data_7H9M
# 
_entry.id   7H9M 
# 
_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   7H9M         pdb_00007h9m 10.2210/pdb7h9m/pdb 
WWPDB D_1001407197 ?            ?                   
# 
_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                        7H9M 
_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 '(1m)-1-(2,4-difluorophenyl)-4-methylpiperidine-2,6-dione' 239.218   1   ?        ? ? ? 
3 water       nat water                                                      18.015    351 ?        ? ? ? 
# 
_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 '(1m)-1-(2,4-difluorophenyl)-4-methylpiperidine-2,6-dione' A1AW8 
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 
A1AW8 non-polymer         . '(1m)-1-(2,4-difluorophenyl)-4-methylpiperidine-2,6-dione' ? 'C12 H11 F2 N O2' 239.218 
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        A1AW8 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1AW8 
_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 A1AW8 1   301 301 A1AW8 CMN A . 
C 3 HOH   1   401 335 HOH   HOH A . 
C 3 HOH   2   402 287 HOH   HOH A . 
C 3 HOH   3   403 347 HOH   HOH A . 
C 3 HOH   4   404 326 HOH   HOH A . 
C 3 HOH   5   405 255 HOH   HOH A . 
C 3 HOH   6   406 222 HOH   HOH A . 
C 3 HOH   7   407 324 HOH   HOH A . 
C 3 HOH   8   408 320 HOH   HOH A . 
C 3 HOH   9   409 166 HOH   HOH A . 
C 3 HOH   10  410 268 HOH   HOH A . 
C 3 HOH   11  411 120 HOH   HOH A . 
C 3 HOH   12  412 242 HOH   HOH A . 
C 3 HOH   13  413 62  HOH   HOH A . 
C 3 HOH   14  414 83  HOH   HOH A . 
C 3 HOH   15  415 212 HOH   HOH A . 
C 3 HOH   16  416 54  HOH   HOH A . 
C 3 HOH   17  417 139 HOH   HOH A . 
C 3 HOH   18  418 171 HOH   HOH A . 
C 3 HOH   19  419 69  HOH   HOH A . 
C 3 HOH   20  420 137 HOH   HOH A . 
C 3 HOH   21  421 291 HOH   HOH A . 
C 3 HOH   22  422 227 HOH   HOH A . 
C 3 HOH   23  423 298 HOH   HOH A . 
C 3 HOH   24  424 189 HOH   HOH A . 
C 3 HOH   25  425 112 HOH   HOH A . 
C 3 HOH   26  426 247 HOH   HOH A . 
C 3 HOH   27  427 29  HOH   HOH A . 
C 3 HOH   28  428 313 HOH   HOH A . 
C 3 HOH   29  429 116 HOH   HOH A . 
C 3 HOH   30  430 38  HOH   HOH A . 
C 3 HOH   31  431 71  HOH   HOH A . 
C 3 HOH   32  432 140 HOH   HOH A . 
C 3 HOH   33  433 111 HOH   HOH A . 
C 3 HOH   34  434 51  HOH   HOH A . 
C 3 HOH   35  435 118 HOH   HOH A . 
C 3 HOH   36  436 8   HOH   HOH A . 
C 3 HOH   37  437 209 HOH   HOH A . 
C 3 HOH   38  438 64  HOH   HOH A . 
C 3 HOH   39  439 141 HOH   HOH A . 
C 3 HOH   40  440 150 HOH   HOH A . 
C 3 HOH   41  441 312 HOH   HOH A . 
C 3 HOH   42  442 172 HOH   HOH A . 
C 3 HOH   43  443 257 HOH   HOH A . 
C 3 HOH   44  444 39  HOH   HOH A . 
C 3 HOH   45  445 206 HOH   HOH A . 
C 3 HOH   46  446 25  HOH   HOH A . 
C 3 HOH   47  447 126 HOH   HOH A . 
C 3 HOH   48  448 159 HOH   HOH A . 
C 3 HOH   49  449 98  HOH   HOH A . 
C 3 HOH   50  450 12  HOH   HOH A . 
C 3 HOH   51  451 14  HOH   HOH A . 
C 3 HOH   52  452 110 HOH   HOH A . 
C 3 HOH   53  453 76  HOH   HOH A . 
C 3 HOH   54  454 204 HOH   HOH A . 
C 3 HOH   55  455 203 HOH   HOH A . 
C 3 HOH   56  456 5   HOH   HOH A . 
C 3 HOH   57  457 94  HOH   HOH A . 
C 3 HOH   58  458 65  HOH   HOH A . 
C 3 HOH   59  459 32  HOH   HOH A . 
C 3 HOH   60  460 44  HOH   HOH A . 
C 3 HOH   61  461 113 HOH   HOH A . 
C 3 HOH   62  462 243 HOH   HOH A . 
C 3 HOH   63  463 234 HOH   HOH A . 
C 3 HOH   64  464 221 HOH   HOH A . 
C 3 HOH   65  465 56  HOH   HOH A . 
C 3 HOH   66  466 68  HOH   HOH A . 
C 3 HOH   67  467 181 HOH   HOH A . 
C 3 HOH   68  468 9   HOH   HOH A . 
C 3 HOH   69  469 11  HOH   HOH A . 
C 3 HOH   70  470 10  HOH   HOH A . 
C 3 HOH   71  471 15  HOH   HOH A . 
C 3 HOH   72  472 49  HOH   HOH A . 
C 3 HOH   73  473 143 HOH   HOH A . 
C 3 HOH   74  474 59  HOH   HOH A . 
C 3 HOH   75  475 72  HOH   HOH A . 
C 3 HOH   76  476 164 HOH   HOH A . 
C 3 HOH   77  477 301 HOH   HOH A . 
C 3 HOH   78  478 264 HOH   HOH A . 
C 3 HOH   79  479 60  HOH   HOH A . 
C 3 HOH   80  480 1   HOH   HOH A . 
C 3 HOH   81  481 99  HOH   HOH A . 
C 3 HOH   82  482 7   HOH   HOH A . 
C 3 HOH   83  483 55  HOH   HOH A . 
C 3 HOH   84  484 3   HOH   HOH A . 
C 3 HOH   85  485 138 HOH   HOH A . 
C 3 HOH   86  486 92  HOH   HOH A . 
C 3 HOH   87  487 142 HOH   HOH A . 
C 3 HOH   88  488 57  HOH   HOH A . 
C 3 HOH   89  489 75  HOH   HOH A . 
C 3 HOH   90  490 13  HOH   HOH A . 
C 3 HOH   91  491 240 HOH   HOH A . 
C 3 HOH   92  492 28  HOH   HOH A . 
C 3 HOH   93  493 201 HOH   HOH A . 
C 3 HOH   94  494 157 HOH   HOH A . 
C 3 HOH   95  495 27  HOH   HOH A . 
C 3 HOH   96  496 93  HOH   HOH A . 
C 3 HOH   97  497 327 HOH   HOH A . 
C 3 HOH   98  498 325 HOH   HOH A . 
C 3 HOH   99  499 30  HOH   HOH A . 
C 3 HOH   100 500 19  HOH   HOH A . 
C 3 HOH   101 501 58  HOH   HOH A . 
C 3 HOH   102 502 155 HOH   HOH A . 
C 3 HOH   103 503 16  HOH   HOH A . 
C 3 HOH   104 504 156 HOH   HOH A . 
C 3 HOH   105 505 103 HOH   HOH A . 
C 3 HOH   106 506 96  HOH   HOH A . 
C 3 HOH   107 507 228 HOH   HOH A . 
C 3 HOH   108 508 244 HOH   HOH A . 
C 3 HOH   109 509 34  HOH   HOH A . 
C 3 HOH   110 510 295 HOH   HOH A . 
C 3 HOH   111 511 81  HOH   HOH A . 
C 3 HOH   112 512 80  HOH   HOH A . 
C 3 HOH   113 513 23  HOH   HOH A . 
C 3 HOH   114 514 107 HOH   HOH A . 
C 3 HOH   115 515 91  HOH   HOH A . 
C 3 HOH   116 516 169 HOH   HOH A . 
C 3 HOH   117 517 176 HOH   HOH A . 
C 3 HOH   118 518 119 HOH   HOH A . 
C 3 HOH   119 519 191 HOH   HOH A . 
C 3 HOH   120 520 101 HOH   HOH A . 
C 3 HOH   121 521 41  HOH   HOH A . 
C 3 HOH   122 522 6   HOH   HOH A . 
C 3 HOH   123 523 36  HOH   HOH A . 
C 3 HOH   124 524 86  HOH   HOH A . 
C 3 HOH   125 525 89  HOH   HOH A . 
C 3 HOH   126 526 130 HOH   HOH A . 
C 3 HOH   127 527 40  HOH   HOH A . 
C 3 HOH   128 528 43  HOH   HOH A . 
C 3 HOH   129 529 185 HOH   HOH A . 
C 3 HOH   130 530 131 HOH   HOH A . 
C 3 HOH   131 531 123 HOH   HOH A . 
C 3 HOH   132 532 290 HOH   HOH A . 
C 3 HOH   133 533 128 HOH   HOH A . 
C 3 HOH   134 534 88  HOH   HOH A . 
C 3 HOH   135 535 52  HOH   HOH A . 
C 3 HOH   136 536 248 HOH   HOH A . 
C 3 HOH   137 537 18  HOH   HOH A . 
C 3 HOH   138 538 77  HOH   HOH A . 
C 3 HOH   139 539 37  HOH   HOH A . 
C 3 HOH   140 540 26  HOH   HOH A . 
C 3 HOH   141 541 147 HOH   HOH A . 
C 3 HOH   142 542 231 HOH   HOH A . 
C 3 HOH   143 543 73  HOH   HOH A . 
C 3 HOH   144 544 67  HOH   HOH A . 
C 3 HOH   145 545 33  HOH   HOH A . 
C 3 HOH   146 546 303 HOH   HOH A . 
C 3 HOH   147 547 70  HOH   HOH A . 
C 3 HOH   148 548 4   HOH   HOH A . 
C 3 HOH   149 549 200 HOH   HOH A . 
C 3 HOH   150 550 17  HOH   HOH A . 
C 3 HOH   151 551 85  HOH   HOH A . 
C 3 HOH   152 552 192 HOH   HOH A . 
C 3 HOH   153 553 337 HOH   HOH A . 
C 3 HOH   154 554 293 HOH   HOH A . 
C 3 HOH   155 555 122 HOH   HOH A . 
C 3 HOH   156 556 272 HOH   HOH A . 
C 3 HOH   157 557 135 HOH   HOH A . 
C 3 HOH   158 558 109 HOH   HOH A . 
C 3 HOH   159 559 121 HOH   HOH A . 
C 3 HOH   160 560 160 HOH   HOH A . 
C 3 HOH   161 561 79  HOH   HOH A . 
C 3 HOH   162 562 256 HOH   HOH A . 
C 3 HOH   163 563 210 HOH   HOH A . 
C 3 HOH   164 564 20  HOH   HOH A . 
C 3 HOH   165 565 134 HOH   HOH A . 
C 3 HOH   166 566 224 HOH   HOH A . 
C 3 HOH   167 567 306 HOH   HOH A . 
C 3 HOH   168 568 182 HOH   HOH A . 
C 3 HOH   169 569 21  HOH   HOH A . 
C 3 HOH   170 570 74  HOH   HOH A . 
C 3 HOH   171 571 179 HOH   HOH A . 
C 3 HOH   172 572 265 HOH   HOH A . 
C 3 HOH   173 573 294 HOH   HOH A . 
C 3 HOH   174 574 53  HOH   HOH A . 
C 3 HOH   175 575 348 HOH   HOH A . 
C 3 HOH   176 576 82  HOH   HOH A . 
C 3 HOH   177 577 124 HOH   HOH A . 
C 3 HOH   178 578 258 HOH   HOH A . 
C 3 HOH   179 579 136 HOH   HOH A . 
C 3 HOH   180 580 278 HOH   HOH A . 
C 3 HOH   181 581 42  HOH   HOH A . 
C 3 HOH   182 582 174 HOH   HOH A . 
C 3 HOH   183 583 186 HOH   HOH A . 
C 3 HOH   184 584 202 HOH   HOH A . 
C 3 HOH   185 585 187 HOH   HOH A . 
C 3 HOH   186 586 151 HOH   HOH A . 
C 3 HOH   187 587 307 HOH   HOH A . 
C 3 HOH   188 588 22  HOH   HOH A . 
C 3 HOH   189 589 63  HOH   HOH A . 
C 3 HOH   190 590 102 HOH   HOH A . 
C 3 HOH   191 591 249 HOH   HOH A . 
C 3 HOH   192 592 50  HOH   HOH A . 
C 3 HOH   193 593 246 HOH   HOH A . 
C 3 HOH   194 594 114 HOH   HOH A . 
C 3 HOH   195 595 316 HOH   HOH A . 
C 3 HOH   196 596 333 HOH   HOH A . 
C 3 HOH   197 597 47  HOH   HOH A . 
C 3 HOH   198 598 46  HOH   HOH A . 
C 3 HOH   199 599 297 HOH   HOH A . 
C 3 HOH   200 600 269 HOH   HOH A . 
C 3 HOH   201 601 132 HOH   HOH A . 
C 3 HOH   202 602 45  HOH   HOH A . 
C 3 HOH   203 603 144 HOH   HOH A . 
C 3 HOH   204 604 158 HOH   HOH A . 
C 3 HOH   205 605 245 HOH   HOH A . 
C 3 HOH   206 606 322 HOH   HOH A . 
C 3 HOH   207 607 35  HOH   HOH A . 
C 3 HOH   208 608 317 HOH   HOH A . 
C 3 HOH   209 609 288 HOH   HOH A . 
C 3 HOH   210 610 178 HOH   HOH A . 
C 3 HOH   211 611 125 HOH   HOH A . 
C 3 HOH   212 612 2   HOH   HOH A . 
C 3 HOH   213 613 330 HOH   HOH A . 
C 3 HOH   214 614 300 HOH   HOH A . 
C 3 HOH   215 615 277 HOH   HOH A . 
C 3 HOH   216 616 163 HOH   HOH A . 
C 3 HOH   217 617 283 HOH   HOH A . 
C 3 HOH   218 618 282 HOH   HOH A . 
C 3 HOH   219 619 167 HOH   HOH A . 
C 3 HOH   220 620 342 HOH   HOH A . 
C 3 HOH   221 621 48  HOH   HOH A . 
C 3 HOH   222 622 343 HOH   HOH A . 
C 3 HOH   223 623 108 HOH   HOH A . 
C 3 HOH   224 624 286 HOH   HOH A . 
C 3 HOH   225 625 238 HOH   HOH A . 
C 3 HOH   226 626 318 HOH   HOH A . 
C 3 HOH   227 627 296 HOH   HOH A . 
C 3 HOH   228 628 314 HOH   HOH A . 
C 3 HOH   229 629 241 HOH   HOH A . 
C 3 HOH   230 630 90  HOH   HOH A . 
C 3 HOH   231 631 310 HOH   HOH A . 
C 3 HOH   232 632 198 HOH   HOH A . 
C 3 HOH   233 633 152 HOH   HOH A . 
C 3 HOH   234 634 31  HOH   HOH A . 
C 3 HOH   235 635 78  HOH   HOH A . 
C 3 HOH   236 636 279 HOH   HOH A . 
C 3 HOH   237 637 259 HOH   HOH A . 
C 3 HOH   238 638 237 HOH   HOH A . 
C 3 HOH   239 639 275 HOH   HOH A . 
C 3 HOH   240 640 334 HOH   HOH A . 
C 3 HOH   241 641 153 HOH   HOH A . 
C 3 HOH   242 642 315 HOH   HOH A . 
C 3 HOH   243 643 230 HOH   HOH A . 
C 3 HOH   244 644 97  HOH   HOH A . 
C 3 HOH   245 645 253 HOH   HOH A . 
C 3 HOH   246 646 104 HOH   HOH A . 
C 3 HOH   247 647 336 HOH   HOH A . 
C 3 HOH   248 648 219 HOH   HOH A . 
C 3 HOH   249 649 216 HOH   HOH A . 
C 3 HOH   250 650 146 HOH   HOH A . 
C 3 HOH   251 651 349 HOH   HOH A . 
C 3 HOH   252 652 190 HOH   HOH A . 
C 3 HOH   253 653 95  HOH   HOH A . 
C 3 HOH   254 654 321 HOH   HOH A . 
C 3 HOH   255 655 133 HOH   HOH A . 
C 3 HOH   256 656 213 HOH   HOH A . 
C 3 HOH   257 657 266 HOH   HOH A . 
C 3 HOH   258 658 217 HOH   HOH A . 
C 3 HOH   259 659 208 HOH   HOH A . 
C 3 HOH   260 660 148 HOH   HOH A . 
C 3 HOH   261 661 329 HOH   HOH A . 
C 3 HOH   262 662 225 HOH   HOH A . 
C 3 HOH   263 663 177 HOH   HOH A . 
C 3 HOH   264 664 215 HOH   HOH A . 
C 3 HOH   265 665 345 HOH   HOH A . 
C 3 HOH   266 666 162 HOH   HOH A . 
C 3 HOH   267 667 214 HOH   HOH A . 
C 3 HOH   268 668 173 HOH   HOH A . 
C 3 HOH   269 669 251 HOH   HOH A . 
C 3 HOH   270 670 254 HOH   HOH A . 
C 3 HOH   271 671 218 HOH   HOH A . 
C 3 HOH   272 672 304 HOH   HOH A . 
C 3 HOH   273 673 66  HOH   HOH A . 
C 3 HOH   274 674 127 HOH   HOH A . 
C 3 HOH   275 675 271 HOH   HOH A . 
C 3 HOH   276 676 145 HOH   HOH A . 
C 3 HOH   277 677 194 HOH   HOH A . 
C 3 HOH   278 678 184 HOH   HOH A . 
C 3 HOH   279 679 117 HOH   HOH A . 
C 3 HOH   280 680 236 HOH   HOH A . 
C 3 HOH   281 681 235 HOH   HOH A . 
C 3 HOH   282 682 61  HOH   HOH A . 
C 3 HOH   283 683 223 HOH   HOH A . 
C 3 HOH   284 684 207 HOH   HOH A . 
C 3 HOH   285 685 100 HOH   HOH A . 
C 3 HOH   286 686 226 HOH   HOH A . 
C 3 HOH   287 687 196 HOH   HOH A . 
C 3 HOH   288 688 331 HOH   HOH A . 
C 3 HOH   289 689 280 HOH   HOH A . 
C 3 HOH   290 690 285 HOH   HOH A . 
C 3 HOH   291 691 319 HOH   HOH A . 
C 3 HOH   292 692 281 HOH   HOH A . 
C 3 HOH   293 693 299 HOH   HOH A . 
C 3 HOH   294 694 87  HOH   HOH A . 
C 3 HOH   295 695 239 HOH   HOH A . 
C 3 HOH   296 696 180 HOH   HOH A . 
C 3 HOH   297 697 341 HOH   HOH A . 
C 3 HOH   298 698 193 HOH   HOH A . 
C 3 HOH   299 699 229 HOH   HOH A . 
C 3 HOH   300 700 129 HOH   HOH A . 
C 3 HOH   301 701 175 HOH   HOH A . 
C 3 HOH   302 702 351 HOH   HOH A . 
C 3 HOH   303 703 267 HOH   HOH A . 
C 3 HOH   304 704 211 HOH   HOH A . 
C 3 HOH   305 705 24  HOH   HOH A . 
C 3 HOH   306 706 274 HOH   HOH A . 
C 3 HOH   307 707 276 HOH   HOH A . 
C 3 HOH   308 708 161 HOH   HOH A . 
C 3 HOH   309 709 309 HOH   HOH A . 
C 3 HOH   310 710 168 HOH   HOH A . 
C 3 HOH   311 711 340 HOH   HOH A . 
C 3 HOH   312 712 311 HOH   HOH A . 
C 3 HOH   313 713 199 HOH   HOH A . 
C 3 HOH   314 714 289 HOH   HOH A . 
C 3 HOH   315 715 183 HOH   HOH A . 
C 3 HOH   316 716 205 HOH   HOH A . 
C 3 HOH   317 717 220 HOH   HOH A . 
C 3 HOH   318 718 250 HOH   HOH A . 
C 3 HOH   319 719 149 HOH   HOH A . 
C 3 HOH   320 720 302 HOH   HOH A . 
C 3 HOH   321 721 154 HOH   HOH A . 
C 3 HOH   322 722 350 HOH   HOH A . 
C 3 HOH   323 723 338 HOH   HOH A . 
C 3 HOH   324 724 292 HOH   HOH A . 
C 3 HOH   325 725 328 HOH   HOH A . 
C 3 HOH   326 726 232 HOH   HOH A . 
C 3 HOH   327 727 197 HOH   HOH A . 
C 3 HOH   328 728 323 HOH   HOH A . 
C 3 HOH   329 729 105 HOH   HOH A . 
C 3 HOH   330 730 339 HOH   HOH A . 
C 3 HOH   331 731 260 HOH   HOH A . 
C 3 HOH   332 732 170 HOH   HOH A . 
C 3 HOH   333 733 305 HOH   HOH A . 
C 3 HOH   334 734 263 HOH   HOH A . 
C 3 HOH   335 735 270 HOH   HOH A . 
C 3 HOH   336 736 106 HOH   HOH A . 
C 3 HOH   337 737 115 HOH   HOH A . 
C 3 HOH   338 738 84  HOH   HOH A . 
C 3 HOH   339 739 233 HOH   HOH A . 
C 3 HOH   340 740 165 HOH   HOH A . 
C 3 HOH   341 741 262 HOH   HOH A . 
C 3 HOH   342 742 252 HOH   HOH A . 
C 3 HOH   343 743 344 HOH   HOH A . 
C 3 HOH   344 744 195 HOH   HOH A . 
C 3 HOH   345 745 273 HOH   HOH A . 
C 3 HOH   346 746 261 HOH   HOH A . 
C 3 HOH   347 747 188 HOH   HOH A . 
C 3 HOH   348 748 308 HOH   HOH A . 
C 3 HOH   349 749 346 HOH   HOH A . 
C 3 HOH   350 750 284 HOH   HOH A . 
C 3 HOH   351 751 332 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             591156.094 
_cell.length_a           65.897 
_cell.length_b           89.439 
_cell.length_c           100.302 
_cell.angle_beta         90.000 
_cell.angle_gamma        90.000 
_cell.angle_alpha        90.000 
_cell.entry_id           7H9M 
_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                         7H9M 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
# 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
_exptl.entry_id          7H9M 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_Matthews      2.88 
_exptl_crystal.density_percent_sol   57.23 
_exptl_crystal.density_meas          ? 
_exptl_crystal.description           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.pH              8.5 
_exptl_crystal_grow.temp            277 
_exptl_crystal_grow.pdbx_details    '100mM Tris-HCl pH 8.5, 22% PEG4000, 200mM MgCl2' 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_diffrn.id                     1 
_diffrn.crystal_id             1 
_diffrn.ambient_temp           100 
_diffrn.ambient_temp_details   ? 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               PIXEL 
_diffrn_detector.type                   'DECTRIS EIGER2 S 9M' 
_diffrn_detector.pdbx_collection_date   2023-07-05 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.pdbx_scattering_type             x-ray 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.monochromator                    Si111 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.97918 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.pdbx_synchrotron_beamline   BL02U1 
_diffrn_source.type                        'SSRF BEAMLINE BL02U1' 
_diffrn_source.pdbx_wavelength_list        0.97918 
_diffrn_source.pdbx_synchrotron_site       SSRF 
_diffrn_source.pdbx_wavelength             ? 
# 
_reflns.entry_id                     7H9M 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             66.750 
_reflns.d_resolution_high            1.490 
_reflns.number_obs                   45869 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         93.600 
_reflns.pdbx_Rmerge_I_obs            0.043 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        30.900 
_reflns.B_iso_Wilson_estimate        ? 
_reflns.pdbx_redundancy              11.900 
_reflns.pdbx_Rrim_I_all              0.045 
_reflns.pdbx_Rpim_I_all              0.013 
_reflns.pdbx_CC_half                 1.000 
_reflns.pdbx_netI_over_av_sigmaI     ? 
_reflns.pdbx_number_measured_all     545940 
_reflns.pdbx_scaling_rejects         2 
_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 1.490 1.570  ? 37240 4706 ? 0.470 ? ? ? 7.900  ? 3.300  ? ? ? ? ? ? 67.000 0.503 0.171 0.897 
1 2 4.700 66.750 ? 19779 1666 ? 0.026 ? ? ? 11.900 ? 82.100 ? ? ? ? ? ? 99.400 0.028 0.008 0.999 
# 
_refine.entry_id                                 7H9M 
_refine.pdbx_method_to_determine_struct          'FOURIER SYNTHESIS' 
_refine.ls_percent_reflns_R_free                 4.99 
_refine.pdbx_overall_phase_error                 19.1057 
_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                          0.1685 
_refine.B_iso_mean                               26.44 
_refine.ls_number_reflns_R_free                  2288 
_refine.ls_percent_reflns_obs                    93.24 
_refine.ls_R_factor_R_work                       0.1679 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_refine.ls_d_res_high                            1.49 
_refine.ls_number_reflns_obs                     45823 
_refine.pdbx_ls_sigma_F                          1.33 
_refine.ls_number_reflns_R_work                  43535 
_refine.ls_d_res_low                             29.55 
_refine.pdbx_stereochemistry_target_values       'GeoStd + Monomer Library + CDL v1.2' 
_refine.ls_R_factor_R_free                       0.1800 
_refine.overall_SU_ML                            0.1519 
_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         17 
_refine_hist.number_atoms_solvent             351 
_refine_hist.number_atoms_total               2012 
_refine_hist.d_res_high                       1.49 
_refine_hist.d_res_low                        29.55 
# 
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           1688 0.0037 ? ? ? 
'X-RAY DIFFRACTION' f_angle_d          2277 0.7368 ? ? ? 
'X-RAY DIFFRACTION' f_chiral_restr     260  0.0707 ? ? ? 
'X-RAY DIFFRACTION' f_plane_restr      291  0.0049 ? ? ? 
'X-RAY DIFFRACTION' f_dihedral_angle_d 229  7.7610 ? ? ? 
# 
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' 1.49 1.52  1736 0.2329 60.16 0.2616 96  . . . . . 
'X-RAY DIFFRACTION' 1.52 1.55  1987 0.2064 69.40 0.2335 106 . . . . . 
'X-RAY DIFFRACTION' 1.55 1.59  2402 0.1980 82.67 0.2016 121 . . . . . 
'X-RAY DIFFRACTION' 1.59 1.63  2774 0.1871 96.40 0.2117 146 . . . . . 
'X-RAY DIFFRACTION' 1.63 1.68  2803 0.2120 97.39 0.2388 149 . . . . . 
'X-RAY DIFFRACTION' 1.68 1.74  2856 0.2072 97.81 0.2221 135 . . . . . 
'X-RAY DIFFRACTION' 1.74 1.80  2816 0.1896 97.71 0.2209 134 . . . . . 
'X-RAY DIFFRACTION' 1.80 1.87  2898 0.1774 98.22 0.2284 135 . . . . . 
'X-RAY DIFFRACTION' 1.87 1.96  2799 0.1863 97.72 0.2033 164 . . . . . 
'X-RAY DIFFRACTION' 1.96 2.06  2858 0.1770 98.56 0.1743 155 . . . . . 
'X-RAY DIFFRACTION' 2.06 2.19  2868 0.1579 98.83 0.1841 165 . . . . . 
'X-RAY DIFFRACTION' 2.19 2.36  2876 0.1711 98.44 0.1999 156 . . . . . 
'X-RAY DIFFRACTION' 2.36 2.59  2893 0.1683 99.22 0.1721 160 . . . . . 
'X-RAY DIFFRACTION' 2.59 2.97  2933 0.1677 99.32 0.1541 151 . . . . . 
'X-RAY DIFFRACTION' 2.97 3.74  2972 0.1562 99.55 0.1723 149 . . . . . 
'X-RAY DIFFRACTION' 3.74 29.55 3064 0.1506 99.51 0.1586 166 . . . . . 
# 
_struct.entry_id                  7H9M 
_struct.title                     'PanDDA analysis group deposition -- Crystal structure of HSP90N in complex with Fr13527' 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_details        ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7H9M 
_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              7H9M 
_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 7H9M MET A 1   ? UNP P07900 ? ? 'initiating methionine' 8   1 
1 7H9M LEU A 230 ? UNP P07900 ? ? 'expression tag'        237 2 
1 7H9M GLU A 231 ? UNP P07900 ? ? 'expression tag'        238 3 
1 7H9M HIS A 232 ? UNP P07900 ? ? 'expression tag'        239 4 
1 7H9M HIS A 233 ? UNP P07900 ? ? 'expression tag'        240 5 
1 7H9M HIS A 234 ? UNP P07900 ? ? 'expression tag'        241 6 
1 7H9M HIS A 235 ? UNP P07900 ? ? 'expression tag'        242 7 
1 7H9M HIS A 236 ? UNP P07900 ? ? 'expression tag'        243 8 
1 7H9M 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 ASN A 99  ? THR A 102 ? ASN A 106 THR A 109 5 ? 4  
HELX_P HELX_P6  AA6 ILE A 103 ? GLN A 116 ? ILE A 110 GLN A 123 1 ? 14 
HELX_P HELX_P7  AA7 ASP A 120 ? GLY A 128 ? ASP A 127 GLY A 135 5 ? 9  
HELX_P HELX_P8  AA8 VAL A 129 ? LEU A 136 ? VAL A 136 LEU A 143 5 ? 8  
HELX_P HELX_P9  AA9 GLU A 185 ? LEU A 191 ? GLU A 192 LEU A 198 5 ? 7  
HELX_P HELX_P10 AB1 GLU A 192 ? SER A 204 ? GLU A 199 SER A 211 1 ? 13 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
_struct_sheet.id               AA1 
_struct_sheet.type             ? 
_struct_sheet.number_strands   8 
_struct_sheet.details          ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA1 5 6 ? anti-parallel 
AA1 6 7 ? anti-parallel 
AA1 7 8 ? parallel      
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 GLU A 11  ? ALA A 14  ? GLU A 18  ALA A 21  
AA1 2 SER A 162 ? THR A 167 ? SER A 169 THR A 174 
AA1 3 TYR A 153 ? SER A 157 ? TYR A 160 SER A 164 
AA1 4 ALA A 138 ? LYS A 146 ? ALA A 145 LYS A 153 
AA1 5 GLY A 176 ? LEU A 183 ? GLY A 183 LEU A 190 
AA1 6 THR A 81  ? ASP A 86  ? THR A 88  ASP A 93  
AA1 7 ILE A 71  ? ASN A 76  ? ILE A 78  ASN A 83  
AA1 8 ILE A 211 ? LEU A 213 ? ILE A 218 LEU A 220 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N PHE A 13  ? N PHE A 20  O PHE A 163 ? O PHE A 170 
AA1 2 3 O ARG A 166 ? O ARG A 173 N ALA A 154 ? N ALA A 161 
AA1 3 4 O TRP A 155 ? O TRP A 162 N VAL A 143 ? N VAL A 150 
AA1 4 5 N THR A 142 ? N THR A 149 O ILE A 180 ? O ILE A 187 
AA1 5 6 O LEU A 181 ? O LEU A 188 N LEU A 82  ? N LEU A 89  
AA1 6 7 O VAL A 85  ? O VAL A 92  N ASN A 72  ? N ASN A 79  
AA1 7 8 N LEU A 73  ? N LEU A 80  O THR A 212 ? O THR A 219 
# 
_pdbx_entry_details.entry_id                   7H9M 
_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 688 ? ? O A HOH 691 ? ? 1.82 
2 1 O   A GLU 120 ? ? O A HOH 401 ? ? 2.03 
3 1 O   A HOH 703 ? ? O A HOH 746 ? ? 2.03 
4 1 O   A HOH 636 ? ? O A HOH 689 ? ? 2.07 
5 1 O   A HOH 686 ? ? O A HOH 709 ? ? 2.12 
6 1 O   A HOH 426 ? ? O A HOH 628 ? ? 2.17 
7 1 OD1 A ASP 71  ? ? O A HOH 402 ? ? 2.18 
8 1 O   A HOH 519 ? ? O A HOH 622 ? ? 2.18 
9 1 N   A ALA 124 ? ? O A HOH 401 ? ? 2.19 
# 
_pdbx_validate_symm_contact.id                1 
_pdbx_validate_symm_contact.PDB_model_num     1 
_pdbx_validate_symm_contact.auth_atom_id_1    O 
_pdbx_validate_symm_contact.auth_asym_id_1    A 
_pdbx_validate_symm_contact.auth_comp_id_1    HOH 
_pdbx_validate_symm_contact.auth_seq_id_1     517 
_pdbx_validate_symm_contact.PDB_ins_code_1    ? 
_pdbx_validate_symm_contact.label_alt_id_1    ? 
_pdbx_validate_symm_contact.site_symmetry_1   1_555 
_pdbx_validate_symm_contact.auth_atom_id_2    O 
_pdbx_validate_symm_contact.auth_asym_id_2    A 
_pdbx_validate_symm_contact.auth_comp_id_2    HOH 
_pdbx_validate_symm_contact.auth_seq_id_2     599 
_pdbx_validate_symm_contact.PDB_ins_code_2    ? 
_pdbx_validate_symm_contact.label_alt_id_2    ? 
_pdbx_validate_symm_contact.site_symmetry_2   3_555 
_pdbx_validate_symm_contact.dist              2.04 
# 
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  ? ? -161.18 109.90  
2 1 THR A 94  ? ? -103.63 40.11   
3 1 ALA A 166 ? ? 62.79   -141.88 
# 
_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     705 
_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 12.3496482066  -17.848740633  -18.7243241726 0.111089286821 0.145717123367  0.151151759076 
0.0124143185627   -0.0210285678551   -0.0235038099857  2.91831277933  0.932327503413 6.31422437954 -0.920292751022  -3.40807456653 
0.509945043813  0.113299352448    -0.219709741889  -0.0142804423678 0.0196238564879 -0.0552746849877  -0.052072882371  
0.0243988298762  0.276628393748   -0.102626243675  
2  ? 'X-RAY DIFFRACTION' refined -5.21371660986 -6.30128837003 -20.8683956635 0.12399466632  0.120263761814  0.159973327972 
-0.00458234475925 -0.00573552040746  -0.0347188595649  2.05128753872  5.83663396311  8.46016265035 -2.42817680098   3.05006422768 
-5.90083822723  -0.0423234882367  0.0312919105025  0.111480375564   0.0973027088825 -0.00897047699718 0.0835205927408  
-0.301667481045  0.0964663076013  0.0534398634529  
3  ? 'X-RAY DIFFRACTION' refined -13.6354402389 -10.8011626076 -28.0295328892 0.152545039749 0.184237884139  0.21336799547  
0.0111219313912   -0.0527627425216   -0.0239031358543  1.28995509032  4.8230461433   7.07601225168 -0.631702732942  0.313331144444 
-4.84040556992  0.07937473625     0.185259384588   -0.0377842678835 -0.222004048595 0.134849672803    0.373694035976   
-0.0896294066353 -0.37033389836   -0.334992232146  
4  ? 'X-RAY DIFFRACTION' refined -6.00987822071 -19.8269218699 -21.8740393001 0.146798493301 0.113681713294  0.168160862157 
0.00305770122461  -0.0242252465316   -0.0427209282288  2.21178791163  4.19302496379  6.42966594929 -0.0428994114571 
-0.689689676933 -4.0348859408   -0.0325209637477  -0.0565691634495 -0.190025243846  -0.202020882348 0.109981605904    
0.17834753934    0.366466638314   -0.0273426877397 -0.0955360306119 
5  ? 'X-RAY DIFFRACTION' refined 6.92805717399  -10.9915614755 -29.7080869403 0.179211101129 0.161896680622  0.224781777225 
0.0144230034551   0.00499911265838   -0.0065792770496  4.23430995572  5.86503579588  4.48415179815 2.3782340782     3.37726469188 
4.71997484409   -0.00852234755057 0.0959712082631  0.19687988298    -0.307071339829 -0.208129676252   -0.0111889683559 
-0.180520744815  0.00626973540111 0.176767294739   
6  ? 'X-RAY DIFFRACTION' refined 12.3438207283  -5.95843055662 -12.6117753677 0.226722384374 0.463520489135  0.324823678633 
-0.105248751184   0.0319268645012    -0.152200084489   0.791545636147 2.51669019872  4.4630383654  0.728085811197   1.23446980617 
0.610515492882  0.567071626504    -1.10478428036   0.863752945405   0.254419998587  -0.073334622449   -0.241801962767  
-0.624090829412  1.24365520442    -0.217587558466  
7  ? 'X-RAY DIFFRACTION' refined 0.927334676904 -19.2595782197 -27.8597710503 0.144398232059 0.114155140125  0.160622212093 
-0.00314555047613 -0.0158432890912   -0.0308416372021  2.64294531251  1.61738947599  2.55287270639 -1.1102485087    0.626638113131 
-0.439189581931 0.124630877449    0.19307290836    -0.214863765164  -0.182571439997 -0.0500422717296  0.125160414203   
0.185484524965   0.0427467753203  -0.0982661149369 
8  ? 'X-RAY DIFFRACTION' refined -2.51709481637 -23.6877788874 -13.725309427  0.127088816357 0.0935189762806 0.170957725267 
-0.0178174308169  -0.0132382830494   -0.00775289162384 4.05702144999  5.5052555257   8.31171001824 -1.38237424062   0.55563516621 
-3.88172518171  0.029856061539    -0.255339668133  -0.318157431854  0.137685428651  -0.0532057335908  -0.0109541584009 
0.379400213182   0.244869868825   0.00784132759975 
9  ? 'X-RAY DIFFRACTION' refined -9.91601279062 -15.2603091543 -5.64126675023 0.161041346135 0.220126218239  0.11233222269  
0.00507851514714  -0.000212523612459 -0.00233392282376 7.70334043435  8.13737936712  2.14510857938 -0.180697241615  -1.42159546543 
-3.11920665197  -0.0202955386791  -0.341952253604  -0.139185478682  0.240290605368  0.197268432511    0.303255474846   
-0.110312028602  -0.117866008177  -0.153323002219  
10 ? 'X-RAY DIFFRACTION' refined -13.9371448861 -13.4252342519 -14.7061908895 0.106569223196 0.149138823889  0.109901564544 
0.0102998288558   0.0001976968216    -0.0220720705062  4.47344678658  1.79510156548  4.3642633519  -0.300218449742  
-0.376052910704 -1.50561821044  -0.014598113281   -0.229960027288  -0.0720972496755 0.360674047006  0.0729240004025   
0.0307885338896  -0.140057938866  -0.122998903116  -0.0492394528381 
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
1  1  'X-RAY DIFFRACTION' A 16  A 1   A 40  A 25  . 
;chain 'A' and (resid 16 through 40 )
;
2  2  'X-RAY DIFFRACTION' A 41  A 26  A 65  A 50  . 
;chain 'A' and (resid 41 through 65 )
;
3  3  'X-RAY DIFFRACTION' A 66  A 51  A 83  A 68  . 
;chain 'A' and (resid 66 through 83 )
;
4  4  'X-RAY DIFFRACTION' A 84  A 69  A 99  A 84  . 
;chain 'A' and (resid 84 through 99 )
;
5  5  'X-RAY DIFFRACTION' A 100 A 85  A 110 A 95  . 
;chain 'A' and (resid 100 through 110 )
;
6  6  'X-RAY DIFFRACTION' A 111 A 96  A 136 A 121 . 
;chain 'A' and (resid 111 through 136 )
;
7  7  'X-RAY DIFFRACTION' A 137 A 122 A 182 A 167 . 
;chain 'A' and (resid 137 through 182 )
;
8  8  'X-RAY DIFFRACTION' A 183 A 168 A 199 A 184 . 
;chain 'A' and (resid 183 through 199 )
;
9  9  'X-RAY DIFFRACTION' A 200 A 185 A 210 A 195 . 
;chain 'A' and (resid 200 through 210 )
;
10 10 'X-RAY DIFFRACTION' A 211 A 196 A 224 A 209 . 
;chain 'A' and (resid 211 through 224 )
;
# 
loop_
_pdbx_distant_solvent_atoms.id 
_pdbx_distant_solvent_atoms.PDB_model_num 
_pdbx_distant_solvent_atoms.auth_atom_id 
_pdbx_distant_solvent_atoms.label_alt_id 
_pdbx_distant_solvent_atoms.auth_asym_id 
_pdbx_distant_solvent_atoms.auth_comp_id 
_pdbx_distant_solvent_atoms.auth_seq_id 
_pdbx_distant_solvent_atoms.PDB_ins_code 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance 
1 1 O ? A HOH 748 ? 5.83 . 
2 1 O ? A HOH 749 ? 5.91 . 
3 1 O ? A HOH 750 ? 6.02 . 
4 1 O ? A HOH 751 ? 6.74 . 
# 
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 
A1AW8 C1   C N N 1   
A1AW8 C2   C N N 2   
A1AW8 C3   C N N 3   
A1AW8 C4   C N N 4   
A1AW8 C5   C N N 5   
A1AW8 C6   C N N 6   
A1AW8 C7   C Y N 7   
A1AW8 N1   N N N 8   
A1AW8 O2   O N N 9   
A1AW8 C10  C Y N 10  
A1AW8 C11  C Y N 11  
A1AW8 C12  C Y N 12  
A1AW8 C8   C Y N 13  
A1AW8 C9   C Y N 14  
A1AW8 F1   F N N 15  
A1AW8 F2   F N N 16  
A1AW8 O1   O N N 17  
A1AW8 H12  H N N 18  
A1AW8 H14  H N N 19  
A1AW8 H13  H N N 20  
A1AW8 H2   H N N 21  
A1AW8 H33  H N N 22  
A1AW8 H32  H N N 23  
A1AW8 H62  H N N 24  
A1AW8 H63  H N N 25  
A1AW8 H11  H N N 26  
A1AW8 H8   H N N 27  
A1AW8 H9   H N N 28  
ALA   N    N N N 29  
ALA   CA   C N S 30  
ALA   C    C N N 31  
ALA   O    O N N 32  
ALA   CB   C N N 33  
ALA   OXT  O N N 34  
ALA   H    H N N 35  
ALA   H2   H N N 36  
ALA   HA   H N N 37  
ALA   HB1  H N N 38  
ALA   HB2  H N N 39  
ALA   HB3  H N N 40  
ALA   HXT  H N N 41  
ARG   N    N N N 42  
ARG   CA   C N S 43  
ARG   C    C N N 44  
ARG   O    O N N 45  
ARG   CB   C N N 46  
ARG   CG   C N N 47  
ARG   CD   C N N 48  
ARG   NE   N N N 49  
ARG   CZ   C N N 50  
ARG   NH1  N N N 51  
ARG   NH2  N N N 52  
ARG   OXT  O N N 53  
ARG   H    H N N 54  
ARG   H2   H N N 55  
ARG   HA   H N N 56  
ARG   HB2  H N N 57  
ARG   HB3  H N N 58  
ARG   HG2  H N N 59  
ARG   HG3  H N N 60  
ARG   HD2  H N N 61  
ARG   HD3  H N N 62  
ARG   HE   H N N 63  
ARG   HH11 H N N 64  
ARG   HH12 H N N 65  
ARG   HH21 H N N 66  
ARG   HH22 H N N 67  
ARG   HXT  H N N 68  
ASN   N    N N N 69  
ASN   CA   C N S 70  
ASN   C    C N N 71  
ASN   O    O N N 72  
ASN   CB   C N N 73  
ASN   CG   C N N 74  
ASN   OD1  O N N 75  
ASN   ND2  N N N 76  
ASN   OXT  O N N 77  
ASN   H    H N N 78  
ASN   H2   H N N 79  
ASN   HA   H N N 80  
ASN   HB2  H N N 81  
ASN   HB3  H N N 82  
ASN   HD21 H N N 83  
ASN   HD22 H N N 84  
ASN   HXT  H N N 85  
ASP   N    N N N 86  
ASP   CA   C N S 87  
ASP   C    C N N 88  
ASP   O    O N N 89  
ASP   CB   C N N 90  
ASP   CG   C N N 91  
ASP   OD1  O N N 92  
ASP   OD2  O N N 93  
ASP   OXT  O N N 94  
ASP   H    H N N 95  
ASP   H2   H N N 96  
ASP   HA   H N N 97  
ASP   HB2  H N N 98  
ASP   HB3  H N N 99  
ASP   HD2  H N N 100 
ASP   HXT  H N N 101 
GLN   N    N N N 102 
GLN   CA   C N S 103 
GLN   C    C N N 104 
GLN   O    O N N 105 
GLN   CB   C N N 106 
GLN   CG   C N N 107 
GLN   CD   C N N 108 
GLN   OE1  O N N 109 
GLN   NE2  N N N 110 
GLN   OXT  O N N 111 
GLN   H    H N N 112 
GLN   H2   H N N 113 
GLN   HA   H N N 114 
GLN   HB2  H N N 115 
GLN   HB3  H N N 116 
GLN   HG2  H N N 117 
GLN   HG3  H N N 118 
GLN   HE21 H N N 119 
GLN   HE22 H N N 120 
GLN   HXT  H N N 121 
GLU   N    N N N 122 
GLU   CA   C N S 123 
GLU   C    C N N 124 
GLU   O    O N N 125 
GLU   CB   C N N 126 
GLU   CG   C N N 127 
GLU   CD   C N N 128 
GLU   OE1  O N N 129 
GLU   OE2  O N N 130 
GLU   OXT  O N N 131 
GLU   H    H N N 132 
GLU   H2   H N N 133 
GLU   HA   H N N 134 
GLU   HB2  H N N 135 
GLU   HB3  H N N 136 
GLU   HG2  H N N 137 
GLU   HG3  H N N 138 
GLU   HE2  H N N 139 
GLU   HXT  H N N 140 
GLY   N    N N N 141 
GLY   CA   C N N 142 
GLY   C    C N N 143 
GLY   O    O N N 144 
GLY   OXT  O N N 145 
GLY   H    H N N 146 
GLY   H2   H N N 147 
GLY   HA2  H N N 148 
GLY   HA3  H N N 149 
GLY   HXT  H N N 150 
HIS   N    N N N 151 
HIS   CA   C N S 152 
HIS   C    C N N 153 
HIS   O    O N N 154 
HIS   CB   C N N 155 
HIS   CG   C Y N 156 
HIS   ND1  N Y N 157 
HIS   CD2  C Y N 158 
HIS   CE1  C Y N 159 
HIS   NE2  N Y N 160 
HIS   OXT  O N N 161 
HIS   H    H N N 162 
HIS   H2   H N N 163 
HIS   HA   H N N 164 
HIS   HB2  H N N 165 
HIS   HB3  H N N 166 
HIS   HD1  H N N 167 
HIS   HD2  H N N 168 
HIS   HE1  H N N 169 
HIS   HE2  H N N 170 
HIS   HXT  H N N 171 
HOH   O    O N N 172 
HOH   H1   H N N 173 
HOH   H2   H N N 174 
ILE   N    N N N 175 
ILE   CA   C N S 176 
ILE   C    C N N 177 
ILE   O    O N N 178 
ILE   CB   C N S 179 
ILE   CG1  C N N 180 
ILE   CG2  C N N 181 
ILE   CD1  C N N 182 
ILE   OXT  O N N 183 
ILE   H    H N N 184 
ILE   H2   H N N 185 
ILE   HA   H N N 186 
ILE   HB   H N N 187 
ILE   HG12 H N N 188 
ILE   HG13 H N N 189 
ILE   HG21 H N N 190 
ILE   HG22 H N N 191 
ILE   HG23 H N N 192 
ILE   HD11 H N N 193 
ILE   HD12 H N N 194 
ILE   HD13 H N N 195 
ILE   HXT  H N N 196 
LEU   N    N N N 197 
LEU   CA   C N S 198 
LEU   C    C N N 199 
LEU   O    O N N 200 
LEU   CB   C N N 201 
LEU   CG   C N N 202 
LEU   CD1  C N N 203 
LEU   CD2  C N N 204 
LEU   OXT  O N N 205 
LEU   H    H N N 206 
LEU   H2   H N N 207 
LEU   HA   H N N 208 
LEU   HB2  H N N 209 
LEU   HB3  H N N 210 
LEU   HG   H N N 211 
LEU   HD11 H N N 212 
LEU   HD12 H N N 213 
LEU   HD13 H N N 214 
LEU   HD21 H N N 215 
LEU   HD22 H N N 216 
LEU   HD23 H N N 217 
LEU   HXT  H N N 218 
LYS   N    N N N 219 
LYS   CA   C N S 220 
LYS   C    C N N 221 
LYS   O    O N N 222 
LYS   CB   C N N 223 
LYS   CG   C N N 224 
LYS   CD   C N N 225 
LYS   CE   C N N 226 
LYS   NZ   N N N 227 
LYS   OXT  O N N 228 
LYS   H    H N N 229 
LYS   H2   H N N 230 
LYS   HA   H N N 231 
LYS   HB2  H N N 232 
LYS   HB3  H N N 233 
LYS   HG2  H N N 234 
LYS   HG3  H N N 235 
LYS   HD2  H N N 236 
LYS   HD3  H N N 237 
LYS   HE2  H N N 238 
LYS   HE3  H N N 239 
LYS   HZ1  H N N 240 
LYS   HZ2  H N N 241 
LYS   HZ3  H N N 242 
LYS   HXT  H N N 243 
MET   N    N N N 244 
MET   CA   C N S 245 
MET   C    C N N 246 
MET   O    O N N 247 
MET   CB   C N N 248 
MET   CG   C N N 249 
MET   SD   S N N 250 
MET   CE   C N N 251 
MET   OXT  O N N 252 
MET   H    H N N 253 
MET   H2   H N N 254 
MET   HA   H N N 255 
MET   HB2  H N N 256 
MET   HB3  H N N 257 
MET   HG2  H N N 258 
MET   HG3  H N N 259 
MET   HE1  H N N 260 
MET   HE2  H N N 261 
MET   HE3  H N N 262 
MET   HXT  H N N 263 
PHE   N    N N N 264 
PHE   CA   C N S 265 
PHE   C    C N N 266 
PHE   O    O N N 267 
PHE   CB   C N N 268 
PHE   CG   C Y N 269 
PHE   CD1  C Y N 270 
PHE   CD2  C Y N 271 
PHE   CE1  C Y N 272 
PHE   CE2  C Y N 273 
PHE   CZ   C Y N 274 
PHE   OXT  O N N 275 
PHE   H    H N N 276 
PHE   H2   H N N 277 
PHE   HA   H N N 278 
PHE   HB2  H N N 279 
PHE   HB3  H N N 280 
PHE   HD1  H N N 281 
PHE   HD2  H N N 282 
PHE   HE1  H N N 283 
PHE   HE2  H N N 284 
PHE   HZ   H N N 285 
PHE   HXT  H N N 286 
PRO   N    N N N 287 
PRO   CA   C N S 288 
PRO   C    C N N 289 
PRO   O    O N N 290 
PRO   CB   C N N 291 
PRO   CG   C N N 292 
PRO   CD   C N N 293 
PRO   OXT  O N N 294 
PRO   H    H N N 295 
PRO   HA   H N N 296 
PRO   HB2  H N N 297 
PRO   HB3  H N N 298 
PRO   HG2  H N N 299 
PRO   HG3  H N N 300 
PRO   HD2  H N N 301 
PRO   HD3  H N N 302 
PRO   HXT  H N N 303 
SER   N    N N N 304 
SER   CA   C N S 305 
SER   C    C N N 306 
SER   O    O N N 307 
SER   CB   C N N 308 
SER   OG   O N N 309 
SER   OXT  O N N 310 
SER   H    H N N 311 
SER   H2   H N N 312 
SER   HA   H N N 313 
SER   HB2  H N N 314 
SER   HB3  H N N 315 
SER   HG   H N N 316 
SER   HXT  H N N 317 
THR   N    N N N 318 
THR   CA   C N S 319 
THR   C    C N N 320 
THR   O    O N N 321 
THR   CB   C N R 322 
THR   OG1  O N N 323 
THR   CG2  C N N 324 
THR   OXT  O N N 325 
THR   H    H N N 326 
THR   H2   H N N 327 
THR   HA   H N N 328 
THR   HB   H N N 329 
THR   HG1  H N N 330 
THR   HG21 H N N 331 
THR   HG22 H N N 332 
THR   HG23 H N N 333 
THR   HXT  H N N 334 
TRP   N    N N N 335 
TRP   CA   C N S 336 
TRP   C    C N N 337 
TRP   O    O N N 338 
TRP   CB   C N N 339 
TRP   CG   C Y N 340 
TRP   CD1  C Y N 341 
TRP   CD2  C Y N 342 
TRP   NE1  N Y N 343 
TRP   CE2  C Y N 344 
TRP   CE3  C Y N 345 
TRP   CZ2  C Y N 346 
TRP   CZ3  C Y N 347 
TRP   CH2  C Y N 348 
TRP   OXT  O N N 349 
TRP   H    H N N 350 
TRP   H2   H N N 351 
TRP   HA   H N N 352 
TRP   HB2  H N N 353 
TRP   HB3  H N N 354 
TRP   HD1  H N N 355 
TRP   HE1  H N N 356 
TRP   HE3  H N N 357 
TRP   HZ2  H N N 358 
TRP   HZ3  H N N 359 
TRP   HH2  H N N 360 
TRP   HXT  H N N 361 
TYR   N    N N N 362 
TYR   CA   C N S 363 
TYR   C    C N N 364 
TYR   O    O N N 365 
TYR   CB   C N N 366 
TYR   CG   C Y N 367 
TYR   CD1  C Y N 368 
TYR   CD2  C Y N 369 
TYR   CE1  C Y N 370 
TYR   CE2  C Y N 371 
TYR   CZ   C Y N 372 
TYR   OH   O N N 373 
TYR   OXT  O N N 374 
TYR   H    H N N 375 
TYR   H2   H N N 376 
TYR   HA   H N N 377 
TYR   HB2  H N N 378 
TYR   HB3  H N N 379 
TYR   HD1  H N N 380 
TYR   HD2  H N N 381 
TYR   HE1  H N N 382 
TYR   HE2  H N N 383 
TYR   HH   H N N 384 
TYR   HXT  H N N 385 
VAL   N    N N N 386 
VAL   CA   C N S 387 
VAL   C    C N N 388 
VAL   O    O N N 389 
VAL   CB   C N N 390 
VAL   CG1  C N N 391 
VAL   CG2  C N N 392 
VAL   OXT  O N N 393 
VAL   H    H N N 394 
VAL   H2   H N N 395 
VAL   HA   H N N 396 
VAL   HB   H N N 397 
VAL   HG11 H N N 398 
VAL   HG12 H N N 399 
VAL   HG13 H N N 400 
VAL   HG21 H N N 401 
VAL   HG22 H N N 402 
VAL   HG23 H N N 403 
VAL   HXT  H N N 404 
# 
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 
A1AW8 C1  C2   sing N N 1   
A1AW8 C2  C3   sing N N 2   
A1AW8 C2  C6   sing N N 3   
A1AW8 C3  C4   sing N N 4   
A1AW8 C4  O1   doub N N 5   
A1AW8 C4  N1   sing N N 6   
A1AW8 N1  C5   sing N N 7   
A1AW8 N1  C7   sing N N 8   
A1AW8 C5  O2   doub N N 9   
A1AW8 C5  C6   sing N N 10  
A1AW8 C7  C8   doub Y N 11  
A1AW8 C7  C12  sing Y N 12  
A1AW8 C8  C9   sing Y N 13  
A1AW8 C9  C10  doub Y N 14  
A1AW8 C10 F1   sing N N 15  
A1AW8 C10 C11  sing Y N 16  
A1AW8 C11 C12  doub Y N 17  
A1AW8 C12 F2   sing N N 18  
A1AW8 C1  H12  sing N N 19  
A1AW8 C1  H14  sing N N 20  
A1AW8 C1  H13  sing N N 21  
A1AW8 C2  H2   sing N N 22  
A1AW8 C3  H33  sing N N 23  
A1AW8 C3  H32  sing N N 24  
A1AW8 C6  H62  sing N N 25  
A1AW8 C6  H63  sing N N 26  
A1AW8 C11 H11  sing N N 27  
A1AW8 C8  H8   sing N N 28  
A1AW8 C9  H9   sing N N 29  
ALA   N   CA   sing N N 30  
ALA   N   H    sing N N 31  
ALA   N   H2   sing N N 32  
ALA   CA  C    sing N N 33  
ALA   CA  CB   sing N N 34  
ALA   CA  HA   sing N N 35  
ALA   C   O    doub N N 36  
ALA   C   OXT  sing N N 37  
ALA   CB  HB1  sing N N 38  
ALA   CB  HB2  sing N N 39  
ALA   CB  HB3  sing N N 40  
ALA   OXT HXT  sing N N 41  
ARG   N   CA   sing N N 42  
ARG   N   H    sing N N 43  
ARG   N   H2   sing N N 44  
ARG   CA  C    sing N N 45  
ARG   CA  CB   sing N N 46  
ARG   CA  HA   sing N N 47  
ARG   C   O    doub N N 48  
ARG   C   OXT  sing N N 49  
ARG   CB  CG   sing N N 50  
ARG   CB  HB2  sing N N 51  
ARG   CB  HB3  sing N N 52  
ARG   CG  CD   sing N N 53  
ARG   CG  HG2  sing N N 54  
ARG   CG  HG3  sing N N 55  
ARG   CD  NE   sing N N 56  
ARG   CD  HD2  sing N N 57  
ARG   CD  HD3  sing N N 58  
ARG   NE  CZ   sing N N 59  
ARG   NE  HE   sing N N 60  
ARG   CZ  NH1  sing N N 61  
ARG   CZ  NH2  doub N N 62  
ARG   NH1 HH11 sing N N 63  
ARG   NH1 HH12 sing N N 64  
ARG   NH2 HH21 sing N N 65  
ARG   NH2 HH22 sing N N 66  
ARG   OXT HXT  sing N N 67  
ASN   N   CA   sing N N 68  
ASN   N   H    sing N N 69  
ASN   N   H2   sing N N 70  
ASN   CA  C    sing N N 71  
ASN   CA  CB   sing N N 72  
ASN   CA  HA   sing N N 73  
ASN   C   O    doub N N 74  
ASN   C   OXT  sing N N 75  
ASN   CB  CG   sing N N 76  
ASN   CB  HB2  sing N N 77  
ASN   CB  HB3  sing N N 78  
ASN   CG  OD1  doub N N 79  
ASN   CG  ND2  sing N N 80  
ASN   ND2 HD21 sing N N 81  
ASN   ND2 HD22 sing N N 82  
ASN   OXT HXT  sing N N 83  
ASP   N   CA   sing N N 84  
ASP   N   H    sing N N 85  
ASP   N   H2   sing N N 86  
ASP   CA  C    sing N N 87  
ASP   CA  CB   sing N N 88  
ASP   CA  HA   sing N N 89  
ASP   C   O    doub N N 90  
ASP   C   OXT  sing N N 91  
ASP   CB  CG   sing N N 92  
ASP   CB  HB2  sing N N 93  
ASP   CB  HB3  sing N N 94  
ASP   CG  OD1  doub N N 95  
ASP   CG  OD2  sing N N 96  
ASP   OD2 HD2  sing N N 97  
ASP   OXT HXT  sing N N 98  
GLN   N   CA   sing N N 99  
GLN   N   H    sing N N 100 
GLN   N   H2   sing N N 101 
GLN   CA  C    sing N N 102 
GLN   CA  CB   sing N N 103 
GLN   CA  HA   sing N N 104 
GLN   C   O    doub N N 105 
GLN   C   OXT  sing N N 106 
GLN   CB  CG   sing N N 107 
GLN   CB  HB2  sing N N 108 
GLN   CB  HB3  sing N N 109 
GLN   CG  CD   sing N N 110 
GLN   CG  HG2  sing N N 111 
GLN   CG  HG3  sing N N 112 
GLN   CD  OE1  doub N N 113 
GLN   CD  NE2  sing N N 114 
GLN   NE2 HE21 sing N N 115 
GLN   NE2 HE22 sing N N 116 
GLN   OXT HXT  sing N N 117 
GLU   N   CA   sing N N 118 
GLU   N   H    sing N N 119 
GLU   N   H2   sing N N 120 
GLU   CA  C    sing N N 121 
GLU   CA  CB   sing N N 122 
GLU   CA  HA   sing N N 123 
GLU   C   O    doub N N 124 
GLU   C   OXT  sing N N 125 
GLU   CB  CG   sing N N 126 
GLU   CB  HB2  sing N N 127 
GLU   CB  HB3  sing N N 128 
GLU   CG  CD   sing N N 129 
GLU   CG  HG2  sing N N 130 
GLU   CG  HG3  sing N N 131 
GLU   CD  OE1  doub N N 132 
GLU   CD  OE2  sing N N 133 
GLU   OE2 HE2  sing N N 134 
GLU   OXT HXT  sing N N 135 
GLY   N   CA   sing N N 136 
GLY   N   H    sing N N 137 
GLY   N   H2   sing N N 138 
GLY   CA  C    sing N N 139 
GLY   CA  HA2  sing N N 140 
GLY   CA  HA3  sing N N 141 
GLY   C   O    doub N N 142 
GLY   C   OXT  sing N N 143 
GLY   OXT HXT  sing N N 144 
HIS   N   CA   sing N N 145 
HIS   N   H    sing N N 146 
HIS   N   H2   sing N N 147 
HIS   CA  C    sing N N 148 
HIS   CA  CB   sing N N 149 
HIS   CA  HA   sing N N 150 
HIS   C   O    doub N N 151 
HIS   C   OXT  sing N N 152 
HIS   CB  CG   sing N N 153 
HIS   CB  HB2  sing N N 154 
HIS   CB  HB3  sing N N 155 
HIS   CG  ND1  sing Y N 156 
HIS   CG  CD2  doub Y N 157 
HIS   ND1 CE1  doub Y N 158 
HIS   ND1 HD1  sing N N 159 
HIS   CD2 NE2  sing Y N 160 
HIS   CD2 HD2  sing N N 161 
HIS   CE1 NE2  sing Y N 162 
HIS   CE1 HE1  sing N N 163 
HIS   NE2 HE2  sing N N 164 
HIS   OXT HXT  sing N N 165 
HOH   O   H1   sing N N 166 
HOH   O   H2   sing N N 167 
ILE   N   CA   sing N N 168 
ILE   N   H    sing N N 169 
ILE   N   H2   sing N N 170 
ILE   CA  C    sing N N 171 
ILE   CA  CB   sing N N 172 
ILE   CA  HA   sing N N 173 
ILE   C   O    doub N N 174 
ILE   C   OXT  sing N N 175 
ILE   CB  CG1  sing N N 176 
ILE   CB  CG2  sing N N 177 
ILE   CB  HB   sing N N 178 
ILE   CG1 CD1  sing N N 179 
ILE   CG1 HG12 sing N N 180 
ILE   CG1 HG13 sing N N 181 
ILE   CG2 HG21 sing N N 182 
ILE   CG2 HG22 sing N N 183 
ILE   CG2 HG23 sing N N 184 
ILE   CD1 HD11 sing N N 185 
ILE   CD1 HD12 sing N N 186 
ILE   CD1 HD13 sing N N 187 
ILE   OXT HXT  sing N N 188 
LEU   N   CA   sing N N 189 
LEU   N   H    sing N N 190 
LEU   N   H2   sing N N 191 
LEU   CA  C    sing N N 192 
LEU   CA  CB   sing N N 193 
LEU   CA  HA   sing N N 194 
LEU   C   O    doub N N 195 
LEU   C   OXT  sing N N 196 
LEU   CB  CG   sing N N 197 
LEU   CB  HB2  sing N N 198 
LEU   CB  HB3  sing N N 199 
LEU   CG  CD1  sing N N 200 
LEU   CG  CD2  sing N N 201 
LEU   CG  HG   sing N N 202 
LEU   CD1 HD11 sing N N 203 
LEU   CD1 HD12 sing N N 204 
LEU   CD1 HD13 sing N N 205 
LEU   CD2 HD21 sing N N 206 
LEU   CD2 HD22 sing N N 207 
LEU   CD2 HD23 sing N N 208 
LEU   OXT HXT  sing N N 209 
LYS   N   CA   sing N N 210 
LYS   N   H    sing N N 211 
LYS   N   H2   sing N N 212 
LYS   CA  C    sing N N 213 
LYS   CA  CB   sing N N 214 
LYS   CA  HA   sing N N 215 
LYS   C   O    doub N N 216 
LYS   C   OXT  sing N N 217 
LYS   CB  CG   sing N N 218 
LYS   CB  HB2  sing N N 219 
LYS   CB  HB3  sing N N 220 
LYS   CG  CD   sing N N 221 
LYS   CG  HG2  sing N N 222 
LYS   CG  HG3  sing N N 223 
LYS   CD  CE   sing N N 224 
LYS   CD  HD2  sing N N 225 
LYS   CD  HD3  sing N N 226 
LYS   CE  NZ   sing N N 227 
LYS   CE  HE2  sing N N 228 
LYS   CE  HE3  sing N N 229 
LYS   NZ  HZ1  sing N N 230 
LYS   NZ  HZ2  sing N N 231 
LYS   NZ  HZ3  sing N N 232 
LYS   OXT HXT  sing N N 233 
MET   N   CA   sing N N 234 
MET   N   H    sing N N 235 
MET   N   H2   sing N N 236 
MET   CA  C    sing N N 237 
MET   CA  CB   sing N N 238 
MET   CA  HA   sing N N 239 
MET   C   O    doub N N 240 
MET   C   OXT  sing N N 241 
MET   CB  CG   sing N N 242 
MET   CB  HB2  sing N N 243 
MET   CB  HB3  sing N N 244 
MET   CG  SD   sing N N 245 
MET   CG  HG2  sing N N 246 
MET   CG  HG3  sing N N 247 
MET   SD  CE   sing N N 248 
MET   CE  HE1  sing N N 249 
MET   CE  HE2  sing N N 250 
MET   CE  HE3  sing N N 251 
MET   OXT HXT  sing N N 252 
PHE   N   CA   sing N N 253 
PHE   N   H    sing N N 254 
PHE   N   H2   sing N N 255 
PHE   CA  C    sing N N 256 
PHE   CA  CB   sing N N 257 
PHE   CA  HA   sing N N 258 
PHE   C   O    doub N N 259 
PHE   C   OXT  sing N N 260 
PHE   CB  CG   sing N N 261 
PHE   CB  HB2  sing N N 262 
PHE   CB  HB3  sing N N 263 
PHE   CG  CD1  doub Y N 264 
PHE   CG  CD2  sing Y N 265 
PHE   CD1 CE1  sing Y N 266 
PHE   CD1 HD1  sing N N 267 
PHE   CD2 CE2  doub Y N 268 
PHE   CD2 HD2  sing N N 269 
PHE   CE1 CZ   doub Y N 270 
PHE   CE1 HE1  sing N N 271 
PHE   CE2 CZ   sing Y N 272 
PHE   CE2 HE2  sing N N 273 
PHE   CZ  HZ   sing N N 274 
PHE   OXT HXT  sing N N 275 
PRO   N   CA   sing N N 276 
PRO   N   CD   sing N N 277 
PRO   N   H    sing N N 278 
PRO   CA  C    sing N N 279 
PRO   CA  CB   sing N N 280 
PRO   CA  HA   sing N N 281 
PRO   C   O    doub N N 282 
PRO   C   OXT  sing N N 283 
PRO   CB  CG   sing N N 284 
PRO   CB  HB2  sing N N 285 
PRO   CB  HB3  sing N N 286 
PRO   CG  CD   sing N N 287 
PRO   CG  HG2  sing N N 288 
PRO   CG  HG3  sing N N 289 
PRO   CD  HD2  sing N N 290 
PRO   CD  HD3  sing N N 291 
PRO   OXT HXT  sing N N 292 
SER   N   CA   sing N N 293 
SER   N   H    sing N N 294 
SER   N   H2   sing N N 295 
SER   CA  C    sing N N 296 
SER   CA  CB   sing N N 297 
SER   CA  HA   sing N N 298 
SER   C   O    doub N N 299 
SER   C   OXT  sing N N 300 
SER   CB  OG   sing N N 301 
SER   CB  HB2  sing N N 302 
SER   CB  HB3  sing N N 303 
SER   OG  HG   sing N N 304 
SER   OXT HXT  sing N N 305 
THR   N   CA   sing N N 306 
THR   N   H    sing N N 307 
THR   N   H2   sing N N 308 
THR   CA  C    sing N N 309 
THR   CA  CB   sing N N 310 
THR   CA  HA   sing N N 311 
THR   C   O    doub N N 312 
THR   C   OXT  sing N N 313 
THR   CB  OG1  sing N N 314 
THR   CB  CG2  sing N N 315 
THR   CB  HB   sing N N 316 
THR   OG1 HG1  sing N N 317 
THR   CG2 HG21 sing N N 318 
THR   CG2 HG22 sing N N 319 
THR   CG2 HG23 sing N N 320 
THR   OXT HXT  sing N N 321 
TRP   N   CA   sing N N 322 
TRP   N   H    sing N N 323 
TRP   N   H2   sing N N 324 
TRP   CA  C    sing N N 325 
TRP   CA  CB   sing N N 326 
TRP   CA  HA   sing N N 327 
TRP   C   O    doub N N 328 
TRP   C   OXT  sing N N 329 
TRP   CB  CG   sing N N 330 
TRP   CB  HB2  sing N N 331 
TRP   CB  HB3  sing N N 332 
TRP   CG  CD1  doub Y N 333 
TRP   CG  CD2  sing Y N 334 
TRP   CD1 NE1  sing Y N 335 
TRP   CD1 HD1  sing N N 336 
TRP   CD2 CE2  doub Y N 337 
TRP   CD2 CE3  sing Y N 338 
TRP   NE1 CE2  sing Y N 339 
TRP   NE1 HE1  sing N N 340 
TRP   CE2 CZ2  sing Y N 341 
TRP   CE3 CZ3  doub Y N 342 
TRP   CE3 HE3  sing N N 343 
TRP   CZ2 CH2  doub Y N 344 
TRP   CZ2 HZ2  sing N N 345 
TRP   CZ3 CH2  sing Y N 346 
TRP   CZ3 HZ3  sing N N 347 
TRP   CH2 HH2  sing N N 348 
TRP   OXT HXT  sing N N 349 
TYR   N   CA   sing N N 350 
TYR   N   H    sing N N 351 
TYR   N   H2   sing N N 352 
TYR   CA  C    sing N N 353 
TYR   CA  CB   sing N N 354 
TYR   CA  HA   sing N N 355 
TYR   C   O    doub N N 356 
TYR   C   OXT  sing N N 357 
TYR   CB  CG   sing N N 358 
TYR   CB  HB2  sing N N 359 
TYR   CB  HB3  sing N N 360 
TYR   CG  CD1  doub Y N 361 
TYR   CG  CD2  sing Y N 362 
TYR   CD1 CE1  sing Y N 363 
TYR   CD1 HD1  sing N N 364 
TYR   CD2 CE2  doub Y N 365 
TYR   CD2 HD2  sing N N 366 
TYR   CE1 CZ   doub Y N 367 
TYR   CE1 HE1  sing N N 368 
TYR   CE2 CZ   sing Y N 369 
TYR   CE2 HE2  sing N N 370 
TYR   CZ  OH   sing N N 371 
TYR   OH  HH   sing N N 372 
TYR   OXT HXT  sing N N 373 
VAL   N   CA   sing N N 374 
VAL   N   H    sing N N 375 
VAL   N   H2   sing N N 376 
VAL   CA  C    sing N N 377 
VAL   CA  CB   sing N N 378 
VAL   CA  HA   sing N N 379 
VAL   C   O    doub N N 380 
VAL   C   OXT  sing N N 381 
VAL   CB  CG1  sing N N 382 
VAL   CB  CG2  sing N N 383 
VAL   CB  HB   sing N N 384 
VAL   CG1 HG11 sing N N 385 
VAL   CG1 HG12 sing N N 386 
VAL   CG1 HG13 sing N N 387 
VAL   CG2 HG21 sing N N 388 
VAL   CG2 HG22 sing N N 389 
VAL   CG2 HG23 sing N N 390 
VAL   OXT HXT  sing N N 391 
# 
_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                    7H9M 
_atom_sites.fract_transf_matrix[1][1]   0.015175 
_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]   0.011181 
_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]   0.009970 
_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.
;
? 
F ? ? 4.90428 4.07044 ? ? 12.99538 1.63651  ? ? 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   ? 4.35336   -28.55523 -38.90779 1.000 44.04801 ? 16  GLU   A N   1 
ATOM   2    C CA  . GLU   A 1 9   ? 5.59720   -27.82743 -39.12223 1.000 50.29165 ? 16  GLU   A CA  1 
ATOM   3    C C   . GLU   A 1 9   ? 5.85472   -26.90793 -37.92717 1.000 45.43071 ? 16  GLU   A C   1 
ATOM   4    O O   . GLU   A 1 9   ? 5.14121   -25.92517 -37.72377 1.000 44.78600 ? 16  GLU   A O   1 
ATOM   5    C CB  . GLU   A 1 9   ? 5.51868   -27.02417 -40.42330 1.000 54.68133 ? 16  GLU   A CB  1 
ATOM   6    C CG  . GLU   A 1 9   ? 6.83752   -26.93271 -41.17162 1.000 72.37093 ? 16  GLU   A CG  1 
ATOM   7    C CD  . GLU   A 1 9   ? 7.76171   -25.86645 -40.62732 1.000 78.28277 ? 16  GLU   A CD  1 
ATOM   8    O OE1 . GLU   A 1 9   ? 7.39971   -25.18944 -39.64317 1.000 73.97670 ? 16  GLU   A OE1 1 
ATOM   9    O OE2 . GLU   A 1 9   ? 8.87074   -25.71073 -41.17977 1.000 78.80534 ? 16  GLU   A OE2 1 
ATOM   10   N N   . VAL   A 1 10  ? 6.88069   -27.22890 -37.14190 1.000 32.92856 ? 17  VAL   A N   1 
ATOM   11   C CA  . VAL   A 1 10  ? 7.15930   -26.55860 -35.87606 1.000 27.01469 ? 17  VAL   A CA  1 
ATOM   12   C C   . VAL   A 1 10  ? 8.51182   -25.86764 -35.97306 1.000 26.75909 ? 17  VAL   A C   1 
ATOM   13   O O   . VAL   A 1 10  ? 9.50743   -26.49482 -36.34815 1.000 28.88040 ? 17  VAL   A O   1 
ATOM   14   C CB  . VAL   A 1 10  ? 7.15560   -27.56095 -34.70793 1.000 34.33299 ? 17  VAL   A CB  1 
ATOM   15   C CG1 . VAL   A 1 10  ? 7.32833   -26.83954 -33.38373 1.000 34.56022 ? 17  VAL   A CG1 1 
ATOM   16   C CG2 . VAL   A 1 10  ? 5.87723   -28.38562 -34.71969 1.000 43.45455 ? 17  VAL   A CG2 1 
ATOM   17   N N   . GLU   A 1 11  ? 8.55077   -24.58333 -35.62953 1.000 22.20084 ? 18  GLU   A N   1 
ATOM   18   C CA  . GLU   A 1 11  ? 9.79803   -23.83011 -35.56832 1.000 20.61191 ? 18  GLU   A CA  1 
ATOM   19   C C   . GLU   A 1 11  ? 10.21311  -23.66887 -34.11331 1.000 18.36087 ? 18  GLU   A C   1 
ATOM   20   O O   . GLU   A 1 11  ? 9.39837   -23.27695 -33.27231 1.000 18.11217 ? 18  GLU   A O   1 
ATOM   21   C CB  . GLU   A 1 11  ? 9.63500   -22.45404 -36.21513 1.000 22.45853 ? 18  GLU   A CB  1 
ATOM   22   C CG  . GLU   A 1 11  ? 9.44055   -22.49992 -37.72370 1.000 24.55331 ? 18  GLU   A CG  1 
ATOM   23   C CD  . GLU   A 1 11  ? 9.15493   -21.13253 -38.31573 1.000 32.51194 ? 18  GLU   A CD  1 
ATOM   24   O OE1 . GLU   A 1 11  ? 8.07441   -20.57775 -38.02894 1.000 34.87079 ? 18  GLU   A OE1 1 
ATOM   25   O OE2 . GLU   A 1 11  ? 10.00263  -20.61678 -39.07494 1.000 36.92257 ? 18  GLU   A OE2 1 
ATOM   26   N N   . THR   A 1 12  ? 11.47634  -23.97368 -33.81816 1.000 18.20621 ? 19  THR   A N   1 
ATOM   27   C CA  . THR   A 1 12  ? 12.03130  -23.86933 -32.47648 1.000 16.06346 ? 19  THR   A CA  1 
ATOM   28   C C   . THR   A 1 12  ? 13.02746  -22.72219 -32.43772 1.000 17.11610 ? 19  THR   A C   1 
ATOM   29   O O   . THR   A 1 12  ? 13.90510  -22.63499 -33.30111 1.000 15.99306 ? 19  THR   A O   1 
ATOM   30   C CB  . THR   A 1 12  ? 12.72039  -25.17434 -32.06908 1.000 16.65767 ? 19  THR   A CB  1 
ATOM   31   O OG1 . THR   A 1 12  ? 11.79351  -26.25830 -32.17582 1.000 18.76630 ? 19  THR   A OG1 1 
ATOM   32   C CG2 . THR   A 1 12  ? 13.23254  -25.07880 -30.63965 1.000 18.11067 ? 19  THR   A CG2 1 
ATOM   33   N N   . PHE   A 1 13  ? 12.88468  -21.84901 -31.44163 1.000 15.29940 ? 20  PHE   A N   1 
ATOM   34   C CA  . PHE   A 1 13  ? 13.70251  -20.65479 -31.28637 1.000 14.95758 ? 20  PHE   A CA  1 
ATOM   35   C C   . PHE   A 1 13  ? 14.34712  -20.65473 -29.90811 1.000 18.04012 ? 20  PHE   A C   1 
ATOM   36   O O   . PHE   A 1 13  ? 13.78309  -21.17582 -28.94371 1.000 16.72611 ? 20  PHE   A O   1 
ATOM   37   C CB  . PHE   A 1 13  ? 12.83453  -19.38849 -31.33453 1.000 15.46058 ? 20  PHE   A CB  1 
ATOM   38   C CG  . PHE   A 1 13  ? 12.07293  -19.20225 -32.61642 1.000 18.07601 ? 20  PHE   A CG  1 
ATOM   39   C CD1 . PHE   A 1 13  ? 10.87161  -19.86302 -32.83870 1.000 18.38876 ? 20  PHE   A CD1 1 
ATOM   40   C CD2 . PHE   A 1 13  ? 12.55338  -18.35134 -33.59831 1.000 19.73080 ? 20  PHE   A CD2 1 
ATOM   41   C CE1 . PHE   A 1 13  ? 10.17261  -19.68279 -34.02300 1.000 20.28997 ? 20  PHE   A CE1 1 
ATOM   42   C CE2 . PHE   A 1 13  ? 11.85268  -18.16278 -34.78320 1.000 21.81798 ? 20  PHE   A CE2 1 
ATOM   43   C CZ  . PHE   A 1 13  ? 10.66489  -18.83523 -34.99551 1.000 20.92308 ? 20  PHE   A CZ  1 
ATOM   44   N N   . ALA   A 1 14  ? 15.52528  -20.04154 -29.80869 1.000 15.83677 ? 21  ALA   A N   1 
ATOM   45   C CA  . ALA   A 1 14  ? 16.14366  -19.78905 -28.51676 1.000 14.23981 ? 21  ALA   A CA  1 
ATOM   46   C C   . ALA   A 1 14  ? 15.64595  -18.46135 -27.96190 1.000 15.38239 ? 21  ALA   A C   1 
ATOM   47   O O   . ALA   A 1 14  ? 15.55150  -17.46993 -28.69102 1.000 17.59758 ? 21  ALA   A O   1 
ATOM   48   C CB  . ALA   A 1 14  ? 17.66252  -19.71603 -28.66829 1.000 17.06129 ? 21  ALA   A CB  1 
ATOM   49   N N   . PHE   A 1 15  ? 15.31696  -18.44544 -26.66858 1.000 15.53269 ? 22  PHE   A N   1 
ATOM   50   C CA  . PHE   A 1 15  ? 15.10872  -17.16772 -25.99970 1.000 15.94800 ? 22  PHE   A CA  1 
ATOM   51   C C   . PHE   A 1 15  ? 16.39553  -16.35898 -26.03920 1.000 16.58393 ? 22  PHE   A C   1 
ATOM   52   O O   . PHE   A 1 15  ? 17.49915  -16.90923 -25.94509 1.000 18.18079 ? 22  PHE   A O   1 
ATOM   53   C CB  . PHE   A 1 15  ? 14.72622  -17.36670 -24.52851 1.000 14.92450 ? 22  PHE   A CB  1 
ATOM   54   C CG  . PHE   A 1 15  ? 13.33666  -17.90265 -24.31702 1.000 13.57730 ? 22  PHE   A CG  1 
ATOM   55   C CD1 . PHE   A 1 15  ? 12.22567  -17.12279 -24.60620 1.000 15.94436 ? 22  PHE   A CD1 1 
ATOM   56   C CD2 . PHE   A 1 15  ? 13.14209  -19.16695 -23.79346 1.000 14.58984 ? 22  PHE   A CD2 1 
ATOM   57   C CE1 . PHE   A 1 15  ? 10.93808  -17.61431 -24.40808 1.000 16.66907 ? 22  PHE   A CE1 1 
ATOM   58   C CE2 . PHE   A 1 15  ? 11.86707  -19.66365 -23.58969 1.000 15.48554 ? 22  PHE   A CE2 1 
ATOM   59   C CZ  . PHE   A 1 15  ? 10.76075  -18.88228 -23.89475 1.000 15.68729 ? 22  PHE   A CZ  1 
ATOM   60   N N   . GLN   A 1 16  ? 16.25120  -15.04387 -26.17574 1.000 15.56315 ? 23  GLN   A N   1 
ATOM   61   C CA  . GLN   A 1 16  ? 17.36885  -14.16496 -25.86968 1.000 16.26065 ? 23  GLN   A CA  1 
ATOM   62   C C   . GLN   A 1 16  ? 17.87261  -14.47740 -24.46978 1.000 18.16144 ? 23  GLN   A C   1 
ATOM   63   O O   . GLN   A 1 16  ? 17.09859  -14.84863 -23.58074 1.000 16.48577 ? 23  GLN   A O   1 
ATOM   64   C CB  . GLN   A 1 16  ? 16.92476  -12.70534 -25.93510 1.000 22.02040 ? 23  GLN   A CB  1 
ATOM   65   C CG  . GLN   A 1 16  ? 16.57626  -12.22330 -27.32733 1.000 23.59418 ? 23  GLN   A CG  1 
ATOM   66   C CD  . GLN   A 1 16  ? 15.98818  -10.82974 -27.30965 1.000 36.64419 ? 23  GLN   A CD  1 
ATOM   67   O OE1 . GLN   A 1 16  ? 14.77382  -10.66502 -27.25611 1.000 33.72906 ? 23  GLN   A OE1 1 
ATOM   68   N NE2 . GLN   A 1 16  ? 16.84868  -9.81630  -27.34991 1.000 34.16374 ? 23  GLN   A NE2 1 
ATOM   69   N N   . ALA   A 1 17  ? 19.18779  -14.33899 -24.28122 1.000 20.96784 ? 24  ALA   A N   1 
ATOM   70   C CA  . ALA   A 1 17  ? 19.80567  -14.74763 -23.02366 1.000 21.11148 ? 24  ALA   A CA  1 
ATOM   71   C C   . ALA   A 1 17  ? 19.14605  -14.06835 -21.83167 1.000 18.76446 ? 24  ALA   A C   1 
ATOM   72   O O   . ALA   A 1 17  ? 18.89946  -14.70666 -20.80303 1.000 21.08254 ? 24  ALA   A O   1 
ATOM   73   C CB  . ALA   A 1 17  ? 21.30172  -14.43901 -23.06075 1.000 23.28472 ? 24  ALA   A CB  1 
ATOM   74   N N   . GLU   A 1 18  ? 18.82556  -12.78113 -21.96431 1.000 20.92641 ? 25  GLU   A N   1 
ATOM   75   C CA  . GLU   A 1 18  ? 18.23097  -12.04306 -20.85717 1.000 20.51449 ? 25  GLU   A CA  1 
ATOM   76   C C   . GLU   A 1 18  ? 16.85342  -12.58667 -20.49405 1.000 19.23697 ? 25  GLU   A C   1 
ATOM   77   O O   . GLU   A 1 18  ? 16.47477  -12.58291 -19.31530 1.000 20.25789 ? 25  GLU   A O   1 
ATOM   78   C CB  . GLU   A 1 18  ? 18.15611  -10.55711 -21.21410 1.000 25.40438 ? 25  GLU   A CB  1 
ATOM   79   C CG  . GLU   A 1 18  ? 19.51381  -9.89114  -21.45205 1.000 30.71297 ? 25  GLU   A CG  1 
ATOM   80   C CD  . GLU   A 1 18  ? 20.05518  -10.08811 -22.86456 1.000 36.58497 ? 25  GLU   A CD  1 
ATOM   81   O OE1 . GLU   A 1 18  ? 19.41385  -10.78745 -23.68099 1.000 28.35770 ? 25  GLU   A OE1 1 
ATOM   82   O OE2 . GLU   A 1 18  ? 21.13001  -9.52515  -23.16463 1.000 41.93500 ? 25  GLU   A OE2 1 
ATOM   83   N N   . ILE   A 1 19  ? 16.09951  -13.06992 -21.48258 1.000 18.94720 ? 26  ILE   A N   1 
ATOM   84   C CA  . ILE   A 1 19  ? 14.76779  -13.59740 -21.20599 1.000 16.93511 ? 26  ILE   A CA  1 
ATOM   85   C C   . ILE   A 1 19  ? 14.86847  -14.97690 -20.56676 1.000 16.70580 ? 26  ILE   A C   1 
ATOM   86   O O   . ILE   A 1 19  ? 14.10814  -15.30793 -19.65084 1.000 17.26138 ? 26  ILE   A O   1 
ATOM   87   C CB  . ILE   A 1 19  ? 13.88931  -13.59702 -22.47663 1.000 17.27369 ? 26  ILE   A CB  1 
ATOM   88   C CG1 . ILE   A 1 19  ? 13.36690  -12.19279 -22.82482 1.000 20.56465 ? 26  ILE   A CG1 1 
ATOM   89   C CG2 . ILE   A 1 19  ? 12.67427  -14.50788 -22.29947 1.000 17.69542 ? 26  ILE   A CG2 1 
ATOM   90   C CD1 . ILE   A 1 19  ? 14.40924  -11.08690 -22.96312 1.000 25.87975 ? 26  ILE   A CD1 1 
ATOM   91   N N   . ALA   A 1 20  ? 15.81371  -15.80127 -21.02760 1.000 15.92323 ? 27  ALA   A N   1 
ATOM   92   C CA  . ALA   A 1 20  ? 16.06887  -17.06268 -20.34135 1.000 16.55353 ? 27  ALA   A CA  1 
ATOM   93   C C   . ALA   A 1 20  ? 16.45797  -16.81659 -18.88750 1.000 18.44651 ? 27  ALA   A C   1 
ATOM   94   O O   . ALA   A 1 20  ? 16.01475  -17.53856 -17.98586 1.000 17.93139 ? 27  ALA   A O   1 
ATOM   95   C CB  . ALA   A 1 20  ? 17.15551  -17.85048 -21.07542 1.000 18.43458 ? 27  ALA   A CB  1 
ATOM   96   N N   . GLN   A 1 21  ? 17.26102  -15.77826 -18.64047 1.000 18.91578 ? 28  GLN   A N   1 
ATOM   97   C CA  . GLN   A 1 21  ? 17.65601  -15.44248 -17.27563 1.000 20.31430 ? 28  GLN   A CA  1 
ATOM   98   C C   . GLN   A 1 21  ? 16.44952  -15.02982 -16.43915 1.000 21.05633 ? 28  GLN   A C   1 
ATOM   99   O O   . GLN   A 1 21  ? 16.31882  -15.44491 -15.28177 1.000 21.13554 ? 28  GLN   A O   1 
ATOM   100  C CB  . GLN   A 1 21  ? 18.70936  -14.33469 -17.31272 1.000 20.85468 ? 28  GLN   A CB  1 
ATOM   101  C CG  . GLN   A 1 21  ? 19.39190  -14.04221 -15.99411 1.000 33.66764 ? 28  GLN   A CG  1 
ATOM   102  C CD  . GLN   A 1 21  ? 20.30187  -12.82793 -16.08456 1.000 55.71750 ? 28  GLN   A CD  1 
ATOM   103  O OE1 . GLN   A 1 21  ? 20.82401  -12.34839 -15.07729 1.000 53.05770 ? 28  GLN   A OE1 1 
ATOM   104  N NE2 . GLN   A 1 21  ? 20.50483  -12.33232 -17.30205 1.000 44.43295 ? 28  GLN   A NE2 1 
ATOM   105  N N   . LEU   A 1 22  ? 15.55370  -14.21787 -17.01313 1.000 17.10070 ? 29  LEU   A N   1 
ATOM   106  C CA  . LEU   A 1 22  ? 14.31785  -13.84673 -16.32322 1.000 19.99046 ? 29  LEU   A CA  1 
ATOM   107  C C   . LEU   A 1 22  ? 13.49901  -15.07557 -15.94799 1.000 20.64956 ? 29  LEU   A C   1 
ATOM   108  O O   . LEU   A 1 22  ? 13.01394  -15.19507 -14.81551 1.000 19.16071 ? 29  LEU   A O   1 
ATOM   109  C CB  . LEU   A 1 22  ? 13.48748  -12.92408 -17.21350 1.000 19.73352 ? 29  LEU   A CB  1 
ATOM   110  C CG  . LEU   A 1 22  ? 12.10362  -12.57290 -16.66188 1.000 18.57570 ? 29  LEU   A CG  1 
ATOM   111  C CD1 . LEU   A 1 22  ? 12.24206  -11.65916 -15.46470 1.000 23.51924 ? 29  LEU   A CD1 1 
ATOM   112  C CD2 . LEU   A 1 22  ? 11.24484  -11.93012 -17.74136 1.000 22.38581 ? 29  LEU   A CD2 1 
ATOM   113  N N   . MET   A 1 23  ? 13.30713  -15.98971 -16.90038 1.000 14.93459 ? 30  MET   A N   1 
ATOM   114  C CA  . MET   A 1 23  ? 12.50855  -17.17856 -16.62917 1.000 17.75289 ? 30  MET   A CA  1 
ATOM   115  C C   . MET   A 1 23  ? 13.14198  -18.04421 -15.54713 1.000 17.67331 ? 30  MET   A C   1 
ATOM   116  O O   . MET   A 1 23  ? 12.43884  -18.56044 -14.67096 1.000 18.19741 ? 30  MET   A O   1 
ATOM   117  C CB  . MET   A 1 23  ? 12.26858  -17.96453 -17.91685 1.000 15.59151 ? 30  MET   A CB  1 
ATOM   118  C CG  . MET   A 1 23  ? 11.51157  -17.13738 -18.95662 1.000 16.04089 ? 30  MET   A CG  1 
ATOM   119  S SD  . MET   A 1 23  ? 11.31560  -17.94919 -20.54939 1.000 16.83904 ? 30  MET   A SD  1 
ATOM   120  C CE  . MET   A 1 23  ? 10.22860  -19.30621 -20.10940 1.000 17.78908 ? 30  MET   A CE  1 
ATOM   121  N N   . SER   A 1 24  ? 14.46904  -18.20795 -15.58261 1.000 19.39962 ? 31  SER   A N   1 
ATOM   122  C CA  . SER   A 1 24  ? 15.14433  -18.98341 -14.54512 1.000 18.90920 ? 31  SER   A CA  1 
ATOM   123  C C   . SER   A 1 24  ? 14.95235  -18.35614 -13.17132 1.000 20.57736 ? 31  SER   A C   1 
ATOM   124  O O   . SER   A 1 24  ? 14.73225  -19.06484 -12.18099 1.000 23.13365 ? 31  SER   A O   1 
ATOM   125  C CB  . SER   A 1 24  ? 16.63082  -19.10308 -14.86595 1.000 22.88342 ? 31  SER   A CB  1 
ATOM   126  O OG  . SER   A 1 24  ? 16.82535  -19.90278 -16.01713 1.000 32.16601 ? 31  SER   A OG  1 
ATOM   127  N N   . LEU   A 1 25  ? 15.02230  -17.02586 -13.09014 1.000 19.99288 ? 32  LEU   A N   1 
ATOM   128  C CA  . LEU   A 1 25  ? 14.83187  -16.36204 -11.80488 1.000 19.14503 ? 32  LEU   A CA  1 
ATOM   129  C C   . LEU   A 1 25  ? 13.41519  -16.57934 -11.28668 1.000 20.55110 ? 32  LEU   A C   1 
ATOM   130  O O   . LEU   A 1 25  ? 13.21391  -16.83465 -10.09310 1.000 22.52536 ? 32  LEU   A O   1 
ATOM   131  C CB  . LEU   A 1 25  ? 15.18411  -14.87311 -11.92769 1.000 26.01109 ? 32  LEU   A CB  1 
ATOM   132  C CG  . LEU   A 1 25  ? 15.02396  -13.86511 -10.77520 1.000 30.76276 ? 32  LEU   A CG  1 
ATOM   133  C CD1 . LEU   A 1 25  ? 15.75363  -12.58199 -11.13606 1.000 39.77851 ? 32  LEU   A CD1 1 
ATOM   134  C CD2 . LEU   A 1 25  ? 13.57000  -13.52390 -10.46239 1.000 32.86203 ? 32  LEU   A CD2 1 
ATOM   135  N N   . ILE   A 1 26  ? 12.42239  -16.49517 -12.17397 1.000 17.76907 ? 33  ILE   A N   1 
ATOM   136  C CA  . ILE   A 1 26  ? 11.03805  -16.71276 -11.76451 1.000 19.70248 ? 33  ILE   A CA  1 
ATOM   137  C C   . ILE   A 1 26  ? 10.83860  -18.14677 -11.28940 1.000 18.43146 ? 33  ILE   A C   1 
ATOM   138  O O   . ILE   A 1 26  ? 10.12084  -18.40209 -10.31385 1.000 19.90479 ? 33  ILE   A O   1 
ATOM   139  C CB  . ILE   A 1 26  ? 10.09275  -16.34265 -12.92040 1.000 15.78026 ? 33  ILE   A CB  1 
ATOM   140  C CG1 . ILE   A 1 26  ? 10.09149  -14.82759 -13.12930 1.000 19.29827 ? 33  ILE   A CG1 1 
ATOM   141  C CG2 . ILE   A 1 26  ? 8.67463   -16.86577 -12.66659 1.000 18.18776 ? 33  ILE   A CG2 1 
ATOM   142  C CD1 . ILE   A 1 26  ? 9.47920   -14.38808 -14.43676 1.000 19.38349 ? 33  ILE   A CD1 1 
ATOM   143  N N   . ILE   A 1 27  ? 11.48731  -19.10075 -11.95501 1.000 19.39265 ? 34  ILE   A N   1 
ATOM   144  C CA  . ILE   A 1 27  ? 11.29856  -20.51052 -11.62913 1.000 21.85692 ? 34  ILE   A CA  1 
ATOM   145  C C   . ILE   A 1 27  ? 12.05616  -20.89483 -10.36290 1.000 22.75857 ? 34  ILE   A C   1 
ATOM   146  O O   . ILE   A 1 27  ? 11.57471  -21.70434 -9.56133  1.000 25.43957 ? 34  ILE   A O   1 
ATOM   147  C CB  . ILE   A 1 27  ? 11.70106  -21.37704 -12.83820 1.000 20.46931 ? 34  ILE   A CB  1 
ATOM   148  C CG1 . ILE   A 1 27  ? 10.69660  -21.18166 -13.97373 1.000 20.23756 ? 34  ILE   A CG1 1 
ATOM   149  C CG2 . ILE   A 1 27  ? 11.82205  -22.84589 -12.44456 1.000 22.95963 ? 34  ILE   A CG2 1 
ATOM   150  C CD1 . ILE   A 1 27  ? 11.16802  -21.72470 -15.31143 1.000 22.50913 ? 34  ILE   A CD1 1 
ATOM   151  N N   . ASN   A 1 28  ? 13.24191  -20.31868 -10.14751 1.000 20.51837 ? 35  ASN   A N   1 
ATOM   152  C CA  . ASN   A 1 28  ? 14.14400  -20.81175 -9.11302  1.000 23.28491 ? 35  ASN   A CA  1 
ATOM   153  C C   . ASN   A 1 28  ? 14.11043  -20.01576 -7.81460  1.000 28.24597 ? 35  ASN   A C   1 
ATOM   154  O O   . ASN   A 1 28  ? 14.55012  -20.53687 -6.78353  1.000 36.38617 ? 35  ASN   A O   1 
ATOM   155  C CB  . ASN   A 1 28  ? 15.58242  -20.85143 -9.63689  1.000 27.84534 ? 35  ASN   A CB  1 
ATOM   156  C CG  . ASN   A 1 28  ? 15.76013  -21.84605 -10.75569 1.000 33.98256 ? 35  ASN   A CG  1 
ATOM   157  O OD1 . ASN   A 1 28  ? 15.10838  -22.88997 -10.78056 1.000 36.76069 ? 35  ASN   A OD1 1 
ATOM   158  N ND2 . ASN   A 1 28  ? 16.63710  -21.52465 -11.69931 1.000 42.31725 ? 35  ASN   A ND2 1 
ATOM   159  N N   . THR   A 1 29  ? 13.62323  -18.77877 -7.83024  1.000 23.19573 ? 36  THR   A N   1 
ATOM   160  C CA  . THR   A 1 29  ? 13.62684  -17.96926 -6.61754  1.000 22.98555 ? 36  THR   A CA  1 
ATOM   161  C C   . THR   A 1 29  ? 12.54403  -18.44736 -5.65836  1.000 24.27348 ? 36  THR   A C   1 
ATOM   162  O O   . THR   A 1 29  ? 11.40121  -18.68198 -6.06553  1.000 23.41852 ? 36  THR   A O   1 
ATOM   163  C CB  . THR   A 1 29  ? 13.39775  -16.49739 -6.96742  1.000 26.12350 ? 36  THR   A CB  1 
ATOM   164  O OG1 . THR   A 1 29  ? 14.44334  -16.04262 -7.83418  1.000 27.35792 ? 36  THR   A OG1 1 
ATOM   165  C CG2 . THR   A 1 29  ? 13.39772  -15.63776 -5.70972  1.000 29.28247 ? 36  THR   A CG2 1 
ATOM   166  N N   . PHE   A 1 30  ? 12.90059  -18.59995 -4.38329  1.000 24.71594 ? 37  PHE   A N   1 
ATOM   167  C CA  . PHE   A 1 30  ? 11.88818  -18.88341 -3.37573  1.000 21.69163 ? 37  PHE   A CA  1 
ATOM   168  C C   . PHE   A 1 30  ? 11.02245  -17.64719 -3.17693  1.000 25.15535 ? 37  PHE   A C   1 
ATOM   169  O O   . PHE   A 1 30  ? 11.52103  -16.58382 -2.78961  1.000 26.92445 ? 37  PHE   A O   1 
ATOM   170  C CB  . PHE   A 1 30  ? 12.50617  -19.32224 -2.05185  1.000 23.92109 ? 37  PHE   A CB  1 
ATOM   171  C CG  . PHE   A 1 30  ? 11.47820  -19.62656 -1.00216  1.000 26.24421 ? 37  PHE   A CG  1 
ATOM   172  C CD1 . PHE   A 1 30  ? 10.68925  -20.76170 -1.10115  1.000 32.59007 ? 37  PHE   A CD1 1 
ATOM   173  C CD2 . PHE   A 1 30  ? 11.26782  -18.76236 0.05929   1.000 27.14174 ? 37  PHE   A CD2 1 
ATOM   174  C CE1 . PHE   A 1 30  ? 9.72458   -21.04082 -0.14942  1.000 28.53857 ? 37  PHE   A CE1 1 
ATOM   175  C CE2 . PHE   A 1 30  ? 10.30554  -19.03880 1.01734   1.000 29.94228 ? 37  PHE   A CE2 1 
ATOM   176  C CZ  . PHE   A 1 30  ? 9.53433   -20.17972 0.91248   1.000 29.20278 ? 37  PHE   A CZ  1 
ATOM   177  N N   . TYR   A 1 31  ? 9.72504   -17.78955 -3.43892  1.000 20.58828 ? 38  TYR   A N   1 
ATOM   178  C CA  . TYR   A 1 31  ? 8.81923   -16.64754 -3.40834  1.000 20.50999 ? 38  TYR   A CA  1 
ATOM   179  C C   . TYR   A 1 31  ? 7.40249   -17.19642 -3.27773  1.000 18.06233 ? 38  TYR   A C   1 
ATOM   180  O O   . TYR   A 1 31  ? 6.87783   -17.78493 -4.22816  1.000 19.51815 ? 38  TYR   A O   1 
ATOM   181  C CB  . TYR   A 1 31  ? 8.97622   -15.82772 -4.68372  1.000 21.90781 ? 38  TYR   A CB  1 
ATOM   182  C CG  . TYR   A 1 31  ? 8.03580   -14.65755 -4.73470  1.000 21.27153 ? 38  TYR   A CG  1 
ATOM   183  C CD1 . TYR   A 1 31  ? 8.22963   -13.56516 -3.90653  1.000 25.57640 ? 38  TYR   A CD1 1 
ATOM   184  C CD2 . TYR   A 1 31  ? 6.93690   -14.65674 -5.58320  1.000 28.88308 ? 38  TYR   A CD2 1 
ATOM   185  C CE1 . TYR   A 1 31  ? 7.37051   -12.49428 -3.92548  1.000 36.37456 ? 38  TYR   A CE1 1 
ATOM   186  C CE2 . TYR   A 1 31  ? 6.06652   -13.58524 -5.60874  1.000 28.33103 ? 38  TYR   A CE2 1 
ATOM   187  C CZ  . TYR   A 1 31  ? 6.29347   -12.50917 -4.77836  1.000 34.81120 ? 38  TYR   A CZ  1 
ATOM   188  O OH  . TYR   A 1 31  ? 5.43912   -11.43679 -4.79016  1.000 46.83959 ? 38  TYR   A OH  1 
ATOM   189  N N   . SER   A 1 32  ? 6.78666   -16.99436 -2.11164  1.000 18.54980 ? 39  SER   A N   1 
ATOM   190  C CA  . SER   A 1 32  ? 5.53900   -17.68473 -1.79897  1.000 18.55258 ? 39  SER   A CA  1 
ATOM   191  C C   . SER   A 1 32  ? 4.32009   -17.04604 -2.45875  1.000 19.80027 ? 39  SER   A C   1 
ATOM   192  O O   . SER   A 1 32  ? 3.31901   -17.73450 -2.68224  1.000 22.23650 ? 39  SER   A O   1 
ATOM   193  C CB  . SER   A 1 32  ? 5.35328   -17.76467 -0.28420  1.000 20.01038 ? 39  SER   A CB  1 
ATOM   194  O OG  . SER   A 1 32  ? 6.37669   -18.55974 0.29454   1.000 22.25206 ? 39  SER   A OG  1 
ATOM   195  N N   . ASN   A 1 33  ? 4.38481   -15.75649 -2.79163  1.000 19.93149 ? 40  ASN   A N   1 
ATOM   196  C CA  . ASN   A 1 33  ? 3.21300   -14.99386 -3.23124  1.000 20.27597 ? 40  ASN   A CA  1 
ATOM   197  C C   . ASN   A 1 33  ? 2.95752   -15.19750 -4.72996  1.000 19.22663 ? 40  ASN   A C   1 
ATOM   198  O O   . ASN   A 1 33  ? 2.94588   -14.26349 -5.53467  1.000 19.89370 ? 40  ASN   A O   1 
ATOM   199  C CB  . ASN   A 1 33  ? 3.40114   -13.52626 -2.86133  1.000 22.28480 ? 40  ASN   A CB  1 
ATOM   200  C CG  . ASN   A 1 33  ? 2.21942   -12.65418 -3.24969  1.000 25.84344 ? 40  ASN   A CG  1 
ATOM   201  O OD1 . ASN   A 1 33  ? 1.06459   -13.06923 -3.15634  1.000 25.97650 ? 40  ASN   A OD1 1 
ATOM   202  N ND2 . ASN   A 1 33  ? 2.50799   -11.42228 -3.65710  1.000 25.96331 ? 40  ASN   A ND2 1 
ATOM   203  N N   . LYS   A 1 34  ? 2.73105   -16.46484 -5.09522  1.000 16.99772 ? 41  LYS   A N   1 
ATOM   204  C CA  . LYS   A 1 34  ? 2.63315   -16.84522 -6.50229  1.000 16.52269 ? 41  LYS   A CA  1 
ATOM   205  C C   . LYS   A 1 34  ? 1.34487   -16.37352 -7.16606  1.000 17.44047 ? 41  LYS   A C   1 
ATOM   206  O O   . LYS   A 1 34  ? 1.30705   -16.28286 -8.39947  1.000 16.69116 ? 41  LYS   A O   1 
ATOM   207  C CB  . LYS   A 1 34  ? 2.72518   -18.36692 -6.64494  1.000 16.68623 ? 41  LYS   A CB  1 
ATOM   208  C CG  . LYS   A 1 34  ? 4.09928   -18.97451 -6.32480  1.000 17.01126 ? 41  LYS   A CG  1 
ATOM   209  C CD  . LYS   A 1 34  ? 4.06276   -20.48925 -6.52440  1.000 20.33128 ? 41  LYS   A CD  1 
ATOM   210  C CE  . LYS   A 1 34  ? 5.41203   -21.14645 -6.25902  1.000 21.31018 ? 41  LYS   A CE  1 
ATOM   211  N NZ  . LYS   A 1 34  ? 6.39717   -20.87946 -7.34137  1.000 22.32414 ? 41  LYS   A NZ  1 
ATOM   212  N N   . GLU   A 1 35  ? 0.29942   -16.07322 -6.38678  1.000 16.64275 ? 42  GLU   A N   1 
ATOM   213  C CA  . GLU   A 1 35  ? -1.01441  -15.79338 -6.96364  1.000 16.05848 ? 42  GLU   A CA  1 
ATOM   214  C C   . GLU   A 1 35  ? -1.00789  -14.58440 -7.88907  1.000 17.06485 ? 42  GLU   A C   1 
ATOM   215  O O   . GLU   A 1 35  ? -1.94002  -14.42969 -8.68803  1.000 17.10839 ? 42  GLU   A O   1 
ATOM   216  C CB  . GLU   A 1 35  ? -2.05409  -15.56977 -5.86114  1.000 17.89268 ? 42  GLU   A CB  1 
ATOM   217  C CG  . GLU   A 1 35  ? -1.85335  -14.27800 -5.07227  1.000 17.33351 ? 42  GLU   A CG  1 
ATOM   218  C CD  . GLU   A 1 35  ? -2.77686  -14.16114 -3.87258  1.000 25.10565 ? 42  GLU   A CD  1 
ATOM   219  O OE1 . GLU   A 1 35  ? -2.93612  -15.15724 -3.14028  1.000 28.51800 ? 42  GLU   A OE1 1 
ATOM   220  O OE2 . GLU   A 1 35  ? -3.33375  -13.06483 -3.65832  1.000 34.33382 ? 42  GLU   A OE2 1 
ATOM   221  N N   . ILE   A 1 36  ? 0.01543   -13.72800 -7.80473  1.000 15.89460 ? 43  ILE   A N   1 
ATOM   222  C CA  . ILE   A 1 36  ? 0.06202   -12.53762 -8.64482  1.000 16.61766 ? 43  ILE   A CA  1 
ATOM   223  C C   . ILE   A 1 36  ? 0.14318   -12.85659 -10.13357 1.000 15.98010 ? 43  ILE   A C   1 
ATOM   224  O O   . ILE   A 1 36  ? -0.09516  -11.96457 -10.95520 1.000 16.13316 ? 43  ILE   A O   1 
ATOM   225  C CB  . ILE   A 1 36  ? 1.18465   -11.57399 -8.19858  1.000 19.26687 ? 43  ILE   A CB  1 
ATOM   226  C CG1 . ILE   A 1 36  ? 2.55913   -12.22181 -8.37037  1.000 20.68548 ? 43  ILE   A CG1 1 
ATOM   227  C CG2 . ILE   A 1 36  ? 0.95409   -11.11228 -6.75716  1.000 21.10553 ? 43  ILE   A CG2 1 
ATOM   228  C CD1 . ILE   A 1 36  ? 3.22658   -11.89584 -9.70315  1.000 23.14264 ? 43  ILE   A CD1 1 
ATOM   229  N N   . PHE   A 1 37  ? 0.48316   -14.09847 -10.51279 1.000 14.84606 ? 44  PHE   A N   1 
ATOM   230  C CA  . PHE   A 1 37  ? 0.48905   -14.44355 -11.93446 1.000 15.21710 ? 44  PHE   A CA  1 
ATOM   231  C C   . PHE   A 1 37  ? -0.85108  -14.11422 -12.58153 1.000 13.88406 ? 44  PHE   A C   1 
ATOM   232  O O   . PHE   A 1 37  ? -0.90200  -13.65327 -13.72920 1.000 14.92239 ? 44  PHE   A O   1 
ATOM   233  C CB  . PHE   A 1 37  ? 0.82190   -15.93073 -12.14794 1.000 15.66143 ? 44  PHE   A CB  1 
ATOM   234  C CG  . PHE   A 1 37  ? -0.36133  -16.84551 -11.95241 1.000 14.15586 ? 44  PHE   A CG  1 
ATOM   235  C CD1 . PHE   A 1 37  ? -0.69146  -17.31384 -10.69027 1.000 16.03682 ? 44  PHE   A CD1 1 
ATOM   236  C CD2 . PHE   A 1 37  ? -1.17218  -17.19864 -13.02627 1.000 15.99745 ? 44  PHE   A CD2 1 
ATOM   237  C CE1 . PHE   A 1 37  ? -1.79866  -18.13393 -10.50454 1.000 15.53338 ? 44  PHE   A CE1 1 
ATOM   238  C CE2 . PHE   A 1 37  ? -2.28779  -18.01046 -12.83997 1.000 16.46614 ? 44  PHE   A CE2 1 
ATOM   239  C CZ  . PHE   A 1 37  ? -2.59762  -18.47877 -11.58363 1.000 16.11633 ? 44  PHE   A CZ  1 
ATOM   240  N N   . LEU   A 1 38  ? -1.95159  -14.34189 -11.85767 1.000 13.71612 ? 45  LEU   A N   1 
ATOM   241  C CA  . LEU   A 1 38  ? -3.26362  -14.17466 -12.46998 1.000 13.33662 ? 45  LEU   A CA  1 
ATOM   242  C C   . LEU   A 1 38  ? -3.57100  -12.70200 -12.69212 1.000 16.33456 ? 45  LEU   A C   1 
ATOM   243  O O   . LEU   A 1 38  ? -4.10343  -12.32656 -13.74374 1.000 15.91930 ? 45  LEU   A O   1 
ATOM   244  C CB  . LEU   A 1 38  ? -4.33368  -14.85278 -11.62043 1.000 14.32075 ? 45  LEU   A CB  1 
ATOM   245  C CG  . LEU   A 1 38  ? -5.74103  -14.87420 -12.22621 1.000 14.56193 ? 45  LEU   A CG  1 
ATOM   246  C CD1 . LEU   A 1 38  ? -5.72637  -15.57398 -13.57948 1.000 17.10066 ? 45  LEU   A CD1 1 
ATOM   247  C CD2 . LEU   A 1 38  ? -6.69774  -15.57665 -11.27834 1.000 20.21944 ? 45  LEU   A CD2 1 
ATOM   248  N N   . ARG   A 1 39  ? -3.22146  -11.85097 -11.72179 1.000 15.28167 ? 46  ARG   A N   1 
ATOM   249  C CA  . ARG   A 1 39  ? -3.35696  -10.41191 -11.91541 1.000 14.51625 ? 46  ARG   A CA  1 
ATOM   250  C C   . ARG   A 1 39  ? -2.57670  -9.94675  -13.13526 1.000 16.22359 ? 46  ARG   A C   1 
ATOM   251  O O   . ARG   A 1 39  ? -3.06117  -9.11852  -13.91602 1.000 16.39695 ? 46  ARG   A O   1 
ATOM   252  C CB  . ARG   A 1 39  ? -2.85998  -9.67440  -10.67213 1.000 18.60884 ? 46  ARG   A CB  1 
ATOM   253  C CG  . ARG   A 1 39  ? -2.76596  -8.16831  -10.83032 1.000 21.75571 ? 46  ARG   A CG  1 
ATOM   254  C CD  . ARG   A 1 39  ? -2.06227  -7.53463  -9.63144  1.000 24.18948 ? 46  ARG   A CD  1 
ATOM   255  N NE  . ARG   A 1 39  ? -0.62509  -7.78805  -9.63816  1.000 27.42339 ? 46  ARG   A NE  1 
ATOM   256  C CZ  . ARG   A 1 39  ? 0.16103   -7.68215  -8.57557  1.000 32.39049 ? 46  ARG   A CZ  1 
ATOM   257  N NH1 . ARG   A 1 39  ? -0.31513  -7.31930  -7.39448  1.000 30.30640 ? 46  ARG   A NH1 1 
ATOM   258  N NH2 . ARG   A 1 39  ? 1.45856   -7.95004  -8.69964  1.000 33.51063 ? 46  ARG   A NH2 1 
ATOM   259  N N   . GLU   A 1 40  ? -1.36660  -10.47721 -13.32377 1.000 14.69604 ? 47  GLU   A N   1 
ATOM   260  C CA  . GLU   A 1 40  ? -0.53139  -10.01135 -14.42260 1.000 15.41073 ? 47  GLU   A CA  1 
ATOM   261  C C   . GLU   A 1 40  ? -1.10713  -10.43257 -15.76688 1.000 14.65884 ? 47  GLU   A C   1 
ATOM   262  O O   . GLU   A 1 40  ? -1.07626  -9.65865  -16.73385 1.000 15.02816 ? 47  GLU   A O   1 
ATOM   263  C CB  . GLU   A 1 40  ? 0.89280   -10.54627 -14.25987 1.000 14.51715 ? 47  GLU   A CB  1 
ATOM   264  C CG  . GLU   A 1 40  ? 1.59561   -10.06691 -12.99052 1.000 18.47283 ? 47  GLU   A CG  1 
ATOM   265  C CD  . GLU   A 1 40  ? 1.58981   -8.55652  -12.83215 1.000 21.36307 ? 47  GLU   A CD  1 
ATOM   266  O OE1 . GLU   A 1 40  ? 1.65536   -7.83641  -13.84982 1.000 21.61681 ? 47  GLU   A OE1 1 
ATOM   267  O OE2 . GLU   A 1 40  ? 1.51642   -8.08519  -11.67712 1.000 28.40293 ? 47  GLU   A OE2 1 
ATOM   268  N N   . LEU   A 1 41  ? -1.62968  -11.65818 -15.85293 1.000 13.58103 ? 48  LEU   A N   1 
ATOM   269  C CA  . LEU   A 1 41  ? -2.20000  -12.11496 -17.11783 1.000 14.25968 ? 48  LEU   A CA  1 
ATOM   270  C C   . LEU   A 1 41  ? -3.50559  -11.39492 -17.42383 1.000 15.46621 ? 48  LEU   A C   1 
ATOM   271  O O   . LEU   A 1 41  ? -3.78219  -11.06242 -18.58398 1.000 14.83013 ? 48  LEU   A O   1 
ATOM   272  C CB  . LEU   A 1 41  ? -2.40971  -13.62738 -17.08567 1.000 14.33030 ? 48  LEU   A CB  1 
ATOM   273  C CG  . LEU   A 1 41  ? -1.11310  -14.44707 -17.03882 1.000 15.52280 ? 48  LEU   A CG  1 
ATOM   274  C CD1 . LEU   A 1 41  ? -1.40820  -15.94594 -16.98235 1.000 16.05354 ? 48  LEU   A CD1 1 
ATOM   275  C CD2 . LEU   A 1 41  ? -0.17806  -14.13096 -18.20707 1.000 17.23187 ? 48  LEU   A CD2 1 
ATOM   276  N N   . ILE   A 1 42  ? -4.33158  -11.16040 -16.40236 1.000 13.67848 ? 49  ILE   A N   1 
ATOM   277  C CA  . ILE   A 1 42  ? -5.56386  -10.41085 -16.61628 1.000 13.59709 ? 49  ILE   A CA  1 
ATOM   278  C C   . ILE   A 1 42  ? -5.24450  -8.98193  -17.03289 1.000 14.52291 ? 49  ILE   A C   1 
ATOM   279  O O   . ILE   A 1 42  ? -5.90969  -8.40968  -17.90841 1.000 14.56516 ? 49  ILE   A O   1 
ATOM   280  C CB  . ILE   A 1 42  ? -6.45496  -10.48327 -15.36084 1.000 13.27373 ? 49  ILE   A CB  1 
ATOM   281  C CG1 . ILE   A 1 42  ? -7.03090  -11.89435 -15.21538 1.000 13.88014 ? 49  ILE   A CG1 1 
ATOM   282  C CG2 . ILE   A 1 42  ? -7.58086  -9.44030  -15.40851 1.000 15.42105 ? 49  ILE   A CG2 1 
ATOM   283  C CD1 . ILE   A 1 42  ? -7.77097  -12.11980 -13.90072 1.000 16.89623 ? 49  ILE   A CD1 1 
ATOM   284  N N   . SER   A 1 43  ? -4.19631  -8.39787  -16.44267 1.000 15.03737 ? 50  SER   A N   1 
ATOM   285  C CA  . SER   A 1 43  ? -3.78602  -7.05605  -16.83295 1.000 14.75014 ? 50  SER   A CA  1 
ATOM   286  C C   . SER   A 1 43  ? -3.33472  -7.03177  -18.28820 1.000 15.01173 ? 50  SER   A C   1 
ATOM   287  O O   . SER   A 1 43  ? -3.68616  -6.11265  -19.03842 1.000 15.26317 ? 50  SER   A O   1 
ATOM   288  C CB  . SER   A 1 43  ? -2.68077  -6.55517  -15.89719 1.000 17.69639 ? 50  SER   A CB  1 
ATOM   289  O OG  . SER   A 1 43  ? -2.18425  -5.29331  -16.31879 1.000 25.10095 ? 50  SER   A OG  1 
ATOM   290  N N   . ASN   A 1 44  ? -2.56985  -8.04304  -18.71230 1.000 15.16749 ? 51  ASN   A N   1 
ATOM   291  C CA  . ASN   A 1 44  ? -2.17668  -8.11791  -20.11523 1.000 14.63268 ? 51  ASN   A CA  1 
ATOM   292  C C   . ASN   A 1 44  ? -3.39592  -8.23049  -21.01765 1.000 14.42523 ? 51  ASN   A C   1 
ATOM   293  O O   . ASN   A 1 44  ? -3.44362  -7.61582  -22.08909 1.000 14.77214 ? 51  ASN   A O   1 
ATOM   294  C CB  . ASN   A 1 44  ? -1.26058  -9.31699  -20.34674 1.000 14.35706 ? 51  ASN   A CB  1 
ATOM   295  C CG  . ASN   A 1 44  ? 0.12312   -9.11305  -19.78576 1.000 22.05162 ? 51  ASN   A CG  1 
ATOM   296  O OD1 . ASN   A 1 44  ? 0.47265   -8.02791  -19.31423 1.000 21.24034 ? 51  ASN   A OD1 1 
ATOM   297  N ND2 . ASN   A 1 44  ? 0.93338   -10.15614 -19.86080 1.000 23.53803 ? 51  ASN   A ND2 1 
ATOM   298  N N   . SER   A 1 45  ? -4.38227  -9.03258  -20.61047 1.000 12.44645 ? 52  SER   A N   1 
ATOM   299  C CA  . SER   A 1 45  ? -5.60199  -9.15865  -21.39932 1.000 15.12845 ? 52  SER   A CA  1 
ATOM   300  C C   . SER   A 1 45  ? -6.32676  -7.82272  -21.49705 1.000 14.18985 ? 52  SER   A C   1 
ATOM   301  O O   . SER   A 1 45  ? -6.79054  -7.43573  -22.57795 1.000 13.90191 ? 52  SER   A O   1 
ATOM   302  C CB  . SER   A 1 45  ? -6.50996  -10.21326 -20.77088 1.000 13.74486 ? 52  SER   A CB  1 
ATOM   303  O OG  . SER   A 1 45  ? -5.99472  -11.52265 -20.96519 1.000 15.41159 ? 52  SER   A OG  1 
ATOM   304  N N   . SER   A 1 46  ? -6.43281  -7.10438  -20.37477 1.000 12.75352 ? 53  SER   A N   1 
ATOM   305  C CA  . SER   A 1 46  ? -7.06253  -5.78850  -20.39606 1.000 13.46847 ? 53  SER   A CA  1 
ATOM   306  C C   . SER   A 1 46  ? -6.33081  -4.85016  -21.35064 1.000 14.15585 ? 53  SER   A C   1 
ATOM   307  O O   . SER   A 1 46  ? -6.96381  -4.11361  -22.11725 1.000 15.25299 ? 53  SER   A O   1 
ATOM   308  C CB  . SER   A 1 46  ? -7.10764  -5.21344  -18.97964 1.000 14.96202 ? 53  SER   A CB  1 
ATOM   309  O OG  . SER   A 1 46  ? -7.63069  -3.89392  -18.97960 1.000 16.77161 ? 53  SER   A OG  1 
ATOM   310  N N   . ASP   A 1 47  ? -4.99462  -4.88044  -21.33503 1.000 15.66058 ? 54  ASP   A N   1 
ATOM   311  C CA  . ASP   A 1 47  ? -4.22442  -4.02496  -22.22890 1.000 15.13309 ? 54  ASP   A CA  1 
ATOM   312  C C   . ASP   A 1 47  ? -4.50518  -4.37287  -23.68917 1.000 15.80511 ? 54  ASP   A C   1 
ATOM   313  O O   . ASP   A 1 47  ? -4.62399  -3.48079  -24.53748 1.000 15.90832 ? 54  ASP   A O   1 
ATOM   314  C CB  . ASP   A 1 47  ? -2.73706  -4.20033  -21.92623 1.000 14.25697 ? 54  ASP   A CB  1 
ATOM   315  C CG  . ASP   A 1 47  ? -2.29715  -3.45369  -20.67808 1.000 19.03462 ? 54  ASP   A CG  1 
ATOM   316  O OD1 . ASP   A 1 47  ? -3.09085  -2.65083  -20.13863 1.000 21.87567 ? 54  ASP   A OD1 1 
ATOM   317  O OD2 . ASP   A 1 47  ? -1.14563  -3.66662  -20.22889 1.000 21.81260 ? 54  ASP   A OD2 1 
ATOM   318  N N   . ALA   A 1 48  ? -4.62818  -5.66858  -23.99744 1.000 13.16517 ? 55  ALA   A N   1 
ATOM   319  C CA  . ALA   A 1 48  ? -4.89704  -6.09361  -25.37068 1.000 12.43125 ? 55  ALA   A CA  1 
ATOM   320  C C   . ALA   A 1 48  ? -6.30538  -5.71062  -25.80378 1.000 14.58171 ? 55  ALA   A C   1 
ATOM   321  O O   . ALA   A 1 48  ? -6.53780  -5.38455  -26.97576 1.000 14.18040 ? 55  ALA   A O   1 
ATOM   322  C CB  . ALA   A 1 48  ? -4.69472  -7.60546  -25.50375 1.000 13.67624 ? 55  ALA   A CB  1 
ATOM   323  N N   . LEU   A 1 49  ? -7.26086  -5.77760  -24.87520 1.000 13.72814 ? 56  LEU   A N   1 
ATOM   324  C CA  . LEU   A 1 49  ? -8.62299  -5.35486  -25.17125 1.000 13.89756 ? 56  LEU   A CA  1 
ATOM   325  C C   . LEU   A 1 49  ? -8.68922  -3.84938  -25.39444 1.000 14.61588 ? 56  LEU   A C   1 
ATOM   326  O O   . LEU   A 1 49  ? -9.41196  -3.38510  -26.28386 1.000 15.38502 ? 56  LEU   A O   1 
ATOM   327  C CB  . LEU   A 1 49  ? -9.54796  -5.79443  -24.03600 1.000 14.78355 ? 56  LEU   A CB  1 
ATOM   328  C CG  . LEU   A 1 49  ? -9.81734  -7.30246  -24.01368 1.000 13.88539 ? 56  LEU   A CG  1 
ATOM   329  C CD1 . LEU   A 1 49  ? -10.27470 -7.74238  -22.63240 1.000 16.36112 ? 56  LEU   A CD1 1 
ATOM   330  C CD2 . LEU   A 1 49  ? -10.86642 -7.66373  -25.05589 1.000 16.27706 ? 56  LEU   A CD2 1 
ATOM   331  N N   . ASP   A 1 50  ? -7.94447  -3.07048  -24.59993 1.000 14.18783 ? 57  ASP   A N   1 
ATOM   332  C CA  . ASP   A 1 50  ? -7.89144  -1.62591  -24.82623 1.000 14.95062 ? 57  ASP   A CA  1 
ATOM   333  C C   . ASP   A 1 50  ? -7.40915  -1.31279  -26.23934 1.000 15.35893 ? 57  ASP   A C   1 
ATOM   334  O O   . ASP   A 1 50  ? -7.90936  -0.38170  -26.88319 1.000 16.39021 ? 57  ASP   A O   1 
ATOM   335  C CB  . ASP   A 1 50  ? -6.95040  -0.95018  -23.81939 1.000 14.04502 ? 57  ASP   A CB  1 
ATOM   336  C CG  . ASP   A 1 50  ? -7.49037  -0.92517  -22.39511 1.000 18.08539 ? 57  ASP   A CG  1 
ATOM   337  O OD1 . ASP   A 1 50  ? -8.65850  -1.29431  -22.15575 1.000 20.16845 ? 57  ASP   A OD1 1 
ATOM   338  O OD2 . ASP   A 1 50  ? -6.72191  -0.50721  -21.49970 1.000 20.20806 ? 57  ASP   A OD2 1 
ATOM   339  N N   . LYS   A 1 51  ? -6.42772  -2.07413  -26.73435 1.000 14.45735 ? 58  LYS   A N   1 
ATOM   340  C CA  . LYS   A 1 51  ? -5.83857  -1.77433  -28.03642 1.000 15.90995 ? 58  LYS   A CA  1 
ATOM   341  C C   . LYS   A 1 51  ? -6.83835  -1.98755  -29.16496 1.000 15.85020 ? 58  LYS   A C   1 
ATOM   342  O O   . LYS   A 1 51  ? -6.94581  -1.15478  -30.07292 1.000 17.49532 ? 58  LYS   A O   1 
ATOM   343  C CB  . LYS   A 1 51  ? -4.58281  -2.62023  -28.25819 1.000 17.61253 ? 58  LYS   A CB  1 
ATOM   344  C CG  . LYS   A 1 51  ? -3.40204  -2.23473  -27.37290 1.000 17.41151 ? 58  LYS   A CG  1 
ATOM   345  C CD  . LYS   A 1 51  ? -2.25941  -3.23617  -27.54741 1.000 18.08795 ? 58  LYS   A CD  1 
ATOM   346  C CE  . LYS   A 1 51  ? -1.19976  -3.04673  -26.47707 1.000 23.48937 ? 58  LYS   A CE  1 
ATOM   347  N NZ  . LYS   A 1 51  ? -0.07099  -4.01562  -26.63762 1.000 28.05431 ? 58  LYS   A NZ  1 
ATOM   348  N N   . ILE   A 1 52  ? -7.56841  -3.10618  -29.14175 1.000 15.34864 ? 59  ILE   A N   1 
ATOM   349  C CA  . ILE   A 1 52  ? -8.55259  -3.32798  -30.19823 1.000 14.46779 ? 59  ILE   A CA  1 
ATOM   350  C C   . ILE   A 1 52  ? -9.71975  -2.35873  -30.06065 1.000 17.25949 ? 59  ILE   A C   1 
ATOM   351  O O   . ILE   A 1 52  ? -10.27264 -1.90299  -31.06839 1.000 18.04015 ? 59  ILE   A O   1 
ATOM   352  C CB  . ILE   A 1 52  ? -8.99241  -4.80289  -30.30289 1.000 16.78139 ? 59  ILE   A CB  1 
ATOM   353  C CG1 . ILE   A 1 52  ? -9.81337  -5.02335  -31.57966 1.000 18.71884 ? 59  ILE   A CG1 1 
ATOM   354  C CG2 . ILE   A 1 52  ? -9.78837  -5.22599  -29.07493 1.000 19.06241 ? 59  ILE   A CG2 1 
ATOM   355  C CD1 . ILE   A 1 52  ? -9.01553  -4.83228  -32.85634 1.000 22.17652 ? 59  ILE   A CD1 1 
ATOM   356  N N   . ARG   A 1 53  ? -10.09477 -1.99689  -28.83031 1.000 15.77571 ? 60  ARG   A N   1 
ATOM   357  C CA  . ARG   A 1 53  ? -11.14669 -0.99906  -28.66906 1.000 17.98183 ? 60  ARG   A CA  1 
ATOM   358  C C   . ARG   A 1 53  ? -10.73138 0.32569   -29.29102 1.000 16.92519 ? 60  ARG   A C   1 
ATOM   359  O O   . ARG   A 1 53  ? -11.50604 0.95109   -30.02395 1.000 18.99001 ? 60  ARG   A O   1 
ATOM   360  C CB  . ARG   A 1 53  ? -11.51396 -0.81614  -27.19636 1.000 19.45784 ? 60  ARG   A CB  1 
ATOM   361  C CG  . ARG   A 1 53  ? -12.56925 0.26869   -26.99131 1.000 23.94958 ? 60  ARG   A CG  1 
ATOM   362  C CD  . ARG   A 1 53  ? -13.01980 0.35998   -25.55092 1.000 33.25301 ? 60  ARG   A CD  1 
ATOM   363  N NE  . ARG   A 1 53  ? -14.10794 -0.56142  -25.24821 1.000 41.96680 ? 60  ARG   A NE  1 
ATOM   364  C CZ  . ARG   A 1 53  ? -14.37728 -1.02015  -24.03377 1.000 46.03784 ? 60  ARG   A CZ  1 
ATOM   365  N NH1 . ARG   A 1 53  ? -13.63560 -0.68729  -22.99002 1.000 36.76068 ? 60  ARG   A NH1 1 
ATOM   366  N NH2 . ARG   A 1 53  ? -15.41766 -1.83089  -23.86156 1.000 34.87451 ? 60  ARG   A NH2 1 
ATOM   367  N N   . TYR   A 1 54  ? -9.49584  0.76198   -29.02620 1.000 16.40979 ? 61  TYR   A N   1 
ATOM   368  C CA  . TYR   A 1 54  ? -9.03878  2.02979   -29.58333 1.000 17.17203 ? 61  TYR   A CA  1 
ATOM   369  C C   . TYR   A 1 54  ? -9.04915  2.00157   -31.10863 1.000 20.84007 ? 61  TYR   A C   1 
ATOM   370  O O   . TYR   A 1 54  ? -9.50656  2.95204   -31.75265 1.000 19.77254 ? 61  TYR   A O   1 
ATOM   371  C CB  . TYR   A 1 54  ? -7.64880  2.38408   -29.05902 1.000 17.63212 ? 61  TYR   A CB  1 
ATOM   372  C CG  . TYR   A 1 54  ? -7.19926  3.73374   -29.56113 1.000 20.23011 ? 61  TYR   A CG  1 
ATOM   373  C CD1 . TYR   A 1 54  ? -7.72843  4.90591   -29.03270 1.000 20.00254 ? 61  TYR   A CD1 1 
ATOM   374  C CD2 . TYR   A 1 54  ? -6.28825  3.83499   -30.60025 1.000 21.67258 ? 61  TYR   A CD2 1 
ATOM   375  C CE1 . TYR   A 1 54  ? -7.33565  6.14047   -29.50600 1.000 21.11381 ? 61  TYR   A CE1 1 
ATOM   376  C CE2 . TYR   A 1 54  ? -5.88922  5.06689   -31.08269 1.000 24.96697 ? 61  TYR   A CE2 1 
ATOM   377  C CZ  . TYR   A 1 54  ? -6.41469  6.21405   -30.53380 1.000 22.37241 ? 61  TYR   A CZ  1 
ATOM   378  O OH  . TYR   A 1 54  ? -6.01850  7.44177   -31.00956 1.000 25.03141 ? 61  TYR   A OH  1 
ATOM   379  N N   . GLU   A 1 55  ? -8.54123  0.91859   -31.70546 1.000 19.84983 ? 62  GLU   A N   1 
ATOM   380  C CA  . GLU   A 1 55  ? -8.54552  0.81226   -33.16330 1.000 20.82345 ? 62  GLU   A CA  1 
ATOM   381  C C   . GLU   A 1 55  ? -9.96403  0.84638   -33.71564 1.000 22.62237 ? 62  GLU   A C   1 
ATOM   382  O O   . GLU   A 1 55  ? -10.21247 1.43420   -34.77599 1.000 23.80571 ? 62  GLU   A O   1 
ATOM   383  C CB  . GLU   A 1 55  ? -7.82682  -0.46369  -33.59895 1.000 21.08994 ? 62  GLU   A CB  1 
ATOM   384  C CG  . GLU   A 1 55  ? -6.31825  -0.40393  -33.40046 1.000 22.43635 ? 62  GLU   A CG  1 
ATOM   385  C CD  . GLU   A 1 55  ? -5.58956  -1.51707  -34.12537 1.000 32.09869 ? 62  GLU   A CD  1 
ATOM   386  O OE1 . GLU   A 1 55  ? -6.26572  -2.42181  -34.65704 1.000 32.07348 ? 62  GLU   A OE1 1 
ATOM   387  O OE2 . GLU   A 1 55  ? -4.34092  -1.48383  -34.17031 1.000 33.43329 ? 62  GLU   A OE2 1 
ATOM   388  N N   . SER   A 1 56  ? -10.91477 0.24292   -32.99818 1.000 20.92508 ? 63  SER   A N   1 
ATOM   389  C CA  . SER   A 1 56  ? -12.29377 0.19924   -33.47115 1.000 22.14991 ? 63  SER   A CA  1 
ATOM   390  C C   . SER   A 1 56  ? -12.97477 1.56348   -33.44258 1.000 22.63705 ? 63  SER   A C   1 
ATOM   391  O O   . SER   A 1 56  ? -13.97516 1.75281   -34.14094 1.000 25.44743 ? 63  SER   A O   1 
ATOM   392  C CB  . SER   A 1 56  ? -13.10125 -0.81031  -32.65325 1.000 21.99054 ? 63  SER   A CB  1 
ATOM   393  O OG  . SER   A 1 56  ? -13.48105 -0.26883  -31.39695 1.000 24.77316 ? 63  SER   A OG  1 
ATOM   394  N N   . LEU   A 1 57  ? -12.46403 2.51506   -32.65733 1.000 20.90007 ? 64  LEU   A N   1 
ATOM   395  C CA  . LEU   A 1 57  ? -13.10610 3.82506   -32.57842 1.000 24.93287 ? 64  LEU   A CA  1 
ATOM   396  C C   . LEU   A 1 57  ? -13.07577 4.55498   -33.91412 1.000 28.07989 ? 64  LEU   A C   1 
ATOM   397  O O   . LEU   A 1 57  ? -13.97828 5.34763   -34.20668 1.000 33.05021 ? 64  LEU   A O   1 
ATOM   398  C CB  . LEU   A 1 57  ? -12.44842 4.67671   -31.49077 1.000 24.21125 ? 64  LEU   A CB  1 
ATOM   399  C CG  . LEU   A 1 57  ? -12.55773 4.13898   -30.06255 1.000 24.41400 ? 64  LEU   A CG  1 
ATOM   400  C CD1 . LEU   A 1 57  ? -11.92426 5.11164   -29.08029 1.000 24.01660 ? 64  LEU   A CD1 1 
ATOM   401  C CD2 . LEU   A 1 57  ? -14.00877 3.88215   -29.69648 1.000 27.53836 ? 64  LEU   A CD2 1 
ATOM   402  N N   . THR   A 1 58  ? -12.05074 4.31822   -34.73144 1.000 25.57024 ? 65  THR   A N   1 
ATOM   403  C CA  . THR   A 1 58  ? -11.96104 4.95056   -36.04080 1.000 27.51581 ? 65  THR   A CA  1 
ATOM   404  C C   . THR   A 1 58  ? -12.20094 3.98896   -37.19474 1.000 30.35561 ? 65  THR   A C   1 
ATOM   405  O O   . THR   A 1 58  ? -12.29793 4.43767   -38.34226 1.000 36.24919 ? 65  THR   A O   1 
ATOM   406  C CB  . THR   A 1 58  ? -10.59559 5.62910   -36.22388 1.000 37.57450 ? 65  THR   A CB  1 
ATOM   407  O OG1 . THR   A 1 58  ? -9.55492  4.65559   -36.08607 1.000 36.38769 ? 65  THR   A OG1 1 
ATOM   408  C CG2 . THR   A 1 58  ? -10.40141 6.72599   -35.18660 1.000 29.79344 ? 65  THR   A CG2 1 
ATOM   409  N N   . ASP   A 1 59  ? -12.30450 2.68990   -36.92559 1.000 29.06383 ? 66  ASP   A N   1 
ATOM   410  C CA  . ASP   A 1 59  ? -12.49963 1.69032   -37.97495 1.000 27.38390 ? 66  ASP   A CA  1 
ATOM   411  C C   . ASP   A 1 59  ? -13.32991 0.57107   -37.37874 1.000 25.34330 ? 66  ASP   A C   1 
ATOM   412  O O   . ASP   A 1 59  ? -12.79351 -0.39626  -36.81834 1.000 26.39158 ? 66  ASP   A O   1 
ATOM   413  C CB  . ASP   A 1 59  ? -11.16133 1.16743   -38.49580 1.000 26.91624 ? 66  ASP   A CB  1 
ATOM   414  C CG  . ASP   A 1 59  ? -11.31627 0.16179   -39.62645 1.000 36.66707 ? 66  ASP   A CG  1 
ATOM   415  O OD1 . ASP   A 1 59  ? -12.46103 -0.13567  -40.02219 1.000 35.07018 ? 66  ASP   A OD1 1 
ATOM   416  O OD2 . ASP   A 1 59  ? -10.28187 -0.32157  -40.13357 1.000 37.74035 ? 66  ASP   A OD2 1 
ATOM   417  N N   . PRO   A 1 60  ? -14.65916 0.66266   -37.46697 1.000 28.84781 ? 67  PRO   A N   1 
ATOM   418  C CA  . PRO   A 1 60  ? -15.51211 -0.36732  -36.85716 1.000 27.46313 ? 67  PRO   A CA  1 
ATOM   419  C C   . PRO   A 1 60  ? -15.27649 -1.76344  -37.40453 1.000 25.33094 ? 67  PRO   A C   1 
ATOM   420  O O   . PRO   A 1 60  ? -15.54502 -2.73989  -36.69223 1.000 26.99659 ? 67  PRO   A O   1 
ATOM   421  C CB  . PRO   A 1 60  ? -16.93268 0.12523   -37.16477 1.000 31.70265 ? 67  PRO   A CB  1 
ATOM   422  C CG  . PRO   A 1 60  ? -16.77347 1.60695   -37.35136 1.000 39.54996 ? 67  PRO   A CG  1 
ATOM   423  C CD  . PRO   A 1 60  ? -15.45986 1.74523   -38.06768 1.000 36.62120 ? 67  PRO   A CD  1 
ATOM   424  N N   . SER   A 1 61  ? -14.77928 -1.89405  -38.63817 1.000 30.21553 ? 68  SER   A N   1 
ATOM   425  C CA  . SER   A 1 61  ? -14.53262 -3.21341  -39.20761 1.000 27.33914 ? 68  SER   A CA  1 
ATOM   426  C C   . SER   A 1 61  ? -13.45270 -3.98565  -38.46060 1.000 23.66553 ? 68  SER   A C   1 
ATOM   427  O O   . SER   A 1 61  ? -13.32338 -5.19523  -38.67460 1.000 25.03274 ? 68  SER   A O   1 
ATOM   428  C CB  . SER   A 1 61  ? -14.17796 -3.10603  -40.69277 1.000 28.68974 ? 68  SER   A CB  1 
ATOM   429  O OG  . SER   A 1 61  ? -12.86003 -2.61900  -40.86708 1.000 32.66514 ? 68  SER   A OG  1 
ATOM   430  N N   . LYS   A 1 62  ? -12.68078 -3.32373  -37.59119 1.000 23.40569 ? 69  LYS   A N   1 
ATOM   431  C CA  . LYS   A 1 62  ? -11.71745 -4.02963  -36.75538 1.000 24.58945 ? 69  LYS   A CA  1 
ATOM   432  C C   . LYS   A 1 62  ? -12.38451 -5.05388  -35.84837 1.000 22.16516 ? 69  LYS   A C   1 
ATOM   433  O O   . LYS   A 1 62  ? -11.71612 -5.98063  -35.37621 1.000 22.20956 ? 69  LYS   A O   1 
ATOM   434  C CB  . LYS   A 1 62  ? -10.93400 -3.02628  -35.90725 1.000 25.75593 ? 69  LYS   A CB  1 
ATOM   435  C CG  . LYS   A 1 62  ? -10.06418 -2.08483  -36.71847 1.000 29.37558 ? 69  LYS   A CG  1 
ATOM   436  C CD  . LYS   A 1 62  ? -8.66666  -2.65012  -36.85728 1.000 28.35287 ? 69  LYS   A CD  1 
ATOM   437  C CE  . LYS   A 1 62  ? -7.80758  -1.81054  -37.77999 1.000 29.46806 ? 69  LYS   A CE  1 
ATOM   438  N NZ  . LYS   A 1 62  ? -6.41151  -2.32817  -37.79692 1.000 33.15140 ? 69  LYS   A NZ  1 
ATOM   439  N N   . LEU   A 1 63  ? -13.68110 -4.90542  -35.58478 1.000 20.88090 ? 70  LEU   A N   1 
ATOM   440  C CA  . LEU   A 1 63  ? -14.41500 -5.83460  -34.73987 1.000 19.93572 ? 70  LEU   A CA  1 
ATOM   441  C C   . LEU   A 1 63  ? -15.22324 -6.84652  -35.54073 1.000 20.83212 ? 70  LEU   A C   1 
ATOM   442  O O   . LEU   A 1 63  ? -16.03097 -7.57397  -34.95488 1.000 25.03874 ? 70  LEU   A O   1 
ATOM   443  C CB  . LEU   A 1 63  ? -15.32584 -5.07383  -33.77293 1.000 22.49163 ? 70  LEU   A CB  1 
ATOM   444  C CG  . LEU   A 1 63  ? -14.62095 -4.13489  -32.79066 1.000 22.73884 ? 70  LEU   A CG  1 
ATOM   445  C CD1 . LEU   A 1 63  ? -15.63882 -3.40631  -31.93005 1.000 27.27477 ? 70  LEU   A CD1 1 
ATOM   446  C CD2 . LEU   A 1 63  ? -13.64118 -4.90438  -31.92172 1.000 22.16573 ? 70  LEU   A CD2 1 
ATOM   447  N N   . ASP   A 1 64  ? -15.01957 -6.91478  -36.86039 1.000 22.91184 ? 71  ASP   A N   1 
ATOM   448  C CA  . ASP   A 1 64  ? -15.70043 -7.93091  -37.66089 1.000 24.98064 ? 71  ASP   A CA  1 
ATOM   449  C C   . ASP   A 1 64  ? -15.33704 -9.33190  -37.19133 1.000 25.28859 ? 71  ASP   A C   1 
ATOM   450  O O   . ASP   A 1 64  ? -16.11818 -10.27314 -37.37152 1.000 28.00693 ? 71  ASP   A O   1 
ATOM   451  C CB  . ASP   A 1 64  ? -15.34305 -7.77510  -39.14131 1.000 27.00034 ? 71  ASP   A CB  1 
ATOM   452  C CG  . ASP   A 1 64  ? -16.02896 -6.58377  -39.79443 1.000 35.72670 ? 71  ASP   A CG  1 
ATOM   453  O OD1 . ASP   A 1 64  ? -16.86045 -5.92612  -39.13311 1.000 30.97774 ? 71  ASP   A OD1 1 
ATOM   454  O OD2 . ASP   A 1 64  ? -15.73154 -6.30506  -40.97680 1.000 35.65504 ? 71  ASP   A OD2 1 
ATOM   455  N N   . SER   A 1 65  ? -14.15611 -9.48476  -36.59872 1.000 22.04499 ? 72  SER   A N   1 
ATOM   456  C CA  . SER   A 1 65  ? -13.67371 -10.73654 -36.03420 1.000 22.43932 ? 72  SER   A CA  1 
ATOM   457  C C   . SER   A 1 65  ? -14.21641 -11.00932 -34.63563 1.000 27.07375 ? 72  SER   A C   1 
ATOM   458  O O   . SER   A 1 65  ? -13.76679 -11.95749 -33.98338 1.000 30.38190 ? 72  SER   A O   1 
ATOM   459  C CB  . SER   A 1 65  ? -12.14203 -10.72614 -36.01057 1.000 23.28868 ? 72  SER   A CB  1 
ATOM   460  O OG  . SER   A 1 65  ? -11.66045 -9.51800  -35.44203 1.000 23.15251 ? 72  SER   A OG  1 
ATOM   461  N N   . GLY   A 1 66  ? -15.16246 -10.20411 -34.15902 1.000 23.17258 ? 73  GLY   A N   1 
ATOM   462  C CA  . GLY   A 1 66  ? -15.73675 -10.40673 -32.84414 1.000 26.86959 ? 73  GLY   A CA  1 
ATOM   463  C C   . GLY   A 1 66  ? -16.00243 -9.09657  -32.13402 1.000 23.75919 ? 73  GLY   A C   1 
ATOM   464  O O   . GLY   A 1 66  ? -15.07291 -8.32892  -31.87729 1.000 21.67568 ? 73  GLY   A O   1 
ATOM   465  N N   . LYS   A 1 67  ? -17.26767 -8.82539  -31.80706 1.000 23.50298 ? 74  LYS   A N   1 
ATOM   466  C CA  . LYS   A 1 67  ? -17.60654 -7.54666  -31.19231 1.000 25.95101 ? 74  LYS   A CA  1 
ATOM   467  C C   . LYS   A 1 67  ? -17.44014 -7.56218  -29.67537 1.000 22.17074 ? 74  LYS   A C   1 
ATOM   468  O O   . LYS   A 1 67  ? -17.22283 -6.50542  -29.07243 1.000 26.58336 ? 74  LYS   A O   1 
ATOM   469  C CB  . LYS   A 1 67  ? -19.03831 -7.15124  -31.56104 1.000 30.86455 ? 74  LYS   A CB  1 
ATOM   470  C CG  . LYS   A 1 67  ? -19.17879 -6.59090  -32.96926 1.000 36.69889 ? 74  LYS   A CG  1 
ATOM   471  C CD  . LYS   A 1 67  ? -20.48924 -5.83263  -33.13813 1.000 48.43106 ? 74  LYS   A CD  1 
ATOM   472  C CE  . LYS   A 1 67  ? -20.87036 -5.69945  -34.60497 1.000 59.04666 ? 74  LYS   A CE  1 
ATOM   473  N NZ  . LYS   A 1 67  ? -20.08753 -6.62523  -35.46945 1.000 62.72117 ? 74  LYS   A NZ  1 
ATOM   474  N N   . GLU   A 1 68  ? -17.53724 -8.72975  -29.04392 1.000 20.94646 ? 75  GLU   A N   1 
ATOM   475  C CA  . GLU   A 1 68  ? -17.50705 -8.80628  -27.58801 1.000 22.38485 ? 75  GLU   A CA  1 
ATOM   476  C C   . GLU   A 1 68  ? -16.07949 -8.66393  -27.07863 1.000 19.30168 ? 75  GLU   A C   1 
ATOM   477  O O   . GLU   A 1 68  ? -15.16840 -9.32342  -27.58058 1.000 21.17010 ? 75  GLU   A O   1 
ATOM   478  C CB  . GLU   A 1 68  ? -18.09132 -10.13296 -27.09742 1.000 30.96652 ? 75  GLU   A CB  1 
ATOM   479  C CG  . GLU   A 1 68  ? -19.57916 -10.35642 -27.38560 1.000 39.38651 ? 75  GLU   A CG  1 
ATOM   480  C CD  . GLU   A 1 68  ? -19.90585 -10.45347 -28.86643 1.000 69.28319 ? 75  GLU   A CD  1 
ATOM   481  O OE1 . GLU   A 1 68  ? -20.96848 -9.94094  -29.28201 1.000 64.08927 ? 75  GLU   A OE1 1 
ATOM   482  O OE2 . GLU   A 1 68  ? -19.10327 -11.05178 -29.61378 1.000 56.70668 ? 75  GLU   A OE2 1 
ATOM   483  N N   . LEU   A 1 69  ? -15.89637 -7.81113  -26.07311 1.000 18.36416 ? 76  LEU   A N   1 
ATOM   484  C CA  . LEU   A 1 69  ? -14.59747 -7.56286  -25.45295 1.000 16.18719 ? 76  LEU   A CA  1 
ATOM   485  C C   . LEU   A 1 69  ? -14.66639 -8.09468  -24.02622 1.000 16.14121 ? 76  LEU   A C   1 
ATOM   486  O O   . LEU   A 1 69  ? -15.31500 -7.49145  -23.16350 1.000 17.68467 ? 76  LEU   A O   1 
ATOM   487  C CB  . LEU   A 1 69  ? -14.30622 -6.06360  -25.46701 1.000 18.05226 ? 76  LEU   A CB  1 
ATOM   488  C CG  . LEU   A 1 69  ? -14.21775 -5.41926  -26.85315 1.000 22.05357 ? 76  LEU   A CG  1 
ATOM   489  C CD1 . LEU   A 1 69  ? -13.77553 -3.96910  -26.74493 1.000 26.69856 ? 76  LEU   A CD1 1 
ATOM   490  C CD2 . LEU   A 1 69  ? -13.27409 -6.19701  -27.76489 1.000 20.21976 ? 76  LEU   A CD2 1 
ATOM   491  N N   . HIS   A 1 70  ? -14.00686 -9.22507  -23.77455 1.000 14.92042 ? 77  HIS   A N   1 
ATOM   492  C CA  . HIS   A 1 70  ? -14.18235 -9.89759  -22.49477 1.000 16.27124 ? 77  HIS   A CA  1 
ATOM   493  C C   . HIS   A 1 70  ? -12.97856 -10.77189 -22.18375 1.000 13.66928 ? 77  HIS   A C   1 
ATOM   494  O O   . HIS   A 1 70  ? -12.11603 -11.01330 -23.03384 1.000 13.49388 ? 77  HIS   A O   1 
ATOM   495  C CB  . HIS   A 1 70  ? -15.48416 -10.71138 -22.46075 1.000 17.24843 ? 77  HIS   A CB  1 
ATOM   496  C CG  . HIS   A 1 70  ? -15.56714 -11.78559 -23.50334 1.000 17.74239 ? 77  HIS   A CG  1 
ATOM   497  N ND1 . HIS   A 1 70  ? -14.62145 -12.77954 -23.64640 1.000 25.40603 ? 77  HIS   A ND1 1 
ATOM   498  C CD2 . HIS   A 1 70  ? -16.49200 -12.00870 -24.46637 1.000 24.16645 ? 77  HIS   A CD2 1 
ATOM   499  C CE1 . HIS   A 1 70  ? -14.96814 -13.57457 -24.64390 1.000 24.41457 ? 77  HIS   A CE1 1 
ATOM   500  N NE2 . HIS   A 1 70  ? -16.09640 -13.12560 -25.15990 1.000 27.08367 ? 77  HIS   A NE2 1 
ATOM   501  N N   . ILE   A 1 71  ? -12.96545 -11.26797 -20.94722 1.000 13.69593 ? 78  ILE   A N   1 
ATOM   502  C CA  . ILE   A 1 71  ? -11.93812 -12.15246 -20.41236 1.000 12.94796 ? 78  ILE   A CA  1 
ATOM   503  C C   . ILE   A 1 71  ? -12.63529 -13.35182 -19.78110 1.000 12.86861 ? 78  ILE   A C   1 
ATOM   504  O O   . ILE   A 1 71  ? -13.53639 -13.18123 -18.95112 1.000 14.67467 ? 78  ILE   A O   1 
ATOM   505  C CB  . ILE   A 1 71  ? -11.09022 -11.43425 -19.34617 1.000 13.56097 ? 78  ILE   A CB  1 
ATOM   506  C CG1 . ILE   A 1 71  ? -10.40529 -10.19614 -19.93156 1.000 15.30336 ? 78  ILE   A CG1 1 
ATOM   507  C CG2 . ILE   A 1 71  ? -10.07838 -12.40057 -18.73983 1.000 14.88901 ? 78  ILE   A CG2 1 
ATOM   508  C CD1 . ILE   A 1 71  ? -9.72400  -9.31776  -18.88689 1.000 15.64112 ? 78  ILE   A CD1 1 
ATOM   509  N N   . ASN   A 1 72  ? -12.23123 -14.55825 -20.17531 1.000 13.43064 ? 79  ASN   A N   1 
ATOM   510  C CA  . ASN   A 1 72  ? -12.75528 -15.78657 -19.59381 1.000 12.48124 ? 79  ASN   A CA  1 
ATOM   511  C C   . ASN   A 1 72  ? -11.63598 -16.53215 -18.88095 1.000 15.43369 ? 79  ASN   A C   1 
ATOM   512  O O   . ASN   A 1 72  ? -10.50732 -16.60883 -19.37925 1.000 14.26810 ? 79  ASN   A O   1 
ATOM   513  C CB  . ASN   A 1 72  ? -13.37517 -16.70956 -20.65696 1.000 13.74025 ? 79  ASN   A CB  1 
ATOM   514  C CG  . ASN   A 1 72  ? -14.59133 -16.10962 -21.31626 1.000 15.63110 ? 79  ASN   A CG  1 
ATOM   515  O OD1 . ASN   A 1 72  ? -15.33338 -15.34599 -20.70112 1.000 17.19225 ? 79  ASN   A OD1 1 
ATOM   516  N ND2 . ASN   A 1 72  ? -14.83071 -16.48776 -22.56596 1.000 20.34683 ? 79  ASN   A ND2 1 
ATOM   517  N N   . LEU   A 1 73  ? -11.95413 -17.09297 -17.71824 1.000 14.33978 ? 80  LEU   A N   1 
ATOM   518  C CA  . LEU   A 1 73  ? -11.02299 -17.91166 -16.95336 1.000 12.45645 ? 80  LEU   A CA  1 
ATOM   519  C C   . LEU   A 1 73  ? -11.59909 -19.31565 -16.92004 1.000 12.31574 ? 80  LEU   A C   1 
ATOM   520  O O   . LEU   A 1 73  ? -12.72164 -19.51867 -16.44186 1.000 14.26498 ? 80  LEU   A O   1 
ATOM   521  C CB  . LEU   A 1 73  ? -10.87231 -17.38108 -15.52911 1.000 13.82349 ? 80  LEU   A CB  1 
ATOM   522  C CG  . LEU   A 1 73  ? -10.53412 -15.89705 -15.39644 1.000 15.13871 ? 80  LEU   A CG  1 
ATOM   523  C CD1 . LEU   A 1 73  ? -10.48866 -15.50401 -13.92843 1.000 15.78238 ? 80  LEU   A CD1 1 
ATOM   524  C CD2 . LEU   A 1 73  ? -9.23749  -15.56279 -16.10523 1.000 15.97504 ? 80  LEU   A CD2 1 
ATOM   525  N N   . ILE   A 1 74  ? -10.85145 -20.27867 -17.44205 1.000 14.08166 ? 81  ILE   A N   1 
ATOM   526  C CA  . ILE   A 1 74  ? -11.36451 -21.61946 -17.67833 1.000 14.90275 ? 81  ILE   A CA  1 
ATOM   527  C C   . ILE   A 1 74  ? -10.45279 -22.62565 -16.98923 1.000 16.31448 ? 81  ILE   A C   1 
ATOM   528  O O   . ILE   A 1 74  ? -9.41972  -23.01854 -17.52078 1.000 15.97694 ? 81  ILE   A O   1 
ATOM   529  C CB  . ILE   A 1 74  ? -11.47340 -21.92243 -19.18719 1.000 16.68092 ? 81  ILE   A CB  1 
ATOM   530  C CG1 . ILE   A 1 74  ? -12.23542 -20.80063 -19.90330 1.000 17.84080 ? 81  ILE   A CG1 1 
ATOM   531  C CG2 . ILE   A 1 74  ? -12.14815 -23.26397 -19.39060 1.000 18.08090 ? 81  ILE   A CG2 1 
ATOM   532  C CD1 . ILE   A 1 74  ? -12.34618 -21.00553 -21.39963 1.000 20.73010 ? 81  ILE   A CD1 1 
ATOM   533  N N   . PRO   A 1 75  ? -10.82806 -23.08781 -15.79592 1.000 14.86527 ? 82  PRO   A N   1 
ATOM   534  C CA  . PRO   A 1 75  ? -10.07828 -24.16830 -15.15363 1.000 16.93161 ? 82  PRO   A CA  1 
ATOM   535  C C   . PRO   A 1 75  ? -10.53541 -25.52113 -15.67592 1.000 16.59868 ? 82  PRO   A C   1 
ATOM   536  O O   . PRO   A 1 75  ? -11.70795 -25.73239 -15.99053 1.000 19.30784 ? 82  PRO   A O   1 
ATOM   537  C CB  . PRO   A 1 75  ? -10.46104 -24.01397 -13.67773 1.000 18.62470 ? 82  PRO   A CB  1 
ATOM   538  C CG  . PRO   A 1 75  ? -11.85395 -23.45837 -13.71596 1.000 21.43507 ? 82  PRO   A CG  1 
ATOM   539  C CD  . PRO   A 1 75  ? -11.98544 -22.65200 -14.99453 1.000 20.40367 ? 82  PRO   A CD  1 
ATOM   540  N N   . ASN   A 1 76  ? -9.58058  -26.44461 -15.77316 1.000 17.49682 ? 83  ASN   A N   1 
ATOM   541  C CA  . ASN   A 1 76  ? -9.86764  -27.82066 -16.18381 1.000 19.70218 ? 83  ASN   A CA  1 
ATOM   542  C C   . ASN   A 1 76  ? -9.01590  -28.73876 -15.31413 1.000 19.93389 ? 83  ASN   A C   1 
ATOM   543  O O   . ASN   A 1 76  ? -7.81141  -28.87541 -15.54173 1.000 20.39402 ? 83  ASN   A O   1 
ATOM   544  C CB  . ASN   A 1 76  ? -9.59196  -28.03291 -17.66896 1.000 22.46395 ? 83  ASN   A CB  1 
ATOM   545  C CG  . ASN   A 1 76  ? -10.04889 -29.39956 -18.15995 1.000 26.43120 ? 83  ASN   A CG  1 
ATOM   546  O OD1 . ASN   A 1 76  ? -9.72350  -30.42826 -17.56881 1.000 27.10231 ? 83  ASN   A OD1 1 
ATOM   547  N ND2 . ASN   A 1 76  ? -10.83266 -29.40949 -19.23122 1.000 31.33539 ? 83  ASN   A ND2 1 
ATOM   548  N N   . LYS   A 1 77  ? -9.64926  -29.38161 -14.33055 1.000 22.82141 ? 84  LYS   A N   1 
ATOM   549  C CA  . LYS   A 1 77  ? -8.90201  -30.22438 -13.40233 1.000 22.06437 ? 84  LYS   A CA  1 
ATOM   550  C C   . LYS   A 1 77  ? -8.44286  -31.52477 -14.05053 1.000 25.29009 ? 84  LYS   A C   1 
ATOM   551  O O   . LYS   A 1 77  ? -7.44501  -32.10912 -13.61550 1.000 29.34088 ? 84  LYS   A O   1 
ATOM   552  C CB  . LYS   A 1 77  ? -9.74095  -30.52003 -12.15936 1.000 25.38482 ? 84  LYS   A CB  1 
ATOM   553  C CG  . LYS   A 1 77  ? -9.98766  -29.30383 -11.27585 1.000 29.43404 ? 84  LYS   A CG  1 
ATOM   554  C CD  . LYS   A 1 77  ? -10.78115 -29.68000 -10.03625 1.000 29.93555 ? 84  LYS   A CD  1 
ATOM   555  C CE  . LYS   A 1 77  ? -11.12407 -28.45899 -9.19731  1.000 32.79224 ? 84  LYS   A CE  1 
ATOM   556  N NZ  . LYS   A 1 77  ? -12.08256 -27.56351 -9.90349  1.000 38.13076 ? 84  LYS   A NZ  1 
ATOM   557  N N   . GLN   A 1 78  ? -9.15153  -31.99466 -15.08033 1.000 27.52365 ? 85  GLN   A N   1 
ATOM   558  C CA  . GLN   A 1 78  ? -8.74811  -33.23140 -15.74248 1.000 31.78329 ? 85  GLN   A CA  1 
ATOM   559  C C   . GLN   A 1 78  ? -7.45565  -33.03888 -16.52624 1.000 28.95251 ? 85  GLN   A C   1 
ATOM   560  O O   . GLN   A 1 78  ? -6.58509  -33.91731 -16.52415 1.000 35.59363 ? 85  GLN   A O   1 
ATOM   561  C CB  . GLN   A 1 78  ? -9.86742  -33.72583 -16.65688 1.000 38.69427 ? 85  GLN   A CB  1 
ATOM   562  C CG  . GLN   A 1 78  ? -10.76369 -34.77946 -16.02467 1.000 57.63784 ? 85  GLN   A CG  1 
ATOM   563  C CD  . GLN   A 1 78  ? -11.33578 -34.33632 -14.68886 1.000 69.29463 ? 85  GLN   A CD  1 
ATOM   564  O OE1 . GLN   A 1 78  ? -11.75555 -33.18877 -14.53026 1.000 66.67564 ? 85  GLN   A OE1 1 
ATOM   565  N NE2 . GLN   A 1 78  ? -11.35673 -35.24716 -13.72076 1.000 63.30697 ? 85  GLN   A NE2 1 
ATOM   566  N N   . ASP   A 1 79  ? -7.31355  -31.89790 -17.19455 1.000 26.70503 ? 86  ASP   A N   1 
ATOM   567  C CA  . ASP   A 1 79  ? -6.10914  -31.55757 -17.93813 1.000 27.44003 ? 86  ASP   A CA  1 
ATOM   568  C C   . ASP   A 1 79  ? -5.06882  -30.85825 -17.07569 1.000 25.79302 ? 86  ASP   A C   1 
ATOM   569  O O   . ASP   A 1 79  ? -3.93250  -30.67798 -17.52717 1.000 26.10746 ? 86  ASP   A O   1 
ATOM   570  C CB  . ASP   A 1 79  ? -6.46141  -30.63199 -19.10737 1.000 31.88552 ? 86  ASP   A CB  1 
ATOM   571  C CG  . ASP   A 1 79  ? -7.37885  -31.28722 -20.11640 1.000 36.58209 ? 86  ASP   A CG  1 
ATOM   572  O OD1 . ASP   A 1 79  ? -7.52792  -32.52642 -20.07850 1.000 41.64872 ? 86  ASP   A OD1 1 
ATOM   573  O OD2 . ASP   A 1 79  ? -7.95585  -30.55633 -20.94793 1.000 40.52224 ? 86  ASP   A OD2 1 
ATOM   574  N N   . ARG   A 1 80  ? -5.43370  -30.47921 -15.85303 1.000 23.17058 ? 87  ARG   A N   1 
ATOM   575  C CA  . ARG   A 1 80  ? -4.60944  -29.64209 -14.97820 1.000 20.22929 ? 87  ARG   A CA  1 
ATOM   576  C C   . ARG   A 1 80  ? -4.16074  -28.35841 -15.67389 1.000 18.58119 ? 87  ARG   A C   1 
ATOM   577  O O   . ARG   A 1 80  ? -2.97930  -28.00014 -15.67553 1.000 21.07159 ? 87  ARG   A O   1 
ATOM   578  C CB  . ARG   A 1 80  ? -3.42934  -30.40101 -14.36561 1.000 23.52215 ? 87  ARG   A CB  1 
ATOM   579  C CG  . ARG   A 1 80  ? -3.00418  -29.79535 -13.03588 1.000 22.55255 ? 87  ARG   A CG  1 
ATOM   580  C CD  . ARG   A 1 80  ? -1.57617  -30.10186 -12.65000 1.000 39.36042 ? 87  ARG   A CD  1 
ATOM   581  N NE  . ARG   A 1 80  ? -1.31868  -31.52726 -12.51839 1.000 46.30653 ? 87  ARG   A NE  1 
ATOM   582  C CZ  . ARG   A 1 80  ? -0.12737  -32.08470 -12.68169 1.000 47.96128 ? 87  ARG   A CZ  1 
ATOM   583  N NH1 . ARG   A 1 80  ? 0.93419   -31.36398 -13.00596 1.000 37.44352 ? 87  ARG   A NH1 1 
ATOM   584  N NH2 . ARG   A 1 80  ? 0.00391   -33.39582 -12.50777 1.000 46.79585 ? 87  ARG   A NH2 1 
ATOM   585  N N   . THR   A 1 81  ? -5.12103  -27.65314 -16.26709 1.000 17.61619 ? 88  THR   A N   1 
ATOM   586  C CA  . THR   A 1 81  ? -4.83376  -26.40904 -16.96173 1.000 17.17893 ? 88  THR   A CA  1 
ATOM   587  C C   . THR   A 1 81  ? -5.75146  -25.29809 -16.48083 1.000 18.98219 ? 88  THR   A C   1 
ATOM   588  O O   . THR   A 1 81  ? -6.91972  -25.52289 -16.15353 1.000 16.86100 ? 88  THR   A O   1 
ATOM   589  C CB  . THR   A 1 81  ? -4.98214  -26.52836 -18.48617 1.000 17.78126 ? 88  THR   A CB  1 
ATOM   590  O OG1 . THR   A 1 81  ? -6.30440  -26.98669 -18.81078 1.000 20.20788 ? 88  THR   A OG1 1 
ATOM   591  C CG2 . THR   A 1 81  ? -3.93974  -27.47575 -19.06521 1.000 18.44957 ? 88  THR   A CG2 1 
ATOM   592  N N   . LEU   A 1 82  ? -5.20256  -24.09092 -16.43509 1.000 15.30635 ? 89  LEU   A N   1 
ATOM   593  C CA  . LEU   A 1 82  ? -5.98738  -22.87853 -16.25775 1.000 14.39264 ? 89  LEU   A CA  1 
ATOM   594  C C   . LEU   A 1 82  ? -5.75772  -22.02874 -17.49682 1.000 15.59019 ? 89  LEU   A C   1 
ATOM   595  O O   . LEU   A 1 82  ? -4.61172  -21.71447 -17.83672 1.000 15.70129 ? 89  LEU   A O   1 
ATOM   596  C CB  . LEU   A 1 82  ? -5.56964  -22.11838 -14.99686 1.000 14.93305 ? 89  LEU   A CB  1 
ATOM   597  C CG  . LEU   A 1 82  ? -6.27993  -20.77718 -14.78500 1.000 14.48338 ? 89  LEU   A CG  1 
ATOM   598  C CD1 . LEU   A 1 82  ? -7.77436  -21.00190 -14.57748 1.000 16.23848 ? 89  LEU   A CD1 1 
ATOM   599  C CD2 . LEU   A 1 82  ? -5.69298  -20.03387 -13.59662 1.000 17.08286 ? 89  LEU   A CD2 1 
ATOM   600  N N   . THR   A 1 83  ? -6.83420  -21.70047 -18.19466 1.000 14.36578 ? 90  THR   A N   1 
ATOM   601  C CA  . THR   A 1 83  ? -6.75799  -20.95432 -19.43959 1.000 14.23436 ? 90  THR   A CA  1 
ATOM   602  C C   . THR   A 1 83  ? -7.34534  -19.56482 -19.23369 1.000 15.51819 ? 90  THR   A C   1 
ATOM   603  O O   . THR   A 1 83  ? -8.44184  -19.42431 -18.67789 1.000 15.66017 ? 90  THR   A O   1 
ATOM   604  C CB  . THR   A 1 83  ? -7.51947  -21.68943 -20.54305 1.000 15.72700 ? 90  THR   A CB  1 
ATOM   605  O OG1 . THR   A 1 83  ? -6.93983  -22.98507 -20.76240 1.000 16.89047 ? 90  THR   A OG1 1 
ATOM   606  C CG2 . THR   A 1 83  ? -7.47227  -20.89566 -21.82170 1.000 19.64918 ? 90  THR   A CG2 1 
ATOM   607  N N   . ILE   A 1 84  ? -6.60884  -18.54328 -19.65552 1.000 14.34955 ? 91  ILE   A N   1 
ATOM   608  C CA  . ILE   A 1 84  ? -7.07255  -17.16015 -19.62124 1.000 13.73947 ? 91  ILE   A CA  1 
ATOM   609  C C   . ILE   A 1 84  ? -7.31102  -16.74428 -21.06599 1.000 15.09927 ? 91  ILE   A C   1 
ATOM   610  O O   . ILE   A 1 84  ? -6.36041  -16.66126 -21.85354 1.000 15.99985 ? 91  ILE   A O   1 
ATOM   611  C CB  . ILE   A 1 84  ? -6.06822  -16.22339 -18.93450 1.000 14.94384 ? 91  ILE   A CB  1 
ATOM   612  C CG1 . ILE   A 1 84  ? -5.86220  -16.61413 -17.46588 1.000 20.85962 ? 91  ILE   A CG1 1 
ATOM   613  C CG2 . ILE   A 1 84  ? -6.56317  -14.78249 -19.01149 1.000 16.03457 ? 91  ILE   A CG2 1 
ATOM   614  C CD1 . ILE   A 1 84  ? -4.77860  -17.64988 -17.22273 1.000 24.74332 ? 91  ILE   A CD1 1 
ATOM   615  N N   . VAL   A 1 85  ? -8.56935  -16.48427 -21.41852 1.000 14.08590 ? 92  VAL   A N   1 
ATOM   616  C CA  . VAL   A 1 85  ? -8.97068  -16.15426 -22.78338 1.000 13.90294 ? 92  VAL   A CA  1 
ATOM   617  C C   . VAL   A 1 85  ? -9.38121  -14.69389 -22.82187 1.000 15.21606 ? 92  VAL   A C   1 
ATOM   618  O O   . VAL   A 1 85  ? -10.16113 -14.24362 -21.97665 1.000 16.32992 ? 92  VAL   A O   1 
ATOM   619  C CB  . VAL   A 1 85  ? -10.15018 -17.02481 -23.25508 1.000 16.74676 ? 92  VAL   A CB  1 
ATOM   620  C CG1 . VAL   A 1 85  ? -10.44393 -16.76928 -24.73070 1.000 20.56260 ? 92  VAL   A CG1 1 
ATOM   621  C CG2 . VAL   A 1 85  ? -9.88221  -18.49962 -23.00864 1.000 17.73955 ? 92  VAL   A CG2 1 
ATOM   622  N N   . ASP   A 1 86  ? -8.89862  -13.96293 -23.82076 1.000 14.73984 ? 93  ASP   A N   1 
ATOM   623  C CA  . ASP   A 1 86  ? -9.38993  -12.61543 -24.05370 1.000 13.81301 ? 93  ASP   A CA  1 
ATOM   624  C C   . ASP   A 1 86  ? -9.65287  -12.42988 -25.53948 1.000 15.25423 ? 93  ASP   A C   1 
ATOM   625  O O   . ASP   A 1 86  ? -9.08391  -13.12400 -26.38602 1.000 15.22275 ? 93  ASP   A O   1 
ATOM   626  C CB  . ASP   A 1 86  ? -8.44134  -11.53629 -23.49125 1.000 15.22301 ? 93  ASP   A CB  1 
ATOM   627  C CG  . ASP   A 1 86  ? -7.13333  -11.43101 -24.25942 1.000 18.96826 ? 93  ASP   A CG  1 
ATOM   628  O OD1 . ASP   A 1 86  ? -7.15516  -11.02891 -25.44424 1.000 17.43246 ? 93  ASP   A OD1 1 
ATOM   629  O OD2 . ASP   A 1 86  ? -6.07128  -11.75804 -23.68372 1.000 17.38928 ? 93  ASP   A OD2 1 
ATOM   630  N N   . THR   A 1 87  ? -10.53971 -11.49344 -25.85066 1.000 13.92284 ? 94  THR   A N   1 
ATOM   631  C CA  . THR   A 1 87  ? -10.82920 -11.13129 -27.23321 1.000 14.51025 ? 94  THR   A CA  1 
ATOM   632  C C   . THR   A 1 87  ? -10.16924 -9.81369  -27.61291 1.000 16.38538 ? 94  THR   A C   1 
ATOM   633  O O   . THR   A 1 87  ? -10.74735 -8.97740  -28.30476 1.000 15.83184 ? 94  THR   A O   1 
ATOM   634  C CB  . THR   A 1 87  ? -12.33183 -11.10135 -27.47175 1.000 16.35844 ? 94  THR   A CB  1 
ATOM   635  O OG1 . THR   A 1 87  ? -12.96611 -10.29620 -26.46992 1.000 17.50622 ? 94  THR   A OG1 1 
ATOM   636  C CG2 . THR   A 1 87  ? -12.89552 -12.51928 -27.38260 1.000 18.14998 ? 94  THR   A CG2 1 
ATOM   637  N N   . GLY   A 1 88  ? -8.94009  -9.61110  -27.15543 1.000 14.21120 ? 95  GLY   A N   1 
ATOM   638  C CA  . GLY   A 1 88  ? -8.20060  -8.40698  -27.46038 1.000 15.88275 ? 95  GLY   A CA  1 
ATOM   639  C C   . GLY   A 1 88  ? -7.62111  -8.41784  -28.85976 1.000 15.68987 ? 95  GLY   A C   1 
ATOM   640  O O   . GLY   A 1 88  ? -8.03611  -9.17730  -29.73930 1.000 14.93486 ? 95  GLY   A O   1 
ATOM   641  N N   . ILE   A 1 89  ? -6.62543  -7.55137  -29.05740 1.000 15.10009 ? 96  ILE   A N   1 
ATOM   642  C CA  . ILE   A 1 89  ? -6.07216  -7.32781  -30.38808 1.000 15.62180 ? 96  ILE   A CA  1 
ATOM   643  C C   . ILE   A 1 89  ? -5.31434  -8.54137  -30.91558 1.000 15.68378 ? 96  ILE   A C   1 
ATOM   644  O O   . ILE   A 1 89  ? -5.13986  -8.67872  -32.13044 1.000 16.46957 ? 96  ILE   A O   1 
ATOM   645  C CB  . ILE   A 1 89  ? -5.23779  -6.02990  -30.38953 1.000 15.25727 ? 96  ILE   A CB  1 
ATOM   646  C CG1 . ILE   A 1 89  ? -4.94067  -5.56427  -31.81643 1.000 18.94150 ? 96  ILE   A CG1 1 
ATOM   647  C CG2 . ILE   A 1 89  ? -3.96019  -6.20554  -29.56742 1.000 15.95959 ? 96  ILE   A CG2 1 
ATOM   648  C CD1 . ILE   A 1 89  ? -4.54157  -4.10172  -31.88579 1.000 20.08294 ? 96  ILE   A CD1 1 
ATOM   649  N N   . GLY   A 1 90  ? -4.86358  -9.43840  -30.04254 1.000 15.83955 ? 97  GLY   A N   1 
ATOM   650  C CA  . GLY   A 1 90  ? -4.10997  -10.58659 -30.50017 1.000 15.55415 ? 97  GLY   A CA  1 
ATOM   651  C C   . GLY   A 1 90  ? -2.67927  -10.21572 -30.84337 1.000 15.28208 ? 97  GLY   A C   1 
ATOM   652  O O   . GLY   A 1 90  ? -2.22538  -9.08661  -30.65488 1.000 17.65147 ? 97  GLY   A O   1 
ATOM   653  N N   . MET   A 1 91  ? -1.95803  -11.20308 -31.36724 1.000 14.35120 ? 98  MET   A N   1 
ATOM   654  C CA  . MET   A 1 91  ? -0.54377  -11.05979 -31.68201 1.000 14.62771 ? 98  MET   A CA  1 
ATOM   655  C C   . MET   A 1 91  ? -0.26891  -11.67354 -33.04308 1.000 15.77310 ? 98  MET   A C   1 
ATOM   656  O O   . MET   A 1 91  ? -0.77863  -12.75021 -33.36486 1.000 17.55744 ? 98  MET   A O   1 
ATOM   657  C CB  . MET   A 1 91  ? 0.28920   -11.79901 -30.62372 1.000 16.91357 ? 98  MET   A CB  1 
ATOM   658  C CG  . MET   A 1 91  ? 0.36425   -11.04759 -29.29751 1.000 17.29863 ? 98  MET   A CG  1 
ATOM   659  S SD  . MET   A 1 91  ? 1.43451   -11.82715 -28.08866 1.000 18.00865 ? 98  MET   A SD  1 
ATOM   660  C CE  . MET   A 1 91  ? 0.31112   -13.09167 -27.49926 1.000 20.29651 ? 98  MET   A CE  1 
ATOM   661  N N   . THR   A 1 92  ? 0.53347   -10.98347 -33.84516 1.000 16.72495 ? 99  THR   A N   1 
ATOM   662  C CA  . THR   A 1 92  ? 1.01145   -11.57384 -35.08486 1.000 17.45428 ? 99  THR   A CA  1 
ATOM   663  C C   . THR   A 1 92  ? 2.10386   -12.58935 -34.77418 1.000 18.50946 ? 99  THR   A C   1 
ATOM   664  O O   . THR   A 1 92  ? 2.59546   -12.68062 -33.64682 1.000 18.49209 ? 99  THR   A O   1 
ATOM   665  C CB  . THR   A 1 92  ? 1.59389   -10.49714 -35.99537 1.000 19.42131 ? 99  THR   A CB  1 
ATOM   666  O OG1 . THR   A 1 92  ? 2.75657   -9.93405  -35.36793 1.000 20.15755 ? 99  THR   A OG1 1 
ATOM   667  C CG2 . THR   A 1 92  ? 0.56660   -9.40019  -36.25307 1.000 24.17383 ? 99  THR   A CG2 1 
ATOM   668  N N   . LYS   A 1 93  ? 2.48458   -13.36513 -35.79476 1.000 18.63293 ? 100 LYS   A N   1 
ATOM   669  C CA  . LYS   A 1 93  ? 3.61809   -14.26991 -35.63516 1.000 17.57097 ? 100 LYS   A CA  1 
ATOM   670  C C   . LYS   A 1 93  ? 4.85921   -13.50933 -35.19461 1.000 19.32257 ? 100 LYS   A C   1 
ATOM   671  O O   . LYS   A 1 93  ? 5.58266   -13.95385 -34.29631 1.000 17.29789 ? 100 LYS   A O   1 
ATOM   672  C CB  . LYS   A 1 93  ? 3.90073   -15.02025 -36.93706 1.000 19.58031 ? 100 LYS   A CB  1 
ATOM   673  C CG  . LYS   A 1 93  ? 4.90522   -16.14469 -36.76123 1.000 21.29323 ? 100 LYS   A CG  1 
ATOM   674  C CD  . LYS   A 1 93  ? 5.24971   -16.80605 -38.08986 1.000 21.30810 ? 100 LYS   A CD  1 
ATOM   675  C CE  . LYS   A 1 93  ? 6.13653   -18.01223 -37.86362 1.000 26.60612 ? 100 LYS   A CE  1 
ATOM   676  N NZ  . LYS   A 1 93  ? 6.91532   -18.35941 -39.08506 1.000 28.22265 ? 100 LYS   A NZ  1 
ATOM   677  N N   . ALA   A 1 94  ? 5.11485   -12.35335 -35.81352 1.000 18.86532 ? 101 ALA   A N   1 
ATOM   678  C CA  . ALA   A 1 94  ? 6.27625   -11.55473 -35.43930 1.000 22.39898 ? 101 ALA   A CA  1 
ATOM   679  C C   . ALA   A 1 94  ? 6.19873   -11.11316 -33.98364 1.000 20.54431 ? 101 ALA   A C   1 
ATOM   680  O O   . ALA   A 1 94  ? 7.21338   -11.11513 -33.27569 1.000 20.44977 ? 101 ALA   A O   1 
ATOM   681  C CB  . ALA   A 1 94  ? 6.41082   -10.35186 -36.37215 1.000 22.30605 ? 101 ALA   A CB  1 
ATOM   682  N N   . ASP   A 1 95  ? 5.00158   -10.73531 -33.51650 1.000 18.76786 ? 102 ASP   A N   1 
ATOM   683  C CA  . ASP   A 1 95  ? 4.83066   -10.36628 -32.11389 1.000 17.28700 ? 102 ASP   A CA  1 
ATOM   684  C C   . ASP   A 1 95  ? 5.18002   -11.52930 -31.19778 1.000 15.65460 ? 102 ASP   A C   1 
ATOM   685  O O   . ASP   A 1 95  ? 5.87735   -11.35122 -30.19162 1.000 17.70644 ? 102 ASP   A O   1 
ATOM   686  C CB  . ASP   A 1 95  ? 3.38064   -9.94949  -31.84304 1.000 20.41039 ? 102 ASP   A CB  1 
ATOM   687  C CG  . ASP   A 1 95  ? 3.01633   -8.60919  -32.44843 1.000 25.09086 ? 102 ASP   A CG  1 
ATOM   688  O OD1 . ASP   A 1 95  ? 3.89595   -7.73561  -32.58699 1.000 25.62798 ? 102 ASP   A OD1 1 
ATOM   689  O OD2 . ASP   A 1 95  ? 1.82156   -8.42162  -32.77212 1.000 27.09329 ? 102 ASP   A OD2 1 
ATOM   690  N N   . LEU   A 1 96  ? 4.68894   -12.72861 -31.51914 1.000 16.06142 ? 103 LEU   A N   1 
ATOM   691  C CA  . LEU   A 1 96  ? 4.96853   -13.88979 -30.68175 1.000 18.76780 ? 103 LEU   A CA  1 
ATOM   692  C C   . LEU   A 1 96  ? 6.46222   -14.11076 -30.55121 1.000 18.26748 ? 103 LEU   A C   1 
ATOM   693  O O   . LEU   A 1 96  ? 6.98180   -14.27412 -29.44203 1.000 16.63903 ? 103 LEU   A O   1 
ATOM   694  C CB  . LEU   A 1 96  ? 4.33166   -15.14290 -31.27749 1.000 19.14923 ? 103 LEU   A CB  1 
ATOM   695  C CG  . LEU   A 1 96  ? 2.83832   -15.35105 -31.08586 1.000 16.79661 ? 103 LEU   A CG  1 
ATOM   696  C CD1 . LEU   A 1 96  ? 2.43587   -16.61241 -31.83678 1.000 17.48886 ? 103 LEU   A CD1 1 
ATOM   697  C CD2 . LEU   A 1 96  ? 2.48256   -15.43256 -29.60839 1.000 18.81429 ? 103 LEU   A CD2 1 
ATOM   698  N N   . ILE   A 1 97  ? 7.16845   -14.12340 -31.68519 1.000 16.80013 ? 104 ILE   A N   1 
ATOM   699  C CA  . ILE   A 1 97  ? 8.60530   -14.37768 -31.67164 1.000 17.43573 ? 104 ILE   A CA  1 
ATOM   700  C C   . ILE   A 1 97  ? 9.33152   -13.28005 -30.90946 1.000 17.40572 ? 104 ILE   A C   1 
ATOM   701  O O   . ILE   A 1 97  ? 10.29209  -13.54575 -30.17229 1.000 19.45528 ? 104 ILE   A O   1 
ATOM   702  C CB  . ILE   A 1 97  ? 9.13097   -14.53219 -33.11066 1.000 18.61499 ? 104 ILE   A CB  1 
ATOM   703  C CG1 . ILE   A 1 97  ? 8.53071   -15.78449 -33.75175 1.000 19.83056 ? 104 ILE   A CG1 1 
ATOM   704  C CG2 . ILE   A 1 97  ? 10.65713  -14.59479 -33.13062 1.000 19.33305 ? 104 ILE   A CG2 1 
ATOM   705  C CD1 . ILE   A 1 97  ? 8.63463   -15.80936 -35.26070 1.000 23.00700 ? 104 ILE   A CD1 1 
ATOM   706  N N   . ASN   A 1 98  ? 8.87119   -12.03527 -31.05559 1.000 16.15716 ? 105 ASN   A N   1 
ATOM   707  C CA  . ASN   A 1 98  ? 9.48147   -10.88567 -30.39104 1.000 18.88554 ? 105 ASN   A CA  1 
ATOM   708  C C   . ASN   A 1 98  ? 8.93552   -10.74360 -28.96635 1.000 17.48808 ? 105 ASN   A C   1 
ATOM   709  O O   . ASN   A 1 98  ? 8.38288   -9.71827  -28.56516 1.000 19.41928 ? 105 ASN   A O   1 
ATOM   710  C CB  . ASN   A 1 98  ? 9.26121   -9.62321  -31.21493 1.000 20.44419 ? 105 ASN   A CB  1 
ATOM   711  C CG  . ASN   A 1 98  ? 10.19091  -8.49605  -30.82047 1.000 44.28759 ? 105 ASN   A CG  1 
ATOM   712  O OD1 . ASN   A 1 98  ? 11.15713  -8.69454  -30.07746 1.000 42.89389 ? 105 ASN   A OD1 1 
ATOM   713  N ND2 . ASN   A 1 98  ? 9.91011   -7.30136  -31.32740 1.000 42.22035 ? 105 ASN   A ND2 1 
ATOM   714  N N   . ASN   A 1 99  ? 9.09298   -11.82717 -28.20461 1.000 17.32172 ? 106 ASN   A N   1 
ATOM   715  C CA  . ASN   A 1 99  ? 8.77295   -11.86430 -26.77648 1.000 16.60165 ? 106 ASN   A CA  1 
ATOM   716  C C   . ASN   A 1 99  ? 7.32255   -11.49469 -26.48936 1.000 18.83066 ? 106 ASN   A C   1 
ATOM   717  O O   . ASN   A 1 99  ? 7.02684   -10.73618 -25.56476 1.000 17.51701 ? 106 ASN   A O   1 
ATOM   718  C CB  . ASN   A 1 99  ? 9.74627   -11.01764 -25.95585 1.000 15.71028 ? 106 ASN   A CB  1 
ATOM   719  C CG  . ASN   A 1 99  ? 11.17875  -11.48385 -26.11782 1.000 15.55799 ? 106 ASN   A CG  1 
ATOM   720  O OD1 . ASN   A 1 99  ? 11.47735  -12.66561 -25.94252 1.000 18.73378 ? 106 ASN   A OD1 1 
ATOM   721  N ND2 . ASN   A 1 99  ? 12.06905  -10.56007 -26.45176 1.000 21.29991 ? 106 ASN   A ND2 1 
ATOM   722  N N   . LEU   A 1 100 ? 6.41598   -12.06332 -27.28308 1.000 14.93387 ? 107 LEU   A N   1 
ATOM   723  C CA  . LEU   A 1 100 ? 4.97664   -11.88727 -27.08136 1.000 15.12079 ? 107 LEU   A CA  1 
ATOM   724  C C   . LEU   A 1 100 ? 4.58427   -10.41194 -27.00759 1.000 17.13168 ? 107 LEU   A C   1 
ATOM   725  O O   . LEU   A 1 100 ? 3.80653   -9.98949  -26.14815 1.000 19.01863 ? 107 LEU   A O   1 
ATOM   726  C CB  . LEU   A 1 100 ? 4.47157   -12.69156 -25.88155 1.000 17.64690 ? 107 LEU   A CB  1 
ATOM   727  C CG  . LEU   A 1 100 ? 4.83063   -14.17792 -26.03029 1.000 23.03193 ? 107 LEU   A CG  1 
ATOM   728  C CD1 . LEU   A 1 100 ? 6.04554   -14.54560 -25.18787 1.000 20.09712 ? 107 LEU   A CD1 1 
ATOM   729  C CD2 . LEU   A 1 100 ? 3.65898   -15.08764 -25.71481 1.000 32.29294 ? 107 LEU   A CD2 1 
ATOM   730  N N   . GLY   A 1 101 ? 5.14107   -9.61783  -27.91988 1.000 16.88283 ? 108 GLY   A N   1 
ATOM   731  C CA  . GLY   A 1 101 ? 4.77217   -8.21828  -28.02084 1.000 18.44384 ? 108 GLY   A CA  1 
ATOM   732  C C   . GLY   A 1 101 ? 5.30682   -7.31810  -26.93147 1.000 21.60085 ? 108 GLY   A C   1 
ATOM   733  O O   . GLY   A 1 101 ? 4.79822   -6.20522  -26.75822 1.000 25.69756 ? 108 GLY   A O   1 
ATOM   734  N N   . THR   A 1 102 ? 6.32426   -7.75516  -26.19459 1.000 18.06308 ? 109 THR   A N   1 
ATOM   735  C CA  . THR   A 1 102 ? 6.89086   -6.97734  -25.10618 1.000 17.37687 ? 109 THR   A CA  1 
ATOM   736  C C   . THR   A 1 102 ? 8.27066   -6.46901  -25.49644 1.000 18.60306 ? 109 THR   A C   1 
ATOM   737  O O   . THR   A 1 102 ? 8.89398   -6.95648  -26.44356 1.000 21.54587 ? 109 THR   A O   1 
ATOM   738  C CB  . THR   A 1 102 ? 7.01997   -7.81830  -23.82779 1.000 19.02836 ? 109 THR   A CB  1 
ATOM   739  O OG1 . THR   A 1 102 ? 8.03851   -8.81290  -24.00398 1.000 19.86401 ? 109 THR   A OG1 1 
ATOM   740  C CG2 . THR   A 1 102 ? 5.71198   -8.50780  -23.49982 1.000 22.96556 ? 109 THR   A CG2 1 
ATOM   741  N N   . ILE   A 1 103 ? 8.74080   -5.47303  -24.75096 1.000 16.69601 ? 110 ILE   A N   1 
ATOM   742  C CA  . ILE   A 1 103 ? 10.13604  -5.05180  -24.82549 1.000 16.79158 ? 110 ILE   A CA  1 
ATOM   743  C C   . ILE   A 1 103 ? 10.91050  -5.75831  -23.71791 1.000 16.50783 ? 110 ILE   A C   1 
ATOM   744  O O   . ILE   A 1 103 ? 11.48837  -5.12390  -22.82574 1.000 16.93697 ? 110 ILE   A O   1 
ATOM   745  C CB  . ILE   A 1 103 ? 10.28365  -3.51855  -24.80574 1.000 22.84084 ? 110 ILE   A CB  1 
ATOM   746  C CG1 . ILE   A 1 103 ? 9.59077   -2.90587  -23.58613 1.000 21.60053 ? 110 ILE   A CG1 1 
ATOM   747  C CG2 . ILE   A 1 103 ? 9.70289   -2.92256  -26.08524 1.000 21.63353 ? 110 ILE   A CG2 1 
ATOM   748  C CD1 . ILE   A 1 103 ? 9.96144   -1.45295  -23.35021 1.000 26.06725 ? 110 ILE   A CD1 1 
ATOM   749  N N   . ALA   A 1 104 ? 10.94768  -7.09015  -23.79300 1.000 17.28376 ? 111 ALA   A N   1 
ATOM   750  C CA  . ALA   A 1 104 ? 11.36497  -7.89125  -22.64962 1.000 16.00985 ? 111 ALA   A CA  1 
ATOM   751  C C   . ALA   A 1 104 ? 12.83981  -7.71936  -22.30869 1.000 17.02707 ? 111 ALA   A C   1 
ATOM   752  O O   . ALA   A 1 104 ? 13.21363  -7.88740  -21.14476 1.000 20.50079 ? 111 ALA   A O   1 
ATOM   753  C CB  . ALA   A 1 104 ? 11.03733  -9.36905  -22.87670 1.000 19.01299 ? 111 ALA   A CB  1 
ATOM   754  N N   . LYS   A 1 105 ? 13.69428  -7.40372  -23.28563 1.000 18.30403 ? 112 LYS   A N   1 
ATOM   755  C CA  . LYS   A 1 105 ? 15.10948  -7.22851  -22.96876 1.000 22.53520 ? 112 LYS   A CA  1 
ATOM   756  C C   . LYS   A 1 105 ? 15.31464  -6.05214  -22.02023 1.000 26.67043 ? 112 LYS   A C   1 
ATOM   757  O O   . LYS   A 1 105 ? 15.90385  -6.20142  -20.94208 1.000 25.53293 ? 112 LYS   A O   1 
ATOM   758  C CB  . LYS   A 1 105 ? 15.93464  -7.06357  -24.24720 1.000 20.80172 ? 112 LYS   A CB  1 
ATOM   759  C CG  . LYS   A 1 105 ? 17.40697  -7.41744  -24.07766 1.000 36.99422 ? 112 LYS   A CG  1 
ATOM   760  C CD  . LYS   A 1 105 ? 18.26707  -6.84962  -25.19850 1.000 33.29251 ? 112 LYS   A CD  1 
ATOM   761  C CE  . LYS   A 1 105 ? 19.64459  -6.45539  -24.68593 1.000 40.20582 ? 112 LYS   A CE  1 
ATOM   762  N NZ  . LYS   A 1 105 ? 20.73643  -6.95726  -25.57117 1.000 48.04972 ? 112 LYS   A NZ  1 
ATOM   763  N N   . SER   A 1 106 ? 14.81779  -4.87116  -22.39633 1.000 23.50287 ? 113 SER   A N   1 
ATOM   764  C CA  . SER   A 1 106 ? 14.97696  -3.71404  -21.52377 1.000 25.66082 ? 113 SER   A CA  1 
ATOM   765  C C   . SER   A 1 106 ? 14.12703  -3.83853  -20.26603 1.000 24.90934 ? 113 SER   A C   1 
ATOM   766  O O   . SER   A 1 106 ? 14.51832  -3.33723  -19.20547 1.000 27.75665 ? 113 SER   A O   1 
ATOM   767  C CB  . SER   A 1 106 ? 14.66174  -2.42158  -22.27907 1.000 31.01400 ? 113 SER   A CB  1 
ATOM   768  O OG  . SER   A 1 106 ? 13.32685  -2.42303  -22.75265 1.000 30.86815 ? 113 SER   A OG  1 
ATOM   769  N N   . GLY   A 1 107 ? 12.97028  -4.49632  -20.35890 1.000 23.08278 ? 114 GLY   A N   1 
ATOM   770  C CA  . GLY   A 1 107 ? 12.15285  -4.69642  -19.17203 1.000 22.46915 ? 114 GLY   A CA  1 
ATOM   771  C C   . GLY   A 1 107 ? 12.82469  -5.59380  -18.15243 1.000 25.36185 ? 114 GLY   A C   1 
ATOM   772  O O   . GLY   A 1 107 ? 12.79151  -5.31633  -16.94972 1.000 23.49185 ? 114 GLY   A O   1 
ATOM   773  N N   . THR   A 1 108 ? 13.45700  -6.67441  -18.61842 1.000 21.01737 ? 115 THR   A N   1 
ATOM   774  C CA  . THR   A 1 108 ? 14.16851  -7.56503  -17.70645 1.000 24.04045 ? 115 THR   A CA  1 
ATOM   775  C C   . THR   A 1 108 ? 15.32094  -6.84291  -17.02473 1.000 25.47141 ? 115 THR   A C   1 
ATOM   776  O O   . THR   A 1 108 ? 15.51716  -6.98301  -15.81275 1.000 26.88123 ? 115 THR   A O   1 
ATOM   777  C CB  . THR   A 1 108 ? 14.67964  -8.78546  -18.47191 1.000 20.90037 ? 115 THR   A CB  1 
ATOM   778  O OG1 . THR   A 1 108 ? 13.55814  -9.51076  -18.99355 1.000 20.68455 ? 115 THR   A OG1 1 
ATOM   779  C CG2 . THR   A 1 108 ? 15.48663  -9.69177  -17.56051 1.000 24.84955 ? 115 THR   A CG2 1 
ATOM   780  N N   . LYS   A 1 109 ? 16.09172  -6.06561  -17.79176 1.000 27.21167 ? 116 LYS   A N   1 
ATOM   781  C CA  . LYS   A 1 109 ? 17.19273  -5.29106  -17.22756 1.000 30.93067 ? 116 LYS   A CA  1 
ATOM   782  C C   . LYS   A 1 109 ? 16.71066  -4.40117  -16.08805 1.000 34.26308 ? 116 LYS   A C   1 
ATOM   783  O O   . LYS   A 1 109 ? 17.29948  -4.38512  -15.00088 1.000 34.79636 ? 116 LYS   A O   1 
ATOM   784  C CB  . LYS   A 1 109 ? 17.84311  -4.45874  -18.33456 1.000 32.50504 ? 116 LYS   A CB  1 
ATOM   785  C CG  . LYS   A 1 109 ? 18.94215  -3.50999  -17.87086 1.000 38.98665 ? 116 LYS   A CG  1 
ATOM   786  C CD  . LYS   A 1 109 ? 19.40719  -2.62445  -19.02155 1.000 38.20281 ? 116 LYS   A CD  1 
ATOM   787  C CE  . LYS   A 1 109 ? 20.68994  -1.88039  -18.67943 1.000 49.73182 ? 116 LYS   A CE  1 
ATOM   788  N NZ  . LYS   A 1 109 ? 21.25035  -2.30300  -17.36877 1.000 63.38729 ? 116 LYS   A NZ  1 
ATOM   789  N N   . ALA   A 1 110 ? 15.62375  -3.66337  -16.31524 1.000 31.24209 ? 117 ALA   A N   1 
ATOM   790  C CA  . ALA   A 1 110 ? 15.10636  -2.78512  -15.27182 1.000 33.78430 ? 117 ALA   A CA  1 
ATOM   791  C C   . ALA   A 1 110 ? 14.58425  -3.58653  -14.08601 1.000 32.04099 ? 117 ALA   A C   1 
ATOM   792  O O   . ALA   A 1 110 ? 14.77156  -3.19196  -12.92884 1.000 34.12897 ? 117 ALA   A O   1 
ATOM   793  C CB  . ALA   A 1 110 ? 14.00718  -1.89310  -15.84524 1.000 31.90375 ? 117 ALA   A CB  1 
ATOM   794  N N   . PHE   A 1 111 ? 13.92948  -4.71566  -14.35804 1.000 29.28663 ? 118 PHE   A N   1 
ATOM   795  C CA  . PHE   A 1 111 ? 13.35015  -5.53038  -13.29469 1.000 28.02387 ? 118 PHE   A CA  1 
ATOM   796  C C   . PHE   A 1 111 ? 14.43326  -6.09061  -12.38138 1.000 31.59498 ? 118 PHE   A C   1 
ATOM   797  O O   . PHE   A 1 111 ? 14.32585  -6.02220  -11.15304 1.000 31.87409 ? 118 PHE   A O   1 
ATOM   798  C CB  . PHE   A 1 111 ? 12.53097  -6.65281  -13.92860 1.000 24.55765 ? 118 PHE   A CB  1 
ATOM   799  C CG  . PHE   A 1 111 ? 11.83632  -7.54533  -12.94465 1.000 23.65816 ? 118 PHE   A CG  1 
ATOM   800  C CD1 . PHE   A 1 111 ? 11.22997  -7.02836  -11.80782 1.000 24.99840 ? 118 PHE   A CD1 1 
ATOM   801  C CD2 . PHE   A 1 111 ? 11.73765  -8.90625  -13.18994 1.000 25.92704 ? 118 PHE   A CD2 1 
ATOM   802  C CE1 . PHE   A 1 111 ? 10.57342  -7.85984  -10.91750 1.000 24.51460 ? 118 PHE   A CE1 1 
ATOM   803  C CE2 . PHE   A 1 111 ? 11.07618  -9.74222  -12.30569 1.000 27.27518 ? 118 PHE   A CE2 1 
ATOM   804  C CZ  . PHE   A 1 111 ? 10.49143  -9.21503  -11.16670 1.000 27.68444 ? 118 PHE   A CZ  1 
ATOM   805  N N   . MET   A 1 112 ? 15.49623  -6.64074  -12.96299 1.000 31.56686 ? 119 MET   A N   1 
ATOM   806  C CA  . MET   A 1 112 ? 16.55099  -7.19428  -12.12457 1.000 35.35261 ? 119 MET   A CA  1 
ATOM   807  C C   . MET   A 1 112 ? 17.30128  -6.10533  -11.36704 1.000 43.84229 ? 119 MET   A C   1 
ATOM   808  O O   . MET   A 1 112 ? 17.78133  -6.35048  -10.25435 1.000 41.75279 ? 119 MET   A O   1 
ATOM   809  C CB  . MET   A 1 112 ? 17.47702  -8.07643  -12.95614 1.000 45.27178 ? 119 MET   A CB  1 
ATOM   810  C CG  . MET   A 1 112 ? 16.89528  -9.46586  -13.20332 1.000 29.41452 ? 119 MET   A CG  1 
ATOM   811  S SD  . MET   A 1 112 ? 17.97792  -10.42016 -14.27653 1.000 58.92194 ? 119 MET   A SD  1 
ATOM   812  C CE  . MET   A 1 112 ? 16.88006  -11.72811 -14.80074 1.000 32.47270 ? 119 MET   A CE  1 
ATOM   813  N N   . GLU   A 1 113 ? 17.39581  -4.89882  -11.93927 1.000 38.12174 ? 120 GLU   A N   1 
ATOM   814  C CA  . GLU   A 1 113 ? 17.96031  -3.77508  -11.19939 1.000 42.11627 ? 120 GLU   A CA  1 
ATOM   815  C C   . GLU   A 1 113 ? 17.03884  -3.31668  -10.08760 1.000 43.03684 ? 120 GLU   A C   1 
ATOM   816  O O   . GLU   A 1 113 ? 17.49019  -2.65370  -9.14491  1.000 48.20209 ? 120 GLU   A O   1 
ATOM   817  C CB  . GLU   A 1 113 ? 18.23153  -2.58608  -12.10957 1.000 46.81123 ? 120 GLU   A CB  1 
ATOM   818  C CG  . GLU   A 1 113 ? 19.40442  -2.74283  -13.02749 1.000 52.93465 ? 120 GLU   A CG  1 
ATOM   819  C CD  . GLU   A 1 113 ? 19.51256  -1.57122  -13.98012 1.000 69.17353 ? 120 GLU   A CD  1 
ATOM   820  O OE1 . GLU   A 1 113 ? 18.84082  -0.54544  -13.73368 1.000 77.60735 ? 120 GLU   A OE1 1 
ATOM   821  O OE2 . GLU   A 1 113 ? 20.26546  -1.66492  -14.96946 1.000 75.14932 ? 120 GLU   A OE2 1 
ATOM   822  N N   . ALA   A 1 114 ? 15.75903  -3.65635  -10.16183 1.000 38.58386 ? 121 ALA   A N   1 
ATOM   823  C CA  . ALA   A 1 114 ? 14.86466  -3.29840  -9.07073  1.000 38.96693 ? 121 ALA   A CA  1 
ATOM   824  C C   . ALA   A 1 114 ? 14.90502  -4.33976  -7.95994  1.000 39.04003 ? 121 ALA   A C   1 
ATOM   825  O O   . ALA   A 1 114 ? 14.71225  -4.00657  -6.78460  1.000 42.14023 ? 121 ALA   A O   1 
ATOM   826  C CB  . ALA   A 1 114 ? 13.43972  -3.09718  -9.58911  1.000 36.47858 ? 121 ALA   A CB  1 
ATOM   827  N N   . LEU   A 1 115 ? 15.16287  -5.60082  -8.31433  1.000 39.92515 ? 122 LEU   A N   1 
ATOM   828  C CA  . LEU   A 1 115 ? 15.12334  -6.68127  -7.33164  1.000 37.19260 ? 122 LEU   A CA  1 
ATOM   829  C C   . LEU   A 1 115 ? 16.28817  -6.59318  -6.34798  1.000 45.47189 ? 122 LEU   A C   1 
ATOM   830  O O   . LEU   A 1 115 ? 16.09845  -6.71322  -5.13305  1.000 47.03921 ? 122 LEU   A O   1 
ATOM   831  C CB  . LEU   A 1 115 ? 15.09127  -8.03824  -8.04109  1.000 35.71969 ? 122 LEU   A CB  1 
ATOM   832  C CG  . LEU   A 1 115 ? 13.81164  -8.36822  -8.81699  1.000 31.34067 ? 122 LEU   A CG  1 
ATOM   833  C CD1 . LEU   A 1 115 ? 13.96398  -9.64366  -9.62154  1.000 37.48781 ? 122 LEU   A CD1 1 
ATOM   834  C CD2 . LEU   A 1 115 ? 12.66361  -8.51492  -7.83679  1.000 33.28092 ? 122 LEU   A CD2 1 
ATOM   835  N N   . GLN   A 1 116 ? 17.50694  -6.40880  -6.85682  1.000 52.84137 ? 123 GLN   A N   1 
ATOM   836  C CA  . GLN   A 1 116 ? 18.68347  -6.25147  -6.00512  1.000 59.42007 ? 123 GLN   A CA  1 
ATOM   837  C C   . GLN   A 1 116 ? 18.64047  -4.96172  -5.19289  1.000 62.51206 ? 123 GLN   A C   1 
ATOM   838  O O   . GLN   A 1 116 ? 19.45406  -4.79173  -4.27771  1.000 68.56663 ? 123 GLN   A O   1 
ATOM   839  C CB  . GLN   A 1 116 ? 19.92770  -6.24999  -6.89482  1.000 54.23303 ? 123 GLN   A CB  1 
ATOM   840  C CG  . GLN   A 1 116 ? 20.32380  -7.62036  -7.42158  1.000 64.87981 ? 123 GLN   A CG  1 
ATOM   841  C CD  . GLN   A 1 116 ? 21.83035  -7.83759  -7.41944  1.000 92.95841 ? 123 GLN   A CD  1 
ATOM   842  O OE1 . GLN   A 1 116 ? 22.59828  -6.95474  -7.03251  1.000 96.08086 ? 123 GLN   A OE1 1 
ATOM   843  N NE2 . GLN   A 1 116 ? 22.25809  -9.02139  -7.84648  1.000 83.16298 ? 123 GLN   A NE2 1 
ATOM   844  N N   . ALA   A 1 117 ? 17.72252  -4.05042  -5.52536  1.000 59.47160 ? 124 ALA   A N   1 
ATOM   845  C CA  . ALA   A 1 117 ? 17.53041  -2.78323  -4.83234  1.000 57.44608 ? 124 ALA   A CA  1 
ATOM   846  C C   . ALA   A 1 117 ? 16.23769  -2.77493  -4.02322  1.000 71.88101 ? 124 ALA   A C   1 
ATOM   847  O O   . ALA   A 1 117 ? 15.65696  -1.71489  -3.77577  1.000 68.06331 ? 124 ALA   A O   1 
ATOM   848  C CB  . ALA   A 1 117 ? 17.54992  -1.61786  -5.82030  1.000 56.65591 ? 124 ALA   A CB  1 
ATOM   849  N N   . GLY   A 1 118 ? 15.75575  -3.95467  -3.63830  1.000 53.90223 ? 125 GLY   A N   1 
ATOM   850  C CA  . GLY   A 1 118 ? 14.69164  -4.08186  -2.66917  1.000 53.89457 ? 125 GLY   A CA  1 
ATOM   851  C C   . GLY   A 1 118 ? 13.37555  -4.58805  -3.21571  1.000 51.54565 ? 125 GLY   A C   1 
ATOM   852  O O   . GLY   A 1 118 ? 12.56445  -5.10601  -2.43739  1.000 51.75927 ? 125 GLY   A O   1 
ATOM   853  N N   . ALA   A 1 119 ? 13.12760  -4.45234  -4.51724  1.000 42.84721 ? 126 ALA   A N   1 
ATOM   854  C CA  . ALA   A 1 119 ? 11.84069  -4.86953  -5.05461  1.000 38.64841 ? 126 ALA   A CA  1 
ATOM   855  C C   . ALA   A 1 119 ? 11.67270  -6.37933  -4.93550  1.000 42.40558 ? 126 ALA   A C   1 
ATOM   856  O O   . ALA   A 1 119 ? 12.62333  -7.12414  -4.68318  1.000 38.92634 ? 126 ALA   A O   1 
ATOM   857  C CB  . ALA   A 1 119 ? 11.69774  -4.45677  -6.51912  1.000 36.71141 ? 126 ALA   A CB  1 
ATOM   858  N N   . ASP   A 1 120 ? 10.43635  -6.82770  -5.11766  1.000 37.81835 ? 127 ASP   A N   1 
ATOM   859  C CA  . ASP   A 1 120 ? 10.11881  -8.24383  -5.10842  1.000 34.34998 ? 127 ASP   A CA  1 
ATOM   860  C C   . ASP   A 1 120 ? 9.43171   -8.61885  -6.41320  1.000 29.44103 ? 127 ASP   A C   1 
ATOM   861  O O   . ASP   A 1 120 ? 9.07232   -7.76327  -7.22817  1.000 29.89979 ? 127 ASP   A O   1 
ATOM   862  C CB  . ASP   A 1 120 ? 9.23114   -8.61343  -3.91597  1.000 38.12445 ? 127 ASP   A CB  1 
ATOM   863  C CG  . ASP   A 1 120 ? 7.89197   -7.92005  -3.95658  1.000 43.99248 ? 127 ASP   A CG  1 
ATOM   864  O OD1 . ASP   A 1 120 ? 7.83337   -6.70783  -3.66231  1.000 51.94778 ? 127 ASP   A OD1 1 
ATOM   865  O OD2 . ASP   A 1 120 ? 6.90046   -8.59041  -4.30581  1.000 38.70107 ? 127 ASP   A OD2 1 
ATOM   866  N N   . ILE   A 1 121 ? 9.24531   -9.92897  -6.59425  1.000 31.35643 ? 128 ILE   A N   1 
ATOM   867  C CA  . ILE   A 1 121 ? 8.73354   -10.45923 -7.85426  1.000 26.79945 ? 128 ILE   A CA  1 
ATOM   868  C C   . ILE   A 1 121 ? 7.34146   -9.92273  -8.17269  1.000 29.28564 ? 128 ILE   A C   1 
ATOM   869  O O   . ILE   A 1 121 ? 6.97535   -9.79198  -9.34684  1.000 26.74201 ? 128 ILE   A O   1 
ATOM   870  C CB  . ILE   A 1 121 ? 8.82685   -12.00257 -7.84925  1.000 29.82981 ? 128 ILE   A CB  1 
ATOM   871  C CG1 . ILE   A 1 121 ? 10.29209  -12.43054 -8.00843  1.000 37.19644 ? 128 ILE   A CG1 1 
ATOM   872  C CG2 . ILE   A 1 121 ? 7.96101   -12.63104 -8.93691  1.000 28.76882 ? 128 ILE   A CG2 1 
ATOM   873  C CD1 . ILE   A 1 121 ? 10.57430  -13.86026 -7.60024  1.000 40.40416 ? 128 ILE   A CD1 1 
ATOM   874  N N   . SER   A 1 122 ? 6.56117   -9.55622  -7.15025  1.000 28.93720 ? 129 SER   A N   1 
ATOM   875  C CA  . SER   A 1 122 ? 5.19494   -9.09897  -7.40241  1.000 28.46441 ? 129 SER   A CA  1 
ATOM   876  C C   . SER   A 1 122 ? 5.13370   -7.81772  -8.22735  1.000 27.99539 ? 129 SER   A C   1 
ATOM   877  O O   . SER   A 1 122 ? 4.07412   -7.50705  -8.78114  1.000 31.30353 ? 129 SER   A O   1 
ATOM   878  C CB  . SER   A 1 122 ? 4.42379   -8.90206  -6.09500  1.000 27.97002 ? 129 SER   A CB  1 
ATOM   879  O OG  . SER   A 1 122 ? 4.80383   -7.70184  -5.45088  1.000 32.06029 ? 129 SER   A OG  1 
ATOM   880  N N   . MET   A 1 123 ? 6.22529   -7.06207  -8.32195  1.000 25.44958 ? 130 MET   A N   1 
ATOM   881  C CA  . MET   A 1 123 ? 6.22069   -5.83135  -9.10323  1.000 27.21116 ? 130 MET   A CA  1 
ATOM   882  C C   . MET   A 1 123 ? 6.61648   -6.03440  -10.56214 1.000 23.64549 ? 130 MET   A C   1 
ATOM   883  O O   . MET   A 1 123 ? 6.82294   -5.04867  -11.27694 1.000 24.18638 ? 130 MET   A O   1 
ATOM   884  C CB  . MET   A 1 123 ? 7.03712   -4.73274  -8.40909  1.000 37.40165 ? 130 MET   A CB  1 
ATOM   885  C CG  . MET   A 1 123 ? 6.88483   -4.75536  -6.88470  1.000 34.26022 ? 130 MET   A CG  1 
ATOM   886  S SD  . MET   A 1 123 ? 8.22772   -4.00848  -5.95380  1.000 41.61297 ? 130 MET   A SD  1 
ATOM   887  C CE  . MET   A 1 123 ? 8.41821   -2.46877  -6.84700  1.000 40.87777 ? 130 MET   A CE  1 
ATOM   888  N N   . ILE   A 1 124 ? 6.65949   -7.28865  -11.02403 1.000 21.29753 ? 131 ILE   A N   1 
ATOM   889  C CA  . ILE   A 1 124 ? 7.13308   -7.61081  -12.36957 1.000 19.32707 ? 131 ILE   A CA  1 
ATOM   890  C C   . ILE   A 1 124 ? 6.35247   -6.84588  -13.43514 1.000 18.32191 ? 131 ILE   A C   1 
ATOM   891  O O   . ILE   A 1 124 ? 6.91270   -6.44126  -14.46192 1.000 17.96398 ? 131 ILE   A O   1 
ATOM   892  C CB  . ILE   A 1 124 ? 7.07396   -9.13513  -12.59006 1.000 17.10983 ? 131 ILE   A CB  1 
ATOM   893  C CG1 . ILE   A 1 124 ? 7.71385   -9.50874  -13.93244 1.000 19.51397 ? 131 ILE   A CG1 1 
ATOM   894  C CG2 . ILE   A 1 124 ? 5.62747   -9.64617  -12.48605 1.000 19.46469 ? 131 ILE   A CG2 1 
ATOM   895  C CD1 . ILE   A 1 124 ? 7.82498   -11.00134 -14.15052 1.000 21.37168 ? 131 ILE   A CD1 1 
ATOM   896  N N   . GLY   A 1 125 ? 5.05334   -6.63992  -13.21548 1.000 20.79838 ? 132 GLY   A N   1 
ATOM   897  C CA  . GLY   A 1 125 ? 4.22937   -5.97678  -14.21148 1.000 21.10815 ? 132 GLY   A CA  1 
ATOM   898  C C   . GLY   A 1 125 ? 4.62213   -4.53893  -14.47057 1.000 24.65232 ? 132 GLY   A C   1 
ATOM   899  O O   . GLY   A 1 125 ? 4.34773   -4.01439  -15.55526 1.000 25.82902 ? 132 GLY   A O   1 
ATOM   900  N N   . GLN   A 1 126 ? 5.26298   -3.88769  -13.49980 1.000 22.16950 ? 133 GLN   A N   1 
ATOM   901  C CA  . GLN   A 1 126 ? 5.73120   -2.52259  -13.69233 1.000 24.29725 ? 133 GLN   A CA  1 
ATOM   902  C C   . GLN   A 1 126 ? 6.86946   -2.43754  -14.69798 1.000 24.59553 ? 133 GLN   A C   1 
ATOM   903  O O   . GLN   A 1 126 ? 7.24099   -1.32845  -15.09717 1.000 27.77298 ? 133 GLN   A O   1 
ATOM   904  C CB  . GLN   A 1 126 ? 6.17368   -1.93588  -12.35394 1.000 28.77876 ? 133 GLN   A CB  1 
ATOM   905  C CG  . GLN   A 1 126 ? 5.05484   -1.86862  -11.32434 1.000 29.39463 ? 133 GLN   A CG  1 
ATOM   906  C CD  . GLN   A 1 126 ? 5.50247   -1.26907  -10.00779 1.000 38.61843 ? 133 GLN   A CD  1 
ATOM   907  O OE1 . GLN   A 1 126 ? 6.21482   -0.26299  -9.97733  1.000 44.64211 ? 133 GLN   A OE1 1 
ATOM   908  N NE2 . GLN   A 1 126 ? 5.08617   -1.88699  -8.90758  1.000 45.49102 ? 133 GLN   A NE2 1 
ATOM   909  N N   . PHE   A 1 127 ? 7.42093   -3.57511  -15.11440 1.000 22.33906 ? 134 PHE   A N   1 
ATOM   910  C CA  . PHE   A 1 127 ? 8.52651   -3.61943  -16.06043 1.000 24.74764 ? 134 PHE   A CA  1 
ATOM   911  C C   . PHE   A 1 127 ? 8.12782   -4.24480  -17.39018 1.000 23.53915 ? 134 PHE   A C   1 
ATOM   912  O O   . PHE   A 1 127 ? 8.99924   -4.56054  -18.20641 1.000 23.94091 ? 134 PHE   A O   1 
ATOM   913  C CB  . PHE   A 1 127 ? 9.72440   -4.33066  -15.42718 1.000 23.13708 ? 134 PHE   A CB  1 
ATOM   914  C CG  . PHE   A 1 127 ? 10.10414  -3.75970  -14.09037 1.000 25.49871 ? 134 PHE   A CG  1 
ATOM   915  C CD1 . PHE   A 1 127 ? 10.93977  -2.65701  -14.00214 1.000 30.35770 ? 134 PHE   A CD1 1 
ATOM   916  C CD2 . PHE   A 1 127 ? 9.57917   -4.29002  -12.92449 1.000 25.53654 ? 134 PHE   A CD2 1 
ATOM   917  C CE1 . PHE   A 1 127 ? 11.27220  -2.11511  -12.77164 1.000 31.70926 ? 134 PHE   A CE1 1 
ATOM   918  C CE2 . PHE   A 1 127 ? 9.90787   -3.75345  -11.68827 1.000 28.31960 ? 134 PHE   A CE2 1 
ATOM   919  C CZ  . PHE   A 1 127 ? 10.75235  -2.66237  -11.61430 1.000 31.09531 ? 134 PHE   A CZ  1 
ATOM   920  N N   . GLY   A 1 128 ? 6.83132   -4.43325  -17.62468 1.000 21.42736 ? 135 GLY   A N   1 
ATOM   921  C CA  . GLY   A 1 128 ? 6.35419   -4.85550  -18.92157 1.000 18.73534 ? 135 GLY   A CA  1 
ATOM   922  C C   . GLY   A 1 128 ? 6.59636   -6.30576  -19.26010 1.000 18.09166 ? 135 GLY   A C   1 
ATOM   923  O O   . GLY   A 1 128 ? 6.45326   -6.68117  -20.42986 1.000 23.12369 ? 135 GLY   A O   1 
ATOM   924  N N   . VAL   A 1 129 ? 6.95335   -7.13630  -18.28228 1.000 16.83684 ? 136 VAL   A N   1 
ATOM   925  C CA  . VAL   A 1 129 ? 7.25491   -8.53753  -18.55077 1.000 15.13331 ? 136 VAL   A CA  1 
ATOM   926  C C   . VAL   A 1 129 ? 6.41662   -9.43766  -17.64921 1.000 15.42172 ? 136 VAL   A C   1 
ATOM   927  O O   . VAL   A 1 129 ? 6.82706   -10.54706 -17.29965 1.000 16.68490 ? 136 VAL   A O   1 
ATOM   928  C CB  . VAL   A 1 129 ? 8.76195   -8.81927  -18.40750 1.000 17.30638 ? 136 VAL   A CB  1 
ATOM   929  C CG1 . VAL   A 1 129 ? 9.51506   -8.17004  -19.56117 1.000 19.48018 ? 136 VAL   A CG1 1 
ATOM   930  C CG2 . VAL   A 1 129 ? 9.28818   -8.30364  -17.07088 1.000 19.10732 ? 136 VAL   A CG2 1 
ATOM   931  N N   . GLY   A 1 130 ? 5.21721   -8.96456  -17.28979 1.000 16.66027 ? 137 GLY   A N   1 
ATOM   932  C CA  . GLY   A 1 130 ? 4.35788   -9.72467  -16.39122 1.000 16.09500 ? 137 GLY   A CA  1 
ATOM   933  C C   . GLY   A 1 130 ? 3.93642   -11.08187 -16.92709 1.000 16.11541 ? 137 GLY   A C   1 
ATOM   934  O O   . GLY   A 1 130 ? 3.64282   -11.99260 -16.14382 1.000 15.36400 ? 137 GLY   A O   1 
ATOM   935  N N   . PHE   A 1 131 ? 3.89194   -11.24016 -18.25647 1.000 15.48329 ? 138 PHE   A N   1 
ATOM   936  C CA  . PHE   A 1 131 ? 3.53791   -12.53269 -18.83511 1.000 14.52787 ? 138 PHE   A CA  1 
ATOM   937  C C   . PHE   A 1 131 ? 4.37011   -13.65784 -18.23433 1.000 13.80020 ? 138 PHE   A C   1 
ATOM   938  O O   . PHE   A 1 131 ? 3.85146   -14.74588 -17.95700 1.000 14.34789 ? 138 PHE   A O   1 
ATOM   939  C CB  . PHE   A 1 131 ? 3.73694   -12.52574 -20.35670 1.000 15.90731 ? 138 PHE   A CB  1 
ATOM   940  C CG  . PHE   A 1 131 ? 3.72985   -13.90396 -20.96173 1.000 15.17999 ? 138 PHE   A CG  1 
ATOM   941  C CD1 . PHE   A 1 131 ? 2.53785   -14.58411 -21.14440 1.000 16.14633 ? 138 PHE   A CD1 1 
ATOM   942  C CD2 . PHE   A 1 131 ? 4.91819   -14.53597 -21.29774 1.000 15.67399 ? 138 PHE   A CD2 1 
ATOM   943  C CE1 . PHE   A 1 131 ? 2.52206   -15.86249 -21.67598 1.000 14.95355 ? 138 PHE   A CE1 1 
ATOM   944  C CE2 . PHE   A 1 131 ? 4.91175   -15.81964 -21.82660 1.000 15.46391 ? 138 PHE   A CE2 1 
ATOM   945  C CZ  . PHE   A 1 131 ? 3.71327   -16.48288 -22.01504 1.000 16.43431 ? 138 PHE   A CZ  1 
ATOM   946  N N   . TYR   A 1 132 ? 5.66980   -13.41846 -18.03351 1.000 14.29243 ? 139 TYR   A N   1 
ATOM   947  C CA  . TYR   A 1 132 ? 6.56333   -14.49270 -17.61736 1.000 14.82981 ? 139 TYR   A CA  1 
ATOM   948  C C   . TYR   A 1 132 ? 6.31300   -14.95206 -16.18768 1.000 15.13647 ? 139 TYR   A C   1 
ATOM   949  O O   . TYR   A 1 132 ? 6.80869   -16.01986 -15.80705 1.000 15.98360 ? 139 TYR   A O   1 
ATOM   950  C CB  . TYR   A 1 132 ? 8.02721   -14.09346 -17.85272 1.000 14.21301 ? 139 TYR   A CB  1 
ATOM   951  C CG  . TYR   A 1 132 ? 8.30491   -13.81805 -19.31999 1.000 15.12483 ? 139 TYR   A CG  1 
ATOM   952  C CD1 . TYR   A 1 132 ? 8.60109   -14.84963 -20.20178 1.000 15.75132 ? 139 TYR   A CD1 1 
ATOM   953  C CD2 . TYR   A 1 132 ? 8.21939   -12.52741 -19.82787 1.000 16.63323 ? 139 TYR   A CD2 1 
ATOM   954  C CE1 . TYR   A 1 132 ? 8.83412   -14.59541 -21.55392 1.000 15.12125 ? 139 TYR   A CE1 1 
ATOM   955  C CE2 . TYR   A 1 132 ? 8.44370   -12.26452 -21.16770 1.000 18.69469 ? 139 TYR   A CE2 1 
ATOM   956  C CZ  . TYR   A 1 132 ? 8.74811   -13.29787 -22.02705 1.000 14.91309 ? 139 TYR   A CZ  1 
ATOM   957  O OH  . TYR   A 1 132 ? 8.96645   -13.00694 -23.35727 1.000 18.41359 ? 139 TYR   A OH  1 
ATOM   958  N N   . SER   A 1 133 ? 5.53150   -14.19650 -15.40602 1.000 14.88821 ? 140 SER   A N   1 
ATOM   959  C CA  . SER   A 1 133 ? 5.09157   -14.66488 -14.09649 1.000 15.39939 ? 140 SER   A CA  1 
ATOM   960  C C   . SER   A 1 133 ? 4.23113   -15.91502 -14.19246 1.000 14.02626 ? 140 SER   A C   1 
ATOM   961  O O   . SER   A 1 133 ? 4.00421   -16.56551 -13.16657 1.000 16.15964 ? 140 SER   A O   1 
ATOM   962  C CB  . SER   A 1 133 ? 4.32745   -13.57445 -13.33227 1.000 15.11100 ? 140 SER   A CB  1 
ATOM   963  O OG  . SER   A 1 133 ? 3.04757   -13.32894 -13.89881 1.000 16.03574 ? 140 SER   A OG  1 
ATOM   964  N N   . ALA   A 1 134 ? 3.75331   -16.26464 -15.39198 1.000 14.39043 ? 141 ALA   A N   1 
ATOM   965  C CA  . ALA   A 1 134 ? 3.05892   -17.53725 -15.56924 1.000 14.13394 ? 141 ALA   A CA  1 
ATOM   966  C C   . ALA   A 1 134 ? 3.89110   -18.70660 -15.06422 1.000 13.09524 ? 141 ALA   A C   1 
ATOM   967  O O   . ALA   A 1 134 ? 3.33764   -19.69110 -14.56146 1.000 15.60578 ? 141 ALA   A O   1 
ATOM   968  C CB  . ALA   A 1 134 ? 2.71321   -17.74408 -17.04528 1.000 13.32652 ? 141 ALA   A CB  1 
ATOM   969  N N   . TYR   A 1 135 ? 5.22432   -18.60954 -15.16536 1.000 13.29905 ? 142 TYR   A N   1 
ATOM   970  C CA  . TYR   A 1 135 ? 6.09834   -19.70231 -14.75750 1.000 15.69749 ? 142 TYR   A CA  1 
ATOM   971  C C   . TYR   A 1 135 ? 6.25718   -19.81266 -13.24503 1.000 16.31879 ? 142 TYR   A C   1 
ATOM   972  O O   . TYR   A 1 135 ? 6.94970   -20.72087 -12.77543 1.000 17.44903 ? 142 TYR   A O   1 
ATOM   973  C CB  . TYR   A 1 135 ? 7.44247   -19.61514 -15.49659 1.000 14.86230 ? 142 TYR   A CB  1 
ATOM   974  C CG  . TYR   A 1 135 ? 7.24314   -19.90342 -16.96524 1.000 15.95649 ? 142 TYR   A CG  1 
ATOM   975  C CD1 . TYR   A 1 135 ? 7.24336   -21.21250 -17.44507 1.000 15.62767 ? 142 TYR   A CD1 1 
ATOM   976  C CD2 . TYR   A 1 135 ? 6.97858   -18.87384 -17.86463 1.000 14.92566 ? 142 TYR   A CD2 1 
ATOM   977  C CE1 . TYR   A 1 135 ? 7.01944   -21.48245 -18.78760 1.000 15.47806 ? 142 TYR   A CE1 1 
ATOM   978  C CE2 . TYR   A 1 135 ? 6.75107   -19.13694 -19.20745 1.000 14.66499 ? 142 TYR   A CE2 1 
ATOM   979  C CZ  . TYR   A 1 135 ? 6.77504   -20.44097 -19.66076 1.000 14.75412 ? 142 TYR   A CZ  1 
ATOM   980  O OH  . TYR   A 1 135 ? 6.55404   -20.71000 -20.99021 1.000 15.88582 ? 142 TYR   A OH  1 
ATOM   981  N N   . LEU   A 1 136 ? 5.62188   -18.92402 -12.47607 1.000 16.22469 ? 143 LEU   A N   1 
ATOM   982  C CA  . LEU   A 1 136 ? 5.48928   -19.15372 -11.04261 1.000 16.39697 ? 143 LEU   A CA  1 
ATOM   983  C C   . LEU   A 1 136 ? 4.63414   -20.37853 -10.75807 1.000 15.67159 ? 143 LEU   A C   1 
ATOM   984  O O   . LEU   A 1 136 ? 4.83381   -21.05410 -9.74526  1.000 18.48373 ? 143 LEU   A O   1 
ATOM   985  C CB  . LEU   A 1 136 ? 4.85185   -17.93396 -10.37295 1.000 17.74075 ? 143 LEU   A CB  1 
ATOM   986  C CG  . LEU   A 1 136 ? 5.65270   -16.63051 -10.32689 1.000 17.16509 ? 143 LEU   A CG  1 
ATOM   987  C CD1 . LEU   A 1 136 ? 4.76366   -15.47897 -9.86093  1.000 18.42724 ? 143 LEU   A CD1 1 
ATOM   988  C CD2 . LEU   A 1 136 ? 6.86639   -16.78026 -9.40940  1.000 18.94944 ? 143 LEU   A CD2 1 
ATOM   989  N N   . VAL   A 1 137 ? 3.67523   -20.67803 -11.63551 1.000 16.11150 ? 144 VAL   A N   1 
ATOM   990  C CA  . VAL   A 1 137 ? 2.72137   -21.75240 -11.37818 1.000 17.73685 ? 144 VAL   A CA  1 
ATOM   991  C C   . VAL   A 1 137 ? 2.66613   -22.79748 -12.47828 1.000 17.53325 ? 144 VAL   A C   1 
ATOM   992  O O   . VAL   A 1 137 ? 2.14669   -23.90227 -12.23674 1.000 18.76891 ? 144 VAL   A O   1 
ATOM   993  C CB  . VAL   A 1 137 ? 1.30604   -21.20166 -11.08488 1.000 17.39012 ? 144 VAL   A CB  1 
ATOM   994  C CG1 . VAL   A 1 137 ? 1.31728   -20.34579 -9.82017  1.000 17.33597 ? 144 VAL   A CG1 1 
ATOM   995  C CG2 . VAL   A 1 137 ? 0.76147   -20.41735 -12.27657 1.000 15.94004 ? 144 VAL   A CG2 1 
ATOM   996  N N   . ALA   A 1 138 ? 3.18049   -22.52472 -13.67414 1.000 16.84406 ? 145 ALA   A N   1 
ATOM   997  C CA  . ALA   A 1 138 ? 3.03280   -23.41222 -14.82190 1.000 16.73680 ? 145 ALA   A CA  1 
ATOM   998  C C   . ALA   A 1 138 ? 4.36863   -24.04809 -15.17404 1.000 17.60836 ? 145 ALA   A C   1 
ATOM   999  O O   . ALA   A 1 138 ? 5.39005   -23.35516 -15.25222 1.000 19.72138 ? 145 ALA   A O   1 
ATOM   1000 C CB  . ALA   A 1 138 ? 2.51049   -22.63884 -16.03360 1.000 18.14988 ? 145 ALA   A CB  1 
ATOM   1001 N N   . GLU   A 1 139 ? 4.35090   -25.36250 -15.40664 1.000 17.69504 ? 146 GLU   A N   1 
ATOM   1002 C CA  . GLU   A 1 139 ? 5.51292   -26.03637 -15.97201 1.000 18.68374 ? 146 GLU   A CA  1 
ATOM   1003 C C   . GLU   A 1 139 ? 5.61354   -25.83806 -17.47576 1.000 19.99056 ? 146 GLU   A C   1 
ATOM   1004 O O   . GLU   A 1 139 ? 6.71001   -25.94249 -18.03506 1.000 20.12264 ? 146 GLU   A O   1 
ATOM   1005 C CB  . GLU   A 1 139 ? 5.47798   -27.53128 -15.64254 1.000 20.80101 ? 146 GLU   A CB  1 
ATOM   1006 C CG  . GLU   A 1 139 ? 4.27449   -28.26828 -16.20087 1.000 27.72862 ? 146 GLU   A CG  1 
ATOM   1007 C CD  . GLU   A 1 139 ? 4.18529   -29.70072 -15.70824 1.000 49.25969 ? 146 GLU   A CD  1 
ATOM   1008 O OE1 . GLU   A 1 139 ? 4.76598   -30.00386 -14.64379 1.000 38.74455 ? 146 GLU   A OE1 1 
ATOM   1009 O OE2 . GLU   A 1 139 ? 3.53339   -30.52264 -16.38892 1.000 46.49872 ? 146 GLU   A OE2 1 
ATOM   1010 N N   . LYS   A 1 140 ? 4.49645   -25.55436 -18.13787 1.000 17.19594 ? 147 LYS   A N   1 
ATOM   1011 C CA  . LYS   A 1 140 ? 4.47497   -25.29462 -19.56696 1.000 16.87682 ? 147 LYS   A CA  1 
ATOM   1012 C C   . LYS   A 1 140 ? 3.38666   -24.26633 -19.81140 1.000 14.07035 ? 147 LYS   A C   1 
ATOM   1013 O O   . LYS   A 1 140 ? 2.36123   -24.27158 -19.12759 1.000 15.77563 ? 147 LYS   A O   1 
ATOM   1014 C CB  . LYS   A 1 140 ? 4.19294   -26.57489 -20.36299 1.000 17.00317 ? 147 LYS   A CB  1 
ATOM   1015 C CG  . LYS   A 1 140 ? 4.11565   -26.38501 -21.87635 1.000 17.84013 ? 147 LYS   A CG  1 
ATOM   1016 C CD  . LYS   A 1 140 ? 4.09958   -27.73148 -22.58289 1.000 22.82911 ? 147 LYS   A CD  1 
ATOM   1017 C CE  . LYS   A 1 140 ? 2.69847   -28.29607 -22.68094 1.000 27.54276 ? 147 LYS   A CE  1 
ATOM   1018 N NZ  . LYS   A 1 140 ? 2.71697   -29.69275 -23.20921 1.000 36.87356 ? 147 LYS   A NZ  1 
ATOM   1019 N N   . VAL   A 1 141 ? 3.62978   -23.36550 -20.75473 1.000 14.03847 ? 148 VAL   A N   1 
ATOM   1020 C CA  . VAL   A 1 141 ? 2.64723   -22.36429 -21.14188 1.000 13.86141 ? 148 VAL   A CA  1 
ATOM   1021 C C   . VAL   A 1 141 ? 2.45273   -22.45871 -22.64482 1.000 16.35770 ? 148 VAL   A C   1 
ATOM   1022 O O   . VAL   A 1 141 ? 3.43196   -22.48633 -23.39877 1.000 14.69899 ? 148 VAL   A O   1 
ATOM   1023 C CB  . VAL   A 1 141 ? 3.08613   -20.94343 -20.74632 1.000 13.86821 ? 148 VAL   A CB  1 
ATOM   1024 C CG1 . VAL   A 1 141 ? 2.05705   -19.92237 -21.24502 1.000 16.32727 ? 148 VAL   A CG1 1 
ATOM   1025 C CG2 . VAL   A 1 141 ? 3.28783   -20.84393 -19.23161 1.000 14.88793 ? 148 VAL   A CG2 1 
ATOM   1026 N N   . THR   A 1 142 ? 1.19666   -22.53121 -23.07592 1.000 14.31204 ? 149 THR   A N   1 
ATOM   1027 C CA  . THR   A 1 142 ? 0.83334   -22.49107 -24.48386 1.000 14.93121 ? 149 THR   A CA  1 
ATOM   1028 C C   . THR   A 1 142 ? 0.02619   -21.22678 -24.72817 1.000 17.60926 ? 149 THR   A C   1 
ATOM   1029 O O   . THR   A 1 142 ? -0.90635  -20.93086 -23.97656 1.000 16.90504 ? 149 THR   A O   1 
ATOM   1030 C CB  . THR   A 1 142 ? -0.00988  -23.71092 -24.86768 1.000 16.31009 ? 149 THR   A CB  1 
ATOM   1031 O OG1 . THR   A 1 142 ? 0.64917   -24.91905 -24.45375 1.000 20.13965 ? 149 THR   A OG1 1 
ATOM   1032 C CG2 . THR   A 1 142 ? -0.24111  -23.74182 -26.37063 1.000 19.04900 ? 149 THR   A CG2 1 
ATOM   1033 N N   . VAL   A 1 143 ? 0.38991   -20.47742 -25.75952 1.000 13.99038 ? 150 VAL   A N   1 
ATOM   1034 C CA  . VAL   A 1 143 ? -0.29334  -19.23615 -26.10149 1.000 13.47423 ? 150 VAL   A CA  1 
ATOM   1035 C C   . VAL   A 1 143 ? -0.84453  -19.39134 -27.51126 1.000 15.67403 ? 150 VAL   A C   1 
ATOM   1036 O O   . VAL   A 1 143 ? -0.07475  -19.55518 -28.46703 1.000 16.62504 ? 150 VAL   A O   1 
ATOM   1037 C CB  . VAL   A 1 143 ? 0.64272   -18.02279 -26.00293 1.000 14.07253 ? 150 VAL   A CB  1 
ATOM   1038 C CG1 . VAL   A 1 143 ? -0.07766  -16.75173 -26.44360 1.000 18.09647 ? 150 VAL   A CG1 1 
ATOM   1039 C CG2 . VAL   A 1 143 ? 1.20260   -17.88211 -24.59186 1.000 14.83979 ? 150 VAL   A CG2 1 
ATOM   1040 N N   . ILE   A 1 144 ? -2.17143  -19.36787 -27.63962 1.000 14.11867 ? 151 ILE   A N   1 
ATOM   1041 C CA  . ILE   A 1 144 ? -2.85261  -19.39909 -28.93201 1.000 14.56767 ? 151 ILE   A CA  1 
ATOM   1042 C C   . ILE   A 1 144 ? -3.34406  -17.99050 -29.21210 1.000 14.89914 ? 151 ILE   A C   1 
ATOM   1043 O O   . ILE   A 1 144 ? -3.94461  -17.35612 -28.33593 1.000 16.45066 ? 151 ILE   A O   1 
ATOM   1044 C CB  . ILE   A 1 144 ? -4.04825  -20.36412 -28.91341 1.000 17.35236 ? 151 ILE   A CB  1 
ATOM   1045 C CG1 . ILE   A 1 144 ? -3.70448  -21.67838 -28.21053 1.000 27.46405 ? 151 ILE   A CG1 1 
ATOM   1046 C CG2 . ILE   A 1 144 ? -4.56307  -20.58277 -30.33776 1.000 18.13144 ? 151 ILE   A CG2 1 
ATOM   1047 C CD1 . ILE   A 1 144 ? -2.82092  -22.58051 -29.00264 1.000 26.73378 ? 151 ILE   A CD1 1 
ATOM   1048 N N   . THR   A 1 145 ? -3.10126  -17.49238 -30.41918 1.000 14.68999 ? 152 THR   A N   1 
ATOM   1049 C CA  . THR   A 1 145 ? -3.39308  -16.08929 -30.67588 1.000 14.19086 ? 152 THR   A CA  1 
ATOM   1050 C C   . THR   A 1 145 ? -3.82117  -15.89107 -32.12200 1.000 16.24191 ? 152 THR   A C   1 
ATOM   1051 O O   . THR   A 1 145 ? -3.39839  -16.62413 -33.02220 1.000 16.21644 ? 152 THR   A O   1 
ATOM   1052 C CB  . THR   A 1 145 ? -2.20780  -15.18393 -30.28744 1.000 14.68989 ? 152 THR   A CB  1 
ATOM   1053 O OG1 . THR   A 1 145 ? -2.62907  -13.81265 -30.25053 1.000 17.12486 ? 152 THR   A OG1 1 
ATOM   1054 C CG2 . THR   A 1 145 ? -1.04175  -15.34141 -31.26121 1.000 17.26770 ? 152 THR   A CG2 1 
ATOM   1055 N N   . LYS   A 1 146 ? -4.67817  -14.89193 -32.32682 1.000 16.42477 ? 153 LYS   A N   1 
ATOM   1056 C CA  . LYS   A 1 146 ? -5.16627  -14.52233 -33.65049 1.000 15.67611 ? 153 LYS   A CA  1 
ATOM   1057 C C   . LYS   A 1 146 ? -5.29335  -13.00965 -33.68929 1.000 17.19684 ? 153 LYS   A C   1 
ATOM   1058 O O   . LYS   A 1 146 ? -6.07083  -12.42816 -32.92587 1.000 17.37149 ? 153 LYS   A O   1 
ATOM   1059 C CB  . LYS   A 1 146 ? -6.52358  -15.16840 -33.94237 1.000 16.28386 ? 153 LYS   A CB  1 
ATOM   1060 C CG  . LYS   A 1 146 ? -7.17147  -14.74513 -35.27055 1.000 17.11871 ? 153 LYS   A CG  1 
ATOM   1061 C CD  . LYS   A 1 146 ? -6.36249  -15.21652 -36.47940 1.000 19.64133 ? 153 LYS   A CD  1 
ATOM   1062 C CE  . LYS   A 1 146 ? -7.06370  -14.88336 -37.80055 1.000 20.11476 ? 153 LYS   A CE  1 
ATOM   1063 N NZ  . LYS   A 1 146 ? -7.04425  -13.42833 -38.12459 1.000 20.91545 ? 153 LYS   A NZ  1 
ATOM   1064 N N   . HIS   A 1 147 ? -4.51637  -12.38522 -34.56000 1.000 16.53951 ? 154 HIS   A N   1 
ATOM   1065 C CA  . HIS   A 1 147 ? -4.56743  -10.95889 -34.82835 1.000 16.30308 ? 154 HIS   A CA  1 
ATOM   1066 C C   . HIS   A 1 147 ? -5.24957  -10.75368 -36.17852 1.000 18.95121 ? 154 HIS   A C   1 
ATOM   1067 O O   . HIS   A 1 147 ? -5.16032  -11.60440 -37.06797 1.000 20.69567 ? 154 HIS   A O   1 
ATOM   1068 C CB  . HIS   A 1 147 ? -3.12536  -10.43738 -34.85912 1.000 17.42467 ? 154 HIS   A CB  1 
ATOM   1069 C CG  . HIS   A 1 147 ? -3.00133  -8.95196  -34.98039 1.000 16.95671 ? 154 HIS   A CG  1 
ATOM   1070 N ND1 . HIS   A 1 147 ? -3.18958  -8.28110  -36.16839 1.000 19.83844 ? 154 HIS   A ND1 1 
ATOM   1071 C CD2 . HIS   A 1 147 ? -2.66661  -8.01105  -34.06545 1.000 19.73832 ? 154 HIS   A CD2 1 
ATOM   1072 C CE1 . HIS   A 1 147 ? -2.99766  -6.98836  -35.97626 1.000 22.64208 ? 154 HIS   A CE1 1 
ATOM   1073 N NE2 . HIS   A 1 147 ? -2.67617  -6.79901  -34.70930 1.000 22.16628 ? 154 HIS   A NE2 1 
ATOM   1074 N N   . ASN   A 1 148 ? -5.95993  -9.62844  -36.32178 1.000 17.88433 ? 155 ASN   A N   1 
ATOM   1075 C CA  . ASN   A 1 148 ? -6.67557  -9.36253  -37.57098 1.000 20.04121 ? 155 ASN   A CA  1 
ATOM   1076 C C   . ASN   A 1 148 ? -5.76834  -9.45604  -38.79444 1.000 19.85730 ? 155 ASN   A C   1 
ATOM   1077 O O   . ASN   A 1 148 ? -6.23197  -9.81670  -39.88325 1.000 23.80563 ? 155 ASN   A O   1 
ATOM   1078 C CB  . ASN   A 1 148 ? -7.34081  -7.97823  -37.53796 1.000 21.24816 ? 155 ASN   A CB  1 
ATOM   1079 C CG  . ASN   A 1 148 ? -8.61224  -7.95257  -36.71292 1.000 21.77233 ? 155 ASN   A CG  1 
ATOM   1080 O OD1 . ASN   A 1 148 ? -9.26869  -8.97706  -36.52516 1.000 24.34683 ? 155 ASN   A OD1 1 
ATOM   1081 N ND2 . ASN   A 1 148 ? -8.96498  -6.77344  -36.20929 1.000 21.44888 ? 155 ASN   A ND2 1 
ATOM   1082 N N   . ASP   A 1 149 ? -4.48281  -9.13728  -38.64344 1.000 22.24995 ? 156 ASP   A N   1 
ATOM   1083 C CA  . ASP   A 1 149 ? -3.56463  -9.04999  -39.77204 1.000 26.15900 ? 156 ASP   A CA  1 
ATOM   1084 C C   . ASP   A 1 149 ? -2.74794  -10.31705 -39.99913 1.000 28.58201 ? 156 ASP   A C   1 
ATOM   1085 O O   . ASP   A 1 149 ? -1.83641  -10.30220 -40.83234 1.000 29.57795 ? 156 ASP   A O   1 
ATOM   1086 C CB  . ASP   A 1 149 ? -2.62185  -7.85445  -39.60763 1.000 25.41110 ? 156 ASP   A CB  1 
ATOM   1087 C CG  . ASP   A 1 149 ? -3.35601  -6.52810  -39.57697 1.000 31.27655 ? 156 ASP   A CG  1 
ATOM   1088 O OD1 . ASP   A 1 149 ? -4.50686  -6.46586  -40.05889 1.000 29.42323 ? 156 ASP   A OD1 1 
ATOM   1089 O OD2 . ASP   A 1 149 ? -2.77744  -5.54720  -39.06578 1.000 33.55871 ? 156 ASP   A OD2 1 
ATOM   1090 N N   . ASP   A 1 150 ? -3.04347  -11.40812 -39.29506 1.000 22.13355 ? 157 ASP   A N   1 
ATOM   1091 C CA  . ASP   A 1 150 ? -2.23703  -12.61759 -39.42205 1.000 19.95063 ? 157 ASP   A CA  1 
ATOM   1092 C C   . ASP   A 1 150 ? -3.11914  -13.84175 -39.19830 1.000 26.43281 ? 157 ASP   A C   1 
ATOM   1093 O O   . ASP   A 1 150 ? -4.31754  -13.73245 -38.92283 1.000 23.29994 ? 157 ASP   A O   1 
ATOM   1094 C CB  . ASP   A 1 150 ? -1.05041  -12.58986 -38.44918 1.000 20.90768 ? 157 ASP   A CB  1 
ATOM   1095 C CG  . ASP   A 1 150 ? 0.16595   -13.33280 -38.98095 1.000 24.60344 ? 157 ASP   A CG  1 
ATOM   1096 O OD1 . ASP   A 1 150 ? 0.02194   -14.13720 -39.92872 1.000 26.92553 ? 157 ASP   A OD1 1 
ATOM   1097 O OD2 . ASP   A 1 150 ? 1.27372   -13.11896 -38.43459 1.000 23.36114 ? 157 ASP   A OD2 1 
ATOM   1098 N N   . GLU   A 1 151 ? -2.51287  -15.01737 -39.33023 1.000 23.77001 ? 158 GLU   A N   1 
ATOM   1099 C CA  . GLU   A 1 151 ? -3.19114  -16.28268 -39.09703 1.000 22.20670 ? 158 GLU   A CA  1 
ATOM   1100 C C   . GLU   A 1 151 ? -3.10455  -16.67009 -37.62299 1.000 18.23328 ? 158 GLU   A C   1 
ATOM   1101 O O   . GLU   A 1 151 ? -2.43270  -16.02274 -36.82127 1.000 20.58157 ? 158 GLU   A O   1 
ATOM   1102 C CB  . GLU   A 1 151 ? -2.57666  -17.37769 -39.96749 1.000 27.89367 ? 158 GLU   A CB  1 
ATOM   1103 C CG  . GLU   A 1 151 ? -2.50642  -17.01680 -41.43852 1.000 37.03087 ? 158 GLU   A CG  1 
ATOM   1104 C CD  . GLU   A 1 151 ? -3.88015  -16.84138 -42.05142 1.000 56.82790 ? 158 GLU   A CD  1 
ATOM   1105 O OE1 . GLU   A 1 151 ? -4.75145  -17.70359 -41.81188 1.000 72.11595 ? 158 GLU   A OE1 1 
ATOM   1106 O OE2 . GLU   A 1 151 ? -4.09192  -15.83972 -42.76760 1.000 66.90953 ? 158 GLU   A OE2 1 
ATOM   1107 N N   . GLN   A 1 152 ? -3.79671  -17.74862 -37.26922 1.000 19.69301 ? 159 GLN   A N   1 
ATOM   1108 C CA  . GLN   A 1 152 ? -3.80860  -18.21447 -35.88843 1.000 17.93552 ? 159 GLN   A CA  1 
ATOM   1109 C C   . GLN   A 1 152 ? -2.56009  -19.04211 -35.60829 1.000 16.92679 ? 159 GLN   A C   1 
ATOM   1110 O O   . GLN   A 1 152 ? -2.24698  -19.97743 -36.35160 1.000 20.03414 ? 159 GLN   A O   1 
ATOM   1111 C CB  . GLN   A 1 152 ? -5.05860  -19.05261 -35.62217 1.000 18.05518 ? 159 GLN   A CB  1 
ATOM   1112 C CG  . GLN   A 1 152 ? -5.27580  -19.37501 -34.14566 1.000 19.63981 ? 159 GLN   A CG  1 
ATOM   1113 C CD  . GLN   A 1 152 ? -6.70026  -19.79133 -33.84767 1.000 24.79738 ? 159 GLN   A CD  1 
ATOM   1114 O OE1 . GLN   A 1 152 ? -7.64500  -19.08092 -34.18374 1.000 27.20168 ? 159 GLN   A OE1 1 
ATOM   1115 N NE2 . GLN   A 1 152 ? -6.86216  -20.94326 -33.21176 1.000 24.35190 ? 159 GLN   A NE2 1 
ATOM   1116 N N   . TYR   A 1 153 ? -1.85924  -18.70575 -34.52801 1.000 15.90277 ? 160 TYR   A N   1 
ATOM   1117 C CA  . TYR   A 1 153 ? -0.59501  -19.33782 -34.19257 1.000 16.59473 ? 160 TYR   A CA  1 
ATOM   1118 C C   . TYR   A 1 153 ? -0.62146  -19.84723 -32.75985 1.000 17.93479 ? 160 TYR   A C   1 
ATOM   1119 O O   . TYR   A 1 153 ? -1.35570  -19.33731 -31.90599 1.000 16.63447 ? 160 TYR   A O   1 
ATOM   1120 C CB  . TYR   A 1 153 ? 0.57251   -18.35469 -34.36056 1.000 16.63388 ? 160 TYR   A CB  1 
ATOM   1121 C CG  . TYR   A 1 153 ? 0.99380   -18.17381 -35.79496 1.000 18.73799 ? 160 TYR   A CG  1 
ATOM   1122 C CD1 . TYR   A 1 153 ? 1.83246   -19.09069 -36.40758 1.000 22.15638 ? 160 TYR   A CD1 1 
ATOM   1123 C CD2 . TYR   A 1 153 ? 0.51828   -17.10990 -36.55141 1.000 22.82597 ? 160 TYR   A CD2 1 
ATOM   1124 C CE1 . TYR   A 1 153 ? 2.21668   -18.94173 -37.72835 1.000 28.42385 ? 160 TYR   A CE1 1 
ATOM   1125 C CE2 . TYR   A 1 153 ? 0.89457   -16.95387 -37.88043 1.000 25.65773 ? 160 TYR   A CE2 1 
ATOM   1126 C CZ  . TYR   A 1 153 ? 1.74443   -17.87510 -38.45837 1.000 31.46387 ? 160 TYR   A CZ  1 
ATOM   1127 O OH  . TYR   A 1 153 ? 2.12998   -17.73730 -39.77350 1.000 35.85928 ? 160 TYR   A OH  1 
ATOM   1128 N N   . ALA   A 1 154 ? 0.22314   -20.84461 -32.50189 1.000 17.21430 ? 161 ALA   A N   1 
ATOM   1129 C CA  . ALA   A 1 154 ? 0.44235   -21.39247 -31.16798 1.000 16.29638 ? 161 ALA   A CA  1 
ATOM   1130 C C   . ALA   A 1 154 ? 1.91691   -21.25894 -30.81018 1.000 16.15127 ? 161 ALA   A C   1 
ATOM   1131 O O   . ALA   A 1 154 ? 2.78035   -21.78131 -31.52422 1.000 16.71345 ? 161 ALA   A O   1 
ATOM   1132 C CB  . ALA   A 1 154 ? 0.02650   -22.86326 -31.10982 1.000 19.99322 ? 161 ALA   A CB  1 
ATOM   1133 N N   . TRP   A 1 155 ? 2.19223   -20.55229 -29.72171 1.000 14.74286 ? 162 TRP   A N   1 
ATOM   1134 C CA  . TRP   A 1 155 ? 3.50109   -20.44077 -29.09169 1.000 13.35995 ? 162 TRP   A CA  1 
ATOM   1135 C C   . TRP   A 1 155 ? 3.51041   -21.36452 -27.88168 1.000 16.59287 ? 162 TRP   A C   1 
ATOM   1136 O O   . TRP   A 1 155 ? 2.48625   -21.54991 -27.22582 1.000 15.22432 ? 162 TRP   A O   1 
ATOM   1137 C CB  . TRP   A 1 155 ? 3.66960   -18.98882 -28.63403 1.000 14.28784 ? 162 TRP   A CB  1 
ATOM   1138 C CG  . TRP   A 1 155 ? 4.91195   -18.59925 -27.87635 1.000 12.60061 ? 162 TRP   A CG  1 
ATOM   1139 C CD1 . TRP   A 1 155 ? 5.98638   -17.90946 -28.37367 1.000 13.68909 ? 162 TRP   A CD1 1 
ATOM   1140 C CD2 . TRP   A 1 155 ? 5.17683   -18.80279 -26.47851 1.000 14.17910 ? 162 TRP   A CD2 1 
ATOM   1141 N NE1 . TRP   A 1 155 ? 6.90440   -17.68686 -27.37416 1.000 13.80882 ? 162 TRP   A NE1 1 
ATOM   1142 C CE2 . TRP   A 1 155 ? 6.43259   -18.22515 -26.20347 1.000 13.87560 ? 162 TRP   A CE2 1 
ATOM   1143 C CE3 . TRP   A 1 155 ? 4.47365   -19.41683 -25.43319 1.000 14.52152 ? 162 TRP   A CE3 1 
ATOM   1144 C CZ2 . TRP   A 1 155 ? 7.00721   -18.25375 -24.92963 1.000 14.17959 ? 162 TRP   A CZ2 1 
ATOM   1145 C CZ3 . TRP   A 1 155 ? 5.04773   -19.44356 -24.16832 1.000 15.33319 ? 162 TRP   A CZ3 1 
ATOM   1146 C CH2 . TRP   A 1 155 ? 6.30142   -18.86269 -23.92883 1.000 14.20214 ? 162 TRP   A CH2 1 
ATOM   1147 N N   . GLU   A 1 156 ? 4.66316   -21.95389 -27.57962 1.000 13.37575 ? 163 GLU   A N   1 
ATOM   1148 C CA  . GLU   A 1 156 ? 4.72970   -22.84563 -26.43036 1.000 13.96120 ? 163 GLU   A CA  1 
ATOM   1149 C C   . GLU   A 1 156 ? 6.13865   -22.87649 -25.86211 1.000 15.43474 ? 163 GLU   A C   1 
ATOM   1150 O O   . GLU   A 1 156 ? 7.11726   -22.82379 -26.61238 1.000 15.21659 ? 163 GLU   A O   1 
ATOM   1151 C CB  . GLU   A 1 156 ? 4.27785   -24.25724 -26.81328 1.000 17.87800 ? 163 GLU   A CB  1 
ATOM   1152 C CG  . GLU   A 1 156 ? 4.00236   -25.17837 -25.65007 1.000 20.77054 ? 163 GLU   A CG  1 
ATOM   1153 C CD  . GLU   A 1 156 ? 3.34369   -26.46491 -26.10019 1.000 29.98076 ? 163 GLU   A CD  1 
ATOM   1154 O OE1 . GLU   A 1 156 ? 3.99890   -27.25479 -26.81546 1.000 29.85855 ? 163 GLU   A OE1 1 
ATOM   1155 O OE2 . GLU   A 1 156 ? 2.15215   -26.66973 -25.76975 1.000 28.30966 ? 163 GLU   A OE2 1 
ATOM   1156 N N   . SER   A 1 157 ? 6.24039   -22.96451 -24.53776 1.000 13.75059 ? 164 SER   A N   1 
ATOM   1157 C CA  . SER   A 1 157 ? 7.54530   -23.13556 -23.91664 1.000 13.39961 ? 164 SER   A CA  1 
ATOM   1158 C C   . SER   A 1 157 ? 7.38908   -23.78257 -22.54961 1.000 12.66563 ? 164 SER   A C   1 
ATOM   1159 O O   . SER   A 1 157 ? 6.48778   -23.42400 -21.77880 1.000 13.57379 ? 164 SER   A O   1 
ATOM   1160 C CB  . SER   A 1 157 ? 8.30042   -21.81191 -23.77988 1.000 14.81396 ? 164 SER   A CB  1 
ATOM   1161 O OG  . SER   A 1 157 ? 9.54869   -22.03726 -23.14018 1.000 14.76933 ? 164 SER   A OG  1 
ATOM   1162 N N   . SER   A 1 158 ? 8.28259   -24.73361 -22.26454 1.000 15.55868 ? 165 SER   A N   1 
ATOM   1163 C CA  . SER   A 1 158 ? 8.49977   -25.26633 -20.92588 1.000 17.56458 ? 165 SER   A CA  1 
ATOM   1164 C C   . SER   A 1 158 ? 9.75751   -24.68583 -20.29973 1.000 16.87621 ? 165 SER   A C   1 
ATOM   1165 O O   . SER   A 1 158 ? 10.39328  -25.33741 -19.45806 1.000 20.74281 ? 165 SER   A O   1 
ATOM   1166 C CB  . SER   A 1 158 ? 8.58774   -26.79211 -20.96346 1.000 19.71353 ? 165 SER   A CB  1 
ATOM   1167 O OG  . SER   A 1 158 ? 7.38356   -27.35996 -21.45083 1.000 21.47504 ? 165 SER   A OG  1 
ATOM   1168 N N   . ALA   A 1 159 ? 10.12319  -23.46903 -20.70929 1.000 16.12764 ? 166 ALA   A N   1 
ATOM   1169 C CA  . ALA   A 1 159 ? 11.38426  -22.83237 -20.34475 1.000 17.95668 ? 166 ALA   A CA  1 
ATOM   1170 C C   . ALA   A 1 159 ? 12.54944  -23.64915 -20.89108 1.000 20.09036 ? 166 ALA   A C   1 
ATOM   1171 O O   . ALA   A 1 159 ? 12.46326  -24.17575 -22.00404 1.000 22.51242 ? 166 ALA   A O   1 
ATOM   1172 C CB  . ALA   A 1 159 ? 11.47729  -22.59519 -18.83567 1.000 23.19656 ? 166 ALA   A CB  1 
ATOM   1173 N N   . GLY   A 1 160 ? 13.63968  -23.76302 -20.13590 1.000 21.43716 ? 167 GLY   A N   1 
ATOM   1174 C CA  . GLY   A 1 160 ? 14.78981  -24.47486 -20.65833 1.000 22.14941 ? 167 GLY   A CA  1 
ATOM   1175 C C   . GLY   A 1 160 ? 15.46414  -23.81939 -21.84148 1.000 21.88744 ? 167 GLY   A C   1 
ATOM   1176 O O   . GLY   A 1 160 ? 16.26303  -24.47062 -22.52608 1.000 24.10320 ? 167 GLY   A O   1 
ATOM   1177 N N   . GLY   A 1 161 ? 15.14715  -22.55836 -22.12379 1.000 18.75246 ? 168 GLY   A N   1 
ATOM   1178 C CA  . GLY   A 1 161 ? 15.88108  -21.78109 -23.09579 1.000 17.16262 ? 168 GLY   A CA  1 
ATOM   1179 C C   . GLY   A 1 161 ? 15.29629  -21.73477 -24.49185 1.000 16.17446 ? 168 GLY   A C   1 
ATOM   1180 O O   . GLY   A 1 161 ? 15.87878  -21.07046 -25.35531 1.000 18.53114 ? 168 GLY   A O   1 
ATOM   1181 N N   . SER   A 1 162 ? 14.16838  -22.39910 -24.74705 1.000 16.17383 ? 169 SER   A N   1 
ATOM   1182 C CA  . SER   A 1 162 ? 13.61690  -22.43065 -26.09380 1.000 15.67102 ? 169 SER   A CA  1 
ATOM   1183 C C   . SER   A 1 162 ? 12.10068  -22.32506 -26.05019 1.000 15.24255 ? 169 SER   A C   1 
ATOM   1184 O O   . SER   A 1 162 ? 11.46124  -22.62318 -25.03930 1.000 16.50160 ? 169 SER   A O   1 
ATOM   1185 C CB  . SER   A 1 162 ? 14.01316  -23.70027 -26.86365 1.000 19.92717 ? 169 SER   A CB  1 
ATOM   1186 O OG  . SER   A 1 162 ? 13.46450  -24.85494 -26.24968 1.000 21.49672 ? 169 SER   A OG  1 
ATOM   1187 N N   . PHE   A 1 163 ? 11.53986  -21.89722 -27.18102 1.000 15.27424 ? 170 PHE   A N   1 
ATOM   1188 C CA  . PHE   A 1 163 ? 10.10208  -21.86549 -27.39791 1.000 13.87953 ? 170 PHE   A CA  1 
ATOM   1189 C C   . PHE   A 1 163 ? 9.83496   -22.32909 -28.82067 1.000 15.99933 ? 170 PHE   A C   1 
ATOM   1190 O O   . PHE   A 1 163 ? 10.72520  -22.31842 -29.67292 1.000 15.86975 ? 170 PHE   A O   1 
ATOM   1191 C CB  . PHE   A 1 163 ? 9.48739   -20.47405 -27.12651 1.000 14.95662 ? 170 PHE   A CB  1 
ATOM   1192 C CG  . PHE   A 1 163 ? 9.97380   -19.37992 -28.05266 1.000 13.30903 ? 170 PHE   A CG  1 
ATOM   1193 C CD1 . PHE   A 1 163 ? 11.10763  -18.64016 -27.73961 1.000 15.85350 ? 170 PHE   A CD1 1 
ATOM   1194 C CD2 . PHE   A 1 163 ? 9.26795   -19.06131 -29.20821 1.000 14.17496 ? 170 PHE   A CD2 1 
ATOM   1195 C CE1 . PHE   A 1 163 ? 11.54449  -17.61767 -28.57767 1.000 15.81477 ? 170 PHE   A CE1 1 
ATOM   1196 C CE2 . PHE   A 1 163 ? 9.69082   -18.04832 -30.04436 1.000 15.07423 ? 170 PHE   A CE2 1 
ATOM   1197 C CZ  . PHE   A 1 163 ? 10.83134  -17.31619 -29.72707 1.000 16.00264 ? 170 PHE   A CZ  1 
ATOM   1198 N N   . THR   A 1 164 ? 8.60674   -22.77489 -29.06763 1.000 14.79614 ? 171 THR   A N   1 
ATOM   1199 C CA  . THR   A 1 164 ? 8.18913   -23.17618 -30.40142 1.000 15.28659 ? 171 THR   A CA  1 
ATOM   1200 C C   . THR   A 1 164 ? 7.04477   -22.29710 -30.88161 1.000 14.71068 ? 171 THR   A C   1 
ATOM   1201 O O   . THR   A 1 164 ? 6.27212   -21.75934 -30.08284 1.000 14.98338 ? 171 THR   A O   1 
ATOM   1202 C CB  . THR   A 1 164 ? 7.75566   -24.64750 -30.46563 1.000 16.30605 ? 171 THR   A CB  1 
ATOM   1203 O OG1 . THR   A 1 164 ? 6.60939   -24.85450 -29.62895 1.000 20.69050 ? 171 THR   A OG1 1 
ATOM   1204 C CG2 . THR   A 1 164 ? 8.89492   -25.57533 -30.03967 1.000 18.22700 ? 171 THR   A CG2 1 
ATOM   1205 N N   . VAL   A 1 165 ? 6.94810   -22.16033 -32.19934 1.000 15.50139 ? 172 VAL   A N   1 
ATOM   1206 C CA  . VAL   A 1 165 ? 5.82846   -21.49796 -32.85196 1.000 15.63644 ? 172 VAL   A CA  1 
ATOM   1207 C C   . VAL   A 1 165 ? 5.37055   -22.38369 -33.99874 1.000 18.92539 ? 172 VAL   A C   1 
ATOM   1208 O O   . VAL   A 1 165 ? 6.19189   -22.89982 -34.76444 1.000 18.13268 ? 172 VAL   A O   1 
ATOM   1209 C CB  . VAL   A 1 165 ? 6.21230   -20.09739 -33.37759 1.000 15.65951 ? 172 VAL   A CB  1 
ATOM   1210 C CG1 . VAL   A 1 165 ? 5.04359   -19.46754 -34.13391 1.000 18.53157 ? 172 VAL   A CG1 1 
ATOM   1211 C CG2 . VAL   A 1 165 ? 6.65894   -19.20187 -32.24114 1.000 15.86259 ? 172 VAL   A CG2 1 
ATOM   1212 N N   . ARG   A 1 166 ? 4.05593   -22.55634 -34.11795 1.000 17.76220 ? 173 ARG   A N   1 
ATOM   1213 C CA  . ARG   A 1 166 ? 3.46768   -23.31049 -35.21114 1.000 18.45966 ? 173 ARG   A CA  1 
ATOM   1214 C C   . ARG   A 1 166 ? 2.12410   -22.69398 -35.56101 1.000 17.94874 ? 173 ARG   A C   1 
ATOM   1215 O O   . ARG   A 1 166 ? 1.48662   -22.04400 -34.73071 1.000 17.84649 ? 173 ARG   A O   1 
ATOM   1216 C CB  . ARG   A 1 166 ? 3.29436   -24.78780 -34.84529 1.000 21.82420 ? 173 ARG   A CB  1 
ATOM   1217 C CG  . ARG   A 1 166 ? 2.25181   -25.04506 -33.76511 1.000 23.48339 ? 173 ARG   A CG  1 
ATOM   1218 C CD  . ARG   A 1 166 ? 2.43105   -26.42409 -33.13767 1.000 28.74517 ? 173 ARG   A CD  1 
ATOM   1219 N NE  . ARG   A 1 166 ? 3.57423   -26.45608 -32.23108 1.000 34.04076 ? 173 ARG   A NE  1 
ATOM   1220 C CZ  . ARG   A 1 166 ? 4.10415   -27.56034 -31.72043 1.000 40.04573 ? 173 ARG   A CZ  1 
ATOM   1221 N NH1 . ARG   A 1 166 ? 3.63690   -28.75935 -32.02820 1.000 38.47116 ? 173 ARG   A NH1 1 
ATOM   1222 N NH2 . ARG   A 1 166 ? 5.13182   -27.45879 -30.88147 1.000 38.76603 ? 173 ARG   A NH2 1 
ATOM   1223 N N   . THR   A 1 167 ? 1.70290   -22.89924 -36.80498 1.000 21.94468 ? 174 THR   A N   1 
ATOM   1224 C CA  . THR   A 1 167 ? 0.33218   -22.57377 -37.16414 1.000 22.00737 ? 174 THR   A CA  1 
ATOM   1225 C C   . THR   A 1 167 ? -0.60622  -23.45955 -36.35913 1.000 24.40332 ? 174 THR   A C   1 
ATOM   1226 O O   . THR   A 1 167 ? -0.35967  -24.65582 -36.18408 1.000 29.89064 ? 174 THR   A O   1 
ATOM   1227 C CB  . THR   A 1 167 ? 0.11259   -22.78106 -38.66164 1.000 29.46485 ? 174 THR   A CB  1 
ATOM   1228 O OG1 . THR   A 1 167 ? 0.99314   -21.91738 -39.38912 1.000 31.75203 ? 174 THR   A OG1 1 
ATOM   1229 C CG2 . THR   A 1 167 ? -1.32503  -22.45678 -39.04100 1.000 33.63438 ? 174 THR   A CG2 1 
ATOM   1230 N N   . ASP   A 1 168 ? -1.67410  -22.86218 -35.83991 1.000 22.34069 ? 175 ASP   A N   1 
ATOM   1231 C CA  . ASP   A 1 168 ? -2.59729  -23.58107 -34.97569 1.000 25.92222 ? 175 ASP   A CA  1 
ATOM   1232 C C   . ASP   A 1 168 ? -3.73493  -24.13440 -35.82131 1.000 34.22704 ? 175 ASP   A C   1 
ATOM   1233 O O   . ASP   A 1 168 ? -4.41260  -23.38098 -36.52788 1.000 35.82094 ? 175 ASP   A O   1 
ATOM   1234 C CB  . ASP   A 1 168 ? -3.14745  -22.66127 -33.88907 1.000 24.64209 ? 175 ASP   A CB  1 
ATOM   1235 C CG  . ASP   A 1 168 ? -3.97422  -23.40941 -32.86162 1.000 33.53915 ? 175 ASP   A CG  1 
ATOM   1236 O OD1 . ASP   A 1 168 ? -3.53870  -24.49369 -32.41953 1.000 43.46011 ? 175 ASP   A OD1 1 
ATOM   1237 O OD2 . ASP   A 1 168 ? -5.06288  -22.92103 -32.50341 1.000 28.99572 ? 175 ASP   A OD2 1 
ATOM   1238 N N   . THR   A 1 169 ? -3.93582  -25.44640 -35.75275 1.000 43.41039 ? 176 THR   A N   1 
ATOM   1239 C CA  . THR   A 1 169 ? -5.05524  -26.09826 -36.41361 1.000 57.99098 ? 176 THR   A CA  1 
ATOM   1240 C C   . THR   A 1 169 ? -6.21460  -26.36408 -35.46612 1.000 51.76111 ? 176 THR   A C   1 
ATOM   1241 O O   . THR   A 1 169 ? -7.20762  -26.97121 -35.87787 1.000 53.86235 ? 176 THR   A O   1 
ATOM   1242 C CB  . THR   A 1 169 ? -4.60151  -27.40843 -37.06767 1.000 58.87406 ? 176 THR   A CB  1 
ATOM   1243 O OG1 . THR   A 1 169 ? -3.72593  -28.11293 -36.17542 1.000 54.59217 ? 176 THR   A OG1 1 
ATOM   1244 C CG2 . THR   A 1 169 ? -3.88252  -27.12115 -38.37052 1.000 45.14431 ? 176 THR   A CG2 1 
ATOM   1245 N N   . GLY   A 1 170 ? -6.11479  -25.92302 -34.21733 1.000 51.51271 ? 177 GLY   A N   1 
ATOM   1246 C CA  . GLY   A 1 170 ? -7.18379  -26.09901 -33.26649 1.000 49.85872 ? 177 GLY   A CA  1 
ATOM   1247 C C   . GLY   A 1 170 ? -8.39432  -25.24421 -33.59421 1.000 37.23905 ? 177 GLY   A C   1 
ATOM   1248 O O   . GLY   A 1 170 ? -8.57864  -24.72462 -34.69766 1.000 37.03852 ? 177 GLY   A O   1 
ATOM   1249 N N   . GLU   A 1 171 ? -9.23650  -25.10091 -32.58429 1.000 35.80024 ? 178 GLU   A N   1 
ATOM   1250 C CA  . GLU   A 1 171 ? -10.48534 -24.36923 -32.73890 1.000 36.08210 ? 178 GLU   A CA  1 
ATOM   1251 C C   . GLU   A 1 171 ? -10.19535 -22.90880 -33.08344 1.000 35.92937 ? 178 GLU   A C   1 
ATOM   1252 O O   . GLU   A 1 171 ? -9.43692  -22.25515 -32.36497 1.000 27.81666 ? 178 GLU   A O   1 
ATOM   1253 C CB  . GLU   A 1 171 ? -11.25516 -24.44518 -31.42065 1.000 40.00337 ? 178 GLU   A CB  1 
ATOM   1254 C CG  . GLU   A 1 171 ? -12.74282 -24.28902 -31.55875 1.000 43.19904 ? 178 GLU   A CG  1 
ATOM   1255 C CD  . GLU   A 1 171 ? -13.36356 -25.37969 -32.41260 1.000 35.40417 ? 178 GLU   A CD  1 
ATOM   1256 O OE1 . GLU   A 1 171 ? -13.18230 -26.57996 -32.10601 1.000 40.64349 ? 178 GLU   A OE1 1 
ATOM   1257 O OE2 . GLU   A 1 171 ? -14.02269 -25.02302 -33.40224 1.000 41.16879 ? 178 GLU   A OE2 1 
ATOM   1258 N N   . PRO   A 1 172 ? -10.74484 -22.37941 -34.17970 1.000 34.64787 ? 179 PRO   A N   1 
ATOM   1259 C CA  . PRO   A 1 172 ? -10.53233 -20.96040 -34.49892 1.000 34.82132 ? 179 PRO   A CA  1 
ATOM   1260 C C   . PRO   A 1 172 ? -11.02415 -20.06577 -33.36852 1.000 37.99308 ? 179 PRO   A C   1 
ATOM   1261 O O   . PRO   A 1 172 ? -12.03930 -20.34466 -32.72637 1.000 42.06389 ? 179 PRO   A O   1 
ATOM   1262 C CB  . PRO   A 1 172 ? -11.38840 -20.78499 -35.75048 1.000 37.46630 ? 179 PRO   A CB  1 
ATOM   1263 C CG  . PRO   A 1 172 ? -11.17202 -22.09232 -36.46597 1.000 49.70891 ? 179 PRO   A CG  1 
ATOM   1264 C CD  . PRO   A 1 172 ? -11.28056 -23.11789 -35.34232 1.000 47.99696 ? 179 PRO   A CD  1 
ATOM   1265 N N   . MET   A 1 173 ? -10.29571 -18.97309 -33.12757 1.000 27.82177 ? 180 MET   A N   1 
ATOM   1266 C CA  . MET   A 1 173 ? -10.63649 -18.05415 -32.04285 1.000 28.13977 ? 180 MET   A CA  1 
ATOM   1267 C C   . MET   A 1 173 ? -11.27014 -16.74378 -32.49658 1.000 36.70641 ? 180 MET   A C   1 
ATOM   1268 O O   . MET   A 1 173 ? -11.75969 -15.98703 -31.64674 1.000 33.30552 ? 180 MET   A O   1 
ATOM   1269 C CB  . MET   A 1 173 ? -9.41096  -17.69888 -31.19092 1.000 33.64687 ? 180 MET   A CB  1 
ATOM   1270 C CG  . MET   A 1 173 ? -8.42300  -18.81048 -30.97284 1.000 47.73059 ? 180 MET   A CG  1 
ATOM   1271 S SD  . MET   A 1 173 ? -6.93427  -18.09045 -30.26385 1.000 44.52014 ? 180 MET   A SD  1 
ATOM   1272 C CE  . MET   A 1 173 ? -7.57776  -16.59972 -29.51092 1.000 31.05161 ? 180 MET   A CE  1 
ATOM   1273 N N   . GLY   A 1 174 ? -11.24825 -16.43223 -33.78624 1.000 27.44212 ? 181 GLY   A N   1 
ATOM   1274 C CA  . GLY   A 1 174 ? -11.80962 -15.17700 -34.24956 1.000 24.29602 ? 181 GLY   A CA  1 
ATOM   1275 C C   . GLY   A 1 174 ? -10.82277 -14.03825 -34.11036 1.000 19.19726 ? 181 GLY   A C   1 
ATOM   1276 O O   . GLY   A 1 174 ? -10.35060 -13.49238 -35.11243 1.000 21.27260 ? 181 GLY   A O   1 
ATOM   1277 N N   . ARG   A 1 175 ? -10.50184 -13.67762 -32.86827 1.000 16.59739 ? 182 ARG   A N   1 
ATOM   1278 C CA  . ARG   A 1 175 ? -9.48572  -12.67799 -32.57022 1.000 16.34977 ? 182 ARG   A CA  1 
ATOM   1279 C C   . ARG   A 1 175 ? -9.22076  -12.71495 -31.07482 1.000 16.73639 ? 182 ARG   A C   1 
ATOM   1280 O O   . ARG   A 1 175 ? -10.15922 -12.82066 -30.28148 1.000 18.67937 ? 182 ARG   A O   1 
ATOM   1281 C CB  . ARG   A 1 175 ? -9.95685  -11.26501 -32.95856 1.000 18.42144 ? 182 ARG   A CB  1 
ATOM   1282 C CG  . ARG   A 1 175 ? -8.88560  -10.18536 -32.73609 1.000 17.83199 ? 182 ARG   A CG  1 
ATOM   1283 C CD  . ARG   A 1 175 ? -9.48224  -8.78653  -32.60044 1.000 16.84568 ? 182 ARG   A CD  1 
ATOM   1284 N NE  . ARG   A 1 175 ? -10.40109 -8.67886  -31.47150 1.000 17.87955 ? 182 ARG   A NE  1 
ATOM   1285 C CZ  . ARG   A 1 175 ? -11.71641 -8.55647  -31.57612 1.000 17.66957 ? 182 ARG   A CZ  1 
ATOM   1286 N NH1 . ARG   A 1 175 ? -12.32108 -8.54187  -32.75548 1.000 17.82039 ? 182 ARG   A NH1 1 
ATOM   1287 N NH2 . ARG   A 1 175 ? -12.44781 -8.45363  -30.46933 1.000 17.99141 ? 182 ARG   A NH2 1 
ATOM   1288 N N   . GLY   A 1 176 ? -7.94697  -12.61408 -30.69442 1.000 19.57189 ? 183 GLY   A N   1 
ATOM   1289 C CA  . GLY   A 1 176 ? -7.59321  -12.50470 -29.29692 1.000 17.48135 ? 183 GLY   A CA  1 
ATOM   1290 C C   . GLY   A 1 176 ? -6.46373  -13.44055 -28.93649 1.000 16.17657 ? 183 GLY   A C   1 
ATOM   1291 O O   . GLY   A 1 176 ? -5.70145  -13.89525 -29.79941 1.000 17.08807 ? 183 GLY   A O   1 
ATOM   1292 N N   . THR   A 1 177 ? -6.35066  -13.72414 -27.64272 1.000 14.47725 ? 184 THR   A N   1 
ATOM   1293 C CA  . THR   A 1 177 ? -5.25816  -14.52697 -27.11863 1.000 13.45486 ? 184 THR   A CA  1 
ATOM   1294 C C   . THR   A 1 177 ? -5.77745  -15.45715 -26.03779 1.000 16.02394 ? 184 THR   A C   1 
ATOM   1295 O O   . THR   A 1 177 ? -6.62046  -15.07306 -25.22041 1.000 14.38031 ? 184 THR   A O   1 
ATOM   1296 C CB  . THR   A 1 177 ? -4.13924  -13.63458 -26.55933 1.000 14.42671 ? 184 THR   A CB  1 
ATOM   1297 O OG1 . THR   A 1 177 ? -3.58700  -12.85785 -27.62129 1.000 17.71890 ? 184 THR   A OG1 1 
ATOM   1298 C CG2 . THR   A 1 177 ? -3.01769  -14.46621 -25.90944 1.000 15.95208 ? 184 THR   A CG2 1 
ATOM   1299 N N   . LYS   A 1 178 ? -5.27358  -16.68427 -26.05155 1.000 14.60595 ? 185 LYS   A N   1 
ATOM   1300 C CA  . LYS   A 1 178 ? -5.58902  -17.69654 -25.05602 1.000 15.19869 ? 185 LYS   A CA  1 
ATOM   1301 C C   . LYS   A 1 178 ? -4.27538  -18.15718 -24.43947 1.000 14.79681 ? 185 LYS   A C   1 
ATOM   1302 O O   . LYS   A 1 178 ? -3.39243  -18.63763 -25.15740 1.000 15.89882 ? 185 LYS   A O   1 
ATOM   1303 C CB  . LYS   A 1 178 ? -6.31609  -18.85116 -25.75466 1.000 20.98222 ? 185 LYS   A CB  1 
ATOM   1304 C CG  . LYS   A 1 178 ? -6.47978  -20.11746 -24.97189 1.000 29.96675 ? 185 LYS   A CG  1 
ATOM   1305 C CD  . LYS   A 1 178 ? -7.54485  -21.01043 -25.61754 1.000 35.36150 ? 185 LYS   A CD  1 
ATOM   1306 C CE  . LYS   A 1 178 ? -7.37419  -21.11081 -27.12832 1.000 35.19225 ? 185 LYS   A CE  1 
ATOM   1307 N NZ  . LYS   A 1 178 ? -8.13734  -22.25995 -27.71380 1.000 41.01833 ? 185 LYS   A NZ  1 
ATOM   1308 N N   . VAL   A 1 179 ? -4.12673  -17.97698 -23.12717 1.000 14.03030 ? 186 VAL   A N   1 
ATOM   1309 C CA  . VAL   A 1 179 ? -2.92926  -18.40710 -22.40531 1.000 12.56327 ? 186 VAL   A CA  1 
ATOM   1310 C C   . VAL   A 1 179 ? -3.30483  -19.65325 -21.62225 1.000 14.57296 ? 186 VAL   A C   1 
ATOM   1311 O O   . VAL   A 1 179 ? -4.11620  -19.58399 -20.68792 1.000 14.26424 ? 186 VAL   A O   1 
ATOM   1312 C CB  . VAL   A 1 179 ? -2.39356  -17.31875 -21.46549 1.000 12.23354 ? 186 VAL   A CB  1 
ATOM   1313 C CG1 . VAL   A 1 179 ? -1.21573  -17.86784 -20.63560 1.000 14.39912 ? 186 VAL   A CG1 1 
ATOM   1314 C CG2 . VAL   A 1 179 ? -1.98389  -16.09540 -22.25216 1.000 14.53723 ? 186 VAL   A CG2 1 
ATOM   1315 N N   . ILE   A 1 180 ? -2.73217  -20.78897 -22.00013 1.000 14.07275 ? 187 ILE   A N   1 
ATOM   1316 C CA  . ILE   A 1 180 ? -3.02388  -22.07213 -21.37322 1.000 13.10417 ? 187 ILE   A CA  1 
ATOM   1317 C C   . ILE   A 1 180 ? -1.88422  -22.38785 -20.41507 1.000 13.12829 ? 187 ILE   A C   1 
ATOM   1318 O O   . ILE   A 1 180 ? -0.74963  -22.61944 -20.84498 1.000 15.47400 ? 187 ILE   A O   1 
ATOM   1319 C CB  . ILE   A 1 180 ? -3.18511  -23.18236 -22.41629 1.000 15.46556 ? 187 ILE   A CB  1 
ATOM   1320 C CG1 . ILE   A 1 180 ? -4.18890  -22.77089 -23.49887 1.000 17.69004 ? 187 ILE   A CG1 1 
ATOM   1321 C CG2 . ILE   A 1 180 ? -3.58965  -24.49827 -21.74602 1.000 17.97810 ? 187 ILE   A CG2 1 
ATOM   1322 C CD1 . ILE   A 1 180 ? -4.24156  -23.74086 -24.66898 1.000 24.08314 ? 187 ILE   A CD1 1 
ATOM   1323 N N   . LEU   A 1 181 ? -2.18088  -22.41238 -19.11893 1.000 14.31047 ? 188 LEU   A N   1 
ATOM   1324 C CA  . LEU   A 1 181 ? -1.18579  -22.69689 -18.08828 1.000 13.05453 ? 188 LEU   A CA  1 
ATOM   1325 C C   . LEU   A 1 181 ? -1.28462  -24.16939 -17.71596 1.000 15.90730 ? 188 LEU   A C   1 
ATOM   1326 O O   . LEU   A 1 181 ? -2.27521  -24.59557 -17.11487 1.000 16.61168 ? 188 LEU   A O   1 
ATOM   1327 C CB  . LEU   A 1 181 ? -1.44173  -21.83493 -16.85474 1.000 13.79677 ? 188 LEU   A CB  1 
ATOM   1328 C CG  . LEU   A 1 181 ? -1.47093  -20.33253 -17.10495 1.000 14.91717 ? 188 LEU   A CG  1 
ATOM   1329 C CD1 . LEU   A 1 181 ? -1.83857  -19.61624 -15.81441 1.000 19.98661 ? 188 LEU   A CD1 1 
ATOM   1330 C CD2 . LEU   A 1 181 ? -0.14742  -19.85251 -17.63898 1.000 17.17447 ? 188 LEU   A CD2 1 
ATOM   1331 N N   . HIS   A 1 182 ? -0.25392  -24.94202 -18.05134 1.000 14.52642 ? 189 HIS   A N   1 
ATOM   1332 C CA  . HIS   A 1 182 ? -0.16063  -26.33940 -17.62900 1.000 16.35363 ? 189 HIS   A CA  1 
ATOM   1333 C C   . HIS   A 1 182 ? 0.47017   -26.31326 -16.24189 1.000 16.22055 ? 189 HIS   A C   1 
ATOM   1334 O O   . HIS   A 1 182 ? 1.68453   -26.15612 -16.10268 1.000 18.59557 ? 189 HIS   A O   1 
ATOM   1335 C CB  . HIS   A 1 182 ? 0.66490   -27.13534 -18.63513 1.000 16.70237 ? 189 HIS   A CB  1 
ATOM   1336 C CG  . HIS   A 1 182 ? 0.16317   -27.01908 -20.04261 1.000 21.08428 ? 189 HIS   A CG  1 
ATOM   1337 N ND1 . HIS   A 1 182 ? -0.62755  -27.98132 -20.63387 1.000 27.12700 ? 189 HIS   A ND1 1 
ATOM   1338 C CD2 . HIS   A 1 182 ? 0.31845   -26.03987 -20.96645 1.000 24.43742 ? 189 HIS   A CD2 1 
ATOM   1339 C CE1 . HIS   A 1 182 ? -0.92822  -27.60511 -21.86463 1.000 25.29141 ? 189 HIS   A CE1 1 
ATOM   1340 N NE2 . HIS   A 1 182 ? -0.36439  -26.43209 -22.09259 1.000 26.97836 ? 189 HIS   A NE2 1 
ATOM   1341 N N   . LEU   A 1 183 ? -0.36064  -26.43592 -15.20955 1.000 17.33358 ? 190 LEU   A N   1 
ATOM   1342 C CA  . LEU   A 1 183 ? 0.07729   -26.12037 -13.85409 1.000 16.94500 ? 190 LEU   A CA  1 
ATOM   1343 C C   . LEU   A 1 183 ? 1.02421   -27.17396 -13.29566 1.000 20.38055 ? 190 LEU   A C   1 
ATOM   1344 O O   . LEU   A 1 183 ? 0.91848   -28.36703 -13.59695 1.000 21.36767 ? 190 LEU   A O   1 
ATOM   1345 C CB  . LEU   A 1 183 ? -1.12550  -25.98565 -12.92157 1.000 18.05807 ? 190 LEU   A CB  1 
ATOM   1346 C CG  . LEU   A 1 183 ? -2.08235  -24.83806 -13.23640 1.000 17.94572 ? 190 LEU   A CG  1 
ATOM   1347 C CD1 . LEU   A 1 183 ? -3.25103  -24.85591 -12.26732 1.000 19.86753 ? 190 LEU   A CD1 1 
ATOM   1348 C CD2 . LEU   A 1 183 ? -1.35777  -23.50839 -13.16006 1.000 19.73767 ? 190 LEU   A CD2 1 
ATOM   1349 N N   . LYS   A 1 184 ? 1.95867   -26.71240 -12.46105 1.000 18.96385 ? 191 LYS   A N   1 
ATOM   1350 C CA  . LYS   A 1 184 ? 2.78138   -27.62456 -11.68049 1.000 20.36921 ? 191 LYS   A CA  1 
ATOM   1351 C C   . LYS   A 1 184 ? 1.90148   -28.43935 -10.74011 1.000 21.08507 ? 191 LYS   A C   1 
ATOM   1352 O O   . LYS   A 1 184 ? 0.81925   -28.00597 -10.33330 1.000 21.70601 ? 191 LYS   A O   1 
ATOM   1353 C CB  . LYS   A 1 184 ? 3.82994   -26.85575 -10.86873 1.000 22.72484 ? 191 LYS   A CB  1 
ATOM   1354 C CG  . LYS   A 1 184 ? 4.79749   -26.01741 -11.69954 1.000 23.01739 ? 191 LYS   A CG  1 
ATOM   1355 C CD  . LYS   A 1 184 ? 5.57166   -25.03577 -10.81727 1.000 29.50110 ? 191 LYS   A CD  1 
ATOM   1356 C CE  . LYS   A 1 184 ? 6.34596   -24.01757 -11.64032 1.000 37.80444 ? 191 LYS   A CE  1 
ATOM   1357 N NZ  . LYS   A 1 184 ? 7.34939   -23.25498 -10.82859 1.000 38.05908 ? 191 LYS   A NZ  1 
ATOM   1358 N N   . GLU   A 1 185 ? 2.38467   -29.63419 -10.39659 1.000 24.82736 ? 192 GLU   A N   1 
ATOM   1359 C CA  . GLU   A 1 185 ? 1.59320   -30.57275 -9.60805  1.000 28.17437 ? 192 GLU   A CA  1 
ATOM   1360 C C   . GLU   A 1 185 ? 1.16840   -29.98784 -8.26868  1.000 28.69379 ? 192 GLU   A C   1 
ATOM   1361 O O   . GLU   A 1 185 ? 0.09409   -30.32741 -7.75951  1.000 31.03959 ? 192 GLU   A O   1 
ATOM   1362 C CB  . GLU   A 1 185 ? 2.38910   -31.85911 -9.39055  1.000 33.67568 ? 192 GLU   A CB  1 
ATOM   1363 C CG  . GLU   A 1 185 ? 1.54605   -33.07648 -9.06979  1.000 54.41048 ? 192 GLU   A CG  1 
ATOM   1364 C CD  . GLU   A 1 185 ? 2.39455   -34.30552 -8.80178  1.000 74.89607 ? 192 GLU   A CD  1 
ATOM   1365 O OE1 . GLU   A 1 185 ? 3.63056   -34.16035 -8.68798  1.000 70.60672 ? 192 GLU   A OE1 1 
ATOM   1366 O OE2 . GLU   A 1 185 ? 1.82809   -35.41396 -8.69610  1.000 73.95759 ? 192 GLU   A OE2 1 
ATOM   1367 N N   . ASP   A 1 186 ? 1.98893   -29.12480 -7.67610  1.000 24.77203 ? 193 ASP   A N   1 
ATOM   1368 C CA  . ASP   A 1 186 ? 1.69679   -28.57564 -6.35908  1.000 24.46357 ? 193 ASP   A CA  1 
ATOM   1369 C C   . ASP   A 1 186 ? 1.00414   -27.21840 -6.41682  1.000 24.23769 ? 193 ASP   A C   1 
ATOM   1370 O O   . ASP   A 1 186 ? 0.88886   -26.55111 -5.38271  1.000 23.92707 ? 193 ASP   A O   1 
ATOM   1371 C CB  . ASP   A 1 186 ? 2.96641   -28.51107 -5.50611  1.000 29.11341 ? 193 ASP   A CB  1 
ATOM   1372 C CG  . ASP   A 1 186 ? 4.00447   -27.55944 -6.06356  1.000 31.22720 ? 193 ASP   A CG  1 
ATOM   1373 O OD1 . ASP   A 1 186 ? 3.90579   -27.17433 -7.24790  1.000 37.43949 ? 193 ASP   A OD1 1 
ATOM   1374 O OD2 . ASP   A 1 186 ? 4.93985   -27.20839 -5.31329  1.000 42.75669 ? 193 ASP   A OD2 1 
ATOM   1375 N N   . GLN   A 1 187 ? 0.52182   -26.81271 -7.59154  1.000 20.83012 ? 194 GLN   A N   1 
ATOM   1376 C CA  . GLN   A 1 187 ? -0.12285  -25.51959 -7.78343  1.000 20.13923 ? 194 GLN   A CA  1 
ATOM   1377 C C   . GLN   A 1 187 ? -1.57326  -25.66900 -8.23404  1.000 20.13061 ? 194 GLN   A C   1 
ATOM   1378 O O   . GLN   A 1 187 ? -2.12473  -24.77311 -8.87609  1.000 19.64532 ? 194 GLN   A O   1 
ATOM   1379 C CB  . GLN   A 1 187 ? 0.67159   -24.64770 -8.75806  1.000 20.66106 ? 194 GLN   A CB  1 
ATOM   1380 C CG  . GLN   A 1 187 ? 2.11440   -24.40669 -8.32207  1.000 20.99754 ? 194 GLN   A CG  1 
ATOM   1381 C CD  . GLN   A 1 187 ? 2.21858   -23.73835 -6.96298  1.000 26.20612 ? 194 GLN   A CD  1 
ATOM   1382 O OE1 . GLN   A 1 187 ? 1.39783   -22.89167 -6.61008  1.000 24.94427 ? 194 GLN   A OE1 1 
ATOM   1383 N NE2 . GLN   A 1 187 ? 3.24187   -24.10433 -6.19989  1.000 26.48870 ? 194 GLN   A NE2 1 
ATOM   1384 N N   . THR   A 1 188 ? -2.21032  -26.78811 -7.89098  1.000 22.08923 ? 195 THR   A N   1 
ATOM   1385 C CA  . THR   A 1 188 ? -3.57394  -27.02728 -8.35332  1.000 21.86930 ? 195 THR   A CA  1 
ATOM   1386 C C   . THR   A 1 188 ? -4.62140  -26.21843 -7.59833  1.000 21.35585 ? 195 THR   A C   1 
ATOM   1387 O O   . THR   A 1 188 ? -5.79945  -26.27173 -7.97079  1.000 22.41621 ? 195 THR   A O   1 
ATOM   1388 C CB  . THR   A 1 188 ? -3.92274  -28.51879 -8.30697  1.000 22.79586 ? 195 THR   A CB  1 
ATOM   1389 O OG1 . THR   A 1 188 ? -3.83602  -28.99847 -6.95834  1.000 27.52809 ? 195 THR   A OG1 1 
ATOM   1390 C CG2 . THR   A 1 188 ? -2.97762  -29.31485 -9.20226  1.000 26.40916 ? 195 THR   A CG2 1 
ATOM   1391 N N   . GLU   A 1 189 ? -4.23616  -25.47136 -6.55931  1.000 20.68016 ? 196 GLU   A N   1 
ATOM   1392 C CA  . GLU   A 1 189 ? -5.20395  -24.59825 -5.90164  1.000 20.24196 ? 196 GLU   A CA  1 
ATOM   1393 C C   . GLU   A 1 189 ? -5.77037  -23.57147 -6.86961  1.000 19.48464 ? 196 GLU   A C   1 
ATOM   1394 O O   . GLU   A 1 189 ? -6.88654  -23.08100 -6.66856  1.000 20.08522 ? 196 GLU   A O   1 
ATOM   1395 C CB  . GLU   A 1 189 ? -4.57600  -23.87162 -4.71322  1.000 21.14505 ? 196 GLU   A CB  1 
ATOM   1396 C CG  . GLU   A 1 189 ? -3.54908  -22.81469 -5.08916  1.000 19.35901 ? 196 GLU   A CG  1 
ATOM   1397 C CD  . GLU   A 1 189 ? -2.72518  -22.37226 -3.90466  1.000 24.53106 ? 196 GLU   A CD  1 
ATOM   1398 O OE1 . GLU   A 1 189 ? -1.84382  -23.14207 -3.46134  1.000 29.00524 ? 196 GLU   A OE1 1 
ATOM   1399 O OE2 . GLU   A 1 189 ? -2.98484  -21.26189 -3.38947  1.000 25.79801 ? 196 GLU   A OE2 1 
ATOM   1400 N N   . TYR   A 1 190 ? -5.02245  -23.23611 -7.91867  1.000 18.87435 ? 197 TYR   A N   1 
ATOM   1401 C CA  . TYR   A 1 190 ? -5.45532  -22.24050 -8.89060  1.000 16.54768 ? 197 TYR   A CA  1 
ATOM   1402 C C   . TYR   A 1 190 ? -6.46162  -22.79358 -9.88787  1.000 17.57179 ? 197 TYR   A C   1 
ATOM   1403 O O   . TYR   A 1 190 ? -6.81700  -22.08579 -10.83681 1.000 19.85025 ? 197 TYR   A O   1 
ATOM   1404 C CB  . TYR   A 1 190 ? -4.23734  -21.59828 -9.57414  1.000 16.34893 ? 197 TYR   A CB  1 
ATOM   1405 C CG  . TYR   A 1 190 ? -3.33016  -20.97367 -8.53625  1.000 16.47248 ? 197 TYR   A CG  1 
ATOM   1406 C CD1 . TYR   A 1 190 ? -3.74595  -19.86627 -7.80974  1.000 19.24204 ? 197 TYR   A CD1 1 
ATOM   1407 C CD2 . TYR   A 1 190 ? -2.08542  -21.52249 -8.23335  1.000 17.38965 ? 197 TYR   A CD2 1 
ATOM   1408 C CE1 . TYR   A 1 190 ? -2.94633  -19.30265 -6.83003  1.000 20.59523 ? 197 TYR   A CE1 1 
ATOM   1409 C CE2 . TYR   A 1 190 ? -1.26927  -20.95900 -7.24819  1.000 17.75922 ? 197 TYR   A CE2 1 
ATOM   1410 C CZ  . TYR   A 1 190 ? -1.70864  -19.84567 -6.54394  1.000 18.81421 ? 197 TYR   A CZ  1 
ATOM   1411 O OH  . TYR   A 1 190 ? -0.93564  -19.26853 -5.56052  1.000 22.75951 ? 197 TYR   A OH  1 
ATOM   1412 N N   . LEU   A 1 191 ? -6.91736  -24.03174 -9.69304  1.000 18.03945 ? 198 LEU   A N   1 
ATOM   1413 C CA  . LEU   A 1 191 ? -8.06638  -24.57376 -10.40381 1.000 18.19113 ? 198 LEU   A CA  1 
ATOM   1414 C C   . LEU   A 1 191 ? -9.33855  -24.54977 -9.57049  1.000 23.16693 ? 198 LEU   A C   1 
ATOM   1415 O O   . LEU   A 1 191 ? -10.40767 -24.88670 -10.09183 1.000 24.43535 ? 198 LEU   A O   1 
ATOM   1416 C CB  . LEU   A 1 191 ? -7.79712  -26.02027 -10.83879 1.000 18.45477 ? 198 LEU   A CB  1 
ATOM   1417 C CG  . LEU   A 1 191 ? -6.57147  -26.19647 -11.72953 1.000 18.10298 ? 198 LEU   A CG  1 
ATOM   1418 C CD1 . LEU   A 1 191 ? -6.33654  -27.67040 -12.03784 1.000 24.33283 ? 198 LEU   A CD1 1 
ATOM   1419 C CD2 . LEU   A 1 191 ? -6.71936  -25.37411 -13.00796 1.000 23.93833 ? 198 LEU   A CD2 1 
ATOM   1420 N N   . GLU   A 1 192 ? -9.25231  -24.20148 -8.28853  1.000 21.44750 ? 199 GLU   A N   1 
ATOM   1421 C CA  . GLU   A 1 192 ? -10.41126 -24.21005 -7.40641  1.000 22.06881 ? 199 GLU   A CA  1 
ATOM   1422 C C   . GLU   A 1 192 ? -11.17024 -22.89454 -7.51633  1.000 25.99174 ? 199 GLU   A C   1 
ATOM   1423 O O   . GLU   A 1 192 ? -10.56578 -21.81614 -7.51146  1.000 21.82387 ? 199 GLU   A O   1 
ATOM   1424 C CB  . GLU   A 1 192 ? -9.99135  -24.46640 -5.96043  1.000 27.53041 ? 199 GLU   A CB  1 
ATOM   1425 C CG  . GLU   A 1 192 ? -9.13907  -25.71341 -5.78093  1.000 30.13856 ? 199 GLU   A CG  1 
ATOM   1426 C CD  . GLU   A 1 192 ? -8.83090  -26.00792 -4.32551  1.000 51.98184 ? 199 GLU   A CD  1 
ATOM   1427 O OE1 . GLU   A 1 192 ? -9.69783  -25.74358 -3.46582  1.000 73.92288 ? 199 GLU   A OE1 1 
ATOM   1428 O OE2 . GLU   A 1 192 ? -7.72108  -26.50546 -4.04101  1.000 58.72138 ? 199 GLU   A OE2 1 
ATOM   1429 N N   . GLU   A 1 193 ? -12.49650 -22.99638 -7.62670  1.000 20.13850 ? 200 GLU   A N   1 
ATOM   1430 C CA  . GLU   A 1 193 ? -13.32732 -21.82244 -7.87403  1.000 20.16910 ? 200 GLU   A CA  1 
ATOM   1431 C C   . GLU   A 1 193 ? -13.13405 -20.76342 -6.79572  1.000 19.24159 ? 200 GLU   A C   1 
ATOM   1432 O O   . GLU   A 1 193 ? -12.97812 -19.57609 -7.09883  1.000 19.08220 ? 200 GLU   A O   1 
ATOM   1433 C CB  . GLU   A 1 193 ? -14.79949 -22.23010 -7.95195  1.000 23.63797 ? 200 GLU   A CB  1 
ATOM   1434 C CG  . GLU   A 1 193 ? -15.70587 -21.10730 -8.42390  1.000 27.00982 ? 200 GLU   A CG  1 
ATOM   1435 C CD  . GLU   A 1 193 ? -17.17547 -21.48451 -8.41714  1.000 52.91315 ? 200 GLU   A CD  1 
ATOM   1436 O OE1 . GLU   A 1 193 ? -17.50767 -22.60028 -7.96609  1.000 38.64739 ? 200 GLU   A OE1 1 
ATOM   1437 O OE2 . GLU   A 1 193 ? -17.99880 -20.66445 -8.87452  1.000 45.86781 ? 200 GLU   A OE2 1 
ATOM   1438 N N   . ARG   A 1 194 ? -13.16507 -21.16926 -5.52409  1.000 22.67303 ? 201 ARG   A N   1 
ATOM   1439 C CA  . ARG   A 1 194 ? -13.09249 -20.17101 -4.46197  1.000 21.82803 ? 201 ARG   A CA  1 
ATOM   1440 C C   . ARG   A 1 194 ? -11.74318 -19.47122 -4.44742  1.000 18.87610 ? 201 ARG   A C   1 
ATOM   1441 O O   . ARG   A 1 194 ? -11.66833 -18.28067 -4.12525  1.000 20.30307 ? 201 ARG   A O   1 
ATOM   1442 C CB  . ARG   A 1 194 ? -13.41581 -20.79273 -3.10307  1.000 25.07198 ? 201 ARG   A CB  1 
ATOM   1443 C CG  . ARG   A 1 194 ? -12.54003 -21.95807 -2.71250  1.000 35.67063 ? 201 ARG   A CG  1 
ATOM   1444 C CD  . ARG   A 1 194 ? -12.77799 -22.31252 -1.25108  1.000 41.12092 ? 201 ARG   A CD  1 
ATOM   1445 N NE  . ARG   A 1 194 ? -11.79679 -23.25952 -0.73905  1.000 46.66740 ? 201 ARG   A NE  1 
ATOM   1446 C CZ  . ARG   A 1 194 ? -11.98276 -24.01230 0.33630   1.000 40.95268 ? 201 ARG   A CZ  1 
ATOM   1447 N NH1 . ARG   A 1 194 ? -13.10522 -23.95230 1.03454   1.000 49.91085 ? 201 ARG   A NH1 1 
ATOM   1448 N NH2 . ARG   A 1 194 ? -11.01582 -24.83838 0.72483   1.000 50.66818 ? 201 ARG   A NH2 1 
ATOM   1449 N N   . ARG   A 1 195 ? -10.67777 -20.18298 -4.81772  1.000 18.08924 ? 202 ARG   A N   1 
ATOM   1450 C CA  . ARG   A 1 195 ? -9.35669  -19.56878 -4.85342  1.000 18.52102 ? 202 ARG   A CA  1 
ATOM   1451 C C   . ARG   A 1 195 ? -9.25634  -18.56805 -5.99604  1.000 17.60768 ? 202 ARG   A C   1 
ATOM   1452 O O   . ARG   A 1 195 ? -8.74671  -17.45626 -5.80981  1.000 16.08075 ? 202 ARG   A O   1 
ATOM   1453 C CB  . ARG   A 1 195 ? -8.28818  -20.65584 -4.98519  1.000 19.52824 ? 202 ARG   A CB  1 
ATOM   1454 C CG  . ARG   A 1 195 ? -6.84830  -20.16117 -4.94510  1.000 19.50999 ? 202 ARG   A CG  1 
ATOM   1455 C CD  . ARG   A 1 195 ? -6.47552  -19.55009 -3.59973  1.000 19.82648 ? 202 ARG   A CD  1 
ATOM   1456 N NE  . ARG   A 1 195 ? -5.03691  -19.31595 -3.51968  1.000 18.86588 ? 202 ARG   A NE  1 
ATOM   1457 C CZ  . ARG   A 1 195 ? -4.46764  -18.13205 -3.32804  1.000 20.99032 ? 202 ARG   A CZ  1 
ATOM   1458 N NH1 . ARG   A 1 195 ? -5.18661  -17.04192 -3.11936  1.000 21.76980 ? 202 ARG   A NH1 1 
ATOM   1459 N NH2 . ARG   A 1 195 ? -3.14009  -18.04080 -3.34648  1.000 19.25727 ? 202 ARG   A NH2 1 
ATOM   1460 N N   . ILE   A 1 196 ? -9.74936  -18.93661 -7.18169  1.000 16.35894 ? 203 ILE   A N   1 
ATOM   1461 C CA  . ILE   A 1 196 ? -9.70642  -18.01129 -8.31060  1.000 15.77470 ? 203 ILE   A CA  1 
ATOM   1462 C C   . ILE   A 1 196 ? -10.54144 -16.77439 -8.00942  1.000 18.12722 ? 203 ILE   A C   1 
ATOM   1463 O O   . ILE   A 1 196 ? -10.10001 -15.64178 -8.23804  1.000 17.51742 ? 203 ILE   A O   1 
ATOM   1464 C CB  . ILE   A 1 196 ? -10.15987 -18.70534 -9.60884  1.000 15.88078 ? 203 ILE   A CB  1 
ATOM   1465 C CG1 . ILE   A 1 196 ? -9.21592  -19.85398 -9.98091  1.000 17.24903 ? 203 ILE   A CG1 1 
ATOM   1466 C CG2 . ILE   A 1 196 ? -10.22697 -17.68864 -10.74909 1.000 18.55032 ? 203 ILE   A CG2 1 
ATOM   1467 C CD1 . ILE   A 1 196 ? -9.81754  -20.82250 -10.98629 1.000 20.82857 ? 203 ILE   A CD1 1 
ATOM   1468 N N   . LYS   A 1 197 ? -11.75366 -16.97156 -7.47471  1.000 16.96092 ? 204 LYS   A N   1 
ATOM   1469 C CA  . LYS   A 1 197 ? -12.61495 -15.84096 -7.13237  1.000 17.08570 ? 204 LYS   A CA  1 
ATOM   1470 C C   . LYS   A 1 197 ? -11.91759 -14.89403 -6.16683  1.000 17.53084 ? 204 LYS   A C   1 
ATOM   1471 O O   . LYS   A 1 197 ? -11.98258 -13.66867 -6.32839  1.000 18.02650 ? 204 LYS   A O   1 
ATOM   1472 C CB  . LYS   A 1 197 ? -13.91323 -16.34333 -6.49308  1.000 18.42894 ? 204 LYS   A CB  1 
ATOM   1473 C CG  . LYS   A 1 197 ? -14.96134 -16.85438 -7.45465  1.000 26.32932 ? 204 LYS   A CG  1 
ATOM   1474 C CD  . LYS   A 1 197 ? -16.17995 -17.35109 -6.67508  1.000 28.84488 ? 204 LYS   A CD  1 
ATOM   1475 C CE  . LYS   A 1 197 ? -17.29858 -17.79412 -7.59673  1.000 42.77285 ? 204 LYS   A CE  1 
ATOM   1476 N NZ  . LYS   A 1 197 ? -18.30794 -18.61108 -6.86203  1.000 50.77000 ? 204 LYS   A NZ  1 
ATOM   1477 N N   . GLU   A 1 198 ? -11.25579 -15.45017 -5.14824  1.000 16.04778 ? 205 GLU   A N   1 
ATOM   1478 C CA  . GLU   A 1 198 ? -10.53936 -14.63729 -4.17243  1.000 18.62830 ? 205 GLU   A CA  1 
ATOM   1479 C C   . GLU   A 1 198 ? -9.45935  -13.79723 -4.83949  1.000 16.28198 ? 205 GLU   A C   1 
ATOM   1480 O O   . GLU   A 1 198 ? -9.32121  -12.60389 -4.54700  1.000 17.36142 ? 205 GLU   A O   1 
ATOM   1481 C CB  . GLU   A 1 198 ? -9.92625  -15.55103 -3.11213  1.000 17.37352 ? 205 GLU   A CB  1 
ATOM   1482 C CG  . GLU   A 1 198 ? -9.03791  -14.83934 -2.10986  1.000 20.09175 ? 205 GLU   A CG  1 
ATOM   1483 C CD  . GLU   A 1 198 ? -8.32610  -15.80191 -1.17439  1.000 19.95250 ? 205 GLU   A CD  1 
ATOM   1484 O OE1 . GLU   A 1 198 ? -7.71172  -16.76447 -1.68694  1.000 22.71467 ? 205 GLU   A OE1 1 
ATOM   1485 O OE2 . GLU   A 1 198 ? -8.36644  -15.58898 0.05132   1.000 22.35032 ? 205 GLU   A OE2 1 
ATOM   1486 N N   . ILE   A 1 199 ? -8.69326  -14.39937 -5.74660  1.000 15.71386 ? 206 ILE   A N   1 
ATOM   1487 C CA  . ILE   A 1 199 ? -7.60448  -13.67515 -6.39344  1.000 16.88751 ? 206 ILE   A CA  1 
ATOM   1488 C C   . ILE   A 1 199 ? -8.14674  -12.56669 -7.28987  1.000 17.82964 ? 206 ILE   A C   1 
ATOM   1489 O O   . ILE   A 1 199 ? -7.61719  -11.44760 -7.30435  1.000 17.84574 ? 206 ILE   A O   1 
ATOM   1490 C CB  . ILE   A 1 199 ? -6.70872  -14.66282 -7.15870  1.000 16.71429 ? 206 ILE   A CB  1 
ATOM   1491 C CG1 . ILE   A 1 199 ? -6.05598  -15.65208 -6.18813  1.000 18.80586 ? 206 ILE   A CG1 1 
ATOM   1492 C CG2 . ILE   A 1 199 ? -5.66675  -13.92311 -7.97745  1.000 17.01107 ? 206 ILE   A CG2 1 
ATOM   1493 C CD1 . ILE   A 1 199 ? -5.53928  -16.89238 -6.88934  1.000 19.58725 ? 206 ILE   A CD1 1 
ATOM   1494 N N   . VAL   A 1 200 ? -9.20556  -12.85650 -8.05144  1.000 15.84776 ? 207 VAL   A N   1 
ATOM   1495 C CA  . VAL   A 1 200 ? -9.78746  -11.84724 -8.93146  1.000 14.26421 ? 207 VAL   A CA  1 
ATOM   1496 C C   . VAL   A 1 200 ? -10.32898 -10.67310 -8.12300  1.000 17.39243 ? 207 VAL   A C   1 
ATOM   1497 O O   . VAL   A 1 200 ? -10.11510 -9.50839  -8.47635  1.000 18.83624 ? 207 VAL   A O   1 
ATOM   1498 C CB  . VAL   A 1 200 ? -10.86285 -12.48602 -9.82873  1.000 15.35581 ? 207 VAL   A CB  1 
ATOM   1499 C CG1 . VAL   A 1 200 ? -11.65673 -11.41746 -10.57751 1.000 16.92616 ? 207 VAL   A CG1 1 
ATOM   1500 C CG2 . VAL   A 1 200 ? -10.20777 -13.45948 -10.80107 1.000 16.75579 ? 207 VAL   A CG2 1 
ATOM   1501 N N   . LYS   A 1 201 ? -11.02327 -10.95824 -7.02042  1.000 16.78899 ? 208 LYS   A N   1 
ATOM   1502 C CA  . LYS   A 1 201 ? -11.56125 -9.88902  -6.18383  1.000 18.47037 ? 208 LYS   A CA  1 
ATOM   1503 C C   . LYS   A 1 201 ? -10.44514 -9.07074  -5.54336  1.000 17.57213 ? 208 LYS   A C   1 
ATOM   1504 O O   . LYS   A 1 201 ? -10.57092 -7.85007  -5.39065  1.000 24.39580 ? 208 LYS   A O   1 
ATOM   1505 C CB  . LYS   A 1 201 ? -12.48153 -10.48512 -5.11602  1.000 21.25008 ? 208 LYS   A CB  1 
ATOM   1506 C CG  . LYS   A 1 201 ? -13.10892 -9.47109  -4.17486  1.000 24.10091 ? 208 LYS   A CG  1 
ATOM   1507 C CD  . LYS   A 1 201 ? -13.87149 -10.15087 -3.05038  1.000 32.53354 ? 208 LYS   A CD  1 
ATOM   1508 C CE  . LYS   A 1 201 ? -14.49378 -9.13549  -2.10879  1.000 39.17633 ? 208 LYS   A CE  1 
ATOM   1509 N NZ  . LYS   A 1 201 ? -15.53513 -9.75622  -1.24426  1.000 49.81138 ? 208 LYS   A NZ  1 
ATOM   1510 N N   . LYS   A 1 202 ? -9.34610  -9.72766  -5.16342  1.000 20.66435 ? 209 LYS   A N   1 
ATOM   1511 C CA  . LYS   A 1 202 ? -8.25677  -9.03829  -4.47439  1.000 21.78979 ? 209 LYS   A CA  1 
ATOM   1512 C C   . LYS   A 1 202 ? -7.47648  -8.12574  -5.41422  1.000 19.45309 ? 209 LYS   A C   1 
ATOM   1513 O O   . LYS   A 1 202 ? -7.13760  -6.99189  -5.04948  1.000 21.73000 ? 209 LYS   A O   1 
ATOM   1514 C CB  . LYS   A 1 202 ? -7.31358  -10.07374 -3.86226  1.000 21.25717 ? 209 LYS   A CB  1 
ATOM   1515 C CG  . LYS   A 1 202 ? -6.11083  -9.48798  -3.13033  1.000 23.90341 ? 209 LYS   A CG  1 
ATOM   1516 C CD  . LYS   A 1 202 ? -5.40435  -10.56238 -2.31678  1.000 34.50993 ? 209 LYS   A CD  1 
ATOM   1517 C CE  . LYS   A 1 202 ? -4.09844  -10.04589 -1.73579  1.000 39.71837 ? 209 LYS   A CE  1 
ATOM   1518 N NZ  . LYS   A 1 202 ? -3.37368  -11.10548 -0.97919  1.000 47.74605 ? 209 LYS   A NZ  1 
ATOM   1519 N N   . HIS   A 1 203 ? -7.17733  -8.59869  -6.62491  1.000 19.32008 ? 210 HIS   A N   1 
ATOM   1520 C CA  . HIS   A 1 203 ? -6.19885  -7.93743  -7.47645  1.000 19.01704 ? 210 HIS   A CA  1 
ATOM   1521 C C   . HIS   A 1 203 ? -6.75633  -7.35178  -8.76297  1.000 20.68561 ? 210 HIS   A C   1 
ATOM   1522 O O   . HIS   A 1 203 ? -6.05200  -6.56546  -9.40865  1.000 23.53715 ? 210 HIS   A O   1 
ATOM   1523 C CB  . HIS   A 1 203 ? -5.07062  -8.90870  -7.85924  1.000 20.92662 ? 210 HIS   A CB  1 
ATOM   1524 C CG  . HIS   A 1 203 ? -4.25736  -9.38800  -6.69844  1.000 22.54870 ? 210 HIS   A CG  1 
ATOM   1525 N ND1 . HIS   A 1 203 ? -3.46987  -8.54739  -5.94157  1.000 26.25463 ? 210 HIS   A ND1 1 
ATOM   1526 C CD2 . HIS   A 1 203 ? -4.10715  -10.62450 -6.16702  1.000 27.02090 ? 210 HIS   A CD2 1 
ATOM   1527 C CE1 . HIS   A 1 203 ? -2.86509  -9.24653  -4.99703  1.000 29.98483 ? 210 HIS   A CE1 1 
ATOM   1528 N NE2 . HIS   A 1 203 ? -3.23753  -10.50893 -5.11006  1.000 28.67002 ? 210 HIS   A NE2 1 
ATOM   1529 N N   . SER   A 1 204 ? -7.96813  -7.71865  -9.17441  1.000 20.98965 ? 211 SER   A N   1 
ATOM   1530 C CA  . SER   A 1 204 ? -8.46277  -7.33765  -10.49069 1.000 19.60223 ? 211 SER   A CA  1 
ATOM   1531 C C   . SER   A 1 204 ? -9.83379  -6.67278  -10.40791 1.000 19.19201 ? 211 SER   A C   1 
ATOM   1532 O O   . SER   A 1 204 ? -10.60700 -6.71010  -11.37177 1.000 21.98356 ? 211 SER   A O   1 
ATOM   1533 C CB  . SER   A 1 204 ? -8.47930  -8.53727  -11.44359 1.000 19.66551 ? 211 SER   A CB  1 
ATOM   1534 O OG  . SER   A 1 204 ? -7.18355  -9.12255  -11.52275 1.000 24.70033 ? 211 SER   A OG  1 
ATOM   1535 N N   . GLN   A 1 205 ? -10.13693 -6.04120  -9.27238  1.000 23.48085 ? 212 GLN   A N   1 
ATOM   1536 C CA  . GLN   A 1 205 ? -11.47358 -5.49521  -9.06904  1.000 29.59366 ? 212 GLN   A CA  1 
ATOM   1537 C C   . GLN   A 1 205 ? -11.79075 -4.33892  -10.01150 1.000 31.77387 ? 212 GLN   A C   1 
ATOM   1538 O O   . GLN   A 1 205 ? -12.97123 -4.06202  -10.25139 1.000 36.96481 ? 212 GLN   A O   1 
ATOM   1539 C CB  . GLN   A 1 205 ? -11.67765 -5.06149  -7.61231  1.000 38.19805 ? 212 GLN   A CB  1 
ATOM   1540 C CG  . GLN   A 1 205 ? -10.78080 -3.92717  -7.13593  1.000 43.21967 ? 212 GLN   A CG  1 
ATOM   1541 C CD  . GLN   A 1 205 ? -9.47073  -4.39373  -6.51906  1.000 59.36188 ? 212 GLN   A CD  1 
ATOM   1542 O OE1 . GLN   A 1 205 ? -8.77973  -5.25760  -7.06035  1.000 35.58007 ? 212 GLN   A OE1 1 
ATOM   1543 N NE2 . GLN   A 1 205 ? -9.12414  -3.81453  -5.37267  1.000 48.75707 ? 212 GLN   A NE2 1 
ATOM   1544 N N   . PHE   A 1 206 ? -10.77643 -3.66374  -10.55653 1.000 25.61482 ? 213 PHE   A N   1 
ATOM   1545 C CA  . PHE   A 1 206 ? -10.99182 -2.48307  -11.38396 1.000 27.59211 ? 213 PHE   A CA  1 
ATOM   1546 C C   . PHE   A 1 206 ? -10.66622 -2.72272  -12.85671 1.000 27.92429 ? 213 PHE   A C   1 
ATOM   1547 O O   . PHE   A 1 206 ? -10.38334 -1.77031  -13.59088 1.000 35.84740 ? 213 PHE   A O   1 
ATOM   1548 C CB  . PHE   A 1 206 ? -10.20518 -1.29659  -10.83030 1.000 30.58486 ? 213 PHE   A CB  1 
ATOM   1549 C CG  . PHE   A 1 206 ? -10.69045 -0.83690  -9.48692  1.000 35.63065 ? 213 PHE   A CG  1 
ATOM   1550 C CD1 . PHE   A 1 206 ? -12.00018 -0.42295  -9.31288  1.000 37.01807 ? 213 PHE   A CD1 1 
ATOM   1551 C CD2 . PHE   A 1 206 ? -9.84036  -0.83331  -8.39475  1.000 39.52755 ? 213 PHE   A CD2 1 
ATOM   1552 C CE1 . PHE   A 1 206 ? -12.45226 -0.00563  -8.07405  1.000 42.20758 ? 213 PHE   A CE1 1 
ATOM   1553 C CE2 . PHE   A 1 206 ? -10.28828 -0.41861  -7.15210  1.000 42.13345 ? 213 PHE   A CE2 1 
ATOM   1554 C CZ  . PHE   A 1 206 ? -11.59512 -0.00395  -6.99364  1.000 40.86240 ? 213 PHE   A CZ  1 
ATOM   1555 N N   . ILE   A 1 207 ? -10.69020 -3.97187  -13.30249 1.000 18.80790 ? 214 ILE   A N   1 
ATOM   1556 C CA  . ILE   A 1 207 ? -10.51017 -4.27550  -14.71688 1.000 17.32114 ? 214 ILE   A CA  1 
ATOM   1557 C C   . ILE   A 1 207 ? -11.82056 -3.99396  -15.44239 1.000 23.21695 ? 214 ILE   A C   1 
ATOM   1558 O O   . ILE   A 1 207 ? -12.88248 -4.48976  -15.04625 1.000 21.86013 ? 214 ILE   A O   1 
ATOM   1559 C CB  . ILE   A 1 207 ? -10.06221 -5.73544  -14.90134 1.000 17.23666 ? 214 ILE   A CB  1 
ATOM   1560 C CG1 . ILE   A 1 207 ? -8.66262  -5.94274  -14.31423 1.000 19.00864 ? 214 ILE   A CG1 1 
ATOM   1561 C CG2 . ILE   A 1 207 ? -10.08193 -6.12731  -16.37102 1.000 18.13026 ? 214 ILE   A CG2 1 
ATOM   1562 C CD1 . ILE   A 1 207 ? -7.57250  -5.16317  -15.01901 1.000 23.14846 ? 214 ILE   A CD1 1 
ATOM   1563 N N   . GLY   A 1 208 ? -11.75131 -3.19513  -16.50482 1.000 17.18910 ? 215 GLY   A N   1 
ATOM   1564 C CA  . GLY   A 1 208 ? -12.94841 -2.67886  -17.14312 1.000 19.81270 ? 215 GLY   A CA  1 
ATOM   1565 C C   . GLY   A 1 208 ? -13.55256 -3.55554  -18.21855 1.000 19.38365 ? 215 GLY   A C   1 
ATOM   1566 O O   . GLY   A 1 208 ? -14.10061 -3.04994  -19.20229 1.000 20.20973 ? 215 GLY   A O   1 
ATOM   1567 N N   . TYR   A 1 209 ? -13.46891 -4.86701  -18.03999 1.000 16.41119 ? 216 TYR   A N   1 
ATOM   1568 C CA  . TYR   A 1 209 ? -14.03594 -5.84027  -18.95772 1.000 17.46692 ? 216 TYR   A CA  1 
ATOM   1569 C C   . TYR   A 1 209 ? -14.61119 -6.96409  -18.12119 1.000 18.57653 ? 216 TYR   A C   1 
ATOM   1570 O O   . TYR   A 1 209 ? -14.11134 -7.24141  -17.02272 1.000 18.66274 ? 216 TYR   A O   1 
ATOM   1571 C CB  . TYR   A 1 209 ? -12.95626 -6.39785  -19.90075 1.000 16.22479 ? 216 TYR   A CB  1 
ATOM   1572 C CG  . TYR   A 1 209 ? -12.37020 -5.32781  -20.78600 1.000 16.29915 ? 216 TYR   A CG  1 
ATOM   1573 C CD1 . TYR   A 1 209 ? -13.04245 -4.89765  -21.92106 1.000 17.53723 ? 216 TYR   A CD1 1 
ATOM   1574 C CD2 . TYR   A 1 209 ? -11.16115 -4.71445  -20.46258 1.000 15.93246 ? 216 TYR   A CD2 1 
ATOM   1575 C CE1 . TYR   A 1 209 ? -12.52502 -3.90226  -22.72134 1.000 16.77078 ? 216 TYR   A CE1 1 
ATOM   1576 C CE2 . TYR   A 1 209 ? -10.62977 -3.71904  -21.25983 1.000 16.65854 ? 216 TYR   A CE2 1 
ATOM   1577 C CZ  . TYR   A 1 209 ? -11.31895 -3.31423  -22.38963 1.000 15.24970 ? 216 TYR   A CZ  1 
ATOM   1578 O OH  . TYR   A 1 209 ? -10.81537 -2.31916  -23.18117 1.000 18.89282 ? 216 TYR   A OH  1 
ATOM   1579 N N   . PRO   A 1 210 ? -15.67417 -7.61633  -18.59028 1.000 16.41469 ? 217 PRO   A N   1 
ATOM   1580 C CA  . PRO   A 1 210 ? -16.24736 -8.72725  -17.82292 1.000 16.85264 ? 217 PRO   A CA  1 
ATOM   1581 C C   . PRO   A 1 210 ? -15.25926 -9.88043  -17.73871 1.000 18.36594 ? 217 PRO   A C   1 
ATOM   1582 O O   . PRO   A 1 210 ? -14.65479 -10.27557 -18.73901 1.000 18.53553 ? 217 PRO   A O   1 
ATOM   1583 C CB  . PRO   A 1 210 ? -17.50931 -9.11402  -18.60797 1.000 19.45409 ? 217 PRO   A CB  1 
ATOM   1584 C CG  . PRO   A 1 210 ? -17.47823 -8.35419  -19.87794 1.000 25.52591 ? 217 PRO   A CG  1 
ATOM   1585 C CD  . PRO   A 1 210 ? -16.42893 -7.29254  -19.81528 1.000 18.64858 ? 217 PRO   A CD  1 
ATOM   1586 N N   . ILE   A 1 211 ? -15.07699 -10.38884 -16.52749 1.000 16.12575 ? 218 ILE   A N   1 
ATOM   1587 C CA  . ILE   A 1 211 ? -14.23056 -11.54250 -16.25610 1.000 15.08689 ? 218 ILE   A CA  1 
ATOM   1588 C C   . ILE   A 1 211 ? -15.17563 -12.65322 -15.83323 1.000 15.40744 ? 218 ILE   A C   1 
ATOM   1589 O O   . ILE   A 1 211 ? -15.82023 -12.56321 -14.78089 1.000 18.92134 ? 218 ILE   A O   1 
ATOM   1590 C CB  . ILE   A 1 211 ? -13.20851 -11.25535 -15.15068 1.000 15.47091 ? 218 ILE   A CB  1 
ATOM   1591 C CG1 . ILE   A 1 211 ? -12.27843 -10.10656 -15.55098 1.000 15.04328 ? 218 ILE   A CG1 1 
ATOM   1592 C CG2 . ILE   A 1 211 ? -12.39586 -12.50358 -14.86779 1.000 17.67219 ? 218 ILE   A CG2 1 
ATOM   1593 C CD1 . ILE   A 1 211 ? -11.48105 -9.56693  -14.38328 1.000 17.07885 ? 218 ILE   A CD1 1 
ATOM   1594 N N   . THR   A 1 212 ? -15.28405 -13.68999 -16.65286 1.000 15.34250 ? 219 THR   A N   1 
ATOM   1595 C CA  . THR   A 1 212 ? -16.20985 -14.78376 -16.38752 1.000 15.16077 ? 219 THR   A CA  1 
ATOM   1596 C C   . THR   A 1 212 ? -15.39738 -15.99805 -15.97207 1.000 14.05770 ? 219 THR   A C   1 
ATOM   1597 O O   . THR   A 1 212 ? -14.56276 -16.48482 -16.74274 1.000 14.58268 ? 219 THR   A O   1 
ATOM   1598 C CB  . THR   A 1 212 ? -17.04801 -15.11298 -17.62148 1.000 15.39938 ? 219 THR   A CB  1 
ATOM   1599 O OG1 . THR   A 1 212 ? -17.79962 -13.95831 -18.01817 1.000 18.20241 ? 219 THR   A OG1 1 
ATOM   1600 C CG2 . THR   A 1 212 ? -18.02475 -16.26356 -17.30276 1.000 16.71647 ? 219 THR   A CG2 1 
ATOM   1601 N N   . LEU   A 1 213 ? -15.64233 -16.48301 -14.76100 1.000 15.09602 ? 220 LEU   A N   1 
ATOM   1602 C CA  . LEU   A 1 213 ? -15.00616 -17.69407 -14.26335 1.000 15.71667 ? 220 LEU   A CA  1 
ATOM   1603 C C   . LEU   A 1 213 ? -15.91114 -18.87091 -14.60647 1.000 14.98875 ? 220 LEU   A C   1 
ATOM   1604 O O   . LEU   A 1 213 ? -17.02020 -18.99137 -14.06735 1.000 16.58346 ? 220 LEU   A O   1 
ATOM   1605 C CB  . LEU   A 1 213 ? -14.77574 -17.58755 -12.75888 1.000 18.38447 ? 220 LEU   A CB  1 
ATOM   1606 C CG  . LEU   A 1 213 ? -14.21310 -18.82227 -12.05686 1.000 19.00781 ? 220 LEU   A CG  1 
ATOM   1607 C CD1 . LEU   A 1 213 ? -12.95628 -19.33045 -12.75283 1.000 18.76424 ? 220 LEU   A CD1 1 
ATOM   1608 C CD2 . LEU   A 1 213 ? -13.93630 -18.50879 -10.57976 1.000 20.21817 ? 220 LEU   A CD2 1 
ATOM   1609 N N   . PHE   A 1 214 ? -15.44785 -19.71518 -15.52337 1.000 15.29439 ? 221 PHE   A N   1 
ATOM   1610 C CA  . PHE   A 1 214 ? -16.19984 -20.89641 -15.90968 1.000 15.05609 ? 221 PHE   A CA  1 
ATOM   1611 C C   . PHE   A 1 214 ? -16.17552 -21.90690 -14.77204 1.000 16.61762 ? 221 PHE   A C   1 
ATOM   1612 O O   . PHE   A 1 214 ? -15.20756 -21.99494 -14.01137 1.000 18.96131 ? 221 PHE   A O   1 
ATOM   1613 C CB  . PHE   A 1 214 ? -15.56780 -21.56302 -17.13104 1.000 15.45655 ? 221 PHE   A CB  1 
ATOM   1614 C CG  . PHE   A 1 214 ? -15.83965 -20.86933 -18.44442 1.000 14.44974 ? 221 PHE   A CG  1 
ATOM   1615 C CD1 . PHE   A 1 214 ? -15.97083 -19.48874 -18.52725 1.000 15.84584 ? 221 PHE   A CD1 1 
ATOM   1616 C CD2 . PHE   A 1 214 ? -15.92596 -21.61707 -19.61303 1.000 17.37294 ? 221 PHE   A CD2 1 
ATOM   1617 C CE1 . PHE   A 1 214 ? -16.19910 -18.86932 -19.75930 1.000 15.49750 ? 221 PHE   A CE1 1 
ATOM   1618 C CE2 . PHE   A 1 214 ? -16.15505 -21.00744 -20.83798 1.000 17.50015 ? 221 PHE   A CE2 1 
ATOM   1619 C CZ  . PHE   A 1 214 ? -16.29611 -19.63383 -20.90954 1.000 15.98076 ? 221 PHE   A CZ  1 
ATOM   1620 N N   . VAL   A 1 215 ? -17.24805 -22.67864 -14.65906 1.000 17.17992 ? 222 VAL   A N   1 
ATOM   1621 C CA  . VAL   A 1 215 ? -17.30133 -23.76710 -13.69677 1.000 18.54252 ? 222 VAL   A CA  1 
ATOM   1622 C C   . VAL   A 1 215 ? -17.15319 -25.08671 -14.43971 1.000 20.05566 ? 222 VAL   A C   1 
ATOM   1623 O O   . VAL   A 1 215 ? -17.26245 -25.15902 -15.66806 1.000 22.75860 ? 222 VAL   A O   1 
ATOM   1624 C CB  . VAL   A 1 215 ? -18.56788 -23.74292 -12.82093 1.000 31.89356 ? 222 VAL   A CB  1 
ATOM   1625 C CG1 . VAL   A 1 215 ? -18.46879 -22.62730 -11.78144 1.000 37.35805 ? 222 VAL   A CG1 1 
ATOM   1626 C CG2 . VAL   A 1 215 ? -19.78958 -23.55816 -13.68479 1.000 25.13832 ? 222 VAL   A CG2 1 
ATOM   1627 N N   . GLU   A 1 216 ? -16.87390 -26.13889 -13.68105 1.000 22.48537 ? 223 GLU   A N   1 
ATOM   1628 C CA  . GLU   A 1 216 ? -16.62928 -27.45867 -14.24253 1.000 26.91431 ? 223 GLU   A CA  1 
ATOM   1629 C C   . GLU   A 1 216 ? -17.72885 -28.43236 -13.84298 1.000 32.94167 ? 223 GLU   A C   1 
ATOM   1630 O O   . GLU   A 1 216 ? -18.35430 -28.29085 -12.78835 1.000 33.61566 ? 223 GLU   A O   1 
ATOM   1631 C CB  . GLU   A 1 216 ? -15.27378 -28.00368 -13.78892 1.000 30.08799 ? 223 GLU   A CB  1 
ATOM   1632 C CG  . GLU   A 1 216 ? -14.13337 -27.02588 -13.98584 1.000 27.36391 ? 223 GLU   A CG  1 
ATOM   1633 C CD  . GLU   A 1 216 ? -12.80086 -27.60780 -13.56296 1.000 29.30274 ? 223 GLU   A CD  1 
ATOM   1634 O OE1 . GLU   A 1 216 ? -12.42926 -28.68353 -14.08029 1.000 30.48702 ? 223 GLU   A OE1 1 
ATOM   1635 O OE2 . GLU   A 1 216 ? -12.13166 -26.98871 -12.70800 1.000 32.67723 ? 223 GLU   A OE2 1 
ATOM   1636 N N   . LYS   A 1 217 ? -17.94676 -29.42903 -14.70019 1.000 32.62909 ? 224 LYS   A N   1 
ATOM   1637 C CA  . LYS   A 1 217 ? -18.92083 -30.48917 -14.45694 1.000 39.62063 ? 224 LYS   A CA  1 
ATOM   1638 C C   . LYS   A 1 217 ? -18.67835 -31.18328 -13.11978 1.000 55.03305 ? 224 LYS   A C   1 
ATOM   1639 O O   . LYS   A 1 217 ? -17.53920 -31.48276 -12.76481 1.000 53.05585 ? 224 LYS   A O   1 
ATOM   1640 C CB  . LYS   A 1 217 ? -18.86874 -31.52361 -15.58647 1.000 46.05284 ? 224 LYS   A CB  1 
ATOM   1641 C CG  . LYS   A 1 217 ? -19.35856 -32.90936 -15.18975 1.000 61.16558 ? 224 LYS   A CG  1 
ATOM   1642 C CD  . LYS   A 1 217 ? -19.78115 -33.72359 -16.40403 1.000 62.61079 ? 224 LYS   A CD  1 
ATOM   1643 C CE  . LYS   A 1 217 ? -19.08237 -35.07590 -16.43141 1.000 65.27497 ? 224 LYS   A CE  1 
ATOM   1644 N NZ  . LYS   A 1 217 ? -19.77103 -36.08002 -15.57405 1.000 57.89112 ? 224 LYS   A NZ  1 
HETATM 1645 C C1  . A1AW8 B 2 .   ? -13.21136 -15.92371 -28.45486 1.000 56.52430 ? 301 A1AW8 A C1  1 
HETATM 1646 C C2  . A1AW8 B 2 .   ? -13.01922 -17.20973 -27.66099 1.000 71.31542 ? 301 A1AW8 A C2  1 
HETATM 1647 C C3  . A1AW8 B 2 .   ? -13.80634 -17.19504 -26.39771 1.000 52.75496 ? 301 A1AW8 A C3  1 
HETATM 1648 C C4  . A1AW8 B 2 .   ? -13.62112 -18.46404 -25.60594 1.000 63.67254 ? 301 A1AW8 A C4  1 
HETATM 1649 C C5  . A1AW8 B 2 .   ? -13.15929 -19.68769 -27.73084 1.000 70.98763 ? 301 A1AW8 A C5  1 
HETATM 1650 C C6  . A1AW8 B 2 .   ? -13.34573 -18.40019 -28.48899 1.000 68.71787 ? 301 A1AW8 A C6  1 
HETATM 1651 C C7  . A1AW8 B 2 .   ? -13.04943 -20.85382 -25.58783 1.000 67.20110 ? 301 A1AW8 A C7  1 
HETATM 1652 N N1  . A1AW8 B 2 .   ? -13.29982 -19.62679 -26.33173 1.000 73.30887 ? 301 A1AW8 A N1  1 
HETATM 1653 O O2  . A1AW8 B 2 .   ? -12.88183 -20.73402 -28.27850 0.592 67.52290 ? 301 A1AW8 A O2  1 
HETATM 1654 C C10 . A1AW8 B 2 .   ? -12.54216 -23.18382 -24.17987 1.000 50.70577 ? 301 A1AW8 A C10 1 
HETATM 1655 C C11 . A1AW8 B 2 .   ? -11.48107 -22.51306 -24.73052 1.000 55.03006 ? 301 A1AW8 A C11 1 
HETATM 1656 C C12 . A1AW8 B 2 .   ? -11.76831 -21.36247 -25.42083 1.000 67.28165 ? 301 A1AW8 A C12 1 
HETATM 1657 C C8  . A1AW8 B 2 .   ? -14.07032 -21.57975 -25.00484 1.000 45.35629 ? 301 A1AW8 A C8  1 
HETATM 1658 C C9  . A1AW8 B 2 .   ? -13.83232 -22.74743 -24.29847 0.149 45.12557 ? 301 A1AW8 A C9  1 
HETATM 1659 F F1  . A1AW8 B 2 .   ? -12.29474 -24.32625 -23.49013 1.000 50.52800 ? 301 A1AW8 A F1  1 
HETATM 1660 F F2  . A1AW8 B 2 .   ? -10.72978 -20.68087 -25.97716 1.000 75.80727 ? 301 A1AW8 A F2  1 
HETATM 1661 O O1  . A1AW8 B 2 .   ? -13.72391 -18.50143 -24.39781 1.000 21.83296 ? 301 A1AW8 A O1  1 
HETATM 1662 O O   . HOH   C 3 .   ? 17.82135  -4.05229  -7.71791  1.000 58.05353 ? 401 HOH   A O   1 
HETATM 1663 O O   . HOH   C 3 .   ? -17.88759 -5.09709  -37.39652 1.000 50.72777 ? 402 HOH   A O   1 
HETATM 1664 O O   . HOH   C 3 .   ? 9.51846   -23.61190 -41.09596 1.000 58.07886 ? 403 HOH   A O   1 
HETATM 1665 O O   . HOH   C 3 .   ? 21.64422  -3.39440  -15.16206 1.000 51.50057 ? 404 HOH   A O   1 
HETATM 1666 O O   . HOH   C 3 .   ? -17.65182 -24.68007 -8.90901  1.000 46.49537 ? 405 HOH   A O   1 
HETATM 1667 O O   . HOH   C 3 .   ? 2.09311   -15.73571 -41.07100 1.000 42.95986 ? 406 HOH   A O   1 
HETATM 1668 O O   . HOH   C 3 .   ? -9.35961  -23.63915 -2.39204  1.000 50.81320 ? 407 HOH   A O   1 
HETATM 1669 O O   . HOH   C 3 .   ? 11.649    -21.662   -40.531   1.000 48.52270 ? 408 HOH   A O   1 
HETATM 1670 O O   . HOH   C 3 .   ? 13.89984  -11.22032 -29.48668 1.000 38.37247 ? 409 HOH   A O   1 
HETATM 1671 O O   . HOH   C 3 .   ? -13.84885 -7.37889  -42.14811 1.000 47.61608 ? 410 HOH   A O   1 
HETATM 1672 O O   . HOH   C 3 .   ? 9.22010   -3.25049  -20.33005 1.000 29.42369 ? 411 HOH   A O   1 
HETATM 1673 O O   . HOH   C 3 .   ? -3.78565  -13.34559 -42.76185 1.000 45.41613 ? 412 HOH   A O   1 
HETATM 1674 O O   . HOH   C 3 .   ? -1.54430  -29.06611 -5.90175  1.000 30.10569 ? 413 HOH   A O   1 
HETATM 1675 O O   . HOH   C 3 .   ? 3.21746   -24.48655 -38.58794 1.000 31.82729 ? 414 HOH   A O   1 
HETATM 1676 O O   . HOH   C 3 .   ? -20.50631 -20.73409 -9.36236  1.000 43.56353 ? 415 HOH   A O   1 
HETATM 1677 O O   . HOH   C 3 .   ? -16.15738 -25.63303 -17.93166 1.000 25.46473 ? 416 HOH   A O   1 
HETATM 1678 O O   . HOH   C 3 .   ? -12.24055 -27.93814 -30.13131 1.000 34.34883 ? 417 HOH   A O   1 
HETATM 1679 O O   . HOH   C 3 .   ? -13.03390 -7.38022  -11.91625 1.000 34.57670 ? 418 HOH   A O   1 
HETATM 1680 O O   . HOH   C 3 .   ? 5.91967   -21.82458 -37.34375 1.000 30.84543 ? 419 HOH   A O   1 
HETATM 1681 O O   . HOH   C 3 .   ? -2.80227  -3.20063  -35.33381 1.000 39.86019 ? 420 HOH   A O   1 
HETATM 1682 O O   . HOH   C 3 .   ? -7.43534  -28.02813 -21.07294 1.000 42.11186 ? 421 HOH   A O   1 
HETATM 1683 O O   . HOH   C 3 .   ? 5.83667   -25.45489 -7.31590  1.000 40.87398 ? 422 HOH   A O   1 
HETATM 1684 O O   . HOH   C 3 .   ? 11.94633  -2.28361  -3.74314  1.000 47.13755 ? 423 HOH   A O   1 
HETATM 1685 O O   . HOH   C 3 .   ? 15.05629  -0.76106  -12.08212 1.000 40.46851 ? 424 HOH   A O   1 
HETATM 1686 O O   . HOH   C 3 .   ? -4.50102  0.60370   -22.23953 1.000 30.74913 ? 425 HOH   A O   1 
HETATM 1687 O O   . HOH   C 3 .   ? 0.21821   -28.40102 -25.58066 1.000 43.19553 ? 426 HOH   A O   1 
HETATM 1688 O O   . HOH   C 3 .   ? 7.69785   -18.74895 -6.50979  1.000 21.33008 ? 427 HOH   A O   1 
HETATM 1689 O O   . HOH   C 3 .   ? 3.03150   -5.91954  -6.15081  1.000 47.18911 ? 428 HOH   A O   1 
HETATM 1690 O O   . HOH   C 3 .   ? 6.63279   -26.61946 -27.70506 1.000 29.72375 ? 429 HOH   A O   1 
HETATM 1691 O O   . HOH   C 3 .   ? 3.18490   -6.14985  -11.10372 1.000 21.40326 ? 430 HOH   A O   1 
HETATM 1692 O O   . HOH   C 3 .   ? -13.31168 -0.84073  -20.36930 1.000 31.40817 ? 431 HOH   A O   1 
HETATM 1693 O O   . HOH   C 3 .   ? -15.85428 0.15712   -30.36739 1.000 37.72140 ? 432 HOH   A O   1 
HETATM 1694 O O   . HOH   C 3 .   ? -2.88034  -6.05101  -6.48607  1.000 36.49751 ? 433 HOH   A O   1 
HETATM 1695 O O   . HOH   C 3 .   ? 6.00519   -21.13735 -0.06143  1.000 25.99992 ? 434 HOH   A O   1 
HETATM 1696 O O   . HOH   C 3 .   ? 0.34471   -1.53578  -19.83744 1.000 33.27685 ? 435 HOH   A O   1 
HETATM 1697 O O   . HOH   C 3 .   ? -5.76204  -2.09188  -19.42884 1.000 20.78495 ? 436 HOH   A O   1 
HETATM 1698 O O   . HOH   C 3 .   ? 10.12242  -23.86728 -9.15704  1.000 42.47043 ? 437 HOH   A O   1 
HETATM 1699 O O   . HOH   C 3 .   ? 7.82417   -23.10557 -14.26872 1.000 26.03324 ? 438 HOH   A O   1 
HETATM 1700 O O   . HOH   C 3 .   ? 18.21948  -7.21284  -20.18139 1.000 28.85046 ? 439 HOH   A O   1 
HETATM 1701 O O   . HOH   C 3 .   ? 0.27472   -14.93795 -1.46797  1.000 36.43015 ? 440 HOH   A O   1 
HETATM 1702 O O   . HOH   C 3 .   ? -13.64892 -36.51892 -14.02958 1.000 55.99831 ? 441 HOH   A O   1 
HETATM 1703 O O   . HOH   C 3 .   ? -0.99880  -11.42624 -3.01343  1.000 34.14157 ? 442 HOH   A O   1 
HETATM 1704 O O   . HOH   C 3 .   ? -12.33434 -25.85979 -3.65823  1.000 44.97871 ? 443 HOH   A O   1 
HETATM 1705 O O   . HOH   C 3 .   ? -8.71227  -11.84674 -36.38284 1.000 22.56167 ? 444 HOH   A O   1 
HETATM 1706 O O   . HOH   C 3 .   ? -4.27524  -4.82746  -8.48793  1.000 39.82826 ? 445 HOH   A O   1 
HETATM 1707 O O   . HOH   C 3 .   ? 1.39928   -7.80865  -16.49063 1.000 19.84858 ? 446 HOH   A O   1 
HETATM 1708 O O   . HOH   C 3 .   ? -14.52256 -7.12075  -14.39181 1.000 34.95233 ? 447 HOH   A O   1 
HETATM 1709 O O   . HOH   C 3 .   ? -11.82691 -0.34834  -15.32597 1.000 31.11609 ? 448 HOH   A O   1 
HETATM 1710 O O   . HOH   C 3 .   ? -3.34097  -12.08829 -9.06544  1.000 32.97215 ? 449 HOH   A O   1 
HETATM 1711 O O   . HOH   C 3 .   ? 9.86525   -14.71743 -25.20006 1.000 17.75800 ? 450 HOH   A O   1 
HETATM 1712 O O   . HOH   C 3 .   ? -16.23445 -12.71835 -19.79319 1.000 18.08001 ? 451 HOH   A O   1 
HETATM 1713 O O   . HOH   C 3 .   ? 7.56959   1.29584   -14.71543 1.000 31.54078 ? 452 HOH   A O   1 
HETATM 1714 O O   . HOH   C 3 .   ? -12.95471 -24.98448 -10.89517 1.000 29.74524 ? 453 HOH   A O   1 
HETATM 1715 O O   . HOH   C 3 .   ? -7.78738  -22.83762 -30.33731 1.000 40.78125 ? 454 HOH   A O   1 
HETATM 1716 O O   . HOH   C 3 .   ? 8.47293   -0.42789  -17.30091 1.000 32.91614 ? 455 HOH   A O   1 
HETATM 1717 O O   . HOH   C 3 .   ? -2.20784  -13.65038 -35.58617 1.000 18.51063 ? 456 HOH   A O   1 
HETATM 1718 O O   . HOH   C 3 .   ? 7.69966   -27.73479 -24.09682 1.000 30.97732 ? 457 HOH   A O   1 
HETATM 1719 O O   . HOH   C 3 .   ? -8.47077  4.73829   -33.47911 1.000 27.54940 ? 458 HOH   A O   1 
HETATM 1720 O O   . HOH   C 3 .   ? -3.60840  -10.73738 -24.06345 1.000 23.86735 ? 459 HOH   A O   1 
HETATM 1721 O O   . HOH   C 3 .   ? 9.18890   -26.42362 -17.09689 1.000 26.92667 ? 460 HOH   A O   1 
HETATM 1722 O O   . HOH   C 3 .   ? 6.67510   -29.65511 -20.22396 1.000 31.60260 ? 461 HOH   A O   1 
HETATM 1723 O O   . HOH   C 3 .   ? -7.48696  -5.48460  -2.83997  1.000 44.63269 ? 462 HOH   A O   1 
HETATM 1724 O O   . HOH   C 3 .   ? -0.15743  -5.68112  -38.41527 1.000 39.33242 ? 463 HOH   A O   1 
HETATM 1725 O O   . HOH   C 3 .   ? -4.31272  -4.29094  -37.22171 1.000 40.84495 ? 464 HOH   A O   1 
HETATM 1726 O O   . HOH   C 3 .   ? 0.87555   -21.06943 -4.65914  1.000 24.95901 ? 465 HOH   A O   1 
HETATM 1727 O O   . HOH   C 3 .   ? -2.47473  -10.63160 -26.54223 1.000 27.60250 ? 466 HOH   A O   1 
HETATM 1728 O O   . HOH   C 3 .   ? 0.70714   -29.59502 -16.00655 1.000 34.14714 ? 467 HOH   A O   1 
HETATM 1729 O O   . HOH   C 3 .   ? -6.40655  -7.71824  -34.32962 1.000 17.95309 ? 468 HOH   A O   1 
HETATM 1730 O O   . HOH   C 3 .   ? 13.57748  -14.14464 -26.82305 1.000 19.25958 ? 469 HOH   A O   1 
HETATM 1731 O O   . HOH   C 3 .   ? -5.48738  -7.69970  -13.09704 1.000 19.12938 ? 470 HOH   A O   1 
HETATM 1732 O O   . HOH   C 3 .   ? 9.76915   -17.31017 -7.75058  1.000 20.83904 ? 471 HOH   A O   1 
HETATM 1733 O O   . HOH   C 3 .   ? -10.70342 -14.57598 1.00375   1.000 25.38917 ? 472 HOH   A O   1 
HETATM 1734 O O   . HOH   C 3 .   ? -3.94074  -13.99686 -0.89493  1.000 38.44245 ? 473 HOH   A O   1 
HETATM 1735 O O   . HOH   C 3 .   ? -17.02168 -5.41877  -22.71122 1.000 25.59121 ? 474 HOH   A O   1 
HETATM 1736 O O   . HOH   C 3 .   ? 11.33435  -28.31934 -30.45675 1.000 31.06426 ? 475 HOH   A O   1 
HETATM 1737 O O   . HOH   C 3 .   ? -8.09577  1.80888   -36.45506 1.000 33.57856 ? 476 HOH   A O   1 
HETATM 1738 O O   . HOH   C 3 .   ? 0.57443   -27.00793 -37.20155 1.000 42.33238 ? 477 HOH   A O   1 
HETATM 1739 O O   . HOH   C 3 .   ? -2.28762  -24.73801 -1.29174  1.000 47.16282 ? 478 HOH   A O   1 
HETATM 1740 O O   . HOH   C 3 .   ? -0.26079  -5.43355  -18.34553 1.000 25.09108 ? 479 HOH   A O   1 
HETATM 1741 O O   . HOH   C 3 .   ? -5.31189  -10.37801 -27.36061 1.000 15.73448 ? 480 HOH   A O   1 
HETATM 1742 O O   . HOH   C 3 .   ? 3.68630   -29.80647 -25.87439 1.000 42.56183 ? 481 HOH   A O   1 
HETATM 1743 O O   . HOH   C 3 .   ? 8.81330   -15.45250 -27.78313 1.000 15.79817 ? 482 HOH   A O   1 
HETATM 1744 O O   . HOH   C 3 .   ? 12.95209  -13.87184 -29.60856 1.000 25.13782 ? 483 HOH   A O   1 
HETATM 1745 O O   . HOH   C 3 .   ? -8.10537  -24.83037 -19.09942 1.000 16.94075 ? 484 HOH   A O   1 
HETATM 1746 O O   . HOH   C 3 .   ? 3.60409   -7.60126  -36.52760 1.000 31.36725 ? 485 HOH   A O   1 
HETATM 1747 O O   . HOH   C 3 .   ? 3.04330   -20.45840 -2.78659  1.000 32.17735 ? 486 HOH   A O   1 
HETATM 1748 O O   . HOH   C 3 .   ? -3.83552  -3.36378  -15.28943 1.000 34.23611 ? 487 HOH   A O   1 
HETATM 1749 O O   . HOH   C 3 .   ? -8.05276  -3.92403  -10.70933 1.000 26.32508 ? 488 HOH   A O   1 
HETATM 1750 O O   . HOH   C 3 .   ? 17.99405  -19.24774 -24.60299 1.000 29.24577 ? 489 HOH   A O   1 
HETATM 1751 O O   . HOH   C 3 .   ? 11.23330  -8.02633  -27.39671 1.000 21.30681 ? 490 HOH   A O   1 
HETATM 1752 O O   . HOH   C 3 .   ? 19.90216  -10.43963 -26.36423 1.000 36.44668 ? 491 HOH   A O   1 
HETATM 1753 O O   . HOH   C 3 .   ? 11.58368  -27.31282 -34.70668 1.000 22.37475 ? 492 HOH   A O   1 
HETATM 1754 O O   . HOH   C 3 .   ? -6.56762  -4.95253  -39.04159 1.000 43.98221 ? 493 HOH   A O   1 
HETATM 1755 O O   . HOH   C 3 .   ? -20.53435 -14.13489 -18.27397 1.000 37.17198 ? 494 HOH   A O   1 
HETATM 1756 O O   . HOH   C 3 .   ? -19.71765 -19.51625 -14.27002 1.000 19.26861 ? 495 HOH   A O   1 
HETATM 1757 O O   . HOH   C 3 .   ? -10.96636 -14.14883 -37.71912 1.000 32.21570 ? 496 HOH   A O   1 
HETATM 1758 O O   . HOH   C 3 .   ? -9.70362  -33.78170 -21.22581 1.000 52.85351 ? 497 HOH   A O   1 
HETATM 1759 O O   . HOH   C 3 .   ? 6.191     1.078     -7.563    1.000 52.44693 ? 498 HOH   A O   1 
HETATM 1760 O O   . HOH   C 3 .   ? -1.13567  -7.36367  -23.58862 1.000 23.13348 ? 499 HOH   A O   1 
HETATM 1761 O O   . HOH   C 3 .   ? 10.66838  -25.31615 -23.77064 1.000 22.10150 ? 500 HOH   A O   1 
HETATM 1762 O O   . HOH   C 3 .   ? -14.59110 -22.71757 -11.41384 1.000 28.78656 ? 501 HOH   A O   1 
HETATM 1763 O O   . HOH   C 3 .   ? -17.92550 -3.83479  -28.89888 1.000 43.13018 ? 502 HOH   A O   1 
HETATM 1764 O O   . HOH   C 3 .   ? -9.35028  -2.25015  -17.56521 1.000 19.09376 ? 503 HOH   A O   1 
HETATM 1765 O O   . HOH   C 3 .   ? -1.36497  -4.57348  -33.71098 1.000 34.90511 ? 504 HOH   A O   1 
HETATM 1766 O O   . HOH   C 3 .   ? 8.54032   -16.14707 -39.47370 1.000 33.16959 ? 505 HOH   A O   1 
HETATM 1767 O O   . HOH   C 3 .   ? -7.65368  -24.36424 -23.05908 1.000 28.42566 ? 506 HOH   A O   1 
HETATM 1768 O O   . HOH   C 3 .   ? -19.75551 -12.88751 -16.36552 1.000 40.73311 ? 507 HOH   A O   1 
HETATM 1769 O O   . HOH   C 3 .   ? -3.02456  -31.28522 -20.07978 1.000 46.29176 ? 508 HOH   A O   1 
HETATM 1770 O O   . HOH   C 3 .   ? -15.20636 -11.11317 -29.70435 1.000 23.83136 ? 509 HOH   A O   1 
HETATM 1771 O O   . HOH   C 3 .   ? 3.40743   -29.98579 -19.11335 1.000 45.20137 ? 510 HOH   A O   1 
HETATM 1772 O O   . HOH   C 3 .   ? -10.29355 -0.68728  -19.98898 1.000 26.25076 ? 511 HOH   A O   1 
HETATM 1773 O O   . HOH   C 3 .   ? -7.67963  -28.32140 -8.04120  1.000 28.66017 ? 512 HOH   A O   1 
HETATM 1774 O O   . HOH   C 3 .   ? -1.56045  -6.30318  -26.09431 1.000 20.60058 ? 513 HOH   A O   1 
HETATM 1775 O O   . HOH   C 3 .   ? -1.14587  -25.92030 -32.42940 1.000 37.86282 ? 514 HOH   A O   1 
HETATM 1776 O O   . HOH   C 3 .   ? 0.64998   -5.24147  -13.99131 1.000 34.19793 ? 515 HOH   A O   1 
HETATM 1777 O O   . HOH   C 3 .   ? 0.35870   -22.18272 -2.04537  1.000 43.89398 ? 516 HOH   A O   1 
HETATM 1778 O O   . HOH   C 3 .   ? 4.98573   -9.92094  -2.49198  1.000 42.77301 ? 517 HOH   A O   1 
HETATM 1779 O O   . HOH   C 3 .   ? -0.30025  -7.08883  -30.95189 1.000 29.77182 ? 518 HOH   A O   1 
HETATM 1780 O O   . HOH   C 3 .   ? -7.58025  -13.46565 -40.86457 1.000 42.25740 ? 519 HOH   A O   1 
HETATM 1781 O O   . HOH   C 3 .   ? -2.05929  -0.56871  -18.58945 1.000 31.29958 ? 520 HOH   A O   1 
HETATM 1782 O O   . HOH   C 3 .   ? -5.73866  -31.14320 -11.62570 1.000 29.36082 ? 521 HOH   A O   1 
HETATM 1783 O O   . HOH   C 3 .   ? 4.12091   -24.12658 -30.68163 1.000 18.97990 ? 522 HOH   A O   1 
HETATM 1784 O O   . HOH   C 3 .   ? -6.35227  -5.07314  -35.55128 1.000 21.71717 ? 523 HOH   A O   1 
HETATM 1785 O O   . HOH   C 3 .   ? -6.28810  -11.33278 -10.05433 1.000 22.45462 ? 524 HOH   A O   1 
HETATM 1786 O O   . HOH   C 3 .   ? 14.03981  -15.62675 -2.00652  1.000 30.07377 ? 525 HOH   A O   1 
HETATM 1787 O O   . HOH   C 3 .   ? 10.39470  -21.16242 -6.91681  1.000 35.36553 ? 526 HOH   A O   1 
HETATM 1788 O O   . HOH   C 3 .   ? -14.15661 -12.69532 -7.82830  1.000 22.49828 ? 527 HOH   A O   1 
HETATM 1789 O O   . HOH   C 3 .   ? -13.74486 -17.02648 -2.68680  1.000 24.72786 ? 528 HOH   A O   1 
HETATM 1790 O O   . HOH   C 3 .   ? 9.62347   -11.14877 -34.74077 1.000 35.12394 ? 529 HOH   A O   1 
HETATM 1791 O O   . HOH   C 3 .   ? 1.44689   -3.03211  -24.47019 1.000 35.42068 ? 530 HOH   A O   1 
HETATM 1792 O O   . HOH   C 3 .   ? -7.21217  1.28426   -19.37342 1.000 27.35157 ? 531 HOH   A O   1 
HETATM 1793 O O   . HOH   C 3 .   ? -5.67995  -28.36667 -4.91352  1.000 49.29889 ? 532 HOH   A O   1 
HETATM 1794 O O   . HOH   C 3 .   ? 7.31619   -4.66238  -22.20847 1.000 31.98099 ? 533 HOH   A O   1 
HETATM 1795 O O   . HOH   C 3 .   ? 8.06104   -23.16118 -7.15327  1.000 33.50092 ? 534 HOH   A O   1 
HETATM 1796 O O   . HOH   C 3 .   ? -16.05059 -3.03567  -21.25541 1.000 26.31700 ? 535 HOH   A O   1 
HETATM 1797 O O   . HOH   C 3 .   ? -10.69492 -6.29996  -3.02311  1.000 45.36239 ? 536 HOH   A O   1 
HETATM 1798 O O   . HOH   C 3 .   ? -10.38311 -11.52578 -2.15111  1.000 21.88106 ? 537 HOH   A O   1 
HETATM 1799 O O   . HOH   C 3 .   ? 8.46147   -20.44695 -9.23508  1.000 26.64601 ? 538 HOH   A O   1 
HETATM 1800 O O   . HOH   C 3 .   ? -13.50444 -26.52219 -18.03962 1.000 23.77464 ? 539 HOH   A O   1 
HETATM 1801 O O   . HOH   C 3 .   ? 3.58043   -6.71667  -17.85822 1.000 21.67796 ? 540 HOH   A O   1 
HETATM 1802 O O   . HOH   C 3 .   ? 18.46862  -16.03647 -13.52074 1.000 30.51733 ? 541 HOH   A O   1 
HETATM 1803 O O   . HOH   C 3 .   ? 21.957    -13.471   -19.464   1.000 46.64409 ? 542 HOH   A O   1 
HETATM 1804 O O   . HOH   C 3 .   ? 14.34651  -15.96937 -30.78355 1.000 29.54254 ? 543 HOH   A O   1 
HETATM 1805 O O   . HOH   C 3 .   ? -6.11501  -14.01755 0.80044   1.000 25.17844 ? 544 HOH   A O   1 
HETATM 1806 O O   . HOH   C 3 .   ? -1.76658  -25.66964 -4.77295  1.000 22.40248 ? 545 HOH   A O   1 
HETATM 1807 O O   . HOH   C 3 .   ? 2.23897   -29.80500 -34.28032 1.000 50.70178 ? 546 HOH   A O   1 
HETATM 1808 O O   . HOH   C 3 .   ? -4.65224  0.50233   -30.40962 1.000 25.04332 ? 547 HOH   A O   1 
HETATM 1809 O O   . HOH   C 3 .   ? -5.06868  -14.23890 -22.62618 1.000 16.63305 ? 548 HOH   A O   1 
HETATM 1810 O O   . HOH   C 3 .   ? 15.27715  -0.59077  -19.40037 1.000 40.50212 ? 549 HOH   A O   1 
HETATM 1811 O O   . HOH   C 3 .   ? 15.42451  -20.24762 -18.67238 1.000 22.31235 ? 550 HOH   A O   1 
HETATM 1812 O O   . HOH   C 3 .   ? 10.72090  -25.54576 -26.68238 1.000 29.34810 ? 551 HOH   A O   1 
HETATM 1813 O O   . HOH   C 3 .   ? -8.98663  -10.36828 -40.43487 1.000 40.01220 ? 552 HOH   A O   1 
HETATM 1814 O O   . HOH   C 3 .   ? 1.67982   -26.17542 -2.65196  1.000 42.93341 ? 553 HOH   A O   1 
HETATM 1815 O O   . HOH   C 3 .   ? -7.18322  -22.60816 -36.53911 1.000 45.27657 ? 554 HOH   A O   1 
HETATM 1816 O O   . HOH   C 3 .   ? -17.69493 -18.79092 -11.27831 1.000 31.14910 ? 555 HOH   A O   1 
HETATM 1817 O O   . HOH   C 3 .   ? -8.72430  -18.07191 -36.65231 1.000 40.98682 ? 556 HOH   A O   1 
HETATM 1818 O O   . HOH   C 3 .   ? -17.10773 -28.63041 -17.33609 1.000 38.96759 ? 557 HOH   A O   1 
HETATM 1819 O O   . HOH   C 3 .   ? -10.11969 -15.01371 -28.29587 1.000 27.06049 ? 558 HOH   A O   1 
HETATM 1820 O O   . HOH   C 3 .   ? -3.26186  -21.05579 -0.52957  1.000 31.80484 ? 559 HOH   A O   1 
HETATM 1821 O O   . HOH   C 3 .   ? -11.89913 -7.66040  -38.23557 1.000 35.90172 ? 560 HOH   A O   1 
HETATM 1822 O O   . HOH   C 3 .   ? -15.17423 -12.23190 -11.98690 1.000 28.36519 ? 561 HOH   A O   1 
HETATM 1823 O O   . HOH   C 3 .   ? -15.82411 6.31306   -32.20560 1.000 43.53772 ? 562 HOH   A O   1 
HETATM 1824 O O   . HOH   C 3 .   ? -3.36349  -3.20446  -40.65427 1.000 47.28436 ? 563 HOH   A O   1 
HETATM 1825 O O   . HOH   C 3 .   ? 13.71792  -20.45424 -20.74831 1.000 18.87267 ? 564 HOH   A O   1 
HETATM 1826 O O   . HOH   C 3 .   ? 3.29784   -4.80359  -28.80188 1.000 42.12093 ? 565 HOH   A O   1 
HETATM 1827 O O   . HOH   C 3 .   ? 12.51806  -27.29523 -19.67080 1.000 39.03495 ? 566 HOH   A O   1 
HETATM 1828 O O   . HOH   C 3 .   ? 6.79359   -29.71697 -30.14361 1.000 48.48299 ? 567 HOH   A O   1 
HETATM 1829 O O   . HOH   C 3 .   ? -5.84194  -18.82754 -39.01904 1.000 34.17369 ? 568 HOH   A O   1 
HETATM 1830 O O   . HOH   C 3 .   ? 4.02146   -9.16781  -20.28407 1.000 19.58642 ? 569 HOH   A O   1 
HETATM 1831 O O   . HOH   C 3 .   ? 3.78637   -11.65994 -38.45582 1.000 26.41101 ? 570 HOH   A O   1 
HETATM 1832 O O   . HOH   C 3 .   ? 1.05357   -6.02931  -34.24248 1.000 43.56593 ? 571 HOH   A O   1 
HETATM 1833 O O   . HOH   C 3 .   ? -6.59790  -3.54413  -7.94381  1.000 46.87628 ? 572 HOH   A O   1 
HETATM 1834 O O   . HOH   C 3 .   ? 10.91080  -11.55091 -4.83882  1.000 31.81138 ? 573 HOH   A O   1 
HETATM 1835 O O   . HOH   C 3 .   ? -3.08400  -1.06457  -23.99851 1.000 25.15702 ? 574 HOH   A O   1 
HETATM 1836 O O   . HOH   C 3 .   ? -19.958   -27.712   -10.414   1.000 54.76672 ? 575 HOH   A O   1 
HETATM 1837 O O   . HOH   C 3 .   ? 15.68375  -18.10620 -3.61031  1.000 29.04600 ? 576 HOH   A O   1 
HETATM 1838 O O   . HOH   C 3 .   ? -5.11228  -5.29286  -11.87752 1.000 33.77595 ? 577 HOH   A O   1 
HETATM 1839 O O   . HOH   C 3 .   ? 20.04749  -5.37946  -14.75031 1.000 45.47650 ? 578 HOH   A O   1 
HETATM 1840 O O   . HOH   C 3 .   ? -14.05693 -11.76003 0.30781   1.000 38.63747 ? 579 HOH   A O   1 
HETATM 1841 O O   . HOH   C 3 .   ? 20.83926  -14.16303 -26.70262 1.000 32.00289 ? 580 HOH   A O   1 
HETATM 1842 O O   . HOH   C 3 .   ? -17.65261 -15.17321 -13.06312 1.000 23.76851 ? 581 HOH   A O   1 
HETATM 1843 O O   . HOH   C 3 .   ? 2.00021   -6.11738  -25.86110 1.000 32.22006 ? 582 HOH   A O   1 
HETATM 1844 O O   . HOH   C 3 .   ? 19.73412  -16.43401 -27.80689 1.000 34.97962 ? 583 HOH   A O   1 
HETATM 1845 O O   . HOH   C 3 .   ? -1.08916  -29.91687 -17.37090 1.000 42.68458 ? 584 HOH   A O   1 
HETATM 1846 O O   . HOH   C 3 .   ? -16.55010 -9.17123  -14.28296 1.000 31.61874 ? 585 HOH   A O   1 
HETATM 1847 O O   . HOH   C 3 .   ? -2.42969  -15.63838 -0.26911  1.000 39.81080 ? 586 HOH   A O   1 
HETATM 1848 O O   . HOH   C 3 .   ? -14.50242 -3.58003  -12.73604 1.000 43.19707 ? 587 HOH   A O   1 
HETATM 1849 O O   . HOH   C 3 .   ? -3.37857  -13.12382 -20.67067 1.000 20.59139 ? 588 HOH   A O   1 
HETATM 1850 O O   . HOH   C 3 .   ? 8.77742   -20.44580 -4.34476  1.000 26.27961 ? 589 HOH   A O   1 
HETATM 1851 O O   . HOH   C 3 .   ? 4.40130   -19.45351 -40.59460 1.000 30.36079 ? 590 HOH   A O   1 
HETATM 1852 O O   . HOH   C 3 .   ? -16.89883 -20.28900 -4.86347  1.000 45.19745 ? 591 HOH   A O   1 
HETATM 1853 O O   . HOH   C 3 .   ? -1.50877  -8.51218  -27.82518 1.000 26.61503 ? 592 HOH   A O   1 
HETATM 1854 O O   . HOH   C 3 .   ? -14.32248 -22.00742 -33.68956 1.000 41.78290 ? 593 HOH   A O   1 
HETATM 1855 O O   . HOH   C 3 .   ? -18.01831 -5.80506  -25.45313 1.000 31.98025 ? 594 HOH   A O   1 
HETATM 1856 O O   . HOH   C 3 .   ? -12.34190 -31.98424 -19.16019 1.000 51.51688 ? 595 HOH   A O   1 
HETATM 1857 O O   . HOH   C 3 .   ? 1.71948   -3.96353  -16.97272 1.000 38.08948 ? 596 HOH   A O   1 
HETATM 1858 O O   . HOH   C 3 .   ? 13.31488  -6.71931  -26.16850 1.000 22.17823 ? 597 HOH   A O   1 
HETATM 1859 O O   . HOH   C 3 .   ? -0.03295  -16.71059 -3.47615  1.000 25.33889 ? 598 HOH   A O   1 
HETATM 1860 O O   . HOH   C 3 .   ? -5.577    -11.241   1.050     1.000 47.22520 ? 599 HOH   A O   1 
HETATM 1861 O O   . HOH   C 3 .   ? 15.50879  -7.17185  -27.80545 1.000 32.97144 ? 600 HOH   A O   1 
HETATM 1862 O O   . HOH   C 3 .   ? -7.58707  7.44375   -33.56829 1.000 32.72959 ? 601 HOH   A O   1 
HETATM 1863 O O   . HOH   C 3 .   ? -13.51272 -25.87352 -7.87463  1.000 27.67116 ? 602 HOH   A O   1 
HETATM 1864 O O   . HOH   C 3 .   ? -16.28896 -25.44613 -10.81431 1.000 33.70302 ? 603 HOH   A O   1 
HETATM 1865 O O   . HOH   C 3 .   ? 0.44451   -5.59347  -21.90376 1.000 34.48090 ? 604 HOH   A O   1 
HETATM 1866 O O   . HOH   C 3 .   ? -5.26191  -31.65414 -7.00191  1.000 45.49106 ? 605 HOH   A O   1 
HETATM 1867 O O   . HOH   C 3 .   ? -15.823   -3.833    -15.225   1.000 52.54822 ? 606 HOH   A O   1 
HETATM 1868 O O   . HOH   C 3 .   ? -13.02589 -12.20360 -31.01146 1.000 23.27612 ? 607 HOH   A O   1 
HETATM 1869 O O   . HOH   C 3 .   ? 8.05303   -30.00026 -37.45496 1.000 53.26496 ? 608 HOH   A O   1 
HETATM 1870 O O   . HOH   C 3 .   ? -2.08767  -8.80678  -43.45194 1.000 49.78367 ? 609 HOH   A O   1 
HETATM 1871 O O   . HOH   C 3 .   ? 8.49009   -19.82521 -41.57799 1.000 44.50389 ? 610 HOH   A O   1 
HETATM 1872 O O   . HOH   C 3 .   ? 3.99866   -22.98921 -3.48297  1.000 34.58904 ? 611 HOH   A O   1 
HETATM 1873 O O   . HOH   C 3 .   ? 13.74533  -4.00428  -25.30865 1.000 18.95647 ? 612 HOH   A O   1 
HETATM 1874 O O   . HOH   C 3 .   ? 1.18077   -8.62889  -26.85643 1.000 32.06513 ? 613 HOH   A O   1 
HETATM 1875 O O   . HOH   C 3 .   ? 3.14203   -4.22357  -8.68862  1.000 47.52099 ? 614 HOH   A O   1 
HETATM 1876 O O   . HOH   C 3 .   ? -0.41813  -12.46477 -21.32418 1.000 30.26652 ? 615 HOH   A O   1 
HETATM 1877 O O   . HOH   C 3 .   ? 5.60402   -3.33593  -26.10603 1.000 34.91037 ? 616 HOH   A O   1 
HETATM 1878 O O   . HOH   C 3 .   ? -12.779   -26.924   -35.442   1.000 43.74701 ? 617 HOH   A O   1 
HETATM 1879 O O   . HOH   C 3 .   ? 10.52731  -17.61005 -38.78862 1.000 44.81804 ? 618 HOH   A O   1 
HETATM 1880 O O   . HOH   C 3 .   ? 9.90358   -6.04543  -1.23780  1.000 49.02744 ? 619 HOH   A O   1 
HETATM 1881 O O   . HOH   C 3 .   ? -0.97232  -27.33030 -34.80516 1.000 53.58951 ? 620 HOH   A O   1 
HETATM 1882 O O   . HOH   C 3 .   ? -12.21969 -26.92124 -20.38643 1.000 25.15619 ? 621 HOH   A O   1 
HETATM 1883 O O   . HOH   C 3 .   ? -9.55262  -13.50963 -39.93049 1.000 55.91282 ? 622 HOH   A O   1 
HETATM 1884 O O   . HOH   C 3 .   ? -13.99364 -24.08348 -4.87401  1.000 31.00911 ? 623 HOH   A O   1 
HETATM 1885 O O   . HOH   C 3 .   ? -18.36505 -3.32374  -35.54395 1.000 42.75652 ? 624 HOH   A O   1 
HETATM 1886 O O   . HOH   C 3 .   ? -18.22251 -33.87992 -10.91306 1.000 52.61779 ? 625 HOH   A O   1 
HETATM 1887 O O   . HOH   C 3 .   ? -17.72916 -16.14712 -23.62706 1.000 33.78393 ? 626 HOH   A O   1 
HETATM 1888 O O   . HOH   C 3 .   ? -14.48041 -29.53034 -9.54128  1.000 45.20330 ? 627 HOH   A O   1 
HETATM 1889 O O   . HOH   C 3 .   ? -0.22854  -30.01555 -24.20265 1.000 52.03871 ? 628 HOH   A O   1 
HETATM 1890 O O   . HOH   C 3 .   ? -5.58454  -12.12302 -41.89433 1.000 43.58098 ? 629 HOH   A O   1 
HETATM 1891 O O   . HOH   C 3 .   ? 11.39114  -1.79107  -20.26388 1.000 31.32757 ? 630 HOH   A O   1 
HETATM 1892 O O   . HOH   C 3 .   ? -15.60494 -14.44829 -33.35178 1.000 43.63377 ? 631 HOH   A O   1 
HETATM 1893 O O   . HOH   C 3 .   ? 17.70179  -15.31843 -29.62071 1.000 42.61060 ? 632 HOH   A O   1 
HETATM 1894 O O   . HOH   C 3 .   ? 1.80824   -18.36167 0.05809   1.000 33.18730 ? 633 HOH   A O   1 
HETATM 1895 O O   . HOH   C 3 .   ? 2.78389   -10.08162 -23.10430 1.000 26.89745 ? 634 HOH   A O   1 
HETATM 1896 O O   . HOH   C 3 .   ? 14.43165  -22.52736 -17.24392 1.000 33.41802 ? 635 HOH   A O   1 
HETATM 1897 O O   . HOH   C 3 .   ? 3.18404   -6.72883  -20.55097 1.000 34.52910 ? 636 HOH   A O   1 
HETATM 1898 O O   . HOH   C 3 .   ? -3.85260  -33.14505 -11.26410 1.000 48.47262 ? 637 HOH   A O   1 
HETATM 1899 O O   . HOH   C 3 .   ? -22.033   -34.515   -13.816   1.000 48.08814 ? 638 HOH   A O   1 
HETATM 1900 O O   . HOH   C 3 .   ? 13.07438  -22.53961 -4.65710  1.000 46.99730 ? 639 HOH   A O   1 
HETATM 1901 O O   . HOH   C 3 .   ? 1.11703   -8.48359  -4.25972  1.000 35.36172 ? 640 HOH   A O   1 
HETATM 1902 O O   . HOH   C 3 .   ? 8.22004   -25.84177 -25.82334 1.000 34.57271 ? 641 HOH   A O   1 
HETATM 1903 O O   . HOH   C 3 .   ? 16.08609  0.29069   -9.74678  1.000 50.88006 ? 642 HOH   A O   1 
HETATM 1904 O O   . HOH   C 3 .   ? -1.91266  -26.93559 -25.12743 1.000 38.75026 ? 643 HOH   A O   1 
HETATM 1905 O O   . HOH   C 3 .   ? 4.68780   -1.91438  -18.28890 1.000 30.58531 ? 644 HOH   A O   1 
HETATM 1906 O O   . HOH   C 3 .   ? 4.38131   -21.71579 -39.42693 1.000 52.25425 ? 645 HOH   A O   1 
HETATM 1907 O O   . HOH   C 3 .   ? 2.02026   -25.85515 -29.27118 1.000 35.32629 ? 646 HOH   A O   1 
HETATM 1908 O O   . HOH   C 3 .   ? -1.03657  -5.99308  -12.58973 1.000 43.22509 ? 647 HOH   A O   1 
HETATM 1909 O O   . HOH   C 3 .   ? -13.592   -24.081   -27.903   1.000 38.00927 ? 648 HOH   A O   1 
HETATM 1910 O O   . HOH   C 3 .   ? 17.54441  -21.50348 -19.85576 1.000 33.51492 ? 649 HOH   A O   1 
HETATM 1911 O O   . HOH   C 3 .   ? 7.08694   1.98262   -12.47546 1.000 39.79804 ? 650 HOH   A O   1 
HETATM 1912 O O   . HOH   C 3 .   ? -8.50713  -3.36266  -1.93032  1.000 52.47649 ? 651 HOH   A O   1 
HETATM 1913 O O   . HOH   C 3 .   ? -0.02324  -19.06559 -1.96593  1.000 36.79210 ? 652 HOH   A O   1 
HETATM 1914 O O   . HOH   C 3 .   ? -13.91811 -14.29114 -3.05617  1.000 29.31332 ? 653 HOH   A O   1 
HETATM 1915 O O   . HOH   C 3 .   ? -9.09655  -5.68993  -39.65419 1.000 42.06579 ? 654 HOH   A O   1 
HETATM 1916 O O   . HOH   C 3 .   ? -0.44441  -1.28453  -22.85493 1.000 34.43253 ? 655 HOH   A O   1 
HETATM 1917 O O   . HOH   C 3 .   ? 12.10396  -27.55056 -23.33019 1.000 44.40473 ? 656 HOH   A O   1 
HETATM 1918 O O   . HOH   C 3 .   ? 3.38175   -8.00188  -2.09921  1.000 46.43911 ? 657 HOH   A O   1 
HETATM 1919 O O   . HOH   C 3 .   ? 12.216    -25.224   -38.471   1.000 29.76806 ? 658 HOH   A O   1 
HETATM 1920 O O   . HOH   C 3 .   ? 18.00956  -17.79184 -11.08934 1.000 39.78001 ? 659 HOH   A O   1 
HETATM 1921 O O   . HOH   C 3 .   ? -14.27413 -9.86090  -8.38131  1.000 34.93297 ? 660 HOH   A O   1 
HETATM 1922 O O   . HOH   C 3 .   ? -13.76656 -26.64576 -1.41089  1.000 52.33300 ? 661 HOH   A O   1 
HETATM 1923 O O   . HOH   C 3 .   ? -6.25368  3.80293   -34.61687 1.000 41.72100 ? 662 HOH   A O   1 
HETATM 1924 O O   . HOH   C 3 .   ? 1.72157   -2.97909  -12.83053 1.000 42.09635 ? 663 HOH   A O   1 
HETATM 1925 O O   . HOH   C 3 .   ? 15.26844  -12.48852 -7.11210  1.000 45.50098 ? 664 HOH   A O   1 
HETATM 1926 O O   . HOH   C 3 .   ? -0.72926  -29.26593 -3.42095  1.000 53.81314 ? 665 HOH   A O   1 
HETATM 1927 O O   . HOH   C 3 .   ? -13.976   -0.742    -13.647   1.000 34.59576 ? 666 HOH   A O   1 
HETATM 1928 O O   . HOH   C 3 .   ? 3.60889   -9.07356  -38.91712 1.000 42.05290 ? 667 HOH   A O   1 
HETATM 1929 O O   . HOH   C 3 .   ? 5.542     1.664     -16.636   1.000 31.23857 ? 668 HOH   A O   1 
HETATM 1930 O O   . HOH   C 3 .   ? -11.47609 -9.53358  -39.58755 1.000 45.93046 ? 669 HOH   A O   1 
HETATM 1931 O O   . HOH   C 3 .   ? 16.07995  1.48635   -15.41432 1.000 49.89783 ? 670 HOH   A O   1 
HETATM 1932 O O   . HOH   C 3 .   ? 7.78665   -13.82768 -38.10911 1.000 33.50522 ? 671 HOH   A O   1 
HETATM 1933 O O   . HOH   C 3 .   ? -14.48806 -29.04753 -17.30331 1.000 45.95178 ? 672 HOH   A O   1 
HETATM 1934 O O   . HOH   C 3 .   ? 3.70063   -0.34913  -16.50833 1.000 36.71901 ? 673 HOH   A O   1 
HETATM 1935 O O   . HOH   C 3 .   ? 19.04929  -8.51885  -17.71304 1.000 41.08306 ? 674 HOH   A O   1 
HETATM 1936 O O   . HOH   C 3 .   ? 14.932    -7.937    -30.121   1.000 35.96506 ? 675 HOH   A O   1 
HETATM 1937 O O   . HOH   C 3 .   ? 11.09401  -1.44269  -17.31649 1.000 29.20520 ? 676 HOH   A O   1 
HETATM 1938 O O   . HOH   C 3 .   ? 1.45875   -7.57847  -23.03680 1.000 41.93463 ? 677 HOH   A O   1 
HETATM 1939 O O   . HOH   C 3 .   ? 2.189     -0.904    -25.893   1.000 34.48625 ? 678 HOH   A O   1 
HETATM 1940 O O   . HOH   C 3 .   ? 6.71463   -21.36521 -2.64480  1.000 32.51243 ? 679 HOH   A O   1 
HETATM 1941 O O   . HOH   C 3 .   ? 6.24940   -29.87773 -24.95458 1.000 44.23875 ? 680 HOH   A O   1 
HETATM 1942 O O   . HOH   C 3 .   ? 2.35719   -0.84854  -14.36110 1.000 41.63833 ? 681 HOH   A O   1 
HETATM 1943 O O   . HOH   C 3 .   ? -9.74565  -26.02767 -20.91854 1.000 26.57699 ? 682 HOH   A O   1 
HETATM 1944 O O   . HOH   C 3 .   ? -10.48188 -8.80418  -1.50159  1.000 36.76165 ? 683 HOH   A O   1 
HETATM 1945 O O   . HOH   C 3 .   ? -3.37122  -27.14242 -3.08822  1.000 43.15007 ? 684 HOH   A O   1 
HETATM 1946 O O   . HOH   C 3 .   ? -18.68417 -11.72797 -21.15509 1.000 29.43534 ? 685 HOH   A O   1 
HETATM 1947 O O   . HOH   C 3 .   ? -2.29355  -1.02862  -30.79230 1.000 42.64620 ? 686 HOH   A O   1 
HETATM 1948 O O   . HOH   C 3 .   ? -16.889   -0.634    -17.590   1.000 41.29899 ? 687 HOH   A O   1 
HETATM 1949 O O   . HOH   C 3 .   ? -0.28130  -10.61009 -23.68494 1.000 45.11472 ? 688 HOH   A O   1 
HETATM 1950 O O   . HOH   C 3 .   ? 2.93098   -4.76860  -19.93487 1.000 41.05217 ? 689 HOH   A O   1 
HETATM 1951 O O   . HOH   C 3 .   ? -16.60181 -18.79146 -3.18509  1.000 47.35508 ? 690 HOH   A O   1 
HETATM 1952 O O   . HOH   C 3 .   ? 1.11275   -11.77358 -23.60049 1.000 36.92970 ? 691 HOH   A O   1 
HETATM 1953 O O   . HOH   C 3 .   ? -2.13021  -11.79708 -22.60039 1.000 41.07200 ? 692 HOH   A O   1 
HETATM 1954 O O   . HOH   C 3 .   ? 7.93564   -28.85997 -28.23586 1.000 41.97433 ? 693 HOH   A O   1 
HETATM 1955 O O   . HOH   C 3 .   ? 5.76650   -12.91716 -39.83283 1.000 30.38329 ? 694 HOH   A O   1 
HETATM 1956 O O   . HOH   C 3 .   ? 10.46629  -21.17950 -43.15126 1.000 51.20687 ? 695 HOH   A O   1 
HETATM 1957 O O   . HOH   C 3 .   ? 5.47598   -3.26426  -23.46886 1.000 39.39075 ? 696 HOH   A O   1 
HETATM 1958 O O   . HOH   C 3 .   ? 8.374     -8.208    0.208     1.000 51.55685 ? 697 HOH   A O   1 
HETATM 1959 O O   . HOH   C 3 .   ? -10.01531 -29.06198 -30.89601 1.000 44.61830 ? 698 HOH   A O   1 
HETATM 1960 O O   . HOH   C 3 .   ? -6.685    -23.025   -1.916    1.000 39.33803 ? 699 HOH   A O   1 
HETATM 1961 O O   . HOH   C 3 .   ? -6.98665  -30.73830 -9.14788  1.000 34.18860 ? 700 HOH   A O   1 
HETATM 1962 O O   . HOH   C 3 .   ? 10.54959  -22.48632 -4.45693  1.000 41.38029 ? 701 HOH   A O   1 
HETATM 1963 O O   . HOH   C 3 .   ? 0.71236   -16.47325 -43.54150 1.000 52.32659 ? 702 HOH   A O   1 
HETATM 1964 O O   . HOH   C 3 .   ? -7.944    7.803     -38.441   1.000 48.13490 ? 703 HOH   A O   1 
HETATM 1965 O O   . HOH   C 3 .   ? 12.23708  -9.93516  -1.51123  1.000 50.22547 ? 704 HOH   A O   1 
HETATM 1966 O O   . HOH   C 3 .   ? -0.00000  -0.00000  -18.39252 0.50  19.99214 ? 705 HOH   A O   1 
HETATM 1967 O O   . HOH   C 3 .   ? -4.91778  -25.14729 -1.12245  1.000 49.06401 ? 706 HOH   A O   1 
HETATM 1968 O O   . HOH   C 3 .   ? 2.23853   -31.93882 -26.81188 1.000 54.75822 ? 707 HOH   A O   1 
HETATM 1969 O O   . HOH   C 3 .   ? 20.30223  -5.86109  -21.11082 1.000 37.33137 ? 708 HOH   A O   1 
HETATM 1970 O O   . HOH   C 3 .   ? -1.00240  -2.48927  -31.62830 1.000 43.84432 ? 709 HOH   A O   1 
HETATM 1971 O O   . HOH   C 3 .   ? 10.91914  -27.99087 -27.84343 1.000 36.13787 ? 710 HOH   A O   1 
HETATM 1972 O O   . HOH   C 3 .   ? -18.739   -16.319   -26.475   1.000 48.05710 ? 711 HOH   A O   1 
HETATM 1973 O O   . HOH   C 3 .   ? -12.09680 -26.34855 -27.88753 1.000 44.25432 ? 712 HOH   A O   1 
HETATM 1974 O O   . HOH   C 3 .   ? 4.81955   -14.74021 -41.45701 1.000 44.34402 ? 713 HOH   A O   1 
HETATM 1975 O O   . HOH   C 3 .   ? -17.13128 4.28494   -31.37800 1.000 46.32088 ? 714 HOH   A O   1 
HETATM 1976 O O   . HOH   C 3 .   ? -21.52187 -14.64141 -15.82334 1.000 36.09084 ? 715 HOH   A O   1 
HETATM 1977 O O   . HOH   C 3 .   ? 1.79678   -5.86087  -36.64463 1.000 45.45373 ? 716 HOH   A O   1 
HETATM 1978 O O   . HOH   C 3 .   ? -16.261   3.108     -26.375   1.000 37.12880 ? 717 HOH   A O   1 
HETATM 1979 O O   . HOH   C 3 .   ? -16.31809 -12.77759 -6.14420  1.000 42.92719 ? 718 HOH   A O   1 
HETATM 1980 O O   . HOH   C 3 .   ? 3.02839   -2.10812  -20.42376 1.000 37.21801 ? 719 HOH   A O   1 
HETATM 1981 O O   . HOH   C 3 .   ? -0.51058  -26.54711 -29.86813 1.000 44.31756 ? 720 HOH   A O   1 
HETATM 1982 O O   . HOH   C 3 .   ? 4.128     -1.950    -27.991   1.000 36.59100 ? 721 HOH   A O   1 
HETATM 1983 O O   . HOH   C 3 .   ? -17.87918 -15.79561 -3.38305  1.000 50.67864 ? 722 HOH   A O   1 
HETATM 1984 O O   . HOH   C 3 .   ? 9.71681   -25.06711 -14.79230 1.000 41.72969 ? 723 HOH   A O   1 
HETATM 1985 O O   . HOH   C 3 .   ? 21.828    -17.918   -25.104   1.000 44.42420 ? 724 HOH   A O   1 
HETATM 1986 O O   . HOH   C 3 .   ? -6.57185  -25.72844 0.98961   1.000 50.19732 ? 725 HOH   A O   1 
HETATM 1987 O O   . HOH   C 3 .   ? -16.24318 -13.49299 -3.73709  1.000 43.39047 ? 726 HOH   A O   1 
HETATM 1988 O O   . HOH   C 3 .   ? 14.49681  -13.12972 -2.85829  1.000 38.95665 ? 727 HOH   A O   1 
HETATM 1989 O O   . HOH   C 3 .   ? -8.90927  -28.47730 -24.89858 1.000 40.99249 ? 728 HOH   A O   1 
HETATM 1990 O O   . HOH   C 3 .   ? 0.49921   -1.26846  -16.69098 1.000 34.03412 ? 729 HOH   A O   1 
HETATM 1991 O O   . HOH   C 3 .   ? -20.53376 -10.51324 -16.62725 1.000 49.29933 ? 730 HOH   A O   1 
HETATM 1992 O O   . HOH   C 3 .   ? -18.94705 -8.27290  -15.14487 1.000 44.60065 ? 731 HOH   A O   1 
HETATM 1993 O O   . HOH   C 3 .   ? -10.389   -11.889   2.000     1.000 30.56246 ? 732 HOH   A O   1 
HETATM 1994 O O   . HOH   C 3 .   ? 14.854    -17.249   0.392     1.000 44.53189 ? 733 HOH   A O   1 
HETATM 1995 O O   . HOH   C 3 .   ? 20.60528  -7.56675  -15.79960 1.000 47.32844 ? 734 HOH   A O   1 
HETATM 1996 O O   . HOH   C 3 .   ? -16.86271 -15.66062 -10.34162 1.000 32.99379 ? 735 HOH   A O   1 
HETATM 1997 O O   . HOH   C 3 .   ? 13.60929  -11.67333 -5.05077  1.000 35.52686 ? 736 HOH   A O   1 
HETATM 1998 O O   . HOH   C 3 .   ? -14.51704 -14.13253 -10.23501 1.000 26.40541 ? 737 HOH   A O   1 
HETATM 1999 O O   . HOH   C 3 .   ? -12.28398 -13.11820 -0.96088  1.000 27.12367 ? 738 HOH   A O   1 
HETATM 2000 O O   . HOH   C 3 .   ? 9.58944   -12.63930 -37.19161 1.000 45.09835 ? 739 HOH   A O   1 
HETATM 2001 O O   . HOH   C 3 .   ? -14.74511 -9.56678  -11.30812 1.000 35.36183 ? 740 HOH   A O   1 
HETATM 2002 O O   . HOH   C 3 .   ? 17.34933  -4.81860  -28.13527 1.000 40.94297 ? 741 HOH   A O   1 
HETATM 2003 O O   . HOH   C 3 .   ? -18.63536 -2.12132  -30.45455 1.000 50.59270 ? 742 HOH   A O   1 
HETATM 2004 O O   . HOH   C 3 .   ? 9.94062   -0.88112  -3.75067  1.000 49.95749 ? 743 HOH   A O   1 
HETATM 2005 O O   . HOH   C 3 .   ? -19.58232 -5.72222  -21.49901 1.000 42.46829 ? 744 HOH   A O   1 
HETATM 2006 O O   . HOH   C 3 .   ? -2.86581  -26.42022 -27.56071 1.000 46.48908 ? 745 HOH   A O   1 
HETATM 2007 O O   . HOH   C 3 .   ? -9.484    9.122     -38.303   1.000 43.69356 ? 746 HOH   A O   1 
HETATM 2008 O O   . HOH   C 3 .   ? -9.00732  -32.81104 -8.83535  1.000 44.14584 ? 747 HOH   A O   1 
HETATM 2009 O O   . HOH   C 3 .   ? -9.93558  -20.66505 -39.69196 1.000 53.24051 ? 748 HOH   A O   1 
HETATM 2010 O O   . HOH   C 3 .   ? -7.96215  -29.52327 -26.76312 1.000 49.46178 ? 749 HOH   A O   1 
HETATM 2011 O O   . HOH   C 3 .   ? 6.14762   -8.32623  -40.16653 1.000 52.13123 ? 750 HOH   A O   1 
HETATM 2012 O O   . HOH   C 3 .   ? -23.03599 -10.40928 -15.69085 1.000 45.88058 ? 751 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   ? 0.46307 0.77084 0.43971 -0.10161 0.00607  -0.24918 16  GLU A N   
2    C CA  . GLU A 9   ? 0.55670 0.83177 0.52239 -0.06867 -0.00377 -0.22920 16  GLU A CA  
3    C C   . GLU A 9   ? 0.49849 0.75624 0.47143 -0.05050 -0.01062 -0.20789 16  GLU A C   
4    O O   . GLU A 9   ? 0.46696 0.77859 0.45612 -0.03531 -0.01901 -0.19899 16  GLU A O   
5    C CB  . GLU A 9   ? 0.58903 0.92885 0.55976 -0.04246 -0.01484 -0.22593 16  GLU A CB  
6    C CG  . GLU A 9   ? 0.83290 1.13263 0.78423 -0.02152 -0.01675 -0.21695 16  GLU A CG  
7    C CD  . GLU A 9   ? 0.91757 1.18975 0.86707 0.01065  -0.02325 -0.19091 16  GLU A CD  
8    O OE1 . GLU A 9   ? 0.85647 1.13635 0.81797 0.01649  -0.02707 -0.17989 16  GLU A OE1 
9    O OE2 . GLU A 9   ? 0.93883 1.18106 0.87436 0.02992  -0.02285 -0.18169 16  GLU A OE2 
10   N N   . VAL A 10  ? 0.36946 0.55252 0.32915 -0.04997 -0.00491 -0.19961 17  VAL A N   
11   C CA  . VAL A 10  ? 0.29963 0.46098 0.26583 -0.03883 -0.00881 -0.18339 17  VAL A CA  
12   C C   . VAL A 10  ? 0.30872 0.44114 0.26687 -0.00851 -0.01349 -0.16726 17  VAL A C   
13   O O   . VAL A 10  ? 0.35594 0.44264 0.29874 -0.00572 -0.00533 -0.16848 17  VAL A O   
14   C CB  . VAL A 10  ? 0.41369 0.51668 0.37412 -0.06293 0.00552  -0.18704 17  VAL A CB  
15   C CG1 . VAL A 10  ? 0.41787 0.50766 0.38759 -0.05246 0.00064  -0.17186 17  VAL A CG1 
16   C CG2 . VAL A 10  ? 0.51888 0.64703 0.48516 -0.09458 0.01501  -0.20485 17  VAL A CG2 
17   N N   . GLU A 11  ? 0.23973 0.39599 0.20782 0.01574  -0.02360 -0.14972 18  GLU A N   
18   C CA  . GLU A 11  ? 0.23035 0.35349 0.19932 0.04203  -0.02367 -0.12311 18  GLU A CA  
19   C C   . GLU A 11  ? 0.21154 0.29609 0.19000 0.03948  -0.02106 -0.10738 18  GLU A C   
20   O O   . GLU A 11  ? 0.19945 0.30114 0.18759 0.03337  -0.02428 -0.10640 18  GLU A O   
21   C CB  . GLU A 11  ? 0.23938 0.40378 0.21016 0.07042  -0.03008 -0.10911 18  GLU A CB  
22   C CG  . GLU A 11  ? 0.25636 0.46150 0.21505 0.08155  -0.03258 -0.11968 18  GLU A CG  
23   C CD  . GLU A 11  ? 0.34493 0.58979 0.30059 0.11472  -0.03490 -0.10254 18  GLU A CD  
24   O OE1 . GLU A 11  ? 0.35794 0.64341 0.32358 0.11889  -0.03729 -0.09943 18  GLU A OE1 
25   O OE2 . GLU A 11  ? 0.40875 0.63870 0.35544 0.13669  -0.03059 -0.08834 18  GLU A OE2 
26   N N   . THR A 12  ? 0.22596 0.26475 0.20104 0.04567  -0.01521 -0.09529 19  THR A N   
27   C CA  . THR A 12  ? 0.20595 0.21603 0.18835 0.04586  -0.01295 -0.08067 19  THR A CA  
28   C C   . THR A 12  ? 0.21621 0.22789 0.20624 0.06483  -0.01532 -0.06171 19  THR A C   
29   O O   . THR A 12  ? 0.20495 0.21244 0.19028 0.07701  -0.01312 -0.05717 19  THR A O   
30   C CB  . THR A 12  ? 0.23306 0.19670 0.20315 0.04009  -0.00164 -0.08148 19  THR A CB  
31   O OG1 . THR A 12  ? 0.26719 0.22005 0.22580 0.01781  0.00655  -0.10214 19  THR A OG1 
32   C CG2 . THR A 12  ? 0.25543 0.20097 0.23172 0.04376  -0.00001 -0.06592 19  THR A CG2 
33   N N   . PHE A 13  ? 0.18797 0.20483 0.18851 0.06496  -0.01766 -0.05250 20  PHE A N   
34   C CA  . PHE A 13  ? 0.18158 0.19865 0.18809 0.07580  -0.01594 -0.03885 20  PHE A CA  
35   C C   . PHE A 13  ? 0.22201 0.22699 0.23645 0.06951  -0.01509 -0.03206 20  PHE A C   
36   O O   . PHE A 13  ? 0.20647 0.20672 0.22233 0.06003  -0.01680 -0.03485 20  PHE A O   
37   C CB  . PHE A 13  ? 0.18166 0.21701 0.18876 0.08206  -0.01570 -0.03557 20  PHE A CB  
38   C CG  . PHE A 13  ? 0.20929 0.27026 0.20725 0.09416  -0.01676 -0.03996 20  PHE A CG  
39   C CD1 . PHE A 13  ? 0.20429 0.29342 0.20097 0.08688  -0.02294 -0.05378 20  PHE A CD1 
40   C CD2 . PHE A 13  ? 0.23361 0.29371 0.22235 0.10954  -0.01009 -0.03020 20  PHE A CD2 
41   C CE1 . PHE A 13  ? 0.21845 0.34575 0.20673 0.09933  -0.02508 -0.05934 20  PHE A CE1 
42   C CE2 . PHE A 13  ? 0.25555 0.34211 0.23132 0.12125  -0.01103 -0.03139 20  PHE A CE2 
43   C CZ  . PHE A 13  ? 0.22904 0.35858 0.20737 0.12295  -0.01963 -0.04782 20  PHE A CZ  
44   N N   . ALA A 14  ? 0.19249 0.19744 0.21179 0.07410  -0.01151 -0.02409 21  ALA A N   
45   C CA  . ALA A 14  ? 0.16830 0.17673 0.19602 0.06775  -0.01124 -0.01976 21  ALA A CA  
46   C C   . ALA A 14  ? 0.18048 0.19224 0.21174 0.06116  -0.00846 -0.01970 21  ALA A C   
47   O O   . ALA A 14  ? 0.21112 0.21948 0.23802 0.06575  -0.00148 -0.01814 21  ALA A O   
48   C CB  . ALA A 14  ? 0.19916 0.21753 0.23156 0.07227  -0.00752 -0.01486 21  ALA A CB  
49   N N   . PHE A 15  ? 0.18018 0.19443 0.21556 0.05245  -0.01115 -0.02047 22  PHE A N   
50   C CA  . PHE A 15  ? 0.18530 0.19889 0.22176 0.04496  -0.00546 -0.02116 22  PHE A CA  
51   C C   . PHE A 15  ? 0.19046 0.20909 0.23057 0.03859  0.00339  -0.02205 22  PHE A C   
52   O O   . PHE A 15  ? 0.20247 0.23873 0.24959 0.03789  0.00071  -0.02184 22  PHE A O   
53   C CB  . PHE A 15  ? 0.16941 0.18815 0.20951 0.03618  -0.01000 -0.02263 22  PHE A CB  
54   C CG  . PHE A 15  ? 0.15476 0.16923 0.19188 0.03725  -0.01497 -0.02356 22  PHE A CG  
55   C CD1 . PHE A 15  ? 0.18678 0.19988 0.21916 0.04058  -0.01195 -0.02407 22  PHE A CD1 
56   C CD2 . PHE A 15  ? 0.16812 0.18102 0.20520 0.03568  -0.01973 -0.02358 22  PHE A CD2 
57   C CE1 . PHE A 15  ? 0.19338 0.21439 0.22558 0.03973  -0.01658 -0.02678 22  PHE A CE1 
58   C CE2 . PHE A 15  ? 0.18095 0.19144 0.21599 0.03144  -0.02145 -0.02719 22  PHE A CE2 
59   C CZ  . PHE A 15  ? 0.18037 0.20035 0.21532 0.03200  -0.02134 -0.02990 22  PHE A CZ  
60   N N   . GLN A 16  ? 0.18483 0.18836 0.21814 0.03416  0.01678  -0.02330 23  GLN A N   
61   C CA  . GLN A 16  ? 0.19157 0.19850 0.22776 0.01829  0.02929  -0.02931 23  GLN A CA  
62   C C   . GLN A 16  ? 0.20243 0.23801 0.24961 0.00401  0.02152  -0.03608 23  GLN A C   
63   O O   . GLN A 16  ? 0.18080 0.21784 0.22774 0.00499  0.01292  -0.03532 23  GLN A O   
64   C CB  . GLN A 16  ? 0.28081 0.25444 0.30142 0.01344  0.05022  -0.03071 23  GLN A CB  
65   C CG  . GLN A 16  ? 0.31445 0.26233 0.31969 0.03198  0.06260  -0.02167 23  GLN A CG  
66   C CD  . GLN A 16  ? 0.50077 0.40827 0.48327 0.03458  0.08739  -0.01898 23  GLN A CD  
67   O OE1 . GLN A 16  ? 0.47057 0.36923 0.44175 0.05119  0.08671  -0.01200 23  GLN A OE1 
68   N NE2 . GLN A 16  ? 0.48069 0.36310 0.45428 0.01818  0.11233  -0.02486 23  GLN A NE2 
69   N N   . ALA A 17  ? 0.22506 0.28986 0.28176 -0.00843 0.02495  -0.04286 24  ALA A N   
70   C CA  . ALA A 17  ? 0.20897 0.31712 0.27604 -0.01716 0.01602  -0.04863 24  ALA A CA  
71   C C   . ALA A 17  ? 0.18309 0.28456 0.24532 -0.03160 0.01889  -0.05659 24  ALA A C   
72   O O   . ALA A 17  ? 0.20480 0.32668 0.26956 -0.02756 0.00716  -0.05479 24  ALA A O   
73   C CB  . ALA A 17  ? 0.21821 0.36986 0.29664 -0.03160 0.02202  -0.05820 24  ALA A CB  
74   N N   . GLU A 18  ? 0.22527 0.29307 0.27677 -0.04615 0.03717  -0.06416 25  GLU A N   
75   C CA  . GLU A 18  ? 0.22673 0.28276 0.26996 -0.06033 0.04359  -0.07288 25  GLU A CA  
76   C C   . GLU A 18  ? 0.21818 0.25662 0.25612 -0.04214 0.03207  -0.06158 25  GLU A C   
77   O O   . GLU A 18  ? 0.22807 0.27647 0.26516 -0.04835 0.02757  -0.06579 25  GLU A O   
78   C CB  . GLU A 18  ? 0.30975 0.31994 0.33556 -0.07609 0.07202  -0.08136 25  GLU A CB  
79   C CG  . GLU A 18  ? 0.37046 0.39609 0.40040 -0.10300 0.08902  -0.09743 25  GLU A CG  
80   C CD  . GLU A 18  ? 0.44598 0.46522 0.47886 -0.09141 0.09318  -0.08846 25  GLU A CD  
81   O OE1 . GLU A 18  ? 0.34679 0.35239 0.37829 -0.06225 0.08144  -0.07076 25  GLU A OE1 
82   O OE2 . GLU A 18  ? 0.50907 0.53908 0.54519 -0.11370 0.10960  -0.10101 25  GLU A OE2 
83   N N   . ILE A 19  ? 0.22250 0.24029 0.25712 -0.02120 0.02761  -0.04887 26  ILE A N   
84   C CA  . ILE A 19  ? 0.20112 0.20986 0.23248 -0.00781 0.01813  -0.04106 26  ILE A CA  
85   C C   . ILE A 19  ? 0.18582 0.22146 0.22746 -0.00315 0.00086  -0.03759 26  ILE A C   
86   O O   . ILE A 19  ? 0.19270 0.22994 0.23322 -0.00254 -0.00467 -0.03613 26  ILE A O   
87   C CB  . ILE A 19  ? 0.21481 0.20308 0.23843 0.01060  0.02046  -0.03218 26  ILE A CB  
88   C CG1 . ILE A 19  ? 0.27360 0.22900 0.27877 0.01468  0.04105  -0.03061 26  ILE A CG1 
89   C CG2 . ILE A 19  ? 0.21678 0.21276 0.24281 0.02066  0.00753  -0.02742 26  ILE A CG2 
90   C CD1 . ILE A 19  ? 0.35059 0.28532 0.34740 -0.00023 0.06248  -0.03778 26  ILE A CD1 
91   N N   . ALA A 20  ? 0.16745 0.22138 0.21618 0.00228  -0.00496 -0.03489 27  ALA A N   
92   C CA  . ALA A 20  ? 0.16764 0.24168 0.21964 0.01046  -0.01532 -0.02947 27  ALA A CA  
93   C C   . ALA A 20  ? 0.18128 0.28431 0.23530 0.00158  -0.01720 -0.03439 27  ALA A C   
94   O O   . ALA A 20  ? 0.17453 0.28165 0.22513 0.00845  -0.02258 -0.02891 27  ALA A O   
95   C CB  . ALA A 20  ? 0.18537 0.27429 0.24077 0.02119  -0.01734 -0.02473 27  ALA A CB  
96   N N   . GLN A 21  ? 0.17914 0.30260 0.23697 -0.01541 -0.01073 -0.04623 28  GLN A N   
97   C CA  . GLN A 21  ? 0.18442 0.34379 0.24364 -0.02760 -0.01213 -0.05551 28  GLN A CA  
98   C C   . GLN A 21  ? 0.20510 0.33934 0.25560 -0.03217 -0.01050 -0.05690 28  GLN A C   
99   O O   . GLN A 21  ? 0.19930 0.35564 0.24812 -0.02913 -0.01705 -0.05559 28  GLN A O   
100  C CB  . GLN A 21  ? 0.18132 0.36564 0.24543 -0.05218 -0.00163 -0.07334 28  GLN A CB  
101  C CG  . GLN A 21  ? 0.32384 0.56396 0.39142 -0.06827 -0.00371 -0.08792 28  GLN A CG  
102  C CD  . GLN A 21  ? 0.60192 0.84903 0.66606 -0.09598 0.01305  -0.10712 28  GLN A CD  
103  O OE1 . GLN A 21  ? 0.56174 0.83608 0.61813 -0.10849 0.01777  -0.11890 28  GLN A OE1 
104  N NE2 . GLN A 21  ? 0.46652 0.68752 0.53420 -0.10497 0.02472  -0.11036 28  GLN A NE2 
105  N N   . LEU A 22  ? 0.17226 0.26234 0.21515 -0.03594 -0.00063 -0.05789 29  LEU A N   
106  C CA  . LEU A 22  ? 0.21970 0.28644 0.25340 -0.03591 0.00190  -0.05699 29  LEU A CA  
107  C C   . LEU A 22  ? 0.22668 0.29559 0.26232 -0.02012 -0.01024 -0.04475 29  LEU A C   
108  O O   . LEU A 22  ? 0.20667 0.28244 0.23891 -0.02109 -0.01293 -0.04458 29  LEU A O   
109  C CB  . LEU A 22  ? 0.23447 0.25793 0.25739 -0.03292 0.01541  -0.05518 29  LEU A CB  
110  C CG  . LEU A 22  ? 0.23014 0.23277 0.24288 -0.02692 0.01875  -0.05140 29  LEU A CG  
111  C CD1 . LEU A 22  ? 0.29688 0.29680 0.29994 -0.04385 0.02867  -0.06357 29  LEU A CD1 
112  C CD2 . LEU A 22  ? 0.29271 0.26369 0.29416 -0.01288 0.03018  -0.04417 29  LEU A CD2 
113  N N   . MET A 23  ? 0.15615 0.21615 0.19515 -0.00726 -0.01504 -0.03572 30  MET A N   
114  C CA  . MET A 23  ? 0.19408 0.24842 0.23203 0.00270  -0.02099 -0.02702 30  MET A CA  
115  C C   . MET A 23  ? 0.18623 0.26280 0.22248 0.00851  -0.02530 -0.02209 30  MET A C   
116  O O   . MET A 23  ? 0.19610 0.26813 0.22718 0.01174  -0.02565 -0.01724 30  MET A O   
117  C CB  . MET A 23  ? 0.17123 0.21084 0.21033 0.01081  -0.02202 -0.02276 30  MET A CB  
118  C CG  . MET A 23  ? 0.18166 0.20794 0.21988 0.01067  -0.01798 -0.02565 30  MET A CG  
119  S SD  . MET A 23  ? 0.19370 0.21354 0.23256 0.01867  -0.01988 -0.02449 30  MET A SD  
120  C CE  . MET A 23  ? 0.20756 0.22325 0.24510 0.01558  -0.02212 -0.02468 30  MET A CE  
121  N N   . SER A 24  ? 0.19778 0.30234 0.23697 0.01224  -0.02724 -0.02222 31  SER A N   
122  C CA  . SER A 24  ? 0.18273 0.31845 0.21728 0.02452  -0.03032 -0.01523 31  SER A CA  
123  C C   . SER A 24  ? 0.19711 0.35554 0.22920 0.01599  -0.03174 -0.02153 31  SER A C   
124  O O   . SER A 24  ? 0.22983 0.39600 0.25314 0.02831  -0.03254 -0.01249 31  SER A O   
125  C CB  . SER A 24  ? 0.21800 0.39387 0.25759 0.03103  -0.03229 -0.01554 31  SER A CB  
126  O OG  . SER A 24  ? 0.34363 0.49692 0.38161 0.04366  -0.03009 -0.00719 31  SER A OG  
127  N N   . LEU A 25  ? 0.18616 0.35099 0.22249 -0.00480 -0.02914 -0.03712 32  LEU A N   
128  C CA  . LEU A 25  ? 0.17077 0.35439 0.20226 -0.01575 -0.02862 -0.04635 32  LEU A CA  
129  C C   . LEU A 25  ? 0.20233 0.35221 0.22631 -0.01081 -0.02737 -0.03876 32  LEU A C   
130  O O   . LEU A 25  ? 0.22391 0.39076 0.24119 -0.00624 -0.02951 -0.03618 32  LEU A O   
131  C CB  . LEU A 25  ? 0.25701 0.44166 0.28963 -0.04202 -0.01992 -0.06674 32  LEU A CB  
132  C CG  . LEU A 25  ? 0.31656 0.51136 0.34093 -0.06142 -0.01404 -0.08321 32  LEU A CG  
133  C CD1 . LEU A 25  ? 0.43195 0.62435 0.45510 -0.08822 0.00042  -0.10359 32  LEU A CD1 
134  C CD2 . LEU A 25  ? 0.36223 0.51025 0.37613 -0.05880 -0.00867 -0.07839 32  LEU A CD2 
135  N N   . ILE A 26  ? 0.18060 0.28902 0.20552 -0.01065 -0.02366 -0.03518 33  ILE A N   
136  C CA  . ILE A 26  ? 0.21437 0.29954 0.23470 -0.00729 -0.02202 -0.02925 33  ILE A CA  
137  C C   . ILE A 26  ? 0.19947 0.28483 0.21601 0.00652  -0.02419 -0.01614 33  ILE A C   
138  O O   . ILE A 26  ? 0.22107 0.30384 0.23138 0.00877  -0.02243 -0.01184 33  ILE A O   
139  C CB  . ILE A 26  ? 0.17358 0.22956 0.19644 -0.00802 -0.01793 -0.02909 33  ILE A CB  
140  C CG1 . ILE A 26  ? 0.22361 0.26829 0.24134 -0.01721 -0.00904 -0.03878 33  ILE A CG1 
141  C CG2 . ILE A 26  ? 0.20833 0.25257 0.23015 -0.00412 -0.01724 -0.02299 33  ILE A CG2 
142  C CD1 . ILE A 26  ? 0.23226 0.25506 0.24916 -0.01119 -0.00337 -0.03628 33  ILE A CD1 
143  N N   . ILE A 27  ? 0.21199 0.29589 0.22895 0.01684  -0.02480 -0.00904 34  ILE A N   
144  C CA  . ILE A 27  ? 0.25145 0.32082 0.25819 0.03112  -0.01987 0.00433  34  ILE A CA  
145  C C   . ILE A 27  ? 0.25654 0.35575 0.25243 0.04634  -0.02003 0.01266  34  ILE A C   
146  O O   . ILE A 27  ? 0.29948 0.38497 0.28214 0.05710  -0.01280 0.02380  34  ILE A O   
147  C CB  . ILE A 27  ? 0.24066 0.29058 0.24650 0.03813  -0.01652 0.00862  34  ILE A CB  
148  C CG1 . ILE A 27  ? 0.24331 0.26864 0.25698 0.02477  -0.01569 0.00067  34  ILE A CG1 
149  C CG2 . ILE A 27  ? 0.28523 0.31410 0.27304 0.05589  -0.00543 0.02329  34  ILE A CG2 
150  C CD1 . ILE A 27  ? 0.27631 0.28841 0.29052 0.02815  -0.01415 0.00018  34  ILE A CD1 
151  N N   . ASN A 28  ? 0.21160 0.35625 0.21175 0.04753  -0.02676 0.00691  35  ASN A N   
152  C CA  . ASN A 28  ? 0.23552 0.42423 0.22498 0.06757  -0.02786 0.01567  35  ASN A CA  
153  C C   . ASN A 28  ? 0.28600 0.51346 0.27376 0.05976  -0.03257 0.00655  35  ASN A C   
154  O O   . ASN A 28  ? 0.38141 0.64465 0.35646 0.07995  -0.03255 0.01623  35  ASN A O   
155  C CB  . ASN A 28  ? 0.27703 0.50902 0.27195 0.07626  -0.03221 0.01460  35  ASN A CB  
156  C CG  . ASN A 28  ? 0.36806 0.56446 0.35866 0.09103  -0.02571 0.02669  35  ASN A CG  
157  O OD1 . ASN A 28  ? 0.42391 0.57336 0.39947 0.10398  -0.01504 0.04039  35  ASN A OD1 
158  N ND2 . ASN A 28  ? 0.46335 0.67905 0.46546 0.08695  -0.02961 0.02016  35  ASN A ND2 
159  N N   . THR A 29  ? 0.22119 0.44232 0.21782 0.03362  -0.03453 -0.01119 36  THR A N   
160  C CA  . THR A 29  ? 0.20872 0.46357 0.20105 0.02322  -0.03682 -0.02322 36  THR A CA  
161  C C   . THR A 29  ? 0.23654 0.46929 0.21645 0.03354  -0.03293 -0.01161 36  THR A C   
162  O O   . THR A 29  ? 0.24231 0.42461 0.22287 0.03128  -0.02749 -0.00533 36  THR A O   
163  C CB  . THR A 29  ? 0.25084 0.49160 0.25013 -0.00681 -0.03387 -0.04503 36  THR A CB  
164  O OG1 . THR A 29  ? 0.25674 0.51654 0.26620 -0.01836 -0.03426 -0.05630 36  THR A OG1 
165  C CG2 . THR A 29  ? 0.28380 0.55377 0.27503 -0.02083 -0.03311 -0.06077 36  THR A CG2 
166  N N   . PHE A 30  ? 0.23139 0.50783 0.19987 0.04495  -0.03520 -0.00933 37  PHE A N   
167  C CA  . PHE A 30  ? 0.20358 0.46130 0.15931 0.05256  -0.03026 -0.00011 37  PHE A CA  
168  C C   . PHE A 30  ? 0.25261 0.49086 0.21232 0.02695  -0.02912 -0.01733 37  PHE A C   
169  O O   . PHE A 30  ? 0.26437 0.53407 0.22456 0.00929  -0.03185 -0.03758 37  PHE A O   
170  C CB  . PHE A 30  ? 0.21877 0.53186 0.15827 0.07481  -0.03225 0.00763  37  PHE A CB  
171  C CG  . PHE A 30  ? 0.26020 0.55221 0.18474 0.08386  -0.02541 0.01838  37  PHE A CG  
172  C CD1 . PHE A 30  ? 0.36147 0.60083 0.27597 0.10043  -0.01292 0.04053  37  PHE A CD1 
173  C CD2 . PHE A 30  ? 0.26370 0.58313 0.18443 0.07238  -0.02831 0.00437  37  PHE A CD2 
174  C CE1 . PHE A 30  ? 0.32139 0.54041 0.22254 0.10665  -0.00421 0.05010  37  PHE A CE1 
175  C CE2 . PHE A 30  ? 0.31014 0.61189 0.21564 0.08191  -0.02193 0.01510  37  PHE A CE2 
176  C CZ  . PHE A 30  ? 0.32022 0.57189 0.21747 0.09910  -0.00969 0.03861  37  PHE A CZ  
177  N N   . TYR A 31  ? 0.21132 0.39899 0.17195 0.02467  -0.02273 -0.01026 38  TYR A N   
178  C CA  . TYR A 31  ? 0.21729 0.38237 0.17963 0.00647  -0.01911 -0.02285 38  TYR A CA  
179  C C   . TYR A 31  ? 0.19838 0.32874 0.15917 0.01248  -0.01260 -0.00990 38  TYR A C   
180  O O   . TYR A 31  ? 0.22303 0.32642 0.19215 0.01343  -0.00992 -0.00275 38  TYR A O   
181  C CB  . TYR A 31  ? 0.23792 0.38352 0.21096 -0.00853 -0.01791 -0.03423 38  TYR A CB  
182  C CG  . TYR A 31  ? 0.24086 0.35742 0.20994 -0.02037 -0.00967 -0.04341 38  TYR A CG  
183  C CD1 . TYR A 31  ? 0.29647 0.42160 0.25371 -0.03350 -0.00442 -0.05967 38  TYR A CD1 
184  C CD2 . TYR A 31  ? 0.34652 0.42995 0.32095 -0.01692 -0.00524 -0.03617 38  TYR A CD2 
185  C CE1 . TYR A 31  ? 0.44777 0.53890 0.39540 -0.04013 0.00757  -0.06607 38  TYR A CE1 
186  C CE2 . TYR A 31  ? 0.34963 0.41012 0.31670 -0.02054 0.00439  -0.04121 38  TYR A CE2 
187  C CZ  . TYR A 31  ? 0.43712 0.49635 0.38920 -0.03068 0.01202  -0.05486 38  TYR A CZ  
188  O OH  . TYR A 31  ? 0.60397 0.63272 0.54300 -0.03054 0.02595  -0.05814 38  TYR A OH  
189  N N   . SER A 32  ? 0.20642 0.34169 0.15669 0.01446  -0.00938 -0.00896 39  SER A N   
190  C CA  . SER A 32  ? 0.21518 0.32638 0.16335 0.02059  -0.00177 0.00421  39  SER A CA  
191  C C   . SER A 32  ? 0.23589 0.32298 0.19345 0.00999  0.00244  -0.00046 39  SER A C   
192  O O   . SER A 32  ? 0.27009 0.34195 0.23284 0.01054  0.00831  0.00788  39  SER A O   
193  C CB  . SER A 32  ? 0.23323 0.36162 0.16545 0.02958  0.00098  0.00890  39  SER A CB  
194  O OG  . SER A 32  ? 0.25630 0.41189 0.17729 0.04697  -0.00116 0.01817  39  SER A OG  
195  N N   . ASN A 33  ? 0.23822 0.32304 0.19604 0.00094  0.00213  -0.01379 40  ASN A N   
196  C CA  . ASN A 33  ? 0.24778 0.31476 0.20786 -0.00129 0.00877  -0.01568 40  ASN A CA  
197  C C   . ASN A 33  ? 0.23309 0.29028 0.20716 -0.00170 0.00775  -0.01372 40  ASN A C   
198  O O   . ASN A 33  ? 0.24523 0.29200 0.21863 -0.00245 0.01100  -0.01952 40  ASN A O   
199  C CB  . ASN A 33  ? 0.28037 0.33995 0.22640 -0.00723 0.01502  -0.02914 40  ASN A CB  
200  C CG  . ASN A 33  ? 0.33374 0.37289 0.27531 -0.00197 0.02573  -0.02790 40  ASN A CG  
201  O OD1 . ASN A 33  ? 0.33180 0.37623 0.27896 0.00588  0.02735  -0.01809 40  ASN A OD1 
202  N ND2 . ASN A 33  ? 0.34691 0.36361 0.27597 -0.00540 0.03588  -0.03781 40  ASN A ND2 
203  N N   . LYS A 34  ? 0.22725 0.23953 0.17905 -0.00220 -0.03468 -0.01669 41  LYS A N   
204  C CA  . LYS A 34  ? 0.20244 0.24095 0.18440 0.00273  -0.02385 -0.01510 41  LYS A CA  
205  C C   . LYS A 34  ? 0.21915 0.24413 0.19937 0.00517  -0.01365 -0.02427 41  LYS A C   
206  O O   . LYS A 34  ? 0.20008 0.23733 0.19678 0.00610  -0.01040 -0.02399 41  LYS A O   
207  C CB  . LYS A 34  ? 0.19955 0.24686 0.18759 0.01629  -0.01567 -0.01263 41  LYS A CB  
208  C CG  . LYS A 34  ? 0.19258 0.26502 0.18875 0.02210  -0.02120 0.00109  41  LYS A CG  
209  C CD  . LYS A 34  ? 0.24144 0.30408 0.22697 0.04192  -0.01389 0.00052  41  LYS A CD  
210  C CE  . LYS A 34  ? 0.24249 0.33342 0.23378 0.05682  -0.01503 0.01701  41  LYS A CE  
211  N NZ  . LYS A 34  ? 0.23443 0.36840 0.24538 0.07273  -0.00850 0.03532  41  LYS A NZ  
212  N N   . GLU A 35  ? 0.22314 0.22667 0.18253 0.01024  -0.00718 -0.02848 42  GLU A N   
213  C CA  . GLU A 35  ? 0.21305 0.21729 0.17980 0.01553  0.00466  -0.02859 42  GLU A CA  
214  C C   . GLU A 35  ? 0.22728 0.22625 0.19485 0.01115  0.00092  -0.03384 42  GLU A C   
215  O O   . GLU A 35  ? 0.22061 0.22693 0.20249 0.01361  0.00852  -0.03250 42  GLU A O   
216  C CB  . GLU A 35  ? 0.24748 0.24121 0.19115 0.03071  0.01732  -0.02308 42  GLU A CB  
217  C CG  . GLU A 35  ? 0.27171 0.22413 0.16275 0.04151  0.01251  -0.03141 42  GLU A CG  
218  C CD  . GLU A 35  ? 0.38835 0.32559 0.23996 0.07017  0.02995  -0.02380 42  GLU A CD  
219  O OE1 . GLU A 35  ? 0.42263 0.37848 0.28245 0.07466  0.03844  -0.01283 42  GLU A OE1 
220  O OE2 . GLU A 35  ? 0.53099 0.43558 0.33796 0.09247  0.03614  -0.02658 42  GLU A OE2 
221  N N   . ILE A 36  ? 0.22086 0.20769 0.17538 0.00138  -0.01457 -0.03553 43  ILE A N   
222  C CA  . ILE A 36  ? 0.23312 0.21138 0.18689 -0.00618 -0.02195 -0.03696 43  ILE A CA  
223  C C   . ILE A 36  ? 0.20162 0.21323 0.19232 -0.00851 -0.01547 -0.03316 43  ILE A C   
224  O O   . ILE A 36  ? 0.20403 0.21176 0.19720 -0.01220 -0.01711 -0.03401 43  ILE A O   
225  C CB  . ILE A 36  ? 0.28155 0.23630 0.21421 -0.02412 -0.04942 -0.03150 43  ILE A CB  
226  C CG1 . ILE A 36  ? 0.27238 0.27182 0.24176 -0.03750 -0.05888 -0.01387 43  ILE A CG1 
227  C CG2 . ILE A 36  ? 0.34529 0.24075 0.21587 -0.01651 -0.06047 -0.03946 43  ILE A CG2 
228  C CD1 . ILE A 36  ? 0.27600 0.31811 0.28521 -0.04663 -0.06020 0.00289  43  ILE A CD1 
229  N N   . PHE A 37  ? 0.17339 0.20842 0.18227 -0.00269 -0.00938 -0.02925 44  PHE A N   
230  C CA  . PHE A 37  ? 0.16898 0.21785 0.19135 0.00384  -0.00400 -0.02747 44  PHE A CA  
231  C C   . PHE A 37  ? 0.15716 0.19132 0.17905 0.00392  -0.00013 -0.03426 44  PHE A C   
232  O O   . PHE A 37  ? 0.16760 0.20510 0.19428 0.00455  0.00022  -0.03410 44  PHE A O   
233  C CB  . PHE A 37  ? 0.17592 0.22608 0.19306 0.01833  -0.00069 -0.02558 44  PHE A CB  
234  C CG  . PHE A 37  ? 0.16895 0.19264 0.17626 0.01836  -0.00246 -0.03119 44  PHE A CG  
235  C CD1 . PHE A 37  ? 0.19446 0.21437 0.20049 0.01417  -0.00267 -0.02930 44  PHE A CD1 
236  C CD2 . PHE A 37  ? 0.20170 0.20460 0.20154 0.01967  -0.00767 -0.03328 44  PHE A CD2 
237  C CE1 . PHE A 37  ? 0.19233 0.19865 0.19922 0.00942  -0.00676 -0.02389 44  PHE A CE1 
238  C CE2 . PHE A 37  ? 0.21513 0.19723 0.21328 0.01080  -0.01790 -0.02873 44  PHE A CE2 
239  C CZ  . PHE A 37  ? 0.20564 0.19467 0.21203 0.00471  -0.01682 -0.02130 44  PHE A CZ  
240  N N   . LEU A 38  ? 0.15913 0.18364 0.17838 0.00453  0.00341  -0.03492 45  LEU A N   
241  C CA  . LEU A 38  ? 0.15110 0.17515 0.18048 0.00416  0.00585  -0.03153 45  LEU A CA  
242  C C   . LEU A 38  ? 0.19207 0.21204 0.21653 0.00608  0.00952  -0.03455 45  LEU A C   
243  O O   . LEU A 38  ? 0.18288 0.20506 0.21692 0.00455  0.00859  -0.03373 45  LEU A O   
244  C CB  . LEU A 38  ? 0.15792 0.18979 0.19642 0.00511  0.00983  -0.01866 45  LEU A CB  
245  C CG  . LEU A 38  ? 0.14832 0.19431 0.21066 0.00061  0.00826  -0.00241 45  LEU A CG  
246  C CD1 . LEU A 38  ? 0.18670 0.21392 0.24913 -0.01106 -0.01088 -0.00462 45  LEU A CD1 
247  C CD2 . LEU A 38  ? 0.20544 0.27547 0.28733 -0.00008 0.01234  0.02285  45  LEU A CD2 
248  N N   . ARG A 39  ? 0.19233 0.19571 0.19260 0.01005  0.00969  -0.03835 46  ARG A N   
249  C CA  . ARG A 39  ? 0.19751 0.17745 0.17659 0.01266  0.00656  -0.04262 46  ARG A CA  
250  C C   . ARG A 39  ? 0.21199 0.19899 0.20544 -0.00167 -0.00346 -0.04288 46  ARG A C   
251  O O   . ARG A 39  ? 0.21655 0.19688 0.20959 -0.00084 -0.00325 -0.04366 46  ARG A O   
252  C CB  . ARG A 39  ? 0.27914 0.21721 0.21071 0.01691  -0.00289 -0.04760 46  ARG A CB  
253  C CG  . ARG A 39  ? 0.34769 0.23879 0.24014 0.01625  -0.01706 -0.05263 46  ARG A CG  
254  C CD  . ARG A 39  ? 0.41950 0.24902 0.25057 0.01433  -0.03983 -0.05723 46  ARG A CD  
255  N NE  . ARG A 39  ? 0.44815 0.29252 0.30130 -0.01697 -0.06379 -0.04873 46  ARG A NE  
256  C CZ  . ARG A 39  ? 0.53556 0.34283 0.35230 -0.02703 -0.08803 -0.04697 46  ARG A CZ  
257  N NH1 . ARG A 39  ? 0.54734 0.30016 0.30401 -0.00408 -0.08701 -0.05290 46  ARG A NH1 
258  N NH2 . ARG A 39  ? 0.52699 0.36670 0.37956 -0.05656 -0.10890 -0.02999 46  ARG A NH2 
259  N N   . GLU A 40  ? 0.18158 0.18780 0.18900 -0.01135 -0.01007 -0.03774 47  GLU A N   
260  C CA  . GLU A 40  ? 0.17893 0.20411 0.20250 -0.02021 -0.01576 -0.02847 47  GLU A CA  
261  C C   . GLU A 40  ? 0.16160 0.19860 0.19677 -0.01055 -0.00554 -0.03036 47  GLU A C   
262  O O   . GLU A 40  ? 0.16366 0.20413 0.20321 -0.01351 -0.00690 -0.02636 47  GLU A O   
263  C CB  . GLU A 40  ? 0.15156 0.20859 0.19144 -0.02523 -0.02068 -0.01285 47  GLU A CB  
264  C CG  . GLU A 40  ? 0.21085 0.25269 0.23834 -0.04151 -0.04018 -0.00656 47  GLU A CG  
265  C CD  . GLU A 40  ? 0.26858 0.27071 0.27241 -0.05973 -0.06284 -0.00460 47  GLU A CD  
266  O OE1 . GLU A 40  ? 0.26409 0.27602 0.28123 -0.06714 -0.06564 0.00410  47  GLU A OE1 
267  O OE2 . GLU A 40  ? 0.38844 0.34001 0.35073 -0.06466 -0.08008 -0.01174 47  GLU A OE2 
268  N N   . LEU A 41  ? 0.14871 0.18427 0.18304 -0.00070 0.00000  -0.03489 48  LEU A N   
269  C CA  . LEU A 41  ? 0.16095 0.18922 0.19163 0.00650  0.00024  -0.03671 48  LEU A CA  
270  C C   . LEU A 41  ? 0.17719 0.19650 0.21395 0.00133  -0.00124 -0.03863 48  LEU A C   
271  O O   . LEU A 41  ? 0.17128 0.18612 0.20607 0.00267  -0.00364 -0.03853 48  LEU A O   
272  C CB  . LEU A 41  ? 0.17222 0.18346 0.18881 0.01390  -0.00431 -0.03861 48  LEU A CB  
273  C CG  . LEU A 41  ? 0.19021 0.20726 0.19232 0.02949  -0.00026 -0.03524 48  LEU A CG  
274  C CD1 . LEU A 41  ? 0.21862 0.19926 0.19208 0.03823  -0.00980 -0.03913 48  LEU A CD1 
275  C CD2 . LEU A 41  ? 0.20939 0.24232 0.20302 0.04703  0.00788  -0.02682 48  LEU A CD2 
276  N N   . ILE A 42  ? 0.15284 0.17205 0.19483 0.00011  0.00203  -0.03707 49  ILE A N   
277  C CA  . ILE A 42  ? 0.14864 0.16945 0.19853 0.00276  0.00507  -0.03203 49  ILE A CA  
278  C C   . ILE A 42  ? 0.16840 0.17727 0.20613 0.00365  0.00528  -0.03709 49  ILE A C   
279  O O   . ILE A 42  ? 0.16715 0.17594 0.21031 0.00496  0.00472  -0.03470 49  ILE A O   
280  C CB  . ILE A 42  ? 0.13990 0.17073 0.19370 0.01215  0.01485  -0.02198 49  ILE A CB  
281  C CG1 . ILE A 42  ? 0.13467 0.18214 0.21057 0.00423  0.00905  -0.00795 49  ILE A CG1 
282  C CG2 . ILE A 42  ? 0.16443 0.20157 0.21993 0.02655  0.02452  -0.01230 49  ILE A CG2 
283  C CD1 . ILE A 42  ? 0.16216 0.23229 0.24753 0.01466  0.02174  0.00995  49  ILE A CD1 
284  N N   . SER A 43  ? 0.18506 0.18071 0.20559 -0.00056 0.00102  -0.04106 50  SER A N   
285  C CA  . SER A 43  ? 0.19275 0.16891 0.19878 -0.00684 -0.00763 -0.04118 50  SER A CA  
286  C C   . SER A 43  ? 0.18304 0.17956 0.20777 -0.01375 -0.00923 -0.03550 50  SER A C   
287  O O   . SER A 43  ? 0.19058 0.17741 0.21194 -0.01485 -0.01175 -0.03439 50  SER A O   
288  C CB  . SER A 43  ? 0.24463 0.19880 0.22895 -0.01847 -0.02273 -0.03946 50  SER A CB  
289  O OG  . SER A 43  ? 0.35088 0.28139 0.32145 -0.03265 -0.04023 -0.03356 50  SER A OG  
290  N N   . ASN A 44  ? 0.17243 0.19400 0.20987 -0.01274 -0.00614 -0.03067 51  ASN A N   
291  C CA  . ASN A 44  ? 0.15871 0.19623 0.20104 -0.00782 -0.00303 -0.02337 51  ASN A CA  
292  C C   . ASN A 44  ? 0.16334 0.18508 0.19968 -0.00118 -0.00277 -0.03087 51  ASN A C   
293  O O   . ASN A 44  ? 0.16851 0.19022 0.20254 0.00007  -0.00314 -0.02713 51  ASN A O   
294  C CB  . ASN A 44  ? 0.14930 0.20664 0.18957 0.00574  0.00372  -0.01675 51  ASN A CB  
295  C CG  . ASN A 44  ? 0.22991 0.32078 0.28718 -0.00099 0.00298  0.00213  51  ASN A CG  
296  O OD1 . ASN A 44  ? 0.21542 0.30812 0.28350 -0.02200 -0.00916 0.01143  51  ASN A OD1 
297  N ND2 . ASN A 44  ? 0.24181 0.35522 0.29731 0.01721  0.01224  0.01143  51  ASN A ND2 
298  N N   . SER A 45  ? 0.14170 0.15298 0.17823 0.00065  -0.00502 -0.03642 52  SER A N   
299  C CA  . SER A 45  ? 0.17876 0.17938 0.21666 0.00035  -0.01225 -0.03545 52  SER A CA  
300  C C   . SER A 45  ? 0.16275 0.16615 0.21026 -0.00097 -0.00942 -0.03281 52  SER A C   
301  O O   . SER A 45  ? 0.16120 0.15952 0.20750 -0.00086 -0.01433 -0.03075 52  SER A O   
302  C CB  . SER A 45  ? 0.15858 0.15772 0.20594 -0.00430 -0.01983 -0.03035 52  SER A CB  
303  O OG  . SER A 45  ? 0.19395 0.17235 0.21926 -0.00190 -0.02919 -0.03369 52  SER A OG  
304  N N   . SER A 46  ? 0.14491 0.14775 0.19192 0.00185  -0.00263 -0.03313 53  SER A N   
305  C CA  . SER A 46  ? 0.16045 0.15160 0.19970 0.00897  0.00009  -0.03154 53  SER A CA  
306  C C   . SER A 46  ? 0.17679 0.15522 0.20584 0.00131  -0.00640 -0.03339 53  SER A C   
307  O O   . SER A 46  ? 0.19293 0.16540 0.22122 0.00478  -0.00759 -0.03090 53  SER A O   
308  C CB  . SER A 46  ? 0.19401 0.16531 0.20917 0.02094  0.00590  -0.03390 53  SER A CB  
309  O OG  . SER A 46  ? 0.23547 0.17791 0.22387 0.03525  0.00702  -0.03399 53  SER A OG  
310  N N   . ASP A 47  ? 0.19585 0.17723 0.22194 -0.00947 -0.01087 -0.03194 54  ASP A N   
311  C CA  . ASP A 47  ? 0.18906 0.17147 0.21446 -0.01931 -0.01730 -0.02301 54  ASP A CA  
312  C C   . ASP A 47  ? 0.19065 0.18747 0.22241 -0.01230 -0.01254 -0.02038 54  ASP A C   
313  O O   . ASP A 47  ? 0.19484 0.18596 0.22365 -0.01463 -0.01557 -0.01518 54  ASP A O   
314  C CB  . ASP A 47  ? 0.16803 0.17126 0.20242 -0.03171 -0.02207 -0.00972 54  ASP A CB  
315  C CG  . ASP A 47  ? 0.24416 0.21741 0.26165 -0.04649 -0.03891 -0.00821 54  ASP A CG  
316  O OD1 . ASP A 47  ? 0.30642 0.23232 0.29243 -0.04137 -0.04528 -0.01942 54  ASP A OD1 
317  O OD2 . ASP A 47  ? 0.26888 0.26163 0.29828 -0.06049 -0.04760 0.00648  54  ASP A OD2 
318  N N   . ALA A 48  ? 0.15491 0.15962 0.18569 -0.00281 -0.00864 -0.02412 55  ALA A N   
319  C CA  . ALA A 48  ? 0.15257 0.15071 0.16905 0.00730  -0.01011 -0.02363 55  ALA A CA  
320  C C   . ALA A 48  ? 0.18377 0.16685 0.20343 0.00458  -0.01863 -0.02656 55  ALA A C   
321  O O   . ALA A 48  ? 0.18560 0.15961 0.19358 0.00827  -0.02272 -0.02419 55  ALA A O   
322  C CB  . ALA A 48  ? 0.17924 0.16607 0.17433 0.01976  -0.01180 -0.02801 55  ALA A CB  
323  N N   . LEU A 49  ? 0.16649 0.15222 0.20290 0.00093  -0.02031 -0.02701 56  LEU A N   
324  C CA  . LEU A 49  ? 0.16337 0.15119 0.21349 0.00113  -0.02587 -0.01983 56  LEU A CA  
325  C C   . LEU A 49  ? 0.17593 0.15767 0.22174 0.00548  -0.02046 -0.01914 56  LEU A C   
326  O O   . LEU A 49  ? 0.18537 0.16532 0.23388 0.00716  -0.02590 -0.01365 56  LEU A O   
327  C CB  . LEU A 49  ? 0.16037 0.16737 0.23396 0.00245  -0.02333 -0.01026 56  LEU A CB  
328  C CG  . LEU A 49  ? 0.14646 0.15429 0.22683 -0.00815 -0.03816 -0.00429 56  LEU A CG  
329  C CD1 . LEU A 49  ? 0.16136 0.19503 0.26526 -0.00672 -0.03015 0.00723  56  LEU A CD1 
330  C CD2 . LEU A 49  ? 0.17554 0.17876 0.26416 -0.01909 -0.06189 0.01026  56  LEU A CD2 
331  N N   . ASP A 50  ? 0.17834 0.14881 0.21192 0.00570  -0.01486 -0.02336 57  ASP A N   
332  C CA  . ASP A 50  ? 0.20165 0.14835 0.21806 0.00695  -0.01756 -0.02230 57  ASP A CA  
333  C C   . ASP A 50  ? 0.20578 0.15568 0.22211 -0.00108 -0.02257 -0.01735 57  ASP A C   
334  O O   . ASP A 50  ? 0.22559 0.16202 0.23514 0.00180  -0.02596 -0.01413 57  ASP A O   
335  C CB  . ASP A 50  ? 0.20754 0.12604 0.20007 0.00034  -0.02316 -0.02502 57  ASP A CB  
336  C CG  . ASP A 50  ? 0.27231 0.17039 0.24447 0.01686  -0.01784 -0.03070 57  ASP A CG  
337  O OD1 . ASP A 50  ? 0.28852 0.20524 0.27254 0.03609  -0.00535 -0.02705 57  ASP A OD1 
338  O OD2 . ASP A 50  ? 0.32082 0.18410 0.26289 0.01094  -0.02803 -0.03436 57  ASP A OD2 
339  N N   . LYS A 51  ? 0.18728 0.15526 0.20677 -0.00588 -0.02083 -0.01417 58  LYS A N   
340  C CA  . LYS A 51  ? 0.20489 0.18084 0.21878 -0.00599 -0.02044 -0.00392 58  LYS A CA  
341  C C   . LYS A 51  ? 0.21066 0.17637 0.21520 0.00337  -0.02430 -0.00730 58  LYS A C   
342  O O   . LYS A 51  ? 0.23550 0.19551 0.23373 0.00348  -0.02651 -0.00090 58  LYS A O   
343  C CB  . LYS A 51  ? 0.21787 0.22026 0.23106 -0.00089 -0.01195 0.00565  58  LYS A CB  
344  C CG  . LYS A 51  ? 0.20289 0.22568 0.23300 -0.01584 -0.01303 0.02005  58  LYS A CG  
345  C CD  . LYS A 51  ? 0.19722 0.25825 0.23178 -0.00308 -0.00028 0.03455  58  LYS A CD  
346  C CE  . LYS A 51  ? 0.24923 0.33533 0.30793 -0.02135 -0.00584 0.05135  58  LYS A CE  
347  N NZ  . LYS A 51  ? 0.28794 0.42221 0.35579 -0.00346 0.00991  0.07181  58  LYS A NZ  
348  N N   . ILE A 52  ? 0.20720 0.16692 0.20906 0.00806  -0.03006 -0.01427 59  ILE A N   
349  C CA  . ILE A 52  ? 0.20540 0.14841 0.19590 0.01076  -0.04376 -0.01335 59  ILE A CA  
350  C C   . ILE A 52  ? 0.23103 0.18003 0.24472 0.00731  -0.04727 -0.00742 59  ILE A C   
351  O O   . ILE A 52  ? 0.24597 0.18621 0.25327 0.00857  -0.05574 -0.00260 59  ILE A O   
352  C CB  . ILE A 52  ? 0.24675 0.16982 0.22104 0.01051  -0.06036 -0.01665 59  ILE A CB  
353  C CG1 . ILE A 52  ? 0.29064 0.18172 0.23888 0.00998  -0.08405 -0.01334 59  ILE A CG1 
354  C CG2 . ILE A 52  ? 0.25765 0.19928 0.26735 -0.00027 -0.06414 -0.01218 59  ILE A CG2 
355  C CD1 . ILE A 52  ? 0.35905 0.22546 0.25810 0.02839  -0.07913 -0.01651 59  ILE A CD1 
356  N N   . ARG A 53  ? 0.20111 0.16290 0.23539 0.00857  -0.03928 -0.00604 60  ARG A N   
357  C CA  . ARG A 53  ? 0.22358 0.18984 0.26981 0.01765  -0.03696 0.00277  60  ARG A CA  
358  C C   . ARG A 53  ? 0.22469 0.16819 0.25020 0.01972  -0.03589 0.00074  60  ARG A C   
359  O O   . ARG A 53  ? 0.25103 0.19233 0.27818 0.02537  -0.04040 0.00809  60  ARG A O   
360  C CB  . ARG A 53  ? 0.23687 0.21185 0.29059 0.03044  -0.02427 0.00540  60  ARG A CB  
361  C CG  . ARG A 53  ? 0.29376 0.26945 0.34676 0.05346  -0.01646 0.01722  60  ARG A CG  
362  C CD  . ARG A 53  ? 0.41088 0.39335 0.45924 0.07812  0.00014  0.02349  60  ARG A CD  
363  N NE  . ARG A 53  ? 0.48614 0.52651 0.58190 0.08241  0.00410  0.04924  60  ARG A NE  
364  C CZ  . ARG A 53  ? 0.52738 0.59055 0.63130 0.09739  0.01845  0.05965  60  ARG A CZ  
365  N NH1 . ARG A 53  ? 0.43750 0.46181 0.49742 0.11106  0.02905  0.04141  60  ARG A NH1 
366  N NH2 . ARG A 53  ? 0.34731 0.47343 0.50433 0.09673  0.01895  0.09336  60  ARG A NH2 
367  N N   . TYR A 54  ? 0.22889 0.15716 0.23745 0.01217  -0.03337 -0.00447 61  TYR A N   
368  C CA  . TYR A 54  ? 0.25219 0.15730 0.24296 0.00738  -0.03833 0.00017  61  TYR A CA  
369  C C   . TYR A 54  ? 0.29581 0.20971 0.28631 0.00571  -0.04147 0.00664  61  TYR A C   
370  O O   . TYR A 54  ? 0.29008 0.18879 0.27240 0.00854  -0.04616 0.01159  61  TYR A O   
371  C CB  . TYR A 54  ? 0.26422 0.15980 0.24591 -0.00897 -0.04264 0.00411  61  TYR A CB  
372  C CG  . TYR A 54  ? 0.31194 0.17991 0.27680 -0.02092 -0.05534 0.01590  61  TYR A CG  
373  C CD1 . TYR A 54  ? 0.33854 0.15151 0.26995 -0.01495 -0.06654 0.01181  61  TYR A CD1 
374  C CD2 . TYR A 54  ? 0.31774 0.21152 0.29421 -0.03398 -0.05617 0.03448  61  TYR A CD2 
375  C CE1 . TYR A 54  ? 0.37236 0.14817 0.28170 -0.02896 -0.08452 0.02381  61  TYR A CE1 
376  C CE2 . TYR A 54  ? 0.36993 0.24250 0.33620 -0.04944 -0.07070 0.05179  61  TYR A CE2 
377  C CZ  . TYR A 54  ? 0.36935 0.17881 0.30189 -0.05038 -0.08791 0.04529  61  TYR A CZ  
378  O OH  . TYR A 54  ? 0.41957 0.19615 0.33536 -0.06897 -0.10863 0.06361  61  TYR A OH  
379  N N   . GLU A 55  ? 0.27802 0.20875 0.26743 0.00574  -0.03917 0.00661  62  GLU A N   
380  C CA  . GLU A 55  ? 0.29730 0.22483 0.26907 0.01182  -0.04218 0.01187  62  GLU A CA  
381  C C   . GLU A 55  ? 0.32372 0.23928 0.29655 0.01549  -0.05509 0.01044  62  GLU A C   
382  O O   . GLU A 55  ? 0.34655 0.25169 0.30626 0.01842  -0.06028 0.01610  62  GLU A O   
383  C CB  . GLU A 55  ? 0.30659 0.23799 0.25674 0.02228  -0.03781 0.01042  62  GLU A CB  
384  C CG  . GLU A 55  ? 0.31322 0.27232 0.26694 0.02341  -0.02231 0.02381  62  GLU A CG  
385  C CD  . GLU A 55  ? 0.44640 0.40801 0.36519 0.04837  -0.01222 0.02782  62  GLU A CD  
386  O OE1 . GLU A 55  ? 0.47125 0.39520 0.35219 0.06177  -0.02326 0.01402  62  GLU A OE1 
387  O OE2 . GLU A 55  ? 0.44912 0.44738 0.37380 0.05634  0.00444  0.04862  62  GLU A OE2 
388  N N   . SER A 56  ? 0.29291 0.21612 0.28603 0.01428  -0.06139 0.00867  63  SER A N   
389  C CA  . SER A 56  ? 0.30275 0.22915 0.30969 0.01400  -0.07728 0.01844  63  SER A CA  
390  C C   . SER A 56  ? 0.30303 0.23448 0.32259 0.02267  -0.07185 0.02705  63  SER A C   
391  O O   . SER A 56  ? 0.33331 0.27058 0.36299 0.02407  -0.08447 0.03949  63  SER A O   
392  C CB  . SER A 56  ? 0.28414 0.23132 0.32008 0.00798  -0.08606 0.02618  63  SER A CB  
393  O OG  . SER A 56  ? 0.30141 0.27471 0.36515 0.01771  -0.06884 0.03219  63  SER A OG  
394  N N   . LEU A 57  ? 0.28670 0.20836 0.29904 0.02921  -0.05742 0.02223  64  LEU A N   
395  C CA  . LEU A 57  ? 0.34422 0.25255 0.35057 0.04420  -0.05417 0.02874  64  LEU A CA  
396  C C   . LEU A 57  ? 0.39458 0.28650 0.38583 0.04084  -0.06282 0.03276  64  LEU A C   
397  O O   . LEU A 57  ? 0.45831 0.34674 0.45070 0.05440  -0.06481 0.04222  64  LEU A O   
398  C CB  . LEU A 57  ? 0.35538 0.22999 0.33455 0.05050  -0.04646 0.02065  64  LEU A CB  
399  C CG  . LEU A 57  ? 0.35358 0.23669 0.33735 0.06072  -0.03623 0.01689  64  LEU A CG  
400  C CD1 . LEU A 57  ? 0.38262 0.21011 0.31979 0.06788  -0.03697 0.00802  64  LEU A CD1 
401  C CD2 . LEU A 57  ? 0.37165 0.29183 0.38285 0.08481  -0.02722 0.03334  64  LEU A CD2 
402  N N   . THR A 58  ? 0.37032 0.25532 0.34591 0.02758  -0.06558 0.02931  65  THR A N   
403  C CA  . THR A 58  ? 0.40493 0.27721 0.36333 0.02646  -0.07168 0.03610  65  THR A CA  
404  C C   . THR A 58  ? 0.44363 0.31886 0.39089 0.02669  -0.08218 0.03687  65  THR A C   
405  O O   . THR A 58  ? 0.52898 0.39138 0.45694 0.02951  -0.08841 0.04291  65  THR A O   
406  C CB  . THR A 58  ? 0.54087 0.40329 0.48350 0.01585  -0.06673 0.04177  65  THR A CB  
407  O OG1 . THR A 58  ? 0.51838 0.40177 0.46242 0.01118  -0.05862 0.04131  65  THR A OG1 
408  C CG2 . THR A 58  ? 0.45404 0.28807 0.38991 0.01145  -0.06938 0.04199  65  THR A CG2 
409  N N   . ASP A 59  ? 0.47334 0.31672 0.31423 0.07015  -0.03985 0.05951  66  ASP A N   
410  C CA  . ASP A 59  ? 0.42668 0.32036 0.29343 0.07370  -0.04453 0.05725  66  ASP A CA  
411  C C   . ASP A 59  ? 0.38295 0.30457 0.27541 0.07849  -0.04709 0.04764  66  ASP A C   
412  O O   . ASP A 59  ? 0.38814 0.32124 0.29338 0.06671  -0.04829 0.03805  66  ASP A O   
413  C CB  . ASP A 59  ? 0.41413 0.32385 0.28472 0.05795  -0.04529 0.05888  66  ASP A CB  
414  C CG  . ASP A 59  ? 0.52589 0.46627 0.40102 0.06572  -0.04822 0.05526  66  ASP A CG  
415  O OD1 . ASP A 59  ? 0.50150 0.45213 0.37887 0.07585  -0.05580 0.05172  66  ASP A OD1 
416  O OD2 . ASP A 59  ? 0.53677 0.48845 0.40874 0.06208  -0.04327 0.05916  66  ASP A OD2 
417  N N   . PRO A 60  ? 0.41839 0.35567 0.32203 0.09555  -0.04815 0.05426  67  PRO A N   
418  C CA  . PRO A 60  ? 0.38020 0.34970 0.31357 0.09693  -0.05228 0.05177  67  PRO A CA  
419  C C   . PRO A 60  ? 0.34113 0.33581 0.28553 0.08114  -0.06618 0.04202  67  PRO A C   
420  O O   . PRO A 60  ? 0.35086 0.36070 0.31418 0.07439  -0.06972 0.03625  67  PRO A O   
421  C CB  . PRO A 60  ? 0.42113 0.41443 0.36900 0.11783  -0.05245 0.07151  67  PRO A CB  
422  C CG  . PRO A 60  ? 0.54467 0.49750 0.46055 0.13368  -0.04014 0.07981  67  PRO A CG  
423  C CD  . PRO A 60  ? 0.52264 0.45313 0.41567 0.11506  -0.04496 0.06985  67  PRO A CD  
424  N N   . SER A 61  ? 0.41021 0.40224 0.33560 0.07692  -0.07294 0.04062  68  SER A N   
425  C CA  . SER A 61  ? 0.37547 0.37204 0.29125 0.06658  -0.08413 0.03066  68  SER A CA  
426  C C   . SER A 61  ? 0.33199 0.31947 0.24773 0.05907  -0.07495 0.01861  68  SER A C   
427  O O   . SER A 61  ? 0.35443 0.33802 0.25868 0.05380  -0.08147 0.00970  68  SER A O   
428  C CB  . SER A 61  ? 0.40782 0.39267 0.28959 0.06987  -0.08886 0.03294  68  SER A CB  
429  O OG  . SER A 61  ? 0.46748 0.43837 0.33527 0.07305  -0.07247 0.03404  68  SER A OG  
430  N N   . LYS A 62  ? 0.32897 0.30830 0.25204 0.05754  -0.06180 0.02003  69  LYS A N   
431  C CA  . LYS A 62  ? 0.34172 0.32082 0.27175 0.04914  -0.05511 0.01365  69  LYS A CA  
432  C C   . LYS A 62  ? 0.30200 0.29028 0.24990 0.04514  -0.06020 0.00444  69  LYS A C   
433  O O   . LYS A 62  ? 0.30134 0.29061 0.25191 0.04002  -0.05687 -0.00191 69  LYS A O   
434  C CB  . LYS A 62  ? 0.36043 0.32609 0.29209 0.04172  -0.04752 0.02051  69  LYS A CB  
435  C CG  . LYS A 62  ? 0.41331 0.37216 0.33067 0.03942  -0.04392 0.03430  69  LYS A CG  
436  C CD  . LYS A 62  ? 0.39205 0.36938 0.31585 0.03299  -0.03709 0.04334  69  LYS A CD  
437  C CE  . LYS A 62  ? 0.40741 0.38915 0.32310 0.03145  -0.03232 0.06369  69  LYS A CE  
438  N NZ  . LYS A 62  ? 0.43898 0.45084 0.36978 0.02769  -0.02257 0.08193  69  LYS A NZ  
439  N N   . LEU A 63  ? 0.27717 0.27626 0.23995 0.04879  -0.06686 0.00787  70  LEU A N   
440  C CA  . LEU A 63  ? 0.25264 0.26723 0.23760 0.04406  -0.07202 0.00510  70  LEU A CA  
441  C C   . LEU A 63  ? 0.26027 0.28681 0.24444 0.03587  -0.09168 0.00610  70  LEU A C   
442  O O   . LEU A 63  ? 0.30001 0.34474 0.30661 0.02832  -0.10034 0.00987  70  LEU A O   
443  C CB  . LEU A 63  ? 0.27571 0.29907 0.27980 0.05499  -0.06421 0.01547  70  LEU A CB  
444  C CG  . LEU A 63  ? 0.29463 0.28671 0.28263 0.05972  -0.04882 0.01289  70  LEU A CG  
445  C CD1 . LEU A 63  ? 0.35284 0.34027 0.34320 0.07886  -0.03738 0.02397  70  LEU A CD1 
446  C CD2 . LEU A 63  ? 0.28960 0.27435 0.27824 0.04624  -0.04684 0.00164  70  LEU A CD2 
447  N N   . ASP A 64  ? 0.30134 0.31395 0.25525 0.03516  -0.10067 0.00472  71  ASP A N   
448  C CA  . ASP A 64  ? 0.33591 0.34228 0.27096 0.02224  -0.12482 0.00436  71  ASP A CA  
449  C C   . ASP A 64  ? 0.35140 0.33671 0.27275 0.01168  -0.12842 -0.00851 71  ASP A C   
450  O O   . ASP A 64  ? 0.39075 0.36978 0.30360 -0.00568 -0.15183 -0.00679 71  ASP A O   
451  C CB  . ASP A 64  ? 0.38640 0.36565 0.27384 0.02630  -0.13101 0.00232  71  ASP A CB  
452  C CG  . ASP A 64  ? 0.48628 0.48662 0.38455 0.03287  -0.13580 0.01812  71  ASP A CG  
453  O OD1 . ASP A 64  ? 0.40028 0.43546 0.34127 0.03657  -0.13398 0.03240  71  ASP A OD1 
454  O OD2 . ASP A 64  ? 0.50474 0.48483 0.36516 0.03793  -0.13899 0.01810  71  ASP A OD2 
455  N N   . SER A 65  ? 0.31542 0.28896 0.23323 0.02010  -0.10746 -0.01822 72  SER A N   
456  C CA  . SER A 65  ? 0.33066 0.28488 0.23705 0.01568  -0.10514 -0.02859 72  SER A CA  
457  C C   . SER A 65  ? 0.36600 0.34626 0.31643 0.00690  -0.10525 -0.02616 72  SER A C   
458  O O   . SER A 65  ? 0.41319 0.38111 0.36007 0.00409  -0.10085 -0.03358 72  SER A O   
459  C CB  . SER A 65  ? 0.35067 0.29287 0.24132 0.03108  -0.08119 -0.03219 72  SER A CB  
460  O OG  . SER A 65  ? 0.32915 0.29836 0.25219 0.03494  -0.06744 -0.02413 72  SER A OG  
461  N N   . GLY A 66  ? 0.29243 0.30696 0.28106 0.00648  -0.10733 -0.01372 73  GLY A N   
462  C CA  . GLY A 66  ? 0.31832 0.35767 0.34493 0.00345  -0.10358 -0.00777 73  GLY A CA  
463  C C   . GLY A 66  ? 0.26495 0.32310 0.31469 0.01881  -0.08723 0.00208  73  GLY A C   
464  O O   . GLY A 66  ? 0.24922 0.28917 0.28518 0.02707  -0.07240 -0.00431 73  GLY A O   
465  N N   . LYS A 67  ? 0.24013 0.33181 0.32106 0.02319  -0.08986 0.02118  74  LYS A N   
466  C CA  . LYS A 67  ? 0.26669 0.36383 0.35551 0.04559  -0.07053 0.03237  74  LYS A CA  
467  C C   . LYS A 67  ? 0.22016 0.30899 0.31323 0.05376  -0.05265 0.02972  74  LYS A C   
468  O O   . LYS A 67  ? 0.29166 0.35424 0.36415 0.07097  -0.03513 0.02970  74  LYS A O   
469  C CB  . LYS A 67  ? 0.30426 0.44500 0.42346 0.05529  -0.07577 0.06104  74  LYS A CB  
470  C CG  . LYS A 67  ? 0.38205 0.52376 0.48858 0.05487  -0.08839 0.06621  74  LYS A CG  
471  C CD  . LYS A 67  ? 0.50547 0.69178 0.64291 0.07339  -0.08588 0.09980  74  LYS A CD  
472  C CE  . LYS A 67  ? 0.63629 0.83715 0.77007 0.06358  -0.10904 0.11002  74  LYS A CE  
473  N NZ  . LYS A 67  ? 0.70550 0.87301 0.80461 0.03599  -0.13137 0.08578  74  LYS A NZ  
474  N N   . GLU A 68  ? 0.19420 0.29645 0.30522 0.04121  -0.05779 0.02764  75  GLU A N   
475  C CA  . GLU A 68  ? 0.21273 0.31004 0.32775 0.04979  -0.04131 0.02777  75  GLU A CA  
476  C C   . GLU A 68  ? 0.19903 0.25336 0.28099 0.04473  -0.03479 0.00648  75  GLU A C   
477  O O   . GLU A 68  ? 0.22813 0.27391 0.30233 0.02951  -0.04419 -0.00637 75  GLU A O   
478  C CB  . GLU A 68  ? 0.30034 0.42859 0.44766 0.03608  -0.05019 0.03557  75  GLU A CB  
479  C CG  . GLU A 68  ? 0.37431 0.55744 0.56476 0.03537  -0.05987 0.06663  75  GLU A CG  
480  C CD  . GLU A 68  ? 0.74905 0.94323 0.94017 0.01944  -0.08519 0.07174  75  GLU A CD  
481  O OE1 . GLU A 68  ? 0.66263 0.89468 0.87779 0.02682  -0.08748 0.09808  75  GLU A OE1 
482  O OE2 . GLU A 68  ? 0.61141 0.77132 0.77187 0.00132  -0.10040 0.04994  75  GLU A OE2 
483  N N   . LEU A 69  ? 0.20467 0.22996 0.26312 0.05827  -0.01895 0.00627  76  LEU A N   
484  C CA  . LEU A 69  ? 0.20112 0.18654 0.22738 0.04850  -0.01746 -0.00761 76  LEU A CA  
485  C C   . LEU A 69  ? 0.20273 0.18250 0.22806 0.05032  -0.00938 -0.00839 76  LEU A C   
486  O O   . LEU A 69  ? 0.23515 0.19550 0.24129 0.06998  0.00549  -0.00089 76  LEU A O   
487  C CB  . LEU A 69  ? 0.25474 0.19362 0.23754 0.05708  -0.01164 -0.00689 76  LEU A CB  
488  C CG  . LEU A 69  ? 0.30488 0.24704 0.28602 0.05659  -0.01812 -0.00433 76  LEU A CG  
489  C CD1 . LEU A 69  ? 0.39918 0.28476 0.33048 0.06023  -0.01439 -0.00359 76  LEU A CD1 
490  C CD2 . LEU A 69  ? 0.26898 0.23284 0.26644 0.03697  -0.03089 -0.01119 76  LEU A CD2 
491  N N   . HIS A 70  ? 0.17768 0.17069 0.21854 0.03373  -0.01672 -0.01592 77  HIS A N   
492  C CA  . HIS A 70  ? 0.19252 0.18730 0.23841 0.03508  -0.01002 -0.01499 77  HIS A CA  
493  C C   . HIS A 70  ? 0.15950 0.15302 0.20685 0.01683  -0.01764 -0.02412 77  HIS A C   
494  O O   . HIS A 70  ? 0.15453 0.15335 0.20483 0.00641  -0.02586 -0.02822 77  HIS A O   
495  C CB  . HIS A 70  ? 0.17761 0.21453 0.26322 0.04154  -0.00787 -0.00187 77  HIS A CB  
496  C CG  . HIS A 70  ? 0.16561 0.22988 0.27864 0.02447  -0.02496 -0.00322 77  HIS A CG  
497  N ND1 . HIS A 70  ? 0.26687 0.32250 0.37595 0.00916  -0.03337 -0.01554 77  HIS A ND1 
498  C CD2 . HIS A 70  ? 0.22999 0.32238 0.36584 0.02084  -0.03622 0.00796  77  HIS A CD2 
499  C CE1 . HIS A 70  ? 0.24805 0.31345 0.36615 -0.00145 -0.04780 -0.01499 77  HIS A CE1 
500  N NE2 . HIS A 70  ? 0.26879 0.35682 0.40344 0.00176  -0.05278 -0.00108 77  HIS A NE2 
501  N N   . ILE A 71  ? 0.16206 0.15100 0.20732 0.01693  -0.01226 -0.02381 78  ILE A N   
502  C CA  . ILE A 71  ? 0.15051 0.14198 0.19947 0.00317  -0.01724 -0.02800 78  ILE A CA  
503  C C   . ILE A 71  ? 0.13403 0.14673 0.20818 0.00548  -0.01309 -0.02489 78  ILE A C   
504  O O   . ILE A 71  ? 0.15746 0.16962 0.23050 0.01735  -0.00272 -0.01791 78  ILE A O   
505  C CB  . ILE A 71  ? 0.18268 0.13853 0.19404 -0.00367 -0.01859 -0.02843 78  ILE A CB  
506  C CG1 . ILE A 71  ? 0.22265 0.15276 0.20604 -0.01187 -0.02662 -0.02767 78  ILE A CG1 
507  C CG2 . ILE A 71  ? 0.19142 0.16044 0.21386 -0.01706 -0.02413 -0.02703 78  ILE A CG2 
508  C CD1 . ILE A 71  ? 0.26085 0.14051 0.19293 -0.02441 -0.03429 -0.02601 78  ILE A CD1 
509  N N   . ASN A 72  ? 0.13004 0.15776 0.22250 -0.00359 -0.01944 -0.02755 79  ASN A N   
510  C CA  . ASN A 72  ? 0.10713 0.14797 0.21913 -0.00612 -0.01860 -0.02400 79  ASN A CA  
511  C C   . ASN A 72  ? 0.14856 0.18294 0.25491 -0.01136 -0.01774 -0.02670 79  ASN A C   
512  O O   . ASN A 72  ? 0.13724 0.16860 0.23628 -0.01407 -0.02050 -0.02881 79  ASN A O   
513  C CB  . ASN A 72  ? 0.11463 0.16539 0.24205 -0.01355 -0.02945 -0.02303 79  ASN A CB  
514  C CG  . ASN A 72  ? 0.12806 0.19637 0.26949 -0.01140 -0.03377 -0.01375 79  ASN A CG  
515  O OD1 . ASN A 72  ? 0.14046 0.22221 0.29055 0.00037  -0.02349 -0.00295 79  ASN A OD1 
516  N ND2 . ASN A 72  ? 0.18917 0.25523 0.32869 -0.02072 -0.04843 -0.01518 79  ASN A ND2 
517  N N   . LEU A 73  ? 0.13181 0.16902 0.24401 -0.01069 -0.01240 -0.02238 80  LEU A N   
518  C CA  . LEU A 73  ? 0.10950 0.14430 0.21948 -0.01473 -0.01163 -0.02184 80  LEU A CA  
519  C C   . LEU A 73  ? 0.09991 0.14064 0.22739 -0.01760 -0.01243 -0.01924 80  LEU A C   
520  O O   . LEU A 73  ? 0.11611 0.16748 0.25842 -0.01768 -0.00994 -0.01189 80  LEU A O   
521  C CB  . LEU A 73  ? 0.13664 0.16015 0.22844 -0.01315 -0.00649 -0.01857 80  LEU A CB  
522  C CG  . LEU A 73  ? 0.17250 0.17161 0.23108 -0.01357 -0.00881 -0.02051 80  LEU A CG  
523  C CD1 . LEU A 73  ? 0.20194 0.17251 0.22520 -0.01214 -0.00542 -0.01827 80  LEU A CD1 
524  C CD2 . LEU A 73  ? 0.18292 0.18517 0.23889 -0.02523 -0.01976 -0.01949 80  LEU A CD2 
525  N N   . ILE A 74  ? 0.12684 0.15851 0.24968 -0.01884 -0.01515 -0.02186 81  ILE A N   
526  C CA  . ILE A 74  ? 0.14111 0.15984 0.26529 -0.02411 -0.01982 -0.02115 81  ILE A CA  
527  C C   . ILE A 74  ? 0.16444 0.17369 0.28175 -0.01929 -0.01337 -0.01837 81  ILE A C   
528  O O   . ILE A 74  ? 0.16970 0.16647 0.27088 -0.00957 -0.00918 -0.01895 81  ILE A O   
529  C CB  . ILE A 74  ? 0.17763 0.17319 0.28298 -0.02628 -0.02922 -0.02764 81  ILE A CB  
530  C CG1 . ILE A 74  ? 0.18454 0.19492 0.29841 -0.02948 -0.03556 -0.02811 81  ILE A CG1 
531  C CG2 . ILE A 74  ? 0.20858 0.17582 0.30259 -0.03830 -0.04017 -0.02624 81  ILE A CG2 
532  C CD1 . ILE A 74  ? 0.23765 0.22281 0.32719 -0.03268 -0.04690 -0.03425 81  ILE A CD1 
533  N N   . PRO A 75  ? 0.13960 0.15636 0.26886 -0.02268 -0.01014 -0.01188 82  PRO A N   
534  C CA  . PRO A 75  ? 0.17126 0.17782 0.29425 -0.01794 -0.00461 -0.00737 82  PRO A CA  
535  C C   . PRO A 75  ? 0.18351 0.15539 0.29178 -0.02301 -0.01028 -0.00834 82  PRO A C   
536  O O   . PRO A 75  ? 0.21785 0.18393 0.33183 -0.03819 -0.02163 -0.00709 82  PRO A O   
537  C CB  . PRO A 75  ? 0.18202 0.20667 0.31897 -0.02058 0.00017  0.00010  82  PRO A CB  
538  C CG  . PRO A 75  ? 0.20857 0.24561 0.36025 -0.02648 -0.00201 0.00257  82  PRO A CG  
539  C CD  . PRO A 75  ? 0.19717 0.23304 0.34504 -0.02705 -0.00853 -0.00497 82  PRO A CD  
540  N N   . ASN A 76  ? 0.21101 0.15716 0.29663 -0.01041 -0.00322 -0.00714 83  ASN A N   
541  C CA  . ASN A 76  ? 0.26759 0.16024 0.32076 -0.01314 -0.00799 -0.00863 83  ASN A CA  
542  C C   . ASN A 76  ? 0.27562 0.15986 0.32192 0.00161  0.00521  0.00022  83  ASN A C   
543  O O   . ASN A 76  ? 0.28701 0.16882 0.31905 0.02540  0.01924  0.00507  83  ASN A O   
544  C CB  . ASN A 76  ? 0.33370 0.17849 0.34133 -0.00452 -0.01062 -0.01787 83  ASN A CB  
545  C CG  . ASN A 76  ? 0.42708 0.19511 0.38208 -0.01233 -0.02114 -0.02146 83  ASN A CG  
546  O OD1 . ASN A 76  ? 0.45150 0.18997 0.38830 -0.00511 -0.01412 -0.01626 83  ASN A OD1 
547  N ND2 . ASN A 76  ? 0.51162 0.24193 0.43706 -0.02969 -0.04075 -0.02915 83  ASN A ND2 
548  N N   . LYS A 77  ? 0.30969 0.20435 0.35308 -0.02450 -0.00862 0.06153  84  LYS A N   
549  C CA  . LYS A 77  ? 0.30839 0.18906 0.34089 -0.00867 0.00199  0.06873  84  LYS A CA  
550  C C   . LYS A 77  ? 0.38273 0.19653 0.38164 -0.01095 0.00165  0.06594  84  LYS A C   
551  O O   . LYS A 77  ? 0.44432 0.24178 0.42871 0.01080  0.01328  0.06881  84  LYS A O   
552  C CB  . LYS A 77  ? 0.33424 0.24207 0.38820 -0.01228 0.00711  0.09145  84  LYS A CB  
553  C CG  . LYS A 77  ? 0.36168 0.32327 0.43341 0.00000  0.01500  0.09455  84  LYS A CG  
554  C CD  . LYS A 77  ? 0.35505 0.34015 0.44221 0.00096  0.02435  0.11930  84  LYS A CD  
555  C CE  . LYS A 77  ? 0.37605 0.40187 0.46804 0.01607  0.03606  0.12202  84  LYS A CE  
556  N NZ  . LYS A 77  ? 0.42980 0.47720 0.54180 0.00896  0.03444  0.12329  84  LYS A NZ  
557  N N   . GLN A 78  ? 0.43099 0.20228 0.41251 -0.03661 -0.01124 0.06218  85  GLN A N   
558  C CA  . GLN A 78  ? 0.52880 0.21723 0.46159 -0.03910 -0.01015 0.05691  85  GLN A CA  
559  C C   . GLN A 78  ? 0.51147 0.17438 0.41422 -0.01189 0.00095  0.03905  85  GLN A C   
560  O O   . GLN A 78  ? 0.62274 0.23674 0.49292 0.01008  0.01601  0.04035  85  GLN A O   
561  C CB  . GLN A 78  ? 0.63798 0.28199 0.55023 -0.07996 -0.03115 0.05707  85  GLN A CB  
562  C CG  . GLN A 78  ? 0.87865 0.51308 0.79824 -0.10239 -0.03575 0.07662  85  GLN A CG  
563  C CD  . GLN A 78  ? 0.98516 0.68864 0.95908 -0.10180 -0.03253 0.10223  85  GLN A CD  
564  O OE1 . GLN A 78  ? 0.91533 0.68897 0.92907 -0.09899 -0.03378 0.10474  85  GLN A OE1 
565  N NE2 . GLN A 78  ? 0.91389 0.60311 0.88837 -0.09884 -0.02385 0.12013  85  GLN A NE2 
566  N N   . ASP A 79  ? 0.46777 0.16474 0.38216 -0.01057 -0.00392 0.02590  86  ASP A N   
567  C CA  . ASP A 79  ? 0.48708 0.17401 0.38151 0.01472  0.00706  0.01312  86  ASP A CA  
568  C C   . ASP A 79  ? 0.43457 0.18426 0.36118 0.04195  0.01863  0.01988  86  ASP A C   
569  O O   . ASP A 79  ? 0.44092 0.19242 0.35862 0.06519  0.02965  0.01731  86  ASP A O   
570  C CB  . ASP A 79  ? 0.54204 0.23619 0.43327 0.00025  -0.00516 -0.00202 86  ASP A CB  
571  C CG  . ASP A 79  ? 0.63279 0.26985 0.48731 -0.02976 -0.02048 -0.00837 86  ASP A CG  
572  O OD1 . ASP A 79  ? 0.71900 0.31508 0.54839 -0.03502 -0.01829 -0.00478 86  ASP A OD1 
573  O OD2 . ASP A 79  ? 0.67467 0.33046 0.53453 -0.04731 -0.03443 -0.01531 86  ASP A OD2 
574  N N   . ARG A 80  ? 0.37329 0.17335 0.33374 0.03834  0.01598  0.03075  87  ARG A N   
575  C CA  . ARG A 80  ? 0.30822 0.16735 0.29305 0.05438  0.02016  0.03603  87  ARG A CA  
576  C C   . ARG A 80  ? 0.27529 0.16302 0.26768 0.05466  0.01563  0.02322  87  ARG A C   
577  O O   . ARG A 80  ? 0.29742 0.20920 0.29400 0.07053  0.02049  0.02637  87  ARG A O   
578  C CB  . ARG A 80  ? 0.35102 0.21128 0.33143 0.08024  0.03327  0.05134  87  ARG A CB  
579  C CG  . ARG A 80  ? 0.31116 0.23110 0.31463 0.08507  0.03099  0.06301  87  ARG A CG  
580  C CD  . ARG A 80  ? 0.51413 0.45915 0.52223 0.10944  0.03924  0.08056  87  ARG A CD  
581  N NE  . ARG A 80  ? 0.61948 0.52634 0.61362 0.12845  0.05386  0.09627  87  ARG A NE  
582  C CZ  . ARG A 80  ? 0.64009 0.54973 0.63248 0.15724  0.06811  0.11351  87  ARG A CZ  
583  N NH1 . ARG A 80  ? 0.48556 0.44288 0.49424 0.16526  0.06741  0.11797  87  ARG A NH1 
584  N NH2 . ARG A 80  ? 0.64334 0.51673 0.61795 0.16779  0.08152  0.12224  87  ARG A NH2 
585  N N   . THR A 81  ? 0.26107 0.15018 0.25808 0.03608  0.00585  0.01263  88  THR A N   
586  C CA  . THR A 81  ? 0.24631 0.15741 0.24901 0.03483  0.00171  0.00126  88  THR A CA  
587  C C   . THR A 81  ? 0.25259 0.19499 0.27365 0.02315  -0.00419 -0.00004 88  THR A C   
588  O O   . THR A 81  ? 0.22260 0.16536 0.25269 0.01227  -0.00657 0.00680  88  THR A O   
589  C CB  . THR A 81  ? 0.27273 0.14794 0.25493 0.02899  -0.00156 -0.01023 88  THR A CB  
590  O OG1 . THR A 81  ? 0.31334 0.16420 0.29027 0.00709  -0.01173 -0.01008 88  THR A OG1 
591  C CG2 . THR A 81  ? 0.30349 0.14021 0.25729 0.04812  0.01042  -0.00963 88  THR A CG2 
592  N N   . LEU A 82  ? 0.19640 0.16373 0.22144 0.02632  -0.00505 -0.00602 89  LEU A N   
593  C CA  . LEU A 82  ? 0.17717 0.16060 0.20908 0.01971  -0.00695 -0.00959 89  LEU A CA  
594  C C   . LEU A 82  ? 0.19366 0.17487 0.22382 0.01651  -0.01102 -0.02018 89  LEU A C   
595  O O   . LEU A 82  ? 0.19512 0.18108 0.22038 0.02119  -0.01133 -0.02402 89  LEU A O   
596  C CB  . LEU A 82  ? 0.18060 0.18139 0.20541 0.02407  -0.00438 -0.00806 89  LEU A CB  
597  C CG  . LEU A 82  ? 0.17635 0.17912 0.19484 0.02243  -0.00145 -0.01279 89  LEU A CG  
598  C CD1 . LEU A 82  ? 0.19292 0.19925 0.22482 0.02362  0.00564  -0.00225 89  LEU A CD1 
599  C CD2 . LEU A 82  ? 0.21770 0.22042 0.21095 0.02373  -0.00074 -0.01484 89  LEU A CD2 
600  N N   . THR A 83  ? 0.17667 0.15554 0.21362 0.00837  -0.01435 -0.02078 90  THR A N   
601  C CA  . THR A 83  ? 0.17672 0.15288 0.21124 0.00503  -0.01858 -0.02870 90  THR A CA  
602  C C   . THR A 83  ? 0.18561 0.17692 0.22709 0.00617  -0.01557 -0.02801 90  THR A C   
603  O O   . THR A 83  ? 0.18017 0.18205 0.23280 0.00698  -0.01139 -0.01785 90  THR A O   
604  C CB  . THR A 83  ? 0.20272 0.16108 0.23375 -0.00667 -0.02699 -0.02762 90  THR A CB  
605  O OG1 . THR A 83  ? 0.23460 0.16161 0.24555 -0.00536 -0.02667 -0.03005 90  THR A OG1 
606  C CG2 . THR A 83  ? 0.25458 0.21172 0.28028 -0.00963 -0.03164 -0.03437 90  THR A CG2 
607  N N   . ILE A 84  ? 0.17356 0.16441 0.20724 0.00796  -0.01547 -0.03597 91  ILE A N   
608  C CA  . ILE A 84  ? 0.16633 0.15812 0.19759 0.01043  -0.01091 -0.03644 91  ILE A CA  
609  C C   . ILE A 84  ? 0.18136 0.17395 0.21839 0.00685  -0.01564 -0.03757 91  ILE A C   
610  O O   . ILE A 84  ? 0.19643 0.18478 0.22671 0.00455  -0.01944 -0.04429 91  ILE A O   
611  C CB  . ILE A 84  ? 0.19136 0.17418 0.20225 0.01023  -0.00939 -0.04342 91  ILE A CB  
612  C CG1 . ILE A 84  ? 0.27097 0.25216 0.26943 0.01205  -0.00689 -0.04138 91  ILE A CG1 
613  C CG2 . ILE A 84  ? 0.21469 0.18213 0.21242 0.01353  -0.00270 -0.04514 91  ILE A CG2 
614  C CD1 . ILE A 84  ? 0.31438 0.30807 0.31768 0.00941  -0.01344 -0.03907 91  ILE A CD1 
615  N N   . VAL A 85  ? 0.16051 0.16330 0.21139 0.00729  -0.01488 -0.02730 92  VAL A N   
616  C CA  . VAL A 85  ? 0.15448 0.16255 0.21122 0.00231  -0.02181 -0.02440 92  VAL A CA  
617  C C   . VAL A 85  ? 0.16974 0.18036 0.22804 0.01259  -0.01225 -0.01906 92  VAL A C   
618  O O   . VAL A 85  ? 0.18041 0.19603 0.24403 0.02391  -0.00030 -0.00856 92  VAL A O   
619  C CB  . VAL A 85  ? 0.17996 0.20314 0.25320 -0.00899 -0.03227 -0.01048 92  VAL A CB  
620  C CG1 . VAL A 85  ? 0.22778 0.25428 0.29922 -0.01802 -0.04379 -0.00798 92  VAL A CG1 
621  C CG2 . VAL A 85  ? 0.20052 0.20853 0.26498 -0.01890 -0.03927 -0.01466 92  VAL A CG2 
622  N N   . ASP A 86  ? 0.16828 0.17249 0.21927 0.01125  -0.01486 -0.02408 93  ASP A N   
623  C CA  . ASP A 86  ? 0.15720 0.15927 0.20836 0.02151  -0.00559 -0.01635 93  ASP A CA  
624  C C   . ASP A 86  ? 0.16851 0.18339 0.22770 0.01641  -0.01476 -0.01020 93  ASP A C   
625  O O   . ASP A 86  ? 0.17102 0.18425 0.22313 0.00530  -0.02641 -0.01811 93  ASP A O   
626  C CB  . ASP A 86  ? 0.19442 0.16507 0.21891 0.02494  0.00304  -0.02783 93  ASP A CB  
627  C CG  . ASP A 86  ? 0.24652 0.21167 0.26252 0.01341  -0.00578 -0.03825 93  ASP A CG  
628  O OD1 . ASP A 86  ? 0.22382 0.19432 0.24421 0.01253  -0.00864 -0.03466 93  ASP A OD1 
629  O OD2 . ASP A 86  ? 0.23123 0.19151 0.23797 0.00596  -0.00941 -0.04654 93  ASP A OD2 
630  N N   . THR A 87  ? 0.14444 0.17002 0.21455 0.02714  -0.00763 0.00592  94  THR A N   
631  C CA  . THR A 87  ? 0.14503 0.18484 0.22145 0.02355  -0.01607 0.01510  94  THR A CA  
632  C C   . THR A 87  ? 0.18222 0.19829 0.24206 0.03170  -0.00638 0.01039  94  THR A C   
633  O O   . THR A 87  ? 0.16984 0.19475 0.23694 0.04036  -0.00253 0.02573  94  THR A O   
634  C CB  . THR A 87  ? 0.14518 0.22437 0.25199 0.02808  -0.01786 0.04394  94  THR A CB  
635  O OG1 . THR A 87  ? 0.15699 0.23617 0.27200 0.05172  0.00473  0.05788  94  THR A OG1 
636  C CG2 . THR A 87  ? 0.15545 0.25751 0.27666 0.00959  -0.03477 0.04979  94  THR A CG2 
637  N N   . GLY A 88  ? 0.17140 0.15879 0.20977 0.02736  -0.00333 -0.00775 95  GLY A N   
638  C CA  . GLY A 88  ? 0.20697 0.16871 0.22779 0.02837  0.00297  -0.01138 95  GLY A CA  
639  C C   . GLY A 88  ? 0.20064 0.17329 0.22222 0.02037  -0.00610 -0.01128 95  GLY A C   
640  O O   . GLY A 88  ? 0.18076 0.17599 0.21071 0.01670  -0.01641 -0.00689 95  GLY A O   
641  N N   . ILE A 89  ? 0.20444 0.15718 0.21211 0.01568  -0.00268 -0.01524 96  ILE A N   
642  C CA  . ILE A 89  ? 0.20818 0.17025 0.21513 0.01163  -0.00665 -0.01123 96  ILE A CA  
643  C C   . ILE A 89  ? 0.20341 0.18272 0.20978 0.00527  -0.01459 -0.01835 96  ILE A C   
644  O O   . ILE A 89  ? 0.21242 0.20040 0.21295 0.00580  -0.01726 -0.01454 96  ILE A O   
645  C CB  . ILE A 89  ? 0.21639 0.15279 0.21053 0.00625  -0.00036 -0.00937 96  ILE A CB  
646  C CG1 . ILE A 89  ? 0.25920 0.20604 0.25445 0.00626  -0.00079 0.00061  96  ILE A CG1 
647  C CG2 . ILE A 89  ? 0.22954 0.15936 0.21749 -0.00898 -0.00409 -0.01828 96  ILE A CG2 
648  C CD1 . ILE A 89  ? 0.28782 0.20433 0.27091 0.00228  0.00653  0.00781  96  ILE A CD1 
649  N N   . GLY A 90  ? 0.20466 0.18520 0.21197 0.00192  -0.01636 -0.02741 97  GLY A N   
650  C CA  . GLY A 90  ? 0.19991 0.18930 0.20178 0.00164  -0.01879 -0.03200 97  GLY A CA  
651  C C   . GLY A 90  ? 0.19377 0.19107 0.19581 -0.00018 -0.01352 -0.02747 97  GLY A C   
652  O O   . GLY A 90  ? 0.22310 0.21795 0.22962 -0.00739 -0.01184 -0.02179 97  GLY A O   
653  N N   . MET A 91  ? 0.18189 0.18672 0.17667 0.00669  -0.00985 -0.02748 98  MET A N   
654  C CA  . MET A 91  ? 0.17680 0.20085 0.17813 0.00917  -0.00176 -0.01650 98  MET A CA  
655  C C   . MET A 91  ? 0.19965 0.22051 0.17915 0.02378  0.00717  -0.01373 98  MET A C   
656  O O   . MET A 91  ? 0.23793 0.23708 0.19210 0.03150  0.00686  -0.02350 98  MET A O   
657  C CB  . MET A 91  ? 0.19643 0.23581 0.21040 0.00987  -0.00025 -0.01408 98  MET A CB  
658  C CG  . MET A 91  ? 0.19598 0.23776 0.22353 -0.00748 -0.00927 -0.01415 98  MET A CG  
659  S SD  . MET A 91  ? 0.19070 0.25938 0.23416 -0.00979 -0.01106 -0.00588 98  MET A SD  
660  C CE  . MET A 91  ? 0.23201 0.27675 0.26242 0.00140  -0.01105 -0.02255 98  MET A CE  
661  N N   . THR A 92  ? 0.20489 0.24211 0.18847 0.02641  0.01526  0.00026  99  THR A N   
662  C CA  . THR A 92  ? 0.22414 0.25751 0.18153 0.04475  0.02887  0.00544  99  THR A CA  
663  C C   . THR A 92  ? 0.23227 0.27900 0.19200 0.06174  0.04364  0.01366  99  THR A C   
664  O O   . THR A 92  ? 0.21468 0.28411 0.20382 0.05579  0.04072  0.01913  99  THR A O   
665  C CB  . THR A 92  ? 0.24011 0.29277 0.20504 0.04434  0.03591  0.02269  99  THR A CB  
666  O OG1 . THR A 92  ? 0.22414 0.31479 0.22696 0.03625  0.03925  0.04180  99  THR A OG1 
667  C CG2 . THR A 92  ? 0.30448 0.34448 0.26953 0.03046  0.02368  0.01878  99  THR A CG2 
668  N N   . LYS A 93  ? 0.26574 0.20433 0.23790 0.06239  -0.03678 -0.03916 100 LYS A N   
669  C CA  . LYS A 93  ? 0.24510 0.20239 0.22012 0.05378  -0.01513 -0.03168 100 LYS A CA  
670  C C   . LYS A 93  ? 0.26927 0.22555 0.23935 0.04194  -0.00443 -0.01767 100 LYS A C   
671  O O   . LYS A 93  ? 0.23038 0.20404 0.22282 0.03713  0.00585  -0.01731 100 LYS A O   
672  C CB  . LYS A 93  ? 0.27809 0.23534 0.23054 0.05649  -0.01114 -0.03327 100 LYS A CB  
673  C CG  . LYS A 93  ? 0.28483 0.26733 0.25689 0.05356  0.00430  -0.03768 100 LYS A CG  
674  C CD  . LYS A 93  ? 0.28792 0.27908 0.24262 0.05569  0.00992  -0.04664 100 LYS A CD  
675  C CE  . LYS A 93  ? 0.33448 0.35299 0.32345 0.05851  0.01717  -0.06054 100 LYS A CE  
676  N NZ  . LYS A 93  ? 0.35119 0.39180 0.32935 0.05536  0.02984  -0.07572 100 LYS A NZ  
677  N N   . ALA A 94  ? 0.28275 0.21320 0.22085 0.03565  -0.01029 -0.00621 101 ALA A N   
678  C CA  . ALA A 94  ? 0.32914 0.25842 0.26350 0.02090  0.00070  0.00565  101 ALA A CA  
679  C C   . ALA A 94  ? 0.29102 0.22951 0.26006 0.02328  -0.00268 0.00342  101 ALA A C   
680  O O   . ALA A 94  ? 0.27885 0.23321 0.26494 0.01578  0.00978  0.00613  101 ALA A O   
681  C CB  . ALA A 94  ? 0.35869 0.24652 0.24232 0.00805  -0.00913 0.02083  101 ALA A CB  
682  N N   . ASP A 95  ? 0.26596 0.19842 0.24872 0.03344  -0.02018 -0.00662 102 ASP A N   
683  C CA  . ASP A 95  ? 0.23133 0.17978 0.24572 0.03265  -0.02062 -0.01489 102 ASP A CA  
684  C C   . ASP A 95  ? 0.19648 0.17082 0.22751 0.02686  -0.00498 -0.01789 102 ASP A C   
685  O O   . ASP A 95  ? 0.21656 0.19838 0.25782 0.01968  0.00050  -0.01436 102 ASP A O   
686  C CB  . ASP A 95  ? 0.26311 0.21418 0.29822 0.04327  -0.03927 -0.03734 102 ASP A CB  
687  C CG  . ASP A 95  ? 0.33796 0.25317 0.36221 0.05202  -0.06791 -0.03757 102 ASP A CG  
688  O OD1 . ASP A 95  ? 0.36029 0.24962 0.36384 0.04404  -0.07097 -0.01867 102 ASP A OD1 
689  O OD2 . ASP A 95  ? 0.36055 0.27044 0.39843 0.06643  -0.09119 -0.05911 102 ASP A OD2 
690  N N   . LEU A 96  ? 0.19936 0.18096 0.22994 0.02936  -0.00230 -0.02419 103 LEU A N   
691  C CA  . LEU A 96  ? 0.22838 0.21921 0.26550 0.02151  0.00424  -0.02455 103 LEU A CA  
692  C C   . LEU A 96  ? 0.22208 0.21151 0.26049 0.01994  0.00821  -0.01429 103 LEU A C   
693  O O   . LEU A 96  ? 0.20026 0.18831 0.24363 0.01300  0.00614  -0.01164 103 LEU A O   
694  C CB  . LEU A 96  ? 0.23375 0.22526 0.26857 0.02458  0.00291  -0.03144 103 LEU A CB  
695  C CG  . LEU A 96  ? 0.19809 0.19882 0.24129 0.02114  0.00085  -0.04884 103 LEU A CG  
696  C CD1 . LEU A 96  ? 0.20834 0.20666 0.24950 0.02489  -0.00119 -0.05353 103 LEU A CD1 
697  C CD2 . LEU A 96  ? 0.21949 0.22961 0.26576 0.00050  0.00717  -0.05517 103 LEU A CD2 
698  N N   . ILE A 97  ? 0.20432 0.19574 0.23827 0.02478  0.01314  -0.01244 104 ILE A N   
699  C CA  . ILE A 97  ? 0.20418 0.20626 0.25204 0.02342  0.01842  -0.01392 104 ILE A CA  
700  C C   . ILE A 97  ? 0.20105 0.20370 0.25659 0.01643  0.02096  -0.00807 104 ILE A C   
701  O O   . ILE A 97  ? 0.21814 0.22729 0.29378 0.01628  0.01774  -0.01209 104 ILE A O   
702  C CB  . ILE A 97  ? 0.21738 0.23161 0.25830 0.02361  0.02939  -0.02046 104 ILE A CB  
703  C CG1 . ILE A 97  ? 0.23212 0.24863 0.27272 0.03325  0.02416  -0.03012 104 ILE A CG1 
704  C CG2 . ILE A 97  ? 0.21009 0.24824 0.27623 0.01920  0.03887  -0.03218 104 ILE A CG2 
705  C CD1 . ILE A 97  ? 0.27571 0.30159 0.29687 0.03171  0.03477  -0.03693 104 ILE A CD1 
706  N N   . ASN A 98  ? 0.19342 0.18537 0.23511 0.01225  0.02144  -0.00052 105 ASN A N   
707  C CA  . ASN A 98  ? 0.22615 0.21574 0.27568 0.00546  0.02184  0.00461  105 ASN A CA  
708  C C   . ASN A 98  ? 0.20479 0.19443 0.26525 0.00674  0.01276  0.00173  105 ASN A C   
709  O O   . ASN A 98  ? 0.23057 0.21476 0.29251 0.00613  0.00665  0.00060  105 ASN A O   
710  C CB  . ASN A 98  ? 0.26073 0.22925 0.28681 -0.00101 0.01987  0.01376  105 ASN A CB  
711  C CG  . ASN A 98  ? 0.56181 0.52620 0.59472 -0.01235 0.02267  0.01963  105 ASN A CG  
712  O OD1 . ASN A 98  ? 0.52869 0.51303 0.58805 -0.01435 0.02942  0.01413  105 ASN A OD1 
713  N ND2 . ASN A 98  ? 0.55417 0.48732 0.56269 -0.01976 0.01291  0.03002  105 ASN A ND2 
714  N N   . ASN A 99  ? 0.19976 0.19328 0.26511 0.00668  0.00955  -0.00172 106 ASN A N   
715  C CA  . ASN A 99  ? 0.19229 0.18334 0.25515 -0.00039 0.00313  -0.00377 106 ASN A CA  
716  C C   . ASN A 99  ? 0.22035 0.21746 0.27767 -0.00505 0.00447  -0.01298 106 ASN A C   
717  O O   . ASN A 99  ? 0.19928 0.20450 0.26179 -0.01114 0.00372  -0.02071 106 ASN A O   
718  C CB  . ASN A 99  ? 0.17608 0.16901 0.25182 -0.00252 0.00040  -0.00233 106 ASN A CB  
719  C CG  . ASN A 99  ? 0.16796 0.16260 0.26058 0.00222  -0.00279 -0.00302 106 ASN A CG  
720  O OD1 . ASN A 99  ? 0.21157 0.19757 0.30266 0.00543  -0.01378 -0.00565 106 ASN A OD1 
721  N ND2 . ASN A 99  ? 0.23074 0.23600 0.34256 0.00164  0.00433  -0.00433 106 ASN A ND2 
722  N N   . LEU A 100 ? 0.17231 0.17045 0.22466 -0.00176 0.00594  -0.01786 107 LEU A N   
723  C CA  . LEU A 100 ? 0.16841 0.18013 0.22598 -0.00566 0.00669  -0.03593 107 LEU A CA  
724  C C   . LEU A 100 ? 0.18480 0.20417 0.26196 0.00142  -0.00022 -0.04816 107 LEU A C   
725  O O   . LEU A 100 ? 0.19646 0.23714 0.28902 -0.00547 0.00054  -0.07016 107 LEU A O   
726  C CB  . LEU A 100 ? 0.20250 0.22121 0.24680 -0.02750 0.01288  -0.04359 107 LEU A CB  
727  C CG  . LEU A 100 ? 0.28540 0.28241 0.30730 -0.03351 0.01002  -0.03003 107 LEU A CG  
728  C CD1 . LEU A 100 ? 0.26163 0.23550 0.26647 -0.03950 0.00036  -0.01467 107 LEU A CD1 
729  C CD2 . LEU A 100 ? 0.40618 0.40697 0.41383 -0.05418 0.01626  -0.04135 107 LEU A CD2 
730  N N   . GLY A 101 ? 0.18851 0.18916 0.26380 0.01264  -0.00831 -0.03627 108 GLY A N   
731  C CA  . GLY A 101 ? 0.20636 0.19890 0.29551 0.02072  -0.02440 -0.04522 108 GLY A CA  
732  C C   . GLY A 101 ? 0.23884 0.23840 0.34349 0.01603  -0.02568 -0.04831 108 GLY A C   
733  O O   . GLY A 101 ? 0.28440 0.28231 0.40968 0.02345  -0.04257 -0.06426 108 GLY A O   
734  N N   . THR A 102 ? 0.19432 0.19950 0.29250 0.00611  -0.01320 -0.03645 109 THR A N   
735  C CA  . THR A 102 ? 0.17885 0.19109 0.29030 0.00169  -0.01498 -0.04005 109 THR A CA  
736  C C   . THR A 102 ? 0.20090 0.19526 0.31067 0.00161  -0.01502 -0.02034 109 THR A C   
737  O O   . THR A 102 ? 0.24595 0.23011 0.34259 0.00064  -0.00823 -0.00620 109 THR A O   
738  C CB  . THR A 102 ? 0.19806 0.22572 0.29921 -0.01217 -0.00552 -0.04418 109 THR A CB  
739  O OG1 . THR A 102 ? 0.21915 0.23212 0.30348 -0.01417 -0.00244 -0.02502 109 THR A OG1 
740  C CG2 . THR A 102 ? 0.24355 0.29039 0.33864 -0.02243 0.00148  -0.06336 109 THR A CG2 
741  N N   . ILE A 103 ? 0.17076 0.16646 0.29715 0.00043  -0.02113 -0.02414 110 ILE A N   
742  C CA  . ILE A 103 ? 0.17314 0.16027 0.30459 -0.00429 -0.01798 -0.01088 110 ILE A CA  
743  C C   . ILE A 103 ? 0.16287 0.16508 0.29928 -0.00748 -0.01351 -0.01339 110 ILE A C   
744  O O   . ILE A 103 ? 0.16166 0.16848 0.31339 -0.00876 -0.01873 -0.01831 110 ILE A O   
745  C CB  . ILE A 103 ? 0.25036 0.22148 0.39600 -0.00437 -0.03159 -0.01176 110 ILE A CB  
746  C CG1 . ILE A 103 ? 0.22133 0.20933 0.39006 0.00162  -0.04327 -0.03441 110 ILE A CG1 
747  C CG2 . ILE A 103 ? 0.25244 0.19002 0.37951 -0.00339 -0.04412 -0.00340 110 ILE A CG2 
748  C CD1 . ILE A 103 ? 0.27577 0.24878 0.46589 0.00298  -0.06000 -0.03767 110 ILE A CD1 
749  N N   . ALA A 104 ? 0.24076 0.12681 0.28913 0.02104  0.03158  0.02780  111 ALA A N   
750  C CA  . ALA A 104 ? 0.21048 0.12002 0.27780 0.03340  0.02930  0.03169  111 ALA A CA  
751  C C   . ALA A 104 ? 0.19213 0.15765 0.29717 0.02181  0.04419  0.01874  111 ALA A C   
752  O O   . ALA A 104 ? 0.21123 0.24393 0.32378 0.01346  0.03599  0.00086  111 ALA A O   
753  C CB  . ALA A 104 ? 0.25183 0.18509 0.28549 0.04636  0.00330  0.03867  111 ALA A CB  
754  N N   . LYS A 105 ? 0.20617 0.17260 0.31670 0.01122  0.05754  0.01868  112 LYS A N   
755  C CA  . LYS A 105 ? 0.22326 0.27863 0.35434 -0.01144 0.06346  -0.00414 112 LYS A CA  
756  C C   . LYS A 105 ? 0.26424 0.33959 0.40953 -0.05453 0.07827  -0.03851 112 LYS A C   
757  O O   . LYS A 105 ? 0.21978 0.37289 0.37747 -0.06461 0.06978  -0.05780 112 LYS A O   
758  C CB  . LYS A 105 ? 0.20143 0.25374 0.33520 -0.01789 0.07831  0.00191  112 LYS A CB  
759  C CG  . LYS A 105 ? 0.36279 0.52358 0.51924 -0.02419 0.07686  -0.01282 112 LYS A CG  
760  C CD  . LYS A 105 ? 0.31271 0.47605 0.47620 -0.04735 0.10061  -0.01648 112 LYS A CD  
761  C CE  . LYS A 105 ? 0.35399 0.62420 0.54945 -0.08057 0.10940  -0.04644 112 LYS A CE  
762  N NZ  . LYS A 105 ? 0.42879 0.75976 0.63712 -0.07135 0.11518  -0.04265 112 LYS A NZ  
763  N N   . SER A 106 ? 0.25083 0.25155 0.39063 -0.07983 0.09862  -0.04674 113 SER A N   
764  C CA  . SER A 106 ? 0.27310 0.28182 0.42008 -0.12057 0.11216  -0.07989 113 SER A CA  
765  C C   . SER A 106 ? 0.26344 0.27592 0.40709 -0.11191 0.10144  -0.08905 113 SER A C   
766  O O   . SER A 106 ? 0.28235 0.33932 0.43295 -0.13869 0.10426  -0.11704 113 SER A O   
767  C CB  . SER A 106 ? 0.37662 0.30296 0.49881 -0.13319 0.12510  -0.08102 113 SER A CB  
768  O OG  . SER A 106 ? 0.40438 0.26634 0.50213 -0.09686 0.11208  -0.05729 113 SER A OG  
769  N N   . GLY A 107 ? 0.25921 0.22692 0.39091 -0.07694 0.08949  -0.06627 114 GLY A N   
770  C CA  . GLY A 107 ? 0.24954 0.22707 0.37712 -0.06933 0.08039  -0.07406 114 GLY A CA  
771  C C   . GLY A 107 ? 0.25434 0.32486 0.38443 -0.06477 0.06150  -0.07931 114 GLY A C   
772  O O   . GLY A 107 ? 0.21966 0.32339 0.34954 -0.08155 0.06090  -0.10216 114 GLY A O   
773  N N   . THR A 108 ? 0.18599 0.29707 0.31551 -0.04124 0.04482  -0.05906 115 THR A N   
774  C CA  . THR A 108 ? 0.19560 0.39280 0.32502 -0.03373 0.02301  -0.06356 115 THR A CA  
775  C C   . THR A 108 ? 0.18425 0.45066 0.33289 -0.07087 0.03111  -0.09696 115 THR A C   
776  O O   . THR A 108 ? 0.18589 0.50349 0.33198 -0.08030 0.01989  -0.11361 115 THR A O   
777  C CB  . THR A 108 ? 0.14970 0.37050 0.27392 0.00122  0.00388  -0.03701 115 THR A CB  
778  O OG1 . THR A 108 ? 0.17643 0.33161 0.27788 0.03388  -0.00688 -0.00549 115 THR A OG1 
779  C CG2 . THR A 108 ? 0.17123 0.47908 0.29386 0.01144  -0.02167 -0.04282 115 THR A CG2 
780  N N   . LYS A 109 ? 0.20021 0.46808 0.36563 -0.09466 0.05009  -0.10675 116 LYS A N   
781  C CA  . LYS A 109 ? 0.22001 0.55125 0.40396 -0.13527 0.05909  -0.13834 116 LYS A CA  
782  C C   . LYS A 109 ? 0.27529 0.58168 0.44487 -0.16003 0.06576  -0.16204 116 LYS A C   
783  O O   . LYS A 109 ? 0.26874 0.62336 0.43000 -0.16881 0.05640  -0.17742 116 LYS A O   
784  C CB  . LYS A 109 ? 0.24701 0.55191 0.43612 -0.15667 0.08029  -0.13987 116 LYS A CB  
785  C CG  . LYS A 109 ? 0.32070 0.65494 0.50568 -0.19023 0.08732  -0.16380 116 LYS A CG  
786  C CD  . LYS A 109 ? 0.32428 0.62024 0.50701 -0.21196 0.10776  -0.16308 116 LYS A CD  
787  C CE  . LYS A 109 ? 0.45482 0.79743 0.63733 -0.24270 0.11249  -0.18362 116 LYS A CE  
788  N NZ  . LYS A 109 ? 0.60186 1.01786 0.78871 -0.24074 0.09574  -0.19756 116 LYS A NZ  
789  N N   . ALA A 110 ? 0.26655 0.49139 0.42912 -0.16764 0.08220  -0.16421 117 ALA A N   
790  C CA  . ALA A 110 ? 0.31405 0.51047 0.45912 -0.18445 0.08982  -0.18623 117 ALA A CA  
791  C C   . ALA A 110 ? 0.28110 0.51594 0.42037 -0.17172 0.07254  -0.18919 117 ALA A C   
792  O O   . ALA A 110 ? 0.30467 0.56195 0.43012 -0.18588 0.07252  -0.20831 117 ALA A O   
793  C CB  . ALA A 110 ? 0.32794 0.42340 0.46086 -0.18173 0.10734  -0.18277 117 ALA A CB  
794  N N   . PHE A 111 ? 0.25049 0.47821 0.38406 -0.13466 0.05669  -0.16129 118 PHE A N   
795  C CA  . PHE A 111 ? 0.23215 0.48433 0.34830 -0.11880 0.03874  -0.15765 118 PHE A CA  
796  C C   . PHE A 111 ? 0.24755 0.58973 0.36319 -0.12702 0.01887  -0.16904 118 PHE A C   
797  O O   . PHE A 111 ? 0.25319 0.60897 0.34891 -0.13471 0.01617  -0.18113 118 PHE A O   
798  C CB  . PHE A 111 ? 0.20300 0.42296 0.30712 -0.07741 0.02398  -0.12066 118 PHE A CB  
799  C CG  . PHE A 111 ? 0.19396 0.43035 0.27459 -0.06244 0.00539  -0.11269 118 PHE A CG  
800  C CD1 . PHE A 111 ? 0.21438 0.45014 0.28531 -0.08113 0.01396  -0.13529 118 PHE A CD1 
801  C CD2 . PHE A 111 ? 0.22503 0.47145 0.28863 -0.03000 -0.02035 -0.08193 118 PHE A CD2 
802  C CE1 . PHE A 111 ? 0.21174 0.46229 0.25741 -0.07061 -0.00171 -0.12729 118 PHE A CE1 
803  C CE2 . PHE A 111 ? 0.24830 0.50411 0.28392 -0.01978 -0.03824 -0.07286 118 PHE A CE2 
804  C CZ  . PHE A 111 ? 0.25504 0.51467 0.28217 -0.04147 -0.02810 -0.09543 118 PHE A CZ  
805  N N   . MET A 112 ? 0.23151 0.61251 0.35537 -0.11423 0.00836  -0.15641 119 MET A N   
806  C CA  . MET A 112 ? 0.26594 0.70100 0.37630 -0.10842 -0.00693 -0.15746 119 MET A CA  
807  C C   . MET A 112 ? 0.36555 0.82159 0.47866 -0.14344 0.00761  -0.18587 119 MET A C   
808  O O   . MET A 112 ? 0.33194 0.82194 0.43254 -0.14526 -0.00143 -0.19171 119 MET A O   
809  C CB  . MET A 112 ? 0.38015 0.84314 0.49683 -0.08263 -0.01984 -0.13818 119 MET A CB  
810  C CG  . MET A 112 ? 0.19541 0.63214 0.29008 -0.04104 -0.04008 -0.10585 119 MET A CG  
811  S SD  . MET A 112 ? 0.56421 1.01345 0.66110 -0.01123 -0.04887 -0.08596 119 MET A SD  
812  C CE  . MET A 112 ? 0.26617 0.63634 0.33131 0.02638  -0.06108 -0.04847 119 MET A CE  
813  N N   . GLU A 113 ? 0.29816 0.72606 0.42423 -0.17075 0.03035  -0.20109 120 GLU A N   
814  C CA  . GLU A 113 ? 0.34808 0.78281 0.46933 -0.20371 0.04435  -0.22621 120 GLU A CA  
815  C C   . GLU A 113 ? 0.37514 0.78190 0.47817 -0.21317 0.05087  -0.23954 120 GLU A C   
816  O O   . GLU A 113 ? 0.43801 0.86099 0.53245 -0.23497 0.05648  -0.25769 120 GLU A O   
817  C CB  . GLU A 113 ? 0.41737 0.81402 0.54723 -0.22830 0.06666  -0.23512 120 GLU A CB  
818  C CG  . GLU A 113 ? 0.47724 0.91044 0.62359 -0.22982 0.06518  -0.22869 120 GLU A CG  
819  C CD  . GLU A 113 ? 0.69944 1.08189 0.84694 -0.25405 0.08776  -0.23369 120 GLU A CD  
820  O OE1 . GLU A 113 ? 0.83110 1.15409 0.96353 -0.27030 0.10293  -0.24475 120 GLU A OE1 
821  O OE2 . GLU A 113 ? 0.76534 1.16448 0.92551 -0.25520 0.09027  -0.22565 120 GLU A OE2 
822  N N   . ALA A 114 ? 0.33400 0.70076 0.43125 -0.19738 0.05042  -0.23096 121 ALA A N   
823  C CA  . ALA A 114 ? 0.35166 0.69720 0.43170 -0.20392 0.05713  -0.24345 121 ALA A CA  
824  C C   . ALA A 114 ? 0.34327 0.73321 0.40687 -0.19039 0.03666  -0.23497 121 ALA A C   
825  O O   . ALA A 114 ? 0.38568 0.78061 0.43484 -0.20291 0.04076  -0.24791 121 ALA A O   
826  C CB  . ALA A 114 ? 0.34184 0.62157 0.42262 -0.19391 0.06833  -0.24000 121 ALA A CB  
827  N N   . LEU A 115 ? 0.34606 0.76176 0.40915 -0.16346 0.01467  -0.21086 122 LEU A N   
828  C CA  . LEU A 115 ? 0.31086 0.74906 0.35323 -0.14615 -0.00524 -0.19600 122 LEU A CA  
829  C C   . LEU A 115 ? 0.40171 0.88451 0.44150 -0.15904 -0.01086 -0.20647 122 LEU A C   
830  O O   . LEU A 115 ? 0.42573 0.91368 0.44786 -0.16484 -0.01500 -0.21028 122 LEU A O   
831  C CB  . LEU A 115 ? 0.29462 0.72986 0.33270 -0.11055 -0.02614 -0.16401 122 LEU A CB  
832  C CG  . LEU A 115 ? 0.25532 0.64638 0.28910 -0.09394 -0.02662 -0.14822 122 LEU A CG  
833  C CD1 . LEU A 115 ? 0.33899 0.71892 0.36645 -0.05865 -0.04576 -0.11461 122 LEU A CD1 
834  C CD2 . LEU A 115 ? 0.29452 0.66427 0.30573 -0.09598 -0.02548 -0.14808 122 LEU A CD2 
835  N N   . GLN A 116 ? 0.47811 0.99418 0.53544 -0.16396 -0.01174 -0.21099 123 GLN A N   
836  C CA  . GLN A 116 ? 0.54581 1.10754 0.60434 -0.17787 -0.01725 -0.22289 123 GLN A CA  
837  C C   . GLN A 116 ? 0.58832 1.14475 0.64211 -0.21341 0.00043  -0.24980 123 GLN A C   
838  O O   . GLN A 116 ? 0.65491 1.24507 0.70525 -0.22744 -0.00504 -0.26038 123 GLN A O   
839  C CB  . GLN A 116 ? 0.46032 1.05902 0.54127 -0.17662 -0.01901 -0.22316 123 GLN A CB  
840  C CG  . GLN A 116 ? 0.58970 1.20275 0.67269 -0.13980 -0.03931 -0.19844 123 GLN A CG  
841  C CD  . GLN A 116 ? 0.92127 1.59104 1.01969 -0.13881 -0.04794 -0.20336 123 GLN A CD  
842  O OE1 . GLN A 116 ? 0.94654 1.64910 1.05499 -0.16744 -0.03967 -0.22446 123 GLN A OE1 
843  N NE2 . GLN A 116 ? 0.79414 1.47237 0.89330 -0.10583 -0.06443 -0.18414 123 GLN A NE2 
844  N N   . ALA A 117 ? 0.56554 1.07565 0.61846 -0.22703 0.02101  -0.26076 124 ALA A N   
845  C CA  . ALA A 117 ? 0.54944 1.03896 0.59429 -0.25732 0.03980  -0.28511 124 ALA A CA  
846  C C   . ALA A 117 ? 0.74934 1.20613 0.77568 -0.25443 0.04509  -0.28770 124 ALA A C   
847  O O   . ALA A 117 ? 0.71508 1.13496 0.73606 -0.27175 0.06450  -0.30538 124 ALA A O   
848  C CB  . ALA A 117 ? 0.54818 1.00007 0.60441 -0.27503 0.06105  -0.29658 124 ALA A CB  
849  N N   . GLY A 118 ? 0.52225 0.98830 0.53749 -0.23141 0.02814  -0.26900 125 GLY A N   
850  C CA  . GLY A 118 ? 0.53517 0.98243 0.53014 -0.23076 0.03055  -0.27056 125 GLY A CA  
851  C C   . GLY A 118 ? 0.51773 0.93036 0.51041 -0.21068 0.03230  -0.25662 125 GLY A C   
852  O O   . GLY A 118 ? 0.52851 0.93543 0.50268 -0.20454 0.02808  -0.25024 125 GLY A O   
853  N N   . ALA A 119 ? 0.41006 0.79810 0.41984 -0.20158 0.03828  -0.25163 126 ALA A N   
854  C CA  . ALA A 119 ? 0.36929 0.72196 0.37722 -0.18356 0.03990  -0.23988 126 ALA A CA  
855  C C   . ALA A 119 ? 0.41677 0.78549 0.40896 -0.15815 0.01487  -0.21010 126 ALA A C   
856  O O   . ALA A 119 ? 0.36421 0.76333 0.35148 -0.14980 -0.00366 -0.19669 126 ALA A O   
857  C CB  . ALA A 119 ? 0.34932 0.66707 0.37848 -0.17858 0.04920  -0.23897 126 ALA A CB  
858  N N   . ASP A 120 ? 0.37087 0.71208 0.35397 -0.14460 0.01480  -0.19882 127 ASP A N   
859  C CA  . ASP A 120 ? 0.33349 0.67388 0.29777 -0.11989 -0.00769 -0.16639 127 ASP A CA  
860  C C   . ASP A 120 ? 0.27907 0.59020 0.24936 -0.09979 -0.01127 -0.14944 127 ASP A C   
861  O O   . ASP A 120 ? 0.28630 0.57470 0.27506 -0.10620 0.00491  -0.16623 127 ASP A O   
862  C CB  . ASP A 120 ? 0.39069 0.72711 0.33075 -0.12388 -0.00750 -0.16392 127 ASP A CB  
863  C CG  . ASP A 120 ? 0.47169 0.78486 0.41497 -0.13135 0.01397  -0.17999 127 ASP A CG  
864  O OD1 . ASP A 120 ? 0.56998 0.87825 0.52555 -0.15038 0.03593  -0.20962 127 ASP A OD1 
865  O OD2 . ASP A 120 ? 0.41395 0.70876 0.34775 -0.11640 0.00924  -0.16203 127 ASP A OD2 
866  N N   . ILE A 121 ? 0.31298 0.61212 0.26630 -0.07481 -0.03211 -0.11505 128 ILE A N   
867  C CA  . ILE A 121 ? 0.26446 0.53385 0.21995 -0.05162 -0.04010 -0.09133 128 ILE A CA  
868  C C   . ILE A 121 ? 0.30312 0.55059 0.25901 -0.05558 -0.02618 -0.10229 128 ILE A C   
869  O O   . ILE A 121 ? 0.27812 0.48442 0.25354 -0.03837 -0.02003 -0.08660 128 ILE A O   
870  C CB  . ILE A 121 ? 0.32024 0.55752 0.25564 -0.02695 -0.06090 -0.05356 128 ILE A CB  
871  C CG1 . ILE A 121 ? 0.40791 0.65587 0.34951 -0.01966 -0.07141 -0.04916 128 ILE A CG1 
872  C CG2 . ILE A 121 ? 0.32442 0.51189 0.25678 -0.00622 -0.06564 -0.02643 128 ILE A CG2 
873  C CD1 . ILE A 121 ? 0.46448 0.68496 0.38573 -0.00676 -0.08776 -0.02919 128 ILE A CD1 
874  N N   . SER A 122 ? 0.30114 0.55103 0.24731 -0.07144 -0.01178 -0.11970 129 SER A N   
875  C CA  . SER A 122 ? 0.30392 0.51715 0.26044 -0.06706 0.00893  -0.12310 129 SER A CA  
876  C C   . SER A 122 ? 0.29920 0.47026 0.29423 -0.06679 0.03464  -0.13921 129 SER A C   
877  O O   . SER A 122 ? 0.34953 0.47839 0.36147 -0.05316 0.04826  -0.13291 129 SER A O   
878  C CB  . SER A 122 ? 0.29740 0.53081 0.23452 -0.08585 0.02148  -0.14529 129 SER A CB  
879  O OG  . SER A 122 ? 0.34237 0.58073 0.29505 -0.10680 0.04237  -0.17944 129 SER A OG  
880  N N   . MET A 123 ? 0.25975 0.43986 0.26735 -0.08252 0.04043  -0.15980 130 MET A N   
881  C CA  . MET A 123 ? 0.28821 0.42137 0.32433 -0.08603 0.06308  -0.17475 130 MET A CA  
882  C C   . MET A 123 ? 0.24801 0.34982 0.30060 -0.06789 0.05635  -0.14811 130 MET A C   
883  O O   . MET A 123 ? 0.26189 0.32419 0.33290 -0.07426 0.07233  -0.15884 130 MET A O   
884  C CB  . MET A 123 ? 0.41119 0.56131 0.44860 -0.11831 0.07691  -0.21413 130 MET A CB  
885  C CG  . MET A 123 ? 0.36494 0.55464 0.38216 -0.13404 0.07722  -0.22973 130 MET A CG  
886  S SD  . MET A 123 ? 0.44579 0.67342 0.46190 -0.16304 0.07924  -0.24906 130 MET A SD  
887  C CE  . MET A 123 ? 0.44686 0.61971 0.48659 -0.17223 0.10262  -0.26452 130 MET A CE  
888  N N   . ILE A 124 ? 0.21842 0.33076 0.26003 -0.04552 0.03303  -0.11344 131 ILE A N   
889  C CA  . ILE A 124 ? 0.19823 0.28598 0.25013 -0.02744 0.02490  -0.08775 131 ILE A CA  
890  C C   . ILE A 124 ? 0.20306 0.21859 0.27451 -0.01771 0.04265  -0.08247 131 ILE A C   
891  O O   . ILE A 124 ? 0.20387 0.19126 0.28742 -0.01705 0.04781  -0.07763 131 ILE A O   
892  C CB  . ILE A 124 ? 0.17291 0.27488 0.20231 -0.00194 -0.00419 -0.05149 131 ILE A CB  
893  C CG1 . ILE A 124 ? 0.20759 0.28977 0.24409 0.01717  -0.01300 -0.02744 131 ILE A CG1 
894  C CG2 . ILE A 124 ? 0.21644 0.28904 0.23409 0.01254  -0.00702 -0.03286 131 ILE A CG2 
895  C CD1 . ILE A 124 ? 0.23600 0.33041 0.24561 0.04334  -0.04382 0.00583  131 ILE A CD1 
896  N N   . GLY A 125 ? 0.24354 0.22905 0.31766 -0.01016 0.05170  -0.08360 132 GLY A N   
897  C CA  . GLY A 125 ? 0.26467 0.18054 0.35680 0.00307  0.06445  -0.07751 132 GLY A CA  
898  C C   . GLY A 125 ? 0.31361 0.21177 0.41129 -0.01496 0.07777  -0.09352 132 GLY A C   
899  O O   . GLY A 125 ? 0.33971 0.21258 0.42910 -0.00594 0.06975  -0.07047 132 GLY A O   
900  N N   . GLN A 126 ? 0.27328 0.19595 0.37312 -0.04153 0.09193  -0.13156 133 GLN A N   
901  C CA  . GLN A 126 ? 0.30503 0.21166 0.40650 -0.05794 0.10280  -0.14252 133 GLN A CA  
902  C C   . GLN A 126 ? 0.31069 0.21024 0.41359 -0.06467 0.10085  -0.13372 133 GLN A C   
903  O O   . GLN A 126 ? 0.35879 0.23848 0.45798 -0.07520 0.10802  -0.13751 133 GLN A O   
904  C CB  . GLN A 126 ? 0.35174 0.29276 0.44896 -0.08561 0.11426  -0.17990 133 GLN A CB  
905  C CG  . GLN A 126 ? 0.35793 0.30686 0.45207 -0.08086 0.11927  -0.19101 133 GLN A CG  
906  C CD  . GLN A 126 ? 0.46650 0.44979 0.55104 -0.10722 0.12837  -0.22319 133 GLN A CD  
907  O OE1 . GLN A 126 ? 0.54620 0.52096 0.62904 -0.12484 0.13601  -0.23585 133 GLN A OE1 
908  N NE2 . GLN A 126 ? 0.54406 0.56663 0.61776 -0.11020 0.12632  -0.23384 133 GLN A NE2 
909  N N   . PHE A 127 ? 0.27595 0.19023 0.38260 -0.05844 0.09085  -0.12334 134 PHE A N   
910  C CA  . PHE A 127 ? 0.30491 0.21872 0.41666 -0.06575 0.09017  -0.11636 134 PHE A CA  
911  C C   . PHE A 127 ? 0.30250 0.18534 0.40654 -0.03401 0.07658  -0.07337 134 PHE A C   
912  O O   . PHE A 127 ? 0.30591 0.18966 0.41408 -0.03456 0.07538  -0.06423 134 PHE A O   
913  C CB  . PHE A 127 ? 0.25657 0.25494 0.36759 -0.07689 0.07712  -0.12206 134 PHE A CB  
914  C CG  . PHE A 127 ? 0.27240 0.31558 0.38086 -0.10645 0.08283  -0.15714 134 PHE A CG  
915  C CD1 . PHE A 127 ? 0.33091 0.37723 0.44531 -0.14156 0.09768  -0.18517 134 PHE A CD1 
916  C CD2 . PHE A 127 ? 0.26580 0.34266 0.36182 -0.10164 0.07373  -0.16221 134 PHE A CD2 
917  C CE1 . PHE A 127 ? 0.33880 0.42191 0.44410 -0.16327 0.10141  -0.21084 134 PHE A CE1 
918  C CE2 . PHE A 127 ? 0.29092 0.40480 0.38030 -0.12944 0.07902  -0.19488 134 PHE A CE2 
919  C CZ  . PHE A 127 ? 0.32358 0.43947 0.41844 -0.15975 0.09266  -0.21920 134 PHE A CZ  
920  N N   . GLY A 128 ? 0.28627 0.15518 0.37269 -0.01113 0.06216  -0.04903 135 GLY A N   
921  C CA  . GLY A 128 ? 0.26189 0.12452 0.32545 0.00631  0.04285  -0.01929 135 GLY A CA  
922  C C   . GLY A 128 ? 0.25156 0.13184 0.30401 0.01992  0.02730  -0.00053 135 GLY A C   
923  O O   . GLY A 128 ? 0.31588 0.19969 0.36302 0.02462  0.02333  0.01316  135 GLY A O   
924  N N   . VAL A 129 ? 0.22795 0.12275 0.28902 0.02638  0.02509  -0.00208 136 VAL A N   
925  C CA  . VAL A 129 ? 0.20786 0.12387 0.24327 0.04204  0.00268  0.01587  136 VAL A CA  
926  C C   . VAL A 129 ? 0.21222 0.14271 0.23103 0.04882  -0.01122 0.01899  136 VAL A C   
927  O O   . VAL A 129 ? 0.21721 0.17766 0.23908 0.04705  -0.02753 0.02586  136 VAL A O   
928  C CB  . VAL A 129 ? 0.21160 0.16241 0.28356 0.04936  0.00591  0.01869  136 VAL A CB  
929  C CG1 . VAL A 129 ? 0.24351 0.16943 0.32722 0.04133  0.02045  0.01742  136 VAL A CG1 
930  C CG2 . VAL A 129 ? 0.21198 0.22327 0.29075 0.02109  0.01203  -0.01588 136 VAL A CG2 
931  N N   . GLY A 130 ? 0.22058 0.17988 0.23255 -0.01102 -0.02857 -0.05040 137 GLY A N   
932  C CA  . GLY A 130 ? 0.21432 0.18199 0.21522 0.00054  -0.02480 -0.05070 137 GLY A CA  
933  C C   . GLY A 130 ? 0.20958 0.18866 0.21407 0.00112  -0.01644 -0.04077 137 GLY A C   
934  O O   . GLY A 130 ? 0.19833 0.18751 0.19792 0.00758  -0.01352 -0.03813 137 GLY A O   
935  N N   . PHE A 131 ? 0.19972 0.17647 0.21211 -0.00521 -0.01306 -0.03499 138 PHE A N   
936  C CA  . PHE A 131 ? 0.18408 0.16829 0.19962 -0.00490 -0.00755 -0.02803 138 PHE A CA  
937  C C   . PHE A 131 ? 0.17119 0.16551 0.18764 -0.00333 -0.00750 -0.02669 138 PHE A C   
938  O O   . PHE A 131 ? 0.17722 0.17536 0.19257 0.00032  -0.00424 -0.02186 138 PHE A O   
939  C CB  . PHE A 131 ? 0.20039 0.18209 0.22193 -0.01080 -0.00575 -0.02436 138 PHE A CB  
940  C CG  . PHE A 131 ? 0.18845 0.17594 0.21238 -0.01021 -0.00272 -0.02049 138 PHE A CG  
941  C CD1 . PHE A 131 ? 0.20113 0.18768 0.22467 -0.00795 -0.00091 -0.01774 138 PHE A CD1 
942  C CD2 . PHE A 131 ? 0.19133 0.18541 0.21879 -0.01144 -0.00253 -0.02011 138 PHE A CD2 
943  C CE1 . PHE A 131 ? 0.18493 0.17236 0.21088 -0.00796 -0.00033 -0.01576 138 PHE A CE1 
944  C CE2 . PHE A 131 ? 0.18811 0.18366 0.21578 -0.00881 -0.00096 -0.01843 138 PHE A CE2 
945  C CZ  . PHE A 131 ? 0.20266 0.19256 0.22921 -0.00756 -0.00056 -0.01682 138 PHE A CZ  
946  N N   . TYR A 132 ? 0.17469 0.17371 0.19465 -0.00627 -0.01155 -0.03001 139 TYR A N   
947  C CA  . TYR A 132 ? 0.17727 0.18725 0.19895 -0.00350 -0.01182 -0.02824 139 TYR A CA  
948  C C   . TYR A 132 ? 0.18263 0.19727 0.19521 0.00471  -0.01283 -0.02829 139 TYR A C   
949  O O   . TYR A 132 ? 0.19113 0.21283 0.20335 0.00902  -0.01219 -0.02439 139 TYR A O   
950  C CB  . TYR A 132 ? 0.16341 0.18232 0.19430 -0.00882 -0.01589 -0.03085 139 TYR A CB  
951  C CG  . TYR A 132 ? 0.17232 0.19078 0.21157 -0.01547 -0.01254 -0.02742 139 TYR A CG  
952  C CD1 . TYR A 132 ? 0.17751 0.20198 0.21899 -0.01284 -0.00794 -0.02328 139 TYR A CD1 
953  C CD2 . TYR A 132 ? 0.19274 0.20346 0.23579 -0.02292 -0.01402 -0.02802 139 TYR A CD2 
954  C CE1 . TYR A 132 ? 0.16730 0.19396 0.21327 -0.01654 -0.00425 -0.02000 139 TYR A CE1 
955  C CE2 . TYR A 132 ? 0.21645 0.22840 0.26546 -0.02797 -0.00994 -0.02250 139 TYR A CE2 
956  C CZ  . TYR A 132 ? 0.16507 0.18679 0.21477 -0.02427 -0.00471 -0.01857 139 TYR A CZ  
957  O OH  . TYR A 132 ? 0.20714 0.23257 0.25992 -0.02721 -0.00019 -0.01300 139 TYR A OH  
958  N N   . SER A 133 ? 0.18356 0.19465 0.18748 0.00871  -0.01395 -0.03192 140 SER A N   
959  C CA  . SER A 133 ? 0.19138 0.20950 0.18423 0.01854  -0.01275 -0.02985 140 SER A CA  
960  C C   . SER A 133 ? 0.17286 0.19286 0.16721 0.02065  -0.00515 -0.01824 140 SER A C   
961  O O   . SER A 133 ? 0.19970 0.22742 0.18687 0.02809  -0.00273 -0.01229 140 SER A O   
962  C CB  . SER A 133 ? 0.19243 0.20758 0.17413 0.02483  -0.01453 -0.03662 140 SER A CB  
963  O OG  . SER A 133 ? 0.20538 0.21516 0.18874 0.02472  -0.00895 -0.03308 140 SER A OG  
964  N N   . ALA A 134 ? 0.17668 0.18983 0.18027 0.01416  -0.00202 -0.01450 141 ALA A N   
965  C CA  . ALA A 134 ? 0.17217 0.18450 0.18036 0.01377  0.00266  -0.00445 141 ALA A CA  
966  C C   . ALA A 134 ? 0.15866 0.17310 0.16580 0.01740  0.00212  0.00070  141 ALA A C   
967  O O   . ALA A 134 ? 0.19030 0.20490 0.19775 0.01967  0.00564  0.01090  141 ALA A O   
968  C CB  . ALA A 134 ? 0.16179 0.16553 0.17903 0.00653  0.00288  -0.00473 141 ALA A CB  
969  N N   . TYR A 135 ? 0.16039 0.17745 0.16747 0.01819  -0.00228 -0.00498 142 TYR A N   
970  C CA  . TYR A 135 ? 0.19016 0.20992 0.19635 0.02365  -0.00343 -0.00052 142 TYR A CA  
971  C C   . TYR A 135 ? 0.19823 0.22800 0.19381 0.03253  -0.00417 0.00322  142 TYR A C   
972  O O   . TYR A 135 ? 0.21236 0.24495 0.20567 0.03889  -0.00532 0.00842  142 TYR A O   
973  C CB  . TYR A 135 ? 0.17628 0.20001 0.18841 0.02240  -0.00722 -0.00693 142 TYR A CB  
974  C CG  . TYR A 135 ? 0.19095 0.20535 0.20998 0.01733  -0.00522 -0.00792 142 TYR A CG  
975  C CD1 . TYR A 135 ? 0.18946 0.19445 0.20988 0.02060  -0.00437 -0.00396 142 TYR A CD1 
976  C CD2 . TYR A 135 ? 0.17719 0.19026 0.19965 0.01030  -0.00483 -0.01287 142 TYR A CD2 
977  C CE1 . TYR A 135 ? 0.18938 0.18553 0.21319 0.01770  -0.00388 -0.00700 142 TYR A CE1 
978  C CE2 . TYR A 135 ? 0.17503 0.18133 0.20085 0.00746  -0.00324 -0.01370 142 TYR A CE2 
979  C CZ  . TYR A 135 ? 0.17871 0.17734 0.20454 0.01152  -0.00310 -0.01174 142 TYR A CZ  
980  O OH  . TYR A 135 ? 0.19508 0.18696 0.22154 0.01044  -0.00293 -0.01475 142 TYR A OH  
981  N N   . LEU A 136 ? 0.19793 0.23325 0.18528 0.03504  -0.00367 0.00064  143 LEU A N   
982  C CA  . LEU A 136 ? 0.20101 0.24686 0.17514 0.04562  -0.00267 0.00612  143 LEU A CA  
983  C C   . LEU A 136 ? 0.19216 0.23593 0.16735 0.04756  0.00499  0.02295  143 LEU A C   
984  O O   . LEU A 136 ? 0.22836 0.27924 0.19470 0.05637  0.00639  0.03231  143 LEU A O   
985  C CB  . LEU A 136 ? 0.21970 0.27122 0.18315 0.04988  -0.00321 -0.00130 143 LEU A CB  
986  C CG  . LEU A 136 ? 0.21344 0.26490 0.17386 0.04876  -0.01273 -0.01803 143 LEU A CG  
987  C CD1 . LEU A 136 ? 0.23330 0.28363 0.18323 0.05362  -0.01286 -0.02565 143 LEU A CD1 
988  C CD2 . LEU A 136 ? 0.23476 0.29760 0.18763 0.05573  -0.02060 -0.02220 143 LEU A CD2 
989  N N   . VAL A 137 ? 0.19703 0.23143 0.18371 0.03904  0.00938  0.02776  144 VAL A N   
990  C CA  . VAL A 137 ? 0.21652 0.24901 0.20839 0.03783  0.01595  0.04445  144 VAL A CA  
991  C C   . VAL A 137 ? 0.21518 0.22987 0.22113 0.02906  0.01466  0.04817  144 VAL A C   
992  O O   . VAL A 137 ? 0.23090 0.23947 0.24277 0.02719  0.01782  0.06265  144 VAL A O   
993  C CB  . VAL A 137 ? 0.20818 0.25116 0.20140 0.03706  0.02252  0.04932  144 VAL A CB  
994  C CG1 . VAL A 137 ? 0.20775 0.26786 0.18308 0.04964  0.02402  0.04632  144 VAL A CG1 
995  C CG2 . VAL A 137 ? 0.18863 0.22558 0.19144 0.02855  0.02074  0.03921  144 VAL A CG2 
996  N N   . ALA A 138 ? 0.20777 0.21326 0.21897 0.02400  0.00984  0.03614  145 ALA A N   
997  C CA  . ALA A 138 ? 0.20856 0.19694 0.23042 0.01730  0.00757  0.03638  145 ALA A CA  
998  C C   . ALA A 138 ? 0.22311 0.20359 0.24234 0.02270  0.00305  0.03170  145 ALA A C   
999  O O   . ALA A 138 ? 0.24831 0.23802 0.26299 0.02651  0.00066  0.02244  145 ALA A O   
1000 C CB  . ALA A 138 ? 0.22518 0.21139 0.25304 0.00977  0.00611  0.02660  145 ALA A CB  
1001 N N   . GLU A 139 ? 0.22847 0.19191 0.25195 0.02301  0.00143  0.03817  146 GLU A N   
1002 C CA  . GLU A 139 ? 0.24486 0.19875 0.26629 0.02980  -0.00305 0.03224  146 GLU A CA  
1003 C C   . GLU A 139 ? 0.26247 0.20963 0.28745 0.02617  -0.00611 0.01952  146 GLU A C   
1004 O O   . GLU A 139 ? 0.26458 0.21340 0.28658 0.03317  -0.00833 0.01175  146 GLU A O   
1005 C CB  . GLU A 139 ? 0.27790 0.21175 0.30070 0.03354  -0.00465 0.04329  146 GLU A CB  
1006 C CG  . GLU A 139 ? 0.36884 0.28226 0.40246 0.02302  -0.00620 0.04819  146 GLU A CG  
1007 C CD  . GLU A 139 ? 0.64803 0.53903 0.68458 0.02502  -0.00808 0.06183  146 GLU A CD  
1008 O OE1 . GLU A 139 ? 0.51567 0.41162 0.54483 0.03426  -0.00559 0.07213  146 GLU A OE1 
1009 O OE2 . GLU A 139 ? 0.61771 0.48512 0.66391 0.01739  -0.01297 0.06232  146 GLU A OE2 
1010 N N   . LYS A 140 ? 0.22661 0.16912 0.25763 0.01658  -0.00608 0.01783  147 LYS A N   
1011 C CA  . LYS A 140 ? 0.22374 0.16178 0.25573 0.01398  -0.00906 0.00634  147 LYS A CA  
1012 C C   . LYS A 140 ? 0.18392 0.13065 0.22003 0.00516  -0.00710 0.00562  147 LYS A C   
1013 O O   . LYS A 140 ? 0.20287 0.15193 0.24460 -0.00004 -0.00483 0.01431  147 LYS A O   
1014 C CB  . LYS A 140 ? 0.23239 0.14647 0.26718 0.01387  -0.01503 0.00396  147 LYS A CB  
1015 C CG  . LYS A 140 ? 0.24513 0.15505 0.27767 0.01334  -0.01902 -0.00888 147 LYS A CG  
1016 C CD  . LYS A 140 ? 0.31725 0.20123 0.34892 0.01690  -0.02690 -0.01441 147 LYS A CD  
1017 C CE  . LYS A 140 ? 0.37838 0.24671 0.42141 0.00490  -0.03244 -0.01069 147 LYS A CE  
1018 N NZ  . LYS A 140 ? 0.50682 0.34439 0.54982 0.00771  -0.04223 -0.01621 147 LYS A NZ  
1019 N N   . VAL A 141 ? 0.18219 0.13561 0.21559 0.00457  -0.00732 -0.00334 148 VAL A N   
1020 C CA  . VAL A 141 ? 0.17689 0.13672 0.21305 -0.00185 -0.00625 -0.00459 148 VAL A CA  
1021 C C   . VAL A 141 ? 0.21102 0.16421 0.24629 -0.00298 -0.01029 -0.01260 148 VAL A C   
1022 O O   . VAL A 141 ? 0.19199 0.14554 0.22097 0.00254  -0.01088 -0.01895 148 VAL A O   
1023 C CB  . VAL A 141 ? 0.17362 0.14765 0.20566 -0.00099 -0.00285 -0.00639 148 VAL A CB  
1024 C CG1 . VAL A 141 ? 0.20304 0.18041 0.23691 -0.00562 -0.00228 -0.00772 148 VAL A CG1 
1025 C CG2 . VAL A 141 ? 0.18484 0.16621 0.21462 0.00213  -0.00037 -0.00069 148 VAL A CG2 
1026 N N   . THR A 142 ? 0.18415 0.13395 0.22569 -0.00915 -0.01318 -0.01204 149 THR A N   
1027 C CA  . THR A 142 ? 0.19404 0.13998 0.23330 -0.00975 -0.01819 -0.02008 149 THR A CA  
1028 C C   . THR A 142 ? 0.22349 0.18143 0.26415 -0.01300 -0.01622 -0.01898 149 THR A C   
1029 O O   . THR A 142 ? 0.20971 0.17409 0.25852 -0.01724 -0.01425 -0.01246 149 THR A O   
1030 C CB  . THR A 142 ? 0.21389 0.14503 0.26079 -0.01436 -0.02623 -0.02163 149 THR A CB  
1031 O OG1 . THR A 142 ? 0.26770 0.18344 0.31407 -0.01106 -0.02831 -0.02087 149 THR A OG1 
1032 C CG2 . THR A 142 ? 0.25196 0.17899 0.29283 -0.01249 -0.03332 -0.03272 149 THR A CG2 
1033 N N   . VAL A 143 ? 0.17912 0.14099 0.21146 -0.00973 -0.01615 -0.02423 150 VAL A N   
1034 C CA  . VAL A 143 ? 0.16989 0.14026 0.20181 -0.01111 -0.01476 -0.02276 150 VAL A CA  
1035 C C   . VAL A 143 ? 0.19957 0.16842 0.22755 -0.00991 -0.02090 -0.02851 150 VAL A C   
1036 O O   . VAL A 143 ? 0.21568 0.18280 0.23319 -0.00447 -0.02181 -0.03385 150 VAL A O   
1037 C CB  . VAL A 143 ? 0.17764 0.15384 0.20321 -0.00870 -0.00915 -0.02132 150 VAL A CB  
1038 C CG1 . VAL A 143 ? 0.22780 0.20789 0.25189 -0.00908 -0.00860 -0.01937 150 VAL A CG1 
1039 C CG2 . VAL A 143 ? 0.18576 0.16402 0.21407 -0.00919 -0.00542 -0.01791 150 VAL A CG2 
1040 N N   . ILE A 144 ? 0.17605 0.14814 0.21226 -0.01393 -0.02532 -0.02745 151 ILE A N   
1041 C CA  . ILE A 144 ? 0.18240 0.15587 0.21524 -0.01254 -0.03284 -0.03319 151 ILE A CA  
1042 C C   . ILE A 144 ? 0.18412 0.16797 0.21401 -0.01006 -0.02984 -0.02897 151 ILE A C   
1043 O O   . ILE A 144 ? 0.19894 0.18899 0.23711 -0.01208 -0.02608 -0.02278 151 ILE A O   
1044 C CB  . ILE A 144 ? 0.21331 0.18522 0.26078 -0.01959 -0.04178 -0.03473 151 ILE A CB  
1045 C CG1 . ILE A 144 ? 0.34338 0.30202 0.39811 -0.02399 -0.04348 -0.03455 151 ILE A CG1 
1046 C CG2 . ILE A 144 ? 0.22513 0.19696 0.26682 -0.01715 -0.05247 -0.04406 151 ILE A CG2 
1047 C CD1 . ILE A 144 ? 0.34329 0.28648 0.38600 -0.01840 -0.04900 -0.04496 151 ILE A CD1 
1048 N N   . THR A 145 ? 0.18519 0.17083 0.20214 -0.00419 -0.03132 -0.03179 152 THR A N   
1049 C CA  . THR A 145 ? 0.17827 0.17006 0.19086 -0.00091 -0.02780 -0.02591 152 THR A CA  
1050 C C   . THR A 145 ? 0.20624 0.20279 0.20809 0.00510  -0.03371 -0.02876 152 THR A C   
1051 O O   . THR A 145 ? 0.20986 0.20471 0.20159 0.00892  -0.03794 -0.03574 152 THR A O   
1052 C CB  . THR A 145 ? 0.18760 0.17627 0.19427 0.00009  -0.01883 -0.02060 152 THR A CB  
1053 O OG1 . THR A 145 ? 0.21858 0.20796 0.22413 0.00194  -0.01632 -0.01433 152 THR A OG1 
1054 C CG2 . THR A 145 ? 0.22428 0.21342 0.21839 0.00440  -0.01662 -0.02204 152 THR A CG2 
1055 N N   . LYS A 146 ? 0.20622 0.20902 0.20882 0.00778  -0.03438 -0.02370 153 LYS A N   
1056 C CA  . LYS A 146 ? 0.19837 0.20760 0.18966 0.01508  -0.03997 -0.02437 153 LYS A CA  
1057 C C   . LYS A 146 ? 0.21913 0.22845 0.20582 0.01975  -0.03447 -0.01415 153 LYS A C   
1058 O O   . LYS A 146 ? 0.21730 0.22824 0.21450 0.01906  -0.03373 -0.01052 153 LYS A O   
1059 C CB  . LYS A 146 ? 0.19961 0.21804 0.20105 0.01363  -0.05168 -0.03036 153 LYS A CB  
1060 C CG  . LYS A 146 ? 0.21089 0.23886 0.20068 0.02245  -0.05940 -0.03152 153 LYS A CG  
1061 C CD  . LYS A 146 ? 0.25083 0.27621 0.21924 0.02951  -0.06219 -0.03813 153 LYS A CD  
1062 C CE  . LYS A 146 ? 0.25764 0.29440 0.21222 0.03971  -0.07121 -0.03992 153 LYS A CE  
1063 N NZ  . LYS A 146 ? 0.27003 0.31008 0.21459 0.04740  -0.06374 -0.02613 153 LYS A NZ  
1064 N N   . HIS A 147 ? 0.21669 0.22401 0.18773 0.02514  -0.03033 -0.00890 154 HIS A N   
1065 C CA  . HIS A 147 ? 0.21696 0.22075 0.18174 0.02985  -0.02607 0.00230  154 HIS A CA  
1066 C C   . HIS A 147 ? 0.25183 0.26484 0.20339 0.03975  -0.03229 0.00394  154 HIS A C   
1067 O O   . HIS A 147 ? 0.27460 0.29541 0.21632 0.04347  -0.03747 -0.00311 154 HIS A O   
1068 C CB  . HIS A 147 ? 0.23557 0.23221 0.19428 0.02728  -0.01654 0.00987  154 HIS A CB  
1069 C CG  . HIS A 147 ? 0.23388 0.22130 0.18910 0.02904  -0.01190 0.02284  154 HIS A CG  
1070 N ND1 . HIS A 147 ? 0.27406 0.26417 0.21554 0.03717  -0.01190 0.03227  154 HIS A ND1 
1071 C CD2 . HIS A 147 ? 0.27120 0.24454 0.23423 0.02390  -0.00786 0.02800  154 HIS A CD2 
1072 C CE1 . HIS A 147 ? 0.31387 0.29015 0.25627 0.03620  -0.00772 0.04403  154 HIS A CE1 
1073 N NE2 . HIS A 147 ? 0.30723 0.27222 0.26277 0.02796  -0.00589 0.04054  154 HIS A NE2 
1074 N N   . ASN A 148 ? 0.23927 0.25089 0.18936 0.04562  -0.03277 0.01242  155 ASN A N   
1075 C CA  . ASN A 148 ? 0.26758 0.28940 0.20450 0.05665  -0.03937 0.01513  155 ASN A CA  
1076 C C   . ASN A 148 ? 0.27106 0.29652 0.18690 0.06243  -0.03636 0.01907  155 ASN A C   
1077 O O   . ASN A 148 ? 0.32146 0.35927 0.22378 0.07156  -0.04408 0.01520  155 ASN A O   
1078 C CB  . ASN A 148 ? 0.28499 0.30111 0.22123 0.06384  -0.03842 0.02660  155 ASN A CB  
1079 C CG  . ASN A 148 ? 0.28382 0.30617 0.23726 0.06451  -0.04399 0.02176  155 ASN A CG  
1080 O OD1 . ASN A 148 ? 0.30784 0.34433 0.27290 0.06069  -0.05106 0.01143  155 ASN A OD1 
1081 N ND2 . ASN A 148 ? 0.28238 0.29428 0.23830 0.06965  -0.04086 0.02967  155 ASN A ND2 
1082 N N   . ASP A 149 ? 0.30501 0.32253 0.21787 0.05794  -0.02550 0.02676  156 ASP A N   
1083 C CA  . ASP A 149 ? 0.35848 0.38308 0.25236 0.06429  -0.01967 0.03458  156 ASP A CA  
1084 C C   . ASP A 149 ? 0.38806 0.42105 0.27687 0.06400  -0.01911 0.02319  156 ASP A C   
1085 O O   . ASP A 149 ? 0.40269 0.44460 0.27653 0.06996  -0.01221 0.02960  156 ASP A O   
1086 C CB  . ASP A 149 ? 0.35193 0.36623 0.24734 0.05967  -0.00780 0.05278  156 ASP A CB  
1087 C CG  . ASP A 149 ? 0.43011 0.43207 0.32619 0.06286  -0.00874 0.06513  156 ASP A CG  
1088 O OD1 . ASP A 149 ? 0.40694 0.41452 0.29649 0.07264  -0.01714 0.06276  156 ASP A OD1 
1089 O OD2 . ASP A 149 ? 0.46176 0.44782 0.36550 0.05588  -0.00203 0.07674  156 ASP A OD2 
1090 N N   . ASP A 150 ? 0.30321 0.33393 0.20383 0.05826  -0.02578 0.00752  157 ASP A N   
1091 C CA  . ASP A 150 ? 0.27592 0.31003 0.17208 0.05891  -0.02575 -0.00368 157 ASP A CA  
1092 C C   . ASP A 150 ? 0.35639 0.38833 0.25961 0.05694  -0.03917 -0.02143 157 ASP A C   
1093 O O   . ASP A 150 ? 0.31321 0.34506 0.22702 0.05398  -0.04737 -0.02371 157 ASP A O   
1094 C CB  . ASP A 150 ? 0.28591 0.31416 0.19432 0.04966  -0.01525 0.00055  157 ASP A CB  
1095 C CG  . ASP A 150 ? 0.33336 0.37061 0.23085 0.05550  -0.00994 -0.00283 157 ASP A CG  
1096 O OD1 . ASP A 150 ? 0.36606 0.41016 0.24683 0.06650  -0.01615 -0.01315 157 ASP A OD1 
1097 O OD2 . ASP A 150 ? 0.31447 0.35285 0.22030 0.04989  -0.00020 0.00399  157 ASP A OD2 
1098 N N   . GLU A 151 ? 0.32471 0.35527 0.22317 0.05880  -0.04158 -0.03346 158 GLU A N   
1099 C CA  . GLU A 151 ? 0.30437 0.32841 0.21097 0.05522  -0.05470 -0.04998 158 GLU A CA  
1100 C C   . GLU A 151 ? 0.24995 0.26298 0.17985 0.04190  -0.05174 -0.04978 158 GLU A C   
1101 O O   . GLU A 151 ? 0.27796 0.28893 0.21512 0.03693  -0.04044 -0.03950 158 GLU A O   
1102 C CB  . GLU A 151 ? 0.38273 0.40637 0.27073 0.06570  -0.05990 -0.06402 158 GLU A CB  
1103 C CG  . GLU A 151 ? 0.50308 0.54042 0.36351 0.08176  -0.06125 -0.06388 158 GLU A CG  
1104 C CD  . GLU A 151 ? 0.75278 0.79570 0.61072 0.08423  -0.07532 -0.06843 158 GLU A CD  
1105 O OE1 . GLU A 151 ? 0.94454 0.98059 0.81495 0.07781  -0.08998 -0.08218 158 GLU A OE1 
1106 O OE2 . GLU A 151 ? 0.88083 0.93570 0.72573 0.09227  -0.07207 -0.05724 158 GLU A OE2 
1107 N N   . GLN A 152 ? 0.26682 0.27284 0.20858 0.03595  -0.06277 -0.06098 159 GLN A N   
1108 C CA  . GLN A 152 ? 0.24057 0.23743 0.20347 0.02418  -0.06028 -0.05945 159 GLN A CA  
1109 C C   . GLN A 152 ? 0.23261 0.21972 0.19081 0.02598  -0.05578 -0.06397 159 GLN A C   
1110 O O   . GLN A 152 ? 0.27787 0.25940 0.22394 0.03318  -0.06275 -0.07599 159 GLN A O   
1111 C CB  . GLN A 152 ? 0.23713 0.23149 0.21739 0.01580  -0.07335 -0.06655 159 GLN A CB  
1112 C CG  . GLN A 152 ? 0.25127 0.24051 0.25444 0.00375  -0.06930 -0.06063 159 GLN A CG  
1113 C CD  . GLN A 152 ? 0.30743 0.30249 0.33226 -0.00572 -0.07925 -0.06127 159 GLN A CD  
1114 O OE1 . GLN A 152 ? 0.33164 0.34130 0.36060 -0.00450 -0.08248 -0.05817 159 GLN A OE1 
1115 N NE2 . GLN A 152 ? 0.30009 0.28489 0.34028 -0.01516 -0.08409 -0.06398 159 GLN A NE2 
1116 N N   . TYR A 153 ? 0.21727 0.20249 0.18448 0.02080  -0.04512 -0.05535 160 TYR A N   
1117 C CA  . TYR A 153 ? 0.22893 0.20874 0.19286 0.02357  -0.03973 -0.05753 160 TYR A CA  
1118 C C   . TYR A 153 ? 0.24300 0.21387 0.22457 0.01416  -0.03843 -0.05492 160 TYR A C   
1119 O O   . TYR A 153 ? 0.22137 0.19426 0.21640 0.00608  -0.03691 -0.04795 160 TYR A O   
1120 C CB  . TYR A 153 ? 0.22838 0.21921 0.18442 0.02796  -0.02729 -0.04811 160 TYR A CB  
1121 C CG  . TYR A 153 ? 0.25843 0.25949 0.19404 0.04012  -0.02625 -0.04984 160 TYR A CG  
1122 C CD1 . TYR A 153 ? 0.30574 0.30785 0.22825 0.05107  -0.02677 -0.05880 160 TYR A CD1 
1123 C CD2 . TYR A 153 ? 0.30981 0.31984 0.23762 0.04261  -0.02486 -0.04232 160 TYR A CD2 
1124 C CE1 . TYR A 153 ? 0.38799 0.40268 0.28931 0.06460  -0.02493 -0.06020 160 TYR A CE1 
1125 C CE2 . TYR A 153 ? 0.34878 0.37038 0.25572 0.05514  -0.02317 -0.04216 160 TYR A CE2 
1126 C CZ  . TYR A 153 ? 0.42563 0.45081 0.31905 0.06625  -0.02287 -0.05122 160 TYR A CZ  
1127 O OH  . TYR A 153 ? 0.48410 0.52386 0.35452 0.08097  -0.02024 -0.05091 160 TYR A OH  
1128 N N   . ALA A 154 ? 0.23738 0.19948 0.21721 0.01730  -0.03847 -0.06004 161 ALA A N   
1129 C CA  . ALA A 154 ? 0.22403 0.17803 0.21713 0.01099  -0.03622 -0.05622 161 ALA A CA  
1130 C C   . ALA A 154 ? 0.22195 0.18123 0.21049 0.01654  -0.02714 -0.05308 161 ALA A C   
1131 O O   . ALA A 154 ? 0.23283 0.19240 0.20980 0.02675  -0.02708 -0.05945 161 ALA A O   
1132 C CB  . ALA A 154 ? 0.27535 0.21120 0.27310 0.00943  -0.04666 -0.06448 161 ALA A CB  
1133 N N   . TRP A 155 ? 0.19913 0.16437 0.19666 0.01081  -0.02013 -0.04396 162 TRP A N   
1134 C CA  . TRP A 155 ? 0.17914 0.15090 0.17758 0.01340  -0.01323 -0.04034 162 TRP A CA  
1135 C C   . TRP A 155 ? 0.22068 0.18242 0.22735 0.01110  -0.01509 -0.03929 162 TRP A C   
1136 O O   . TRP A 155 ? 0.20286 0.15782 0.21777 0.00418  -0.01797 -0.03637 162 TRP A O   
1137 C CB  . TRP A 155 ? 0.18571 0.16844 0.18871 0.00776  -0.00685 -0.03197 162 TRP A CB  
1138 C CG  . TRP A 155 ? 0.15970 0.15172 0.16735 0.00727  -0.00129 -0.02773 162 TRP A CG  
1139 C CD1 . TRP A 155 ? 0.16911 0.17510 0.17591 0.00878  0.00410  -0.02422 162 TRP A CD1 
1140 C CD2 . TRP A 155 ? 0.17768 0.16829 0.19277 0.00453  -0.00110 -0.02565 162 TRP A CD2 
1141 N NE1 . TRP A 155 ? 0.16536 0.17866 0.18066 0.00608  0.00631  -0.02130 162 TRP A NE1 
1142 C CE2 . TRP A 155 ? 0.16827 0.17199 0.18694 0.00446  0.00288  -0.02282 162 TRP A CE2 
1143 C CE3 . TRP A 155 ? 0.18361 0.16516 0.20298 0.00226  -0.00383 -0.02482 162 TRP A CE3 
1144 C CZ2 . TRP A 155 ? 0.16893 0.17625 0.19359 0.00318  0.00264  -0.02135 162 TRP A CZ2 
1145 C CZ3 . TRP A 155 ? 0.19139 0.17656 0.21465 0.00211  -0.00246 -0.02185 162 TRP A CZ3 
1146 C CH2 . TRP A 155 ? 0.17233 0.16992 0.19737 0.00301  -0.00000 -0.02119 162 TRP A CH2 
1147 N N   . GLU A 156 ? 0.18017 0.14299 0.18505 0.01767  -0.01299 -0.04027 163 GLU A N   
1148 C CA  . GLU A 156 ? 0.18886 0.14173 0.19988 0.01707  -0.01465 -0.03757 163 GLU A CA  
1149 C C   . GLU A 156 ? 0.20402 0.16755 0.21487 0.02357  -0.01011 -0.03544 163 GLU A C   
1150 O O   . GLU A 156 ? 0.19952 0.17362 0.20503 0.03155  -0.00756 -0.03894 163 GLU A O   
1151 C CB  . GLU A 156 ? 0.24614 0.17787 0.25527 0.02016  -0.02274 -0.04386 163 GLU A CB  
1152 C CG  . GLU A 156 ? 0.28470 0.20245 0.30204 0.01689  -0.02497 -0.03780 163 GLU A CG  
1153 C CD  . GLU A 156 ? 0.40917 0.30214 0.42783 0.01629  -0.03474 -0.04333 163 GLU A CD  
1154 O OE1 . GLU A 156 ? 0.41472 0.29589 0.42387 0.02702  -0.03925 -0.05297 163 GLU A OE1 
1155 O OE2 . GLU A 156 ? 0.38664 0.27247 0.41653 0.00521  -0.03843 -0.03843 163 GLU A OE2 
1156 N N   . SER A 157 ? 0.18063 0.14439 0.19744 0.02102  -0.00906 -0.02919 164 SER A N   
1157 C CA  . SER A 157 ? 0.17240 0.14685 0.18988 0.02795  -0.00674 -0.02751 164 SER A CA  
1158 C C   . SER A 157 ? 0.16467 0.13153 0.18504 0.02805  -0.00816 -0.02120 164 SER A C   
1159 O O   . SER A 157 ? 0.17578 0.14062 0.19934 0.02058  -0.00763 -0.01578 164 SER A O   
1160 C CB  . SER A 157 ? 0.18166 0.17810 0.20310 0.02444  -0.00234 -0.02541 164 SER A CB  
1161 O OG  . SER A 157 ? 0.17563 0.18527 0.20028 0.03066  -0.00160 -0.02403 164 SER A OG  
1162 N N   . SER A 158 ? 0.20284 0.16711 0.22121 0.03824  -0.00947 -0.02116 165 SER A N   
1163 C CA  . SER A 158 ? 0.22856 0.19083 0.24798 0.04137  -0.01004 -0.01356 165 SER A CA  
1164 C C   . SER A 158 ? 0.21136 0.19747 0.23238 0.04627  -0.00829 -0.01282 165 SER A C   
1165 O O   . SER A 158 ? 0.26020 0.24796 0.27997 0.05465  -0.00973 -0.00865 165 SER A O   
1166 C CB  . SER A 158 ? 0.26423 0.20422 0.28057 0.05022  -0.01413 -0.01285 165 SER A CB  
1167 O OG  . SER A 158 ? 0.29375 0.21066 0.31154 0.04338  -0.01779 -0.01347 165 SER A OG  
1168 N N   . ALA A 159 ? 0.19450 0.19901 0.21927 0.04082  -0.00598 -0.01623 166 ALA A N   
1169 C CA  . ALA A 159 ? 0.20749 0.23689 0.23789 0.04298  -0.00560 -0.01664 166 ALA A CA  
1170 C C   . ALA A 159 ? 0.23118 0.26979 0.26237 0.05593  -0.00526 -0.01891 166 ALA A C   
1171 O O   . ALA A 159 ? 0.26607 0.29638 0.29293 0.06118  -0.00396 -0.02308 166 ALA A O   
1172 C CB  . ALA A 159 ? 0.27180 0.30744 0.30213 0.04241  -0.00825 -0.01255 166 ALA A CB  
1173 N N   . GLY A 160 ? 0.24051 0.29760 0.27640 0.06274  -0.00695 -0.01701 167 GLY A N   
1174 C CA  . GLY A 160 ? 0.24440 0.31486 0.28232 0.07690  -0.00608 -0.01897 167 GLY A CA  
1175 C C   . GLY A 160 ? 0.23113 0.32427 0.27622 0.07582  -0.00115 -0.02174 167 GLY A C   
1176 O O   . GLY A 160 ? 0.25582 0.35963 0.30036 0.08965  0.00116  -0.02405 167 GLY A O   
1177 N N   . GLY A 161 ? 0.18698 0.28747 0.23806 0.06094  0.00094  -0.02079 168 GLY A N   
1178 C CA  . GLY A 161 ? 0.15511 0.28117 0.21582 0.05780  0.00624  -0.01958 168 GLY A CA  
1179 C C   . GLY A 161 ? 0.14853 0.26556 0.20046 0.05838  0.01126  -0.02153 168 GLY A C   
1180 O O   . GLY A 161 ? 0.16858 0.30817 0.22734 0.05627  0.01705  -0.01823 168 GLY A O   
1181 N N   . SER A 162 ? 0.16337 0.25000 0.20117 0.06080  0.00891  -0.02597 169 SER A N   
1182 C CA  . SER A 162 ? 0.16298 0.24182 0.19063 0.06320  0.01174  -0.02955 169 SER A CA  
1183 C C   . SER A 162 ? 0.16937 0.21985 0.18992 0.05378  0.00776  -0.03138 169 SER A C   
1184 O O   . SER A 162 ? 0.19063 0.22447 0.21189 0.04933  0.00334  -0.03044 169 SER A O   
1185 C CB  . SER A 162 ? 0.22213 0.29664 0.23838 0.08243  0.01167  -0.03671 169 SER A CB  
1186 O OG  . SER A 162 ? 0.25410 0.29914 0.26353 0.08772  0.00468  -0.04097 169 SER A OG  
1187 N N   . PHE A 163 ? 0.17272 0.22103 0.18660 0.05173  0.00976  -0.03300 170 PHE A N   
1188 C CA  . PHE A 163 ? 0.16485 0.19020 0.17231 0.04496  0.00556  -0.03559 170 PHE A CA  
1189 C C   . PHE A 163 ? 0.19776 0.21843 0.19171 0.05419  0.00485  -0.04269 170 PHE A C   
1190 O O   . PHE A 163 ? 0.19162 0.23056 0.18080 0.06424  0.00988  -0.04348 170 PHE A O   
1191 C CB  . PHE A 163 ? 0.17540 0.20365 0.18923 0.03049  0.00713  -0.02944 170 PHE A CB  
1192 C CG  . PHE A 163 ? 0.14789 0.19474 0.16305 0.02792  0.01314  -0.02453 170 PHE A CG  
1193 C CD1 . PHE A 163 ? 0.16882 0.23754 0.19600 0.02393  0.01747  -0.01807 170 PHE A CD1 
1194 C CD2 . PHE A 163 ? 0.16335 0.20633 0.16891 0.02860  0.01388  -0.02516 170 PHE A CD2 
1195 C CE1 . PHE A 163 ? 0.16147 0.24691 0.19251 0.01960  0.02344  -0.01061 170 PHE A CE1 
1196 C CE2 . PHE A 163 ? 0.16900 0.22857 0.17519 0.02640  0.02015  -0.01780 170 PHE A CE2 
1197 C CZ  . PHE A 163 ? 0.16933 0.24960 0.18910 0.02115  0.02544  -0.00957 170 PHE A CZ  
1198 N N   . THR A 164 ? 0.19211 0.19012 0.17997 0.05156  -0.00185 -0.04805 171 THR A N   
1199 C CA  . THR A 164 ? 0.20518 0.19683 0.17881 0.05971  -0.00527 -0.05683 171 THR A CA  
1200 C C   . THR A 164 ? 0.19890 0.18861 0.17143 0.04990  -0.00678 -0.05471 171 THR A C   
1201 O O   . THR A 164 ? 0.20081 0.18512 0.18337 0.03751  -0.00779 -0.04908 171 THR A O   
1202 C CB  . THR A 164 ? 0.22920 0.19406 0.19629 0.06689  -0.01511 -0.06777 171 THR A CB  
1203 O OG1 . THR A 164 ? 0.28787 0.23346 0.26481 0.05383  -0.02117 -0.06508 171 THR A OG1 
1204 C CG2 . THR A 164 ? 0.25397 0.21830 0.22028 0.07970  -0.01416 -0.07004 171 THR A CG2 
1205 N N   . VAL A 165 ? 0.21148 0.20716 0.17035 0.05759  -0.00688 -0.05925 172 VAL A N   
1206 C CA  . VAL A 165 ? 0.21540 0.20873 0.16998 0.05198  -0.01013 -0.05881 172 VAL A CA  
1207 C C   . VAL A 165 ? 0.26602 0.24925 0.20382 0.06314  -0.01901 -0.07252 172 VAL A C   
1208 O O   . VAL A 165 ? 0.25843 0.24830 0.18223 0.07835  -0.01737 -0.07915 172 VAL A O   
1209 C CB  . VAL A 165 ? 0.20893 0.22375 0.16231 0.04993  -0.00071 -0.04759 172 VAL A CB  
1210 C CG1 . VAL A 165 ? 0.24861 0.26041 0.19510 0.04715  -0.00477 -0.04705 172 VAL A CG1 
1211 C CG2 . VAL A 165 ? 0.20367 0.22515 0.17389 0.03827  0.00546  -0.03638 172 VAL A CG2 
1212 N N   . ARG A 166 ? 0.25559 0.22432 0.19497 0.05635  -0.02903 -0.07741 173 ARG A N   
1213 C CA  . ARG A 166 ? 0.27285 0.23117 0.19736 0.06497  -0.04052 -0.09191 173 ARG A CA  
1214 C C   . ARG A 166 ? 0.26518 0.22422 0.19257 0.05631  -0.04690 -0.09058 173 ARG A C   
1215 O O   . ARG A 166 ? 0.25797 0.21836 0.20175 0.04303  -0.04460 -0.08059 173 ARG A O   
1216 C CB  . ARG A 166 ? 0.32331 0.25519 0.25072 0.06620  -0.05178 -0.10393 173 ARG A CB  
1217 C CG  . ARG A 166 ? 0.34225 0.25876 0.29126 0.04878  -0.05770 -0.09914 173 ARG A CG  
1218 C CD  . ARG A 166 ? 0.41547 0.30648 0.37023 0.04924  -0.06473 -0.10493 173 ARG A CD  
1219 N NE  . ARG A 166 ? 0.47973 0.37559 0.43807 0.05295  -0.05426 -0.09673 173 ARG A NE  
1220 C CZ  . ARG A 166 ? 0.56167 0.43886 0.52103 0.05841  -0.05744 -0.09999 173 ARG A CZ  
1221 N NH1 . ARG A 166 ? 0.54944 0.40398 0.50830 0.05830  -0.06866 -0.10733 173 ARG A NH1 
1222 N NH2 . ARG A 166 ? 0.54107 0.42767 0.50419 0.06212  -0.04790 -0.09147 173 ARG A NH2 
1223 N N   . THR A 167 ? 0.32130 0.28103 0.23147 0.06575  -0.05531 -0.10131 174 THR A N   
1224 C CA  . THR A 167 ? 0.32104 0.28027 0.23487 0.05866  -0.06511 -0.10292 174 THR A CA  
1225 C C   . THR A 167 ? 0.35125 0.29079 0.28517 0.04543  -0.07662 -0.10781 174 THR A C   
1226 O O   . THR A 167 ? 0.42703 0.34716 0.36151 0.04727  -0.08385 -0.11793 174 THR A O   
1227 C CB  . THR A 167 ? 0.42218 0.38567 0.31168 0.07309  -0.07423 -0.11583 174 THR A CB  
1228 O OG1 . THR A 167 ? 0.44995 0.43495 0.32153 0.08524  -0.06137 -0.10751 174 THR A OG1 
1229 C CG2 . THR A 167 ? 0.47257 0.43824 0.36715 0.06617  -0.08597 -0.11783 174 THR A CG2 
1230 N N   . ASP A 168 ? 0.31751 0.26243 0.26890 0.03241  -0.07777 -0.09927 175 ASP A N   
1231 C CA  . ASP A 168 ? 0.35939 0.29167 0.33386 0.01816  -0.08600 -0.09925 175 ASP A CA  
1232 C C   . ASP A 168 ? 0.46556 0.39338 0.44153 0.01588  -0.10403 -0.11168 175 ASP A C   
1233 O O   . ASP A 168 ? 0.48206 0.42555 0.45342 0.01799  -0.10720 -0.11135 175 ASP A O   
1234 C CB  . ASP A 168 ? 0.33282 0.27708 0.32638 0.00673  -0.07693 -0.08312 175 ASP A CB  
1235 C CG  . ASP A 168 ? 0.44018 0.37578 0.45838 -0.00734 -0.08193 -0.07939 175 ASP A CG  
1236 O OD1 . ASP A 168 ? 0.57069 0.48810 0.59249 -0.00911 -0.08470 -0.08264 175 ASP A OD1 
1237 O OD2 . ASP A 168 ? 0.37319 0.32105 0.40746 -0.01589 -0.08275 -0.07214 175 ASP A OD2 
1238 N N   . THR A 169 ? 0.58484 0.49547 0.56908 0.01163  -0.11123 -0.11622 176 THR A N   
1239 C CA  . THR A 169 ? 0.76779 0.67608 0.75952 0.00645  -0.12471 -0.12248 176 THR A CA  
1240 C C   . THR A 169 ? 0.67833 0.58755 0.70080 -0.01236 -0.12773 -0.11291 176 THR A C   
1241 O O   . THR A 169 ? 0.70179 0.60979 0.73494 -0.01929 -0.13891 -0.11688 176 THR A O   
1242 C CB  . THR A 169 ? 0.78923 0.67787 0.76985 0.01429  -0.13226 -0.13439 176 THR A CB  
1243 O OG1 . THR A 169 ? 0.73938 0.61145 0.72342 0.01389  -0.12605 -0.13063 176 THR A OG1 
1244 C CG2 . THR A 169 ? 0.62290 0.51854 0.57383 0.03384  -0.13219 -0.14467 176 THR A CG2 
1245 N N   . GLY A 170 ? 0.66897 0.58226 0.70603 -0.02032 -0.11775 -0.10003 177 GLY A N   
1246 C CA  . GLY A 170 ? 0.63638 0.55585 0.70217 -0.03651 -0.11784 -0.08830 177 GLY A CA  
1247 C C   . GLY A 170 ? 0.46470 0.40839 0.54182 -0.04115 -0.12223 -0.08567 177 GLY A C   
1248 O O   . GLY A 170 ? 0.46386 0.41662 0.52682 -0.03275 -0.12852 -0.09432 177 GLY A O   
1249 N N   . GLU A 171 ? 0.43356 0.39014 0.53654 -0.05350 -0.11817 -0.07227 178 GLU A N   
1250 C CA  . GLU A 171 ? 0.42303 0.40619 0.54173 -0.05811 -0.12175 -0.06775 178 GLU A CA  
1251 C C   . GLU A 171 ? 0.42040 0.41894 0.52582 -0.04695 -0.11835 -0.06861 178 GLU A C   
1252 O O   . GLU A 171 ? 0.32083 0.31883 0.41725 -0.04168 -0.10256 -0.05975 178 GLU A O   
1253 C CB  . GLU A 171 ? 0.45846 0.45530 0.60619 -0.07084 -0.11420 -0.05097 178 GLU A CB  
1254 C CG  . GLU A 171 ? 0.48280 0.50563 0.65294 -0.07858 -0.11974 -0.04621 178 GLU A CG  
1255 C CD  . GLU A 171 ? 0.38574 0.39978 0.55967 -0.08503 -0.13377 -0.05574 178 GLU A CD  
1256 O OE1 . GLU A 171 ? 0.45749 0.45058 0.63619 -0.09242 -0.13556 -0.05554 178 GLU A OE1 
1257 O OE2 . GLU A 171 ? 0.45490 0.48275 0.62658 -0.08196 -0.14367 -0.06352 178 GLU A OE2 
1258 N N   . PRO A 172 ? 0.40257 0.41443 0.49946 -0.04014 -0.12702 -0.07546 179 PRO A N   
1259 C CA  . PRO A 172 ? 0.40615 0.43180 0.48510 -0.02701 -0.11724 -0.07009 179 PRO A CA  
1260 C C   . PRO A 172 ? 0.43539 0.47785 0.53032 -0.02963 -0.10412 -0.05399 179 PRO A C   
1261 O O   . PRO A 172 ? 0.47302 0.52992 0.59530 -0.03984 -0.10655 -0.04761 179 PRO A O   
1262 C CB  . PRO A 172 ? 0.43632 0.47599 0.51123 -0.02208 -0.13254 -0.07898 179 PRO A CB  
1263 C CG  . PRO A 172 ? 0.60037 0.62079 0.66755 -0.02417 -0.14364 -0.09292 179 PRO A CG  
1264 C CD  . PRO A 172 ? 0.57487 0.58320 0.66560 -0.03943 -0.14025 -0.08689 179 PRO A CD  
1265 N N   . MET A 173 ? 0.31264 0.35382 0.39064 -0.01994 -0.09032 -0.04737 180 MET A N   
1266 C CA  . MET A 173 ? 0.30935 0.36240 0.39743 -0.01940 -0.07818 -0.03458 180 MET A CA  
1267 C C   . MET A 173 ? 0.41449 0.48306 0.49712 -0.00903 -0.07711 -0.03022 180 MET A C   
1268 O O   . MET A 173 ? 0.36461 0.44431 0.45654 -0.00677 -0.06913 -0.02124 180 MET A O   
1269 C CB  . MET A 173 ? 0.38785 0.42644 0.46414 -0.01692 -0.06415 -0.02989 180 MET A CB  
1270 C CG  . MET A 173 ? 0.57365 0.59363 0.64627 -0.02188 -0.06422 -0.03482 180 MET A CG  
1271 S SD  . MET A 173 ? 0.54217 0.55099 0.59840 -0.01610 -0.04947 -0.03016 180 MET A SD  
1272 C CE  . MET A 173 ? 0.36567 0.38798 0.42617 -0.01183 -0.04106 -0.02028 180 MET A CE  
1273 N N   . GLY A 174 ? 0.30258 0.37162 0.36848 -0.00081 -0.08456 -0.03597 181 GLY A N   
1274 C CA  . GLY A 174 ? 0.26090 0.34229 0.31994 0.01043  -0.08369 -0.03033 181 GLY A CA  
1275 C C   . GLY A 174 ? 0.20763 0.27502 0.24676 0.01884  -0.07093 -0.02346 181 GLY A C   
1276 O O   . GLY A 174 ? 0.24256 0.30493 0.26078 0.02759  -0.07137 -0.02316 181 GLY A O   
1277 N N   . ARG A 175 ? 0.17448 0.23597 0.22017 0.01606  -0.05995 -0.01747 182 ARG A N   
1278 C CA  . ARG A 175 ? 0.18165 0.22735 0.21222 0.02091  -0.04921 -0.01207 182 ARG A CA  
1279 C C   . ARG A 175 ? 0.18456 0.22590 0.22544 0.01568  -0.04070 -0.00949 182 ARG A C   
1280 O O   . ARG A 175 ? 0.19918 0.25406 0.25649 0.01447  -0.04039 -0.00718 182 ARG A O   
1281 C CB  . ARG A 175 ? 0.21002 0.25744 0.23247 0.03245  -0.04798 -0.00507 182 ARG A CB  
1282 C CG  . ARG A 175 ? 0.21391 0.24141 0.22222 0.03562  -0.03863 0.00098  182 ARG A CG  
1283 C CD  . ARG A 175 ? 0.20341 0.22762 0.20903 0.04609  -0.03683 0.00810  182 ARG A CD  
1284 N NE  . ARG A 175 ? 0.20812 0.24223 0.22899 0.04815  -0.03561 0.00734  182 ARG A NE  
1285 C CZ  . ARG A 175 ? 0.19552 0.24932 0.22653 0.05530  -0.04050 0.00839  182 ARG A CZ  
1286 N NH1 . ARG A 175 ? 0.19475 0.25986 0.22248 0.06073  -0.04863 0.00928  182 ARG A NH1 
1287 N NH2 . ARG A 175 ? 0.19116 0.25654 0.23588 0.05809  -0.03720 0.00876  182 ARG A NH2 
1288 N N   . GLY A 176 ? 0.24931 0.29663 0.19770 0.05624  -0.02074 0.05953  183 GLY A N   
1289 C CA  . GLY A 176 ? 0.21705 0.25093 0.19623 0.04624  -0.01006 0.05194  183 GLY A CA  
1290 C C   . GLY A 176 ? 0.20499 0.23072 0.17893 0.03677  -0.00467 0.03577  183 GLY A C   
1291 O O   . GLY A 176 ? 0.22544 0.25214 0.17169 0.04313  -0.00031 0.03478  183 GLY A O   
1292 N N   . THR A 177 ? 0.17794 0.19668 0.17545 0.02611  -0.00295 0.02526  184 THR A N   
1293 C CA  . THR A 177 ? 0.16599 0.18045 0.16479 0.01923  0.00254  0.01419  184 THR A CA  
1294 C C   . THR A 177 ? 0.19500 0.20658 0.20725 0.01043  -0.00650 -0.00080 184 THR A C   
1295 O O   . THR A 177 ? 0.16755 0.18045 0.19839 0.00747  -0.00837 0.00099  184 THR A O   
1296 C CB  . THR A 177 ? 0.17465 0.18383 0.18967 0.01128  0.01585  0.02505  184 THR A CB  
1297 O OG1 . THR A 177 ? 0.21745 0.23271 0.22307 0.01656  0.02551  0.04451  184 THR A OG1 
1298 C CG2 . THR A 177 ? 0.18779 0.20551 0.21281 0.00509  0.01949  0.01863  184 THR A CG2 
1299 N N   . LYS A 178 ? 0.18333 0.18900 0.18263 0.00994  -0.00956 -0.01300 185 LYS A N   
1300 C CA  . LYS A 178 ? 0.19012 0.18824 0.19912 0.00068  -0.01711 -0.02419 185 LYS A CA  
1301 C C   . LYS A 178 ? 0.18553 0.17967 0.19702 0.00309  -0.00666 -0.02694 185 LYS A C   
1302 O O   . LYS A 178 ? 0.20707 0.19880 0.19821 0.01600  0.00006  -0.02762 185 LYS A O   
1303 C CB  . LYS A 178 ? 0.27637 0.26058 0.26028 -0.00263 -0.03563 -0.03457 185 LYS A CB  
1304 C CG  . LYS A 178 ? 0.39620 0.36141 0.38098 -0.01342 -0.04442 -0.04438 185 LYS A CG  
1305 C CD  . LYS A 178 ? 0.47676 0.42535 0.44147 -0.02777 -0.07074 -0.05066 185 LYS A CD  
1306 C CE  . LYS A 178 ? 0.49902 0.42633 0.41180 -0.01705 -0.07966 -0.05910 185 LYS A CE  
1307 N NZ  . LYS A 178 ? 0.59365 0.48955 0.47530 -0.03294 -0.10492 -0.06830 185 LYS A NZ  
1308 N N   . VAL A 179 ? 0.16761 0.16414 0.20133 -0.00574 -0.00434 -0.02607 186 VAL A N   
1309 C CA  . VAL A 179 ? 0.14510 0.14607 0.18618 -0.00528 0.00117  -0.02506 186 VAL A CA  
1310 C C   . VAL A 179 ? 0.17625 0.16303 0.21443 -0.00727 -0.00539 -0.03369 186 VAL A C   
1311 O O   . VAL A 179 ? 0.16950 0.15427 0.21820 -0.01682 -0.00933 -0.03430 186 VAL A O   
1312 C CB  . VAL A 179 ? 0.13267 0.14052 0.19163 -0.01698 0.00323  -0.01747 186 VAL A CB  
1313 C CG1 . VAL A 179 ? 0.15162 0.17349 0.22199 -0.01930 0.00294  -0.01355 186 VAL A CG1 
1314 C CG2 . VAL A 179 ? 0.15895 0.17281 0.22059 -0.01959 0.00832  -0.00528 186 VAL A CG2 
1315 N N   . ILE A 180 ? 0.18021 0.15397 0.20052 0.00461  -0.00438 -0.03806 187 ILE A N   
1316 C CA  . ILE A 180 ? 0.17943 0.12766 0.19081 0.00304  -0.01115 -0.04429 187 ILE A CA  
1317 C C   . ILE A 180 ? 0.17150 0.13208 0.19523 0.01081  -0.00383 -0.03671 187 ILE A C   
1318 O O   . ILE A 180 ? 0.19907 0.17042 0.21845 0.02980  0.00588  -0.03097 187 ILE A O   
1319 C CB  . ILE A 180 ? 0.23667 0.14397 0.20698 0.01325  -0.01744 -0.05570 187 ILE A CB  
1320 C CG1 . ILE A 180 ? 0.27135 0.17397 0.22682 0.00463  -0.02921 -0.06110 187 ILE A CG1 
1321 C CG2 . ILE A 180 ? 0.28536 0.15353 0.24419 0.00599  -0.02752 -0.06026 187 ILE A CG2 
1322 C CD1 . ILE A 180 ? 0.38672 0.24167 0.28667 0.01456  -0.03839 -0.07482 187 ILE A CD1 
1323 N N   . LEU A 181 ? 0.18030 0.14456 0.21887 -0.00108 -0.00771 -0.03347 188 LEU A N   
1324 C CA  . LEU A 181 ? 0.15621 0.13502 0.20479 0.00390  -0.00566 -0.02451 188 LEU A CA  
1325 C C   . LEU A 181 ? 0.20796 0.15551 0.24094 0.01254  -0.00739 -0.02473 188 LEU A C   
1326 O O   . LEU A 181 ? 0.22400 0.15255 0.25461 -0.00054 -0.01308 -0.02563 188 LEU A O   
1327 C CB  . LEU A 181 ? 0.15747 0.14954 0.21721 -0.01200 -0.00987 -0.02166 188 LEU A CB  
1328 C CG  . LEU A 181 ? 0.16602 0.16919 0.23157 -0.02215 -0.01008 -0.02268 188 LEU A CG  
1329 C CD1 . LEU A 181 ? 0.23556 0.23100 0.29284 -0.03262 -0.01412 -0.02447 188 LEU A CD1 
1330 C CD2 . LEU A 181 ? 0.18090 0.21116 0.26050 -0.02098 -0.00911 -0.01278 188 LEU A CD2 
1331 N N   . HIS A 182 ? 0.19551 0.13812 0.21830 0.03636  -0.00077 -0.02017 189 HIS A N   
1332 C CA  . HIS A 182 ? 0.23834 0.14193 0.24110 0.04964  -0.00119 -0.01787 189 HIS A CA  
1333 C C   . HIS A 182 ? 0.21850 0.15463 0.24318 0.04936  -0.00230 -0.00181 189 HIS A C   
1334 O O   . HIS A 182 ? 0.22971 0.20588 0.27095 0.06544  0.00235  0.01173  189 HIS A O   
1335 C CB  . HIS A 182 ? 0.26115 0.13912 0.23434 0.08437  0.00969  -0.01963 189 HIS A CB  
1336 C CG  . HIS A 182 ? 0.33727 0.18499 0.27885 0.08632  0.00936  -0.03630 189 HIS A CG  
1337 N ND1 . HIS A 182 ? 0.44399 0.23741 0.34929 0.07644  -0.00047 -0.04854 189 HIS A ND1 
1338 C CD2 . HIS A 182 ? 0.36721 0.24688 0.31442 0.08764  0.01528  -0.03772 189 HIS A CD2 
1339 C CE1 . HIS A 182 ? 0.42863 0.21868 0.31364 0.07536  -0.00208 -0.05828 189 HIS A CE1 
1340 N NE2 . HIS A 182 ? 0.42811 0.26345 0.33350 0.08588  0.00890  -0.05320 189 HIS A NE2 
1341 N N   . LEU A 183 ? 0.23583 0.16132 0.26146 0.03077  -0.00907 -0.00006 190 LEU A N   
1342 C CA  . LEU A 183 ? 0.21624 0.17353 0.25406 0.02638  -0.01284 0.01248  190 LEU A CA  
1343 C C   . LEU A 183 ? 0.26144 0.21766 0.29526 0.04919  -0.01161 0.02885  190 LEU A C   
1344 O O   . LEU A 183 ? 0.29599 0.20606 0.30982 0.06483  -0.00723 0.03020  190 LEU A O   
1345 C CB  . LEU A 183 ? 0.23569 0.18212 0.26831 0.00679  -0.01521 0.01237  190 LEU A CB  
1346 C CG  . LEU A 183 ? 0.22944 0.18464 0.26778 -0.00971 -0.01426 0.00141  190 LEU A CG  
1347 C CD1 . LEU A 183 ? 0.25615 0.20818 0.29055 -0.02010 -0.01062 0.00791  190 LEU A CD1 
1348 C CD2 . LEU A 183 ? 0.24086 0.22462 0.28446 -0.01288 -0.01750 -0.00264 190 LEU A CD2 
1349 N N   . LYS A 184 ? 0.22233 0.22614 0.27207 0.05052  -0.01800 0.04247  191 LYS A N   
1350 C CA  . LYS A 184 ? 0.23716 0.25051 0.28627 0.07153  -0.01955 0.06328  191 LYS A CA  
1351 C C   . LYS A 184 ? 0.26825 0.23919 0.29370 0.06633  -0.02011 0.06741  191 LYS A C   
1352 O O   . LYS A 184 ? 0.28300 0.24140 0.30033 0.04327  -0.02133 0.05884  191 LYS A O   
1353 C CB  . LYS A 184 ? 0.23787 0.31658 0.30900 0.06498  -0.03391 0.07849  191 LYS A CB  
1354 C CG  . LYS A 184 ? 0.21250 0.34498 0.31707 0.06419  -0.03510 0.08362  191 LYS A CG  
1355 C CD  . LYS A 184 ? 0.26975 0.45804 0.39312 0.03998  -0.05860 0.09567  191 LYS A CD  
1356 C CE  . LYS A 184 ? 0.34756 0.58320 0.50564 0.02617  -0.06146 0.10145  191 LYS A CE  
1357 N NZ  . LYS A 184 ? 0.33708 0.60613 0.50286 -0.00002 -0.08151 0.11098  191 LYS A NZ  
1358 N N   . GLU A 185 ? 0.32573 0.27668 0.34091 0.09105  -0.01688 0.08485  192 GLU A N   
1359 C CA  . GLU A 185 ? 0.39134 0.29522 0.38394 0.08684  -0.01569 0.09438  192 GLU A CA  
1360 C C   . GLU A 185 ? 0.38978 0.32194 0.37851 0.06733  -0.02237 0.10170  192 GLU A C   
1361 O O   . GLU A 185 ? 0.43334 0.33700 0.40902 0.05296  -0.01781 0.10597  192 GLU A O   
1362 C CB  . GLU A 185 ? 0.47388 0.35200 0.45364 0.12158  -0.01143 0.11578  192 GLU A CB  
1363 C CG  . GLU A 185 ? 0.76999 0.57480 0.72256 0.11624  -0.00872 0.12254  192 GLU A CG  
1364 C CD  . GLU A 185 ? 1.03862 0.82638 0.98071 0.14198  -0.00693 0.13464  192 GLU A CD  
1365 O OE1 . GLU A 185 ? 0.96208 0.80166 0.91900 0.16642  -0.00593 0.14327  192 GLU A OE1 
1366 O OE2 . GLU A 185 ? 1.05368 0.77994 0.97643 0.13578  -0.00705 0.13796  192 GLU A OE2 
1367 N N   . ASP A 186 ? 0.31935 0.30611 0.31577 0.06613  -0.03374 0.10512  193 ASP A N   
1368 C CA  . ASP A 186 ? 0.31704 0.32018 0.29229 0.05250  -0.04191 0.10950  193 ASP A CA  
1369 C C   . ASP A 186 ? 0.31480 0.32316 0.28296 0.02917  -0.04320 0.08688  193 ASP A C   
1370 O O   . ASP A 186 ? 0.31770 0.33437 0.25705 0.02124  -0.05079 0.08551  193 ASP A O   
1371 C CB  . ASP A 186 ? 0.36082 0.40992 0.33543 0.06260  -0.06009 0.12780  193 ASP A CB  
1372 C CG  . ASP A 186 ? 0.36115 0.46059 0.36475 0.05535  -0.07480 0.12240  193 ASP A CG  
1373 O OD1 . ASP A 186 ? 0.43364 0.52989 0.45900 0.05157  -0.06614 0.10772  193 ASP A OD1 
1374 O OD2 . ASP A 186 ? 0.49142 0.63650 0.49663 0.05149  -0.09694 0.13610  193 ASP A OD2 
1375 N N   . GLN A 187 ? 0.26941 0.26670 0.25535 0.02137  -0.03568 0.06945  194 GLN A N   
1376 C CA  . GLN A 187 ? 0.26213 0.26053 0.24254 0.00456  -0.03499 0.05010  194 GLN A CA  
1377 C C   . GLN A 187 ? 0.26916 0.24296 0.25275 -0.00160 -0.01934 0.04483  194 GLN A C   
1378 O O   . GLN A 187 ? 0.26083 0.23499 0.25061 -0.00977 -0.01590 0.03035  194 GLN A O   
1379 C CB  . GLN A 187 ? 0.25429 0.27410 0.25663 -0.00120 -0.04305 0.03910  194 GLN A CB  
1380 C CG  . GLN A 187 ? 0.24248 0.30200 0.25333 -0.00143 -0.06196 0.05071  194 GLN A CG  
1381 C CD  . GLN A 187 ? 0.32018 0.38076 0.29478 -0.01411 -0.07919 0.04977  194 GLN A CD  
1382 O OE1 . GLN A 187 ? 0.32466 0.35636 0.26674 -0.02416 -0.07681 0.03336  194 GLN A OE1 
1383 N NE2 . GLN A 187 ? 0.31310 0.40543 0.28792 -0.01067 -0.09711 0.06802  194 GLN A NE2 
1384 N N   . THR A 188 ? 0.30079 0.25580 0.28270 0.00057  -0.01133 0.06042  195 THR A N   
1385 C CA  . THR A 188 ? 0.29819 0.23963 0.29312 -0.01144 -0.00109 0.06203  195 THR A CA  
1386 C C   . THR A 188 ? 0.28878 0.24834 0.27431 -0.01487 0.01113  0.06546  195 THR A C   
1387 O O   . THR A 188 ? 0.29366 0.25877 0.29928 -0.02456 0.02003  0.07184  195 THR A O   
1388 C CB  . THR A 188 ? 0.31920 0.22933 0.31761 -0.01459 0.00037  0.08103  195 THR A CB  
1389 O OG1 . THR A 188 ? 0.38419 0.29761 0.36414 -0.00765 0.00508  0.10314  195 THR A OG1 
1390 C CG2 . THR A 188 ? 0.37578 0.25456 0.37309 -0.00317 -0.00785 0.07485  195 THR A CG2 
1391 N N   . GLU A 189 ? 0.28818 0.25690 0.24067 -0.00570 0.01120  0.06269  196 GLU A N   
1392 C CA  . GLU A 189 ? 0.28728 0.26396 0.21786 0.00017  0.02684  0.06276  196 GLU A CA  
1393 C C   . GLU A 189 ? 0.27123 0.25124 0.21786 -0.00254 0.03079  0.04631  196 GLU A C   
1394 O O   . GLU A 189 ? 0.27535 0.26720 0.22060 0.00529  0.04896  0.05271  196 GLU A O   
1395 C CB  . GLU A 189 ? 0.32017 0.28860 0.19465 0.01117  0.02133  0.05530  196 GLU A CB  
1396 C CG  . GLU A 189 ? 0.30563 0.26332 0.16660 0.00460  0.00040  0.03047  196 GLU A CG  
1397 C CD  . GLU A 189 ? 0.39388 0.33960 0.19859 0.00685  -0.01645 0.02554  196 GLU A CD  
1398 O OE1 . GLU A 189 ? 0.44515 0.40504 0.25188 0.00564  -0.03119 0.03848  196 GLU A OE1 
1399 O OE2 . GLU A 189 ? 0.43660 0.35447 0.18914 0.01155  -0.01592 0.00932  196 GLU A OE2 
1400 N N   . TYR A 190 ? 0.26018 0.23425 0.22271 -0.01005 0.01632  0.02925  197 TYR A N   
1401 C CA  . TYR A 190 ? 0.22629 0.20113 0.20132 -0.01188 0.01861  0.01554  197 TYR A CA  
1402 C C   . TYR A 190 ? 0.22145 0.20965 0.23655 -0.01971 0.02358  0.02423  197 TYR A C   
1403 O O   . TYR A 190 ? 0.24429 0.23694 0.27300 -0.02090 0.02332  0.01561  197 TYR A O   
1404 C CB  . TYR A 190 ? 0.22647 0.19366 0.20106 -0.01789 0.00217  -0.00113 197 TYR A CB  
1405 C CG  . TYR A 190 ? 0.24474 0.20074 0.18040 -0.01803 -0.00946 -0.00734 197 TYR A CG  
1406 C CD1 . TYR A 190 ? 0.30308 0.23432 0.19372 -0.01182 -0.00523 -0.01746 197 TYR A CD1 
1407 C CD2 . TYR A 190 ? 0.25147 0.21919 0.19006 -0.02263 -0.02596 -0.00165 197 TYR A CD2 
1408 C CE1 . TYR A 190 ? 0.34352 0.25298 0.18602 -0.01599 -0.02183 -0.02580 197 TYR A CE1 
1409 C CE2 . TYR A 190 ? 0.27005 0.23194 0.17278 -0.02813 -0.04345 -0.00511 197 TYR A CE2 
1410 C CZ  . TYR A 190 ? 0.31204 0.24006 0.16276 -0.02764 -0.04364 -0.01916 197 TYR A CZ  
1411 O OH  . TYR A 190 ? 0.38422 0.29400 0.18654 -0.03685 -0.06651 -0.02589 197 TYR A OH  
1412 N N   . LEU A 191 ? 0.22069 0.21235 0.25237 -0.02757 0.02506  0.04263  198 LEU A N   
1413 C CA  . LEU A 191 ? 0.20628 0.21150 0.27340 -0.04210 0.02556  0.05587  198 LEU A CA  
1414 C C   . LEU A 191 ? 0.25303 0.29318 0.33402 -0.04004 0.04422  0.08242  198 LEU A C   
1415 O O   . LEU A 191 ? 0.24757 0.31378 0.36708 -0.05544 0.04338  0.09990  198 LEU A O   
1416 C CB  . LEU A 191 ? 0.21657 0.19305 0.29158 -0.05779 0.01154  0.06140  198 LEU A CB  
1417 C CG  . LEU A 191 ? 0.22736 0.17261 0.28786 -0.05219 -0.00158 0.03985  198 LEU A CG  
1418 C CD1 . LEU A 191 ? 0.32312 0.22468 0.37674 -0.05937 -0.01187 0.04511  198 LEU A CD1 
1419 C CD2 . LEU A 191 ? 0.29605 0.24834 0.36516 -0.05384 -0.00676 0.02298  198 LEU A CD2 
1420 N N   . GLU A 192 ? 0.24021 0.28474 0.28996 -0.02159 0.06030  0.08882  199 GLU A N   
1421 C CA  . GLU A 192 ? 0.23284 0.31500 0.29068 -0.01222 0.08459  0.11858  199 GLU A CA  
1422 C C   . GLU A 192 ? 0.27550 0.38149 0.33058 0.01047  0.10249  0.11554  199 GLU A C   
1423 O O   . GLU A 192 ? 0.24655 0.32203 0.26063 0.02739  0.10132  0.08839  199 GLU A O   
1424 C CB  . GLU A 192 ? 0.32055 0.39192 0.33356 0.00302  0.09604  0.12780  199 GLU A CB  
1425 C CG  . GLU A 192 ? 0.36343 0.40771 0.37398 -0.01243 0.07937  0.13270  199 GLU A CG  
1426 C CD  . GLU A 192 ? 0.65594 0.69627 0.62287 0.00326  0.09035  0.14791  199 GLU A CD  
1427 O OE1 . GLU A 192 ? 0.92887 0.99593 0.88394 0.01875  0.11406  0.16642  199 GLU A OE1 
1428 O OE2 . GLU A 192 ? 0.75801 0.77109 0.70205 0.00307  0.07442  0.14108  199 GLU A OE2 
1429 N N   . GLU A 193 ? 0.19635 0.22877 0.34006 -0.03775 -0.02765 0.01723  200 GLU A N   
1430 C CA  . GLU A 193 ? 0.19700 0.24503 0.32430 -0.03827 -0.03798 0.02025  200 GLU A CA  
1431 C C   . GLU A 193 ? 0.18575 0.25311 0.29223 -0.02221 -0.02115 0.03578  200 GLU A C   
1432 O O   . GLU A 193 ? 0.19460 0.26331 0.26713 -0.01892 -0.02279 0.02806  200 GLU A O   
1433 C CB  . GLU A 193 ? 0.21789 0.27801 0.40223 -0.04827 -0.05118 0.03506  200 GLU A CB  
1434 C CG  . GLU A 193 ? 0.25590 0.33302 0.43733 -0.05042 -0.06484 0.04175  200 GLU A CG  
1435 C CD  . GLU A 193 ? 0.55326 0.64905 0.80815 -0.06002 -0.07854 0.06434  200 GLU A CD  
1436 O OE1 . GLU A 193 ? 0.35468 0.44961 0.66414 -0.06451 -0.07505 0.07503  200 GLU A OE1 
1437 O OE2 . GLU A 193 ? 0.45377 0.56710 0.72189 -0.06312 -0.09280 0.07558  200 GLU A OE2 
1438 N N   . ARG A 194 ? 0.21865 0.29934 0.34349 -0.01226 -0.00426 0.05780  201 ARG A N   
1439 C CA  . ARG A 194 ? 0.21427 0.30793 0.30717 0.00152  0.01115  0.06721  201 ARG A CA  
1440 C C   . ARG A 194 ? 0.19654 0.28167 0.23900 0.00377  0.00831  0.04939  201 ARG A C   
1441 O O   . ARG A 194 ? 0.22530 0.31075 0.23537 0.00917  0.01266  0.04234  201 ARG A O   
1442 C CB  . ARG A 194 ? 0.24414 0.35408 0.35440 0.01230  0.03042  0.09640  201 ARG A CB  
1443 C CG  . ARG A 194 ? 0.37359 0.48433 0.49740 0.01226  0.03084  0.10728  201 ARG A CG  
1444 C CD  . ARG A 194 ? 0.43553 0.56738 0.55950 0.02597  0.05095  0.14150  201 ARG A CD  
1445 N NE  . ARG A 194 ? 0.50027 0.63915 0.63373 0.02809  0.05017  0.15897  201 ARG A NE  
1446 C CZ  . ARG A 194 ? 0.41480 0.57404 0.56717 0.03829  0.06565  0.19759  201 ARG A CZ  
1447 N NH1 . ARG A 194 ? 0.52102 0.69360 0.68176 0.04838  0.08707  0.22158  201 ARG A NH1 
1448 N NH2 . ARG A 194 ? 0.52964 0.69802 0.69750 0.04007  0.06233  0.21753  201 ARG A NH2 
1449 N N   . ARG A 195 ? 0.18912 0.26484 0.23335 -0.00052 0.00259  0.04250  202 ARG A N   
1450 C CA  . ARG A 195 ? 0.20653 0.27752 0.21966 0.00079  -0.00075 0.03092  202 ARG A CA  
1451 C C   . ARG A 195 ? 0.20585 0.26439 0.19877 -0.00320 -0.00658 0.01085  202 ARG A C   
1452 O O   . ARG A 195 ? 0.19402 0.25301 0.16397 -0.00062 -0.00702 0.00428  202 ARG A O   
1453 C CB  . ARG A 195 ? 0.21336 0.27916 0.24946 -0.00038 0.00018  0.03540  202 ARG A CB  
1454 C CG  . ARG A 195 ? 0.21716 0.28369 0.24044 0.00103  -0.00321 0.03191  202 ARG A CG  
1455 C CD  . ARG A 195 ? 0.22215 0.30873 0.22244 0.00437  -0.01050 0.04356  202 ARG A CD  
1456 N NE  . ARG A 195 ? 0.20603 0.29772 0.21307 0.00247  -0.01980 0.04597  202 ARG A NE  
1457 C CZ  . ARG A 195 ? 0.24012 0.33289 0.22452 -0.00112 -0.03111 0.03471  202 ARG A CZ  
1458 N NH1 . ARG A 195 ? 0.26430 0.35030 0.21255 -0.00165 -0.03151 0.01832  202 ARG A NH1 
1459 N NH2 . ARG A 195 ? 0.20779 0.30769 0.21621 -0.00438 -0.04103 0.04148  202 ARG A NH2 
1460 N N   . ILE A 196 ? 0.19129 0.23827 0.19200 -0.01033 -0.01236 0.00179  203 ILE A N   
1461 C CA  . ILE A 196 ? 0.19455 0.23360 0.17122 -0.01300 -0.01793 -0.01068 203 ILE A CA  
1462 C C   . ILE A 196 ? 0.22066 0.27223 0.19586 -0.00909 -0.01804 -0.00350 203 ILE A C   
1463 O O   . ILE A 196 ? 0.21861 0.26827 0.17869 -0.00577 -0.01547 -0.00751 203 ILE A O   
1464 C CB  . ILE A 196 ? 0.20219 0.22653 0.17468 -0.02313 -0.02842 -0.02225 203 ILE A CB  
1465 C CG1 . ILE A 196 ? 0.22702 0.22904 0.19933 -0.02481 -0.02005 -0.03479 203 ILE A CG1 
1466 C CG2 . ILE A 196 ? 0.24734 0.26950 0.18798 -0.02465 -0.03537 -0.02765 203 ILE A CG2 
1467 C CD1 . ILE A 196 ? 0.28088 0.26107 0.24944 -0.03729 -0.03054 -0.05225 203 ILE A CD1 
1468 N N   . LYS A 197 ? 0.19350 0.25703 0.19391 -0.00830 -0.01713 0.00973  204 LYS A N   
1469 C CA  . LYS A 197 ? 0.18896 0.26218 0.19803 -0.00168 -0.00974 0.01913  204 LYS A CA  
1470 C C   . LYS A 197 ? 0.20494 0.27276 0.18840 0.00727  0.00456  0.01180  204 LYS A C   
1471 O O   . LYS A 197 ? 0.21368 0.27708 0.19417 0.01102  0.00993  0.00797  204 LYS A O   
1472 C CB  . LYS A 197 ? 0.18802 0.27547 0.23672 0.00089  -0.00301 0.03912  204 LYS A CB  
1473 C CG  . LYS A 197 ? 0.27182 0.36833 0.36025 -0.01039 -0.02239 0.04915  204 LYS A CG  
1474 C CD  . LYS A 197 ? 0.27959 0.39297 0.42341 -0.00668 -0.01185 0.07473  204 LYS A CD  
1475 C CE  . LYS A 197 ? 0.43395 0.56023 0.63099 -0.02122 -0.03758 0.08752  204 LYS A CE  
1476 N NZ  . LYS A 197 ? 0.50750 0.64927 0.77226 -0.02009 -0.02812 0.11409  204 LYS A NZ  
1477 N N   . GLU A 198 ? 0.19161 0.25941 0.15872 0.00965  0.00891  0.01060  205 GLU A N   
1478 C CA  . GLU A 198 ? 0.23717 0.29882 0.17180 0.01398  0.01464  0.00003  205 GLU A CA  
1479 C C   . GLU A 198 ? 0.21337 0.26453 0.14075 0.00900  0.00544  -0.01496 205 GLU A C   
1480 O O   . GLU A 198 ? 0.23389 0.27468 0.15108 0.01071  0.01013  -0.02662 205 GLU A O   
1481 C CB  . GLU A 198 ? 0.22401 0.29370 0.14241 0.01480  0.01256  0.00734  205 GLU A CB  
1482 C CG  . GLU A 198 ? 0.27373 0.33871 0.15095 0.01452  0.00790  -0.00509 205 GLU A CG  
1483 C CD  . GLU A 198 ? 0.27151 0.35156 0.13503 0.01383  -0.00124 0.00943  205 GLU A CD  
1484 O OE1 . GLU A 198 ? 0.29293 0.38125 0.18887 0.01008  -0.00979 0.02138  205 GLU A OE1 
1485 O OE2 . GLU A 198 ? 0.31577 0.39836 0.13508 0.01758  0.00129  0.00974  205 GLU A OE2 
1486 N N   . ILE A 199 ? 0.20306 0.25398 0.14002 0.00357  -0.00390 -0.01453 206 ILE A N   
1487 C CA  . ILE A 199 ? 0.22007 0.26341 0.15816 0.00084  -0.00757 -0.02234 206 ILE A CA  
1488 C C   . ILE A 199 ? 0.23127 0.26971 0.17647 0.00268  -0.00290 -0.02248 206 ILE A C   
1489 O O   . ILE A 199 ? 0.23170 0.26308 0.18328 0.00298  -0.00044 -0.02783 206 ILE A O   
1490 C CB  . ILE A 199 ? 0.21533 0.25722 0.16252 -0.00174 -0.00961 -0.01920 206 ILE A CB  
1491 C CG1 . ILE A 199 ? 0.23670 0.28683 0.19101 -0.00232 -0.01364 -0.01211 206 ILE A CG1 
1492 C CG2 . ILE A 199 ? 0.21862 0.25403 0.17370 -0.00185 -0.00659 -0.02117 206 ILE A CG2 
1493 C CD1 . ILE A 199 ? 0.24207 0.28697 0.21519 -0.00238 -0.00827 -0.00740 206 ILE A CD1 
1494 N N   . VAL A 200 ? 0.20253 0.24620 0.15342 0.00284  -0.00393 -0.01375 207 VAL A N   
1495 C CA  . VAL A 200 ? 0.17806 0.22374 0.14018 0.00493  -0.00254 -0.00534 207 VAL A CA  
1496 C C   . VAL A 200 ? 0.21324 0.25562 0.19197 0.01142  0.00993  -0.00540 207 VAL A C   
1497 O O   . VAL A 200 ? 0.22835 0.26486 0.22248 0.01425  0.01626  -0.00348 207 VAL A O   
1498 C CB  . VAL A 200 ? 0.18714 0.24332 0.15299 0.00065  -0.01418 0.00615  207 VAL A CB  
1499 C CG1 . VAL A 200 ? 0.19717 0.26370 0.18225 0.00335  -0.01603 0.02393  207 VAL A CG1 
1500 C CG2 . VAL A 200 ? 0.21631 0.26473 0.15560 -0.00585 -0.02269 -0.00168 207 VAL A CG2 
1501 N N   . LYS A 201 ? 0.20572 0.24895 0.18324 0.01516  0.01798  -0.00706 208 LYS A N   
1502 C CA  . LYS A 201 ? 0.22783 0.26026 0.21370 0.02344  0.03734  -0.01177 208 LYS A CA  
1503 C C   . LYS A 201 ? 0.22992 0.24164 0.19610 0.02113  0.03925  -0.03532 208 LYS A C   
1504 O O   . LYS A 201 ? 0.31689 0.31175 0.29829 0.02506  0.05282  -0.04351 208 LYS A O   
1505 C CB  . LYS A 201 ? 0.26343 0.29997 0.24401 0.03005  0.05110  -0.00705 208 LYS A CB  
1506 C CG  . LYS A 201 ? 0.30514 0.32456 0.28603 0.04167  0.07999  -0.01444 208 LYS A CG  
1507 C CD  . LYS A 201 ? 0.41570 0.43883 0.38160 0.05062  0.09924  -0.00758 208 LYS A CD  
1508 C CE  . LYS A 201 ? 0.51071 0.50999 0.46782 0.06491  0.13621  -0.01823 208 LYS A CE  
1509 N NZ  . LYS A 201 ? 0.64230 0.64981 0.60050 0.07819  0.16409  0.00016  208 LYS A NZ  
1510 N N   . LYS A 202 ? 0.27739 0.28991 0.21785 0.01373  0.02449  -0.04519 209 LYS A N   
1511 C CA  . LYS A 202 ? 0.30173 0.29837 0.22781 0.00746  0.01778  -0.06647 209 LYS A CA  
1512 C C   . LYS A 202 ? 0.26255 0.25295 0.22362 0.00332  0.01431  -0.06601 209 LYS A C   
1513 O O   . LYS A 202 ? 0.29437 0.26474 0.26653 0.00031  0.01731  -0.08258 209 LYS A O   
1514 C CB  . LYS A 202 ? 0.29932 0.30694 0.20141 0.00045  -0.00069 -0.06728 209 LYS A CB  
1515 C CG  . LYS A 202 ? 0.33976 0.33746 0.23099 -0.01020 -0.01802 -0.08583 209 LYS A CG  
1516 C CD  . LYS A 202 ? 0.47615 0.49111 0.34396 -0.01558 -0.03731 -0.07908 209 LYS A CD  
1517 C CE  . LYS A 202 ? 0.54286 0.55510 0.41116 -0.02995 -0.06417 -0.09198 209 LYS A CE  
1518 N NZ  . LYS A 202 ? 0.64121 0.67734 0.49559 -0.03520 -0.08664 -0.07677 209 LYS A NZ  
1519 N N   . HIS A 203 ? 0.25039 0.25496 0.22872 0.00330  0.01023  -0.04762 210 HIS A N   
1520 C CA  . HIS A 203 ? 0.23717 0.23943 0.24596 0.00072  0.00952  -0.04152 210 HIS A CA  
1521 C C   . HIS A 203 ? 0.24912 0.25641 0.28043 0.00768  0.02079  -0.02061 210 HIS A C   
1522 O O   . HIS A 203 ? 0.27594 0.28039 0.33798 0.00806  0.02612  -0.01131 210 HIS A O   
1523 C CB  . HIS A 203 ? 0.25825 0.27086 0.26600 -0.00313 0.00074  -0.03465 210 HIS A CB  
1524 C CG  . HIS A 203 ? 0.28096 0.29526 0.28052 -0.01103 -0.01495 -0.04598 210 HIS A CG  
1525 N ND1 . HIS A 203 ? 0.32576 0.33126 0.34054 -0.02022 -0.02717 -0.05965 210 HIS A ND1 
1526 C CD2 . HIS A 203 ? 0.34016 0.36558 0.32093 -0.01219 -0.02326 -0.04293 210 HIS A CD2 
1527 C CE1 . HIS A 203 ? 0.37503 0.38961 0.37465 -0.02736 -0.04603 -0.06318 210 HIS A CE1 
1528 N NE2 . HIS A 203 ? 0.35999 0.38782 0.34153 -0.02117 -0.04172 -0.05050 210 HIS A NE2 
1529 N N   . SER A 204 ? 0.31998 0.29143 0.18610 -0.04484 -0.06288 -0.08529 211 SER A N   
1530 C CA  . SER A 204 ? 0.29938 0.25627 0.18914 -0.03978 -0.05336 -0.08089 211 SER A CA  
1531 C C   . SER A 204 ? 0.30959 0.23617 0.18345 -0.02523 -0.03795 -0.08978 211 SER A C   
1532 O O   . SER A 204 ? 0.33870 0.26480 0.23178 -0.01470 -0.02706 -0.08146 211 SER A O   
1533 C CB  . SER A 204 ? 0.27972 0.26605 0.20143 -0.03205 -0.04937 -0.06284 211 SER A CB  
1534 O OG  . SER A 204 ? 0.32898 0.34365 0.26588 -0.04124 -0.06154 -0.05385 211 SER A OG  
1535 N N   . GLN A 205 ? 0.38334 0.28743 0.22139 -0.02351 -0.03675 -0.10673 212 GLN A N   
1536 C CA  . GLN A 205 ? 0.47402 0.35441 0.29599 -0.00467 -0.01961 -0.11396 212 GLN A CA  
1537 C C   . GLN A 205 ? 0.50940 0.35530 0.34257 -0.00173 -0.01266 -0.11641 212 GLN A C   
1538 O O   . GLN A 205 ? 0.57808 0.41475 0.41167 0.01778  0.00341  -0.11383 212 GLN A O   
1539 C CB  . GLN A 205 ? 0.59342 0.47098 0.38695 -0.00250 -0.01637 -0.12851 212 GLN A CB  
1540 C CG  . GLN A 205 ? 0.66629 0.52382 0.45204 -0.01801 -0.02699 -0.14628 212 GLN A CG  
1541 C CD  . GLN A 205 ? 0.86131 0.74791 0.64626 -0.03492 -0.04655 -0.14658 212 GLN A CD  
1542 O OE1 . GLN A 205 ? 0.54512 0.45710 0.34966 -0.04165 -0.05601 -0.13056 212 GLN A OE1 
1543 N NE2 . GLN A 205 ? 0.73520 0.61945 0.49790 -0.03937 -0.05322 -0.16437 212 GLN A NE2 
1544 N N   . PHE A 206 ? 0.43193 0.26359 0.27772 -0.02003 -0.02375 -0.11769 213 PHE A N   
1545 C CA  . PHE A 206 ? 0.46575 0.26110 0.32152 -0.01857 -0.01761 -0.11756 213 PHE A CA  
1546 C C   . PHE A 206 ? 0.45065 0.26638 0.34396 -0.02316 -0.01928 -0.09682 213 PHE A C   
1547 O O   . PHE A 206 ? 0.55501 0.34646 0.46057 -0.02992 -0.01947 -0.09262 213 PHE A O   
1548 C CB  . PHE A 206 ? 0.51440 0.28340 0.36429 -0.03462 -0.02576 -0.13163 213 PHE A CB  
1549 C CG  . PHE A 206 ? 0.59191 0.34793 0.41396 -0.02591 -0.02067 -0.15115 213 PHE A CG  
1550 C CD1 . PHE A 206 ? 0.61896 0.35686 0.43070 -0.00183 -0.00279 -0.15460 213 PHE A CD1 
1551 C CD2 . PHE A 206 ? 0.64234 0.40990 0.44962 -0.04066 -0.03374 -0.16504 213 PHE A CD2 
1552 C CE1 . PHE A 206 ? 0.69628 0.42539 0.48203 0.00648  0.00275  -0.17293 213 PHE A CE1 
1553 C CE2 . PHE A 206 ? 0.68812 0.44573 0.46703 -0.03276 -0.02918 -0.18489 213 PHE A CE2 
1554 C CZ  . PHE A 206 ? 0.68256 0.41993 0.45009 -0.00954 -0.01030 -0.18945 213 PHE A CZ  
1555 N N   . ILE A 207 ? 0.31322 0.17491 0.22648 -0.01944 -0.01982 -0.08287 214 ILE A N   
1556 C CA  . ILE A 207 ? 0.27450 0.16207 0.22156 -0.02011 -0.01916 -0.06473 214 ILE A CA  
1557 C C   . ILE A 207 ? 0.34721 0.23210 0.30283 -0.00073 -0.00380 -0.05633 214 ILE A C   
1558 O O   . ILE A 207 ? 0.32951 0.22355 0.27753 0.01438  0.00549  -0.05717 214 ILE A O   
1559 C CB  . ILE A 207 ? 0.25381 0.18563 0.21547 -0.02205 -0.02477 -0.05647 214 ILE A CB  
1560 C CG1 . ILE A 207 ? 0.27380 0.21581 0.23263 -0.03967 -0.04017 -0.05964 214 ILE A CG1 
1561 C CG2 . ILE A 207 ? 0.24642 0.20525 0.23720 -0.01882 -0.02158 -0.04155 214 ILE A CG2 
1562 C CD1 . ILE A 207 ? 0.32085 0.26223 0.29645 -0.05669 -0.04870 -0.05395 214 ILE A CD1 
1563 N N   . GLY A 208 ? 0.26758 0.14479 0.24074 -0.00135 -0.00116 -0.04534 215 GLY A N   
1564 C CA  . GLY A 208 ? 0.29978 0.17277 0.28024 0.01775  0.01293  -0.03540 215 GLY A CA  
1565 C C   . GLY A 208 ? 0.27081 0.19175 0.27393 0.02585  0.01675  -0.01999 215 GLY A C   
1566 O O   . GLY A 208 ? 0.27338 0.20282 0.29168 0.03521  0.02370  -0.00529 215 GLY A O   
1567 N N   . TYR A 209 ? 0.22234 0.17407 0.22714 0.02211  0.01201  -0.02302 216 TYR A N   
1568 C CA  . TYR A 209 ? 0.21604 0.20931 0.23831 0.02648  0.01398  -0.01364 216 TYR A CA  
1569 C C   . TYR A 209 ? 0.22902 0.23387 0.24293 0.02893  0.01508  -0.02019 216 TYR A C   
1570 O O   . TYR A 209 ? 0.24015 0.23062 0.23833 0.02384  0.01073  -0.02979 216 TYR A O   
1571 C CB  . TYR A 209 ? 0.18700 0.20467 0.22480 0.01488  0.00522  -0.00920 216 TYR A CB  
1572 C CG  . TYR A 209 ? 0.18568 0.19891 0.23470 0.01109  0.00465  0.00182  216 TYR A CG  
1573 C CD1 . TYR A 209 ? 0.19076 0.22253 0.25304 0.02002  0.01118  0.01650  216 TYR A CD1 
1574 C CD2 . TYR A 209 ? 0.18831 0.18138 0.23566 -0.00262 -0.00280 -0.00008 216 TYR A CD2 
1575 C CE1 . TYR A 209 ? 0.17837 0.20682 0.25202 0.01698  0.01166  0.03081  216 TYR A CE1 
1576 C CE2 . TYR A 209 ? 0.19472 0.18326 0.25497 -0.00848 -0.00300 0.01315  216 TYR A CE2 
1577 C CZ  . TYR A 209 ? 0.16703 0.17201 0.24038 0.00220  0.00498  0.02950  216 TYR A CZ  
1578 O OH  . TYR A 209 ? 0.20973 0.21112 0.29699 -0.00304 0.00577  0.04672  216 TYR A OH  
1579 N N   . PRO A 210 ? 0.18873 0.22178 0.21318 0.03537  0.02035  -0.01363 217 PRO A N   
1580 C CA  . PRO A 210 ? 0.19192 0.23643 0.21197 0.03496  0.02156  -0.01657 217 PRO A CA  
1581 C C   . PRO A 210 ? 0.20905 0.25770 0.23108 0.02297  0.01198  -0.02147 217 PRO A C   
1582 O O   . PRO A 210 ? 0.20268 0.26441 0.23718 0.01728  0.00670  -0.02060 217 PRO A O   
1583 C CB  . PRO A 210 ? 0.20833 0.28626 0.24458 0.03973  0.02699  -0.00684 217 PRO A CB  
1584 C CG  . PRO A 210 ? 0.27739 0.36653 0.32595 0.04287  0.02715  0.00105  217 PRO A CG  
1585 C CD  . PRO A 210 ? 0.20317 0.26098 0.24441 0.04220  0.02504  -0.00128 217 PRO A CD  
1586 N N   . ILE A 211 ? 0.18847 0.22712 0.19711 0.02141  0.01073  -0.02560 218 ILE A N   
1587 C CA  . ILE A 211 ? 0.17358 0.21542 0.18423 0.01377  0.00333  -0.02687 218 ILE A CA  
1588 C C   . ILE A 211 ? 0.17294 0.22560 0.18687 0.01411  0.00780  -0.02188 218 ILE A C   
1589 O O   . ILE A 211 ? 0.22223 0.27283 0.22386 0.01874  0.01343  -0.01943 218 ILE A O   
1590 C CB  . ILE A 211 ? 0.18932 0.21560 0.18291 0.01067  -0.00289 -0.03160 218 ILE A CB  
1591 C CG1 . ILE A 211 ? 0.18799 0.20292 0.18066 0.00579  -0.00841 -0.03567 218 ILE A CG1 
1592 C CG2 . ILE A 211 ? 0.21285 0.24716 0.21145 0.00651  -0.00929 -0.02835 218 ILE A CG2 
1593 C CD1 . ILE A 211 ? 0.22583 0.22487 0.19821 -0.00002 -0.01533 -0.04287 218 ILE A CD1 
1594 N N   . THR A 212 ? 0.16304 0.22711 0.19280 0.00866  0.00579  -0.02052 219 THR A N   
1595 C CA  . THR A 212 ? 0.15570 0.22784 0.19251 0.00451  0.00906  -0.01498 219 THR A CA  
1596 C C   . THR A 212 ? 0.14535 0.20532 0.18345 0.00034  0.00447  -0.01405 219 THR A C   
1597 O O   . THR A 212 ? 0.15111 0.20665 0.19631 -0.00131 -0.00037 -0.01957 219 THR A O   
1598 C CB  . THR A 212 ? 0.14700 0.23805 0.20006 -0.00110 0.00943  -0.01554 219 THR A CB  
1599 O OG1 . THR A 212 ? 0.17699 0.28358 0.23104 0.00573  0.01426  -0.01222 219 THR A OG1 
1600 C CG2 . THR A 212 ? 0.15804 0.25656 0.22055 -0.01029 0.01149  -0.00926 219 THR A CG2 
1601 N N   . LEU A 213 ? 0.16200 0.21839 0.19319 0.00083  0.00718  -0.00546 220 LEU A N   
1602 C CA  . LEU A 213 ? 0.17262 0.21771 0.20683 -0.00119 0.00433  0.00069  220 LEU A CA  
1603 C C   . LEU A 213 ? 0.15866 0.20209 0.20876 -0.01055 0.00715  0.00575  220 LEU A C   
1604 O O   . LEU A 213 ? 0.17439 0.22909 0.22662 -0.01460 0.01278  0.01555  220 LEU A O   
1605 C CB  . LEU A 213 ? 0.21178 0.25747 0.22928 0.00377  0.00536  0.01012  220 LEU A CB  
1606 C CG  . LEU A 213 ? 0.22110 0.25921 0.24190 0.00407  0.00360  0.02297  220 LEU A CG  
1607 C CD1 . LEU A 213 ? 0.21835 0.24572 0.24889 0.00670  -0.00278 0.01849  220 LEU A CD1 
1608 C CD2 . LEU A 213 ? 0.24034 0.28771 0.24015 0.00965  0.00341  0.03211  220 LEU A CD2 
1609 N N   . PHE A 214 ? 0.16333 0.19341 0.22438 -0.01448 0.00350  -0.00155 221 PHE A N   
1610 C CA  . PHE A 214 ? 0.15888 0.17934 0.23384 -0.02667 0.00442  -0.00051 221 PHE A CA  
1611 C C   . PHE A 214 ? 0.18314 0.18764 0.26061 -0.02791 0.00718  0.01636  221 PHE A C   
1612 O O   . PHE A 214 ? 0.21787 0.21478 0.28779 -0.01727 0.00647  0.02380  221 PHE A O   
1613 C CB  . PHE A 214 ? 0.16770 0.17122 0.24835 -0.02807 0.00048  -0.01628 221 PHE A CB  
1614 C CG  . PHE A 214 ? 0.14846 0.17129 0.22927 -0.03074 -0.00210 -0.03107 221 PHE A CG  
1615 C CD1 . PHE A 214 ? 0.15987 0.20731 0.23490 -0.02486 -0.00149 -0.02968 221 PHE A CD1 
1616 C CD2 . PHE A 214 ? 0.18675 0.20135 0.27200 -0.03846 -0.00497 -0.04653 221 PHE A CD2 
1617 C CE1 . PHE A 214 ? 0.14824 0.21581 0.22478 -0.02601 -0.00345 -0.03900 221 PHE A CE1 
1618 C CE2 . PHE A 214 ? 0.18100 0.21939 0.26453 -0.04040 -0.00774 -0.05854 221 PHE A CE2 
1619 C CZ  . PHE A 214 ? 0.15323 0.22016 0.23381 -0.03381 -0.00685 -0.05250 221 PHE A CZ  
1620 N N   . VAL A 215 ? 0.18672 0.18964 0.27639 -0.04201 0.00989  0.02484  222 VAL A N   
1621 C CA  . VAL A 215 ? 0.20771 0.19316 0.30366 -0.04554 0.01313  0.04415  222 VAL A CA  
1622 C C   . VAL A 215 ? 0.23484 0.18269 0.34449 -0.05557 0.01082  0.03719  222 VAL A C   
1623 O O   . VAL A 215 ? 0.27017 0.21157 0.38299 -0.06278 0.00675  0.01636  222 VAL A O   
1624 C CB  . VAL A 215 ? 0.36697 0.37699 0.46786 -0.05461 0.01932  0.06399  222 VAL A CB  
1625 C CG1 . VAL A 215 ? 0.43373 0.47076 0.51494 -0.03940 0.02356  0.07145  222 VAL A CG1 
1626 C CG2 . VAL A 215 ? 0.27028 0.30086 0.38400 -0.07040 0.01863  0.05685  222 VAL A CG2 
1627 N N   . GLU A 216 ? 0.27232 0.19368 0.38835 -0.05492 0.01376  0.05469  223 GLU A N   
1628 C CA  . GLU A 216 ? 0.34024 0.21454 0.46783 -0.06143 0.01319  0.04898  223 GLU A CA  
1629 C C   . GLU A 216 ? 0.41566 0.27539 0.56058 -0.08392 0.01575  0.06596  223 GLU A C   
1630 O O   . GLU A 216 ? 0.41474 0.29957 0.56293 -0.08769 0.02013  0.09118  223 GLU A O   
1631 C CB  . GLU A 216 ? 0.39024 0.23813 0.51484 -0.04006 0.01528  0.05758  223 GLU A CB  
1632 C CG  . GLU A 216 ? 0.35300 0.22314 0.46356 -0.01963 0.01238  0.04695  223 GLU A CG  
1633 C CD  . GLU A 216 ? 0.38322 0.23558 0.49457 0.00163  0.01404  0.05810  223 GLU A CD  
1634 O OE1 . GLU A 216 ? 0.40919 0.21983 0.52934 0.00610  0.01698  0.05311  223 GLU A OE1 
1635 O OE2 . GLU A 216 ? 0.41936 0.30008 0.52214 0.01419  0.01237  0.07165  223 GLU A OE2 
1636 N N   . LYS A 217 ? 0.42186 0.24082 0.57708 -0.09953 0.01316  0.05151  224 LYS A N   
1637 C CA  . LYS A 217 ? 0.51345 0.31549 0.67646 -0.12177 0.01396  0.06251  224 LYS A CA  
1638 C C   . LYS A 217 ? 0.71200 0.50123 0.87778 -0.11315 0.02084  0.09496  224 LYS A C   
1639 O O   . LYS A 217 ? 0.69635 0.46211 0.85741 -0.09120 0.02348  0.10129  224 LYS A O   
1640 C CB  . LYS A 217 ? 0.61354 0.36807 0.76819 -0.13238 0.00947  0.03597  224 LYS A CB  
1641 C CG  . LYS A 217 ? 0.81740 0.53258 0.97403 -0.14820 0.01190  0.04848  224 LYS A CG  
1642 C CD  . LYS A 217 ? 0.85152 0.53082 0.99659 -0.16945 0.00529  0.02046  224 LYS A CD  
1643 C CE  . LYS A 217 ? 0.91196 0.52115 1.04704 -0.16226 0.00743  0.01831  224 LYS A CE  
1644 N NZ  . LYS A 217 ? 0.82302 0.40935 0.96723 -0.18034 0.01222  0.04296  224 LYS A NZ  
# 
