0.33203 0.07549  -0.00203 -0.07139 169 SER A O   
1185 C CB  . SER A 162 ? 0.35875 0.41034 0.37887 0.10939  0.00469  -0.08476 169 SER A CB  
1186 O OG  . SER A 162 ? 0.34656 0.36460 0.36329 0.11186  -0.00132 -0.08895 169 SER A OG  
1187 N N   . PHE A 163 ? 0.28255 0.32207 0.29592 0.07935  0.00316  -0.07943 170 PHE A N   
1188 C CA  . PHE A 163 ? 0.25296 0.27598 0.26183 0.07073  -0.00090 -0.08249 170 PHE A CA  
1189 C C   . PHE A 163 ? 0.27715 0.30156 0.27514 0.07864  -0.00248 -0.09473 170 PHE A C   
1190 O O   . PHE A 163 ? 0.32037 0.36201 0.31252 0.08962  0.00184  -0.09822 170 PHE A O   
1191 C CB  . PHE A 163 ? 0.27662 0.30734 0.28736 0.05803  0.00138  -0.07286 170 PHE A CB  
1192 C CG  . PHE A 163 ? 0.26638 0.32002 0.27314 0.05873  0.00750  -0.06889 170 PHE A CG  
1193 C CD1 . PHE A 163 ? 0.26830 0.32625 0.26487 0.06044  0.00746  -0.07252 170 PHE A CD1 
1194 C CD2 . PHE A 163 ? 0.30056 0.37175 0.31471 0.05673  0.01313  -0.06034 170 PHE A CD2 
1195 C CE1 . PHE A 163 ? 0.27941 0.35697 0.27096 0.06153  0.01448  -0.06590 170 PHE A CE1 
1196 C CE2 . PHE A 163 ? 0.29126 0.38220 0.30382 0.05544  0.02028  -0.05423 170 PHE A CE2 
1197 C CZ  . PHE A 163 ? 0.30795 0.40071 0.30794 0.05822  0.02164  -0.05596 170 PHE A CZ  
1198 N N   . THR A 164 ? 0.29481 0.30253 0.29027 0.07340  -0.00899 -0.10195 171 THR A N   
1199 C CA  . THR A 164 ? 0.29502 0.30376 0.27874 0.08042  -0.01295 -0.11579 171 THR A CA  
1200 C C   . THR A 164 ? 0.28944 0.30540 0.27035 0.07190  -0.01567 -0.11427 171 THR A C   
1201 O O   . THR A 164 ? 0.31169 0.32342 0.30203 0.05998  -0.01621 -0.10537 171 THR A O   
1202 C CB  . THR A 164 ? 0.36202 0.34362 0.34515 0.08414  -0.02106 -0.13085 171 THR A CB  
1203 O OG1 . THR A 164 ? 0.37575 0.33892 0.37047 0.06989  -0.02593 -0.12773 171 THR A OG1 
1204 C CG2 . THR A 164 ? 0.36806 0.33880 0.35236 0.09573  -0.01894 -0.13287 171 THR A CG2 
1205 N N   . VAL A 165 ? 0.32141 0.35034 0.28803 0.08005  -0.01683 -0.12234 172 VAL A N   
1206 C CA  . VAL A 165 ? 0.34671 0.38379 0.30807 0.07550  -0.02133 -0.12290 172 VAL A CA  
1207 C C   . VAL A 165 ? 0.38372 0.41772 0.33261 0.08349  -0.03081 -0.14247 172 VAL A C   
1208 O O   . VAL A 165 ? 0.37734 0.41561 0.31259 0.09726  -0.02915 -0.15190 172 VAL A O   
1209 C CB  . VAL A 165 ? 0.35236 0.41253 0.30544 0.07782  -0.01263 -0.10942 172 VAL A CB  
1210 C CG1 . VAL A 165 ? 0.34893 0.41726 0.29463 0.07611  -0.01799 -0.10945 172 VAL A CG1 
1211 C CG2 . VAL A 165 ? 0.35154 0.41179 0.31733 0.06862  -0.00520 -0.09299 172 VAL A CG2 
1212 N N   . ARG A 166 ? 0.38218 0.41021 0.33614 0.07530  -0.04118 -0.14970 173 ARG A N   
1213 C CA  . ARG A 166 ? 0.38541 0.41170 0.32841 0.08104  -0.05276 -0.17019 173 ARG A CA  
1214 C C   . ARG A 166 ? 0.37241 0.41158 0.31795 0.07404  -0.06113 -0.17046 173 ARG A C   
1215 O O   . ARG A 166 ? 0.37065 0.41154 0.33184 0.06262  -0.05898 -0.15711 173 ARG A O   
1216 C CB  . ARG A 166 ? 0.44490 0.44204 0.39709 0.07741  -0.06123 -0.18638 173 ARG A CB  
1217 C CG  . ARG A 166 ? 0.47234 0.45276 0.44975 0.05874  -0.06534 -0.18131 173 ARG A CG  
1218 C CD  . ARG A 166 ? 0.60042 0.54837 0.58568 0.05663  -0.06954 -0.19234 173 ARG A CD  
1219 N NE  . ARG A 166 ? 0.67576 0.61492 0.66306 0.06121  -0.05833 -0.17895 173 ARG A NE  
1220 C CZ  . ARG A 166 ? 0.77106 0.68234 0.76317 0.06324  -0.05803 -0.18207 173 ARG A CZ  
1221 N NH1 . ARG A 166 ? 0.73713 0.62146 0.73305 0.06002  -0.06756 -0.19836 173 ARG A NH1 
1222 N NH2 . ARG A 166 ? 0.63646 0.54662 0.62899 0.06958  -0.04848 -0.16912 173 ARG A NH2 
1223 N N   . THR A 167 ? 0.39921 0.44862 0.32855 0.08247  -0.07101 -0.18638 174 THR A N   
1224 C CA  . THR A 167 ? 0.40083 0.46218 0.33604 0.07564  -0.08278 -0.19067 174 THR A CA  
1225 C C   . THR A 167 ? 0.49093 0.53400 0.45365 0.05822  -0.09122 -0.19704 174 THR A C   
1226 O O   . THR A 167 ? 0.53873 0.55759 0.50740 0.05511  -0.09464 -0.20913 174 THR A O   
1227 C CB  . THR A 167 ? 0.53916 0.61440 0.45104 0.08844  -0.09428 -0.20966 174 THR A CB  
1228 O OG1 . THR A 167 ? 0.57482 0.66900 0.46147 0.10432  -0.08388 -0.19944 174 THR A OG1 
1229 C CG2 . THR A 167 ? 0.58896 0.68116 0.50841 0.08225  -0.10698 -0.21281 174 THR A CG2 
1230 N N   . ASP A 168 ? 0.40730 0.46187 0.38746 0.04725  -0.09399 -0.18816 175 ASP A N   
1231 C CA  . ASP A 168 ? 0.44404 0.48563 0.45281 0.02973  -0.09999 -0.19140 175 ASP A CA  
1232 C C   . ASP A 168 ? 0.55811 0.61149 0.57351 0.02501  -0.11794 -0.21036 175 ASP A C   
1233 O O   . ASP A 168 ? 0.59955 0.68053 0.61179 0.02867  -0.12311 -0.20794 175 ASP A O   
1234 C CB  . ASP A 168 ? 0.39765 0.44641 0.42427 0.02058  -0.09085 -0.16987 175 ASP A CB  
1235 C CG  . ASP A 168 ? 0.62924 0.66567 0.68604 0.00260  -0.09351 -0.16967 175 ASP A CG  
1236 O OD1 . ASP A 168 ? 0.66368 0.67355 0.72693 -0.00302 -0.09406 -0.17658 175 ASP A OD1 
1237 O OD2 . ASP A 168 ? 0.51845 0.57257 0.59277 -0.00526 -0.09526 -0.16282 175 ASP A OD2 
1238 N N   . THR A 169 ? 0.65693 0.68874 0.68189 0.01712  -0.12786 -0.22918 176 THR A N   
1239 C CA  . THR A 169 ? 0.95349 0.99084 0.99067 0.00823  -0.14210 -0.24235 176 THR A CA  
1240 C C   . THR A 169 ? 0.75297 0.79261 0.82740 -0.01316 -0.14521 -0.23712 176 THR A C   
1241 O O   . THR A 169 ? 0.68913 0.73747 0.77774 -0.02264 -0.15627 -0.24562 176 THR A O   
1242 C CB  . THR A 169 ? 0.89601 0.90502 0.92484 0.00965  -0.14590 -0.25699 176 THR A CB  
1243 O OG1 . THR A 169 ? 0.88706 0.86272 0.92623 0.00302  -0.13721 -0.25171 176 THR A OG1 
1244 C CG2 . THR A 169 ? 0.81696 0.83223 0.81047 0.03148  -0.14471 -0.26391 176 THR A CG2 
1245 N N   . GLY A 170 ? 0.76134 0.79449 0.85144 -0.02054 -0.13389 -0.22092 177 GLY A N   
1246 C CA  . GLY A 170 ? 0.72459 0.76205 0.84985 -0.03958 -0.13259 -0.21124 177 GLY A CA  
1247 C C   . GLY A 170 ? 0.61466 0.69167 0.75435 -0.04246 -0.13947 -0.20838 177 GLY A C   
1248 O O   . GLY A 170 ? 0.65164 0.75263 0.77412 -0.03025 -0.14859 -0.21652 177 GLY A O   
1249 N N   . GLU A 171 ? 0.67743 0.76247 0.84889 -0.05766 -0.13480 -0.19619 178 GLU A N   
1250 C CA  . GLU A 171 ? 0.65561 0.78001 0.84608 -0.06044 -0.13929 -0.19085 178 GLU A CA  
1251 C C   . GLU A 171 ? 0.55829 0.70401 0.72279 -0.04025 -0.13388 -0.17950 178 GLU A C   
1252 O O   . GLU A 171 ? 0.47129 0.60589 0.62326 -0.03336 -0.11787 -0.16174 178 GLU A O   
1253 C CB  . GLU A 171 ? 0.67559 0.80122 0.89854 -0.07590 -0.12764 -0.17329 178 GLU A CB  
1254 C CG  . GLU A 171 ? 0.63879 0.80443 0.89293 -0.08410 -0.13423 -0.17171 178 GLU A CG  
1255 C CD  . GLU A 171 ? 0.73124 0.90311 0.99727 -0.09435 -0.15167 -0.19047 178 GLU A CD  
1256 O OE1 . GLU A 171 ? 0.53259 0.67772 0.81210 -0.11062 -0.15091 -0.19330 178 GLU A OE1 
1257 O OE2 . GLU A 171 ? 0.68782 0.88642 0.94300 -0.08420 -0.16364 -0.19870 178 GLU A OE2 
1258 N N   . PRO A 172 ? 0.51450 0.68913 0.66956 -0.03026 -0.14685 -0.18885 179 PRO A N   
1259 C CA  . PRO A 172 ? 0.50340 0.69583 0.63409 -0.01091 -0.14062 -0.17527 179 PRO A CA  
1260 C C   . PRO A 172 ? 0.51376 0.71829 0.66082 -0.01211 -0.12779 -0.15336 179 PRO A C   
1261 O O   . PRO A 172 ? 0.59780 0.81913 0.77784 -0.02454 -0.13015 -0.15169 179 PRO A O   
1262 C CB  . PRO A 172 ? 0.54552 0.77015 0.66986 -0.00230 -0.15937 -0.18978 179 PRO A CB  
1263 C CG  . PRO A 172 ? 0.56326 0.78242 0.70529 -0.01732 -0.17329 -0.20980 179 PRO A CG  
1264 C CD  . PRO A 172 ? 0.60661 0.79236 0.76691 -0.03468 -0.16623 -0.21078 179 PRO A CD  
1265 N N   . MET A 173 ? 0.40141 0.59840 0.52557 0.00120  -0.11406 -0.13685 180 MET A N   
1266 C CA  . MET A 173 ? 0.39433 0.59437 0.52949 0.00108  -0.10028 -0.11729 180 MET A CA  
1267 C C   . MET A 173 ? 0.49233 0.71966 0.62267 0.01547  -0.10086 -0.10753 180 MET A C   
1268 O O   . MET A 173 ? 0.59508 0.82862 0.73788 0.01598  -0.09128 -0.09377 180 MET A O   
1269 C CB  . MET A 173 ? 0.39327 0.56385 0.50989 0.00463  -0.08376 -0.10440 180 MET A CB  
1270 C CG  . MET A 173 ? 0.57198 0.71414 0.69309 -0.00675 -0.07876 -0.10741 180 MET A CG  
1271 S SD  . MET A 173 ? 0.52250 0.64008 0.61510 0.00314  -0.06370 -0.09479 180 MET A SD  
1272 C CE  . MET A 173 ? 0.43568 0.56460 0.53067 0.00908  -0.05343 -0.07653 180 MET A CE  
1273 N N   . GLY A 174 ? 0.41707 0.65702 0.52534 0.02958  -0.10956 -0.11228 181 GLY A N   
1274 C CA  . GLY A 174 ? 0.30367 0.56645 0.40517 0.04536  -0.10956 -0.10100 181 GLY A CA  
1275 C C   . GLY A 174 ? 0.36050 0.60204 0.43298 0.05812  -0.09503 -0.08486 181 GLY A C   
1276 O O   . GLY A 174 ? 0.37478 0.61734 0.41953 0.07194  -0.09708 -0.08335 181 GLY A O   
1277 N N   . ARG A 175 ? 0.27936 0.50134 0.35791 0.05295  -0.08029 -0.07293 182 ARG A N   
1278 C CA  . ARG A 175 ? 0.25152 0.44959 0.30640 0.06100  -0.06658 -0.05916 182 ARG A CA  
1279 C C   . ARG A 175 ? 0.24645 0.42399 0.31299 0.05070  -0.05400 -0.05239 182 ARG A C   
1280 O O   . ARG A 175 ? 0.28852 0.47690 0.37816 0.04523  -0.05275 -0.05058 182 ARG A O   
1281 C CB  . ARG A 175 ? 0.28279 0.49138 0.32530 0.07850  -0.06445 -0.04598 182 ARG A CB  
1282 C CG  . ARG A 175 ? 0.27576 0.45586 0.29452 0.08516  -0.05010 -0.03134 182 ARG A CG  
1283 C CD  . ARG A 175 ? 0.29422 0.47748 0.30787 0.09997  -0.04563 -0.01703 182 ARG A CD  
1284 N NE  . ARG A 175 ? 0.29564 0.48416 0.33250 0.09635  -0.04204 -0.01522 182 ARG A NE  
1285 C CZ  . ARG A 175 ? 0.26268 0.47990 0.31665 0.10298  -0.04854 -0.01558 182 ARG A CZ  
1286 N NH1 . ARG A 175 ? 0.26968 0.51389 0.32065 0.11373  -0.06093 -0.01844 182 ARG A NH1 
1287 N NH2 . ARG A 175 ? 0.26557 0.48774 0.34016 0.10018  -0.04255 -0.01273 182 ARG A NH2 
1288 N N   . GLY A 176 ? 0.29760 0.42369 0.21702 0.07770  -0.04214 -0.02001 183 GLY A N   
1289 C CA  . GLY A 176 ? 0.28307 0.39751 0.23188 0.06560  -0.03665 -0.01841 183 GLY A CA  
1290 C C   . GLY A 176 ? 0.31904 0.41829 0.27245 0.05737  -0.03034 -0.02656 183 GLY A C   
1291 O O   . GLY A 176 ? 0.32264 0.41712 0.25700 0.06377  -0.02469 -0.02909 183 GLY A O   
1292 N N   . THR A 177 ? 0.27258 0.36475 0.24972 0.04537  -0.03059 -0.02972 184 THR A N   
1293 C CA  . THR A 177 ? 0.25752 0.33642 0.24194 0.03974  -0.02430 -0.03418 184 THR A CA  
1294 C C   . THR A 177 ? 0.33989 0.41419 0.33854 0.02736  -0.03213 -0.04518 184 THR A C   
1295 O O   . THR A 177 ? 0.29232 0.37241 0.30506 0.02110  -0.03742 -0.04408 184 THR A O   
1296 C CB  . THR A 177 ? 0.28971 0.36283 0.28905 0.03941  -0.01193 -0.02031 184 THR A CB  
1297 O OG1 . THR A 177 ? 0.31677 0.39241 0.30238 0.04991  -0.00233 -0.00902 184 THR A OG1 
1298 C CG2 . THR A 177 ? 0.30090 0.36674 0.31309 0.03448  -0.00684 -0.02315 184 THR A CG2 
1299 N N   . LYS A 178 ? 0.28685 0.34916 0.28072 0.02507  -0.03121 -0.05486 185 LYS A N   
1300 C CA  . LYS A 178 ? 0.28782 0.34006 0.29378 0.01376  -0.03572 -0.06300 185 LYS A CA  
1301 C C   . LYS A 178 ? 0.29915 0.33846 0.31247 0.01547  -0.02706 -0.05957 185 LYS A C   
1302 O O   . LYS A 178 ? 0.31753 0.35045 0.31884 0.02409  -0.02072 -0.06162 185 LYS A O   
1303 C CB  . LYS A 178 ? 0.36825 0.41412 0.35883 0.00957  -0.04383 -0.07922 185 LYS A CB  
1304 C CG  . LYS A 178 ? 0.47291 0.50431 0.47153 -0.00280 -0.04755 -0.08828 185 LYS A CG  
1305 C CD  . LYS A 178 ? 0.51469 0.54404 0.50074 -0.01157 -0.05858 -0.10523 185 LYS A CD  
1306 C CE  . LYS A 178 ? 0.59717 0.65115 0.57233 -0.00649 -0.06704 -0.10635 185 LYS A CE  
1307 N NZ  . LYS A 178 ? 0.78968 0.84676 0.75236 -0.01610 -0.08082 -0.12443 185 LYS A NZ  
1308 N N   . VAL A 179 ? 0.27145 0.30933 0.30316 0.00928  -0.02654 -0.05375 186 VAL A N   
1309 C CA  . VAL A 179 ? 0.23678 0.26702 0.27724 0.01138  -0.02079 -0.04980 186 VAL A CA  
1310 C C   . VAL A 179 ? 0.31634 0.33056 0.35716 0.00528  -0.02434 -0.05685 186 VAL A C   
1311 O O   . VAL A 179 ? 0.31032 0.32448 0.35910 -0.00390 -0.02890 -0.05661 186 VAL A O   
1312 C CB  . VAL A 179 ? 0.23711 0.27596 0.29478 0.00847  -0.01906 -0.03895 186 VAL A CB  
1313 C CG1 . VAL A 179 ? 0.25078 0.28760 0.31913 0.01062  -0.01608 -0.03515 186 VAL A CG1 
1314 C CG2 . VAL A 179 ? 0.26152 0.31132 0.31956 0.01275  -0.01362 -0.03065 186 VAL A CG2 
1315 N N   . ILE A 180 ? 0.28754 0.28649 0.31917 0.01133  -0.02051 -0.06199 187 ILE A N   
1316 C CA  . ILE A 180 ? 0.29888 0.27504 0.32683 0.00660  -0.02188 -0.06847 187 ILE A CA  
1317 C C   . ILE A 180 ? 0.27744 0.24880 0.31462 0.01362  -0.01696 -0.05950 187 ILE A C   
1318 O O   . ILE A 180 ? 0.30053 0.27241 0.33593 0.02644  -0.01044 -0.05690 187 ILE A O   
1319 C CB  . ILE A 180 ? 0.33722 0.29261 0.34418 0.00922  -0.02116 -0.08218 187 ILE A CB  
1320 C CG1 . ILE A 180 ? 0.31528 0.28099 0.31193 0.00292  -0.02872 -0.09161 187 ILE A CG1 
1321 C CG2 . ILE A 180 ? 0.34563 0.27058 0.34932 0.00235  -0.02114 -0.08787 187 ILE A CG2 
1322 C CD1 . ILE A 180 ? 0.38012 0.32762 0.35126 0.00673  -0.02902 -0.10677 187 ILE A CD1 
1323 N N   . LEU A 181 ? 0.27331 0.24307 0.32018 0.00667  -0.01989 -0.05404 188 LEU A N   
1324 C CA  . LEU A 181 ? 0.23421 0.20223 0.28840 0.01356  -0.01780 -0.04486 188 LEU A CA  
1325 C C   . LEU A 181 ? 0.29810 0.23575 0.34173 0.01578  -0.01489 -0.04745 188 LEU A C   
1326 O O   . LEU A 181 ? 0.32697 0.25044 0.36780 0.00462  -0.01673 -0.04943 188 LEU A O   
1327 C CB  . LEU A 181 ? 0.27666 0.25762 0.34169 0.00620  -0.02257 -0.03754 188 LEU A CB  
1328 C CG  . LEU A 181 ? 0.28756 0.29046 0.36083 0.00216  -0.02485 -0.03572 188 LEU A CG  
1329 C CD1 . LEU A 181 ? 0.28729 0.29412 0.36534 -0.00501 -0.02910 -0.03128 188 LEU A CD1 
1330 C CD2 . LEU A 181 ? 0.28703 0.30558 0.36886 0.01029  -0.02176 -0.03068 188 LEU A CD2 
1331 N N   . HIS A 182 ? 0.31420 0.24124 0.35273 0.03088  -0.00887 -0.04613 189 HIS A N   
1332 C CA  . HIS A 182 ? 0.34657 0.23950 0.37349 0.03671  -0.00426 -0.04638 189 HIS A CA  
1333 C C   . HIS A 182 ? 0.35895 0.25899 0.39514 0.04275  -0.00570 -0.03208 189 HIS A C   
1334 O O   . HIS A 182 ? 0.35340 0.27281 0.39932 0.05666  -0.00500 -0.02388 189 HIS A O   
1335 C CB  . HIS A 182 ? 0.35007 0.22632 0.36438 0.05329  0.00396  -0.05193 189 HIS A CB  
1336 C CG  . HIS A 182 ? 0.39860 0.27255 0.40020 0.04922  0.00426  -0.06618 189 HIS A CG  
1337 N ND1 . HIS A 182 ? 0.52673 0.36621 0.50784 0.04269  0.00479  -0.08102 189 HIS A ND1 
1338 C CD2 . HIS A 182 ? 0.38670 0.28831 0.39147 0.04979  0.00331  -0.06780 189 HIS A CD2 
1339 C CE1 . HIS A 182 ? 0.51360 0.36211 0.48437 0.04105  0.00294  -0.09187 189 HIS A CE1 
1340 N NE2 . HIS A 182 ? 0.45189 0.33734 0.43597 0.04641  0.00292  -0.08295 189 HIS A NE2 
1341 N N   . LEU A 183 ? 0.34597 0.23613 0.38053 0.03172  -0.00839 -0.02861 190 LEU A N   
1342 C CA  . LEU A 183 ? 0.34749 0.25063 0.38809 0.03522  -0.01217 -0.01577 190 LEU A CA  
1343 C C   . LEU A 183 ? 0.36117 0.24798 0.39539 0.05320  -0.00820 -0.00583 190 LEU A C   
1344 O O   . LEU A 183 ? 0.41153 0.26339 0.43262 0.05909  -0.00068 -0.00803 190 LEU A O   
1345 C CB  . LEU A 183 ? 0.35401 0.24914 0.39086 0.01984  -0.01360 -0.01448 190 LEU A CB  
1346 C CG  . LEU A 183 ? 0.31561 0.23170 0.36054 0.00494  -0.01794 -0.02096 190 LEU A CG  
1347 C CD1 . LEU A 183 ? 0.34647 0.25718 0.38861 -0.00642 -0.01703 -0.01700 190 LEU A CD1 
1348 C CD2 . LEU A 183 ? 0.36454 0.31181 0.42017 0.00848  -0.02377 -0.01811 190 LEU A CD2 
1349 N N   . LYS A 184 ? 0.36623 0.27853 0.40942 0.06259  -0.01385 0.00505  191 LYS A N   
1350 C CA  . LYS A 184 ? 0.38115 0.28414 0.41893 0.08144  -0.01223 0.01749  191 LYS A CA  
1351 C C   . LYS A 184 ? 0.43181 0.30010 0.45124 0.07734  -0.00861 0.02373  191 LYS A C   
1352 O O   . LYS A 184 ? 0.45326 0.32078 0.46976 0.06028  -0.01050 0.02162  191 LYS A O   
1353 C CB  . LYS A 184 ? 0.38601 0.33053 0.43867 0.08923  -0.02247 0.02692  191 LYS A CB  
1354 C CG  . LYS A 184 ? 0.39610 0.37833 0.47136 0.09313  -0.02473 0.02398  191 LYS A CG  
1355 C CD  . LYS A 184 ? 0.47296 0.49686 0.56436 0.08969  -0.03794 0.02974  191 LYS A CD  
1356 C CE  . LYS A 184 ? 0.47712 0.53943 0.59412 0.08715  -0.04003 0.02721  191 LYS A CE  
1357 N NZ  . LYS A 184 ? 0.55986 0.66179 0.69412 0.08306  -0.05400 0.03219  191 LYS A NZ  
1358 N N   . GLU A 185 ? 0.46474 0.30484 0.47195 0.09472  -0.00208 0.03320  192 GLU A N   
1359 C CA  . GLU A 185 ? 0.54582 0.34601 0.53380 0.09194  0.00462  0.04127  192 GLU A CA  
1360 C C   . GLU A 185 ? 0.56289 0.37910 0.54723 0.08398  -0.00154 0.05021  192 GLU A C   
1361 O O   . GLU A 185 ? 0.53205 0.32434 0.50555 0.07043  0.00449  0.05208  192 GLU A O   
1362 C CB  . GLU A 185 ? 0.65827 0.42973 0.63348 0.11737  0.01185  0.05389  192 GLU A CB  
1363 C CG  . GLU A 185 ? 0.99105 0.72623 0.94526 0.12036  0.01826  0.06929  192 GLU A CG  
1364 C CD  . GLU A 185 ? 1.14797 0.91084 1.09870 0.13757  0.00947  0.08776  192 GLU A CD  
1365 O OE1 . GLU A 185 ? 1.10614 0.90434 1.06951 0.15606  0.00119  0.09161  192 GLU A OE1 
1366 O OE2 . GLU A 185 ? 1.01889 0.77017 0.95408 0.13282  0.01073  0.09868  192 GLU A OE2 
1367 N N   . ASP A 186 ? 0.49079 0.34726 0.48349 0.09160  -0.01307 0.05547  193 ASP A N   
1368 C CA  . ASP A 186 ? 0.48275 0.35107 0.46572 0.08683  -0.01913 0.06318  193 ASP A CA  
1369 C C   . ASP A 186 ? 0.44024 0.33317 0.43243 0.06657  -0.02501 0.05146  193 ASP A C   
1370 O O   . ASP A 186 ? 0.41400 0.31972 0.39741 0.06333  -0.03070 0.05522  193 ASP A O   
1371 C CB  . ASP A 186 ? 0.49145 0.38601 0.47302 0.10666  -0.02990 0.07564  193 ASP A CB  
1372 C CG  . ASP A 186 ? 0.58781 0.52849 0.59418 0.10848  -0.04174 0.06873  193 ASP A CG  
1373 O OD1 . ASP A 186 ? 0.65493 0.60054 0.67795 0.10332  -0.03804 0.05801  193 ASP A OD1 
1374 O OD2 . ASP A 186 ? 0.68092 0.65342 0.68994 0.11675  -0.05464 0.07530  193 ASP A OD2 
1375 N N   . GLN A 187 ? 0.36894 0.26487 0.37489 0.05394  -0.02270 0.03761  194 GLN A N   
1376 C CA  . GLN A 187 ? 0.30673 0.22436 0.32156 0.03787  -0.02733 0.02762  194 GLN A CA  
1377 C C   . GLN A 187 ? 0.33146 0.23047 0.34515 0.02152  -0.01897 0.02041  194 GLN A C   
1378 O O   . GLN A 187 ? 0.36389 0.27801 0.38782 0.01022  -0.02091 0.01054  194 GLN A O   
1379 C CB  . GLN A 187 ? 0.34055 0.28636 0.37458 0.03853  -0.03349 0.01952  194 GLN A CB  
1380 C CG  . GLN A 187 ? 0.33279 0.30463 0.37412 0.05194  -0.04266 0.02661  194 GLN A CG  
1381 C CD  . GLN A 187 ? 0.34305 0.33008 0.37609 0.04984  -0.05258 0.03084  194 GLN A CD  
1382 O OE1 . GLN A 187 ? 0.36042 0.35005 0.38968 0.03625  -0.05415 0.02421  194 GLN A OE1 
1383 N NE2 . GLN A 187 ? 0.38712 0.38718 0.41750 0.06410  -0.06020 0.04079  194 GLN A NE2 
1384 N N   . THR A 188 ? 0.38389 0.25091 0.38606 0.01981  -0.00958 0.02614  195 THR A N   
1385 C CA  . THR A 188 ? 0.43527 0.28937 0.44135 0.00170  -0.00259 0.01874  195 THR A CA  
1386 C C   . THR A 188 ? 0.42714 0.29510 0.43337 -0.00970 -0.00115 0.02044  195 THR A C   
1387 O O   . THR A 188 ? 0.40943 0.27575 0.42411 -0.02494 0.00383  0.01466  195 THR A O   
1388 C CB  . THR A 188 ? 0.47900 0.29198 0.47551 -0.00061 0.00810  0.02307  195 THR A CB  
1389 O OG1 . THR A 188 ? 0.51442 0.31158 0.49479 0.00655  0.01364  0.03963  195 THR A OG1 
1390 C CG2 . THR A 188 ? 0.45339 0.24804 0.44792 0.01107  0.00866  0.01855  195 THR A CG2 
1391 N N   . GLU A 189 ? 0.38741 0.27053 0.38465 -0.00254 -0.00557 0.02730  196 GLU A N   
1392 C CA  . GLU A 189 ? 0.39717 0.29552 0.39346 -0.01117 -0.00390 0.02611  196 GLU A CA  
1393 C C   . GLU A 189 ? 0.36340 0.28252 0.37743 -0.02056 -0.00739 0.01302  196 GLU A C   
1394 O O   . GLU A 189 ? 0.34683 0.27458 0.36520 -0.02931 -0.00246 0.01112  196 GLU A O   
1395 C CB  . GLU A 189 ? 0.40410 0.31505 0.38469 -0.00134 -0.01055 0.03143  196 GLU A CB  
1396 C CG  . GLU A 189 ? 0.35545 0.28970 0.34405 0.00302  -0.02388 0.02331  196 GLU A CG  
1397 C CD  . GLU A 189 ? 0.42601 0.36946 0.39727 0.01219  -0.03259 0.02835  196 GLU A CD  
1398 O OE1 . GLU A 189 ? 0.46858 0.40797 0.43138 0.02432  -0.03645 0.03783  196 GLU A OE1 
1399 O OE2 . GLU A 189 ? 0.43750 0.39096 0.40114 0.00831  -0.03550 0.02299  196 GLU A OE2 
1400 N N   . TYR A 190 ? 0.33705 0.26568 0.36130 -0.01753 -0.01468 0.00528  197 TYR A N   
1401 C CA  . TYR A 190 ? 0.30998 0.25692 0.34783 -0.02422 -0.01762 -0.00496 197 TYR A CA  
1402 C C   . TYR A 190 ? 0.37134 0.31352 0.41928 -0.03465 -0.01344 -0.01137 197 TYR A C   
1403 O O   . TYR A 190 ? 0.35041 0.30803 0.40843 -0.03815 -0.01676 -0.01929 197 TYR A O   
1404 C CB  . TYR A 190 ? 0.30820 0.26799 0.35226 -0.01724 -0.02559 -0.00911 197 TYR A CB  
1405 C CG  . TYR A 190 ? 0.29410 0.26308 0.33127 -0.01062 -0.03194 -0.00452 197 TYR A CG  
1406 C CD1 . TYR A 190 ? 0.32518 0.30231 0.35662 -0.01405 -0.03361 -0.00620 197 TYR A CD1 
1407 C CD2 . TYR A 190 ? 0.30938 0.27858 0.34411 -0.00026 -0.03651 0.00136  197 TYR A CD2 
1408 C CE1 . TYR A 190 ? 0.32834 0.31188 0.35002 -0.00974 -0.04106 -0.00433 197 TYR A CE1 
1409 C CE2 . TYR A 190 ? 0.35042 0.33183 0.37925 0.00440  -0.04481 0.00474  197 TYR A CE2 
1410 C CZ  . TYR A 190 ? 0.33373 0.32125 0.35484 -0.00165 -0.04769 0.00085  197 TYR A CZ  
1411 O OH  . TYR A 190 ? 0.33715 0.33468 0.34871 0.00133  -0.05742 0.00174  197 TYR A OH  
1412 N N   . LEU A 191 ? 0.30903 0.22946 0.35378 -0.03995 -0.00686 -0.00825 198 LEU A N   
1413 C CA  . LEU A 191 ? 0.33502 0.25299 0.39059 -0.05438 -0.00376 -0.01521 198 LEU A CA  
1414 C C   . LEU A 191 ? 0.32291 0.24802 0.38462 -0.06527 0.00388  -0.00980 198 LEU A C   
1415 O O   . LEU A 191 ? 0.36681 0.29675 0.44242 -0.07967 0.00605  -0.01483 198 LEU A O   
1416 C CB  . LEU A 191 ? 0.35606 0.24198 0.40545 -0.05642 -0.00035 -0.01678 198 LEU A CB  
1417 C CG  . LEU A 191 ? 0.38241 0.26214 0.42619 -0.04411 -0.00545 -0.02232 198 LEU A CG  
1418 C CD1 . LEU A 191 ? 0.43534 0.27756 0.46950 -0.04435 -0.00013 -0.02420 198 LEU A CD1 
1419 C CD2 . LEU A 191 ? 0.41511 0.31860 0.46794 -0.04619 -0.01266 -0.03421 198 LEU A CD2 
1420 N N   . GLU A 192 ? 0.33875 0.26502 0.39012 -0.05900 0.00835  0.00042  199 GLU A N   
1421 C CA  . GLU A 192 ? 0.32299 0.25557 0.37776 -0.06696 0.01879  0.00765  199 GLU A CA  
1422 C C   . GLU A 192 ? 0.31754 0.28197 0.38391 -0.06723 0.01737  0.00290  199 GLU A C   
1423 O O   . GLU A 192 ? 0.30836 0.28254 0.36789 -0.05677 0.01108  -0.00010 199 GLU A O   
1424 C CB  . GLU A 192 ? 0.39973 0.31755 0.43303 -0.05835 0.02578  0.02128  199 GLU A CB  
1425 C CG  . GLU A 192 ? 0.45228 0.33628 0.47252 -0.05468 0.02819  0.02868  199 GLU A CG  
1426 C CD  . GLU A 192 ? 0.88154 0.75206 0.87692 -0.04280 0.03337  0.04380  199 GLU A CD  
1427 O OE1 . GLU A 192 ? 1.04306 0.92579 1.03104 -0.04217 0.03942  0.04937  199 GLU A OE1 
1428 O OE2 . GLU A 192 ? 1.00926 0.85730 0.99087 -0.03241 0.03173  0.05047  199 GLU A OE2 
1429 N N   . GLU A 193 ? 0.31963 0.30019 0.40496 -0.07945 0.02354  0.00249  200 GLU A N   
1430 C CA  . GLU A 193 ? 0.28969 0.30238 0.38844 -0.07735 0.02273  -0.00130 200 GLU A CA  
1431 C C   . GLU A 193 ? 0.29208 0.30777 0.37360 -0.06363 0.02701  0.00375  200 GLU A C   
1432 O O   . GLU A 193 ? 0.30029 0.32684 0.37956 -0.05447 0.02137  -0.00173 200 GLU A O   
1433 C CB  . GLU A 193 ? 0.33349 0.36734 0.45742 -0.09207 0.03066  0.00068  200 GLU A CB  
1434 C CG  . GLU A 193 ? 0.40902 0.47923 0.54959 -0.08750 0.02946  -0.00245 200 GLU A CG  
1435 C CD  . GLU A 193 ? 0.64197 0.74188 0.81182 -0.10080 0.03773  0.00119  200 GLU A CD  
1436 O OE1 . GLU A 193 ? 0.60044 0.69011 0.77628 -0.11508 0.04685  0.00743  200 GLU A OE1 
1437 O OE2 . GLU A 193 ? 0.67402 0.80844 0.86242 -0.09702 0.03504  -0.00159 200 GLU A OE2 
1438 N N   . ARG A 194 ? 0.31714 0.32046 0.38359 -0.06191 0.03739  0.01404  201 ARG A N   
1439 C CA  . ARG A 194 ? 0.29212 0.29815 0.33881 -0.04929 0.04188  0.01703  201 ARG A CA  
1440 C C   . ARG A 194 ? 0.34092 0.33531 0.36775 -0.03845 0.02934  0.01116  201 ARG A C   
1441 O O   . ARG A 194 ? 0.31135 0.31076 0.32750 -0.02984 0.02785  0.00668  201 ARG A O   
1442 C CB  . ARG A 194 ? 0.38606 0.38121 0.41682 -0.04882 0.05604  0.02999  201 ARG A CB  
1443 C CG  . ARG A 194 ? 0.46760 0.43494 0.48046 -0.04816 0.05448  0.03731  201 ARG A CG  
1444 C CD  . ARG A 194 ? 0.51018 0.46856 0.50206 -0.04441 0.07014  0.05188  201 ARG A CD  
1445 N NE  . ARG A 194 ? 0.61387 0.54428 0.58324 -0.03954 0.06864  0.06133  201 ARG A NE  
1446 C CZ  . ARG A 194 ? 0.58392 0.50072 0.53071 -0.03516 0.08165  0.07650  201 ARG A CZ  
1447 N NH1 . ARG A 194 ? 0.59938 0.52848 0.54535 -0.03680 0.09846  0.08352  201 ARG A NH1 
1448 N NH2 . ARG A 194 ? 0.70356 0.59517 0.62765 -0.02724 0.07871  0.08603  201 ARG A NH2 
1449 N N   . ARG A 195 ? 0.33095 0.31004 0.35383 -0.03889 0.02067  0.01077  202 ARG A N   
1450 C CA  . ARG A 195 ? 0.32396 0.29845 0.33446 -0.03045 0.00836  0.00571  202 ARG A CA  
1451 C C   . ARG A 195 ? 0.29380 0.28129 0.31911 -0.03099 0.00082  -0.00451 202 ARG A C   
1452 O O   . ARG A 195 ? 0.28725 0.27625 0.30422 -0.02554 -0.00506 -0.00949 202 ARG A O   
1453 C CB  . ARG A 195 ? 0.33505 0.29386 0.34085 -0.02860 0.00273  0.00977  202 ARG A CB  
1454 C CG  . ARG A 195 ? 0.31250 0.27289 0.31045 -0.02037 -0.01046 0.00608  202 ARG A CG  
1455 C CD  . ARG A 195 ? 0.34043 0.29924 0.31400 -0.01316 -0.01276 0.00907  202 ARG A CD  
1456 N NE  . ARG A 195 ? 0.33960 0.30260 0.30888 -0.00744 -0.02659 0.00684  202 ARG A NE  
1457 C CZ  . ARG A 195 ? 0.35637 0.32794 0.32076 -0.00714 -0.03580 -0.00128 202 ARG A CZ  
1458 N NH1 . ARG A 195 ? 0.36542 0.33704 0.32295 -0.00943 -0.03226 -0.00796 202 ARG A NH1 
1459 N NH2 . ARG A 195 ? 0.36621 0.34633 0.33358 -0.00454 -0.04856 -0.00276 202 ARG A NH2 
1460 N N   . ILE A 196 ? 0.29269 0.28745 0.33818 -0.03788 0.00018  -0.00791 203 ILE A N   
1461 C CA  . ILE A 196 ? 0.28591 0.29315 0.34247 -0.03657 -0.00601 -0.01560 203 ILE A CA  
1462 C C   . ILE A 196 ? 0.23618 0.25527 0.29282 -0.03207 -0.00150 -0.01686 203 ILE A C   
1463 O O   . ILE A 196 ? 0.27540 0.29399 0.32764 -0.02649 -0.00576 -0.02106 203 ILE A O   
1464 C CB  . ILE A 196 ? 0.26853 0.28307 0.34259 -0.04383 -0.00807 -0.01953 203 ILE A CB  
1465 C CG1 . ILE A 196 ? 0.30501 0.30224 0.37499 -0.04524 -0.01168 -0.01971 203 ILE A CG1 
1466 C CG2 . ILE A 196 ? 0.24970 0.27778 0.33092 -0.03976 -0.01368 -0.02528 203 ILE A CG2 
1467 C CD1 . ILE A 196 ? 0.33334 0.33004 0.41532 -0.05529 -0.01158 -0.02445 203 ILE A CD1 
1468 N N   . LYS A 197 ? 0.24940 0.27828 0.31129 -0.03397 0.00847  -0.01263 204 LYS A N   
1469 C CA  . LYS A 197 ? 0.27288 0.31379 0.33483 -0.02636 0.01494  -0.01310 204 LYS A CA  
1470 C C   . LYS A 197 ? 0.25983 0.28387 0.29601 -0.01735 0.01454  -0.01542 204 LYS A C   
1471 O O   . LYS A 197 ? 0.28183 0.30470 0.31333 -0.00973 0.01450  -0.01999 204 LYS A O   
1472 C CB  . LYS A 197 ? 0.31116 0.36699 0.38245 -0.02903 0.02809  -0.00627 204 LYS A CB  
1473 C CG  . LYS A 197 ? 0.38357 0.46544 0.48442 -0.03689 0.02882  -0.00596 204 LYS A CG  
1474 C CD  . LYS A 197 ? 0.38334 0.48419 0.49654 -0.04014 0.04408  0.00236  204 LYS A CD  
1475 C CE  . LYS A 197 ? 0.67325 0.80363 0.82080 -0.05320 0.04307  0.00248  204 LYS A CE  
1476 N NZ  . LYS A 197 ? 0.70602 0.84638 0.86633 -0.06421 0.05750  0.01191  204 LYS A NZ  
1477 N N   . GLU A 198 ? 0.27826 0.28764 0.29543 -0.01772 0.01448  -0.01227 205 GLU A N   
1478 C CA  . GLU A 198 ? 0.28945 0.28375 0.27945 -0.01071 0.01158  -0.01621 205 GLU A CA  
1479 C C   . GLU A 198 ? 0.29020 0.27775 0.27998 -0.01118 -0.00089 -0.02430 205 GLU A C   
1480 O O   . GLU A 198 ? 0.31146 0.28910 0.28699 -0.00680 -0.00216 -0.03103 205 GLU A O   
1481 C CB  . GLU A 198 ? 0.27769 0.26113 0.24796 -0.01058 0.01112  -0.01014 205 GLU A CB  
1482 C CG  . GLU A 198 ? 0.33235 0.30214 0.27268 -0.00497 0.00291  -0.01554 205 GLU A CG  
1483 C CD  . GLU A 198 ? 0.36925 0.33183 0.29039 -0.00286 0.00039  -0.00756 205 GLU A CD  
1484 O OE1 . GLU A 198 ? 0.38190 0.34562 0.31663 -0.00654 -0.00442 -0.00208 205 GLU A OE1 
1485 O OE2 . GLU A 198 ? 0.38688 0.34133 0.27717 0.00399  0.00272  -0.00702 205 GLU A OE2 
1486 N N   . ILE A 199 ? 0.26272 0.25358 0.26715 -0.01672 -0.00915 -0.02377 206 ILE A N   
1487 C CA  . ILE A 199 ? 0.24680 0.23417 0.25366 -0.01816 -0.01927 -0.02950 206 ILE A CA  
1488 C C   . ILE A 199 ? 0.27102 0.26125 0.28809 -0.01642 -0.01674 -0.03305 206 ILE A C   
1489 O O   . ILE A 199 ? 0.29202 0.27251 0.30321 -0.01632 -0.02047 -0.03812 206 ILE A O   
1490 C CB  . ILE A 199 ? 0.27435 0.26632 0.29386 -0.02195 -0.02609 -0.02668 206 ILE A CB  
1491 C CG1 . ILE A 199 ? 0.32179 0.30864 0.32865 -0.02045 -0.02946 -0.02183 206 ILE A CG1 
1492 C CG2 . ILE A 199 ? 0.31460 0.30897 0.34347 -0.02398 -0.03320 -0.03060 206 ILE A CG2 
1493 C CD1 . ILE A 199 ? 0.34010 0.32889 0.36043 -0.02137 -0.03099 -0.01726 206 ILE A CD1 
1494 N N   . VAL A 200 ? 0.24537 0.24881 0.27771 -0.01535 -0.01087 -0.03007 207 VAL A N   
1495 C CA  . VAL A 200 ? 0.24926 0.25706 0.28917 -0.01036 -0.00850 -0.03142 207 VAL A CA  
1496 C C   . VAL A 200 ? 0.28645 0.28288 0.31102 -0.00213 -0.00169 -0.03402 207 VAL A C   
1497 O O   . VAL A 200 ? 0.28780 0.27123 0.30679 0.00180  -0.00192 -0.03721 207 VAL A O   
1498 C CB  . VAL A 200 ? 0.26121 0.29073 0.32030 -0.01047 -0.00554 -0.02795 207 VAL A CB  
1499 C CG1 . VAL A 200 ? 0.27563 0.31289 0.34027 -0.00132 -0.00238 -0.02725 207 VAL A CG1 
1500 C CG2 . VAL A 200 ? 0.24458 0.27847 0.31364 -0.01761 -0.01269 -0.02827 207 VAL A CG2 
1501 N N   . LYS A 201 ? 0.26741 0.26501 0.28232 0.00115  0.00591  -0.03257 208 LYS A N   
1502 C CA  . LYS A 201 ? 0.28075 0.26535 0.27716 0.01134  0.01409  -0.03606 208 LYS A CA  
1503 C C   . LYS A 201 ? 0.30631 0.26359 0.27848 0.00947  0.00761  -0.04469 208 LYS A C   
1504 O O   . LYS A 201 ? 0.36152 0.29987 0.31960 0.01616  0.01138  -0.05048 208 LYS A O   
1505 C CB  . LYS A 201 ? 0.31191 0.30503 0.30131 0.01583  0.02553  -0.03176 208 LYS A CB  
1506 C CG  . LYS A 201 ? 0.41902 0.40171 0.38968 0.03011  0.03759  -0.03487 208 LYS A CG  
1507 C CD  . LYS A 201 ? 0.55426 0.55506 0.52718 0.03467  0.05155  -0.02742 208 LYS A CD  
1508 C CE  . LYS A 201 ? 0.66381 0.65030 0.60918 0.04993  0.06481  -0.03106 208 LYS A CE  
1509 N NZ  . LYS A 201 ? 0.78363 0.78760 0.72847 0.05223  0.07915  -0.02211 208 LYS A NZ  
1510 N N   . LYS A 202 ? 0.29460 0.24932 0.26169 0.00040  -0.00258 -0.04591 209 LYS A N   
1511 C CA  . LYS A 202 ? 0.32808 0.26255 0.27487 -0.00378 -0.01153 -0.05497 209 LYS A CA  
1512 C C   . LYS A 202 ? 0.30344 0.22883 0.26037 -0.00991 -0.01789 -0.05918 209 LYS A C   
1513 O O   . LYS A 202 ? 0.35039 0.25266 0.29072 -0.01160 -0.01988 -0.06830 209 LYS A O   
1514 C CB  . LYS A 202 ? 0.32209 0.26318 0.26442 -0.01015 -0.02173 -0.05311 209 LYS A CB  
1515 C CG  . LYS A 202 ? 0.37200 0.29838 0.29259 -0.01493 -0.03324 -0.06307 209 LYS A CG  
1516 C CD  . LYS A 202 ? 0.60449 0.54073 0.51590 -0.01595 -0.04191 -0.05889 209 LYS A CD  
1517 C CE  . LYS A 202 ? 0.90473 0.83295 0.79400 -0.02091 -0.05678 -0.06913 209 LYS A CE  
1518 N NZ  . LYS A 202 ? 0.69060 0.63500 0.57778 -0.02033 -0.06754 -0.06212 209 LYS A NZ  
1519 N N   . HIS A 203 ? 0.30761 0.24871 0.28950 -0.01389 -0.02053 -0.05294 210 HIS A N   
1520 C CA  . HIS A 203 ? 0.32621 0.26275 0.31918 -0.02138 -0.02645 -0.05431 210 HIS A CA  
1521 C C   . HIS A 203 ? 0.31842 0.25568 0.32423 -0.01626 -0.01951 -0.04938 210 HIS A C   
1522 O O   . HIS A 203 ? 0.34127 0.26864 0.35205 -0.02123 -0.02097 -0.04962 210 HIS A O   
1523 C CB  . HIS A 203 ? 0.34023 0.29503 0.34897 -0.02888 -0.03544 -0.05044 210 HIS A CB  
1524 C CG  . HIS A 203 ? 0.35705 0.31314 0.35473 -0.03336 -0.04499 -0.05388 210 HIS A CG  
1525 N ND1 . HIS A 203 ? 0.44350 0.38739 0.42883 -0.04037 -0.05301 -0.06261 210 HIS A ND1 
1526 C CD2 . HIS A 203 ? 0.40230 0.37000 0.39804 -0.03127 -0.04828 -0.04940 210 HIS A CD2 
1527 C CE1 . HIS A 203 ? 0.42015 0.37267 0.39689 -0.04171 -0.06246 -0.06332 210 HIS A CE1 
1528 N NE2 . HIS A 203 ? 0.42724 0.39296 0.40943 -0.03506 -0.05887 -0.05429 210 HIS A NE2 
1529 N N   . SER A 204 ? 0.32264 0.25077 0.25910 -0.02070 -0.05373 -0.03388 211 SER A N   
1530 C CA  . SER A 204 ? 0.28406 0.22351 0.24231 -0.01528 -0.04139 -0.03428 211 SER A CA  
1531 C C   . SER A 204 ? 0.29102 0.22073 0.23310 -0.00966 -0.02612 -0.03794 211 SER A C   
1532 O O   . SER A 204 ? 0.34123 0.28355 0.29857 -0.00331 -0.01617 -0.03648 211 SER A O   
1533 C CB  . SER A 204 ? 0.31304 0.27354 0.29738 -0.00981 -0.03948 -0.02894 211 SER A CB  
1534 O OG  . SER A 204 ? 0.31408 0.28551 0.31675 -0.01229 -0.05231 -0.02507 211 SER A OG  
1535 N N   . GLN A 205 ? 0.35617 0.26454 0.26724 -0.01165 -0.02481 -0.04315 212 GLN A N   
1536 C CA  . GLN A 205 ? 0.39684 0.29961 0.29460 -0.00418 -0.00811 -0.04572 212 GLN A CA  
1537 C C   . GLN A 205 ? 0.43300 0.33313 0.34011 0.00230  0.00184  -0.04884 212 GLN A C   
1538 O O   . GLN A 205 ? 0.43045 0.33492 0.33819 0.01117  0.01576  -0.04890 212 GLN A O   
1539 C CB  . GLN A 205 ? 0.47125 0.35122 0.32984 -0.00574 -0.00530 -0.05129 212 GLN A CB  
1540 C CG  . GLN A 205 ? 0.53086 0.38832 0.37009 -0.01238 -0.01500 -0.05962 212 GLN A CG  
1541 C CD  . GLN A 205 ? 0.80509 0.63923 0.59912 -0.01541 -0.01574 -0.06628 212 GLN A CD  
1542 O OE1 . GLN A 205 ? 0.66895 0.49034 0.44395 -0.02511 -0.03251 -0.07045 212 GLN A OE1 
1543 N NE2 . GLN A 205 ? 0.56233 0.39177 0.33852 -0.00719 0.00281  -0.06788 212 GLN A NE2 
1544 N N   . PHE A 206 ? 0.38703 0.28101 0.30321 -0.00158 -0.00443 -0.05001 213 PHE A N   
1545 C CA  . PHE A 206 ? 0.32858 0.21477 0.25084 0.00498  0.00492  -0.05074 213 PHE A CA  
1546 C C   . PHE A 206 ? 0.35659 0.26406 0.30827 0.00735  0.00494  -0.04268 213 PHE A C   
1547 O O   . PHE A 206 ? 0.35053 0.25126 0.30725 0.01280  0.01142  -0.04034 213 PHE A O   
1548 C CB  . PHE A 206 ? 0.37992 0.23466 0.28462 -0.00188 0.00066  -0.05831 213 PHE A CB  
1549 C CG  . PHE A 206 ? 0.43874 0.27004 0.30782 -0.00433 0.00028  -0.06831 213 PHE A CG  
1550 C CD1 . PHE A 206 ? 0.44577 0.27197 0.29756 0.00694  0.01567  -0.07161 213 PHE A CD1 
1551 C CD2 . PHE A 206 ? 0.45796 0.27405 0.30999 -0.01772 -0.01497 -0.07448 213 PHE A CD2 
1552 C CE1 . PHE A 206 ? 0.51109 0.31451 0.32451 0.00519  0.01766  -0.08129 213 PHE A CE1 
1553 C CE2 . PHE A 206 ? 0.51611 0.30953 0.32818 -0.02028 -0.01638 -0.08441 213 PHE A CE2 
1554 C CZ  . PHE A 206 ? 0.53641 0.32189 0.32667 -0.00847 0.00116  -0.08806 213 PHE A CZ  
1555 N N   . ILE A 207 ? 0.31427 0.24567 0.28308 0.00511  -0.00066 -0.03813 214 ILE A N   
1556 C CA  . ILE A 207 ? 0.29829 0.24972 0.28989 0.00787  0.00068  -0.03193 214 ILE A CA  
1557 C C   . ILE A 207 ? 0.32239 0.28069 0.31684 0.01909  0.01102  -0.02906 214 ILE A C   
1558 O O   . ILE A 207 ? 0.33427 0.29704 0.32413 0.02483  0.01644  -0.03093 214 ILE A O   
1559 C CB  . ILE A 207 ? 0.27741 0.24984 0.28287 0.00586  -0.00506 -0.03036 214 ILE A CB  
1560 C CG1 . ILE A 207 ? 0.31388 0.28341 0.32268 -0.00321 -0.01665 -0.03061 214 ILE A CG1 
1561 C CG2 . ILE A 207 ? 0.26449 0.25876 0.28782 0.01084  -0.00116 -0.02638 214 ILE A CG2 
1562 C CD1 . ILE A 207 ? 0.33433 0.30744 0.35860 -0.00863 -0.01889 -0.02737 214 ILE A CD1 
1563 N N   . GLY A 208 ? 0.29816 0.25825 0.30080 0.02222  0.01384  -0.02318 215 GLY A N   
1564 C CA  . GLY A 208 ? 0.29980 0.26560 0.30447 0.03435  0.02157  -0.01836 215 GLY A CA  
1565 C C   . GLY A 208 ? 0.32528 0.32136 0.34190 0.03969  0.02121  -0.01487 215 GLY A C   
1566 O O   . GLY A 208 ? 0.35629 0.36116 0.37643 0.04846  0.02413  -0.00801 215 GLY A O   
1567 N N   . TYR A 209 ? 0.28499 0.29536 0.30645 0.03447  0.01674  -0.01947 216 TYR A N   
1568 C CA  . TYR A 209 ? 0.27906 0.31484 0.30959 0.03722  0.01519  -0.01975 216 TYR A CA  
1569 C C   . TYR A 209 ? 0.29301 0.33259 0.32490 0.03320  0.01416  -0.02564 216 TYR A C   
1570 O O   . TYR A 209 ? 0.28134 0.30618 0.30649 0.02726  0.01267  -0.02836 216 TYR A O   
1571 C CB  . TYR A 209 ? 0.24192 0.28712 0.27734 0.03340  0.01180  -0.01973 216 TYR A CB  
1572 C CG  . TYR A 209 ? 0.23774 0.28005 0.27162 0.03582  0.01494  -0.01172 216 TYR A CG  
1573 C CD1 . TYR A 209 ? 0.25675 0.31127 0.28798 0.04395  0.01701  -0.00522 216 TYR A CD1 
1574 C CD2 . TYR A 209 ? 0.26883 0.29704 0.30427 0.02919  0.01529  -0.00919 216 TYR A CD2 
1575 C CE1 . TYR A 209 ? 0.25923 0.30838 0.28656 0.04627  0.02119  0.00509  216 TYR A CE1 
1576 C CE2 . TYR A 209 ? 0.27787 0.30155 0.31298 0.02974  0.01989  0.00010  216 TYR A CE2 
1577 C CZ  . TYR A 209 ? 0.28204 0.31497 0.31188 0.03864  0.02363  0.00784  216 TYR A CZ  
1578 O OH  . TYR A 209 ? 0.33545 0.36236 0.36265 0.03940  0.02904  0.01947  216 TYR A OH  
1579 N N   . PRO A 210 ? 0.25646 0.31555 0.29671 0.03523  0.01427  -0.02685 217 PRO A N   
1580 C CA  . PRO A 210 ? 0.23673 0.29846 0.28018 0.02908  0.01461  -0.03093 217 PRO A CA  
1581 C C   . PRO A 210 ? 0.29231 0.34802 0.33582 0.02111  0.00894  -0.03487 217 PRO A C   
1582 O O   . PRO A 210 ? 0.30220 0.36576 0.35032 0.02098  0.00495  -0.03743 217 PRO A O   
1583 C CB  . PRO A 210 ? 0.26550 0.35346 0.32288 0.03144  0.01433  -0.03109 217 PRO A CB  
1584 C CG  . PRO A 210 ? 0.29838 0.39767 0.35664 0.03759  0.01055  -0.02859 217 PRO A CG  
1585 C CD  . PRO A 210 ? 0.29745 0.37763 0.34470 0.04225  0.01323  -0.02357 217 PRO A CD  
1586 N N   . ILE A 211 ? 0.26787 0.30910 0.30481 0.01576  0.00927  -0.03498 218 ILE A N   
1587 C CA  . ILE A 211 ? 0.25586 0.28855 0.29353 0.01012  0.00379  -0.03656 218 ILE A CA  
1588 C C   . ILE A 211 ? 0.27259 0.30690 0.31422 0.00415  0.00596  -0.03710 218 ILE A C   
1589 O O   . ILE A 211 ? 0.32873 0.35777 0.36291 0.00201  0.01156  -0.03365 218 ILE A O   
1590 C CB  . ILE A 211 ? 0.27645 0.29060 0.30248 0.00832  0.00003  -0.03371 218 ILE A CB  
1591 C CG1 . ILE A 211 ? 0.28464 0.29814 0.31112 0.01117  -0.00213 -0.03306 218 ILE A CG1 
1592 C CG2 . ILE A 211 ? 0.28055 0.28730 0.30971 0.00488  -0.00596 -0.03304 218 ILE A CG2 
1593 C CD1 . ILE A 211 ? 0.29543 0.29177 0.30974 0.00737  -0.00758 -0.03137 218 ILE A CD1 
1594 N N   . THR A 212 ? 0.24922 0.29007 0.30172 0.00088  0.00269  -0.04186 219 THR A N   
1595 C CA  . THR A 212 ? 0.24298 0.28418 0.30236 -0.00761 0.00447  -0.04254 219 THR A CA  
1596 C C   . THR A 212 ? 0.25848 0.27835 0.31535 -0.01142 0.00066  -0.04201 219 THR A C   
1597 O O   . THR A 212 ? 0.25810 0.27438 0.31889 -0.00846 -0.00408 -0.04746 219 THR A O   
1598 C CB  . THR A 212 ? 0.25683 0.31827 0.33010 -0.01054 0.00214  -0.04957 219 THR A CB  
1599 O OG1 . THR A 212 ? 0.29280 0.37591 0.36994 -0.00457 0.00455  -0.04753 219 THR A OG1 
1600 C CG2 . THR A 212 ? 0.25669 0.31810 0.34102 -0.02303 0.00355  -0.05051 219 THR A CG2 
1601 N N   . LEU A 213 ? 0.26015 0.26568 0.30978 -0.01673 0.00369  -0.03474 220 LEU A N   
1602 C CA  . LEU A 213 ? 0.26995 0.25309 0.31755 -0.01985 -0.00005 -0.03141 220 LEU A CA  
1603 C C   . LEU A 213 ? 0.27687 0.25784 0.33679 -0.03033 0.00229  -0.03449 220 LEU A C   
1604 O O   . LEU A 213 ? 0.31826 0.30461 0.38041 -0.03893 0.00936  -0.02966 220 LEU A O   
1605 C CB  . LEU A 213 ? 0.28589 0.25289 0.31482 -0.02043 0.00104  -0.02001 220 LEU A CB  
1606 C CG  . LEU A 213 ? 0.34431 0.28658 0.36839 -0.02314 -0.00262 -0.01191 220 LEU A CG  
1607 C CD1 . LEU A 213 ? 0.30591 0.23986 0.33977 -0.01549 -0.01172 -0.01539 220 LEU A CD1 
1608 C CD2 . LEU A 213 ? 0.39500 0.32501 0.39379 -0.02263 -0.00302 -0.00018 220 LEU A CD2 
1609 N N   . PHE A 214 ? 0.25900 0.23115 0.32710 -0.03011 -0.00276 -0.04267 221 PHE A N   
1610 C CA  . PHE A 214 ? 0.26202 0.22616 0.34111 -0.04166 -0.00240 -0.04815 221 PHE A CA  
1611 C C   . PHE A 214 ? 0.30805 0.24369 0.38283 -0.04823 0.00011  -0.03684 221 PHE A C   
1612 O O   . PHE A 214 ? 0.36233 0.28007 0.42604 -0.04029 -0.00237 -0.02805 221 PHE A O   
1613 C CB  . PHE A 214 ? 0.30070 0.25714 0.38500 -0.03850 -0.00788 -0.06261 221 PHE A CB  
1614 C CG  . PHE A 214 ? 0.25321 0.23623 0.33975 -0.03526 -0.01044 -0.07457 221 PHE A CG  
1615 C CD1 . PHE A 214 ? 0.26417 0.27232 0.34746 -0.02875 -0.00913 -0.07043 221 PHE A CD1 
1616 C CD2 . PHE A 214 ? 0.27903 0.25836 0.36838 -0.03896 -0.01441 -0.09019 221 PHE A CD2 
1617 C CE1 . PHE A 214 ? 0.24331 0.27404 0.32640 -0.02477 -0.01186 -0.07860 221 PHE A CE1 
1618 C CE2 . PHE A 214 ? 0.26832 0.27245 0.35458 -0.03579 -0.01791 -0.10084 221 PHE A CE2 
1619 C CZ  . PHE A 214 ? 0.24324 0.27387 0.32680 -0.02836 -0.01663 -0.09321 221 PHE A CZ  
1620 N N   . VAL A 215 ? 0.30386 0.23598 0.38825 -0.06333 0.00437  -0.03584 222 VAL A N   
1621 C CA  . VAL A 215 ? 0.37833 0.27894 0.45858 -0.07108 0.00759  -0.02380 222 VAL A CA  
1622 C C   . VAL A 215 ? 0.42635 0.30113 0.51729 -0.07768 0.00355  -0.03339 222 VAL A C   
1623 O O   . VAL A 215 ? 0.39653 0.28039 0.49684 -0.07859 -0.00122 -0.05087 222 VAL A O   
1624 C CB  . VAL A 215 ? 0.50188 0.41133 0.58353 -0.08455 0.01834  -0.01180 222 VAL A CB  
1625 C CG1 . VAL A 215 ? 0.54678 0.46741 0.60841 -0.07503 0.02332  -0.00102 222 VAL A CG1 
1626 C CG2 . VAL A 215 ? 0.39424 0.33297 0.49806 -0.09629 0.02047  -0.02155 222 VAL A CG2 
1627 N N   . GLU A 216 ? 0.43984 0.27886 0.52604 -0.08092 0.00509  -0.02201 223 GLU A N   
1628 C CA  . GLU A 216 ? 0.50635 0.31091 0.60062 -0.08566 0.00209  -0.03020 223 GLU A CA  
1629 C C   . GLU A 216 ? 0.58479 0.37003 0.68758 -0.10764 0.00837  -0.02242 223 GLU A C   
1630 O O   . GLU A 216 ? 0.61517 0.40045 0.71136 -0.11422 0.01612  -0.00321 223 GLU A O   
1631 C CB  . GLU A 216 ? 0.58737 0.35815 0.67267 -0.06849 -0.00225 -0.02343 223 GLU A CB  
1632 C CG  . GLU A 216 ? 0.54576 0.33656 0.62515 -0.04766 -0.00758 -0.02574 223 GLU A CG  
1633 C CD  . GLU A 216 ? 0.62256 0.38496 0.69922 -0.03063 -0.01256 -0.01683 223 GLU A CD  
1634 O OE1 . GLU A 216 ? 0.59919 0.33143 0.68388 -0.02644 -0.01317 -0.02469 223 GLU A OE1 
1635 O OE2 . GLU A 216 ? 0.66367 0.43469 0.73049 -0.02088 -0.01646 -0.00242 223 GLU A OE2 
1636 N N   . LYS A 217 ? 0.58932 0.35617 0.70534 -0.11946 0.00540  -0.03800 224 LYS A N   
1637 C CA  . LYS A 217 ? 0.65407 0.39555 0.78180 -0.14300 0.01028  -0.03269 224 LYS A CA  
1638 C C   . LYS A 217 ? 0.78056 0.48410 0.89588 -0.14188 0.01687  -0.00658 224 LYS A C   
1639 O O   . LYS A 217 ? 0.80177 0.47772 0.90373 -0.12303 0.01289  -0.00060 224 LYS A O   
1640 C CB  . LYS A 217 ? 0.74919 0.45925 0.88619 -0.15147 0.00401  -0.05432 224 LYS A CB  
1641 C CG  . LYS A 217 ? 1.02808 0.71881 1.15410 -0.12833 -0.00239 -0.06917 224 LYS A CG  
1642 C CD  . LYS A 217 ? 1.11953 0.76332 1.24943 -0.13601 -0.00550 -0.08799 224 LYS A CD  
1643 C CE  . LYS A 217 ? 1.08468 0.70500 1.20213 -0.10874 -0.00784 -0.09819 224 LYS A CE  
1644 N NZ  . LYS A 217 ? 0.96256 0.56053 1.06921 -0.11066 -0.01171 -0.12148 224 LYS A NZ  
# 
