data_7HAT
# 
_entry.id   7HAT 
# 
_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   7HAT         pdb_00007hat 10.2210/pdb7hat/pdb 
WWPDB D_1001407240 ?            ?                   
# 
_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                        7HAT 
_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 '(furan-2-yl)(thiomorpholin-4-yl)methanone' 197.254   1   ?        ? ? ? 
3 water       nat water                                       18.015    182 ?        ? ? ? 
# 
_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 '(furan-2-yl)(thiomorpholin-4-yl)methanone' A1AY5 
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 
A1AY5 non-polymer         . '(furan-2-yl)(thiomorpholin-4-yl)methanone' ? 'C9 H11 N O2 S'  197.254 
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        A1AY5 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1AY5 
_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 A1AY5 1   301 301 A1AY5 A2S A . 
C 3 HOH   1   401 142 HOH   HOH A . 
C 3 HOH   2   402 95  HOH   HOH A . 
C 3 HOH   3   403 86  HOH   HOH A . 
C 3 HOH   4   404 181 HOH   HOH A . 
C 3 HOH   5   405 103 HOH   HOH A . 
C 3 HOH   6   406 157 HOH   HOH A . 
C 3 HOH   7   407 43  HOH   HOH A . 
C 3 HOH   8   408 178 HOH   HOH A . 
C 3 HOH   9   409 90  HOH   HOH A . 
C 3 HOH   10  410 62  HOH   HOH A . 
C 3 HOH   11  411 29  HOH   HOH A . 
C 3 HOH   12  412 155 HOH   HOH A . 
C 3 HOH   13  413 54  HOH   HOH A . 
C 3 HOH   14  414 102 HOH   HOH A . 
C 3 HOH   15  415 105 HOH   HOH A . 
C 3 HOH   16  416 61  HOH   HOH A . 
C 3 HOH   17  417 27  HOH   HOH A . 
C 3 HOH   18  418 13  HOH   HOH A . 
C 3 HOH   19  419 63  HOH   HOH A . 
C 3 HOH   20  420 51  HOH   HOH A . 
C 3 HOH   21  421 144 HOH   HOH A . 
C 3 HOH   22  422 69  HOH   HOH A . 
C 3 HOH   23  423 38  HOH   HOH A . 
C 3 HOH   24  424 7   HOH   HOH A . 
C 3 HOH   25  425 26  HOH   HOH A . 
C 3 HOH   26  426 5   HOH   HOH A . 
C 3 HOH   27  427 55  HOH   HOH A . 
C 3 HOH   28  428 42  HOH   HOH A . 
C 3 HOH   29  429 132 HOH   HOH A . 
C 3 HOH   30  430 4   HOH   HOH A . 
C 3 HOH   31  431 1   HOH   HOH A . 
C 3 HOH   32  432 10  HOH   HOH A . 
C 3 HOH   33  433 170 HOH   HOH A . 
C 3 HOH   34  434 20  HOH   HOH A . 
C 3 HOH   35  435 53  HOH   HOH A . 
C 3 HOH   36  436 76  HOH   HOH A . 
C 3 HOH   37  437 8   HOH   HOH A . 
C 3 HOH   38  438 2   HOH   HOH A . 
C 3 HOH   39  439 17  HOH   HOH A . 
C 3 HOH   40  440 78  HOH   HOH A . 
C 3 HOH   41  441 163 HOH   HOH A . 
C 3 HOH   42  442 15  HOH   HOH A . 
C 3 HOH   43  443 83  HOH   HOH A . 
C 3 HOH   44  444 14  HOH   HOH A . 
C 3 HOH   45  445 104 HOH   HOH A . 
C 3 HOH   46  446 82  HOH   HOH A . 
C 3 HOH   47  447 6   HOH   HOH A . 
C 3 HOH   48  448 22  HOH   HOH A . 
C 3 HOH   49  449 77  HOH   HOH A . 
C 3 HOH   50  450 37  HOH   HOH A . 
C 3 HOH   51  451 74  HOH   HOH A . 
C 3 HOH   52  452 121 HOH   HOH A . 
C 3 HOH   53  453 44  HOH   HOH A . 
C 3 HOH   54  454 50  HOH   HOH A . 
C 3 HOH   55  455 156 HOH   HOH A . 
C 3 HOH   56  456 16  HOH   HOH A . 
C 3 HOH   57  457 24  HOH   HOH A . 
C 3 HOH   58  458 32  HOH   HOH A . 
C 3 HOH   59  459 108 HOH   HOH A . 
C 3 HOH   60  460 134 HOH   HOH A . 
C 3 HOH   61  461 46  HOH   HOH A . 
C 3 HOH   62  462 153 HOH   HOH A . 
C 3 HOH   63  463 25  HOH   HOH A . 
C 3 HOH   64  464 173 HOH   HOH A . 
C 3 HOH   65  465 162 HOH   HOH A . 
C 3 HOH   66  466 39  HOH   HOH A . 
C 3 HOH   67  467 31  HOH   HOH A . 
C 3 HOH   68  468 154 HOH   HOH A . 
C 3 HOH   69  469 12  HOH   HOH A . 
C 3 HOH   70  470 67  HOH   HOH A . 
C 3 HOH   71  471 91  HOH   HOH A . 
C 3 HOH   72  472 30  HOH   HOH A . 
C 3 HOH   73  473 35  HOH   HOH A . 
C 3 HOH   74  474 88  HOH   HOH A . 
C 3 HOH   75  475 75  HOH   HOH A . 
C 3 HOH   76  476 9   HOH   HOH A . 
C 3 HOH   77  477 64  HOH   HOH A . 
C 3 HOH   78  478 143 HOH   HOH A . 
C 3 HOH   79  479 93  HOH   HOH A . 
C 3 HOH   80  480 73  HOH   HOH A . 
C 3 HOH   81  481 148 HOH   HOH A . 
C 3 HOH   82  482 47  HOH   HOH A . 
C 3 HOH   83  483 158 HOH   HOH A . 
C 3 HOH   84  484 23  HOH   HOH A . 
C 3 HOH   85  485 3   HOH   HOH A . 
C 3 HOH   86  486 172 HOH   HOH A . 
C 3 HOH   87  487 19  HOH   HOH A . 
C 3 HOH   88  488 58  HOH   HOH A . 
C 3 HOH   89  489 80  HOH   HOH A . 
C 3 HOH   90  490 48  HOH   HOH A . 
C 3 HOH   91  491 56  HOH   HOH A . 
C 3 HOH   92  492 171 HOH   HOH A . 
C 3 HOH   93  493 145 HOH   HOH A . 
C 3 HOH   94  494 71  HOH   HOH A . 
C 3 HOH   95  495 130 HOH   HOH A . 
C 3 HOH   96  496 152 HOH   HOH A . 
C 3 HOH   97  497 137 HOH   HOH A . 
C 3 HOH   98  498 126 HOH   HOH A . 
C 3 HOH   99  499 28  HOH   HOH A . 
C 3 HOH   100 500 116 HOH   HOH A . 
C 3 HOH   101 501 106 HOH   HOH A . 
C 3 HOH   102 502 94  HOH   HOH A . 
C 3 HOH   103 503 34  HOH   HOH A . 
C 3 HOH   104 504 119 HOH   HOH A . 
C 3 HOH   105 505 68  HOH   HOH A . 
C 3 HOH   106 506 18  HOH   HOH A . 
C 3 HOH   107 507 128 HOH   HOH A . 
C 3 HOH   108 508 135 HOH   HOH A . 
C 3 HOH   109 509 59  HOH   HOH A . 
C 3 HOH   110 510 65  HOH   HOH A . 
C 3 HOH   111 511 141 HOH   HOH A . 
C 3 HOH   112 512 49  HOH   HOH A . 
C 3 HOH   113 513 123 HOH   HOH A . 
C 3 HOH   114 514 96  HOH   HOH A . 
C 3 HOH   115 515 45  HOH   HOH A . 
C 3 HOH   116 516 164 HOH   HOH A . 
C 3 HOH   117 517 11  HOH   HOH A . 
C 3 HOH   118 518 169 HOH   HOH A . 
C 3 HOH   119 519 40  HOH   HOH A . 
C 3 HOH   120 520 120 HOH   HOH A . 
C 3 HOH   121 521 179 HOH   HOH A . 
C 3 HOH   122 522 70  HOH   HOH A . 
C 3 HOH   123 523 52  HOH   HOH A . 
C 3 HOH   124 524 100 HOH   HOH A . 
C 3 HOH   125 525 174 HOH   HOH A . 
C 3 HOH   126 526 66  HOH   HOH A . 
C 3 HOH   127 527 139 HOH   HOH A . 
C 3 HOH   128 528 92  HOH   HOH A . 
C 3 HOH   129 529 101 HOH   HOH A . 
C 3 HOH   130 530 81  HOH   HOH A . 
C 3 HOH   131 531 160 HOH   HOH A . 
C 3 HOH   132 532 117 HOH   HOH A . 
C 3 HOH   133 533 97  HOH   HOH A . 
C 3 HOH   134 534 151 HOH   HOH A . 
C 3 HOH   135 535 21  HOH   HOH A . 
C 3 HOH   136 536 122 HOH   HOH A . 
C 3 HOH   137 537 138 HOH   HOH A . 
C 3 HOH   138 538 175 HOH   HOH A . 
C 3 HOH   139 539 161 HOH   HOH A . 
C 3 HOH   140 540 84  HOH   HOH A . 
C 3 HOH   141 541 115 HOH   HOH A . 
C 3 HOH   142 542 72  HOH   HOH A . 
C 3 HOH   143 543 99  HOH   HOH A . 
C 3 HOH   144 544 133 HOH   HOH A . 
C 3 HOH   145 545 41  HOH   HOH A . 
C 3 HOH   146 546 159 HOH   HOH A . 
C 3 HOH   147 547 180 HOH   HOH A . 
C 3 HOH   148 548 113 HOH   HOH A . 
C 3 HOH   149 549 109 HOH   HOH A . 
C 3 HOH   150 550 87  HOH   HOH A . 
C 3 HOH   151 551 98  HOH   HOH A . 
C 3 HOH   152 552 124 HOH   HOH A . 
C 3 HOH   153 553 33  HOH   HOH A . 
C 3 HOH   154 554 85  HOH   HOH A . 
C 3 HOH   155 555 168 HOH   HOH A . 
C 3 HOH   156 556 136 HOH   HOH A . 
C 3 HOH   157 557 89  HOH   HOH A . 
C 3 HOH   158 558 36  HOH   HOH A . 
C 3 HOH   159 559 166 HOH   HOH A . 
C 3 HOH   160 560 112 HOH   HOH A . 
C 3 HOH   161 561 60  HOH   HOH A . 
C 3 HOH   162 562 114 HOH   HOH A . 
C 3 HOH   163 563 110 HOH   HOH A . 
C 3 HOH   164 564 118 HOH   HOH A . 
C 3 HOH   165 565 107 HOH   HOH A . 
C 3 HOH   166 566 147 HOH   HOH A . 
C 3 HOH   167 567 149 HOH   HOH A . 
C 3 HOH   168 568 131 HOH   HOH A . 
C 3 HOH   169 569 146 HOH   HOH A . 
C 3 HOH   170 570 129 HOH   HOH A . 
C 3 HOH   171 571 167 HOH   HOH A . 
C 3 HOH   172 572 150 HOH   HOH A . 
C 3 HOH   173 573 165 HOH   HOH A . 
C 3 HOH   174 574 111 HOH   HOH A . 
C 3 HOH   175 575 57  HOH   HOH A . 
C 3 HOH   176 576 125 HOH   HOH A . 
C 3 HOH   177 577 127 HOH   HOH A . 
C 3 HOH   178 578 79  HOH   HOH A . 
C 3 HOH   179 579 182 HOH   HOH A . 
C 3 HOH   180 580 140 HOH   HOH A . 
C 3 HOH   181 581 176 HOH   HOH A . 
C 3 HOH   182 582 177 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             607809.023 
_cell.length_a           68.150 
_cell.length_b           90.490 
_cell.length_c           98.560 
_cell.angle_beta         90.000 
_cell.angle_gamma        90.000 
_cell.angle_alpha        90.000 
_cell.entry_id           7HAT 
_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                         7HAT 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
# 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
_exptl.entry_id          7HAT 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_Matthews      2.88 
_exptl_crystal.density_percent_sol   57.23 
_exptl_crystal.density_meas          ? 
_exptl_crystal.description           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.pH              8.5 
_exptl_crystal_grow.temp            277 
_exptl_crystal_grow.pdbx_details    '100mM Tris-HCl pH 8.5, 22% PEG4000, 200mM MgCl2' 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_diffrn.id                     1 
_diffrn.crystal_id             1 
_diffrn.ambient_temp           100 
_diffrn.ambient_temp_details   ? 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               PIXEL 
_diffrn_detector.type                   'DECTRIS EIGER X 16M' 
_diffrn_detector.pdbx_collection_date   2024-01-21 
_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   BL10U2 
_diffrn_source.type                        'SSRF BEAMLINE BL10U2' 
_diffrn_source.pdbx_wavelength_list        0.97918 
_diffrn_source.pdbx_synchrotron_site       SSRF 
_diffrn_source.pdbx_wavelength             ? 
# 
_reflns.entry_id                     7HAT 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             30.340 
_reflns.d_resolution_high            2.040 
_reflns.number_obs                   19771 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         99.900 
_reflns.pdbx_Rmerge_I_obs            0.133 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        13.900 
_reflns.B_iso_Wilson_estimate        ? 
_reflns.pdbx_redundancy              12.700 
_reflns.pdbx_Rrim_I_all              0.139 
_reflns.pdbx_Rpim_I_all              0.039 
_reflns.pdbx_CC_half                 0.998 
_reflns.pdbx_netI_over_av_sigmaI     ? 
_reflns.pdbx_number_measured_all     251557 
_reflns.pdbx_scaling_rejects         30 
_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 2.040 2.090  ? 18358 1449 ? 1.661 ? ? ? 12.700 ? 2.200  ? ? ? ? ? ? 99.800 1.732 0.486 0.828 
1 2 9.120 30.340 ? 2202  254  ? 0.039 ? ? ? 8.700  ? 34.200 ? ? ? ? ? ? 97.200 0.041 0.013 0.999 
# 
_refine.entry_id                                 7HAT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.ls_percent_reflns_R_free                 4.92 
_refine.pdbx_overall_phase_error                 25.1287 
_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                          0.1894 
_refine.B_iso_mean                               40.85 
_refine.ls_number_reflns_R_free                  972 
_refine.ls_percent_reflns_obs                    99.82 
_refine.ls_R_factor_R_work                       0.1879 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_refine.ls_d_res_high                            2.04 
_refine.ls_number_reflns_obs                     19749 
_refine.pdbx_ls_sigma_F                          1.34 
_refine.ls_number_reflns_R_work                  18777 
_refine.ls_d_res_low                             29.59 
_refine.pdbx_stereochemistry_target_values       'GeoStd + Monomer Library + CDL v1.2' 
_refine.ls_R_factor_R_free                       0.2188 
_refine.overall_SU_ML                            0.2588 
_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             182 
_refine_hist.number_atoms_total               1839 
_refine_hist.d_res_high                       2.04 
_refine_hist.d_res_low                        29.59 
# 
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 0.0052 ? ? ? 
'X-RAY DIFFRACTION' f_angle_d          2269 0.7487 ? ? ? 
'X-RAY DIFFRACTION' f_chiral_restr     259  0.0471 ? ? ? 
'X-RAY DIFFRACTION' f_plane_restr      290  0.0037 ? ? ? 
'X-RAY DIFFRACTION' f_dihedral_angle_d 230  6.7266 ? ? ? 
# 
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' 2.04 2.15  2689 0.2597 99.68  0.3170 117 . . . . . 
'X-RAY DIFFRACTION' 2.15 2.28  2606 0.3300 99.35  0.4048 131 . . . . . 
'X-RAY DIFFRACTION' 2.28 2.46  2653 0.2168 100.00 0.2578 127 . . . . . 
'X-RAY DIFFRACTION' 2.46 2.71  2660 0.2070 99.93  0.2464 144 . . . . . 
'X-RAY DIFFRACTION' 2.71 3.10  2672 0.1899 100.00 0.2390 157 . . . . . 
'X-RAY DIFFRACTION' 3.10 3.90  2696 0.1709 99.96  0.2063 136 . . . . . 
'X-RAY DIFFRACTION' 3.90 29.59 2801 0.1523 99.80  0.1661 160 . . . . . 
# 
_struct.entry_id                  7HAT 
_struct.title                     'PanDDA analysis group deposition -- Crystal structure of HSP90N in complex with Fr12860' 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_details        ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HAT 
_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              7HAT 
_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 7HAT MET A 1   ? UNP P07900 ? ? 'initiating methionine' 8   1 
1 7HAT LEU A 230 ? UNP P07900 ? ? 'expression tag'        237 2 
1 7HAT GLU A 231 ? UNP P07900 ? ? 'expression tag'        238 3 
1 7HAT HIS A 232 ? UNP P07900 ? ? 'expression tag'        239 4 
1 7HAT HIS A 233 ? UNP P07900 ? ? 'expression tag'        240 5 
1 7HAT HIS A 234 ? UNP P07900 ? ? 'expression tag'        241 6 
1 7HAT HIS A 235 ? UNP P07900 ? ? 'expression tag'        242 7 
1 7HAT HIS A 236 ? UNP P07900 ? ? 'expression tag'        243 8 
1 7HAT 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 GLU A 185 ? LEU A 191 ? GLU A 192 LEU A 198 5 ? 7  
HELX_P HELX_P9 AA9 GLU A 192 ? SER A 204 ? GLU A 199 SER A 211 1 ? 13 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
_struct_sheet.id               AA1 
_struct_sheet.type             ? 
_struct_sheet.number_strands   8 
_struct_sheet.details          ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA1 5 6 ? anti-parallel 
AA1 6 7 ? anti-parallel 
AA1 7 8 ? parallel      
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 GLU A 11  ? ALA A 14  ? GLU A 18  ALA A 21  
AA1 2 SER A 162 ? THR A 167 ? SER A 169 THR A 174 
AA1 3 TYR A 153 ? SER A 157 ? TYR A 160 SER A 164 
AA1 4 ALA A 138 ? LYS A 146 ? ALA A 145 LYS A 153 
AA1 5 GLY A 176 ? LEU A 183 ? GLY A 183 LEU A 190 
AA1 6 THR A 81  ? ASP A 86  ? THR A 88  ASP A 93  
AA1 7 ILE A 71  ? ASN A 76  ? ILE A 78  ASN A 83  
AA1 8 ILE A 211 ? LEU A 213 ? ILE A 218 LEU A 220 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N PHE A 13  ? N PHE A 20  O PHE A 163 ? O PHE A 170 
AA1 2 3 O ARG A 166 ? O ARG A 173 N ALA A 154 ? N ALA A 161 
AA1 3 4 O TRP A 155 ? O TRP A 162 N VAL A 143 ? N VAL A 150 
AA1 4 5 N THR A 142 ? N THR A 149 O ILE A 180 ? O ILE A 187 
AA1 5 6 O VAL A 179 ? O VAL A 186 N ILE A 84  ? N ILE A 91  
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                   7HAT 
_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 OE1 A GLU 178 ? ? O A HOH 401 ? ? 1.84 
2 1 O   A HOH 493 ? ? O A HOH 505 ? ? 1.98 
3 1 O   A HOH 540 ? ? O A HOH 549 ? ? 2.11 
# 
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 ALA A 166 ? ? 57.64   -143.14 
2 1 ARG A 182 ? ? -175.78 138.43  
# 
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 13.3952241178   27.3719700761 31.2476147259 0.376159356685 0.328298325517 0.316482285296 
0.0500526742485   -0.047304063165  -0.00220714122731 2.45818002871 1.93937844428 4.10527936057 -0.965419218646  -1.68679992895  
0.683717831155  -0.0437670036545 -0.251163611419  -0.1158187962   0.158012716122    -0.00872062611673 -0.0233147010575 
0.169291958263   0.283757883448   -0.00757494046543 
2 ? 'X-RAY DIFFRACTION' refined -6.70865808668  38.6599376907 23.5512141654 0.305677450531 0.28765700909  0.315100485516 
0.00259251881354  -0.0182461763968 -0.010570222961   1.89554926181 2.23577104194 3.27612797444 -0.780197092592  0.432752076859  
-0.853804429755 0.0372837952197  0.241776392745   0.119780939159  -0.108984193208   -0.0582750010181  0.0493923910469  
-0.165748352495  -0.068892637766  -0.0227710395585  
3 ? 'X-RAY DIFFRACTION' refined -3.53181533111  26.8090444284 25.5353363098 0.338144529847 0.266135532804 0.275440667451 
-0.00826666824027 -0.0356512270831 -0.0468891019963  2.39559615627 1.77814482329 2.20652515482 -1.07602332492   -0.876173148389 
0.0754210947056 -0.0207341653853 0.0840030877381  -0.149688069583 -0.00751610778601 0.140888183205    0.109377653177   
0.370182149905   -0.152978807415  0.0294752480932   
4 ? 'X-RAY DIFFRACTION' refined 12.8431583452   39.1436894072 34.0294311682 0.241087345789 0.280772108886 0.339634527637 
-0.0204414566383  -0.0340903145531 -0.0156459891175  4.60339583848 5.06440870611 2.20143083198 -0.842203913886  -2.1355450119   
-1.70511081688  0.132022114329   -0.480445498346  0.464726821029  0.511775667666    -0.187782445221   -0.470342691476  
-0.251444997132  0.459904154213   0.0837568640171   
5 ? 'X-RAY DIFFRACTION' refined -0.460234619632 25.4401678926 28.4737563522 0.279185043653 0.209239789304 0.292467513044 
-0.00423532951871 0.00521782786484 -0.00541326345268 2.55237968166 1.47323456829 2.7397192497  0.00917907575757 -0.288854505771 
0.0578103712205 -0.0526374803563 0.00608757195776 -0.295202762454 -0.0574401773114  0.0494140940123   0.0508934702534  
0.335250065632   -0.0252289407487 -0.0020265987551  
6 ? 'X-RAY DIFFRACTION' refined -13.2834547261  31.8789180431 33.6328045096 0.348576988649 0.361986318693 0.333817107216 
-0.0119519201853  0.0125623568358  0.0148046428688   3.65169396703 3.71403611449 2.77272715806 1.01359489545    0.251783004983  
-0.277826906918 0.148452354456   -0.467438971143  -0.109497212141 0.641563088827    -0.309243230489   0.0223697849535  
-0.0546404314222 -0.269342284447  -0.0119345964661  
# 
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 210 A 195 . 
;chain 'A' and (resid 137 through 210 )
;
6 6 'X-RAY DIFFRACTION' A 211 A 196 A 224 A 209 . 
;chain 'A' and (resid 211 through 224 )
;
# 
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 
A1AY5 C8   C N N 1   
A1AY5 C5   C Y N 2   
A1AY5 C6   C N N 3   
A1AY5 N1   N N N 4   
A1AY5 C2   C Y N 5   
A1AY5 C4   C Y N 6   
A1AY5 C1   C N N 7   
A1AY5 C3   C Y N 8   
A1AY5 C7   C N N 9   
A1AY5 C9   C N N 10  
A1AY5 O1   O N N 11  
A1AY5 O2   O Y N 12  
A1AY5 S1   S N N 13  
A1AY5 H82  H N N 14  
A1AY5 H83  H N N 15  
A1AY5 H5   H N N 16  
A1AY5 H62  H N N 17  
A1AY5 H63  H N N 18  
A1AY5 H4   H N N 19  
A1AY5 H3   H N N 20  
A1AY5 H72  H N N 21  
A1AY5 H73  H N N 22  
A1AY5 H93  H N N 23  
A1AY5 H92  H N N 24  
ALA   N    N N N 25  
ALA   CA   C N S 26  
ALA   C    C N N 27  
ALA   O    O N N 28  
ALA   CB   C N N 29  
ALA   OXT  O N N 30  
ALA   H    H N N 31  
ALA   H2   H N N 32  
ALA   HA   H N N 33  
ALA   HB1  H N N 34  
ALA   HB2  H N N 35  
ALA   HB3  H N N 36  
ALA   HXT  H N N 37  
ARG   N    N N N 38  
ARG   CA   C N S 39  
ARG   C    C N N 40  
ARG   O    O N N 41  
ARG   CB   C N N 42  
ARG   CG   C N N 43  
ARG   CD   C N N 44  
ARG   NE   N N N 45  
ARG   CZ   C N N 46  
ARG   NH1  N N N 47  
ARG   NH2  N N N 48  
ARG   OXT  O N N 49  
ARG   H    H N N 50  
ARG   H2   H N N 51  
ARG   HA   H N N 52  
ARG   HB2  H N N 53  
ARG   HB3  H N N 54  
ARG   HG2  H N N 55  
ARG   HG3  H N N 56  
ARG   HD2  H N N 57  
ARG   HD3  H N N 58  
ARG   HE   H N N 59  
ARG   HH11 H N N 60  
ARG   HH12 H N N 61  
ARG   HH21 H N N 62  
ARG   HH22 H N N 63  
ARG   HXT  H N N 64  
ASN   N    N N N 65  
ASN   CA   C N S 66  
ASN   C    C N N 67  
ASN   O    O N N 68  
ASN   CB   C N N 69  
ASN   CG   C N N 70  
ASN   OD1  O N N 71  
ASN   ND2  N N N 72  
ASN   OXT  O N N 73  
ASN   H    H N N 74  
ASN   H2   H N N 75  
ASN   HA   H N N 76  
ASN   HB2  H N N 77  
ASN   HB3  H N N 78  
ASN   HD21 H N N 79  
ASN   HD22 H N N 80  
ASN   HXT  H N N 81  
ASP   N    N N N 82  
ASP   CA   C N S 83  
ASP   C    C N N 84  
ASP   O    O N N 85  
ASP   CB   C N N 86  
ASP   CG   C N N 87  
ASP   OD1  O N N 88  
ASP   OD2  O N N 89  
ASP   OXT  O N N 90  
ASP   H    H N N 91  
ASP   H2   H N N 92  
ASP   HA   H N N 93  
ASP   HB2  H N N 94  
ASP   HB3  H N N 95  
ASP   HD2  H N N 96  
ASP   HXT  H N N 97  
GLN   N    N N N 98  
GLN   CA   C N S 99  
GLN   C    C N N 100 
GLN   O    O N N 101 
GLN   CB   C N N 102 
GLN   CG   C N N 103 
GLN   CD   C N N 104 
GLN   OE1  O N N 105 
GLN   NE2  N N N 106 
GLN   OXT  O N N 107 
GLN   H    H N N 108 
GLN   H2   H N N 109 
GLN   HA   H N N 110 
GLN   HB2  H N N 111 
GLN   HB3  H N N 112 
GLN   HG2  H N N 113 
GLN   HG3  H N N 114 
GLN   HE21 H N N 115 
GLN   HE22 H N N 116 
GLN   HXT  H N N 117 
GLU   N    N N N 118 
GLU   CA   C N S 119 
GLU   C    C N N 120 
GLU   O    O N N 121 
GLU   CB   C N N 122 
GLU   CG   C N N 123 
GLU   CD   C N N 124 
GLU   OE1  O N N 125 
GLU   OE2  O N N 126 
GLU   OXT  O N N 127 
GLU   H    H N N 128 
GLU   H2   H N N 129 
GLU   HA   H N N 130 
GLU   HB2  H N N 131 
GLU   HB3  H N N 132 
GLU   HG2  H N N 133 
GLU   HG3  H N N 134 
GLU   HE2  H N N 135 
GLU   HXT  H N N 136 
GLY   N    N N N 137 
GLY   CA   C N N 138 
GLY   C    C N N 139 
GLY   O    O N N 140 
GLY   OXT  O N N 141 
GLY   H    H N N 142 
GLY   H2   H N N 143 
GLY   HA2  H N N 144 
GLY   HA3  H N N 145 
GLY   HXT  H N N 146 
HIS   N    N N N 147 
HIS   CA   C N S 148 
HIS   C    C N N 149 
HIS   O    O N N 150 
HIS   CB   C N N 151 
HIS   CG   C Y N 152 
HIS   ND1  N Y N 153 
HIS   CD2  C Y N 154 
HIS   CE1  C Y N 155 
HIS   NE2  N Y N 156 
HIS   OXT  O N N 157 
HIS   H    H N N 158 
HIS   H2   H N N 159 
HIS   HA   H N N 160 
HIS   HB2  H N N 161 
HIS   HB3  H N N 162 
HIS   HD1  H N N 163 
HIS   HD2  H N N 164 
HIS   HE1  H N N 165 
HIS   HE2  H N N 166 
HIS   HXT  H N N 167 
HOH   O    O N N 168 
HOH   H1   H N N 169 
HOH   H2   H N N 170 
ILE   N    N N N 171 
ILE   CA   C N S 172 
ILE   C    C N N 173 
ILE   O    O N N 174 
ILE   CB   C N S 175 
ILE   CG1  C N N 176 
ILE   CG2  C N N 177 
ILE   CD1  C N N 178 
ILE   OXT  O N N 179 
ILE   H    H N N 180 
ILE   H2   H N N 181 
ILE   HA   H N N 182 
ILE   HB   H N N 183 
ILE   HG12 H N N 184 
ILE   HG13 H N N 185 
ILE   HG21 H N N 186 
ILE   HG22 H N N 187 
ILE   HG23 H N N 188 
ILE   HD11 H N N 189 
ILE   HD12 H N N 190 
ILE   HD13 H N N 191 
ILE   HXT  H N N 192 
LEU   N    N N N 193 
LEU   CA   C N S 194 
LEU   C    C N N 195 
LEU   O    O N N 196 
LEU   CB   C N N 197 
LEU   CG   C N N 198 
LEU   CD1  C N N 199 
LEU   CD2  C N N 200 
LEU   OXT  O N N 201 
LEU   H    H N N 202 
LEU   H2   H N N 203 
LEU   HA   H N N 204 
LEU   HB2  H N N 205 
LEU   HB3  H N N 206 
LEU   HG   H N N 207 
LEU   HD11 H N N 208 
LEU   HD12 H N N 209 
LEU   HD13 H N N 210 
LEU   HD21 H N N 211 
LEU   HD22 H N N 212 
LEU   HD23 H N N 213 
LEU   HXT  H N N 214 
LYS   N    N N N 215 
LYS   CA   C N S 216 
LYS   C    C N N 217 
LYS   O    O N N 218 
LYS   CB   C N N 219 
LYS   CG   C N N 220 
LYS   CD   C N N 221 
LYS   CE   C N N 222 
LYS   NZ   N N N 223 
LYS   OXT  O N N 224 
LYS   H    H N N 225 
LYS   H2   H N N 226 
LYS   HA   H N N 227 
LYS   HB2  H N N 228 
LYS   HB3  H N N 229 
LYS   HG2  H N N 230 
LYS   HG3  H N N 231 
LYS   HD2  H N N 232 
LYS   HD3  H N N 233 
LYS   HE2  H N N 234 
LYS   HE3  H N N 235 
LYS   HZ1  H N N 236 
LYS   HZ2  H N N 237 
LYS   HZ3  H N N 238 
LYS   HXT  H N N 239 
MET   N    N N N 240 
MET   CA   C N S 241 
MET   C    C N N 242 
MET   O    O N N 243 
MET   CB   C N N 244 
MET   CG   C N N 245 
MET   SD   S N N 246 
MET   CE   C N N 247 
MET   OXT  O N N 248 
MET   H    H N N 249 
MET   H2   H N N 250 
MET   HA   H N N 251 
MET   HB2  H N N 252 
MET   HB3  H N N 253 
MET   HG2  H N N 254 
MET   HG3  H N N 255 
MET   HE1  H N N 256 
MET   HE2  H N N 257 
MET   HE3  H N N 258 
MET   HXT  H N N 259 
PHE   N    N N N 260 
PHE   CA   C N S 261 
PHE   C    C N N 262 
PHE   O    O N N 263 
PHE   CB   C N N 264 
PHE   CG   C Y N 265 
PHE   CD1  C Y N 266 
PHE   CD2  C Y N 267 
PHE   CE1  C Y N 268 
PHE   CE2  C Y N 269 
PHE   CZ   C Y N 270 
PHE   OXT  O N N 271 
PHE   H    H N N 272 
PHE   H2   H N N 273 
PHE   HA   H N N 274 
PHE   HB2  H N N 275 
PHE   HB3  H N N 276 
PHE   HD1  H N N 277 
PHE   HD2  H N N 278 
PHE   HE1  H N N 279 
PHE   HE2  H N N 280 
PHE   HZ   H N N 281 
PHE   HXT  H N N 282 
PRO   N    N N N 283 
PRO   CA   C N S 284 
PRO   C    C N N 285 
PRO   O    O N N 286 
PRO   CB   C N N 287 
PRO   CG   C N N 288 
PRO   CD   C N N 289 
PRO   OXT  O N N 290 
PRO   H    H N N 291 
PRO   HA   H N N 292 
PRO   HB2  H N N 293 
PRO   HB3  H N N 294 
PRO   HG2  H N N 295 
PRO   HG3  H N N 296 
PRO   HD2  H N N 297 
PRO   HD3  H N N 298 
PRO   HXT  H N N 299 
SER   N    N N N 300 
SER   CA   C N S 301 
SER   C    C N N 302 
SER   O    O N N 303 
SER   CB   C N N 304 
SER   OG   O N N 305 
SER   OXT  O N N 306 
SER   H    H N N 307 
SER   H2   H N N 308 
SER   HA   H N N 309 
SER   HB2  H N N 310 
SER   HB3  H N N 311 
SER   HG   H N N 312 
SER   HXT  H N N 313 
THR   N    N N N 314 
THR   CA   C N S 315 
THR   C    C N N 316 
THR   O    O N N 317 
THR   CB   C N R 318 
THR   OG1  O N N 319 
THR   CG2  C N N 320 
THR   OXT  O N N 321 
THR   H    H N N 322 
THR   H2   H N N 323 
THR   HA   H N N 324 
THR   HB   H N N 325 
THR   HG1  H N N 326 
THR   HG21 H N N 327 
THR   HG22 H N N 328 
THR   HG23 H N N 329 
THR   HXT  H N N 330 
TRP   N    N N N 331 
TRP   CA   C N S 332 
TRP   C    C N N 333 
TRP   O    O N N 334 
TRP   CB   C N N 335 
TRP   CG   C Y N 336 
TRP   CD1  C Y N 337 
TRP   CD2  C Y N 338 
TRP   NE1  N Y N 339 
TRP   CE2  C Y N 340 
TRP   CE3  C Y N 341 
TRP   CZ2  C Y N 342 
TRP   CZ3  C Y N 343 
TRP   CH2  C Y N 344 
TRP   OXT  O N N 345 
TRP   H    H N N 346 
TRP   H2   H N N 347 
TRP   HA   H N N 348 
TRP   HB2  H N N 349 
TRP   HB3  H N N 350 
TRP   HD1  H N N 351 
TRP   HE1  H N N 352 
TRP   HE3  H N N 353 
TRP   HZ2  H N N 354 
TRP   HZ3  H N N 355 
TRP   HH2  H N N 356 
TRP   HXT  H N N 357 
TYR   N    N N N 358 
TYR   CA   C N S 359 
TYR   C    C N N 360 
TYR   O    O N N 361 
TYR   CB   C N N 362 
TYR   CG   C Y N 363 
TYR   CD1  C Y N 364 
TYR   CD2  C Y N 365 
TYR   CE1  C Y N 366 
TYR   CE2  C Y N 367 
TYR   CZ   C Y N 368 
TYR   OH   O N N 369 
TYR   OXT  O N N 370 
TYR   H    H N N 371 
TYR   H2   H N N 372 
TYR   HA   H N N 373 
TYR   HB2  H N N 374 
TYR   HB3  H N N 375 
TYR   HD1  H N N 376 
TYR   HD2  H N N 377 
TYR   HE1  H N N 378 
TYR   HE2  H N N 379 
TYR   HH   H N N 380 
TYR   HXT  H N N 381 
VAL   N    N N N 382 
VAL   CA   C N S 383 
VAL   C    C N N 384 
VAL   O    O N N 385 
VAL   CB   C N N 386 
VAL   CG1  C N N 387 
VAL   CG2  C N N 388 
VAL   OXT  O N N 389 
VAL   H    H N N 390 
VAL   H2   H N N 391 
VAL   HA   H N N 392 
VAL   HB   H N N 393 
VAL   HG11 H N N 394 
VAL   HG12 H N N 395 
VAL   HG13 H N N 396 
VAL   HG21 H N N 397 
VAL   HG22 H N N 398 
VAL   HG23 H N N 399 
VAL   HXT  H N N 400 
# 
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 
A1AY5 O1  C1   doub N N 1   
A1AY5 C1  C2   sing N N 2   
A1AY5 C1  N1   sing N N 3   
A1AY5 C2  C3   doub Y N 4   
A1AY5 C2  O2   sing Y N 5   
A1AY5 C3  C4   sing Y N 6   
A1AY5 C4  C5   doub Y N 7   
A1AY5 C5  O2   sing Y N 8   
A1AY5 N1  C6   sing N N 9   
A1AY5 N1  C9   sing N N 10  
A1AY5 C6  C7   sing N N 11  
A1AY5 C7  S1   sing N N 12  
A1AY5 S1  C8   sing N N 13  
A1AY5 C8  C9   sing N N 14  
A1AY5 C8  H82  sing N N 15  
A1AY5 C8  H83  sing N N 16  
A1AY5 C5  H5   sing N N 17  
A1AY5 C6  H62  sing N N 18  
A1AY5 C6  H63  sing N N 19  
A1AY5 C4  H4   sing N N 20  
A1AY5 C3  H3   sing N N 21  
A1AY5 C7  H72  sing N N 22  
A1AY5 C7  H73  sing N N 23  
A1AY5 C9  H93  sing N N 24  
A1AY5 C9  H92  sing N N 25  
ALA   N   CA   sing N N 26  
ALA   N   H    sing N N 27  
ALA   N   H2   sing N N 28  
ALA   CA  C    sing N N 29  
ALA   CA  CB   sing N N 30  
ALA   CA  HA   sing N N 31  
ALA   C   O    doub N N 32  
ALA   C   OXT  sing N N 33  
ALA   CB  HB1  sing N N 34  
ALA   CB  HB2  sing N N 35  
ALA   CB  HB3  sing N N 36  
ALA   OXT HXT  sing N N 37  
ARG   N   CA   sing N N 38  
ARG   N   H    sing N N 39  
ARG   N   H2   sing N N 40  
ARG   CA  C    sing N N 41  
ARG   CA  CB   sing N N 42  
ARG   CA  HA   sing N N 43  
ARG   C   O    doub N N 44  
ARG   C   OXT  sing N N 45  
ARG   CB  CG   sing N N 46  
ARG   CB  HB2  sing N N 47  
ARG   CB  HB3  sing N N 48  
ARG   CG  CD   sing N N 49  
ARG   CG  HG2  sing N N 50  
ARG   CG  HG3  sing N N 51  
ARG   CD  NE   sing N N 52  
ARG   CD  HD2  sing N N 53  
ARG   CD  HD3  sing N N 54  
ARG   NE  CZ   sing N N 55  
ARG   NE  HE   sing N N 56  
ARG   CZ  NH1  sing N N 57  
ARG   CZ  NH2  doub N N 58  
ARG   NH1 HH11 sing N N 59  
ARG   NH1 HH12 sing N N 60  
ARG   NH2 HH21 sing N N 61  
ARG   NH2 HH22 sing N N 62  
ARG   OXT HXT  sing N N 63  
ASN   N   CA   sing N N 64  
ASN   N   H    sing N N 65  
ASN   N   H2   sing N N 66  
ASN   CA  C    sing N N 67  
ASN   CA  CB   sing N N 68  
ASN   CA  HA   sing N N 69  
ASN   C   O    doub N N 70  
ASN   C   OXT  sing N N 71  
ASN   CB  CG   sing N N 72  
ASN   CB  HB2  sing N N 73  
ASN   CB  HB3  sing N N 74  
ASN   CG  OD1  doub N N 75  
ASN   CG  ND2  sing N N 76  
ASN   ND2 HD21 sing N N 77  
ASN   ND2 HD22 sing N N 78  
ASN   OXT HXT  sing N N 79  
ASP   N   CA   sing N N 80  
ASP   N   H    sing N N 81  
ASP   N   H2   sing N N 82  
ASP   CA  C    sing N N 83  
ASP   CA  CB   sing N N 84  
ASP   CA  HA   sing N N 85  
ASP   C   O    doub N N 86  
ASP   C   OXT  sing N N 87  
ASP   CB  CG   sing N N 88  
ASP   CB  HB2  sing N N 89  
ASP   CB  HB3  sing N N 90  
ASP   CG  OD1  doub N N 91  
ASP   CG  OD2  sing N N 92  
ASP   OD2 HD2  sing N N 93  
ASP   OXT HXT  sing N N 94  
GLN   N   CA   sing N N 95  
GLN   N   H    sing N N 96  
GLN   N   H2   sing N N 97  
GLN   CA  C    sing N N 98  
GLN   CA  CB   sing N N 99  
GLN   CA  HA   sing N N 100 
GLN   C   O    doub N N 101 
GLN   C   OXT  sing N N 102 
GLN   CB  CG   sing N N 103 
GLN   CB  HB2  sing N N 104 
GLN   CB  HB3  sing N N 105 
GLN   CG  CD   sing N N 106 
GLN   CG  HG2  sing N N 107 
GLN   CG  HG3  sing N N 108 
GLN   CD  OE1  doub N N 109 
GLN   CD  NE2  sing N N 110 
GLN   NE2 HE21 sing N N 111 
GLN   NE2 HE22 sing N N 112 
GLN   OXT HXT  sing N N 113 
GLU   N   CA   sing N N 114 
GLU   N   H    sing N N 115 
GLU   N   H2   sing N N 116 
GLU   CA  C    sing N N 117 
GLU   CA  CB   sing N N 118 
GLU   CA  HA   sing N N 119 
GLU   C   O    doub N N 120 
GLU   C   OXT  sing N N 121 
GLU   CB  CG   sing N N 122 
GLU   CB  HB2  sing N N 123 
GLU   CB  HB3  sing N N 124 
GLU   CG  CD   sing N N 125 
GLU   CG  HG2  sing N N 126 
GLU   CG  HG3  sing N N 127 
GLU   CD  OE1  doub N N 128 
GLU   CD  OE2  sing N N 129 
GLU   OE2 HE2  sing N N 130 
GLU   OXT HXT  sing N N 131 
GLY   N   CA   sing N N 132 
GLY   N   H    sing N N 133 
GLY   N   H2   sing N N 134 
GLY   CA  C    sing N N 135 
GLY   CA  HA2  sing N N 136 
GLY   CA  HA3  sing N N 137 
GLY   C   O    doub N N 138 
GLY   C   OXT  sing N N 139 
GLY   OXT HXT  sing N N 140 
HIS   N   CA   sing N N 141 
HIS   N   H    sing N N 142 
HIS   N   H2   sing N N 143 
HIS   CA  C    sing N N 144 
HIS   CA  CB   sing N N 145 
HIS   CA  HA   sing N N 146 
HIS   C   O    doub N N 147 
HIS   C   OXT  sing N N 148 
HIS   CB  CG   sing N N 149 
HIS   CB  HB2  sing N N 150 
HIS   CB  HB3  sing N N 151 
HIS   CG  ND1  sing Y N 152 
HIS   CG  CD2  doub Y N 153 
HIS   ND1 CE1  doub Y N 154 
HIS   ND1 HD1  sing N N 155 
HIS   CD2 NE2  sing Y N 156 
HIS   CD2 HD2  sing N N 157 
HIS   CE1 NE2  sing Y N 158 
HIS   CE1 HE1  sing N N 159 
HIS   NE2 HE2  sing N N 160 
HIS   OXT HXT  sing N N 161 
HOH   O   H1   sing N N 162 
HOH   O   H2   sing N N 163 
ILE   N   CA   sing N N 164 
ILE   N   H    sing N N 165 
ILE   N   H2   sing N N 166 
ILE   CA  C    sing N N 167 
ILE   CA  CB   sing N N 168 
ILE   CA  HA   sing N N 169 
ILE   C   O    doub N N 170 
ILE   C   OXT  sing N N 171 
ILE   CB  CG1  sing N N 172 
ILE   CB  CG2  sing N N 173 
ILE   CB  HB   sing N N 174 
ILE   CG1 CD1  sing N N 175 
ILE   CG1 HG12 sing N N 176 
ILE   CG1 HG13 sing N N 177 
ILE   CG2 HG21 sing N N 178 
ILE   CG2 HG22 sing N N 179 
ILE   CG2 HG23 sing N N 180 
ILE   CD1 HD11 sing N N 181 
ILE   CD1 HD12 sing N N 182 
ILE   CD1 HD13 sing N N 183 
ILE   OXT HXT  sing N N 184 
LEU   N   CA   sing N N 185 
LEU   N   H    sing N N 186 
LEU   N   H2   sing N N 187 
LEU   CA  C    sing N N 188 
LEU   CA  CB   sing N N 189 
LEU   CA  HA   sing N N 190 
LEU   C   O    doub N N 191 
LEU   C   OXT  sing N N 192 
LEU   CB  CG   sing N N 193 
LEU   CB  HB2  sing N N 194 
LEU   CB  HB3  sing N N 195 
LEU   CG  CD1  sing N N 196 
LEU   CG  CD2  sing N N 197 
LEU   CG  HG   sing N N 198 
LEU   CD1 HD11 sing N N 199 
LEU   CD1 HD12 sing N N 200 
LEU   CD1 HD13 sing N N 201 
LEU   CD2 HD21 sing N N 202 
LEU   CD2 HD22 sing N N 203 
LEU   CD2 HD23 sing N N 204 
LEU   OXT HXT  sing N N 205 
LYS   N   CA   sing N N 206 
LYS   N   H    sing N N 207 
LYS   N   H2   sing N N 208 
LYS   CA  C    sing N N 209 
LYS   CA  CB   sing N N 210 
LYS   CA  HA   sing N N 211 
LYS   C   O    doub N N 212 
LYS   C   OXT  sing N N 213 
LYS   CB  CG   sing N N 214 
LYS   CB  HB2  sing N N 215 
LYS   CB  HB3  sing N N 216 
LYS   CG  CD   sing N N 217 
LYS   CG  HG2  sing N N 218 
LYS   CG  HG3  sing N N 219 
LYS   CD  CE   sing N N 220 
LYS   CD  HD2  sing N N 221 
LYS   CD  HD3  sing N N 222 
LYS   CE  NZ   sing N N 223 
LYS   CE  HE2  sing N N 224 
LYS   CE  HE3  sing N N 225 
LYS   NZ  HZ1  sing N N 226 
LYS   NZ  HZ2  sing N N 227 
LYS   NZ  HZ3  sing N N 228 
LYS   OXT HXT  sing N N 229 
MET   N   CA   sing N N 230 
MET   N   H    sing N N 231 
MET   N   H2   sing N N 232 
MET   CA  C    sing N N 233 
MET   CA  CB   sing N N 234 
MET   CA  HA   sing N N 235 
MET   C   O    doub N N 236 
MET   C   OXT  sing N N 237 
MET   CB  CG   sing N N 238 
MET   CB  HB2  sing N N 239 
MET   CB  HB3  sing N N 240 
MET   CG  SD   sing N N 241 
MET   CG  HG2  sing N N 242 
MET   CG  HG3  sing N N 243 
MET   SD  CE   sing N N 244 
MET   CE  HE1  sing N N 245 
MET   CE  HE2  sing N N 246 
MET   CE  HE3  sing N N 247 
MET   OXT HXT  sing N N 248 
PHE   N   CA   sing N N 249 
PHE   N   H    sing N N 250 
PHE   N   H2   sing N N 251 
PHE   CA  C    sing N N 252 
PHE   CA  CB   sing N N 253 
PHE   CA  HA   sing N N 254 
PHE   C   O    doub N N 255 
PHE   C   OXT  sing N N 256 
PHE   CB  CG   sing N N 257 
PHE   CB  HB2  sing N N 258 
PHE   CB  HB3  sing N N 259 
PHE   CG  CD1  doub Y N 260 
PHE   CG  CD2  sing Y N 261 
PHE   CD1 CE1  sing Y N 262 
PHE   CD1 HD1  sing N N 263 
PHE   CD2 CE2  doub Y N 264 
PHE   CD2 HD2  sing N N 265 
PHE   CE1 CZ   doub Y N 266 
PHE   CE1 HE1  sing N N 267 
PHE   CE2 CZ   sing Y N 268 
PHE   CE2 HE2  sing N N 269 
PHE   CZ  HZ   sing N N 270 
PHE   OXT HXT  sing N N 271 
PRO   N   CA   sing N N 272 
PRO   N   CD   sing N N 273 
PRO   N   H    sing N N 274 
PRO   CA  C    sing N N 275 
PRO   CA  CB   sing N N 276 
PRO   CA  HA   sing N N 277 
PRO   C   O    doub N N 278 
PRO   C   OXT  sing N N 279 
PRO   CB  CG   sing N N 280 
PRO   CB  HB2  sing N N 281 
PRO   CB  HB3  sing N N 282 
PRO   CG  CD   sing N N 283 
PRO   CG  HG2  sing N N 284 
PRO   CG  HG3  sing N N 285 
PRO   CD  HD2  sing N N 286 
PRO   CD  HD3  sing N N 287 
PRO   OXT HXT  sing N N 288 
SER   N   CA   sing N N 289 
SER   N   H    sing N N 290 
SER   N   H2   sing N N 291 
SER   CA  C    sing N N 292 
SER   CA  CB   sing N N 293 
SER   CA  HA   sing N N 294 
SER   C   O    doub N N 295 
SER   C   OXT  sing N N 296 
SER   CB  OG   sing N N 297 
SER   CB  HB2  sing N N 298 
SER   CB  HB3  sing N N 299 
SER   OG  HG   sing N N 300 
SER   OXT HXT  sing N N 301 
THR   N   CA   sing N N 302 
THR   N   H    sing N N 303 
THR   N   H2   sing N N 304 
THR   CA  C    sing N N 305 
THR   CA  CB   sing N N 306 
THR   CA  HA   sing N N 307 
THR   C   O    doub N N 308 
THR   C   OXT  sing N N 309 
THR   CB  OG1  sing N N 310 
THR   CB  CG2  sing N N 311 
THR   CB  HB   sing N N 312 
THR   OG1 HG1  sing N N 313 
THR   CG2 HG21 sing N N 314 
THR   CG2 HG22 sing N N 315 
THR   CG2 HG23 sing N N 316 
THR   OXT HXT  sing N N 317 
TRP   N   CA   sing N N 318 
TRP   N   H    sing N N 319 
TRP   N   H2   sing N N 320 
TRP   CA  C    sing N N 321 
TRP   CA  CB   sing N N 322 
TRP   CA  HA   sing N N 323 
TRP   C   O    doub N N 324 
TRP   C   OXT  sing N N 325 
TRP   CB  CG   sing N N 326 
TRP   CB  HB2  sing N N 327 
TRP   CB  HB3  sing N N 328 
TRP   CG  CD1  doub Y N 329 
TRP   CG  CD2  sing Y N 330 
TRP   CD1 NE1  sing Y N 331 
TRP   CD1 HD1  sing N N 332 
TRP   CD2 CE2  doub Y N 333 
TRP   CD2 CE3  sing Y N 334 
TRP   NE1 CE2  sing Y N 335 
TRP   NE1 HE1  sing N N 336 
TRP   CE2 CZ2  sing Y N 337 
TRP   CE3 CZ3  doub Y N 338 
TRP   CE3 HE3  sing N N 339 
TRP   CZ2 CH2  doub Y N 340 
TRP   CZ2 HZ2  sing N N 341 
TRP   CZ3 CH2  sing Y N 342 
TRP   CZ3 HZ3  sing N N 343 
TRP   CH2 HH2  sing N N 344 
TRP   OXT HXT  sing N N 345 
TYR   N   CA   sing N N 346 
TYR   N   H    sing N N 347 
TYR   N   H2   sing N N 348 
TYR   CA  C    sing N N 349 
TYR   CA  CB   sing N N 350 
TYR   CA  HA   sing N N 351 
TYR   C   O    doub N N 352 
TYR   C   OXT  sing N N 353 
TYR   CB  CG   sing N N 354 
TYR   CB  HB2  sing N N 355 
TYR   CB  HB3  sing N N 356 
TYR   CG  CD1  doub Y N 357 
TYR   CG  CD2  sing Y N 358 
TYR   CD1 CE1  sing Y N 359 
TYR   CD1 HD1  sing N N 360 
TYR   CD2 CE2  doub Y N 361 
TYR   CD2 HD2  sing N N 362 
TYR   CE1 CZ   doub Y N 363 
TYR   CE1 HE1  sing N N 364 
TYR   CE2 CZ   sing Y N 365 
TYR   CE2 HE2  sing N N 366 
TYR   CZ  OH   sing N N 367 
TYR   OH  HH   sing N N 368 
TYR   OXT HXT  sing N N 369 
VAL   N   CA   sing N N 370 
VAL   N   H    sing N N 371 
VAL   N   H2   sing N N 372 
VAL   CA  C    sing N N 373 
VAL   CA  CB   sing N N 374 
VAL   CA  HA   sing N N 375 
VAL   C   O    doub N N 376 
VAL   C   OXT  sing N N 377 
VAL   CB  CG1  sing N N 378 
VAL   CB  CG2  sing N N 379 
VAL   CB  HB   sing N N 380 
VAL   CG1 HG11 sing N N 381 
VAL   CG1 HG12 sing N N 382 
VAL   CG1 HG13 sing N N 383 
VAL   CG2 HG21 sing N N 384 
VAL   CG2 HG22 sing N N 385 
VAL   CG2 HG23 sing N N 386 
VAL   OXT HXT  sing N N 387 
# 
_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                    7HAT 
_atom_sites.fract_transf_matrix[1][1]   0.014674 
_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]   0.011051 
_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]   0.010146 
_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   ? 6.80451   15.75583 11.10810 1.000 79.03551  ? 16  GLU   A N   1 
ATOM   2    C CA  . GLU   A 1 9   ? 8.08034   16.46045 11.04393 1.000 65.21728  ? 16  GLU   A CA  1 
ATOM   3    C C   . GLU   A 1 9   ? 8.21080   17.43653 12.20370 1.000 55.85445  ? 16  GLU   A C   1 
ATOM   4    O O   . GLU   A 1 9   ? 7.54677   18.47027 12.24293 1.000 55.48739  ? 16  GLU   A O   1 
ATOM   5    C CB  . GLU   A 1 9   ? 8.23051   17.18991 9.70637  1.000 74.09751  ? 16  GLU   A CB  1 
ATOM   6    C CG  . GLU   A 1 9   ? 6.97267   17.90835 9.23974  1.000 90.35079  ? 16  GLU   A CG  1 
ATOM   7    C CD  . GLU   A 1 9   ? 6.08090   17.03092 8.37393  1.000 100.62561 ? 16  GLU   A CD  1 
ATOM   8    O OE1 . GLU   A 1 9   ? 5.22573   16.31215 8.93906  1.000 101.18756 ? 16  GLU   A OE1 1 
ATOM   9    O OE2 . GLU   A 1 9   ? 6.23874   17.05819 7.13302  1.000 86.92667  ? 16  GLU   A OE2 1 
ATOM   10   N N   . VAL   A 1 10  ? 9.08128   17.09550 13.14622 1.000 45.43649  ? 17  VAL   A N   1 
ATOM   11   C CA  . VAL   A 1 10  ? 9.27796   17.85785 14.37321 1.000 52.31480  ? 17  VAL   A CA  1 
ATOM   12   C C   . VAL   A 1 10  ? 10.64581  18.52323 14.31492 1.000 36.89726  ? 17  VAL   A C   1 
ATOM   13   O O   . VAL   A 1 10  ? 11.65491  17.85248 14.06611 1.000 45.99261  ? 17  VAL   A O   1 
ATOM   14   C CB  . VAL   A 1 10  ? 9.16355   16.94583 15.60544 1.000 48.29939  ? 17  VAL   A CB  1 
ATOM   15   C CG1 . VAL   A 1 10  ? 9.19925   17.76701 16.88667 1.000 39.77414  ? 17  VAL   A CG1 1 
ATOM   16   C CG2 . VAL   A 1 10  ? 7.90310   16.09623 15.51198 1.000 41.11075  ? 17  VAL   A CG2 1 
ATOM   17   N N   . GLU   A 1 11  ? 10.68322  19.83200 14.54529 1.000 35.75432  ? 18  GLU   A N   1 
ATOM   18   C CA  . GLU   A 1 11  ? 11.93378  20.58060 14.61262 1.000 34.71205  ? 18  GLU   A CA  1 
ATOM   19   C C   . GLU   A 1 11  ? 12.28305  20.86176 16.06693 1.000 32.71732  ? 18  GLU   A C   1 
ATOM   20   O O   . GLU   A 1 11  ? 11.42476  21.27095 16.84905 1.000 32.20820  ? 18  GLU   A O   1 
ATOM   21   C CB  . GLU   A 1 11  ? 11.85108  21.89514 13.83022 1.000 36.98176  ? 18  GLU   A CB  1 
ATOM   22   C CG  . GLU   A 1 11  ? 11.69135  21.71699 12.32205 1.000 49.83390  ? 18  GLU   A CG  1 
ATOM   23   C CD  . GLU   A 1 11  ? 11.62736  23.04378 11.57715 1.000 57.57793  ? 18  GLU   A CD  1 
ATOM   24   O OE1 . GLU   A 1 11  ? 10.64331  23.78849 11.77045 1.000 49.50315  ? 18  GLU   A OE1 1 
ATOM   25   O OE2 . GLU   A 1 11  ? 12.55762  23.33183 10.79083 1.000 58.31544  ? 18  GLU   A OE2 1 
ATOM   26   N N   . THR   A 1 12  ? 13.53886  20.63825 16.42790 1.000 36.55064  ? 19  THR   A N   1 
ATOM   27   C CA  . THR   A 1 12  ? 14.00929  20.87968 17.78276 1.000 32.18276  ? 19  THR   A CA  1 
ATOM   28   C C   . THR   A 1 12  ? 14.93780  22.08715 17.78744 1.000 32.17553  ? 19  THR   A C   1 
ATOM   29   O O   . THR   A 1 12  ? 15.84336  22.17635 16.95292 1.000 35.25207  ? 19  THR   A O   1 
ATOM   30   C CB  . THR   A 1 12  ? 14.72289  19.64820 18.33994 1.000 32.06097  ? 19  THR   A CB  1 
ATOM   31   O OG1 . THR   A 1 12  ? 13.84036  18.52075 18.28986 1.000 33.28254  ? 19  THR   A OG1 1 
ATOM   32   C CG2 . THR   A 1 12  ? 15.14849  19.88867 19.77269 1.000 31.32268  ? 19  THR   A CG2 1 
ATOM   33   N N   . PHE   A 1 13  ? 14.71630  23.00073 18.73528 1.000 29.41985  ? 20  PHE   A N   1 
ATOM   34   C CA  . PHE   A 1 13  ? 15.48750  24.23249 18.87227 1.000 35.53025  ? 20  PHE   A CA  1 
ATOM   35   C C   . PHE   A 1 13  ? 16.04302  24.34538 20.28408 1.000 39.11027  ? 20  PHE   A C   1 
ATOM   36   O O   . PHE   A 1 13  ? 15.44155  23.84910 21.23871 1.000 30.30723  ? 20  PHE   A O   1 
ATOM   37   C CB  . PHE   A 1 13  ? 14.63070  25.48520 18.59917 1.000 28.40149  ? 20  PHE   A CB  1 
ATOM   38   C CG  . PHE   A 1 13  ? 13.90659  25.45862 17.28374 1.000 31.46024  ? 20  PHE   A CG  1 
ATOM   39   C CD1 . PHE   A 1 13  ? 12.67985  24.81375 17.16029 1.000 40.29173  ? 20  PHE   A CD1 1 
ATOM   40   C CD2 . PHE   A 1 13  ? 14.44020  26.08728 16.16752 1.000 38.29677  ? 20  PHE   A CD2 1 
ATOM   41   C CE1 . PHE   A 1 13  ? 12.00643  24.78938 15.93935 1.000 37.73194  ? 20  PHE   A CE1 1 
ATOM   42   C CE2 . PHE   A 1 13  ? 13.76681  26.06900 14.95455 1.000 35.22295  ? 20  PHE   A CE2 1 
ATOM   43   C CZ  . PHE   A 1 13  ? 12.55519  25.41493 14.84062 1.000 34.20436  ? 20  PHE   A CZ  1 
ATOM   44   N N   . ALA   A 1 14  ? 17.18195  25.02494 20.41487 1.000 34.25244  ? 21  ALA   A N   1 
ATOM   45   C CA  . ALA   A 1 14  ? 17.73217  25.35245 21.72409 1.000 45.06141  ? 21  ALA   A CA  1 
ATOM   46   C C   . ALA   A 1 14  ? 17.23482  26.71854 22.17766 1.000 37.87188  ? 21  ALA   A C   1 
ATOM   47   O O   . ALA   A 1 14  ? 17.12007  27.65130 21.37694 1.000 41.01251  ? 21  ALA   A O   1 
ATOM   48   C CB  . ALA   A 1 14  ? 19.26293  25.34389 21.70286 1.000 39.64713  ? 21  ALA   A CB  1 
ATOM   49   N N   . PHE   A 1 15  ? 16.92490  26.82575 23.46618 1.000 33.69911  ? 22  PHE   A N   1 
ATOM   50   C CA  . PHE   A 1 15  ? 16.63291  28.12101 24.05641 1.000 32.59271  ? 22  PHE   A CA  1 
ATOM   51   C C   . PHE   A 1 15  ? 17.89161  28.97763 24.07012 1.000 28.53759  ? 22  PHE   A C   1 
ATOM   52   O O   . PHE   A 1 15  ? 19.01026  28.47205 24.18854 1.000 32.32161  ? 22  PHE   A O   1 
ATOM   53   C CB  . PHE   A 1 15  ? 16.13863  27.95776 25.49248 1.000 37.46063  ? 22  PHE   A CB  1 
ATOM   54   C CG  . PHE   A 1 15  ? 14.69136  27.58431 25.61186 1.000 43.91053  ? 22  PHE   A CG  1 
ATOM   55   C CD1 . PHE   A 1 15  ? 13.69791  28.45504 25.20116 1.000 29.42919  ? 22  PHE   A CD1 1 
ATOM   56   C CD2 . PHE   A 1 15  ? 14.32249  26.36768 26.17124 1.000 31.43167  ? 22  PHE   A CD2 1 
ATOM   57   C CE1 . PHE   A 1 15  ? 12.36227  28.11322 25.32613 1.000 33.59509  ? 22  PHE   A CE1 1 
ATOM   58   C CE2 . PHE   A 1 15  ? 12.98861  26.02506 26.30673 1.000 27.79342  ? 22  PHE   A CE2 1 
ATOM   59   C CZ  . PHE   A 1 15  ? 12.00834  26.90006 25.87887 1.000 37.23903  ? 22  PHE   A CZ  1 
ATOM   60   N N   . GLN   A 1 16  ? 17.70689  30.28894 23.95863 1.000 36.68195  ? 23  GLN   A N   1 
ATOM   61   C CA  . GLN   A 1 16  ? 18.79976  31.19965 24.26874 1.000 34.10767  ? 23  GLN   A CA  1 
ATOM   62   C C   . GLN   A 1 16  ? 19.27699  30.96807 25.69835 1.000 43.40182  ? 23  GLN   A C   1 
ATOM   63   O O   . GLN   A 1 16  ? 18.48000  30.67465 26.59240 1.000 34.99440  ? 23  GLN   A O   1 
ATOM   64   C CB  . GLN   A 1 16  ? 18.34538  32.64385 24.08063 1.000 42.19975  ? 23  GLN   A CB  1 
ATOM   65   C CG  . GLN   A 1 16  ? 17.94212  32.93811 22.65897 1.000 55.37789  ? 23  GLN   A CG  1 
ATOM   66   C CD  . GLN   A 1 16  ? 16.43602  32.94646 22.46609 1.000 61.89570  ? 23  GLN   A CD  1 
ATOM   67   O OE1 . GLN   A 1 16  ? 15.72839  31.97467 22.80143 1.000 43.94937  ? 23  GLN   A OE1 1 
ATOM   68   N NE2 . GLN   A 1 16  ? 15.93352  34.04732 21.91268 1.000 57.36065  ? 23  GLN   A NE2 1 
ATOM   69   N N   . ALA   A 1 17  ? 20.59150  31.09689 25.90885 1.000 45.24068  ? 24  ALA   A N   1 
ATOM   70   C CA  . ALA   A 1 17  ? 21.18525  30.72491 27.19155 1.000 44.84627  ? 24  ALA   A CA  1 
ATOM   71   C C   . ALA   A 1 17  ? 20.50079  31.42145 28.35881 1.000 38.21009  ? 24  ALA   A C   1 
ATOM   72   O O   . ALA   A 1 17  ? 20.27630  30.80741 29.40998 1.000 42.68762  ? 24  ALA   A O   1 
ATOM   73   C CB  . ALA   A 1 17  ? 22.68221  31.03889 27.19118 1.000 39.30890  ? 24  ALA   A CB  1 
ATOM   74   N N   . GLU   A 1 18  ? 20.15375  32.70306 28.18916 1.000 40.41834  ? 25  GLU   A N   1 
ATOM   75   C CA  . GLU   A 1 18  ? 19.52349  33.45452 29.26929 1.000 43.48175  ? 25  GLU   A CA  1 
ATOM   76   C C   . GLU   A 1 18  ? 18.16253  32.88152 29.63564 1.000 40.05205  ? 25  GLU   A C   1 
ATOM   77   O O   . GLU   A 1 18  ? 17.79471  32.86795 30.81386 1.000 42.18064  ? 25  GLU   A O   1 
ATOM   78   C CB  . GLU   A 1 18  ? 19.37521  34.92802 28.88150 1.000 51.05206  ? 25  GLU   A CB  1 
ATOM   79   C CG  . GLU   A 1 18  ? 20.68403  35.68486 28.69006 1.000 66.89429  ? 25  GLU   A CG  1 
ATOM   80   C CD  . GLU   A 1 18  ? 21.20714  35.60674 27.25715 1.000 74.59676  ? 25  GLU   A CD  1 
ATOM   81   O OE1 . GLU   A 1 18  ? 20.70093  34.76862 26.47131 1.000 53.87452  ? 25  GLU   A OE1 1 
ATOM   82   O OE2 . GLU   A 1 18  ? 22.12672  36.38766 26.91827 1.000 79.12144  ? 25  GLU   A OE2 1 
ATOM   83   N N   . ILE   A 1 19  ? 17.40670  32.40607 28.64936 1.000 39.56919  ? 26  ILE   A N   1 
ATOM   84   C CA  . ILE   A 1 19  ? 16.07589  31.87109 28.91676 1.000 35.52554  ? 26  ILE   A CA  1 
ATOM   85   C C   . ILE   A 1 19  ? 16.15890  30.49399 29.56044 1.000 36.90303  ? 26  ILE   A C   1 
ATOM   86   O O   . ILE   A 1 19  ? 15.39868  30.19008 30.48535 1.000 34.49878  ? 26  ILE   A O   1 
ATOM   87   C CB  . ILE   A 1 19  ? 15.24923  31.84220 27.62059 1.000 31.36780  ? 26  ILE   A CB  1 
ATOM   88   C CG1 . ILE   A 1 19  ? 14.95006  33.27556 27.15836 1.000 31.39489  ? 26  ILE   A CG1 1 
ATOM   89   C CG2 . ILE   A 1 19  ? 13.97189  31.04359 27.83195 1.000 26.30290  ? 26  ILE   A CG2 1 
ATOM   90   C CD1 . ILE   A 1 19  ? 14.16804  33.35889 25.86601 1.000 45.30509  ? 26  ILE   A CD1 1 
ATOM   91   N N   . ALA   A 1 20  ? 17.06667  29.63546 29.08055 1.000 27.94212  ? 27  ALA   A N   1 
ATOM   92   C CA  . ALA   A 1 20  ? 17.26427  28.34261 29.73121 1.000 34.95055  ? 27  ALA   A CA  1 
ATOM   93   C C   . ALA   A 1 20  ? 17.67807  28.52636 31.18513 1.000 31.08459  ? 27  ALA   A C   1 
ATOM   94   O O   . ALA   A 1 20  ? 17.26405  27.76086 32.06269 1.000 33.84985  ? 27  ALA   A O   1 
ATOM   95   C CB  . ALA   A 1 20  ? 18.31045  27.51913 28.97735 1.000 40.16738  ? 27  ALA   A CB  1 
ATOM   96   N N   . GLN   A 1 21  ? 18.47315  29.55757 31.45922 1.000 33.18550  ? 28  GLN   A N   1 
ATOM   97   C CA  . GLN   A 1 21  ? 18.90253  29.82961 32.82599 1.000 33.73700  ? 28  GLN   A CA  1 
ATOM   98   C C   . GLN   A 1 21  ? 17.72422  30.23543 33.71054 1.000 38.10946  ? 28  GLN   A C   1 
ATOM   99   O O   . GLN   A 1 21  ? 17.64679  29.83765 34.88053 1.000 39.79955  ? 28  GLN   A O   1 
ATOM   100  C CB  . GLN   A 1 21  ? 19.97159  30.91735 32.80027 1.000 38.28250  ? 28  GLN   A CB  1 
ATOM   101  C CG  . GLN   A 1 21  ? 20.62751  31.21833 34.11664 1.000 62.70266  ? 28  GLN   A CG  1 
ATOM   102  C CD  . GLN   A 1 21  ? 21.85897  32.07827 33.92757 1.000 79.36984  ? 28  GLN   A CD  1 
ATOM   103  O OE1 . GLN   A 1 21  ? 22.03684  32.69695 32.87081 1.000 56.99033  ? 28  GLN   A OE1 1 
ATOM   104  N NE2 . GLN   A 1 21  ? 22.72120  32.12011 34.94446 1.000 67.33455  ? 28  GLN   A NE2 1 
ATOM   105  N N   . LEU   A 1 22  ? 16.79841  31.03238 33.17458 1.000 31.71496  ? 29  LEU   A N   1 
ATOM   106  C CA  . LEU   A 1 22  ? 15.63551  31.42783 33.96394 1.000 34.40459  ? 29  LEU   A CA  1 
ATOM   107  C C   . LEU   A 1 22  ? 14.69898  30.25110 34.19471 1.000 35.66332  ? 29  LEU   A C   1 
ATOM   108  O O   . LEU   A 1 22  ? 14.14919  30.09833 35.28815 1.000 30.92492  ? 29  LEU   A O   1 
ATOM   109  C CB  . LEU   A 1 22  ? 14.88801  32.56373 33.27932 1.000 33.19019  ? 29  LEU   A CB  1 
ATOM   110  C CG  . LEU   A 1 22  ? 13.52912  32.92101 33.88697 1.000 32.04516  ? 29  LEU   A CG  1 
ATOM   111  C CD1 . LEU   A 1 22  ? 13.69113  33.42319 35.31409 1.000 29.46380  ? 29  LEU   A CD1 1 
ATOM   112  C CD2 . LEU   A 1 22  ? 12.83526  33.96676 33.03656 1.000 47.10635  ? 29  LEU   A CD2 1 
ATOM   113  N N   . MET   A 1 23  ? 14.48901  29.42326 33.16781 1.000 37.10171  ? 30  MET   A N   1 
ATOM   114  C CA  . MET   A 1 23  ? 13.61501  28.26187 33.31415 1.000 41.53190  ? 30  MET   A CA  1 
ATOM   115  C C   . MET   A 1 23  ? 14.14098  27.32098 34.38937 1.000 37.14869  ? 30  MET   A C   1 
ATOM   116  O O   . MET   A 1 23  ? 13.37223  26.79660 35.20518 1.000 39.60127  ? 30  MET   A O   1 
ATOM   117  C CB  . MET   A 1 23  ? 13.48550  27.53585 31.97106 1.000 32.79446  ? 30  MET   A CB  1 
ATOM   118  C CG  . MET   A 1 23  ? 12.67716  28.29471 30.93900 1.000 32.78958  ? 30  MET   A CG  1 
ATOM   119  S SD  . MET   A 1 23  ? 12.66412  27.53531 29.30607 1.000 37.69841  ? 30  MET   A SD  1 
ATOM   120  C CE  . MET   A 1 23  ? 11.18897  26.53085 29.43606 1.000 37.94498  ? 30  MET   A CE  1 
ATOM   121  N N   . SER   A 1 24  ? 15.45518  27.12041 34.42691 1.000 30.96505  ? 31  SER   A N   1 
ATOM   122  C CA  . SER   A 1 24  ? 16.02223  26.26876 35.46117 1.000 38.63596  ? 31  SER   A CA  1 
ATOM   123  C C   . SER   A 1 24  ? 15.87851  26.91189 36.83840 1.000 40.32960  ? 31  SER   A C   1 
ATOM   124  O O   . SER   A 1 24  ? 15.59566  26.22027 37.82194 1.000 40.27411  ? 31  SER   A O   1 
ATOM   125  C CB  . SER   A 1 24  ? 17.47981  25.95313 35.12636 1.000 33.27443  ? 31  SER   A CB  1 
ATOM   126  O OG  . SER   A 1 24  ? 18.20836  25.65588 36.29387 1.000 53.15217  ? 31  SER   A OG  1 
ATOM   127  N N   . LEU   A 1 25  ? 16.02579  28.23825 36.92623 1.000 36.70463  ? 32  LEU   A N   1 
ATOM   128  C CA  . LEU   A 1 25  ? 15.77171  28.92800 38.19161 1.000 35.90070  ? 32  LEU   A CA  1 
ATOM   129  C C   . LEU   A 1 25  ? 14.32968  28.73603 38.65298 1.000 37.14786  ? 32  LEU   A C   1 
ATOM   130  O O   . LEU   A 1 25  ? 14.07597  28.49737 39.83731 1.000 40.72762  ? 32  LEU   A O   1 
ATOM   131  C CB  . LEU   A 1 25  ? 16.09729  30.41895 38.05389 1.000 38.85960  ? 32  LEU   A CB  1 
ATOM   132  C CG  . LEU   A 1 25  ? 16.15230  31.32242 39.29162 1.000 60.77969  ? 32  LEU   A CG  1 
ATOM   133  C CD1 . LEU   A 1 25  ? 16.97059  32.56996 38.98748 1.000 54.85537  ? 32  LEU   A CD1 1 
ATOM   134  C CD2 . LEU   A 1 25  ? 14.75461  31.73806 39.75357 1.000 47.41623  ? 32  LEU   A CD2 1 
ATOM   135  N N   . ILE   A 1 26  ? 13.36958  28.84152 37.73561 1.000 34.27782  ? 33  ILE   A N   1 
ATOM   136  C CA  . ILE   A 1 26  ? 11.96597  28.70921 38.11959 1.000 33.61496  ? 33  ILE   A CA  1 
ATOM   137  C C   . ILE   A 1 26  ? 11.65159  27.27939 38.56287 1.000 42.03019  ? 33  ILE   A C   1 
ATOM   138  O O   . ILE   A 1 26  ? 10.86824  27.06173 39.49573 1.000 31.79058  ? 33  ILE   A O   1 
ATOM   139  C CB  . ILE   A 1 26  ? 11.06270  29.17249 36.96179 1.000 33.26818  ? 33  ILE   A CB  1 
ATOM   140  C CG1 . ILE   A 1 26  ? 11.08836  30.69805 36.85544 1.000 30.02975  ? 33  ILE   A CG1 1 
ATOM   141  C CG2 . ILE   A 1 26  ? 9.62834   28.65591 37.12670 1.000 32.61021  ? 33  ILE   A CG2 1 
ATOM   142  C CD1 . ILE   A 1 26  ? 10.47537  31.20202 35.56293 1.000 43.66910  ? 33  ILE   A CD1 1 
ATOM   143  N N   . ILE   A 1 27  ? 12.27428  26.28314 37.92866 1.000 40.01353  ? 34  ILE   A N   1 
ATOM   144  C CA  . ILE   A 1 27  ? 11.96018  24.89551 38.26860 1.000 38.65594  ? 34  ILE   A CA  1 
ATOM   145  C C   . ILE   A 1 27  ? 12.60177  24.48708 39.58957 1.000 39.67797  ? 34  ILE   A C   1 
ATOM   146  O O   . ILE   A 1 27  ? 12.02026  23.71131 40.35806 1.000 52.25756  ? 34  ILE   A O   1 
ATOM   147  C CB  . ILE   A 1 27  ? 12.38991  23.97304 37.11411 1.000 55.31519  ? 34  ILE   A CB  1 
ATOM   148  C CG1 . ILE   A 1 27  ? 11.42068  24.12801 35.95316 1.000 34.35065  ? 34  ILE   A CG1 1 
ATOM   149  C CG2 . ILE   A 1 27  ? 12.44277  22.51005 37.55775 1.000 49.42540  ? 34  ILE   A CG2 1 
ATOM   150  C CD1 . ILE   A 1 27  ? 12.00080  23.66495 34.67593 1.000 40.78600  ? 34  ILE   A CD1 1 
ATOM   151  N N   . ASN   A 1 28  ? 13.78226  25.01570 39.89744 1.000 44.00064  ? 35  ASN   A N   1 
ATOM   152  C CA  . ASN   A 1 28  ? 14.58695  24.51446 41.00149 1.000 51.71736  ? 35  ASN   A CA  1 
ATOM   153  C C   . ASN   A 1 28  ? 14.60916  25.41859 42.22657 1.000 54.20298  ? 35  ASN   A C   1 
ATOM   154  O O   . ASN   A 1 28  ? 15.21984  25.04521 43.23467 1.000 48.64561  ? 35  ASN   A O   1 
ATOM   155  C CB  . ASN   A 1 28  ? 16.01955  24.26612 40.51826 1.000 45.58997  ? 35  ASN   A CB  1 
ATOM   156  C CG  . ASN   A 1 28  ? 16.08160  23.20207 39.44880 1.000 41.90155  ? 35  ASN   A CG  1 
ATOM   157  O OD1 . ASN   A 1 28  ? 16.44259  23.47275 38.30482 1.000 50.63581  ? 35  ASN   A OD1 1 
ATOM   158  N ND2 . ASN   A 1 28  ? 15.70495  21.98441 39.81087 1.000 44.13620  ? 35  ASN   A ND2 1 
ATOM   159  N N   . THR   A 1 29  ? 13.97872  26.58966 42.18133 1.000 46.41868  ? 36  THR   A N   1 
ATOM   160  C CA  . THR   A 1 29  ? 13.94140  27.45963 43.35103 1.000 46.65352  ? 36  THR   A CA  1 
ATOM   161  C C   . THR   A 1 29  ? 12.74955  27.10331 44.22887 1.000 45.05217  ? 36  THR   A C   1 
ATOM   162  O O   . THR   A 1 29  ? 11.64462  26.85127 43.73872 1.000 42.75974  ? 36  THR   A O   1 
ATOM   163  C CB  . THR   A 1 29  ? 13.89365  28.94093 42.95050 1.000 54.82005  ? 36  THR   A CB  1 
ATOM   164  O OG1 . THR   A 1 29  ? 15.18159  29.34581 42.47293 1.000 54.77008  ? 36  THR   A OG1 1 
ATOM   165  C CG2 . THR   A 1 29  ? 13.51832  29.83261 44.13063 1.000 52.00692  ? 36  THR   A CG2 1 
ATOM   166  N N   . PHE   A 1 30  ? 12.99944  27.04003 45.52981 1.000 39.58237  ? 37  PHE   A N   1 
ATOM   167  C CA  . PHE   A 1 30  ? 11.93225  26.84853 46.49594 1.000 48.43000  ? 37  PHE   A CA  1 
ATOM   168  C C   . PHE   A 1 30  ? 11.10362  28.12380 46.59390 1.000 48.44451  ? 37  PHE   A C   1 
ATOM   169  O O   . PHE   A 1 30  ? 11.60908  29.16709 47.02323 1.000 45.67920  ? 37  PHE   A O   1 
ATOM   170  C CB  . PHE   A 1 30  ? 12.52695  26.48607 47.85196 1.000 42.94235  ? 37  PHE   A CB  1 
ATOM   171  C CG  . PHE   A 1 30  ? 11.50776  26.09787 48.86985 1.000 44.89253  ? 37  PHE   A CG  1 
ATOM   172  C CD1 . PHE   A 1 30  ? 10.98208  24.81548 48.88177 1.000 53.18498  ? 37  PHE   A CD1 1 
ATOM   173  C CD2 . PHE   A 1 30  ? 11.06582  27.01100 49.81453 1.000 44.88947  ? 37  PHE   A CD2 1 
ATOM   174  C CE1 . PHE   A 1 30  ? 10.04009  24.44002 49.82825 1.000 54.76570  ? 37  PHE   A CE1 1 
ATOM   175  C CE2 . PHE   A 1 30  ? 10.11542  26.64486 50.75971 1.000 57.01512  ? 37  PHE   A CE2 1 
ATOM   176  C CZ  . PHE   A 1 30  ? 9.60549   25.35276 50.76688 1.000 48.67691  ? 37  PHE   A CZ  1 
ATOM   177  N N   . TYR   A 1 31  ? 9.83963   28.04787 46.18162 1.000 45.78628  ? 38  TYR   A N   1 
ATOM   178  C CA  . TYR   A 1 31  ? 8.96277   29.21908 46.18153 1.000 37.78676  ? 38  TYR   A CA  1 
ATOM   179  C C   . TYR   A 1 31  ? 7.53053   28.71469 46.29163 1.000 37.79245  ? 38  TYR   A C   1 
ATOM   180  O O   . TYR   A 1 31  ? 7.01628   28.11398 45.34620 1.000 39.72202  ? 38  TYR   A O   1 
ATOM   181  C CB  . TYR   A 1 31  ? 9.16187   30.05238 44.91955 1.000 36.48580  ? 38  TYR   A CB  1 
ATOM   182  C CG  . TYR   A 1 31  ? 8.32108   31.31039 44.90377 1.000 43.84840  ? 38  TYR   A CG  1 
ATOM   183  C CD1 . TYR   A 1 31  ? 8.62340   32.37505 45.74482 1.000 41.42426  ? 38  TYR   A CD1 1 
ATOM   184  C CD2 . TYR   A 1 31  ? 7.21854   31.42938 44.06590 1.000 40.22889  ? 38  TYR   A CD2 1 
ATOM   185  C CE1 . TYR   A 1 31  ? 7.86039   33.52137 45.75207 1.000 49.01052  ? 38  TYR   A CE1 1 
ATOM   186  C CE2 . TYR   A 1 31  ? 6.43873   32.58039 44.06983 1.000 40.06968  ? 38  TYR   A CE2 1 
ATOM   187  C CZ  . TYR   A 1 31  ? 6.77201   33.62033 44.91278 1.000 37.45525  ? 38  TYR   A CZ  1 
ATOM   188  O OH  . TYR   A 1 31  ? 6.01729   34.76856 44.93447 1.000 55.17314  ? 38  TYR   A OH  1 
ATOM   189  N N   . SER   A 1 32  ? 6.89396   28.95464 47.43824 1.000 39.33352  ? 39  SER   A N   1 
ATOM   190  C CA  . SER   A 1 32  ? 5.62728   28.30457 47.75079 1.000 39.72417  ? 39  SER   A CA  1 
ATOM   191  C C   . SER   A 1 32  ? 4.42993   28.96456 47.08723 1.000 45.64430  ? 39  SER   A C   1 
ATOM   192  O O   . SER   A 1 32  ? 3.39625   28.30794 46.92528 1.000 39.33118  ? 39  SER   A O   1 
ATOM   193  C CB  . SER   A 1 32  ? 5.41599   28.28419 49.26457 1.000 41.80756  ? 39  SER   A CB  1 
ATOM   194  O OG  . SER   A 1 32  ? 6.33639   27.39741 49.88246 1.000 43.23113  ? 39  SER   A OG  1 
ATOM   195  N N   . ASN   A 1 33  ? 4.54041   30.23826 46.71254 1.000 37.77822  ? 40  ASN   A N   1 
ATOM   196  C CA  . ASN   A 1 33  ? 3.42146   31.00055 46.15582 1.000 40.84518  ? 40  ASN   A CA  1 
ATOM   197  C C   . ASN   A 1 33  ? 3.25811   30.71566 44.65608 1.000 46.05588  ? 40  ASN   A C   1 
ATOM   198  O O   . ASN   A 1 33  ? 3.33838   31.59625 43.79916 1.000 36.46432  ? 40  ASN   A O   1 
ATOM   199  C CB  . ASN   A 1 33  ? 3.63722   32.48230 46.42966 1.000 37.23344  ? 40  ASN   A CB  1 
ATOM   200  C CG  . ASN   A 1 33  ? 2.46984   33.33922 45.98169 1.000 40.75636  ? 40  ASN   A CG  1 
ATOM   201  O OD1 . ASN   A 1 33  ? 1.31271   32.94621 46.11593 1.000 47.32574  ? 40  ASN   A OD1 1 
ATOM   202  N ND2 . ASN   A 1 33  ? 2.76959   34.52564 45.45619 1.000 43.22313  ? 40  ASN   A ND2 1 
ATOM   203  N N   . LYS   A 1 34  ? 3.00882   29.44303 44.34405 1.000 38.38911  ? 41  LYS   A N   1 
ATOM   204  C CA  . LYS   A 1 34  ? 2.98933   29.00892 42.95182 1.000 33.91012  ? 41  LYS   A CA  1 
ATOM   205  C C   . LYS   A 1 34  ? 1.72695   29.41740 42.20533 1.000 32.15432  ? 41  LYS   A C   1 
ATOM   206  O O   . LYS   A 1 34  ? 1.73495   29.42636 40.96819 1.000 32.56011  ? 41  LYS   A O   1 
ATOM   207  C CB  . LYS   A 1 34  ? 3.13016   27.49180 42.87090 1.000 35.97037  ? 41  LYS   A CB  1 
ATOM   208  C CG  . LYS   A 1 34  ? 4.50212   26.97687 43.14868 1.000 31.20946  ? 41  LYS   A CG  1 
ATOM   209  C CD  . LYS   A 1 34  ? 4.45841   25.46983 43.34068 1.000 35.36181  ? 41  LYS   A CD  1 
ATOM   210  C CE  . LYS   A 1 34  ? 5.79564   24.90299 43.76315 1.000 43.85707  ? 41  LYS   A CE  1 
ATOM   211  N NZ  . LYS   A 1 34  ? 6.71329   24.67152 42.60851 1.000 42.57612  ? 41  LYS   A NZ  1 
ATOM   212  N N   . GLU   A 1 35  ? 0.65168   29.76503 42.91827 1.000 32.10027  ? 42  GLU   A N   1 
ATOM   213  C CA  . GLU   A 1 35  ? -0.62105  30.05405 42.26404 1.000 37.38332  ? 42  GLU   A CA  1 
ATOM   214  C C   . GLU   A 1 35  ? -0.54250  31.22413 41.28461 1.000 35.96796  ? 42  GLU   A C   1 
ATOM   215  O O   . GLU   A 1 35  ? -1.43370  31.36377 40.43386 1.000 31.42613  ? 42  GLU   A O   1 
ATOM   216  C CB  . GLU   A 1 35  ? -1.69813  30.33743 43.31295 1.000 32.85835  ? 42  GLU   A CB  1 
ATOM   217  C CG  . GLU   A 1 35  ? -1.59591  31.71722 43.97021 1.000 34.89330  ? 42  GLU   A CG  1 
ATOM   218  C CD  . GLU   A 1 35  ? -2.51572  31.87243 45.17438 1.000 44.84975  ? 42  GLU   A CD  1 
ATOM   219  O OE1 . GLU   A 1 35  ? -2.62250  30.91694 45.97033 1.000 41.59124  ? 42  GLU   A OE1 1 
ATOM   220  O OE2 . GLU   A 1 35  ? -3.12426  32.95156 45.33190 1.000 49.08568  ? 42  GLU   A OE2 1 
ATOM   221  N N   . ILE   A 1 36  ? 0.50260   32.05261 41.36506 1.000 35.53310  ? 43  ILE   A N   1 
ATOM   222  C CA  . ILE   A 1 36  ? 0.57900   33.22844 40.50508 1.000 28.33296  ? 43  ILE   A CA  1 
ATOM   223  C C   . ILE   A 1 36  ? 0.70425   32.86315 39.03349 1.000 39.40370  ? 43  ILE   A C   1 
ATOM   224  O O   . ILE   A 1 36  ? 0.48628   33.72317 38.17094 1.000 33.83477  ? 43  ILE   A O   1 
ATOM   225  C CB  . ILE   A 1 36  ? 1.73505   34.15519 40.94714 1.000 34.38611  ? 43  ILE   A CB  1 
ATOM   226  C CG1 . ILE   A 1 36  ? 3.09006   33.45183 40.83209 1.000 38.38862  ? 43  ILE   A CG1 1 
ATOM   227  C CG2 . ILE   A 1 36  ? 1.49072   34.66432 42.35866 1.000 36.83422  ? 43  ILE   A CG2 1 
ATOM   228  C CD1 . ILE   A 1 36  ? 3.84716   33.75440 39.53880 1.000 35.92070  ? 43  ILE   A CD1 1 
ATOM   229  N N   . PHE   A 1 37  ? 1.03484   31.60241 38.71200 1.000 31.31565  ? 44  PHE   A N   1 
ATOM   230  C CA  . PHE   A 1 37  ? 1.13942   31.22116 37.30705 1.000 27.16427  ? 44  PHE   A CA  1 
ATOM   231  C C   . PHE   A 1 37  ? -0.16801  31.46452 36.56521 1.000 28.86527  ? 44  PHE   A C   1 
ATOM   232  O O   . PHE   A 1 37  ? -0.14624  31.80993 35.37920 1.000 28.02482  ? 44  PHE   A O   1 
ATOM   233  C CB  . PHE   A 1 37  ? 1.54476   29.74634 37.16484 1.000 30.17529  ? 44  PHE   A CB  1 
ATOM   234  C CG  . PHE   A 1 37  ? 0.38369   28.79126 37.29249 1.000 28.44378  ? 44  PHE   A CG  1 
ATOM   235  C CD1 . PHE   A 1 37  ? -0.37246  28.43758 36.18332 1.000 28.71571  ? 44  PHE   A CD1 1 
ATOM   236  C CD2 . PHE   A 1 37  ? 0.02901   28.27497 38.52772 1.000 26.09064  ? 44  PHE   A CD2 1 
ATOM   237  C CE1 . PHE   A 1 37  ? -1.45168  27.58212 36.30362 1.000 27.82608  ? 44  PHE   A CE1 1 
ATOM   238  C CE2 . PHE   A 1 37  ? -1.04349  27.41358 38.65265 1.000 33.87800  ? 44  PHE   A CE2 1 
ATOM   239  C CZ  . PHE   A 1 37  ? -1.78969  27.07554 37.54107 1.000 28.74523  ? 44  PHE   A CZ  1 
ATOM   240  N N   . LEU   A 1 38  ? -1.31110  31.28198 37.23914 1.000 31.46151  ? 45  LEU   A N   1 
ATOM   241  C CA  . LEU   A 1 38  ? -2.60327  31.42227 36.57090 1.000 30.23112  ? 45  LEU   A CA  1 
ATOM   242  C C   . LEU   A 1 38  ? -2.88542  32.87557 36.22108 1.000 32.53993  ? 45  LEU   A C   1 
ATOM   243  O O   . LEU   A 1 38  ? -3.40703  33.16665 35.14114 1.000 30.37444  ? 45  LEU   A O   1 
ATOM   244  C CB  . LEU   A 1 38  ? -3.72885  30.87094 37.44926 1.000 29.09909  ? 45  LEU   A CB  1 
ATOM   245  C CG  . LEU   A 1 38  ? -5.06408  30.68788 36.72139 1.000 29.62463  ? 45  LEU   A CG  1 
ATOM   246  C CD1 . LEU   A 1 38  ? -4.86726  29.77928 35.50923 1.000 26.11028  ? 45  LEU   A CD1 1 
ATOM   247  C CD2 . LEU   A 1 38  ? -6.14943  30.12558 37.63092 1.000 36.04206  ? 45  LEU   A CD2 1 
ATOM   248  N N   . ARG   A 1 39  ? -2.56512  33.79159 37.13765 1.000 25.82410  ? 46  ARG   A N   1 
ATOM   249  C CA  . ARG   A 1 39  ? -2.65341  35.21776 36.85562 1.000 26.90820  ? 46  ARG   A CA  1 
ATOM   250  C C   . ARG   A 1 39  ? -1.83286  35.59028 35.62879 1.000 29.04648  ? 46  ARG   A C   1 
ATOM   251  O O   . ARG   A 1 39  ? -2.29918  36.34266 34.76652 1.000 33.13227  ? 46  ARG   A O   1 
ATOM   252  C CB  . ARG   A 1 39  ? -2.18145  36.01366 38.07881 1.000 26.37496  ? 46  ARG   A CB  1 
ATOM   253  C CG  . ARG   A 1 39  ? -2.26284  37.53471 37.92746 1.000 36.33088  ? 46  ARG   A CG  1 
ATOM   254  C CD  . ARG   A 1 39  ? -1.60845  38.25386 39.10257 1.000 32.49466  ? 46  ARG   A CD  1 
ATOM   255  N NE  . ARG   A 1 39  ? -0.16694  38.04718 39.15891 1.000 40.46456  ? 46  ARG   A NE  1 
ATOM   256  C CZ  . ARG   A 1 39  ? 0.54984   38.11886 40.27323 1.000 55.58949  ? 46  ARG   A CZ  1 
ATOM   257  N NH1 . ARG   A 1 39  ? -0.01581  38.37619 41.44285 1.000 42.37430  ? 46  ARG   A NH1 1 
ATOM   258  N NH2 . ARG   A 1 39  ? 1.86685   37.93305 40.21288 1.000 43.75341  ? 46  ARG   A NH2 1 
ATOM   259  N N   . GLU   A 1 40  ? -0.60821  35.06022 35.52575 1.000 32.75706  ? 47  GLU   A N   1 
ATOM   260  C CA  . GLU   A 1 40  ? 0.27620   35.45522 34.43160 1.000 26.74442  ? 47  GLU   A CA  1 
ATOM   261  C C   . GLU   A 1 40  ? -0.25500  34.97107 33.08658 1.000 29.59749  ? 47  GLU   A C   1 
ATOM   262  O O   . GLU   A 1 40  ? -0.22643  35.71672 32.09717 1.000 31.81979  ? 47  GLU   A O   1 
ATOM   263  C CB  . GLU   A 1 40  ? 1.69477   34.92368 34.67248 1.000 27.69470  ? 47  GLU   A CB  1 
ATOM   264  C CG  . GLU   A 1 40  ? 2.39293   35.46484 35.93413 1.000 29.89917  ? 47  GLU   A CG  1 
ATOM   265  C CD  . GLU   A 1 40  ? 2.33417   36.98746 36.04358 1.000 40.89801  ? 47  GLU   A CD  1 
ATOM   266  O OE1 . GLU   A 1 40  ? 2.56082   37.65251 35.01408 1.000 37.12386  ? 47  GLU   A OE1 1 
ATOM   267  O OE2 . GLU   A 1 40  ? 2.06499   37.51864 37.15010 1.000 39.13066  ? 47  GLU   A OE2 1 
ATOM   268  N N   . LEU   A 1 41  ? -0.74556  33.72836 33.02926 1.000 27.00184  ? 48  LEU   A N   1 
ATOM   269  C CA  . LEU   A 1 41  ? -1.23086  33.18186 31.76389 1.000 26.81942  ? 48  LEU   A CA  1 
ATOM   270  C C   . LEU   A 1 41  ? -2.54797  33.82627 31.35539 1.000 32.14800  ? 48  LEU   A C   1 
ATOM   271  O O   . LEU   A 1 41  ? -2.79108  34.05656 30.16795 1.000 27.84264  ? 48  LEU   A O   1 
ATOM   272  C CB  . LEU   A 1 41  ? -1.39989  31.66421 31.86881 1.000 27.84613  ? 48  LEU   A CB  1 
ATOM   273  C CG  . LEU   A 1 41  ? -0.12816  30.85331 32.12831 1.000 29.11202  ? 48  LEU   A CG  1 
ATOM   274  C CD1 . LEU   A 1 41  ? -0.44993  29.37185 32.17010 1.000 34.14848  ? 48  LEU   A CD1 1 
ATOM   275  C CD2 . LEU   A 1 41  ? 0.96153   31.13368 31.09002 1.000 28.82841  ? 48  LEU   A CD2 1 
ATOM   276  N N   . ILE   A 1 42  ? -3.42153  34.09943 32.32357 1.000 26.50386  ? 49  ILE   A N   1 
ATOM   277  C CA  . ILE   A 1 42  ? -4.66518  34.79072 32.01698 1.000 28.85717  ? 49  ILE   A CA  1 
ATOM   278  C C   . ILE   A 1 42  ? -4.37213  36.20973 31.53593 1.000 37.76243  ? 49  ILE   A C   1 
ATOM   279  O O   . ILE   A 1 42  ? -5.02154  36.71646 30.61014 1.000 28.80344  ? 49  ILE   A O   1 
ATOM   280  C CB  . ILE   A 1 42  ? -5.58550  34.77955 33.25076 1.000 25.91649  ? 49  ILE   A CB  1 
ATOM   281  C CG1 . ILE   A 1 42  ? -6.17948  33.37807 33.46839 1.000 27.41609  ? 49  ILE   A CG1 1 
ATOM   282  C CG2 . ILE   A 1 42  ? -6.68574  35.83074 33.12668 1.000 26.52042  ? 49  ILE   A CG2 1 
ATOM   283  C CD1 . ILE   A 1 42  ? -7.01489  33.26711 34.74288 1.000 31.49076  ? 49  ILE   A CD1 1 
ATOM   284  N N   . SER   A 1 43  ? -3.37753  36.86254 32.14149 1.000 24.70044  ? 50  SER   A N   1 
ATOM   285  C CA  . SER   A 1 43  ? -3.00026  38.19796 31.69076 1.000 33.97476  ? 50  SER   A CA  1 
ATOM   286  C C   . SER   A 1 43  ? -2.43045  38.15093 30.27830 1.000 27.89102  ? 50  SER   A C   1 
ATOM   287  O O   . SER   A 1 43  ? -2.72163  39.03051 29.46032 1.000 31.08715  ? 50  SER   A O   1 
ATOM   288  C CB  . SER   A 1 43  ? -1.99812  38.82222 32.66613 1.000 28.63131  ? 50  SER   A CB  1 
ATOM   289  O OG  . SER   A 1 43  ? -1.44175  40.01429 32.13527 1.000 46.28732  ? 50  SER   A OG  1 
ATOM   290  N N   . ASN   A 1 44  ? -1.63019  37.12237 29.97219 1.000 32.26269  ? 51  ASN   A N   1 
ATOM   291  C CA  . ASN   A 1 44  ? -1.14357  36.93527 28.60590 1.000 31.45898  ? 51  ASN   A CA  1 
ATOM   292  C C   . ASN   A 1 44  ? -2.30471  36.74245 27.64261 1.000 33.92687  ? 51  ASN   A C   1 
ATOM   293  O O   . ASN   A 1 44  ? -2.31746  37.32039 26.54871 1.000 28.66347  ? 51  ASN   A O   1 
ATOM   294  C CB  . ASN   A 1 44  ? -0.18795  35.73735 28.53537 1.000 23.48231  ? 51  ASN   A CB  1 
ATOM   295  C CG  . ASN   A 1 44  ? 1.20220   36.05661 29.08679 1.000 43.63151  ? 51  ASN   A CG  1 
ATOM   296  O OD1 . ASN   A 1 44  ? 1.46626   37.17786 29.54643 1.000 31.13861  ? 51  ASN   A OD1 1 
ATOM   297  N ND2 . ASN   A 1 44  ? 2.09813   35.06614 29.04713 1.000 27.41024  ? 51  ASN   A ND2 1 
ATOM   298  N N   . SER   A 1 45  ? -3.29826  35.94493 28.04223 1.000 31.99014  ? 52  SER   A N   1 
ATOM   299  C CA  . SER   A 1 45  ? -4.47952  35.74035 27.20897 1.000 23.66876  ? 52  SER   A CA  1 
ATOM   300  C C   . SER   A 1 45  ? -5.22509  37.05272 26.98494 1.000 34.92008  ? 52  SER   A C   1 
ATOM   301  O O   . SER   A 1 45  ? -5.62708  37.36813 25.85928 1.000 30.57226  ? 52  SER   A O   1 
ATOM   302  C CB  . SER   A 1 45  ? -5.39902  34.71191 27.86390 1.000 26.14300  ? 52  SER   A CB  1 
ATOM   303  O OG  . SER   A 1 45  ? -4.89027  33.39897 27.73908 1.000 31.68804  ? 52  SER   A OG  1 
ATOM   304  N N   . SER   A 1 46  ? -5.43263  37.82320 28.06052 1.000 28.59374  ? 53  SER   A N   1 
ATOM   305  C CA  . SER   A 1 46  ? -6.11570  39.11003 27.95733 1.000 25.01892  ? 53  SER   A CA  1 
ATOM   306  C C   . SER   A 1 46  ? -5.39405  40.05642 26.99775 1.000 29.78430  ? 53  SER   A C   1 
ATOM   307  O O   . SER   A 1 46  ? -6.03995  40.77849 26.22817 1.000 33.07933  ? 53  SER   A O   1 
ATOM   308  C CB  . SER   A 1 46  ? -6.24146  39.73814 29.34861 1.000 26.44873  ? 53  SER   A CB  1 
ATOM   309  O OG  . SER   A 1 46  ? -6.91092  40.98857 29.31961 1.000 28.66332  ? 53  SER   A OG  1 
ATOM   310  N N   . ASP   A 1 47  ? -4.05770  40.07094 27.03025 1.000 30.25745  ? 54  ASP   A N   1 
ATOM   311  C CA  . ASP   A 1 47  ? -3.30381  40.89885 26.08924 1.000 32.29401  ? 54  ASP   A CA  1 
ATOM   312  C C   . ASP   A 1 47  ? -3.52065  40.44135 24.64748 1.000 40.55216  ? 54  ASP   A C   1 
ATOM   313  O O   . ASP   A 1 47  ? -3.65026  41.26949 23.73394 1.000 28.61080  ? 54  ASP   A O   1 
ATOM   314  C CB  . ASP   A 1 47  ? -1.81342  40.87005 26.43919 1.000 35.26591  ? 54  ASP   A CB  1 
ATOM   315  C CG  . ASP   A 1 47  ? -1.50135  41.56715 27.76541 1.000 37.25167  ? 54  ASP   A CG  1 
ATOM   316  O OD1 . ASP   A 1 47  ? -2.34002  42.36064 28.24017 1.000 39.13639  ? 54  ASP   A OD1 1 
ATOM   317  O OD2 . ASP   A 1 47  ? -0.41444  41.31737 28.33359 1.000 37.34875  ? 54  ASP   A OD2 1 
ATOM   318  N N   . ALA   A 1 48  ? -3.56393  39.12419 24.42216 1.000 27.77967  ? 55  ALA   A N   1 
ATOM   319  C CA  . ALA   A 1 48  ? -3.76267  38.60443 23.06902 1.000 29.94010  ? 55  ALA   A CA  1 
ATOM   320  C C   . ALA   A 1 48  ? -5.14632  38.96662 22.53853 1.000 33.23348  ? 55  ALA   A C   1 
ATOM   321  O O   . ALA   A 1 48  ? -5.31438  39.27215 21.34753 1.000 25.16614  ? 55  ALA   A O   1 
ATOM   322  C CB  . ALA   A 1 48  ? -3.57284  37.08764 23.06881 1.000 34.18263  ? 55  ALA   A CB  1 
ATOM   323  N N   . LEU   A 1 49  ? -6.14829  38.92085 23.41569 1.000 24.24152  ? 56  LEU   A N   1 
ATOM   324  C CA  . LEU   A 1 49  ? -7.49883  39.32826 23.06450 1.000 29.38180  ? 56  LEU   A CA  1 
ATOM   325  C C   . LEU   A 1 49  ? -7.57367  40.82828 22.78301 1.000 34.68114  ? 56  LEU   A C   1 
ATOM   326  O O   . LEU   A 1 49  ? -8.21976  41.24576 21.81778 1.000 27.54676  ? 56  LEU   A O   1 
ATOM   327  C CB  . LEU   A 1 49  ? -8.44745  38.93135 24.19372 1.000 24.37879  ? 56  LEU   A CB  1 
ATOM   328  C CG  . LEU   A 1 49  ? -8.61222  37.41200 24.27002 1.000 27.06862  ? 56  LEU   A CG  1 
ATOM   329  C CD1 . LEU   A 1 49  ? -9.08855  36.97766 25.64894 1.000 25.94999  ? 56  LEU   A CD1 1 
ATOM   330  C CD2 . LEU   A 1 49  ? -9.59208  36.97370 23.19681 1.000 24.70770  ? 56  LEU   A CD2 1 
ATOM   331  N N   . ASP   A 1 50  ? -6.92032  41.65244 23.61356 1.000 36.17519  ? 57  ASP   A N   1 
ATOM   332  C CA  . ASP   A 1 50  ? -6.83203  43.08411 23.31839 1.000 34.69999  ? 57  ASP   A CA  1 
ATOM   333  C C   . ASP   A 1 50  ? -6.28627  43.32498 21.91359 1.000 32.66198  ? 57  ASP   A C   1 
ATOM   334  O O   . ASP   A 1 50  ? -6.77673  44.19532 21.18039 1.000 30.95041  ? 57  ASP   A O   1 
ATOM   335  C CB  . ASP   A 1 50  ? -5.92772  43.78893 24.33444 1.000 28.82092  ? 57  ASP   A CB  1 
ATOM   336  C CG  . ASP   A 1 50  ? -6.56271  43.93706 25.69267 1.000 36.43552  ? 57  ASP   A CG  1 
ATOM   337  O OD1 . ASP   A 1 50  ? -7.80536  43.86069 25.79214 1.000 37.12072  ? 57  ASP   A OD1 1 
ATOM   338  O OD2 . ASP   A 1 50  ? -5.80357  44.14051 26.66593 1.000 38.44661  ? 57  ASP   A OD2 1 
ATOM   339  N N   . LYS   A 1 51  ? -5.26292  42.56270 21.52691 1.000 28.23916  ? 58  LYS   A N   1 
ATOM   340  C CA  . LYS   A 1 51  ? -4.58813  42.81437 20.25866 1.000 28.47589  ? 58  LYS   A CA  1 
ATOM   341  C C   . LYS   A 1 51  ? -5.50603  42.52574 19.07392 1.000 30.82673  ? 58  LYS   A C   1 
ATOM   342  O O   . LYS   A 1 51  ? -5.60205  43.33470 18.13835 1.000 32.45834  ? 58  LYS   A O   1 
ATOM   343  C CB  . LYS   A 1 51  ? -3.30399  41.98668 20.18461 1.000 33.16907  ? 58  LYS   A CB  1 
ATOM   344  C CG  . LYS   A 1 51  ? -2.48567  42.22927 18.93229 1.000 59.97880  ? 58  LYS   A CG  1 
ATOM   345  C CD  . LYS   A 1 51  ? -0.98125  42.17401 19.19788 1.000 61.99318  ? 58  LYS   A CD  1 
ATOM   346  C CE  . LYS   A 1 51  ? -0.21430  42.73521 17.99615 1.000 63.70765  ? 58  LYS   A CE  1 
ATOM   347  N NZ  . LYS   A 1 51  ? 1.17810   42.21513 17.88324 1.000 67.61436  ? 58  LYS   A NZ  1 
ATOM   348  N N   . ILE   A 1 52  ? -6.20241  41.38656 19.09359 1.000 27.86446  ? 59  ILE   A N   1 
ATOM   349  C CA  . ILE   A 1 52  ? -7.09876  41.08340 17.97689 1.000 27.71310  ? 59  ILE   A CA  1 
ATOM   350  C C   . ILE   A 1 52  ? -8.31239  42.00884 17.99289 1.000 28.23309  ? 59  ILE   A C   1 
ATOM   351  O O   . ILE   A 1 52  ? -8.84911  42.35782 16.93381 1.000 31.08281  ? 59  ILE   A O   1 
ATOM   352  C CB  . ILE   A 1 52  ? -7.51900  39.59873 17.98520 1.000 27.27839  ? 59  ILE   A CB  1 
ATOM   353  C CG1 . ILE   A 1 52  ? -8.25487  39.25266 16.69383 1.000 34.90134  ? 59  ILE   A CG1 1 
ATOM   354  C CG2 . ILE   A 1 52  ? -8.40768  39.27390 19.18951 1.000 30.81452  ? 59  ILE   A CG2 1 
ATOM   355  C CD1 . ILE   A 1 52  ? -7.44192  39.53145 15.45150 1.000 36.90988  ? 59  ILE   A CD1 1 
ATOM   356  N N   . ARG   A 1 53  ? -8.76510  42.42946 19.17818 1.000 29.20876  ? 60  ARG   A N   1 
ATOM   357  C CA  . ARG   A 1 53  ? -9.89124  43.35763 19.23179 1.000 34.78749  ? 60  ARG   A CA  1 
ATOM   358  C C   . ARG   A 1 53  ? -9.53039  44.69419 18.59461 1.000 29.61368  ? 60  ARG   A C   1 
ATOM   359  O O   . ARG   A 1 53  ? -10.33525 45.27719 17.85479 1.000 32.40923  ? 60  ARG   A O   1 
ATOM   360  C CB  . ARG   A 1 53  ? -10.34195 43.56396 20.67368 1.000 29.09004  ? 60  ARG   A CB  1 
ATOM   361  C CG  . ARG   A 1 53  ? -11.48951 44.54206 20.81235 1.000 38.37960  ? 60  ARG   A CG  1 
ATOM   362  C CD  . ARG   A 1 53  ? -11.90044 44.71983 22.26309 1.000 46.07853  ? 60  ARG   A CD  1 
ATOM   363  N NE  . ARG   A 1 53  ? -10.80791 45.23003 23.08410 1.000 64.47138  ? 60  ARG   A NE  1 
ATOM   364  C CZ  . ARG   A 1 53  ? -10.88855 45.43029 24.39359 1.000 71.33020  ? 60  ARG   A CZ  1 
ATOM   365  N NH1 . ARG   A 1 53  ? -12.00168 45.17104 25.06379 1.000 56.98122  ? 60  ARG   A NH1 1 
ATOM   366  N NH2 . ARG   A 1 53  ? -9.82468  45.89962 25.04748 1.000 45.53783  ? 60  ARG   A NH2 1 
ATOM   367  N N   . TYR   A 1 54  ? -8.32221  45.19377 18.87158 1.000 35.43476  ? 61  TYR   A N   1 
ATOM   368  C CA  . TYR   A 1 54  ? -7.88385  46.46114 18.29205 1.000 33.46990  ? 61  TYR   A CA  1 
ATOM   369  C C   . TYR   A 1 54  ? -7.76157  46.36380 16.77656 1.000 31.65392  ? 61  TYR   A C   1 
ATOM   370  O O   . TYR   A 1 54  ? -8.27128  47.22271 16.04552 1.000 32.89102  ? 61  TYR   A O   1 
ATOM   371  C CB  . TYR   A 1 54  ? -6.55309  46.89166 18.90833 1.000 32.79882  ? 61  TYR   A CB  1 
ATOM   372  C CG  . TYR   A 1 54  ? -5.94992  48.12808 18.26108 1.000 38.82515  ? 61  TYR   A CG  1 
ATOM   373  C CD1 . TYR   A 1 54  ? -6.32371  49.40288 18.66733 1.000 48.08296  ? 61  TYR   A CD1 1 
ATOM   374  C CD2 . TYR   A 1 54  ? -4.99448  48.01527 17.25704 1.000 38.29851  ? 61  TYR   A CD2 1 
ATOM   375  C CE1 . TYR   A 1 54  ? -5.77180  50.53490 18.07962 1.000 35.10994  ? 61  TYR   A CE1 1 
ATOM   376  C CE2 . TYR   A 1 54  ? -4.43675  49.13793 16.65983 1.000 43.90889  ? 61  TYR   A CE2 1 
ATOM   377  C CZ  . TYR   A 1 54  ? -4.82785  50.39768 17.07387 1.000 56.60337  ? 61  TYR   A CZ  1 
ATOM   378  O OH  . TYR   A 1 54  ? -4.26424  51.52215 16.47677 1.000 48.56765  ? 61  TYR   A OH  1 
ATOM   379  N N   . GLU   A 1 55  ? -7.07454  45.32644 16.28804 1.000 31.26106  ? 62  GLU   A N   1 
ATOM   380  C CA  . GLU   A 1 55  ? -6.86050  45.18161 14.85134 1.000 35.17868  ? 62  GLU   A CA  1 
ATOM   381  C C   . GLU   A 1 55  ? -8.18110  45.06968 14.10525 1.000 32.90333  ? 62  GLU   A C   1 
ATOM   382  O O   . GLU   A 1 55  ? -8.31926  45.58311 12.98734 1.000 37.86600  ? 62  GLU   A O   1 
ATOM   383  C CB  . GLU   A 1 55  ? -5.98212  43.95993 14.57174 1.000 31.67658  ? 62  GLU   A CB  1 
ATOM   384  C CG  . GLU   A 1 55  ? -4.51453  44.16547 14.91183 1.000 36.12917  ? 62  GLU   A CG  1 
ATOM   385  C CD  . GLU   A 1 55  ? -3.59256  43.12571 14.27859 1.000 64.58348  ? 62  GLU   A CD  1 
ATOM   386  O OE1 . GLU   A 1 55  ? -4.06865  42.31615 13.44851 1.000 49.10308  ? 62  GLU   A OE1 1 
ATOM   387  O OE2 . GLU   A 1 55  ? -2.38599  43.12382 14.61680 1.000 54.33972  ? 62  GLU   A OE2 1 
ATOM   388  N N   . SER   A 1 56  ? -9.17524  44.42584 14.71886 1.000 35.32186  ? 63  SER   A N   1 
ATOM   389  C CA  . SER   A 1 56  ? -10.45498 44.22731 14.04608 1.000 41.56879  ? 63  SER   A CA  1 
ATOM   390  C C   . SER   A 1 56  ? -11.22799 45.52769 13.87547 1.000 45.18542  ? 63  SER   A C   1 
ATOM   391  O O   . SER   A 1 56  ? -12.16969 45.57268 13.07465 1.000 38.72010  ? 63  SER   A O   1 
ATOM   392  C CB  . SER   A 1 56  ? -11.30172 43.21265 14.81253 1.000 42.20323  ? 63  SER   A CB  1 
ATOM   393  O OG  . SER   A 1 56  ? -11.76545 43.76490 16.02843 1.000 43.86494  ? 63  SER   A OG  1 
ATOM   394  N N   . LEU   A 1 57  ? -10.84320 46.58693 14.59325 1.000 44.15834  ? 64  LEU   A N   1 
ATOM   395  C CA  . LEU   A 1 57  ? -11.51107 47.87438 14.42341 1.000 52.09289  ? 64  LEU   A CA  1 
ATOM   396  C C   . LEU   A 1 57  ? -11.26704 48.45100 13.03325 1.000 50.46633  ? 64  LEU   A C   1 
ATOM   397  O O   . LEU   A 1 57  ? -12.18330 49.00744 12.41551 1.000 58.00955  ? 64  LEU   A O   1 
ATOM   398  C CB  . LEU   A 1 57  ? -11.04178 48.85923 15.49513 1.000 44.08138  ? 64  LEU   A CB  1 
ATOM   399  C CG  . LEU   A 1 57  ? -11.42074 48.52221 16.93271 1.000 50.56140  ? 64  LEU   A CG  1 
ATOM   400  C CD1 . LEU   A 1 57  ? -11.01948 49.66096 17.86912 1.000 47.53291  ? 64  LEU   A CD1 1 
ATOM   401  C CD2 . LEU   A 1 57  ? -12.90721 48.25553 17.00751 1.000 56.21721  ? 64  LEU   A CD2 1 
ATOM   402  N N   . THR   A 1 58  ? -10.03935 48.34747 12.52530 1.000 45.75533  ? 65  THR   A N   1 
ATOM   403  C CA  . THR   A 1 58  ? -9.75957  48.86042 11.18977 1.000 52.71257  ? 65  THR   A CA  1 
ATOM   404  C C   . THR   A 1 58  ? -9.85712  47.79059 10.11171 1.000 53.16376  ? 65  THR   A C   1 
ATOM   405  O O   . THR   A 1 58  ? -9.78535  48.12407 8.92578  1.000 49.12604  ? 65  THR   A O   1 
ATOM   406  C CB  . THR   A 1 58  ? -8.37059  49.51381 11.13462 1.000 43.95306  ? 65  THR   A CB  1 
ATOM   407  O OG1 . THR   A 1 58  ? -7.36155  48.51432 11.27390 1.000 66.10497  ? 65  THR   A OG1 1 
ATOM   408  C CG2 . THR   A 1 58  ? -8.21371  50.52550 12.25168 1.000 48.03195  ? 65  THR   A CG2 1 
ATOM   409  N N   . ASP   A 1 59  ? -10.02495 46.52279 10.48647 1.000 55.12138  ? 66  ASP   A N   1 
ATOM   410  C CA  . ASP   A 1 59  ? -10.13984 45.43158 9.51672  1.000 43.40505  ? 66  ASP   A CA  1 
ATOM   411  C C   . ASP   A 1 59  ? -11.04348 44.35736 10.10231 1.000 51.96059  ? 66  ASP   A C   1 
ATOM   412  O O   . ASP   A 1 59  ? -10.57545 43.37090 10.68648 1.000 40.56562  ? 66  ASP   A O   1 
ATOM   413  C CB  . ASP   A 1 59  ? -8.76079  44.87550 9.15209  1.000 41.81518  ? 66  ASP   A CB  1 
ATOM   414  C CG  . ASP   A 1 59  ? -8.82191  43.81716 8.06076  1.000 60.10384  ? 66  ASP   A CG  1 
ATOM   415  O OD1 . ASP   A 1 59  ? -9.92274  43.57087 7.52360  1.000 55.16719  ? 66  ASP   A OD1 1 
ATOM   416  O OD2 . ASP   A 1 59  ? -7.76420  43.23128 7.73647  1.000 64.37665  ? 66  ASP   A OD2 1 
ATOM   417  N N   . PRO   A 1 60  ? -12.36363 44.51609 9.96842  1.000 44.80100  ? 67  PRO   A N   1 
ATOM   418  C CA  . PRO   A 1 60  ? -13.29396 43.56630 10.60582 1.000 54.05897  ? 67  PRO   A CA  1 
ATOM   419  C C   . PRO   A 1 60  ? -13.16700 42.13552 10.10053 1.000 42.07977  ? 67  PRO   A C   1 
ATOM   420  O O   . PRO   A 1 60  ? -13.57633 41.20335 10.80560 1.000 44.13127  ? 67  PRO   A O   1 
ATOM   421  C CB  . PRO   A 1 60  ? -14.67402 44.15505 10.27469 1.000 44.03676  ? 67  PRO   A CB  1 
ATOM   422  C CG  . PRO   A 1 60  ? -14.41004 45.60581 10.03024 1.000 52.39662  ? 67  PRO   A CG  1 
ATOM   423  C CD  . PRO   A 1 60  ? -13.07911 45.63114 9.32735  1.000 49.15773  ? 67  PRO   A CD  1 
ATOM   424  N N   . SER   A 1 61  ? -12.60970 41.92462 8.90988  1.000 38.80213  ? 68  SER   A N   1 
ATOM   425  C CA  . SER   A 1 61  ? -12.47766 40.56500 8.40888  1.000 38.94127  ? 68  SER   A CA  1 
ATOM   426  C C   . SER   A 1 61  ? -11.51952 39.72953 9.25388  1.000 39.95964  ? 68  SER   A C   1 
ATOM   427  O O   . SER   A 1 61  ? -11.56236 38.49994 9.17987  1.000 43.98644  ? 68  SER   A O   1 
ATOM   428  C CB  . SER   A 1 61  ? -12.03348 40.58376 6.94355  1.000 39.96881  ? 68  SER   A CB  1 
ATOM   429  O OG  . SER   A 1 61  ? -10.69455 41.01854 6.82091  1.000 48.13995  ? 68  SER   A OG  1 
ATOM   430  N N   . LYS   A 1 62  ? -10.67880 40.36002 10.07553 1.000 41.73357  ? 69  LYS   A N   1 
ATOM   431  C CA  . LYS   A 1 62  ? -9.80235  39.60894 10.96880 1.000 38.08635  ? 69  LYS   A CA  1 
ATOM   432  C C   . LYS   A 1 62  ? -10.56837 38.76785 11.98273 1.000 34.54475  ? 69  LYS   A C   1 
ATOM   433  O O   . LYS   A 1 62  ? -9.97356  37.87855 12.59829 1.000 37.39700  ? 69  LYS   A O   1 
ATOM   434  C CB  . LYS   A 1 62  ? -8.84778  40.57773 11.67007 1.000 40.36972  ? 69  LYS   A CB  1 
ATOM   435  C CG  . LYS   A 1 62  ? -7.86633  41.20356 10.68166 1.000 44.33973  ? 69  LYS   A CG  1 
ATOM   436  C CD  . LYS   A 1 62  ? -6.63143  41.76900 11.34497 1.000 42.36760  ? 69  LYS   A CD  1 
ATOM   437  C CE  . LYS   A 1 62  ? -5.77032  42.50273 10.32216 1.000 45.32084  ? 69  LYS   A CE  1 
ATOM   438  N NZ  . LYS   A 1 62  ? -4.52305  43.01968 10.93668 1.000 51.46392  ? 69  LYS   A NZ  1 
ATOM   439  N N   . LEU   A 1 63  ? -11.86568 39.00702 12.15741 1.000 38.62788  ? 70  LEU   A N   1 
ATOM   440  C CA  . LEU   A 1 63  ? -12.70082 38.21473 13.04846 1.000 38.55781  ? 70  LEU   A CA  1 
ATOM   441  C C   . LEU   A 1 63  ? -13.50333 37.15331 12.30380 1.000 43.18242  ? 70  LEU   A C   1 
ATOM   442  O O   . LEU   A 1 63  ? -14.35645 36.50188 12.91387 1.000 39.90381  ? 70  LEU   A O   1 
ATOM   443  C CB  . LEU   A 1 63  ? -13.65276 39.12215 13.83755 1.000 32.87242  ? 70  LEU   A CB  1 
ATOM   444  C CG  . LEU   A 1 63  ? -13.04584 40.07845 14.87183 1.000 37.64664  ? 70  LEU   A CG  1 
ATOM   445  C CD1 . LEU   A 1 63  ? -14.13578 40.93018 15.53505 1.000 32.66064  ? 70  LEU   A CD1 1 
ATOM   446  C CD2 . LEU   A 1 63  ? -12.23437 39.31883 15.92483 1.000 30.28894  ? 70  LEU   A CD2 1 
ATOM   447  N N   . ASP   A 1 64  ? -13.26486 36.98084 10.99669 1.000 36.74362  ? 71  ASP   A N   1 
ATOM   448  C CA  . ASP   A 1 64  ? -13.92148 35.90422 10.25727 1.000 42.02567  ? 71  ASP   A CA  1 
ATOM   449  C C   . ASP   A 1 64  ? -13.59817 34.53516 10.84070 1.000 45.19052  ? 71  ASP   A C   1 
ATOM   450  O O   . ASP   A 1 64  ? -14.39162 33.60061 10.69921 1.000 37.65224  ? 71  ASP   A O   1 
ATOM   451  C CB  . ASP   A 1 64  ? -13.51726 35.95088 8.78568  1.000 38.61330  ? 71  ASP   A CB  1 
ATOM   452  C CG  . ASP   A 1 64  ? -14.09548 37.15074 8.07035  1.000 51.60419  ? 71  ASP   A CG  1 
ATOM   453  O OD1 . ASP   A 1 64  ? -14.96807 37.82592 8.66048  1.000 46.48320  ? 71  ASP   A OD1 1 
ATOM   454  O OD2 . ASP   A 1 64  ? -13.66628 37.42603 6.93426  1.000 48.70891  ? 71  ASP   A OD2 1 
ATOM   455  N N   . SER   A 1 65  ? -12.44593 34.39764 11.49260 1.000 42.43175  ? 72  SER   A N   1 
ATOM   456  C CA  . SER   A 1 65  ? -12.04424 33.15399 12.13057 1.000 34.62749  ? 72  SER   A CA  1 
ATOM   457  C C   . SER   A 1 65  ? -12.59965 33.01115 13.54078 1.000 50.81288  ? 72  SER   A C   1 
ATOM   458  O O   . SER   A 1 65  ? -12.18799 32.09803 14.26238 1.000 40.21425  ? 72  SER   A O   1 
ATOM   459  C CB  . SER   A 1 65  ? -10.51705 33.05603 12.16483 1.000 37.03483  ? 72  SER   A CB  1 
ATOM   460  O OG  . SER   A 1 65  ? -9.94809  34.23263 12.72317 1.000 40.07904  ? 72  SER   A OG  1 
ATOM   461  N N   . GLY   A 1 66  ? -13.50600 33.89844 13.95541 1.000 40.40161  ? 73  GLY   A N   1 
ATOM   462  C CA  . GLY   A 1 66  ? -14.11392 33.80031 15.26555 1.000 33.35234  ? 73  GLY   A CA  1 
ATOM   463  C C   . GLY   A 1 66  ? -14.41811 35.14546 15.89001 1.000 31.93614  ? 73  GLY   A C   1 
ATOM   464  O O   . GLY   A 1 66  ? -13.50108 35.89246 16.24026 1.000 37.99222  ? 73  GLY   A O   1 
ATOM   465  N N   . LYS   A 1 67  ? -15.70440 35.44957 16.06327 1.000 39.19417  ? 74  LYS   A N   1 
ATOM   466  C CA  . LYS   A 1 67  ? -16.11339 36.72676 16.63948 1.000 49.51991  ? 74  LYS   A CA  1 
ATOM   467  C C   . LYS   A 1 67  ? -15.98409 36.75448 18.15892 1.000 46.98346  ? 74  LYS   A C   1 
ATOM   468  O O   . LYS   A 1 67  ? -15.77260 37.82752 18.73488 1.000 41.16014  ? 74  LYS   A O   1 
ATOM   469  C CB  . LYS   A 1 67  ? -17.55537 37.04008 16.24205 1.000 43.71571  ? 74  LYS   A CB  1 
ATOM   470  C CG  . LYS   A 1 67  ? -17.68377 37.73051 14.89222 1.000 60.11734  ? 74  LYS   A CG  1 
ATOM   471  C CD  . LYS   A 1 67  ? -19.03700 38.42194 14.73082 1.000 62.98902  ? 74  LYS   A CD  1 
ATOM   472  C CE  . LYS   A 1 67  ? -19.65151 38.14211 13.36145 1.000 75.84028  ? 74  LYS   A CE  1 
ATOM   473  N NZ  . LYS   A 1 67  ? -21.14404 38.22664 13.36540 1.000 63.60564  ? 74  LYS   A NZ  1 
ATOM   474  N N   . GLU   A 1 68  ? -16.09468 35.60332 18.81587 1.000 34.16899  ? 75  GLU   A N   1 
ATOM   475  C CA  . GLU   A 1 68  ? -16.12813 35.55794 20.27279 1.000 35.13480  ? 75  GLU   A CA  1 
ATOM   476  C C   . GLU   A 1 68  ? -14.73982 35.75867 20.87177 1.000 36.13254  ? 75  GLU   A C   1 
ATOM   477  O O   . GLU   A 1 68  ? -13.77224 35.12230 20.44863 1.000 38.22630  ? 75  GLU   A O   1 
ATOM   478  C CB  . GLU   A 1 68  ? -16.70414 34.22154 20.72659 1.000 37.86066  ? 75  GLU   A CB  1 
ATOM   479  C CG  . GLU   A 1 68  ? -17.78285 33.68805 19.81680 1.000 53.79147  ? 75  GLU   A CG  1 
ATOM   480  C CD  . GLU   A 1 68  ? -19.15698 34.17813 20.20950 1.000 72.49451  ? 75  GLU   A CD  1 
ATOM   481  O OE1 . GLU   A 1 68  ? -20.10792 33.37107 20.16086 1.000 94.29839  ? 75  GLU   A OE1 1 
ATOM   482  O OE2 . GLU   A 1 68  ? -19.28781 35.36643 20.57612 1.000 83.68990  ? 75  GLU   A OE2 1 
ATOM   483  N N   . LEU   A 1 69  ? -14.64596 36.63496 21.87487 1.000 34.23872  ? 76  LEU   A N   1 
ATOM   484  C CA  . LEU   A 1 69  ? -13.39706 36.92125 22.57876 1.000 29.80396  ? 76  LEU   A CA  1 
ATOM   485  C C   . LEU   A 1 69  ? -13.54958 36.46524 24.02734 1.000 31.97082  ? 76  LEU   A C   1 
ATOM   486  O O   . LEU   A 1 69  ? -14.22973 37.12722 24.82013 1.000 32.72726  ? 76  LEU   A O   1 
ATOM   487  C CB  . LEU   A 1 69  ? -13.05471 38.41213 22.51623 1.000 26.92453  ? 76  LEU   A CB  1 
ATOM   488  C CG  . LEU   A 1 69  ? -13.01589 39.10195 21.15131 1.000 42.42470  ? 76  LEU   A CG  1 
ATOM   489  C CD1 . LEU   A 1 69  ? -12.55594 40.56006 21.29610 1.000 31.72236  ? 76  LEU   A CD1 1 
ATOM   490  C CD2 . LEU   A 1 69  ? -12.09762 38.34996 20.20830 1.000 27.76486  ? 76  LEU   A CD2 1 
ATOM   491  N N   . HIS   A 1 70  ? -12.90140 35.35656 24.38710 1.000 29.26656  ? 77  HIS   A N   1 
ATOM   492  C CA  . HIS   A 1 70  ? -13.10880 34.79541 25.71740 1.000 26.36682  ? 77  HIS   A CA  1 
ATOM   493  C C   . HIS   A 1 70  ? -11.90656 33.95822 26.12411 1.000 32.00812  ? 77  HIS   A C   1 
ATOM   494  O O   . HIS   A 1 70  ? -10.98458 33.73597 25.33804 1.000 25.35604  ? 77  HIS   A O   1 
ATOM   495  C CB  . HIS   A 1 70  ? -14.38931 33.95311 25.78106 1.000 36.30679  ? 77  HIS   A CB  1 
ATOM   496  C CG  . HIS   A 1 70  ? -14.41239 32.80688 24.81568 1.000 35.45566  ? 77  HIS   A CG  1 
ATOM   497  N ND1 . HIS   A 1 70  ? -15.36237 32.68931 23.82379 1.000 39.62677  ? 77  HIS   A ND1 1 
ATOM   498  C CD2 . HIS   A 1 70  ? -13.60312 31.72800 24.69019 1.000 34.84619  ? 77  HIS   A CD2 1 
ATOM   499  C CE1 . HIS   A 1 70  ? -15.14160 31.58540 23.13310 1.000 29.30949  ? 77  HIS   A CE1 1 
ATOM   500  N NE2 . HIS   A 1 70  ? -14.07648 30.98644 23.63546 1.000 42.21099  ? 77  HIS   A NE2 1 
ATOM   501  N N   . ILE   A 1 71  ? -11.94086 33.50426 27.38214 1.000 28.73241  ? 78  ILE   A N   1 
ATOM   502  C CA  . ILE   A 1 71  ? -10.92470 32.64954 27.99024 1.000 26.50264  ? 78  ILE   A CA  1 
ATOM   503  C C   . ILE   A 1 71  ? -11.62125 31.46260 28.65330 1.000 27.75896  ? 78  ILE   A C   1 
ATOM   504  O O   . ILE   A 1 71  ? -12.58326 31.64064 29.40961 1.000 31.47568  ? 78  ILE   A O   1 
ATOM   505  C CB  . ILE   A 1 71  ? -10.08499 33.42613 29.02397 1.000 30.35389  ? 78  ILE   A CB  1 
ATOM   506  C CG1 . ILE   A 1 71  ? -9.44788  34.65757 28.37269 1.000 27.48858  ? 78  ILE   A CG1 1 
ATOM   507  C CG2 . ILE   A 1 71  ? -9.04649  32.52019 29.68777 1.000 30.77326  ? 78  ILE   A CG2 1 
ATOM   508  C CD1 . ILE   A 1 71  ? -8.68934  35.56308 29.35203 1.000 26.84997  ? 78  ILE   A CD1 1 
ATOM   509  N N   . ASN   A 1 72  ? -11.13439 30.25615 28.38433 1.000 30.55172  ? 79  ASN   A N   1 
ATOM   510  C CA  . ASN   A 1 72  ? -11.66835 29.04700 28.99640 1.000 27.60385  ? 79  ASN   A CA  1 
ATOM   511  C C   . ASN   A 1 72  ? -10.58262 28.38715 29.83052 1.000 27.14519  ? 79  ASN   A C   1 
ATOM   512  O O   . ASN   A 1 72  ? -9.43149  28.28292 29.39338 1.000 27.26747  ? 79  ASN   A O   1 
ATOM   513  C CB  . ASN   A 1 72  ? -12.17830 28.05980 27.93762 1.000 26.85721  ? 79  ASN   A CB  1 
ATOM   514  C CG  . ASN   A 1 72  ? -13.41918 28.55420 27.22684 1.000 32.26784  ? 79  ASN   A CG  1 
ATOM   515  O OD1 . ASN   A 1 72  ? -14.21345 29.32124 27.78605 1.000 31.08764  ? 79  ASN   A OD1 1 
ATOM   516  N ND2 . ASN   A 1 72  ? -13.60418 28.10759 25.98820 1.000 31.45182  ? 79  ASN   A ND2 1 
ATOM   517  N N   . LEU   A 1 73  ? -10.95299 27.94692 31.03080 1.000 26.29009  ? 80  LEU   A N   1 
ATOM   518  C CA  . LEU   A 1 73  ? -10.07420 27.17876 31.90514 1.000 29.07628  ? 80  LEU   A CA  1 
ATOM   519  C C   . LEU   A 1 73  ? -10.61233 25.75648 31.98420 1.000 29.22879  ? 80  LEU   A C   1 
ATOM   520  O O   . LEU   A 1 73  ? -11.76701 25.55561 32.37638 1.000 29.58905  ? 80  LEU   A O   1 
ATOM   521  C CB  . LEU   A 1 73  ? -10.00052 27.81250 33.29238 1.000 28.85823  ? 80  LEU   A CB  1 
ATOM   522  C CG  . LEU   A 1 73  ? -9.72101  29.31566 33.30676 1.000 31.44340  ? 80  LEU   A CG  1 
ATOM   523  C CD1 . LEU   A 1 73  ? -9.82227  29.82201 34.73322 1.000 32.19627  ? 80  LEU   A CD1 1 
ATOM   524  C CD2 . LEU   A 1 73  ? -8.34318  29.60221 32.70243 1.000 27.73991  ? 80  LEU   A CD2 1 
ATOM   525  N N   . ILE   A 1 74  ? -9.78982  24.78347 31.59200 1.000 28.53855  ? 81  ILE   A N   1 
ATOM   526  C CA  . ILE   A 1 74  ? -10.24064 23.40229 31.40606 1.000 29.05040  ? 81  ILE   A CA  1 
ATOM   527  C C   . ILE   A 1 74  ? -9.35176  22.42751 32.16873 1.000 34.11957  ? 81  ILE   A C   1 
ATOM   528  O O   . ILE   A 1 74  ? -8.34133  21.95389 31.62662 1.000 35.42393  ? 81  ILE   A O   1 
ATOM   529  C CB  . ILE   A 1 74  ? -10.27690 23.02043 29.91950 1.000 30.37805  ? 81  ILE   A CB  1 
ATOM   530  C CG1 . ILE   A 1 74  ? -11.00677 24.08342 29.10578 1.000 29.40116  ? 81  ILE   A CG1 1 
ATOM   531  C CG2 . ILE   A 1 74  ? -10.93504 21.64587 29.73669 1.000 33.58049  ? 81  ILE   A CG2 1 
ATOM   532  C CD1 . ILE   A 1 74  ? -10.98353 23.82225 27.61070 1.000 33.99139  ? 81  ILE   A CD1 1 
ATOM   533  N N   . PRO   A 1 75  ? -9.68668  22.08780 33.40909 1.000 32.76671  ? 82  PRO   A N   1 
ATOM   534  C CA  . PRO   A 1 75  ? -8.91525  21.07253 34.12932 1.000 33.97404  ? 82  PRO   A CA  1 
ATOM   535  C C   . PRO   A 1 75  ? -9.31522  19.67258 33.68912 1.000 38.58828  ? 82  PRO   A C   1 
ATOM   536  O O   . PRO   A 1 75  ? -10.45919 19.41504 33.31512 1.000 36.69147  ? 82  PRO   A O   1 
ATOM   537  C CB  . PRO   A 1 75  ? -9.29498  21.31850 35.59390 1.000 39.35665  ? 82  PRO   A CB  1 
ATOM   538  C CG  . PRO   A 1 75  ? -10.68575 21.86958 35.52236 1.000 33.37941  ? 82  PRO   A CG  1 
ATOM   539  C CD  . PRO   A 1 75  ? -10.81758 22.60112 34.20082 1.000 31.00043  ? 82  PRO   A CD  1 
ATOM   540  N N   . ASN   A 1 76  ? -8.34146  18.76486 33.73075 1.000 34.93694  ? 83  ASN   A N   1 
ATOM   541  C CA  . ASN   A 1 76  ? -8.53292  17.37628 33.30801 1.000 34.93239  ? 83  ASN   A CA  1 
ATOM   542  C C   . ASN   A 1 76  ? -7.75389  16.49563 34.27757 1.000 37.11510  ? 83  ASN   A C   1 
ATOM   543  O O   . ASN   A 1 76  ? -6.53371  16.36507 34.15193 1.000 42.65697  ? 83  ASN   A O   1 
ATOM   544  C CB  . ASN   A 1 76  ? -8.06631  17.15822 31.87641 1.000 36.41331  ? 83  ASN   A CB  1 
ATOM   545  C CG  . ASN   A 1 76  ? -8.51047  15.81796 31.31402 1.000 39.37610  ? 83  ASN   A CG  1 
ATOM   546  O OD1 . ASN   A 1 76  ? -8.44978  14.78806 31.98694 1.000 41.04997  ? 83  ASN   A OD1 1 
ATOM   547  N ND2 . ASN   A 1 76  ? -8.95820  15.82969 30.07221 1.000 37.88030  ? 83  ASN   A ND2 1 
ATOM   548  N N   . LYS   A 1 77  ? -8.46480  15.88998 35.23054 1.000 37.71135  ? 84  LYS   A N   1 
ATOM   549  C CA  . LYS   A 1 77  ? -7.80524  15.06628 36.23656 1.000 44.86876  ? 84  LYS   A CA  1 
ATOM   550  C C   . LYS   A 1 77  ? -7.22797  13.78833 35.64114 1.000 50.43269  ? 84  LYS   A C   1 
ATOM   551  O O   . LYS   A 1 77  ? -6.18258  13.31870 36.10528 1.000 40.68212  ? 84  LYS   A O   1 
ATOM   552  C CB  . LYS   A 1 77  ? -8.78015  14.72865 37.36163 1.000 44.25351  ? 84  LYS   A CB  1 
ATOM   553  C CG  . LYS   A 1 77  ? -8.95347  15.84831 38.38349 1.000 55.00876  ? 84  LYS   A CG  1 
ATOM   554  C CD  . LYS   A 1 77  ? -9.91657  15.43840 39.49155 1.000 60.69434  ? 84  LYS   A CD  1 
ATOM   555  C CE  . LYS   A 1 77  ? -10.05449 16.53091 40.54844 1.000 70.57804  ? 84  LYS   A CE  1 
ATOM   556  N NZ  . LYS   A 1 77  ? -11.47896 16.93983 40.75412 1.000 71.77561  ? 84  LYS   A NZ  1 
ATOM   557  N N   . GLN   A 1 78  ? -7.88469  13.21747 34.62241 1.000 54.44883  ? 85  GLN   A N   1 
ATOM   558  C CA  . GLN   A 1 78  ? -7.42565  11.94987 34.05270 1.000 63.87718  ? 85  GLN   A CA  1 
ATOM   559  C C   . GLN   A 1 78  ? -6.07908  12.10955 33.36040 1.000 57.77727  ? 85  GLN   A C   1 
ATOM   560  O O   . GLN   A 1 78  ? -5.19190  11.25931 33.50774 1.000 52.42747  ? 85  GLN   A O   1 
ATOM   561  C CB  . GLN   A 1 78  ? -8.45474  11.39884 33.06335 1.000 62.57431  ? 85  GLN   A CB  1 
ATOM   562  C CG  . GLN   A 1 78  ? -9.66249  10.69321 33.67855 1.000 75.73349  ? 85  GLN   A CG  1 
ATOM   563  C CD  . GLN   A 1 78  ? -10.55452 11.63115 34.47328 1.000 91.98818  ? 85  GLN   A CD  1 
ATOM   564  O OE1 . GLN   A 1 78  ? -10.76696 12.78696 34.08819 1.000 92.24547  ? 85  GLN   A OE1 1 
ATOM   565  N NE2 . GLN   A 1 78  ? -11.08858 11.13583 35.58578 1.000 83.76637  ? 85  GLN   A NE2 1 
ATOM   566  N N   . ASP   A 1 79  ? -5.91871  13.17919 32.58738 1.000 45.14686  ? 86  ASP   A N   1 
ATOM   567  C CA  . ASP   A 1 79  ? -4.65823  13.49835 31.93055 1.000 48.22400  ? 86  ASP   A CA  1 
ATOM   568  C C   . ASP   A 1 79  ? -3.71594  14.30567 32.81275 1.000 51.19138  ? 86  ASP   A C   1 
ATOM   569  O O   . ASP   A 1 79  ? -2.55284  14.49377 32.43553 1.000 46.95176  ? 86  ASP   A O   1 
ATOM   570  C CB  . ASP   A 1 79  ? -4.91764  14.29041 30.64230 1.000 43.61404  ? 86  ASP   A CB  1 
ATOM   571  C CG  . ASP   A 1 79  ? -5.87842  13.58061 29.69812 1.000 64.34462  ? 86  ASP   A CG  1 
ATOM   572  O OD1 . ASP   A 1 79  ? -6.04118  12.34416 29.80970 1.000 57.18457  ? 86  ASP   A OD1 1 
ATOM   573  O OD2 . ASP   A 1 79  ? -6.47768  14.26718 28.84380 1.000 62.45809  ? 86  ASP   A OD2 1 
ATOM   574  N N   . ARG   A 1 80  ? -4.19354  14.79135 33.96200 1.000 38.46149  ? 87  ARG   A N   1 
ATOM   575  C CA  . ARG   A 1 80  ? -3.43843  15.70273 34.82360 1.000 39.12086  ? 87  ARG   A CA  1 
ATOM   576  C C   . ARG   A 1 80  ? -2.98689  16.94873 34.05064 1.000 40.14521  ? 87  ARG   A C   1 
ATOM   577  O O   . ARG   A 1 80  ? -1.81752  17.33637 34.06871 1.000 33.22415  ? 87  ARG   A O   1 
ATOM   578  C CB  . ARG   A 1 80  ? -2.24926  14.99123 35.47131 1.000 47.32977  ? 87  ARG   A CB  1 
ATOM   579  C CG  . ARG   A 1 80  ? -1.84916  15.58298 36.81444 1.000 55.17236  ? 87  ARG   A CG  1 
ATOM   580  C CD  . ARG   A 1 80  ? -0.37019  15.39128 37.09407 1.000 52.87386  ? 87  ARG   A CD  1 
ATOM   581  N NE  . ARG   A 1 80  ? -0.05338  14.02571 37.48843 1.000 54.79305  ? 87  ARG   A NE  1 
ATOM   582  C CZ  . ARG   A 1 80  ? 1.14489   13.46723 37.35959 1.000 62.77233  ? 87  ARG   A CZ  1 
ATOM   583  N NH1 . ARG   A 1 80  ? 2.16630   14.12764 36.83201 1.000 55.41088  ? 87  ARG   A NH1 1 
ATOM   584  N NH2 . ARG   A 1 80  ? 1.32252   12.21407 37.76300 1.000 49.79220  ? 87  ARG   A NH2 1 
ATOM   585  N N   . THR   A 1 81  ? -3.92912  17.58048 33.36073 1.000 39.29902  ? 88  THR   A N   1 
ATOM   586  C CA  . THR   A 1 81  ? -3.62965  18.77827 32.59163 1.000 40.09258  ? 88  THR   A CA  1 
ATOM   587  C C   . THR   A 1 81  ? -4.57445  19.89717 32.98649 1.000 38.11963  ? 88  THR   A C   1 
ATOM   588  O O   . THR   A 1 81  ? -5.74426  19.66980 33.31028 1.000 34.20557  ? 88  THR   A O   1 
ATOM   589  C CB  . THR   A 1 81  ? -3.74710  18.56316 31.07039 1.000 32.55694  ? 88  THR   A CB  1 
ATOM   590  O OG1 . THR   A 1 81  ? -5.10124  18.23415 30.74692 1.000 38.54976  ? 88  THR   A OG1 1 
ATOM   591  C CG2 . THR   A 1 81  ? -2.82051  17.44823 30.59293 1.000 37.29723  ? 88  THR   A CG2 1 
ATOM   592  N N   . LEU   A 1 82  ? -4.04102  21.11099 32.95700 1.000 33.36463  ? 89  LEU   A N   1 
ATOM   593  C CA  . LEU   A 1 82  ? -4.83543  22.32551 33.01905 1.000 33.28189  ? 89  LEU   A CA  1 
ATOM   594  C C   . LEU   A 1 82  ? -4.58344  23.08526 31.72985 1.000 32.60648  ? 89  LEU   A C   1 
ATOM   595  O O   . LEU   A 1 82  ? -3.43574  23.40616 31.40194 1.000 32.97345  ? 89  LEU   A O   1 
ATOM   596  C CB  . LEU   A 1 82  ? -4.48571  23.17310 34.24151 1.000 29.84703  ? 89  LEU   A CB  1 
ATOM   597  C CG  . LEU   A 1 82  ? -5.22691  24.51701 34.32041 1.000 30.61884  ? 89  LEU   A CG  1 
ATOM   598  C CD1 . LEU   A 1 82  ? -6.73352  24.31968 34.41092 1.000 29.44705  ? 89  LEU   A CD1 1 
ATOM   599  C CD2 . LEU   A 1 82  ? -4.73109  25.26670 35.51883 1.000 26.95286  ? 89  LEU   A CD2 1 
ATOM   600  N N   . THR   A 1 83  ? -5.64640  23.33316 30.98655 1.000 28.88174  ? 90  THR   A N   1 
ATOM   601  C CA  . THR   A 1 83  ? -5.56921  24.01217 29.70989 1.000 29.82803  ? 90  THR   A CA  1 
ATOM   602  C C   . THR   A 1 83  ? -6.16704  25.40620 29.84509 1.000 36.20292  ? 90  THR   A C   1 
ATOM   603  O O   . THR   A 1 83  ? -7.28969  25.55995 30.34956 1.000 31.29496  ? 90  THR   A O   1 
ATOM   604  C CB  . THR   A 1 83  ? -6.30793  23.21065 28.64061 1.000 27.52451  ? 90  THR   A CB  1 
ATOM   605  O OG1 . THR   A 1 83  ? -5.69938  21.91451 28.50201 1.000 32.31747  ? 90  THR   A OG1 1 
ATOM   606  C CG2 . THR   A 1 83  ? -6.27163  23.93038 27.33838 1.000 31.58174  ? 90  THR   A CG2 1 
ATOM   607  N N   . ILE   A 1 84  ? -5.41447  26.41631 29.41389 1.000 29.65301  ? 91  ILE   A N   1 
ATOM   608  C CA  . ILE   A 1 84  ? -5.92154  27.78410 29.29991 1.000 30.76949  ? 91  ILE   A CA  1 
ATOM   609  C C   . ILE   A 1 84  ? -6.09122  28.10038 27.81534 1.000 34.44482  ? 91  ILE   A C   1 
ATOM   610  O O   . ILE   A 1 84  ? -5.10716  28.13050 27.06633 1.000 28.96584  ? 91  ILE   A O   1 
ATOM   611  C CB  . ILE   A 1 84  ? -4.99706  28.80855 29.97324 1.000 25.87869  ? 91  ILE   A CB  1 
ATOM   612  C CG1 . ILE   A 1 84  ? -4.96872  28.60704 31.48633 1.000 40.90825  ? 91  ILE   A CG1 1 
ATOM   613  C CG2 . ILE   A 1 84  ? -5.49924  30.21846 29.69397 1.000 25.07262  ? 91  ILE   A CG2 1 
ATOM   614  C CD1 . ILE   A 1 84  ? -3.79825  27.79222 31.97797 1.000 44.28717  ? 91  ILE   A CD1 1 
ATOM   615  N N   . VAL   A 1 85  ? -7.32928  28.36466 27.39713 1.000 24.58523  ? 92  VAL   A N   1 
ATOM   616  C CA  . VAL   A 1 85  ? -7.66527  28.63482 26.00092 1.000 24.01830  ? 92  VAL   A CA  1 
ATOM   617  C C   . VAL   A 1 85  ? -8.15118  30.07036 25.87387 1.000 38.80022  ? 92  VAL   A C   1 
ATOM   618  O O   . VAL   A 1 85  ? -9.04621  30.48550 26.61982 1.000 26.85860  ? 92  VAL   A O   1 
ATOM   619  C CB  . VAL   A 1 85  ? -8.76023  27.69021 25.47890 1.000 25.48506  ? 92  VAL   A CB  1 
ATOM   620  C CG1 . VAL   A 1 85  ? -8.97921  27.93932 23.97267 1.000 25.41224  ? 92  VAL   A CG1 1 
ATOM   621  C CG2 . VAL   A 1 85  ? -8.41025  26.24536 25.75134 1.000 42.27552  ? 92  VAL   A CG2 1 
ATOM   622  N N   . ASP   A 1 86  ? -7.60284  30.81031 24.89905 1.000 25.69434  ? 93  ASP   A N   1 
ATOM   623  C CA  . ASP   A 1 86  ? -8.14183  32.11325 24.52950 1.000 28.12090  ? 93  ASP   A CA  1 
ATOM   624  C C   . ASP   A 1 86  ? -8.36578  32.16628 23.02170 1.000 30.14055  ? 93  ASP   A C   1 
ATOM   625  O O   . ASP   A 1 86  ? -7.80616  31.37573 22.25402 1.000 34.52888  ? 93  ASP   A O   1 
ATOM   626  C CB  . ASP   A 1 86  ? -7.23073  33.27528 25.00114 1.000 29.82501  ? 93  ASP   A CB  1 
ATOM   627  C CG  . ASP   A 1 86  ? -5.85704  33.27621 24.33760 1.000 29.16585  ? 93  ASP   A CG  1 
ATOM   628  O OD1 . ASP   A 1 86  ? -5.75736  33.65064 23.14687 1.000 38.46713  ? 93  ASP   A OD1 1 
ATOM   629  O OD2 . ASP   A 1 86  ? -4.86246  32.91778 25.01388 1.000 36.04592  ? 93  ASP   A OD2 1 
ATOM   630  N N   . THR   A 1 87  ? -9.22692  33.08385 22.59894 1.000 29.82793  ? 94  THR   A N   1 
ATOM   631  C CA  . THR   A 1 87  ? -9.43212  33.35924 21.18014 1.000 28.68777  ? 94  THR   A CA  1 
ATOM   632  C C   . THR   A 1 87  ? -8.78057  34.68244 20.78104 1.000 26.49360  ? 94  THR   A C   1 
ATOM   633  O O   . THR   A 1 87  ? -9.32150  35.44874 19.98242 1.000 32.65527  ? 94  THR   A O   1 
ATOM   634  C CB  . THR   A 1 87  ? -10.91775 33.34622 20.83021 1.000 26.91709  ? 94  THR   A CB  1 
ATOM   635  O OG1 . THR   A 1 87  ? -11.64060 34.14933 21.76487 1.000 26.18133  ? 94  THR   A OG1 1 
ATOM   636  C CG2 . THR   A 1 87  ? -11.46828 31.90889 20.88613 1.000 31.90138  ? 94  THR   A CG2 1 
ATOM   637  N N   . GLY   A 1 88  ? -7.59571  34.95508 21.32483 1.000 29.29280  ? 95  GLY   A N   1 
ATOM   638  C CA  . GLY   A 1 88  ? -6.85895  36.15615 20.95726 1.000 28.42928  ? 95  GLY   A CA  1 
ATOM   639  C C   . GLY   A 1 88  ? -6.24764  36.10875 19.56524 1.000 30.77467  ? 95  GLY   A C   1 
ATOM   640  O O   . GLY   A 1 88  ? -6.71513  35.35765 18.69960 1.000 30.08903  ? 95  GLY   A O   1 
ATOM   641  N N   . ILE   A 1 89  ? -5.18491  36.89118 19.34212 1.000 29.06776  ? 96  ILE   A N   1 
ATOM   642  C CA  . ILE   A 1 89  ? -4.60910  37.01655 18.00166 1.000 26.38476  ? 96  ILE   A CA  1 
ATOM   643  C C   . ILE   A 1 89  ? -3.81503  35.78705 17.55937 1.000 30.34142  ? 96  ILE   A C   1 
ATOM   644  O O   . ILE   A 1 89  ? -3.62403  35.58640 16.35631 1.000 30.69728  ? 96  ILE   A O   1 
ATOM   645  C CB  . ILE   A 1 89  ? -3.70858  38.25740 17.92855 1.000 29.43346  ? 96  ILE   A CB  1 
ATOM   646  C CG1 . ILE   A 1 89  ? -3.32072  38.55864 16.46432 1.000 38.70647  ? 96  ILE   A CG1 1 
ATOM   647  C CG2 . ILE   A 1 89  ? -2.50143  38.04257 18.80047 1.000 29.73648  ? 96  ILE   A CG2 1 
ATOM   648  C CD1 . ILE   A 1 89  ? -2.96381  40.00789 16.17262 1.000 47.88077  ? 96  ILE   A CD1 1 
ATOM   649  N N   . GLY   A 1 90  ? -3.33522  34.96233 18.48548 1.000 26.17918  ? 97  GLY   A N   1 
ATOM   650  C CA  . GLY   A 1 90  ? -2.55358  33.80047 18.11306 1.000 26.31839  ? 97  GLY   A CA  1 
ATOM   651  C C   . GLY   A 1 90  ? -1.12712  34.18193 17.77644 1.000 30.78184  ? 97  GLY   A C   1 
ATOM   652  O O   . GLY   A 1 90  ? -0.73041  35.34884 17.81076 1.000 32.22687  ? 97  GLY   A O   1 
ATOM   653  N N   . MET   A 1 91  ? -0.32625  33.17053 17.45715 1.000 28.77030  ? 98  MET   A N   1 
ATOM   654  C CA  . MET   A 1 91  ? 1.06481   33.40405 17.09859 1.000 27.07721  ? 98  MET   A CA  1 
ATOM   655  C C   . MET   A 1 91  ? 1.43108   32.67958 15.81368 1.000 34.28236  ? 98  MET   A C   1 
ATOM   656  O O   . MET   A 1 91  ? 0.98850   31.55302 15.56724 1.000 30.96736  ? 98  MET   A O   1 
ATOM   657  C CB  . MET   A 1 91  ? 2.01640   32.99382 18.21827 1.000 26.38594  ? 98  MET   A CB  1 
ATOM   658  C CG  . MET   A 1 91  ? 1.66551   33.58882 19.59412 1.000 31.14080  ? 98  MET   A CG  1 
ATOM   659  S SD  . MET   A 1 91  ? 2.62009   32.84056 20.91408 1.000 37.42162  ? 98  MET   A SD  1 
ATOM   660  C CE  . MET   A 1 91  ? 1.56057   31.48621 21.40905 1.000 30.18370  ? 98  MET   A CE  1 
ATOM   661  N N   . THR   A 1 92  ? 2.23887   33.34782 14.99657 1.000 30.17734  ? 99  THR   A N   1 
ATOM   662  C CA  . THR   A 1 92  ? 2.79425   32.75471 13.79369 1.000 35.13114  ? 99  THR   A CA  1 
ATOM   663  C C   . THR   A 1 92  ? 3.97055   31.84086 14.14188 1.000 32.49442  ? 99  THR   A C   1 
ATOM   664  O O   . THR   A 1 92  ? 4.44296   31.78355 15.28366 1.000 36.97977  ? 99  THR   A O   1 
ATOM   665  C CB  . THR   A 1 92  ? 3.26969   33.84170 12.83598 1.000 38.71481  ? 99  THR   A CB  1 
ATOM   666  O OG1 . THR   A 1 92  ? 4.42130   34.48198 13.40770 1.000 37.94733  ? 99  THR   A OG1 1 
ATOM   667  C CG2 . THR   A 1 92  ? 2.17797   34.87550 12.61877 1.000 32.17953  ? 99  THR   A CG2 1 
ATOM   668  N N   . LYS   A 1 93  ? 4.45027   31.12521 13.12925 1.000 34.80245  ? 100 LYS   A N   1 
ATOM   669  C CA  . LYS   A 1 93  ? 5.64899   30.31233 13.30759 1.000 36.57762  ? 100 LYS   A CA  1 
ATOM   670  C C   . LYS   A 1 93  ? 6.84854   31.17130 13.68616 1.000 41.30322  ? 100 LYS   A C   1 
ATOM   671  O O   . LYS   A 1 93  ? 7.62153   30.80796 14.58426 1.000 29.78437  ? 100 LYS   A O   1 
ATOM   672  C CB  . LYS   A 1 93  ? 5.94474   29.51916 12.03345 1.000 33.42740  ? 100 LYS   A CB  1 
ATOM   673  C CG  . LYS   A 1 93  ? 6.96970   28.40844 12.24302 1.000 35.23190  ? 100 LYS   A CG  1 
ATOM   674  C CD  . LYS   A 1 93  ? 7.28465   27.68519 10.95143 1.000 48.51687  ? 100 LYS   A CD  1 
ATOM   675  C CE  . LYS   A 1 93  ? 8.07922   26.41253 11.19583 1.000 41.79736  ? 100 LYS   A CE  1 
ATOM   676  N NZ  . LYS   A 1 93  ? 8.73668   25.93209 9.93506  1.000 58.51077  ? 100 LYS   A NZ  1 
ATOM   677  N N   . ALA   A 1 94  ? 7.01970   32.31684 13.01048 1.000 33.34187  ? 101 ALA   A N   1 
ATOM   678  C CA  . ALA   A 1 94  ? 8.11134   33.22793 13.34677 1.000 34.11434  ? 101 ALA   A CA  1 
ATOM   679  C C   . ALA   A 1 94  ? 8.01776   33.70858 14.79303 1.000 37.15573  ? 101 ALA   A C   1 
ATOM   680  O O   . ALA   A 1 94  ? 9.04190   33.83293 15.47389 1.000 41.06607  ? 101 ALA   A O   1 
ATOM   681  C CB  . ALA   A 1 94  ? 8.12775   34.41607 12.38284 1.000 37.98260  ? 101 ALA   A CB  1 
ATOM   682  N N   . ASP   A 1 95  ? 6.80374   33.99060 15.27842 1.000 36.24416  ? 102 ASP   A N   1 
ATOM   683  C CA  . ASP   A 1 95  ? 6.62548   34.32858 16.69340 1.000 34.84385  ? 102 ASP   A CA  1 
ATOM   684  C C   . ASP   A 1 95  ? 7.15049   33.22023 17.59994 1.000 41.84617  ? 102 ASP   A C   1 
ATOM   685  O O   . ASP   A 1 95  ? 7.91221   33.47958 18.54062 1.000 36.50073  ? 102 ASP   A O   1 
ATOM   686  C CB  . ASP   A 1 95  ? 5.14694   34.57382 17.00436 1.000 33.23521  ? 102 ASP   A CB  1 
ATOM   687  C CG  . ASP   A 1 95  ? 4.63242   35.88867 16.46079 1.000 46.70307  ? 102 ASP   A CG  1 
ATOM   688  O OD1 . ASP   A 1 95  ? 5.43576   36.83854 16.29966 1.000 39.20504  ? 102 ASP   A OD1 1 
ATOM   689  O OD2 . ASP   A 1 95  ? 3.40405   35.96608 16.21149 1.000 38.39912  ? 102 ASP   A OD2 1 
ATOM   690  N N   . LEU   A 1 96  ? 6.72157   31.97199 17.34247 1.000 42.46543  ? 103 LEU   A N   1 
ATOM   691  C CA  . LEU   A 1 96  ? 7.08111   30.84552 18.20220 1.000 33.55620  ? 103 LEU   A CA  1 
ATOM   692  C C   . LEU   A 1 96  ? 8.58338   30.61429 18.22615 1.000 37.32063  ? 103 LEU   A C   1 
ATOM   693  O O   . LEU   A 1 96  ? 9.15441   30.31128 19.27756 1.000 36.57026  ? 103 LEU   A O   1 
ATOM   694  C CB  . LEU   A 1 96  ? 6.37776   29.56983 17.72792 1.000 34.03655  ? 103 LEU   A CB  1 
ATOM   695  C CG  . LEU   A 1 96  ? 4.86349   29.49320 17.90689 1.000 24.72978  ? 103 LEU   A CG  1 
ATOM   696  C CD1 . LEU   A 1 96  ? 4.32197   28.18048 17.34035 1.000 26.59841  ? 103 LEU   A CD1 1 
ATOM   697  C CD2 . LEU   A 1 96  ? 4.49678   29.64233 19.38877 1.000 26.66561  ? 103 LEU   A CD2 1 
ATOM   698  N N   . ILE   A 1 97  ? 9.23619   30.72684 17.07316 1.000 30.53587  ? 104 ILE   A N   1 
ATOM   699  C CA  . ILE   A 1 97  ? 10.64609  30.37939 16.94805 1.000 32.67937  ? 104 ILE   A CA  1 
ATOM   700  C C   . ILE   A 1 97  ? 11.55406  31.57678 17.21499 1.000 43.17400  ? 104 ILE   A C   1 
ATOM   701  O O   . ILE   A 1 97  ? 12.52059  31.46997 17.97455 1.000 42.73951  ? 104 ILE   A O   1 
ATOM   702  C CB  . ILE   A 1 97  ? 10.90493  29.77251 15.55284 1.000 31.64345  ? 104 ILE   A CB  1 
ATOM   703  C CG1 . ILE   A 1 97  ? 10.19190  28.42002 15.42832 1.000 37.35039  ? 104 ILE   A CG1 1 
ATOM   704  C CG2 . ILE   A 1 97  ? 12.39880  29.63260 15.29246 1.000 45.33527  ? 104 ILE   A CG2 1 
ATOM   705  C CD1 . ILE   A 1 97  ? 10.15094  27.86728 13.99882 1.000 35.30470  ? 104 ILE   A CD1 1 
ATOM   706  N N   . ASN   A 1 98  ? 11.26727  32.73704 16.61399 1.000 43.33624  ? 105 ASN   A N   1 
ATOM   707  C CA  . ASN   A 1 98  ? 12.19948  33.86612 16.60366 1.000 37.80856  ? 105 ASN   A CA  1 
ATOM   708  C C   . ASN   A 1 98  ? 11.75132  35.03014 17.48270 1.000 38.68582  ? 105 ASN   A C   1 
ATOM   709  O O   . ASN   A 1 98  ? 12.47082  35.41589 18.40721 1.000 36.07120  ? 105 ASN   A O   1 
ATOM   710  C CB  . ASN   A 1 98  ? 12.41589  34.37329 15.16436 1.000 41.79026  ? 105 ASN   A CB  1 
ATOM   711  C CG  . ASN   A 1 98  ? 13.15121  33.37542 14.28540 1.000 55.84958  ? 105 ASN   A CG  1 
ATOM   712  O OD1 . ASN   A 1 98  ? 14.18848  32.83063 14.67177 1.000 71.38358  ? 105 ASN   A OD1 1 
ATOM   713  N ND2 . ASN   A 1 98  ? 12.62194  33.14096 13.08628 1.000 59.64167  ? 105 ASN   A ND2 1 
ATOM   714  N N   . ASN   A 1 99  ? 10.58118  35.61158 17.20642 1.000 43.19134  ? 106 ASN   A N   1 
ATOM   715  C CA  . ASN   A 1 99  ? 10.27406  36.96062 17.68498 1.000 43.71920  ? 106 ASN   A CA  1 
ATOM   716  C C   . ASN   A 1 99  ? 10.13290  37.00620 19.20176 1.000 50.70244  ? 106 ASN   A C   1 
ATOM   717  O O   . ASN   A 1 99  ? 10.80225  37.79413 19.87704 1.000 66.37365  ? 106 ASN   A O   1 
ATOM   718  C CB  . ASN   A 1 99  ? 8.99504   37.48428 17.02447 1.000 40.32479  ? 106 ASN   A CB  1 
ATOM   719  C CG  . ASN   A 1 99  ? 9.05814   37.47704 15.50795 1.000 50.70047  ? 106 ASN   A CG  1 
ATOM   720  O OD1 . ASN   A 1 99  ? 10.12804  37.59806 14.90715 1.000 46.10666  ? 106 ASN   A OD1 1 
ATOM   721  N ND2 . ASN   A 1 99  ? 7.89043   37.36926 14.87660 1.000 48.58121  ? 106 ASN   A ND2 1 
ATOM   722  N N   . LEU   A 1 100 ? 9.24773   36.17445 19.75144 1.000 43.78241  ? 107 LEU   A N   1 
ATOM   723  C CA  . LEU   A 1 100 ? 8.93785   36.25541 21.17385 1.000 39.09030  ? 107 LEU   A CA  1 
ATOM   724  C C   . LEU   A 1 100 ? 10.16553  35.96465 22.02604 1.000 35.03941  ? 107 LEU   A C   1 
ATOM   725  O O   . LEU   A 1 100 ? 10.36008  36.58439 23.07709 1.000 38.01579  ? 107 LEU   A O   1 
ATOM   726  C CB  . LEU   A 1 100 ? 7.79575   35.29902 21.51594 1.000 35.94758  ? 107 LEU   A CB  1 
ATOM   727  C CG  . LEU   A 1 100 ? 6.38933   35.91259 21.53399 1.000 59.32421  ? 107 LEU   A CG  1 
ATOM   728  C CD1 . LEU   A 1 100 ? 6.07607   36.68739 20.27419 1.000 43.87506  ? 107 LEU   A CD1 1 
ATOM   729  C CD2 . LEU   A 1 100 ? 5.34699   34.83712 21.74226 1.000 55.03802  ? 107 LEU   A CD2 1 
ATOM   730  N N   . GLY   A 1 101 ? 11.01870  35.04009 21.57922 1.000 37.06979  ? 108 GLY   A N   1 
ATOM   731  C CA  . GLY   A 1 101 ? 12.20475  34.71213 22.35251 1.000 33.61098  ? 108 GLY   A CA  1 
ATOM   732  C C   . GLY   A 1 101 ? 13.25863  35.80203 22.29123 1.000 44.56692  ? 108 GLY   A C   1 
ATOM   733  O O   . GLY   A 1 101 ? 13.99242  36.02678 23.25849 1.000 37.70546  ? 108 GLY   A O   1 
ATOM   734  N N   . THR   A 1 102 ? 13.35989  36.48208 21.14893 1.000 34.73982  ? 109 THR   A N   1 
ATOM   735  C CA  . THR   A 1 102 ? 14.25995  37.62400 21.04960 1.000 37.79483  ? 109 THR   A CA  1 
ATOM   736  C C   . THR   A 1 102 ? 13.86766  38.71230 22.03816 1.000 50.59655  ? 109 THR   A C   1 
ATOM   737  O O   . THR   A 1 102 ? 14.72940  39.30924 22.69388 1.000 41.19747  ? 109 THR   A O   1 
ATOM   738  C CB  . THR   A 1 102 ? 14.25745  38.16671 19.62315 1.000 41.32095  ? 109 THR   A CB  1 
ATOM   739  O OG1 . THR   A 1 102 ? 14.74644  37.15690 18.72999 1.000 44.50465  ? 109 THR   A OG1 1 
ATOM   740  C CG2 . THR   A 1 102 ? 15.12186  39.41212 19.52011 1.000 43.31933  ? 109 THR   A CG2 1 
ATOM   741  N N   . ILE   A 1 103 ? 12.56665  38.96802 22.17567 1.000 36.94114  ? 110 ILE   A N   1 
ATOM   742  C CA  . ILE   A 1 103 ? 12.10689  39.95370 23.14557 1.000 45.55323  ? 110 ILE   A CA  1 
ATOM   743  C C   . ILE   A 1 103 ? 12.32793  39.44356 24.56655 1.000 47.49781  ? 110 ILE   A C   1 
ATOM   744  O O   . ILE   A 1 103 ? 12.86300  40.15702 25.42219 1.000 53.72820  ? 110 ILE   A O   1 
ATOM   745  C CB  . ILE   A 1 103 ? 10.63329  40.31019 22.88481 1.000 37.97913  ? 110 ILE   A CB  1 
ATOM   746  C CG1 . ILE   A 1 103 ? 10.51857  41.15878 21.62208 1.000 50.26164  ? 110 ILE   A CG1 1 
ATOM   747  C CG2 . ILE   A 1 103 ? 10.04572  41.06078 24.05985 1.000 52.00571  ? 110 ILE   A CG2 1 
ATOM   748  C CD1 . ILE   A 1 103 ? 9.13769   41.16333 21.04580 1.000 61.38485  ? 110 ILE   A CD1 1 
ATOM   749  N N   . ALA   A 1 104 ? 11.95284  38.19099 24.83238 1.000 37.29528  ? 111 ALA   A N   1 
ATOM   750  C CA  . ALA   A 1 104 ? 12.12840  37.62929 26.16431 1.000 35.20210  ? 111 ALA   A CA  1 
ATOM   751  C C   . ALA   A 1 104 ? 13.58037  37.65389 26.63240 1.000 53.77561  ? 111 ALA   A C   1 
ATOM   752  O O   . ALA   A 1 104 ? 13.82662  37.49385 27.83209 1.000 42.57834  ? 111 ALA   A O   1 
ATOM   753  C CB  . ALA   A 1 104 ? 11.59826  36.19362 26.20077 1.000 41.21711  ? 111 ALA   A CB  1 
ATOM   754  N N   . LYS   A 1 105 ? 14.54192  37.85256 25.72577 1.000 39.19436  ? 112 LYS   A N   1 
ATOM   755  C CA  . LYS   A 1 105 ? 15.94867  37.81982 26.11363 1.000 44.22317  ? 112 LYS   A CA  1 
ATOM   756  C C   . LYS   A 1 105 ? 16.29138  38.95425 27.07428 1.000 35.60166  ? 112 LYS   A C   1 
ATOM   757  O O   . LYS   A 1 105 ? 16.95220  38.73232 28.09209 1.000 44.01810  ? 112 LYS   A O   1 
ATOM   758  C CB  . LYS   A 1 105 ? 16.83277  37.87484 24.86542 1.000 43.02638  ? 112 LYS   A CB  1 
ATOM   759  C CG  . LYS   A 1 105 ? 18.20428  37.24250 25.03434 1.000 49.28027  ? 112 LYS   A CG  1 
ATOM   760  C CD  . LYS   A 1 105 ? 19.01423  37.32799 23.74038 1.000 56.00553  ? 112 LYS   A CD  1 
ATOM   761  C CE  . LYS   A 1 105 ? 20.52367  37.30835 24.00441 1.000 74.05052  ? 112 LYS   A CE  1 
ATOM   762  N NZ  . LYS   A 1 105 ? 21.10342  38.67858 24.16009 1.000 70.89685  ? 112 LYS   A NZ  1 
ATOM   763  N N   . SER   A 1 106 ? 15.84254  40.17261 26.78257 1.000 41.10219  ? 113 SER   A N   1 
ATOM   764  C CA  . SER   A 1 106 ? 16.17861  41.29167 27.65310 1.000 45.09011  ? 113 SER   A CA  1 
ATOM   765  C C   . SER   A 1 106 ? 15.35923  41.26824 28.94315 1.000 38.70284  ? 113 SER   A C   1 
ATOM   766  O O   . SER   A 1 106 ? 15.86504  41.63979 30.00748 1.000 48.17741  ? 113 SER   A O   1 
ATOM   767  C CB  . SER   A 1 106 ? 15.98490  42.61033 26.90183 1.000 44.69268  ? 113 SER   A CB  1 
ATOM   768  O OG  . SER   A 1 106 ? 14.61395  42.86831 26.66930 1.000 57.94848  ? 113 SER   A OG  1 
ATOM   769  N N   . GLY   A 1 107 ? 14.10062  40.83408 28.87243 1.000 40.09025  ? 114 GLY   A N   1 
ATOM   770  C CA  . GLY   A 1 107 ? 13.28185  40.78671 30.07142 1.000 44.49390  ? 114 GLY   A CA  1 
ATOM   771  C C   . GLY   A 1 107 ? 13.74511  39.71113 31.03232 1.000 42.52881  ? 114 GLY   A C   1 
ATOM   772  O O   . GLY   A 1 107 ? 13.68218  39.88251 32.25166 1.000 30.92243  ? 114 GLY   A O   1 
ATOM   773  N N   . THR   A 1 108 ? 14.22605  38.59305 30.49288 1.000 39.52317  ? 115 THR   A N   1 
ATOM   774  C CA  . THR   A 1 108 ? 14.81560  37.54487 31.31884 1.000 38.62667  ? 115 THR   A CA  1 
ATOM   775  C C   . THR   A 1 108 ? 16.04290  38.05528 32.06309 1.000 38.09879  ? 115 THR   A C   1 
ATOM   776  O O   . THR   A 1 108 ? 16.20274  37.81714 33.26840 1.000 41.43328  ? 115 THR   A O   1 
ATOM   777  C CB  . THR   A 1 108 ? 15.18407  36.34984 30.43765 1.000 39.95277  ? 115 THR   A CB  1 
ATOM   778  O OG1 . THR   A 1 108 ? 13.98886  35.73656 29.94394 1.000 46.19403  ? 115 THR   A OG1 1 
ATOM   779  C CG2 . THR   A 1 108 ? 15.94746  35.34654 31.22860 1.000 42.34107  ? 115 THR   A CG2 1 
ATOM   780  N N   . LYS   A 1 109 ? 16.92669  38.75670 31.35313 1.000 33.95238  ? 116 LYS   A N   1 
ATOM   781  C CA  . LYS   A 1 109 ? 18.11947  39.31492 31.97777 1.000 36.77626  ? 116 LYS   A CA  1 
ATOM   782  C C   . LYS   A 1 109 ? 17.74925  40.29806 33.08505 1.000 43.35459  ? 116 LYS   A C   1 
ATOM   783  O O   . LYS   A 1 109 ? 18.31383  40.25351 34.18333 1.000 43.81497  ? 116 LYS   A O   1 
ATOM   784  C CB  . LYS   A 1 109 ? 18.98905  39.98705 30.91178 1.000 44.15966  ? 116 LYS   A CB  1 
ATOM   785  C CG  . LYS   A 1 109 ? 20.04369  40.95220 31.44171 1.000 50.99974  ? 116 LYS   A CG  1 
ATOM   786  C CD  . LYS   A 1 109 ? 21.14310  41.16768 30.40344 1.000 65.59485  ? 116 LYS   A CD  1 
ATOM   787  C CE  . LYS   A 1 109 ? 22.42861  41.72826 31.01055 1.000 73.66829  ? 116 LYS   A CE  1 
ATOM   788  N NZ  . LYS   A 1 109 ? 22.22549  43.02167 31.72853 1.000 72.43472  ? 116 LYS   A NZ  1 
ATOM   789  N N   . ALA   A 1 110 ? 16.78372  41.18243 32.81935 1.000 40.64312  ? 117 ALA   A N   1 
ATOM   790  C CA  . ALA   A 1 110 ? 16.37145  42.15333 33.82991 1.000 34.37197  ? 117 ALA   A CA  1 
ATOM   791  C C   . ALA   A 1 110 ? 15.66219  41.47582 34.99771 1.000 34.63290  ? 117 ALA   A C   1 
ATOM   792  O O   . ALA   A 1 110 ? 15.84100  41.87741 36.15484 1.000 34.63836  ? 117 ALA   A O   1 
ATOM   793  C CB  . ALA   A 1 110 ? 15.47486  43.22278 33.20379 1.000 32.73232  ? 117 ALA   A CB  1 
ATOM   794  N N   . PHE   A 1 111 ? 14.85289  40.44872 34.72194 1.000 32.46352  ? 118 PHE   A N   1 
ATOM   795  C CA  . PHE   A 1 111 ? 14.17791  39.74960 35.81229 1.000 36.01114  ? 118 PHE   A CA  1 
ATOM   796  C C   . PHE   A 1 111 ? 15.18658  39.08465 36.74490 1.000 35.12460  ? 118 PHE   A C   1 
ATOM   797  O O   . PHE   A 1 111 ? 15.06058  39.16424 37.97410 1.000 35.29656  ? 118 PHE   A O   1 
ATOM   798  C CB  . PHE   A 1 111 ? 13.18061  38.73438 35.24871 1.000 32.62323  ? 118 PHE   A CB  1 
ATOM   799  C CG  . PHE   A 1 111 ? 12.40429  37.98817 36.30579 1.000 41.10792  ? 118 PHE   A CG  1 
ATOM   800  C CD1 . PHE   A 1 111 ? 11.86940  38.65725 37.39354 1.000 41.74933  ? 118 PHE   A CD1 1 
ATOM   801  C CD2 . PHE   A 1 111 ? 12.20302  36.61888 36.20552 1.000 31.14398  ? 118 PHE   A CD2 1 
ATOM   802  C CE1 . PHE   A 1 111 ? 11.15312  37.97604 38.36591 1.000 41.33304  ? 118 PHE   A CE1 1 
ATOM   803  C CE2 . PHE   A 1 111 ? 11.48711  35.93819 37.16550 1.000 36.19896  ? 118 PHE   A CE2 1 
ATOM   804  C CZ  . PHE   A 1 111 ? 10.96375  36.61503 38.25233 1.000 33.66460  ? 118 PHE   A CZ  1 
ATOM   805  N N   . MET   A 1 112 ? 16.22493  38.47001 36.18800 1.000 35.05294  ? 119 MET   A N   1 
ATOM   806  C CA  . MET   A 1 112 ? 17.16913  37.76977 37.04572 1.000 37.95060  ? 119 MET   A CA  1 
ATOM   807  C C   . MET   A 1 112 ? 18.06591  38.74205 37.79259 1.000 33.86395  ? 119 MET   A C   1 
ATOM   808  O O   . MET   A 1 112 ? 18.50203  38.44656 38.90986 1.000 37.31646  ? 119 MET   A O   1 
ATOM   809  C CB  . MET   A 1 112 ? 17.99886  36.79119 36.22309 1.000 50.68747  ? 119 MET   A CB  1 
ATOM   810  C CG  . MET   A 1 112 ? 17.15016  35.69357 35.60919 1.000 50.43167  ? 119 MET   A CG  1 
ATOM   811  S SD  . MET   A 1 112 ? 18.08070  34.18389 35.36933 1.000 55.79887  ? 119 MET   A SD  1 
ATOM   812  C CE  . MET   A 1 112 ? 18.31622  34.22525 33.59770 1.000 51.45605  ? 119 MET   A CE  1 
ATOM   813  N N   . GLU   A 1 113 ? 18.34974  39.90199 37.20255 1.000 44.14621  ? 120 GLU   A N   1 
ATOM   814  C CA  . GLU   A 1 113 ? 19.08513  40.92246 37.93908 1.000 51.09685  ? 120 GLU   A CA  1 
ATOM   815  C C   . GLU   A 1 113 ? 18.25808  41.43917 39.10907 1.000 52.90778  ? 120 GLU   A C   1 
ATOM   816  O O   . GLU   A 1 113 ? 18.79037  41.67320 40.20121 1.000 42.90899  ? 120 GLU   A O   1 
ATOM   817  C CB  . GLU   A 1 113 ? 19.47536  42.06519 37.00484 1.000 52.90410  ? 120 GLU   A CB  1 
ATOM   818  C CG  . GLU   A 1 113 ? 20.83858  41.91323 36.36377 1.000 55.60715  ? 120 GLU   A CG  1 
ATOM   819  C CD  . GLU   A 1 113 ? 20.94710  42.65207 35.04248 1.000 76.21148  ? 120 GLU   A CD  1 
ATOM   820  O OE1 . GLU   A 1 113 ? 20.48255  43.80984 34.96007 1.000 80.29415  ? 120 GLU   A OE1 1 
ATOM   821  O OE2 . GLU   A 1 113 ? 21.49523  42.07122 34.08494 1.000 77.03023  ? 120 GLU   A OE2 1 
ATOM   822  N N   . ALA   A 1 114 ? 16.94888  41.60623 38.89775 1.000 36.80102  ? 121 ALA   A N   1 
ATOM   823  C CA  . ALA   A 1 114 ? 16.06960  42.04273 39.97663 1.000 41.26038  ? 121 ALA   A CA  1 
ATOM   824  C C   . ALA   A 1 114 ? 16.00981  41.01008 41.10089 1.000 55.86454  ? 121 ALA   A C   1 
ATOM   825  O O   . ALA   A 1 114 ? 16.04120  41.37081 42.28447 1.000 51.00736  ? 121 ALA   A O   1 
ATOM   826  C CB  . ALA   A 1 114 ? 14.67246  42.32382 39.42082 1.000 43.20300  ? 121 ALA   A CB  1 
ATOM   827  N N   . LEU   A 1 115 ? 15.92950  39.71788 40.75159 1.000 43.67128  ? 122 LEU   A N   1 
ATOM   828  C CA  . LEU   A 1 115 ? 15.87929  38.66809 41.76893 1.000 41.85696  ? 122 LEU   A CA  1 
ATOM   829  C C   . LEU   A 1 115 ? 17.11748  38.67942 42.65403 1.000 53.35679  ? 122 LEU   A C   1 
ATOM   830  O O   . LEU   A 1 115 ? 17.05112  38.26573 43.81762 1.000 50.10271  ? 122 LEU   A O   1 
ATOM   831  C CB  . LEU   A 1 115 ? 15.70681  37.29623 41.11183 1.000 35.44058  ? 122 LEU   A CB  1 
ATOM   832  C CG  . LEU   A 1 115 ? 14.33286  37.08024 40.46676 1.000 42.15865  ? 122 LEU   A CG  1 
ATOM   833  C CD1 . LEU   A 1 115 ? 14.30627  35.84785 39.56874 1.000 40.03334  ? 122 LEU   A CD1 1 
ATOM   834  C CD2 . LEU   A 1 115 ? 13.23143  36.99608 41.51420 1.000 43.49114  ? 122 LEU   A CD2 1 
ATOM   835  N N   . GLN   A 1 116 ? 18.25072  39.15127 42.13134 1.000 60.19758  ? 123 GLN   A N   1 
ATOM   836  C CA  . GLN   A 1 116 ? 19.42828  39.32762 42.97269 1.000 62.29954  ? 123 GLN   A CA  1 
ATOM   837  C C   . GLN   A 1 116 ? 19.34651  40.57270 43.84135 1.000 57.62319  ? 123 GLN   A C   1 
ATOM   838  O O   . GLN   A 1 116 ? 20.00973  40.63576 44.88259 1.000 62.03769  ? 123 GLN   A O   1 
ATOM   839  C CB  . GLN   A 1 116 ? 20.69169  39.38911 42.12027 1.000 67.97590  ? 123 GLN   A CB  1 
ATOM   840  C CG  . GLN   A 1 116 ? 21.18229  38.04120 41.68717 1.000 72.31796  ? 123 GLN   A CG  1 
ATOM   841  C CD  . GLN   A 1 116 ? 22.40412  37.62332 42.47806 1.000 85.05405  ? 123 GLN   A CD  1 
ATOM   842  O OE1 . GLN   A 1 116 ? 23.04089  38.44611 43.14366 1.000 98.68834  ? 123 GLN   A OE1 1 
ATOM   843  N NE2 . GLN   A 1 116 ? 22.73251  36.33965 42.42346 1.000 88.53652  ? 123 GLN   A NE2 1 
ATOM   844  N N   . ALA   A 1 117 ? 18.56611  41.56997 43.43405 1.000 57.18860  ? 124 ALA   A N   1 
ATOM   845  C CA  . ALA   A 1 117 ? 18.41317  42.78219 44.22857 1.000 67.81047  ? 124 ALA   A CA  1 
ATOM   846  C C   . ALA   A 1 117 ? 17.36433  42.63771 45.32421 1.000 63.55569  ? 124 ALA   A C   1 
ATOM   847  O O   . ALA   A 1 117 ? 17.10854  43.60453 46.04905 1.000 69.16242  ? 124 ALA   A O   1 
ATOM   848  C CB  . ALA   A 1 117 ? 18.06243  43.96296 43.32081 1.000 57.17399  ? 124 ALA   A CB  1 
ATOM   849  N N   . GLY   A 1 118 ? 16.74293  41.46516 45.45056 1.000 63.33010  ? 125 GLY   A N   1 
ATOM   850  C CA  . GLY   A 1 118 ? 15.73106  41.22230 46.45947 1.000 57.61364  ? 125 GLY   A CA  1 
ATOM   851  C C   . GLY   A 1 118 ? 14.32575  41.05540 45.92755 1.000 50.06381  ? 125 GLY   A C   1 
ATOM   852  O O   . GLY   A 1 118 ? 13.42121  40.74588 46.71359 1.000 55.48748  ? 125 GLY   A O   1 
ATOM   853  N N   . ALA   A 1 119 ? 14.10569  41.26076 44.62878 1.000 55.68291  ? 126 ALA   A N   1 
ATOM   854  C CA  . ALA   A 1 119 ? 12.80115  41.01690 44.03434 1.000 45.45755  ? 126 ALA   A CA  1 
ATOM   855  C C   . ALA   A 1 119 ? 12.41271  39.55519 44.21757 1.000 57.48113  ? 126 ALA   A C   1 
ATOM   856  O O   . ALA   A 1 119 ? 13.24642  38.69699 44.51610 1.000 60.88290  ? 126 ALA   A O   1 
ATOM   857  C CB  . ALA   A 1 119 ? 12.80976  41.37262 42.54732 1.000 39.68730  ? 126 ALA   A CB  1 
ATOM   858  N N   . ASP   A 1 120 ? 11.12859  39.26617 44.04408 1.000 45.91094  ? 127 ASP   A N   1 
ATOM   859  C CA  . ASP   A 1 120 ? 10.67200  37.89359 44.17994 1.000 55.46632  ? 127 ASP   A CA  1 
ATOM   860  C C   . ASP   A 1 120 ? 9.93702   37.46928 42.91667 1.000 45.41268  ? 127 ASP   A C   1 
ATOM   861  O O   . ASP   A 1 120 ? 9.58499   38.28596 42.05674 1.000 43.52209  ? 127 ASP   A O   1 
ATOM   862  C CB  . ASP   A 1 120 ? 9.79948   37.69306 45.43262 1.000 50.01277  ? 127 ASP   A CB  1 
ATOM   863  C CG  . ASP   A 1 120 ? 8.38006   38.14965 45.23762 1.000 64.26469  ? 127 ASP   A CG  1 
ATOM   864  O OD1 . ASP   A 1 120 ? 8.14737   39.37728 45.19456 1.000 69.81211  ? 127 ASP   A OD1 1 
ATOM   865  O OD2 . ASP   A 1 120 ? 7.49672   37.27203 45.11443 1.000 70.52695  ? 127 ASP   A OD2 1 
ATOM   866  N N   . ILE   A 1 121 ? 9.70785   36.15743 42.83319 1.000 39.38721  ? 128 ILE   A N   1 
ATOM   867  C CA  . ILE   A 1 121 ? 9.27898   35.52380 41.59196 1.000 40.22362  ? 128 ILE   A CA  1 
ATOM   868  C C   . ILE   A 1 121 ? 7.91149   36.03068 41.15465 1.000 36.93079  ? 128 ILE   A C   1 
ATOM   869  O O   . ILE   A 1 121 ? 7.62676   36.10449 39.95409 1.000 34.72751  ? 128 ILE   A O   1 
ATOM   870  C CB  . ILE   A 1 121 ? 9.33450   33.99040 41.77474 1.000 42.28102  ? 128 ILE   A CB  1 
ATOM   871  C CG1 . ILE   A 1 121 ? 10.76372  33.50555 41.51342 1.000 51.19065  ? 128 ILE   A CG1 1 
ATOM   872  C CG2 . ILE   A 1 121 ? 8.34623   33.25489 40.87071 1.000 42.98386  ? 128 ILE   A CG2 1 
ATOM   873  C CD1 . ILE   A 1 121 ? 11.22478  32.38475 42.42612 1.000 49.16352  ? 128 ILE   A CD1 1 
ATOM   874  N N   . SER   A 1 122 ? 7.07061   36.45271 42.10296 1.000 40.93013  ? 129 SER   A N   1 
ATOM   875  C CA  . SER   A 1 122 ? 5.72785   36.90847 41.75878 1.000 34.93223  ? 129 SER   A CA  1 
ATOM   876  C C   . SER   A 1 122 ? 5.72778   38.17304 40.90506 1.000 42.61174  ? 129 SER   A C   1 
ATOM   877  O O   . SER   A 1 122 ? 4.69661   38.49589 40.30310 1.000 39.39869  ? 129 SER   A O   1 
ATOM   878  C CB  . SER   A 1 122 ? 4.91549   37.14193 43.02776 1.000 38.13735  ? 129 SER   A CB  1 
ATOM   879  O OG  . SER   A 1 122 ? 5.45205   38.22633 43.76228 1.000 46.01594  ? 129 SER   A OG  1 
ATOM   880  N N   . MET   A 1 123 ? 6.85025   38.89296 40.83387 1.000 46.68795  ? 130 MET   A N   1 
ATOM   881  C CA  . MET   A 1 123 ? 6.95944   40.08702 40.00267 1.000 35.57034  ? 130 MET   A CA  1 
ATOM   882  C C   . MET   A 1 123 ? 7.35903   39.78644 38.55730 1.000 38.28296  ? 130 MET   A C   1 
ATOM   883  O O   . MET   A 1 123 ? 7.55307   40.72794 37.78097 1.000 34.52682  ? 130 MET   A O   1 
ATOM   884  C CB  . MET   A 1 123 ? 7.96055   41.05686 40.63690 1.000 37.06733  ? 130 MET   A CB  1 
ATOM   885  C CG  . MET   A 1 123 ? 7.38519   41.79396 41.83341 1.000 37.25973  ? 130 MET   A CG  1 
ATOM   886  S SD  . MET   A 1 123 ? 8.54513   41.93438 43.19510 1.000 74.64081  ? 130 MET   A SD  1 
ATOM   887  C CE  . MET   A 1 123 ? 9.66278   43.16496 42.57337 1.000 55.88822  ? 130 MET   A CE  1 
ATOM   888  N N   . ILE   A 1 124 ? 7.45414   38.50837 38.17472 1.000 36.11178  ? 131 ILE   A N   1 
ATOM   889  C CA  . ILE   A 1 124 ? 7.91525   38.11054 36.84247 1.000 30.74896  ? 131 ILE   A CA  1 
ATOM   890  C C   . ILE   A 1 124 ? 7.15385   38.81705 35.72217 1.000 32.94874  ? 131 ILE   A C   1 
ATOM   891  O O   . ILE   A 1 124 ? 7.72582   39.10806 34.66165 1.000 33.19493  ? 131 ILE   A O   1 
ATOM   892  C CB  . ILE   A 1 124 ? 7.82814   36.57111 36.70456 1.000 33.77600  ? 131 ILE   A CB  1 
ATOM   893  C CG1 . ILE   A 1 124 ? 8.33396   36.11542 35.33696 1.000 30.91546  ? 131 ILE   A CG1 1 
ATOM   894  C CG2 . ILE   A 1 124 ? 6.41405   36.07650 36.93903 1.000 30.19700  ? 131 ILE   A CG2 1 
ATOM   895  C CD1 . ILE   A 1 124 ? 8.40179   34.59482 35.18799 1.000 32.76688  ? 131 ILE   A CD1 1 
ATOM   896  N N   . GLY   A 1 125 ? 5.87230   39.12490 35.93669 1.000 33.53148  ? 132 GLY   A N   1 
ATOM   897  C CA  . GLY   A 1 125 ? 5.08277   39.77684 34.89794 1.000 39.99143  ? 132 GLY   A CA  1 
ATOM   898  C C   . GLY   A 1 125 ? 5.56913   41.16824 34.52518 1.000 45.29862  ? 132 GLY   A C   1 
ATOM   899  O O   . GLY   A 1 125 ? 5.40681   41.59853 33.38108 1.000 38.97297  ? 132 GLY   A O   1 
ATOM   900  N N   . GLN   A 1 126 ? 6.17255   41.89210 35.47119 1.000 36.36723  ? 133 GLN   A N   1 
ATOM   901  C CA  . GLN   A 1 126 ? 6.65104   43.23403 35.14500 1.000 46.08487  ? 133 GLN   A CA  1 
ATOM   902  C C   . GLN   A 1 126 ? 7.82263   43.21495 34.18031 1.000 39.67908  ? 133 GLN   A C   1 
ATOM   903  O O   . GLN   A 1 126 ? 8.25287   44.27996 33.73055 1.000 42.05885  ? 133 GLN   A O   1 
ATOM   904  C CB  . GLN   A 1 126 ? 7.06108   43.98237 36.40870 1.000 42.47472  ? 133 GLN   A CB  1 
ATOM   905  C CG  . GLN   A 1 126 ? 6.08704   43.82715 37.55002 1.000 34.54088  ? 133 GLN   A CG  1 
ATOM   906  C CD  . GLN   A 1 126 ? 6.41005   44.74716 38.68770 1.000 58.73886  ? 133 GLN   A CD  1 
ATOM   907  O OE1 . GLN   A 1 126 ? 6.97004   45.83304 38.48922 1.000 64.04624  ? 133 GLN   A OE1 1 
ATOM   908  N NE2 . GLN   A 1 126 ? 6.08202   44.31645 39.90083 1.000 62.92360  ? 133 GLN   A NE2 1 
ATOM   909  N N   . PHE   A 1 127 ? 8.35993   42.04090 33.87545 1.000 29.07775  ? 134 PHE   A N   1 
ATOM   910  C CA  . PHE   A 1 127 ? 9.48145   41.90799 32.96512 1.000 28.50400  ? 134 PHE   A CA  1 
ATOM   911  C C   . PHE   A 1 127 ? 9.08466   41.26136 31.65090 1.000 33.43494  ? 134 PHE   A C   1 
ATOM   912  O O   . PHE   A 1 127 ? 9.95594   41.00410 30.81309 1.000 38.24482  ? 134 PHE   A O   1 
ATOM   913  C CB  . PHE   A 1 127 ? 10.60078  41.11884 33.65995 1.000 27.46097  ? 134 PHE   A CB  1 
ATOM   914  C CG  . PHE   A 1 127 ? 11.03624  41.75058 34.94868 1.000 32.68787  ? 134 PHE   A CG  1 
ATOM   915  C CD1 . PHE   A 1 127 ? 10.38039  41.45631 36.13830 1.000 35.68653  ? 134 PHE   A CD1 1 
ATOM   916  C CD2 . PHE   A 1 127 ? 12.04611  42.70332 34.96142 1.000 35.82641  ? 134 PHE   A CD2 1 
ATOM   917  C CE1 . PHE   A 1 127 ? 10.76334  42.06423 37.32790 1.000 33.92306  ? 134 PHE   A CE1 1 
ATOM   918  C CE2 . PHE   A 1 127 ? 12.42672  43.30977 36.13910 1.000 34.89819  ? 134 PHE   A CE2 1 
ATOM   919  C CZ  . PHE   A 1 127 ? 11.78205  42.99189 37.32345 1.000 29.44969  ? 134 PHE   A CZ  1 
ATOM   920  N N   . GLY   A 1 128 ? 7.79377   41.00011 31.44777 1.000 32.27040  ? 135 GLY   A N   1 
ATOM   921  C CA  . GLY   A 1 128 ? 7.31080   40.48375 30.18490 1.000 36.41053  ? 135 GLY   A CA  1 
ATOM   922  C C   . GLY   A 1 128 ? 7.56766   39.02053 29.93864 1.000 37.55344  ? 135 GLY   A C   1 
ATOM   923  O O   . GLY   A 1 128 ? 7.33261   38.55277 28.81954 1.000 36.38372  ? 135 GLY   A O   1 
ATOM   924  N N   . VAL   A 1 129 ? 8.03159   38.27311 30.93964 1.000 37.86675  ? 136 VAL   A N   1 
ATOM   925  C CA  . VAL   A 1 129 ? 8.31659   36.85555 30.73869 1.000 34.75625  ? 136 VAL   A CA  1 
ATOM   926  C C   . VAL   A 1 129 ? 7.44973   35.99317 31.65159 1.000 35.47752  ? 136 VAL   A C   1 
ATOM   927  O O   . VAL   A 1 129 ? 7.86944   34.91365 32.09168 1.000 32.52321  ? 136 VAL   A O   1 
ATOM   928  C CB  . VAL   A 1 129 ? 9.81567   36.57434 30.95058 1.000 27.84634  ? 136 VAL   A CB  1 
ATOM   929  C CG1 . VAL   A 1 129 ? 10.61680  37.22841 29.83574 1.000 35.47986  ? 136 VAL   A CG1 1 
ATOM   930  C CG2 . VAL   A 1 129 ? 10.27053  37.09742 32.29711 1.000 30.13997  ? 136 VAL   A CG2 1 
ATOM   931  N N   . GLY   A 1 130 ? 6.22733   36.45200 31.92958 1.000 27.93343  ? 137 GLY   A N   1 
ATOM   932  C CA  . GLY   A 1 130 ? 5.36835   35.74557 32.86486 1.000 25.86742  ? 137 GLY   A CA  1 
ATOM   933  C C   . GLY   A 1 130 ? 4.96366   34.34869 32.42667 1.000 27.42610  ? 137 GLY   A C   1 
ATOM   934  O O   . GLY   A 1 130 ? 4.56743   33.53939 33.27054 1.000 27.19236  ? 137 GLY   A O   1 
ATOM   935  N N   . PHE   A 1 131 ? 5.05823   34.04578 31.12769 1.000 24.93155  ? 138 PHE   A N   1 
ATOM   936  C CA  . PHE   A 1 131 ? 4.70666   32.70900 30.64598 1.000 29.15286  ? 138 PHE   A CA  1 
ATOM   937  C C   . PHE   A 1 131 ? 5.54257   31.63543 31.33815 1.000 36.39788  ? 138 PHE   A C   1 
ATOM   938  O O   . PHE   A 1 131 ? 5.04578   30.54094 31.62951 1.000 28.16300  ? 138 PHE   A O   1 
ATOM   939  C CB  . PHE   A 1 131 ? 4.88250   32.63025 29.12218 1.000 26.12128  ? 138 PHE   A CB  1 
ATOM   940  C CG  . PHE   A 1 131 ? 4.86888   31.22272 28.58145 1.000 25.78806  ? 138 PHE   A CG  1 
ATOM   941  C CD1 . PHE   A 1 131 ? 3.66841   30.59909 28.27755 1.000 30.81940  ? 138 PHE   A CD1 1 
ATOM   942  C CD2 . PHE   A 1 131 ? 6.04896   30.51943 28.38923 1.000 33.56439  ? 138 PHE   A CD2 1 
ATOM   943  C CE1 . PHE   A 1 131 ? 3.63664   29.29936 27.78789 1.000 34.35282  ? 138 PHE   A CE1 1 
ATOM   944  C CE2 . PHE   A 1 131 ? 6.03032   29.21379 27.90205 1.000 32.78113  ? 138 PHE   A CE2 1 
ATOM   945  C CZ  . PHE   A 1 131 ? 4.82070   28.60851 27.59969 1.000 26.26493  ? 138 PHE   A CZ  1 
ATOM   946  N N   . TYR   A 1 132 ? 6.81017   31.93470 31.63072 1.000 35.20535  ? 139 TYR   A N   1 
ATOM   947  C CA  . TYR   A 1 132 ? 7.68347   30.92217 32.20731 1.000 29.67735  ? 139 TYR   A CA  1 
ATOM   948  C C   . TYR   A 1 132 ? 7.27841   30.52842 33.62101 1.000 31.66581  ? 139 TYR   A C   1 
ATOM   949  O O   . TYR   A 1 132 ? 7.70003   29.46558 34.08785 1.000 30.22373  ? 139 TYR   A O   1 
ATOM   950  C CB  . TYR   A 1 132 ? 9.12635   31.41192 32.16767 1.000 39.49199  ? 139 TYR   A CB  1 
ATOM   951  C CG  . TYR   A 1 132 ? 9.58570   31.58982 30.74758 1.000 37.33844  ? 139 TYR   A CG  1 
ATOM   952  C CD1 . TYR   A 1 132 ? 9.66187   30.50346 29.88819 1.000 30.54195  ? 139 TYR   A CD1 1 
ATOM   953  C CD2 . TYR   A 1 132 ? 9.89801   32.84519 30.24961 1.000 33.40669  ? 139 TYR   A CD2 1 
ATOM   954  C CE1 . TYR   A 1 132 ? 10.05754  30.65861 28.57074 1.000 29.91543  ? 139 TYR   A CE1 1 
ATOM   955  C CE2 . TYR   A 1 132 ? 10.29563  33.00909 28.92935 1.000 44.21358  ? 139 TYR   A CE2 1 
ATOM   956  C CZ  . TYR   A 1 132 ? 10.36925  31.91438 28.09947 1.000 36.19935  ? 139 TYR   A CZ  1 
ATOM   957  O OH  . TYR   A 1 132 ? 10.76886  32.08041 26.79713 1.000 41.38800  ? 139 TYR   A OH  1 
ATOM   958  N N   . SER   A 1 133 ? 6.46378   31.34318 34.30651 1.000 28.76385  ? 140 SER   A N   1 
ATOM   959  C CA  . SER   A 1 133 ? 5.92281   30.92925 35.59664 1.000 29.03307  ? 140 SER   A CA  1 
ATOM   960  C C   . SER   A 1 133 ? 5.08232   29.65934 35.49416 1.000 32.09105  ? 140 SER   A C   1 
ATOM   961  O O   . SER   A 1 133 ? 4.74260   29.07399 36.53032 1.000 32.24930  ? 140 SER   A O   1 
ATOM   962  C CB  . SER   A 1 133 ? 5.08857   32.05132 36.21554 1.000 27.29630  ? 140 SER   A CB  1 
ATOM   963  O OG  . SER   A 1 133 ? 3.82602   32.16976 35.58305 1.000 34.83014  ? 140 SER   A OG  1 
ATOM   964  N N   . ALA   A 1 134 ? 4.74203   29.21984 34.28201 1.000 28.56964  ? 141 ALA   A N   1 
ATOM   965  C CA  . ALA   A 1 134 ? 4.05272   27.94277 34.12744 1.000 30.40334  ? 141 ALA   A CA  1 
ATOM   966  C C   . ALA   A 1 134 ? 4.88526   26.78551 34.66649 1.000 27.19611  ? 141 ALA   A C   1 
ATOM   967  O O   . ALA   A 1 134 ? 4.32728   25.79143 35.14651 1.000 36.75418  ? 141 ALA   A O   1 
ATOM   968  C CB  . ALA   A 1 134 ? 3.71514   27.70298 32.65697 1.000 24.15965  ? 141 ALA   A CB  1 
ATOM   969  N N   . TYR   A 1 135 ? 6.21166   26.88143 34.58571 1.000 27.03559  ? 142 TYR   A N   1 
ATOM   970  C CA  . TYR   A 1 135 ? 7.07114   25.80067 35.05425 1.000 30.80246  ? 142 TYR   A CA  1 
ATOM   971  C C   . TYR   A 1 135 ? 7.21483   25.77818 36.56983 1.000 34.72747  ? 142 TYR   A C   1 
ATOM   972  O O   . TYR   A 1 135 ? 7.95831   24.93944 37.09701 1.000 30.96815  ? 142 TYR   A O   1 
ATOM   973  C CB  . TYR   A 1 135 ? 8.43404   25.88995 34.36836 1.000 26.74019  ? 142 TYR   A CB  1 
ATOM   974  C CG  . TYR   A 1 135 ? 8.31065   25.58654 32.88818 1.000 27.92867  ? 142 TYR   A CG  1 
ATOM   975  C CD1 . TYR   A 1 135 ? 8.35283   24.27069 32.42025 1.000 31.51722  ? 142 TYR   A CD1 1 
ATOM   976  C CD2 . TYR   A 1 135 ? 8.10144   26.60963 31.96643 1.000 28.19656  ? 142 TYR   A CD2 1 
ATOM   977  C CE1 . TYR   A 1 135 ? 8.22410   23.98491 31.06543 1.000 29.35004  ? 142 TYR   A CE1 1 
ATOM   978  C CE2 . TYR   A 1 135 ? 7.96529   26.33870 30.61422 1.000 30.25546  ? 142 TYR   A CE2 1 
ATOM   979  C CZ  . TYR   A 1 135 ? 8.02118   25.02524 30.16933 1.000 28.22576  ? 142 TYR   A CZ  1 
ATOM   980  O OH  . TYR   A 1 135 ? 7.87438   24.74771 28.82575 1.000 34.08070  ? 142 TYR   A OH  1 
ATOM   981  N N   . LEU   A 1 136 ? 6.51910   26.67262 37.27452 1.000 28.30187  ? 143 LEU   A N   1 
ATOM   982  C CA  . LEU   A 1 136 ? 6.30169   26.47483 38.70309 1.000 30.19852  ? 143 LEU   A CA  1 
ATOM   983  C C   . LEU   A 1 136 ? 5.46570   25.22732 38.95755 1.000 35.08370  ? 143 LEU   A C   1 
ATOM   984  O O   . LEU   A 1 136 ? 5.70422   24.50267 39.92751 1.000 30.16717  ? 143 LEU   A O   1 
ATOM   985  C CB  . LEU   A 1 136 ? 5.61324   27.70091 39.31760 1.000 27.04142  ? 143 LEU   A CB  1 
ATOM   986  C CG  . LEU   A 1 136 ? 6.39817   29.01526 39.41404 1.000 31.74551  ? 143 LEU   A CG  1 
ATOM   987  C CD1 . LEU   A 1 136 ? 5.46990   30.17137 39.74914 1.000 33.45895  ? 143 LEU   A CD1 1 
ATOM   988  C CD2 . LEU   A 1 136 ? 7.51047   28.90896 40.44807 1.000 33.82983  ? 143 LEU   A CD2 1 
ATOM   989  N N   . VAL   A 1 137 ? 4.47215   24.96757 38.11161 1.000 35.12653  ? 144 VAL   A N   1 
ATOM   990  C CA  . VAL   A 1 137 ? 3.50684   23.90471 38.37235 1.000 27.68123  ? 144 VAL   A CA  1 
ATOM   991  C C   . VAL   A 1 137 ? 3.53110   22.79569 37.33185 1.000 36.49079  ? 144 VAL   A C   1 
ATOM   992  O O   . VAL   A 1 137 ? 2.97734   21.71681 37.59731 1.000 33.30473  ? 144 VAL   A O   1 
ATOM   993  C CB  . VAL   A 1 137 ? 2.07350   24.46207 38.50627 1.000 35.44921  ? 144 VAL   A CB  1 
ATOM   994  C CG1 . VAL   A 1 137 ? 1.96216   25.44109 39.70301 1.000 27.91035  ? 144 VAL   A CG1 1 
ATOM   995  C CG2 . VAL   A 1 137 ? 1.63822   25.12705 37.20360 1.000 37.04835  ? 144 VAL   A CG2 1 
ATOM   996  N N   . ALA   A 1 138 ? 4.14435   23.00623 36.16424 1.000 29.87164  ? 145 ALA   A N   1 
ATOM   997  C CA  . ALA   A 1 138 ? 4.09578   22.05358 35.06293 1.000 33.40541  ? 145 ALA   A CA  1 
ATOM   998  C C   . ALA   A 1 138 ? 5.47689   21.46558 34.80995 1.000 28.28264  ? 145 ALA   A C   1 
ATOM   999  O O   . ALA   A 1 138 ? 6.48483   22.17202 34.88351 1.000 36.40242  ? 145 ALA   A O   1 
ATOM   1000 C CB  . ALA   A 1 138 ? 3.57383   22.70922 33.77506 1.000 31.11847  ? 145 ALA   A CB  1 
ATOM   1001 N N   . GLU   A 1 139 ? 5.52165   20.15870 34.53990 1.000 27.68756  ? 146 GLU   A N   1 
ATOM   1002 C CA  . GLU   A 1 139 ? 6.76168   19.55042 34.07551 1.000 34.07112  ? 146 GLU   A CA  1 
ATOM   1003 C C   . GLU   A 1 139 ? 6.92347   19.70154 32.57015 1.000 32.20878  ? 146 GLU   A C   1 
ATOM   1004 O O   . GLU   A 1 139 ? 8.04462   19.61255 32.06409 1.000 38.51432  ? 146 GLU   A O   1 
ATOM   1005 C CB  . GLU   A 1 139 ? 6.81554   18.06530 34.44102 1.000 35.60484  ? 146 GLU   A CB  1 
ATOM   1006 C CG  . GLU   A 1 139 ? 5.47383   17.37456 34.36219 1.000 50.97388  ? 146 GLU   A CG  1 
ATOM   1007 C CD  . GLU   A 1 139 ? 5.53201   15.90568 34.75107 1.000 74.04975  ? 146 GLU   A CD  1 
ATOM   1008 O OE1 . GLU   A 1 139 ? 5.04741   15.06809 33.95500 1.000 68.31810  ? 146 GLU   A OE1 1 
ATOM   1009 O OE2 . GLU   A 1 139 ? 6.05979   15.58907 35.84399 1.000 74.59224  ? 146 GLU   A OE2 1 
ATOM   1010 N N   . LYS   A 1 140 ? 5.82696   19.92706 31.85409 1.000 36.07001  ? 147 LYS   A N   1 
ATOM   1011 C CA  . LYS   A 1 140 ? 5.85636   20.09354 30.41170 1.000 35.14835  ? 147 LYS   A CA  1 
ATOM   1012 C C   . LYS   A 1 140 ? 4.73944   21.05147 30.02242 1.000 35.79461  ? 147 LYS   A C   1 
ATOM   1013 O O   . LYS   A 1 140 ? 3.64582   21.01049 30.59520 1.000 31.11880  ? 147 LYS   A O   1 
ATOM   1014 C CB  . LYS   A 1 140 ? 5.70375   18.74313 29.70012 1.000 29.84981  ? 147 LYS   A CB  1 
ATOM   1015 C CG  . LYS   A 1 140 ? 5.42789   18.83812 28.20683 1.000 47.05750  ? 147 LYS   A CG  1 
ATOM   1016 C CD  . LYS   A 1 140 ? 5.60904   17.48573 27.53562 1.000 41.72921  ? 147 LYS   A CD  1 
ATOM   1017 C CE  . LYS   A 1 140 ? 4.28032   16.97018 27.01597 1.000 47.95074  ? 147 LYS   A CE  1 
ATOM   1018 N NZ  . LYS   A 1 140 ? 4.25261   15.48185 26.96989 1.000 52.02482  ? 147 LYS   A NZ  1 
ATOM   1019 N N   . VAL   A 1 141 ? 5.02263   21.92712 29.06434 1.000 26.65953  ? 148 VAL   A N   1 
ATOM   1020 C CA  . VAL   A 1 141 ? 4.04141   22.89424 28.59000 1.000 24.40393  ? 148 VAL   A CA  1 
ATOM   1021 C C   . VAL   A 1 141 ? 3.90887   22.72094 27.08415 1.000 31.64071  ? 148 VAL   A C   1 
ATOM   1022 O O   . VAL   A 1 141 ? 4.91453   22.75211 26.36587 1.000 27.58101  ? 148 VAL   A O   1 
ATOM   1023 C CB  . VAL   A 1 141 ? 4.43372   24.34425 28.94505 1.000 26.19645  ? 148 VAL   A CB  1 
ATOM   1024 C CG1 . VAL   A 1 141 ? 3.40650   25.31820 28.40421 1.000 26.01135  ? 148 VAL   A CG1 1 
ATOM   1025 C CG2 . VAL   A 1 141 ? 4.56420   24.52249 30.46808 1.000 29.88483  ? 148 VAL   A CG2 1 
ATOM   1026 N N   . THR   A 1 142 ? 2.68019   22.51847 26.61101 1.000 29.37638  ? 149 THR   A N   1 
ATOM   1027 C CA  . THR   A 1 142 ? 2.35852   22.51294 25.18501 1.000 32.19914  ? 149 THR   A CA  1 
ATOM   1028 C C   . THR   A 1 142 ? 1.54855   23.75853 24.83317 1.000 35.17625  ? 149 THR   A C   1 
ATOM   1029 O O   . THR   A 1 142 ? 0.58438   24.09191 25.52836 1.000 34.57173  ? 149 THR   A O   1 
ATOM   1030 C CB  . THR   A 1 142 ? 1.55767   21.26673 24.80410 1.000 33.12611  ? 149 THR   A CB  1 
ATOM   1031 O OG1 . THR   A 1 142 ? 2.16554   20.11470 25.38869 1.000 34.75043  ? 149 THR   A OG1 1 
ATOM   1032 C CG2 . THR   A 1 142 ? 1.51563   21.10148 23.28463 1.000 31.07062  ? 149 THR   A CG2 1 
ATOM   1033 N N   . VAL   A 1 143 ? 1.91264   24.42366 23.74119 1.000 24.19110  ? 150 VAL   A N   1 
ATOM   1034 C CA  . VAL   A 1 143 ? 1.20028   25.60854 23.27302 1.000 27.50294  ? 150 VAL   A CA  1 
ATOM   1035 C C   . VAL   A 1 143 ? 0.69889   25.33971 21.86081 1.000 32.38467  ? 150 VAL   A C   1 
ATOM   1036 O O   . VAL   A 1 143 ? 1.50086   25.12263 20.94149 1.000 32.83525  ? 150 VAL   A O   1 
ATOM   1037 C CB  . VAL   A 1 143 ? 2.08897   26.86181 23.31304 1.000 28.26122  ? 150 VAL   A CB  1 
ATOM   1038 C CG1 . VAL   A 1 143 ? 1.32008   28.07951 22.81065 1.000 28.06927  ? 150 VAL   A CG1 1 
ATOM   1039 C CG2 . VAL   A 1 143 ? 2.61494   27.09664 24.72363 1.000 29.39407  ? 150 VAL   A CG2 1 
ATOM   1040 N N   . ILE   A 1 144 ? -0.62134  25.33159 21.68994 1.000 28.84863  ? 151 ILE   A N   1 
ATOM   1041 C CA  . ILE   A 1 144 ? -1.24576  25.20396 20.37629 1.000 28.49663  ? 151 ILE   A CA  1 
ATOM   1042 C C   . ILE   A 1 144 ? -1.75746  26.58216 19.98258 1.000 28.89151  ? 151 ILE   A C   1 
ATOM   1043 O O   . ILE   A 1 144 ? -2.45965  27.22546 20.76607 1.000 28.05277  ? 151 ILE   A O   1 
ATOM   1044 C CB  . ILE   A 1 144 ? -2.39517  24.18117 20.38587 1.000 31.28107  ? 151 ILE   A CB  1 
ATOM   1045 C CG1 . ILE   A 1 144 ? -2.02354  22.92013 21.17774 1.000 38.69753  ? 151 ILE   A CG1 1 
ATOM   1046 C CG2 . ILE   A 1 144 ? -2.78979  23.82559 18.95602 1.000 32.55115  ? 151 ILE   A CG2 1 
ATOM   1047 C CD1 . ILE   A 1 144 ? -1.08851  22.00921 20.46030 1.000 39.64614  ? 151 ILE   A CD1 1 
ATOM   1048 N N   . THR   A 1 145 ? -1.42770  27.03564 18.77302 1.000 29.46460  ? 152 THR   A N   1 
ATOM   1049 C CA  . THR   A 1 145 ? -1.74918  28.41050 18.41392 1.000 26.69382  ? 152 THR   A CA  1 
ATOM   1050 C C   . THR   A 1 145 ? -2.05105  28.51722 16.92195 1.000 32.27613  ? 152 THR   A C   1 
ATOM   1051 O O   . THR   A 1 145 ? -1.53901  27.74029 16.10719 1.000 34.08934  ? 152 THR   A O   1 
ATOM   1052 C CB  . THR   A 1 145 ? -0.61540  29.36431 18.82078 1.000 31.96340  ? 152 THR   A CB  1 
ATOM   1053 O OG1 . THR   A 1 145 ? -1.06837  30.72542 18.73319 1.000 30.01418  ? 152 THR   A OG1 1 
ATOM   1054 C CG2 . THR   A 1 145 ? 0.60556   29.16683 17.93681 1.000 31.17295  ? 152 THR   A CG2 1 
ATOM   1055 N N   . LYS   A 1 146 ? -2.91164  29.48301 16.58172 1.000 26.64943  ? 153 LYS   A N   1 
ATOM   1056 C CA  . LYS   A 1 146 ? -3.35833  29.71487 15.20634 1.000 28.04136  ? 153 LYS   A CA  1 
ATOM   1057 C C   . LYS   A 1 146 ? -3.52368  31.21811 15.02084 1.000 35.18085  ? 153 LYS   A C   1 
ATOM   1058 O O   . LYS   A 1 146 ? -4.37506  31.83124 15.66731 1.000 28.83747  ? 153 LYS   A O   1 
ATOM   1059 C CB  . LYS   A 1 146 ? -4.66515  28.97705 14.91204 1.000 28.00083  ? 153 LYS   A CB  1 
ATOM   1060 C CG  . LYS   A 1 146 ? -5.30171  29.31652 13.55350 1.000 28.79608  ? 153 LYS   A CG  1 
ATOM   1061 C CD  . LYS   A 1 146 ? -4.40951  28.89611 12.38998 1.000 32.25331  ? 153 LYS   A CD  1 
ATOM   1062 C CE  . LYS   A 1 146 ? -5.16807  28.94026 11.07247 1.000 37.14361  ? 153 LYS   A CE  1 
ATOM   1063 N NZ  . LYS   A 1 146 ? -5.39007  30.35636 10.64185 1.000 38.96391  ? 153 LYS   A NZ  1 
ATOM   1064 N N   . HIS   A 1 147 ? -2.69452  31.80338 14.16207 1.000 31.76644  ? 154 HIS   A N   1 
ATOM   1065 C CA  . HIS   A 1 147 ? -2.76934  33.20555 13.78276 1.000 28.60451  ? 154 HIS   A CA  1 
ATOM   1066 C C   . HIS   A 1 147 ? -3.39761  33.29603 12.39587 1.000 29.34210  ? 154 HIS   A C   1 
ATOM   1067 O O   . HIS   A 1 147 ? -3.19738  32.40222 11.56692 1.000 36.39521  ? 154 HIS   A O   1 
ATOM   1068 C CB  . HIS   A 1 147 ? -1.36343  33.81158 13.79623 1.000 38.13125  ? 154 HIS   A CB  1 
ATOM   1069 C CG  . HIS   A 1 147 ? -1.31866  35.28670 13.54605 1.000 34.56329  ? 154 HIS   A CG  1 
ATOM   1070 N ND1 . HIS   A 1 147 ? -1.31717  35.82881 12.27975 1.000 33.82999  ? 154 HIS   A ND1 1 
ATOM   1071 C CD2 . HIS   A 1 147 ? -1.22787  36.33203 14.40439 1.000 33.41825  ? 154 HIS   A CD2 1 
ATOM   1072 C CE1 . HIS   A 1 147 ? -1.24510  37.14558 12.36758 1.000 33.63847  ? 154 HIS   A CE1 1 
ATOM   1073 N NE2 . HIS   A 1 147 ? -1.19446  37.47542 13.64646 1.000 34.02222  ? 154 HIS   A NE2 1 
ATOM   1074 N N   . ASN   A 1 148 ? -4.16704  34.36989 12.14977 1.000 29.72192  ? 155 ASN   A N   1 
ATOM   1075 C CA  . ASN   A 1 148 ? -4.87929  34.52355 10.87628 1.000 36.22239  ? 155 ASN   A CA  1 
ATOM   1076 C C   . ASN   A 1 148 ? -3.95381  34.40330 9.66888  1.000 42.26104  ? 155 ASN   A C   1 
ATOM   1077 O O   . ASN   A 1 148 ? -4.40111  34.02901 8.57928  1.000 36.27750  ? 155 ASN   A O   1 
ATOM   1078 C CB  . ASN   A 1 148 ? -5.59505  35.88230 10.80297 1.000 37.39641  ? 155 ASN   A CB  1 
ATOM   1079 C CG  . ASN   A 1 148 ? -6.91190  35.91555 11.57413 1.000 49.87111  ? 155 ASN   A CG  1 
ATOM   1080 O OD1 . ASN   A 1 148 ? -7.56106  34.88861 11.78597 1.000 40.31547  ? 155 ASN   A OD1 1 
ATOM   1081 N ND2 . ASN   A 1 148 ? -7.31647  37.11695 11.98898 1.000 37.79195  ? 155 ASN   A ND2 1 
ATOM   1082 N N   . ASP   A 1 149 ? -2.67362  34.73393 9.83210  1.000 34.59208  ? 156 ASP   A N   1 
ATOM   1083 C CA  . ASP   A 1 149 ? -1.72906  34.76439 8.72564  1.000 34.79609  ? 156 ASP   A CA  1 
ATOM   1084 C C   . ASP   A 1 149 ? -0.89589  33.48665 8.60861  1.000 44.00107  ? 156 ASP   A C   1 
ATOM   1085 O O   . ASP   A 1 149 ? 0.05532   33.45738 7.82712  1.000 38.50701  ? 156 ASP   A O   1 
ATOM   1086 C CB  . ASP   A 1 149 ? -0.78743  35.96626 8.86470  1.000 36.46278  ? 156 ASP   A CB  1 
ATOM   1087 C CG  . ASP   A 1 149 ? -1.51240  37.30873 8.78610  1.000 50.24787  ? 156 ASP   A CG  1 
ATOM   1088 O OD1 . ASP   A 1 149 ? -2.65251  37.36627 8.27152  1.000 43.55360  ? 156 ASP   A OD1 1 
ATOM   1089 O OD2 . ASP   A 1 149 ? -0.92291  38.31628 9.23447  1.000 42.14178  ? 156 ASP   A OD2 1 
ATOM   1090 N N   . ASP   A 1 150 ? -1.20900  32.43846 9.36660  1.000 39.55846  ? 157 ASP   A N   1 
ATOM   1091 C CA  . ASP   A 1 150 ? -0.35136  31.25765 9.38464  1.000 32.79714  ? 157 ASP   A CA  1 
ATOM   1092 C C   . ASP   A 1 150 ? -1.20381  30.02103 9.64297  1.000 33.25081  ? 157 ASP   A C   1 
ATOM   1093 O O   . ASP   A 1 150 ? -2.41745  30.11482 9.84521  1.000 42.56788  ? 157 ASP   A O   1 
ATOM   1094 C CB  . ASP   A 1 150 ? 0.75586   31.41069 10.43274 1.000 30.38818  ? 157 ASP   A CB  1 
ATOM   1095 C CG  . ASP   A 1 150 ? 2.04974   30.74431 10.01147 1.000 47.59835  ? 157 ASP   A CG  1 
ATOM   1096 O OD1 . ASP   A 1 150 ? 1.99734   29.87121 9.11377  1.000 42.43213  ? 157 ASP   A OD1 1 
ATOM   1097 O OD2 . ASP   A 1 150 ? 3.11684   31.09720 10.56772 1.000 38.99224  ? 157 ASP   A OD2 1 
ATOM   1098 N N   . GLU   A 1 151 ? -0.55792  28.85224 9.62827  1.000 37.48038  ? 158 GLU   A N   1 
ATOM   1099 C CA  . GLU   A 1 151 ? -1.23365  27.60006 9.94152  1.000 37.16292  ? 158 GLU   A CA  1 
ATOM   1100 C C   . GLU   A 1 151 ? -1.21975  27.35009 11.44722 1.000 38.98611  ? 158 GLU   A C   1 
ATOM   1101 O O   . GLU   A 1 151 ? -0.59393  28.07697 12.22282 1.000 34.39789  ? 158 GLU   A O   1 
ATOM   1102 C CB  . GLU   A 1 151 ? -0.57914  26.41164 9.23534  1.000 38.05491  ? 158 GLU   A CB  1 
ATOM   1103 C CG  . GLU   A 1 151 ? -0.19467  26.60509 7.79398  1.000 46.07078  ? 158 GLU   A CG  1 
ATOM   1104 C CD  . GLU   A 1 151 ? 0.94900   25.67978 7.39171  1.000 80.77017  ? 158 GLU   A CD  1 
ATOM   1105 O OE1 . GLU   A 1 151 ? 0.95963   24.51246 7.84904  1.000 72.58028  ? 158 GLU   A OE1 1 
ATOM   1106 O OE2 . GLU   A 1 151 ? 1.84266   26.11800 6.63448  1.000 85.78975  ? 158 GLU   A OE2 1 
ATOM   1107 N N   . GLN   A 1 152 ? -1.88806  26.27759 11.86452 1.000 33.16260  ? 159 GLN   A N   1 
ATOM   1108 C CA  . GLN   A 1 152 ? -1.92870  25.90564 13.27280 1.000 37.01383  ? 159 GLN   A CA  1 
ATOM   1109 C C   . GLN   A 1 152 ? -0.64800  25.16132 13.65072 1.000 49.04531  ? 159 GLN   A C   1 
ATOM   1110 O O   . GLN   A 1 152 ? -0.24541  24.22084 12.95635 1.000 36.98513  ? 159 GLN   A O   1 
ATOM   1111 C CB  . GLN   A 1 152 ? -3.16283  25.04554 13.54024 1.000 29.73555  ? 159 GLN   A CB  1 
ATOM   1112 C CG  . GLN   A 1 152 ? -3.45916  24.78263 15.00176 1.000 32.48002  ? 159 GLN   A CG  1 
ATOM   1113 C CD  . GLN   A 1 152 ? -4.90351  24.39330 15.21220 1.000 51.81591  ? 159 GLN   A CD  1 
ATOM   1114 O OE1 . GLN   A 1 152 ? -5.81385  25.08683 14.75104 1.000 49.17124  ? 159 GLN   A OE1 1 
ATOM   1115 N NE2 . GLN   A 1 152 ? -5.12754  23.27142 15.89241 1.000 37.62899  ? 159 GLN   A NE2 1 
ATOM   1116 N N   . TYR   A 1 153 ? 0.00109   25.59142 14.74288 1.000 36.24384  ? 160 TYR   A N   1 
ATOM   1117 C CA  . TYR   A 1 153 ? 1.27937   25.02814 15.17283 1.000 32.43277  ? 160 TYR   A CA  1 
ATOM   1118 C C   . TYR   A 1 153 ? 1.21185   24.57796 16.62715 1.000 43.06369  ? 160 TYR   A C   1 
ATOM   1119 O O   . TYR   A 1 153 ? 0.40452   25.07230 17.42180 1.000 32.39833  ? 160 TYR   A O   1 
ATOM   1120 C CB  . TYR   A 1 153 ? 2.43969   26.02975 15.01161 1.000 30.44743  ? 160 TYR   A CB  1 
ATOM   1121 C CG  . TYR   A 1 153 ? 2.83312   26.28647 13.57093 1.000 43.84650  ? 160 TYR   A CG  1 
ATOM   1122 C CD1 . TYR   A 1 153 ? 3.71365   25.44263 12.90364 1.000 35.16529  ? 160 TYR   A CD1 1 
ATOM   1123 C CD2 . TYR   A 1 153 ? 2.30968   27.37108 12.87273 1.000 42.95529  ? 160 TYR   A CD2 1 
ATOM   1124 C CE1 . TYR   A 1 153 ? 4.06399   25.67485 11.57902 1.000 44.41069  ? 160 TYR   A CE1 1 
ATOM   1125 C CE2 . TYR   A 1 153 ? 2.65349   27.60933 11.55191 1.000 41.04584  ? 160 TYR   A CE2 1 
ATOM   1126 C CZ  . TYR   A 1 153 ? 3.52564   26.76131 10.91058 1.000 56.24171  ? 160 TYR   A CZ  1 
ATOM   1127 O OH  . TYR   A 1 153 ? 3.86595   27.00440 9.59767  1.000 75.24901  ? 160 TYR   A OH  1 
ATOM   1128 N N   . ALA   A 1 154 ? 2.09664   23.63984 16.96943 1.000 31.58455  ? 161 ALA   A N   1 
ATOM   1129 C CA  . ALA   A 1 154 ? 2.27529   23.17500 18.34140 1.000 34.02293  ? 161 ALA   A CA  1 
ATOM   1130 C C   . ALA   A 1 154 ? 3.71510   23.41832 18.77128 1.000 28.96165  ? 161 ALA   A C   1 
ATOM   1131 O O   . ALA   A 1 154 ? 4.64865   22.90990 18.13974 1.000 42.83790  ? 161 ALA   A O   1 
ATOM   1132 C CB  . ALA   A 1 154 ? 1.92679   21.69166 18.47745 1.000 35.77092  ? 161 ALA   A CB  1 
ATOM   1133 N N   . TRP   A 1 155 ? 3.88336   24.18657 19.84551 1.000 25.40626  ? 162 TRP   A N   1 
ATOM   1134 C CA  . TRP   A 1 155 ? 5.14445   24.41388 20.53574 1.000 27.23233  ? 162 TRP   A CA  1 
ATOM   1135 C C   . TRP   A 1 155 ? 5.13648   23.57561 21.80948 1.000 38.30256  ? 162 TRP   A C   1 
ATOM   1136 O O   . TRP   A 1 155 ? 4.08410   23.38043 22.42074 1.000 28.49753  ? 162 TRP   A O   1 
ATOM   1137 C CB  . TRP   A 1 155 ? 5.28593   25.90611 20.86583 1.000 23.37953  ? 162 TRP   A CB  1 
ATOM   1138 C CG  . TRP   A 1 155 ? 6.52224   26.36816 21.60386 1.000 28.19737  ? 162 TRP   A CG  1 
ATOM   1139 C CD1 . TRP   A 1 155 ? 7.59818   27.01568 21.06240 1.000 28.40004  ? 162 TRP   A CD1 1 
ATOM   1140 C CD2 . TRP   A 1 155 ? 6.77646   26.29039 23.01744 1.000 29.68575  ? 162 TRP   A CD2 1 
ATOM   1141 N NE1 . TRP   A 1 155 ? 8.51341   27.31926 22.03849 1.000 31.26936  ? 162 TRP   A NE1 1 
ATOM   1142 C CE2 . TRP   A 1 155 ? 8.03291   26.88950 23.24855 1.000 32.16553  ? 162 TRP   A CE2 1 
ATOM   1143 C CE3 . TRP   A 1 155 ? 6.06304   25.77839 24.10925 1.000 33.48774  ? 162 TRP   A CE3 1 
ATOM   1144 C CZ2 . TRP   A 1 155 ? 8.59631   26.97731 24.51902 1.000 26.93953  ? 162 TRP   A CZ2 1 
ATOM   1145 C CZ3 . TRP   A 1 155 ? 6.62262   25.87849 25.37589 1.000 25.83121  ? 162 TRP   A CZ3 1 
ATOM   1146 C CH2 . TRP   A 1 155 ? 7.87701   26.46568 25.56605 1.000 29.54778  ? 162 TRP   A CH2 1 
ATOM   1147 N N   . GLU   A 1 156 ? 6.30426   23.07028 22.20753 1.000 25.35870  ? 163 GLU   A N   1 
ATOM   1148 C CA  . GLU   A 1 156 ? 6.35101   22.19432 23.37175 1.000 32.43898  ? 163 GLU   A CA  1 
ATOM   1149 C C   . GLU   A 1 156 ? 7.72238   22.21344 24.02863 1.000 39.70339  ? 163 GLU   A C   1 
ATOM   1150 O O   . GLU   A 1 156 ? 8.74777   22.12944 23.34295 1.000 32.55596  ? 163 GLU   A O   1 
ATOM   1151 C CB  . GLU   A 1 156 ? 6.00318   20.75646 22.97744 1.000 38.90022  ? 163 GLU   A CB  1 
ATOM   1152 C CG  . GLU   A 1 156 ? 5.88288   19.79556 24.13918 1.000 47.23871  ? 163 GLU   A CG  1 
ATOM   1153 C CD  . GLU   A 1 156 ? 5.06002   18.57235 23.77595 1.000 56.41915  ? 163 GLU   A CD  1 
ATOM   1154 O OE1 . GLU   A 1 156 ? 3.88851   18.47379 24.20992 1.000 56.97900  ? 163 GLU   A OE1 1 
ATOM   1155 O OE2 . GLU   A 1 156 ? 5.58004   17.73052 23.01241 1.000 52.15918  ? 163 GLU   A OE2 1 
ATOM   1156 N N   . SER   A 1 157 ? 7.74063   22.26680 25.36253 1.000 29.81443  ? 164 SER   A N   1 
ATOM   1157 C CA  . SER   A 1 157 ? 9.01464   22.19116 26.06095 1.000 28.61873  ? 164 SER   A CA  1 
ATOM   1158 C C   . SER   A 1 157 ? 8.85400   21.61588 27.46201 1.000 36.62970  ? 164 SER   A C   1 
ATOM   1159 O O   . SER   A 1 157 ? 7.95657   22.00937 28.21389 1.000 32.48487  ? 164 SER   A O   1 
ATOM   1160 C CB  . SER   A 1 157 ? 9.68589   23.56663 26.14329 1.000 25.01643  ? 164 SER   A CB  1 
ATOM   1161 O OG  . SER   A 1 157 ? 10.93256  23.45847 26.80261 1.000 34.72415  ? 164 SER   A OG  1 
ATOM   1162 N N   . SER   A 1 158 ? 9.75462   20.69204 27.80175 1.000 34.14161  ? 165 SER   A N   1 
ATOM   1163 C CA  . SER   A 1 158 ? 9.95723   20.21877 29.16437 1.000 39.99650  ? 165 SER   A CA  1 
ATOM   1164 C C   . SER   A 1 158 ? 11.14661  20.90061 29.82445 1.000 33.39980  ? 165 SER   A C   1 
ATOM   1165 O O   . SER   A 1 158 ? 11.75739  20.33538 30.73604 1.000 41.70361  ? 165 SER   A O   1 
ATOM   1166 C CB  . SER   A 1 158 ? 10.15072  18.69957 29.18949 1.000 37.17667  ? 165 SER   A CB  1 
ATOM   1167 O OG  . SER   A 1 158 ? 9.02417   18.02072 28.66489 1.000 39.96873  ? 165 SER   A OG  1 
ATOM   1168 N N   . ALA   A 1 159 ? 11.47641  22.10648 29.38175 1.000 31.84190  ? 166 ALA   A N   1 
ATOM   1169 C CA  . ALA   A 1 159 ? 12.70288  22.81646 29.78119 1.000 41.05751  ? 166 ALA   A CA  1 
ATOM   1170 C C   . ALA   A 1 159 ? 13.88478  21.91240 29.41050 1.000 41.69912  ? 166 ALA   A C   1 
ATOM   1171 O O   . ALA   A 1 159 ? 13.84586  21.23191 28.37268 1.000 42.06147  ? 166 ALA   A O   1 
ATOM   1172 C CB  . ALA   A 1 159 ? 12.62705  23.22778 31.24061 1.000 35.60064  ? 166 ALA   A CB  1 
ATOM   1173 N N   . GLY   A 1 160 ? 14.94408  21.86598 30.21353 1.000 40.16059  ? 167 GLY   A N   1 
ATOM   1174 C CA  . GLY   A 1 160 ? 16.11225  21.11750 29.79918 1.000 35.46060  ? 167 GLY   A CA  1 
ATOM   1175 C C   . GLY   A 1 160 ? 16.91656  21.76673 28.69776 1.000 33.86577  ? 167 GLY   A C   1 
ATOM   1176 O O   . GLY   A 1 160 ? 17.88541  21.16767 28.22075 1.000 40.75487  ? 167 GLY   A O   1 
ATOM   1177 N N   . GLY   A 1 161 ? 16.54344  22.97420 28.27926 1.000 31.67463  ? 168 GLY   A N   1 
ATOM   1178 C CA  . GLY   A 1 161 ? 17.29897  23.73943 27.31176 1.000 41.38352  ? 168 GLY   A CA  1 
ATOM   1179 C C   . GLY   A 1 161 ? 16.79963  23.69087 25.88224 1.000 37.36422  ? 168 GLY   A C   1 
ATOM   1180 O O   . GLY   A 1 161 ? 17.44740  24.27921 25.00493 1.000 32.55616  ? 168 GLY   A O   1 
ATOM   1181 N N   . SER   A 1 162 ? 15.67793  23.02083 25.60996 1.000 32.94811  ? 169 SER   A N   1 
ATOM   1182 C CA  . SER   A 1 162 ? 15.21620  22.87979 24.23553 1.000 30.29483  ? 169 SER   A CA  1 
ATOM   1183 C C   . SER   A 1 162 ? 13.69314  22.90145 24.17471 1.000 32.61289  ? 169 SER   A C   1 
ATOM   1184 O O   . SER   A 1 162 ? 12.99226  22.67936 25.16887 1.000 28.24493  ? 169 SER   A O   1 
ATOM   1185 C CB  . SER   A 1 162 ? 15.78111  21.59893 23.56954 1.000 37.28370  ? 169 SER   A CB  1 
ATOM   1186 O OG  . SER   A 1 162 ? 15.17096  20.41938 24.06474 1.000 34.70431  ? 169 SER   A OG  1 
ATOM   1187 N N   . PHE   A 1 163 ? 13.19549  23.21991 22.98197 1.000 29.31240  ? 170 PHE   A N   1 
ATOM   1188 C CA  . PHE   A 1 163 ? 11.77847  23.18031 22.66759 1.000 27.63287  ? 170 PHE   A CA  1 
ATOM   1189 C C   . PHE   A 1 163 ? 11.62875  22.65561 21.24445 1.000 35.62611  ? 170 PHE   A C   1 
ATOM   1190 O O   . PHE   A 1 163 ? 12.59804  22.60685 20.47537 1.000 31.39662  ? 170 PHE   A O   1 
ATOM   1191 C CB  . PHE   A 1 163 ? 11.10494  24.55907 22.85808 1.000 26.10811  ? 170 PHE   A CB  1 
ATOM   1192 C CG  . PHE   A 1 163 ? 11.59900  25.63200 21.92253 1.000 31.11977  ? 170 PHE   A CG  1 
ATOM   1193 C CD1 . PHE   A 1 163 ? 12.68507  26.42154 22.26965 1.000 30.84442  ? 170 PHE   A CD1 1 
ATOM   1194 C CD2 . PHE   A 1 163 ? 10.95754  25.88003 20.71100 1.000 32.68470  ? 170 PHE   A CD2 1 
ATOM   1195 C CE1 . PHE   A 1 163 ? 13.14592  27.41876 21.42287 1.000 28.57707  ? 170 PHE   A CE1 1 
ATOM   1196 C CE2 . PHE   A 1 163 ? 11.42052  26.88432 19.85818 1.000 31.79700  ? 170 PHE   A CE2 1 
ATOM   1197 C CZ  . PHE   A 1 163 ? 12.50923  27.65471 20.22267 1.000 29.30419  ? 170 PHE   A CZ  1 
ATOM   1198 N N   . THR   A 1 164 ? 10.42058  22.19250 20.92394 1.000 28.98791  ? 171 THR   A N   1 
ATOM   1199 C CA  . THR   A 1 164 ? 10.09871  21.69273 19.59402 1.000 29.26169  ? 171 THR   A CA  1 
ATOM   1200 C C   . THR   A 1 164 ? 8.94188   22.48970 19.01116 1.000 37.46393  ? 171 THR   A C   1 
ATOM   1201 O O   . THR   A 1 164 ? 8.11990   23.05631 19.74274 1.000 30.71074  ? 171 THR   A O   1 
ATOM   1202 C CB  . THR   A 1 164 ? 9.70113   20.21085 19.60020 1.000 32.17994  ? 171 THR   A CB  1 
ATOM   1203 O OG1 . THR   A 1 164 ? 8.53628   20.03773 20.41996 1.000 37.84983  ? 171 THR   A OG1 1 
ATOM   1204 C CG2 . THR   A 1 164 ? 10.83458  19.32259 20.10455 1.000 37.43931  ? 171 THR   A CG2 1 
ATOM   1205 N N   . VAL   A 1 165 ? 8.89172   22.53702 17.68356 1.000 35.75510  ? 172 VAL   A N   1 
ATOM   1206 C CA  . VAL   A 1 165 ? 7.76193   23.10161 16.96112 1.000 29.95303  ? 172 VAL   A CA  1 
ATOM   1207 C C   . VAL   A 1 165 ? 7.36630   22.12849 15.86000 1.000 30.09845  ? 172 VAL   A C   1 
ATOM   1208 O O   . VAL   A 1 165 ? 8.22737   21.54390 15.19405 1.000 31.54611  ? 172 VAL   A O   1 
ATOM   1209 C CB  . VAL   A 1 165 ? 8.08046   24.49145 16.36774 1.000 35.71228  ? 172 VAL   A CB  1 
ATOM   1210 C CG1 . VAL   A 1 165 ? 6.88623   25.01602 15.59362 1.000 34.07917  ? 172 VAL   A CG1 1 
ATOM   1211 C CG2 . VAL   A 1 165 ? 8.46808   25.46713 17.46267 1.000 28.64173  ? 172 VAL   A CG2 1 
ATOM   1212 N N   . ARG   A 1 166 ? 6.06168   21.95252 15.67593 1.000 32.61624  ? 173 ARG   A N   1 
ATOM   1213 C CA  . ARG   A 1 166 ? 5.54459   21.15469 14.57445 1.000 37.21022  ? 173 ARG   A CA  1 
ATOM   1214 C C   . ARG   A 1 166 ? 4.20428   21.74047 14.15389 1.000 42.44738  ? 173 ARG   A C   1 
ATOM   1215 O O   . ARG   A 1 166 ? 3.53376   22.42357 14.93797 1.000 36.89072  ? 173 ARG   A O   1 
ATOM   1216 C CB  . ARG   A 1 166 ? 5.39828   19.68168 14.97974 1.000 39.47888  ? 173 ARG   A CB  1 
ATOM   1217 C CG  . ARG   A 1 166 ? 4.13498   19.41502 15.77879 1.000 49.13413  ? 173 ARG   A CG  1 
ATOM   1218 C CD  . ARG   A 1 166 ? 4.10364   18.05238 16.46733 1.000 46.49686  ? 173 ARG   A CD  1 
ATOM   1219 N NE  . ARG   A 1 166 ? 3.39658   18.12945 17.74208 1.000 69.02575  ? 173 ARG   A NE  1 
ATOM   1220 C CZ  . ARG   A 1 166 ? 2.07270   18.16053 17.86865 1.000 78.93748  ? 173 ARG   A CZ  1 
ATOM   1221 N NH1 . ARG   A 1 166 ? 1.27126   18.14149 16.81186 1.000 64.41720  ? 173 ARG   A NH1 1 
ATOM   1222 N NH2 . ARG   A 1 166 ? 1.53679   18.21969 19.08614 1.000 60.45970  ? 173 ARG   A NH2 1 
ATOM   1223 N N   . THR   A 1 167 ? 3.82049   21.48842 12.89977 1.000 42.32382  ? 174 THR   A N   1 
ATOM   1224 C CA  . THR   A 1 167 ? 2.45913   21.80208 12.49171 1.000 37.15587  ? 174 THR   A CA  1 
ATOM   1225 C C   . THR   A 1 167 ? 1.51108   20.87769 13.23944 1.000 46.94594  ? 174 THR   A C   1 
ATOM   1226 O O   . THR   A 1 167 ? 1.83410   19.71633 13.49303 1.000 42.07439  ? 174 THR   A O   1 
ATOM   1227 C CB  . THR   A 1 167 ? 2.27704   21.65557 10.97668 1.000 44.09354  ? 174 THR   A CB  1 
ATOM   1228 O OG1 . THR   A 1 167 ? 2.43556   20.28579 10.59343 1.000 64.08651  ? 174 THR   A OG1 1 
ATOM   1229 C CG2 . THR   A 1 167 ? 3.28194   22.51178 10.21238 1.000 37.24525  ? 174 THR   A CG2 1 
ATOM   1230 N N   . ASP   A 1 168 ? 0.35545   21.40257 13.63315 1.000 41.58566  ? 175 ASP   A N   1 
ATOM   1231 C CA  . ASP   A 1 168 ? -0.57584  20.65889 14.46819 1.000 48.14361  ? 175 ASP   A CA  1 
ATOM   1232 C C   . ASP   A 1 168 ? -1.67662  20.04988 13.61545 1.000 66.78524  ? 175 ASP   A C   1 
ATOM   1233 O O   . ASP   A 1 168 ? -2.34337  20.75610 12.85058 1.000 60.65227  ? 175 ASP   A O   1 
ATOM   1234 C CB  . ASP   A 1 168 ? -1.19045  21.54003 15.55476 1.000 42.00660  ? 175 ASP   A CB  1 
ATOM   1235 C CG  . ASP   A 1 168 ? -2.05969  20.74457 16.50561 1.000 54.97998  ? 175 ASP   A CG  1 
ATOM   1236 O OD1 . ASP   A 1 168 ? -1.70263  19.58078 16.79744 1.000 77.20738  ? 175 ASP   A OD1 1 
ATOM   1237 O OD2 . ASP   A 1 168 ? -3.10222  21.26457 16.94924 1.000 46.12788  ? 175 ASP   A OD2 1 
ATOM   1238 N N   . THR   A 1 169 ? -1.86662  18.74092 13.76512 1.000 70.81245  ? 176 THR   A N   1 
ATOM   1239 C CA  . THR   A 1 169 ? -2.87618  17.98795 13.03561 1.000 87.40741  ? 176 THR   A CA  1 
ATOM   1240 C C   . THR   A 1 169 ? -4.14424  17.74852 13.84779 1.000 76.32321  ? 176 THR   A C   1 
ATOM   1241 O O   . THR   A 1 169 ? -5.08705  17.13942 13.33098 1.000 78.18657  ? 176 THR   A O   1 
ATOM   1242 C CB  . THR   A 1 169 ? -2.29727  16.64378 12.58056 1.000 78.54184  ? 176 THR   A CB  1 
ATOM   1243 O OG1 . THR   A 1 169 ? -1.73542  15.96585 13.71279 1.000 71.78188  ? 176 THR   A OG1 1 
ATOM   1244 C CG2 . THR   A 1 169 ? -1.22737  16.85121 11.51621 1.000 62.94315  ? 176 THR   A CG2 1 
ATOM   1245 N N   . GLY   A 1 170 ? -4.19028  18.20432 15.09941 1.000 62.58747  ? 177 GLY   A N   1 
ATOM   1246 C CA  . GLY   A 1 170 ? -5.36159  18.02278 15.93478 1.000 60.51007  ? 177 GLY   A CA  1 
ATOM   1247 C C   . GLY   A 1 170 ? -6.57194  18.83136 15.50769 1.000 76.88322  ? 177 GLY   A C   1 
ATOM   1248 O O   . GLY   A 1 170 ? -6.67321  19.25942 14.35216 1.000 58.82446  ? 177 GLY   A O   1 
ATOM   1249 N N   . GLU   A 1 171 ? -7.50293  19.03432 16.43626 1.000 71.88762  ? 178 GLU   A N   1 
ATOM   1250 C CA  . GLU   A 1 171 ? -8.70157  19.81283 16.14715 1.000 74.89826  ? 178 GLU   A CA  1 
ATOM   1251 C C   . GLU   A 1 171 ? -8.32090  21.22750 15.70751 1.000 63.62852  ? 178 GLU   A C   1 
ATOM   1252 O O   . GLU   A 1 171 ? -7.53103  21.88826 16.39151 1.000 45.26643  ? 178 GLU   A O   1 
ATOM   1253 C CB  . GLU   A 1 171 ? -9.60182  19.87703 17.38440 1.000 77.13893  ? 178 GLU   A CB  1 
ATOM   1254 C CG  . GLU   A 1 171 ? -11.02820 20.36780 17.11682 1.000 82.23622  ? 178 GLU   A CG  1 
ATOM   1255 C CD  . GLU   A 1 171 ? -12.06468 19.25067 17.14845 1.000 100.96648 ? 178 GLU   A CD  1 
ATOM   1256 O OE1 . GLU   A 1 171 ? -11.96754 18.37421 18.03598 1.000 95.17121  ? 178 GLU   A OE1 1 
ATOM   1257 O OE2 . GLU   A 1 171 ? -12.98667 19.25099 16.29565 1.000 87.10810  ? 178 GLU   A OE2 1 
ATOM   1258 N N   . PRO   A 1 172 ? -8.84924  21.71965 14.58579 1.000 63.27928  ? 179 PRO   A N   1 
ATOM   1259 C CA  . PRO   A 1 172 ? -8.58759  23.11593 14.20157 1.000 51.01803  ? 179 PRO   A CA  1 
ATOM   1260 C C   . PRO   A 1 172 ? -9.21094  24.08596 15.20165 1.000 55.51613  ? 179 PRO   A C   1 
ATOM   1261 O O   . PRO   A 1 172 ? -10.31336 23.86392 15.70273 1.000 51.13818  ? 179 PRO   A O   1 
ATOM   1262 C CB  . PRO   A 1 172 ? -9.23082  23.23593 12.81266 1.000 50.06110  ? 179 PRO   A CB  1 
ATOM   1263 C CG  . PRO   A 1 172 ? -9.55680  21.80966 12.37635 1.000 49.67851  ? 179 PRO   A CG  1 
ATOM   1264 C CD  . PRO   A 1 172 ? -9.70496  21.00627 13.62025 1.000 47.15382  ? 179 PRO   A CD  1 
ATOM   1265 N N   . MET   A 1 173 ? -8.49296  25.17997 15.48195 1.000 41.73218  ? 180 MET   A N   1 
ATOM   1266 C CA  . MET   A 1 173 ? -8.86590  26.11701 16.53793 1.000 48.91315  ? 180 MET   A CA  1 
ATOM   1267 C C   . MET   A 1 173 ? -9.58722  27.36780 16.05465 1.000 45.06348  ? 180 MET   A C   1 
ATOM   1268 O O   . MET   A 1 173 ? -10.16155 28.08482 16.88203 1.000 62.96863  ? 180 MET   A O   1 
ATOM   1269 C CB  . MET   A 1 173 ? -7.62598  26.57641 17.30732 1.000 44.04297  ? 180 MET   A CB  1 
ATOM   1270 C CG  . MET   A 1 173 ? -7.34281  25.80516 18.56286 1.000 57.98244  ? 180 MET   A CG  1 
ATOM   1271 S SD  . MET   A 1 173 ? -6.06936  26.69719 19.45240 1.000 71.41253  ? 180 MET   A SD  1 
ATOM   1272 C CE  . MET   A 1 173 ? -4.79573  26.68438 18.21488 1.000 38.43108  ? 180 MET   A CE  1 
ATOM   1273 N N   . GLY   A 1 174 ? -9.53769  27.67885 14.76762 1.000 41.18026  ? 181 GLY   A N   1 
ATOM   1274 C CA  . GLY   A 1 174 ? -10.12129 28.92065 14.30250 1.000 43.64545  ? 181 GLY   A CA  1 
ATOM   1275 C C   . GLY   A 1 174 ? -9.15264  30.07832 14.43129 1.000 43.55575  ? 181 GLY   A C   1 
ATOM   1276 O O   . GLY   A 1 174 ? -8.70204  30.62029 13.41834 1.000 39.45422  ? 181 GLY   A O   1 
ATOM   1277 N N   . ARG   A 1 175 ? -8.81410  30.44850 15.66924 1.000 31.27241  ? 182 ARG   A N   1 
ATOM   1278 C CA  . ARG   A 1 175 ? -7.86427  31.51172 15.97415 1.000 33.84514  ? 182 ARG   A CA  1 
ATOM   1279 C C   . ARG   A 1 175 ? -7.66449  31.56472 17.48023 1.000 32.66481  ? 182 ARG   A C   1 
ATOM   1280 O O   . ARG   A 1 175 ? -8.63188  31.43939 18.23515 1.000 36.27315  ? 182 ARG   A O   1 
ATOM   1281 C CB  . ARG   A 1 175 ? -8.35107  32.88204 15.47031 1.000 28.29837  ? 182 ARG   A CB  1 
ATOM   1282 C CG  . ARG   A 1 175 ? -7.28632  33.97650 15.58291 1.000 27.64657  ? 182 ARG   A CG  1 
ATOM   1283 C CD  . ARG   A 1 175 ? -7.89805  35.37149 15.56599 1.000 36.00404  ? 182 ARG   A CD  1 
ATOM   1284 N NE  . ARG   A 1 175 ? -8.79004  35.57738 16.70215 1.000 31.13463  ? 182 ARG   A NE  1 
ATOM   1285 C CZ  . ARG   A 1 175 ? -10.11019 35.66394 16.61438 1.000 29.03598  ? 182 ARG   A CZ  1 
ATOM   1286 N NH1 . ARG   A 1 175 ? -10.73492 35.58982 15.44620 1.000 33.20778  ? 182 ARG   A NH1 1 
ATOM   1287 N NH2 . ARG   A 1 175 ? -10.82344 35.82891 17.72512 1.000 30.01120  ? 182 ARG   A NH2 1 
ATOM   1288 N N   . GLY   A 1 176 ? -6.40782  31.74664 17.91232 1.000 25.03436  ? 183 GLY   A N   1 
ATOM   1289 C CA  . GLY   A 1 176 ? -6.15120  31.91376 19.32269 1.000 26.37993  ? 183 GLY   A CA  1 
ATOM   1290 C C   . GLY   A 1 176 ? -5.00772  31.04105 19.80609 1.000 32.29948  ? 183 GLY   A C   1 
ATOM   1291 O O   . GLY   A 1 176 ? -4.15622  30.59472 19.02817 1.000 25.49614  ? 183 GLY   A O   1 
ATOM   1292 N N   . THR   A 1 177 ? -4.97774  30.81774 21.11695 1.000 29.80949  ? 184 THR   A N   1 
ATOM   1293 C CA  . THR   A 1 177 ? -3.87674  30.11615 21.75767 1.000 26.02304  ? 184 THR   A CA  1 
ATOM   1294 C C   . THR   A 1 177 ? -4.44152  29.22708 22.85281 1.000 30.32032  ? 184 THR   A C   1 
ATOM   1295 O O   . THR   A 1 177 ? -5.36843  29.61996 23.57206 1.000 30.97867  ? 184 THR   A O   1 
ATOM   1296 C CB  . THR   A 1 177 ? -2.84216  31.10087 22.33611 1.000 32.00587  ? 184 THR   A CB  1 
ATOM   1297 O OG1 . THR   A 1 177 ? -2.23461  31.83023 21.26472 1.000 32.35602  ? 184 THR   A OG1 1 
ATOM   1298 C CG2 . THR   A 1 177 ? -1.74214  30.36240 23.10820 1.000 30.46358  ? 184 THR   A CG2 1 
ATOM   1299 N N   . LYS   A 1 178 ? -3.88479  28.02267 22.95443 1.000 29.25518  ? 185 LYS   A N   1 
ATOM   1300 C CA  . LYS   A 1 178 ? -4.22455  27.04812 23.98005 1.000 22.83350  ? 185 LYS   A CA  1 
ATOM   1301 C C   . LYS   A 1 178 ? -2.93649  26.62608 24.67520 1.000 33.24894  ? 185 LYS   A C   1 
ATOM   1302 O O   . LYS   A 1 178 ? -2.02907  26.09253 24.03024 1.000 31.56246  ? 185 LYS   A O   1 
ATOM   1303 C CB  . LYS   A 1 178 ? -4.94152  25.85319 23.34558 1.000 33.50310  ? 185 LYS   A CB  1 
ATOM   1304 C CG  . LYS   A 1 178 ? -4.97133  24.61057 24.18757 1.000 58.59090  ? 185 LYS   A CG  1 
ATOM   1305 C CD  . LYS   A 1 178 ? -6.03133  23.61640 23.67983 1.000 51.77885  ? 185 LYS   A CD  1 
ATOM   1306 C CE  . LYS   A 1 178 ? -6.27106  23.75615 22.18514 1.000 59.52155  ? 185 LYS   A CE  1 
ATOM   1307 N NZ  . LYS   A 1 178 ? -7.60558  23.23500 21.78161 1.000 66.08945  ? 185 LYS   A NZ  1 
ATOM   1308 N N   . VAL   A 1 179 ? -2.83862  26.89132 25.97556 1.000 24.38232  ? 186 VAL   A N   1 
ATOM   1309 C CA  . VAL   A 1 179 ? -1.67173  26.50376 26.76308 1.000 28.11062  ? 186 VAL   A CA  1 
ATOM   1310 C C   . VAL   A 1 179 ? -2.04754  25.29719 27.61489 1.000 32.24102  ? 186 VAL   A C   1 
ATOM   1311 O O   . VAL   A 1 179 ? -2.90639  25.39993 28.49897 1.000 30.65563  ? 186 VAL   A O   1 
ATOM   1312 C CB  . VAL   A 1 179 ? -1.17013  27.65774 27.64068 1.000 29.05454  ? 186 VAL   A CB  1 
ATOM   1313 C CG1 . VAL   A 1 179 ? 0.00674   27.18503 28.50851 1.000 26.59901  ? 186 VAL   A CG1 1 
ATOM   1314 C CG2 . VAL   A 1 179 ? -0.79804  28.87766 26.77084 1.000 30.18301  ? 186 VAL   A CG2 1 
ATOM   1315 N N   . ILE   A 1 180 ? -1.40659  24.16001 27.34890 1.000 28.09233  ? 187 ILE   A N   1 
ATOM   1316 C CA  . ILE   A 1 180 ? -1.66050  22.90798 28.06038 1.000 30.02729  ? 187 ILE   A CA  1 
ATOM   1317 C C   . ILE   A 1 180 ? -0.54936  22.70670 29.08129 1.000 30.08133  ? 187 ILE   A C   1 
ATOM   1318 O O   . ILE   A 1 180 ? 0.61633   22.52941 28.70641 1.000 32.79567  ? 187 ILE   A O   1 
ATOM   1319 C CB  . ILE   A 1 180 ? -1.72985  21.71955 27.08927 1.000 37.88226  ? 187 ILE   A CB  1 
ATOM   1320 C CG1 . ILE   A 1 180 ? -2.67523  22.03579 25.92747 1.000 31.18476  ? 187 ILE   A CG1 1 
ATOM   1321 C CG2 . ILE   A 1 180 ? -2.13552  20.43453 27.82193 1.000 30.14737  ? 187 ILE   A CG2 1 
ATOM   1322 C CD1 . ILE   A 1 180 ? -2.53843  21.05363 24.76668 1.000 43.30781  ? 187 ILE   A CD1 1 
ATOM   1323 N N   . LEU   A 1 181 ? -0.90007  22.74140 30.36841 1.000 25.28593  ? 188 LEU   A N   1 
ATOM   1324 C CA  . LEU   A 1 181 ? 0.05945   22.53842 31.45271 1.000 35.93747  ? 188 LEU   A CA  1 
ATOM   1325 C C   . LEU   A 1 181 ? 0.00665   21.07942 31.89573 1.000 29.04227  ? 188 LEU   A C   1 
ATOM   1326 O O   . LEU   A 1 181 ? -0.98189  20.64272 32.49276 1.000 34.97768  ? 188 LEU   A O   1 
ATOM   1327 C CB  . LEU   A 1 181 ? -0.24074  23.46209 32.63095 1.000 22.67610  ? 188 LEU   A CB  1 
ATOM   1328 C CG  . LEU   A 1 181 ? -0.37609  24.94733 32.30566 1.000 28.61964  ? 188 LEU   A CG  1 
ATOM   1329 C CD1 . LEU   A 1 181 ? -0.89758  25.66562 33.51642 1.000 34.79081  ? 188 LEU   A CD1 1 
ATOM   1330 C CD2 . LEU   A 1 181 ? 0.95533   25.55959 31.84839 1.000 26.52600  ? 188 LEU   A CD2 1 
ATOM   1331 N N   . HIS   A 1 182 ? 1.07636   20.33455 31.62933 1.000 28.23362  ? 189 HIS   A N   1 
ATOM   1332 C CA  . HIS   A 1 182 ? 1.20590   18.96604 32.13454 1.000 35.71739  ? 189 HIS   A CA  1 
ATOM   1333 C C   . HIS   A 1 182 ? 1.75391   19.06218 33.55541 1.000 40.09306  ? 189 HIS   A C   1 
ATOM   1334 O O   . HIS   A 1 182 ? 2.94433   19.30939 33.75703 1.000 34.86379  ? 189 HIS   A O   1 
ATOM   1335 C CB  . HIS   A 1 182 ? 2.10248   18.14953 31.20954 1.000 36.87224  ? 189 HIS   A CB  1 
ATOM   1336 C CG  . HIS   A 1 182 ? 1.68659   18.22012 29.77207 1.000 38.78961  ? 189 HIS   A CG  1 
ATOM   1337 N ND1 . HIS   A 1 182 ? 0.94112   17.23431 29.16055 1.000 35.42077  ? 189 HIS   A ND1 1 
ATOM   1338 C CD2 . HIS   A 1 182 ? 1.87387   19.18470 28.83772 1.000 39.13778  ? 189 HIS   A CD2 1 
ATOM   1339 C CE1 . HIS   A 1 182 ? 0.70631   17.57828 27.90622 1.000 39.82562  ? 189 HIS   A CE1 1 
ATOM   1340 N NE2 . HIS   A 1 182 ? 1.25641   18.76089 27.68612 1.000 37.48484  ? 189 HIS   A NE2 1 
ATOM   1341 N N   . LEU   A 1 183 ? 0.88268   18.90138 34.55130 1.000 31.22774  ? 190 LEU   A N   1 
ATOM   1342 C CA  . LEU   A 1 183 ? 1.20959   19.36647 35.89626 1.000 39.01274  ? 190 LEU   A CA  1 
ATOM   1343 C C   . LEU   A 1 183 ? 2.15591   18.41493 36.61811 1.000 37.25186  ? 190 LEU   A C   1 
ATOM   1344 O O   . LEU   A 1 183 ? 2.16387   17.20420 36.37984 1.000 33.15926  ? 190 LEU   A O   1 
ATOM   1345 C CB  . LEU   A 1 183 ? -0.06207  19.55464 36.73154 1.000 31.09907  ? 190 LEU   A CB  1 
ATOM   1346 C CG  . LEU   A 1 183 ? -1.02409  20.67677 36.31290 1.000 30.87340  ? 190 LEU   A CG  1 
ATOM   1347 C CD1 . LEU   A 1 183 ? -2.20325  20.74747 37.26382 1.000 32.78808  ? 190 LEU   A CD1 1 
ATOM   1348 C CD2 . LEU   A 1 183 ? -0.32609  22.04374 36.24892 1.000 26.05057  ? 190 LEU   A CD2 1 
ATOM   1349 N N   . LYS   A 1 184 ? 2.96070   18.98142 37.51609 1.000 35.06613  ? 191 LYS   A N   1 
ATOM   1350 C CA  . LYS   A 1 184 ? 3.78573   18.15192 38.37907 1.000 39.86375  ? 191 LYS   A CA  1 
ATOM   1351 C C   . LYS   A 1 184 ? 2.89530   17.31720 39.29264 1.000 39.21520  ? 191 LYS   A C   1 
ATOM   1352 O O   . LYS   A 1 184 ? 1.74184   17.66399 39.57449 1.000 35.16716  ? 191 LYS   A O   1 
ATOM   1353 C CB  . LYS   A 1 184 ? 4.74534   19.00470 39.21628 1.000 42.30932  ? 191 LYS   A CB  1 
ATOM   1354 C CG  . LYS   A 1 184 ? 5.78726   19.79059 38.41340 1.000 38.02897  ? 191 LYS   A CG  1 
ATOM   1355 C CD  . LYS   A 1 184 ? 6.49216   20.81986 39.28718 1.000 35.72430  ? 191 LYS   A CD  1 
ATOM   1356 C CE  . LYS   A 1 184 ? 7.45169   21.68172 38.46485 1.000 55.52585  ? 191 LYS   A CE  1 
ATOM   1357 N NZ  . LYS   A 1 184 ? 8.05599   22.82140 39.23547 1.000 40.99804  ? 191 LYS   A NZ  1 
ATOM   1358 N N   . GLU   A 1 185 ? 3.45901   16.20721 39.76486 1.000 38.62309  ? 192 GLU   A N   1 
ATOM   1359 C CA  . GLU   A 1 185 ? 2.69767   15.25355 40.56111 1.000 50.50520  ? 192 GLU   A CA  1 
ATOM   1360 C C   . GLU   A 1 185 ? 2.14778   15.88577 41.83794 1.000 51.74525  ? 192 GLU   A C   1 
ATOM   1361 O O   . GLU   A 1 185 ? 1.02557   15.57460 42.25838 1.000 46.11181  ? 192 GLU   A O   1 
ATOM   1362 C CB  . GLU   A 1 185 ? 3.58091   14.05227 40.89141 1.000 46.85728  ? 192 GLU   A CB  1 
ATOM   1363 C CG  . GLU   A 1 185 ? 2.82466   12.80098 41.25411 1.000 68.25699  ? 192 GLU   A CG  1 
ATOM   1364 C CD  . GLU   A 1 185 ? 3.71007   11.56786 41.21617 1.000 85.61956  ? 192 GLU   A CD  1 
ATOM   1365 O OE1 . GLU   A 1 185 ? 4.05747   11.05143 42.30069 1.000 83.56733  ? 192 GLU   A OE1 1 
ATOM   1366 O OE2 . GLU   A 1 185 ? 4.05874   11.11799 40.09932 1.000 80.15558  ? 192 GLU   A OE2 1 
ATOM   1367 N N   . ASP   A 1 186 ? 2.91902   16.76424 42.47910 1.000 36.95222  ? 193 ASP   A N   1 
ATOM   1368 C CA  . ASP   A 1 186 ? 2.48906   17.35749 43.73963 1.000 45.84076  ? 193 ASP   A CA  1 
ATOM   1369 C C   . ASP   A 1 186 ? 1.72248   18.66533 43.55232 1.000 44.23549  ? 193 ASP   A C   1 
ATOM   1370 O O   . ASP   A 1 186 ? 1.54435   19.41336 44.52264 1.000 39.90859  ? 193 ASP   A O   1 
ATOM   1371 C CB  . ASP   A 1 186 ? 3.68781   17.57545 44.66923 1.000 39.01797  ? 193 ASP   A CB  1 
ATOM   1372 C CG  . ASP   A 1 186 ? 4.80281   18.38922 44.02895 1.000 58.94182  ? 193 ASP   A CG  1 
ATOM   1373 O OD1 . ASP   A 1 186 ? 4.73416   18.68979 42.81870 1.000 59.42855  ? 193 ASP   A OD1 1 
ATOM   1374 O OD2 . ASP   A 1 186 ? 5.76347   18.72924 44.75096 1.000 74.49417  ? 193 ASP   A OD2 1 
ATOM   1375 N N   . GLN   A 1 187 ? 1.24529   18.94915 42.33902 1.000 33.06979  ? 194 GLN   A N   1 
ATOM   1376 C CA  . GLN   A 1 187 ? 0.54220   20.19749 42.06813 1.000 30.28193  ? 194 GLN   A CA  1 
ATOM   1377 C C   . GLN   A 1 187 ? -0.87422  19.97505 41.55067 1.000 30.10853  ? 194 GLN   A C   1 
ATOM   1378 O O   . GLN   A 1 187 ? -1.41524  20.85702 40.87598 1.000 32.69707  ? 194 GLN   A O   1 
ATOM   1379 C CB  . GLN   A 1 187 ? 1.32557   21.05789 41.06828 1.000 36.14388  ? 194 GLN   A CB  1 
ATOM   1380 C CG  . GLN   A 1 187 ? 2.76434   21.36965 41.45273 1.000 32.87093  ? 194 GLN   A CG  1 
ATOM   1381 C CD  . GLN   A 1 187 ? 2.87060   22.15576 42.74789 1.000 39.02178  ? 194 GLN   A CD  1 
ATOM   1382 O OE1 . GLN   A 1 187 ? 2.03586   23.01251 43.03978 1.000 36.84362  ? 194 GLN   A OE1 1 
ATOM   1383 N NE2 . GLN   A 1 187 ? 3.90638   21.86968 43.52975 1.000 38.45472  ? 194 GLN   A NE2 1 
ATOM   1384 N N   . THR   A 1 188 ? -1.49803  18.82741 41.84553 1.000 33.20807  ? 195 THR   A N   1 
ATOM   1385 C CA  . THR   A 1 188 ? -2.84330  18.59028 41.32222 1.000 39.81557  ? 195 THR   A CA  1 
ATOM   1386 C C   . THR   A 1 188 ? -3.90302  19.46882 41.97794 1.000 39.48717  ? 195 THR   A C   1 
ATOM   1387 O O   . THR   A 1 188 ? -5.05956  19.43722 41.54112 1.000 36.84372  ? 195 THR   A O   1 
ATOM   1388 C CB  . THR   A 1 188 ? -3.26089  17.12410 41.47929 1.000 38.95793  ? 195 THR   A CB  1 
ATOM   1389 O OG1 . THR   A 1 188 ? -3.17898  16.73850 42.85381 1.000 43.23223  ? 195 THR   A OG1 1 
ATOM   1390 C CG2 . THR   A 1 188 ? -2.37189  16.21487 40.64224 1.000 49.37370  ? 195 THR   A CG2 1 
ATOM   1391 N N   . GLU   A 1 189 ? -3.54963  20.24561 43.00665 1.000 37.29385  ? 196 GLU   A N   1 
ATOM   1392 C CA  . GLU   A 1 189 ? -4.53274  21.14139 43.60588 1.000 31.97600  ? 196 GLU   A CA  1 
ATOM   1393 C C   . GLU   A 1 189 ? -5.09805  22.12258 42.58244 1.000 31.03523  ? 196 GLU   A C   1 
ATOM   1394 O O   . GLU   A 1 189 ? -6.24200  22.56857 42.72020 1.000 34.60637  ? 196 GLU   A O   1 
ATOM   1395 C CB  . GLU   A 1 189 ? -3.91633  21.89457 44.78825 1.000 36.01707  ? 196 GLU   A CB  1 
ATOM   1396 C CG  . GLU   A 1 189 ? -2.90834  22.97459 44.40617 1.000 39.08642  ? 196 GLU   A CG  1 
ATOM   1397 C CD  . GLU   A 1 189 ? -2.28264  23.64382 45.62345 1.000 57.08085  ? 196 GLU   A CD  1 
ATOM   1398 O OE1 . GLU   A 1 189 ? -2.85467  24.63966 46.12931 1.000 46.71766  ? 196 GLU   A OE1 1 
ATOM   1399 O OE2 . GLU   A 1 189 ? -1.22335  23.16490 46.07434 1.000 55.41670  ? 196 GLU   A OE2 1 
ATOM   1400 N N   . TYR   A 1 190 ? -4.33178  22.45640 41.54317 1.000 30.01905  ? 197 TYR   A N   1 
ATOM   1401 C CA  . TYR   A 1 190 ? -4.79339  23.39738 40.52478 1.000 37.16518  ? 197 TYR   A CA  1 
ATOM   1402 C C   . TYR   A 1 190 ? -5.71895  22.75160 39.49219 1.000 41.38126  ? 197 TYR   A C   1 
ATOM   1403 O O   . TYR   A 1 190 ? -6.04889  23.38746 38.48548 1.000 31.29039  ? 197 TYR   A O   1 
ATOM   1404 C CB  . TYR   A 1 190 ? -3.58799  24.06710 39.85497 1.000 33.99625  ? 197 TYR   A CB  1 
ATOM   1405 C CG  . TYR   A 1 190 ? -2.70814  24.74569 40.88372 1.000 25.75592  ? 197 TYR   A CG  1 
ATOM   1406 C CD1 . TYR   A 1 190 ? -3.14790  25.88004 41.55436 1.000 30.33030  ? 197 TYR   A CD1 1 
ATOM   1407 C CD2 . TYR   A 1 190 ? -1.46787  24.22258 41.22207 1.000 32.49957  ? 197 TYR   A CD2 1 
ATOM   1408 C CE1 . TYR   A 1 190 ? -2.36829  26.49021 42.52341 1.000 33.42006  ? 197 TYR   A CE1 1 
ATOM   1409 C CE2 . TYR   A 1 190 ? -0.67404  24.82973 42.19114 1.000 37.23665  ? 197 TYR   A CE2 1 
ATOM   1410 C CZ  . TYR   A 1 190 ? -1.13288  25.96291 42.83686 1.000 41.31732  ? 197 TYR   A CZ  1 
ATOM   1411 O OH  . TYR   A 1 190 ? -0.36031  26.56710 43.80130 1.000 38.77997  ? 197 TYR   A OH  1 
ATOM   1412 N N   . LEU   A 1 191 ? -6.15000  21.51459 39.72704 1.000 34.32178  ? 198 LEU   A N   1 
ATOM   1413 C CA  . LEU   A 1 191 ? -7.24625  20.90589 38.98734 1.000 39.66213  ? 198 LEU   A CA  1 
ATOM   1414 C C   . LEU   A 1 191 ? -8.55644  20.92800 39.75833 1.000 41.99241  ? 198 LEU   A C   1 
ATOM   1415 O O   . LEU   A 1 191 ? -9.56111  20.41902 39.25438 1.000 51.56109  ? 198 LEU   A O   1 
ATOM   1416 C CB  . LEU   A 1 191 ? -6.90917  19.45722 38.61680 1.000 33.79632  ? 198 LEU   A CB  1 
ATOM   1417 C CG  . LEU   A 1 191 ? -5.58020  19.22406 37.90171 1.000 36.96547  ? 198 LEU   A CG  1 
ATOM   1418 C CD1 . LEU   A 1 191 ? -5.27610  17.73795 37.81926 1.000 51.34916  ? 198 LEU   A CD1 1 
ATOM   1419 C CD2 . LEU   A 1 191 ? -5.61352  19.84960 36.52899 1.000 38.15896  ? 198 LEU   A CD2 1 
ATOM   1420 N N   . GLU   A 1 192 ? -8.56503  21.46410 40.97513 1.000 35.52566  ? 199 GLU   A N   1 
ATOM   1421 C CA  . GLU   A 1 192 ? -9.77845  21.53254 41.77832 1.000 45.95287  ? 199 GLU   A CA  1 
ATOM   1422 C C   . GLU   A 1 192 ? -10.56015 22.79039 41.43589 1.000 37.24534  ? 199 GLU   A C   1 
ATOM   1423 O O   . GLU   A 1 192 ? -9.98537  23.87776 41.29544 1.000 33.33624  ? 199 GLU   A O   1 
ATOM   1424 C CB  . GLU   A 1 192 ? -9.45435  21.51482 43.27502 1.000 44.96030  ? 199 GLU   A CB  1 
ATOM   1425 C CG  . GLU   A 1 192 ? -8.65992  20.30418 43.75161 1.000 50.96961  ? 199 GLU   A CG  1 
ATOM   1426 C CD  . GLU   A 1 192 ? -9.41196  18.99631 43.57024 1.000 72.88802  ? 199 GLU   A CD  1 
ATOM   1427 O OE1 . GLU   A 1 192 ? -10.66468 19.02458 43.54861 1.000 74.57880  ? 199 GLU   A OE1 1 
ATOM   1428 O OE2 . GLU   A 1 192 ? -8.75314  17.93677 43.45679 1.000 78.23349  ? 199 GLU   A OE2 1 
ATOM   1429 N N   . GLU   A 1 193 ? -11.87957 22.63325 41.32012 1.000 38.30022  ? 200 GLU   A N   1 
ATOM   1430 C CA  . GLU   A 1 193 ? -12.73514 23.75034 40.93627 1.000 44.52714  ? 200 GLU   A CA  1 
ATOM   1431 C C   . GLU   A 1 193 ? -12.68113 24.87823 41.96739 1.000 40.16717  ? 200 GLU   A C   1 
ATOM   1432 O O   . GLU   A 1 193 ? -12.52771 26.05136 41.60975 1.000 41.71035  ? 200 GLU   A O   1 
ATOM   1433 C CB  . GLU   A 1 193 ? -14.16817 23.25835 40.73480 1.000 43.00567  ? 200 GLU   A CB  1 
ATOM   1434 C CG  . GLU   A 1 193 ? -15.21344 24.36628 40.74081 1.000 59.30512  ? 200 GLU   A CG  1 
ATOM   1435 C CD  . GLU   A 1 193 ? -16.57748 23.90166 40.24899 1.000 70.89224  ? 200 GLU   A CD  1 
ATOM   1436 O OE1 . GLU   A 1 193 ? -16.86627 22.68533 40.32786 1.000 75.64071  ? 200 GLU   A OE1 1 
ATOM   1437 O OE2 . GLU   A 1 193 ? -17.36589 24.76080 39.79371 1.000 81.64455  ? 200 GLU   A OE2 1 
ATOM   1438 N N   . ARG   A 1 194 ? -12.80190 24.54702 43.25686 1.000 40.99529  ? 201 ARG   A N   1 
ATOM   1439 C CA  . ARG   A 1 194 ? -12.81226 25.60369 44.26307 1.000 35.98219  ? 201 ARG   A CA  1 
ATOM   1440 C C   . ARG   A 1 194 ? -11.45158 26.27851 44.38586 1.000 33.31211  ? 201 ARG   A C   1 
ATOM   1441 O O   . ARG   A 1 194 ? -11.38259 27.46179 44.72864 1.000 38.97792  ? 201 ARG   A O   1 
ATOM   1442 C CB  . ARG   A 1 194 ? -13.27375 25.05323 45.61504 1.000 37.09660  ? 201 ARG   A CB  1 
ATOM   1443 C CG  . ARG   A 1 194 ? -12.51742 23.83231 46.09044 1.000 57.73197  ? 201 ARG   A CG  1 
ATOM   1444 C CD  . ARG   A 1 194 ? -13.21047 23.21554 47.29779 1.000 57.05406  ? 201 ARG   A CD  1 
ATOM   1445 N NE  . ARG   A 1 194 ? -12.34647 22.26873 47.98988 1.000 58.73308  ? 201 ARG   A NE  1 
ATOM   1446 C CZ  . ARG   A 1 194 ? -12.50714 21.89782 49.25335 1.000 72.71482  ? 201 ARG   A CZ  1 
ATOM   1447 N NH1 . ARG   A 1 194 ? -13.51228 22.35510 49.98639 1.000 63.71691  ? 201 ARG   A NH1 1 
ATOM   1448 N NH2 . ARG   A 1 194 ? -11.63284 21.05598 49.79819 1.000 70.27991  ? 201 ARG   A NH2 1 
ATOM   1449 N N   . ARG   A 1 195 ? -10.36577 25.56059 44.09471 1.000 37.87216  ? 202 ARG   A N   1 
ATOM   1450 C CA  . ARG   A 1 195 ? -9.04645  26.18598 44.09263 1.000 36.20056  ? 202 ARG   A CA  1 
ATOM   1451 C C   . ARG   A 1 195 ? -8.90911  27.17378 42.93553 1.000 42.16228  ? 202 ARG   A C   1 
ATOM   1452 O O   . ARG   A 1 195 ? -8.49042  28.32166 43.13192 1.000 30.01862  ? 202 ARG   A O   1 
ATOM   1453 C CB  . ARG   A 1 195 ? -7.96043  25.11392 44.02389 1.000 33.80271  ? 202 ARG   A CB  1 
ATOM   1454 C CG  . ARG   A 1 195 ? -6.54702  25.64551 44.11819 1.000 33.44854  ? 202 ARG   A CG  1 
ATOM   1455 C CD  . ARG   A 1 195 ? -6.25688  26.23416 45.49872 1.000 33.97187  ? 202 ARG   A CD  1 
ATOM   1456 N NE  . ARG   A 1 195 ? -4.85277  26.60119 45.63502 1.000 36.33011  ? 202 ARG   A NE  1 
ATOM   1457 C CZ  . ARG   A 1 195 ? -4.41565  27.84041 45.82359 1.000 43.25981  ? 202 ARG   A CZ  1 
ATOM   1458 N NH1 . ARG   A 1 195 ? -5.25067  28.86163 45.91885 1.000 32.13663  ? 202 ARG   A NH1 1 
ATOM   1459 N NH2 . ARG   A 1 195 ? -3.10909  28.05865 45.92247 1.000 34.78650  ? 202 ARG   A NH2 1 
ATOM   1460 N N   . ILE   A 1 196 ? -9.26241  26.74535 41.71887 1.000 29.64705  ? 203 ILE   A N   1 
ATOM   1461 C CA  . ILE   A 1 196 ? -9.16546  27.62548 40.55702 1.000 30.41362  ? 203 ILE   A CA  1 
ATOM   1462 C C   . ILE   A 1 196 ? -10.04468 28.85708 40.73647 1.000 31.89548  ? 203 ILE   A C   1 
ATOM   1463 O O   . ILE   A 1 196 ? -9.63752  29.98024 40.40067 1.000 29.82212  ? 203 ILE   A O   1 
ATOM   1464 C CB  . ILE   A 1 196 ? -9.52697  26.86270 39.26822 1.000 34.20166  ? 203 ILE   A CB  1 
ATOM   1465 C CG1 . ILE   A 1 196 ? -8.53146  25.73709 39.01930 1.000 31.47865  ? 203 ILE   A CG1 1 
ATOM   1466 C CG2 . ILE   A 1 196 ? -9.52811  27.80602 38.06662 1.000 28.59673  ? 203 ILE   A CG2 1 
ATOM   1467 C CD1 . ILE   A 1 196 ? -9.02816  24.71416 38.02387 1.000 38.02864  ? 203 ILE   A CD1 1 
ATOM   1468 N N   . LYS   A 1 197 ? -11.26636 28.66625 41.25182 1.000 27.93850  ? 204 LYS   A N   1 
ATOM   1469 C CA  . LYS   A 1 197 ? -12.14924 29.80228 41.50319 1.000 36.28647  ? 204 LYS   A CA  1 
ATOM   1470 C C   . LYS   A 1 197 ? -11.49310 30.79688 42.44957 1.000 37.43623  ? 204 LYS   A C   1 
ATOM   1471 O O   . LYS   A 1 197 ? -11.51804 32.00913 42.21157 1.000 35.06066  ? 204 LYS   A O   1 
ATOM   1472 C CB  . LYS   A 1 197 ? -13.47743 29.33090 42.09464 1.000 30.16664  ? 204 LYS   A CB  1 
ATOM   1473 C CG  . LYS   A 1 197 ? -14.47584 28.75622 41.11955 1.000 45.44573  ? 204 LYS   A CG  1 
ATOM   1474 C CD  . LYS   A 1 197 ? -15.80114 28.52017 41.83785 1.000 50.34007  ? 204 LYS   A CD  1 
ATOM   1475 C CE  . LYS   A 1 197 ? -16.81661 27.79430 40.96722 1.000 56.58264  ? 204 LYS   A CE  1 
ATOM   1476 N NZ  . LYS   A 1 197 ? -17.98823 27.35422 41.78293 1.000 62.37669  ? 204 LYS   A NZ  1 
ATOM   1477 N N   . GLU   A 1 198 ? -10.91977 30.28886 43.54658 1.000 34.86122  ? 205 GLU   A N   1 
ATOM   1478 C CA  . GLU   A 1 198 ? -10.22425 31.13614 44.51093 1.000 38.27941  ? 205 GLU   A CA  1 
ATOM   1479 C C   . GLU   A 1 198 ? -9.13440  31.97299 43.84861 1.000 36.33973  ? 205 GLU   A C   1 
ATOM   1480 O O   . GLU   A 1 198 ? -8.99343  33.16966 44.13533 1.000 33.56627  ? 205 GLU   A O   1 
ATOM   1481 C CB  . GLU   A 1 198 ? -9.62082  30.26258 45.60795 1.000 31.12145  ? 205 GLU   A CB  1 
ATOM   1482 C CG  . GLU   A 1 198 ? -8.94777  31.01977 46.72325 1.000 34.72146  ? 205 GLU   A CG  1 
ATOM   1483 C CD  . GLU   A 1 198 ? -8.24174  30.07201 47.68444 1.000 51.54375  ? 205 GLU   A CD  1 
ATOM   1484 O OE1 . GLU   A 1 198 ? -7.71174  29.04132 47.20954 1.000 44.36836  ? 205 GLU   A OE1 1 
ATOM   1485 O OE2 . GLU   A 1 198 ? -8.23901  30.33916 48.90732 1.000 44.86567  ? 205 GLU   A OE2 1 
ATOM   1486 N N   . ILE   A 1 199 ? -8.36056  31.35977 42.95316 1.000 32.54674  ? 206 ILE   A N   1 
ATOM   1487 C CA  . ILE   A 1 199 ? -7.21452  32.04175 42.36190 1.000 32.23915  ? 206 ILE   A CA  1 
ATOM   1488 C C   . ILE   A 1 199 ? -7.66667  33.11057 41.37275 1.000 39.30309  ? 206 ILE   A C   1 
ATOM   1489 O O   . ILE   A 1 199 ? -7.10260  34.21280 41.32501 1.000 33.76164  ? 206 ILE   A O   1 
ATOM   1490 C CB  . ILE   A 1 199 ? -6.28869  31.01138 41.70109 1.000 27.35865  ? 206 ILE   A CB  1 
ATOM   1491 C CG1 . ILE   A 1 199 ? -5.76403  30.03252 42.75494 1.000 36.77583  ? 206 ILE   A CG1 1 
ATOM   1492 C CG2 . ILE   A 1 199 ? -5.14009  31.70569 40.98155 1.000 28.96867  ? 206 ILE   A CG2 1 
ATOM   1493 C CD1 . ILE   A 1 199 ? -4.90198  28.95284 42.16969 1.000 31.57560  ? 206 ILE   A CD1 1 
ATOM   1494 N N   . VAL   A 1 200 ? -8.67294  32.79520 40.55564 1.000 31.36788  ? 207 VAL   A N   1 
ATOM   1495 C CA  . VAL   A 1 200 ? -9.20392  33.77238 39.61029 1.000 24.95411  ? 207 VAL   A CA  1 
ATOM   1496 C C   . VAL   A 1 200 ? -9.81116  34.95323 40.36501 1.000 28.88017  ? 207 VAL   A C   1 
ATOM   1497 O O   . VAL   A 1 200 ? -9.58253  36.11693 40.01846 1.000 33.67121  ? 207 VAL   A O   1 
ATOM   1498 C CB  . VAL   A 1 200 ? -10.22422 33.10424 38.66718 1.000 28.99675  ? 207 VAL   A CB  1 
ATOM   1499 C CG1 . VAL   A 1 200 ? -11.00169 34.15367 37.88041 1.000 30.74789  ? 207 VAL   A CG1 1 
ATOM   1500 C CG2 . VAL   A 1 200 ? -9.52029  32.12947 37.70785 1.000 25.88746  ? 207 VAL   A CG2 1 
ATOM   1501 N N   . LYS   A 1 201 ? -10.58243 34.66437 41.41705 1.000 31.27024  ? 208 LYS   A N   1 
ATOM   1502 C CA  . LYS   A 1 201 ? -11.18278 35.71566 42.23609 1.000 32.86492  ? 208 LYS   A CA  1 
ATOM   1503 C C   . LYS   A 1 201 ? -10.11924 36.61643 42.85658 1.000 35.73441  ? 208 LYS   A C   1 
ATOM   1504 O O   . LYS   A 1 201 ? -10.25106 37.84635 42.85547 1.000 44.69608  ? 208 LYS   A O   1 
ATOM   1505 C CB  . LYS   A 1 201 ? -12.04902 35.08365 43.33141 1.000 41.60778  ? 208 LYS   A CB  1 
ATOM   1506 C CG  . LYS   A 1 201 ? -13.04439 36.03522 43.98410 1.000 41.28642  ? 208 LYS   A CG  1 
ATOM   1507 C CD  . LYS   A 1 201 ? -14.39517 35.92554 43.29495 1.000 76.38289  ? 208 LYS   A CD  1 
ATOM   1508 C CE  . LYS   A 1 201 ? -14.99523 37.29384 42.99130 1.000 82.12798  ? 208 LYS   A CE  1 
ATOM   1509 N NZ  . LYS   A 1 201 ? -15.91491 37.24535 41.81054 1.000 63.01508  ? 208 LYS   A NZ  1 
ATOM   1510 N N   . LYS   A 1 202 ? -9.05322  36.02064 43.38317 1.000 39.29137  ? 209 LYS   A N   1 
ATOM   1511 C CA  . LYS   A 1 202 ? -8.00805  36.79587 44.04142 1.000 37.65845  ? 209 LYS   A CA  1 
ATOM   1512 C C   . LYS   A 1 202 ? -7.22992  37.65707 43.04573 1.000 40.40912  ? 209 LYS   A C   1 
ATOM   1513 O O   . LYS   A 1 202 ? -6.99320  38.84275 43.29881 1.000 32.51314  ? 209 LYS   A O   1 
ATOM   1514 C CB  . LYS   A 1 202 ? -7.07435  35.83932 44.78129 1.000 36.78015  ? 209 LYS   A CB  1 
ATOM   1515 C CG  . LYS   A 1 202 ? -6.00562  36.47811 45.63307 1.000 42.90371  ? 209 LYS   A CG  1 
ATOM   1516 C CD  . LYS   A 1 202 ? -5.12972  35.38066 46.22572 1.000 55.41373  ? 209 LYS   A CD  1 
ATOM   1517 C CE  . LYS   A 1 202 ? -4.09917  35.91848 47.19874 1.000 53.40215  ? 209 LYS   A CE  1 
ATOM   1518 N NZ  . LYS   A 1 202 ? -3.47607  34.79202 47.96526 1.000 67.45166  ? 209 LYS   A NZ  1 
ATOM   1519 N N   . HIS   A 1 203 ? -6.86166  37.09182 41.89053 1.000 34.99481  ? 210 HIS   A N   1 
ATOM   1520 C CA  . HIS   A 1 203 ? -5.84024  37.67279 41.02549 1.000 35.67218  ? 210 HIS   A CA  1 
ATOM   1521 C C   . HIS   A 1 203 ? -6.34261  38.19919 39.68849 1.000 38.07790  ? 210 HIS   A C   1 
ATOM   1522 O O   . HIS   A 1 203 ? -5.62142  38.96800 39.04322 1.000 37.84487  ? 210 HIS   A O   1 
ATOM   1523 C CB  . HIS   A 1 203 ? -4.74314  36.63872 40.73118 1.000 32.39693  ? 210 HIS   A CB  1 
ATOM   1524 C CG  . HIS   A 1 203 ? -3.92846  36.26197 41.92692 1.000 36.68689  ? 210 HIS   A CG  1 
ATOM   1525 N ND1 . HIS   A 1 203 ? -3.17031  37.17546 42.62542 1.000 40.45532  ? 210 HIS   A ND1 1 
ATOM   1526 C CD2 . HIS   A 1 203 ? -3.72864  35.06556 42.53076 1.000 37.82166  ? 210 HIS   A CD2 1 
ATOM   1527 C CE1 . HIS   A 1 203 ? -2.55449  36.56398 43.62130 1.000 50.21502  ? 210 HIS   A CE1 1 
ATOM   1528 N NE2 . HIS   A 1 203 ? -2.87495  35.28229 43.58500 1.000 52.43733  ? 210 HIS   A NE2 1 
ATOM   1529 N N   . SER   A 1 204 ? -7.53442  37.80530 39.24434 1.000 36.47850  ? 211 SER   A N   1 
ATOM   1530 C CA  . SER   A 1 204 ? -7.95905  38.09218 37.88120 1.000 35.72303  ? 211 SER   A CA  1 
ATOM   1531 C C   . SER   A 1 204 ? -9.39613  38.59852 37.82995 1.000 37.68269  ? 211 SER   A C   1 
ATOM   1532 O O   . SER   A 1 204 ? -10.07258 38.45365 36.80841 1.000 34.19919  ? 211 SER   A O   1 
ATOM   1533 C CB  . SER   A 1 204 ? -7.79453  36.84934 37.00108 1.000 40.58741  ? 211 SER   A CB  1 
ATOM   1534 O OG  . SER   A 1 204 ? -6.43187  36.43845 36.94515 1.000 36.20785  ? 211 SER   A OG  1 
ATOM   1535 N N   . GLN   A 1 205 ? -9.87112  39.22124 38.91120 1.000 36.56265  ? 212 GLN   A N   1 
ATOM   1536 C CA  . GLN   A 1 205 ? -11.28954 39.56870 38.99144 1.000 42.52951  ? 212 GLN   A CA  1 
ATOM   1537 C C   . GLN   A 1 205 ? -11.70544 40.61495 37.95467 1.000 43.24919  ? 212 GLN   A C   1 
ATOM   1538 O O   . GLN   A 1 205 ? -12.86651 40.62963 37.53291 1.000 42.21511  ? 212 GLN   A O   1 
ATOM   1539 C CB  . GLN   A 1 205 ? -11.63486 40.06099 40.39729 1.000 44.87973  ? 212 GLN   A CB  1 
ATOM   1540 C CG  . GLN   A 1 205 ? -10.81767 41.24440 40.85189 1.000 51.24521  ? 212 GLN   A CG  1 
ATOM   1541 C CD  . GLN   A 1 205 ? -10.97786 41.52190 42.33263 1.000 71.82851  ? 212 GLN   A CD  1 
ATOM   1542 O OE1 . GLN   A 1 205 ? -10.05427 42.01013 42.99079 1.000 82.84997  ? 212 GLN   A OE1 1 
ATOM   1543 N NE2 . GLN   A 1 205 ? -12.15981 41.21995 42.86486 1.000 54.25797  ? 212 GLN   A NE2 1 
ATOM   1544 N N   . PHE   A 1 206 ? -10.78873 41.48342 37.51861 1.000 37.54365  ? 213 PHE   A N   1 
ATOM   1545 C CA  . PHE   A 1 206 ? -11.14084 42.59326 36.63672 1.000 36.12404  ? 213 PHE   A CA  1 
ATOM   1546 C C   . PHE   A 1 206 ? -10.71405 42.38868 35.18600 1.000 36.89793  ? 213 PHE   A C   1 
ATOM   1547 O O   . PHE   A 1 206 ? -10.71685 43.35487 34.41079 1.000 36.53856  ? 213 PHE   A O   1 
ATOM   1548 C CB  . PHE   A 1 206 ? -10.55619 43.89771 37.18467 1.000 38.22150  ? 213 PHE   A CB  1 
ATOM   1549 C CG  . PHE   A 1 206 ? -11.11008 44.27150 38.51919 1.000 40.87538  ? 213 PHE   A CG  1 
ATOM   1550 C CD1 . PHE   A 1 206 ? -12.47960 44.36148 38.70952 1.000 41.76062  ? 213 PHE   A CD1 1 
ATOM   1551 C CD2 . PHE   A 1 206 ? -10.27345 44.49363 39.59472 1.000 42.79276  ? 213 PHE   A CD2 1 
ATOM   1552 C CE1 . PHE   A 1 206 ? -13.00574 44.68641 39.94892 1.000 44.56822  ? 213 PHE   A CE1 1 
ATOM   1553 C CE2 . PHE   A 1 206 ? -10.79263 44.81659 40.82994 1.000 54.58286  ? 213 PHE   A CE2 1 
ATOM   1554 C CZ  . PHE   A 1 206 ? -12.15882 44.91910 41.00854 1.000 51.97821  ? 213 PHE   A CZ  1 
ATOM   1555 N N   . ILE   A 1 207 ? -10.34929 41.16100 34.79681 1.000 34.84402  ? 214 ILE   A N   1 
ATOM   1556 C CA  . ILE   A 1 207 ? -10.08034 40.87094 33.39430 1.000 30.42141  ? 214 ILE   A CA  1 
ATOM   1557 C C   . ILE   A 1 207 ? -11.31959 41.17579 32.56419 1.000 32.87876  ? 214 ILE   A C   1 
ATOM   1558 O O   . ILE   A 1 207 ? -12.44315 40.81565 32.93412 1.000 34.15487  ? 214 ILE   A O   1 
ATOM   1559 C CB  . ILE   A 1 207 ? -9.63334  39.41230 33.22870 1.000 29.15053  ? 214 ILE   A CB  1 
ATOM   1560 C CG1 . ILE   A 1 207 ? -8.33151  39.17226 33.98973 1.000 29.85807  ? 214 ILE   A CG1 1 
ATOM   1561 C CG2 . ILE   A 1 207 ? -9.46922  39.05908 31.75810 1.000 30.53767  ? 214 ILE   A CG2 1 
ATOM   1562 C CD1 . ILE   A 1 207 ? -7.13673  39.88603 33.39939 1.000 30.38941  ? 214 ILE   A CD1 1 
ATOM   1563 N N   . GLY   A 1 208 ? -11.11944 41.85328 31.43767 1.000 31.16534  ? 215 GLY   A N   1 
ATOM   1564 C CA  . GLY   A 1 208 ? -12.22916 42.39653 30.67815 1.000 33.16875  ? 215 GLY   A CA  1 
ATOM   1565 C C   . GLY   A 1 208 ? -12.79053 41.47059 29.61642 1.000 36.96846  ? 215 GLY   A C   1 
ATOM   1566 O O   . GLY   A 1 208 ? -13.29618 41.93255 28.58394 1.000 38.20545  ? 215 GLY   A O   1 
ATOM   1567 N N   . TYR   A 1 209 ? -12.72534 40.16723 29.86793 1.000 32.85018  ? 216 TYR   A N   1 
ATOM   1568 C CA  . TYR   A 1 209 ? -13.25852 39.14263 28.98456 1.000 36.50789  ? 216 TYR   A CA  1 
ATOM   1569 C C   . TYR   A 1 209 ? -13.87087 38.04842 29.84396 1.000 28.91460  ? 216 TYR   A C   1 
ATOM   1570 O O   . TYR   A 1 209 ? -13.45006 37.85543 30.99117 1.000 37.14002  ? 216 TYR   A O   1 
ATOM   1571 C CB  . TYR   A 1 209 ? -12.17192 38.55227 28.07149 1.000 28.97691  ? 216 TYR   A CB  1 
ATOM   1572 C CG  . TYR   A 1 209 ? -11.54147 39.59368 27.19406 1.000 33.17332  ? 216 TYR   A CG  1 
ATOM   1573 C CD1 . TYR   A 1 209 ? -12.14844 39.99152 26.00868 1.000 25.76736  ? 216 TYR   A CD1 1 
ATOM   1574 C CD2 . TYR   A 1 209 ? -10.34727 40.20926 27.56595 1.000 26.70400  ? 216 TYR   A CD2 1 
ATOM   1575 C CE1 . TYR   A 1 209 ? -11.57255 40.97174 25.20679 1.000 38.83650  ? 216 TYR   A CE1 1 
ATOM   1576 C CE2 . TYR   A 1 209 ? -9.76585  41.18688 26.77224 1.000 27.34965  ? 216 TYR   A CE2 1 
ATOM   1577 C CZ  . TYR   A 1 209 ? -10.38492 41.56468 25.59504 1.000 29.99131  ? 216 TYR   A CZ  1 
ATOM   1578 O OH  . TYR   A 1 209 ? -9.81696  42.54054 24.81091 1.000 36.74738  ? 216 TYR   A OH  1 
ATOM   1579 N N   . PRO   A 1 210 ? -14.88162 37.34191 29.33518 1.000 36.89505  ? 217 PRO   A N   1 
ATOM   1580 C CA  . PRO   A 1 210 ? -15.47891 36.25459 30.12596 1.000 36.08966  ? 217 PRO   A CA  1 
ATOM   1581 C C   . PRO   A 1 210 ? -14.47463 35.13029 30.32080 1.000 28.09640  ? 217 PRO   A C   1 
ATOM   1582 O O   . PRO   A 1 210 ? -13.86975 34.64948 29.36066 1.000 32.41163  ? 217 PRO   A O   1 
ATOM   1583 C CB  . PRO   A 1 210 ? -16.68477 35.79962 29.29217 1.000 32.94074  ? 217 PRO   A CB  1 
ATOM   1584 C CG  . PRO   A 1 210 ? -16.66452 36.57518 28.04177 1.000 37.65412  ? 217 PRO   A CG  1 
ATOM   1585 C CD  . PRO   A 1 210 ? -15.56779 37.57804 28.05390 1.000 32.79095  ? 217 PRO   A CD  1 
ATOM   1586 N N   . ILE   A 1 211 ? -14.28006 34.74022 31.58043 1.000 29.67541  ? 218 ILE   A N   1 
ATOM   1587 C CA  . ILE   A 1 211 ? -13.44986 33.60420 31.96578 1.000 28.53879  ? 218 ILE   A CA  1 
ATOM   1588 C C   . ILE   A 1 211 ? -14.38839 32.49155 32.41926 1.000 36.89993  ? 218 ILE   A C   1 
ATOM   1589 O O   . ILE   A 1 211 ? -15.08737 32.63929 33.42702 1.000 32.46718  ? 218 ILE   A O   1 
ATOM   1590 C CB  . ILE   A 1 211 ? -12.47627 33.96127 33.10066 1.000 33.33242  ? 218 ILE   A CB  1 
ATOM   1591 C CG1 . ILE   A 1 211 ? -11.52642 35.08826 32.68794 1.000 28.91415  ? 218 ILE   A CG1 1 
ATOM   1592 C CG2 . ILE   A 1 211 ? -11.71273 32.71391 33.54551 1.000 29.30151  ? 218 ILE   A CG2 1 
ATOM   1593 C CD1 . ILE   A 1 211 ? -10.62156 35.58278 33.82196 1.000 28.57504  ? 218 ILE   A CD1 1 
ATOM   1594 N N   . THR   A 1 212 ? -14.39523 31.37361 31.70231 1.000 31.13129  ? 219 THR   A N   1 
ATOM   1595 C CA  . THR   A 1 212 ? -15.30690 30.27650 32.00290 1.000 31.61799  ? 219 THR   A CA  1 
ATOM   1596 C C   . THR   A 1 212 ? -14.51470 29.10192 32.55419 1.000 35.04508  ? 219 THR   A C   1 
ATOM   1597 O O   . THR   A 1 212 ? -13.62073 28.57623 31.88072 1.000 27.92828  ? 219 THR   A O   1 
ATOM   1598 C CB  . THR   A 1 212 ? -16.09120 29.86079 30.75850 1.000 40.55290  ? 219 THR   A CB  1 
ATOM   1599 O OG1 . THR   A 1 212 ? -16.79140 31.00022 30.24980 1.000 32.35197  ? 219 THR   A OG1 1 
ATOM   1600 C CG2 . THR   A 1 212 ? -17.09190 28.73681 31.08071 1.000 28.74299  ? 219 THR   A CG2 1 
ATOM   1601 N N   . LEU   A 1 213 ? -14.84178 28.69262 33.77320 1.000 30.00108  ? 220 LEU   A N   1 
ATOM   1602 C CA  . LEU   A 1 213 ? -14.19924 27.53875 34.39207 1.000 39.21247  ? 220 LEU   A CA  1 
ATOM   1603 C C   . LEU   A 1 213 ? -15.01836 26.29381 34.06522 1.000 36.43174  ? 220 LEU   A C   1 
ATOM   1604 O O   . LEU   A 1 213 ? -16.12473 26.11830 34.58414 1.000 38.95034  ? 220 LEU   A O   1 
ATOM   1605 C CB  . LEU   A 1 213 ? -14.06854 27.73670 35.89901 1.000 38.54880  ? 220 LEU   A CB  1 
ATOM   1606 C CG  . LEU   A 1 213 ? -13.47994 26.51549 36.61515 1.000 43.74682  ? 220 LEU   A CG  1 
ATOM   1607 C CD1 . LEU   A 1 213 ? -12.16157 26.10331 35.97797 1.000 32.27153  ? 220 LEU   A CD1 1 
ATOM   1608 C CD2 . LEU   A 1 213 ? -13.29653 26.78762 38.10000 1.000 34.97193  ? 220 LEU   A CD2 1 
ATOM   1609 N N   . PHE   A 1 214 ? -14.48331 25.43882 33.19942 1.000 31.13187  ? 221 PHE   A N   1 
ATOM   1610 C CA  . PHE   A 1 214 ? -15.15974 24.19299 32.85416 1.000 34.19272  ? 221 PHE   A CA  1 
ATOM   1611 C C   . PHE   A 1 214 ? -15.15784 23.22643 34.03532 1.000 39.21077  ? 221 PHE   A C   1 
ATOM   1612 O O   . PHE   A 1 214 ? -14.14254 23.05108 34.71429 1.000 45.11883  ? 221 PHE   A O   1 
ATOM   1613 C CB  . PHE   A 1 214 ? -14.48153 23.52330 31.65871 1.000 32.43952  ? 221 PHE   A CB  1 
ATOM   1614 C CG  . PHE   A 1 214 ? -14.81052 24.14764 30.32184 1.000 39.36813  ? 221 PHE   A CG  1 
ATOM   1615 C CD1 . PHE   A 1 214 ? -14.94838 25.51944 30.18204 1.000 31.58245  ? 221 PHE   A CD1 1 
ATOM   1616 C CD2 . PHE   A 1 214 ? -14.95655 23.34874 29.19339 1.000 40.41291  ? 221 PHE   A CD2 1 
ATOM   1617 C CE1 . PHE   A 1 214 ? -15.23598 26.08242 28.95011 1.000 33.61367  ? 221 PHE   A CE1 1 
ATOM   1618 C CE2 . PHE   A 1 214 ? -15.25182 23.90950 27.95162 1.000 33.49327  ? 221 PHE   A CE2 1 
ATOM   1619 C CZ  . PHE   A 1 214 ? -15.39179 25.27681 27.83431 1.000 30.11794  ? 221 PHE   A CZ  1 
ATOM   1620 N N   . VAL   A 1 215 ? -16.30358 22.58941 34.26664 1.000 34.14070  ? 222 VAL   A N   1 
ATOM   1621 C CA  . VAL   A 1 215 ? -16.46508 21.57052 35.29675 1.000 36.39159  ? 222 VAL   A CA  1 
ATOM   1622 C C   . VAL   A 1 215 ? -16.19036 20.20812 34.67660 1.000 46.80916  ? 222 VAL   A C   1 
ATOM   1623 O O   . VAL   A 1 215 ? -16.50631 19.96715 33.50497 1.000 40.26677  ? 222 VAL   A O   1 
ATOM   1624 C CB  . VAL   A 1 215 ? -17.87919 21.63338 35.90958 1.000 42.14606  ? 222 VAL   A CB  1 
ATOM   1625 C CG1 . VAL   A 1 215 ? -18.07127 20.55228 36.96532 1.000 49.23066  ? 222 VAL   A CG1 1 
ATOM   1626 C CG2 . VAL   A 1 215 ? -18.13422 23.00258 36.52122 1.000 49.11623  ? 222 VAL   A CG2 1 
ATOM   1627 N N   . GLU   A 1 216 ? -15.59010 19.31303 35.44916 1.000 40.25806  ? 223 GLU   A N   1 
ATOM   1628 C CA  . GLU   A 1 216 ? -15.29562 17.98154 34.94626 1.000 46.84715  ? 223 GLU   A CA  1 
ATOM   1629 C C   . GLU   A 1 216 ? -16.49175 17.06202 35.11086 1.000 41.98245  ? 223 GLU   A C   1 
ATOM   1630 O O   . GLU   A 1 216 ? -17.29291 17.20595 36.03792 1.000 44.96729  ? 223 GLU   A O   1 
ATOM   1631 C CB  . GLU   A 1 216 ? -14.08950 17.38515 35.65875 1.000 50.75003  ? 223 GLU   A CB  1 
ATOM   1632 C CG  . GLU   A 1 216 ? -12.79383 18.00372 35.21631 1.000 61.80422  ? 223 GLU   A CG  1 
ATOM   1633 C CD  . GLU   A 1 216 ? -11.60429 17.23623 35.71724 1.000 63.54875  ? 223 GLU   A CD  1 
ATOM   1634 O OE1 . GLU   A 1 216 ? -11.33130 16.14961 35.16499 1.000 59.20874  ? 223 GLU   A OE1 1 
ATOM   1635 O OE2 . GLU   A 1 216 ? -10.95163 17.72503 36.66612 1.000 71.02202  ? 223 GLU   A OE2 1 
ATOM   1636 N N   . LYS   A 1 217 ? -16.60316 16.11382 34.18723 1.000 54.03579  ? 224 LYS   A N   1 
ATOM   1637 C CA  . LYS   A 1 217 ? -17.62880 15.08488 34.23734 1.000 50.36959  ? 224 LYS   A CA  1 
ATOM   1638 C C   . LYS   A 1 217 ? -17.10060 13.86920 34.99549 1.000 53.02690  ? 224 LYS   A C   1 
ATOM   1639 O O   . LYS   A 1 217 ? -17.60337 13.52049 36.06278 1.000 59.26965  ? 224 LYS   A O   1 
ATOM   1640 C CB  . LYS   A 1 217 ? -18.06673 14.68336 32.82235 1.000 44.23981  ? 224 LYS   A CB  1 
ATOM   1641 C CG  . LYS   A 1 217 ? -18.11650 15.83656 31.82135 1.000 47.94523  ? 224 LYS   A CG  1 
ATOM   1642 C CD  . LYS   A 1 217 ? -18.58866 15.37029 30.44684 1.000 41.59975  ? 224 LYS   A CD  1 
ATOM   1643 C CE  . LYS   A 1 217 ? -17.44059 14.81410 29.60512 1.000 42.11043  ? 224 LYS   A CE  1 
ATOM   1644 N NZ  . LYS   A 1 217 ? -16.13878 15.50905 29.83090 1.000 43.66446  ? 224 LYS   A NZ  1 
HETATM 1645 C C8  . A1AY5 B 2 .   ? 5.84887   29.76942 24.34408 0.891 35.62232  ? 301 A1AY5 A C8  1 
HETATM 1646 C C5  . A1AY5 B 2 .   ? 11.72249  30.76520 21.50490 0.891 44.09795  ? 301 A1AY5 A C5  1 
HETATM 1647 C C6  . A1AY5 B 2 .   ? 7.62477   30.61967 22.46689 0.891 43.26351  ? 301 A1AY5 A C6  1 
HETATM 1648 N N1  . A1AY5 B 2 .   ? 8.11281   30.60314 23.85079 0.891 46.53814  ? 301 A1AY5 A N1  1 
HETATM 1649 C C2  . A1AY5 B 2 .   ? 10.53932  30.79758 23.35970 0.891 38.33230  ? 301 A1AY5 A C2  1 
HETATM 1650 C C4  . A1AY5 B 2 .   ? 12.55274  31.22021 22.50354 0.891 31.80819  ? 301 A1AY5 A C4  1 
HETATM 1651 C C1  . A1AY5 B 2 .   ? 9.39884   30.63216 24.27275 0.891 46.58355  ? 301 A1AY5 A C1  1 
HETATM 1652 C C3  . A1AY5 B 2 .   ? 11.77726  31.23208 23.68172 0.891 27.20119  ? 301 A1AY5 A C3  1 
HETATM 1653 C C7  . A1AY5 B 2 .   ? 6.38198   31.46964 22.33126 0.891 41.51826  ? 301 A1AY5 A C7  1 
HETATM 1654 C C9  . A1AY5 B 2 .   ? 7.04638   30.53815 24.85443 0.891 38.89971  ? 301 A1AY5 A C9  1 
HETATM 1655 O O1  . A1AY5 B 2 .   ? 9.66114   30.53799 25.47394 0.891 41.06772  ? 301 A1AY5 A O1  1 
HETATM 1656 O O2  . A1AY5 B 2 .   ? 10.49019  30.49225 22.02343 0.891 40.28595  ? 301 A1AY5 A O2  1 
HETATM 1657 S S1  . A1AY5 B 2 .   ? 4.94385   30.70100 23.09668 0.891 43.17607  ? 301 A1AY5 A S1  1 
HETATM 1658 O O   . HOH   C 3 .   ? -11.88640 16.95683 19.20696 1.000 56.48246  ? 401 HOH   A O   1 
HETATM 1659 O O   . HOH   C 3 .   ? -1.23509  16.81782 43.93626 1.000 39.73099  ? 402 HOH   A O   1 
HETATM 1660 O O   . HOH   C 3 .   ? -12.44915 17.92338 14.49346 1.000 61.45769  ? 403 HOH   A O   1 
HETATM 1661 O O   . HOH   C 3 .   ? -2.63514  15.97434 15.91901 1.000 63.68013  ? 404 HOH   A O   1 
HETATM 1662 O O   . HOH   C 3 .   ? 6.14914   15.29765 38.22269 1.000 51.50356  ? 405 HOH   A O   1 
HETATM 1663 O O   . HOH   C 3 .   ? -10.35451 21.21560 47.16317 1.000 52.89675  ? 406 HOH   A O   1 
HETATM 1664 O O   . HOH   C 3 .   ? 5.71230   19.73123 11.30500 1.000 47.55555  ? 407 HOH   A O   1 
HETATM 1665 O O   . HOH   C 3 .   ? -3.78498  36.19604 6.47780  1.000 61.87488  ? 408 HOH   A O   1 
HETATM 1666 O O   . HOH   C 3 .   ? -3.50838  31.21548 48.21137 1.000 51.67789  ? 409 HOH   A O   1 
HETATM 1667 O O   . HOH   C 3 .   ? -1.87980  12.85736 38.63175 1.000 60.91244  ? 410 HOH   A O   1 
HETATM 1668 O O   . HOH   C 3 .   ? 10.06947  32.93839 19.66562 1.000 35.76721  ? 411 HOH   A O   1 
HETATM 1669 O O   . HOH   C 3 .   ? 10.55621  28.33804 42.05756 1.000 43.92251  ? 412 HOH   A O   1 
HETATM 1670 O O   . HOH   C 3 .   ? 10.24574  19.12662 33.15818 1.000 44.02394  ? 413 HOH   A O   1 
HETATM 1671 O O   . HOH   C 3 .   ? 9.15928   17.54488 26.19689 1.000 41.60483  ? 414 HOH   A O   1 
HETATM 1672 O O   . HOH   C 3 .   ? -6.69457  17.18135 42.21378 1.000 50.10213  ? 415 HOH   A O   1 
HETATM 1673 O O   . HOH   C 3 .   ? -6.29411  45.85147 11.50296 1.000 41.49205  ? 416 HOH   A O   1 
HETATM 1674 O O   . HOH   C 3 .   ? 0.48409   39.76126 30.12975 1.000 38.71012  ? 417 HOH   A O   1 
HETATM 1675 O O   . HOH   C 3 .   ? -7.00903  32.06688 12.14303 1.000 35.11715  ? 418 HOH   A O   1 
HETATM 1676 O O   . HOH   C 3 .   ? -16.60723 40.25437 18.48757 1.000 45.87663  ? 419 HOH   A O   1 
HETATM 1677 O O   . HOH   C 3 .   ? 19.47024  29.16917 36.57908 1.000 40.90838  ? 420 HOH   A O   1 
HETATM 1678 O O   . HOH   C 3 .   ? 18.80582  19.02819 29.35069 1.000 52.29484  ? 421 HOH   A O   1 
HETATM 1679 O O   . HOH   C 3 .   ? 17.55934  43.60167 29.97647 1.000 44.78753  ? 422 HOH   A O   1 
HETATM 1680 O O   . HOH   C 3 .   ? -15.35883 19.02908 31.36980 1.000 44.08049  ? 423 HOH   A O   1 
HETATM 1681 O O   . HOH   C 3 .   ? -4.79436  37.72300 35.37559 1.000 32.78644  ? 424 HOH   A O   1 
HETATM 1682 O O   . HOH   C 3 .   ? 1.18357   24.72832 44.83149 1.000 41.63436  ? 425 HOH   A O   1 
HETATM 1683 O O   . HOH   C 3 .   ? -15.32997 32.19862 28.44481 1.000 32.34384  ? 426 HOH   A O   1 
HETATM 1684 O O   . HOH   C 3 .   ? -10.60213 31.22253 49.59924 1.000 45.96325  ? 427 HOH   A O   1 
HETATM 1685 O O   . HOH   C 3 .   ? -13.75301 33.40025 18.47758 1.000 34.49176  ? 428 HOH   A O   1 
HETATM 1686 O O   . HOH   C 3 .   ? 4.14986   11.45074 37.49710 1.000 54.29420  ? 429 HOH   A O   1 
HETATM 1687 O O   . HOH   C 3 .   ? -4.79627  36.42277 14.14915 1.000 28.02468  ? 430 HOH   A O   1 
HETATM 1688 O O   . HOH   C 3 .   ? -3.89516  34.28383 21.38851 1.000 26.75615  ? 431 HOH   A O   1 
HETATM 1689 O O   . HOH   C 3 .   ? 12.24949  20.10471 26.59565 1.000 31.54243  ? 432 HOH   A O   1 
HETATM 1690 O O   . HOH   C 3 .   ? 8.67343   18.72428 22.71852 1.000 47.01011  ? 433 HOH   A O   1 
HETATM 1691 O O   . HOH   C 3 .   ? -5.02478  42.89115 28.88282 1.000 30.00796  ? 434 HOH   A O   1 
HETATM 1692 O O   . HOH   C 3 .   ? 0.88105   43.28609 29.57042 1.000 51.87438  ? 435 HOH   A O   1 
HETATM 1693 O O   . HOH   C 3 .   ? 13.87332  33.07642 19.61470 1.000 51.89499  ? 436 HOH   A O   1 
HETATM 1694 O O   . HOH   C 3 .   ? -8.73942  42.72986 30.60948 1.000 27.77356  ? 437 HOH   A O   1 
HETATM 1695 O O   . HOH   C 3 .   ? -6.91743  20.12922 30.22616 1.000 31.83672  ? 438 HOH   A O   1 
HETATM 1696 O O   . HOH   C 3 .   ? -13.44724 28.74393 45.88125 1.000 39.02895  ? 439 HOH   A O   1 
HETATM 1697 O O   . HOH   C 3 .   ? -19.53332 16.63546 37.42854 1.000 55.83024  ? 440 HOH   A O   1 
HETATM 1698 O O   . HOH   C 3 .   ? -12.22327 43.64216 6.10613  1.000 58.74463  ? 441 HOH   A O   1 
HETATM 1699 O O   . HOH   C 3 .   ? -15.06241 41.75557 26.51868 1.000 37.61161  ? 442 HOH   A O   1 
HETATM 1700 O O   . HOH   C 3 .   ? 5.75804   24.74770 49.60510 1.000 41.91258  ? 443 HOH   A O   1 
HETATM 1701 O O   . HOH   C 3 .   ? 2.38560   37.56429 32.28759 1.000 33.19530  ? 444 HOH   A O   1 
HETATM 1702 O O   . HOH   C 3 .   ? -8.95874  29.78319 10.82160 1.000 46.89302  ? 445 HOH   A O   1 
HETATM 1703 O O   . HOH   C 3 .   ? -4.76635  14.24794 38.26124 1.000 49.71705  ? 446 HOH   A O   1 
HETATM 1704 O O   . HOH   C 3 .   ? -0.35834  30.57195 13.36376 1.000 31.50602  ? 447 HOH   A O   1 
HETATM 1705 O O   . HOH   C 3 .   ? 3.92035   39.56399 37.83111 1.000 40.52858  ? 448 HOH   A O   1 
HETATM 1706 O O   . HOH   C 3 .   ? -0.81192  34.68645 45.86272 1.000 49.92993  ? 449 HOH   A O   1 
HETATM 1707 O O   . HOH   C 3 .   ? 13.36734  16.83988 20.42797 1.000 37.49087  ? 450 HOH   A O   1 
HETATM 1708 O O   . HOH   C 3 .   ? -12.22094 44.32254 27.71646 1.000 42.64321  ? 451 HOH   A O   1 
HETATM 1709 O O   . HOH   C 3 .   ? 7.23267   46.72467 32.95135 1.000 46.58602  ? 452 HOH   A O   1 
HETATM 1710 O O   . HOH   C 3 .   ? 16.94381  25.11035 31.31774 1.000 34.42279  ? 453 HOH   A O   1 
HETATM 1711 O O   . HOH   C 3 .   ? -9.06845  44.38103 28.20886 1.000 41.67879  ? 454 HOH   A O   1 
HETATM 1712 O O   . HOH   C 3 .   ? -12.63979 37.57021 36.18501 1.000 49.51168  ? 455 HOH   A O   1 
HETATM 1713 O O   . HOH   C 3 .   ? -3.98627  30.58945 26.37461 1.000 32.95736  ? 456 HOH   A O   1 
HETATM 1714 O O   . HOH   C 3 .   ? -18.913   26.027   34.725   1.000 35.11624  ? 457 HOH   A O   1 
HETATM 1715 O O   . HOH   C 3 .   ? -6.53312  20.54256 26.21130 1.000 44.86569  ? 458 HOH   A O   1 
HETATM 1716 O O   . HOH   C 3 .   ? 10.96996  37.57784 12.23802 1.000 52.08311  ? 459 HOH   A O   1 
HETATM 1717 O O   . HOH   C 3 .   ? 7.11113   20.50528 43.05645 1.000 61.85245  ? 460 HOH   A O   1 
HETATM 1718 O O   . HOH   C 3 .   ? -17.85524 33.76214 24.52732 1.000 47.53989  ? 461 HOH   A O   1 
HETATM 1719 O O   . HOH   C 3 .   ? -5.93322  31.79255 49.59180 1.000 43.07073  ? 462 HOH   A O   1 
HETATM 1720 O O   . HOH   C 3 .   ? -8.73808  29.38340 20.50293 1.000 36.80489  ? 463 HOH   A O   1 
HETATM 1721 O O   . HOH   C 3 .   ? 12.56028  19.60735 23.40505 1.000 47.59724  ? 464 HOH   A O   1 
HETATM 1722 O O   . HOH   C 3 .   ? 1.34501   40.17475 34.72538 1.000 48.74881  ? 465 HOH   A O   1 
HETATM 1723 O O   . HOH   C 3 .   ? -8.03928  46.41163 22.37766 1.000 38.29850  ? 466 HOH   A O   1 
HETATM 1724 O O   . HOH   C 3 .   ? 2.32590   15.79385 33.84199 1.000 37.97596  ? 467 HOH   A O   1 
HETATM 1725 O O   . HOH   C 3 .   ? -17.01402 29.79254 35.19409 1.000 38.60028  ? 468 HOH   A O   1 
HETATM 1726 O O   . HOH   C 3 .   ? 13.77737  17.14634 15.78465 1.000 35.22852  ? 469 HOH   A O   1 
HETATM 1727 O O   . HOH   C 3 .   ? -4.65036  39.02550 9.37337  1.000 43.92164  ? 470 HOH   A O   1 
HETATM 1728 O O   . HOH   C 3 .   ? 11.96907  24.22347 8.17597  1.000 56.90738  ? 471 HOH   A O   1 
HETATM 1729 O O   . HOH   C 3 .   ? 1.46716   37.33874 17.74436 1.000 35.40778  ? 472 HOH   A O   1 
HETATM 1730 O O   . HOH   C 3 .   ? -13.03094 20.04623 41.31301 1.000 49.37537  ? 473 HOH   A O   1 
HETATM 1731 O O   . HOH   C 3 .   ? 6.52134   24.66684 8.69000  1.000 48.19141  ? 474 HOH   A O   1 
HETATM 1732 O O   . HOH   C 3 .   ? -10.33213 34.36135 46.33990 1.000 37.01750  ? 475 HOH   A O   1 
HETATM 1733 O O   . HOH   C 3 .   ? -12.44915 25.97970 24.49930 1.000 29.75299  ? 476 HOH   A O   1 
HETATM 1734 O O   . HOH   C 3 .   ? 5.51617   32.62248 10.39893 1.000 43.86478  ? 477 HOH   A O   1 
HETATM 1735 O O   . HOH   C 3 .   ? -6.307    46.643   27.936   1.000 50.59200  ? 478 HOH   A O   1 
HETATM 1736 O O   . HOH   C 3 .   ? 14.22174  29.71356 48.02586 1.000 50.55226  ? 479 HOH   A O   1 
HETATM 1737 O O   . HOH   C 3 .   ? 0.08931   37.53245 25.02042 1.000 43.61362  ? 480 HOH   A O   1 
HETATM 1738 O O   . HOH   C 3 .   ? -5.14908  44.30481 7.30057  1.000 54.43652  ? 481 HOH   A O   1 
HETATM 1739 O O   . HOH   C 3 .   ? 4.45549   38.53003 31.05237 1.000 32.93167  ? 482 HOH   A O   1 
HETATM 1740 O O   . HOH   C 3 .   ? -13.81079 38.04952 33.83116 1.000 48.83856  ? 483 HOH   A O   1 
HETATM 1741 O O   . HOH   C 3 .   ? 5.98880   20.58054 19.14641 1.000 29.85653  ? 484 HOH   A O   1 
HETATM 1742 O O   . HOH   C 3 .   ? 14.96796  25.15263 29.29997 1.000 33.35941  ? 485 HOH   A O   1 
HETATM 1743 O O   . HOH   C 3 .   ? 1.93641   43.58482 15.46503 1.000 52.27533  ? 486 HOH   A O   1 
HETATM 1744 O O   . HOH   C 3 .   ? -1.22564  20.09224 44.93431 1.000 41.52007  ? 487 HOH   A O   1 
HETATM 1745 O O   . HOH   C 3 .   ? -3.18052  45.33438 26.38236 1.000 46.41596  ? 488 HOH   A O   1 
HETATM 1746 O O   . HOH   C 3 .   ? -1.00511  34.22619 22.35487 1.000 39.90929  ? 489 HOH   A O   1 
HETATM 1747 O O   . HOH   C 3 .   ? 9.13835   25.23809 40.98118 1.000 42.04188  ? 490 HOH   A O   1 
HETATM 1748 O O   . HOH   C 3 .   ? -11.40581 31.83440 17.40956 1.000 42.71699  ? 491 HOH   A O   1 
HETATM 1749 O O   . HOH   C 3 .   ? -7.81535  40.71078 41.20844 1.000 42.36364  ? 492 HOH   A O   1 
HETATM 1750 O O   . HOH   C 3 .   ? -3.63017  40.72008 40.28106 1.000 55.56076  ? 493 HOH   A O   1 
HETATM 1751 O O   . HOH   C 3 .   ? 0.19956   15.46685 32.65235 1.000 45.01092  ? 494 HOH   A O   1 
HETATM 1752 O O   . HOH   C 3 .   ? 1.53948   28.01075 49.17145 1.000 48.42531  ? 495 HOH   A O   1 
HETATM 1753 O O   . HOH   C 3 .   ? 1.72906   38.48945 10.46774 1.000 52.64328  ? 496 HOH   A O   1 
HETATM 1754 O O   . HOH   C 3 .   ? 5.41821   37.10511 12.56296 1.000 47.53223  ? 497 HOH   A O   1 
HETATM 1755 O O   . HOH   C 3 .   ? -17.00449 38.31639 22.35013 1.000 45.55947  ? 498 HOH   A O   1 
HETATM 1756 O O   . HOH   C 3 .   ? -2.17443  31.99813 28.16154 1.000 32.44630  ? 499 HOH   A O   1 
HETATM 1757 O O   . HOH   C 3 .   ? 21.24940  28.80907 22.30639 1.000 49.42010  ? 500 HOH   A O   1 
HETATM 1758 O O   . HOH   C 3 .   ? -5.28598  21.49046 13.00826 1.000 51.02954  ? 501 HOH   A O   1 
HETATM 1759 O O   . HOH   C 3 .   ? -6.71113  25.96053 12.07195 1.000 55.19890  ? 502 HOH   A O   1 
HETATM 1760 O O   . HOH   C 3 .   ? -2.09685  33.97149 24.86456 1.000 31.75189  ? 503 HOH   A O   1 
HETATM 1761 O O   . HOH   C 3 .   ? 9.09043   39.54259 26.62752 1.000 52.14474  ? 504 HOH   A O   1 
HETATM 1762 O O   . HOH   C 3 .   ? -2.60182  39.98987 41.80739 1.000 43.20455  ? 505 HOH   A O   1 
HETATM 1763 O O   . HOH   C 3 .   ? 5.25708   36.04726 28.91509 1.000 33.62074  ? 506 HOH   A O   1 
HETATM 1764 O O   . HOH   C 3 .   ? 8.88114   22.60670 42.74336 1.000 53.45978  ? 507 HOH   A O   1 
HETATM 1765 O O   . HOH   C 3 .   ? 14.10763  18.47458 30.79326 1.000 53.59001  ? 508 HOH   A O   1 
HETATM 1766 O O   . HOH   C 3 .   ? -16.27259 39.30221 25.11955 1.000 42.59620  ? 509 HOH   A O   1 
HETATM 1767 O O   . HOH   C 3 .   ? -7.80390  41.64371 37.85319 1.000 48.82033  ? 510 HOH   A O   1 
HETATM 1768 O O   . HOH   C 3 .   ? -7.34588  33.43812 8.37683  1.000 56.31542  ? 511 HOH   A O   1 
HETATM 1769 O O   . HOH   C 3 .   ? -13.72851 47.20960 23.65262 1.000 60.67746  ? 512 HOH   A O   1 
HETATM 1770 O O   . HOH   C 3 .   ? -5.03185  40.36702 36.42768 1.000 45.95574  ? 513 HOH   A O   1 
HETATM 1771 O O   . HOH   C 3 .   ? 13.384    44.446   28.948   1.000 42.67960  ? 514 HOH   A O   1 
HETATM 1772 O O   . HOH   C 3 .   ? -13.89244 32.83389 40.51262 1.000 38.82771  ? 515 HOH   A O   1 
HETATM 1773 O O   . HOH   C 3 .   ? 4.01947   18.99198 20.72229 1.000 49.94566  ? 516 HOH   A O   1 
HETATM 1774 O O   . HOH   C 3 .   ? -4.98056  39.07839 12.32485 1.000 32.18622  ? 517 HOH   A O   1 
HETATM 1775 O O   . HOH   C 3 .   ? 22.49339  39.43154 27.15582 1.000 60.23443  ? 518 HOH   A O   1 
HETATM 1776 O O   . HOH   C 3 .   ? 0.13599   29.15612 45.89015 1.000 44.36081  ? 519 HOH   A O   1 
HETATM 1777 O O   . HOH   C 3 .   ? -3.81710  25.27823 9.68511  1.000 48.46813  ? 520 HOH   A O   1 
HETATM 1778 O O   . HOH   C 3 .   ? -5.80635  34.60071 49.97372 1.000 52.53173  ? 521 HOH   A O   1 
HETATM 1779 O O   . HOH   C 3 .   ? -13.22805 28.30489 22.36773 1.000 41.77530  ? 522 HOH   A O   1 
HETATM 1780 O O   . HOH   C 3 .   ? 4.59521   23.37540 46.13775 1.000 44.81531  ? 523 HOH   A O   1 
HETATM 1781 O O   . HOH   C 3 .   ? -13.41476 21.60107 44.00085 1.000 52.03228  ? 524 HOH   A O   1 
HETATM 1782 O O   . HOH   C 3 .   ? 12.31194  26.42163 10.93836 1.000 55.33605  ? 525 HOH   A O   1 
HETATM 1783 O O   . HOH   C 3 .   ? 0.82299   32.69657 27.50017 1.000 39.86844  ? 526 HOH   A O   1 
HETATM 1784 O O   . HOH   C 3 .   ? -9.19209  47.12783 6.03375  1.000 55.28417  ? 527 HOH   A O   1 
HETATM 1785 O O   . HOH   C 3 .   ? 15.87021  27.46947 46.66296 1.000 49.44974  ? 528 HOH   A O   1 
HETATM 1786 O O   . HOH   C 3 .   ? -15.79061 36.11830 33.94191 1.000 55.85606  ? 529 HOH   A O   1 
HETATM 1787 O O   . HOH   C 3 .   ? 11.35285  34.67655 45.04648 1.000 52.31007  ? 530 HOH   A O   1 
HETATM 1788 O O   . HOH   C 3 .   ? 10.94418  41.45820 27.86841 1.000 54.19443  ? 531 HOH   A O   1 
HETATM 1789 O O   . HOH   C 3 .   ? -9.95575  25.09181 20.81115 1.000 52.21722  ? 532 HOH   A O   1 
HETATM 1790 O O   . HOH   C 3 .   ? 1.37422   37.34888 45.04318 1.000 46.50058  ? 533 HOH   A O   1 
HETATM 1791 O O   . HOH   C 3 .   ? -18.88821 32.57619 32.04385 1.000 60.99982  ? 534 HOH   A O   1 
HETATM 1792 O O   . HOH   C 3 .   ? 15.69589  23.02921 33.07733 1.000 42.69659  ? 535 HOH   A O   1 
HETATM 1793 O O   . HOH   C 3 .   ? 19.427    21.129   25.347   1.000 42.64917  ? 536 HOH   A O   1 
HETATM 1794 O O   . HOH   C 3 .   ? -2.79898  18.12600 19.60306 1.000 61.80241  ? 537 HOH   A O   1 
HETATM 1795 O O   . HOH   C 3 .   ? -17.43945 34.96904 32.92676 1.000 58.77645  ? 538 HOH   A O   1 
HETATM 1796 O O   . HOH   C 3 .   ? -13.470   14.134   28.312   1.000 54.98123  ? 539 HOH   A O   1 
HETATM 1797 O O   . HOH   C 3 .   ? -15.07135 20.04405 38.70189 1.000 50.54368  ? 540 HOH   A O   1 
HETATM 1798 O O   . HOH   C 3 .   ? -14.745   21.171   18.445   1.000 49.57140  ? 541 HOH   A O   1 
HETATM 1799 O O   . HOH   C 3 .   ? -8.71673  18.75633 28.39742 1.000 42.29472  ? 542 HOH   A O   1 
HETATM 1800 O O   . HOH   C 3 .   ? -20.13825 32.32673 23.40007 1.000 58.32050  ? 543 HOH   A O   1 
HETATM 1801 O O   . HOH   C 3 .   ? -7.680    48.045   26.604   1.000 49.00767  ? 544 HOH   A O   1 
HETATM 1802 O O   . HOH   C 3 .   ? -12.75905 18.60737 30.87772 1.000 38.25754  ? 545 HOH   A O   1 
HETATM 1803 O O   . HOH   C 3 .   ? 14.21545  44.78719 44.51715 1.000 51.19288  ? 546 HOH   A O   1 
HETATM 1804 O O   . HOH   C 3 .   ? -13.389   52.211   13.089   1.000 60.62196  ? 547 HOH   A O   1 
HETATM 1805 O O   . HOH   C 3 .   ? -0.00223  36.35304 21.07758 1.000 49.33973  ? 548 HOH   A O   1 
HETATM 1806 O O   . HOH   C 3 .   ? -13.16440 20.21804 37.82233 1.000 45.56336  ? 549 HOH   A O   1 
HETATM 1807 O O   . HOH   C 3 .   ? -19.460   26.205   37.329   1.000 47.38451  ? 550 HOH   A O   1 
HETATM 1808 O O   . HOH   C 3 .   ? 6.755     47.714   35.340   1.000 45.51132  ? 551 HOH   A O   1 
HETATM 1809 O O   . HOH   C 3 .   ? -14.94594 43.23032 24.01095 1.000 54.29737  ? 552 HOH   A O   1 
HETATM 1810 O O   . HOH   C 3 .   ? -11.37216 18.40285 28.82753 1.000 36.91951  ? 553 HOH   A O   1 
HETATM 1811 O O   . HOH   C 3 .   ? -5.83144  14.80122 40.92985 1.000 46.18900  ? 554 HOH   A O   1 
HETATM 1812 O O   . HOH   C 3 .   ? 8.08935   15.36964 21.34278 1.000 57.92464  ? 555 HOH   A O   1 
HETATM 1813 O O   . HOH   C 3 .   ? -15.57114 44.73580 29.91363 1.000 53.94230  ? 556 HOH   A O   1 
HETATM 1814 O O   . HOH   C 3 .   ? 24.174    28.561   34.737   1.000 58.08812  ? 557 HOH   A O   1 
HETATM 1815 O O   . HOH   C 3 .   ? 2.49157   33.04463 25.78940 1.000 45.92824  ? 558 HOH   A O   1 
HETATM 1816 O O   . HOH   C 3 .   ? 11.87489  44.40541 44.88062 1.000 58.25194  ? 559 HOH   A O   1 
HETATM 1817 O O   . HOH   C 3 .   ? -17.78155 33.03951 26.86336 1.000 46.25840  ? 560 HOH   A O   1 
HETATM 1818 O O   . HOH   C 3 .   ? -0.25328  38.50291 22.36177 1.000 53.88488  ? 561 HOH   A O   1 
HETATM 1819 O O   . HOH   C 3 .   ? 7.95776   31.60658 9.21851  1.000 44.58469  ? 562 HOH   A O   1 
HETATM 1820 O O   . HOH   C 3 .   ? -11.09116 27.92280 20.75857 1.000 48.80139  ? 563 HOH   A O   1 
HETATM 1821 O O   . HOH   C 3 .   ? 12.472    44.220   31.155   1.000 40.41417  ? 564 HOH   A O   1 
HETATM 1822 O O   . HOH   C 3 .   ? -2.87909  18.94741 46.89162 1.000 56.43532  ? 565 HOH   A O   1 
HETATM 1823 O O   . HOH   C 3 .   ? 15.229    43.249   21.284   1.000 58.80218  ? 566 HOH   A O   1 
HETATM 1824 O O   . HOH   C 3 .   ? 0.71866   41.48080 22.05334 1.000 54.47450  ? 567 HOH   A O   1 
HETATM 1825 O O   . HOH   C 3 .   ? 14.18975  34.53190 44.28862 1.000 52.18119  ? 568 HOH   A O   1 
HETATM 1826 O O   . HOH   C 3 .   ? 19.28009  43.26728 27.83361 1.000 55.65992  ? 569 HOH   A O   1 
HETATM 1827 O O   . HOH   C 3 .   ? -6.07063  48.14319 23.29073 1.000 49.68905  ? 570 HOH   A O   1 
HETATM 1828 O O   . HOH   C 3 .   ? -1.03373  15.45121 21.67632 1.000 59.91939  ? 571 HOH   A O   1 
HETATM 1829 O O   . HOH   C 3 .   ? -9.23538  21.18705 25.54131 1.000 57.81238  ? 572 HOH   A O   1 
HETATM 1830 O O   . HOH   C 3 .   ? -5.20748  46.28980 5.30035  1.000 55.98579  ? 573 HOH   A O   1 
HETATM 1831 O O   . HOH   C 3 .   ? 7.08848   23.48587 47.15630 1.000 56.02311  ? 574 HOH   A O   1 
HETATM 1832 O O   . HOH   C 3 .   ? -12.30929 32.65281 47.48356 1.000 49.02138  ? 575 HOH   A O   1 
HETATM 1833 O O   . HOH   C 3 .   ? -14.22043 35.94908 36.87692 1.000 51.26056  ? 576 HOH   A O   1 
HETATM 1834 O O   . HOH   C 3 .   ? 10.79030  15.18271 20.06287 1.000 55.38918  ? 577 HOH   A O   1 
HETATM 1835 O O   . HOH   C 3 .   ? -14.12098 31.22927 38.04483 1.000 52.09092  ? 578 HOH   A O   1 
HETATM 1836 O O   . HOH   C 3 .   ? -17.806   28.890   21.160   1.000 70.45394  ? 579 HOH   A O   1 
HETATM 1837 O O   . HOH   C 3 .   ? -2.15984  18.25579 22.37167 1.000 60.00205  ? 580 HOH   A O   1 
HETATM 1838 O O   . HOH   C 3 .   ? 10.19713  37.05974 9.94599  1.000 54.08410  ? 581 HOH   A O   1 
HETATM 1839 O O   . HOH   C 3 .   ? 22.683    25.006   23.008   1.000 55.47157  ? 582 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   ? 1.06052 0.99678 0.94570 0.00677  -0.06335 -0.26164 16  GLU A N   
2    C CA  . GLU A 9   ? 0.89557 0.81801 0.76438 0.03264  -0.06111 -0.23323 16  GLU A CA  
3    C C   . GLU A 9   ? 0.77017 0.69808 0.65397 0.03787  -0.06109 -0.20547 16  GLU A C   
4    O O   . GLU A 9   ? 0.75036 0.71562 0.64229 0.04257  -0.07234 -0.20109 16  GLU A O   
5    C CB  . GLU A 9   ? 1.00468 0.95818 0.85251 0.05321  -0.07319 -0.23617 16  GLU A CB  
6    C CG  . GLU A 9   ? 1.18971 1.19889 1.04433 0.05333  -0.09081 -0.24942 16  GLU A CG  
7    C CD  . GLU A 9   ? 1.31323 1.34375 1.16633 0.03825  -0.09815 -0.28726 16  GLU A CD  
8    O OE1 . GLU A 9   ? 1.31203 1.34456 1.18807 0.01159  -0.09567 -0.30622 16  GLU A OE1 
9    O OE2 . GLU A 9   ? 1.14281 1.18858 0.97143 0.05209  -0.10549 -0.29897 16  GLU A OE2 
10   N N   . VAL A 10  ? 0.65012 0.54067 0.53559 0.03873  -0.04812 -0.18727 17  VAL A N   
11   C CA  . VAL A 10  ? 0.73253 0.62407 0.63112 0.04141  -0.04669 -0.16332 17  VAL A CA  
12   C C   . VAL A 10  ? 0.54326 0.42792 0.43074 0.06200  -0.04423 -0.14054 17  VAL A C   
13   O O   . VAL A 10  ? 0.67102 0.52977 0.54672 0.06983  -0.03527 -0.13748 17  VAL A O   
14   C CB  . VAL A 10  ? 0.68909 0.54792 0.59816 0.02639  -0.03377 -0.16063 17  VAL A CB  
15   C CG1 . VAL A 10  ? 0.57462 0.44037 0.49625 0.02837  -0.03412 -0.13900 17  VAL A CG1 
16   C CG2 . VAL A 10  ? 0.59394 0.45446 0.51362 0.00225  -0.03182 -0.18683 17  VAL A CG2 
17   N N   . GLU A 11  ? 0.51974 0.42735 0.41141 0.07036  -0.05069 -0.12547 18  GLU A N   
18   C CA  . GLU A 11  ? 0.50965 0.41386 0.39540 0.08518  -0.04692 -0.10491 18  GLU A CA  
19   C C   . GLU A 11  ? 0.48220 0.37897 0.38194 0.08118  -0.04288 -0.08849 18  GLU A C   
20   O O   . GLU A 11  ? 0.46855 0.37512 0.38010 0.07235  -0.04673 -0.08778 18  GLU A O   
21   C CB  . GLU A 11  ? 0.53325 0.46188 0.41001 0.09719  -0.05353 -0.09924 18  GLU A CB  
22   C CG  . GLU A 11  ? 0.69937 0.63764 0.55645 0.10646  -0.05749 -0.11267 18  GLU A CG  
23   C CD  . GLU A 11  ? 0.79555 0.75347 0.63868 0.12195  -0.06152 -0.10345 18  GLU A CD  
24   O OE1 . GLU A 11  ? 0.68513 0.66302 0.53274 0.12229  -0.06931 -0.10348 18  GLU A OE1 
25   O OE2 . GLU A 11  ? 0.81243 0.76451 0.63878 0.13501  -0.05522 -0.09555 18  GLU A OE2 
26   N N   . THR A 12  ? 0.53588 0.41887 0.43401 0.08884  -0.03535 -0.07610 19  THR A N   
27   C CA  . THR A 12  ? 0.47780 0.35820 0.38680 0.08745  -0.03261 -0.06137 19  THR A CA  
28   C C   . THR A 12  ? 0.47133 0.36872 0.38248 0.09515  -0.03320 -0.04807 19  THR A C   
29   O O   . THR A 12  ? 0.51167 0.41188 0.41587 0.10482  -0.02946 -0.04575 19  THR A O   
30   C CB  . THR A 12  ? 0.48543 0.34095 0.39179 0.09136  -0.02341 -0.05773 19  THR A CB  
31   O OG1 . THR A 12  ? 0.50970 0.34247 0.41241 0.08145  -0.01928 -0.07133 19  THR A OG1 
32   C CG2 . THR A 12  ? 0.47246 0.33015 0.38751 0.09209  -0.02222 -0.04301 19  THR A CG2 
33   N N   . PHE A 13  ? 0.42990 0.33743 0.35049 0.08967  -0.03622 -0.04042 20  PHE A N   
34   C CA  . PHE A 13  ? 0.50169 0.42269 0.42560 0.09211  -0.03520 -0.03024 20  PHE A CA  
35   C C   . PHE A 13  ? 0.54198 0.46711 0.47692 0.08843  -0.03463 -0.02193 20  PHE A C   
36   O O   . PHE A 13  ? 0.43172 0.34996 0.36986 0.08352  -0.03635 -0.02236 20  PHE A O   
37   C CB  . PHE A 13  ? 0.40989 0.33861 0.33063 0.08976  -0.03884 -0.03058 20  PHE A CB  
38   C CG  . PHE A 13  ? 0.45221 0.38306 0.36008 0.09585  -0.04178 -0.03896 20  PHE A CG  
39   C CD1 . PHE A 13  ? 0.56302 0.49633 0.47155 0.09165  -0.04811 -0.05123 20  PHE A CD1 
40   C CD2 . PHE A 13  ? 0.54247 0.47545 0.43718 0.10560  -0.03771 -0.03535 20  PHE A CD2 
41   C CE1 . PHE A 13  ? 0.53138 0.47415 0.42812 0.09792  -0.05292 -0.06141 20  PHE A CE1 
42   C CE2 . PHE A 13  ? 0.50718 0.44494 0.38620 0.11414  -0.04140 -0.04293 20  PHE A CE2 
43   C CZ  . PHE A 13  ? 0.49141 0.43649 0.37170 0.11071  -0.05030 -0.05678 20  PHE A CZ  
44   N N   . ALA A 14  ? 0.47411 0.41269 0.41463 0.09026  -0.03166 -0.01517 21  ALA A N   
45   C CA  . ALA A 14  ? 0.60355 0.55407 0.55451 0.08618  -0.03298 -0.00964 21  ALA A CA  
46   C C   . ALA A 14  ? 0.51047 0.46487 0.46362 0.07612  -0.03458 -0.00955 21  ALA A C   
47   O O   . ALA A 14  ? 0.55253 0.50484 0.50091 0.07475  -0.03124 -0.00995 21  ALA A O   
48   C CB  . ALA A 14  ? 0.52562 0.49568 0.48510 0.09166  -0.02917 -0.00542 21  ALA A CB  
49   N N   . PHE A 15  ? 0.45545 0.41234 0.41262 0.07074  -0.03823 -0.00848 22  PHE A N   
50   C CA  . PHE A 15  ? 0.44005 0.39971 0.39861 0.06160  -0.03843 -0.00912 22  PHE A CA  
51   C C   . PHE A 15  ? 0.38100 0.35606 0.34723 0.05632  -0.03420 -0.00875 22  PHE A C   
52   O O   . PHE A 15  ? 0.42003 0.41315 0.39489 0.05954  -0.03416 -0.00757 22  PHE A O   
53   C CB  . PHE A 15  ? 0.50101 0.46166 0.46066 0.05791  -0.04268 -0.00870 22  PHE A CB  
54   C CG  . PHE A 15  ? 0.58890 0.53587 0.54363 0.05747  -0.04419 -0.01059 22  PHE A CG  
55   C CD1 . PHE A 15  ? 0.40840 0.35010 0.35968 0.05521  -0.04382 -0.01360 22  PHE A CD1 
56   C CD2 . PHE A 15  ? 0.43355 0.37360 0.38711 0.05980  -0.04450 -0.00921 22  PHE A CD2 
57   C CE1 . PHE A 15  ? 0.46263 0.40031 0.41352 0.05451  -0.04549 -0.01687 22  PHE A CE1 
58   C CE2 . PHE A 15  ? 0.39090 0.32162 0.34349 0.05599  -0.04401 -0.01261 22  PHE A CE2 
59   C CZ  . PHE A 15  ? 0.50934 0.44288 0.46270 0.05292  -0.04539 -0.01730 22  PHE A CZ  
60   N N   . GLN A 16  ? 0.48739 0.45562 0.45074 0.04816  -0.02932 -0.01029 23  GLN A N   
61   C CA  . GLN A 16  ? 0.44726 0.42888 0.41980 0.03712  -0.02382 -0.01294 23  GLN A CA  
62   C C   . GLN A 16  ? 0.55435 0.55806 0.53666 0.03229  -0.03111 -0.01644 23  GLN A C   
63   O O   . GLN A 16  ? 0.45153 0.44980 0.42830 0.03421  -0.03737 -0.01620 23  GLN A O   
64   C CB  . GLN A 16  ? 0.55968 0.52051 0.52320 0.02868  -0.01511 -0.01430 23  GLN A CB  
65   C CG  . GLN A 16  ? 0.73780 0.67866 0.68765 0.03714  -0.00738 -0.00914 23  GLN A CG  
66   C CD  . GLN A 16  ? 0.83084 0.75454 0.76637 0.04713  -0.01181 -0.00727 23  GLN A CD  
67   O OE1 . GLN A 16  ? 0.60059 0.53072 0.53856 0.05241  -0.02184 -0.00871 23  GLN A OE1 
68   N NE2 . GLN A 16  ? 0.78565 0.68782 0.70597 0.05030  -0.00297 -0.00405 23  GLN A NE2 
69   N N   . ALA A 17  ? 0.56329 0.59551 0.56014 0.02668  -0.02998 -0.02001 24  ALA A N   
70   C CA  . ALA A 17  ? 0.54542 0.60764 0.55090 0.02657  -0.03889 -0.02337 24  ALA A CA  
71   C C   . ALA A 17  ? 0.46615 0.52119 0.46447 0.01743  -0.04254 -0.02871 24  ALA A C   
72   O O   . ALA A 17  ? 0.52138 0.58537 0.51518 0.02429  -0.05099 -0.02719 24  ALA A O   
73   C CB  . ALA A 17  ? 0.45560 0.55694 0.48102 0.01890  -0.03679 -0.02980 24  ALA A CB  
74   N N   . GLU A 18  ? 0.50193 0.53760 0.49618 0.00352  -0.03454 -0.03428 25  GLU A N   
75   C CA  . GLU A 18  ? 0.54670 0.57290 0.53250 -0.00498 -0.03614 -0.04072 25  GLU A CA  
76   C C   . GLU A 18  ? 0.51469 0.52064 0.48647 0.00675  -0.04083 -0.03384 25  GLU A C   
77   O O   . GLU A 18  ? 0.54214 0.55243 0.50809 0.00621  -0.04611 -0.03659 25  GLU A O   
78   C CB  . GLU A 18  ? 0.65285 0.65340 0.63350 -0.01977 -0.02316 -0.04684 25  GLU A CB  
79   C CG  . GLU A 18  ? 0.84266 0.86085 0.83817 -0.03795 -0.01494 -0.05683 25  GLU A CG  
80   C CD  . GLU A 18  ? 0.94000 0.95351 0.94083 -0.03546 -0.00474 -0.05002 25  GLU A CD  
81   O OE1 . GLU A 18  ? 0.68295 0.68699 0.67704 -0.01790 -0.00756 -0.03865 25  GLU A OE1 
82   O OE2 . GLU A 18  ? 0.99184 1.01121 1.00320 -0.05220 0.00720  -0.05714 25  GLU A OE2 
83   N N   . ILE A 19  ? 0.51680 0.50331 0.48334 0.01667  -0.03854 -0.02611 26  ILE A N   
84   C CA  . ILE A 19  ? 0.47367 0.44511 0.43103 0.02487  -0.04162 -0.02178 26  ILE A CA  
85   C C   . ILE A 19  ? 0.48677 0.47008 0.44530 0.03351  -0.04838 -0.01706 26  ILE A C   
86   O O   . ILE A 19  ? 0.46001 0.43889 0.41190 0.03545  -0.05046 -0.01564 26  ILE A O   
87   C CB  . ILE A 19  ? 0.42882 0.38167 0.38135 0.03161  -0.03772 -0.01801 26  ILE A CB  
88   C CG1 . ILE A 19  ? 0.43789 0.37251 0.38246 0.02743  -0.02917 -0.01996 26  ILE A CG1 
89   C CG2 . ILE A 19  ? 0.36792 0.31451 0.31696 0.03830  -0.04145 -0.01578 26  ILE A CG2 
90   C CD1 . ILE A 19  ? 0.62151 0.54199 0.55788 0.03781  -0.02599 -0.01566 26  ILE A CD1 
91   N N   . ALA A 20  ? 0.36697 0.36278 0.33192 0.04022  -0.04984 -0.01365 27  ALA A N   
92   C CA  . ALA A 20  ? 0.45439 0.45692 0.41665 0.05126  -0.05382 -0.00761 27  ALA A CA  
93   C C   . ALA A 20  ? 0.39986 0.42201 0.35921 0.05075  -0.05914 -0.00905 27  ALA A C   
94   O O   . ALA A 20  ? 0.43988 0.45729 0.38897 0.05886  -0.06052 -0.00319 27  ALA A O   
95   C CB  . ALA A 20  ? 0.51462 0.52832 0.48324 0.06092  -0.05333 -0.00406 27  ALA A CB  
96   N N   . GLN A 21  ? 0.41679 0.46041 0.38369 0.04048  -0.06107 -0.01767 28  GLN A N   
97   C CA  . GLN A 21  ? 0.41684 0.48450 0.38052 0.03874  -0.06762 -0.02264 28  GLN A CA  
98   C C   . GLN A 21  ? 0.48360 0.53158 0.43281 0.03505  -0.06663 -0.02385 28  GLN A C   
99   O O   . GLN A 21  ? 0.50560 0.56293 0.44368 0.04201  -0.07110 -0.02153 28  GLN A O   
100  C CB  . GLN A 21  ? 0.46073 0.55554 0.43829 0.02372  -0.06836 -0.03570 28  GLN A CB  
101  C CG  . GLN A 21  ? 0.75844 0.88840 0.73558 0.02041  -0.07699 -0.04510 28  GLN A CG  
102  C CD  . GLN A 21  ? 0.95158 1.11566 0.94844 0.00393  -0.07707 -0.05988 28  GLN A CD  
103  O OE1 . GLN A 21  ? 0.66906 0.81990 0.67641 -0.00808 -0.06742 -0.06283 28  GLN A OE1 
104  N NE2 . GLN A 21  ? 0.78220 0.99227 0.78394 0.00316  -0.08723 -0.06974 28  GLN A NE2 
105  N N   . LEU A 22  ? 0.41193 0.43367 0.35942 0.02641  -0.06009 -0.02675 29  LEU A N   
106  C CA  . LEU A 22  ? 0.45578 0.46063 0.39081 0.02466  -0.05789 -0.02786 29  LEU A CA  
107  C C   . LEU A 22  ? 0.47827 0.47054 0.40623 0.03575  -0.05666 -0.01724 29  LEU A C   
108  O O   . LEU A 22  ? 0.42265 0.41322 0.33914 0.03845  -0.05640 -0.01550 29  LEU A O   
109  C CB  . LEU A 22  ? 0.44843 0.42988 0.38276 0.01673  -0.05040 -0.03250 29  LEU A CB  
110  C CG  . LEU A 22  ? 0.44348 0.40740 0.36669 0.01825  -0.04661 -0.03251 29  LEU A CG  
111  C CD1 . LEU A 22  ? 0.41146 0.38393 0.32410 0.01368  -0.04870 -0.03992 29  LEU A CD1 
112  C CD2 . LEU A 22  ? 0.64218 0.58395 0.56370 0.01612  -0.03887 -0.03481 29  LEU A CD2 
113  N N   . MET A 23  ? 0.49797 0.47993 0.43180 0.04099  -0.05432 -0.01112 30  MET A N   
114  C CA  . MET A 23  ? 0.56067 0.52794 0.48942 0.04772  -0.05061 -0.00332 30  MET A CA  
115  C C   . MET A 23  ? 0.50651 0.48054 0.42442 0.05795  -0.05190 0.00450  30  MET A C   
116  O O   . MET A 23  ? 0.54508 0.50747 0.45212 0.06100  -0.04699 0.01002  30  MET A O   
117  C CB  . MET A 23  ? 0.45102 0.40755 0.38747 0.05004  -0.04818 -0.00148 30  MET A CB  
118  C CG  . MET A 23  ? 0.45140 0.40058 0.39388 0.04422  -0.04650 -0.00726 30  MET A CG  
119  S SD  . MET A 23  ? 0.51388 0.45599 0.46250 0.04761  -0.04553 -0.00786 30  MET A SD  
120  C CE  . MET A 23  ? 0.52086 0.45075 0.47012 0.04529  -0.04113 -0.00882 30  MET A CE  
121  N N   . SER A 24  ? 0.42069 0.41530 0.34054 0.06473  -0.05757 0.00558  31  SER A N   
122  C CA  . SER A 24  ? 0.51893 0.52363 0.42543 0.07939  -0.05956 0.01423  31  SER A CA  
123  C C   . SER A 24  ? 0.54020 0.55797 0.43417 0.07792  -0.06323 0.01091  31  SER A C   
124  O O   . SER A 24  ? 0.54769 0.55913 0.42341 0.08906  -0.06028 0.02019  31  SER A O   
125  C CB  . SER A 24  ? 0.43963 0.47116 0.35349 0.08932  -0.06568 0.01518  31  SER A CB  
126  O OG  . SER A 24  ? 0.68696 0.74371 0.58887 0.10319  -0.07176 0.01942  31  SER A OG  
127  N N   . LEU A 25  ? 0.48727 0.51926 0.38808 0.06423  -0.06774 -0.00240 32  LEU A N   
128  C CA  . LEU A 25  ? 0.47877 0.51934 0.36595 0.06106  -0.07021 -0.00847 32  LEU A CA  
129  C C   . LEU A 25  ? 0.50808 0.52036 0.38301 0.06137  -0.06102 -0.00265 32  LEU A C   
130  O O   . LEU A 25  ? 0.55906 0.57322 0.41519 0.06874  -0.06005 0.00150  32  LEU A O   
131  C CB  . LEU A 25  ? 0.50954 0.56096 0.40598 0.04361  -0.07312 -0.02561 32  LEU A CB  
132  C CG  . LEU A 25  ? 0.78684 0.85203 0.67049 0.03725  -0.07698 -0.03782 32  LEU A CG  
133  C CD1 . LEU A 25  ? 0.70247 0.78277 0.59901 0.01908  -0.07947 -0.05600 32  LEU A CD1 
134  C CD2 . LEU A 25  ? 0.63162 0.66795 0.50203 0.03483  -0.06857 -0.03734 32  LEU A CD2 
135  N N   . ILE A 26  ? 0.47591 0.46533 0.36117 0.05416  -0.05395 -0.00263 33  ILE A N   
136  C CA  . ILE A 26  ? 0.47620 0.44595 0.35507 0.05292  -0.04478 0.00086  33  ILE A CA  
137  C C   . ILE A 26  ? 0.59054 0.54750 0.45891 0.06306  -0.03754 0.01467  33  ILE A C   
138  O O   . ILE A 26  ? 0.46818 0.41641 0.32330 0.06517  -0.02989 0.01944  33  ILE A O   
139  C CB  . ILE A 26  ? 0.47097 0.42772 0.36535 0.04453  -0.04058 -0.00380 33  ILE A CB  
140  C CG1 . ILE A 26  ? 0.42852 0.38796 0.32451 0.03676  -0.04257 -0.01524 33  ILE A CG1 
141  C CG2 . ILE A 26  ? 0.46710 0.41017 0.36177 0.04388  -0.03076 0.00041  33  ILE A CG2 
142  C CD1 . ILE A 26  ? 0.60062 0.54970 0.50890 0.03344  -0.03965 -0.01809 33  ILE A CD1 
143  N N   . ILE A 27  ? 0.56520 0.51794 0.43719 0.07000  -0.03768 0.02163  34  ILE A N   
144  C CA  . ILE A 27  ? 0.55929 0.49051 0.41896 0.07926  -0.02709 0.03504  34  ILE A CA  
145  C C   . ILE A 27  ? 0.57800 0.51690 0.41268 0.09569  -0.02792 0.04511  34  ILE A C   
146  O O   . ILE A 27  ? 0.75018 0.66865 0.56673 0.10233  -0.01593 0.05646  34  ILE A O   
147  C CB  . ILE A 27  ? 0.77123 0.69029 0.64021 0.08237  -0.02521 0.03818  34  ILE A CB  
148  C CG1 . ILE A 27  ? 0.50303 0.41105 0.39109 0.06757  -0.02160 0.02948  34  ILE A CG1 
149  C CG2 . ILE A 27  ? 0.71126 0.60466 0.56202 0.09561  -0.01339 0.05302  34  ILE A CG2 
150  C CD1 . ILE A 27  ? 0.58227 0.48673 0.48068 0.06892  -0.02393 0.02734  34  ILE A CD1 
151  N N   . ASN A 28  ? 0.62301 0.59320 0.45561 0.10247  -0.04125 0.04073  35  ASN A N   
152  C CA  . ASN A 28  ? 0.72341 0.70912 0.53250 0.12267  -0.04494 0.05021  35  ASN A CA  
153  C C   . ASN A 28  ? 0.75191 0.76111 0.54644 0.12224  -0.05194 0.04290  35  ASN A C   
154  O O   . ASN A 28  ? 0.68344 0.70984 0.45504 0.14075  -0.05613 0.05011  35  ASN A O   
155  C CB  . ASN A 28  ? 0.63398 0.64705 0.45118 0.13419  -0.05574 0.05011  35  ASN A CB  
156  C CG  . ASN A 28  ? 0.59351 0.58059 0.41797 0.13961  -0.04740 0.05890  35  ASN A CG  
157  O OD1 . ASN A 28  ? 0.69467 0.68801 0.54125 0.13081  -0.05130 0.05086  35  ASN A OD1 
158  N ND2 . ASN A 28  ? 0.63974 0.59384 0.44339 0.15375  -0.03390 0.07520  35  ASN A ND2 
159  N N   . THR A 29  ? 0.64961 0.66001 0.45408 0.10379  -0.05308 0.02864  36  THR A N   
160  C CA  . THR A 29  ? 0.65206 0.68023 0.44033 0.10249  -0.05809 0.01963  36  THR A CA  
161  C C   . THR A 29  ? 0.64714 0.65050 0.41414 0.10680  -0.04430 0.02942  36  THR A C   
162  O O   . THR A 29  ? 0.62434 0.59965 0.40069 0.09863  -0.03152 0.03365  36  THR A O   
163  C CB  . THR A 29  ? 0.74693 0.78384 0.55214 0.08199  -0.06349 -0.00081 36  THR A CB  
164  O OG1 . THR A 29  ? 0.73127 0.79814 0.55161 0.07786  -0.07574 -0.01123 36  THR A OG1 
165  C CG2 . THR A 29  ? 0.71549 0.75879 0.50175 0.07858  -0.06410 -0.01118 36  THR A CG2 
166  N N   . PHE A 30  ? 0.58283 0.60004 0.32107 0.12035  -0.04665 0.03281  37  PHE A N   
167  C CA  . PHE A 30  ? 0.70940 0.70637 0.42435 0.12452  -0.03277 0.04105  37  PHE A CA  
168  C C   . PHE A 30  ? 0.70748 0.70301 0.43018 0.10711  -0.03118 0.02456  37  PHE A C   
169  O O   . PHE A 30  ? 0.66625 0.68473 0.38461 0.10231  -0.04251 0.00797  37  PHE A O   
170  C CB  . PHE A 30  ? 0.64628 0.66117 0.32416 0.14670  -0.03677 0.04902  37  PHE A CB  
171  C CG  . PHE A 30  ? 0.68848 0.67966 0.33758 0.15449  -0.01954 0.06160  37  PHE A CG  
172  C CD1 . PHE A 30  ? 0.80898 0.76519 0.44661 0.16441  -0.00049 0.08396  37  PHE A CD1 
173  C CD2 . PHE A 30  ? 0.69063 0.69180 0.32316 0.15108  -0.02007 0.05059  37  PHE A CD2 
174  C CE1 . PHE A 30  ? 0.84554 0.77866 0.45665 0.17026  0.01863  0.09635  37  PHE A CE1 
175  C CE2 . PHE A 30  ? 0.86030 0.84038 0.46564 0.15884  -0.00223 0.06290  37  PHE A CE2 
176  C CZ  . PHE A 30  ? 0.76916 0.71593 0.36441 0.16812  0.01758  0.08640  37  PHE A CZ  
177  N N   . TYR A 31  ? 0.67849 0.64809 0.41309 0.09768  -0.01658 0.02788  38  TYR A N   
178  C CA  . TYR A 31  ? 0.57546 0.54219 0.31807 0.08481  -0.01322 0.01407  38  TYR A CA  
179  C C   . TYR A 31  ? 0.58207 0.52724 0.32664 0.08293  0.00596  0.02376  38  TYR A C   
180  O O   . TYR A 31  ? 0.60329 0.53602 0.36995 0.07642  0.01266  0.02880  38  TYR A O   
181  C CB  . TYR A 31  ? 0.54847 0.51773 0.32009 0.07091  -0.02095 0.00084  38  TYR A CB  
182  C CG  . TYR A 31  ? 0.64230 0.60532 0.41842 0.06168  -0.01656 -0.01228 38  TYR A CG  
183  C CD1 . TYR A 31  ? 0.61471 0.58580 0.37343 0.06003  -0.02102 -0.02637 38  TYR A CD1 
184  C CD2 . TYR A 31  ? 0.59407 0.54407 0.39037 0.05600  -0.00758 -0.01141 38  TYR A CD2 
185  C CE1 . TYR A 31  ? 0.71439 0.67413 0.47366 0.05400  -0.01473 -0.03783 38  TYR A CE1 
186  C CE2 . TYR A 31  ? 0.59334 0.53777 0.39136 0.05231  -0.00264 -0.02179 38  TYR A CE2 
187  C CZ  . TYR A 31  ? 0.56623 0.51222 0.34468 0.05184  -0.00530 -0.03424 38  TYR A CZ  
188  O OH  . TYR A 31  ? 0.79488 0.72981 0.57163 0.05028  0.00168  -0.04425 38  TYR A OH  
189  N N   . SER A 32  ? 0.60965 0.55304 0.33180 0.08778  0.01517  0.02489  39  SER A N   
190  C CA  . SER A 32  ? 0.62057 0.54702 0.34175 0.08712  0.03598  0.03610  39  SER A CA  
191  C C   . SER A 32  ? 0.68657 0.61239 0.43531 0.07447  0.04310  0.02672  39  SER A C   
192  O O   . SER A 32  ? 0.60517 0.52257 0.36666 0.06926  0.05911  0.03380  39  SER A O   
193  C CB  . SER A 32  ? 0.65943 0.58549 0.34357 0.09916  0.04485  0.04214  39  SER A CB  
194  O OG  . SER A 32  ? 0.68706 0.61224 0.34329 0.11518  0.04207  0.05585  39  SER A OG  
195  N N   . ASN A 33  ? 0.58094 0.51591 0.33855 0.06993  0.03281  0.01082  40  ASN A N   
196  C CA  . ASN A 33  ? 0.61234 0.54839 0.39120 0.06359  0.03920  0.00247  40  ASN A CA  
197  C C   . ASN A 33  ? 0.66697 0.60399 0.47895 0.05566  0.03538  0.00183  40  ASN A C   
198  O O   . ASN A 33  ? 0.54004 0.47977 0.36566 0.05302  0.02753  -0.00791 40  ASN A O   
199  C CB  . ASN A 33  ? 0.56953 0.50750 0.33768 0.06462  0.03258  -0.01308 40  ASN A CB  
200  C CG  . ASN A 33  ? 0.60908 0.54642 0.39306 0.06390  0.04077  -0.02011 40  ASN A CG  
201  O OD1 . ASN A 33  ? 0.68734 0.62964 0.48119 0.06508  0.05430  -0.01452 40  ASN A OD1 
202  N ND2 . ASN A 33  ? 0.64153 0.57318 0.42757 0.06268  0.03396  -0.03237 40  ASN A ND2 
203  N N   . LYS A 34  ? 0.55139 0.47802 0.42920 0.04304  -0.06443 -0.00410 41  LYS A N   
204  C CA  . LYS A 34  ? 0.48358 0.41783 0.38702 0.03982  -0.05739 -0.00292 41  LYS A CA  
205  C C   . LYS A 34  ? 0.46209 0.38869 0.37094 0.03282  -0.04593 -0.00651 41  LYS A C   
206  O O   . LYS A 34  ? 0.45821 0.39208 0.38685 0.02847  -0.04269 -0.00809 41  LYS A O   
207  C CB  . LYS A 34  ? 0.51154 0.44049 0.41469 0.04896  -0.05209 0.00563  41  LYS A CB  
208  C CG  . LYS A 34  ? 0.44553 0.38789 0.35240 0.05809  -0.06249 0.01008  41  LYS A CG  
209  C CD  . LYS A 34  ? 0.50623 0.43369 0.40366 0.06961  -0.05679 0.01906  41  LYS A CD  
210  C CE  . LYS A 34  ? 0.60912 0.54976 0.50749 0.08254  -0.06720 0.02490  41  LYS A CE  
211  N NZ  . LYS A 34  ? 0.57787 0.53826 0.50157 0.08718  -0.06808 0.02437  41  LYS A NZ  
212  N N   . GLU A 35  ? 0.47136 0.38559 0.36271 0.03300  -0.03962 -0.00736 42  GLU A N   
213  C CA  . GLU A 35  ? 0.53703 0.44794 0.43543 0.02807  -0.02843 -0.00894 42  GLU A CA  
214  C C   . GLU A 35  ? 0.51175 0.42966 0.42520 0.02091  -0.03184 -0.01649 42  GLU A C   
215  O O   . GLU A 35  ? 0.45020 0.36915 0.37469 0.01715  -0.02412 -0.01723 42  GLU A O   
216  C CB  . GLU A 35  ? 0.49001 0.39140 0.36706 0.03213  -0.02068 -0.00760 42  GLU A CB  
217  C CG  . GLU A 35  ? 0.52324 0.41943 0.38311 0.03407  -0.02742 -0.01632 42  GLU A CG  
218  C CD  . GLU A 35  ? 0.66176 0.54825 0.49408 0.04283  -0.01910 -0.01460 42  GLU A CD  
219  O OE1 . GLU A 35  ? 0.62572 0.50964 0.44492 0.04839  -0.01416 -0.00583 42  GLU A OE1 
220  O OE2 . GLU A 35  ? 0.72074 0.60139 0.54290 0.04550  -0.01687 -0.02135 42  GLU A OE2 
221  N N   . ILE A 36  ? 0.50404 0.42713 0.41892 0.01812  -0.04393 -0.02104 43  ILE A N   
222  C CA  . ILE A 36  ? 0.40766 0.33405 0.33482 0.01024  -0.04717 -0.02645 43  ILE A CA  
223  C C   . ILE A 36  ? 0.53573 0.47455 0.48688 0.00653  -0.04254 -0.02397 43  ILE A C   
224  O O   . ILE A 36  ? 0.46148 0.40195 0.42214 0.00083  -0.04182 -0.02656 43  ILE A O   
225  C CB  . ILE A 36  ? 0.48432 0.41300 0.40920 0.00508  -0.06267 -0.03040 43  ILE A CB  
226  C CG1 . ILE A 36  ? 0.52346 0.47188 0.46325 0.00516  -0.07043 -0.02515 43  ILE A CG1 
227  C CG2 . ILE A 36  ? 0.53115 0.44229 0.42609 0.00945  -0.06832 -0.03550 43  ILE A CG2 
228  C CD1 . ILE A 36  ? 0.47639 0.44426 0.44418 -0.00231 -0.07178 -0.02276 43  ILE A CD1 
229  N N   . PHE A 37  ? 0.42894 0.37387 0.38704 0.01095  -0.03933 -0.01906 44  PHE A N   
230  C CA  . PHE A 37  ? 0.36763 0.32141 0.34307 0.00967  -0.03489 -0.01811 44  PHE A CA  
231  C C   . PHE A 37  ? 0.39063 0.33793 0.36819 0.00605  -0.02693 -0.02033 44  PHE A C   
232  O O   . PHE A 37  ? 0.37376 0.32810 0.36295 0.00289  -0.02562 -0.02151 44  PHE A O   
233  C CB  . PHE A 37  ? 0.40558 0.35916 0.38178 0.01754  -0.03237 -0.01384 44  PHE A CB  
234  C CG  . PHE A 37  ? 0.39228 0.32889 0.35956 0.01879  -0.02450 -0.01213 44  PHE A CG  
235  C CD1 . PHE A 37  ? 0.39479 0.32743 0.36885 0.01563  -0.01896 -0.01391 44  PHE A CD1 
236  C CD2 . PHE A 37  ? 0.37142 0.29659 0.32331 0.02202  -0.02325 -0.00797 44  PHE A CD2 
237  C CE1 . PHE A 37  ? 0.38999 0.30838 0.35890 0.01350  -0.01352 -0.01155 44  PHE A CE1 
238  C CE2 . PHE A 37  ? 0.47642 0.38780 0.42298 0.02064  -0.01565 -0.00408 44  PHE A CE2 
239  C CZ  . PHE A 37  ? 0.40902 0.31744 0.36573 0.01522  -0.01134 -0.00589 44  PHE A CZ  
240  N N   . LEU A 38  ? 0.43060 0.36722 0.39758 0.00702  -0.02141 -0.01977 45  LEU A N   
241  C CA  . LEU A 38  ? 0.41358 0.34911 0.38596 0.00391  -0.01446 -0.02048 45  LEU A CA  
242  C C   . LEU A 38  ? 0.44149 0.37892 0.41596 0.00141  -0.01593 -0.02449 45  LEU A C   
243  O O   . LEU A 38  ? 0.40925 0.35122 0.39363 -0.00121 -0.01373 -0.02530 45  LEU A O   
244  C CB  . LEU A 38  ? 0.40419 0.33334 0.36811 0.00545  -0.00725 -0.01646 45  LEU A CB  
245  C CG  . LEU A 38  ? 0.40582 0.33912 0.38066 0.00112  -0.00080 -0.01502 45  LEU A CG  
246  C CD1 . LEU A 38  ? 0.35802 0.29082 0.34323 -0.00278 -0.00286 -0.01568 45  LEU A CD1 
247  C CD2 . LEU A 38  ? 0.48889 0.42114 0.45941 0.00122  0.00736  -0.00828 45  LEU A CD2 
248  N N   . ARG A 39  ? 0.36249 0.29361 0.32510 0.00273  -0.02054 -0.02717 46  ARG A N   
249  C CA  . ARG A 39  ? 0.37822 0.30453 0.33964 0.00046  -0.02383 -0.03124 46  ARG A CA  
250  C C   . ARG A 39  ? 0.39723 0.33223 0.37418 -0.00595 -0.02808 -0.03041 46  ARG A C   
251  O O   . ARG A 39  ? 0.44747 0.38175 0.42965 -0.00785 -0.02640 -0.03073 46  ARG A O   
252  C CB  . ARG A 39  ? 0.38204 0.29535 0.32474 0.00203  -0.03133 -0.03553 46  ARG A CB  
253  C CG  . ARG A 39  ? 0.51473 0.41449 0.45119 -0.00024 -0.03627 -0.04059 46  ARG A CG  
254  C CD  . ARG A 39  ? 0.47863 0.36171 0.39431 -0.00050 -0.04725 -0.04645 46  ARG A CD  
255  N NE  . ARG A 39  ? 0.57341 0.46600 0.49806 -0.00902 -0.05879 -0.04488 46  ARG A NE  
256  C CZ  . ARG A 39  ? 0.77215 0.65830 0.68170 -0.00933 -0.06971 -0.04821 46  ARG A CZ  
257  N NH1 . ARG A 39  ? 0.62077 0.48788 0.50137 -0.00079 -0.07004 -0.05404 46  ARG A NH1 
258  N NH2 . ARG A 39  ? 0.61269 0.51374 0.53601 -0.01744 -0.08066 -0.04527 46  ARG A NH2 
259  N N   . GLU A 40  ? 0.43834 0.38348 0.42280 -0.00804 -0.03285 -0.02804 47  GLU A N   
260  C CA  . GLU A 40  ? 0.35297 0.31053 0.35266 -0.01350 -0.03550 -0.02537 47  GLU A CA  
261  C C   . GLU A 40  ? 0.38405 0.34828 0.39224 -0.01169 -0.02795 -0.02376 47  GLU A C   
262  O O   . GLU A 40  ? 0.40876 0.37676 0.42349 -0.01528 -0.02732 -0.02212 47  GLU A O   
263  C CB  . GLU A 40  ? 0.35727 0.32981 0.36519 -0.01381 -0.04119 -0.02195 47  GLU A CB  
264  C CG  . GLU A 40  ? 0.38899 0.35763 0.38941 -0.01730 -0.05230 -0.02358 47  GLU A CG  
265  C CD  . GLU A 40  ? 0.53409 0.48982 0.53004 -0.02637 -0.05916 -0.02674 47  GLU A CD  
266  O OE1 . GLU A 40  ? 0.48007 0.44156 0.48891 -0.03316 -0.05834 -0.02343 47  GLU A OE1 
267  O OE2 . GLU A 40  ? 0.52409 0.46151 0.50119 -0.02597 -0.06530 -0.03237 47  GLU A OE2 
268  N N   . LEU A 41  ? 0.35205 0.31560 0.35830 -0.00656 -0.02308 -0.02402 48  LEU A N   
269  C CA  . LEU A 41  ? 0.34700 0.31398 0.35803 -0.00519 -0.01840 -0.02414 48  LEU A CA  
270  C C   . LEU A 41  ? 0.41625 0.37873 0.42650 -0.00714 -0.01598 -0.02561 48  LEU A C   
271  O O   . LEU A 41  ? 0.35884 0.32600 0.37306 -0.00767 -0.01492 -0.02537 48  LEU A O   
272  C CB  . LEU A 41  ? 0.36297 0.32484 0.37022 -0.00070 -0.01600 -0.02460 48  LEU A CB  
273  C CG  . LEU A 41  ? 0.37748 0.34376 0.38488 0.00511  -0.01775 -0.02260 48  LEU A CG  
274  C CD1 . LEU A 41  ? 0.44797 0.40141 0.44811 0.01003  -0.01552 -0.02320 48  LEU A CD1 
275  C CD2 . LEU A 41  ? 0.36536 0.34806 0.38193 0.00738  -0.01765 -0.02077 48  LEU A CD2 
276  N N   . ILE A 42  ? 0.34921 0.30427 0.35354 -0.00655 -0.01470 -0.02652 49  ILE A N   
277  C CA  . ILE A 42  ? 0.37887 0.33336 0.38421 -0.00598 -0.01208 -0.02692 49  ILE A CA  
278  C C   . ILE A 42  ? 0.49275 0.44438 0.49768 -0.00700 -0.01497 -0.02684 49  ILE A C   
279  O O   . ILE A 42  ? 0.37719 0.33154 0.38567 -0.00619 -0.01400 -0.02580 49  ILE A O   
280  C CB  . ILE A 42  ? 0.34539 0.29535 0.34396 -0.00259 -0.00818 -0.02677 49  ILE A CB  
281  C CG1 . ILE A 42  ? 0.36206 0.31546 0.36417 -0.00394 -0.00427 -0.02416 49  ILE A CG1 
282  C CG2 . ILE A 42  ? 0.35287 0.30332 0.35147 0.00138  -0.00550 -0.02691 49  ILE A CG2 
283  C CD1 . ILE A 42  ? 0.41606 0.36849 0.41195 -0.00062 0.00170  -0.02124 49  ILE A CD1 
284  N N   . SER A 43  ? 0.33097 0.27620 0.33134 -0.00950 -0.01970 -0.02729 50  SER A N   
285  C CA  . SER A 43  ? 0.45074 0.38938 0.45077 -0.01316 -0.02355 -0.02606 50  SER A CA  
286  C C   . SER A 43  ? 0.36601 0.31697 0.37675 -0.01662 -0.02271 -0.02125 50  SER A C   
287  O O   . SER A 43  ? 0.40752 0.35514 0.41851 -0.01737 -0.02243 -0.01838 50  SER A O   
288  C CB  . SER A 43  ? 0.38838 0.31726 0.38221 -0.01803 -0.03118 -0.02761 50  SER A CB  
289  O OG  . SER A 43  ? 0.61355 0.53549 0.60966 -0.02516 -0.03609 -0.02482 50  SER A OG  
290  N N   . ASN A 44  ? 0.41460 0.37915 0.43208 -0.01685 -0.02163 -0.01983 51  ASN A N   
291  C CA  . ASN A 44  ? 0.39784 0.37539 0.42207 -0.01683 -0.01878 -0.01558 51  ASN A CA  
292  C C   . ASN A 44  ? 0.43049 0.40729 0.45129 -0.01259 -0.01558 -0.01694 51  ASN A C   
293  O O   . ASN A 44  ? 0.36257 0.34299 0.38353 -0.01267 -0.01441 -0.01298 51  ASN A O   
294  C CB  . ASN A 44  ? 0.29099 0.28144 0.31979 -0.01355 -0.01722 -0.01507 51  ASN A CB  
295  C CG  . ASN A 44  ? 0.53978 0.54061 0.57741 -0.01811 -0.02110 -0.01071 51  ASN A CG  
296  O OD1 . ASN A 44  ? 0.38268 0.37827 0.42217 -0.02612 -0.02636 -0.00878 51  ASN A OD1 
297  N ND2 . ASN A 44  ? 0.32783 0.34284 0.37079 -0.01280 -0.01952 -0.00914 51  ASN A ND2 
298  N N   . SER A 45  ? 0.40811 0.38125 0.42612 -0.00958 -0.01476 -0.02149 52  SER A N   
299  C CA  . SER A 45  ? 0.30232 0.27734 0.31964 -0.00732 -0.01413 -0.02279 52  SER A CA  
300  C C   . SER A 45  ? 0.44615 0.41787 0.46278 -0.00623 -0.01480 -0.02024 52  SER A C   
301  O O   . SER A 45  ? 0.38995 0.36594 0.40571 -0.00432 -0.01541 -0.01810 52  SER A O   
302  C CB  . SER A 45  ? 0.33393 0.30721 0.35218 -0.00727 -0.01367 -0.02618 52  SER A CB  
303  O OG  . SER A 45  ? 0.40527 0.37722 0.42151 -0.00715 -0.01378 -0.02850 52  SER A OG  
304  N N   . SER A 46  ? 0.37006 0.33217 0.38420 -0.00572 -0.01501 -0.02067 53  SER A N   
305  C CA  . SER A 46  ? 0.32873 0.28267 0.33920 -0.00200 -0.01554 -0.01870 53  SER A CA  
306  C C   . SER A 46  ? 0.39113 0.34074 0.39979 -0.00483 -0.01734 -0.01323 53  SER A C   
307  O O   . SER A 46  ? 0.43435 0.38186 0.44066 -0.00069 -0.01759 -0.00970 53  SER A O   
308  C CB  . SER A 46  ? 0.35429 0.29365 0.35699 0.00047  -0.01567 -0.02162 53  SER A CB  
309  O OG  . SER A 46  ? 0.38882 0.31558 0.38468 0.00681  -0.01599 -0.02061 53  SER A OG  
310  N N   . ASP A 47  ? 0.39626 0.34636 0.40702 -0.01179 -0.01849 -0.01093 54  ASP A N   
311  C CA  . ASP A 47  ? 0.42187 0.37161 0.43355 -0.01637 -0.01882 -0.00303 54  ASP A CA  
312  C C   . ASP A 47  ? 0.52176 0.48559 0.53345 -0.01235 -0.01547 0.00050  54  ASP A C   
313  O O   . ASP A 47  ? 0.37286 0.33368 0.38055 -0.01146 -0.01500 0.00737  54  ASP A O   
314  C CB  . ASP A 47  ? 0.45532 0.41048 0.47415 -0.02538 -0.02042 0.00010  54  ASP A CB  
315  C CG  . ASP A 47  ? 0.48740 0.42513 0.50286 -0.03098 -0.02679 -0.00315 54  ASP A CG  
316  O OD1 . ASP A 47  ? 0.52176 0.43876 0.52648 -0.02736 -0.02893 -0.00651 54  ASP A OD1 
317  O OD2 . ASP A 47  ? 0.48398 0.42885 0.50625 -0.03781 -0.03020 -0.00263 54  ASP A OD2 
318  N N   . ALA A 48  ? 0.35533 0.33166 0.36851 -0.00933 -0.01375 -0.00420 55  ALA A N   
319  C CA  . ALA A 48  ? 0.38096 0.36741 0.38922 -0.00460 -0.01207 -0.00316 55  ALA A CA  
320  C C   . ALA A 48  ? 0.42502 0.40898 0.42872 0.00027  -0.01505 -0.00374 55  ALA A C   
321  O O   . ALA A 48  ? 0.32390 0.31178 0.32052 0.00389  -0.01518 0.00068  55  ALA A O   
322  C CB  . ALA A 48  ? 0.43274 0.42584 0.44021 -0.00210 -0.01134 -0.01003 55  ALA A CB  
323  N N   . LEU A 49  ? 0.31108 0.29112 0.31887 0.00138  -0.01721 -0.00827 56  LEU A N   
324  C CA  . LEU A 49  ? 0.37534 0.35783 0.38320 0.00693  -0.02008 -0.00764 56  LEU A CA  
325  C C   . LEU A 49  ? 0.44778 0.41954 0.45040 0.01060  -0.02013 -0.00026 56  LEU A C   
326  O O   . LEU A 49  ? 0.35752 0.33315 0.35598 0.01631  -0.02246 0.00392  56  LEU A O   
327  C CB  . LEU A 49  ? 0.30857 0.29329 0.32443 0.00776  -0.02009 -0.01228 56  LEU A CB  
328  C CG  . LEU A 49  ? 0.33823 0.33152 0.35873 0.00339  -0.02128 -0.01787 56  LEU A CG  
329  C CD1 . LEU A 49  ? 0.32171 0.31495 0.34932 0.00184  -0.01862 -0.02012 56  LEU A CD1 
330  C CD2 . LEU A 49  ? 0.30382 0.30900 0.32596 0.00449  -0.02699 -0.01872 56  LEU A CD2 
331  N N   . ASP A 50  ? 0.47250 0.42840 0.47359 0.00736  -0.01880 0.00146  57  ASP A N   
332  C CA  . ASP A 50  ? 0.46200 0.40077 0.45567 0.00907  -0.01964 0.00893  57  ASP A CA  
333  C C   . ASP A 50  ? 0.43602 0.37993 0.42506 0.00755  -0.01862 0.01801  57  ASP A C   
334  O O   . ASP A 50  ? 0.41922 0.35596 0.40080 0.01334  -0.01978 0.02514  57  ASP A O   
335  C CB  . ASP A 50  ? 0.39488 0.31372 0.38646 0.00171  -0.02051 0.00874  57  ASP A CB  
336  C CG  . ASP A 50  ? 0.49630 0.40326 0.48482 0.00667  -0.02139 0.00093  57  ASP A CG  
337  O OD1 . ASP A 50  ? 0.50309 0.41550 0.49183 0.01734  -0.02010 -0.00141 57  ASP A OD1 
338  O OD2 . ASP A 50  ? 0.52707 0.42094 0.51279 0.00024  -0.02351 -0.00236 57  ASP A OD2 
339  N N   . LYS A 51  ? 0.37478 0.33142 0.36676 0.00154  -0.01574 0.01868  58  LYS A N   
340  C CA  . LYS A 51  ? 0.37748 0.34069 0.36378 0.00074  -0.01243 0.02867  58  LYS A CA  
341  C C   . LYS A 51  ? 0.40752 0.37987 0.38389 0.01047  -0.01412 0.02903  58  LYS A C   
342  O O   . LYS A 51  ? 0.43269 0.40117 0.39942 0.01406  -0.01361 0.03904  58  LYS A O   
343  C CB  . LYS A 51  ? 0.42993 0.40828 0.42207 -0.00475 -0.00766 0.02892  58  LYS A CB  
344  C CG  . LYS A 51  ? 0.76764 0.75681 0.75448 -0.00470 -0.00158 0.04077  58  LYS A CG  
345  C CD  . LYS A 51  ? 0.78510 0.78614 0.78422 -0.01360 0.00365  0.04723  58  LYS A CD  
346  C CE  . LYS A 51  ? 0.80428 0.81642 0.79991 -0.01471 0.01135  0.06333  58  LYS A CE  
347  N NZ  . LYS A 51  ? 0.84146 0.87858 0.84900 -0.01787 0.01916  0.06933  58  LYS A NZ  
348  N N   . ILE A 52  ? 0.36589 0.34923 0.34360 0.01417  -0.01726 0.01876  59  ILE A N   
349  C CA  . ILE A 52  ? 0.36422 0.35648 0.33227 0.02191  -0.02190 0.01797  59  ILE A CA  
350  C C   . ILE A 52  ? 0.37207 0.35980 0.34086 0.02846  -0.02686 0.02155  59  ILE A C   
351  O O   . ILE A 52  ? 0.41023 0.40202 0.36875 0.03566  -0.03055 0.02682  59  ILE A O   
352  C CB  . ILE A 52  ? 0.35486 0.35725 0.32434 0.02161  -0.02607 0.00592  59  ILE A CB  
353  C CG1 . ILE A 52  ? 0.45312 0.46366 0.40931 0.02801  -0.03299 0.00446  59  ILE A CG1 
354  C CG2 . ILE A 52  ? 0.39453 0.39723 0.37905 0.01880  -0.02925 -0.00081 59  ILE A CG2 
355  C CD1 . ILE A 52  ? 0.48462 0.49595 0.42183 0.03302  -0.02868 0.01175  59  ILE A CD1 
356  N N   . ARG A 53  ? 0.38370 0.36335 0.36275 0.02814  -0.02692 0.01909  60  ARG A N   
357  C CA  . ARG A 53  ? 0.45564 0.43119 0.43494 0.03776  -0.03025 0.02299  60  ARG A CA  
358  C C   . ARG A 53  ? 0.40028 0.35804 0.36687 0.04153  -0.02896 0.03512  60  ARG A C   
359  O O   . ARG A 53  ? 0.43744 0.39649 0.39747 0.05186  -0.03282 0.04136  60  ARG A O   
360  C CB  . ARG A 53  ? 0.38258 0.35116 0.37156 0.03897  -0.02855 0.01786  60  ARG A CB  
361  C CG  . ARG A 53  ? 0.50165 0.46622 0.49038 0.05238  -0.03036 0.02179  60  ARG A CG  
362  C CD  . ARG A 53  ? 0.59946 0.55721 0.59410 0.05607  -0.02687 0.01629  60  ARG A CD  
363  N NE  . ARG A 53  ? 0.84425 0.77500 0.83036 0.04916  -0.02384 0.01460  60  ARG A NE  
364  C CZ  . ARG A 53  ? 0.93567 0.85420 0.92036 0.05150  -0.02119 0.00881  60  ARG A CZ  
365  N NH1 . ARG A 53  ? 0.74685 0.67928 0.73890 0.06153  -0.01867 0.00538  60  ARG A NH1 
366  N NH2 . ARG A 53  ? 0.62042 0.51382 0.59598 0.04350  -0.02127 0.00695  60  ARG A NH2 
367  N N   . TYR A 54  ? 0.48042 0.42181 0.44414 0.03265  -0.02425 0.03970  61  TYR A N   
368  C CA  . TYR A 54  ? 0.46592 0.38745 0.41833 0.03285  -0.02289 0.05309  61  TYR A CA  
369  C C   . TYR A 54  ? 0.44268 0.37641 0.38361 0.03647  -0.02207 0.06230  61  TYR A C   
370  O O   . TYR A 54  ? 0.46520 0.38995 0.39456 0.04515  -0.02415 0.07229  61  TYR A O   
371  C CB  . TYR A 54  ? 0.46162 0.36736 0.41723 0.01878  -0.01930 0.05650  61  TYR A CB  
372  C CG  . TYR A 54  ? 0.54802 0.43324 0.49392 0.01453  -0.01772 0.07246  61  TYR A CG  
373  C CD1 . TYR A 54  ? 0.67920 0.53102 0.61672 0.01766  -0.02121 0.07683  61  TYR A CD1 
374  C CD2 . TYR A 54  ? 0.53778 0.43564 0.48175 0.00784  -0.01212 0.08388  61  TYR A CD2 
375  C CE1 . TYR A 54  ? 0.52584 0.35442 0.45377 0.01207  -0.02035 0.09271  61  TYR A CE1 
376  C CE2 . TYR A 54  ? 0.61727 0.49745 0.55362 0.00220  -0.00973 0.10109  61  TYR A CE2 
377  C CZ  . TYR A 54  ? 0.79267 0.63669 0.72131 0.00315  -0.01445 0.10573  61  TYR A CZ  
378  O OH  . TYR A 54  ? 0.70099 0.52303 0.62133 -0.00419 -0.01262 0.12423  61  TYR A OH  
379  N N   . GLU A 55  ? 0.43127 0.38402 0.37249 0.03168  -0.01883 0.05928  62  GLU A N   
380  C CA  . GLU A 55  ? 0.48235 0.44619 0.40810 0.03654  -0.01694 0.06725  62  GLU A CA  
381  C C   . GLU A 55  ? 0.45401 0.42597 0.37019 0.04934  -0.02541 0.06516  62  GLU A C   
382  O O   . GLU A 55  ? 0.52266 0.49417 0.42191 0.05678  -0.02607 0.07589  62  GLU A O   
383  C CB  . GLU A 55  ? 0.43201 0.41382 0.35774 0.03258  -0.01205 0.06125  62  GLU A CB  
384  C CG  . GLU A 55  ? 0.48572 0.46718 0.41984 0.02162  -0.00288 0.06857  62  GLU A CG  
385  C CD  . GLU A 55  ? 0.84093 0.84259 0.77036 0.02302  0.00423  0.06711  62  GLU A CD  
386  O OE1 . GLU A 55  ? 0.64704 0.65763 0.56103 0.03289  0.00178  0.06038  62  GLU A OE1 
387  O OE2 . GLU A 55  ? 0.70512 0.71371 0.64584 0.01486  0.01168  0.07254  62  GLU A OE2 
388  N N   . SER A 56  ? 0.47781 0.45886 0.40540 0.05175  -0.03233 0.05275  63  SER A N   
389  C CA  . SER A 56  ? 0.55378 0.54847 0.47718 0.06203  -0.04232 0.05061  63  SER A CA  
390  C C   . SER A 56  ? 0.60424 0.58885 0.52375 0.07315  -0.04536 0.06158  63  SER A C   
391  O O   . SER A 56  ? 0.52038 0.51735 0.43346 0.08351  -0.05393 0.06395  63  SER A O   
392  C CB  . SER A 56  ? 0.55086 0.56062 0.49205 0.05926  -0.04840 0.03672  63  SER A CB  
393  O OG  . SER A 56  ? 0.56888 0.57195 0.52583 0.06016  -0.04640 0.03608  63  SER A OG  
394  N N   . LEU A 57  ? 0.59845 0.55924 0.52013 0.07181  -0.03969 0.06821  64  LEU A N   
395  C CA  . LEU A 57  ? 0.70692 0.65129 0.62109 0.08426  -0.04218 0.07906  64  LEU A CA  
396  C C   . LEU A 57  ? 0.69517 0.63475 0.58757 0.08988  -0.04241 0.09402  64  LEU A C   
397  O O   . LEU A 57  ? 0.79310 0.73406 0.67694 0.10440  -0.04883 0.10117  64  LEU A O   
398  C CB  . LEU A 57  ? 0.61532 0.52779 0.53178 0.08045  -0.03700 0.08152  64  LEU A CB  
399  C CG  . LEU A 57  ? 0.69170 0.60491 0.62449 0.07919  -0.03657 0.06829  64  LEU A CG  
400  C CD1 . LEU A 57  ? 0.66773 0.54324 0.59506 0.07816  -0.03366 0.07062  64  LEU A CD1 
401  C CD2 . LEU A 57  ? 0.75261 0.68829 0.69510 0.09368  -0.04232 0.06379  64  LEU A CD2 
402  N N   . THR A 58  ? 0.63985 0.57560 0.52304 0.07973  -0.03494 0.10033  65  THR A N   
403  C CA  . THR A 58  ? 0.73646 0.66932 0.59706 0.08524  -0.03315 0.11626  65  THR A CA  
404  C C   . THR A 58  ? 0.73746 0.69713 0.58538 0.08953  -0.03639 0.11129  65  THR A C   
405  O O   . THR A 58  ? 0.69365 0.65410 0.51881 0.09721  -0.03600 0.12354  65  THR A O   
406  C CB  . THR A 58  ? 0.63297 0.54758 0.48947 0.07267  -0.02189 0.13014  65  THR A CB  
407  O OG1 . THR A 58  ? 0.90494 0.83710 0.76964 0.06102  -0.01510 0.12299  65  THR A OG1 
408  C CG2 . THR A 58  ? 0.69176 0.57486 0.55838 0.06613  -0.02111 0.13265  65  THR A CG2 
409  N N   . ASP A 59  ? 0.75221 0.73083 0.61132 0.08521  -0.04004 0.09378  66  ASP A N   
410  C CA  . ASP A 59  ? 0.60224 0.60066 0.44630 0.08901  -0.04516 0.08603  66  ASP A CA  
411  C C   . ASP A 59  ? 0.69990 0.71378 0.56058 0.08678  -0.05581 0.06761  66  ASP A C   
412  O O   . ASP A 59  ? 0.55101 0.56870 0.42160 0.07748  -0.05302 0.05551  66  ASP A O   
413  C CB  . ASP A 59  ? 0.58468 0.58530 0.41880 0.08254  -0.03342 0.08699  66  ASP A CB  
414  C CG  . ASP A 59  ? 0.81934 0.83433 0.63001 0.08960  -0.03813 0.07873  66  ASP A CG  
415  O OD1 . ASP A 59  ? 0.75735 0.77992 0.55884 0.09756  -0.05223 0.07303  66  ASP A OD1 
416  O OD2 . ASP A 59  ? 0.87547 0.89439 0.67616 0.08790  -0.02827 0.07775  66  ASP A OD2 
417  N N   . PRO A 60  ? 0.60415 0.62850 0.46959 0.09508  -0.06836 0.06634  67  PRO A N   
418  C CA  . PRO A 60  ? 0.70850 0.75038 0.59511 0.09066  -0.07827 0.05152  67  PRO A CA  
419  C C   . PRO A 60  ? 0.55643 0.60841 0.43400 0.08453  -0.08494 0.03752  67  PRO A C   
420  O O   . PRO A 60  ? 0.57345 0.63387 0.46947 0.07578  -0.08979 0.02519  67  PRO A O   
421  C CB  . PRO A 60  ? 0.57530 0.63116 0.46674 0.10284  -0.09056 0.05708  67  PRO A CB  
422  C CG  . PRO A 60  ? 0.69174 0.72822 0.57088 0.11314  -0.08362 0.07421  67  PRO A CG  
423  C CD  . PRO A 60  ? 0.66372 0.68534 0.51871 0.10889  -0.07365 0.08019  67  PRO A CD  
424  N N   . SER A 61  ? 0.52586 0.57499 0.37346 0.08941  -0.08504 0.03923  68  SER A N   
425  C CA  . SER A 61  ? 0.53110 0.58392 0.36457 0.08577  -0.09199 0.02425  68  SER A CA  
426  C C   . SER A 61  ? 0.54363 0.58785 0.38681 0.07545  -0.08144 0.01500  68  SER A C   
427  O O   . SER A 61  ? 0.59656 0.64025 0.43448 0.07088  -0.08817 0.00041  68  SER A O   
428  C CB  . SER A 61  ? 0.55823 0.60818 0.35222 0.09657  -0.09260 0.02836  68  SER A CB  
429  O OG  . SER A 61  ? 0.66887 0.70858 0.45165 0.09822  -0.07391 0.03867  68  SER A OG  
430  N N   . LYS A 62  ? 0.56429 0.60028 0.42112 0.07156  -0.06655 0.02301  69  LYS A N   
431  C CA  . LYS A 62  ? 0.51605 0.54650 0.38455 0.06253  -0.05774 0.01520  69  LYS A CA  
432  C C   . LYS A 62  ? 0.46236 0.49648 0.35370 0.05363  -0.06554 0.00266  69  LYS A C   
433  O O   . LYS A 62  ? 0.49846 0.52730 0.39516 0.04716  -0.06125 -0.00582 69  LYS A O   
434  C CB  . LYS A 62  ? 0.54373 0.56625 0.42389 0.05893  -0.04332 0.02717  69  LYS A CB  
435  C CG  . LYS A 62  ? 0.60160 0.62211 0.46100 0.06458  -0.03327 0.04079  69  LYS A CG  
436  C CD  . LYS A 62  ? 0.57410 0.58939 0.44629 0.05688  -0.01941 0.05034  69  LYS A CD  
437  C CE  . LYS A 62  ? 0.61693 0.63346 0.47160 0.06108  -0.00912 0.06761  69  LYS A CE  
438  N NZ  . LYS A 62  ? 0.68985 0.70500 0.56054 0.05078  0.00314  0.07803  69  LYS A NZ  
439  N N   . LEU A 63  ? 0.50590 0.55062 0.41117 0.05377  -0.07641 0.00258  70  LEU A N   
440  C CA  . LEU A 63  ? 0.49453 0.54736 0.42313 0.04471  -0.08352 -0.00675 70  LEU A CA  
441  C C   . LEU A 63  ? 0.55289 0.61380 0.47404 0.04140  -0.10033 -0.01741 70  LEU A C   
442  O O   . LEU A 63  ? 0.50102 0.57179 0.44334 0.03215  -0.10834 -0.02322 70  LEU A O   
443  C CB  . LEU A 63  ? 0.41076 0.47448 0.36376 0.04693  -0.08376 0.00076  70  LEU A CB  
444  C CG  . LEU A 63  ? 0.47220 0.52361 0.43459 0.04805  -0.06984 0.00809  70  LEU A CG  
445  C CD1 . LEU A 63  ? 0.39963 0.46051 0.38081 0.05439  -0.07116 0.01398  70  LEU A CD1 
446  C CD2 . LEU A 63  ? 0.37925 0.42157 0.35002 0.03792  -0.06176 0.00086  70  LEU A CD2 
447  N N   . ASP A 64  ? 0.48289 0.53963 0.37357 0.04832  -0.10632 -0.01958 71  ASP A N   
448  C CA  . ASP A 64  ? 0.55341 0.61199 0.43138 0.04437  -0.12439 -0.03218 71  ASP A CA  
449  C C   . ASP A 64  ? 0.59716 0.64177 0.47810 0.03293  -0.12521 -0.04593 71  ASP A C   
450  O O   . ASP A 64  ? 0.50048 0.54617 0.38397 0.02352  -0.14156 -0.05622 71  ASP A O   
451  C CB  . ASP A 64  ? 0.52611 0.57761 0.36341 0.05619  -0.12844 -0.03305 71  ASP A CB  
452  C CG  . ASP A 64  ? 0.68788 0.75315 0.51969 0.06714  -0.13271 -0.01980 71  ASP A CG  
453  O OD1 . ASP A 64  ? 0.60821 0.68942 0.46853 0.06579  -0.13563 -0.01214 71  ASP A OD1 
454  O OD2 . ASP A 64  ? 0.66431 0.72422 0.46219 0.07864  -0.13220 -0.01626 71  ASP A OD2 
455  N N   . SER A 65  ? 0.56676 0.59777 0.44768 0.03311  -0.10885 -0.04562 72  SER A N   
456  C CA  . SER A 65  ? 0.47238 0.48785 0.35545 0.02458  -0.10789 -0.05682 72  SER A CA  
457  C C   . SER A 65  ? 0.66302 0.68569 0.58195 0.01226  -0.10615 -0.05488 72  SER A C   
458  O O   . SER A 65  ? 0.53194 0.54105 0.45497 0.00547  -0.10272 -0.06116 72  SER A O   
459  C CB  . SER A 65  ? 0.51292 0.51433 0.37991 0.03251  -0.09129 -0.05625 72  SER A CB  
460  O OG  . SER A 65  ? 0.54361 0.55376 0.42546 0.03545  -0.07660 -0.04249 72  SER A OG  
461  N N   . GLY A 66  ? 0.51621 0.55954 0.45933 0.01118  -0.10749 -0.04561 73  GLY A N   
462  C CA  . GLY A 66  ? 0.41291 0.46614 0.38819 0.00174  -0.10469 -0.04283 73  GLY A CA  
463  C C   . GLY A 66  ? 0.38411 0.45181 0.37751 0.00854  -0.09581 -0.03060 73  GLY A C   
464  O O   . GLY A 66  ? 0.46603 0.52349 0.45401 0.01480  -0.08278 -0.02537 73  GLY A O   
465  N N   . LYS A 67  ? 0.46083 0.55213 0.47624 0.00740  -0.10318 -0.02594 74  LYS A N   
466  C CA  . LYS A 67  ? 0.58265 0.68597 0.61292 0.01707  -0.09531 -0.01505 74  LYS A CA  
467  C C   . LYS A 67  ? 0.54529 0.64629 0.59357 0.01375  -0.08266 -0.01328 74  LYS A C   
468  O O   . LYS A 67  ? 0.47275 0.56897 0.52218 0.02300  -0.07261 -0.00688 74  LYS A O   
469  C CB  . LYS A 67  ? 0.49325 0.62676 0.54099 0.02032  -0.10736 -0.00989 74  LYS A CB  
470  C CG  . LYS A 67  ? 0.70660 0.84282 0.73477 0.03165  -0.11625 -0.00613 74  LYS A CG  
471  C CD  . LYS A 67  ? 0.72577 0.89345 0.77408 0.04024  -0.12470 0.00267  74  LYS A CD  
472  C CE  . LYS A 67  ? 0.88737 1.06934 0.92488 0.04079  -0.14465 0.00070  74  LYS A CE  
473  N NZ  . LYS A 67  ? 0.70875 0.93112 0.77686 0.04157  -0.15745 0.00645  74  LYS A NZ  
474  N N   . GLU A 68  ? 0.37922 0.48043 0.43862 0.00101  -0.08345 -0.01878 75  GLU A N   
475  C CA  . GLU A 68  ? 0.38565 0.48783 0.46148 -0.00172 -0.07219 -0.01612 75  GLU A CA  
476  C C   . GLU A 68  ? 0.41220 0.48821 0.47246 0.00069  -0.06033 -0.01808 75  GLU A C   
477  O O   . GLU A 68  ? 0.45000 0.50863 0.49380 -0.00296 -0.06105 -0.02406 75  GLU A O   
478  C CB  . GLU A 68  ? 0.41219 0.52223 0.50411 -0.01719 -0.07730 -0.01934 75  GLU A CB  
479  C CG  . GLU A 68  ? 0.60367 0.73407 0.70610 -0.02506 -0.09410 -0.02046 75  GLU A CG  
480  C CD  . GLU A 68  ? 0.81762 0.98564 0.95120 -0.02308 -0.09513 -0.01060 75  GLU A CD  
481  O OE1 . GLU A 68  ? 1.07949 1.26877 1.23465 -0.03679 -0.10548 -0.00945 75  GLU A OE1 
482  O OE2 . GLU A 68  ? 0.95557 1.13185 1.09242 -0.00770 -0.08570 -0.00359 75  GLU A OE2 
483  N N   . LEU A 69  ? 0.38734 0.46111 0.45246 0.00753  -0.04995 -0.01321 76  LEU A N   
484  C CA  . LEU A 69  ? 0.34253 0.39410 0.39578 0.00862  -0.04056 -0.01448 76  LEU A CA  
485  C C   . LEU A 69  ? 0.36621 0.41841 0.43013 0.00473  -0.03355 -0.01476 76  LEU A C   
486  O O   . LEU A 69  ? 0.37012 0.43064 0.44273 0.01149  -0.02824 -0.01047 76  LEU A O   
487  C CB  . LEU A 69  ? 0.31242 0.35405 0.35654 0.01939  -0.03623 -0.00926 76  LEU A CB  
488  C CG  . LEU A 69  ? 0.51266 0.55385 0.54544 0.02545  -0.04154 -0.00542 76  LEU A CG  
489  C CD1 . LEU A 69  ? 0.38598 0.41022 0.40911 0.03386  -0.03632 0.00084  76  LEU A CD1 
490  C CD2 . LEU A 69  ? 0.33380 0.36847 0.35267 0.01982  -0.04443 -0.00945 76  LEU A CD2 
491  N N   . HIS A 70  ? 0.32279 0.42977 0.35944 0.00791  -0.00919 0.02832  77  HIS A N   
492  C CA  . HIS A 70  ? 0.28781 0.38757 0.32644 0.00269  -0.00697 0.02675  77  HIS A CA  
493  C C   . HIS A 70  ? 0.37203 0.44596 0.39817 -0.00251 -0.00966 0.01620  77  HIS A C   
494  O O   . HIS A 70  ? 0.29395 0.35758 0.31188 -0.00337 -0.01371 0.00972  77  HIS A O   
495  C CB  . HIS A 70  ? 0.40282 0.52405 0.45262 -0.00702 -0.01150 0.03128  77  HIS A CB  
496  C CG  . HIS A 70  ? 0.39147 0.51646 0.43922 -0.01921 -0.02277 0.02488  77  HIS A CG  
497  N ND1 . HIS A 70  ? 0.43159 0.58504 0.48901 -0.02296 -0.03031 0.02722  77  HIS A ND1 
498  C CD2 . HIS A 70  ? 0.39445 0.49844 0.43111 -0.02775 -0.02798 0.01514  77  HIS A CD2 
499  C CE1 . HIS A 70  ? 0.30424 0.45307 0.35631 -0.03443 -0.04000 0.01767  77  HIS A CE1 
500  N NE2 . HIS A 70  ? 0.48241 0.59977 0.52165 -0.03723 -0.03802 0.01074  77  HIS A NE2 
501  N N   . ILE A 71  ? 0.33426 0.39906 0.35838 -0.00421 -0.00658 0.01553  78  ILE A N   
502  C CA  . ILE A 71  ? 0.31764 0.35993 0.32941 -0.00676 -0.00856 0.00752  78  ILE A CA  
503  C C   . ILE A 71  ? 0.33368 0.37513 0.34591 -0.01527 -0.00886 0.01116  78  ILE A C   
504  O O   . ILE A 71  ? 0.37445 0.42720 0.39429 -0.01441 -0.00297 0.01918  78  ILE A O   
505  C CB  . ILE A 71  ? 0.37252 0.40228 0.37851 0.00335  -0.00286 0.00302  78  ILE A CB  
506  C CG1 . ILE A 71  ? 0.33518 0.36431 0.34495 0.00999  -0.00023 -0.00018 78  ILE A CG1 
507  C CG2 . ILE A 71  ? 0.38854 0.39932 0.38139 0.00303  -0.00593 -0.00464 78  ILE A CG2 
508  C CD1 . ILE A 71  ? 0.33111 0.34971 0.33935 0.01830  0.00528  -0.00708 78  ILE A CD1 
509  N N   . ASN A 72  ? 0.37652 0.40332 0.38099 -0.02299 -0.01415 0.00585  79  ASN A N   
510  C CA  . ASN A 72  ? 0.34147 0.36130 0.34605 -0.03165 -0.01259 0.00942  79  ASN A CA  
511  C C   . ASN A 72  ? 0.34996 0.34388 0.33755 -0.02647 -0.01105 0.00558  79  ASN A C   
512  O O   . ASN A 72  ? 0.35910 0.34019 0.33675 -0.02288 -0.01566 -0.00294 79  ASN A O   
513  C CB  . ASN A 72  ? 0.32871 0.35196 0.33978 -0.04613 -0.01959 0.00640  79  ASN A CB  
514  C CG  . ASN A 72  ? 0.38083 0.43506 0.41015 -0.05135 -0.02218 0.01082  79  ASN A CG  
515  O OD1 . ASN A 72  ? 0.35626 0.42857 0.39636 -0.04659 -0.01616 0.01963  79  ASN A OD1 
516  N ND2 . ASN A 72  ? 0.36691 0.42895 0.39917 -0.06000 -0.03143 0.00431  79  ASN A ND2 
517  N N   . LEU A 73  ? 0.34226 0.33026 0.32639 -0.02471 -0.00397 0.01274  80  LEU A N   
518  C CA  . LEU A 73  ? 0.39112 0.35599 0.35765 -0.01824 -0.00193 0.01171  80  LEU A CA  
519  C C   . LEU A 73  ? 0.39743 0.34851 0.36462 -0.02925 0.00133  0.01745  80  LEU A C   
520  O O   . LEU A 73  ? 0.39505 0.35542 0.37378 -0.03613 0.00814  0.02708  80  LEU A O   
521  C CB  . LEU A 73  ? 0.39046 0.35758 0.34844 -0.00464 0.00480  0.01586  80  LEU A CB  
522  C CG  . LEU A 73  ? 0.41751 0.39830 0.37889 0.00428  0.00371  0.01010  80  LEU A CG  
523  C CD1 . LEU A 73  ? 0.42955 0.41231 0.38145 0.01683  0.01055  0.01311  80  LEU A CD1 
524  C CD2 . LEU A 73  ? 0.37485 0.34798 0.33117 0.00806  -0.00386 -0.00240 80  LEU A CD2 
525  N N   . ILE A 74  ? 0.39970 0.32843 0.35621 -0.03112 -0.00249 0.01157  81  ILE A N   
526  C CA  . ILE A 74  ? 0.41133 0.32244 0.37001 -0.04378 0.00028  0.01439  81  ILE A CA  
527  C C   . ILE A 74  ? 0.49231 0.37324 0.43084 -0.03470 0.00479  0.01681  81  ILE A C   
528  O O   . ILE A 74  ? 0.51799 0.38235 0.44561 -0.03143 -0.00069 0.00824  81  ILE A O   
529  C CB  . ILE A 74  ? 0.42560 0.33695 0.39168 -0.05672 -0.00886 0.00369  81  ILE A CB  
530  C CG1 . ILE A 74  ? 0.39707 0.34049 0.37956 -0.06130 -0.01445 0.00163  81  ILE A CG1 
531  C CG2 . ILE A 74  ? 0.46968 0.36391 0.44232 -0.07286 -0.00561 0.00481  81  ILE A CG2 
532  C CD1 . ILE A 74  ? 0.45280 0.40005 0.43867 -0.07078 -0.02455 -0.00952 81  ILE A CD1 
533  N N   . PRO A 75  ? 0.47984 0.35323 0.41192 -0.02883 0.01543  0.02919  82  PRO A N   
534  C CA  . PRO A 75  ? 0.51179 0.35575 0.42331 -0.01858 0.02081  0.03391  82  PRO A CA  
535  C C   . PRO A 75  ? 0.57746 0.39525 0.49347 -0.03319 0.02593  0.03644  82  PRO A C   
536  O O   . PRO A 75  ? 0.54460 0.36875 0.48077 -0.05129 0.02928  0.03903  82  PRO A O   
537  C CB  . PRO A 75  ? 0.58133 0.42990 0.48414 -0.00649 0.03154  0.04769  82  PRO A CB  
538  C CG  . PRO A 75  ? 0.49033 0.36239 0.41554 -0.01904 0.03610  0.05336  82  PRO A CG  
539  C CD  . PRO A 75  ? 0.44781 0.33973 0.39034 -0.02984 0.02421  0.04068  82  PRO A CD  
540  N N   . ASN A 76  ? 0.54696 0.33542 0.44506 -0.02500 0.02652  0.03481  83  ASN A N   
541  C CA  . ASN A 76  ? 0.55721 0.31352 0.45654 -0.03707 0.03208  0.03545  83  ASN A CA  
542  C C   . ASN A 76  ? 0.60338 0.32833 0.47850 -0.01942 0.04152  0.04593  83  ASN A C   
543  O O   . ASN A 76  ? 0.68265 0.39747 0.54065 -0.00455 0.03562  0.03956  83  ASN A O   
544  C CB  . ASN A 76  ? 0.57659 0.32778 0.47918 -0.04601 0.02061  0.01812  83  ASN A CB  
545  C CG  . ASN A 76  ? 0.62235 0.34294 0.53082 -0.06302 0.02556  0.01538  83  ASN A CG  
546  O OD1 . ASN A 76  ? 0.65742 0.34557 0.55673 -0.06006 0.03769  0.02541  83  ASN A OD1 
547  N ND2 . ASN A 76  ? 0.59529 0.32548 0.51850 -0.08041 0.01645  0.00143  83  ASN A ND2 
548  N N   . LYS A 77  ? 0.61593 0.32679 0.49014 -0.02018 0.05693  0.06290  84  LYS A N   
549  C CA  . LYS A 77  ? 0.72480 0.40625 0.57377 -0.00075 0.06776  0.07620  84  LYS A CA  
550  C C   . LYS A 77  ? 0.81136 0.45230 0.65255 -0.00302 0.07028  0.07237  84  LYS A C   
551  O O   . LYS A 77  ? 0.70240 0.32391 0.51942 0.01840  0.07208  0.07656  84  LYS A O   
552  C CB  . LYS A 77  ? 0.71868 0.39405 0.56870 -0.00114 0.08613  0.09725  84  LYS A CB  
553  C CG  . LYS A 77  ? 0.84659 0.55399 0.68950 0.01383  0.08647  0.10437  84  LYS A CG  
554  C CD  . LYS A 77  ? 0.92126 0.62143 0.76341 0.01484  0.10688  0.12669  84  LYS A CD  
555  C CE  . LYS A 77  ? 1.04005 0.77060 0.87099 0.03225  0.10767  0.13281  84  LYS A CE  
556  N NZ  . LYS A 77  ? 1.04041 0.79177 0.89497 0.01747  0.11777  0.14147  84  LYS A NZ  
557  N N   . GLN A 78  ? 0.85973 0.48838 0.72070 -0.02769 0.07011  0.06362  85  GLN A N   
558  C CA  . GLN A 78  ? 0.99577 0.58172 0.84955 -0.03117 0.07402  0.05875  85  GLN A CA  
559  C C   . GLN A 78  ? 0.92394 0.50941 0.76193 -0.01675 0.06047  0.04394  85  GLN A C   
560  O O   . GLN A 78  ? 0.87353 0.42669 0.69179 -0.00176 0.06530  0.04655  85  GLN A O   
561  C CB  . GLN A 78  ? 0.97343 0.55070 0.85340 -0.06229 0.07456  0.04861  85  GLN A CB  
562  C CG  . GLN A 78  ? 1.13979 0.70101 1.03673 -0.07873 0.09277  0.06359  85  GLN A CG  
563  C CD  . GLN A 78  ? 1.32868 0.92778 1.23867 -0.07965 0.09655  0.07619  85  GLN A CD  
564  O OE1 . GLN A 78  ? 1.31459 0.95544 1.23488 -0.08195 0.08303  0.06738  85  GLN A OE1 
565  N NE2 . GLN A 78  ? 1.23011 0.81359 1.13904 -0.07679 0.11640  0.09774  85  GLN A NE2 
566  N N   . ASP A 79  ? 0.74919 0.36989 0.59630 -0.02049 0.04480  0.02927  86  ASP A N   
567  C CA  . ASP A 79  ? 0.79006 0.41669 0.62554 -0.00716 0.03275  0.01588  86  ASP A CA  
568  C C   . ASP A 79  ? 0.82524 0.47322 0.64658 0.01775  0.02885  0.02086  86  ASP A C   
569  O O   . ASP A 79  ? 0.77305 0.42561 0.58529 0.03119  0.02068  0.01162  86  ASP A O   
570  C CB  . ASP A 79  ? 0.71702 0.37115 0.56897 -0.02245 0.01921  -0.00129 86  ASP A CB  
571  C CG  . ASP A 79  ? 0.97924 0.61930 0.84626 -0.04772 0.01979  -0.00974 86  ASP A CG  
572  O OD1 . ASP A 79  ? 0.90268 0.50421 0.76586 -0.05320 0.02983  -0.00669 86  ASP A OD1 
573  O OD2 . ASP A 79  ? 0.94074 0.60862 0.82376 -0.06185 0.01023  -0.01980 86  ASP A OD2 
574  N N   . ARG A 80  ? 0.65950 0.32218 0.47969 0.02397  0.03444  0.03412  87  ARG A N   
575  C CA  . ARG A 80  ? 0.66311 0.35134 0.47197 0.04541  0.02906  0.03594  87  ARG A CA  
576  C C   . ARG A 80  ? 0.66088 0.38292 0.48154 0.04284  0.01440  0.01960  87  ARG A C   
577  O O   . ARG A 80  ? 0.57207 0.30518 0.38511 0.05828  0.00657  0.01217  87  ARG A O   
578  C CB  . ARG A 80  ? 0.78167 0.45079 0.56585 0.07067  0.03149  0.04142  87  ARG A CB  
579  C CG  . ARG A 80  ? 0.87931 0.56857 0.64842 0.09307  0.03105  0.04961  87  ARG A CG  
580  C CD  . ARG A 80  ? 0.85579 0.54617 0.60700 0.11840  0.02445  0.04590  87  ARG A CD  
581  N NE  . ARG A 80  ? 0.89935 0.55201 0.63052 0.13225  0.03560  0.05922  87  ARG A NE  
582  C CZ  . ARG A 80  ? 1.00811 0.65078 0.72618 0.15082  0.03222  0.05628  87  ARG A CZ  
583  N NH1 . ARG A 80  ? 0.90388 0.57293 0.62855 0.15667  0.01801  0.04005  87  ARG A NH1 
584  N NH2 . ARG A 80  ? 0.86258 0.46768 0.56162 0.16424  0.04457  0.07068  87  ARG A NH2 
585  N N   . THR A 81  ? 0.63769 0.37706 0.47843 0.02341  0.01139  0.01457  88  THR A N   
586  C CA  . THR A 81  ? 0.63400 0.40296 0.48638 0.02046  0.00005  0.00159  88  THR A CA  
587  C C   . THR A 81  ? 0.59527 0.39217 0.46093 0.01448  0.00045  0.00537  88  THR A C   
588  O O   . THR A 81  ? 0.54357 0.33903 0.41705 0.00393  0.00799  0.01485  88  THR A O   
589  C CB  . THR A 81  ? 0.53644 0.30161 0.39896 0.00494  -0.00563 -0.01032 88  THR A CB  
590  O OG1 . THR A 81  ? 0.60862 0.37120 0.48490 -0.01500 -0.00178 -0.00705 88  THR A OG1 
591  C CG2 . THR A 81  ? 0.61087 0.34660 0.45966 0.01118  -0.00534 -0.01551 88  THR A CG2 
592  N N   . LEU A 82  ? 0.52541 0.34742 0.39487 0.02147  -0.00680 -0.00222 89  LEU A N   
593  C CA  . LEU A 82  ? 0.51078 0.35923 0.39454 0.01561  -0.00753 -0.00189 89  LEU A CA  
594  C C   . LEU A 82  ? 0.49315 0.35620 0.38955 0.00842  -0.01555 -0.01348 89  LEU A C   
595  O O   . LEU A 82  ? 0.49791 0.36384 0.39109 0.01666  -0.02102 -0.02252 89  LEU A O   
596  C CB  . LEU A 82  ? 0.46495 0.32790 0.34120 0.03119  -0.00698 -0.00025 89  LEU A CB  
597  C CG  . LEU A 82  ? 0.46175 0.34976 0.35186 0.02716  -0.00692 -0.00110 89  LEU A CG  
598  C CD1 . LEU A 82  ? 0.44271 0.33329 0.34285 0.01515  0.00102  0.01031  89  LEU A CD1 
599  C CD2 . LEU A 82  ? 0.41507 0.31389 0.29513 0.04329  -0.00722 -0.00297 89  LEU A CD2 
600  N N   . THR A 83  ? 0.43770 0.31096 0.34871 -0.00624 -0.01571 -0.01257 90  THR A N   
601  C CA  . THR A 83  ? 0.44164 0.32895 0.36274 -0.01232 -0.02215 -0.02111 90  THR A CA  
602  C C   . THR A 83  ? 0.50966 0.42258 0.44331 -0.01193 -0.02146 -0.01869 90  THR A C   
603  O O   . THR A 83  ? 0.44195 0.36388 0.38323 -0.01667 -0.01683 -0.01028 90  THR A O   
604  C CB  . THR A 83  ? 0.41262 0.29382 0.33937 -0.02782 -0.02431 -0.02327 90  THR A CB  
605  O OG1 . THR A 83  ? 0.48693 0.33994 0.40105 -0.02749 -0.02389 -0.02667 90  THR A OG1 
606  C CG2 . THR A 83  ? 0.45612 0.35394 0.38991 -0.03153 -0.03079 -0.03079 90  THR A CG2 
607  N N   . ILE A 84  ? 0.42208 0.34584 0.35876 -0.00587 -0.02466 -0.02553 91  ILE A N   
608  C CA  . ILE A 84  ? 0.42518 0.36971 0.37421 -0.00546 -0.02322 -0.02398 91  ILE A CA  
609  C C   . ILE A 84  ? 0.46627 0.41981 0.42267 -0.01192 -0.02683 -0.02688 91  ILE A C   
610  O O   . ILE A 84  ? 0.39955 0.34868 0.35234 -0.00903 -0.02958 -0.03396 91  ILE A O   
611  C CB  . ILE A 84  ? 0.36181 0.31101 0.31046 0.00603  -0.02229 -0.02930 91  ILE A CB  
612  C CG1 . ILE A 84  ? 0.55680 0.50162 0.49591 0.01433  -0.01943 -0.02652 91  ILE A CG1 
613  C CG2 . ILE A 84  ? 0.34169 0.30747 0.30349 0.00606  -0.01932 -0.02803 91  ILE A CG2 
614  C CD1 . ILE A 84  ? 0.60864 0.54013 0.53394 0.02286  -0.02258 -0.03139 91  ILE A CD1 
615  N N   . VAL A 85  ? 0.33302 0.30150 0.29961 -0.01923 -0.02651 -0.02099 92  VAL A N   
616  C CA  . VAL A 85  ? 0.32007 0.30078 0.29174 -0.02391 -0.03066 -0.02253 92  VAL A CA  
617  C C   . VAL A 85  ? 0.49717 0.49749 0.47957 -0.01862 -0.02697 -0.01694 92  VAL A C   
618  O O   . VAL A 85  ? 0.33982 0.35043 0.33025 -0.01821 -0.02285 -0.00978 92  VAL A O   
619  C CB  . VAL A 85  ? 0.33567 0.32112 0.31152 -0.03674 -0.03496 -0.02138 92  VAL A CB  
620  C CG1 . VAL A 85  ? 0.32953 0.32940 0.30662 -0.03925 -0.04122 -0.02504 92  VAL A CG1 
621  C CG2 . VAL A 85  ? 0.55952 0.52092 0.52584 -0.04251 -0.03610 -0.02577 92  VAL A CG2 
622  N N   . ASP A 86  ? 0.32969 0.33454 0.31204 -0.01386 -0.02713 -0.01916 93  ASP A N   
623  C CA  . ASP A 86  ? 0.35169 0.37332 0.34346 -0.00843 -0.02279 -0.01233 93  ASP A CA  
624  C C   . ASP A 86  ? 0.37412 0.40734 0.36374 -0.00893 -0.02689 -0.01136 93  ASP A C   
625  O O   . ASP A 86  ? 0.43553 0.46120 0.41521 -0.01198 -0.03212 -0.01816 93  ASP A O   
626  C CB  . ASP A 86  ? 0.37452 0.38929 0.36940 0.00073  -0.01526 -0.01401 93  ASP A CB  
627  C CG  . ASP A 86  ? 0.37136 0.37546 0.36135 0.00331  -0.01517 -0.02131 93  ASP A CG  
628  O OD1 . ASP A 86  ? 0.48750 0.49719 0.47688 0.00547  -0.01401 -0.01883 93  ASP A OD1 
629  O OD2 . ASP A 86  ? 0.46368 0.45548 0.45042 0.00439  -0.01578 -0.02901 93  ASP A OD2 
630  N N   . THR A 87  ? 0.36117 0.41353 0.35863 -0.00444 -0.02445 -0.00266 94  THR A N   
631  C CA  . THR A 87  ? 0.34340 0.40970 0.33690 -0.00079 -0.02738 0.00013  94  THR A CA  
632  C C   . THR A 87  ? 0.31645 0.37961 0.31058 0.01118  -0.01741 0.00568  94  THR A C   
633  O O   . THR A 87  ? 0.38902 0.46751 0.38422 0.01900  -0.01494 0.01470  94  THR A O   
634  C CB  . THR A 87  ? 0.30916 0.40287 0.31069 -0.00309 -0.03270 0.00674  94  THR A CB  
635  O OG1 . THR A 87  ? 0.29279 0.39470 0.30728 0.00106  -0.02565 0.01552  94  THR A OG1 
636  C CG2 . THR A 87  ? 0.37133 0.46754 0.37324 -0.01758 -0.04292 -0.00084 94  THR A CG2 
637  N N   . GLY A 88  ? 0.35837 0.40196 0.35266 0.01296  -0.01116 0.00045  95  GLY A N   
638  C CA  . GLY A 88  ? 0.34818 0.38576 0.34624 0.02182  -0.00023 0.00429  95  GLY A CA  
639  C C   . GLY A 88  ? 0.38094 0.41918 0.36918 0.02603  0.00065  0.00529  95  GLY A C   
640  O O   . GLY A 88  ? 0.37227 0.42139 0.34959 0.02441  -0.00804 0.00483  95  GLY A O   
641  N N   . ILE A 89  ? 0.36171 0.38867 0.35406 0.03118  0.01147  0.00584  96  ILE A N   
642  C CA  . ILE A 89  ? 0.33046 0.35844 0.31360 0.03748  0.01590  0.00967  96  ILE A CA  
643  C C   . ILE A 89  ? 0.38654 0.40910 0.35719 0.03310  0.00837  -0.00108 96  ILE A C   
644  O O   . ILE A 89  ? 0.39392 0.42115 0.35129 0.03836  0.00854  0.00115  96  ILE A O   
645  C CB  . ILE A 89  ? 0.36888 0.38559 0.36387 0.04330  0.03242  0.01448  96  ILE A CB  
646  C CG1 . ILE A 89  ? 0.48876 0.50847 0.47344 0.05259  0.04032  0.02342  96  ILE A CG1 
647  C CG2 . ILE A 89  ? 0.37385 0.37672 0.37929 0.03651  0.03362  0.00166  96  ILE A CG2 
648  C CD1 . ILE A 89  ? 0.60381 0.61541 0.60003 0.06079  0.05951  0.03533  96  ILE A CD1 
649  N N   . GLY A 90  ? 0.33649 0.34892 0.30928 0.02541  0.00243  -0.01228 97  GLY A N   
650  C CA  . GLY A 90  ? 0.34472 0.34953 0.30573 0.02293  -0.00342 -0.02209 97  GLY A CA  
651  C C   . GLY A 90  ? 0.40229 0.39951 0.36777 0.02772  0.00642  -0.02431 97  GLY A C   
652  O O   . GLY A 90  ? 0.41616 0.41306 0.39525 0.03143  0.01815  -0.01865 97  GLY A O   
653  N N   . MET A 91  ? 0.38241 0.37285 0.33787 0.02745  0.00253  -0.03296 98  MET A N   
654  C CA  . MET A 91  ? 0.36051 0.34679 0.32151 0.03216  0.01184  -0.03547 98  MET A CA  
655  C C   . MET A 91  ? 0.45830 0.44439 0.39989 0.03757  0.01134  -0.03717 98  MET A C   
656  O O   . MET A 91  ? 0.42314 0.40598 0.34750 0.03523  0.00055  -0.04349 98  MET A O   
657  C CB  . MET A 91  ? 0.35045 0.32956 0.32253 0.02908  0.00966  -0.04575 98  MET A CB  
658  C CG  . MET A 91  ? 0.40548 0.38476 0.39297 0.02458  0.00846  -0.04666 98  MET A CG  
659  S SD  . MET A 91  ? 0.48493 0.45890 0.47802 0.02339  0.00190  -0.05926 98  MET A SD  
660  C CE  . MET A 91  ? 0.40239 0.36847 0.37598 0.01972  -0.01065 -0.05999 98  MET A CE  
661  N N   . THR A 92  ? 0.40438 0.39310 0.34912 0.04478  0.02414  -0.03174 99  THR A N   
662  C CA  . THR A 92  ? 0.47330 0.46190 0.39962 0.05219  0.02650  -0.03334 99  THR A CA  
663  C C   . THR A 92  ? 0.44206 0.42239 0.37019 0.05201  0.02503  -0.04497 99  THR A C   
664  O O   . THR A 92  ? 0.49435 0.47131 0.43941 0.04714  0.02297  -0.05075 99  THR A O   
665  C CB  . THR A 92  ? 0.51554 0.50997 0.44547 0.06119  0.04356  -0.02109 99  THR A CB  
666  O OG1 . THR A 92  ? 0.49780 0.48970 0.45432 0.05921  0.05541  -0.02178 99  THR A OG1 
667  C CG2 . THR A 92  ? 0.43014 0.43176 0.36078 0.06357  0.04696  -0.00766 99  THR A CG2 
668  N N   . LYS A 93  ? 0.47834 0.45653 0.38747 0.05914  0.02616  -0.04846 100 LYS A N   
669  C CA  . LYS A 93  ? 0.50259 0.47411 0.41308 0.06215  0.02715  -0.05799 100 LYS A CA  
670  C C   . LYS A 93  ? 0.55064 0.52921 0.48949 0.06358  0.04034  -0.05527 100 LYS A C   
671  O O   . LYS A 93  ? 0.40031 0.37786 0.35350 0.06179  0.03765  -0.06322 100 LYS A O   
672  C CB  . LYS A 93  ? 0.47266 0.44085 0.35657 0.07143  0.02837  -0.06164 100 LYS A CB  
673  C CG  . LYS A 93  ? 0.50007 0.45828 0.38030 0.07545  0.02677  -0.07286 100 LYS A CG  
674  C CD  . LYS A 93  ? 0.67895 0.63277 0.53170 0.08595  0.02950  -0.07717 100 LYS A CD  
675  C CE  . LYS A 93  ? 0.60111 0.54083 0.44616 0.09039  0.02607  -0.08928 100 LYS A CE  
676  N NZ  . LYS A 93  ? 0.82084 0.75853 0.64378 0.10360  0.03380  -0.09266 100 LYS A NZ  
677  N N   . ALA A 94  ? 0.44407 0.43057 0.39220 0.06701  0.05501  -0.04402 101 ALA A N   
678  C CA  . ALA A 94  ? 0.44103 0.43435 0.42081 0.06580  0.06897  -0.04182 101 ALA A CA  
679  C C   . ALA A 94  ? 0.47102 0.46490 0.47583 0.05567  0.06336  -0.04704 101 ALA A C   
680  O O   . ALA A 94  ? 0.51049 0.51033 0.53950 0.05312  0.06586  -0.05433 101 ALA A O   
681  C CB  . ALA A 94  ? 0.48692 0.48463 0.47162 0.07054  0.08731  -0.02674 101 ALA A CB  
682  N N   . ASP A 95  ? 0.46255 0.45248 0.46209 0.05057  0.05562  -0.04401 102 ASP A N   
683  C CA  . ASP A 95  ? 0.43882 0.42839 0.45670 0.04246  0.04913  -0.05004 102 ASP A CA  
684  C C   . ASP A 95  ? 0.52842 0.51673 0.54482 0.04172  0.03686  -0.06288 102 ASP A C   
685  O O   . ASP A 95  ? 0.45155 0.44575 0.48956 0.03909  0.03635  -0.07062 102 ASP A O   
686  C CB  . ASP A 95  ? 0.42304 0.40903 0.43071 0.03901  0.04213  -0.04444 102 ASP A CB  
687  C CG  . ASP A 95  ? 0.59078 0.57827 0.60546 0.04058  0.05469  -0.03139 102 ASP A CG  
688  O OD1 . ASP A 95  ? 0.48852 0.47690 0.52420 0.04072  0.06943  -0.02828 102 ASP A OD1 
689  O OD2 . ASP A 95  ? 0.49019 0.47825 0.49055 0.04180  0.05020  -0.02398 102 ASP A OD2 
690  N N   . LEU A 96  ? 0.54749 0.52790 0.53811 0.04443  0.02671  -0.06558 103 LEU A N   
691  C CA  . LEU A 96  ? 0.43817 0.41319 0.42363 0.04534  0.01594  -0.07539 103 LEU A CA  
692  C C   . LEU A 96  ? 0.47895 0.46136 0.47770 0.05146  0.02059  -0.08196 103 LEU A C   
693  O O   . LEU A 96  ? 0.46481 0.45093 0.47377 0.05239  0.01462  -0.08944 103 LEU A O   
694  C CB  . LEU A 96  ? 0.45845 0.42011 0.41467 0.04667  0.00717  -0.07686 103 LEU A CB  
695  C CG  . LEU A 96  ? 0.34608 0.30265 0.29089 0.03954  -0.00061 -0.07283 103 LEU A CG  
696  C CD1 . LEU A 96  ? 0.38254 0.32614 0.30194 0.03931  -0.00859 -0.07706 103 LEU A CD1 
697  C CD2 . LEU A 96  ? 0.36709 0.32313 0.32295 0.03444  -0.00631 -0.07404 103 LEU A CD2 
698  N N   . ILE A 97  ? 0.39184 0.37840 0.38999 0.05703  0.03130  -0.07891 104 ILE A N   
699  C CA  . ILE A 97  ? 0.41216 0.40751 0.42200 0.06418  0.03657  -0.08453 104 ILE A CA  
700  C C   . ILE A 97  ? 0.52688 0.54003 0.57351 0.06051  0.04743  -0.08470 104 ILE A C   
701  O O   . ILE A 97  ? 0.51036 0.53599 0.57755 0.06163  0.04492  -0.09334 104 ILE A O   
702  C CB  . ILE A 97  ? 0.40778 0.39827 0.39626 0.07325  0.04341  -0.08178 104 ILE A CB  
703  C CG1 . ILE A 97  ? 0.49738 0.46916 0.45260 0.07597  0.03132  -0.08634 104 ILE A CG1 
704  C CG2 . ILE A 97  ? 0.57149 0.57477 0.57627 0.08143  0.05281  -0.08534 104 ILE A CG2 
705  C CD1 . ILE A 97  ? 0.48274 0.44744 0.41123 0.08394  0.03609  -0.08533 104 ILE A CD1 
706  N N   . ASN A 98  ? 0.52495 0.53998 0.58165 0.05621  0.05979  -0.07551 105 ASN A N   
707  C CA  . ASN A 98  ? 0.43826 0.46725 0.53105 0.05214  0.07422  -0.07481 105 ASN A CA  
708  C C   . ASN A 98  ? 0.44201 0.47115 0.55673 0.04136  0.07453  -0.07576 105 ASN A C   
709  O O   . ASN A 98  ? 0.39536 0.43633 0.53886 0.03583  0.07261  -0.08629 105 ASN A O   
710  C CB  . ASN A 98  ? 0.48952 0.51861 0.57970 0.05702  0.09311  -0.06213 105 ASN A CB  
711  C CG  . ASN A 98  ? 0.67188 0.70398 0.74617 0.06857  0.09635  -0.06287 105 ASN A CG  
712  O OD1 . ASN A 98  ? 0.86021 0.90351 0.94854 0.07165  0.09423  -0.07203 105 ASN A OD1 
713  N ND2 . ASN A 98  ? 0.73282 0.75624 0.77705 0.07636  0.10150  -0.05358 105 ASN A ND2 
714  N N   . ASN A 99  ? 0.59559 0.59146 0.45402 0.12057  0.04953  0.04518  106 ASN A N   
715  C CA  . ASN A 99  ? 0.58164 0.59840 0.48110 0.11934  0.04638  0.06328  106 ASN A CA  
716  C C   . ASN A 99  ? 0.65213 0.67363 0.60070 0.10240  0.03883  0.05632  106 ASN A C   
717  O O   . ASN A 99  ? 0.83610 0.86153 0.82426 0.10045  0.04882  0.06796  106 ASN A O   
718  C CB  . ASN A 99  ? 0.53942 0.57379 0.41894 0.12224  0.02795  0.06702  106 ASN A CB  
719  C CG  . ASN A 99  ? 0.69097 0.72349 0.51193 0.14021  0.03200  0.07453  106 ASN A CG  
720  O OD1 . ASN A 99  ? 0.64263 0.66205 0.44716 0.15542  0.05678  0.08721  106 ASN A OD1 
721  N ND2 . ASN A 99  ? 0.66954 0.71717 0.45915 0.13928  0.00744  0.06856  106 ASN A ND2 
722  N N   . LEU A 100 ? 0.56573 0.58625 0.51155 0.08976  0.02140  0.03693  107 LEU A N   
723  C CA  . LEU A 100 ? 0.49207 0.51664 0.47654 0.07624  0.01507  0.03188  107 LEU A CA  
724  C C   . LEU A 100 ? 0.43579 0.45349 0.44205 0.07356  0.02691  0.03342  107 LEU A C   
725  O O   . LEU A 100 ? 0.46108 0.48450 0.49885 0.06628  0.02640  0.03688  107 LEU A O   
726  C CB  . LEU A 100 ? 0.45442 0.47788 0.43355 0.06547  -0.00164 0.01358  107 LEU A CB  
727  C CG  . LEU A 100 ? 0.74081 0.78089 0.73235 0.06148  -0.01698 0.01613  107 LEU A CG  
728  C CD1 . LEU A 100 ? 0.54727 0.60102 0.51876 0.07282  -0.02097 0.02947  107 LEU A CD1 
729  C CD2 . LEU A 100 ? 0.68662 0.72610 0.67847 0.05043  -0.03237 -0.00138 107 LEU A CD2 
730  N N   . GLY A 101 ? 0.47108 0.47676 0.46063 0.07971  0.03786  0.03138  108 GLY A N   
731  C CA  . GLY A 101 ? 0.41868 0.42368 0.43470 0.07866  0.04810  0.03741  108 GLY A CA  
732  C C   . GLY A 101 ? 0.54468 0.55938 0.58928 0.08337  0.05956  0.05659  108 GLY A C   
733  O O   . GLY A 101 ? 0.44273 0.46710 0.52281 0.07641  0.05858  0.06185  108 GLY A O   
734  N N   . THR A 102 ? 0.42534 0.43863 0.45599 0.09519  0.07028  0.06801  109 THR A N   
735  C CA  . THR A 102 ? 0.44957 0.47125 0.51522 0.09937  0.08371  0.08790  109 THR A CA  
736  C C   . THR A 102 ? 0.59656 0.62862 0.69726 0.08566  0.07260  0.08632  109 THR A C   
737  O O   . THR A 102 ? 0.46110 0.50047 0.60374 0.07831  0.07566  0.09269  109 THR A O   
738  C CB  . THR A 102 ? 0.50424 0.52139 0.54438 0.11720  0.09940  0.10284  109 THR A CB  
739  O OG1 . THR A 102 ? 0.56231 0.56417 0.56449 0.13049  0.11351  0.10239  109 THR A OG1 
740  C CG2 . THR A 102 ? 0.51215 0.53683 0.59696 0.12169  0.11675  0.12572  109 THR A CG2 
741  N N   . ILE A 103 ? 0.42858 0.46073 0.51428 0.08130  0.05986  0.07704  110 ILE A N   
742  C CA  . ILE A 103 ? 0.52698 0.56251 0.64132 0.06940  0.05355  0.07369  110 ILE A CA  
743  C C   . ILE A 103 ? 0.54739 0.58335 0.67396 0.05462  0.04194  0.05937  110 ILE A C   
744  O O   . ILE A 103 ? 0.61582 0.65408 0.77153 0.04414  0.04090  0.05802  110 ILE A O   
745  C CB  . ILE A 103 ? 0.43575 0.47238 0.53490 0.07136  0.04625  0.07170  110 ILE A CB  
746  C CG1 . ILE A 103 ? 0.59142 0.63245 0.68584 0.08676  0.05820  0.09173  110 ILE A CG1 
747  C CG2 . ILE A 103 ? 0.60621 0.64003 0.72974 0.05914  0.04234  0.06445  110 ILE A CG2 
748  C CD1 . ILE A 103 ? 0.73695 0.78625 0.80914 0.09241  0.04733  0.09341  110 ILE A CD1 
749  N N   . ALA A 104 ? 0.42659 0.46000 0.53046 0.05363  0.03336  0.04863  111 ALA A N   
750  C CA  . ALA A 104 ? 0.39703 0.43219 0.50829 0.04323  0.02404  0.03923  111 ALA A CA  
751  C C   . ALA A 104 ? 0.62005 0.66539 0.75779 0.04001  0.02566  0.04692  111 ALA A C   
752  O O   . ALA A 104 ? 0.47342 0.52503 0.61933 0.03053  0.01520  0.04142  111 ALA A O   
753  C CB  . ALA A 104 ? 0.48284 0.51228 0.57094 0.04557  0.02016  0.03083  111 ALA A CB  
754  N N   . LYS A 105 ? 0.42933 0.47834 0.58153 0.04833  0.03842  0.06126  112 LYS A N   
755  C CA  . LYS A 105 ? 0.47642 0.53986 0.66400 0.04552  0.03990  0.07216  112 LYS A CA  
756  C C   . LYS A 105 ? 0.35326 0.42615 0.57329 0.02922  0.02898  0.06792  112 LYS A C   
757  O O   . LYS A 105 ? 0.44912 0.53685 0.68652 0.01923  0.01540  0.06613  112 LYS A O   
758  C CB  . LYS A 105 ? 0.45732 0.52036 0.65713 0.05975  0.06091  0.09092  112 LYS A CB  
759  C CG  . LYS A 105 ? 0.52097 0.59822 0.75324 0.06301  0.06699  0.10599  112 LYS A CG  
760  C CD  . LYS A 105 ? 0.60424 0.67663 0.84708 0.07998  0.09396  0.12643  112 LYS A CD  
761  C CE  . LYS A 105 ? 0.80583 0.89978 1.10798 0.07980  0.10074  0.14747  112 LYS A CE  
762  N NZ  . LYS A 105 ? 0.74336 0.85162 1.09878 0.06905  0.09925  0.15583  112 LYS A NZ  
763  N N   . SER A 106 ? 0.42323 0.48737 0.65110 0.02613  0.03451  0.06595  113 SER A N   
764  C CA  . SER A 106 ? 0.46257 0.52914 0.72150 0.00885  0.02692  0.05802  113 SER A CA  
765  C C   . SER A 106 ? 0.39257 0.45172 0.62624 -0.00342 0.01069  0.03674  113 SER A C   
766  O O   . SER A 106 ? 0.50632 0.57130 0.75290 -0.01935 -0.00328 0.02592  113 SER A O   
767  C CB  . SER A 106 ? 0.45417 0.50961 0.73434 0.01116  0.04402  0.06489  113 SER A CB  
768  O OG  . SER A 106 ? 0.63716 0.67734 0.88727 0.01705  0.04821  0.05947  113 SER A OG  
769  N N   . GLY A 107 ? 0.42633 0.47303 0.62388 0.00369  0.01226  0.03068  114 GLY A N   
770  C CA  . GLY A 107 ? 0.49313 0.53038 0.66705 -0.00479 0.00240  0.01374  114 GLY A CA  
771  C C   . GLY A 107 ? 0.46845 0.51823 0.62923 -0.00775 -0.01224 0.01091  114 GLY A C   
772  O O   . GLY A 107 ? 0.32645 0.37415 0.47432 -0.01811 -0.02334 -0.00167 114 GLY A O   
773  N N   . THR A 108 ? 0.42613 0.48765 0.58792 0.00264  -0.01051 0.02355  115 THR A N   
774  C CA  . THR A 108 ? 0.41101 0.48776 0.56887 0.00282  -0.02115 0.02750  115 THR A CA  
775  C C   . THR A 108 ? 0.38830 0.48618 0.57310 -0.00957 -0.03624 0.02923  115 THR A C   
776  O O   . THR A 108 ? 0.43145 0.53948 0.60335 -0.01648 -0.05247 0.02393  115 THR A O   
777  C CB  . THR A 108 ? 0.42541 0.50639 0.58623 0.01729  -0.01036 0.04205  115 THR A CB  
778  O OG1 . THR A 108 ? 0.51974 0.58239 0.65302 0.02496  -0.00209 0.03583  115 THR A OG1 
779  C CG2 . THR A 108 ? 0.44734 0.54659 0.61484 0.01956  -0.01769 0.05210  115 THR A CG2 
780  N N   . LYS A 109 ? 0.32009 0.42644 0.54351 -0.01242 -0.03160 0.03770  116 LYS A N   
781  C CA  . LYS A 109 ? 0.33582 0.46529 0.59622 -0.02719 -0.04781 0.03913  116 LYS A CA  
782  C C   . LYS A 109 ? 0.42746 0.54703 0.67279 -0.04642 -0.06327 0.01472  116 LYS A C   
783  O O   . LYS A 109 ? 0.42772 0.56548 0.67157 -0.05883 -0.08644 0.00819  116 LYS A O   
784  C CB  . LYS A 109 ? 0.41054 0.54618 0.72115 -0.02610 -0.03427 0.05354  116 LYS A CB  
785  C CG  . LYS A 109 ? 0.47441 0.62890 0.83446 -0.04641 -0.04945 0.05059  116 LYS A CG  
786  C CD  . LYS A 109 ? 0.63440 0.80360 1.05430 -0.04036 -0.03352 0.07494  116 LYS A CD  
787  C CE  . LYS A 109 ? 0.70536 0.90586 1.18784 -0.06057 -0.05337 0.07788  116 LYS A CE  
788  N NZ  . LYS A 109 ? 0.69163 0.87980 1.18077 -0.08592 -0.06737 0.05048  116 LYS A NZ  
789  N N   . ALA A 110 ? 0.40755 0.49770 0.63901 -0.04828 -0.05012 0.00135  117 ALA A N   
790  C CA  . ALA A 110 ? 0.33986 0.41197 0.55415 -0.06532 -0.05834 -0.02369 117 ALA A CA  
791  C C   . ALA A 110 ? 0.36300 0.42917 0.52372 -0.06399 -0.06878 -0.03509 117 ALA A C   
792  O O   . ALA A 110 ? 0.37043 0.43456 0.51111 -0.07883 -0.08539 -0.05351 117 ALA A O   
793  C CB  . ALA A 110 ? 0.32830 0.36939 0.54599 -0.06383 -0.03593 -0.03007 117 ALA A CB  
794  N N   . PHE A 111 ? 0.34511 0.40722 0.48114 -0.04655 -0.05862 -0.02490 118 PHE A N   
795  C CA  . PHE A 111 ? 0.40714 0.46346 0.49767 -0.04278 -0.06397 -0.03124 118 PHE A CA  
796  C C   . PHE A 111 ? 0.38779 0.47373 0.47305 -0.04662 -0.08709 -0.02568 118 PHE A C   
797  O O   . PHE A 111 ? 0.40325 0.48645 0.45141 -0.05299 -0.09979 -0.03822 118 PHE A O   
798  C CB  . PHE A 111 ? 0.37122 0.41939 0.44893 -0.02486 -0.04798 -0.01993 118 PHE A CB  
799  C CG  . PHE A 111 ? 0.49445 0.53468 0.53279 -0.01873 -0.04757 -0.02257 118 PHE A CG  
800  C CD1 . PHE A 111 ? 0.52012 0.54109 0.52508 -0.02569 -0.04827 -0.03967 118 PHE A CD1 
801  C CD2 . PHE A 111 ? 0.36667 0.41509 0.40157 -0.00508 -0.04273 -0.00762 118 PHE A CD2 
802  C CE1 . PHE A 111 ? 0.53034 0.54248 0.49764 -0.01726 -0.04368 -0.03903 118 PHE A CE1 
803  C CE2 . PHE A 111 ? 0.44355 0.48404 0.44780 0.00209  -0.03842 -0.00665 118 PHE A CE2 
804  C CZ  . PHE A 111 ? 0.42870 0.45213 0.39827 -0.00301 -0.03866 -0.02093 118 PHE A CZ  
805  N N   . MET A 112 ? 0.36500 0.48024 0.48662 -0.04205 -0.09232 -0.00554 119 MET A N   
806  C CA  . MET A 112 ? 0.38995 0.53913 0.51288 -0.04300 -0.11407 0.00585  119 MET A CA  
807  C C   . MET A 112 ? 0.32849 0.49477 0.46342 -0.06533 -0.14091 -0.00799 119 MET A C   
808  O O   . MET A 112 ? 0.37189 0.56047 0.48549 -0.07030 -0.16500 -0.00845 119 MET A O   
809  C CB  . MET A 112 ? 0.52947 0.70369 0.69273 -0.02958 -0.10750 0.03423  119 MET A CB  
810  C CG  . MET A 112 ? 0.53777 0.69377 0.68463 -0.00985 -0.08376 0.04398  119 MET A CG  
811  S SD  . MET A 112 ? 0.58726 0.77078 0.76206 0.00746  -0.07810 0.07600  119 MET A SD  
812  C CE  . MET A 112 ? 0.52608 0.69583 0.73319 0.01537  -0.05316 0.08306  119 MET A CE  
813  N N   . GLU A 113 ? 0.45047 0.60720 0.61969 -0.07926 -0.13768 -0.01916 120 GLU A N   
814  C CA  . GLU A 113 ? 0.53111 0.69749 0.71285 -0.10466 -0.16271 -0.03874 120 GLU A CA  
815  C C   . GLU A 113 ? 0.58527 0.72236 0.70262 -0.11457 -0.16955 -0.06934 120 GLU A C   
816  O O   . GLU A 113 ? 0.46059 0.61241 0.55734 -0.13083 -0.19879 -0.08436 120 GLU A O   
817  C CB  . GLU A 113 ? 0.53876 0.69520 0.77615 -0.11623 -0.15105 -0.04310 120 GLU A CB  
818  C CG  . GLU A 113 ? 0.53597 0.73167 0.84517 -0.11814 -0.15795 -0.01887 120 GLU A CG  
819  C CD  . GLU A 113 ? 0.78531 0.96582 1.14456 -0.11520 -0.13046 -0.01031 120 GLU A CD  
820  O OE1 . GLU A 113 ? 0.84694 0.99644 1.20743 -0.12682 -0.12019 -0.03064 120 GLU A OE1 
821  O OE2 . GLU A 113 ? 0.77769 0.97543 1.17367 -0.09956 -0.11629 0.01819  120 GLU A OE2 
822  N N   . ALA A 114 ? 0.40607 0.50219 0.49001 -0.10428 -0.14267 -0.07809 121 ALA A N   
823  C CA  . ALA A 114 ? 0.49445 0.55741 0.51584 -0.10945 -0.14129 -0.10426 121 ALA A CA  
824  C C   . ALA A 114 ? 0.69170 0.77090 0.66000 -0.10014 -0.15668 -0.09808 121 ALA A C   
825  O O   . ALA A 114 ? 0.64913 0.72079 0.56813 -0.11140 -0.17337 -0.11956 121 ALA A O   
826  C CB  . ALA A 114 ? 0.53701 0.55866 0.54585 -0.09681 -0.10651 -0.10689 121 ALA A CB  
827  N N   . LEU A 115 ? 0.52804 0.62769 0.50358 -0.07900 -0.14978 -0.06881 122 LEU A N   
828  C CA  . LEU A 115 ? 0.51419 0.63034 0.44584 -0.06662 -0.15979 -0.05667 122 LEU A CA  
829  C C   . LEU A 115 ? 0.64755 0.80428 0.57548 -0.07974 -0.19836 -0.05660 122 LEU A C   
830  O O   . LEU A 115 ? 0.62189 0.78655 0.49524 -0.07524 -0.21211 -0.05671 122 LEU A O   
831  C CB  . LEU A 115 ? 0.42079 0.55107 0.37472 -0.04332 -0.14323 -0.02458 122 LEU A CB  
832  C CG  . LEU A 115 ? 0.52020 0.61396 0.46768 -0.02999 -0.11001 -0.02491 122 LEU A CG  
833  C CD1 . LEU A 115 ? 0.47874 0.58413 0.45822 -0.01255 -0.09527 0.00105  122 LEU A CD1 
834  C CD2 . LEU A 115 ? 0.56586 0.63206 0.45454 -0.02281 -0.09879 -0.03428 122 LEU A CD2 
835  N N   . GLN A 116 ? 0.70529 0.89019 0.69175 -0.09544 -0.21652 -0.05460 123 GLN A N   
836  C CA  . GLN A 116 ? 0.71655 0.94329 0.70726 -0.11269 -0.25796 -0.05742 123 GLN A CA  
837  C C   . GLN A 116 ? 0.67919 0.88194 0.62829 -0.13902 -0.27636 -0.09968 123 GLN A C   
838  O O   . GLN A 116 ? 0.73514 0.96512 0.65689 -0.15151 -0.31261 -0.10870 123 GLN A O   
839  C CB  . GLN A 116 ? 0.74592 1.01323 0.82363 -0.12079 -0.26972 -0.03830 123 GLN A CB  
840  C CG  . GLN A 116 ? 0.77708 1.08138 0.88929 -0.09740 -0.26369 0.00449  123 GLN A CG  
841  C CD  . GLN A 116 ? 0.91376 1.27398 1.04393 -0.10020 -0.29852 0.02161  123 GLN A CD  
842  O OE1 . GLN A 116 ? 1.08348 1.45327 1.21296 -0.11909 -0.32361 -0.00182 123 GLN A OE1 
843  N NE2 . GLN A 116 ? 0.94434 1.33062 1.08902 -0.07555 -0.28997 0.05853  123 GLN A NE2 
844  N N   . ALA A 117 ? 0.69221 0.84411 0.63658 -0.14695 -0.25145 -0.12577 124 ALA A N   
845  C CA  . ALA A 117 ? 0.85133 0.97002 0.75513 -0.17157 -0.26180 -0.16889 124 ALA A CA  
846  C C   . ALA A 117 ? 0.84158 0.92388 0.64937 -0.16143 -0.25171 -0.18544 124 ALA A C   
847  O O   . ALA A 117 ? 0.94042 0.98576 0.70168 -0.17889 -0.25451 -0.22351 124 ALA A O   
848  C CB  . ALA A 117 ? 0.71594 0.79410 0.66230 -0.18293 -0.23482 -0.18668 124 ALA A CB  
849  N N   . GLY A 118 ? 0.84635 0.93445 0.62545 -0.13293 -0.23630 -0.15777 125 GLY A N   
850  C CA  . GLY A 118 ? 0.81357 0.86863 0.50686 -0.11902 -0.22147 -0.16663 125 GLY A CA  
851  C C   . GLY A 118 ? 0.73332 0.74548 0.42339 -0.09825 -0.17460 -0.15900 125 GLY A C   
852  O O   . GLY A 118 ? 0.83199 0.81736 0.45892 -0.08301 -0.15658 -0.16031 125 GLY A O   
853  N N   . ALA A 119 ? 0.78445 0.79062 0.54062 -0.09666 -0.15443 -0.14981 126 ALA A N   
854  C CA  . ALA A 119 ? 0.66342 0.63862 0.42513 -0.07738 -0.11519 -0.13880 126 ALA A CA  
855  C C   . ALA A 119 ? 0.81408 0.80748 0.56246 -0.05242 -0.10744 -0.10810 126 ALA A C   
856  O O   . ALA A 119 ? 0.84325 0.87676 0.59327 -0.04797 -0.12947 -0.08956 126 ALA A O   
857  C CB  . ALA A 119 ? 0.56564 0.54229 0.40001 -0.07927 -0.10191 -0.13007 126 ALA A CB  
858  N N   . ASP A 120 ? 0.67972 0.64412 0.42057 -0.03581 -0.07453 -0.10084 127 ASP A N   
859  C CA  . ASP A 120 ? 0.79810 0.77496 0.53441 -0.01322 -0.06283 -0.07259 127 ASP A CA  
860  C C   . ASP A 120 ? 0.65404 0.62660 0.44483 -0.00376 -0.04036 -0.05733 127 ASP A C   
861  O O   . ASP A 120 ? 0.62515 0.58198 0.44651 -0.01134 -0.03088 -0.06735 127 ASP A O   
862  C CB  . ASP A 120 ? 0.76062 0.71027 0.42936 0.00010  -0.04558 -0.07487 127 ASP A CB  
863  C CG  . ASP A 120 ? 0.95552 0.86157 0.62467 0.00705  -0.00919 -0.08127 127 ASP A CG  
864  O OD1 . ASP A 120 ? 1.03799 0.91435 0.70020 -0.00578 -0.00267 -0.10617 127 ASP A OD1 
865  O OD2 . ASP A 120 ? 1.03165 0.93382 0.71424 0.02527  0.01401  -0.05995 127 ASP A OD2 
866  N N   . ILE A 121 ? 0.56922 0.55628 0.37103 0.01319  -0.03206 -0.03238 128 ILE A N   
867  C CA  . ILE A 121 ? 0.56109 0.55213 0.41509 0.01987  -0.01873 -0.01827 128 ILE A CA  
868  C C   . ILE A 121 ? 0.52628 0.48633 0.39060 0.02183  0.00556  -0.02553 128 ILE A C   
869  O O   . ILE A 121 ? 0.48396 0.44571 0.38982 0.01992  0.00989  -0.02339 128 ILE A O   
870  C CB  . ILE A 121 ? 0.57914 0.58738 0.43996 0.03643  -0.01314 0.00740  128 ILE A CB  
871  C CG1 . ILE A 121 ? 0.67267 0.71757 0.55477 0.03421  -0.03503 0.01987  128 ILE A CG1 
872  C CG2 . ILE A 121 ? 0.57916 0.57641 0.47762 0.04481  0.00868  0.01679  128 ILE A CG2 
873  C CD1 . ILE A 121 ? 0.64558 0.71192 0.51050 0.04878  -0.03800 0.04336  128 ILE A CD1 
874  N N   . SER A 122 ? 0.59896 0.53104 0.42516 0.02607  0.02173  -0.03348 129 SER A N   
875  C CA  . SER A 122 ? 0.52644 0.43167 0.36915 0.03005  0.04730  -0.03555 129 SER A CA  
876  C C   . SER A 122 ? 0.61821 0.51463 0.48622 0.01745  0.04594  -0.04981 129 SER A C   
877  O O   . SER A 122 ? 0.57201 0.45616 0.46881 0.02124  0.06373  -0.04588 129 SER A O   
878  C CB  . SER A 122 ? 0.59345 0.46758 0.38802 0.03909  0.06922  -0.03966 129 SER A CB  
879  O OG  . SER A 122 ? 0.71450 0.57139 0.46251 0.02796  0.06110  -0.06337 129 SER A OG  
880  N N   . MET A 123 ? 0.66871 0.57321 0.53201 0.00305  0.02586  -0.06368 130 MET A N   
881  C CA  . MET A 123 ? 0.52083 0.41728 0.41340 -0.00807 0.02692  -0.07431 130 MET A CA  
882  C C   . MET A 123 ? 0.52973 0.45247 0.47238 -0.00818 0.01824  -0.06087 130 MET A C   
883  O O   . MET A 123 ? 0.47424 0.39410 0.44353 -0.01521 0.01955  -0.06510 130 MET A O   
884  C CB  . MET A 123 ? 0.55001 0.43959 0.41878 -0.02525 0.01159  -0.09703 130 MET A CB  
885  C CG  . MET A 123 ? 0.58271 0.43279 0.40020 -0.02733 0.02661  -0.11756 130 MET A CG  
886  S SD  . MET A 123 ? 1.07514 0.92885 0.83203 -0.04172 -0.00172 -0.14002 130 MET A SD  
887  C CE  . MET A 123 ? 0.82289 0.68152 0.61909 -0.06738 -0.02020 -0.15982 130 MET A CE  
888  N N   . ILE A 124 ? 0.49101 0.43569 0.44538 0.00060  0.01279  -0.04457 131 ILE A N   
889  C CA  . ILE A 124 ? 0.40365 0.36966 0.39501 0.00148  0.00564  -0.03381 131 ILE A CA  
890  C C   . ILE A 124 ? 0.42456 0.38320 0.44415 0.00255  0.01650  -0.03197 131 ILE A C   
891  O O   . ILE A 124 ? 0.41597 0.38644 0.45884 0.00045  0.01128  -0.02788 131 ILE A O   
892  C CB  . ILE A 124 ? 0.43592 0.41586 0.43156 0.01191  0.00539  -0.01933 131 ILE A CB  
893  C CG1 . ILE A 124 ? 0.38445 0.38058 0.40962 0.01328  0.00041  -0.01128 131 ILE A CG1 
894  C CG2 . ILE A 124 ? 0.39561 0.36097 0.39077 0.02062  0.02239  -0.01490 131 ILE A CG2 
895  C CD1 . ILE A 124 ? 0.40320 0.40819 0.43361 0.02199  0.00227  0.00004  131 ILE A CD1 
896  N N   . GLY A 125 ? 0.43801 0.37868 0.45735 0.00743  0.03294  -0.03197 132 GLY A N   
897  C CA  . GLY A 125 ? 0.51032 0.44958 0.55960 0.01032  0.04201  -0.02555 132 GLY A CA  
898  C C   . GLY A 125 ? 0.57620 0.50776 0.63718 0.00362  0.04513  -0.03098 132 GLY A C   
899  O O   . GLY A 125 ? 0.48425 0.42462 0.57192 0.00699  0.04729  -0.02099 132 GLY A O   
900  N N   . GLN A 126 ? 0.47529 0.39004 0.51646 -0.00603 0.04557  -0.04679 133 GLN A N   
901  C CA  . GLN A 126 ? 0.59604 0.49979 0.65519 -0.01440 0.05103  -0.05355 133 GLN A CA  
902  C C   . GLN A 126 ? 0.49890 0.42625 0.58248 -0.01822 0.03734  -0.04663 133 GLN A C   
903  O O   . GLN A 126 ? 0.52302 0.44407 0.63095 -0.02374 0.04389  -0.04772 133 GLN A O   
904  C CB  . GLN A 126 ? 0.56840 0.44625 0.59919 -0.02732 0.05250  -0.07714 133 GLN A CB  
905  C CG  . GLN A 126 ? 0.48882 0.34117 0.48240 -0.02201 0.06676  -0.08492 133 GLN A CG  
906  C CD  . GLN A 126 ? 0.81766 0.63734 0.77682 -0.03486 0.07127  -0.11173 133 GLN A CD  
907  O OE1 . GLN A 126 ? 0.88334 0.69041 0.85971 -0.04761 0.07293  -0.12452 133 GLN A OE1 
908  N NE2 . GLN A 126 ? 0.89274 0.69674 0.80133 -0.03190 0.07401  -0.12129 133 GLN A NE2 
909  N N   . PHE A 127 ? 0.35766 0.30932 0.43784 -0.01451 0.02233  -0.03841 134 PHE A N   
910  C CA  . PHE A 127 ? 0.33596 0.30859 0.43847 -0.01536 0.01339  -0.02936 134 PHE A CA  
911  C C   . PHE A 127 ? 0.39063 0.37653 0.50322 -0.00225 0.01638  -0.01280 134 PHE A C   
912  O O   . PHE A 127 ? 0.44238 0.44302 0.56773 0.00057  0.01283  -0.00360 134 PHE A O   
913  C CB  . PHE A 127 ? 0.32071 0.31004 0.41264 -0.02134 -0.00465 -0.03244 134 PHE A CB  
914  C CG  . PHE A 127 ? 0.39556 0.37521 0.47122 -0.03589 -0.01321 -0.05082 134 PHE A CG  
915  C CD1 . PHE A 127 ? 0.45142 0.41700 0.48750 -0.03548 -0.01313 -0.06126 134 PHE A CD1 
916  C CD2 . PHE A 127 ? 0.42663 0.40865 0.52595 -0.05037 -0.01987 -0.05873 134 PHE A CD2 
917  C CE1 . PHE A 127 ? 0.44164 0.39542 0.45187 -0.04901 -0.02189 -0.08128 134 PHE A CE1 
918  C CE2 . PHE A 127 ? 0.42438 0.39609 0.50550 -0.06679 -0.03085 -0.08034 134 PHE A CE2 
919  C CZ  . PHE A 127 ? 0.37687 0.33372 0.40837 -0.06597 -0.03264 -0.09278 134 PHE A CZ  
920  N N   . GLY A 128 ? 0.37929 0.36023 0.48661 0.00557  0.02291  -0.00902 135 GLY A N   
921  C CA  . GLY A 128 ? 0.42540 0.41898 0.53905 0.01561  0.02220  0.00327  135 GLY A CA  
922  C C   . GLY A 128 ? 0.44047 0.44488 0.54151 0.01885  0.01270  0.00393  135 GLY A C   
923  O O   . GLY A 128 ? 0.42313 0.43571 0.52358 0.02543  0.01057  0.01011  135 GLY A O   
924  N N   . VAL A 129 ? 0.44864 0.45232 0.53780 0.01508  0.00779  -0.00202 136 VAL A N   
925  C CA  . VAL A 129 ? 0.40913 0.42010 0.49134 0.01936  0.00342  0.00052  136 VAL A CA  
926  C C   . VAL A 129 ? 0.42343 0.42775 0.49681 0.02031  0.00534  -0.00261 136 VAL A C   
927  O O   . VAL A 129 ? 0.38694 0.39411 0.45469 0.02267  0.00435  -0.00040 136 VAL A O   
928  C CB  . VAL A 129 ? 0.31730 0.33860 0.40213 0.01788  -0.00135 0.00422  136 VAL A CB  
929  C CG1 . VAL A 129 ? 0.40695 0.43448 0.50664 0.01969  0.00138  0.01111  136 VAL A CG1 
930  C CG2 . VAL A 129 ? 0.34798 0.36954 0.42766 0.00956  -0.00741 -0.00147 136 VAL A CG2 
931  N N   . GLY A 130 ? 0.34141 0.34609 0.37385 -0.01854 0.00596  -0.02862 137 GLY A N   
932  C CA  . GLY A 130 ? 0.31646 0.32200 0.34438 -0.01149 0.00396  -0.02739 137 GLY A CA  
933  C C   . GLY A 130 ? 0.33678 0.34186 0.36343 -0.00463 0.00379  -0.02056 137 GLY A C   
934  O O   . GLY A 130 ? 0.33365 0.34218 0.35735 0.00025  0.00240  -0.01806 137 GLY A O   
935  N N   . PHE A 131 ? 0.30656 0.30652 0.33421 -0.00483 0.00556  -0.01771 138 PHE A N   
936  C CA  . PHE A 131 ? 0.36171 0.35844 0.38753 0.00052  0.00556  -0.01363 138 PHE A CA  
937  C C   . PHE A 131 ? 0.44947 0.45627 0.47721 0.00640  0.00411  -0.01249 138 PHE A C   
938  O O   . PHE A 131 ? 0.34800 0.34904 0.37302 0.01127  0.00360  -0.00852 138 PHE A O   
939  C CB  . PHE A 131 ? 0.32516 0.31740 0.34992 -0.00106 0.00782  -0.01311 138 PHE A CB  
940  C CG  . PHE A 131 ? 0.32263 0.31178 0.34542 0.00392  0.00825  -0.01223 138 PHE A CG  
941  C CD1 . PHE A 131 ? 0.39133 0.36962 0.41005 0.00414  0.00723  -0.01059 138 PHE A CD1 
942  C CD2 . PHE A 131 ? 0.41733 0.41466 0.44331 0.00837  0.00981  -0.01388 138 PHE A CD2 
943  C CE1 . PHE A 131 ? 0.43914 0.41066 0.45545 0.00720  0.00780  -0.01148 138 PHE A CE1 
944  C CE2 . PHE A 131 ? 0.41060 0.40072 0.43421 0.01407  0.01088  -0.01442 138 PHE A CE2 
945  C CZ  . PHE A 131 ? 0.33494 0.31009 0.35292 0.01270  0.00989  -0.01366 138 PHE A CZ  
946  N N   . TYR A 132 ? 0.42743 0.44970 0.46051 0.00595  0.00328  -0.01528 139 TYR A N   
947  C CA  . TYR A 132 ? 0.35224 0.38689 0.38847 0.01392  0.00120  -0.01308 139 TYR A CA  
948  C C   . TYR A 132 ? 0.37832 0.41534 0.40950 0.01791  -0.00224 -0.00936 139 TYR A C   
949  O O   . TYR A 132 ? 0.35865 0.39996 0.38975 0.02660  -0.00403 -0.00414 139 TYR A O   
950  C CB  . TYR A 132 ? 0.46614 0.52269 0.51169 0.01193  0.00060  -0.01718 139 TYR A CB  
951  C CG  . TYR A 132 ? 0.43767 0.49380 0.48722 0.00890  0.00552  -0.01916 139 TYR A CG  
952  C CD1 . TYR A 132 ? 0.35373 0.40420 0.40253 0.01658  0.00844  -0.01759 139 TYR A CD1 
953  C CD2 . TYR A 132 ? 0.38586 0.44515 0.43829 -0.00206 0.00792  -0.02264 139 TYR A CD2 
954  C CE1 . TYR A 132 ? 0.34498 0.39681 0.39486 0.01394  0.01367  -0.02001 139 TYR A CE1 
955  C CE2 . TYR A 132 ? 0.52209 0.58185 0.57598 -0.00532 0.01331  -0.02280 139 TYR A CE2 
956  C CZ  . TYR A 132 ? 0.42187 0.47962 0.47391 0.00294  0.01617  -0.02175 139 TYR A CZ  
957  O OH  . TYR A 132 ? 0.48693 0.54745 0.53818 -0.00018 0.02212  -0.02258 139 TYR A OH  
958  N N   . SER A 133 ? 0.34427 0.37819 0.37044 0.01274  -0.00266 -0.01141 140 SER A N   
959  C CA  . SER A 133 ? 0.34930 0.38565 0.36817 0.01619  -0.00443 -0.00735 140 SER A CA  
960  C C   . SER A 133 ? 0.39411 0.41612 0.40909 0.02098  -0.00250 0.00122  140 SER A C   
961  O O   . SER A 133 ? 0.39770 0.42146 0.40617 0.02436  -0.00319 0.00750  140 SER A O   
962  C CB  . SER A 133 ? 0.32941 0.36410 0.34362 0.01040  -0.00343 -0.01274 140 SER A CB  
963  O OG  . SER A 133 ? 0.43019 0.44917 0.44402 0.00858  0.00022  -0.01150 140 SER A OG  
964  N N   . ALA A 134 ? 0.35324 0.36120 0.37107 0.02031  0.00001  0.00153  141 ALA A N   
965  C CA  . ALA A 134 ? 0.38248 0.37525 0.39746 0.02303  0.00166  0.00806  141 ALA A CA  
966  C C   . ALA A 134 ? 0.34208 0.33533 0.35592 0.03241  0.00022  0.01481  141 ALA A C   
967  O O   . ALA A 134 ? 0.46873 0.45001 0.47775 0.03465  0.00131  0.02286  141 ALA A O   
968  C CB  . ALA A 134 ? 0.30693 0.28672 0.32430 0.02018  0.00372  0.00456  141 ALA A CB  
969  N N   . TYR A 135 ? 0.33367 0.34085 0.35271 0.03814  -0.00199 0.01249  142 TYR A N   
970  C CA  . TYR A 135 ? 0.38032 0.39003 0.40000 0.04999  -0.00391 0.01951  142 TYR A CA  
971  C C   . TYR A 135 ? 0.42754 0.45095 0.44099 0.05375  -0.00805 0.02693  142 TYR A C   
972  O O   . TYR A 135 ? 0.37840 0.40664 0.39161 0.06513  -0.01084 0.03486  142 TYR A O   
973  C CB  . TYR A 135 ? 0.32049 0.34513 0.35038 0.05576  -0.00450 0.01417  142 TYR A CB  
974  C CG  . TYR A 135 ? 0.33974 0.34913 0.37229 0.05451  0.00044  0.00841  142 TYR A CG  
975  C CD1 . TYR A 135 ? 0.39183 0.38227 0.42342 0.06342  0.00302  0.01092  142 TYR A CD1 
976  C CD2 . TYR A 135 ? 0.34176 0.35367 0.37590 0.04437  0.00265  0.00054  142 TYR A CD2 
977  C CE1 . TYR A 135 ? 0.36876 0.34599 0.40042 0.06181  0.00750  0.00356  142 TYR A CE1 
978  C CE2 . TYR A 135 ? 0.37187 0.37218 0.40552 0.04309  0.00681  -0.00444 142 TYR A CE2 
979  C CZ  . TYR A 135 ? 0.35211 0.33622 0.38412 0.05147  0.00913  -0.00393 142 TYR A CZ  
980  O OH  . TYR A 135 ? 0.43074 0.40410 0.46007 0.04974  0.01318  -0.01091 142 TYR A OH  
981  N N   . LEU A 136 ? 0.34587 0.37601 0.35347 0.04555  -0.00842 0.02456  143 LEU A N   
982  C CA  . LEU A 136 ? 0.37053 0.40928 0.36759 0.04816  -0.01072 0.03249  143 LEU A CA  
983  C C   . LEU A 136 ? 0.44193 0.45932 0.43177 0.05105  -0.00723 0.04520  143 LEU A C   
984  O O   . LEU A 136 ? 0.38137 0.40171 0.36314 0.05847  -0.00925 0.05692  143 LEU A O   
985  C CB  . LEU A 136 ? 0.32918 0.37741 0.32086 0.03883  -0.01006 0.02507  143 LEU A CB  
986  C CG  . LEU A 136 ? 0.38076 0.44874 0.37669 0.03404  -0.01368 0.01262  143 LEU A CG  
987  C CD1 . LEU A 136 ? 0.40454 0.47106 0.39568 0.02534  -0.01083 0.00402  143 LEU A CD1 
988  C CD2 . LEU A 136 ? 0.39972 0.49318 0.39248 0.03981  -0.02071 0.01464  143 LEU A CD2 
989  N N   . VAL A 137 ? 0.44869 0.44501 0.44095 0.04451  -0.00218 0.04367  144 VAL A N   
990  C CA  . VAL A 137 ? 0.36309 0.33918 0.34948 0.04277  0.00192  0.05441  144 VAL A CA  
991  C C   . VAL A 137 ? 0.48178 0.43190 0.47281 0.04501  0.00416  0.05569  144 VAL A C   
992  O O   . VAL A 137 ? 0.44978 0.37957 0.43608 0.04448  0.00722  0.06584  144 VAL A O   
993  C CB  . VAL A 137 ? 0.46197 0.43811 0.44683 0.03113  0.00623  0.05194  144 VAL A CB  
994  C CG1 . VAL A 137 ? 0.36124 0.36044 0.33878 0.03006  0.00541  0.05045  144 VAL A CG1 
995  C CG2 . VAL A 137 ? 0.48047 0.45243 0.47477 0.02435  0.00715  0.04000  144 VAL A CG2 
996  N N   . ALA A 138 ? 0.39559 0.34465 0.39474 0.04679  0.00342  0.04550  145 ALA A N   
997  C CA  . ALA A 138 ? 0.44746 0.37220 0.44960 0.04792  0.00614  0.04293  145 ALA A CA  
998  C C   . ALA A 138 ? 0.38125 0.30609 0.38728 0.06250  0.00469  0.04316  145 ALA A C   
999  O O   . ALA A 138 ? 0.47426 0.42339 0.48548 0.06783  0.00156  0.03922  145 ALA A O   
1000 C CB  . ALA A 138 ? 0.41724 0.34114 0.42398 0.03837  0.00746  0.03036  145 ALA A CB  
1001 N N   . GLU A 139 ? 0.38326 0.28105 0.38769 0.06897  0.00728  0.04762  146 GLU A N   
1002 C CA  . GLU A 139 ? 0.46300 0.35867 0.47288 0.08443  0.00723  0.04559  146 GLU A CA  
1003 C C   . GLU A 139 ? 0.43907 0.33083 0.45389 0.08165  0.01037  0.03026  146 GLU A C   
1004 O O   . GLU A 139 ? 0.51339 0.41509 0.53489 0.09306  0.01097  0.02505  146 GLU A O   
1005 C CB  . GLU A 139 ? 0.49425 0.35888 0.49969 0.09504  0.00924  0.05681  146 GLU A CB  
1006 C CG  . GLU A 139 ? 0.70214 0.53410 0.70053 0.08206  0.01333  0.05990  146 GLU A CG  
1007 C CD  . GLU A 139 ? 1.00806 0.80408 1.00141 0.09131  0.01604  0.07212  146 GLU A CD  
1008 O OE1 . GLU A 139 ? 0.94704 0.70941 0.93933 0.08631  0.02047  0.06606  146 GLU A OE1 
1009 O OE2 . GLU A 139 ? 1.01467 0.81516 1.00434 0.10339  0.01354  0.08774  146 GLU A OE2 
1010 N N   . LYS A 140 ? 0.49279 0.37332 0.50439 0.06706  0.01237  0.02325  147 LYS A N   
1011 C CA  . LYS A 140 ? 0.48158 0.35944 0.49446 0.06312  0.01488  0.00927  147 LYS A CA  
1012 C C   . LYS A 140 ? 0.48794 0.37329 0.49880 0.04679  0.01375  0.00475  147 LYS A C   
1013 O O   . LYS A 140 ? 0.43178 0.31056 0.44003 0.03777  0.01301  0.01037  147 LYS A O   
1014 C CB  . LYS A 140 ? 0.42690 0.27117 0.43609 0.06637  0.01882  0.00459  147 LYS A CB  
1015 C CG  . LYS A 140 ? 0.64737 0.48686 0.65374 0.05909  0.02118  -0.01080 147 LYS A CG  
1016 C CD  . LYS A 140 ? 0.59184 0.39927 0.59440 0.06564  0.02552  -0.01820 147 LYS A CD  
1017 C CE  . LYS A 140 ? 0.68106 0.46400 0.67685 0.04947  0.02567  -0.02413 147 LYS A CE  
1018 N NZ  . LYS A 140 ? 0.74739 0.48986 0.73945 0.05400  0.02944  -0.02594 147 LYS A NZ  
1019 N N   . VAL A 141 ? 0.36663 0.26720 0.37911 0.04366  0.01395  -0.00438 148 VAL A N   
1020 C CA  . VAL A 141 ? 0.33614 0.24423 0.34687 0.03079  0.01245  -0.00783 148 VAL A CA  
1021 C C   . VAL A 141 ? 0.43148 0.33283 0.43789 0.02713  0.01419  -0.01863 148 VAL A C   
1022 O O   . VAL A 141 ? 0.37784 0.28568 0.38443 0.03362  0.01684  -0.02457 148 VAL A O   
1023 C CB  . VAL A 141 ? 0.34918 0.28239 0.36377 0.02932  0.01059  -0.00659 148 VAL A CB  
1024 C CG1 . VAL A 141 ? 0.34599 0.28351 0.35881 0.01860  0.00927  -0.00913 148 VAL A CG1 
1025 C CG2 . VAL A 141 ? 0.39237 0.33421 0.40890 0.03249  0.00841  0.00213  148 VAL A CG2 
1026 N N   . THR A 142 ? 0.40750 0.29867 0.41001 0.01660  0.01279  -0.02147 149 THR A N   
1027 C CA  . THR A 142 ? 0.44602 0.33518 0.44222 0.01096  0.01277  -0.03187 149 THR A CA  
1028 C C   . THR A 142 ? 0.47805 0.38443 0.47405 0.00241  0.00913  -0.03052 149 THR A C   
1029 O O   . THR A 142 ? 0.46779 0.37771 0.46807 -0.00322 0.00649  -0.02457 149 THR A O   
1030 C CB  . THR A 142 ? 0.46712 0.33251 0.45901 0.00471  0.01280  -0.03765 149 THR A CB  
1031 O OG1 . THR A 142 ? 0.49442 0.33868 0.48727 0.01334  0.01623  -0.03568 149 THR A OG1 
1032 C CG2 . THR A 142 ? 0.44473 0.30835 0.42746 0.00109  0.01299  -0.05105 149 THR A CG2 
1033 N N   . VAL A 143 ? 0.33714 0.25412 0.32790 0.00210  0.00949  -0.03548 150 VAL A N   
1034 C CA  . VAL A 143 ? 0.37497 0.30583 0.36418 -0.00409 0.00598  -0.03295 150 VAL A CA  
1035 C C   . VAL A 143 ? 0.44049 0.37066 0.41932 -0.00949 0.00404  -0.04098 150 VAL A C   
1036 O O   . VAL A 143 ? 0.44887 0.37924 0.41947 -0.00643 0.00744  -0.04775 150 VAL A O   
1037 C CB  . VAL A 143 ? 0.37924 0.32435 0.37020 -0.00057 0.00793  -0.02867 150 VAL A CB  
1038 C CG1 . VAL A 143 ? 0.37456 0.32885 0.36309 -0.00562 0.00458  -0.02462 150 VAL A CG1 
1039 C CG2 . VAL A 143 ? 0.38957 0.33756 0.38971 0.00386  0.00884  -0.02286 150 VAL A CG2 
1040 N N   . ILE A 144 ? 0.39493 0.32706 0.37413 -0.01750 -0.00135 -0.04082 151 ILE A N   
1041 C CA  . ILE A 144 ? 0.39235 0.32902 0.36137 -0.02375 -0.00537 -0.04802 151 ILE A CA  
1042 C C   . ILE A 144 ? 0.39155 0.34650 0.35970 -0.02436 -0.00962 -0.04032 151 ILE A C   
1043 O O   . ILE A 144 ? 0.37540 0.33672 0.35376 -0.02458 -0.01211 -0.03234 151 ILE A O   
1044 C CB  . ILE A 144 ? 0.42942 0.35837 0.40075 -0.03335 -0.00949 -0.05381 151 ILE A CB  
1045 C CG1 . ILE A 144 ? 0.52973 0.43549 0.50511 -0.03234 -0.00481 -0.05666 151 ILE A CG1 
1046 C CG2 . ILE A 144 ? 0.44861 0.38134 0.40685 -0.03988 -0.01361 -0.06506 151 ILE A CG2 
1047 C CD1 . ILE A 144 ? 0.55054 0.44011 0.51572 -0.02800 -0.00029 -0.06812 151 ILE A CD1 
1048 N N   . THR A 145 ? 0.40045 0.36334 0.35574 -0.02392 -0.00998 -0.04227 152 THR A N   
1049 C CA  . THR A 145 ? 0.36149 0.33792 0.31483 -0.02262 -0.01310 -0.03231 152 THR A CA  
1050 C C   . THR A 145 ? 0.43427 0.42108 0.37100 -0.02560 -0.01724 -0.03525 152 THR A C   
1051 O O   . THR A 145 ? 0.46236 0.44629 0.38658 -0.02718 -0.01474 -0.04566 152 THR A O   
1052 C CB  . THR A 145 ? 0.42775 0.40329 0.38342 -0.01700 -0.00677 -0.02510 152 THR A CB  
1053 O OG1 . THR A 145 ? 0.40053 0.38292 0.35695 -0.01576 -0.00960 -0.01423 152 THR A OG1 
1054 C CG2 . THR A 145 ? 0.42138 0.39771 0.36534 -0.01549 -0.00048 -0.03004 152 THR A CG2 
1055 N N   . LYS A 146 ? 0.35898 0.35849 0.29509 -0.02536 -0.02370 -0.02605 153 LYS A N   
1056 C CA  . LYS A 146 ? 0.37753 0.39077 0.29714 -0.02743 -0.02966 -0.02583 153 LYS A CA  
1057 C C   . LYS A 146 ? 0.46607 0.48630 0.38434 -0.02175 -0.03152 -0.00970 153 LYS A C   
1058 O O   . LYS A 146 ? 0.38003 0.40393 0.31173 -0.01863 -0.03589 -0.00185 153 LYS A O   
1059 C CB  . LYS A 146 ? 0.37279 0.39675 0.29437 -0.03431 -0.03938 -0.03307 153 LYS A CB  
1060 C CG  . LYS A 146 ? 0.38170 0.42551 0.28691 -0.03603 -0.04826 -0.03156 153 LYS A CG  
1061 C CD  . LYS A 146 ? 0.43393 0.47639 0.31516 -0.03779 -0.04425 -0.04041 153 LYS A CD  
1062 C CE  . LYS A 146 ? 0.49476 0.55881 0.35771 -0.04153 -0.05452 -0.04226 153 LYS A CE  
1063 N NZ  . LYS A 146 ? 0.51548 0.59246 0.37251 -0.03408 -0.05835 -0.02268 153 LYS A NZ  
1064 N N   . HIS A 147 ? 0.42790 0.44885 0.33023 -0.02013 -0.02723 -0.00462 154 HIS A N   
1065 C CA  . HIS A 147 ? 0.38874 0.41239 0.28570 -0.01550 -0.02827 0.01186  154 HIS A CA  
1066 C C   . HIS A 147 ? 0.39910 0.43939 0.27637 -0.01612 -0.03619 0.01517  154 HIS A C   
1067 O O   . HIS A 147 ? 0.49107 0.53846 0.35332 -0.02102 -0.03650 0.00362  154 HIS A O   
1068 C CB  . HIS A 147 ? 0.51424 0.52777 0.40681 -0.01522 -0.01715 0.01680  154 HIS A CB  
1069 C CG  . HIS A 147 ? 0.47188 0.48119 0.36018 -0.01192 -0.01628 0.03446  154 HIS A CG  
1070 N ND1 . HIS A 147 ? 0.46710 0.48372 0.33456 -0.01178 -0.01751 0.04456  154 HIS A ND1 
1071 C CD2 . HIS A 147 ? 0.45758 0.45361 0.35855 -0.00889 -0.01365 0.04377  154 HIS A CD2 
1072 C CE1 . HIS A 147 ? 0.46801 0.47389 0.33621 -0.00861 -0.01559 0.06089  154 HIS A CE1 
1073 N NE2 . HIS A 147 ? 0.47050 0.46293 0.35926 -0.00699 -0.01322 0.05961  154 HIS A NE2 
1074 N N   . ASN A 148 ? 0.40200 0.44859 0.27870 -0.01030 -0.04283 0.03059  155 ASN A N   
1075 C CA  . ASN A 148 ? 0.48402 0.55001 0.34225 -0.00937 -0.05249 0.03613  155 ASN A CA  
1076 C C   . ASN A 148 ? 0.56855 0.63787 0.39930 -0.01309 -0.04716 0.03524  155 ASN A C   
1077 O O   . ASN A 148 ? 0.49300 0.58066 0.30472 -0.01539 -0.05455 0.03195  155 ASN A O   
1078 C CB  . ASN A 148 ? 0.49727 0.56549 0.35812 0.00055  -0.05839 0.05676  155 ASN A CB  
1079 C CG  . ASN A 148 ? 0.64432 0.72234 0.52821 0.00563  -0.06743 0.05699  155 ASN A CG  
1080 O OD1 . ASN A 148 ? 0.51580 0.60718 0.40882 -0.00017 -0.07288 0.04327  155 ASN A OD1 
1081 N ND2 . ASN A 148 ? 0.49036 0.56143 0.38413 0.01641  -0.06836 0.07261  155 ASN A ND2 
1082 N N   . ASP A 149 ? 0.47715 0.53189 0.30530 -0.01413 -0.03438 0.03785  156 ASP A N   
1083 C CA  . ASP A 149 ? 0.48633 0.54613 0.28963 -0.01730 -0.02700 0.03910  156 ASP A CA  
1084 C C   . ASP A 149 ? 0.60398 0.66472 0.40314 -0.02258 -0.01940 0.01805  156 ASP A C   
1085 O O   . ASP A 149 ? 0.53873 0.60415 0.32020 -0.02473 -0.01038 0.01695  156 ASP A O   
1086 C CB  . ASP A 149 ? 0.51200 0.55825 0.31517 -0.01637 -0.01656 0.05574  156 ASP A CB  
1087 C CG  . ASP A 149 ? 0.68860 0.72937 0.49122 -0.00997 -0.02267 0.07807  156 ASP A CG  
1088 O OD1 . ASP A 149 ? 0.60161 0.65573 0.39750 -0.00514 -0.03505 0.08320  156 ASP A OD1 
1089 O OD2 . ASP A 149 ? 0.58962 0.61260 0.39897 -0.00965 -0.01509 0.09035  156 ASP A OD2 
1090 N N   . ASP A 150 ? 0.54408 0.59986 0.35910 -0.02420 -0.02191 0.00195  157 ASP A N   
1091 C CA  . ASP A 150 ? 0.46049 0.51158 0.27407 -0.02685 -0.01369 -0.01696 157 ASP A CA  
1092 C C   . ASP A 150 ? 0.46458 0.51408 0.28472 -0.03042 -0.02146 -0.03395 157 ASP A C   
1093 O O   . ASP A 150 ? 0.57808 0.63356 0.40575 -0.03184 -0.03269 -0.03077 157 ASP A O   
1094 C CB  . ASP A 150 ? 0.42842 0.46575 0.26044 -0.02450 -0.00260 -0.01569 157 ASP A CB  
1095 C CG  . ASP A 150 ? 0.64851 0.68755 0.47246 -0.02436 0.00940  -0.02727 157 ASP A CG  
1096 O OD1 . ASP A 150 ? 0.58671 0.63222 0.39330 -0.02581 0.00920  -0.04117 157 ASP A OD1 
1097 O OD2 . ASP A 150 ? 0.53690 0.57244 0.37218 -0.02271 0.01902  -0.02338 157 ASP A OD2 
1098 N N   . GLU A 151 ? 0.52152 0.56291 0.33965 -0.03190 -0.01493 -0.05204 158 GLU A N   
1099 C CA  . GLU A 151 ? 0.51787 0.55128 0.34287 -0.03661 -0.02029 -0.06875 158 GLU A CA  
1100 C C   . GLU A 151 ? 0.53763 0.55405 0.38961 -0.03468 -0.01813 -0.06689 158 GLU A C   
1101 O O   . GLU A 151 ? 0.47699 0.48878 0.34119 -0.02944 -0.01241 -0.05540 158 GLU A O   
1102 C CB  . GLU A 151 ? 0.53625 0.56393 0.34573 -0.03802 -0.01394 -0.08979 158 GLU A CB  
1103 C CG  . GLU A 151 ? 0.64208 0.68616 0.42224 -0.03843 -0.01150 -0.09336 158 GLU A CG  
1104 C CD  . GLU A 151 ? 1.08756 1.12369 0.85765 -0.03504 0.00100  -0.11136 158 GLU A CD  
1105 O OE1 . GLU A 151 ? 0.98723 1.00452 0.76597 -0.03536 0.00247  -0.12780 158 GLU A OE1 
1106 O OE2 . GLU A 151 ? 1.15241 1.20068 0.90654 -0.03158 0.01006  -0.10858 158 GLU A OE2 
1107 N N   . GLN A 152 ? 0.46431 0.47113 0.32459 -0.03994 -0.02242 -0.07880 159 GLN A N   
1108 C CA  . GLN A 152 ? 0.51083 0.50163 0.39390 -0.03876 -0.02024 -0.07691 159 GLN A CA  
1109 C C   . GLN A 152 ? 0.66841 0.64162 0.55347 -0.03283 -0.00909 -0.08487 159 GLN A C   
1110 O O   . GLN A 152 ? 0.52228 0.48809 0.39490 -0.03333 -0.00549 -0.10036 159 GLN A O   
1111 C CB  . GLN A 152 ? 0.41707 0.40470 0.30805 -0.04814 -0.02843 -0.08491 159 GLN A CB  
1112 C CG  . GLN A 152 ? 0.44849 0.42357 0.36203 -0.04829 -0.02715 -0.07958 159 GLN A CG  
1113 C CD  . GLN A 152 ? 0.68771 0.66989 0.61117 -0.05887 -0.03622 -0.08166 159 GLN A CD  
1114 O OE1 . GLN A 152 ? 0.64671 0.65157 0.57000 -0.06140 -0.04491 -0.07607 159 GLN A OE1 
1115 N NE2 . GLN A 152 ? 0.51107 0.47489 0.44377 -0.06517 -0.03421 -0.08903 159 GLN A NE2 
1116 N N   . TYR A 153 ? 0.50293 0.47068 0.40349 -0.02644 -0.00382 -0.07493 160 TYR A N   
1117 C CA  . TYR A 153 ? 0.45689 0.41341 0.36199 -0.01871 0.00595  -0.07971 160 TYR A CA  
1118 C C   . TYR A 153 ? 0.59010 0.53208 0.51405 -0.01637 0.00617  -0.07581 160 TYR A C   
1119 O O   . TYR A 153 ? 0.45065 0.39495 0.38538 -0.01962 0.00093  -0.06626 160 TYR A O   
1120 C CB  . TYR A 153 ? 0.42778 0.39720 0.33188 -0.01291 0.01315  -0.07129 160 TYR A CB  
1121 C CG  . TYR A 153 ? 0.59994 0.58266 0.48337 -0.01384 0.01656  -0.07553 160 TYR A CG  
1122 C CD1 . TYR A 153 ? 0.49372 0.47501 0.36739 -0.00937 0.02473  -0.08946 160 TYR A CD1 
1123 C CD2 . TYR A 153 ? 0.58751 0.58439 0.46020 -0.01822 0.01199  -0.06513 160 TYR A CD2 
1124 C CE1 . TYR A 153 ? 0.61299 0.60879 0.46563 -0.01043 0.02883  -0.09367 160 TYR A CE1 
1125 C CE2 . TYR A 153 ? 0.56612 0.57621 0.41722 -0.01934 0.01527  -0.06725 160 TYR A CE2 
1126 C CZ  . TYR A 153 ? 0.76192 0.77251 0.60250 -0.01606 0.02392  -0.08187 160 TYR A CZ  
1127 O OH  . TYR A 153 ? 1.00530 1.03131 0.82252 -0.01734 0.02816  -0.08419 160 TYR A OH  
1128 N N   . ALA A 154 ? 0.44829 0.37622 0.37556 -0.00943 0.01278  -0.08283 161 ALA A N   
1129 C CA  . ALA A 154 ? 0.47844 0.39306 0.42122 -0.00490 0.01401  -0.07757 161 ALA A CA  
1130 C C   . ALA A 154 ? 0.40992 0.33089 0.35959 0.00637  0.02120  -0.07391 161 ALA A C   
1131 O O   . ALA A 154 ? 0.58756 0.50816 0.53193 0.01340  0.02773  -0.08284 161 ALA A O   
1132 C CB  . ALA A 154 ? 0.50931 0.39847 0.45135 -0.00625 0.01428  -0.08775 161 ALA A CB  
1133 N N   . TRP A 155 ? 0.35821 0.28700 0.32011 0.00798  0.02002  -0.06187 162 TRP A N   
1134 C CA  . TRP A 155 ? 0.37509 0.31248 0.34714 0.01709  0.02477  -0.05744 162 TRP A CA  
1135 C C   . TRP A 155 ? 0.51682 0.43989 0.49861 0.02266  0.02362  -0.05386 162 TRP A C   
1136 O O   . TRP A 155 ? 0.39569 0.30813 0.37896 0.01679  0.01899  -0.04979 162 TRP A O   
1137 C CB  . TRP A 155 ? 0.31859 0.27398 0.29575 0.01319  0.02344  -0.04738 162 TRP A CB  
1138 C CG  . TRP A 155 ? 0.37110 0.34037 0.35989 0.01897  0.02691  -0.04295 162 TRP A CG  
1139 C CD1 . TRP A 155 ? 0.36718 0.35454 0.35735 0.01964  0.03239  -0.04328 162 TRP A CD1 
1140 C CD2 . TRP A 155 ? 0.38591 0.35553 0.38648 0.02326  0.02468  -0.03724 162 TRP A CD2 
1141 N NE1 . TRP A 155 ? 0.39477 0.39466 0.39867 0.02350  0.03316  -0.03927 162 TRP A NE1 
1142 C CE2 . TRP A 155 ? 0.40774 0.39726 0.41715 0.02633  0.02797  -0.03562 162 TRP A CE2 
1143 C CE3 . TRP A 155 ? 0.43714 0.39420 0.44104 0.02404  0.02037  -0.03300 162 TRP A CE3 
1144 C CZ2 . TRP A 155 ? 0.33491 0.33299 0.35568 0.03063  0.02580  -0.03097 162 TRP A CZ2 
1145 C CZ3 . TRP A 155 ? 0.33463 0.29898 0.34786 0.02900  0.01905  -0.02720 162 TRP A CZ3 
1146 C CH2 . TRP A 155 ? 0.37213 0.35717 0.39339 0.03250  0.02111  -0.02673 162 TRP A CH2 
1147 N N   . GLU A 156 ? 0.35011 0.27471 0.33870 0.03436  0.02802  -0.05446 163 GLU A N   
1148 C CA  . GLU A 156 ? 0.44233 0.35221 0.43799 0.04141  0.02686  -0.04938 163 GLU A CA  
1149 C C   . GLU A 156 ? 0.52569 0.45060 0.53225 0.05438  0.02943  -0.04536 163 GLU A C   
1150 O O   . GLU A 156 ? 0.43068 0.36723 0.43907 0.06209  0.03480  -0.05177 163 GLU A O   
1151 C CB  . GLU A 156 ? 0.53598 0.41682 0.52523 0.04402  0.02879  -0.05763 163 GLU A CB  
1152 C CG  . GLU A 156 ? 0.64691 0.50674 0.64121 0.04987  0.02781  -0.05012 163 GLU A CG  
1153 C CD  . GLU A 156 ? 0.77683 0.60313 0.76371 0.04496  0.02849  -0.05716 163 GLU A CD  
1154 O OE1 . GLU A 156 ? 0.78760 0.60370 0.77364 0.03284  0.02472  -0.05244 163 GLU A OE1 
1155 O OE2 . GLU A 156 ? 0.72953 0.54058 0.71170 0.05248  0.03327  -0.06861 163 GLU A OE2 
1156 N N   . SER A 157 ? 0.39738 0.32426 0.41117 0.05718  0.02568  -0.03503 164 SER A N   
1157 C CA  . SER A 157 ? 0.37305 0.31669 0.39764 0.07006  0.02641  -0.03086 164 SER A CA  
1158 C C   . SER A 157 ? 0.47671 0.41101 0.50405 0.07600  0.02228  -0.01997 164 SER A C   
1159 O O   . SER A 157 ? 0.42633 0.35732 0.45062 0.06702  0.01828  -0.01331 164 SER A O   
1160 C CB  . SER A 157 ? 0.31431 0.29009 0.34610 0.06520  0.02574  -0.02940 164 SER A CB  
1161 O OG  . SER A 157 ? 0.42629 0.42285 0.47022 0.07678  0.02559  -0.02635 164 SER A OG  
1162 N N   . SER A 158 ? 0.44425 0.37586 0.47712 0.09232  0.02371  -0.01768 165 SER A N   
1163 C CA  . SER A 158 ? 0.51786 0.44799 0.55383 0.10149  0.01957  -0.00511 165 SER A CA  
1164 C C   . SER A 158 ? 0.41799 0.38550 0.46556 0.10887  0.01631  -0.00122 165 SER A C   
1165 O O   . SER A 158 ? 0.51995 0.49253 0.57207 0.12257  0.01321  0.00777  165 SER A O   
1166 C CB  . SER A 158 ? 0.49256 0.39305 0.52694 0.11641  0.02238  -0.00291 165 SER A CB  
1167 O OG  . SER A 158 ? 0.54333 0.40796 0.56733 0.10722  0.02492  -0.00715 165 SER A OG  
1168 N N   . ALA A 159 ? 0.38790 0.38176 0.44019 0.09942  0.01665  -0.00734 166 ALA A N   
1169 C CA  . ALA A 159 ? 0.48735 0.51978 0.55287 0.10338  0.01440  -0.00686 166 ALA A CA  
1170 C C   . ALA A 159 ? 0.48884 0.53054 0.56499 0.12257  0.01803  -0.00909 166 ALA A C   
1171 O O   . ALA A 159 ? 0.50045 0.52427 0.57342 0.12762  0.02472  -0.01656 166 ALA A O   
1172 C CB  . ALA A 159 ? 0.41398 0.45911 0.47957 0.10161  0.00661  0.00245  166 ALA A CB  
1173 N N   . GLY A 160 ? 0.45546 0.52611 0.54436 0.13438  0.01380  -0.00367 167 GLY A N   
1174 C CA  . GLY A 160 ? 0.38673 0.47183 0.48878 0.15386  0.01773  -0.00642 167 GLY A CA  
1175 C C   . GLY A 160 ? 0.35347 0.46704 0.46624 0.14963  0.02473  -0.01771 167 GLY A C   
1176 O O   . GLY A 160 ? 0.43183 0.56017 0.55649 0.16601  0.02986  -0.02184 167 GLY A O   
1177 N N   . GLY A 161 ? 0.32436 0.44590 0.43323 0.12872  0.02578  -0.02217 168 GLY A N   
1178 C CA  . GLY A 161 ? 0.43475 0.58486 0.55278 0.12152  0.03264  -0.03039 168 GLY A CA  
1179 C C   . GLY A 161 ? 0.39452 0.52482 0.50033 0.11536  0.04175  -0.03911 168 GLY A C   
1180 O O   . GLY A 161 ? 0.32375 0.47790 0.43534 0.10973  0.04886  -0.04497 168 GLY A O   
1181 N N   . SER A 162 ? 0.35780 0.44747 0.44661 0.11516  0.04180  -0.04010 169 SER A N   
1182 C CA  . SER A 162 ? 0.33411 0.40702 0.40993 0.11014  0.04938  -0.04958 169 SER A CA  
1183 C C   . SER A 162 ? 0.38121 0.41893 0.43900 0.09771  0.04533  -0.04826 169 SER A C   
1184 O O   . SER A 162 ? 0.33238 0.35311 0.38768 0.09676  0.03845  -0.04072 169 SER A O   
1185 C CB  . SER A 162 ? 0.42508 0.48947 0.50206 0.12931  0.05689  -0.05821 169 SER A CB  
1186 O OG  . SER A 162 ? 0.40690 0.43445 0.47726 0.13944  0.05369  -0.05607 169 SER A OG  
1187 N N   . PHE A 163 ? 0.34583 0.37670 0.39121 0.08773  0.04978  -0.05526 170 PHE A N   
1188 C CA  . PHE A 163 ? 0.33952 0.34173 0.36868 0.07662  0.04642  -0.05604 170 PHE A CA  
1189 C C   . PHE A 163 ? 0.44859 0.44045 0.46459 0.07703  0.05300  -0.06821 170 PHE A C   
1190 O O   . PHE A 163 ? 0.38812 0.39824 0.40657 0.08354  0.06096  -0.07511 170 PHE A O   
1191 C CB  . PHE A 163 ? 0.31870 0.32828 0.34501 0.05988  0.04173  -0.04925 170 PHE A CB  
1192 C CG  . PHE A 163 ? 0.37535 0.40678 0.40028 0.05141  0.04680  -0.05088 170 PHE A CG  
1193 C CD1 . PHE A 163 ? 0.35761 0.41794 0.39640 0.05029  0.04882  -0.04754 170 PHE A CD1 
1194 C CD2 . PHE A 163 ? 0.40285 0.42681 0.41220 0.04332  0.04921  -0.05490 170 PHE A CD2 
1195 C CE1 . PHE A 163 ? 0.32312 0.40191 0.36077 0.04062  0.05450  -0.04755 170 PHE A CE1 
1196 C CE2 . PHE A 163 ? 0.38626 0.42932 0.39256 0.03534  0.05445  -0.05384 170 PHE A CE2 
1197 C CZ  . PHE A 163 ? 0.34128 0.41023 0.36192 0.03349  0.05764  -0.04973 170 PHE A CZ  
1198 N N   . THR A 164 ? 0.37835 0.34243 0.38063 0.07028  0.04983  -0.07170 171 THR A N   
1199 C CA  . THR A 164 ? 0.39073 0.34363 0.37745 0.06830  0.05428  -0.08469 171 THR A CA  
1200 C C   . THR A 164 ? 0.49943 0.45099 0.47304 0.05150  0.04940  -0.08313 171 THR A C   
1201 O O   . THR A 164 ? 0.41402 0.36228 0.39057 0.04307  0.04221  -0.07346 171 THR A O   
1202 C CB  . THR A 164 ? 0.44073 0.35973 0.42223 0.07557  0.05469  -0.09335 171 THR A CB  
1203 O OG1 . THR A 164 ? 0.51980 0.41757 0.50075 0.06696  0.04670  -0.08592 171 THR A OG1 
1204 C CG2 . THR A 164 ? 0.50394 0.42088 0.49770 0.09555  0.05971  -0.09453 171 THR A CG2 
1205 N N   . VAL A 165 ? 0.48123 0.43731 0.43998 0.04779  0.05348  -0.09264 172 VAL A N   
1206 C CA  . VAL A 165 ? 0.41321 0.36774 0.35713 0.03398  0.04821  -0.09230 172 VAL A CA  
1207 C C   . VAL A 165 ? 0.42563 0.36580 0.35217 0.03341  0.05002  -0.10862 172 VAL A C   
1208 O O   . VAL A 165 ? 0.44471 0.38753 0.36637 0.04240  0.05859  -0.12015 172 VAL A O   
1209 C CB  . VAL A 165 ? 0.47893 0.45917 0.41880 0.02728  0.05032  -0.08456 172 VAL A CB  
1210 C CG1 . VAL A 165 ? 0.46419 0.44269 0.38797 0.01561  0.04400  -0.08293 172 VAL A CG1 
1211 C CG2 . VAL A 165 ? 0.37989 0.37174 0.33663 0.02616  0.04848  -0.07081 172 VAL A CG2 
1212 N N   . ARG A 166 ? 0.46496 0.39159 0.38272 0.02272  0.04204  -0.11066 173 ARG A N   
1213 C CA  . ARG A 166 ? 0.53300 0.44838 0.43243 0.01848  0.04186  -0.12724 173 ARG A CA  
1214 C C   . ARG A 166 ? 0.60051 0.52175 0.49055 0.00391  0.03181  -0.12359 173 ARG A C   
1215 O O   . ARG A 166 ? 0.52536 0.45020 0.42611 -0.00131 0.02510  -0.10981 173 ARG A O   
1216 C CB  . ARG A 166 ? 0.57152 0.45449 0.47401 0.02289  0.04274  -0.13855 173 ARG A CB  
1217 C CG  . ARG A 166 ? 0.69741 0.56288 0.60658 0.01229  0.03352  -0.13273 173 ARG A CG  
1218 C CD  . ARG A 166 ? 0.67343 0.50419 0.58905 0.01680  0.03538  -0.13826 173 ARG A CD  
1219 N NE  . ARG A 166 ? 0.95670 0.77971 0.88625 0.01158  0.02968  -0.12349 173 ARG A NE  
1220 C CZ  . ARG A 166 ? 1.08333 0.90305 1.01288 -0.00370 0.02204  -0.12146 173 ARG A CZ  
1221 N NH1 . ARG A 166 ? 0.90206 0.72647 0.81903 -0.01577 0.01748  -0.13284 173 ARG A NH1 
1222 N NH2 . ARG A 166 ? 0.84660 0.66145 0.78915 -0.00696 0.01886  -0.10771 173 ARG A NH2 
1223 N N   . THR A 167 ? 0.60463 0.52918 0.47430 -0.00182 0.03070  -0.13640 174 THR A N   
1224 C CA  . THR A 167 ? 0.54004 0.47017 0.40155 -0.01501 0.01957  -0.13505 174 THR A CA  
1225 C C   . THR A 167 ? 0.66834 0.57529 0.54010 -0.02163 0.01346  -0.13938 174 THR A C   
1226 O O   . THR A 167 ? 0.61420 0.49619 0.48824 -0.01783 0.01811  -0.15076 174 THR A O   
1227 C CB  . THR A 167 ? 0.63298 0.57381 0.46857 -0.01993 0.01887  -0.14901 174 THR A CB  
1228 O OG1 . THR A 167 ? 0.89621 0.81540 0.72339 -0.01887 0.02283  -0.17105 174 THR A OG1 
1229 C CG2 . THR A 167 ? 0.54246 0.50622 0.36647 -0.01385 0.02698  -0.14388 174 THR A CG2 
1230 N N   . ASP A 168 ? 0.59539 0.51020 0.47448 -0.03103 0.00377  -0.12931 175 ASP A N   
1231 C CA  . ASP A 168 ? 0.68011 0.57727 0.57186 -0.03884 -0.00120 -0.13010 175 ASP A CA  
1232 C C   . ASP A 168 ? 0.91991 0.81688 0.80074 -0.05301 -0.00916 -0.14438 175 ASP A C   
1233 O O   . ASP A 168 ? 0.83696 0.75850 0.70905 -0.05911 -0.01689 -0.14254 175 ASP A O   
1234 C CB  . ASP A 168 ? 0.59289 0.50083 0.50234 -0.04035 -0.00589 -0.11121 175 ASP A CB  
1235 C CG  . ASP A 168 ? 0.75822 0.64944 0.68133 -0.04825 -0.00880 -0.11063 175 ASP A CG  
1236 O OD1 . ASP A 168 ? 1.04855 0.91262 0.97236 -0.04710 -0.00386 -0.11901 175 ASP A OD1 
1237 O OD2 . ASP A 168 ? 0.63820 0.54305 0.57140 -0.05534 -0.01540 -0.10153 175 ASP A OD2 
1238 N N   . THR A 169 ? 0.98001 0.84896 0.86159 -0.05839 -0.00762 -0.15819 176 THR A N   
1239 C CA  . THR A 169 ? 1.19455 1.05934 1.06720 -0.07431 -0.01486 -0.17483 176 THR A CA  
1240 C C   . THR A 169 ? 1.04896 0.91175 0.93923 -0.08843 -0.02213 -0.16867 176 THR A C   
1241 O O   . THR A 169 ? 1.07396 0.93630 0.96048 -0.10445 -0.02913 -0.18187 176 THR A O   
1242 C CB  . THR A 169 ? 1.09723 0.92881 0.95819 -0.07314 -0.00778 -0.19685 176 THR A CB  
1243 O OG1 . THR A 169 ? 1.01728 0.81743 0.89267 -0.06483 0.00012  -0.19122 176 THR A OG1 
1244 C CG2 . THR A 169 ? 0.90337 0.74407 0.74411 -0.06160 -0.00106 -0.20687 176 THR A CG2 
1245 N N   . GLY A 170 ? 0.86841 0.73200 0.77763 -0.08373 -0.02038 -0.14981 177 GLY A N   
1246 C CA  . GLY A 170 ? 0.83582 0.70083 0.76246 -0.09640 -0.02544 -0.14262 177 GLY A CA  
1247 C C   . GLY A 170 ? 1.02963 0.93144 0.96015 -0.10632 -0.03675 -0.13861 177 GLY A C   
1248 O O   . GLY A 170 ? 0.79897 0.72125 0.71484 -0.10720 -0.04262 -0.14549 177 GLY A O   
1249 N N   . GLU A 171 ? 0.95640 0.86854 0.90646 -0.11305 -0.03971 -0.12700 178 GLU A N   
1250 C CA  . GLU A 171 ? 0.97930 0.92919 0.93731 -0.12033 -0.05030 -0.12180 178 GLU A CA  
1251 C C   . GLU A 171 ? 0.83062 0.80530 0.78167 -0.10588 -0.05264 -0.11083 178 GLU A C   
1252 O O   . GLU A 171 ? 0.59897 0.56775 0.55320 -0.09233 -0.04581 -0.09856 178 GLU A O   
1253 C CB  . GLU A 171 ? 0.99717 0.95464 0.97912 -0.12636 -0.05008 -0.10940 178 GLU A CB  
1254 C CG  . GLU A 171 ? 1.04433 1.04125 1.03902 -0.13659 -0.06101 -0.10708 178 GLU A CG  
1255 C CD  . GLU A 171 ? 1.27842 1.27413 1.28371 -0.15919 -0.06459 -0.11789 178 GLU A CD  
1256 O OE1 . GLU A 171 ? 1.21205 1.17923 1.22479 -0.16581 -0.05657 -0.11716 178 GLU A OE1 
1257 O OE2 . GLU A 171 ? 1.09309 1.11716 1.09946 -0.17101 -0.07564 -0.12648 178 GLU A OE2 
1258 N N   . PRO A 172 ? 0.82046 0.82238 0.76148 -0.10878 -0.06227 -0.11443 179 PRO A N   
1259 C CA  . PRO A 172 ? 0.66001 0.68360 0.59485 -0.09544 -0.06450 -0.10093 179 PRO A CA  
1260 C C   . PRO A 172 ? 0.70459 0.74407 0.66069 -0.08959 -0.06572 -0.08292 179 PRO A C   
1261 O O   . PRO A 172 ? 0.63879 0.69160 0.61262 -0.09830 -0.07039 -0.08181 179 PRO A O   
1262 C CB  . PRO A 172 ? 0.64412 0.69419 0.56378 -0.10186 -0.07611 -0.10878 179 PRO A CB  
1263 C CG  . PRO A 172 ? 0.64524 0.68303 0.55929 -0.11858 -0.07847 -0.13080 179 PRO A CG  
1264 C CD  . PRO A 172 ? 0.61466 0.62827 0.54870 -0.12494 -0.07191 -0.13089 179 PRO A CD  
1265 N N   . MET A 173 ? 0.53087 0.56943 0.48533 -0.07517 -0.06090 -0.06956 180 MET A N   
1266 C CA  . MET A 173 ? 0.61299 0.65976 0.58572 -0.06755 -0.05958 -0.05424 180 MET A CA  
1267 C C   . MET A 173 ? 0.55436 0.62898 0.52887 -0.06056 -0.06776 -0.04283 180 MET A C   
1268 O O   . MET A 173 ? 0.77220 0.85655 0.76377 -0.05477 -0.06777 -0.03229 180 MET A O   
1269 C CB  . MET A 173 ? 0.55852 0.58457 0.53034 -0.05658 -0.04897 -0.04715 180 MET A CB  
1270 C CG  . MET A 173 ? 0.73788 0.74409 0.72109 -0.05866 -0.04150 -0.04850 180 MET A CG  
1271 S SD  . MET A 173 ? 0.91185 0.90558 0.89591 -0.04502 -0.03237 -0.03821 180 MET A SD  
1272 C CE  . MET A 173 ? 0.50365 0.49006 0.46650 -0.04121 -0.02941 -0.04445 180 MET A CE  
1273 N N   . GLY A 174 ? 0.50712 0.59395 0.46359 -0.05945 -0.07408 -0.04393 181 GLY A N   
1274 C CA  . GLY A 174 ? 0.53062 0.64067 0.48704 -0.05022 -0.08155 -0.03022 181 GLY A CA  
1275 C C   . GLY A 174 ? 0.53661 0.63254 0.48578 -0.03709 -0.07427 -0.01707 181 GLY A C   
1276 O O   . GLY A 174 ? 0.49018 0.58902 0.41988 -0.03295 -0.07576 -0.01224 181 GLY A O   
1277 N N   . ARG A 175 ? 0.38121 0.46205 0.34495 -0.03173 -0.06613 -0.01151 182 ARG A N   
1278 C CA  . ARG A 175 ? 0.42032 0.48550 0.38014 -0.02176 -0.05852 -0.00095 182 ARG A CA  
1279 C C   . ARG A 175 ? 0.40402 0.45569 0.38141 -0.01947 -0.05095 -0.00006 182 ARG A C   
1280 O O   . ARG A 175 ? 0.44059 0.50240 0.43522 -0.02015 -0.05333 0.00019  182 ARG A O   
1281 C CB  . ARG A 175 ? 0.34700 0.42376 0.30445 -0.01143 -0.06398 0.01434  182 ARG A CB  
1282 C CG  . ARG A 175 ? 0.34772 0.40488 0.29784 -0.00398 -0.05581 0.02469  182 ARG A CG  
1283 C CD  . ARG A 175 ? 0.45082 0.51152 0.40565 0.00778  -0.05945 0.04060  182 ARG A CD  
1284 N NE  . ARG A 175 ? 0.37977 0.44544 0.35777 0.01283  -0.06026 0.04099  182 ARG A NE  
1285 C CZ  . ARG A 175 ? 0.34126 0.43078 0.33119 0.01731  -0.06920 0.04398  182 ARG A CZ  
1286 N NH1 . ARG A 175 ? 0.38984 0.50119 0.37071 0.01746  -0.07976 0.04732  182 ARG A NH1 
1287 N NH2 . ARG A 175 ? 0.34469 0.43938 0.35621 0.02187  -0.06755 0.04338  182 ARG A NH2 
1288 N N   . GLY A 176 ? 0.31547 0.34734 0.28837 -0.01711 -0.04181 0.00028  183 GLY A N   
1289 C CA  . GLY A 176 ? 0.33149 0.35257 0.31826 -0.01434 -0.03543 0.00159  183 GLY A CA  
1290 C C   . GLY A 176 ? 0.41272 0.41778 0.39673 -0.01780 -0.02801 -0.00608 183 GLY A C   
1291 O O   . GLY A 176 ? 0.33266 0.33234 0.30374 -0.01987 -0.02570 -0.01116 183 GLY A O   
1292 N N   . THR A 177 ? 0.37922 0.37814 0.37526 -0.01721 -0.02400 -0.00647 184 THR A N   
1293 C CA  . THR A 177 ? 0.33620 0.32120 0.33136 -0.01776 -0.01747 -0.01108 184 THR A CA  
1294 C C   . THR A 177 ? 0.38786 0.37049 0.39369 -0.02111 -0.01656 -0.01310 184 THR A C   
1295 O O   . THR A 177 ? 0.38972 0.38116 0.40616 -0.02056 -0.01781 -0.00889 184 THR A O   
1296 C CB  . THR A 177 ? 0.41372 0.39284 0.40951 -0.01215 -0.01222 -0.00637 184 THR A CB  
1297 O OG1 . THR A 177 ? 0.42151 0.40125 0.40662 -0.01105 -0.01167 -0.00365 184 THR A OG1 
1298 C CG2 . THR A 177 ? 0.39673 0.36679 0.39395 -0.01149 -0.00677 -0.01042 184 THR A CG2 
1299 N N   . LYS A 178 ? 0.37948 0.34994 0.38215 -0.02408 -0.01373 -0.01911 185 LYS A N   
1300 C CA  . LYS A 178 ? 0.29809 0.26125 0.30823 -0.02763 -0.01161 -0.01941 185 LYS A CA  
1301 C C   . LYS A 178 ? 0.43535 0.38484 0.44312 -0.02200 -0.00596 -0.01918 185 LYS A C   
1302 O O   . LYS A 178 ? 0.41954 0.35996 0.41973 -0.01987 -0.00406 -0.02465 185 LYS A O   
1303 C CB  . LYS A 178 ? 0.43514 0.39401 0.44381 -0.03735 -0.01457 -0.02666 185 LYS A CB  
1304 C CG  . LYS A 178 ? 0.75703 0.69964 0.76952 -0.04178 -0.01084 -0.02735 185 LYS A CG  
1305 C CD  . LYS A 178 ? 0.67065 0.61136 0.68535 -0.05502 -0.01434 -0.03398 185 LYS A CD  
1306 C CE  . LYS A 178 ? 0.76851 0.71832 0.77472 -0.05874 -0.02050 -0.04290 185 LYS A CE  
1307 N NZ  . LYS A 178 ? 0.84597 0.80672 0.85841 -0.07267 -0.02645 -0.04799 185 LYS A NZ  
1308 N N   . VAL A 179 ? 0.32060 0.27118 0.33463 -0.01868 -0.00335 -0.01317 186 VAL A N   
1309 C CA  . VAL A 179 ? 0.37110 0.31315 0.38382 -0.01264 0.00059  -0.01163 186 VAL A CA  
1310 C C   . VAL A 179 ? 0.42641 0.35722 0.44139 -0.01529 0.00240  -0.00873 186 VAL A C   
1311 O O   . VAL A 179 ? 0.40257 0.33933 0.42287 -0.01860 0.00286  -0.00343 186 VAL A O   
1312 C CB  . VAL A 179 ? 0.37889 0.33061 0.39444 -0.00741 0.00174  -0.00733 186 VAL A CB  
1313 C CG1 . VAL A 179 ? 0.34933 0.29710 0.36421 -0.00136 0.00429  -0.00555 186 VAL A CG1 
1314 C CG2 . VAL A 179 ? 0.39169 0.35030 0.40484 -0.00625 0.00076  -0.00890 186 VAL A CG2 
1315 N N   . ILE A 180 ? 0.38092 0.29484 0.39162 -0.01346 0.00421  -0.01182 187 ILE A N   
1316 C CA  . ILE A 180 ? 0.41095 0.30772 0.42222 -0.01573 0.00651  -0.00795 187 ILE A CA  
1317 C C   . ILE A 180 ? 0.41324 0.30629 0.42342 -0.00494 0.00901  -0.00123 187 ILE A C   
1318 O O   . ILE A 180 ? 0.44964 0.33903 0.45741 0.00388  0.00992  -0.00461 187 ILE A O   
1319 C CB  . ILE A 180 ? 0.51883 0.39490 0.52562 -0.02014 0.00687  -0.01636 187 ILE A CB  
1320 C CG1 . ILE A 180 ? 0.43106 0.31651 0.43731 -0.03020 0.00270  -0.02458 187 ILE A CG1 
1321 C CG2 . ILE A 180 ? 0.42805 0.28171 0.43571 -0.02467 0.00971  -0.01127 187 ILE A CG2 
1322 C CD1 . ILE A 180 ? 0.59300 0.46090 0.59160 -0.03387 0.00256  -0.03680 187 ILE A CD1 
1323 N N   . LEU A 181 ? 0.35053 0.24772 0.36249 -0.00519 0.01011  0.00828  188 LEU A N   
1324 C CA  . LEU A 181 ? 0.48625 0.38332 0.49589 0.00486  0.01121  0.01606  188 LEU A CA  
1325 C C   . LEU A 181 ? 0.40812 0.28078 0.41458 0.00568  0.01386  0.02316  188 LEU A C   
1326 O O   . LEU A 181 ? 0.48524 0.35209 0.49166 -0.00272 0.01590  0.02996  188 LEU A O   
1327 C CB  . LEU A 181 ? 0.31163 0.22812 0.32184 0.00464  0.01096  0.02205  188 LEU A CB  
1328 C CG  . LEU A 181 ? 0.37942 0.31512 0.39288 0.00303  0.00906  0.01568  188 LEU A CG  
1329 C CD1 . LEU A 181 ? 0.45282 0.40306 0.46601 0.00216  0.01003  0.02006  188 LEU A CD1 
1330 C CD2 . LEU A 181 ? 0.35062 0.29313 0.36412 0.00999  0.00738  0.01050  188 LEU A CD2 
1331 N N   . HIS A 182 ? 0.40335 0.26173 0.40767 0.01615  0.01447  0.02225  189 HIS A N   
1332 C CA  . HIS A 182 ? 0.50835 0.33972 0.50903 0.02034  0.01715  0.03076  189 HIS A CA  
1333 C C   . HIS A 182 ? 0.56115 0.40320 0.55900 0.02973  0.01636  0.04469  189 HIS A C   
1334 O O   . HIS A 182 ? 0.49054 0.34483 0.48930 0.04290  0.01408  0.04528  189 HIS A O   
1335 C CB  . HIS A 182 ? 0.52983 0.34133 0.52981 0.02987  0.01847  0.02290  189 HIS A CB  
1336 C CG  . HIS A 182 ? 0.55557 0.36262 0.55564 0.02126  0.01860  0.00736  189 HIS A CG  
1337 N ND1 . HIS A 182 ? 0.52295 0.30254 0.52034 0.01168  0.02051  0.00149  189 HIS A ND1 
1338 C CD2 . HIS A 182 ? 0.55278 0.38023 0.55405 0.01972  0.01678  -0.00312 189 HIS A CD2 
1339 C CE1 . HIS A 182 ? 0.57709 0.36279 0.57332 0.00537  0.01913  -0.01280 189 HIS A CE1 
1340 N NE2 . HIS A 182 ? 0.53728 0.35163 0.53535 0.01055  0.01710  -0.01470 189 HIS A NE2 
1341 N N   . LEU A 183 ? 0.45029 0.29154 0.44468 0.02243  0.01817  0.05578  190 LEU A N   
1342 C CA  . LEU A 183 ? 0.54388 0.40494 0.53348 0.02858  0.01679  0.06677  190 LEU A CA  
1343 C C   . LEU A 183 ? 0.52783 0.37603 0.51155 0.04305  0.01622  0.07973  190 LEU A C   
1344 O O   . LEU A 183 ? 0.48712 0.30370 0.46908 0.04553  0.01900  0.08480  190 LEU A O   
1345 C CB  . LEU A 183 ? 0.44226 0.31040 0.42896 0.01631  0.02009  0.07419  190 LEU A CB  
1346 C CG  . LEU A 183 ? 0.43049 0.31879 0.42377 0.00512  0.02018  0.06370  190 LEU A CG  
1347 C CD1 . LEU A 183 ? 0.45219 0.35003 0.44357 -0.00453 0.02470  0.07204  190 LEU A CD1 
1348 C CD2 . LEU A 183 ? 0.36033 0.27397 0.35551 0.01146  0.01604  0.05475  190 LEU A CD2 
1349 N N   . LYS A 184 ? 0.49297 0.36586 0.47352 0.05294  0.01221  0.08496  191 LYS A N   
1350 C CA  . LYS A 184 ? 0.55799 0.42460 0.53206 0.06769  0.01043  0.10008  191 LYS A CA  
1351 C C   . LYS A 184 ? 0.55966 0.40720 0.52314 0.06188  0.01490  0.11739  191 LYS A C   
1352 O O   . LYS A 184 ? 0.50753 0.35989 0.46877 0.04697  0.01867  0.11778  191 LYS A O   
1353 C CB  . LYS A 184 ? 0.57747 0.48028 0.54981 0.07723  0.00402  0.10143  191 LYS A CB  
1354 C CG  . LYS A 184 ? 0.51251 0.43613 0.49630 0.08275  -0.00002 0.08641  191 LYS A CG  
1355 C CD  . LYS A 184 ? 0.47104 0.43272 0.45361 0.08587  -0.00627 0.08523  191 LYS A CD  
1356 C CE  . LYS A 184 ? 0.71051 0.69338 0.70585 0.08743  -0.00917 0.07022  191 LYS A CE  
1357 N NZ  . LYS A 184 ? 0.51438 0.53359 0.50977 0.08599  -0.01513 0.06574  191 LYS A NZ  
1358 N N   . GLU A 185 ? 0.56120 0.38770 0.51860 0.07454  0.01489  0.13271  192 GLU A N   
1359 C CA  . GLU A 185 ? 0.72354 0.52540 0.67003 0.06923  0.02014  0.15173  192 GLU A CA  
1360 C C   . GLU A 185 ? 0.73364 0.56338 0.66906 0.06277  0.02061  0.16177  192 GLU A C   
1361 O O   . GLU A 185 ? 0.66740 0.48730 0.59734 0.04870  0.02730  0.17041  192 GLU A O   
1362 C CB  . GLU A 185 ? 0.68795 0.46338 0.62904 0.08782  0.01909  0.16795  192 GLU A CB  
1363 C CG  . GLU A 185 ? 0.97595 0.70919 0.90832 0.08133  0.02622  0.18562  192 GLU A CG  
1364 C CD  . GLU A 185 ? 1.20859 0.90589 1.13868 0.10107  0.02581  0.19777  192 GLU A CD  
1365 O OE1 . GLU A 185 ? 1.18795 0.88151 1.10572 0.11281  0.02454  0.22088  192 GLU A OE1 
1366 O OE2 . GLU A 185 ? 1.14424 0.81722 1.08409 0.10582  0.02691  0.18426  192 GLU A OE2 
1367 N N   . ASP A 186 ? 0.53540 0.40130 0.46732 0.07211  0.01403  0.16008  193 ASP A N   
1368 C CA  . ASP A 186 ? 0.64328 0.53644 0.56201 0.06755  0.01439  0.16801  193 ASP A CA  
1369 C C   . ASP A 186 ? 0.61271 0.53119 0.53685 0.05368  0.01613  0.15053  193 ASP A C   
1370 O O   . ASP A 186 ? 0.55186 0.49835 0.46614 0.05187  0.01563  0.15130  193 ASP A O   
1371 C CB  . ASP A 186 ? 0.55108 0.47077 0.46065 0.08430  0.00579  0.17564  193 ASP A CB  
1372 C CG  . ASP A 186 ? 0.79147 0.73397 0.71408 0.09255  -0.00214 0.15802  193 ASP A CG  
1373 O OD1 . ASP A 186 ? 0.79555 0.72959 0.73288 0.08726  -0.00057 0.14170  193 ASP A OD1 
1374 O OD2 . ASP A 186 ? 0.98054 0.95158 0.89832 0.10373  -0.01008 0.16093  193 ASP A OD2 
1375 N N   . GLN A 187 ? 0.46970 0.37860 0.40820 0.04462  0.01822  0.13492  194 GLN A N   
1376 C CA  . GLN A 187 ? 0.42498 0.35571 0.36988 0.03392  0.01942  0.11916  194 GLN A CA  
1377 C C   . GLN A 187 ? 0.42481 0.34267 0.37651 0.01805  0.02664  0.11706  194 GLN A C   
1378 O O   . GLN A 187 ? 0.45051 0.37972 0.41211 0.01096  0.02683  0.10253  194 GLN A O   
1379 C CB  . GLN A 187 ? 0.49208 0.43265 0.44857 0.03806  0.01377  0.10118  194 GLN A CB  
1380 C CG  . GLN A 187 ? 0.44538 0.40396 0.39961 0.05183  0.00624  0.10059  194 GLN A CG  
1381 C CD  . GLN A 187 ? 0.51723 0.50546 0.45996 0.05275  0.00373  0.10245  194 GLN A CD  
1382 O OE1 . GLN A 187 ? 0.48615 0.48689 0.42685 0.04346  0.00702  0.09538  194 GLN A OE1 
1383 N NE2 . GLN A 187 ? 0.50840 0.50928 0.44342 0.06482  -0.00236 0.11128  194 GLN A NE2 
1384 N N   . THR A 188 ? 0.47310 0.36828 0.42038 0.01191  0.03245  0.13170  195 THR A N   
1385 C CA  . THR A 188 ? 0.55671 0.44309 0.51301 -0.00519 0.03883  0.12878  195 THR A CA  
1386 C C   . THR A 188 ? 0.54241 0.45889 0.49903 -0.01435 0.04372  0.12685  195 THR A C   
1387 O O   . THR A 188 ? 0.50503 0.42268 0.47218 -0.02819 0.04848  0.12300  195 THR A O   
1388 C CB  . THR A 188 ? 0.55835 0.41108 0.51079 -0.01215 0.04461  0.14477  195 THR A CB  
1389 O OG1 . THR A 188 ? 0.61671 0.47277 0.55315 -0.00836 0.04802  0.16491  195 THR A OG1 
1390 C CG2 . THR A 188 ? 0.70109 0.51933 0.65555 -0.00347 0.04103  0.14344  195 THR A CG2 
1391 N N   . GLU A 189 ? 0.50959 0.45195 0.45545 -0.00685 0.04269  0.12839  196 GLU A N   
1392 C CA  . GLU A 189 ? 0.43261 0.40363 0.37870 -0.01362 0.04818  0.12395  196 GLU A CA  
1393 C C   . GLU A 189 ? 0.41147 0.39312 0.37461 -0.01813 0.04681  0.10514  196 GLU A C   
1394 O O   . GLU A 189 ? 0.44866 0.44754 0.41868 -0.02623 0.05274  0.10187  196 GLU A O   
1395 C CB  . GLU A 189 ? 0.48078 0.47665 0.41105 -0.00383 0.04617  0.12458  196 GLU A CB  
1396 C CG  . GLU A 189 ? 0.51498 0.52202 0.44811 0.00575  0.03735  0.10818  196 GLU A CG  
1397 C CD  . GLU A 189 ? 0.74022 0.77177 0.65682 0.01346  0.03466  0.10774  196 GLU A CD  
1398 O OE1 . GLU A 189 ? 0.60263 0.65585 0.51658 0.01088  0.03830  0.09800  196 GLU A OE1 
1399 O OE2 . GLU A 189 ? 0.72315 0.75302 0.62942 0.02262  0.02871  0.11658  196 GLU A OE2 
1400 N N   . TYR A 190 ? 0.39911 0.37204 0.36943 -0.01250 0.03944  0.09363  197 TYR A N   
1401 C CA  . TYR A 190 ? 0.48209 0.46353 0.46648 -0.01557 0.03746  0.07784  197 TYR A CA  
1402 C C   . TYR A 190 ? 0.53542 0.50411 0.53277 -0.02712 0.03916  0.07645  197 TYR A C   
1403 O O   . TYR A 190 ? 0.40221 0.37604 0.41063 -0.02904 0.03613  0.06472  197 TYR A O   
1404 C CB  . TYR A 190 ? 0.44230 0.42179 0.42761 -0.00607 0.02970  0.06710  197 TYR A CB  
1405 C CG  . TYR A 190 ? 0.33641 0.33179 0.31041 0.00294  0.02723  0.06666  197 TYR A CG  
1406 C CD1 . TYR A 190 ? 0.38790 0.40505 0.35946 0.00291  0.02950  0.05960  197 TYR A CD1 
1407 C CD2 . TYR A 190 ? 0.42642 0.41619 0.39223 0.01170  0.02259  0.07286  197 TYR A CD2 
1408 C CE1 . TYR A 190 ? 0.42599 0.45801 0.38582 0.00944  0.02689  0.05719  197 TYR A CE1 
1409 C CE2 . TYR A 190 ? 0.48360 0.49206 0.43917 0.01873  0.01911  0.07186  197 TYR A CE2 
1410 C CZ  . TYR A 190 ? 0.52965 0.55869 0.48153 0.01653  0.02117  0.06335  197 TYR A CZ  
1411 O OH  . TYR A 190 ? 0.49509 0.54277 0.43561 0.02190  0.01731  0.06016  197 TYR A OH  
1412 N N   . LEU A 191 ? 0.45207 0.40433 0.44767 -0.03545 0.04370  0.08837  198 LEU A N   
1413 C CA  . LEU A 191 ? 0.51789 0.46308 0.52601 -0.05026 0.04641  0.08709  198 LEU A CA  
1414 C C   . LEU A 191 ? 0.53871 0.50502 0.55180 -0.06147 0.05482  0.09374  198 LEU A C   
1415 O O   . LEU A 191 ? 0.65596 0.62171 0.68142 -0.07592 0.05747  0.09327  198 LEU A O   
1416 C CB  . LEU A 191 ? 0.45680 0.36570 0.46161 -0.05484 0.04661  0.09428  198 LEU A CB  
1417 C CG  . LEU A 191 ? 0.50583 0.39284 0.50585 -0.04264 0.03998  0.08880  198 LEU A CG  
1418 C CD1 . LEU A 191 ? 0.70238 0.55139 0.69727 -0.04482 0.04207  0.09797  198 LEU A CD1 
1419 C CD2 . LEU A 191 ? 0.51590 0.40803 0.52594 -0.04350 0.03442  0.07154  198 LEU A CD2 
1420 N N   . GLU A 192 ? 0.45321 0.43970 0.45691 -0.05588 0.05936  0.09948  199 GLU A N   
1421 C CA  . GLU A 192 ? 0.57589 0.58654 0.58357 -0.06527 0.06898  0.10557  199 GLU A CA  
1422 C C   . GLU A 192 ? 0.45053 0.49196 0.47266 -0.06350 0.06893  0.09142  199 GLU A C   
1423 O O   . GLU A 192 ? 0.39941 0.44807 0.41915 -0.05109 0.06381  0.08049  199 GLU A O   
1424 C CB  . GLU A 192 ? 0.56674 0.58650 0.55505 -0.05954 0.07473  0.11795  199 GLU A CB  
1425 C CG  . GLU A 192 ? 0.65794 0.64851 0.63016 -0.05836 0.07464  0.13514  199 GLU A CG  
1426 C CD  . GLU A 192 ? 0.94063 0.91015 0.91864 -0.07516 0.08098  0.14767  199 GLU A CD  
1427 O OE1 . GLU A 192 ? 0.95153 0.93930 0.94283 -0.08939 0.08817  0.14697  199 GLU A OE1 
1428 O OE2 . GLU A 192 ? 1.02252 0.95731 0.99269 -0.07423 0.07903  0.15805  199 GLU A OE2 
1429 N N   . GLU A 193 ? 0.45252 0.51223 0.49048 -0.07603 0.07491  0.09219  200 GLU A N   
1430 C CA  . GLU A 193 ? 0.51568 0.60586 0.57029 -0.07319 0.07484  0.07998  200 GLU A CA  
1431 C C   . GLU A 193 ? 0.45551 0.56889 0.50177 -0.06043 0.07963  0.07610  200 GLU A C   
1432 O O   . GLU A 193 ? 0.47099 0.59270 0.52112 -0.04900 0.07526  0.06346  200 GLU A O   
1433 C CB  . GLU A 193 ? 0.48302 0.59334 0.55767 -0.08955 0.08079  0.08297  200 GLU A CB  
1434 C CG  . GLU A 193 ? 0.67030 0.82061 0.76241 -0.08485 0.08393  0.07408  200 GLU A CG  
1435 C CD  . GLU A 193 ? 0.80102 0.97473 0.91783 -0.10108 0.08678  0.07488  200 GLU A CD  
1436 O OE1 . GLU A 193 ? 0.86438 1.02701 0.98262 -0.11899 0.09063  0.08473  200 GLU A OE1 
1437 O OE2 . GLU A 193 ? 0.92102 1.12462 1.05648 -0.09593 0.08509  0.06587  200 GLU A OE2 
1438 N N   . ARG A 194 ? 0.46721 0.58990 0.50052 -0.06237 0.08895  0.08671  201 ARG A N   
1439 C CA  . ARG A 194 ? 0.39906 0.54524 0.42286 -0.05099 0.09420  0.08085  201 ARG A CA  
1440 C C   . ARG A 194 ? 0.37584 0.50707 0.38280 -0.03711 0.08594  0.07334  201 ARG A C   
1441 O O   . ARG A 194 ? 0.44383 0.58922 0.44794 -0.02663 0.08647  0.06115  201 ARG A O   
1442 C CB  . ARG A 194 ? 0.41198 0.57412 0.42341 -0.05709 0.10663  0.09441  201 ARG A CB  
1443 C CG  . ARG A 194 ? 0.68827 0.82452 0.68076 -0.06241 0.10616  0.11206  201 ARG A CG  
1444 C CD  . ARG A 194 ? 0.67730 0.83061 0.65989 -0.07150 0.11985  0.12814  201 ARG A CD  
1445 N NE  . ARG A 194 ? 0.71429 0.84440 0.67290 -0.07158 0.11921  0.14605  201 ARG A NE  
1446 C CZ  . ARG A 194 ? 0.89374 1.03614 0.83295 -0.07403 0.12904  0.16120  201 ARG A CZ  
1447 N NH1 . ARG A 194 ? 0.76713 0.94575 0.70807 -0.07765 0.14162  0.15989  201 ARG A NH1 
1448 N NH2 . ARG A 194 ? 0.87802 0.99723 0.79506 -0.07168 0.12645  0.17851  201 ARG A NH2 
1449 N N   . ARG A 195 ? 0.44630 0.54941 0.44326 -0.03690 0.07847  0.07955  202 ARG A N   
1450 C CA  . ARG A 195 ? 0.43271 0.52512 0.41763 -0.02505 0.06991  0.07189  202 ARG A CA  
1451 C C   . ARG A 195 ? 0.50480 0.59370 0.50348 -0.01987 0.06281  0.05629  202 ARG A C   
1452 O O   . ARG A 195 ? 0.35018 0.44559 0.34480 -0.01092 0.06064  0.04462  202 ARG A O   
1453 C CB  . ARG A 195 ? 0.41471 0.48107 0.38857 -0.02489 0.06421  0.08313  202 ARG A CB  
1454 C CG  . ARG A 195 ? 0.41589 0.47645 0.37855 -0.01350 0.05554  0.07681  202 ARG A CG  
1455 C CD  . ARG A 195 ? 0.42187 0.50274 0.36616 -0.00738 0.05806  0.07609  202 ARG A CD  
1456 N NE  . ARG A 195 ? 0.45621 0.53370 0.39047 0.00149  0.04884  0.07108  202 ARG A NE  
1457 C CZ  . ARG A 195 ? 0.54093 0.63025 0.47250 0.00679  0.04558  0.05541  202 ARG A CZ  
1458 N NH1 . ARG A 195 ? 0.39395 0.49635 0.33075 0.00642  0.05099  0.04309  202 ARG A NH1 
1459 N NH2 . ARG A 195 ? 0.43644 0.52444 0.36085 0.01260  0.03686  0.05173  202 ARG A NH2 
1460 N N   . ILE A 196 ? 0.34490 0.42273 0.35882 -0.02605 0.05920  0.05594  203 ILE A N   
1461 C CA  . ILE A 196 ? 0.35189 0.42652 0.37717 -0.02139 0.05246  0.04361  203 ILE A CA  
1462 C C   . ILE A 196 ? 0.35996 0.45756 0.39436 -0.01582 0.05648  0.03421  203 ILE A C   
1463 O O   . ILE A 196 ? 0.33440 0.42954 0.36917 -0.00701 0.05254  0.02369  203 ILE A O   
1464 C CB  . ILE A 196 ? 0.39960 0.46218 0.43772 -0.03007 0.04825  0.04514  203 ILE A CB  
1465 C CG1 . ILE A 196 ? 0.37730 0.41282 0.40593 -0.03263 0.04438  0.05185  203 ILE A CG1 
1466 C CG2 . ILE A 196 ? 0.32526 0.38788 0.37340 -0.02505 0.04156  0.03412  203 ILE A CG2 
1467 C CD1 . ILE A 196 ? 0.46140 0.48378 0.49974 -0.04395 0.04268  0.05394  203 ILE A CD1 
1468 N N   . LYS A 197 ? 0.29964 0.41946 0.34243 -0.02071 0.06497  0.03805  204 LYS A N   
1469 C CA  . LYS A 197 ? 0.39407 0.53798 0.44667 -0.01311 0.07010  0.02907  204 LYS A CA  
1470 C C   . LYS A 197 ? 0.41362 0.55848 0.45031 -0.00207 0.07224  0.02048  204 LYS A C   
1471 O O   . LYS A 197 ? 0.38179 0.52760 0.42275 0.00790  0.07087  0.00863  204 LYS A O   
1472 C CB  . LYS A 197 ? 0.30369 0.47559 0.36692 -0.02046 0.08063  0.03545  204 LYS A CB  
1473 C CG  . LYS A 197 ? 0.48652 0.66801 0.57219 -0.03073 0.07897  0.03892  204 LYS A CG  
1474 C CD  . LYS A 197 ? 0.53276 0.74890 0.63104 -0.03714 0.09083  0.04357  204 LYS A CD  
1475 C CE  . LYS A 197 ? 0.59961 0.82904 0.72124 -0.05114 0.08922  0.04763  204 LYS A CE  
1476 N NZ  . LYS A 197 ? 0.65794 0.92111 0.79098 -0.06109 0.10210  0.05458  204 LYS A NZ  
1477 N N   . GLU A 198 ? 0.38761 0.53183 0.40513 -0.00397 0.07552  0.02647  205 GLU A N   
1478 C CA  . GLU A 198 ? 0.43597 0.58272 0.43576 0.00461  0.07652  0.01745  205 GLU A CA  
1479 C C   . GLU A 198 ? 0.41878 0.54543 0.41653 0.01072  0.06670  0.00668  205 GLU A C   
1480 O O   . GLU A 198 ? 0.38417 0.51255 0.37864 0.01849  0.06745  -0.00699 205 GLU A O   
1481 C CB  . GLU A 198 ? 0.35213 0.49982 0.33052 0.00082  0.07849  0.02849  205 GLU A CB  
1482 C CG  . GLU A 198 ? 0.40203 0.55751 0.35972 0.00797  0.07918  0.01934  205 GLU A CG  
1483 C CD  . GLU A 198 ? 0.62211 0.77843 0.55788 0.00508  0.07855  0.03284  205 GLU A CD  
1484 O OE1 . GLU A 198 ? 0.53670 0.67579 0.47331 0.00077  0.07292  0.04588  205 GLU A OE1 
1485 O OE2 . GLU A 198 ? 0.53783 0.71197 0.45490 0.00783  0.08385  0.03067  205 GLU A OE2 
1486 N N   . ILE A 199 ? 0.37664 0.48353 0.37646 0.00682  0.05822  0.01224  206 ILE A N   
1487 C CA  . ILE A 199 ? 0.37923 0.46921 0.37649 0.01084  0.04975  0.00386  206 ILE A CA  
1488 C C   . ILE A 199 ? 0.46542 0.55076 0.47716 0.01527  0.04817  -0.00557 206 ILE A C   
1489 O O   . ILE A 199 ? 0.39888 0.47632 0.40759 0.02040  0.04579  -0.01646 206 ILE A O   
1490 C CB  . ILE A 199 ? 0.32358 0.39667 0.31926 0.00644  0.04266  0.01278  206 ILE A CB  
1491 C CG1 . ILE A 199 ? 0.44708 0.52305 0.42718 0.00484  0.04371  0.02338  206 ILE A CG1 
1492 C CG2 . ILE A 199 ? 0.34854 0.40786 0.34428 0.00953  0.03495  0.00457  206 ILE A CG2 
1493 C CD1 . ILE A 199 ? 0.38733 0.44577 0.36663 0.00291  0.03775  0.03256  206 ILE A CD1 
1494 N N   . VAL A 200 ? 0.35817 0.44798 0.38569 0.01291  0.04902  -0.00100 207 VAL A N   
1495 C CA  . VAL A 200 ? 0.27300 0.36099 0.31416 0.01868  0.04700  -0.00745 207 VAL A CA  
1496 C C   . VAL A 200 ? 0.31863 0.41791 0.36077 0.02835  0.05374  -0.01757 207 VAL A C   
1497 O O   . VAL A 200 ? 0.38274 0.47040 0.42621 0.03586  0.05184  -0.02647 207 VAL A O   
1498 C CB  . VAL A 200 ? 0.31581 0.41236 0.37357 0.01370  0.04575  -0.00032 207 VAL A CB  
1499 C CG1 . VAL A 200 ? 0.33131 0.43338 0.40359 0.02213  0.04430  -0.00540 207 VAL A CG1 
1500 C CG2 . VAL A 200 ? 0.28277 0.36228 0.33855 0.00558  0.03840  0.00581  207 VAL A CG2 
1501 N N   . LYS A 201 ? 0.34217 0.46301 0.38295 0.02829  0.06255  -0.01637 208 LYS A N   
1502 C CA  . LYS A 201 ? 0.35825 0.49177 0.39870 0.03844  0.07064  -0.02746 208 LYS A CA  
1503 C C   . LYS A 201 ? 0.40557 0.52353 0.42864 0.04271  0.06930  -0.03985 208 LYS A C   
1504 O O   . LYS A 201 ? 0.52078 0.63146 0.54601 0.05217  0.07118  -0.05222 208 LYS A O   
1505 C CB  . LYS A 201 ? 0.46022 0.62175 0.49893 0.03568  0.08128  -0.02291 208 LYS A CB  
1506 C CG  . LYS A 201 ? 0.44733 0.62926 0.49211 0.04713  0.09163  -0.03360 208 LYS A CG  
1507 C CD  . LYS A 201 ? 0.87599 1.07923 0.94698 0.04926  0.09441  -0.02867 208 LYS A CD  
1508 C CE  . LYS A 201 ? 0.94387 1.14873 1.02789 0.06614  0.09649  -0.04059 208 LYS A CE  
1509 N NZ  . LYS A 201 ? 0.68928 0.90577 0.79924 0.06857  0.09205  -0.03413 208 LYS A NZ  
1510 N N   . LYS A 202 ? 0.45805 0.57050 0.46434 0.03582  0.06572  -0.03685 209 LYS A N   
1511 C CA  . LYS A 202 ? 0.44609 0.54873 0.43602 0.03756  0.06347  -0.04915 209 LYS A CA  
1512 C C   . LYS A 202 ? 0.48759 0.56509 0.48268 0.03852  0.05591  -0.05580 209 LYS A C   
1513 O O   . LYS A 202 ? 0.39237 0.45950 0.38348 0.04312  0.05705  -0.07014 209 LYS A O   
1514 C CB  . LYS A 202 ? 0.43909 0.54656 0.41183 0.03053  0.06012  -0.04183 209 LYS A CB  
1515 C CG  . LYS A 202 ? 0.52330 0.62886 0.47799 0.03066  0.05701  -0.05404 209 LYS A CG  
1516 C CD  . LYS A 202 ? 0.68398 0.79725 0.62424 0.02531  0.05218  -0.04286 209 LYS A CD  
1517 C CE  . LYS A 202 ? 0.66287 0.78191 0.58426 0.02482  0.04810  -0.05451 209 LYS A CE  
1518 N NZ  . LYS A 202 ? 0.84141 0.97407 0.74738 0.02235  0.04448  -0.04113 209 LYS A NZ  
1519 N N   . HIS A 203 ? 0.41982 0.48638 0.42345 0.03381  0.04897  -0.04583 210 HIS A N   
1520 C CA  . HIS A 203 ? 0.43524 0.48027 0.43987 0.03181  0.04179  -0.04939 210 HIS A CA  
1521 C C   . HIS A 203 ? 0.46501 0.49745 0.48432 0.03547  0.03985  -0.04698 210 HIS A C   
1522 O O   . HIS A 203 ? 0.46835 0.48187 0.48771 0.03476  0.03600  -0.05101 210 HIS A O   
1523 C CB  . HIS A 203 ? 0.39619 0.43867 0.39607 0.02407  0.03503  -0.04059 210 HIS A CB  
1524 C CG  . HIS A 203 ? 0.45233 0.50491 0.43670 0.02138  0.03413  -0.04239 210 HIS A CG  
1525 N ND1 . HIS A 203 ? 0.50379 0.55506 0.47826 0.02097  0.03286  -0.05563 210 HIS A ND1 
1526 C CD2 . HIS A 203 ? 0.46552 0.52952 0.44202 0.01890  0.03364  -0.03208 210 HIS A CD2 
1527 C CE1 . HIS A 203 ? 0.62721 0.69260 0.58813 0.01880  0.03091  -0.05362 210 HIS A CE1 
1528 N NE2 . HIS A 203 ? 0.65281 0.72516 0.61442 0.01835  0.03152  -0.03831 210 HIS A NE2 
1529 N N   . SER A 204 ? 0.55979 0.46081 0.36542 -0.07308 -0.08271 0.00272  211 SER A N   
1530 C CA  . SER A 204 ? 0.53371 0.44245 0.38115 -0.05516 -0.06994 -0.00153 211 SER A CA  
1531 C C   . SER A 204 ? 0.56272 0.46827 0.40078 -0.04432 -0.04620 -0.02316 211 SER A C   
1532 O O   . SER A 204 ? 0.50397 0.42226 0.37318 -0.02968 -0.03376 -0.02401 211 SER A O   
1533 C CB  . SER A 204 ? 0.57545 0.50600 0.46068 -0.04755 -0.06861 0.01745  211 SER A CB  
1534 O OG  . SER A 204 ? 0.51191 0.44792 0.41591 -0.05405 -0.08910 0.03672  211 SER A OG  
1535 N N   . GLN A 205 ? 0.56772 0.45741 0.36408 -0.05117 -0.03983 -0.04166 212 GLN A N   
1536 C CA  . GLN A 205 ? 0.64441 0.53609 0.43543 -0.04007 -0.01453 -0.06236 212 GLN A CA  
1537 C C   . GLN A 205 ? 0.64446 0.52996 0.46885 -0.02201 -0.00838 -0.07389 212 GLN A C   
1538 O O   . GLN A 205 ? 0.62095 0.51919 0.46384 -0.00767 0.01005  -0.08288 212 GLN A O   
1539 C CB  . GLN A 205 ? 0.69771 0.57270 0.43482 -0.05132 -0.00682 -0.08235 212 GLN A CB  
1540 C CG  . GLN A 205 ? 0.79634 0.64072 0.51003 -0.05986 -0.02219 -0.09500 212 GLN A CG  
1541 C CD  . GLN A 205 ? 1.08358 0.91128 0.73429 -0.07573 -0.01774 -0.11330 212 GLN A CD  
1542 O OE1 . GLN A 205 ? 1.24075 1.04737 0.85981 -0.09212 -0.03768 -0.11621 212 GLN A OE1 
1543 N NE2 . GLN A 205 ? 0.86390 0.70238 0.49528 -0.07231 0.00888  -0.12635 212 GLN A NE2 
1544 N N   . PHE A 206 ? 0.57481 0.44208 0.40960 -0.02308 -0.02447 -0.07182 213 PHE A N   
1545 C CA  . PHE A 206 ? 0.55222 0.40710 0.41323 -0.00788 -0.02066 -0.08095 213 PHE A CA  
1546 C C   . PHE A 206 ? 0.54340 0.41203 0.44652 -0.00004 -0.02810 -0.06119 213 PHE A C   
1547 O O   . PHE A 206 ? 0.53691 0.39208 0.45931 0.00878  -0.03044 -0.06278 213 PHE A O   
1548 C CB  . PHE A 206 ? 0.59787 0.41645 0.43793 -0.01555 -0.03081 -0.09544 213 PHE A CB  
1549 C CG  . PHE A 206 ? 0.65194 0.45352 0.44762 -0.02118 -0.01991 -0.12075 213 PHE A CG  
1550 C CD1 . PHE A 206 ? 0.66089 0.46917 0.45666 -0.00651 0.00500  -0.13914 213 PHE A CD1 
1551 C CD2 . PHE A 206 ? 0.69682 0.47872 0.45039 -0.04194 -0.03403 -0.12646 213 PHE A CD2 
1552 C CE1 . PHE A 206 ? 0.71514 0.50992 0.46832 -0.01173 0.01927  -0.16450 213 PHE A CE1 
1553 C CE2 . PHE A 206 ? 0.86747 0.63341 0.57303 -0.04859 -0.02240 -0.15160 213 PHE A CE2 
1554 C CZ  . PHE A 206 ? 0.83280 0.60479 0.53735 -0.03315 0.00607  -0.17146 213 PHE A CZ  
1555 N N   . ILE A 207 ? 0.50481 0.39797 0.42113 -0.00330 -0.03128 -0.04277 214 ILE A N   
1556 C CA  . ILE A 207 ? 0.43170 0.34014 0.38403 0.00472  -0.03377 -0.02751 214 ILE A CA  
1557 C C   . ILE A 207 ? 0.45410 0.37005 0.42509 0.02206  -0.02071 -0.03484 214 ILE A C   
1558 O O   . ILE A 207 ? 0.46789 0.39488 0.43497 0.02792  -0.00707 -0.04515 214 ILE A O   
1559 C CB  . ILE A 207 ? 0.40482 0.33606 0.36671 -0.00018 -0.03604 -0.01132 214 ILE A CB  
1560 C CG1 . ILE A 207 ? 0.41931 0.34515 0.37000 -0.01573 -0.05265 -0.00090 214 ILE A CG1 
1561 C CG2 . ILE A 207 ? 0.40608 0.35338 0.40084 0.00850  -0.03476 0.00003  214 ILE A CG2 
1562 C CD1 . ILE A 207 ? 0.42168 0.34174 0.39124 -0.01992 -0.06612 0.00807  214 ILE A CD1 
1563 N N   . GLY A 208 ? 0.42669 0.33834 0.41911 0.02941  -0.02552 -0.02807 215 GLY A N   
1564 C CA  . GLY A 208 ? 0.44535 0.35982 0.45509 0.04591  -0.01815 -0.03345 215 GLY A CA  
1565 C C   . GLY A 208 ? 0.47687 0.42078 0.50698 0.05299  -0.01370 -0.02445 215 GLY A C   
1566 O O   . GLY A 208 ? 0.48542 0.43319 0.53303 0.06399  -0.01492 -0.02050 215 GLY A O   
1567 N N   . TYR A 209 ? 0.41953 0.38234 0.44629 0.04605  -0.00986 -0.02099 216 TYR A N   
1568 C CA  . TYR A 209 ? 0.45194 0.44027 0.49492 0.04990  -0.00545 -0.01560 216 TYR A CA  
1569 C C   . TYR A 209 ? 0.35374 0.35542 0.38947 0.04452  0.00398  -0.02115 216 TYR A C   
1570 O O   . TYR A 209 ? 0.46797 0.45993 0.48325 0.03484  0.00408  -0.02275 216 TYR A O   
1571 C CB  . TYR A 209 ? 0.35206 0.34616 0.40277 0.04465  -0.01200 -0.00110 216 TYR A CB  
1572 C CG  . TYR A 209 ? 0.40697 0.39005 0.46341 0.04708  -0.01947 0.00693  216 TYR A CG  
1573 C CD1 . TYR A 209 ? 0.30751 0.29731 0.37422 0.05627  -0.02000 0.01031  216 TYR A CD1 
1574 C CD2 . TYR A 209 ? 0.33245 0.29850 0.38368 0.03848  -0.02732 0.01266  216 TYR A CD2 
1575 C CE1 . TYR A 209 ? 0.47632 0.45398 0.54531 0.05675  -0.02685 0.02077  216 TYR A CE1 
1576 C CE2 . TYR A 209 ? 0.34222 0.29739 0.39956 0.03821  -0.03334 0.02175  216 TYR A CE2 
1577 C CZ  . TYR A 209 ? 0.37158 0.33151 0.43644 0.04736  -0.03237 0.02647  216 TYR A CZ  
1578 O OH  . TYR A 209 ? 0.46025 0.40763 0.52835 0.04546  -0.03828 0.03844  216 TYR A OH  
1579 N N   . PRO A 210 ? 0.44247 0.46612 0.49325 0.04887  0.01103  -0.02330 217 PRO A N   
1580 C CA  . PRO A 210 ? 0.42984 0.46594 0.47546 0.04121  0.02073  -0.02649 217 PRO A CA  
1581 C C   . PRO A 210 ? 0.33259 0.36441 0.37054 0.02965  0.01564  -0.01480 217 PRO A C   
1582 O O   . PRO A 210 ? 0.38217 0.41685 0.43247 0.03038  0.00992  -0.00693 217 PRO A O   
1583 C CB  . PRO A 210 ? 0.37354 0.43488 0.44318 0.04729  0.02610  -0.02993 217 PRO A CB  
1584 C CG  . PRO A 210 ? 0.42819 0.49039 0.51210 0.05816  0.01739  -0.02714 217 PRO A CG  
1585 C CD  . PRO A 210 ? 0.37868 0.41642 0.45080 0.05945  0.00911  -0.02235 217 PRO A CD  
1586 N N   . ILE A 211 ? 0.36211 0.38643 0.37900 0.01933  0.01779  -0.01361 218 ILE A N   
1587 C CA  . ILE A 211 ? 0.35115 0.37087 0.36232 0.00877  0.01200  -0.00056 218 ILE A CA  
1588 C C   . ILE A 211 ? 0.45376 0.48437 0.46389 0.00162  0.02261  -0.00028 218 ILE A C   
1589 O O   . ILE A 211 ? 0.40321 0.43561 0.39478 -0.00391 0.03212  -0.00613 218 ILE A O   
1590 C CB  . ILE A 211 ? 0.42631 0.42853 0.41164 -0.00024 0.00254  0.00471  218 ILE A CB  
1591 C CG1 . ILE A 211 ? 0.37284 0.36401 0.36175 0.00388  -0.00850 0.00478  218 ILE A CG1 
1592 C CG2 . ILE A 211 ? 0.37695 0.37606 0.36031 -0.00993 -0.00527 0.02106  218 ILE A CG2 
1593 C CD1 . ILE A 211 ? 0.38274 0.35710 0.34588 -0.00692 -0.02021 0.00752  218 ILE A CD1 
1594 N N   . THR A 212 ? 0.37235 0.40917 0.40132 0.00042  0.02217  0.00584  219 THR A N   
1595 C CA  . THR A 212 ? 0.37443 0.42011 0.40680 -0.00817 0.03153  0.00687  219 THR A CA  
1596 C C   . THR A 212 ? 0.42486 0.45573 0.45097 -0.01835 0.02507  0.02277  219 THR A C   
1597 O O   . THR A 212 ? 0.33210 0.35538 0.37367 -0.01465 0.01655  0.02947  219 THR A O   
1598 C CB  . THR A 212 ? 0.47310 0.53507 0.53265 -0.00338 0.03518  -0.00012 219 THR A CB  
1599 O OG1 . THR A 212 ? 0.36195 0.43778 0.42950 0.00737  0.03788  -0.01163 219 THR A OG1 
1600 C CG2 . THR A 212 ? 0.31804 0.38971 0.38435 -0.01503 0.04460  0.00054  219 THR A CG2 
1601 N N   . LEU A 213 ? 0.36967 0.39654 0.37369 -0.03078 0.02966  0.02930  220 LEU A N   
1602 C CA  . LEU A 213 ? 0.49383 0.50497 0.49110 -0.04128 0.02204  0.04798  220 LEU A CA  
1603 C C   . LEU A 213 ? 0.45163 0.46609 0.46651 -0.04837 0.03025  0.05042  220 LEU A C   
1604 O O   . LEU A 213 ? 0.48251 0.50795 0.48948 -0.05822 0.04342  0.04751  220 LEU A O   
1605 C CB  . LEU A 213 ? 0.50136 0.50407 0.45925 -0.05368 0.02065  0.05668  220 LEU A CB  
1606 C CG  . LEU A 213 ? 0.57579 0.56152 0.52487 -0.06561 0.01051  0.08035  220 LEU A CG  
1607 C CD1 . LEU A 213 ? 0.42550 0.39980 0.40087 -0.05639 -0.00701 0.09110  220 LEU A CD1 
1608 C CD2 . LEU A 213 ? 0.48285 0.46053 0.38540 -0.07952 0.00660  0.09006  220 LEU A CD2 
1609 N N   . PHE A 214 ? 0.37919 0.38443 0.41925 -0.04403 0.02365  0.05444  221 PHE A N   
1610 C CA  . PHE A 214 ? 0.41317 0.41545 0.47055 -0.05211 0.02937  0.05583  221 PHE A CA  
1611 C C   . PHE A 214 ? 0.48754 0.47307 0.52922 -0.06801 0.02823  0.07597  221 PHE A C   
1612 O O   . PHE A 214 ? 0.57215 0.54044 0.60173 -0.06869 0.01599  0.09282  221 PHE A O   
1613 C CB  . PHE A 214 ? 0.38525 0.37687 0.47044 -0.04291 0.02322  0.05264  221 PHE A CB  
1614 C CG  . PHE A 214 ? 0.46250 0.47131 0.56200 -0.03221 0.02663  0.03321  221 PHE A CG  
1615 C CD1 . PHE A 214 ? 0.36132 0.38685 0.45182 -0.02412 0.02751  0.02484  221 PHE A CD1 
1616 C CD2 . PHE A 214 ? 0.47005 0.47543 0.59002 -0.03086 0.02790  0.02369  221 PHE A CD2 
1617 C CE1 . PHE A 214 ? 0.37856 0.41828 0.48033 -0.01495 0.02835  0.01095  221 PHE A CE1 
1618 C CE2 . PHE A 214 ? 0.37471 0.39599 0.50190 -0.02284 0.02923  0.00744  221 PHE A CE2 
1619 C CZ  . PHE A 214 ? 0.32906 0.36807 0.44721 -0.01489 0.02880  0.00292  221 PHE A CZ  
1620 N N   . VAL A 215 ? 0.42072 0.41249 0.46399 -0.08191 0.03998  0.07591  222 VAL A N   
1621 C CA  . VAL A 215 ? 0.45948 0.43481 0.48842 -0.10009 0.04083  0.09680  222 VAL A CA  
1622 C C   . VAL A 215 ? 0.59012 0.54138 0.64703 -0.10205 0.03439  0.10410  222 VAL A C   
1623 O O   . VAL A 215 ? 0.49650 0.45232 0.58113 -0.09620 0.03704  0.08756  222 VAL A O   
1624 C CB  . VAL A 215 ? 0.52895 0.52590 0.54650 -0.11619 0.05972  0.09316  222 VAL A CB  
1625 C CG1 . VAL A 215 ? 0.63043 0.60983 0.63029 -0.13803 0.06188  0.11746  222 VAL A CG1 
1626 C CG2 . VAL A 215 ? 0.61897 0.63702 0.61020 -0.11185 0.06817  0.08243  222 VAL A CG2 
1627 N N   . GLU A 216 ? 0.51905 0.44264 0.56794 -0.11023 0.02494  0.12864  223 GLU A N   
1628 C CA  . GLU A 216 ? 0.60273 0.49733 0.67991 -0.11118 0.01877  0.13616  223 GLU A CA  
1629 C C   . GLU A 216 ? 0.54093 0.43144 0.62277 -0.13246 0.03000  0.13961  223 GLU A C   
1630 O O   . GLU A 216 ? 0.58250 0.48605 0.64001 -0.14968 0.04008  0.14837  223 GLU A O   
1631 C CB  . GLU A 216 ? 0.66335 0.52793 0.73699 -0.10875 0.00118  0.16342  223 GLU A CB  
1632 C CG  . GLU A 216 ? 0.79857 0.66536 0.88435 -0.08708 -0.01117 0.15923  223 GLU A CG  
1633 C CD  . GLU A 216 ? 0.82622 0.66494 0.92340 -0.08225 -0.03002 0.18541  223 GLU A CD  
1634 O OE1 . GLU A 216 ? 0.76854 0.58211 0.89901 -0.07689 -0.03251 0.18777  223 GLU A OE1 
1635 O OE2 . GLU A 216 ? 0.92782 0.76926 1.00143 -0.08380 -0.04315 0.20307  223 GLU A OE2 
1636 N N   . LYS A 217 ? 0.68903 0.56149 0.80260 -0.13214 0.02924  0.13135  224 LYS A N   
1637 C CA  . LYS A 217 ? 0.64230 0.50477 0.76674 -0.15389 0.03710  0.13500  224 LYS A CA  
1638 C C   . LYS A 217 ? 0.69077 0.50941 0.81460 -0.16394 0.02733  0.16522  224 LYS A C   
1639 O O   . LYS A 217 ? 0.77831 0.59273 0.88094 -0.18489 0.03138  0.18783  224 LYS A O   
1640 C CB  . LYS A 217 ? 0.55379 0.41651 0.71060 -0.15068 0.03979  0.10824  224 LYS A CB  
1641 C CG  . LYS A 217 ? 0.58830 0.48479 0.74862 -0.13330 0.04219  0.08087  224 LYS A CG  
1642 C CD  . LYS A 217 ? 0.49963 0.39567 0.68530 -0.13355 0.04308  0.05569  224 LYS A CD  
1643 C CE  . LYS A 217 ? 0.51206 0.37570 0.71224 -0.11711 0.03515  0.04784  224 LYS A CE  
1644 N NZ  . LYS A 217 ? 0.53492 0.39758 0.72655 -0.09590 0.02900  0.05606  224 LYS A NZ  
# 
