data_7HAA
# 
_entry.id   7HAA 
# 
_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   7HAA         pdb_00007haa 10.2210/pdb7haa/pdb 
WWPDB D_1001407221 ?            ?                   
# 
_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                        7HAA 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.recvd_initial_deposition_date   2024-07-10 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.pdb_format_compatible           N 
_pdbx_database_status.methods_development_category    ? 
# 
_pdbx_contact_author.id                 1 
_pdbx_contact_author.name_last          Yu 
_pdbx_contact_author.name_first         Feng 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.email              yufeng@sari.ac.cn 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-9502-3277 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Huang, L.' 1  ? 
'Wang, W.'  2  ? 
'Zhu, Z.'   3  ? 
'Li, Q.'    4  ? 
'Li, M.'    5  ? 
'Zhou, H.'  6  ? 
'Xu, Q.'    7  ? 
'Wen, W.'   8  ? 
'Wang, Q.'  9  ? 
'Yu, F.'    10 ? 
# 
_citation.id                        primary 
_citation.title                     
;Novel starting points for fragment-based drug design against human heat-shock protein 90 identified using crystallographic fragment screening.
;
_citation.journal_abbrev            Iucrj 
_citation.journal_volume            12 
_citation.page_first                177 
_citation.page_last                 187 
_citation.year                      2025 
_citation.journal_id_ASTM           ? 
_citation.country                   UK 
_citation.journal_id_ISSN           2052-2525 
_citation.journal_id_CSD            ? 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   39819741 
_citation.pdbx_database_id_DOI      10.1107/S2052252524012247 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.identifier_ORCID 
_citation_author.ordinal 
primary 'Huang, L.' 0009-0001-8431-0182 1  
primary 'Wang, W.'  ?                   2  
primary 'Zhu, Z.'   ?                   3  
primary 'Li, Q.'    ?                   4  
primary 'Li, M.'    ?                   5  
primary 'Zhou, H.'  ?                   6  
primary 'Xu, Q.'    0000-0002-7137-0768 7  
primary 'Wen, W.'   ?                   8  
primary 'Wang, Q.'  ?                   9  
primary 'Yu, F.'    0000-0002-9502-3277 10 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Heat shock protein HSP 90-alpha'      26859.117 1   3.6.4.10 ? ? ? 
2 non-polymer syn 'N-(5-chloro-2-methoxyphenyl)thiourea' 216.688   1   ?        ? ? ? 
3 water       nat water                                  18.015    231 ?        ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        
;Heat shock 86 kDa,HSP 86,HSP86,Heat shock protein family C member 1,Lipopolysaccharide-associated protein 2,LAP-2,LPS-associated protein 2,Renal carcinoma antigen NY-REN-38
;
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;MDQPMEEEEVETFAFQAEIAQLMSLIINTFYSNKEIFLRELISNSSDALDKIRYESLTDPSKLDSGKELHINLIPNKQDR
TLTIVDTGIGMTKADLINNLGTIAKSGTKAFMEALQAGADISMIGQFGVGFYSAYLVAEKVTVITKHNDDEQYAWESSAG
GSFTVRTDTGEPMGRGTKVILHLKEDQTEYLEERRIKEIVKKHSQFIGYPITLFVEKERDKEVSDDEAELEHHHHHH
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MDQPMEEEEVETFAFQAEIAQLMSLIINTFYSNKEIFLRELISNSSDALDKIRYESLTDPSKLDSGKELHINLIPNKQDR
TLTIVDTGIGMTKADLINNLGTIAKSGTKAFMEALQAGADISMIGQFGVGFYSAYLVAEKVTVITKHNDDEQYAWESSAG
GSFTVRTDTGEPMGRGTKVILHLKEDQTEYLEERRIKEIVKKHSQFIGYPITLFVEKERDKEVSDDEAELEHHHHHH
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'N-(5-chloro-2-methoxyphenyl)thiourea' A1AXB 
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 
A1AXB non-polymer         . 'N-(5-chloro-2-methoxyphenyl)thiourea' ? 'C8 H9 Cl N2 O S' 216.688 
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        A1AXB 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1AXB 
_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 A1AXB 1   301 301 A1AXB DWU A . 
C 3 HOH   1   401 216 HOH   HOH A . 
C 3 HOH   2   402 107 HOH   HOH A . 
C 3 HOH   3   403 167 HOH   HOH A . 
C 3 HOH   4   404 27  HOH   HOH A . 
C 3 HOH   5   405 184 HOH   HOH A . 
C 3 HOH   6   406 113 HOH   HOH A . 
C 3 HOH   7   407 42  HOH   HOH A . 
C 3 HOH   8   408 186 HOH   HOH A . 
C 3 HOH   9   409 189 HOH   HOH A . 
C 3 HOH   10  410 92  HOH   HOH A . 
C 3 HOH   11  411 52  HOH   HOH A . 
C 3 HOH   12  412 131 HOH   HOH A . 
C 3 HOH   13  413 95  HOH   HOH A . 
C 3 HOH   14  414 85  HOH   HOH A . 
C 3 HOH   15  415 69  HOH   HOH A . 
C 3 HOH   16  416 84  HOH   HOH A . 
C 3 HOH   17  417 128 HOH   HOH A . 
C 3 HOH   18  418 199 HOH   HOH A . 
C 3 HOH   19  419 26  HOH   HOH A . 
C 3 HOH   20  420 32  HOH   HOH A . 
C 3 HOH   21  421 47  HOH   HOH A . 
C 3 HOH   22  422 104 HOH   HOH A . 
C 3 HOH   23  423 19  HOH   HOH A . 
C 3 HOH   24  424 127 HOH   HOH A . 
C 3 HOH   25  425 91  HOH   HOH A . 
C 3 HOH   26  426 31  HOH   HOH A . 
C 3 HOH   27  427 22  HOH   HOH A . 
C 3 HOH   28  428 7   HOH   HOH A . 
C 3 HOH   29  429 187 HOH   HOH A . 
C 3 HOH   30  430 146 HOH   HOH A . 
C 3 HOH   31  431 80  HOH   HOH A . 
C 3 HOH   32  432 61  HOH   HOH A . 
C 3 HOH   33  433 68  HOH   HOH A . 
C 3 HOH   34  434 175 HOH   HOH A . 
C 3 HOH   35  435 123 HOH   HOH A . 
C 3 HOH   36  436 200 HOH   HOH A . 
C 3 HOH   37  437 60  HOH   HOH A . 
C 3 HOH   38  438 227 HOH   HOH A . 
C 3 HOH   39  439 3   HOH   HOH A . 
C 3 HOH   40  440 169 HOH   HOH A . 
C 3 HOH   41  441 51  HOH   HOH A . 
C 3 HOH   42  442 119 HOH   HOH A . 
C 3 HOH   43  443 18  HOH   HOH A . 
C 3 HOH   44  444 35  HOH   HOH A . 
C 3 HOH   45  445 192 HOH   HOH A . 
C 3 HOH   46  446 76  HOH   HOH A . 
C 3 HOH   47  447 53  HOH   HOH A . 
C 3 HOH   48  448 2   HOH   HOH A . 
C 3 HOH   49  449 78  HOH   HOH A . 
C 3 HOH   50  450 109 HOH   HOH A . 
C 3 HOH   51  451 165 HOH   HOH A . 
C 3 HOH   52  452 151 HOH   HOH A . 
C 3 HOH   53  453 11  HOH   HOH A . 
C 3 HOH   54  454 10  HOH   HOH A . 
C 3 HOH   55  455 161 HOH   HOH A . 
C 3 HOH   56  456 181 HOH   HOH A . 
C 3 HOH   57  457 1   HOH   HOH A . 
C 3 HOH   58  458 16  HOH   HOH A . 
C 3 HOH   59  459 183 HOH   HOH A . 
C 3 HOH   60  460 63  HOH   HOH A . 
C 3 HOH   61  461 29  HOH   HOH A . 
C 3 HOH   62  462 40  HOH   HOH A . 
C 3 HOH   63  463 96  HOH   HOH A . 
C 3 HOH   64  464 17  HOH   HOH A . 
C 3 HOH   65  465 124 HOH   HOH A . 
C 3 HOH   66  466 65  HOH   HOH A . 
C 3 HOH   67  467 153 HOH   HOH A . 
C 3 HOH   68  468 64  HOH   HOH A . 
C 3 HOH   69  469 79  HOH   HOH A . 
C 3 HOH   70  470 48  HOH   HOH A . 
C 3 HOH   71  471 6   HOH   HOH A . 
C 3 HOH   72  472 93  HOH   HOH A . 
C 3 HOH   73  473 182 HOH   HOH A . 
C 3 HOH   74  474 134 HOH   HOH A . 
C 3 HOH   75  475 8   HOH   HOH A . 
C 3 HOH   76  476 24  HOH   HOH A . 
C 3 HOH   77  477 130 HOH   HOH A . 
C 3 HOH   78  478 21  HOH   HOH A . 
C 3 HOH   79  479 116 HOH   HOH A . 
C 3 HOH   80  480 82  HOH   HOH A . 
C 3 HOH   81  481 46  HOH   HOH A . 
C 3 HOH   82  482 38  HOH   HOH A . 
C 3 HOH   83  483 90  HOH   HOH A . 
C 3 HOH   84  484 15  HOH   HOH A . 
C 3 HOH   85  485 49  HOH   HOH A . 
C 3 HOH   86  486 39  HOH   HOH A . 
C 3 HOH   87  487 58  HOH   HOH A . 
C 3 HOH   88  488 62  HOH   HOH A . 
C 3 HOH   89  489 110 HOH   HOH A . 
C 3 HOH   90  490 105 HOH   HOH A . 
C 3 HOH   91  491 72  HOH   HOH A . 
C 3 HOH   92  492 77  HOH   HOH A . 
C 3 HOH   93  493 218 HOH   HOH A . 
C 3 HOH   94  494 5   HOH   HOH A . 
C 3 HOH   95  495 168 HOH   HOH A . 
C 3 HOH   96  496 37  HOH   HOH A . 
C 3 HOH   97  497 44  HOH   HOH A . 
C 3 HOH   98  498 87  HOH   HOH A . 
C 3 HOH   99  499 14  HOH   HOH A . 
C 3 HOH   100 500 118 HOH   HOH A . 
C 3 HOH   101 501 41  HOH   HOH A . 
C 3 HOH   102 502 117 HOH   HOH A . 
C 3 HOH   103 503 25  HOH   HOH A . 
C 3 HOH   104 504 122 HOH   HOH A . 
C 3 HOH   105 505 75  HOH   HOH A . 
C 3 HOH   106 506 140 HOH   HOH A . 
C 3 HOH   107 507 56  HOH   HOH A . 
C 3 HOH   108 508 45  HOH   HOH A . 
C 3 HOH   109 509 88  HOH   HOH A . 
C 3 HOH   110 510 171 HOH   HOH A . 
C 3 HOH   111 511 30  HOH   HOH A . 
C 3 HOH   112 512 190 HOH   HOH A . 
C 3 HOH   113 513 13  HOH   HOH A . 
C 3 HOH   114 514 50  HOH   HOH A . 
C 3 HOH   115 515 101 HOH   HOH A . 
C 3 HOH   116 516 33  HOH   HOH A . 
C 3 HOH   117 517 23  HOH   HOH A . 
C 3 HOH   118 518 83  HOH   HOH A . 
C 3 HOH   119 519 89  HOH   HOH A . 
C 3 HOH   120 520 188 HOH   HOH A . 
C 3 HOH   121 521 43  HOH   HOH A . 
C 3 HOH   122 522 99  HOH   HOH A . 
C 3 HOH   123 523 73  HOH   HOH A . 
C 3 HOH   124 524 132 HOH   HOH A . 
C 3 HOH   125 525 142 HOH   HOH A . 
C 3 HOH   126 526 125 HOH   HOH A . 
C 3 HOH   127 527 170 HOH   HOH A . 
C 3 HOH   128 528 20  HOH   HOH A . 
C 3 HOH   129 529 166 HOH   HOH A . 
C 3 HOH   130 530 201 HOH   HOH A . 
C 3 HOH   131 531 70  HOH   HOH A . 
C 3 HOH   132 532 86  HOH   HOH A . 
C 3 HOH   133 533 147 HOH   HOH A . 
C 3 HOH   134 534 71  HOH   HOH A . 
C 3 HOH   135 535 143 HOH   HOH A . 
C 3 HOH   136 536 81  HOH   HOH A . 
C 3 HOH   137 537 178 HOH   HOH A . 
C 3 HOH   138 538 136 HOH   HOH A . 
C 3 HOH   139 539 54  HOH   HOH A . 
C 3 HOH   140 540 217 HOH   HOH A . 
C 3 HOH   141 541 115 HOH   HOH A . 
C 3 HOH   142 542 135 HOH   HOH A . 
C 3 HOH   143 543 57  HOH   HOH A . 
C 3 HOH   144 544 36  HOH   HOH A . 
C 3 HOH   145 545 28  HOH   HOH A . 
C 3 HOH   146 546 159 HOH   HOH A . 
C 3 HOH   147 547 163 HOH   HOH A . 
C 3 HOH   148 548 4   HOH   HOH A . 
C 3 HOH   149 549 180 HOH   HOH A . 
C 3 HOH   150 550 94  HOH   HOH A . 
C 3 HOH   151 551 198 HOH   HOH A . 
C 3 HOH   152 552 197 HOH   HOH A . 
C 3 HOH   153 553 114 HOH   HOH A . 
C 3 HOH   154 554 195 HOH   HOH A . 
C 3 HOH   155 555 59  HOH   HOH A . 
C 3 HOH   156 556 160 HOH   HOH A . 
C 3 HOH   157 557 225 HOH   HOH A . 
C 3 HOH   158 558 126 HOH   HOH A . 
C 3 HOH   159 559 111 HOH   HOH A . 
C 3 HOH   160 560 12  HOH   HOH A . 
C 3 HOH   161 561 226 HOH   HOH A . 
C 3 HOH   162 562 173 HOH   HOH A . 
C 3 HOH   163 563 34  HOH   HOH A . 
C 3 HOH   164 564 158 HOH   HOH A . 
C 3 HOH   165 565 196 HOH   HOH A . 
C 3 HOH   166 566 9   HOH   HOH A . 
C 3 HOH   167 567 194 HOH   HOH A . 
C 3 HOH   168 568 213 HOH   HOH A . 
C 3 HOH   169 569 224 HOH   HOH A . 
C 3 HOH   170 570 129 HOH   HOH A . 
C 3 HOH   171 571 179 HOH   HOH A . 
C 3 HOH   172 572 138 HOH   HOH A . 
C 3 HOH   173 573 172 HOH   HOH A . 
C 3 HOH   174 574 67  HOH   HOH A . 
C 3 HOH   175 575 121 HOH   HOH A . 
C 3 HOH   176 576 231 HOH   HOH A . 
C 3 HOH   177 577 145 HOH   HOH A . 
C 3 HOH   178 578 229 HOH   HOH A . 
C 3 HOH   179 579 141 HOH   HOH A . 
C 3 HOH   180 580 149 HOH   HOH A . 
C 3 HOH   181 581 139 HOH   HOH A . 
C 3 HOH   182 582 133 HOH   HOH A . 
C 3 HOH   183 583 155 HOH   HOH A . 
C 3 HOH   184 584 206 HOH   HOH A . 
C 3 HOH   185 585 106 HOH   HOH A . 
C 3 HOH   186 586 150 HOH   HOH A . 
C 3 HOH   187 587 162 HOH   HOH A . 
C 3 HOH   188 588 212 HOH   HOH A . 
C 3 HOH   189 589 222 HOH   HOH A . 
C 3 HOH   190 590 214 HOH   HOH A . 
C 3 HOH   191 591 98  HOH   HOH A . 
C 3 HOH   192 592 211 HOH   HOH A . 
C 3 HOH   193 593 108 HOH   HOH A . 
C 3 HOH   194 594 74  HOH   HOH A . 
C 3 HOH   195 595 154 HOH   HOH A . 
C 3 HOH   196 596 55  HOH   HOH A . 
C 3 HOH   197 597 164 HOH   HOH A . 
C 3 HOH   198 598 219 HOH   HOH A . 
C 3 HOH   199 599 120 HOH   HOH A . 
C 3 HOH   200 600 152 HOH   HOH A . 
C 3 HOH   201 601 100 HOH   HOH A . 
C 3 HOH   202 602 102 HOH   HOH A . 
C 3 HOH   203 603 148 HOH   HOH A . 
C 3 HOH   204 604 215 HOH   HOH A . 
C 3 HOH   205 605 177 HOH   HOH A . 
C 3 HOH   206 606 228 HOH   HOH A . 
C 3 HOH   207 607 202 HOH   HOH A . 
C 3 HOH   208 608 203 HOH   HOH A . 
C 3 HOH   209 609 205 HOH   HOH A . 
C 3 HOH   210 610 103 HOH   HOH A . 
C 3 HOH   211 611 97  HOH   HOH A . 
C 3 HOH   212 612 137 HOH   HOH A . 
C 3 HOH   213 613 230 HOH   HOH A . 
C 3 HOH   214 614 223 HOH   HOH A . 
C 3 HOH   215 615 112 HOH   HOH A . 
C 3 HOH   216 616 208 HOH   HOH A . 
C 3 HOH   217 617 210 HOH   HOH A . 
C 3 HOH   218 618 220 HOH   HOH A . 
C 3 HOH   219 619 144 HOH   HOH A . 
C 3 HOH   220 620 193 HOH   HOH A . 
C 3 HOH   221 621 209 HOH   HOH A . 
C 3 HOH   222 622 174 HOH   HOH A . 
C 3 HOH   223 623 176 HOH   HOH A . 
C 3 HOH   224 624 207 HOH   HOH A . 
C 3 HOH   225 625 221 HOH   HOH A . 
C 3 HOH   226 626 204 HOH   HOH A . 
C 3 HOH   227 627 191 HOH   HOH A . 
C 3 HOH   228 628 66  HOH   HOH A . 
C 3 HOH   229 629 156 HOH   HOH A . 
C 3 HOH   230 630 185 HOH   HOH A . 
C 3 HOH   231 631 157 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             598106.833 
_cell.length_a           66.900 
_cell.length_b           90.940 
_cell.length_c           98.310 
_cell.angle_beta         90.000 
_cell.angle_gamma        90.000 
_cell.angle_alpha        90.000 
_cell.entry_id           7HAA 
_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                         7HAA 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
# 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
_exptl.entry_id          7HAA 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_Matthews      2.88 
_exptl_crystal.density_percent_sol   57.23 
_exptl_crystal.density_meas          ? 
_exptl_crystal.description           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.pH              8.5 
_exptl_crystal_grow.temp            277 
_exptl_crystal_grow.pdbx_details    '100mM Tris-HCl pH 8.5, 22% PEG4000, 200mM MgCl2' 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_diffrn.id                     1 
_diffrn.crystal_id             1 
_diffrn.ambient_temp           100 
_diffrn.ambient_temp_details   ? 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               PIXEL 
_diffrn_detector.type                   'DECTRIS EIGER X 16M' 
_diffrn_detector.pdbx_collection_date   2024-01-13 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.pdbx_scattering_type             x-ray 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.monochromator                    Si111 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.97919 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.pdbx_synchrotron_beamline   BL10U2 
_diffrn_source.type                        'SSRF BEAMLINE BL10U2' 
_diffrn_source.pdbx_wavelength_list        0.97919 
_diffrn_source.pdbx_synchrotron_site       SSRF 
_diffrn_source.pdbx_wavelength             ? 
# 
_reflns.entry_id                     7HAA 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             30.830 
_reflns.d_resolution_high            1.670 
_reflns.number_obs                   35134 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         100.000 
_reflns.pdbx_Rmerge_I_obs            0.075 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        18.200 
_reflns.B_iso_Wilson_estimate        ? 
_reflns.pdbx_redundancy              12.600 
_reflns.pdbx_Rrim_I_all              0.078 
_reflns.pdbx_Rpim_I_all              0.022 
_reflns.pdbx_CC_half                 1.000 
_reflns.pdbx_netI_over_av_sigmaI     ? 
_reflns.pdbx_number_measured_all     443121 
_reflns.pdbx_scaling_rejects         38 
_reflns.pdbx_chi_squared             ? 
_reflns.Rmerge_F_all                 ? 
_reflns.Rmerge_F_obs                 ? 
_reflns.observed_criterion_F_max     ? 
_reflns.observed_criterion_F_min     ? 
_reflns.observed_criterion_I_max     ? 
_reflns.observed_criterion_I_min     ? 
_reflns.pdbx_d_res_high_opt          ? 
_reflns.pdbx_d_res_low_opt           ? 
_reflns.details                      ? 
# 
loop_
_reflns_shell.pdbx_diffrn_id 
_reflns_shell.pdbx_ordinal 
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_reflns_shell.number_measured_obs 
_reflns_shell.number_measured_all 
_reflns_shell.number_unique_obs 
_reflns_shell.pdbx_rejects 
_reflns_shell.Rmerge_I_obs 
_reflns_shell.meanI_over_sigI_obs 
_reflns_shell.pdbx_Rsym_value 
_reflns_shell.pdbx_chi_squared 
_reflns_shell.pdbx_redundancy 
_reflns_shell.percent_possible_obs 
_reflns_shell.pdbx_netI_over_sigmaI_obs 
_reflns_shell.number_possible 
_reflns_shell.number_unique_all 
_reflns_shell.Rmerge_F_all 
_reflns_shell.Rmerge_F_obs 
_reflns_shell.Rmerge_I_all 
_reflns_shell.meanI_over_sigI_all 
_reflns_shell.percent_possible_all 
_reflns_shell.pdbx_Rrim_I_all 
_reflns_shell.pdbx_Rpim_I_all 
_reflns_shell.pdbx_CC_half 
1 1 1.670 1.710  ? 28020 2565 ? 1.860 ? ? ? 10.900 ? 1.400  ? ? ? ? ? ? 100.000 1.951 0.585 0.472 
1 2 7.470 30.830 ? 4029  431  ? 0.028 ? ? ? 9.300  ? 50.900 ? ? ? ? ? ? 97.900  0.030 0.009 0.999 
# 
_refine.entry_id                                 7HAA 
_refine.pdbx_method_to_determine_struct          'FOURIER SYNTHESIS' 
_refine.ls_percent_reflns_R_free                 5.08 
_refine.pdbx_overall_phase_error                 19.7304 
_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                          0.1711 
_refine.B_iso_mean                               34.62 
_refine.ls_number_reflns_R_free                  1783 
_refine.ls_percent_reflns_obs                    99.96 
_refine.ls_R_factor_R_work                       0.1706 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_refine.ls_d_res_high                            1.67 
_refine.ls_number_reflns_obs                     35125 
_refine.pdbx_ls_sigma_F                          1.34 
_refine.ls_number_reflns_R_work                  33342 
_refine.ls_d_res_low                             24.71 
_refine.pdbx_stereochemistry_target_values       'GeoStd + Monomer Library + CDL v1.2' 
_refine.ls_R_factor_R_free                       0.1805 
_refine.overall_SU_ML                            0.1745 
_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             231 
_refine_hist.number_atoms_total               1888 
_refine_hist.d_res_high                       1.67 
_refine_hist.d_res_low                        24.71 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.type 
_refine_ls_restr.number 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
_refine_ls_restr.dev_ideal_target 
'X-RAY DIFFRACTION' f_bond_d           1683 0.0067 ? ? ? 
'X-RAY DIFFRACTION' f_angle_d          2268 0.9297 ? ? ? 
'X-RAY DIFFRACTION' f_chiral_restr     259  0.0569 ? ? ? 
'X-RAY DIFFRACTION' f_plane_restr      289  0.0068 ? ? ? 
'X-RAY DIFFRACTION' f_dihedral_angle_d 225  6.2273 ? ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.R_factor_R_free 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.R_factor_all 
'X-RAY DIFFRACTION' 1.67 1.72  2538 0.2971 100.00 0.3085 129 . . . . . 
'X-RAY DIFFRACTION' 1.72 1.77  2517 0.2636 99.96  0.3175 132 . . . . . 
'X-RAY DIFFRACTION' 1.77 1.82  2554 0.2335 100.00 0.2681 144 . . . . . 
'X-RAY DIFFRACTION' 1.82 1.89  2516 0.2019 99.96  0.2223 138 . . . . . 
'X-RAY DIFFRACTION' 1.89 1.96  2542 0.1856 100.00 0.2171 133 . . . . . 
'X-RAY DIFFRACTION' 1.96 2.05  2556 0.1781 100.00 0.2059 122 . . . . . 
'X-RAY DIFFRACTION' 2.05 2.16  2567 0.1660 100.00 0.1801 124 . . . . . 
'X-RAY DIFFRACTION' 2.16 2.30  2551 0.1618 100.00 0.1703 124 . . . . . 
'X-RAY DIFFRACTION' 2.30 2.47  2571 0.1788 100.00 0.2054 137 . . . . . 
'X-RAY DIFFRACTION' 2.47 2.72  2564 0.1886 99.96  0.2062 138 . . . . . 
'X-RAY DIFFRACTION' 2.72 3.11  2585 0.1811 100.00 0.1848 149 . . . . . 
'X-RAY DIFFRACTION' 3.12 3.92  2575 0.1526 99.96  0.1681 174 . . . . . 
'X-RAY DIFFRACTION' 3.92 24.71 2706 0.1505 99.65  0.1463 139 . . . . . 
# 
_struct.entry_id                  7HAA 
_struct.title                     'PanDDA analysis group deposition -- Crystal structure of HSP90N in complex with Fr13279' 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_details        ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HAA 
_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              7HAA 
_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 7HAA MET A 1   ? UNP P07900 ? ? 'initiating methionine' 8   1 
1 7HAA LEU A 230 ? UNP P07900 ? ? 'expression tag'        237 2 
1 7HAA GLU A 231 ? UNP P07900 ? ? 'expression tag'        238 3 
1 7HAA HIS A 232 ? UNP P07900 ? ? 'expression tag'        239 4 
1 7HAA HIS A 233 ? UNP P07900 ? ? 'expression tag'        240 5 
1 7HAA HIS A 234 ? UNP P07900 ? ? 'expression tag'        241 6 
1 7HAA HIS A 235 ? UNP P07900 ? ? 'expression tag'        242 7 
1 7HAA HIS A 236 ? UNP P07900 ? ? 'expression tag'        243 8 
1 7HAA 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  ? GLY A 118 ? ASN A 105 GLY A 125 1 ? 21 
HELX_P HELX_P6 AA6 ASP A 120 ? GLY A 128 ? ASP A 127 GLY A 135 5 ? 9  
HELX_P HELX_P7 AA7 VAL A 129 ? LEU A 136 ? VAL A 136 LEU A 143 5 ? 8  
HELX_P HELX_P8 AA8 GLN A 187 ? LEU A 191 ? GLN A 194 LEU A 198 5 ? 5  
HELX_P HELX_P9 AA9 GLU A 192 ? SER A 204 ? GLU A 199 SER A 211 1 ? 13 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
_struct_sheet.id               AA1 
_struct_sheet.type             ? 
_struct_sheet.number_strands   8 
_struct_sheet.details          ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA1 5 6 ? anti-parallel 
AA1 6 7 ? anti-parallel 
AA1 7 8 ? parallel      
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 VAL A 10  ? ALA A 14  ? VAL A 17  ALA A 21  
AA1 2 SER A 162 ? THR A 167 ? SER A 169 THR A 174 
AA1 3 TYR A 153 ? SER A 157 ? TYR A 160 SER A 164 
AA1 4 ALA A 138 ? LYS A 146 ? ALA A 145 LYS A 153 
AA1 5 GLY A 176 ? LEU A 183 ? GLY A 183 LEU A 190 
AA1 6 THR A 81  ? ASP A 86  ? THR A 88  ASP A 93  
AA1 7 ILE A 71  ? ASN A 76  ? ILE A 78  ASN A 83  
AA1 8 ILE A 211 ? LEU A 213 ? ILE A 218 LEU A 220 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N PHE A 13  ? N PHE A 20  O PHE A 163 ? O PHE A 170 
AA1 2 3 O ARG A 166 ? O ARG A 173 N ALA A 154 ? N ALA A 161 
AA1 3 4 O TRP A 155 ? O TRP A 162 N VAL A 143 ? N VAL A 150 
AA1 4 5 N THR A 142 ? N THR A 149 O ILE A 180 ? O ILE A 187 
AA1 5 6 O LEU A 181 ? O LEU A 188 N LEU A 82  ? N LEU A 89  
AA1 6 7 O 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                   7HAA 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 O A HOH 424 ? ? O A HOH 557 ? ? 1.81 
2 1 O A HOH 502 ? ? O A HOH 610 ? ? 2.01 
3 1 O A HOH 529 ? ? O A HOH 571 ? ? 2.07 
4 1 O A HOH 535 ? ? O A HOH 562 ? ? 2.07 
5 1 O A HOH 604 ? ? O A HOH 630 ? ? 2.09 
6 1 O A HOH 452 ? ? O A HOH 525 ? ? 2.10 
7 1 O A HOH 514 ? ? O A HOH 524 ? ? 2.10 
8 1 O A LYS 224 ? ? O A HOH 401 ? ? 2.15 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 TYR A 38  ? ? -160.10 111.94  
2 1 ALA A 166 ? ? 61.98   -146.36 
# 
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 13.1825117061  -18.1281418881 -18.0663125171 0.210436347503 0.236617619677 0.231102887506 
0.0123917914006   -0.0110862716703 -0.0262740650072 2.3470297071  1.45991539317 4.41077652087 -0.856503206753 -1.18947225663  
0.778909138243   -0.0960525609939 -0.148494109852 -0.0435706744914  0.11352825033    0.0329068528243  -0.0206833431317 
0.0432919768781  0.322756969838   -0.0379651749157 
2 ? 'X-RAY DIFFRACTION' refined -6.79822631292 -6.48964907478 -25.4889242609 0.243136068103 0.219407450479 0.270502744358 
-0.00417950546834 -0.025964495312  -0.0129783787078 2.10616022245 2.05745105693 3.91641396546 -1.00716140375  0.880233941684  
-1.22031429474   -0.0607610724045 0.143734066812  0.220604844734    -0.0943842892264 -0.0761012606843 0.0752034261934  
-0.351034232481  -0.0950030532671 0.0639862709592  
3 ? 'X-RAY DIFFRACTION' refined -3.79249687867 -18.3845431005 -23.5252106022 0.215357740087 0.154531488544 0.195180626081 
-0.0134365209129  -0.0369457449101 -0.0485694419718 2.41503806215 2.30668170758 3.42518022621 -0.70776224558  -1.0194142651   
-0.861647683509  -0.0414130699029 0.0399201166721 -0.149498769643   -0.064299336969  0.0193772233488  0.0319672465803  
0.177256166215   -0.0583322244408 0.029791834978   
4 ? 'X-RAY DIFFRACTION' refined 12.8411125426  -6.2802613661  -15.3213342569 0.231377668755 0.316664270102 0.324448684332 
-0.0422861282669  -0.0182078205717 -0.0301680341711 4.45396398105 4.89814648925 2.17833280765 -1.0702254917   -2.96629102927  
-0.21525814017   0.13268270506    -0.6454243823   0.58060722235     0.51857394607    0.028275540285   -0.405291606193  
-0.13523868651   0.669393056733   -0.0346441879111 
5 ? 'X-RAY DIFFRACTION' refined 1.5309989168   -20.0410607337 -26.6741307886 0.217370752066 0.198681415431 0.23142097692  
-0.00578359226254 -0.0103589782346 -0.0312376794053 2.83366170237 1.75536710408 2.81379937959 -0.813341599468 0.577390307336  
-0.202894417924  0.0907805702782  0.281847365718  -0.263272655919   -0.21028847248   -0.0210991639342 0.148382213222   
0.217657879281   0.102195321241   -0.0182303446079 
6 ? 'X-RAY DIFFRACTION' refined -6.13123218627 -19.3709522979 -6.80147996594 0.285067943632 0.309538943424 0.232826645304 
-0.018401096188   0.0183814035376  0.0380585533147  5.5372399077  4.41213500003 3.85279679189 -1.5583479373   -0.105404614223 
0.248598335759   -0.0751473132028 -0.42117184759  -0.371050711747   0.353238189737   -0.0432148487318 0.361257734504   
0.35262353381    -0.187572476251  0.03813212321    
7 ? 'X-RAY DIFFRACTION' refined -13.3687458851 -13.1554257993 -15.4551022196 0.227687531499 0.29948693568  0.222565143676 
0.0276652302336   0.0208217206629  -0.0282906732849 4.36547818726 4.1661283025  3.81616383639 0.640319447898  0.293680257398  
-0.0117887441057 0.0694082336367  -0.393522383152 -0.00224063765325 0.434907303495   -0.157775393033  0.147907170954   
-0.0380927222114 -0.247228546349  0.0823822639853  
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
1 1 'X-RAY DIFFRACTION' A 16  A 1   A 40  A 25  . 
;chain 'A' and (resid 16 through 40 )
;
2 2 'X-RAY DIFFRACTION' A 41  A 26  A 76  A 61  . 
;chain 'A' and (resid 41 through 76 )
;
3 3 'X-RAY DIFFRACTION' A 77  A 62  A 105 A 90  . 
;chain 'A' and (resid 77 through 105 )
;
4 4 'X-RAY DIFFRACTION' A 106 A 91  A 136 A 121 . 
;chain 'A' and (resid 106 through 136 )
;
5 5 'X-RAY DIFFRACTION' A 137 A 122 A 190 A 175 . 
;chain 'A' and (resid 137 through 190 )
;
6 6 'X-RAY DIFFRACTION' A 191 A 176 A 210 A 195 . 
;chain 'A' and (resid 191 through 210 )
;
7 7 'X-RAY DIFFRACTION' A 211 A 196 A 224 A 209 . 
;chain 'A' and (resid 211 through 224 )
;
# 
loop_
_pdbx_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 
A1AXB C8   C  N N 1   
A1AXB C5   C  Y N 2   
A1AXB C6   C  Y N 3   
A1AXB C2   C  Y N 4   
A1AXB C4   C  Y N 5   
A1AXB C1   C  N N 6   
A1AXB C3   C  Y N 7   
A1AXB C7   C  Y N 8   
A1AXB N1   N  N N 9   
A1AXB N2   N  N N 10  
A1AXB O1   O  N N 11  
A1AXB S1   S  N N 12  
A1AXB CL1  CL N N 13  
A1AXB H6   H  N N 14  
A1AXB H5   H  N N 15  
A1AXB H3   H  N N 16  
A1AXB H2   H  N N 17  
A1AXB H1   H  N N 18  
A1AXB H4   H  N N 19  
A1AXB H7   H  N N 20  
A1AXB H8   H  N N 21  
A1AXB H9   H  N N 22  
ALA   N    N  N N 23  
ALA   CA   C  N S 24  
ALA   C    C  N N 25  
ALA   O    O  N N 26  
ALA   CB   C  N N 27  
ALA   OXT  O  N N 28  
ALA   H    H  N N 29  
ALA   H2   H  N N 30  
ALA   HA   H  N N 31  
ALA   HB1  H  N N 32  
ALA   HB2  H  N N 33  
ALA   HB3  H  N N 34  
ALA   HXT  H  N N 35  
ARG   N    N  N N 36  
ARG   CA   C  N S 37  
ARG   C    C  N N 38  
ARG   O    O  N N 39  
ARG   CB   C  N N 40  
ARG   CG   C  N N 41  
ARG   CD   C  N N 42  
ARG   NE   N  N N 43  
ARG   CZ   C  N N 44  
ARG   NH1  N  N N 45  
ARG   NH2  N  N N 46  
ARG   OXT  O  N N 47  
ARG   H    H  N N 48  
ARG   H2   H  N N 49  
ARG   HA   H  N N 50  
ARG   HB2  H  N N 51  
ARG   HB3  H  N N 52  
ARG   HG2  H  N N 53  
ARG   HG3  H  N N 54  
ARG   HD2  H  N N 55  
ARG   HD3  H  N N 56  
ARG   HE   H  N N 57  
ARG   HH11 H  N N 58  
ARG   HH12 H  N N 59  
ARG   HH21 H  N N 60  
ARG   HH22 H  N N 61  
ARG   HXT  H  N N 62  
ASN   N    N  N N 63  
ASN   CA   C  N S 64  
ASN   C    C  N N 65  
ASN   O    O  N N 66  
ASN   CB   C  N N 67  
ASN   CG   C  N N 68  
ASN   OD1  O  N N 69  
ASN   ND2  N  N N 70  
ASN   OXT  O  N N 71  
ASN   H    H  N N 72  
ASN   H2   H  N N 73  
ASN   HA   H  N N 74  
ASN   HB2  H  N N 75  
ASN   HB3  H  N N 76  
ASN   HD21 H  N N 77  
ASN   HD22 H  N N 78  
ASN   HXT  H  N N 79  
ASP   N    N  N N 80  
ASP   CA   C  N S 81  
ASP   C    C  N N 82  
ASP   O    O  N N 83  
ASP   CB   C  N N 84  
ASP   CG   C  N N 85  
ASP   OD1  O  N N 86  
ASP   OD2  O  N N 87  
ASP   OXT  O  N N 88  
ASP   H    H  N N 89  
ASP   H2   H  N N 90  
ASP   HA   H  N N 91  
ASP   HB2  H  N N 92  
ASP   HB3  H  N N 93  
ASP   HD2  H  N N 94  
ASP   HXT  H  N N 95  
GLN   N    N  N N 96  
GLN   CA   C  N S 97  
GLN   C    C  N N 98  
GLN   O    O  N N 99  
GLN   CB   C  N N 100 
GLN   CG   C  N N 101 
GLN   CD   C  N N 102 
GLN   OE1  O  N N 103 
GLN   NE2  N  N N 104 
GLN   OXT  O  N N 105 
GLN   H    H  N N 106 
GLN   H2   H  N N 107 
GLN   HA   H  N N 108 
GLN   HB2  H  N N 109 
GLN   HB3  H  N N 110 
GLN   HG2  H  N N 111 
GLN   HG3  H  N N 112 
GLN   HE21 H  N N 113 
GLN   HE22 H  N N 114 
GLN   HXT  H  N N 115 
GLU   N    N  N N 116 
GLU   CA   C  N S 117 
GLU   C    C  N N 118 
GLU   O    O  N N 119 
GLU   CB   C  N N 120 
GLU   CG   C  N N 121 
GLU   CD   C  N N 122 
GLU   OE1  O  N N 123 
GLU   OE2  O  N N 124 
GLU   OXT  O  N N 125 
GLU   H    H  N N 126 
GLU   H2   H  N N 127 
GLU   HA   H  N N 128 
GLU   HB2  H  N N 129 
GLU   HB3  H  N N 130 
GLU   HG2  H  N N 131 
GLU   HG3  H  N N 132 
GLU   HE2  H  N N 133 
GLU   HXT  H  N N 134 
GLY   N    N  N N 135 
GLY   CA   C  N N 136 
GLY   C    C  N N 137 
GLY   O    O  N N 138 
GLY   OXT  O  N N 139 
GLY   H    H  N N 140 
GLY   H2   H  N N 141 
GLY   HA2  H  N N 142 
GLY   HA3  H  N N 143 
GLY   HXT  H  N N 144 
HIS   N    N  N N 145 
HIS   CA   C  N S 146 
HIS   C    C  N N 147 
HIS   O    O  N N 148 
HIS   CB   C  N N 149 
HIS   CG   C  Y N 150 
HIS   ND1  N  Y N 151 
HIS   CD2  C  Y N 152 
HIS   CE1  C  Y N 153 
HIS   NE2  N  Y N 154 
HIS   OXT  O  N N 155 
HIS   H    H  N N 156 
HIS   H2   H  N N 157 
HIS   HA   H  N N 158 
HIS   HB2  H  N N 159 
HIS   HB3  H  N N 160 
HIS   HD1  H  N N 161 
HIS   HD2  H  N N 162 
HIS   HE1  H  N N 163 
HIS   HE2  H  N N 164 
HIS   HXT  H  N N 165 
HOH   O    O  N N 166 
HOH   H1   H  N N 167 
HOH   H2   H  N N 168 
ILE   N    N  N N 169 
ILE   CA   C  N S 170 
ILE   C    C  N N 171 
ILE   O    O  N N 172 
ILE   CB   C  N S 173 
ILE   CG1  C  N N 174 
ILE   CG2  C  N N 175 
ILE   CD1  C  N N 176 
ILE   OXT  O  N N 177 
ILE   H    H  N N 178 
ILE   H2   H  N N 179 
ILE   HA   H  N N 180 
ILE   HB   H  N N 181 
ILE   HG12 H  N N 182 
ILE   HG13 H  N N 183 
ILE   HG21 H  N N 184 
ILE   HG22 H  N N 185 
ILE   HG23 H  N N 186 
ILE   HD11 H  N N 187 
ILE   HD12 H  N N 188 
ILE   HD13 H  N N 189 
ILE   HXT  H  N N 190 
LEU   N    N  N N 191 
LEU   CA   C  N S 192 
LEU   C    C  N N 193 
LEU   O    O  N N 194 
LEU   CB   C  N N 195 
LEU   CG   C  N N 196 
LEU   CD1  C  N N 197 
LEU   CD2  C  N N 198 
LEU   OXT  O  N N 199 
LEU   H    H  N N 200 
LEU   H2   H  N N 201 
LEU   HA   H  N N 202 
LEU   HB2  H  N N 203 
LEU   HB3  H  N N 204 
LEU   HG   H  N N 205 
LEU   HD11 H  N N 206 
LEU   HD12 H  N N 207 
LEU   HD13 H  N N 208 
LEU   HD21 H  N N 209 
LEU   HD22 H  N N 210 
LEU   HD23 H  N N 211 
LEU   HXT  H  N N 212 
LYS   N    N  N N 213 
LYS   CA   C  N S 214 
LYS   C    C  N N 215 
LYS   O    O  N N 216 
LYS   CB   C  N N 217 
LYS   CG   C  N N 218 
LYS   CD   C  N N 219 
LYS   CE   C  N N 220 
LYS   NZ   N  N N 221 
LYS   OXT  O  N N 222 
LYS   H    H  N N 223 
LYS   H2   H  N N 224 
LYS   HA   H  N N 225 
LYS   HB2  H  N N 226 
LYS   HB3  H  N N 227 
LYS   HG2  H  N N 228 
LYS   HG3  H  N N 229 
LYS   HD2  H  N N 230 
LYS   HD3  H  N N 231 
LYS   HE2  H  N N 232 
LYS   HE3  H  N N 233 
LYS   HZ1  H  N N 234 
LYS   HZ2  H  N N 235 
LYS   HZ3  H  N N 236 
LYS   HXT  H  N N 237 
MET   N    N  N N 238 
MET   CA   C  N S 239 
MET   C    C  N N 240 
MET   O    O  N N 241 
MET   CB   C  N N 242 
MET   CG   C  N N 243 
MET   SD   S  N N 244 
MET   CE   C  N N 245 
MET   OXT  O  N N 246 
MET   H    H  N N 247 
MET   H2   H  N N 248 
MET   HA   H  N N 249 
MET   HB2  H  N N 250 
MET   HB3  H  N N 251 
MET   HG2  H  N N 252 
MET   HG3  H  N N 253 
MET   HE1  H  N N 254 
MET   HE2  H  N N 255 
MET   HE3  H  N N 256 
MET   HXT  H  N N 257 
PHE   N    N  N N 258 
PHE   CA   C  N S 259 
PHE   C    C  N N 260 
PHE   O    O  N N 261 
PHE   CB   C  N N 262 
PHE   CG   C  Y N 263 
PHE   CD1  C  Y N 264 
PHE   CD2  C  Y N 265 
PHE   CE1  C  Y N 266 
PHE   CE2  C  Y N 267 
PHE   CZ   C  Y N 268 
PHE   OXT  O  N N 269 
PHE   H    H  N N 270 
PHE   H2   H  N N 271 
PHE   HA   H  N N 272 
PHE   HB2  H  N N 273 
PHE   HB3  H  N N 274 
PHE   HD1  H  N N 275 
PHE   HD2  H  N N 276 
PHE   HE1  H  N N 277 
PHE   HE2  H  N N 278 
PHE   HZ   H  N N 279 
PHE   HXT  H  N N 280 
PRO   N    N  N N 281 
PRO   CA   C  N S 282 
PRO   C    C  N N 283 
PRO   O    O  N N 284 
PRO   CB   C  N N 285 
PRO   CG   C  N N 286 
PRO   CD   C  N N 287 
PRO   OXT  O  N N 288 
PRO   H    H  N N 289 
PRO   HA   H  N N 290 
PRO   HB2  H  N N 291 
PRO   HB3  H  N N 292 
PRO   HG2  H  N N 293 
PRO   HG3  H  N N 294 
PRO   HD2  H  N N 295 
PRO   HD3  H  N N 296 
PRO   HXT  H  N N 297 
SER   N    N  N N 298 
SER   CA   C  N S 299 
SER   C    C  N N 300 
SER   O    O  N N 301 
SER   CB   C  N N 302 
SER   OG   O  N N 303 
SER   OXT  O  N N 304 
SER   H    H  N N 305 
SER   H2   H  N N 306 
SER   HA   H  N N 307 
SER   HB2  H  N N 308 
SER   HB3  H  N N 309 
SER   HG   H  N N 310 
SER   HXT  H  N N 311 
THR   N    N  N N 312 
THR   CA   C  N S 313 
THR   C    C  N N 314 
THR   O    O  N N 315 
THR   CB   C  N R 316 
THR   OG1  O  N N 317 
THR   CG2  C  N N 318 
THR   OXT  O  N N 319 
THR   H    H  N N 320 
THR   H2   H  N N 321 
THR   HA   H  N N 322 
THR   HB   H  N N 323 
THR   HG1  H  N N 324 
THR   HG21 H  N N 325 
THR   HG22 H  N N 326 
THR   HG23 H  N N 327 
THR   HXT  H  N N 328 
TRP   N    N  N N 329 
TRP   CA   C  N S 330 
TRP   C    C  N N 331 
TRP   O    O  N N 332 
TRP   CB   C  N N 333 
TRP   CG   C  Y N 334 
TRP   CD1  C  Y N 335 
TRP   CD2  C  Y N 336 
TRP   NE1  N  Y N 337 
TRP   CE2  C  Y N 338 
TRP   CE3  C  Y N 339 
TRP   CZ2  C  Y N 340 
TRP   CZ3  C  Y N 341 
TRP   CH2  C  Y N 342 
TRP   OXT  O  N N 343 
TRP   H    H  N N 344 
TRP   H2   H  N N 345 
TRP   HA   H  N N 346 
TRP   HB2  H  N N 347 
TRP   HB3  H  N N 348 
TRP   HD1  H  N N 349 
TRP   HE1  H  N N 350 
TRP   HE3  H  N N 351 
TRP   HZ2  H  N N 352 
TRP   HZ3  H  N N 353 
TRP   HH2  H  N N 354 
TRP   HXT  H  N N 355 
TYR   N    N  N N 356 
TYR   CA   C  N S 357 
TYR   C    C  N N 358 
TYR   O    O  N N 359 
TYR   CB   C  N N 360 
TYR   CG   C  Y N 361 
TYR   CD1  C  Y N 362 
TYR   CD2  C  Y N 363 
TYR   CE1  C  Y N 364 
TYR   CE2  C  Y N 365 
TYR   CZ   C  Y N 366 
TYR   OH   O  N N 367 
TYR   OXT  O  N N 368 
TYR   H    H  N N 369 
TYR   H2   H  N N 370 
TYR   HA   H  N N 371 
TYR   HB2  H  N N 372 
TYR   HB3  H  N N 373 
TYR   HD1  H  N N 374 
TYR   HD2  H  N N 375 
TYR   HE1  H  N N 376 
TYR   HE2  H  N N 377 
TYR   HH   H  N N 378 
TYR   HXT  H  N N 379 
VAL   N    N  N N 380 
VAL   CA   C  N S 381 
VAL   C    C  N N 382 
VAL   O    O  N N 383 
VAL   CB   C  N N 384 
VAL   CG1  C  N N 385 
VAL   CG2  C  N N 386 
VAL   OXT  O  N N 387 
VAL   H    H  N N 388 
VAL   H2   H  N N 389 
VAL   HA   H  N N 390 
VAL   HB   H  N N 391 
VAL   HG11 H  N N 392 
VAL   HG12 H  N N 393 
VAL   HG13 H  N N 394 
VAL   HG21 H  N N 395 
VAL   HG22 H  N N 396 
VAL   HG23 H  N N 397 
VAL   HXT  H  N N 398 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
A1AXB C1  O1   sing N N 1   
A1AXB O1  C2   sing N N 2   
A1AXB C2  C3   doub Y N 3   
A1AXB C3  C4   sing Y N 4   
A1AXB C4  C5   doub Y N 5   
A1AXB C5  CL1  sing N N 6   
A1AXB C5  C6   sing Y N 7   
A1AXB C6  C7   doub Y N 8   
A1AXB C7  N1   sing N N 9   
A1AXB N1  C8   sing N N 10  
A1AXB C8  N2   sing N N 11  
A1AXB C8  S1   doub N N 12  
A1AXB C2  C7   sing Y N 13  
A1AXB C6  H6   sing N N 14  
A1AXB C4  H5   sing N N 15  
A1AXB C1  H3   sing N N 16  
A1AXB C1  H2   sing N N 17  
A1AXB C1  H1   sing N N 18  
A1AXB C3  H4   sing N N 19  
A1AXB N1  H7   sing N N 20  
A1AXB N2  H8   sing N N 21  
A1AXB N2  H9   sing N N 22  
ALA   N   CA   sing N N 23  
ALA   N   H    sing N N 24  
ALA   N   H2   sing N N 25  
ALA   CA  C    sing N N 26  
ALA   CA  CB   sing N N 27  
ALA   CA  HA   sing N N 28  
ALA   C   O    doub N N 29  
ALA   C   OXT  sing N N 30  
ALA   CB  HB1  sing N N 31  
ALA   CB  HB2  sing N N 32  
ALA   CB  HB3  sing N N 33  
ALA   OXT HXT  sing N N 34  
ARG   N   CA   sing N N 35  
ARG   N   H    sing N N 36  
ARG   N   H2   sing N N 37  
ARG   CA  C    sing N N 38  
ARG   CA  CB   sing N N 39  
ARG   CA  HA   sing N N 40  
ARG   C   O    doub N N 41  
ARG   C   OXT  sing N N 42  
ARG   CB  CG   sing N N 43  
ARG   CB  HB2  sing N N 44  
ARG   CB  HB3  sing N N 45  
ARG   CG  CD   sing N N 46  
ARG   CG  HG2  sing N N 47  
ARG   CG  HG3  sing N N 48  
ARG   CD  NE   sing N N 49  
ARG   CD  HD2  sing N N 50  
ARG   CD  HD3  sing N N 51  
ARG   NE  CZ   sing N N 52  
ARG   NE  HE   sing N N 53  
ARG   CZ  NH1  sing N N 54  
ARG   CZ  NH2  doub N N 55  
ARG   NH1 HH11 sing N N 56  
ARG   NH1 HH12 sing N N 57  
ARG   NH2 HH21 sing N N 58  
ARG   NH2 HH22 sing N N 59  
ARG   OXT HXT  sing N N 60  
ASN   N   CA   sing N N 61  
ASN   N   H    sing N N 62  
ASN   N   H2   sing N N 63  
ASN   CA  C    sing N N 64  
ASN   CA  CB   sing N N 65  
ASN   CA  HA   sing N N 66  
ASN   C   O    doub N N 67  
ASN   C   OXT  sing N N 68  
ASN   CB  CG   sing N N 69  
ASN   CB  HB2  sing N N 70  
ASN   CB  HB3  sing N N 71  
ASN   CG  OD1  doub N N 72  
ASN   CG  ND2  sing N N 73  
ASN   ND2 HD21 sing N N 74  
ASN   ND2 HD22 sing N N 75  
ASN   OXT HXT  sing N N 76  
ASP   N   CA   sing N N 77  
ASP   N   H    sing N N 78  
ASP   N   H2   sing N N 79  
ASP   CA  C    sing N N 80  
ASP   CA  CB   sing N N 81  
ASP   CA  HA   sing N N 82  
ASP   C   O    doub N N 83  
ASP   C   OXT  sing N N 84  
ASP   CB  CG   sing N N 85  
ASP   CB  HB2  sing N N 86  
ASP   CB  HB3  sing N N 87  
ASP   CG  OD1  doub N N 88  
ASP   CG  OD2  sing N N 89  
ASP   OD2 HD2  sing N N 90  
ASP   OXT HXT  sing N N 91  
GLN   N   CA   sing N N 92  
GLN   N   H    sing N N 93  
GLN   N   H2   sing N N 94  
GLN   CA  C    sing N N 95  
GLN   CA  CB   sing N N 96  
GLN   CA  HA   sing N N 97  
GLN   C   O    doub N N 98  
GLN   C   OXT  sing N N 99  
GLN   CB  CG   sing N N 100 
GLN   CB  HB2  sing N N 101 
GLN   CB  HB3  sing N N 102 
GLN   CG  CD   sing N N 103 
GLN   CG  HG2  sing N N 104 
GLN   CG  HG3  sing N N 105 
GLN   CD  OE1  doub N N 106 
GLN   CD  NE2  sing N N 107 
GLN   NE2 HE21 sing N N 108 
GLN   NE2 HE22 sing N N 109 
GLN   OXT HXT  sing N N 110 
GLU   N   CA   sing N N 111 
GLU   N   H    sing N N 112 
GLU   N   H2   sing N N 113 
GLU   CA  C    sing N N 114 
GLU   CA  CB   sing N N 115 
GLU   CA  HA   sing N N 116 
GLU   C   O    doub N N 117 
GLU   C   OXT  sing N N 118 
GLU   CB  CG   sing N N 119 
GLU   CB  HB2  sing N N 120 
GLU   CB  HB3  sing N N 121 
GLU   CG  CD   sing N N 122 
GLU   CG  HG2  sing N N 123 
GLU   CG  HG3  sing N N 124 
GLU   CD  OE1  doub N N 125 
GLU   CD  OE2  sing N N 126 
GLU   OE2 HE2  sing N N 127 
GLU   OXT HXT  sing N N 128 
GLY   N   CA   sing N N 129 
GLY   N   H    sing N N 130 
GLY   N   H2   sing N N 131 
GLY   CA  C    sing N N 132 
GLY   CA  HA2  sing N N 133 
GLY   CA  HA3  sing N N 134 
GLY   C   O    doub N N 135 
GLY   C   OXT  sing N N 136 
GLY   OXT HXT  sing N N 137 
HIS   N   CA   sing N N 138 
HIS   N   H    sing N N 139 
HIS   N   H2   sing N N 140 
HIS   CA  C    sing N N 141 
HIS   CA  CB   sing N N 142 
HIS   CA  HA   sing N N 143 
HIS   C   O    doub N N 144 
HIS   C   OXT  sing N N 145 
HIS   CB  CG   sing N N 146 
HIS   CB  HB2  sing N N 147 
HIS   CB  HB3  sing N N 148 
HIS   CG  ND1  sing Y N 149 
HIS   CG  CD2  doub Y N 150 
HIS   ND1 CE1  doub Y N 151 
HIS   ND1 HD1  sing N N 152 
HIS   CD2 NE2  sing Y N 153 
HIS   CD2 HD2  sing N N 154 
HIS   CE1 NE2  sing Y N 155 
HIS   CE1 HE1  sing N N 156 
HIS   NE2 HE2  sing N N 157 
HIS   OXT HXT  sing N N 158 
HOH   O   H1   sing N N 159 
HOH   O   H2   sing N N 160 
ILE   N   CA   sing N N 161 
ILE   N   H    sing N N 162 
ILE   N   H2   sing N N 163 
ILE   CA  C    sing N N 164 
ILE   CA  CB   sing N N 165 
ILE   CA  HA   sing N N 166 
ILE   C   O    doub N N 167 
ILE   C   OXT  sing N N 168 
ILE   CB  CG1  sing N N 169 
ILE   CB  CG2  sing N N 170 
ILE   CB  HB   sing N N 171 
ILE   CG1 CD1  sing N N 172 
ILE   CG1 HG12 sing N N 173 
ILE   CG1 HG13 sing N N 174 
ILE   CG2 HG21 sing N N 175 
ILE   CG2 HG22 sing N N 176 
ILE   CG2 HG23 sing N N 177 
ILE   CD1 HD11 sing N N 178 
ILE   CD1 HD12 sing N N 179 
ILE   CD1 HD13 sing N N 180 
ILE   OXT HXT  sing N N 181 
LEU   N   CA   sing N N 182 
LEU   N   H    sing N N 183 
LEU   N   H2   sing N N 184 
LEU   CA  C    sing N N 185 
LEU   CA  CB   sing N N 186 
LEU   CA  HA   sing N N 187 
LEU   C   O    doub N N 188 
LEU   C   OXT  sing N N 189 
LEU   CB  CG   sing N N 190 
LEU   CB  HB2  sing N N 191 
LEU   CB  HB3  sing N N 192 
LEU   CG  CD1  sing N N 193 
LEU   CG  CD2  sing N N 194 
LEU   CG  HG   sing N N 195 
LEU   CD1 HD11 sing N N 196 
LEU   CD1 HD12 sing N N 197 
LEU   CD1 HD13 sing N N 198 
LEU   CD2 HD21 sing N N 199 
LEU   CD2 HD22 sing N N 200 
LEU   CD2 HD23 sing N N 201 
LEU   OXT HXT  sing N N 202 
LYS   N   CA   sing N N 203 
LYS   N   H    sing N N 204 
LYS   N   H2   sing N N 205 
LYS   CA  C    sing N N 206 
LYS   CA  CB   sing N N 207 
LYS   CA  HA   sing N N 208 
LYS   C   O    doub N N 209 
LYS   C   OXT  sing N N 210 
LYS   CB  CG   sing N N 211 
LYS   CB  HB2  sing N N 212 
LYS   CB  HB3  sing N N 213 
LYS   CG  CD   sing N N 214 
LYS   CG  HG2  sing N N 215 
LYS   CG  HG3  sing N N 216 
LYS   CD  CE   sing N N 217 
LYS   CD  HD2  sing N N 218 
LYS   CD  HD3  sing N N 219 
LYS   CE  NZ   sing N N 220 
LYS   CE  HE2  sing N N 221 
LYS   CE  HE3  sing N N 222 
LYS   NZ  HZ1  sing N N 223 
LYS   NZ  HZ2  sing N N 224 
LYS   NZ  HZ3  sing N N 225 
LYS   OXT HXT  sing N N 226 
MET   N   CA   sing N N 227 
MET   N   H    sing N N 228 
MET   N   H2   sing N N 229 
MET   CA  C    sing N N 230 
MET   CA  CB   sing N N 231 
MET   CA  HA   sing N N 232 
MET   C   O    doub N N 233 
MET   C   OXT  sing N N 234 
MET   CB  CG   sing N N 235 
MET   CB  HB2  sing N N 236 
MET   CB  HB3  sing N N 237 
MET   CG  SD   sing N N 238 
MET   CG  HG2  sing N N 239 
MET   CG  HG3  sing N N 240 
MET   SD  CE   sing N N 241 
MET   CE  HE1  sing N N 242 
MET   CE  HE2  sing N N 243 
MET   CE  HE3  sing N N 244 
MET   OXT HXT  sing N N 245 
PHE   N   CA   sing N N 246 
PHE   N   H    sing N N 247 
PHE   N   H2   sing N N 248 
PHE   CA  C    sing N N 249 
PHE   CA  CB   sing N N 250 
PHE   CA  HA   sing N N 251 
PHE   C   O    doub N N 252 
PHE   C   OXT  sing N N 253 
PHE   CB  CG   sing N N 254 
PHE   CB  HB2  sing N N 255 
PHE   CB  HB3  sing N N 256 
PHE   CG  CD1  doub Y N 257 
PHE   CG  CD2  sing Y N 258 
PHE   CD1 CE1  sing Y N 259 
PHE   CD1 HD1  sing N N 260 
PHE   CD2 CE2  doub Y N 261 
PHE   CD2 HD2  sing N N 262 
PHE   CE1 CZ   doub Y N 263 
PHE   CE1 HE1  sing N N 264 
PHE   CE2 CZ   sing Y N 265 
PHE   CE2 HE2  sing N N 266 
PHE   CZ  HZ   sing N N 267 
PHE   OXT HXT  sing N N 268 
PRO   N   CA   sing N N 269 
PRO   N   CD   sing N N 270 
PRO   N   H    sing N N 271 
PRO   CA  C    sing N N 272 
PRO   CA  CB   sing N N 273 
PRO   CA  HA   sing N N 274 
PRO   C   O    doub N N 275 
PRO   C   OXT  sing N N 276 
PRO   CB  CG   sing N N 277 
PRO   CB  HB2  sing N N 278 
PRO   CB  HB3  sing N N 279 
PRO   CG  CD   sing N N 280 
PRO   CG  HG2  sing N N 281 
PRO   CG  HG3  sing N N 282 
PRO   CD  HD2  sing N N 283 
PRO   CD  HD3  sing N N 284 
PRO   OXT HXT  sing N N 285 
SER   N   CA   sing N N 286 
SER   N   H    sing N N 287 
SER   N   H2   sing N N 288 
SER   CA  C    sing N N 289 
SER   CA  CB   sing N N 290 
SER   CA  HA   sing N N 291 
SER   C   O    doub N N 292 
SER   C   OXT  sing N N 293 
SER   CB  OG   sing N N 294 
SER   CB  HB2  sing N N 295 
SER   CB  HB3  sing N N 296 
SER   OG  HG   sing N N 297 
SER   OXT HXT  sing N N 298 
THR   N   CA   sing N N 299 
THR   N   H    sing N N 300 
THR   N   H2   sing N N 301 
THR   CA  C    sing N N 302 
THR   CA  CB   sing N N 303 
THR   CA  HA   sing N N 304 
THR   C   O    doub N N 305 
THR   C   OXT  sing N N 306 
THR   CB  OG1  sing N N 307 
THR   CB  CG2  sing N N 308 
THR   CB  HB   sing N N 309 
THR   OG1 HG1  sing N N 310 
THR   CG2 HG21 sing N N 311 
THR   CG2 HG22 sing N N 312 
THR   CG2 HG23 sing N N 313 
THR   OXT HXT  sing N N 314 
TRP   N   CA   sing N N 315 
TRP   N   H    sing N N 316 
TRP   N   H2   sing N N 317 
TRP   CA  C    sing N N 318 
TRP   CA  CB   sing N N 319 
TRP   CA  HA   sing N N 320 
TRP   C   O    doub N N 321 
TRP   C   OXT  sing N N 322 
TRP   CB  CG   sing N N 323 
TRP   CB  HB2  sing N N 324 
TRP   CB  HB3  sing N N 325 
TRP   CG  CD1  doub Y N 326 
TRP   CG  CD2  sing Y N 327 
TRP   CD1 NE1  sing Y N 328 
TRP   CD1 HD1  sing N N 329 
TRP   CD2 CE2  doub Y N 330 
TRP   CD2 CE3  sing Y N 331 
TRP   NE1 CE2  sing Y N 332 
TRP   NE1 HE1  sing N N 333 
TRP   CE2 CZ2  sing Y N 334 
TRP   CE3 CZ3  doub Y N 335 
TRP   CE3 HE3  sing N N 336 
TRP   CZ2 CH2  doub Y N 337 
TRP   CZ2 HZ2  sing N N 338 
TRP   CZ3 CH2  sing Y N 339 
TRP   CZ3 HZ3  sing N N 340 
TRP   CH2 HH2  sing N N 341 
TRP   OXT HXT  sing N N 342 
TYR   N   CA   sing N N 343 
TYR   N   H    sing N N 344 
TYR   N   H2   sing N N 345 
TYR   CA  C    sing N N 346 
TYR   CA  CB   sing N N 347 
TYR   CA  HA   sing N N 348 
TYR   C   O    doub N N 349 
TYR   C   OXT  sing N N 350 
TYR   CB  CG   sing N N 351 
TYR   CB  HB2  sing N N 352 
TYR   CB  HB3  sing N N 353 
TYR   CG  CD1  doub Y N 354 
TYR   CG  CD2  sing Y N 355 
TYR   CD1 CE1  sing Y N 356 
TYR   CD1 HD1  sing N N 357 
TYR   CD2 CE2  doub Y N 358 
TYR   CD2 HD2  sing N N 359 
TYR   CE1 CZ   doub Y N 360 
TYR   CE1 HE1  sing N N 361 
TYR   CE2 CZ   sing Y N 362 
TYR   CE2 HE2  sing N N 363 
TYR   CZ  OH   sing N N 364 
TYR   OH  HH   sing N N 365 
TYR   OXT HXT  sing N N 366 
VAL   N   CA   sing N N 367 
VAL   N   H    sing N N 368 
VAL   N   H2   sing N N 369 
VAL   CA  C    sing N N 370 
VAL   CA  CB   sing N N 371 
VAL   CA  HA   sing N N 372 
VAL   C   O    doub N N 373 
VAL   C   OXT  sing N N 374 
VAL   CB  CG1  sing N N 375 
VAL   CB  CG2  sing N N 376 
VAL   CB  HB   sing N N 377 
VAL   CG1 HG11 sing N N 378 
VAL   CG1 HG12 sing N N 379 
VAL   CG1 HG13 sing N N 380 
VAL   CG2 HG21 sing N N 381 
VAL   CG2 HG22 sing N N 382 
VAL   CG2 HG23 sing N N 383 
VAL   OXT HXT  sing N N 384 
# 
_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                    7HAA 
_atom_sites.fract_transf_matrix[1][1]   0.014948 
_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]   0.010996 
_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]   0.010172 
_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.
;
? 
CL ? ? 9.50761 7.44341 ? ? 1.04373  23.83732 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
N  ? ? 4.01032 2.96436 ? ? 19.97189 1.75589  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O  ? ? 4.49882 3.47563 ? ? 15.80542 1.70748  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
S  ? ? 9.55732 6.39887 ? ? 1.23737  29.19336 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . GLU   A 1 9   ? 5.67291   -29.37559 -38.10334 1.000 54.35956  ? 16  GLU   A N   1 
ATOM   2    C  CA  . GLU   A 1 9   ? 7.04693   -28.88666 -38.20515 1.000 55.15517  ? 16  GLU   A CA  1 
ATOM   3    C  C   . GLU   A 1 9   ? 7.33977   -27.92659 -37.04943 1.000 48.45041  ? 16  GLU   A C   1 
ATOM   4    O  O   . GLU   A 1 9   ? 6.76215   -26.84317 -36.96105 1.000 42.76224  ? 16  GLU   A O   1 
ATOM   5    C  CB  . GLU   A 1 9   ? 7.27723   -28.20768 -39.55946 1.000 64.88542  ? 16  GLU   A CB  1 
ATOM   6    C  CG  . GLU   A 1 9   ? 8.73601   -27.87556 -39.88856 1.000 70.95171  ? 16  GLU   A CG  1 
ATOM   7    C  CD  . GLU   A 1 9   ? 9.09584   -26.41236 -39.65435 1.000 88.25838  ? 16  GLU   A CD  1 
ATOM   8    O  OE1 . GLU   A 1 9   ? 8.37324   -25.71776 -38.90277 1.000 84.82909  ? 16  GLU   A OE1 1 
ATOM   9    O  OE2 . GLU   A 1 9   ? 10.10435  -25.95268 -40.23511 1.000 85.93947  ? 16  GLU   A OE2 1 
ATOM   10   N  N   . VAL   A 1 10  ? 8.24066   -28.32795 -36.16069 1.000 36.69366  ? 17  VAL   A N   1 
ATOM   11   C  CA  . VAL   A 1 10  ? 8.49515   -27.61011 -34.91811 1.000 28.94669  ? 17  VAL   A CA  1 
ATOM   12   C  C   . VAL   A 1 10  ? 9.86382   -26.94996 -35.00868 1.000 31.78886  ? 17  VAL   A C   1 
ATOM   13   O  O   . VAL   A 1 10  ? 10.85172  -27.60901 -35.35285 1.000 35.60263  ? 17  VAL   A O   1 
ATOM   14   C  CB  . VAL   A 1 10  ? 8.41781   -28.55758 -33.71281 1.000 45.03164  ? 17  VAL   A CB  1 
ATOM   15   C  CG1 . VAL   A 1 10  ? 8.73486   -27.81047 -32.43588 1.000 34.88909  ? 17  VAL   A CG1 1 
ATOM   16   C  CG2 . VAL   A 1 10  ? 7.04701   -29.21853 -33.65862 1.000 50.25752  ? 17  VAL   A CG2 1 
ATOM   17   N  N   . GLU   A 1 11  ? 9.91511   -25.64762 -34.74174 1.000 27.56688  ? 18  GLU   A N   1 
ATOM   18   C  CA  . GLU   A 1 11  ? 11.17472  -24.92423 -34.67091 1.000 26.26221  ? 18  GLU   A CA  1 
ATOM   19   C  C   . GLU   A 1 11  ? 11.55331  -24.69353 -33.21158 1.000 23.23415  ? 18  GLU   A C   1 
ATOM   20   O  O   . GLU   A 1 11  ? 10.71389  -24.30758 -32.39934 1.000 23.37435  ? 18  GLU   A O   1 
ATOM   21   C  CB  . GLU   A 1 11  ? 11.09502  -23.58144 -35.40183 1.000 26.06621  ? 18  GLU   A CB  1 
ATOM   22   C  CG  . GLU   A 1 11  ? 10.92801  -23.71817 -36.89781 1.000 30.31365  ? 18  GLU   A CG  1 
ATOM   23   C  CD  . GLU   A 1 11  ? 10.84671  -22.37661 -37.59187 1.000 41.64571  ? 18  GLU   A CD  1 
ATOM   24   O  OE1 . GLU   A 1 11  ? 9.93252   -21.58700 -37.29207 1.000 43.72718  ? 18  GLU   A OE1 1 
ATOM   25   O  OE2 . GLU   A 1 11  ? 11.70244  -22.11846 -38.45626 1.000 45.49394  ? 18  GLU   A OE2 1 
ATOM   26   N  N   . THR   A 1 12  ? 12.82864  -24.90952 -32.88600 1.000 23.11919  ? 19  THR   A N   1 
ATOM   27   C  CA  . THR   A 1 12  ? 13.31900  -24.71929 -31.52514 1.000 21.90553  ? 19  THR   A CA  1 
ATOM   28   C  C   . THR   A 1 12  ? 14.30050  -23.55275 -31.51211 1.000 21.97635  ? 19  THR   A C   1 
ATOM   29   O  O   . THR   A 1 12  ? 15.17935  -23.47616 -32.37889 1.000 23.63033  ? 19  THR   A O   1 
ATOM   30   C  CB  . THR   A 1 12  ? 14.00245  -25.98794 -30.99909 1.000 26.64949  ? 19  THR   A CB  1 
ATOM   31   O  OG1 . THR   A 1 12  ? 13.08986  -27.09442 -31.09235 1.000 26.14522  ? 19  THR   A OG1 1 
ATOM   32   C  CG2 . THR   A 1 12  ? 14.44567  -25.80123 -29.53535 1.000 26.47216  ? 19  THR   A CG2 1 
ATOM   33   N  N   . PHE   A 1 13  ? 14.14875  -22.66745 -30.52675 1.000 22.84382  ? 20  PHE   A N   1 
ATOM   34   C  CA  . PHE   A 1 13  ? 14.92679  -21.43960 -30.39848 1.000 24.06159  ? 20  PHE   A CA  1 
ATOM   35   C  C   . PHE   A 1 13  ? 15.54441  -21.36521 -29.01444 1.000 26.10909  ? 20  PHE   A C   1 
ATOM   36   O  O   . PHE   A 1 13  ? 14.96695  -21.85621 -28.04605 1.000 23.87099  ? 20  PHE   A O   1 
ATOM   37   C  CB  . PHE   A 1 13  ? 14.04803  -20.19554 -30.59048 1.000 21.83238  ? 20  PHE   A CB  1 
ATOM   38   C  CG  . PHE   A 1 13  ? 13.31550  -20.16445 -31.89360 1.000 23.71883  ? 20  PHE   A CG  1 
ATOM   39   C  CD1 . PHE   A 1 13  ? 12.08764  -20.80668 -32.03566 1.000 24.98498  ? 20  PHE   A CD1 1 
ATOM   40   C  CD2 . PHE   A 1 13  ? 13.86448  -19.51857 -32.99859 1.000 26.32524  ? 20  PHE   A CD2 1 
ATOM   41   C  CE1 . PHE   A 1 13  ? 11.41588  -20.77855 -33.24548 1.000 23.95045  ? 20  PHE   A CE1 1 
ATOM   42   C  CE2 . PHE   A 1 13  ? 13.18982  -19.47839 -34.21469 1.000 26.88787  ? 20  PHE   A CE2 1 
ATOM   43   C  CZ  . PHE   A 1 13  ? 11.96934  -20.11751 -34.34512 1.000 25.63284  ? 20  PHE   A CZ  1 
ATOM   44   N  N   . ALA   A 1 14  ? 16.72177  -20.74236 -28.92291 1.000 22.12822  ? 21  ALA   A N   1 
ATOM   45   C  CA  . ALA   A 1 14  ? 17.33162  -20.43625 -27.63420 1.000 23.04169  ? 21  ALA   A CA  1 
ATOM   46   C  C   . ALA   A 1 14  ? 16.81266  -19.09081 -27.14782 1.000 25.19328  ? 21  ALA   A C   1 
ATOM   47   O  O   . ALA   A 1 14  ? 16.73732  -18.13458 -27.92430 1.000 27.38067  ? 21  ALA   A O   1 
ATOM   48   C  CB  . ALA   A 1 14  ? 18.85763  -20.40057 -27.75237 1.000 25.54697  ? 21  ALA   A CB  1 
ATOM   49   N  N   . PHE   A 1 15  ? 16.43939  -19.01440 -25.87304 1.000 24.22746  ? 22  PHE   A N   1 
ATOM   50   C  CA  . PHE   A 1 15  ? 16.23810  -17.69702 -25.29462 1.000 23.17658  ? 22  PHE   A CA  1 
ATOM   51   C  C   . PHE   A 1 15  ? 17.55003  -16.92853 -25.32325 1.000 25.34592  ? 22  PHE   A C   1 
ATOM   52   O  O   . PHE   A 1 15  ? 18.63682  -17.50260 -25.23048 1.000 31.08877  ? 22  PHE   A O   1 
ATOM   53   C  CB  . PHE   A 1 15  ? 15.76904  -17.79121 -23.84065 1.000 23.82056  ? 22  PHE   A CB  1 
ATOM   54   C  CG  . PHE   A 1 15  ? 14.34372  -18.22563 -23.67560 1.000 24.51295  ? 22  PHE   A CG  1 
ATOM   55   C  CD1 . PHE   A 1 15  ? 13.28498  -17.37345 -23.97379 1.000 24.84588  ? 22  PHE   A CD1 1 
ATOM   56   C  CD2 . PHE   A 1 15  ? 14.07365  -19.48206 -23.17131 1.000 21.85157  ? 22  PHE   A CD2 1 
ATOM   57   C  CE1 . PHE   A 1 15  ? 11.96781  -17.79674 -23.80019 1.000 24.66674  ? 22  PHE   A CE1 1 
ATOM   58   C  CE2 . PHE   A 1 15  ? 12.75770  -19.91680 -22.97998 1.000 23.33706  ? 22  PHE   A CE2 1 
ATOM   59   C  CZ  . PHE   A 1 15  ? 11.71086  -19.07281 -23.29127 1.000 22.94530  ? 22  PHE   A CZ  1 
ATOM   60   N  N   . GLN   A 1 16  ? 17.44439  -15.61674 -25.43212 1.000 26.36242  ? 23  GLN   A N   1 
ATOM   61   C  CA  . GLN   A 1 16  ? 18.59048  -14.79085 -25.09962 1.000 29.66877  ? 23  GLN   A CA  1 
ATOM   62   C  C   . GLN   A 1 16  ? 19.05736  -15.09098 -23.68085 1.000 31.05423  ? 23  GLN   A C   1 
ATOM   63   O  O   . GLN   A 1 16  ? 18.25830  -15.41960 -22.79750 1.000 30.09958  ? 23  GLN   A O   1 
ATOM   64   C  CB  . GLN   A 1 16  ? 18.21677  -13.33029 -25.20944 1.000 32.48028  ? 23  GLN   A CB  1 
ATOM   65   C  CG  . GLN   A 1 16  ? 17.93844  -12.87762 -26.59645 1.000 38.55560  ? 23  GLN   A CG  1 
ATOM   66   C  CD  . GLN   A 1 16  ? 17.27449  -11.53736 -26.55075 1.000 50.25956  ? 23  GLN   A CD  1 
ATOM   67   O  OE1 . GLN   A 1 16  ? 17.91026  -10.51140 -26.78480 1.000 44.26798  ? 23  GLN   A OE1 1 
ATOM   68   N  NE2 . GLN   A 1 16  ? 15.99630  -11.52676 -26.18343 1.000 43.56972  ? 23  GLN   A NE2 1 
ATOM   69   N  N   . ALA   A 1 17  ? 20.37144  -14.98149 -23.46871 1.000 31.69251  ? 24  ALA   A N   1 
ATOM   70   C  CA  . ALA   A 1 17  ? 20.93786  -15.31602 -22.17107 1.000 34.65529  ? 24  ALA   A CA  1 
ATOM   71   C  C   . ALA   A 1 17  ? 20.23578  -14.56118 -21.04793 1.000 32.56099  ? 24  ALA   A C   1 
ATOM   72   O  O   . ALA   A 1 17  ? 19.97474  -15.12630 -19.98013 1.000 31.35752  ? 24  ALA   A O   1 
ATOM   73   C  CB  . ALA   A 1 17  ? 22.44236  -15.02947 -22.16846 1.000 33.72839  ? 24  ALA   A CB  1 
ATOM   74   N  N   . GLU   A 1 18  ? 19.87664  -13.29692 -21.28844 1.000 31.29290  ? 25  GLU   A N   1 
ATOM   75   C  CA  . GLU   A 1 18  ? 19.28141  -12.49220 -20.22451 1.000 31.87580  ? 25  GLU   A CA  1 
ATOM   76   C  C   . GLU   A 1 18  ? 17.90476  -13.01215 -19.83016 1.000 30.56495  ? 25  GLU   A C   1 
ATOM   77   O  O   . GLU   A 1 18  ? 17.56680  -13.03313 -18.64067 1.000 31.64454  ? 25  GLU   A O   1 
ATOM   78   C  CB  . GLU   A 1 18  ? 19.18430  -11.03301 -20.65638 1.000 37.75283  ? 25  GLU   A CB  1 
ATOM   79   C  CG  . GLU   A 1 18  ? 20.52539  -10.33407 -20.83645 1.000 46.53453  ? 25  GLU   A CG  1 
ATOM   80   C  CD  . GLU   A 1 18  ? 21.23707  -10.69773 -22.13993 1.000 55.28716  ? 25  GLU   A CD  1 
ATOM   81   O  OE1 . GLU   A 1 18  ? 20.61594  -11.35035 -23.01282 1.000 38.17126  ? 25  GLU   A OE1 1 
ATOM   82   O  OE2 . GLU   A 1 18  ? 22.41708  -10.30949 -22.30088 1.000 55.10253  ? 25  GLU   A OE2 1 
ATOM   83   N  N   . ILE   A 1 19  ? 17.08935  -13.40842 -20.81704 1.000 26.65044  ? 26  ILE   A N   1 
ATOM   84   C  CA  . ILE   A 1 19  ? 15.75925  -13.95001 -20.53641 1.000 27.46079  ? 26  ILE   A CA  1 
ATOM   85   C  C   . ILE   A 1 19  ? 15.85561  -15.30785 -19.86100 1.000 30.38076  ? 26  ILE   A C   1 
ATOM   86   O  O   . ILE   A 1 19  ? 15.07531  -15.61598 -18.94878 1.000 26.36076  ? 26  ILE   A O   1 
ATOM   87   C  CB  . ILE   A 1 19  ? 14.91964  -14.02674 -21.82473 1.000 28.36541  ? 26  ILE   A CB  1 
ATOM   88   C  CG1 . ILE   A 1 19  ? 14.82247  -12.63461 -22.43540 1.000 36.67626  ? 26  ILE   A CG1 1 
ATOM   89   C  CG2 . ILE   A 1 19  ? 13.54689  -14.67056 -21.54382 1.000 28.40072  ? 26  ILE   A CG2 1 
ATOM   90   C  CD1 . ILE   A 1 19  ? 13.87252  -11.77612 -21.68979 1.000 45.33586  ? 26  ILE   A CD1 1 
ATOM   91   N  N   . ALA   A 1 20  ? 16.78089  -16.15790 -20.31800 1.000 25.47412  ? 27  ALA   A N   1 
ATOM   92   C  CA  . ALA   A 1 20  ? 17.02535  -17.41699 -19.61892 1.000 26.25425  ? 27  ALA   A CA  1 
ATOM   93   C  C   . ALA   A 1 20  ? 17.36377  -17.17126 -18.15472 1.000 25.61736  ? 27  ALA   A C   1 
ATOM   94   O  O   . ALA   A 1 20  ? 16.87906  -17.88453 -17.27033 1.000 26.65480  ? 27  ALA   A O   1 
ATOM   95   C  CB  . ALA   A 1 20  ? 18.15866  -18.19973 -20.29439 1.000 28.30346  ? 27  ALA   A CB  1 
ATOM   96   N  N   . GLN   A 1 21  ? 18.19655  -16.16315 -17.88163 1.000 25.46943  ? 28  GLN   A N   1 
ATOM   97   C  CA  . GLN   A 1 21  ? 18.56635  -15.83986 -16.50816 1.000 28.01658  ? 28  GLN   A CA  1 
ATOM   98   C  C   . GLN   A 1 21  ? 17.35314  -15.37831 -15.70707 1.000 25.73174  ? 28  GLN   A C   1 
ATOM   99   O  O   . GLN   A 1 21  ? 17.17963  -15.76027 -14.53878 1.000 30.41928  ? 28  GLN   A O   1 
ATOM   100  C  CB  . GLN   A 1 21  ? 19.65190  -14.76157 -16.52034 1.000 31.20274  ? 28  GLN   A CB  1 
ATOM   101  C  CG  . GLN   A 1 21  ? 20.36945  -14.55163 -15.21205 1.000 43.31026  ? 28  GLN   A CG  1 
ATOM   102  C  CD  . GLN   A 1 21  ? 21.47324  -13.52129 -15.35896 1.000 60.92909  ? 28  GLN   A CD  1 
ATOM   103  O  OE1 . GLN   A 1 21  ? 21.59193  -12.87322 -16.40546 1.000 59.56352  ? 28  GLN   A OE1 1 
ATOM   104  N  NE2 . GLN   A 1 21  ? 22.29582  -13.37438 -14.32483 1.000 63.57306  ? 28  GLN   A NE2 1 
ATOM   105  N  N   . LEU   A 1 22  ? 16.49927  -14.56271 -16.32385 1.000 25.89908  ? 29  LEU   A N   1 
ATOM   106  C  CA  . LEU   A 1 22  ? 15.26028  -14.14856 -15.67385 1.000 26.97377  ? 29  LEU   A CA  1 
ATOM   107  C  C   . LEU   A 1 22  ? 14.38259  -15.35250 -15.34007 1.000 25.16083  ? 29  LEU   A C   1 
ATOM   108  O  O   . LEU   A 1 22  ? 13.82834  -15.44967 -14.23805 1.000 27.26176  ? 29  LEU   A O   1 
ATOM   109  C  CB  . LEU   A 1 22  ? 14.50755  -13.17836 -16.58292 1.000 29.06241  ? 29  LEU   A CB  1 
ATOM   110  C  CG  . LEU   A 1 22  ? 13.10473  -12.83914 -16.07658 1.000 34.64816  ? 29  LEU   A CG  1 
ATOM   111  C  CD1 . LEU   A 1 22  ? 13.22741  -12.02303 -14.80666 1.000 29.19799  ? 29  LEU   A CD1 1 
ATOM   112  C  CD2 . LEU   A 1 22  ? 12.26692  -12.12338 -17.13953 1.000 32.70379  ? 29  LEU   A CD2 1 
ATOM   113  N  N   . MET   A 1 23  ? 14.21379  -16.27565 -16.29102 1.000 24.29888  ? 30  MET   A N   1 
ATOM   114  C  CA  . MET   A 1 23  ? 13.34746  -17.42098 -16.00522 1.000 20.92784  ? 30  MET   A CA  1 
ATOM   115  C  C   . MET   A 1 23  ? 13.92747  -18.29139 -14.89696 1.000 24.68879  ? 30  MET   A C   1 
ATOM   116  O  O   . MET   A 1 23  ? 13.18744  -18.76836 -14.02566 1.000 26.22508  ? 30  MET   A O   1 
ATOM   117  C  CB  . MET   A 1 23  ? 13.06550  -18.24077 -17.26797 1.000 23.40401  ? 30  MET   A CB  1 
ATOM   118  C  CG  . MET   A 1 23  ? 12.37438  -17.40269 -18.34523 1.000 22.05206  ? 30  MET   A CG  1 
ATOM   119  S  SD  . MET   A 1 23  ? 12.31884  -18.22877 -19.93972 1.000 26.34518  ? 30  MET   A SD  1 
ATOM   120  C  CE  . MET   A 1 23  ? 11.12447  -19.51052 -19.57847 1.000 28.81181  ? 30  MET   A CE  1 
ATOM   121  N  N   . SER   A 1 24  ? 15.25344  -18.47464 -14.87388 1.000 25.54033  ? 31  SER   A N   1 
ATOM   122  C  CA  . SER   A 1 24  ? 15.84027  -19.22783 -13.77293 1.000 25.32886  ? 31  SER   A CA  1 
ATOM   123  C  C   . SER   A 1 24  ? 15.60546  -18.53163 -12.44403 1.000 28.37964  ? 31  SER   A C   1 
ATOM   124  O  O   . SER   A 1 24  ? 15.34105  -19.18998 -11.43482 1.000 30.88654  ? 31  SER   A O   1 
ATOM   125  C  CB  . SER   A 1 24  ? 17.33628  -19.45341 -13.98914 1.000 30.79956  ? 31  SER   A CB  1 
ATOM   126  O  OG  . SER   A 1 24  ? 17.56938  -20.13520 -15.20304 1.000 39.29988  ? 31  SER   A OG  1 
ATOM   127  N  N   . LEU   A 1 25  ? 15.71080  -17.20157 -12.41556 1.000 25.13002  ? 32  LEU   A N   1 
ATOM   128  C  CA  . LEU   A 1 25  ? 15.47880  -16.48949 -11.16212 1.000 26.21928  ? 32  LEU   A CA  1 
ATOM   129  C  C   . LEU   A 1 25  ? 14.04714  -16.69490 -10.69107 1.000 27.35503  ? 32  LEU   A C   1 
ATOM   130  O  O   . LEU   A 1 25  ? 13.79986  -16.93748 -9.50387  1.000 29.55765  ? 32  LEU   A O   1 
ATOM   131  C  CB  . LEU   A 1 25  ? 15.78496  -15.00151 -11.34821 1.000 30.14605  ? 32  LEU   A CB  1 
ATOM   132  C  CG  . LEU   A 1 25  ? 15.58008  -14.03224 -10.17135 1.000 36.60142  ? 32  LEU   A CG  1 
ATOM   133  C  CD1 . LEU   A 1 25  ? 16.56674  -12.88523 -10.31563 1.000 42.55360  ? 32  LEU   A CD1 1 
ATOM   134  C  CD2 . LEU   A 1 25  ? 14.15016  -13.49442 -10.05141 1.000 43.41109  ? 32  LEU   A CD2 1 
ATOM   135  N  N   . ILE   A 1 26  ? 13.09067  -16.61351 -11.61602 1.000 24.56530  ? 33  ILE   A N   1 
ATOM   136  C  CA  . ILE   A 1 26  ? 11.68457  -16.75449 -11.25024 1.000 24.29116  ? 33  ILE   A CA  1 
ATOM   137  C  C   . ILE   A 1 26  ? 11.40636  -18.16630 -10.75290 1.000 28.32114  ? 33  ILE   A C   1 
ATOM   138  O  O   . ILE   A 1 26  ? 10.64107  -18.37289 -9.80254  1.000 28.80606  ? 33  ILE   A O   1 
ATOM   139  C  CB  . ILE   A 1 26  ? 10.80576  -16.38013 -12.45319 1.000 22.72369  ? 33  ILE   A CB  1 
ATOM   140  C  CG1 . ILE   A 1 26  ? 10.82656  -14.86182 -12.63664 1.000 24.81301  ? 33  ILE   A CG1 1 
ATOM   141  C  CG2 . ILE   A 1 26  ? 9.37892   -16.92321 -12.26826 1.000 25.89319  ? 33  ILE   A CG2 1 
ATOM   142  C  CD1 . ILE   A 1 26  ? 10.34465  -14.41005 -14.01154 1.000 29.47005  ? 33  ILE   A CD1 1 
ATOM   143  N  N   . ILE   A 1 27  ? 12.05002  -19.15715 -11.36685 1.000 28.08830  ? 34  ILE   A N   1 
ATOM   144  C  CA  . ILE   A 1 27  ? 11.81624  -20.54756 -10.99053 1.000 29.62826  ? 34  ILE   A CA  1 
ATOM   145  C  C   . ILE   A 1 27  ? 12.52641  -20.90167 -9.68935  1.000 30.87609  ? 34  ILE   A C   1 
ATOM   146  O  O   . ILE   A 1 27  ? 12.00356  -21.67705 -8.87904  1.000 35.69923  ? 34  ILE   A O   1 
ATOM   147  C  CB  . ILE   A 1 27  ? 12.24816  -21.44961 -12.15920 1.000 29.23572  ? 34  ILE   A CB  1 
ATOM   148  C  CG1 . ILE   A 1 27  ? 11.23817  -21.31449 -13.29984 1.000 24.49916  ? 34  ILE   A CG1 1 
ATOM   149  C  CG2 . ILE   A 1 27  ? 12.38597  -22.91094 -11.71472 1.000 36.92121  ? 34  ILE   A CG2 1 
ATOM   150  C  CD1 . ILE   A 1 27  ? 11.77218  -21.81560 -14.61234 1.000 27.44975  ? 34  ILE   A CD1 1 
ATOM   151  N  N   . ASN   A 1 28  ? 13.68662  -20.31276 -9.42112  1.000 31.14860  ? 35  ASN   A N   1 
ATOM   152  C  CA  . ASN   A 1 28  ? 14.50397  -20.78032 -8.30808  1.000 31.83889  ? 35  ASN   A CA  1 
ATOM   153  C  C   . ASN   A 1 28  ? 14.42976  -19.91412 -7.05916  1.000 32.99835  ? 35  ASN   A C   1 
ATOM   154  O  O   . ASN   A 1 28  ? 14.81859  -20.38285 -5.98502  1.000 38.82524  ? 35  ASN   A O   1 
ATOM   155  C  CB  . ASN   A 1 28  ? 15.95880  -20.89479 -8.75992  1.000 37.60209  ? 35  ASN   A CB  1 
ATOM   156  C  CG  . ASN   A 1 28  ? 16.12819  -21.94045 -9.83405  1.000 50.03203  ? 35  ASN   A CG  1 
ATOM   157  O  OD1 . ASN   A 1 28  ? 15.43721  -22.95836 -9.82486  1.000 45.05386  ? 35  ASN   A OD1 1 
ATOM   158  N  ND2 . ASN   A 1 28  ? 17.01941  -21.68548 -10.78419 1.000 49.97038  ? 35  ASN   A ND2 1 
ATOM   159  N  N   . THR   A 1 29  ? 13.95913  -18.67751 -7.15509  1.000 30.98409  ? 36  THR   A N   1 
ATOM   160  C  CA  . THR   A 1 29  ? 13.95993  -17.80253 -5.99025  1.000 35.59669  ? 36  THR   A CA  1 
ATOM   161  C  C   . THR   A 1 29  ? 12.79642  -18.17319 -5.07454  1.000 33.41626  ? 36  THR   A C   1 
ATOM   162  O  O   . THR   A 1 29  ? 11.69578  -18.47998 -5.54212  1.000 36.92619  ? 36  THR   A O   1 
ATOM   163  C  CB  . THR   A 1 29  ? 13.86742  -16.33507 -6.42616  1.000 39.52676  ? 36  THR   A CB  1 
ATOM   164  O  OG1 . THR   A 1 29  ? 15.04895  -15.98260 -7.15613  1.000 37.83996  ? 36  THR   A OG1 1 
ATOM   165  C  CG2 . THR   A 1 29  ? 13.75171  -15.41089 -5.23238  1.000 39.14228  ? 36  THR   A CG2 1 
ATOM   166  N  N   . PHE   A 1 30  ? 13.05064  -18.18481 -3.76527  1.000 31.63388  ? 37  PHE   A N   1 
ATOM   167  C  CA  . PHE   A 1 30  ? 11.96523  -18.41711 -2.82052  1.000 34.63971  ? 37  PHE   A CA  1 
ATOM   168  C  C   . PHE   A 1 30  ? 11.11845  -17.15413 -2.71780  1.000 34.69050  ? 37  PHE   A C   1 
ATOM   169  O  O   . PHE   A 1 30  ? 11.61945  -16.08449 -2.35023  1.000 35.41674  ? 37  PHE   A O   1 
ATOM   170  C  CB  . PHE   A 1 30  ? 12.50307  -18.82404 -1.45392  1.000 35.19134  ? 37  PHE   A CB  1 
ATOM   171  C  CG  . PHE   A 1 30  ? 11.42204  -19.13129 -0.44895  1.000 31.28436  ? 37  PHE   A CG  1 
ATOM   172  C  CD1 . PHE   A 1 30  ? 10.79164  -20.37044 -0.45441  1.000 43.58851  ? 37  PHE   A CD1 1 
ATOM   173  C  CD2 . PHE   A 1 30  ? 11.04056  -18.18930 0.49711   1.000 34.00982  ? 37  PHE   A CD2 1 
ATOM   174  C  CE1 . PHE   A 1 30  ? 9.79510   -20.66992 0.46685   1.000 43.87708  ? 37  PHE   A CE1 1 
ATOM   175  C  CE2 . PHE   A 1 30  ? 10.03878  -18.48050 1.43045   1.000 37.25957  ? 37  PHE   A CE2 1 
ATOM   176  C  CZ  . PHE   A 1 30  ? 9.41806   -19.72670 1.40874   1.000 33.98028  ? 37  PHE   A CZ  1 
ATOM   177  N  N   . TYR   A 1 31  ? 9.83377   -17.28082 -3.03377  1.000 29.38516  ? 38  TYR   A N   1 
ATOM   178  C  CA  . TYR   A 1 31  ? 8.94045   -16.12631 -3.06309  1.000 26.80532  ? 38  TYR   A CA  1 
ATOM   179  C  C   . TYR   A 1 31  ? 7.51172   -16.64716 -2.95943  1.000 28.24498  ? 38  TYR   A C   1 
ATOM   180  O  O   . TYR   A 1 31  ? 7.03216   -17.30475 -3.88697  1.000 29.01063  ? 38  TYR   A O   1 
ATOM   181  C  CB  . TYR   A 1 31  ? 9.16050   -15.32350 -4.34337  1.000 28.65005  ? 38  TYR   A CB  1 
ATOM   182  C  CG  . TYR   A 1 31  ? 8.29380   -14.10121 -4.41874  1.000 29.92757  ? 38  TYR   A CG  1 
ATOM   183  C  CD1 . TYR   A 1 31  ? 8.59090   -12.98407 -3.65135  1.000 34.39896  ? 38  TYR   A CD1 1 
ATOM   184  C  CD2 . TYR   A 1 31  ? 7.19538   -14.04664 -5.27346  1.000 32.25039  ? 38  TYR   A CD2 1 
ATOM   185  C  CE1 . TYR   A 1 31  ? 7.81384   -11.86630 -3.69269  1.000 40.44971  ? 38  TYR   A CE1 1 
ATOM   186  C  CE2 . TYR   A 1 31  ? 6.40921   -12.91362 -5.33029  1.000 32.62861  ? 38  TYR   A CE2 1 
ATOM   187  C  CZ  . TYR   A 1 31  ? 6.72965   -11.82693 -4.53644  1.000 37.28845  ? 38  TYR   A CZ  1 
ATOM   188  O  OH  . TYR   A 1 31  ? 5.96961   -10.68079 -4.55846  1.000 41.03346  ? 38  TYR   A OH  1 
ATOM   189  N  N   . SER   A 1 32  ? 6.84264   -16.36820 -1.83711  1.000 29.27827  ? 39  SER   A N   1 
ATOM   190  C  CA  . SER   A 1 32  ? 5.57620   -17.03138 -1.55511  1.000 30.31689  ? 39  SER   A CA  1 
ATOM   191  C  C   . SER   A 1 32  ? 4.38636   -16.38221 -2.24861  1.000 34.46237  ? 39  SER   A C   1 
ATOM   192  O  O   . SER   A 1 32  ? 3.37035   -17.05984 -2.44758  1.000 34.60883  ? 39  SER   A O   1 
ATOM   193  C  CB  . SER   A 1 32  ? 5.33873   -17.08388 -0.04619  1.000 31.87046  ? 39  SER   A CB  1 
ATOM   194  O  OG  . SER   A 1 32  ? 6.34041   -17.88425 0.56004   1.000 34.57169  ? 39  SER   A OG  1 
ATOM   195  N  N   . ASN   A 1 33  ? 4.50350   -15.11312 -2.65430  1.000 27.59295  ? 40  ASN   A N   1 
ATOM   196  C  CA  . ASN   A 1 33  ? 3.38333   -14.33223 -3.20065  1.000 26.64799  ? 40  ASN   A CA  1 
ATOM   197  C  C   . ASN   A 1 33  ? 3.19754   -14.62467 -4.69443  1.000 28.60180  ? 40  ASN   A C   1 
ATOM   198  O  O   . ASN   A 1 33  ? 3.22961   -13.74562 -5.55713  1.000 27.72858  ? 40  ASN   A O   1 
ATOM   199  C  CB  . ASN   A 1 33  ? 3.62696   -12.84883 -2.93861  1.000 31.77117  ? 40  ASN   A CB  1 
ATOM   200  C  CG  . ASN   A 1 33  ? 2.46592   -11.95840 -3.35948  1.000 33.84740  ? 40  ASN   A CG  1 
ATOM   201  O  OD1 . ASN   A 1 33  ? 1.29608   -12.33178 -3.25378  1.000 33.45454  ? 40  ASN   A OD1 1 
ATOM   202  N  ND2 . ASN   A 1 33  ? 2.79617   -10.76184 -3.85355  1.000 36.51560  ? 40  ASN   A ND2 1 
ATOM   203  N  N   . LYS   A 1 34  ? 3.00539   -15.91137 -4.99514  1.000 24.21063  ? 41  LYS   A N   1 
ATOM   204  C  CA  . LYS   A 1 34  ? 2.96377   -16.33980 -6.38839  1.000 23.61804  ? 41  LYS   A CA  1 
ATOM   205  C  C   . LYS   A 1 34  ? 1.70148   -15.88529 -7.12185  1.000 24.57466  ? 41  LYS   A C   1 
ATOM   206  O  O   . LYS   A 1 34  ? 1.70719   -15.85690 -8.36258  1.000 23.28378  ? 41  LYS   A O   1 
ATOM   207  C  CB  . LYS   A 1 34  ? 3.09353   -17.86409 -6.45846  1.000 26.10188  ? 41  LYS   A CB  1 
ATOM   208  C  CG  . LYS   A 1 34  ? 4.50328   -18.41450 -6.16115  1.000 27.36143  ? 41  LYS   A CG  1 
ATOM   209  C  CD  . LYS   A 1 34  ? 4.42973   -19.93786 -6.09929  1.000 31.31847  ? 41  LYS   A CD  1 
ATOM   210  C  CE  . LYS   A 1 34  ? 5.76007   -20.62386 -5.76168  1.000 30.99255  ? 41  LYS   A CE  1 
ATOM   211  N  NZ  . LYS   A 1 34  ? 6.78219   -20.53472 -6.84411  1.000 34.05036  ? 41  LYS   A NZ  1 
ATOM   212  N  N   . GLU   A 1 35  ? 0.64622   -15.49435 -6.39873  1.000 25.49851  ? 42  GLU   A N   1 
ATOM   213  C  CA  . GLU   A 1 35  ? -0.62606  -15.21377 -7.06259  1.000 24.10216  ? 42  GLU   A CA  1 
ATOM   214  C  C   . GLU   A 1 35  ? -0.54527  -14.04281 -8.02373  1.000 27.81919  ? 42  GLU   A C   1 
ATOM   215  O  O   . GLU   A 1 35  ? -1.45866  -13.86910 -8.84551  1.000 24.88347  ? 42  GLU   A O   1 
ATOM   216  C  CB  . GLU   A 1 35  ? -1.74595  -14.90259 -6.06775  1.000 24.70263  ? 42  GLU   A CB  1 
ATOM   217  C  CG  . GLU   A 1 35  ? -1.51929  -13.62440 -5.28350  1.000 28.26683  ? 42  GLU   A CG  1 
ATOM   218  C  CD  . GLU   A 1 35  ? -2.43918  -13.48883 -4.07216  1.000 47.36512  ? 42  GLU   A CD  1 
ATOM   219  O  OE1 . GLU   A 1 35  ? -2.64923  -14.46620 -3.33216  1.000 39.12754  ? 42  GLU   A OE1 1 
ATOM   220  O  OE2 . GLU   A 1 35  ? -2.95493  -12.37252 -3.86324  1.000 46.19863  ? 42  GLU   A OE2 1 
ATOM   221  N  N   . ILE   A 1 36  ? 0.50789   -13.22547 -7.94396  1.000 24.42759  ? 43  ILE   A N   1 
ATOM   222  C  CA  . ILE   A 1 36  ? 0.59760   -12.08732 -8.84683  1.000 24.63124  ? 43  ILE   A CA  1 
ATOM   223  C  C   . ILE   A 1 36  ? 0.71957   -12.50352 -10.29807 1.000 23.89413  ? 43  ILE   A C   1 
ATOM   224  O  O   . ILE   A 1 36  ? 0.50866   -11.66759 -11.18243 1.000 23.92369  ? 43  ILE   A O   1 
ATOM   225  C  CB  . ILE   A 1 36  ? 1.76221   -11.15949 -8.44439  1.000 25.72023  ? 43  ILE   A CB  1 
ATOM   226  C  CG1 . ILE   A 1 36  ? 3.10994   -11.86503 -8.57135  1.000 30.34865  ? 43  ILE   A CG1 1 
ATOM   227  C  CG2 . ILE   A 1 36  ? 1.53661   -10.63265 -7.03326  1.000 31.55488  ? 43  ILE   A CG2 1 
ATOM   228  C  CD1 . ILE   A 1 36  ? 3.84651   -11.51841 -9.84272  1.000 37.86985  ? 43  ILE   A CD1 1 
ATOM   229  N  N   . PHE   A 1 37  ? 1.02542   -13.77538 -10.58821 1.000 21.72188  ? 44  PHE   A N   1 
ATOM   230  C  CA  . PHE   A 1 37  ? 1.09215   -14.17468 -11.98868 1.000 21.56214  ? 44  PHE   A CA  1 
ATOM   231  C  C   . PHE   A 1 37  ? -0.22281  -13.86630 -12.69531 1.000 22.37034  ? 44  PHE   A C   1 
ATOM   232  O  O   . PHE   A 1 37  ? -0.22730  -13.49679 -13.87608 1.000 22.52342  ? 44  PHE   A O   1 
ATOM   233  C  CB  . PHE   A 1 37  ? 1.42173   -15.66949 -12.14518 1.000 22.18295  ? 44  PHE   A CB  1 
ATOM   234  C  CG  . PHE   A 1 37  ? 0.22065   -16.57062 -11.95391 1.000 25.61977  ? 44  PHE   A CG  1 
ATOM   235  C  CD1 . PHE   A 1 37  ? -0.15364  -16.99501 -10.68355 1.000 23.03965  ? 44  PHE   A CD1 1 
ATOM   236  C  CD2 . PHE   A 1 37  ? -0.57906  -16.93383 -13.03857 1.000 22.60112  ? 44  PHE   A CD2 1 
ATOM   237  C  CE1 . PHE   A 1 37  ? -1.28647  -17.78284 -10.50142 1.000 24.35191  ? 44  PHE   A CE1 1 
ATOM   238  C  CE2 . PHE   A 1 37  ? -1.72481  -17.70830 -12.84343 1.000 20.01677  ? 44  PHE   A CE2 1 
ATOM   239  C  CZ  . PHE   A 1 37  ? -2.06062  -18.14408 -11.58590 1.000 25.49298  ? 44  PHE   A CZ  1 
ATOM   240  N  N   . LEU   A 1 38  ? -1.34929  -14.02416 -11.99775 1.000 22.72814  ? 45  LEU   A N   1 
ATOM   241  C  CA  . LEU   A 1 38  ? -2.63120  -13.86888 -12.67761 1.000 23.26903  ? 45  LEU   A CA  1 
ATOM   242  C  C   . LEU   A 1 38  ? -2.90137  -12.40322 -12.98585 1.000 23.82508  ? 45  LEU   A C   1 
ATOM   243  O  O   . LEU   A 1 38  ? -3.39050  -12.07068 -14.07309 1.000 23.51314  ? 45  LEU   A O   1 
ATOM   244  C  CB  . LEU   A 1 38  ? -3.76023  -14.47242 -11.83991 1.000 22.32621  ? 45  LEU   A CB  1 
ATOM   245  C  CG  . LEU   A 1 38  ? -5.13594  -14.46316 -12.52243 1.000 21.44521  ? 45  LEU   A CG  1 
ATOM   246  C  CD1 . LEU   A 1 38  ? -5.08789  -15.28149 -13.79068 1.000 23.44210  ? 45  LEU   A CD1 1 
ATOM   247  C  CD2 . LEU   A 1 38  ? -6.18566  -15.01312 -11.58713 1.000 25.30448  ? 45  LEU   A CD2 1 
ATOM   248  N  N   . ARG   A 1 39  ? -2.57528  -11.50794 -12.04570 1.000 21.61659  ? 46  ARG   A N   1 
ATOM   249  C  CA  . ARG   A 1 39  ? -2.67468  -10.07349 -12.32365 1.000 21.60757  ? 46  ARG   A CA  1 
ATOM   250  C  C   . ARG   A 1 39  ? -1.85883  -9.69452  -13.55317 1.000 24.64304  ? 46  ARG   A C   1 
ATOM   251  O  O   . ARG   A 1 39  ? -2.30111  -8.89306  -14.38883 1.000 24.65319  ? 46  ARG   A O   1 
ATOM   252  C  CB  . ARG   A 1 39  ? -2.17738  -9.27748  -11.11610 1.000 23.78937  ? 46  ARG   A CB  1 
ATOM   253  C  CG  . ARG   A 1 39  ? -2.13380  -7.76603  -11.32785 1.000 29.47672  ? 46  ARG   A CG  1 
ATOM   254  C  CD  . ARG   A 1 39  ? -1.42294  -7.04855  -10.15926 1.000 29.49005  ? 46  ARG   A CD  1 
ATOM   255  N  NE  . ARG   A 1 39  ? 0.00115   -7.36759  -10.08253 1.000 35.84827  ? 46  ARG   A NE  1 
ATOM   256  C  CZ  . ARG   A 1 39  ? 0.73835   -7.25822  -8.98247  1.000 36.15937  ? 46  ARG   A CZ  1 
ATOM   257  N  NH1 . ARG   A 1 39  ? 0.20469   -6.90946  -7.82435  1.000 35.28252  ? 46  ARG   A NH1 1 
ATOM   258  N  NH2 . ARG   A 1 39  ? 2.04721   -7.49659  -9.04845  1.000 37.96058  ? 46  ARG   A NH2 1 
ATOM   259  N  N   . GLU   A 1 40  ? -0.65057  -10.24654 -13.67058 1.000 21.97854  ? 47  GLU   A N   1 
ATOM   260  C  CA  . GLU   A 1 40  ? 0.22441   -9.88025  -14.77866 1.000 20.72339  ? 47  GLU   A CA  1 
ATOM   261  C  C   . GLU   A 1 40  ? -0.34588  -10.35858 -16.10791 1.000 21.94571  ? 47  GLU   A C   1 
ATOM   262  O  O   . GLU   A 1 40  ? -0.27376  -9.64076  -17.11051 1.000 22.81402  ? 47  GLU   A O   1 
ATOM   263  C  CB  . GLU   A 1 40  ? 1.61766   -10.47737 -14.56610 1.000 21.54514  ? 47  GLU   A CB  1 
ATOM   264  C  CG  . GLU   A 1 40  ? 2.42357   -9.87579  -13.41798 1.000 24.19988  ? 47  GLU   A CG  1 
ATOM   265  C  CD  . GLU   A 1 40  ? 2.29562   -8.36293  -13.30547 1.000 28.75429  ? 47  GLU   A CD  1 
ATOM   266  O  OE1 . GLU   A 1 40  ? 2.44251   -7.70142  -14.34246 1.000 30.73240  ? 47  GLU   A OE1 1 
ATOM   267  O  OE2 . GLU   A 1 40  ? 2.10360   -7.82697  -12.18168 1.000 32.31180  ? 47  GLU   A OE2 1 
ATOM   268  N  N   . LEU   A 1 41  ? -0.88181  -11.58562 -16.14621 1.000 21.41015  ? 48  LEU   A N   1 
ATOM   269  C  CA  . LEU   A 1 41  ? -1.41091  -12.11195 -17.39911 1.000 21.51893  ? 48  LEU   A CA  1 
ATOM   270  C  C   . LEU   A 1 41  ? -2.71303  -11.41678 -17.77672 1.000 22.09642  ? 48  LEU   A C   1 
ATOM   271  O  O   . LEU   A 1 41  ? -2.96166  -11.16188 -18.96210 1.000 21.65602  ? 48  LEU   A O   1 
ATOM   272  C  CB  . LEU   A 1 41  ? -1.61959  -13.62373 -17.29177 1.000 20.82444  ? 48  LEU   A CB  1 
ATOM   273  C  CG  . LEU   A 1 41  ? -0.31235  -14.40456 -17.10730 1.000 19.94039  ? 48  LEU   A CG  1 
ATOM   274  C  CD1 . LEU   A 1 41  ? -0.64637  -15.89137 -17.02187 1.000 23.52237  ? 48  LEU   A CD1 1 
ATOM   275  C  CD2 . LEU   A 1 41  ? 0.69162   -14.17064 -18.22946 1.000 23.31112  ? 48  LEU   A CD2 1 
ATOM   276  N  N   . ILE   A 1 42  ? -3.54504  -11.07859 -16.78368 1.000 19.90792  ? 49  ILE   A N   1 
ATOM   277  C  CA  . ILE   A 1 42  ? -4.77280  -10.34722 -17.08926 1.000 21.94778  ? 49  ILE   A CA  1 
ATOM   278  C  C   . ILE   A 1 42  ? -4.43478  -8.94646  -17.57553 1.000 24.84606  ? 49  ILE   A C   1 
ATOM   279  O  O   . ILE   A 1 42  ? -5.06111  -8.42485  -18.50897 1.000 21.94990  ? 49  ILE   A O   1 
ATOM   280  C  CB  . ILE   A 1 42  ? -5.71085  -10.33639 -15.86254 1.000 19.83366  ? 49  ILE   A CB  1 
ATOM   281  C  CG1 . ILE   A 1 42  ? -6.30463  -11.73190 -15.65267 1.000 20.88769  ? 49  ILE   A CG1 1 
ATOM   282  C  CG2 . ILE   A 1 42  ? -6.80755  -9.23994  -16.00176 1.000 24.18602  ? 49  ILE   A CG2 1 
ATOM   283  C  CD1 . ILE   A 1 42  ? -7.09924  -11.87494 -14.34637 1.000 21.70504  ? 49  ILE   A CD1 1 
ATOM   284  N  N   . SER   A 1 43  ? -3.41585  -8.33068  -16.97718 1.000 21.25742  ? 50  SER   A N   1 
ATOM   285  C  CA  . SER   A 1 43  ? -2.96785  -7.02615  -17.43663 1.000 24.36821  ? 50  SER   A CA  1 
ATOM   286  C  C   . SER   A 1 43  ? -2.46951  -7.09407  -18.87542 1.000 26.53514  ? 50  SER   A C   1 
ATOM   287  O  O   . SER   A 1 43  ? -2.77372  -6.21524  -19.69158 1.000 22.67771  ? 50  SER   A O   1 
ATOM   288  C  CB  . SER   A 1 43  ? -1.87323  -6.51086  -16.50411 1.000 28.09180  ? 50  SER   A CB  1 
ATOM   289  O  OG  . SER   A 1 43  ? -1.37969  -5.27023  -16.95206 1.000 34.38010  ? 50  SER   A OG  1 
ATOM   290  N  N   . ASN   A 1 44  ? -1.70050  -8.13469  -19.20692 1.000 22.77240  ? 51  ASN   A N   1 
ATOM   291  C  CA  . ASN   A 1 44  ? -1.26581  -8.30861  -20.58849 1.000 27.41111  ? 51  ASN   A CA  1 
ATOM   292  C  C   . ASN   A 1 44  ? -2.45280  -8.44873  -21.52813 1.000 25.93442  ? 51  ASN   A C   1 
ATOM   293  O  O   . ASN   A 1 44  ? -2.45966  -7.86006  -22.61928 1.000 23.80180  ? 51  ASN   A O   1 
ATOM   294  C  CB  . ASN   A 1 44  ? -0.36054  -9.53589  -20.70651 1.000 23.36023  ? 51  ASN   A CB  1 
ATOM   295  C  CG  . ASN   A 1 44  ? 1.03634   -9.28872  -20.17986 1.000 30.63984  ? 51  ASN   A CG  1 
ATOM   296  O  OD1 . ASN   A 1 44  ? 1.36929   -8.18838  -19.72046 1.000 30.74601  ? 51  ASN   A OD1 1 
ATOM   297  N  ND2 . ASN   A 1 44  ? 1.87259   -10.32229 -20.24449 1.000 33.99641  ? 51  ASN   A ND2 1 
ATOM   298  N  N   . SER   A 1 45  ? -3.45255  -9.24503  -21.13188 1.000 21.59414  ? 52  SER   A N   1 
ATOM   299  C  CA  . SER   A 1 45  ? -4.65853  -9.41627  -21.94307 1.000 21.51837  ? 52  SER   A CA  1 
ATOM   300  C  C   . SER   A 1 45  ? -5.37615  -8.09245  -22.14049 1.000 21.82879  ? 52  SER   A C   1 
ATOM   301  O  O   . SER   A 1 45  ? -5.80673  -7.76673  -23.25585 1.000 22.11835  ? 52  SER   A O   1 
ATOM   302  C  CB  . SER   A 1 45  ? -5.59211  -10.42521 -21.27747 1.000 20.34949  ? 52  SER   A CB  1 
ATOM   303  O  OG  . SER   A 1 45  ? -5.01310  -11.72009 -21.35321 1.000 24.13696  ? 52  SER   A OG  1 
ATOM   304  N  N   . SER   A 1 46  ? -5.53033  -7.33077  -21.06037 1.000 20.32877  ? 53  SER   A N   1 
ATOM   305  C  CA  . SER   A 1 46  ? -6.14945  -6.01637  -21.16116 1.000 22.50920  ? 53  SER   A CA  1 
ATOM   306  C  C   . SER   A 1 46  ? -5.39426  -5.11014  -22.13698 1.000 24.79602  ? 53  SER   A C   1 
ATOM   307  O  O   . SER   A 1 46  ? -6.01628  -4.38307  -22.92182 1.000 26.18708  ? 53  SER   A O   1 
ATOM   308  C  CB  . SER   A 1 46  ? -6.22631  -5.38928  -19.77086 1.000 24.04400  ? 53  SER   A CB  1 
ATOM   309  O  OG  . SER   A 1 46  ? -6.84826  -4.11313  -19.83076 1.000 27.17344  ? 53  SER   A OG  1 
ATOM   310  N  N   . ASP   A 1 47  ? -4.05603  -5.13043  -22.10575 1.000 23.44104  ? 54  ASP   A N   1 
ATOM   311  C  CA  . ASP   A 1 47  ? -3.30297  -4.28916  -23.03794 1.000 22.38856  ? 54  ASP   A CA  1 
ATOM   312  C  C   . ASP   A 1 47  ? -3.52588  -4.73737  -24.48092 1.000 25.27427  ? 54  ASP   A C   1 
ATOM   313  O  O   . ASP   A 1 47  ? -3.61733  -3.90769  -25.39447 1.000 23.91501  ? 54  ASP   A O   1 
ATOM   314  C  CB  . ASP   A 1 47  ? -1.80352  -4.32998  -22.73874 1.000 23.23752  ? 54  ASP   A CB  1 
ATOM   315  C  CG  . ASP   A 1 47  ? -1.43077  -3.69692  -21.40948 1.000 34.90336  ? 54  ASP   A CG  1 
ATOM   316  O  OD1 . ASP   A 1 47  ? -2.19808  -2.86755  -20.88425 1.000 32.89812  ? 54  ASP   A OD1 1 
ATOM   317  O  OD2 . ASP   A 1 47  ? -0.28841  -3.95146  -20.94984 1.000 33.74155  ? 54  ASP   A OD2 1 
ATOM   318  N  N   . ALA   A 1 48  ? -3.58555  -6.05139  -24.70964 1.000 23.46961  ? 55  ALA   A N   1 
ATOM   319  C  CA  . ALA   A 1 48  ? -3.80486  -6.56119  -26.05934 1.000 21.25218  ? 55  ALA   A CA  1 
ATOM   320  C  C   . ALA   A 1 48  ? -5.19442  -6.19188  -26.56465 1.000 24.69149  ? 55  ALA   A C   1 
ATOM   321  O  O   . ALA   A 1 48  ? -5.37950  -5.91317  -27.75520 1.000 23.38848  ? 55  ALA   A O   1 
ATOM   322  C  CB  . ALA   A 1 48  ? -3.62073  -8.07649  -26.07027 1.000 20.74541  ? 55  ALA   A CB  1 
ATOM   323  N  N   . LEU   A 1 49  ? -6.18744  -6.21327  -25.67454 1.000 22.41305  ? 56  LEU   A N   1 
ATOM   324  C  CA  . LEU   A 1 49  ? -7.53783  -5.80612  -26.04426 1.000 20.74141  ? 56  LEU   A CA  1 
ATOM   325  C  C   . LEU   A 1 49  ? -7.60016  -4.30334  -26.31619 1.000 23.89797  ? 56  LEU   A C   1 
ATOM   326  O  O   . LEU   A 1 49  ? -8.26668  -3.86522  -27.26571 1.000 23.76352  ? 56  LEU   A O   1 
ATOM   327  C  CB  . LEU   A 1 49  ? -8.50473  -6.20830  -24.92793 1.000 23.24973  ? 56  LEU   A CB  1 
ATOM   328  C  CG  . LEU   A 1 49  ? -8.74476  -7.72108  -24.86046 1.000 20.54694  ? 56  LEU   A CG  1 
ATOM   329  C  CD1 . LEU   A 1 49  ? -9.20050  -8.08075  -23.45725 1.000 23.40039  ? 56  LEU   A CD1 1 
ATOM   330  C  CD2 . LEU   A 1 49  ? -9.77479  -8.16901  -25.91026 1.000 20.86947  ? 56  LEU   A CD2 1 
ATOM   331  N  N   . ASP   A 1 50  ? -6.88714  -3.50058  -25.51291 1.000 24.14428  ? 57  ASP   A N   1 
ATOM   332  C  CA  . ASP   A 1 50  ? -6.81447  -2.06280  -25.78728 1.000 24.11933  ? 57  ASP   A CA  1 
ATOM   333  C  C   . ASP   A 1 50  ? -6.26454  -1.81141  -27.18710 1.000 24.59592  ? 57  ASP   A C   1 
ATOM   334  O  O   . ASP   A 1 50  ? -6.72428  -0.90267  -27.89610 1.000 25.84273  ? 57  ASP   A O   1 
ATOM   335  C  CB  . ASP   A 1 50  ? -5.91193  -1.33656  -24.78077 1.000 23.33751  ? 57  ASP   A CB  1 
ATOM   336  C  CG  . ASP   A 1 50  ? -6.51133  -1.20263  -23.39170 1.000 30.68679  ? 57  ASP   A CG  1 
ATOM   337  O  OD1 . ASP   A 1 50  ? -7.73759  -1.36942  -23.20440 1.000 31.38455  ? 57  ASP   A OD1 1 
ATOM   338  O  OD2 . ASP   A 1 50  ? -5.72270  -0.87864  -22.47708 1.000 31.25792  ? 57  ASP   A OD2 1 
ATOM   339  N  N   . LYS   A 1 51  ? -5.23816  -2.57887  -27.57391 1.000 22.98645  ? 58  LYS   A N   1 
ATOM   340  C  CA  . LYS   A 1 51  ? -4.58251  -2.36936  -28.86064 1.000 23.91021  ? 58  LYS   A CA  1 
ATOM   341  C  C   . LYS   A 1 51  ? -5.51762  -2.65949  -30.02539 1.000 25.33738  ? 58  LYS   A C   1 
ATOM   342  O  O   . LYS   A 1 51  ? -5.59718  -1.86354  -30.96541 1.000 24.52319  ? 58  LYS   A O   1 
ATOM   343  C  CB  . LYS   A 1 51  ? -3.31474  -3.21830  -28.97137 1.000 27.78841  ? 58  LYS   A CB  1 
ATOM   344  C  CG  . LYS   A 1 51  ? -2.16209  -2.71921  -28.10069 1.000 34.61342  ? 58  LYS   A CG  1 
ATOM   345  C  CD  . LYS   A 1 51  ? -1.03473  -3.75305  -28.00387 1.000 39.81999  ? 58  LYS   A CD  1 
ATOM   346  C  CE  . LYS   A 1 51  ? -0.08424  -3.45712  -26.84717 1.000 47.97725  ? 58  LYS   A CE  1 
ATOM   347  N  NZ  . LYS   A 1 51  ? 1.11108   -4.35669  -26.87363 1.000 49.72375  ? 58  LYS   A NZ  1 
ATOM   348  N  N   . ILE   A 1 52  ? -6.23215  -3.79120  -29.99919 1.000 25.47075  ? 59  ILE   A N   1 
ATOM   349  C  CA  . ILE   A 1 52  ? -7.12434  -4.05613  -31.13378 1.000 26.47799  ? 59  ILE   A CA  1 
ATOM   350  C  C   . ILE   A 1 52  ? -8.31839  -3.09853  -31.10929 1.000 27.30096  ? 59  ILE   A C   1 
ATOM   351  O  O   . ILE   A 1 52  ? -8.79586  -2.65743  -32.16423 1.000 26.47073  ? 59  ILE   A O   1 
ATOM   352  C  CB  . ILE   A 1 52  ? -7.56616  -5.53662  -31.18388 1.000 23.83427  ? 59  ILE   A CB  1 
ATOM   353  C  CG1 . ILE   A 1 52  ? -8.33673  -5.81792  -32.48453 1.000 26.67616  ? 59  ILE   A CG1 1 
ATOM   354  C  CG2 . ILE   A 1 52  ? -8.40151  -5.92862  -29.96281 1.000 23.70971  ? 59  ILE   A CG2 1 
ATOM   355  C  CD1 . ILE   A 1 52  ? -7.46784  -5.69795  -33.72553 1.000 30.46747  ? 59  ILE   A CD1 1 
ATOM   356  N  N   . ARG   A 1 53  ? -8.79625  -2.72222  -29.92368 1.000 24.27936  ? 60  ARG   A N   1 
ATOM   357  C  CA  . ARG   A 1 53  ? -9.87867  -1.74746  -29.86072 1.000 24.56823  ? 60  ARG   A CA  1 
ATOM   358  C  C   . ARG   A 1 53  ? -9.47140  -0.41974  -30.49680 1.000 25.90692  ? 60  ARG   A C   1 
ATOM   359  O  O   . ARG   A 1 53  ? -10.20562 0.14418   -31.32260 1.000 27.72435  ? 60  ARG   A O   1 
ATOM   360  C  CB  . ARG   A 1 53  ? -10.30386 -1.53697  -28.41118 1.000 24.58701  ? 60  ARG   A CB  1 
ATOM   361  C  CG  . ARG   A 1 53  ? -11.55421 -0.70991  -28.33826 1.000 28.09582  ? 60  ARG   A CG  1 
ATOM   362  C  CD  . ARG   A 1 53  ? -11.93092 -0.39468  -26.91052 1.000 34.12509  ? 60  ARG   A CD  1 
ATOM   363  N  NE  . ARG   A 1 53  ? -13.13207 0.43175   -26.88757 1.000 67.29708  ? 60  ARG   A NE  1 
ATOM   364  C  CZ  . ARG   A 1 53  ? -13.37972 1.37241   -25.98564 1.000 65.25245  ? 60  ARG   A CZ  1 
ATOM   365  N  NH1 . ARG   A 1 53  ? -12.55600 1.59053   -24.97212 1.000 48.95890  ? 60  ARG   A NH1 1 
ATOM   366  N  NH2 . ARG   A 1 53  ? -14.48049 2.11262   -26.10469 1.000 57.29559  ? 60  ARG   A NH2 1 
ATOM   367  N  N   . TYR   A 1 54  ? -8.29122  0.09292   -30.13350 1.000 26.28741  ? 61  TYR   A N   1 
ATOM   368  C  CA  . TYR   A 1 54  ? -7.83967  1.35606   -30.71614 1.000 28.95134  ? 61  TYR   A CA  1 
ATOM   369  C  C   . TYR   A 1 54  ? -7.66492  1.24365   -32.22057 1.000 28.18950  ? 61  TYR   A C   1 
ATOM   370  O  O   . TYR   A 1 54  ? -8.08247  2.13472   -32.96693 1.000 29.61970  ? 61  TYR   A O   1 
ATOM   371  C  CB  . TYR   A 1 54  ? -6.52446  1.81978   -30.09116 1.000 27.97161  ? 61  TYR   A CB  1 
ATOM   372  C  CG  . TYR   A 1 54  ? -6.36149  3.31889   -30.19746 1.000 32.93756  ? 61  TYR   A CG  1 
ATOM   373  C  CD1 . TYR   A 1 54  ? -7.14655  4.17180   -29.43372 1.000 46.81549  ? 61  TYR   A CD1 1 
ATOM   374  C  CD2 . TYR   A 1 54  ? -5.51336  3.87998   -31.13807 1.000 43.64965  ? 61  TYR   A CD2 1 
ATOM   375  C  CE1 . TYR   A 1 54  ? -7.02605  5.54173   -29.53798 1.000 48.27607  ? 61  TYR   A CE1 1 
ATOM   376  C  CE2 . TYR   A 1 54  ? -5.39564  5.26267   -31.26414 1.000 33.43799  ? 61  TYR   A CE2 1 
ATOM   377  C  CZ  . TYR   A 1 54  ? -6.15326  6.08479   -30.45577 1.000 46.22565  ? 61  TYR   A CZ  1 
ATOM   378  O  OH  . TYR   A 1 54  ? -6.05629  7.45825   -30.55286 1.000 47.09846  ? 61  TYR   A OH  1 
ATOM   379  N  N   . GLU   A 1 55  ? -7.05802  0.15201   -32.68779 1.000 27.68920  ? 62  GLU   A N   1 
ATOM   380  C  CA  . GLU   A 1 55  ? -6.83204  0.00917   -34.12010 1.000 30.60553  ? 62  GLU   A CA  1 
ATOM   381  C  C   . GLU   A 1 55  ? -8.15560  -0.03718  -34.87162 1.000 30.45334  ? 62  GLU   A C   1 
ATOM   382  O  O   . GLU   A 1 55  ? -8.27238  0.51620   -35.97197 1.000 32.15398  ? 62  GLU   A O   1 
ATOM   383  C  CB  . GLU   A 1 55  ? -6.00229  -1.24892  -34.39064 1.000 31.11891  ? 62  GLU   A CB  1 
ATOM   384  C  CG  . GLU   A 1 55  ? -4.49264  -0.99002  -34.34079 1.000 40.08437  ? 62  GLU   A CG  1 
ATOM   385  C  CD  . GLU   A 1 55  ? -3.64003  -2.19601  -34.72526 1.000 55.82142  ? 62  GLU   A CD  1 
ATOM   386  O  OE1 . GLU   A 1 55  ? -4.13792  -3.10131  -35.43245 1.000 56.46872  ? 62  GLU   A OE1 1 
ATOM   387  O  OE2 . GLU   A 1 55  ? -2.45724  -2.23404  -34.31466 1.000 60.84586  ? 62  GLU   A OE2 1 
ATOM   388  N  N   . SER   A 1 56  ? -9.17710  -0.66521  -34.27286 1.000 27.61028  ? 63  SER   A N   1 
ATOM   389  C  CA  . SER   A 1 56  ? -10.47941 -0.78564  -34.92078 1.000 31.78297  ? 63  SER   A CA  1 
ATOM   390  C  C   . SER   A 1 56  ? -11.18312 0.55506   -35.08389 1.000 34.46163  ? 63  SER   A C   1 
ATOM   391  O  O   . SER   A 1 56  ? -12.10432 0.65631   -35.89953 1.000 34.90496  ? 63  SER   A O   1 
ATOM   392  C  CB  . SER   A 1 56  ? -11.37991 -1.74032  -34.12949 1.000 31.25041  ? 63  SER   A CB  1 
ATOM   393  O  OG  . SER   A 1 56  ? -11.93279 -1.09577  -32.98958 1.000 33.06262  ? 63  SER   A OG  1 
ATOM   394  N  N   . LEU   A 1 57  ? -10.77792 1.58547   -34.33311 1.000 32.68690  ? 64  LEU   A N   1 
ATOM   395  C  CA  . LEU   A 1 57  ? -11.43640 2.88531   -34.44788 1.000 31.92275  ? 64  LEU   A CA  1 
ATOM   396  C  C   . LEU   A 1 57  ? -11.21296 3.49061   -35.82519 1.000 42.80995  ? 64  LEU   A C   1 
ATOM   397  O  O   . LEU   A 1 57  ? -12.10097 4.14919   -36.37935 1.000 47.20391  ? 64  LEU   A O   1 
ATOM   398  C  CB  . LEU   A 1 57  ? -10.90870 3.82557   -33.36492 1.000 32.90549  ? 64  LEU   A CB  1 
ATOM   399  C  CG  . LEU   A 1 57  ? -11.36763 3.45811   -31.94987 1.000 36.91740  ? 64  LEU   A CG  1 
ATOM   400  C  CD1 . LEU   A 1 57  ? -10.78925 4.43644   -30.93140 1.000 40.12762  ? 64  LEU   A CD1 1 
ATOM   401  C  CD2 . LEU   A 1 57  ? -12.88054 3.39225   -31.85384 1.000 43.21250  ? 64  LEU   A CD2 1 
ATOM   402  N  N   . THR   A 1 58  ? -10.03044 3.27450   -36.39561 1.000 38.81859  ? 65  THR   A N   1 
ATOM   403  C  CA  . THR   A 1 58  ? -9.70556  3.78325   -37.71718 1.000 43.98511  ? 65  THR   A CA  1 
ATOM   404  C  C   . THR   A 1 58  ? -9.83450  2.73429   -38.81313 1.000 44.35320  ? 65  THR   A C   1 
ATOM   405  O  O   . THR   A 1 58  ? -9.88948  3.10109   -39.99038 1.000 42.57412  ? 65  THR   A O   1 
ATOM   406  C  CB  . THR   A 1 58  ? -8.29101  4.38294   -37.71566 1.000 52.04127  ? 65  THR   A CB  1 
ATOM   407  O  OG1 . THR   A 1 58  ? -7.31787  3.33735   -37.78105 1.000 58.17197  ? 65  THR   A OG1 1 
ATOM   408  C  CG2 . THR   A 1 58  ? -8.05597  5.22112   -36.47313 1.000 41.45352  ? 65  THR   A CG2 1 
ATOM   409  N  N   . ASP   A 1 59  ? -9.90915  1.45085   -38.46345 1.000 40.09690  ? 66  ASP   A N   1 
ATOM   410  C  CA  . ASP   A 1 59  ? -10.08222 0.38432   -39.44858 1.000 38.99649  ? 66  ASP   A CA  1 
ATOM   411  C  C   . ASP   A 1 59  ? -11.05257 -0.63137  -38.85363 1.000 38.44639  ? 66  ASP   A C   1 
ATOM   412  O  O   . ASP   A 1 59  ? -10.63561 -1.61608  -38.22912 1.000 38.77913  ? 66  ASP   A O   1 
ATOM   413  C  CB  . ASP   A 1 59  ? -8.73978  -0.26684  -39.79711 1.000 37.26229  ? 66  ASP   A CB  1 
ATOM   414  C  CG  . ASP   A 1 59  ? -8.84850  -1.27581  -40.93493 1.000 54.20285  ? 66  ASP   A CG  1 
ATOM   415  O  OD1 . ASP   A 1 59  ? -9.98210  -1.60044  -41.34791 1.000 44.66235  ? 66  ASP   A OD1 1 
ATOM   416  O  OD2 . ASP   A 1 59  ? -7.79362  -1.75488  -41.40991 1.000 51.28948  ? 66  ASP   A OD2 1 
ATOM   417  N  N   . PRO   A 1 60  ? -12.36279 -0.41427  -39.01405 1.000 41.37677  ? 67  PRO   A N   1 
ATOM   418  C  CA  . PRO   A 1 60  ? -13.33361 -1.32321  -38.37816 1.000 35.97237  ? 67  PRO   A CA  1 
ATOM   419  C  C   . PRO   A 1 60  ? -13.21365 -2.76983  -38.82980 1.000 38.32597  ? 67  PRO   A C   1 
ATOM   420  O  O   . PRO   A 1 60  ? -13.60106 -3.68011  -38.08160 1.000 38.98536  ? 67  PRO   A O   1 
ATOM   421  C  CB  . PRO   A 1 60  ? -14.68029 -0.71824  -38.79028 1.000 44.35724  ? 67  PRO   A CB  1 
ATOM   422  C  CG  . PRO   A 1 60  ? -14.39596 0.72497   -38.88680 1.000 47.13643  ? 67  PRO   A CG  1 
ATOM   423  C  CD  . PRO   A 1 60  ? -13.02592 0.79218   -39.53353 1.000 44.42481  ? 67  PRO   A CD  1 
ATOM   424  N  N   . SER   A 1 61  ? -12.67484 -3.01271  -40.02520 1.000 36.43245  ? 68  SER   A N   1 
ATOM   425  C  CA  . SER   A 1 61  ? -12.52602 -4.37875  -40.51409 1.000 34.92738  ? 68  SER   A CA  1 
ATOM   426  C  C   . SER   A 1 61  ? -11.53798 -5.19420  -39.68918 1.000 34.82833  ? 68  SER   A C   1 
ATOM   427  O  O   . SER   A 1 61  ? -11.52564 -6.42432  -39.80687 1.000 35.65669  ? 68  SER   A O   1 
ATOM   428  C  CB  . SER   A 1 61  ? -12.12126 -4.35218  -41.99231 1.000 40.85427  ? 68  SER   A CB  1 
ATOM   429  O  OG  . SER   A 1 61  ? -10.72443 -4.16122  -42.16172 1.000 43.37135  ? 68  SER   A OG  1 
ATOM   430  N  N   . LYS   A 1 62  ? -10.73016 -4.55613  -38.83675 1.000 33.78101  ? 69  LYS   A N   1 
ATOM   431  C  CA  . LYS   A 1 62  ? -9.85502  -5.32438  -37.96361 1.000 29.75200  ? 69  LYS   A CA  1 
ATOM   432  C  C   . LYS   A 1 62  ? -10.63543 -6.18477  -36.98453 1.000 31.61977  ? 69  LYS   A C   1 
ATOM   433  O  O   . LYS   A 1 62  ? -10.06219 -7.11434  -36.40765 1.000 30.58650  ? 69  LYS   A O   1 
ATOM   434  C  CB  . LYS   A 1 62  ? -8.90496  -4.39278  -37.20634 1.000 35.62760  ? 69  LYS   A CB  1 
ATOM   435  C  CG  . LYS   A 1 62  ? -8.03040  -3.58528  -38.14607 1.000 40.29943  ? 69  LYS   A CG  1 
ATOM   436  C  CD  . LYS   A 1 62  ? -6.64727  -3.36779  -37.59711 1.000 40.20027  ? 69  LYS   A CD  1 
ATOM   437  C  CE  . LYS   A 1 62  ? -5.75511  -2.72704  -38.64207 1.000 46.01794  ? 69  LYS   A CE  1 
ATOM   438  N  NZ  . LYS   A 1 62  ? -4.35386  -2.70471  -38.16318 1.000 56.33593  ? 69  LYS   A NZ  1 
ATOM   439  N  N   . LEU   A 1 63  ? -11.92651 -5.91028  -36.79236 1.000 30.40272  ? 70  LEU   A N   1 
ATOM   440  C  CA  . LEU   A 1 63  ? -12.77003 -6.74012  -35.94164 1.000 32.05172  ? 70  LEU   A CA  1 
ATOM   441  C  C   . LEU   A 1 63  ? -13.54832 -7.78932  -36.73192 1.000 32.46567  ? 70  LEU   A C   1 
ATOM   442  O  O   . LEU   A 1 63  ? -14.40412 -8.46818  -36.15968 1.000 34.71648  ? 70  LEU   A O   1 
ATOM   443  C  CB  . LEU   A 1 63  ? -13.73668 -5.86782  -35.14144 1.000 30.97812  ? 70  LEU   A CB  1 
ATOM   444  C  CG  . LEU   A 1 63  ? -13.11281 -4.98610  -34.05138 1.000 33.50245  ? 70  LEU   A CG  1 
ATOM   445  C  CD1 . LEU   A 1 63  ? -14.19995 -4.28503  -33.22558 1.000 40.72671  ? 70  LEU   A CD1 1 
ATOM   446  C  CD2 . LEU   A 1 63  ? -12.17867 -5.76712  -33.13348 1.000 31.59685  ? 70  LEU   A CD2 1 
ATOM   447  N  N   . ASP   A 1 64  ? -13.27671 -7.94020  -38.03161 1.000 34.47955  ? 71  ASP   A N   1 
ATOM   448  C  CA  . ASP   A 1 64  ? -13.91877 -9.01669  -38.77914 1.000 36.05045  ? 71  ASP   A CA  1 
ATOM   449  C  C   . ASP   A 1 64  ? -13.56269 -10.38716 -38.21953 1.000 37.31004  ? 71  ASP   A C   1 
ATOM   450  O  O   . ASP   A 1 64  ? -14.31154 -11.34623 -38.42422 1.000 36.60140  ? 71  ASP   A O   1 
ATOM   451  C  CB  . ASP   A 1 64  ? -13.53901 -8.96007  -40.25715 1.000 37.70340  ? 71  ASP   A CB  1 
ATOM   452  C  CG  . ASP   A 1 64  ? -14.04798 -7.70517  -40.94571 1.000 48.05930  ? 71  ASP   A CG  1 
ATOM   453  O  OD1 . ASP   A 1 64  ? -14.90653 -7.00803  -40.36236 1.000 45.16187  ? 71  ASP   A OD1 1 
ATOM   454  O  OD2 . ASP   A 1 64  ? -13.61751 -7.44082  -42.08834 1.000 52.51776  ? 71  ASP   A OD2 1 
ATOM   455  N  N   . SER   A 1 65  ? -12.43169 -10.50322 -37.54708 1.000 33.89459  ? 72  SER   A N   1 
ATOM   456  C  CA  . SER   A 1 65  ? -12.02125 -11.74546 -36.90791 1.000 30.99621  ? 72  SER   A CA  1 
ATOM   457  C  C   . SER   A 1 65  ? -12.65354 -11.93368 -35.53118 1.000 38.36041  ? 72  SER   A C   1 
ATOM   458  O  O   . SER   A 1 65  ? -12.26676 -12.86258 -34.81005 1.000 38.92799  ? 72  SER   A O   1 
ATOM   459  C  CB  . SER   A 1 65  ? -10.49795 -11.78042 -36.77921 1.000 33.56776  ? 72  SER   A CB  1 
ATOM   460  O  OG  . SER   A 1 65  ? -10.01719 -10.53126 -36.30961 1.000 31.77190  ? 72  SER   A OG  1 
ATOM   461  N  N   . GLY   A 1 66  ? -13.58678 -11.06058 -35.14733 1.000 33.36568  ? 73  GLY   A N   1 
ATOM   462  C  CA  . GLY   A 1 66  ? -14.29390 -11.18403 -33.88131 1.000 31.91701  ? 73  GLY   A CA  1 
ATOM   463  C  C   . GLY   A 1 66  ? -14.54785 -9.84368  -33.22025 1.000 31.65737  ? 73  GLY   A C   1 
ATOM   464  O  O   . GLY   A 1 66  ? -13.60198 -9.10765  -32.93271 1.000 30.07255  ? 73  GLY   A O   1 
ATOM   465  N  N   . LYS   A 1 67  ? -15.81585 -9.50901  -32.96347 1.000 32.16591  ? 74  LYS   A N   1 
ATOM   466  C  CA  . LYS   A 1 67  ? -16.13341 -8.22181  -32.35704 1.000 31.27990  ? 74  LYS   A CA  1 
ATOM   467  C  C   . LYS   A 1 67  ? -16.06181 -8.23801  -30.83573 1.000 34.59612  ? 74  LYS   A C   1 
ATOM   468  O  O   . LYS   A 1 67  ? -15.87696 -7.17520  -30.23141 1.000 32.85447  ? 74  LYS   A O   1 
ATOM   469  C  CB  . LYS   A 1 67  ? -17.53135 -7.76242  -32.79293 1.000 35.80134  ? 74  LYS   A CB  1 
ATOM   470  C  CG  . LYS   A 1 67  ? -18.64372 -8.71197  -32.36661 1.000 55.49046  ? 74  LYS   A CG  1 
ATOM   471  C  CD  . LYS   A 1 67  ? -20.00577 -8.02623  -32.33151 1.000 65.32217  ? 74  LYS   A CD  1 
ATOM   472  C  CE  . LYS   A 1 67  ? -20.89101 -8.52179  -33.46800 1.000 68.53435  ? 74  LYS   A CE  1 
ATOM   473  N  NZ  . LYS   A 1 67  ? -22.33980 -8.41704  -33.13708 1.000 69.93290  ? 74  LYS   A NZ  1 
ATOM   474  N  N   . GLU   A 1 68  ? -16.18943 -9.40381  -30.20228 1.000 29.60911  ? 75  GLU   A N   1 
ATOM   475  C  CA  . GLU   A 1 68  ? -16.20846 -9.45343  -28.74666 1.000 29.62565  ? 75  GLU   A CA  1 
ATOM   476  C  C   . GLU   A 1 68  ? -14.81033 -9.23376  -28.17499 1.000 29.33675  ? 75  GLU   A C   1 
ATOM   477  O  O   . GLU   A 1 68  ? -13.82608 -9.80899  -28.65106 1.000 30.81749  ? 75  GLU   A O   1 
ATOM   478  C  CB  . GLU   A 1 68  ? -16.77576 -10.79120 -28.27206 1.000 39.73770  ? 75  GLU   A CB  1 
ATOM   479  C  CG  . GLU   A 1 68  ? -18.27599 -10.89011 -28.46209 1.000 41.34797  ? 75  GLU   A CG  1 
ATOM   480  C  CD  . GLU   A 1 68  ? -18.63767 -11.49942 -29.80290 1.000 71.97885  ? 75  GLU   A CD  1 
ATOM   481  O  OE1 . GLU   A 1 68  ? -17.71899 -11.71452 -30.62704 1.000 68.23061  ? 75  GLU   A OE1 1 
ATOM   482  O  OE2 . GLU   A 1 68  ? -19.84175 -11.73742 -30.04320 1.000 77.76590  ? 75  GLU   A OE2 1 
ATOM   483  N  N   . LEU   A 1 69  ? -14.72781 -8.38464  -27.14621 1.000 25.73111  ? 76  LEU   A N   1 
ATOM   484  C  CA  . LEU   A 1 69  ? -13.46810 -8.05482  -26.47903 1.000 24.87715  ? 76  LEU   A CA  1 
ATOM   485  C  C   . LEU   A 1 69  ? -13.58343 -8.50239  -25.02616 1.000 26.16523  ? 76  LEU   A C   1 
ATOM   486  O  O   . LEU   A 1 69  ? -14.24953 -7.84434  -24.21590 1.000 26.44144  ? 76  LEU   A O   1 
ATOM   487  C  CB  . LEU   A 1 69  ? -13.17305 -6.56309  -26.57167 1.000 26.66586  ? 76  LEU   A CB  1 
ATOM   488  C  CG  . LEU   A 1 69  ? -13.11647 -5.99699  -27.99312 1.000 27.00068  ? 76  LEU   A CG  1 
ATOM   489  C  CD1 . LEU   A 1 69  ? -12.81748 -4.49897  -27.94435 1.000 33.55766  ? 76  LEU   A CD1 1 
ATOM   490  C  CD2 . LEU   A 1 69  ? -12.06110 -6.72101  -28.80587 1.000 30.52170  ? 76  LEU   A CD2 1 
ATOM   491  N  N   . HIS   A 1 70  ? -12.95361 -9.62477  -24.68835 1.000 22.46063  ? 77  HIS   A N   1 
ATOM   492  C  CA  . HIS   A 1 70  ? -13.20328 -10.20156 -23.37612 1.000 23.72932  ? 77  HIS   A CA  1 
ATOM   493  C  C   . HIS   A 1 70  ? -12.01474 -11.04451 -22.94205 1.000 21.77853  ? 77  HIS   A C   1 
ATOM   494  O  O   . HIS   A 1 70  ? -11.08094 -11.30412 -23.71562 1.000 21.74730  ? 77  HIS   A O   1 
ATOM   495  C  CB  . HIS   A 1 70  ? -14.50453 -11.01961 -23.39499 1.000 25.14494  ? 77  HIS   A CB  1 
ATOM   496  C  CG  . HIS   A 1 70  ? -14.46207 -12.19520 -24.32231 1.000 28.26628  ? 77  HIS   A CG  1 
ATOM   497  N  ND1 . HIS   A 1 70  ? -15.33194 -12.33115 -25.38759 1.000 31.22133  ? 77  HIS   A ND1 1 
ATOM   498  C  CD2 . HIS   A 1 70  ? -13.68769 -13.30588 -24.32568 1.000 27.59498  ? 77  HIS   A CD2 1 
ATOM   499  C  CE1 . HIS   A 1 70  ? -15.06655 -13.45630 -26.02695 1.000 30.88436  ? 77  HIS   A CE1 1 
ATOM   500  N  NE2 . HIS   A 1 70  ? -14.07642 -14.06756 -25.40160 1.000 31.14610  ? 77  HIS   A NE2 1 
ATOM   501  N  N   . ILE   A 1 71  ? -12.04673 -11.43208 -21.66627 1.000 20.21621  ? 78  ILE   A N   1 
ATOM   502  C  CA  . ILE   A 1 71  ? -11.04443 -12.29790 -21.05361 1.000 19.57679  ? 78  ILE   A CA  1 
ATOM   503  C  C   . ILE   A 1 71  ? -11.76716 -13.46004 -20.37479 1.000 23.45989  ? 78  ILE   A C   1 
ATOM   504  O  O   . ILE   A 1 71  ? -12.68651 -13.23571 -19.57703 1.000 23.00610  ? 78  ILE   A O   1 
ATOM   505  C  CB  . ILE   A 1 71  ? -10.18612 -11.53191 -20.03027 1.000 19.64290  ? 78  ILE   A CB  1 
ATOM   506  C  CG1 . ILE   A 1 71  ? -9.52693  -10.31660 -20.69422 1.000 21.34584  ? 78  ILE   A CG1 1 
ATOM   507  C  CG2 . ILE   A 1 71  ? -9.17927  -12.48910 -19.36681 1.000 21.28993  ? 78  ILE   A CG2 1 
ATOM   508  C  CD1 . ILE   A 1 71  ? -8.88408  -9.35498  -19.68746 1.000 21.44361  ? 78  ILE   A CD1 1 
ATOM   509  N  N   . ASN   A 1 72  ? -11.34309 -14.69807 -20.67204 1.000 21.21433  ? 79  ASN   A N   1 
ATOM   510  C  CA  . ASN   A 1 72  ? -11.87978 -15.89557 -20.03368 1.000 20.27266  ? 79  ASN   A CA  1 
ATOM   511  C  C   . ASN   A 1 72  ? -10.78955 -16.59620 -19.23893 1.000 24.33325  ? 79  ASN   A C   1 
ATOM   512  O  O   . ASN   A 1 72  ? -9.64657  -16.71890 -19.70453 1.000 24.37870  ? 79  ASN   A O   1 
ATOM   513  C  CB  . ASN   A 1 72  ? -12.45325 -16.86522 -21.06387 1.000 19.32699  ? 79  ASN   A CB  1 
ATOM   514  C  CG  . ASN   A 1 72  ? -13.64637 -16.28802 -21.79481 1.000 20.51267  ? 79  ASN   A CG  1 
ATOM   515  O  OD1 . ASN   A 1 72  ? -14.37121 -15.42928 -21.26326 1.000 25.79752  ? 79  ASN   A OD1 1 
ATOM   516  N  ND2 . ASN   A 1 72  ? -13.88335 -16.77765 -23.01091 1.000 22.43679  ? 79  ASN   A ND2 1 
ATOM   517  N  N   . LEU   A 1 73  ? -11.15056 -17.06432 -18.04494 1.000 21.65141  ? 80  LEU   A N   1 
ATOM   518  C  CA  . LEU   A 1 73  ? -10.25251 -17.82333 -17.18107 1.000 20.23577  ? 80  LEU   A CA  1 
ATOM   519  C  C   . LEU   A 1 73  ? -10.80108 -19.23526 -17.07110 1.000 23.62640  ? 80  LEU   A C   1 
ATOM   520  O  O   . LEU   A 1 73  ? -11.91652 -19.43167 -16.57876 1.000 22.67821  ? 80  LEU   A O   1 
ATOM   521  C  CB  . LEU   A 1 73  ? -10.15662 -17.19285 -15.79402 1.000 20.83538  ? 80  LEU   A CB  1 
ATOM   522  C  CG  . LEU   A 1 73  ? -9.79138  -15.71644 -15.79164 1.000 21.15818  ? 80  LEU   A CG  1 
ATOM   523  C  CD1 . LEU   A 1 73  ? -9.81559  -15.20419 -14.35960 1.000 24.38485  ? 80  LEU   A CD1 1 
ATOM   524  C  CD2 . LEU   A 1 73  ? -8.40482  -15.52645 -16.40226 1.000 25.59912  ? 80  LEU   A CD2 1 
ATOM   525  N  N   . ILE   A 1 74  ? -10.02008 -20.21619 -17.49989 1.000 19.81513  ? 81  ILE   A N   1 
ATOM   526  C  CA  . ILE   A 1 74  ? -10.56372 -21.55862 -17.65386 1.000 20.96725  ? 81  ILE   A CA  1 
ATOM   527  C  C   . ILE   A 1 74  ? -9.69435  -22.56625 -16.91948 1.000 25.16587  ? 81  ILE   A C   1 
ATOM   528  O  O   . ILE   A 1 74  ? -8.63563  -22.96948 -17.42939 1.000 25.95619  ? 81  ILE   A O   1 
ATOM   529  C  CB  . ILE   A 1 74  ? -10.69424 -21.93775 -19.13644 1.000 20.71977  ? 81  ILE   A CB  1 
ATOM   530  C  CG1 . ILE   A 1 74  ? -11.45656 -20.85048 -19.89672 1.000 23.80382  ? 81  ILE   A CG1 1 
ATOM   531  C  CG2 . ILE   A 1 74  ? -11.39774 -23.29275 -19.26280 1.000 24.85908  ? 81  ILE   A CG2 1 
ATOM   532  C  CD1 . ILE   A 1 74  ? -11.55491 -21.10919 -21.39900 1.000 29.39471  ? 81  ILE   A CD1 1 
ATOM   533  N  N   . PRO   A 1 75  ? -10.10379 -23.00175 -15.73330 1.000 24.13341  ? 82  PRO   A N   1 
ATOM   534  C  CA  . PRO   A 1 75  ? -9.36309  -24.04933 -15.02869 1.000 23.28274  ? 82  PRO   A CA  1 
ATOM   535  C  C   . PRO   A 1 75  ? -9.77959  -25.41912 -15.52157 1.000 30.58726  ? 82  PRO   A C   1 
ATOM   536  O  O   . PRO   A 1 75  ? -10.93848 -25.65446 -15.87079 1.000 32.01446  ? 82  PRO   A O   1 
ATOM   537  C  CB  . PRO   A 1 75  ? -9.77474  -23.85104 -13.56650 1.000 26.52346  ? 82  PRO   A CB  1 
ATOM   538  C  CG  . PRO   A 1 75  ? -11.17236 -23.28110 -13.65039 1.000 31.81976  ? 82  PRO   A CG  1 
ATOM   539  C  CD  . PRO   A 1 75  ? -11.29227 -22.55040 -14.98385 1.000 30.36461  ? 82  PRO   A CD  1 
ATOM   540  N  N   . ASN   A 1 76  ? -8.81509  -26.33580 -15.54097 1.000 27.45776  ? 83  ASN   A N   1 
ATOM   541  C  CA  . ASN   A 1 76  ? -9.09994  -27.72619 -15.89440 1.000 28.38919  ? 83  ASN   A CA  1 
ATOM   542  C  C   . ASN   A 1 76  ? -8.30046  -28.62656 -14.96657 1.000 32.09310  ? 83  ASN   A C   1 
ATOM   543  O  O   . ASN   A 1 76  ? -7.08931  -28.77674 -15.14361 1.000 31.53611  ? 83  ASN   A O   1 
ATOM   544  C  CB  . ASN   A 1 76  ? -8.76721  -28.01486 -17.35777 1.000 32.08136  ? 83  ASN   A CB  1 
ATOM   545  C  CG  . ASN   A 1 76  ? -9.25928  -29.38181 -17.80038 1.000 38.23054  ? 83  ASN   A CG  1 
ATOM   546  O  OD1 . ASN   A 1 76  ? -8.99444  -30.39111 -17.15633 1.000 40.22880  ? 83  ASN   A OD1 1 
ATOM   547  N  ND2 . ASN   A 1 76  ? -10.01329 -29.40929 -18.89096 1.000 44.58675  ? 83  ASN   A ND2 1 
ATOM   548  N  N   . LYS   A 1 77  ? -8.98757  -29.26031 -14.00916 1.000 35.07515  ? 84  LYS   A N   1 
ATOM   549  C  CA  . LYS   A 1 77  ? -8.28993  -30.05452 -13.00133 1.000 33.70683  ? 84  LYS   A CA  1 
ATOM   550  C  C   . LYS   A 1 77  ? -7.77453  -31.36924 -13.57397 1.000 35.92397  ? 84  LYS   A C   1 
ATOM   551  O  O   . LYS   A 1 77  ? -6.74262  -31.87536 -13.11988 1.000 41.53678  ? 84  LYS   A O   1 
ATOM   552  C  CB  . LYS   A 1 77  ? -9.20729  -30.32335 -11.80631 1.000 38.67511  ? 84  LYS   A CB  1 
ATOM   553  C  CG  . LYS   A 1 77  ? -9.20112  -29.19625 -10.76676 1.000 48.90911  ? 84  LYS   A CG  1 
ATOM   554  C  CD  . LYS   A 1 77  ? -10.35011 -29.32974 -9.77340  1.000 46.81200  ? 84  LYS   A CD  1 
ATOM   555  C  CE  . LYS   A 1 77  ? -10.36242 -28.17605 -8.77431  1.000 54.30533  ? 84  LYS   A CE  1 
ATOM   556  N  NZ  . LYS   A 1 77  ? -11.68197 -28.05564 -8.07734  1.000 61.07719  ? 84  LYS   A NZ  1 
ATOM   557  N  N   . GLN   A 1 78  ? -8.47545  -31.93312 -14.56228 1.000 40.66543  ? 85  GLN   A N   1 
ATOM   558  C  CA  . GLN   A 1 78  ? -8.02063  -33.16545 -15.20389 1.000 44.49179  ? 85  GLN   A CA  1 
ATOM   559  C  C   . GLN   A 1 78  ? -6.66168  -32.97575 -15.86611 1.000 43.42269  ? 85  GLN   A C   1 
ATOM   560  O  O   . GLN   A 1 78  ? -5.75290  -33.79730 -15.69375 1.000 44.14575  ? 85  GLN   A O   1 
ATOM   561  C  CB  . GLN   A 1 78  ? -9.05175  -33.63107 -16.23344 1.000 50.61442  ? 85  GLN   A CB  1 
ATOM   562  C  CG  . GLN   A 1 78  ? -8.91413  -35.08359 -16.65310 1.000 63.70583  ? 85  GLN   A CG  1 
ATOM   563  C  CD  . GLN   A 1 78  ? -9.90851  -35.98946 -15.96198 1.000 77.90238  ? 85  GLN   A CD  1 
ATOM   564  O  OE1 . GLN   A 1 78  ? -9.70249  -36.40332 -14.81885 1.000 78.04459  ? 85  GLN   A OE1 1 
ATOM   565  N  NE2 . GLN   A 1 78  ? -11.00319 -36.29508 -16.64879 1.000 83.17055  ? 85  GLN   A NE2 1 
ATOM   566  N  N   . ASP   A 1 79  ? -6.50801  -31.90104 -16.63791 1.000 38.26941  ? 86  ASP   A N   1 
ATOM   567  C  CA  . ASP   A 1 79  ? -5.24502  -31.60657 -17.30037 1.000 36.00361  ? 86  ASP   A CA  1 
ATOM   568  C  C   . ASP   A 1 79  ? -4.28632  -30.82023 -16.42003 1.000 32.90632  ? 86  ASP   A C   1 
ATOM   569  O  O   . ASP   A 1 79  ? -3.13612  -30.61725 -16.82461 1.000 33.63424  ? 86  ASP   A O   1 
ATOM   570  C  CB  . ASP   A 1 79  ? -5.48877  -30.80958 -18.58950 1.000 35.93290  ? 86  ASP   A CB  1 
ATOM   571  C  CG  . ASP   A 1 79  ? -6.44763  -31.50610 -19.53290 1.000 50.20409  ? 86  ASP   A CG  1 
ATOM   572  O  OD1 . ASP   A 1 79  ? -6.62484  -32.73935 -19.40858 1.000 54.93653  ? 86  ASP   A OD1 1 
ATOM   573  O  OD2 . ASP   A 1 79  ? -7.01744  -30.81360 -20.40192 1.000 51.89976  ? 86  ASP   A OD2 1 
ATOM   574  N  N   . ARG   A 1 80  ? -4.74402  -30.36322 -15.25324 1.000 31.58668  ? 87  ARG   A N   1 
ATOM   575  C  CA  . ARG   A 1 80  ? -3.98970  -29.46714 -14.37433 1.000 25.12377  ? 87  ARG   A CA  1 
ATOM   576  C  C   . ARG   A 1 80  ? -3.48753  -28.23685 -15.12686 1.000 28.57724  ? 87  ARG   A C   1 
ATOM   577  O  O   . ARG   A 1 80  ? -2.30814  -27.87546 -15.07726 1.000 28.20474  ? 87  ARG   A O   1 
ATOM   578  C  CB  . ARG   A 1 80  ? -2.84276  -30.20386 -13.69252 1.000 28.72539  ? 87  ARG   A CB  1 
ATOM   579  C  CG  . ARG   A 1 80  ? -2.50099  -29.56229 -12.35886 1.000 38.36030  ? 87  ARG   A CG  1 
ATOM   580  C  CD  . ARG   A 1 80  ? -1.06182  -29.77288 -11.99130 1.000 41.62156  ? 87  ARG   A CD  1 
ATOM   581  N  NE  . ARG   A 1 80  ? -0.82667  -31.16525 -11.66116 1.000 42.04195  ? 87  ARG   A NE  1 
ATOM   582  C  CZ  . ARG   A 1 80  ? 0.33666   -31.78447 -11.81056 1.000 57.09000  ? 87  ARG   A CZ  1 
ATOM   583  N  NH1 . ARG   A 1 80  ? 1.41325   -31.14273 -12.24292 1.000 45.06059  ? 87  ARG   A NH1 1 
ATOM   584  N  NH2 . ARG   A 1 80  ? 0.42603   -33.07630 -11.50601 1.000 50.30004  ? 87  ARG   A NH2 1 
ATOM   585  N  N   . THR   A 1 81  ? -4.40768  -27.56528 -15.81112 1.000 24.77346  ? 88  THR   A N   1 
ATOM   586  C  CA  . THR   A 1 81  ? -4.08746  -26.35609 -16.55127 1.000 22.94075  ? 88  THR   A CA  1 
ATOM   587  C  C   . THR   A 1 81  ? -5.00964  -25.22602 -16.13458 1.000 25.42795  ? 88  THR   A C   1 
ATOM   588  O  O   . THR   A 1 81  ? -6.18398  -25.44744 -15.81992 1.000 26.67178  ? 88  THR   A O   1 
ATOM   589  C  CB  . THR   A 1 81  ? -4.20212  -26.54383 -18.07552 1.000 26.79578  ? 88  THR   A CB  1 
ATOM   590  O  OG1 . THR   A 1 81  ? -5.52156  -27.00817 -18.40388 1.000 29.30088  ? 88  THR   A OG1 1 
ATOM   591  C  CG2 . THR   A 1 81  ? -3.15799  -27.53661 -18.59795 1.000 28.70534  ? 88  THR   A CG2 1 
ATOM   592  N  N   . LEU   A 1 82  ? -4.46109  -24.01737 -16.12004 1.000 22.23787  ? 89  LEU   A N   1 
ATOM   593  C  CA  . LEU   A 1 82  ? -5.24512  -22.78968 -16.04385 1.000 21.45336  ? 89  LEU   A CA  1 
ATOM   594  C  C   . LEU   A 1 82  ? -4.98737  -22.02746 -17.33386 1.000 25.91184  ? 89  LEU   A C   1 
ATOM   595  O  O   . LEU   A 1 82  ? -3.83138  -21.75396 -17.67668 1.000 23.27913  ? 89  LEU   A O   1 
ATOM   596  C  CB  . LEU   A 1 82  ? -4.85462  -21.95053 -14.82808 1.000 21.65607  ? 89  LEU   A CB  1 
ATOM   597  C  CG  . LEU   A 1 82  ? -5.57368  -20.61781 -14.70968 1.000 24.23515  ? 89  LEU   A CG  1 
ATOM   598  C  CD1 . LEU   A 1 82  ? -7.07972  -20.87280 -14.50437 1.000 24.57235  ? 89  LEU   A CD1 1 
ATOM   599  C  CD2 . LEU   A 1 82  ? -4.99477  -19.83090 -13.55319 1.000 24.59249  ? 89  LEU   A CD2 1 
ATOM   600  N  N   . THR   A 1 83  ? -6.04975  -21.70951 -18.06214 1.000 20.59294  ? 90  THR   A N   1 
ATOM   601  C  CA  . THR   A 1 83  ? -5.92911  -21.05022 -19.35217 1.000 20.13834  ? 90  THR   A CA  1 
ATOM   602  C  C   . THR   A 1 83  ? -6.50017  -19.64535 -19.24991 1.000 25.42232  ? 90  THR   A C   1 
ATOM   603  O  O   . THR   A 1 83  ? -7.60915  -19.45926 -18.73546 1.000 23.97715  ? 90  THR   A O   1 
ATOM   604  C  CB  . THR   A 1 83  ? -6.64588  -21.83758 -20.44788 1.000 21.98988  ? 90  THR   A CB  1 
ATOM   605  O  OG1 . THR   A 1 83  ? -6.09395  -23.15765 -20.54922 1.000 24.40040  ? 90  THR   A OG1 1 
ATOM   606  C  CG2 . THR   A 1 83  ? -6.51465  -21.13350 -21.76449 1.000 26.05910  ? 90  THR   A CG2 1 
ATOM   607  N  N   . ILE   A 1 84  ? -5.72801  -18.65918 -19.70025 1.000 20.27176  ? 91  ILE   A N   1 
ATOM   608  C  CA  . ILE   A 1 84  ? -6.17995  -17.26874 -19.77319 1.000 18.88359  ? 91  ILE   A CA  1 
ATOM   609  C  C   . ILE   A 1 84  ? -6.37009  -16.95493 -21.25272 1.000 24.71603  ? 91  ILE   A C   1 
ATOM   610  O  O   . ILE   A 1 84  ? -5.40038  -16.95778 -22.02250 1.000 23.13546  ? 91  ILE   A O   1 
ATOM   611  C  CB  . ILE   A 1 84  ? -5.19584  -16.28434 -19.11833 1.000 19.46818  ? 91  ILE   A CB  1 
ATOM   612  C  CG1 . ILE   A 1 84  ? -5.03015  -16.52702 -17.60811 1.000 26.66101  ? 91  ILE   A CG1 1 
ATOM   613  C  CG2 . ILE   A 1 84  ? -5.65661  -14.85353 -19.34526 1.000 23.66841  ? 91  ILE   A CG2 1 
ATOM   614  C  CD1 . ILE   A 1 84  ? -4.02774  -17.61389 -17.23663 1.000 31.18347  ? 91  ILE   A CD1 1 
ATOM   615  N  N   . VAL   A 1 85  ? -7.61246  -16.70154 -21.66547 1.000 21.67095  ? 92  VAL   A N   1 
ATOM   616  C  CA  . VAL   A 1 85  ? -7.94325  -16.45656 -23.06715 1.000 21.25538  ? 92  VAL   A CA  1 
ATOM   617  C  C   . VAL   A 1 85  ? -8.35211  -14.99977 -23.21757 1.000 24.41178  ? 92  VAL   A C   1 
ATOM   618  O  O   . VAL   A 1 85  ? -9.17396  -14.50229 -22.44272 1.000 25.25554  ? 92  VAL   A O   1 
ATOM   619  C  CB  . VAL   A 1 85  ? -9.09630  -17.35205 -23.55598 1.000 25.65241  ? 92  VAL   A CB  1 
ATOM   620  C  CG1 . VAL   A 1 85  ? -9.35670  -17.11712 -25.05104 1.000 27.49892  ? 92  VAL   A CG1 1 
ATOM   621  C  CG2 . VAL   A 1 85  ? -8.83762  -18.81439 -23.26426 1.000 30.88527  ? 92  VAL   A CG2 1 
ATOM   622  N  N   . ASP   A 1 86  ? -7.82621  -14.32539 -24.23690 1.000 20.77762  ? 93  ASP   A N   1 
ATOM   623  C  CA  . ASP   A 1 86  ? -8.31941  -12.99567 -24.55901 1.000 19.36611  ? 93  ASP   A CA  1 
ATOM   624  C  C   . ASP   A 1 86  ? -8.52475  -12.91034 -26.05968 1.000 23.04128  ? 93  ASP   A C   1 
ATOM   625  O  O   . ASP   A 1 86  ? -7.93596  -13.66396 -26.84289 1.000 25.50809  ? 93  ASP   A O   1 
ATOM   626  C  CB  . ASP   A 1 86  ? -7.36824  -11.89184 -24.04685 1.000 22.60418  ? 93  ASP   A CB  1 
ATOM   627  C  CG  . ASP   A 1 86  ? -6.04430  -11.84330 -24.79874 1.000 24.75245  ? 93  ASP   A CG  1 
ATOM   628  O  OD1 . ASP   A 1 86  ? -6.04422  -11.57803 -26.02386 1.000 27.25671  ? 93  ASP   A OD1 1 
ATOM   629  O  OD2 . ASP   A 1 86  ? -4.99606  -12.15105 -24.17680 1.000 26.62243  ? 93  ASP   A OD2 1 
ATOM   630  N  N   . THR   A 1 87  ? -9.40639  -12.00604 -26.45534 1.000 19.71545  ? 94  THR   A N   1 
ATOM   631  C  CA  . THR   A 1 87  ? -9.61331  -11.73249 -27.87475 1.000 20.17100  ? 94  THR   A CA  1 
ATOM   632  C  C   . THR   A 1 87  ? -8.91780  -10.44150 -28.28879 1.000 24.20313  ? 94  THR   A C   1 
ATOM   633  O  O   . THR   A 1 87  ? -9.43258  -9.65399  -29.09103 1.000 24.91614  ? 94  THR   A O   1 
ATOM   634  C  CB  . THR   A 1 87  ? -11.09956 -11.68426 -28.19883 1.000 25.43307  ? 94  THR   A CB  1 
ATOM   635  O  OG1 . THR   A 1 87  ? -11.74370 -10.82492 -27.26459 1.000 24.19782  ? 94  THR   A OG1 1 
ATOM   636  C  CG2 . THR   A 1 87  ? -11.72261 -13.08564 -28.10338 1.000 28.66762  ? 94  THR   A CG2 1 
ATOM   637  N  N   . GLY   A 1 88  ? -7.71483  -10.22161 -27.75869 1.000 22.85474  ? 95  GLY   A N   1 
ATOM   638  C  CA  . GLY   A 1 88  ? -6.95205  -9.03019  -28.09796 1.000 23.45174  ? 95  GLY   A CA  1 
ATOM   639  C  C   . GLY   A 1 88  ? -6.29035  -9.08031  -29.46445 1.000 24.58200  ? 95  GLY   A C   1 
ATOM   640  O  O   . GLY   A 1 88  ? -6.66675  -9.88364  -30.32077 1.000 22.73931  ? 95  GLY   A O   1 
ATOM   641  N  N   . ILE   A 1 89  ? -5.29607  -8.21120  -29.67814 1.000 20.18520  ? 96  ILE   A N   1 
ATOM   642  C  CA  . ILE   A 1 89  ? -4.67097  -8.08840  -30.99613 1.000 20.73899  ? 96  ILE   A CA  1 
ATOM   643  C  C   . ILE   A 1 89  ? -3.89224  -9.33745  -31.41099 1.000 25.58436  ? 96  ILE   A C   1 
ATOM   644  O  O   . ILE   A 1 89  ? -3.67025  -9.56070  -32.60973 1.000 24.36438  ? 96  ILE   A O   1 
ATOM   645  C  CB  . ILE   A 1 89  ? -3.78358  -6.82728  -31.01177 1.000 23.03393  ? 96  ILE   A CB  1 
ATOM   646  C  CG1 . ILE   A 1 89  ? -3.38160  -6.48370  -32.45704 1.000 28.12937  ? 96  ILE   A CG1 1 
ATOM   647  C  CG2 . ILE   A 1 89  ? -2.58557  -6.99985  -30.05420 1.000 25.68143  ? 96  ILE   A CG2 1 
ATOM   648  C  CD1 . ILE   A 1 89  ? -3.11181  -5.01418  -32.68520 1.000 37.60958  ? 96  ILE   A CD1 1 
ATOM   649  N  N   . GLY   A 1 90  ? -3.47061  -10.17273 -30.46727 1.000 22.92942  ? 97  GLY   A N   1 
ATOM   650  C  CA  . GLY   A 1 90  ? -2.72133  -11.35294 -30.83725 1.000 23.26986  ? 97  GLY   A CA  1 
ATOM   651  C  C   . GLY   A 1 90  ? -1.28222  -11.01116 -31.18618 1.000 27.59587  ? 97  GLY   A C   1 
ATOM   652  O  O   . GLY   A 1 90  ? -0.84213  -9.86226  -31.11485 1.000 25.47267  ? 97  GLY   A O   1 
ATOM   653  N  N   . MET   A 1 91  ? -0.52501  -12.04061 -31.55174 1.000 24.04636  ? 98  MET   A N   1 
ATOM   654  C  CA  . MET   A 1 91  ? 0.90505   -11.87633 -31.79210 1.000 22.62416  ? 98  MET   A CA  1 
ATOM   655  C  C   . MET   A 1 91  ? 1.27153   -12.55815 -33.09979 1.000 23.11160  ? 98  MET   A C   1 
ATOM   656  O  O   . MET   A 1 91  ? 0.76984   -13.64693 -33.40842 1.000 23.32670  ? 98  MET   A O   1 
ATOM   657  C  CB  . MET   A 1 91  ? 1.73313   -12.47437 -30.63741 1.000 23.09568  ? 98  MET   A CB  1 
ATOM   658  C  CG  . MET   A 1 91  ? 1.54652   -11.72910 -29.32712 1.000 22.42551  ? 98  MET   A CG  1 
ATOM   659  S  SD  . MET   A 1 91  ? 2.48074   -12.55982 -28.01903 1.000 29.55382  ? 98  MET   A SD  1 
ATOM   660  C  CE  . MET   A 1 91  ? 1.24069   -13.75996 -27.51664 1.000 30.07728  ? 98  MET   A CE  1 
ATOM   661  N  N   . THR   A 1 92  ? 2.14518   -11.91004 -33.86728 1.000 23.35865  ? 99  THR   A N   1 
ATOM   662  C  CA  . THR   A 1 92  ? 2.67118   -12.50407 -35.08781 1.000 25.20291  ? 99  THR   A CA  1 
ATOM   663  C  C   . THR   A 1 92  ? 3.84318   -13.43647 -34.76736 1.000 24.47474  ? 99  THR   A C   1 
ATOM   664  O  O   . THR   A 1 92  ? 4.37480   -13.45688 -33.65494 1.000 24.33499  ? 99  THR   A O   1 
ATOM   665  C  CB  . THR   A 1 92  ? 3.14181   -11.42511 -36.05808 1.000 27.40772  ? 99  THR   A CB  1 
ATOM   666  O  OG1 . THR   A 1 92  ? 4.24801   -10.73620 -35.47144 1.000 29.78290  ? 99  THR   A OG1 1 
ATOM   667  C  CG2 . THR   A 1 92  ? 2.03617   -10.41845 -36.33677 1.000 25.17931  ? 99  THR   A CG2 1 
ATOM   668  N  N   . LYS   A 1 93  ? 4.25835   -14.21520 -35.77033 1.000 25.29989  ? 100 LYS   A N   1 
ATOM   669  C  CA  . LYS   A 1 93  ? 5.43228   -15.05438 -35.56845 1.000 27.40264  ? 100 LYS   A CA  1 
ATOM   670  C  C   . LYS   A 1 93  ? 6.63394   -14.19369 -35.20030 1.000 26.57757  ? 100 LYS   A C   1 
ATOM   671  O  O   . LYS   A 1 93  ? 7.41660   -14.54581 -34.30281 1.000 26.46150  ? 100 LYS   A O   1 
ATOM   672  C  CB  . LYS   A 1 93  ? 5.71393   -15.88609 -36.82307 1.000 28.92110  ? 100 LYS   A CB  1 
ATOM   673  C  CG  . LYS   A 1 93  ? 6.79369   -16.93519 -36.61229 1.000 33.16937  ? 100 LYS   A CG  1 
ATOM   674  C  CD  . LYS   A 1 93  ? 6.99203   -17.82658 -37.83921 1.000 34.63714  ? 100 LYS   A CD  1 
ATOM   675  C  CE  . LYS   A 1 93  ? 7.84754   -19.03871 -37.47192 1.000 38.93260  ? 100 LYS   A CE  1 
ATOM   676  N  NZ  . LYS   A 1 93  ? 8.58460   -19.60884 -38.64487 1.000 41.90145  ? 100 LYS   A NZ  1 
ATOM   677  N  N   . ALA   A 1 94  ? 6.76983   -13.04005 -35.85776 1.000 27.30066  ? 101 ALA   A N   1 
ATOM   678  C  CA  . ALA   A 1 94  ? 7.89192   -12.14607 -35.58066 1.000 31.15439  ? 101 ALA   A CA  1 
ATOM   679  C  C   . ALA   A 1 94  ? 7.83657   -11.62511 -34.14727 1.000 31.83031  ? 101 ALA   A C   1 
ATOM   680  O  O   . ALA   A 1 94  ? 8.87465   -11.51905 -33.47846 1.000 28.36850  ? 101 ALA   A O   1 
ATOM   681  C  CB  . ALA   A 1 94  ? 7.90327   -10.98850 -36.57831 1.000 30.86590  ? 101 ALA   A CB  1 
ATOM   682  N  N   . ASP   A 1 95  ? 6.63456   -11.30259 -33.65685 1.000 27.11044  ? 102 ASP   A N   1 
ATOM   683  C  CA  . ASP   A 1 95  ? 6.47664   -10.95650 -32.24539 1.000 24.53986  ? 102 ASP   A CA  1 
ATOM   684  C  C   . ASP   A 1 95  ? 7.04430   -12.05297 -31.35643 1.000 29.17650  ? 102 ASP   A C   1 
ATOM   685  O  O   . ASP   A 1 95  ? 7.86450   -11.78946 -30.46480 1.000 27.96696  ? 102 ASP   A O   1 
ATOM   686  C  CB  . ASP   A 1 95  ? 4.99621   -10.74793 -31.90124 1.000 28.53308  ? 102 ASP   A CB  1 
ATOM   687  C  CG  . ASP   A 1 95  ? 4.42693   -9.45907  -32.45770 1.000 29.01109  ? 102 ASP   A CG  1 
ATOM   688  O  OD1 . ASP   A 1 95  ? 5.18695   -8.47615  -32.62827 1.000 31.55129  ? 102 ASP   A OD1 1 
ATOM   689  O  OD2 . ASP   A 1 95  ? 3.19260   -9.43929  -32.71903 1.000 29.68128  ? 102 ASP   A OD2 1 
ATOM   690  N  N   . LEU   A 1 96  ? 6.61971   -13.30005 -31.60186 1.000 24.51277  ? 103 LEU   A N   1 
ATOM   691  C  CA  . LEU   A 1 96  ? 6.97588   -14.41453 -30.72009 1.000 26.12626  ? 103 LEU   A CA  1 
ATOM   692  C  C   . LEU   A 1 96  ? 8.47271   -14.66452 -30.67843 1.000 32.14616  ? 103 LEU   A C   1 
ATOM   693  O  O   . LEU   A 1 96  ? 9.01918   -14.97759 -29.61585 1.000 32.49186  ? 103 LEU   A O   1 
ATOM   694  C  CB  . LEU   A 1 96  ? 6.25959   -15.69084 -31.16240 1.000 25.73093  ? 103 LEU   A CB  1 
ATOM   695  C  CG  . LEU   A 1 96  ? 4.75021   -15.73817 -31.00049 1.000 24.63829  ? 103 LEU   A CG  1 
ATOM   696  C  CD1 . LEU   A 1 96  ? 4.23315   -17.03081 -31.63044 1.000 28.77198  ? 103 LEU   A CD1 1 
ATOM   697  C  CD2 . LEU   A 1 96  ? 4.39222   -15.72411 -29.51940 1.000 24.37474  ? 103 LEU   A CD2 1 
ATOM   698  N  N   . ILE   A 1 97  ? 9.14159   -14.56308 -31.82406 1.000 29.36082  ? 104 ILE   A N   1 
ATOM   699  C  CA  . ILE   A 1 97  ? 10.54930  -14.94001 -31.94988 1.000 30.15497  ? 104 ILE   A CA  1 
ATOM   700  C  C   . ILE   A 1 97  ? 11.47306  -13.77879 -31.63071 1.000 39.40232  ? 104 ILE   A C   1 
ATOM   701  O  O   . ILE   A 1 97  ? 12.46523  -13.94503 -30.91521 1.000 42.13062  ? 104 ILE   A O   1 
ATOM   702  C  CB  . ILE   A 1 97  ? 10.85179  -15.46920 -33.37227 1.000 34.01304  ? 104 ILE   A CB  1 
ATOM   703  C  CG1 . ILE   A 1 97  ? 9.97453   -16.64986 -33.77793 1.000 43.12678  ? 104 ILE   A CG1 1 
ATOM   704  C  CG2 . ILE   A 1 97  ? 12.29841  -15.88962 -33.46290 1.000 41.83273  ? 104 ILE   A CG2 1 
ATOM   705  C  CD1 . ILE   A 1 97  ? 9.53141   -17.44183 -32.65556 1.000 48.72011  ? 104 ILE   A CD1 1 
ATOM   706  N  N   . ASN   A 1 98  ? 11.18807  -12.61020 -32.20842 1.000 29.06718  ? 105 ASN   A N   1 
ATOM   707  C  CA  . ASN   A 1 98  ? 12.12978  -11.49376 -32.26433 1.000 33.71753  ? 105 ASN   A CA  1 
ATOM   708  C  C   . ASN   A 1 98  ? 11.68543  -10.28888 -31.44895 1.000 32.72796  ? 105 ASN   A C   1 
ATOM   709  O  O   . ASN   A 1 98  ? 12.44109  -9.80240  -30.60103 1.000 33.38335  ? 105 ASN   A O   1 
ATOM   710  C  CB  . ASN   A 1 98  ? 12.34646  -11.04971 -33.71922 1.000 39.28213  ? 105 ASN   A CB  1 
ATOM   711  C  CG  . ASN   A 1 98  ? 12.81614  -12.16722 -34.61148 1.000 63.13569  ? 105 ASN   A CG  1 
ATOM   712  O  OD1 . ASN   A 1 98  ? 13.92390  -12.67563 -34.44878 1.000 62.16658  ? 105 ASN   A OD1 1 
ATOM   713  N  ND2 . ASN   A 1 98  ? 11.97715  -12.56032 -35.56431 1.000 62.92487  ? 105 ASN   A ND2 1 
ATOM   714  N  N   . ASN   A 1 99  ? 10.50215  -9.74055  -31.73502 1.000 30.45163  ? 106 ASN   A N   1 
ATOM   715  C  CA  . ASN   A 1 99  ? 10.17981  -8.40225  -31.24447 1.000 28.81821  ? 106 ASN   A CA  1 
ATOM   716  C  C   . ASN   A 1 99  ? 10.00711  -8.39853  -29.73607 1.000 31.50483  ? 106 ASN   A C   1 
ATOM   717  O  O   . ASN   A 1 99  ? 10.55296  -7.53594  -29.04395 1.000 32.41355  ? 106 ASN   A O   1 
ATOM   718  C  CB  . ASN   A 1 99  ? 8.92428   -7.83918  -31.93298 1.000 30.60375  ? 106 ASN   A CB  1 
ATOM   719  C  CG  . ASN   A 1 99  ? 9.01990   -7.83568  -33.45396 1.000 40.97581  ? 106 ASN   A CG  1 
ATOM   720  O  OD1 . ASN   A 1 99  ? 10.10925  -7.77821  -34.02169 1.000 41.86687  ? 106 ASN   A OD1 1 
ATOM   721  N  ND2 . ASN   A 1 99  ? 7.86358   -7.85793  -34.12203 1.000 39.46605  ? 106 ASN   A ND2 1 
ATOM   722  N  N   . LEU   A 1 100 ? 9.25115   -9.35750  -29.20751 1.000 30.63221  ? 107 LEU   A N   1 
ATOM   723  C  CA  . LEU   A 1 100 ? 9.05501   -9.41051  -27.76620 1.000 28.31310  ? 107 LEU   A CA  1 
ATOM   724  C  C   . LEU   A 1 100 ? 10.35792  -9.68434  -27.03232 1.000 29.33435  ? 107 LEU   A C   1 
ATOM   725  O  O   . LEU   A 1 100 ? 10.58021  -9.14740  -25.94271 1.000 37.99947  ? 107 LEU   A O   1 
ATOM   726  C  CB  . LEU   A 1 100 ? 8.03037   -10.48224 -27.42933 1.000 28.04197  ? 107 LEU   A CB  1 
ATOM   727  C  CG  . LEU   A 1 100 ? 6.63128   -10.09654 -27.88903 1.000 32.00357  ? 107 LEU   A CG  1 
ATOM   728  C  CD1 . LEU   A 1 100 ? 5.71430   -11.26103 -27.63625 1.000 30.56546  ? 107 LEU   A CD1 1 
ATOM   729  C  CD2 . LEU   A 1 100 ? 6.15435   -8.84803  -27.16298 1.000 39.54050  ? 107 LEU   A CD2 1 
ATOM   730  N  N   . GLY   A 1 101 ? 11.22849  -10.50931 -27.61416 1.000 33.20125  ? 108 GLY   A N   1 
ATOM   731  C  CA  . GLY   A 1 101 ? 12.51338  -10.77195 -26.98554 1.000 42.99443  ? 108 GLY   A CA  1 
ATOM   732  C  C   . GLY   A 1 101 ? 13.40144  -9.54360  -26.94443 1.000 35.58918  ? 108 GLY   A C   1 
ATOM   733  O  O   . GLY   A 1 101 ? 14.14052  -9.33292  -25.97726 1.000 35.13289  ? 108 GLY   A O   1 
ATOM   734  N  N   . THR   A 1 102 ? 13.35456  -8.72242  -27.99338 1.000 29.94507  ? 109 THR   A N   1 
ATOM   735  C  CA  . THR   A 1 102 ? 14.10175  -7.46873  -27.97559 1.000 29.55411  ? 109 THR   A CA  1 
ATOM   736  C  C   . THR   A 1 102 ? 13.62136  -6.55469  -26.85784 1.000 35.69596  ? 109 THR   A C   1 
ATOM   737  O  O   . THR   A 1 102 ? 14.43121  -5.99084  -26.11371 1.000 35.71851  ? 109 THR   A O   1 
ATOM   738  C  CB  . THR   A 1 102 ? 13.99269  -6.76069  -29.32162 1.000 36.97104  ? 109 THR   A CB  1 
ATOM   739  O  OG1 . THR   A 1 102 ? 14.40411  -7.65670  -30.35731 1.000 42.33089  ? 109 THR   A OG1 1 
ATOM   740  C  CG2 . THR   A 1 102 ? 14.86028  -5.51237  -29.33860 1.000 40.65837  ? 109 THR   A CG2 1 
ATOM   741  N  N   . ILE   A 1 103 ? 12.30450  -6.38296  -26.73144 1.000 32.45558  ? 110 ILE   A N   1 
ATOM   742  C  CA  . ILE   A 1 103 ? 11.77602  -5.55736  -25.64421 1.000 38.14654  ? 110 ILE   A CA  1 
ATOM   743  C  C   . ILE   A 1 103 ? 12.10544  -6.18167  -24.29697 1.000 39.09709  ? 110 ILE   A C   1 
ATOM   744  O  O   . ILE   A 1 103 ? 12.43549  -5.48455  -23.32817 1.000 48.30375  ? 110 ILE   A O   1 
ATOM   745  C  CB  . ILE   A 1 103 ? 10.25834  -5.34548  -25.81507 1.000 47.65456  ? 110 ILE   A CB  1 
ATOM   746  C  CG1 . ILE   A 1 103 ? 9.94516   -4.87047  -27.23043 1.000 47.17844  ? 110 ILE   A CG1 1 
ATOM   747  C  CG2 . ILE   A 1 103 ? 9.73164   -4.35239  -24.79464 1.000 52.01293  ? 110 ILE   A CG2 1 
ATOM   748  C  CD1 . ILE   A 1 103 ? 10.41909  -3.45642  -27.52400 1.000 52.58446  ? 110 ILE   A CD1 1 
ATOM   749  N  N   . ALA   A 1 104 ? 12.04228  -7.50351  -24.21675 1.000 30.72965  ? 111 ALA   A N   1 
ATOM   750  C  CA  . ALA   A 1 104 ? 12.23372  -8.17189  -22.93921 1.000 38.30510  ? 111 ALA   A CA  1 
ATOM   751  C  C   . ALA   A 1 104 ? 13.68621  -8.13143  -22.46980 1.000 44.42720  ? 111 ALA   A C   1 
ATOM   752  O  O   . ALA   A 1 104 ? 13.93813  -8.23529  -21.26257 1.000 40.91677  ? 111 ALA   A O   1 
ATOM   753  C  CB  . ALA   A 1 104 ? 11.74167  -9.60902  -23.03872 1.000 38.74279  ? 111 ALA   A CB  1 
ATOM   754  N  N   . LYS   A 1 105 ? 14.64439  -7.97796  -23.38686 1.000 36.45934  ? 112 LYS   A N   1 
ATOM   755  C  CA  . LYS   A 1 105 ? 16.04668  -7.89076  -22.98211 1.000 31.86210  ? 112 LYS   A CA  1 
ATOM   756  C  C   . LYS   A 1 105 ? 16.29313  -6.66246  -22.11817 1.000 39.01814  ? 112 LYS   A C   1 
ATOM   757  O  O   . LYS   A 1 105 ? 16.93538  -6.74215  -21.06093 1.000 34.42794  ? 112 LYS   A O   1 
ATOM   758  C  CB  . LYS   A 1 105 ? 16.94838  -7.86140  -24.21968 1.000 35.66084  ? 112 LYS   A CB  1 
ATOM   759  C  CG  . LYS   A 1 105 ? 18.41968  -8.14863  -23.95132 1.000 39.46281  ? 112 LYS   A CG  1 
ATOM   760  C  CD  . LYS   A 1 105 ? 19.22102  -7.99909  -25.24216 1.000 42.04704  ? 112 LYS   A CD  1 
ATOM   761  C  CE  . LYS   A 1 105 ? 20.57072  -8.68529  -25.16661 1.000 58.96771  ? 112 LYS   A CE  1 
ATOM   762  N  NZ  . LYS   A 1 105 ? 21.60788  -7.78887  -24.60352 1.000 60.97715  ? 112 LYS   A NZ  1 
ATOM   763  N  N   . SER   A 1 106 ? 15.81547  -5.50476  -22.56686 1.000 35.95481  ? 113 SER   A N   1 
ATOM   764  C  CA  . SER   A 1 106 ? 16.06670  -4.28698  -21.80945 1.000 35.45061  ? 113 SER   A CA  1 
ATOM   765  C  C   . SER   A 1 106 ? 15.23776  -4.26883  -20.53786 1.000 35.32179  ? 113 SER   A C   1 
ATOM   766  O  O   . SER   A 1 106 ? 15.70438  -3.79562  -19.49538 1.000 36.88865  ? 113 SER   A O   1 
ATOM   767  C  CB  . SER   A 1 106 ? 15.76835  -3.05497  -22.66062 1.000 42.49610  ? 113 SER   A CB  1 
ATOM   768  O  OG  . SER   A 1 106 ? 14.60204  -3.26257  -23.43056 1.000 51.70312  ? 113 SER   A OG  1 
ATOM   769  N  N   . GLY   A 1 107 ? 14.00708  -4.79273  -20.60316 1.000 37.21878  ? 114 GLY   A N   1 
ATOM   770  C  CA  . GLY   A 1 107 ? 13.17429  -4.84424  -19.41331 1.000 32.46090  ? 114 GLY   A CA  1 
ATOM   771  C  C   . GLY   A 1 107 ? 13.76099  -5.75374  -18.35357 1.000 29.95549  ? 114 GLY   A C   1 
ATOM   772  O  O   . GLY   A 1 107 ? 13.70683  -5.45120  -17.15811 1.000 28.28395  ? 114 GLY   A O   1 
ATOM   773  N  N   . THR   A 1 108 ? 14.33427  -6.87879  -18.77887 1.000 27.67258  ? 115 THR   A N   1 
ATOM   774  C  CA  . THR   A 1 108 ? 14.96921  -7.79552  -17.83535 1.000 32.84455  ? 115 THR   A CA  1 
ATOM   775  C  C   . THR   A 1 108 ? 16.15802  -7.14052  -17.15327 1.000 35.95481  ? 115 THR   A C   1 
ATOM   776  O  O   . THR   A 1 108 ? 16.31739  -7.23939  -15.92883 1.000 32.35581  ? 115 THR   A O   1 
ATOM   777  C  CB  . THR   A 1 108 ? 15.42097  -9.06993  -18.55312 1.000 34.18884  ? 115 THR   A CB  1 
ATOM   778  O  OG1 . THR   A 1 108 ? 14.27520  -9.79457  -19.00544 1.000 36.61108  ? 115 THR   A OG1 1 
ATOM   779  C  CG2 . THR   A 1 108 ? 16.22326  -9.95440  -17.61070 1.000 33.99897  ? 115 THR   A CG2 1 
ATOM   780  N  N   . LYS   A 1 109 ? 17.03881  -6.51422  -17.94270 1.000 30.31156  ? 116 LYS   A N   1 
ATOM   781  C  CA  . LYS   A 1 109 ? 18.18133  -5.80746  -17.37309 1.000 36.34759  ? 116 LYS   A CA  1 
ATOM   782  C  C   . LYS   A 1 109 ? 17.73847  -4.84768  -16.28031 1.000 34.92912  ? 116 LYS   A C   1 
ATOM   783  O  O   . LYS   A 1 109 ? 18.31432  -4.82541  -15.18934 1.000 36.46718  ? 116 LYS   A O   1 
ATOM   784  C  CB  . LYS   A 1 109 ? 18.94086  -5.03962  -18.46253 1.000 38.44750  ? 116 LYS   A CB  1 
ATOM   785  C  CG  . LYS   A 1 109 ? 20.11032  -5.76898  -19.10743 1.000 62.22042  ? 116 LYS   A CG  1 
ATOM   786  C  CD  . LYS   A 1 109 ? 20.55880  -5.03667  -20.37457 1.000 69.87199  ? 116 LYS   A CD  1 
ATOM   787  C  CE  . LYS   A 1 109 ? 20.99450  -5.98977  -21.47924 1.000 58.55191  ? 116 LYS   A CE  1 
ATOM   788  N  NZ  . LYS   A 1 109 ? 21.50367  -7.27316  -20.93552 1.000 61.36999  ? 116 LYS   A NZ  1 
ATOM   789  N  N   . ALA   A 1 110 ? 16.71187  -4.04241  -16.56458 1.000 33.48589  ? 117 ALA   A N   1 
ATOM   790  C  CA  . ALA   A 1 110 ? 16.21719  -3.07246  -15.58727 1.000 33.62813  ? 117 ALA   A CA  1 
ATOM   791  C  C   . ALA   A 1 110 ? 15.62827  -3.75518  -14.35743 1.000 29.76121  ? 117 ALA   A C   1 
ATOM   792  O  O   . ALA   A 1 110 ? 15.82825  -3.29354  -13.22413 1.000 33.96979  ? 117 ALA   A O   1 
ATOM   793  C  CB  . ALA   A 1 110 ? 15.16958  -2.17054  -16.24263 1.000 35.99055  ? 117 ALA   A CB  1 
ATOM   794  N  N   . PHE   A 1 111 ? 14.87483  -4.83492  -14.56365 1.000 27.24809  ? 118 PHE   A N   1 
ATOM   795  C  CA  . PHE   A 1 111 ? 14.26330  -5.54490  -13.44918 1.000 30.27209  ? 118 PHE   A CA  1 
ATOM   796  C  C   . PHE   A 1 111 ? 15.32835  -6.14486  -12.54505 1.000 31.94583  ? 118 PHE   A C   1 
ATOM   797  O  O   . PHE   A 1 111 ? 15.22605  -6.06276  -11.31899 1.000 32.75027  ? 118 PHE   A O   1 
ATOM   798  C  CB  . PHE   A 1 111 ? 13.31440  -6.61056  -14.00411 1.000 26.49692  ? 118 PHE   A CB  1 
ATOM   799  C  CG  . PHE   A 1 111 ? 12.59308  -7.43252  -12.95492 1.000 28.68677  ? 118 PHE   A CG  1 
ATOM   800  C  CD1 . PHE   A 1 111 ? 11.90944  -6.83201  -11.90189 1.000 29.62496  ? 118 PHE   A CD1 1 
ATOM   801  C  CD2 . PHE   A 1 111 ? 12.53095  -8.81092  -13.08141 1.000 32.55480  ? 118 PHE   A CD2 1 
ATOM   802  C  CE1 . PHE   A 1 111 ? 11.22818  -7.60030  -10.96827 1.000 31.72432  ? 118 PHE   A CE1 1 
ATOM   803  C  CE2 . PHE   A 1 111 ? 11.84571  -9.58451  -12.16042 1.000 34.45710  ? 118 PHE   A CE2 1 
ATOM   804  C  CZ  . PHE   A 1 111 ? 11.18941  -8.97602  -11.09912 1.000 34.35843  ? 118 PHE   A CZ  1 
ATOM   805  N  N   . MET   A 1 112 ? 16.37715  -6.72280  -13.13666 1.000 33.02401  ? 119 MET   A N   1 
ATOM   806  C  CA  . MET   A 1 112 ? 17.45812  -7.28487  -12.33228 1.000 36.54507  ? 119 MET   A CA  1 
ATOM   807  C  C   . MET   A 1 112 ? 18.16233  -6.21735  -11.51303 1.000 39.69984  ? 119 MET   A C   1 
ATOM   808  O  O   . MET   A 1 112 ? 18.48505  -6.44573  -10.34149 1.000 46.05526  ? 119 MET   A O   1 
ATOM   809  C  CB  . MET   A 1 112 ? 18.46507  -8.01694  -13.22135 1.000 42.34843  ? 119 MET   A CB  1 
ATOM   810  C  CG  . MET   A 1 112 ? 17.82859  -9.07446  -14.07832 1.000 38.70512  ? 119 MET   A CG  1 
ATOM   811  S  SD  . MET   A 1 112 ? 17.33987  -10.46374 -13.04409 1.000 59.47770  ? 119 MET   A SD  1 
ATOM   812  C  CE  . MET   A 1 112 ? 17.75343  -11.81785 -14.14308 1.000 42.28627  ? 119 MET   A CE  1 
ATOM   813  N  N   . GLU   A 1 113 ? 18.43286  -5.05271  -12.11119 1.000 43.49830  ? 120 GLU   A N   1 
ATOM   814  C  CA  . GLU   A 1 113 ? 19.02046  -3.96603  -11.33092 1.000 45.89854  ? 120 GLU   A CA  1 
ATOM   815  C  C   . GLU   A 1 113 ? 18.11293  -3.57364  -10.17296 1.000 45.23152  ? 120 GLU   A C   1 
ATOM   816  O  O   . GLU   A 1 113 ? 18.58520  -3.38355  -9.04658  1.000 45.19219  ? 120 GLU   A O   1 
ATOM   817  C  CB  . GLU   A 1 113 ? 19.31553  -2.75196  -12.21504 1.000 48.21841  ? 120 GLU   A CB  1 
ATOM   818  C  CG  . GLU   A 1 113 ? 19.86821  -3.08672  -13.58492 1.000 61.56033  ? 120 GLU   A CG  1 
ATOM   819  C  CD  . GLU   A 1 113 ? 20.96784  -2.16027  -14.04637 1.000 71.47292  ? 120 GLU   A CD  1 
ATOM   820  O  OE1 . GLU   A 1 113 ? 20.76110  -0.92910  -13.98881 1.000 86.69750  ? 120 GLU   A OE1 1 
ATOM   821  O  OE2 . GLU   A 1 113 ? 22.02688  -2.65795  -14.48713 1.000 78.21053  ? 120 GLU   A OE2 1 
ATOM   822  N  N   . ALA   A 1 114 ? 16.80380  -3.46839  -10.42624 1.000 43.53586  ? 121 ALA   A N   1 
ATOM   823  C  CA  . ALA   A 1 114 ? 15.87561  -3.07899  -9.36740  1.000 43.16568  ? 121 ALA   A CA  1 
ATOM   824  C  C   . ALA   A 1 114 ? 15.84503  -4.11276  -8.24882  1.000 40.60482  ? 121 ALA   A C   1 
ATOM   825  O  O   . ALA   A 1 114 ? 15.83527  -3.75905  -7.06469  1.000 44.91181  ? 121 ALA   A O   1 
ATOM   826  C  CB  . ALA   A 1 114 ? 14.48037  -2.87464  -9.95395  1.000 40.77664  ? 121 ALA   A CB  1 
ATOM   827  N  N   . LEU   A 1 115 ? 15.81915  -5.39950  -8.60449  1.000 40.05512  ? 122 LEU   A N   1 
ATOM   828  C  CA  . LEU   A 1 115 ? 15.82408  -6.44551  -7.58489  1.000 45.14189  ? 122 LEU   A CA  1 
ATOM   829  C  C   . LEU   A 1 115 ? 17.05065  -6.33802  -6.69137  1.000 57.31659  ? 122 LEU   A C   1 
ATOM   830  O  O   . LEU   A 1 115 ? 16.94950  -6.45494  -5.46255  1.000 55.82272  ? 122 LEU   A O   1 
ATOM   831  C  CB  . LEU   A 1 115 ? 15.76496  -7.81881  -8.24922  1.000 38.76370  ? 122 LEU   A CB  1 
ATOM   832  C  CG  . LEU   A 1 115 ? 14.39996  -8.22346  -8.80212  1.000 37.12166  ? 122 LEU   A CG  1 
ATOM   833  C  CD1 . LEU   A 1 115 ? 14.46203  -9.60717  -9.43149  1.000 42.23398  ? 122 LEU   A CD1 1 
ATOM   834  C  CD2 . LEU   A 1 115 ? 13.33844  -8.18178  -7.71694  1.000 41.75401  ? 122 LEU   A CD2 1 
ATOM   835  N  N   . GLN   A 1 116 ? 18.22190  -6.11165  -7.28622  1.000 55.22432  ? 123 GLN   A N   1 
ATOM   836  C  CA  . GLN   A 1 116 ? 19.41635  -5.97411  -6.46666  1.000 55.74761  ? 123 GLN   A CA  1 
ATOM   837  C  C   . GLN   A 1 116 ? 19.37279  -4.70620  -5.62390  1.000 56.65563  ? 123 GLN   A C   1 
ATOM   838  O  O   . GLN   A 1 116 ? 20.00254  -4.64692  -4.56095  1.000 66.79974  ? 123 GLN   A O   1 
ATOM   839  C  CB  . GLN   A 1 116 ? 20.66814  -5.99709  -7.33889  1.000 62.38992  ? 123 GLN   A CB  1 
ATOM   840  C  CG  . GLN   A 1 116 ? 21.18762  -7.39524  -7.59743  1.000 74.89326  ? 123 GLN   A CG  1 
ATOM   841  C  CD  . GLN   A 1 116 ? 22.60128  -7.39359  -8.14500  1.000 103.36598 ? 123 GLN   A CD  1 
ATOM   842  O  OE1 . GLN   A 1 116 ? 23.15555  -6.33989  -8.46191  1.000 109.55698 ? 123 GLN   A OE1 1 
ATOM   843  N  NE2 . GLN   A 1 116 ? 23.20223  -8.57536  -8.23775  1.000 108.45467 ? 123 GLN   A NE2 1 
ATOM   844  N  N   . ALA   A 1 117 ? 18.63315  -3.69248  -6.07368  1.000 63.02962  ? 124 ALA   A N   1 
ATOM   845  C  CA  . ALA   A 1 117 ? 18.44786  -2.47239  -5.30082  1.000 58.44347  ? 124 ALA   A CA  1 
ATOM   846  C  C   . ALA   A 1 117 ? 17.43330  -2.63124  -4.17424  1.000 67.20844  ? 124 ALA   A C   1 
ATOM   847  O  O   . ALA   A 1 117 ? 17.33427  -1.74127  -3.32515  1.000 71.83408  ? 124 ALA   A O   1 
ATOM   848  C  CB  . ALA   A 1 117 ? 18.01323  -1.32894  -6.22308  1.000 58.27374  ? 124 ALA   A CB  1 
ATOM   849  N  N   . GLY   A 1 118 ? 16.67187  -3.72249  -4.14917  1.000 65.21038  ? 125 GLY   A N   1 
ATOM   850  C  CA  . GLY   A 1 118 ? 15.72241  -3.96987  -3.07580  1.000 58.45164  ? 125 GLY   A CA  1 
ATOM   851  C  C   . GLY   A 1 118 ? 14.27928  -4.13624  -3.51181  1.000 56.00544  ? 125 GLY   A C   1 
ATOM   852  O  O   . GLY   A 1 118 ? 13.42304  -4.38899  -2.65155  1.000 60.46486  ? 125 GLY   A O   1 
ATOM   853  N  N   . ALA   A 1 119 ? 13.95565  -3.99159  -4.79440  1.000 49.32936  ? 126 ALA   A N   1 
ATOM   854  C  CA  . ALA   A 1 119 ? 12.60446  -4.26715  -5.26262  1.000 44.69460  ? 126 ALA   A CA  1 
ATOM   855  C  C   . ALA   A 1 119 ? 12.29508  -5.75111  -5.09819  1.000 48.36741  ? 126 ALA   A C   1 
ATOM   856  O  O   . ALA   A 1 119 ? 13.17507  -6.56765  -4.82465  1.000 51.96490  ? 126 ALA   A O   1 
ATOM   857  C  CB  . ALA   A 1 119 ? 12.44132  -3.84226  -6.71754  1.000 42.86920  ? 126 ALA   A CB  1 
ATOM   858  N  N   . ASP   A 1 120 ? 11.02480  -6.11030  -5.24596  1.000 49.60549  ? 127 ASP   A N   1 
ATOM   859  C  CA  . ASP   A 1 120 ? 10.70978  -7.52515  -5.18432  1.000 49.58079  ? 127 ASP   A CA  1 
ATOM   860  C  C   . ASP   A 1 120 ? 10.02371  -7.95756  -6.46599  1.000 37.97892  ? 127 ASP   A C   1 
ATOM   861  O  O   . ASP   A 1 120 ? 9.65401   -7.14986  -7.32807  1.000 39.04582  ? 127 ASP   A O   1 
ATOM   862  C  CB  . ASP   A 1 120 ? 9.81312   -7.90393  -3.99788  1.000 54.00622  ? 127 ASP   A CB  1 
ATOM   863  C  CG  . ASP   A 1 120 ? 8.41614   -7.36670  -4.13067  1.000 58.97404  ? 127 ASP   A CG  1 
ATOM   864  O  OD1 . ASP   A 1 120 ? 8.25279   -6.14993  -4.26704  1.000 68.31020  ? 127 ASP   A OD1 1 
ATOM   865  O  OD2 . ASP   A 1 120 ? 7.47602   -8.18929  -4.17964  1.000 55.64389  ? 127 ASP   A OD2 1 
ATOM   866  N  N   . ILE   A 1 121 ? 9.85171   -9.27211  -6.55955  1.000 38.88742  ? 128 ILE   A N   1 
ATOM   867  C  CA  . ILE   A 1 121 ? 9.37921   -9.88260  -7.79073  1.000 33.77511  ? 128 ILE   A CA  1 
ATOM   868  C  C   . ILE   A 1 121 ? 8.02136   -9.32571  -8.20069  1.000 32.52243  ? 128 ILE   A C   1 
ATOM   869  O  O   . ILE   A 1 121 ? 7.70045   -9.28979  -9.39194  1.000 33.20101  ? 128 ILE   A O   1 
ATOM   870  C  CB  . ILE   A 1 121 ? 9.38410   -11.41418 -7.60619  1.000 33.27457  ? 128 ILE   A CB  1 
ATOM   871  C  CG1 . ILE   A 1 121 ? 10.83261  -11.91676 -7.66401  1.000 44.55350  ? 128 ILE   A CG1 1 
ATOM   872  C  CG2 . ILE   A 1 121 ? 8.53793   -12.12027 -8.65162  1.000 33.81029  ? 128 ILE   A CG2 1 
ATOM   873  C  CD1 . ILE   A 1 121 ? 11.05660  -13.30067 -7.06978  1.000 50.13207  ? 128 ILE   A CD1 1 
ATOM   874  N  N   . SER   A 1 122 ? 7.22394   -8.83687  -7.24800  1.000 34.28990  ? 129 SER   A N   1 
ATOM   875  C  CA  . SER   A 1 122 ? 5.87855   -8.39989  -7.61320  1.000 33.90311  ? 129 SER   A CA  1 
ATOM   876  C  C   . SER   A 1 122 ? 5.86397   -7.14714  -8.48629  1.000 41.29340  ? 129 SER   A C   1 
ATOM   877  O  O   . SER   A 1 122 ? 4.82582   -6.85843  -9.08795  1.000 37.31027  ? 129 SER   A O   1 
ATOM   878  C  CB  . SER   A 1 122 ? 5.02130   -8.15979  -6.36860  1.000 34.44519  ? 129 SER   A CB  1 
ATOM   879  O  OG  . SER   A 1 122 ? 5.35167   -6.93997  -5.72989  1.000 42.75003  ? 129 SER   A OG  1 
ATOM   880  N  N   . MET   A 1 123 ? 6.95971   -6.38451  -8.57474  1.000 31.98355  ? 130 MET   A N   1 
ATOM   881  C  CA  . MET   A 1 123 ? 6.97779   -5.26675  -9.51362  1.000 33.48413  ? 130 MET   A CA  1 
ATOM   882  C  C   . MET   A 1 123 ? 7.42425   -5.64841  -10.92286 1.000 32.30026  ? 130 MET   A C   1 
ATOM   883  O  O   . MET   A 1 123 ? 7.65710   -4.75429  -11.74171 1.000 30.64392  ? 130 MET   A O   1 
ATOM   884  C  CB  . MET   A 1 123 ? 7.84025   -4.10234  -9.00672  1.000 40.03900  ? 130 MET   A CB  1 
ATOM   885  C  CG  . MET   A 1 123 ? 7.40066   -3.44195  -7.71245  1.000 41.57463  ? 130 MET   A CG  1 
ATOM   886  S  SD  . MET   A 1 123 ? 8.81358   -2.66225  -6.91743  1.000 59.68154  ? 130 MET   A SD  1 
ATOM   887  C  CE  . MET   A 1 123 ? 9.03169   -3.65984  -5.47345  1.000 60.63386  ? 130 MET   A CE  1 
ATOM   888  N  N   . ILE   A 1 124 ? 7.47708   -6.94536  -11.24163 1.000 28.76637  ? 131 ILE   A N   1 
ATOM   889  C  CA  . ILE   A 1 124 ? 7.96244   -7.41077  -12.53619 1.000 25.03776  ? 131 ILE   A CA  1 
ATOM   890  C  C   . ILE   A 1 124 ? 7.21050   -6.75242  -13.68982 1.000 29.80861  ? 131 ILE   A C   1 
ATOM   891  O  O   . ILE   A 1 124 ? 7.79264   -6.46564  -14.74120 1.000 28.18911  ? 131 ILE   A O   1 
ATOM   892  C  CB  . ILE   A 1 124 ? 7.87020   -8.94892  -12.61031 1.000 26.84585  ? 131 ILE   A CB  1 
ATOM   893  C  CG1 . ILE   A 1 124 ? 8.45823   -9.45433  -13.92198 1.000 27.83066  ? 131 ILE   A CG1 1 
ATOM   894  C  CG2 . ILE   A 1 124 ? 6.41102   -9.43103  -12.43736 1.000 28.94941  ? 131 ILE   A CG2 1 
ATOM   895  C  CD1 . ILE   A 1 124 ? 8.52448   -10.97964 -13.99985 1.000 30.82397  ? 131 ILE   A CD1 1 
ATOM   896  N  N   . GLY   A 1 125 ? 5.91150   -6.49292  -13.51488 1.000 32.08729  ? 132 GLY   A N   1 
ATOM   897  C  CA  . GLY   A 1 125 ? 5.13019   -5.94684  -14.61692 1.000 30.09918  ? 132 GLY   A CA  1 
ATOM   898  C  C   . GLY   A 1 125 ? 5.53263   -4.54156  -15.01067 1.000 34.19849  ? 132 GLY   A C   1 
ATOM   899  O  O   . GLY   A 1 125 ? 5.28328   -4.12176  -16.14641 1.000 34.62810  ? 132 GLY   A O   1 
ATOM   900  N  N   . GLN   A 1 126 ? 6.17641   -3.81092  -14.10560 1.000 31.00514  ? 133 GLN   A N   1 
ATOM   901  C  CA  . GLN   A 1 126 ? 6.62864   -2.46294  -14.41502 1.000 37.96922  ? 133 GLN   A CA  1 
ATOM   902  C  C   . GLN   A 1 126 ? 7.73732   -2.47186  -15.45042 1.000 41.90068  ? 133 GLN   A C   1 
ATOM   903  O  O   . GLN   A 1 126 ? 8.02897   -1.43651  -16.05838 1.000 34.97138  ? 133 GLN   A O   1 
ATOM   904  C  CB  . GLN   A 1 126 ? 7.10993   -1.80693  -13.13078 1.000 38.17321  ? 133 GLN   A CB  1 
ATOM   905  C  CG  . GLN   A 1 126 ? 5.99244   -1.22345  -12.32018 1.000 37.71949  ? 133 GLN   A CG  1 
ATOM   906  C  CD  . GLN   A 1 126 ? 6.50447   -0.41392  -11.16220 1.000 47.94557  ? 133 GLN   A CD  1 
ATOM   907  O  OE1 . GLN   A 1 126 ? 7.22408   0.56978   -11.34098 1.000 61.76489  ? 133 GLN   A OE1 1 
ATOM   908  N  NE2 . GLN   A 1 126 ? 6.17403   -0.85149  -9.95542  1.000 52.23430  ? 133 GLN   A NE2 1 
ATOM   909  N  N   . PHE   A 1 127 ? 8.35496   -3.62538  -15.66901 1.000 28.56870  ? 134 PHE   A N   1 
ATOM   910  C  CA  . PHE   A 1 127 ? 9.49236   -3.75311  -16.56034 1.000 31.96166  ? 134 PHE   A CA  1 
ATOM   911  C  C   . PHE   A 1 127 ? 9.12790   -4.46119  -17.85207 1.000 32.24621  ? 134 PHE   A C   1 
ATOM   912  O  O   . PHE   A 1 127 ? 10.01973  -4.80655  -18.63299 1.000 31.68987  ? 134 PHE   A O   1 
ATOM   913  C  CB  . PHE   A 1 127 ? 10.62342  -4.47617  -15.82227 1.000 30.51715  ? 134 PHE   A CB  1 
ATOM   914  C  CG  . PHE   A 1 127 ? 11.01824  -3.78839  -14.55340 1.000 30.38455  ? 134 PHE   A CG  1 
ATOM   915  C  CD1 . PHE   A 1 127 ? 11.91952  -2.73313  -14.58306 1.000 29.60451  ? 134 PHE   A CD1 1 
ATOM   916  C  CD2 . PHE   A 1 127 ? 10.46195  -4.16016  -13.33629 1.000 31.39473  ? 134 PHE   A CD2 1 
ATOM   917  C  CE1 . PHE   A 1 127 ? 12.27884  -2.07392  -13.42521 1.000 29.19478  ? 134 PHE   A CE1 1 
ATOM   918  C  CE2 . PHE   A 1 127 ? 10.81471  -3.50616  -12.16665 1.000 32.84100  ? 134 PHE   A CE2 1 
ATOM   919  C  CZ  . PHE   A 1 127 ? 11.72318  -2.45572  -12.20862 1.000 34.35409  ? 134 PHE   A CZ  1 
ATOM   920  N  N   . GLY   A 1 128 ? 7.83758   -4.70049  -18.08646 1.000 32.59178  ? 135 GLY   A N   1 
ATOM   921  C  CA  . GLY   A 1 128 ? 7.38594   -5.25791  -19.34018 1.000 33.86954  ? 135 GLY   A CA  1 
ATOM   922  C  C   . GLY   A 1 128 ? 7.57445   -6.74511  -19.50181 1.000 34.12514  ? 135 GLY   A C   1 
ATOM   923  O  O   . GLY   A 1 128 ? 7.28483   -7.27309  -20.58047 1.000 36.90660  ? 135 GLY   A O   1 
ATOM   924  N  N   . VAL   A 1 129 ? 8.03247   -7.44700  -18.46760 1.000 27.41110  ? 136 VAL   A N   1 
ATOM   925  C  CA  . VAL   A 1 129 ? 8.30272   -8.87146  -18.59540 1.000 25.21722  ? 136 VAL   A CA  1 
ATOM   926  C  C   . VAL   A 1 129 ? 7.41052   -9.66519  -17.64979 1.000 23.68029  ? 136 VAL   A C   1 
ATOM   927  O  O   . VAL   A 1 129 ? 7.76031   -10.78356 -17.26054 1.000 24.48901  ? 136 VAL   A O   1 
ATOM   928  C  CB  . VAL   A 1 129 ? 9.78825   -9.17032  -18.33693 1.000 25.71746  ? 136 VAL   A CB  1 
ATOM   929  C  CG1 . VAL   A 1 129 ? 10.61146  -8.68258  -19.51315 1.000 32.16437  ? 136 VAL   A CG1 1 
ATOM   930  C  CG2 . VAL   A 1 129 ? 10.24189  -8.48523  -17.04921 1.000 26.36712  ? 136 VAL   A CG2 1 
ATOM   931  N  N   . GLY   A 1 130 ? 6.24830   -9.10633  -17.29748 1.000 23.37960  ? 137 GLY   A N   1 
ATOM   932  C  CA  . GLY   A 1 130 ? 5.32160   -9.78459  -16.39946 1.000 22.30342  ? 137 GLY   A CA  1 
ATOM   933  C  C   . GLY   A 1 130 ? 4.84303   -11.13611 -16.89646 1.000 22.31350  ? 137 GLY   A C   1 
ATOM   934  O  O   . GLY   A 1 130 ? 4.50003   -11.98836 -16.07250 1.000 23.99700  ? 137 GLY   A O   1 
ATOM   935  N  N   . PHE   A 1 131 ? 4.84158   -11.36166 -18.21940 1.000 23.67452  ? 138 PHE   A N   1 
ATOM   936  C  CA  . PHE   A 1 131 ? 4.49921   -12.67747 -18.76126 1.000 19.37954  ? 138 PHE   A CA  1 
ATOM   937  C  C   . PHE   A 1 131 ? 5.28691   -13.78294 -18.07400 1.000 22.08024  ? 138 PHE   A C   1 
ATOM   938  O  O   . PHE   A 1 131 ? 4.73370   -14.83688 -17.74658 1.000 22.36627  ? 138 PHE   A O   1 
ATOM   939  C  CB  . PHE   A 1 131 ? 4.76620   -12.72981 -20.26886 1.000 21.17382  ? 138 PHE   A CB  1 
ATOM   940  C  CG  . PHE   A 1 131 ? 4.71989   -14.13095 -20.84484 1.000 22.32275  ? 138 PHE   A CG  1 
ATOM   941  C  CD1 . PHE   A 1 131 ? 3.50205   -14.73348 -21.11623 1.000 23.80913  ? 138 PHE   A CD1 1 
ATOM   942  C  CD2 . PHE   A 1 131 ? 5.88779   -14.82901 -21.12193 1.000 26.85544  ? 138 PHE   A CD2 1 
ATOM   943  C  CE1 . PHE   A 1 131 ? 3.43638   -16.01664 -21.65468 1.000 24.20705  ? 138 PHE   A CE1 1 
ATOM   944  C  CE2 . PHE   A 1 131 ? 5.83292   -16.10970 -21.65761 1.000 26.16073  ? 138 PHE   A CE2 1 
ATOM   945  C  CZ  . PHE   A 1 131 ? 4.60620   -16.70311 -21.92047 1.000 24.74052  ? 138 PHE   A CZ  1 
ATOM   946  N  N   . TYR   A 1 132 ? 6.58118   -13.55624 -17.83748 1.000 22.07774  ? 139 TYR   A N   1 
ATOM   947  C  CA  . TYR   A 1 132 ? 7.39926   -14.63064 -17.28210 1.000 23.00975  ? 139 TYR   A CA  1 
ATOM   948  C  C   . TYR   A 1 132 ? 7.06245   -14.96377 -15.83881 1.000 22.49956  ? 139 TYR   A C   1 
ATOM   949  O  O   . TYR   A 1 132 ? 7.51693   -16.00932 -15.35381 1.000 24.51059  ? 139 TYR   A O   1 
ATOM   950  C  CB  . TYR   A 1 132 ? 8.88555   -14.29188 -17.44757 1.000 22.67269  ? 139 TYR   A CB  1 
ATOM   951  C  CG  . TYR   A 1 132 ? 9.25231   -14.41329 -18.90166 1.000 28.08620  ? 139 TYR   A CG  1 
ATOM   952  C  CD1 . TYR   A 1 132 ? 9.31012   -15.67122 -19.49404 1.000 26.92582  ? 139 TYR   A CD1 1 
ATOM   953  C  CD2 . TYR   A 1 132 ? 9.45235   -13.29221 -19.69883 1.000 31.44693  ? 139 TYR   A CD2 1 
ATOM   954  C  CE1 . TYR   A 1 132 ? 9.59448   -15.82688 -20.84160 1.000 32.35199  ? 139 TYR   A CE1 1 
ATOM   955  C  CE2 . TYR   A 1 132 ? 9.74925   -13.43455 -21.07392 1.000 31.49388  ? 139 TYR   A CE2 1 
ATOM   956  C  CZ  . TYR   A 1 132 ? 9.81787   -14.71156 -21.62230 1.000 34.18973  ? 139 TYR   A CZ  1 
ATOM   957  O  OH  . TYR   A 1 132 ? 10.09982  -14.90803 -22.95422 1.000 43.25621  ? 139 TYR   A OH  1 
ATOM   958  N  N   . SER   A 1 133 ? 6.24557   -14.15167 -15.15601 1.000 20.67755  ? 140 SER   A N   1 
ATOM   959  C  CA  . SER   A 1 133 ? 5.77035   -14.54824 -13.83643 1.000 20.34706  ? 140 SER   A CA  1 
ATOM   960  C  C   . SER   A 1 133 ? 4.90384   -15.79543 -13.89853 1.000 22.28641  ? 140 SER   A C   1 
ATOM   961  O  O   . SER   A 1 133 ? 4.67102   -16.42154 -12.86009 1.000 23.70221  ? 140 SER   A O   1 
ATOM   962  C  CB  . SER   A 1 133 ? 5.00126   -13.39421 -13.18393 1.000 24.02910  ? 140 SER   A CB  1 
ATOM   963  O  OG  . SER   A 1 133 ? 3.76529   -13.18156 -13.84327 1.000 25.72996  ? 140 SER   A OG  1 
ATOM   964  N  N   . ALA   A 1 134 ? 4.46081   -16.18959 -15.10012 1.000 22.94573  ? 141 ALA   A N   1 
ATOM   965  C  CA  . ALA   A 1 134 ? 3.77421   -17.46778 -15.25563 1.000 20.95410  ? 141 ALA   A CA  1 
ATOM   966  C  C   . ALA   A 1 134 ? 4.58883   -18.61749 -14.68373 1.000 21.06430  ? 141 ALA   A C   1 
ATOM   967  O  O   . ALA   A 1 134 ? 4.01485   -19.58519 -14.16361 1.000 22.12756  ? 141 ALA   A O   1 
ATOM   968  C  CB  . ALA   A 1 134 ? 3.48204   -17.73539 -16.73355 1.000 23.17911  ? 141 ALA   A CB  1 
ATOM   969  N  N   . TYR   A 1 135 ? 5.91981   -18.52826 -14.75503 1.000 21.92366  ? 142 TYR   A N   1 
ATOM   970  C  CA  . TYR   A 1 135 ? 6.76139   -19.62112 -14.26156 1.000 20.44406  ? 142 TYR   A CA  1 
ATOM   971  C  C   . TYR   A 1 135 ? 6.85374   -19.66118 -12.73258 1.000 22.77617  ? 142 TYR   A C   1 
ATOM   972  O  O   . TYR   A 1 135 ? 7.49935   -20.56113 -12.17935 1.000 24.94286  ? 142 TYR   A O   1 
ATOM   973  C  CB  . TYR   A 1 135 ? 8.14161   -19.53701 -14.93062 1.000 21.71916  ? 142 TYR   A CB  1 
ATOM   974  C  CG  . TYR   A 1 135 ? 8.01990   -19.92232 -16.40092 1.000 22.90390  ? 142 TYR   A CG  1 
ATOM   975  C  CD1 . TYR   A 1 135 ? 8.04209   -21.25680 -16.79941 1.000 22.39054  ? 142 TYR   A CD1 1 
ATOM   976  C  CD2 . TYR   A 1 135 ? 7.76328   -18.95602 -17.36628 1.000 20.51550  ? 142 TYR   A CD2 1 
ATOM   977  C  CE1 . TYR   A 1 135 ? 7.86960   -21.61139 -18.14899 1.000 21.43122  ? 142 TYR   A CE1 1 
ATOM   978  C  CE2 . TYR   A 1 135 ? 7.59876   -19.30191 -18.71056 1.000 21.59514  ? 142 TYR   A CE2 1 
ATOM   979  C  CZ  . TYR   A 1 135 ? 7.64482   -20.62519 -19.08331 1.000 21.83924  ? 142 TYR   A CZ  1 
ATOM   980  O  OH  . TYR   A 1 135 ? 7.46142   -20.94568 -20.42150 1.000 21.98099  ? 142 TYR   A OH  1 
ATOM   981  N  N   . LEU   A 1 136 ? 6.18467   -18.73876 -12.03367 1.000 22.38875  ? 143 LEU   A N   1 
ATOM   982  C  CA  . LEU   A 1 136 ? 6.01474   -18.90110 -10.59996 1.000 23.88957  ? 143 LEU   A CA  1 
ATOM   983  C  C   . LEU   A 1 136 ? 5.15383   -20.11601 -10.29192 1.000 24.78686  ? 143 LEU   A C   1 
ATOM   984  O  O   . LEU   A 1 136 ? 5.33287   -20.75424 -9.25009  1.000 25.77343  ? 143 LEU   A O   1 
ATOM   985  C  CB  . LEU   A 1 136 ? 5.38115   -17.64351 -10.00804 1.000 24.66774  ? 143 LEU   A CB  1 
ATOM   986  C  CG  . LEU   A 1 136 ? 6.24219   -16.37852 -9.97638  1.000 24.66800  ? 143 LEU   A CG  1 
ATOM   987  C  CD1 . LEU   A 1 136 ? 5.38230   -15.18145 -9.55361  1.000 28.02420  ? 143 LEU   A CD1 1 
ATOM   988  C  CD2 . LEU   A 1 136 ? 7.42468   -16.55666 -9.03529  1.000 25.06984  ? 143 LEU   A CD2 1 
ATOM   989  N  N   . VAL   A 1 137 ? 4.20774   -20.43860 -11.17157 1.000 23.14968  ? 144 VAL   A N   1 
ATOM   990  C  CA  . VAL   A 1 137 ? 3.23248   -21.48668 -10.89642 1.000 22.56324  ? 144 VAL   A CA  1 
ATOM   991  C  C   . VAL   A 1 137 ? 3.20776   -22.57145 -11.96126 1.000 26.00540  ? 144 VAL   A C   1 
ATOM   992  O  O   . VAL   A 1 137 ? 2.63311   -23.63549 -11.70981 1.000 24.65208  ? 144 VAL   A O   1 
ATOM   993  C  CB  . VAL   A 1 137 ? 1.80978   -20.91102 -10.70783 1.000 20.76659  ? 144 VAL   A CB  1 
ATOM   994  C  CG1 . VAL   A 1 137 ? 1.76739   -19.92696 -9.51697  1.000 26.86546  ? 144 VAL   A CG1 1 
ATOM   995  C  CG2 . VAL   A 1 137 ? 1.32398   -20.22583 -11.99484 1.000 20.64293  ? 144 VAL   A CG2 1 
ATOM   996  N  N   . ALA   A 1 138 ? 3.80361   -22.35716 -13.13487 1.000 23.96040  ? 145 ALA   A N   1 
ATOM   997  C  CA  . ALA   A 1 138 ? 3.69510   -23.30126 -14.24051 1.000 23.45794  ? 145 ALA   A CA  1 
ATOM   998  C  C   . ALA   A 1 138 ? 5.04389   -23.94733 -14.51286 1.000 26.26694  ? 145 ALA   A C   1 
ATOM   999  O  O   . ALA   A 1 138 ? 6.07245   -23.26951 -14.51474 1.000 26.84070  ? 145 ALA   A O   1 
ATOM   1000 C  CB  . ALA   A 1 138 ? 3.19865   -22.59799 -15.51114 1.000 21.80897  ? 145 ALA   A CB  1 
ATOM   1001 N  N   . GLU   A 1 139 ? 5.03526   -25.26254 -14.74074 1.000 22.77101  ? 146 GLU   A N   1 
ATOM   1002 C  CA  . GLU   A 1 139 ? 6.25242   -25.92851 -15.18668 1.000 26.20168  ? 146 GLU   A CA  1 
ATOM   1003 C  C   . GLU   A 1 139 ? 6.41642   -25.81978 -16.69620 1.000 26.02433  ? 146 GLU   A C   1 
ATOM   1004 O  O   . GLU   A 1 139 ? 7.53340   -25.94218 -17.20065 1.000 27.26831  ? 146 GLU   A O   1 
ATOM   1005 C  CB  . GLU   A 1 139 ? 6.23109   -27.39134 -14.74893 1.000 31.29237  ? 146 GLU   A CB  1 
ATOM   1006 C  CG  . GLU   A 1 139 ? 5.00712   -28.15392 -15.20950 1.000 35.39627  ? 146 GLU   A CG  1 
ATOM   1007 C  CD  . GLU   A 1 139 ? 4.98856   -29.59519 -14.72089 1.000 64.74527  ? 146 GLU   A CD  1 
ATOM   1008 O  OE1 . GLU   A 1 139 ? 5.78317   -29.93257 -13.81497 1.000 65.75851  ? 146 GLU   A OE1 1 
ATOM   1009 O  OE2 . GLU   A 1 139 ? 4.17710   -30.39065 -15.24443 1.000 63.03927  ? 146 GLU   A OE2 1 
ATOM   1010 N  N   . LYS   A 1 140 ? 5.32167   -25.58480 -17.41325 1.000 24.04817  ? 147 LYS   A N   1 
ATOM   1011 C  CA  . LYS   A 1 140 ? 5.32098   -25.41241 -18.85808 1.000 23.83313  ? 147 LYS   A CA  1 
ATOM   1012 C  C   . LYS   A 1 140 ? 4.26547   -24.37592 -19.18780 1.000 24.27989  ? 147 LYS   A C   1 
ATOM   1013 O  O   . LYS   A 1 140 ? 3.20815   -24.35078 -18.55592 1.000 24.39414  ? 147 LYS   A O   1 
ATOM   1014 C  CB  . LYS   A 1 140 ? 5.01086   -26.72458 -19.58969 1.000 24.91555  ? 147 LYS   A CB  1 
ATOM   1015 C  CG  . LYS   A 1 140 ? 5.01152   -26.59033 -21.11572 1.000 25.29755  ? 147 LYS   A CG  1 
ATOM   1016 C  CD  . LYS   A 1 140 ? 5.04322   -27.96344 -21.76765 1.000 30.17304  ? 147 LYS   A CD  1 
ATOM   1017 C  CE  . LYS   A 1 140 ? 3.65110   -28.50781 -21.95079 1.000 37.48271  ? 147 LYS   A CE  1 
ATOM   1018 N  NZ  . LYS   A 1 140 ? 3.69762   -29.96230 -22.26705 1.000 45.92672  ? 147 LYS   A NZ  1 
ATOM   1019 N  N   . VAL   A 1 141 ? 4.55326   -23.50983 -20.15193 1.000 21.28580  ? 148 VAL   A N   1 
ATOM   1020 C  CA  . VAL   A 1 141 ? 3.57389   -22.53178 -20.61512 1.000 18.34481  ? 148 VAL   A CA  1 
ATOM   1021 C  C   . VAL   A 1 141 ? 3.40586   -22.72298 -22.10767 1.000 22.46246  ? 148 VAL   A C   1 
ATOM   1022 O  O   . VAL   A 1 141 ? 4.39899   -22.83070 -22.83439 1.000 22.80189  ? 148 VAL   A O   1 
ATOM   1023 C  CB  . VAL   A 1 141 ? 3.99650   -21.08686 -20.29839 1.000 21.97471  ? 148 VAL   A CB  1 
ATOM   1024 C  CG1 . VAL   A 1 141 ? 2.97627   -20.09949 -20.87533 1.000 22.39593  ? 148 VAL   A CG1 1 
ATOM   1025 C  CG2 . VAL   A 1 141 ? 4.15402   -20.89489 -18.77242 1.000 22.57146  ? 148 VAL   A CG2 1 
ATOM   1026 N  N   . THR   A 1 142 ? 2.15707   -22.82252 -22.55789 1.000 22.35822  ? 149 THR   A N   1 
ATOM   1027 C  CA  . THR   A 1 142 ? 1.84257   -22.90849 -23.98461 1.000 20.30223  ? 149 THR   A CA  1 
ATOM   1028 C  C   . THR   A 1 142 ? 1.05061   -21.66312 -24.34733 1.000 24.64092  ? 149 THR   A C   1 
ATOM   1029 O  O   . THR   A 1 142 ? 0.13624   -21.27981 -23.61631 1.000 25.61846  ? 149 THR   A O   1 
ATOM   1030 C  CB  . THR   A 1 142 ? 1.03542   -24.17196 -24.31938 1.000 20.67408  ? 149 THR   A CB  1 
ATOM   1031 O  OG1 . THR   A 1 142 ? 1.71321   -25.33721 -23.83082 1.000 26.95585  ? 149 THR   A OG1 1 
ATOM   1032 C  CG2 . THR   A 1 142 ? 0.86151   -24.31579 -25.83871 1.000 28.12737  ? 149 THR   A CG2 1 
ATOM   1033 N  N   . VAL   A 1 143 ? 1.41909   -21.00802 -25.44642 1.000 21.22570  ? 150 VAL   A N   1 
ATOM   1034 C  CA  . VAL   A 1 143 ? 0.74241   -19.78777 -25.88911 1.000 20.96225  ? 150 VAL   A CA  1 
ATOM   1035 C  C   . VAL   A 1 143 ? 0.24078   -20.02824 -27.30526 1.000 24.38327  ? 150 VAL   A C   1 
ATOM   1036 O  O   . VAL   A 1 143 ? 1.04459   -20.26713 -28.21189 1.000 24.18056  ? 150 VAL   A O   1 
ATOM   1037 C  CB  . VAL   A 1 143 ? 1.66740   -18.56169 -25.84683 1.000 22.55686  ? 150 VAL   A CB  1 
ATOM   1038 C  CG1 . VAL   A 1 143 ? 0.92085   -17.34459 -26.38950 1.000 23.91338  ? 150 VAL   A CG1 1 
ATOM   1039 C  CG2 . VAL   A 1 143 ? 2.14452   -18.28035 -24.41576 1.000 24.78005  ? 150 VAL   A CG2 1 
ATOM   1040 N  N   . ILE   A 1 144 ? -1.07987  -20.01101 -27.48620 1.000 23.24516  ? 151 ILE   A N   1 
ATOM   1041 C  CA  . ILE   A 1 144 ? -1.70587  -20.10118 -28.80501 1.000 21.77507  ? 151 ILE   A CA  1 
ATOM   1042 C  C   . ILE   A 1 144 ? -2.12876  -18.69318 -29.17233 1.000 23.30447  ? 151 ILE   A C   1 
ATOM   1043 O  O   . ILE   A 1 144 ? -2.76491  -18.00735 -28.36532 1.000 22.29837  ? 151 ILE   A O   1 
ATOM   1044 C  CB  . ILE   A 1 144 ? -2.92459  -21.04342 -28.80361 1.000 26.93579  ? 151 ILE   A CB  1 
ATOM   1045 C  CG1 . ILE   A 1 144 ? -2.63871  -22.35920 -28.07493 1.000 29.45909  ? 151 ILE   A CG1 1 
ATOM   1046 C  CG2 . ILE   A 1 144 ? -3.39504  -21.30520 -30.23171 1.000 28.54796  ? 151 ILE   A CG2 1 
ATOM   1047 C  CD1 . ILE   A 1 144 ? -1.55726  -23.16578 -28.67672 1.000 30.00586  ? 151 ILE   A CD1 1 
ATOM   1048 N  N   . THR   A 1 145 ? -1.78253  -18.24264 -30.37286 1.000 22.00637  ? 152 THR   A N   1 
ATOM   1049 C  CA  . THR   A 1 145 ? -2.04825  -16.84119 -30.65195 1.000 22.38166  ? 152 THR   A CA  1 
ATOM   1050 C  C   . THR   A 1 145 ? -2.33416  -16.65496 -32.12993 1.000 23.82478  ? 152 THR   A C   1 
ATOM   1051 O  O   . THR   A 1 145 ? -1.81659  -17.38488 -32.98313 1.000 24.52020  ? 152 THR   A O   1 
ATOM   1052 C  CB  . THR   A 1 145 ? -0.87603  -15.96108 -30.19523 1.000 24.06039  ? 152 THR   A CB  1 
ATOM   1053 O  OG1 . THR   A 1 145 ? -1.24778  -14.57743 -30.25969 1.000 23.39438  ? 152 THR   A OG1 1 
ATOM   1054 C  CG2 . THR   A 1 145 ? 0.34907   -16.20326 -31.05665 1.000 25.66110  ? 152 THR   A CG2 1 
ATOM   1055 N  N   . LYS   A 1 146 ? -3.17072  -15.66638 -32.42347 1.000 22.41788  ? 153 LYS   A N   1 
ATOM   1056 C  CA  . LYS   A 1 146 ? -3.57703  -15.38831 -33.79686 1.000 23.94028  ? 153 LYS   A CA  1 
ATOM   1057 C  C   . LYS   A 1 146 ? -3.73012  -13.88379 -33.93283 1.000 26.44043  ? 153 LYS   A C   1 
ATOM   1058 O  O   . LYS   A 1 146 ? -4.58921  -13.28644 -33.27497 1.000 23.76687  ? 153 LYS   A O   1 
ATOM   1059 C  CB  . LYS   A 1 146 ? -4.88276  -16.10588 -34.14449 1.000 25.15599  ? 153 LYS   A CB  1 
ATOM   1060 C  CG  . LYS   A 1 146 ? -5.47444  -15.73739 -35.50956 1.000 27.05707  ? 153 LYS   A CG  1 
ATOM   1061 C  CD  . LYS   A 1 146 ? -4.60696  -16.24721 -36.66834 1.000 26.93977  ? 153 LYS   A CD  1 
ATOM   1062 C  CE  . LYS   A 1 146 ? -5.28933  -15.99799 -38.00882 1.000 31.67864  ? 153 LYS   A CE  1 
ATOM   1063 N  NZ  . LYS   A 1 146 ? -5.31414  -14.55027 -38.39737 1.000 31.03911  ? 153 LYS   A NZ  1 
ATOM   1064 N  N   . HIS   A 1 147 ? -2.87979  -13.29120 -34.76457 1.000 26.59258  ? 154 HIS   A N   1 
ATOM   1065 C  CA  . HIS   A 1 147 ? -2.92458  -11.89759 -35.17738 1.000 26.06280  ? 154 HIS   A CA  1 
ATOM   1066 C  C   . HIS   A 1 147 ? -3.55395  -11.82075 -36.56455 1.000 28.83486  ? 154 HIS   A C   1 
ATOM   1067 O  O   . HIS   A 1 147 ? -3.37449  -12.72013 -37.39436 1.000 30.95922  ? 154 HIS   A O   1 
ATOM   1068 C  CB  . HIS   A 1 147 ? -1.49827  -11.33689 -35.20023 1.000 28.75947  ? 154 HIS   A CB  1 
ATOM   1069 C  CG  . HIS   A 1 147 ? -1.40305  -9.85852  -35.42231 1.000 31.58217  ? 154 HIS   A CG  1 
ATOM   1070 N  ND1 . HIS   A 1 147 ? -1.51907  -9.26962  -36.66350 1.000 30.95915  ? 154 HIS   A ND1 1 
ATOM   1071 C  CD2 . HIS   A 1 147 ? -1.11687  -8.85664  -34.55518 1.000 29.67126  ? 154 HIS   A CD2 1 
ATOM   1072 C  CE1 . HIS   A 1 147 ? -1.35153  -7.96299  -36.54635 1.000 35.31308  ? 154 HIS   A CE1 1 
ATOM   1073 N  NE2 . HIS   A 1 147 ? -1.10708  -7.68761  -35.27436 1.000 28.35154  ? 154 HIS   A NE2 1 
ATOM   1074 N  N   . ASN   A 1 148 ? -4.29433  -10.73171 -36.82173 1.000 27.44436  ? 155 ASN   A N   1 
ATOM   1075 C  CA  . ASN   A 1 148 ? -4.97023  -10.57083 -38.10749 1.000 27.47773  ? 155 ASN   A CA  1 
ATOM   1076 C  C   . ASN   A 1 148 ? -4.02237  -10.70395 -39.29748 1.000 32.69386  ? 155 ASN   A C   1 
ATOM   1077 O  O   . ASN   A 1 148 ? -4.45451  -11.06659 -40.39448 1.000 32.49174  ? 155 ASN   A O   1 
ATOM   1078 C  CB  . ASN   A 1 148 ? -5.65735  -9.20389  -38.20443 1.000 30.47873  ? 155 ASN   A CB  1 
ATOM   1079 C  CG  . ASN   A 1 148 ? -6.95836  -9.13271  -37.42796 1.000 34.11622  ? 155 ASN   A CG  1 
ATOM   1080 O  OD1 . ASN   A 1 148 ? -7.64398  -10.13627 -37.23998 1.000 35.86215  ? 155 ASN   A OD1 1 
ATOM   1081 N  ND2 . ASN   A 1 148 ? -7.33720  -7.91779  -37.02421 1.000 32.03636  ? 155 ASN   A ND2 1 
ATOM   1082 N  N   . ASP   A 1 149 ? -2.74302  -10.38914 -39.11525 1.000 30.77641  ? 156 ASP   A N   1 
ATOM   1083 C  CA  . ASP   A 1 149 ? -1.80271  -10.33783 -40.22529 1.000 37.49405  ? 156 ASP   A CA  1 
ATOM   1084 C  C   . ASP   A 1 149 ? -0.94356  -11.59321 -40.34814 1.000 38.61125  ? 156 ASP   A C   1 
ATOM   1085 O  O   . ASP   A 1 149 ? -0.02384  -11.61765 -41.16775 1.000 38.06142  ? 156 ASP   A O   1 
ATOM   1086 C  CB  . ASP   A 1 149 ? -0.91436  -9.09781  -40.08867 1.000 39.60917  ? 156 ASP   A CB  1 
ATOM   1087 C  CG  . ASP   A 1 149 ? -1.69269  -7.79227  -40.25423 1.000 46.93339  ? 156 ASP   A CG  1 
ATOM   1088 O  OD1 . ASP   A 1 149 ? -2.82871  -7.81321  -40.79048 1.000 44.00533  ? 156 ASP   A OD1 1 
ATOM   1089 O  OD2 . ASP   A 1 149 ? -1.16560  -6.74189  -39.82932 1.000 50.17352  ? 156 ASP   A OD2 1 
ATOM   1090 N  N   . ASP   A 1 150 ? -1.22851  -12.64114 -39.58210 1.000 31.72367  ? 157 ASP   A N   1 
ATOM   1091 C  CA  . ASP   A 1 150 ? -0.37493  -13.82485 -39.57744 1.000 30.77320  ? 157 ASP   A CA  1 
ATOM   1092 C  C   . ASP   A 1 150 ? -1.23307  -15.05279 -39.29379 1.000 39.95669  ? 157 ASP   A C   1 
ATOM   1093 O  O   . ASP   A 1 150 ? -2.44492  -14.95515 -39.08524 1.000 32.65739  ? 157 ASP   A O   1 
ATOM   1094 C  CB  . ASP   A 1 150 ? 0.76503   -13.67653 -38.56173 1.000 29.91867  ? 157 ASP   A CB  1 
ATOM   1095 C  CG  . ASP   A 1 150 ? 2.02612   -14.43146 -38.97361 1.000 37.96857  ? 157 ASP   A CG  1 
ATOM   1096 O  OD1 . ASP   A 1 150 ? 1.92674   -15.32565 -39.84239 1.000 34.85856  ? 157 ASP   A OD1 1 
ATOM   1097 O  OD2 . ASP   A 1 150 ? 3.11957   -14.13329 -38.43333 1.000 34.49211  ? 157 ASP   A OD2 1 
ATOM   1098 N  N   . GLU   A 1 151 ? -0.58676  -16.21656 -39.29268 1.000 32.89158  ? 158 GLU   A N   1 
ATOM   1099 C  CA  . GLU   A 1 151 ? -1.23182  -17.50056 -39.06323 1.000 35.29203  ? 158 GLU   A CA  1 
ATOM   1100 C  C   . GLU   A 1 151 ? -1.37360  -17.75668 -37.56351 1.000 33.51443  ? 158 GLU   A C   1 
ATOM   1101 O  O   . GLU   A 1 151 ? -0.80288  -17.04803 -36.72867 1.000 31.08600  ? 158 GLU   A O   1 
ATOM   1102 C  CB  . GLU   A 1 151 ? -0.40979  -18.62127 -39.70438 1.000 36.58292  ? 158 GLU   A CB  1 
ATOM   1103 C  CG  . GLU   A 1 151 ? -0.38007  -18.57081 -41.22198 1.000 51.46255  ? 158 GLU   A CG  1 
ATOM   1104 C  CD  . GLU   A 1 151 ? -1.76102  -18.56440 -41.83736 1.000 77.27308  ? 158 GLU   A CD  1 
ATOM   1105 O  OE1 . GLU   A 1 151 ? -2.17819  -17.50175 -42.35152 1.000 92.17622  ? 158 GLU   A OE1 1 
ATOM   1106 O  OE2 . GLU   A 1 151 ? -2.43218  -19.61621 -41.79888 1.000 84.67684  ? 158 GLU   A OE2 1 
ATOM   1107 N  N   . GLN   A 1 152 ? -2.11499  -18.80494 -37.21115 1.000 25.76418  ? 159 GLN   A N   1 
ATOM   1108 C  CA  . GLN   A 1 152 ? -2.21490  -19.18494 -35.80366 1.000 26.16608  ? 159 GLN   A CA  1 
ATOM   1109 C  C   . GLN   A 1 152 ? -0.96999  -19.97958 -35.42078 1.000 27.93024  ? 159 GLN   A C   1 
ATOM   1110 O  O   . GLN   A 1 152 ? -0.59951  -20.93057 -36.12229 1.000 31.60095  ? 159 GLN   A O   1 
ATOM   1111 C  CB  . GLN   A 1 152 ? -3.48052  -20.01244 -35.55709 1.000 29.17766  ? 159 GLN   A CB  1 
ATOM   1112 C  CG  . GLN   A 1 152 ? -3.80112  -20.24620 -34.07842 1.000 28.63685  ? 159 GLN   A CG  1 
ATOM   1113 C  CD  . GLN   A 1 152 ? -5.23769  -20.71292 -33.88115 1.000 33.33206  ? 159 GLN   A CD  1 
ATOM   1114 O  OE1 . GLN   A 1 152 ? -6.18235  -20.02214 -34.27162 1.000 32.88501  ? 159 GLN   A OE1 1 
ATOM   1115 N  NE2 . GLN   A 1 152 ? -5.40886  -21.87368 -33.25887 1.000 30.61567  ? 159 GLN   A NE2 1 
ATOM   1116 N  N   . TYR   A 1 153 ? -0.32041  -19.58860 -34.32192 1.000 23.56600  ? 160 TYR   A N   1 
ATOM   1117 C  CA  . TYR   A 1 153 ? 0.90708   -20.22390 -33.85449 1.000 25.60311  ? 160 TYR   A CA  1 
ATOM   1118 C  C   . TYR   A 1 153 ? 0.75361   -20.73729 -32.43224 1.000 26.50987  ? 160 TYR   A C   1 
ATOM   1119 O  O   . TYR   A 1 153 ? -0.00983  -20.18816 -31.62938 1.000 24.42405  ? 160 TYR   A O   1 
ATOM   1120 C  CB  . TYR   A 1 153 ? 2.08572   -19.24146 -33.85967 1.000 24.89959  ? 160 TYR   A CB  1 
ATOM   1121 C  CG  . TYR   A 1 153 ? 2.50161   -18.89930 -35.24325 1.000 30.11718  ? 160 TYR   A CG  1 
ATOM   1122 C  CD1 . TYR   A 1 153 ? 3.29431   -19.76230 -35.98553 1.000 26.93124  ? 160 TYR   A CD1 1 
ATOM   1123 C  CD2 . TYR   A 1 153 ? 2.05963   -17.72433 -35.83532 1.000 36.42301  ? 160 TYR   A CD2 1 
ATOM   1124 C  CE1 . TYR   A 1 153 ? 3.65590   -19.44835 -37.28370 1.000 30.68311  ? 160 TYR   A CE1 1 
ATOM   1125 C  CE2 . TYR   A 1 153 ? 2.40590   -17.40404 -37.11656 1.000 35.03532  ? 160 TYR   A CE2 1 
ATOM   1126 C  CZ  . TYR   A 1 153 ? 3.19766   -18.25747 -37.83875 1.000 35.18028  ? 160 TYR   A CZ  1 
ATOM   1127 O  OH  . TYR   A 1 153 ? 3.53158   -17.90064 -39.12487 1.000 47.13640  ? 160 TYR   A OH  1 
ATOM   1128 N  N   . ALA   A 1 154 ? 1.55055   -21.75463 -32.11009 1.000 23.99050  ? 161 ALA   A N   1 
ATOM   1129 C  CA  . ALA   A 1 154 ? 1.71955   -22.23505 -30.74442 1.000 24.94600  ? 161 ALA   A CA  1 
ATOM   1130 C  C   . ALA   A 1 154 ? 3.17000   -22.03831 -30.34192 1.000 24.84043  ? 161 ALA   A C   1 
ATOM   1131 O  O   . ALA   A 1 154 ? 4.07832   -22.55579 -31.00882 1.000 25.86691  ? 161 ALA   A O   1 
ATOM   1132 C  CB  . ALA   A 1 154 ? 1.33630   -23.70804 -30.62134 1.000 26.63285  ? 161 ALA   A CB  1 
ATOM   1133 N  N   . TRP   A 1 155 ? 3.37182   -21.28386 -29.26859 1.000 22.14438  ? 162 TRP   A N   1 
ATOM   1134 C  CA  . TRP   A 1 155 ? 4.65928   -21.08646 -28.60518 1.000 21.64979  ? 162 TRP   A CA  1 
ATOM   1135 C  C   . TRP   A 1 155 ? 4.66614   -21.92736 -27.34337 1.000 25.00647  ? 162 TRP   A C   1 
ATOM   1136 O  O   . TRP   A 1 155 ? 3.64078   -22.03180 -26.66482 1.000 23.34024  ? 162 TRP   A O   1 
ATOM   1137 C  CB  . TRP   A 1 155 ? 4.80912   -19.60490 -28.24952 1.000 21.57937  ? 162 TRP   A CB  1 
ATOM   1138 C  CG  . TRP   A 1 155 ? 6.03677   -19.15531 -27.50971 1.000 22.79140  ? 162 TRP   A CG  1 
ATOM   1139 C  CD1 . TRP   A 1 155 ? 7.10019   -18.47451 -28.03369 1.000 23.95531  ? 162 TRP   A CD1 1 
ATOM   1140 C  CD2 . TRP   A 1 155 ? 6.28149   -19.27007 -26.10640 1.000 22.29342  ? 162 TRP   A CD2 1 
ATOM   1141 N  NE1 . TRP   A 1 155 ? 8.00443   -18.17040 -27.03362 1.000 23.88569  ? 162 TRP   A NE1 1 
ATOM   1142 C  CE2 . TRP   A 1 155 ? 7.52145   -18.64788 -25.84462 1.000 22.95773  ? 162 TRP   A CE2 1 
ATOM   1143 C  CE3 . TRP   A 1 155 ? 5.56715   -19.83741 -25.03483 1.000 23.90524  ? 162 TRP   A CE3 1 
ATOM   1144 C  CZ2 . TRP   A 1 155 ? 8.07394   -18.59100 -24.56835 1.000 26.81171  ? 162 TRP   A CZ2 1 
ATOM   1145 C  CZ3 . TRP   A 1 155 ? 6.12494   -19.78445 -23.76249 1.000 21.88393  ? 162 TRP   A CZ3 1 
ATOM   1146 C  CH2 . TRP   A 1 155 ? 7.36316   -19.15826 -23.54051 1.000 23.95502  ? 162 TRP   A CH2 1 
ATOM   1147 N  N   . GLU   A 1 156 ? 5.80477   -22.52804 -27.00909 1.000 22.76408  ? 163 GLU   A N   1 
ATOM   1148 C  CA  . GLU   A 1 156 ? 5.79264   -23.32104 -25.79063 1.000 19.90669  ? 163 GLU   A CA  1 
ATOM   1149 C  C   . GLU   A 1 156 ? 7.17714   -23.35528 -25.16791 1.000 20.79338  ? 163 GLU   A C   1 
ATOM   1150 O  O   . GLU   A 1 156 ? 8.17932   -23.42546 -25.88227 1.000 23.50811  ? 163 GLU   A O   1 
ATOM   1151 C  CB  . GLU   A 1 156 ? 5.29376   -24.72655 -26.11640 1.000 26.38230  ? 163 GLU   A CB  1 
ATOM   1152 C  CG  . GLU   A 1 156 ? 5.24172   -25.68677 -24.95649 1.000 32.59454  ? 163 GLU   A CG  1 
ATOM   1153 C  CD  . GLU   A 1 156 ? 4.49502   -26.95152 -25.34720 1.000 43.37065  ? 163 GLU   A CD  1 
ATOM   1154 O  OE1 . GLU   A 1 156 ? 5.15667   -27.87574 -25.85940 1.000 37.47477  ? 163 GLU   A OE1 1 
ATOM   1155 O  OE2 . GLU   A 1 156 ? 3.25360   -27.01994 -25.16231 1.000 36.32149  ? 163 GLU   A OE2 1 
ATOM   1156 N  N   . SER   A 1 157 ? 7.23300   -23.29551 -23.83743 1.000 20.98450  ? 164 SER   A N   1 
ATOM   1157 C  CA  . SER   A 1 157 ? 8.52699   -23.45991 -23.18139 1.000 20.78021  ? 164 SER   A CA  1 
ATOM   1158 C  C   . SER   A 1 157 ? 8.35281   -24.04054 -21.78889 1.000 22.59788  ? 164 SER   A C   1 
ATOM   1159 O  O   . SER   A 1 157 ? 7.45230   -23.63897 -21.04251 1.000 24.28480  ? 164 SER   A O   1 
ATOM   1160 C  CB  . SER   A 1 157 ? 9.28921   -22.13340 -23.08195 1.000 21.31174  ? 164 SER   A CB  1 
ATOM   1161 O  OG  . SER   A 1 157 ? 10.52395  -22.34660 -22.41603 1.000 23.80395  ? 164 SER   A OG  1 
ATOM   1162 N  N   . SER   A 1 158 ? 9.22103   -24.99717 -21.45074 1.000 24.08364  ? 165 SER   A N   1 
ATOM   1163 C  CA  . SER   A 1 158 ? 9.39794   -25.43146 -20.06892 1.000 27.12689  ? 165 SER   A CA  1 
ATOM   1164 C  C   . SER   A 1 158 ? 10.67103  -24.85510 -19.46122 1.000 27.88949  ? 165 SER   A C   1 
ATOM   1165 O  O   . SER   A 1 158 ? 11.27097  -25.46780 -18.56837 1.000 29.27087  ? 165 SER   A O   1 
ATOM   1166 C  CB  . SER   A 1 158 ? 9.40983   -26.95581 -19.96375 1.000 29.74235  ? 165 SER   A CB  1 
ATOM   1167 O  OG  . SER   A 1 158 ? 8.25159   -27.53139 -20.55655 1.000 30.58039  ? 165 SER   A OG  1 
ATOM   1168 N  N   . ALA   A 1 159 ? 11.07919  -23.67994 -19.92540 1.000 24.25906  ? 166 ALA   A N   1 
ATOM   1169 C  CA  . ALA   A 1 159 ? 12.32944  -23.02875 -19.51056 1.000 24.97308  ? 166 ALA   A CA  1 
ATOM   1170 C  C   . ALA   A 1 159 ? 13.48874  -23.94221 -19.91597 1.000 27.91566  ? 166 ALA   A C   1 
ATOM   1171 O  O   . ALA   A 1 159 ? 13.44662  -24.60941 -20.96064 1.000 30.39498  ? 166 ALA   A O   1 
ATOM   1172 C  CB  . ALA   A 1 159 ? 12.28318  -22.66018 -18.02955 1.000 28.66142  ? 166 ALA   A CB  1 
ATOM   1173 N  N   . GLY   A 1 160 ? 14.55481  -23.96339 -19.12508 1.000 30.04859  ? 167 GLY   A N   1 
ATOM   1174 C  CA  . GLY   A 1 160 ? 15.71846  -24.68868 -19.56937 1.000 30.94372  ? 167 GLY   A CA  1 
ATOM   1175 C  C   . GLY   A 1 160 ? 16.44557  -24.07348 -20.74215 1.000 28.13524  ? 167 GLY   A C   1 
ATOM   1176 O  O   . GLY   A 1 160 ? 17.33853  -24.72211 -21.29550 1.000 34.26840  ? 167 GLY   A O   1 
ATOM   1177 N  N   . GLY   A 1 161 ? 16.08011  -22.85161 -21.14831 1.000 26.95420  ? 168 GLY   A N   1 
ATOM   1178 C  CA  . GLY   A 1 161 ? 16.85251  -22.09976 -22.11833 1.000 30.79496  ? 168 GLY   A CA  1 
ATOM   1179 C  C   . GLY   A 1 161 ? 16.34151  -22.13060 -23.54148 1.000 27.47660  ? 168 GLY   A C   1 
ATOM   1180 O  O   . GLY   A 1 161 ? 16.99008  -21.55283 -24.42583 1.000 29.14588  ? 168 GLY   A O   1 
ATOM   1181 N  N   . SER   A 1 162 ? 15.21967  -22.79611 -23.80127 1.000 25.80617  ? 169 SER   A N   1 
ATOM   1182 C  CA  . SER   A 1 162 ? 14.73553  -22.94029 -25.16677 1.000 23.23360  ? 169 SER   A CA  1 
ATOM   1183 C  C   . SER   A 1 162 ? 13.22113  -22.87147 -25.17870 1.000 22.81209  ? 169 SER   A C   1 
ATOM   1184 O  O   . SER   A 1 162 ? 12.55583  -23.11545 -24.17140 1.000 24.32754  ? 169 SER   A O   1 
ATOM   1185 C  CB  . SER   A 1 162 ? 15.22542  -24.25018 -25.80022 1.000 28.01643  ? 169 SER   A CB  1 
ATOM   1186 O  OG  . SER   A 1 162 ? 14.58262  -25.37425 -25.23243 1.000 30.88884  ? 169 SER   A OG  1 
ATOM   1187 N  N   . PHE   A 1 163 ? 12.69365  -22.50699 -26.34035 1.000 21.95363  ? 170 PHE   A N   1 
ATOM   1188 C  CA  . PHE   A 1 163 ? 11.25963  -22.50568 -26.58087 1.000 24.68806  ? 170 PHE   A CA  1 
ATOM   1189 C  C   . PHE   A 1 163 ? 11.02071  -22.99790 -27.99846 1.000 22.31817  ? 170 PHE   A C   1 
ATOM   1190 O  O   . PHE   A 1 163 ? 11.93126  -23.02671 -28.82704 1.000 23.93846  ? 170 PHE   A O   1 
ATOM   1191 C  CB  . PHE   A 1 163 ? 10.63013  -21.12055 -26.36149 1.000 23.59752  ? 170 PHE   A CB  1 
ATOM   1192 C  CG  . PHE   A 1 163 ? 11.11856  -20.04915 -27.31230 1.000 24.48228  ? 170 PHE   A CG  1 
ATOM   1193 C  CD1 . PHE   A 1 163 ? 12.24758  -19.30536 -27.01180 1.000 26.22712  ? 170 PHE   A CD1 1 
ATOM   1194 C  CD2 . PHE   A 1 163 ? 10.43894  -19.77304 -28.50161 1.000 22.16508  ? 170 PHE   A CD2 1 
ATOM   1195 C  CE1 . PHE   A 1 163 ? 12.69424  -18.30416 -27.85634 1.000 27.34971  ? 170 PHE   A CE1 1 
ATOM   1196 C  CE2 . PHE   A 1 163 ? 10.88841  -18.77147 -29.36156 1.000 23.86864  ? 170 PHE   A CE2 1 
ATOM   1197 C  CZ  . PHE   A 1 163 ? 12.00972  -18.02925 -29.03677 1.000 28.50624  ? 170 PHE   A CZ  1 
ATOM   1198 N  N   . THR   A 1 164 ? 9.78857   -23.41896 -28.26363 1.000 23.22501  ? 171 THR   A N   1 
ATOM   1199 C  CA  . THR   A 1 164 ? 9.42780   -23.87163 -29.59606 1.000 22.83773  ? 171 THR   A CA  1 
ATOM   1200 C  C   . THR   A 1 164 ? 8.30827   -23.01041 -30.15657 1.000 22.15742  ? 171 THR   A C   1 
ATOM   1201 O  O   . THR   A 1 164 ? 7.50042   -22.44117 -29.41194 1.000 22.24329  ? 171 THR   A O   1 
ATOM   1202 C  CB  . THR   A 1 164 ? 8.98685   -25.34215 -29.62330 1.000 28.20135  ? 171 THR   A CB  1 
ATOM   1203 O  OG1 . THR   A 1 164 ? 7.81226   -25.51529 -28.81555 1.000 26.56522  ? 171 THR   A OG1 1 
ATOM   1204 C  CG2 . THR   A 1 164 ? 10.09732  -26.27673 -29.15301 1.000 30.44994  ? 171 THR   A CG2 1 
ATOM   1205 N  N   . VAL   A 1 165 ? 8.25942   -22.94589 -31.48668 1.000 23.66016  ? 172 VAL   A N   1 
ATOM   1206 C  CA  . VAL   A 1 165 ? 7.15272   -22.32578 -32.20798 1.000 26.18874  ? 172 VAL   A CA  1 
ATOM   1207 C  C   . VAL   A 1 165 ? 6.74247   -23.26173 -33.33282 1.000 24.98952  ? 172 VAL   A C   1 
ATOM   1208 O  O   . VAL   A 1 165 ? 7.59419   -23.77130 -34.07419 1.000 25.97917  ? 172 VAL   A O   1 
ATOM   1209 C  CB  . VAL   A 1 165 ? 7.53359   -20.93301 -32.74878 1.000 24.90473  ? 172 VAL   A CB  1 
ATOM   1210 C  CG1 . VAL   A 1 165 ? 6.36843   -20.32387 -33.51935 1.000 28.79083  ? 172 VAL   A CG1 1 
ATOM   1211 C  CG2 . VAL   A 1 165 ? 7.88734   -20.04149 -31.59702 1.000 25.00264  ? 172 VAL   A CG2 1 
ATOM   1212 N  N   . ARG   A 1 166 ? 5.44271   -23.51789 -33.44300 1.000 26.94208  ? 173 ARG   A N   1 
ATOM   1213 C  CA  . ARG   A 1 166 ? 4.92597   -24.29252 -34.55782 1.000 27.96038  ? 173 ARG   A CA  1 
ATOM   1214 C  C   . ARG   A 1 166 ? 3.62421   -23.65291 -35.01953 1.000 29.33848  ? 173 ARG   A C   1 
ATOM   1215 O  O   . ARG   A 1 166 ? 2.96172   -22.94383 -34.25826 1.000 28.67424  ? 173 ARG   A O   1 
ATOM   1216 C  CB  . ARG   A 1 166 ? 4.68636   -25.76289 -34.17585 1.000 37.80839  ? 173 ARG   A CB  1 
ATOM   1217 C  CG  . ARG   A 1 166 ? 3.52471   -25.97946 -33.20147 1.000 32.93516  ? 173 ARG   A CG  1 
ATOM   1218 C  CD  . ARG   A 1 166 ? 3.67661   -27.26538 -32.38992 1.000 47.25560  ? 173 ARG   A CD  1 
ATOM   1219 N  NE  . ARG   A 1 166 ? 4.85584   -27.24573 -31.52628 1.000 52.26142  ? 173 ARG   A NE  1 
ATOM   1220 C  CZ  . ARG   A 1 166 ? 5.34337   -28.30452 -30.89017 1.000 60.73690  ? 173 ARG   A CZ  1 
ATOM   1221 N  NH1 . ARG   A 1 166 ? 4.81269   -29.50785 -31.03959 1.000 58.42609  ? 173 ARG   A NH1 1 
ATOM   1222 N  NH2 . ARG   A 1 166 ? 6.39367   -28.15401 -30.08687 1.000 56.63709  ? 173 ARG   A NH2 1 
ATOM   1223 N  N   . THR   A 1 167 ? 3.27938   -23.88225 -36.28784 1.000 31.78443  ? 174 THR   A N   1 
ATOM   1224 C  CA  . THR   A 1 167 ? 1.93926   -23.52727 -36.74063 1.000 30.38693  ? 174 THR   A CA  1 
ATOM   1225 C  C   . THR   A 1 167 ? 0.92096   -24.39123 -36.01048 1.000 38.67986  ? 174 THR   A C   1 
ATOM   1226 O  O   . THR   A 1 167 ? 1.11961   -25.59750 -35.85280 1.000 41.51277  ? 174 THR   A O   1 
ATOM   1227 C  CB  . THR   A 1 167 ? 1.83290   -23.70500 -38.25206 1.000 43.99256  ? 174 THR   A CB  1 
ATOM   1228 O  OG1 . THR   A 1 167 ? 2.76827   -22.82275 -38.88438 1.000 41.57103  ? 174 THR   A OG1 1 
ATOM   1229 C  CG2 . THR   A 1 167 ? 0.43102   -23.39134 -38.73460 1.000 45.12031  ? 174 THR   A CG2 1 
ATOM   1230 N  N   . ASP   A 1 168 ? -0.15633  -23.77310 -35.52446 1.000 33.51294  ? 175 ASP   A N   1 
ATOM   1231 C  CA  . ASP   A 1 168 ? -1.11513  -24.49422 -34.69843 1.000 39.10562  ? 175 ASP   A CA  1 
ATOM   1232 C  C   . ASP   A 1 168 ? -2.23222  -25.03667 -35.57101 1.000 46.06171  ? 175 ASP   A C   1 
ATOM   1233 O  O   . ASP   A 1 168 ? -2.87165  -24.27786 -36.30700 1.000 46.91655  ? 175 ASP   A O   1 
ATOM   1234 C  CB  . ASP   A 1 168 ? -1.71485  -23.60538 -33.61397 1.000 32.37033  ? 175 ASP   A CB  1 
ATOM   1235 C  CG  . ASP   A 1 168 ? -2.62599  -24.38235 -32.66672 1.000 49.99198  ? 175 ASP   A CG  1 
ATOM   1236 O  OD1 . ASP   A 1 168 ? -2.27027  -25.52411 -32.29875 1.000 60.29010  ? 175 ASP   A OD1 1 
ATOM   1237 O  OD2 . ASP   A 1 168 ? -3.70380  -23.86582 -32.30195 1.000 44.73766  ? 175 ASP   A OD2 1 
ATOM   1238 N  N   . THR   A 1 169 ? -2.47709  -26.33954 -35.46486 1.000 50.43816  ? 176 THR   A N   1 
ATOM   1239 C  CA  . THR   A 1 169 ? -3.57489  -26.99189 -36.16265 1.000 68.30014  ? 176 THR   A CA  1 
ATOM   1240 C  C   . THR   A 1 169 ? -4.78764  -27.21130 -35.26252 1.000 70.48196  ? 176 THR   A C   1 
ATOM   1241 O  O   . THR   A 1 169 ? -5.76009  -27.84315 -35.69050 1.000 64.33851  ? 176 THR   A O   1 
ATOM   1242 C  CB  . THR   A 1 169 ? -3.10158  -28.32044 -36.75786 1.000 67.60473  ? 176 THR   A CB  1 
ATOM   1243 O  OG1 . THR   A 1 169 ? -2.25366  -28.99218 -35.81546 1.000 68.24504  ? 176 THR   A OG1 1 
ATOM   1244 C  CG2 . THR   A 1 169 ? -2.33031  -28.07155 -38.05216 1.000 56.42026  ? 176 THR   A CG2 1 
ATOM   1245 N  N   . GLY   A 1 170 ? -4.75611  -26.69416 -34.03747 1.000 64.20291  ? 177 GLY   A N   1 
ATOM   1246 C  CA  . GLY   A 1 170 ? -5.87503  -26.80308 -33.12813 1.000 57.02099  ? 177 GLY   A CA  1 
ATOM   1247 C  C   . GLY   A 1 170 ? -7.08761  -26.01651 -33.60855 1.000 58.91031  ? 177 GLY   A C   1 
ATOM   1248 O  O   . GLY   A 1 170 ? -7.16825  -25.53702 -34.74017 1.000 58.02443  ? 177 GLY   A O   1 
ATOM   1249 N  N   . GLU   A 1 171 ? -8.05335  -25.89297 -32.70559 1.000 57.89594  ? 178 GLU   A N   1 
ATOM   1250 C  CA  . GLU   A 1 171 ? -9.28003  -25.16424 -33.00043 1.000 55.77142  ? 178 GLU   A CA  1 
ATOM   1251 C  C   . GLU   A 1 171 ? -8.94339  -23.71306 -33.35300 1.000 44.39114  ? 178 GLU   A C   1 
ATOM   1252 O  O   . GLU   A 1 171 ? -8.21198  -23.05224 -32.59935 1.000 43.96920  ? 178 GLU   A O   1 
ATOM   1253 C  CB  . GLU   A 1 171 ? -10.20905 -25.22887 -31.78242 1.000 57.17786  ? 178 GLU   A CB  1 
ATOM   1254 C  CG  . GLU   A 1 171 ? -11.59889 -24.61017 -31.94169 1.000 61.35932  ? 178 GLU   A CG  1 
ATOM   1255 C  CD  . GLU   A 1 171 ? -12.60286 -25.55230 -32.61231 1.000 67.68189  ? 178 GLU   A CD  1 
ATOM   1256 O  OE1 . GLU   A 1 171 ? -12.75221 -26.70405 -32.14104 1.000 57.47185  ? 178 GLU   A OE1 1 
ATOM   1257 O  OE2 . GLU   A 1 171 ? -13.26097 -25.13955 -33.59462 1.000 55.35772  ? 178 GLU   A OE2 1 
ATOM   1258 N  N   . PRO   A 1 172 ? -9.41710  -23.19815 -34.48853 1.000 42.98175  ? 179 PRO   A N   1 
ATOM   1259 C  CA  . PRO   A 1 172 ? -9.13378  -21.80054 -34.85378 1.000 43.92538  ? 179 PRO   A CA  1 
ATOM   1260 C  C   . PRO   A 1 172 ? -9.71005  -20.82525 -33.83310 1.000 43.55313  ? 179 PRO   A C   1 
ATOM   1261 O  O   . PRO   A 1 172 ? -10.86859 -20.94126 -33.42797 1.000 44.64042  ? 179 PRO   A O   1 
ATOM   1262 C  CB  . PRO   A 1 172 ? -9.81407  -21.65263 -36.22051 1.000 44.00726  ? 179 PRO   A CB  1 
ATOM   1263 C  CG  . PRO   A 1 172 ? -9.86156  -23.04859 -36.76402 1.000 42.16457  ? 179 PRO   A CG  1 
ATOM   1264 C  CD  . PRO   A 1 172 ? -10.11821 -23.91580 -35.56497 1.000 48.52941  ? 179 PRO   A CD  1 
ATOM   1265 N  N   . MET   A 1 173 ? -8.89404  -19.84447 -33.43047 1.000 36.37150  ? 180 MET   A N   1 
ATOM   1266 C  CA  . MET   A 1 173 ? -9.29679  -18.87085 -32.42061 1.000 33.05809  ? 180 MET   A CA  1 
ATOM   1267 C  C   . MET   A 1 173 ? -9.90242  -17.59962 -32.99049 1.000 45.91661  ? 180 MET   A C   1 
ATOM   1268 O  O   . MET   A 1 173 ? -10.45425 -16.80304 -32.22285 1.000 40.49285  ? 180 MET   A O   1 
ATOM   1269 C  CB  . MET   A 1 173 ? -8.11005  -18.41782 -31.57406 1.000 32.36072  ? 180 MET   A CB  1 
ATOM   1270 C  CG  . MET   A 1 173 ? -7.32792  -19.49580 -30.91488 1.000 47.16596  ? 180 MET   A CG  1 
ATOM   1271 S  SD  . MET   A 1 173 ? -5.84295  -18.68947 -30.31556 1.000 51.15689  ? 180 MET   A SD  1 
ATOM   1272 C  CE  . MET   A 1 173 ? -6.52476  -17.29759 -29.43068 1.000 40.67967  ? 180 MET   A CE  1 
ATOM   1273 N  N   . GLY   A 1 174 ? -9.73937  -17.34137 -34.28096 1.000 33.56977  ? 181 GLY   A N   1 
ATOM   1274 C  CA  . GLY   A 1 174 ? -10.22763 -16.09201 -34.83672 1.000 35.41420  ? 181 GLY   A CA  1 
ATOM   1275 C  C   . GLY   A 1 174 ? -9.22421  -14.97069 -34.66622 1.000 31.65688  ? 181 GLY   A C   1 
ATOM   1276 O  O   . GLY   A 1 174 ? -8.66039  -14.47857 -35.65262 1.000 34.19991  ? 181 GLY   A O   1 
ATOM   1277 N  N   . ARG   A 1 175 ? -8.97977  -14.57439 -33.41727 1.000 27.26257  ? 182 ARG   A N   1 
ATOM   1278 C  CA  . ARG   A 1 175 ? -7.99982  -13.54424 -33.09437 1.000 24.58713  ? 182 ARG   A CA  1 
ATOM   1279 C  C   . ARG   A 1 175 ? -7.79885  -13.52213 -31.58983 1.000 26.38565  ? 182 ARG   A C   1 
ATOM   1280 O  O   . ARG   A 1 175 ? -8.76996  -13.63159 -30.82933 1.000 26.85395  ? 182 ARG   A O   1 
ATOM   1281 C  CB  . ARG   A 1 175 ? -8.45867  -12.15781 -33.58664 1.000 26.15270  ? 182 ARG   A CB  1 
ATOM   1282 C  CG  . ARG   A 1 175 ? -7.39402  -11.06731 -33.40159 1.000 26.05147  ? 182 ARG   A CG  1 
ATOM   1283 C  CD  . ARG   A 1 175 ? -8.00119  -9.66315  -33.42213 1.000 26.73181  ? 182 ARG   A CD  1 
ATOM   1284 N  NE  . ARG   A 1 175 ? -8.94286  -9.46820  -32.32339 1.000 24.29815  ? 182 ARG   A NE  1 
ATOM   1285 C  CZ  . ARG   A 1 175 ? -10.25092 -9.33081  -32.47425 1.000 24.46704  ? 182 ARG   A CZ  1 
ATOM   1286 N  NH1 . ARG   A 1 175 ? -10.81595 -9.32606  -33.67844 1.000 27.77338  ? 182 ARG   A NH1 1 
ATOM   1287 N  NH2 . ARG   A 1 175 ? -11.01750 -9.19949  -31.39298 1.000 26.04769  ? 182 ARG   A NH2 1 
ATOM   1288 N  N   . GLY   A 1 176 ? -6.54537  -13.40365 -31.16418 1.000 22.19042  ? 183 GLY   A N   1 
ATOM   1289 C  CA  . GLY   A 1 176 ? -6.28592  -13.20243 -29.75406 1.000 21.43538  ? 183 GLY   A CA  1 
ATOM   1290 C  C   . GLY   A 1 176 ? -5.20435  -14.12909 -29.26765 1.000 28.05890  ? 183 GLY   A C   1 
ATOM   1291 O  O   . GLY   A 1 176 ? -4.39947  -14.64457 -30.04852 1.000 23.79174  ? 183 GLY   A O   1 
ATOM   1292 N  N   . THR   A 1 177 ? -5.19796  -14.36660 -27.96047 1.000 24.14144  ? 184 THR   A N   1 
ATOM   1293 C  CA  . THR   A 1 177 ? -4.13350  -15.13153 -27.33265 1.000 21.75172  ? 184 THR   A CA  1 
ATOM   1294 C  C   . THR   A 1 177 ? -4.71660  -15.99240 -26.23164 1.000 24.46617  ? 184 THR   A C   1 
ATOM   1295 O  O   . THR   A 1 177 ? -5.58625  -15.54713 -25.47627 1.000 22.81785  ? 184 THR   A O   1 
ATOM   1296 C  CB  . THR   A 1 177 ? -3.06167  -14.21167 -26.74901 1.000 25.21231  ? 184 THR   A CB  1 
ATOM   1297 O  OG1 . THR   A 1 177 ? -2.48728  -13.43687 -27.80122 1.000 24.99288  ? 184 THR   A OG1 1 
ATOM   1298 C  CG2 . THR   A 1 177 ? -1.97355  -15.02492 -26.05439 1.000 23.16533  ? 184 THR   A CG2 1 
ATOM   1299 N  N   . LYS   A 1 178 ? -4.24573  -17.23379 -26.18054 1.000 21.74710  ? 185 LYS   A N   1 
ATOM   1300 C  CA  . LYS   A 1 178 ? -4.56808  -18.21173 -25.14660 1.000 23.23046  ? 185 LYS   A CA  1 
ATOM   1301 C  C   . LYS   A 1 178 ? -3.26119  -18.55582 -24.44596 1.000 23.90144  ? 185 LYS   A C   1 
ATOM   1302 O  O   . LYS   A 1 178 ? -2.32901  -19.02924 -25.10053 1.000 24.32550  ? 185 LYS   A O   1 
ATOM   1303 C  CB  . LYS   A 1 178 ? -5.17265  -19.44970 -25.81166 1.000 26.73271  ? 185 LYS   A CB  1 
ATOM   1304 C  CG  . LYS   A 1 178 ? -5.74194  -20.51140 -24.93118 1.000 40.21142  ? 185 LYS   A CG  1 
ATOM   1305 C  CD  . LYS   A 1 178 ? -6.51308  -21.54973 -25.77354 1.000 39.97874  ? 185 LYS   A CD  1 
ATOM   1306 C  CE  . LYS   A 1 178 ? -7.31496  -20.88730 -26.88500 1.000 51.73817  ? 185 LYS   A CE  1 
ATOM   1307 N  NZ  . LYS   A 1 178 ? -8.03571  -21.88834 -27.72652 1.000 66.92670  ? 185 LYS   A NZ  1 
ATOM   1308 N  N   . VAL   A 1 179 ? -3.16574  -18.28206 -23.14224 1.000 19.17515  ? 186 VAL   A N   1 
ATOM   1309 C  CA  . VAL   A 1 179 ? -1.99704  -18.68428 -22.35865 1.000 17.90452  ? 186 VAL   A CA  1 
ATOM   1310 C  C   . VAL   A 1 179 ? -2.39878  -19.88044 -21.51465 1.000 23.22636  ? 186 VAL   A C   1 
ATOM   1311 O  O   . VAL   A 1 179 ? -3.29992  -19.77910 -20.66546 1.000 23.73162  ? 186 VAL   A O   1 
ATOM   1312 C  CB  . VAL   A 1 179 ? -1.47049  -17.54564 -21.47620 1.000 19.92448  ? 186 VAL   A CB  1 
ATOM   1313 C  CG1 . VAL   A 1 179 ? -0.29601  -18.06348 -20.59660 1.000 21.93266  ? 186 VAL   A CG1 1 
ATOM   1314 C  CG2 . VAL   A 1 179 ? -1.01840  -16.37493 -22.34490 1.000 25.97971  ? 186 VAL   A CG2 1 
ATOM   1315 N  N   . ILE   A 1 180 ? -1.76176  -21.02377 -21.75940 1.000 19.17992  ? 187 ILE   A N   1 
ATOM   1316 C  CA  . ILE   A 1 180 ? -2.09766  -22.26435 -21.07292 1.000 20.47079  ? 187 ILE   A CA  1 
ATOM   1317 C  C   . ILE   A 1 180 ? -0.99863  -22.54162 -20.06241 1.000 22.78575  ? 187 ILE   A C   1 
ATOM   1318 O  O   . ILE   A 1 180 ? 0.15482   -22.78051 -20.43853 1.000 24.43034  ? 187 ILE   A O   1 
ATOM   1319 C  CB  . ILE   A 1 180 ? -2.26132  -23.44172 -22.04446 1.000 24.98876  ? 187 ILE   A CB  1 
ATOM   1320 C  CG1 . ILE   A 1 180 ? -3.28405  -23.09393 -23.13113 1.000 24.95311  ? 187 ILE   A CG1 1 
ATOM   1321 C  CG2 . ILE   A 1 180 ? -2.66017  -24.70795 -21.29002 1.000 26.06024  ? 187 ILE   A CG2 1 
ATOM   1322 C  CD1 . ILE   A 1 180 ? -3.22299  -24.04471 -24.32164 1.000 30.07953  ? 187 ILE   A CD1 1 
ATOM   1323 N  N   . LEU   A 1 181 ? -1.35295  -22.50697 -18.77776 1.000 20.67436  ? 188 LEU   A N   1 
ATOM   1324 C  CA  . LEU   A 1 181 ? -0.40376  -22.72364 -17.69404 1.000 21.64759  ? 188 LEU   A CA  1 
ATOM   1325 C  C   . LEU   A 1 181 ? -0.50896  -24.17498 -17.25886 1.000 24.48066  ? 188 LEU   A C   1 
ATOM   1326 O  O   . LEU   A 1 181 ? -1.52774  -24.58019 -16.69410 1.000 23.98629  ? 188 LEU   A O   1 
ATOM   1327 C  CB  . LEU   A 1 181 ? -0.71635  -21.80827 -16.51083 1.000 19.70358  ? 188 LEU   A CB  1 
ATOM   1328 C  CG  . LEU   A 1 181 ? -0.77308  -20.33872 -16.88351 1.000 22.37458  ? 188 LEU   A CG  1 
ATOM   1329 C  CD1 . LEU   A 1 181 ? -1.16199  -19.54712 -15.65830 1.000 25.89797  ? 188 LEU   A CD1 1 
ATOM   1330 C  CD2 . LEU   A 1 181 ? 0.57953   -19.89754 -17.42825 1.000 22.66396  ? 188 LEU   A CD2 1 
ATOM   1331 N  N   . HIS   A 1 182 ? 0.53654   -24.95789 -17.50873 1.000 21.98024  ? 189 HIS   A N   1 
ATOM   1332 C  CA  . HIS   A 1 182 ? 0.58942   -26.32549 -17.00723 1.000 26.17058  ? 189 HIS   A CA  1 
ATOM   1333 C  C   . HIS   A 1 182 ? 1.15345   -26.24536 -15.59791 1.000 24.46766  ? 189 HIS   A C   1 
ATOM   1334 O  O   . HIS   A 1 182 ? 2.35412   -26.05147 -15.41288 1.000 25.73049  ? 189 HIS   A O   1 
ATOM   1335 C  CB  . HIS   A 1 182 ? 1.44924   -27.20586 -17.91008 1.000 25.55325  ? 189 HIS   A CB  1 
ATOM   1336 C  CG  . HIS   A 1 182 ? 1.02704   -27.17809 -19.34857 1.000 26.71845  ? 189 HIS   A CG  1 
ATOM   1337 N  ND1 . HIS   A 1 182 ? 0.23704   -28.15958 -19.90988 1.000 31.62521  ? 189 HIS   A ND1 1 
ATOM   1338 C  CD2 . HIS   A 1 182 ? 1.27469   -26.28225 -20.33370 1.000 28.16039  ? 189 HIS   A CD2 1 
ATOM   1339 C  CE1 . HIS   A 1 182 ? 0.01739   -27.86946 -21.18200 1.000 31.44234  ? 189 HIS   A CE1 1 
ATOM   1340 N  NE2 . HIS   A 1 182 ? 0.64142   -26.73864 -21.46559 1.000 29.62372  ? 189 HIS   A NE2 1 
ATOM   1341 N  N   . LEU   A 1 183 ? 0.28777   -26.37659 -14.59710 1.000 24.38891  ? 190 LEU   A N   1 
ATOM   1342 C  CA  . LEU   A 1 183 ? 0.68075   -25.98559 -13.25062 1.000 24.66360  ? 190 LEU   A CA  1 
ATOM   1343 C  C   . LEU   A 1 183 ? 1.62405   -26.99222 -12.61072 1.000 27.82600  ? 190 LEU   A C   1 
ATOM   1344 O  O   . LEU   A 1 183 ? 1.50848   -28.20862 -12.81347 1.000 30.67135  ? 190 LEU   A O   1 
ATOM   1345 C  CB  . LEU   A 1 183 ? -0.55199  -25.81768 -12.36548 1.000 23.22490  ? 190 LEU   A CB  1 
ATOM   1346 C  CG  . LEU   A 1 183 ? -1.47015  -24.69181 -12.81035 1.000 24.00736  ? 190 LEU   A CG  1 
ATOM   1347 C  CD1 . LEU   A 1 183 ? -2.67771  -24.62683 -11.86545 1.000 27.34080  ? 190 LEU   A CD1 1 
ATOM   1348 C  CD2 . LEU   A 1 183 ? -0.70881  -23.35686 -12.86546 1.000 26.43463  ? 190 LEU   A CD2 1 
ATOM   1349 N  N   . LYS   A 1 184 ? 2.55334   -26.46616 -11.81430 1.000 27.58596  ? 191 LYS   A N   1 
ATOM   1350 C  CA  . LYS   A 1 184 ? 3.36497   -27.29420 -10.93256 1.000 29.30360  ? 191 LYS   A CA  1 
ATOM   1351 C  C   . LYS   A 1 184 ? 2.46493   -28.06894 -9.97632  1.000 34.72869  ? 191 LYS   A C   1 
ATOM   1352 O  O   . LYS   A 1 184 ? 1.37695   -27.60783 -9.61165  1.000 31.67372  ? 191 LYS   A O   1 
ATOM   1353 C  CB  . LYS   A 1 184 ? 4.32392   -26.41683 -10.12510 1.000 32.21883  ? 191 LYS   A CB  1 
ATOM   1354 C  CG  . LYS   A 1 184 ? 5.36705   -25.65259 -10.94972 1.000 35.94402  ? 191 LYS   A CG  1 
ATOM   1355 C  CD  . LYS   A 1 184 ? 6.12487   -24.65954 -10.04828 1.000 37.41680  ? 191 LYS   A CD  1 
ATOM   1356 C  CE  . LYS   A 1 184 ? 7.09027   -23.78116 -10.84761 1.000 49.43887  ? 191 LYS   A CE  1 
ATOM   1357 N  NZ  . LYS   A 1 184 ? 7.76410   -22.69661 -10.04740 1.000 41.87883  ? 191 LYS   A NZ  1 
ATOM   1358 N  N   . GLU   A 1 185 ? 2.94946   -29.24468 -9.55124  1.000 33.89787  ? 192 GLU   A N   1 
ATOM   1359 C  CA  . GLU   A 1 185 ? 2.14743   -30.16725 -8.74284  1.000 34.67249  ? 192 GLU   A CA  1 
ATOM   1360 C  C   . GLU   A 1 185 ? 1.63127   -29.53364 -7.45617  1.000 44.10738  ? 192 GLU   A C   1 
ATOM   1361 O  O   . GLU   A 1 185 ? 0.54513   -29.89221 -6.98671  1.000 40.88178  ? 192 GLU   A O   1 
ATOM   1362 C  CB  . GLU   A 1 185 ? 2.96649   -31.41364 -8.39601  1.000 40.64100  ? 192 GLU   A CB  1 
ATOM   1363 C  CG  . GLU   A 1 185 ? 2.81520   -32.54736 -9.38682  1.000 65.30207  ? 192 GLU   A CG  1 
ATOM   1364 C  CD  . GLU   A 1 185 ? 3.29472   -33.87123 -8.82512  1.000 82.70743  ? 192 GLU   A CD  1 
ATOM   1365 O  OE1 . GLU   A 1 185 ? 2.57429   -34.88368 -8.97858  1.000 88.51480  ? 192 GLU   A OE1 1 
ATOM   1366 O  OE2 . GLU   A 1 185 ? 4.39130   -33.89410 -8.22459  1.000 88.09558  ? 192 GLU   A OE2 1 
ATOM   1367 N  N   . ASP   A 1 186 ? 2.38642   -28.61417 -6.86047  1.000 35.17693  ? 193 ASP   A N   1 
ATOM   1368 C  CA  . ASP   A 1 186 ? 1.99592   -28.01567 -5.58954  1.000 36.10389  ? 193 ASP   A CA  1 
ATOM   1369 C  C   . ASP   A 1 186 ? 1.31318   -26.67028 -5.75885  1.000 37.90824  ? 193 ASP   A C   1 
ATOM   1370 O  O   . ASP   A 1 186 ? 1.13069   -25.95061 -4.76933  1.000 37.21834  ? 193 ASP   A O   1 
ATOM   1371 C  CB  . ASP   A 1 186 ? 3.20743   -27.87110 -4.66300  1.000 41.68525  ? 193 ASP   A CB  1 
ATOM   1372 C  CG  . ASP   A 1 186 ? 4.32965   -27.05357 -5.27895  1.000 54.19363  ? 193 ASP   A CG  1 
ATOM   1373 O  OD1 . ASP   A 1 186 ? 5.33042   -26.80942 -4.57330  1.000 64.58161  ? 193 ASP   A OD1 1 
ATOM   1374 O  OD2 . ASP   A 1 186 ? 4.22452   -26.65790 -6.45717  1.000 57.07688  ? 193 ASP   A OD2 1 
ATOM   1375 N  N   . GLN   A 1 187 ? 0.91376   -26.31801 -6.98024  1.000 29.85025  ? 194 GLN   A N   1 
ATOM   1376 C  CA  . GLN   A 1 187 ? 0.25743   -25.04322 -7.24005  1.000 26.46411  ? 194 GLN   A CA  1 
ATOM   1377 C  C   . GLN   A 1 187 ? -1.18210  -25.22785 -7.73052  1.000 28.86198  ? 194 GLN   A C   1 
ATOM   1378 O  O   . GLN   A 1 187 ? -1.71268  -24.36671 -8.42839  1.000 28.55306  ? 194 GLN   A O   1 
ATOM   1379 C  CB  . GLN   A 1 187 ? 1.07122   -24.22530 -8.25200  1.000 28.97145  ? 194 GLN   A CB  1 
ATOM   1380 C  CG  . GLN   A 1 187 ? 2.51051   -23.90713 -7.81224  1.000 30.52061  ? 194 GLN   A CG  1 
ATOM   1381 C  CD  . GLN   A 1 187 ? 2.57782   -23.17123 -6.47375  1.000 32.47953  ? 194 GLN   A CD  1 
ATOM   1382 O  OE1 . GLN   A 1 187 ? 1.75823   -22.29128 -6.19703  1.000 33.69207  ? 194 GLN   A OE1 1 
ATOM   1383 N  NE2 . GLN   A 1 187 ? 3.58128   -23.49195 -5.66345  1.000 33.64856  ? 194 GLN   A NE2 1 
ATOM   1384 N  N   . THR   A 1 188 ? -1.83756  -26.33515 -7.37070  1.000 31.29141  ? 195 THR   A N   1 
ATOM   1385 C  CA  . THR   A 1 188 ? -3.18227  -26.58059 -7.88734  1.000 33.19040  ? 195 THR   A CA  1 
ATOM   1386 C  C   . THR   A 1 188 ? -4.24712  -25.72405 -7.21509  1.000 32.09564  ? 195 THR   A C   1 
ATOM   1387 O  O   . THR   A 1 188 ? -5.41958  -25.79226 -7.60919  1.000 29.80320  ? 195 THR   A O   1 
ATOM   1388 C  CB  . THR   A 1 188 ? -3.55438  -28.05857 -7.74654  1.000 36.29503  ? 195 THR   A CB  1 
ATOM   1389 O  OG1 . THR   A 1 188 ? -3.46579  -28.45533 -6.37226  1.000 37.32864  ? 195 THR   A OG1 1 
ATOM   1390 C  CG2 . THR   A 1 188 ? -2.60678  -28.91105 -8.56197  1.000 36.39968  ? 195 THR   A CG2 1 
ATOM   1391 N  N   . GLU   A 1 189 ? -3.87744  -24.92225 -6.21652  1.000 29.93285  ? 196 GLU   A N   1 
ATOM   1392 C  CA  . GLU   A 1 189 ? -4.84357  -23.99372 -5.63802  1.000 34.18330  ? 196 GLU   A CA  1 
ATOM   1393 C  C   . GLU   A 1 189 ? -5.38470  -23.02835 -6.68812  1.000 31.51704  ? 196 GLU   A C   1 
ATOM   1394 O  O   . GLU   A 1 189 ? -6.51340  -22.54338 -6.56517  1.000 30.04512  ? 196 GLU   A O   1 
ATOM   1395 C  CB  . GLU   A 1 189 ? -4.19577  -23.24769 -4.47130  1.000 32.09845  ? 196 GLU   A CB  1 
ATOM   1396 C  CG  . GLU   A 1 189 ? -3.22472  -22.15315 -4.88916  1.000 28.91831  ? 196 GLU   A CG  1 
ATOM   1397 C  CD  . GLU   A 1 189 ? -2.46143  -21.57896 -3.70286  1.000 43.52516  ? 196 GLU   A CD  1 
ATOM   1398 O  OE1 . GLU   A 1 189 ? -2.79796  -20.46267 -3.24585  1.000 35.21692  ? 196 GLU   A OE1 1 
ATOM   1399 O  OE2 . GLU   A 1 189 ? -1.51629  -22.24927 -3.22689  1.000 43.17094  ? 196 GLU   A OE2 1 
ATOM   1400 N  N   . TYR   A 1 190 ? -4.61605  -22.76086 -7.74139  1.000 27.42018  ? 197 TYR   A N   1 
ATOM   1401 C  CA  . TYR   A 1 190 ? -5.04592  -21.83277 -8.78244  1.000 23.41495  ? 197 TYR   A CA  1 
ATOM   1402 C  C   . TYR   A 1 190 ? -6.01212  -22.46806 -9.77886  1.000 28.58215  ? 197 TYR   A C   1 
ATOM   1403 O  O   . TYR   A 1 190 ? -6.36107  -21.83179 -10.77738 1.000 29.43432  ? 197 TYR   A O   1 
ATOM   1404 C  CB  . TYR   A 1 190 ? -3.81522  -21.23776 -9.48509  1.000 22.50454  ? 197 TYR   A CB  1 
ATOM   1405 C  CG  . TYR   A 1 190 ? -2.94535  -20.54361 -8.47707  1.000 24.27709  ? 197 TYR   A CG  1 
ATOM   1406 C  CD1 . TYR   A 1 190 ? -3.39637  -19.41002 -7.81747  1.000 25.07725  ? 197 TYR   A CD1 1 
ATOM   1407 C  CD2 . TYR   A 1 190 ? -1.71813  -21.08237 -8.09865  1.000 26.13327  ? 197 TYR   A CD2 1 
ATOM   1408 C  CE1 . TYR   A 1 190 ? -2.62037  -18.79493 -6.84828  1.000 28.31506  ? 197 TYR   A CE1 1 
ATOM   1409 C  CE2 . TYR   A 1 190 ? -0.94083  -20.47889 -7.14991  1.000 28.26493  ? 197 TYR   A CE2 1 
ATOM   1410 C  CZ  . TYR   A 1 190 ? -1.39324  -19.33694 -6.51763  1.000 29.33652  ? 197 TYR   A CZ  1 
ATOM   1411 O  OH  . TYR   A 1 190 ? -0.62123  -18.74870 -5.54620  1.000 31.70721  ? 197 TYR   A OH  1 
ATOM   1412 N  N   . LEU   A 1 191 ? -6.45342  -23.70118 -9.52970  1.000 25.81983  ? 198 LEU   A N   1 
ATOM   1413 C  CA  . LEU   A 1 191 ? -7.57269  -24.28835 -10.24764 1.000 29.95906  ? 198 LEU   A CA  1 
ATOM   1414 C  C   . LEU   A 1 191 ? -8.88180  -24.14255 -9.48887  1.000 33.03737  ? 198 LEU   A C   1 
ATOM   1415 O  O   . LEU   A 1 191 ? -9.93310  -24.50910 -10.02478 1.000 33.15742  ? 198 LEU   A O   1 
ATOM   1416 C  CB  . LEU   A 1 191 ? -7.31644  -25.77639 -10.51369 1.000 30.33039  ? 198 LEU   A CB  1 
ATOM   1417 C  CG  . LEU   A 1 191 ? -6.07593  -26.00998 -11.37499 1.000 31.09282  ? 198 LEU   A CG  1 
ATOM   1418 C  CD1 . LEU   A 1 191 ? -5.82075  -27.50175 -11.54718 1.000 32.60854  ? 198 LEU   A CD1 1 
ATOM   1419 C  CD2 . LEU   A 1 191 ? -6.21662  -25.30524 -12.71159 1.000 32.62964  ? 198 LEU   A CD2 1 
ATOM   1420 N  N   . GLU   A 1 192 ? -8.84185  -23.63531 -8.25630  1.000 27.77225  ? 199 GLU   A N   1 
ATOM   1421 C  CA  . GLU   A 1 192 ? -10.02751 -23.55736 -7.40867  1.000 32.01066  ? 199 GLU   A CA  1 
ATOM   1422 C  C   . GLU   A 1 192 ? -10.79320 -22.27064 -7.68874  1.000 27.89490  ? 199 GLU   A C   1 
ATOM   1423 O  O   . GLU   A 1 192 ? -10.20432 -21.18359 -7.70743  1.000 28.59558  ? 199 GLU   A O   1 
ATOM   1424 C  CB  . GLU   A 1 192 ? -9.63820  -23.61277 -5.92811  1.000 33.57837  ? 199 GLU   A CB  1 
ATOM   1425 C  CG  . GLU   A 1 192 ? -8.97745  -24.90710 -5.48144  1.000 39.19495  ? 199 GLU   A CG  1 
ATOM   1426 C  CD  . GLU   A 1 192 ? -9.89897  -26.10990 -5.58735  1.000 65.43225  ? 199 GLU   A CD  1 
ATOM   1427 O  OE1 . GLU   A 1 192 ? -11.13660 -25.91891 -5.64020  1.000 73.05606  ? 199 GLU   A OE1 1 
ATOM   1428 O  OE2 . GLU   A 1 192 ? -9.38328  -27.25098 -5.61388  1.000 66.69823  ? 199 GLU   A OE2 1 
ATOM   1429 N  N   . GLU   A 1 193 ? -12.11049 -22.39698 -7.86965  1.000 31.51233  ? 200 GLU   A N   1 
ATOM   1430 C  CA  . GLU   A 1 193 ? -12.92923 -21.23351 -8.20243  1.000 31.76408  ? 200 GLU   A CA  1 
ATOM   1431 C  C   . GLU   A 1 193 ? -12.79397 -20.13588 -7.14739  1.000 28.52443  ? 200 GLU   A C   1 
ATOM   1432 O  O   . GLU   A 1 193 ? -12.56785 -18.96889 -7.48589  1.000 27.84613  ? 200 GLU   A O   1 
ATOM   1433 C  CB  . GLU   A 1 193 ? -14.39536 -21.64682 -8.37109  1.000 35.98049  ? 200 GLU   A CB  1 
ATOM   1434 C  CG  . GLU   A 1 193 ? -15.34881 -20.48023 -8.65599  1.000 36.98874  ? 200 GLU   A CG  1 
ATOM   1435 C  CD  . GLU   A 1 193 ? -16.82209 -20.88228 -8.63547  1.000 63.09304  ? 200 GLU   A CD  1 
ATOM   1436 O  OE1 . GLU   A 1 193 ? -17.12644 -22.09350 -8.54068  1.000 63.11802  ? 200 GLU   A OE1 1 
ATOM   1437 O  OE2 . GLU   A 1 193 ? -17.68026 -19.98248 -8.74865  1.000 67.34303  ? 200 GLU   A OE2 1 
ATOM   1438 N  N   . ARG   A 1 194 ? -12.90765 -20.48943 -5.86053  1.000 29.99741  ? 201 ARG   A N   1 
ATOM   1439 C  CA  . ARG   A 1 194 ? -12.85342 -19.43960 -4.84214  1.000 29.89689  ? 201 ARG   A CA  1 
ATOM   1440 C  C   . ARG   A 1 194 ? -11.48580 -18.77980 -4.79430  1.000 28.77255  ? 201 ARG   A C   1 
ATOM   1441 O  O   . ARG   A 1 194 ? -11.38752 -17.59188 -4.47201  1.000 30.48893  ? 201 ARG   A O   1 
ATOM   1442 C  CB  . ARG   A 1 194 ? -13.21431 -19.97563 -3.45652  1.000 33.27293  ? 201 ARG   A CB  1 
ATOM   1443 C  CG  . ARG   A 1 194 ? -12.74083 -21.36814 -3.16532  1.000 51.01972  ? 201 ARG   A CG  1 
ATOM   1444 C  CD  . ARG   A 1 194 ? -13.42885 -21.88541 -1.91268  1.000 57.75993  ? 201 ARG   A CD  1 
ATOM   1445 N  NE  . ARG   A 1 194 ? -12.52540 -22.68948 -1.10062  1.000 72.26881  ? 201 ARG   A NE  1 
ATOM   1446 C  CZ  . ARG   A 1 194 ? -12.80156 -23.11390 0.12494   1.000 66.14935  ? 201 ARG   A CZ  1 
ATOM   1447 N  NH1 . ARG   A 1 194 ? -13.94954 -22.81528 0.71806   1.000 54.13361  ? 201 ARG   A NH1 1 
ATOM   1448 N  NH2 . ARG   A 1 194 ? -11.90192 -23.84962 0.77334   1.000 63.62317  ? 201 ARG   A NH2 1 
ATOM   1449 N  N   . ARG   A 1 195 ? -10.42218 -19.51888 -5.11808  1.000 26.68918  ? 202 ARG   A N   1 
ATOM   1450 C  CA  . ARG   A 1 195 ? -9.09344  -18.91826 -5.10810  1.000 24.95518  ? 202 ARG   A CA  1 
ATOM   1451 C  C   . ARG   A 1 195 ? -8.91335  -17.95165 -6.27339  1.000 26.44025  ? 202 ARG   A C   1 
ATOM   1452 O  O   . ARG   A 1 195 ? -8.37098  -16.85544 -6.10109  1.000 24.33585  ? 202 ARG   A O   1 
ATOM   1453 C  CB  . ARG   A 1 195 ? -8.02605  -20.00935 -5.14562  1.000 26.70217  ? 202 ARG   A CB  1 
ATOM   1454 C  CG  . ARG   A 1 195 ? -6.58663  -19.48868 -5.10890  1.000 26.18351  ? 202 ARG   A CG  1 
ATOM   1455 C  CD  . ARG   A 1 195 ? -6.24744  -18.83055 -3.76133  1.000 29.32669  ? 202 ARG   A CD  1 
ATOM   1456 N  NE  . ARG   A 1 195 ? -4.81417  -18.57864 -3.64943  1.000 29.83783  ? 202 ARG   A NE  1 
ATOM   1457 C  CZ  . ARG   A 1 195 ? -4.26963  -17.38254 -3.46358  1.000 32.80619  ? 202 ARG   A CZ  1 
ATOM   1458 N  NH1 . ARG   A 1 195 ? -5.01461  -16.30405 -3.28751  1.000 29.18993  ? 202 ARG   A NH1 1 
ATOM   1459 N  NH2 . ARG   A 1 195 ? -2.94264  -17.26408 -3.47634  1.000 31.79098  ? 202 ARG   A NH2 1 
ATOM   1460 N  N   . ILE   A 1 196 ? -9.36244  -18.33468 -7.47054  1.000 25.23054  ? 203 ILE   A N   1 
ATOM   1461 C  CA  . ILE   A 1 196 ? -9.23227  -17.44004 -8.61831  1.000 23.32348  ? 203 ILE   A CA  1 
ATOM   1462 C  C   . ILE   A 1 196 ? -10.07743 -16.18827 -8.41235  1.000 24.21182  ? 203 ILE   A C   1 
ATOM   1463 O  O   . ILE   A 1 196 ? -9.61554  -15.06279 -8.66197  1.000 24.82536  ? 203 ILE   A O   1 
ATOM   1464 C  CB  . ILE   A 1 196 ? -9.60058  -18.18346 -9.91490  1.000 22.12896  ? 203 ILE   A CB  1 
ATOM   1465 C  CG1 . ILE   A 1 196 ? -8.64255  -19.36652 -10.12090 1.000 22.24337  ? 203 ILE   A CG1 1 
ATOM   1466 C  CG2 . ILE   A 1 196 ? -9.52226  -17.24737 -11.14236 1.000 21.88255  ? 203 ILE   A CG2 1 
ATOM   1467 C  CD1 . ILE   A 1 196 ? -9.20945  -20.45732 -11.04213 1.000 34.06707  ? 203 ILE   A CD1 1 
ATOM   1468 N  N   . LYS   A 1 197 ? -11.31180 -16.35939 -7.92946  1.000 23.82787  ? 204 LYS   A N   1 
ATOM   1469 C  CA  . LYS   A 1 197 ? -12.18100 -15.21610 -7.66052  1.000 24.63267  ? 204 LYS   A CA  1 
ATOM   1470 C  C   . LYS   A 1 197 ? -11.52056 -14.25331 -6.69063  1.000 26.76880  ? 204 LYS   A C   1 
ATOM   1471 O  O   . LYS   A 1 197 ? -11.55290 -13.03482 -6.88832  1.000 26.26334  ? 204 LYS   A O   1 
ATOM   1472 C  CB  . LYS   A 1 197 ? -13.51622 -15.67694 -7.07867  1.000 26.82078  ? 204 LYS   A CB  1 
ATOM   1473 C  CG  . LYS   A 1 197 ? -14.57133 -16.02622 -8.08810  1.000 42.79424  ? 204 LYS   A CG  1 
ATOM   1474 C  CD  . LYS   A 1 197 ? -15.93911 -15.98750 -7.42025  1.000 50.31234  ? 204 LYS   A CD  1 
ATOM   1475 C  CE  . LYS   A 1 197 ? -16.58802 -17.35473 -7.40807  1.000 61.50424  ? 204 LYS   A CE  1 
ATOM   1476 N  NZ  . LYS   A 1 197 ? -18.03335 -17.26883 -7.76640  1.000 58.71528  ? 204 LYS   A NZ  1 
ATOM   1477 N  N   . GLU   A 1 198 ? -10.92969 -14.79522 -5.62382  1.000 25.48254  ? 205 GLU   A N   1 
ATOM   1478 C  CA  . GLU   A 1 198 ? -10.23141 -13.97407 -4.63793  1.000 25.42411  ? 205 GLU   A CA  1 
ATOM   1479 C  C   . GLU   A 1 198 ? -9.13206  -13.14709 -5.29477  1.000 28.28521  ? 205 GLU   A C   1 
ATOM   1480 O  O   . GLU   A 1 198 ? -8.98690  -11.94609 -5.01796  1.000 26.17566  ? 205 GLU   A O   1 
ATOM   1481 C  CB  . GLU   A 1 198 ? -9.65248  -14.87923 -3.54769  1.000 25.62442  ? 205 GLU   A CB  1 
ATOM   1482 C  CG  . GLU   A 1 198 ? -8.90725  -14.16574 -2.43563  1.000 33.86029  ? 205 GLU   A CG  1 
ATOM   1483 C  CD  . GLU   A 1 198 ? -8.25103  -15.14144 -1.46626  1.000 34.16242  ? 205 GLU   A CD  1 
ATOM   1484 O  OE1 . GLU   A 1 198 ? -7.68912  -16.15669 -1.93987  1.000 33.33481  ? 205 GLU   A OE1 1 
ATOM   1485 O  OE2 . GLU   A 1 198 ? -8.32020  -14.90131 -0.23663  1.000 33.13356  ? 205 GLU   A OE2 1 
ATOM   1486 N  N   . ILE   A 1 199 ? -8.33345  -13.78313 -6.15598  1.000 23.06910  ? 206 ILE   A N   1 
ATOM   1487 C  CA  . ILE   A 1 199 ? -7.19988  -13.09466 -6.76732  1.000 21.72628  ? 206 ILE   A CA  1 
ATOM   1488 C  C   . ILE   A 1 199 ? -7.67488  -12.01661 -7.72490  1.000 25.41277  ? 206 ILE   A C   1 
ATOM   1489 O  O   . ILE   A 1 199 ? -7.10930  -10.91386 -7.77436  1.000 26.29247  ? 206 ILE   A O   1 
ATOM   1490 C  CB  . ILE   A 1 199 ? -6.28051  -14.10119 -7.47923  1.000 23.51525  ? 206 ILE   A CB  1 
ATOM   1491 C  CG1 . ILE   A 1 199 ? -5.67602  -15.06693 -6.46528  1.000 24.65612  ? 206 ILE   A CG1 1 
ATOM   1492 C  CG2 . ILE   A 1 199 ? -5.18421  -13.38369 -8.26169  1.000 25.46819  ? 206 ILE   A CG2 1 
ATOM   1493 C  CD1 . ILE   A 1 199 ? -5.09046  -16.28940 -7.15677  1.000 27.02780  ? 206 ILE   A CD1 1 
ATOM   1494 N  N   . VAL   A 1 200 ? -8.69500  -12.32389 -8.53017  1.000 24.21436  ? 207 VAL   A N   1 
ATOM   1495 C  CA  . VAL   A 1 200 ? -9.18776  -11.33681 -9.48367  1.000 24.80120  ? 207 VAL   A CA  1 
ATOM   1496 C  C   . VAL   A 1 200 ? -9.77547  -10.13837 -8.74154  1.000 26.96092  ? 207 VAL   A C   1 
ATOM   1497 O  O   . VAL   A 1 200 ? -9.54765  -8.98257  -9.11896  1.000 27.25219  ? 207 VAL   A O   1 
ATOM   1498 C  CB  . VAL   A 1 200 ? -10.20790 -11.98124 -10.43945 1.000 23.30405  ? 207 VAL   A CB  1 
ATOM   1499 C  CG1 . VAL   A 1 200 ? -10.98280 -10.90352 -11.21994 1.000 27.43254  ? 207 VAL   A CG1 1 
ATOM   1500 C  CG2 . VAL   A 1 200 ? -9.51986  -12.99106 -11.36562 1.000 24.86415  ? 207 VAL   A CG2 1 
ATOM   1501 N  N   . LYS   A 1 201 ? -10.52852 -10.39188 -7.66730  1.000 26.96937  ? 208 LYS   A N   1 
ATOM   1502 C  CA  . LYS   A 1 201 ? -11.10653 -9.29358  -6.89949  1.000 27.99597  ? 208 LYS   A CA  1 
ATOM   1503 C  C   . LYS   A 1 201 ? -10.01650 -8.40842  -6.30397  1.000 30.22820  ? 208 LYS   A C   1 
ATOM   1504 O  O   . LYS   A 1 201 ? -10.15383 -7.18012  -6.25476  1.000 31.88555  ? 208 LYS   A O   1 
ATOM   1505 C  CB  . LYS   A 1 201 ? -12.00718 -9.85108  -5.79581  1.000 28.71846  ? 208 LYS   A CB  1 
ATOM   1506 C  CG  . LYS   A 1 201 ? -12.79195 -8.77446  -5.05343  1.000 37.45696  ? 208 LYS   A CG  1 
ATOM   1507 C  CD  . LYS   A 1 201 ? -13.60668 -9.37011  -3.91548  1.000 44.66778  ? 208 LYS   A CD  1 
ATOM   1508 C  CE  . LYS   A 1 201 ? -14.48663 -8.31470  -3.25624  1.000 61.36266  ? 208 LYS   A CE  1 
ATOM   1509 N  NZ  . LYS   A 1 201 ? -15.22064 -8.86544  -2.08023  1.000 68.57708  ? 208 LYS   A NZ  1 
ATOM   1510 N  N   . LYS   A 1 202 ? -8.91857  -9.01992  -5.85723  1.000 28.56102  ? 209 LYS   A N   1 
ATOM   1511 C  CA  . LYS   A 1 202 ? -7.85562  -8.27379  -5.18625  1.000 29.85256  ? 209 LYS   A CA  1 
ATOM   1512 C  C   . LYS   A 1 202 ? -7.04301  -7.42645  -6.16362  1.000 30.77703  ? 209 LYS   A C   1 
ATOM   1513 O  O   . LYS   A 1 202 ? -6.70678  -6.27184  -5.86642  1.000 31.66908  ? 209 LYS   A O   1 
ATOM   1514 C  CB  . LYS   A 1 202 ? -6.94626  -9.25361  -4.44776  1.000 32.06737  ? 209 LYS   A CB  1 
ATOM   1515 C  CG  . LYS   A 1 202 ? -5.80388  -8.62995  -3.67832  1.000 32.82535  ? 209 LYS   A CG  1 
ATOM   1516 C  CD  . LYS   A 1 202 ? -5.16669  -9.69019  -2.78159  1.000 46.55475  ? 209 LYS   A CD  1 
ATOM   1517 C  CE  . LYS   A 1 202 ? -4.12329  -9.11830  -1.83734  1.000 57.57941  ? 209 LYS   A CE  1 
ATOM   1518 N  NZ  . LYS   A 1 202 ? -3.28989  -10.21395 -1.24381  1.000 57.12050  ? 209 LYS   A NZ  1 
ATOM   1519 N  N   . HIS   A 1 203 ? -6.69594  -7.98410  -7.32267  1.000 28.12169  ? 210 HIS   A N   1 
ATOM   1520 C  CA  . HIS   A 1 203 ? -5.69140  -7.38181  -8.19101  1.000 30.38520  ? 210 HIS   A CA  1 
ATOM   1521 C  C   . HIS   A 1 203 ? -6.22269  -6.85669  -9.51323  1.000 31.74453  ? 210 HIS   A C   1 
ATOM   1522 O  O   . HIS   A 1 203 ? -5.52536  -6.06619  -10.16289 1.000 30.19069  ? 210 HIS   A O   1 
ATOM   1523 C  CB  . HIS   A 1 203 ? -4.58411  -8.39939  -8.50305  1.000 33.12068  ? 210 HIS   A CB  1 
ATOM   1524 C  CG  . HIS   A 1 203 ? -3.79800  -8.81783  -7.30621  1.000 31.27335  ? 210 HIS   A CG  1 
ATOM   1525 N  ND1 . HIS   A 1 203 ? -2.95643  -7.95532  -6.63731  1.000 33.81142  ? 210 HIS   A ND1 1 
ATOM   1526 C  CD2 . HIS   A 1 203 ? -3.73217  -9.99925  -6.64669  1.000 35.77857  ? 210 HIS   A CD2 1 
ATOM   1527 C  CE1 . HIS   A 1 203 ? -2.40441  -8.58859  -5.61614  1.000 40.27073  ? 210 HIS   A CE1 1 
ATOM   1528 N  NE2 . HIS   A 1 203 ? -2.85623  -9.83055  -5.60055  1.000 36.75472  ? 210 HIS   A NE2 1 
ATOM   1529 N  N   . SER   A 1 204 ? -7.41167  -7.28372  -9.94693  1.000 28.97544  ? 211 SER   A N   1 
ATOM   1530 C  CA  . SER   A 1 204 ? -7.85899  -7.02627  -11.30646 1.000 26.22624  ? 211 SER   A CA  1 
ATOM   1531 C  C   . SER   A 1 204 ? -9.28503  -6.49054  -11.34049 1.000 27.93208  ? 211 SER   A C   1 
ATOM   1532 O  O   . SER   A 1 204 ? -9.97463  -6.63302  -12.34958 1.000 32.81303  ? 211 SER   A O   1 
ATOM   1533 C  CB  . SER   A 1 204 ? -7.75714  -8.29270  -12.16219 1.000 27.97620  ? 211 SER   A CB  1 
ATOM   1534 O  OG  . SER   A 1 204 ? -6.42859  -8.80382  -12.13893 1.000 31.78166  ? 211 SER   A OG  1 
ATOM   1535 N  N   . GLN   A 1 205 ? -9.72210  -5.85655  -10.25345 1.000 33.17987  ? 212 GLN   A N   1 
ATOM   1536 C  CA  . GLN   A 1 205 ? -11.13711 -5.52528  -10.11545 1.000 42.89839  ? 212 GLN   A CA  1 
ATOM   1537 C  C   . GLN   A 1 205 ? -11.59217 -4.47285  -11.12595 1.000 43.93182  ? 212 GLN   A C   1 
ATOM   1538 O  O   . GLN   A 1 205 ? -12.77063 -4.44867  -11.50240 1.000 44.09130  ? 212 GLN   A O   1 
ATOM   1539 C  CB  . GLN   A 1 205 ? -11.40077 -5.08065  -8.67654  1.000 46.64570  ? 212 GLN   A CB  1 
ATOM   1540 C  CG  . GLN   A 1 205 ? -12.73667 -4.43278  -8.41155  1.000 57.77805  ? 212 GLN   A CG  1 
ATOM   1541 C  CD  . GLN   A 1 205 ? -12.93082 -4.11108  -6.94068  1.000 60.10934  ? 212 GLN   A CD  1 
ATOM   1542 O  OE1 . GLN   A 1 205 ? -12.22833 -3.27315  -6.36762  1.000 60.75141  ? 212 GLN   A OE1 1 
ATOM   1543 N  NE2 . GLN   A 1 205 ? -13.89317 -4.78444  -6.32019  1.000 68.79711  ? 212 GLN   A NE2 1 
ATOM   1544 N  N   . PHE   A 1 206 ? -10.68115 -3.62839  -11.61354 1.000 32.35488  ? 213 PHE   A N   1 
ATOM   1545 C  CA  . PHE   A 1 206 ? -11.05839 -2.51329  -12.47737 1.000 30.25601  ? 213 PHE   A CA  1 
ATOM   1546 C  C   . PHE   A 1 206 ? -10.62639 -2.70120  -13.92519 1.000 35.95671  ? 213 PHE   A C   1 
ATOM   1547 O  O   . PHE   A 1 206 ? -10.61504 -1.73527  -14.69181 1.000 35.32408  ? 213 PHE   A O   1 
ATOM   1548 C  CB  . PHE   A 1 206 ? -10.49640 -1.21130  -11.92066 1.000 32.12130  ? 213 PHE   A CB  1 
ATOM   1549 C  CG  . PHE   A 1 206 ? -11.08694 -0.83819  -10.60084 1.000 37.45546  ? 213 PHE   A CG  1 
ATOM   1550 C  CD1 . PHE   A 1 206 ? -12.46488 -0.85641  -10.42110 1.000 43.04466  ? 213 PHE   A CD1 1 
ATOM   1551 C  CD2 . PHE   A 1 206 ? -10.27682 -0.50979  -9.53229  1.000 46.61866  ? 213 PHE   A CD2 1 
ATOM   1552 C  CE1 . PHE   A 1 206 ? -13.02313 -0.53040  -9.20312  1.000 48.49685  ? 213 PHE   A CE1 1 
ATOM   1553 C  CE2 . PHE   A 1 206 ? -10.82900 -0.17686  -8.30698  1.000 49.70170  ? 213 PHE   A CE2 1 
ATOM   1554 C  CZ  . PHE   A 1 206 ? -12.20711 -0.18928  -8.14353  1.000 54.27200  ? 213 PHE   A CZ  1 
ATOM   1555 N  N   . ILE   A 1 207 ? -10.28577 -3.92499  -14.32472 1.000 27.24691  ? 214 ILE   A N   1 
ATOM   1556 C  CA  . ILE   A 1 207 ? -9.98277  -4.18164  -15.72642 1.000 24.30520  ? 214 ILE   A CA  1 
ATOM   1557 C  C   . ILE   A 1 207 ? -11.21321 -3.86655  -16.57609 1.000 28.72801  ? 214 ILE   A C   1 
ATOM   1558 O  O   . ILE   A 1 207 ? -12.34631 -4.20123  -16.21029 1.000 30.80206  ? 214 ILE   A O   1 
ATOM   1559 C  CB  . ILE   A 1 207 ? -9.51874  -5.63841  -15.88474 1.000 25.21027  ? 214 ILE   A CB  1 
ATOM   1560 C  CG1 . ILE   A 1 207 ? -8.19361  -5.82664  -15.14464 1.000 25.15768  ? 214 ILE   A CG1 1 
ATOM   1561 C  CG2 . ILE   A 1 207 ? -9.40344  -6.02853  -17.36381 1.000 28.14736  ? 214 ILE   A CG2 1 
ATOM   1562 C  CD1 . ILE   A 1 207 ? -7.00229  -5.17854  -15.86342 1.000 29.45729  ? 214 ILE   A CD1 1 
ATOM   1563 N  N   . GLY   A 1 208 ? -10.99961 -3.19374  -17.70849 1.000 28.90068  ? 215 GLY   A N   1 
ATOM   1564 C  CA  . GLY   A 1 208 ? -12.10987 -2.62947  -18.46081 1.000 29.80941  ? 215 GLY   A CA  1 
ATOM   1565 C  C   . GLY   A 1 208 ? -12.71935 -3.55622  -19.49718 1.000 30.91449  ? 215 GLY   A C   1 
ATOM   1566 O  O   . GLY   A 1 208 ? -13.28233 -3.09621  -20.49528 1.000 33.15167  ? 215 GLY   A O   1 
ATOM   1567 N  N   . TYR   A 1 209 ? -12.60811 -4.85943  -19.27906 1.000 27.05281  ? 216 TYR   A N   1 
ATOM   1568 C  CA  . TYR   A 1 209 ? -13.15971 -5.87361  -20.16974 1.000 24.82311  ? 216 TYR   A CA  1 
ATOM   1569 C  C   . TYR   A 1 209 ? -13.78643 -6.94811  -19.28938 1.000 29.83641  ? 216 TYR   A C   1 
ATOM   1570 O  O   . TYR   A 1 209 ? -13.32336 -7.16751  -18.16707 1.000 30.09246  ? 216 TYR   A O   1 
ATOM   1571 C  CB  . TYR   A 1 209 ? -12.08504 -6.49332  -21.07791 1.000 24.42013  ? 216 TYR   A CB  1 
ATOM   1572 C  CG  . TYR   A 1 209 ? -11.43297 -5.44719  -21.94252 1.000 24.84204  ? 216 TYR   A CG  1 
ATOM   1573 C  CD1 . TYR   A 1 209 ? -12.04093 -5.01308  -23.10945 1.000 28.35951  ? 216 TYR   A CD1 1 
ATOM   1574 C  CD2 . TYR   A 1 209 ? -10.22094 -4.85224  -21.55391 1.000 25.90027  ? 216 TYR   A CD2 1 
ATOM   1575 C  CE1 . TYR   A 1 209 ? -11.46398 -4.03467  -23.88655 1.000 28.69869  ? 216 TYR   A CE1 1 
ATOM   1576 C  CE2 . TYR   A 1 209 ? -9.63787  -3.86807  -22.32437 1.000 26.41990  ? 216 TYR   A CE2 1 
ATOM   1577 C  CZ  . TYR   A 1 209 ? -10.26731 -3.46402  -23.48881 1.000 27.63429  ? 216 TYR   A CZ  1 
ATOM   1578 O  OH  . TYR   A 1 209 ? -9.72114  -2.48536  -24.27549 1.000 31.13609  ? 216 TYR   A OH  1 
ATOM   1579 N  N   . PRO   A 1 210 ? -14.84567 -7.59981  -19.76402 1.000 29.96977  ? 217 PRO   A N   1 
ATOM   1580 C  CA  . PRO   A 1 210 ? -15.48166 -8.63980  -18.93871 1.000 25.88535  ? 217 PRO   A CA  1 
ATOM   1581 C  C   . PRO   A 1 210 ? -14.56176 -9.83732  -18.77076 1.000 23.99028  ? 217 PRO   A C   1 
ATOM   1582 O  O   . PRO   A 1 210 ? -14.04459 -10.38811 -19.74725 1.000 29.83009  ? 217 PRO   A O   1 
ATOM   1583 C  CB  . PRO   A 1 210 ? -16.75055 -8.99839  -19.72557 1.000 27.97918  ? 217 PRO   A CB  1 
ATOM   1584 C  CG  . PRO   A 1 210 ? -16.48684 -8.56724  -21.11519 1.000 33.84343  ? 217 PRO   A CG  1 
ATOM   1585 C  CD  . PRO   A 1 210 ? -15.55110 -7.38547  -21.03829 1.000 32.86960  ? 217 PRO   A CD  1 
ATOM   1586 N  N   . ILE   A 1 211 ? -14.36551 -10.22649 -17.51421 1.000 25.31742  ? 218 ILE   A N   1 
ATOM   1587 C  CA  . ILE   A 1 211 ? -13.57388 -11.39237 -17.13393 1.000 22.83497  ? 218 ILE   A CA  1 
ATOM   1588 C  C   . ILE   A 1 211 ? -14.55536 -12.46619 -16.68907 1.000 23.26427  ? 218 ILE   A C   1 
ATOM   1589 O  O   . ILE   A 1 211 ? -15.26078 -12.28723 -15.69307 1.000 26.62752  ? 218 ILE   A O   1 
ATOM   1590 C  CB  . ILE   A 1 211 ? -12.59403 -11.06312 -15.99749 1.000 25.94325  ? 218 ILE   A CB  1 
ATOM   1591 C  CG1 . ILE   A 1 211 ? -11.61480 -9.95796  -16.40791 1.000 24.25684  ? 218 ILE   A CG1 1 
ATOM   1592 C  CG2 . ILE   A 1 211 ? -11.85456 -12.31355 -15.53576 1.000 24.85064  ? 218 ILE   A CG2 1 
ATOM   1593 C  CD1 . ILE   A 1 211 ? -10.68436 -9.50655  -15.26189 1.000 23.86967  ? 218 ILE   A CD1 1 
ATOM   1594 N  N   . THR   A 1 212 ? -14.60659 -13.57237 -17.41726 1.000 25.47619  ? 219 THR   A N   1 
ATOM   1595 C  CA  . THR   A 1 212 ? -15.50008 -14.66834 -17.06676 1.000 23.51903  ? 219 THR   A CA  1 
ATOM   1596 C  C   . THR   A 1 212 ? -14.66351 -15.80967 -16.52396 1.000 22.54555  ? 219 THR   A C   1 
ATOM   1597 O  O   . THR   A 1 212 ? -13.76477 -16.30470 -17.21723 1.000 22.96526  ? 219 THR   A O   1 
ATOM   1598 C  CB  . THR   A 1 212 ? -16.30219 -15.13727 -18.27368 1.000 25.28175  ? 219 THR   A CB  1 
ATOM   1599 O  OG1 . THR   A 1 212 ? -17.06146 -14.03523 -18.80346 1.000 27.04438  ? 219 THR   A OG1 1 
ATOM   1600 C  CG2 . THR   A 1 212 ? -17.24668 -16.29035 -17.86595 1.000 24.74880  ? 219 THR   A CG2 1 
ATOM   1601 N  N   . LEU   A 1 213 ? -14.94859 -16.20728 -15.29123 1.000 23.74951  ? 220 LEU   A N   1 
ATOM   1602 C  CA  . LEU   A 1 213 ? -14.28549 -17.34221 -14.66837 1.000 22.36724  ? 220 LEU   A CA  1 
ATOM   1603 C  C   . LEU   A 1 213 ? -15.15781 -18.56074 -14.93228 1.000 22.64636  ? 220 LEU   A C   1 
ATOM   1604 O  O   . LEU   A 1 213 ? -16.25224 -18.68348 -14.36278 1.000 26.77037  ? 220 LEU   A O   1 
ATOM   1605 C  CB  . LEU   A 1 213 ? -14.08602 -17.10153 -13.17547 1.000 24.99357  ? 220 LEU   A CB  1 
ATOM   1606 C  CG  . LEU   A 1 213 ? -13.63033 -18.31182 -12.37098 1.000 28.11164  ? 220 LEU   A CG  1 
ATOM   1607 C  CD1 . LEU   A 1 213 ? -12.33680 -18.86338 -12.99687 1.000 27.11210  ? 220 LEU   A CD1 1 
ATOM   1608 C  CD2 . LEU   A 1 213 ? -13.43049 -17.93842 -10.89442 1.000 28.91379  ? 220 LEU   A CD2 1 
ATOM   1609 N  N   . PHE   A 1 214 ? -14.68300 -19.44020 -15.81057 1.000 22.67307  ? 221 PHE   A N   1 
ATOM   1610 C  CA  . PHE   A 1 214 ? -15.39010 -20.68482 -16.08331 1.000 26.36708  ? 221 PHE   A CA  1 
ATOM   1611 C  C   . PHE   A 1 214 ? -15.31655 -21.59898 -14.87267 1.000 29.23548  ? 221 PHE   A C   1 
ATOM   1612 O  O   . PHE   A 1 214 ? -14.35046 -21.57416 -14.10235 1.000 29.40269  ? 221 PHE   A O   1 
ATOM   1613 C  CB  . PHE   A 1 214 ? -14.78513 -21.42171 -17.28066 1.000 23.29386  ? 221 PHE   A CB  1 
ATOM   1614 C  CG  . PHE   A 1 214 ? -15.05467 -20.78079 -18.63676 1.000 22.20746  ? 221 PHE   A CG  1 
ATOM   1615 C  CD1 . PHE   A 1 214 ? -15.14003 -19.41045 -18.79827 1.000 21.55098  ? 221 PHE   A CD1 1 
ATOM   1616 C  CD2 . PHE   A 1 214 ? -15.23392 -21.58995 -19.75161 1.000 22.82102  ? 221 PHE   A CD2 1 
ATOM   1617 C  CE1 . PHE   A 1 214 ? -15.37333 -18.84822 -20.05936 1.000 23.49921  ? 221 PHE   A CE1 1 
ATOM   1618 C  CE2 . PHE   A 1 214 ? -15.47788 -21.03942 -21.00937 1.000 26.47227  ? 221 PHE   A CE2 1 
ATOM   1619 C  CZ  . PHE   A 1 214 ? -15.54871 -19.67353 -21.16506 1.000 24.30040  ? 221 PHE   A CZ  1 
ATOM   1620 N  N   . VAL   A 1 215 ? -16.34554 -22.42187 -14.70423 1.000 27.04331  ? 222 VAL   A N   1 
ATOM   1621 C  CA  . VAL   A 1 215 ? -16.35162 -23.38916 -13.62206 1.000 29.25090  ? 222 VAL   A CA  1 
ATOM   1622 C  C   . VAL   A 1 215 ? -16.25739 -24.78352 -14.22081 1.000 33.97332  ? 222 VAL   A C   1 
ATOM   1623 O  O   . VAL   A 1 215 ? -16.49223 -25.00675 -15.41136 1.000 29.96713  ? 222 VAL   A O   1 
ATOM   1624 C  CB  . VAL   A 1 215 ? -17.57578 -23.23545 -12.70413 1.000 44.29145  ? 222 VAL   A CB  1 
ATOM   1625 C  CG1 . VAL   A 1 215 ? -17.41989 -21.96989 -11.86262 1.000 44.61467  ? 222 VAL   A CG1 1 
ATOM   1626 C  CG2 . VAL   A 1 215 ? -18.81859 -23.15866 -13.50691 1.000 33.79558  ? 222 VAL   A CG2 1 
ATOM   1627 N  N   . GLU   A 1 216 ? -15.87990 -25.72610 -13.38779 1.000 38.61747  ? 223 GLU   A N   1 
ATOM   1628 C  CA  . GLU   A 1 216 ? -15.51667 -27.03630 -13.88843 1.000 45.47342  ? 223 GLU   A CA  1 
ATOM   1629 C  C   . GLU   A 1 216 ? -16.65036 -28.03489 -13.75715 1.000 51.60712  ? 223 GLU   A C   1 
ATOM   1630 O  O   . GLU   A 1 216 ? -17.49974 -27.94783 -12.86457 1.000 49.30528  ? 223 GLU   A O   1 
ATOM   1631 C  CB  . GLU   A 1 216 ? -14.28007 -27.55534 -13.17702 1.000 50.30957  ? 223 GLU   A CB  1 
ATOM   1632 C  CG  . GLU   A 1 216 ? -13.03488 -27.14720 -13.89806 1.000 50.83782  ? 223 GLU   A CG  1 
ATOM   1633 C  CD  . GLU   A 1 216 ? -11.98150 -28.19914 -13.79232 1.000 52.54860  ? 223 GLU   A CD  1 
ATOM   1634 O  OE1 . GLU   A 1 216 ? -11.96744 -29.12002 -14.64105 1.000 60.42144  ? 223 GLU   A OE1 1 
ATOM   1635 O  OE2 . GLU   A 1 216 ? -11.17233 -28.09762 -12.85473 1.000 64.91994  ? 223 GLU   A OE2 1 
ATOM   1636 N  N   . LYS   A 1 217 ? -16.63296 -28.99587 -14.66948 1.000 57.01013  ? 224 LYS   A N   1 
ATOM   1637 C  CA  . LYS   A 1 217 ? -17.61835 -30.04587 -14.74712 1.000 56.71157  ? 224 LYS   A CA  1 
ATOM   1638 C  C   . LYS   A 1 217 ? -17.20145 -31.23180 -13.87596 1.000 56.24941  ? 224 LYS   A C   1 
ATOM   1639 O  O   . LYS   A 1 217 ? -17.71531 -31.41289 -12.76792 1.000 65.60000  ? 224 LYS   A O   1 
ATOM   1640 C  CB  . LYS   A 1 217 ? -17.79448 -30.46119 -16.21084 1.000 55.73545  ? 224 LYS   A CB  1 
ATOM   1641 C  CG  . LYS   A 1 217 ? -17.38778 -29.36647 -17.20937 1.000 54.12918  ? 224 LYS   A CG  1 
ATOM   1642 C  CD  . LYS   A 1 217 ? -17.94471 -29.63514 -18.61228 1.000 51.10681  ? 224 LYS   A CD  1 
ATOM   1643 C  CE  . LYS   A 1 217 ? -16.84482 -30.14302 -19.54846 1.000 39.99429  ? 224 LYS   A CE  1 
ATOM   1644 N  NZ  . LYS   A 1 217 ? -15.66133 -29.22841 -19.56563 1.000 44.96464  ? 224 LYS   A NZ  1 
HETATM 1645 C  C8  . A1AXB B 2 .   ? 10.45980  -14.25079 -26.30942 0.772 37.58906  ? 301 A1AXB A C8  1 
HETATM 1646 C  C5  . A1AXB B 2 .   ? 7.64985   -11.75909 -23.63806 0.772 30.32382  ? 301 A1AXB A C5  1 
HETATM 1647 C  C6  . A1AXB B 2 .   ? 8.58945   -12.25528 -24.51514 0.772 37.71798  ? 301 A1AXB A C6  1 
HETATM 1648 C  C2  . A1AXB B 2 .   ? 7.01421   -13.96964 -25.14672 0.772 28.82488  ? 301 A1AXB A C2  1 
HETATM 1649 C  C4  . A1AXB B 2 .   ? 6.39869   -12.33603 -23.50638 0.772 28.90078  ? 301 A1AXB A C4  1 
HETATM 1650 C  C1  . A1AXB B 2 .   ? 5.47839   -15.61660 -25.91328 0.772 27.42352  ? 301 A1AXB A C1  1 
HETATM 1651 C  C3  . A1AXB B 2 .   ? 6.08462   -13.44032 -24.26513 0.772 29.74165  ? 301 A1AXB A C3  1 
HETATM 1652 C  C7  . A1AXB B 2 .   ? 8.27946   -13.37479 -25.28041 0.772 38.29446  ? 301 A1AXB A C7  1 
HETATM 1653 N  N1  . A1AXB B 2 .   ? 9.14227   -13.98390 -26.22687 0.772 43.39456  ? 301 A1AXB A N1  1 
HETATM 1654 N  N2  . A1AXB B 2 .   ? 10.89104  -14.82840 -27.42164 0.772 49.45870  ? 301 A1AXB A N2  1 
HETATM 1655 O  O1  . A1AXB B 2 .   ? 6.78831   -15.05182 -25.94367 0.772 36.44418  ? 301 A1AXB A O1  1 
HETATM 1656 S  S1  . A1AXB B 2 .   ? 11.53183  -13.89686 -25.03792 0.772 36.37530  ? 301 A1AXB A S1  1 
HETATM 1657 CL CL1 . A1AXB B 2 .   ? 8.02195   -10.35374 -22.67518 0.772 34.95315  ? 301 A1AXB A CL1 1 
HETATM 1658 O  O   . HOH   C 3 .   ? -17.30501 -31.83815 -10.69624 1.000 63.28121  ? 401 HOH   A O   1 
HETATM 1659 O  O   . HOH   C 3 .   ? -13.00519 -22.90908 -33.92027 1.000 54.48441  ? 402 HOH   A O   1 
HETATM 1660 O  O   . HOH   C 3 .   ? -4.05436  -8.84505  -42.58212 1.000 52.25053  ? 403 HOH   A O   1 
HETATM 1661 O  O   . HOH   C 3 .   ? -1.30739  -28.51212 -5.27979  1.000 37.96777  ? 404 HOH   A O   1 
HETATM 1662 O  O   . HOH   C 3 .   ? -16.52701 -24.39715 -9.00888  1.000 51.40412  ? 405 HOH   A O   1 
HETATM 1663 O  O   . HOH   C 3 .   ? 6.28354   -25.30505 -6.56470  1.000 44.98219  ? 406 HOH   A O   1 
HETATM 1664 O  O   . HOH   C 3 .   ? 8.38606   -23.12087 -13.57948 1.000 39.80416  ? 407 HOH   A O   1 
HETATM 1665 O  O   . HOH   C 3 .   ? -2.24515  -15.05392 -42.92596 1.000 57.58196  ? 408 HOH   A O   1 
HETATM 1666 O  O   . HOH   C 3 .   ? -19.56912 -28.69769 -11.64562 1.000 59.27098  ? 409 HOH   A O   1 
HETATM 1667 O  O   . HOH   C 3 .   ? 4.91208   -25.46363 -38.01300 1.000 38.88363  ? 410 HOH   A O   1 
HETATM 1668 O  O   . HOH   C 3 .   ? 8.06924   -18.44936 -6.13790  1.000 35.44850  ? 411 HOH   A O   1 
HETATM 1669 O  O   . HOH   C 3 .   ? 10.44369  -12.44856 -29.08310 1.000 38.64629  ? 412 HOH   A O   1 
HETATM 1670 O  O   . HOH   C 3 .   ? 7.67106   -22.69909 -36.70583 1.000 42.55636  ? 413 HOH   A O   1 
HETATM 1671 O  O   . HOH   C 3 .   ? -2.48901  -5.46653  -7.17489  1.000 46.28812  ? 414 HOH   A O   1 
HETATM 1672 O  O   . HOH   C 3 .   ? -10.63956 -14.01237 0.49341   1.000 36.51875  ? 415 HOH   A O   1 
HETATM 1673 O  O   . HOH   C 3 .   ? 9.91703   -26.30466 -16.21984 1.000 38.88668  ? 416 HOH   A O   1 
HETATM 1674 O  O   . HOH   C 3 .   ? -8.18180  -4.71255  -41.85249 1.000 56.18735  ? 417 HOH   A O   1 
HETATM 1675 O  O   . HOH   C 3 .   ? 12.33764  -2.75757  -22.18331 1.000 52.42154  ? 418 HOH   A O   1 
HETATM 1676 O  O   . HOH   C 3 .   ? 1.09829   -20.39276 -4.40942  1.000 35.00882  ? 419 HOH   A O   1 
HETATM 1677 O  O   . HOH   C 3 .   ? -15.44794 -25.43866 -17.79973 1.000 32.00094  ? 420 HOH   A O   1 
HETATM 1678 O  O   . HOH   C 3 .   ? 7.76889   -27.10929 -26.70749 1.000 39.57191  ? 421 HOH   A O   1 
HETATM 1679 O  O   . HOH   C 3 .   ? -4.48012  -6.10100  -39.63382 1.000 46.69792  ? 422 HOH   A O   1 
HETATM 1680 O  O   . HOH   C 3 .   ? 2.39034   -7.98225  -16.97417 1.000 29.36690  ? 423 HOH   A O   1 
HETATM 1681 O  O   . HOH   C 3 .   ? -3.50631  -13.81542 -0.90061  1.000 45.17127  ? 424 HOH   A O   1 
HETATM 1682 O  O   . HOH   C 3 .   ? -19.69277 -14.17924 -19.22724 1.000 44.95111  ? 425 HOH   A O   1 
HETATM 1683 O  O   . HOH   C 3 .   ? 5.01891   -8.46995  -36.65449 1.000 38.42406  ? 426 HOH   A O   1 
HETATM 1684 O  O   . HOH   C 3 .   ? -4.84635  -2.29621  -20.38866 1.000 31.96744  ? 427 HOH   A O   1 
HETATM 1685 O  O   . HOH   C 3 .   ? -8.43424  -2.46443  -18.44971 1.000 28.11331  ? 428 HOH   A O   1 
HETATM 1686 O  O   . HOH   C 3 .   ? -3.30303  -20.55837 -0.62055  1.000 52.57569  ? 429 HOH   A O   1 
HETATM 1687 O  O   . HOH   C 3 .   ? 16.23183  -0.71083  -12.65362 1.000 44.55385  ? 430 HOH   A O   1 
HETATM 1688 O  O   . HOH   C 3 .   ? 8.53235   -27.97065 -23.18218 1.000 38.35001  ? 431 HOH   A O   1 
HETATM 1689 O  O   . HOH   C 3 .   ? -9.26978  -15.16247 -38.16840 1.000 42.20710  ? 432 HOH   A O   1 
HETATM 1690 O  O   . HOH   C 3 .   ? -7.25759  -27.70141 -7.22547  1.000 40.55050  ? 433 HOH   A O   1 
HETATM 1691 O  O   . HOH   C 3 .   ? 17.46228  -8.84971  -28.83799 1.000 52.19453  ? 434 HOH   A O   1 
HETATM 1692 O  O   . HOH   C 3 .   ? 10.38157  -20.70246 -6.26756  1.000 45.96927  ? 435 HOH   A O   1 
HETATM 1693 O  O   . HOH   C 3 .   ? -0.91165  -30.34537 -18.85572 1.000 56.52485  ? 436 HOH   A O   1 
HETATM 1694 O  O   . HOH   C 3 .   ? 0.73480   -5.69465  -18.95376 1.000 35.64731  ? 437 HOH   A O   1 
HETATM 1695 O  O   . HOH   C 3 .   ? 21.16444  -2.70513  -8.71856  1.000 56.64768  ? 438 HOH   A O   1 
HETATM 1696 O  O   . HOH   C 3 .   ? -7.30706  -24.87318 -18.86584 1.000 26.13506  ? 439 HOH   A O   1 
HETATM 1697 O  O   . HOH   C 3 .   ? 10.16844  -17.77196 -39.81660 1.000 54.62668  ? 440 HOH   A O   1 
HETATM 1698 O  O   . HOH   C 3 .   ? -14.97189 -3.29267  -22.58487 1.000 38.87548  ? 441 HOH   A O   1 
HETATM 1699 O  O   . HOH   C 3 .   ? -7.29011  -23.19425 -29.96826 1.000 53.14014  ? 442 HOH   A O   1 
HETATM 1700 O  O   . HOH   C 3 .   ? -6.90919  -12.82115 -36.86969 1.000 33.12863  ? 443 HOH   A O   1 
HETATM 1701 O  O   . HOH   C 3 .   ? 12.55295  -28.92130 -29.17142 1.000 34.63343  ? 444 HOH   A O   1 
HETATM 1702 O  O   . HOH   C 3 .   ? 16.95156  -5.09045  -26.53479 1.000 48.13635  ? 445 HOH   A O   1 
HETATM 1703 O  O   . HOH   C 3 .   ? 6.03127   -20.56232 0.28784   1.000 43.13618  ? 446 HOH   A O   1 
HETATM 1704 O  O   . HOH   C 3 .   ? 19.14389  -20.05745 -23.74225 1.000 40.44338  ? 447 HOH   A O   1 
HETATM 1705 O  O   . HOH   C 3 .   ? -0.53177  -14.59451 -35.58936 1.000 26.22549  ? 448 HOH   A O   1 
HETATM 1706 O  O   . HOH   C 3 .   ? -11.91036 -28.17133 -30.02247 1.000 46.53941  ? 449 HOH   A O   1 
HETATM 1707 O  O   . HOH   C 3 .   ? 2.98468   -19.73900 -2.26628  1.000 46.65934  ? 450 HOH   A O   1 
HETATM 1708 O  O   . HOH   C 3 .   ? -3.65670  -4.44788  -9.04535  1.000 47.35289  ? 451 HOH   A O   1 
HETATM 1709 O  O   . HOH   C 3 .   ? 16.58620  -26.64041 -23.91053 1.000 50.21280  ? 452 HOH   A O   1 
HETATM 1710 O  O   . HOH   C 3 .   ? 3.99542   -5.98080  -11.55637 1.000 31.94765  ? 453 HOH   A O   1 
HETATM 1711 O  O   . HOH   C 3 .   ? -15.36067 -12.86683 -20.57400 1.000 27.16343  ? 454 HOH   A O   1 
HETATM 1712 O  O   . HOH   C 3 .   ? -12.39158 -27.19090 -35.15685 1.000 47.33962  ? 455 HOH   A O   1 
HETATM 1713 O  O   . HOH   C 3 .   ? -12.54034 -7.21327  -13.04788 1.000 49.55139  ? 456 HOH   A O   1 
HETATM 1714 O  O   . HOH   C 3 .   ? -3.98590  -11.02589 -27.72196 1.000 24.81602  ? 457 HOH   A O   1 
HETATM 1715 O  O   . HOH   C 3 .   ? 11.64744  -25.61974 -22.74496 1.000 28.44229  ? 458 HOH   A O   1 
HETATM 1716 O  O   . HOH   C 3 .   ? -10.501   -0.004    -16.798   1.000 46.96434  ? 459 HOH   A O   1 
HETATM 1717 O  O   . HOH   C 3 .   ? 8.86180   -20.38028 -8.61185  1.000 38.91928  ? 460 HOH   A O   1 
HETATM 1718 O  O   . HOH   C 3 .   ? 10.10740  -17.08169 -7.27298  1.000 31.22328  ? 461 HOH   A O   1 
HETATM 1719 O  O   . HOH   C 3 .   ? -13.83394 -11.72143 -30.60768 1.000 33.06014  ? 462 HOH   A O   1 
HETATM 1720 O  O   . HOH   C 3 .   ? 17.45261  -1.70792  -19.22529 1.000 40.69096  ? 463 HOH   A O   1 
HETATM 1721 O  O   . HOH   C 3 .   ? -4.74098  -7.40968  -13.78268 1.000 25.85930  ? 464 HOH   A O   1 
HETATM 1722 O  O   . HOH   C 3 .   ? 14.00407  -15.16332 -1.36499  1.000 45.00453  ? 465 HOH   A O   1 
HETATM 1723 O  O   . HOH   C 3 .   ? -16.09589 -5.81605  -24.15619 1.000 37.10130  ? 466 HOH   A O   1 
HETATM 1724 O  O   . HOH   C 3 .   ? -7.29046  -18.70996 -36.41190 1.000 48.69511  ? 467 HOH   A O   1 
HETATM 1725 O  O   . HOH   C 3 .   ? 1.22555   -7.96622  -31.48284 1.000 38.21148  ? 468 HOH   A O   1 
HETATM 1726 O  O   . HOH   C 3 .   ? -5.82067  -27.99562 -20.95420 1.000 42.94584  ? 469 HOH   A O   1 
HETATM 1727 O  O   . HOH   C 3 .   ? -13.44520 -16.24398 -3.23896  1.000 33.69936  ? 470 HOH   A O   1 
HETATM 1728 O  O   . HOH   C 3 .   ? -4.80666  -8.64356  -34.94194 1.000 26.85185  ? 471 HOH   A O   1 
HETATM 1729 O  O   . HOH   C 3 .   ? -5.69590  -23.75101 -36.23819 1.000 44.09283  ? 472 HOH   A O   1 
HETATM 1730 O  O   . HOH   C 3 .   ? 19.17663  -11.58323 -16.73981 1.000 43.10449  ? 473 HOH   A O   1 
HETATM 1731 O  O   . HOH   C 3 .   ? -0.75486  -10.48935 -3.40151  1.000 43.37126  ? 474 HOH   A O   1 
HETATM 1732 O  O   . HOH   C 3 .   ? -18.98531 -19.13321 -14.41307 1.000 27.51523  ? 475 HOH   A O   1 
HETATM 1733 O  O   . HOH   C 3 .   ? -2.35503  -11.31072 -24.20852 1.000 30.23999  ? 476 HOH   A O   1 
HETATM 1734 O  O   . HOH   C 3 .   ? 1.39690   -5.14105  -14.52604 1.000 44.67543  ? 477 HOH   A O   1 
HETATM 1735 O  O   . HOH   C 3 .   ? 13.09598  -28.29314 -33.59178 1.000 32.54523  ? 478 HOH   A O   1 
HETATM 1736 O  O   . HOH   C 3 .   ? 7.40702   -29.75044 -19.12574 1.000 39.82438  ? 479 HOH   A O   1 
HETATM 1737 O  O   . HOH   C 3 .   ? 1.46802   -5.43904  -22.51104 1.000 43.53609  ? 480 HOH   A O   1 
HETATM 1738 O  O   . HOH   C 3 .   ? -13.57471 -21.99613 -11.46427 1.000 36.26911  ? 481 HOH   A O   1 
HETATM 1739 O  O   . HOH   C 3 .   ? 19.19062  -16.39429 -12.71450 1.000 36.39164  ? 482 HOH   A O   1 
HETATM 1740 O  O   . HOH   C 3 .   ? 7.23430   1.21145   -16.42276 1.000 42.72213  ? 483 HOH   A O   1 
HETATM 1741 O  O   . HOH   C 3 .   ? 5.37771   -24.85077 -30.01112 1.000 28.39639  ? 484 HOH   A O   1 
HETATM 1742 O  O   . HOH   C 3 .   ? -17.76179 -11.13763 -24.67840 1.000 35.20483  ? 485 HOH   A O   1 
HETATM 1743 O  O   . HOH   C 3 .   ? -5.94810  0.78441   -37.50987 1.000 36.33360  ? 486 HOH   A O   1 
HETATM 1744 O  O   . HOH   C 3 .   ? -0.18668  -6.82499  -26.59215 1.000 39.82472  ? 487 HOH   A O   1 
HETATM 1745 O  O   . HOH   C 3 .   ? -10.04345 -10.73386 -2.71745  1.000 30.17277  ? 488 HOH   A O   1 
HETATM 1746 O  O   . HOH   C 3 .   ? -11.76709 -0.94546  -21.47586 1.000 38.06885  ? 489 HOH   A O   1 
HETATM 1747 O  O   . HOH   C 3 .   ? -5.72101  -11.01791 -10.55504 1.000 34.73415  ? 490 HOH   A O   1 
HETATM 1748 O  O   . HOH   C 3 .   ? -9.02268  -0.72983  -20.78432 1.000 34.28060  ? 491 HOH   A O   1 
HETATM 1749 O  O   . HOH   C 3 .   ? -8.01546  1.26110   -26.63903 1.000 33.44097  ? 492 HOH   A O   1 
HETATM 1750 O  O   . HOH   C 3 .   ? 10.47379  -3.97262  -21.28724 1.000 48.83217  ? 493 HOH   A O   1 
HETATM 1751 O  O   . HOH   C 3 .   ? 14.65676  -20.71726 -19.97429 1.000 26.88156  ? 494 HOH   A O   1 
HETATM 1752 O  O   . HOH   C 3 .   ? -16.24616 -4.38988  -30.50115 1.000 46.77931  ? 495 HOH   A O   1 
HETATM 1753 O  O   . HOH   C 3 .   ? 5.49675   -12.61093 -38.49573 1.000 31.52288  ? 496 HOH   A O   1 
HETATM 1754 O  O   . HOH   C 3 .   ? -0.06721  -7.54065  -24.08602 1.000 34.79226  ? 497 HOH   A O   1 
HETATM 1755 O  O   . HOH   C 3 .   ? -5.11194  -31.00549 -10.98053 1.000 42.57653  ? 498 HOH   A O   1 
HETATM 1756 O  O   . HOH   C 3 .   ? -4.04914  -14.47453 -22.87121 1.000 25.43742  ? 499 HOH   A O   1 
HETATM 1757 O  O   . HOH   C 3 .   ? -1.13208  -11.17720 -26.76706 1.000 41.49122  ? 500 HOH   A O   1 
HETATM 1758 O  O   . HOH   C 3 .   ? 11.91185  -26.09924 -25.82740 1.000 35.73131  ? 501 HOH   A O   1 
HETATM 1759 O  O   . HOH   C 3 .   ? 0.07053   -27.03072 -31.75717 1.000 52.49599  ? 502 HOH   A O   1 
HETATM 1760 O  O   . HOH   C 3 .   ? 4.98728   -9.36360  -20.23388 1.000 27.53664  ? 503 HOH   A O   1 
HETATM 1761 O  O   . HOH   C 3 .   ? 0.25673   -5.34346  -34.42397 1.000 43.54087  ? 504 HOH   A O   1 
HETATM 1762 O  O   . HOH   C 3 .   ? -6.64485  -24.61107 -22.92961 1.000 36.13456  ? 505 HOH   A O   1 
HETATM 1763 O  O   . HOH   C 3 .   ? -1.38162  -31.95219 -6.54520  1.000 51.90492  ? 506 HOH   A O   1 
HETATM 1764 O  O   . HOH   C 3 .   ? 16.38548  -20.62223 -17.92031 1.000 33.22407  ? 507 HOH   A O   1 
HETATM 1765 O  O   . HOH   C 3 .   ? -13.82666 -6.91273  -15.35830 1.000 41.54909  ? 508 HOH   A O   1 
HETATM 1766 O  O   . HOH   C 3 .   ? -6.16149  -13.26769 0.70284   1.000 41.17446  ? 509 HOH   A O   1 
HETATM 1767 O  O   . HOH   C 3 .   ? 21.003    -17.177   -26.824   1.000 52.03647  ? 510 HOH   A O   1 
HETATM 1768 O  O   . HOH   C 3 .   ? -12.90862 -26.49513 -17.78629 1.000 31.34159  ? 511 HOH   A O   1 
HETATM 1769 O  O   . HOH   C 3 .   ? 10.48367  -20.93307 -40.77350 1.000 57.76180  ? 512 HOH   A O   1 
HETATM 1770 O  O   . HOH   C 3 .   ? 4.59436   -6.93647  -18.22339 1.000 26.61746  ? 513 HOH   A O   1 
HETATM 1771 O  O   . HOH   C 3 .   ? 1.28512   -29.67478 -15.29115 1.000 42.97178  ? 514 HOH   A O   1 
HETATM 1772 O  O   . HOH   C 3 .   ? 13.11148  -27.67023 -18.89261 1.000 47.62084  ? 515 HOH   A O   1 
HETATM 1773 O  O   . HOH   C 3 .   ? -9.00223  -15.65663 -28.64383 1.000 34.65191  ? 516 HOH   A O   1 
HETATM 1774 O  O   . HOH   C 3 .   ? -1.56052  -24.92372 -4.32285  1.000 30.87741  ? 517 HOH   A O   1 
HETATM 1775 O  O   . HOH   C 3 .   ? -7.79747  -3.54325  -11.36414 1.000 45.17092  ? 518 HOH   A O   1 
HETATM 1776 O  O   . HOH   C 3 .   ? -17.04604 -18.16760 -11.61942 1.000 43.99810  ? 519 HOH   A O   1 
HETATM 1777 O  O   . HOH   C 3 .   ? -13.87437 -15.00035 -33.68192 1.000 57.87799  ? 520 HOH   A O   1 
HETATM 1778 O  O   . HOH   C 3 .   ? -13.00760 -16.57098 -26.41593 1.000 31.72296  ? 521 HOH   A O   1 
HETATM 1779 O  O   . HOH   C 3 .   ? 6.73945   2.19189   -13.70300 1.000 45.21717  ? 522 HOH   A O   1 
HETATM 1780 O  O   . HOH   C 3 .   ? -4.11308  -19.66017 -39.14179 1.000 41.08069  ? 523 HOH   A O   1 
HETATM 1781 O  O   . HOH   C 3 .   ? -0.29089  -30.04717 -16.63211 1.000 45.37224  ? 524 HOH   A O   1 
HETATM 1782 O  O   . HOH   C 3 .   ? 18.239    -25.344   -23.995   1.000 46.37035  ? 525 HOH   A O   1 
HETATM 1783 O  O   . HOH   C 3 .   ? -13.65967 -12.00891 -8.62184  1.000 42.81499  ? 526 HOH   A O   1 
HETATM 1784 O  O   . HOH   C 3 .   ? 11.05467  -8.02693  -36.77878 1.000 49.42698  ? 527 HOH   A O   1 
HETATM 1785 O  O   . HOH   C 3 .   ? -2.37282  -13.21078 -20.98359 1.000 30.33229  ? 528 HOH   A O   1 
HETATM 1786 O  O   . HOH   C 3 .   ? 6.18834   -20.63709 -40.00248 1.000 46.42502  ? 529 HOH   A O   1 
HETATM 1787 O  O   . HOH   C 3 .   ? -14.95511 1.27865   -29.03784 1.000 53.71652  ? 530 HOH   A O   1 
HETATM 1788 O  O   . HOH   C 3 .   ? 8.95631   -20.00552 -3.72608  1.000 36.53405  ? 531 HOH   A O   1 
HETATM 1789 O  O   . HOH   C 3 .   ? 4.13893   -22.08876 -3.13362  1.000 45.13370  ? 532 HOH   A O   1 
HETATM 1790 O  O   . HOH   C 3 .   ? -17.86263 -11.49756 -33.70783 1.000 51.55363  ? 533 HOH   A O   1 
HETATM 1791 O  O   . HOH   C 3 .   ? 5.40107   -30.28625 -10.84891 1.000 42.61476  ? 534 HOH   A O   1 
HETATM 1792 O  O   . HOH   C 3 .   ? -12.80952 -24.53117 -10.75818 1.000 49.14236  ? 535 HOH   A O   1 
HETATM 1793 O  O   . HOH   C 3 .   ? 8.10247   -23.19546 -6.68782  1.000 45.26707  ? 536 HOH   A O   1 
HETATM 1794 O  O   . HOH   C 3 .   ? -4.61081  -5.01867  -12.80092 1.000 50.15600  ? 537 HOH   A O   1 
HETATM 1795 O  O   . HOH   C 3 .   ? -2.94916  0.08711   -23.02475 1.000 47.22341  ? 538 HOH   A O   1 
HETATM 1796 O  O   . HOH   C 3 .   ? -13.37716 -25.10714 -7.68938  1.000 42.70708  ? 539 HOH   A O   1 
HETATM 1797 O  O   . HOH   C 3 .   ? -13.260   -0.666    -15.611   1.000 53.10264  ? 540 HOH   A O   1 
HETATM 1798 O  O   . HOH   C 3 .   ? 22.10882  -14.72063 -25.90033 1.000 44.19518  ? 541 HOH   A O   1 
HETATM 1799 O  O   . HOH   C 3 .   ? -3.09871  -32.54478 -10.25193 1.000 58.78037  ? 542 HOH   A O   1 
HETATM 1800 O  O   . HOH   C 3 .   ? -11.62787 -13.05220 -31.62113 1.000 32.05967  ? 543 HOH   A O   1 
HETATM 1801 O  O   . HOH   C 3 .   ? -17.26956 -14.89812 -13.86353 1.000 36.69209  ? 544 HOH   A O   1 
HETATM 1802 O  O   . HOH   C 3 .   ? 0.09582   -16.12265 -3.48802  1.000 31.49231  ? 545 HOH   A O   1 
HETATM 1803 O  O   . HOH   C 3 .   ? -8.11874  -4.52475  -7.89980  1.000 44.11552  ? 546 HOH   A O   1 
HETATM 1804 O  O   . HOH   C 3 .   ? 3.30715   -26.62221 -28.98698 1.000 49.53373  ? 547 HOH   A O   1 
HETATM 1805 O  O   . HOH   C 3 .   ? -12.70977 -19.07825 -24.63188 1.000 27.84072  ? 548 HOH   A O   1 
HETATM 1806 O  O   . HOH   C 3 .   ? -15.35567 -8.57081  -15.15177 1.000 39.35355  ? 549 HOH   A O   1 
HETATM 1807 O  O   . HOH   C 3 .   ? -17.24591 -6.77736  -26.47474 1.000 46.09561  ? 550 HOH   A O   1 
HETATM 1808 O  O   . HOH   C 3 .   ? -14.06343 -28.90391 -16.96608 1.000 48.63829  ? 551 HOH   A O   1 
HETATM 1809 O  O   . HOH   C 3 .   ? 11.36811  -10.62388 -4.25640  1.000 44.31443  ? 552 HOH   A O   1 
HETATM 1810 O  O   . HOH   C 3 .   ? -0.60460  -9.17933  -28.12381 1.000 42.81478  ? 553 HOH   A O   1 
HETATM 1811 O  O   . HOH   C 3 .   ? 1.73184   -7.08086  -38.82305 1.000 50.44665  ? 554 HOH   A O   1 
HETATM 1812 O  O   . HOH   C 3 .   ? 0.39444   -12.73125 -21.50509 1.000 33.72029  ? 555 HOH   A O   1 
HETATM 1813 O  O   . HOH   C 3 .   ? 12.16205  -19.04334 -38.20688 1.000 50.85168  ? 556 HOH   A O   1 
HETATM 1814 O  O   . HOH   C 3 .   ? -2.01821  -14.62962 -0.28152  1.000 55.23403  ? 557 HOH   A O   1 
HETATM 1815 O  O   . HOH   C 3 .   ? -14.72182 -12.16490 -12.62250 1.000 53.21620  ? 558 HOH   A O   1 
HETATM 1816 O  O   . HOH   C 3 .   ? 16.01440  -17.89767 -2.82786  1.000 42.68602  ? 559 HOH   A O   1 
HETATM 1817 O  O   . HOH   C 3 .   ? -11.48558 -26.97454 -20.18675 1.000 33.52351  ? 560 HOH   A O   1 
HETATM 1818 O  O   . HOH   C 3 .   ? 8.22488   -7.63364  -24.54973 1.000 48.55590  ? 561 HOH   A O   1 
HETATM 1819 O  O   . HOH   C 3 .   ? -14.85462 -24.82467 -10.57413 1.000 51.65508  ? 562 HOH   A O   1 
HETATM 1820 O  O   . HOH   C 3 .   ? 15.45411  -22.77488 -16.36334 1.000 38.69288  ? 563 HOH   A O   1 
HETATM 1821 O  O   . HOH   C 3 .   ? 14.58705  -14.34394 -26.01250 1.000 25.40056  ? 564 HOH   A O   1 
HETATM 1822 O  O   . HOH   C 3 .   ? 13.11203  -7.15555  -33.25637 1.000 51.06575  ? 565 HOH   A O   1 
HETATM 1823 O  O   . HOH   C 3 .   ? -4.80427  -6.09823  -36.49752 1.000 29.17045  ? 566 HOH   A O   1 
HETATM 1824 O  O   . HOH   C 3 .   ? 1.43287   -7.96683  -4.43230  1.000 44.56818  ? 567 HOH   A O   1 
HETATM 1825 O  O   . HOH   C 3 .   ? 1.63004   -17.47600 0.16364   1.000 49.48622  ? 568 HOH   A O   1 
HETATM 1826 O  O   . HOH   C 3 .   ? 3.66770   -6.22910  -20.76290 1.000 50.26739  ? 569 HOH   A O   1 
HETATM 1827 O  O   . HOH   C 3 .   ? 9.45723   -26.35035 -25.12137 1.000 43.39614  ? 570 HOH   A O   1 
HETATM 1828 O  O   . HOH   C 3 .   ? 5.99182   -22.06897 -38.52345 1.000 51.92721  ? 571 HOH   A O   1 
HETATM 1829 O  O   . HOH   C 3 .   ? -14.54933 -1.81847  -24.87412 1.000 52.14750  ? 572 HOH   A O   1 
HETATM 1830 O  O   . HOH   C 3 .   ? -3.14412  -26.99758 -29.43359 1.000 58.23110  ? 573 HOH   A O   1 
HETATM 1831 O  O   . HOH   C 3 .   ? 18.54824  -21.93064 -19.00506 1.000 39.24908  ? 574 HOH   A O   1 
HETATM 1832 O  O   . HOH   C 3 .   ? 1.89411   -4.31921  -16.89655 1.000 43.88935  ? 575 HOH   A O   1 
HETATM 1833 O  O   . HOH   C 3 .   ? -15.81877 -1.72716  -27.20873 1.000 56.21916  ? 576 HOH   A O   1 
HETATM 1834 O  O   . HOH   C 3 .   ? -15.363   -0.432    -19.439   1.000 50.84927  ? 577 HOH   A O   1 
HETATM 1835 O  O   . HOH   C 3 .   ? 7.17822   -30.26246 -24.13863 1.000 56.36802  ? 578 HOH   A O   1 
HETATM 1836 O  O   . HOH   C 3 .   ? -13.63143 -13.64271 -3.53703  1.000 44.69151  ? 579 HOH   A O   1 
HETATM 1837 O  O   . HOH   C 3 .   ? -1.27104  -27.32871 -24.46441 1.000 43.99663  ? 580 HOH   A O   1 
HETATM 1838 O  O   . HOH   C 3 .   ? 13.689    -26.580   -37.331   1.000 43.78973  ? 581 HOH   A O   1 
HETATM 1839 O  O   . HOH   C 3 .   ? 18.79404  -18.50320 -10.60667 1.000 46.43812  ? 582 HOH   A O   1 
HETATM 1840 O  O   . HOH   C 3 .   ? -10.605   -22.118   3.755     1.000 53.75927  ? 583 HOH   A O   1 
HETATM 1841 O  O   . HOH   C 3 .   ? 9.130     -1.387    -19.683   1.000 51.42970  ? 584 HOH   A O   1 
HETATM 1842 O  O   . HOH   C 3 .   ? 13.24726  -0.98940  -20.15253 1.000 42.40298  ? 585 HOH   A O   1 
HETATM 1843 O  O   . HOH   C 3 .   ? 3.38286   -3.38300  -10.48427 1.000 50.96976  ? 586 HOH   A O   1 
HETATM 1844 O  O   . HOH   C 3 .   ? -1.08862  -5.03911  -12.90811 1.000 48.60013  ? 587 HOH   A O   1 
HETATM 1845 O  O   . HOH   C 3 .   ? -4.08603  2.30468   -35.95444 1.000 55.94823  ? 588 HOH   A O   1 
HETATM 1846 O  O   . HOH   C 3 .   ? 2.685     -1.414    -28.813   1.000 50.73428  ? 589 HOH   A O   1 
HETATM 1847 O  O   . HOH   C 3 .   ? -18.21567 -33.61643 -9.62436  1.000 60.97350  ? 590 HOH   A O   1 
HETATM 1848 O  O   . HOH   C 3 .   ? 9.85538   -14.68504 -38.01255 1.000 50.26764  ? 591 HOH   A O   1 
HETATM 1849 O  O   . HOH   C 3 .   ? -3.69152  1.25586   -26.79735 1.000 52.97313  ? 592 HOH   A O   1 
HETATM 1850 O  O   . HOH   C 3 .   ? -11.12440 -17.12823 -28.39937 1.000 41.28161  ? 593 HOH   A O   1 
HETATM 1851 O  O   . HOH   C 3 .   ? -9.01151  -26.06941 -20.64163 1.000 39.16854  ? 594 HOH   A O   1 
HETATM 1852 O  O   . HOH   C 3 .   ? -13.95638 -9.55497  -9.35970  1.000 44.94897  ? 595 HOH   A O   1 
HETATM 1853 O  O   . HOH   C 3 .   ? -17.73634 -11.84148 -21.99908 1.000 33.53630  ? 596 HOH   A O   1 
HETATM 1854 O  O   . HOH   C 3 .   ? -15.482   -1.778    -16.844   1.000 48.56160  ? 597 HOH   A O   1 
HETATM 1855 O  O   . HOH   C 3 .   ? -11.18466 -21.12041 -25.36058 1.000 53.53989  ? 598 HOH   A O   1 
HETATM 1856 O  O   . HOH   C 3 .   ? 4.94138   -10.39763 -39.44749 1.000 48.25311  ? 599 HOH   A O   1 
HETATM 1857 O  O   . HOH   C 3 .   ? -10.22124 -7.92847  -2.15523  1.000 48.08634  ? 600 HOH   A O   1 
HETATM 1858 O  O   . HOH   C 3 .   ? 7.71765   -13.74513 -39.76916 1.000 43.02564  ? 601 HOH   A O   1 
HETATM 1859 O  O   . HOH   C 3 .   ? 6.92225   -21.07494 -2.28486  1.000 42.83867  ? 602 HOH   A O   1 
HETATM 1860 O  O   . HOH   C 3 .   ? 12.42901  -28.36377 -22.32992 1.000 49.94944  ? 603 HOH   A O   1 
HETATM 1861 O  O   . HOH   C 3 .   ? 0.65734   -11.60602 -23.98547 1.000 53.06541  ? 604 HOH   A O   1 
HETATM 1862 O  O   . HOH   C 3 .   ? -8.67339  -10.77471 -0.42546  1.000 52.70966  ? 605 HOH   A O   1 
HETATM 1863 O  O   . HOH   C 3 .   ? -12.06210 -14.91201 -38.83730 1.000 57.48438  ? 606 HOH   A O   1 
HETATM 1864 O  O   . HOH   C 3 .   ? 10.20173  -25.41783 -13.94199 1.000 50.73593  ? 607 HOH   A O   1 
HETATM 1865 O  O   . HOH   C 3 .   ? 9.04257   -29.61690 -27.10522 1.000 51.70140  ? 608 HOH   A O   1 
HETATM 1866 O  O   . HOH   C 3 .   ? 14.77641  0.83421   -13.30552 1.000 52.95433  ? 609 HOH   A O   1 
HETATM 1867 O  O   . HOH   C 3 .   ? 0.77358   -27.28740 -29.89072 1.000 54.05074  ? 610 HOH   A O   1 
HETATM 1868 O  O   . HOH   C 3 .   ? 12.11345  -1.10721  -18.05513 1.000 39.16614  ? 611 HOH   A O   1 
HETATM 1869 O  O   . HOH   C 3 .   ? -6.55282  -30.40896 -8.62447  1.000 44.99461  ? 612 HOH   A O   1 
HETATM 1870 O  O   . HOH   C 3 .   ? 10.02263  -30.42966 -29.52966 1.000 61.47847  ? 613 HOH   A O   1 
HETATM 1871 O  O   . HOH   C 3 .   ? 21.970    -18.725   -21.317   1.000 55.33210  ? 614 HOH   A O   1 
HETATM 1872 O  O   . HOH   C 3 .   ? -12.34604 -12.09926 -2.02126  1.000 48.80029  ? 615 HOH   A O   1 
HETATM 1873 O  O   . HOH   C 3 .   ? -14.994   -21.279   -32.149   1.000 54.38284  ? 616 HOH   A O   1 
HETATM 1874 O  O   . HOH   C 3 .   ? -15.72832 -11.89435 -7.08288  1.000 55.34985  ? 617 HOH   A O   1 
HETATM 1875 O  O   . HOH   C 3 .   ? 18.11122  -6.10580  -28.43683 1.000 55.65578  ? 618 HOH   A O   1 
HETATM 1876 O  O   . HOH   C 3 .   ? 11.94323  -28.64829 -26.63379 1.000 49.82065  ? 619 HOH   A O   1 
HETATM 1877 O  O   . HOH   C 3 .   ? -3.28929  -28.43168 -22.84902 1.000 53.34548  ? 620 HOH   A O   1 
HETATM 1878 O  O   . HOH   C 3 .   ? 14.41107  -10.93109 -4.98369  1.000 53.66268  ? 621 HOH   A O   1 
HETATM 1879 O  O   . HOH   C 3 .   ? -19.91541 -12.15352 -25.26070 1.000 48.95493  ? 622 HOH   A O   1 
HETATM 1880 O  O   . HOH   C 3 .   ? -7.028    -22.523   -1.973    1.000 52.46334  ? 623 HOH   A O   1 
HETATM 1881 O  O   . HOH   C 3 .   ? -18.47008 -6.02949  -23.09976 1.000 53.56423  ? 624 HOH   A O   1 
HETATM 1882 O  O   . HOH   C 3 .   ? 20.50720  -21.12139 -21.27009 1.000 49.98099  ? 625 HOH   A O   1 
HETATM 1883 O  O   . HOH   C 3 .   ? -10.67264 -11.13733 1.44471   1.000 55.92638  ? 626 HOH   A O   1 
HETATM 1884 O  O   . HOH   C 3 .   ? -15.89235 -17.27694 -2.87014  1.000 56.34292  ? 627 HOH   A O   1 
HETATM 1885 O  O   . HOH   C 3 .   ? -13.90376 -13.67697 -11.18789 1.000 41.76257  ? 628 HOH   A O   1 
HETATM 1886 O  O   . HOH   C 3 .   ? -14.27732 -9.16911  -11.88822 1.000 55.28406  ? 629 HOH   A O   1 
HETATM 1887 O  O   . HOH   C 3 .   ? 1.61470   -13.46452 -24.10894 1.000 49.72553  ? 630 HOH   A O   1 
HETATM 1888 O  O   . HOH   C 3 .   ? -2.19668  -26.96498 -27.07904 1.000 51.31300  ? 631 HOH   A O   1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N N   . GLU A 9   ? 0.64074 0.77114 0.65353 -0.02971 -0.01756 -0.26069 16  GLU A N   
2    C CA  . GLU A 9   ? 0.66179 0.77503 0.65882 -0.00903 -0.01564 -0.23694 16  GLU A CA  
3    C C   . GLU A 9   ? 0.57705 0.68232 0.58153 -0.00353 -0.01491 -0.20916 16  GLU A C   
4    O O   . GLU A 9   ? 0.49371 0.62719 0.50386 0.00119  -0.02344 -0.20088 16  GLU A O   
5    C CB  . GLU A 9   ? 0.77849 0.92664 0.76023 0.00850  -0.02565 -0.23745 16  GLU A CB  
6    C CG  . GLU A 9   ? 0.86580 0.99937 0.83067 0.02679  -0.02125 -0.21774 16  GLU A CG  
7    C CD  . GLU A 9   ? 1.08142 1.22766 1.04433 0.03962  -0.02517 -0.19049 16  GLU A CD  
8    O OE1 . GLU A 9   ? 1.03148 1.18524 1.00640 0.03532  -0.02924 -0.18291 16  GLU A OE1 
9    O OE2 . GLU A 9   ? 1.05641 1.20407 1.00483 0.05345  -0.02295 -0.17727 16  GLU A OE2 
10   N N   . VAL A 10  ? 0.44155 0.50844 0.44419 -0.00257 -0.00469 -0.19555 17  VAL A N   
11   C CA  . VAL A 10  ? 0.34424 0.40124 0.35437 -0.00044 -0.00307 -0.17315 17  VAL A CA  
12   C C   . VAL A 10  ? 0.38452 0.43877 0.38454 0.01619  -0.00274 -0.15279 17  VAL A C   
13   O O   . VAL A 10  ? 0.44136 0.48011 0.43126 0.02358  0.00325  -0.15306 17  VAL A O   
14   C CB  . VAL A 10  ? 0.55861 0.57823 0.57416 -0.01201 0.00845  -0.17317 17  VAL A CB  
15   C CG1 . VAL A 10  ? 0.43065 0.44331 0.45167 -0.00800 0.00928  -0.15090 17  VAL A CG1 
16   C CG2 . VAL A 10  ? 0.61963 0.64330 0.64663 -0.03282 0.01056  -0.19480 17  VAL A CG2 
17   N N   . GLU A 11  ? 0.32498 0.39513 0.32730 0.02178  -0.00833 -0.13649 18  GLU A N   
18   C CA  . GLU A 11  ? 0.31112 0.37971 0.30701 0.03241  -0.00653 -0.11763 18  GLU A CA  
19   C C   . GLU A 11  ? 0.27542 0.32754 0.27983 0.02936  -0.00291 -0.10367 18  GLU A C   
20   O O   . GLU A 11  ? 0.27448 0.32608 0.28756 0.02248  -0.00524 -0.10199 18  GLU A O   
21   C CB  . GLU A 11  ? 0.30354 0.39500 0.29185 0.03996  -0.01282 -0.10861 18  GLU A CB  
22   C CG  . GLU A 11  ? 0.35529 0.46604 0.33045 0.04731  -0.01632 -0.11941 18  GLU A CG  
23   C CD  . GLU A 11  ? 0.49725 0.62538 0.45972 0.05751  -0.02064 -0.10744 18  GLU A CD  
24   O OE1 . GLU A 11  ? 0.52032 0.65603 0.48508 0.05821  -0.02623 -0.10407 18  GLU A OE1 
25   O OE2 . GLU A 11  ? 0.54913 0.68210 0.49734 0.06608  -0.01718 -0.10092 18  GLU A OE2 
26   N N   . THR A 12  ? 0.27791 0.32099 0.27953 0.03588  0.00249  -0.09427 19  THR A N   
27   C CA  . THR A 12  ? 0.26389 0.29659 0.27183 0.03522  0.00502  -0.08198 19  THR A CA  
28   C C   . THR A 12  ? 0.25940 0.30828 0.26732 0.03885  0.00350  -0.06817 19  THR A C   
29   O O   . THR A 12  ? 0.27817 0.33919 0.28049 0.04509  0.00555  -0.06659 19  THR A O   
30   C CB  . THR A 12  ? 0.33220 0.34361 0.33674 0.04113  0.01285  -0.08304 19  THR A CB  
31   O OG1 . THR A 12  ? 0.33380 0.32363 0.33597 0.03463  0.01703  -0.09711 19  THR A OG1 
32   C CG2 . THR A 12  ? 0.33072 0.33538 0.33972 0.04277  0.01439  -0.07045 19  THR A CG2 
33   N N   . PHE A 13  ? 0.26852 0.31716 0.28228 0.03370  0.00113  -0.05940 20  PHE A N   
34   C CA  . PHE A 13  ? 0.28006 0.34008 0.29408 0.03215  0.00062  -0.04836 20  PHE A CA  
35   C C   . PHE A 13  ? 0.30413 0.36255 0.32534 0.03034  0.00142  -0.04211 20  PHE A C   
36   O O   . PHE A 13  ? 0.27905 0.32479 0.30316 0.02950  0.00101  -0.04356 20  PHE A O   
37   C CB  . PHE A 13  ? 0.25325 0.31285 0.26343 0.02788  -0.00335 -0.04520 20  PHE A CB  
38   C CG  . PHE A 13  ? 0.27805 0.34393 0.27923 0.03245  -0.00579 -0.05100 20  PHE A CG  
39   C CD1 . PHE A 13  ? 0.29308 0.35937 0.29687 0.03226  -0.00970 -0.06262 20  PHE A CD1 
40   C CD2 . PHE A 13  ? 0.31214 0.38643 0.30167 0.03664  -0.00360 -0.04562 20  PHE A CD2 
41   C CE1 . PHE A 13  ? 0.27837 0.35766 0.27398 0.03743  -0.01351 -0.07008 20  PHE A CE1 
42   C CE2 . PHE A 13  ? 0.32031 0.40310 0.29821 0.04378  -0.00650 -0.05061 20  PHE A CE2 
43   C CZ  . PHE A 13  ? 0.30169 0.38928 0.28296 0.04489  -0.01250 -0.06367 20  PHE A CZ  
44   N N   . ALA A 14  ? 0.24768 0.32165 0.27144 0.02914  0.00305  -0.03577 21  ALA A N   
45   C CA  . ALA A 14  ? 0.25487 0.33506 0.28555 0.02632  0.00211  -0.03142 21  ALA A CA  
46   C C   . ALA A 14  ? 0.28449 0.35804 0.31470 0.01534  -0.00044 -0.02828 21  ALA A C   
47   O O   . ALA A 14  ? 0.31452 0.38658 0.33924 0.00997  0.00101  -0.02577 21  ALA A O   
48   C CB  . ALA A 14  ? 0.27576 0.38292 0.31200 0.02847  0.00499  -0.02912 21  ALA A CB  
49   N N   . PHE A 15  ? 0.27371 0.34024 0.30657 0.01351  -0.00316 -0.02798 22  PHE A N   
50   C CA  . PHE A 15  ? 0.26257 0.32394 0.29409 0.00375  -0.00471 -0.02598 22  PHE A CA  
51   C C   . PHE A 15  ? 0.28284 0.36201 0.31817 -0.00506 -0.00232 -0.02453 22  PHE A C   
52   O O   . PHE A 15  ? 0.34524 0.44795 0.38804 -0.00198 -0.00155 -0.02536 22  PHE A O   
53   C CB  . PHE A 15  ? 0.27239 0.32727 0.30541 0.00414  -0.00767 -0.02679 22  PHE A CB  
54   C CG  . PHE A 15  ? 0.28758 0.32569 0.31811 0.00781  -0.00836 -0.02864 22  PHE A CG  
55   C CD1 . PHE A 15  ? 0.29681 0.32421 0.32301 0.00539  -0.00960 -0.02935 22  PHE A CD1 
56   C CD2 . PHE A 15  ? 0.25496 0.28853 0.28677 0.01404  -0.00665 -0.02968 22  PHE A CD2 
57   C CE1 . PHE A 15  ? 0.29633 0.31720 0.32370 0.00816  -0.01019 -0.03280 22  PHE A CE1 
58   C CE2 . PHE A 15  ? 0.27804 0.29888 0.30978 0.01368  -0.00538 -0.03275 22  PHE A CE2 
59   C CZ  . PHE A 15  ? 0.27379 0.29259 0.30544 0.01013  -0.00771 -0.03513 22  PHE A CZ  
60   N N   . GLN A 16  ? 0.30129 0.36936 0.33100 -0.01609 -0.00024 -0.02291 23  GLN A N   
61   C CA  . GLN A 16  ? 0.33667 0.41924 0.37137 -0.03001 0.00282  -0.02419 23  GLN A CA  
62   C C   . GLN A 16  ? 0.34514 0.44575 0.38902 -0.03031 -0.00245 -0.02917 23  GLN A C   
63   O O   . GLN A 16  ? 0.33787 0.42688 0.37890 -0.02337 -0.00702 -0.02988 23  GLN A O   
64   C CB  . GLN A 16  ? 0.38502 0.44104 0.40803 -0.04216 0.00719  -0.02236 23  GLN A CB  
65   C CG  . GLN A 16  ? 0.47176 0.51141 0.48176 -0.04076 0.01362  -0.01567 23  GLN A CG  
66   C CD  . GLN A 16  ? 0.63767 0.64145 0.63051 -0.04617 0.01772  -0.01236 23  GLN A CD  
67   O OE1 . GLN A 16  ? 0.56831 0.55986 0.55381 -0.06084 0.02675  -0.01027 23  GLN A OE1 
68   N NE2 . GLN A 16  ? 0.56123 0.54710 0.54712 -0.03471 0.01226  -0.01241 23  GLN A NE2 
69   N N   . ALA A 17  ? 0.33876 0.47190 0.39351 -0.03790 -0.00146 -0.03292 24  ALA A N   
70   C CA  . ALA A 17  ? 0.36502 0.52401 0.42771 -0.03511 -0.00758 -0.03821 24  ALA A CA  
71   C C   . ALA A 17  ? 0.34737 0.48663 0.40317 -0.04170 -0.01119 -0.04189 24  ALA A C   
72   O O   . ALA A 17  ? 0.33118 0.47481 0.38545 -0.03114 -0.01681 -0.04276 24  ALA A O   
73   C CB  . ALA A 17  ? 0.33364 0.53712 0.41077 -0.04587 -0.00607 -0.04428 24  ALA A CB  
74   N N   . GLU A 18  ? 0.34235 0.45595 0.39069 -0.05724 -0.00683 -0.04331 25  GLU A N   
75   C CA  . GLU A 18  ? 0.35896 0.45298 0.39919 -0.06329 -0.00936 -0.04845 25  GLU A CA  
76   C C   . GLU A 18  ? 0.35321 0.42349 0.38463 -0.04718 -0.01275 -0.04380 25  GLU A C   
77   O O   . GLU A 18  ? 0.36785 0.43825 0.39626 -0.04375 -0.01713 -0.04751 25  GLU A O   
78   C CB  . GLU A 18  ? 0.44680 0.51075 0.47689 -0.08137 -0.00171 -0.05025 25  GLU A CB  
79   C CG  . GLU A 18  ? 0.54801 0.63322 0.58687 -0.10410 0.00398  -0.05749 25  GLU A CG  
80   C CD  . GLU A 18  ? 0.65066 0.75317 0.69684 -0.10545 0.01047  -0.05126 25  GLU A CD  
81   O OE1 . GLU A 18  ? 0.43962 0.53033 0.48038 -0.08919 0.01084  -0.04148 25  GLU A OE1 
82   O OE2 . GLU A 18  ? 0.63534 0.76545 0.69286 -0.12382 0.01573  -0.05741 25  GLU A OE2 
83   N N   . ILE A 19  ? 0.31091 0.36356 0.33813 -0.03808 -0.01034 -0.03675 26  ILE A N   
84   C CA  . ILE A 19  ? 0.32834 0.36445 0.35060 -0.02540 -0.01251 -0.03406 26  ILE A CA  
85   C C   . ILE A 19  ? 0.35803 0.41031 0.38599 -0.01411 -0.01545 -0.03309 26  ILE A C   
86   O O   . ILE A 19  ? 0.31096 0.35546 0.33517 -0.00809 -0.01676 -0.03301 26  ILE A O   
87   C CB  . ILE A 19  ? 0.34650 0.36709 0.36417 -0.01971 -0.00986 -0.02942 26  ILE A CB  
88   C CG1 . ILE A 19  ? 0.46270 0.46197 0.46886 -0.02728 -0.00550 -0.02784 26  ILE A CG1 
89   C CG2 . ILE A 19  ? 0.35009 0.36212 0.36689 -0.00912 -0.01183 -0.02925 26  ILE A CG2 
90   C CD1 . ILE A 19  ? 0.58345 0.55982 0.57928 -0.02574 -0.00602 -0.02972 26  ILE A CD1 
91   N N   . ALA A 20  ? 0.28685 0.35938 0.32168 -0.00957 -0.01503 -0.03155 27  ALA A N   
92   C CA  . ALA A 20  ? 0.29275 0.37637 0.32842 0.00374  -0.01634 -0.02942 27  ALA A CA  
93   C C   . ALA A 20  ? 0.28116 0.37774 0.31443 0.00453  -0.02053 -0.03206 27  ALA A C   
94   O O   . ALA A 20  ? 0.29881 0.38865 0.32530 0.01519  -0.02050 -0.02882 27  ALA A O   
95   C CB  . ALA A 20  ? 0.30919 0.41525 0.35097 0.01063  -0.01514 -0.02812 27  ALA A CB  
96   N N   . GLN A 21  ? 0.27161 0.38692 0.30920 -0.00761 -0.02332 -0.03862 28  GLN A N   
97   C CA  . GLN A 21  ? 0.29899 0.43152 0.33399 -0.00814 -0.02852 -0.04426 28  GLN A CA  
98   C C   . GLN A 21  ? 0.28290 0.38802 0.30677 -0.00861 -0.02845 -0.04489 28  GLN A C   
99   O O   . GLN A 21  ? 0.34291 0.45348 0.35941 0.00086  -0.03103 -0.04449 28  GLN A O   
100  C CB  . GLN A 21  ? 0.32824 0.48565 0.37168 -0.02636 -0.03035 -0.05456 28  GLN A CB  
101  C CG  . GLN A 21  ? 0.47045 0.66062 0.51452 -0.02714 -0.03735 -0.06380 28  GLN A CG  
102  C CD  . GLN A 21  ? 0.68049 0.89835 0.73619 -0.04980 -0.03778 -0.07670 28  GLN A CD  
103  O OE1 . GLN A 21  ? 0.66639 0.87020 0.72655 -0.06562 -0.03095 -0.07687 28  GLN A OE1 
104  N NE2 . GLN A 21  ? 0.69893 0.95770 0.75886 -0.05199 -0.04504 -0.08795 28  GLN A NE2 
105  N N   . LEU A 22  ? 0.29551 0.37223 0.31630 -0.01724 -0.02497 -0.04528 29  LEU A N   
106  C CA  . LEU A 22  ? 0.32042 0.37314 0.33132 -0.01496 -0.02412 -0.04580 29  LEU A CA  
107  C C   . LEU A 22  ? 0.30023 0.34701 0.30876 -0.00070 -0.02201 -0.03857 29  LEU A C   
108  O O   . LEU A 22  ? 0.33041 0.37413 0.33128 0.00478  -0.02196 -0.03867 29  LEU A O   
109  C CB  . LEU A 22  ? 0.35730 0.38264 0.36430 -0.02158 -0.02036 -0.04583 29  LEU A CB  
110  C CG  . LEU A 22  ? 0.43809 0.44219 0.43620 -0.01525 -0.01898 -0.04585 29  LEU A CG  
111  C CD1 . LEU A 22  ? 0.37267 0.37490 0.36182 -0.01940 -0.02100 -0.05396 29  LEU A CD1 
112  C CD2 . LEU A 22  ? 0.42274 0.40375 0.41611 -0.01465 -0.01561 -0.04358 29  LEU A CD2 
113  N N   . MET A 23  ? 0.28870 0.33202 0.30253 0.00423  -0.01889 -0.03295 30  MET A N   
114  C CA  . MET A 23  ? 0.25031 0.28338 0.26148 0.01368  -0.01444 -0.02763 30  MET A CA  
115  C C   . MET A 23  ? 0.29696 0.34004 0.30106 0.02454  -0.01419 -0.02338 30  MET A C   
116  O O   . MET A 23  ? 0.32256 0.35541 0.31847 0.03030  -0.00996 -0.01969 30  MET A O   
117  C CB  . MET A 23  ? 0.28214 0.30787 0.29924 0.01489  -0.01076 -0.02536 30  MET A CB  
118  C CG  . MET A 23  ? 0.26636 0.28445 0.28707 0.00800  -0.01140 -0.02865 30  MET A CG  
119  S SD  . MET A 23  ? 0.31914 0.33635 0.34551 0.00920  -0.00916 -0.02866 30  MET A SD  
120  C CE  . MET A 23  ? 0.35378 0.35983 0.38111 0.01198  -0.00318 -0.02927 30  MET A CE  
121  N N   . SER A 24  ? 0.29967 0.36517 0.30558 0.02869  -0.01816 -0.02355 31  SER A N   
122  C CA  . SER A 24  ? 0.29593 0.37451 0.29193 0.04341  -0.01894 -0.01898 31  SER A CA  
123  C C   . SER A 24  ? 0.33552 0.42026 0.32252 0.04276  -0.02243 -0.02265 31  SER A C   
124  O O   . SER A 24  ? 0.37322 0.45387 0.34645 0.05543  -0.01947 -0.01632 31  SER A O   
125  C CB  . SER A 24  ? 0.35267 0.46364 0.35393 0.04988  -0.02390 -0.02020 31  SER A CB  
126  O OG  . SER A 24  ? 0.46018 0.56529 0.46775 0.05249  -0.01995 -0.01712 31  SER A OG  
127  N N   . LEU A 25  ? 0.29035 0.38222 0.28225 0.02848  -0.02756 -0.03288 32  LEU A N   
128  C CA  . LEU A 25  ? 0.30610 0.40227 0.28784 0.02748  -0.03082 -0.03890 32  LEU A CA  
129  C C   . LEU A 25  ? 0.33238 0.40205 0.30494 0.03178  -0.02400 -0.03377 32  LEU A C   
130  O O   . LEU A 25  ? 0.36384 0.43631 0.32290 0.04112  -0.02303 -0.03155 32  LEU A O   
131  C CB  . LEU A 25  ? 0.35310 0.45232 0.34000 0.00925  -0.03514 -0.05203 32  LEU A CB  
132  C CG  . LEU A 25  ? 0.43825 0.53836 0.41408 0.00474  -0.03851 -0.06260 32  LEU A CG  
133  C CD1 . LEU A 25  ? 0.50673 0.62140 0.48871 -0.01381 -0.04325 -0.07722 32  LEU A CD1 
134  C CD2 . LEU A 25  ? 0.53822 0.60510 0.50610 0.00418  -0.03307 -0.06210 32  LEU A CD2 
135  N N   . ILE A 26  ? 0.30201 0.34970 0.28166 0.02567  -0.01893 -0.03212 33  ILE A N   
136  C CA  . ILE A 26  ? 0.30603 0.33581 0.28111 0.02793  -0.01210 -0.02926 33  ILE A CA  
137  C C   . ILE A 26  ? 0.36132 0.38551 0.32924 0.03861  -0.00423 -0.01874 33  ILE A C   
138  O O   . ILE A 26  ? 0.37282 0.39095 0.33073 0.04318  0.00168  -0.01553 33  ILE A O   
139  C CB  . ILE A 26  ? 0.28725 0.30314 0.27301 0.02046  -0.00977 -0.03116 33  ILE A CB  
140  C CG1 . ILE A 26  ? 0.31563 0.32706 0.30009 0.01300  -0.01435 -0.03972 33  ILE A CG1 
141  C CG2 . ILE A 26  ? 0.33042 0.33655 0.31685 0.02295  -0.00157 -0.02801 33  ILE A CG2 
142  C CD1 . ILE A 26  ? 0.37590 0.37618 0.36764 0.00870  -0.01357 -0.04019 33  ILE A CD1 
143  N N   . ILE A 27  ? 0.35764 0.38135 0.32824 0.04325  -0.00257 -0.01293 34  ILE A N   
144  C CA  . ILE A 27  ? 0.38559 0.39440 0.34574 0.05344  0.00746  -0.00222 34  ILE A CA  
145  C C   . ILE A 27  ? 0.40434 0.42337 0.34544 0.06935  0.00662  0.00422  34  ILE A C   
146  O O   . ILE A 27  ? 0.47597 0.47915 0.40129 0.07782  0.01667  0.01358  34  ILE A O   
147  C CB  . ILE A 27  ? 0.38122 0.38153 0.34808 0.05443  0.01017  0.00047  34  ILE A CB  
148  C CG1 . ILE A 27  ? 0.32010 0.30903 0.30172 0.04051  0.01313  -0.00528 34  ILE A CG1 
149  C CG2 . ILE A 27  ? 0.49056 0.47123 0.44106 0.06824  0.02086  0.01204  34  ILE A CG2 
150  C CD1 . ILE A 27  ? 0.35543 0.34241 0.34512 0.03946  0.01236  -0.00681 34  ILE A CD1 
151  N N   . ASN A 28  ? 0.39831 0.44575 0.33944 0.07339  -0.00468 -0.00107 35  ASN A N   
152  C CA  . ASN A 28  ? 0.40740 0.47206 0.33027 0.09228  -0.00712 0.00471  35  ASN A CA  
153  C C   . ASN A 28  ? 0.41979 0.50193 0.33207 0.09315  -0.01292 -0.00171 35  ASN A C   
154  O O   . ASN A 28  ? 0.49647 0.59002 0.38869 0.11112  -0.01314 0.00464  35  ASN A O   
155  C CB  . ASN A 28  ? 0.46813 0.56275 0.39782 0.09940  -0.01608 0.00206  35  ASN A CB  
156  C CG  . ASN A 28  ? 0.63006 0.70684 0.56410 0.10452  -0.00930 0.00954  35  ASN A CG  
157  O OD1 . ASN A 28  ? 0.58220 0.62495 0.50469 0.11104  0.00288  0.02005  35  ASN A OD1 
158  N ND2 . ASN A 28  ? 0.61682 0.71480 0.56703 0.09991  -0.01575 0.00319  35  ASN A ND2 
159  N N   . THR A 29  ? 0.39063 0.47393 0.31269 0.07645  -0.01723 -0.01406 36  THR A N   
160  C CA  . THR A 29  ? 0.44763 0.54654 0.35834 0.07684  -0.02299 -0.02302 36  THR A CA  
161  C C   . THR A 29  ? 0.43217 0.51169 0.32581 0.08463  -0.01250 -0.01480 36  THR A C   
162  O O   . THR A 29  ? 0.48331 0.53711 0.38261 0.07884  -0.00208 -0.00933 36  THR A O   
163  C CB  . THR A 29  ? 0.49297 0.59240 0.41647 0.05704  -0.02916 -0.03927 36  THR A CB  
164  O OG1 . THR A 29  ? 0.45993 0.58022 0.39760 0.04830  -0.03723 -0.04688 36  THR A OG1 
165  C CG2 . THR A 29  ? 0.48940 0.59863 0.39920 0.05639  -0.03370 -0.05073 36  THR A CG2 
166  N N   . PHE A 30  ? 0.41126 0.50686 0.28383 0.09800  -0.01478 -0.01426 37  PHE A N   
167  C CA  . PHE A 30  ? 0.46055 0.54034 0.31526 0.10478  -0.00386 -0.00706 37  PHE A CA  
168  C C   . PHE A 30  ? 0.46059 0.53597 0.32151 0.09112  -0.00519 -0.02092 37  PHE A C   
169  O O   . PHE A 30  ? 0.46452 0.55721 0.32395 0.08634  -0.01604 -0.03642 37  PHE A O   
170  C CB  . PHE A 30  ? 0.47073 0.56936 0.29701 0.12607  -0.00548 -0.00127 37  PHE A CB  
171  C CG  . PHE A 30  ? 0.43389 0.51604 0.23873 0.13401  0.00802  0.00815  37  PHE A CG  
172  C CD1 . PHE A 30  ? 0.60289 0.65573 0.39755 0.14090  0.02565  0.02759  37  PHE A CD1 
173  C CD2 . PHE A 30  ? 0.46793 0.56248 0.26181 0.13361  0.00464  -0.00308 37  PHE A CD2 
174  C CE1 . PHE A 30  ? 0.61780 0.65630 0.39303 0.14608  0.04059  0.03684  37  PHE A CE1 
175  C CE2 . PHE A 30  ? 0.51993 0.60211 0.29365 0.14152  0.01844  0.00596  37  PHE A CE2 
176  C CZ  . PHE A 30  ? 0.49020 0.54552 0.25538 0.14714  0.03686  0.02653  37  PHE A CZ  
177  N N   . TYR A 31  ? 0.39881 0.45162 0.26608 0.08514  0.00642  -0.01641 38  TYR A N   
178  C CA  . TYR A 31  ? 0.36589 0.41337 0.23922 0.07583  0.00625  -0.02835 38  TYR A CA  
179  C C   . TYR A 31  ? 0.38846 0.42190 0.26282 0.07616  0.02164  -0.01985 38  TYR A C   
180  O O   . TYR A 31  ? 0.39678 0.41881 0.28669 0.06936  0.02847  -0.01361 38  TYR A O   
181  C CB  . TYR A 31  ? 0.38405 0.42623 0.27829 0.06169  -0.00119 -0.03810 38  TYR A CB  
182  C CG  . TYR A 31  ? 0.40282 0.43505 0.29924 0.05603  -0.00098 -0.04933 38  TYR A CG  
183  C CD1 . TYR A 31  ? 0.46256 0.49852 0.34593 0.05577  -0.00741 -0.06326 38  TYR A CD1 
184  C CD2 . TYR A 31  ? 0.43175 0.45154 0.34207 0.05211  0.00550  -0.04728 38  TYR A CD2 
185  C CE1 . TYR A 31  ? 0.54477 0.56614 0.42600 0.05356  -0.00597 -0.07328 38  TYR A CE1 
186  C CE2 . TYR A 31  ? 0.43966 0.45090 0.34918 0.05181  0.00576  -0.05674 38  TYR A CE2 
187  C CZ  . TYR A 31  ? 0.50477 0.51354 0.39848 0.05326  0.00063  -0.06904 38  TYR A CZ  
188  O OH  . TYR A 31  ? 0.55864 0.55312 0.44733 0.05560  0.00207  -0.07849 38  TYR A OH  
189  N N   . SER A 32  ? 0.40564 0.44287 0.26393 0.08316  0.02751  -0.02091 39  SER A N   
190  C CA  . SER A 32  ? 0.42151 0.45118 0.27922 0.08361  0.04456  -0.01146 39  SER A CA  
191  C C   . SER A 32  ? 0.46757 0.49635 0.34550 0.07441  0.04791  -0.01965 39  SER A C   
192  O O   . SER A 32  ? 0.46677 0.49369 0.35451 0.06944  0.06148  -0.01333 39  SER A O   
193  C CB  . SER A 32  ? 0.44787 0.48470 0.27837 0.09651  0.05145  -0.00762 39  SER A CB  
194  O OG  . SER A 32  ? 0.48844 0.52701 0.29812 0.10865  0.05019  0.00315  39  SER A OG  
195  N N   . ASN A 33  ? 0.37817 0.40823 0.26201 0.07210  0.03662  -0.03366 40  ASN A N   
196  C CA  . ASN A 33  ? 0.36162 0.39187 0.25900 0.06969  0.03887  -0.04162 40  ASN A CA  
197  C C   . ASN A 33  ? 0.37955 0.40612 0.30107 0.06021  0.03744  -0.04009 40  ASN A C   
198  O O   . ASN A 33  ? 0.36758 0.38889 0.29709 0.05837  0.02962  -0.04778 40  ASN A O   
199  C CB  . ASN A 33  ? 0.43177 0.45696 0.31843 0.07373  0.02930  -0.05627 40  ASN A CB  
200  C CG  . ASN A 33  ? 0.45626 0.47943 0.35036 0.07764  0.03222  -0.06378 40  ASN A CG  
201  O OD1 . ASN A 33  ? 0.44421 0.48045 0.34646 0.08103  0.04274  -0.06031 40  ASN A OD1 
202  N ND2 . ASN A 33  ? 0.49663 0.50361 0.38719 0.07758  0.02374  -0.07425 40  ASN A ND2 
203  N N   . LYS A 34  ? 0.29940 0.37411 0.24638 0.02724  -0.00657 -0.00588 41  LYS A N   
204  C CA  . LYS A 34  ? 0.28483 0.35976 0.25279 0.02145  -0.00025 -0.00180 41  LYS A CA  
205  C C   . LYS A 34  ? 0.29963 0.36166 0.27244 0.01772  0.00567  -0.00741 41  LYS A C   
206  O O   . LYS A 34  ? 0.27886 0.33933 0.26648 0.01147  0.00685  -0.00704 41  LYS A O   
207  C CB  . LYS A 34  ? 0.31439 0.39219 0.28517 0.02858  0.01011  0.00931  41  LYS A CB  
208  C CG  . LYS A 34  ? 0.32456 0.41866 0.29639 0.03402  0.00493  0.01689  41  LYS A CG  
209  C CD  . LYS A 34  ? 0.37811 0.46586 0.34598 0.04418  0.01556  0.02724  41  LYS A CD  
210  C CE  . LYS A 34  ? 0.36893 0.47280 0.33584 0.05446  0.01206  0.03620  41  LYS A CE  
211  N NZ  . LYS A 34  ? 0.39671 0.51667 0.38038 0.05420  0.00898  0.03822  41  LYS A NZ  
212  N N   . GLU A 35  ? 0.31780 0.37322 0.27781 0.02303  0.00926  -0.01209 42  GLU A N   
213  C CA  . GLU A 35  ? 0.29981 0.34898 0.26698 0.02163  0.01613  -0.01490 42  GLU A CA  
214  C C   . GLU A 35  ? 0.34751 0.38813 0.32136 0.01427  0.00760  -0.02293 42  GLU A C   
215  O O   . GLU A 35  ? 0.30839 0.34552 0.29154 0.01244  0.01216  -0.02416 42  GLU A O   
216  C CB  . GLU A 35  ? 0.31220 0.36182 0.26456 0.03186  0.02232  -0.01727 42  GLU A CB  
217  C CG  . GLU A 35  ? 0.36797 0.40791 0.29813 0.03812  0.01159  -0.02903 42  GLU A CG  
218  C CD  . GLU A 35  ? 0.61602 0.65912 0.52452 0.05400  0.01915  -0.03038 42  GLU A CD  
219  O OE1 . GLU A 35  ? 0.50856 0.56465 0.41346 0.05978  0.02931  -0.02017 42  GLU A OE1 
220  O OE2 . GLU A 35  ? 0.61020 0.64185 0.50329 0.06218  0.01511  -0.04117 42  GLU A OE2 
221  N N   . ILE A 36  ? 0.30690 0.34450 0.27674 0.00901  -0.00562 -0.02713 43  ILE A N   
222  C CA  . ILE A 36  ? 0.31114 0.33805 0.28669 0.00040  -0.01420 -0.03237 43  ILE A CA  
223  C C   . ILE A 36  ? 0.29285 0.32609 0.28893 -0.00649 -0.00934 -0.02615 43  ILE A C   
224  O O   . ILE A 36  ? 0.29441 0.31902 0.29556 -0.01215 -0.01320 -0.02874 43  ILE A O   
225  C CB  . ILE A 36  ? 0.32869 0.35108 0.29748 -0.00769 -0.03140 -0.03568 43  ILE A CB  
226  C CG1 . ILE A 36  ? 0.37521 0.41997 0.35793 -0.01367 -0.03400 -0.02564 43  ILE A CG1 
227  C CG2 . ILE A 36  ? 0.41604 0.42545 0.35745 0.00096  -0.03844 -0.04502 43  ILE A CG2 
228  C CD1 . ILE A 36  ? 0.46075 0.51421 0.46391 -0.02597 -0.03767 -0.01912 43  ILE A CD1 
229  N N   . PHE A 37  ? 0.25848 0.30360 0.26325 -0.00451 -0.00119 -0.01819 44  PHE A N   
230  C CA  . PHE A 37  ? 0.25115 0.29869 0.26942 -0.00804 0.00303  -0.01414 44  PHE A CA  
231  C C   . PHE A 37  ? 0.26409 0.30105 0.28484 -0.00862 0.00677  -0.01850 44  PHE A C   
232  O O   . PHE A 37  ? 0.26432 0.29916 0.29231 -0.01305 0.00536  -0.01835 44  PHE A O   
233  C CB  . PHE A 37  ? 0.25626 0.30973 0.27686 -0.00230 0.01105  -0.00701 44  PHE A CB  
234  C CG  . PHE A 37  ? 0.30400 0.34795 0.32148 0.00120  0.01951  -0.00656 44  PHE A CG  
235  C CD1 . PHE A 37  ? 0.27401 0.31861 0.28278 0.00598  0.02307  -0.00434 44  PHE A CD1 
236  C CD2 . PHE A 37  ? 0.26658 0.30221 0.28995 -0.00154 0.02291  -0.00737 44  PHE A CD2 
237  C CE1 . PHE A 37  ? 0.29216 0.33168 0.30143 0.00640  0.03084  -0.00068 44  PHE A CE1 
238  C CE2 . PHE A 37  ? 0.23586 0.26499 0.25970 -0.00218 0.02841  -0.00531 44  PHE A CE2 
239  C CZ  . PHE A 37  ? 0.30602 0.33818 0.32442 0.00099  0.03282  -0.00085 44  PHE A CZ  
240  N N   . LEU A 38  ? 0.27144 0.30527 0.28686 -0.00343 0.01186  -0.02088 45  LEU A N   
241  C CA  . LEU A 38  ? 0.27728 0.30792 0.29892 -0.00353 0.01554  -0.02284 45  LEU A CA  
242  C C   . LEU A 38  ? 0.28836 0.31019 0.30670 -0.00369 0.00860  -0.02952 45  LEU A C   
243  O O   . LEU A 38  ? 0.28300 0.30183 0.30857 -0.00624 0.00777  -0.03011 45  LEU A O   
244  C CB  . LEU A 38  ? 0.26352 0.30054 0.28423 0.00178  0.02386  -0.02015 45  LEU A CB  
245  C CG  . LEU A 38  ? 0.24713 0.28850 0.27919 0.00060  0.02739  -0.01954 45  LEU A CG  
246  C CD1 . LEU A 38  ? 0.27045 0.30767 0.31258 -0.00746 0.02641  -0.01682 45  LEU A CD1 
247  C CD2 . LEU A 38  ? 0.29075 0.34565 0.32505 0.00480  0.03617  -0.01346 45  LEU A CD2 
248  N N   . ARG A 39  ? 0.26750 0.28173 0.27210 -0.00044 0.00219  -0.03482 46  ARG A N   
249  C CA  . ARG A 39  ? 0.27549 0.27282 0.27268 -0.00094 -0.00703 -0.04136 46  ARG A CA  
250  C C   . ARG A 39  ? 0.31152 0.30591 0.31890 -0.01253 -0.01319 -0.03734 46  ARG A C   
251  O O   . ARG A 39  ? 0.31478 0.29860 0.32333 -0.01370 -0.01633 -0.03861 46  ARG A O   
252  C CB  . ARG A 39  ? 0.31443 0.29822 0.29123 0.00235  -0.01650 -0.04832 46  ARG A CB  
253  C CG  . ARG A 39  ? 0.39950 0.35655 0.36393 0.00056  -0.02937 -0.05554 46  ARG A CG  
254  C CD  . ARG A 39  ? 0.41345 0.35210 0.35494 0.00061  -0.04304 -0.06327 46  ARG A CD  
255  N NE  . ARG A 39  ? 0.48735 0.43692 0.43780 -0.01404 -0.05100 -0.05710 46  ARG A NE  
256  C CZ  . ARG A 39  ? 0.49732 0.44340 0.43317 -0.01519 -0.06131 -0.06091 46  ARG A CZ  
257  N NH1 . ARG A 39  ? 0.50095 0.43081 0.40882 -0.00124 -0.06400 -0.07177 46  ARG A NH1 
258  N NH2 . ARG A 39  ? 0.51070 0.47212 0.45951 -0.02939 -0.06937 -0.05323 46  ARG A NH2 
259  N N   . GLU A 40  ? 0.27156 0.27749 0.28603 -0.01975 -0.01448 -0.03101 47  GLU A N   
260  C CA  . GLU A 40  ? 0.25104 0.26060 0.27576 -0.02979 -0.01887 -0.02445 47  GLU A CA  
261  C C   . GLU A 40  ? 0.26226 0.27602 0.29556 -0.02809 -0.01121 -0.02132 47  GLU A C   
262  O O   . GLU A 40  ? 0.27377 0.28288 0.31018 -0.03296 -0.01453 -0.01841 47  GLU A O   
263  C CB  . GLU A 40  ? 0.25259 0.28138 0.28464 -0.03449 -0.02005 -0.01668 47  GLU A CB  
264  C CG  . GLU A 40  ? 0.28908 0.31610 0.31431 -0.03991 -0.03194 -0.01836 47  GLU A CG  
265  C CD  . GLU A 40  ? 0.35823 0.36054 0.37377 -0.04770 -0.04558 -0.02396 47  GLU A CD  
266  O OE1 . GLU A 40  ? 0.38210 0.38014 0.40546 -0.05622 -0.04857 -0.01878 47  GLU A OE1 
267  O OE2 . GLU A 40  ? 0.41507 0.40002 0.41262 -0.04477 -0.05406 -0.03314 47  GLU A OE2 
268  N N   . LEU A 41  ? 0.25234 0.27317 0.28797 -0.02194 -0.00217 -0.02123 48  LEU A N   
269  C CA  . LEU A 41  ? 0.25183 0.27352 0.29227 -0.02086 0.00234  -0.01973 48  LEU A CA  
270  C C   . LEU A 41  ? 0.26213 0.27513 0.30231 -0.01908 0.00077  -0.02433 48  LEU A C   
271  O O   . LEU A 41  ? 0.25655 0.26750 0.29878 -0.02021 -0.00049 -0.02302 48  LEU A O   
272  C CB  . LEU A 41  ? 0.24172 0.26710 0.28242 -0.01670 0.00936  -0.01863 48  LEU A CB  
273  C CG  . LEU A 41  ? 0.22802 0.26199 0.26763 -0.01448 0.01159  -0.01324 48  LEU A CG  
274  C CD1 . LEU A 41  ? 0.27653 0.30503 0.31219 -0.00944 0.01729  -0.01265 48  LEU A CD1 
275  C CD2 . LEU A 41  ? 0.26690 0.30957 0.30925 -0.01511 0.01099  -0.00784 48  LEU A CD2 
276  N N   . ILE A 42  ? 0.23670 0.24655 0.27316 -0.01423 0.00106  -0.02904 49  ILE A N   
277  C CA  . ILE A 42  ? 0.26389 0.26940 0.30062 -0.00928 -0.00010 -0.03247 49  ILE A CA  
278  C C   . ILE A 42  ? 0.30803 0.29775 0.33826 -0.01088 -0.00843 -0.03357 49  ILE A C   
279  O O   . ILE A 42  ? 0.27217 0.25777 0.30406 -0.00907 -0.01048 -0.03308 49  ILE A O   
280  C CB  . ILE A 42  ? 0.23670 0.24697 0.26991 -0.00020 0.00412  -0.03579 49  ILE A CB  
281  C CG1 . ILE A 42  ? 0.24119 0.26779 0.28465 -0.00139 0.01221  -0.03118 49  ILE A CG1 
282  C CG2 . ILE A 42  ? 0.29451 0.29993 0.32452 0.00940  0.00198  -0.03967 49  ILE A CG2 
283  C CD1 . ILE A 42  ? 0.24854 0.28637 0.28978 0.00707  0.01887  -0.03051 49  ILE A CD1 
284  N N   . SER A 43  ? 0.26840 0.24824 0.29104 -0.01548 -0.01470 -0.03399 50  SER A N   
285  C CA  . SER A 43  ? 0.31606 0.27713 0.33269 -0.02097 -0.02455 -0.03288 50  SER A CA  
286  C C   . SER A 43  ? 0.33802 0.30614 0.36406 -0.02865 -0.02391 -0.02382 50  SER A C   
287  O O   . SER A 43  ? 0.29428 0.24989 0.31747 -0.02919 -0.02821 -0.02151 50  SER A O   
288  C CB  . SER A 43  ? 0.36909 0.32036 0.37791 -0.02840 -0.03362 -0.03378 50  SER A CB  
289  O OG  . SER A 43  ? 0.45730 0.38775 0.46124 -0.03757 -0.04508 -0.03083 50  SER A OG  
290  N N   . ASN A 44  ? 0.28097 0.26854 0.31574 -0.03238 -0.01816 -0.01813 51  ASN A N   
291  C CA  . ASN A 44  ? 0.33489 0.33168 0.37492 -0.03550 -0.01555 -0.00977 51  ASN A CA  
292  C C   . ASN A 44  ? 0.31776 0.31152 0.35612 -0.02862 -0.01312 -0.01256 51  ASN A C   
293  O O   . ASN A 44  ? 0.29250 0.28282 0.32905 -0.02986 -0.01521 -0.00723 51  ASN A O   
294  C CB  . ASN A 44  ? 0.27504 0.29209 0.32046 -0.03489 -0.00860 -0.00506 51  ASN A CB  
295  C CG  . ASN A 44  ? 0.36153 0.39001 0.41264 -0.04288 -0.01189 0.00239  51  ASN A CG  
296  O OD1 . ASN A 44  ? 0.36623 0.38495 0.41703 -0.05196 -0.02122 0.00382  51  ASN A OD1 
297  N ND2 . ASN A 44  ? 0.39582 0.44440 0.45149 -0.03927 -0.00550 0.00742  51  ASN A ND2 
298  N N   . SER A 45  ? 0.26123 0.25835 0.30091 -0.02223 -0.00929 -0.01931 52  SER A N   
299  C CA  . SER A 45  ? 0.25957 0.25757 0.30046 -0.01737 -0.00923 -0.02167 52  SER A CA  
300  C C   . SER A 45  ? 0.26855 0.25492 0.30592 -0.01350 -0.01488 -0.02248 52  SER A C   
301  O O   . SER A 45  ? 0.27317 0.25819 0.30904 -0.01152 -0.01747 -0.01992 52  SER A O   
302  C CB  . SER A 45  ? 0.24006 0.24642 0.28671 -0.01445 -0.00536 -0.02624 52  SER A CB  
303  O OG  . SER A 45  ? 0.28652 0.29738 0.33319 -0.01705 -0.00141 -0.02509 52  SER A OG  
304  N N   . SER A 46  ? 0.25454 0.23041 0.28744 -0.01032 -0.01733 -0.02645 53  SER A N   
305  C CA  . SER A 46  ? 0.29069 0.24904 0.31552 -0.00364 -0.02341 -0.02798 53  SER A CA  
306  C C   . SER A 46  ? 0.32652 0.26975 0.34586 -0.01076 -0.02961 -0.02036 53  SER A C   
307  O O   . SER A 46  ? 0.34871 0.28259 0.36369 -0.00540 -0.03329 -0.01809 53  SER A O   
308  C CB  . SER A 46  ? 0.31836 0.26240 0.33281 0.00236  -0.02585 -0.03486 53  SER A CB  
309  O OG  . SER A 46  ? 0.36964 0.29111 0.37172 0.01223  -0.03224 -0.03756 53  SER A OG  
310  N N   . ASP A 47  ? 0.30897 0.25220 0.32948 -0.02278 -0.03080 -0.01440 54  ASP A N   
311  C CA  . ASP A 47  ? 0.29957 0.23335 0.31775 -0.03167 -0.03576 -0.00339 54  ASP A CA  
312  C C   . ASP A 47  ? 0.33045 0.27870 0.35115 -0.02887 -0.03086 0.00307  54  ASP A C   
313  O O   . ASP A 47  ? 0.31862 0.25632 0.33371 -0.02925 -0.03461 0.01067  54  ASP A O   
314  C CB  . ASP A 47  ? 0.30596 0.24699 0.32997 -0.04600 -0.03727 0.00456  54  ASP A CB  
315  C CG  . ASP A 47  ? 0.46193 0.38425 0.47998 -0.05139 -0.04628 -0.00103 54  ASP A CG  
316  O OD1 . ASP A 47  ? 0.45020 0.34505 0.45473 -0.04437 -0.05294 -0.00939 54  ASP A OD1 
317  O OD2 . ASP A 47  ? 0.44072 0.37525 0.46606 -0.06236 -0.04796 0.00384  54  ASP A OD2 
318  N N   . ALA A 48  ? 0.29875 0.26815 0.32484 -0.02568 -0.02341 0.00029  55  ALA A N   
319  C CA  . ALA A 48  ? 0.26817 0.24795 0.29137 -0.02148 -0.02040 0.00394  55  ALA A CA  
320  C C   . ALA A 48  ? 0.31508 0.28838 0.33471 -0.01288 -0.02478 -0.00031 55  ALA A C   
321  O O   . ALA A 48  ? 0.30086 0.27405 0.31375 -0.00986 -0.02657 0.00526  55  ALA A O   
322  C CB  . ALA A 48  ? 0.25581 0.25134 0.28109 -0.01907 -0.01395 -0.00053 55  ALA A CB  
323  N N   . LEU A 49  ? 0.28525 0.25688 0.30946 -0.00758 -0.02615 -0.00905 56  LEU A N   
324  C CA  . LEU A 49  ? 0.26413 0.23559 0.28836 0.00208  -0.03035 -0.01169 56  LEU A CA  
325  C C   . LEU A 49  ? 0.31466 0.26429 0.32906 0.00615  -0.03640 -0.00656 56  LEU A C   
326  O O   . LEU A 49  ? 0.31477 0.26328 0.32486 0.01299  -0.04039 -0.00305 56  LEU A O   
327  C CB  . LEU A 49  ? 0.28950 0.27080 0.32309 0.00766  -0.02830 -0.01963 56  LEU A CB  
328  C CG  . LEU A 49  ? 0.24551 0.24619 0.28900 0.00304  -0.02439 -0.02280 56  LEU A CG  
329  C CD1 . LEU A 49  ? 0.27598 0.28516 0.32797 0.00501  -0.01982 -0.02698 56  LEU A CD1 
330  C CD2 . LEU A 49  ? 0.24387 0.25733 0.29174 0.00520  -0.02925 -0.02284 56  LEU A CD2 
331  N N   . ASP A 50  ? 0.32637 0.25575 0.33525 0.00163  -0.03873 -0.00574 57  ASP A N   
332  C CA  . ASP A 50  ? 0.33996 0.24016 0.33631 0.00310  -0.04648 0.00004  57  ASP A CA  
333  C C   . ASP A 50  ? 0.34698 0.24775 0.33980 -0.00312 -0.04724 0.01343  57  ASP A C   
334  O O   . ASP A 50  ? 0.37134 0.25600 0.35456 0.00302  -0.05256 0.01938  57  ASP A O   
335  C CB  . ASP A 50  ? 0.34067 0.21585 0.33020 -0.00580 -0.05168 -0.00050 57  ASP A CB  
336  C CG  . ASP A 50  ? 0.43892 0.30409 0.42294 0.00456  -0.05281 -0.01358 57  ASP A CG  
337  O OD1 . ASP A 50  ? 0.44408 0.31909 0.42930 0.02073  -0.04966 -0.02023 57  ASP A OD1 
338  O OD2 . ASP A 50  ? 0.45384 0.30225 0.43157 -0.00336 -0.05749 -0.01629 57  ASP A OD2 
339  N N   . LYS A 51  ? 0.31844 0.23774 0.31721 -0.01362 -0.04145 0.01943  58  LYS A N   
340  C CA  . LYS A 51  ? 0.32997 0.25433 0.32418 -0.01837 -0.03995 0.03405  58  LYS A CA  
341  C C   . LYS A 51  ? 0.34714 0.28084 0.33473 -0.00650 -0.03981 0.03371  58  LYS A C   
342  O O   . LYS A 51  ? 0.34336 0.26739 0.32102 -0.00418 -0.04304 0.04448  58  LYS A O   
343  C CB  . LYS A 51  ? 0.36897 0.31647 0.37039 -0.02758 -0.03209 0.04018  58  LYS A CB  
344  C CG  . LYS A 51  ? 0.45484 0.39664 0.46367 -0.04253 -0.03446 0.04648  58  LYS A CG  
345  C CD  . LYS A 51  ? 0.50744 0.47908 0.52645 -0.04761 -0.02589 0.05043  58  LYS A CD  
346  C CE  . LYS A 51  ? 0.60797 0.57794 0.63701 -0.06136 -0.03020 0.05247  58  LYS A CE  
347  N NZ  . LYS A 51  ? 0.61510 0.61870 0.65548 -0.06499 -0.02183 0.06013  58  LYS A NZ  
348  N N   . ILE A 52  ? 0.34137 0.29288 0.33352 0.00014  -0.03745 0.02238  59  ILE A N   
349  C CA  . ILE A 52  ? 0.35364 0.31366 0.33874 0.00972  -0.04054 0.02172  59  ILE A CA  
350  C C   . ILE A 52  ? 0.36835 0.31689 0.35207 0.01982  -0.04822 0.02060  59  ILE A C   
351  O O   . ILE A 52  ? 0.36153 0.30874 0.33550 0.02719  -0.05284 0.02666  59  ILE A O   
352  C CB  . ILE A 52  ? 0.31248 0.29122 0.30189 0.01137  -0.03904 0.01065  59  ILE A CB  
353  C CG1 . ILE A 52  ? 0.34964 0.33557 0.32836 0.01922  -0.04504 0.01024  59  ILE A CG1 
354  C CG2 . ILE A 52  ? 0.30431 0.28774 0.30880 0.01165  -0.03989 -0.00018 59  ILE A CG2 
355  C CD1 . ILE A 52  ? 0.40388 0.38954 0.36420 0.02109  -0.04204 0.02075  59  ILE A CD1 
356  N N   . ARG A 53  ? 0.33045 0.27061 0.32145 0.02274  -0.04951 0.01359  60  ARG A N   
357  C CA  . ARG A 53  ? 0.33904 0.26792 0.32652 0.03645  -0.05581 0.01308  60  ARG A CA  
358  C C   . ARG A 53  ? 0.37109 0.27084 0.34242 0.03753  -0.06079 0.02530  60  ARG A C   
359  O O   . ARG A 53  ? 0.39788 0.29418 0.36135 0.04890  -0.06610 0.03044  60  ARG A O   
360  C CB  . ARG A 53  ? 0.33928 0.26231 0.33260 0.04194  -0.05476 0.00372  60  ARG A CB  
361  C CG  . ARG A 53  ? 0.38632 0.30468 0.37651 0.06114  -0.05965 0.00226  60  ARG A CG  
362  C CD  . ARG A 53  ? 0.46515 0.37588 0.45557 0.07066  -0.05755 -0.00657 60  ARG A CD  
363  N NE  . ARG A 53  ? 0.88775 0.79581 0.87342 0.09349  -0.06124 -0.00712 60  ARG A NE  
364  C CZ  . ARG A 53  ? 0.87544 0.75714 0.84671 0.10886  -0.06277 -0.01208 60  ARG A CZ  
365  N NH1 . ARG A 53  ? 0.68141 0.53703 0.64177 0.10217  -0.06227 -0.01802 60  ARG A NH1 
366  N NH2 . ARG A 53  ? 0.77679 0.65772 0.74246 0.13309  -0.06571 -0.01142 60  ARG A NH2 
367  N N   . TYR A 54  ? 0.38441 0.26328 0.35111 0.02469  -0.06016 0.03155  61  TYR A N   
368  C CA  . TYR A 54  ? 0.43312 0.28154 0.38536 0.02172  -0.06590 0.04581  61  TYR A CA  
369  C C   . TYR A 54  ? 0.42112 0.28290 0.36706 0.02153  -0.06413 0.05921  61  TYR A C   
370  O O   . TYR A 54  ? 0.44929 0.29388 0.38225 0.02950  -0.06970 0.06875  61  TYR A O   
371  C CB  . TYR A 54  ? 0.42734 0.25595 0.37951 0.00315  -0.06705 0.05216  61  TYR A CB  
372  C CG  . TYR A 54  ? 0.51044 0.29441 0.44663 0.00074  -0.07719 0.06286  61  TYR A CG  
373  C CD1 . TYR A 54  ? 0.70217 0.45106 0.62555 0.01411  -0.08554 0.05327  61  TYR A CD1 
374  C CD2 . TYR A 54  ? 0.65019 0.42647 0.58183 -0.01246 -0.07829 0.08356  61  TYR A CD2 
375  C CE1 . TYR A 54  ? 0.74335 0.44326 0.64767 0.01314  -0.09658 0.06220  61  TYR A CE1 
376  C CE2 . TYR A 54  ? 0.54139 0.27182 0.45728 -0.01636 -0.08903 0.09513  61  TYR A CE2 
377  C CZ  . TYR A 54  ? 0.72210 0.41109 0.62318 -0.00361 -0.09904 0.08347  61  TYR A CZ  
378  O OH  . TYR A 54  ? 0.75778 0.39288 0.63887 -0.00626 -0.11148 0.09371  61  TYR A OH  
379  N N   . GLU A 55  ? 0.40311 0.29403 0.35493 0.01479  -0.05644 0.06010  62  GLU A N   
380  C CA  . GLU A 55  ? 0.43932 0.34321 0.38034 0.01708  -0.05398 0.07227  62  GLU A CA  
381  C C   . GLU A 55  ? 0.43797 0.34785 0.37127 0.03384  -0.06009 0.06756  62  GLU A C   
382  O O   . GLU A 55  ? 0.46595 0.37131 0.38444 0.03987  -0.06279 0.07990  62  GLU A O   
383  C CB  . GLU A 55  ? 0.43502 0.36742 0.37994 0.01148  -0.04458 0.07086  62  GLU A CB  
384  C CG  . GLU A 55  ? 0.54645 0.48149 0.49508 -0.00337 -0.03785 0.08634  62  GLU A CG  
385  C CD  . GLU A 55  ? 0.73535 0.70074 0.68487 -0.00373 -0.02723 0.08683  62  GLU A CD  
386  O OE1 . GLU A 55  ? 0.74271 0.72122 0.68162 0.00818  -0.02583 0.07847  62  GLU A OE1 
387  O OE2 . GLU A 55  ? 0.79222 0.76765 0.75200 -0.01533 -0.02126 0.09562  62  GLU A OE2 
388  N N   . SER A 56  ? 0.39424 0.31642 0.33841 0.04112  -0.06285 0.05141  63  SER A N   
389  C CA  . SER A 56  ? 0.44361 0.37849 0.38551 0.05537  -0.07026 0.04723  63  SER A CA  
390  C C   . SER A 56  ? 0.48737 0.40118 0.42084 0.06827  -0.07754 0.05466  63  SER A C   
391  O O   . SER A 56  ? 0.49132 0.41552 0.41939 0.08097  -0.08441 0.05639  63  SER A O   
392  C CB  . SER A 56  ? 0.42344 0.38011 0.38382 0.05723  -0.07142 0.03133  63  SER A CB  
393  O OG  . SER A 56  ? 0.44641 0.39354 0.41629 0.06337  -0.07210 0.02686  63  SER A OG  
394  N N   . LEU A 57  ? 0.47649 0.35873 0.40673 0.06606  -0.07767 0.05883  64  LEU A N   
395  C CA  . LEU A 57  ? 0.48024 0.33461 0.39806 0.08071  -0.08538 0.06527  64  LEU A CA  
396  C C   . LEU A 57  ? 0.62749 0.47215 0.52694 0.08290  -0.08851 0.08306  64  LEU A C   
397  O O   . LEU A 57  ? 0.68882 0.52652 0.57819 0.10002  -0.09571 0.08787  64  LEU A O   
398  C CB  . LEU A 57  ? 0.50778 0.32203 0.42045 0.07601  -0.08679 0.06505  64  LEU A CB  
399  C CG  . LEU A 57  ? 0.55253 0.37261 0.47756 0.08087  -0.08470 0.04762  64  LEU A CG  
400  C CD1 . LEU A 57  ? 0.61229 0.38687 0.52550 0.07694  -0.08854 0.04627  64  LEU A CD1 
401  C CD2 . LEU A 57  ? 0.62337 0.46393 0.55457 0.10405  -0.08723 0.03982  64  LEU A CD2 
402  N N   . THR A 58  ? 0.57778 0.42467 0.47247 0.06722  -0.08254 0.09443  65  THR A N   
403  C CA  . THR A 58  ? 0.65100 0.49283 0.52740 0.06855  -0.08317 0.11389  65  THR A CA  
404  C C   . THR A 58  ? 0.64531 0.52338 0.51653 0.07317  -0.08032 0.11253  65  THR A C   
405  O O   . THR A 58  ? 0.62893 0.50705 0.48164 0.08048  -0.08224 0.12651  65  THR A O   
406  C CB  . THR A 58  ? 0.76083 0.58278 0.63372 0.04907  -0.07829 0.13199  65  THR A CB  
407  O OG1 . THR A 58  ? 0.82513 0.67762 0.70752 0.03627  -0.06779 0.13134  65  THR A OG1 
408  C CG2 . THR A 58  ? 0.63779 0.42195 0.51530 0.04085  -0.08334 0.12894  65  THR A CG2 
409  N N   . ASP A 59  ? 0.57807 0.48349 0.46194 0.07001  -0.07692 0.09602  66  ASP A N   
410  C CA  . ASP A 59  ? 0.55794 0.49106 0.43269 0.07502  -0.07698 0.09126  66  ASP A CA  
411  C C   . ASP A 59  ? 0.53898 0.49161 0.43020 0.07758  -0.08227 0.07020  66  ASP A C   
412  O O   . ASP A 59  ? 0.53608 0.49889 0.43845 0.06811  -0.07683 0.05933  66  ASP A O   
413  C CB  . ASP A 59  ? 0.53453 0.47827 0.40300 0.06489  -0.06539 0.09727  66  ASP A CB  
414  C CG  . ASP A 59  ? 0.74837 0.71317 0.59792 0.07375  -0.06605 0.09260  66  ASP A CG  
415  O OD1 . ASP A 59  ? 0.62667 0.59878 0.47152 0.08385  -0.07737 0.08236  66  ASP A OD1 
416  O OD2 . ASP A 59  ? 0.71184 0.68657 0.55036 0.07132  -0.05590 0.09911  66  ASP A OD2 
417  N N   . PRO A 60  ? 0.57256 0.53249 0.46707 0.09005  -0.09313 0.06573  67  PRO A N   
418  C CA  . PRO A 60  ? 0.48959 0.47235 0.40485 0.08996  -0.09844 0.04902  67  PRO A CA  
419  C C   . PRO A 60  ? 0.51428 0.51546 0.42647 0.08282  -0.10013 0.03835  67  PRO A C   
420  O O   . PRO A 60  ? 0.51196 0.52656 0.44274 0.07565  -0.10124 0.02576  67  PRO A O   
421  C CB  . PRO A 60  ? 0.59204 0.58450 0.50884 0.10624  -0.11049 0.05140  67  PRO A CB  
422  C CG  . PRO A 60  ? 0.64153 0.60438 0.54506 0.11463  -0.10867 0.06601  67  PRO A CG  
423  C CD  . PRO A 60  ? 0.61901 0.56597 0.50296 0.10449  -0.10058 0.07725  67  PRO A CD  
424  N N   . SER A 61  ? 0.49925 0.49912 0.38590 0.08538  -0.10040 0.04345  68  SER A N   
425  C CA  . SER A 61  ? 0.48038 0.49026 0.35644 0.08163  -0.10331 0.03178  68  SER A CA  
426  C C   . SER A 61  ? 0.47785 0.48380 0.36166 0.07005  -0.09159 0.02519  68  SER A C   
427  O O   . SER A 61  ? 0.48885 0.49876 0.36718 0.06658  -0.09479 0.01280  68  SER A O   
428  C CB  . SER A 61  ? 0.56786 0.57553 0.40888 0.09142  -0.10500 0.03930  68  SER A CB  
429  O OG  . SER A 61  ? 0.60693 0.60621 0.43477 0.08965  -0.08952 0.05057  68  SER A OG  
430  N N   . LYS A 62  ? 0.46395 0.46023 0.35935 0.06399  -0.07978 0.03282  69  LYS A N   
431  C CA  . LYS A 62  ? 0.40981 0.40563 0.31500 0.05374  -0.06987 0.02676  69  LYS A CA  
432  C C   . LYS A 62  ? 0.42385 0.42728 0.35027 0.04751  -0.07459 0.01166  69  LYS A C   
433  O O   . LYS A 62  ? 0.40934 0.41273 0.34007 0.04043  -0.06881 0.00456  69  LYS A O   
434  C CB  . LYS A 62  ? 0.48474 0.46960 0.39935 0.04697  -0.05952 0.03822  69  LYS A CB  
435  C CG  . LYS A 62  ? 0.55161 0.53127 0.44831 0.04934  -0.05405 0.05687  69  LYS A CG  
436  C CD  . LYS A 62  ? 0.54846 0.52649 0.45247 0.03827  -0.04242 0.06698  69  LYS A CD  
437  C CE  . LYS A 62  ? 0.62672 0.60722 0.51453 0.03942  -0.03596 0.08840  69  LYS A CE  
438  N NZ  . LYS A 62  ? 0.75124 0.73956 0.64971 0.02741  -0.02477 0.09939  69  LYS A NZ  
439  N N   . LEU A 63  ? 0.40088 0.41319 0.34110 0.05067  -0.08455 0.00833  70  LEU A N   
440  C CA  . LEU A 63  ? 0.40981 0.43564 0.37237 0.04403  -0.08916 -0.00273 70  LEU A CA  
441  C C   . LEU A 63  ? 0.41335 0.44996 0.37024 0.04205  -0.10312 -0.01141 70  LEU A C   
442  O O   . LEU A 63  ? 0.43023 0.48116 0.40768 0.03447  -0.10966 -0.01803 70  LEU A O   
443  C CB  . LEU A 63  ? 0.38584 0.42103 0.37016 0.04917  -0.09084 -0.00000 70  LEU A CB  
444  C CG  . LEU A 63  ? 0.42081 0.44089 0.41124 0.04956  -0.07980 0.00424  70  LEU A CG  
445  C CD1 . LEU A 63  ? 0.50327 0.53282 0.51135 0.05887  -0.08181 0.00419  70  LEU A CD1 
446  C CD2 . LEU A 63  ? 0.39644 0.41170 0.39240 0.03783  -0.07013 -0.00109 70  LEU A CD2 
447  N N   . ASP A 64  ? 0.45057 0.48049 0.37901 0.04819  -0.10866 -0.01089 71  ASP A N   
448  C CA  . ASP A 64  ? 0.47294 0.50646 0.39035 0.04536  -0.12444 -0.02152 71  ASP A CA  
449  C C   . ASP A 64  ? 0.49149 0.51569 0.41043 0.03377  -0.12344 -0.03306 71  ASP A C   
450  O O   . ASP A 64  ? 0.48169 0.50753 0.40146 0.02578  -0.13864 -0.04264 71  ASP A O   
451  C CB  . ASP A 64  ? 0.50980 0.53379 0.38897 0.05680  -0.12934 -0.01996 71  ASP A CB  
452  C CG  . ASP A 64  ? 0.63965 0.67190 0.51448 0.06853  -0.13367 -0.00799 71  ASP A CG  
453  O OD1 . ASP A 64  ? 0.58952 0.63564 0.49078 0.06871  -0.13664 -0.00353 71  ASP A OD1 
454  O OD2 . ASP A 64  ? 0.70905 0.73423 0.55216 0.07942  -0.13415 -0.00263 71  ASP A OD2 
455  N N   . SER A 65  ? 0.45202 0.46532 0.37050 0.03227  -0.10737 -0.03159 72  SER A N   
456  C CA  . SER A 65  ? 0.41846 0.42104 0.33821 0.02334  -0.10483 -0.04091 72  SER A CA  
457  C C   . SER A 65  ? 0.49589 0.51045 0.45118 0.01107  -0.10343 -0.04156 72  SER A C   
458  O O   . SER A 65  ? 0.50479 0.51036 0.46393 0.00331  -0.09924 -0.04669 72  SER A O   
459  C CB  . SER A 65  ? 0.45992 0.45076 0.36474 0.02898  -0.08792 -0.03733 72  SER A CB  
460  O OG  . SER A 65  ? 0.43017 0.42870 0.34831 0.03092  -0.07599 -0.02482 72  SER A OG  
461  N N   . GLY A 66  ? 0.41786 0.45274 0.39715 0.01148  -0.10583 -0.03548 73  GLY A N   
462  C CA  . GLY A 66  ? 0.38295 0.43482 0.39494 0.00302  -0.10364 -0.03456 73  GLY A CA  
463  C C   . GLY A 66  ? 0.37020 0.43429 0.39835 0.01182  -0.09549 -0.02615 73  GLY A C   
464  O O   . GLY A 66  ? 0.35770 0.40766 0.37727 0.01731  -0.08409 -0.02223 73  GLY A O   
465  N N   . LYS A 67  ? 0.36035 0.45044 0.41136 0.01372  -0.10195 -0.02292 74  LYS A N   
466  C CA  . LYS A 67  ? 0.34291 0.44106 0.40452 0.02652  -0.09503 -0.01615 74  LYS A CA  
467  C C   . LYS A 67  ? 0.37734 0.48061 0.45654 0.02465  -0.08296 -0.01616 74  LYS A C   
468  O O   . LYS A 67  ? 0.35846 0.45400 0.43586 0.03592  -0.07520 -0.01317 74  LYS A O   
469  C CB  . LYS A 67  ? 0.38543 0.51281 0.46204 0.03485  -0.10634 -0.01147 74  LYS A CB  
470  C CG  . LYS A 67  ? 0.61344 0.77523 0.71972 0.02347  -0.11370 -0.01168 74  LYS A CG  
471  C CD  . LYS A 67  ? 0.71725 0.91764 0.84706 0.03540  -0.11945 -0.00376 74  LYS A CD  
472  C CE  . LYS A 67  ? 0.74887 0.97112 0.88401 0.02884  -0.13985 -0.00313 74  LYS A CE  
473  N NZ  . LYS A 67  ? 0.73693 1.01143 0.90877 0.03187  -0.14611 0.00576  74  LYS A NZ  
474  N N   . GLU A 68  ? 0.30643 0.41914 0.39944 0.01118  -0.08198 -0.01932 75  GLU A N   
475  C CA  . GLU A 68  ? 0.29859 0.41970 0.40736 0.01061  -0.07042 -0.01805 75  GLU A CA  
476  C C   . GLU A 68  ? 0.31042 0.40220 0.40204 0.01104  -0.05916 -0.02087 75  GLU A C   
477  O O   . GLU A 68  ? 0.34113 0.41303 0.41676 0.00401  -0.05902 -0.02419 75  GLU A O   
478  C CB  . GLU A 68  ? 0.41374 0.55362 0.54249 -0.00538 -0.07321 -0.01783 75  GLU A CB  
479  C CG  . GLU A 68  ? 0.41205 0.59159 0.56740 -0.00708 -0.08297 -0.01158 75  GLU A CG  
480  C CD  . GLU A 68  ? 0.80223 0.98069 0.95195 -0.01704 -0.10127 -0.01447 75  GLU A CD  
481  O OE1 . GLU A 68  ? 0.77531 0.92073 0.89641 -0.01819 -0.10461 -0.02170 75  GLU A OE1 
482  O OE2 . GLU A 68  ? 0.85637 1.06884 1.02954 -0.02272 -0.11272 -0.00905 75  GLU A OE2 
483  N N   . LEU A 69  ? 0.26456 0.35460 0.35851 0.02058  -0.05041 -0.01947 76  LEU A N   
484  C CA  . LEU A 69  ? 0.26685 0.33160 0.34676 0.02016  -0.04200 -0.02157 76  LEU A CA  
485  C C   . LEU A 69  ? 0.27587 0.35098 0.36730 0.01862  -0.03350 -0.02269 76  LEU A C   
486  O O   . LEU A 69  ? 0.27376 0.35959 0.37130 0.03040  -0.02967 -0.02161 76  LEU A O   
487  C CB  . LEU A 69  ? 0.30081 0.34572 0.36664 0.03230  -0.04216 -0.01963 76  LEU A CB  
488  C CG  . LEU A 69  ? 0.31237 0.34774 0.36579 0.03544  -0.04980 -0.01564 76  LEU A CG  
489  C CD1 . LEU A 69  ? 0.40854 0.41891 0.44758 0.04600  -0.05034 -0.01205 76  LEU A CD1 
490  C CD2 . LEU A 69  ? 0.36409 0.38958 0.40601 0.02421  -0.04983 -0.01557 76  LEU A CD2 
491  N N   . HIS A 70  ? 0.27392 0.30448 0.27500 0.05029  -0.01798 0.00622  77  HIS A N   
492  C CA  . HIS A 70  ? 0.28838 0.31850 0.29473 0.04628  -0.01476 0.00365  77  HIS A CA  
493  C C   . HIS A 70  ? 0.27224 0.28318 0.27207 0.03219  -0.01896 -0.00794 77  HIS A C   
494  O O   . HIS A 70  ? 0.27641 0.27876 0.27113 0.02493  -0.02464 -0.01381 77  HIS A O   
495  C CB  . HIS A 70  ? 0.28612 0.35455 0.31473 0.04345  -0.01873 0.01062  77  HIS A CB  
496  C CG  . HIS A 70  ? 0.31699 0.40221 0.35480 0.02735  -0.03190 0.00535  77  HIS A CG  
497  N ND1 . HIS A 70  ? 0.33920 0.45783 0.38924 0.02654  -0.04059 0.01056  77  HIS A ND1 
498  C CD2 . HIS A 70  ? 0.31374 0.38613 0.34861 0.01203  -0.03761 -0.00499 77  HIS A CD2 
499  C CE1 . HIS A 70  ? 0.33333 0.45529 0.38484 0.00979  -0.05149 0.00142  77  HIS A CE1 
500  N NE2 . HIS A 70  ? 0.34948 0.44196 0.39196 0.00168  -0.04869 -0.00759 77  HIS A NE2 
501  N N   . ILE A 71  ? 0.25470 0.25974 0.25369 0.03071  -0.01480 -0.00975 78  ILE A N   
502  C CA  . ILE A 71  ? 0.25301 0.24411 0.24671 0.02035  -0.01800 -0.01791 78  ILE A CA  
503  C C   . ILE A 71  ? 0.29315 0.29934 0.29888 0.01514  -0.01744 -0.01440 78  ILE A C   
504  O O   . ILE A 71  ? 0.28302 0.29843 0.29267 0.02252  -0.00988 -0.00749 78  ILE A O   
505  C CB  . ILE A 71  ? 0.26850 0.23367 0.24417 0.02424  -0.01314 -0.02344 78  ILE A CB  
506  C CG1 . ILE A 71  ? 0.29913 0.24689 0.26503 0.02721  -0.01190 -0.02613 78  ILE A CG1 
507  C CG2 . ILE A 71  ? 0.29303 0.25099 0.26489 0.01544  -0.01762 -0.02959 78  ILE A CG2 
508  C CD1 . ILE A 71  ? 0.31544 0.23625 0.26307 0.02959  -0.00687 -0.03270 78  ILE A CD1 
509  N N   . ASN A 72  ? 0.26291 0.26937 0.27377 0.00317  -0.02351 -0.01839 79  ASN A N   
510  C CA  . ASN A 72  ? 0.24495 0.25904 0.26628 -0.00387 -0.02166 -0.01499 79  ASN A CA  
511  C C   . ASN A 72  ? 0.30688 0.30072 0.31695 -0.00621 -0.02069 -0.01890 79  ASN A C   
512  O O   . ASN A 72  ? 0.31452 0.29528 0.31648 -0.00858 -0.02546 -0.02555 79  ASN A O   
513  C CB  . ASN A 72  ? 0.22287 0.25202 0.25945 -0.01660 -0.02863 -0.01587 79  ASN A CB  
514  C CG  . ASN A 72  ? 0.22356 0.28157 0.27425 -0.01440 -0.03137 -0.01014 79  ASN A CG  
515  O OD1 . ASN A 72  ? 0.28496 0.35534 0.33989 -0.00283 -0.02454 -0.00178 79  ASN A OD1 
516  N ND2 . ASN A 72  ? 0.24185 0.31185 0.29879 -0.02439 -0.04124 -0.01430 79  ASN A ND2 
517  N N   . LEU A 73  ? 0.27294 0.26675 0.28297 -0.00409 -0.01374 -0.01309 80  LEU A N   
518  C CA  . LEU A 73  ? 0.26371 0.24213 0.26303 -0.00401 -0.01220 -0.01363 80  LEU A CA  
519  C C   . LEU A 73  ? 0.30186 0.28219 0.31364 -0.01280 -0.00864 -0.00781 80  LEU A C   
520  O O   . LEU A 73  ? 0.28179 0.27501 0.30487 -0.01367 -0.00170 0.00065  80  LEU A O   
521  C CB  . LEU A 73  ? 0.27829 0.25173 0.26164 0.00714  -0.00608 -0.01105 80  LEU A CB  
522  C CG  . LEU A 73  ? 0.28906 0.25599 0.25886 0.01429  -0.00776 -0.01757 80  LEU A CG  
523  C CD1 . LEU A 73  ? 0.33904 0.29844 0.28903 0.02443  -0.00144 -0.01679 80  LEU A CD1 
524  C CD2 . LEU A 73  ? 0.35065 0.30722 0.31479 0.00976  -0.01662 -0.02642 80  LEU A CD2 
525  N N   . ILE A 74  ? 0.25888 0.22518 0.26882 -0.01897 -0.01175 -0.01157 81  ILE A N   
526  C CA  . ILE A 74  ? 0.27112 0.23299 0.29255 -0.03016 -0.00831 -0.00813 81  ILE A CA  
527  C C   . ILE A 74  ? 0.33489 0.27565 0.34565 -0.02648 -0.00295 -0.00432 81  ILE A C   
528  O O   . ILE A 74  ? 0.35255 0.27850 0.35516 -0.02535 -0.00643 -0.00990 81  ILE A O   
529  C CB  . ILE A 74  ? 0.26567 0.22718 0.29441 -0.04239 -0.01618 -0.01702 81  ILE A CB  
530  C CG1 . ILE A 74  ? 0.29397 0.27938 0.33109 -0.04261 -0.02239 -0.01905 81  ILE A CG1 
531  C CG2 . ILE A 74  ? 0.31643 0.27101 0.35709 -0.05746 -0.01270 -0.01525 81  ILE A CG2 
532  C CD1 . ILE A 74  ? 0.36307 0.35107 0.40273 -0.05293 -0.03185 -0.02821 81  ILE A CD1 
533  N N   . PRO A 75  ? 0.32237 0.26212 0.33247 -0.02263 0.00671  0.00673  82  PRO A N   
534  C CA  . PRO A 75  ? 0.32170 0.24154 0.32140 -0.01741 0.01313  0.01335  82  PRO A CA  
535  C C   . PRO A 75  ? 0.41651 0.31884 0.42683 -0.03070 0.01871  0.01522  82  PRO A C   
536  O O   . PRO A 75  ? 0.42595 0.33651 0.45394 -0.04476 0.02056  0.01601  82  PRO A O   
537  C CB  . PRO A 75  ? 0.36275 0.28977 0.35525 -0.00714 0.02224  0.02546  82  PRO A CB  
538  C CG  . PRO A 75  ? 0.41758 0.36503 0.42639 -0.01331 0.02530  0.02780  82  PRO A CG  
539  C CD  . PRO A 75  ? 0.39250 0.35032 0.41090 -0.02082 0.01389  0.01552  82  PRO A CD  
540  N N   . ASN A 76  ? 0.38857 0.26645 0.38824 -0.02628 0.02169  0.01606  83  ASN A N   
541  C CA  . ASN A 76  ? 0.40760 0.25881 0.41225 -0.03768 0.02961  0.01776  83  ASN A CA  
542  C C   . ASN A 76  ? 0.46677 0.29526 0.45736 -0.02376 0.04058  0.03022  83  ASN A C   
543  O O   . ASN A 76  ? 0.46739 0.28565 0.44518 -0.01162 0.03828  0.02816  83  ASN A O   
544  C CB  . ASN A 76  ? 0.45923 0.29663 0.46308 -0.04738 0.02217  0.00251  83  ASN A CB  
545  C CG  . ASN A 76  ? 0.54597 0.35280 0.55382 -0.06337 0.02963  0.00069  83  ASN A CG  
546  O OD1 . ASN A 76  ? 0.58246 0.36208 0.58397 -0.05898 0.04220  0.01055  83  ASN A OD1 
547  N ND2 . ASN A 76  ? 0.62192 0.43267 0.63950 -0.08248 0.02188  -0.01179 83  ASN A ND2 
548  N N   . LYS A 77  ? 0.50557 0.32749 0.49964 -0.02480 0.05353  0.04478  84  LYS A N   
549  C CA  . LYS A 77  ? 0.49971 0.30253 0.47846 -0.00839 0.06505  0.06011  84  LYS A CA  
550  C C   . LYS A 77  ? 0.54286 0.30539 0.51669 -0.01049 0.07300  0.05987  84  LYS A C   
551  O O   . LYS A 77  ? 0.62399 0.37194 0.58228 0.00821  0.07839  0.06886  84  LYS A O   
552  C CB  . LYS A 77  ? 0.56019 0.36693 0.54235 -0.00765 0.07878  0.07767  84  LYS A CB  
553  C CG  . LYS A 77  ? 0.68295 0.52058 0.65480 0.00739  0.07525  0.08281  84  LYS A CG  
554  C CD  . LYS A 77  ? 0.65173 0.49736 0.62956 0.00602  0.08967  0.09855  84  LYS A CD  
555  C CE  . LYS A 77  ? 0.74292 0.61525 0.70519 0.02200  0.08688  0.10129  84  LYS A CE  
556  N NZ  . LYS A 77  ? 0.82054 0.70705 0.79307 0.01892  0.10039  0.11346  84  LYS A NZ  
557  N N   . GLN A 78  ? 0.60510 0.34929 0.59072 -0.03236 0.07383  0.04960  85  GLN A N   
558  C CA  . GLN A 78  ? 0.67143 0.37054 0.64852 -0.03558 0.08200  0.04600  85  GLN A CA  
559  C C   . GLN A 78  ? 0.66445 0.35911 0.62630 -0.01960 0.07493  0.03723  85  GLN A C   
560  O O   . GLN A 78  ? 0.68777 0.35424 0.63532 -0.00367 0.08494  0.04477  85  GLN A O   
561  C CB  . GLN A 78  ? 0.74933 0.43370 0.74009 -0.06510 0.08016  0.03200  85  GLN A CB  
562  C CG  . GLN A 78  ? 0.93690 0.56539 0.91824 -0.07317 0.09325  0.02983  85  GLN A CG  
563  C CD  . GLN A 78  ? 1.11949 0.72734 1.11310 -0.08878 0.10910  0.04292  85  GLN A CD  
564  O OE1 . GLN A 78  ? 1.12639 0.72441 1.11454 -0.07332 0.12396  0.06388  85  GLN A OE1 
565  N NE2 . GLN A 78  ? 1.17933 0.79051 1.19026 -0.11793 0.10281  0.03117  85  GLN A NE2 
566  N N   . ASP A 79  ? 0.58856 0.31139 0.55411 -0.02254 0.05913  0.02291  86  ASP A N   
567  C CA  . ASP A 79  ? 0.56305 0.28733 0.51760 -0.00854 0.05288  0.01548  86  ASP A CA  
568  C C   . ASP A 79  ? 0.51527 0.26933 0.46569 0.01275  0.04816  0.02520  86  ASP A C   
569  O O   . ASP A 79  ? 0.52466 0.28407 0.46921 0.02561  0.04423  0.02238  86  ASP A O   
570  C CB  . ASP A 79  ? 0.55539 0.29506 0.51483 -0.02159 0.03918  -0.00330 86  ASP A CB  
571  C CG  . ASP A 79  ? 0.74308 0.45903 0.70541 -0.04464 0.03990  -0.01556 86  ASP A CG  
572  O OD1 . ASP A 79  ? 0.81760 0.49494 0.77479 -0.04980 0.05232  -0.01249 86  ASP A OD1 
573  O OD2 . ASP A 79  ? 0.75579 0.49140 0.72476 -0.05777 0.02784  -0.02822 86  ASP A OD2 
574  N N   . ARG A 80  ? 0.49077 0.26543 0.44395 0.01590  0.04833  0.03591  87  ARG A N   
575  C CA  . ARG A 80  ? 0.40054 0.20610 0.34795 0.03212  0.04091  0.04190  87  ARG A CA  
576  C C   . ARG A 80  ? 0.43444 0.26536 0.38601 0.02975  0.02596  0.02777  87  ARG A C   
577  O O   . ARG A 80  ? 0.42629 0.27145 0.37392 0.04215  0.02009  0.02816  87  ARG A O   
578  C CB  . ARG A 80  ? 0.45284 0.25050 0.38810 0.05409  0.04752  0.05610  87  ARG A CB  
579  C CG  . ARG A 80  ? 0.56788 0.39474 0.49490 0.06794  0.04248  0.06647  87  ARG A CG  
580  C CD  . ARG A 80  ? 0.60802 0.44635 0.52705 0.08930  0.03979  0.07517  87  ARG A CD  
581  N NE  . ARG A 80  ? 0.62579 0.43479 0.53682 0.10306  0.05580  0.09166  87  ARG A NE  
582  C CZ  . ARG A 80  ? 0.81885 0.62409 0.72622 0.12149  0.05920  0.09956  87  ARG A CZ  
583  N NH1 . ARG A 80  ? 0.65492 0.48884 0.56833 0.12767  0.04706  0.09319  87  ARG A NH1 
584  N NH2 . ARG A 80  ? 0.74685 0.51907 0.64526 0.13475  0.07650  0.11564  87  ARG A NH2 
585  N N   . THR A 81  ? 0.38046 0.21930 0.34152 0.01367  0.02013  0.01660  88  THR A N   
586  C CA  . THR A 81  ? 0.34912 0.20880 0.31373 0.01077  0.00799  0.00469  88  THR A CA  
587  C C   . THR A 81  ? 0.37184 0.25292 0.34138 0.00482  0.00296  0.00283  88  THR A C   
588  O O   . THR A 81  ? 0.38592 0.26582 0.36166 -0.00294 0.00823  0.00677  88  THR A O   
589  C CB  . THR A 81  ? 0.40072 0.24853 0.36887 0.00008  0.00562  -0.00785 88  THR A CB  
590  O OG1 . THR A 81  ? 0.43341 0.27118 0.40870 -0.01600 0.00844  -0.01074 88  THR A OG1 
591  C CG2 . THR A 81  ? 0.43529 0.26018 0.39521 0.00891  0.01171  -0.00765 88  THR A CG2 
592  N N   . LEU A 82  ? 0.32590 0.22587 0.29317 0.00876  -0.00599 -0.00250 89  LEU A N   
593  C CA  . LEU A 82  ? 0.30977 0.22537 0.27999 0.00400  -0.01044 -0.00703 89  LEU A CA  
594  C C   . LEU A 82  ? 0.36294 0.28343 0.33816 -0.00160 -0.01776 -0.01780 89  LEU A C   
595  O O   . LEU A 82  ? 0.32968 0.25255 0.30228 0.00263  -0.02210 -0.02115 89  LEU A O   
596  C CB  . LEU A 82  ? 0.31216 0.23979 0.27088 0.01329  -0.01320 -0.00448 89  LEU A CB  
597  C CG  . LEU A 82  ? 0.34184 0.27958 0.29941 0.01097  -0.01577 -0.00974 89  LEU A CG  
598  C CD1 . LEU A 82  ? 0.34316 0.28217 0.30830 0.00720  -0.00740 -0.00372 89  LEU A CD1 
599  C CD2 . LEU A 82  ? 0.34985 0.29374 0.29081 0.01920  -0.01940 -0.01058 89  LEU A CD2 
600  N N   . THR A 83  ? 0.29153 0.21602 0.27489 -0.01053 -0.01870 -0.02171 90  THR A N   
601  C CA  . THR A 83  ? 0.28343 0.21224 0.26950 -0.01473 -0.02469 -0.03010 90  THR A CA  
602  C C   . THR A 83  ? 0.34528 0.28804 0.33262 -0.01347 -0.02731 -0.03109 90  THR A C   
603  O O   . THR A 83  ? 0.32284 0.27331 0.31487 -0.01419 -0.02413 -0.02672 90  THR A O   
604  C CB  . THR A 83  ? 0.30700 0.22973 0.29879 -0.02515 -0.02503 -0.03429 90  THR A CB  
605  O OG1 . THR A 83  ? 0.34596 0.24807 0.33308 -0.02560 -0.02052 -0.03433 90  THR A OG1 
606  C CG2 . THR A 83  ? 0.35693 0.28565 0.34755 -0.02717 -0.03118 -0.04180 90  THR A CG2 
607  N N   . ILE A 84  ? 0.28063 0.22557 0.26404 -0.01078 -0.03137 -0.03568 91  ILE A N   
608  C CA  . ILE A 84  ? 0.26121 0.21269 0.24358 -0.00884 -0.03229 -0.03694 91  ILE A CA  
609  C C   . ILE A 84  ? 0.33266 0.28748 0.31896 -0.01206 -0.03514 -0.04000 91  ILE A C   
610  O O   . ILE A 84  ? 0.31487 0.26544 0.29873 -0.01252 -0.03702 -0.04339 91  ILE A O   
611  C CB  . ILE A 84  ? 0.27266 0.22083 0.24622 -0.00495 -0.03389 -0.03972 91  ILE A CB  
612  C CG1 . ILE A 84  ? 0.36700 0.31406 0.33194 -0.00064 -0.03264 -0.03728 91  ILE A CG1 
613  C CG2 . ILE A 84  ? 0.32729 0.27427 0.29774 -0.00308 -0.03272 -0.04151 91  ILE A CG2 
614  C CD1 . ILE A 84  ? 0.42446 0.37151 0.38885 0.00089  -0.03433 -0.03481 91  ILE A CD1 
615  N N   . VAL A 85  ? 0.28856 0.25384 0.28099 -0.01322 -0.03517 -0.03767 92  VAL A N   
616  C CA  . VAL A 85  ? 0.28032 0.25272 0.27457 -0.01521 -0.03908 -0.03946 92  VAL A CA  
617  C C   . VAL A 85  ? 0.31895 0.29694 0.31165 -0.00760 -0.03727 -0.03583 92  VAL A C   
618  O O   . VAL A 85  ? 0.32671 0.31049 0.32240 -0.00271 -0.03333 -0.03104 92  VAL A O   
619  C CB  . VAL A 85  ? 0.32874 0.31343 0.33250 -0.02315 -0.04240 -0.03910 92  VAL A CB  
620  C CG1 . VAL A 85  ? 0.34979 0.34383 0.35122 -0.02475 -0.04864 -0.04202 92  VAL A CG1 
621  C CG2 . VAL A 85  ? 0.39883 0.37145 0.40322 -0.03107 -0.04155 -0.04205 92  VAL A CG2 
622  N N   . ASP A 86  ? 0.27578 0.25078 0.26290 -0.00520 -0.03834 -0.03692 93  ASP A N   
623  C CA  . ASP A 86  ? 0.25771 0.23551 0.24260 0.00313  -0.03524 -0.03168 93  ASP A CA  
624  C C   . ASP A 86  ? 0.30169 0.28925 0.28452 0.00438  -0.03906 -0.03004 93  ASP A C   
625  O O   . ASP A 86  ? 0.33486 0.32064 0.31369 -0.00093 -0.04290 -0.03499 93  ASP A O   
626  C CB  . ASP A 86  ? 0.30795 0.26644 0.28447 0.00640  -0.02984 -0.03292 93  ASP A CB  
627  C CG  . ASP A 86  ? 0.33913 0.28913 0.31222 0.00246  -0.03049 -0.03602 93  ASP A CG  
628  O OD1 . ASP A 86  ? 0.37058 0.32391 0.34114 0.00502  -0.03028 -0.03306 93  ASP A OD1 
629  O OD2 . ASP A 86  ? 0.36496 0.30820 0.33837 -0.00253 -0.03120 -0.04045 93  ASP A OD2 
630  N N   . THR A 87  ? 0.25571 0.25403 0.23936 0.01328  -0.03744 -0.02244 94  THR A N   
631  C CA  . THR A 87  ? 0.25960 0.26881 0.23800 0.01753  -0.04092 -0.01881 94  THR A CA  
632  C C   . THR A 87  ? 0.31987 0.31192 0.28782 0.02645  -0.03287 -0.01359 94  THR A C   
633  O O   . THR A 87  ? 0.32786 0.32749 0.29135 0.03700  -0.03104 -0.00465 94  THR A O   
634  C CB  . THR A 87  ? 0.31330 0.35207 0.30096 0.02237  -0.04563 -0.01154 94  THR A CB  
635  O OG1 . THR A 87  ? 0.29560 0.33466 0.28916 0.03240  -0.03760 -0.00378 94  THR A OG1 
636  C CG2 . THR A 87  ? 0.34459 0.40109 0.34356 0.00893  -0.05480 -0.01762 94  THR A CG2 
637  N N   . GLY A 88  ? 0.31136 0.28100 0.27602 0.02189  -0.02787 -0.01829 95  GLY A N   
638  C CA  . GLY A 88  ? 0.32766 0.27849 0.28491 0.02630  -0.01940 -0.01398 95  GLY A CA  
639  C C   . GLY A 88  ? 0.34380 0.29615 0.29405 0.02713  -0.01889 -0.01139 95  GLY A C   
640  O O   . GLY A 88  ? 0.31601 0.28505 0.26293 0.02738  -0.02579 -0.01247 95  GLY A O   
641  N N   . ILE A 89  ? 0.29527 0.22945 0.24223 0.02687  -0.01018 -0.00821 96  ILE A N   
642  C CA  . ILE A 89  ? 0.30466 0.23947 0.24386 0.03004  -0.00624 -0.00275 96  ILE A CA  
643  C C   . ILE A 89  ? 0.36322 0.30646 0.30241 0.02340  -0.01099 -0.01025 96  ILE A C   
644  O O   . ILE A 89  ? 0.34953 0.29822 0.27799 0.02814  -0.00969 -0.00724 96  ILE A O   
645  C CB  . ILE A 89  ? 0.34128 0.25344 0.28047 0.02928  0.00624  0.00358  96  ILE A CB  
646  C CG1 . ILE A 89  ? 0.40887 0.32180 0.33811 0.03654  0.01355  0.01395  96  ILE A CG1 
647  C CG2 . ILE A 89  ? 0.37379 0.27721 0.32478 0.01497  0.00636  -0.00512 96  ILE A CG2 
648  C CD1 . ILE A 89  ? 0.53769 0.42757 0.46373 0.04082  0.02781  0.02562  96  ILE A CD1 
649  N N   . GLY A 90  ? 0.32652 0.26982 0.27488 0.01448  -0.01544 -0.01932 97  GLY A N   
650  C CA  . GLY A 90  ? 0.32969 0.27747 0.27698 0.01097  -0.01764 -0.02522 97  GLY A CA  
651  C C   . GLY A 90  ? 0.38493 0.32759 0.33599 0.00964  -0.00885 -0.02170 97  GLY A C   
652  O O   . GLY A 90  ? 0.35910 0.29379 0.31495 0.00846  -0.00167 -0.01541 97  GLY A O   
653  N N   . MET A 91  ? 0.33906 0.28572 0.28888 0.00957  -0.00832 -0.02546 98  MET A N   
654  C CA  . MET A 91  ? 0.31778 0.26584 0.27599 0.00869  0.00052  -0.02114 98  MET A CA  
655  C C   . MET A 91  ? 0.32811 0.27841 0.27161 0.01703  0.00584  -0.02020 98  MET A C   
656  O O   . MET A 91  ? 0.33577 0.28465 0.26589 0.01990  0.00049  -0.02793 98  MET A O   
657  C CB  . MET A 91  ? 0.31654 0.26972 0.29127 0.00233  -0.00231 -0.02548 98  MET A CB  
658  C CG  . MET A 91  ? 0.30541 0.25562 0.29104 -0.00599 -0.00704 -0.02729 98  MET A CG  
659  S SD  . MET A 91  ? 0.38694 0.34812 0.38784 -0.01111 -0.01247 -0.03163 98  MET A SD  
660  C CE  . MET A 91  ? 0.39911 0.35511 0.38859 -0.00724 -0.02002 -0.03820 98  MET A CE  
661  N N   . THR A 92  ? 0.33030 0.28223 0.27500 0.02041  0.01729  -0.01095 99  THR A N   
662  C CA  . THR A 92  ? 0.35821 0.31197 0.28742 0.03018  0.02528  -0.00905 99  THR A CA  
663  C C   . THR A 92  ? 0.34297 0.30300 0.28396 0.03093  0.02987  -0.01110 99  THR A C   
664  O O   . THR A 92  ? 0.33138 0.29826 0.29498 0.02345  0.02698  -0.01162 99  THR A O   
665  C CB  . THR A 92  ? 0.38716 0.34124 0.31297 0.03521  0.03838  0.00444  99  THR A CB  
666  O OG1 . THR A 92  ? 0.40638 0.36578 0.35946 0.02674  0.04616  0.01176  99  THR A OG1 
667  C CG2 . THR A 92  ? 0.36475 0.31230 0.27965 0.03735  0.03562  0.00950  99  THR A CG2 
668  N N   . LYS A 93  ? 0.35987 0.31804 0.28337 0.04176  0.03751  -0.01184 100 LYS A N   
669  C CA  . LYS A 93  ? 0.38063 0.34543 0.31512 0.04655  0.04509  -0.01099 100 LYS A CA  
670  C C   . LYS A 93  ? 0.35348 0.33710 0.31925 0.04164  0.05367  0.00158  100 LYS A C   
671  O O   . LYS A 93  ? 0.33967 0.33684 0.32891 0.03842  0.05246  0.00260  100 LYS A O   
672  C CB  . LYS A 93  ? 0.41186 0.36836 0.31865 0.06125  0.05523  -0.01304 100 LYS A CB  
673  C CG  . LYS A 93  ? 0.46206 0.42181 0.37642 0.07008  0.06409  -0.01274 100 LYS A CG  
674  C CD  . LYS A 93  ? 0.49694 0.44153 0.37759 0.08620  0.07526  -0.01721 100 LYS A CD  
675  C CE  . LYS A 93  ? 0.55092 0.49220 0.43614 0.09677  0.08329  -0.01866 100 LYS A CE  
676  N NZ  . LYS A 93  ? 0.59916 0.53256 0.46035 0.11603  0.10181  -0.01666 100 LYS A NZ  
677  N N   . ALA A 94  ? 0.36151 0.34707 0.32872 0.04015  0.06190  0.01179  101 ALA A N   
678  C CA  . ALA A 94  ? 0.39428 0.39664 0.39280 0.03188  0.07068  0.02376  101 ALA A CA  
679  C C   . ALA A 94  ? 0.39339 0.39980 0.41622 0.01518  0.05852  0.01950  101 ALA A C   
680  O O   . ALA A 94  ? 0.33314 0.35960 0.38514 0.00711  0.05925  0.02339  101 ALA A O   
681  C CB  . ALA A 94  ? 0.39448 0.39163 0.38666 0.03296  0.08307  0.03605  101 ALA A CB  
682  N N   . ASP A 95  ? 0.34324 0.33294 0.35389 0.01038  0.04715  0.01158  102 ASP A N   
683  C CA  . ASP A 95  ? 0.30522 0.29538 0.33180 -0.00293 0.03549  0.00528  102 ASP A CA  
684  C C   . ASP A 95  ? 0.35464 0.36031 0.39363 -0.00247 0.02860  0.00020  102 ASP A C   
685  O O   . ASP A 95  ? 0.32581 0.34792 0.38888 -0.01241 0.02500  0.00136  102 ASP A O   
686  C CB  . ASP A 95  ? 0.36821 0.33953 0.37638 -0.00308 0.02580  -0.00234 102 ASP A CB  
687  C CG  . ASP A 95  ? 0.38211 0.33843 0.38174 -0.00371 0.03167  0.00416  102 ASP A CG  
688  O OD1 . ASP A 95  ? 0.41015 0.36561 0.42305 -0.01073 0.04110  0.01251  102 ASP A OD1 
689  O OD2 . ASP A 95  ? 0.40045 0.34642 0.38089 0.00295  0.02716  0.00175  102 ASP A OD2 
690  N N   . LEU A 96  ? 0.30314 0.30332 0.32491 0.00904  0.02668  -0.00526 103 LEU A N   
691  C CA  . LEU A 96  ? 0.31823 0.32704 0.34741 0.01205  0.02100  -0.00920 103 LEU A CA  
692  C C   . LEU A 96  ? 0.37792 0.41274 0.43074 0.01542  0.02841  -0.00026 103 LEU A C   
693  O O   . LEU A 96  ? 0.37073 0.42252 0.44130 0.01259  0.02171  0.00012  103 LEU A O   
694  C CB  . LEU A 96  ? 0.32718 0.31896 0.33152 0.02316  0.02062  -0.01635 103 LEU A CB  
695  C CG  . LEU A 96  ? 0.32563 0.29882 0.31169 0.01912  0.01092  -0.02538 103 LEU A CG  
696  C CD1 . LEU A 96  ? 0.39104 0.34817 0.35400 0.02748  0.01183  -0.03277 103 LEU A CD1 
697  C CD2 . LEU A 96  ? 0.31781 0.29328 0.31503 0.01109  0.00034  -0.02885 103 LEU A CD2 
698  N N   . ILE A 97  ? 0.34050 0.38149 0.39359 0.02296  0.04253  0.00807  104 ILE A N   
699  C CA  . ILE A 97  ? 0.33369 0.40257 0.40948 0.02998  0.05251  0.01856  104 ILE A CA  
700  C C   . ILE A 97  ? 0.43049 0.52611 0.54051 0.01476  0.05369  0.02767  104 ILE A C   
701  O O   . ILE A 97  ? 0.44496 0.57183 0.58398 0.01173  0.05093  0.03300  104 ILE A O   
702  C CB  . ILE A 97  ? 0.39070 0.45331 0.44833 0.04751  0.06971  0.02369  104 ILE A CB  
703  C CG1 . ILE A 97  ? 0.52819 0.56109 0.54934 0.06036  0.06854  0.01237  104 ILE A CG1 
704  C CG2 . ILE A 97  ? 0.47084 0.56485 0.55377 0.05742  0.08191  0.03619  104 ILE A CG2 
705  C CD1 . ILE A 97  ? 0.60127 0.62740 0.62247 0.05853  0.05618  0.00414  104 ILE A CD1 
706  N N   . ASN A 98  ? 0.30425 0.38864 0.41153 0.00529  0.05849  0.03046  105 ASN A N   
707  C CA  . ASN A 98  ? 0.34619 0.45083 0.48409 -0.00922 0.06512  0.04094  105 ASN A CA  
708  C C   . ASN A 98  ? 0.33566 0.42782 0.48003 -0.03081 0.05451  0.03472  105 ASN A C   
709  O O   . ASN A 98  ? 0.32716 0.44067 0.50058 -0.04755 0.04793  0.03505  105 ASN A O   
710  C CB  . ASN A 98  ? 0.42120 0.52036 0.55098 -0.00156 0.08471  0.05277  105 ASN A CB  
711  C CG  . ASN A 98  ? 0.72413 0.83189 0.84285 0.02100  0.09776  0.05835  105 ASN A CG  
712  O OD1 . ASN A 98  ? 0.69296 0.83205 0.83704 0.02595  0.10352  0.06630  105 ASN A OD1 
713  N ND2 . ASN A 98  ? 0.74351 0.82412 0.82323 0.03553  0.10253  0.05407  105 ASN A ND2 
714  N N   . ASN A 99  ? 0.41532 0.41077 0.33094 0.06219  0.03582  0.08634  106 ASN A N   
715  C CA  . ASN A 99  ? 0.38250 0.38467 0.32780 0.06340  0.03709  0.09959  106 ASN A CA  
716  C C   . ASN A 99  ? 0.40060 0.40989 0.38655 0.04891  0.03130  0.08948  106 ASN A C   
717  O O   . ASN A 99  ? 0.40201 0.41043 0.41914 0.04465  0.04190  0.09472  106 ASN A O   
718  C CB  . ASN A 99  ? 0.40742 0.42041 0.33497 0.07369  0.02303  0.10781  106 ASN A CB  
719  C CG  . ASN A 99  ? 0.55754 0.56570 0.43366 0.09117  0.02589  0.11845  106 ASN A CG  
720  O OD1 . ASN A 99  ? 0.58023 0.57074 0.43978 0.09837  0.04752  0.12736  106 ASN A OD1 
721  N ND2 . ASN A 99  ? 0.54106 0.56643 0.39204 0.09924  0.00418  0.11834  106 ASN A ND2 
722  N N   . LEU A 100 ? 0.38776 0.40287 0.37325 0.04110  0.01626  0.07370  107 LEU A N   
723  C CA  . LEU A 100 ? 0.34712 0.36570 0.36295 0.03024  0.01312  0.06573  107 LEU A CA  
724  C C   . LEU A 100 ? 0.35601 0.37266 0.38590 0.02586  0.02319  0.06425  107 LEU A C   
725  O O   . LEU A 100 ? 0.45625 0.47729 0.51026 0.01929  0.02394  0.06256  107 LEU A O   
726  C CB  . LEU A 100 ? 0.34352 0.36502 0.35692 0.02481  0.00058  0.05099  107 LEU A CB  
727  C CG  . LEU A 100 ? 0.38987 0.42173 0.40439 0.02717  -0.01314 0.05129  107 LEU A CG  
728  C CD1 . LEU A 100 ? 0.36893 0.40396 0.38846 0.01988  -0.02298 0.03369  107 LEU A CD1 
729  C CD2 . LEU A 100 ? 0.47534 0.50950 0.51752 0.02673  -0.01031 0.06119  107 LEU A CD2 
730  N N   . GLY A 101 ? 0.41149 0.42305 0.42696 0.02979  0.03086  0.06438  108 GLY A N   
731  C CA  . GLY A 101 ? 0.52770 0.54320 0.56269 0.02801  0.03960  0.06606  108 GLY A CA  
732  C C   . GLY A 101 ? 0.42367 0.44411 0.48445 0.02711  0.04931  0.07486  108 GLY A C   
733  O O   . GLY A 101 ? 0.40405 0.43721 0.49364 0.02089  0.04850  0.07198  108 GLY A O   
734  N N   . THR A 102 ? 0.35820 0.36957 0.41001 0.03377  0.05936  0.08534  109 THR A N   
735  C CA  . THR A 102 ? 0.34266 0.35463 0.42563 0.03234  0.07408  0.09354  109 THR A CA  
736  C C   . THR A 102 ? 0.40880 0.42819 0.51930 0.02136  0.06741  0.08612  109 THR A C   
737  O O   . THR A 102 ? 0.39414 0.42269 0.54032 0.01186  0.07189  0.08027  109 THR A O   
738  C CB  . THR A 102 ? 0.44810 0.44476 0.51187 0.04537  0.09005  0.11003  109 THR A CB  
739  O OG1 . THR A 102 ? 0.53086 0.51718 0.56034 0.05548  0.09712  0.11423  109 THR A OG1 
740  C CG2 . THR A 102 ? 0.48300 0.47577 0.58606 0.04413  0.11278  0.11925  109 THR A CG2 
741  N N   . ILE A 103 ? 0.37349 0.38968 0.46999 0.02192  0.05732  0.08477  110 ILE A N   
742  C CA  . ILE A 103 ? 0.43721 0.45533 0.55685 0.01187  0.05471  0.07712  110 ILE A CA  
743  C C   . ILE A 103 ? 0.44292 0.47231 0.57027 0.00133  0.04290  0.06125  110 ILE A C   
744  O O   . ILE A 103 ? 0.55024 0.58455 0.70053 -0.00938 0.04400  0.05123  110 ILE A O   
745  C CB  . ILE A 103 ? 0.56347 0.57674 0.67045 0.01660  0.04789  0.08126  110 ILE A CB  
746  C CG1 . ILE A 103 ? 0.56445 0.57226 0.65586 0.03163  0.05555  0.09997  110 ILE A CG1 
747  C CG2 . ILE A 103 ? 0.61171 0.62072 0.74383 0.00760  0.05258  0.07561  110 ILE A CG2 
748  C CD1 . ILE A 103 ? 0.62817 0.62588 0.74392 0.03496  0.07929  0.11336  110 ILE A CD1 
749  N N   . ALA A 104 ? 0.34251 0.37566 0.44942 0.00495  0.03281  0.05847  111 ALA A N   
750  C CA  . ALA A 104 ? 0.43479 0.47757 0.54306 -0.00004 0.02304  0.04827  111 ALA A CA  
751  C C   . ALA A 104 ? 0.49906 0.55982 0.62915 -0.00349 0.02312  0.04581  111 ALA A C   
752  O O   . ALA A 104 ? 0.44867 0.52270 0.58327 -0.00835 0.01340  0.03682  111 ALA A O   
753  C CB  . ALA A 104 ? 0.44948 0.48798 0.53459 0.00648  0.01801  0.04832  111 ALA A CB  
754  N N   . LYS A 105 ? 0.39267 0.45576 0.53686 -0.00019 0.03387  0.05388  112 LYS A N   
755  C CA  . LYS A 105 ? 0.31632 0.40135 0.49295 -0.00406 0.03402  0.05162  112 LYS A CA  
756  C C   . LYS A 105 ? 0.39310 0.48957 0.59985 -0.01846 0.03105  0.03771  112 LYS A C   
757  O O   . LYS A 105 ? 0.32151 0.44294 0.54365 -0.02495 0.01748  0.02655  112 LYS A O   
758  C CB  . LYS A 105 ? 0.36145 0.44170 0.55180 0.00251  0.05209  0.06405  112 LYS A CB  
759  C CG  . LYS A 105 ? 0.38868 0.49406 0.61666 0.00188  0.05319  0.06518  112 LYS A CG  
760  C CD  . LYS A 105 ? 0.42040 0.51406 0.66313 0.00892  0.07768  0.07873  112 LYS A CD  
761  C CE  . LYS A 105 ? 0.61608 0.73180 0.89263 0.01304  0.08142  0.08456  112 LYS A CE  
762  N NZ  . LYS A 105 ? 0.61095 0.75604 0.94986 0.00111  0.08015  0.07645  112 LYS A NZ  
763  N N   . SER A 106 ? 0.35701 0.43621 0.57290 -0.02309 0.04448  0.03784  113 SER A N   
764  C CA  . SER A 106 ? 0.33783 0.42280 0.58633 -0.03885 0.04732  0.02171  113 SER A CA  
765  C C   . SER A 106 ? 0.34306 0.42798 0.57103 -0.04596 0.03272  0.00645  113 SER A C   
766  O O   . SER A 106 ? 0.35220 0.45293 0.59648 -0.05935 0.02446  -0.01324 113 SER A O   
767  C CB  . SER A 106 ? 0.42885 0.49059 0.69522 -0.03941 0.07230  0.02936  113 SER A CB  
768  O OG  . SER A 106 ? 0.56417 0.60497 0.79535 -0.02596 0.07585  0.04546  113 SER A OG  
769  N N   . GLY A 107 ? 0.38469 0.45237 0.57709 -0.03735 0.02986  0.01394  114 GLY A N   
770  C CA  . GLY A 107 ? 0.33286 0.39578 0.50473 -0.04185 0.02086  0.00201  114 GLY A CA  
771  C C   . GLY A 107 ? 0.29853 0.38370 0.45595 -0.04078 0.00252  -0.00572 114 GLY A C   
772  O O   . GLY A 107 ? 0.27853 0.36891 0.42722 -0.04856 -0.00536 -0.02177 114 GLY A O   
773  N N   . THR A 108 ? 0.26712 0.36483 0.41948 -0.02956 -0.00292 0.00651  115 THR A N   
774  C CA  . THR A 108 ? 0.32834 0.44983 0.46978 -0.02392 -0.01842 0.00513  115 THR A CA  
775  C C   . THR A 108 ? 0.34752 0.50143 0.51716 -0.03476 -0.03027 -0.00973 115 THR A C   
776  O O   . THR A 108 ? 0.30112 0.47293 0.45532 -0.03623 -0.04628 -0.02099 115 THR A O   
777  C CB  . THR A 108 ? 0.34481 0.47083 0.48338 -0.00931 -0.01599 0.02291  115 THR A CB  
778  O OG1 . THR A 108 ? 0.39336 0.49252 0.50517 -0.00148 -0.00799 0.03086  115 THR A OG1 
779  C CG2 . THR A 108 ? 0.33427 0.48862 0.46891 -0.00031 -0.02963 0.02634  115 THR A CG2 
780  N N   . LYS A 109 ? 0.25882 0.42244 0.47044 -0.04162 -0.02252 -0.01003 116 LYS A N   
781  C CA  . LYS A 109 ? 0.31082 0.50810 0.56213 -0.05538 -0.03290 -0.02786 116 LYS A CA  
782  C C   . LYS A 109 ? 0.29658 0.49141 0.53916 -0.07164 -0.03956 -0.05413 116 LYS A C   
783  O O   . LYS A 109 ? 0.30564 0.53228 0.54767 -0.07794 -0.06097 -0.07170 116 LYS A O   
784  C CB  . LYS A 109 ? 0.32058 0.51685 0.62340 -0.06248 -0.01408 -0.02532 116 LYS A CB  
785  C CG  . LYS A 109 ? 0.60399 0.82342 0.93669 -0.05276 -0.01291 -0.00986 116 LYS A CG  
786  C CD  . LYS A 109 ? 0.69336 0.89612 1.06534 -0.05563 0.01507  -0.00199 116 LYS A CD  
787  C CE  . LYS A 109 ? 0.55342 0.74901 0.92227 -0.03800 0.02846  0.02305  116 LYS A CE  
788  N NZ  . LYS A 109 ? 0.58230 0.80608 0.94340 -0.02677 0.01021  0.03028  116 LYS A NZ  
789  N N   . ALA A 110 ? 0.29330 0.45104 0.52796 -0.07772 -0.02093 -0.05706 117 ALA A N   
790  C CA  . ALA A 110 ? 0.30131 0.44838 0.52803 -0.09358 -0.02024 -0.08235 117 ALA A CA  
791  C C   . ALA A 110 ? 0.26983 0.41792 0.44303 -0.08686 -0.03681 -0.08761 117 ALA A C   
792  O O   . ALA A 110 ? 0.32293 0.48311 0.48466 -0.09861 -0.04869 -0.11295 117 ALA A O   
793  C CB  . ALA A 110 ? 0.34351 0.44862 0.57535 -0.09663 0.00737  -0.07727 117 ALA A CB  
794  N N   . PHE A 111 ? 0.25430 0.38756 0.39344 -0.06821 -0.03553 -0.06522 118 PHE A N   
795  C CA  . PHE A 111 ? 0.31078 0.43925 0.40017 -0.05862 -0.04456 -0.06567 118 PHE A CA  
796  C C   . PHE A 111 ? 0.32175 0.49228 0.39977 -0.05330 -0.07010 -0.07070 118 PHE A C   
797  O O   . PHE A 111 ? 0.34178 0.51820 0.38437 -0.05428 -0.08151 -0.08544 118 PHE A O   
798  C CB  . PHE A 111 ? 0.27781 0.38257 0.34638 -0.04092 -0.03418 -0.04082 118 PHE A CB  
799  C CG  . PHE A 111 ? 0.32495 0.41806 0.34696 -0.02841 -0.03566 -0.03671 118 PHE A CG  
800  C CD1 . PHE A 111 ? 0.35234 0.42688 0.34639 -0.03449 -0.03118 -0.05234 118 PHE A CD1 
801  C CD2 . PHE A 111 ? 0.37842 0.47295 0.38557 -0.00979 -0.03559 -0.01612 118 PHE A CD2 
802  C CE1 . PHE A 111 ? 0.39877 0.45795 0.34866 -0.02057 -0.02738 -0.04575 118 PHE A CE1 
803  C CE2 . PHE A 111 ? 0.42060 0.49996 0.38865 0.00363  -0.03074 -0.00940 118 PHE A CE2 
804  C CZ  . PHE A 111 ? 0.43520 0.49678 0.37347 -0.00099 -0.02655 -0.02326 118 PHE A CZ  
805  N N   . MET A 112 ? 0.31534 0.51663 0.42279 -0.04648 -0.07887 -0.05797 119 MET A N   
806  C CA  . MET A 112 ? 0.34486 0.59361 0.45007 -0.03909 -0.10468 -0.05923 119 MET A CA  
807  C C   . MET A 112 ? 0.36921 0.64881 0.49040 -0.05956 -0.12332 -0.09242 119 MET A C   
808  O O   . MET A 112 ? 0.45033 0.75899 0.54057 -0.05514 -0.14695 -0.10252 119 MET A O   
809  C CB  . MET A 112 ? 0.39674 0.67114 0.54117 -0.02866 -0.10593 -0.03846 119 MET A CB  
810  C CG  . MET A 112 ? 0.36601 0.60931 0.49530 -0.01120 -0.08661 -0.01085 119 MET A CG  
811  S SD  . MET A 112 ? 0.64825 0.88936 0.72227 0.01394  -0.09161 0.00694  119 MET A SD  
812  C CE  . MET A 112 ? 0.42500 0.66322 0.51846 0.03269  -0.07640 0.03718  119 MET A CE  
813  N N   . GLU A 113 ? 0.40289 0.67753 0.57232 -0.08161 -0.11239 -0.11034 120 GLU A N   
814  C CA  . GLU A 113 ? 0.41842 0.71782 0.60770 -0.10544 -0.12640 -0.14807 120 GLU A CA  
815  C C   . GLU A 113 ? 0.43729 0.71300 0.56830 -0.11093 -0.12782 -0.16907 120 GLU A C   
816  O O   . GLU A 113 ? 0.43306 0.74043 0.54361 -0.11811 -0.15295 -0.19464 120 GLU A O   
817  C CB  . GLU A 113 ? 0.43058 0.71740 0.68410 -0.12768 -0.10453 -0.16209 120 GLU A CB  
818  C CG  . GLU A 113 ? 0.58305 0.87206 0.88390 -0.11907 -0.08999 -0.13549 120 GLU A CG  
819  C CD  . GLU A 113 ? 0.67654 0.98661 1.05249 -0.13839 -0.08335 -0.15175 120 GLU A CD  
820  O OE1 . GLU A 113 ? 0.87555 1.15634 1.26222 -0.15522 -0.06494 -0.17004 120 GLU A OE1 
821  O OE2 . GLU A 113 ? 0.74031 1.08046 1.15087 -0.13064 -0.08996 -0.13701 120 GLU A OE2 
822  N N   . ALA A 114 ? 0.44328 0.66474 0.54614 -0.10670 -0.10130 -0.15857 121 ALA A N   
823  C CA  . ALA A 114 ? 0.46607 0.65818 0.51585 -0.11100 -0.09593 -0.17651 121 ALA A CA  
824  C C   . ALA A 114 ? 0.44940 0.65844 0.43496 -0.09085 -0.11719 -0.16919 121 ALA A C   
825  O O   . ALA A 114 ? 0.51622 0.73058 0.45964 -0.09707 -0.12922 -0.19466 121 ALA A O   
826  C CB  . ALA A 114 ? 0.45733 0.59230 0.49969 -0.10713 -0.06253 -0.16087 121 ALA A CB  
827  N N   . LEU A 115 ? 0.44404 0.65913 0.41874 -0.06553 -0.11941 -0.13433 122 LEU A N   
828  C CA  . LEU A 115 ? 0.52300 0.75269 0.43950 -0.04201 -0.13474 -0.12132 122 LEU A CA  
829  C C   . LEU A 115 ? 0.65917 0.94870 0.56990 -0.04476 -0.17167 -0.14066 122 LEU A C   
830  O O   . LEU A 115 ? 0.65794 0.95516 0.50790 -0.03684 -0.18582 -0.15079 122 LEU A O   
831  C CB  . LEU A 115 ? 0.44126 0.66957 0.36202 -0.01633 -0.12745 -0.08151 122 LEU A CB  
832  C CG  . LEU A 115 ? 0.44263 0.61577 0.35206 -0.00850 -0.09581 -0.06272 122 LEU A CG  
833  C CD1 . LEU A 115 ? 0.50456 0.67903 0.42111 0.01399  -0.08909 -0.02921 122 LEU A CD1 
834  C CD2 . LEU A 115 ? 0.53249 0.67072 0.38326 -0.00280 -0.08384 -0.06819 122 LEU A CD2 
835  N N   . GLN A 116 ? 0.59680 0.93101 0.57047 -0.05521 -0.18787 -0.14612 123 GLN A N   
836  C CA  . GLN A 116 ? 0.58258 0.97394 0.56163 -0.05887 -0.22335 -0.16339 123 GLN A CA  
837  C C   . GLN A 116 ? 0.60374 0.98093 0.56798 -0.08469 -0.22668 -0.20425 123 GLN A C   
838  O O   . GLN A 116 ? 0.73334 1.13368 0.67107 -0.08340 -0.25116 -0.21492 123 GLN A O   
839  C CB  . GLN A 116 ? 0.62776 1.05634 0.68643 -0.06392 -0.23128 -0.15477 123 GLN A CB  
840  C CG  . GLN A 116 ? 0.77608 1.23103 0.83850 -0.03343 -0.23856 -0.11439 123 GLN A CG  
841  C CD  . GLN A 116 ? 1.09902 1.59370 1.23472 -0.03796 -0.24987 -0.10849 123 GLN A CD  
842  O OE1 . GLN A 116 ? 1.15801 1.65909 1.34557 -0.06412 -0.24965 -0.13282 123 GLN A OE1 
843  N NE2 . GLN A 116 ? 1.15366 1.67147 1.29566 -0.01182 -0.25615 -0.07488 123 GLN A NE2 
844  N N   . ALA A 117 ? 0.69209 1.02950 0.67326 -0.10758 -0.20071 -0.22624 124 ALA A N   
845  C CA  . ALA A 117 ? 0.64709 0.96049 0.61300 -0.13083 -0.19548 -0.26332 124 ALA A CA  
846  C C   . ALA A 117 ? 0.79881 1.07852 0.67629 -0.12085 -0.19050 -0.26925 124 ALA A C   
847  O O   . ALA A 117 ? 0.87181 1.13295 0.72460 -0.13641 -0.18915 -0.29913 124 ALA A O   
848  C CB  . ALA A 117 ? 0.63936 0.91517 0.65960 -0.15541 -0.16187 -0.27827 124 ALA A CB  
849  N N   . GLY A 118 ? 0.79344 1.06132 0.62294 -0.09458 -0.18421 -0.24097 125 GLY A N   
850  C CA  . GLY A 118 ? 0.74841 0.98032 0.49216 -0.08072 -0.17445 -0.24104 125 GLY A CA  
851  C C   . GLY A 118 ? 0.74341 0.91129 0.47325 -0.07282 -0.13342 -0.22128 125 GLY A C   
852  O O   . GLY A 118 ? 0.83420 0.96657 0.49661 -0.05938 -0.11906 -0.21767 125 GLY A O   
853  N N   . ALA A 119 ? 0.64475 0.79228 0.43726 -0.07894 -0.11182 -0.20504 126 ALA A N   
854  C CA  . ALA A 119 ? 0.60626 0.69776 0.39417 -0.06842 -0.07626 -0.18026 126 ALA A CA  
855  C C   . ALA A 119 ? 0.66502 0.75539 0.41734 -0.03607 -0.07603 -0.14316 126 ALA A C   
856  O O   . ALA A 119 ? 0.70073 0.83349 0.44021 -0.02036 -0.10112 -0.13136 126 ALA A O   
857  C CB  . ALA A 119 ? 0.56301 0.64272 0.42310 -0.07945 -0.05923 -0.16994 126 ALA A CB  
858  N N   . ASP A 120 ? 0.70077 0.74256 0.44146 -0.02539 -0.04537 -0.12404 127 ASP A N   
859  C CA  . ASP A 120 ? 0.70964 0.74658 0.42762 0.00338  -0.03943 -0.08976 127 ASP A CA  
860  C C   . ASP A 120 ? 0.55271 0.56894 0.32137 0.00531  -0.01964 -0.06717 127 ASP A C   
861  O O   . ASP A 120 ? 0.55598 0.55876 0.36882 -0.01223 -0.00958 -0.07495 127 ASP A O   
862  C CB  . ASP A 120 ? 0.80080 0.80057 0.45063 0.02060  -0.02001 -0.08434 127 ASP A CB  
863  C CG  . ASP A 120 ? 0.87929 0.82324 0.53821 0.01233  0.01571  -0.08714 127 ASP A CG  
864  O OD1 . ASP A 120 ? 0.99496 0.92695 0.67357 -0.01086 0.02106  -0.11200 127 ASP A OD1 
865  O OD2 . ASP A 120 ? 0.84859 0.76151 0.50412 0.02919  0.04050  -0.06287 127 ASP A OD2 
866  N N   . ILE A 121 ? 0.56785 0.58191 0.32778 0.02825  -0.01333 -0.03877 128 ILE A N   
867  C CA  . ILE A 121 ? 0.49157 0.49443 0.29730 0.03068  0.00004  -0.01964 128 ILE A CA  
868  C C   . ILE A 121 ? 0.48247 0.44427 0.30897 0.02033  0.02513  -0.02323 128 ILE A C   
869  O O   . ILE A 121 ? 0.47664 0.43630 0.34855 0.01352  0.02942  -0.01747 128 ILE A O   
870  C CB  . ILE A 121 ? 0.49108 0.49337 0.27983 0.05696  0.00756  0.00808  128 ILE A CB  
871  C CG1 . ILE A 121 ? 0.61681 0.66720 0.40882 0.06596  -0.01810 0.01597  128 ILE A CG1 
872  C CG2 . ILE A 121 ? 0.49295 0.47167 0.32001 0.05885  0.02832  0.02295  128 ILE A CG2 
873  C CD1 . ILE A 121 ? 0.69598 0.75043 0.45838 0.09610  -0.01184 0.04348  128 ILE A CD1 
874  N N   . SER A 122 ? 0.52611 0.45650 0.32026 0.01947  0.04178  -0.03275 129 SER A N   
875  C CA  . SER A 122 ? 0.52483 0.41786 0.34547 0.01273  0.06792  -0.03190 129 SER A CA  
876  C C   . SER A 122 ? 0.60231 0.49900 0.46764 -0.00845 0.06552  -0.04531 129 SER A C   
877  O O   . SER A 122 ? 0.54750 0.42316 0.44696 -0.01185 0.08300  -0.03915 129 SER A O   
878  C CB  . SER A 122 ? 0.55918 0.41334 0.33623 0.01799  0.09178  -0.03751 129 SER A CB  
879  O OG  . SER A 122 ? 0.67297 0.52434 0.42699 0.00276  0.08766  -0.06398 129 SER A OG  
880  N N   . MET A 123 ? 0.47384 0.39724 0.34416 -0.02181 0.04617  -0.06233 130 MET A N   
881  C CA  . MET A 123 ? 0.47666 0.40113 0.39445 -0.03902 0.04918  -0.07033 130 MET A CA  
882  C C   . MET A 123 ? 0.43988 0.38826 0.39912 -0.03727 0.03817  -0.05495 130 MET A C   
883  O O   . MET A 123 ? 0.40528 0.35839 0.40066 -0.04869 0.03974  -0.05896 130 MET A O   
884  C CB  . MET A 123 ? 0.55731 0.49260 0.47139 -0.05756 0.04118  -0.09906 130 MET A CB  
885  C CG  . MET A 123 ? 0.59980 0.50708 0.47276 -0.06415 0.05477  -0.12119 130 MET A CG  
886  S SD  . MET A 123 ? 0.82477 0.76345 0.67940 -0.08292 0.03071  -0.15877 130 MET A SD  
887  C CE  . MET A 123 ? 0.86069 0.80897 0.63416 -0.06447 0.01446  -0.15971 130 MET A CE  
888  N N   . ILE A 124 ? 0.39347 0.35198 0.34755 -0.02234 0.03178  -0.03682 131 ILE A N   
889  C CA  . ILE A 124 ? 0.32924 0.30795 0.31413 -0.02003 0.02255  -0.02426 131 ILE A CA  
890  C C   . ILE A 124 ? 0.38118 0.34838 0.40304 -0.02605 0.03278  -0.01907 131 ILE A C   
891  O O   . ILE A 124 ? 0.34743 0.32976 0.39387 -0.02948 0.02681  -0.01536 131 ILE A O   
892  C CB  . ILE A 124 ? 0.35546 0.33647 0.32808 -0.00330 0.02196  -0.00732 131 ILE A CB  
893  C CG1 . ILE A 124 ? 0.35311 0.35246 0.35187 -0.00159 0.01409  0.00260  131 ILE A CG1 
894  C CG2 . ILE A 124 ? 0.39279 0.34288 0.36427 0.00314  0.04172  0.00012  131 ILE A CG2 
895  C CD1 . ILE A 124 ? 0.39372 0.39416 0.38329 0.01349  0.01659  0.01681  131 ILE A CD1 
896  N N   . GLY A 125 ? 0.41704 0.35823 0.44389 -0.02548 0.04939  -0.01677 132 GLY A N   
897  C CA  . GLY A 125 ? 0.38158 0.31771 0.44434 -0.02725 0.05661  -0.00792 132 GLY A CA  
898  C C   . GLY A 125 ? 0.42603 0.36296 0.51040 -0.03779 0.06143  -0.01377 132 GLY A C   
899  O O   . GLY A 125 ? 0.42099 0.36206 0.53267 -0.03591 0.06365  -0.00229 132 GLY A O   
900  N N   . GLN A 126 ? 0.39075 0.32422 0.46308 -0.04840 0.06387  -0.03194 133 GLN A N   
901  C CA  . GLN A 126 ? 0.47089 0.40221 0.56956 -0.06063 0.07317  -0.04073 133 GLN A CA  
902  C C   . GLN A 126 ? 0.50565 0.46204 0.62434 -0.06119 0.06197  -0.03518 133 GLN A C   
903  O O   . GLN A 126 ? 0.40884 0.36216 0.55775 -0.06754 0.07398  -0.03510 133 GLN A O   
904  C CB  . GLN A 126 ? 0.48232 0.40617 0.56192 -0.07447 0.07639  -0.06771 133 GLN A CB  
905  C CG  . GLN A 126 ? 0.49151 0.37999 0.56168 -0.07712 0.09956  -0.07445 133 GLN A CG  
906  C CD  . GLN A 126 ? 0.63109 0.50968 0.68095 -0.09346 0.10469  -0.10576 133 GLN A CD  
907  O OE1 . GLN A 126 ? 0.79615 0.67915 0.87149 -0.10878 0.10897  -0.12198 133 GLN A OE1 
908  N NE2 . GLN A 126 ? 0.70569 0.57090 0.70808 -0.09032 0.10489  -0.11592 133 GLN A NE2 
909  N N   . PHE A 127 ? 0.33441 0.31240 0.43867 -0.05341 0.04358  -0.02891 134 PHE A N   
910  C CA  . PHE A 127 ? 0.36423 0.36476 0.48541 -0.05298 0.03497  -0.02374 134 PHE A CA  
911  C C   . PHE A 127 ? 0.36622 0.36862 0.49036 -0.04005 0.03354  -0.00256 134 PHE A C   
912  O O   . PHE A 127 ? 0.35183 0.36945 0.48279 -0.03668 0.02819  0.00396  134 PHE A O   
913  C CB  . PHE A 127 ? 0.34268 0.36861 0.44822 -0.05374 0.01649  -0.03329 134 PHE A CB  
914  C CG  . PHE A 127 ? 0.34254 0.37210 0.43983 -0.06693 0.01300  -0.05782 134 PHE A CG  
915  C CD1 . PHE A 127 ? 0.31849 0.35934 0.44701 -0.08287 0.01483  -0.07488 134 PHE A CD1 
916  C CD2 . PHE A 127 ? 0.37165 0.39128 0.42993 -0.06392 0.01022  -0.06555 134 PHE A CD2 
917  C CE1 . PHE A 127 ? 0.31420 0.35990 0.43517 -0.09795 0.01016  -0.10322 134 PHE A CE1 
918  C CE2 . PHE A 127 ? 0.39440 0.41678 0.43663 -0.07618 0.00604  -0.09113 134 PHE A CE2 
919  C CZ  . PHE A 127 ? 0.39829 0.43515 0.47186 -0.09453 0.00430  -0.11217 134 PHE A CZ  
920  N N   . GLY A 128 ? 0.37673 0.36490 0.49672 -0.03312 0.03829  0.00678  135 GLY A N   
921  C CA  . GLY A 128 ? 0.39073 0.38296 0.51320 -0.02279 0.03477  0.02248  135 GLY A CA  
922  C C   . GLY A 128 ? 0.39715 0.39849 0.50096 -0.01593 0.02320  0.02462  135 GLY A C   
923  O O   . GLY A 128 ? 0.43153 0.43660 0.53415 -0.00927 0.01942  0.03309  135 GLY A O   
924  N N   . VAL A 129 ? 0.31644 0.32091 0.40415 -0.01638 0.01868  0.01727  136 VAL A N   
925  C CA  . VAL A 129 ? 0.29129 0.30177 0.36508 -0.00828 0.01311  0.02156  136 VAL A CA  
926  C C   . VAL A 129 ? 0.28068 0.27780 0.34126 -0.00406 0.01778  0.02000  136 VAL A C   
927  O O   . VAL A 129 ? 0.29480 0.29386 0.34182 0.00336  0.01769  0.02295  136 VAL A O   
928  C CB  . VAL A 129 ? 0.29257 0.32172 0.36285 -0.00719 0.00633  0.02084  136 VAL A CB  
929  C CG1 . VAL A 129 ? 0.36535 0.40398 0.45278 -0.00886 0.00695  0.02551  136 VAL A CG1 
930  C CG2 . VAL A 129 ? 0.30017 0.33595 0.36570 -0.01381 0.00231  0.00940  136 VAL A CG2 
931  N N   . GLY A 130 ? 0.29792 0.27295 0.31745 -0.03281 -0.01141 -0.02738 137 GLY A N   
932  C CA  . GLY A 130 ? 0.28621 0.26340 0.29782 -0.02078 -0.00895 -0.02967 137 GLY A CA  
933  C C   . GLY A 130 ? 0.28240 0.26944 0.29597 -0.01646 -0.00260 -0.02263 137 GLY A C   
934  O O   . GLY A 130 ? 0.30265 0.29651 0.31262 -0.00915 -0.00032 -0.02217 137 GLY A O   
935  N N   . PHE A 131 ? 0.29793 0.28526 0.31633 -0.02094 -0.00018 -0.01705 138 PHE A N   
936  C CA  . PHE A 131 ? 0.24062 0.23488 0.26084 -0.01752 0.00377  -0.01290 138 PHE A CA  
937  C C   . PHE A 131 ? 0.27080 0.27637 0.29178 -0.01382 0.00428  -0.01357 138 PHE A C   
938  O O   . PHE A 131 ? 0.27454 0.28047 0.29480 -0.00847 0.00650  -0.01095 138 PHE A O   
939  C CB  . PHE A 131 ? 0.26199 0.25794 0.28457 -0.02219 0.00503  -0.00933 138 PHE A CB  
940  C CG  . PHE A 131 ? 0.27417 0.27634 0.29765 -0.01842 0.00721  -0.00848 138 PHE A CG  
941  C CD1 . PHE A 131 ? 0.29486 0.29147 0.31831 -0.01542 0.00737  -0.00736 138 PHE A CD1 
942  C CD2 . PHE A 131 ? 0.32711 0.34072 0.35256 -0.01760 0.00832  -0.00959 138 PHE A CD2 
943  C CE1 . PHE A 131 ? 0.29916 0.29695 0.32365 -0.01289 0.00746  -0.00823 138 PHE A CE1 
944  C CE2 . PHE A 131 ? 0.31811 0.33296 0.34292 -0.01238 0.00924  -0.01075 138 PHE A CE2 
945  C CZ  . PHE A 131 ? 0.30384 0.30848 0.32771 -0.01065 0.00824  -0.01051 138 PHE A CZ  
946  N N   . TYR A 132 ? 0.26664 0.28185 0.29036 -0.01682 0.00174  -0.01620 139 TYR A N   
947  C CA  . TYR A 132 ? 0.27393 0.30155 0.29879 -0.01131 0.00148  -0.01625 139 TYR A CA  
948  C C   . TYR A 132 ? 0.26994 0.29730 0.28764 -0.00400 0.00027  -0.01667 139 TYR A C   
949  O O   . TYR A 132 ? 0.29337 0.32778 0.31014 0.00256  0.00033  -0.01419 139 TYR A O   
950  C CB  . TYR A 132 ? 0.26173 0.30547 0.29426 -0.01613 -0.00122 -0.01862 139 TYR A CB  
951  C CG  . TYR A 132 ? 0.32654 0.37602 0.36459 -0.01996 0.00269  -0.01568 139 TYR A CG  
952  C CD1 . TYR A 132 ? 0.31081 0.36405 0.34819 -0.01234 0.00593  -0.01455 139 TYR A CD1 
953  C CD2 . TYR A 132 ? 0.36800 0.41689 0.40996 -0.03025 0.00316  -0.01375 139 TYR A CD2 
954  C CE1 . TYR A 132 ? 0.37691 0.43654 0.41578 -0.01334 0.00968  -0.01342 139 TYR A CE1 
955  C CE2 . TYR A 132 ? 0.36525 0.42211 0.40926 -0.03239 0.00800  -0.00959 139 TYR A CE2 
956  C CZ  . TYR A 132 ? 0.39798 0.46157 0.43951 -0.02306 0.01128  -0.01043 139 TYR A CZ  
957  O OH  . TYR A 132 ? 0.51012 0.58303 0.55038 -0.02253 0.01597  -0.00827 139 TYR A OH  
958  N N   . SER A 133 ? 0.25160 0.27112 0.26293 -0.00322 -0.00039 -0.01909 140 SER A N   
959  C CA  . SER A 133 ? 0.24970 0.27162 0.25177 0.00537  0.00051  -0.01797 140 SER A CA  
960  C C   . SER A 133 ? 0.27471 0.29445 0.27762 0.00955  0.00646  -0.00878 140 SER A C   
961  O O   . SER A 133 ? 0.29347 0.31744 0.28966 0.01637  0.00849  -0.00392 140 SER A O   
962  C CB  . SER A 133 ? 0.30119 0.31636 0.29545 0.00740  -0.00052 -0.02369 140 SER A CB  
963  O OG  . SER A 133 ? 0.32461 0.33102 0.32199 0.00678  0.00392  -0.02050 140 SER A OG  
964  N N   . ALA A 134 ? 0.28256 0.29588 0.29339 0.00514  0.00867  -0.00596 141 ALA A N   
965  C CA  . ALA A 134 ? 0.25753 0.26670 0.27193 0.00679  0.01215  0.00160  141 ALA A CA  
966  C C   . ALA A 134 ? 0.25888 0.27045 0.27102 0.01251  0.01144  0.00579  141 ALA A C   
967  O O   . ALA A 134 ? 0.27391 0.28118 0.28566 0.01530  0.01430  0.01434  141 ALA A O   
968  C CB  . ALA A 134 ? 0.28546 0.28792 0.30732 0.00156  0.01174  0.00056  141 ALA A CB  
969  N N   . TYR A 135 ? 0.26731 0.28658 0.27912 0.01436  0.00760  0.00108  142 TYR A N   
970  C CA  . TYR A 135 ? 0.24804 0.27061 0.25813 0.02229  0.00599  0.00492  142 TYR A CA  
971  C C   . TYR A 135 ? 0.27867 0.30827 0.27845 0.02930  0.00520  0.00933  142 TYR A C   
972  O O   . TYR A 135 ? 0.30633 0.33859 0.30280 0.03755  0.00338  0.01448  142 TYR A O   
973  C CB  . TYR A 135 ? 0.25853 0.29242 0.27428 0.02305  0.00250  -0.00146 142 TYR A CB  
974  C CG  . TYR A 135 ? 0.27381 0.30065 0.29578 0.02018  0.00440  -0.00378 142 TYR A CG  
975  C CD1 . TYR A 135 ? 0.27043 0.28703 0.29328 0.02670  0.00453  -0.00170 142 TYR A CD1 
976  C CD2 . TYR A 135 ? 0.24232 0.26994 0.26724 0.01164  0.00551  -0.00792 142 TYR A CD2 
977  C CE1 . TYR A 135 ? 0.25970 0.26924 0.28535 0.02529  0.00519  -0.00626 142 TYR A CE1 
978  C CE2 . TYR A 135 ? 0.25682 0.27970 0.28400 0.01032  0.00694  -0.01014 142 TYR A CE2 
979  C CZ  . TYR A 135 ? 0.26273 0.27735 0.28972 0.01735  0.00655  -0.01040 142 TYR A CZ  
980  O OH  . TYR A 135 ? 0.26621 0.27613 0.29283 0.01715  0.00683  -0.01506 142 TYR A OH  
981  N N   . LEU A 136 ? 0.27509 0.30752 0.26806 0.02804  0.00646  0.00756  143 LEU A N   
982  C CA  . LEU A 136 ? 0.29621 0.33540 0.27608 0.03623  0.00730  0.01290  143 LEU A CA  
983  C C   . LEU A 136 ? 0.31039 0.34181 0.28958 0.03896  0.01374  0.02772  143 LEU A C   
984  O O   . LEU A 136 ? 0.32482 0.36066 0.29380 0.04717  0.01446  0.03682  143 LEU A O   
985  C CB  . LEU A 136 ? 0.30748 0.35061 0.27918 0.03599  0.00786  0.00602  143 LEU A CB  
986  C CG  . LEU A 136 ? 0.30631 0.35442 0.27655 0.03316  -0.00021 -0.00836 143 LEU A CG  
987  C CD1 . LEU A 136 ? 0.35265 0.39713 0.31502 0.03389  0.00054  -0.01587 143 LEU A CD1 
988  C CD2 . LEU A 136 ? 0.30936 0.37151 0.27167 0.03982  -0.00751 -0.01109 143 LEU A CD2 
989  N N   . VAL A 137 ? 0.28973 0.30995 0.27990 0.03163  0.01788  0.03107  144 VAL A N   
990  C CA  . VAL A 137 ? 0.28369 0.29651 0.27710 0.03056  0.02378  0.04549  144 VAL A CA  
991  C C   . VAL A 137 ? 0.32905 0.32431 0.33473 0.02557  0.02198  0.04795  144 VAL A C   
992  O O   . VAL A 137 ? 0.31405 0.29898 0.32364 0.02399  0.02485  0.06063  144 VAL A O   
993  C CB  . VAL A 137 ? 0.25780 0.27692 0.25432 0.02630  0.03052  0.04846  144 VAL A CB  
994  C CG1 . VAL A 137 ? 0.33485 0.37008 0.31584 0.03441  0.03260  0.04527  144 VAL A CG1 
995  C CG2 . VAL A 137 ? 0.25377 0.26847 0.26210 0.01816  0.02867  0.03858  144 VAL A CG2 
996  N N   . ALA A 138 ? 0.30263 0.29373 0.31403 0.02305  0.01726  0.03649  145 ALA A N   
997  C CA  . ALA A 138 ? 0.29871 0.27315 0.31943 0.01953  0.01488  0.03539  145 ALA A CA  
998  C C   . ALA A 138 ? 0.33643 0.30714 0.35446 0.02819  0.01018  0.03122  145 ALA A C   
999  O O   . ALA A 138 ? 0.33998 0.32532 0.35452 0.03236  0.00803  0.02380  145 ALA A O   
1000 C CB  . ALA A 138 ? 0.27542 0.25006 0.30316 0.01167  0.01374  0.02551  145 ALA A CB  
1001 N N   . GLU A 139 ? 0.29764 0.24889 0.31867 0.03096  0.00820  0.03590  146 GLU A N   
1002 C CA  . GLU A 139 ? 0.34312 0.28987 0.36256 0.04150  0.00361  0.03001  146 GLU A CA  
1003 C C   . GLU A 139 ? 0.34011 0.28453 0.36416 0.03931  0.00132  0.01624  146 GLU A C   
1004 O O   . GLU A 139 ? 0.35390 0.30554 0.37664 0.04829  -0.00081 0.00834  146 GLU A O   
1005 C CB  . GLU A 139 ? 0.41577 0.33867 0.43453 0.04786  0.00157  0.04048  146 GLU A CB  
1006 C CG  . GLU A 139 ? 0.47322 0.37124 0.50044 0.03742  0.00127  0.04478  146 GLU A CG  
1007 C CD  . GLU A 139 ? 0.85431 0.72402 0.88170 0.04213  -0.00129 0.05702  146 GLU A CD  
1008 O OE1 . GLU A 139 ? 0.86933 0.74097 0.88822 0.05417  -0.00149 0.06555  146 GLU A OE1 
1009 O OE2 . GLU A 139 ? 0.83808 0.68273 0.87439 0.03358  -0.00404 0.05836  146 GLU A OE2 
1010 N N   . LYS A 140 ? 0.31561 0.25333 0.34478 0.02848  0.00185  0.01364  147 LYS A N   
1011 C CA  . LYS A 140 ? 0.31267 0.24958 0.34330 0.02630  -0.00050 0.00125  147 LYS A CA  
1012 C C   . LYS A 140 ? 0.31452 0.25947 0.34854 0.01479  0.00145  0.00084  147 LYS A C   
1013 O O   . LYS A 140 ? 0.31533 0.25727 0.35426 0.00795  0.00332  0.00917  147 LYS A O   
1014 C CB  . LYS A 140 ? 0.33425 0.24526 0.36716 0.02804  -0.00583 -0.00309 147 LYS A CB  
1015 C CG  . LYS A 140 ? 0.33966 0.25120 0.37033 0.02786  -0.00899 -0.01750 147 LYS A CG  
1016 C CD  . LYS A 140 ? 0.41067 0.29549 0.44028 0.03402  -0.01585 -0.02549 147 LYS A CD  
1017 C CE  . LYS A 140 ? 0.50736 0.37127 0.54554 0.02141  -0.02100 -0.02382 147 LYS A CE  
1018 N NZ  . LYS A 140 ? 0.62527 0.45601 0.66372 0.02649  -0.02904 -0.02974 147 LYS A NZ  
1019 N N   . VAL A 141 ? 0.27345 0.23025 0.30506 0.01348  0.00151  -0.00753 148 VAL A N   
1020 C CA  . VAL A 141 ? 0.23359 0.19595 0.26748 0.00463  0.00220  -0.00806 148 VAL A CA  
1021 C C   . VAL A 141 ? 0.28771 0.24613 0.31964 0.00400  -0.00166 -0.01725 148 VAL A C   
1022 O O   . VAL A 141 ? 0.29240 0.25583 0.31814 0.01054  -0.00181 -0.02413 148 VAL A O   
1023 C CB  . VAL A 141 ? 0.27499 0.25414 0.30580 0.00314  0.00549  -0.00739 148 VAL A CB  
1024 C CG1 . VAL A 141 ? 0.27904 0.26050 0.31140 -0.00369 0.00541  -0.00777 148 VAL A CG1 
1025 C CG2 . VAL A 141 ? 0.28133 0.26510 0.31118 0.00520  0.00794  -0.00063 148 VAL A CG2 
1026 N N   . THR A 142 ? 0.28680 0.23871 0.32400 -0.00296 -0.00499 -0.01757 149 THR A N   
1027 C CA  . THR A 142 ? 0.26264 0.21263 0.29613 -0.00359 -0.01021 -0.02695 149 THR A CA  
1028 C C   . THR A 142 ? 0.31330 0.27534 0.34760 -0.00918 -0.00962 -0.02443 149 THR A C   
1029 O O   . THR A 142 ? 0.32188 0.28656 0.36495 -0.01441 -0.00819 -0.01735 149 THR A O   
1030 C CB  . THR A 142 ? 0.27142 0.20271 0.31139 -0.00692 -0.01774 -0.03126 149 THR A CB  
1031 O OG1 . THR A 142 ? 0.35653 0.27147 0.39619 -0.00105 -0.01858 -0.03168 149 THR A OG1 
1032 C CG2 . THR A 142 ? 0.36882 0.29877 0.40112 -0.00521 -0.02483 -0.04411 149 THR A CG2 
1033 N N   . VAL A 143 ? 0.27050 0.24090 0.29509 -0.00680 -0.01010 -0.02918 150 VAL A N   
1034 C CA  . VAL A 143 ? 0.26459 0.24392 0.28796 -0.01037 -0.01023 -0.02573 150 VAL A CA  
1035 C C   . VAL A 143 ? 0.31002 0.28967 0.32677 -0.00941 -0.01713 -0.03308 150 VAL A C   
1036 O O   . VAL A 143 ? 0.31064 0.29296 0.31515 -0.00372 -0.01726 -0.03945 150 VAL A O   
1037 C CB  . VAL A 143 ? 0.28375 0.27289 0.30042 -0.00931 -0.00433 -0.02132 150 VAL A CB  
1038 C CG1 . VAL A 143 ? 0.30044 0.29343 0.31473 -0.01189 -0.00558 -0.01703 150 VAL A CG1 
1039 C CG2 . VAL A 143 ? 0.30992 0.29951 0.33210 -0.01005 0.00033  -0.01628 150 VAL A CG2 
1040 N N   . ILE A 144 ? 0.29294 0.27251 0.31776 -0.01407 -0.02308 -0.03270 151 ILE A N   
1041 C CA  . ILE A 144 ? 0.27539 0.25805 0.29392 -0.01326 -0.03166 -0.03972 151 ILE A CA  
1042 C C   . ILE A 144 ? 0.29241 0.28632 0.30674 -0.01260 -0.03056 -0.03238 151 ILE A C   
1043 O O   . ILE A 144 ? 0.27513 0.27187 0.30024 -0.01529 -0.02803 -0.02459 151 ILE A O   
1044 C CB  . ILE A 144 ? 0.33768 0.31484 0.37092 -0.01968 -0.04109 -0.04436 151 ILE A CB  
1045 C CG1 . ILE A 144 ? 0.37226 0.33307 0.41398 -0.02234 -0.04125 -0.04702 151 ILE A CG1 
1046 C CG2 . ILE A 144 ? 0.36020 0.34008 0.38441 -0.01779 -0.05234 -0.05526 151 ILE A CG2 
1047 C CD1 . ILE A 144 ? 0.38767 0.33740 0.41501 -0.01459 -0.04280 -0.05784 151 ILE A CD1 
1048 N N   . THR A 145 ? 0.27949 0.27952 0.27713 -0.00779 -0.03217 -0.03424 152 THR A N   
1049 C CA  . THR A 145 ? 0.28367 0.29042 0.27631 -0.00670 -0.03039 -0.02450 152 THR A CA  
1050 C C   . THR A 145 ? 0.30472 0.31922 0.28129 -0.00181 -0.03710 -0.02703 152 THR A C   
1051 O O   . THR A 145 ? 0.31727 0.33385 0.28053 0.00231  -0.03938 -0.03596 152 THR A O   
1052 C CB  . THR A 145 ? 0.30682 0.31290 0.29447 -0.00689 -0.02018 -0.01637 152 THR A CB  
1053 O OG1 . THR A 145 ? 0.29903 0.30507 0.28479 -0.00695 -0.01933 -0.00623 152 THR A OG1 
1054 C CG2 . THR A 145 ? 0.33013 0.34246 0.30241 -0.00319 -0.01621 -0.01897 152 THR A CG2 
1055 N N   . LYS A 146 ? 0.28541 0.30455 0.26182 -0.00050 -0.04057 -0.01939 153 LYS A N   
1056 C CA  . LYS A 146 ? 0.30718 0.33518 0.26727 0.00528  -0.04810 -0.01972 153 LYS A CA  
1057 C C   . LYS A 146 ? 0.34066 0.36875 0.29521 0.00802  -0.04524 -0.00471 153 LYS A C   
1058 O O   . LYS A 146 ? 0.30285 0.32875 0.27143 0.00770  -0.04702 0.00037  153 LYS A O   
1059 C CB  . LYS A 146 ? 0.31739 0.35148 0.28694 0.00475  -0.06172 -0.02916 153 LYS A CB  
1060 C CG  . LYS A 146 ? 0.34307 0.38891 0.29607 0.01185  -0.07197 -0.02951 153 LYS A CG  
1061 C CD  . LYS A 146 ? 0.34937 0.39844 0.27578 0.01789  -0.07264 -0.03753 153 LYS A CD  
1062 C CE  . LYS A 146 ? 0.41103 0.47357 0.31904 0.02586  -0.08458 -0.03922 153 LYS A CE  
1063 N NZ  . LYS A 146 ? 0.40549 0.47257 0.30128 0.03130  -0.08041 -0.02033 153 LYS A NZ  
1064 N N   . HIS A 147 ? 0.34852 0.37891 0.28296 0.01114  -0.04032 0.00279  154 HIS A N   
1065 C CA  . HIS A 147 ? 0.34597 0.37365 0.27065 0.01386  -0.03845 0.01876  154 HIS A CA  
1066 C C   . HIS A 147 ? 0.38352 0.42259 0.28949 0.02221  -0.04766 0.02003  154 HIS A C   
1067 O O   . HIS A 147 ? 0.41123 0.46108 0.30399 0.02566  -0.05151 0.00956  154 HIS A O   
1068 C CB  . HIS A 147 ? 0.38400 0.40883 0.29990 0.00979  -0.02630 0.02856  154 HIS A CB  
1069 C CG  . HIS A 147 ? 0.42499 0.44067 0.33432 0.00931  -0.02331 0.04695  154 HIS A CG  
1070 N ND1 . HIS A 147 ? 0.42216 0.44327 0.31087 0.01500  -0.02527 0.05856  154 HIS A ND1 
1071 C CD2 . HIS A 147 ? 0.40283 0.40210 0.32245 0.00358  -0.01866 0.05595  154 HIS A CD2 
1072 C CE1 . HIS A 147 ? 0.48249 0.48877 0.37047 0.01226  -0.02186 0.07552  154 HIS A CE1 
1073 N NE2 . HIS A 147 ? 0.39280 0.38464 0.29979 0.00512  -0.01835 0.07303  154 HIS A NE2 
1074 N N   . ASN A 148 ? 0.36777 0.40389 0.27110 0.02702  -0.05204 0.03232  155 ASN A N   
1075 C CA  . ASN A 148 ? 0.37034 0.41850 0.25518 0.03647  -0.06220 0.03515  155 ASN A CA  
1076 C C   . ASN A 148 ? 0.44277 0.50070 0.29874 0.03998  -0.05769 0.03856  155 ASN A C   
1077 O O   . ASN A 148 ? 0.44155 0.51380 0.27919 0.04821  -0.06698 0.03365  155 ASN A O   
1078 C CB  . ASN A 148 ? 0.41139 0.45178 0.29488 0.04270  -0.06545 0.05200  155 ASN A CB  
1079 C CG  . ASN A 148 ? 0.44920 0.49012 0.35694 0.04526  -0.07377 0.04701  155 ASN A CG  
1080 O OD1 . ASN A 148 ? 0.46225 0.51604 0.38431 0.04348  -0.08120 0.03225  155 ASN A OD1 
1081 N ND2 . ASN A 148 ? 0.42572 0.45320 0.33832 0.05006  -0.07296 0.05988  155 ASN A ND2 
1082 N N   . ASP A 149 ? 0.42155 0.47481 0.27301 0.03436  -0.04375 0.04705  156 ASP A N   
1083 C CA  . ASP A 149 ? 0.51106 0.57755 0.33600 0.03801  -0.03665 0.05436  156 ASP A CA  
1084 C C   . ASP A 149 ? 0.52256 0.60125 0.34325 0.03828  -0.03193 0.03761  156 ASP A C   
1085 O O   . ASP A 149 ? 0.51749 0.61088 0.31779 0.04199  -0.02348 0.04256  156 ASP A O   
1086 C CB  . ASP A 149 ? 0.54138 0.59881 0.36478 0.03128  -0.02401 0.07728  156 ASP A CB  
1087 C CG  . ASP A 149 ? 0.64000 0.68284 0.46041 0.03421  -0.02920 0.09578  156 ASP A CG  
1088 O OD1 . ASP A 149 ? 0.60394 0.65114 0.41692 0.04431  -0.04182 0.09329  156 ASP A OD1 
1089 O OD2 . ASP A 149 ? 0.68453 0.71075 0.51108 0.02659  -0.02159 0.11239  156 ASP A OD2 
1090 N N   . ASP A 150 ? 0.43101 0.50453 0.26982 0.03552  -0.03694 0.01870  157 ASP A N   
1091 C CA  . ASP A 150 ? 0.41761 0.49752 0.25411 0.03686  -0.03270 0.00295  157 ASP A CA  
1092 C C   . ASP A 150 ? 0.53215 0.60606 0.37996 0.03751  -0.04580 -0.01860 157 ASP A C   
1093 O O   . ASP A 150 ? 0.43739 0.50658 0.29686 0.03562  -0.05690 -0.02020 157 ASP A O   
1094 C CB  . ASP A 150 ? 0.40308 0.47806 0.25564 0.02849  -0.01908 0.00833  157 ASP A CB  
1095 C CG  . ASP A 150 ? 0.50367 0.59369 0.34528 0.03345  -0.01004 0.00099  157 ASP A CG  
1096 O OD1 . ASP A 150 ? 0.46719 0.56617 0.29111 0.04379  -0.01566 -0.01366 157 ASP A OD1 
1097 O OD2 . ASP A 150 ? 0.45517 0.54924 0.30613 0.02783  0.00205  0.00884  157 ASP A OD2 
1098 N N   . GLU A 151 ? 0.44321 0.51771 0.28881 0.04024  -0.04450 -0.03472 158 GLU A N   
1099 C CA  . GLU A 151 ? 0.47337 0.53835 0.32921 0.03977  -0.05667 -0.05540 158 GLU A CA  
1100 C C   . GLU A 151 ? 0.44593 0.49509 0.33238 0.02911  -0.05408 -0.05458 158 GLU A C   
1101 O O   . GLU A 151 ? 0.41263 0.45913 0.30937 0.02394  -0.04282 -0.04147 158 GLU A O   
1102 C CB  . GLU A 151 ? 0.49442 0.56280 0.33277 0.04937  -0.05637 -0.07303 158 GLU A CB  
1103 C CG  . GLU A 151 ? 0.68827 0.77393 0.49314 0.06210  -0.06070 -0.07793 158 GLU A CG  
1104 C CD  . GLU A 151 ? 1.01618 1.10299 0.81685 0.06279  -0.07880 -0.08408 158 GLU A CD  
1105 O OE1 . GLU A 151 ? 1.20464 1.30263 0.99500 0.06458  -0.07924 -0.06849 158 GLU A OE1 
1106 O OE2 . GLU A 151 ? 1.11069 1.18703 0.91961 0.06122  -0.09327 -0.10392 158 GLU A OE2 
1107 N N   . GLN A 152 ? 0.34650 0.38517 0.24725 0.02544  -0.06487 -0.06873 159 GLN A N   
1108 C CA  . GLN A 152 ? 0.34728 0.37225 0.27467 0.01620  -0.06163 -0.06722 159 GLN A CA  
1109 C C   . GLN A 152 ? 0.37284 0.39041 0.29797 0.01932  -0.05357 -0.07360 159 GLN A C   
1110 O O   . GLN A 152 ? 0.42466 0.43963 0.33641 0.02689  -0.05824 -0.08885 159 GLN A O   
1111 C CB  . GLN A 152 ? 0.38167 0.39933 0.32762 0.00935  -0.07541 -0.07695 159 GLN A CB  
1112 C CG  . GLN A 152 ? 0.36890 0.37639 0.34278 -0.00074 -0.07124 -0.07089 159 GLN A CG  
1113 C CD  . GLN A 152 ? 0.42085 0.42910 0.41651 -0.00942 -0.08339 -0.07455 159 GLN A CD  
1114 O OE1 . GLN A 152 ? 0.40937 0.43164 0.40847 -0.00950 -0.08958 -0.07026 159 GLN A OE1 
1115 N NE2 . GLN A 152 ? 0.38571 0.37986 0.39768 -0.01688 -0.08682 -0.08115 159 GLN A NE2 
1116 N N   . TYR A 153 ? 0.31446 0.32913 0.25181 0.01504  -0.04239 -0.06304 160 TYR A N   
1117 C CA  . TYR A 153 ? 0.34142 0.35256 0.27882 0.01882  -0.03449 -0.06680 160 TYR A CA  
1118 C C   . TYR A 153 ? 0.35047 0.34702 0.30976 0.01193  -0.03358 -0.06490 160 TYR A C   
1119 O O   . TYR A 153 ? 0.31986 0.31424 0.29391 0.00385  -0.03354 -0.05576 160 TYR A O   
1120 C CB  . TYR A 153 ? 0.32977 0.35587 0.26042 0.02058  -0.02128 -0.05475 160 TYR A CB  
1121 C CG  . TYR A 153 ? 0.39807 0.44087 0.30538 0.02864  -0.01922 -0.05506 160 TYR A CG  
1122 C CD1 . TYR A 153 ? 0.36037 0.41053 0.25236 0.04022  -0.01784 -0.06756 160 TYR A CD1 
1123 C CD2 . TYR A 153 ? 0.47793 0.52914 0.37684 0.02629  -0.01883 -0.04263 160 TYR A CD2 
1124 C CE1 . TYR A 153 ? 0.40961 0.47875 0.27746 0.04904  -0.01490 -0.06736 160 TYR A CE1 
1125 C CE2 . TYR A 153 ? 0.46271 0.53040 0.33807 0.03399  -0.01646 -0.04050 160 TYR A CE2 
1126 C CZ  . TYR A 153 ? 0.46633 0.54463 0.32574 0.04515  -0.01402 -0.05268 160 TYR A CZ  
1127 O OH  . TYR A 153 ? 0.61970 0.71799 0.45328 0.05390  -0.01042 -0.04944 160 TYR A OH  
1128 N N   . ALA A 154 ? 0.32123 0.30925 0.28105 0.01696  -0.03193 -0.07268 161 ALA A N   
1129 C CA  . ALA A 154 ? 0.33176 0.30775 0.30833 0.01287  -0.02898 -0.06848 161 ALA A CA  
1130 C C   . ALA A 154 ? 0.32820 0.31386 0.30176 0.01897  -0.01854 -0.06455 161 ALA A C   
1131 O O   . ALA A 154 ? 0.34329 0.33426 0.30527 0.02959  -0.01679 -0.07308 161 ALA A O   
1132 C CB  . ALA A 154 ? 0.35850 0.31268 0.34075 0.01347  -0.03797 -0.07980 161 ALA A CB  
1133 N N   . TRP A 155 ? 0.28909 0.27907 0.27323 0.01298  -0.01218 -0.05263 162 TRP A N   
1134 C CA  . TRP A 155 ? 0.27866 0.27856 0.26537 0.01619  -0.00407 -0.04812 162 TRP A CA  
1135 C C   . TRP A 155 ? 0.32211 0.30805 0.31997 0.01633  -0.00532 -0.04725 162 TRP A C   
1136 O O   . TRP A 155 ? 0.30201 0.27611 0.30870 0.00936  -0.00861 -0.04323 162 TRP A O   
1137 C CB  . TRP A 155 ? 0.27262 0.28464 0.26265 0.00856  0.00162  -0.03632 162 TRP A CB  
1138 C CG  . TRP A 155 ? 0.28189 0.30646 0.27761 0.00824  0.00831  -0.03101 162 TRP A CG  
1139 C CD1 . TRP A 155 ? 0.29092 0.33542 0.28385 0.00831  0.01455  -0.02734 162 TRP A CD1 
1140 C CD2 . TRP A 155 ? 0.27346 0.29409 0.27950 0.00663  0.00882  -0.02787 162 TRP A CD2 
1141 N NE1 . TRP A 155 ? 0.28361 0.33698 0.28695 0.00585  0.01776  -0.02330 162 TRP A NE1 
1142 C CE2 . TRP A 155 ? 0.27465 0.31327 0.28437 0.00578  0.01388  -0.02420 162 TRP A CE2 
1143 C CE3 . TRP A 155 ? 0.29673 0.30233 0.30923 0.00560  0.00559  -0.02690 162 TRP A CE3 
1144 C CZ2 . TRP A 155 ? 0.31967 0.36121 0.33784 0.00503  0.01409  -0.02171 162 TRP A CZ2 
1145 C CZ3 . TRP A 155 ? 0.26821 0.27661 0.28667 0.00592  0.00734  -0.02294 162 TRP A CZ3 
1146 C CH2 . TRP A 155 ? 0.28788 0.31382 0.30848 0.00606  0.01072  -0.02135 162 TRP A CH2 
1147 N N   . GLU A 156 ? 0.29262 0.28191 0.29041 0.02491  -0.00238 -0.04974 163 GLU A N   
1148 C CA  . GLU A 156 ? 0.25829 0.23331 0.26476 0.02596  -0.00394 -0.04669 163 GLU A CA  
1149 C C   . GLU A 156 ? 0.26429 0.25308 0.27268 0.03383  0.00090  -0.04453 163 GLU A C   
1150 O O   . GLU A 156 ? 0.29525 0.29934 0.29862 0.04261  0.00384  -0.05010 163 GLU A O   
1151 C CB  . GLU A 156 ? 0.34881 0.29955 0.35405 0.03038  -0.01147 -0.05540 163 GLU A CB  
1152 C CG  . GLU A 156 ? 0.43115 0.36292 0.44437 0.03162  -0.01342 -0.05031 163 GLU A CG  
1153 C CD  . GLU A 156 ? 0.57681 0.47980 0.59128 0.03135  -0.02236 -0.05777 163 GLU A CD  
1154 O OE1 . GLU A 156 ? 0.50836 0.39967 0.51584 0.04358  -0.02592 -0.06851 163 GLU A OE1 
1155 O OE2 . GLU A 156 ? 0.48804 0.38063 0.51138 0.01911  -0.02627 -0.05355 163 GLU A OE2 
1156 N N   . SER A 157 ? 0.26499 0.25172 0.28061 0.03142  0.00172  -0.03634 164 SER A N   
1157 C CA  . SER A 157 ? 0.25698 0.25736 0.27521 0.03998  0.00410  -0.03487 164 SER A CA  
1158 C C   . SER A 157 ? 0.28293 0.27070 0.30499 0.04153  0.00202  -0.02756 164 SER A C   
1159 O O   . SER A 157 ? 0.30576 0.28694 0.33002 0.03262  0.00211  -0.02043 164 SER A O   
1160 C CB  . SER A 157 ? 0.25356 0.28087 0.27532 0.03447  0.00875  -0.03115 164 SER A CB  
1161 O OG  . SER A 157 ? 0.27794 0.32164 0.30486 0.04235  0.00952  -0.03030 164 SER A OG  
1162 N N   . SER A 158 ? 0.30247 0.28818 0.32442 0.05446  0.00048  -0.02879 165 SER A N   
1163 C CA  . SER A 158 ? 0.34216 0.32268 0.36586 0.05850  -0.00093 -0.01985 165 SER A CA  
1164 C C   . SER A 158 ? 0.34121 0.35046 0.36801 0.06386  0.00038  -0.01846 165 SER A C   
1165 O O   . SER A 158 ? 0.35850 0.36840 0.38526 0.07404  -0.00205 -0.01397 165 SER A O   
1166 C CB  . SER A 158 ? 0.38472 0.33899 0.40637 0.06980  -0.00525 -0.01989 165 SER A CB  
1167 O OG  . SER A 158 ? 0.40448 0.33169 0.42575 0.06298  -0.00822 -0.02237 165 SER A OG  
1168 N N   . ALA A 159 ? 0.28617 0.31916 0.31640 0.05656  0.00342  -0.02147 166 ALA A N   
1169 C CA  . ALA A 159 ? 0.28265 0.34648 0.31974 0.05840  0.00382  -0.02133 166 ALA A CA  
1170 C C   . ALA A 159 ? 0.31456 0.39135 0.35476 0.07507  0.00363  -0.02615 166 ALA A C   
1171 O O   . ALA A 159 ? 0.34994 0.41859 0.38634 0.08242  0.00513  -0.03270 166 ALA A O   
1172 C CB  . ALA A 159 ? 0.32875 0.39478 0.36548 0.05578  0.00060  -0.01481 166 ALA A CB  
1173 N N   . GLY A 160 ? 0.33189 0.43100 0.37881 0.08257  0.00122  -0.02419 167 GLY A N   
1174 C CA  . GLY A 160 ? 0.33511 0.45320 0.38741 0.09952  0.00165  -0.02911 167 GLY A CA  
1175 C C   . GLY A 160 ? 0.28656 0.43574 0.34671 0.09708  0.00793  -0.03456 167 GLY A C   
1176 O O   . GLY A 160 ? 0.35714 0.52394 0.42097 0.11302  0.00997  -0.03986 167 GLY A O   
1177 N N   . GLY A 161 ? 0.26848 0.42487 0.33078 0.07862  0.01148  -0.03263 168 GLY A N   
1178 C CA  . GLY A 161 ? 0.30291 0.49286 0.37430 0.07341  0.01811  -0.03366 168 GLY A CA  
1179 C C   . GLY A 161 ? 0.26678 0.44921 0.32799 0.07303  0.02422  -0.03741 168 GLY A C   
1180 O O   . GLY A 161 ? 0.27616 0.48825 0.34299 0.06979  0.03127  -0.03647 168 GLY A O   
1181 N N   . SER A 162 ? 0.26259 0.40859 0.30934 0.07607  0.02153  -0.04116 169 SER A N   
1182 C CA  . SER A 162 ? 0.23621 0.37537 0.27119 0.07798  0.02522  -0.04689 169 SER A CA  
1183 C C   . SER A 162 ? 0.24619 0.34934 0.27123 0.06784  0.02083  -0.04625 169 SER A C   
1184 O O   . SER A 162 ? 0.27262 0.35303 0.29869 0.06424  0.01556  -0.04285 169 SER A O   
1185 C CB  . SER A 162 ? 0.29945 0.43750 0.32755 0.10025  0.02534  -0.05788 169 SER A CB  
1186 O OG  . SER A 162 ? 0.35037 0.45076 0.37250 0.10816  0.01748  -0.06165 169 SER A OG  
1187 N N   . PHE A 163 ? 0.23883 0.34081 0.25450 0.06361  0.02341  -0.04865 170 PHE A N   
1188 C CA  . PHE A 163 ? 0.28610 0.35878 0.29315 0.05585  0.01867  -0.04958 170 PHE A CA  
1189 C C   . PHE A 163 ? 0.26167 0.33188 0.25444 0.06408  0.01871  -0.05955 170 PHE A C   
1190 O O   . PHE A 163 ? 0.27547 0.37025 0.26383 0.07353  0.02461  -0.06341 170 PHE A O   
1191 C CB  . PHE A 163 ? 0.27081 0.34464 0.28115 0.03831  0.01979  -0.03985 170 PHE A CB  
1192 C CG  . PHE A 163 ? 0.27449 0.37261 0.28311 0.03245  0.02643  -0.03516 170 PHE A CG  
1193 C CD1 . PHE A 163 ? 0.28368 0.40897 0.30386 0.02772  0.03157  -0.02866 170 PHE A CD1 
1194 C CD2 . PHE A 163 ? 0.25056 0.34509 0.24652 0.03085  0.02702  -0.03609 170 PHE A CD2 
1195 C CE1 . PHE A 163 ? 0.29058 0.43745 0.31114 0.02002  0.03825  -0.02144 170 PHE A CE1 
1196 C CE2 . PHE A 163 ? 0.26581 0.38217 0.25892 0.02531  0.03385  -0.02860 170 PHE A CE2 
1197 C CZ  . PHE A 163 ? 0.31181 0.45347 0.31783 0.01906  0.04002  -0.02035 170 PHE A CZ  
1198 N N   . THR A 164 ? 0.28475 0.32727 0.27043 0.06100  0.01178  -0.06423 171 THR A N   
1199 C CA  . THR A 164 ? 0.28645 0.32454 0.25674 0.06819  0.00918  -0.07561 171 THR A CA  
1200 C C   . THR A 164 ? 0.28081 0.31526 0.24581 0.05559  0.00693  -0.07137 171 THR A C   
1201 O O   . THR A 164 ? 0.28230 0.30651 0.25633 0.04282  0.00472  -0.06263 171 THR A O   
1202 C CB  . THR A 164 ? 0.36612 0.37334 0.33207 0.07790  -0.00009 -0.08875 171 THR A CB  
1203 O OG1 . THR A 164 ? 0.35137 0.33177 0.32622 0.06553  -0.00704 -0.08373 171 THR A OG1 
1204 C CG2 . THR A 164 ? 0.39330 0.40113 0.36252 0.09406  0.00119  -0.09351 171 THR A CG2 
1205 N N   . VAL A 165 ? 0.30197 0.34608 0.25093 0.06131  0.00731  -0.07803 172 VAL A N   
1206 C CA  . VAL A 165 ? 0.33820 0.37808 0.27878 0.05320  0.00292  -0.07618 172 VAL A CA  
1207 C C   . VAL A 165 ? 0.33190 0.36247 0.25512 0.06405  -0.00504 -0.09328 172 VAL A C   
1208 O O   . VAL A 165 ? 0.34465 0.38768 0.25476 0.07893  -0.00161 -0.10315 172 VAL A O   
1209 C CB  . VAL A 165 ? 0.31489 0.38049 0.25089 0.04741  0.01179  -0.06299 172 VAL A CB  
1210 C CG1 . VAL A 165 ? 0.36929 0.42960 0.29503 0.04163  0.00617  -0.06045 172 VAL A CG1 
1211 C CG2 . VAL A 165 ? 0.30882 0.37870 0.26246 0.03592  0.01695  -0.04900 172 VAL A CG2 
1212 N N   . ARG A 166 ? 0.36332 0.37329 0.28707 0.05728  -0.01623 -0.09796 173 ARG A N   
1213 C CA  . ARG A 166 ? 0.38479 0.38568 0.29190 0.06541  -0.02650 -0.11538 173 ARG A CA  
1214 C C   . ARG A 166 ? 0.40309 0.40314 0.30850 0.05502  -0.03436 -0.11188 173 ARG A C   
1215 O O   . ARG A 166 ? 0.39015 0.38798 0.31136 0.04199  -0.03376 -0.09850 173 ARG A O   
1216 C CB  . ARG A 166 ? 0.51794 0.48775 0.43087 0.06949  -0.03685 -0.13028 173 ARG A CB  
1217 C CG  . ARG A 166 ? 0.45688 0.40345 0.39105 0.05345  -0.04469 -0.12420 173 ARG A CG  
1218 C CD  . ARG A 166 ? 0.64433 0.56183 0.58933 0.05581  -0.04941 -0.12990 173 ARG A CD  
1219 N NE  . ARG A 166 ? 0.70365 0.62827 0.65378 0.06268  -0.03858 -0.12150 173 ARG A NE  
1220 C CZ  . ARG A 166 ? 0.81623 0.72000 0.77150 0.07020  -0.04053 -0.12522 173 ARG A CZ  
1221 N NH1 . ARG A 166 ? 0.79788 0.66848 0.75357 0.07160  -0.05255 -0.13757 173 ARG A NH1 
1222 N NH2 . ARG A 166 ? 0.75858 0.67421 0.71916 0.07642  -0.03120 -0.11622 173 ARG A NH2 
1223 N N   . THR A 167 ? 0.43955 0.44361 0.32450 0.06267  -0.04194 -0.12449 174 THR A N   
1224 C CA  . THR A 167 ? 0.42283 0.42437 0.30736 0.05439  -0.05324 -0.12450 174 THR A CA  
1225 C C   . THR A 167 ? 0.52965 0.50476 0.43525 0.04400  -0.06556 -0.13100 174 THR A C   
1226 O O   . THR A 167 ? 0.57177 0.52605 0.47948 0.04814  -0.07143 -0.14494 174 THR A O   
1227 C CB  . THR A 167 ? 0.60115 0.61321 0.45715 0.06634  -0.06043 -0.13866 174 THR A CB  
1228 O OG1 . THR A 167 ? 0.56732 0.60718 0.40501 0.07452  -0.04672 -0.12816 174 THR A OG1 
1229 C CG2 . THR A 167 ? 0.61548 0.62707 0.47181 0.05873  -0.07432 -0.13964 174 THR A CG2 
1230 N N   . ASP A 168 ? 0.45829 0.43423 0.38082 0.03064  -0.06893 -0.11976 175 ASP A N   
1231 C CA  . ASP A 168 ? 0.52756 0.48391 0.47436 0.01860  -0.07775 -0.12137 175 ASP A CA  
1232 C C   . ASP A 168 ? 0.61770 0.56933 0.56311 0.01545  -0.09567 -0.13598 175 ASP A C   
1233 O O   . ASP A 168 ? 0.62515 0.59437 0.56309 0.01542  -0.10043 -0.13387 175 ASP A O   
1234 C CB  . ASP A 168 ? 0.43291 0.39588 0.40114 0.00677  -0.07135 -0.10215 175 ASP A CB  
1235 C CG  . ASP A 168 ? 0.65271 0.59966 0.64710 -0.00567 -0.07749 -0.10099 175 ASP A CG  
1236 O OD1 . ASP A 168 ? 0.78875 0.71456 0.78744 -0.00539 -0.07988 -0.10819 175 ASP A OD1 
1237 O OD2 . ASP A 168 ? 0.57762 0.53358 0.58863 -0.01521 -0.07975 -0.09214 175 ASP A OD2 
1238 N N   . THR A 169 ? 0.67864 0.60566 0.63212 0.01246  -0.10657 -0.15030 176 THR A N   
1239 C CA  . THR A 169 ? 0.90612 0.82542 0.86356 0.00624  -0.12608 -0.16578 176 THR A CA  
1240 C C   . THR A 169 ? 0.92412 0.83755 0.91633 -0.01331 -0.13199 -0.15678 176 THR A C   
1241 O O   . THR A 169 ? 0.84496 0.75178 0.84783 -0.02227 -0.14912 -0.16858 176 THR A O   
1242 C CB  . THR A 169 ? 0.91063 0.80399 0.85405 0.01519  -0.13675 -0.18994 176 THR A CB  
1243 O OG1 . THR A 169 ? 0.92355 0.79496 0.87449 0.01757  -0.12795 -0.18642 176 THR A OG1 
1244 C CG2 . THR A 169 ? 0.77632 0.68454 0.68285 0.03494  -0.13588 -0.20313 176 THR A CG2 
1245 N N   . GLY A 170 ? 0.83701 0.75515 0.84725 -0.02009 -0.11840 -0.13642 177 GLY A N   
1246 C CA  . GLY A 170 ? 0.73502 0.65395 0.77757 -0.03714 -0.12070 -0.12519 177 GLY A CA  
1247 C C   . GLY A 170 ? 0.74707 0.69227 0.79899 -0.04296 -0.12837 -0.12211 177 GLY A C   
1248 O O   . GLY A 170 ? 0.73770 0.69655 0.77042 -0.03468 -0.13534 -0.13052 177 GLY A O   
1249 N N   . GLU A 171 ? 0.72113 0.67549 0.80317 -0.05640 -0.12669 -0.10886 178 GLU A N   
1250 C CA  . GLU A 171 ? 0.68007 0.66246 0.77653 -0.06145 -0.13341 -0.10430 178 GLU A CA  
1251 C C   . GLU A 171 ? 0.53613 0.53835 0.61218 -0.04791 -0.12461 -0.09606 178 GLU A C   
1252 O O   . GLU A 171 ? 0.53312 0.53421 0.60330 -0.04273 -0.10859 -0.08369 178 GLU A O   
1253 C CB  . GLU A 171 ? 0.68267 0.67472 0.81511 -0.07594 -0.12834 -0.08878 178 GLU A CB  
1254 C CG  . GLU A 171 ? 0.71730 0.74189 0.87219 -0.08181 -0.13531 -0.08349 178 GLU A CG  
1255 C CD  . GLU A 171 ? 0.78980 0.81686 0.96494 -0.09551 -0.15619 -0.09665 178 GLU A CD  
1256 O OE1 . GLU A 171 ? 0.66036 0.66841 0.85490 -0.11007 -0.16007 -0.09846 178 GLU A OE1 
1257 O OE2 . GLU A 171 ? 0.62770 0.67541 0.80023 -0.09227 -0.16956 -0.10461 178 GLU A OE2 
1258 N N   . PRO A 172 ? 0.51674 0.53563 0.58074 -0.04193 -0.13537 -0.10240 179 PRO A N   
1259 C CA  . PRO A 172 ? 0.52989 0.56456 0.57451 -0.02955 -0.12753 -0.09214 179 PRO A CA  
1260 C C   . PRO A 172 ? 0.51375 0.56250 0.57857 -0.03195 -0.11743 -0.07388 179 PRO A C   
1261 O O   . PRO A 172 ? 0.51347 0.57645 0.60621 -0.04047 -0.12300 -0.07072 179 PRO A O   
1262 C CB  . PRO A 172 ? 0.52968 0.58015 0.56225 -0.02445 -0.14454 -0.10235 179 PRO A CB  
1263 C CG  . PRO A 172 ? 0.51142 0.54719 0.54345 -0.02991 -0.15942 -0.12336 179 PRO A CG  
1264 C CD  . PRO A 172 ? 0.58629 0.60753 0.65008 -0.04521 -0.15634 -0.12034 179 PRO A CD  
1265 N N   . MET A 173 ? 0.42832 0.47432 0.47931 -0.02406 -0.10278 -0.06242 180 MET A N   
1266 C CA  . MET A 173 ? 0.37845 0.43348 0.44413 -0.02377 -0.09277 -0.04730 180 MET A CA  
1267 C C   . MET A 173 ? 0.53784 0.60924 0.59754 -0.01460 -0.09596 -0.03997 180 MET A C   
1268 O O   . MET A 173 ? 0.46160 0.54170 0.53525 -0.01263 -0.09020 -0.02956 180 MET A O   
1269 C CB  . MET A 173 ? 0.37762 0.41878 0.43316 -0.02069 -0.07667 -0.03944 180 MET A CB  
1270 C CG  . MET A 173 ? 0.56983 0.59426 0.62801 -0.02626 -0.07160 -0.04384 180 MET A CG  
1271 S SD  . MET A 173 ? 0.62926 0.64419 0.67028 -0.01979 -0.05591 -0.03587 180 MET A SD  
1272 C CE  . MET A 173 ? 0.48957 0.51466 0.54141 -0.01777 -0.04934 -0.02243 180 MET A CE  
1273 N N   . GLY A 174 ? 0.38803 0.46266 0.42480 -0.00705 -0.10402 -0.04437 181 GLY A N   
1274 C CA  . GLY A 174 ? 0.41015 0.49716 0.43827 0.00315  -0.10680 -0.03493 181 GLY A CA  
1275 C C   . GLY A 174 ? 0.37322 0.44752 0.38208 0.01005  -0.09340 -0.02266 181 GLY A C   
1276 O O   . GLY A 174 ? 0.41468 0.48730 0.39746 0.01723  -0.09393 -0.01960 181 GLY A O   
1277 N N   . ARG A 175 ? 0.31624 0.38207 0.33755 0.00736  -0.08156 -0.01544 182 ARG A N   
1278 C CA  . ARG A 175 ? 0.29181 0.34337 0.29901 0.01113  -0.06975 -0.00513 182 ARG A CA  
1279 C C   . ARG A 175 ? 0.31171 0.35550 0.33533 0.00639  -0.05937 -0.00287 182 ARG A C   
1280 O O   . ARG A 175 ? 0.30734 0.36062 0.35237 0.00531  -0.06041 -0.00274 182 ARG A O   
1281 C CB  . ARG A 175 ? 0.31401 0.36726 0.31241 0.02119  -0.07233 0.00649  182 ARG A CB  
1282 C CG  . ARG A 175 ? 0.32389 0.35880 0.30715 0.02297  -0.06177 0.01763  182 ARG A CG  
1283 C CD  . ARG A 175 ? 0.33474 0.36431 0.31664 0.03245  -0.06363 0.02962  182 ARG A CD  
1284 N NE  . ARG A 175 ? 0.29493 0.32858 0.29971 0.03526  -0.06348 0.02790  182 ARG A NE  
1285 C CZ  . ARG A 175 ? 0.28720 0.33770 0.30473 0.04303  -0.07215 0.02786  182 ARG A CZ  
1286 N NH1 . ARG A 175 ? 0.32755 0.39095 0.33677 0.04888  -0.08347 0.02927  182 ARG A NH1 
1287 N NH2 . ARG A 175 ? 0.29763 0.35537 0.33669 0.04589  -0.06953 0.02634  182 ARG A NH2 
1288 N N   . GLY A 176 ? 0.26648 0.29633 0.28032 0.00392  -0.04948 -0.00103 183 GLY A N   
1289 C CA  . GLY A 176 ? 0.25560 0.27821 0.28064 0.00131  -0.04045 0.00147  183 GLY A CA  
1290 C C   . GLY A 176 ? 0.34234 0.35791 0.36586 -0.00483 -0.03447 -0.00365 183 GLY A C   
1291 O O   . GLY A 176 ? 0.29319 0.30691 0.30388 -0.00554 -0.03508 -0.00786 183 GLY A O   
1292 N N   . THR A 177 ? 0.28936 0.30261 0.32529 -0.00764 -0.02862 -0.00329 184 THR A N   
1293 C CA  . THR A 177 ? 0.26197 0.26809 0.29640 -0.01163 -0.02282 -0.00635 184 THR A CA  
1294 C C   . THR A 177 ? 0.28979 0.29869 0.34112 -0.01539 -0.02109 -0.00689 184 THR A C   
1295 O O   . THR A 177 ? 0.26284 0.27882 0.32532 -0.01393 -0.01914 -0.00262 184 THR A O   
1296 C CB  . THR A 177 ? 0.31113 0.30942 0.33740 -0.01063 -0.01548 -0.00213 184 THR A CB  
1297 O OG1 . THR A 177 ? 0.31379 0.30996 0.32586 -0.00916 -0.01614 0.00111  184 THR A OG1 
1298 C CG2 . THR A 177 ? 0.28639 0.28122 0.31257 -0.01341 -0.01052 -0.00522 184 THR A CG2 
1299 N N   . LYS A 178 ? 0.25668 0.26024 0.30936 -0.01932 -0.02162 -0.01154 185 LYS A N   
1300 C CA  . LYS A 178 ? 0.27119 0.27354 0.33792 -0.02399 -0.01927 -0.00982 185 LYS A CA  
1301 C C   . LYS A 178 ? 0.28563 0.27833 0.34419 -0.02242 -0.01308 -0.00967 185 LYS A C   
1302 O O   . LYS A 178 ? 0.29660 0.28255 0.34510 -0.02071 -0.01470 -0.01539 185 LYS A O   
1303 C CB  . LYS A 178 ? 0.31326 0.31343 0.38903 -0.02996 -0.02792 -0.01561 185 LYS A CB  
1304 C CG  . LYS A 178 ? 0.47866 0.47681 0.57238 -0.03752 -0.02712 -0.01166 185 LYS A CG  
1305 C CD  . LYS A 178 ? 0.47284 0.46824 0.57793 -0.04540 -0.03872 -0.01860 185 LYS A CD  
1306 C CE  . LYS A 178 ? 0.61700 0.62664 0.72217 -0.04396 -0.04737 -0.02333 185 LYS A CE  
1307 N NZ  . LYS A 178 ? 0.80644 0.81432 0.92214 -0.05193 -0.06093 -0.03246 185 LYS A NZ  
1308 N N   . VAL A 179 ? 0.22409 0.21861 0.28587 -0.02137 -0.00623 -0.00372 186 VAL A N   
1309 C CA  . VAL A 179 ? 0.21225 0.20034 0.26770 -0.01934 -0.00167 -0.00310 186 VAL A CA  
1310 C C   . VAL A 179 ? 0.27742 0.26203 0.34305 -0.02254 -0.00030 0.00174  186 VAL A C   
1311 O O   . VAL A 179 ? 0.27790 0.27078 0.35301 -0.02424 0.00340  0.00881  186 VAL A O   
1312 C CB  . VAL A 179 ? 0.23882 0.23054 0.28769 -0.01543 0.00357  -0.00062 186 VAL A CB  
1313 C CG1 . VAL A 179 ? 0.26696 0.25566 0.31072 -0.01307 0.00671  -0.00009 186 VAL A CG1 
1314 C CG2 . VAL A 179 ? 0.31853 0.30991 0.35867 -0.01433 0.00195  -0.00336 186 VAL A CG2 
1315 N N   . ILE A 180 ? 0.23080 0.20331 0.29464 -0.02277 -0.00299 -0.00128 187 ILE A N   
1316 C CA  . ILE A 180 ? 0.24698 0.21051 0.32031 -0.02662 -0.00281 0.00466  187 ILE A CA  
1317 C C   . ILE A 180 ? 0.28055 0.23973 0.34548 -0.02031 0.00203  0.00891  187 ILE A C   
1318 O O   . ILE A 180 ? 0.30653 0.25963 0.36208 -0.01437 0.00033  0.00276  187 ILE A O   
1319 C CB  . ILE A 180 ? 0.30792 0.25588 0.38565 -0.03059 -0.01135 -0.00238 187 ILE A CB  
1320 C CG1 . ILE A 180 ? 0.30282 0.25825 0.38704 -0.03589 -0.01815 -0.00831 187 ILE A CG1 
1321 C CG2 . ILE A 180 ? 0.32208 0.25648 0.41161 -0.03650 -0.01162 0.00590  187 ILE A CG2 
1322 C CD1 . ILE A 180 ? 0.37338 0.31399 0.45552 -0.03720 -0.02861 -0.02045 187 ILE A CD1 
1323 N N   . LEU A 181 ? 0.25073 0.21611 0.31868 -0.02042 0.00809  0.01958  188 LEU A N   
1324 C CA  . LEU A 181 ? 0.26652 0.23073 0.32525 -0.01352 0.01196  0.02471  188 LEU A CA  
1325 C C   . LEU A 181 ? 0.30574 0.25445 0.36997 -0.01547 0.01135  0.03352  188 LEU A C   
1326 O O   . LEU A 181 ? 0.29542 0.24581 0.37014 -0.02210 0.01461  0.04457  188 LEU A O   
1327 C CB  . LEU A 181 ? 0.23785 0.21816 0.29263 -0.01057 0.01863  0.03085  188 LEU A CB  
1328 C CG  . LEU A 181 ? 0.26963 0.26026 0.32024 -0.00908 0.01843  0.02279  188 LEU A CG  
1329 C CD1 . LEU A 181 ? 0.31157 0.31514 0.35730 -0.00441 0.02422  0.02696  188 LEU A CD1 
1330 C CD2 . LEU A 181 ? 0.27743 0.26511 0.31859 -0.00563 0.01488  0.01383  188 LEU A CD2 
1331 N N   . HIS A 182 ? 0.28103 0.21504 0.33909 -0.00943 0.00744  0.02961  189 HIS A N   
1332 C CA  . HIS A 182 ? 0.33964 0.25401 0.40072 -0.00907 0.00623  0.03886  189 HIS A CA  
1333 C C   . HIS A 182 ? 0.31852 0.24107 0.37007 -0.00122 0.01191  0.05023  189 HIS A C   
1334 O O   . HIS A 182 ? 0.33670 0.26353 0.37741 0.00926  0.01076  0.04554  189 HIS A O   
1335 C CB  . HIS A 182 ? 0.33982 0.23376 0.39733 -0.00290 -0.00115 0.02834  189 HIS A CB  
1336 C CG  . HIS A 182 ? 0.35482 0.24375 0.41661 -0.00803 -0.00748 0.01443  189 HIS A CG  
1337 N ND1 . HIS A 182 ? 0.42050 0.28846 0.49266 -0.01621 -0.01428 0.01253  189 HIS A ND1 
1338 C CD2 . HIS A 182 ? 0.37039 0.27287 0.42671 -0.00628 -0.00864 0.00226  189 HIS A CD2 
1339 C CE1 . HIS A 182 ? 0.41768 0.28798 0.48900 -0.01803 -0.02003 -0.00183 189 HIS A CE1 
1340 N NE2 . HIS A 182 ? 0.39108 0.28240 0.45209 -0.01162 -0.01603 -0.00714 189 HIS A NE2 
1341 N N   . LEU A 183 ? 0.31429 0.24243 0.36995 -0.00593 0.01805  0.06539  190 LEU A N   
1342 C CA  . LEU A 183 ? 0.31702 0.26000 0.36009 0.00236  0.02398  0.07456  190 LEU A CA  
1343 C C   . LEU A 183 ? 0.36474 0.29362 0.39891 0.01179  0.02200  0.08306  190 LEU A C   
1344 O O   . LEU A 183 ? 0.40670 0.31129 0.44738 0.00918  0.01905  0.09012  190 LEU A O   
1345 C CB  . LEU A 183 ? 0.29228 0.24959 0.34057 -0.00362 0.03268  0.08898  190 LEU A CB  
1346 C CG  . LEU A 183 ? 0.29360 0.26915 0.34942 -0.00907 0.03506  0.08111  190 LEU A CG  
1347 C CD1 . LEU A 183 ? 0.32757 0.32154 0.38972 -0.01281 0.04496  0.09637  190 LEU A CD1 
1348 C CD2 . LEU A 183 ? 0.32476 0.31245 0.36719 -0.00061 0.03338  0.06660  190 LEU A CD2 
1349 N N   . LYS A 184 ? 0.39806 0.30709 0.34299 0.08883  -0.00423 0.03918  191 LYS A N   
1350 C CA  . LYS A 184 ? 0.42331 0.31873 0.37136 0.10419  -0.00595 0.05533  191 LYS A CA  
1351 C C   . LYS A 184 ? 0.50674 0.36416 0.44863 0.09384  -0.00492 0.06886  191 LYS A C   
1352 O O   . LYS A 184 ? 0.46901 0.32766 0.40679 0.07327  -0.00294 0.07027  191 LYS A O   
1353 C CB  . LYS A 184 ? 0.44502 0.38155 0.39760 0.10934  -0.01163 0.06889  191 LYS A CB  
1354 C CG  . LYS A 184 ? 0.47330 0.45097 0.44144 0.11798  -0.00991 0.06079  191 LYS A CG  
1355 C CD  . LYS A 184 ? 0.47445 0.49300 0.45422 0.11542  -0.01847 0.07110  191 LYS A CD  
1356 C CE  . LYS A 184 ? 0.60440 0.66563 0.60842 0.11786  -0.01411 0.06549  191 LYS A CE  
1357 N NZ  . LYS A 184 ? 0.48897 0.58980 0.51244 0.10989  -0.02417 0.07073  191 LYS A NZ  
1358 N N   . GLU A 185 ? 0.50679 0.33121 0.44997 0.10968  -0.00458 0.08113  192 GLU A N   
1359 C CA  . GLU A 185 ? 0.53271 0.31256 0.47213 0.10092  0.00019  0.09815  192 GLU A CA  
1360 C C   . GLU A 185 ? 0.65152 0.44885 0.57551 0.08793  0.00173  0.11957  192 GLU A C   
1361 O O   . GLU A 185 ? 0.61900 0.39244 0.54189 0.07044  0.01056  0.12921  192 GLU A O   
1362 C CB  . GLU A 185 ? 0.61998 0.36265 0.56155 0.12535  -0.00035 0.11366  192 GLU A CB  
1363 C CG  . GLU A 185 ? 0.94375 0.63747 0.89996 0.13076  0.00299  0.09465  192 GLU A CG  
1364 C CD  . GLU A 185 ? 1.18042 0.82202 1.14007 0.15098  0.00459  0.11534  192 GLU A CD  
1365 O OE1 . GLU A 185 ? 1.26970 0.85310 1.24036 0.14140  0.01032  0.11317  192 GLU A OE1 
1366 O OE2 . GLU A 185 ? 1.24474 0.90344 1.19905 0.17654  -0.00090 0.13404  192 GLU A OE2 
1367 N N   . ASP A 186 ? 0.52772 0.36743 0.44142 0.09607  -0.00609 0.12599  193 ASP A N   
1368 C CA  . ASP A 186 ? 0.54065 0.39774 0.43340 0.08823  -0.00607 0.14262  193 ASP A CA  
1369 C C   . ASP A 186 ? 0.55214 0.44272 0.44548 0.06922  -0.00551 0.12616  193 ASP A C   
1370 O O   . ASP A 186 ? 0.54215 0.45432 0.41766 0.06547  -0.00707 0.13315  193 ASP A O   
1371 C CB  . ASP A 186 ? 0.60777 0.48919 0.48689 0.10987  -0.01890 0.15785  193 ASP A CB  
1372 C CG  . ASP A 186 ? 0.74557 0.66979 0.64375 0.11868  -0.03061 0.14036  193 ASP A CG  
1373 O OD1 . ASP A 186 ? 0.86841 0.82163 0.76377 0.13391  -0.04425 0.14811  193 ASP A OD1 
1374 O OD2 . ASP A 186 ? 0.77354 0.70476 0.69035 0.11064  -0.02629 0.11990  193 ASP A OD2 
1375 N N   . GLN A 187 ? 0.44310 0.33723 0.35384 0.05943  -0.00377 0.10415  194 GLN A N   
1376 C CA  . GLN A 187 ? 0.39000 0.31219 0.30333 0.04443  -0.00374 0.09014  194 GLN A CA  
1377 C C   . GLN A 187 ? 0.42210 0.32918 0.34534 0.02627  0.00430  0.08113  194 GLN A C   
1378 O O   . GLN A 187 ? 0.40944 0.33493 0.34052 0.01789  0.00269  0.06564  194 GLN A O   
1379 C CB  . GLN A 187 ? 0.40917 0.35764 0.33397 0.05024  -0.00997 0.07494  194 GLN A CB  
1380 C CG  . GLN A 187 ? 0.41960 0.39324 0.34680 0.06505  -0.01869 0.08124  194 GLN A CG  
1381 C CD  . GLN A 187 ? 0.44220 0.43574 0.35613 0.06209  -0.02570 0.08874  194 GLN A CD  
1382 O OE1 . GLN A 187 ? 0.45685 0.45836 0.36494 0.04856  -0.02363 0.08243  194 GLN A OE1 
1383 N NE2 . GLN A 187 ? 0.45516 0.45923 0.36410 0.07709  -0.03552 0.09992  194 GLN A NE2 
1384 N N   . THR A 188 ? 0.46261 0.33716 0.38916 0.01984  0.01254  0.09171  195 THR A N   
1385 C CA  . THR A 188 ? 0.48343 0.34786 0.42980 0.00056  0.01835  0.08068  195 THR A CA  
1386 C C   . THR A 188 ? 0.46062 0.35078 0.40809 -0.01385 0.02580  0.08345  195 THR A C   
1387 O O   . THR A 188 ? 0.42336 0.31539 0.39364 -0.03003 0.02988  0.07367  195 THR A O   
1388 C CB  . THR A 188 ? 0.53369 0.35272 0.49264 -0.00526 0.02598  0.09059  195 THR A CB  
1389 O OG1 . THR A 188 ? 0.55610 0.36335 0.49887 -0.00278 0.03647  0.12141  195 THR A OG1 
1390 C CG2 . THR A 188 ? 0.54375 0.33451 0.50476 0.01100  0.01852  0.08148  195 THR A CG2 
1391 N N   . GLU A 189 ? 0.43318 0.34545 0.35868 -0.00733 0.02674  0.09388  196 GLU A N   
1392 C CA  . GLU A 189 ? 0.47841 0.41692 0.40347 -0.01705 0.03417  0.09163  196 GLU A CA  
1393 C C   . GLU A 189 ? 0.43118 0.39091 0.37542 -0.02249 0.02715  0.06849  196 GLU A C   
1394 O O   . GLU A 189 ? 0.40227 0.37901 0.36030 -0.03239 0.03383  0.06309  196 GLU A O   
1395 C CB  . GLU A 189 ? 0.45613 0.41327 0.35020 -0.00587 0.03238  0.10016  196 GLU A CB  
1396 C CG  . GLU A 189 ? 0.41005 0.38742 0.30130 0.00326  0.01661  0.08505  196 GLU A CG  
1397 C CD  . GLU A 189 ? 0.59880 0.59249 0.46247 0.01383  0.01026  0.09009  196 GLU A CD  
1398 O OE1 . GLU A 189 ? 0.48907 0.50285 0.34616 0.01182  0.00961  0.07871  196 GLU A OE1 
1399 O OE2 . GLU A 189 ? 0.60166 0.58811 0.45053 0.02581  0.00416  0.10372  196 GLU A OE2 
1400 N N   . TYR A 190 ? 0.37851 0.33900 0.32433 -0.01446 0.01494  0.05646  197 TYR A N   
1401 C CA  . TYR A 190 ? 0.31779 0.29637 0.27550 -0.01621 0.00808  0.03918  197 TYR A CA  
1402 C C   . TYR A 190 ? 0.37843 0.35011 0.35746 -0.02515 0.00571  0.02650  197 TYR A C   
1403 O O   . TYR A 190 ? 0.38233 0.36850 0.36754 -0.02349 -0.00259 0.01279  197 TYR A O   
1404 C CB  . TYR A 190 ? 0.30709 0.29208 0.25590 -0.00389 -0.00075 0.03517  197 TYR A CB  
1405 C CG  . TYR A 190 ? 0.32989 0.32631 0.26622 0.00168  -0.00186 0.04338  197 TYR A CG  
1406 C CD1 . TYR A 190 ? 0.33526 0.34790 0.26966 -0.00186 -0.00105 0.04017  197 TYR A CD1 
1407 C CD2 . TYR A 190 ? 0.35792 0.34932 0.28571 0.01159  -0.00506 0.05242  197 TYR A CD2 
1408 C CE1 . TYR A 190 ? 0.37699 0.39952 0.29933 0.00268  -0.00511 0.04255  197 TYR A CE1 
1409 C CE2 . TYR A 190 ? 0.38306 0.38924 0.30164 0.01638  -0.01022 0.05694  197 TYR A CE2 
1410 C CZ  . TYR A 190 ? 0.39298 0.41398 0.30769 0.01098  -0.01095 0.05065  197 TYR A CZ  
1411 O OH  . TYR A 190 ? 0.42159 0.45690 0.32624 0.01547  -0.01917 0.05014  197 TYR A OH  
1412 N N   . LEU A 191 ? 0.34687 0.29619 0.33798 -0.03450 0.01171  0.03092  198 LEU A N   
1413 C CA  . LEU A 191 ? 0.39065 0.33688 0.41078 -0.04814 0.00874  0.01650  198 LEU A CA  
1414 C C   . LEU A 191 ? 0.41522 0.37964 0.46041 -0.06428 0.02021  0.02184  198 LEU A C   
1415 O O   . LEU A 191 ? 0.40324 0.37455 0.48205 -0.07802 0.01685  0.00876  198 LEU A O   
1416 C CB  . LEU A 191 ? 0.40597 0.31265 0.43379 -0.05153 0.00861  0.01521  198 LEU A CB  
1417 C CG  . LEU A 191 ? 0.42778 0.31935 0.43426 -0.03298 -0.00106 0.00631  198 LEU A CG  
1418 C CD1 . LEU A 191 ? 0.45902 0.30612 0.47384 -0.03345 -0.00040 0.00366  198 LEU A CD1 
1419 C CD2 . LEU A 191 ? 0.44112 0.35508 0.44357 -0.02675 -0.01447 -0.01625 198 LEU A CD2 
1420 N N   . GLU A 192 ? 0.34961 0.32509 0.38051 -0.06232 0.03354  0.03908  199 GLU A N   
1421 C CA  . GLU A 192 ? 0.38983 0.38475 0.44167 -0.07530 0.05012  0.04683  199 GLU A CA  
1422 C C   . GLU A 192 ? 0.32036 0.35412 0.38540 -0.07234 0.04584  0.03210  199 GLU A C   
1423 O O   . GLU A 192 ? 0.33395 0.37701 0.37554 -0.05796 0.03883  0.02801  199 GLU A O   
1424 C CB  . GLU A 192 ? 0.42116 0.41127 0.44340 -0.07059 0.06741  0.07130  199 GLU A CB  
1425 C CG  . GLU A 192 ? 0.50976 0.46064 0.51882 -0.07102 0.07365  0.09227  199 GLU A CG  
1426 C CD  . GLU A 192 ? 0.83561 0.76701 0.88351 -0.09216 0.08544  0.09892  199 GLU A CD  
1427 O OE1 . GLU A 192 ? 0.91126 0.86868 0.99586 -0.10802 0.09396  0.09223  199 GLU A OE1 
1428 O OE2 . GLU A 192 ? 0.86600 0.75594 0.91229 -0.09295 0.08610  0.11050  199 GLU A OE2 
1429 N N   . GLU A 193 ? 0.34461 0.40095 0.45177 -0.08602 0.05028  0.02475  200 GLU A N   
1430 C CA  . GLU A 193 ? 0.32890 0.42347 0.45452 -0.08041 0.04478  0.01068  200 GLU A CA  
1431 C C   . GLU A 193 ? 0.29103 0.40053 0.39224 -0.06786 0.05704  0.01759  200 GLU A C   
1432 O O   . GLU A 193 ? 0.28317 0.40194 0.37291 -0.05348 0.04641  0.00784  200 GLU A O   
1433 C CB  . GLU A 193 ? 0.35388 0.47702 0.53620 -0.09762 0.04958  0.00336  200 GLU A CB  
1434 C CG  . GLU A 193 ? 0.34333 0.51096 0.55112 -0.08893 0.04413  -0.01014 200 GLU A CG  
1435 C CD  . GLU A 193 ? 0.63975 0.84556 0.91194 -0.10614 0.05146  -0.01601 200 GLU A CD  
1436 O OE1 . GLU A 193 ? 0.63408 0.82907 0.93505 -0.12835 0.05895  -0.01138 200 GLU A OE1 
1437 O OE2 . GLU A 193 ? 0.67091 0.91787 0.96995 -0.09739 0.04913  -0.02564 200 GLU A OE2 
1438 N N   . ARG A 194 ? 0.31326 0.42272 0.40379 -0.07217 0.07955  0.03435  201 ARG A N   
1439 C CA  . ARG A 194 ? 0.31526 0.44102 0.37966 -0.05862 0.09021  0.03534  201 ARG A CA  
1440 C C   . ARG A 194 ? 0.32231 0.42798 0.34293 -0.04353 0.07571  0.03264  201 ARG A C   
1441 O O   . ARG A 194 ? 0.34478 0.46150 0.35216 -0.03114 0.07335  0.02227  201 ARG A O   
1442 C CB  . ARG A 194 ? 0.35995 0.49175 0.41252 -0.06355 0.11832  0.05491  201 ARG A CB  
1443 C CG  . ARG A 194 ? 0.59876 0.69902 0.64074 -0.07439 0.12568  0.07757  201 ARG A CG  
1444 C CD  . ARG A 194 ? 0.68107 0.79309 0.72045 -0.08132 0.15807  0.10067  201 ARG A CD  
1445 N NE  . ARG A 194 ? 0.89048 0.97048 0.88492 -0.07707 0.16489  0.12678  201 ARG A NE  
1446 C CZ  . ARG A 194 ? 0.81946 0.90329 0.79062 -0.07704 0.19256  0.15311  201 ARG A CZ  
1447 N NH1 . ARG A 194 ? 0.64883 0.76943 0.63857 -0.08199 0.21936  0.15613  201 ARG A NH1 
1448 N NH2 . ARG A 194 ? 0.81257 0.86492 0.73991 -0.06967 0.19430  0.17838  201 ARG A NH2 
1449 N N   . ARG A 195 ? 0.31152 0.38831 0.31424 -0.04429 0.06582  0.04038  202 ARG A N   
1450 C CA  . ARG A 195 ? 0.30436 0.36864 0.27518 -0.03168 0.05207  0.03781  202 ARG A CA  
1451 C C   . ARG A 195 ? 0.31784 0.38608 0.30068 -0.02595 0.03545  0.02217  202 ARG A C   
1452 O O   . ARG A 195 ? 0.29470 0.36526 0.26470 -0.01689 0.02916  0.01536  202 ARG A O   
1453 C CB  . ARG A 195 ? 0.34111 0.37837 0.29509 -0.03155 0.04748  0.05109  202 ARG A CB  
1454 C CG  . ARG A 195 ? 0.34485 0.37599 0.27401 -0.01940 0.03339  0.04929  202 ARG A CG  
1455 C CD  . ARG A 195 ? 0.39093 0.43309 0.29026 -0.01127 0.03614  0.05084  202 ARG A CD  
1456 N NE  . ARG A 195 ? 0.40428 0.44270 0.28672 -0.00222 0.02079  0.05001  202 ARG A NE  
1457 C CZ  . ARG A 195 ? 0.43969 0.48902 0.31777 0.00263  0.01014  0.03578  202 ARG A CZ  
1458 N NH1 . ARG A 195 ? 0.38871 0.44849 0.27188 0.00226  0.01347  0.02117  202 ARG A NH1 
1459 N NH2 . ARG A 195 ? 0.42818 0.47784 0.30189 0.00792  -0.00435 0.03526  202 ARG A NH2 
1460 N N   . ILE A 196 ? 0.29463 0.36260 0.30141 -0.03094 0.02779  0.01646  203 ILE A N   
1461 C CA  . ILE A 196 ? 0.26729 0.33940 0.27950 -0.02304 0.01328  0.00606  203 ILE A CA  
1462 C C   . ILE A 196 ? 0.26736 0.35994 0.29264 -0.01655 0.01507  -0.00204 203 ILE A C   
1463 O O   . ILE A 196 ? 0.27897 0.36772 0.29656 -0.00677 0.00813  -0.00548 203 ILE A O   
1464 C CB  . ILE A 196 ? 0.24731 0.31765 0.27584 -0.02723 0.00310  -0.00029 203 ILE A CB  
1465 C CG1 . ILE A 196 ? 0.26211 0.30692 0.27612 -0.02982 0.00172  0.00504  203 ILE A CG1 
1466 C CG2 . ILE A 196 ? 0.24261 0.31934 0.26950 -0.01593 -0.01106 -0.00730 203 ILE A CG2 
1467 C CD1 . ILE A 196 ? 0.40772 0.44635 0.44032 -0.03781 -0.00515 -0.00489 203 ILE A CD1 
1468 N N   . LYS A 197 ? 0.24756 0.36149 0.29630 -0.02159 0.02591  -0.00457 204 LYS A N   
1469 C CA  . LYS A 197 ? 0.24513 0.38105 0.30975 -0.01215 0.02959  -0.01352 204 LYS A CA  
1470 C C   . LYS A 197 ? 0.28442 0.41083 0.32184 -0.00244 0.03431  -0.01603 204 LYS A C   
1471 O O   . LYS A 197 ? 0.27743 0.40251 0.31795 0.00930  0.02818  -0.02479 204 LYS A O   
1472 C CB  . LYS A 197 ? 0.25246 0.41809 0.34853 -0.01967 0.04579  -0.01422 204 LYS A CB  
1473 C CG  . LYS A 197 ? 0.43245 0.62139 0.57215 -0.02523 0.03668  -0.02105 204 LYS A CG  
1474 C CD  . LYS A 197 ? 0.50113 0.72966 0.68085 -0.02838 0.05421  -0.02405 204 LYS A CD  
1475 C CE  . LYS A 197 ? 0.62750 0.86772 0.84166 -0.05106 0.06280  -0.01873 204 LYS A CE  
1476 N NZ  . LYS A 197 ? 0.55579 0.84360 0.83153 -0.05457 0.06235  -0.02916 204 LYS A NZ  
1477 N N   . GLU A 198 ? 0.27975 0.39813 0.29035 -0.00647 0.04398  -0.00893 205 GLU A N   
1478 C CA  . GLU A 198 ? 0.29115 0.40238 0.27247 0.00238  0.04471  -0.01521 205 GLU A CA  
1479 C C   . GLU A 198 ? 0.33592 0.42723 0.31155 0.00670  0.02682  -0.02015 205 GLU A C   
1480 O O   . GLU A 198 ? 0.31143 0.39785 0.28528 0.01491  0.02288  -0.03288 205 GLU A O   
1481 C CB  . GLU A 198 ? 0.30599 0.41250 0.25513 -0.00130 0.05335  -0.00346 205 GLU A CB  
1482 C CG  . GLU A 198 ? 0.42302 0.52654 0.33697 0.00835  0.05072  -0.01246 205 GLU A CG  
1483 C CD  . GLU A 198 ? 0.44013 0.53991 0.31798 0.00783  0.05519  0.00280  205 GLU A CD  
1484 O OE1 . GLU A 198 ? 0.43343 0.51990 0.31324 0.00126  0.05050  0.01874  205 GLU A OE1 
1485 O OE2 . GLU A 198 ? 0.43454 0.54439 0.28000 0.01633  0.06346  -0.00118 205 GLU A OE2 
1486 N N   . ILE A 199 ? 0.27429 0.35313 0.24910 0.00111  0.01743  -0.01043 206 ILE A N   
1487 C CA  . ILE A 199 ? 0.26312 0.32707 0.23531 0.00345  0.00469  -0.01109 206 ILE A CA  
1488 C C   . ILE A 199 ? 0.30403 0.36562 0.29592 0.00971  -0.00058 -0.01537 206 ILE A C   
1489 O O   . ILE A 199 ? 0.31858 0.36757 0.31284 0.01322  -0.00599 -0.01955 206 ILE A O   
1490 C CB  . ILE A 199 ? 0.29024 0.34601 0.25722 -0.00118 -0.00038 0.00051  206 ILE A CB  
1491 C CG1 . ILE A 199 ? 0.31199 0.36603 0.25881 -0.00360 0.00301  0.00729  206 ILE A CG1 
1492 C CG2 . ILE A 199 ? 0.31670 0.36351 0.28747 0.00075  -0.00930 0.00241  206 ILE A CG2 
1493 C CD1 . ILE A 199 ? 0.34538 0.39010 0.29145 -0.00580 0.00088  0.01788  206 ILE A CD1 
1494 N N   . VAL A 200 ? 0.27969 0.35248 0.28786 0.01128  -0.00046 -0.01364 207 VAL A N   
1495 C CA  . VAL A 200 ? 0.28225 0.35420 0.30588 0.02114  -0.00740 -0.01445 207 VAL A CA  
1496 C C   . VAL A 200 ? 0.30629 0.37824 0.33986 0.03070  -0.00338 -0.02572 207 VAL A C   
1497 O O   . VAL A 200 ? 0.31375 0.36871 0.35299 0.03887  -0.00869 -0.02584 207 VAL A O   
1498 C CB  . VAL A 200 ? 0.25198 0.34231 0.29115 0.02230  -0.01208 -0.01330 207 VAL A CB  
1499 C CG1 . VAL A 200 ? 0.29699 0.39285 0.35248 0.03730  -0.02002 -0.01401 207 VAL A CG1 
1500 C CG2 . VAL A 200 ? 0.27829 0.36209 0.30434 0.01645  -0.01835 -0.00635 207 VAL A CG2 
1501 N N   . LYS A 201 ? 0.29993 0.38906 0.33573 0.03068  0.00788  -0.03484 208 LYS A N   
1502 C CA  . LYS A 201 ? 0.31009 0.40070 0.35293 0.04283  0.01368  -0.04951 208 LYS A CA  
1503 C C   . LYS A 201 ? 0.35316 0.41664 0.37873 0.04364  0.00909  -0.05832 208 LYS A C   
1504 O O   . LYS A 201 ? 0.37595 0.42365 0.41191 0.05437  0.00631  -0.06921 208 LYS A O   
1505 C CB  . LYS A 201 ? 0.30996 0.42804 0.35318 0.04254  0.03087  -0.05614 208 LYS A CB  
1506 C CG  . LYS A 201 ? 0.41494 0.54099 0.46726 0.05908  0.03980  -0.07411 208 LYS A CG  
1507 C CD  . LYS A 201 ? 0.49705 0.65445 0.54568 0.05908  0.06173  -0.07812 208 LYS A CD  
1508 C CE  . LYS A 201 ? 0.70028 0.87076 0.76046 0.07923  0.07304  -0.09819 208 LYS A CE  
1509 N NZ  . LYS A 201 ? 0.78311 0.98743 0.83508 0.08049  0.09915  -0.10070 208 LYS A NZ  
1510 N N   . LYS A 202 ? 0.34164 0.39900 0.34455 0.03263  0.00671  -0.05467 209 LYS A N   
1511 C CA  . LYS A 202 ? 0.36834 0.40691 0.35901 0.03113  -0.00054 -0.06644 209 LYS A CA  
1512 C C   . LYS A 202 ? 0.38244 0.39621 0.39074 0.02813  -0.01140 -0.06047 209 LYS A C   
1513 O O   . LYS A 202 ? 0.39780 0.39062 0.41487 0.03029  -0.01657 -0.07399 209 LYS A O   
1514 C CB  . LYS A 202 ? 0.40274 0.44869 0.36699 0.02241  -0.00199 -0.06241 209 LYS A CB  
1515 C CG  . LYS A 202 ? 0.41973 0.45489 0.37259 0.02002  -0.01355 -0.07694 209 LYS A CG  
1516 C CD  . LYS A 202 ? 0.59902 0.64865 0.52120 0.01722  -0.01488 -0.07220 209 LYS A CD  
1517 C CE  . LYS A 202 ? 0.74406 0.79151 0.65218 0.01695  -0.02995 -0.09104 209 LYS A CE  
1518 N NZ  . LYS A 202 ? 0.74197 0.80410 0.62425 0.01585  -0.03574 -0.08003 209 LYS A NZ  
1519 N N   . HIS A 203 ? 0.34681 0.36131 0.36038 0.02300  -0.01378 -0.04056 210 HIS A N   
1520 C CA  . HIS A 203 ? 0.37782 0.37332 0.40336 0.01800  -0.01984 -0.02962 210 HIS A CA  
1521 C C   . HIS A 203 ? 0.39377 0.38005 0.43233 0.02644  -0.01970 -0.01459 210 HIS A C   
1522 O O   . HIS A 203 ? 0.37705 0.34299 0.42707 0.02420  -0.02122 -0.00369 210 HIS A O   
1523 C CB  . HIS A 203 ? 0.41233 0.41722 0.42889 0.00794  -0.02139 -0.01724 210 HIS A CB  
1524 C CG  . HIS A 203 ? 0.39033 0.40312 0.39479 0.00153  -0.02528 -0.02786 210 HIS A CG  
1525 N ND1 . HIS A 203 ? 0.42248 0.42628 0.43591 -0.00394 -0.03337 -0.04118 210 HIS A ND1 
1526 C CD2 . HIS A 203 ? 0.44904 0.47745 0.43294 0.00074  -0.02375 -0.02684 210 HIS A CD2 
1527 C CE1 . HIS A 203 ? 0.50541 0.52356 0.50114 -0.00608 -0.03877 -0.04901 210 HIS A CE1 
1528 N NE2 . HIS A 203 ? 0.46295 0.49451 0.43905 -0.00240 -0.03190 -0.03807 210 HIS A NE2 
1529 N N   . SER A 204 ? 0.40958 0.41112 0.28024 -0.01660 -0.05066 -0.07616 211 SER A N   
1530 C CA  . SER A 204 ? 0.36451 0.36301 0.26895 -0.00642 -0.03985 -0.07278 211 SER A CA  
1531 C C   . SER A 204 ? 0.39191 0.37923 0.29015 0.00485  -0.02181 -0.08706 211 SER A C   
1532 O O   . SER A 204 ? 0.44439 0.43623 0.36613 0.01540  -0.01239 -0.08124 211 SER A O   
1533 C CB  . SER A 204 ? 0.37200 0.39050 0.30047 -0.00061 -0.03742 -0.05259 211 SER A CB  
1534 O OG  . SER A 204 ? 0.41159 0.44335 0.35262 -0.00737 -0.05293 -0.04006 211 SER A OG  
1535 N N   . GLN A 205 ? 0.47282 0.44744 0.34043 0.00322  -0.01737 -0.10691 212 GLN A N   
1536 C CA  . GLN A 205 ? 0.59778 0.56988 0.46228 0.01618  0.00270  -0.12121 212 GLN A CA  
1537 C C   . GLN A 205 ? 0.60690 0.56110 0.50121 0.02853  0.00641  -0.12722 212 GLN A C   
1538 O O   . GLN A 205 ? 0.60093 0.56285 0.51149 0.04313  0.02052  -0.13020 212 GLN A O   
1539 C CB  . GLN A 205 ? 0.66265 0.62566 0.48402 0.01173  0.00857  -0.14378 212 GLN A CB  
1540 C CG  . GLN A 205 ? 0.80562 0.76398 0.62571 0.02635  0.03083  -0.16555 212 GLN A CG  
1541 C CD  . GLN A 205 ? 0.85381 0.80581 0.62426 0.02077  0.03944  -0.18952 212 GLN A CD  
1542 O OE1 . GLN A 205 ? 0.87894 0.80513 0.62421 0.01230  0.02794  -0.20730 212 GLN A OE1 
1543 N NE2 . GLN A 205 ? 0.96109 0.93733 0.71555 0.02360  0.06036  -0.19069 212 GLN A NE2 
1544 N N   . PHE A 206 ? 0.46421 0.39627 0.36886 0.02235  -0.00699 -0.12637 213 PHE A N   
1545 C CA  . PHE A 206 ? 0.43838 0.34542 0.36579 0.03274  -0.00532 -0.12992 213 PHE A CA  
1546 C C   . PHE A 206 ? 0.49895 0.41195 0.45529 0.03252  -0.01159 -0.10611 213 PHE A C   
1547 O O   . PHE A 206 ? 0.49408 0.38263 0.46545 0.03619  -0.01464 -0.10321 213 PHE A O   
1548 C CB  . PHE A 206 ? 0.47922 0.34764 0.39360 0.02470  -0.01334 -0.14891 213 PHE A CB  
1549 C CG  . PHE A 206 ? 0.56098 0.41841 0.44374 0.02809  -0.00411 -0.17771 213 PHE A CG  
1550 C CD1 . PHE A 206 ? 0.62795 0.49371 0.51383 0.04783  0.01562  -0.18913 213 PHE A CD1 
1551 C CD2 . PHE A 206 ? 0.69275 0.53603 0.54252 0.01103  -0.01462 -0.19412 213 PHE A CD2 
1552 C CE1 . PHE A 206 ? 0.70935 0.56861 0.56470 0.05148  0.02854  -0.21742 213 PHE A CE1 
1553 C CE2 . PHE A 206 ? 0.74743 0.58060 0.56041 0.01359  -0.00443 -0.22310 213 PHE A CE2 
1554 C CZ  . PHE A 206 ? 0.80196 0.64311 0.61703 0.03436  0.01921  -0.23513 213 PHE A CZ  
1555 N N   . ILE A 207 ? 0.37675 0.31943 0.33908 0.02855  -0.01283 -0.08901 214 ILE A N   
1556 C CA  . ILE A 207 ? 0.32919 0.28013 0.31417 0.02966  -0.01517 -0.06957 214 ILE A CA  
1557 C C   . ILE A 207 ? 0.38156 0.32971 0.38026 0.04631  -0.00826 -0.06769 214 ILE A C   
1558 O O   . ILE A 207 ? 0.40366 0.36406 0.40262 0.05726  0.00060  -0.07576 214 ILE A O   
1559 C CB  . ILE A 207 ? 0.32970 0.31077 0.31740 0.02528  -0.01569 -0.05678 214 ILE A CB  
1560 C CG1 . ILE A 207 ? 0.32979 0.31513 0.31096 0.01071  -0.02662 -0.05561 214 ILE A CG1 
1561 C CG2 . ILE A 207 ? 0.35715 0.34892 0.36340 0.02860  -0.01426 -0.04108 214 ILE A CG2 
1562 C CD1 . ILE A 207 ? 0.37990 0.36039 0.37896 0.00012  -0.03441 -0.04723 214 ILE A CD1 
1563 N N   . GLY A 208 ? 0.38436 0.31831 0.39543 0.04759  -0.01284 -0.05568 215 GLY A N   
1564 C CA  . GLY A 208 ? 0.39450 0.32028 0.41784 0.06418  -0.01130 -0.05277 215 GLY A CA  
1565 C C   . GLY A 208 ? 0.39593 0.35031 0.42837 0.07079  -0.01022 -0.03994 215 GLY A C   
1566 O O   . GLY A 208 ? 0.42293 0.37225 0.46444 0.08050  -0.01457 -0.02979 215 GLY A O   
1567 N N   . TYR A 209 ? 0.33902 0.32106 0.36781 0.06510  -0.00624 -0.03997 216 TYR A N   
1568 C CA  . TYR A 209 ? 0.30012 0.30743 0.33561 0.06847  -0.00554 -0.03199 216 TYR A CA  
1569 C C   . TYR A 209 ? 0.35636 0.38524 0.39205 0.06794  0.00193  -0.04114 216 TYR A C   
1570 O O   . TYR A 209 ? 0.36435 0.39062 0.38841 0.06102  0.00528  -0.04773 216 TYR A O   
1571 C CB  . TYR A 209 ? 0.29450 0.30829 0.32506 0.05842  -0.00779 -0.01958 216 TYR A CB  
1572 C CG  . TYR A 209 ? 0.30696 0.30162 0.33530 0.05538  -0.01236 -0.00777 216 TYR A CG  
1573 C CD1 . TYR A 209 ? 0.35273 0.34411 0.38070 0.06273  -0.01694 0.00306  216 TYR A CD1 
1574 C CD2 . TYR A 209 ? 0.32589 0.30572 0.35248 0.04348  -0.01334 -0.00606 216 TYR A CD2 
1575 C CE1 . TYR A 209 ? 0.36582 0.33649 0.38810 0.05830  -0.02054 0.01762  216 TYR A CE1 
1576 C CE2 . TYR A 209 ? 0.33895 0.29995 0.36493 0.03740  -0.01606 0.00667  216 TYR A CE2 
1577 C CZ  . TYR A 209 ? 0.35775 0.31244 0.37978 0.04487  -0.01874 0.01955  216 TYR A CZ  
1578 O OH  . TYR A 209 ? 0.41075 0.34390 0.42837 0.03753  -0.02102 0.03616  216 TYR A OH  
1579 N N   . PRO A 210 ? 0.34689 0.39709 0.39473 0.07346  0.00359  -0.04061 217 PRO A N   
1580 C CA  . PRO A 210 ? 0.28787 0.35795 0.33770 0.06966  0.01217  -0.04700 217 PRO A CA  
1581 C C   . PRO A 210 ? 0.26738 0.33875 0.30540 0.05738  0.01208  -0.04128 217 PRO A C   
1582 O O   . PRO A 210 ? 0.34067 0.41314 0.37960 0.05458  0.00728  -0.03417 217 PRO A O   
1583 C CB  . PRO A 210 ? 0.29947 0.39295 0.37066 0.07593  0.01081  -0.04633 217 PRO A CB  
1584 C CG  . PRO A 210 ? 0.37596 0.46255 0.44738 0.07997  -0.00093 -0.03669 217 PRO A CG  
1585 C CD  . PRO A 210 ? 0.37704 0.43484 0.43702 0.08178  -0.00361 -0.03341 217 PRO A CD  
1586 N N   . ILE A 211 ? 0.28856 0.35916 0.31422 0.05115  0.01756  -0.04461 218 ILE A N   
1587 C CA  . ILE A 211 ? 0.26044 0.33065 0.27654 0.04167  0.01617  -0.03738 218 ILE A CA  
1588 C C   . ILE A 211 ? 0.26036 0.34419 0.27939 0.03689  0.02435  -0.03682 218 ILE A C   
1589 O O   . ILE A 211 ? 0.30297 0.39350 0.31525 0.03549  0.03361  -0.04216 218 ILE A O   
1590 C CB  . ILE A 211 ? 0.31008 0.36890 0.30674 0.03629  0.01276  -0.03778 218 ILE A CB  
1591 C CG1 . ILE A 211 ? 0.29257 0.33843 0.29065 0.03711  0.00458  -0.03852 218 ILE A CG1 
1592 C CG2 . ILE A 211 ? 0.29833 0.35793 0.28795 0.02912  0.00892  -0.02738 218 ILE A CG2 
1593 C CD1 . ILE A 211 ? 0.29673 0.33303 0.27718 0.02953  -0.00201 -0.04175 218 ILE A CD1 
1594 N N   . THR A 212 ? 0.28407 0.37131 0.31259 0.03318  0.02235  -0.03138 219 THR A N   
1595 C CA  . THR A 212 ? 0.25429 0.35097 0.28835 0.02490  0.02924  -0.02939 219 THR A CA  
1596 C C   . THR A 212 ? 0.25100 0.33261 0.27302 0.01734  0.02692  -0.01885 219 THR A C   
1597 O O   . THR A 212 ? 0.25882 0.32944 0.28432 0.01977  0.01963  -0.01556 219 THR A O   
1598 C CB  . THR A 212 ? 0.26586 0.37408 0.32065 0.02440  0.02669  -0.03266 219 THR A CB  
1599 O OG1 . THR A 212 ? 0.27885 0.40193 0.34678 0.03386  0.02530  -0.03941 219 THR A OG1 
1600 C CG2 . THR A 212 ? 0.25276 0.37036 0.31723 0.01165  0.03376  -0.03060 219 THR A CG2 
1601 N N   . LEU A 213 ? 0.27111 0.35249 0.27877 0.00924  0.03363  -0.01306 220 LEU A N   
1602 C CA  . LEU A 213 ? 0.26321 0.32814 0.25851 0.00221  0.02989  0.00114  220 LEU A CA  
1603 C C   . LEU A 213 ? 0.26273 0.32636 0.27137 -0.00809 0.03553  0.00562  220 LEU A C   
1604 O O   . LEU A 213 ? 0.31031 0.38759 0.31925 -0.01789 0.04739  0.00620  220 LEU A O   
1605 C CB  . LEU A 213 ? 0.30713 0.37024 0.27228 -0.00303 0.03237  0.00772  220 LEU A CB  
1606 C CG  . LEU A 213 ? 0.35764 0.40411 0.30636 -0.01148 0.02801  0.02723  220 LEU A CG  
1607 C CD1 . LEU A 213 ? 0.34601 0.37632 0.30781 -0.00299 0.01237  0.03407  220 LEU A CD1 
1608 C CD2 . LEU A 213 ? 0.38048 0.42746 0.29065 -0.01737 0.02870  0.03345  220 LEU A CD2 
1609 N N   . PHE A 214 ? 0.26405 0.31206 0.28536 -0.00660 0.02824  0.00708  221 PHE A N   
1610 C CA  . PHE A 214 ? 0.30980 0.34857 0.34345 -0.01834 0.03122  0.01005  221 PHE A CA  
1611 C C   . PHE A 214 ? 0.35737 0.37816 0.37528 -0.02940 0.03395  0.02916  221 PHE A C   
1612 O O   . PHE A 214 ? 0.36987 0.37854 0.36875 -0.02435 0.02765  0.04100  221 PHE A O   
1613 C CB  . PHE A 214 ? 0.27275 0.29294 0.31937 -0.01274 0.02310  0.00382  221 PHE A CB  
1614 C CG  . PHE A 214 ? 0.24986 0.28614 0.30778 -0.00627 0.02061  -0.01334 221 PHE A CG  
1615 C CD1 . PHE A 214 ? 0.23517 0.29304 0.29063 0.00190  0.02073  -0.01872 221 PHE A CD1 
1616 C CD2 . PHE A 214 ? 0.25763 0.28372 0.32574 -0.00913 0.01716  -0.02375 221 PHE A CD2 
1617 C CE1 . PHE A 214 ? 0.25366 0.32342 0.31578 0.00760  0.01649  -0.03000 221 PHE A CE1 
1618 C CE2 . PHE A 214 ? 0.29789 0.33877 0.36917 -0.00440 0.01316  -0.03786 221 PHE A CE2 
1619 C CZ  . PHE A 214 ? 0.26407 0.32722 0.33202 0.00404  0.01240  -0.03889 221 PHE A CZ  
1620 N N   . VAL A 215 ? 0.32725 0.34694 0.35333 -0.04611 0.04212  0.03391  222 VAL A N   
1621 C CA  . VAL A 215 ? 0.36778 0.36620 0.37742 -0.05958 0.04538  0.05590  222 VAL A CA  
1622 C C   . VAL A 215 ? 0.43379 0.39755 0.45949 -0.06610 0.03929  0.06064  222 VAL A C   
1623 O O   . VAL A 215 ? 0.37587 0.33841 0.42434 -0.06465 0.03594  0.04370  222 VAL A O   
1624 C CB  . VAL A 215 ? 0.55254 0.57526 0.55508 -0.07715 0.06323  0.06145  222 VAL A CB  
1625 C CG1 . VAL A 215 ? 0.55736 0.60302 0.53477 -0.06873 0.06898  0.05751  222 VAL A CG1 
1626 C CG2 . VAL A 215 ? 0.39942 0.44922 0.43544 -0.08542 0.07105  0.04591  222 VAL A CG2 
1627 N N   . GLU A 216 ? 0.50801 0.44022 0.51906 -0.07294 0.03665  0.08373  223 GLU A N   
1628 C CA  . GLU A 216 ? 0.60458 0.49339 0.62981 -0.07409 0.02845  0.08883  223 GLU A CA  
1629 C C   . GLU A 216 ? 0.68390 0.55785 0.71908 -0.10065 0.03720  0.09679  223 GLU A C   
1630 O O   . GLU A 216 ? 0.65268 0.54412 0.67657 -0.11942 0.05007  0.11006  223 GLU A O   
1631 C CB  . GLU A 216 ? 0.68187 0.53823 0.69143 -0.06209 0.01602  0.11118  223 GLU A CB  
1632 C CG  . GLU A 216 ? 0.68418 0.54222 0.70520 -0.03610 0.00453  0.09796  223 GLU A CG  
1633 C CD  . GLU A 216 ? 0.71710 0.53362 0.74588 -0.02329 -0.00842 0.11291  223 GLU A CD  
1634 O OE1 . GLU A 216 ? 0.81972 0.60542 0.87060 -0.02067 -0.00913 0.10292  223 GLU A OE1 
1635 O OE2 . GLU A 216 ? 0.87963 0.69432 0.89271 -0.01524 -0.01888 0.13374  223 GLU A OE2 
1636 N N   . LYS A 217 ? 0.75606 0.59725 0.81281 -0.10296 0.03106  0.08723  224 LYS A N   
1637 C CA  . LYS A 217 ? 0.75430 0.57422 0.82626 -0.12979 0.03620  0.09129  224 LYS A CA  
1638 C C   . LYS A 217 ? 0.77082 0.53612 0.83029 -0.13760 0.03260  0.12249  224 LYS A C   
1639 O O   . LYS A 217 ? 0.89441 0.66147 0.93662 -0.15689 0.04194  0.14867  224 LYS A O   
1640 C CB  . LYS A 217 ? 0.73726 0.54532 0.83510 -0.12906 0.02943  0.06171  224 LYS A CB  
1641 C CG  . LYS A 217 ? 0.70469 0.54726 0.80472 -0.10648 0.02502  0.03516  224 LYS A CG  
1642 C CD  . LYS A 217 ? 0.65952 0.50357 0.77873 -0.11289 0.02011  0.00557  224 LYS A CD  
1643 C CE  . LYS A 217 ? 0.53168 0.33853 0.64939 -0.09284 0.01174  -0.01108 224 LYS A CE  
1644 N NZ  . LYS A 217 ? 0.59318 0.41674 0.69853 -0.06412 0.01061  -0.01061 224 LYS A NZ  
# 
