data_7HAF
# 
_entry.id   7HAF 
# 
_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   7HAF         pdb_00007haf 10.2210/pdb7haf/pdb 
WWPDB D_1001407226 ?            ?                   
# 
_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                        7HAF 
_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 '(2M)-2-(1H-imidazol-1-yl)benzonitrile' 169.183   1   ?        ? ? ? 
3 water       nat water                                   18.015    377 ?        ? ? ? 
# 
_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 '(2M)-2-(1H-imidazol-1-yl)benzonitrile' A1AXM 
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 
A1AXM non-polymer         . '(2M)-2-(1H-imidazol-1-yl)benzonitrile' ? 'C10 H7 N3'      169.183 
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        A1AXM 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1AXM 
_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 A1AXM 1   301 301 A1AXM E3R A . 
C 3 HOH   1   401 360 HOH   HOH A . 
C 3 HOH   2   402 372 HOH   HOH A . 
C 3 HOH   3   403 366 HOH   HOH A . 
C 3 HOH   4   404 216 HOH   HOH A . 
C 3 HOH   5   405 340 HOH   HOH A . 
C 3 HOH   6   406 311 HOH   HOH A . 
C 3 HOH   7   407 357 HOH   HOH A . 
C 3 HOH   8   408 252 HOH   HOH A . 
C 3 HOH   9   409 321 HOH   HOH A . 
C 3 HOH   10  410 117 HOH   HOH A . 
C 3 HOH   11  411 294 HOH   HOH A . 
C 3 HOH   12  412 249 HOH   HOH A . 
C 3 HOH   13  413 305 HOH   HOH A . 
C 3 HOH   14  414 303 HOH   HOH A . 
C 3 HOH   15  415 47  HOH   HOH A . 
C 3 HOH   16  416 282 HOH   HOH A . 
C 3 HOH   17  417 65  HOH   HOH A . 
C 3 HOH   18  418 118 HOH   HOH A . 
C 3 HOH   19  419 291 HOH   HOH A . 
C 3 HOH   20  420 267 HOH   HOH A . 
C 3 HOH   21  421 164 HOH   HOH A . 
C 3 HOH   22  422 34  HOH   HOH A . 
C 3 HOH   23  423 138 HOH   HOH A . 
C 3 HOH   24  424 96  HOH   HOH A . 
C 3 HOH   25  425 17  HOH   HOH A . 
C 3 HOH   26  426 5   HOH   HOH A . 
C 3 HOH   27  427 56  HOH   HOH A . 
C 3 HOH   28  428 116 HOH   HOH A . 
C 3 HOH   29  429 284 HOH   HOH A . 
C 3 HOH   30  430 197 HOH   HOH A . 
C 3 HOH   31  431 251 HOH   HOH A . 
C 3 HOH   32  432 33  HOH   HOH A . 
C 3 HOH   33  433 226 HOH   HOH A . 
C 3 HOH   34  434 238 HOH   HOH A . 
C 3 HOH   35  435 307 HOH   HOH A . 
C 3 HOH   36  436 150 HOH   HOH A . 
C 3 HOH   37  437 49  HOH   HOH A . 
C 3 HOH   38  438 255 HOH   HOH A . 
C 3 HOH   39  439 89  HOH   HOH A . 
C 3 HOH   40  440 72  HOH   HOH A . 
C 3 HOH   41  441 182 HOH   HOH A . 
C 3 HOH   42  442 93  HOH   HOH A . 
C 3 HOH   43  443 21  HOH   HOH A . 
C 3 HOH   44  444 36  HOH   HOH A . 
C 3 HOH   45  445 139 HOH   HOH A . 
C 3 HOH   46  446 256 HOH   HOH A . 
C 3 HOH   47  447 336 HOH   HOH A . 
C 3 HOH   48  448 1   HOH   HOH A . 
C 3 HOH   49  449 31  HOH   HOH A . 
C 3 HOH   50  450 27  HOH   HOH A . 
C 3 HOH   51  451 123 HOH   HOH A . 
C 3 HOH   52  452 42  HOH   HOH A . 
C 3 HOH   53  453 37  HOH   HOH A . 
C 3 HOH   54  454 220 HOH   HOH A . 
C 3 HOH   55  455 15  HOH   HOH A . 
C 3 HOH   56  456 48  HOH   HOH A . 
C 3 HOH   57  457 9   HOH   HOH A . 
C 3 HOH   58  458 237 HOH   HOH A . 
C 3 HOH   59  459 98  HOH   HOH A . 
C 3 HOH   60  460 60  HOH   HOH A . 
C 3 HOH   61  461 134 HOH   HOH A . 
C 3 HOH   62  462 23  HOH   HOH A . 
C 3 HOH   63  463 3   HOH   HOH A . 
C 3 HOH   64  464 119 HOH   HOH A . 
C 3 HOH   65  465 261 HOH   HOH A . 
C 3 HOH   66  466 57  HOH   HOH A . 
C 3 HOH   67  467 345 HOH   HOH A . 
C 3 HOH   68  468 155 HOH   HOH A . 
C 3 HOH   69  469 151 HOH   HOH A . 
C 3 HOH   70  470 208 HOH   HOH A . 
C 3 HOH   71  471 191 HOH   HOH A . 
C 3 HOH   72  472 106 HOH   HOH A . 
C 3 HOH   73  473 146 HOH   HOH A . 
C 3 HOH   74  474 170 HOH   HOH A . 
C 3 HOH   75  475 8   HOH   HOH A . 
C 3 HOH   76  476 2   HOH   HOH A . 
C 3 HOH   77  477 248 HOH   HOH A . 
C 3 HOH   78  478 102 HOH   HOH A . 
C 3 HOH   79  479 135 HOH   HOH A . 
C 3 HOH   80  480 124 HOH   HOH A . 
C 3 HOH   81  481 83  HOH   HOH A . 
C 3 HOH   82  482 137 HOH   HOH A . 
C 3 HOH   83  483 74  HOH   HOH A . 
C 3 HOH   84  484 68  HOH   HOH A . 
C 3 HOH   85  485 4   HOH   HOH A . 
C 3 HOH   86  486 7   HOH   HOH A . 
C 3 HOH   87  487 131 HOH   HOH A . 
C 3 HOH   88  488 41  HOH   HOH A . 
C 3 HOH   89  489 141 HOH   HOH A . 
C 3 HOH   90  490 157 HOH   HOH A . 
C 3 HOH   91  491 85  HOH   HOH A . 
C 3 HOH   92  492 97  HOH   HOH A . 
C 3 HOH   93  493 264 HOH   HOH A . 
C 3 HOH   94  494 30  HOH   HOH A . 
C 3 HOH   95  495 67  HOH   HOH A . 
C 3 HOH   96  496 190 HOH   HOH A . 
C 3 HOH   97  497 80  HOH   HOH A . 
C 3 HOH   98  498 50  HOH   HOH A . 
C 3 HOH   99  499 180 HOH   HOH A . 
C 3 HOH   100 500 39  HOH   HOH A . 
C 3 HOH   101 501 273 HOH   HOH A . 
C 3 HOH   102 502 78  HOH   HOH A . 
C 3 HOH   103 503 174 HOH   HOH A . 
C 3 HOH   104 504 244 HOH   HOH A . 
C 3 HOH   105 505 59  HOH   HOH A . 
C 3 HOH   106 506 142 HOH   HOH A . 
C 3 HOH   107 507 16  HOH   HOH A . 
C 3 HOH   108 508 73  HOH   HOH A . 
C 3 HOH   109 509 172 HOH   HOH A . 
C 3 HOH   110 510 103 HOH   HOH A . 
C 3 HOH   111 511 144 HOH   HOH A . 
C 3 HOH   112 512 153 HOH   HOH A . 
C 3 HOH   113 513 75  HOH   HOH A . 
C 3 HOH   114 514 32  HOH   HOH A . 
C 3 HOH   115 515 113 HOH   HOH A . 
C 3 HOH   116 516 309 HOH   HOH A . 
C 3 HOH   117 517 260 HOH   HOH A . 
C 3 HOH   118 518 179 HOH   HOH A . 
C 3 HOH   119 519 13  HOH   HOH A . 
C 3 HOH   120 520 66  HOH   HOH A . 
C 3 HOH   121 521 90  HOH   HOH A . 
C 3 HOH   122 522 76  HOH   HOH A . 
C 3 HOH   123 523 26  HOH   HOH A . 
C 3 HOH   124 524 61  HOH   HOH A . 
C 3 HOH   125 525 108 HOH   HOH A . 
C 3 HOH   126 526 62  HOH   HOH A . 
C 3 HOH   127 527 38  HOH   HOH A . 
C 3 HOH   128 528 152 HOH   HOH A . 
C 3 HOH   129 529 10  HOH   HOH A . 
C 3 HOH   130 530 194 HOH   HOH A . 
C 3 HOH   131 531 250 HOH   HOH A . 
C 3 HOH   132 532 127 HOH   HOH A . 
C 3 HOH   133 533 95  HOH   HOH A . 
C 3 HOH   134 534 63  HOH   HOH A . 
C 3 HOH   135 535 58  HOH   HOH A . 
C 3 HOH   136 536 94  HOH   HOH A . 
C 3 HOH   137 537 177 HOH   HOH A . 
C 3 HOH   138 538 132 HOH   HOH A . 
C 3 HOH   139 539 265 HOH   HOH A . 
C 3 HOH   140 540 156 HOH   HOH A . 
C 3 HOH   141 541 363 HOH   HOH A . 
C 3 HOH   142 542 242 HOH   HOH A . 
C 3 HOH   143 543 19  HOH   HOH A . 
C 3 HOH   144 544 29  HOH   HOH A . 
C 3 HOH   145 545 163 HOH   HOH A . 
C 3 HOH   146 546 230 HOH   HOH A . 
C 3 HOH   147 547 310 HOH   HOH A . 
C 3 HOH   148 548 302 HOH   HOH A . 
C 3 HOH   149 549 121 HOH   HOH A . 
C 3 HOH   150 550 79  HOH   HOH A . 
C 3 HOH   151 551 6   HOH   HOH A . 
C 3 HOH   152 552 111 HOH   HOH A . 
C 3 HOH   153 553 11  HOH   HOH A . 
C 3 HOH   154 554 233 HOH   HOH A . 
C 3 HOH   155 555 276 HOH   HOH A . 
C 3 HOH   156 556 196 HOH   HOH A . 
C 3 HOH   157 557 136 HOH   HOH A . 
C 3 HOH   158 558 299 HOH   HOH A . 
C 3 HOH   159 559 314 HOH   HOH A . 
C 3 HOH   160 560 159 HOH   HOH A . 
C 3 HOH   161 561 12  HOH   HOH A . 
C 3 HOH   162 562 28  HOH   HOH A . 
C 3 HOH   163 563 53  HOH   HOH A . 
C 3 HOH   164 564 120 HOH   HOH A . 
C 3 HOH   165 565 86  HOH   HOH A . 
C 3 HOH   166 566 107 HOH   HOH A . 
C 3 HOH   167 567 18  HOH   HOH A . 
C 3 HOH   168 568 22  HOH   HOH A . 
C 3 HOH   169 569 289 HOH   HOH A . 
C 3 HOH   170 570 35  HOH   HOH A . 
C 3 HOH   171 571 109 HOH   HOH A . 
C 3 HOH   172 572 44  HOH   HOH A . 
C 3 HOH   173 573 70  HOH   HOH A . 
C 3 HOH   174 574 14  HOH   HOH A . 
C 3 HOH   175 575 222 HOH   HOH A . 
C 3 HOH   176 576 25  HOH   HOH A . 
C 3 HOH   177 577 263 HOH   HOH A . 
C 3 HOH   178 578 322 HOH   HOH A . 
C 3 HOH   179 579 160 HOH   HOH A . 
C 3 HOH   180 580 43  HOH   HOH A . 
C 3 HOH   181 581 204 HOH   HOH A . 
C 3 HOH   182 582 275 HOH   HOH A . 
C 3 HOH   183 583 171 HOH   HOH A . 
C 3 HOH   184 584 92  HOH   HOH A . 
C 3 HOH   185 585 24  HOH   HOH A . 
C 3 HOH   186 586 183 HOH   HOH A . 
C 3 HOH   187 587 297 HOH   HOH A . 
C 3 HOH   188 588 112 HOH   HOH A . 
C 3 HOH   189 589 45  HOH   HOH A . 
C 3 HOH   190 590 71  HOH   HOH A . 
C 3 HOH   191 591 286 HOH   HOH A . 
C 3 HOH   192 592 187 HOH   HOH A . 
C 3 HOH   193 593 227 HOH   HOH A . 
C 3 HOH   194 594 325 HOH   HOH A . 
C 3 HOH   195 595 358 HOH   HOH A . 
C 3 HOH   196 596 110 HOH   HOH A . 
C 3 HOH   197 597 234 HOH   HOH A . 
C 3 HOH   198 598 211 HOH   HOH A . 
C 3 HOH   199 599 266 HOH   HOH A . 
C 3 HOH   200 600 84  HOH   HOH A . 
C 3 HOH   201 601 105 HOH   HOH A . 
C 3 HOH   202 602 218 HOH   HOH A . 
C 3 HOH   203 603 199 HOH   HOH A . 
C 3 HOH   204 604 55  HOH   HOH A . 
C 3 HOH   205 605 259 HOH   HOH A . 
C 3 HOH   206 606 133 HOH   HOH A . 
C 3 HOH   207 607 272 HOH   HOH A . 
C 3 HOH   208 608 64  HOH   HOH A . 
C 3 HOH   209 609 308 HOH   HOH A . 
C 3 HOH   210 610 100 HOH   HOH A . 
C 3 HOH   211 611 210 HOH   HOH A . 
C 3 HOH   212 612 165 HOH   HOH A . 
C 3 HOH   213 613 257 HOH   HOH A . 
C 3 HOH   214 614 292 HOH   HOH A . 
C 3 HOH   215 615 339 HOH   HOH A . 
C 3 HOH   216 616 81  HOH   HOH A . 
C 3 HOH   217 617 130 HOH   HOH A . 
C 3 HOH   218 618 364 HOH   HOH A . 
C 3 HOH   219 619 82  HOH   HOH A . 
C 3 HOH   220 620 254 HOH   HOH A . 
C 3 HOH   221 621 224 HOH   HOH A . 
C 3 HOH   222 622 51  HOH   HOH A . 
C 3 HOH   223 623 99  HOH   HOH A . 
C 3 HOH   224 624 217 HOH   HOH A . 
C 3 HOH   225 625 246 HOH   HOH A . 
C 3 HOH   226 626 285 HOH   HOH A . 
C 3 HOH   227 627 301 HOH   HOH A . 
C 3 HOH   228 628 329 HOH   HOH A . 
C 3 HOH   229 629 185 HOH   HOH A . 
C 3 HOH   230 630 239 HOH   HOH A . 
C 3 HOH   231 631 149 HOH   HOH A . 
C 3 HOH   232 632 20  HOH   HOH A . 
C 3 HOH   233 633 101 HOH   HOH A . 
C 3 HOH   234 634 215 HOH   HOH A . 
C 3 HOH   235 635 352 HOH   HOH A . 
C 3 HOH   236 636 365 HOH   HOH A . 
C 3 HOH   237 637 337 HOH   HOH A . 
C 3 HOH   238 638 335 HOH   HOH A . 
C 3 HOH   239 639 268 HOH   HOH A . 
C 3 HOH   240 640 295 HOH   HOH A . 
C 3 HOH   241 641 370 HOH   HOH A . 
C 3 HOH   242 642 247 HOH   HOH A . 
C 3 HOH   243 643 350 HOH   HOH A . 
C 3 HOH   244 644 332 HOH   HOH A . 
C 3 HOH   245 645 104 HOH   HOH A . 
C 3 HOH   246 646 40  HOH   HOH A . 
C 3 HOH   247 647 147 HOH   HOH A . 
C 3 HOH   248 648 205 HOH   HOH A . 
C 3 HOH   249 649 69  HOH   HOH A . 
C 3 HOH   250 650 154 HOH   HOH A . 
C 3 HOH   251 651 200 HOH   HOH A . 
C 3 HOH   252 652 361 HOH   HOH A . 
C 3 HOH   253 653 319 HOH   HOH A . 
C 3 HOH   254 654 356 HOH   HOH A . 
C 3 HOH   255 655 300 HOH   HOH A . 
C 3 HOH   256 656 320 HOH   HOH A . 
C 3 HOH   257 657 223 HOH   HOH A . 
C 3 HOH   258 658 228 HOH   HOH A . 
C 3 HOH   259 659 202 HOH   HOH A . 
C 3 HOH   260 660 207 HOH   HOH A . 
C 3 HOH   261 661 229 HOH   HOH A . 
C 3 HOH   262 662 258 HOH   HOH A . 
C 3 HOH   263 663 158 HOH   HOH A . 
C 3 HOH   264 664 169 HOH   HOH A . 
C 3 HOH   265 665 125 HOH   HOH A . 
C 3 HOH   266 666 377 HOH   HOH A . 
C 3 HOH   267 667 375 HOH   HOH A . 
C 3 HOH   268 668 355 HOH   HOH A . 
C 3 HOH   269 669 353 HOH   HOH A . 
C 3 HOH   270 670 269 HOH   HOH A . 
C 3 HOH   271 671 195 HOH   HOH A . 
C 3 HOH   272 672 52  HOH   HOH A . 
C 3 HOH   273 673 166 HOH   HOH A . 
C 3 HOH   274 674 140 HOH   HOH A . 
C 3 HOH   275 675 114 HOH   HOH A . 
C 3 HOH   276 676 176 HOH   HOH A . 
C 3 HOH   277 677 87  HOH   HOH A . 
C 3 HOH   278 678 279 HOH   HOH A . 
C 3 HOH   279 679 221 HOH   HOH A . 
C 3 HOH   280 680 214 HOH   HOH A . 
C 3 HOH   281 681 168 HOH   HOH A . 
C 3 HOH   282 682 331 HOH   HOH A . 
C 3 HOH   283 683 270 HOH   HOH A . 
C 3 HOH   284 684 115 HOH   HOH A . 
C 3 HOH   285 685 184 HOH   HOH A . 
C 3 HOH   286 686 235 HOH   HOH A . 
C 3 HOH   287 687 181 HOH   HOH A . 
C 3 HOH   288 688 243 HOH   HOH A . 
C 3 HOH   289 689 192 HOH   HOH A . 
C 3 HOH   290 690 317 HOH   HOH A . 
C 3 HOH   291 691 145 HOH   HOH A . 
C 3 HOH   292 692 315 HOH   HOH A . 
C 3 HOH   293 693 122 HOH   HOH A . 
C 3 HOH   294 694 148 HOH   HOH A . 
C 3 HOH   295 695 326 HOH   HOH A . 
C 3 HOH   296 696 188 HOH   HOH A . 
C 3 HOH   297 697 283 HOH   HOH A . 
C 3 HOH   298 698 198 HOH   HOH A . 
C 3 HOH   299 699 298 HOH   HOH A . 
C 3 HOH   300 700 186 HOH   HOH A . 
C 3 HOH   301 701 288 HOH   HOH A . 
C 3 HOH   302 702 193 HOH   HOH A . 
C 3 HOH   303 703 333 HOH   HOH A . 
C 3 HOH   304 704 369 HOH   HOH A . 
C 3 HOH   305 705 126 HOH   HOH A . 
C 3 HOH   306 706 278 HOH   HOH A . 
C 3 HOH   307 707 241 HOH   HOH A . 
C 3 HOH   308 708 162 HOH   HOH A . 
C 3 HOH   309 709 371 HOH   HOH A . 
C 3 HOH   310 710 306 HOH   HOH A . 
C 3 HOH   311 711 189 HOH   HOH A . 
C 3 HOH   312 712 203 HOH   HOH A . 
C 3 HOH   313 713 323 HOH   HOH A . 
C 3 HOH   314 714 77  HOH   HOH A . 
C 3 HOH   315 715 277 HOH   HOH A . 
C 3 HOH   316 716 287 HOH   HOH A . 
C 3 HOH   317 717 359 HOH   HOH A . 
C 3 HOH   318 718 253 HOH   HOH A . 
C 3 HOH   319 719 201 HOH   HOH A . 
C 3 HOH   320 720 312 HOH   HOH A . 
C 3 HOH   321 721 209 HOH   HOH A . 
C 3 HOH   322 722 129 HOH   HOH A . 
C 3 HOH   323 723 245 HOH   HOH A . 
C 3 HOH   324 724 225 HOH   HOH A . 
C 3 HOH   325 725 161 HOH   HOH A . 
C 3 HOH   326 726 316 HOH   HOH A . 
C 3 HOH   327 727 351 HOH   HOH A . 
C 3 HOH   328 728 206 HOH   HOH A . 
C 3 HOH   329 729 304 HOH   HOH A . 
C 3 HOH   330 730 236 HOH   HOH A . 
C 3 HOH   331 731 296 HOH   HOH A . 
C 3 HOH   332 732 54  HOH   HOH A . 
C 3 HOH   333 733 347 HOH   HOH A . 
C 3 HOH   334 734 143 HOH   HOH A . 
C 3 HOH   335 735 91  HOH   HOH A . 
C 3 HOH   336 736 293 HOH   HOH A . 
C 3 HOH   337 737 324 HOH   HOH A . 
C 3 HOH   338 738 343 HOH   HOH A . 
C 3 HOH   339 739 368 HOH   HOH A . 
C 3 HOH   340 740 178 HOH   HOH A . 
C 3 HOH   341 741 330 HOH   HOH A . 
C 3 HOH   342 742 88  HOH   HOH A . 
C 3 HOH   343 743 344 HOH   HOH A . 
C 3 HOH   344 744 262 HOH   HOH A . 
C 3 HOH   345 745 281 HOH   HOH A . 
C 3 HOH   346 746 362 HOH   HOH A . 
C 3 HOH   347 747 173 HOH   HOH A . 
C 3 HOH   348 748 46  HOH   HOH A . 
C 3 HOH   349 749 212 HOH   HOH A . 
C 3 HOH   350 750 271 HOH   HOH A . 
C 3 HOH   351 751 280 HOH   HOH A . 
C 3 HOH   352 752 175 HOH   HOH A . 
C 3 HOH   353 753 274 HOH   HOH A . 
C 3 HOH   354 754 128 HOH   HOH A . 
C 3 HOH   355 755 213 HOH   HOH A . 
C 3 HOH   356 756 232 HOH   HOH A . 
C 3 HOH   357 757 349 HOH   HOH A . 
C 3 HOH   358 758 167 HOH   HOH A . 
C 3 HOH   359 759 219 HOH   HOH A . 
C 3 HOH   360 760 373 HOH   HOH A . 
C 3 HOH   361 761 313 HOH   HOH A . 
C 3 HOH   362 762 328 HOH   HOH A . 
C 3 HOH   363 763 231 HOH   HOH A . 
C 3 HOH   364 764 341 HOH   HOH A . 
C 3 HOH   365 765 376 HOH   HOH A . 
C 3 HOH   366 766 374 HOH   HOH A . 
C 3 HOH   367 767 327 HOH   HOH A . 
C 3 HOH   368 768 354 HOH   HOH A . 
C 3 HOH   369 769 342 HOH   HOH A . 
C 3 HOH   370 770 348 HOH   HOH A . 
C 3 HOH   371 771 290 HOH   HOH A . 
C 3 HOH   372 772 346 HOH   HOH A . 
C 3 HOH   373 773 240 HOH   HOH A . 
C 3 HOH   374 774 318 HOH   HOH A . 
C 3 HOH   375 775 367 HOH   HOH A . 
C 3 HOH   376 776 334 HOH   HOH A . 
C 3 HOH   377 777 338 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             609191.191 
_cell.length_a           67.191 
_cell.length_b           91.336 
_cell.length_c           99.266 
_cell.angle_beta         90.000 
_cell.angle_gamma        90.000 
_cell.angle_alpha        90.000 
_cell.entry_id           7HAF 
_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                         7HAF 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
# 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
_exptl.entry_id          7HAF 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_Matthews      2.88 
_exptl_crystal.density_percent_sol   57.23 
_exptl_crystal.density_meas          ? 
_exptl_crystal.description           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.pH              8.5 
_exptl_crystal_grow.temp            277 
_exptl_crystal_grow.pdbx_details    '100mM Tris-HCl pH 8.5, 22% PEG4000, 200mM MgCl2' 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_diffrn.id                     1 
_diffrn.crystal_id             1 
_diffrn.ambient_temp           100 
_diffrn.ambient_temp_details   ? 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               PIXEL 
_diffrn_detector.type                   'DECTRIS EIGER2 S 9M' 
_diffrn_detector.pdbx_collection_date   2023-07-04 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.pdbx_scattering_type             x-ray 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.monochromator                    Si111 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.97918 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.pdbx_synchrotron_beamline   BL02U1 
_diffrn_source.type                        'SSRF BEAMLINE BL02U1' 
_diffrn_source.pdbx_wavelength_list        0.97918 
_diffrn_source.pdbx_synchrotron_site       SSRF 
_diffrn_source.pdbx_wavelength             ? 
# 
_reflns.entry_id                     7HAF 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             55.640 
_reflns.d_resolution_high            1.610 
_reflns.number_obs                   39455 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         99.000 
_reflns.pdbx_Rmerge_I_obs            0.067 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        20.400 
_reflns.B_iso_Wilson_estimate        ? 
_reflns.pdbx_redundancy              8.700 
_reflns.pdbx_Rrim_I_all              0.072 
_reflns.pdbx_Rpim_I_all              0.025 
_reflns.pdbx_CC_half                 0.998 
_reflns.pdbx_netI_over_av_sigmaI     ? 
_reflns.pdbx_number_measured_all     342352 
_reflns.pdbx_scaling_rejects         155 
_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 1.610 1.700  ? 40466 5722 ? 0.697 ? ? ? 7.100 ? 2.600  ? ? ? ? ? ? 99.800 0.753 0.277 0.791 
1 2 5.090 55.640 ? 11826 1333 ? 0.031 ? ? ? 8.900 ? 56.800 ? ? ? ? ? ? 97.800 0.033 0.011 0.998 
# 
_refine.entry_id                                 7HAF 
_refine.pdbx_method_to_determine_struct          'FOURIER SYNTHESIS' 
_refine.ls_percent_reflns_R_free                 4.99 
_refine.pdbx_overall_phase_error                 20.5733 
_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                          0.2013 
_refine.B_iso_mean                               25.26 
_refine.ls_number_reflns_R_free                  1933 
_refine.ls_percent_reflns_obs                    97.17 
_refine.ls_R_factor_R_work                       0.2004 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_refine.ls_d_res_high                            1.61 
_refine.ls_number_reflns_obs                     38764 
_refine.pdbx_ls_sigma_F                          1.34 
_refine.ls_number_reflns_R_work                  36831 
_refine.ls_d_res_low                             36.58 
_refine.pdbx_stereochemistry_target_values       'GeoStd + Monomer Library + CDL v1.2' 
_refine.ls_R_factor_R_free                       0.2186 
_refine.overall_SU_ML                            0.2022 
_refine.pdbx_solvent_vdw_probe_radii             1.1000 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.solvent_model_param_ksol                 ? 
_refine.solvent_model_param_bsol                 ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.details                                  ? 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.overall_SU_B                             ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        1644 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         13 
_refine_hist.number_atoms_solvent             377 
_refine_hist.number_atoms_total               2034 
_refine_hist.d_res_high                       1.61 
_refine_hist.d_res_low                        36.58 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.type 
_refine_ls_restr.number 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
_refine_ls_restr.dev_ideal_target 
'X-RAY DIFFRACTION' f_bond_d           1684 0.0075 ? ? ? 
'X-RAY DIFFRACTION' f_angle_d          2269 0.8555 ? ? ? 
'X-RAY DIFFRACTION' f_chiral_restr     259  0.0547 ? ? ? 
'X-RAY DIFFRACTION' f_plane_restr      289  0.0066 ? ? ? 
'X-RAY DIFFRACTION' f_dihedral_angle_d 224  6.0568 ? ? ? 
# 
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' 1.61 1.65  2650 0.2749 99.78  0.2877 133 . . . . . 
'X-RAY DIFFRACTION' 1.65 1.69  2682 0.2667 99.72  0.2961 132 . . . . . 
'X-RAY DIFFRACTION' 1.69 1.74  2669 0.2341 99.79  0.2530 142 . . . . . 
'X-RAY DIFFRACTION' 1.74 1.80  2677 0.2127 99.93  0.2668 140 . . . . . 
'X-RAY DIFFRACTION' 1.80 1.87  2664 0.2223 100.00 0.2603 167 . . . . . 
'X-RAY DIFFRACTION' 1.87 1.94  2115 0.4460 79.17  0.5222 123 . . . . . 
'X-RAY DIFFRACTION' 1.94 2.03  2671 0.2202 99.19  0.2270 131 . . . . . 
'X-RAY DIFFRACTION' 2.03 2.14  2706 0.1889 99.93  0.1661 126 . . . . . 
'X-RAY DIFFRACTION' 2.14 2.27  2356 0.2111 87.73  0.2284 133 . . . . . 
'X-RAY DIFFRACTION' 2.27 2.44  2670 0.1961 99.08  0.2293 143 . . . . . 
'X-RAY DIFFRACTION' 2.44 2.69  2707 0.1832 99.86  0.2120 165 . . . . . 
'X-RAY DIFFRACTION' 2.69 3.08  2687 0.1851 99.86  0.2137 153 . . . . . 
'X-RAY DIFFRACTION' 3.08 3.88  2749 0.1716 98.90  0.1723 121 . . . . . 
'X-RAY DIFFRACTION' 3.88 36.58 2828 0.1672 97.49  0.1554 124 . . . . . 
# 
_struct.entry_id                  7HAF 
_struct.title                     'PanDDA analysis group deposition -- Crystal structure of HSP90N in complex with Fr13854' 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_details        ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HAF 
_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              7HAF 
_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 7HAF MET A 1   ? UNP P07900 ? ? 'initiating methionine' 8   1 
1 7HAF LEU A 230 ? UNP P07900 ? ? 'expression tag'        237 2 
1 7HAF GLU A 231 ? UNP P07900 ? ? 'expression tag'        238 3 
1 7HAF HIS A 232 ? UNP P07900 ? ? 'expression tag'        239 4 
1 7HAF HIS A 233 ? UNP P07900 ? ? 'expression tag'        240 5 
1 7HAF HIS A 234 ? UNP P07900 ? ? 'expression tag'        241 6 
1 7HAF HIS A 235 ? UNP P07900 ? ? 'expression tag'        242 7 
1 7HAF HIS A 236 ? UNP P07900 ? ? 'expression tag'        243 8 
1 7HAF 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 98  ? ALA A 117 ? ASN A 105 ALA A 124 1 ? 20 
HELX_P HELX_P6 AA6 ASP A 120 ? GLY A 128 ? ASP A 127 GLY A 135 5 ? 9  
HELX_P HELX_P7 AA7 VAL A 129 ? LEU A 136 ? VAL A 136 LEU A 143 5 ? 8  
HELX_P HELX_P8 AA8 GLN A 187 ? LEU A 191 ? GLN A 194 LEU A 198 5 ? 5  
HELX_P HELX_P9 AA9 GLU A 192 ? SER A 204 ? GLU A 199 SER A 211 1 ? 13 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
_struct_sheet.id               AA1 
_struct_sheet.type             ? 
_struct_sheet.number_strands   8 
_struct_sheet.details          ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA1 5 6 ? anti-parallel 
AA1 6 7 ? anti-parallel 
AA1 7 8 ? parallel      
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 GLU A 11  ? ALA A 14  ? GLU A 18  ALA A 21  
AA1 2 SER A 162 ? THR A 167 ? SER A 169 THR A 174 
AA1 3 GLN A 152 ? SER A 157 ? GLN A 159 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                   7HAF 
_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 640 ? ? O A HOH 655 ? ? 1.74 
2  1 O   A HOH 539 ? ? O A HOH 620 ? ? 1.85 
3  1 O   A HOH 592 ? ? O A HOH 627 ? ? 1.87 
4  1 O   A THR 65  ? ? O A HOH 401 ? ? 1.89 
5  1 O   A HOH 704 ? ? O A HOH 713 ? ? 1.90 
6  1 O   A HOH 651 ? ? O A HOH 688 ? ? 1.92 
7  1 O   A HOH 431 ? ? O A HOH 582 ? ? 1.92 
8  1 O   A HOH 554 ? ? O A HOH 695 ? ? 1.95 
9  1 O   A HOH 614 ? ? O A HOH 628 ? ? 1.96 
10 1 O   A HOH 577 ? ? O A HOH 597 ? ? 1.96 
11 1 O   A HOH 715 ? ? O A HOH 716 ? ? 1.99 
12 1 O   A HOH 411 ? ? O A HOH 596 ? ? 2.02 
13 1 OE1 A GLN 212 ? ? O A HOH 402 ? ? 2.03 
14 1 O   A HOH 430 ? ? O A HOH 633 ? ? 2.04 
15 1 O   A HOH 413 ? ? O A HOH 587 ? ? 2.06 
16 1 O   A HOH 515 ? ? O A HOH 695 ? ? 2.06 
17 1 O   A HOH 604 ? ? O A HOH 646 ? ? 2.08 
18 1 O   A HOH 546 ? ? O A HOH 749 ? ? 2.08 
19 1 O   A HOH 412 ? ? O A HOH 531 ? ? 2.10 
20 1 O   A HOH 503 ? ? O A HOH 613 ? ? 2.12 
21 1 OH  A TYR 160 ? ? O A HOH 403 ? ? 2.14 
22 1 O   A HOH 664 ? ? O A HOH 763 ? ? 2.16 
23 1 O   A HOH 744 ? ? O A HOH 756 ? ? 2.17 
24 1 OE2 A GLU 178 ? ? O A HOH 404 ? ? 2.17 
25 1 O   A HOH 652 ? ? O A HOH 760 ? ? 2.18 
26 1 O   A HOH 621 ? ? O A HOH 701 ? ? 2.18 
27 1 O   A HOH 487 ? ? O A HOH 587 ? ? 2.19 
# 
loop_
_pdbx_validate_symm_contact.id 
_pdbx_validate_symm_contact.PDB_model_num 
_pdbx_validate_symm_contact.auth_atom_id_1 
_pdbx_validate_symm_contact.auth_asym_id_1 
_pdbx_validate_symm_contact.auth_comp_id_1 
_pdbx_validate_symm_contact.auth_seq_id_1 
_pdbx_validate_symm_contact.PDB_ins_code_1 
_pdbx_validate_symm_contact.label_alt_id_1 
_pdbx_validate_symm_contact.site_symmetry_1 
_pdbx_validate_symm_contact.auth_atom_id_2 
_pdbx_validate_symm_contact.auth_asym_id_2 
_pdbx_validate_symm_contact.auth_comp_id_2 
_pdbx_validate_symm_contact.auth_seq_id_2 
_pdbx_validate_symm_contact.PDB_ins_code_2 
_pdbx_validate_symm_contact.label_alt_id_2 
_pdbx_validate_symm_contact.site_symmetry_2 
_pdbx_validate_symm_contact.dist 
1 1 O A HOH 490 ? ? 1_555 O A HOH 541 ? ? 3_555 2.10 
2 1 O A HOH 536 ? ? 1_555 O A HOH 613 ? ? 2_555 2.15 
3 1 O A HOH 569 ? ? 1_555 O A HOH 611 ? ? 8_444 2.15 
4 1 O A HOH 670 ? ? 1_555 O A HOH 718 ? ? 2_555 2.16 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 TYR A 38  ? ? -163.23 106.90  
2 1 ASP A 66  ? ? -155.47 88.91   
3 1 ASN A 105 ? ? -136.19 -48.49  
4 1 ALA A 166 ? ? 64.05   -149.13 
5 1 ARG A 182 ? ? -170.12 135.56  
# 
_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     761 
_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 13.0849797411  -18.2798070035 -18.2076826334 0.0864091122114 0.113242990829  0.112629404888  
0.000619959492978 -0.0110930463505  -0.0242707265109  2.50124779772 1.69541182299 7.28117067032 -0.717106549484 -2.36550593785  
1.08697879455   0.0402937683673   -0.0938123100908 -0.0566247759206 -0.0582008288988 0.0868283776813  -0.0722075168872 
-0.0090148027407 0.333722223452   -0.165141902823    
2 ? 'X-RAY DIFFRACTION' refined -6.76659509138 -6.47958785162 -25.5090368908 0.143040359975  0.132893938363  0.148866751873  
0.00236221708242  -0.0284328336277  -0.00271049143944 2.05310547915 2.93989079355 5.03651788435 -1.08238825244  1.2666836798    
-2.39810010596  -0.0682148141248  0.246637154887   0.172641419182   -0.139549147893  0.0105520876652  0.135638921229   
-0.248266722234  -0.18858346696   0.0557627177899    
3 ? 'X-RAY DIFFRACTION' refined -3.89999051596 -18.4462078012 -23.6086206876 0.144927688492  0.0840258928574 0.118062436757  
-0.0145110600308  -0.0513918825751  -0.0548414686927  2.65132158309 2.14130414809 3.20544071147 -0.613089887567 -1.14212423371  
-0.849182429299 -0.00952082673235 0.0572549380428  -0.134049960033  -0.0907433833476 0.076829418286   0.0619644010066  
0.178227063375   -0.0594801605527 -0.0642521703409   
4 ? 'X-RAY DIFFRACTION' refined 12.6611585962  -6.41515222606 -14.9211143695 0.130874425078  0.17926995658   0.235073583756  
-0.0142949027237  -0.010193933505   -0.0204986243087  2.61822664193 3.02599247373 6.8578303775  0.555199073914  -1.17027558235  
0.4486686706    0.0588829816621   -0.242605204038  0.2516612773     0.147800425353   -0.0578632453659 -0.23397732411   
-0.250494949047  0.649773181398   -0.000824466473064 
5 ? 'X-RAY DIFFRACTION' refined 1.3921981724   -20.0545525011 -26.8020130198 0.145297910922  0.115815932276  0.144721907791  
-0.00693819689673 -0.0157643063013  -0.0347188171107  2.63648673131 1.67660368704 2.68662279568 -0.945378032315 0.226893131361  
-0.523306409094 0.0481132165374   0.24674773201    -0.173252641878  -0.171647551247  -0.0267776657889 0.158277778273   
0.177526982413   -0.0321799148734 -0.0339981897201   
6 ? 'X-RAY DIFFRACTION' refined -6.18678758269 -19.6581424244 -6.85988912281 0.148449378808  0.173966594699  0.0792483746475 
-0.0264840947652  -0.00493000873961 0.0158149489322   6.54774682892 5.39823011054 4.43474761809 -1.94428272878  -0.388013294122 
0.434410802522  0.0238797285829   -0.419876492304  -0.292615644029  0.1868700788     -0.0650659988445 0.178862323615   
0.198138631375   -0.204439212834  0.0350657895501    
7 ? 'X-RAY DIFFRACTION' refined -13.3191934623 -13.2600741339 -15.5460548536 0.0882796490297 0.137694601237  0.0827696967961 
0.0254839645625   0.00803256799522  -0.0194003619751  4.20566090087 5.60382934709 2.99174623357 1.18747520738   -0.226747010972 
0.0389420723293 0.0329837144332   -0.256898453929  0.0639597728809  0.447070183787   -0.0593082968424 0.109995824729   
-0.0147220484208 -0.0150054689146 0.0159024332649    
# 
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 76  A 61  . 
;chain 'A' and (resid 41 through 76 )
;
3 3 'X-RAY DIFFRACTION' A 77  A 62  A 105 A 90  . 
;chain 'A' and (resid 77 through 105 )
;
4 4 'X-RAY DIFFRACTION' A 106 A 91  A 136 A 121 . 
;chain 'A' and (resid 106 through 136 )
;
5 5 'X-RAY DIFFRACTION' A 137 A 122 A 190 A 175 . 
;chain 'A' and (resid 137 through 190 )
;
6 6 'X-RAY DIFFRACTION' A 191 A 176 A 210 A 195 . 
;chain 'A' and (resid 191 through 210 )
;
7 7 '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 775 ? 6.55 . 
2 1 O ? A HOH 776 ? 6.94 . 
3 1 O ? A HOH 777 ? 8.56 . 
# 
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 
A1AXM C1   C N N 1   
A1AXM C2   C Y N 2   
A1AXM C3   C Y N 3   
A1AXM C4   C Y N 4   
A1AXM C5   C Y N 5   
A1AXM N1   N N N 6   
A1AXM C10  C Y N 7   
A1AXM C6   C Y N 8   
A1AXM C7   C Y N 9   
A1AXM C8   C Y N 10  
A1AXM C9   C Y N 11  
A1AXM N2   N Y N 12  
A1AXM N3   N Y N 13  
A1AXM H1   H N N 14  
A1AXM H2   H N N 15  
A1AXM H3   H N N 16  
A1AXM H7   H N N 17  
A1AXM H4   H N N 18  
A1AXM H5   H N N 19  
A1AXM H6   H N N 20  
ALA   N    N N N 21  
ALA   CA   C N S 22  
ALA   C    C N N 23  
ALA   O    O N N 24  
ALA   CB   C N N 25  
ALA   OXT  O N N 26  
ALA   H    H N N 27  
ALA   H2   H N N 28  
ALA   HA   H N N 29  
ALA   HB1  H N N 30  
ALA   HB2  H N N 31  
ALA   HB3  H N N 32  
ALA   HXT  H N N 33  
ARG   N    N N N 34  
ARG   CA   C N S 35  
ARG   C    C N N 36  
ARG   O    O N N 37  
ARG   CB   C N N 38  
ARG   CG   C N N 39  
ARG   CD   C N N 40  
ARG   NE   N N N 41  
ARG   CZ   C N N 42  
ARG   NH1  N N N 43  
ARG   NH2  N N N 44  
ARG   OXT  O N N 45  
ARG   H    H N N 46  
ARG   H2   H N N 47  
ARG   HA   H N N 48  
ARG   HB2  H N N 49  
ARG   HB3  H N N 50  
ARG   HG2  H N N 51  
ARG   HG3  H N N 52  
ARG   HD2  H N N 53  
ARG   HD3  H N N 54  
ARG   HE   H N N 55  
ARG   HH11 H N N 56  
ARG   HH12 H N N 57  
ARG   HH21 H N N 58  
ARG   HH22 H N N 59  
ARG   HXT  H N N 60  
ASN   N    N N N 61  
ASN   CA   C N S 62  
ASN   C    C N N 63  
ASN   O    O N N 64  
ASN   CB   C N N 65  
ASN   CG   C N N 66  
ASN   OD1  O N N 67  
ASN   ND2  N N N 68  
ASN   OXT  O N N 69  
ASN   H    H N N 70  
ASN   H2   H N N 71  
ASN   HA   H N N 72  
ASN   HB2  H N N 73  
ASN   HB3  H N N 74  
ASN   HD21 H N N 75  
ASN   HD22 H N N 76  
ASN   HXT  H N N 77  
ASP   N    N N N 78  
ASP   CA   C N S 79  
ASP   C    C N N 80  
ASP   O    O N N 81  
ASP   CB   C N N 82  
ASP   CG   C N N 83  
ASP   OD1  O N N 84  
ASP   OD2  O N N 85  
ASP   OXT  O N N 86  
ASP   H    H N N 87  
ASP   H2   H N N 88  
ASP   HA   H N N 89  
ASP   HB2  H N N 90  
ASP   HB3  H N N 91  
ASP   HD2  H N N 92  
ASP   HXT  H N N 93  
GLN   N    N N N 94  
GLN   CA   C N S 95  
GLN   C    C N N 96  
GLN   O    O N N 97  
GLN   CB   C N N 98  
GLN   CG   C N N 99  
GLN   CD   C N N 100 
GLN   OE1  O N N 101 
GLN   NE2  N N N 102 
GLN   OXT  O N N 103 
GLN   H    H N N 104 
GLN   H2   H N N 105 
GLN   HA   H N N 106 
GLN   HB2  H N N 107 
GLN   HB3  H N N 108 
GLN   HG2  H N N 109 
GLN   HG3  H N N 110 
GLN   HE21 H N N 111 
GLN   HE22 H N N 112 
GLN   HXT  H N N 113 
GLU   N    N N N 114 
GLU   CA   C N S 115 
GLU   C    C N N 116 
GLU   O    O N N 117 
GLU   CB   C N N 118 
GLU   CG   C N N 119 
GLU   CD   C N N 120 
GLU   OE1  O N N 121 
GLU   OE2  O N N 122 
GLU   OXT  O N N 123 
GLU   H    H N N 124 
GLU   H2   H N N 125 
GLU   HA   H N N 126 
GLU   HB2  H N N 127 
GLU   HB3  H N N 128 
GLU   HG2  H N N 129 
GLU   HG3  H N N 130 
GLU   HE2  H N N 131 
GLU   HXT  H N N 132 
GLY   N    N N N 133 
GLY   CA   C N N 134 
GLY   C    C N N 135 
GLY   O    O N N 136 
GLY   OXT  O N N 137 
GLY   H    H N N 138 
GLY   H2   H N N 139 
GLY   HA2  H N N 140 
GLY   HA3  H N N 141 
GLY   HXT  H N N 142 
HIS   N    N N N 143 
HIS   CA   C N S 144 
HIS   C    C N N 145 
HIS   O    O N N 146 
HIS   CB   C N N 147 
HIS   CG   C Y N 148 
HIS   ND1  N Y N 149 
HIS   CD2  C Y N 150 
HIS   CE1  C Y N 151 
HIS   NE2  N Y N 152 
HIS   OXT  O N N 153 
HIS   H    H N N 154 
HIS   H2   H N N 155 
HIS   HA   H N N 156 
HIS   HB2  H N N 157 
HIS   HB3  H N N 158 
HIS   HD1  H N N 159 
HIS   HD2  H N N 160 
HIS   HE1  H N N 161 
HIS   HE2  H N N 162 
HIS   HXT  H N N 163 
HOH   O    O N N 164 
HOH   H1   H N N 165 
HOH   H2   H N N 166 
ILE   N    N N N 167 
ILE   CA   C N S 168 
ILE   C    C N N 169 
ILE   O    O N N 170 
ILE   CB   C N S 171 
ILE   CG1  C N N 172 
ILE   CG2  C N N 173 
ILE   CD1  C N N 174 
ILE   OXT  O N N 175 
ILE   H    H N N 176 
ILE   H2   H N N 177 
ILE   HA   H N N 178 
ILE   HB   H N N 179 
ILE   HG12 H N N 180 
ILE   HG13 H N N 181 
ILE   HG21 H N N 182 
ILE   HG22 H N N 183 
ILE   HG23 H N N 184 
ILE   HD11 H N N 185 
ILE   HD12 H N N 186 
ILE   HD13 H N N 187 
ILE   HXT  H N N 188 
LEU   N    N N N 189 
LEU   CA   C N S 190 
LEU   C    C N N 191 
LEU   O    O N N 192 
LEU   CB   C N N 193 
LEU   CG   C N N 194 
LEU   CD1  C N N 195 
LEU   CD2  C N N 196 
LEU   OXT  O N N 197 
LEU   H    H N N 198 
LEU   H2   H N N 199 
LEU   HA   H N N 200 
LEU   HB2  H N N 201 
LEU   HB3  H N N 202 
LEU   HG   H N N 203 
LEU   HD11 H N N 204 
LEU   HD12 H N N 205 
LEU   HD13 H N N 206 
LEU   HD21 H N N 207 
LEU   HD22 H N N 208 
LEU   HD23 H N N 209 
LEU   HXT  H N N 210 
LYS   N    N N N 211 
LYS   CA   C N S 212 
LYS   C    C N N 213 
LYS   O    O N N 214 
LYS   CB   C N N 215 
LYS   CG   C N N 216 
LYS   CD   C N N 217 
LYS   CE   C N N 218 
LYS   NZ   N N N 219 
LYS   OXT  O N N 220 
LYS   H    H N N 221 
LYS   H2   H N N 222 
LYS   HA   H N N 223 
LYS   HB2  H N N 224 
LYS   HB3  H N N 225 
LYS   HG2  H N N 226 
LYS   HG3  H N N 227 
LYS   HD2  H N N 228 
LYS   HD3  H N N 229 
LYS   HE2  H N N 230 
LYS   HE3  H N N 231 
LYS   HZ1  H N N 232 
LYS   HZ2  H N N 233 
LYS   HZ3  H N N 234 
LYS   HXT  H N N 235 
MET   N    N N N 236 
MET   CA   C N S 237 
MET   C    C N N 238 
MET   O    O N N 239 
MET   CB   C N N 240 
MET   CG   C N N 241 
MET   SD   S N N 242 
MET   CE   C N N 243 
MET   OXT  O N N 244 
MET   H    H N N 245 
MET   H2   H N N 246 
MET   HA   H N N 247 
MET   HB2  H N N 248 
MET   HB3  H N N 249 
MET   HG2  H N N 250 
MET   HG3  H N N 251 
MET   HE1  H N N 252 
MET   HE2  H N N 253 
MET   HE3  H N N 254 
MET   HXT  H N N 255 
PHE   N    N N N 256 
PHE   CA   C N S 257 
PHE   C    C N N 258 
PHE   O    O N N 259 
PHE   CB   C N N 260 
PHE   CG   C Y N 261 
PHE   CD1  C Y N 262 
PHE   CD2  C Y N 263 
PHE   CE1  C Y N 264 
PHE   CE2  C Y N 265 
PHE   CZ   C Y N 266 
PHE   OXT  O N N 267 
PHE   H    H N N 268 
PHE   H2   H N N 269 
PHE   HA   H N N 270 
PHE   HB2  H N N 271 
PHE   HB3  H N N 272 
PHE   HD1  H N N 273 
PHE   HD2  H N N 274 
PHE   HE1  H N N 275 
PHE   HE2  H N N 276 
PHE   HZ   H N N 277 
PHE   HXT  H N N 278 
PRO   N    N N N 279 
PRO   CA   C N S 280 
PRO   C    C N N 281 
PRO   O    O N N 282 
PRO   CB   C N N 283 
PRO   CG   C N N 284 
PRO   CD   C N N 285 
PRO   OXT  O N N 286 
PRO   H    H N N 287 
PRO   HA   H N N 288 
PRO   HB2  H N N 289 
PRO   HB3  H N N 290 
PRO   HG2  H N N 291 
PRO   HG3  H N N 292 
PRO   HD2  H N N 293 
PRO   HD3  H N N 294 
PRO   HXT  H N N 295 
SER   N    N N N 296 
SER   CA   C N S 297 
SER   C    C N N 298 
SER   O    O N N 299 
SER   CB   C N N 300 
SER   OG   O N N 301 
SER   OXT  O N N 302 
SER   H    H N N 303 
SER   H2   H N N 304 
SER   HA   H N N 305 
SER   HB2  H N N 306 
SER   HB3  H N N 307 
SER   HG   H N N 308 
SER   HXT  H N N 309 
THR   N    N N N 310 
THR   CA   C N S 311 
THR   C    C N N 312 
THR   O    O N N 313 
THR   CB   C N R 314 
THR   OG1  O N N 315 
THR   CG2  C N N 316 
THR   OXT  O N N 317 
THR   H    H N N 318 
THR   H2   H N N 319 
THR   HA   H N N 320 
THR   HB   H N N 321 
THR   HG1  H N N 322 
THR   HG21 H N N 323 
THR   HG22 H N N 324 
THR   HG23 H N N 325 
THR   HXT  H N N 326 
TRP   N    N N N 327 
TRP   CA   C N S 328 
TRP   C    C N N 329 
TRP   O    O N N 330 
TRP   CB   C N N 331 
TRP   CG   C Y N 332 
TRP   CD1  C Y N 333 
TRP   CD2  C Y N 334 
TRP   NE1  N Y N 335 
TRP   CE2  C Y N 336 
TRP   CE3  C Y N 337 
TRP   CZ2  C Y N 338 
TRP   CZ3  C Y N 339 
TRP   CH2  C Y N 340 
TRP   OXT  O N N 341 
TRP   H    H N N 342 
TRP   H2   H N N 343 
TRP   HA   H N N 344 
TRP   HB2  H N N 345 
TRP   HB3  H N N 346 
TRP   HD1  H N N 347 
TRP   HE1  H N N 348 
TRP   HE3  H N N 349 
TRP   HZ2  H N N 350 
TRP   HZ3  H N N 351 
TRP   HH2  H N N 352 
TRP   HXT  H N N 353 
TYR   N    N N N 354 
TYR   CA   C N S 355 
TYR   C    C N N 356 
TYR   O    O N N 357 
TYR   CB   C N N 358 
TYR   CG   C Y N 359 
TYR   CD1  C Y N 360 
TYR   CD2  C Y N 361 
TYR   CE1  C Y N 362 
TYR   CE2  C Y N 363 
TYR   CZ   C Y N 364 
TYR   OH   O N N 365 
TYR   OXT  O N N 366 
TYR   H    H N N 367 
TYR   H2   H N N 368 
TYR   HA   H N N 369 
TYR   HB2  H N N 370 
TYR   HB3  H N N 371 
TYR   HD1  H N N 372 
TYR   HD2  H N N 373 
TYR   HE1  H N N 374 
TYR   HE2  H N N 375 
TYR   HH   H N N 376 
TYR   HXT  H N N 377 
VAL   N    N N N 378 
VAL   CA   C N S 379 
VAL   C    C N N 380 
VAL   O    O N N 381 
VAL   CB   C N N 382 
VAL   CG1  C N N 383 
VAL   CG2  C N N 384 
VAL   OXT  O N N 385 
VAL   H    H N N 386 
VAL   H2   H N N 387 
VAL   HA   H N N 388 
VAL   HB   H N N 389 
VAL   HG11 H N N 390 
VAL   HG12 H N N 391 
VAL   HG13 H N N 392 
VAL   HG21 H N N 393 
VAL   HG22 H N N 394 
VAL   HG23 H N N 395 
VAL   HXT  H N N 396 
# 
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 
A1AXM N1  C1   trip N N 1   
A1AXM C1  C2   sing N N 2   
A1AXM C2  C3   doub Y N 3   
A1AXM C3  C4   sing Y N 4   
A1AXM C4  C5   doub Y N 5   
A1AXM C5  C6   sing Y N 6   
A1AXM C6  C7   doub Y N 7   
A1AXM C7  N2   sing N N 8   
A1AXM N2  C8   sing Y N 9   
A1AXM C8  C9   doub Y N 10  
A1AXM C9  N3   sing Y N 11  
A1AXM N3  C10  doub Y N 12  
A1AXM C2  C7   sing Y N 13  
A1AXM N2  C10  sing Y N 14  
A1AXM C3  H1   sing N N 15  
A1AXM C4  H2   sing N N 16  
A1AXM C5  H3   sing N N 17  
A1AXM C10 H7   sing N N 18  
A1AXM C6  H4   sing N N 19  
A1AXM C8  H5   sing N N 20  
A1AXM C9  H6   sing N N 21  
ALA   N   CA   sing N N 22  
ALA   N   H    sing N N 23  
ALA   N   H2   sing N N 24  
ALA   CA  C    sing N N 25  
ALA   CA  CB   sing N N 26  
ALA   CA  HA   sing N N 27  
ALA   C   O    doub N N 28  
ALA   C   OXT  sing N N 29  
ALA   CB  HB1  sing N N 30  
ALA   CB  HB2  sing N N 31  
ALA   CB  HB3  sing N N 32  
ALA   OXT HXT  sing N N 33  
ARG   N   CA   sing N N 34  
ARG   N   H    sing N N 35  
ARG   N   H2   sing N N 36  
ARG   CA  C    sing N N 37  
ARG   CA  CB   sing N N 38  
ARG   CA  HA   sing N N 39  
ARG   C   O    doub N N 40  
ARG   C   OXT  sing N N 41  
ARG   CB  CG   sing N N 42  
ARG   CB  HB2  sing N N 43  
ARG   CB  HB3  sing N N 44  
ARG   CG  CD   sing N N 45  
ARG   CG  HG2  sing N N 46  
ARG   CG  HG3  sing N N 47  
ARG   CD  NE   sing N N 48  
ARG   CD  HD2  sing N N 49  
ARG   CD  HD3  sing N N 50  
ARG   NE  CZ   sing N N 51  
ARG   NE  HE   sing N N 52  
ARG   CZ  NH1  sing N N 53  
ARG   CZ  NH2  doub N N 54  
ARG   NH1 HH11 sing N N 55  
ARG   NH1 HH12 sing N N 56  
ARG   NH2 HH21 sing N N 57  
ARG   NH2 HH22 sing N N 58  
ARG   OXT HXT  sing N N 59  
ASN   N   CA   sing N N 60  
ASN   N   H    sing N N 61  
ASN   N   H2   sing N N 62  
ASN   CA  C    sing N N 63  
ASN   CA  CB   sing N N 64  
ASN   CA  HA   sing N N 65  
ASN   C   O    doub N N 66  
ASN   C   OXT  sing N N 67  
ASN   CB  CG   sing N N 68  
ASN   CB  HB2  sing N N 69  
ASN   CB  HB3  sing N N 70  
ASN   CG  OD1  doub N N 71  
ASN   CG  ND2  sing N N 72  
ASN   ND2 HD21 sing N N 73  
ASN   ND2 HD22 sing N N 74  
ASN   OXT HXT  sing N N 75  
ASP   N   CA   sing N N 76  
ASP   N   H    sing N N 77  
ASP   N   H2   sing N N 78  
ASP   CA  C    sing N N 79  
ASP   CA  CB   sing N N 80  
ASP   CA  HA   sing N N 81  
ASP   C   O    doub N N 82  
ASP   C   OXT  sing N N 83  
ASP   CB  CG   sing N N 84  
ASP   CB  HB2  sing N N 85  
ASP   CB  HB3  sing N N 86  
ASP   CG  OD1  doub N N 87  
ASP   CG  OD2  sing N N 88  
ASP   OD2 HD2  sing N N 89  
ASP   OXT HXT  sing N N 90  
GLN   N   CA   sing N N 91  
GLN   N   H    sing N N 92  
GLN   N   H2   sing N N 93  
GLN   CA  C    sing N N 94  
GLN   CA  CB   sing N N 95  
GLN   CA  HA   sing N N 96  
GLN   C   O    doub N N 97  
GLN   C   OXT  sing N N 98  
GLN   CB  CG   sing N N 99  
GLN   CB  HB2  sing N N 100 
GLN   CB  HB3  sing N N 101 
GLN   CG  CD   sing N N 102 
GLN   CG  HG2  sing N N 103 
GLN   CG  HG3  sing N N 104 
GLN   CD  OE1  doub N N 105 
GLN   CD  NE2  sing N N 106 
GLN   NE2 HE21 sing N N 107 
GLN   NE2 HE22 sing N N 108 
GLN   OXT HXT  sing N N 109 
GLU   N   CA   sing N N 110 
GLU   N   H    sing N N 111 
GLU   N   H2   sing N N 112 
GLU   CA  C    sing N N 113 
GLU   CA  CB   sing N N 114 
GLU   CA  HA   sing N N 115 
GLU   C   O    doub N N 116 
GLU   C   OXT  sing N N 117 
GLU   CB  CG   sing N N 118 
GLU   CB  HB2  sing N N 119 
GLU   CB  HB3  sing N N 120 
GLU   CG  CD   sing N N 121 
GLU   CG  HG2  sing N N 122 
GLU   CG  HG3  sing N N 123 
GLU   CD  OE1  doub N N 124 
GLU   CD  OE2  sing N N 125 
GLU   OE2 HE2  sing N N 126 
GLU   OXT HXT  sing N N 127 
GLY   N   CA   sing N N 128 
GLY   N   H    sing N N 129 
GLY   N   H2   sing N N 130 
GLY   CA  C    sing N N 131 
GLY   CA  HA2  sing N N 132 
GLY   CA  HA3  sing N N 133 
GLY   C   O    doub N N 134 
GLY   C   OXT  sing N N 135 
GLY   OXT HXT  sing N N 136 
HIS   N   CA   sing N N 137 
HIS   N   H    sing N N 138 
HIS   N   H2   sing N N 139 
HIS   CA  C    sing N N 140 
HIS   CA  CB   sing N N 141 
HIS   CA  HA   sing N N 142 
HIS   C   O    doub N N 143 
HIS   C   OXT  sing N N 144 
HIS   CB  CG   sing N N 145 
HIS   CB  HB2  sing N N 146 
HIS   CB  HB3  sing N N 147 
HIS   CG  ND1  sing Y N 148 
HIS   CG  CD2  doub Y N 149 
HIS   ND1 CE1  doub Y N 150 
HIS   ND1 HD1  sing N N 151 
HIS   CD2 NE2  sing Y N 152 
HIS   CD2 HD2  sing N N 153 
HIS   CE1 NE2  sing Y N 154 
HIS   CE1 HE1  sing N N 155 
HIS   NE2 HE2  sing N N 156 
HIS   OXT HXT  sing N N 157 
HOH   O   H1   sing N N 158 
HOH   O   H2   sing N N 159 
ILE   N   CA   sing N N 160 
ILE   N   H    sing N N 161 
ILE   N   H2   sing N N 162 
ILE   CA  C    sing N N 163 
ILE   CA  CB   sing N N 164 
ILE   CA  HA   sing N N 165 
ILE   C   O    doub N N 166 
ILE   C   OXT  sing N N 167 
ILE   CB  CG1  sing N N 168 
ILE   CB  CG2  sing N N 169 
ILE   CB  HB   sing N N 170 
ILE   CG1 CD1  sing N N 171 
ILE   CG1 HG12 sing N N 172 
ILE   CG1 HG13 sing N N 173 
ILE   CG2 HG21 sing N N 174 
ILE   CG2 HG22 sing N N 175 
ILE   CG2 HG23 sing N N 176 
ILE   CD1 HD11 sing N N 177 
ILE   CD1 HD12 sing N N 178 
ILE   CD1 HD13 sing N N 179 
ILE   OXT HXT  sing N N 180 
LEU   N   CA   sing N N 181 
LEU   N   H    sing N N 182 
LEU   N   H2   sing N N 183 
LEU   CA  C    sing N N 184 
LEU   CA  CB   sing N N 185 
LEU   CA  HA   sing N N 186 
LEU   C   O    doub N N 187 
LEU   C   OXT  sing N N 188 
LEU   CB  CG   sing N N 189 
LEU   CB  HB2  sing N N 190 
LEU   CB  HB3  sing N N 191 
LEU   CG  CD1  sing N N 192 
LEU   CG  CD2  sing N N 193 
LEU   CG  HG   sing N N 194 
LEU   CD1 HD11 sing N N 195 
LEU   CD1 HD12 sing N N 196 
LEU   CD1 HD13 sing N N 197 
LEU   CD2 HD21 sing N N 198 
LEU   CD2 HD22 sing N N 199 
LEU   CD2 HD23 sing N N 200 
LEU   OXT HXT  sing N N 201 
LYS   N   CA   sing N N 202 
LYS   N   H    sing N N 203 
LYS   N   H2   sing N N 204 
LYS   CA  C    sing N N 205 
LYS   CA  CB   sing N N 206 
LYS   CA  HA   sing N N 207 
LYS   C   O    doub N N 208 
LYS   C   OXT  sing N N 209 
LYS   CB  CG   sing N N 210 
LYS   CB  HB2  sing N N 211 
LYS   CB  HB3  sing N N 212 
LYS   CG  CD   sing N N 213 
LYS   CG  HG2  sing N N 214 
LYS   CG  HG3  sing N N 215 
LYS   CD  CE   sing N N 216 
LYS   CD  HD2  sing N N 217 
LYS   CD  HD3  sing N N 218 
LYS   CE  NZ   sing N N 219 
LYS   CE  HE2  sing N N 220 
LYS   CE  HE3  sing N N 221 
LYS   NZ  HZ1  sing N N 222 
LYS   NZ  HZ2  sing N N 223 
LYS   NZ  HZ3  sing N N 224 
LYS   OXT HXT  sing N N 225 
MET   N   CA   sing N N 226 
MET   N   H    sing N N 227 
MET   N   H2   sing N N 228 
MET   CA  C    sing N N 229 
MET   CA  CB   sing N N 230 
MET   CA  HA   sing N N 231 
MET   C   O    doub N N 232 
MET   C   OXT  sing N N 233 
MET   CB  CG   sing N N 234 
MET   CB  HB2  sing N N 235 
MET   CB  HB3  sing N N 236 
MET   CG  SD   sing N N 237 
MET   CG  HG2  sing N N 238 
MET   CG  HG3  sing N N 239 
MET   SD  CE   sing N N 240 
MET   CE  HE1  sing N N 241 
MET   CE  HE2  sing N N 242 
MET   CE  HE3  sing N N 243 
MET   OXT HXT  sing N N 244 
PHE   N   CA   sing N N 245 
PHE   N   H    sing N N 246 
PHE   N   H2   sing N N 247 
PHE   CA  C    sing N N 248 
PHE   CA  CB   sing N N 249 
PHE   CA  HA   sing N N 250 
PHE   C   O    doub N N 251 
PHE   C   OXT  sing N N 252 
PHE   CB  CG   sing N N 253 
PHE   CB  HB2  sing N N 254 
PHE   CB  HB3  sing N N 255 
PHE   CG  CD1  doub Y N 256 
PHE   CG  CD2  sing Y N 257 
PHE   CD1 CE1  sing Y N 258 
PHE   CD1 HD1  sing N N 259 
PHE   CD2 CE2  doub Y N 260 
PHE   CD2 HD2  sing N N 261 
PHE   CE1 CZ   doub Y N 262 
PHE   CE1 HE1  sing N N 263 
PHE   CE2 CZ   sing Y N 264 
PHE   CE2 HE2  sing N N 265 
PHE   CZ  HZ   sing N N 266 
PHE   OXT HXT  sing N N 267 
PRO   N   CA   sing N N 268 
PRO   N   CD   sing N N 269 
PRO   N   H    sing N N 270 
PRO   CA  C    sing N N 271 
PRO   CA  CB   sing N N 272 
PRO   CA  HA   sing N N 273 
PRO   C   O    doub N N 274 
PRO   C   OXT  sing N N 275 
PRO   CB  CG   sing N N 276 
PRO   CB  HB2  sing N N 277 
PRO   CB  HB3  sing N N 278 
PRO   CG  CD   sing N N 279 
PRO   CG  HG2  sing N N 280 
PRO   CG  HG3  sing N N 281 
PRO   CD  HD2  sing N N 282 
PRO   CD  HD3  sing N N 283 
PRO   OXT HXT  sing N N 284 
SER   N   CA   sing N N 285 
SER   N   H    sing N N 286 
SER   N   H2   sing N N 287 
SER   CA  C    sing N N 288 
SER   CA  CB   sing N N 289 
SER   CA  HA   sing N N 290 
SER   C   O    doub N N 291 
SER   C   OXT  sing N N 292 
SER   CB  OG   sing N N 293 
SER   CB  HB2  sing N N 294 
SER   CB  HB3  sing N N 295 
SER   OG  HG   sing N N 296 
SER   OXT HXT  sing N N 297 
THR   N   CA   sing N N 298 
THR   N   H    sing N N 299 
THR   N   H2   sing N N 300 
THR   CA  C    sing N N 301 
THR   CA  CB   sing N N 302 
THR   CA  HA   sing N N 303 
THR   C   O    doub N N 304 
THR   C   OXT  sing N N 305 
THR   CB  OG1  sing N N 306 
THR   CB  CG2  sing N N 307 
THR   CB  HB   sing N N 308 
THR   OG1 HG1  sing N N 309 
THR   CG2 HG21 sing N N 310 
THR   CG2 HG22 sing N N 311 
THR   CG2 HG23 sing N N 312 
THR   OXT HXT  sing N N 313 
TRP   N   CA   sing N N 314 
TRP   N   H    sing N N 315 
TRP   N   H2   sing N N 316 
TRP   CA  C    sing N N 317 
TRP   CA  CB   sing N N 318 
TRP   CA  HA   sing N N 319 
TRP   C   O    doub N N 320 
TRP   C   OXT  sing N N 321 
TRP   CB  CG   sing N N 322 
TRP   CB  HB2  sing N N 323 
TRP   CB  HB3  sing N N 324 
TRP   CG  CD1  doub Y N 325 
TRP   CG  CD2  sing Y N 326 
TRP   CD1 NE1  sing Y N 327 
TRP   CD1 HD1  sing N N 328 
TRP   CD2 CE2  doub Y N 329 
TRP   CD2 CE3  sing Y N 330 
TRP   NE1 CE2  sing Y N 331 
TRP   NE1 HE1  sing N N 332 
TRP   CE2 CZ2  sing Y N 333 
TRP   CE3 CZ3  doub Y N 334 
TRP   CE3 HE3  sing N N 335 
TRP   CZ2 CH2  doub Y N 336 
TRP   CZ2 HZ2  sing N N 337 
TRP   CZ3 CH2  sing Y N 338 
TRP   CZ3 HZ3  sing N N 339 
TRP   CH2 HH2  sing N N 340 
TRP   OXT HXT  sing N N 341 
TYR   N   CA   sing N N 342 
TYR   N   H    sing N N 343 
TYR   N   H2   sing N N 344 
TYR   CA  C    sing N N 345 
TYR   CA  CB   sing N N 346 
TYR   CA  HA   sing N N 347 
TYR   C   O    doub N N 348 
TYR   C   OXT  sing N N 349 
TYR   CB  CG   sing N N 350 
TYR   CB  HB2  sing N N 351 
TYR   CB  HB3  sing N N 352 
TYR   CG  CD1  doub Y N 353 
TYR   CG  CD2  sing Y N 354 
TYR   CD1 CE1  sing Y N 355 
TYR   CD1 HD1  sing N N 356 
TYR   CD2 CE2  doub Y N 357 
TYR   CD2 HD2  sing N N 358 
TYR   CE1 CZ   doub Y N 359 
TYR   CE1 HE1  sing N N 360 
TYR   CE2 CZ   sing Y N 361 
TYR   CE2 HE2  sing N N 362 
TYR   CZ  OH   sing N N 363 
TYR   OH  HH   sing N N 364 
TYR   OXT HXT  sing N N 365 
VAL   N   CA   sing N N 366 
VAL   N   H    sing N N 367 
VAL   N   H2   sing N N 368 
VAL   CA  C    sing N N 369 
VAL   CA  CB   sing N N 370 
VAL   CA  HA   sing N N 371 
VAL   C   O    doub N N 372 
VAL   C   OXT  sing N N 373 
VAL   CB  CG1  sing N N 374 
VAL   CB  CG2  sing N N 375 
VAL   CB  HB   sing N N 376 
VAL   CG1 HG11 sing N N 377 
VAL   CG1 HG12 sing N N 378 
VAL   CG1 HG13 sing N N 379 
VAL   CG2 HG21 sing N N 380 
VAL   CG2 HG22 sing N N 381 
VAL   CG2 HG23 sing N N 382 
VAL   OXT HXT  sing N N 383 
# 
_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                    7HAF 
_atom_sites.fract_transf_matrix[1][1]   0.014883 
_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]   0.010949 
_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]   0.010074 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
_atom_type.scat_dispersion_real 
_atom_type.scat_dispersion_imag 
_atom_type.scat_Cromer_Mann_a1 
_atom_type.scat_Cromer_Mann_a2 
_atom_type.scat_Cromer_Mann_a3 
_atom_type.scat_Cromer_Mann_a4 
_atom_type.scat_Cromer_Mann_b1 
_atom_type.scat_Cromer_Mann_b2 
_atom_type.scat_Cromer_Mann_b3 
_atom_type.scat_Cromer_Mann_b4 
_atom_type.scat_Cromer_Mann_c 
_atom_type.scat_source 
_atom_type.scat_dispersion_source 
C ? ? 3.54356 2.42580 ? ? 25.62398 1.50364  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
N ? ? 4.01032 2.96436 ? ? 19.97189 1.75589  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O ? ? 4.49882 3.47563 ? ? 15.80542 1.70748  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
S ? ? 9.55732 6.39887 ? ? 1.23737  29.19336 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N   . GLU   A 1 9   ? 5.74877   -29.60629 -38.33369 1.000 43.14358 ? 16  GLU   A N   1 
ATOM   2    C CA  . GLU   A 1 9   ? 7.01846   -28.89439 -38.45479 1.000 46.24100 ? 16  GLU   A CA  1 
ATOM   3    C C   . GLU   A 1 9   ? 7.24013   -27.96808 -37.25460 1.000 41.04056 ? 16  GLU   A C   1 
ATOM   4    O O   . GLU   A 1 9   ? 6.64573   -26.89106 -37.17136 1.000 45.92559 ? 16  GLU   A O   1 
ATOM   5    C CB  . GLU   A 1 9   ? 7.05471   -28.10473 -39.76753 1.000 54.32491 ? 16  GLU   A CB  1 
ATOM   6    C CG  . GLU   A 1 9   ? 8.44338   -27.96095 -40.40144 1.000 59.83587 ? 16  GLU   A CG  1 
ATOM   7    C CD  . GLU   A 1 9   ? 9.17460   -26.70021 -39.97223 1.000 58.24740 ? 16  GLU   A CD  1 
ATOM   8    O OE1 . GLU   A 1 9   ? 8.76375   -26.08043 -38.96809 1.000 58.44737 ? 16  GLU   A OE1 1 
ATOM   9    O OE2 . GLU   A 1 9   ? 10.15461  -26.31819 -40.65028 1.000 61.19820 ? 16  GLU   A OE2 1 
ATOM   10   N N   . VAL   A 1 10  ? 8.10184   -28.38298 -36.33233 1.000 32.91736 ? 17  VAL   A N   1 
ATOM   11   C CA  . VAL   A 1 10  ? 8.34507   -27.64676 -35.09901 1.000 25.32276 ? 17  VAL   A CA  1 
ATOM   12   C C   . VAL   A 1 10  ? 9.72890   -27.02018 -35.15378 1.000 28.28508 ? 17  VAL   A C   1 
ATOM   13   O O   . VAL   A 1 10  ? 10.72146  -27.70855 -35.41874 1.000 30.66911 ? 17  VAL   A O   1 
ATOM   14   C CB  . VAL   A 1 10  ? 8.21677   -28.55260 -33.86336 1.000 34.56639 ? 17  VAL   A CB  1 
ATOM   15   C CG1 . VAL   A 1 10  ? 8.55834   -27.76428 -32.60401 1.000 28.03355 ? 17  VAL   A CG1 1 
ATOM   16   C CG2 . VAL   A 1 10  ? 6.81932   -29.16164 -33.79271 1.000 36.95399 ? 17  VAL   A CG2 1 
ATOM   17   N N   . GLU   A 1 11  ? 9.79589   -25.72036 -34.89433 1.000 21.45992 ? 18  GLU   A N   1 
ATOM   18   C CA  . GLU   A 1 11  ? 11.06584  -25.00852 -34.80929 1.000 22.41351 ? 18  GLU   A CA  1 
ATOM   19   C C   . GLU   A 1 11  ? 11.42558  -24.77722 -33.34823 1.000 18.45401 ? 18  GLU   A C   1 
ATOM   20   O O   . GLU   A 1 11  ? 10.58490  -24.32060 -32.55344 1.000 17.34115 ? 18  GLU   A O   1 
ATOM   21   C CB  . GLU   A 1 11  ? 11.00578  -23.68215 -35.56775 1.000 21.27255 ? 18  GLU   A CB  1 
ATOM   22   C CG  . GLU   A 1 11  ? 10.87922  -23.85583 -37.08553 1.000 23.34571 ? 18  GLU   A CG  1 
ATOM   23   C CD  . GLU   A 1 11  ? 10.75051  -22.52802 -37.82793 1.000 29.79006 ? 18  GLU   A CD  1 
ATOM   24   O OE1 . GLU   A 1 11  ? 9.77579   -21.79212 -37.57524 1.000 32.83975 ? 18  GLU   A OE1 1 
ATOM   25   O OE2 . GLU   A 1 11  ? 11.58548  -22.25136 -38.71589 1.000 35.40755 ? 18  GLU   A OE2 1 
ATOM   26   N N   . THR   A 1 12  ? 12.67568  -25.07955 -32.99936 1.000 17.38817 ? 19  THR   A N   1 
ATOM   27   C CA  . THR   A 1 12  ? 13.20588  -24.88713 -31.65471 1.000 16.00256 ? 19  THR   A CA  1 
ATOM   28   C C   . THR   A 1 12  ? 14.20188  -23.73602 -31.66846 1.000 16.16647 ? 19  THR   A C   1 
ATOM   29   O O   . THR   A 1 12  ? 15.11306  -23.70841 -32.50794 1.000 15.77760 ? 19  THR   A O   1 
ATOM   30   C CB  . THR   A 1 12  ? 13.86274  -26.17263 -31.14347 1.000 16.80123 ? 19  THR   A CB  1 
ATOM   31   O OG1 . THR   A 1 12  ? 12.91346  -27.24387 -31.22058 1.000 19.58637 ? 19  THR   A OG1 1 
ATOM   32   C CG2 . THR   A 1 12  ? 14.35836  -26.02200 -29.70747 1.000 18.69414 ? 19  THR   A CG2 1 
ATOM   33   N N   . PHE   A 1 13  ? 14.02968  -22.81021 -30.72721 1.000 13.98818 ? 20  PHE   A N   1 
ATOM   34   C CA  . PHE   A 1 13  ? 14.84982  -21.61441 -30.57726 1.000 16.94298 ? 20  PHE   A CA  1 
ATOM   35   C C   . PHE   A 1 13  ? 15.47890  -21.53754 -29.18444 1.000 20.31186 ? 20  PHE   A C   1 
ATOM   36   O O   . PHE   A 1 13  ? 14.92243  -22.02816 -28.19287 1.000 16.89989 ? 20  PHE   A O   1 
ATOM   37   C CB  . PHE   A 1 13  ? 13.99409  -20.34632 -30.78580 1.000 14.94273 ? 20  PHE   A CB  1 
ATOM   38   C CG  . PHE   A 1 13  ? 13.25204  -20.30845 -32.10802 1.000 14.15754 ? 20  PHE   A CG  1 
ATOM   39   C CD1 . PHE   A 1 13  ? 12.02203  -20.94444 -32.24425 1.000 18.55331 ? 20  PHE   A CD1 1 
ATOM   40   C CD2 . PHE   A 1 13  ? 13.76923  -19.62556 -33.20427 1.000 18.31016 ? 20  PHE   A CD2 1 
ATOM   41   C CE1 . PHE   A 1 13  ? 11.31519  -20.91732 -33.43874 1.000 19.28973 ? 20  PHE   A CE1 1 
ATOM   42   C CE2 . PHE   A 1 13  ? 13.06788  -19.58869 -34.41648 1.000 21.70535 ? 20  PHE   A CE2 1 
ATOM   43   C CZ  . PHE   A 1 13  ? 11.83375  -20.24207 -34.53332 1.000 19.31781 ? 20  PHE   A CZ  1 
ATOM   44   N N   . ALA   A 1 14  ? 16.61307  -20.85190 -29.08825 1.000 15.53681 ? 21  ALA   A N   1 
ATOM   45   C CA  . ALA   A 1 14  ? 17.17637  -20.54331 -27.77713 1.000 16.86557 ? 21  ALA   A CA  1 
ATOM   46   C C   . ALA   A 1 14  ? 16.65343  -19.19685 -27.30200 1.000 16.36974 ? 21  ALA   A C   1 
ATOM   47   O O   . ALA   A 1 14  ? 16.59136  -18.24382 -28.07949 1.000 19.10652 ? 21  ALA   A O   1 
ATOM   48   C CB  . ALA   A 1 14  ? 18.70401  -20.51318 -27.83241 1.000 18.77020 ? 21  ALA   A CB  1 
ATOM   49   N N   . PHE   A 1 15  ? 16.25529  -19.12284 -26.03258 1.000 16.78117 ? 22  PHE   A N   1 
ATOM   50   C CA  . PHE   A 1 15  ? 16.04534  -17.80904 -25.43745 1.000 19.19664 ? 22  PHE   A CA  1 
ATOM   51   C C   . PHE   A 1 15  ? 17.34724  -17.01748 -25.48325 1.000 20.67850 ? 22  PHE   A C   1 
ATOM   52   O O   . PHE   A 1 15  ? 18.44316  -17.58441 -25.44431 1.000 20.31435 ? 22  PHE   A O   1 
ATOM   53   C CB  . PHE   A 1 15  ? 15.60062  -17.92090 -23.97271 1.000 17.45345 ? 22  PHE   A CB  1 
ATOM   54   C CG  . PHE   A 1 15  ? 14.18540  -18.39751 -23.78656 1.000 15.13408 ? 22  PHE   A CG  1 
ATOM   55   C CD1 . PHE   A 1 15  ? 13.10895  -17.57290 -24.06711 1.000 15.74694 ? 22  PHE   A CD1 1 
ATOM   56   C CD2 . PHE   A 1 15  ? 13.94249  -19.66334 -23.27572 1.000 14.92722 ? 22  PHE   A CD2 1 
ATOM   57   C CE1 . PHE   A 1 15  ? 11.80299  -18.02166 -23.87339 1.000 15.42519 ? 22  PHE   A CE1 1 
ATOM   58   C CE2 . PHE   A 1 15  ? 12.64789  -20.12031 -23.07643 1.000 15.83247 ? 22  PHE   A CE2 1 
ATOM   59   C CZ  . PHE   A 1 15  ? 11.57436  -19.30832 -23.38045 1.000 13.43860 ? 22  PHE   A CZ  1 
ATOM   60   N N   . GLN   A 1 16  ? 17.23035  -15.69364 -25.56258 1.000 20.83131 ? 23  GLN   A N   1 
ATOM   61   C CA  . GLN   A 1 16  ? 18.37771  -14.86506 -25.24171 1.000 24.33613 ? 23  GLN   A CA  1 
ATOM   62   C C   . GLN   A 1 16  ? 18.82841  -15.17980 -23.82480 1.000 25.27551 ? 23  GLN   A C   1 
ATOM   63   O O   . GLN   A 1 16  ? 18.01880  -15.53239 -22.96734 1.000 23.39356 ? 23  GLN   A O   1 
ATOM   64   C CB  . GLN   A 1 16  ? 18.02686  -13.38894 -25.36950 1.000 24.64694 ? 23  GLN   A CB  1 
ATOM   65   C CG  . GLN   A 1 16  ? 17.52051  -13.00979 -26.74209 1.000 31.13046 ? 23  GLN   A CG  1 
ATOM   66   C CD  . GLN   A 1 16  ? 17.11732  -11.56017 -26.79773 1.000 42.48225 ? 23  GLN   A CD  1 
ATOM   67   O OE1 . GLN   A 1 16  ? 17.95341  -10.68051 -26.99995 1.000 39.88165 ? 23  GLN   A OE1 1 
ATOM   68   N NE2 . GLN   A 1 16  ? 15.83204  -11.29691 -26.58955 1.000 42.38193 ? 23  GLN   A NE2 1 
ATOM   69   N N   . ALA   A 1 17  ? 20.13976  -15.08653 -23.59385 1.000 21.98413 ? 24  ALA   A N   1 
ATOM   70   C CA  . ALA   A 1 17  ? 20.69309  -15.47299 -22.29917 1.000 24.44511 ? 24  ALA   A CA  1 
ATOM   71   C C   . ALA   A 1 17  ? 20.01356  -14.72057 -21.16285 1.000 25.60748 ? 24  ALA   A C   1 
ATOM   72   O O   . ALA   A 1 17  ? 19.74092  -15.29212 -20.09876 1.000 24.47006 ? 24  ALA   A O   1 
ATOM   73   C CB  . ALA   A 1 17  ? 22.19882  -15.22115 -22.28444 1.000 28.22623 ? 24  ALA   A CB  1 
ATOM   74   N N   . GLU   A 1 18  ? 19.70735  -13.44094 -21.38792 1.000 22.78690 ? 25  GLU   A N   1 
ATOM   75   C CA  . GLU   A 1 18  ? 19.10742  -12.61120 -20.34731 1.000 26.29856 ? 25  GLU   A CA  1 
ATOM   76   C C   . GLU   A 1 18  ? 17.70433  -13.08675 -19.96250 1.000 21.34395 ? 25  GLU   A C   1 
ATOM   77   O O   . GLU   A 1 18  ? 17.32687  -13.00936 -18.78609 1.000 22.19695 ? 25  GLU   A O   1 
ATOM   78   C CB  . GLU   A 1 18  ? 19.08213  -11.15459 -20.81052 1.000 25.47030 ? 25  GLU   A CB  1 
ATOM   79   C CG  . GLU   A 1 18  ? 20.47331  -10.56045 -21.02709 1.000 26.62629 ? 25  GLU   A CG  1 
ATOM   80   C CD  . GLU   A 1 18  ? 21.04474  -10.83225 -22.41130 1.000 38.80948 ? 25  GLU   A CD  1 
ATOM   81   O OE1 . GLU   A 1 18  ? 20.45027  -11.62098 -23.18617 1.000 33.38771 ? 25  GLU   A OE1 1 
ATOM   82   O OE2 . GLU   A 1 18  ? 22.10839  -10.25479 -22.72308 1.000 42.35009 ? 25  GLU   A OE2 1 
ATOM   83   N N   . ILE   A 1 19  ? 16.91214  -13.55425 -20.94220 1.000 19.36654 ? 26  ILE   A N   1 
ATOM   84   C CA  . ILE   A 1 19  ? 15.55805  -14.04855 -20.68513 1.000 18.85628 ? 26  ILE   A CA  1 
ATOM   85   C C   . ILE   A 1 19  ? 15.61820  -15.41607 -20.01545 1.000 19.76959 ? 26  ILE   A C   1 
ATOM   86   O O   . ILE   A 1 19  ? 14.84223  -15.71583 -19.09541 1.000 18.50931 ? 26  ILE   A O   1 
ATOM   87   C CB  . ILE   A 1 19  ? 14.74744  -14.11318 -21.99819 1.000 18.45674 ? 26  ILE   A CB  1 
ATOM   88   C CG1 . ILE   A 1 19  ? 14.56933  -12.71037 -22.58631 1.000 23.68407 ? 26  ILE   A CG1 1 
ATOM   89   C CG2 . ILE   A 1 19  ? 13.39038  -14.79735 -21.74507 1.000 19.45780 ? 26  ILE   A CG2 1 
ATOM   90   C CD1 . ILE   A 1 19  ? 13.78872  -11.78833 -21.67875 1.000 30.74658 ? 26  ILE   A CD1 1 
ATOM   91   N N   . ALA   A 1 20  ? 16.55605  -16.26033 -20.45442 1.000 17.14080 ? 27  ALA   A N   1 
ATOM   92   C CA  . ALA   A 1 20  ? 16.78258  -17.52951 -19.77297 1.000 20.82095 ? 27  ALA   A CA  1 
ATOM   93   C C   . ALA   A 1 20  ? 17.17407  -17.29170 -18.32124 1.000 19.91981 ? 27  ALA   A C   1 
ATOM   94   O O   . ALA   A 1 20  ? 16.72741  -18.01634 -17.42844 1.000 20.05495 ? 27  ALA   A O   1 
ATOM   95   C CB  . ALA   A 1 20  ? 17.85823  -18.34774 -20.49205 1.000 19.33212 ? 27  ALA   A CB  1 
ATOM   96   N N   . GLN   A 1 21  ? 17.98059  -16.25498 -18.07004 1.000 21.09383 ? 28  GLN   A N   1 
ATOM   97   C CA  . GLN   A 1 21  ? 18.37046  -15.90706 -16.70630 1.000 18.72807 ? 28  GLN   A CA  1 
ATOM   98   C C   . GLN   A 1 21  ? 17.17554  -15.42784 -15.89448 1.000 21.48442 ? 28  GLN   A C   1 
ATOM   99   O O   . GLN   A 1 21  ? 17.04811  -15.76296 -14.70717 1.000 20.36815 ? 28  GLN   A O   1 
ATOM   100  C CB  . GLN   A 1 21  ? 19.46200  -14.83214 -16.72687 1.000 22.21867 ? 28  GLN   A CB  1 
ATOM   101  C CG  . GLN   A 1 21  ? 20.14487  -14.59739 -15.39183 1.000 32.90178 ? 28  GLN   A CG  1 
ATOM   102  C CD  . GLN   A 1 21  ? 21.30746  -13.63508 -15.52499 1.000 41.55107 ? 28  GLN   A CD  1 
ATOM   103  O OE1 . GLN   A 1 21  ? 21.43608  -12.94207 -16.53756 1.000 42.94703 ? 28  GLN   A OE1 1 
ATOM   104  N NE2 . GLN   A 1 21  ? 22.16002  -13.58047 -14.50439 1.000 42.63785 ? 28  GLN   A NE2 1 
ATOM   105  N N   . LEU   A 1 22  ? 16.29673  -14.63330 -16.51699 1.000 17.67972 ? 29  LEU   A N   1 
ATOM   106  C CA  . LEU   A 1 22  ? 15.07504  -14.19632 -15.84530 1.000 18.24462 ? 29  LEU   A CA  1 
ATOM   107  C C   . LEU   A 1 22  ? 14.20030  -15.38480 -15.49082 1.000 17.63160 ? 29  LEU   A C   1 
ATOM   108  O O   . LEU   A 1 22  ? 13.64637  -15.45369 -14.38472 1.000 19.19232 ? 29  LEU   A O   1 
ATOM   109  C CB  . LEU   A 1 22  ? 14.30421  -13.20982 -16.72545 1.000 18.31931 ? 29  LEU   A CB  1 
ATOM   110  C CG  . LEU   A 1 22  ? 12.91076  -12.84459 -16.18066 1.000 20.65292 ? 29  LEU   A CG  1 
ATOM   111  C CD1 . LEU   A 1 22  ? 13.02766  -12.01267 -14.88110 1.000 18.91290 ? 29  LEU   A CD1 1 
ATOM   112  C CD2 . LEU   A 1 22  ? 12.09428  -12.12210 -17.22836 1.000 17.44929 ? 29  LEU   A CD2 1 
ATOM   113  N N   . MET   A 1 23  ? 14.07028  -16.33925 -16.41788 1.000 17.60030 ? 30  MET   A N   1 
ATOM   114  C CA  . MET   A 1 23  ? 13.22064  -17.48916 -16.15094 1.000 15.20846 ? 30  MET   A CA  1 
ATOM   115  C C   . MET   A 1 23  ? 13.79461  -18.33733 -15.01381 1.000 16.46567 ? 30  MET   A C   1 
ATOM   116  O O   . MET   A 1 23  ? 13.04810  -18.78196 -14.13318 1.000 16.47430 ? 30  MET   A O   1 
ATOM   117  C CB  . MET   A 1 23  ? 13.04949  -18.29759 -17.43589 1.000 15.15195 ? 30  MET   A CB  1 
ATOM   118  C CG  . MET   A 1 23  ? 12.02704  -17.67970 -18.37499 1.000 15.27330 ? 30  MET   A CG  1 
ATOM   119  S SD  . MET   A 1 23  ? 12.08573  -18.33700 -20.03842 1.000 15.18349 ? 30  MET   A SD  1 
ATOM   120  C CE  . MET   A 1 23  ? 10.79949  -19.57395 -19.86714 1.000 18.92430 ? 30  MET   A CE  1 
ATOM   121  N N   . SER   A 1 24  ? 15.12031  -18.54739 -14.99996 1.000 16.23287 ? 31  SER   A N   1 
ATOM   122  C CA  . SER   A 1 24  ? 15.75061  -19.28119 -13.89643 1.000 14.95602 ? 31  SER   A CA  1 
ATOM   123  C C   . SER   A 1 24  ? 15.55789  -18.57401 -12.56285 1.000 19.45611 ? 31  SER   A C   1 
ATOM   124  O O   . SER   A 1 24  ? 15.33535  -19.22743 -11.53938 1.000 19.41237 ? 31  SER   A O   1 
ATOM   125  C CB  . SER   A 1 24  ? 17.24952  -19.52107 -14.14060 1.000 20.51302 ? 31  SER   A CB  1 
ATOM   126  O OG  . SER   A 1 24  ? 17.47896  -20.18053 -15.36951 1.000 28.22454 ? 31  SER   A OG  1 
ATOM   127  N N   . LEU   A 1 25  ? 15.62820  -17.24124 -12.54748 1.000 19.39197 ? 32  LEU   A N   1 
ATOM   128  C CA  . LEU   A 1 25  ? 15.39720  -16.52016 -11.29829 1.000 19.59539 ? 32  LEU   A CA  1 
ATOM   129  C C   . LEU   A 1 25  ? 13.96296  -16.71171 -10.80647 1.000 21.22004 ? 32  LEU   A C   1 
ATOM   130  O O   . LEU   A 1 25  ? 13.72705  -16.88033 -9.60372  1.000 22.15424 ? 32  LEU   A O   1 
ATOM   131  C CB  . LEU   A 1 25  ? 15.72506  -15.03644 -11.48656 1.000 18.80903 ? 32  LEU   A CB  1 
ATOM   132  C CG  . LEU   A 1 25  ? 15.53423  -14.11543 -10.27980 1.000 23.31216 ? 32  LEU   A CG  1 
ATOM   133  C CD1 . LEU   A 1 25  ? 16.52906  -12.98253 -10.36262 1.000 28.50906 ? 32  LEU   A CD1 1 
ATOM   134  C CD2 . LEU   A 1 25  ? 14.09365  -13.56974 -10.13201 1.000 23.69852 ? 32  LEU   A CD2 1 
ATOM   135  N N   . ILE   A 1 26  ? 12.99015  -16.67489 -11.71727 1.000 16.85441 ? 33  ILE   A N   1 
ATOM   136  C CA  . ILE   A 1 26  ? 11.59759  -16.86609 -11.33070 1.000 14.02845 ? 33  ILE   A CA  1 
ATOM   137  C C   . ILE   A 1 26  ? 11.36995  -18.28190 -10.81512 1.000 18.30819 ? 33  ILE   A C   1 
ATOM   138  O O   . ILE   A 1 26  ? 10.62464  -18.49775 -9.85422  1.000 18.62194 ? 33  ILE   A O   1 
ATOM   139  C CB  . ILE   A 1 26  ? 10.69479  -16.53983 -12.53835 1.000 15.19493 ? 33  ILE   A CB  1 
ATOM   140  C CG1 . ILE   A 1 26  ? 10.72389  -15.03663 -12.80728 1.000 17.09915 ? 33  ILE   A CG1 1 
ATOM   141  C CG2 . ILE   A 1 26  ? 9.25434   -17.10722 -12.34879 1.000 18.32458 ? 33  ILE   A CG2 1 
ATOM   142  C CD1 . ILE   A 1 26  ? 10.14192  -14.64558 -14.18126 1.000 18.92553 ? 33  ILE   A CD1 1 
ATOM   143  N N   . ILE   A 1 27  ? 12.01263  -19.26715 -11.43649 1.000 17.21850 ? 34  ILE   A N   1 
ATOM   144  C CA  . ILE   A 1 27  ? 11.79720  -20.65773 -11.04749 1.000 19.45572 ? 34  ILE   A CA  1 
ATOM   145  C C   . ILE   A 1 27  ? 12.50968  -20.99160 -9.74394  1.000 17.88891 ? 34  ILE   A C   1 
ATOM   146  O O   . ILE   A 1 27  ? 11.97535  -21.73831 -8.91731  1.000 22.76251 ? 34  ILE   A O   1 
ATOM   147  C CB  . ILE   A 1 27  ? 12.22528  -21.58975 -12.19173 1.000 19.33355 ? 34  ILE   A CB  1 
ATOM   148  C CG1 . ILE   A 1 27  ? 11.24918  -21.41807 -13.36533 1.000 20.04331 ? 34  ILE   A CG1 1 
ATOM   149  C CG2 . ILE   A 1 27  ? 12.29606  -23.05867 -11.71046 1.000 18.68751 ? 34  ILE   A CG2 1 
ATOM   150  C CD1 . ILE   A 1 27  ? 11.77856  -21.99279 -14.67563 1.000 23.77887 ? 34  ILE   A CD1 1 
ATOM   151  N N   . ASN   A 1 28  ? 13.70869  -20.43959 -9.52495  1.000 17.89551 ? 35  ASN   A N   1 
ATOM   152  C CA  . ASN   A 1 28  ? 14.56205  -20.86991 -8.42286  1.000 20.12973 ? 35  ASN   A CA  1 
ATOM   153  C C   . ASN   A 1 28  ? 14.43625  -20.03029 -7.16137  1.000 21.00054 ? 35  ASN   A C   1 
ATOM   154  O O   . ASN   A 1 28  ? 14.75104  -20.53386 -6.08164  1.000 27.66116 ? 35  ASN   A O   1 
ATOM   155  C CB  . ASN   A 1 28  ? 16.03320  -20.86739 -8.84122  1.000 21.88326 ? 35  ASN   A CB  1 
ATOM   156  C CG  . ASN   A 1 28  ? 16.32614  -21.85414 -9.94601  1.000 24.78403 ? 35  ASN   A CG  1 
ATOM   157  O OD1 . ASN   A 1 28  ? 15.72699  -22.92591 -10.01118 1.000 31.07540 ? 35  ASN   A OD1 1 
ATOM   158  N ND2 . ASN   A 1 28  ? 17.27514  -21.50935 -10.80985 1.000 34.50695 ? 35  ASN   A ND2 1 
ATOM   159  N N   . THR   A 1 29  ? 14.02671  -18.76742 -7.25706  1.000 20.72963 ? 36  THR   A N   1 
ATOM   160  C CA  . THR   A 1 29  ? 13.99188  -17.91995 -6.06837  1.000 19.23550 ? 36  THR   A CA  1 
ATOM   161  C C   . THR   A 1 29  ? 12.87173  -18.36059 -5.12539  1.000 19.69771 ? 36  THR   A C   1 
ATOM   162  O O   . THR   A 1 29  ? 11.74892  -18.63457 -5.55196  1.000 21.50299 ? 36  THR   A O   1 
ATOM   163  C CB  . THR   A 1 29  ? 13.79520  -16.44849 -6.45744  1.000 23.08471 ? 36  THR   A CB  1 
ATOM   164  O OG1 . THR   A 1 29  ? 14.83836  -16.03233 -7.34824  1.000 22.29855 ? 36  THR   A OG1 1 
ATOM   165  C CG2 . THR   A 1 29  ? 13.81139  -15.55285 -5.22057  1.000 24.45990 ? 36  THR   A CG2 1 
ATOM   166  N N   . PHE   A 1 30  ? 13.16802  -18.41603 -3.82785  1.000 20.74629 ? 37  PHE   A N   1 
ATOM   167  C CA  . PHE   A 1 30  ? 12.09683  -18.66443 -2.86992  1.000 23.85145 ? 37  PHE   A CA  1 
ATOM   168  C C   . PHE   A 1 30  ? 11.22576  -17.42057 -2.74295  1.000 23.72164 ? 37  PHE   A C   1 
ATOM   169  O O   . PHE   A 1 30  ? 11.71491  -16.35736 -2.34532  1.000 22.75348 ? 37  PHE   A O   1 
ATOM   170  C CB  . PHE   A 1 30  ? 12.64913  -19.05354 -1.50690  1.000 20.17708 ? 37  PHE   A CB  1 
ATOM   171  C CG  . PHE   A 1 30  ? 11.57261  -19.33300 -0.50047  1.000 24.23818 ? 37  PHE   A CG  1 
ATOM   172  C CD1 . PHE   A 1 30  ? 10.80072  -20.47879 -0.59705  1.000 25.96699 ? 37  PHE   A CD1 1 
ATOM   173  C CD2 . PHE   A 1 30  ? 11.29094  -18.42625 0.50586   1.000 25.22541 ? 37  PHE   A CD2 1 
ATOM   174  C CE1 . PHE   A 1 30  ? 9.78932   -20.73656 0.31233   1.000 24.62321 ? 37  PHE   A CE1 1 
ATOM   175  C CE2 . PHE   A 1 30  ? 10.26870  -18.67332 1.41747   1.000 23.97677 ? 37  PHE   A CE2 1 
ATOM   176  C CZ  . PHE   A 1 30  ? 9.51060   -19.82804 1.31058   1.000 22.22857 ? 37  PHE   A CZ  1 
ATOM   177  N N   . TYR   A 1 31  ? 9.93038   -17.56906 -3.02500  1.000 17.40230 ? 38  TYR   A N   1 
ATOM   178  C CA  . TYR   A 1 31  ? 9.01988   -16.42685 -3.08146  1.000 17.44415 ? 38  TYR   A CA  1 
ATOM   179  C C   . TYR   A 1 31  ? 7.58467   -16.95840 -3.00412  1.000 17.02148 ? 38  TYR   A C   1 
ATOM   180  O O   . TYR   A 1 31  ? 7.07719   -17.54908 -3.96704  1.000 16.36719 ? 38  TYR   A O   1 
ATOM   181  C CB  . TYR   A 1 31  ? 9.27533   -15.61419 -4.35811  1.000 17.31879 ? 38  TYR   A CB  1 
ATOM   182  C CG  . TYR   A 1 31  ? 8.20878   -14.58924 -4.65886  1.000 21.93954 ? 38  TYR   A CG  1 
ATOM   183  C CD1 . TYR   A 1 31  ? 8.15141   -13.37452 -3.96562  1.000 23.71372 ? 38  TYR   A CD1 1 
ATOM   184  C CD2 . TYR   A 1 31  ? 7.25476   -14.84272 -5.62880  1.000 21.15659 ? 38  TYR   A CD2 1 
ATOM   185  C CE1 . TYR   A 1 31  ? 7.14385   -12.43782 -4.24292  1.000 25.37002 ? 38  TYR   A CE1 1 
ATOM   186  C CE2 . TYR   A 1 31  ? 6.26627   -13.93150 -5.91288  1.000 22.60918 ? 38  TYR   A CE2 1 
ATOM   187  C CZ  . TYR   A 1 31  ? 6.21931   -12.73532 -5.22923  1.000 22.48439 ? 38  TYR   A CZ  1 
ATOM   188  O OH  . TYR   A 1 31  ? 5.20997   -11.85567 -5.54884  1.000 28.66150 ? 38  TYR   A OH  1 
ATOM   189  N N   . SER   A 1 32  ? 6.93861   -16.75877 -1.85570  1.000 17.69716 ? 39  SER   A N   1 
ATOM   190  C CA  . SER   A 1 32  ? 5.65708   -17.40257 -1.58612  1.000 17.30695 ? 39  SER   A CA  1 
ATOM   191  C C   . SER   A 1 32  ? 4.46704   -16.74782 -2.28210  1.000 16.61700 ? 39  SER   A C   1 
ATOM   192  O O   . SER   A 1 32  ? 3.44565   -17.41605 -2.47446  1.000 20.64186 ? 39  SER   A O   1 
ATOM   193  C CB  . SER   A 1 32  ? 5.40355   -17.44229 -0.07975  1.000 18.54353 ? 39  SER   A CB  1 
ATOM   194  O OG  . SER   A 1 32  ? 6.40257   -18.21086 0.57256   1.000 19.23447 ? 39  SER   A OG  1 
ATOM   195  N N   . ASN   A 1 33  ? 4.57522   -15.48067 -2.68159  1.000 16.75244 ? 40  ASN   A N   1 
ATOM   196  C CA  . ASN   A 1 33  ? 3.43701   -14.70542 -3.19378  1.000 16.67477 ? 40  ASN   A CA  1 
ATOM   197  C C   . ASN   A 1 33  ? 3.24059   -14.95404 -4.69402  1.000 13.35667 ? 40  ASN   A C   1 
ATOM   198  O O   . ASN   A 1 33  ? 3.25418   -14.04731 -5.52343  1.000 16.10972 ? 40  ASN   A O   1 
ATOM   199  C CB  . ASN   A 1 33  ? 3.64033   -13.22542 -2.88208  1.000 19.63713 ? 40  ASN   A CB  1 
ATOM   200  C CG  . ASN   A 1 33  ? 2.46424   -12.35028 -3.31214  1.000 20.27406 ? 40  ASN   A CG  1 
ATOM   201  O OD1 . ASN   A 1 33  ? 1.30268   -12.75367 -3.24877  1.000 21.74027 ? 40  ASN   A OD1 1 
ATOM   202  N ND2 . ASN   A 1 33  ? 2.77324   -11.11770 -3.70475  1.000 23.09280 ? 40  ASN   A ND2 1 
ATOM   203  N N   . LYS   A 1 34  ? 3.09947   -16.24307 -5.03127  1.000 14.53354 ? 41  LYS   A N   1 
ATOM   204  C CA  . LYS   A 1 34  ? 3.00886   -16.67594 -6.42780  1.000 13.76929 ? 41  LYS   A CA  1 
ATOM   205  C C   . LYS   A 1 34  ? 1.74226   -16.20044 -7.13944  1.000 20.05517 ? 41  LYS   A C   1 
ATOM   206  O O   . LYS   A 1 34  ? 1.73642   -16.13216 -8.38062  1.000 13.90014 ? 41  LYS   A O   1 
ATOM   207  C CB  . LYS   A 1 34  ? 3.07775   -18.20412 -6.49567  1.000 13.90522 ? 41  LYS   A CB  1 
ATOM   208  C CG  . LYS   A 1 34  ? 4.45721   -18.77821 -6.17689  1.000 15.03195 ? 41  LYS   A CG  1 
ATOM   209  C CD  . LYS   A 1 34  ? 4.39031   -20.30894 -6.18675  1.000 17.18473 ? 41  LYS   A CD  1 
ATOM   210  C CE  . LYS   A 1 34  ? 5.73530   -20.96240 -5.88331  1.000 18.81541 ? 41  LYS   A CE  1 
ATOM   211  N NZ  . LYS   A 1 34  ? 6.68108   -20.79780 -7.00972  1.000 18.61766 ? 41  LYS   A NZ  1 
ATOM   212  N N   . GLU   A 1 35  ? 0.68308   -15.86780 -6.40028  1.000 16.73541 ? 42  GLU   A N   1 
ATOM   213  C CA  . GLU   A 1 35  ? -0.63020  -15.62948 -7.01194  1.000 15.13549 ? 42  GLU   A CA  1 
ATOM   214  C C   . GLU   A 1 35  ? -0.62262  -14.43839 -7.96441  1.000 14.98300 ? 42  GLU   A C   1 
ATOM   215  O O   . GLU   A 1 35  ? -1.54587  -14.29913 -8.77953  1.000 16.25861 ? 42  GLU   A O   1 
ATOM   216  C CB  . GLU   A 1 35  ? -1.68583  -15.41475 -5.92081  1.000 15.65230 ? 42  GLU   A CB  1 
ATOM   217  C CG  . GLU   A 1 35  ? -1.53025  -14.12266 -5.10906  1.000 15.71274 ? 42  GLU   A CG  1 
ATOM   218  C CD  . GLU   A 1 35  ? -2.50176  -14.01861 -3.94048  1.000 18.42950 ? 42  GLU   A CD  1 
ATOM   219  O OE1 . GLU   A 1 35  ? -2.68979  -14.99762 -3.20021  1.000 25.40600 ? 42  GLU   A OE1 1 
ATOM   220  O OE2 . GLU   A 1 35  ? -3.03744  -12.92152 -3.73415  1.000 27.65542 ? 42  GLU   A OE2 1 
ATOM   221  N N   . ILE   A 1 36  ? 0.38856   -13.56870 -7.87202  1.000 14.46199 ? 43  ILE   A N   1 
ATOM   222  C CA  . ILE   A 1 36  ? 0.43990   -12.39987 -8.74048  1.000 13.38907 ? 43  ILE   A CA  1 
ATOM   223  C C   . ILE   A 1 36  ? 0.59149   -12.77166 -10.20592 1.000 15.58694 ? 43  ILE   A C   1 
ATOM   224  O O   . ILE   A 1 36  ? 0.37185   -11.91184 -11.06816 1.000 13.14927 ? 43  ILE   A O   1 
ATOM   225  C CB  . ILE   A 1 36  ? 1.56526   -11.43177 -8.30322  1.000 17.52731 ? 43  ILE   A CB  1 
ATOM   226  C CG1 . ILE   A 1 36  ? 2.94703   -12.10311 -8.39108  1.000 18.26204 ? 43  ILE   A CG1 1 
ATOM   227  C CG2 . ILE   A 1 36  ? 1.33369   -10.92066 -6.88660  1.000 21.56049 ? 43  ILE   A CG2 1 
ATOM   228  C CD1 . ILE   A 1 36  ? 3.70454   -11.76168 -9.67260  1.000 19.60747 ? 43  ILE   A CD1 1 
ATOM   229  N N   . PHE   A 1 37  ? 0.93742   -14.02339 -10.53039 1.000 13.28199 ? 44  PHE   A N   1 
ATOM   230  C CA  . PHE   A 1 37  ? 1.03783   -14.37871 -11.94840 1.000 12.11730 ? 44  PHE   A CA  1 
ATOM   231  C C   . PHE   A 1 37  ? -0.26131  -14.04963 -12.66524 1.000 13.37195 ? 44  PHE   A C   1 
ATOM   232  O O   . PHE   A 1 37  ? -0.24601  -13.64047 -13.82974 1.000 11.86789 ? 44  PHE   A O   1 
ATOM   233  C CB  . PHE   A 1 37  ? 1.36930   -15.87769 -12.12477 1.000 13.28049 ? 44  PHE   A CB  1 
ATOM   234  C CG  . PHE   A 1 37  ? 0.15765   -16.77254 -11.96744 1.000 15.92255 ? 44  PHE   A CG  1 
ATOM   235  C CD1 . PHE   A 1 37  ? -0.22919  -17.21569 -10.71009 1.000 17.01161 ? 44  PHE   A CD1 1 
ATOM   236  C CD2 . PHE   A 1 37  ? -0.64061  -17.11572 -13.06709 1.000 13.15053 ? 44  PHE   A CD2 1 
ATOM   237  C CE1 . PHE   A 1 37  ? -1.36848  -17.99134 -10.54569 1.000 16.88552 ? 44  PHE   A CE1 1 
ATOM   238  C CE2 . PHE   A 1 37  ? -1.78759  -17.88659 -12.90231 1.000 15.17370 ? 44  PHE   A CE2 1 
ATOM   239  C CZ  . PHE   A 1 37  ? -2.14724  -18.33740 -11.64285 1.000 17.20048 ? 44  PHE   A CZ  1 
ATOM   240  N N   . LEU   A 1 38  ? -1.40394  -14.22472 -11.98566 1.000 13.30422 ? 45  LEU   A N   1 
ATOM   241  C CA  . LEU   A 1 38  ? -2.68297  -14.09514 -12.68591 1.000 14.56482 ? 45  LEU   A CA  1 
ATOM   242  C C   . LEU   A 1 38  ? -2.96013  -12.64898 -13.05821 1.000 12.29152 ? 45  LEU   A C   1 
ATOM   243  O O   . LEU   A 1 38  ? -3.41425  -12.37267 -14.17971 1.000 14.51498 ? 45  LEU   A O   1 
ATOM   244  C CB  . LEU   A 1 38  ? -3.83839  -14.64630 -11.85534 1.000 14.85097 ? 45  LEU   A CB  1 
ATOM   245  C CG  . LEU   A 1 38  ? -5.17228  -14.70914 -12.63020 1.000 14.40198 ? 45  LEU   A CG  1 
ATOM   246  C CD1 . LEU   A 1 38  ? -5.06842  -15.60567 -13.87400 1.000 15.54234 ? 45  LEU   A CD1 1 
ATOM   247  C CD2 . LEU   A 1 38  ? -6.25939  -15.21258 -11.70783 1.000 21.65843 ? 45  LEU   A CD2 1 
ATOM   248  N N   . ARG   A 1 39  ? -2.70099  -11.72542 -12.12397 1.000 13.99148 ? 46  ARG   A N   1 
ATOM   249  C CA  . ARG   A 1 39  ? -2.77886  -10.30042 -12.40848 1.000 13.74704 ? 46  ARG   A CA  1 
ATOM   250  C C   . ARG   A 1 39  ? -1.91463  -9.91646  -13.60778 1.000 17.37852 ? 46  ARG   A C   1 
ATOM   251  O O   . ARG   A 1 39  ? -2.30317  -9.06313  -14.42389 1.000 15.52392 ? 46  ARG   A O   1 
ATOM   252  C CB  . ARG   A 1 39  ? -2.34456  -9.51085  -11.16506 1.000 17.32778 ? 46  ARG   A CB  1 
ATOM   253  C CG  . ARG   A 1 39  ? -2.33083  -8.00523  -11.38859 1.000 27.28616 ? 46  ARG   A CG  1 
ATOM   254  C CD  . ARG   A 1 39  ? -1.49708  -7.24309  -10.34990 1.000 30.82187 ? 46  ARG   A CD  1 
ATOM   255  N NE  . ARG   A 1 39  ? -0.10656  -7.67113  -10.20942 1.000 28.87669 ? 46  ARG   A NE  1 
ATOM   256  C CZ  . ARG   A 1 39  ? 0.58811   -7.53699  -9.08344  1.000 28.99707 ? 46  ARG   A CZ  1 
ATOM   257  N NH1 . ARG   A 1 39  ? 0.04207   -7.02738  -7.99338  1.000 25.22153 ? 46  ARG   A NH1 1 
ATOM   258  N NH2 . ARG   A 1 39  ? 1.87323   -7.88629  -9.05827  1.000 33.45978 ? 46  ARG   A NH2 1 
ATOM   259  N N   . GLU   A 1 40  ? -0.72644  -10.52987 -13.72976 1.000 14.61215 ? 47  GLU   A N   1 
ATOM   260  C CA  . GLU   A 1 40  ? 0.19292   -10.12843 -14.78901 1.000 14.84666 ? 47  GLU   A CA  1 
ATOM   261  C C   . GLU   A 1 40  ? -0.31509  -10.58244 -16.15076 1.000 14.18603 ? 47  GLU   A C   1 
ATOM   262  O O   . GLU   A 1 40  ? -0.24032  -9.82641  -17.12620 1.000 14.35333 ? 47  GLU   A O   1 
ATOM   263  C CB  . GLU   A 1 40  ? 1.59767   -10.68295 -14.53022 1.000 13.08252 ? 47  GLU   A CB  1 
ATOM   264  C CG  . GLU   A 1 40  ? 2.24942   -10.13981 -13.27091 1.000 15.01183 ? 47  GLU   A CG  1 
ATOM   265  C CD  . GLU   A 1 40  ? 2.27511   -8.60323  -13.18449 1.000 15.85995 ? 47  GLU   A CD  1 
ATOM   266  O OE1 . GLU   A 1 40  ? 2.38607   -7.93344  -14.22245 1.000 19.56724 ? 47  GLU   A OE1 1 
ATOM   267  O OE2 . GLU   A 1 40  ? 2.23773   -8.04244  -12.05940 1.000 21.58249 ? 47  GLU   A OE2 1 
ATOM   268  N N   . LEU   A 1 41  ? -0.86479  -11.79838 -16.22615 1.000 15.11443 ? 48  LEU   A N   1 
ATOM   269  C CA  . LEU   A 1 41  ? -1.43098  -12.29032 -17.48503 1.000 14.83642 ? 48  LEU   A CA  1 
ATOM   270  C C   . LEU   A 1 41  ? -2.71303  -11.54199 -17.86438 1.000 14.52807 ? 48  LEU   A C   1 
ATOM   271  O O   . LEU   A 1 41  ? -2.92530  -11.23287 -19.04421 1.000 14.82507 ? 48  LEU   A O   1 
ATOM   272  C CB  . LEU   A 1 41  ? -1.68716  -13.79823 -17.39446 1.000 13.76163 ? 48  LEU   A CB  1 
ATOM   273  C CG  . LEU   A 1 41  ? -0.40115  -14.61870 -17.16857 1.000 10.79924 ? 48  LEU   A CG  1 
ATOM   274  C CD1 . LEU   A 1 41  ? -0.75962  -16.10136 -17.04296 1.000 12.33549 ? 48  LEU   A CD1 1 
ATOM   275  C CD2 . LEU   A 1 41  ? 0.63543   -14.38339 -18.25240 1.000 14.16585 ? 48  LEU   A CD2 1 
ATOM   276  N N   . ILE   A 1 42  ? -3.58494  -11.25553 -16.89023 1.000 14.65766 ? 49  ILE   A N   1 
ATOM   277  C CA  . ILE   A 1 42  ? -4.80457  -10.49100 -17.17794 1.000 11.70121 ? 49  ILE   A CA  1 
ATOM   278  C C   . ILE   A 1 42  ? -4.44884  -9.07634  -17.63306 1.000 15.65437 ? 49  ILE   A C   1 
ATOM   279  O O   . ILE   A 1 42  ? -5.07164  -8.53674  -18.55877 1.000 15.47536 ? 49  ILE   A O   1 
ATOM   280  C CB  . ILE   A 1 42  ? -5.73601  -10.48677 -15.94875 1.000 10.54670 ? 49  ILE   A CB  1 
ATOM   281  C CG1 . ILE   A 1 42  ? -6.31994  -11.89259 -15.72958 1.000 10.65316 ? 49  ILE   A CG1 1 
ATOM   282  C CG2 . ILE   A 1 42  ? -6.85116  -9.40113  -16.10144 1.000 16.40121 ? 49  ILE   A CG2 1 
ATOM   283  C CD1 . ILE   A 1 42  ? -7.17026  -11.99854 -14.47677 1.000 14.68001 ? 49  ILE   A CD1 1 
ATOM   284  N N   . SER   A 1 43  ? -3.42017  -8.47157  -17.01798 1.000 13.22801 ? 50  SER   A N   1 
ATOM   285  C CA  . SER   A 1 43  ? -2.96296  -7.14788  -17.43894 1.000 14.38587 ? 50  SER   A CA  1 
ATOM   286  C C   . SER   A 1 43  ? -2.46697  -7.18601  -18.87849 1.000 14.04179 ? 50  SER   A C   1 
ATOM   287  O O   . SER   A 1 43  ? -2.77580  -6.28985  -19.67405 1.000 14.74139 ? 50  SER   A O   1 
ATOM   288  C CB  . SER   A 1 43  ? -1.86883  -6.63467  -16.49976 1.000 16.09540 ? 50  SER   A CB  1 
ATOM   289  O OG  . SER   A 1 43  ? -1.27614  -5.42644  -16.97889 1.000 24.28181 ? 50  SER   A OG  1 
ATOM   290  N N   . ASN   A 1 44  ? -1.71536  -8.23327  -19.23714 1.000 14.68601 ? 51  ASN   A N   1 
ATOM   291  C CA  . ASN   A 1 44  ? -1.30305  -8.39916  -20.62717 1.000 15.47519 ? 51  ASN   A CA  1 
ATOM   292  C C   . ASN   A 1 44  ? -2.50604  -8.51572  -21.55256 1.000 13.87576 ? 51  ASN   A C   1 
ATOM   293  O O   . ASN   A 1 44  ? -2.52683  -7.90096  -22.62978 1.000 13.17655 ? 51  ASN   A O   1 
ATOM   294  C CB  . ASN   A 1 44  ? -0.40597  -9.62871  -20.77881 1.000 13.16000 ? 51  ASN   A CB  1 
ATOM   295  C CG  . ASN   A 1 44  ? 1.00986   -9.37796  -20.28604 1.000 15.42062 ? 51  ASN   A CG  1 
ATOM   296  O OD1 . ASN   A 1 44  ? 1.36113   -8.26094  -19.87255 1.000 15.57666 ? 51  ASN   A OD1 1 
ATOM   297  N ND2 . ASN   A 1 44  ? 1.84528   -10.41055 -20.36556 1.000 17.92637 ? 51  ASN   A ND2 1 
ATOM   298  N N   . SER   A 1 45  ? -3.50743  -9.30860  -21.15598 1.000 13.63145 ? 52  SER   A N   1 
ATOM   299  C CA  . SER   A 1 45  ? -4.71746  -9.45110  -21.96731 1.000 12.39276 ? 52  SER   A CA  1 
ATOM   300  C C   . SER   A 1 45  ? -5.40146  -8.10000  -22.14731 1.000 13.05197 ? 52  SER   A C   1 
ATOM   301  O O   . SER   A 1 45  ? -5.81449  -7.74240  -23.25771 1.000 15.04586 ? 52  SER   A O   1 
ATOM   302  C CB  . SER   A 1 45  ? -5.67132  -10.46471 -21.31622 1.000 12.22115 ? 52  SER   A CB  1 
ATOM   303  O OG  . SER   A 1 45  ? -5.15004  -11.79325 -21.40888 1.000 14.62128 ? 52  SER   A OG  1 
ATOM   304  N N   . SER   A 1 46  ? -5.51374  -7.32528  -21.05571 1.000 12.81973 ? 53  SER   A N   1 
ATOM   305  C CA  . SER   A 1 46  ? -6.18158  -6.02988  -21.12912 1.000 15.47654 ? 53  SER   A CA  1 
ATOM   306  C C   . SER   A 1 46  ? -5.43837  -5.10071  -22.07419 1.000 16.21787 ? 53  SER   A C   1 
ATOM   307  O O   . SER   A 1 46  ? -6.06120  -4.35590  -22.83740 1.000 17.51613 ? 53  SER   A O   1 
ATOM   308  C CB  . SER   A 1 46  ? -6.30389  -5.41448  -19.73350 1.000 18.93061 ? 53  SER   A CB  1 
ATOM   309  O OG  . SER   A 1 46  ? -6.87236  -4.10800  -19.76686 1.000 19.64117 ? 53  SER   A OG  1 
ATOM   310  N N   . ASP   A 1 47  ? -4.10276  -5.14677  -22.05386 1.000 17.19133 ? 54  ASP   A N   1 
ATOM   311  C CA  . ASP   A 1 47  ? -3.32271  -4.31556  -22.96999 1.000 15.48374 ? 54  ASP   A CA  1 
ATOM   312  C C   . ASP   A 1 47  ? -3.57188  -4.71417  -24.42338 1.000 16.26769 ? 54  ASP   A C   1 
ATOM   313  O O   . ASP   A 1 47  ? -3.70080  -3.85343  -25.30235 1.000 16.14236 ? 54  ASP   A O   1 
ATOM   314  C CB  . ASP   A 1 47  ? -1.83231  -4.44615  -22.64983 1.000 18.81338 ? 54  ASP   A CB  1 
ATOM   315  C CG  . ASP   A 1 47  ? -1.43003  -3.80208  -21.33175 1.000 21.85121 ? 54  ASP   A CG  1 
ATOM   316  O OD1 . ASP   A 1 47  ? -2.20092  -3.01851  -20.72162 1.000 20.29969 ? 54  ASP   A OD1 1 
ATOM   317  O OD2 . ASP   A 1 47  ? -0.28139  -4.03941  -20.92445 1.000 21.79290 ? 54  ASP   A OD2 1 
ATOM   318  N N   . ALA   A 1 48  ? -3.62808  -6.02269  -24.69432 1.000 13.48701 ? 55  ALA   A N   1 
ATOM   319  C CA  . ALA   A 1 48  ? -3.85035  -6.48967  -26.05898 1.000 13.33713 ? 55  ALA   A CA  1 
ATOM   320  C C   . ALA   A 1 48  ? -5.25007  -6.13580  -26.54283 1.000 14.66117 ? 55  ALA   A C   1 
ATOM   321  O O   . ALA   A 1 48  ? -5.44725  -5.86902  -27.73488 1.000 16.76028 ? 55  ALA   A O   1 
ATOM   322  C CB  . ALA   A 1 48  ? -3.61790  -8.00004  -26.11519 1.000 14.45589 ? 55  ALA   A CB  1 
ATOM   323  N N   . LEU   A 1 49  ? -6.22205  -6.10787  -25.62234 1.000 14.43538 ? 56  LEU   A N   1 
ATOM   324  C CA  . LEU   A 1 49  ? -7.58487  -5.71030  -25.96733 1.000 14.07897 ? 56  LEU   A CA  1 
ATOM   325  C C   . LEU   A 1 49  ? -7.65313  -4.21602  -26.24943 1.000 15.03322 ? 56  LEU   A C   1 
ATOM   326  O O   . LEU   A 1 49  ? -8.29616  -3.79595  -27.22442 1.000 15.75833 ? 56  LEU   A O   1 
ATOM   327  C CB  . LEU   A 1 49  ? -8.54708  -6.11824  -24.84647 1.000 13.68437 ? 56  LEU   A CB  1 
ATOM   328  C CG  . LEU   A 1 49  ? -8.81844  -7.63547  -24.79079 1.000 14.02696 ? 56  LEU   A CG  1 
ATOM   329  C CD1 . LEU   A 1 49  ? -9.30983  -8.00866  -23.41372 1.000 14.15460 ? 56  LEU   A CD1 1 
ATOM   330  C CD2 . LEU   A 1 49  ? -9.85336  -8.05800  -25.87483 1.000 15.49672 ? 56  LEU   A CD2 1 
ATOM   331  N N   . ASP   A 1 50  ? -6.96535  -3.41149  -25.42368 1.000 15.82764 ? 57  ASP   A N   1 
ATOM   332  C CA  . ASP   A 1 50  ? -6.85210  -1.97755  -25.68622 1.000 15.07165 ? 57  ASP   A CA  1 
ATOM   333  C C   . ASP   A 1 50  ? -6.31608  -1.72066  -27.08788 1.000 16.02996 ? 57  ASP   A C   1 
ATOM   334  O O   . ASP   A 1 50  ? -6.80644  -0.82868  -27.78402 1.000 19.13096 ? 57  ASP   A O   1 
ATOM   335  C CB  . ASP   A 1 50  ? -5.92992  -1.26693  -24.67869 1.000 16.15694 ? 57  ASP   A CB  1 
ATOM   336  C CG  . ASP   A 1 50  ? -6.52784  -1.13141  -23.28772 1.000 19.80874 ? 57  ASP   A CG  1 
ATOM   337  O OD1 . ASP   A 1 50  ? -7.74338  -1.33059  -23.10065 1.000 19.14831 ? 57  ASP   A OD1 1 
ATOM   338  O OD2 . ASP   A 1 50  ? -5.77916  -0.74854  -22.36983 1.000 20.73686 ? 57  ASP   A OD2 1 
ATOM   339  N N   . LYS   A 1 51  ? -5.30565  -2.48852  -27.50965 1.000 16.81422 ? 58  LYS   A N   1 
ATOM   340  C CA  . LYS   A 1 51  ? -4.66078  -2.24083  -28.79920 1.000 17.94021 ? 58  LYS   A CA  1 
ATOM   341  C C   . LYS   A 1 51  ? -5.61187  -2.48614  -29.96619 1.000 19.80721 ? 58  LYS   A C   1 
ATOM   342  O O   . LYS   A 1 51  ? -5.71983  -1.65194  -30.88248 1.000 17.53823 ? 58  LYS   A O   1 
ATOM   343  C CB  . LYS   A 1 51  ? -3.41471  -3.11920  -28.93348 1.000 17.29842 ? 58  LYS   A CB  1 
ATOM   344  C CG  . LYS   A 1 51  ? -2.25243  -2.67938  -28.03920 1.000 27.26576 ? 58  LYS   A CG  1 
ATOM   345  C CD  . LYS   A 1 51  ? -0.96260  -3.41089  -28.38224 1.000 31.60481 ? 58  LYS   A CD  1 
ATOM   346  C CE  . LYS   A 1 51  ? 0.04018   -3.33759  -27.24362 1.000 34.41752 ? 58  LYS   A CE  1 
ATOM   347  N NZ  . LYS   A 1 51  ? 0.81538   -4.59653  -27.09533 1.000 36.80587 ? 58  LYS   A NZ  1 
ATOM   348  N N   . ILE   A 1 52  ? -6.28780  -3.64113  -29.97722 1.000 17.77348 ? 59  ILE   A N   1 
ATOM   349  C CA  . ILE   A 1 52  ? -7.19307  -3.91968  -31.08915 1.000 19.76373 ? 59  ILE   A CA  1 
ATOM   350  C C   . ILE   A 1 52  ? -8.38037  -2.96006  -31.06324 1.000 21.92434 ? 59  ILE   A C   1 
ATOM   351  O O   . ILE   A 1 52  ? -8.85090  -2.50896  -32.11507 1.000 17.65916 ? 59  ILE   A O   1 
ATOM   352  C CB  . ILE   A 1 52  ? -7.62301  -5.40728  -31.07812 1.000 20.03215 ? 59  ILE   A CB  1 
ATOM   353  C CG1 . ILE   A 1 52  ? -8.39254  -5.74323  -32.36180 1.000 21.47266 ? 59  ILE   A CG1 1 
ATOM   354  C CG2 . ILE   A 1 52  ? -8.47859  -5.74005  -29.85791 1.000 16.78084 ? 59  ILE   A CG2 1 
ATOM   355  C CD1 . ILE   A 1 52  ? -7.52834  -5.65318  -33.64466 1.000 21.85309 ? 59  ILE   A CD1 1 
ATOM   356  N N   . ARG   A 1 53  ? -8.85617  -2.59147  -29.87388 1.000 18.42542 ? 60  ARG   A N   1 
ATOM   357  C CA  . ARG   A 1 53  ? -9.92380  -1.60280  -29.80006 1.000 18.07941 ? 60  ARG   A CA  1 
ATOM   358  C C   . ARG   A 1 53  ? -9.48122  -0.27758  -30.40927 1.000 18.01358 ? 60  ARG   A C   1 
ATOM   359  O O   . ARG   A 1 53  ? -10.20237 0.31145   -31.21669 1.000 21.59303 ? 60  ARG   A O   1 
ATOM   360  C CB  . ARG   A 1 53  ? -10.36732 -1.40372  -28.34895 1.000 19.82980 ? 60  ARG   A CB  1 
ATOM   361  C CG  . ARG   A 1 53  ? -11.48924 -0.39545  -28.22509 1.000 26.45068 ? 60  ARG   A CG  1 
ATOM   362  C CD  . ARG   A 1 53  ? -12.08397 -0.37549  -26.83952 1.000 28.46270 ? 60  ARG   A CD  1 
ATOM   363  N NE  . ARG   A 1 53  ? -11.18884 0.28738   -25.90129 1.000 34.34309 ? 60  ARG   A NE  1 
ATOM   364  C CZ  . ARG   A 1 53  ? -11.34533 0.27591   -24.58561 1.000 34.60390 ? 60  ARG   A CZ  1 
ATOM   365  N NH1 . ARG   A 1 53  ? -12.36243 -0.35479  -24.01714 1.000 35.33116 ? 60  ARG   A NH1 1 
ATOM   366  N NH2 . ARG   A 1 53  ? -10.45028 0.89807   -23.82216 1.000 32.96210 ? 60  ARG   A NH2 1 
ATOM   367  N N   . TYR   A 1 54  ? -8.28046  0.19753   -30.05693 1.000 17.85253 ? 61  TYR   A N   1 
ATOM   368  C CA  . TYR   A 1 54  ? -7.81910  1.47705   -30.59714 1.000 21.74743 ? 61  TYR   A CA  1 
ATOM   369  C C   . TYR   A 1 54  ? -7.66385  1.40599   -32.11855 1.000 24.75987 ? 61  TYR   A C   1 
ATOM   370  O O   . TYR   A 1 54  ? -8.10513  2.30687   -32.84402 1.000 24.32727 ? 61  TYR   A O   1 
ATOM   371  C CB  . TYR   A 1 54  ? -6.50887  1.90335   -29.92575 1.000 19.42775 ? 61  TYR   A CB  1 
ATOM   372  C CG  . TYR   A 1 54  ? -5.83360  3.08691   -30.60149 1.000 24.97177 ? 61  TYR   A CG  1 
ATOM   373  C CD1 . TYR   A 1 54  ? -6.19281  4.38419   -30.28492 1.000 23.73034 ? 61  TYR   A CD1 1 
ATOM   374  C CD2 . TYR   A 1 54  ? -4.83867  2.90036   -31.55313 1.000 24.91041 ? 61  TYR   A CD2 1 
ATOM   375  C CE1 . TYR   A 1 54  ? -5.58293  5.46882   -30.90173 1.000 24.62721 ? 61  TYR   A CE1 1 
ATOM   376  C CE2 . TYR   A 1 54  ? -4.22056  3.97930   -32.18117 1.000 31.66299 ? 61  TYR   A CE2 1 
ATOM   377  C CZ  . TYR   A 1 54  ? -4.59756  5.26394   -31.85342 1.000 29.02223 ? 61  TYR   A CZ  1 
ATOM   378  O OH  . TYR   A 1 54  ? -3.98760  6.34865   -32.47451 1.000 32.00758 ? 61  TYR   A OH  1 
ATOM   379  N N   . GLU   A 1 55  ? -7.05221  0.32904   -32.62228 1.000 21.11668 ? 62  GLU   A N   1 
ATOM   380  C CA  . GLU   A 1 55  ? -6.84756  0.20720   -34.06410 1.000 21.19186 ? 62  GLU   A CA  1 
ATOM   381  C C   . GLU   A 1 55  ? -8.17791  0.15556   -34.81030 1.000 23.10351 ? 62  GLU   A C   1 
ATOM   382  O O   . GLU   A 1 55  ? -8.30907  0.70938   -35.91187 1.000 23.26770 ? 62  GLU   A O   1 
ATOM   383  C CB  . GLU   A 1 55  ? -6.00757  -1.03941  -34.35679 1.000 23.62625 ? 62  GLU   A CB  1 
ATOM   384  C CG  . GLU   A 1 55  ? -4.51405  -0.85867  -34.12715 1.000 29.31276 ? 62  GLU   A CG  1 
ATOM   385  C CD  . GLU   A 1 55  ? -3.69506  -2.03026  -34.63063 1.000 32.05273 ? 62  GLU   A CD  1 
ATOM   386  O OE1 . GLU   A 1 55  ? -4.26786  -2.93390  -35.27411 1.000 34.28070 ? 62  GLU   A OE1 1 
ATOM   387  O OE2 . GLU   A 1 55  ? -2.47206  -2.04369  -34.39038 1.000 39.02334 ? 62  GLU   A OE2 1 
ATOM   388  N N   . SER   A 1 56  ? -9.18349  -0.49609  -34.22179 1.000 20.06924 ? 63  SER   A N   1 
ATOM   389  C CA  . SER   A 1 56  ? -10.48087 -0.62204  -34.87868 1.000 23.29924 ? 63  SER   A CA  1 
ATOM   390  C C   . SER   A 1 56  ? -11.19836 0.71589   -35.01833 1.000 28.13542 ? 63  SER   A C   1 
ATOM   391  O O   . SER   A 1 56  ? -12.05635 0.85222   -35.89932 1.000 30.92855 ? 63  SER   A O   1 
ATOM   392  C CB  . SER   A 1 56  ? -11.36295 -1.61566  -34.11271 1.000 23.95612 ? 63  SER   A CB  1 
ATOM   393  O OG  . SER   A 1 56  ? -11.94088 -1.03068  -32.95500 1.000 31.03790 ? 63  SER   A OG  1 
ATOM   394  N N   . LEU   A 1 57  ? -10.86750 1.71047   -34.18627 1.000 29.71542 ? 64  LEU   A N   1 
ATOM   395  C CA  . LEU   A 1 57  ? -11.53535 3.00749   -34.29983 1.000 33.57545 ? 64  LEU   A CA  1 
ATOM   396  C C   . LEU   A 1 57  ? -11.32358 3.62220   -35.67444 1.000 36.43512 ? 64  LEU   A C   1 
ATOM   397  O O   . LEU   A 1 57  ? -12.23988 4.24015   -36.24004 1.000 34.10629 ? 64  LEU   A O   1 
ATOM   398  C CB  . LEU   A 1 57  ? -11.03130 3.96608   -33.22176 1.000 31.38729 ? 64  LEU   A CB  1 
ATOM   399  C CG  . LEU   A 1 57  ? -11.58447 3.80558   -31.80979 1.000 36.40015 ? 64  LEU   A CG  1 
ATOM   400  C CD1 . LEU   A 1 57  ? -11.37824 5.12077   -31.07070 1.000 39.13458 ? 64  LEU   A CD1 1 
ATOM   401  C CD2 . LEU   A 1 57  ? -13.05403 3.42076   -31.84189 1.000 43.96506 ? 64  LEU   A CD2 1 
ATOM   402  N N   . THR   A 1 58  ? -10.12093 3.48223   -36.22562 1.000 29.56862 ? 65  THR   A N   1 
ATOM   403  C CA  . THR   A 1 58  ? -9.83913  4.03839   -37.53585 1.000 37.16767 ? 65  THR   A CA  1 
ATOM   404  C C   . THR   A 1 58  ? -9.79181  2.99772   -38.63591 1.000 37.74288 ? 65  THR   A C   1 
ATOM   405  O O   . THR   A 1 58  ? -9.49572  3.33345   -39.78291 1.000 38.29474 ? 65  THR   A O   1 
ATOM   406  C CB  . THR   A 1 58  ? -8.52742  4.82784   -37.49938 1.000 36.45315 ? 65  THR   A CB  1 
ATOM   407  O OG1 . THR   A 1 58  ? -7.43110  3.91562   -37.35799 1.000 36.54301 ? 65  THR   A OG1 1 
ATOM   408  C CG2 . THR   A 1 58  ? -8.54026  5.83167   -36.35289 1.000 41.43363 ? 65  THR   A CG2 1 
ATOM   409  N N   . ASP   A 1 59  ? -10.11643 1.72668   -38.32614 1.000 30.48325 ? 66  ASP   A N   1 
ATOM   410  C CA  . ASP   A 1 59  ? -10.27720 0.70437   -39.34888 1.000 34.25896 ? 66  ASP   A CA  1 
ATOM   411  C C   . ASP   A 1 59  ? -11.19969 -0.37007  -38.77737 1.000 33.47687 ? 66  ASP   A C   1 
ATOM   412  O O   . ASP   A 1 59  ? -10.74638 -1.33176  -38.14959 1.000 32.11795 ? 66  ASP   A O   1 
ATOM   413  C CB  . ASP   A 1 59  ? -8.92946  0.10838   -39.76674 1.000 34.69408 ? 66  ASP   A CB  1 
ATOM   414  C CG  . ASP   A 1 59  ? -9.05737  -0.97391  -40.83850 1.000 35.62403 ? 66  ASP   A CG  1 
ATOM   415  O OD1 . ASP   A 1 59  ? -10.18654 -1.30904  -41.24613 1.000 41.65921 ? 66  ASP   A OD1 1 
ATOM   416  O OD2 . ASP   A 1 59  ? -8.01024  -1.48199  -41.28768 1.000 42.13471 ? 66  ASP   A OD2 1 
ATOM   417  N N   . PRO   A 1 60  ? -12.51593 -0.20504  -38.96296 1.000 34.23880 ? 67  PRO   A N   1 
ATOM   418  C CA  . PRO   A 1 60  ? -13.46649 -1.19297  -38.40682 1.000 37.26418 ? 67  PRO   A CA  1 
ATOM   419  C C   . PRO   A 1 60  ? -13.23363 -2.61616  -38.88140 1.000 33.59889 ? 67  PRO   A C   1 
ATOM   420  O O   . PRO   A 1 60  ? -13.59208 -3.55793  -38.16529 1.000 29.53926 ? 67  PRO   A O   1 
ATOM   421  C CB  . PRO   A 1 60  ? -14.83170 -0.68045  -38.88735 1.000 35.45202 ? 67  PRO   A CB  1 
ATOM   422  C CG  . PRO   A 1 60  ? -14.63899 0.71237   -39.33566 1.000 39.46579 ? 67  PRO   A CG  1 
ATOM   423  C CD  . PRO   A 1 60  ? -13.17441 1.06182   -39.31178 1.000 30.72468 ? 67  PRO   A CD  1 
ATOM   424  N N   . SER   A 1 61  ? -12.68192 -2.81207  -40.08404 1.000 33.45339 ? 68  SER   A N   1 
ATOM   425  C CA  . SER   A 1 61  ? -12.46203 -4.17011  -40.57794 1.000 28.77381 ? 68  SER   A CA  1 
ATOM   426  C C   . SER   A 1 61  ? -11.52656 -4.99080  -39.68817 1.000 31.81119 ? 68  SER   A C   1 
ATOM   427  O O   . SER   A 1 61  ? -11.52833 -6.22110  -39.78499 1.000 30.41079 ? 68  SER   A O   1 
ATOM   428  C CB  . SER   A 1 61  ? -11.93278 -4.12162  -42.01397 1.000 32.56413 ? 68  SER   A CB  1 
ATOM   429  O OG  . SER   A 1 61  ? -10.52637 -3.95750  -42.05796 1.000 36.18285 ? 68  SER   A OG  1 
ATOM   430  N N   . LYS   A 1 62  ? -10.74865 -4.35817  -38.80886 1.000 26.91842 ? 69  LYS   A N   1 
ATOM   431  C CA  . LYS   A 1 62  ? -9.88273  -5.12992  -37.92153 1.000 25.92407 ? 69  LYS   A CA  1 
ATOM   432  C C   . LYS   A 1 62  ? -10.66855 -6.00692  -36.95164 1.000 21.66591 ? 69  LYS   A C   1 
ATOM   433  O O   . LYS   A 1 62  ? -10.09057 -6.91791  -36.34838 1.000 26.13714 ? 69  LYS   A O   1 
ATOM   434  C CB  . LYS   A 1 62  ? -8.95515  -4.19481  -37.14902 1.000 30.63485 ? 69  LYS   A CB  1 
ATOM   435  C CG  . LYS   A 1 62  ? -8.12345  -3.28590  -38.03856 1.000 33.03795 ? 69  LYS   A CG  1 
ATOM   436  C CD  . LYS   A 1 62  ? -6.71229  -3.17508  -37.52117 1.000 28.16504 ? 69  LYS   A CD  1 
ATOM   437  C CE  . LYS   A 1 62  ? -5.76768  -2.69008  -38.58713 1.000 32.51785 ? 69  LYS   A CE  1 
ATOM   438  N NZ  . LYS   A 1 62  ? -4.36110  -2.75450  -38.10878 1.000 38.42961 ? 69  LYS   A NZ  1 
ATOM   439  N N   . LEU   A 1 63  ? -11.96356 -5.74713  -36.77385 1.000 27.52069 ? 70  LEU   A N   1 
ATOM   440  C CA  . LEU   A 1 63  ? -12.81309 -6.57019  -35.92586 1.000 27.40858 ? 70  LEU   A CA  1 
ATOM   441  C C   . LEU   A 1 63  ? -13.60131 -7.60293  -36.72296 1.000 28.26336 ? 70  LEU   A C   1 
ATOM   442  O O   . LEU   A 1 63  ? -14.49670 -8.24646  -36.16450 1.000 29.34205 ? 70  LEU   A O   1 
ATOM   443  C CB  . LEU   A 1 63  ? -13.76900 -5.68836  -35.12106 1.000 22.55732 ? 70  LEU   A CB  1 
ATOM   444  C CG  . LEU   A 1 63  ? -13.15153 -4.80611  -34.03576 1.000 30.72839 ? 70  LEU   A CG  1 
ATOM   445  C CD1 . LEU   A 1 63  ? -14.24939 -3.99549  -33.33326 1.000 35.74900 ? 70  LEU   A CD1 1 
ATOM   446  C CD2 . LEU   A 1 63  ? -12.31488 -5.61372  -33.03989 1.000 24.71678 ? 70  LEU   A CD2 1 
ATOM   447  N N   . ASP   A 1 64  ? -13.29800 -7.77084  -38.01539 1.000 25.96717 ? 71  ASP   A N   1 
ATOM   448  C CA  . ASP   A 1 64  ? -13.94222 -8.82681  -38.78909 1.000 28.41779 ? 71  ASP   A CA  1 
ATOM   449  C C   . ASP   A 1 64  ? -13.61382 -10.20014 -38.23357 1.000 28.02066 ? 71  ASP   A C   1 
ATOM   450  O O   . ASP   A 1 64  ? -14.37498 -11.14879 -38.44122 1.000 31.75054 ? 71  ASP   A O   1 
ATOM   451  C CB  . ASP   A 1 64  ? -13.51910 -8.76043  -40.25808 1.000 31.60895 ? 71  ASP   A CB  1 
ATOM   452  C CG  . ASP   A 1 64  ? -14.09486 -7.56200  -40.98445 1.000 30.58657 ? 71  ASP   A CG  1 
ATOM   453  O OD1 . ASP   A 1 64  ? -14.99606 -6.89066  -40.43056 1.000 38.24239 ? 71  ASP   A OD1 1 
ATOM   454  O OD2 . ASP   A 1 64  ? -13.64573 -7.30114  -42.12155 1.000 33.98672 ? 71  ASP   A OD2 1 
ATOM   455  N N   . SER   A 1 65  ? -12.50525 -10.31439 -37.50847 1.000 28.57211 ? 72  SER   A N   1 
ATOM   456  C CA  . SER   A 1 65  ? -12.09789 -11.55388 -36.86843 1.000 27.96242 ? 72  SER   A CA  1 
ATOM   457  C C   . SER   A 1 65  ? -12.73304 -11.73998 -35.49933 1.000 31.28365 ? 72  SER   A C   1 
ATOM   458  O O   . SER   A 1 65  ? -12.32402 -12.64670 -34.76665 1.000 28.51802 ? 72  SER   A O   1 
ATOM   459  C CB  . SER   A 1 65  ? -10.57345 -11.59334 -36.75194 1.000 26.34102 ? 72  SER   A CB  1 
ATOM   460  O OG  . SER   A 1 65  ? -10.06804 -10.36840 -36.23704 1.000 24.54414 ? 72  SER   A OG  1 
ATOM   461  N N   . GLY   A 1 66  ? -13.70894 -10.90353 -35.13842 1.000 26.59153 ? 73  GLY   A N   1 
ATOM   462  C CA  . GLY   A 1 66  ? -14.37819 -11.00922 -33.85549 1.000 28.20954 ? 73  GLY   A CA  1 
ATOM   463  C C   . GLY   A 1 66  ? -14.61779 -9.66914  -33.18949 1.000 25.57842 ? 73  GLY   A C   1 
ATOM   464  O O   . GLY   A 1 66  ? -13.66819 -8.94340  -32.87399 1.000 25.48614 ? 73  GLY   A O   1 
ATOM   465  N N   . LYS   A 1 67  ? -15.88937 -9.33350  -32.95821 1.000 23.98182 ? 74  LYS   A N   1 
ATOM   466  C CA  . LYS   A 1 67  ? -16.21502 -8.04893  -32.35056 1.000 27.39290 ? 74  LYS   A CA  1 
ATOM   467  C C   . LYS   A 1 67  ? -16.08019 -8.06682  -30.83343 1.000 25.47501 ? 74  LYS   A C   1 
ATOM   468  O O   . LYS   A 1 67  ? -15.84633 -7.01164  -30.23448 1.000 27.13967 ? 74  LYS   A O   1 
ATOM   469  C CB  . LYS   A 1 67  ? -17.63648 -7.63543  -32.72911 1.000 29.63823 ? 74  LYS   A CB  1 
ATOM   470  C CG  . LYS   A 1 67  ? -17.79541 -7.21164  -34.17935 1.000 39.53875 ? 74  LYS   A CG  1 
ATOM   471  C CD  . LYS   A 1 67  ? -19.22018 -6.75834  -34.46902 1.000 43.38421 ? 74  LYS   A CD  1 
ATOM   472  C CE  . LYS   A 1 67  ? -19.25173 -5.78222  -35.63215 1.000 47.91757 ? 74  LYS   A CE  1 
ATOM   473  N NZ  . LYS   A 1 67  ? -19.00786 -6.47882  -36.92067 1.000 49.14222 ? 74  LYS   A NZ  1 
ATOM   474  N N   . GLU   A 1 68  ? -16.22831 -9.23165  -30.19844 1.000 22.16034 ? 75  GLU   A N   1 
ATOM   475  C CA  . GLU   A 1 68  ? -16.25605 -9.29687  -28.73909 1.000 26.43859 ? 75  GLU   A CA  1 
ATOM   476  C C   . GLU   A 1 68  ? -14.86523 -9.09735  -28.15093 1.000 20.47434 ? 75  GLU   A C   1 
ATOM   477  O O   . GLU   A 1 68  ? -13.88145 -9.67261  -28.62176 1.000 22.05865 ? 75  GLU   A O   1 
ATOM   478  C CB  . GLU   A 1 68  ? -16.82733 -10.64046 -28.26171 1.000 21.90938 ? 75  GLU   A CB  1 
ATOM   479  C CG  . GLU   A 1 68  ? -18.30137 -10.86518 -28.60180 1.000 32.15769 ? 75  GLU   A CG  1 
ATOM   480  C CD  . GLU   A 1 68  ? -18.54600 -11.05313 -30.08502 1.000 44.43694 ? 75  GLU   A CD  1 
ATOM   481  O OE1 . GLU   A 1 68  ? -17.61737 -11.50207 -30.79681 1.000 46.23114 ? 75  GLU   A OE1 1 
ATOM   482  O OE2 . GLU   A 1 68  ? -19.66977 -10.75841 -30.54274 1.000 52.47806 ? 75  GLU   A OE2 1 
ATOM   483  N N   . LEU   A 1 69  ? -14.77914 -8.26198  -27.12385 1.000 17.93698 ? 76  LEU   A N   1 
ATOM   484  C CA  . LEU   A 1 69  ? -13.51305 -7.95984  -26.45750 1.000 18.34923 ? 76  LEU   A CA  1 
ATOM   485  C C   . LEU   A 1 69  ? -13.64588 -8.43681  -25.01335 1.000 20.71756 ? 76  LEU   A C   1 
ATOM   486  O O   . LEU   A 1 69  ? -14.31974 -7.80366  -24.19272 1.000 17.61505 ? 76  LEU   A O   1 
ATOM   487  C CB  . LEU   A 1 69  ? -13.21697 -6.46667  -26.55381 1.000 18.18993 ? 76  LEU   A CB  1 
ATOM   488  C CG  . LEU   A 1 69  ? -13.10847 -5.84526  -27.95559 1.000 21.55342 ? 76  LEU   A CG  1 
ATOM   489  C CD1 . LEU   A 1 69  ? -12.69907 -4.36726  -27.88872 1.000 22.28225 ? 76  LEU   A CD1 1 
ATOM   490  C CD2 . LEU   A 1 69  ? -12.12300 -6.62188  -28.80231 1.000 17.61967 ? 76  LEU   A CD2 1 
ATOM   491  N N   . HIS   A 1 70  ? -13.02490 -9.56317  -24.68859 1.000 15.35892 ? 77  HIS   A N   1 
ATOM   492  C CA  . HIS   A 1 70  ? -13.26284 -10.15020 -23.37968 1.000 15.59655 ? 77  HIS   A CA  1 
ATOM   493  C C   . HIS   A 1 70  ? -12.07560 -11.00356 -22.97438 1.000 15.64819 ? 77  HIS   A C   1 
ATOM   494  O O   . HIS   A 1 70  ? -11.16958 -11.27559 -23.77132 1.000 14.15877 ? 77  HIS   A O   1 
ATOM   495  C CB  . HIS   A 1 70  ? -14.55004 -10.98143 -23.36245 1.000 18.32026 ? 77  HIS   A CB  1 
ATOM   496  C CG  . HIS   A 1 70  ? -14.53768 -12.14400 -24.31893 1.000 19.62329 ? 77  HIS   A CG  1 
ATOM   497  N ND1 . HIS   A 1 70  ? -15.39902 -12.23149 -25.39236 1.000 27.23456 ? 77  HIS   A ND1 1 
ATOM   498  C CD2 . HIS   A 1 70  ? -13.76041 -13.25176 -24.37518 1.000 20.68573 ? 77  HIS   A CD2 1 
ATOM   499  C CE1 . HIS   A 1 70  ? -15.16283 -13.34840 -26.05776 1.000 21.05589 ? 77  HIS   A CE1 1 
ATOM   500  N NE2 . HIS   A 1 70  ? -14.17993 -13.98954 -25.45740 1.000 20.73009 ? 77  HIS   A NE2 1 
ATOM   501  N N   . ILE   A 1 71  ? -12.13433 -11.45541 -21.72494 1.000 14.41113 ? 78  ILE   A N   1 
ATOM   502  C CA  . ILE   A 1 71  ? -11.15300 -12.34709 -21.12663 1.000 13.98420 ? 78  ILE   A CA  1 
ATOM   503  C C   . ILE   A 1 71  ? -11.89745 -13.50194 -20.46661 1.000 15.19838 ? 78  ILE   A C   1 
ATOM   504  O O   . ILE   A 1 71  ? -12.81747 -13.27596 -19.66761 1.000 15.67396 ? 78  ILE   A O   1 
ATOM   505  C CB  . ILE   A 1 71  ? -10.29890 -11.62132 -20.07497 1.000 14.77141 ? 78  ILE   A CB  1 
ATOM   506  C CG1 . ILE   A 1 71  ? -9.58256  -10.40977 -20.69420 1.000 13.83699 ? 78  ILE   A CG1 1 
ATOM   507  C CG2 . ILE   A 1 71  ? -9.33542  -12.61545 -19.41668 1.000 15.92250 ? 78  ILE   A CG2 1 
ATOM   508  C CD1 . ILE   A 1 71  ? -8.93399  -9.46834  -19.64799 1.000 15.51403 ? 78  ILE   A CD1 1 
ATOM   509  N N   . ASN   A 1 72  ? -11.48184 -14.73434 -20.77462 1.000 15.84865 ? 79  ASN   A N   1 
ATOM   510  C CA  . ASN   A 1 72  ? -12.03106 -15.93993 -20.16707 1.000 13.87023 ? 79  ASN   A CA  1 
ATOM   511  C C   . ASN   A 1 72  ? -10.94718 -16.64247 -19.36989 1.000 12.88628 ? 79  ASN   A C   1 
ATOM   512  O O   . ASN   A 1 72  ? -9.78903  -16.71887 -19.81477 1.000 14.15377 ? 79  ASN   A O   1 
ATOM   513  C CB  . ASN   A 1 72  ? -12.59525 -16.91074 -21.22817 1.000 13.54836 ? 79  ASN   A CB  1 
ATOM   514  C CG  . ASN   A 1 72  ? -13.79158 -16.34656 -21.93811 1.000 13.45666 ? 79  ASN   A CG  1 
ATOM   515  O OD1 . ASN   A 1 72  ? -14.52545 -15.53333 -21.37793 1.000 14.52742 ? 79  ASN   A OD1 1 
ATOM   516  N ND2 . ASN   A 1 72  ? -14.02499 -16.80189 -23.16240 1.000 16.33813 ? 79  ASN   A ND2 1 
ATOM   517  N N   . LEU   A 1 73  ? -11.29952 -17.10314 -18.17654 1.000 12.88251 ? 80  LEU   A N   1 
ATOM   518  C CA  . LEU   A 1 73  ? -10.41228 -17.90459 -17.34036 1.000 12.94827 ? 80  LEU   A CA  1 
ATOM   519  C C   . LEU   A 1 73  ? -10.98209 -19.30977 -17.25038 1.000 16.24446 ? 80  LEU   A C   1 
ATOM   520  O O   . LEU   A 1 73  ? -12.11737 -19.49238 -16.79079 1.000 15.06957 ? 80  LEU   A O   1 
ATOM   521  C CB  . LEU   A 1 73  ? -10.27470 -17.30138 -15.93775 1.000 13.78388 ? 80  LEU   A CB  1 
ATOM   522  C CG  . LEU   A 1 73  ? -9.91201  -15.81480 -15.86758 1.000 11.44302 ? 80  LEU   A CG  1 
ATOM   523  C CD1 . LEU   A 1 73  ? -9.89207  -15.33991 -14.40846 1.000 12.69290 ? 80  LEU   A CD1 1 
ATOM   524  C CD2 . LEU   A 1 73  ? -8.56713  -15.55177 -16.55188 1.000 14.53749 ? 80  LEU   A CD2 1 
ATOM   525  N N   . ILE   A 1 74  ? -10.21008 -20.29977 -17.69006 1.000 14.24125 ? 81  ILE   A N   1 
ATOM   526  C CA  . ILE   A 1 74  ? -10.74340 -21.64939 -17.87335 1.000 15.90241 ? 81  ILE   A CA  1 
ATOM   527  C C   . ILE   A 1 74  ? -9.87911  -22.65275 -17.13068 1.000 17.15412 ? 81  ILE   A C   1 
ATOM   528  O O   . ILE   A 1 74  ? -8.80430  -23.03619 -17.62361 1.000 16.50738 ? 81  ILE   A O   1 
ATOM   529  C CB  . ILE   A 1 74  ? -10.84314 -22.02175 -19.36081 1.000 14.87087 ? 81  ILE   A CB  1 
ATOM   530  C CG1 . ILE   A 1 74  ? -11.55667 -20.92429 -20.15022 1.000 18.30816 ? 81  ILE   A CG1 1 
ATOM   531  C CG2 . ILE   A 1 74  ? -11.47062 -23.40984 -19.53214 1.000 19.25334 ? 81  ILE   A CG2 1 
ATOM   532  C CD1 . ILE   A 1 74  ? -11.67430 -21.20911 -21.63407 1.000 20.23523 ? 81  ILE   A CD1 1 
ATOM   533  N N   . PRO   A 1 75  ? -10.31784 -23.12889 -15.96965 1.000 20.33701 ? 82  PRO   A N   1 
ATOM   534  C CA  . PRO   A 1 75  ? -9.59679  -24.20422 -15.28862 1.000 23.68032 ? 82  PRO   A CA  1 
ATOM   535  C C   . PRO   A 1 75  ? -10.03906 -25.57801 -15.77138 1.000 21.79849 ? 82  PRO   A C   1 
ATOM   536  O O   . PRO   A 1 75  ? -11.19163 -25.81012 -16.15576 1.000 23.95345 ? 82  PRO   A O   1 
ATOM   537  C CB  . PRO   A 1 75  ? -9.97551  -23.99974 -13.81580 1.000 23.36474 ? 82  PRO   A CB  1 
ATOM   538  C CG  . PRO   A 1 75  ? -11.39227 -23.40259 -13.89613 1.000 21.81694 ? 82  PRO   A CG  1 
ATOM   539  C CD  . PRO   A 1 75  ? -11.49729 -22.66083 -15.21411 1.000 20.04437 ? 82  PRO   A CD  1 
ATOM   540  N N   . ASN   A 1 76  ? -9.09035  -26.51361 -15.74939 1.000 20.28634 ? 83  ASN   A N   1 
ATOM   541  C CA  . ASN   A 1 76  ? -9.37645  -27.89193 -16.14282 1.000 21.40837 ? 83  ASN   A CA  1 
ATOM   542  C C   . ASN   A 1 76  ? -8.55457  -28.82837 -15.25849 1.000 26.25436 ? 83  ASN   A C   1 
ATOM   543  O O   . ASN   A 1 76  ? -7.35838  -29.01538 -15.49710 1.000 23.09954 ? 83  ASN   A O   1 
ATOM   544  C CB  . ASN   A 1 76  ? -9.07662  -28.10402 -17.62452 1.000 25.96059 ? 83  ASN   A CB  1 
ATOM   545  C CG  . ASN   A 1 76  ? -9.48324  -29.48466 -18.10953 1.000 27.10281 ? 83  ASN   A CG  1 
ATOM   546  O OD1 . ASN   A 1 76  ? -9.21296  -30.49482 -17.45814 1.000 27.98508 ? 83  ASN   A OD1 1 
ATOM   547  N ND2 . ASN   A 1 76  ? -10.18110 -29.52799 -19.24178 1.000 34.91162 ? 83  ASN   A ND2 1 
ATOM   548  N N   . LYS   A 1 77  ? -9.20622  -29.43657 -14.25795 1.000 25.27913 ? 84  LYS   A N   1 
ATOM   549  C CA  . LYS   A 1 77  ? -8.49010  -30.31294 -13.33466 1.000 26.73686 ? 84  LYS   A CA  1 
ATOM   550  C C   . LYS   A 1 77  ? -8.02292  -31.59357 -14.00800 1.000 26.44807 ? 84  LYS   A C   1 
ATOM   551  O O   . LYS   A 1 77  ? -6.99368  -32.15341 -13.61459 1.000 28.82257 ? 84  LYS   A O   1 
ATOM   552  C CB  . LYS   A 1 77  ? -9.36366  -30.65385 -12.12373 1.000 30.07476 ? 84  LYS   A CB  1 
ATOM   553  C CG  . LYS   A 1 77  ? -9.56730  -29.49043 -11.16310 1.000 34.76318 ? 84  LYS   A CG  1 
ATOM   554  C CD  . LYS   A 1 77  ? -10.80953 -29.70002 -10.31644 1.000 33.25359 ? 84  LYS   A CD  1 
ATOM   555  C CE  . LYS   A 1 77  ? -10.55377 -29.35433 -8.86402  1.000 45.33057 ? 84  LYS   A CE  1 
ATOM   556  N NZ  . LYS   A 1 77  ? -10.44673 -27.88171 -8.66986  1.000 41.13852 ? 84  LYS   A NZ  1 
ATOM   557  N N   . GLN   A 1 78  ? -8.75546  -32.07505 -15.01486 1.000 32.55979 ? 85  GLN   A N   1 
ATOM   558  C CA  . GLN   A 1 78  ? -8.33288  -33.28368 -15.71965 1.000 31.70832 ? 85  GLN   A CA  1 
ATOM   559  C C   . GLN   A 1 78  ? -6.97159  -33.08273 -16.37119 1.000 34.05870 ? 85  GLN   A C   1 
ATOM   560  O O   . GLN   A 1 78  ? -6.09026  -33.94300 -16.27080 1.000 30.27614 ? 85  GLN   A O   1 
ATOM   561  C CB  . GLN   A 1 78  ? -9.37494  -33.67730 -16.76559 1.000 35.17220 ? 85  GLN   A CB  1 
ATOM   562  C CG  . GLN   A 1 78  ? -9.44984  -35.17960 -17.03137 1.000 46.39803 ? 85  GLN   A CG  1 
ATOM   563  C CD  . GLN   A 1 78  ? -10.62434 -35.85273 -16.34446 1.000 60.39243 ? 85  GLN   A CD  1 
ATOM   564  O OE1 . GLN   A 1 78  ? -11.55325 -35.18908 -15.88260 1.000 64.71247 ? 85  GLN   A OE1 1 
ATOM   565  N NE2 . GLN   A 1 78  ? -10.58683 -37.17994 -16.27211 1.000 59.32996 ? 85  GLN   A NE2 1 
ATOM   566  N N   . ASP   A 1 79  ? -6.78429  -31.94092 -17.03758 1.000 24.88556 ? 86  ASP   A N   1 
ATOM   567  C CA  . ASP   A 1 79  ? -5.53835  -31.60312 -17.70548 1.000 24.87084 ? 86  ASP   A CA  1 
ATOM   568  C C   . ASP   A 1 79  ? -4.55426  -30.91101 -16.78065 1.000 24.53244 ? 86  ASP   A C   1 
ATOM   569  O O   . ASP   A 1 79  ? -3.38691  -30.73901 -17.15817 1.000 23.98510 ? 86  ASP   A O   1 
ATOM   570  C CB  . ASP   A 1 79  ? -5.80454  -30.68726 -18.91281 1.000 24.82878 ? 86  ASP   A CB  1 
ATOM   571  C CG  . ASP   A 1 79  ? -6.64467  -31.35520 -19.98345 1.000 33.95990 ? 86  ASP   A CG  1 
ATOM   572  O OD1 . ASP   A 1 79  ? -6.80283  -32.59471 -19.92632 1.000 35.37760 ? 86  ASP   A OD1 1 
ATOM   573  O OD2 . ASP   A 1 79  ? -7.14154  -30.63082 -20.87438 1.000 36.55759 ? 86  ASP   A OD2 1 
ATOM   574  N N   . ARG   A 1 80  ? -5.00690  -30.50717 -15.59454 1.000 22.94563 ? 87  ARG   A N   1 
ATOM   575  C CA  . ARG   A 1 80  ? -4.24340  -29.64213 -14.69596 1.000 22.74394 ? 87  ARG   A CA  1 
ATOM   576  C C   . ARG   A 1 80  ? -3.74226  -28.39059 -15.42170 1.000 20.25439 ? 87  ARG   A C   1 
ATOM   577  O O   . ARG   A 1 80  ? -2.57028  -28.01428 -15.34328 1.000 23.06040 ? 87  ARG   A O   1 
ATOM   578  C CB  . ARG   A 1 80  ? -3.08899  -30.39490 -14.04280 1.000 22.97741 ? 87  ARG   A CB  1 
ATOM   579  C CG  . ARG   A 1 80  ? -2.67454  -29.72529 -12.73184 1.000 26.27550 ? 87  ARG   A CG  1 
ATOM   580  C CD  . ARG   A 1 80  ? -1.25371  -30.09306 -12.35061 1.000 29.81387 ? 87  ARG   A CD  1 
ATOM   581  N NE  . ARG   A 1 80  ? -1.11471  -31.48298 -11.96446 1.000 36.77900 ? 87  ARG   A NE  1 
ATOM   582  C CZ  . ARG   A 1 80  ? 0.02834   -32.15254 -12.04354 1.000 38.85639 ? 87  ARG   A CZ  1 
ATOM   583  N NH1 . ARG   A 1 80  ? 1.12723   -31.58845 -12.52631 1.000 37.23118 ? 87  ARG   A NH1 1 
ATOM   584  N NH2 . ARG   A 1 80  ? 0.07192   -33.41554 -11.63394 1.000 38.29251 ? 87  ARG   A NH2 1 
ATOM   585  N N   . THR   A 1 81  ? -4.65249  -27.71619 -16.10835 1.000 16.33976 ? 88  THR   A N   1 
ATOM   586  C CA  . THR   A 1 81  ? -4.31424  -26.48344 -16.80206 1.000 14.61657 ? 88  THR   A CA  1 
ATOM   587  C C   . THR   A 1 81  ? -5.22690  -25.35095 -16.36821 1.000 16.41238 ? 88  THR   A C   1 
ATOM   588  O O   . THR   A 1 81  ? -6.41344  -25.55709 -16.08515 1.000 18.47925 ? 88  THR   A O   1 
ATOM   589  C CB  . THR   A 1 81  ? -4.42627  -26.62564 -18.32294 1.000 15.65462 ? 88  THR   A CB  1 
ATOM   590  O OG1 . THR   A 1 81  ? -5.76113  -27.03262 -18.67133 1.000 20.82328 ? 88  THR   A OG1 1 
ATOM   591  C CG2 . THR   A 1 81  ? -3.44128  -27.65489 -18.83757 1.000 18.80019 ? 88  THR   A CG2 1 
ATOM   592  N N   . LEU   A 1 82  ? -4.65726  -24.14920 -16.33079 1.000 13.53503 ? 89  LEU   A N   1 
ATOM   593  C CA  . LEU   A 1 82  ? -5.39928  -22.89830 -16.24072 1.000 15.63428 ? 89  LEU   A CA  1 
ATOM   594  C C   . LEU   A 1 82  ? -5.10844  -22.11986 -17.50937 1.000 14.79582 ? 89  LEU   A C   1 
ATOM   595  O O   . LEU   A 1 82  ? -3.93990  -21.84431 -17.81249 1.000 16.78868 ? 89  LEU   A O   1 
ATOM   596  C CB  . LEU   A 1 82  ? -5.00998  -22.08318 -15.00262 1.000 13.35244 ? 89  LEU   A CB  1 
ATOM   597  C CG  . LEU   A 1 82  ? -5.74106  -20.75669 -14.84649 1.000 14.56105 ? 89  LEU   A CG  1 
ATOM   598  C CD1 . LEU   A 1 82  ? -7.27481  -21.00265 -14.71274 1.000 18.69783 ? 89  LEU   A CD1 1 
ATOM   599  C CD2 . LEU   A 1 82  ? -5.19272  -19.99139 -13.64914 1.000 17.15763 ? 89  LEU   A CD2 1 
ATOM   600  N N   . THR   A 1 83  ? -6.16185  -21.80192 -18.26656 1.000 14.93243 ? 90  THR   A N   1 
ATOM   601  C CA  . THR   A 1 83  ? -6.04880  -21.06635 -19.52334 1.000 14.75089 ? 90  THR   A CA  1 
ATOM   602  C C   . THR   A 1 83  ? -6.61250  -19.66116 -19.35831 1.000 18.73079 ? 90  THR   A C   1 
ATOM   603  O O   . THR   A 1 83  ? -7.73059  -19.48202 -18.84730 1.000 14.70720 ? 90  THR   A O   1 
ATOM   604  C CB  . THR   A 1 83  ? -6.76556  -21.79842 -20.66245 1.000 17.26488 ? 90  THR   A CB  1 
ATOM   605  O OG1 . THR   A 1 83  ? -6.24611  -23.12703 -20.80061 1.000 17.03698 ? 90  THR   A OG1 1 
ATOM   606  C CG2 . THR   A 1 83  ? -6.57742  -21.06913 -21.99107 1.000 18.77758 ? 90  THR   A CG2 1 
ATOM   607  N N   . ILE   A 1 84  ? -5.83111  -18.66899 -19.77663 1.000 12.32586 ? 91  ILE   A N   1 
ATOM   608  C CA  . ILE   A 1 84  ? -6.26074  -17.27741 -19.83298 1.000 15.60241 ? 91  ILE   A CA  1 
ATOM   609  C C   . ILE   A 1 84  ? -6.42769  -16.93901 -21.30568 1.000 16.18786 ? 91  ILE   A C   1 
ATOM   610  O O   . ILE   A 1 84  ? -5.44120  -16.88495 -22.05496 1.000 15.32912 ? 91  ILE   A O   1 
ATOM   611  C CB  . ILE   A 1 84  ? -5.26094  -16.32139 -19.17379 1.000 15.73810 ? 91  ILE   A CB  1 
ATOM   612  C CG1 . ILE   A 1 84  ? -5.07575  -16.60079 -17.67636 1.000 13.51501 ? 91  ILE   A CG1 1 
ATOM   613  C CG2 . ILE   A 1 84  ? -5.71057  -14.89600 -19.38404 1.000 13.69790 ? 91  ILE   A CG2 1 
ATOM   614  C CD1 . ILE   A 1 84  ? -4.13094  -17.77396 -17.34717 1.000 19.78296 ? 91  ILE   A CD1 1 
ATOM   615  N N   . VAL   A 1 85  ? -7.66946  -16.71933 -21.72551 1.000 11.96764 ? 92  VAL   A N   1 
ATOM   616  C CA  . VAL   A 1 85  ? -8.02552  -16.44546 -23.11856 1.000 13.17469 ? 92  VAL   A CA  1 
ATOM   617  C C   . VAL   A 1 85  ? -8.42025  -14.98210 -23.24373 1.000 17.09807 ? 92  VAL   A C   1 
ATOM   618  O O   . VAL   A 1 85  ? -9.21061  -14.48436 -22.43744 1.000 16.60217 ? 92  VAL   A O   1 
ATOM   619  C CB  . VAL   A 1 85  ? -9.19347  -17.33690 -23.59943 1.000 16.97867 ? 92  VAL   A CB  1 
ATOM   620  C CG1 . VAL   A 1 85  ? -9.47077  -17.14205 -25.10625 1.000 20.51431 ? 92  VAL   A CG1 1 
ATOM   621  C CG2 . VAL   A 1 85  ? -8.91696  -18.79501 -23.30358 1.000 21.67988 ? 92  VAL   A CG2 1 
ATOM   622  N N   . ASP   A 1 86  ? -7.91645  -14.30089 -24.27281 1.000 15.32818 ? 93  ASP   A N   1 
ATOM   623  C CA  . ASP   A 1 86  ? -8.42558  -12.97777 -24.62432 1.000 12.72458 ? 93  ASP   A CA  1 
ATOM   624  C C   . ASP   A 1 86  ? -8.66246  -12.89609 -26.12964 1.000 13.99953 ? 93  ASP   A C   1 
ATOM   625  O O   . ASP   A 1 86  ? -8.14123  -13.68878 -26.91892 1.000 14.27899 ? 93  ASP   A O   1 
ATOM   626  C CB  . ASP   A 1 86  ? -7.49097  -11.84906 -24.14744 1.000 12.54063 ? 93  ASP   A CB  1 
ATOM   627  C CG  . ASP   A 1 86  ? -6.15509  -11.84704 -24.86830 1.000 16.18487 ? 93  ASP   A CG  1 
ATOM   628  O OD1 . ASP   A 1 86  ? -6.12577  -11.49484 -26.07626 1.000 16.46780 ? 93  ASP   A OD1 1 
ATOM   629  O OD2 . ASP   A 1 86  ? -5.14511  -12.21926 -24.21916 1.000 16.25923 ? 93  ASP   A OD2 1 
ATOM   630  N N   . THR   A 1 87  ? -9.49162  -11.93927 -26.52230 1.000 15.86785 ? 94  THR   A N   1 
ATOM   631  C CA  . THR   A 1 87  ? -9.71315  -11.62122 -27.92578 1.000 15.53506 ? 94  THR   A CA  1 
ATOM   632  C C   . THR   A 1 87  ? -8.98981  -10.32948 -28.29385 1.000 14.98000 ? 94  THR   A C   1 
ATOM   633  O O   . THR   A 1 87  ? -9.48457  -9.51178  -29.07097 1.000 15.98449 ? 94  THR   A O   1 
ATOM   634  C CB  . THR   A 1 87  ? -11.20341 -11.53895 -28.20930 1.000 19.25152 ? 94  THR   A CB  1 
ATOM   635  O OG1 . THR   A 1 87  ? -11.80513 -10.66262 -27.25311 1.000 17.49753 ? 94  THR   A OG1 1 
ATOM   636  C CG2 . THR   A 1 87  ? -11.83031 -12.90833 -28.05795 1.000 17.03064 ? 94  THR   A CG2 1 
ATOM   637  N N   . GLY   A 1 88  ? -7.79215  -10.13559 -27.73204 1.000 16.61148 ? 95  GLY   A N   1 
ATOM   638  C CA  . GLY   A 1 88  ? -7.03791  -8.94724  -28.08704 1.000 13.72422 ? 95  GLY   A CA  1 
ATOM   639  C C   . GLY   A 1 88  ? -6.37570  -9.02297  -29.45400 1.000 13.44739 ? 95  GLY   A C   1 
ATOM   640  O O   . GLY   A 1 88  ? -6.77249  -9.82075  -30.30696 1.000 16.44915 ? 95  GLY   A O   1 
ATOM   641  N N   . ILE   A 1 89  ? -5.33339  -8.20885  -29.66008 1.000 16.13888 ? 96  ILE   A N   1 
ATOM   642  C CA  . ILE   A 1 89  ? -4.72044  -8.06285  -30.98006 1.000 16.90473 ? 96  ILE   A CA  1 
ATOM   643  C C   . ILE   A 1 89  ? -3.92609  -9.29034  -31.40658 1.000 15.60204 ? 96  ILE   A C   1 
ATOM   644  O O   . ILE   A 1 89  ? -3.67904  -9.47352  -32.60060 1.000 18.58253 ? 96  ILE   A O   1 
ATOM   645  C CB  . ILE   A 1 89  ? -3.84415  -6.79551  -31.00115 1.000 16.65478 ? 96  ILE   A CB  1 
ATOM   646  C CG1 . ILE   A 1 89  ? -3.45866  -6.43585  -32.44741 1.000 19.25274 ? 96  ILE   A CG1 1 
ATOM   647  C CG2 . ILE   A 1 89  ? -2.63988  -6.97212  -30.05675 1.000 17.63130 ? 96  ILE   A CG2 1 
ATOM   648  C CD1 . ILE   A 1 89  ? -3.30796  -4.97098  -32.68400 1.000 22.02063 ? 96  ILE   A CD1 1 
ATOM   649  N N   . GLY   A 1 90  ? -3.54060  -10.15691 -30.46980 1.000 17.19594 ? 97  GLY   A N   1 
ATOM   650  C CA  . GLY   A 1 90  ? -2.77894  -11.33558 -30.81612 1.000 15.99929 ? 97  GLY   A CA  1 
ATOM   651  C C   . GLY   A 1 90  ? -1.32955  -11.00915 -31.09205 1.000 16.39993 ? 97  GLY   A C   1 
ATOM   652  O O   . GLY   A 1 90  ? -0.88240  -9.85796  -31.01536 1.000 20.51548 ? 97  GLY   A O   1 
ATOM   653  N N   . MET   A 1 91  ? -0.56495  -12.05809 -31.40138 1.000 16.77961 ? 98  MET   A N   1 
ATOM   654  C CA  . MET   A 1 91  ? 0.86593   -11.93284 -31.66209 1.000 15.26050 ? 98  MET   A CA  1 
ATOM   655  C C   . MET   A 1 91  ? 1.24279   -12.55073 -32.99886 1.000 15.57590 ? 98  MET   A C   1 
ATOM   656  O O   . MET   A 1 91  ? 0.73519   -13.61944 -33.37261 1.000 17.23232 ? 98  MET   A O   1 
ATOM   657  C CB  . MET   A 1 91  ? 1.73216   -12.60337 -30.59923 1.000 16.76726 ? 98  MET   A CB  1 
ATOM   658  C CG  . MET   A 1 91  ? 1.90474   -11.77158 -29.35438 1.000 20.30011 ? 98  MET   A CG  1 
ATOM   659  S SD  . MET   A 1 91  ? 2.31174   -12.66377 -27.82883 1.000 17.98771 ? 98  MET   A SD  1 
ATOM   660  C CE  . MET   A 1 91  ? 1.17618   -14.03968 -27.77551 1.000 16.39657 ? 98  MET   A CE  1 
ATOM   661  N N   . THR   A 1 92  ? 2.17601   -11.89601 -33.69047 1.000 18.38150 ? 99  THR   A N   1 
ATOM   662  C CA  . THR   A 1 92  ? 2.71558   -12.41891 -34.93973 1.000 17.72338 ? 99  THR   A CA  1 
ATOM   663  C C   . THR   A 1 92  ? 3.82672   -13.43233 -34.66758 1.000 17.16893 ? 99  THR   A C   1 
ATOM   664  O O   . THR   A 1 92  ? 4.32497   -13.57176 -33.54590 1.000 17.67664 ? 99  THR   A O   1 
ATOM   665  C CB  . THR   A 1 92  ? 3.26647   -11.29489 -35.82249 1.000 18.80686 ? 99  THR   A CB  1 
ATOM   666  O OG1 . THR   A 1 92  ? 4.38245   -10.67295 -35.16354 1.000 19.67774 ? 99  THR   A OG1 1 
ATOM   667  C CG2 . THR   A 1 92  ? 2.19625   -10.25467 -36.09167 1.000 19.74060 ? 99  THR   A CG2 1 
ATOM   668  N N   . LYS   A 1 93  ? 4.21487   -14.16494 -35.71298 1.000 20.04097 ? 100 LYS   A N   1 
ATOM   669  C CA  . LYS   A 1 93  ? 5.36231   -15.05580 -35.57908 1.000 17.15811 ? 100 LYS   A CA  1 
ATOM   670  C C   . LYS   A 1 93  ? 6.60723   -14.26674 -35.18123 1.000 19.36932 ? 100 LYS   A C   1 
ATOM   671  O O   . LYS   A 1 93  ? 7.38803   -14.70859 -34.33002 1.000 20.91455 ? 100 LYS   A O   1 
ATOM   672  C CB  . LYS   A 1 93  ? 5.59021   -15.82202 -36.88113 1.000 20.27285 ? 100 LYS   A CB  1 
ATOM   673  C CG  . LYS   A 1 93  ? 6.62660   -16.91470 -36.75617 1.000 22.80811 ? 100 LYS   A CG  1 
ATOM   674  C CD  . LYS   A 1 93  ? 6.84253   -17.65635 -38.05422 1.000 27.44135 ? 100 LYS   A CD  1 
ATOM   675  C CE  . LYS   A 1 93  ? 7.64659   -18.92179 -37.81502 1.000 31.48769 ? 100 LYS   A CE  1 
ATOM   676  N NZ  . LYS   A 1 93  ? 8.18734   -19.48017 -39.07355 1.000 35.48478 ? 100 LYS   A NZ  1 
ATOM   677  N N   . ALA   A 1 94  ? 6.77944   -13.07088 -35.74920 1.000 19.76182 ? 101 ALA   A N   1 
ATOM   678  C CA  . ALA   A 1 94  ? 7.94130   -12.25381 -35.40565 1.000 18.70052 ? 101 ALA   A CA  1 
ATOM   679  C C   . ALA   A 1 94  ? 7.89076   -11.80336 -33.95120 1.000 18.43732 ? 101 ALA   A C   1 
ATOM   680  O O   . ALA   A 1 94  ? 8.93374   -11.71667 -33.28722 1.000 20.95689 ? 101 ALA   A O   1 
ATOM   681  C CB  . ALA   A 1 94  ? 8.02441   -11.04438 -36.33275 1.000 20.85661 ? 101 ALA   A CB  1 
ATOM   682  N N   . ASP   A 1 95  ? 6.68812   -11.50493 -33.45029 1.000 19.37371 ? 102 ASP   A N   1 
ATOM   683  C CA  . ASP   A 1 95  ? 6.52337   -11.18581 -32.03254 1.000 18.93922 ? 102 ASP   A CA  1 
ATOM   684  C C   . ASP   A 1 95  ? 6.98347   -12.34316 -31.16317 1.000 16.57264 ? 102 ASP   A C   1 
ATOM   685  O O   . ASP   A 1 95  ? 7.69861   -12.14907 -30.17414 1.000 20.98929 ? 102 ASP   A O   1 
ATOM   686  C CB  . ASP   A 1 95  ? 5.06540   -10.88411 -31.70810 1.000 18.19329 ? 102 ASP   A CB  1 
ATOM   687  C CG  . ASP   A 1 95  ? 4.60959   -9.52626  -32.17915 1.000 19.89355 ? 102 ASP   A CG  1 
ATOM   688  O OD1 . ASP   A 1 95  ? 5.44860   -8.61109  -32.31887 1.000 24.87738 ? 102 ASP   A OD1 1 
ATOM   689  O OD2 . ASP   A 1 95  ? 3.38516   -9.38827  -32.40215 1.000 21.71978 ? 102 ASP   A OD2 1 
ATOM   690  N N   . LEU   A 1 96  ? 6.53699   -13.55509 -31.50174 1.000 16.99054 ? 103 LEU   A N   1 
ATOM   691  C CA  . LEU   A 1 96  ? 6.83294   -14.73984 -30.70085 1.000 16.79764 ? 103 LEU   A CA  1 
ATOM   692  C C   . LEU   A 1 96  ? 8.31791   -15.07384 -30.71041 1.000 22.42927 ? 103 LEU   A C   1 
ATOM   693  O O   . LEU   A 1 96  ? 8.87978   -15.47089 -29.68382 1.000 20.29299 ? 103 LEU   A O   1 
ATOM   694  C CB  . LEU   A 1 96  ? 6.04035   -15.91847 -31.24082 1.000 17.30816 ? 103 LEU   A CB  1 
ATOM   695  C CG  . LEU   A 1 96  ? 4.53477   -15.90637 -31.03515 1.000 16.03099 ? 103 LEU   A CG  1 
ATOM   696  C CD1 . LEU   A 1 96  ? 3.94652   -17.12876 -31.71107 1.000 20.19827 ? 103 LEU   A CD1 1 
ATOM   697  C CD2 . LEU   A 1 96  ? 4.17909   -15.89952 -29.54811 1.000 17.58711 ? 103 LEU   A CD2 1 
ATOM   698  N N   . ILE   A 1 97  ? 8.95666   -14.95280 -31.86914 1.000 22.08172 ? 104 ILE   A N   1 
ATOM   699  C CA  . ILE   A 1 97  ? 10.33478  -15.39928 -32.03441 1.000 18.78149 ? 104 ILE   A CA  1 
ATOM   700  C C   . ILE   A 1 97  ? 11.32877  -14.32369 -31.61776 1.000 27.46876 ? 104 ILE   A C   1 
ATOM   701  O O   . ILE   A 1 97  ? 12.35177  -14.63115 -30.99972 1.000 29.60162 ? 104 ILE   A O   1 
ATOM   702  C CB  . ILE   A 1 97  ? 10.59454  -15.85454 -33.48402 1.000 21.22965 ? 104 ILE   A CB  1 
ATOM   703  C CG1 . ILE   A 1 97  ? 9.76235   -17.09771 -33.81318 1.000 25.71014 ? 104 ILE   A CG1 1 
ATOM   704  C CG2 . ILE   A 1 97  ? 12.07603  -16.13955 -33.69249 1.000 31.25246 ? 104 ILE   A CG2 1 
ATOM   705  C CD1 . ILE   A 1 97  ? 9.74988   -17.41620 -35.25525 1.000 28.37147 ? 104 ILE   A CD1 1 
ATOM   706  N N   . ASN   A 1 98  ? 11.04961  -13.05341 -31.91470 1.000 26.05583 ? 105 ASN   A N   1 
ATOM   707  C CA  . ASN   A 1 98  ? 12.08500  -12.04692 -31.72576 1.000 25.84749 ? 105 ASN   A CA  1 
ATOM   708  C C   . ASN   A 1 98  ? 11.62056  -10.74591 -31.06821 1.000 25.91354 ? 105 ASN   A C   1 
ATOM   709  O O   . ASN   A 1 98  ? 12.29264  -10.26402 -30.15230 1.000 27.60026 ? 105 ASN   A O   1 
ATOM   710  C CB  . ASN   A 1 98  ? 12.73797  -11.72400 -33.06661 1.000 28.80063 ? 105 ASN   A CB  1 
ATOM   711  C CG  . ASN   A 1 98  ? 14.07540  -11.03361 -32.90264 1.000 45.27439 ? 105 ASN   A CG  1 
ATOM   712  O OD1 . ASN   A 1 98  ? 15.07346  -11.66815 -32.54663 1.000 50.02525 ? 105 ASN   A OD1 1 
ATOM   713  N ND2 . ASN   A 1 98  ? 14.10116  -9.72483  -33.13319 1.000 50.23110 ? 105 ASN   A ND2 1 
ATOM   714  N N   . ASN   A 1 99  ? 10.51933  -10.14241 -31.53542 1.000 22.87609 ? 106 ASN   A N   1 
ATOM   715  C CA  . ASN   A 1 99  ? 10.21790  -8.76919  -31.12680 1.000 21.91951 ? 106 ASN   A CA  1 
ATOM   716  C C   . ASN   A 1 99  ? 9.98602   -8.66613  -29.62739 1.000 20.35669 ? 106 ASN   A C   1 
ATOM   717  O O   . ASN   A 1 99  ? 10.47132  -7.73284  -28.98072 1.000 22.51580 ? 106 ASN   A O   1 
ATOM   718  C CB  . ASN   A 1 99  ? 9.00525   -8.20237  -31.87338 1.000 23.54055 ? 106 ASN   A CB  1 
ATOM   719  C CG  . ASN   A 1 99  ? 9.15194   -8.24560  -33.37240 1.000 33.32801 ? 106 ASN   A CG  1 
ATOM   720  O OD1 . ASN   A 1 99  ? 10.25741  -8.27355  -33.91238 1.000 31.61817 ? 106 ASN   A OD1 1 
ATOM   721  N ND2 . ASN   A 1 99  ? 8.01056   -8.22240  -34.07166 1.000 29.96720 ? 106 ASN   A ND2 1 
ATOM   722  N N   . LEU   A 1 100 ? 9.23586   -9.60880  -29.05612 1.000 16.39200 ? 107 LEU   A N   1 
ATOM   723  C CA  . LEU   A 1 100 ? 8.87870   -9.48172  -27.64506 1.000 18.83746 ? 107 LEU   A CA  1 
ATOM   724  C C   . LEU   A 1 100 ? 10.06819  -9.77492  -26.74557 1.000 22.88325 ? 107 LEU   A C   1 
ATOM   725  O O   . LEU   A 1 100 ? 10.22210  -9.14573  -25.69105 1.000 23.53176 ? 107 LEU   A O   1 
ATOM   726  C CB  . LEU   A 1 100 ? 7.69911   -10.39517 -27.31531 1.000 23.69880 ? 107 LEU   A CB  1 
ATOM   727  C CG  . LEU   A 1 100 ? 6.40583   -10.01072 -28.03802 1.000 21.36603 ? 107 LEU   A CG  1 
ATOM   728  C CD1 . LEU   A 1 100 ? 5.34299   -11.06468 -27.78637 1.000 21.80583 ? 107 LEU   A CD1 1 
ATOM   729  C CD2 . LEU   A 1 100 ? 5.90660   -8.62938  -27.57909 1.000 30.43458 ? 107 LEU   A CD2 1 
ATOM   730  N N   . GLY   A 1 101 ? 10.91873  -10.71997 -27.14637 1.000 22.98830 ? 108 GLY   A N   1 
ATOM   731  C CA  . GLY   A 1 101 ? 12.12801  -10.98172 -26.38367 1.000 25.60219 ? 108 GLY   A CA  1 
ATOM   732  C C   . GLY   A 1 101 ? 13.10173  -9.82267  -26.44059 1.000 25.35343 ? 108 GLY   A C   1 
ATOM   733  O O   . GLY   A 1 101 ? 13.78069  -9.52770  -25.45057 1.000 25.94050 ? 108 GLY   A O   1 
ATOM   734  N N   . THR   A 1 102 ? 13.17059  -9.14372  -27.59051 1.000 22.05529 ? 109 THR   A N   1 
ATOM   735  C CA  . THR   A 1 102 ? 14.03051  -7.97457  -27.73291 1.000 25.53645 ? 109 THR   A CA  1 
ATOM   736  C C   . THR   A 1 102 ? 13.61953  -6.86339  -26.77124 1.000 25.29003 ? 109 THR   A C   1 
ATOM   737  O O   . THR   A 1 102 ? 14.46374  -6.28937  -26.07078 1.000 32.85881 ? 109 THR   A O   1 
ATOM   738  C CB  . THR   A 1 102 ? 13.99721  -7.49269  -29.18471 1.000 30.40188 ? 109 THR   A CB  1 
ATOM   739  O OG1 . THR   A 1 102 ? 14.53781  -8.52353  -30.01800 1.000 36.15489 ? 109 THR   A OG1 1 
ATOM   740  C CG2 . THR   A 1 102 ? 14.80769  -6.22139  -29.36637 1.000 29.84926 ? 109 THR   A CG2 1 
ATOM   741  N N   . ILE   A 1 103 ? 12.32379  -6.55453  -26.71773 1.000 25.59106 ? 110 ILE   A N   1 
ATOM   742  C CA  . ILE   A 1 103 ? 11.83309  -5.54679  -25.78116 1.000 26.93229 ? 110 ILE   A CA  1 
ATOM   743  C C   . ILE   A 1 103 ? 12.08290  -5.98611  -24.34787 1.000 29.71470 ? 110 ILE   A C   1 
ATOM   744  O O   . ILE   A 1 103 ? 12.47575  -5.17825  -23.49634 1.000 32.59406 ? 110 ILE   A O   1 
ATOM   745  C CB  . ILE   A 1 103 ? 10.33829  -5.25560  -26.02526 1.000 32.69068 ? 110 ILE   A CB  1 
ATOM   746  C CG1 . ILE   A 1 103 ? 10.07146  -4.93767  -27.49347 1.000 33.82649 ? 110 ILE   A CG1 1 
ATOM   747  C CG2 . ILE   A 1 103 ? 9.87027   -4.10502  -25.15360 1.000 33.54718 ? 110 ILE   A CG2 1 
ATOM   748  C CD1 . ILE   A 1 103 ? 10.83655  -3.73474  -27.99646 1.000 37.29320 ? 110 ILE   A CD1 1 
ATOM   749  N N   . ALA   A 1 104 ? 11.87666  -7.27506  -24.06243 1.000 25.74250 ? 111 ALA   A N   1 
ATOM   750  C CA  . ALA   A 1 104 ? 12.01177  -7.78902  -22.70568 1.000 28.72030 ? 111 ALA   A CA  1 
ATOM   751  C C   . ALA   A 1 104 ? 13.44553  -7.72155  -22.19686 1.000 32.55750 ? 111 ALA   A C   1 
ATOM   752  O O   . ALA   A 1 104 ? 13.66325  -7.79401  -20.98017 1.000 28.15027 ? 111 ALA   A O   1 
ATOM   753  C CB  . ALA   A 1 104 ? 11.50471  -9.22899  -22.64394 1.000 24.55031 ? 111 ALA   A CB  1 
ATOM   754  N N   . LYS   A 1 105 ? 14.42303  -7.56476  -23.09095 1.000 25.96460 ? 112 LYS   A N   1 
ATOM   755  C CA  . LYS   A 1 105 ? 15.81853  -7.53431  -22.66396 1.000 29.04423 ? 112 LYS   A CA  1 
ATOM   756  C C   . LYS   A 1 105 ? 16.09086  -6.35718  -21.72871 1.000 27.68628 ? 112 LYS   A C   1 
ATOM   757  O O   . LYS   A 1 105 ? 16.72657  -6.52100  -20.67912 1.000 24.63655 ? 112 LYS   A O   1 
ATOM   758  C CB  . LYS   A 1 105 ? 16.72973  -7.49482  -23.89308 1.000 30.03506 ? 112 LYS   A CB  1 
ATOM   759  C CG  . LYS   A 1 105 ? 18.21191  -7.36339  -23.59873 1.000 34.72237 ? 112 LYS   A CG  1 
ATOM   760  C CD  . LYS   A 1 105 ? 19.05506  -8.01134  -24.69690 1.000 36.03227 ? 112 LYS   A CD  1 
ATOM   761  C CE  . LYS   A 1 105 ? 20.51851  -8.06997  -24.29496 1.000 38.65648 ? 112 LYS   A CE  1 
ATOM   762  N NZ  . LYS   A 1 105 ? 21.42818  -7.95254  -25.46400 1.000 43.08883 ? 112 LYS   A NZ  1 
ATOM   763  N N   . SER   A 1 106 ? 15.60900  -5.16026  -22.08472 1.000 26.25862 ? 113 SER   A N   1 
ATOM   764  C CA  . SER   A 1 106 ? 15.87945  -3.99388  -21.24994 1.000 25.04556 ? 113 SER   A CA  1 
ATOM   765  C C   . SER   A 1 106 ? 15.07291  -4.04611  -19.95941 1.000 26.30985 ? 113 SER   A C   1 
ATOM   766  O O   . SER   A 1 106 ? 15.58760  -3.70044  -18.89077 1.000 23.34127 ? 113 SER   A O   1 
ATOM   767  C CB  . SER   A 1 106 ? 15.58660  -2.69551  -22.00866 1.000 31.10220 ? 113 SER   A CB  1 
ATOM   768  O OG  . SER   A 1 106 ? 14.22934  -2.62038  -22.37823 1.000 33.27063 ? 113 SER   A OG  1 
ATOM   769  N N   . GLY   A 1 107 ? 13.82015  -4.50248  -20.03512 1.000 27.11210 ? 114 GLY   A N   1 
ATOM   770  C CA  . GLY   A 1 107 ? 13.00381  -4.60029  -18.83316 1.000 26.31604 ? 114 GLY   A CA  1 
ATOM   771  C C   . GLY   A 1 107 ? 13.56423  -5.60768  -17.85220 1.000 23.91651 ? 114 GLY   A C   1 
ATOM   772  O O   . GLY   A 1 107 ? 13.51881  -5.39898  -16.63385 1.000 22.08214 ? 114 GLY   A O   1 
ATOM   773  N N   . THR   A 1 108 ? 14.10409  -6.71369  -18.37544 1.000 20.34980 ? 115 THR   A N   1 
ATOM   774  C CA  . THR   A 1 108 ? 14.73844  -7.71421  -17.52541 1.000 18.19712 ? 115 THR   A CA  1 
ATOM   775  C C   . THR   A 1 108 ? 15.92370  -7.12557  -16.78364 1.000 22.81598 ? 115 THR   A C   1 
ATOM   776  O O   . THR   A 1 108 ? 16.05221  -7.30241  -15.56922 1.000 22.52983 ? 115 THR   A O   1 
ATOM   777  C CB  . THR   A 1 108 ? 15.17505  -8.91773  -18.35758 1.000 23.01305 ? 115 THR   A CB  1 
ATOM   778  O OG1 . THR   A 1 108 ? 14.02040  -9.53744  -18.92292 1.000 24.66857 ? 115 THR   A OG1 1 
ATOM   779  C CG2 . THR   A 1 108 ? 15.92440  -9.92050  -17.49826 1.000 24.13611 ? 115 THR   A CG2 1 
ATOM   780  N N   . LYS   A 1 109 ? 16.80068  -6.41745  -17.50192 1.000 18.76248 ? 116 LYS   A N   1 
ATOM   781  C CA  . LYS   A 1 109 ? 17.97247  -5.81787  -16.86773 1.000 23.45557 ? 116 LYS   A CA  1 
ATOM   782  C C   . LYS   A 1 109 ? 17.56803  -4.83574  -15.77211 1.000 23.94041 ? 116 LYS   A C   1 
ATOM   783  O O   . LYS   A 1 109 ? 18.13387  -4.85652  -14.67420 1.000 24.96711 ? 116 LYS   A O   1 
ATOM   784  C CB  . LYS   A 1 109 ? 18.84712  -5.14104  -17.92355 1.000 22.88637 ? 116 LYS   A CB  1 
ATOM   785  C CG  . LYS   A 1 109 ? 20.11467  -4.51440  -17.36810 1.000 25.72665 ? 116 LYS   A CG  1 
ATOM   786  C CD  . LYS   A 1 109 ? 20.59435  -3.38140  -18.27570 1.000 30.89164 ? 116 LYS   A CD  1 
ATOM   787  C CE  . LYS   A 1 109 ? 22.08358  -3.16094  -18.14259 1.000 39.14583 ? 116 LYS   A CE  1 
ATOM   788  N NZ  . LYS   A 1 109 ? 22.37372  -2.40854  -16.90565 1.000 43.22992 ? 116 LYS   A NZ  1 
ATOM   789  N N   . ALA   A 1 110 ? 16.56803  -3.99015  -16.03890 1.000 24.02625 ? 117 ALA   A N   1 
ATOM   790  C CA  . ALA   A 1 110 ? 16.09375  -3.06440  -15.01362 1.000 23.64519 ? 117 ALA   A CA  1 
ATOM   791  C C   . ALA   A 1 110 ? 15.45036  -3.80283  -13.84188 1.000 23.84365 ? 117 ALA   A C   1 
ATOM   792  O O   . ALA   A 1 110 ? 15.61865  -3.40348  -12.68368 1.000 23.79408 ? 117 ALA   A O   1 
ATOM   793  C CB  . ALA   A 1 110 ? 15.10482  -2.07776  -15.62884 1.000 25.81085 ? 117 ALA   A CB  1 
ATOM   794  N N   . PHE   A 1 111 ? 14.68773  -4.86100  -14.12943 1.000 21.85967 ? 118 PHE   A N   1 
ATOM   795  C CA  . PHE   A 1 111 ? 14.05321  -5.65473  -13.07698 1.000 20.93239 ? 118 PHE   A CA  1 
ATOM   796  C C   . PHE   A 1 111 ? 15.10431  -6.31142  -12.19192 1.000 23.72636 ? 118 PHE   A C   1 
ATOM   797  O O   . PHE   A 1 111 ? 14.98724  -6.29588  -10.96304 1.000 20.75471 ? 118 PHE   A O   1 
ATOM   798  C CB  . PHE   A 1 111 ? 13.12447  -6.69677  -13.72193 1.000 19.01679 ? 118 PHE   A CB  1 
ATOM   799  C CG  . PHE   A 1 111 ? 12.42748  -7.62881  -12.74491 1.000 20.47406 ? 118 PHE   A CG  1 
ATOM   800  C CD1 . PHE   A 1 111 ? 11.73825  -7.13566  -11.64699 1.000 20.56039 ? 118 PHE   A CD1 1 
ATOM   801  C CD2 . PHE   A 1 111 ? 12.45486  -9.00309  -12.94807 1.000 18.89337 ? 118 PHE   A CD2 1 
ATOM   802  C CE1 . PHE   A 1 111 ? 11.09642  -7.98734  -10.75425 1.000 18.20693 ? 118 PHE   A CE1 1 
ATOM   803  C CE2 . PHE   A 1 111 ? 11.79152  -9.85763  -12.08097 1.000 22.73367 ? 118 PHE   A CE2 1 
ATOM   804  C CZ  . PHE   A 1 111 ? 11.11742  -9.34042  -10.96883 1.000 18.60541 ? 118 PHE   A CZ  1 
ATOM   805  N N   . MET   A 1 112 ? 16.15505  -6.87300  -12.79991 1.000 22.16947 ? 119 MET   A N   1 
ATOM   806  C CA  . MET   A 1 112 ? 17.23637  -7.47864  -12.02101 1.000 25.70037 ? 119 MET   A CA  1 
ATOM   807  C C   . MET   A 1 112 ? 17.93378  -6.45481  -11.14176 1.000 30.88934 ? 119 MET   A C   1 
ATOM   808  O O   . MET   A 1 112 ? 18.28182  -6.74194  -9.98957  1.000 31.53351 ? 119 MET   A O   1 
ATOM   809  C CB  . MET   A 1 112 ? 18.25697  -8.12648  -12.95227 1.000 27.70996 ? 119 MET   A CB  1 
ATOM   810  C CG  . MET   A 1 112 ? 17.70404  -9.22305  -13.80412 1.000 31.56587 ? 119 MET   A CG  1 
ATOM   811  S SD  . MET   A 1 112 ? 17.19674  -10.62304 -12.82136 1.000 42.13335 ? 119 MET   A SD  1 
ATOM   812  C CE  . MET   A 1 112 ? 17.56254  -11.95305 -13.98130 1.000 33.19695 ? 119 MET   A CE  1 
ATOM   813  N N   . GLU   A 1 113 ? 18.18243  -5.26594  -11.68569 1.000 28.86508 ? 120 GLU   A N   1 
ATOM   814  C CA  . GLU   A 1 113 ? 18.80221  -4.21070  -10.89712 1.000 33.64741 ? 120 GLU   A CA  1 
ATOM   815  C C   . GLU   A 1 113 ? 17.90864  -3.80108  -9.73070  1.000 30.48234 ? 120 GLU   A C   1 
ATOM   816  O O   . GLU   A 1 113 ? 18.40087  -3.57322  -8.61589  1.000 38.52695 ? 120 GLU   A O   1 
ATOM   817  C CB  . GLU   A 1 113 ? 19.11799  -3.01622  -11.79692 1.000 33.09721 ? 120 GLU   A CB  1 
ATOM   818  C CG  . GLU   A 1 113 ? 20.53665  -3.02056  -12.33294 1.000 42.73258 ? 120 GLU   A CG  1 
ATOM   819  C CD  . GLU   A 1 113 ? 20.65190  -2.38343  -13.70513 1.000 43.59997 ? 120 GLU   A CD  1 
ATOM   820  O OE1 . GLU   A 1 113 ? 19.76757  -1.57437  -14.05637 1.000 48.10106 ? 120 GLU   A OE1 1 
ATOM   821  O OE2 . GLU   A 1 113 ? 21.63833  -2.66640  -14.42237 1.000 45.70630 ? 120 GLU   A OE2 1 
ATOM   822  N N   . ALA   A 1 114 ? 16.58863  -3.71774  -9.96819  1.000 29.65412 ? 121 ALA   A N   1 
ATOM   823  C CA  . ALA   A 1 114 ? 15.65825  -3.32768  -8.91269  1.000 25.33182 ? 121 ALA   A CA  1 
ATOM   824  C C   . ALA   A 1 114 ? 15.60427  -4.37858  -7.81277  1.000 32.65827 ? 121 ALA   A C   1 
ATOM   825  O O   . ALA   A 1 114 ? 15.55457  -4.04030  -6.62234  1.000 29.59891 ? 121 ALA   A O   1 
ATOM   826  C CB  . ALA   A 1 114 ? 14.27262  -3.07048  -9.49854  1.000 23.43756 ? 121 ALA   A CB  1 
ATOM   827  N N   . LEU   A 1 115 ? 15.66721  -5.65595  -8.18979  1.000 25.49488 ? 122 LEU   A N   1 
ATOM   828  C CA  . LEU   A 1 115 ? 15.62000  -6.72965  -7.20059  1.000 25.53036 ? 122 LEU   A CA  1 
ATOM   829  C C   . LEU   A 1 115 ? 16.81766  -6.66746  -6.26325  1.000 34.23137 ? 122 LEU   A C   1 
ATOM   830  O O   . LEU   A 1 115 ? 16.68020  -6.87199  -5.05125  1.000 32.63449 ? 122 LEU   A O   1 
ATOM   831  C CB  . LEU   A 1 115 ? 15.57790  -8.08534  -7.90347  1.000 22.09057 ? 122 LEU   A CB  1 
ATOM   832  C CG  . LEU   A 1 115 ? 14.23144  -8.47842  -8.51029  1.000 20.72669 ? 122 LEU   A CG  1 
ATOM   833  C CD1 . LEU   A 1 115 ? 14.36130  -9.74843  -9.34005  1.000 25.62622 ? 122 LEU   A CD1 1 
ATOM   834  C CD2 . LEU   A 1 115 ? 13.16493  -8.63316  -7.43797  1.000 21.32177 ? 122 LEU   A CD2 1 
ATOM   835  N N   . GLN   A 1 116 ? 18.00755  -6.40587  -6.80993  1.000 36.11882 ? 123 GLN   A N   1 
ATOM   836  C CA  . GLN   A 1 116 ? 19.19278  -6.26110  -5.97371  1.000 37.39931 ? 123 GLN   A CA  1 
ATOM   837  C C   . GLN   A 1 116 ? 19.10542  -5.04335  -5.06549  1.000 35.96435 ? 123 GLN   A C   1 
ATOM   838  O O   . GLN   A 1 116 ? 19.73737  -5.02795  -4.00415  1.000 38.81924 ? 123 GLN   A O   1 
ATOM   839  C CB  . GLN   A 1 116 ? 20.44205  -6.17281  -6.85018  1.000 38.31262 ? 123 GLN   A CB  1 
ATOM   840  C CG  . GLN   A 1 116 ? 20.90999  -7.51528  -7.39063  1.000 44.52711 ? 123 GLN   A CG  1 
ATOM   841  C CD  . GLN   A 1 116 ? 21.78749  -8.27155  -6.40021  1.000 63.40219 ? 123 GLN   A CD  1 
ATOM   842  O OE1 . GLN   A 1 116 ? 21.67836  -8.08929  -5.18520  1.000 61.99331 ? 123 GLN   A OE1 1 
ATOM   843  N NE2 . GLN   A 1 116 ? 22.66159  -9.12854  -6.91917  1.000 65.12920 ? 123 GLN   A NE2 1 
ATOM   844  N N   . ALA   A 1 117 ? 18.32300  -4.03810  -5.45012  1.000 34.16715 ? 124 ALA   A N   1 
ATOM   845  C CA  . ALA   A 1 117 ? 18.16799  -2.81301  -4.68288  1.000 40.58094 ? 124 ALA   A CA  1 
ATOM   846  C C   . ALA   A 1 117 ? 17.01747  -2.86198  -3.68257  1.000 36.29948 ? 124 ALA   A C   1 
ATOM   847  O O   . ALA   A 1 117 ? 16.79145  -1.87023  -2.97982  1.000 40.12409 ? 124 ALA   A O   1 
ATOM   848  C CB  . ALA   A 1 117 ? 17.97203  -1.62541  -5.63095  1.000 37.92049 ? 124 ALA   A CB  1 
ATOM   849  N N   . GLY   A 1 118 ? 16.28034  -3.96731  -3.60573  1.000 37.22408 ? 125 GLY   A N   1 
ATOM   850  C CA  . GLY   A 1 118 ? 15.23782  -4.13073  -2.60660  1.000 30.22409 ? 125 GLY   A CA  1 
ATOM   851  C C   . GLY   A 1 118 ? 13.84934  -4.41774  -3.14647  1.000 33.92735 ? 125 GLY   A C   1 
ATOM   852  O O   . GLY   A 1 118 ? 12.92895  -4.62840  -2.34265  1.000 30.43382 ? 125 GLY   A O   1 
ATOM   853  N N   . ALA   A 1 119 ? 13.63931  -4.42989  -4.46139  1.000 26.95754 ? 126 ALA   A N   1 
ATOM   854  C CA  . ALA   A 1 119 ? 12.34013  -4.79714  -4.99852  1.000 22.88606 ? 126 ALA   A CA  1 
ATOM   855  C C   . ALA   A 1 119 ? 12.09762  -6.29395  -4.81443  1.000 26.28398 ? 126 ALA   A C   1 
ATOM   856  O O   . ALA   A 1 119 ? 12.98451  -7.05246  -4.40659  1.000 25.43334 ? 126 ALA   A O   1 
ATOM   857  C CB  . ALA   A 1 119 ? 12.23501  -4.41437  -6.47307  1.000 24.15074 ? 126 ALA   A CB  1 
ATOM   858  N N   . ASP   A 1 120 ? 10.86590  -6.71923  -5.10967  1.000 25.42078 ? 127 ASP   A N   1 
ATOM   859  C CA  . ASP   A 1 120 ? 10.49888  -8.12783  -5.01767  1.000 21.04394 ? 127 ASP   A CA  1 
ATOM   860  C C   . ASP   A 1 120 ? 9.81726   -8.56738  -6.30621  1.000 20.43797 ? 127 ASP   A C   1 
ATOM   861  O O   . ASP   A 1 120 ? 9.50332   -7.75307  -7.18331  1.000 19.97784 ? 127 ASP   A O   1 
ATOM   862  C CB  . ASP   A 1 120 ? 9.59139   -8.40351  -3.81414  1.000 25.35171 ? 127 ASP   A CB  1 
ATOM   863  C CG  . ASP   A 1 120 ? 8.24630   -7.75040  -3.94947  1.000 28.11808 ? 127 ASP   A CG  1 
ATOM   864  O OD1 . ASP   A 1 120 ? 8.15321   -6.51983  -3.75069  1.000 33.51484 ? 127 ASP   A OD1 1 
ATOM   865  O OD2 . ASP   A 1 120 ? 7.28523   -8.47132  -4.27345  1.000 25.64010 ? 127 ASP   A OD2 1 
ATOM   866  N N   . ILE   A 1 121 ? 9.59711   -9.88273  -6.41490  1.000 18.70415 ? 128 ILE   A N   1 
ATOM   867  C CA  . ILE   A 1 121 ? 9.15710   -10.45154 -7.68652  1.000 19.38439 ? 128 ILE   A CA  1 
ATOM   868  C C   . ILE   A 1 121 ? 7.77000   -9.95201  -8.07545  1.000 22.81115 ? 128 ILE   A C   1 
ATOM   869  O O   . ILE   A 1 121 ? 7.44904   -9.88636  -9.27006  1.000 20.28404 ? 128 ILE   A O   1 
ATOM   870  C CB  . ILE   A 1 121 ? 9.23330   -11.99506 -7.62430  1.000 16.96858 ? 128 ILE   A CB  1 
ATOM   871  C CG1 . ILE   A 1 121 ? 10.69523  -12.45136 -7.76196  1.000 24.18140 ? 128 ILE   A CG1 1 
ATOM   872  C CG2 . ILE   A 1 121 ? 8.35526   -12.64030 -8.69845  1.000 15.91637 ? 128 ILE   A CG2 1 
ATOM   873  C CD1 . ILE   A 1 121 ? 10.94346  -13.88124 -7.37365  1.000 23.09646 ? 128 ILE   A CD1 1 
ATOM   874  N N   . SER   A 1 122 ? 6.93868   -9.55268  -7.09836  1.000 17.90519 ? 129 SER   A N   1 
ATOM   875  C CA  . SER   A 1 122 ? 5.60419   -9.04641  -7.42321  1.000 23.66403 ? 129 SER   A CA  1 
ATOM   876  C C   . SER   A 1 122 ? 5.63539   -7.77491  -8.26626  1.000 24.64232 ? 129 SER   A C   1 
ATOM   877  O O   . SER   A 1 122 ? 4.63371   -7.45395  -8.90997  1.000 22.88514 ? 129 SER   A O   1 
ATOM   878  C CB  . SER   A 1 122 ? 4.80223   -8.80694  -6.14325  1.000 22.50667 ? 129 SER   A CB  1 
ATOM   879  O OG  . SER   A 1 122 ? 5.16818   -7.59779  -5.49117  1.000 21.91047 ? 129 SER   A OG  1 
ATOM   880  N N   . MET   A 1 123 ? 6.75720   -7.07136  -8.31129  1.000 22.64582 ? 130 MET   A N   1 
ATOM   881  C CA  . MET   A 1 123 ? 6.88167   -5.83330  -9.06424  1.000 17.28960 ? 130 MET   A CA  1 
ATOM   882  C C   . MET   A 1 123 ? 7.28061   -6.06018  -10.52453 1.000 19.50874 ? 130 MET   A C   1 
ATOM   883  O O   . MET   A 1 123 ? 7.49324   -5.08658  -11.25615 1.000 19.97241 ? 130 MET   A O   1 
ATOM   884  C CB  . MET   A 1 123 ? 7.89110   -4.94324  -8.35019  1.000 21.19983 ? 130 MET   A CB  1 
ATOM   885  C CG  . MET   A 1 123 ? 7.41300   -4.56347  -6.94427  1.000 23.16326 ? 130 MET   A CG  1 
ATOM   886  S SD  . MET   A 1 123 ? 8.66919   -3.80515  -5.92884  1.000 27.67746 ? 130 MET   A SD  1 
ATOM   887  C CE  . MET   A 1 123 ? 8.96713   -2.34122  -6.90543  1.000 24.87377 ? 130 MET   A CE  1 
ATOM   888  N N   . ILE   A 1 124 ? 7.36096   -7.31969  -10.96089 1.000 19.36241 ? 131 ILE   A N   1 
ATOM   889  C CA  . ILE   A 1 124 ? 7.81543   -7.66947  -12.30879 1.000 17.12178 ? 131 ILE   A CA  1 
ATOM   890  C C   . ILE   A 1 124 ? 7.04450   -6.92567  -13.40563 1.000 19.17804 ? 131 ILE   A C   1 
ATOM   891  O O   . ILE   A 1 124 ? 7.61546   -6.57132  -14.44431 1.000 19.01569 ? 131 ILE   A O   1 
ATOM   892  C CB  . ILE   A 1 124 ? 7.71964   -9.20374  -12.48080 1.000 14.72286 ? 131 ILE   A CB  1 
ATOM   893  C CG1 . ILE   A 1 124 ? 8.34971   -9.64417  -13.80450 1.000 15.89685 ? 131 ILE   A CG1 1 
ATOM   894  C CG2 . ILE   A 1 124 ? 6.22636   -9.67774  -12.40697 1.000 19.09510 ? 131 ILE   A CG2 1 
ATOM   895  C CD1 . ILE   A 1 124 ? 8.49964   -11.17382 -13.94547 1.000 16.27457 ? 131 ILE   A CD1 1 
ATOM   896  N N   . GLY   A 1 125 ? 5.75349   -6.65840  -13.19607 1.000 20.55417 ? 132 GLY   A N   1 
ATOM   897  C CA  . GLY   A 1 125 ? 4.96944   -5.99140  -14.22704 1.000 23.13117 ? 132 GLY   A CA  1 
ATOM   898  C C   . GLY   A 1 125 ? 5.38524   -4.55565  -14.48454 1.000 24.48470 ? 132 GLY   A C   1 
ATOM   899  O O   . GLY   A 1 125 ? 5.18066   -4.03421  -15.58528 1.000 24.02680 ? 132 GLY   A O   1 
ATOM   900  N N   . GLN   A 1 126 ? 5.95924   -3.89082  -13.48486 1.000 21.99837 ? 133 GLN   A N   1 
ATOM   901  C CA  . GLN   A 1 126 ? 6.45144   -2.53372  -13.68852 1.000 26.31731 ? 133 GLN   A CA  1 
ATOM   902  C C   . GLN   A 1 126 ? 7.63914   -2.46829  -14.63315 1.000 21.44014 ? 133 GLN   A C   1 
ATOM   903  O O   . GLN   A 1 126 ? 8.07791   -1.35839  -14.94582 1.000 27.10056 ? 133 GLN   A O   1 
ATOM   904  C CB  . GLN   A 1 126 ? 6.83417   -1.89899  -12.35259 1.000 24.59747 ? 133 GLN   A CB  1 
ATOM   905  C CG  . GLN   A 1 126 ? 5.74466   -1.98481  -11.30768 1.000 26.69382 ? 133 GLN   A CG  1 
ATOM   906  C CD  . GLN   A 1 126 ? 6.09944   -1.23835  -10.03872 1.000 32.20834 ? 133 GLN   A CD  1 
ATOM   907  O OE1 . GLN   A 1 126 ? 6.57804   -0.10704  -10.08705 1.000 38.04964 ? 133 GLN   A OE1 1 
ATOM   908  N NE2 . GLN   A 1 126 ? 5.86393   -1.87047  -8.89159  1.000 36.88697 ? 133 GLN   A NE2 1 
ATOM   909  N N   . PHE   A 1 127 ? 8.15858   -3.60978  -15.08688 1.000 20.19289 ? 134 PHE   A N   1 
ATOM   910  C CA  . PHE   A 1 127 ? 9.28127   -3.65543  -16.01378 1.000 19.70359 ? 134 PHE   A CA  1 
ATOM   911  C C   . PHE   A 1 127 ? 8.90832   -4.29619  -17.34124 1.000 25.01856 ? 134 PHE   A C   1 
ATOM   912  O O   . PHE   A 1 127 ? 9.78808   -4.52758  -18.17471 1.000 25.96049 ? 134 PHE   A O   1 
ATOM   913  C CB  . PHE   A 1 127 ? 10.45737  -4.38433  -15.35532 1.000 17.85751 ? 134 PHE   A CB  1 
ATOM   914  C CG  . PHE   A 1 127 ? 10.84834  -3.77372  -14.04867 1.000 21.95936 ? 134 PHE   A CG  1 
ATOM   915  C CD1 . PHE   A 1 127 ? 11.75469  -2.71702  -14.01549 1.000 21.46603 ? 134 PHE   A CD1 1 
ATOM   916  C CD2 . PHE   A 1 127 ? 10.28141  -4.22261  -12.85825 1.000 19.33573 ? 134 PHE   A CD2 1 
ATOM   917  C CE1 . PHE   A 1 127 ? 12.11638  -2.12957  -12.81930 1.000 21.78815 ? 134 PHE   A CE1 1 
ATOM   918  C CE2 . PHE   A 1 127 ? 10.63576  -3.63853  -11.64581 1.000 20.88592 ? 134 PHE   A CE2 1 
ATOM   919  C CZ  . PHE   A 1 127 ? 11.54690  -2.58215  -11.62565 1.000 21.97473 ? 134 PHE   A CZ  1 
ATOM   920  N N   . GLY   A 1 128 ? 7.62892   -4.57820  -17.55957 1.000 22.37569 ? 135 GLY   A N   1 
ATOM   921  C CA  . GLY   A 1 128 ? 7.16021   -5.06228  -18.84438 1.000 24.56282 ? 135 GLY   A CA  1 
ATOM   922  C C   . GLY   A 1 128 ? 7.42683   -6.51622  -19.15169 1.000 22.82027 ? 135 GLY   A C   1 
ATOM   923  O O   . GLY   A 1 128 ? 7.29590   -6.91707  -20.31314 1.000 24.58111 ? 135 GLY   A O   1 
ATOM   924  N N   . VAL   A 1 129 ? 7.77922   -7.33168  -18.16282 1.000 17.93616 ? 136 VAL   A N   1 
ATOM   925  C CA  . VAL   A 1 129 ? 8.09337   -8.73182  -18.43319 1.000 20.09454 ? 136 VAL   A CA  1 
ATOM   926  C C   . VAL   A 1 129 ? 7.23968   -9.63863  -17.55053 1.000 14.60671 ? 136 VAL   A C   1 
ATOM   927  O O   . VAL   A 1 129 ? 7.65370   -10.75000 -17.18716 1.000 14.41053 ? 136 VAL   A O   1 
ATOM   928  C CB  . VAL   A 1 129 ? 9.60404   -8.99230  -18.24371 1.000 16.57408 ? 136 VAL   A CB  1 
ATOM   929  C CG1 . VAL   A 1 129 ? 10.39753  -8.27384  -19.32942 1.000 20.21989 ? 136 VAL   A CG1 1 
ATOM   930  C CG2 . VAL   A 1 129 ? 10.06808  -8.49134  -16.87180 1.000 19.55615 ? 136 VAL   A CG2 1 
ATOM   931  N N   . GLY   A 1 130 ? 6.03004   -9.17394  -17.21406 1.000 17.58324 ? 137 GLY   A N   1 
ATOM   932  C CA  . GLY   A 1 130 ? 5.14363   -9.95078  -16.35810 1.000 14.06138 ? 137 GLY   A CA  1 
ATOM   933  C C   . GLY   A 1 130 ? 4.72184   -11.30275 -16.92020 1.000 16.55208 ? 137 GLY   A C   1 
ATOM   934  O O   . GLY   A 1 130 ? 4.35189   -12.18471 -16.14176 1.000 14.86959 ? 137 GLY   A O   1 
ATOM   935  N N   . PHE   A 1 131 ? 4.72970   -11.47805 -18.25156 1.000 14.12492 ? 138 PHE   A N   1 
ATOM   936  C CA  . PHE   A 1 131 ? 4.40414   -12.77625 -18.83123 1.000 13.41426 ? 138 PHE   A CA  1 
ATOM   937  C C   . PHE   A 1 131 ? 5.20608   -13.89931 -18.18497 1.000 15.08357 ? 138 PHE   A C   1 
ATOM   938  O O   . PHE   A 1 131 ? 4.66720   -14.97636 -17.91335 1.000 12.97767 ? 138 PHE   A O   1 
ATOM   939  C CB  . PHE   A 1 131 ? 4.66178   -12.77636 -20.33891 1.000 13.07095 ? 138 PHE   A CB  1 
ATOM   940  C CG  . PHE   A 1 131 ? 4.68568   -14.16493 -20.94636 1.000 12.92520 ? 138 PHE   A CG  1 
ATOM   941  C CD1 . PHE   A 1 131 ? 3.49450   -14.88191 -21.12656 1.000 11.82160 ? 138 PHE   A CD1 1 
ATOM   942  C CD2 . PHE   A 1 131 ? 5.90157   -14.76954 -21.29551 1.000 14.11874 ? 138 PHE   A CD2 1 
ATOM   943  C CE1 . PHE   A 1 131 ? 3.50526   -16.16524 -21.69147 1.000 13.07062 ? 138 PHE   A CE1 1 
ATOM   944  C CE2 . PHE   A 1 131 ? 5.93956   -16.06611 -21.84883 1.000 15.79623 ? 138 PHE   A CE2 1 
ATOM   945  C CZ  . PHE   A 1 131 ? 4.73246   -16.76623 -22.05063 1.000 15.25622 ? 138 PHE   A CZ  1 
ATOM   946  N N   . TYR   A 1 132 ? 6.49446   -13.66033 -17.91743 1.000 15.88979 ? 139 TYR   A N   1 
ATOM   947  C CA  . TYR   A 1 132 ? 7.34663   -14.74182 -17.43833 1.000 14.49374 ? 139 TYR   A CA  1 
ATOM   948  C C   . TYR   A 1 132 ? 7.02364   -15.14888 -16.00456 1.000 16.02395 ? 139 TYR   A C   1 
ATOM   949  O O   . TYR   A 1 132 ? 7.44946   -16.22920 -15.58156 1.000 14.82770 ? 139 TYR   A O   1 
ATOM   950  C CB  . TYR   A 1 132 ? 8.83753   -14.35847 -17.61899 1.000 13.52766 ? 139 TYR   A CB  1 
ATOM   951  C CG  . TYR   A 1 132 ? 9.16924   -14.04190 -19.07230 1.000 15.19266 ? 139 TYR   A CG  1 
ATOM   952  C CD1 . TYR   A 1 132 ? 9.47614   -15.05863 -19.97386 1.000 18.47122 ? 139 TYR   A CD1 1 
ATOM   953  C CD2 . TYR   A 1 132 ? 9.14206   -12.73161 -19.54521 1.000 17.27384 ? 139 TYR   A CD2 1 
ATOM   954  C CE1 . TYR   A 1 132 ? 9.75269   -14.77063 -21.31548 1.000 18.07023 ? 139 TYR   A CE1 1 
ATOM   955  C CE2 . TYR   A 1 132 ? 9.41723   -12.43416 -20.87028 1.000 18.24077 ? 139 TYR   A CE2 1 
ATOM   956  C CZ  . TYR   A 1 132 ? 9.70669   -13.45893 -21.74940 1.000 18.66264 ? 139 TYR   A CZ  1 
ATOM   957  O OH  . TYR   A 1 132 ? 9.96736   -13.15329 -23.06376 1.000 21.13903 ? 139 TYR   A OH  1 
ATOM   958  N N   . SER   A 1 133 ? 6.24806   -14.34547 -15.26570 1.000 15.72832 ? 140 SER   A N   1 
ATOM   959  C CA  . SER   A 1 133 ? 5.77720   -14.80271 -13.95366 1.000 12.25577 ? 140 SER   A CA  1 
ATOM   960  C C   . SER   A 1 133 ? 4.87579   -16.02585 -14.05157 1.000 11.45992 ? 140 SER   A C   1 
ATOM   961  O O   . SER   A 1 133 ? 4.59425   -16.66013 -13.02261 1.000 13.24207 ? 140 SER   A O   1 
ATOM   962  C CB  . SER   A 1 133 ? 5.05518   -13.65837 -13.22859 1.000 13.57213 ? 140 SER   A CB  1 
ATOM   963  O OG  . SER   A 1 133 ? 3.76887   -13.42902 -13.77949 1.000 15.54530 ? 140 SER   A OG  1 
ATOM   964  N N   . ALA   A 1 134 ? 4.39968   -16.36090 -15.25260 1.000 11.08175 ? 141 ALA   A N   1 
ATOM   965  C CA  . ALA   A 1 134 ? 3.68804   -17.62165 -15.41871 1.000 12.53045 ? 141 ALA   A CA  1 
ATOM   966  C C   . ALA   A 1 134 ? 4.48868   -18.79745 -14.85903 1.000 14.64201 ? 141 ALA   A C   1 
ATOM   967  O O   . ALA   A 1 134 ? 3.89990   -19.76324 -14.36157 1.000 13.39950 ? 141 ALA   A O   1 
ATOM   968  C CB  . ALA   A 1 134 ? 3.37796   -17.85727 -16.90044 1.000 13.62416 ? 141 ALA   A CB  1 
ATOM   969  N N   . TYR   A 1 135 ? 5.82988   -18.73516 -14.92086 1.000 13.10683 ? 142 TYR   A N   1 
ATOM   970  C CA  . TYR   A 1 135 ? 6.66175   -19.84126 -14.43924 1.000 14.01417 ? 142 TYR   A CA  1 
ATOM   971  C C   . TYR   A 1 135 ? 6.75477   -19.89480 -12.91703 1.000 14.03357 ? 142 TYR   A C   1 
ATOM   972  O O   . TYR   A 1 135 ? 7.38270   -20.81310 -12.37428 1.000 16.76828 ? 142 TYR   A O   1 
ATOM   973  C CB  . TYR   A 1 135 ? 8.05170   -19.78207 -15.10336 1.000 14.14405 ? 142 TYR   A CB  1 
ATOM   974  C CG  . TYR   A 1 135 ? 7.90661   -20.14503 -16.57785 1.000 14.85041 ? 142 TYR   A CG  1 
ATOM   975  C CD1 . TYR   A 1 135 ? 7.95184   -21.47773 -16.99107 1.000 14.65668 ? 142 TYR   A CD1 1 
ATOM   976  C CD2 . TYR   A 1 135 ? 7.64010   -19.16583 -17.54026 1.000 14.10810 ? 142 TYR   A CD2 1 
ATOM   977  C CE1 . TYR   A 1 135 ? 7.77566   -21.81717 -18.33208 1.000 15.26265 ? 142 TYR   A CE1 1 
ATOM   978  C CE2 . TYR   A 1 135 ? 7.47745   -19.50350 -18.88923 1.000 14.00280 ? 142 TYR   A CE2 1 
ATOM   979  C CZ  . TYR   A 1 135 ? 7.52891   -20.82429 -19.26194 1.000 14.06598 ? 142 TYR   A CZ  1 
ATOM   980  O OH  . TYR   A 1 135 ? 7.33163   -21.13807 -20.58639 1.000 14.74119 ? 142 TYR   A OH  1 
ATOM   981  N N   . LEU   A 1 136 ? 6.09867   -18.97786 -12.21415 1.000 15.12504 ? 143 LEU   A N   1 
ATOM   982  C CA  . LEU   A 1 136 ? 5.91842   -19.16509 -10.78323 1.000 15.77988 ? 143 LEU   A CA  1 
ATOM   983  C C   . LEU   A 1 136 ? 5.06140   -20.38796 -10.49019 1.000 16.47664 ? 143 LEU   A C   1 
ATOM   984  O O   . LEU   A 1 136 ? 5.22802   -21.02621 -9.44833  1.000 16.00757 ? 143 LEU   A O   1 
ATOM   985  C CB  . LEU   A 1 136 ? 5.27129   -17.91639 -10.17547 1.000 16.54689 ? 143 LEU   A CB  1 
ATOM   986  C CG  . LEU   A 1 136 ? 6.11312   -16.63252 -10.10644 1.000 14.31095 ? 143 LEU   A CG  1 
ATOM   987  C CD1 . LEU   A 1 136 ? 5.22612   -15.45144 -9.71821  1.000 16.86662 ? 143 LEU   A CD1 1 
ATOM   988  C CD2 . LEU   A 1 136 ? 7.25954   -16.80630 -9.10479  1.000 14.68319 ? 143 LEU   A CD2 1 
ATOM   989  N N   . VAL   A 1 137 ? 4.11987   -20.71695 -11.37734 1.000 14.01967 ? 144 VAL   A N   1 
ATOM   990  C CA  . VAL   A 1 137 ? 3.13379   -21.75304 -11.06834 1.000 14.52554 ? 144 VAL   A CA  1 
ATOM   991  C C   . VAL   A 1 137 ? 3.08285   -22.84049 -12.13013 1.000 16.25143 ? 144 VAL   A C   1 
ATOM   992  O O   . VAL   A 1 137 ? 2.49768   -23.89947 -11.89136 1.000 15.98276 ? 144 VAL   A O   1 
ATOM   993  C CB  . VAL   A 1 137 ? 1.72756   -21.16825 -10.85260 1.000 16.82729 ? 144 VAL   A CB  1 
ATOM   994  C CG1 . VAL   A 1 137 ? 1.70528   -20.21999 -9.64943  1.000 15.05413 ? 144 VAL   A CG1 1 
ATOM   995  C CG2 . VAL   A 1 137 ? 1.18054   -20.45966 -12.15192 1.000 13.49407 ? 144 VAL   A CG2 1 
ATOM   996  N N   . ALA   A 1 138 ? 3.65829   -22.59534 -13.30540 1.000 16.14425 ? 145 ALA   A N   1 
ATOM   997  C CA  . ALA   A 1 138 ? 3.53490   -23.51526 -14.43717 1.000 15.36975 ? 145 ALA   A CA  1 
ATOM   998  C C   . ALA   A 1 138 ? 4.87310   -24.17232 -14.72471 1.000 17.39026 ? 145 ALA   A C   1 
ATOM   999  O O   . ALA   A 1 138 ? 5.90310   -23.49307 -14.77515 1.000 17.33149 ? 145 ALA   A O   1 
ATOM   1000 C CB  . ALA   A 1 138 ? 3.05136   -22.79163 -15.69732 1.000 13.23845 ? 145 ALA   A CB  1 
ATOM   1001 N N   . GLU   A 1 139 ? 4.85263   -25.49039 -14.92822 1.000 18.05207 ? 146 GLU   A N   1 
ATOM   1002 C CA  . GLU   A 1 139 ? 6.03166   -26.20747 -15.39586 1.000 18.65624 ? 146 GLU   A CA  1 
ATOM   1003 C C   . GLU   A 1 139 ? 6.20349   -26.09935 -16.90118 1.000 20.09494 ? 146 GLU   A C   1 
ATOM   1004 O O   . GLU   A 1 139 ? 7.32699   -26.21590 -17.39307 1.000 19.64120 ? 146 GLU   A O   1 
ATOM   1005 C CB  . GLU   A 1 139 ? 5.95441   -27.68125 -14.97560 1.000 23.65667 ? 146 GLU   A CB  1 
ATOM   1006 C CG  . GLU   A 1 139 ? 4.81821   -28.45576 -15.62278 1.000 23.75168 ? 146 GLU   A CG  1 
ATOM   1007 C CD  . GLU   A 1 139 ? 4.65973   -29.86661 -15.06826 1.000 38.70059 ? 146 GLU   A CD  1 
ATOM   1008 O OE1 . GLU   A 1 139 ? 5.35521   -30.22477 -14.08922 1.000 43.04258 ? 146 GLU   A OE1 1 
ATOM   1009 O OE2 . GLU   A 1 139 ? 3.83233   -30.62375 -15.62324 1.000 36.12455 ? 146 GLU   A OE2 1 
ATOM   1010 N N   . LYS   A 1 140 ? 5.11783   -25.86000 -17.62912 1.000 16.17011 ? 147 LYS   A N   1 
ATOM   1011 C CA  . LYS   A 1 140 ? 5.13785   -25.66355 -19.06657 1.000 16.25302 ? 147 LYS   A CA  1 
ATOM   1012 C C   . LYS   A 1 140 ? 4.09700   -24.60564 -19.39052 1.000 14.57302 ? 147 LYS   A C   1 
ATOM   1013 O O   . LYS   A 1 140 ? 3.04731   -24.54322 -18.74553 1.000 15.09016 ? 147 LYS   A O   1 
ATOM   1014 C CB  . LYS   A 1 140 ? 4.83296   -26.96941 -19.80857 1.000 12.91139 ? 147 LYS   A CB  1 
ATOM   1015 C CG  . LYS   A 1 140 ? 4.90930   -26.84757 -21.34262 1.000 15.44603 ? 147 LYS   A CG  1 
ATOM   1016 C CD  . LYS   A 1 140 ? 4.93211   -28.23092 -21.98441 1.000 20.97051 ? 147 LYS   A CD  1 
ATOM   1017 C CE  . LYS   A 1 140 ? 3.52635   -28.75557 -22.15021 1.000 22.03060 ? 147 LYS   A CE  1 
ATOM   1018 N NZ  . LYS   A 1 140 ? 3.52632   -30.17088 -22.62742 1.000 32.18393 ? 147 LYS   A NZ  1 
ATOM   1019 N N   . VAL   A 1 141 ? 4.40088   -23.74662 -20.35309 1.000 13.39121 ? 148 VAL   A N   1 
ATOM   1020 C CA  . VAL   A 1 141 ? 3.45046   -22.74923 -20.82919 1.000 12.17100 ? 148 VAL   A CA  1 
ATOM   1021 C C   . VAL   A 1 141 ? 3.27330   -22.93992 -22.32588 1.000 13.53377 ? 148 VAL   A C   1 
ATOM   1022 O O   . VAL   A 1 141 ? 4.25669   -23.00245 -23.06746 1.000 16.13115 ? 148 VAL   A O   1 
ATOM   1023 C CB  . VAL   A 1 141 ? 3.90670   -21.31720 -20.50910 1.000 15.40643 ? 148 VAL   A CB  1 
ATOM   1024 C CG1 . VAL   A 1 141 ? 2.87753   -20.31345 -21.02746 1.000 16.84064 ? 148 VAL   A CG1 1 
ATOM   1025 C CG2 . VAL   A 1 141 ? 4.12908   -21.14297 -18.98381 1.000 16.87201 ? 148 VAL   A CG2 1 
ATOM   1026 N N   . THR   A 1 142 ? 2.01923   -22.99287 -22.76627 1.000 13.04528 ? 149 THR   A N   1 
ATOM   1027 C CA  . THR   A 1 142 ? 1.68408   -23.08152 -24.18117 1.000 16.13265 ? 149 THR   A CA  1 
ATOM   1028 C C   . THR   A 1 142 ? 0.87702   -21.84458 -24.53862 1.000 17.07101 ? 149 THR   A C   1 
ATOM   1029 O O   . THR   A 1 142 ? -0.09185  -21.50529 -23.84796 1.000 17.67870 ? 149 THR   A O   1 
ATOM   1030 C CB  . THR   A 1 142 ? 0.89523   -24.36780 -24.48879 1.000 14.02584 ? 149 THR   A CB  1 
ATOM   1031 O OG1 . THR   A 1 142 ? 1.58859   -25.51544 -23.97027 1.000 16.92117 ? 149 THR   A OG1 1 
ATOM   1032 C CG2 . THR   A 1 142 ? 0.68737   -24.54617 -26.00145 1.000 15.50885 ? 149 THR   A CG2 1 
ATOM   1033 N N   . VAL   A 1 143 ? 1.28491   -21.14287 -25.58669 1.000 13.10463 ? 150 VAL   A N   1 
ATOM   1034 C CA  . VAL   A 1 143 ? 0.58632   -19.93127 -26.00311 1.000 15.08864 ? 150 VAL   A CA  1 
ATOM   1035 C C   . VAL   A 1 143 ? 0.08732   -20.11698 -27.42945 1.000 14.77698 ? 150 VAL   A C   1 
ATOM   1036 O O   . VAL   A 1 143 ? 0.88684   -20.32389 -28.35878 1.000 17.05483 ? 150 VAL   A O   1 
ATOM   1037 C CB  . VAL   A 1 143 ? 1.47143   -18.68262 -25.88051 1.000 13.63824 ? 150 VAL   A CB  1 
ATOM   1038 C CG1 . VAL   A 1 143 ? 0.67052   -17.44684 -26.30112 1.000 13.54523 ? 150 VAL   A CG1 1 
ATOM   1039 C CG2 . VAL   A 1 143 ? 1.98433   -18.53508 -24.43277 1.000 14.25083 ? 150 VAL   A CG2 1 
ATOM   1040 N N   . ILE   A 1 144 ? -1.23531  -20.06252 -27.60413 1.000 13.46714 ? 151 ILE   A N   1 
ATOM   1041 C CA  . ILE   A 1 144 ? -1.86284  -20.11444 -28.92444 1.000 15.06060 ? 151 ILE   A CA  1 
ATOM   1042 C C   . ILE   A 1 144 ? -2.29098  -18.69800 -29.26990 1.000 16.39933 ? 151 ILE   A C   1 
ATOM   1043 O O   . ILE   A 1 144 ? -2.95025  -18.04051 -28.46063 1.000 15.19448 ? 151 ILE   A O   1 
ATOM   1044 C CB  . ILE   A 1 144 ? -3.07764  -21.06397 -28.95215 1.000 18.16929 ? 151 ILE   A CB  1 
ATOM   1045 C CG1 . ILE   A 1 144 ? -2.81746  -22.37727 -28.21339 1.000 20.45265 ? 151 ILE   A CG1 1 
ATOM   1046 C CG2 . ILE   A 1 144 ? -3.51518  -21.33861 -30.39226 1.000 18.68113 ? 151 ILE   A CG2 1 
ATOM   1047 C CD1 . ILE   A 1 144 ? -1.73974  -23.17163 -28.82744 1.000 21.94519 ? 151 ILE   A CD1 1 
ATOM   1048 N N   . THR   A 1 145 ? -1.93584  -18.21781 -30.46044 1.000 16.20293 ? 152 THR   A N   1 
ATOM   1049 C CA  . THR   A 1 145 ? -2.20078  -16.81184 -30.72293 1.000 14.83649 ? 152 THR   A CA  1 
ATOM   1050 C C   . THR   A 1 145 ? -2.50196  -16.60077 -32.19751 1.000 17.14692 ? 152 THR   A C   1 
ATOM   1051 O O   . THR   A 1 145 ? -1.98622  -17.31318 -33.05853 1.000 17.44986 ? 152 THR   A O   1 
ATOM   1052 C CB  . THR   A 1 145 ? -1.02949  -15.93074 -30.24205 1.000 14.00403 ? 152 THR   A CB  1 
ATOM   1053 O OG1 . THR   A 1 145 ? -1.39347  -14.53972 -30.30801 1.000 15.04553 ? 152 THR   A OG1 1 
ATOM   1054 C CG2 . THR   A 1 145 ? 0.24062   -16.17807 -31.06533 1.000 15.02504 ? 152 THR   A CG2 1 
ATOM   1055 N N   . LYS   A 1 146 ? -3.36294  -15.62446 -32.47918 1.000 18.32235 ? 153 LYS   A N   1 
ATOM   1056 C CA  . LYS   A 1 146 ? -3.71795  -15.29983 -33.85468 1.000 15.68033 ? 153 LYS   A CA  1 
ATOM   1057 C C   . LYS   A 1 146 ? -3.83382  -13.79011 -33.97151 1.000 18.84713 ? 153 LYS   A C   1 
ATOM   1058 O O   . LYS   A 1 146 ? -4.69251  -13.18376 -33.32381 1.000 17.59788 ? 153 LYS   A O   1 
ATOM   1059 C CB  . LYS   A 1 146 ? -5.02519  -15.98298 -34.26756 1.000 16.94733 ? 153 LYS   A CB  1 
ATOM   1060 C CG  . LYS   A 1 146 ? -5.55559  -15.52510 -35.61029 1.000 21.76377 ? 153 LYS   A CG  1 
ATOM   1061 C CD  . LYS   A 1 146 ? -4.78738  -16.20840 -36.74098 1.000 19.82748 ? 153 LYS   A CD  1 
ATOM   1062 C CE  . LYS   A 1 146 ? -5.41131  -15.85638 -38.09903 1.000 21.08271 ? 153 LYS   A CE  1 
ATOM   1063 N NZ  . LYS   A 1 146 ? -5.39182  -14.38919 -38.43148 1.000 23.56082 ? 153 LYS   A NZ  1 
ATOM   1064 N N   . HIS   A 1 147 ? -2.95812  -13.20267 -34.78203 1.000 16.86853 ? 154 HIS   A N   1 
ATOM   1065 C CA  . HIS   A 1 147 ? -2.97333  -11.79840 -35.15581 1.000 17.74686 ? 154 HIS   A CA  1 
ATOM   1066 C C   . HIS   A 1 147 ? -3.61628  -11.65437 -36.53569 1.000 19.38762 ? 154 HIS   A C   1 
ATOM   1067 O O   . HIS   A 1 147 ? -3.53569  -12.56137 -37.36763 1.000 21.85918 ? 154 HIS   A O   1 
ATOM   1068 C CB  . HIS   A 1 147 ? -1.52980  -11.26371 -35.14255 1.000 19.08807 ? 154 HIS   A CB  1 
ATOM   1069 C CG  . HIS   A 1 147 ? -1.41959  -9.78472  -35.30897 1.000 17.56245 ? 154 HIS   A CG  1 
ATOM   1070 N ND1 . HIS   A 1 147 ? -1.57224  -9.15666  -36.52547 1.000 21.88875 ? 154 HIS   A ND1 1 
ATOM   1071 C CD2 . HIS   A 1 147 ? -1.16553  -8.80537  -34.40614 1.000 22.80743 ? 154 HIS   A CD2 1 
ATOM   1072 C CE1 . HIS   A 1 147 ? -1.42147  -7.85336  -36.36659 1.000 25.38743 ? 154 HIS   A CE1 1 
ATOM   1073 N NE2 . HIS   A 1 147 ? -1.17761  -7.61256  -35.08977 1.000 21.59217 ? 154 HIS   A NE2 1 
ATOM   1074 N N   . ASN   A 1 148 ? -4.29668  -10.52463 -36.77041 1.000 21.86424 ? 155 ASN   A N   1 
ATOM   1075 C CA  . ASN   A 1 148 ? -4.97007  -10.33553 -38.05936 1.000 20.77786 ? 155 ASN   A CA  1 
ATOM   1076 C C   . ASN   A 1 148 ? -4.01485  -10.48905 -39.24176 1.000 25.17571 ? 155 ASN   A C   1 
ATOM   1077 O O   . ASN   A 1 148 ? -4.42749  -10.93192 -40.32052 1.000 28.27709 ? 155 ASN   A O   1 
ATOM   1078 C CB  . ASN   A 1 148 ? -5.62488  -8.95355  -38.13072 1.000 21.58031 ? 155 ASN   A CB  1 
ATOM   1079 C CG  . ASN   A 1 148 ? -6.94308  -8.89453  -37.39818 1.000 24.35531 ? 155 ASN   A CG  1 
ATOM   1080 O OD1 . ASN   A 1 148 ? -7.64946  -9.90209  -37.27146 1.000 26.27040 ? 155 ASN   A OD1 1 
ATOM   1081 N ND2 . ASN   A 1 148 ? -7.32089  -7.69102  -36.95730 1.000 21.90817 ? 155 ASN   A ND2 1 
ATOM   1082 N N   . ASP   A 1 149 ? -2.74615  -10.12736 -39.06950 1.000 23.40509 ? 156 ASP   A N   1 
ATOM   1083 C CA  . ASP   A 1 149 ? -1.80086  -10.08046 -40.17521 1.000 29.09955 ? 156 ASP   A CA  1 
ATOM   1084 C C   . ASP   A 1 149 ? -0.97978  -11.36054 -40.32820 1.000 29.32190 ? 156 ASP   A C   1 
ATOM   1085 O O   . ASP   A 1 149 ? -0.11108  -11.42374 -41.20554 1.000 33.96364 ? 156 ASP   A O   1 
ATOM   1086 C CB  . ASP   A 1 149 ? -0.87646  -8.87468  -39.99730 1.000 28.17390 ? 156 ASP   A CB  1 
ATOM   1087 C CG  . ASP   A 1 149 ? -1.61362  -7.54681  -40.15077 1.000 34.39090 ? 156 ASP   A CG  1 
ATOM   1088 O OD1 . ASP   A 1 149 ? -2.77457  -7.51858  -40.63153 1.000 32.20091 ? 156 ASP   A OD1 1 
ATOM   1089 O OD2 . ASP   A 1 149 ? -1.01937  -6.52408  -39.75286 1.000 38.94799 ? 156 ASP   A OD2 1 
ATOM   1090 N N   . ASP   A 1 150 ? -1.25279  -12.39603 -39.53768 1.000 25.93203 ? 157 ASP   A N   1 
ATOM   1091 C CA  . ASP   A 1 150 ? -0.41694  -13.58891 -39.53851 1.000 22.17807 ? 157 ASP   A CA  1 
ATOM   1092 C C   . ASP   A 1 150 ? -1.29115  -14.81876 -39.30216 1.000 21.05352 ? 157 ASP   A C   1 
ATOM   1093 O O   . ASP   A 1 150 ? -2.50544  -14.71926 -39.12933 1.000 23.88784 ? 157 ASP   A O   1 
ATOM   1094 C CB  . ASP   A 1 150 ? 0.70496   -13.44909 -38.50353 1.000 24.22450 ? 157 ASP   A CB  1 
ATOM   1095 C CG  . ASP   A 1 150 ? 1.93329   -14.25649 -38.86578 1.000 24.92407 ? 157 ASP   A CG  1 
ATOM   1096 O OD1 . ASP   A 1 150 ? 1.82283   -15.13893 -39.74702 1.000 24.47685 ? 157 ASP   A OD1 1 
ATOM   1097 O OD2 . ASP   A 1 150 ? 3.01335   -13.97135 -38.29940 1.000 25.91898 ? 157 ASP   A OD2 1 
ATOM   1098 N N   . GLU   A 1 151 ? -0.65913  -15.99237 -39.29871 1.000 27.98717 ? 158 GLU   A N   1 
ATOM   1099 C CA  . GLU   A 1 151 ? -1.34276  -17.26303 -39.10730 1.000 28.00265 ? 158 GLU   A CA  1 
ATOM   1100 C C   . GLU   A 1 151 ? -1.48959  -17.56987 -37.61418 1.000 22.22332 ? 158 GLU   A C   1 
ATOM   1101 O O   . GLU   A 1 151 ? -1.00606  -16.83701 -36.74831 1.000 22.41989 ? 158 GLU   A O   1 
ATOM   1102 C CB  . GLU   A 1 151 ? -0.57206  -18.38163 -39.81057 1.000 30.01480 ? 158 GLU   A CB  1 
ATOM   1103 C CG  . GLU   A 1 151 ? -0.56518  -18.30378 -41.32226 1.000 34.36321 ? 158 GLU   A CG  1 
ATOM   1104 C CD  . GLU   A 1 151 ? -1.95380  -18.39708 -41.90304 1.000 46.67398 ? 158 GLU   A CD  1 
ATOM   1105 O OE1 . GLU   A 1 151 ? -2.61514  -19.43690 -41.69321 1.000 54.82714 ? 158 GLU   A OE1 1 
ATOM   1106 O OE2 . GLU   A 1 151 ? -2.39668  -17.42700 -42.55673 1.000 49.35381 ? 158 GLU   A OE2 1 
ATOM   1107 N N   . GLN   A 1 152 ? -2.16895  -18.67200 -37.29774 1.000 20.74760 ? 159 GLN   A N   1 
ATOM   1108 C CA  . GLN   A 1 152 ? -2.30422  -19.10564 -35.91036 1.000 19.05719 ? 159 GLN   A CA  1 
ATOM   1109 C C   . GLN   A 1 152 ? -1.08897  -19.94093 -35.52635 1.000 19.59904 ? 159 GLN   A C   1 
ATOM   1110 O O   . GLN   A 1 152 ? -0.75010  -20.91066 -36.21987 1.000 23.81775 ? 159 GLN   A O   1 
ATOM   1111 C CB  . GLN   A 1 152 ? -3.59110  -19.90478 -35.70138 1.000 19.74350 ? 159 GLN   A CB  1 
ATOM   1112 C CG  . GLN   A 1 152 ? -3.92835  -20.23254 -34.24280 1.000 17.31718 ? 159 GLN   A CG  1 
ATOM   1113 C CD  . GLN   A 1 152 ? -5.37180  -20.65110 -34.07847 1.000 22.05987 ? 159 GLN   A CD  1 
ATOM   1114 O OE1 . GLN   A 1 152 ? -6.28675  -19.94411 -34.51312 1.000 26.04973 ? 159 GLN   A OE1 1 
ATOM   1115 N NE2 . GLN   A 1 152 ? -5.58930  -21.79574 -33.44184 1.000 23.81178 ? 159 GLN   A NE2 1 
ATOM   1116 N N   . TYR   A 1 153 ? -0.44965  -19.57660 -34.41341 1.000 16.96790 ? 160 TYR   A N   1 
ATOM   1117 C CA  . TYR   A 1 153 ? 0.78433   -20.21369 -33.97629 1.000 19.20286 ? 160 TYR   A CA  1 
ATOM   1118 C C   . TYR   A 1 153 ? 0.63247   -20.75347 -32.56416 1.000 18.29556 ? 160 TYR   A C   1 
ATOM   1119 O O   . TYR   A 1 153 ? -0.14744  -20.22677 -31.75559 1.000 20.03536 ? 160 TYR   A O   1 
ATOM   1120 C CB  . TYR   A 1 153 ? 1.98821   -19.24201 -33.99820 1.000 19.17898 ? 160 TYR   A CB  1 
ATOM   1121 C CG  . TYR   A 1 153 ? 2.35938   -18.77424 -35.37268 1.000 20.26738 ? 160 TYR   A CG  1 
ATOM   1122 C CD1 . TYR   A 1 153 ? 3.06540   -19.58621 -36.24358 1.000 21.33823 ? 160 TYR   A CD1 1 
ATOM   1123 C CD2 . TYR   A 1 153 ? 1.98756   -17.51341 -35.80398 1.000 24.20637 ? 160 TYR   A CD2 1 
ATOM   1124 C CE1 . TYR   A 1 153 ? 3.38495   -19.14789 -37.52564 1.000 24.07404 ? 160 TYR   A CE1 1 
ATOM   1125 C CE2 . TYR   A 1 153 ? 2.29551   -17.06714 -37.06276 1.000 22.51261 ? 160 TYR   A CE2 1 
ATOM   1126 C CZ  . TYR   A 1 153 ? 2.98917   -17.88154 -37.92616 1.000 23.71162 ? 160 TYR   A CZ  1 
ATOM   1127 O OH  . TYR   A 1 153 ? 3.29648   -17.41802 -39.18828 1.000 29.27214 ? 160 TYR   A OH  1 
ATOM   1128 N N   . ALA   A 1 154 ? 1.38341   -21.81545 -32.28074 1.000 17.21431 ? 161 ALA   A N   1 
ATOM   1129 C CA  . ALA   A 1 154 ? 1.57534   -22.31871 -30.92321 1.000 16.93201 ? 161 ALA   A CA  1 
ATOM   1130 C C   . ALA   A 1 154 ? 3.02863   -22.12595 -30.52189 1.000 14.79635 ? 161 ALA   A C   1 
ATOM   1131 O O   . ALA   A 1 154 ? 3.93670   -22.69943 -31.14271 1.000 18.21715 ? 161 ALA   A O   1 
ATOM   1132 C CB  . ALA   A 1 154 ? 1.19564   -23.79626 -30.80753 1.000 18.15118 ? 161 ALA   A CB  1 
ATOM   1133 N N   . TRP   A 1 155 ? 3.23388   -21.33668 -29.47801 1.000 15.96100 ? 162 TRP   A N   1 
ATOM   1134 C CA  . TRP   A 1 155 ? 4.50783   -21.16444 -28.79941 1.000 14.79438 ? 162 TRP   A CA  1 
ATOM   1135 C C   . TRP   A 1 155 ? 4.49443   -22.02658 -27.54058 1.000 15.42781 ? 162 TRP   A C   1 
ATOM   1136 O O   . TRP   A 1 155 ? 3.44417   -22.20779 -26.91900 1.000 15.13982 ? 162 TRP   A O   1 
ATOM   1137 C CB  . TRP   A 1 155 ? 4.69952   -19.67488 -28.46782 1.000 15.33516 ? 162 TRP   A CB  1 
ATOM   1138 C CG  . TRP   A 1 155 ? 5.94122   -19.25443 -27.65275 1.000 10.79421 ? 162 TRP   A CG  1 
ATOM   1139 C CD1 . TRP   A 1 155 ? 7.03743   -18.58021 -28.12045 1.000 13.48339 ? 162 TRP   A CD1 1 
ATOM   1140 C CD2 . TRP   A 1 155 ? 6.15219   -19.41015 -26.23281 1.000 10.98021 ? 162 TRP   A CD2 1 
ATOM   1141 N NE1 . TRP   A 1 155 ? 7.92623   -18.34405 -27.10199 1.000 13.85609 ? 162 TRP   A NE1 1 
ATOM   1142 C CE2 . TRP   A 1 155 ? 7.39500   -18.80582 -25.92915 1.000 14.77691 ? 162 TRP   A CE2 1 
ATOM   1143 C CE3 . TRP   A 1 155 ? 5.40559   -19.98462 -25.19032 1.000 14.03128 ? 162 TRP   A CE3 1 
ATOM   1144 C CZ2 . TRP   A 1 155 ? 7.92845   -18.78841 -24.64271 1.000 13.62911 ? 162 TRP   A CZ2 1 
ATOM   1145 C CZ3 . TRP   A 1 155 ? 5.93525   -19.95728 -23.91145 1.000 16.28716 ? 162 TRP   A CZ3 1 
ATOM   1146 C CH2 . TRP   A 1 155 ? 7.18287   -19.35665 -23.65179 1.000 12.93516 ? 162 TRP   A CH2 1 
ATOM   1147 N N   . GLU   A 1 156 ? 5.64833   -22.60526 -27.18864 1.000 15.11287 ? 163 GLU   A N   1 
ATOM   1148 C CA  . GLU   A 1 156 ? 5.67679   -23.44720 -25.99506 1.000 15.63042 ? 163 GLU   A CA  1 
ATOM   1149 C C   . GLU   A 1 156 ? 7.06324   -23.44102 -25.36307 1.000 16.66021 ? 163 GLU   A C   1 
ATOM   1150 O O   . GLU   A 1 156 ? 8.07398   -23.44459 -26.07289 1.000 15.56071 ? 163 GLU   A O   1 
ATOM   1151 C CB  . GLU   A 1 156 ? 5.27241   -24.88513 -26.34262 1.000 18.49291 ? 163 GLU   A CB  1 
ATOM   1152 C CG  . GLU   A 1 156 ? 4.99021   -25.75148 -25.15878 1.000 17.23056 ? 163 GLU   A CG  1 
ATOM   1153 C CD  . GLU   A 1 156 ? 4.27933   -27.02807 -25.54933 1.000 26.25018 ? 163 GLU   A CD  1 
ATOM   1154 O OE1 . GLU   A 1 156 ? 4.91993   -27.92917 -26.13407 1.000 23.84258 ? 163 GLU   A OE1 1 
ATOM   1155 O OE2 . GLU   A 1 156 ? 3.07251   -27.13345 -25.27403 1.000 26.84166 ? 163 GLU   A OE2 1 
ATOM   1156 N N   . SER   A 1 157 ? 7.11199   -23.47034 -24.02999 1.000 13.48607 ? 164 SER   A N   1 
ATOM   1157 C CA  . SER   A 1 157 ? 8.39860   -23.61982 -23.35775 1.000 15.02831 ? 164 SER   A CA  1 
ATOM   1158 C C   . SER   A 1 157 ? 8.21141   -24.24218 -21.98344 1.000 11.44160 ? 164 SER   A C   1 
ATOM   1159 O O   . SER   A 1 157 ? 7.29761   -23.86565 -21.24488 1.000 15.48300 ? 164 SER   A O   1 
ATOM   1160 C CB  . SER   A 1 157 ? 9.13027   -22.27546 -23.22119 1.000 14.11937 ? 164 SER   A CB  1 
ATOM   1161 O OG  . SER   A 1 157 ? 10.39596  -22.49933 -22.61301 1.000 13.56830 ? 164 SER   A OG  1 
ATOM   1162 N N   . SER   A 1 158 ? 9.07285   -25.20786 -21.65635 1.000 15.97466 ? 165 SER   A N   1 
ATOM   1163 C CA  . SER   A 1 158 ? 9.24674   -25.68196 -20.28974 1.000 16.13543 ? 165 SER   A CA  1 
ATOM   1164 C C   . SER   A 1 158 ? 10.50735  -25.09373 -19.66000 1.000 15.67648 ? 165 SER   A C   1 
ATOM   1165 O O   . SER   A 1 158 ? 11.13131  -25.72378 -18.79680 1.000 19.49514 ? 165 SER   A O   1 
ATOM   1166 C CB  . SER   A 1 158 ? 9.29409   -27.21136 -20.23654 1.000 21.87041 ? 165 SER   A CB  1 
ATOM   1167 O OG  . SER   A 1 158 ? 8.11176   -27.78542 -20.77423 1.000 19.12188 ? 165 SER   A OG  1 
ATOM   1168 N N   . ALA   A 1 159 ? 10.91389  -23.90855 -20.10556 1.000 14.83680 ? 166 ALA   A N   1 
ATOM   1169 C CA  . ALA   A 1 159 ? 12.13739  -23.23181 -19.64673 1.000 17.02996 ? 166 ALA   A CA  1 
ATOM   1170 C C   . ALA   A 1 159 ? 13.33706  -24.08782 -20.05340 1.000 21.37358 ? 166 ALA   A C   1 
ATOM   1171 O O   . ALA   A 1 159 ? 13.32025  -24.75572 -21.09544 1.000 20.90900 ? 166 ALA   A O   1 
ATOM   1172 C CB  . ALA   A 1 159 ? 12.05436  -22.91482 -18.14647 1.000 19.20337 ? 166 ALA   A CB  1 
ATOM   1173 N N   . GLY   A 1 160 ? 14.41130  -24.05447 -19.27239 1.000 18.49173 ? 167 GLY   A N   1 
ATOM   1174 C CA  . GLY   A 1 160 ? 15.60112  -24.78233 -19.66817 1.000 21.97951 ? 167 GLY   A CA  1 
ATOM   1175 C C   . GLY   A 1 160 ? 16.34368  -24.20639 -20.84904 1.000 19.65779 ? 167 GLY   A C   1 
ATOM   1176 O O   . GLY   A 1 160 ? 17.22964  -24.87156 -21.39038 1.000 22.93315 ? 167 GLY   A O   1 
ATOM   1177 N N   . GLY   A 1 161 ? 15.99920  -23.00026 -21.28354 1.000 17.73960 ? 168 GLY   A N   1 
ATOM   1178 C CA  . GLY   A 1 161 ? 16.79728  -22.28858 -22.25775 1.000 21.25492 ? 168 GLY   A CA  1 
ATOM   1179 C C   . GLY   A 1 161 ? 16.23716  -22.28207 -23.65879 1.000 20.16410 ? 168 GLY   A C   1 
ATOM   1180 O O   . GLY   A 1 161 ? 16.81634  -21.62400 -24.53103 1.000 18.21899 ? 168 GLY   A O   1 
ATOM   1181 N N   . SER   A 1 162 ? 15.13970  -22.99333 -23.91066 1.000 18.28320 ? 169 SER   A N   1 
ATOM   1182 C CA  . SER   A 1 162 ? 14.64087  -23.11790 -25.27143 1.000 14.78136 ? 169 SER   A CA  1 
ATOM   1183 C C   . SER   A 1 162 ? 13.11618  -23.02488 -25.30735 1.000 13.64563 ? 169 SER   A C   1 
ATOM   1184 O O   . SER   A 1 162 ? 12.42060  -23.24305 -24.30922 1.000 15.63215 ? 169 SER   A O   1 
ATOM   1185 C CB  . SER   A 1 162 ? 15.12380  -24.42251 -25.91775 1.000 17.59099 ? 169 SER   A CB  1 
ATOM   1186 O OG  . SER   A 1 162 ? 14.43578  -25.52064 -25.36352 1.000 20.24815 ? 169 SER   A OG  1 
ATOM   1187 N N   . PHE   A 1 163 ? 12.60382  -22.68863 -26.48998 1.000 16.06242 ? 170 PHE   A N   1 
ATOM   1188 C CA  . PHE   A 1 163 ? 11.17062  -22.66574 -26.73742 1.000 13.90491 ? 170 PHE   A CA  1 
ATOM   1189 C C   . PHE   A 1 163 ? 10.94733  -23.13341 -28.16699 1.000 17.53729 ? 170 PHE   A C   1 
ATOM   1190 O O   . PHE   A 1 163 ? 11.87396  -23.17706 -28.98006 1.000 15.77772 ? 170 PHE   A O   1 
ATOM   1191 C CB  . PHE   A 1 163 ? 10.55631  -21.26212 -26.49067 1.000 14.59495 ? 170 PHE   A CB  1 
ATOM   1192 C CG  . PHE   A 1 163 ? 11.07176  -20.19287 -27.42924 1.000 17.29206 ? 170 PHE   A CG  1 
ATOM   1193 C CD1 . PHE   A 1 163 ? 12.21425  -19.46942 -27.12069 1.000 16.91851 ? 170 PHE   A CD1 1 
ATOM   1194 C CD2 . PHE   A 1 163 ? 10.37956  -19.88598 -28.61435 1.000 16.74220 ? 170 PHE   A CD2 1 
ATOM   1195 C CE1 . PHE   A 1 163 ? 12.69426  -18.47890 -27.98792 1.000 17.85653 ? 170 PHE   A CE1 1 
ATOM   1196 C CE2 . PHE   A 1 163 ? 10.84885  -18.90270 -29.48807 1.000 18.97720 ? 170 PHE   A CE2 1 
ATOM   1197 C CZ  . PHE   A 1 163 ? 12.00204  -18.19527 -29.17581 1.000 17.20262 ? 170 PHE   A CZ  1 
ATOM   1198 N N   . THR   A 1 164 ? 9.71891   -23.53826 -28.44731 1.000 14.07363 ? 171 THR   A N   1 
ATOM   1199 C CA  . THR   A 1 164 ? 9.33335   -23.97357 -29.77677 1.000 14.83527 ? 171 THR   A CA  1 
ATOM   1200 C C   . THR   A 1 164 ? 8.19211   -23.11761 -30.29812 1.000 16.09157 ? 171 THR   A C   1 
ATOM   1201 O O   . THR   A 1 164 ? 7.42118   -22.52734 -29.53250 1.000 17.07824 ? 171 THR   A O   1 
ATOM   1202 C CB  . THR   A 1 164 ? 8.87577   -25.43285 -29.80474 1.000 15.37946 ? 171 THR   A CB  1 
ATOM   1203 O OG1 . THR   A 1 164 ? 7.68146   -25.55174 -29.02038 1.000 18.93563 ? 171 THR   A OG1 1 
ATOM   1204 C CG2 . THR   A 1 164 ? 9.95516   -26.40985 -29.32563 1.000 16.09818 ? 171 THR   A CG2 1 
ATOM   1205 N N   . VAL   A 1 165 ? 8.09513   -23.08374 -31.62821 1.000 15.50300 ? 172 VAL   A N   1 
ATOM   1206 C CA  . VAL   A 1 165 ? 7.02824   -22.40821 -32.36233 1.000 17.24371 ? 172 VAL   A CA  1 
ATOM   1207 C C   . VAL   A 1 165 ? 6.62136   -23.31027 -33.51949 1.000 20.32955 ? 172 VAL   A C   1 
ATOM   1208 O O   . VAL   A 1 165 ? 7.47993   -23.84534 -34.23430 1.000 19.14695 ? 172 VAL   A O   1 
ATOM   1209 C CB  . VAL   A 1 165 ? 7.46367   -21.01721 -32.88093 1.000 19.60576 ? 172 VAL   A CB  1 
ATOM   1210 C CG1 . VAL   A 1 165 ? 6.35686   -20.35816 -33.72162 1.000 20.31615 ? 172 VAL   A CG1 1 
ATOM   1211 C CG2 . VAL   A 1 165 ? 7.87688   -20.12371 -31.72300 1.000 18.39080 ? 172 VAL   A CG2 1 
ATOM   1212 N N   . ARG   A 1 166 ? 5.31197   -23.48637 -33.69316 1.000 18.63876 ? 173 ARG   A N   1 
ATOM   1213 C CA  . ARG   A 1 166 ? 4.78083   -24.20826 -34.83780 1.000 23.04622 ? 173 ARG   A CA  1 
ATOM   1214 C C   . ARG   A 1 166 ? 3.45890   -23.58000 -35.25667 1.000 22.15334 ? 173 ARG   A C   1 
ATOM   1215 O O   . ARG   A 1 166 ? 2.79218   -22.89233 -34.47249 1.000 20.93463 ? 173 ARG   A O   1 
ATOM   1216 C CB  . ARG   A 1 166 ? 4.57944   -25.69788 -34.52794 1.000 24.90349 ? 173 ARG   A CB  1 
ATOM   1217 C CG  . ARG   A 1 166 ? 3.65401   -25.92931 -33.35205 1.000 27.07251 ? 173 ARG   A CG  1 
ATOM   1218 C CD  . ARG   A 1 166 ? 4.15457   -27.07400 -32.52041 1.000 32.32713 ? 173 ARG   A CD  1 
ATOM   1219 N NE  . ARG   A 1 166 ? 3.57124   -27.09999 -31.18453 1.000 45.79216 ? 173 ARG   A NE  1 
ATOM   1220 C CZ  . ARG   A 1 166 ? 3.93932   -26.33443 -30.15790 1.000 46.97582 ? 173 ARG   A CZ  1 
ATOM   1221 N NH1 . ARG   A 1 166 ? 4.91568   -25.42579 -30.26679 1.000 24.08977 ? 173 ARG   A NH1 1 
ATOM   1222 N NH2 . ARG   A 1 166 ? 3.29385   -26.46085 -28.99493 1.000 32.33971 ? 173 ARG   A NH2 1 
ATOM   1223 N N   . THR   A 1 167 ? 3.08080   -23.83542 -36.50645 1.000 23.92812 ? 174 THR   A N   1 
ATOM   1224 C CA  . THR   A 1 167 ? 1.74228   -23.47870 -36.95066 1.000 24.15542 ? 174 THR   A CA  1 
ATOM   1225 C C   . THR   A 1 167 ? 0.72870   -24.35649 -36.23034 1.000 27.13273 ? 174 THR   A C   1 
ATOM   1226 O O   . THR   A 1 167 ? 0.91590   -25.57296 -36.12335 1.000 35.29357 ? 174 THR   A O   1 
ATOM   1227 C CB  . THR   A 1 167 ? 1.63475   -23.64537 -38.46333 1.000 30.75606 ? 174 THR   A CB  1 
ATOM   1228 O OG1 . THR   A 1 167 ? 2.67152   -22.88169 -39.09529 1.000 34.11450 ? 174 THR   A OG1 1 
ATOM   1229 C CG2 . THR   A 1 167 ? 0.28372   -23.19199 -38.96563 1.000 31.23135 ? 174 THR   A CG2 1 
ATOM   1230 N N   . ASP   A 1 168 ? -0.33318  -23.74532 -35.70847 1.000 24.98025 ? 175 ASP   A N   1 
ATOM   1231 C CA  . ASP   A 1 168 ? -1.29600  -24.47031 -34.89035 1.000 30.32819 ? 175 ASP   A CA  1 
ATOM   1232 C C   . ASP   A 1 168 ? -2.39792  -25.04379 -35.76958 1.000 36.05627 ? 175 ASP   A C   1 
ATOM   1233 O O   . ASP   A 1 168 ? -3.10304  -24.29411 -36.45390 1.000 37.48620 ? 175 ASP   A O   1 
ATOM   1234 C CB  . ASP   A 1 168 ? -1.90331  -23.56521 -33.82546 1.000 27.98373 ? 175 ASP   A CB  1 
ATOM   1235 C CG  . ASP   A 1 168 ? -2.86522  -24.30668 -32.92870 1.000 29.85259 ? 175 ASP   A CG  1 
ATOM   1236 O OD1 . ASP   A 1 168 ? -2.54325  -25.44146 -32.51787 1.000 42.89759 ? 175 ASP   A OD1 1 
ATOM   1237 O OD2 . ASP   A 1 168 ? -3.94566  -23.76396 -32.64322 1.000 35.91748 ? 175 ASP   A OD2 1 
ATOM   1238 N N   . THR   A 1 169 ? -2.55630  -26.36766 -35.72890 1.000 38.52814 ? 176 THR   A N   1 
ATOM   1239 C CA  . THR   A 1 169 ? -3.57254  -27.06287 -36.50784 1.000 48.50849 ? 176 THR   A CA  1 
ATOM   1240 C C   . THR   A 1 169 ? -4.90552  -27.17843 -35.78046 1.000 47.11753 ? 176 THR   A C   1 
ATOM   1241 O O   . THR   A 1 169 ? -5.88268  -27.64077 -36.38150 1.000 48.95765 ? 176 THR   A O   1 
ATOM   1242 C CB  . THR   A 1 169 ? -3.08582  -28.47242 -36.88805 1.000 44.64027 ? 176 THR   A CB  1 
ATOM   1243 O OG1 . THR   A 1 169 ? -2.73871  -29.20260 -35.70138 1.000 50.22939 ? 176 THR   A OG1 1 
ATOM   1244 C CG2 . THR   A 1 169 ? -1.87647  -28.39316 -37.80853 1.000 45.61693 ? 176 THR   A CG2 1 
ATOM   1245 N N   . GLY   A 1 170 ? -4.96888  -26.76638 -34.51554 1.000 44.23018 ? 177 GLY   A N   1 
ATOM   1246 C CA  . GLY   A 1 170 ? -6.15335  -26.96116 -33.70370 1.000 44.36499 ? 177 GLY   A CA  1 
ATOM   1247 C C   . GLY   A 1 170 ? -7.33627  -26.07278 -34.03650 1.000 40.64802 ? 177 GLY   A C   1 
ATOM   1248 O O   . GLY   A 1 170 ? -7.45867  -25.55499 -35.15109 1.000 42.67552 ? 177 GLY   A O   1 
ATOM   1249 N N   . GLU   A 1 171 ? -8.21993  -25.90790 -33.06394 1.000 41.97180 ? 178 GLU   A N   1 
ATOM   1250 C CA  . GLU   A 1 171 ? -9.42856  -25.12550 -33.25983 1.000 42.87511 ? 178 GLU   A CA  1 
ATOM   1251 C C   . GLU   A 1 171 ? -9.05962  -23.67683 -33.58464 1.000 38.72922 ? 178 GLU   A C   1 
ATOM   1252 O O   . GLU   A 1 171 ? -8.27964  -23.06311 -32.84493 1.000 35.52990 ? 178 GLU   A O   1 
ATOM   1253 C CB  . GLU   A 1 171 ? -10.28679 -25.21142 -31.99167 1.000 39.26832 ? 178 GLU   A CB  1 
ATOM   1254 C CG  . GLU   A 1 171 ? -11.66782 -24.59245 -32.08343 1.000 43.59797 ? 178 GLU   A CG  1 
ATOM   1255 C CD  . GLU   A 1 171 ? -12.70309 -25.52262 -32.72658 1.000 51.58481 ? 178 GLU   A CD  1 
ATOM   1256 O OE1 . GLU   A 1 171 ? -12.92858 -26.64063 -32.20562 1.000 48.15291 ? 178 GLU   A OE1 1 
ATOM   1257 O OE2 . GLU   A 1 171 ? -13.30987 -25.13664 -33.74979 1.000 42.86011 ? 178 GLU   A OE2 1 
ATOM   1258 N N   . PRO   A 1 172 ? -9.55013  -23.11475 -34.69145 1.000 33.53736 ? 179 PRO   A N   1 
ATOM   1259 C CA  . PRO   A 1 172 ? -9.22269  -21.71705 -35.01297 1.000 33.81353 ? 179 PRO   A CA  1 
ATOM   1260 C C   . PRO   A 1 172 ? -9.79398  -20.75709 -33.97589 1.000 35.77902 ? 179 PRO   A C   1 
ATOM   1261 O O   . PRO   A 1 172 ? -10.90734 -20.94529 -33.47765 1.000 40.20057 ? 179 PRO   A O   1 
ATOM   1262 C CB  . PRO   A 1 172 ? -9.87055  -21.50802 -36.38324 1.000 38.98573 ? 179 PRO   A CB  1 
ATOM   1263 C CG  . PRO   A 1 172 ? -9.97906  -22.90266 -36.96998 1.000 34.29807 ? 179 PRO   A CG  1 
ATOM   1264 C CD  . PRO   A 1 172 ? -10.26141 -23.79106 -35.79145 1.000 38.74049 ? 179 PRO   A CD  1 
ATOM   1265 N N   . MET   A 1 173 ? -9.02744  -19.70046 -33.67429 1.000 28.83860 ? 180 MET   A N   1 
ATOM   1266 C CA  . MET   A 1 173 ? -9.37862  -18.76062 -32.61510 1.000 29.22506 ? 180 MET   A CA  1 
ATOM   1267 C C   . MET   A 1 173 ? -10.02752 -17.47469 -33.10180 1.000 32.22135 ? 180 MET   A C   1 
ATOM   1268 O O   . MET   A 1 173 ? -10.56534 -16.72348 -32.27658 1.000 34.33897 ? 180 MET   A O   1 
ATOM   1269 C CB  . MET   A 1 173 ? -8.14228  -18.34384 -31.82010 1.000 26.78143 ? 180 MET   A CB  1 
ATOM   1270 C CG  . MET   A 1 173 ? -7.56889  -19.38206 -30.89788 1.000 40.72120 ? 180 MET   A CG  1 
ATOM   1271 S SD  . MET   A 1 173 ? -5.92669  -18.81438 -30.43615 1.000 36.46898 ? 180 MET   A SD  1 
ATOM   1272 C CE  . MET   A 1 173 ? -6.36196  -17.22860 -29.76508 1.000 25.87429 ? 180 MET   A CE  1 
ATOM   1273 N N   . GLY   A 1 174 ? -9.94104  -17.16807 -34.38572 1.000 30.19301 ? 181 GLY   A N   1 
ATOM   1274 C CA  . GLY   A 1 174 ? -10.41224 -15.87956 -34.85572 1.000 25.41922 ? 181 GLY   A CA  1 
ATOM   1275 C C   . GLY   A 1 174 ? -9.35026  -14.81351 -34.69704 1.000 26.70565 ? 181 GLY   A C   1 
ATOM   1276 O O   . GLY   A 1 174 ? -8.76005  -14.35478 -35.67748 1.000 26.65552 ? 181 GLY   A O   1 
ATOM   1277 N N   . ARG   A 1 175 ? -9.09021  -14.43158 -33.44927 1.000 24.29889 ? 182 ARG   A N   1 
ATOM   1278 C CA  . ARG   A 1 175 ? -8.11945  -13.40208 -33.10825 1.000 17.52488 ? 182 ARG   A CA  1 
ATOM   1279 C C   . ARG   A 1 175 ? -7.92817  -13.42389 -31.60049 1.000 16.61665 ? 182 ARG   A C   1 
ATOM   1280 O O   . ARG   A 1 175 ? -8.90902  -13.52812 -30.85530 1.000 22.88706 ? 182 ARG   A O   1 
ATOM   1281 C CB  . ARG   A 1 175 ? -8.59058  -12.00418 -33.56218 1.000 22.20001 ? 182 ARG   A CB  1 
ATOM   1282 C CG  . ARG   A 1 175 ? -7.50132  -10.93694 -33.46892 1.000 20.13959 ? 182 ARG   A CG  1 
ATOM   1283 C CD  . ARG   A 1 175 ? -8.08625  -9.51903  -33.40468 1.000 20.08018 ? 182 ARG   A CD  1 
ATOM   1284 N NE  . ARG   A 1 175 ? -9.02298  -9.35296  -32.29501 1.000 19.15995 ? 182 ARG   A NE  1 
ATOM   1285 C CZ  . ARG   A 1 175 ? -10.33367 -9.20141  -32.43140 1.000 19.64975 ? 182 ARG   A CZ  1 
ATOM   1286 N NH1 . ARG   A 1 175 ? -10.91220 -9.17790  -33.62459 1.000 21.29784 ? 182 ARG   A NH1 1 
ATOM   1287 N NH2 . ARG   A 1 175 ? -11.08505 -9.05467  -31.34164 1.000 19.68122 ? 182 ARG   A NH2 1 
ATOM   1288 N N   . GLY   A 1 176 ? -6.68021  -13.35076 -31.15898 1.000 15.26853 ? 183 GLY   A N   1 
ATOM   1289 C CA  . GLY   A 1 176 ? -6.42296  -13.17112 -29.74687 1.000 14.89392 ? 183 GLY   A CA  1 
ATOM   1290 C C   . GLY   A 1 176 ? -5.33881  -14.10642 -29.27277 1.000 19.18438 ? 183 GLY   A C   1 
ATOM   1291 O O   . GLY   A 1 176 ? -4.53682  -14.61207 -30.06588 1.000 19.32301 ? 183 GLY   A O   1 
ATOM   1292 N N   . THR   A 1 177 ? -5.31983  -14.36162 -27.96248 1.000 15.03807 ? 184 THR   A N   1 
ATOM   1293 C CA  . THR   A 1 177 ? -4.26254  -15.16642 -27.35644 1.000 15.05305 ? 184 THR   A CA  1 
ATOM   1294 C C   . THR   A 1 177 ? -4.82343  -16.07746 -26.27127 1.000 14.76037 ? 184 THR   A C   1 
ATOM   1295 O O   . THR   A 1 177 ? -5.68744  -15.67056 -25.49132 1.000 16.42161 ? 184 THR   A O   1 
ATOM   1296 C CB  . THR   A 1 177 ? -3.13326  -14.26861 -26.77574 1.000 13.76815 ? 184 THR   A CB  1 
ATOM   1297 O OG1 . THR   A 1 177 ? -2.52634  -13.49326 -27.81518 1.000 17.34185 ? 184 THR   A OG1 1 
ATOM   1298 C CG2 . THR   A 1 177 ? -2.07060  -15.09509 -26.09534 1.000 17.99901 ? 184 THR   A CG2 1 
ATOM   1299 N N   . LYS   A 1 178 ? -4.34018  -17.32240 -26.24659 1.000 14.97866 ? 185 LYS   A N   1 
ATOM   1300 C CA  . LYS   A 1 178 ? -4.63425  -18.28422 -25.18952 1.000 16.61779 ? 185 LYS   A CA  1 
ATOM   1301 C C   . LYS   A 1 178 ? -3.32513  -18.63736 -24.50776 1.000 15.43011 ? 185 LYS   A C   1 
ATOM   1302 O O   . LYS   A 1 178 ? -2.42620  -19.18195 -25.15674 1.000 16.36549 ? 185 LYS   A O   1 
ATOM   1303 C CB  . LYS   A 1 178 ? -5.25474  -19.56399 -25.76219 1.000 21.36114 ? 185 LYS   A CB  1 
ATOM   1304 C CG  . LYS   A 1 178 ? -6.69124  -19.46913 -26.15443 1.000 27.58688 ? 185 LYS   A CG  1 
ATOM   1305 C CD  . LYS   A 1 178 ? -7.34154  -20.86357 -26.12141 1.000 29.42891 ? 185 LYS   A CD  1 
ATOM   1306 C CE  . LYS   A 1 178 ? -7.77876  -21.29561 -27.51405 1.000 43.93392 ? 185 LYS   A CE  1 
ATOM   1307 N NZ  . LYS   A 1 178 ? -9.16455  -20.79954 -27.82640 1.000 43.30776 ? 185 LYS   A NZ  1 
ATOM   1308 N N   . VAL   A 1 179 ? -3.20296  -18.33650 -23.21739 1.000 13.71207 ? 186 VAL   A N   1 
ATOM   1309 C CA  . VAL   A 1 179 ? -2.04137  -18.74794 -22.43403 1.000 15.71654 ? 186 VAL   A CA  1 
ATOM   1310 C C   . VAL   A 1 179 ? -2.47128  -19.96034 -21.61894 1.000 14.50912 ? 186 VAL   A C   1 
ATOM   1311 O O   . VAL   A 1 179 ? -3.32058  -19.84159 -20.72850 1.000 16.08816 ? 186 VAL   A O   1 
ATOM   1312 C CB  . VAL   A 1 179 ? -1.53373  -17.62811 -21.51396 1.000 11.89233 ? 186 VAL   A CB  1 
ATOM   1313 C CG1 . VAL   A 1 179 ? -0.40365  -18.14755 -20.63894 1.000 12.84795 ? 186 VAL   A CG1 1 
ATOM   1314 C CG2 . VAL   A 1 179 ? -1.08839  -16.41184 -22.30404 1.000 12.22052 ? 186 VAL   A CG2 1 
ATOM   1315 N N   . ILE   A 1 180 ? -1.90125  -21.12379 -21.91960 1.000 12.60634 ? 187 ILE   A N   1 
ATOM   1316 C CA  . ILE   A 1 180 ? -2.23424  -22.37569 -21.24984 1.000 17.66064 ? 187 ILE   A CA  1 
ATOM   1317 C C   . ILE   A 1 180 ? -1.13455  -22.67720 -20.24072 1.000 13.41358 ? 187 ILE   A C   1 
ATOM   1318 O O   . ILE   A 1 180 ? 0.00557   -22.99992 -20.61165 1.000 16.33768 ? 187 ILE   A O   1 
ATOM   1319 C CB  . ILE   A 1 180 ? -2.38374  -23.53381 -22.24478 1.000 17.11785 ? 187 ILE   A CB  1 
ATOM   1320 C CG1 . ILE   A 1 180 ? -3.36298  -23.15308 -23.35085 1.000 17.24785 ? 187 ILE   A CG1 1 
ATOM   1321 C CG2 . ILE   A 1 180 ? -2.76745  -24.82060 -21.51970 1.000 17.03955 ? 187 ILE   A CG2 1 
ATOM   1322 C CD1 . ILE   A 1 180 ? -3.34139  -24.13149 -24.52447 1.000 19.75587 ? 187 ILE   A CD1 1 
ATOM   1323 N N   . LEU   A 1 181 ? -1.48573  -22.60032 -18.96369 1.000 12.93358 ? 188 LEU   A N   1 
ATOM   1324 C CA  . LEU   A 1 181 ? -0.56349  -22.88068 -17.87335 1.000 15.82053 ? 188 LEU   A CA  1 
ATOM   1325 C C   . LEU   A 1 181 ? -0.69289  -24.34121 -17.46985 1.000 15.03230 ? 188 LEU   A C   1 
ATOM   1326 O O   . LEU   A 1 181 ? -1.71417  -24.74509 -16.90928 1.000 14.86976 ? 188 LEU   A O   1 
ATOM   1327 C CB  . LEU   A 1 181 ? -0.86143  -21.98047 -16.68421 1.000 12.79433 ? 188 LEU   A CB  1 
ATOM   1328 C CG  . LEU   A 1 181 ? -0.82566  -20.48563 -16.99109 1.000 11.41966 ? 188 LEU   A CG  1 
ATOM   1329 C CD1 . LEU   A 1 181 ? -1.21593  -19.67797 -15.77203 1.000 15.78081 ? 188 LEU   A CD1 1 
ATOM   1330 C CD2 . LEU   A 1 181 ? 0.56481   -20.09079 -17.49833 1.000 12.76088 ? 188 LEU   A CD2 1 
ATOM   1331 N N   . HIS   A 1 182 ? 0.34627   -25.12978 -17.73828 1.000 14.22735 ? 189 HIS   A N   1 
ATOM   1332 C CA  . HIS   A 1 182 ? 0.40487   -26.50341 -17.24343 1.000 16.78324 ? 189 HIS   A CA  1 
ATOM   1333 C C   . HIS   A 1 182 ? 0.98022   -26.42738 -15.83781 1.000 15.80708 ? 189 HIS   A C   1 
ATOM   1334 O O   . HIS   A 1 182 ? 2.18867   -26.25335 -15.65522 1.000 17.16560 ? 189 HIS   A O   1 
ATOM   1335 C CB  . HIS   A 1 182 ? 1.23374   -27.39367 -18.16616 1.000 19.86980 ? 189 HIS   A CB  1 
ATOM   1336 C CG  . HIS   A 1 182 ? 0.78903   -27.35837 -19.59711 1.000 18.82280 ? 189 HIS   A CG  1 
ATOM   1337 N ND1 . HIS   A 1 182 ? -0.04918  -28.30914 -20.13878 1.000 23.55709 ? 189 HIS   A ND1 1 
ATOM   1338 C CD2 . HIS   A 1 182 ? 1.06425   -26.48375 -20.59542 1.000 21.86466 ? 189 HIS   A CD2 1 
ATOM   1339 C CE1 . HIS   A 1 182 ? -0.26851  -28.02329 -21.41079 1.000 21.27347 ? 189 HIS   A CE1 1 
ATOM   1340 N NE2 . HIS   A 1 182 ? 0.40306   -26.92569 -21.71373 1.000 23.07063 ? 189 HIS   A NE2 1 
ATOM   1341 N N   . LEU   A 1 183 ? 0.10264   -26.51599 -14.84542 1.000 16.67695 ? 190 LEU   A N   1 
ATOM   1342 C CA  . LEU   A 1 183 ? 0.46589   -26.16186 -13.48340 1.000 17.75780 ? 190 LEU   A CA  1 
ATOM   1343 C C   . LEU   A 1 183 ? 1.40088   -27.18301 -12.84907 1.000 18.72800 ? 190 LEU   A C   1 
ATOM   1344 O O   . LEU   A 1 183 ? 1.32344   -28.39458 -13.10035 1.000 19.74706 ? 190 LEU   A O   1 
ATOM   1345 C CB  . LEU   A 1 183 ? -0.78973  -26.00710 -12.62154 1.000 15.76380 ? 190 LEU   A CB  1 
ATOM   1346 C CG  . LEU   A 1 183 ? -1.75240  -24.87252 -13.00699 1.000 15.70868 ? 190 LEU   A CG  1 
ATOM   1347 C CD1 . LEU   A 1 183 ? -2.98774  -24.90269 -12.10617 1.000 16.88383 ? 190 LEU   A CD1 1 
ATOM   1348 C CD2 . LEU   A 1 183 ? -1.07764  -23.51639 -12.97247 1.000 15.59020 ? 190 LEU   A CD2 1 
ATOM   1349 N N   . LYS   A 1 184 ? 2.29155   -26.67341 -12.00040 1.000 18.41351 ? 191 LYS   A N   1 
ATOM   1350 C CA  . LYS   A 1 184 ? 3.11392   -27.56136 -11.19228 1.000 19.78036 ? 191 LYS   A CA  1 
ATOM   1351 C C   . LYS   A 1 184 ? 2.21889   -28.35613 -10.24947 1.000 22.89652 ? 191 LYS   A C   1 
ATOM   1352 O O   . LYS   A 1 184 ? 1.12519   -27.90517 -9.87666  1.000 20.85559 ? 191 LYS   A O   1 
ATOM   1353 C CB  . LYS   A 1 184 ? 4.13986   -26.76412 -10.38614 1.000 23.26776 ? 191 LYS   A CB  1 
ATOM   1354 C CG  . LYS   A 1 184 ? 5.27037   -26.15979 -11.19448 1.000 22.77221 ? 191 LYS   A CG  1 
ATOM   1355 C CD  . LYS   A 1 184 ? 6.15438   -25.27826 -10.30608 1.000 25.79034 ? 191 LYS   A CD  1 
ATOM   1356 C CE  . LYS   A 1 184 ? 6.12578   -23.81038 -10.71270 1.000 31.74499 ? 191 LYS   A CE  1 
ATOM   1357 N NZ  . LYS   A 1 184 ? 7.44705   -23.10337 -10.46715 1.000 34.60310 ? 191 LYS   A NZ  1 
ATOM   1358 N N   . GLU   A 1 185 ? 2.71676   -29.53734 -9.85224  1.000 24.77568 ? 192 GLU   A N   1 
ATOM   1359 C CA  . GLU   A 1 185 ? 1.95609   -30.49003 -9.04219  1.000 27.64012 ? 192 GLU   A CA  1 
ATOM   1360 C C   . GLU   A 1 185 ? 1.45433   -29.88135 -7.73799  1.000 30.20569 ? 192 GLU   A C   1 
ATOM   1361 O O   . GLU   A 1 185 ? 0.38487   -30.26513 -7.24980  1.000 28.03315 ? 192 GLU   A O   1 
ATOM   1362 C CB  . GLU   A 1 185 ? 2.81460   -31.72598 -8.75214  1.000 30.60193 ? 192 GLU   A CB  1 
ATOM   1363 C CG  . GLU   A 1 185 ? 2.03494   -32.91629 -8.27224  1.000 42.90259 ? 192 GLU   A CG  1 
ATOM   1364 C CD  . GLU   A 1 185 ? 2.83315   -34.19839 -8.37908  1.000 56.32870 ? 192 GLU   A CD  1 
ATOM   1365 O OE1 . GLU   A 1 185 ? 2.21001   -35.27550 -8.49210  1.000 59.44650 ? 192 GLU   A OE1 1 
ATOM   1366 O OE2 . GLU   A 1 185 ? 4.08044   -34.13531 -8.34777  1.000 60.22073 ? 192 GLU   A OE2 1 
ATOM   1367 N N   . ASP   A 1 186 ? 2.20041   -28.94709 -7.15403  1.000 23.98097 ? 193 ASP   A N   1 
ATOM   1368 C CA  . ASP   A 1 186 ? 1.82791   -28.36475 -5.87314  1.000 24.66613 ? 193 ASP   A CA  1 
ATOM   1369 C C   . ASP   A 1 186 ? 1.14749   -27.01346 -6.02723  1.000 23.75389 ? 193 ASP   A C   1 
ATOM   1370 O O   . ASP   A 1 186 ? 0.99309   -26.28869 -5.03779  1.000 25.15273 ? 193 ASP   A O   1 
ATOM   1371 C CB  . ASP   A 1 186 ? 3.05786   -28.25077 -4.96660  1.000 27.88535 ? 193 ASP   A CB  1 
ATOM   1372 C CG  . ASP   A 1 186 ? 4.15227   -27.40563 -5.57329  1.000 32.34284 ? 193 ASP   A CG  1 
ATOM   1373 O OD1 . ASP   A 1 186 ? 4.06964   -27.11974 -6.78685  1.000 32.55149 ? 193 ASP   A OD1 1 
ATOM   1374 O OD2 . ASP   A 1 186 ? 5.09822   -27.03461 -4.84070  1.000 37.17971 ? 193 ASP   A OD2 1 
ATOM   1375 N N   . GLN   A 1 187 ? 0.72737   -26.66417 -7.23724  1.000 18.59506 ? 194 GLN   A N   1 
ATOM   1376 C CA  . GLN   A 1 187 ? 0.09321   -25.37685 -7.49497  1.000 18.78884 ? 194 GLN   A CA  1 
ATOM   1377 C C   . GLN   A 1 187 ? -1.33675  -25.53138 -8.01319  1.000 19.67048 ? 194 GLN   A C   1 
ATOM   1378 O O   . GLN   A 1 187 ? -1.84527  -24.65504 -8.71001  1.000 19.48132 ? 194 GLN   A O   1 
ATOM   1379 C CB  . GLN   A 1 187 ? 0.94757   -24.56561 -8.47215  1.000 20.89102 ? 194 GLN   A CB  1 
ATOM   1380 C CG  . GLN   A 1 187 ? 2.37160   -24.29172 -7.96856  1.000 18.62710 ? 194 GLN   A CG  1 
ATOM   1381 C CD  . GLN   A 1 187 ? 2.42177   -23.53727 -6.64592  1.000 21.15245 ? 194 GLN   A CD  1 
ATOM   1382 O OE1 . GLN   A 1 187 ? 1.60050   -22.65029 -6.39612  1.000 22.63413 ? 194 GLN   A OE1 1 
ATOM   1383 N NE2 . GLN   A 1 187 ? 3.39761   -23.86789 -5.80809  1.000 26.14780 ? 194 GLN   A NE2 1 
ATOM   1384 N N   . THR   A 1 188 ? -2.01716  -26.62562 -7.65338  1.000 20.15699 ? 195 THR   A N   1 
ATOM   1385 C CA  . THR   A 1 188 ? -3.36205  -26.85537 -8.18806  1.000 21.16532 ? 195 THR   A CA  1 
ATOM   1386 C C   . THR   A 1 188 ? -4.43070  -25.99557 -7.52266  1.000 19.46561 ? 195 THR   A C   1 
ATOM   1387 O O   . THR   A 1 188 ? -5.59627  -26.03847 -7.94353  1.000 23.83368 ? 195 THR   A O   1 
ATOM   1388 C CB  . THR   A 1 188 ? -3.75475  -28.32593 -8.05644  1.000 24.61986 ? 195 THR   A CB  1 
ATOM   1389 O OG1 . THR   A 1 188 ? -3.72530  -28.73248 -6.67671  1.000 27.87903 ? 195 THR   A OG1 1 
ATOM   1390 C CG2 . THR   A 1 188 ? -2.81164  -29.22122 -8.88712  1.000 26.65216 ? 195 THR   A CG2 1 
ATOM   1391 N N   . GLU   A 1 189 ? -4.08217  -25.24448 -6.48115  1.000 22.97645 ? 196 GLU   A N   1 
ATOM   1392 C CA  . GLU   A 1 189 ? -5.05196  -24.33670 -5.88838  1.000 22.39758 ? 196 GLU   A CA  1 
ATOM   1393 C C   . GLU   A 1 189 ? -5.56972  -23.33839 -6.90704  1.000 23.56144 ? 196 GLU   A C   1 
ATOM   1394 O O   . GLU   A 1 189 ? -6.68522  -22.83202 -6.76061  1.000 19.66409 ? 196 GLU   A O   1 
ATOM   1395 C CB  . GLU   A 1 189 ? -4.43043  -23.60196 -4.70707  1.000 18.86905 ? 196 GLU   A CB  1 
ATOM   1396 C CG  . GLU   A 1 189 ? -3.39575  -22.52650 -5.09059  1.000 17.41456 ? 196 GLU   A CG  1 
ATOM   1397 C CD  . GLU   A 1 189 ? -2.61809  -22.06565 -3.86014  1.000 20.91260 ? 196 GLU   A CD  1 
ATOM   1398 O OE1 . GLU   A 1 189 ? -1.74735  -22.82592 -3.38253  1.000 28.93011 ? 196 GLU   A OE1 1 
ATOM   1399 O OE2 . GLU   A 1 189 ? -2.88643  -20.96880 -3.33727  1.000 23.37931 ? 196 GLU   A OE2 1 
ATOM   1400 N N   . TYR   A 1 190 ? -4.78521  -23.05195 -7.94603  1.000 16.19333 ? 197 TYR   A N   1 
ATOM   1401 C CA  . TYR   A 1 190 ? -5.19839  -22.08810 -8.96498  1.000 15.84480 ? 197 TYR   A CA  1 
ATOM   1402 C C   . TYR   A 1 190 ? -6.15898  -22.68165 -9.98467  1.000 21.78918 ? 197 TYR   A C   1 
ATOM   1403 O O   . TYR   A 1 190 ? -6.48501  -22.01265 -10.97044 1.000 20.59298 ? 197 TYR   A O   1 
ATOM   1404 C CB  . TYR   A 1 190 ? -3.95862  -21.48161 -9.63880  1.000 15.47648 ? 197 TYR   A CB  1 
ATOM   1405 C CG  . TYR   A 1 190 ? -3.07861  -20.81759 -8.60434  1.000 15.69479 ? 197 TYR   A CG  1 
ATOM   1406 C CD1 . TYR   A 1 190 ? -3.53021  -19.69402 -7.90592  1.000 15.97899 ? 197 TYR   A CD1 1 
ATOM   1407 C CD2 . TYR   A 1 190 ? -1.82615  -21.33095 -8.28499  1.000 16.25682 ? 197 TYR   A CD2 1 
ATOM   1408 C CE1 . TYR   A 1 190 ? -2.75244  -19.09535 -6.91439  1.000 17.53003 ? 197 TYR   A CE1 1 
ATOM   1409 C CE2 . TYR   A 1 190 ? -1.02141  -20.73293 -7.30122  1.000 15.79430 ? 197 TYR   A CE2 1 
ATOM   1410 C CZ  . TYR   A 1 190 ? -1.48717  -19.61214 -6.62052  1.000 20.90832 ? 197 TYR   A CZ  1 
ATOM   1411 O OH  . TYR   A 1 190 ? -0.70214  -19.01674 -5.63809  1.000 19.50199 ? 197 TYR   A OH  1 
ATOM   1412 N N   . LEU   A 1 191 ? -6.63170  -23.90832 -9.74985  1.000 21.11998 ? 198 LEU   A N   1 
ATOM   1413 C CA  . LEU   A 1 191 ? -7.76654  -24.46538 -10.46198 1.000 20.10653 ? 198 LEU   A CA  1 
ATOM   1414 C C   . LEU   A 1 191 ? -9.06415  -24.35695 -9.67590  1.000 20.36887 ? 198 LEU   A C   1 
ATOM   1415 O O   . LEU   A 1 191 ? -10.11715 -24.69856 -10.21515 1.000 23.44473 ? 198 LEU   A O   1 
ATOM   1416 C CB  . LEU   A 1 191 ? -7.51729  -25.94128 -10.80554 1.000 23.12264 ? 198 LEU   A CB  1 
ATOM   1417 C CG  . LEU   A 1 191 ? -6.25372  -26.22191 -11.61372 1.000 23.95722 ? 198 LEU   A CG  1 
ATOM   1418 C CD1 . LEU   A 1 191 ? -5.97039  -27.70457 -11.70161 1.000 25.01700 ? 198 LEU   A CD1 1 
ATOM   1419 C CD2 . LEU   A 1 191 ? -6.39096  -25.61174 -13.02103 1.000 26.62619 ? 198 LEU   A CD2 1 
ATOM   1420 N N   . GLU   A 1 192 ? -9.00606  -23.93066 -8.41304  1.000 19.72647 ? 199 GLU   A N   1 
ATOM   1421 C CA  . GLU   A 1 192 ? -10.19212 -23.83864 -7.57302  1.000 24.00042 ? 199 GLU   A CA  1 
ATOM   1422 C C   . GLU   A 1 192 ? -10.94333 -22.54163 -7.83779  1.000 20.04454 ? 199 GLU   A C   1 
ATOM   1423 O O   . GLU   A 1 192 ? -10.34375 -21.46019 -7.82812  1.000 22.04354 ? 199 GLU   A O   1 
ATOM   1424 C CB  . GLU   A 1 192 ? -9.79530  -23.91085 -6.09996  1.000 23.43380 ? 199 GLU   A CB  1 
ATOM   1425 C CG  . GLU   A 1 192 ? -9.33146  -25.28091 -5.63777  1.000 32.33255 ? 199 GLU   A CG  1 
ATOM   1426 C CD  . GLU   A 1 192 ? -8.76343  -25.24658 -4.23006  1.000 46.11243 ? 199 GLU   A CD  1 
ATOM   1427 O OE1 . GLU   A 1 192 ? -9.22181  -24.41403 -3.41452  1.000 42.46516 ? 199 GLU   A OE1 1 
ATOM   1428 O OE2 . GLU   A 1 192 ? -7.85133  -26.05337 -3.93725  1.000 44.38537 ? 199 GLU   A OE2 1 
ATOM   1429 N N   . GLU   A 1 193 ? -12.26541 -22.65297 -8.02853  1.000 25.10779 ? 200 GLU   A N   1 
ATOM   1430 C CA  . GLU   A 1 193 ? -13.08480 -21.48000 -8.33071  1.000 20.94861 ? 200 GLU   A CA  1 
ATOM   1431 C C   . GLU   A 1 193 ? -12.91351 -20.39288 -7.26831  1.000 18.56522 ? 200 GLU   A C   1 
ATOM   1432 O O   . GLU   A 1 193 ? -12.66908 -19.22520 -7.59099  1.000 18.88457 ? 200 GLU   A O   1 
ATOM   1433 C CB  . GLU   A 1 193 ? -14.55707 -21.88201 -8.45260  1.000 24.36373 ? 200 GLU   A CB  1 
ATOM   1434 C CG  . GLU   A 1 193 ? -15.45962 -20.75937 -8.93860  1.000 28.77501 ? 200 GLU   A CG  1 
ATOM   1435 C CD  . GLU   A 1 193 ? -16.90067 -21.18782 -9.21070  1.000 40.62258 ? 200 GLU   A CD  1 
ATOM   1436 O OE1 . GLU   A 1 193 ? -17.32208 -22.29142 -8.78524  1.000 36.79156 ? 200 GLU   A OE1 1 
ATOM   1437 O OE2 . GLU   A 1 193 ? -17.61656 -20.39821 -9.86088  1.000 47.94959 ? 200 GLU   A OE2 1 
ATOM   1438 N N   . ARG   A 1 194 ? -13.04661 -20.75443 -5.99094  1.000 22.77714 ? 201 ARG   A N   1 
ATOM   1439 C CA  . ARG   A 1 194 ? -12.97312 -19.73194 -4.95419  1.000 22.98400 ? 201 ARG   A CA  1 
ATOM   1440 C C   . ARG   A 1 194 ? -11.60014 -19.08233 -4.89652  1.000 21.02599 ? 201 ARG   A C   1 
ATOM   1441 O O   . ARG   A 1 194 ? -11.49634 -17.89466 -4.57592  1.000 20.10868 ? 201 ARG   A O   1 
ATOM   1442 C CB  . ARG   A 1 194 ? -13.35137 -20.32179 -3.59375  1.000 23.68630 ? 201 ARG   A CB  1 
ATOM   1443 C CG  . ARG   A 1 194 ? -12.51379 -21.50524 -3.16035  1.000 32.18849 ? 201 ARG   A CG  1 
ATOM   1444 C CD  . ARG   A 1 194 ? -13.06806 -22.07114 -1.85906  1.000 34.20388 ? 201 ARG   A CD  1 
ATOM   1445 N NE  . ARG   A 1 194 ? -12.15960 -23.04740 -1.27108  1.000 41.67773 ? 201 ARG   A NE  1 
ATOM   1446 C CZ  . ARG   A 1 194 ? -12.29728 -23.56534 -0.05920  1.000 37.00040 ? 201 ARG   A CZ  1 
ATOM   1447 N NH1 . ARG   A 1 194 ? -13.32541 -23.24987 0.71627   1.000 40.59263 ? 201 ARG   A NH1 1 
ATOM   1448 N NH2 . ARG   A 1 194 ? -11.38700 -24.42963 0.38003   1.000 46.25233 ? 201 ARG   A NH2 1 
ATOM   1449 N N   . ARG   A 1 195 ? -10.53534 -19.82769 -5.20357  1.000 20.04761 ? 202 ARG   A N   1 
ATOM   1450 C CA  . ARG   A 1 195 ? -9.20348  -19.22761 -5.18250  1.000 17.35417 ? 202 ARG   A CA  1 
ATOM   1451 C C   . ARG   A 1 195 ? -9.01884  -18.24642 -6.33500  1.000 19.53643 ? 202 ARG   A C   1 
ATOM   1452 O O   . ARG   A 1 195 ? -8.46256  -17.15434 -6.15093  1.000 16.27680 ? 202 ARG   A O   1 
ATOM   1453 C CB  . ARG   A 1 195 ? -8.13266  -20.32148 -5.21418  1.000 19.32059 ? 202 ARG   A CB  1 
ATOM   1454 C CG  . ARG   A 1 195 ? -6.70038  -19.80150 -5.21667  1.000 17.84080 ? 202 ARG   A CG  1 
ATOM   1455 C CD  . ARG   A 1 195 ? -6.32466  -19.21062 -3.87021  1.000 20.12298 ? 202 ARG   A CD  1 
ATOM   1456 N NE  . ARG   A 1 195 ? -4.88738  -18.99682 -3.75721  1.000 20.10525 ? 202 ARG   A NE  1 
ATOM   1457 C CZ  . ARG   A 1 195 ? -4.31718  -17.82560 -3.49704  1.000 20.48935 ? 202 ARG   A CZ  1 
ATOM   1458 N NH1 . ARG   A 1 195 ? -5.03641  -16.73936 -3.25307  1.000 18.15174 ? 202 ARG   A NH1 1 
ATOM   1459 N NH2 . ARG   A 1 195 ? -2.99231  -17.74089 -3.48499  1.000 21.35908 ? 202 ARG   A NH2 1 
ATOM   1460 N N   . ILE   A 1 196 ? -9.46617  -18.61831 -7.53541  1.000 17.04368 ? 203 ILE   A N   1 
ATOM   1461 C CA  . ILE   A 1 196 ? -9.36510  -17.70287 -8.66977  1.000 15.36021 ? 203 ILE   A CA  1 
ATOM   1462 C C   . ILE   A 1 196 ? -10.21878 -16.45711 -8.44047  1.000 18.31422 ? 203 ILE   A C   1 
ATOM   1463 O O   . ILE   A 1 196 ? -9.76081  -15.33809 -8.68690  1.000 17.50603 ? 203 ILE   A O   1 
ATOM   1464 C CB  . ILE   A 1 196 ? -9.74516  -18.41001 -9.97854  1.000 15.82966 ? 203 ILE   A CB  1 
ATOM   1465 C CG1 . ILE   A 1 196 ? -8.78820  -19.57584 -10.24555 1.000 15.78541 ? 203 ILE   A CG1 1 
ATOM   1466 C CG2 . ILE   A 1 196 ? -9.71778  -17.41438 -11.13466 1.000 16.75316 ? 203 ILE   A CG2 1 
ATOM   1467 C CD1 . ILE   A 1 196 ? -9.39876  -20.64359 -11.13855 1.000 18.92481 ? 203 ILE   A CD1 1 
ATOM   1468 N N   . LYS   A 1 197 ? -11.46337 -16.62462 -7.97149  1.000 14.85627 ? 204 LYS   A N   1 
ATOM   1469 C CA  . LYS   A 1 197 ? -12.29716 -15.46192 -7.65246  1.000 18.58551 ? 204 LYS   A CA  1 
ATOM   1470 C C   . LYS   A 1 197 ? -11.60329 -14.52465 -6.68264  1.000 15.42693 ? 204 LYS   A C   1 
ATOM   1471 O O   . LYS   A 1 197 ? -11.63180 -13.29633 -6.85607  1.000 17.62668 ? 204 LYS   A O   1 
ATOM   1472 C CB  . LYS   A 1 197 ? -13.65254 -15.87676 -7.06842  1.000 19.68590 ? 204 LYS   A CB  1 
ATOM   1473 C CG  . LYS   A 1 197 ? -14.53639 -16.69912 -7.98406  1.000 23.75514 ? 204 LYS   A CG  1 
ATOM   1474 C CD  . LYS   A 1 197 ? -15.96917 -16.62834 -7.48189  1.000 30.00075 ? 204 LYS   A CD  1 
ATOM   1475 C CE  . LYS   A 1 197 ? -16.80040 -17.79524 -7.96001  1.000 33.44650 ? 204 LYS   A CE  1 
ATOM   1476 N NZ  . LYS   A 1 197 ? -18.05380 -17.98185 -7.17044  1.000 44.42136 ? 204 LYS   A NZ  1 
ATOM   1477 N N   . GLU   A 1 198 ? -11.00402 -15.08410 -5.63251  1.000 15.84345 ? 205 GLU   A N   1 
ATOM   1478 C CA  . GLU   A 1 198 ? -10.33067 -14.25651 -4.64017  1.000 16.39421 ? 205 GLU   A CA  1 
ATOM   1479 C C   . GLU   A 1 198 ? -9.22633  -13.43104 -5.28508  1.000 15.02072 ? 205 GLU   A C   1 
ATOM   1480 O O   . GLU   A 1 198 ? -9.09883  -12.23058 -5.01382  1.000 18.19696 ? 205 GLU   A O   1 
ATOM   1481 C CB  . GLU   A 1 198 ? -9.78797  -15.15465 -3.53090  1.000 17.66580 ? 205 GLU   A CB  1 
ATOM   1482 C CG  . GLU   A 1 198 ? -8.90386  -14.49418 -2.50017  1.000 20.02795 ? 205 GLU   A CG  1 
ATOM   1483 C CD  . GLU   A 1 198 ? -8.29116  -15.50572 -1.55627  1.000 19.55127 ? 205 GLU   A CD  1 
ATOM   1484 O OE1 . GLU   A 1 198 ? -7.68387  -16.48922 -2.03815  1.000 18.90461 ? 205 GLU   A OE1 1 
ATOM   1485 O OE2 . GLU   A 1 198 ? -8.42480  -15.32264 -0.33647  1.000 20.31407 ? 205 GLU   A OE2 1 
ATOM   1486 N N   . ILE   A 1 199 ? -8.43731  -14.05659 -6.16173  1.000 15.58090 ? 206 ILE   A N   1 
ATOM   1487 C CA  . ILE   A 1 199 ? -7.28135  -13.38355 -6.75368  1.000 16.23682 ? 206 ILE   A CA  1 
ATOM   1488 C C   . ILE   A 1 199 ? -7.71810  -12.31274 -7.74499  1.000 15.02448 ? 206 ILE   A C   1 
ATOM   1489 O O   . ILE   A 1 199 ? -7.10393  -11.23592 -7.81218  1.000 16.45283 ? 206 ILE   A O   1 
ATOM   1490 C CB  . ILE   A 1 199 ? -6.36027  -14.41131 -7.42805  1.000 14.20406 ? 206 ILE   A CB  1 
ATOM   1491 C CG1 . ILE   A 1 199 ? -5.76572  -15.36416 -6.39833  1.000 19.80569 ? 206 ILE   A CG1 1 
ATOM   1492 C CG2 . ILE   A 1 199 ? -5.26741  -13.72791 -8.24517  1.000 17.60954 ? 206 ILE   A CG2 1 
ATOM   1493 C CD1 . ILE   A 1 199 ? -5.20153  -16.60662 -7.06698  1.000 19.53452 ? 206 ILE   A CD1 1 
ATOM   1494 N N   . VAL   A 1 200 ? -8.75254  -12.59570 -8.54621  1.000 16.88585 ? 207 VAL   A N   1 
ATOM   1495 C CA  . VAL   A 1 200 ? -9.26574  -11.59802 -9.49073  1.000 15.99152 ? 207 VAL   A CA  1 
ATOM   1496 C C   . VAL   A 1 200 ? -9.79796  -10.38290 -8.73515  1.000 15.97503 ? 207 VAL   A C   1 
ATOM   1497 O O   . VAL   A 1 200 ? -9.49289  -9.23230  -9.07430  1.000 19.83838 ? 207 VAL   A O   1 
ATOM   1498 C CB  . VAL   A 1 200 ? -10.34360 -12.21611 -10.40848 1.000 17.25684 ? 207 VAL   A CB  1 
ATOM   1499 C CG1 . VAL   A 1 200 ? -11.05426 -11.13068 -11.20812 1.000 16.55393 ? 207 VAL   A CG1 1 
ATOM   1500 C CG2 . VAL   A 1 200 ? -9.72990  -13.23996 -11.37118 1.000 16.32860 ? 207 VAL   A CG2 1 
ATOM   1501 N N   . LYS   A 1 201 ? -10.57558 -10.62198 -7.67384  1.000 17.41037 ? 208 LYS   A N   1 
ATOM   1502 C CA  . LYS   A 1 201 ? -11.11812 -9.53370  -6.87086  1.000 18.87070 ? 208 LYS   A CA  1 
ATOM   1503 C C   . LYS   A 1 201 ? -10.00880 -8.70763  -6.22136  1.000 18.99775 ? 208 LYS   A C   1 
ATOM   1504 O O   . LYS   A 1 201 ? -10.09672 -7.47600  -6.14794  1.000 25.76057 ? 208 LYS   A O   1 
ATOM   1505 C CB  . LYS   A 1 201 ? -12.06431 -10.10559 -5.80989  1.000 19.86014 ? 208 LYS   A CB  1 
ATOM   1506 C CG  . LYS   A 1 201 ? -12.69792 -9.04652  -4.91499  1.000 25.06515 ? 208 LYS   A CG  1 
ATOM   1507 C CD  . LYS   A 1 201 ? -13.45484 -9.67890  -3.75291  1.000 33.55957 ? 208 LYS   A CD  1 
ATOM   1508 C CE  . LYS   A 1 201 ? -13.98872 -8.62879  -2.78685  1.000 44.14154 ? 208 LYS   A CE  1 
ATOM   1509 N NZ  . LYS   A 1 201 ? -12.90116 -7.83269  -2.14038  1.000 45.51533 ? 208 LYS   A NZ  1 
ATOM   1510 N N   . LYS   A 1 202 ? -8.93756  -9.36714  -5.78946  1.000 20.74203 ? 209 LYS   A N   1 
ATOM   1511 C CA  . LYS   A 1 202 ? -7.86024  -8.68889  -5.07330  1.000 20.68877 ? 209 LYS   A CA  1 
ATOM   1512 C C   . LYS   A 1 202 ? -7.00565  -7.83038  -6.00740  1.000 20.22439 ? 209 LYS   A C   1 
ATOM   1513 O O   . LYS   A 1 202 ? -6.62452  -6.70806  -5.65146  1.000 23.99328 ? 209 LYS   A O   1 
ATOM   1514 C CB  . LYS   A 1 202 ? -6.99727  -9.74094  -4.36955  1.000 21.27840 ? 209 LYS   A CB  1 
ATOM   1515 C CG  . LYS   A 1 202 ? -5.84931  -9.20464  -3.52591  1.000 24.72445 ? 209 LYS   A CG  1 
ATOM   1516 C CD  . LYS   A 1 202 ? -5.04446  -10.37309 -2.94404  1.000 25.26488 ? 209 LYS   A CD  1 
ATOM   1517 C CE  . LYS   A 1 202 ? -4.00835  -9.89057  -1.94058  1.000 38.87225 ? 209 LYS   A CE  1 
ATOM   1518 N NZ  . LYS   A 1 202 ? -3.36887  -11.00883 -1.18536  1.000 41.07362 ? 209 LYS   A NZ  1 
ATOM   1519 N N   . HIS   A 1 203 ? -6.68756  -8.33945  -7.20417  1.000 19.19108 ? 210 HIS   A N   1 
ATOM   1520 C CA  . HIS   A 1 203 ? -5.66508  -7.73408  -8.05001  1.000 23.79798 ? 210 HIS   A CA  1 
ATOM   1521 C C   . HIS   A 1 203 ? -6.15662  -7.22946  -9.39991  1.000 22.49952 ? 210 HIS   A C   1 
ATOM   1522 O O   . HIS   A 1 203 ? -5.41630  -6.49241  -10.06265 1.000 23.71219 ? 210 HIS   A O   1 
ATOM   1523 C CB  . HIS   A 1 203 ? -4.53024  -8.73662  -8.30815  1.000 22.99274 ? 210 HIS   A CB  1 
ATOM   1524 C CG  . HIS   A 1 203 ? -3.75931  -9.11121  -7.08214  1.000 23.94830 ? 210 HIS   A CG  1 
ATOM   1525 N ND1 . HIS   A 1 203 ? -3.11560  -8.18261  -6.29735  1.000 26.16599 ? 210 HIS   A ND1 1 
ATOM   1526 C CD2 . HIS   A 1 203 ? -3.52998  -10.31573 -6.50605  1.000 23.40815 ? 210 HIS   A CD2 1 
ATOM   1527 C CE1 . HIS   A 1 203 ? -2.50818  -8.79990  -5.29889  1.000 29.95754 ? 210 HIS   A CE1 1 
ATOM   1528 N NE2 . HIS   A 1 203 ? -2.75006  -10.09407 -5.40092  1.000 23.41435 ? 210 HIS   A NE2 1 
ATOM   1529 N N   . SER   A 1 204 ? -7.34581  -7.62789  -9.84807  1.000 22.02845 ? 211 SER   A N   1 
ATOM   1530 C CA  . SER   A 1 204 ? -7.80606  -7.28895  -11.19044 1.000 18.98779 ? 211 SER   A CA  1 
ATOM   1531 C C   . SER   A 1 204 ? -9.23377  -6.74856  -11.17427 1.000 22.80394 ? 211 SER   A C   1 
ATOM   1532 O O   . SER   A 1 204 ? -9.99592  -6.97485  -12.11665 1.000 23.66492 ? 211 SER   A O   1 
ATOM   1533 C CB  . SER   A 1 204 ? -7.69845  -8.49685  -12.14076 1.000 17.72885 ? 211 SER   A CB  1 
ATOM   1534 O OG  . SER   A 1 204 ? -6.38136  -9.03225  -12.08441 1.000 21.10529 ? 211 SER   A OG  1 
ATOM   1535 N N   . GLN   A 1 205 ? -9.61065  -6.00820  -10.12653 1.000 23.52881 ? 212 GLN   A N   1 
ATOM   1536 C CA  . GLN   A 1 205 ? -11.01733 -5.63264  -9.96070  1.000 28.72095 ? 212 GLN   A CA  1 
ATOM   1537 C C   . GLN   A 1 205 ? -11.47132 -4.55316  -10.94056 1.000 24.66419 ? 212 GLN   A C   1 
ATOM   1538 O O   . GLN   A 1 205 ? -12.67287 -4.44154  -11.19135 1.000 29.76662 ? 212 GLN   A O   1 
ATOM   1539 C CB  . GLN   A 1 205 ? -11.30069 -5.15982  -8.52487  1.000 36.65409 ? 212 GLN   A CB  1 
ATOM   1540 C CG  . GLN   A 1 205 ? -10.40100 -4.05893  -8.05513  1.000 35.13471 ? 212 GLN   A CG  1 
ATOM   1541 C CD  . GLN   A 1 205 ? -9.17276  -4.56745  -7.30671  1.000 45.62728 ? 212 GLN   A CD  1 
ATOM   1542 O OE1 . GLN   A 1 205 ? -8.15368  -4.93956  -7.91033  1.000 34.65226 ? 212 GLN   A OE1 1 
ATOM   1543 N NE2 . GLN   A 1 205 ? -9.25874  -4.56623  -5.97915  1.000 41.66640 ? 212 GLN   A NE2 1 
ATOM   1544 N N   . PHE   A 1 206 ? -10.55418 -3.75998  -11.50359 1.000 26.18043 ? 213 PHE   A N   1 
ATOM   1545 C CA  . PHE   A 1 206 ? -10.94110 -2.61995  -12.33137 1.000 24.72817 ? 213 PHE   A CA  1 
ATOM   1546 C C   . PHE   A 1 206 ? -10.60212 -2.81911  -13.80259 1.000 24.58185 ? 213 PHE   A C   1 
ATOM   1547 O O   . PHE   A 1 206 ? -10.60948 -1.86320  -14.57897 1.000 24.62181 ? 213 PHE   A O   1 
ATOM   1548 C CB  . PHE   A 1 206 ? -10.31051 -1.33529  -11.79100 1.000 22.83846 ? 213 PHE   A CB  1 
ATOM   1549 C CG  . PHE   A 1 206 ? -10.85046 -0.93207  -10.44750 1.000 22.69207 ? 213 PHE   A CG  1 
ATOM   1550 C CD1 . PHE   A 1 206 ? -12.21712 -0.75879  -10.26446 1.000 27.40787 ? 213 PHE   A CD1 1 
ATOM   1551 C CD2 . PHE   A 1 206 ? -10.00981 -0.78399  -9.35868  1.000 30.78809 ? 213 PHE   A CD2 1 
ATOM   1552 C CE1 . PHE   A 1 206 ? -12.72610 -0.41005  -9.03178  1.000 25.90607 ? 213 PHE   A CE1 1 
ATOM   1553 C CE2 . PHE   A 1 206 ? -10.51816 -0.44023  -8.11960  1.000 33.60788 ? 213 PHE   A CE2 1 
ATOM   1554 C CZ  . PHE   A 1 206 ? -11.87769 -0.24537  -7.96019  1.000 31.23137 ? 213 PHE   A CZ  1 
ATOM   1555 N N   . ILE   A 1 207 ? -10.33767 -4.05219  -14.21448 1.000 19.81480 ? 214 ILE   A N   1 
ATOM   1556 C CA  . ILE   A 1 207 ? -10.03690 -4.28631  -15.61699 1.000 18.01855 ? 214 ILE   A CA  1 
ATOM   1557 C C   . ILE   A 1 207 ? -11.25425 -3.93162  -16.46484 1.000 17.20096 ? 214 ILE   A C   1 
ATOM   1558 O O   . ILE   A 1 207 ? -12.39360 -4.28867  -16.13269 1.000 19.77236 ? 214 ILE   A O   1 
ATOM   1559 C CB  . ILE   A 1 207 ? -9.60251  -5.74659  -15.80932 1.000 17.59572 ? 214 ILE   A CB  1 
ATOM   1560 C CG1 . ILE   A 1 207 ? -8.28653  -5.97538  -15.06481 1.000 23.64120 ? 214 ILE   A CG1 1 
ATOM   1561 C CG2 . ILE   A 1 207 ? -9.51268  -6.08840  -17.29576 1.000 20.19820 ? 214 ILE   A CG2 1 
ATOM   1562 C CD1 . ILE   A 1 207 ? -7.05388  -5.35614  -15.72800 1.000 23.37720 ? 214 ILE   A CD1 1 
ATOM   1563 N N   . GLY   A 1 208 ? -11.01295 -3.22577  -17.57181 1.000 18.98239 ? 215 GLY   A N   1 
ATOM   1564 C CA  . GLY   A 1 208 ? -12.07708 -2.64746  -18.36678 1.000 18.87461 ? 215 GLY   A CA  1 
ATOM   1565 C C   . GLY   A 1 208 ? -12.72774 -3.55531  -19.39760 1.000 20.21560 ? 215 GLY   A C   1 
ATOM   1566 O O   . GLY   A 1 208 ? -13.21822 -3.07492  -20.42204 1.000 19.76219 ? 215 GLY   A O   1 
ATOM   1567 N N   . TYR   A 1 209 ? -12.74065 -4.85779  -19.13531 1.000 19.57917 ? 216 TYR   A N   1 
ATOM   1568 C CA  . TYR   A 1 209 ? -13.27570 -5.86970  -20.03506 1.000 22.60416 ? 216 TYR   A CA  1 
ATOM   1569 C C   . TYR   A 1 209 ? -13.88697 -6.95962  -19.17960 1.000 20.98418 ? 216 TYR   A C   1 
ATOM   1570 O O   . TYR   A 1 209 ? -13.43288 -7.19657  -18.04965 1.000 22.88597 ? 216 TYR   A O   1 
ATOM   1571 C CB  . TYR   A 1 209 ? -12.18871 -6.46970  -20.95578 1.000 17.24262 ? 216 TYR   A CB  1 
ATOM   1572 C CG  . TYR   A 1 209 ? -11.53726 -5.44055  -21.85001 1.000 18.17062 ? 216 TYR   A CG  1 
ATOM   1573 C CD1 . TYR   A 1 209 ? -12.18243 -4.99203  -23.00718 1.000 18.48747 ? 216 TYR   A CD1 1 
ATOM   1574 C CD2 . TYR   A 1 209 ? -10.31277 -4.85126  -21.49197 1.000 17.25276 ? 216 TYR   A CD2 1 
ATOM   1575 C CE1 . TYR   A 1 209 ? -11.60840 -4.01927  -23.79907 1.000 19.12190 ? 216 TYR   A CE1 1 
ATOM   1576 C CE2 . TYR   A 1 209 ? -9.72584  -3.86570  -22.27633 1.000 18.22512 ? 216 TYR   A CE2 1 
ATOM   1577 C CZ  . TYR   A 1 209 ? -10.38281 -3.45430  -23.42500 1.000 17.17845 ? 216 TYR   A CZ  1 
ATOM   1578 O OH  . TYR   A 1 209 ? -9.82002  -2.48778  -24.22101 1.000 20.83560 ? 216 TYR   A OH  1 
ATOM   1579 N N   . PRO   A 1 210 ? -14.92897 -7.62915  -19.66502 1.000 19.28477 ? 217 PRO   A N   1 
ATOM   1580 C CA  . PRO   A 1 210 ? -15.53415 -8.70884  -18.88015 1.000 19.20401 ? 217 PRO   A CA  1 
ATOM   1581 C C   . PRO   A 1 210 ? -14.57687 -9.87937  -18.72389 1.000 20.79502 ? 217 PRO   A C   1 
ATOM   1582 O O   . PRO   A 1 210 ? -13.98624 -10.35007 -19.69905 1.000 19.31754 ? 217 PRO   A O   1 
ATOM   1583 C CB  . PRO   A 1 210 ? -16.77076 -9.09624  -19.69505 1.000 24.09939 ? 217 PRO   A CB  1 
ATOM   1584 C CG  . PRO   A 1 210 ? -16.48111 -8.63689  -21.07868 1.000 24.65637 ? 217 PRO   A CG  1 
ATOM   1585 C CD  . PRO   A 1 210 ? -15.62131 -7.41932  -20.95100 1.000 18.94579 ? 217 PRO   A CD  1 
ATOM   1586 N N   . ILE   A 1 211 ? -14.43088 -10.33500 -17.48077 1.000 20.15259 ? 218 ILE   A N   1 
ATOM   1587 C CA  . ILE   A 1 211 ? -13.65033 -11.51132 -17.11633 1.000 16.84582 ? 218 ILE   A CA  1 
ATOM   1588 C C   . ILE   A 1 211 ? -14.63584 -12.59262 -16.68416 1.000 15.49342 ? 218 ILE   A C   1 
ATOM   1589 O O   . ILE   A 1 211 ? -15.29453 -12.46953 -15.64280 1.000 19.12860 ? 218 ILE   A O   1 
ATOM   1590 C CB  . ILE   A 1 211 ? -12.64248 -11.20227 -15.99900 1.000 15.77967 ? 218 ILE   A CB  1 
ATOM   1591 C CG1 . ILE   A 1 211 ? -11.68669 -10.08056 -16.41890 1.000 14.32719 ? 218 ILE   A CG1 1 
ATOM   1592 C CG2 . ILE   A 1 211 ? -11.91491 -12.48508 -15.57238 1.000 20.24235 ? 218 ILE   A CG2 1 
ATOM   1593 C CD1 . ILE   A 1 211 ? -10.77943 -9.56605  -15.25898 1.000 16.24483 ? 218 ILE   A CD1 1 
ATOM   1594 N N   . THR   A 1 212 ? -14.76156 -13.64781 -17.48894 1.000 17.21169 ? 219 THR   A N   1 
ATOM   1595 C CA  . THR   A 1 212 ? -15.65262 -14.75752 -17.16293 1.000 17.19461 ? 219 THR   A CA  1 
ATOM   1596 C C   . THR   A 1 212 ? -14.82305 -15.91736 -16.63428 1.000 16.01362 ? 219 THR   A C   1 
ATOM   1597 O O   . THR   A 1 212 ? -13.97340 -16.46253 -17.35306 1.000 14.79696 ? 219 THR   A O   1 
ATOM   1598 C CB  . THR   A 1 212 ? -16.47100 -15.20549 -18.37269 1.000 18.62820 ? 219 THR   A CB  1 
ATOM   1599 O OG1 . THR   A 1 212 ? -17.13925 -14.07431 -18.93836 1.000 17.87077 ? 219 THR   A OG1 1 
ATOM   1600 C CG2 . THR   A 1 212 ? -17.53031 -16.22704 -17.93930 1.000 17.96621 ? 219 THR   A CG2 1 
ATOM   1601 N N   . LEU   A 1 213 ? -15.07876 -16.30108 -15.39044 1.000 15.95171 ? 220 LEU   A N   1 
ATOM   1602 C CA  . LEU   A 1 213 ? -14.45116 -17.47781 -14.80548 1.000 16.90258 ? 220 LEU   A CA  1 
ATOM   1603 C C   . LEU   A 1 213 ? -15.32740 -18.68525 -15.12415 1.000 14.70500 ? 220 LEU   A C   1 
ATOM   1604 O O   . LEU   A 1 213 ? -16.41600 -18.82699 -14.56605 1.000 17.91230 ? 220 LEU   A O   1 
ATOM   1605 C CB  . LEU   A 1 213 ? -14.26962 -17.29893 -13.29966 1.000 19.05642 ? 220 LEU   A CB  1 
ATOM   1606 C CG  . LEU   A 1 213 ? -13.73531 -18.52335 -12.55691 1.000 20.57047 ? 220 LEU   A CG  1 
ATOM   1607 C CD1 . LEU   A 1 213 ? -12.41170 -19.01836 -13.17381 1.000 17.17505 ? 220 LEU   A CD1 1 
ATOM   1608 C CD2 . LEU   A 1 213 ? -13.52461 -18.17948 -11.09935 1.000 21.70581 ? 220 LEU   A CD2 1 
ATOM   1609 N N   . PHE   A 1 214 ? -14.84439 -19.56103 -16.00727 1.000 12.98934 ? 221 PHE   A N   1 
ATOM   1610 C CA  . PHE   A 1 214 ? -15.58655 -20.77311 -16.33538 1.000 16.70568 ? 221 PHE   A CA  1 
ATOM   1611 C C   . PHE   A 1 214 ? -15.59563 -21.71513 -15.13512 1.000 18.89099 ? 221 PHE   A C   1 
ATOM   1612 O O   . PHE   A 1 214 ? -14.66559 -21.72911 -14.32338 1.000 20.36515 ? 221 PHE   A O   1 
ATOM   1613 C CB  . PHE   A 1 214 ? -14.97721 -21.51278 -17.52776 1.000 14.91541 ? 221 PHE   A CB  1 
ATOM   1614 C CG  . PHE   A 1 214 ? -15.24708 -20.88196 -18.88169 1.000 16.11205 ? 221 PHE   A CG  1 
ATOM   1615 C CD1 . PHE   A 1 214 ? -15.31855 -19.49956 -19.04109 1.000 17.43847 ? 221 PHE   A CD1 1 
ATOM   1616 C CD2 . PHE   A 1 214 ? -15.36748 -21.69086 -20.00097 1.000 17.80810 ? 221 PHE   A CD2 1 
ATOM   1617 C CE1 . PHE   A 1 214 ? -15.52066 -18.94170 -20.29933 1.000 13.62731 ? 221 PHE   A CE1 1 
ATOM   1618 C CE2 . PHE   A 1 214 ? -15.58855 -21.13799 -21.27102 1.000 16.36638 ? 221 PHE   A CE2 1 
ATOM   1619 C CZ  . PHE   A 1 214 ? -15.67244 -19.76707 -21.40929 1.000 12.11354 ? 221 PHE   A CZ  1 
ATOM   1620 N N   . VAL   A 1 215 ? -16.67491 -22.48711 -15.02899 1.000 19.39168 ? 222 VAL   A N   1 
ATOM   1621 C CA  . VAL   A 1 215 ? -16.86842 -23.52613 -14.02012 1.000 18.77663 ? 222 VAL   A CA  1 
ATOM   1622 C C   . VAL   A 1 215 ? -16.52106 -24.87944 -14.63212 1.000 23.41115 ? 222 VAL   A C   1 
ATOM   1623 O O   . VAL   A 1 215 ? -16.69764 -25.11184 -15.83353 1.000 21.52351 ? 222 VAL   A O   1 
ATOM   1624 C CB  . VAL   A 1 215 ? -18.32745 -23.49734 -13.49477 1.000 20.61456 ? 222 VAL   A CB  1 
ATOM   1625 C CG1 . VAL   A 1 215 ? -18.61929 -24.65276 -12.52586 1.000 27.53216 ? 222 VAL   A CG1 1 
ATOM   1626 C CG2 . VAL   A 1 215 ? -18.64484 -22.16089 -12.85015 1.000 27.97784 ? 222 VAL   A CG2 1 
ATOM   1627 N N   . GLU   A 1 216 ? -16.04327 -25.79560 -13.80413 1.000 26.32600 ? 223 GLU   A N   1 
ATOM   1628 C CA  . GLU   A 1 216 ? -15.70757 -27.12591 -14.29255 1.000 28.54774 ? 223 GLU   A CA  1 
ATOM   1629 C C   . GLU   A 1 216 ? -16.90536 -28.06736 -14.28400 1.000 33.01545 ? 223 GLU   A C   1 
ATOM   1630 O O   . GLU   A 1 216 ? -17.80806 -27.95892 -13.44795 1.000 30.92919 ? 223 GLU   A O   1 
ATOM   1631 C CB  . GLU   A 1 216 ? -14.58409 -27.70849 -13.45582 1.000 33.06131 ? 223 GLU   A CB  1 
ATOM   1632 C CG  . GLU   A 1 216 ? -13.29017 -26.99637 -13.73442 1.000 32.84430 ? 223 GLU   A CG  1 
ATOM   1633 C CD  . GLU   A 1 216 ? -12.11090 -27.90437 -13.58797 1.000 31.94356 ? 223 GLU   A CD  1 
ATOM   1634 O OE1 . GLU   A 1 216 ? -12.06616 -28.92760 -14.30455 1.000 36.07993 ? 223 GLU   A OE1 1 
ATOM   1635 O OE2 . GLU   A 1 216 ? -11.24212 -27.60624 -12.74705 1.000 44.36938 ? 223 GLU   A OE2 1 
ATOM   1636 N N   . LYS   A 1 217 ? -16.87954 -29.02883 -15.20382 1.000 32.51941 ? 224 LYS   A N   1 
ATOM   1637 C CA  . LYS   A 1 217 ? -17.98124 -29.97482 -15.35739 1.000 33.51893 ? 224 LYS   A CA  1 
ATOM   1638 C C   . LYS   A 1 217 ? -17.81969 -31.22191 -14.47507 1.000 38.96628 ? 224 LYS   A C   1 
ATOM   1639 O O   . LYS   A 1 217 ? -16.81811 -31.93691 -14.54530 1.000 53.01393 ? 224 LYS   A O   1 
ATOM   1640 C CB  . LYS   A 1 217 ? -18.12910 -30.38049 -16.83371 1.000 33.31978 ? 224 LYS   A CB  1 
ATOM   1641 C CG  . LYS   A 1 217 ? -17.81510 -29.25231 -17.82315 1.000 31.06733 ? 224 LYS   A CG  1 
ATOM   1642 C CD  . LYS   A 1 217 ? -18.13387 -29.63061 -19.27739 1.000 28.74765 ? 224 LYS   A CD  1 
ATOM   1643 C CE  . LYS   A 1 217 ? -16.94296 -30.29384 -19.96328 1.000 29.30911 ? 224 LYS   A CE  1 
ATOM   1644 N NZ  . LYS   A 1 217 ? -15.82268 -29.33261 -20.17871 1.000 28.57191 ? 224 LYS   A NZ  1 
HETATM 1645 C C1  . A1AXM B 2 .   ? 3.09912   -13.99688 -24.39672 0.810 16.14352 ? 301 A1AXM A C1  1 
HETATM 1646 C C2  . A1AXM B 2 .   ? 4.38835   -14.27991 -24.96222 0.810 18.60202 ? 301 A1AXM A C2  1 
HETATM 1647 C C3  . A1AXM B 2 .   ? 4.54533   -15.48069 -25.66769 0.810 18.27331 ? 301 A1AXM A C3  1 
HETATM 1648 C C4  . A1AXM B 2 .   ? 5.76457   -15.79816 -26.21546 0.810 17.47093 ? 301 A1AXM A C4  1 
HETATM 1649 C C5  . A1AXM B 2 .   ? 6.83677   -14.95113 -26.08280 0.810 21.95460 ? 301 A1AXM A C5  1 
HETATM 1650 N N1  . A1AXM B 2 .   ? 2.07465   -13.77219 -23.94683 0.810 21.16737 ? 301 A1AXM A N1  1 
HETATM 1651 C C10 . A1AXM B 2 .   ? 4.30320   -11.30881 -24.13355 0.810 18.36514 ? 301 A1AXM A C10 1 
HETATM 1652 C C6  . A1AXM B 2 .   ? 6.70553   -13.75971 -25.38826 0.810 22.91807 ? 301 A1AXM A C6  1 
HETATM 1653 C C7  . A1AXM B 2 .   ? 5.47162   -13.41168 -24.83134 0.810 17.47247 ? 301 A1AXM A C7  1 
HETATM 1654 C C8  . A1AXM B 2 .   ? 6.32489   -11.60331 -23.35466 0.810 22.79722 ? 301 A1AXM A C8  1 
HETATM 1655 C C9  . A1AXM B 2 .   ? 5.82942   -10.44708 -22.89827 0.810 21.03025 ? 301 A1AXM A C9  1 
HETATM 1656 N N2  . A1AXM B 2 .   ? 5.34722   -12.17250 -24.12643 0.810 21.79162 ? 301 A1AXM A N2  1 
HETATM 1657 N N3  . A1AXM B 2 .   ? 4.55904   -10.25506 -23.38600 0.810 22.05811 ? 301 A1AXM A N3  1 
HETATM 1658 O O   . HOH   C 3 .   ? -7.61683  3.40343   -39.56994 1.000 45.66205 ? 401 HOH   A O   1 
HETATM 1659 O O   . HOH   C 3 .   ? -6.58728  -3.65256  -8.07497  1.000 48.86809 ? 402 HOH   A O   1 
HETATM 1660 O O   . HOH   C 3 .   ? 3.80705   -18.66170 -40.84958 1.000 48.74958 ? 403 HOH   A O   1 
HETATM 1661 O O   . HOH   C 3 .   ? -13.15898 -22.99648 -34.07732 1.000 44.37006 ? 404 HOH   A O   1 
HETATM 1662 O O   . HOH   C 3 .   ? 20.76426  -12.41014 -13.22017 1.000 49.28387 ? 405 HOH   A O   1 
HETATM 1663 O O   . HOH   C 3 .   ? -5.32649  -24.65394 -31.10100 1.000 34.85729 ? 406 HOH   A O   1 
HETATM 1664 O O   . HOH   C 3 .   ? 14.15623  -3.06578  -24.69771 1.000 46.39022 ? 407 HOH   A O   1 
HETATM 1665 O O   . HOH   C 3 .   ? 18.31327  0.24839   -13.43559 1.000 40.79892 ? 408 HOH   A O   1 
HETATM 1666 O O   . HOH   C 3 .   ? 5.34301   -28.74760 -30.97810 1.000 47.58631 ? 409 HOH   A O   1 
HETATM 1667 O O   . HOH   C 3 .   ? 4.50112   -30.21715 -25.36520 1.000 37.40847 ? 410 HOH   A O   1 
HETATM 1668 O O   . HOH   C 3 .   ? -12.69163 -28.92307 -16.67669 1.000 44.28979 ? 411 HOH   A O   1 
HETATM 1669 O O   . HOH   C 3 .   ? 11.97349  -3.75717  -21.52946 1.000 37.80280 ? 412 HOH   A O   1 
HETATM 1670 O O   . HOH   C 3 .   ? -4.70399  -18.11964 -41.40994 1.000 36.86453 ? 413 HOH   A O   1 
HETATM 1671 O O   . HOH   C 3 .   ? -1.89211  -15.01615 -42.96342 1.000 41.01191 ? 414 HOH   A O   1 
HETATM 1672 O O   . HOH   C 3 .   ? -15.67598 -25.50009 -18.09298 1.000 23.10965 ? 415 HOH   A O   1 
HETATM 1673 O O   . HOH   C 3 .   ? 13.74330  -21.62557 -4.05548  1.000 39.71097 ? 416 HOH   A O   1 
HETATM 1674 O O   . HOH   C 3 .   ? -0.40659  -6.71096  -26.47466 1.000 26.23138 ? 417 HOH   A O   1 
HETATM 1675 O O   . HOH   C 3 .   ? -14.54795 -1.48284  -24.56632 1.000 37.44043 ? 418 HOH   A O   1 
HETATM 1676 O O   . HOH   C 3 .   ? 13.90414  -9.27988  -3.65802  1.000 39.09720 ? 419 HOH   A O   1 
HETATM 1677 O O   . HOH   C 3 .   ? 0.24067   -10.35140 -43.46302 1.000 41.62093 ? 420 HOH   A O   1 
HETATM 1678 O O   . HOH   C 3 .   ? -16.77421 -24.72493 -9.19383  1.000 40.50366 ? 421 HOH   A O   1 
HETATM 1679 O O   . HOH   C 3 .   ? 8.44815   -28.40413 -23.21695 1.000 25.20921 ? 422 HOH   A O   1 
HETATM 1680 O O   . HOH   C 3 .   ? -4.23662  -13.40040 -1.19191  1.000 37.85769 ? 423 HOH   A O   1 
HETATM 1681 O O   . HOH   C 3 .   ? -12.02027 -28.10878 -30.33418 1.000 38.78037 ? 424 HOH   A O   1 
HETATM 1682 O O   . HOH   C 3 .   ? -8.42329  -2.48084  -18.56109 1.000 21.01532 ? 425 HOH   A O   1 
HETATM 1683 O O   . HOH   C 3 .   ? 8.03004   -18.59334 -6.09849  1.000 32.11579 ? 426 HOH   A O   1 
HETATM 1684 O O   . HOH   C 3 .   ? 10.92404  -14.63791 -24.91849 1.000 22.88022 ? 427 HOH   A O   1 
HETATM 1685 O O   . HOH   C 3 .   ? 4.73725   -25.45517 -38.14582 1.000 28.21259 ? 428 HOH   A O   1 
HETATM 1686 O O   . HOH   C 3 .   ? -3.62295  -4.90089  -9.07065  1.000 40.78976 ? 429 HOH   A O   1 
HETATM 1687 O O   . HOH   C 3 .   ? 3.74281   -4.32948  -17.72598 1.000 32.08118 ? 430 HOH   A O   1 
HETATM 1688 O O   . HOH   C 3 .   ? -11.54791 -19.91614 -27.27366 1.000 46.35274 ? 431 HOH   A O   1 
HETATM 1689 O O   . HOH   C 3 .   ? 0.94675   -20.76441 -4.61056  1.000 23.72064 ? 432 HOH   A O   1 
HETATM 1690 O O   . HOH   C 3 .   ? 18.81864  -1.10205  -16.44632 1.000 38.36523 ? 433 HOH   A O   1 
HETATM 1691 O O   . HOH   C 3 .   ? -4.505    6.072     -35.028   1.000 39.27484 ? 434 HOH   A O   1 
HETATM 1692 O O   . HOH   C 3 .   ? 22.770    -13.700   -18.662   1.000 46.47408 ? 435 HOH   A O   1 
HETATM 1693 O O   . HOH   C 3 .   ? -13.89815 -4.28095  -13.50414 1.000 36.48973 ? 436 HOH   A O   1 
HETATM 1694 O O   . HOH   C 3 .   ? -10.65142 -14.27655 0.57674   1.000 23.11228 ? 437 HOH   A O   1 
HETATM 1695 O O   . HOH   C 3 .   ? 16.46673  -26.75640 -24.25182 1.000 38.43545 ? 438 HOH   A O   1 
HETATM 1696 O O   . HOH   C 3 .   ? 17.39965  -1.80181  -18.90379 1.000 28.86690 ? 439 HOH   A O   1 
HETATM 1697 O O   . HOH   C 3 .   ? -1.40619  -28.71892 -5.43871  1.000 27.73120 ? 440 HOH   A O   1 
HETATM 1698 O O   . HOH   C 3 .   ? 11.66467  -14.78114 -28.46648 1.000 34.46972 ? 441 HOH   A O   1 
HETATM 1699 O O   . HOH   C 3 .   ? -3.30223  0.04411   -22.76951 1.000 27.88256 ? 442 HOH   A O   1 
HETATM 1700 O O   . HOH   C 3 .   ? 3.77736   -6.03650  -11.31984 1.000 22.38375 ? 443 HOH   A O   1 
HETATM 1701 O O   . HOH   C 3 .   ? 8.34321   -23.24895 -13.79976 1.000 21.90087 ? 444 HOH   A O   1 
HETATM 1702 O O   . HOH   C 3 .   ? 7.50929   -22.91515 -36.81636 1.000 29.77557 ? 445 HOH   A O   1 
HETATM 1703 O O   . HOH   C 3 .   ? -13.51746 -30.31062 -21.01874 1.000 38.89663 ? 446 HOH   A O   1 
HETATM 1704 O O   . HOH   C 3 .   ? 21.09979  -9.71433  -3.18452  1.000 50.86058 ? 447 HOH   A O   1 
HETATM 1705 O O   . HOH   C 3 .   ? -4.10142  -11.04917 -27.71989 1.000 15.73577 ? 448 HOH   A O   1 
HETATM 1706 O O   . HOH   C 3 .   ? -1.73792  -25.21214 -4.52885  1.000 21.77271 ? 449 HOH   A O   1 
HETATM 1707 O O   . HOH   C 3 .   ? -15.54189 -12.87754 -20.67851 1.000 18.36643 ? 450 HOH   A O   1 
HETATM 1708 O O   . HOH   C 3 .   ? 10.76163  -20.90910 -6.48933  1.000 29.40309 ? 451 HOH   A O   1 
HETATM 1709 O O   . HOH   C 3 .   ? 12.63537  -29.06488 -29.31359 1.000 28.38894 ? 452 HOH   A O   1 
HETATM 1710 O O   . HOH   C 3 .   ? 10.19442  -12.72349 -28.73414 1.000 22.15245 ? 453 HOH   A O   1 
HETATM 1711 O O   . HOH   C 3 .   ? 10.39387  -23.87712 -8.74499  1.000 42.12122 ? 454 HOH   A O   1 
HETATM 1712 O O   . HOH   C 3 .   ? 2.17138   -8.07222  -16.87774 1.000 16.26663 ? 455 HOH   A O   1 
HETATM 1713 O O   . HOH   C 3 .   ? -8.97832  -15.56474 -28.62600 1.000 25.05662 ? 456 HOH   A O   1 
HETATM 1714 O O   . HOH   C 3 .   ? -4.90983  -2.36388  -20.29355 1.000 30.66202 ? 457 HOH   A O   1 
HETATM 1715 O O   . HOH   C 3 .   ? 21.50198  -12.13242 -25.59960 1.000 39.47633 ? 458 HOH   A O   1 
HETATM 1716 O O   . HOH   C 3 .   ? 18.89583  -7.94037  -19.99081 1.000 27.54005 ? 459 HOH   A O   1 
HETATM 1717 O O   . HOH   C 3 .   ? -2.81507  -11.99454 -9.30792  1.000 22.94408 ? 460 HOH   A O   1 
HETATM 1718 O O   . HOH   C 3 .   ? 16.01895  -0.82201  -12.06961 1.000 34.56420 ? 461 HOH   A O   1 
HETATM 1719 O O   . HOH   C 3 .   ? 0.68459   -5.82273  -18.96735 1.000 19.99257 ? 462 HOH   A O   1 
HETATM 1720 O O   . HOH   C 3 .   ? -0.55704  -14.43796 -35.62204 1.000 31.69899 ? 463 HOH   A O   1 
HETATM 1721 O O   . HOH   C 3 .   ? -12.49925 -7.52432  -12.93629 1.000 31.01326 ? 464 HOH   A O   1 
HETATM 1722 O O   . HOH   C 3 .   ? 20.62210  -2.21761  -7.92798  1.000 42.23204 ? 465 HOH   A O   1 
HETATM 1723 O O   . HOH   C 3 .   ? 6.13029   -20.88533 0.35383   1.000 22.47325 ? 466 HOH   A O   1 
HETATM 1724 O O   . HOH   C 3 .   ? 1.40904   -5.32473  -22.59249 1.000 30.52859 ? 467 HOH   A O   1 
HETATM 1725 O O   . HOH   C 3 .   ? -11.32468 -8.05827  -43.27917 1.000 43.61320 ? 468 HOH   A O   1 
HETATM 1726 O O   . HOH   C 3 .   ? 9.83653   -26.42340 -16.39672 1.000 29.94439 ? 469 HOH   A O   1 
HETATM 1727 O O   . HOH   C 3 .   ? -3.92098  -8.51308  -42.87635 1.000 43.24690 ? 470 HOH   A O   1 
HETATM 1728 O O   . HOH   C 3 .   ? -10.13261 0.06161   -16.43269 1.000 33.37141 ? 471 HOH   A O   1 
HETATM 1729 O O   . HOH   C 3 .   ? 3.32254   -20.12894 -2.57543  1.000 28.09795 ? 472 HOH   A O   1 
HETATM 1730 O O   . HOH   C 3 .   ? 9.87219   -5.21620  -2.09726  1.000 33.03811 ? 473 HOH   A O   1 
HETATM 1731 O O   . HOH   C 3 .   ? -4.71489  -5.76016  -39.89683 1.000 38.24362 ? 474 HOH   A O   1 
HETATM 1732 O O   . HOH   C 3 .   ? -4.77776  -7.63081  -13.77948 1.000 20.14585 ? 475 HOH   A O   1 
HETATM 1733 O O   . HOH   C 3 .   ? -7.51815  -24.91666 -19.18842 1.000 19.48930 ? 476 HOH   A O   1 
HETATM 1734 O O   . HOH   C 3 .   ? 18.91172  -20.01370 -23.86341 1.000 30.50119 ? 477 HOH   A O   1 
HETATM 1735 O O   . HOH   C 3 .   ? -0.81419  -11.04651 -3.02415  1.000 30.36313 ? 478 HOH   A O   1 
HETATM 1736 O O   . HOH   C 3 .   ? 8.89372   -6.00891  -22.33518 1.000 31.85585 ? 479 HOH   A O   1 
HETATM 1737 O O   . HOH   C 3 .   ? -7.03626  -10.93152 -41.13952 1.000 42.30272 ? 480 HOH   A O   1 
HETATM 1738 O O   . HOH   C 3 .   ? -17.38040 -18.45465 -11.77044 1.000 25.05465 ? 481 HOH   A O   1 
HETATM 1739 O O   . HOH   C 3 .   ? -2.25133  -3.02711  -17.86406 1.000 32.84554 ? 482 HOH   A O   1 
HETATM 1740 O O   . HOH   C 3 .   ? -3.38622  -20.86464 -0.64739  1.000 25.15602 ? 483 HOH   A O   1 
HETATM 1741 O O   . HOH   C 3 .   ? -13.84207 -22.19202 -11.75280 1.000 24.27146 ? 484 HOH   A O   1 
HETATM 1742 O O   . HOH   C 3 .   ? 10.10478  -17.37803 -7.34847  1.000 18.54183 ? 485 HOH   A O   1 
HETATM 1743 O O   . HOH   C 3 .   ? 9.90439   -16.44340 -27.12113 1.000 20.42114 ? 486 HOH   A O   1 
HETATM 1744 O O   . HOH   C 3 .   ? -6.16115  -14.46382 -41.06640 1.000 32.36434 ? 487 HOH   A O   1 
HETATM 1745 O O   . HOH   C 3 .   ? 1.17795   -5.46904  -14.38135 1.000 23.48150 ? 488 HOH   A O   1 
HETATM 1746 O O   . HOH   C 3 .   ? -10.20134 -8.54110  -39.13618 1.000 31.76287 ? 489 HOH   A O   1 
HETATM 1747 O O   . HOH   C 3 .   ? 0.63918   -14.33798 -1.09617  1.000 35.99872 ? 490 HOH   A O   1 
HETATM 1748 O O   . HOH   C 3 .   ? 1.23821   -6.62748  -5.54171  1.000 33.97092 ? 491 HOH   A O   1 
HETATM 1749 O O   . HOH   C 3 .   ? -17.93314 -11.24364 -24.93966 1.000 26.73705 ? 492 HOH   A O   1 
HETATM 1750 O O   . HOH   C 3 .   ? 5.81047   -5.88916  -22.39889 1.000 39.43503 ? 493 HOH   A O   1 
HETATM 1751 O O   . HOH   C 3 .   ? 7.51578   -27.41467 -26.98954 1.000 23.57750 ? 494 HOH   A O   1 
HETATM 1752 O O   . HOH   C 3 .   ? -11.80394 -0.79152  -21.34699 1.000 24.50167 ? 495 HOH   A O   1 
HETATM 1753 O O   . HOH   C 3 .   ? -4.82442  -4.87113  -12.22315 1.000 36.61135 ? 496 HOH   A O   1 
HETATM 1754 O O   . HOH   C 3 .   ? 14.14891  -15.30811 -1.55553  1.000 27.29008 ? 497 HOH   A O   1 
HETATM 1755 O O   . HOH   C 3 .   ? 8.99574   -20.45417 -8.77026  1.000 21.84595 ? 498 HOH   A O   1 
HETATM 1756 O O   . HOH   C 3 .   ? 19.04792  -11.61570 -16.97756 1.000 31.84240 ? 499 HOH   A O   1 
HETATM 1757 O O   . HOH   C 3 .   ? 5.28428   -8.26710  -36.19725 1.000 28.60097 ? 500 HOH   A O   1 
HETATM 1758 O O   . HOH   C 3 .   ? -6.83891  4.22315   -34.39389 1.000 34.48212 ? 501 HOH   A O   1 
HETATM 1759 O O   . HOH   C 3 .   ? -13.97371 -11.55603 -30.65215 1.000 24.10707 ? 502 HOH   A O   1 
HETATM 1760 O O   . HOH   C 3 .   ? 7.14992   1.19508   -14.39237 1.000 41.22285 ? 503 HOH   A O   1 
HETATM 1761 O O   . HOH   C 3 .   ? 2.62047   -3.99344  -29.11348 1.000 45.26456 ? 504 HOH   A O   1 
HETATM 1762 O O   . HOH   C 3 .   ? -16.13416 -5.72139  -23.93321 1.000 27.36378 ? 505 HOH   A O   1 
HETATM 1763 O O   . HOH   C 3 .   ? 7.26010   -29.92118 -19.22041 1.000 27.70213 ? 506 HOH   A O   1 
HETATM 1764 O O   . HOH   C 3 .   ? -4.86184  -8.51465  -34.92428 1.000 17.56824 ? 507 HOH   A O   1 
HETATM 1765 O O   . HOH   C 3 .   ? -6.91673  -12.56031 -36.93024 1.000 24.77129 ? 508 HOH   A O   1 
HETATM 1766 O O   . HOH   C 3 .   ? 4.67712   -1.87617  -17.26582 1.000 43.03514 ? 509 HOH   A O   1 
HETATM 1767 O O   . HOH   C 3 .   ? -15.00260 -3.18672  -22.55301 1.000 28.60678 ? 510 HOH   A O   1 
HETATM 1768 O O   . HOH   C 3 .   ? -1.51260  -32.31195 -7.31794  1.000 41.14820 ? 511 HOH   A O   1 
HETATM 1769 O O   . HOH   C 3 .   ? -13.99114 -6.98695  -15.32116 1.000 32.60860 ? 512 HOH   A O   1 
HETATM 1770 O O   . HOH   C 3 .   ? 8.23000   -23.11281 -6.77997  1.000 31.36761 ? 513 HOH   A O   1 
HETATM 1771 O O   . HOH   C 3 .   ? -0.16585  -7.43539  -24.05981 1.000 22.12289 ? 514 HOH   A O   1 
HETATM 1772 O O   . HOH   C 3 .   ? -4.12774  -19.65682 -39.34749 1.000 34.11482 ? 515 HOH   A O   1 
HETATM 1773 O O   . HOH   C 3 .   ? -0.82918  -4.38573  -41.55169 1.000 39.73071 ? 516 HOH   A O   1 
HETATM 1774 O O   . HOH   C 3 .   ? -2.06959  -4.15638  -36.50717 1.000 40.45167 ? 517 HOH   A O   1 
HETATM 1775 O O   . HOH   C 3 .   ? -7.27497  -23.42392 -30.25202 1.000 37.07269 ? 518 HOH   A O   1 
HETATM 1776 O O   . HOH   C 3 .   ? 11.46569  -25.89290 -22.95378 1.000 19.17879 ? 519 HOH   A O   1 
HETATM 1777 O O   . HOH   C 3 .   ? 1.21167   -7.89991  -31.42414 1.000 26.22663 ? 520 HOH   A O   1 
HETATM 1778 O O   . HOH   C 3 .   ? -16.88979 -6.48132  -26.59847 1.000 28.90412 ? 521 HOH   A O   1 
HETATM 1779 O O   . HOH   C 3 .   ? -8.17919  1.32388   -26.60545 1.000 25.02798 ? 522 HOH   A O   1 
HETATM 1780 O O   . HOH   C 3 .   ? -9.08086  -0.72938  -20.70099 1.000 20.39987 ? 523 HOH   A O   1 
HETATM 1781 O O   . HOH   C 3 .   ? -5.66916  -11.17880 -10.41033 1.000 22.84963 ? 524 HOH   A O   1 
HETATM 1782 O O   . HOH   C 3 .   ? -5.51523  -31.14406 -11.44151 1.000 27.91672 ? 525 HOH   A O   1 
HETATM 1783 O O   . HOH   C 3 .   ? -6.83454  -24.55044 -23.15925 1.000 27.21744 ? 526 HOH   A O   1 
HETATM 1784 O O   . HOH   C 3 .   ? -13.54371 -16.57725 -3.15583  1.000 23.45758 ? 527 HOH   A O   1 
HETATM 1785 O O   . HOH   C 3 .   ? 5.43712   -9.75576  -2.57653  1.000 31.10866 ? 528 HOH   A O   1 
HETATM 1786 O O   . HOH   C 3 .   ? -13.04684 -26.60310 -18.12413 1.000 20.95150 ? 529 HOH   A O   1 
HETATM 1787 O O   . HOH   C 3 .   ? 20.789    -17.340   -26.988   1.000 29.69753 ? 530 HOH   A O   1 
HETATM 1788 O O   . HOH   C 3 .   ? 9.96781   -3.98648  -20.94035 1.000 37.15179 ? 531 HOH   A O   1 
HETATM 1789 O O   . HOH   C 3 .   ? 3.42483   -5.50747  -6.24555  1.000 34.59387 ? 532 HOH   A O   1 
HETATM 1790 O O   . HOH   C 3 .   ? -7.57422  -28.01867 -7.55441  1.000 29.73712 ? 533 HOH   A O   1 
HETATM 1791 O O   . HOH   C 3 .   ? 19.08186  -16.46430 -12.87436 1.000 28.48161 ? 534 HOH   A O   1 
HETATM 1792 O O   . HOH   C 3 .   ? -10.21568 -11.06585 -2.69247  1.000 23.24703 ? 535 HOH   A O   1 
HETATM 1793 O O   . HOH   C 3 .   ? -7.72525  -3.82116  -11.59515 1.000 30.26363 ? 536 HOH   A O   1 
HETATM 1794 O O   . HOH   C 3 .   ? -10.08301 -8.11566  -2.14799  1.000 44.29611 ? 537 HOH   A O   1 
HETATM 1795 O O   . HOH   C 3 .   ? -16.25185 -3.61314  -37.19137 1.000 33.65090 ? 538 HOH   A O   1 
HETATM 1796 O O   . HOH   C 3 .   ? -17.98411 -11.69677 -16.08519 1.000 47.94620 ? 539 HOH   A O   1 
HETATM 1797 O O   . HOH   C 3 .   ? -6.38057  1.49894   -20.75143 1.000 32.68978 ? 540 HOH   A O   1 
HETATM 1798 O O   . HOH   C 3 .   ? -1.470    -12.798   -0.073    1.000 44.80263 ? 541 HOH   A O   1 
HETATM 1799 O O   . HOH   C 3 .   ? -10.48153 -6.24533  -3.62128  1.000 42.05514 ? 542 HOH   A O   1 
HETATM 1800 O O   . HOH   C 3 .   ? 12.86186  -28.57836 -33.72465 1.000 22.36869 ? 543 HOH   A O   1 
HETATM 1801 O O   . HOH   C 3 .   ? 4.96068   -9.44607  -20.21932 1.000 17.80875 ? 544 HOH   A O   1 
HETATM 1802 O O   . HOH   C 3 .   ? -12.62436 -27.22213 -35.55857 1.000 38.78113 ? 545 HOH   A O   1 
HETATM 1803 O O   . HOH   C 3 .   ? -5.46521  -5.62931  -3.28035  1.000 38.13902 ? 546 HOH   A O   1 
HETATM 1804 O O   . HOH   C 3 .   ? 14.24087  -24.99641 -8.72773  1.000 41.81716 ? 547 HOH   A O   1 
HETATM 1805 O O   . HOH   C 3 .   ? 17.74259  -27.51196 -20.41935 1.000 38.72123 ? 548 HOH   A O   1 
HETATM 1806 O O   . HOH   C 3 .   ? -0.02552  -26.78646 -32.33009 1.000 36.49494 ? 549 HOH   A O   1 
HETATM 1807 O O   . HOH   C 3 .   ? 16.24935  -20.75686 -18.09673 1.000 25.04177 ? 550 HOH   A O   1 
HETATM 1808 O O   . HOH   C 3 .   ? -4.03952  -14.51880 -22.92305 1.000 16.60041 ? 551 HOH   A O   1 
HETATM 1809 O O   . HOH   C 3 .   ? 8.30539   -7.60986  -24.21993 1.000 29.26888 ? 552 HOH   A O   1 
HETATM 1810 O O   . HOH   C 3 .   ? -19.24973 -19.23090 -14.65183 1.000 19.61073 ? 553 HOH   A O   1 
HETATM 1811 O O   . HOH   C 3 .   ? -7.14966  -18.90692 -37.03908 1.000 35.76317 ? 554 HOH   A O   1 
HETATM 1812 O O   . HOH   C 3 .   ? 0.98502   -27.75274 -30.10181 1.000 39.35259 ? 555 HOH   A O   1 
HETATM 1813 O O   . HOH   C 3 .   ? -19.904   -14.192   -19.697   1.000 40.60524 ? 556 HOH   A O   1 
HETATM 1814 O O   . HOH   C 3 .   ? 5.20427   -30.50661 -11.23619 1.000 31.91421 ? 557 HOH   A O   1 
HETATM 1815 O O   . HOH   C 3 .   ? -3.02563  -27.00260 -30.15300 1.000 41.37172 ? 558 HOH   A O   1 
HETATM 1816 O O   . HOH   C 3 .   ? 16.07182  -4.06970  -25.20259 1.000 45.48466 ? 559 HOH   A O   1 
HETATM 1817 O O   . HOH   C 3 .   ? 3.08465   -30.32387 -18.38948 1.000 40.74239 ? 560 HOH   A O   1 
HETATM 1818 O O   . HOH   C 3 .   ? 4.44523   -6.96399  -18.17392 1.000 20.27103 ? 561 HOH   A O   1 
HETATM 1819 O O   . HOH   C 3 .   ? 11.23063  -11.28798 -4.49782  1.000 22.00145 ? 562 HOH   A O   1 
HETATM 1820 O O   . HOH   C 3 .   ? 11.72805  -26.33887 -25.94169 1.000 23.28011 ? 563 HOH   A O   1 
HETATM 1821 O O   . HOH   C 3 .   ? -13.16296 -0.72236  -15.30812 1.000 28.59095 ? 564 HOH   A O   1 
HETATM 1822 O O   . HOH   C 3 .   ? -5.92183  0.79669   -37.55038 1.000 28.20490 ? 565 HOH   A O   1 
HETATM 1823 O O   . HOH   C 3 .   ? -2.68185  -15.25423 -0.31472  1.000 33.12938 ? 566 HOH   A O   1 
HETATM 1824 O O   . HOH   C 3 .   ? -13.80634 -12.37238 -8.53557  1.000 21.11635 ? 567 HOH   A O   1 
HETATM 1825 O O   . HOH   C 3 .   ? -2.40330  -13.27130 -21.05265 1.000 19.85018 ? 568 HOH   A O   1 
HETATM 1826 O O   . HOH   C 3 .   ? -20.352   -28.095   -12.041   1.000 46.63440 ? 569 HOH   A O   1 
HETATM 1827 O O   . HOH   C 3 .   ? -12.85461 -18.89327 -24.81653 1.000 23.70283 ? 570 HOH   A O   1 
HETATM 1828 O O   . HOH   C 3 .   ? 0.91492   -29.89513 -15.56867 1.000 30.49319 ? 571 HOH   A O   1 
HETATM 1829 O O   . HOH   C 3 .   ? 5.55087   -12.54345 -38.52909 1.000 25.45821 ? 572 HOH   A O   1 
HETATM 1830 O O   . HOH   C 3 .   ? 5.60388   -5.19257  -3.22835  1.000 31.93531 ? 573 HOH   A O   1 
HETATM 1831 O O   . HOH   C 3 .   ? 14.42375  -20.84857 -20.08654 1.000 20.32013 ? 574 HOH   A O   1 
HETATM 1832 O O   . HOH   C 3 .   ? 3.84901   -7.02875  -20.79140 1.000 35.68016 ? 575 HOH   A O   1 
HETATM 1833 O O   . HOH   C 3 .   ? 8.97047   -20.22080 -3.83737  1.000 22.81805 ? 576 HOH   A O   1 
HETATM 1834 O O   . HOH   C 3 .   ? 22.99705  -9.12451  -27.65370 1.000 59.54519 ? 577 HOH   A O   1 
HETATM 1835 O O   . HOH   C 3 .   ? 0.29629   -5.25062  -34.13050 1.000 34.09076 ? 578 HOH   A O   1 
HETATM 1836 O O   . HOH   C 3 .   ? 5.05665   -1.32077  -6.11165  1.000 39.90422 ? 579 HOH   A O   1 
HETATM 1837 O O   . HOH   C 3 .   ? 15.29278  -23.04925 -16.64220 1.000 26.35222 ? 580 HOH   A O   1 
HETATM 1838 O O   . HOH   C 3 .   ? -0.46310  -30.31845 -17.32219 1.000 38.68721 ? 581 HOH   A O   1 
HETATM 1839 O O   . HOH   C 3 .   ? -11.16753 -20.86454 -25.64938 1.000 37.66878 ? 582 HOH   A O   1 
HETATM 1840 O O   . HOH   C 3 .   ? 5.81429   -20.70195 -40.35417 1.000 36.54976 ? 583 HOH   A O   1 
HETATM 1841 O O   . HOH   C 3 .   ? -11.65405 -12.83851 -31.73089 1.000 26.00250 ? 584 HOH   A O   1 
HETATM 1842 O O   . HOH   C 3 .   ? 0.43605   -12.74409 -21.53927 1.000 16.88070 ? 585 HOH   A O   1 
HETATM 1843 O O   . HOH   C 3 .   ? -18.17641 -11.03979 -33.78179 1.000 37.47173 ? 586 HOH   A O   1 
HETATM 1844 O O   . HOH   C 3 .   ? -4.98912  -16.13689 -41.86885 1.000 44.96347 ? 587 HOH   A O   1 
HETATM 1845 O O   . HOH   C 3 .   ? 15.91562  -17.76423 -2.88073  1.000 28.57342 ? 588 HOH   A O   1 
HETATM 1846 O O   . HOH   C 3 .   ? -6.14735  -13.64572 0.60122   1.000 24.24650 ? 589 HOH   A O   1 
HETATM 1847 O O   . HOH   C 3 .   ? 3.79905   -22.73862 -3.07455  1.000 28.57150 ? 590 HOH   A O   1 
HETATM 1848 O O   . HOH   C 3 .   ? 5.96143   -29.10157 -7.97799  1.000 41.39089 ? 591 HOH   A O   1 
HETATM 1849 O O   . HOH   C 3 .   ? -14.95601 -25.20009 -11.07132 1.000 30.53948 ? 592 HOH   A O   1 
HETATM 1850 O O   . HOH   C 3 .   ? 4.91387   -31.33857 -20.22515 1.000 38.89697 ? 593 HOH   A O   1 
HETATM 1851 O O   . HOH   C 3 .   ? -14.30982 -12.40299 -12.79588 1.000 39.98216 ? 594 HOH   A O   1 
HETATM 1852 O O   . HOH   C 3 .   ? -9.12010  -27.98045 -5.96067  1.000 44.73036 ? 595 HOH   A O   1 
HETATM 1853 O O   . HOH   C 3 .   ? -14.54763 -28.99660 -17.45843 1.000 28.59611 ? 596 HOH   A O   1 
HETATM 1854 O O   . HOH   C 3 .   ? 21.97266  -7.63732  -28.42308 1.000 51.39055 ? 597 HOH   A O   1 
HETATM 1855 O O   . HOH   C 3 .   ? 21.77755  -14.56998 -26.09194 1.000 35.63722 ? 598 HOH   A O   1 
HETATM 1856 O O   . HOH   C 3 .   ? 18.38775  0.69190   -2.68852  1.000 41.59202 ? 599 HOH   A O   1 
HETATM 1857 O O   . HOH   C 3 .   ? -12.99746 -16.55777 -26.56098 1.000 27.42600 ? 600 HOH   A O   1 
HETATM 1858 O O   . HOH   C 3 .   ? 14.31161  -1.36901  -5.88703  1.000 36.94553 ? 601 HOH   A O   1 
HETATM 1859 O O   . HOH   C 3 .   ? -10.85001 -21.40115 -30.46503 1.000 41.76127 ? 602 HOH   A O   1 
HETATM 1860 O O   . HOH   C 3 .   ? -15.70393 -8.58776  -15.33218 1.000 41.04284 ? 603 HOH   A O   1 
HETATM 1861 O O   . HOH   C 3 .   ? -2.22507  -11.30996 -24.10602 1.000 22.59279 ? 604 HOH   A O   1 
HETATM 1862 O O   . HOH   C 3 .   ? -16.18760 -5.70858  -37.85813 1.000 44.44373 ? 605 HOH   A O   1 
HETATM 1863 O O   . HOH   C 3 .   ? -16.22768 -3.97137  -30.46304 1.000 35.28759 ? 606 HOH   A O   1 
HETATM 1864 O O   . HOH   C 3 .   ? 0.25333   -16.36236 -3.39593  1.000 19.98866 ? 607 HOH   A O   1 
HETATM 1865 O O   . HOH   C 3 .   ? -13.44352 -25.50357 -7.77348  1.000 29.09550 ? 608 HOH   A O   1 
HETATM 1866 O O   . HOH   C 3 .   ? 0.75605   -31.51759 -22.27076 1.000 37.88373 ? 609 HOH   A O   1 
HETATM 1867 O O   . HOH   C 3 .   ? 1.83584   -18.04958 0.11081   1.000 27.12013 ? 610 HOH   A O   1 
HETATM 1868 O O   . HOH   C 3 .   ? 12.10442  -19.19584 -38.43414 1.000 34.60726 ? 611 HOH   A O   1 
HETATM 1869 O O   . HOH   C 3 .   ? -2.03423  -1.21546  -25.13379 1.000 38.39772 ? 612 HOH   A O   1 
HETATM 1870 O O   . HOH   C 3 .   ? 7.110     1.930     -12.399   1.000 50.10074 ? 613 HOH   A O   1 
HETATM 1871 O O   . HOH   C 3 .   ? -15.42652 -4.28595  -16.89539 1.000 38.13768 ? 614 HOH   A O   1 
HETATM 1872 O O   . HOH   C 3 .   ? -3.29340  -25.55141 -39.31960 1.000 53.95036 ? 615 HOH   A O   1 
HETATM 1873 O O   . HOH   C 3 .   ? -0.36582  -8.90062  -28.06927 1.000 27.26401 ? 616 HOH   A O   1 
HETATM 1874 O O   . HOH   C 3 .   ? -14.02270 -23.66516 -5.32475  1.000 29.00519 ? 617 HOH   A O   1 
HETATM 1875 O O   . HOH   C 3 .   ? 24.20486  -6.77521  -24.57234 1.000 46.02039 ? 618 HOH   A O   1 
HETATM 1876 O O   . HOH   C 3 .   ? 13.24310  -0.98717  -19.87800 1.000 25.84871 ? 619 HOH   A O   1 
HETATM 1877 O O   . HOH   C 3 .   ? -19.205   -12.803   -16.926   1.000 48.02168 ? 620 HOH   A O   1 
HETATM 1878 O O   . HOH   C 3 .   ? 13.55896  -27.72666 -18.62279 1.000 40.63320 ? 621 HOH   A O   1 
HETATM 1879 O O   . HOH   C 3 .   ? -4.71727  -5.99746  -36.41115 1.000 27.27357 ? 622 HOH   A O   1 
HETATM 1880 O O   . HOH   C 3 .   ? 1.17511   -8.41966  -4.05772  1.000 27.76752 ? 623 HOH   A O   1 
HETATM 1881 O O   . HOH   C 3 .   ? 5.63826   -22.01673 -38.36426 1.000 39.53528 ? 624 HOH   A O   1 
HETATM 1882 O O   . HOH   C 3 .   ? 18.370    -25.335   -24.321   1.000 30.72144 ? 625 HOH   A O   1 
HETATM 1883 O O   . HOH   C 3 .   ? -11.60416 -19.46678 -29.43036 1.000 48.76785 ? 626 HOH   A O   1 
HETATM 1884 O O   . HOH   C 3 .   ? -13.17352 -24.64067 -11.22034 1.000 33.94312 ? 627 HOH   A O   1 
HETATM 1885 O O   . HOH   C 3 .   ? -16.06798 -4.78166  -18.67805 1.000 41.20971 ? 628 HOH   A O   1 
HETATM 1886 O O   . HOH   C 3 .   ? 3.63710   -4.21710  -8.92813  1.000 35.32628 ? 629 HOH   A O   1 
HETATM 1887 O O   . HOH   C 3 .   ? -14.88329 -0.33365  -31.80294 1.000 39.55033 ? 630 HOH   A O   1 
HETATM 1888 O O   . HOH   C 3 .   ? -1.50663  -27.39565 -24.29833 1.000 34.86404 ? 631 HOH   A O   1 
HETATM 1889 O O   . HOH   C 3 .   ? -11.84532 -26.97068 -20.39112 1.000 27.23315 ? 632 HOH   A O   1 
HETATM 1890 O O   . HOH   C 3 .   ? 1.91752   -4.72279  -16.89515 1.000 31.17032 ? 633 HOH   A O   1 
HETATM 1891 O O   . HOH   C 3 .   ? 19.731    -22.564   -12.696   1.000 36.93014 ? 634 HOH   A O   1 
HETATM 1892 O O   . HOH   C 3 .   ? -4.23569  -13.66495 -42.11240 1.000 43.98488 ? 635 HOH   A O   1 
HETATM 1893 O O   . HOH   C 3 .   ? -9.80952  -23.78137 -26.59555 1.000 44.72321 ? 636 HOH   A O   1 
HETATM 1894 O O   . HOH   C 3 .   ? -11.72955 -32.41658 -19.78116 1.000 48.93988 ? 637 HOH   A O   1 
HETATM 1895 O O   . HOH   C 3 .   ? 10.98812  -8.09944  -37.15314 1.000 47.23793 ? 638 HOH   A O   1 
HETATM 1896 O O   . HOH   C 3 .   ? -11.288   -7.209    0.708     1.000 45.27492 ? 639 HOH   A O   1 
HETATM 1897 O O   . HOH   C 3 .   ? 7.21976   -1.31832  -18.28442 1.000 35.68013 ? 640 HOH   A O   1 
HETATM 1898 O O   . HOH   C 3 .   ? -9.15014  -6.98491  -42.60417 1.000 50.39800 ? 641 HOH   A O   1 
HETATM 1899 O O   . HOH   C 3 .   ? -6.693    -22.659   -2.008    1.000 34.79088 ? 642 HOH   A O   1 
HETATM 1900 O O   . HOH   C 3 .   ? 18.68681  -18.43377 -10.71010 1.000 40.67338 ? 643 HOH   A O   1 
HETATM 1901 O O   . HOH   C 3 .   ? 18.71054  -10.06980 -9.52142  1.000 37.04953 ? 644 HOH   A O   1 
HETATM 1902 O O   . HOH   C 3 .   ? 0.30610   -18.56980 -1.91338  1.000 31.51874 ? 645 HOH   A O   1 
HETATM 1903 O O   . HOH   C 3 .   ? -0.92409  -11.34857 -25.72567 1.000 21.65716 ? 646 HOH   A O   1 
HETATM 1904 O O   . HOH   C 3 .   ? 9.18231   -26.55117 -25.23745 1.000 28.23335 ? 647 HOH   A O   1 
HETATM 1905 O O   . HOH   C 3 .   ? -4.06068  -3.56117  -16.31536 1.000 37.27971 ? 648 HOH   A O   1 
HETATM 1906 O O   . HOH   C 3 .   ? 18.35135  -21.82582 -19.07685 1.000 28.26265 ? 649 HOH   A O   1 
HETATM 1907 O O   . HOH   C 3 .   ? 15.23753  -12.68522 -6.66549  1.000 33.07727 ? 650 HOH   A O   1 
HETATM 1908 O O   . HOH   C 3 .   ? 2.55890   -3.68800  -12.99737 1.000 33.62975 ? 651 HOH   A O   1 
HETATM 1909 O O   . HOH   C 3 .   ? 3.48284   -1.09844  -14.92725 1.000 45.97789 ? 652 HOH   A O   1 
HETATM 1910 O O   . HOH   C 3 .   ? -12.13421 -12.19565 -40.87296 1.000 43.10274 ? 653 HOH   A O   1 
HETATM 1911 O O   . HOH   C 3 .   ? -9.54355  -17.97356 -37.75428 1.000 45.36493 ? 654 HOH   A O   1 
HETATM 1912 O O   . HOH   C 3 .   ? 8.871     -1.200    -18.818   1.000 44.60814 ? 655 HOH   A O   1 
HETATM 1913 O O   . HOH   C 3 .   ? -1.03245  -4.79415  -13.53335 1.000 32.43104 ? 656 HOH   A O   1 
HETATM 1914 O O   . HOH   C 3 .   ? 13.443    -26.707   -37.415   1.000 35.21302 ? 657 HOH   A O   1 
HETATM 1915 O O   . HOH   C 3 .   ? -15.33134 -14.02654 -29.76324 1.000 39.71816 ? 658 HOH   A O   1 
HETATM 1916 O O   . HOH   C 3 .   ? -0.676    5.342     -31.592   1.000 43.22378 ? 659 HOH   A O   1 
HETATM 1917 O O   . HOH   C 3 .   ? -7.80692  2.87800   -22.45193 1.000 36.54291 ? 660 HOH   A O   1 
HETATM 1918 O O   . HOH   C 3 .   ? 23.212    -16.996   -14.759   1.000 49.52333 ? 661 HOH   A O   1 
HETATM 1919 O O   . HOH   C 3 .   ? -1.929    1.315     -33.251   1.000 42.79384 ? 662 HOH   A O   1 
HETATM 1920 O O   . HOH   C 3 .   ? -3.59697  -4.98720  -14.25614 1.000 34.50262 ? 663 HOH   A O   1 
HETATM 1921 O O   . HOH   C 3 .   ? 16.83186  -0.15166  -9.33588  1.000 37.27699 ? 664 HOH   A O   1 
HETATM 1922 O O   . HOH   C 3 .   ? -13.81258 -13.96114 -3.53542  1.000 29.09077 ? 665 HOH   A O   1 
HETATM 1923 O O   . HOH   C 3 .   ? 0.73120   -29.38984 -36.92291 1.000 46.94844 ? 666 HOH   A O   1 
HETATM 1924 O O   . HOH   C 3 .   ? -7.69967  -7.08035  -40.60695 1.000 48.89992 ? 667 HOH   A O   1 
HETATM 1925 O O   . HOH   C 3 .   ? 21.265    -19.483   -26.999   1.000 46.60828 ? 668 HOH   A O   1 
HETATM 1926 O O   . HOH   C 3 .   ? -3.42738  -26.73397 -3.06682  1.000 42.28593 ? 669 HOH   A O   1 
HETATM 1927 O O   . HOH   C 3 .   ? -3.34268  0.72696   -27.04410 1.000 40.85224 ? 670 HOH   A O   1 
HETATM 1928 O O   . HOH   C 3 .   ? -15.594   -0.404    -19.101   1.000 32.06366 ? 671 HOH   A O   1 
HETATM 1929 O O   . HOH   C 3 .   ? -9.31356  -26.20143 -20.88819 1.000 26.99895 ? 672 HOH   A O   1 
HETATM 1930 O O   . HOH   C 3 .   ? 19.58870  -8.99741  -17.15752 1.000 30.89837 ? 673 HOH   A O   1 
HETATM 1931 O O   . HOH   C 3 .   ? 6.57611   1.69320   -16.67325 1.000 38.60707 ? 674 HOH   A O   1 
HETATM 1932 O O   . HOH   C 3 .   ? -12.420   -9.599    1.215     1.000 32.85718 ? 675 HOH   A O   1 
HETATM 1933 O O   . HOH   C 3 .   ? -13.92560 -9.61760  -9.22508  1.000 32.83878 ? 676 HOH   A O   1 
HETATM 1934 O O   . HOH   C 3 .   ? 20.738    -20.280   -11.896   1.000 39.89522 ? 677 HOH   A O   1 
HETATM 1935 O O   . HOH   C 3 .   ? 21.67750  -7.66486  -11.55557 1.000 40.90981 ? 678 HOH   A O   1 
HETATM 1936 O O   . HOH   C 3 .   ? -11.22407 -17.06550 -28.45438 1.000 32.80037 ? 679 HOH   A O   1 
HETATM 1937 O O   . HOH   C 3 .   ? -6.55059  -30.44155 -8.76359  1.000 34.80751 ? 680 HOH   A O   1 
HETATM 1938 O O   . HOH   C 3 .   ? 11.03962  -22.14061 -3.96391  1.000 35.85820 ? 681 HOH   A O   1 
HETATM 1939 O O   . HOH   C 3 .   ? -9.67938  -10.94573 -40.45405 1.000 49.98522 ? 682 HOH   A O   1 
HETATM 1940 O O   . HOH   C 3 .   ? 3.31239   -7.05666  -25.27279 1.000 42.91565 ? 683 HOH   A O   1 
HETATM 1941 O O   . HOH   C 3 .   ? -15.45914 -1.84462  -16.61657 1.000 27.93166 ? 684 HOH   A O   1 
HETATM 1942 O O   . HOH   C 3 .   ? -0.33903  -8.62781  -2.15715  1.000 40.40988 ? 685 HOH   A O   1 
HETATM 1943 O O   . HOH   C 3 .   ? -14.02309 -11.35835 -0.63196  1.000 36.82618 ? 686 HOH   A O   1 
HETATM 1944 O O   . HOH   C 3 .   ? 19.58747  -4.21372  -22.24677 1.000 37.75714 ? 687 HOH   A O   1 
HETATM 1945 O O   . HOH   C 3 .   ? 2.75232   -3.76134  -11.09126 1.000 48.02567 ? 688 HOH   A O   1 
HETATM 1946 O O   . HOH   C 3 .   ? -4.02917  2.26172   -36.02980 1.000 31.60932 ? 689 HOH   A O   1 
HETATM 1947 O O   . HOH   C 3 .   ? 22.35331  -3.85451  -9.22952  1.000 52.40657 ? 690 HOH   A O   1 
HETATM 1948 O O   . HOH   C 3 .   ? 7.26601   -30.54761 -24.19924 1.000 34.97947 ? 691 HOH   A O   1 
HETATM 1949 O O   . HOH   C 3 .   ? 6.12974   -23.40006 -2.90127  1.000 42.52428 ? 692 HOH   A O   1 
HETATM 1950 O O   . HOH   C 3 .   ? 6.88453   -21.22319 -2.34274  1.000 28.44642 ? 693 HOH   A O   1 
HETATM 1951 O O   . HOH   C 3 .   ? -17.90313 -11.60787 -22.02975 1.000 29.25894 ? 694 HOH   A O   1 
HETATM 1952 O O   . HOH   C 3 .   ? -5.99509  -19.41070 -38.52533 1.000 52.04616 ? 695 HOH   A O   1 
HETATM 1953 O O   . HOH   C 3 .   ? -4.522    -0.900    -18.143   1.000 39.78130 ? 696 HOH   A O   1 
HETATM 1954 O O   . HOH   C 3 .   ? 7.67835   -13.60928 -39.69347 1.000 32.70881 ? 697 HOH   A O   1 
HETATM 1955 O O   . HOH   C 3 .   ? 18.46445  -3.92550  -24.75401 1.000 39.12529 ? 698 HOH   A O   1 
HETATM 1956 O O   . HOH   C 3 .   ? -1.07933  -29.32569 -3.21146  1.000 39.93418 ? 699 HOH   A O   1 
HETATM 1957 O O   . HOH   C 3 .   ? 20.11677  -21.96296 -20.98026 1.000 37.60020 ? 700 HOH   A O   1 
HETATM 1958 O O   . HOH   C 3 .   ? 14.64637  -27.33118 -16.77399 1.000 47.43739 ? 701 HOH   A O   1 
HETATM 1959 O O   . HOH   C 3 .   ? -14.41295 -1.05844  -13.15175 1.000 35.46345 ? 702 HOH   A O   1 
HETATM 1960 O O   . HOH   C 3 .   ? 16.705    -9.953    -2.282    1.000 46.31153 ? 703 HOH   A O   1 
HETATM 1961 O O   . HOH   C 3 .   ? 10.86243  -29.76844 -23.15548 1.000 49.18366 ? 704 HOH   A O   1 
HETATM 1962 O O   . HOH   C 3 .   ? 9.95160   -14.56368 -37.99150 1.000 38.29788 ? 705 HOH   A O   1 
HETATM 1963 O O   . HOH   C 3 .   ? 2.29147   -8.51347  -27.07372 1.000 40.51641 ? 706 HOH   A O   1 
HETATM 1964 O O   . HOH   C 3 .   ? 23.601    -16.230   -18.705   1.000 40.06826 ? 707 HOH   A O   1 
HETATM 1965 O O   . HOH   C 3 .   ? 18.41251  -24.15894 -17.40508 1.000 38.84800 ? 708 HOH   A O   1 
HETATM 1966 O O   . HOH   C 3 .   ? -17.64666 -2.64797  -38.89996 1.000 47.58238 ? 709 HOH   A O   1 
HETATM 1967 O O   . HOH   C 3 .   ? 21.28197  -6.46066  -21.04486 1.000 43.89477 ? 710 HOH   A O   1 
HETATM 1968 O O   . HOH   C 3 .   ? 11.96510  -28.53542 -27.06842 1.000 35.30220 ? 711 HOH   A O   1 
HETATM 1969 O O   . HOH   C 3 .   ? 13.02866  -30.92190 -33.36641 1.000 37.68758 ? 712 HOH   A O   1 
HETATM 1970 O O   . HOH   C 3 .   ? 12.23628  -28.63661 -22.49611 1.000 37.69176 ? 713 HOH   A O   1 
HETATM 1971 O O   . HOH   C 3 .   ? 12.28812  -1.13190  -17.50499 1.000 31.24858 ? 714 HOH   A O   1 
HETATM 1972 O O   . HOH   C 3 .   ? 11.49549  -11.06109 -36.91018 1.000 47.69442 ? 715 HOH   A O   1 
HETATM 1973 O O   . HOH   C 3 .   ? 11.35072  -13.02610 -36.61041 1.000 49.75453 ? 716 HOH   A O   1 
HETATM 1974 O O   . HOH   C 3 .   ? 1.86313   -30.82191 -32.56957 1.000 44.25984 ? 717 HOH   A O   1 
HETATM 1975 O O   . HOH   C 3 .   ? 2.48095   -1.06202  -29.00040 1.000 34.30582 ? 718 HOH   A O   1 
HETATM 1976 O O   . HOH   C 3 .   ? 0.63016   -3.02432  -31.18112 1.000 32.52452 ? 719 HOH   A O   1 
HETATM 1977 O O   . HOH   C 3 .   ? 13.62213  -25.22669 -15.09391 1.000 37.76430 ? 720 HOH   A O   1 
HETATM 1978 O O   . HOH   C 3 .   ? 4.83670   -3.26440  -4.72528  1.000 35.97384 ? 721 HOH   A O   1 
HETATM 1979 O O   . HOH   C 3 .   ? 8.84300   -29.65561 -27.19122 1.000 32.24052 ? 722 HOH   A O   1 
HETATM 1980 O O   . HOH   C 3 .   ? -14.77945 -2.42818  -29.87304 1.000 42.95165 ? 723 HOH   A O   1 
HETATM 1981 O O   . HOH   C 3 .   ? -15.87400 -12.05277 -6.99417  1.000 35.28940 ? 724 HOH   A O   1 
HETATM 1982 O O   . HOH   C 3 .   ? -14.04960 -9.81729  -12.31728 1.000 36.54499 ? 725 HOH   A O   1 
HETATM 1983 O O   . HOH   C 3 .   ? -6.100    3.061     -25.770   1.000 45.26811 ? 726 HOH   A O   1 
HETATM 1984 O O   . HOH   C 3 .   ? -9.75659  -24.45299 -23.18427 1.000 45.51119 ? 727 HOH   A O   1 
HETATM 1985 O O   . HOH   C 3 .   ? 1.42681   -2.91408  -8.97069  1.000 38.76896 ? 728 HOH   A O   1 
HETATM 1986 O O   . HOH   C 3 .   ? 9.96827   -25.54449 -13.87495 1.000 41.90575 ? 729 HOH   A O   1 
HETATM 1987 O O   . HOH   C 3 .   ? 10.38553  -30.42879 -29.34566 1.000 48.42789 ? 730 HOH   A O   1 
HETATM 1988 O O   . HOH   C 3 .   ? -19.84631 -12.13364 -25.91791 1.000 36.53224 ? 731 HOH   A O   1 
HETATM 1989 O O   . HOH   C 3 .   ? -12.15821 -12.73764 -1.74560  1.000 26.65359 ? 732 HOH   A O   1 
HETATM 1990 O O   . HOH   C 3 .   ? 19.17416  -1.72081  -20.84148 1.000 39.97391 ? 733 HOH   A O   1 
HETATM 1991 O O   . HOH   C 3 .   ? -13.83861 -13.87398 -10.77985 1.000 30.78773 ? 734 HOH   A O   1 
HETATM 1992 O O   . HOH   C 3 .   ? -3.72698  -28.18958 -23.11722 1.000 32.95297 ? 735 HOH   A O   1 
HETATM 1993 O O   . HOH   C 3 .   ? -4.110    2.914     -20.210   1.000 38.53307 ? 736 HOH   A O   1 
HETATM 1994 O O   . HOH   C 3 .   ? 18.04086  -10.95343 -7.29152  1.000 38.41592 ? 737 HOH   A O   1 
HETATM 1995 O O   . HOH   C 3 .   ? 23.32463  -5.73821  -9.94703  1.000 53.64852 ? 738 HOH   A O   1 
HETATM 1996 O O   . HOH   C 3 .   ? -0.66418  -1.65627  -14.39359 1.000 46.38282 ? 739 HOH   A O   1 
HETATM 1997 O O   . HOH   C 3 .   ? 5.90860   -4.09432  -0.52616  1.000 42.11372 ? 740 HOH   A O   1 
HETATM 1998 O O   . HOH   C 3 .   ? -8.57628  -10.70709 -0.43463  1.000 45.80580 ? 741 HOH   A O   1 
HETATM 1999 O O   . HOH   C 3 .   ? 13.99276  -11.56761 -4.70773  1.000 26.93702 ? 742 HOH   A O   1 
HETATM 2000 O O   . HOH   C 3 .   ? 21.44871  -19.29244 -22.13456 1.000 43.39941 ? 743 HOH   A O   1 
HETATM 2001 O O   . HOH   C 3 .   ? 19.20712  -14.74115 -8.29989  1.000 47.61441 ? 744 HOH   A O   1 
HETATM 2002 O O   . HOH   C 3 .   ? 21.13047  -10.29757 -11.36965 1.000 43.13795 ? 745 HOH   A O   1 
HETATM 2003 O O   . HOH   C 3 .   ? -19.61325 -7.55612  -27.11434 1.000 48.61975 ? 746 HOH   A O   1 
HETATM 2004 O O   . HOH   C 3 .   ? 16.08411  -19.35744 -0.23757  1.000 41.92903 ? 747 HOH   A O   1 
HETATM 2005 O O   . HOH   C 3 .   ? -10.502   -11.610   1.750     1.000 25.00697 ? 748 HOH   A O   1 
HETATM 2006 O O   . HOH   C 3 .   ? -4.781    -5.921    -1.339    1.000 44.77321 ? 749 HOH   A O   1 
HETATM 2007 O O   . HOH   C 3 .   ? 21.536    -21.583   -25.270   1.000 38.44511 ? 750 HOH   A O   1 
HETATM 2008 O O   . HOH   C 3 .   ? -3.50424  -10.05154 -44.94046 1.000 46.45391 ? 751 HOH   A O   1 
HETATM 2009 O O   . HOH   C 3 .   ? -6.79597  -24.51661 -25.93702 1.000 38.94953 ? 752 HOH   A O   1 
HETATM 2010 O O   . HOH   C 3 .   ? -16.64319 -15.21651 -10.97948 1.000 32.18008 ? 753 HOH   A O   1 
HETATM 2011 O O   . HOH   C 3 .   ? 15.07244  -12.89992 -2.50274  1.000 33.75562 ? 754 HOH   A O   1 
HETATM 2012 O O   . HOH   C 3 .   ? 6.26453   -5.96636  -24.93529 1.000 36.37715 ? 755 HOH   A O   1 
HETATM 2013 O O   . HOH   C 3 .   ? 19.75930  -12.98228 -7.16219  1.000 43.48056 ? 756 HOH   A O   1 
HETATM 2014 O O   . HOH   C 3 .   ? -19.05122 -5.42731  -20.90594 1.000 46.52142 ? 757 HOH   A O   1 
HETATM 2015 O O   . HOH   C 3 .   ? -15.60796 -1.59511  -27.38057 1.000 43.55092 ? 758 HOH   A O   1 
HETATM 2016 O O   . HOH   C 3 .   ? -19.11692 -8.87376  -25.07279 1.000 39.30490 ? 759 HOH   A O   1 
HETATM 2017 O O   . HOH   C 3 .   ? 3.84449   0.84387   -14.00978 1.000 43.52332 ? 760 HOH   A O   1 
HETATM 2018 O O   . HOH   C 3 .   ? -0.00000  -0.00000  -28.46890 0.50  41.89745 ? 761 HOH   A O   1 
HETATM 2019 O O   . HOH   C 3 .   ? -19.81817 -10.48634 -20.92886 1.000 39.97509 ? 762 HOH   A O   1 
HETATM 2020 O O   . HOH   C 3 .   ? 16.29757  0.95322   -7.56418  1.000 39.98497 ? 763 HOH   A O   1 
HETATM 2021 O O   . HOH   C 3 .   ? -8.28669  -29.00797 -28.97756 1.000 52.11393 ? 764 HOH   A O   1 
HETATM 2022 O O   . HOH   C 3 .   ? 12.16192  -30.12678 -25.17131 1.000 49.04434 ? 765 HOH   A O   1 
HETATM 2023 O O   . HOH   C 3 .   ? -17.00488 -7.30285  -11.38689 1.000 48.32504 ? 766 HOH   A O   1 
HETATM 2024 O O   . HOH   C 3 .   ? 9.04172   -8.66794  -39.16213 1.000 40.24184 ? 767 HOH   A O   1 
HETATM 2025 O O   . HOH   C 3 .   ? -20.11052 -9.84336  -18.14309 1.000 46.21315 ? 768 HOH   A O   1 
HETATM 2026 O O   . HOH   C 3 .   ? -10.79641 -25.80531 -39.18731 1.000 54.34066 ? 769 HOH   A O   1 
HETATM 2027 O O   . HOH   C 3 .   ? 18.54738  0.56702   -22.16269 1.000 44.60239 ? 770 HOH   A O   1 
HETATM 2028 O O   . HOH   C 3 .   ? 3.02728   -12.85851 -45.33666 1.000 52.86212 ? 771 HOH   A O   1 
HETATM 2029 O O   . HOH   C 3 .   ? 1.37517   -31.96021 -30.19232 1.000 45.36876 ? 772 HOH   A O   1 
HETATM 2030 O O   . HOH   C 3 .   ? 1.01770   -2.14243  -11.60905 1.000 43.86159 ? 773 HOH   A O   1 
HETATM 2031 O O   . HOH   C 3 .   ? -16.11495 -11.64246 0.72714   1.000 49.82941 ? 774 HOH   A O   1 
HETATM 2032 O O   . HOH   C 3 .   ? -17.99967 -7.24716  -8.60582  1.000 44.07024 ? 775 HOH   A O   1 
HETATM 2033 O O   . HOH   C 3 .   ? -20.30755 -4.28711  -24.19184 1.000 45.60901 ? 776 HOH   A O   1 
HETATM 2034 O O   . HOH   C 3 .   ? -22.61797 -5.71352  -24.18287 1.000 50.95903 ? 777 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   ? 0.55995 0.65902 0.42030 -0.11752 -0.02447 -0.20781 16  GLU A N   
2    C CA  . GLU A 9   ? 0.61191 0.68429 0.46074 -0.09027 -0.02582 -0.19259 16  GLU A CA  
3    C C   . GLU A 9   ? 0.54007 0.61254 0.40674 -0.07728 -0.02781 -0.17404 16  GLU A C   
4    O O   . GLU A 9   ? 0.58206 0.70002 0.46288 -0.06678 -0.03701 -0.16465 16  GLU A O   
5    C CB  . GLU A 9   ? 0.70563 0.81506 0.54342 -0.07364 -0.03486 -0.19074 16  GLU A CB  
6    C CG  . GLU A 9   ? 0.79596 0.86808 0.60945 -0.05511 -0.02942 -0.18472 16  GLU A CG  
7    C CD  . GLU A 9   ? 0.77412 0.84673 0.59229 -0.03235 -0.02960 -0.16378 16  GLU A CD  
8    O OE1 . GLU A 9   ? 0.76501 0.85214 0.60359 -0.03067 -0.03324 -0.15394 16  GLU A OE1 
9    O OE2 . GLU A 9   ? 0.82175 0.88093 0.62257 -0.01704 -0.02453 -0.15763 16  GLU A OE2 
10   N N   . VAL A 10  ? 0.45485 0.47669 0.31918 -0.07535 -0.01848 -0.16872 17  VAL A N   
11   C CA  . VAL A 10  ? 0.35420 0.37312 0.23483 -0.06620 -0.01910 -0.15375 17  VAL A CA  
12   C C   . VAL A 10  ? 0.40121 0.40003 0.27347 -0.04403 -0.01580 -0.14323 17  VAL A C   
13   O O   . VAL A 10  ? 0.44925 0.41037 0.30567 -0.03818 -0.00658 -0.14677 17  VAL A O   
14   C CB  . VAL A 10  ? 0.48148 0.46429 0.36759 -0.08015 -0.00960 -0.15478 17  VAL A CB  
15   C CG1 . VAL A 10  ? 0.39455 0.37470 0.29589 -0.06925 -0.01064 -0.13977 17  VAL A CG1 
16   C CG2 . VAL A 10  ? 0.50088 0.50752 0.39569 -0.10587 -0.00881 -0.16615 17  VAL A CG2 
17   N N   . GLU A 11  ? 0.30244 0.32790 0.18504 -0.03042 -0.02152 -0.13052 18  GLU A N   
18   C CA  . GLU A 11  ? 0.31977 0.33288 0.19897 -0.01225 -0.01606 -0.12082 18  GLU A CA  
19   C C   . GLU A 11  ? 0.26809 0.26740 0.16568 -0.00998 -0.01316 -0.11152 18  GLU A C   
20   O O   . GLU A 11  ? 0.24349 0.25950 0.15590 -0.01456 -0.01936 -0.10604 18  GLU A O   
21   C CB  . GLU A 11  ? 0.29794 0.34064 0.16968 0.00332  -0.02091 -0.11043 18  GLU A CB  
22   C CG  . GLU A 11  ? 0.32719 0.38093 0.17892 0.00557  -0.02215 -0.11587 18  GLU A CG  
23   C CD  . GLU A 11  ? 0.40583 0.48178 0.24428 0.02429  -0.02462 -0.10195 18  GLU A CD  
24   O OE1 . GLU A 11  ? 0.43376 0.53594 0.27806 0.03091  -0.03247 -0.09414 18  GLU A OE1 
25   O OE2 . GLU A 11  ? 0.48683 0.55197 0.30653 0.03368  -0.01701 -0.09805 18  GLU A OE2 
26   N N   . THR A 12  ? 0.26326 0.23584 0.16157 -0.00057 -0.00360 -0.10624 19  THR A N   
27   C CA  . THR A 12  ? 0.24303 0.20608 0.15892 0.00487  -0.00071 -0.09396 19  THR A CA  
28   C C   . THR A 12  ? 0.23735 0.21567 0.16123 0.01649  0.00222  -0.08151 19  THR A C   
29   O O   . THR A 12  ? 0.23490 0.21476 0.14982 0.02385  0.00874  -0.08333 19  THR A O   
30   C CB  . THR A 12  ? 0.26772 0.19482 0.17583 0.00923  0.00869  -0.09841 19  THR A CB  
31   O OG1 . THR A 12  ? 0.31611 0.21859 0.20949 -0.00745 0.01072  -0.11230 19  THR A OG1 
32   C CG2 . THR A 12  ? 0.28751 0.21156 0.21123 0.01792  0.01011  -0.08579 19  THR A CG2 
33   N N   . PHE A 13  ? 0.20145 0.18973 0.14031 0.01564  -0.00050 -0.07060 20  PHE A N   
34   C CA  . PHE A 13  ? 0.23366 0.23212 0.17798 0.01924  0.00487  -0.06108 20  PHE A CA  
35   C C   . PHE A 13  ? 0.26891 0.27097 0.23188 0.01945  0.00648  -0.05651 20  PHE A C   
36   O O   . PHE A 13  ? 0.22527 0.22085 0.19600 0.01806  0.00155  -0.05553 20  PHE A O   
37   C CB  . PHE A 13  ? 0.20930 0.21256 0.14589 0.01851  0.00233  -0.05294 20  PHE A CB  
38   C CG  . PHE A 13  ? 0.20425 0.21360 0.12006 0.02299  -0.00144 -0.05605 20  PHE A CG  
39   C CD1 . PHE A 13  ? 0.25570 0.27791 0.17133 0.01965  -0.01209 -0.06398 20  PHE A CD1 
40   C CD2 . PHE A 13  ? 0.26476 0.27121 0.15974 0.02940  0.00646  -0.05207 20  PHE A CD2 
41   C CE1 . PHE A 13  ? 0.26520 0.30534 0.16238 0.02419  -0.01754 -0.06929 20  PHE A CE1 
42   C CE2 . PHE A 13  ? 0.31213 0.32831 0.18426 0.03723  0.00196  -0.05432 20  PHE A CE2 
43   C CZ  . PHE A 13  ? 0.27416 0.31142 0.14840 0.03544  -0.01148 -0.06368 20  PHE A CZ  
44   N N   . ALA A 14  ? 0.20166 0.21788 0.17079 0.01932  0.01416  -0.05451 21  ALA A N   
45   C CA  . ALA A 14  ? 0.20792 0.23851 0.19439 0.01736  0.01462  -0.05212 21  ALA A CA  
46   C C   . ALA A 14  ? 0.20351 0.22938 0.18908 0.00658  0.01577  -0.04621 21  ALA A C   
47   O O   . ALA A 14  ? 0.24628 0.26264 0.21704 0.00164  0.02301  -0.04351 21  ALA A O   
48   C CB  . ALA A 14  ? 0.21912 0.27904 0.21502 0.01960  0.02289  -0.05708 21  ALA A CB  
49   N N   . PHE A 15  ? 0.20492 0.23179 0.20090 0.00501  0.01052  -0.04347 22  PHE A N   
50   C CA  . PHE A 15  ? 0.23814 0.25963 0.23162 -0.00477 0.01482  -0.03988 22  PHE A CA  
51   C C   . PHE A 15  ? 0.25131 0.28778 0.24660 -0.01733 0.02705  -0.04556 22  PHE A C   
52   O O   . PHE A 15  ? 0.23206 0.29894 0.24086 -0.01619 0.02821  -0.05246 22  PHE A O   
53   C CB  . PHE A 15  ? 0.21104 0.23611 0.21600 -0.00460 0.00811  -0.03795 22  PHE A CB  
54   C CG  . PHE A 15  ? 0.18674 0.19871 0.18958 0.00118  -0.00029 -0.03317 22  PHE A CG  
55   C CD1 . PHE A 15  ? 0.20219 0.20237 0.19375 0.00214  -0.00028 -0.02813 22  PHE A CD1 
56   C CD2 . PHE A 15  ? 0.18167 0.19411 0.19138 0.00618  -0.00618 -0.03400 22  PHE A CD2 
57   C CE1 . PHE A 15  ? 0.19650 0.19913 0.19045 0.00592  -0.00799 -0.02628 22  PHE A CE1 
58   C CE2 . PHE A 15  ? 0.19623 0.20045 0.20488 0.00510  -0.01113 -0.03237 22  PHE A CE2 
59   C CZ  . PHE A 15  ? 0.16671 0.17289 0.17100 0.00380  -0.01303 -0.02969 22  PHE A CZ  
60   N N   . GLN A 16  ? 0.26570 0.28101 0.24479 -0.02942 0.03821  -0.04352 23  GLN A N   
61   C CA  . GLN A 16  ? 0.30478 0.33373 0.28615 -0.05011 0.05199  -0.05244 23  GLN A CA  
62   C C   . GLN A 16  ? 0.29688 0.36141 0.30206 -0.05363 0.04416  -0.05978 23  GLN A C   
63   O O   . GLN A 16  ? 0.27351 0.33200 0.28334 -0.04349 0.03286  -0.05463 23  GLN A O   
64   C CB  . GLN A 16  ? 0.33351 0.31787 0.28509 -0.06334 0.06841  -0.04889 23  GLN A CB  
65   C CG  . GLN A 16  ? 0.43839 0.38552 0.35891 -0.05377 0.07669  -0.03872 23  GLN A CG  
66   C CD  . GLN A 16  ? 0.61348 0.50548 0.49517 -0.05999 0.09547  -0.03218 23  GLN A CD  
67   O OE1 . GLN A 16  ? 0.59331 0.46534 0.45667 -0.08275 0.11770  -0.03783 23  GLN A OE1 
68   N NE2 . GLN A 16  ? 0.62597 0.49202 0.49232 -0.03994 0.08883  -0.02094 23  GLN A NE2 
69   N N   . ALA A 17  ? 0.23569 0.34386 0.25575 -0.06728 0.05038  -0.07247 24  ALA A N   
70   C CA  . ALA A 17  ? 0.24374 0.39916 0.28590 -0.06599 0.04133  -0.08032 24  ALA A CA  
71   C C   . ALA A 17  ? 0.26767 0.40246 0.30284 -0.07559 0.04023  -0.08007 24  ALA A C   
72   O O   . ALA A 17  ? 0.24454 0.39539 0.28983 -0.06279 0.02753  -0.07783 24  ALA A O   
73   C CB  . ALA A 17  ? 0.27044 0.47807 0.32396 -0.08084 0.04771  -0.09557 24  ALA A CB  
74   N N   . GLU A 18  ? 0.25348 0.34634 0.26598 -0.09594 0.05550  -0.08135 25  GLU A N   
75   C CA  . GLU A 18  ? 0.31038 0.37793 0.31091 -0.10533 0.05805  -0.08271 25  GLU A CA  
76   C C   . GLU A 18  ? 0.25790 0.29816 0.25491 -0.08043 0.04454  -0.06739 25  GLU A C   
77   O O   . GLU A 18  ? 0.26632 0.31066 0.26640 -0.07934 0.03870  -0.06852 25  GLU A O   
78   C CB  . GLU A 18  ? 0.32920 0.34347 0.29509 -0.12573 0.08087  -0.08500 25  GLU A CB  
79   C CG  . GLU A 18  ? 0.33856 0.37423 0.29889 -0.14586 0.09275  -0.10058 25  GLU A CG  
80   C CD  . GLU A 18  ? 0.49152 0.53072 0.45234 -0.14787 0.09836  -0.09998 25  GLU A CD  
81   O OE1 . GLU A 18  ? 0.42189 0.45683 0.38986 -0.13137 0.09363  -0.08705 25  GLU A OE1 
82   O OE2 . GLU A 18  ? 0.53587 0.58457 0.48867 -0.16660 0.10910  -0.11318 25  GLU A OE2 
83   N N   . ILE A 19  ? 0.24308 0.25966 0.23310 -0.06236 0.04036  -0.05475 26  ILE A N   
84   C CA  . ILE A 19  ? 0.24214 0.24290 0.23142 -0.04277 0.02872  -0.04312 26  ILE A CA  
85   C C   . ILE A 19  ? 0.23556 0.26823 0.24736 -0.03109 0.01393  -0.04261 26  ILE A C   
86   O O   . ILE A 19  ? 0.21924 0.24974 0.23429 -0.02401 0.00683  -0.03810 26  ILE A O   
87   C CB  . ILE A 19  ? 0.25014 0.22653 0.22460 -0.02992 0.02906  -0.03354 26  ILE A CB  
88   C CG1 . ILE A 19  ? 0.34121 0.27563 0.28305 -0.03434 0.04598  -0.02995 26  ILE A CG1 
89   C CG2 . ILE A 19  ? 0.26069 0.23788 0.24074 -0.01369 0.01619  -0.02578 26  ILE A CG2 
90   C CD1 . ILE A 19  ? 0.44523 0.35195 0.37105 -0.03219 0.05102  -0.02671 26  ILE A CD1 
91   N N   . ALA A 20  ? 0.18946 0.24884 0.21297 -0.02727 0.01144  -0.04664 27  ALA A N   
92   C CA  . ALA A 20  ? 0.22438 0.30630 0.26043 -0.01229 0.00140  -0.04522 27  ALA A CA  
93   C C   . ALA A 20  ? 0.20207 0.30980 0.24500 -0.01490 -0.00160 -0.04953 27  ALA A C   
94   O O   . ALA A 20  ? 0.20389 0.31085 0.24726 -0.00206 -0.00875 -0.04339 27  ALA A O   
95   C CB  . ALA A 20  ? 0.19507 0.30160 0.23786 -0.00345 0.00193  -0.04929 27  ALA A CB  
96   N N   . GLN A 21  ? 0.20906 0.33824 0.25417 -0.03379 0.00545  -0.06117 28  GLN A N   
97   C CA  . GLN A 21  ? 0.16736 0.32681 0.21742 -0.04008 0.00265  -0.06914 28  GLN A CA  
98   C C   . GLN A 21  ? 0.21795 0.34221 0.25615 -0.04108 0.00188  -0.06297 28  GLN A C   
99   O O   . GLN A 21  ? 0.19773 0.33813 0.23803 -0.03302 -0.00535 -0.06186 28  GLN A O   
100  C CB  . GLN A 21  ? 0.20471 0.38637 0.25313 -0.06479 0.01428  -0.08481 28  GLN A CB  
101  C CG  . GLN A 21  ? 0.32901 0.54446 0.37665 -0.06659 0.01273  -0.09279 28  GLN A CG  
102  C CD  . GLN A 21  ? 0.43380 0.66965 0.47530 -0.08992 0.02624  -0.10886 28  GLN A CD  
103  O OE1 . GLN A 21  ? 0.46290 0.67380 0.49510 -0.10708 0.03899  -0.11257 28  GLN A OE1 
104  N NE2 . GLN A 21  ? 0.43164 0.71312 0.47528 -0.09113 0.02480  -0.11928 28  GLN A NE2 
105  N N   . LEU A 22  ? 0.19020 0.26827 0.21328 -0.04775 0.01000  -0.05830 29  LEU A N   
106  C CA  . LEU A 22  ? 0.21137 0.25897 0.22287 -0.04376 0.01005  -0.05160 29  LEU A CA  
107  C C   . LEU A 22  ? 0.20062 0.24951 0.21979 -0.02442 -0.00110 -0.03988 29  LEU A C   
108  O O   . LEU A 22  ? 0.22062 0.27021 0.23838 -0.02023 -0.00427 -0.03716 29  LEU A O   
109  C CB  . LEU A 22  ? 0.23459 0.23630 0.22516 -0.04595 0.02109  -0.04673 29  LEU A CB  
110  C CG  . LEU A 22  ? 0.27644 0.25263 0.25565 -0.03442 0.02081  -0.03816 29  LEU A CG  
111  C CD1 . LEU A 22  ? 0.25947 0.23045 0.22869 -0.04504 0.02670  -0.04662 29  LEU A CD1 
112  C CD2 . LEU A 22  ? 0.25527 0.19473 0.21300 -0.02522 0.02915  -0.03000 29  LEU A CD2 
113  N N   . MET A 23  ? 0.19924 0.24586 0.22363 -0.01484 -0.00500 -0.03409 30  MET A N   
114  C CA  . MET A 23  ? 0.17021 0.21046 0.19718 -0.00273 -0.01125 -0.02542 30  MET A CA  
115  C C   . MET A 23  ? 0.17911 0.23793 0.20858 0.00664  -0.01571 -0.02416 30  MET A C   
116  O O   . MET A 23  ? 0.18352 0.23365 0.20879 0.01187  -0.01702 -0.01771 30  MET A O   
117  C CB  . MET A 23  ? 0.17255 0.20317 0.19998 0.00149  -0.01214 -0.02333 30  MET A CB  
118  C CG  . MET A 23  ? 0.18116 0.19647 0.20269 -0.00130 -0.01022 -0.02134 30  MET A CG  
119  S SD  . MET A 23  ? 0.18223 0.19346 0.20122 0.00076  -0.01091 -0.02311 30  MET A SD  
120  C CE  . MET A 23  ? 0.23006 0.23731 0.25167 0.00092  -0.01535 -0.02158 30  MET A CE  
121  N N   . SER A 24  ? 0.16478 0.25282 0.19917 0.01070  -0.01716 -0.03001 31  SER A N   
122  C CA  . SER A 24  ? 0.14093 0.25381 0.17351 0.02643  -0.02190 -0.02797 31  SER A CA  
123  C C   . SER A 24  ? 0.19453 0.32043 0.22428 0.02092  -0.02358 -0.03073 31  SER A C   
124  O O   . SER A 24  ? 0.19681 0.32313 0.21764 0.03517  -0.02641 -0.02314 31  SER A O   
125  C CB  . SER A 24  ? 0.19384 0.35133 0.23423 0.03482  -0.02386 -0.03564 31  SER A CB  
126  O OG  . SER A 24  ? 0.29560 0.44046 0.33634 0.04160  -0.02118 -0.03375 31  SER A OG  
127  N N   . LEU A 25  ? 0.19139 0.32201 0.22341 0.00044  -0.01968 -0.04154 32  LEU A N   
128  C CA  . LEU A 25  ? 0.19380 0.33146 0.21928 -0.00645 -0.01964 -0.04641 32  LEU A CA  
129  C C   . LEU A 25  ? 0.22899 0.33159 0.24568 0.00006  -0.01861 -0.03431 32  LEU A C   
130  O O   . LEU A 25  ? 0.24065 0.35085 0.25026 0.00669  -0.02097 -0.03162 32  LEU A O   
131  C CB  . LEU A 25  ? 0.18566 0.32111 0.20789 -0.03218 -0.01092 -0.06176 32  LEU A CB  
132  C CG  . LEU A 25  ? 0.24628 0.38252 0.25695 -0.04384 -0.00779 -0.07113 32  LEU A CG  
133  C CD1 . LEU A 25  ? 0.30963 0.45599 0.31760 -0.06815 0.00335  -0.08744 32  LEU A CD1 
134  C CD2 . LEU A 25  ? 0.27277 0.35871 0.26895 -0.04142 -0.00144 -0.06229 32  LEU A CD2 
135  N N   . ILE A 26  ? 0.18442 0.25474 0.20124 -0.00161 -0.01483 -0.02783 33  ILE A N   
136  C CA  . ILE A 26  ? 0.15705 0.20638 0.16958 0.00281  -0.01324 -0.01863 33  ILE A CA  
137  C C   . ILE A 26  ? 0.21256 0.26030 0.22277 0.01465  -0.01561 -0.00875 33  ILE A C   
138  O O   . ILE A 26  ? 0.22061 0.26280 0.22414 0.01762  -0.01353 -0.00299 33  ILE A O   
139  C CB  . ILE A 26  ? 0.17786 0.20723 0.19224 0.00012  -0.00993 -0.01604 33  ILE A CB  
140  C CG1 . ILE A 26  ? 0.20958 0.22596 0.21415 -0.00700 -0.00302 -0.02231 33  ILE A CG1 
141  C CG2 . ILE A 26  ? 0.21899 0.24205 0.23521 0.00423  -0.00935 -0.00805 33  ILE A CG2 
142  C CD1 . ILE A 26  ? 0.23975 0.23903 0.24030 -0.00402 0.00036  -0.01897 33  ILE A CD1 
143  N N   . ILE A 27  ? 0.19861 0.24594 0.20967 0.02212  -0.01734 -0.00642 34  ILE A N   
144  C CA  . ILE A 27  ? 0.23677 0.26651 0.23595 0.03411  -0.01480 0.00374  34  ILE A CA  
145  C C   . ILE A 27  ? 0.21596 0.26165 0.20209 0.05049  -0.01692 0.00800  34  ILE A C   
146  O O   . ILE A 27  ? 0.29002 0.31557 0.25928 0.05857  -0.01180 0.01828  34  ILE A O   
147  C CB  . ILE A 27  ? 0.24052 0.25589 0.23818 0.03915  -0.01336 0.00431  34  ILE A CB  
148  C CG1 . ILE A 27  ? 0.25152 0.25216 0.25788 0.02347  -0.01132 0.00076  34  ILE A CG1 
149  C CG2 . ILE A 27  ? 0.24951 0.23628 0.22425 0.05539  -0.00691 0.01478  34  ILE A CG2 
150  C CD1 . ILE A 27  ? 0.30154 0.29400 0.30795 0.02521  -0.01093 -0.00288 34  ILE A CD1 
151  N N   . ASN A 28  ? 0.20095 0.28621 0.19279 0.05492  -0.02350 -0.00054 35  ASN A N   
152  C CA  . ASN A 28  ? 0.22378 0.33806 0.20299 0.07587  -0.02785 0.00231  35  ASN A CA  
153  C C   . ASN A 28  ? 0.22819 0.36584 0.20389 0.07035  -0.03082 -0.00296 35  ASN A C   
154  O O   . ASN A 28  ? 0.31304 0.46634 0.27162 0.09017  -0.03331 0.00338  35  ASN A O   
155  C CB  . ASN A 28  ? 0.22713 0.38854 0.21579 0.08553  -0.03413 -0.00673 35  ASN A CB  
156  C CG  . ASN A 28  ? 0.27168 0.41199 0.25800 0.09839  -0.03067 -0.00084 35  ASN A CG  
157  O OD1 . ASN A 28  ? 0.37367 0.46632 0.34074 0.11044  -0.02369 0.01239  35  ASN A OD1 
158  N ND2 . ASN A 28  ? 0.38008 0.54928 0.38175 0.09176  -0.03179 -0.01209 35  ASN A ND2 
159  N N   . THR A 29  ? 0.22099 0.35925 0.20739 0.04668  -0.02950 -0.01431 36  THR A N   
160  C CA  . THR A 29  ? 0.19773 0.35590 0.17724 0.04020  -0.03086 -0.02249 36  THR A CA  
161  C C   . THR A 29  ? 0.21796 0.34913 0.18134 0.04893  -0.02635 -0.00903 36  THR A C   
162  O O   . THR A 29  ? 0.25273 0.34692 0.21736 0.04475  -0.01948 -0.00001 36  THR A O   
163  C CB  . THR A 29  ? 0.24660 0.39733 0.23318 0.01392  -0.02599 -0.03763 36  THR A CB  
164  O OG1 . THR A 29  ? 0.22538 0.39772 0.22414 0.00181  -0.02665 -0.05038 36  THR A OG1 
165  C CG2 . THR A 29  ? 0.26268 0.42916 0.23752 0.00522  -0.02535 -0.04926 36  THR A CG2 
166  N N   . PHE A 30  ? 0.22837 0.38368 0.17621 0.06008  -0.02971 -0.00891 37  PHE A N   
167  C CA  . PHE A 30  ? 0.28159 0.41225 0.21241 0.06525  -0.02320 0.00242  37  PHE A CA  
168  C C   . PHE A 30  ? 0.28199 0.40105 0.21827 0.04516  -0.01801 -0.00729 37  PHE A C   
169  O O   . PHE A 30  ? 0.26274 0.40378 0.19801 0.03416  -0.02050 -0.02384 37  PHE A O   
170  C CB  . PHE A 30  ? 0.23330 0.39244 0.14090 0.08584  -0.02772 0.00626  37  PHE A CB  
171  C CG  . PHE A 30  ? 0.30067 0.43282 0.18745 0.09090  -0.01879 0.01875  37  PHE A CG  
172  C CD1 . PHE A 30  ? 0.34186 0.42959 0.21518 0.09928  -0.00765 0.03821  37  PHE A CD1 
173  C CD2 . PHE A 30  ? 0.31040 0.45853 0.18952 0.08373  -0.01889 0.00933  37  PHE A CD2 
174  C CE1 . PHE A 30  ? 0.33901 0.40330 0.19326 0.10003  0.00353  0.04893  37  PHE A CE1 
175  C CE2 . PHE A 30  ? 0.30849 0.43380 0.16872 0.08823  -0.00913 0.02082  37  PHE A CE2 
176  C CZ  . PHE A 30  ? 0.30339 0.38862 0.15257 0.09567  0.00235  0.04095  37  PHE A CZ  
177  N N   . TYR A 31  ? 0.21204 0.29812 0.15105 0.04100  -0.00935 0.00191  38  TYR A N   
178  C CA  . TYR A 31  ? 0.21513 0.28944 0.15823 0.02888  -0.00326 -0.00514 38  TYR A CA  
179  C C   . TYR A 31  ? 0.21564 0.27141 0.15969 0.03058  0.00567  0.00731  38  TYR A C   
180  O O   . TYR A 31  ? 0.20700 0.25143 0.16344 0.02708  0.00784  0.01301  38  TYR A O   
181  C CB  . TYR A 31  ? 0.21142 0.27845 0.16817 0.01729  -0.00369 -0.01481 38  TYR A CB  
182  C CG  . TYR A 31  ? 0.27715 0.32341 0.23305 0.01300  0.00472  -0.01729 38  TYR A CG  
183  C CD1 . TYR A 31  ? 0.30742 0.34622 0.24737 0.00877  0.01063  -0.02831 38  TYR A CD1 
184  C CD2 . TYR A 31  ? 0.26686 0.30241 0.23458 0.01531  0.00748  -0.00943 38  TYR A CD2 
185  C CE1 . TYR A 31  ? 0.33874 0.35355 0.27165 0.01219  0.02047  -0.02856 38  TYR A CE1 
186  C CE2 . TYR A 31  ? 0.28999 0.31415 0.25491 0.01885  0.01462  -0.01023 38  TYR A CE2 
187  C CZ  . TYR A 31  ? 0.29906 0.30999 0.24525 0.01982  0.02162  -0.01843 38  TYR A CZ  
188  O OH  . TYR A 31  ? 0.38497 0.38076 0.32327 0.03033  0.03043  -0.01714 38  TYR A OH  
189  N N   . SER A 32  ? 0.22802 0.28547 0.15892 0.03395  0.01154  0.00958  39  SER A N   
190  C CA  . SER A 32  ? 0.22613 0.27457 0.15689 0.03359  0.02195  0.02074  39  SER A CA  
191  C C   . SER A 32  ? 0.21103 0.26163 0.15871 0.02765  0.02743  0.01745  39  SER A C   
192  O O   . SER A 32  ? 0.25819 0.31158 0.21452 0.02241  0.03495  0.02387  39  SER A O   
193  C CB  . SER A 32  ? 0.24773 0.30037 0.15647 0.04068  0.02768  0.02491  39  SER A CB  
194  O OG  . SER A 32  ? 0.26255 0.31678 0.15149 0.05210  0.02303  0.03110  39  SER A OG  
195  N N   . ASN A 33  ? 0.21225 0.26224 0.16202 0.02869  0.02538  0.00720  40  ASN A N   
196  C CA  . ASN A 33  ? 0.20753 0.26076 0.16527 0.03261  0.03150  0.00552  40  ASN A CA  
197  C C   . ASN A 33  ? 0.15835 0.21445 0.13469 0.02985  0.02761  0.00672  40  ASN A C   
198  O O   . ASN A 33  ? 0.19607 0.24432 0.17170 0.03528  0.02711  0.00236  40  ASN A O   
199  C CB  . ASN A 33  ? 0.25602 0.29410 0.19600 0.03856  0.03520  -0.00467 40  ASN A CB  
200  C CG  . ASN A 33  ? 0.26443 0.30188 0.20401 0.05197  0.04356  -0.00431 40  ASN A CG  
201  O OD1 . ASN A 33  ? 0.27025 0.33331 0.22247 0.05781  0.04765  0.00193  40  ASN A OD1 
202  N ND2 . ASN A 33  ? 0.31588 0.32426 0.23728 0.05769  0.04814  -0.01162 40  ASN A ND2 
203  N N   . LYS A 34  ? 0.21833 0.17731 0.15656 0.01694  -0.01590 -0.00596 41  LYS A N   
204  C CA  . LYS A 34  ? 0.19620 0.16780 0.15917 0.01431  -0.00725 -0.00453 41  LYS A CA  
205  C C   . LYS A 34  ? 0.27786 0.24249 0.24165 0.01383  -0.00000 -0.01179 41  LYS A C   
206  O O   . LYS A 34  ? 0.19250 0.16389 0.17175 0.00976  0.00212  -0.01235 41  LYS A O   
207  C CB  . LYS A 34  ? 0.19363 0.17059 0.16411 0.02078  0.00347  0.00159  41  LYS A CB  
208  C CG  . LYS A 34  ? 0.20145 0.19192 0.17778 0.02458  -0.00176 0.01124  41  LYS A CG  
209  C CD  . LYS A 34  ? 0.23086 0.21563 0.20646 0.03430  0.00883  0.01615  41  LYS A CD  
210  C CE  . LYS A 34  ? 0.24486 0.24443 0.22561 0.04338  0.00562  0.02727  41  LYS A CE  
211  N NZ  . LYS A 34  ? 0.22880 0.25054 0.22804 0.04671  0.00567  0.03241  41  LYS A NZ  
212  N N   . GLU A 35  ? 0.24487 0.19914 0.19186 0.01994  0.00432  -0.01576 42  GLU A N   
213  C CA  . GLU A 35  ? 0.22213 0.17832 0.17464 0.02182  0.01327  -0.01852 42  GLU A CA  
214  C C   . GLU A 35  ? 0.22084 0.17205 0.17639 0.01755  0.00634  -0.02429 42  GLU A C   
215  O O   . GLU A 35  ? 0.23175 0.18860 0.19740 0.01763  0.01221  -0.02531 42  GLU A O   
216  C CB  . GLU A 35  ? 0.23608 0.18907 0.16957 0.03379  0.02088  -0.01803 42  GLU A CB  
217  C CG  . GLU A 35  ? 0.25516 0.18592 0.15593 0.04298  0.01185  -0.02589 42  GLU A CG  
218  C CD  . GLU A 35  ? 0.29904 0.22715 0.17404 0.06149  0.02237  -0.02440 42  GLU A CD  
219  O OE1 . GLU A 35  ? 0.38301 0.32364 0.25867 0.06494  0.03160  -0.01565 42  GLU A OE1 
220  O OE2 . GLU A 35  ? 0.42957 0.34117 0.28004 0.07468  0.02142  -0.03114 42  GLU A OE2 
221  N N   . ILE A 36  ? 0.22038 0.16134 0.16778 0.01223  -0.00780 -0.02607 43  ILE A N   
222  C CA  . ILE A 36  ? 0.20906 0.14183 0.15783 0.00629  -0.01602 -0.02908 43  ILE A CA  
223  C C   . ILE A 36  ? 0.22186 0.17344 0.19693 -0.00036 -0.01101 -0.02508 43  ILE A C   
224  O O   . ILE A 36  ? 0.19140 0.13899 0.16922 -0.00392 -0.01444 -0.02640 43  ILE A O   
225  C CB  . ILE A 36  ? 0.27143 0.18780 0.20673 -0.00307 -0.03614 -0.02821 43  ILE A CB  
226  C CG1 . ILE A 36  ? 0.26593 0.20599 0.22195 -0.01289 -0.04136 -0.01728 43  ILE A CG1 
227  C CG2 . ILE A 36  ? 0.34512 0.23167 0.24241 0.00568  -0.04401 -0.03524 43  ILE A CG2 
228  C CD1 . ILE A 36  ? 0.26809 0.22750 0.24940 -0.02449 -0.04512 -0.00816 43  ILE A CD1 
229  N N   . PHE A 37  ? 0.18248 0.15019 0.17199 -0.00002 -0.00322 -0.02043 44  PHE A N   
230  C CA  . PHE A 37  ? 0.15883 0.13795 0.16362 -0.00224 0.00153  -0.01835 44  PHE A CA  
231  C C   . PHE A 37  ? 0.17606 0.15071 0.18130 -0.00169 0.00554  -0.02348 44  PHE A C   
232  O O   . PHE A 37  ? 0.15367 0.13213 0.16513 -0.00470 0.00453  -0.02313 44  PHE A O   
233  C CB  . PHE A 37  ? 0.17008 0.15519 0.17933 0.00287  0.00945  -0.01519 44  PHE A CB  
234  C CG  . PHE A 37  ? 0.20804 0.18365 0.21329 0.00463  0.01627  -0.01835 44  PHE A CG  
235  C CD1 . PHE A 37  ? 0.22542 0.19699 0.22396 0.00695  0.01865  -0.01653 44  PHE A CD1 
236  C CD2 . PHE A 37  ? 0.17323 0.14515 0.18128 0.00218  0.01863  -0.02104 44  PHE A CD2 
237  C CE1 . PHE A 37  ? 0.22460 0.19299 0.22398 0.00534  0.02415  -0.01451 44  PHE A CE1 
238  C CE2 . PHE A 37  ? 0.20085 0.16679 0.20889 -0.00123 0.02108  -0.02027 44  PHE A CE2 
239  C CZ  . PHE A 37  ? 0.22708 0.19333 0.23313 -0.00042 0.02431  -0.01557 44  PHE A CZ  
240  N N   . LEU A 38  ? 0.17826 0.14913 0.17811 0.00285  0.01044  -0.02581 45  LEU A N   
241  C CA  . LEU A 38  ? 0.19057 0.16606 0.19677 0.00323  0.01424  -0.02678 45  LEU A CA  
242  C C   . LEU A 38  ? 0.16555 0.13488 0.16659 0.00556  0.00922  -0.02972 45  LEU A C   
243  O O   . LEU A 38  ? 0.18957 0.16360 0.19834 0.00314  0.00853  -0.02964 45  LEU A O   
244  C CB  . LEU A 38  ? 0.19138 0.17422 0.19867 0.00749  0.02166  -0.02301 45  LEU A CB  
245  C CG  . LEU A 38  ? 0.17645 0.17318 0.19758 0.00499  0.02403  -0.01932 45  LEU A CG  
246  C CD1 . LEU A 38  ? 0.18906 0.18329 0.21819 -0.00603 0.01980  -0.01964 45  LEU A CD1 
247  C CD2 . LEU A 38  ? 0.26082 0.27405 0.28804 0.00837  0.03194  -0.00992 45  LEU A CD2 
248  N N   . ARG A 39  ? 0.19809 0.15194 0.18158 0.01083  0.00406  -0.03246 46  ARG A N   
249  C CA  . ARG A 39  ? 0.20497 0.14117 0.17618 0.01300  -0.00410 -0.03554 46  ARG A CA  
250  C C   . ARG A 39  ? 0.24667 0.18481 0.22883 0.00071  -0.01149 -0.03207 46  ARG A C   
251  O O   . ARG A 39  ? 0.22538 0.15760 0.20686 0.00077  -0.01466 -0.03186 46  ARG A O   
252  C CB  . ARG A 39  ? 0.26924 0.17754 0.21160 0.01823  -0.01327 -0.03995 46  ARG A CB  
253  C CG  . ARG A 39  ? 0.41272 0.28971 0.33432 0.01959  -0.02579 -0.04359 46  ARG A CG  
254  C CD  . ARG A 39  ? 0.47704 0.32337 0.37069 0.01644  -0.04154 -0.04554 46  ARG A CD  
255  N NE  . ARG A 39  ? 0.44759 0.29890 0.35070 -0.00144 -0.05287 -0.04081 46  ARG A NE  
256  C CZ  . ARG A 39  ? 0.45986 0.29713 0.34476 -0.00393 -0.06383 -0.04054 46  ARG A CZ  
257  N NH1 . ARG A 39  ? 0.43046 0.24425 0.28360 0.01107  -0.06427 -0.04587 46  ARG A NH1 
258  N NH2 . ARG A 39  ? 0.50773 0.35677 0.40682 -0.02138 -0.07551 -0.03280 46  ARG A NH2 
259  N N   . GLU A 40  ? 0.20451 0.15379 0.19689 -0.00805 -0.01338 -0.02708 47  GLU A N   
260  C CA  . GLU A 40  ? 0.20087 0.15887 0.20436 -0.01781 -0.01859 -0.01955 47  GLU A CA  
261  C C   . GLU A 40  ? 0.18443 0.15626 0.19831 -0.01567 -0.01012 -0.01897 47  GLU A C   
262  O O   . GLU A 40  ? 0.18555 0.15806 0.20176 -0.01952 -0.01345 -0.01482 47  GLU A O   
263  C CB  . GLU A 40  ? 0.16966 0.14407 0.18335 -0.02383 -0.02099 -0.01088 47  GLU A CB  
264  C CG  . GLU A 40  ? 0.20244 0.16291 0.20503 -0.02980 -0.03457 -0.00965 47  GLU A CG  
265  C CD  . GLU A 40  ? 0.22763 0.16002 0.21495 -0.03882 -0.05145 -0.00961 47  GLU A CD  
266  O OE1 . GLU A 40  ? 0.27093 0.20607 0.26646 -0.04594 -0.05442 -0.00319 47  GLU A OE1 
267  O OE2 . GLU A 40  ? 0.31817 0.22105 0.28082 -0.03865 -0.06341 -0.01555 47  GLU A OE2 
268  N N   . LEU A 41  ? 0.19279 0.17180 0.20968 -0.01046 -0.00117 -0.02258 48  LEU A N   
269  C CA  . LEU A 41  ? 0.18642 0.17107 0.20623 -0.00932 0.00298  -0.02364 48  LEU A CA  
270  C C   . LEU A 41  ? 0.18382 0.16502 0.20316 -0.00817 0.00077  -0.02613 48  LEU A C   
271  O O   . LEU A 41  ? 0.18650 0.17051 0.20628 -0.00924 -0.00082 -0.02473 48  LEU A O   
272  C CB  . LEU A 41  ? 0.17349 0.15757 0.19182 -0.00686 0.00839  -0.02643 48  LEU A CB  
273  C CG  . LEU A 41  ? 0.13549 0.12274 0.15209 -0.00310 0.01182  -0.02308 48  LEU A CG  
274  C CD1 . LEU A 41  ? 0.16133 0.13711 0.17025 0.00003  0.01519  -0.02646 48  LEU A CD1 
275  C CD2 . LEU A 41  ? 0.17402 0.17285 0.19137 0.00000  0.01358  -0.01690 48  LEU A CD2 
276  N N   . ILE A 42  ? 0.18737 0.16490 0.20466 -0.00340 0.00153  -0.02839 49  ILE A N   
277  C CA  . ILE A 42  ? 0.14911 0.12835 0.16712 0.00223  0.00080  -0.02818 49  ILE A CA  
278  C C   . ILE A 42  ? 0.20703 0.17162 0.21614 0.00306  -0.00625 -0.02734 49  ILE A C   
279  O O   . ILE A 42  ? 0.20321 0.17042 0.21436 0.00496  -0.00825 -0.02530 49  ILE A O   
280  C CB  . ILE A 42  ? 0.13405 0.11678 0.14990 0.01234  0.00614  -0.02803 49  ILE A CB  
281  C CG1 . ILE A 42  ? 0.12491 0.12566 0.15420 0.00768  0.01170  -0.02423 49  ILE A CG1 
282  C CG2 . ILE A 42  ? 0.20859 0.19293 0.22166 0.02482  0.00635  -0.02615 49  ILE A CG2 
283  C CD1 . ILE A 42  ? 0.17190 0.18403 0.20184 0.01758  0.01951  -0.01952 49  ILE A CD1 
284  N N   . SER A 43  ? 0.18536 0.13311 0.18413 -0.00031 -0.01234 -0.02730 50  SER A N   
285  C CA  . SER A 43  ? 0.20958 0.13812 0.19890 -0.00436 -0.02262 -0.02394 50  SER A CA  
286  C C   . SER A 43  ? 0.19629 0.13974 0.19749 -0.01296 -0.02267 -0.01633 50  SER A C   
287  O O   . SER A 43  ? 0.20897 0.14469 0.20644 -0.01280 -0.02710 -0.01264 50  SER A O   
288  C CB  . SER A 43  ? 0.24207 0.15017 0.21931 -0.01183 -0.03334 -0.02294 50  SER A CB  
289  O OG  . SER A 43  ? 0.35472 0.24304 0.32484 -0.02186 -0.04674 -0.01617 50  SER A OG  
290  N N   . ASN A 44  ? 0.19403 0.15780 0.20617 -0.01750 -0.01689 -0.01335 51  ASN A N   
291  C CA  . ASN A 44  ? 0.19709 0.17618 0.21471 -0.02007 -0.01391 -0.00637 51  ASN A CA  
292  C C   . ASN A 44  ? 0.17724 0.15792 0.19206 -0.01431 -0.01192 -0.01050 51  ASN A C   
293  O O   . ASN A 44  ? 0.16866 0.15096 0.18103 -0.01525 -0.01413 -0.00468 51  ASN A O   
294  C CB  . ASN A 44  ? 0.16009 0.15704 0.18289 -0.01868 -0.00605 -0.00407 51  ASN A CB  
295  C CG  . ASN A 44  ? 0.18231 0.18986 0.21375 -0.02563 -0.00892 0.00702  51  ASN A CG  
296  O OD1 . ASN A 44  ? 0.18715 0.18509 0.21960 -0.03562 -0.01974 0.01317  51  ASN A OD1 
297  N ND2 . ASN A 44  ? 0.20615 0.23244 0.24253 -0.02032 -0.00088 0.01111  51  ASN A ND2 
298  N N   . SER A 45  ? 0.17303 0.15562 0.18928 -0.00981 -0.00897 -0.01810 52  SER A N   
299  C CA  . SER A 45  ? 0.15521 0.14337 0.17229 -0.00731 -0.01052 -0.01958 52  SER A CA  
300  C C   . SER A 45  ? 0.16590 0.14844 0.18158 -0.00260 -0.01530 -0.01629 52  SER A C   
301  O O   . SER A 45  ? 0.19056 0.17675 0.20436 -0.00197 -0.01873 -0.01288 52  SER A O   
302  C CB  . SER A 45  ? 0.14841 0.14351 0.17243 -0.00705 -0.00863 -0.02347 52  SER A CB  
303  O OG  . SER A 45  ? 0.18093 0.17373 0.20089 -0.01102 -0.00649 -0.02657 52  SER A OG  
304  N N   . SER A 46  ? 0.16868 0.13812 0.18030 0.00291  -0.01624 -0.01749 53  SER A N   
305  C CA  . SER A 46  ? 0.20956 0.16547 0.21300 0.01214  -0.02084 -0.01522 53  SER A CA  
306  C C   . SER A 46  ? 0.22584 0.16832 0.22204 0.00544  -0.02781 -0.00850 53  SER A C   
307  O O   . SER A 46  ? 0.24466 0.18366 0.23721 0.01084  -0.03145 -0.00427 53  SER A O   
308  C CB  . SER A 46  ? 0.26506 0.19957 0.25464 0.02247  -0.02119 -0.01953 53  SER A CB  
309  O OG  . SER A 46  ? 0.28711 0.19870 0.26046 0.03547  -0.02624 -0.01830 53  SER A OG  
310  N N   . ASP A 47  ? 0.23935 0.17831 0.23554 -0.00650 -0.02973 -0.00456 54  ASP A N   
311  C CA  . ASP A 47  ? 0.22041 0.15384 0.21406 -0.01552 -0.03568 0.00701  54  ASP A CA  
312  C C   . ASP A 47  ? 0.22202 0.17656 0.21952 -0.01424 -0.03102 0.01153  54  ASP A C   
313  O O   . ASP A 47  ? 0.22421 0.17290 0.21622 -0.01459 -0.03554 0.01992  54  ASP A O   
314  C CB  . ASP A 47  ? 0.25882 0.19731 0.25869 -0.02916 -0.03759 0.01485  54  ASP A CB  
315  C CG  . ASP A 47  ? 0.30987 0.22022 0.30016 -0.03434 -0.04828 0.01259  54  ASP A CG  
316  O OD1 . ASP A 47  ? 0.30706 0.18531 0.27892 -0.02571 -0.05479 0.00527  54  ASP A OD1 
317  O OD2 . ASP A 47  ? 0.30340 0.22270 0.30193 -0.04616 -0.05132 0.01934  54  ASP A OD2 
318  N N   . ALA A 48  ? 0.17866 0.15295 0.18083 -0.01232 -0.02340 0.00606  55  ALA A N   
319  C CA  . ALA A 48  ? 0.17436 0.16135 0.17104 -0.00974 -0.02115 0.00803  55  ALA A CA  
320  C C   . ALA A 48  ? 0.19232 0.17786 0.18688 -0.00394 -0.02685 0.00575  55  ALA A C   
321  O O   . ALA A 48  ? 0.22039 0.20960 0.20682 -0.00239 -0.02948 0.01111  55  ALA A O   
322  C CB  . ALA A 48  ? 0.18636 0.18262 0.18028 -0.00790 -0.01485 0.00061  55  ALA A CB  
323  N N   . LEU A 49  ? 0.18754 0.17136 0.18958 0.00079  -0.02832 0.00002  56  LEU A N   
324  C CA  . LEU A 49  ? 0.17965 0.17022 0.18506 0.00843  -0.03319 0.00165  56  LEU A CA  
325  C C   . LEU A 49  ? 0.20003 0.17401 0.19715 0.01477  -0.03786 0.00917  56  LEU A C   
326  O O   . LEU A 49  ? 0.20822 0.18774 0.20278 0.01904  -0.04273 0.01489  56  LEU A O   
327  C CB  . LEU A 49  ? 0.16693 0.16800 0.18501 0.01426  -0.03060 -0.00231 56  LEU A CB  
328  C CG  . LEU A 49  ? 0.16290 0.18021 0.18986 0.00572  -0.02985 -0.00654 56  LEU A CG  
329  C CD1 . LEU A 49  ? 0.15759 0.18354 0.19668 0.00937  -0.02422 -0.00771 56  LEU A CD1 
330  C CD2 . LEU A 49  ? 0.17440 0.20866 0.20574 0.00201  -0.03907 -0.00283 56  LEU A CD2 
331  N N   . ASP A 50  ? 0.22070 0.17020 0.21047 0.01449  -0.03871 0.00971  57  ASP A N   
332  C CA  . ASP A 50  ? 0.22486 0.14698 0.20081 0.01759  -0.04624 0.01748  57  ASP A CA  
333  C C   . ASP A 50  ? 0.23597 0.16393 0.20917 0.00906  -0.04872 0.02881  57  ASP A C   
334  O O   . ASP A 50  ? 0.28131 0.19928 0.24630 0.01503  -0.05433 0.03636  57  ASP A O   
335  C CB  . ASP A 50  ? 0.25382 0.14223 0.21784 0.01173  -0.05160 0.01717  57  ASP A CB  
336  C CG  . ASP A 50  ? 0.30913 0.17986 0.26365 0.02585  -0.05070 0.00674  57  ASP A CG  
337  O OD1 . ASP A 50  ? 0.29442 0.17999 0.25314 0.04299  -0.04496 0.00317  57  ASP A OD1 
338  O OD2 . ASP A 50  ? 0.33508 0.17679 0.27604 0.02051  -0.05670 0.00393  57  ASP A OD2 
339  N N   . LYS A 51  ? 0.23869 0.18349 0.21668 -0.00215 -0.04353 0.03147  58  LYS A N   
340  C CA  . LYS A 51  ? 0.25173 0.20533 0.22458 -0.00778 -0.04306 0.04487  58  LYS A CA  
341  C C   . LYS A 51  ? 0.27334 0.23984 0.23940 0.00074  -0.04399 0.04444  58  LYS A C   
342  O O   . LYS A 51  ? 0.24922 0.21080 0.20635 0.00220  -0.04830 0.05595  58  LYS A O   
343  C CB  . LYS A 51  ? 0.23515 0.20903 0.21309 -0.01528 -0.03427 0.04836  58  LYS A CB  
344  C CG  . LYS A 51  ? 0.36074 0.32764 0.34759 -0.02774 -0.03648 0.05627  58  LYS A CG  
345  C CD  . LYS A 51  ? 0.40307 0.39961 0.39816 -0.03246 -0.02664 0.06642  58  LYS A CD  
346  C CE  . LYS A 51  ? 0.43415 0.43065 0.44290 -0.04447 -0.02993 0.07104  58  LYS A CE  
347  N NZ  . LYS A 51  ? 0.45205 0.47733 0.46907 -0.03992 -0.01790 0.06975  58  LYS A NZ  
348  N N   . ILE A 52  ? 0.24167 0.22325 0.21040 0.00465  -0.04208 0.03269  59  ILE A N   
349  C CA  . ILE A 52  ? 0.26612 0.25831 0.22650 0.00966  -0.04746 0.03263  59  ILE A CA  
350  C C   . ILE A 52  ? 0.29287 0.28191 0.25825 0.01810  -0.05546 0.03683  59  ILE A C   
351  O O   . ILE A 52  ? 0.24078 0.23302 0.19716 0.02229  -0.06159 0.04442  59  ILE A O   
352  C CB  . ILE A 52  ? 0.26607 0.26911 0.22595 0.00779  -0.04813 0.02033  59  ILE A CB  
353  C CG1 . ILE A 52  ? 0.28739 0.29649 0.23199 0.00964  -0.05788 0.02072  59  ILE A CG1 
354  C CG2 . ILE A 52  ? 0.21642 0.22490 0.19627 0.00773  -0.04942 0.01338  59  ILE A CG2 
355  C CD1 . ILE A 52  ? 0.30251 0.30764 0.22017 0.01287  -0.05450 0.02708  59  ILE A CD1 
356  N N   . ARG A 53  ? 0.24700 0.22934 0.22374 0.02375  -0.05487 0.03312  60  ARG A N   
357  C CA  . ARG A 53  ? 0.24344 0.22181 0.22169 0.03792  -0.06016 0.03858  60  ARG A CA  
358  C C   . ARG A 53  ? 0.25677 0.20901 0.21865 0.04011  -0.06471 0.05003  60  ARG A C   
359  O O   . ARG A 53  ? 0.30278 0.25779 0.25987 0.04901  -0.07076 0.05829  60  ARG A O   
360  C CB  . ARG A 53  ? 0.26543 0.23696 0.25105 0.04843  -0.05607 0.03280  60  ARG A CB  
361  C CG  . ARG A 53  ? 0.35105 0.31909 0.33486 0.06989  -0.05906 0.03909  60  ARG A CG  
362  C CD  . ARG A 53  ? 0.37455 0.34362 0.36329 0.08574  -0.05227 0.03408  60  ARG A CD  
363  N NE  . ARG A 53  ? 0.47132 0.39535 0.43821 0.08693  -0.05149 0.02779  60  ARG A NE  
364  C CZ  . ARG A 53  ? 0.47984 0.39391 0.44104 0.09894  -0.04552 0.02069  60  ARG A CZ  
365  N NH1 . ARG A 53  ? 0.47066 0.42168 0.45009 0.11176  -0.03696 0.02125  60  ARG A NH1 
366  N NH2 . ARG A 53  ? 0.48312 0.35013 0.41916 0.09690  -0.04931 0.01463  60  ARG A NH2 
367  N N   . TYR A 54  ? 0.26562 0.19315 0.21954 0.03023  -0.06353 0.05299  61  TYR A N   
368  C CA  . TYR A 54  ? 0.32931 0.22876 0.26823 0.02797  -0.07028 0.06714  61  TYR A CA  
369  C C   . TYR A 54  ? 0.36313 0.28087 0.29676 0.02393  -0.07054 0.07891  61  TYR A C   
370  O O   . TYR A 54  ? 0.36504 0.27134 0.28795 0.03074  -0.07710 0.08995  61  TYR A O   
371  C CB  . TYR A 54  ? 0.30965 0.18366 0.24486 0.01243  -0.07214 0.07131  61  TYR A CB  
372  C CG  . TYR A 54  ? 0.39247 0.24108 0.31526 0.00234  -0.08075 0.09070  61  TYR A CG  
373  C CD1 . TYR A 54  ? 0.39899 0.19997 0.30268 0.00901  -0.09274 0.09491  61  TYR A CD1 
374  C CD2 . TYR A 54  ? 0.38248 0.25362 0.31038 -0.01249 -0.07668 0.10646  61  TYR A CD2 
375  C CE1 . TYR A 54  ? 0.42020 0.20049 0.31504 -0.00297 -0.09961 0.11123  61  TYR A CE1 
376  C CE2 . TYR A 54  ? 0.47693 0.32949 0.39663 -0.02411 -0.08444 0.12876  61  TYR A CE2 
377  C CZ  . TYR A 54  ? 0.46296 0.27139 0.36836 -0.02077 -0.09544 0.12870  61  TYR A CZ  
378  O OH  . TYR A 54  ? 0.50582 0.30268 0.40764 -0.03286 -0.09968 0.14422  61  TYR A OH  
379  N N   . GLU A 55  ? 0.30728 0.25112 0.24394 0.01573  -0.06324 0.07673  62  GLU A N   
380  C CA  . GLU A 55  ? 0.30739 0.26649 0.23132 0.01534  -0.06219 0.08713  62  GLU A CA  
381  C C   . GLU A 55  ? 0.33042 0.29901 0.24839 0.02702  -0.07002 0.08483  62  GLU A C   
382  O O   . GLU A 55  ? 0.33726 0.30586 0.24094 0.03052  -0.07416 0.09725  62  GLU A O   
383  C CB  . GLU A 55  ? 0.33191 0.31253 0.25324 0.01062  -0.05203 0.08232  62  GLU A CB  
384  C CG  . GLU A 55  ? 0.40115 0.38468 0.32793 -0.00019 -0.04378 0.09459  62  GLU A CG  
385  C CD  . GLU A 55  ? 0.43026 0.43798 0.34962 0.00243  -0.03147 0.09324  62  GLU A CD  
386  O OE1 . GLU A 55  ? 0.46237 0.47550 0.36464 0.01209  -0.03131 0.08171  62  GLU A OE1 
387  O OE2 . GLU A 55  ? 0.51131 0.53145 0.43995 -0.00441 -0.02311 0.10471  62  GLU A OE2 
388  N N   . SER A 56  ? 0.28408 0.26400 0.21446 0.03227  -0.07301 0.07166  63  SER A N   
389  C CA  . SER A 56  ? 0.31929 0.31599 0.24999 0.04058  -0.08295 0.07222  63  SER A CA  
390  C C   . SER A 56  ? 0.38437 0.37030 0.31435 0.05373  -0.08941 0.08421  63  SER A C   
391  O O   . SER A 56  ? 0.41628 0.41643 0.34243 0.06068  -0.09854 0.09081  63  SER A O   
392  C CB  . SER A 56  ? 0.31433 0.33119 0.26470 0.04013  -0.08510 0.06031  63  SER A CB  
393  O OG  . SER A 56  ? 0.39899 0.41361 0.36669 0.05022  -0.08262 0.06028  63  SER A OG  
394  N N   . LEU A 57  ? 0.41404 0.37127 0.34375 0.05810  -0.08674 0.08736  64  LEU A N   
395  C CA  . LEU A 57  ? 0.47216 0.40948 0.39408 0.07425  -0.09343 0.09819  64  LEU A CA  
396  C C   . LEU A 57  ? 0.51606 0.44804 0.42027 0.07262  -0.09916 0.11401  64  LEU A C   
397  O O   . LEU A 57  ? 0.48723 0.42162 0.38704 0.08730  -0.10687 0.12309  64  LEU A O   
398  C CB  . LEU A 57  ? 0.46218 0.35517 0.37523 0.07746  -0.09248 0.09763  64  LEU A CB  
399  C CG  . LEU A 57  ? 0.52377 0.41360 0.44567 0.09036  -0.08812 0.08494  64  LEU A CG  
400  C CD1 . LEU A 57  ? 0.58527 0.41825 0.48341 0.10141  -0.09274 0.08692  64  LEU A CD1 
401  C CD2 . LEU A 57  ? 0.60049 0.52992 0.54006 0.10893  -0.08782 0.08476  64  LEU A CD2 
402  N N   . THR A 58  ? 0.43380 0.36168 0.32799 0.05663  -0.09473 0.11994  65  THR A N   
403  C CA  . THR A 58  ? 0.53681 0.46268 0.41272 0.05523  -0.09796 0.13763  65  THR A CA  
404  C C   . THR A 58  ? 0.53675 0.49426 0.40305 0.05241  -0.09596 0.13549  65  THR A C   
405  O O   . THR A 58  ? 0.54956 0.50892 0.39655 0.05262  -0.09673 0.15016  65  THR A O   
406  C CB  . THR A 58  ? 0.53885 0.43867 0.40754 0.04094  -0.09494 0.15306  65  THR A CB  
407  O OG1 . THR A 58  ? 0.53117 0.45045 0.40684 0.02678  -0.08403 0.14929  65  THR A OG1 
408  C CG2 . THR A 58  ? 0.61465 0.47366 0.48598 0.04243  -0.09885 0.15026  65  THR A CG2 
409  N N   . ASP A 59  ? 0.43487 0.41363 0.30973 0.05066  -0.09464 0.11770  66  ASP A N   
410  C CA  . ASP A 59  ? 0.48206 0.48026 0.33936 0.05018  -0.09775 0.11246  66  ASP A CA  
411  C C   . ASP A 59  ? 0.46175 0.47581 0.33440 0.04879  -0.10463 0.09513  66  ASP A C   
412  O O   . ASP A 59  ? 0.44228 0.45770 0.32035 0.04143  -0.09822 0.08204  66  ASP A O   
413  C CB  . ASP A 59  ? 0.49302 0.49242 0.33278 0.04393  -0.08491 0.11333  66  ASP A CB  
414  C CG  . ASP A 59  ? 0.51186 0.52066 0.32103 0.04795  -0.08850 0.10547  66  ASP A CG  
415  O OD1 . ASP A 59  ? 0.58859 0.60235 0.39192 0.05064  -0.10414 0.09902  66  ASP A OD1 
416  O OD2 . ASP A 59  ? 0.60062 0.61119 0.38912 0.04937  -0.07647 0.10690  66  ASP A OD2 
417  N N   . PRO A 60  ? 0.46334 0.49202 0.34556 0.05538  -0.11835 0.09763  67  PRO A N   
418  C CA  . PRO A 60  ? 0.48756 0.53790 0.39041 0.05082  -0.12671 0.08668  67  PRO A CA  
419  C C   . PRO A 60  ? 0.44737 0.49800 0.33123 0.03890  -0.13225 0.07360  67  PRO A C   
420  O O   . PRO A 60  ? 0.38765 0.44689 0.28782 0.03019  -0.13533 0.06337  67  PRO A O   
421  C CB  . PRO A 60  ? 0.45365 0.52628 0.36709 0.06002  -0.14234 0.09835  67  PRO A CB  
422  C CG  . PRO A 60  ? 0.51383 0.56983 0.41586 0.07306  -0.13925 0.11284  67  PRO A CG  
423  C CD  . PRO A 60  ? 0.41911 0.44548 0.30281 0.06816  -0.12481 0.11336  67  PRO A CD  
424  N N   . SER A 61  ? 0.46218 0.50090 0.30800 0.03975  -0.13433 0.07432  68  SER A N   
425  C CA  . SER A 61  ? 0.41615 0.44467 0.23246 0.03285  -0.14089 0.06004  68  SER A CA  
426  C C   . SER A 61  ? 0.45727 0.47437 0.27704 0.02811  -0.12602 0.04727  68  SER A C   
427  O O   . SER A 61  ? 0.45004 0.45493 0.25050 0.02222  -0.13318 0.03349  68  SER A O   
428  C CB  . SER A 61  ? 0.48256 0.49995 0.25479 0.03984  -0.13934 0.06354  68  SER A CB  
429  O OG  . SER A 61  ? 0.53847 0.54427 0.29205 0.04717  -0.11944 0.06710  68  SER A OG  
430  N N   . LYS A 62  ? 0.38791 0.40530 0.22956 0.03002  -0.10797 0.05173  69  LYS A N   
431  C CA  . LYS A 62  ? 0.37583 0.38601 0.22315 0.02578  -0.09512 0.04113  69  LYS A CA  
432  C C   . LYS A 62  ? 0.31257 0.32788 0.18275 0.01639  -0.10300 0.02967  69  LYS A C   
433  O O   . LYS A 62  ? 0.37281 0.37903 0.24125 0.01244  -0.09620 0.01911  69  LYS A O   
434  C CB  . LYS A 62  ? 0.42895 0.43886 0.29617 0.02684  -0.07875 0.05020  69  LYS A CB  
435  C CG  . LYS A 62  ? 0.46568 0.47374 0.31587 0.03208  -0.07122 0.06677  69  LYS A CG  
436  C CD  . LYS A 62  ? 0.40144 0.40997 0.25874 0.02895  -0.05467 0.07286  69  LYS A CD  
437  C CE  . LYS A 62  ? 0.46115 0.47626 0.29812 0.03353  -0.04555 0.09132  69  LYS A CE  
438  N NZ  . LYS A 62  ? 0.52885 0.55435 0.37696 0.02950  -0.02987 0.10030  69  LYS A NZ  
439  N N   . LEU A 63  ? 0.37313 0.40617 0.26636 0.01354  -0.11650 0.03423  70  LEU A N   
440  C CA  . LEU A 63  ? 0.35892 0.40508 0.27741 0.00323  -0.12474 0.02888  70  LEU A CA  
441  C C   . LEU A 63  ? 0.37597 0.42068 0.27723 -0.00858 -0.14805 0.02456  70  LEU A C   
442  O O   . LEU A 63  ? 0.37592 0.43695 0.30199 -0.02079 -0.15891 0.02520  70  LEU A O   
443  C CB  . LEU A 63  ? 0.27515 0.34865 0.23328 0.00895  -0.12394 0.04015  70  LEU A CB  
444  C CG  . LEU A 63  ? 0.37603 0.44273 0.34879 0.01890  -0.10517 0.04157  70  LEU A CG  
445  C CD1 . LEU A 63  ? 0.42197 0.51192 0.42441 0.03064  -0.10546 0.05199  70  LEU A CD1 
446  C CD2 . LEU A 63  ? 0.30283 0.35789 0.27841 0.01193  -0.09373 0.03008  70  LEU A CD2 
447  N N   . ASP A 64  ? 0.36785 0.39279 0.22599 -0.00553 -0.15604 0.02137  71  ASP A N   
448  C CA  . ASP A 64  ? 0.40766 0.42328 0.24881 -0.01562 -0.17030 0.01296  71  ASP A CA  
449  C C   . ASP A 64  ? 0.41322 0.40521 0.24623 -0.02573 -0.16965 -0.00105 71  ASP A C   
450  O O   . ASP A 64  ? 0.46283 0.44803 0.29552 -0.03907 -0.18374 -0.00524 71  ASP A O   
451  C CB  . ASP A 64  ? 0.47030 0.46631 0.26438 -0.00630 -0.17177 0.01041  71  ASP A CB  
452  C CG  . ASP A 64  ? 0.44770 0.46617 0.24828 0.00129  -0.17659 0.02510  71  ASP A CG  
453  O OD1 . ASP A 64  ? 0.52115 0.56949 0.36241 -0.00004 -0.18113 0.03614  71  ASP A OD1 
454  O OD2 . ASP A 64  ? 0.50677 0.51339 0.27118 0.01058  -0.17436 0.02653  71  ASP A OD2 
455  N N   . SER A 65  ? 0.42687 0.40502 0.25371 -0.01966 -0.15417 -0.00674 72  SER A N   
456  C CA  . SER A 65  ? 0.42894 0.38425 0.24925 -0.02614 -0.15089 -0.01885 72  SER A CA  
457  C C   . SER A 65  ? 0.44794 0.42555 0.31514 -0.03924 -0.15195 -0.01436 72  SER A C   
458  O O   . SER A 65  ? 0.41866 0.37983 0.28507 -0.04394 -0.14682 -0.02210 72  SER A O   
459  C CB  . SER A 65  ? 0.42471 0.35933 0.21680 -0.01053 -0.13173 -0.02549 72  SER A CB  
460  O OG  . SER A 65  ? 0.38437 0.34390 0.20430 -0.00241 -0.11401 -0.01469 72  SER A OG  
461  N N   . GLY A 66  ? 0.36227 0.37831 0.26978 -0.04233 -0.15631 -0.00056 73  GLY A N   
462  C CA  . GLY A 66  ? 0.35801 0.40246 0.31136 -0.05060 -0.15371 0.00693  73  GLY A CA  
463  C C   . GLY A 66  ? 0.30180 0.38040 0.28966 -0.03824 -0.14303 0.01974  73  GLY A C   
464  O O   . GLY A 66  ? 0.30614 0.37368 0.28854 -0.02430 -0.12353 0.01645  73  GLY A O   
465  N N   . LYS A 67  ? 0.25690 0.37407 0.28023 -0.03953 -0.14877 0.03386  74  LYS A N   
466  C CA  . LYS A 67  ? 0.28112 0.42731 0.33238 -0.02166 -0.13741 0.04629  74  LYS A CA  
467  C C   . LYS A 67  ? 0.24553 0.40129 0.32111 -0.01612 -0.11920 0.04628  74  LYS A C   
468  O O   . LYS A 67  ? 0.26525 0.42039 0.34554 0.00304  -0.10346 0.04814  74  LYS A O   
469  C CB  . LYS A 67  ? 0.28976 0.47147 0.36488 -0.01829 -0.14500 0.06061  74  LYS A CB  
470  C CG  . LYS A 67  ? 0.42628 0.59875 0.47726 -0.01604 -0.15764 0.06132  74  LYS A CG  
471  C CD  . LYS A 67  ? 0.45392 0.66315 0.53133 -0.01152 -0.16419 0.07619  74  LYS A CD  
472  C CE  . LYS A 67  ? 0.52008 0.72305 0.57751 0.00110  -0.17043 0.07994  74  LYS A CE  
473  N NZ  . LYS A 67  ? 0.55592 0.73406 0.57720 -0.01223 -0.18643 0.07057  74  LYS A NZ  
474  N N   . GLU A 68  ? 0.19827 0.35848 0.28523 -0.03228 -0.12247 0.04454  75  GLU A N   
475  C CA  . GLU A 68  ? 0.23955 0.41457 0.35043 -0.02669 -0.10604 0.04739  75  GLU A CA  
476  C C   . GLU A 68  ? 0.18408 0.32142 0.27243 -0.01798 -0.08823 0.03204  75  GLU A C   
477  O O   . GLU A 68  ? 0.22457 0.32836 0.28520 -0.02560 -0.08976 0.01930  75  GLU A O   
478  C CB  . GLU A 68  ? 0.17415 0.35859 0.29972 -0.04706 -0.11208 0.05082  75  GLU A CB  
479  C CG  . GLU A 68  ? 0.28665 0.50182 0.43338 -0.05471 -0.12096 0.06599  75  GLU A CG  
480  C CD  . GLU A 68  ? 0.45472 0.65378 0.57990 -0.06484 -0.14039 0.06258  75  GLU A CD  
481  O OE1 . GLU A 68  ? 0.50360 0.66079 0.59219 -0.07067 -0.14746 0.04679  75  GLU A OE1 
482  O OE2 . GLU A 68  ? 0.54118 0.76914 0.68361 -0.06534 -0.14787 0.07605  75  GLU A OE2 
483  N N   . LEU A 69  ? 0.14688 0.28969 0.24496 -0.00040 -0.07205 0.03424  76  LEU A N   
484  C CA  . LEU A 69  ? 0.16925 0.27913 0.24881 0.00626  -0.05819 0.02234  76  LEU A CA  
485  C C   . LEU A 69  ? 0.19042 0.31138 0.28537 0.00795  -0.04765 0.02321  76  LEU A C   
486  O O   . LEU A 69  ? 0.14000 0.28071 0.24858 0.02436  -0.03931 0.03132  76  LEU A O   
487  C CB  . LEU A 69  ? 0.17639 0.27086 0.24388 0.02448  -0.05261 0.02334  76  LEU A CB  
488  C CG  . LEU A 69  ? 0.22725 0.31226 0.27942 0.02478  -0.06166 0.02586  76  LEU A CG  
489  C CD1 . LEU A 69  ? 0.24895 0.31051 0.28717 0.04059  -0.05671 0.02804  76  LEU A CD1 
490  C CD2 . LEU A 69  ? 0.19092 0.25633 0.22222 0.01028  -0.06548 0.01734  76  LEU A CD2 
491  N N   . HIS A 70  ? 0.17907 0.20737 0.19713 0.04485  -0.01427 0.03011  77  HIS A N   
492  C CA  . HIS A 70  ? 0.18127 0.20762 0.20371 0.04107  -0.01253 0.02610  77  HIS A CA  
493  C C   . HIS A 70  ? 0.19104 0.19935 0.20416 0.02793  -0.01864 0.01026  77  HIS A C   
494  O O   . HIS A 70  ? 0.17674 0.17818 0.18305 0.02108  -0.02503 0.00276  77  HIS A O   
495  C CB  . HIS A 70  ? 0.19741 0.25892 0.23976 0.03816  -0.01915 0.03599  77  HIS A CB  
496  C CG  . HIS A 70  ? 0.20633 0.28526 0.25400 0.02303  -0.03558 0.03136  77  HIS A CG  
497  N ND1 . HIS A 70  ? 0.28823 0.39969 0.34687 0.02241  -0.04465 0.04031  77  HIS A ND1 
498  C CD2 . HIS A 70  ? 0.22584 0.29283 0.26729 0.00861  -0.04415 0.01814  77  HIS A CD2 
499  C CE1 . HIS A 70  ? 0.20886 0.32526 0.26591 0.00645  -0.05850 0.03058  77  HIS A CE1 
500  N NE2 . HIS A 70  ? 0.21765 0.30547 0.26453 -0.00132 -0.05727 0.01753  77  HIS A NE2 
501  N N   . ILE A 71  ? 0.17706 0.18039 0.19011 0.02627  -0.01579 0.00709  78  ILE A N   
502  C CA  . ILE A 71  ? 0.17831 0.16896 0.18406 0.01673  -0.02074 -0.00456 78  ILE A CA  
503  C C   . ILE A 71  ? 0.18546 0.19019 0.20182 0.01203  -0.02345 0.00002  78  ILE A C   
504  O O   . ILE A 71  ? 0.18662 0.19996 0.20896 0.01898  -0.01569 0.00870  78  ILE A O   
505  C CB  . ILE A 71  ? 0.20115 0.16835 0.19175 0.02043  -0.01307 -0.01313 78  ILE A CB  
506  C CG1 . ILE A 71  ? 0.19760 0.14805 0.18010 0.02286  -0.00842 -0.01728 78  ILE A CG1 
507  C CG2 . ILE A 71  ? 0.21960 0.18104 0.20435 0.01257  -0.01926 -0.02235 78  ILE A CG2 
508  C CD1 . ILE A 71  ? 0.23180 0.15804 0.19963 0.02496  0.00007  -0.02666 78  ILE A CD1 
509  N N   . ASN A 72  ? 0.19306 0.19784 0.21127 0.00091  -0.03247 -0.00525 79  ASN A N   
510  C CA  . ASN A 72  ? 0.16244 0.17437 0.19020 -0.00567 -0.03392 -0.00138 79  ASN A CA  
511  C C   . ASN A 72  ? 0.16011 0.15339 0.17612 -0.00734 -0.03367 -0.00872 79  ASN A C   
512  O O   . ASN A 72  ? 0.18364 0.16440 0.18974 -0.00920 -0.03785 -0.01803 79  ASN A O   
513  C CB  . ASN A 72  ? 0.14966 0.17526 0.18986 -0.01820 -0.04395 -0.00075 79  ASN A CB  
514  C CG  . ASN A 72  ? 0.13451 0.18752 0.18926 -0.01673 -0.04610 0.00884  79  ASN A CG  
515  O OD1 . ASN A 72  ? 0.14183 0.20659 0.20355 -0.00616 -0.03766 0.01917  79  ASN A OD1 
516  N ND2 . ASN A 72  ? 0.16576 0.23059 0.22442 -0.02642 -0.05723 0.00588  79  ASN A ND2 
517  N N   . LEU A 73  ? 0.15956 0.15327 0.17665 -0.00487 -0.02783 -0.00294 80  LEU A N   
518  C CA  . LEU A 73  ? 0.16826 0.14864 0.17508 -0.00460 -0.02737 -0.00617 80  LEU A CA  
519  C C   . LEU A 73  ? 0.20557 0.18747 0.22418 -0.01272 -0.02753 0.00068  80  LEU A C   
520  O O   . LEU A 73  ? 0.18228 0.17669 0.21361 -0.01362 -0.02206 0.01144  80  LEU A O   
521  C CB  . LEU A 73  ? 0.18424 0.16163 0.17786 0.00612  -0.01944 -0.00462 80  LEU A CB  
522  C CG  . LEU A 73  ? 0.16042 0.13234 0.14201 0.01278  -0.01683 -0.01188 80  LEU A CG  
523  C CD1 . LEU A 73  ? 0.18338 0.15064 0.14825 0.02224  -0.00901 -0.01216 80  LEU A CD1 
524  C CD2 . LEU A 73  ? 0.20508 0.16746 0.17982 0.00851  -0.02416 -0.02371 80  LEU A CD2 
525  N N   . ILE A 74  ? 0.18587 0.15411 0.20113 -0.01854 -0.03228 -0.00491 81  ILE A N   
526  C CA  . ILE A 74  ? 0.20497 0.16807 0.23118 -0.02920 -0.03233 -0.00075 81  ILE A CA  
527  C C   . ILE A 74  ? 0.23034 0.17455 0.24689 -0.02494 -0.02809 0.00089  81  ILE A C   
528  O O   . ILE A 74  ? 0.23007 0.16006 0.23708 -0.02365 -0.03153 -0.00703 81  ILE A O   
529  C CB  . ILE A 74  ? 0.19111 0.15207 0.22185 -0.04138 -0.04130 -0.00940 81  ILE A CB  
530  C CG1 . ILE A 74  ? 0.22505 0.20778 0.26280 -0.04215 -0.04618 -0.00953 81  ILE A CG1 
531  C CG2 . ILE A 74  ? 0.24590 0.19808 0.28756 -0.05564 -0.04122 -0.00736 81  ILE A CG2 
532  C CD1 . ILE A 74  ? 0.24860 0.23327 0.28698 -0.05296 -0.05622 -0.01799 81  ILE A CD1 
533  N N   . PRO A 75  ? 0.26980 0.21429 0.28863 -0.02114 -0.01950 0.01274  82  PRO A N   
534  C CA  . PRO A 75  ? 0.32088 0.24759 0.33127 -0.01584 -0.01431 0.01773  82  PRO A CA  
535  C C   . PRO A 75  ? 0.29935 0.20810 0.32079 -0.02859 -0.01164 0.02046  82  PRO A C   
536  O O   . PRO A 75  ? 0.31864 0.23395 0.35754 -0.04251 -0.01163 0.02313  82  PRO A O   
537  C CB  . PRO A 75  ? 0.31526 0.25144 0.32105 -0.00514 -0.00506 0.03065  82  PRO A CB  
538  C CG  . PRO A 75  ? 0.28395 0.23887 0.30612 -0.01140 -0.00236 0.03585  82  PRO A CG  
539  C CD  . PRO A 75  ? 0.25688 0.21923 0.28549 -0.01917 -0.01249 0.02397  82  PRO A CD  
540  N N   . ASN A 76  ? 0.29120 0.17684 0.30275 -0.02393 -0.00899 0.01977  83  ASN A N   
541  C CA  . ASN A 76  ? 0.31204 0.17133 0.33005 -0.03509 -0.00402 0.02132  83  ASN A CA  
542  C C   . ASN A 76  ? 0.38402 0.22250 0.39102 -0.02113 0.00634  0.03210  83  ASN A C   
543  O O   . ASN A 76  ? 0.35199 0.17966 0.34603 -0.01034 0.00496  0.02713  83  ASN A O   
544  C CB  . ASN A 76  ? 0.37509 0.22085 0.39044 -0.04563 -0.01234 0.00453  83  ASN A CB  
545  C CG  . ASN A 76  ? 0.39835 0.21300 0.41843 -0.06052 -0.00761 0.00242  83  ASN A CG  
546  O OD1 . ASN A 76  ? 0.41888 0.20853 0.43589 -0.05548 0.00379  0.01186  83  ASN A OD1 
547  N ND2 . ASN A 76  ? 0.49453 0.31036 0.52160 -0.07945 -0.01615 -0.00970 83  ASN A ND2 
548  N N   . LYS A 77  ? 0.37096 0.20540 0.38413 -0.02036 0.01773  0.04866  84  LYS A N   
549  C CA  . LYS A 77  ? 0.39916 0.21571 0.40101 -0.00448 0.02891  0.06266  84  LYS A CA  
550  C C   . LYS A 77  ? 0.40946 0.18645 0.40899 -0.00808 0.03471  0.05973  84  LYS A C   
551  O O   . LYS A 77  ? 0.44867 0.21136 0.43510 0.00960  0.04084  0.06676  84  LYS A O   
552  C CB  . LYS A 77  ? 0.43785 0.25877 0.44608 -0.00235 0.04177  0.08304  84  LYS A CB  
553  C CG  . LYS A 77  ? 0.48806 0.34312 0.48966 0.00903  0.03988  0.08821  84  LYS A CG  
554  C CD  . LYS A 77  ? 0.46228 0.32514 0.47606 0.00522  0.05248  0.10566  84  LYS A CD  
555  C CE  . LYS A 77  ? 0.61653 0.49458 0.61124 0.02676  0.05967  0.11991  84  LYS A CE  
556  N NZ  . LYS A 77  ? 0.55791 0.46383 0.54134 0.03354  0.04999  0.10885  84  LYS A NZ  
557  N N   . GLN A 78  ? 0.48900 0.24812 0.50000 -0.03009 0.03306  0.04932  85  GLN A N   
558  C CA  . GLN A 78  ? 0.49427 0.21132 0.49917 -0.03450 0.03876  0.04299  85  GLN A CA  
559  C C   . GLN A 78  ? 0.53159 0.24321 0.51928 -0.01981 0.03359  0.03159  85  GLN A C   
560  O O   . GLN A 78  ? 0.49258 0.18711 0.47067 -0.00577 0.04008  0.03538  85  GLN A O   
561  C CB  . GLN A 78  ? 0.53553 0.24882 0.55203 -0.06165 0.03046  0.02908  85  GLN A CB  
562  C CG  . GLN A 78  ? 0.68905 0.37059 0.70326 -0.06813 0.03555  0.02810  85  GLN A CG  
563  C CD  . GLN A 78  ? 0.86251 0.54047 0.89166 -0.08254 0.04359  0.04128  85  GLN A CD  
564  O OE1 . GLN A 78  ? 0.90347 0.60744 0.94787 -0.09130 0.04356  0.04890  85  GLN A OE1 
565  N NE2 . GLN A 78  ? 0.86047 0.50707 0.88673 -0.08449 0.05197  0.04459  85  GLN A NE2 
566  N N   . ASP A 79  ? 0.40690 0.14542 0.39322 -0.02178 0.01975  0.01807  86  ASP A N   
567  C CA  . ASP A 79  ? 0.41062 0.15062 0.38374 -0.00939 0.01459  0.00767  86  ASP A CA  
568  C C   . ASP A 79  ? 0.39889 0.16666 0.36657 0.01231  0.01314  0.01717  86  ASP A C   
569  O O   . ASP A 79  ? 0.39335 0.16494 0.35304 0.02471  0.01085  0.01236  86  ASP A O   
570  C CB  . ASP A 79  ? 0.40415 0.16070 0.37853 -0.02240 0.00099  -0.01037 86  ASP A CB  
571  C CG  . ASP A 79  ? 0.52129 0.26563 0.50340 -0.04230 -0.00131 -0.02243 86  ASP A CG  
572  O OD1 . ASP A 79  ? 0.54628 0.26691 0.53099 -0.04510 0.00537  -0.01942 86  ASP A OD1 
573  O OD2 . ASP A 79  ? 0.54478 0.31224 0.53200 -0.05282 -0.01067 -0.03388 86  ASP A OD2 
574  N N   . ARG A 80  ? 0.37049 0.15919 0.34215 0.01648  0.01435  0.03003  87  ARG A N   
575  C CA  . ARG A 80  ? 0.35967 0.17981 0.32468 0.03282  0.00966  0.03554  87  ARG A CA  
576  C C   . ARG A 80  ? 0.32056 0.16393 0.28509 0.03003  -0.00314 0.02004  87  ARG A C   
577  O O   . ARG A 80  ? 0.35307 0.21106 0.31206 0.04200  -0.00726 0.01829  87  ARG A O   
578  C CB  . ARG A 80  ? 0.36779 0.18204 0.32321 0.05433  0.01665  0.04796  87  ARG A CB  
579  C CG  . ARG A 80  ? 0.40090 0.24837 0.34909 0.06881  0.01299  0.05804  87  ARG A CG  
580  C CD  . ARG A 80  ? 0.44514 0.30208 0.38557 0.09027  0.01345  0.06607  87  ARG A CD  
581  N NE  . ARG A 80  ? 0.54368 0.37329 0.48047 0.10337  0.02818  0.08355  87  ARG A NE  
582  C CZ  . ARG A 80  ? 0.57267 0.39789 0.50581 0.12186  0.03277  0.09090  87  ARG A CZ  
583  N NH1 . ARG A 80  ? 0.54351 0.39260 0.47851 0.12790  0.02334  0.08206  87  ARG A NH1 
584  N NH2 . ARG A 80  ? 0.57183 0.37878 0.50434 0.12827  0.04606  0.10326  87  ARG A NH2 
585  N N   . THR A 81  ? 0.26656 0.11574 0.23853 0.01417  -0.00906 0.01026  88  THR A N   
586  C CA  . THR A 81  ? 0.23836 0.10691 0.21009 0.01128  -0.01912 -0.00231 88  THR A CA  
587  C C   . THR A 81  ? 0.25242 0.14227 0.22890 0.00583  -0.02281 -0.00202 88  THR A C   
588  O O   . THR A 81  ? 0.27623 0.16521 0.26069 -0.00175 -0.01911 0.00413  88  THR A O   
589  C CB  . THR A 81  ? 0.25552 0.11072 0.22856 0.00010  -0.02271 -0.01531 88  THR A CB  
590  O OG1 . THR A 81  ? 0.32126 0.16729 0.30263 -0.01570 -0.02223 -0.01590 88  THR A OG1 
591  C CG2 . THR A 81  ? 0.30584 0.13746 0.27102 0.00764  -0.01742 -0.01744 88  THR A CG2 
592  N N   . LEU A 82  ? 0.21115 0.11952 0.18360 0.00972  -0.02893 -0.00841 89  LEU A N   
593  C CA  . LEU A 82  ? 0.23177 0.15546 0.20680 0.00520  -0.03179 -0.01147 89  LEU A CA  
594  C C   . LEU A 82  ? 0.21958 0.14595 0.19664 -0.00058 -0.03788 -0.02290 89  LEU A C   
595  O O   . LEU A 82  ? 0.24546 0.17425 0.21818 0.00363  -0.04080 -0.02867 89  LEU A O   
596  C CB  . LEU A 82  ? 0.20134 0.13951 0.16648 0.01448  -0.03188 -0.00957 89  LEU A CB  
597  C CG  . LEU A 82  ? 0.21353 0.16159 0.17813 0.01197  -0.03210 -0.01326 89  LEU A CG  
598  C CD1 . LEU A 82  ? 0.26252 0.21103 0.23688 0.00778  -0.02582 -0.00417 89  LEU A CD1 
599  C CD2 . LEU A 82  ? 0.24820 0.20572 0.19799 0.02013  -0.03264 -0.01526 89  LEU A CD2 
600  N N   . THR A 83  ? 0.21807 0.14653 0.20277 -0.00970 -0.03940 -0.02459 90  THR A N   
601  C CA  . THR A 83  ? 0.21444 0.14630 0.19973 -0.01414 -0.04436 -0.03298 90  THR A CA  
602  C C   . THR A 83  ? 0.25970 0.20503 0.24696 -0.01287 -0.04417 -0.03221 90  THR A C   
603  O O   . THR A 83  ? 0.20414 0.15698 0.19768 -0.01353 -0.04119 -0.02530 90  THR A O   
604  C CB  . THR A 83  ? 0.24691 0.17218 0.23690 -0.02460 -0.04735 -0.03575 90  THR A CB  
605  O OG1 . THR A 83  ? 0.25208 0.15763 0.23762 -0.02541 -0.04526 -0.03760 90  THR A OG1 
606  C CG2 . THR A 83  ? 0.26408 0.19803 0.25135 -0.02585 -0.04926 -0.04134 90  THR A CG2 
607  N N   . ILE A 84  ? 0.17947 0.12684 0.16202 -0.01044 -0.04564 -0.03835 91  ILE A N   
608  C CA  . ILE A 84  ? 0.21883 0.17236 0.20163 -0.00882 -0.04369 -0.03840 91  ILE A CA  
609  C C   . ILE A 84  ? 0.22477 0.18019 0.21010 -0.01233 -0.04646 -0.04033 91  ILE A C   
610  O O   . ILE A 84  ? 0.21472 0.17042 0.19730 -0.01215 -0.04342 -0.04202 91  ILE A O   
611  C CB  . ILE A 84  ? 0.22373 0.17544 0.19880 -0.00508 -0.04211 -0.04392 91  ILE A CB  
612  C CG1 . ILE A 84  ? 0.19746 0.15039 0.16567 -0.00063 -0.04073 -0.04259 91  ILE A CG1 
613  C CG2 . ILE A 84  ? 0.19862 0.14909 0.17274 -0.00372 -0.03787 -0.04446 91  ILE A CG2 
614  C CD1 . ILE A 84  ? 0.27714 0.23073 0.24379 0.00129  -0.04395 -0.04200 91  ILE A CD1 
615  N N   . VAL A 85  ? 0.16590 0.13066 0.15815 -0.01388 -0.04684 -0.03459 92  VAL A N   
616  C CA  . VAL A 85  ? 0.17856 0.15008 0.17194 -0.01624 -0.05071 -0.03446 92  VAL A CA  
617  C C   . VAL A 85  ? 0.22620 0.20312 0.22033 -0.00912 -0.04560 -0.02913 92  VAL A C   
618  O O   . VAL A 85  ? 0.21665 0.19848 0.21568 -0.00436 -0.04045 -0.02275 92  VAL A O   
619  C CB  . VAL A 85  ? 0.21993 0.20305 0.22213 -0.02407 -0.05667 -0.03110 92  VAL A CB  
620  C CG1 . VAL A 85  ? 0.26246 0.25529 0.26170 -0.02671 -0.06313 -0.03245 92  VAL A CG1 
621  C CG2 . VAL A 85  ? 0.28370 0.25487 0.28516 -0.03128 -0.05875 -0.03558 92  VAL A CG2 
622  N N   . ASP A 86  ? 0.20633 0.18110 0.19498 -0.00710 -0.04523 -0.03046 93  ASP A N   
623  C CA  . ASP A 86  ? 0.17190 0.15026 0.16131 0.00066  -0.03930 -0.02283 93  ASP A CA  
624  C C   . ASP A 86  ? 0.18529 0.17451 0.17212 0.00140  -0.04373 -0.01909 93  ASP A C   
625  O O   . ASP A 86  ? 0.19110 0.17981 0.17163 -0.00416 -0.05001 -0.02539 93  ASP A O   
626  C CB  . ASP A 86  ? 0.17765 0.13795 0.16089 0.00428  -0.03034 -0.02639 93  ASP A CB  
627  C CG  . ASP A 86  ? 0.22825 0.18058 0.20612 0.00041  -0.03097 -0.03284 93  ASP A CG  
628  O OD1 . ASP A 86  ? 0.23176 0.18714 0.20681 0.00285  -0.03014 -0.02858 93  ASP A OD1 
629  O OD2 . ASP A 86  ? 0.23169 0.17761 0.20848 -0.00407 -0.03203 -0.04089 93  ASP A OD2 
630  N N   . THR A 87  ? 0.20450 0.20394 0.19447 0.00995  -0.03978 -0.00807 94  THR A N   
631  C CA  . THR A 87  ? 0.19785 0.20955 0.18286 0.01396  -0.04278 -0.00184 94  THR A CA  
632  C C   . THR A 87  ? 0.19877 0.19410 0.17630 0.02252  -0.03118 0.00245  94  THR A C   
633  O O   . THR A 87  ? 0.20937 0.21288 0.18508 0.03254  -0.02724 0.01450  94  THR A O   
634  C CB  . THR A 87  ? 0.23182 0.27228 0.22736 0.01858  -0.04730 0.01041  94  THR A CB  
635  O OG1 . THR A 87  ? 0.20742 0.24574 0.21167 0.02846  -0.03650 0.01940  94  THR A OG1 
636  C CG2 . THR A 87  ? 0.19547 0.25213 0.19948 0.00589  -0.05956 0.00509  94  THR A CG2 
637  N N   . GLY A 88  ? 0.22804 0.20099 0.20213 0.01832  -0.02531 -0.00654 95  GLY A N   
638  C CA  . GLY A 88  ? 0.19873 0.15462 0.16810 0.02286  -0.01374 -0.00328 95  GLY A CA  
639  C C   . GLY A 88  ? 0.19691 0.15610 0.15793 0.02334  -0.01435 -0.00139 95  GLY A C   
640  O O   . GLY A 88  ? 0.23094 0.20749 0.18656 0.02311  -0.02395 -0.00084 95  GLY A O   
641  N N   . ILE A 89  ? 0.23729 0.17943 0.19648 0.02301  -0.00371 -0.00111 96  ILE A N   
642  C CA  . ILE A 89  ? 0.24903 0.19345 0.19982 0.02614  -0.00013 0.00418  96  ILE A CA  
643  C C   . ILE A 89  ? 0.23183 0.18350 0.17747 0.01954  -0.00820 -0.00616 96  ILE A C   
644  O O   . ILE A 89  ? 0.27118 0.22949 0.20538 0.02369  -0.00786 -0.00261 96  ILE A O   
645  C CB  . ILE A 89  ? 0.25198 0.17503 0.20579 0.02626  0.01586  0.00878  96  ILE A CB  
646  C CG1 . ILE A 89  ? 0.28695 0.21320 0.23137 0.03337  0.02305  0.02004  96  ILE A CG1 
647  C CG2 . ILE A 89  ? 0.26482 0.17723 0.22787 0.01309  0.01638  -0.00498 96  ILE A CG2 
648  C CD1 . ILE A 89  ? 0.32808 0.23454 0.27407 0.03917  0.04078  0.03299  96  ILE A CD1 
649  N N   . GLY A 90  ? 0.25056 0.20052 0.20229 0.01118  -0.01452 -0.01812 97  GLY A N   
650  C CA  . GLY A 90  ? 0.23592 0.18932 0.18266 0.00733  -0.01987 -0.02697 97  GLY A CA  
651  C C   . GLY A 90  ? 0.24186 0.18969 0.19157 0.00606  -0.01067 -0.02778 97  GLY A C   
652  O O   . GLY A 90  ? 0.29415 0.23451 0.25084 0.00548  -0.00054 -0.02229 97  GLY A O   
653  N N   . MET A 91  ? 0.24702 0.19795 0.19258 0.00533  -0.01316 -0.03456 98  MET A N   
654  C CA  . MET A 91  ? 0.22561 0.17718 0.17705 0.00492  -0.00442 -0.03456 98  MET A CA  
655  C C   . MET A 91  ? 0.23396 0.18870 0.16915 0.01207  -0.00137 -0.03383 98  MET A C   
656  O O   . MET A 91  ? 0.26016 0.21418 0.18042 0.01427  -0.00910 -0.04023 98  MET A O   
657  C CB  . MET A 91  ? 0.23941 0.19396 0.20371 -0.00007 -0.00746 -0.04243 98  MET A CB  
658  C CG  . MET A 91  ? 0.27946 0.23248 0.25937 -0.00788 -0.00729 -0.04378 98  MET A CG  
659  S SD  . MET A 91  ? 0.24494 0.20437 0.23414 -0.01202 -0.01629 -0.05247 98  MET A SD  
660  C CE  . MET A 91  ? 0.23080 0.18558 0.20661 -0.00717 -0.02522 -0.05529 98  MET A CE  
661  N N   . THR A 92  ? 0.26792 0.22485 0.20564 0.01494  0.01086  -0.02669 99  THR A N   
662  C CA  . THR A 92  ? 0.26410 0.22409 0.18522 0.02344  0.01689  -0.02536 99  THR A CA  
663  C C   . THR A 92  ? 0.25395 0.21724 0.18115 0.02447  0.01876  -0.03244 99  THR A C   
664  O O   . THR A 92  ? 0.25246 0.21958 0.19959 0.01845  0.01606  -0.03597 99  THR A O   
665  C CB  . THR A 92  ? 0.27687 0.23897 0.19873 0.02765  0.03190  -0.01195 99  THR A CB  
666  O OG1 . THR A 92  ? 0.27791 0.24327 0.22649 0.01998  0.04064  -0.00918 99  THR A OG1 
667  C CG2 . THR A 92  ? 0.29215 0.24989 0.20802 0.02974  0.03219  -0.00216 99  THR A CG2 
668  N N   . LYS A 93  ? 0.29706 0.25942 0.20498 0.03381  0.02383  -0.03415 100 LYS A N   
669  C CA  . LYS A 93  ? 0.25754 0.22316 0.17123 0.03868  0.02953  -0.03801 100 LYS A CA  
670  C C   . LYS A 93  ? 0.27030 0.25202 0.21363 0.03548  0.04001  -0.02912 100 LYS A C   
671  O O   . LYS A 93  ? 0.28011 0.27165 0.24290 0.03384  0.03903  -0.03134 100 LYS A O   
672  C CB  . LYS A 93  ? 0.30883 0.26800 0.19345 0.05101  0.03655  -0.04086 100 LYS A CB  
673  C CG  . LYS A 93  ? 0.34056 0.29884 0.22721 0.05936  0.04329  -0.04539 100 LYS A CG  
674  C CD  . LYS A 93  ? 0.41397 0.36121 0.26746 0.07275  0.05217  -0.04978 100 LYS A CD  
675  C CE  . LYS A 93  ? 0.46833 0.40757 0.32049 0.08264  0.05829  -0.05603 100 LYS A CE  
676  N NZ  . LYS A 93  ? 0.53192 0.46184 0.35450 0.09837  0.07253  -0.05833 100 LYS A NZ  
677  N N   . ALA A 94  ? 0.27221 0.25798 0.22066 0.03371  0.04978  -0.01829 101 ALA A N   
678  C CA  . ALA A 94  ? 0.24350 0.24443 0.22260 0.02692  0.05998  -0.01020 101 ALA A CA  
679  C C   . ALA A 94  ? 0.23111 0.23494 0.23449 0.01242  0.05026  -0.01509 101 ALA A C   
680  O O   . ALA A 94  ? 0.24837 0.26980 0.27810 0.00577  0.05185  -0.01469 101 ALA A O   
681  C CB  . ALA A 94  ? 0.27175 0.27091 0.24979 0.02716  0.07399  0.00326  101 ALA A CB  
682  N N   . ASP A 95  ? 0.25088 0.23998 0.24525 0.00785  0.04021  -0.01950 102 ASP A N   
683  C CA  . ASP A 95  ? 0.23998 0.22895 0.25068 -0.00390 0.03079  -0.02595 102 ASP A CA  
684  C C   . ASP A 95  ? 0.20392 0.20436 0.22141 -0.00260 0.02185  -0.03367 102 ASP A C   
685  O O   . ASP A 95  ? 0.24822 0.26248 0.28679 -0.01097 0.01852  -0.03609 102 ASP A O   
686  C CB  . ASP A 95  ? 0.24082 0.21288 0.23756 -0.00483 0.02284  -0.02856 102 ASP A CB  
687  C CG  . ASP A 95  ? 0.26687 0.22700 0.26200 -0.00663 0.03171  -0.01970 102 ASP A CG  
688  O OD1 . ASP A 95  ? 0.32462 0.28565 0.33496 -0.01309 0.04290  -0.01390 102 ASP A OD1 
689  O OD2 . ASP A 95  ? 0.29839 0.24879 0.27807 -0.00141 0.02791  -0.01763 102 ASP A OD2 
690  N N   . LEU A 96  ? 0.21769 0.21166 0.21621 0.00767  0.01760  -0.03769 103 LEU A N   
691  C CA  . LEU A 96  ? 0.21250 0.21160 0.21414 0.01142  0.01072  -0.04333 103 LEU A CA  
692  C C   . LEU A 96  ? 0.27052 0.29143 0.29026 0.01626  0.01805  -0.03900 103 LEU A C   
693  O O   . LEU A 96  ? 0.23327 0.26914 0.26863 0.01531  0.01254  -0.04011 103 LEU A O   
694  C CB  . LEU A 96  ? 0.23326 0.21501 0.20936 0.02021  0.00746  -0.04861 103 LEU A CB  
695  C CG  . LEU A 96  ? 0.22670 0.19332 0.18909 0.01532  -0.00242 -0.05302 103 LEU A CG  
696  C CD1 . LEU A 96  ? 0.29235 0.24379 0.23131 0.02138  -0.00501 -0.05940 103 LEU A CD1 
697  C CD2 . LEU A 96  ? 0.24164 0.21019 0.21640 0.00849  -0.01139 -0.05561 103 LEU A CD2 
698  N N   . ILE A 97  ? 0.26530 0.29090 0.28280 0.02306  0.03085  -0.03275 104 ILE A N   
699  C CA  . ILE A 97  ? 0.21040 0.25869 0.24453 0.03110  0.04015  -0.02686 104 ILE A CA  
700  C C   . ILE A 97  ? 0.29987 0.37567 0.36815 0.01879  0.04362  -0.02018 104 ILE A C   
701  O O   . ILE A 97  ? 0.30957 0.41320 0.40196 0.01941  0.04284  -0.01725 104 ILE A O   
702  C CB  . ILE A 97  ? 0.25054 0.29149 0.26460 0.04585  0.05426  -0.02314 104 ILE A CB  
703  C CG1 . ILE A 97  ? 0.32735 0.34131 0.30821 0.05632  0.04995  -0.03271 104 ILE A CG1 
704  C CG2 . ILE A 97  ? 0.36132 0.42957 0.39657 0.05515  0.06708  -0.01425 104 ILE A CG2 
705  C CD1 . ILE A 97  ? 0.37475 0.37585 0.32739 0.06837  0.06134  -0.03272 104 ILE A CD1 
706  N N   . ASN A 98  ? 0.28294 0.35216 0.35490 0.00694  0.04737  -0.01736 105 ASN A N   
707  C CA  . ASN A 98  ? 0.26165 0.35422 0.36622 -0.00632 0.05372  -0.01096 105 ASN A CA  
708  C C   . ASN A 98  ? 0.26348 0.34465 0.37647 -0.02585 0.04885  -0.01490 105 ASN A C   
709  O O   . ASN A 98  ? 0.26990 0.36990 0.40888 -0.04084 0.04356  -0.01795 105 ASN A O   
710  C CB  . ASN A 98  ? 0.29623 0.39502 0.40304 0.00029  0.07282  0.00132  105 ASN A CB  
711  C CG  . ASN A 98  ? 0.48058 0.61227 0.62738 -0.01170 0.08099  0.00967  105 ASN A CG  
712  O OD1 . ASN A 98  ? 0.52278 0.68661 0.69135 -0.00763 0.08048  0.01227  105 ASN A OD1 
713  N ND2 . ASN A 98  ? 0.54179 0.66654 0.70023 -0.02692 0.08881  0.01461  105 ASN A ND2 
714  N N   . ASN A 99  ? 0.32828 0.29428 0.24663 -0.00938 0.04300  0.01929  106 ASN A N   
715  C CA  . ASN A 99  ? 0.31116 0.27802 0.24366 -0.00851 0.03254  0.03163  106 ASN A CA  
716  C C   . ASN A 99  ? 0.27810 0.25143 0.24394 -0.00269 0.02637  0.02810  106 ASN A C   
717  O O   . ASN A 99  ? 0.30002 0.27260 0.28288 -0.00298 0.02726  0.03341  106 ASN A O   
718  C CB  . ASN A 99  ? 0.34010 0.30313 0.25120 -0.00808 0.01662  0.04006  106 ASN A CB  
719  C CG  . ASN A 99  ? 0.47994 0.43552 0.35086 -0.01478 0.02039  0.04486  106 ASN A CG  
720  O OD1 . ASN A 99  ? 0.46427 0.41379 0.32329 -0.02069 0.03735  0.04559  106 ASN A OD1 
721  N ND2 . ASN A 99  ? 0.44276 0.40387 0.29199 -0.01419 0.00419  0.04816  106 ASN A ND2 
722  N N   . LEU A 100 ? 0.22486 0.20196 0.19600 -0.00042 0.02116  0.01839  107 LEU A N   
723  C CA  . LEU A 100 ? 0.24531 0.22773 0.24269 0.00400  0.01549  0.01555  107 LEU A CA  
724  C C   . LEU A 100 ? 0.28976 0.27540 0.30430 0.00742  0.02494  0.01257  107 LEU A C   
725  O O   . LEU A 100 ? 0.28971 0.28023 0.32416 0.00886  0.02155  0.01375  107 LEU A O   
726  C CB  . LEU A 100 ? 0.30644 0.29267 0.30134 0.00137  0.00906  0.00652  107 LEU A CB  
727  C CG  . LEU A 100 ? 0.27527 0.27457 0.26197 -0.00113 -0.00422 0.00903  107 LEU A CG  
728  C CD1 . LEU A 100 ? 0.27802 0.28815 0.26236 -0.01089 -0.00795 -0.00280 107 LEU A CD1 
729  C CD2 . LEU A 100 ? 0.38168 0.38813 0.38656 0.00949  -0.01367 0.01831  107 LEU A CD2 
730  N N   . GLY A 101 ? 0.29431 0.27901 0.30013 0.01026  0.03662  0.00824  108 GLY A N   
731  C CA  . GLY A 101 ? 0.31686 0.31454 0.34136 0.01805  0.04420  0.00703  108 GLY A CA  
732  C C   . GLY A 101 ? 0.30176 0.31860 0.34295 0.01190  0.04740  0.01331  108 GLY A C   
733  O O   . GLY A 101 ? 0.29539 0.33071 0.35952 0.01280  0.04605  0.01298  108 GLY A O   
734  N N   . THR A 102 ? 0.26667 0.27845 0.29287 0.00279  0.05164  0.01901  109 THR A N   
735  C CA  . THR A 102 ? 0.30443 0.32652 0.33932 -0.00931 0.05709  0.02534  109 THR A CA  
736  C C   . THR A 102 ? 0.30092 0.31317 0.34681 -0.01555 0.04664  0.02827  109 THR A C   
737  O O   . THR A 102 ? 0.38541 0.41329 0.44978 -0.02463 0.04914  0.02692  109 THR A O   
738  C CB  . THR A 102 ? 0.38054 0.38810 0.38649 -0.01834 0.06386  0.03283  109 THR A CB  
739  O OG1 . THR A 102 ? 0.45375 0.47144 0.44853 -0.01333 0.07695  0.02735  109 THR A OG1 
740  C CG2 . THR A 102 ? 0.37286 0.38120 0.38008 -0.03584 0.07164  0.04047  109 THR A CG2 
741  N N   . ILE A 103 ? 0.31623 0.30535 0.35077 -0.01088 0.03533  0.03090  110 ILE A N   
742  C CA  . ILE A 103 ? 0.33536 0.31048 0.37747 -0.01225 0.02749  0.03191  110 ILE A CA  
743  C C   . ILE A 103 ? 0.35712 0.34951 0.42239 -0.00975 0.02457  0.02271  110 ILE A C   
744  O O   . ILE A 103 ? 0.39101 0.38198 0.46544 -0.01800 0.02385  0.02055  110 ILE A O   
745  C CB  . ILE A 103 ? 0.41857 0.37541 0.44811 -0.00177 0.01651  0.03591  110 ILE A CB  
746  C CG1 . ILE A 103 ? 0.44677 0.38986 0.44862 -0.00178 0.01647  0.04667  110 ILE A CG1 
747  C CG2 . ILE A 103 ? 0.43460 0.37165 0.46839 0.00065  0.01191  0.03681  110 ILE A CG2 
748  C CD1 . ILE A 103 ? 0.50446 0.42291 0.48960 -0.01302 0.02469  0.05705  110 ILE A CD1 
749  N N   . ALA A 104 ? 0.30139 0.30589 0.37082 0.00015  0.02334  0.01713  111 ALA A N   
750  C CA  . ALA A 104 ? 0.33056 0.34641 0.41427 0.00475  0.01978  0.01082  111 ALA A CA  
751  C C   . ALA A 104 ? 0.36441 0.40762 0.46501 0.00094  0.02346  0.00950  111 ALA A C   
752  O O   . ALA A 104 ? 0.30132 0.35597 0.41229 0.00218  0.01802  0.00561  111 ALA A O   
753  C CB  . ALA A 104 ? 0.28169 0.29406 0.35705 0.01500  0.02009  0.00703  111 ALA A CB  
754  N N   . LYS A 105 ? 0.27462 0.33373 0.37819 -0.00469 0.03247  0.01237  112 LYS A N   
755  C CA  . LYS A 105 ? 0.29264 0.39251 0.41840 -0.00882 0.03607  0.01023  112 LYS A CA  
756  C C   . LYS A 105 ? 0.27049 0.37569 0.40577 -0.02738 0.03030  0.00725  112 LYS A C   
757  O O   . LYS A 105 ? 0.21589 0.35222 0.36796 -0.02726 0.02435  0.00272  112 LYS A O   
758  C CB  . LYS A 105 ? 0.29821 0.41741 0.42557 -0.01444 0.04992  0.01292  112 LYS A CB  
759  C CG  . LYS A 105 ? 0.32942 0.50433 0.48554 -0.02138 0.05532  0.01009  112 LYS A CG  
760  C CD  . LYS A 105 ? 0.33511 0.53804 0.49592 -0.01318 0.07133  0.01058  112 LYS A CD  
761  C CE  . LYS A 105 ? 0.33232 0.60644 0.53000 -0.01407 0.07580  0.00685  112 LYS A CE  
762  N NZ  . LYS A 105 ? 0.37552 0.68167 0.57998 -0.02276 0.09558  0.00676  112 LYS A NZ  
763  N N   . SER A 106 ? 0.26863 0.34019 0.38888 -0.04291 0.03178  0.00967  113 SER A N   
764  C CA  . SER A 106 ? 0.25506 0.32004 0.37652 -0.06330 0.02922  0.00482  113 SER A CA  
765  C C   . SER A 106 ? 0.27636 0.32742 0.39587 -0.05507 0.01860  -0.00137 113 SER A C   
766  O O   . SER A 106 ? 0.23092 0.29812 0.35782 -0.06679 0.01390  -0.00903 113 SER A O   
767  C CB  . SER A 106 ? 0.35486 0.37438 0.45250 -0.07949 0.03616  0.01026  113 SER A CB  
768  O OG  . SER A 106 ? 0.40255 0.38073 0.48085 -0.06234 0.03212  0.01588  113 SER A OG  
769  N N   . GLY A 107 ? 0.29833 0.32438 0.40744 -0.03701 0.01512  0.00084  114 GLY A N   
770  C CA  . GLY A 107 ? 0.29237 0.30829 0.39922 -0.02994 0.00809  -0.00546 114 GLY A CA  
771  C C   . GLY A 107 ? 0.24734 0.29620 0.36517 -0.02392 0.00266  -0.00908 114 GLY A C   
772  O O   . GLY A 107 ? 0.22409 0.27488 0.34005 -0.02798 -0.00280 -0.01570 114 GLY A O   
773  N N   . THR A 108 ? 0.19215 0.26387 0.31718 -0.01235 0.00462  -0.00443 115 THR A N   
774  C CA  . THR A 108 ? 0.15317 0.25314 0.28510 -0.00079 -0.00048 -0.00474 115 THR A CA  
775  C C   . THR A 108 ? 0.19338 0.33260 0.34092 -0.01375 -0.00606 -0.00878 115 THR A C   
776  O O   . THR A 108 ? 0.18621 0.33804 0.33178 -0.01203 -0.01523 -0.01186 115 THR A O   
777  C CB  . THR A 108 ? 0.20998 0.32075 0.34367 0.01700  0.00553  0.00074  115 THR A CB  
778  O OG1 . THR A 108 ? 0.24932 0.32364 0.36434 0.02429  0.00940  0.00202  115 THR A OG1 
779  C CG2 . THR A 108 ? 0.21405 0.35080 0.35221 0.03485  0.00034  0.00290  115 THR A CG2 
780  N N   . LYS A 109 ? 0.13026 0.29138 0.29125 -0.02968 -0.00049 -0.00920 116 LYS A N   
781  C CA  . LYS A 109 ? 0.16856 0.37578 0.34686 -0.04859 -0.00543 -0.01502 116 LYS A CA  
782  C C   . LYS A 109 ? 0.18695 0.37167 0.35100 -0.06833 -0.01216 -0.02427 116 LYS A C   
783  O O   . LYS A 109 ? 0.18702 0.40528 0.35634 -0.07418 -0.02284 -0.02997 116 LYS A O   
784  C CB  . LYS A 109 ? 0.14980 0.37856 0.34122 -0.06884 0.00557  -0.01470 116 LYS A CB  
785  C CG  . LYS A 109 ? 0.15951 0.44573 0.37225 -0.09489 0.00181  -0.02242 116 LYS A CG  
786  C CD  . LYS A 109 ? 0.23058 0.50454 0.43862 -0.12604 0.01519  -0.02352 116 LYS A CD  
787  C CE  . LYS A 109 ? 0.31194 0.63843 0.53699 -0.13767 0.01444  -0.02681 116 LYS A CE  
788  N NZ  . LYS A 109 ? 0.36579 0.69431 0.58244 -0.15800 0.00341  -0.03673 116 LYS A NZ  
789  N N   . ALA A 110 ? 0.21395 0.34164 0.35730 -0.07623 -0.00621 -0.02602 117 ALA A N   
790  C CA  . ALA A 110 ? 0.22523 0.32272 0.35046 -0.09108 -0.00935 -0.03639 117 ALA A CA  
791  C C   . ALA A 110 ? 0.23056 0.32772 0.34767 -0.07433 -0.01793 -0.03893 117 ALA A C   
792  O O   . ALA A 110 ? 0.23159 0.33340 0.33908 -0.08689 -0.02432 -0.04877 117 ALA A O   
793  C CB  . ALA A 110 ? 0.28060 0.31519 0.38491 -0.09409 0.00016  -0.03577 117 ALA A CB  
794  N N   . PHE A 111 ? 0.20872 0.29704 0.32481 -0.04930 -0.01701 -0.03094 118 PHE A N   
795  C CA  . PHE A 111 ? 0.20242 0.28648 0.30644 -0.03570 -0.02230 -0.03176 118 PHE A CA  
796  C C   . PHE A 111 ? 0.22151 0.34979 0.33020 -0.03269 -0.03359 -0.03051 118 PHE A C   
797  O O   . PHE A 111 ? 0.18867 0.31790 0.28201 -0.03602 -0.04060 -0.03574 118 PHE A O   
798  C CB  . PHE A 111 ? 0.18543 0.25118 0.28594 -0.01534 -0.01714 -0.02373 118 PHE A CB  
799  C CG  . PHE A 111 ? 0.21256 0.26883 0.29653 -0.00447 -0.01916 -0.02324 118 PHE A CG  
800  C CD1 . PHE A 111 ? 0.22365 0.26481 0.29275 -0.01153 -0.01927 -0.03173 118 PHE A CD1 
801  C CD2 . PHE A 111 ? 0.19420 0.25100 0.27266 0.01193  -0.01845 -0.01460 118 PHE A CD2 
802  C CE1 . PHE A 111 ? 0.20323 0.23503 0.25352 -0.00475 -0.01870 -0.03079 118 PHE A CE1 
803  C CE2 . PHE A 111 ? 0.25588 0.29544 0.31246 0.01829  -0.01789 -0.01305 118 PHE A CE2 
804  C CZ  . PHE A 111 ? 0.21136 0.24105 0.25450 0.00879  -0.01807 -0.02075 118 PHE A CZ  
805  N N   . MET A 112 ? 0.18176 0.34994 0.31064 -0.02476 -0.03549 -0.02348 119 MET A N   
806  C CA  . MET A 112 ? 0.20635 0.42635 0.34380 -0.01649 -0.04797 -0.02062 119 MET A CA  
807  C C   . MET A 112 ? 0.26070 0.51200 0.40095 -0.04380 -0.05769 -0.03194 119 MET A C   
808  O O   . MET A 112 ? 0.26320 0.54033 0.39460 -0.04112 -0.07121 -0.03289 119 MET A O   
809  C CB  . MET A 112 ? 0.20894 0.47148 0.37244 -0.00131 -0.04545 -0.01266 119 MET A CB  
810  C CG  . MET A 112 ? 0.27104 0.50172 0.42659 0.02448  -0.03555 -0.00349 119 MET A CG  
811  S SD  . MET A 112 ? 0.42325 0.62807 0.54956 0.05289  -0.04144 0.00525  119 MET A SD  
812  C CE  . MET A 112 ? 0.31124 0.51021 0.43988 0.08420  -0.03037 0.01501  119 MET A CE  
813  N N   . GLU A 113 ? 0.23361 0.48127 0.38187 -0.07197 -0.05095 -0.04047 120 GLU A N   
814  C CA  . GLU A 113 ? 0.28832 0.55671 0.43341 -0.10515 -0.05786 -0.05429 120 GLU A CA  
815  C C   . GLU A 113 ? 0.27408 0.49885 0.38526 -0.11178 -0.06069 -0.06403 120 GLU A C   
816  O O   . GLU A 113 ? 0.37007 0.62238 0.47140 -0.12671 -0.07300 -0.07302 120 GLU A O   
817  C CB  . GLU A 113 ? 0.28592 0.53656 0.43506 -0.13396 -0.04525 -0.05983 120 GLU A CB  
818  C CG  . GLU A 113 ? 0.38264 0.68533 0.55567 -0.13864 -0.04428 -0.05526 120 GLU A CG  
819  C CD  . GLU A 113 ? 0.39930 0.68040 0.57690 -0.15216 -0.02785 -0.05248 120 GLU A CD  
820  O OE1 . GLU A 113 ? 0.48449 0.70298 0.64015 -0.16461 -0.01842 -0.05545 120 GLU A OE1 
821  O OE2 . GLU A 113 ? 0.40432 0.72822 0.60410 -0.14936 -0.02367 -0.04713 120 GLU A OE2 
822  N N   . ALA A 114 ? 0.29061 0.45239 0.38372 -0.10053 -0.04936 -0.06303 121 ALA A N   
823  C CA  . ALA A 114 ? 0.25951 0.38104 0.32194 -0.10424 -0.04803 -0.07327 121 ALA A CA  
824  C C   . ALA A 114 ? 0.34945 0.49234 0.39908 -0.08811 -0.05922 -0.06875 121 ALA A C   
825  O O   . ALA A 114 ? 0.31971 0.46009 0.34483 -0.10053 -0.06491 -0.07939 121 ALA A O   
826  C CB  . ALA A 114 ? 0.25793 0.32116 0.31143 -0.09182 -0.03326 -0.07214 121 ALA A CB  
827  N N   . LEU A 115 ? 0.24937 0.40945 0.30987 -0.06125 -0.06191 -0.05300 122 LEU A N   
828  C CA  . LEU A 115 ? 0.25292 0.42303 0.29409 -0.04354 -0.07124 -0.04521 122 LEU A CA  
829  C C   . LEU A 115 ? 0.34514 0.57038 0.38512 -0.05204 -0.09020 -0.04749 122 LEU A C   
830  O O   . LEU A 115 ? 0.33507 0.55953 0.34536 -0.05241 -0.09885 -0.04918 122 LEU A O   
831  C CB  . LEU A 115 ? 0.20690 0.37650 0.25594 -0.01358 -0.06864 -0.02797 122 LEU A CB  
832  C CG  . LEU A 115 ? 0.20977 0.32775 0.25000 -0.00492 -0.05302 -0.02529 122 LEU A CG  
833  C CD1 . LEU A 115 ? 0.27096 0.38617 0.31655 0.01920  -0.04956 -0.01114 122 LEU A CD1 
834  C CD2 . LEU A 115 ? 0.23899 0.32442 0.24671 -0.00730 -0.04905 -0.02924 122 LEU A CD2 
835  N N   . GLN A 116 ? 0.34058 0.61947 0.41230 -0.05963 -0.09705 -0.04751 123 GLN A N   
836  C CA  . GLN A 116 ? 0.33448 0.67597 0.41056 -0.07008 -0.11563 -0.05073 123 GLN A CA  
837  C C   . GLN A 116 ? 0.33155 0.65219 0.38274 -0.10460 -0.11564 -0.06914 123 GLN A C   
838  O O   . GLN A 116 ? 0.36345 0.71042 0.40108 -0.10918 -0.12832 -0.07069 123 GLN A O   
839  C CB  . GLN A 116 ? 0.31860 0.70403 0.43307 -0.06969 -0.11311 -0.04590 123 GLN A CB  
840  C CG  . GLN A 116 ? 0.38226 0.79431 0.51526 -0.03011 -0.11478 -0.02748 123 GLN A CG  
841  C CD  . GLN A 116 ? 0.61020 1.06168 0.73711 -0.00995 -0.13089 -0.01821 123 GLN A CD  
842  O OE1 . GLN A 116 ? 0.60140 1.05232 0.70175 -0.01888 -0.14291 -0.02218 123 GLN A OE1 
843  N NE2 . GLN A 116 ? 0.61421 1.09734 0.76306 0.01798  -0.13030 -0.00622 123 GLN A NE2 
844  N N   . ALA A 117 ? 0.32912 0.59796 0.37112 -0.12612 -0.10060 -0.08259 124 ALA A N   
845  C CA  . ALA A 117 ? 0.43143 0.66505 0.44541 -0.15467 -0.09549 -0.10006 124 ALA A CA  
846  C C   . ALA A 117 ? 0.40538 0.59499 0.37885 -0.15229 -0.09259 -0.10854 124 ALA A C   
847  O O   . ALA A 117 ? 0.47438 0.62904 0.42112 -0.17147 -0.08587 -0.12334 124 ALA A O   
848  C CB  . ALA A 117 ? 0.41058 0.60032 0.42990 -0.17377 -0.07780 -0.10797 124 ALA A CB  
849  N N   . GLY A 118 ? 0.42191 0.60415 0.38828 -0.12537 -0.09290 -0.09709 125 GLY A N   
850  C CA  . GLY A 118 ? 0.35974 0.50180 0.28684 -0.12019 -0.08657 -0.10178 125 GLY A CA  
851  C C   . GLY A 118 ? 0.42374 0.51439 0.35096 -0.10101 -0.06643 -0.09693 125 GLY A C   
852  O O   . GLY A 118 ? 0.39862 0.46146 0.29627 -0.09667 -0.05848 -0.10058 125 GLY A O   
853  N N   . ALA A 119 ? 0.32834 0.40932 0.28661 -0.09096 -0.05760 -0.08953 126 ALA A N   
854  C CA  . ALA A 119 ? 0.28805 0.33249 0.24902 -0.07318 -0.04168 -0.08442 126 ALA A CA  
855  C C   . ALA A 119 ? 0.33084 0.38306 0.28477 -0.05215 -0.04443 -0.06792 126 ALA A C   
856  O O   . ALA A 119 ? 0.31185 0.39418 0.26032 -0.04532 -0.05878 -0.05768 126 ALA A O   
857  C CB  . ALA A 119 ? 0.29730 0.33169 0.28863 -0.06914 -0.03401 -0.08031 126 ALA A CB  
858  N N   . ASP A 120 ? 0.32995 0.35396 0.28197 -0.04175 -0.03011 -0.06532 127 ASP A N   
859  C CA  . ASP A 120 ? 0.28044 0.29909 0.22004 -0.02680 -0.02843 -0.05094 127 ASP A CA  
860  C C   . ASP A 120 ? 0.26917 0.27585 0.23153 -0.01708 -0.01835 -0.04469 127 ASP A C   
861  O O   . ASP A 120 ? 0.25657 0.26005 0.24244 -0.01968 -0.01306 -0.05070 127 ASP A O   
862  C CB  . ASP A 120 ? 0.35369 0.35236 0.25720 -0.03136 -0.01977 -0.05553 127 ASP A CB  
863  C CG  . ASP A 120 ? 0.39281 0.37255 0.30300 -0.03628 -0.00139 -0.06869 127 ASP A CG  
864  O OD1 . ASP A 120 ? 0.46190 0.43664 0.37487 -0.04471 0.00200  -0.08412 127 ASP A OD1 
865  O OD2 . ASP A 120 ? 0.36388 0.33422 0.27611 -0.03145 0.01012  -0.06400 127 ASP A OD2 
866  N N   . ILE A 121 ? 0.25484 0.25107 0.20476 -0.00639 -0.01588 -0.03217 128 ILE A N   
867  C CA  . ILE A 121 ? 0.26065 0.24786 0.22801 0.00061  -0.00875 -0.02638 128 ILE A CA  
868  C C   . ILE A 121 ? 0.30304 0.28161 0.28206 -0.00676 0.00436  -0.03623 128 ILE A C   
869  O O   . ILE A 121 ? 0.26311 0.24359 0.26400 -0.00389 0.00715  -0.03529 128 ILE A O   
870  C CB  . ILE A 121 ? 0.24498 0.21249 0.18725 0.01124  -0.00710 -0.01250 128 ILE A CB  
871  C CG1 . ILE A 121 ? 0.33012 0.31414 0.27452 0.02819  -0.02039 -0.00101 128 ILE A CG1 
872  C CG2 . ILE A 121 ? 0.23578 0.18482 0.18415 0.01005  0.00462  -0.01147 128 ILE A CG2 
873  C CD1 . ILE A 121 ? 0.33682 0.29451 0.24623 0.04440  -0.02035 0.01403  128 ILE A CD1 
874  N N   . SER A 122 ? 0.24717 0.22071 0.21243 -0.01486 0.01242  -0.04612 129 SER A N   
875  C CA  . SER A 122 ? 0.31409 0.28971 0.29533 -0.01738 0.02508  -0.05593 129 SER A CA  
876  C C   . SER A 122 ? 0.31546 0.29636 0.32447 -0.01233 0.02286  -0.06178 129 SER A C   
877  O O   . SER A 122 ? 0.28491 0.27197 0.31266 -0.00757 0.02983  -0.06543 129 SER A O   
878  C CB  . SER A 122 ? 0.30714 0.27982 0.26819 -0.02494 0.03638  -0.06679 129 SER A CB  
879  O OG  . SER A 122 ? 0.30213 0.27201 0.25836 -0.02657 0.03434  -0.07823 129 SER A OG  
880  N N   . MET A 123 ? 0.29007 0.26965 0.30072 -0.01378 0.01328  -0.06190 130 MET A N   
881  C CA  . MET A 123 ? 0.21870 0.19191 0.24631 -0.01218 0.01284  -0.06623 130 MET A CA  
882  C C   . MET A 123 ? 0.23823 0.21741 0.28560 -0.00682 0.00796  -0.05517 130 MET A C   
883  O O   . MET A 123 ? 0.24405 0.21401 0.30080 -0.00649 0.00753  -0.05564 130 MET A O   
884  C CB  . MET A 123 ? 0.27456 0.24158 0.28936 -0.02389 0.00716  -0.07395 130 MET A CB  
885  C CG  . MET A 123 ? 0.31133 0.26756 0.30122 -0.03005 0.01369  -0.08774 130 MET A CG  
886  S SD  . MET A 123 ? 0.37680 0.33142 0.34340 -0.04995 0.00417  -0.09826 130 MET A SD  
887  C CE  . MET A 123 ? 0.34571 0.27489 0.32449 -0.05580 0.00754  -0.10417 130 MET A CE  
888  N N   . ILE A 124 ? 0.23306 0.22134 0.28128 -0.00319 0.00605  -0.04556 131 ILE A N   
889  C CA  . ILE A 124 ? 0.19866 0.19176 0.26013 0.00138  0.00283  -0.03637 131 ILE A CA  
890  C C   . ILE A 124 ? 0.22116 0.21043 0.29709 0.00570  0.00577  -0.03672 131 ILE A C   
891  O O   . ILE A 124 ? 0.21693 0.20519 0.30039 0.00658  0.00303  -0.03105 131 ILE A O   
892  C CB  . ILE A 124 ? 0.17182 0.16417 0.22341 0.00495  0.00429  -0.02917 131 ILE A CB  
893  C CG1 . ILE A 124 ? 0.18303 0.17804 0.24294 0.01023  0.00244  -0.02145 131 ILE A CG1 
894  C CG2 . ILE A 124 ? 0.22958 0.21857 0.27737 0.00150  0.01292  -0.03345 131 ILE A CG2 
895  C CD1 . ILE A 124 ? 0.19736 0.18079 0.24021 0.01545  0.00532  -0.01517 131 ILE A CD1 
896  N N   . GLY A 125 ? 0.23716 0.22729 0.31651 0.00966  0.01149  -0.04270 132 GLY A N   
897  C CA  . GLY A 125 ? 0.26469 0.25665 0.35754 0.01901  0.01185  -0.04103 132 GLY A CA  
898  C C   . GLY A 125 ? 0.28963 0.25949 0.38119 0.02305  0.01119  -0.04111 132 GLY A C   
899  O O   . GLY A 125 ? 0.28434 0.24816 0.38041 0.03114  0.00904  -0.03428 132 GLY A O   
900  N N   . GLN A 126 ? 0.26741 0.22087 0.34755 0.01584  0.01331  -0.04877 133 GLN A N   
901  C CA  . GLN A 126 ? 0.33536 0.25779 0.40679 0.01367  0.01479  -0.05030 133 GLN A CA  
902  C C   . GLN A 126 ? 0.27412 0.19446 0.34604 0.00310  0.01008  -0.04099 133 GLN A C   
903  O O   . GLN A 126 ? 0.35927 0.24992 0.42051 -0.00308 0.01284  -0.04084 133 GLN A O   
904  C CB  . GLN A 126 ? 0.32495 0.23020 0.37944 0.00241  0.01850  -0.06373 133 GLN A CB  
905  C CG  . GLN A 126 ? 0.35165 0.26025 0.40235 0.01102  0.02608  -0.07460 133 GLN A CG  
906  C CD  . GLN A 126 ? 0.43704 0.32256 0.46417 -0.00072 0.03092  -0.08973 133 GLN A CD  
907  O OE1 . GLN A 126 ? 0.52783 0.37773 0.54015 -0.00777 0.03356  -0.09515 133 GLN A OE1 
908  N NE2 . GLN A 126 ? 0.49396 0.39552 0.51206 -0.00539 0.03302  -0.09706 133 GLN A NE2 
909  N N   . PHE A 127 ? 0.24623 0.19374 0.32727 0.00056  0.00534  -0.03389 134 PHE A N   
910  C CA  . PHE A 127 ? 0.23693 0.19053 0.32119 -0.00773 0.00340  -0.02594 134 PHE A CA  
911  C C   . PHE A 127 ? 0.30009 0.26122 0.38928 0.00170  0.00286  -0.01603 134 PHE A C   
912  O O   . PHE A 127 ? 0.30865 0.27808 0.39965 -0.00351 0.00335  -0.00977 134 PHE A O   
913  C CB  . PHE A 127 ? 0.20286 0.18402 0.29163 -0.01704 -0.00079 -0.02758 134 PHE A CB  
914  C CG  . PHE A 127 ? 0.25834 0.23711 0.33891 -0.02927 -0.00264 -0.03816 134 PHE A CG  
915  C CD1 . PHE A 127 ? 0.25569 0.22756 0.33235 -0.04856 -0.00195 -0.04276 134 PHE A CD1 
916  C CD2 . PHE A 127 ? 0.22710 0.20817 0.29940 -0.02506 -0.00390 -0.04456 134 PHE A CD2 
917  C CE1 . PHE A 127 ? 0.26472 0.23359 0.32954 -0.06403 -0.00408 -0.05500 134 PHE A CE1 
918  C CE2 . PHE A 127 ? 0.25216 0.23006 0.31135 -0.03782 -0.00581 -0.05558 134 PHE A CE2 
919  C CZ  . PHE A 127 ? 0.26924 0.24114 0.32455 -0.05753 -0.00660 -0.06165 134 PHE A CZ  
920  N N   . GLY A 128 ? 0.26548 0.22807 0.35663 0.01393  0.00236  -0.01573 135 GLY A N   
921  C CA  . GLY A 128 ? 0.29036 0.26059 0.38233 0.02019  0.00028  -0.00805 135 GLY A CA  
922  C C   . GLY A 128 ? 0.26255 0.25001 0.35451 0.01710  0.00022  -0.00721 135 GLY A C   
923  O O   . GLY A 128 ? 0.28531 0.27593 0.37273 0.01829  -0.00061 -0.00217 135 GLY A O   
924  N N   . VAL A 129 ? 0.19874 0.19251 0.29025 0.01403  0.00151  -0.01177 136 VAL A N   
925  C CA  . VAL A 129 ? 0.22703 0.22496 0.31152 0.01420  0.00346  -0.01019 136 VAL A CA  
926  C C   . VAL A 129 ? 0.16057 0.15680 0.23763 0.01257  0.00554  -0.01528 136 VAL A C   
927  O O   . VAL A 129 ? 0.16492 0.15341 0.22920 0.01321  0.00831  -0.01424 136 VAL A O   
928  C CB  . VAL A 129 ? 0.17983 0.18428 0.26563 0.01508  0.00410  -0.00722 136 VAL A CB  
929  C CG1 . VAL A 129 ? 0.22252 0.23167 0.31407 0.01203  0.00570  -0.00256 136 VAL A CG1 
930  C CG2 . VAL A 129 ? 0.21436 0.22492 0.30377 0.01192  0.00059  -0.01092 136 VAL A CG2 
931  N N   . GLY A 130 ? 0.25380 0.16959 0.24470 -0.01369 -0.03118 -0.04810 137 GLY A N   
932  C CA  . GLY A 130 ? 0.21034 0.13269 0.19124 -0.00185 -0.02692 -0.05044 137 GLY A CA  
933  C C   . GLY A 130 ? 0.23520 0.17313 0.22057 0.00038  -0.01953 -0.04198 137 GLY A C   
934  O O   . GLY A 130 ? 0.21269 0.15931 0.19297 0.00715  -0.01618 -0.04177 137 GLY A O   
935  N N   . PHE A 131 ? 0.20079 0.14127 0.19462 -0.00481 -0.01709 -0.03497 138 PHE A N   
936  C CA  . PHE A 131 ? 0.18679 0.13897 0.18392 -0.00340 -0.01202 -0.02953 138 PHE A CA  
937  C C   . PHE A 131 ? 0.20457 0.16752 0.20101 -0.00233 -0.01149 -0.02991 138 PHE A C   
938  O O   . PHE A 131 ? 0.17682 0.14419 0.17209 0.00206  -0.00754 -0.02744 138 PHE A O   
939  C CB  . PHE A 131 ? 0.17958 0.13428 0.18278 -0.00873 -0.01109 -0.02404 138 PHE A CB  
940  C CG  . PHE A 131 ? 0.17380 0.13862 0.17867 -0.00777 -0.00785 -0.02152 138 PHE A CG  
941  C CD1 . PHE A 131 ? 0.15961 0.12507 0.16449 -0.00443 -0.00565 -0.02064 138 PHE A CD1 
942  C CD2 . PHE A 131 ? 0.18518 0.15888 0.19239 -0.00991 -0.00743 -0.02051 138 PHE A CD2 
943  C CE1 . PHE A 131 ? 0.17355 0.14348 0.17960 -0.00444 -0.00420 -0.02011 138 PHE A CE1 
944  C CE2 . PHE A 131 ? 0.20496 0.18376 0.21146 -0.00709 -0.00481 -0.01994 138 PHE A CE2 
945  C CZ  . PHE A 131 ? 0.20000 0.17439 0.20527 -0.00489 -0.00375 -0.02045 138 PHE A CZ  
946  N N   . TYR A 132 ? 0.21254 0.18021 0.21100 -0.00642 -0.01572 -0.03211 139 TYR A N   
947  C CA  . TYR A 132 ? 0.19061 0.17080 0.18929 -0.00383 -0.01541 -0.03113 139 TYR A CA  
948  C C   . TYR A 132 ? 0.21282 0.19416 0.20186 0.00409  -0.01550 -0.03349 139 TYR A C   
949  O O   . TYR A 132 ? 0.19532 0.18511 0.18296 0.00874  -0.01376 -0.03033 139 TYR A O   
950  C CB  . TYR A 132 ? 0.17220 0.16293 0.17886 -0.01038 -0.02017 -0.03164 139 TYR A CB  
951  C CG  . TYR A 132 ? 0.18954 0.18257 0.20514 -0.01700 -0.01786 -0.02648 139 TYR A CG  
952  C CD1 . TYR A 132 ? 0.22705 0.22973 0.24504 -0.01408 -0.01281 -0.02187 139 TYR A CD1 
953  C CD2 . TYR A 132 ? 0.21744 0.20156 0.23733 -0.02487 -0.02040 -0.02588 139 TYR A CD2 
954  C CE1 . TYR A 132 ? 0.21884 0.22590 0.24184 -0.01803 -0.00990 -0.01688 139 TYR A CE1 
955  C CE2 . TYR A 132 ? 0.22627 0.21392 0.25288 -0.02993 -0.01719 -0.01872 139 TYR A CE2 
956  C CZ  . TYR A 132 ? 0.22699 0.22780 0.25430 -0.02600 -0.01170 -0.01430 139 TYR A CZ  
957  O OH  . TYR A 132 ? 0.25523 0.26171 0.28625 -0.02911 -0.00791 -0.00702 139 TYR A OH  
958  N N   . SER A 133 ? 0.21450 0.18749 0.19561 0.00750  -0.01668 -0.03814 140 SER A N   
959  C CA  . SER A 133 ? 0.17309 0.14968 0.14289 0.01718  -0.01455 -0.03859 140 SER A CA  
960  C C   . SER A 133 ? 0.16127 0.14108 0.13307 0.02125  -0.00606 -0.02962 140 SER A C   
961  O O   . SER A 133 ? 0.18453 0.16983 0.14877 0.02886  -0.00252 -0.02601 140 SER A O   
962  C CB  . SER A 133 ? 0.19633 0.16360 0.15575 0.02222  -0.01650 -0.04607 140 SER A CB  
963  O OG  . SER A 133 ? 0.22230 0.18357 0.18478 0.02411  -0.01084 -0.04280 140 SER A OG  
964  N N   . ALA A 134 ? 0.15427 0.13086 0.13592 0.01609  -0.00311 -0.02566 141 ALA A N   
965  C CA  . ALA A 134 ? 0.17063 0.14872 0.15675 0.01716  0.00289  -0.01814 141 ALA A CA  
966  C C   . ALA A 134 ? 0.19697 0.17885 0.18051 0.02078  0.00409  -0.01381 141 ALA A C   
967  O O   . ALA A 134 ? 0.18126 0.16302 0.16484 0.02398  0.00937  -0.00645 141 ALA A O   
968  C CB  . ALA A 134 ? 0.18262 0.15686 0.17818 0.01054  0.00286  -0.01733 141 ALA A CB  
969  N N   . TYR A 135 ? 0.17638 0.16263 0.15899 0.02056  -0.00055 -0.01692 142 TYR A N   
970  C CA  . TYR A 135 ? 0.18703 0.17807 0.16737 0.02624  0.00022  -0.01229 142 TYR A CA  
971  C C   . TYR A 135 ? 0.18874 0.18671 0.15776 0.03472  0.00005  -0.01012 142 TYR A C   
972  O O   . TYR A 135 ? 0.22300 0.22557 0.18854 0.04147  0.00081  -0.00448 142 TYR A O   
973  C CB  . TYR A 135 ? 0.18445 0.18297 0.16999 0.02429  -0.00417 -0.01534 142 TYR A CB  
974  C CG  . TYR A 135 ? 0.19304 0.18525 0.18596 0.01974  -0.00177 -0.01529 142 TYR A CG  
975  C CD1 . TYR A 135 ? 0.19247 0.17834 0.18608 0.02390  0.00177  -0.01166 142 TYR A CD1 
976  C CD2 . TYR A 135 ? 0.18278 0.17327 0.18000 0.01232  -0.00325 -0.01896 142 TYR A CD2 
977  C CE1 . TYR A 135 ? 0.20119 0.18048 0.19824 0.02100  0.00289  -0.01395 142 TYR A CE1 
978  C CE2 . TYR A 135 ? 0.18153 0.16821 0.18230 0.00980  -0.00141 -0.01907 142 TYR A CE2 
979  C CZ  . TYR A 135 ? 0.18435 0.16585 0.18425 0.01425  0.00127  -0.01764 142 TYR A CZ  
980  O OH  . TYR A 135 ? 0.19420 0.17129 0.19460 0.01277  0.00192  -0.02007 142 TYR A OH  
981  N N   . LEU A 136 ? 0.20487 0.20344 0.16638 0.03646  -0.00054 -0.01403 143 LEU A N   
982  C CA  . LEU A 136 ? 0.21544 0.22098 0.16314 0.04668  0.00130  -0.01080 143 LEU A CA  
983  C C   . LEU A 136 ? 0.22448 0.22823 0.17333 0.05063  0.01107  0.00271  143 LEU A C   
984  O O   . LEU A 136 ? 0.21968 0.22987 0.15867 0.05972  0.01388  0.01040  143 LEU A O   
985  C CB  . LEU A 136 ? 0.22864 0.23362 0.16645 0.04955  -0.00044 -0.01902 143 LEU A CB  
986  C CG  . LEU A 136 ? 0.20208 0.20578 0.13590 0.04622  -0.01144 -0.03296 143 LEU A CG  
987  C CD1 . LEU A 136 ? 0.24016 0.23602 0.16467 0.04980  -0.01188 -0.04133 143 LEU A CD1 
988  C CD2 . LEU A 136 ? 0.20605 0.22215 0.12969 0.05195  -0.01871 -0.03592 143 LEU A CD2 
989  N N   . VAL A 137 ? 0.19195 0.18761 0.15313 0.04356  0.01593  0.00648  144 VAL A N   
990  C CA  . VAL A 137 ? 0.19739 0.19142 0.16310 0.04443  0.02483  0.01956  144 VAL A CA  
991  C C   . VAL A 137 ? 0.21892 0.20035 0.19822 0.03662  0.02577  0.02362  144 VAL A C   
992  O O   . VAL A 137 ? 0.21541 0.19168 0.20018 0.03575  0.03182  0.03511  144 VAL A O   
993  C CB  . VAL A 137 ? 0.22367 0.22348 0.19221 0.04411  0.03031  0.02146  144 VAL A CB  
994  C CG1 . VAL A 137 ? 0.20349 0.21391 0.15459 0.05524  0.03044  0.01721  144 VAL A CG1 
995  C CG2 . VAL A 137 ? 0.17908 0.17390 0.15974 0.03485  0.02685  0.01349  144 VAL A CG2 
996  N N   . ALA A 138 ? 0.21772 0.19346 0.20222 0.03094  0.01996  0.01452  145 ALA A N   
997  C CA  . ALA A 138 ? 0.20883 0.17172 0.20343 0.02451  0.01976  0.01493  145 ALA A CA  
998  C C   . ALA A 138 ? 0.23720 0.19537 0.22818 0.02934  0.01700  0.01317  145 ALA A C   
999  O O   . ALA A 138 ? 0.23477 0.20234 0.22141 0.03223  0.01266  0.00703  145 ALA A O   
1000 C CB  . ALA A 138 ? 0.17978 0.14168 0.18155 0.01634  0.01611  0.00646  145 ALA A CB  
1001 N N   . GLU A 139 ? 0.24943 0.19299 0.24347 0.03020  0.01937  0.01872  146 GLU A N   
1002 C CA  . GLU A 139 ? 0.26024 0.19725 0.25136 0.03661  0.01730  0.01630  146 GLU A CA  
1003 C C   . GLU A 139 ? 0.27894 0.21084 0.27373 0.03193  0.01369  0.00567  146 GLU A C   
1004 O O   . GLU A 139 ? 0.27305 0.20846 0.26476 0.03820  0.01192  0.00133  146 GLU A O   
1005 C CB  . GLU A 139 ? 0.32971 0.24846 0.32067 0.04137  0.02127  0.02644  146 GLU A CB  
1006 C CG  . GLU A 139 ? 0.33448 0.23282 0.33516 0.03130  0.02239  0.02751  146 GLU A CG  
1007 C CD  . GLU A 139 ? 0.53048 0.40737 0.53260 0.03416  0.02658  0.03973  146 GLU A CD  
1008 O OE1 . GLU A 139 ? 0.58730 0.46673 0.58139 0.04557  0.02968  0.04935  146 GLU A OE1 
1009 O OE2 . GLU A 139 ? 0.50134 0.35821 0.51302 0.02465  0.02610  0.04000  146 GLU A OE2 
1010 N N   . LYS A 140 ? 0.22880 0.15574 0.22985 0.02216  0.01270  0.00202  147 LYS A N   
1011 C CA  . LYS A 140 ? 0.23037 0.15470 0.23247 0.01821  0.00890  -0.00784 147 LYS A CA  
1012 C C   . LYS A 140 ? 0.20451 0.13744 0.21175 0.00956  0.00730  -0.01002 147 LYS A C   
1013 O O   . LYS A 140 ? 0.20871 0.14286 0.22179 0.00529  0.00940  -0.00440 147 LYS A O   
1014 C CB  . LYS A 140 ? 0.19494 0.09736 0.19828 0.01708  0.00761  -0.01087 147 LYS A CB  
1015 C CG  . LYS A 140 ? 0.22878 0.12918 0.22892 0.01552  0.00311  -0.02256 147 LYS A CG  
1016 C CD  . LYS A 140 ? 0.30803 0.18380 0.30495 0.01807  0.00087  -0.02831 147 LYS A CD  
1017 C CE  . LYS A 140 ? 0.32296 0.18460 0.32950 0.00576  -0.00275 -0.02883 147 LYS A CE  
1018 N NZ  . LYS A 140 ? 0.46234 0.29413 0.46637 0.00688  -0.00612 -0.03487 147 LYS A NZ  
1019 N N   . VAL A 141 ? 0.18762 0.12830 0.19288 0.00821  0.00436  -0.01662 148 VAL A N   
1020 C CA  . VAL A 141 ? 0.16867 0.11590 0.17787 0.00186  0.00237  -0.01839 148 VAL A CA  
1021 C C   . VAL A 141 ? 0.18756 0.13124 0.19542 -0.00060 -0.00155 -0.02529 148 VAL A C   
1022 O O   . VAL A 141 ? 0.22228 0.16723 0.22340 0.00386  -0.00199 -0.02936 148 VAL A O   
1023 C CB  . VAL A 141 ? 0.20649 0.16566 0.21322 0.00285  0.00222  -0.01828 148 VAL A CB  
1024 C CG1 . VAL A 141 ? 0.22228 0.18518 0.23241 -0.00158 0.00043  -0.01918 148 VAL A CG1 
1025 C CG2 . VAL A 141 ? 0.22450 0.18749 0.22907 0.00675  0.00463  -0.01385 148 VAL A CG2 
1026 N N   . THR A 142 ? 0.17967 0.12215 0.19384 -0.00695 -0.00448 -0.02638 149 THR A N   
1027 C CA  . THR A 142 ? 0.21997 0.16154 0.23145 -0.00913 -0.00992 -0.03370 149 THR A CA  
1028 C C   . THR A 142 ? 0.22638 0.18100 0.24124 -0.01187 -0.01183 -0.03194 149 THR A C   
1029 O O   . THR A 142 ? 0.22910 0.18916 0.25345 -0.01506 -0.01082 -0.02697 149 THR A O   
1030 C CB  . THR A 142 ? 0.19595 0.12411 0.21286 -0.01464 -0.01426 -0.03781 149 THR A CB  
1031 O OG1 . THR A 142 ? 0.23893 0.15079 0.25320 -0.01107 -0.01169 -0.03746 149 THR A OG1 
1032 C CG2 . THR A 142 ? 0.21752 0.14420 0.22755 -0.01526 -0.02168 -0.04836 149 THR A CG2 
1033 N N   . VAL A 143 ? 0.17681 0.13743 0.18367 -0.00921 -0.01370 -0.03463 150 VAL A N   
1034 C CA  . VAL A 143 ? 0.19795 0.16880 0.20655 -0.01004 -0.01551 -0.03165 150 VAL A CA  
1035 C C   . VAL A 143 ? 0.19442 0.16904 0.19799 -0.01028 -0.02193 -0.03700 150 VAL A C   
1036 O O   . VAL A 143 ? 0.22740 0.20152 0.21909 -0.00613 -0.02245 -0.04115 150 VAL A O   
1037 C CB  . VAL A 143 ? 0.17982 0.15464 0.18373 -0.00690 -0.01187 -0.02704 150 VAL A CB  
1038 C CG1 . VAL A 143 ? 0.17619 0.15694 0.18153 -0.00660 -0.01374 -0.02303 150 VAL A CG1 
1039 C CG2 . VAL A 143 ? 0.18750 0.15925 0.19472 -0.00644 -0.00766 -0.02413 150 VAL A CG2 
1040 N N   . ILE A 144 ? 0.17276 0.15383 0.18510 -0.01420 -0.02694 -0.03694 151 ILE A N   
1041 C CA  . ILE A 144 ? 0.19200 0.18036 0.19987 -0.01424 -0.03505 -0.04209 151 ILE A CA  
1042 C C   . ILE A 144 ? 0.20507 0.20579 0.21224 -0.01020 -0.03498 -0.03480 151 ILE A C   
1043 O O   . ILE A 144 ? 0.18471 0.18992 0.20268 -0.01052 -0.03252 -0.02846 151 ILE A O   
1044 C CB  . ILE A 144 ? 0.22659 0.21636 0.24741 -0.02229 -0.04264 -0.04701 151 ILE A CB  
1045 C CG1 . ILE A 144 ? 0.25911 0.23247 0.28553 -0.02759 -0.04100 -0.05023 151 ILE A CG1 
1046 C CG2 . ILE A 144 ? 0.23380 0.22951 0.24649 -0.02211 -0.05338 -0.05607 151 ILE A CG2 
1047 C CD1 . ILE A 144 ? 0.28830 0.24671 0.29880 -0.02313 -0.04181 -0.05922 151 ILE A CD1 
1048 N N   . THR A 145 ? 0.20539 0.21130 0.19895 -0.00498 -0.03716 -0.03495 152 THR A N   
1049 C CA  . THR A 145 ? 0.18601 0.19950 0.17820 -0.00029 -0.03583 -0.02554 152 THR A CA  
1050 C C   . THR A 145 ? 0.21562 0.24025 0.19563 0.00474  -0.04219 -0.02613 152 THR A C   
1051 O O   . THR A 145 ? 0.22375 0.24864 0.19062 0.00661  -0.04475 -0.03329 152 THR A O   
1052 C CB  . THR A 145 ? 0.17943 0.18496 0.16770 0.00164  -0.02728 -0.01835 152 THR A CB  
1053 O OG1 . THR A 145 ? 0.19187 0.19875 0.18104 0.00533  -0.02618 -0.00894 152 THR A OG1 
1054 C CG2 . THR A 145 ? 0.19683 0.20253 0.17152 0.00421  -0.02437 -0.01926 152 THR A CG2 
1055 N N   . LYS A 146 ? 0.22627 0.26062 0.20928 0.00872  -0.04487 -0.01869 153 LYS A N   
1056 C CA  . LYS A 146 ? 0.19268 0.24002 0.16308 0.01526  -0.05123 -0.01702 153 LYS A CA  
1057 C C   . LYS A 146 ? 0.23295 0.28136 0.20179 0.02228  -0.04733 -0.00254 153 LYS A C   
1058 O O   . LYS A 146 ? 0.21235 0.26228 0.19401 0.02363  -0.04764 0.00214  153 LYS A O   
1059 C CB  . LYS A 146 ? 0.20139 0.26342 0.17911 0.01292  -0.06337 -0.02499 153 LYS A CB  
1060 C CG  . LYS A 146 ? 0.26092 0.34006 0.22594 0.02118  -0.07159 -0.02257 153 LYS A CG  
1061 C CD  . LYS A 146 ? 0.24412 0.32320 0.18604 0.02453  -0.07466 -0.03134 153 LYS A CD  
1062 C CE  . LYS A 146 ? 0.25839 0.35745 0.18520 0.03370  -0.08453 -0.03009 153 LYS A CE  
1063 N NZ  . LYS A 146 ? 0.28985 0.39462 0.21073 0.04370  -0.07876 -0.01126 153 LYS A NZ  
1064 N N   . HIS A 147 ? 0.21349 0.26059 0.16685 0.02728  -0.04301 0.00512  154 HIS A N   
1065 C CA  . HIS A 147 ? 0.22655 0.27220 0.17555 0.03411  -0.03964 0.02060  154 HIS A CA  
1066 C C   . HIS A 147 ? 0.24597 0.30950 0.18118 0.04328  -0.04700 0.02427  154 HIS A C   
1067 O O   . HIS A 147 ? 0.27760 0.35239 0.20056 0.04441  -0.05242 0.01504  154 HIS A O   
1068 C CB  . HIS A 147 ? 0.24930 0.28353 0.19244 0.03195  -0.02948 0.02909  154 HIS A CB  
1069 C CG  . HIS A 147 ? 0.23320 0.25868 0.17541 0.03586  -0.02498 0.04606  154 HIS A CG  
1070 N ND1 . HIS A 147 ? 0.28954 0.32385 0.21828 0.04445  -0.02556 0.05850  154 HIS A ND1 
1071 C CD2 . HIS A 147 ? 0.30267 0.30899 0.25492 0.03258  -0.02026 0.05264  154 HIS A CD2 
1072 C CE1 . HIS A 147 ? 0.33780 0.35704 0.26976 0.04578  -0.02078 0.07350  154 HIS A CE1 
1073 N NE2 . HIS A 147 ? 0.29108 0.29204 0.23729 0.03835  -0.01806 0.06908  154 HIS A NE2 
1074 N N   . ASN A 148 ? 0.27633 0.34209 0.21233 0.05120  -0.04803 0.03701  155 ASN A N   
1075 C CA  . ASN A 148 ? 0.26062 0.34588 0.18297 0.06164  -0.05588 0.04192  155 ASN A CA  
1076 C C   . ASN A 148 ? 0.32210 0.41351 0.22094 0.06589  -0.05290 0.04563  155 ASN A C   
1077 O O   . ASN A 148 ? 0.36017 0.47068 0.24354 0.07284  -0.06144 0.04126  155 ASN A O   
1078 C CB  . ASN A 148 ? 0.27069 0.35366 0.19561 0.07171  -0.05511 0.05874  155 ASN A CB  
1079 C CG  . ASN A 148 ? 0.29710 0.38717 0.24112 0.07356  -0.06131 0.05469  155 ASN A CG  
1080 O OD1 . ASN A 148 ? 0.31278 0.41922 0.26616 0.06869  -0.06969 0.04128  155 ASN A OD1 
1081 N ND2 . ASN A 148 ? 0.26786 0.34639 0.21817 0.08136  -0.05736 0.06700  155 ASN A ND2 
1082 N N   . ASP A 149 ? 0.30515 0.38317 0.20097 0.06230  -0.04114 0.05362  156 ASP A N   
1083 C CA  . ASP A 149 ? 0.38129 0.46811 0.25625 0.06779  -0.03538 0.06175  156 ASP A CA  
1084 C C   . ASP A 149 ? 0.38520 0.47702 0.25188 0.06460  -0.03416 0.04627  156 ASP A C   
1085 O O   . ASP A 149 ? 0.44663 0.54827 0.29557 0.07040  -0.02793 0.05182  156 ASP A O   
1086 C CB  . ASP A 149 ? 0.37301 0.44568 0.25179 0.06549  -0.02286 0.08224  156 ASP A CB  
1087 C CG  . ASP A 149 ? 0.45348 0.51902 0.33419 0.07237  -0.02371 0.09987  156 ASP A CG  
1088 O OD1 . ASP A 149 ? 0.42336 0.50133 0.29879 0.08193  -0.03329 0.09885  156 ASP A OD1 
1089 O OD2 . ASP A 149 ? 0.51485 0.56140 0.40360 0.06803  -0.01530 0.11457  156 ASP A OD2 
1090 N N   . ASP A 150 ? 0.34041 0.42634 0.21855 0.05699  -0.03953 0.02785  157 ASP A N   
1091 C CA  . ASP A 150 ? 0.29531 0.38028 0.16708 0.05466  -0.03761 0.01366  157 ASP A CA  
1092 C C   . ASP A 150 ? 0.27982 0.36394 0.15618 0.05065  -0.04993 -0.00714 157 ASP A C   
1093 O O   . ASP A 150 ? 0.31095 0.39912 0.19755 0.04867  -0.05928 -0.00942 157 ASP A O   
1094 C CB  . ASP A 150 ? 0.32117 0.39231 0.20694 0.04646  -0.02628 0.01780  157 ASP A CB  
1095 C CG  . ASP A 150 ? 0.33221 0.40815 0.20664 0.04931  -0.01979 0.01214  157 ASP A CG  
1096 O OD1 . ASP A 150 ? 0.32976 0.41462 0.18563 0.05709  -0.02511 0.00023  157 ASP A OD1 
1097 O OD2 . ASP A 150 ? 0.34305 0.41498 0.22678 0.04466  -0.00976 0.01951  157 ASP A OD2 
1098 N N   . GLU A 151 ? 0.37146 0.45046 0.24147 0.04952  -0.04979 -0.02173 158 GLU A N   
1099 C CA  . GLU A 151 ? 0.37212 0.44559 0.24627 0.04435  -0.06118 -0.04161 158 GLU A CA  
1100 C C   . GLU A 151 ? 0.29563 0.35331 0.19545 0.03236  -0.05872 -0.04355 158 GLU A C   
1101 O O   . GLU A 151 ? 0.29633 0.34762 0.20790 0.02923  -0.04898 -0.03195 158 GLU A O   
1102 C CB  . GLU A 151 ? 0.40545 0.47640 0.25858 0.05076  -0.06201 -0.05653 158 GLU A CB  
1103 C CG  . GLU A 151 ? 0.46457 0.55265 0.28843 0.06419  -0.06648 -0.05867 158 GLU A CG  
1104 C CD  . GLU A 151 ? 0.61727 0.71430 0.44183 0.06268  -0.08203 -0.06549 158 GLU A CD  
1105 O OE1 . GLU A 151 ? 0.72056 0.80747 0.55514 0.05399  -0.09234 -0.08185 158 GLU A OE1 
1106 O OE2 . GLU A 151 ? 0.64777 0.76071 0.46674 0.06876  -0.08275 -0.05235 158 GLU A OE2 
1107 N N   . GLN A 152 ? 0.27628 0.32736 0.18467 0.02532  -0.06801 -0.05827 159 GLN A N   
1108 C CA  . GLN A 152 ? 0.25204 0.28927 0.18278 0.01484  -0.06506 -0.05934 159 GLN A CA  
1109 C C   . GLN A 152 ? 0.26596 0.28745 0.19126 0.01547  -0.05789 -0.06532 159 GLN A C   
1110 O O   . GLN A 152 ? 0.32623 0.34227 0.23646 0.01964  -0.06221 -0.07851 159 GLN A O   
1111 C CB  . GLN A 152 ? 0.25538 0.29351 0.20127 0.00559  -0.07724 -0.06925 159 GLN A CB  
1112 C CG  . GLN A 152 ? 0.21971 0.24804 0.19022 -0.00485 -0.07323 -0.06638 159 GLN A CG  
1113 C CD  . GLN A 152 ? 0.26996 0.30790 0.26032 -0.01432 -0.08391 -0.07002 159 GLN A CD  
1114 O OE1 . GLN A 152 ? 0.31227 0.37003 0.30747 -0.01227 -0.08980 -0.06532 159 GLN A OE1 
1115 N NE2 . GLN A 152 ? 0.29199 0.31717 0.29559 -0.02471 -0.08628 -0.07698 159 GLN A NE2 
1116 N N   . TYR A 153 ? 0.23120 0.24545 0.16806 0.01249  -0.04772 -0.05649 160 TYR A N   
1117 C CA  . TYR A 153 ? 0.26429 0.26768 0.19766 0.01459  -0.04017 -0.05926 160 TYR A CA  
1118 C C   . TYR A 153 ? 0.25126 0.24129 0.20260 0.00655  -0.03832 -0.05959 160 TYR A C   
1119 O O   . TYR A 153 ? 0.26751 0.25944 0.23430 0.00036  -0.03845 -0.05307 160 TYR A O   
1120 C CB  . TYR A 153 ? 0.26287 0.27397 0.19187 0.01957  -0.02912 -0.04690 160 TYR A CB  
1121 C CG  . TYR A 153 ? 0.27821 0.30359 0.18827 0.02868  -0.02791 -0.04359 160 TYR A CG  
1122 C CD1 . TYR A 153 ? 0.29708 0.32515 0.18852 0.03809  -0.02706 -0.05249 160 TYR A CD1 
1123 C CD2 . TYR A 153 ? 0.32479 0.36072 0.23423 0.02947  -0.02713 -0.03086 160 TYR A CD2 
1124 C CE1 . TYR A 153 ? 0.33291 0.37717 0.20463 0.04813  -0.02495 -0.04833 160 TYR A CE1 
1125 C CE2 . TYR A 153 ? 0.30467 0.35479 0.19591 0.03842  -0.02527 -0.02519 160 TYR A CE2 
1126 C CZ  . TYR A 153 ? 0.32433 0.38025 0.19634 0.04773  -0.02392 -0.03367 160 TYR A CZ  
1127 O OH  . TYR A 153 ? 0.39581 0.46881 0.24759 0.05821  -0.02091 -0.02669 160 TYR A OH  
1128 N N   . ALA A 154 ? 0.24300 0.22013 0.19094 0.00850  -0.03608 -0.06663 161 ALA A N   
1129 C CA  . ALA A 154 ? 0.23896 0.20398 0.20040 0.00374  -0.03193 -0.06421 161 ALA A CA  
1130 C C   . ALA A 154 ? 0.21263 0.17933 0.17024 0.01009  -0.02251 -0.05897 161 ALA A C   
1131 O O   . ALA A 154 ? 0.26052 0.22612 0.20553 0.01862  -0.02041 -0.06447 161 ALA A O   
1132 C CB  . ALA A 154 ? 0.26001 0.20644 0.22322 0.00052  -0.03776 -0.07517 161 ALA A CB  
1133 N N   . TRP A 155 ? 0.22240 0.19303 0.19102 0.00656  -0.01740 -0.04912 162 TRP A N   
1134 C CA  . TRP A 155 ? 0.20607 0.17970 0.17635 0.00983  -0.01029 -0.04392 162 TRP A CA  
1135 C C   . TRP A 155 ? 0.21553 0.17698 0.19368 0.00816  -0.00944 -0.04455 162 TRP A C   
1136 O O   . TRP A 155 ? 0.21132 0.16610 0.19783 0.00204  -0.01212 -0.04392 162 TRP A O   
1137 C CB  . TRP A 155 ? 0.20741 0.19154 0.18372 0.00631  -0.00721 -0.03388 162 TRP A CB  
1138 C CG  . TRP A 155 ? 0.14611 0.13609 0.12793 0.00652  -0.00197 -0.02820 162 TRP A CG  
1139 C CD1 . TRP A 155 ? 0.17592 0.17915 0.15724 0.00785  0.00218  -0.02246 162 TRP A CD1 
1140 C CD2 . TRP A 155 ? 0.14735 0.13282 0.13703 0.00460  -0.00116 -0.02702 162 TRP A CD2 
1141 N NE1 . TRP A 155 ? 0.17627 0.18384 0.16636 0.00582  0.00422  -0.01908 162 TRP A NE1 
1142 C CE2 . TRP A 155 ? 0.19041 0.18700 0.18405 0.00455  0.00185  -0.02225 162 TRP A CE2 
1143 C CE3 . TRP A 155 ? 0.18799 0.16321 0.18193 0.00292  -0.00258 -0.02853 162 TRP A CE3 
1144 C CZ2 . TRP A 155 ? 0.17351 0.17107 0.17326 0.00371  0.00189  -0.02099 162 TRP A CZ2 
1145 C CZ3 . TRP A 155 ? 0.21496 0.19082 0.21306 0.00339  -0.00091 -0.02581 162 TRP A CZ3 
1146 C CH2 . TRP A 155 ? 0.16820 0.15500 0.16828 0.00407  0.00050  -0.02303 162 TRP A CH2 
1147 N N   . GLU A 156 ? 0.21270 0.17310 0.18842 0.01458  -0.00534 -0.04465 163 GLU A N   
1148 C CA  . GLU A 156 ? 0.22123 0.16998 0.20268 0.01472  -0.00427 -0.04336 163 GLU A CA  
1149 C C   . GLU A 156 ? 0.23125 0.18861 0.21315 0.02153  0.00060  -0.03905 163 GLU A C   
1150 O O   . GLU A 156 ? 0.21576 0.18325 0.19222 0.02865  0.00320  -0.04035 163 GLU A O   
1151 C CB  . GLU A 156 ? 0.26557 0.19434 0.24273 0.01673  -0.00762 -0.05139 163 GLU A CB  
1152 C CG  . GLU A 156 ? 0.25212 0.16598 0.23658 0.01483  -0.00665 -0.04748 163 GLU A CG  
1153 C CD  . GLU A 156 ? 0.37433 0.26488 0.35817 0.01220  -0.01159 -0.05478 163 GLU A CD  
1154 O OE1 . GLU A 156 ? 0.35179 0.22871 0.32541 0.02082  -0.01244 -0.06267 163 GLU A OE1 
1155 O OE2 . GLU A 156 ? 0.37990 0.26574 0.37422 0.00155  -0.01485 -0.05285 163 GLU A OE2 
1156 N N   . SER A 157 ? 0.18939 0.14534 0.17768 0.02026  0.00183  -0.03360 164 SER A N   
1157 C CA  . SER A 157 ? 0.20550 0.17084 0.19466 0.02743  0.00473  -0.02998 164 SER A CA  
1158 C C   . SER A 157 ? 0.16215 0.11882 0.15376 0.02896  0.00527  -0.02535 164 SER A C   
1159 O O   . SER A 157 ? 0.21318 0.16678 0.20832 0.02257  0.00458  -0.02220 164 SER A O   
1160 C CB  . SER A 157 ? 0.18533 0.17143 0.17972 0.02390  0.00515  -0.02596 164 SER A CB  
1161 O OG  . SER A 157 ? 0.17309 0.17200 0.17044 0.03046  0.00660  -0.02296 164 SER A OG  
1162 N N   . SER A 158 ? 0.22144 0.17518 0.21035 0.03912  0.00714  -0.02404 165 SER A N   
1163 C CA  . SER A 158 ? 0.22398 0.17532 0.21378 0.04343  0.00822  -0.01703 165 SER A CA  
1164 C C   . SER A 158 ? 0.20953 0.18446 0.20165 0.04855  0.00785  -0.01373 165 SER A C   
1165 O O   . SER A 158 ? 0.25763 0.23484 0.24826 0.05767  0.00849  -0.00870 165 SER A O   
1166 C CB  . SER A 158 ? 0.30525 0.23493 0.29079 0.05212  0.00988  -0.01610 165 SER A CB  
1167 O OG  . SER A 158 ? 0.27786 0.18504 0.26365 0.04496  0.00853  -0.01978 165 SER A OG  
1168 N N   . ALA A 159 ? 0.19138 0.18433 0.18801 0.04264  0.00628  -0.01588 166 ALA A N   
1169 C CA  . ALA A 159 ? 0.20884 0.22667 0.21155 0.04407  0.00437  -0.01358 166 ALA A CA  
1170 C C   . ALA A 159 ? 0.25994 0.28866 0.26349 0.05680  0.00700  -0.01249 166 ALA A C   
1171 O O   . ALA A 159 ? 0.25848 0.27852 0.25744 0.06249  0.01041  -0.01583 166 ALA A O   
1172 C CB  . ALA A 159 ? 0.23539 0.25690 0.23734 0.04329  0.00091  -0.01053 166 ALA A CB  
1173 N N   . GLY A 160 ? 0.21467 0.26428 0.22365 0.06255  0.00499  -0.00856 167 GLY A N   
1174 C CA  . GLY A 160 ? 0.25274 0.31785 0.26453 0.07625  0.00789  -0.00672 167 GLY A CA  
1175 C C   . GLY A 160 ? 0.21331 0.30048 0.23311 0.07439  0.01080  -0.00762 167 GLY A C   
1176 O O   . GLY A 160 ? 0.25019 0.35019 0.27098 0.08776  0.01508  -0.00663 167 GLY A O   
1177 N N   . GLY A 161 ? 0.18571 0.27756 0.21075 0.05946  0.00944  -0.00845 168 GLY A N   
1178 C CA  . GLY A 161 ? 0.21840 0.33559 0.25360 0.05585  0.01254  -0.00569 168 GLY A CA  
1179 C C   . GLY A 161 ? 0.21095 0.31771 0.23748 0.05568  0.01781  -0.00837 168 GLY A C   
1180 O O   . GLY A 161 ? 0.17688 0.30488 0.21048 0.05247  0.02164  -0.00412 168 GLY A O   
1181 N N   . SER A 162 ? 0.20207 0.27862 0.21399 0.05878  0.01784  -0.01461 169 SER A N   
1182 C CA  . SER A 162 ? 0.16409 0.23208 0.16546 0.06072  0.02126  -0.01892 169 SER A CA  
1183 C C   . SER A 162 ? 0.16170 0.20164 0.15514 0.05181  0.01716  -0.02385 169 SER A C   
1184 O O   . SER A 162 ? 0.19211 0.21571 0.18613 0.04782  0.01345  -0.02444 169 SER A O   
1185 C CB  . SER A 162 ? 0.20456 0.26875 0.19506 0.07911  0.02567  -0.02403 169 SER A CB  
1186 O OG  . SER A 162 ? 0.25128 0.28480 0.23326 0.08394  0.02264  -0.02957 169 SER A OG  
1187 N N   . PHE A 163 ? 0.19542 0.23320 0.18167 0.04950  0.01817  -0.02641 170 PHE A N   
1188 C CA  . PHE A 163 ? 0.17768 0.19350 0.15715 0.04259  0.01387  -0.03141 170 PHE A CA  
1189 C C   . PHE A 163 ? 0.22961 0.24187 0.19486 0.04970  0.01484  -0.03830 170 PHE A C   
1190 O O   . PHE A 163 ? 0.20318 0.23260 0.16370 0.05889  0.02008  -0.03739 170 PHE A O   
1191 C CB  . PHE A 163 ? 0.18276 0.20198 0.16980 0.02897  0.01140  -0.02600 170 PHE A CB  
1192 C CG  . PHE A 163 ? 0.20999 0.24801 0.19901 0.02598  0.01462  -0.01977 170 PHE A CG  
1193 C CD1 . PHE A 163 ? 0.19420 0.25315 0.19547 0.02272  0.01727  -0.01188 170 PHE A CD1 
1194 C CD2 . PHE A 163 ? 0.20701 0.24262 0.18649 0.02565  0.01452  -0.02070 170 PHE A CD2 
1195 C CE1 . PHE A 163 ? 0.19899 0.27505 0.20443 0.01835  0.02110  -0.00349 170 PHE A CE1 
1196 C CE2 . PHE A 163 ? 0.22926 0.28204 0.20974 0.02352  0.01858  -0.01217 170 PHE A CE2 
1197 C CZ  . PHE A 163 ? 0.19575 0.26793 0.18994 0.01927  0.02247  -0.00278 170 PHE A CZ  
1198 N N   . THR A 164 ? 0.19494 0.18650 0.15329 0.04615  0.00954  -0.04552 171 THR A N   
1199 C CA  . THR A 164 ? 0.21148 0.19776 0.15443 0.05194  0.00766  -0.05450 171 THR A CA  
1200 C C   . THR A 164 ? 0.22749 0.21416 0.16976 0.04208  0.00297  -0.05366 171 THR A C   
1201 O O   . THR A 164 ? 0.23765 0.22028 0.19096 0.03136  0.00017  -0.04897 171 THR A O   
1202 C CB  . THR A 164 ? 0.23014 0.18955 0.16465 0.05739  0.00308  -0.06660 171 THR A CB  
1203 O OG1 . THR A 164 ? 0.27772 0.22004 0.22171 0.04514  -0.00268 -0.06636 171 THR A OG1 
1204 C CG2 . THR A 164 ? 0.24122 0.19604 0.17439 0.07025  0.00752  -0.06764 171 THR A CG2 
1205 N N   . VAL A 165 ? 0.22291 0.21566 0.15048 0.04793  0.00223  -0.05839 172 VAL A N   
1206 C CA  . VAL A 165 ? 0.24573 0.24057 0.16888 0.04213  -0.00312 -0.05847 172 VAL A CA  
1207 C C   . VAL A 165 ? 0.29393 0.28079 0.19771 0.05025  -0.00898 -0.07282 172 VAL A C   
1208 O O   . VAL A 165 ? 0.28231 0.27397 0.17122 0.06346  -0.00497 -0.07822 172 VAL A O   
1209 C CB  . VAL A 165 ? 0.26793 0.28505 0.19195 0.04099  0.00250  -0.04527 172 VAL A CB  
1210 C CG1 . VAL A 165 ? 0.27849 0.29786 0.19557 0.03796  -0.00320 -0.04445 172 VAL A CG1 
1211 C CG2 . VAL A 165 ? 0.24481 0.26631 0.18765 0.03200  0.00626  -0.03369 172 VAL A CG2 
1212 N N   . ARG A 166 ? 0.27606 0.25198 0.18015 0.04291  -0.01890 -0.07966 173 ARG A N   
1213 C CA  . ARG A 166 ? 0.34017 0.30949 0.22598 0.04849  -0.02750 -0.09469 173 ARG A CA  
1214 C C   . ARG A 166 ? 0.32582 0.30147 0.21443 0.03993  -0.03656 -0.09400 173 ARG A C   
1215 O O   . ARG A 166 ? 0.30343 0.28166 0.21034 0.02924  -0.03691 -0.08435 173 ARG A O   
1216 C CB  . ARG A 166 ? 0.37338 0.31481 0.25802 0.04871  -0.03371 -0.10963 173 ARG A CB  
1217 C CG  . ARG A 166 ? 0.39819 0.32520 0.30525 0.03358  -0.03799 -0.10635 173 ARG A CG  
1218 C CD  . ARG A 166 ? 0.47106 0.37483 0.38239 0.03573  -0.03560 -0.10979 173 ARG A CD  
1219 N NE  . ARG A 166 ? 0.63680 0.53305 0.57004 0.02334  -0.03488 -0.10046 173 ARG A NE  
1220 C CZ  . ARG A 166 ? 0.64373 0.55206 0.58907 0.02097  -0.02690 -0.08620 173 ARG A CZ  
1221 N NH1 . ARG A 166 ? 0.34860 0.27677 0.28993 0.02767  -0.01939 -0.07875 173 ARG A NH1 
1222 N NH2 . ARG A 166 ? 0.45512 0.35643 0.41721 0.01121  -0.02670 -0.07911 173 ARG A NH2 
1223 N N   . THR A 167 ? 0.35355 0.33292 0.22270 0.04635  -0.04426 -0.10492 174 THR A N   
1224 C CA  . THR A 167 ? 0.35352 0.33907 0.22521 0.03910  -0.05571 -0.10707 174 THR A CA  
1225 C C   . THR A 167 ? 0.39166 0.35839 0.28087 0.02598  -0.06562 -0.11593 174 THR A C   
1226 O O   . THR A 167 ? 0.50184 0.44831 0.39085 0.02514  -0.06681 -0.12498 174 THR A O   
1227 C CB  . THR A 167 ? 0.44197 0.43687 0.28975 0.04894  -0.06143 -0.11548 174 THR A CB  
1228 O OG1 . THR A 167 ? 0.48377 0.49741 0.31502 0.06192  -0.05048 -0.10568 174 THR A OG1 
1229 C CG2 . THR A 167 ? 0.44309 0.44914 0.29442 0.04245  -0.07326 -0.11559 174 THR A CG2 
1230 N N   . ASP A 168 ? 0.35510 0.32991 0.26413 0.01474  -0.06928 -0.10762 175 ASP A N   
1231 C CA  . ASP A 168 ? 0.41989 0.38196 0.35048 0.00095  -0.07614 -0.11142 175 ASP A CA  
1232 C C   . ASP A 168 ? 0.49194 0.45615 0.42189 -0.00488 -0.08983 -0.12185 175 ASP A C   
1233 O O   . ASP A 168 ? 0.50395 0.48880 0.43155 -0.00395 -0.09643 -0.11998 175 ASP A O   
1234 C CB  . ASP A 168 ? 0.37874 0.35178 0.33273 -0.00719 -0.07091 -0.09533 175 ASP A CB  
1235 C CG  . ASP A 168 ? 0.39754 0.36165 0.37507 -0.02087 -0.07556 -0.09625 175 ASP A CG  
1236 O OD1 . ASP A 168 ? 0.56951 0.51160 0.54880 -0.02409 -0.07561 -0.10285 175 ASP A OD1 
1237 O OD2 . ASP A 168 ? 0.46342 0.44308 0.45820 -0.02778 -0.07866 -0.08933 175 ASP A OD2 
1238 N N   . THR A 169 ? 0.52905 0.47267 0.46217 -0.01114 -0.09284 -0.13023 176 THR A N   
1239 C CA  . THR A 169 ? 0.65523 0.59850 0.58937 -0.01895 -0.10488 -0.13963 176 THR A CA  
1240 C C   . THR A 169 ? 0.62601 0.57491 0.58933 -0.03625 -0.11086 -0.13455 176 THR A C   
1241 O O   . THR A 169 ? 0.64627 0.59983 0.61406 -0.04480 -0.12179 -0.14114 176 THR A O   
1242 C CB  . THR A 169 ? 0.61904 0.53595 0.54113 -0.01720 -0.10576 -0.15217 176 THR A CB  
1243 O OG1 . THR A 169 ? 0.69259 0.58759 0.62831 -0.02265 -0.09870 -0.14805 176 THR A OG1 
1244 C CG2 . THR A 169 ? 0.64100 0.55801 0.53422 0.00130  -0.10053 -0.15769 176 THR A CG2 
1245 N N   . GLY A 170 ? 0.58214 0.53281 0.56559 -0.04137 -0.10380 -0.12274 177 GLY A N   
1246 C CA  . GLY A 170 ? 0.57185 0.52914 0.58468 -0.05691 -0.10661 -0.11577 177 GLY A CA  
1247 C C   . GLY A 170 ? 0.50989 0.49860 0.53595 -0.06083 -0.11463 -0.11127 177 GLY A C   
1248 O O   . GLY A 170 ? 0.53591 0.53910 0.54646 -0.05348 -0.12164 -0.11618 177 GLY A O   
1249 N N   . GLU A 171 ? 0.51291 0.51406 0.56776 -0.07124 -0.11294 -0.10066 178 GLU A N   
1250 C CA  . GLU A 171 ? 0.50764 0.54177 0.57965 -0.07451 -0.11982 -0.09479 178 GLU A CA  
1251 C C   . GLU A 171 ? 0.45314 0.50467 0.51372 -0.05948 -0.11854 -0.09038 178 GLU A C   
1252 O O   . GLU A 171 ? 0.41643 0.46096 0.47258 -0.05205 -0.10543 -0.08138 178 GLU A O   
1253 C CB  . GLU A 171 ? 0.44707 0.49226 0.55269 -0.08603 -0.11447 -0.08209 178 GLU A CB  
1254 C CG  . GLU A 171 ? 0.48179 0.56425 0.61049 -0.09022 -0.12056 -0.07487 178 GLU A CG  
1255 C CD  . GLU A 171 ? 0.57711 0.66762 0.71526 -0.10424 -0.13163 -0.08164 178 GLU A CD  
1256 O OE1 . GLU A 171 ? 0.53446 0.61024 0.68490 -0.11768 -0.12938 -0.08221 178 GLU A OE1 
1257 O OE2 . GLU A 171 ? 0.46101 0.57295 0.59453 -0.10196 -0.14292 -0.08589 178 GLU A OE2 
1258 N N   . PRO A 172 ? 0.38388 0.45581 0.43457 -0.05345 -0.12771 -0.09278 179 PRO A N   
1259 C CA  . PRO A 172 ? 0.38677 0.47370 0.42428 -0.03801 -0.12371 -0.08460 179 PRO A CA  
1260 C C   . PRO A 172 ? 0.39963 0.50151 0.45830 -0.03667 -0.11367 -0.06717 179 PRO A C   
1261 O O   . PRO A 172 ? 0.44068 0.55993 0.52683 -0.04563 -0.11758 -0.06346 179 PRO A O   
1262 C CB  . PRO A 172 ? 0.44962 0.55633 0.47533 -0.03344 -0.13689 -0.08954 179 PRO A CB  
1263 C CG  . PRO A 172 ? 0.39787 0.48818 0.41712 -0.04365 -0.14418 -0.10326 179 PRO A CG  
1264 C CD  . PRO A 172 ? 0.44989 0.52726 0.49481 -0.05911 -0.14020 -0.10217 179 PRO A CD  
1265 N N   . MET A 173 ? 0.31801 0.41388 0.36385 -0.02500 -0.10083 -0.05658 180 MET A N   
1266 C CA  . MET A 173 ? 0.31557 0.41864 0.37620 -0.02135 -0.09023 -0.04221 180 MET A CA  
1267 C C   . MET A 173 ? 0.34690 0.47087 0.40650 -0.00969 -0.09208 -0.03266 180 MET A C   
1268 O O   . MET A 173 ? 0.36624 0.49864 0.43984 -0.00543 -0.08527 -0.02223 180 MET A O   
1269 C CB  . MET A 173 ? 0.29598 0.37645 0.34514 -0.01658 -0.07568 -0.03695 180 MET A CB  
1270 C CG  . MET A 173 ? 0.47711 0.53866 0.53145 -0.02525 -0.07013 -0.04103 180 MET A CG  
1271 S SD  . MET A 173 ? 0.43681 0.47696 0.47188 -0.01749 -0.05717 -0.03719 180 MET A SD  
1272 C CE  . MET A 173 ? 0.29759 0.34683 0.33868 -0.00928 -0.05014 -0.02407 180 MET A CE  
1273 N N   . GLY A 174 ? 0.32490 0.45613 0.36617 -0.00240 -0.10012 -0.03525 181 GLY A N   
1274 C CA  . GLY A 174 ? 0.26054 0.40762 0.29766 0.01089  -0.10054 -0.02378 181 GLY A CA  
1275 C C   . GLY A 174 ? 0.28919 0.41661 0.30889 0.02069  -0.08773 -0.01373 181 GLY A C   
1276 O O   . GLY A 174 ? 0.29664 0.42162 0.29454 0.02859  -0.08826 -0.01086 181 GLY A O   
1277 N N   . ARG A 175 ? 0.26001 0.37383 0.28940 0.01970  -0.07633 -0.00820 182 ARG A N   
1278 C CA  . ARG A 175 ? 0.18501 0.27851 0.20235 0.02635  -0.06514 0.00043  182 ARG A CA  
1279 C C   . ARG A 175 ? 0.17375 0.25421 0.20339 0.02206  -0.05577 0.00069  182 ARG A C   
1280 O O   . ARG A 175 ? 0.24303 0.33564 0.29093 0.02138  -0.05584 0.00164  182 ARG A O   
1281 C CB  . ARG A 175 ? 0.24378 0.34303 0.25669 0.03990  -0.06505 0.01317  182 ARG A CB  
1282 C CG  . ARG A 175 ? 0.23026 0.30562 0.22933 0.04485  -0.05537 0.02229  182 ARG A CG  
1283 C CD  . ARG A 175 ? 0.22995 0.30267 0.23034 0.05774  -0.05331 0.03505  182 ARG A CD  
1284 N NE  . ARG A 175 ? 0.21064 0.28828 0.22908 0.06071  -0.05161 0.03409  182 ARG A NE  
1285 C CZ  . ARG A 175 ? 0.20488 0.30633 0.23540 0.06872  -0.05726 0.03707  182 ARG A CZ  
1286 N NH1 . ARG A 175 ? 0.22012 0.34250 0.24659 0.07438  -0.06664 0.04063  182 ARG A NH1 
1287 N NH2 . ARG A 175 ? 0.19796 0.30506 0.24477 0.07229  -0.05338 0.03686  182 ARG A NH2 
1288 N N   . GLY A 176 ? 0.16702 0.22613 0.18699 0.01964  -0.04789 0.00019  183 GLY A N   
1289 C CA  . GLY A 176 ? 0.16390 0.21060 0.19140 0.01802  -0.03958 0.00095  183 GLY A CA  
1290 C C   . GLY A 176 ? 0.22380 0.25751 0.24760 0.00963  -0.03587 -0.00574 183 GLY A C   
1291 O O   . GLY A 176 ? 0.23051 0.26060 0.24308 0.00718  -0.03762 -0.00965 183 GLY A O   
1292 N N   . THR A 177 ? 0.17030 0.19845 0.20263 0.00694  -0.03040 -0.00675 184 THR A N   
1293 C CA  . THR A 177 ? 0.17579 0.19154 0.20462 0.00103  -0.02638 -0.01142 184 THR A CA  
1294 C C   . THR A 177 ? 0.16652 0.18581 0.20849 -0.00367 -0.02417 -0.01287 184 THR A C   
1295 O O   . THR A 177 ? 0.18158 0.20902 0.23334 -0.00035 -0.02134 -0.00865 184 THR A O   
1296 C CB  . THR A 177 ? 0.16738 0.16810 0.18765 0.00371  -0.02036 -0.00878 184 THR A CB  
1297 O OG1 . THR A 177 ? 0.21717 0.21461 0.22713 0.00617  -0.02134 -0.00503 184 THR A OG1 
1298 C CG2 . THR A 177 ? 0.22451 0.21685 0.24252 -0.00097 -0.01690 -0.01294 184 THR A CG2 
1299 N N   . LYS A 178 ? 0.17134 0.18460 0.21318 -0.01037 -0.02492 -0.01796 185 LYS A N   
1300 C CA  . LYS A 178 ? 0.18875 0.20113 0.24151 -0.01550 -0.02159 -0.01723 185 LYS A CA  
1301 C C   . LYS A 178 ? 0.18197 0.17912 0.22518 -0.01482 -0.01632 -0.01854 185 LYS A C   
1302 O O   . LYS A 178 ? 0.19974 0.18815 0.23392 -0.01582 -0.01833 -0.02360 185 LYS A O   
1303 C CB  . LYS A 178 ? 0.24461 0.25998 0.30703 -0.02450 -0.02832 -0.02169 185 LYS A CB  
1304 C CG  . LYS A 178 ? 0.31146 0.34691 0.38981 -0.02765 -0.03419 -0.01972 185 LYS A CG  
1305 C CD  . LYS A 178 ? 0.32901 0.36556 0.42360 -0.04008 -0.03901 -0.02217 185 LYS A CD  
1306 C CE  . LYS A 178 ? 0.51106 0.55259 0.60564 -0.04527 -0.05222 -0.03148 185 LYS A CE  
1307 N NZ  . LYS A 178 ? 0.48786 0.55762 0.60002 -0.04653 -0.05816 -0.02745 185 LYS A NZ  
1308 N N   . VAL A 179 ? 0.16031 0.15617 0.20452 -0.01168 -0.00985 -0.01430 186 VAL A N   
1309 C CA  . VAL A 179 ? 0.19181 0.17692 0.22842 -0.01060 -0.00579 -0.01491 186 VAL A CA  
1310 C C   . VAL A 179 ? 0.17379 0.15832 0.21917 -0.01437 -0.00276 -0.01128 186 VAL A C   
1311 O O   . VAL A 179 ? 0.18807 0.18175 0.24146 -0.01326 0.00156  -0.00521 186 VAL A O   
1312 C CB  . VAL A 179 ? 0.14634 0.12973 0.17579 -0.00434 -0.00205 -0.01353 186 VAL A CB  
1313 C CG1 . VAL A 179 ? 0.16279 0.13954 0.18583 -0.00317 0.00076  -0.01402 186 VAL A CG1 
1314 C CG2 . VAL A 179 ? 0.15368 0.13417 0.17648 -0.00233 -0.00485 -0.01526 186 VAL A CG2 
1315 N N   . ILE A 180 ? 0.15388 0.12747 0.19763 -0.01794 -0.00436 -0.01408 187 ILE A N   
1316 C CA  . ILE A 180 ? 0.21696 0.18487 0.26919 -0.02243 -0.00182 -0.00944 187 ILE A CA  
1317 C C   . ILE A 180 ? 0.16900 0.12887 0.21178 -0.01639 0.00350  -0.00634 187 ILE A C   
1318 O O   . ILE A 180 ? 0.21243 0.16271 0.24561 -0.01318 0.00200  -0.01111 187 ILE A O   
1319 C CB  . ILE A 180 ? 0.21257 0.16909 0.26875 -0.02967 -0.00828 -0.01541 187 ILE A CB  
1320 C CG1 . ILE A 180 ? 0.20826 0.17568 0.27139 -0.03467 -0.01578 -0.02014 187 ILE A CG1 
1321 C CG2 . ILE A 180 ? 0.21127 0.15787 0.27829 -0.03583 -0.00567 -0.00899 187 ILE A CG2 
1322 C CD1 . ILE A 180 ? 0.24470 0.20000 0.30593 -0.04009 -0.02464 -0.03037 187 ILE A CD1 
1323 N N   . LEU A 181 ? 0.15994 0.12629 0.20519 -0.01362 0.00983  0.00209  188 LEU A N   
1324 C CA  . LEU A 181 ? 0.20110 0.16326 0.23675 -0.00678 0.01437  0.00621  188 LEU A CA  
1325 C C   . LEU A 181 ? 0.19277 0.14403 0.23435 -0.00990 0.01734  0.01388  188 LEU A C   
1326 O O   . LEU A 181 ? 0.18516 0.14171 0.23811 -0.01418 0.02179  0.02336  188 LEU A O   
1327 C CB  . LEU A 181 ? 0.15998 0.13499 0.19116 -0.00001 0.01941  0.01069  188 LEU A CB  
1328 C CG  . LEU A 181 ? 0.14242 0.12341 0.16806 0.00324  0.01634  0.00339  188 LEU A CG  
1329 C CD1 . LEU A 181 ? 0.19654 0.18709 0.21597 0.01149  0.02099  0.00597  188 LEU A CD1 
1330 C CD2 . LEU A 181 ? 0.16499 0.13887 0.18099 0.00442  0.01144  -0.00422 188 LEU A CD2 
1331 N N   . HIS A 182 ? 0.18987 0.12616 0.22455 -0.00723 0.01545  0.01095  189 HIS A N   
1332 C CA  . HIS A 182 ? 0.22631 0.14735 0.26402 -0.00777 0.01855  0.01914  189 HIS A CA  
1333 C C   . HIS A 182 ? 0.21487 0.14256 0.24317 0.00224  0.02477  0.02858  189 HIS A C   
1334 O O   . HIS A 182 ? 0.23589 0.16408 0.25224 0.01111  0.02340  0.02506  189 HIS A O   
1335 C CB  . HIS A 182 ? 0.27377 0.17449 0.30670 -0.00648 0.01376  0.01115  189 HIS A CB  
1336 C CG  . HIS A 182 ? 0.26064 0.15689 0.29765 -0.01393 0.00646  -0.00057 189 HIS A CG  
1337 N ND1 . HIS A 182 ? 0.32198 0.20328 0.36980 -0.02397 0.00246  -0.00216 189 HIS A ND1 
1338 C CD2 . HIS A 182 ? 0.29810 0.20340 0.32925 -0.01274 0.00194  -0.01087 189 HIS A CD2 
1339 C CE1 . HIS A 182 ? 0.29303 0.17562 0.33965 -0.02761 -0.00506 -0.01446 189 HIS A CE1 
1340 N NE2 . HIS A 182 ? 0.31444 0.21173 0.35041 -0.02023 -0.00471 -0.01886 189 HIS A NE2 
1341 N N   . LEU A 183 ? 0.22115 0.15749 0.25501 0.00128  0.03148  0.04081  190 LEU A N   
1342 C CA  . LEU A 183 ? 0.23478 0.18326 0.25668 0.01215  0.03710  0.04857  190 LEU A CA  
1343 C C   . LEU A 183 ? 0.25380 0.19059 0.26718 0.02007  0.03924  0.05662  190 LEU A C   
1344 O O   . LEU A 183 ? 0.27076 0.18829 0.29124 0.01610  0.04026  0.06288  190 LEU A O   
1345 C CB  . LEU A 183 ? 0.20201 0.16580 0.23115 0.01080  0.04525  0.06068  190 LEU A CB  
1346 C CG  . LEU A 183 ? 0.19358 0.17354 0.22974 0.00731  0.04436  0.05444  190 LEU A CG  
1347 C CD1 . LEU A 183 ? 0.19946 0.19755 0.24450 0.00771  0.05422  0.06871  190 LEU A CD1 
1348 C CD2 . LEU A 183 ? 0.19494 0.18162 0.21580 0.01560  0.03988  0.04181  190 LEU A CD2 
1349 N N   . LYS A 184 ? 0.26859 0.18239 0.24864 0.07175  0.00175  0.00810  191 LYS A N   
1350 C CA  . LYS A 184 ? 0.28103 0.18887 0.28166 0.08524  -0.00277 0.02167  191 LYS A CA  
1351 C C   . LYS A 184 ? 0.33251 0.20865 0.32881 0.07513  -0.01164 0.03519  191 LYS A C   
1352 O O   . LYS A 184 ? 0.31062 0.18728 0.29452 0.05505  -0.01411 0.03790  191 LYS A O   
1353 C CB  . LYS A 184 ? 0.30399 0.25621 0.32387 0.08806  -0.00618 0.03518  191 LYS A CB  
1354 C CG  . LYS A 184 ? 0.27960 0.26566 0.31998 0.09852  0.00625  0.02721  191 LYS A CG  
1355 C CD  . LYS A 184 ? 0.29269 0.32555 0.36167 0.09430  -0.00122 0.03689  191 LYS A CD  
1356 C CE  . LYS A 184 ? 0.35881 0.41613 0.43122 0.07695  0.00794  0.03157  191 LYS A CE  
1357 N NZ  . LYS A 184 ? 0.36276 0.46911 0.48289 0.07715  0.00908  0.03322  191 LYS A NZ  
1358 N N   . GLU A 185 ? 0.36092 0.21014 0.37031 0.09081  -0.01413 0.04616  192 GLU A N   
1359 C CA  . GLU A 185 ? 0.41075 0.22028 0.41917 0.08324  -0.01761 0.06418  192 GLU A CA  
1360 C C   . GLU A 185 ? 0.44047 0.27235 0.43486 0.06886  -0.02177 0.08799  192 GLU A C   
1361 O O   . GLU A 185 ? 0.42238 0.23137 0.41138 0.05243  -0.01854 0.09953  192 GLU A O   
1362 C CB  . GLU A 185 ? 0.45304 0.23146 0.47824 0.10843  -0.01923 0.07794  192 GLU A CB  
1363 C CG  . GLU A 185 ? 0.62678 0.34852 0.65481 0.10086  -0.01816 0.09354  192 GLU A CG  
1364 C CD  . GLU A 185 ? 0.80488 0.49299 0.84236 0.12289  -0.02127 0.09223  192 GLU A CD  
1365 O OE1 . GLU A 185 ? 0.86182 0.49765 0.89922 0.11493  -0.01800 0.08947  192 GLU A OE1 
1366 O OE2 . GLU A 185 ? 0.84117 0.55699 0.88996 0.14747  -0.02654 0.09339  192 GLU A OE2 
1367 N N   . ASP A 186 ? 0.34767 0.22533 0.33816 0.07448  -0.02807 0.09385  193 ASP A N   
1368 C CA  . ASP A 186 ? 0.35528 0.25572 0.32620 0.06554  -0.03355 0.11172  193 ASP A CA  
1369 C C   . ASP A 186 ? 0.33779 0.26651 0.29824 0.04616  -0.03119 0.09543  193 ASP A C   
1370 O O   . ASP A 186 ? 0.35239 0.30694 0.29636 0.04130  -0.03612 0.10218  193 ASP A O   
1371 C CB  . ASP A 186 ? 0.38479 0.31710 0.35762 0.08556  -0.04751 0.12576  193 ASP A CB  
1372 C CG  . ASP A 186 ? 0.41943 0.39245 0.41700 0.09176  -0.05177 0.10566  193 ASP A CG  
1373 O OD1 . ASP A 186 ? 0.41989 0.38813 0.42879 0.08580  -0.04036 0.08566  193 ASP A OD1 
1374 O OD2 . ASP A 186 ? 0.46473 0.47652 0.47141 0.10273  -0.06644 0.11031  193 ASP A OD2 
1375 N N   . GLN A 187 ? 0.27233 0.19538 0.23882 0.03788  -0.02443 0.07372  194 GLN A N   
1376 C CA  . GLN A 187 ? 0.27013 0.21537 0.22838 0.02361  -0.02215 0.06027  194 GLN A CA  
1377 C C   . GLN A 187 ? 0.28874 0.21576 0.24290 0.00885  -0.01708 0.05202  194 GLN A C   
1378 O O   . GLN A 187 ? 0.28379 0.22219 0.23422 0.00275  -0.01554 0.03742  194 GLN A O   
1379 C CB  . GLN A 187 ? 0.28707 0.25113 0.25557 0.02956  -0.01931 0.04521  194 GLN A CB  
1380 C CG  . GLN A 187 ? 0.24279 0.23566 0.22930 0.04074  -0.02505 0.05035  194 GLN A CG  
1381 C CD  . GLN A 187 ? 0.26818 0.28719 0.24833 0.03459  -0.03634 0.05600  194 GLN A CD  
1382 O OE1 . GLN A 187 ? 0.29013 0.31354 0.25632 0.02130  -0.03512 0.04991  194 GLN A OE1 
1383 N NE2 . GLN A 187 ? 0.32184 0.36015 0.31150 0.04703  -0.04883 0.06528  194 GLN A NE2 
1384 N N   . THR A 188 ? 0.30239 0.20232 0.26116 0.00283  -0.01484 0.06262  195 THR A N   
1385 C CA  . THR A 188 ? 0.31626 0.20410 0.28383 -0.01345 -0.01218 0.05152  195 THR A CA  
1386 C C   . THR A 188 ? 0.28725 0.20191 0.25044 -0.02735 -0.00811 0.05535  195 THR A C   
1387 O O   . THR A 188 ? 0.33740 0.25333 0.31484 -0.04064 -0.00704 0.04512  195 THR A O   
1388 C CB  . THR A 188 ? 0.36747 0.21500 0.35298 -0.01943 -0.00925 0.06048  195 THR A CB  
1389 O OG1 . THR A 188 ? 0.41193 0.25524 0.39211 -0.02018 -0.00263 0.09270  195 THR A OG1 
1390 C CG2 . THR A 188 ? 0.40161 0.21721 0.39384 -0.00295 -0.01307 0.04949  195 THR A CG2 
1391 N N   . GLU A 189 ? 0.32943 0.26788 0.27569 -0.02340 -0.00685 0.06714  196 GLU A N   
1392 C CA  . GLU A 189 ? 0.31551 0.28003 0.25547 -0.03235 -0.00142 0.06604  196 GLU A CA  
1393 C C   . GLU A 189 ? 0.32387 0.30140 0.26996 -0.03436 -0.00473 0.04358  196 GLU A C   
1394 O O   . GLU A 189 ? 0.26673 0.26129 0.21912 -0.04179 -0.00037 0.03909  196 GLU A O   
1395 C CB  . GLU A 189 ? 0.27150 0.25814 0.18730 -0.02422 -0.00301 0.07407  196 GLU A CB  
1396 C CG  . GLU A 189 ? 0.24926 0.24974 0.16268 -0.01589 -0.01284 0.05816  196 GLU A CG  
1397 C CD  . GLU A 189 ? 0.29299 0.31393 0.18767 -0.00818 -0.02026 0.06279  196 GLU A CD  
1398 O OE1 . GLU A 189 ? 0.39690 0.41515 0.28716 0.00167  -0.02713 0.07690  196 GLU A OE1 
1399 O OE2 . GLU A 189 ? 0.32156 0.36138 0.20537 -0.00994 -0.02105 0.05092  196 GLU A OE2 
1400 N N   . TYR A 190 ? 0.23319 0.20452 0.17756 -0.02557 -0.01081 0.03159  197 TYR A N   
1401 C CA  . TYR A 190 ? 0.22625 0.20654 0.16925 -0.02348 -0.01322 0.01589  197 TYR A CA  
1402 C C   . TYR A 190 ? 0.30071 0.27326 0.25392 -0.02756 -0.01825 0.00328  197 TYR A C   
1403 O O   . TYR A 190 ? 0.28552 0.26484 0.23208 -0.02146 -0.02308 -0.00860 197 TYR A O   
1404 C CB  . TYR A 190 ? 0.22456 0.20376 0.15972 -0.01233 -0.01329 0.01250  197 TYR A CB  
1405 C CG  . TYR A 190 ? 0.22301 0.21570 0.15762 -0.01145 -0.01276 0.01949  197 TYR A CG  
1406 C CD1 . TYR A 190 ? 0.22307 0.23014 0.15392 -0.01540 -0.01231 0.01631  197 TYR A CD1 
1407 C CD2 . TYR A 190 ? 0.22819 0.22121 0.16829 -0.00521 -0.01492 0.02615  197 TYR A CD2 
1408 C CE1 . TYR A 190 ? 0.23881 0.25872 0.16854 -0.01515 -0.01585 0.01616  197 TYR A CE1 
1409 C CE2 . TYR A 190 ? 0.21517 0.22694 0.15799 -0.00451 -0.01996 0.02855  197 TYR A CE2 
1410 C CZ  . TYR A 190 ? 0.27794 0.30231 0.21417 -0.01055 -0.02135 0.02178  197 TYR A CZ  
1411 O OH  . TYR A 190 ? 0.25324 0.29639 0.19136 -0.01020 -0.03017 0.01760  197 TYR A OH  
1412 N N   . LEU A 191 ? 0.29139 0.24953 0.26155 -0.03759 -0.01822 0.00587  198 LEU A N   
1413 C CA  . LEU A 191 ? 0.27195 0.22882 0.26318 -0.04738 -0.02545 -0.00942 198 LEU A CA  
1414 C C   . LEU A 191 ? 0.25893 0.23913 0.27586 -0.06289 -0.01968 -0.00335 198 LEU A C   
1415 O O   . LEU A 191 ? 0.28542 0.27492 0.33045 -0.07320 -0.02714 -0.01760 198 LEU A O   
1416 C CB  . LEU A 191 ? 0.31734 0.23912 0.32209 -0.05169 -0.02855 -0.01454 198 LEU A CB  
1417 C CG  . LEU A 191 ? 0.34235 0.24234 0.32558 -0.03361 -0.03142 -0.02296 198 LEU A CG  
1418 C CD1 . LEU A 191 ? 0.36390 0.22371 0.36292 -0.03544 -0.03225 -0.02643 198 LEU A CD1 
1419 C CD2 . LEU A 191 ? 0.37900 0.29016 0.34251 -0.02220 -0.04114 -0.04646 198 LEU A CD2 
1420 N N   . GLU A 192 ? 0.24895 0.24212 0.25845 -0.06412 -0.00667 0.01566  199 GLU A N   
1421 C CA  . GLU A 192 ? 0.28705 0.30614 0.31871 -0.07644 0.00499  0.02364  199 GLU A CA  
1422 C C   . GLU A 192 ? 0.22472 0.27780 0.25908 -0.06938 0.00188  0.01014  199 GLU A C   
1423 O O   . GLU A 192 ? 0.25823 0.31378 0.26554 -0.05502 -0.00013 0.00733  199 GLU A O   
1424 C CB  . GLU A 192 ? 0.28622 0.30611 0.29804 -0.07569 0.02109  0.04870  199 GLU A CB  
1425 C CG  . GLU A 192 ? 0.40892 0.39637 0.42320 -0.08202 0.02731  0.07001  199 GLU A CG  
1426 C CD  . GLU A 192 ? 0.59358 0.58393 0.57455 -0.07393 0.03882  0.09617  199 GLU A CD  
1427 O OE1 . GLU A 192 ? 0.54201 0.56355 0.50792 -0.07121 0.04864  0.09859  199 GLU A OE1 
1428 O OE2 . GLU A 192 ? 0.58547 0.54779 0.55318 -0.06735 0.03687  0.11306  199 GLU A OE2 
1429 N N   . GLU A 193 ? 0.26713 0.34669 0.34016 -0.07963 0.00187  0.00229  200 GLU A N   
1430 C CA  . GLU A 193 ? 0.20007 0.31391 0.28196 -0.06923 -0.00269 -0.01027 200 GLU A CA  
1431 C C   . GLU A 193 ? 0.17360 0.29990 0.23190 -0.05798 0.01198  -0.00216 200 GLU A C   
1432 O O   . GLU A 193 ? 0.18381 0.31037 0.22335 -0.04145 0.00584  -0.01052 200 GLU A O   
1433 C CB  . GLU A 193 ? 0.21262 0.36248 0.35061 -0.08319 -0.00290 -0.01798 200 GLU A CB  
1434 C CG  . GLU A 193 ? 0.25043 0.43880 0.40409 -0.06821 -0.01240 -0.03249 200 GLU A CG  
1435 C CD  . GLU A 193 ? 0.36361 0.59663 0.58322 -0.08130 -0.01796 -0.04407 200 GLU A CD  
1436 O OE1 . GLU A 193 ? 0.30035 0.53731 0.56025 -0.10658 -0.00739 -0.03805 200 GLU A OE1 
1437 O OE2 . GLU A 193 ? 0.44052 0.70567 0.67567 -0.06581 -0.03333 -0.05832 200 GLU A OE2 
1438 N N   . ARG A 194 ? 0.22459 0.35910 0.28174 -0.06586 0.03199  0.01388  201 ARG A N   
1439 C CA  . ARG A 194 ? 0.23089 0.38021 0.26219 -0.05339 0.04459  0.01529  201 ARG A CA  
1440 C C   . ARG A 194 ? 0.22932 0.35169 0.21788 -0.04124 0.03512  0.01211  201 ARG A C   
1441 O O   . ARG A 194 ? 0.22099 0.34908 0.19398 -0.02844 0.03567  0.00123  201 ARG A O   
1442 C CB  . ARG A 194 ? 0.23545 0.40045 0.26407 -0.06164 0.06928  0.03490  201 ARG A CB  
1443 C CG  . ARG A 194 ? 0.35943 0.49434 0.36925 -0.07067 0.07230  0.05733  201 ARG A CG  
1444 C CD  . ARG A 194 ? 0.38128 0.53107 0.38724 -0.07648 0.09970  0.08145  201 ARG A CD  
1445 N NE  . ARG A 194 ? 0.49832 0.61039 0.47485 -0.07534 0.10005  0.10276  201 ARG A NE  
1446 C CZ  . ARG A 194 ? 0.44927 0.55334 0.40324 -0.07244 0.11733  0.12056  201 ARG A CZ  
1447 N NH1 . ARG A 194 ? 0.48482 0.61497 0.44254 -0.07248 0.13858  0.12077  201 ARG A NH1 
1448 N NH2 . ARG A 194 ? 0.58688 0.65741 0.51309 -0.06905 0.11305  0.13857  201 ARG A NH2 
1449 N N   . ARG A 195 ? 0.23102 0.32456 0.20613 -0.04499 0.02659  0.01969  202 ARG A N   
1450 C CA  . ARG A 195 ? 0.21244 0.28813 0.15882 -0.03532 0.01776  0.01614  202 ARG A CA  
1451 C C   . ARG A 195 ? 0.24152 0.30937 0.19140 -0.02678 0.00723  0.00171  202 ARG A C   
1452 O O   . ARG A 195 ? 0.20575 0.26938 0.14332 -0.01895 0.00554  -0.00573 202 ARG A O   
1453 C CB  . ARG A 195 ? 0.24792 0.30055 0.18562 -0.03857 0.01289  0.02889  202 ARG A CB  
1454 C CG  . ARG A 195 ? 0.23850 0.28107 0.15829 -0.02991 0.00346  0.02523  202 ARG A CG  
1455 C CD  . ARG A 195 ? 0.27037 0.32742 0.16679 -0.02484 0.00462  0.02513  202 ARG A CD  
1456 N NE  . ARG A 195 ? 0.27408 0.32669 0.16314 -0.01962 -0.00736 0.02242  202 ARG A NE  
1457 C CZ  . ARG A 195 ? 0.27763 0.33709 0.16378 -0.01653 -0.01422 0.00614  202 ARG A CZ  
1458 N NH1 . ARG A 195 ? 0.24692 0.31235 0.13041 -0.01522 -0.00991 -0.00905 202 ARG A NH1 
1459 N NH2 . ARG A 195 ? 0.28638 0.34688 0.17828 -0.01470 -0.02571 0.00356  202 ARG A NH2 
1460 N N   . ILE A 196 ? 0.20591 0.27010 0.17157 -0.02781 -0.00021 -0.00227 203 ILE A N   
1461 C CA  . ILE A 196 ? 0.18839 0.24545 0.14978 -0.01617 -0.00854 -0.01060 203 ILE A CA  
1462 C C   . ILE A 196 ? 0.21827 0.29100 0.18659 -0.00620 -0.00566 -0.01750 203 ILE A C   
1463 O O   . ILE A 196 ? 0.21617 0.27488 0.17410 0.00404  -0.00618 -0.01979 203 ILE A O   
1464 C CB  . ILE A 196 ? 0.19283 0.24701 0.16161 -0.01581 -0.01978 -0.01582 203 ILE A CB  
1465 C CG1 . ILE A 196 ? 0.20223 0.23450 0.16304 -0.02165 -0.02138 -0.01243 203 ILE A CG1 
1466 C CG2 . ILE A 196 ? 0.21084 0.25977 0.16594 0.00060  -0.02703 -0.01953 203 ILE A CG2 
1467 C CD1 . ILE A 196 ? 0.23816 0.26838 0.21252 -0.02658 -0.03208 -0.02306 203 ILE A CD1 
1468 N N   . LYS A 197 ? 0.15748 0.25870 0.14829 -0.00865 -0.00079 -0.02042 204 LYS A N   
1469 C CA  . LYS A 197 ? 0.19554 0.31437 0.19626 0.00463  0.00395  -0.02846 204 LYS A CA  
1470 C C   . LYS A 197 ? 0.16733 0.27250 0.14632 0.01017  0.01221  -0.03279 204 LYS A C   
1471 O O   . LYS A 197 ? 0.19946 0.29325 0.17703 0.02417  0.01114  -0.04075 204 LYS A O   
1472 C CB  . LYS A 197 ? 0.18504 0.34445 0.21848 -0.00002 0.01349  -0.03019 204 LYS A CB  
1473 C CG  . LYS A 197 ? 0.21782 0.39838 0.28638 -0.00730 0.00220  -0.03232 204 LYS A CG  
1474 C CD  . LYS A 197 ? 0.26592 0.49509 0.37888 -0.00724 0.01239  -0.03671 204 LYS A CD  
1475 C CE  . LYS A 197 ? 0.28529 0.54062 0.44491 -0.02562 0.00550  -0.03854 204 LYS A CE  
1476 N NZ  . LYS A 197 ? 0.39014 0.69662 0.60105 -0.03358 0.02425  -0.03749 204 LYS A NZ  
1477 N N   . GLU A 198 ? 0.17815 0.28336 0.14047 0.00048  0.01919  -0.02853 205 GLU A N   
1478 C CA  . GLU A 198 ? 0.19531 0.29232 0.13527 0.00554  0.02239  -0.03821 205 GLU A CA  
1479 C C   . GLU A 198 ? 0.19000 0.25551 0.12521 0.00802  0.01216  -0.04312 205 GLU A C   
1480 O O   . GLU A 198 ? 0.23465 0.28781 0.16895 0.01599  0.01246  -0.05732 205 GLU A O   
1481 C CB  . GLU A 198 ? 0.21634 0.32091 0.13397 -0.00292 0.02693  -0.02947 205 GLU A CB  
1482 C CG  . GLU A 198 ? 0.25715 0.35699 0.14683 0.00176  0.02342  -0.04201 205 GLU A CG  
1483 C CD  . GLU A 198 ? 0.25731 0.35905 0.12651 -0.00259 0.02239  -0.02687 205 GLU A CD  
1484 O OE1 . GLU A 198 ? 0.25082 0.34446 0.12301 -0.01002 0.01694  -0.01112 205 GLU A OE1 
1485 O OE2 . GLU A 198 ? 0.27137 0.37993 0.12054 0.00375  0.02695  -0.03042 205 GLU A OE2 
1486 N N   . ILE A 199 ? 0.20169 0.25298 0.13734 0.00129  0.00521  -0.03189 206 ILE A N   
1487 C CA  . ILE A 199 ? 0.21839 0.24456 0.15397 0.00114  0.00062  -0.03226 206 ILE A CA  
1488 C C   . ILE A 199 ? 0.20583 0.21504 0.14999 0.01241  0.00159  -0.03219 206 ILE A C   
1489 O O   . ILE A 199 ? 0.22987 0.21615 0.17911 0.01391  0.00322  -0.03619 206 ILE A O   
1490 C CB  . ILE A 199 ? 0.19514 0.21576 0.12879 -0.00569 -0.00299 -0.01987 206 ILE A CB  
1491 C CG1 . ILE A 199 ? 0.26504 0.29698 0.19051 -0.01295 -0.00523 -0.01682 206 ILE A CG1 
1492 C CG2 . ILE A 199 ? 0.24295 0.24349 0.18264 -0.00542 -0.00221 -0.01663 206 ILE A CG2 
1493 C CD1 . ILE A 199 ? 0.26298 0.28942 0.18983 -0.01586 -0.00750 -0.00488 206 ILE A CD1 
1494 N N   . VAL A 200 ? 0.22469 0.24403 0.17286 0.02060  -0.00052 -0.02685 207 VAL A N   
1495 C CA  . VAL A 200 ? 0.21679 0.22240 0.16841 0.03691  -0.00190 -0.02322 207 VAL A CA  
1496 C C   . VAL A 200 ? 0.21514 0.21495 0.17689 0.04732  0.00309  -0.03552 207 VAL A C   
1497 O O   . VAL A 200 ? 0.27362 0.24209 0.23806 0.05589  0.00571  -0.03369 207 VAL A O   
1498 C CB  . VAL A 200 ? 0.22446 0.25168 0.17954 0.04553  -0.01086 -0.01925 207 VAL A CB  
1499 C CG1 . VAL A 200 ? 0.21747 0.23691 0.17459 0.06831  -0.01494 -0.01472 207 VAL A CG1 
1500 C CG2 . VAL A 200 ? 0.21903 0.24208 0.15930 0.03948  -0.01667 -0.01152 207 VAL A CG2 
1501 N N   . LYS A 201 ? 0.22201 0.24957 0.18994 0.04715  0.00700  -0.04801 208 LYS A N   
1502 C CA  . LYS A 201 ? 0.23898 0.26398 0.21404 0.06007  0.01355  -0.06471 208 LYS A CA  
1503 C C   . LYS A 201 ? 0.25392 0.24680 0.22111 0.05401  0.01473  -0.07775 208 LYS A C   
1504 O O   . LYS A 201 ? 0.34575 0.31120 0.32184 0.06561  0.01704  -0.08912 208 LYS A O   
1505 C CB  . LYS A 201 ? 0.23618 0.30322 0.21520 0.06014  0.02220  -0.07401 208 LYS A CB  
1506 C CG  . LYS A 201 ? 0.29962 0.36976 0.28298 0.07731  0.03194  -0.09520 208 LYS A CG  
1507 C CD  . LYS A 201 ? 0.39333 0.50808 0.37371 0.07621  0.04640  -0.10181 208 LYS A CD  
1508 C CE  . LYS A 201 ? 0.52781 0.64357 0.50581 0.09403  0.05751  -0.12455 208 LYS A CE  
1509 N NZ  . LYS A 201 ? 0.56706 0.64235 0.51996 0.09000  0.05131  -0.14077 208 LYS A NZ  
1510 N N   . LYS A 202 ? 0.27938 0.27418 0.23454 0.03629  0.01136  -0.07712 209 LYS A N   
1511 C CA  . LYS A 202 ? 0.28591 0.26060 0.23957 0.02807  0.00789  -0.09407 209 LYS A CA  
1512 C C   . LYS A 202 ? 0.28705 0.22183 0.25955 0.02379  0.00726  -0.08667 209 LYS A C   
1513 O O   . LYS A 202 ? 0.33971 0.24598 0.32594 0.02294  0.00703  -0.10398 209 LYS A O   
1514 C CB  . LYS A 202 ? 0.29132 0.28773 0.22943 0.01358  0.00174  -0.09285 209 LYS A CB  
1515 C CG  . LYS A 202 ? 0.33762 0.32606 0.27574 0.00465  -0.00789 -0.11375 209 LYS A CG  
1516 C CD  . LYS A 202 ? 0.34102 0.35580 0.26313 -0.00443 -0.01653 -0.10671 209 LYS A CD  
1517 C CE  . LYS A 202 ? 0.51271 0.53055 0.43371 -0.01034 -0.03112 -0.12960 209 LYS A CE  
1518 N NZ  . LYS A 202 ? 0.53836 0.58179 0.44046 -0.01191 -0.03992 -0.11633 209 LYS A NZ  
1519 N N   . HIS A 203 ? 0.27483 0.20573 0.24861 0.02092  0.00863  -0.06151 210 HIS A N   
1520 C CA  . HIS A 203 ? 0.33850 0.23798 0.32773 0.01374  0.01311  -0.04878 210 HIS A CA  
1521 C C   . HIS A 203 ? 0.33066 0.20647 0.31775 0.02895  0.02042  -0.02521 210 HIS A C   
1522 O O   . HIS A 203 ? 0.35248 0.19600 0.35248 0.02516  0.02944  -0.01131 210 HIS A O   
1523 C CB  . HIS A 203 ? 0.32288 0.23889 0.31185 -0.00118 0.01165  -0.03808 210 HIS A CB  
1524 C CG  . HIS A 203 ? 0.32680 0.26309 0.32003 -0.01446 0.00208  -0.05692 210 HIS A CG  
1525 N ND1 . HIS A 203 ? 0.35208 0.27670 0.36540 -0.02375 -0.00309 -0.07902 210 HIS A ND1 
1526 C CD2 . HIS A 203 ? 0.31454 0.28136 0.29349 -0.01823 -0.00522 -0.05693 210 HIS A CD2 
1527 C CE1 . HIS A 203 ? 0.39257 0.34534 0.40034 -0.03120 -0.01559 -0.09268 210 HIS A CE1 
1528 N NE2 . HIS A 203 ? 0.30897 0.28599 0.29468 -0.02687 -0.01582 -0.07670 210 HIS A NE2 
1529 N N   . SER A 204 ? 0.31674 0.31755 0.20269 -0.02797 -0.07089 -0.07364 211 SER A N   
1530 C CA  . SER A 204 ? 0.26358 0.26919 0.18868 -0.01976 -0.05466 -0.07006 211 SER A CA  
1531 C C   . SER A 204 ? 0.32174 0.30822 0.23649 -0.01381 -0.03164 -0.07941 211 SER A C   
1532 O O   . SER A 204 ? 0.32285 0.31567 0.26065 -0.00389 -0.01927 -0.07151 211 SER A O   
1533 C CB  . SER A 204 ? 0.23150 0.25912 0.18299 -0.00969 -0.05366 -0.05224 211 SER A CB  
1534 O OG  . SER A 204 ? 0.26220 0.30896 0.23074 -0.01256 -0.07309 -0.04451 211 SER A OG  
1535 N N   . GLN A 205 ? 0.34934 0.31291 0.23174 -0.01991 -0.02580 -0.09752 212 GLN A N   
1536 C CA  . GLN A 205 ? 0.42184 0.37037 0.29906 -0.01218 -0.00063 -0.10760 212 GLN A CA  
1537 C C   . GLN A 205 ? 0.35972 0.30024 0.27717 -0.00513 0.00887  -0.11026 212 GLN A C   
1538 O O   . GLN A 205 ? 0.41984 0.35821 0.35294 0.00594  0.02690  -0.11141 212 GLN A O   
1539 C CB  . GLN A 205 ? 0.54391 0.46978 0.37900 -0.01702 0.00554  -0.12243 212 GLN A CB  
1540 C CG  . GLN A 205 ? 0.53301 0.44223 0.35972 -0.02743 -0.00843 -0.13580 212 GLN A CG  
1541 C CD  . GLN A 205 ? 0.66999 0.59028 0.47336 -0.03793 -0.03526 -0.13176 212 GLN A CD  
1542 O OE1 . GLN A 205 ? 0.51741 0.45648 0.34274 -0.04267 -0.05497 -0.12111 212 GLN A OE1 
1543 N NE2 . GLN A 205 ? 0.63542 0.54824 0.39947 -0.04141 -0.03570 -0.13989 212 GLN A NE2 
1544 N N   . PHE A 206 ? 0.37357 0.31004 0.31113 -0.01162 -0.00332 -0.10944 213 PHE A N   
1545 C CA  . PHE A 206 ? 0.34963 0.27044 0.31949 -0.00659 0.00433  -0.11001 213 PHE A CA  
1546 C C   . PHE A 206 ? 0.33112 0.26934 0.33354 -0.00344 -0.00224 -0.08775 213 PHE A C   
1547 O O   . PHE A 206 ? 0.32859 0.25286 0.35406 -0.00300 -0.00108 -0.08292 213 PHE A O   
1548 C CB  . PHE A 206 ? 0.33726 0.22932 0.30117 -0.01897 0.00031  -0.12843 213 PHE A CB  
1549 C CG  . PHE A 206 ? 0.35469 0.22453 0.28298 -0.01967 0.01037  -0.14767 213 PHE A CG  
1550 C CD1 . PHE A 206 ? 0.41494 0.27820 0.34823 -0.00460 0.03103  -0.14980 213 PHE A CD1 
1551 C CD2 . PHE A 206 ? 0.47194 0.33347 0.36440 -0.03344 -0.00347 -0.15793 213 PHE A CD2 
1552 C CE1 . PHE A 206 ? 0.41063 0.25929 0.31439 -0.00389 0.04115  -0.16446 213 PHE A CE1 
1553 C CE2 . PHE A 206 ? 0.52473 0.36899 0.38323 -0.03188 0.00452  -0.17280 213 PHE A CE2 
1554 C CZ  . PHE A 206 ? 0.49504 0.33274 0.35888 -0.01754 0.02882  -0.17698 213 PHE A CZ  
1555 N N   . ILE A 207 ? 0.26189 0.22708 0.26390 -0.00148 -0.00777 -0.07399 214 ILE A N   
1556 C CA  . ILE A 207 ? 0.22648 0.20641 0.25173 0.00030  -0.01059 -0.05608 214 ILE A CA  
1557 C C   . ILE A 207 ? 0.21312 0.18651 0.25393 0.01159  -0.00238 -0.04820 214 ILE A C   
1558 O O   . ILE A 207 ? 0.24532 0.22061 0.28533 0.02121  0.00541  -0.05163 214 ILE A O   
1559 C CB  . ILE A 207 ? 0.21365 0.21993 0.23498 0.00157  -0.01542 -0.04715 214 ILE A CB  
1560 C CG1 . ILE A 207 ? 0.28906 0.30394 0.30526 -0.00838 -0.02823 -0.05153 214 ILE A CG1 
1561 C CG2 . ILE A 207 ? 0.23676 0.25593 0.27475 0.00400  -0.01349 -0.03230 214 ILE A CG2 
1562 C CD1 . ILE A 207 ? 0.27509 0.29700 0.31614 -0.01882 -0.03396 -0.04773 214 ILE A CD1 
1563 N N   . GLY A 208 ? 0.23265 0.19936 0.28923 0.00956  -0.00483 -0.03599 215 GLY A N   
1564 C CA  . GLY A 208 ? 0.22950 0.18572 0.30193 0.01962  -0.00275 -0.02582 215 GLY A CA  
1565 C C   . GLY A 208 ? 0.23913 0.21578 0.31319 0.02604  -0.00591 -0.01107 215 GLY A C   
1566 O O   . GLY A 208 ? 0.23224 0.20283 0.31581 0.02987  -0.01088 0.00390  215 GLY A O   
1567 N N   . TYR A 209 ? 0.22755 0.22565 0.29072 0.02629  -0.00483 -0.01466 216 TYR A N   
1568 C CA  . TYR A 209 ? 0.26026 0.27648 0.32212 0.02935  -0.00796 -0.00505 216 TYR A CA  
1569 C C   . TYR A 209 ? 0.23651 0.26534 0.29545 0.03322  -0.00288 -0.01412 216 TYR A C   
1570 O O   . TYR A 209 ? 0.26520 0.29169 0.31267 0.03055  0.00137  -0.02436 216 TYR A O   
1571 C CB  . TYR A 209 ? 0.19328 0.21949 0.24237 0.02057  -0.00996 0.00219  216 TYR A CB  
1572 C CG  . TYR A 209 ? 0.20939 0.22322 0.25780 0.01343  -0.01133 0.01333  216 TYR A CG  
1573 C CD1 . TYR A 209 ? 0.21695 0.22358 0.26191 0.01483  -0.01720 0.02885  216 TYR A CD1 
1574 C CD2 . TYR A 209 ? 0.19850 0.20658 0.25044 0.00391  -0.00825 0.00976  216 TYR A CD2 
1575 C CE1 . TYR A 209 ? 0.23209 0.22272 0.27174 0.00681  -0.01749 0.04241  216 TYR A CE1 
1576 C CE2 . TYR A 209 ? 0.21486 0.20945 0.26816 -0.00521 -0.00693 0.02113  216 TYR A CE2 
1577 C CZ  . TYR A 209 ? 0.20804 0.19195 0.25271 -0.00364 -0.01034 0.03834  216 TYR A CZ  
1578 O OH  . TYR A 209 ? 0.26142 0.22800 0.30223 -0.01410 -0.00820 0.05320  216 TYR A OH  
1579 N N   . PRO A 210 ? 0.20787 0.24918 0.27569 0.03781  -0.00429 -0.00975 217 PRO A N   
1580 C CA  . PRO A 210 ? 0.20365 0.25553 0.27049 0.03892  0.00266  -0.01665 217 PRO A CA  
1581 C C   . PRO A 210 ? 0.22881 0.28526 0.27604 0.03282  0.00217  -0.01741 217 PRO A C   
1582 O O   . PRO A 210 ? 0.21009 0.27137 0.25252 0.02950  -0.00294 -0.01220 217 PRO A O   
1583 C CB  . PRO A 210 ? 0.25425 0.32017 0.34125 0.04238  -0.00218 -0.01043 217 PRO A CB  
1584 C CG  . PRO A 210 ? 0.26313 0.32696 0.34674 0.04064  -0.01519 0.00131  217 PRO A CG  
1585 C CD  . PRO A 210 ? 0.19853 0.24430 0.27702 0.04033  -0.01416 0.00281  217 PRO A CD  
1586 N N   . ILE A 211 ? 0.22580 0.27903 0.26088 0.03168  0.00817  -0.02378 218 ILE A N   
1587 C CA  . ILE A 211 ? 0.18798 0.24337 0.20872 0.02839  0.00613  -0.02224 218 ILE A CA  
1588 C C   . ILE A 211 ? 0.17019 0.22832 0.19017 0.02823  0.01339  -0.02154 218 ILE A C   
1589 O O   . ILE A 211 ? 0.22005 0.27375 0.23300 0.02778  0.02302  -0.02556 218 ILE A O   
1590 C CB  . ILE A 211 ? 0.18289 0.23031 0.18636 0.02530  0.00262  -0.02613 218 ILE A CB  
1591 C CG1 . ILE A 211 ? 0.16285 0.20820 0.17332 0.02247  -0.00382 -0.02759 218 ILE A CG1 
1592 C CG2 . ILE A 211 ? 0.24193 0.29163 0.23557 0.02438  -0.00278 -0.02083 218 ILE A CG2 
1593 C CD1 . ILE A 211 ? 0.19455 0.23237 0.19031 0.01669  -0.01061 -0.03431 218 ILE A CD1 
1594 N N   . THR A 212 ? 0.18789 0.25172 0.21435 0.02699  0.01102  -0.01766 219 THR A N   
1595 C CA  . THR A 212 ? 0.18650 0.25102 0.21580 0.02404  0.01759  -0.01641 219 THR A CA  
1596 C C   . THR A 212 ? 0.17998 0.23418 0.19428 0.02268  0.01616  -0.01193 219 THR A C   
1597 O O   . THR A 212 ? 0.16387 0.21722 0.18113 0.02425  0.01010  -0.01114 219 THR A O   
1598 C CB  . THR A 212 ? 0.19521 0.26960 0.24298 0.02159  0.01409  -0.01660 219 THR A CB  
1599 O OG1 . THR A 212 ? 0.17699 0.26100 0.24102 0.02468  0.01019  -0.01691 219 THR A OG1 
1600 C CG2 . THR A 212 ? 0.18285 0.25914 0.24064 0.01581  0.02207  -0.01624 219 THR A CG2 
1601 N N   . LEU A 213 ? 0.18751 0.23271 0.18588 0.02003  0.02271  -0.00847 220 LEU A N   
1602 C CA  . LEU A 213 ? 0.20870 0.24049 0.19303 0.01913  0.01938  0.00035  220 LEU A CA  
1603 C C   . LEU A 213 ? 0.17861 0.20567 0.17443 0.01405  0.02666  0.00328  220 LEU A C   
1604 O O   . LEU A 213 ? 0.21952 0.24645 0.21462 0.00753  0.03898  0.00442  220 LEU A O   
1605 C CB  . LEU A 213 ? 0.25052 0.27090 0.20263 0.01633  0.02083  0.00536  220 LEU A CB  
1606 C CG  . LEU A 213 ? 0.28160 0.28466 0.21532 0.01524  0.01478  0.01979  220 LEU A CG  
1607 C CD1 . LEU A 213 ? 0.23224 0.23650 0.18384 0.02362  -0.00155 0.02376  220 LEU A CD1 
1608 C CD2 . LEU A 213 ? 0.31394 0.30539 0.20539 0.01051  0.01293  0.02501  220 LEU A CD2 
1609 N N   . PHE A 214 ? 0.15430 0.17682 0.16242 0.01594  0.02102  0.00293  221 PHE A N   
1610 C CA  . PHE A 214 ? 0.20089 0.21396 0.21989 0.00923  0.02653  0.00359  221 PHE A CA  
1611 C C   . PHE A 214 ? 0.24100 0.23251 0.24427 0.00582  0.03111  0.01737  221 PHE A C   
1612 O O   . PHE A 214 ? 0.26922 0.25075 0.25381 0.01141  0.02406  0.02706  221 PHE A O   
1613 C CB  . PHE A 214 ? 0.17606 0.18334 0.20732 0.01196  0.02138  -0.00340 221 PHE A CB  
1614 C CG  . PHE A 214 ? 0.18295 0.20663 0.22260 0.01026  0.01819  -0.01569 221 PHE A CG  
1615 C CD1 . PHE A 214 ? 0.19447 0.23579 0.23232 0.01278  0.01500  -0.01683 221 PHE A CD1 
1616 C CD2 . PHE A 214 ? 0.20471 0.22185 0.25006 0.00558  0.01761  -0.02575 221 PHE A CD2 
1617 C CE1 . PHE A 214 ? 0.14156 0.19406 0.18215 0.01091  0.00971  -0.02364 221 PHE A CE1 
1618 C CE2 . PHE A 214 ? 0.18307 0.21277 0.22601 0.00212  0.01247  -0.03545 221 PHE A CE2 
1619 C CZ  . PHE A 214 ? 0.12421 0.17175 0.16430 0.00497  0.00774  -0.03221 221 PHE A CZ  
1620 N N   . VAL A 215 ? 0.24698 0.23166 0.25816 -0.00491 0.04162  0.01959  222 VAL A N   
1621 C CA  . VAL A 215 ? 0.25242 0.21216 0.24885 -0.01178 0.04875  0.03507  222 VAL A CA  
1622 C C   . VAL A 215 ? 0.31395 0.25024 0.32533 -0.01172 0.04434  0.03675  222 VAL A C   
1623 O O   . VAL A 215 ? 0.28069 0.22244 0.31466 -0.01303 0.04222  0.02210  222 VAL A O   
1624 C CB  . VAL A 215 ? 0.27168 0.23900 0.27259 -0.02613 0.06765  0.03607  222 VAL A CB  
1625 C CG1 . VAL A 215 ? 0.37456 0.31296 0.35857 -0.03714 0.07842  0.05418  222 VAL A CG1 
1626 C CG2 . VAL A 215 ? 0.36271 0.34959 0.35072 -0.02416 0.07559  0.03148  222 VAL A CG2 
1627 N N   . GLU A 216 ? 0.36562 0.27243 0.36221 -0.01067 0.04264  0.05460  223 GLU A N   
1628 C CA  . GLU A 216 ? 0.39756 0.27552 0.41161 -0.00914 0.03996  0.05663  223 GLU A CA  
1629 C C   . GLU A 216 ? 0.45640 0.31708 0.48096 -0.02724 0.05346  0.05871  223 GLU A C   
1630 O O   . GLU A 216 ? 0.43340 0.29634 0.44543 -0.04030 0.06601  0.06876  223 GLU A O   
1631 C CB  . GLU A 216 ? 0.46795 0.31985 0.46838 0.00248  0.02846  0.07761  223 GLU A CB  
1632 C CG  . GLU A 216 ? 0.45702 0.32752 0.46339 0.01986  0.01362  0.07214  223 GLU A CG  
1633 C CD  . GLU A 216 ? 0.44833 0.29555 0.46983 0.03493  0.00085  0.08468  223 GLU A CD  
1634 O OE1 . GLU A 216 ? 0.49918 0.32457 0.54712 0.03775  0.00585  0.07815  223 GLU A OE1 
1635 O OE2 . GLU A 216 ? 0.60899 0.45899 0.61786 0.04385  -0.01506 0.10046  223 GLU A OE2 
1636 N N   . LYS A 217 ? 0.44851 0.29022 0.49687 -0.02913 0.05261  0.04804  224 LYS A N   
1637 C CA  . LYS A 217 ? 0.46159 0.28577 0.52621 -0.04882 0.06341  0.04645  224 LYS A CA  
1638 C C   . LYS A 217 ? 0.54889 0.32560 0.60605 -0.05260 0.06763  0.07029  224 LYS A C   
1639 O O   . LYS A 217 ? 0.73584 0.48195 0.79650 -0.03879 0.05917  0.07601  224 LYS A O   
1640 C CB  . LYS A 217 ? 0.45082 0.27474 0.54044 -0.05279 0.05973  0.01965  224 LYS A CB  
1641 C CG  . LYS A 217 ? 0.41034 0.27086 0.49922 -0.04368 0.05110  -0.00003 224 LYS A CG  
1642 C CD  . LYS A 217 ? 0.37662 0.23663 0.47902 -0.05243 0.04741  -0.02651 224 LYS A CD  
1643 C CE  . LYS A 217 ? 0.39313 0.22575 0.49472 -0.03925 0.04651  -0.03853 224 LYS A CE  
1644 N NZ  . LYS A 217 ? 0.38011 0.23437 0.47113 -0.02006 0.04226  -0.03995 224 LYS A NZ  
# 
