data_7HBD
# 
_entry.id   7HBD 
# 
_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   7HBD         pdb_00007hbd 10.2210/pdb7hbd/pdb 
WWPDB D_1001407260 ?            ?                   
# 
_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                        7HBD 
_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-(3-chlorophenyl)-2-cyanoacetamide' 194.618   1   ?        ? ? ? 
3 water       nat water                                 18.015    303 ?        ? ? ? 
# 
_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-(3-chlorophenyl)-2-cyanoacetamide' A1AYX 
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 
A1AYX non-polymer         . 'N-(3-chlorophenyl)-2-cyanoacetamide' ? 'C9 H7 Cl N2 O'  194.618 
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        A1AYX 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1AYX 
_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 A1AYX 1   301 301 A1AYX BGI A . 
C 3 HOH   1   401 287 HOH   HOH A . 
C 3 HOH   2   402 131 HOH   HOH A . 
C 3 HOH   3   403 236 HOH   HOH A . 
C 3 HOH   4   404 173 HOH   HOH A . 
C 3 HOH   5   405 105 HOH   HOH A . 
C 3 HOH   6   406 34  HOH   HOH A . 
C 3 HOH   7   407 143 HOH   HOH A . 
C 3 HOH   8   408 161 HOH   HOH A . 
C 3 HOH   9   409 193 HOH   HOH A . 
C 3 HOH   10  410 292 HOH   HOH A . 
C 3 HOH   11  411 46  HOH   HOH A . 
C 3 HOH   12  412 256 HOH   HOH A . 
C 3 HOH   13  413 199 HOH   HOH A . 
C 3 HOH   14  414 30  HOH   HOH A . 
C 3 HOH   15  415 112 HOH   HOH A . 
C 3 HOH   16  416 141 HOH   HOH A . 
C 3 HOH   17  417 49  HOH   HOH A . 
C 3 HOH   18  418 114 HOH   HOH A . 
C 3 HOH   19  419 237 HOH   HOH A . 
C 3 HOH   20  420 224 HOH   HOH A . 
C 3 HOH   21  421 196 HOH   HOH A . 
C 3 HOH   22  422 33  HOH   HOH A . 
C 3 HOH   23  423 110 HOH   HOH A . 
C 3 HOH   24  424 302 HOH   HOH A . 
C 3 HOH   25  425 85  HOH   HOH A . 
C 3 HOH   26  426 271 HOH   HOH A . 
C 3 HOH   27  427 210 HOH   HOH A . 
C 3 HOH   28  428 104 HOH   HOH A . 
C 3 HOH   29  429 45  HOH   HOH A . 
C 3 HOH   30  430 130 HOH   HOH A . 
C 3 HOH   31  431 61  HOH   HOH A . 
C 3 HOH   32  432 109 HOH   HOH A . 
C 3 HOH   33  433 29  HOH   HOH A . 
C 3 HOH   34  434 124 HOH   HOH A . 
C 3 HOH   35  435 181 HOH   HOH A . 
C 3 HOH   36  436 63  HOH   HOH A . 
C 3 HOH   37  437 40  HOH   HOH A . 
C 3 HOH   38  438 171 HOH   HOH A . 
C 3 HOH   39  439 276 HOH   HOH A . 
C 3 HOH   40  440 178 HOH   HOH A . 
C 3 HOH   41  441 21  HOH   HOH A . 
C 3 HOH   42  442 25  HOH   HOH A . 
C 3 HOH   43  443 15  HOH   HOH A . 
C 3 HOH   44  444 16  HOH   HOH A . 
C 3 HOH   45  445 9   HOH   HOH A . 
C 3 HOH   46  446 152 HOH   HOH A . 
C 3 HOH   47  447 138 HOH   HOH A . 
C 3 HOH   48  448 43  HOH   HOH A . 
C 3 HOH   49  449 75  HOH   HOH A . 
C 3 HOH   50  450 17  HOH   HOH A . 
C 3 HOH   51  451 189 HOH   HOH A . 
C 3 HOH   52  452 303 HOH   HOH A . 
C 3 HOH   53  453 73  HOH   HOH A . 
C 3 HOH   54  454 11  HOH   HOH A . 
C 3 HOH   55  455 55  HOH   HOH A . 
C 3 HOH   56  456 69  HOH   HOH A . 
C 3 HOH   57  457 254 HOH   HOH A . 
C 3 HOH   58  458 54  HOH   HOH A . 
C 3 HOH   59  459 123 HOH   HOH A . 
C 3 HOH   60  460 48  HOH   HOH A . 
C 3 HOH   61  461 103 HOH   HOH A . 
C 3 HOH   62  462 195 HOH   HOH A . 
C 3 HOH   63  463 79  HOH   HOH A . 
C 3 HOH   64  464 26  HOH   HOH A . 
C 3 HOH   65  465 157 HOH   HOH A . 
C 3 HOH   66  466 7   HOH   HOH A . 
C 3 HOH   67  467 2   HOH   HOH A . 
C 3 HOH   68  468 116 HOH   HOH A . 
C 3 HOH   69  469 70  HOH   HOH A . 
C 3 HOH   70  470 163 HOH   HOH A . 
C 3 HOH   71  471 177 HOH   HOH A . 
C 3 HOH   72  472 180 HOH   HOH A . 
C 3 HOH   73  473 91  HOH   HOH A . 
C 3 HOH   74  474 24  HOH   HOH A . 
C 3 HOH   75  475 84  HOH   HOH A . 
C 3 HOH   76  476 88  HOH   HOH A . 
C 3 HOH   77  477 4   HOH   HOH A . 
C 3 HOH   78  478 264 HOH   HOH A . 
C 3 HOH   79  479 3   HOH   HOH A . 
C 3 HOH   80  480 211 HOH   HOH A . 
C 3 HOH   81  481 147 HOH   HOH A . 
C 3 HOH   82  482 64  HOH   HOH A . 
C 3 HOH   83  483 96  HOH   HOH A . 
C 3 HOH   84  484 8   HOH   HOH A . 
C 3 HOH   85  485 201 HOH   HOH A . 
C 3 HOH   86  486 22  HOH   HOH A . 
C 3 HOH   87  487 67  HOH   HOH A . 
C 3 HOH   88  488 270 HOH   HOH A . 
C 3 HOH   89  489 99  HOH   HOH A . 
C 3 HOH   90  490 44  HOH   HOH A . 
C 3 HOH   91  491 77  HOH   HOH A . 
C 3 HOH   92  492 32  HOH   HOH A . 
C 3 HOH   93  493 260 HOH   HOH A . 
C 3 HOH   94  494 47  HOH   HOH A . 
C 3 HOH   95  495 272 HOH   HOH A . 
C 3 HOH   96  496 18  HOH   HOH A . 
C 3 HOH   97  497 108 HOH   HOH A . 
C 3 HOH   98  498 299 HOH   HOH A . 
C 3 HOH   99  499 14  HOH   HOH A . 
C 3 HOH   100 500 74  HOH   HOH A . 
C 3 HOH   101 501 13  HOH   HOH A . 
C 3 HOH   102 502 59  HOH   HOH A . 
C 3 HOH   103 503 10  HOH   HOH A . 
C 3 HOH   104 504 53  HOH   HOH A . 
C 3 HOH   105 505 227 HOH   HOH A . 
C 3 HOH   106 506 78  HOH   HOH A . 
C 3 HOH   107 507 35  HOH   HOH A . 
C 3 HOH   108 508 115 HOH   HOH A . 
C 3 HOH   109 509 5   HOH   HOH A . 
C 3 HOH   110 510 50  HOH   HOH A . 
C 3 HOH   111 511 31  HOH   HOH A . 
C 3 HOH   112 512 275 HOH   HOH A . 
C 3 HOH   113 513 150 HOH   HOH A . 
C 3 HOH   114 514 118 HOH   HOH A . 
C 3 HOH   115 515 27  HOH   HOH A . 
C 3 HOH   116 516 267 HOH   HOH A . 
C 3 HOH   117 517 279 HOH   HOH A . 
C 3 HOH   118 518 57  HOH   HOH A . 
C 3 HOH   119 519 119 HOH   HOH A . 
C 3 HOH   120 520 111 HOH   HOH A . 
C 3 HOH   121 521 76  HOH   HOH A . 
C 3 HOH   122 522 82  HOH   HOH A . 
C 3 HOH   123 523 72  HOH   HOH A . 
C 3 HOH   124 524 172 HOH   HOH A . 
C 3 HOH   125 525 266 HOH   HOH A . 
C 3 HOH   126 526 222 HOH   HOH A . 
C 3 HOH   127 527 120 HOH   HOH A . 
C 3 HOH   128 528 90  HOH   HOH A . 
C 3 HOH   129 529 97  HOH   HOH A . 
C 3 HOH   130 530 101 HOH   HOH A . 
C 3 HOH   131 531 66  HOH   HOH A . 
C 3 HOH   132 532 137 HOH   HOH A . 
C 3 HOH   133 533 83  HOH   HOH A . 
C 3 HOH   134 534 229 HOH   HOH A . 
C 3 HOH   135 535 175 HOH   HOH A . 
C 3 HOH   136 536 92  HOH   HOH A . 
C 3 HOH   137 537 300 HOH   HOH A . 
C 3 HOH   138 538 20  HOH   HOH A . 
C 3 HOH   139 539 41  HOH   HOH A . 
C 3 HOH   140 540 135 HOH   HOH A . 
C 3 HOH   141 541 153 HOH   HOH A . 
C 3 HOH   142 542 60  HOH   HOH A . 
C 3 HOH   143 543 231 HOH   HOH A . 
C 3 HOH   144 544 168 HOH   HOH A . 
C 3 HOH   145 545 297 HOH   HOH A . 
C 3 HOH   146 546 39  HOH   HOH A . 
C 3 HOH   147 547 113 HOH   HOH A . 
C 3 HOH   148 548 174 HOH   HOH A . 
C 3 HOH   149 549 293 HOH   HOH A . 
C 3 HOH   150 550 166 HOH   HOH A . 
C 3 HOH   151 551 155 HOH   HOH A . 
C 3 HOH   152 552 23  HOH   HOH A . 
C 3 HOH   153 553 37  HOH   HOH A . 
C 3 HOH   154 554 117 HOH   HOH A . 
C 3 HOH   155 555 277 HOH   HOH A . 
C 3 HOH   156 556 182 HOH   HOH A . 
C 3 HOH   157 557 71  HOH   HOH A . 
C 3 HOH   158 558 58  HOH   HOH A . 
C 3 HOH   159 559 125 HOH   HOH A . 
C 3 HOH   160 560 295 HOH   HOH A . 
C 3 HOH   161 561 241 HOH   HOH A . 
C 3 HOH   162 562 243 HOH   HOH A . 
C 3 HOH   163 563 258 HOH   HOH A . 
C 3 HOH   164 564 19  HOH   HOH A . 
C 3 HOH   165 565 107 HOH   HOH A . 
C 3 HOH   166 566 146 HOH   HOH A . 
C 3 HOH   167 567 156 HOH   HOH A . 
C 3 HOH   168 568 98  HOH   HOH A . 
C 3 HOH   169 569 246 HOH   HOH A . 
C 3 HOH   170 570 100 HOH   HOH A . 
C 3 HOH   171 571 200 HOH   HOH A . 
C 3 HOH   172 572 209 HOH   HOH A . 
C 3 HOH   173 573 290 HOH   HOH A . 
C 3 HOH   174 574 205 HOH   HOH A . 
C 3 HOH   175 575 158 HOH   HOH A . 
C 3 HOH   176 576 202 HOH   HOH A . 
C 3 HOH   177 577 12  HOH   HOH A . 
C 3 HOH   178 578 86  HOH   HOH A . 
C 3 HOH   179 579 51  HOH   HOH A . 
C 3 HOH   180 580 38  HOH   HOH A . 
C 3 HOH   181 581 164 HOH   HOH A . 
C 3 HOH   182 582 133 HOH   HOH A . 
C 3 HOH   183 583 244 HOH   HOH A . 
C 3 HOH   184 584 36  HOH   HOH A . 
C 3 HOH   185 585 169 HOH   HOH A . 
C 3 HOH   186 586 274 HOH   HOH A . 
C 3 HOH   187 587 127 HOH   HOH A . 
C 3 HOH   188 588 52  HOH   HOH A . 
C 3 HOH   189 589 42  HOH   HOH A . 
C 3 HOH   190 590 228 HOH   HOH A . 
C 3 HOH   191 591 268 HOH   HOH A . 
C 3 HOH   192 592 93  HOH   HOH A . 
C 3 HOH   193 593 294 HOH   HOH A . 
C 3 HOH   194 594 278 HOH   HOH A . 
C 3 HOH   195 595 281 HOH   HOH A . 
C 3 HOH   196 596 142 HOH   HOH A . 
C 3 HOH   197 597 204 HOH   HOH A . 
C 3 HOH   198 598 129 HOH   HOH A . 
C 3 HOH   199 599 6   HOH   HOH A . 
C 3 HOH   200 600 183 HOH   HOH A . 
C 3 HOH   201 601 265 HOH   HOH A . 
C 3 HOH   202 602 126 HOH   HOH A . 
C 3 HOH   203 603 206 HOH   HOH A . 
C 3 HOH   204 604 1   HOH   HOH A . 
C 3 HOH   205 605 284 HOH   HOH A . 
C 3 HOH   206 606 192 HOH   HOH A . 
C 3 HOH   207 607 185 HOH   HOH A . 
C 3 HOH   208 608 213 HOH   HOH A . 
C 3 HOH   209 609 136 HOH   HOH A . 
C 3 HOH   210 610 56  HOH   HOH A . 
C 3 HOH   211 611 239 HOH   HOH A . 
C 3 HOH   212 612 301 HOH   HOH A . 
C 3 HOH   213 613 167 HOH   HOH A . 
C 3 HOH   214 614 221 HOH   HOH A . 
C 3 HOH   215 615 250 HOH   HOH A . 
C 3 HOH   216 616 122 HOH   HOH A . 
C 3 HOH   217 617 242 HOH   HOH A . 
C 3 HOH   218 618 288 HOH   HOH A . 
C 3 HOH   219 619 128 HOH   HOH A . 
C 3 HOH   220 620 149 HOH   HOH A . 
C 3 HOH   221 621 262 HOH   HOH A . 
C 3 HOH   222 622 151 HOH   HOH A . 
C 3 HOH   223 623 28  HOH   HOH A . 
C 3 HOH   224 624 165 HOH   HOH A . 
C 3 HOH   225 625 235 HOH   HOH A . 
C 3 HOH   226 626 252 HOH   HOH A . 
C 3 HOH   227 627 186 HOH   HOH A . 
C 3 HOH   228 628 215 HOH   HOH A . 
C 3 HOH   229 629 217 HOH   HOH A . 
C 3 HOH   230 630 162 HOH   HOH A . 
C 3 HOH   231 631 159 HOH   HOH A . 
C 3 HOH   232 632 176 HOH   HOH A . 
C 3 HOH   233 633 154 HOH   HOH A . 
C 3 HOH   234 634 240 HOH   HOH A . 
C 3 HOH   235 635 80  HOH   HOH A . 
C 3 HOH   236 636 191 HOH   HOH A . 
C 3 HOH   237 637 234 HOH   HOH A . 
C 3 HOH   238 638 184 HOH   HOH A . 
C 3 HOH   239 639 102 HOH   HOH A . 
C 3 HOH   240 640 94  HOH   HOH A . 
C 3 HOH   241 641 62  HOH   HOH A . 
C 3 HOH   242 642 190 HOH   HOH A . 
C 3 HOH   243 643 253 HOH   HOH A . 
C 3 HOH   244 644 289 HOH   HOH A . 
C 3 HOH   245 645 144 HOH   HOH A . 
C 3 HOH   246 646 280 HOH   HOH A . 
C 3 HOH   247 647 188 HOH   HOH A . 
C 3 HOH   248 648 282 HOH   HOH A . 
C 3 HOH   249 649 81  HOH   HOH A . 
C 3 HOH   250 650 68  HOH   HOH A . 
C 3 HOH   251 651 170 HOH   HOH A . 
C 3 HOH   252 652 212 HOH   HOH A . 
C 3 HOH   253 653 198 HOH   HOH A . 
C 3 HOH   254 654 106 HOH   HOH A . 
C 3 HOH   255 655 261 HOH   HOH A . 
C 3 HOH   256 656 187 HOH   HOH A . 
C 3 HOH   257 657 255 HOH   HOH A . 
C 3 HOH   258 658 214 HOH   HOH A . 
C 3 HOH   259 659 203 HOH   HOH A . 
C 3 HOH   260 660 219 HOH   HOH A . 
C 3 HOH   261 661 218 HOH   HOH A . 
C 3 HOH   262 662 65  HOH   HOH A . 
C 3 HOH   263 663 247 HOH   HOH A . 
C 3 HOH   264 664 283 HOH   HOH A . 
C 3 HOH   265 665 238 HOH   HOH A . 
C 3 HOH   266 666 89  HOH   HOH A . 
C 3 HOH   267 667 208 HOH   HOH A . 
C 3 HOH   268 668 95  HOH   HOH A . 
C 3 HOH   269 669 249 HOH   HOH A . 
C 3 HOH   270 670 296 HOH   HOH A . 
C 3 HOH   271 671 248 HOH   HOH A . 
C 3 HOH   272 672 179 HOH   HOH A . 
C 3 HOH   273 673 291 HOH   HOH A . 
C 3 HOH   274 674 269 HOH   HOH A . 
C 3 HOH   275 675 245 HOH   HOH A . 
C 3 HOH   276 676 160 HOH   HOH A . 
C 3 HOH   277 677 263 HOH   HOH A . 
C 3 HOH   278 678 194 HOH   HOH A . 
C 3 HOH   279 679 121 HOH   HOH A . 
C 3 HOH   280 680 197 HOH   HOH A . 
C 3 HOH   281 681 259 HOH   HOH A . 
C 3 HOH   282 682 145 HOH   HOH A . 
C 3 HOH   283 683 226 HOH   HOH A . 
C 3 HOH   284 684 230 HOH   HOH A . 
C 3 HOH   285 685 139 HOH   HOH A . 
C 3 HOH   286 686 216 HOH   HOH A . 
C 3 HOH   287 687 286 HOH   HOH A . 
C 3 HOH   288 688 87  HOH   HOH A . 
C 3 HOH   289 689 225 HOH   HOH A . 
C 3 HOH   290 690 134 HOH   HOH A . 
C 3 HOH   291 691 223 HOH   HOH A . 
C 3 HOH   292 692 140 HOH   HOH A . 
C 3 HOH   293 693 257 HOH   HOH A . 
C 3 HOH   294 694 132 HOH   HOH A . 
C 3 HOH   295 695 273 HOH   HOH A . 
C 3 HOH   296 696 220 HOH   HOH A . 
C 3 HOH   297 697 148 HOH   HOH A . 
C 3 HOH   298 698 207 HOH   HOH A . 
C 3 HOH   299 699 251 HOH   HOH A . 
C 3 HOH   300 700 232 HOH   HOH A . 
C 3 HOH   301 701 285 HOH   HOH A . 
C 3 HOH   302 702 298 HOH   HOH A . 
C 3 HOH   303 703 233 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             593647.099 
_cell.length_a           66.080 
_cell.length_b           89.560 
_cell.length_c           100.310 
_cell.angle_beta         90.000 
_cell.angle_gamma        90.000 
_cell.angle_alpha        90.000 
_cell.entry_id           7HBD 
_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                         7HBD 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
# 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
_exptl.entry_id          7HBD 
# 
_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   2023-07-19 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.pdbx_scattering_type             x-ray 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.monochromator                    Si111 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.97918 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.pdbx_synchrotron_beamline   BL10U2 
_diffrn_source.type                        'SSRF BEAMLINE BL10U2' 
_diffrn_source.pdbx_wavelength_list        0.97918 
_diffrn_source.pdbx_synchrotron_site       SSRF 
_diffrn_source.pdbx_wavelength             ? 
# 
_reflns.entry_id                     7HBD 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             36.490 
_reflns.d_resolution_high            1.800 
_reflns.number_obs                   27517 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         98.500 
_reflns.pdbx_Rmerge_I_obs            0.053 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        25.800 
_reflns.B_iso_Wilson_estimate        ? 
_reflns.pdbx_redundancy              9.800 
_reflns.pdbx_Rrim_I_all              0.055 
_reflns.pdbx_Rpim_I_all              0.017 
_reflns.pdbx_CC_half                 0.999 
_reflns.pdbx_netI_over_av_sigmaI     ? 
_reflns.pdbx_number_measured_all     268672 
_reflns.pdbx_scaling_rejects         153 
_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 1.800 1.850  ? 7035 1805 ? 0.315 ? ? ? 3.900 ? 3.600  ? ? ? ? ? ? 89.200 0.365 0.178 0.901 
1 2 8.050 36.490 ? 3445 359  ? 0.031 ? ? ? 9.600 ? 49.700 ? ? ? ? ? ? 98.500 0.032 0.010 0.999 
# 
_refine.entry_id                                 7HBD 
_refine.pdbx_method_to_determine_struct          'FOURIER SYNTHESIS' 
_refine.ls_percent_reflns_R_free                 4.90 
_refine.pdbx_overall_phase_error                 19.5408 
_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                          0.1676 
_refine.B_iso_mean                               29.44 
_refine.ls_number_reflns_R_free                  1347 
_refine.ls_percent_reflns_obs                    98.26 
_refine.ls_R_factor_R_work                       0.1663 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_refine.ls_d_res_high                            1.80 
_refine.ls_number_reflns_obs                     27486 
_refine.pdbx_ls_sigma_F                          1.34 
_refine.ls_number_reflns_R_work                  26139 
_refine.ls_d_res_low                             36.49 
_refine.pdbx_stereochemistry_target_values       'GeoStd + Monomer Library + CDL v1.2' 
_refine.ls_R_factor_R_free                       0.1916 
_refine.overall_SU_ML                            0.1819 
_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             303 
_refine_hist.number_atoms_total               1960 
_refine_hist.d_res_high                       1.80 
_refine_hist.d_res_low                        36.49 
# 
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           1939 0.0038 ? ? ? 
'X-RAY DIFFRACTION' f_angle_d          2619 0.6864 ? ? ? 
'X-RAY DIFFRACTION' f_chiral_restr     299  0.0457 ? ? ? 
'X-RAY DIFFRACTION' f_plane_restr      337  0.0051 ? ? ? 
'X-RAY DIFFRACTION' f_dihedral_angle_d 266  5.9911 ? ? ? 
# 
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' 1.80 1.86  2368 0.2240 89.78  0.2426 110 . . . . . 
'X-RAY DIFFRACTION' 1.86 1.94  2464 0.2395 94.19  0.3173 132 . . . . . 
'X-RAY DIFFRACTION' 1.94 2.03  2629 0.1906 99.64  0.2518 137 . . . . . 
'X-RAY DIFFRACTION' 2.03 2.13  2634 0.1703 99.96  0.1680 136 . . . . . 
'X-RAY DIFFRACTION' 2.13 2.27  2626 0.1859 99.32  0.2461 129 . . . . . 
'X-RAY DIFFRACTION' 2.27 2.44  2627 0.1679 100.00 0.1883 138 . . . . . 
'X-RAY DIFFRACTION' 2.44 2.69  2654 0.1739 100.00 0.1953 128 . . . . . 
'X-RAY DIFFRACTION' 2.69 3.08  2654 0.1714 99.96  0.1981 151 . . . . . 
'X-RAY DIFFRACTION' 3.08 3.88  2710 0.1490 99.93  0.1794 128 . . . . . 
'X-RAY DIFFRACTION' 3.88 36.49 2773 0.1463 99.59  0.1568 158 . . . . . 
# 
_struct.entry_id                  7HBD 
_struct.title                     'PanDDA analysis group deposition -- Crystal structure of HSP90N in complex with Fr12810' 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_details        ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HBD 
_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              7HBD 
_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 7HBD MET A 1   ? UNP P07900 ? ? 'initiating methionine' 8   1 
1 7HBD LEU A 230 ? UNP P07900 ? ? 'expression tag'        237 2 
1 7HBD GLU A 231 ? UNP P07900 ? ? 'expression tag'        238 3 
1 7HBD HIS A 232 ? UNP P07900 ? ? 'expression tag'        239 4 
1 7HBD HIS A 233 ? UNP P07900 ? ? 'expression tag'        240 5 
1 7HBD HIS A 234 ? UNP P07900 ? ? 'expression tag'        241 6 
1 7HBD HIS A 235 ? UNP P07900 ? ? 'expression tag'        242 7 
1 7HBD HIS A 236 ? UNP P07900 ? ? 'expression tag'        243 8 
1 7HBD HIS A 237 ? UNP P07900 ? ? 'expression tag'        244 9 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 GLN A 16  ? THR A 29  ? GLN A 23  THR A 36  1 ? 14 
HELX_P HELX_P2  AA2 GLU A 35  ? ASP A 59  ? GLU A 42  ASP A 66  1 ? 25 
HELX_P HELX_P3  AA3 PRO A 60  ? ASP A 64  ? PRO A 67  ASP A 71  5 ? 5  
HELX_P HELX_P4  AA4 THR A 92  ? ASN A 98  ? THR A 99  ASN A 105 1 ? 7  
HELX_P HELX_P5  AA5 ASN A 99  ? THR A 102 ? ASN A 106 THR A 109 5 ? 4  
HELX_P HELX_P6  AA6 ILE A 103 ? ALA A 117 ? ILE A 110 ALA A 124 1 ? 15 
HELX_P HELX_P7  AA7 ASP A 120 ? GLY A 128 ? ASP A 127 GLY A 135 5 ? 9  
HELX_P HELX_P8  AA8 VAL A 129 ? LEU A 136 ? VAL A 136 LEU A 143 5 ? 8  
HELX_P HELX_P9  AA9 GLU A 185 ? LEU A 191 ? GLU A 192 LEU A 198 5 ? 7  
HELX_P HELX_P10 AB1 GLU A 192 ? SER A 204 ? GLU A 199 SER A 211 1 ? 13 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
_struct_sheet.id               AA1 
_struct_sheet.type             ? 
_struct_sheet.number_strands   8 
_struct_sheet.details          ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA1 5 6 ? anti-parallel 
AA1 6 7 ? anti-parallel 
AA1 7 8 ? parallel      
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 VAL A 10  ? ALA A 14  ? VAL A 17  ALA A 21  
AA1 2 SER A 162 ? THR A 167 ? SER A 169 THR A 174 
AA1 3 TYR A 153 ? SER A 157 ? TYR A 160 SER A 164 
AA1 4 ALA A 138 ? LYS A 146 ? ALA A 145 LYS A 153 
AA1 5 GLY A 176 ? LEU A 183 ? GLY A 183 LEU A 190 
AA1 6 THR A 81  ? ASP A 86  ? THR A 88  ASP A 93  
AA1 7 ILE A 71  ? ASN A 76  ? ILE A 78  ASN A 83  
AA1 8 ILE A 211 ? LEU A 213 ? ILE A 218 LEU A 220 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N PHE A 13  ? N PHE A 20  O PHE A 163 ? O PHE A 170 
AA1 2 3 O ARG A 166 ? O ARG A 173 N ALA A 154 ? N ALA A 161 
AA1 3 4 O TRP A 155 ? O TRP A 162 N VAL A 143 ? N VAL A 150 
AA1 4 5 N THR A 142 ? N THR A 149 O ILE A 180 ? O ILE A 187 
AA1 5 6 O LEU A 181 ? O LEU A 188 N LEU A 82  ? N LEU A 89  
AA1 6 7 O THR A 83  ? O THR A 90  N ILE A 74  ? N ILE A 81  
AA1 7 8 N LEU A 73  ? N LEU A 80  O THR A 212 ? O THR A 219 
# 
_pdbx_entry_details.entry_id                   7HBD 
_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 517 ? ? O A HOH 664 ? ? 1.86 
2  1 O   A HOH 628 ? ? O A HOH 652 ? ? 1.94 
3  1 O   A HOH 573 ? ? O A HOH 670 ? ? 1.95 
4  1 O   A HOH 594 ? ? O A HOH 646 ? ? 2.05 
5  1 O   A HOH 545 ? ? O A HOH 612 ? ? 2.08 
6  1 O   A HOH 409 ? ? O A HOH 620 ? ? 2.10 
7  1 OD2 A ASP 127 ? B O A HOH 401 ? ? 2.12 
8  1 O   A HOH 626 ? ? O A HOH 643 ? ? 2.13 
9  1 O   A HOH 495 ? ? O A HOH 673 ? ? 2.15 
10 1 O   A HOH 472 ? ? O A HOH 543 ? ? 2.17 
11 1 O   A HOH 403 ? ? O A HOH 439 ? ? 2.18 
# 
loop_
_pdbx_validate_symm_contact.id 
_pdbx_validate_symm_contact.PDB_model_num 
_pdbx_validate_symm_contact.auth_atom_id_1 
_pdbx_validate_symm_contact.auth_asym_id_1 
_pdbx_validate_symm_contact.auth_comp_id_1 
_pdbx_validate_symm_contact.auth_seq_id_1 
_pdbx_validate_symm_contact.PDB_ins_code_1 
_pdbx_validate_symm_contact.label_alt_id_1 
_pdbx_validate_symm_contact.site_symmetry_1 
_pdbx_validate_symm_contact.auth_atom_id_2 
_pdbx_validate_symm_contact.auth_asym_id_2 
_pdbx_validate_symm_contact.auth_comp_id_2 
_pdbx_validate_symm_contact.auth_seq_id_2 
_pdbx_validate_symm_contact.PDB_ins_code_2 
_pdbx_validate_symm_contact.label_alt_id_2 
_pdbx_validate_symm_contact.site_symmetry_2 
_pdbx_validate_symm_contact.dist 
1 1 O A HOH 516 ? ? 1_555 O A HOH 621 ? ? 3_555 2.08 
2 1 O A HOH 489 ? ? 1_555 O A HOH 631 ? ? 2_555 2.09 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 TYR A 38  ? ? -161.07 107.74  
2 1 ALA A 166 ? ? 61.96   -144.01 
# 
_pdbx_struct_special_symmetry.id              1 
_pdbx_struct_special_symmetry.PDB_model_num   1 
_pdbx_struct_special_symmetry.auth_asym_id    A 
_pdbx_struct_special_symmetry.auth_comp_id    HOH 
_pdbx_struct_special_symmetry.auth_seq_id     677 
_pdbx_struct_special_symmetry.PDB_ins_code    ? 
_pdbx_struct_special_symmetry.label_asym_id   C 
_pdbx_struct_special_symmetry.label_comp_id   HOH 
_pdbx_struct_special_symmetry.label_seq_id    . 
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z               
2 x,-y,-z             
3 -x,y,-z             
4 -x,-y,z             
5 x+1/2,y+1/2,z+1/2   
6 x+1/2,-y+1/2,-z+1/2 
7 -x+1/2,y+1/2,-z+1/2 
8 -x+1/2,-y+1/2,z+1/2 
# 
loop_
_pdbx_refine_tls.id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][3] 
1 ? 'X-RAY DIFFRACTION' refined 13.1643657689  -17.1756803138 -18.3074673216 0.139145936388 0.186612489152 0.177570206827  
-0.00020302028189 -0.0287856738488  -0.0263656986667 2.93412647869 1.37108216897 6.03691008978 -0.83248286922  -3.62998560989  
-0.207929712941 0.117237465995   -0.32841917311  0.0130393303527 0.0507456531473 -0.106273695687  -0.108811594931 -0.0728940685926 
0.490335852922    -0.0457993228897 
2 ? 'X-RAY DIFFRACTION' refined -5.19639925023 -6.29381799919 -20.878880554  0.17407176783  0.159705680934 0.1966181572    
-0.00703641576012 -0.00588747664207 -0.0314118363873 2.23634730285 5.95542138548 9.01631837477 -2.6675579201   3.4340095841    
-6.12541697767  -0.0565106491504 0.0929990138719 0.138513345243  0.111860688272  -0.0805104672413 0.0313593294858 -0.329342925187  
0.24750496764     0.138537769306   
3 ? 'X-RAY DIFFRACTION' refined -10.0337766372 -14.9035210243 -25.1593585966 0.144500392379 0.160467243757 0.187911122159  
-0.00649050932113 -0.0499035568948  -0.0449502312381 1.4840862035  3.33284674413 4.66365270751 0.0132906078011 -0.564288301293 
-2.30188012468  0.0449515247545  0.138245993889  -0.104672627737 -0.227349304158 0.0907589838098  0.295157201003  0.0688067946514  
-0.309967978688   -0.166162729495  
4 ? 'X-RAY DIFFRACTION' refined 11.6821477214  -6.60422656207 -15.8300006308 0.198266605273 0.252043290191 0.264827753108  
-0.0600769607599  0.0202032629693   -0.0681428762071 2.21163983721 2.97519888308 5.58454700602 0.694727120314  -0.303168976396 
1.28574806909   0.225593368657   -0.359539142286 0.363895870612  0.222801229777  -0.097655696344  -0.116158279708 -0.404335636423  
0.59836267428     -0.0826439941163 
5 ? 'X-RAY DIFFRACTION' refined 0.907234666959 -19.2688685663 -28.1279664083 0.17596795952  0.14284972617  0.197172537609  
-0.00781342825854 -0.0136840791192  -0.0368628312972 3.14968484407 1.89126146782 2.49137636301 -1.36741445811  0.500329111191  
-0.571662058373 0.138701013366   0.270819875092  -0.295289754599 -0.181753352245 -0.0552505888287 0.163728953622  0.217096778061   
0.00714203116149  -0.0967491937718 
6 ? 'X-RAY DIFFRACTION' refined -5.31864372068 -20.4392536363 -10.2307603043 0.134279169062 0.161202435361 0.166250108143  
-0.0380946688505  -0.0216743142373  0.0106928624669  3.2832170498  3.97738555684 5.52746546691 -1.32348652686  -0.786618849177 
-0.76350895586  -0.13673503327   -0.371316557638 -0.229570298219 0.294918436381  0.101878921837   0.0560340401425 0.34116844777    
-0.00737300186555 0.0397899894121  
7 ? 'X-RAY DIFFRACTION' refined -13.9304505    -13.4218508619 -14.7388052249 0.134344024836 0.18276885331  0.0984687737952 
0.0105395787532   0.0013845389519   -0.0245280797837 6.05707136675 1.99514070237 5.20211083917 -0.480396893858 -0.253688581884 
-1.88454238964  0.0305350571666  -0.3469867082   0.0366622394549 0.526686126172  -0.0089224717451 0.0220665282979 -0.24149041414   
-0.093064025558   0.00823363875703 
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
1 1 'X-RAY DIFFRACTION' A 16  A 1   A 40  A 25  . 
;chain 'A' and (resid 16 through 40 )
;
2 2 'X-RAY DIFFRACTION' A 41  A 26  A 65  A 50  . 
;chain 'A' and (resid 41 through 65 )
;
3 3 'X-RAY DIFFRACTION' A 66  A 51  A 99  A 84  . 
;chain 'A' and (resid 66 through 99 )
;
4 4 'X-RAY DIFFRACTION' A 100 A 85  A 136 A 121 . 
;chain 'A' and (resid 100 through 136 )
;
5 5 'X-RAY DIFFRACTION' A 137 A 122 A 182 A 167 . 
;chain 'A' and (resid 137 through 182 )
;
6 6 'X-RAY DIFFRACTION' A 183 A 168 A 210 A 195 . 
;chain 'A' and (resid 183 through 210 )
;
7 7 'X-RAY DIFFRACTION' A 211 A 196 A 224 A 209 . 
;chain 'A' and (resid 211 through 224 )
;
# 
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 
A1AYX C1   C  Y N 1   
A1AYX C2   C  Y N 2   
A1AYX C3   C  Y N 3   
A1AYX C4   C  Y N 4   
A1AYX C5   C  Y N 5   
A1AYX C6   C  N N 6   
A1AYX C7   C  N N 7   
A1AYX C8   C  N N 8   
A1AYX C9   C  Y N 9   
A1AYX N1   N  N N 10  
A1AYX N2   N  N N 11  
A1AYX O1   O  N N 12  
A1AYX CL1  CL N N 13  
A1AYX H2   H  N N 14  
A1AYX H3   H  N N 15  
A1AYX H4   H  N N 16  
A1AYX H73  H  N N 17  
A1AYX H72  H  N N 18  
A1AYX H9   H  N N 19  
A1AYX H1   H  N N 20  
ALA   N    N  N N 21  
ALA   CA   C  N S 22  
ALA   C    C  N N 23  
ALA   O    O  N N 24  
ALA   CB   C  N N 25  
ALA   OXT  O  N N 26  
ALA   H    H  N N 27  
ALA   H2   H  N N 28  
ALA   HA   H  N N 29  
ALA   HB1  H  N N 30  
ALA   HB2  H  N N 31  
ALA   HB3  H  N N 32  
ALA   HXT  H  N N 33  
ARG   N    N  N N 34  
ARG   CA   C  N S 35  
ARG   C    C  N N 36  
ARG   O    O  N N 37  
ARG   CB   C  N N 38  
ARG   CG   C  N N 39  
ARG   CD   C  N N 40  
ARG   NE   N  N N 41  
ARG   CZ   C  N N 42  
ARG   NH1  N  N N 43  
ARG   NH2  N  N N 44  
ARG   OXT  O  N N 45  
ARG   H    H  N N 46  
ARG   H2   H  N N 47  
ARG   HA   H  N N 48  
ARG   HB2  H  N N 49  
ARG   HB3  H  N N 50  
ARG   HG2  H  N N 51  
ARG   HG3  H  N N 52  
ARG   HD2  H  N N 53  
ARG   HD3  H  N N 54  
ARG   HE   H  N N 55  
ARG   HH11 H  N N 56  
ARG   HH12 H  N N 57  
ARG   HH21 H  N N 58  
ARG   HH22 H  N N 59  
ARG   HXT  H  N N 60  
ASN   N    N  N N 61  
ASN   CA   C  N S 62  
ASN   C    C  N N 63  
ASN   O    O  N N 64  
ASN   CB   C  N N 65  
ASN   CG   C  N N 66  
ASN   OD1  O  N N 67  
ASN   ND2  N  N N 68  
ASN   OXT  O  N N 69  
ASN   H    H  N N 70  
ASN   H2   H  N N 71  
ASN   HA   H  N N 72  
ASN   HB2  H  N N 73  
ASN   HB3  H  N N 74  
ASN   HD21 H  N N 75  
ASN   HD22 H  N N 76  
ASN   HXT  H  N N 77  
ASP   N    N  N N 78  
ASP   CA   C  N S 79  
ASP   C    C  N N 80  
ASP   O    O  N N 81  
ASP   CB   C  N N 82  
ASP   CG   C  N N 83  
ASP   OD1  O  N N 84  
ASP   OD2  O  N N 85  
ASP   OXT  O  N N 86  
ASP   H    H  N N 87  
ASP   H2   H  N N 88  
ASP   HA   H  N N 89  
ASP   HB2  H  N N 90  
ASP   HB3  H  N N 91  
ASP   HD2  H  N N 92  
ASP   HXT  H  N N 93  
GLN   N    N  N N 94  
GLN   CA   C  N S 95  
GLN   C    C  N N 96  
GLN   O    O  N N 97  
GLN   CB   C  N N 98  
GLN   CG   C  N N 99  
GLN   CD   C  N N 100 
GLN   OE1  O  N N 101 
GLN   NE2  N  N N 102 
GLN   OXT  O  N N 103 
GLN   H    H  N N 104 
GLN   H2   H  N N 105 
GLN   HA   H  N N 106 
GLN   HB2  H  N N 107 
GLN   HB3  H  N N 108 
GLN   HG2  H  N N 109 
GLN   HG3  H  N N 110 
GLN   HE21 H  N N 111 
GLN   HE22 H  N N 112 
GLN   HXT  H  N N 113 
GLU   N    N  N N 114 
GLU   CA   C  N S 115 
GLU   C    C  N N 116 
GLU   O    O  N N 117 
GLU   CB   C  N N 118 
GLU   CG   C  N N 119 
GLU   CD   C  N N 120 
GLU   OE1  O  N N 121 
GLU   OE2  O  N N 122 
GLU   OXT  O  N N 123 
GLU   H    H  N N 124 
GLU   H2   H  N N 125 
GLU   HA   H  N N 126 
GLU   HB2  H  N N 127 
GLU   HB3  H  N N 128 
GLU   HG2  H  N N 129 
GLU   HG3  H  N N 130 
GLU   HE2  H  N N 131 
GLU   HXT  H  N N 132 
GLY   N    N  N N 133 
GLY   CA   C  N N 134 
GLY   C    C  N N 135 
GLY   O    O  N N 136 
GLY   OXT  O  N N 137 
GLY   H    H  N N 138 
GLY   H2   H  N N 139 
GLY   HA2  H  N N 140 
GLY   HA3  H  N N 141 
GLY   HXT  H  N N 142 
HIS   N    N  N N 143 
HIS   CA   C  N S 144 
HIS   C    C  N N 145 
HIS   O    O  N N 146 
HIS   CB   C  N N 147 
HIS   CG   C  Y N 148 
HIS   ND1  N  Y N 149 
HIS   CD2  C  Y N 150 
HIS   CE1  C  Y N 151 
HIS   NE2  N  Y N 152 
HIS   OXT  O  N N 153 
HIS   H    H  N N 154 
HIS   H2   H  N N 155 
HIS   HA   H  N N 156 
HIS   HB2  H  N N 157 
HIS   HB3  H  N N 158 
HIS   HD1  H  N N 159 
HIS   HD2  H  N N 160 
HIS   HE1  H  N N 161 
HIS   HE2  H  N N 162 
HIS   HXT  H  N N 163 
HOH   O    O  N N 164 
HOH   H1   H  N N 165 
HOH   H2   H  N N 166 
ILE   N    N  N N 167 
ILE   CA   C  N S 168 
ILE   C    C  N N 169 
ILE   O    O  N N 170 
ILE   CB   C  N S 171 
ILE   CG1  C  N N 172 
ILE   CG2  C  N N 173 
ILE   CD1  C  N N 174 
ILE   OXT  O  N N 175 
ILE   H    H  N N 176 
ILE   H2   H  N N 177 
ILE   HA   H  N N 178 
ILE   HB   H  N N 179 
ILE   HG12 H  N N 180 
ILE   HG13 H  N N 181 
ILE   HG21 H  N N 182 
ILE   HG22 H  N N 183 
ILE   HG23 H  N N 184 
ILE   HD11 H  N N 185 
ILE   HD12 H  N N 186 
ILE   HD13 H  N N 187 
ILE   HXT  H  N N 188 
LEU   N    N  N N 189 
LEU   CA   C  N S 190 
LEU   C    C  N N 191 
LEU   O    O  N N 192 
LEU   CB   C  N N 193 
LEU   CG   C  N N 194 
LEU   CD1  C  N N 195 
LEU   CD2  C  N N 196 
LEU   OXT  O  N N 197 
LEU   H    H  N N 198 
LEU   H2   H  N N 199 
LEU   HA   H  N N 200 
LEU   HB2  H  N N 201 
LEU   HB3  H  N N 202 
LEU   HG   H  N N 203 
LEU   HD11 H  N N 204 
LEU   HD12 H  N N 205 
LEU   HD13 H  N N 206 
LEU   HD21 H  N N 207 
LEU   HD22 H  N N 208 
LEU   HD23 H  N N 209 
LEU   HXT  H  N N 210 
LYS   N    N  N N 211 
LYS   CA   C  N S 212 
LYS   C    C  N N 213 
LYS   O    O  N N 214 
LYS   CB   C  N N 215 
LYS   CG   C  N N 216 
LYS   CD   C  N N 217 
LYS   CE   C  N N 218 
LYS   NZ   N  N N 219 
LYS   OXT  O  N N 220 
LYS   H    H  N N 221 
LYS   H2   H  N N 222 
LYS   HA   H  N N 223 
LYS   HB2  H  N N 224 
LYS   HB3  H  N N 225 
LYS   HG2  H  N N 226 
LYS   HG3  H  N N 227 
LYS   HD2  H  N N 228 
LYS   HD3  H  N N 229 
LYS   HE2  H  N N 230 
LYS   HE3  H  N N 231 
LYS   HZ1  H  N N 232 
LYS   HZ2  H  N N 233 
LYS   HZ3  H  N N 234 
LYS   HXT  H  N N 235 
MET   N    N  N N 236 
MET   CA   C  N S 237 
MET   C    C  N N 238 
MET   O    O  N N 239 
MET   CB   C  N N 240 
MET   CG   C  N N 241 
MET   SD   S  N N 242 
MET   CE   C  N N 243 
MET   OXT  O  N N 244 
MET   H    H  N N 245 
MET   H2   H  N N 246 
MET   HA   H  N N 247 
MET   HB2  H  N N 248 
MET   HB3  H  N N 249 
MET   HG2  H  N N 250 
MET   HG3  H  N N 251 
MET   HE1  H  N N 252 
MET   HE2  H  N N 253 
MET   HE3  H  N N 254 
MET   HXT  H  N N 255 
PHE   N    N  N N 256 
PHE   CA   C  N S 257 
PHE   C    C  N N 258 
PHE   O    O  N N 259 
PHE   CB   C  N N 260 
PHE   CG   C  Y N 261 
PHE   CD1  C  Y N 262 
PHE   CD2  C  Y N 263 
PHE   CE1  C  Y N 264 
PHE   CE2  C  Y N 265 
PHE   CZ   C  Y N 266 
PHE   OXT  O  N N 267 
PHE   H    H  N N 268 
PHE   H2   H  N N 269 
PHE   HA   H  N N 270 
PHE   HB2  H  N N 271 
PHE   HB3  H  N N 272 
PHE   HD1  H  N N 273 
PHE   HD2  H  N N 274 
PHE   HE1  H  N N 275 
PHE   HE2  H  N N 276 
PHE   HZ   H  N N 277 
PHE   HXT  H  N N 278 
PRO   N    N  N N 279 
PRO   CA   C  N S 280 
PRO   C    C  N N 281 
PRO   O    O  N N 282 
PRO   CB   C  N N 283 
PRO   CG   C  N N 284 
PRO   CD   C  N N 285 
PRO   OXT  O  N N 286 
PRO   H    H  N N 287 
PRO   HA   H  N N 288 
PRO   HB2  H  N N 289 
PRO   HB3  H  N N 290 
PRO   HG2  H  N N 291 
PRO   HG3  H  N N 292 
PRO   HD2  H  N N 293 
PRO   HD3  H  N N 294 
PRO   HXT  H  N N 295 
SER   N    N  N N 296 
SER   CA   C  N S 297 
SER   C    C  N N 298 
SER   O    O  N N 299 
SER   CB   C  N N 300 
SER   OG   O  N N 301 
SER   OXT  O  N N 302 
SER   H    H  N N 303 
SER   H2   H  N N 304 
SER   HA   H  N N 305 
SER   HB2  H  N N 306 
SER   HB3  H  N N 307 
SER   HG   H  N N 308 
SER   HXT  H  N N 309 
THR   N    N  N N 310 
THR   CA   C  N S 311 
THR   C    C  N N 312 
THR   O    O  N N 313 
THR   CB   C  N R 314 
THR   OG1  O  N N 315 
THR   CG2  C  N N 316 
THR   OXT  O  N N 317 
THR   H    H  N N 318 
THR   H2   H  N N 319 
THR   HA   H  N N 320 
THR   HB   H  N N 321 
THR   HG1  H  N N 322 
THR   HG21 H  N N 323 
THR   HG22 H  N N 324 
THR   HG23 H  N N 325 
THR   HXT  H  N N 326 
TRP   N    N  N N 327 
TRP   CA   C  N S 328 
TRP   C    C  N N 329 
TRP   O    O  N N 330 
TRP   CB   C  N N 331 
TRP   CG   C  Y N 332 
TRP   CD1  C  Y N 333 
TRP   CD2  C  Y N 334 
TRP   NE1  N  Y N 335 
TRP   CE2  C  Y N 336 
TRP   CE3  C  Y N 337 
TRP   CZ2  C  Y N 338 
TRP   CZ3  C  Y N 339 
TRP   CH2  C  Y N 340 
TRP   OXT  O  N N 341 
TRP   H    H  N N 342 
TRP   H2   H  N N 343 
TRP   HA   H  N N 344 
TRP   HB2  H  N N 345 
TRP   HB3  H  N N 346 
TRP   HD1  H  N N 347 
TRP   HE1  H  N N 348 
TRP   HE3  H  N N 349 
TRP   HZ2  H  N N 350 
TRP   HZ3  H  N N 351 
TRP   HH2  H  N N 352 
TRP   HXT  H  N N 353 
TYR   N    N  N N 354 
TYR   CA   C  N S 355 
TYR   C    C  N N 356 
TYR   O    O  N N 357 
TYR   CB   C  N N 358 
TYR   CG   C  Y N 359 
TYR   CD1  C  Y N 360 
TYR   CD2  C  Y N 361 
TYR   CE1  C  Y N 362 
TYR   CE2  C  Y N 363 
TYR   CZ   C  Y N 364 
TYR   OH   O  N N 365 
TYR   OXT  O  N N 366 
TYR   H    H  N N 367 
TYR   H2   H  N N 368 
TYR   HA   H  N N 369 
TYR   HB2  H  N N 370 
TYR   HB3  H  N N 371 
TYR   HD1  H  N N 372 
TYR   HD2  H  N N 373 
TYR   HE1  H  N N 374 
TYR   HE2  H  N N 375 
TYR   HH   H  N N 376 
TYR   HXT  H  N N 377 
VAL   N    N  N N 378 
VAL   CA   C  N S 379 
VAL   C    C  N N 380 
VAL   O    O  N N 381 
VAL   CB   C  N N 382 
VAL   CG1  C  N N 383 
VAL   CG2  C  N N 384 
VAL   OXT  O  N N 385 
VAL   H    H  N N 386 
VAL   H2   H  N N 387 
VAL   HA   H  N N 388 
VAL   HB   H  N N 389 
VAL   HG11 H  N N 390 
VAL   HG12 H  N N 391 
VAL   HG13 H  N N 392 
VAL   HG21 H  N N 393 
VAL   HG22 H  N N 394 
VAL   HG23 H  N N 395 
VAL   HXT  H  N N 396 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
A1AYX CL1 C1   sing N N 1   
A1AYX C1  C2   doub Y N 2   
A1AYX C1  C9   sing Y N 3   
A1AYX C2  C3   sing Y N 4   
A1AYX C3  C4   doub Y N 5   
A1AYX C4  C5   sing Y N 6   
A1AYX C5  N1   sing N N 7   
A1AYX C5  C9   doub Y N 8   
A1AYX N1  C6   sing N N 9   
A1AYX C6  O1   doub N N 10  
A1AYX C6  C7   sing N N 11  
A1AYX C7  C8   sing N N 12  
A1AYX C8  N2   trip N N 13  
A1AYX C2  H2   sing N N 14  
A1AYX C3  H3   sing N N 15  
A1AYX C4  H4   sing N N 16  
A1AYX C7  H73  sing N N 17  
A1AYX C7  H72  sing N N 18  
A1AYX C9  H9   sing N N 19  
A1AYX N1  H1   sing N N 20  
ALA   N   CA   sing N N 21  
ALA   N   H    sing N N 22  
ALA   N   H2   sing N N 23  
ALA   CA  C    sing N N 24  
ALA   CA  CB   sing N N 25  
ALA   CA  HA   sing N N 26  
ALA   C   O    doub N N 27  
ALA   C   OXT  sing N N 28  
ALA   CB  HB1  sing N N 29  
ALA   CB  HB2  sing N N 30  
ALA   CB  HB3  sing N N 31  
ALA   OXT HXT  sing N N 32  
ARG   N   CA   sing N N 33  
ARG   N   H    sing N N 34  
ARG   N   H2   sing N N 35  
ARG   CA  C    sing N N 36  
ARG   CA  CB   sing N N 37  
ARG   CA  HA   sing N N 38  
ARG   C   O    doub N N 39  
ARG   C   OXT  sing N N 40  
ARG   CB  CG   sing N N 41  
ARG   CB  HB2  sing N N 42  
ARG   CB  HB3  sing N N 43  
ARG   CG  CD   sing N N 44  
ARG   CG  HG2  sing N N 45  
ARG   CG  HG3  sing N N 46  
ARG   CD  NE   sing N N 47  
ARG   CD  HD2  sing N N 48  
ARG   CD  HD3  sing N N 49  
ARG   NE  CZ   sing N N 50  
ARG   NE  HE   sing N N 51  
ARG   CZ  NH1  sing N N 52  
ARG   CZ  NH2  doub N N 53  
ARG   NH1 HH11 sing N N 54  
ARG   NH1 HH12 sing N N 55  
ARG   NH2 HH21 sing N N 56  
ARG   NH2 HH22 sing N N 57  
ARG   OXT HXT  sing N N 58  
ASN   N   CA   sing N N 59  
ASN   N   H    sing N N 60  
ASN   N   H2   sing N N 61  
ASN   CA  C    sing N N 62  
ASN   CA  CB   sing N N 63  
ASN   CA  HA   sing N N 64  
ASN   C   O    doub N N 65  
ASN   C   OXT  sing N N 66  
ASN   CB  CG   sing N N 67  
ASN   CB  HB2  sing N N 68  
ASN   CB  HB3  sing N N 69  
ASN   CG  OD1  doub N N 70  
ASN   CG  ND2  sing N N 71  
ASN   ND2 HD21 sing N N 72  
ASN   ND2 HD22 sing N N 73  
ASN   OXT HXT  sing N N 74  
ASP   N   CA   sing N N 75  
ASP   N   H    sing N N 76  
ASP   N   H2   sing N N 77  
ASP   CA  C    sing N N 78  
ASP   CA  CB   sing N N 79  
ASP   CA  HA   sing N N 80  
ASP   C   O    doub N N 81  
ASP   C   OXT  sing N N 82  
ASP   CB  CG   sing N N 83  
ASP   CB  HB2  sing N N 84  
ASP   CB  HB3  sing N N 85  
ASP   CG  OD1  doub N N 86  
ASP   CG  OD2  sing N N 87  
ASP   OD2 HD2  sing N N 88  
ASP   OXT HXT  sing N N 89  
GLN   N   CA   sing N N 90  
GLN   N   H    sing N N 91  
GLN   N   H2   sing N N 92  
GLN   CA  C    sing N N 93  
GLN   CA  CB   sing N N 94  
GLN   CA  HA   sing N N 95  
GLN   C   O    doub N N 96  
GLN   C   OXT  sing N N 97  
GLN   CB  CG   sing N N 98  
GLN   CB  HB2  sing N N 99  
GLN   CB  HB3  sing N N 100 
GLN   CG  CD   sing N N 101 
GLN   CG  HG2  sing N N 102 
GLN   CG  HG3  sing N N 103 
GLN   CD  OE1  doub N N 104 
GLN   CD  NE2  sing N N 105 
GLN   NE2 HE21 sing N N 106 
GLN   NE2 HE22 sing N N 107 
GLN   OXT HXT  sing N N 108 
GLU   N   CA   sing N N 109 
GLU   N   H    sing N N 110 
GLU   N   H2   sing N N 111 
GLU   CA  C    sing N N 112 
GLU   CA  CB   sing N N 113 
GLU   CA  HA   sing N N 114 
GLU   C   O    doub N N 115 
GLU   C   OXT  sing N N 116 
GLU   CB  CG   sing N N 117 
GLU   CB  HB2  sing N N 118 
GLU   CB  HB3  sing N N 119 
GLU   CG  CD   sing N N 120 
GLU   CG  HG2  sing N N 121 
GLU   CG  HG3  sing N N 122 
GLU   CD  OE1  doub N N 123 
GLU   CD  OE2  sing N N 124 
GLU   OE2 HE2  sing N N 125 
GLU   OXT HXT  sing N N 126 
GLY   N   CA   sing N N 127 
GLY   N   H    sing N N 128 
GLY   N   H2   sing N N 129 
GLY   CA  C    sing N N 130 
GLY   CA  HA2  sing N N 131 
GLY   CA  HA3  sing N N 132 
GLY   C   O    doub N N 133 
GLY   C   OXT  sing N N 134 
GLY   OXT HXT  sing N N 135 
HIS   N   CA   sing N N 136 
HIS   N   H    sing N N 137 
HIS   N   H2   sing N N 138 
HIS   CA  C    sing N N 139 
HIS   CA  CB   sing N N 140 
HIS   CA  HA   sing N N 141 
HIS   C   O    doub N N 142 
HIS   C   OXT  sing N N 143 
HIS   CB  CG   sing N N 144 
HIS   CB  HB2  sing N N 145 
HIS   CB  HB3  sing N N 146 
HIS   CG  ND1  sing Y N 147 
HIS   CG  CD2  doub Y N 148 
HIS   ND1 CE1  doub Y N 149 
HIS   ND1 HD1  sing N N 150 
HIS   CD2 NE2  sing Y N 151 
HIS   CD2 HD2  sing N N 152 
HIS   CE1 NE2  sing Y N 153 
HIS   CE1 HE1  sing N N 154 
HIS   NE2 HE2  sing N N 155 
HIS   OXT HXT  sing N N 156 
HOH   O   H1   sing N N 157 
HOH   O   H2   sing N N 158 
ILE   N   CA   sing N N 159 
ILE   N   H    sing N N 160 
ILE   N   H2   sing N N 161 
ILE   CA  C    sing N N 162 
ILE   CA  CB   sing N N 163 
ILE   CA  HA   sing N N 164 
ILE   C   O    doub N N 165 
ILE   C   OXT  sing N N 166 
ILE   CB  CG1  sing N N 167 
ILE   CB  CG2  sing N N 168 
ILE   CB  HB   sing N N 169 
ILE   CG1 CD1  sing N N 170 
ILE   CG1 HG12 sing N N 171 
ILE   CG1 HG13 sing N N 172 
ILE   CG2 HG21 sing N N 173 
ILE   CG2 HG22 sing N N 174 
ILE   CG2 HG23 sing N N 175 
ILE   CD1 HD11 sing N N 176 
ILE   CD1 HD12 sing N N 177 
ILE   CD1 HD13 sing N N 178 
ILE   OXT HXT  sing N N 179 
LEU   N   CA   sing N N 180 
LEU   N   H    sing N N 181 
LEU   N   H2   sing N N 182 
LEU   CA  C    sing N N 183 
LEU   CA  CB   sing N N 184 
LEU   CA  HA   sing N N 185 
LEU   C   O    doub N N 186 
LEU   C   OXT  sing N N 187 
LEU   CB  CG   sing N N 188 
LEU   CB  HB2  sing N N 189 
LEU   CB  HB3  sing N N 190 
LEU   CG  CD1  sing N N 191 
LEU   CG  CD2  sing N N 192 
LEU   CG  HG   sing N N 193 
LEU   CD1 HD11 sing N N 194 
LEU   CD1 HD12 sing N N 195 
LEU   CD1 HD13 sing N N 196 
LEU   CD2 HD21 sing N N 197 
LEU   CD2 HD22 sing N N 198 
LEU   CD2 HD23 sing N N 199 
LEU   OXT HXT  sing N N 200 
LYS   N   CA   sing N N 201 
LYS   N   H    sing N N 202 
LYS   N   H2   sing N N 203 
LYS   CA  C    sing N N 204 
LYS   CA  CB   sing N N 205 
LYS   CA  HA   sing N N 206 
LYS   C   O    doub N N 207 
LYS   C   OXT  sing N N 208 
LYS   CB  CG   sing N N 209 
LYS   CB  HB2  sing N N 210 
LYS   CB  HB3  sing N N 211 
LYS   CG  CD   sing N N 212 
LYS   CG  HG2  sing N N 213 
LYS   CG  HG3  sing N N 214 
LYS   CD  CE   sing N N 215 
LYS   CD  HD2  sing N N 216 
LYS   CD  HD3  sing N N 217 
LYS   CE  NZ   sing N N 218 
LYS   CE  HE2  sing N N 219 
LYS   CE  HE3  sing N N 220 
LYS   NZ  HZ1  sing N N 221 
LYS   NZ  HZ2  sing N N 222 
LYS   NZ  HZ3  sing N N 223 
LYS   OXT HXT  sing N N 224 
MET   N   CA   sing N N 225 
MET   N   H    sing N N 226 
MET   N   H2   sing N N 227 
MET   CA  C    sing N N 228 
MET   CA  CB   sing N N 229 
MET   CA  HA   sing N N 230 
MET   C   O    doub N N 231 
MET   C   OXT  sing N N 232 
MET   CB  CG   sing N N 233 
MET   CB  HB2  sing N N 234 
MET   CB  HB3  sing N N 235 
MET   CG  SD   sing N N 236 
MET   CG  HG2  sing N N 237 
MET   CG  HG3  sing N N 238 
MET   SD  CE   sing N N 239 
MET   CE  HE1  sing N N 240 
MET   CE  HE2  sing N N 241 
MET   CE  HE3  sing N N 242 
MET   OXT HXT  sing N N 243 
PHE   N   CA   sing N N 244 
PHE   N   H    sing N N 245 
PHE   N   H2   sing N N 246 
PHE   CA  C    sing N N 247 
PHE   CA  CB   sing N N 248 
PHE   CA  HA   sing N N 249 
PHE   C   O    doub N N 250 
PHE   C   OXT  sing N N 251 
PHE   CB  CG   sing N N 252 
PHE   CB  HB2  sing N N 253 
PHE   CB  HB3  sing N N 254 
PHE   CG  CD1  doub Y N 255 
PHE   CG  CD2  sing Y N 256 
PHE   CD1 CE1  sing Y N 257 
PHE   CD1 HD1  sing N N 258 
PHE   CD2 CE2  doub Y N 259 
PHE   CD2 HD2  sing N N 260 
PHE   CE1 CZ   doub Y N 261 
PHE   CE1 HE1  sing N N 262 
PHE   CE2 CZ   sing Y N 263 
PHE   CE2 HE2  sing N N 264 
PHE   CZ  HZ   sing N N 265 
PHE   OXT HXT  sing N N 266 
PRO   N   CA   sing N N 267 
PRO   N   CD   sing N N 268 
PRO   N   H    sing N N 269 
PRO   CA  C    sing N N 270 
PRO   CA  CB   sing N N 271 
PRO   CA  HA   sing N N 272 
PRO   C   O    doub N N 273 
PRO   C   OXT  sing N N 274 
PRO   CB  CG   sing N N 275 
PRO   CB  HB2  sing N N 276 
PRO   CB  HB3  sing N N 277 
PRO   CG  CD   sing N N 278 
PRO   CG  HG2  sing N N 279 
PRO   CG  HG3  sing N N 280 
PRO   CD  HD2  sing N N 281 
PRO   CD  HD3  sing N N 282 
PRO   OXT HXT  sing N N 283 
SER   N   CA   sing N N 284 
SER   N   H    sing N N 285 
SER   N   H2   sing N N 286 
SER   CA  C    sing N N 287 
SER   CA  CB   sing N N 288 
SER   CA  HA   sing N N 289 
SER   C   O    doub N N 290 
SER   C   OXT  sing N N 291 
SER   CB  OG   sing N N 292 
SER   CB  HB2  sing N N 293 
SER   CB  HB3  sing N N 294 
SER   OG  HG   sing N N 295 
SER   OXT HXT  sing N N 296 
THR   N   CA   sing N N 297 
THR   N   H    sing N N 298 
THR   N   H2   sing N N 299 
THR   CA  C    sing N N 300 
THR   CA  CB   sing N N 301 
THR   CA  HA   sing N N 302 
THR   C   O    doub N N 303 
THR   C   OXT  sing N N 304 
THR   CB  OG1  sing N N 305 
THR   CB  CG2  sing N N 306 
THR   CB  HB   sing N N 307 
THR   OG1 HG1  sing N N 308 
THR   CG2 HG21 sing N N 309 
THR   CG2 HG22 sing N N 310 
THR   CG2 HG23 sing N N 311 
THR   OXT HXT  sing N N 312 
TRP   N   CA   sing N N 313 
TRP   N   H    sing N N 314 
TRP   N   H2   sing N N 315 
TRP   CA  C    sing N N 316 
TRP   CA  CB   sing N N 317 
TRP   CA  HA   sing N N 318 
TRP   C   O    doub N N 319 
TRP   C   OXT  sing N N 320 
TRP   CB  CG   sing N N 321 
TRP   CB  HB2  sing N N 322 
TRP   CB  HB3  sing N N 323 
TRP   CG  CD1  doub Y N 324 
TRP   CG  CD2  sing Y N 325 
TRP   CD1 NE1  sing Y N 326 
TRP   CD1 HD1  sing N N 327 
TRP   CD2 CE2  doub Y N 328 
TRP   CD2 CE3  sing Y N 329 
TRP   NE1 CE2  sing Y N 330 
TRP   NE1 HE1  sing N N 331 
TRP   CE2 CZ2  sing Y N 332 
TRP   CE3 CZ3  doub Y N 333 
TRP   CE3 HE3  sing N N 334 
TRP   CZ2 CH2  doub Y N 335 
TRP   CZ2 HZ2  sing N N 336 
TRP   CZ3 CH2  sing Y N 337 
TRP   CZ3 HZ3  sing N N 338 
TRP   CH2 HH2  sing N N 339 
TRP   OXT HXT  sing N N 340 
TYR   N   CA   sing N N 341 
TYR   N   H    sing N N 342 
TYR   N   H2   sing N N 343 
TYR   CA  C    sing N N 344 
TYR   CA  CB   sing N N 345 
TYR   CA  HA   sing N N 346 
TYR   C   O    doub N N 347 
TYR   C   OXT  sing N N 348 
TYR   CB  CG   sing N N 349 
TYR   CB  HB2  sing N N 350 
TYR   CB  HB3  sing N N 351 
TYR   CG  CD1  doub Y N 352 
TYR   CG  CD2  sing Y N 353 
TYR   CD1 CE1  sing Y N 354 
TYR   CD1 HD1  sing N N 355 
TYR   CD2 CE2  doub Y N 356 
TYR   CD2 HD2  sing N N 357 
TYR   CE1 CZ   doub Y N 358 
TYR   CE1 HE1  sing N N 359 
TYR   CE2 CZ   sing Y N 360 
TYR   CE2 HE2  sing N N 361 
TYR   CZ  OH   sing N N 362 
TYR   OH  HH   sing N N 363 
TYR   OXT HXT  sing N N 364 
VAL   N   CA   sing N N 365 
VAL   N   H    sing N N 366 
VAL   N   H2   sing N N 367 
VAL   CA  C    sing N N 368 
VAL   CA  CB   sing N N 369 
VAL   CA  HA   sing N N 370 
VAL   C   O    doub N N 371 
VAL   C   OXT  sing N N 372 
VAL   CB  CG1  sing N N 373 
VAL   CB  CG2  sing N N 374 
VAL   CB  HB   sing N N 375 
VAL   CG1 HG11 sing N N 376 
VAL   CG1 HG12 sing N N 377 
VAL   CG1 HG13 sing N N 378 
VAL   CG2 HG21 sing N N 379 
VAL   CG2 HG22 sing N N 380 
VAL   CG2 HG23 sing N N 381 
VAL   OXT HXT  sing N N 382 
# 
_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                    7HBD 
_atom_sites.fract_transf_matrix[1][1]   0.015133 
_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]   0.011166 
_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]   0.009969 
_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   ? 4.40155   -28.65377 -39.03807 1.000 49.84343 ? 16  GLU   A N   1 
ATOM   2    C  CA  . GLU   A 1 9   ? 5.67662   -27.95860 -39.15372 1.000 62.47359 ? 16  GLU   A CA  1 
ATOM   3    C  C   . GLU   A 1 9   ? 5.84394   -27.05926 -37.93049 1.000 61.38716 ? 16  GLU   A C   1 
ATOM   4    O  O   . GLU   A 1 9   ? 5.05016   -26.14684 -37.70023 1.000 51.16408 ? 16  GLU   A O   1 
ATOM   5    C  CB  . GLU   A 1 9   ? 5.71981   -27.16300 -40.46451 1.000 61.13176 ? 16  GLU   A CB  1 
ATOM   6    C  CG  . GLU   A 1 9   ? 7.11869   -26.87992 -41.06630 1.000 74.32427 ? 16  GLU   A CG  1 
ATOM   7    C  CD  . GLU   A 1 9   ? 7.98917   -25.87090 -40.31288 1.000 82.60904 ? 16  GLU   A CD  1 
ATOM   8    O  OE1 . GLU   A 1 9   ? 7.62421   -25.43161 -39.21784 1.000 78.20794 ? 16  GLU   A OE1 1 
ATOM   9    O  OE2 . GLU   A 1 9   ? 9.08005   -25.51828 -40.84395 1.000 67.41444 ? 16  GLU   A OE2 1 
ATOM   10   N  N   . VAL   A 1 10  ? 6.89110   -27.32521 -37.15270 1.000 36.01846 ? 17  VAL   A N   1 
ATOM   11   C  CA  . VAL   A 1 10  ? 7.15112   -26.64112 -35.89089 1.000 31.56565 ? 17  VAL   A CA  1 
ATOM   12   C  C   . VAL   A 1 10  ? 8.50685   -25.95605 -35.96145 1.000 32.40246 ? 17  VAL   A C   1 
ATOM   13   O  O   . VAL   A 1 10  ? 9.51052   -26.58783 -36.30894 1.000 33.39672 ? 17  VAL   A O   1 
ATOM   14   C  CB  . VAL   A 1 10  ? 7.11321   -27.61291 -34.70037 1.000 37.17059 ? 17  VAL   A CB  1 
ATOM   15   C  CG1 . VAL   A 1 10  ? 7.09755   -26.83999 -33.40562 1.000 38.10561 ? 17  VAL   A CG1 1 
ATOM   16   C  CG2 . VAL   A 1 10  ? 5.89880   -28.52307 -34.79999 1.000 53.53365 ? 17  VAL   A CG2 1 
ATOM   17   N  N   . GLU   A 1 11  ? 8.53950   -24.67584 -35.60319 1.000 25.88332 ? 18  GLU   A N   1 
ATOM   18   C  CA  . GLU   A 1 11  ? 9.77379   -23.90357 -35.56029 1.000 26.55634 ? 18  GLU   A CA  1 
ATOM   19   C  C   . GLU   A 1 11  ? 10.21092  -23.75458 -34.10898 1.000 24.58779 ? 18  GLU   A C   1 
ATOM   20   O  O   . GLU   A 1 11  ? 9.39860   -23.40558 -33.24877 1.000 21.32148 ? 18  GLU   A O   1 
ATOM   21   C  CB  . GLU   A 1 11  ? 9.57128   -22.53223 -36.20498 1.000 23.42430 ? 18  GLU   A CB  1 
ATOM   22   C  CG  . GLU   A 1 11  ? 9.40063   -22.59430 -37.71855 1.000 25.42567 ? 18  GLU   A CG  1 
ATOM   23   C  CD  . GLU   A 1 11  ? 9.26227   -21.22462 -38.35471 1.000 37.96860 ? 18  GLU   A CD  1 
ATOM   24   O  OE1 . GLU   A 1 11  ? 8.23704   -20.56008 -38.10398 1.000 38.41574 ? 18  GLU   A OE1 1 
ATOM   25   O  OE2 . GLU   A 1 11  ? 10.15640  -20.81945 -39.12359 1.000 43.37234 ? 18  GLU   A OE2 1 
ATOM   26   N  N   . THR   A 1 12  ? 11.48562  -24.03016 -33.83724 1.000 20.87530 ? 19  THR   A N   1 
ATOM   27   C  CA  . THR   A 1 12  ? 12.04004  -23.93268 -32.49422 1.000 19.41423 ? 19  THR   A CA  1 
ATOM   28   C  C   . THR   A 1 12  ? 13.03194  -22.77817 -32.44521 1.000 20.27887 ? 19  THR   A C   1 
ATOM   29   O  O   . THR   A 1 12  ? 13.91901  -22.68044 -33.29969 1.000 19.07683 ? 19  THR   A O   1 
ATOM   30   C  CB  . THR   A 1 12  ? 12.72956  -25.23828 -32.08597 1.000 22.37020 ? 19  THR   A CB  1 
ATOM   31   O  OG1 . THR   A 1 12  ? 11.80577  -26.32175 -32.21441 1.000 22.87199 ? 19  THR   A OG1 1 
ATOM   32   C  CG2 . THR   A 1 12  ? 13.19410  -25.16145 -30.63734 1.000 22.64664 ? 19  THR   A CG2 1 
ATOM   33   N  N   . PHE   A 1 13  ? 12.87576  -21.91678 -31.44559 1.000 18.06704 ? 20  PHE   A N   1 
ATOM   34   C  CA  . PHE   A 1 13  ? 13.66469  -20.70548 -31.27515 1.000 19.77871 ? 20  PHE   A CA  1 
ATOM   35   C  C   . PHE   A 1 13  ? 14.34100  -20.71897 -29.91334 1.000 23.29079 ? 20  PHE   A C   1 
ATOM   36   O  O   . PHE   A 1 13  ? 13.78549  -21.23246 -28.93961 1.000 20.08097 ? 20  PHE   A O   1 
ATOM   37   C  CB  . PHE   A 1 13  ? 12.78349  -19.45319 -31.33830 1.000 18.36139 ? 20  PHE   A CB  1 
ATOM   38   C  CG  . PHE   A 1 13  ? 12.05546  -19.27354 -32.63639 1.000 18.64694 ? 20  PHE   A CG  1 
ATOM   39   C  CD1 . PHE   A 1 13  ? 10.82736  -19.88183 -32.84630 1.000 23.16533 ? 20  PHE   A CD1 1 
ATOM   40   C  CD2 . PHE   A 1 13  ? 12.58223  -18.46543 -33.63554 1.000 21.89688 ? 20  PHE   A CD2 1 
ATOM   41   C  CE1 . PHE   A 1 13  ? 10.14677  -19.71141 -34.04065 1.000 22.17665 ? 20  PHE   A CE1 1 
ATOM   42   C  CE2 . PHE   A 1 13  ? 11.90145  -18.28326 -34.82969 1.000 24.15259 ? 20  PHE   A CE2 1 
ATOM   43   C  CZ  . PHE   A 1 13  ? 10.68538  -18.90985 -35.03249 1.000 23.39562 ? 20  PHE   A CZ  1 
ATOM   44   N  N   . ALA   A 1 14  ? 15.52514  -20.11434 -29.83573 1.000 18.87828 ? 21  ALA   A N   1 
ATOM   45   C  CA  . ALA   A 1 14  ? 16.16279  -19.85110 -28.55334 1.000 15.42940 ? 21  ALA   A CA  1 
ATOM   46   C  C   . ALA   A 1 14  ? 15.66318  -18.53118 -27.97760 1.000 18.04843 ? 21  ALA   A C   1 
ATOM   47   O  O   . ALA   A 1 14  ? 15.56193  -17.53142 -28.69388 1.000 17.83364 ? 21  ALA   A O   1 
ATOM   48   C  CB  . ALA   A 1 14  ? 17.68731  -19.80096 -28.70791 1.000 17.62367 ? 21  ALA   A CB  1 
ATOM   49   N  N   . PHE   A 1 15  ? 15.34113  -18.52847 -26.68286 1.000 18.14418 ? 22  PHE   A N   1 
ATOM   50   C  CA  . PHE   A 1 15  ? 15.12023  -17.25657 -26.00253 1.000 18.24731 ? 22  PHE   A CA  1 
ATOM   51   C  C   . PHE   A 1 15  ? 16.39146  -16.42007 -26.04024 1.000 19.82130 ? 22  PHE   A C   1 
ATOM   52   O  O   . PHE   A 1 15  ? 17.50796  -16.94514 -25.96087 1.000 19.83187 ? 22  PHE   A O   1 
ATOM   53   C  CB  . PHE   A 1 15  ? 14.72349  -17.45595 -24.53392 1.000 16.52138 ? 22  PHE   A CB  1 
ATOM   54   C  CG  . PHE   A 1 15  ? 13.32910  -17.97676 -24.33035 1.000 16.81105 ? 22  PHE   A CG  1 
ATOM   55   C  CD1 . PHE   A 1 15  ? 12.22979  -17.18335 -24.62091 1.000 19.16852 ? 22  PHE   A CD1 1 
ATOM   56   C  CD2 . PHE   A 1 15  ? 13.12100  -19.24357 -23.81092 1.000 19.09399 ? 22  PHE   A CD2 1 
ATOM   57   C  CE1 . PHE   A 1 15  ? 10.93843  -17.65168 -24.41996 1.000 22.27531 ? 22  PHE   A CE1 1 
ATOM   58   C  CE2 . PHE   A 1 15  ? 11.83394  -19.72140 -23.61001 1.000 21.50251 ? 22  PHE   A CE2 1 
ATOM   59   C  CZ  . PHE   A 1 15  ? 10.74204  -18.92591 -23.91287 1.000 19.31898 ? 22  PHE   A CZ  1 
ATOM   60   N  N   . GLN   A 1 16  ? 16.22184  -15.10196 -26.14524 1.000 18.46065 ? 23  GLN   A N   1 
ATOM   61   C  CA  . GLN   A 1 16  ? 17.34164  -14.21636 -25.85161 1.000 20.72716 ? 23  GLN   A CA  1 
ATOM   62   C  C   . GLN   A 1 16  ? 17.87699  -14.52017 -24.46138 1.000 20.55080 ? 23  GLN   A C   1 
ATOM   63   O  O   . GLN   A 1 16  ? 17.12415  -14.86328 -23.54789 1.000 21.61454 ? 23  GLN   A O   1 
ATOM   64   C  CB  . GLN   A 1 16  ? 16.92038  -12.75164 -25.94213 1.000 21.84394 ? 23  GLN   A CB  1 
ATOM   65   C  CG  . GLN   A 1 16  ? 16.52946  -12.30196 -27.32478 1.000 26.81495 ? 23  GLN   A CG  1 
ATOM   66   C  CD  . GLN   A 1 16  ? 16.01504  -10.88065 -27.32400 1.000 39.13103 ? 23  GLN   A CD  1 
ATOM   67   O  OE1 . GLN   A 1 16  ? 14.81460  -10.65726 -27.22399 1.000 34.08772 ? 23  GLN   A OE1 1 
ATOM   68   N  NE2 . GLN   A 1 16  ? 16.91747  -9.91218  -27.44582 1.000 37.78759 ? 23  GLN   A NE2 1 
ATOM   69   N  N   A ALA   A 1 17  ? 19.19668  -14.40944 -24.30981 0.653 22.13852 ? 24  ALA   A N   1 
ATOM   70   N  N   B ALA   A 1 17  ? 19.19192  -14.36527 -24.29882 0.347 22.18548 ? 24  ALA   A N   1 
ATOM   71   C  CA  A ALA   A 1 17  ? 19.82252  -14.77652 -23.04526 0.653 23.61810 ? 24  ALA   A CA  1 
ATOM   72   C  CA  B ALA   A 1 17  ? 19.82962  -14.72268 -23.03648 0.347 23.73436 ? 24  ALA   A CA  1 
ATOM   73   C  C   A ALA   A 1 17  ? 19.16809  -14.05786 -21.87608 0.653 21.37572 ? 24  ALA   A C   1 
ATOM   74   C  C   B ALA   A 1 17  ? 19.13298  -14.07370 -21.84802 0.347 21.49284 ? 24  ALA   A C   1 
ATOM   75   O  O   A ALA   A 1 17  ? 18.95588  -14.64949 -20.81138 0.653 22.55813 ? 24  ALA   A O   1 
ATOM   76   O  O   B ALA   A 1 17  ? 18.93172  -14.71601 -20.81113 0.347 22.61219 ? 24  ALA   A O   1 
ATOM   77   C  CB  A ALA   A 1 17  ? 21.31908  -14.46864 -23.09124 0.653 23.40839 ? 24  ALA   A CB  1 
ATOM   78   C  CB  B ALA   A 1 17  ? 21.30694  -14.32997 -23.06690 0.347 23.36508 ? 24  ALA   A CB  1 
ATOM   79   N  N   A GLU   A 1 18  ? 18.84408  -12.77567 -22.05409 0.653 25.12259 ? 25  GLU   A N   1 
ATOM   80   N  N   B GLU   A 1 18  ? 18.76136  -12.79758 -21.97477 0.347 25.21849 ? 25  GLU   A N   1 
ATOM   81   C  CA  A GLU   A 1 18  ? 18.25470  -12.00824 -20.96347 0.653 24.34389 ? 25  GLU   A CA  1 
ATOM   82   C  CA  B GLU   A 1 18  ? 18.20786  -12.07919 -20.83030 0.347 24.37935 ? 25  GLU   A CA  1 
ATOM   83   C  C   A GLU   A 1 18  ? 16.88152  -12.54367 -20.57825 0.653 25.65592 ? 25  GLU   A C   1 
ATOM   84   C  C   B GLU   A 1 18  ? 16.86379  -12.65747 -20.40180 0.347 25.64135 ? 25  GLU   A C   1 
ATOM   85   O  O   A GLU   A 1 18  ? 16.50111  -12.48764 -19.40191 0.653 23.11305 ? 25  GLU   A O   1 
ATOM   86   O  O   B GLU   A 1 18  ? 16.59241  -12.78733 -19.20191 0.347 24.40036 ? 25  GLU   A O   1 
ATOM   87   C  CB  A GLU   A 1 18  ? 18.16608  -10.53031 -21.34919 0.653 29.88496 ? 25  GLU   A CB  1 
ATOM   88   C  CB  B GLU   A 1 18  ? 18.07386  -10.59154 -21.15465 0.347 29.68912 ? 25  GLU   A CB  1 
ATOM   89   C  CG  A GLU   A 1 18  ? 19.50802  -9.84404  -21.62400 0.653 35.71558 ? 25  GLU   A CG  1 
ATOM   90   C  CG  B GLU   A 1 18  ? 19.39719  -9.85625  -21.32802 0.347 35.12227 ? 25  GLU   A CG  1 
ATOM   91   C  CD  A GLU   A 1 18  ? 20.10275  -10.15752 -22.99472 0.653 39.62159 ? 25  GLU   A CD  1 
ATOM   92   C  CD  B GLU   A 1 18  ? 19.98418  -9.99511  -22.72252 0.347 39.07361 ? 25  GLU   A CD  1 
ATOM   93   O  OE1 A GLU   A 1 18  ? 19.53679  -10.98370 -23.74191 0.653 31.22339 ? 25  GLU   A OE1 1 
ATOM   94   O  OE1 B GLU   A 1 18  ? 19.38097  -10.68646 -23.57038 0.347 33.68720 ? 25  GLU   A OE1 1 
ATOM   95   O  OE2 A GLU   A 1 18  ? 21.15034  -9.56205  -23.32794 0.653 45.97590 ? 25  GLU   A OE2 1 
ATOM   96   O  OE2 B GLU   A 1 18  ? 21.05413  -9.40136  -22.97260 0.347 43.37365 ? 25  GLU   A OE2 1 
ATOM   97   N  N   A ILE   A 1 19  ? 16.12965  -13.06932 -21.54606 0.653 22.84772 ? 26  ILE   A N   1 
ATOM   98   N  N   B ILE   A 1 19  ? 16.00575  -13.00331 -21.36296 0.347 22.55024 ? 26  ILE   A N   1 
ATOM   99   C  CA  A ILE   A 1 19  ? 14.79983  -13.60086 -21.25661 0.653 17.66998 ? 26  ILE   A CA  1 
ATOM   100  C  CA  B ILE   A 1 19  ? 14.71090  -13.58618 -21.01893 0.347 18.92980 ? 26  ILE   A CA  1 
ATOM   101  C  C   A ILE   A 1 19  ? 14.90116  -14.98999 -20.63710 0.653 19.92508 ? 26  ILE   A C   1 
ATOM   102  C  C   B ILE   A 1 19  ? 14.90342  -14.94011 -20.34665 0.347 20.49680 ? 26  ILE   A C   1 
ATOM   103  O  O   A ILE   A 1 19  ? 14.14380  -15.33305 -19.72344 0.653 18.17868 ? 26  ILE   A O   1 
ATOM   104  O  O   B ILE   A 1 19  ? 14.25164  -15.25182 -19.34216 0.347 19.53887 ? 26  ILE   A O   1 
ATOM   105  C  CB  A ILE   A 1 19  ? 13.92509  -13.59600 -22.52811 0.653 17.19807 ? 26  ILE   A CB  1 
ATOM   106  C  CB  B ILE   A 1 19  ? 13.81399  -13.68627 -22.26895 0.347 18.90953 ? 26  ILE   A CB  1 
ATOM   107  C  CG1 A ILE   A 1 19  ? 13.37275  -12.19282 -22.82112 0.653 24.71497 ? 26  ILE   A CG1 1 
ATOM   108  C  CG1 B ILE   A 1 19  ? 13.33518  -12.29644 -22.70133 0.347 24.25001 ? 26  ILE   A CG1 1 
ATOM   109  C  CG2 A ILE   A 1 19  ? 12.75299  -14.55561 -22.38526 0.653 20.11859 ? 26  ILE   A CG2 1 
ATOM   110  C  CG2 B ILE   A 1 19  ? 12.61067  -14.57830 -22.00181 0.347 19.45821 ? 26  ILE   A CG2 1 
ATOM   111  C  CD1 A ILE   A 1 19  ? 14.40874  -11.13906 -23.17572 0.653 25.03001 ? 26  ILE   A CD1 1 
ATOM   112  C  CD1 B ILE   A 1 19  ? 14.28094  -11.57452 -23.64075 0.347 27.24601 ? 26  ILE   A CD1 1 
ATOM   113  N  N   A ALA   A 1 20  ? 15.84678  -15.80762 -21.10270 0.653 17.04063 ? 27  ALA   A N   1 
ATOM   114  N  N   B ALA   A 1 20  ? 15.81554  -15.75914 -20.87515 0.347 17.90037 ? 27  ALA   A N   1 
ATOM   115  C  CA  A ALA   A 1 20  ? 16.10064  -17.07349 -20.42603 0.653 19.02349 ? 27  ALA   A CA  1 
ATOM   116  C  CA  B ALA   A 1 20  ? 16.11081  -17.03693 -20.23694 0.347 19.22614 ? 27  ALA   A CA  1 
ATOM   117  C  C   A ALA   A 1 20  ? 16.47716  -16.83945 -18.96828 0.653 20.42288 ? 27  ALA   A C   1 
ATOM   118  C  C   B ALA   A 1 20  ? 16.46407  -16.84945 -18.76654 0.347 20.88138 ? 27  ALA   A C   1 
ATOM   119  O  O   A ALA   A 1 20  ? 16.06864  -17.59865 -18.08057 0.653 23.44033 ? 27  ALA   A O   1 
ATOM   120  O  O   B ALA   A 1 20  ? 15.99067  -17.59937 -17.90439 0.347 22.29302 ? 27  ALA   A O   1 
ATOM   121  C  CB  A ALA   A 1 20  ? 17.20059  -17.85043 -21.15103 0.653 21.17373 ? 27  ALA   A CB  1 
ATOM   122  C  CB  B ALA   A 1 20  ? 17.24703  -17.74558 -20.97724 0.347 21.57544 ? 27  ALA   A CB  1 
ATOM   123  N  N   A GLN   A 1 21  ? 17.24967  -15.78407 -18.70102 0.653 22.50396 ? 28  GLN   A N   1 
ATOM   124  N  N   B GLN   A 1 21  ? 17.29387  -15.84956 -18.45898 0.347 23.09956 ? 28  GLN   A N   1 
ATOM   125  C  CA  A GLN   A 1 21  ? 17.64540  -15.48915 -17.32910 0.653 22.29103 ? 28  GLN   A CA  1 
ATOM   126  C  CA  B GLN   A 1 21  ? 17.68756  -15.61992 -17.07253 0.347 22.75440 ? 28  GLN   A CA  1 
ATOM   127  C  C   A GLN   A 1 21  ? 16.45043  -15.04896 -16.49621 0.653 23.77874 ? 28  GLN   A C   1 
ATOM   128  C  C   B GLN   A 1 21  ? 16.48104  -15.26578 -16.21447 0.347 24.18883 ? 28  GLN   A C   1 
ATOM   129  O  O   A GLN   A 1 21  ? 16.32467  -15.43653 -15.32856 0.653 24.24108 ? 28  GLN   A O   1 
ATOM   130  O  O   B GLN   A 1 21  ? 16.29269  -15.82146 -15.12667 0.347 25.78407 ? 28  GLN   A O   1 
ATOM   131  C  CB  A GLN   A 1 21  ? 18.73008  -14.41534 -17.31528 0.653 23.97087 ? 28  GLN   A CB  1 
ATOM   132  C  CB  B GLN   A 1 21  ? 18.73966  -14.51375 -16.99389 0.347 26.07116 ? 28  GLN   A CB  1 
ATOM   133  C  CG  A GLN   A 1 21  ? 19.43167  -14.26852 -15.97421 0.653 37.60165 ? 28  GLN   A CG  1 
ATOM   134  C  CG  B GLN   A 1 21  ? 19.32197  -14.32955 -15.59707 0.347 34.82706 ? 28  GLN   A CG  1 
ATOM   135  C  CD  A GLN   A 1 21  ? 20.44844  -13.14089 -15.97077 0.653 50.45848 ? 28  GLN   A CD  1 
ATOM   136  C  CD  B GLN   A 1 21  ? 20.45012  -13.31451 -15.55547 0.347 47.71120 ? 28  GLN   A CD  1 
ATOM   137  O  OE1 A GLN   A 1 21  ? 20.58497  -12.40992 -16.95398 0.653 46.91894 ? 28  GLN   A OE1 1 
ATOM   138  O  OE1 B GLN   A 1 21  ? 20.45484  -12.34243 -16.31085 0.347 45.30422 ? 28  GLN   A OE1 1 
ATOM   139  N  NE2 A GLN   A 1 21  ? 21.16395  -12.99094 -14.86034 0.653 54.52759 ? 28  GLN   A NE2 1 
ATOM   140  N  NE2 B GLN   A 1 21  ? 21.41317  -13.53577 -14.66679 0.347 53.52406 ? 28  GLN   A NE2 1 
ATOM   141  N  N   A LEU   A 1 22  ? 15.56982  -14.22863 -17.07573 0.653 20.24480 ? 29  LEU   A N   1 
ATOM   142  N  N   B LEU   A 1 22  ? 15.65408  -14.33053 -16.68582 0.347 23.53336 ? 29  LEU   A N   1 
ATOM   143  C  CA  A LEU   A 1 22  ? 14.34476  -13.85068 -16.37659 0.653 24.74975 ? 29  LEU   A CA  1 
ATOM   144  C  CA  B LEU   A 1 22  ? 14.46082  -13.95767 -15.93253 0.347 22.38916 ? 29  LEU   A CA  1 
ATOM   145  C  C   A LEU   A 1 22  ? 13.51950  -15.07813 -16.01636 0.653 22.46731 ? 29  LEU   A C   1 
ATOM   146  C  C   B LEU   A 1 22  ? 13.58899  -15.17668 -15.65990 0.347 22.68945 ? 29  LEU   A C   1 
ATOM   147  O  O   A LEU   A 1 22  ? 13.01644  -15.19633 -14.89162 0.653 20.60501 ? 29  LEU   A O   1 
ATOM   148  O  O   B LEU   A 1 22  ? 13.11800  -15.38238 -14.53500 0.347 20.31581 ? 29  LEU   A O   1 
ATOM   149  C  CB  A LEU   A 1 22  ? 13.52196  -12.89185 -17.23880 0.653 19.96445 ? 29  LEU   A CB  1 
ATOM   150  C  CB  B LEU   A 1 22  ? 13.67509  -12.88633 -16.68966 0.347 26.25800 ? 29  LEU   A CB  1 
ATOM   151  C  CG  A LEU   A 1 22  ? 12.10499  -12.60940 -16.73417 0.653 23.71085 ? 29  LEU   A CG  1 
ATOM   152  C  CG  B LEU   A 1 22  ? 12.31103  -12.52148 -16.10036 0.347 23.61485 ? 29  LEU   A CG  1 
ATOM   153  C  CD1 A LEU   A 1 22  ? 12.14831  -11.70494 -15.51311 0.653 26.15319 ? 29  LEU   A CD1 1 
ATOM   154  C  CD1 B LEU   A 1 22  ? 12.48178  -11.50976 -14.98073 0.347 23.84646 ? 29  LEU   A CD1 1 
ATOM   155  C  CD2 A LEU   A 1 22  ? 11.25262  -11.99126 -17.83282 0.653 26.78402 ? 29  LEU   A CD2 1 
ATOM   156  C  CD2 B LEU   A 1 22  ? 11.37855  -11.98505 -17.17669 0.347 28.62616 ? 29  LEU   A CD2 1 
ATOM   157  N  N   A MET   A 1 23  ? 13.37402  -16.00949 -16.95891 0.653 17.94227 ? 30  MET   A N   1 
ATOM   158  N  N   B MET   A 1 23  ? 13.37084  -16.00780 -16.68115 0.347 19.60897 ? 30  MET   A N   1 
ATOM   159  C  CA  A MET   A 1 23  ? 12.53885  -17.17537 -16.70581 0.653 20.07792 ? 30  MET   A CA  1 
ATOM   160  C  CA  B MET   A 1 23  ? 12.54912  -17.19633 -16.48841 0.347 20.31834 ? 30  MET   A CA  1 
ATOM   161  C  C   A MET   A 1 23  ? 13.14726  -18.07126 -15.63371 0.653 22.34132 ? 30  MET   A C   1 
ATOM   162  C  C   B MET   A 1 23  ? 13.13577  -18.10411 -15.41327 0.347 21.31581 ? 30  MET   A C   1 
ATOM   163  O  O   A MET   A 1 23  ? 12.42592  -18.60030 -14.78119 0.653 20.18392 ? 30  MET   A O   1 
ATOM   164  O  O   B MET   A 1 23  ? 12.40296  -18.62399 -14.56449 0.347 21.28038 ? 30  MET   A O   1 
ATOM   165  C  CB  A MET   A 1 23  ? 12.30854  -17.94628 -18.00599 0.653 18.09813 ? 30  MET   A CB  1 
ATOM   166  C  CB  B MET   A 1 23  ? 12.38867  -17.94852 -17.81156 0.347 18.59051 ? 30  MET   A CB  1 
ATOM   167  C  CG  A MET   A 1 23  ? 11.33293  -17.25667 -18.95001 0.653 19.50972 ? 30  MET   A CG  1 
ATOM   168  C  CG  B MET   A 1 23  ? 11.35950  -17.32953 -18.75149 0.347 19.34186 ? 30  MET   A CG  1 
ATOM   169  S  SD  A MET   A 1 23  ? 11.28708  -18.00194 -20.59619 0.653 20.23331 ? 30  MET   A SD  1 
ATOM   170  S  SD  B MET   A 1 23  ? 11.46300  -17.93668 -20.45165 0.347 23.14789 ? 30  MET   A SD  1 
ATOM   171  C  CE  A MET   A 1 23  ? 10.10995  -19.31910 -20.31193 0.653 21.96615 ? 30  MET   A CE  1 
ATOM   172  C  CE  B MET   A 1 23  ? 10.06356  -19.05072 -20.48325 0.347 21.66202 ? 30  MET   A CE  1 
ATOM   173  N  N   A SER   A 1 24  ? 14.46856  -18.25570 -15.65063 0.653 21.38483 ? 31  SER   A N   1 
ATOM   174  N  N   B SER   A 1 24  ? 14.45672  -18.29848 -15.42122 0.347 21.99723 ? 31  SER   A N   1 
ATOM   175  C  CA  A SER   A 1 24  ? 15.07626  -19.09361 -14.62211 0.653 21.05328 ? 31  SER   A CA  1 
ATOM   176  C  CA  B SER   A 1 24  ? 15.06061  -19.21274 -14.45519 0.347 21.29348 ? 31  SER   A CA  1 
ATOM   177  C  C   A SER   A 1 24  ? 15.01638  -18.42300 -13.25180 0.653 25.48038 ? 31  SER   A C   1 
ATOM   178  C  C   B SER   A 1 24  ? 14.91024  -18.69239 -13.02962 0.347 25.46648 ? 31  SER   A C   1 
ATOM   179  O  O   A SER   A 1 24  ? 14.88909  -19.11149 -12.23024 0.653 28.85835 ? 31  SER   A O   1 
ATOM   180  O  O   B SER   A 1 24  ? 14.67469  -19.47355 -12.09856 0.347 26.25095 ? 31  SER   A O   1 
ATOM   181  C  CB  A SER   A 1 24  ? 16.51377  -19.45379 -15.01026 0.653 27.12733 ? 31  SER   A CB  1 
ATOM   182  C  CB  B SER   A 1 24  ? 16.53428  -19.44501 -14.79158 0.347 27.70847 ? 31  SER   A CB  1 
ATOM   183  O  OG  A SER   A 1 24  ? 17.38702  -18.35465 -14.86501 0.653 39.38293 ? 31  SER   A OG  1 
ATOM   184  O  OG  B SER   A 1 24  ? 17.21965  -20.02453 -13.69199 0.347 24.19681 ? 31  SER   A OG  1 
ATOM   185  N  N   A LEU   A 1 25  ? 15.07027  -17.08828 -13.20608 0.653 19.13341 ? 32  LEU   A N   1 
ATOM   186  N  N   B LEU   A 1 25  ? 15.04248  -17.37747 -12.83603 0.347 23.66129 ? 32  LEU   A N   1 
ATOM   187  C  CA  A LEU   A 1 25  ? 14.89763  -16.39654 -11.93349 0.653 19.39121 ? 32  LEU   A CA  1 
ATOM   188  C  CA  B LEU   A 1 25  ? 14.86722  -16.81723 -11.50054 0.347 20.62602 ? 32  LEU   A CA  1 
ATOM   189  C  C   A LEU   A 1 25  ? 13.50225  -16.63799 -11.37020 0.653 24.01255 ? 32  LEU   A C   1 
ATOM   190  C  C   B LEU   A 1 25  ? 13.40253  -16.84919 -11.08122 0.347 24.00438 ? 32  LEU   A C   1 
ATOM   191  O  O   A LEU   A 1 25  ? 13.34187  -16.88490 -10.16940 0.653 22.65816 ? 32  LEU   A O   1 
ATOM   192  O  O   B LEU   A 1 25  ? 13.09112  -17.14643 -9.92232  0.347 25.72026 ? 32  LEU   A O   1 
ATOM   193  C  CB  A LEU   A 1 25  ? 15.16219  -14.89828 -12.11117 0.653 24.67524 ? 32  LEU   A CB  1 
ATOM   194  C  CB  B LEU   A 1 25  ? 15.42058  -15.39528 -11.44736 0.347 30.61342 ? 32  LEU   A CB  1 
ATOM   195  C  CG  A LEU   A 1 25  ? 15.09263  -13.96353 -10.89577 0.653 35.24453 ? 32  LEU   A CG  1 
ATOM   196  C  CG  B LEU   A 1 25  ? 16.62518  -15.22823 -10.51578 0.347 42.43128 ? 32  LEU   A CG  1 
ATOM   197  C  CD1 A LEU   A 1 25  ? 15.94415  -12.73228 -11.16029 0.653 44.45241 ? 32  LEU   A CD1 1 
ATOM   198  C  CD1 B LEU   A 1 25  ? 17.91731  -15.26997 -11.30805 0.347 28.71397 ? 32  LEU   A CD1 1 
ATOM   199  C  CD2 A LEU   A 1 25  ? 13.66680  -13.54173 -10.54212 0.653 33.61521 ? 32  LEU   A CD2 1 
ATOM   200  C  CD2 B LEU   A 1 25  ? 16.52617  -13.94315 -9.71301  0.347 33.52086 ? 32  LEU   A CD2 1 
ATOM   201  N  N   A ILE   A 1 26  ? 12.47896  -16.56222 -12.22302 0.653 18.37057 ? 33  ILE   A N   1 
ATOM   202  N  N   B ILE   A 1 26  ? 12.48748  -16.54893 -12.00749 0.347 20.16109 ? 33  ILE   A N   1 
ATOM   203  C  CA  A ILE   A 1 26  ? 11.10704  -16.75224 -11.75965 0.653 21.17198 ? 33  ILE   A CA  1 
ATOM   204  C  CA  B ILE   A 1 26  ? 11.06899  -16.76394 -11.73016 0.347 21.22410 ? 33  ILE   A CA  1 
ATOM   205  C  C   A ILE   A 1 26  ? 10.89759  -18.18101 -11.27064 0.653 23.49462 ? 33  ILE   A C   1 
ATOM   206  C  C   B ILE   A 1 26  ? 10.83435  -18.20324 -11.29541 0.347 23.48517 ? 33  ILE   A C   1 
ATOM   207  O  O   A ILE   A 1 26  ? 10.20884  -18.41872 -10.27067 0.653 24.39141 ? 33  ILE   A O   1 
ATOM   208  O  O   B ILE   A 1 26  ? 10.06762  -18.47329 -10.36219 0.347 23.69914 ? 33  ILE   A O   1 
ATOM   209  C  CB  A ILE   A 1 26  ? 10.12280  -16.38427 -12.88344 0.653 17.98184 ? 33  ILE   A CB  1 
ATOM   210  C  CB  B ILE   A 1 26  ? 10.21551  -16.40443 -12.96126 0.347 18.05040 ? 33  ILE   A CB  1 
ATOM   211  C  CG1 A ILE   A 1 26  ? 10.09944  -14.87012 -13.09167 0.653 25.20221 ? 33  ILE   A CG1 1 
ATOM   212  C  CG1 B ILE   A 1 26  ? 10.24468  -14.89890 -13.21844 0.347 24.37384 ? 33  ILE   A CG1 1 
ATOM   213  C  CG2 A ILE   A 1 26  ? 8.72241   -16.90363 -12.57161 0.653 20.13413 ? 33  ILE   A CG2 1 
ATOM   214  C  CG2 B ILE   A 1 26  ? 8.77908   -16.88627 -12.78050 0.347 20.59708 ? 33  ILE   A CG2 1 
ATOM   215  C  CD1 A ILE   A 1 26  ? 9.45045   -14.43993 -14.39428 0.653 25.10629 ? 33  ILE   A CD1 1 
ATOM   216  C  CD1 B ILE   A 1 26  ? 9.64549   -14.50071 -14.54918 0.347 24.43553 ? 33  ILE   A CD1 1 
ATOM   217  N  N   . ILE   A 1 27  ? 11.49442  -19.15171 -11.96148 1.000 21.25371 ? 34  ILE   A N   1 
ATOM   218  C  CA  . ILE   A 1 27  ? 11.27868  -20.55778 -11.63311 1.000 25.36319 ? 34  ILE   A CA  1 
ATOM   219  C  C   . ILE   A 1 27  ? 12.03547  -20.94877 -10.36693 1.000 29.50835 ? 34  ILE   A C   1 
ATOM   220  O  O   . ILE   A 1 27  ? 11.53692  -21.73397 -9.55083  1.000 26.62041 ? 34  ILE   A O   1 
ATOM   221  C  CB  . ILE   A 1 27  ? 11.67559  -21.43196 -12.83967 1.000 26.15329 ? 34  ILE   A CB  1 
ATOM   222  C  CG1 . ILE   A 1 27  ? 10.67069  -21.23749 -13.98360 1.000 23.64762 ? 34  ILE   A CG1 1 
ATOM   223  C  CG2 . ILE   A 1 27  ? 11.81779  -22.89714 -12.44502 1.000 27.76683 ? 34  ILE   A CG2 1 
ATOM   224  C  CD1 . ILE   A 1 27  ? 11.15403  -21.78205 -15.31586 1.000 25.88837 ? 34  ILE   A CD1 1 
ATOM   225  N  N   . ASN   A 1 28  ? 13.23171  -20.39312 -10.16694 1.000 25.95382 ? 35  ASN   A N   1 
ATOM   226  C  CA  . ASN   A 1 28  ? 14.14935  -20.88134 -9.13839  1.000 26.57868 ? 35  ASN   A CA  1 
ATOM   227  C  C   . ASN   A 1 28  ? 14.06522  -20.12972 -7.81899  1.000 35.80403 ? 35  ASN   A C   1 
ATOM   228  O  O   . ASN   A 1 28  ? 14.39175  -20.70267 -6.77194  1.000 34.81228 ? 35  ASN   A O   1 
ATOM   229  C  CB  . ASN   A 1 28  ? 15.58894  -20.79944 -9.64600  1.000 28.74382 ? 35  ASN   A CB  1 
ATOM   230  C  CG  . ASN   A 1 28  ? 15.81818  -21.64817 -10.86549 1.000 47.78145 ? 35  ASN   A CG  1 
ATOM   231  O  OD1 . ASN   A 1 28  ? 16.62212  -21.30138 -11.73539 1.000 57.18634 ? 35  ASN   A OD1 1 
ATOM   232  N  ND2 . ASN   A 1 28  ? 15.14081  -22.79127 -10.92275 1.000 33.19892 ? 35  ASN   A ND2 1 
ATOM   233  N  N   . THR   A 1 29  ? 13.67610  -18.85827 -7.83715  1.000 26.84880 ? 36  THR   A N   1 
ATOM   234  C  CA  . THR   A 1 29  ? 13.67615  -18.06695 -6.61350  1.000 30.84902 ? 36  THR   A CA  1 
ATOM   235  C  C   . THR   A 1 29  ? 12.56821  -18.53007 -5.67551  1.000 32.43316 ? 36  THR   A C   1 
ATOM   236  O  O   . THR   A 1 29  ? 11.43025  -18.74747 -6.10095  1.000 31.31824 ? 36  THR   A O   1 
ATOM   237  C  CB  . THR   A 1 29  ? 13.50165  -16.58530 -6.94215  1.000 31.07808 ? 36  THR   A CB  1 
ATOM   238  O  OG1 . THR   A 1 29  ? 14.54578  -16.16985 -7.82847  1.000 32.25592 ? 36  THR   A OG1 1 
ATOM   239  C  CG2 . THR   A 1 29  ? 13.53949  -15.73737 -5.67369  1.000 35.80148 ? 36  THR   A CG2 1 
ATOM   240  N  N   . PHE   A 1 30  ? 12.90017  -18.68754 -4.39702  1.000 27.48733 ? 37  PHE   A N   1 
ATOM   241  C  CA  . PHE   A 1 30  ? 11.86686  -18.95032 -3.40527  1.000 24.99880 ? 37  PHE   A CA  1 
ATOM   242  C  C   . PHE   A 1 30  ? 11.02272  -17.69458 -3.21131  1.000 27.65186 ? 37  PHE   A C   1 
ATOM   243  O  O   . PHE   A 1 30  ? 11.53966  -16.63751 -2.82901  1.000 27.87323 ? 37  PHE   A O   1 
ATOM   244  C  CB  . PHE   A 1 30  ? 12.48000  -19.40190 -2.08474  1.000 27.67365 ? 37  PHE   A CB  1 
ATOM   245  C  CG  . PHE   A 1 30  ? 11.45848  -19.68418 -1.02619  1.000 30.67175 ? 37  PHE   A CG  1 
ATOM   246  C  CD1 . PHE   A 1 30  ? 10.72197  -20.85643 -1.05349  1.000 36.77861 ? 37  PHE   A CD1 1 
ATOM   247  C  CD2 . PHE   A 1 30  ? 11.21966  -18.77080 -0.01322  1.000 30.39956 ? 37  PHE   A CD2 1 
ATOM   248  C  CE1 . PHE   A 1 30  ? 9.76487   -21.11508 -0.08750  1.000 31.74671 ? 37  PHE   A CE1 1 
ATOM   249  C  CE2 . PHE   A 1 30  ? 10.26437  -19.02454 0.95835   1.000 36.23684 ? 37  PHE   A CE2 1 
ATOM   250  C  CZ  . PHE   A 1 30  ? 9.53772   -20.19918 0.92149   1.000 29.25146 ? 37  PHE   A CZ  1 
ATOM   251  N  N   . TYR   A 1 31  ? 9.72211   -17.81375 -3.47195  1.000 23.97596 ? 38  TYR   A N   1 
ATOM   252  C  CA  . TYR   A 1 31  ? 8.82593   -16.66051 -3.45479  1.000 23.36709 ? 38  TYR   A CA  1 
ATOM   253  C  C   . TYR   A 1 31  ? 7.40423   -17.19478 -3.31759  1.000 20.60385 ? 38  TYR   A C   1 
ATOM   254  O  O   . TYR   A 1 31  ? 6.86948   -17.76616 -4.26921  1.000 21.84615 ? 38  TYR   A O   1 
ATOM   255  C  CB  . TYR   A 1 31  ? 8.99399   -15.83038 -4.72627  1.000 26.93171 ? 38  TYR   A CB  1 
ATOM   256  C  CG  . TYR   A 1 31  ? 8.07352   -14.64175 -4.78990  1.000 29.34188 ? 38  TYR   A CG  1 
ATOM   257  C  CD1 . TYR   A 1 31  ? 8.29332   -13.53253 -3.98556  1.000 28.36079 ? 38  TYR   A CD1 1 
ATOM   258  C  CD2 . TYR   A 1 31  ? 6.97044   -14.63451 -5.63988  1.000 28.02770 ? 38  TYR   A CD2 1 
ATOM   259  C  CE1 . TYR   A 1 31  ? 7.45038   -12.44271 -4.02553  1.000 41.72455 ? 38  TYR   A CE1 1 
ATOM   260  C  CE2 . TYR   A 1 31  ? 6.11739   -13.54338 -5.68613  1.000 25.68165 ? 38  TYR   A CE2 1 
ATOM   261  C  CZ  . TYR   A 1 31  ? 6.36823   -12.45184 -4.87597  1.000 35.33125 ? 38  TYR   A CZ  1 
ATOM   262  O  OH  . TYR   A 1 31  ? 5.53215   -11.35936 -4.90535  1.000 46.27181 ? 38  TYR   A OH  1 
ATOM   263  N  N   . SER   A 1 32  ? 6.80280   -17.01451 -2.14007  1.000 21.96525 ? 39  SER   A N   1 
ATOM   264  C  CA  . SER   A 1 32  ? 5.55170   -17.69309 -1.82420  1.000 22.21612 ? 39  SER   A CA  1 
ATOM   265  C  C   . SER   A 1 32  ? 4.33128   -17.04993 -2.47879  1.000 23.02651 ? 39  SER   A C   1 
ATOM   266  O  O   . SER   A 1 32  ? 3.32217   -17.73379 -2.67453  1.000 26.58799 ? 39  SER   A O   1 
ATOM   267  C  CB  . SER   A 1 32  ? 5.35407   -17.73289 -0.30766  1.000 23.77230 ? 39  SER   A CB  1 
ATOM   268  O  OG  . SER   A 1 32  ? 6.36149   -18.52758 0.30137   1.000 24.31288 ? 39  SER   A OG  1 
ATOM   269  N  N   . ASN   A 1 33  ? 4.40241   -15.76693 -2.83225  1.000 20.92547 ? 40  ASN   A N   1 
ATOM   270  C  CA  . ASN   A 1 33  ? 3.23219   -14.99954 -3.26558  1.000 23.51325 ? 40  ASN   A CA  1 
ATOM   271  C  C   . ASN   A 1 33  ? 2.96466   -15.22194 -4.76138  1.000 24.38322 ? 40  ASN   A C   1 
ATOM   272  O  O   . ASN   A 1 33  ? 2.93467   -14.30007 -5.57856  1.000 20.46899 ? 40  ASN   A O   1 
ATOM   273  C  CB  . ASN   A 1 33  ? 3.45288   -13.52854 -2.92746  1.000 26.26857 ? 40  ASN   A CB  1 
ATOM   274  C  CG  . ASN   A 1 33  ? 2.27660   -12.64304 -3.30411  1.000 32.09928 ? 40  ASN   A CG  1 
ATOM   275  O  OD1 . ASN   A 1 33  ? 1.11691   -13.02653 -3.14701  1.000 29.71546 ? 40  ASN   A OD1 1 
ATOM   276  N  ND2 . ASN   A 1 33  ? 2.57509   -11.44089 -3.78519  1.000 30.00939 ? 40  ASN   A ND2 1 
ATOM   277  N  N   . LYS   A 1 34  ? 2.74150   -16.49391 -5.10933  1.000 19.15825 ? 41  LYS   A N   1 
ATOM   278  C  CA  . LYS   A 1 34  ? 2.64226   -16.88309 -6.51235  1.000 18.17308 ? 41  LYS   A CA  1 
ATOM   279  C  C   . LYS   A 1 34  ? 1.34780   -16.41014 -7.16872  1.000 17.41251 ? 41  LYS   A C   1 
ATOM   280  O  O   . LYS   A 1 34  ? 1.28303   -16.35074 -8.40420  1.000 19.07150 ? 41  LYS   A O   1 
ATOM   281  C  CB  . LYS   A 1 34  ? 2.74516   -18.40576 -6.63921  1.000 19.02009 ? 41  LYS   A CB  1 
ATOM   282  C  CG  . LYS   A 1 34  ? 4.12413   -18.99861 -6.32396  1.000 19.83515 ? 41  LYS   A CG  1 
ATOM   283  C  CD  . LYS   A 1 34  ? 4.08556   -20.52129 -6.42351  1.000 25.89770 ? 41  LYS   A CD  1 
ATOM   284  C  CE  . LYS   A 1 34  ? 5.46009   -21.15891 -6.22149  1.000 25.14626 ? 41  LYS   A CE  1 
ATOM   285  N  NZ  . LYS   A 1 34  ? 6.37147   -20.96595 -7.37906  1.000 23.93415 ? 41  LYS   A NZ  1 
ATOM   286  N  N   . GLU   A 1 35  ? 0.32208   -16.07109 -6.38049  1.000 18.79887 ? 42  GLU   A N   1 
ATOM   287  C  CA  . GLU   A 1 35  ? -0.99346  -15.76441 -6.94552  1.000 17.81745 ? 42  GLU   A CA  1 
ATOM   288  C  C   . GLU   A 1 35  ? -0.97218  -14.57026 -7.88996  1.000 21.54983 ? 42  GLU   A C   1 
ATOM   289  O  O   . GLU   A 1 35  ? -1.91498  -14.40273 -8.67424  1.000 20.67538 ? 42  GLU   A O   1 
ATOM   290  C  CB  . GLU   A 1 35  ? -2.01529  -15.50341 -5.83109  1.000 20.33434 ? 42  GLU   A CB  1 
ATOM   291  C  CG  . GLU   A 1 35  ? -1.76895  -14.23550 -5.03750  1.000 19.76067 ? 42  GLU   A CG  1 
ATOM   292  C  CD  . GLU   A 1 35  ? -2.69967  -14.09796 -3.83717  1.000 31.88306 ? 42  GLU   A CD  1 
ATOM   293  O  OE1 . GLU   A 1 35  ? -2.93903  -15.10711 -3.14066  1.000 32.18523 ? 42  GLU   A OE1 1 
ATOM   294  O  OE2 . GLU   A 1 35  ? -3.17475  -12.97246 -3.58229  1.000 38.82524 ? 42  GLU   A OE2 1 
ATOM   295  N  N   . ILE   A 1 36  ? 0.07302   -13.73908 -7.83957  1.000 21.05110 ? 43  ILE   A N   1 
ATOM   296  C  CA  . ILE   A 1 36  ? 0.11467   -12.54884 -8.68038  1.000 17.34888 ? 43  ILE   A CA  1 
ATOM   297  C  C   . ILE   A 1 36  ? 0.15975   -12.88600 -10.16446 1.000 19.07342 ? 43  ILE   A C   1 
ATOM   298  O  O   . ILE   A 1 36  ? -0.10156  -12.00779 -10.99356 1.000 19.16238 ? 43  ILE   A O   1 
ATOM   299  C  CB  . ILE   A 1 36  ? 1.30686   -11.64374 -8.29157  1.000 23.00096 ? 43  ILE   A CB  1 
ATOM   300  C  CG1 . ILE   A 1 36  ? 2.62922   -12.38958 -8.44742  1.000 23.47701 ? 43  ILE   A CG1 1 
ATOM   301  C  CG2 . ILE   A 1 36  ? 1.12846   -11.11274 -6.87630  1.000 28.74477 ? 43  ILE   A CG2 1 
ATOM   302  C  CD1 . ILE   A 1 36  ? 3.34942   -12.08479 -9.74405  1.000 37.39914 ? 43  ILE   A CD1 1 
ATOM   303  N  N   . PHE   A 1 37  ? 0.49168   -14.13340 -10.53247 1.000 15.84895 ? 44  PHE   A N   1 
ATOM   304  C  CA  . PHE   A 1 37  ? 0.49187   -14.49155 -11.95274 1.000 17.29073 ? 44  PHE   A CA  1 
ATOM   305  C  C   . PHE   A 1 37  ? -0.85112  -14.16272 -12.59574 1.000 19.61273 ? 44  PHE   A C   1 
ATOM   306  O  O   . PHE   A 1 37  ? -0.91074  -13.71478 -13.74677 1.000 16.38654 ? 44  PHE   A O   1 
ATOM   307  C  CB  . PHE   A 1 37  ? 0.81094   -15.98116 -12.15267 1.000 16.92246 ? 44  PHE   A CB  1 
ATOM   308  C  CG  . PHE   A 1 37  ? -0.37898  -16.88765 -11.94978 1.000 19.79868 ? 44  PHE   A CG  1 
ATOM   309  C  CD1 . PHE   A 1 37  ? -0.69170  -17.36782 -10.69318 1.000 19.28228 ? 44  PHE   A CD1 1 
ATOM   310  C  CD2 . PHE   A 1 37  ? -1.20837  -17.21866 -13.01501 1.000 23.60827 ? 44  PHE   A CD2 1 
ATOM   311  C  CE1 . PHE   A 1 37  ? -1.80171  -18.18777 -10.49973 1.000 18.75755 ? 44  PHE   A CE1 1 
ATOM   312  C  CE2 . PHE   A 1 37  ? -2.32162  -18.02640 -12.82596 1.000 17.27098 ? 44  PHE   A CE2 1 
ATOM   313  C  CZ  . PHE   A 1 37  ? -2.61464  -18.51215 -11.56578 1.000 17.31474 ? 44  PHE   A CZ  1 
ATOM   314  N  N   . LEU   A 1 38  ? -1.94699  -14.36438 -11.85989 1.000 16.30538 ? 45  LEU   A N   1 
ATOM   315  C  CA  . LEU   A 1 38  ? -3.25934  -14.18794 -12.47270 1.000 14.82768 ? 45  LEU   A CA  1 
ATOM   316  C  C   . LEU   A 1 38  ? -3.56637  -12.71035 -12.68149 1.000 17.09462 ? 45  LEU   A C   1 
ATOM   317  O  O   . LEU   A 1 38  ? -4.11528  -12.32314 -13.72273 1.000 18.61297 ? 45  LEU   A O   1 
ATOM   318  C  CB  . LEU   A 1 38  ? -4.33260  -14.85416 -11.61835 1.000 15.00811 ? 45  LEU   A CB  1 
ATOM   319  C  CG  . LEU   A 1 38  ? -5.73640  -14.83555 -12.23690 1.000 17.78744 ? 45  LEU   A CG  1 
ATOM   320  C  CD1 . LEU   A 1 38  ? -5.73590  -15.52600 -13.59481 1.000 17.80697 ? 45  LEU   A CD1 1 
ATOM   321  C  CD2 . LEU   A 1 38  ? -6.71807  -15.51774 -11.30461 1.000 24.52598 ? 45  LEU   A CD2 1 
ATOM   322  N  N   . ARG   A 1 39  ? -3.20475  -11.87170 -11.70500 1.000 17.22385 ? 46  ARG   A N   1 
ATOM   323  C  CA  . ARG   A 1 39  ? -3.31910  -10.42738 -11.87786 1.000 18.06591 ? 46  ARG   A CA  1 
ATOM   324  C  C   . ARG   A 1 39  ? -2.56154  -9.96854  -13.11236 1.000 19.86788 ? 46  ARG   A C   1 
ATOM   325  O  O   . ARG   A 1 39  ? -3.06701  -9.16075  -13.90060 1.000 17.79462 ? 46  ARG   A O   1 
ATOM   326  C  CB  . ARG   A 1 39  ? -2.78497  -9.70622  -10.63903 1.000 19.58596 ? 46  ARG   A CB  1 
ATOM   327  C  CG  . ARG   A 1 39  ? -2.74468  -8.19070  -10.78046 1.000 22.94142 ? 46  ARG   A CG  1 
ATOM   328  C  CD  . ARG   A 1 39  ? -2.03006  -7.51888  -9.61133  1.000 31.92067 ? 46  ARG   A CD  1 
ATOM   329  N  NE  . ARG   A 1 39  ? -0.58979  -7.74338  -9.65605  1.000 32.98328 ? 46  ARG   A NE  1 
ATOM   330  C  CZ  . ARG   A 1 39  ? 0.22425   -7.66056  -8.61120  1.000 37.18462 ? 46  ARG   A CZ  1 
ATOM   331  N  NH1 . ARG   A 1 39  ? -0.22064  -7.33895  -7.40615  1.000 30.75984 ? 46  ARG   A NH1 1 
ATOM   332  N  NH2 . ARG   A 1 39  ? 1.52139   -7.89712  -8.78155  1.000 37.25233 ? 46  ARG   A NH2 1 
ATOM   333  N  N   . GLU   A 1 40  ? -1.34932  -10.48919 -13.30437 1.000 16.73531 ? 47  GLU   A N   1 
ATOM   334  C  CA  . GLU   A 1 40  ? -0.52077  -10.03022 -14.41126 1.000 18.71680 ? 47  GLU   A CA  1 
ATOM   335  C  C   . GLU   A 1 40  ? -1.11213  -10.44359 -15.75359 1.000 18.62134 ? 47  GLU   A C   1 
ATOM   336  O  O   . GLU   A 1 40  ? -1.10052  -9.66028  -16.71094 1.000 16.68083 ? 47  GLU   A O   1 
ATOM   337  C  CB  . GLU   A 1 40  ? 0.90237   -10.56894 -14.25779 1.000 16.92767 ? 47  GLU   A CB  1 
ATOM   338  C  CG  . GLU   A 1 40  ? 1.64836   -10.02155 -13.04055 1.000 21.29135 ? 47  GLU   A CG  1 
ATOM   339  C  CD  . GLU   A 1 40  ? 1.56501   -8.50594  -12.91852 1.000 28.42913 ? 47  GLU   A CD  1 
ATOM   340  O  OE1 . GLU   A 1 40  ? 1.64316   -7.81249  -13.95330 1.000 27.10326 ? 47  GLU   A OE1 1 
ATOM   341  O  OE2 . GLU   A 1 40  ? 1.42452   -8.00604  -11.78203 1.000 33.64058 ? 47  GLU   A OE2 1 
ATOM   342  N  N   . LEU   A 1 41  ? -1.63079  -11.66797 -15.84906 1.000 15.96718 ? 48  LEU   A N   1 
ATOM   343  C  CA  . LEU   A 1 41  ? -2.19867  -12.11446 -17.12019 1.000 17.61810 ? 48  LEU   A CA  1 
ATOM   344  C  C   . LEU   A 1 41  ? -3.50801  -11.39793 -17.42492 1.000 16.51463 ? 48  LEU   A C   1 
ATOM   345  O  O   . LEU   A 1 41  ? -3.79744  -11.08903 -18.58803 1.000 16.68852 ? 48  LEU   A O   1 
ATOM   346  C  CB  . LEU   A 1 41  ? -2.40364  -13.62923 -17.11222 1.000 14.99669 ? 48  LEU   A CB  1 
ATOM   347  C  CG  . LEU   A 1 41  ? -1.11855  -14.46024 -17.03730 1.000 16.29531 ? 48  LEU   A CG  1 
ATOM   348  C  CD1 . LEU   A 1 41  ? -1.44022  -15.94918 -16.95297 1.000 18.72232 ? 48  LEU   A CD1 1 
ATOM   349  C  CD2 . LEU   A 1 41  ? -0.20872  -14.17822 -18.22768 1.000 16.80574 ? 48  LEU   A CD2 1 
ATOM   350  N  N   . ILE   A 1 42  ? -4.31922  -11.13863 -16.40034 1.000 14.34908 ? 49  ILE   A N   1 
ATOM   351  C  CA  . ILE   A 1 42  ? -5.55628  -10.39788 -16.61715 1.000 16.21747 ? 49  ILE   A CA  1 
ATOM   352  C  C   . ILE   A 1 42  ? -5.24588  -8.96551  -17.03489 1.000 17.70880 ? 49  ILE   A C   1 
ATOM   353  O  O   . ILE   A 1 42  ? -5.91650  -8.39349  -17.90578 1.000 17.28843 ? 49  ILE   A O   1 
ATOM   354  C  CB  . ILE   A 1 42  ? -6.43651  -10.46191 -15.35382 1.000 16.96185 ? 49  ILE   A CB  1 
ATOM   355  C  CG1 . ILE   A 1 42  ? -7.02656  -11.86906 -15.20561 1.000 15.12582 ? 49  ILE   A CG1 1 
ATOM   356  C  CG2 . ILE   A 1 42  ? -7.55274  -9.41503  -15.41252 1.000 21.89564 ? 49  ILE   A CG2 1 
ATOM   357  C  CD1 . ILE   A 1 42  ? -7.80772  -12.08659 -13.90949 1.000 20.13027 ? 49  ILE   A CD1 1 
ATOM   358  N  N   . SER   A 1 43  ? -4.19866  -8.37385  -16.45359 1.000 16.40767 ? 50  SER   A N   1 
ATOM   359  C  CA  . SER   A 1 43  ? -3.82625  -7.02160  -16.84432 1.000 19.52557 ? 50  SER   A CA  1 
ATOM   360  C  C   . SER   A 1 43  ? -3.33251  -6.99757  -18.28853 1.000 18.53238 ? 50  SER   A C   1 
ATOM   361  O  O   . SER   A 1 43  ? -3.66448  -6.08121  -19.04899 1.000 18.09049 ? 50  SER   A O   1 
ATOM   362  C  CB  . SER   A 1 43  ? -2.77452  -6.47389  -15.87328 1.000 24.21654 ? 50  SER   A CB  1 
ATOM   363  O  OG  . SER   A 1 43  ? -2.10687  -5.34696  -16.40979 1.000 28.97614 ? 50  SER   A OG  1 
ATOM   364  N  N   . ASN   A 1 44  ? -2.56630  -8.01565  -18.69350 1.000 17.11189 ? 51  ASN   A N   1 
ATOM   365  C  CA  . ASN   A 1 44  ? -2.16815  -8.13148  -20.09280 1.000 18.77581 ? 51  ASN   A CA  1 
ATOM   366  C  C   . ASN   A 1 44  ? -3.38576  -8.22523  -21.00083 1.000 19.18194 ? 51  ASN   A C   1 
ATOM   367  O  O   . ASN   A 1 44  ? -3.43381  -7.59016  -22.06105 1.000 17.38793 ? 51  ASN   A O   1 
ATOM   368  C  CB  . ASN   A 1 44  ? -1.29274  -9.36443  -20.29121 1.000 17.66530 ? 51  ASN   A CB  1 
ATOM   369  C  CG  . ASN   A 1 44  ? 0.10503   -9.15982  -19.80000 1.000 30.16959 ? 51  ASN   A CG  1 
ATOM   370  O  OD1 . ASN   A 1 44  ? 0.47822   -8.05862  -19.39695 1.000 22.18028 ? 51  ASN   A OD1 1 
ATOM   371  N  ND2 . ASN   A 1 44  ? 0.89284   -10.22443 -19.81959 1.000 26.08857 ? 51  ASN   A ND2 1 
ATOM   372  N  N   . SER   A 1 45  ? -4.37025  -9.03274  -20.60785 1.000 14.13869 ? 52  SER   A N   1 
ATOM   373  C  CA  . SER   A 1 45  ? -5.59413  -9.14576  -21.39764 1.000 15.50030 ? 52  SER   A CA  1 
ATOM   374  C  C   . SER   A 1 45  ? -6.30934  -7.80327  -21.49827 1.000 17.83662 ? 52  SER   A C   1 
ATOM   375  O  O   . SER   A 1 45  ? -6.76713  -7.40945  -22.57982 1.000 17.21348 ? 52  SER   A O   1 
ATOM   376  C  CB  . SER   A 1 45  ? -6.51786  -10.20511 -20.79536 1.000 14.40885 ? 52  SER   A CB  1 
ATOM   377  O  OG  . SER   A 1 45  ? -5.97418  -11.51048 -20.94487 1.000 18.34704 ? 52  SER   A OG  1 
ATOM   378  N  N   . SER   A 1 46  ? -6.42751  -7.09067  -20.37317 1.000 15.51557 ? 53  SER   A N   1 
ATOM   379  C  CA  . SER   A 1 46  ? -7.06086  -5.77492  -20.39375 1.000 19.43250 ? 53  SER   A CA  1 
ATOM   380  C  C   . SER   A 1 46  ? -6.32907  -4.82442  -21.33797 1.000 23.33462 ? 53  SER   A C   1 
ATOM   381  O  O   . SER   A 1 46  ? -6.96404  -4.06301  -22.08012 1.000 19.04919 ? 53  SER   A O   1 
ATOM   382  C  CB  . SER   A 1 46  ? -7.11108  -5.19893  -18.97761 1.000 18.35400 ? 53  SER   A CB  1 
ATOM   383  O  OG  . SER   A 1 46  ? -7.69770  -3.89844  -18.96523 1.000 20.38089 ? 53  SER   A OG  1 
ATOM   384  N  N   . ASP   A 1 47  ? -4.99197  -4.85458  -21.32181 1.000 18.60902 ? 54  ASP   A N   1 
ATOM   385  C  CA  . ASP   A 1 47  ? -4.21116  -4.01429  -22.22822 1.000 17.07890 ? 54  ASP   A CA  1 
ATOM   386  C  C   . ASP   A 1 47  ? -4.50618  -4.35252  -23.68542 1.000 23.13971 ? 54  ASP   A C   1 
ATOM   387  O  O   . ASP   A 1 47  ? -4.62808  -3.45471  -24.52506 1.000 18.89981 ? 54  ASP   A O   1 
ATOM   388  C  CB  . ASP   A 1 47  ? -2.71513  -4.17859  -21.94140 1.000 17.31487 ? 54  ASP   A CB  1 
ATOM   389  C  CG  . ASP   A 1 47  ? -2.26739  -3.45069  -20.67962 1.000 26.75302 ? 54  ASP   A CG  1 
ATOM   390  O  OD1 . ASP   A 1 47  ? -3.07503  -2.70636  -20.08425 1.000 25.52590 ? 54  ASP   A OD1 1 
ATOM   391  O  OD2 . ASP   A 1 47  ? -1.09731  -3.63369  -20.27451 1.000 25.08745 ? 54  ASP   A OD2 1 
ATOM   392  N  N   . ALA   A 1 48  ? -4.62555  -5.64774  -24.00132 1.000 16.63677 ? 55  ALA   A N   1 
ATOM   393  C  CA  . ALA   A 1 48  ? -4.90551  -6.06999  -25.37136 1.000 19.28352 ? 55  ALA   A CA  1 
ATOM   394  C  C   . ALA   A 1 48  ? -6.32009  -5.68974  -25.78540 1.000 16.91004 ? 55  ALA   A C   1 
ATOM   395  O  O   . ALA   A 1 48  ? -6.56666  -5.35988  -26.95014 1.000 16.24496 ? 55  ALA   A O   1 
ATOM   396  C  CB  . ALA   A 1 48  ? -4.69539  -7.58031  -25.50992 1.000 16.30527 ? 55  ALA   A CB  1 
ATOM   397  N  N   . LEU   A 1 49  ? -7.26665  -5.75058  -24.85043 1.000 17.12219 ? 56  LEU   A N   1 
ATOM   398  C  CA  . LEU   A 1 49  ? -8.62279  -5.30886  -25.15179 1.000 16.83645 ? 56  LEU   A CA  1 
ATOM   399  C  C   . LEU   A 1 49  ? -8.67766  -3.80136  -25.38105 1.000 20.67691 ? 56  LEU   A C   1 
ATOM   400  O  O   . LEU   A 1 49  ? -9.37101  -3.33818  -26.29497 1.000 18.03448 ? 56  LEU   A O   1 
ATOM   401  C  CB  . LEU   A 1 49  ? -9.56400  -5.73171  -24.02759 1.000 16.60326 ? 56  LEU   A CB  1 
ATOM   402  C  CG  . LEU   A 1 49  ? -9.76583  -7.25261  -24.02125 1.000 16.19447 ? 56  LEU   A CG  1 
ATOM   403  C  CD1 . LEU   A 1 49  ? -10.13215 -7.75864  -22.64122 1.000 17.04479 ? 56  LEU   A CD1 1 
ATOM   404  C  CD2 . LEU   A 1 49  ? -10.82952 -7.65386  -25.04514 1.000 19.30539 ? 56  LEU   A CD2 1 
ATOM   405  N  N   . ASP   A 1 50  ? -7.95497  -3.01882  -24.56550 1.000 16.00308 ? 57  ASP   A N   1 
ATOM   406  C  CA  . ASP   A 1 50  ? -7.86829  -1.57839  -24.80878 1.000 17.74276 ? 57  ASP   A CA  1 
ATOM   407  C  C   . ASP   A 1 50  ? -7.39397  -1.29012  -26.22732 1.000 22.69152 ? 57  ASP   A C   1 
ATOM   408  O  O   . ASP   A 1 50  ? -7.87496  -0.35172  -26.87437 1.000 18.61202 ? 57  ASP   A O   1 
ATOM   409  C  CB  . ASP   A 1 50  ? -6.90980  -0.90792  -23.81886 1.000 17.79919 ? 57  ASP   A CB  1 
ATOM   410  C  CG  . ASP   A 1 50  ? -7.41968  -0.89428  -22.38569 1.000 23.63062 ? 57  ASP   A CG  1 
ATOM   411  O  OD1 . ASP   A 1 50  ? -8.58996  -1.24744  -22.12640 1.000 22.26834 ? 57  ASP   A OD1 1 
ATOM   412  O  OD2 . ASP   A 1 50  ? -6.62607  -0.49286  -21.50901 1.000 23.68522 ? 57  ASP   A OD2 1 
ATOM   413  N  N   . LYS   A 1 51  ? -6.43348  -2.08200  -26.72048 1.000 17.01704 ? 58  LYS   A N   1 
ATOM   414  C  CA  . LYS   A 1 51  ? -5.83115  -1.80050  -28.01937 1.000 19.13017 ? 58  LYS   A CA  1 
ATOM   415  C  C   . LYS   A 1 51  ? -6.83354  -1.99614  -29.15060 1.000 18.22516 ? 58  LYS   A C   1 
ATOM   416  O  O   . LYS   A 1 51  ? -6.95021  -1.14699  -30.04385 1.000 21.69753 ? 58  LYS   A O   1 
ATOM   417  C  CB  . LYS   A 1 51  ? -4.60061  -2.68542  -28.22798 1.000 20.01826 ? 58  LYS   A CB  1 
ATOM   418  C  CG  . LYS   A 1 51  ? -3.37961  -2.23657  -27.43090 1.000 20.61619 ? 58  LYS   A CG  1 
ATOM   419  C  CD  . LYS   A 1 51  ? -2.20804  -3.19926  -27.62647 1.000 23.13476 ? 58  LYS   A CD  1 
ATOM   420  C  CE  . LYS   A 1 51  ? -1.20180  -3.09160  -26.48291 1.000 29.26027 ? 58  LYS   A CE  1 
ATOM   421  N  NZ  . LYS   A 1 51  ? -0.03258  -4.00391  -26.68667 1.000 35.71438 ? 58  LYS   A NZ  1 
ATOM   422  N  N   . ILE   A 1 52  ? -7.56571  -3.11168  -29.14022 1.000 18.10448 ? 59  ILE   A N   1 
ATOM   423  C  CA  . ILE   A 1 52  ? -8.53645  -3.32744  -30.21137 1.000 18.27298 ? 59  ILE   A CA  1 
ATOM   424  C  C   . ILE   A 1 52  ? -9.70019  -2.35113  -30.08324 1.000 19.49191 ? 59  ILE   A C   1 
ATOM   425  O  O   . ILE   A 1 52  ? -10.24472 -1.89403  -31.09690 1.000 19.98816 ? 59  ILE   A O   1 
ATOM   426  C  CB  . ILE   A 1 52  ? -9.00667  -4.79939  -30.24773 1.000 21.88241 ? 59  ILE   A CB  1 
ATOM   427  C  CG1 . ILE   A 1 52  ? -9.77401  -5.09526  -31.54606 1.000 22.39220 ? 59  ILE   A CG1 1 
ATOM   428  C  CG2 . ILE   A 1 52  ? -9.86168  -5.14288  -29.03497 1.000 20.90369 ? 59  ILE   A CG2 1 
ATOM   429  C  CD1 . ILE   A 1 52  ? -8.97994  -4.84204  -32.82659 1.000 22.98609 ? 59  ILE   A CD1 1 
ATOM   430  N  N   . ARG   A 1 53  ? -10.08905 -1.98239  -28.85768 1.000 18.73555 ? 60  ARG   A N   1 
ATOM   431  C  CA  . ARG   A 1 53  ? -11.14326 -0.97932  -28.72139 1.000 20.74492 ? 60  ARG   A CA  1 
ATOM   432  C  C   . ARG   A 1 53  ? -10.72022 0.35146   -29.32838 1.000 21.19966 ? 60  ARG   A C   1 
ATOM   433  O  O   . ARG   A 1 53  ? -11.48755 0.97819   -30.06947 1.000 19.84893 ? 60  ARG   A O   1 
ATOM   434  C  CB  . ARG   A 1 53  ? -11.54893 -0.78095  -27.26371 1.000 24.27234 ? 60  ARG   A CB  1 
ATOM   435  C  CG  . ARG   A 1 53  ? -12.84510 0.03244   -27.19171 1.000 38.13953 ? 60  ARG   A CG  1 
ATOM   436  C  CD  . ARG   A 1 53  ? -13.25932 0.38550   -25.78930 1.000 45.78559 ? 60  ARG   A CD  1 
ATOM   437  N  NE  . ARG   A 1 53  ? -14.26346 -0.52287  -25.25102 1.000 52.96882 ? 60  ARG   A NE  1 
ATOM   438  C  CZ  . ARG   A 1 53  ? -14.27678 -0.95411  -23.99861 1.000 58.20383 ? 60  ARG   A CZ  1 
ATOM   439  N  NH1 . ARG   A 1 53  ? -13.31417 -0.63186  -23.14944 1.000 39.19046 ? 60  ARG   A NH1 1 
ATOM   440  N  NH2 . ARG   A 1 53  ? -15.28578 -1.71709  -23.58541 1.000 34.99848 ? 60  ARG   A NH2 1 
ATOM   441  N  N   . TYR   A 1 54  ? -9.49625  0.79854   -29.03192 1.000 21.63716 ? 61  TYR   A N   1 
ATOM   442  C  CA  . TYR   A 1 54  ? -9.03493  2.06570   -29.59073 1.000 19.93636 ? 61  TYR   A CA  1 
ATOM   443  C  C   . TYR   A 1 54  ? -9.03040  2.02590   -31.11443 1.000 24.13848 ? 61  TYR   A C   1 
ATOM   444  O  O   . TYR   A 1 54  ? -9.45587  2.98496   -31.76883 1.000 24.01066 ? 61  TYR   A O   1 
ATOM   445  C  CB  . TYR   A 1 54  ? -7.63830  2.41283   -29.07406 1.000 20.62711 ? 61  TYR   A CB  1 
ATOM   446  C  CG  . TYR   A 1 54  ? -7.18400  3.76226   -29.57913 1.000 29.09742 ? 61  TYR   A CG  1 
ATOM   447  C  CD1 . TYR   A 1 54  ? -7.74942  4.93383   -29.08708 1.000 23.89056 ? 61  TYR   A CD1 1 
ATOM   448  C  CD2 . TYR   A 1 54  ? -6.24107  3.86436   -30.59047 1.000 25.23965 ? 61  TYR   A CD2 1 
ATOM   449  C  CE1 . TYR   A 1 54  ? -7.36346  6.16645   -29.56140 1.000 26.04513 ? 61  TYR   A CE1 1 
ATOM   450  C  CE2 . TYR   A 1 54  ? -5.84758  5.10017   -31.07685 1.000 32.52862 ? 61  TYR   A CE2 1 
ATOM   451  C  CZ  . TYR   A 1 54  ? -6.41148  6.24609   -30.55638 1.000 28.33442 ? 61  TYR   A CZ  1 
ATOM   452  O  OH  . TYR   A 1 54  ? -6.02854  7.47698   -31.03189 1.000 32.10670 ? 61  TYR   A OH  1 
ATOM   453  N  N   . GLU   A 1 55  ? -8.54582  0.92588   -31.69934 1.000 20.93379 ? 62  GLU   A N   1 
ATOM   454  C  CA  . GLU   A 1 55  ? -8.51648  0.81759   -33.15659 1.000 22.59485 ? 62  GLU   A CA  1 
ATOM   455  C  C   . GLU   A 1 55  ? -9.92212  0.86377   -33.74126 1.000 24.82193 ? 62  GLU   A C   1 
ATOM   456  O  O   . GLU   A 1 55  ? -10.14692 1.47044   -34.79601 1.000 27.18964 ? 62  GLU   A O   1 
ATOM   457  C  CB  . GLU   A 1 55  ? -7.80884  -0.47173  -33.57079 1.000 25.65095 ? 62  GLU   A CB  1 
ATOM   458  C  CG  . GLU   A 1 55  ? -6.30159  -0.42864  -33.38354 1.000 28.14349 ? 62  GLU   A CG  1 
ATOM   459  C  CD  . GLU   A 1 55  ? -5.58508  -1.48522  -34.20140 1.000 38.22271 ? 62  GLU   A CD  1 
ATOM   460  O  OE1 . GLU   A 1 55  ? -6.26466  -2.38959  -34.72948 1.000 36.00200 ? 62  GLU   A OE1 1 
ATOM   461  O  OE2 . GLU   A 1 55  ? -4.34207  -1.41814  -34.30800 1.000 39.18085 ? 62  GLU   A OE2 1 
ATOM   462  N  N   . SER   A 1 56  ? -10.88567 0.24141   -33.06101 1.000 24.47194 ? 63  SER   A N   1 
ATOM   463  C  CA  . SER   A 1 56  ? -12.25835 0.22241   -33.55355 1.000 24.13922 ? 63  SER   A CA  1 
ATOM   464  C  C   . SER   A 1 56  ? -12.92544 1.58760   -33.47408 1.000 28.81039 ? 63  SER   A C   1 
ATOM   465  O  O   . SER   A 1 56  ? -13.97066 1.78646   -34.10290 1.000 25.04204 ? 63  SER   A O   1 
ATOM   466  C  CB  . SER   A 1 56  ? -13.08570 -0.79029  -32.76602 1.000 24.59136 ? 63  SER   A CB  1 
ATOM   467  O  OG  . SER   A 1 56  ? -13.40565 -0.28687  -31.47788 1.000 27.26258 ? 63  SER   A OG  1 
ATOM   468  N  N   . LEU   A 1 57  ? -12.36006 2.52563   -32.70968 1.000 23.88771 ? 64  LEU   A N   1 
ATOM   469  C  CA  . LEU   A 1 57  ? -12.98049 3.84308   -32.59030 1.000 31.85847 ? 64  LEU   A CA  1 
ATOM   470  C  C   . LEU   A 1 57  ? -13.00597 4.57197   -33.92512 1.000 32.01567 ? 64  LEU   A C   1 
ATOM   471  O  O   . LEU   A 1 57  ? -13.93711 5.33820   -34.19827 1.000 32.90898 ? 64  LEU   A O   1 
ATOM   472  C  CB  . LEU   A 1 57  ? -12.24289 4.68206   -31.54645 1.000 29.17465 ? 64  LEU   A CB  1 
ATOM   473  C  CG  . LEU   A 1 57  ? -12.39674 4.21504   -30.09755 1.000 28.85201 ? 64  LEU   A CG  1 
ATOM   474  C  CD1 . LEU   A 1 57  ? -11.78985 5.23094   -29.14422 1.000 29.71232 ? 64  LEU   A CD1 1 
ATOM   475  C  CD2 . LEU   A 1 57  ? -13.85474 3.95398   -29.75476 1.000 30.80070 ? 64  LEU   A CD2 1 
ATOM   476  N  N   . THR   A 1 58  ? -11.99779 4.35363   -34.76427 1.000 29.81206 ? 65  THR   A N   1 
ATOM   477  C  CA  . THR   A 1 58  ? -11.93827 4.97717   -36.07688 1.000 32.37366 ? 65  THR   A CA  1 
ATOM   478  C  C   . THR   A 1 58  ? -12.19278 4.00667   -37.21914 1.000 39.98535 ? 65  THR   A C   1 
ATOM   479  O  O   . THR   A 1 58  ? -12.36928 4.45340   -38.35697 1.000 39.10542 ? 65  THR   A O   1 
ATOM   480  C  CB  . THR   A 1 58  ? -10.57489 5.65209   -36.28568 1.000 51.46468 ? 65  THR   A CB  1 
ATOM   481  O  OG1 . THR   A 1 58  ? -9.53227  4.67483   -36.17584 1.000 45.54051 ? 65  THR   A OG1 1 
ATOM   482  C  CG2 . THR   A 1 58  ? -10.35771 6.75045   -35.25374 1.000 34.98063 ? 65  THR   A CG2 1 
ATOM   483  N  N   . ASP   A 1 59  ? -12.21661 2.70166   -36.95369 1.000 37.09597 ? 66  ASP   A N   1 
ATOM   484  C  CA  . ASP   A 1 59  ? -12.45894 1.69781   -37.98778 1.000 36.39059 ? 66  ASP   A CA  1 
ATOM   485  C  C   . ASP   A 1 59  ? -13.29586 0.58067   -37.38062 1.000 30.17449 ? 66  ASP   A C   1 
ATOM   486  O  O   . ASP   A 1 59  ? -12.75892 -0.38829  -36.82813 1.000 28.12237 ? 66  ASP   A O   1 
ATOM   487  C  CB  . ASP   A 1 59  ? -11.14558 1.15827   -38.55646 1.000 33.64257 ? 66  ASP   A CB  1 
ATOM   488  C  CG  . ASP   A 1 59  ? -11.35917 0.15357   -39.67838 1.000 46.29689 ? 66  ASP   A CG  1 
ATOM   489  O  OD1 . ASP   A 1 59  ? -12.52522 -0.11369  -40.04276 1.000 40.18250 ? 66  ASP   A OD1 1 
ATOM   490  O  OD2 . ASP   A 1 59  ? -10.35392 -0.37175  -40.19830 1.000 40.12862 ? 66  ASP   A OD2 1 
ATOM   491  N  N   . PRO   A 1 60  ? -14.62368 0.66683   -37.49166 1.000 39.05385 ? 67  PRO   A N   1 
ATOM   492  C  CA  . PRO   A 1 60  ? -15.47705 -0.35350  -36.86155 1.000 30.97788 ? 67  PRO   A CA  1 
ATOM   493  C  C   . PRO   A 1 60  ? -15.26242 -1.74999  -37.41597 1.000 33.73513 ? 67  PRO   A C   1 
ATOM   494  O  O   . PRO   A 1 60  ? -15.54534 -2.72379  -36.70884 1.000 33.26839 ? 67  PRO   A O   1 
ATOM   495  C  CB  . PRO   A 1 60  ? -16.90289 0.14705   -37.13647 1.000 37.12290 ? 67  PRO   A CB  1 
ATOM   496  C  CG  . PRO   A 1 60  ? -16.77749 1.42883   -37.88720 1.000 58.51367 ? 67  PRO   A CG  1 
ATOM   497  C  CD  . PRO   A 1 60  ? -15.37629 1.58289   -38.36142 1.000 43.85026 ? 67  PRO   A CD  1 
ATOM   498  N  N   . SER   A 1 61  ? -14.76564 -1.88318  -38.65130 1.000 36.98758 ? 68  SER   A N   1 
ATOM   499  C  CA  . SER   A 1 61  ? -14.55736 -3.20838  -39.22353 1.000 31.31502 ? 68  SER   A CA  1 
ATOM   500  C  C   . SER   A 1 61  ? -13.49172 -3.99774  -38.47444 1.000 36.16971 ? 68  SER   A C   1 
ATOM   501  O  O   . SER   A 1 61  ? -13.40514 -5.21807  -38.65059 1.000 29.14781 ? 68  SER   A O   1 
ATOM   502  C  CB  . SER   A 1 61  ? -14.17896 -3.10027  -40.70169 1.000 34.87061 ? 68  SER   A CB  1 
ATOM   503  O  OG  . SER   A 1 61  ? -12.88361 -2.54780  -40.85622 1.000 35.60701 ? 68  SER   A OG  1 
ATOM   504  N  N   . LYS   A 1 62  ? -12.68347 -3.33353  -37.64165 1.000 25.72751 ? 69  LYS   A N   1 
ATOM   505  C  CA  . LYS   A 1 62  ? -11.72283 -4.04595  -36.80941 1.000 26.01543 ? 69  LYS   A CA  1 
ATOM   506  C  C   . LYS   A 1 62  ? -12.39538 -5.04572  -35.87975 1.000 27.68139 ? 69  LYS   A C   1 
ATOM   507  O  O   . LYS   A 1 62  ? -11.73714 -5.97873  -35.40664 1.000 24.80621 ? 69  LYS   A O   1 
ATOM   508  C  CB  . LYS   A 1 62  ? -10.90522 -3.04839  -35.98868 1.000 30.47015 ? 69  LYS   A CB  1 
ATOM   509  C  CG  . LYS   A 1 62  ? -10.04268 -2.12570  -36.83105 1.000 38.85091 ? 69  LYS   A CG  1 
ATOM   510  C  CD  . LYS   A 1 62  ? -8.60058  -2.58915  -36.83233 1.000 35.63648 ? 69  LYS   A CD  1 
ATOM   511  C  CE  . LYS   A 1 62  ? -7.75656  -1.80047  -37.81680 1.000 35.75774 ? 69  LYS   A CE  1 
ATOM   512  N  NZ  . LYS   A 1 62  ? -6.35526  -2.31205  -37.81516 1.000 39.24846 ? 69  LYS   A NZ  1 
ATOM   513  N  N   . LEU   A 1 63  ? -13.68486 -4.87173  -35.59754 1.000 24.55799 ? 70  LEU   A N   1 
ATOM   514  C  CA  . LEU   A 1 63  ? -14.41801 -5.80244  -34.75407 1.000 24.27844 ? 70  LEU   A CA  1 
ATOM   515  C  C   . LEU   A 1 63  ? -15.21961 -6.81691  -35.56126 1.000 26.68968 ? 70  LEU   A C   1 
ATOM   516  O  O   . LEU   A 1 63  ? -16.03563 -7.54331  -34.98457 1.000 29.90201 ? 70  LEU   A O   1 
ATOM   517  C  CB  . LEU   A 1 63  ? -15.34162 -5.03827  -33.80022 1.000 30.49941 ? 70  LEU   A CB  1 
ATOM   518  C  CG  . LEU   A 1 63  ? -14.64922 -4.07035  -32.83980 1.000 28.67130 ? 70  LEU   A CG  1 
ATOM   519  C  CD1 . LEU   A 1 63  ? -15.64355 -3.43492  -31.88407 1.000 32.32062 ? 70  LEU   A CD1 1 
ATOM   520  C  CD2 . LEU   A 1 63  ? -13.57118 -4.80954  -32.06323 1.000 27.25474 ? 70  LEU   A CD2 1 
ATOM   521  N  N   . ASP   A 1 64  ? -15.00375 -6.89328  -36.87742 1.000 26.16286 ? 71  ASP   A N   1 
ATOM   522  C  CA  . ASP   A 1 64  ? -15.69868 -7.90797  -37.66533 1.000 29.41865 ? 71  ASP   A CA  1 
ATOM   523  C  C   . ASP   A 1 64  ? -15.33188 -9.31119  -37.20391 1.000 29.72906 ? 71  ASP   A C   1 
ATOM   524  O  O   . ASP   A 1 64  ? -16.11990 -10.24738 -37.37594 1.000 32.28978 ? 71  ASP   A O   1 
ATOM   525  C  CB  . ASP   A 1 64  ? -15.38468 -7.73780  -39.15173 1.000 31.48933 ? 71  ASP   A CB  1 
ATOM   526  C  CG  . ASP   A 1 64  ? -16.06266 -6.52246  -39.75611 1.000 42.00939 ? 71  ASP   A CG  1 
ATOM   527  O  OD1 . ASP   A 1 64  ? -16.90826 -5.90691  -39.07231 1.000 43.13959 ? 71  ASP   A OD1 1 
ATOM   528  O  OD2 . ASP   A 1 64  ? -15.74937 -6.18611  -40.91670 1.000 43.08256 ? 71  ASP   A OD2 1 
ATOM   529  N  N   . SER   A 1 65  ? -14.14924 -9.46899  -36.61129 1.000 26.79223 ? 72  SER   A N   1 
ATOM   530  C  CA  . SER   A 1 65  ? -13.68014 -10.71996 -36.03095 1.000 27.68776 ? 72  SER   A CA  1 
ATOM   531  C  C   . SER   A 1 65  ? -14.24524 -10.97831 -34.63722 1.000 34.04226 ? 72  SER   A C   1 
ATOM   532  O  O   . SER   A 1 65  ? -13.81677 -11.93134 -33.97801 1.000 35.06633 ? 72  SER   A O   1 
ATOM   533  C  CB  . SER   A 1 65  ? -12.14982 -10.71491 -35.96654 1.000 30.45803 ? 72  SER   A CB  1 
ATOM   534  O  OG  . SER   A 1 65  ? -11.67760 -9.45720  -35.49435 1.000 24.14892 ? 72  SER   A OG  1 
ATOM   535  N  N   . GLY   A 1 66  ? -15.17802 -10.15103 -34.17054 1.000 28.39169 ? 73  GLY   A N   1 
ATOM   536  C  CA  . GLY   A 1 66  ? -15.77864 -10.33837 -32.86577 1.000 34.52241 ? 73  GLY   A CA  1 
ATOM   537  C  C   . GLY   A 1 66  ? -16.04026 -9.02899  -32.15070 1.000 31.38963 ? 73  GLY   A C   1 
ATOM   538  O  O   . GLY   A 1 66  ? -15.10269 -8.28616  -31.85443 1.000 25.26330 ? 73  GLY   A O   1 
ATOM   539  N  N   . LYS   A 1 67  ? -17.31024 -8.73307  -31.86384 1.000 29.82289 ? 74  LYS   A N   1 
ATOM   540  C  CA  . LYS   A 1 67  ? -17.65220 -7.46830  -31.21961 1.000 25.29483 ? 74  LYS   A CA  1 
ATOM   541  C  C   . LYS   A 1 67  ? -17.46615 -7.51420  -29.70659 1.000 26.99870 ? 74  LYS   A C   1 
ATOM   542  O  O   . LYS   A 1 67  ? -17.23265 -6.47014  -29.08720 1.000 31.50236 ? 74  LYS   A O   1 
ATOM   543  C  CB  . LYS   A 1 67  ? -19.10110 -7.08202  -31.54505 1.000 28.07370 ? 74  LYS   A CB  1 
ATOM   544  C  CG  . LYS   A 1 67  ? -19.41260 -6.95655  -33.02840 1.000 48.00899 ? 74  LYS   A CG  1 
ATOM   545  C  CD  . LYS   A 1 67  ? -20.12824 -5.64845  -33.34257 1.000 68.65332 ? 74  LYS   A CD  1 
ATOM   546  C  CE  . LYS   A 1 67  ? -20.09768 -5.33930  -34.83276 1.000 64.99005 ? 74  LYS   A CE  1 
ATOM   547  N  NZ  . LYS   A 1 67  ? -18.99867 -4.40011  -35.19672 1.000 69.91292 ? 74  LYS   A NZ  1 
ATOM   548  N  N   . GLU   A 1 68  ? -17.56821 -8.69293  -29.09521 1.000 24.14743 ? 75  GLU   A N   1 
ATOM   549  C  CA  . GLU   A 1 68  ? -17.51634 -8.80016  -27.64123 1.000 25.76299 ? 75  GLU   A CA  1 
ATOM   550  C  C   . GLU   A 1 68  ? -16.08521 -8.65339  -27.13265 1.000 24.06222 ? 75  GLU   A C   1 
ATOM   551  O  O   . GLU   A 1 68  ? -15.16769 -9.30442  -27.63755 1.000 28.16451 ? 75  GLU   A O   1 
ATOM   552  C  CB  . GLU   A 1 68  ? -18.09007 -10.13988 -27.18002 1.000 32.89734 ? 75  GLU   A CB  1 
ATOM   553  C  CG  . GLU   A 1 68  ? -19.60932 -10.22768 -27.20273 1.000 42.74725 ? 75  GLU   A CG  1 
ATOM   554  C  CD  . GLU   A 1 68  ? -20.17312 -10.27088 -28.61008 1.000 82.35450 ? 75  GLU   A CD  1 
ATOM   555  O  OE1 . GLU   A 1 68  ? -19.80784 -11.19641 -29.36605 1.000 77.71707 ? 75  GLU   A OE1 1 
ATOM   556  O  OE2 . GLU   A 1 68  ? -20.98542 -9.38545  -28.95783 1.000 80.39396 ? 75  GLU   A OE2 1 
ATOM   557  N  N   . LEU   A 1 69  ? -15.90790 -7.81620  -26.11361 1.000 21.19221 ? 76  LEU   A N   1 
ATOM   558  C  CA  . LEU   A 1 69  ? -14.61098 -7.55588  -25.49162 1.000 19.28212 ? 76  LEU   A CA  1 
ATOM   559  C  C   . LEU   A 1 69  ? -14.67187 -8.08741  -24.06150 1.000 18.90886 ? 76  LEU   A C   1 
ATOM   560  O  O   . LEU   A 1 69  ? -15.31978 -7.48010  -23.19850 1.000 19.78301 ? 76  LEU   A O   1 
ATOM   561  C  CB  . LEU   A 1 69  ? -14.30958 -6.05785  -25.51904 1.000 23.67051 ? 76  LEU   A CB  1 
ATOM   562  C  CG  . LEU   A 1 69  ? -14.13890 -5.41875  -26.90505 1.000 28.72799 ? 76  LEU   A CG  1 
ATOM   563  C  CD1 . LEU   A 1 69  ? -13.64337 -3.98539  -26.77696 1.000 32.69133 ? 76  LEU   A CD1 1 
ATOM   564  C  CD2 . LEU   A 1 69  ? -13.19720 -6.22601  -27.78719 1.000 23.60395 ? 76  LEU   A CD2 1 
ATOM   565  N  N   . HIS   A 1 70  ? -14.01362 -9.22019  -23.80636 1.000 18.84805 ? 77  HIS   A N   1 
ATOM   566  C  CA  . HIS   A 1 70  ? -14.19104 -9.89653  -22.52645 1.000 19.68009 ? 77  HIS   A CA  1 
ATOM   567  C  C   . HIS   A 1 70  ? -12.99097 -10.77766 -22.20681 1.000 17.66469 ? 77  HIS   A C   1 
ATOM   568  O  O   . HIS   A 1 70  ? -12.11333 -11.01036 -23.04219 1.000 15.31400 ? 77  HIS   A O   1 
ATOM   569  C  CB  . HIS   A 1 70  ? -15.48169 -10.72413 -22.52398 1.000 20.81660 ? 77  HIS   A CB  1 
ATOM   570  C  CG  . HIS   A 1 70  ? -15.48206 -11.85587 -23.50709 1.000 22.29772 ? 77  HIS   A CG  1 
ATOM   571  N  ND1 . HIS   A 1 70  ? -16.48274 -12.02046 -24.43876 1.000 31.13624 ? 77  HIS   A ND1 1 
ATOM   572  C  CD2 . HIS   A 1 70  ? -14.62915 -12.89242 -23.68655 1.000 26.71000 ? 77  HIS   A CD2 1 
ATOM   573  C  CE1 . HIS   A 1 70  ? -16.23363 -13.09311 -25.16811 1.000 27.67386 ? 77  HIS   A CE1 1 
ATOM   574  N  NE2 . HIS   A 1 70  ? -15.11600 -13.64309 -24.72968 1.000 27.34245 ? 77  HIS   A NE2 1 
ATOM   575  N  N   . ILE   A 1 71  ? -12.98313 -11.26607 -20.96714 1.000 15.93209 ? 78  ILE   A N   1 
ATOM   576  C  CA  . ILE   A 1 71  ? -11.95511 -12.14872 -20.43110 1.000 14.49304 ? 78  ILE   A CA  1 
ATOM   577  C  C   . ILE   A 1 71  ? -12.64531 -13.34967 -19.80201 1.000 19.27333 ? 78  ILE   A C   1 
ATOM   578  O  O   . ILE   A 1 71  ? -13.51714 -13.18077 -18.94223 1.000 16.84622 ? 78  ILE   A O   1 
ATOM   579  C  CB  . ILE   A 1 71  ? -11.08709 -11.44312 -19.37205 1.000 18.16107 ? 78  ILE   A CB  1 
ATOM   580  C  CG1 . ILE   A 1 71  ? -10.48895 -10.14605 -19.92820 1.000 18.27799 ? 78  ILE   A CG1 1 
ATOM   581  C  CG2 . ILE   A 1 71  ? -10.03205 -12.41798 -18.84278 1.000 19.41599 ? 78  ILE   A CG2 1 
ATOM   582  C  CD1 . ILE   A 1 71  ? -9.68678  -9.33860  -18.89298 1.000 17.63342 ? 78  ILE   A CD1 1 
ATOM   583  N  N   . ASN   A 1 72  ? -12.24863 -14.55662 -20.21024 1.000 17.04896 ? 79  ASN   A N   1 
ATOM   584  C  CA  . ASN   A 1 72  ? -12.76501 -15.78383 -19.61774 1.000 15.83170 ? 79  ASN   A CA  1 
ATOM   585  C  C   . ASN   A 1 72  ? -11.65014 -16.53655 -18.90381 1.000 19.48854 ? 79  ASN   A C   1 
ATOM   586  O  O   . ASN   A 1 72  ? -10.52905 -16.64227 -19.41578 1.000 17.37384 ? 79  ASN   A O   1 
ATOM   587  C  CB  . ASN   A 1 72  ? -13.40819 -16.69843 -20.67311 1.000 15.46405 ? 79  ASN   A CB  1 
ATOM   588  C  CG  . ASN   A 1 72  ? -14.61549 -16.07331 -21.33059 1.000 22.40979 ? 79  ASN   A CG  1 
ATOM   589  O  OD1 . ASN   A 1 72  ? -15.33738 -15.29392 -20.70807 1.000 20.76311 ? 79  ASN   A OD1 1 
ATOM   590  N  ND2 . ASN   A 1 72  ? -14.86306 -16.43462 -22.58648 1.000 23.04151 ? 79  ASN   A ND2 1 
ATOM   591  N  N   . LEU   A 1 73  ? -11.97482 -17.07830 -17.73333 1.000 15.97584 ? 80  LEU   A N   1 
ATOM   592  C  CA  . LEU   A 1 73  ? -11.06817 -17.91894 -16.96264 1.000 14.14373 ? 80  LEU   A CA  1 
ATOM   593  C  C   . LEU   A 1 73  ? -11.63391 -19.32938 -16.94828 1.000 17.65375 ? 80  LEU   A C   1 
ATOM   594  O  O   . LEU   A 1 73  ? -12.74140 -19.55319 -16.44876 1.000 15.65370 ? 80  LEU   A O   1 
ATOM   595  C  CB  . LEU   A 1 73  ? -10.91571 -17.39601 -15.53676 1.000 15.82353 ? 80  LEU   A CB  1 
ATOM   596  C  CG  . LEU   A 1 73  ? -10.53558 -15.92339 -15.40329 1.000 18.77594 ? 80  LEU   A CG  1 
ATOM   597  C  CD1 . LEU   A 1 73  ? -10.48235 -15.52019 -13.93401 1.000 18.64141 ? 80  LEU   A CD1 1 
ATOM   598  C  CD2 . LEU   A 1 73  ? -9.21439  -15.65908 -16.09797 1.000 17.49182 ? 80  LEU   A CD2 1 
ATOM   599  N  N   . ILE   A 1 74  ? -10.87421 -20.27623 -17.47998 1.000 15.56216 ? 81  ILE   A N   1 
ATOM   600  C  CA  . ILE   A 1 74  ? -11.38836 -21.62437 -17.68163 1.000 16.38977 ? 81  ILE   A CA  1 
ATOM   601  C  C   . ILE   A 1 74  ? -10.50043 -22.65005 -16.98943 1.000 18.18806 ? 81  ILE   A C   1 
ATOM   602  O  O   . ILE   A 1 74  ? -9.47535  -23.06321 -17.54706 1.000 17.80028 ? 81  ILE   A O   1 
ATOM   603  C  CB  . ILE   A 1 74  ? -11.53479 -21.94505 -19.17612 1.000 16.92350 ? 81  ILE   A CB  1 
ATOM   604  C  CG1 . ILE   A 1 74  ? -12.29313 -20.81372 -19.88477 1.000 18.26415 ? 81  ILE   A CG1 1 
ATOM   605  C  CG2 . ILE   A 1 74  ? -12.23422 -23.28106 -19.35136 1.000 17.34286 ? 81  ILE   A CG2 1 
ATOM   606  C  CD1 . ILE   A 1 74  ? -12.43550 -20.98527 -21.37976 1.000 21.06938 ? 81  ILE   A CD1 1 
ATOM   607  N  N   . PRO   A 1 75  ? -10.85299 -23.08647 -15.78466 1.000 21.38638 ? 82  PRO   A N   1 
ATOM   608  C  CA  . PRO   A 1 75  ? -10.10251 -24.16581 -15.14636 1.000 19.11220 ? 82  PRO   A CA  1 
ATOM   609  C  C   . PRO   A 1 75  ? -10.55819 -25.51816 -15.66454 1.000 18.91286 ? 82  PRO   A C   1 
ATOM   610  O  O   . PRO   A 1 75  ? -11.73363 -25.73432 -15.97342 1.000 20.62323 ? 82  PRO   A O   1 
ATOM   611  C  CB  . PRO   A 1 75  ? -10.44249 -23.99643 -13.66083 1.000 23.04003 ? 82  PRO   A CB  1 
ATOM   612  C  CG  . PRO   A 1 75  ? -11.82951 -23.43168 -13.66674 1.000 24.36156 ? 82  PRO   A CG  1 
ATOM   613  C  CD  . PRO   A 1 75  ? -12.02175 -22.67898 -14.98185 1.000 23.78006 ? 82  PRO   A CD  1 
ATOM   614  N  N   . ASN   A 1 76  ? -9.60186  -26.43781 -15.75949 1.000 19.40226 ? 83  ASN   A N   1 
ATOM   615  C  CA  . ASN   A 1 76  ? -9.88865  -27.80782 -16.18760 1.000 21.39662 ? 83  ASN   A CA  1 
ATOM   616  C  C   . ASN   A 1 76  ? -9.05986  -28.74277 -15.31480 1.000 21.96149 ? 83  ASN   A C   1 
ATOM   617  O  O   . ASN   A 1 76  ? -7.85159  -28.87569 -15.51957 1.000 24.46057 ? 83  ASN   A O   1 
ATOM   618  C  CB  . ASN   A 1 76  ? -9.58074  -28.00544 -17.66563 1.000 22.64419 ? 83  ASN   A CB  1 
ATOM   619  C  CG  . ASN   A 1 76  ? -10.07750 -29.33994 -18.18848 1.000 33.34969 ? 83  ASN   A CG  1 
ATOM   620  O  OD1 . ASN   A 1 76  ? -9.84593  -30.38763 -17.58081 1.000 32.07494 ? 83  ASN   A OD1 1 
ATOM   621  N  ND2 . ASN   A 1 76  ? -10.78003 -29.30524 -19.31246 1.000 35.25697 ? 83  ASN   A ND2 1 
ATOM   622  N  N   . LYS   A 1 77  ? -9.71530  -29.39698 -14.35152 1.000 25.02158 ? 84  LYS   A N   1 
ATOM   623  C  CA  . LYS   A 1 77  ? -8.98604  -30.23489 -13.40461 1.000 26.11968 ? 84  LYS   A CA  1 
ATOM   624  C  C   . LYS   A 1 77  ? -8.50339  -31.53007 -14.04220 1.000 30.30992 ? 84  LYS   A C   1 
ATOM   625  O  O   . LYS   A 1 77  ? -7.50578  -32.10072 -13.59070 1.000 29.68588 ? 84  LYS   A O   1 
ATOM   626  C  CB  . LYS   A 1 77  ? -9.85741  -30.55506 -12.19146 1.000 27.69029 ? 84  LYS   A CB  1 
ATOM   627  C  CG  . LYS   A 1 77  ? -10.04694 -29.39581 -11.22391 1.000 35.61414 ? 84  LYS   A CG  1 
ATOM   628  C  CD  . LYS   A 1 77  ? -10.90759 -29.82326 -10.04118 1.000 35.46879 ? 84  LYS   A CD  1 
ATOM   629  C  CE  . LYS   A 1 77  ? -11.17802 -28.67120 -9.08953  1.000 38.46609 ? 84  LYS   A CE  1 
ATOM   630  N  NZ  . LYS   A 1 77  ? -11.90068 -27.56694 -9.77825  1.000 40.90904 ? 84  LYS   A NZ  1 
ATOM   631  N  N   . GLN   A 1 78  ? -9.19423  -32.01425 -15.07680 1.000 31.11383 ? 85  GLN   A N   1 
ATOM   632  C  CA  . GLN   A 1 78  ? -8.77827  -33.25951 -15.71786 1.000 36.26320 ? 85  GLN   A CA  1 
ATOM   633  C  C   . GLN   A 1 78  ? -7.48837  -33.06838 -16.50297 1.000 38.40446 ? 85  GLN   A C   1 
ATOM   634  O  O   . GLN   A 1 78  ? -6.61299  -33.93943 -16.48992 1.000 35.75511 ? 85  GLN   A O   1 
ATOM   635  C  CB  . GLN   A 1 78  ? -9.88504  -33.79258 -16.62861 1.000 38.31756 ? 85  GLN   A CB  1 
ATOM   636  C  CG  . GLN   A 1 78  ? -11.12996 -34.30774 -15.90363 1.000 60.12019 ? 85  GLN   A CG  1 
ATOM   637  C  CD  . GLN   A 1 78  ? -11.85432 -33.23163 -15.11380 1.000 67.82836 ? 85  GLN   A CD  1 
ATOM   638  O  OE1 . GLN   A 1 78  ? -11.96587 -32.08634 -15.55556 1.000 72.88928 ? 85  GLN   A OE1 1 
ATOM   639  N  NE2 . GLN   A 1 78  ? -12.33641 -33.59307 -13.92787 1.000 57.86885 ? 85  GLN   A NE2 1 
ATOM   640  N  N   . ASP   A 1 79  ? -7.35794  -31.93974 -17.19094 1.000 27.34998 ? 86  ASP   A N   1 
ATOM   641  C  CA  . ASP   A 1 79  ? -6.14708  -31.58786 -17.91797 1.000 34.13072 ? 86  ASP   A CA  1 
ATOM   642  C  C   . ASP   A 1 79  ? -5.11879  -30.88752 -17.04268 1.000 22.94172 ? 86  ASP   A C   1 
ATOM   643  O  O   . ASP   A 1 79  ? -3.96621  -30.74651 -17.46457 1.000 27.64999 ? 86  ASP   A O   1 
ATOM   644  C  CB  . ASP   A 1 79  ? -6.48796  -30.67707 -19.10068 1.000 34.83140 ? 86  ASP   A CB  1 
ATOM   645  C  CG  . ASP   A 1 79  ? -7.40013  -31.34257 -20.10820 1.000 53.61761 ? 86  ASP   A CG  1 
ATOM   646  O  OD1 . ASP   A 1 79  ? -7.61233  -32.57112 -20.01188 1.000 44.57758 ? 86  ASP   A OD1 1 
ATOM   647  O  OD2 . ASP   A 1 79  ? -7.91183  -30.62620 -20.99395 1.000 41.46746 ? 86  ASP   A OD2 1 
ATOM   648  N  N   . ARG   A 1 80  ? -5.51743  -30.46351 -15.84390 1.000 24.60307 ? 87  ARG   A N   1 
ATOM   649  C  CA  . ARG   A 1 80  ? -4.70805  -29.63605 -14.94823 1.000 21.03497 ? 87  ARG   A CA  1 
ATOM   650  C  C   . ARG   A 1 80  ? -4.22644  -28.36981 -15.65245 1.000 22.44844 ? 87  ARG   A C   1 
ATOM   651  O  O   . ARG   A 1 80  ? -3.04075  -28.02533 -15.63937 1.000 21.83956 ? 87  ARG   A O   1 
ATOM   652  C  CB  . ARG   A 1 80  ? -3.53589  -30.42373 -14.35609 1.000 24.87718 ? 87  ARG   A CB  1 
ATOM   653  C  CG  . ARG   A 1 80  ? -3.16368  -29.92848 -12.96729 1.000 26.53870 ? 87  ARG   A CG  1 
ATOM   654  C  CD  . ARG   A 1 80  ? -1.70344  -30.12278 -12.61772 1.000 39.00006 ? 87  ARG   A CD  1 
ATOM   655  N  NE  . ARG   A 1 80  ? -1.35699  -31.52392 -12.43485 1.000 50.80529 ? 87  ARG   A NE  1 
ATOM   656  C  CZ  . ARG   A 1 80  ? -0.17355  -32.04585 -12.72480 1.000 52.23398 ? 87  ARG   A CZ  1 
ATOM   657  N  NH1 . ARG   A 1 80  ? 0.81357   -31.30324 -13.19695 1.000 40.24168 ? 87  ARG   A NH1 1 
ATOM   658  N  NH2 . ARG   A 1 80  ? 0.02976   -33.34343 -12.52138 1.000 53.75073 ? 87  ARG   A NH2 1 
ATOM   659  N  N   . THR   A 1 81  ? -5.16876  -27.66226 -16.26826 1.000 18.73202 ? 88  THR   A N   1 
ATOM   660  C  CA  . THR   A 1 81  ? -4.86381  -26.42281 -16.96563 1.000 20.64678 ? 88  THR   A CA  1 
ATOM   661  C  C   . THR   A 1 81  ? -5.76874  -25.30555 -16.48124 1.000 20.20719 ? 88  THR   A C   1 
ATOM   662  O  O   . THR   A 1 81  ? -6.94069  -25.52708 -16.16861 1.000 21.29775 ? 88  THR   A O   1 
ATOM   663  C  CB  . THR   A 1 81  ? -5.01273  -26.54808 -18.49163 1.000 22.25848 ? 88  THR   A CB  1 
ATOM   664  O  OG1 . THR   A 1 81  ? -6.34539  -26.97212 -18.81495 1.000 21.20452 ? 88  THR   A OG1 1 
ATOM   665  C  CG2 . THR   A 1 81  ? -3.98987  -27.52253 -19.06070 1.000 22.12419 ? 88  THR   A CG2 1 
ATOM   666  N  N   . LEU   A 1 82  ? -5.20763  -24.10576 -16.41723 1.000 17.99441 ? 89  LEU   A N   1 
ATOM   667  C  CA  . LEU   A 1 82  ? -5.97781  -22.88123 -16.26400 1.000 17.37094 ? 89  LEU   A CA  1 
ATOM   668  C  C   . LEU   A 1 82  ? -5.77694  -22.06065 -17.52999 1.000 16.53090 ? 89  LEU   A C   1 
ATOM   669  O  O   . LEU   A 1 82  ? -4.63934  -21.76045 -17.90266 1.000 19.90001 ? 89  LEU   A O   1 
ATOM   670  C  CB  . LEU   A 1 82  ? -5.54185  -22.10060 -15.02315 1.000 18.12838 ? 89  LEU   A CB  1 
ATOM   671  C  CG  . LEU   A 1 82  ? -6.29697  -20.78106 -14.84125 1.000 15.27173 ? 89  LEU   A CG  1 
ATOM   672  C  CD1 . LEU   A 1 82  ? -7.77006  -21.05236 -14.66490 1.000 19.03718 ? 89  LEU   A CD1 1 
ATOM   673  C  CD2 . LEU   A 1 82  ? -5.74764  -20.03435 -13.63105 1.000 16.44268 ? 89  LEU   A CD2 1 
ATOM   674  N  N   . THR   A 1 83  ? -6.87011  -21.72948 -18.20572 1.000 15.85534 ? 90  THR   A N   1 
ATOM   675  C  CA  . THR   A 1 83  ? -6.81296  -20.99758 -19.46107 1.000 17.28859 ? 90  THR   A CA  1 
ATOM   676  C  C   . THR   A 1 83  ? -7.40644  -19.60828 -19.26684 1.000 20.02043 ? 90  THR   A C   1 
ATOM   677  O  O   . THR   A 1 83  ? -8.51682  -19.47209 -18.73873 1.000 19.44115 ? 90  THR   A O   1 
ATOM   678  C  CB  . THR   A 1 83  ? -7.55816  -21.74002 -20.57199 1.000 19.53535 ? 90  THR   A CB  1 
ATOM   679  O  OG1 . THR   A 1 83  ? -6.97038  -23.03130 -20.78405 1.000 19.57183 ? 90  THR   A OG1 1 
ATOM   680  C  CG2 . THR   A 1 83  ? -7.47398  -20.95688 -21.85112 1.000 22.11278 ? 90  THR   A CG2 1 
ATOM   681  N  N   . ILE   A 1 84  ? -6.66088  -18.58454 -19.68130 1.000 14.60736 ? 91  ILE   A N   1 
ATOM   682  C  CA  . ILE   A 1 84  ? -7.11214  -17.19517 -19.64896 1.000 15.89617 ? 91  ILE   A CA  1 
ATOM   683  C  C   . ILE   A 1 84  ? -7.34861  -16.76533 -21.09188 1.000 20.00125 ? 91  ILE   A C   1 
ATOM   684  O  O   . ILE   A 1 84  ? -6.39618  -16.65032 -21.87429 1.000 20.55848 ? 91  ILE   A O   1 
ATOM   685  C  CB  . ILE   A 1 84  ? -6.09436  -16.27217 -18.96067 1.000 20.43743 ? 91  ILE   A CB  1 
ATOM   686  C  CG1 . ILE   A 1 84  ? -5.92115  -16.65292 -17.48772 1.000 27.07346 ? 91  ILE   A CG1 1 
ATOM   687  C  CG2 . ILE   A 1 84  ? -6.53502  -14.81970 -19.07941 1.000 17.17240 ? 91  ILE   A CG2 1 
ATOM   688  C  CD1 . ILE   A 1 84  ? -4.76673  -17.58844 -17.22112 1.000 32.34443 ? 91  ILE   A CD1 1 
ATOM   689  N  N   . VAL   A 1 85  ? -8.60986  -16.52273 -21.44962 1.000 15.16702 ? 92  VAL   A N   1 
ATOM   690  C  CA  . VAL   A 1 85  ? -8.99619  -16.15164 -22.80542 1.000 16.54920 ? 92  VAL   A CA  1 
ATOM   691  C  C   . VAL   A 1 85  ? -9.40612  -14.69014 -22.82184 1.000 22.33142 ? 92  VAL   A C   1 
ATOM   692  O  O   . VAL   A 1 85  ? -10.14415 -14.23681 -21.94276 1.000 19.26285 ? 92  VAL   A O   1 
ATOM   693  C  CB  . VAL   A 1 85  ? -10.16147 -17.00940 -23.33973 1.000 21.72071 ? 92  VAL   A CB  1 
ATOM   694  C  CG1 . VAL   A 1 85  ? -10.32794 -16.79800 -24.84132 1.000 21.09173 ? 92  VAL   A CG1 1 
ATOM   695  C  CG2 . VAL   A 1 85  ? -9.95434  -18.47913 -23.01192 1.000 22.75936 ? 92  VAL   A CG2 1 
ATOM   696  N  N   A ASP   A 1 86  ? -8.93950  -13.95684 -23.82993 0.500 17.42448 ? 93  ASP   A N   1 
ATOM   697  N  N   B ASP   A 1 86  ? -8.93950  -13.95684 -23.82993 0.500 17.42448 ? 93  ASP   A N   1 
ATOM   698  C  CA  A ASP   A 1 86  ? -9.42193  -12.60468 -24.07290 0.500 17.52318 ? 93  ASP   A CA  1 
ATOM   699  C  CA  B ASP   A 1 86  ? -9.42193  -12.60468 -24.07290 0.500 17.52318 ? 93  ASP   A CA  1 
ATOM   700  C  C   A ASP   A 1 86  ? -9.66316  -12.42589 -25.56452 0.500 22.27916 ? 93  ASP   A C   1 
ATOM   701  C  C   B ASP   A 1 86  ? -9.66316  -12.42589 -25.56452 0.500 22.27916 ? 93  ASP   A C   1 
ATOM   702  O  O   A ASP   A 1 86  ? -9.09723  -13.13879 -26.39995 0.500 19.22651 ? 93  ASP   A O   1 
ATOM   703  O  O   B ASP   A 1 86  ? -9.09723  -13.13879 -26.39995 0.500 19.22651 ? 93  ASP   A O   1 
ATOM   704  C  CB  A ASP   A 1 86  ? -8.44621  -11.54539 -23.52083 0.500 17.45590 ? 93  ASP   A CB  1 
ATOM   705  C  CB  B ASP   A 1 86  ? -8.44621  -11.54539 -23.52083 0.500 17.45590 ? 93  ASP   A CB  1 
ATOM   706  C  CG  A ASP   A 1 86  ? -7.14109  -11.46789 -24.30379 0.500 23.37654 ? 93  ASP   A CG  1 
ATOM   707  C  CG  B ASP   A 1 86  ? -7.14109  -11.46789 -24.30379 0.500 23.37654 ? 93  ASP   A CG  1 
ATOM   708  O  OD1 A ASP   A 1 86  ? -7.15566  -11.06374 -25.48896 0.500 22.29594 ? 93  ASP   A OD1 1 
ATOM   709  O  OD1 B ASP   A 1 86  ? -7.15566  -11.06374 -25.48896 0.500 22.29594 ? 93  ASP   A OD1 1 
ATOM   710  O  OD2 A ASP   A 1 86  ? -6.08786  -11.80558 -23.72007 0.500 22.77516 ? 93  ASP   A OD2 1 
ATOM   711  O  OD2 B ASP   A 1 86  ? -6.08786  -11.80558 -23.72007 0.500 22.77516 ? 93  ASP   A OD2 1 
ATOM   712  N  N   . THR   A 1 87  ? -10.53615 -11.47717 -25.89146 1.000 16.61007 ? 94  THR   A N   1 
ATOM   713  C  CA  . THR   A 1 87  ? -10.82989 -11.13725 -27.27959 1.000 14.76819 ? 94  THR   A CA  1 
ATOM   714  C  C   . THR   A 1 87  ? -10.16308 -9.82311  -27.66232 1.000 21.81518 ? 94  THR   A C   1 
ATOM   715  O  O   . THR   A 1 87  ? -10.74595 -8.99361  -28.35891 1.000 18.44046 ? 94  THR   A O   1 
ATOM   716  C  CB  . THR   A 1 87  ? -12.33730 -11.07394 -27.51106 1.000 19.52622 ? 94  THR   A CB  1 
ATOM   717  O  OG1 . THR   A 1 87  ? -12.94788 -10.26117 -26.50576 1.000 18.69962 ? 94  THR   A OG1 1 
ATOM   718  C  CG2 . THR   A 1 87  ? -12.93163 -12.47867 -27.43333 1.000 20.36821 ? 94  THR   A CG2 1 
ATOM   719  N  N   . GLY   A 1 88  ? -8.93560  -9.60827  -27.19094 1.000 19.77037 ? 95  GLY   A N   1 
ATOM   720  C  CA  . GLY   A 1 88  ? -8.20613  -8.39315  -27.48418 1.000 19.41985 ? 95  GLY   A CA  1 
ATOM   721  C  C   . GLY   A 1 88  ? -7.60951  -8.39943  -28.87827 1.000 15.50864 ? 95  GLY   A C   1 
ATOM   722  O  O   . GLY   A 1 88  ? -8.00680  -9.16837  -29.75992 1.000 18.84411 ? 95  GLY   A O   1 
ATOM   723  N  N   . ILE   A 1 89  ? -6.61764  -7.52357  -29.07039 1.000 17.70859 ? 96  ILE   A N   1 
ATOM   724  C  CA  . ILE   A 1 89  ? -6.06410  -7.31085  -30.40456 1.000 17.32324 ? 96  ILE   A CA  1 
ATOM   725  C  C   . ILE   A 1 89  ? -5.28882  -8.52504  -30.90773 1.000 20.98727 ? 96  ILE   A C   1 
ATOM   726  O  O   . ILE   A 1 89  ? -5.11663  -8.68533  -32.12231 1.000 19.74361 ? 96  ILE   A O   1 
ATOM   727  C  CB  . ILE   A 1 89  ? -5.19862  -6.03340  -30.40446 1.000 18.52420 ? 96  ILE   A CB  1 
ATOM   728  C  CG1 . ILE   A 1 89  ? -4.94573  -5.53693  -31.83038 1.000 21.58487 ? 96  ILE   A CG1 1 
ATOM   729  C  CG2 . ILE   A 1 89  ? -3.89467  -6.25098  -29.62855 1.000 17.14437 ? 96  ILE   A CG2 1 
ATOM   730  C  CD1 . ILE   A 1 89  ? -4.47612  -4.09518  -31.88023 1.000 22.91020 ? 96  ILE   A CD1 1 
ATOM   731  N  N   . GLY   A 1 90  ? -4.84785  -9.40818  -30.01776 1.000 19.23335 ? 97  GLY   A N   1 
ATOM   732  C  CA  . GLY   A 1 90  ? -4.09490  -10.57798 -30.43555 1.000 20.06120 ? 97  GLY   A CA  1 
ATOM   733  C  C   . GLY   A 1 90  ? -2.67813  -10.21397 -30.83772 1.000 18.84524 ? 97  GLY   A C   1 
ATOM   734  O  O   . GLY   A 1 90  ? -2.23560  -9.07576  -30.71682 1.000 18.69363 ? 97  GLY   A O   1 
ATOM   735  N  N   . MET   A 1 91  ? -1.95093  -11.21833 -31.32303 1.000 17.51346 ? 98  MET   A N   1 
ATOM   736  C  CA  . MET   A 1 91  ? -0.55630  -11.03502 -31.71093 1.000 16.54206 ? 98  MET   A CA  1 
ATOM   737  C  C   . MET   A 1 91  ? -0.29517  -11.68051 -33.06007 1.000 17.66433 ? 98  MET   A C   1 
ATOM   738  O  O   . MET   A 1 91  ? -0.79917  -12.76979 -33.34384 1.000 20.56308 ? 98  MET   A O   1 
ATOM   739  C  CB  . MET   A 1 91  ? 0.41489   -11.64055 -30.68546 1.000 19.80302 ? 98  MET   A CB  1 
ATOM   740  C  CG  . MET   A 1 91  ? 0.49353   -10.90320 -29.36742 1.000 26.09989 ? 98  MET   A CG  1 
ATOM   741  S  SD  . MET   A 1 91  ? 1.43945   -11.83639 -28.14640 1.000 23.09206 ? 98  MET   A SD  1 
ATOM   742  C  CE  . MET   A 1 91  ? 0.26952   -13.09142 -27.63825 1.000 19.63149 ? 98  MET   A CE  1 
ATOM   743  N  N   . THR   A 1 92  ? 0.52347   -11.01596 -33.87495 1.000 18.82195 ? 99  THR   A N   1 
ATOM   744  C  CA  . THR   A 1 92  ? 1.01890   -11.60147 -35.11262 1.000 20.22929 ? 99  THR   A CA  1 
ATOM   745  C  C   . THR   A 1 92  ? 2.11217   -12.62859 -34.80744 1.000 21.13526 ? 99  THR   A C   1 
ATOM   746  O  O   . THR   A 1 92  ? 2.60544   -12.73017 -33.68208 1.000 21.25948 ? 99  THR   A O   1 
ATOM   747  C  CB  . THR   A 1 92  ? 1.58748   -10.52043 -36.02221 1.000 24.68823 ? 99  THR   A CB  1 
ATOM   748  O  OG1 . THR   A 1 92  ? 2.73199   -9.93896  -35.38319 1.000 23.25473 ? 99  THR   A OG1 1 
ATOM   749  C  CG2 . THR   A 1 92  ? 0.55609   -9.42568  -36.25277 1.000 22.64290 ? 99  THR   A CG2 1 
ATOM   750  N  N   . LYS   A 1 93  ? 2.49349   -13.40238 -35.82975 1.000 20.60873 ? 100 LYS   A N   1 
ATOM   751  C  CA  . LYS   A 1 93  ? 3.61968   -14.31812 -35.66332 1.000 20.50889 ? 100 LYS   A CA  1 
ATOM   752  C  C   . LYS   A 1 93  ? 4.87110   -13.56164 -35.24560 1.000 18.87410 ? 100 LYS   A C   1 
ATOM   753  O  O   . LYS   A 1 93  ? 5.60174   -14.00174 -34.35085 1.000 19.94044 ? 100 LYS   A O   1 
ATOM   754  C  CB  . LYS   A 1 93  ? 3.88362   -15.09634 -36.95288 1.000 22.59348 ? 100 LYS   A CB  1 
ATOM   755  C  CG  . LYS   A 1 93  ? 4.96079   -16.17674 -36.79807 1.000 21.17029 ? 100 LYS   A CG  1 
ATOM   756  C  CD  . LYS   A 1 93  ? 5.21522   -16.90315 -38.11809 1.000 26.40217 ? 100 LYS   A CD  1 
ATOM   757  C  CE  . LYS   A 1 93  ? 6.12436   -18.10705 -37.91703 1.000 32.69912 ? 100 LYS   A CE  1 
ATOM   758  N  NZ  . LYS   A 1 93  ? 6.91599   -18.40582 -39.14231 1.000 30.51180 ? 100 LYS   A NZ  1 
ATOM   759  N  N   . ALA   A 1 94  ? 5.12344   -12.41078 -35.87431 1.000 21.90743 ? 101 ALA   A N   1 
ATOM   760  C  CA  . ALA   A 1 94  ? 6.28965   -11.61085 -35.51541 1.000 24.83461 ? 101 ALA   A CA  1 
ATOM   761  C  C   . ALA   A 1 94  ? 6.22062   -11.16306 -34.06129 1.000 23.72578 ? 101 ALA   A C   1 
ATOM   762  O  O   . ALA   A 1 94  ? 7.23884   -11.16454 -33.35865 1.000 25.02176 ? 101 ALA   A O   1 
ATOM   763  C  CB  . ALA   A 1 94  ? 6.40816   -10.40560 -36.44700 1.000 25.64497 ? 101 ALA   A CB  1 
ATOM   764  N  N   . ASP   A 1 95  ? 5.02515   -10.78076 -33.59007 1.000 21.90188 ? 102 ASP   A N   1 
ATOM   765  C  CA  . ASP   A 1 95  ? 4.86112   -10.41321 -32.18354 1.000 20.98587 ? 102 ASP   A CA  1 
ATOM   766  C  C   . ASP   A 1 95  ? 5.20803   -11.57661 -31.26575 1.000 19.94776 ? 102 ASP   A C   1 
ATOM   767  O  O   . ASP   A 1 95  ? 5.90523   -11.40472 -30.26028 1.000 20.56530 ? 102 ASP   A O   1 
ATOM   768  C  CB  . ASP   A 1 95  ? 3.42331   -9.96289  -31.89890 1.000 21.83114 ? 102 ASP   A CB  1 
ATOM   769  C  CG  . ASP   A 1 95  ? 3.07660   -8.63371  -32.52745 1.000 29.75788 ? 102 ASP   A CG  1 
ATOM   770  O  OD1 . ASP   A 1 95  ? 3.95217   -7.74448  -32.59106 1.000 34.56363 ? 102 ASP   A OD1 1 
ATOM   771  O  OD2 . ASP   A 1 95  ? 1.89188   -8.45667  -32.90014 1.000 31.84513 ? 102 ASP   A OD2 1 
ATOM   772  N  N   . LEU   A 1 96  ? 4.68960   -12.76768 -31.57627 1.000 21.29440 ? 103 LEU   A N   1 
ATOM   773  C  CA  . LEU   A 1 96  ? 4.96047   -13.94012 -30.74927 1.000 19.34050 ? 103 LEU   A CA  1 
ATOM   774  C  C   . LEU   A 1 96  ? 6.45524   -14.17398 -30.60200 1.000 19.72132 ? 103 LEU   A C   1 
ATOM   775  O  O   . LEU   A 1 96  ? 6.96335   -14.35692 -29.48930 1.000 20.54776 ? 103 LEU   A O   1 
ATOM   776  C  CB  . LEU   A 1 96  ? 4.30214   -15.17626 -31.35837 1.000 22.96739 ? 103 LEU   A CB  1 
ATOM   777  C  CG  . LEU   A 1 96  ? 2.82199   -15.40225 -31.10655 1.000 25.45136 ? 103 LEU   A CG  1 
ATOM   778  C  CD1 . LEU   A 1 96  ? 2.40910   -16.68869 -31.80410 1.000 21.89688 ? 103 LEU   A CD1 1 
ATOM   779  C  CD2 . LEU   A 1 96  ? 2.51824   -15.46401 -29.61354 1.000 17.60531 ? 103 LEU   A CD2 1 
ATOM   780  N  N   . ILE   A 1 97  ? 7.17465   -14.17465 -31.72502 1.000 21.19929 ? 104 ILE   A N   1 
ATOM   781  C  CA  . ILE   A 1 97  ? 8.60745   -14.44480 -31.70830 1.000 21.37341 ? 104 ILE   A CA  1 
ATOM   782  C  C   . ILE   A 1 97  ? 9.34723   -13.34591 -30.95328 1.000 22.61387 ? 104 ILE   A C   1 
ATOM   783  O  O   . ILE   A 1 97  ? 10.29479  -13.61265 -30.20438 1.000 24.54225 ? 104 ILE   A O   1 
ATOM   784  C  CB  . ILE   A 1 97  ? 9.11576   -14.58992 -33.15462 1.000 24.28942 ? 104 ILE   A CB  1 
ATOM   785  C  CG1 . ILE   A 1 97  ? 8.52688   -15.84695 -33.79661 1.000 19.26085 ? 104 ILE   A CG1 1 
ATOM   786  C  CG2 . ILE   A 1 97  ? 10.64137  -14.63483 -33.19655 1.000 20.47229 ? 104 ILE   A CG2 1 
ATOM   787  C  CD1 . ILE   A 1 97  ? 8.66788   -15.87685 -35.30484 1.000 23.99892 ? 104 ILE   A CD1 1 
ATOM   788  N  N   . ASN   A 1 98  ? 8.91877   -12.09788 -31.12721 1.000 16.64948 ? 105 ASN   A N   1 
ATOM   789  C  CA  . ASN   A 1 98  ? 9.52118   -10.95470 -30.44413 1.000 20.56990 ? 105 ASN   A CA  1 
ATOM   790  C  C   . ASN   A 1 98  ? 8.96186   -10.82183 -29.02296 1.000 19.69218 ? 105 ASN   A C   1 
ATOM   791  O  O   . ASN   A 1 98  ? 8.38333   -9.80686  -28.63418 1.000 22.29511 ? 105 ASN   A O   1 
ATOM   792  C  CB  . ASN   A 1 98  ? 9.29249   -9.68948  -31.26094 1.000 26.62611 ? 105 ASN   A CB  1 
ATOM   793  C  CG  . ASN   A 1 98  ? 10.34274  -8.63367  -31.00528 1.000 47.15403 ? 105 ASN   A CG  1 
ATOM   794  O  OD1 . ASN   A 1 98  ? 11.33286  -8.87175  -30.30268 1.000 54.22337 ? 105 ASN   A OD1 1 
ATOM   795  N  ND2 . ASN   A 1 98  ? 10.13963  -7.45453  -31.58269 1.000 61.78183 ? 105 ASN   A ND2 1 
ATOM   796  N  N   . ASN   A 1 99  ? 9.14303   -11.89753 -28.25347 1.000 21.24368 ? 106 ASN   A N   1 
ATOM   797  C  CA  . ASN   A 1 99  ? 8.80859   -11.94188 -26.82607 1.000 19.65016 ? 106 ASN   A CA  1 
ATOM   798  C  C   . ASN   A 1 99  ? 7.35816   -11.54888 -26.55268 1.000 22.99487 ? 106 ASN   A C   1 
ATOM   799  O  O   . ASN   A 1 99  ? 7.05760   -10.78156 -25.63574 1.000 18.62777 ? 106 ASN   A O   1 
ATOM   800  C  CB  . ASN   A 1 99  ? 9.77980   -11.07745 -26.02122 1.000 22.55322 ? 106 ASN   A CB  1 
ATOM   801  C  CG  . ASN   A 1 99  ? 11.21309  -11.52650 -26.19437 1.000 20.09001 ? 106 ASN   A CG  1 
ATOM   802  O  OD1 . ASN   A 1 99  ? 11.52688  -12.69599 -25.99911 1.000 20.49845 ? 106 ASN   A OD1 1 
ATOM   803  N  ND2 . ASN   A 1 99  ? 12.09193  -10.59885 -26.56516 1.000 20.79539 ? 106 ASN   A ND2 1 
ATOM   804  N  N   . LEU   A 1 100 ? 6.45243   -12.12421 -27.34131 1.000 18.62154 ? 107 LEU   A N   1 
ATOM   805  C  CA  . LEU   A 1 100 ? 5.00959   -11.94659 -27.16606 1.000 21.94072 ? 107 LEU   A CA  1 
ATOM   806  C  C   . LEU   A 1 100 ? 4.63020   -10.46888 -27.08137 1.000 22.84581 ? 107 LEU   A C   1 
ATOM   807  O  O   . LEU   A 1 100 ? 3.83750   -10.04410 -26.23701 1.000 22.39557 ? 107 LEU   A O   1 
ATOM   808  C  CB  . LEU   A 1 100 ? 4.51101   -12.72305 -25.94854 1.000 17.93682 ? 107 LEU   A CB  1 
ATOM   809  C  CG  . LEU   A 1 100 ? 4.91488   -14.20438 -26.02103 1.000 28.02690 ? 107 LEU   A CG  1 
ATOM   810  C  CD1 . LEU   A 1 100 ? 5.90586   -14.56301 -24.92657 1.000 37.98932 ? 107 LEU   A CD1 1 
ATOM   811  C  CD2 . LEU   A 1 100 ? 3.70995   -15.12212 -25.96530 1.000 25.37723 ? 107 LEU   A CD2 1 
ATOM   812  N  N   . GLY   A 1 101 ? 5.20241   -9.67580  -27.98654 1.000 19.76132 ? 108 GLY   A N   1 
ATOM   813  C  CA  . GLY   A 1 101 ? 4.82088   -8.27701  -28.08382 1.000 21.77846 ? 108 GLY   A CA  1 
ATOM   814  C  C   . GLY   A 1 101 ? 5.35309   -7.37334  -26.99532 1.000 24.34919 ? 108 GLY   A C   1 
ATOM   815  O  O   . GLY   A 1 101 ? 4.86236   -6.24466  -26.85053 1.000 25.49835 ? 108 GLY   A O   1 
ATOM   816  N  N   . THR   A 1 102 ? 6.33723   -7.82653  -26.22178 1.000 20.31976 ? 109 THR   A N   1 
ATOM   817  C  CA  . THR   A 1 102 ? 6.91453   -7.04458  -25.13847 1.000 22.16189 ? 109 THR   A CA  1 
ATOM   818  C  C   . THR   A 1 102 ? 8.29666   -6.53068  -25.52261 1.000 22.02734 ? 109 THR   A C   1 
ATOM   819  O  O   . THR   A 1 102 ? 8.93677   -7.03764  -26.44693 1.000 22.99254 ? 109 THR   A O   1 
ATOM   820  C  CB  . THR   A 1 102 ? 7.01848   -7.88215  -23.85917 1.000 19.94423 ? 109 THR   A CB  1 
ATOM   821  O  OG1 . THR   A 1 102 ? 8.08793   -8.83059  -24.00364 1.000 24.45625 ? 109 THR   A OG1 1 
ATOM   822  C  CG2 . THR   A 1 102 ? 5.71521   -8.63021  -23.59125 1.000 24.37019 ? 109 THR   A CG2 1 
ATOM   823  N  N   . ILE   A 1 103 ? 8.75455   -5.51089  -24.79577 1.000 21.45531 ? 110 ILE   A N   1 
ATOM   824  C  CA  . ILE   A 1 103 ? 10.15041  -5.08310  -24.87965 1.000 18.74279 ? 110 ILE   A CA  1 
ATOM   825  C  C   . ILE   A 1 103 ? 10.90317  -5.79269  -23.75813 1.000 22.70638 ? 110 ILE   A C   1 
ATOM   826  O  O   . ILE   A 1 103 ? 11.47954  -5.15886  -22.86492 1.000 20.58653 ? 110 ILE   A O   1 
ATOM   827  C  CB  . ILE   A 1 103 ? 10.27624  -3.55219  -24.81744 1.000 25.98170 ? 110 ILE   A CB  1 
ATOM   828  C  CG1 . ILE   A 1 103 ? 9.52356   -2.97712  -23.61869 1.000 29.05479 ? 110 ILE   A CG1 1 
ATOM   829  C  CG2 . ILE   A 1 103 ? 9.72397   -2.93403  -26.09079 1.000 28.66959 ? 110 ILE   A CG2 1 
ATOM   830  C  CD1 . ILE   A 1 103 ? 9.90346   -1.52836  -23.31868 1.000 37.27315 ? 110 ILE   A CD1 1 
ATOM   831  N  N   A ALA   A 1 104 ? 10.91647  -7.12583  -23.81539 0.653 22.19347 ? 111 ALA   A N   1 
ATOM   832  N  N   B ALA   A 1 104 ? 10.91867  -7.12755  -23.82147 0.347 22.17587 ? 111 ALA   A N   1 
ATOM   833  C  CA  A ALA   A 1 104 ? 11.34471  -7.91705  -22.66955 0.653 21.96441 ? 111 ALA   A CA  1 
ATOM   834  C  CA  B ALA   A 1 104 ? 11.31323  -7.93586  -22.67264 0.347 22.07884 ? 111 ALA   A CA  1 
ATOM   835  C  C   A ALA   A 1 104 ? 12.82175  -7.72298  -22.34599 0.653 20.24747 ? 111 ALA   A C   1 
ATOM   836  C  C   B ALA   A 1 104 ? 12.79001  -7.78627  -22.32680 0.347 20.38153 ? 111 ALA   A C   1 
ATOM   837  O  O   A ALA   A 1 104 ? 13.21041  -7.83726  -21.17824 0.653 22.16194 ? 111 ALA   A O   1 
ATOM   838  O  O   B ALA   A 1 104 ? 13.17246  -8.01320  -21.17315 0.347 22.29853 ? 111 ALA   A O   1 
ATOM   839  C  CB  A ALA   A 1 104 ? 11.03566  -9.39596  -22.91554 0.653 20.73846 ? 111 ALA   A CB  1 
ATOM   840  C  CB  B ALA   A 1 104 ? 10.97699  -9.40607  -22.92922 0.347 20.65982 ? 111 ALA   A CB  1 
ATOM   841  N  N   A LYS   A 1 105 ? 13.65969  -7.42894  -23.34343 0.653 19.85684 ? 112 LYS   A N   1 
ATOM   842  N  N   B LYS   A 1 105 ? 13.63685  -7.42481  -23.29323 0.347 20.14287 ? 112 LYS   A N   1 
ATOM   843  C  CA  A LYS   A 1 105 ? 15.08556  -7.27646  -23.06700 0.653 25.16586 ? 112 LYS   A CA  1 
ATOM   844  C  CA  B LYS   A 1 105 ? 15.05234  -7.24063  -22.98440 0.347 25.10750 ? 112 LYS   A CA  1 
ATOM   845  C  C   A LYS   A 1 105 ? 15.33871  -6.10573  -22.12445 0.653 32.00217 ? 112 LYS   A C   1 
ATOM   846  C  C   B LYS   A 1 105 ? 15.26147  -5.99632  -22.12908 0.347 31.29603 ? 112 LYS   A C   1 
ATOM   847  O  O   A LYS   A 1 105 ? 15.99556  -6.25866  -21.08834 0.653 26.67573 ? 112 LYS   A O   1 
ATOM   848  O  O   B LYS   A 1 105 ? 15.79791  -6.07161  -21.01748 0.347 26.18839 ? 112 LYS   A O   1 
ATOM   849  C  CB  A LYS   A 1 105 ? 15.86776  -7.10162  -24.37030 0.653 24.45116 ? 112 LYS   A CB  1 
ATOM   850  C  CB  B LYS   A 1 105 ? 15.87592  -7.16112  -24.27336 0.347 24.66736 ? 112 LYS   A CB  1 
ATOM   851  C  CG  A LYS   A 1 105 ? 17.37204  -6.94645  -24.17867 0.653 29.17075 ? 112 LYS   A CG  1 
ATOM   852  C  CG  B LYS   A 1 105 ? 16.91254  -8.26898  -24.40763 0.347 37.39871 ? 112 LYS   A CG  1 
ATOM   853  C  CD  A LYS   A 1 105 ? 18.10178  -6.95078  -25.52290 0.653 32.56849 ? 112 LYS   A CD  1 
ATOM   854  C  CD  B LYS   A 1 105 ? 18.10837  -7.83638  -25.24574 0.347 30.34698 ? 112 LYS   A CD  1 
ATOM   855  C  CE  A LYS   A 1 105 ? 19.60962  -7.04432  -25.35275 0.653 53.07311 ? 112 LYS   A CE  1 
ATOM   856  C  CE  B LYS   A 1 105 ? 18.75464  -6.58236  -24.67997 0.347 32.63504 ? 112 LYS   A CE  1 
ATOM   857  N  NZ  A LYS   A 1 105 ? 20.14255  -6.00232  -24.43044 0.653 44.80541 ? 112 LYS   A NZ  1 
ATOM   858  N  NZ  B LYS   A 1 105 ? 20.08941  -6.87173  -24.07913 0.347 46.69681 ? 112 LYS   A NZ  1 
ATOM   859  N  N   A SER   A 1 106 ? 14.82573  -4.92166  -22.46713 0.653 24.09503 ? 113 SER   A N   1 
ATOM   860  N  N   B SER   A 1 106 ? 14.84063  -4.83482  -22.63410 0.347 24.90446 ? 113 SER   A N   1 
ATOM   861  C  CA  A SER   A 1 106 ? 15.02205  -3.77216  -21.59141 0.653 27.75159 ? 113 SER   A CA  1 
ATOM   862  C  CA  B SER   A 1 106 ? 14.94380  -3.61489  -21.84262 0.347 28.05770 ? 113 SER   A CA  1 
ATOM   863  C  C   A SER   A 1 106 ? 14.16309  -3.87592  -20.33729 0.653 24.95462 ? 113 SER   A C   1 
ATOM   864  C  C   B SER   A 1 106 ? 14.07429  -3.68718  -20.59456 0.347 26.10795 ? 113 SER   A C   1 
ATOM   865  O  O   A SER   A 1 106 ? 14.58358  -3.43347  -19.26200 0.653 28.24870 ? 113 SER   A O   1 
ATOM   866  O  O   B SER   A 1 106 ? 14.36691  -3.02075  -19.59529 0.347 29.45622 ? 113 SER   A O   1 
ATOM   867  C  CB  A SER   A 1 106 ? 14.73143  -2.47411  -22.34904 0.653 32.50753 ? 113 SER   A CB  1 
ATOM   868  C  CB  B SER   A 1 106 ? 14.56423  -2.40388  -22.69603 0.347 32.22358 ? 113 SER   A CB  1 
ATOM   869  O  OG  A SER   A 1 106 ? 13.36925  -2.39639  -22.73376 0.653 32.77150 ? 113 SER   A OG  1 
ATOM   870  O  OG  B SER   A 1 106 ? 13.15623  -2.28063  -22.80517 0.347 32.41692 ? 113 SER   A OG  1 
ATOM   871  N  N   A GLY   A 1 107 ? 12.96776  -4.45979  -20.44936 0.653 24.64895 ? 114 GLY   A N   1 
ATOM   872  N  N   B GLY   A 1 107 ? 13.00797  -4.48891  -20.62986 0.347 24.48472 ? 114 GLY   A N   1 
ATOM   873  C  CA  A GLY   A 1 107 ? 12.15130  -4.67912  -19.26439 0.653 27.40858 ? 114 GLY   A CA  1 
ATOM   874  C  CA  B GLY   A 1 107 ? 12.15951  -4.62740  -19.45521 0.347 27.88767 ? 114 GLY   A CA  1 
ATOM   875  C  C   A GLY   A 1 107 ? 12.83534  -5.56800  -18.24321 0.653 27.38833 ? 114 GLY   A C   1 
ATOM   876  C  C   B GLY   A 1 107 ? 12.83427  -5.40351  -18.33945 0.347 27.08452 ? 114 GLY   A C   1 
ATOM   877  O  O   A GLY   A 1 107 ? 12.81287  -5.28436  -17.04208 0.653 25.11673 ? 114 GLY   A O   1 
ATOM   878  O  O   B GLY   A 1 107 ? 12.89047  -4.94745  -17.19343 0.347 27.33259 ? 114 GLY   A O   1 
ATOM   879  N  N   A THR   A 1 108 ? 13.45201  -6.65843  -18.70540 0.653 22.58969 ? 115 THR   A N   1 
ATOM   880  N  N   B THR   A 1 108 ? 13.35319  -6.59181  -18.65807 0.347 22.89921 ? 115 THR   A N   1 
ATOM   881  C  CA  A THR   A 1 108 ? 14.19623  -7.52676  -17.79774 0.653 24.50126 ? 115 THR   A CA  1 
ATOM   882  C  CA  B THR   A 1 108 ? 14.06535  -7.37650  -17.65401 0.347 23.54009 ? 115 THR   A CA  1 
ATOM   883  C  C   A THR   A 1 108 ? 15.35210  -6.77825  -17.14758 0.653 29.84770 ? 115 THR   A C   1 
ATOM   884  C  C   B THR   A 1 108 ? 15.21449  -6.57937  -17.05040 0.347 29.45862 ? 115 THR   A C   1 
ATOM   885  O  O   A THR   A 1 108 ? 15.59160  -6.91112  -15.94188 0.653 28.65661 ? 115 THR   A O   1 
ATOM   886  O  O   B THR   A 1 108 ? 15.47144  -6.65924  -15.84334 0.347 29.63450 ? 115 THR   A O   1 
ATOM   887  C  CB  A THR   A 1 108 ? 14.71431  -8.75356  -18.55100 0.653 23.26180 ? 115 THR   A CB  1 
ATOM   888  C  CB  B THR   A 1 108 ? 14.58165  -8.67802  -18.27118 0.347 24.20247 ? 115 THR   A CB  1 
ATOM   889  O  OG1 A THR   A 1 108 ? 13.60631  -9.50190  -19.07083 0.653 22.82408 ? 115 THR   A OG1 1 
ATOM   890  O  OG1 B THR   A 1 108 ? 13.48108  -9.42951  -18.79907 0.347 24.35574 ? 115 THR   A OG1 1 
ATOM   891  C  CG2 A THR   A 1 108 ? 15.53624  -9.63958  -17.63033 0.653 26.46822 ? 115 THR   A CG2 1 
ATOM   892  C  CG2 B THR   A 1 108 ? 15.30408  -9.51628  -17.22915 0.347 28.83282 ? 115 THR   A CG2 1 
ATOM   893  N  N   A LYS   A 1 109 ? 16.08062  -5.98476  -17.93235 0.653 26.41989 ? 116 LYS   A N   1 
ATOM   894  N  N   B LYS   A 1 109 ? 15.91609  -5.80107  -17.87566 0.347 27.04181 ? 116 LYS   A N   1 
ATOM   895  C  CA  A LYS   A 1 109 ? 17.18922  -5.21310  -17.38212 0.653 27.03601 ? 116 LYS   A CA  1 
ATOM   896  C  CA  B LYS   A 1 109 ? 17.00906  -4.97899  -17.36795 0.347 27.49994 ? 116 LYS   A CA  1 
ATOM   897  C  C   A LYS   A 1 109 ? 16.71749  -4.34069  -16.22429 0.653 35.53893 ? 116 LYS   A C   1 
ATOM   898  C  C   B LYS   A 1 109 ? 16.50122  -3.96080  -16.35375 0.347 34.28999 ? 116 LYS   A C   1 
ATOM   899  O  O   A LYS   A 1 109 ? 17.31551  -4.34470  -15.14212 0.653 36.06657 ? 116 LYS   A O   1 
ATOM   900  O  O   B LYS   A 1 109 ? 17.06310  -3.82075  -15.26167 0.347 31.23614 ? 116 LYS   A O   1 
ATOM   901  C  CB  A LYS   A 1 109 ? 17.82459  -4.37554  -18.49377 0.653 28.92719 ? 116 LYS   A CB  1 
ATOM   902  C  CB  B LYS   A 1 109 ? 17.71930  -4.28400  -18.53050 0.347 29.11110 ? 116 LYS   A CB  1 
ATOM   903  C  CG  A LYS   A 1 109 ? 18.94271  -3.42691  -18.07270 0.653 42.46486 ? 116 LYS   A CG  1 
ATOM   904  C  CG  B LYS   A 1 109 ? 18.39063  -2.96671  -18.17219 0.347 42.27648 ? 116 LYS   A CG  1 
ATOM   905  C  CD  A LYS   A 1 109 ? 19.27942  -2.48785  -19.23138 0.653 44.43193 ? 116 LYS   A CD  1 
ATOM   906  C  CD  B LYS   A 1 109 ? 19.14859  -2.40011  -19.36523 0.347 44.57825 ? 116 LYS   A CD  1 
ATOM   907  C  CE  A LYS   A 1 109 ? 20.01152  -1.23333  -18.77030 0.653 56.35113 ? 116 LYS   A CE  1 
ATOM   908  C  CE  B LYS   A 1 109 ? 20.65456  -2.51649  -19.18460 0.347 42.43268 ? 116 LYS   A CE  1 
ATOM   909  N  NZ  A LYS   A 1 109 ? 21.11185  -1.55312  -17.82612 0.653 48.38616 ? 116 LYS   A NZ  1 
ATOM   910  N  NZ  B LYS   A 1 109 ? 21.04540  -2.58804  -17.75046 0.347 44.26106 ? 116 LYS   A NZ  1 
ATOM   911  N  N   A ALA   A 1 110 ? 15.62592  -3.60080  -16.42769 0.653 31.42387 ? 117 ALA   A N   1 
ATOM   912  N  N   B ALA   A 1 110 ? 15.43105  -3.23990  -16.69680 0.347 32.25040 ? 117 ALA   A N   1 
ATOM   913  C  CA  A ALA   A 1 110 ? 15.10084  -2.74236  -15.36977 0.653 37.53044 ? 117 ALA   A CA  1 
ATOM   914  C  CA  B ALA   A 1 110 ? 14.91915  -2.21486  -15.79343 0.347 33.24276 ? 117 ALA   A CA  1 
ATOM   915  C  C   A ALA   A 1 110 ? 14.60174  -3.56615  -14.18744 0.653 34.45476 ? 117 ALA   A C   1 
ATOM   916  C  C   B ALA   A 1 110 ? 14.23456  -2.82575  -14.57688 0.347 31.29908 ? 117 ALA   A C   1 
ATOM   917  O  O   A ALA   A 1 110 ? 14.91282  -3.26332  -13.02959 0.653 32.49737 ? 117 ALA   A O   1 
ATOM   918  O  O   B ALA   A 1 110 ? 14.23550  -2.21865  -13.50044 0.347 29.78731 ? 117 ALA   A O   1 
ATOM   919  C  CB  A ALA   A 1 110 ? 13.98377  -1.85731  -15.92358 0.653 32.66002 ? 117 ALA   A CB  1 
ATOM   920  C  CB  B ALA   A 1 110 ? 13.96802  -1.28195  -16.54054 0.347 26.49055 ? 117 ALA   A CB  1 
ATOM   921  N  N   A PHE   A 1 111 ? 13.82223  -4.61340  -14.46136 0.653 32.20057 ? 118 PHE   A N   1 
ATOM   922  N  N   B PHE   A 1 111 ? 13.64804  -4.01655  -14.72118 0.347 27.92333 ? 118 PHE   A N   1 
ATOM   923  C  CA  A PHE   A 1 111 ? 13.26535  -5.43567  -13.39074 0.653 27.44273 ? 118 PHE   A CA  1 
ATOM   924  C  CA  B PHE   A 1 111 ? 13.18087  -4.75390  -13.55065 0.347 29.59313 ? 118 PHE   A CA  1 
ATOM   925  C  C   A PHE   A 1 111 ? 14.36215  -5.98505  -12.48431 0.653 31.91618 ? 118 PHE   A C   1 
ATOM   926  C  C   B PHE   A 1 111 ? 14.33863  -5.02560  -12.59907 0.347 29.45614 ? 118 PHE   A C   1 
ATOM   927  O  O   A PHE   A 1 111 ? 14.25177  -5.93850  -11.25432 0.653 29.91584 ? 118 PHE   A O   1 
ATOM   928  O  O   B PHE   A 1 111 ? 14.27194  -4.70175  -11.40788 0.347 29.17178 ? 118 PHE   A O   1 
ATOM   929  C  CB  A PHE   A 1 111 ? 12.43619  -6.56990  -13.99997 0.653 26.68360 ? 118 PHE   A CB  1 
ATOM   930  C  CB  B PHE   A 1 111 ? 12.50589  -6.05769  -13.99425 0.347 28.40773 ? 118 PHE   A CB  1 
ATOM   931  C  CG  A PHE   A 1 111 ? 11.76346  -7.45864  -12.98884 0.653 26.62161 ? 118 PHE   A CG  1 
ATOM   932  C  CG  B PHE   A 1 111 ? 11.90557  -6.87302  -12.86710 0.347 27.34554 ? 118 PHE   A CG  1 
ATOM   933  C  CD1 A PHE   A 1 111 ? 11.12904  -6.92242  -11.88005 0.653 25.99500 ? 118 PHE   A CD1 1 
ATOM   934  C  CD1 B PHE   A 1 111 ? 11.58984  -6.29809  -11.64500 0.347 28.13146 ? 118 PHE   A CD1 1 
ATOM   935  C  CD2 A PHE   A 1 111 ? 11.73483  -8.83367  -13.17138 0.653 24.62894 ? 118 PHE   A CD2 1 
ATOM   936  C  CD2 B PHE   A 1 111 ? 11.61538  -8.21414  -13.05678 0.347 26.81230 ? 118 PHE   A CD2 1 
ATOM   937  C  CE1 A PHE   A 1 111 ? 10.49953  -7.74236  -10.95838 0.653 22.36471 ? 118 PHE   A CE1 1 
ATOM   938  C  CE1 B PHE   A 1 111 ? 11.02265  -7.04629  -10.63022 0.347 30.11146 ? 118 PHE   A CE1 1 
ATOM   939  C  CE2 A PHE   A 1 111 ? 11.10272  -9.65842  -12.25652 0.653 25.18623 ? 118 PHE   A CE2 1 
ATOM   940  C  CE2 B PHE   A 1 111 ? 11.04909  -8.97017  -12.04476 0.347 28.71231 ? 118 PHE   A CE2 1 
ATOM   941  C  CZ  A PHE   A 1 111 ? 10.48646  -9.10979  -11.14712 0.653 24.85652 ? 118 PHE   A CZ  1 
ATOM   942  C  CZ  B PHE   A 1 111 ? 10.75372  -8.38551  -10.83007 0.347 22.90477 ? 118 PHE   A CZ  1 
ATOM   943  N  N   A MET   A 1 112 ? 15.43813  -6.50378  -13.07444 0.653 31.83062 ? 119 MET   A N   1 
ATOM   944  N  N   B MET   A 1 112 ? 15.42434  -5.59890  -13.11806 0.347 31.77642 ? 119 MET   A N   1 
ATOM   945  C  CA  A MET   A 1 112 ? 16.43547  -7.20612  -12.27564 0.653 42.23927 ? 119 MET   A CA  1 
ATOM   946  C  CA  B MET   A 1 112 ? 16.57609  -5.89779  -12.27520 0.347 33.03351 ? 119 MET   A CA  1 
ATOM   947  C  C   A MET   A 1 112 ? 17.29351  -6.24506  -11.46042 0.653 40.91170 ? 119 MET   A C   1 
ATOM   948  C  C   B MET   A 1 112 ? 17.16696  -4.62536  -11.68388 0.347 35.45001 ? 119 MET   A C   1 
ATOM   949  O  O   A MET   A 1 112 ? 17.83724  -6.63326  -10.41858 0.653 38.21521 ? 119 MET   A O   1 
ATOM   950  O  O   B MET   A 1 112 ? 17.47846  -4.57134  -10.48895 0.347 31.07060 ? 119 MET   A O   1 
ATOM   951  C  CB  A MET   A 1 112 ? 17.29413  -8.08087  -13.18384 0.653 41.89824 ? 119 MET   A CB  1 
ATOM   952  C  CB  B MET   A 1 112 ? 17.62262  -6.66697  -13.07775 0.347 30.88720 ? 119 MET   A CB  1 
ATOM   953  C  CG  A MET   A 1 112 ? 16.86515  -9.53577  -13.17880 0.653 25.24884 ? 119 MET   A CG  1 
ATOM   954  C  CG  B MET   A 1 112 ? 17.28293  -8.13579  -13.24878 0.347 41.69234 ? 119 MET   A CG  1 
ATOM   955  S  SD  A MET   A 1 112 ? 17.91730  -10.54095 -14.23404 0.653 64.66621 ? 119 MET   A SD  1 
ATOM   956  S  SD  B MET   A 1 112 ? 18.32553  -8.92547  -14.47869 0.347 47.07698 ? 119 MET   A SD  1 
ATOM   957  C  CE  A MET   A 1 112 ? 16.77369  -11.80793 -14.75413 0.653 40.73022 ? 119 MET   A CE  1 
ATOM   958  C  CE  B MET   A 1 112 ? 18.75668  -10.44392 -13.62854 0.347 54.28210 ? 119 MET   A CE  1 
ATOM   959  N  N   A GLU   A 1 113 ? 17.42771  -4.99572  -11.90808 0.653 35.28131 ? 120 GLU   A N   1 
ATOM   960  N  N   B GLU   A 1 113 ? 17.33261  -3.58806  -12.50894 0.347 30.83602 ? 120 GLU   A N   1 
ATOM   961  C  CA  A GLU   A 1 113 ? 18.05091  -3.98437  -11.06086 0.653 39.61259 ? 120 GLU   A CA  1 
ATOM   962  C  CA  B GLU   A 1 113 ? 17.80730  -2.30604  -11.99750 0.347 33.45776 ? 120 GLU   A CA  1 
ATOM   963  C  C   A GLU   A 1 113 ? 17.16407  -3.65515  -9.86594  0.653 46.08799 ? 120 GLU   A C   1 
ATOM   964  C  C   B GLU   A 1 113 ? 16.96367  -1.85379  -10.81285 0.347 37.83388 ? 120 GLU   A C   1 
ATOM   965  O  O   A GLU   A 1 113 ? 17.65718  -3.48074  -8.74417  0.653 40.62273 ? 120 GLU   A O   1 
ATOM   966  O  O   B GLU   A 1 113 ? 17.48901  -1.44774  -9.76960  0.347 34.81791 ? 120 GLU   A O   1 
ATOM   967  C  CB  A GLU   A 1 113 ? 18.34846  -2.72212  -11.87163 0.653 39.05633 ? 120 GLU   A CB  1 
ATOM   968  C  CB  B GLU   A 1 113 ? 17.77668  -1.25234  -13.10832 0.347 40.04598 ? 120 GLU   A CB  1 
ATOM   969  C  CG  A GLU   A 1 113 ? 19.43344  -2.90020  -12.92371 0.653 48.25516 ? 120 GLU   A CG  1 
ATOM   970  C  CG  B GLU   A 1 113 ? 19.05524  -1.15471  -13.92993 0.347 51.68336 ? 120 GLU   A CG  1 
ATOM   971  C  CD  A GLU   A 1 113 ? 19.54535  -1.71294  -13.86203 0.653 54.71949 ? 120 GLU   A CD  1 
ATOM   972  C  CD  B GLU   A 1 113 ? 18.81262  -0.61450  -15.33079 0.347 46.41008 ? 120 GLU   A CD  1 
ATOM   973  O  OE1 A GLU   A 1 113 ? 18.94356  -0.65901  -13.56622 0.653 62.52420 ? 120 GLU   A OE1 1 
ATOM   974  O  OE1 B GLU   A 1 113 ? 17.65760  -0.25470  -15.64064 0.347 40.65746 ? 120 GLU   A OE1 1 
ATOM   975  O  OE2 A GLU   A 1 113 ? 20.23891  -1.83487  -14.89614 0.653 74.14645 ? 120 GLU   A OE2 1 
ATOM   976  O  OE2 B GLU   A 1 113 ? 19.77874  -0.54410  -16.12079 0.347 43.41553 ? 120 GLU   A OE2 1 
ATOM   977  N  N   A ALA   A 1 114 ? 15.84967  -3.57310  -10.08769 0.653 35.70100 ? 121 ALA   A N   1 
ATOM   978  N  N   B ALA   A 1 114 ? 15.64136  -1.92367  -10.96221 0.347 30.78250 ? 121 ALA   A N   1 
ATOM   979  C  CA  A ALA   A 1 114 ? 14.93000  -3.28339  -8.99327  0.653 32.15328 ? 121 ALA   A CA  1 
ATOM   980  C  CA  B ALA   A 1 114 ? 14.74486  -1.50140  -9.89419  0.347 37.72743 ? 121 ALA   A CA  1 
ATOM   981  C  C   A ALA   A 1 114 ? 14.97785  -4.37580  -7.93367  0.653 31.89301 ? 121 ALA   A C   1 
ATOM   982  C  C   B ALA   A 1 114 ? 14.82873  -2.41946  -8.68297  0.347 31.51480 ? 121 ALA   A C   1 
ATOM   983  O  O   A ALA   A 1 114 ? 14.85779  -4.09626  -6.73528  0.653 42.59040 ? 121 ALA   A O   1 
ATOM   984  O  O   B ALA   A 1 114 ? 14.68517  -1.95675  -7.54477  0.347 33.10694 ? 121 ALA   A O   1 
ATOM   985  C  CB  A ALA   A 1 114 ? 13.51052  -3.11212  -9.53166  0.653 32.06553 ? 121 ALA   A CB  1 
ATOM   986  C  CB  B ALA   A 1 114 ? 13.31602  -1.45292  -10.41871 0.347 34.24929 ? 121 ALA   A CB  1 
ATOM   987  N  N   A LEU   A 1 115 ? 15.15291  -5.62955  -8.35585  0.653 34.91689 ? 122 LEU   A N   1 
ATOM   988  N  N   B LEU   A 1 115 ? 15.04557  -3.71774  -8.90434  0.347 30.26284 ? 122 LEU   A N   1 
ATOM   989  C  CA  A LEU   A 1 115 ? 15.16774  -6.73661  -7.40378  0.653 31.21724 ? 122 LEU   A CA  1 
ATOM   990  C  CA  B LEU   A 1 115 ? 15.13843  -4.65241  -7.78798  0.347 33.08773 ? 122 LEU   A CA  1 
ATOM   991  C  C   A LEU   A 1 115 ? 16.35493  -6.63341  -6.45390  0.653 49.44787 ? 122 LEU   A C   1 
ATOM   992  C  C   B LEU   A 1 115 ? 16.37213  -4.36259  -6.94200  0.347 33.62707 ? 122 LEU   A C   1 
ATOM   993  O  O   A LEU   A 1 115 ? 16.23557  -6.94110  -5.26121  0.653 44.69944 ? 122 LEU   A O   1 
ATOM   994  O  O   B LEU   A 1 115 ? 16.29480  -4.30547  -5.70912  0.347 37.39355 ? 122 LEU   A O   1 
ATOM   995  C  CB  A LEU   A 1 115 ? 15.19219  -8.06611  -8.15152  0.653 30.71780 ? 122 LEU   A CB  1 
ATOM   996  C  CB  B LEU   A 1 115 ? 15.16056  -6.08931  -8.30910  0.347 32.92956 ? 122 LEU   A CB  1 
ATOM   997  C  CG  A LEU   A 1 115 ? 13.87777  -8.39724  -8.85847  0.653 29.16406 ? 122 LEU   A CG  1 
ATOM   998  C  CG  B LEU   A 1 115 ? 13.80945  -6.69041  -8.70820  0.347 27.08498 ? 122 LEU   A CG  1 
ATOM   999  C  CD1 A LEU   A 1 115 ? 13.98047  -9.72516  -9.58743  0.653 35.15500 ? 122 LEU   A CD1 1 
ATOM   1000 C  CD1 B LEU   A 1 115 ? 13.98586  -8.13288  -9.16163  0.347 28.55064 ? 122 LEU   A CD1 1 
ATOM   1001 C  CD2 A LEU   A 1 115 ? 12.73278  -8.40819  -7.85526  0.653 30.97082 ? 122 LEU   A CD2 1 
ATOM   1002 C  CD2 B LEU   A 1 115 ? 12.78925  -6.59445  -7.57826  0.347 27.53448 ? 122 LEU   A CD2 1 
ATOM   1003 N  N   A GLN   A 1 116 ? 17.50977  -6.20719  -6.96065  0.653 40.24162 ? 123 GLN   A N   1 
ATOM   1004 N  N   B GLN   A 1 116 ? 17.52402  -4.17849  -7.58979  0.347 35.72416 ? 123 GLN   A N   1 
ATOM   1005 C  CA  A GLN   A 1 116 ? 18.64584  -5.96412  -6.08444  0.653 40.82116 ? 123 GLN   A CA  1 
ATOM   1006 C  CA  B GLN   A 1 116 ? 18.71485  -3.73858  -6.87738  0.347 47.83581 ? 123 GLN   A CA  1 
ATOM   1007 C  C   A GLN   A 1 116 ? 18.51710  -4.64863  -5.32764  0.653 57.21261 ? 123 GLN   A C   1 
ATOM   1008 C  C   B GLN   A 1 116 ? 18.51240  -2.38347  -6.21129  0.347 44.34324 ? 123 GLN   A C   1 
ATOM   1009 O  O   A GLN   A 1 116 ? 19.14310  -4.49178  -4.27356  0.653 59.62262 ? 123 GLN   A O   1 
ATOM   1010 O  O   B GLN   A 1 116 ? 19.32443  -1.99895  -5.36243  0.347 46.39885 ? 123 GLN   A O   1 
ATOM   1011 C  CB  A GLN   A 1 116 ? 19.94579  -5.98770  -6.89289  0.653 57.10689 ? 123 GLN   A CB  1 
ATOM   1012 C  CB  B GLN   A 1 116 ? 19.90495  -3.69397  -7.84490  0.347 38.54608 ? 123 GLN   A CB  1 
ATOM   1013 C  CG  A GLN   A 1 116 ? 20.37178  -7.38609  -7.31823  0.653 50.25680 ? 123 GLN   A CG  1 
ATOM   1014 C  CG  B GLN   A 1 116 ? 21.27493  -3.52783  -7.19084  0.347 48.40735 ? 123 GLN   A CG  1 
ATOM   1015 C  CD  A GLN   A 1 116 ? 21.85707  -7.63082  -7.12809  0.653 73.17832 ? 123 GLN   A CD  1 
ATOM   1016 C  CD  B GLN   A 1 116 ? 21.47167  -4.43467  -5.98943  0.347 57.98235 ? 123 GLN   A CD  1 
ATOM   1017 O  OE1 A GLN   A 1 116 ? 22.58982  -6.75454  -6.66779  0.653 79.49915 ? 123 GLN   A OE1 1 
ATOM   1018 O  OE1 B GLN   A 1 116 ? 21.34968  -4.00299  -4.84191  0.347 54.88394 ? 123 GLN   A OE1 1 
ATOM   1019 N  NE2 A GLN   A 1 116 ? 22.30825  -8.83080  -7.47846  0.653 68.26973 ? 123 GLN   A NE2 1 
ATOM   1020 N  NE2 B GLN   A 1 116 ? 21.76781  -5.70281  -6.24890  0.347 58.56459 ? 123 GLN   A NE2 1 
ATOM   1021 N  N   A ALA   A 1 117 ? 17.71295  -3.71053  -5.83382  0.653 55.11550 ? 124 ALA   A N   1 
ATOM   1022 N  N   B ALA   A 1 117 ? 17.44179  -1.66521  -6.55539  0.347 42.57856 ? 124 ALA   A N   1 
ATOM   1023 C  CA  A ALA   A 1 117 ? 17.48963  -2.42072  -5.19247  0.653 53.65513 ? 124 ALA   A CA  1 
ATOM   1024 C  CA  B ALA   A 1 117 ? 17.17228  -0.34051  -6.00971  0.347 42.27288 ? 124 ALA   A CA  1 
ATOM   1025 C  C   A ALA   A 1 117 ? 16.20297  -2.39360  -4.36903  0.653 63.35944 ? 124 ALA   A C   1 
ATOM   1026 C  C   B ALA   A 1 117 ? 16.02630  -0.32985  -5.00344  0.347 46.99890 ? 124 ALA   A C   1 
ATOM   1027 O  O   A ALA   A 1 117 ? 15.59615  -1.32892  -4.19926  0.653 51.31806 ? 124 ALA   A O   1 
ATOM   1028 O  O   B ALA   A 1 117 ? 15.55674  0.74914   -4.62824  0.347 40.97739 ? 124 ALA   A O   1 
ATOM   1029 C  CB  A ALA   A 1 117 ? 17.47643  -1.30554  -6.23833  0.653 47.03411 ? 124 ALA   A CB  1 
ATOM   1030 C  CB  B ALA   A 1 117 ? 16.87892  0.64596   -7.14172  0.347 47.98855 ? 124 ALA   A CB  1 
ATOM   1031 N  N   A GLY   A 1 118 ? 15.76374  -3.54702  -3.86492  0.653 52.03005 ? 125 GLY   A N   1 
ATOM   1032 N  N   B GLY   A 1 118 ? 15.55892  -1.49334  -4.56275  0.347 48.86775 ? 125 GLY   A N   1 
ATOM   1033 C  CA  A GLY   A 1 118 ? 14.67472  -3.56869  -2.90593  0.653 51.06954 ? 125 GLY   A CA  1 
ATOM   1034 C  CA  B GLY   A 1 118 ? 14.53233  -1.56398  -3.54518  0.347 39.10355 ? 125 GLY   A CA  1 
ATOM   1035 C  C   A GLY   A 1 118 ? 13.40052  -4.28258  -3.31734  0.653 53.21107 ? 125 GLY   A C   1 
ATOM   1036 C  C   B GLY   A 1 118 ? 13.14423  -1.90363  -4.03504  0.347 36.19276 ? 125 GLY   A C   1 
ATOM   1037 O  O   A GLY   A 1 118 ? 12.74200  -4.90056  -2.47472  0.653 47.25365 ? 125 GLY   A O   1 
ATOM   1038 O  O   B GLY   A 1 118 ? 12.20349  -1.88007  -3.23311  0.347 36.63350 ? 125 GLY   A O   1 
ATOM   1039 N  N   A ALA   A 1 119 ? 13.03809  -4.20976  -4.59673  0.653 37.19495 ? 126 ALA   A N   1 
ATOM   1040 N  N   B ALA   A 1 119 ? 12.98188  -2.21695  -5.31727  0.347 34.38104 ? 126 ALA   A N   1 
ATOM   1041 C  CA  A ALA   A 1 119 ? 11.74206  -4.70151  -5.04693  0.653 31.35142 ? 126 ALA   A CA  1 
ATOM   1042 C  CA  B ALA   A 1 119 ? 11.67731  -2.60902  -5.81988  0.347 31.93984 ? 126 ALA   A CA  1 
ATOM   1043 C  C   A ALA   A 1 119 ? 11.64844  -6.22201  -4.91292  0.653 30.39380 ? 126 ALA   A C   1 
ATOM   1044 C  C   B ALA   A 1 119 ? 11.26362  -3.96154  -5.24596  0.347 39.23352 ? 126 ALA   A C   1 
ATOM   1045 O  O   A ALA   A 1 119 ? 12.62120  -6.91540  -4.60474  0.653 40.28730 ? 126 ALA   A O   1 
ATOM   1046 O  O   B ALA   A 1 119 ? 12.06616  -4.71263  -4.68623  0.347 40.35793 ? 126 ALA   A O   1 
ATOM   1047 C  CB  A ALA   A 1 119 ? 11.48427  -4.28687  -6.49507  0.653 36.19248 ? 126 ALA   A CB  1 
ATOM   1048 C  CB  B ALA   A 1 119 ? 11.68006  -2.67023  -7.34667  0.347 30.01362 ? 126 ALA   A CB  1 
ATOM   1049 N  N   A ASP   A 1 120 ? 10.44500  -6.74034  -5.15288  0.653 35.46098 ? 127 ASP   A N   1 
ATOM   1050 N  N   B ASP   A 1 120 ? 9.98298   -4.26264  -5.39545  0.347 35.62981 ? 127 ASP   A N   1 
ATOM   1051 C  CA  A ASP   A 1 120 ? 10.18910  -8.17136  -5.12674  0.653 34.24784 ? 127 ASP   A CA  1 
ATOM   1052 C  CA  B ASP   A 1 120 ? 9.41793   -5.54446  -5.01319  0.347 29.43537 ? 127 ASP   A CA  1 
ATOM   1053 C  C   A ASP   A 1 120 ? 9.47683   -8.58272  -6.40955  0.653 26.17469 ? 127 ASP   A C   1 
ATOM   1054 C  C   B ASP   A 1 120 ? 9.21027   -6.41060  -6.24986  0.347 27.63768 ? 127 ASP   A C   1 
ATOM   1055 O  O   A ASP   A 1 120 ? 9.03908   -7.74787  -7.20301  0.653 28.07330 ? 127 ASP   A O   1 
ATOM   1056 O  O   B ASP   A 1 120 ? 9.07058   -5.91267  -7.36938  0.347 26.91721 ? 127 ASP   A O   1 
ATOM   1057 C  CB  A ASP   A 1 120 ? 9.36042   -8.57634  -3.89939  0.653 32.63284 ? 127 ASP   A CB  1 
ATOM   1058 C  CB  B ASP   A 1 120 ? 8.09576   -5.34879  -4.26718  0.347 37.20713 ? 127 ASP   A CB  1 
ATOM   1059 C  CG  A ASP   A 1 120 ? 7.95336   -8.01803  -3.93460  0.653 39.75966 ? 127 ASP   A CG  1 
ATOM   1060 C  CG  B ASP   A 1 120 ? 8.26118   -4.55919  -2.98310  0.347 44.95538 ? 127 ASP   A CG  1 
ATOM   1061 O  OD1 A ASP   A 1 120 ? 7.79386   -6.78447  -3.81956  0.653 49.46836 ? 127 ASP   A OD1 1 
ATOM   1062 O  OD1 B ASP   A 1 120 ? 8.49267   -3.33218  -3.05863  0.347 49.51556 ? 127 ASP   A OD1 1 
ATOM   1063 O  OD2 A ASP   A 1 120 ? 7.00584   -8.81810  -4.08321  0.653 35.67761 ? 127 ASP   A OD2 1 
ATOM   1064 O  OD2 B ASP   A 1 120 ? 8.16626   -5.16765  -1.89986  0.347 56.65551 ? 127 ASP   A OD2 1 
ATOM   1065 N  N   A ILE   A 1 121 ? 9.35448   -9.89865  -6.59717  0.653 28.46554 ? 128 ILE   A N   1 
ATOM   1066 N  N   B ILE   A 1 121 ? 9.20984   -7.72771  -6.03506  0.347 26.81853 ? 128 ILE   A N   1 
ATOM   1067 C  CA  A ILE   A 1 121 ? 8.84762   -10.44408 -7.85414  0.653 23.64277 ? 128 ILE   A CA  1 
ATOM   1068 C  CA  B ILE   A 1 121 ? 8.93104   -8.64925  -7.13208  0.347 27.30036 ? 128 ILE   A CA  1 
ATOM   1069 C  C   A ILE   A 1 121 ? 7.45954   -9.90388  -8.17974  0.653 29.14600 ? 128 ILE   A C   1 
ATOM   1070 C  C   B ILE   A 1 121 ? 7.55026   -8.37157  -7.71161  0.347 24.00005 ? 128 ILE   A C   1 
ATOM   1071 O  O   A ILE   A 1 121 ? 7.10846   -9.73944  -9.35520  0.653 28.62444 ? 128 ILE   A O   1 
ATOM   1072 O  O   B ILE   A 1 121 ? 7.34990   -8.41371  -8.93239  0.347 28.40957 ? 128 ILE   A O   1 
ATOM   1073 C  CB  A ILE   A 1 121 ? 8.87371   -11.98492 -7.78231  0.653 26.30902 ? 128 ILE   A CB  1 
ATOM   1074 C  CB  B ILE   A 1 121 ? 9.06818   -10.10710 -6.65234  0.347 27.66640 ? 128 ILE   A CB  1 
ATOM   1075 C  CG1 A ILE   A 1 121 ? 10.32508  -12.48014 -7.77685  0.653 36.10528 ? 128 ILE   A CG1 1 
ATOM   1076 C  CG1 B ILE   A 1 121 ? 10.53881  -10.52423 -6.62617  0.347 40.76838 ? 128 ILE   A CG1 1 
ATOM   1077 C  CG2 A ILE   A 1 121 ? 8.07355   -12.61237 -8.91769  0.653 25.64593 ? 128 ILE   A CG2 1 
ATOM   1078 C  CG2 B ILE   A 1 121 ? 8.28067   -11.05075 -7.55110  0.347 28.32567 ? 128 ILE   A CG2 1 
ATOM   1079 C  CD1 A ILE   A 1 121 ? 10.47632  -13.98296 -7.64883  0.653 32.97366 ? 128 ILE   A CD1 1 
ATOM   1080 C  CD1 B ILE   A 1 121 ? 10.80086  -11.77328 -5.81054  0.347 39.19834 ? 128 ILE   A CD1 1 
ATOM   1081 N  N   A SER   A 1 122 ? 6.65528   -9.59746  -7.15944  0.653 29.11912 ? 129 SER   A N   1 
ATOM   1082 N  N   B SER   A 1 122 ? 6.58029   -8.06664  -6.84621  0.347 27.83757 ? 129 SER   A N   1 
ATOM   1083 C  CA  A SER   A 1 122 ? 5.28599   -9.15347  -7.40860  0.653 34.64359 ? 129 SER   A CA  1 
ATOM   1084 C  CA  B SER   A 1 122 ? 5.22290   -7.79205  -7.30087  0.347 30.03257 ? 129 SER   A CA  1 
ATOM   1085 C  C   A SER   A 1 122 ? 5.21832   -7.87058  -8.23001  0.653 28.78398 ? 129 SER   A C   1 
ATOM   1086 C  C   B SER   A 1 122 ? 5.17958   -6.71644  -8.37566  0.347 34.95500 ? 129 SER   A C   1 
ATOM   1087 O  O   A SER   A 1 122 ? 4.14592   -7.53532  -8.74463  0.653 27.28668 ? 129 SER   A O   1 
ATOM   1088 O  O   B SER   A 1 122 ? 4.16460   -6.58745  -9.06940  0.347 29.73842 ? 129 SER   A O   1 
ATOM   1089 C  CB  A SER   A 1 122 ? 4.54688   -8.94516  -6.08852  0.653 26.03231 ? 129 SER   A CB  1 
ATOM   1090 C  CB  B SER   A 1 122 ? 4.34775   -7.37882  -6.11482  0.347 35.57943 ? 129 SER   A CB  1 
ATOM   1091 O  OG  A SER   A 1 122 ? 4.85765   -7.68242  -5.53373  0.653 30.27243 ? 129 SER   A OG  1 
ATOM   1092 O  OG  B SER   A 1 122 ? 4.90408   -6.26963  -5.42854  0.347 35.54102 ? 129 SER   A OG  1 
ATOM   1093 N  N   A MET   A 1 123 ? 6.32137   -7.14019  -8.35823  0.653 24.86312 ? 130 MET   A N   1 
ATOM   1094 N  N   B MET   A 1 123 ? 6.25317   -5.94376  -8.53121  0.347 24.52116 ? 130 MET   A N   1 
ATOM   1095 C  CA  A MET   A 1 123 ? 6.32794   -5.87130  -9.07612  0.653 26.25948 ? 130 MET   A CA  1 
ATOM   1096 C  CA  B MET   A 1 123 ? 6.31367   -4.89118  -9.53744  0.347 33.13562 ? 130 MET   A CA  1 
ATOM   1097 C  C   A MET   A 1 123 ? 6.67725   -6.02671  -10.55515 0.653 22.72373 ? 130 MET   A C   1 
ATOM   1098 C  C   B MET   A 1 123 ? 6.61742   -5.41804  -10.93462 0.347 25.67553 ? 130 MET   A C   1 
ATOM   1099 O  O   A MET   A 1 123 ? 6.87675   -5.02015  -11.24271 0.653 27.23751 ? 130 MET   A O   1 
ATOM   1100 O  O   B MET   A 1 123 ? 6.62675   -4.62785  -11.88540 0.347 23.34828 ? 130 MET   A O   1 
ATOM   1101 C  CB  A MET   A 1 123 ? 7.29581   -4.89974  -8.39316  0.653 29.20366 ? 130 MET   A CB  1 
ATOM   1102 C  CB  B MET   A 1 123 ? 7.36685   -3.85119  -9.14134  0.347 26.06820 ? 130 MET   A CB  1 
ATOM   1103 C  CG  A MET   A 1 123 ? 6.99791   -4.71607  -6.90696  0.653 35.93456 ? 130 MET   A CG  1 
ATOM   1104 C  CG  B MET   A 1 123 ? 7.44977   -3.59320  -7.64407  0.347 38.21940 ? 130 MET   A CG  1 
ATOM   1105 S  SD  A MET   A 1 123 ? 8.31574   -3.91646  -5.97319  0.653 42.17522 ? 130 MET   A SD  1 
ATOM   1106 S  SD  B MET   A 1 123 ? 7.75471   -1.86392  -7.22808  0.347 38.95931 ? 130 MET   A SD  1 
ATOM   1107 C  CE  A MET   A 1 123 ? 8.18265   -2.23067  -6.57157  0.653 44.84172 ? 130 MET   A CE  1 
ATOM   1108 C  CE  B MET   A 1 123 ? 7.09717   -1.79938  -5.56229  0.347 34.82415 ? 130 MET   A CE  1 
ATOM   1109 N  N   A ILE   A 1 124 ? 6.70618   -7.26350  -11.06075 0.653 22.35700 ? 131 ILE   A N   1 
ATOM   1110 N  N   B ILE   A 1 124 ? 6.85558   -6.72155  -11.08539 0.347 24.02417 ? 131 ILE   A N   1 
ATOM   1111 C  CA  A ILE   A 1 124 ? 7.16678   -7.55246  -12.41913 0.653 23.33669 ? 131 ILE   A CA  1 
ATOM   1112 C  CA  B ILE   A 1 124 ? 7.24629   -7.29421  -12.36911 0.347 22.76319 ? 131 ILE   A CA  1 
ATOM   1113 C  C   A ILE   A 1 124 ? 6.37681   -6.77954  -13.47272 0.653 24.86287 ? 131 ILE   A C   1 
ATOM   1114 C  C   B ILE   A 1 124 ? 6.38662   -6.71233  -13.48527 0.347 24.79535 ? 131 ILE   A C   1 
ATOM   1115 O  O   A ILE   A 1 124 ? 6.93289   -6.36898  -14.50003 0.653 21.41623 ? 131 ILE   A O   1 
ATOM   1116 O  O   B ILE   A 1 124 ? 6.89657   -6.38622  -14.56376 0.347 21.73215 ? 131 ILE   A O   1 
ATOM   1117 C  CB  A ILE   A 1 124 ? 7.09564   -9.07695  -12.66176 0.653 19.13849 ? 131 ILE   A CB  1 
ATOM   1118 C  CB  B ILE   A 1 124 ? 7.17107   -8.83575  -12.34851 0.347 21.34650 ? 131 ILE   A CB  1 
ATOM   1119 C  CG1 A ILE   A 1 124 ? 7.67361   -9.44952  -14.02785 0.653 21.17478 ? 131 ILE   A CG1 1 
ATOM   1120 C  CG1 B ILE   A 1 124 ? 7.57803   -9.40905  -13.70932 0.347 21.84578 ? 131 ILE   A CG1 1 
ATOM   1121 C  CG2 A ILE   A 1 124 ? 5.66068   -9.59417  -12.50672 0.653 18.55621 ? 131 ILE   A CG2 1 
ATOM   1122 C  CG2 B ILE   A 1 124 ? 5.78614   -9.32573  -11.92682 0.347 21.74905 ? 131 ILE   A CG2 1 
ATOM   1123 C  CD1 A ILE   A 1 124 ? 7.90852   -10.94046 -14.19774 0.653 24.45634 ? 131 ILE   A CD1 1 
ATOM   1124 C  CD1 B ILE   A 1 124 ? 7.87521   -10.89361 -13.68898 0.347 25.37425 ? 131 ILE   A CD1 1 
ATOM   1125 N  N   . GLY   A 1 125 ? 5.08058   -6.56628  -13.24126 1.000 24.61224 ? 132 GLY   A N   1 
ATOM   1126 C  CA  . GLY   A 1 125 ? 4.22678   -5.98865  -14.26647 1.000 24.21740 ? 132 GLY   A CA  1 
ATOM   1127 C  C   . GLY   A 1 125 ? 4.60511   -4.56584  -14.62753 1.000 31.01965 ? 132 GLY   A C   1 
ATOM   1128 O  O   . GLY   A 1 125 ? 4.35183   -4.11586  -15.74815 1.000 28.63160 ? 132 GLY   A O   1 
ATOM   1129 N  N   . GLN   A 1 126 ? 5.20600   -3.83758  -13.68916 1.000 23.97794 ? 133 GLN   A N   1 
ATOM   1130 C  CA  . GLN   A 1 126 ? 5.62287   -2.46509  -13.95303 1.000 29.26805 ? 133 GLN   A CA  1 
ATOM   1131 C  C   . GLN   A 1 126 ? 6.74758   -2.38189  -14.97450 1.000 32.87936 ? 133 GLN   A C   1 
ATOM   1132 O  O   . GLN   A 1 126 ? 7.09099   -1.27812  -15.40693 1.000 35.73871 ? 133 GLN   A O   1 
ATOM   1133 C  CB  . GLN   A 1 126 ? 6.06192   -1.79202  -12.65345 1.000 37.57116 ? 133 GLN   A CB  1 
ATOM   1134 C  CG  . GLN   A 1 126 ? 5.01425   -1.82297  -11.55289 1.000 45.52608 ? 133 GLN   A CG  1 
ATOM   1135 C  CD  . GLN   A 1 126 ? 5.52570   -1.25251  -10.24435 1.000 56.30238 ? 133 GLN   A CD  1 
ATOM   1136 O  OE1 . GLN   A 1 126 ? 6.25347   -0.25383  -10.22713 1.000 43.43713 ? 133 GLN   A OE1 1 
ATOM   1137 N  NE2 . GLN   A 1 126 ? 5.15530   -1.89054  -9.13744  1.000 52.46523 ? 133 GLN   A NE2 1 
ATOM   1138 N  N   . PHE   A 1 127 ? 7.32172   -3.51687  -15.36893 1.000 25.27193 ? 134 PHE   A N   1 
ATOM   1139 C  CA  . PHE   A 1 127 ? 8.45546   -3.55753  -16.28420 1.000 27.79747 ? 134 PHE   A CA  1 
ATOM   1140 C  C   . PHE   A 1 127 ? 8.10047   -4.24658  -17.59214 1.000 27.22765 ? 134 PHE   A C   1 
ATOM   1141 O  O   . PHE   A 1 127 ? 8.99648   -4.55879  -18.38578 1.000 26.89974 ? 134 PHE   A O   1 
ATOM   1142 C  CB  . PHE   A 1 127 ? 9.61968   -4.24628  -15.57619 1.000 21.40847 ? 134 PHE   A CB  1 
ATOM   1143 C  CG  . PHE   A 1 127 ? 9.99739   -3.56635  -14.30323 1.000 26.77513 ? 134 PHE   A CG  1 
ATOM   1144 C  CD1 . PHE   A 1 127 ? 10.45957  -2.26053  -14.31140 1.000 47.77278 ? 134 PHE   A CD1 1 
ATOM   1145 C  CD2 . PHE   A 1 127 ? 9.69211   -4.14859  -13.09084 1.000 28.69713 ? 134 PHE   A CD2 1 
ATOM   1146 C  CE1 . PHE   A 1 127 ? 10.75732  -1.61245  -13.13128 1.000 38.94242 ? 134 PHE   A CE1 1 
ATOM   1147 C  CE2 . PHE   A 1 127 ? 9.96766   -3.50655  -11.90598 1.000 40.68273 ? 134 PHE   A CE2 1 
ATOM   1148 C  CZ  . PHE   A 1 127 ? 10.49831  -2.23418  -11.92508 1.000 41.55365 ? 134 PHE   A CZ  1 
ATOM   1149 N  N   . GLY   A 1 128 ? 6.81381   -4.49160  -17.83297 1.000 20.74028 ? 135 GLY   A N   1 
ATOM   1150 C  CA  . GLY   A 1 128 ? 6.36379   -4.97091  -19.11746 1.000 21.82577 ? 135 GLY   A CA  1 
ATOM   1151 C  C   . GLY   A 1 128 ? 6.60334   -6.43608  -19.38579 1.000 24.23005 ? 135 GLY   A C   1 
ATOM   1152 O  O   . GLY   A 1 128 ? 6.38546   -6.87579  -20.51877 1.000 28.62171 ? 135 GLY   A O   1 
ATOM   1153 N  N   . VAL   A 1 129 ? 7.02601   -7.21061  -18.38386 1.000 19.37705 ? 136 VAL   A N   1 
ATOM   1154 C  CA  . VAL   A 1 129 ? 7.32997   -8.62475  -18.58404 1.000 15.82241 ? 136 VAL   A CA  1 
ATOM   1155 C  C   . VAL   A 1 129 ? 6.47158   -9.47996  -17.65671 1.000 19.65899 ? 136 VAL   A C   1 
ATOM   1156 O  O   . VAL   A 1 129 ? 6.85534   -10.59634 -17.28556 1.000 18.67861 ? 136 VAL   A O   1 
ATOM   1157 C  CB  . VAL   A 1 129 ? 8.83094   -8.89130  -18.37006 1.000 17.10048 ? 136 VAL   A CB  1 
ATOM   1158 C  CG1 . VAL   A 1 129 ? 9.63636   -8.25958  -19.49529 1.000 22.50997 ? 136 VAL   A CG1 1 
ATOM   1159 C  CG2 . VAL   A 1 129 ? 9.28654   -8.32580  -17.03172 1.000 20.43718 ? 136 VAL   A CG2 1 
ATOM   1160 N  N   . GLY   A 1 130 ? 5.28579   -8.97340  -17.30431 1.000 19.22622 ? 137 GLY   A N   1 
ATOM   1161 C  CA  . GLY   A 1 130 ? 4.39444   -9.69402  -16.41174 1.000 17.81107 ? 137 GLY   A CA  1 
ATOM   1162 C  C   . GLY   A 1 130 ? 3.95384   -11.04844 -16.93248 1.000 21.59671 ? 137 GLY   A C   1 
ATOM   1163 O  O   . GLY   A 1 130 ? 3.60577   -11.92623 -16.13106 1.000 17.69373 ? 137 GLY   A O   1 
ATOM   1164 N  N   . PHE   A 1 131 ? 3.96094   -11.24278 -18.25678 1.000 16.37350 ? 138 PHE   A N   1 
ATOM   1165 C  CA  . PHE   A 1 131 ? 3.57363   -12.53669 -18.81785 1.000 16.65049 ? 138 PHE   A CA  1 
ATOM   1166 C  C   . PHE   A 1 131 ? 4.39083   -13.67478 -18.21986 1.000 17.69165 ? 138 PHE   A C   1 
ATOM   1167 O  O   . PHE   A 1 131 ? 3.85903   -14.75729 -17.94914 1.000 17.11965 ? 138 PHE   A O   1 
ATOM   1168 C  CB  . PHE   A 1 131 ? 3.73897   -12.54450 -20.34108 1.000 20.13888 ? 138 PHE   A CB  1 
ATOM   1169 C  CG  . PHE   A 1 131 ? 3.74992   -13.93634 -20.93102 1.000 20.51397 ? 138 PHE   A CG  1 
ATOM   1170 C  CD1 . PHE   A 1 131 ? 2.55778   -14.60641 -21.15948 1.000 19.26791 ? 138 PHE   A CD1 1 
ATOM   1171 C  CD2 . PHE   A 1 131 ? 4.94501   -14.57625 -21.23939 1.000 20.09573 ? 138 PHE   A CD2 1 
ATOM   1172 C  CE1 . PHE   A 1 131 ? 2.54985   -15.89154 -21.68590 1.000 17.18420 ? 138 PHE   A CE1 1 
ATOM   1173 C  CE2 . PHE   A 1 131 ? 4.94468   -15.86948 -21.76391 1.000 18.06722 ? 138 PHE   A CE2 1 
ATOM   1174 C  CZ  . PHE   A 1 131 ? 3.74428   -16.52162 -21.98749 1.000 19.00317 ? 138 PHE   A CZ  1 
ATOM   1175 N  N   . TYR   A 1 132 ? 5.69386   -13.45422 -18.02052 1.000 17.03103 ? 139 TYR   A N   1 
ATOM   1176 C  CA  . TYR   A 1 132 ? 6.56446   -14.54714 -17.61034 1.000 16.84178 ? 139 TYR   A CA  1 
ATOM   1177 C  C   . TYR   A 1 132 ? 6.31714   -14.98638 -16.17134 1.000 18.20620 ? 139 TYR   A C   1 
ATOM   1178 O  O   . TYR   A 1 132 ? 6.82866   -16.03694 -15.77062 1.000 17.02245 ? 139 TYR   A O   1 
ATOM   1179 C  CB  . TYR   A 1 132 ? 8.03278   -14.15203 -17.83478 1.000 15.48605 ? 139 TYR   A CB  1 
ATOM   1180 C  CG  . TYR   A 1 132 ? 8.30578   -13.86836 -19.29916 1.000 17.67990 ? 139 TYR   A CG  1 
ATOM   1181 C  CD1 . TYR   A 1 132 ? 8.56601   -14.90135 -20.18434 1.000 17.53045 ? 139 TYR   A CD1 1 
ATOM   1182 C  CD2 . TYR   A 1 132 ? 8.24997   -12.57312 -19.80319 1.000 17.23448 ? 139 TYR   A CD2 1 
ATOM   1183 C  CE1 . TYR   A 1 132 ? 8.79662   -14.65535 -21.53837 1.000 18.46792 ? 139 TYR   A CE1 1 
ATOM   1184 C  CE2 . TYR   A 1 132 ? 8.47289   -12.31416 -21.14971 1.000 19.30449 ? 139 TYR   A CE2 1 
ATOM   1185 C  CZ  . TYR   A 1 132 ? 8.74265   -13.36156 -22.01220 1.000 21.15886 ? 139 TYR   A CZ  1 
ATOM   1186 O  OH  . TYR   A 1 132 ? 8.96227   -13.11088 -23.34831 1.000 20.55887 ? 139 TYR   A OH  1 
ATOM   1187 N  N   . SER   A 1 133 ? 5.52364   -14.23874 -15.39882 1.000 17.02818 ? 140 SER   A N   1 
ATOM   1188 C  CA  . SER   A 1 133 ? 5.11695   -14.72709 -14.08449 1.000 16.68448 ? 140 SER   A CA  1 
ATOM   1189 C  C   . SER   A 1 133 ? 4.23737   -15.96572 -14.17290 1.000 16.24646 ? 140 SER   A C   1 
ATOM   1190 O  O   . SER   A 1 133 ? 3.99531   -16.60673 -13.14287 1.000 17.30540 ? 140 SER   A O   1 
ATOM   1191 C  CB  . SER   A 1 133 ? 4.38407   -13.63253 -13.30024 1.000 17.72514 ? 140 SER   A CB  1 
ATOM   1192 O  OG  . SER   A 1 133 ? 3.12237   -13.33886 -13.87045 1.000 19.27538 ? 140 SER   A OG  1 
ATOM   1193 N  N   . ALA   A 1 134 ? 3.75781   -16.31754 -15.36915 1.000 16.38429 ? 141 ALA   A N   1 
ATOM   1194 C  CA  . ALA   A 1 134 ? 3.04902   -17.58506 -15.54010 1.000 17.43100 ? 141 ALA   A CA  1 
ATOM   1195 C  C   . ALA   A 1 134 ? 3.88083   -18.76567 -15.05515 1.000 16.34464 ? 141 ALA   A C   1 
ATOM   1196 O  O   . ALA   A 1 134 ? 3.32590   -19.76187 -14.57502 1.000 16.25986 ? 141 ALA   A O   1 
ATOM   1197 C  CB  . ALA   A 1 134 ? 2.66987   -17.77333 -17.01183 1.000 17.19787 ? 141 ALA   A CB  1 
ATOM   1198 N  N   . TYR   A 1 135 ? 5.21529   -18.67094 -15.15666 1.000 16.54461 ? 142 TYR   A N   1 
ATOM   1199 C  CA  . TYR   A 1 135 ? 6.08583   -19.76720 -14.74488 1.000 18.59357 ? 142 TYR   A CA  1 
ATOM   1200 C  C   . TYR   A 1 135 ? 6.26137   -19.84620 -13.23142 1.000 17.36659 ? 142 TYR   A C   1 
ATOM   1201 O  O   . TYR   A 1 135 ? 6.97360   -20.73124 -12.74708 1.000 18.46836 ? 142 TYR   A O   1 
ATOM   1202 C  CB  . TYR   A 1 135 ? 7.43579   -19.64693 -15.46978 1.000 16.40088 ? 142 TYR   A CB  1 
ATOM   1203 C  CG  . TYR   A 1 135 ? 7.24695   -19.93604 -16.94232 1.000 16.80611 ? 142 TYR   A CG  1 
ATOM   1204 C  CD1 . TYR   A 1 135 ? 7.25775   -21.24316 -17.42519 1.000 17.94756 ? 142 TYR   A CD1 1 
ATOM   1205 C  CD2 . TYR   A 1 135 ? 6.96016   -18.91092 -17.83563 1.000 17.13178 ? 142 TYR   A CD2 1 
ATOM   1206 C  CE1 . TYR   A 1 135 ? 7.04215   -21.51180 -18.77441 1.000 16.60123 ? 142 TYR   A CE1 1 
ATOM   1207 C  CE2 . TYR   A 1 135 ? 6.74225   -19.16621 -19.18217 1.000 17.15755 ? 142 TYR   A CE2 1 
ATOM   1208 C  CZ  . TYR   A 1 135 ? 6.77962   -20.46602 -19.64502 1.000 20.84824 ? 142 TYR   A CZ  1 
ATOM   1209 O  OH  . TYR   A 1 135 ? 6.56279   -20.70443 -20.98463 1.000 18.01827 ? 142 TYR   A OH  1 
ATOM   1210 N  N   . LEU   A 1 136 ? 5.59631   -18.97352 -12.47107 1.000 18.59762 ? 143 LEU   A N   1 
ATOM   1211 C  CA  . LEU   A 1 136 ? 5.46162   -19.20848 -11.03990 1.000 21.56519 ? 143 LEU   A CA  1 
ATOM   1212 C  C   . LEU   A 1 136 ? 4.61223   -20.44142 -10.75412 1.000 20.36347 ? 143 LEU   A C   1 
ATOM   1213 O  O   . LEU   A 1 136 ? 4.81428   -21.10671 -9.73300  1.000 20.54729 ? 143 LEU   A O   1 
ATOM   1214 C  CB  . LEU   A 1 136 ? 4.84518   -17.98239 -10.36137 1.000 22.08229 ? 143 LEU   A CB  1 
ATOM   1215 C  CG  . LEU   A 1 136 ? 5.68066   -16.69643 -10.29568 1.000 19.42497 ? 143 LEU   A CG  1 
ATOM   1216 C  CD1 . LEU   A 1 136 ? 4.80669   -15.54173 -9.83319  1.000 21.75525 ? 143 LEU   A CD1 1 
ATOM   1217 C  CD2 . LEU   A 1 136 ? 6.90177   -16.86714 -9.38583  1.000 20.52312 ? 143 LEU   A CD2 1 
ATOM   1218 N  N   . VAL   A 1 137 ? 3.66222   -20.76714 -11.63677 1.000 18.57539 ? 144 VAL   A N   1 
ATOM   1219 C  CA  . VAL   A 1 137 ? 2.71343   -21.83780 -11.33914 1.000 19.30727 ? 144 VAL   A CA  1 
ATOM   1220 C  C   . VAL   A 1 137 ? 2.62391   -22.88034 -12.45012 1.000 19.22962 ? 144 VAL   A C   1 
ATOM   1221 O  O   . VAL   A 1 137 ? 2.09211   -23.97419 -12.23093 1.000 24.83058 ? 144 VAL   A O   1 
ATOM   1222 C  CB  . VAL   A 1 137 ? 1.31646   -21.26582 -11.03287 1.000 20.61071 ? 144 VAL   A CB  1 
ATOM   1223 C  CG1 . VAL   A 1 137 ? 1.36088   -20.34126 -9.82315  1.000 23.54469 ? 144 VAL   A CG1 1 
ATOM   1224 C  CG2 . VAL   A 1 137 ? 0.75977   -20.52975 -12.23742 1.000 18.31121 ? 144 VAL   A CG2 1 
ATOM   1225 N  N   . ALA   A 1 138 ? 3.14454   -22.57197 -13.63638 1.000 17.68993 ? 145 ALA   A N   1 
ATOM   1226 C  CA  . ALA   A 1 138 ? 3.00462   -23.45088 -14.79172 1.000 17.51399 ? 145 ALA   A CA  1 
ATOM   1227 C  C   . ALA   A 1 138 ? 4.33576   -24.09625 -15.14922 1.000 19.30591 ? 145 ALA   A C   1 
ATOM   1228 O  O   . ALA   A 1 138 ? 5.37174   -23.42601 -15.17714 1.000 24.46474 ? 145 ALA   A O   1 
ATOM   1229 C  CB  . ALA   A 1 138 ? 2.46690   -22.69345 -16.00698 1.000 17.81489 ? 145 ALA   A CB  1 
ATOM   1230 N  N   . GLU   A 1 139 ? 4.30732   -25.40409 -15.41642 1.000 18.42011 ? 146 GLU   A N   1 
ATOM   1231 C  CA  . GLU   A 1 139 ? 5.48715   -26.06936 -15.96527 1.000 19.93909 ? 146 GLU   A CA  1 
ATOM   1232 C  C   . GLU   A 1 139 ? 5.59736   -25.87119 -17.46900 1.000 22.86797 ? 146 GLU   A C   1 
ATOM   1233 O  O   . GLU   A 1 139 ? 6.69130   -25.98905 -18.02726 1.000 23.94303 ? 146 GLU   A O   1 
ATOM   1234 C  CB  . GLU   A 1 139 ? 5.45711   -27.56318 -15.62978 1.000 21.31743 ? 146 GLU   A CB  1 
ATOM   1235 C  CG  . GLU   A 1 139 ? 4.18930   -28.28246 -16.05465 1.000 30.20504 ? 146 GLU   A CG  1 
ATOM   1236 C  CD  . GLU   A 1 139 ? 4.19155   -29.75530 -15.66381 1.000 68.81483 ? 146 GLU   A CD  1 
ATOM   1237 O  OE1 . GLU   A 1 139 ? 3.52652   -30.55532 -16.35868 1.000 51.43134 ? 146 GLU   A OE1 1 
ATOM   1238 O  OE2 . GLU   A 1 139 ? 4.85715   -30.11249 -14.66536 1.000 48.71262 ? 146 GLU   A OE2 1 
ATOM   1239 N  N   . LYS   A 1 140 ? 4.48701   -25.56426 -18.12931 1.000 18.82514 ? 147 LYS   A N   1 
ATOM   1240 C  CA  . LYS   A 1 140 ? 4.46174   -25.33451 -19.56196 1.000 18.89584 ? 147 LYS   A CA  1 
ATOM   1241 C  C   . LYS   A 1 140 ? 3.37616   -24.30763 -19.82558 1.000 19.03251 ? 147 LYS   A C   1 
ATOM   1242 O  O   . LYS   A 1 140 ? 2.34602   -24.30480 -19.14856 1.000 19.09069 ? 147 LYS   A O   1 
ATOM   1243 C  CB  . LYS   A 1 140 ? 4.19015   -26.63247 -20.33361 1.000 19.83851 ? 147 LYS   A CB  1 
ATOM   1244 C  CG  . LYS   A 1 140 ? 4.10765   -26.46538 -21.83379 1.000 18.82592 ? 147 LYS   A CG  1 
ATOM   1245 C  CD  . LYS   A 1 140 ? 3.99785   -27.82199 -22.49304 1.000 23.66578 ? 147 LYS   A CD  1 
ATOM   1246 C  CE  . LYS   A 1 140 ? 2.65776   -28.03733 -23.15463 1.000 42.06164 ? 147 LYS   A CE  1 
ATOM   1247 N  NZ  . LYS   A 1 140 ? 2.41192   -29.49748 -23.34899 1.000 43.85467 ? 147 LYS   A NZ  1 
ATOM   1248 N  N   . VAL   A 1 141 ? 3.62189   -23.41870 -20.77711 1.000 15.35090 ? 148 VAL   A N   1 
ATOM   1249 C  CA  . VAL   A 1 141 ? 2.63690   -22.41090 -21.16080 1.000 15.93173 ? 148 VAL   A CA  1 
ATOM   1250 C  C   . VAL   A 1 141 ? 2.43879   -22.48829 -22.66462 1.000 21.88320 ? 148 VAL   A C   1 
ATOM   1251 O  O   . VAL   A 1 141 ? 3.41478   -22.49362 -23.42552 1.000 16.12432 ? 148 VAL   A O   1 
ATOM   1252 C  CB  . VAL   A 1 141 ? 3.06011   -20.99000 -20.74749 1.000 17.44440 ? 148 VAL   A CB  1 
ATOM   1253 C  CG1 . VAL   A 1 141 ? 2.01906   -19.97690 -21.22683 1.000 18.89770 ? 148 VAL   A CG1 1 
ATOM   1254 C  CG2 . VAL   A 1 141 ? 3.24276   -20.89807 -19.23152 1.000 15.33111 ? 148 VAL   A CG2 1 
ATOM   1255 N  N   . THR   A 1 142 ? 1.18013   -22.56707 -23.08585 1.000 18.99560 ? 149 THR   A N   1 
ATOM   1256 C  CA  . THR   A 1 142 ? 0.80000   -22.52315 -24.48790 1.000 19.49170 ? 149 THR   A CA  1 
ATOM   1257 C  C   . THR   A 1 142 ? 0.02721   -21.23190 -24.72671 1.000 18.60071 ? 149 THR   A C   1 
ATOM   1258 O  O   . THR   A 1 142 ? -0.89368  -20.91075 -23.97191 1.000 20.78414 ? 149 THR   A O   1 
ATOM   1259 C  CB  . THR   A 1 142 ? -0.06218  -23.73119 -24.86782 1.000 19.72803 ? 149 THR   A CB  1 
ATOM   1260 O  OG1 . THR   A 1 142 ? 0.60041   -24.94847 -24.49708 1.000 24.34191 ? 149 THR   A OG1 1 
ATOM   1261 C  CG2 . THR   A 1 142 ? -0.31965  -23.74577 -26.36611 1.000 22.89006 ? 149 THR   A CG2 1 
ATOM   1262 N  N   . VAL   A 1 143 ? 0.40610   -20.48567 -25.75550 1.000 17.66081 ? 150 VAL   A N   1 
ATOM   1263 C  CA  . VAL   A 1 143 ? -0.30077  -19.26364 -26.12588 1.000 18.88635 ? 150 VAL   A CA  1 
ATOM   1264 C  C   . VAL   A 1 143 ? -0.85154  -19.44983 -27.53160 1.000 20.28029 ? 150 VAL   A C   1 
ATOM   1265 O  O   . VAL   A 1 143 ? -0.08233  -19.63203 -28.48475 1.000 20.45588 ? 150 VAL   A O   1 
ATOM   1266 C  CB  . VAL   A 1 143 ? 0.60549   -18.02612 -26.05731 1.000 17.18272 ? 150 VAL   A CB  1 
ATOM   1267 C  CG1 . VAL   A 1 143 ? -0.17239  -16.78515 -26.50541 1.000 15.15833 ? 150 VAL   A CG1 1 
ATOM   1268 C  CG2 . VAL   A 1 143 ? 1.15687   -17.84088 -24.64574 1.000 19.07818 ? 150 VAL   A CG2 1 
ATOM   1269 N  N   . ILE   A 1 144 ? -2.17645  -19.42544 -27.65537 1.000 15.85316 ? 151 ILE   A N   1 
ATOM   1270 C  CA  . ILE   A 1 144 ? -2.85953  -19.42612 -28.94397 1.000 16.56709 ? 151 ILE   A CA  1 
ATOM   1271 C  C   . ILE   A 1 144 ? -3.31290  -18.00395 -29.21768 1.000 20.26254 ? 151 ILE   A C   1 
ATOM   1272 O  O   . ILE   A 1 144 ? -3.90570  -17.36218 -28.34092 1.000 19.40234 ? 151 ILE   A O   1 
ATOM   1273 C  CB  . ILE   A 1 144 ? -4.07462  -20.36933 -28.94706 1.000 18.41236 ? 151 ILE   A CB  1 
ATOM   1274 C  CG1 . ILE   A 1 144 ? -3.77079  -21.70123 -28.26035 1.000 31.84330 ? 151 ILE   A CG1 1 
ATOM   1275 C  CG2 . ILE   A 1 144 ? -4.57933  -20.56477 -30.37137 1.000 24.51879 ? 151 ILE   A CG2 1 
ATOM   1276 C  CD1 . ILE   A 1 144 ? -2.79667  -22.54761 -28.99874 1.000 26.25515 ? 151 ILE   A CD1 1 
ATOM   1277 N  N   . THR   A 1 145 ? -3.06437  -17.50652 -30.42736 1.000 15.52886 ? 152 THR   A N   1 
ATOM   1278 C  CA  . THR   A 1 145 ? -3.39670  -16.11000 -30.68162 1.000 18.19381 ? 152 THR   A CA  1 
ATOM   1279 C  C   . THR   A 1 145 ? -3.82699  -15.90362 -32.12647 1.000 22.40038 ? 152 THR   A C   1 
ATOM   1280 O  O   . THR   A 1 145 ? -3.39136  -16.61809 -33.03391 1.000 20.85925 ? 152 THR   A O   1 
ATOM   1281 C  CB  . THR   A 1 145 ? -2.21619  -15.19060 -30.32450 1.000 22.70120 ? 152 THR   A CB  1 
ATOM   1282 O  OG1 . THR   A 1 145 ? -2.66352  -13.82768 -30.24664 1.000 20.79988 ? 152 THR   A OG1 1 
ATOM   1283 C  CG2 . THR   A 1 145 ? -1.08394  -15.32325 -31.33715 1.000 20.98633 ? 152 THR   A CG2 1 
ATOM   1284 N  N   . LYS   A 1 146 ? -4.70426  -14.91680 -32.31897 1.000 19.31397 ? 153 LYS   A N   1 
ATOM   1285 C  CA  . LYS   A 1 146 ? -5.19239  -14.52361 -33.63472 1.000 18.09014 ? 153 LYS   A CA  1 
ATOM   1286 C  C   . LYS   A 1 146 ? -5.29558  -13.00846 -33.67610 1.000 19.40766 ? 153 LYS   A C   1 
ATOM   1287 O  O   . LYS   A 1 146 ? -6.08770  -12.41714 -32.93522 1.000 20.83018 ? 153 LYS   A O   1 
ATOM   1288 C  CB  . LYS   A 1 146 ? -6.55511  -15.15406 -33.93398 1.000 18.58205 ? 153 LYS   A CB  1 
ATOM   1289 C  CG  . LYS   A 1 146 ? -7.16254  -14.73795 -35.27798 1.000 21.36693 ? 153 LYS   A CG  1 
ATOM   1290 C  CD  . LYS   A 1 146 ? -6.41344  -15.33742 -36.46636 1.000 25.71727 ? 153 LYS   A CD  1 
ATOM   1291 C  CE  . LYS   A 1 146 ? -7.11257  -15.00602 -37.78549 1.000 26.03827 ? 153 LYS   A CE  1 
ATOM   1292 N  NZ  . LYS   A 1 146 ? -7.06111  -13.55166 -38.12082 1.000 22.37999 ? 153 LYS   A NZ  1 
ATOM   1293 N  N   . HIS   A 1 147 ? -4.50194  -12.39677 -34.54335 1.000 17.72687 ? 154 HIS   A N   1 
ATOM   1294 C  CA  . HIS   A 1 147 ? -4.53716  -10.97375 -34.84174 1.000 24.32503 ? 154 HIS   A CA  1 
ATOM   1295 C  C   . HIS   A 1 147 ? -5.25237  -10.77586 -36.17663 1.000 26.83189 ? 154 HIS   A C   1 
ATOM   1296 O  O   . HIS   A 1 147 ? -5.17418  -11.63121 -37.06116 1.000 23.30043 ? 154 HIS   A O   1 
ATOM   1297 C  CB  . HIS   A 1 147 ? -3.10072  -10.43181 -34.90552 1.000 18.70152 ? 154 HIS   A CB  1 
ATOM   1298 C  CG  . HIS   A 1 147 ? -2.99799  -8.94231  -35.02541 1.000 21.96261 ? 154 HIS   A CG  1 
ATOM   1299 N  ND1 . HIS   A 1 147 ? -3.18601  -8.27642  -36.21640 1.000 23.44339 ? 154 HIS   A ND1 1 
ATOM   1300 C  CD2 . HIS   A 1 147 ? -2.66764  -7.99602  -34.11470 1.000 22.15609 ? 154 HIS   A CD2 1 
ATOM   1301 C  CE1 . HIS   A 1 147 ? -3.01218  -6.98170  -36.02791 1.000 26.79401 ? 154 HIS   A CE1 1 
ATOM   1302 N  NE2 . HIS   A 1 147 ? -2.69379  -6.78590  -34.76134 1.000 24.35199 ? 154 HIS   A NE2 1 
ATOM   1303 N  N   . ASN   A 1 148 ? -5.96196  -9.64742  -36.32101 1.000 21.45771 ? 155 ASN   A N   1 
ATOM   1304 C  CA  . ASN   A 1 148 ? -6.67981  -9.39081  -37.57288 1.000 22.64272 ? 155 ASN   A CA  1 
ATOM   1305 C  C   . ASN   A 1 148 ? -5.77475  -9.48501  -38.79982 1.000 24.64111 ? 155 ASN   A C   1 
ATOM   1306 O  O   . ASN   A 1 148 ? -6.24023  -9.84987  -39.88634 1.000 26.70083 ? 155 ASN   A O   1 
ATOM   1307 C  CB  . ASN   A 1 148 ? -7.35423  -8.01085  -37.55035 1.000 23.19419 ? 155 ASN   A CB  1 
ATOM   1308 C  CG  . ASN   A 1 148 ? -8.62938  -7.98636  -36.72907 1.000 27.80341 ? 155 ASN   A CG  1 
ATOM   1309 O  OD1 . ASN   A 1 148 ? -9.28218  -9.01403  -36.54174 1.000 26.91500 ? 155 ASN   A OD1 1 
ATOM   1310 N  ND2 . ASN   A 1 148 ? -9.01661  -6.79588  -36.26518 1.000 25.73902 ? 155 ASN   A ND2 1 
ATOM   1311 N  N   . ASP   A 1 149 ? -4.48862  -9.16634  -38.65407 1.000 24.87809 ? 156 ASP   A N   1 
ATOM   1312 C  CA  . ASP   A 1 149 ? -3.56971  -9.07455  -39.78395 1.000 26.89928 ? 156 ASP   A CA  1 
ATOM   1313 C  C   . ASP   A 1 149 ? -2.75194  -10.34223 -40.01315 1.000 33.66402 ? 156 ASP   A C   1 
ATOM   1314 O  O   . ASP   A 1 149 ? -1.81641  -10.31906 -40.82081 1.000 31.11755 ? 156 ASP   A O   1 
ATOM   1315 C  CB  . ASP   A 1 149 ? -2.61511  -7.89394  -39.59059 1.000 26.30373 ? 156 ASP   A CB  1 
ATOM   1316 C  CG  . ASP   A 1 149 ? -3.32004  -6.55814  -39.62980 1.000 41.11753 ? 156 ASP   A CG  1 
ATOM   1317 O  OD1 . ASP   A 1 149 ? -4.48154  -6.50449  -40.08292 1.000 32.80340 ? 156 ASP   A OD1 1 
ATOM   1318 O  OD2 . ASP   A 1 149 ? -2.71606  -5.56347  -39.17805 1.000 37.92507 ? 156 ASP   A OD2 1 
ATOM   1319 N  N   . ASP   A 1 150 ? -3.06328  -11.44031 -39.32963 1.000 26.67840 ? 157 ASP   A N   1 
ATOM   1320 C  CA  . ASP   A 1 150 ? -2.26239  -12.64942 -39.46863 1.000 22.33765 ? 157 ASP   A CA  1 
ATOM   1321 C  C   . ASP   A 1 150 ? -3.15378  -13.86872 -39.26056 1.000 29.13027 ? 157 ASP   A C   1 
ATOM   1322 O  O   . ASP   A 1 150 ? -4.35722  -13.75395 -39.00514 1.000 27.89577 ? 157 ASP   A O   1 
ATOM   1323 C  CB  . ASP   A 1 150 ? -1.08718  -12.64103 -38.48082 1.000 22.37096 ? 157 ASP   A CB  1 
ATOM   1324 C  CG  . ASP   A 1 150 ? 0.12388   -13.40183 -38.99305 1.000 27.85761 ? 157 ASP   A CG  1 
ATOM   1325 O  OD1 . ASP   A 1 150 ? -0.01594  -14.20931 -39.94098 1.000 27.23417 ? 157 ASP   A OD1 1 
ATOM   1326 O  OD2 . ASP   A 1 150 ? 1.22252   -13.19338 -38.43240 1.000 30.66512 ? 157 ASP   A OD2 1 
ATOM   1327 N  N   . GLU   A 1 151 ? -2.54606  -15.04492 -39.38321 1.000 27.36460 ? 158 GLU   A N   1 
ATOM   1328 C  CA  . GLU   A 1 151 ? -3.19754  -16.32218 -39.14378 1.000 27.11448 ? 158 GLU   A CA  1 
ATOM   1329 C  C   . GLU   A 1 151 ? -3.10967  -16.68891 -37.66373 1.000 22.07694 ? 158 GLU   A C   1 
ATOM   1330 O  O   . GLU   A 1 151 ? -2.40881  -16.04644 -36.87860 1.000 23.52497 ? 158 GLU   A O   1 
ATOM   1331 C  CB  . GLU   A 1 151 ? -2.55024  -17.41552 -39.99853 1.000 29.07371 ? 158 GLU   A CB  1 
ATOM   1332 C  CG  . GLU   A 1 151 ? -2.67002  -17.22562 -41.51156 1.000 43.83533 ? 158 GLU   A CG  1 
ATOM   1333 C  CD  . GLU   A 1 151 ? -3.99041  -16.60761 -41.94364 1.000 69.57932 ? 158 GLU   A CD  1 
ATOM   1334 O  OE1 . GLU   A 1 151 ? -5.05322  -17.10583 -41.51378 1.000 77.92440 ? 158 GLU   A OE1 1 
ATOM   1335 O  OE2 . GLU   A 1 151 ? -3.96737  -15.62737 -42.72080 1.000 72.85810 ? 158 GLU   A OE2 1 
ATOM   1336 N  N   . GLN   A 1 152 ? -3.82434  -17.74933 -37.28963 1.000 22.41490 ? 159 GLN   A N   1 
ATOM   1337 C  CA  . GLN   A 1 152 ? -3.80501  -18.24999 -35.91847 1.000 21.74520 ? 159 GLN   A CA  1 
ATOM   1338 C  C   . GLN   A 1 152 ? -2.54071  -19.06552 -35.66395 1.000 20.57202 ? 159 GLN   A C   1 
ATOM   1339 O  O   . GLN   A 1 152 ? -2.21815  -19.98074 -36.42937 1.000 24.13522 ? 159 GLN   A O   1 
ATOM   1340 C  CB  . GLN   A 1 152 ? -5.03491  -19.11360 -35.65012 1.000 23.78088 ? 159 GLN   A CB  1 
ATOM   1341 C  CG  . GLN   A 1 152 ? -5.28927  -19.39624 -34.17432 1.000 24.46737 ? 159 GLN   A CG  1 
ATOM   1342 C  CD  . GLN   A 1 152 ? -6.72867  -19.79799 -33.90074 1.000 27.83474 ? 159 GLN   A CD  1 
ATOM   1343 O  OE1 . GLN   A 1 152 ? -7.66115  -19.07561 -34.24413 1.000 29.39417 ? 159 GLN   A OE1 1 
ATOM   1344 N  NE2 . GLN   A 1 152 ? -6.91348  -20.95038 -33.26896 1.000 26.93250 ? 159 GLN   A NE2 1 
ATOM   1345 N  N   A TYR   A 1 153 ? -1.83952  -18.74405 -34.57781 0.500 19.43270 ? 160 TYR   A N   1 
ATOM   1346 N  N   B TYR   A 1 153 ? -1.83952  -18.74405 -34.57781 0.500 19.43270 ? 160 TYR   A N   1 
ATOM   1347 C  CA  A TYR   A 1 153 ? -0.57185  -19.37657 -34.24533 0.500 20.84487 ? 160 TYR   A CA  1 
ATOM   1348 C  CA  B TYR   A 1 153 ? -0.57185  -19.37657 -34.24533 0.500 20.84487 ? 160 TYR   A CA  1 
ATOM   1349 C  C   A TYR   A 1 153 ? -0.58736  -19.86616 -32.80371 0.500 24.71308 ? 160 TYR   A C   1 
ATOM   1350 C  C   B TYR   A 1 153 ? -0.58736  -19.86616 -32.80371 0.500 24.71308 ? 160 TYR   A C   1 
ATOM   1351 O  O   A TYR   A 1 153 ? -1.30463  -19.32894 -31.95405 0.500 20.18815 ? 160 TYR   A O   1 
ATOM   1352 O  O   B TYR   A 1 153 ? -1.30463  -19.32894 -31.95405 0.500 20.18815 ? 160 TYR   A O   1 
ATOM   1353 C  CB  A TYR   A 1 153 ? 0.60430   -18.41058 -34.44607 0.500 18.03213 ? 160 TYR   A CB  1 
ATOM   1354 C  CB  B TYR   A 1 153 ? 0.60430   -18.41058 -34.44607 0.500 18.03213 ? 160 TYR   A CB  1 
ATOM   1355 C  CG  A TYR   A 1 153 ? 0.99876   -18.21998 -35.89243 0.500 22.81097 ? 160 TYR   A CG  1 
ATOM   1356 C  CG  B TYR   A 1 153 ? 0.99876   -18.21998 -35.89243 0.500 22.81097 ? 160 TYR   A CG  1 
ATOM   1357 C  CD1 A TYR   A 1 153 ? 1.86299   -19.10735 -36.51617 0.500 26.87859 ? 160 TYR   A CD1 1 
ATOM   1358 C  CD1 B TYR   A 1 153 ? 1.86299   -19.10735 -36.51617 0.500 26.87859 ? 160 TYR   A CD1 1 
ATOM   1359 C  CD2 A TYR   A 1 153 ? 0.50933   -17.15133 -36.63291 0.500 24.48238 ? 160 TYR   A CD2 1 
ATOM   1360 C  CD2 B TYR   A 1 153 ? 0.50933   -17.15133 -36.63291 0.500 24.48238 ? 160 TYR   A CD2 1 
ATOM   1361 C  CE1 A TYR   A 1 153 ? 2.22701   -18.94282 -37.83811 0.500 27.00922 ? 160 TYR   A CE1 1 
ATOM   1362 C  CE1 B TYR   A 1 153 ? 2.22701   -18.94282 -37.83811 0.500 27.00922 ? 160 TYR   A CE1 1 
ATOM   1363 C  CE2 A TYR   A 1 153 ? 0.86728   -16.97659 -37.96047 0.500 26.68274 ? 160 TYR   A CE2 1 
ATOM   1364 C  CE2 B TYR   A 1 153 ? 0.86728   -16.97659 -37.96047 0.500 26.68274 ? 160 TYR   A CE2 1 
ATOM   1365 C  CZ  A TYR   A 1 153 ? 1.72654   -17.87589 -38.55589 0.500 30.51564 ? 160 TYR   A CZ  1 
ATOM   1366 C  CZ  B TYR   A 1 153 ? 1.72654   -17.87589 -38.55589 0.500 30.51564 ? 160 TYR   A CZ  1 
ATOM   1367 O  OH  A TYR   A 1 153 ? 2.09046   -17.71088 -39.87257 0.500 41.57435 ? 160 TYR   A OH  1 
ATOM   1368 O  OH  B TYR   A 1 153 ? 2.09046   -17.71088 -39.87257 0.500 41.57435 ? 160 TYR   A OH  1 
ATOM   1369 N  N   . ALA   A 1 154 ? 0.22696   -20.88607 -32.53514 1.000 17.86303 ? 161 ALA   A N   1 
ATOM   1370 C  CA  . ALA   A 1 154 ? 0.41837   -21.42797 -31.19445 1.000 18.65528 ? 161 ALA   A CA  1 
ATOM   1371 C  C   . ALA   A 1 154 ? 1.88560   -21.29423 -30.80438 1.000 21.87169 ? 161 ALA   A C   1 
ATOM   1372 O  O   . ALA   A 1 154 ? 2.76309   -21.84404 -31.48074 1.000 20.44950 ? 161 ALA   A O   1 
ATOM   1373 C  CB  . ALA   A 1 154 ? -0.00607  -22.89674 -31.12909 1.000 25.08580 ? 161 ALA   A CB  1 
ATOM   1374 N  N   . TRP   A 1 155 ? 2.14059   -20.57945 -29.71319 1.000 16.22421 ? 162 TRP   A N   1 
ATOM   1375 C  CA  . TRP   A 1 155 ? 3.44687   -20.46943 -29.07537 1.000 17.19823 ? 162 TRP   A CA  1 
ATOM   1376 C  C   . TRP   A 1 155 ? 3.47418   -21.39760 -27.86815 1.000 19.08376 ? 162 TRP   A C   1 
ATOM   1377 O  O   . TRP   A 1 155 ? 2.45210   -21.60956 -27.20954 1.000 19.67575 ? 162 TRP   A O   1 
ATOM   1378 C  CB  . TRP   A 1 155 ? 3.68209   -19.01236 -28.65646 1.000 17.85126 ? 162 TRP   A CB  1 
ATOM   1379 C  CG  . TRP   A 1 155 ? 4.93379   -18.64139 -27.87428 1.000 18.85949 ? 162 TRP   A CG  1 
ATOM   1380 C  CD1 . TRP   A 1 155 ? 6.01003   -17.94062 -28.35067 1.000 17.82365 ? 162 TRP   A CD1 1 
ATOM   1381 C  CD2 . TRP   A 1 155 ? 5.17885   -18.83941 -26.46931 1.000 17.89361 ? 162 TRP   A CD2 1 
ATOM   1382 N  NE1 . TRP   A 1 155 ? 6.92179   -17.72924 -27.34315 1.000 16.81949 ? 162 TRP   A NE1 1 
ATOM   1383 C  CE2 . TRP   A 1 155 ? 6.43559   -18.27304 -26.18174 1.000 18.69636 ? 162 TRP   A CE2 1 
ATOM   1384 C  CE3 . TRP   A 1 155 ? 4.46677   -19.45891 -25.43418 1.000 16.79946 ? 162 TRP   A CE3 1 
ATOM   1385 C  CZ2 . TRP   A 1 155 ? 6.99792   -18.30672 -24.90341 1.000 19.37669 ? 162 TRP   A CZ2 1 
ATOM   1386 C  CZ3 . TRP   A 1 155 ? 5.02873   -19.49668 -24.16768 1.000 18.36780 ? 162 TRP   A CZ3 1 
ATOM   1387 C  CH2 . TRP   A 1 155 ? 6.28211   -18.91677 -23.91359 1.000 18.88210 ? 162 TRP   A CH2 1 
ATOM   1388 N  N   . GLU   A 1 156 ? 4.64058   -21.96949 -27.57958 1.000 16.55708 ? 163 GLU   A N   1 
ATOM   1389 C  CA  . GLU   A 1 156 ? 4.71627   -22.89630 -26.46271 1.000 15.46152 ? 163 GLU   A CA  1 
ATOM   1390 C  C   . GLU   A 1 156 ? 6.12195   -22.92130 -25.88328 1.000 19.21961 ? 163 GLU   A C   1 
ATOM   1391 O  O   . GLU   A 1 156 ? 7.10655   -22.91885 -26.62950 1.000 17.30516 ? 163 GLU   A O   1 
ATOM   1392 C  CB  . GLU   A 1 156 ? 4.31572   -24.30943 -26.89264 1.000 20.82075 ? 163 GLU   A CB  1 
ATOM   1393 C  CG  . GLU   A 1 156 ? 4.00128   -25.23612 -25.74290 1.000 26.65836 ? 163 GLU   A CG  1 
ATOM   1394 C  CD  . GLU   A 1 156 ? 3.30721   -26.50219 -26.20317 1.000 43.15512 ? 163 GLU   A CD  1 
ATOM   1395 O  OE1 . GLU   A 1 156 ? 3.99647   -27.39130 -26.75036 1.000 33.73798 ? 163 GLU   A OE1 1 
ATOM   1396 O  OE2 . GLU   A 1 156 ? 2.07413   -26.60520 -26.02347 1.000 32.71409 ? 163 GLU   A OE2 1 
ATOM   1397 N  N   . SER   A 1 157 ? 6.20888   -22.96268 -24.55493 1.000 18.25912 ? 164 SER   A N   1 
ATOM   1398 C  CA  . SER   A 1 157 ? 7.50628   -23.14329 -23.91624 1.000 15.79341 ? 164 SER   A CA  1 
ATOM   1399 C  C   . SER   A 1 157 ? 7.35447   -23.81799 -22.56301 1.000 18.13406 ? 164 SER   A C   1 
ATOM   1400 O  O   . SER   A 1 157 ? 6.45068   -23.49436 -21.78219 1.000 19.05025 ? 164 SER   A O   1 
ATOM   1401 C  CB  . SER   A 1 157 ? 8.25100   -21.81935 -23.73650 1.000 16.28855 ? 164 SER   A CB  1 
ATOM   1402 O  OG  . SER   A 1 157 ? 9.53138   -22.06958 -23.16014 1.000 17.18886 ? 164 SER   A OG  1 
ATOM   1403 N  N   . SER   A 1 158 ? 8.26035   -24.75402 -22.29283 1.000 17.44213 ? 165 SER   A N   1 
ATOM   1404 C  CA  . SER   A 1 158 ? 8.47100   -25.28418 -20.95242 1.000 20.33846 ? 165 SER   A CA  1 
ATOM   1405 C  C   . SER   A 1 158 ? 9.72872   -24.70066 -20.31802 1.000 21.21847 ? 165 SER   A C   1 
ATOM   1406 O  O   . SER   A 1 158 ? 10.36533  -25.35150 -19.48017 1.000 24.34622 ? 165 SER   A O   1 
ATOM   1407 C  CB  . SER   A 1 158 ? 8.54784   -26.80888 -20.99414 1.000 25.52674 ? 165 SER   A CB  1 
ATOM   1408 O  OG  . SER   A 1 158 ? 7.31484   -27.36629 -21.42111 1.000 26.08018 ? 165 SER   A OG  1 
ATOM   1409 N  N   . ALA   A 1 159 ? 10.09412  -23.48667 -20.71519 1.000 18.83215 ? 166 ALA   A N   1 
ATOM   1410 C  CA  . ALA   A 1 159 ? 11.33353  -22.80574 -20.30457 1.000 21.69249 ? 166 ALA   A CA  1 
ATOM   1411 C  C   . ALA   A 1 159 ? 12.49819  -23.66443 -20.80857 1.000 23.92723 ? 166 ALA   A C   1 
ATOM   1412 O  O   . ALA   A 1 159 ? 12.40693  -24.24501 -21.90080 1.000 27.86350 ? 166 ALA   A O   1 
ATOM   1413 C  CB  . ALA   A 1 159 ? 11.32415  -22.53100 -18.81727 1.000 26.72206 ? 166 ALA   A CB  1 
ATOM   1414 N  N   . GLY   A 1 160 ? 13.59962  -23.76539 -20.07078 1.000 23.51291 ? 167 GLY   A N   1 
ATOM   1415 C  CA  . GLY   A 1 160 ? 14.71278  -24.52731 -20.60299 1.000 23.09526 ? 167 GLY   A CA  1 
ATOM   1416 C  C   . GLY   A 1 160 ? 15.40112  -23.90966 -21.79924 1.000 28.63650 ? 167 GLY   A C   1 
ATOM   1417 O  O   . GLY   A 1 160 ? 16.19595  -24.59048 -22.46036 1.000 26.33047 ? 167 GLY   A O   1 
ATOM   1418 N  N   . GLY   A 1 161 ? 15.11277  -22.64764 -22.11131 1.000 18.98851 ? 168 GLY   A N   1 
ATOM   1419 C  CA  . GLY   A 1 161 ? 15.88154  -21.90176 -23.08653 1.000 20.28370 ? 168 GLY   A CA  1 
ATOM   1420 C  C   . GLY   A 1 161 ? 15.30149  -21.82826 -24.48459 1.000 22.46160 ? 168 GLY   A C   1 
ATOM   1421 O  O   . GLY   A 1 161 ? 15.89179  -21.16135 -25.33954 1.000 20.20296 ? 168 GLY   A O   1 
ATOM   1422 N  N   . SER   A 1 162 ? 14.17117  -22.47665 -24.75224 1.000 18.82841 ? 169 SER   A N   1 
ATOM   1423 C  CA  . SER   A 1 162 ? 13.62876  -22.48700 -26.10136 1.000 18.18526 ? 169 SER   A CA  1 
ATOM   1424 C  C   . SER   A 1 162 ? 12.11244  -22.38897 -26.05899 1.000 17.19629 ? 169 SER   A C   1 
ATOM   1425 O  O   . SER   A 1 162 ? 11.47381  -22.70095 -25.04978 1.000 19.59660 ? 169 SER   A O   1 
ATOM   1426 C  CB  . SER   A 1 162 ? 14.04844  -23.74620 -26.87173 1.000 24.23682 ? 169 SER   A CB  1 
ATOM   1427 O  OG  . SER   A 1 162 ? 13.39214  -24.88792 -26.35771 1.000 21.36868 ? 169 SER   A OG  1 
ATOM   1428 N  N   . PHE   A 1 163 ? 11.54777  -21.93603 -27.17865 1.000 17.12650 ? 170 PHE   A N   1 
ATOM   1429 C  CA  . PHE   A 1 163 ? 10.10764  -21.95928 -27.39352 1.000 18.21251 ? 170 PHE   A CA  1 
ATOM   1430 C  C   . PHE   A 1 163 ? 9.84470   -22.41537 -28.81948 1.000 18.33333 ? 170 PHE   A C   1 
ATOM   1431 O  O   . PHE   A 1 163 ? 10.73526  -22.40276 -29.67192 1.000 18.60422 ? 170 PHE   A O   1 
ATOM   1432 C  CB  . PHE   A 1 163 ? 9.45102   -20.58866 -27.12656 1.000 16.08649 ? 170 PHE   A CB  1 
ATOM   1433 C  CG  . PHE   A 1 163 ? 9.94742   -19.47228 -28.02410 1.000 15.77231 ? 170 PHE   A CG  1 
ATOM   1434 C  CD1 . PHE   A 1 163 ? 11.06439  -18.72905 -27.67535 1.000 18.63901 ? 170 PHE   A CD1 1 
ATOM   1435 C  CD2 . PHE   A 1 163 ? 9.26903   -19.14247 -29.18800 1.000 18.01885 ? 170 PHE   A CD2 1 
ATOM   1436 C  CE1 . PHE   A 1 163 ? 11.51517  -17.69333 -28.48430 1.000 19.52570 ? 170 PHE   A CE1 1 
ATOM   1437 C  CE2 . PHE   A 1 163 ? 9.71262   -18.11687 -30.00162 1.000 16.41778 ? 170 PHE   A CE2 1 
ATOM   1438 C  CZ  . PHE   A 1 163 ? 10.83535  -17.38219 -29.64516 1.000 20.61664 ? 170 PHE   A CZ  1 
ATOM   1439 N  N   . THR   A 1 164 ? 8.61259   -22.84642 -29.07155 1.000 18.14726 ? 171 THR   A N   1 
ATOM   1440 C  CA  . THR   A 1 164 ? 8.20084   -23.23779 -30.40798 1.000 18.32692 ? 171 THR   A CA  1 
ATOM   1441 C  C   . THR   A 1 164 ? 7.05615   -22.35736 -30.88260 1.000 17.76521 ? 171 THR   A C   1 
ATOM   1442 O  O   . THR   A 1 164 ? 6.30331   -21.79864 -30.07816 1.000 16.70858 ? 171 THR   A O   1 
ATOM   1443 C  CB  . THR   A 1 164 ? 7.78080   -24.72028 -30.47621 1.000 21.06158 ? 171 THR   A CB  1 
ATOM   1444 O  OG1 . THR   A 1 164 ? 6.59479   -24.91313 -29.69692 1.000 22.44401 ? 171 THR   A OG1 1 
ATOM   1445 C  CG2 . THR   A 1 164 ? 8.89811   -25.64501 -29.98122 1.000 20.14009 ? 171 THR   A CG2 1 
ATOM   1446 N  N   . VAL   A 1 165 ? 6.95341   -22.22060 -32.20097 1.000 18.77581 ? 172 VAL   A N   1 
ATOM   1447 C  CA  . VAL   A 1 165 ? 5.83789   -21.53498 -32.84250 1.000 19.33591 ? 172 VAL   A CA  1 
ATOM   1448 C  C   . VAL   A 1 165 ? 5.35776   -22.40526 -33.98961 1.000 22.98939 ? 172 VAL   A C   1 
ATOM   1449 O  O   . VAL   A 1 165 ? 6.16521   -22.88691 -34.79101 1.000 21.75130 ? 172 VAL   A O   1 
ATOM   1450 C  CB  . VAL   A 1 165 ? 6.21936   -20.13311 -33.35733 1.000 22.64690 ? 172 VAL   A CB  1 
ATOM   1451 C  CG1 . VAL   A 1 165 ? 5.03924   -19.50029 -34.07982 1.000 22.08582 ? 172 VAL   A CG1 1 
ATOM   1452 C  CG2 . VAL   A 1 165 ? 6.65520   -19.24437 -32.21353 1.000 18.49355 ? 172 VAL   A CG2 1 
ATOM   1453 N  N   . ARG   A 1 166 ? 4.04576   -22.60500 -34.07369 1.000 20.15773 ? 173 ARG   A N   1 
ATOM   1454 C  CA  . ARG   A 1 166 ? 3.49830   -23.36197 -35.18368 1.000 23.12008 ? 173 ARG   A CA  1 
ATOM   1455 C  C   . ARG   A 1 166 ? 2.16007   -22.75937 -35.56533 1.000 22.41392 ? 173 ARG   A C   1 
ATOM   1456 O  O   . ARG   A 1 166 ? 1.50761   -22.08661 -34.76326 1.000 20.50274 ? 173 ARG   A O   1 
ATOM   1457 C  CB  . ARG   A 1 166 ? 3.31243   -24.84481 -34.84354 1.000 24.34388 ? 173 ARG   A CB  1 
ATOM   1458 C  CG  . ARG   A 1 166 ? 2.19783   -25.12392 -33.84416 1.000 29.09541 ? 173 ARG   A CG  1 
ATOM   1459 C  CD  . ARG   A 1 166 ? 2.41397   -26.43264 -33.08432 1.000 39.76602 ? 173 ARG   A CD  1 
ATOM   1460 N  NE  . ARG   A 1 166 ? 3.63626   -26.43632 -32.28811 1.000 44.05391 ? 173 ARG   A NE  1 
ATOM   1461 C  CZ  . ARG   A 1 166 ? 4.11448   -27.50272 -31.66028 1.000 55.37759 ? 173 ARG   A CZ  1 
ATOM   1462 N  NH1 . ARG   A 1 166 ? 3.54069   -28.68869 -31.77844 1.000 41.37574 ? 173 ARG   A NH1 1 
ATOM   1463 N  NH2 . ARG   A 1 166 ? 5.19831   -27.37778 -30.89909 1.000 58.59264 ? 173 ARG   A NH2 1 
ATOM   1464 N  N   . THR   A 1 167 ? 1.76719   -23.00094 -36.80771 1.000 23.55318 ? 174 THR   A N   1 
ATOM   1465 C  CA  . THR   A 1 167 ? 0.40795   -22.69273 -37.21734 1.000 30.21443 ? 174 THR   A CA  1 
ATOM   1466 C  C   . THR   A 1 167 ? -0.55331  -23.54774 -36.40686 1.000 30.39655 ? 174 THR   A C   1 
ATOM   1467 O  O   . THR   A 1 167 ? -0.34176  -24.75172 -36.24180 1.000 31.11043 ? 174 THR   A O   1 
ATOM   1468 C  CB  . THR   A 1 167 ? 0.23372   -22.95623 -38.71244 1.000 34.31256 ? 174 THR   A CB  1 
ATOM   1469 O  OG1 . THR   A 1 167 ? 1.05157   -22.03906 -39.44919 1.000 37.85712 ? 174 THR   A OG1 1 
ATOM   1470 C  CG2 . THR   A 1 167 ? -1.21799  -22.77191 -39.12090 1.000 45.39522 ? 174 THR   A CG2 1 
ATOM   1471 N  N   . ASP   A 1 168 ? -1.60016  -22.92498 -35.87958 1.000 23.78922 ? 175 ASP   A N   1 
ATOM   1472 C  CA  . ASP   A 1 168 ? -2.54707  -23.62954 -35.02869 1.000 29.40330 ? 175 ASP   A CA  1 
ATOM   1473 C  C   . ASP   A 1 168 ? -3.69823  -24.16036 -35.87444 1.000 38.88442 ? 175 ASP   A C   1 
ATOM   1474 O  O   . ASP   A 1 168 ? -4.40931  -23.38558 -36.52121 1.000 38.21702 ? 175 ASP   A O   1 
ATOM   1475 C  CB  . ASP   A 1 168 ? -3.06786  -22.71214 -33.92786 1.000 29.53716 ? 175 ASP   A CB  1 
ATOM   1476 C  CG  . ASP   A 1 168 ? -3.93894  -23.44358 -32.93525 1.000 36.78365 ? 175 ASP   A CG  1 
ATOM   1477 O  OD1 . ASP   A 1 168 ? -3.55292  -24.54969 -32.50049 1.000 52.83704 ? 175 ASP   A OD1 1 
ATOM   1478 O  OD2 . ASP   A 1 168 ? -5.01788  -22.91974 -32.60482 1.000 32.47280 ? 175 ASP   A OD2 1 
ATOM   1479 N  N   . THR   A 1 169 ? -3.87815  -25.47649 -35.86833 1.000 47.87960 ? 176 THR   A N   1 
ATOM   1480 C  CA  . THR   A 1 169 ? -4.99096  -26.11201 -36.55803 1.000 73.03832 ? 176 THR   A CA  1 
ATOM   1481 C  C   . THR   A 1 169 ? -6.17649  -26.36903 -35.63922 1.000 63.16888 ? 176 THR   A C   1 
ATOM   1482 O  O   . THR   A 1 169 ? -7.16102  -26.97642 -36.07307 1.000 54.39356 ? 176 THR   A O   1 
ATOM   1483 C  CB  . THR   A 1 169 ? -4.53573  -27.42920 -37.19431 1.000 67.65522 ? 176 THR   A CB  1 
ATOM   1484 O  OG1 . THR   A 1 169 ? -3.70857  -28.14674 -36.26685 1.000 65.79696 ? 176 THR   A OG1 1 
ATOM   1485 C  CG2 . THR   A 1 169 ? -3.74591  -27.15350 -38.46704 1.000 46.54326 ? 176 THR   A CG2 1 
ATOM   1486 N  N   . GLY   A 1 170 ? -6.10738  -25.91716 -34.38858 1.000 58.56035 ? 177 GLY   A N   1 
ATOM   1487 C  CA  . GLY   A 1 170 ? -7.17112  -26.14397 -33.43222 1.000 68.47551 ? 177 GLY   A CA  1 
ATOM   1488 C  C   . GLY   A 1 170 ? -8.41063  -25.30885 -33.67887 1.000 48.89634 ? 177 GLY   A C   1 
ATOM   1489 O  O   . GLY   A 1 170 ? -8.62013  -24.79126 -34.78115 1.000 44.07373 ? 177 GLY   A O   1 
ATOM   1490 N  N   . GLU   A 1 171 ? -9.23999  -25.17864 -32.65364 1.000 53.23240 ? 178 GLU   A N   1 
ATOM   1491 C  CA  . GLU   A 1 171 ? -10.48480 -24.43099 -32.75514 1.000 43.74642 ? 178 GLU   A CA  1 
ATOM   1492 C  C   . GLU   A 1 171 ? -10.19925 -22.98520 -33.14747 1.000 36.63176 ? 178 GLU   A C   1 
ATOM   1493 O  O   . GLU   A 1 171 ? -9.40319  -22.31866 -32.47086 1.000 28.94916 ? 178 GLU   A O   1 
ATOM   1494 C  CB  . GLU   A 1 171 ? -11.22357 -24.48598 -31.41976 1.000 46.92871 ? 178 GLU   A CB  1 
ATOM   1495 C  CG  . GLU   A 1 171 ? -12.73496 -24.51771 -31.52645 1.000 61.35740 ? 178 GLU   A CG  1 
ATOM   1496 C  CD  . GLU   A 1 171 ? -13.24138 -25.61247 -32.44604 1.000 49.62333 ? 178 GLU   A CD  1 
ATOM   1497 O  OE1 . GLU   A 1 171 ? -13.68633 -25.28523 -33.56424 1.000 49.59538 ? 178 GLU   A OE1 1 
ATOM   1498 O  OE2 . GLU   A 1 171 ? -13.17855 -26.79795 -32.05913 1.000 50.62583 ? 178 GLU   A OE2 1 
ATOM   1499 N  N   . PRO   A 1 172 ? -10.78917 -22.47602 -34.22962 1.000 35.50513 ? 179 PRO   A N   1 
ATOM   1500 C  CA  . PRO   A 1 172 ? -10.55493 -21.07718 -34.61062 1.000 32.77980 ? 179 PRO   A CA  1 
ATOM   1501 C  C   . PRO   A 1 172 ? -11.03088 -20.11840 -33.52809 1.000 40.13340 ? 179 PRO   A C   1 
ATOM   1502 O  O   . PRO   A 1 172 ? -12.06727 -20.33065 -32.89503 1.000 42.99473 ? 179 PRO   A O   1 
ATOM   1503 C  CB  . PRO   A 1 172 ? -11.37258 -20.91930 -35.89525 1.000 38.82638 ? 179 PRO   A CB  1 
ATOM   1504 C  CG  . PRO   A 1 172 ? -11.44256 -22.29238 -36.46665 1.000 55.43488 ? 179 PRO   A CG  1 
ATOM   1505 C  CD  . PRO   A 1 172 ? -11.45740 -23.24163 -35.29564 1.000 41.96888 ? 179 PRO   A CD  1 
ATOM   1506 N  N   . MET   A 1 173 ? -10.26832 -19.04157 -33.33427 1.000 26.56018 ? 180 MET   A N   1 
ATOM   1507 C  CA  . MET   A 1 173 ? -10.51548 -18.10525 -32.24364 1.000 26.93053 ? 180 MET   A CA  1 
ATOM   1508 C  C   . MET   A 1 173 ? -11.25000 -16.84158 -32.66327 1.000 36.62730 ? 180 MET   A C   1 
ATOM   1509 O  O   . MET   A 1 173 ? -11.87425 -16.19620 -31.81662 1.000 42.46453 ? 180 MET   A O   1 
ATOM   1510 C  CB  . MET   A 1 173 ? -9.19464  -17.69135 -31.59622 1.000 29.60929 ? 180 MET   A CB  1 
ATOM   1511 C  CG  . MET   A 1 173 ? -8.53768  -18.76643 -30.77801 1.000 57.14227 ? 180 MET   A CG  1 
ATOM   1512 S  SD  . MET   A 1 173 ? -7.12443  -18.06635 -29.92008 1.000 54.57707 ? 180 MET   A SD  1 
ATOM   1513 C  CE  . MET   A 1 173 ? -7.74257  -16.46018 -29.45940 1.000 38.72641 ? 180 MET   A CE  1 
ATOM   1514 N  N   . GLY   A 1 174 ? -11.16959 -16.44856 -33.92638 1.000 30.85243 ? 181 GLY   A N   1 
ATOM   1515 C  CA  . GLY   A 1 174 ? -11.77665 -15.19817 -34.33965 1.000 32.43629 ? 181 GLY   A CA  1 
ATOM   1516 C  C   . GLY   A 1 174 ? -10.82171 -14.03803 -34.15525 1.000 24.69497 ? 181 GLY   A C   1 
ATOM   1517 O  O   . GLY   A 1 174 ? -10.33561 -13.46694 -35.13777 1.000 24.40611 ? 181 GLY   A O   1 
ATOM   1518 N  N   . ARG   A 1 175 ? -10.54200 -13.68687 -32.89924 1.000 20.04124 ? 182 ARG   A N   1 
ATOM   1519 C  CA  . ARG   A 1 175 ? -9.54471  -12.67706 -32.56097 1.000 20.55078 ? 182 ARG   A CA  1 
ATOM   1520 C  C   . ARG   A 1 175 ? -9.25734  -12.73679 -31.07049 1.000 23.13520 ? 182 ARG   A C   1 
ATOM   1521 O  O   . ARG   A 1 175 ? -10.18547 -12.82720 -30.26468 1.000 20.61181 ? 182 ARG   A O   1 
ATOM   1522 C  CB  . ARG   A 1 175 ? -10.01518 -11.26158 -32.92280 1.000 19.31309 ? 182 ARG   A CB  1 
ATOM   1523 C  CG  . ARG   A 1 175 ? -8.91488  -10.20625 -32.75948 1.000 18.52890 ? 182 ARG   A CG  1 
ATOM   1524 C  CD  . ARG   A 1 175 ? -9.50792  -8.80378  -32.67579 1.000 19.04380 ? 182 ARG   A CD  1 
ATOM   1525 N  NE  . ARG   A 1 175 ? -10.38688 -8.65834  -31.51824 1.000 18.99987 ? 182 ARG   A NE  1 
ATOM   1526 C  CZ  . ARG   A 1 175 ? -11.70699 -8.53722  -31.59068 1.000 20.02014 ? 182 ARG   A CZ  1 
ATOM   1527 N  NH1 . ARG   A 1 175 ? -12.33980 -8.54013  -32.75509 1.000 21.51612 ? 182 ARG   A NH1 1 
ATOM   1528 N  NH2 . ARG   A 1 175 ? -12.41371 -8.41236  -30.46613 1.000 20.17592 ? 182 ARG   A NH2 1 
ATOM   1529 N  N   . GLY   A 1 176 ? -7.98393  -12.66103 -30.71167 1.000 23.82987 ? 183 GLY   A N   1 
ATOM   1530 C  CA  . GLY   A 1 176 ? -7.61259  -12.53131 -29.32210 1.000 21.41413 ? 183 GLY   A CA  1 
ATOM   1531 C  C   . GLY   A 1 176 ? -6.45781  -13.43956 -28.97265 1.000 20.86414 ? 183 GLY   A C   1 
ATOM   1532 O  O   . GLY   A 1 176 ? -5.69216  -13.86603 -29.83741 1.000 21.77464 ? 183 GLY   A O   1 
ATOM   1533 N  N   . THR   A 1 177 ? -6.35381  -13.72546 -27.67843 1.000 18.25144 ? 184 THR   A N   1 
ATOM   1534 C  CA  . THR   A 1 177 ? -5.25763  -14.51594 -27.13642 1.000 17.18545 ? 184 THR   A CA  1 
ATOM   1535 C  C   . THR   A 1 177 ? -5.78333  -15.45155 -26.06338 1.000 26.41223 ? 184 THR   A C   1 
ATOM   1536 O  O   . THR   A 1 177 ? -6.63925  -15.07618 -25.25487 1.000 19.31891 ? 184 THR   A O   1 
ATOM   1537 C  CB  . THR   A 1 177 ? -4.14946  -13.61080 -26.57121 1.000 20.97444 ? 184 THR   A CB  1 
ATOM   1538 O  OG1 . THR   A 1 177 ? -3.59328  -12.83287 -27.63494 1.000 21.79754 ? 184 THR   A OG1 1 
ATOM   1539 C  CG2 . THR   A 1 177 ? -3.03635  -14.41955 -25.89600 1.000 19.61605 ? 184 THR   A CG2 1 
ATOM   1540 N  N   . LYS   A 1 178 ? -5.26063  -16.67359 -26.07401 1.000 15.95917 ? 185 LYS   A N   1 
ATOM   1541 C  CA  . LYS   A 1 178 ? -5.57708  -17.70452 -25.09846 1.000 16.99784 ? 185 LYS   A CA  1 
ATOM   1542 C  C   . LYS   A 1 178 ? -4.26908  -18.16333 -24.46854 1.000 19.58596 ? 185 LYS   A C   1 
ATOM   1543 O  O   . LYS   A 1 178 ? -3.39873  -18.67578 -25.17430 1.000 20.36450 ? 185 LYS   A O   1 
ATOM   1544 C  CB  . LYS   A 1 178 ? -6.29272  -18.86250 -25.80290 1.000 21.15224 ? 185 LYS   A CB  1 
ATOM   1545 C  CG  . LYS   A 1 178 ? -6.63256  -20.04470 -24.94122 1.000 33.21009 ? 185 LYS   A CG  1 
ATOM   1546 C  CD  . LYS   A 1 178 ? -7.11821  -21.26458 -25.74652 1.000 44.82038 ? 185 LYS   A CD  1 
ATOM   1547 C  CE  . LYS   A 1 178 ? -7.67425  -20.92078 -27.12959 1.000 49.14714 ? 185 LYS   A CE  1 
ATOM   1548 N  NZ  . LYS   A 1 178 ? -8.87843  -20.04076 -27.07917 1.000 63.18929 ? 185 LYS   A NZ  1 
ATOM   1549 N  N   . VAL   A 1 179 ? -4.11494  -17.95310 -23.16258 1.000 17.30553 ? 186 VAL   A N   1 
ATOM   1550 C  CA  . VAL   A 1 179 ? -2.94097  -18.42186 -22.42407 1.000 14.38211 ? 186 VAL   A CA  1 
ATOM   1551 C  C   . VAL   A 1 179 ? -3.34398  -19.67431 -21.66003 1.000 18.41253 ? 186 VAL   A C   1 
ATOM   1552 O  O   . VAL   A 1 179 ? -4.18479  -19.61701 -20.75389 1.000 17.56271 ? 186 VAL   A O   1 
ATOM   1553 C  CB  . VAL   A 1 179 ? -2.39151  -17.35141 -21.47068 1.000 15.69357 ? 186 VAL   A CB  1 
ATOM   1554 C  CG1 . VAL   A 1 179 ? -1.18452  -17.90316 -20.69617 1.000 16.34449 ? 186 VAL   A CG1 1 
ATOM   1555 C  CG2 . VAL   A 1 179 ? -1.97093  -16.12201 -22.24945 1.000 17.32297 ? 186 VAL   A CG2 1 
ATOM   1556 N  N   . ILE   A 1 180 ? -2.75118  -20.80693 -22.02477 1.000 16.96782 ? 187 ILE   A N   1 
ATOM   1557 C  CA  . ILE   A 1 180 ? -3.03432  -22.08973 -21.39106 1.000 16.42955 ? 187 ILE   A CA  1 
ATOM   1558 C  C   . ILE   A 1 180 ? -1.90792  -22.39868 -20.41947 1.000 16.91190 ? 187 ILE   A C   1 
ATOM   1559 O  O   . ILE   A 1 180 ? -0.75825  -22.57526 -20.83322 1.000 16.67876 ? 187 ILE   A O   1 
ATOM   1560 C  CB  . ILE   A 1 180 ? -3.18335  -23.20785 -22.43046 1.000 16.13061 ? 187 ILE   A CB  1 
ATOM   1561 C  CG1 . ILE   A 1 180 ? -4.21799  -22.80169 -23.48759 1.000 16.67973 ? 187 ILE   A CG1 1 
ATOM   1562 C  CG2 . ILE   A 1 180 ? -3.55922  -24.52913 -21.75009 1.000 18.41371 ? 187 ILE   A CG2 1 
ATOM   1563 C  CD1 . ILE   A 1 180 ? -4.22377  -23.68795 -24.70567 1.000 27.03171 ? 187 ILE   A CD1 1 
ATOM   1564 N  N   . LEU   A 1 181 ? -2.23397  -22.46161 -19.13092 1.000 16.11494 ? 188 LEU   A N   1 
ATOM   1565 C  CA  . LEU   A 1 181 ? -1.25077  -22.71963 -18.08418 1.000 17.12963 ? 188 LEU   A CA  1 
ATOM   1566 C  C   . LEU   A 1 181 ? -1.32919  -24.19337 -17.71015 1.000 17.96902 ? 188 LEU   A C   1 
ATOM   1567 O  O   . LEU   A 1 181 ? -2.30699  -24.62422 -17.09305 1.000 19.16236 ? 188 LEU   A O   1 
ATOM   1568 C  CB  . LEU   A 1 181 ? -1.52112  -21.84737 -16.86234 1.000 14.30206 ? 188 LEU   A CB  1 
ATOM   1569 C  CG  . LEU   A 1 181 ? -1.57164  -20.33995 -17.09797 1.000 20.64372 ? 188 LEU   A CG  1 
ATOM   1570 C  CD1 . LEU   A 1 181 ? -1.89420  -19.62925 -15.79305 1.000 22.72236 ? 188 LEU   A CD1 1 
ATOM   1571 C  CD2 . LEU   A 1 181 ? -0.25658  -19.86307 -17.66574 1.000 20.32797 ? 188 LEU   A CD2 1 
ATOM   1572 N  N   . HIS   A 1 182 ? -0.29844  -24.96111 -18.06229 1.000 16.84734 ? 189 HIS   A N   1 
ATOM   1573 C  CA  . HIS   A 1 182 ? -0.20309  -26.35545 -17.62403 1.000 18.18451 ? 189 HIS   A CA  1 
ATOM   1574 C  C   . HIS   A 1 182 ? 0.42658   -26.34412 -16.23737 1.000 19.01858 ? 189 HIS   A C   1 
ATOM   1575 O  O   . HIS   A 1 182 ? 1.64024   -26.19604 -16.09295 1.000 19.73671 ? 189 HIS   A O   1 
ATOM   1576 C  CB  . HIS   A 1 182 ? 0.60236   -27.18109 -18.62220 1.000 20.01232 ? 189 HIS   A CB  1 
ATOM   1577 C  CG  . HIS   A 1 182 ? 0.11145   -27.05148 -20.03284 1.000 25.74519 ? 189 HIS   A CG  1 
ATOM   1578 N  ND1 . HIS   A 1 182 ? -0.67905  -28.00385 -20.64135 1.000 29.44168 ? 189 HIS   A ND1 1 
ATOM   1579 C  CD2 . HIS   A 1 182 ? 0.27977   -26.06432 -20.94524 1.000 22.77294 ? 189 HIS   A CD2 1 
ATOM   1580 C  CE1 . HIS   A 1 182 ? -0.96524  -27.61448 -21.87276 1.000 24.55512 ? 189 HIS   A CE1 1 
ATOM   1581 N  NE2 . HIS   A 1 182 ? -0.39158  -26.44248 -22.08315 1.000 28.27772 ? 189 HIS   A NE2 1 
ATOM   1582 N  N   . LEU   A 1 183 ? -0.40686  -26.48072 -15.21021 1.000 18.73225 ? 190 LEU   A N   1 
ATOM   1583 C  CA  . LEU   A 1 183 ? 0.00381   -26.15148 -13.85217 1.000 20.65235 ? 190 LEU   A CA  1 
ATOM   1584 C  C   . LEU   A 1 183 ? 0.95284   -27.19858 -13.28188 1.000 24.00244 ? 190 LEU   A C   1 
ATOM   1585 O  O   . LEU   A 1 183 ? 0.85040   -28.39357 -13.57687 1.000 22.26759 ? 190 LEU   A O   1 
ATOM   1586 C  CB  . LEU   A 1 183 ? -1.22008  -26.03274 -12.94073 1.000 19.60130 ? 190 LEU   A CB  1 
ATOM   1587 C  CG  . LEU   A 1 183 ? -2.13422  -24.83198 -13.19990 1.000 20.48666 ? 190 LEU   A CG  1 
ATOM   1588 C  CD1 . LEU   A 1 183 ? -3.26922  -24.78591 -12.17488 1.000 22.47686 ? 190 LEU   A CD1 1 
ATOM   1589 C  CD2 . LEU   A 1 183 ? -1.35216  -23.53484 -13.20182 1.000 22.08729 ? 190 LEU   A CD2 1 
ATOM   1590 N  N   . LYS   A 1 184 ? 1.87871   -26.73156 -12.44285 1.000 20.32215 ? 191 LYS   A N   1 
ATOM   1591 C  CA  . LYS   A 1 184 ? 2.71624   -27.62589 -11.65891 1.000 23.05161 ? 191 LYS   A CA  1 
ATOM   1592 C  C   . LYS   A 1 184 ? 1.85833   -28.46723 -10.71938 1.000 26.12254 ? 191 LYS   A C   1 
ATOM   1593 O  O   . LYS   A 1 184 ? 0.76723   -28.06895 -10.30983 1.000 26.38660 ? 191 LYS   A O   1 
ATOM   1594 C  CB  . LYS   A 1 184 ? 3.73748   -26.83737 -10.83611 1.000 26.74227 ? 191 LYS   A CB  1 
ATOM   1595 C  CG  . LYS   A 1 184 ? 4.80997   -26.12416 -11.64771 1.000 30.20100 ? 191 LYS   A CG  1 
ATOM   1596 C  CD  . LYS   A 1 184 ? 5.50307   -25.06102 -10.78998 1.000 37.21649 ? 191 LYS   A CD  1 
ATOM   1597 C  CE  . LYS   A 1 184 ? 6.48927   -24.23112 -11.60071 1.000 52.74019 ? 191 LYS   A CE  1 
ATOM   1598 N  NZ  . LYS   A 1 184 ? 7.21961   -23.21506 -10.76928 1.000 52.68705 ? 191 LYS   A NZ  1 
ATOM   1599 N  N   . GLU   A 1 185 ? 2.39040   -29.63672 -10.35690 1.000 27.66867 ? 192 GLU   A N   1 
ATOM   1600 C  CA  . GLU   A 1 185 ? 1.63104   -30.60470 -9.57301  1.000 34.51101 ? 192 GLU   A CA  1 
ATOM   1601 C  C   . GLU   A 1 185 ? 1.16615   -30.03634 -8.23754  1.000 34.70940 ? 192 GLU   A C   1 
ATOM   1602 O  O   . GLU   A 1 185 ? 0.07740   -30.38455 -7.76912  1.000 37.50397 ? 192 GLU   A O   1 
ATOM   1603 C  CB  . GLU   A 1 185 ? 2.47997   -31.85719 -9.34695  1.000 40.14220 ? 192 GLU   A CB  1 
ATOM   1604 C  CG  . GLU   A 1 185 ? 1.70929   -33.08045 -8.89671  1.000 50.68843 ? 192 GLU   A CG  1 
ATOM   1605 C  CD  . GLU   A 1 185 ? 2.60483   -34.29308 -8.72309  1.000 80.60359 ? 192 GLU   A CD  1 
ATOM   1606 O  OE1 . GLU   A 1 185 ? 3.81370   -34.10535 -8.47126  1.000 73.23686 ? 192 GLU   A OE1 1 
ATOM   1607 O  OE2 . GLU   A 1 185 ? 2.10330   -35.43157 -8.84000  1.000 89.65770 ? 192 GLU   A OE2 1 
ATOM   1608 N  N   A ASP   A 1 186 ? 1.96296   -29.16934 -7.61228  0.500 29.58939 ? 193 ASP   A N   1 
ATOM   1609 N  N   B ASP   A 1 186 ? 1.96296   -29.16934 -7.61228  0.500 29.58939 ? 193 ASP   A N   1 
ATOM   1610 C  CA  A ASP   A 1 186 ? 1.63700   -28.62526 -6.30093  0.500 32.62245 ? 193 ASP   A CA  1 
ATOM   1611 C  CA  B ASP   A 1 186 ? 1.63700   -28.62526 -6.30093  0.500 32.62245 ? 193 ASP   A CA  1 
ATOM   1612 C  C   A ASP   A 1 186 ? 0.94819   -27.26752 -6.37837  0.500 28.29433 ? 193 ASP   A C   1 
ATOM   1613 C  C   B ASP   A 1 186 ? 0.94819   -27.26752 -6.37837  0.500 28.29433 ? 193 ASP   A C   1 
ATOM   1614 O  O   A ASP   A 1 186 ? 0.84814   -26.57739 -5.35928  0.500 29.38798 ? 193 ASP   A O   1 
ATOM   1615 O  O   B ASP   A 1 186 ? 0.84814   -26.57739 -5.35928  0.500 29.38798 ? 193 ASP   A O   1 
ATOM   1616 C  CB  A ASP   A 1 186 ? 2.90007   -28.52919 -5.43789  0.500 35.42337 ? 193 ASP   A CB  1 
ATOM   1617 C  CB  B ASP   A 1 186 ? 2.90007   -28.52919 -5.43789  0.500 35.42337 ? 193 ASP   A CB  1 
ATOM   1618 C  CG  A ASP   A 1 186 ? 3.98105   -27.66403 -6.06424  0.500 39.10435 ? 193 ASP   A CG  1 
ATOM   1619 C  CG  B ASP   A 1 186 ? 3.98105   -27.66403 -6.06424  0.500 39.10435 ? 193 ASP   A CG  1 
ATOM   1620 O  OD1 A ASP   A 1 186 ? 3.79897   -27.19632 -7.20610  0.500 48.38268 ? 193 ASP   A OD1 1 
ATOM   1621 O  OD1 B ASP   A 1 186 ? 3.79897   -27.19632 -7.20610  0.500 48.38268 ? 193 ASP   A OD1 1 
ATOM   1622 O  OD2 A ASP   A 1 186 ? 5.02502   -27.45633 -5.40903  0.500 51.76697 ? 193 ASP   A OD2 1 
ATOM   1623 O  OD2 B ASP   A 1 186 ? 5.02502   -27.45633 -5.40903  0.500 51.76697 ? 193 ASP   A OD2 1 
ATOM   1624 N  N   . GLN   A 1 187 ? 0.46073   -26.87455 -7.55542  1.000 22.51582 ? 194 GLN   A N   1 
ATOM   1625 C  CA  . GLN   A 1 187 ? -0.17115  -25.57590 -7.75056  1.000 21.57768 ? 194 GLN   A CA  1 
ATOM   1626 C  C   . GLN   A 1 187 ? -1.62147  -25.71564 -8.20630  1.000 22.21831 ? 194 GLN   A C   1 
ATOM   1627 O  O   . GLN   A 1 187 ? -2.16829  -24.80830 -8.83683  1.000 23.98265 ? 194 GLN   A O   1 
ATOM   1628 C  CB  . GLN   A 1 187 ? 0.62642   -24.73914 -8.75385  1.000 19.18758 ? 194 GLN   A CB  1 
ATOM   1629 C  CG  . GLN   A 1 187 ? 2.06557   -24.45794 -8.32262  1.000 21.71977 ? 194 GLN   A CG  1 
ATOM   1630 C  CD  . GLN   A 1 187 ? 2.15809   -23.76327 -6.97437  1.000 25.01875 ? 194 GLN   A CD  1 
ATOM   1631 O  OE1 . GLN   A 1 187 ? 1.35839   -22.88021 -6.66047  1.000 26.39418 ? 194 GLN   A OE1 1 
ATOM   1632 N  NE2 . GLN   A 1 187 ? 3.14121   -24.15442 -6.17373  1.000 27.59886 ? 194 GLN   A NE2 1 
ATOM   1633 N  N   . THR   A 1 188 ? -2.26593  -26.83601 -7.88491  1.000 25.76092 ? 195 THR   A N   1 
ATOM   1634 C  CA  . THR   A 1 188 ? -3.63107  -27.05356 -8.35657  1.000 31.99524 ? 195 THR   A CA  1 
ATOM   1635 C  C   . THR   A 1 188 ? -4.67230  -26.24376 -7.58854  1.000 25.40823 ? 195 THR   A C   1 
ATOM   1636 O  O   . THR   A 1 188 ? -5.85502  -26.28379 -7.95426  1.000 27.18697 ? 195 THR   A O   1 
ATOM   1637 C  CB  . THR   A 1 188 ? -3.98299  -28.54558 -8.30551  1.000 29.35854 ? 195 THR   A CB  1 
ATOM   1638 O  OG1 . THR   A 1 188 ? -3.87555  -29.02791 -6.96019  1.000 32.11337 ? 195 THR   A OG1 1 
ATOM   1639 C  CG2 . THR   A 1 188 ? -3.05271  -29.34381 -9.21296  1.000 28.49790 ? 195 THR   A CG2 1 
ATOM   1640 N  N   . GLU   A 1 189 ? -4.27396  -25.50120 -6.55131  1.000 23.94370 ? 196 GLU   A N   1 
ATOM   1641 C  CA  . GLU   A 1 189 ? -5.22280  -24.61076 -5.88513  1.000 22.09726 ? 196 GLU   A CA  1 
ATOM   1642 C  C   . GLU   A 1 189 ? -5.78326  -23.56757 -6.84189  1.000 20.76331 ? 196 GLU   A C   1 
ATOM   1643 O  O   . GLU   A 1 189 ? -6.90080  -23.08011 -6.64370  1.000 21.19656 ? 196 GLU   A O   1 
ATOM   1644 C  CB  . GLU   A 1 189 ? -4.56242  -23.92697 -4.68923  1.000 20.38570 ? 196 GLU   A CB  1 
ATOM   1645 C  CG  . GLU   A 1 189 ? -3.56762  -22.84329 -5.05460  1.000 20.71784 ? 196 GLU   A CG  1 
ATOM   1646 C  CD  . GLU   A 1 189 ? -2.80424  -22.34134 -3.84744  1.000 35.37074 ? 196 GLU   A CD  1 
ATOM   1647 O  OE1 . GLU   A 1 189 ? -1.89840  -23.06338 -3.38587  1.000 32.69131 ? 196 GLU   A OE1 1 
ATOM   1648 O  OE2 . GLU   A 1 189 ? -3.11047  -21.23275 -3.35892  1.000 29.32301 ? 196 GLU   A OE2 1 
ATOM   1649 N  N   . TYR   A 1 190 ? -5.03808  -23.21966 -7.88348  1.000 22.88049 ? 197 TYR   A N   1 
ATOM   1650 C  CA  . TYR   A 1 190 ? -5.48693  -22.20893 -8.83346  1.000 22.38128 ? 197 TYR   A CA  1 
ATOM   1651 C  C   . TYR   A 1 190 ? -6.48484  -22.75986 -9.84054  1.000 21.63616 ? 197 TYR   A C   1 
ATOM   1652 O  O   . TYR   A 1 190 ? -6.86993  -22.04419 -10.77345 1.000 23.55008 ? 197 TYR   A O   1 
ATOM   1653 C  CB  . TYR   A 1 190 ? -4.26798  -21.58419 -9.52272  1.000 19.63001 ? 197 TYR   A CB  1 
ATOM   1654 C  CG  . TYR   A 1 190 ? -3.35945  -20.94272 -8.49858  1.000 16.33332 ? 197 TYR   A CG  1 
ATOM   1655 C  CD1 . TYR   A 1 190 ? -3.78140  -19.83111 -7.77972  1.000 23.12447 ? 197 TYR   A CD1 1 
ATOM   1656 C  CD2 . TYR   A 1 190 ? -2.11956  -21.49171 -8.18982  1.000 18.15191 ? 197 TYR   A CD2 1 
ATOM   1657 C  CE1 . TYR   A 1 190 ? -2.97723  -19.25523 -6.81506  1.000 19.61865 ? 197 TYR   A CE1 1 
ATOM   1658 C  CE2 . TYR   A 1 190 ? -1.30134  -20.91695 -7.22013  1.000 22.03868 ? 197 TYR   A CE2 1 
ATOM   1659 C  CZ  . TYR   A 1 190 ? -1.74265  -19.79531 -6.53748  1.000 20.19443 ? 197 TYR   A CZ  1 
ATOM   1660 O  OH  . TYR   A 1 190 ? -0.95810  -19.21729 -5.56146  1.000 22.20142 ? 197 TYR   A OH  1 
ATOM   1661 N  N   . LEU   A 1 191 ? -6.91807  -24.01039 -9.65994  1.000 22.16484 ? 198 LEU   A N   1 
ATOM   1662 C  CA  . LEU   A 1 191 ? -8.05393  -24.56011 -10.38283 1.000 23.11370 ? 198 LEU   A CA  1 
ATOM   1663 C  C   . LEU   A 1 191 ? -9.33653  -24.52686 -9.56798  1.000 25.08926 ? 198 LEU   A C   1 
ATOM   1664 O  O   . LEU   A 1 191 ? -10.39647 -24.87706 -10.09726 1.000 25.04037 ? 198 LEU   A O   1 
ATOM   1665 C  CB  . LEU   A 1 191 ? -7.77226  -26.00893 -10.79422 1.000 22.34461 ? 198 LEU   A CB  1 
ATOM   1666 C  CG  . LEU   A 1 191 ? -6.57234  -26.18151 -11.72219 1.000 22.71963 ? 198 LEU   A CG  1 
ATOM   1667 C  CD1 . LEU   A 1 191 ? -6.37720  -27.64597 -12.06942 1.000 27.33879 ? 198 LEU   A CD1 1 
ATOM   1668 C  CD2 . LEU   A 1 191 ? -6.74377  -25.33291 -12.96714 1.000 25.82631 ? 198 LEU   A CD2 1 
ATOM   1669 N  N   . GLU   A 1 192 ? -9.26463  -24.15539 -8.29277  1.000 20.32053 ? 199 GLU   A N   1 
ATOM   1670 C  CA  . GLU   A 1 192 ? -10.43420 -24.18787 -7.42599  1.000 21.78450 ? 199 GLU   A CA  1 
ATOM   1671 C  C   . GLU   A 1 192 ? -11.19419 -22.87666 -7.53289  1.000 24.88731 ? 199 GLU   A C   1 
ATOM   1672 O  O   . GLU   A 1 192 ? -10.59865 -21.79602 -7.53135  1.000 22.50012 ? 199 GLU   A O   1 
ATOM   1673 C  CB  . GLU   A 1 192 ? -10.04465 -24.45791 -5.97080  1.000 26.89776 ? 199 GLU   A CB  1 
ATOM   1674 C  CG  . GLU   A 1 192 ? -9.23475  -25.74001 -5.77161  1.000 31.25086 ? 199 GLU   A CG  1 
ATOM   1675 C  CD  . GLU   A 1 192 ? -8.95987  -26.03866 -4.30849  1.000 60.82135 ? 199 GLU   A CD  1 
ATOM   1676 O  OE1 . GLU   A 1 192 ? -9.89163  -25.89984 -3.48600  1.000 92.36878 ? 199 GLU   A OE1 1 
ATOM   1677 O  OE2 . GLU   A 1 192 ? -7.81320  -26.41180 -3.97957  1.000 74.47501 ? 199 GLU   A OE2 1 
ATOM   1678 N  N   . GLU   A 1 193 ? -12.52052 -22.98749 -7.61022  1.000 26.50073 ? 200 GLU   A N   1 
ATOM   1679 C  CA  . GLU   A 1 193 ? -13.35812 -21.82298 -7.86887  1.000 21.88043 ? 200 GLU   A CA  1 
ATOM   1680 C  C   . GLU   A 1 193 ? -13.17366 -20.75246 -6.79386  1.000 21.17554 ? 200 GLU   A C   1 
ATOM   1681 O  O   . GLU   A 1 193 ? -12.98558 -19.57253 -7.10760  1.000 24.21256 ? 200 GLU   A O   1 
ATOM   1682 C  CB  . GLU   A 1 193 ? -14.82279 -22.25788 -7.96485  1.000 24.57564 ? 200 GLU   A CB  1 
ATOM   1683 C  CG  . GLU   A 1 193 ? -15.80732 -21.10942 -7.97899  1.000 38.74602 ? 200 GLU   A CG  1 
ATOM   1684 C  CD  . GLU   A 1 193 ? -17.20999 -21.53648 -8.39485  1.000 75.51390 ? 200 GLU   A CD  1 
ATOM   1685 O  OE1 . GLU   A 1 193 ? -17.90306 -20.73693 -9.06134  1.000 62.10346 ? 200 GLU   A OE1 1 
ATOM   1686 O  OE2 . GLU   A 1 193 ? -17.62182 -22.66391 -8.04542  1.000 54.06657 ? 200 GLU   A OE2 1 
ATOM   1687 N  N   . ARG   A 1 194 ? -13.20940 -21.14086 -5.51636  1.000 23.99913 ? 201 ARG   A N   1 
ATOM   1688 C  CA  . ARG   A 1 194 ? -13.13748 -20.11785 -4.47541  1.000 24.94093 ? 201 ARG   A CA  1 
ATOM   1689 C  C   . ARG   A 1 194 ? -11.77178 -19.44708 -4.43574  1.000 24.98756 ? 201 ARG   A C   1 
ATOM   1690 O  O   . ARG   A 1 194 ? -11.67014 -18.27653 -4.05075  1.000 25.24516 ? 201 ARG   A O   1 
ATOM   1691 C  CB  . ARG   A 1 194 ? -13.46081 -20.70233 -3.10384  1.000 29.85436 ? 201 ARG   A CB  1 
ATOM   1692 C  CG  . ARG   A 1 194 ? -12.58430 -21.84643 -2.67632  1.000 36.32936 ? 201 ARG   A CG  1 
ATOM   1693 C  CD  . ARG   A 1 194 ? -13.10337 -22.38591 -1.35703  1.000 52.14605 ? 201 ARG   A CD  1 
ATOM   1694 N  NE  . ARG   A 1 194 ? -12.17937 -23.32474 -0.73782  1.000 46.92494 ? 201 ARG   A NE  1 
ATOM   1695 C  CZ  . ARG   A 1 194 ? -12.41124 -23.93562 0.41507   1.000 39.87822 ? 201 ARG   A CZ  1 
ATOM   1696 N  NH1 . ARG   A 1 194 ? -13.52955 -23.72787 1.09236   1.000 46.06688 ? 201 ARG   A NH1 1 
ATOM   1697 N  NH2 . ARG   A 1 194 ? -11.49257 -24.76153 0.90782   1.000 64.39115 ? 201 ARG   A NH2 1 
ATOM   1698 N  N   . ARG   A 1 195 ? -10.71424 -20.16566 -4.81685  1.000 19.79135 ? 202 ARG   A N   1 
ATOM   1699 C  CA  . ARG   A 1 195 ? -9.39037  -19.55372 -4.83333  1.000 20.50791 ? 202 ARG   A CA  1 
ATOM   1700 C  C   . ARG   A 1 195 ? -9.26911  -18.55975 -5.98024  1.000 19.98532 ? 202 ARG   A C   1 
ATOM   1701 O  O   . ARG   A 1 195 ? -8.72907  -17.46367 -5.80012  1.000 20.62329 ? 202 ARG   A O   1 
ATOM   1702 C  CB  . ARG   A 1 195 ? -8.31479  -20.63598 -4.92776  1.000 22.02161 ? 202 ARG   A CB  1 
ATOM   1703 C  CG  . ARG   A 1 195 ? -6.88108  -20.11789 -4.97395  1.000 22.16988 ? 202 ARG   A CG  1 
ATOM   1704 C  CD  . ARG   A 1 195 ? -6.46859  -19.54798 -3.62697  1.000 24.95222 ? 202 ARG   A CD  1 
ATOM   1705 N  NE  . ARG   A 1 195 ? -5.03496  -19.29864 -3.56998  1.000 22.41790 ? 202 ARG   A NE  1 
ATOM   1706 C  CZ  . ARG   A 1 195 ? -4.48046  -18.12280 -3.31130  1.000 24.26379 ? 202 ARG   A CZ  1 
ATOM   1707 N  NH1 . ARG   A 1 195 ? -5.21364  -17.04508 -3.08387  1.000 23.09101 ? 202 ARG   A NH1 1 
ATOM   1708 N  NH2 . ARG   A 1 195 ? -3.15420  -18.02356 -3.29162  1.000 25.13283 ? 202 ARG   A NH2 1 
ATOM   1709 N  N   . ILE   A 1 196 ? -9.78647  -18.91226 -7.16227  1.000 20.83406 ? 203 ILE   A N   1 
ATOM   1710 C  CA  . ILE   A 1 196 ? -9.73480  -17.98236 -8.28985  1.000 17.40546 ? 203 ILE   A CA  1 
ATOM   1711 C  C   . ILE   A 1 196 ? -10.56555 -16.74041 -7.99454  1.000 18.98450 ? 203 ILE   A C   1 
ATOM   1712 O  O   . ILE   A 1 196 ? -10.11893 -15.60993 -8.23924  1.000 18.38504 ? 203 ILE   A O   1 
ATOM   1713 C  CB  . ILE   A 1 196 ? -10.19047 -18.66648 -9.59244  1.000 22.89786 ? 203 ILE   A CB  1 
ATOM   1714 C  CG1 . ILE   A 1 196 ? -9.24331  -19.80867 -9.96792  1.000 19.83822 ? 203 ILE   A CG1 1 
ATOM   1715 C  CG2 . ILE   A 1 196 ? -10.25270 -17.64895 -10.73131 1.000 21.53775 ? 203 ILE   A CG2 1 
ATOM   1716 C  CD1 . ILE   A 1 196 ? -9.85281  -20.79876 -10.95494 1.000 28.13319 ? 203 ILE   A CD1 1 
ATOM   1717 N  N   . LYS   A 1 197 ? -11.77559 -16.92530 -7.44651  1.000 20.27793 ? 204 LYS   A N   1 
ATOM   1718 C  CA  . LYS   A 1 197 ? -12.61774 -15.77857 -7.10573  1.000 18.22030 ? 204 LYS   A CA  1 
ATOM   1719 C  C   . LYS   A 1 197 ? -11.91710 -14.84239 -6.13014  1.000 23.56665 ? 204 LYS   A C   1 
ATOM   1720 O  O   . LYS   A 1 197 ? -11.99262 -13.61544 -6.27102  1.000 23.87032 ? 204 LYS   A O   1 
ATOM   1721 C  CB  . LYS   A 1 197 ? -13.94970 -16.23069 -6.49784  1.000 20.20944 ? 204 LYS   A CB  1 
ATOM   1722 C  CG  . LYS   A 1 197 ? -14.87528 -17.00078 -7.40398  1.000 35.67637 ? 204 LYS   A CG  1 
ATOM   1723 C  CD  . LYS   A 1 197 ? -16.29093 -16.94652 -6.81750  1.000 33.84515 ? 204 LYS   A CD  1 
ATOM   1724 C  CE  . LYS   A 1 197 ? -17.26074 -17.88557 -7.50591  1.000 55.53510 ? 204 LYS   A CE  1 
ATOM   1725 N  NZ  . LYS   A 1 197 ? -17.70121 -18.97232 -6.58405  1.000 65.34330 ? 204 LYS   A NZ  1 
ATOM   1726 N  N   . GLU   A 1 198 ? -11.25428 -15.40675 -5.11836  1.000 18.88816 ? 205 GLU   A N   1 
ATOM   1727 C  CA  . GLU   A 1 198 ? -10.53782 -14.59210 -4.14420  1.000 21.09462 ? 205 GLU   A CA  1 
ATOM   1728 C  C   . GLU   A 1 198 ? -9.46274  -13.74860 -4.81727  1.000 20.79602 ? 205 GLU   A C   1 
ATOM   1729 O  O   . GLU   A 1 198 ? -9.30932  -12.55897 -4.51239  1.000 19.45909 ? 205 GLU   A O   1 
ATOM   1730 C  CB  . GLU   A 1 198 ? -9.92024  -15.50066 -3.07623  1.000 23.93456 ? 205 GLU   A CB  1 
ATOM   1731 C  CG  . GLU   A 1 198 ? -8.99984  -14.80039 -2.09408  1.000 22.20223 ? 205 GLU   A CG  1 
ATOM   1732 C  CD  . GLU   A 1 198 ? -8.29472  -15.77910 -1.17726  1.000 24.04333 ? 205 GLU   A CD  1 
ATOM   1733 O  OE1 . GLU   A 1 198 ? -7.72820  -16.76543 -1.69375  1.000 27.27229 ? 205 GLU   A OE1 1 
ATOM   1734 O  OE2 . GLU   A 1 198 ? -8.31636  -15.57134 0.05262   1.000 25.10345 ? 205 GLU   A OE2 1 
ATOM   1735 N  N   . ILE   A 1 199 ? -8.70618  -14.35112 -5.73288  1.000 17.49057 ? 206 ILE   A N   1 
ATOM   1736 C  CA  . ILE   A 1 199 ? -7.60179  -13.63947 -6.37490  1.000 20.49456 ? 206 ILE   A CA  1 
ATOM   1737 C  C   . ILE   A 1 199 ? -8.12767  -12.54037 -7.28055  1.000 22.66557 ? 206 ILE   A C   1 
ATOM   1738 O  O   . ILE   A 1 199 ? -7.58898  -11.42892 -7.30711  1.000 20.39583 ? 206 ILE   A O   1 
ATOM   1739 C  CB  . ILE   A 1 199 ? -6.70607  -14.62148 -7.15064  1.000 15.75911 ? 206 ILE   A CB  1 
ATOM   1740 C  CG1 . ILE   A 1 199 ? -6.08971  -15.64601 -6.19466  1.000 22.38924 ? 206 ILE   A CG1 1 
ATOM   1741 C  CG2 . ILE   A 1 199 ? -5.62956  -13.87641 -7.94073  1.000 19.63080 ? 206 ILE   A CG2 1 
ATOM   1742 C  CD1 . ILE   A 1 199 ? -5.54633  -16.86618 -6.89797  1.000 25.73950 ? 206 ILE   A CD1 1 
ATOM   1743 N  N   . VAL   A 1 200 ? -9.18775  -12.82749 -8.03484  1.000 17.79556 ? 207 VAL   A N   1 
ATOM   1744 C  CA  . VAL   A 1 200 ? -9.74967  -11.81442 -8.92010  1.000 16.62467 ? 207 VAL   A CA  1 
ATOM   1745 C  C   . VAL   A 1 200 ? -10.27589 -10.63656 -8.11522  1.000 18.82383 ? 207 VAL   A C   1 
ATOM   1746 O  O   . VAL   A 1 200 ? -10.04164 -9.47382  -8.46495  1.000 22.42157 ? 207 VAL   A O   1 
ATOM   1747 C  CB  . VAL   A 1 200 ? -10.84282 -12.43607 -9.80611  1.000 20.31415 ? 207 VAL   A CB  1 
ATOM   1748 C  CG1 . VAL   A 1 200 ? -11.63181 -11.34446 -10.50245 1.000 20.33724 ? 207 VAL   A CG1 1 
ATOM   1749 C  CG2 . VAL   A 1 200 ? -10.20859 -13.37636 -10.82367 1.000 18.86909 ? 207 VAL   A CG2 1 
ATOM   1750 N  N   . LYS   A 1 201 ? -10.96735 -10.91421 -7.00890  1.000 18.51395 ? 208 LYS   A N   1 
ATOM   1751 C  CA  . LYS   A 1 201 ? -11.49523 -9.83564  -6.17996  1.000 20.66273 ? 208 LYS   A CA  1 
ATOM   1752 C  C   . LYS   A 1 201 ? -10.37846 -9.04233  -5.51520  1.000 25.18045 ? 208 LYS   A C   1 
ATOM   1753 O  O   . LYS   A 1 201 ? -10.50303 -7.82499  -5.34185  1.000 27.11974 ? 208 LYS   A O   1 
ATOM   1754 C  CB  . LYS   A 1 201 ? -12.45106 -10.40793 -5.13074  1.000 22.18357 ? 208 LYS   A CB  1 
ATOM   1755 C  CG  . LYS   A 1 201 ? -13.04598 -9.38215  -4.18447  1.000 26.98569 ? 208 LYS   A CG  1 
ATOM   1756 C  CD  . LYS   A 1 201 ? -13.88688 -10.06275 -3.11914  1.000 36.90297 ? 208 LYS   A CD  1 
ATOM   1757 C  CE  . LYS   A 1 201 ? -14.45379 -9.06430  -2.12721  1.000 43.54792 ? 208 LYS   A CE  1 
ATOM   1758 N  NZ  . LYS   A 1 201 ? -15.43091 -9.71523  -1.21007  1.000 60.81466 ? 208 LYS   A NZ  1 
ATOM   1759 N  N   . LYS   A 1 202 ? -9.27754  -9.70839  -5.15825  1.000 23.90117 ? 209 LYS   A N   1 
ATOM   1760 C  CA  . LYS   A 1 202 ? -8.17949  -9.03133  -4.47177  1.000 22.65247 ? 209 LYS   A CA  1 
ATOM   1761 C  C   . LYS   A 1 202 ? -7.40178  -8.11361  -5.41260  1.000 23.00071 ? 209 LYS   A C   1 
ATOM   1762 O  O   . LYS   A 1 202 ? -7.07591  -6.97555  -5.05022  1.000 25.12219 ? 209 LYS   A O   1 
ATOM   1763 C  CB  . LYS   A 1 202 ? -7.24184  -10.06990 -3.85472  1.000 24.87831 ? 209 LYS   A CB  1 
ATOM   1764 C  CG  . LYS   A 1 202 ? -6.08656  -9.48133  -3.05696  1.000 30.05436 ? 209 LYS   A CG  1 
ATOM   1765 C  CD  . LYS   A 1 202 ? -5.29551  -10.59100 -2.38190  1.000 40.98302 ? 209 LYS   A CD  1 
ATOM   1766 C  CE  . LYS   A 1 202 ? -4.02277  -10.06609 -1.73999  1.000 59.59478 ? 209 LYS   A CE  1 
ATOM   1767 N  NZ  . LYS   A 1 202 ? -4.29988  -8.92488  -0.82584  1.000 62.40669 ? 209 LYS   A NZ  1 
ATOM   1768 N  N   . HIS   A 1 203 ? -7.10112  -8.58364  -6.62654  1.000 23.46449 ? 210 HIS   A N   1 
ATOM   1769 C  CA  . HIS   A 1 203 ? -6.12309  -7.92662  -7.48387  1.000 29.65247 ? 210 HIS   A CA  1 
ATOM   1770 C  C   . HIS   A 1 203 ? -6.69095  -7.34847  -8.77078  1.000 26.24272 ? 210 HIS   A C   1 
ATOM   1771 O  O   . HIS   A 1 203 ? -6.00481  -6.54900  -9.41656  1.000 27.20247 ? 210 HIS   A O   1 
ATOM   1772 C  CB  . HIS   A 1 203 ? -5.00501  -8.90975  -7.86992  1.000 29.13548 ? 210 HIS   A CB  1 
ATOM   1773 C  CG  . HIS   A 1 203 ? -4.19481  -9.39328  -6.71037  1.000 23.29582 ? 210 HIS   A CG  1 
ATOM   1774 N  ND1 . HIS   A 1 203 ? -3.36380  -8.56729  -5.98570  1.000 25.68247 ? 210 HIS   A ND1 1 
ATOM   1775 C  CD2 . HIS   A 1 203 ? -4.08329  -10.62333 -6.15315  1.000 27.83748 ? 210 HIS   A CD2 1 
ATOM   1776 C  CE1 . HIS   A 1 203 ? -2.77939  -9.26499  -5.02737  1.000 32.09023 ? 210 HIS   A CE1 1 
ATOM   1777 N  NE2 . HIS   A 1 203 ? -3.20012  -10.51501 -5.10566  1.000 29.94413 ? 210 HIS   A NE2 1 
ATOM   1778 N  N   . SER   A 1 204 ? -7.90005  -7.73497  -9.17500  1.000 25.19790 ? 211 SER   A N   1 
ATOM   1779 C  CA  . SER   A 1 204 ? -8.42168  -7.35867  -10.48283 1.000 23.29789 ? 211 SER   A CA  1 
ATOM   1780 C  C   . SER   A 1 204 ? -9.82465  -6.76847  -10.38885 1.000 25.35998 ? 211 SER   A C   1 
ATOM   1781 O  O   . SER   A 1 204 ? -10.56803 -6.78833  -11.37833 1.000 25.32920 ? 211 SER   A O   1 
ATOM   1782 C  CB  . SER   A 1 204 ? -8.41509  -8.56733  -11.42803 1.000 28.10350 ? 211 SER   A CB  1 
ATOM   1783 O  OG  . SER   A 1 204 ? -7.10356  -9.11175  -11.53107 1.000 27.95718 ? 211 SER   A OG  1 
ATOM   1784 N  N   . GLN   A 1 205 ? -10.19518 -6.22979  -9.22761  1.000 27.18004 ? 212 GLN   A N   1 
ATOM   1785 C  CA  . GLN   A 1 205 ? -11.57007 -5.79654  -9.01626  1.000 47.56047 ? 212 GLN   A CA  1 
ATOM   1786 C  C   . GLN   A 1 205 ? -11.96195 -4.61848  -9.89877  1.000 45.55260 ? 212 GLN   A C   1 
ATOM   1787 O  O   . GLN   A 1 205 ? -13.15841 -4.34088  -10.03640 1.000 43.55175 ? 212 GLN   A O   1 
ATOM   1788 C  CB  . GLN   A 1 205 ? -11.78391 -5.43115  -7.54476  1.000 39.41263 ? 212 GLN   A CB  1 
ATOM   1789 C  CG  . GLN   A 1 205 ? -10.89183 -4.31201  -7.05314  1.000 51.46526 ? 212 GLN   A CG  1 
ATOM   1790 C  CD  . GLN   A 1 205 ? -9.71991  -4.81304  -6.22840  1.000 86.35797 ? 212 GLN   A CD  1 
ATOM   1791 O  OE1 . GLN   A 1 205 ? -8.75376  -5.36098  -6.76916  1.000 48.89044 ? 212 GLN   A OE1 1 
ATOM   1792 N  NE2 . GLN   A 1 205 ? -9.79413  -4.61897  -4.91138  1.000 60.91290 ? 212 GLN   A NE2 1 
ATOM   1793 N  N   . PHE   A 1 206 ? -10.99717 -3.93404  -10.51278 1.000 37.94962 ? 213 PHE   A N   1 
ATOM   1794 C  CA  . PHE   A 1 206 ? -11.28482 -2.70811  -11.24030 1.000 37.18388 ? 213 PHE   A CA  1 
ATOM   1795 C  C   . PHE   A 1 206 ? -10.98701 -2.83601  -12.73200 1.000 30.77745 ? 213 PHE   A C   1 
ATOM   1796 O  O   . PHE   A 1 206 ? -10.93537 -1.82116  -13.43606 1.000 45.06419 ? 213 PHE   A O   1 
ATOM   1797 C  CB  . PHE   A 1 206 ? -10.49356 -1.55926  -10.61718 1.000 38.28993 ? 213 PHE   A CB  1 
ATOM   1798 C  CG  . PHE   A 1 206 ? -10.95140 -1.22651  -9.22199  1.000 39.74681 ? 213 PHE   A CG  1 
ATOM   1799 C  CD1 . PHE   A 1 206 ? -12.29266 -1.29985  -8.88968  1.000 56.88279 ? 213 PHE   A CD1 1 
ATOM   1800 C  CD2 . PHE   A 1 206 ? -10.03823 -0.90166  -8.23433  1.000 42.80167 ? 213 PHE   A CD2 1 
ATOM   1801 C  CE1 . PHE   A 1 206 ? -12.72500 -1.01886  -7.60999  1.000 65.29870 ? 213 PHE   A CE1 1 
ATOM   1802 C  CE2 . PHE   A 1 206 ? -10.46249 -0.61906  -6.94755  1.000 51.43217 ? 213 PHE   A CE2 1 
ATOM   1803 C  CZ  . PHE   A 1 206 ? -11.80703 -0.68327  -6.63417  1.000 55.32226 ? 213 PHE   A CZ  1 
ATOM   1804 N  N   . ILE   A 1 207 ? -10.78608 -4.05779  -13.22698 1.000 24.12481 ? 214 ILE   A N   1 
ATOM   1805 C  CA  . ILE   A 1 207 ? -10.59597 -4.28942  -14.65565 1.000 22.02075 ? 214 ILE   A CA  1 
ATOM   1806 C  C   . ILE   A 1 207 ? -11.89107 -3.95559  -15.38372 1.000 31.75896 ? 214 ILE   A C   1 
ATOM   1807 O  O   . ILE   A 1 207 ? -12.97820 -4.37872  -14.97025 1.000 25.40212 ? 214 ILE   A O   1 
ATOM   1808 C  CB  . ILE   A 1 207 ? -10.16179 -5.74437  -14.90092 1.000 22.38240 ? 214 ILE   A CB  1 
ATOM   1809 C  CG1 . ILE   A 1 207 ? -8.74826  -5.98003  -14.35062 1.000 20.81590 ? 214 ILE   A CG1 1 
ATOM   1810 C  CG2 . ILE   A 1 207 ? -10.21218 -6.10639  -16.37895 1.000 19.97961 ? 214 ILE   A CG2 1 
ATOM   1811 C  CD1 . ILE   A 1 207 ? -7.67844  -5.14637  -15.01477 1.000 24.83947 ? 214 ILE   A CD1 1 
ATOM   1812 N  N   . GLY   A 1 208 ? -11.78401 -3.18688  -16.46770 1.000 22.07879 ? 215 GLY   A N   1 
ATOM   1813 C  CA  . GLY   A 1 208 ? -12.95501 -2.63451  -17.12273 1.000 23.72190 ? 215 GLY   A CA  1 
ATOM   1814 C  C   . GLY   A 1 208 ? -13.58348 -3.51095  -18.18621 1.000 27.18132 ? 215 GLY   A C   1 
ATOM   1815 O  O   . GLY   A 1 208 ? -14.19035 -3.00866  -19.13820 1.000 29.14822 ? 215 GLY   A O   1 
ATOM   1816 N  N   . TYR   A 1 209 ? -13.46292 -4.82246  -18.02477 1.000 19.98894 ? 216 TYR   A N   1 
ATOM   1817 C  CA  . TYR   A 1 209 ? -14.02670 -5.79457  -18.94519 1.000 20.36018 ? 216 TYR   A CA  1 
ATOM   1818 C  C   . TYR   A 1 209 ? -14.61496 -6.93089  -18.12681 1.000 20.32696 ? 216 TYR   A C   1 
ATOM   1819 O  O   . TYR   A 1 209 ? -14.10646 -7.24087  -17.04319 1.000 20.57769 ? 216 TYR   A O   1 
ATOM   1820 C  CB  . TYR   A 1 209 ? -12.95725 -6.33537  -19.90900 1.000 17.47595 ? 216 TYR   A CB  1 
ATOM   1821 C  CG  . TYR   A 1 209 ? -12.36436 -5.25672  -20.78082 1.000 20.90285 ? 216 TYR   A CG  1 
ATOM   1822 C  CD1 . TYR   A 1 209 ? -13.02458 -4.82277  -21.92070 1.000 20.64219 ? 216 TYR   A CD1 1 
ATOM   1823 C  CD2 . TYR   A 1 209 ? -11.15723 -4.65153  -20.44796 1.000 19.10251 ? 216 TYR   A CD2 1 
ATOM   1824 C  CE1 . TYR   A 1 209 ? -12.49651 -3.82382  -22.71459 1.000 20.42811 ? 216 TYR   A CE1 1 
ATOM   1825 C  CE2 . TYR   A 1 209 ? -10.61619 -3.65066  -21.24060 1.000 19.23745 ? 216 TYR   A CE2 1 
ATOM   1826 C  CZ  . TYR   A 1 209 ? -11.29446 -3.24397  -22.37359 1.000 19.02927 ? 216 TYR   A CZ  1 
ATOM   1827 O  OH  . TYR   A 1 209 ? -10.78450 -2.24707  -23.16344 1.000 24.72549 ? 216 TYR   A OH  1 
ATOM   1828 N  N   . PRO   A 1 210 ? -15.68472 -7.56317  -18.60855 1.000 21.20544 ? 217 PRO   A N   1 
ATOM   1829 C  CA  . PRO   A 1 210 ? -16.27788 -8.67441  -17.85296 1.000 18.00449 ? 217 PRO   A CA  1 
ATOM   1830 C  C   . PRO   A 1 210 ? -15.32288 -9.85748  -17.76932 1.000 24.71972 ? 217 PRO   A C   1 
ATOM   1831 O  O   . PRO   A 1 210 ? -14.74384 -10.28652 -18.77113 1.000 23.90368 ? 217 PRO   A O   1 
ATOM   1832 C  CB  . PRO   A 1 210 ? -17.54701 -9.01632  -18.64710 1.000 23.58451 ? 217 PRO   A CB  1 
ATOM   1833 C  CG  . PRO   A 1 210 ? -17.32137 -8.47523  -20.00722 1.000 24.85130 ? 217 PRO   A CG  1 
ATOM   1834 C  CD  . PRO   A 1 210 ? -16.42139 -7.27104  -19.85191 1.000 21.82497 ? 217 PRO   A CD  1 
ATOM   1835 N  N   . ILE   A 1 211 ? -15.13236 -10.35326 -16.55171 1.000 20.86913 ? 218 ILE   A N   1 
ATOM   1836 C  CA  . ILE   A 1 211 ? -14.30557 -11.52372 -16.28681 1.000 16.76627 ? 218 ILE   A CA  1 
ATOM   1837 C  C   . ILE   A 1 211 ? -15.24296 -12.63861 -15.86098 1.000 18.32331 ? 218 ILE   A C   1 
ATOM   1838 O  O   . ILE   A 1 211 ? -15.91258 -12.53200 -14.82551 1.000 21.89036 ? 218 ILE   A O   1 
ATOM   1839 C  CB  . ILE   A 1 211 ? -13.25189 -11.25180 -15.20483 1.000 18.96081 ? 218 ILE   A CB  1 
ATOM   1840 C  CG1 . ILE   A 1 211 ? -12.33143 -10.09500 -15.61529 1.000 17.92988 ? 218 ILE   A CG1 1 
ATOM   1841 C  CG2 . ILE   A 1 211 ? -12.45994 -12.51981 -14.91455 1.000 16.59951 ? 218 ILE   A CG2 1 
ATOM   1842 C  CD1 . ILE   A 1 211 ? -11.44704 -9.60327  -14.47487 1.000 21.01423 ? 218 ILE   A CD1 1 
ATOM   1843 N  N   . THR   A 1 212 ? -15.31376 -13.69102 -16.66413 1.000 17.16695 ? 219 THR   A N   1 
ATOM   1844 C  CA  . THR   A 1 212 ? -16.23206 -14.79355 -16.41135 1.000 15.56030 ? 219 THR   A CA  1 
ATOM   1845 C  C   . THR   A 1 212 ? -15.42008 -16.00242 -15.98291 1.000 13.60437 ? 219 THR   A C   1 
ATOM   1846 O  O   . THR   A 1 212 ? -14.56496 -16.47879 -16.73687 1.000 17.44743 ? 219 THR   A O   1 
ATOM   1847 C  CB  . THR   A 1 212 ? -17.06431 -15.11902 -17.65018 1.000 20.97829 ? 219 THR   A CB  1 
ATOM   1848 O  OG1 . THR   A 1 212 ? -17.80608 -13.95606 -18.04407 1.000 21.36991 ? 219 THR   A OG1 1 
ATOM   1849 C  CG2 . THR   A 1 212 ? -18.03468 -16.25730 -17.34716 1.000 22.64837 ? 219 THR   A CG2 1 
ATOM   1850 N  N   . LEU   A 1 213 ? -15.67898 -16.48361 -14.77562 1.000 17.57050 ? 220 LEU   A N   1 
ATOM   1851 C  CA  . LEU   A 1 213 ? -15.03771 -17.69117 -14.27342 1.000 18.34425 ? 220 LEU   A CA  1 
ATOM   1852 C  C   . LEU   A 1 213 ? -15.94592 -18.86753 -14.61906 1.000 20.82453 ? 220 LEU   A C   1 
ATOM   1853 O  O   . LEU   A 1 213 ? -17.06217 -18.97777 -14.09250 1.000 17.30357 ? 220 LEU   A O   1 
ATOM   1854 C  CB  . LEU   A 1 213 ? -14.78868 -17.58224 -12.77102 1.000 19.80760 ? 220 LEU   A CB  1 
ATOM   1855 C  CG  . LEU   A 1 213 ? -14.25332 -18.81440 -12.04355 1.000 23.51978 ? 220 LEU   A CG  1 
ATOM   1856 C  CD1 . LEU   A 1 213 ? -13.00602 -19.34614 -12.72883 1.000 22.05400 ? 220 LEU   A CD1 1 
ATOM   1857 C  CD2 . LEU   A 1 213 ? -13.95365 -18.46208 -10.58460 1.000 22.12332 ? 220 LEU   A CD2 1 
ATOM   1858 N  N   . PHE   A 1 214 ? -15.48929 -19.70872 -15.54169 1.000 19.89435 ? 221 PHE   A N   1 
ATOM   1859 C  CA  . PHE   A 1 214 ? -16.24401 -20.88872 -15.93926 1.000 21.12515 ? 221 PHE   A CA  1 
ATOM   1860 C  C   . PHE   A 1 214 ? -16.24039 -21.90098 -14.79916 1.000 23.89815 ? 221 PHE   A C   1 
ATOM   1861 O  O   . PHE   A 1 214 ? -15.28319 -21.99189 -14.02686 1.000 21.99692 ? 221 PHE   A O   1 
ATOM   1862 C  CB  . PHE   A 1 214 ? -15.61699 -21.53331 -17.18034 1.000 18.58120 ? 221 PHE   A CB  1 
ATOM   1863 C  CG  . PHE   A 1 214 ? -15.91279 -20.82270 -18.48210 1.000 17.44687 ? 221 PHE   A CG  1 
ATOM   1864 C  CD1 . PHE   A 1 214 ? -16.01218 -19.44048 -18.54745 1.000 17.13918 ? 221 PHE   A CD1 1 
ATOM   1865 C  CD2 . PHE   A 1 214 ? -16.03112 -21.55283 -19.65730 1.000 20.07086 ? 221 PHE   A CD2 1 
ATOM   1866 C  CE1 . PHE   A 1 214 ? -16.26011 -18.80125 -19.75805 1.000 16.04865 ? 221 PHE   A CE1 1 
ATOM   1867 C  CE2 . PHE   A 1 214 ? -16.27331 -20.92521 -20.87093 1.000 21.12742 ? 221 PHE   A CE2 1 
ATOM   1868 C  CZ  . PHE   A 1 214 ? -16.39482 -19.54542 -20.92082 1.000 18.92331 ? 221 PHE   A CZ  1 
ATOM   1869 N  N   . VAL   A 1 215 ? -17.30710 -22.68526 -14.70612 1.000 21.02495 ? 222 VAL   A N   1 
ATOM   1870 C  CA  . VAL   A 1 215 ? -17.37833 -23.76920 -13.73788 1.000 22.36046 ? 222 VAL   A CA  1 
ATOM   1871 C  C   . VAL   A 1 215 ? -17.22305 -25.09776 -14.47479 1.000 24.22034 ? 222 VAL   A C   1 
ATOM   1872 O  O   . VAL   A 1 215 ? -17.32532 -25.17532 -15.69849 1.000 22.80226 ? 222 VAL   A O   1 
ATOM   1873 C  CB  . VAL   A 1 215 ? -18.67763 -23.73178 -12.91290 1.000 43.45959 ? 222 VAL   A CB  1 
ATOM   1874 C  CG1 . VAL   A 1 215 ? -18.54023 -22.74016 -11.76263 1.000 47.27930 ? 222 VAL   A CG1 1 
ATOM   1875 C  CG2 . VAL   A 1 215 ? -19.83840 -23.35234 -13.78842 1.000 28.46657 ? 222 VAL   A CG2 1 
ATOM   1876 N  N   . GLU   A 1 216 ? -16.96723 -26.15146 -13.71226 1.000 25.78790 ? 223 GLU   A N   1 
ATOM   1877 C  CA  . GLU   A 1 216 ? -16.74693 -27.47785 -14.26587 1.000 30.47107 ? 223 GLU   A CA  1 
ATOM   1878 C  C   . GLU   A 1 216 ? -17.85438 -28.43548 -13.84988 1.000 33.86309 ? 223 GLU   A C   1 
ATOM   1879 O  O   . GLU   A 1 216 ? -18.52173 -28.24092 -12.83248 1.000 42.27913 ? 223 GLU   A O   1 
ATOM   1880 C  CB  . GLU   A 1 216 ? -15.38728 -28.03224 -13.83261 1.000 34.81953 ? 223 GLU   A CB  1 
ATOM   1881 C  CG  . GLU   A 1 216 ? -14.22292 -27.14520 -14.18838 1.000 32.48476 ? 223 GLU   A CG  1 
ATOM   1882 C  CD  . GLU   A 1 216 ? -12.91873 -27.68168 -13.64407 1.000 49.15827 ? 223 GLU   A CD  1 
ATOM   1883 O  OE1 . GLU   A 1 216 ? -12.42225 -28.68614 -14.19617 1.000 33.99058 ? 223 GLU   A OE1 1 
ATOM   1884 O  OE2 . GLU   A 1 216 ? -12.38002 -27.08073 -12.68550 1.000 43.40755 ? 223 GLU   A OE2 1 
ATOM   1885 N  N   . LYS   A 1 217 ? -18.03517 -29.48081 -14.65888 1.000 40.36854 ? 224 LYS   A N   1 
ATOM   1886 C  CA  . LYS   A 1 217 ? -19.04199 -30.51325 -14.40607 1.000 54.12154 ? 224 LYS   A CA  1 
ATOM   1887 C  C   . LYS   A 1 217 ? -18.87390 -31.13358 -13.02042 1.000 64.06381 ? 224 LYS   A C   1 
ATOM   1888 O  O   . LYS   A 1 217 ? -17.76026 -31.45822 -12.60958 1.000 54.77456 ? 224 LYS   A O   1 
ATOM   1889 C  CB  . LYS   A 1 217 ? -18.97292 -31.61807 -15.47001 1.000 51.62154 ? 224 LYS   A CB  1 
ATOM   1890 C  CG  . LYS   A 1 217 ? -17.68857 -31.61920 -16.29049 1.000 82.47644 ? 224 LYS   A CG  1 
ATOM   1891 C  CD  . LYS   A 1 217 ? -17.65660 -32.76968 -17.29544 1.000 80.54129 ? 224 LYS   A CD  1 
ATOM   1892 C  CE  . LYS   A 1 217 ? -16.40795 -32.70341 -18.17573 1.000 81.76066 ? 224 LYS   A CE  1 
ATOM   1893 N  NZ  . LYS   A 1 217 ? -16.07758 -34.02211 -18.79316 1.000 71.57616 ? 224 LYS   A NZ  1 
HETATM 1894 C  C1  B A1AYX B 2 .   ? 9.17957   -13.27374 -10.12641 0.347 35.32398 ? 301 A1AYX A C1  1 
HETATM 1895 C  C2  B A1AYX B 2 .   ? 9.35125   -14.16231 -9.08988  0.347 33.67301 ? 301 A1AYX A C2  1 
HETATM 1896 C  C3  B A1AYX B 2 .   ? 10.63008  -14.42025 -8.64826  0.347 31.70937 ? 301 A1AYX A C3  1 
HETATM 1897 C  C4  B A1AYX B 2 .   ? 11.71802  -13.79701 -9.23090  0.347 33.93368 ? 301 A1AYX A C4  1 
HETATM 1898 C  C5  B A1AYX B 2 .   ? 11.52947  -12.90065 -10.27121 0.347 32.95896 ? 301 A1AYX A C5  1 
HETATM 1899 C  C6  B A1AYX B 2 .   ? 13.77002  -11.81677 -10.25792 0.347 39.92571 ? 301 A1AYX A C6  1 
HETATM 1900 C  C7  B A1AYX B 2 .   ? 14.91020  -11.45726 -11.19617 0.347 33.92620 ? 301 A1AYX A C7  1 
HETATM 1901 C  C8  B A1AYX B 2 .   ? 14.52303  -10.39494 -12.10243 0.347 30.34728 ? 301 A1AYX A C8  1 
HETATM 1902 C  C9  B A1AYX B 2 .   ? 10.24717  -12.63365 -10.73138 0.347 31.05447 ? 301 A1AYX A C9  1 
HETATM 1903 N  N1  B A1AYX B 2 .   ? 12.65713  -12.28517 -10.86248 0.347 33.88424 ? 301 A1AYX A N1  1 
HETATM 1904 N  N2  B A1AYX B 2 .   ? 14.21654  -9.54838  -12.79556 0.347 41.95379 ? 301 A1AYX A N2  1 
HETATM 1905 O  O1  B A1AYX B 2 .   ? 13.89589  -11.75347 -9.04233  0.347 49.16978 ? 301 A1AYX A O1  1 
HETATM 1906 CL CL1 B A1AYX B 2 .   ? 7.57008   -12.93963 -10.69964 0.347 37.57852 ? 301 A1AYX A CL1 1 
HETATM 1907 O  O   . HOH   C 3 .   ? 10.06586  -6.06969  -1.62365  1.000 52.59647 ? 401 HOH   A O   1 
HETATM 1908 O  O   . HOH   C 3 .   ? -12.440   -27.850   -30.221   1.000 35.62965 ? 402 HOH   A O   1 
HETATM 1909 O  O   . HOH   C 3 .   ? 11.67618  -21.73267 -40.58034 1.000 44.41971 ? 403 HOH   A O   1 
HETATM 1910 O  O   . HOH   C 3 .   ? 16.29997  1.54173   -15.16441 1.000 47.11542 ? 404 HOH   A O   1 
HETATM 1911 O  O   . HOH   C 3 .   ? -2.94837  -2.87658  -35.42575 1.000 40.92996 ? 405 HOH   A O   1 
HETATM 1912 O  O   . HOH   C 3 .   ? 3.17648   -6.14729  -11.15648 1.000 29.57175 ? 406 HOH   A O   1 
HETATM 1913 O  O   . HOH   C 3 .   ? 2.17617   -15.65365 -41.03871 1.000 45.73552 ? 407 HOH   A O   1 
HETATM 1914 O  O   . HOH   C 3 .   ? 17.21853  0.63287   -17.84145 1.000 42.78669 ? 408 HOH   A O   1 
HETATM 1915 O  O   . HOH   C 3 .   ? -3.82491  -13.22385 -42.53637 1.000 48.68351 ? 409 HOH   A O   1 
HETATM 1916 O  O   . HOH   C 3 .   ? -12.30958 -25.84839 -3.42964  1.000 52.78209 ? 410 HOH   A O   1 
HETATM 1917 O  O   . HOH   C 3 .   ? -1.61764  -29.06699 -5.91981  1.000 32.84043 ? 411 HOH   A O   1 
HETATM 1918 O  O   . HOH   C 3 .   ? -16.91683 -20.31989 -4.61494  1.000 51.21375 ? 412 HOH   A O   1 
HETATM 1919 O  O   . HOH   C 3 .   ? 9.15758   -3.17370  -20.49642 1.000 44.71016 ? 413 HOH   A O   1 
HETATM 1920 O  O   . HOH   C 3 .   ? -16.23252 -25.53888 -17.95502 1.000 26.21921 ? 414 HOH   A O   1 
HETATM 1921 O  O   . HOH   C 3 .   ? 18.29514  -7.07947  -20.37923 1.000 34.01636 ? 415 HOH   A O   1 
HETATM 1922 O  O   . HOH   C 3 .   ? -4.31044  0.46206   -22.10296 1.000 37.63313 ? 416 HOH   A O   1 
HETATM 1923 O  O   . HOH   C 3 .   ? -8.73960  -11.86679 -36.37139 1.000 28.40541 ? 417 HOH   A O   1 
HETATM 1924 O  O   . HOH   C 3 .   ? 0.37464   -14.77219 -1.38936  1.000 39.51883 ? 418 HOH   A O   1 
HETATM 1925 O  O   . HOH   C 3 .   ? -7.92220  -22.70431 -30.38198 1.000 44.90529 ? 419 HOH   A O   1 
HETATM 1926 O  O   . HOH   C 3 .   ? 0.61526   -26.98696 -37.19526 1.000 48.10888 ? 420 HOH   A O   1 
HETATM 1927 O  O   . HOH   C 3 .   ? -0.19885  -5.51060  -38.48347 1.000 44.10844 ? 421 HOH   A O   1 
HETATM 1928 O  O   . HOH   C 3 .   ? 1.45609   -7.88572  -16.56034 1.000 24.25246 ? 422 HOH   A O   1 
HETATM 1929 O  O   . HOH   C 3 .   ? 3.58770   -29.81174 -25.84297 1.000 53.74936 ? 423 HOH   A O   1 
HETATM 1930 O  O   . HOH   C 3 .   ? 1.30910   -26.70193 -2.78569  1.000 50.94794 ? 424 HOH   A O   1 
HETATM 1931 O  O   . HOH   C 3 .   ? -18.78300 -10.99871 -23.71745 1.000 31.43743 ? 425 HOH   A O   1 
HETATM 1932 O  O   . HOH   C 3 .   ? 3.13416   -20.34591 -2.78050  1.000 35.12567 ? 426 HOH   A O   1 
HETATM 1933 O  O   . HOH   C 3 .   ? 15.47317  -12.42760 -7.05891  1.000 49.47439 ? 427 HOH   A O   1 
HETATM 1934 O  O   . HOH   C 3 .   ? -2.72956  -6.09213  -6.57741  1.000 37.91704 ? 428 HOH   A O   1 
HETATM 1935 O  O   . HOH   C 3 .   ? -0.33173  -5.33765  -18.34242 1.000 28.51449 ? 429 HOH   A O   1 
HETATM 1936 O  O   . HOH   C 3 .   ? 3.53274   -7.74222  -36.58076 1.000 33.59838 ? 430 HOH   A O   1 
HETATM 1937 O  O   . HOH   C 3 .   ? 7.82405   -23.13771 -14.27838 1.000 25.15568 ? 431 HOH   A O   1 
HETATM 1938 O  O   . HOH   C 3 .   ? 7.66830   -27.73271 -23.99922 1.000 30.66621 ? 432 HOH   A O   1 
HETATM 1939 O  O   . HOH   C 3 .   ? 9.11094   -26.39407 -17.07050 1.000 28.67152 ? 433 HOH   A O   1 
HETATM 1940 O  O   . HOH   C 3 .   ? -13.04881 -7.39879  -12.02025 1.000 33.09220 ? 434 HOH   A O   1 
HETATM 1941 O  O   . HOH   C 3 .   ? 14.06527  -11.13724 -29.70426 1.000 42.48386 ? 435 HOH   A O   1 
HETATM 1942 O  O   . HOH   C 3 .   ? 5.96531   -21.10516 -0.08077  1.000 28.15255 ? 436 HOH   A O   1 
HETATM 1943 O  O   . HOH   C 3 .   ? 7.67780   -18.81939 -6.57369  1.000 26.62000 ? 437 HOH   A O   1 
HETATM 1944 O  O   . HOH   C 3 .   ? -6.43326  -5.15478  -38.91858 1.000 46.72905 ? 438 HOH   A O   1 
HETATM 1945 O  O   . HOH   C 3 .   ? 10.32199  -23.24717 -41.38128 1.000 58.93617 ? 439 HOH   A O   1 
HETATM 1946 O  O   . HOH   C 3 .   ? -4.02132  -4.99602  -8.59416  1.000 45.00550 ? 440 HOH   A O   1 
HETATM 1947 O  O   . HOH   C 3 .   ? -9.31372  -2.32733  -17.56913 1.000 22.97161 ? 441 HOH   A O   1 
HETATM 1948 O  O   . HOH   C 3 .   ? 9.84765   -14.74123 -25.25107 1.000 22.30510 ? 442 HOH   A O   1 
HETATM 1949 O  O   . HOH   C 3 .   ? 13.61242  -14.13899 -26.79482 1.000 24.63047 ? 443 HOH   A O   1 
HETATM 1950 O  O   . HOH   C 3 .   ? 11.22416  -8.06108  -27.33604 1.000 23.89294 ? 444 HOH   A O   1 
HETATM 1951 O  O   . HOH   C 3 .   ? -2.18383  -13.71225 -35.62268 1.000 24.01565 ? 445 HOH   A O   1 
HETATM 1952 O  O   . HOH   C 3 .   ? -8.08907  1.80412   -36.45420 1.000 39.27078 ? 446 HOH   A O   1 
HETATM 1953 O  O   . HOH   C 3 .   ? 15.53252  -0.62478  -19.63513 1.000 38.33867 ? 447 HOH   A O   1 
HETATM 1954 O  O   . HOH   C 3 .   ? 11.48081  -27.40471 -34.70845 1.000 26.46091 ? 448 HOH   A O   1 
HETATM 1955 O  O   . HOH   C 3 .   ? -13.39622 -0.78681  -20.38454 1.000 31.22707 ? 449 HOH   A O   1 
HETATM 1956 O  O   . HOH   C 3 .   ? -16.29832 -12.68796 -19.84858 1.000 21.14808 ? 450 HOH   A O   1 
HETATM 1957 O  O   . HOH   C 3 .   ? 0.72371   -29.55218 -15.98116 1.000 39.83005 ? 451 HOH   A O   1 
HETATM 1958 O  O   . HOH   C 3 .   ? -10.65764 -6.20552  -2.93986  1.000 54.37583 ? 452 HOH   A O   1 
HETATM 1959 O  O   . HOH   C 3 .   ? -7.69775  -28.22304 -7.82493  1.000 32.01045 ? 453 HOH   A O   1 
HETATM 1960 O  O   . HOH   C 3 .   ? -5.73256  -2.12647  -19.38857 1.000 23.88460 ? 454 HOH   A O   1 
HETATM 1961 O  O   . HOH   C 3 .   ? -8.45543  4.77517   -33.49434 1.000 31.94451 ? 455 HOH   A O   1 
HETATM 1962 O  O   . HOH   C 3 .   ? -17.12476 -5.52483  -22.83042 1.000 29.08010 ? 456 HOH   A O   1 
HETATM 1963 O  O   . HOH   C 3 .   ? 0.34924   -22.15967 -2.21872  1.000 48.52937 ? 457 HOH   A O   1 
HETATM 1964 O  O   . HOH   C 3 .   ? 0.81241   -21.03483 -4.67022  1.000 31.38862 ? 458 HOH   A O   1 
HETATM 1965 O  O   . HOH   C 3 .   ? -15.85277 0.22784   -30.48736 1.000 40.01520 ? 459 HOH   A O   1 
HETATM 1966 O  O   . HOH   C 3 .   ? 11.46957  -28.30376 -30.42512 1.000 32.84970 ? 460 HOH   A O   1 
HETATM 1967 O  O   . HOH   C 3 .   ? 0.75471   -5.26958  -14.02743 1.000 41.06147 ? 461 HOH   A O   1 
HETATM 1968 O  O   . HOH   C 3 .   ? -7.02109  -28.10330 -21.35100 1.000 51.80084 ? 462 HOH   A O   1 
HETATM 1969 O  O   . HOH   C 3 .   ? -7.67533  -24.32929 -23.04446 1.000 30.61271 ? 463 HOH   A O   1 
HETATM 1970 O  O   . HOH   C 3 .   ? -1.42576  -6.25758  -26.16493 1.000 24.35775 ? 464 HOH   A O   1 
HETATM 1971 O  O   . HOH   C 3 .   ? -0.90104  -11.22843 -3.07094  1.000 38.88570 ? 465 HOH   A O   1 
HETATM 1972 O  O   . HOH   C 3 .   ? -5.41799  -7.64187  -13.05259 1.000 20.61846 ? 466 HOH   A O   1 
HETATM 1973 O  O   . HOH   C 3 .   ? -5.31983  -10.40175 -27.37177 1.000 19.87685 ? 467 HOH   A O   1 
HETATM 1974 O  O   . HOH   C 3 .   ? 6.67600   -29.61873 -20.05247 1.000 35.73229 ? 468 HOH   A O   1 
HETATM 1975 O  O   . HOH   C 3 .   ? 3.24461   -24.37191 -38.67466 1.000 35.16645 ? 469 HOH   A O   1 
HETATM 1976 O  O   . HOH   C 3 .   ? 9.56496   -10.93317 -34.73922 1.000 38.79882 ? 470 HOH   A O   1 
HETATM 1977 O  O   . HOH   C 3 .   ? -19.39219 -9.91653  -33.14311 1.000 44.52890 ? 471 HOH   A O   1 
HETATM 1978 O  O   . HOH   C 3 .   ? -20.51707 -14.09266 -18.14030 1.000 43.69438 ? 472 HOH   A O   1 
HETATM 1979 O  O   . HOH   C 3 .   ? 8.56860   -16.27090 -39.48214 1.000 35.67503 ? 473 HOH   A O   1 
HETATM 1980 O  O   . HOH   C 3 .   ? 9.69180   -17.38499 -7.69253  1.000 25.76693 ? 474 HOH   A O   1 
HETATM 1981 O  O   . HOH   C 3 .   ? 7.93102   -23.19206 -7.18671  1.000 40.40340 ? 475 HOH   A O   1 
HETATM 1982 O  O   . HOH   C 3 .   ? 6.69233   -26.61956 -27.57289 1.000 31.58080 ? 476 HOH   A O   1 
HETATM 1983 O  O   . HOH   C 3 .   ? -8.14710  -24.85133 -19.12187 1.000 17.87433 ? 477 HOH   A O   1 
HETATM 1984 O  O   . HOH   C 3 .   ? 0.336     -1.359    -19.812   1.000 37.07298 ? 478 HOH   A O   1 
HETATM 1985 O  O   . HOH   C 3 .   ? 4.16346   -24.16040 -30.68325 1.000 19.80401 ? 479 HOH   A O   1 
HETATM 1986 O  O   . HOH   C 3 .   ? 5.87630   -25.42183 -7.16309  1.000 46.98171 ? 480 HOH   A O   1 
HETATM 1987 O  O   . HOH   C 3 .   ? -14.22613 -11.67191 0.27308   1.000 45.87416 ? 481 HOH   A O   1 
HETATM 1988 O  O   . HOH   C 3 .   ? 12.96062  -13.91613 -29.67098 1.000 28.30948 ? 482 HOH   A O   1 
HETATM 1989 O  O   . HOH   C 3 .   ? -13.03251 -24.87529 -10.83035 1.000 35.04091 ? 483 HOH   A O   1 
HETATM 1990 O  O   . HOH   C 3 .   ? -6.46476  -7.73850  -34.31449 1.000 20.77372 ? 484 HOH   A O   1 
HETATM 1991 O  O   . HOH   C 3 .   ? 20.14921  -10.48297 -26.36977 1.000 42.03408 ? 485 HOH   A O   1 
HETATM 1992 O  O   . HOH   C 3 .   ? -10.31622 -11.53043 -2.17557  1.000 25.13745 ? 486 HOH   A O   1 
HETATM 1993 O  O   . HOH   C 3 .   ? 14.56473  -15.89436 -30.66579 1.000 37.23126 ? 487 HOH   A O   1 
HETATM 1994 O  O   . HOH   C 3 .   ? -3.37618  -3.32971  -40.65429 1.000 51.36206 ? 488 HOH   A O   1 
HETATM 1995 O  O   . HOH   C 3 .   ? 7.61086   1.38942   -14.92609 1.000 33.30353 ? 489 HOH   A O   1 
HETATM 1996 O  O   . HOH   C 3 .   ? -10.75963 -14.63209 0.93623   1.000 26.50165 ? 490 HOH   A O   1 
HETATM 1997 O  O   . HOH   C 3 .   ? -11.02983 -14.09587 -37.73910 1.000 34.79840 ? 491 HOH   A O   1 
HETATM 1998 O  O   . HOH   C 3 .   ? -14.15665 -12.78419 -7.77940  1.000 23.32808 ? 492 HOH   A O   1 
HETATM 1999 O  O   . HOH   C 3 .   ? -2.270    -24.742   -1.218    1.000 51.10622 ? 493 HOH   A O   1 
HETATM 2000 O  O   . HOH   C 3 .   ? -1.14944  -7.33303  -23.60425 1.000 27.70240 ? 494 HOH   A O   1 
HETATM 2001 O  O   . HOH   C 3 .   ? -1.22310  -26.01758 -32.20132 1.000 43.23050 ? 495 HOH   A O   1 
HETATM 2002 O  O   . HOH   C 3 .   ? 3.64851   -6.79844  -17.82045 1.000 24.06523 ? 496 HOH   A O   1 
HETATM 2003 O  O   . HOH   C 3 .   ? 19.78820  -16.61093 -27.50640 1.000 36.01456 ? 497 HOH   A O   1 
HETATM 2004 O  O   . HOH   C 3 .   ? -19.917   -27.555   -10.533   1.000 54.08602 ? 498 HOH   A O   1 
HETATM 2005 O  O   . HOH   C 3 .   ? -19.776   -19.531   -14.284   1.000 20.44580 ? 499 HOH   A O   1 
HETATM 2006 O  O   . HOH   C 3 .   ? 10.73982  -25.62352 -26.72170 1.000 33.89360 ? 500 HOH   A O   1 
HETATM 2007 O  O   . HOH   C 3 .   ? 15.38142  -20.23206 -18.63690 1.000 23.64520 ? 501 HOH   A O   1 
HETATM 2008 O  O   . HOH   C 3 .   ? -14.65375 -22.75938 -11.43176 1.000 32.36102 ? 502 HOH   A O   1 
HETATM 2009 O  O   . HOH   C 3 .   ? 8.85408   -15.47927 -27.78642 1.000 21.87344 ? 503 HOH   A O   1 
HETATM 2010 O  O   . HOH   C 3 .   ? -16.17625 -3.00132  -21.28348 1.000 30.61560 ? 504 HOH   A O   1 
HETATM 2011 O  O   . HOH   C 3 .   ? -0.03360  -30.70252 -23.94014 1.000 53.31696 ? 505 HOH   A O   1 
HETATM 2012 O  O   . HOH   C 3 .   ? 5.86425   -21.84295 -37.38112 1.000 33.06624 ? 506 HOH   A O   1 
HETATM 2013 O  O   . HOH   C 3 .   ? -6.28853  -5.05844  -35.55677 1.000 23.69759 ? 507 HOH   A O   1 
HETATM 2014 O  O   . HOH   C 3 .   ? -2.20085  -0.41769  -18.74037 1.000 46.23798 ? 508 HOH   A O   1 
HETATM 2015 O  O   . HOH   C 3 .   ? -5.14492  -14.19019 -22.60427 1.000 18.92554 ? 509 HOH   A O   1 
HETATM 2016 O  O   . HOH   C 3 .   ? -3.47505  -10.81491 -23.87450 1.000 30.48951 ? 510 HOH   A O   1 
HETATM 2017 O  O   . HOH   C 3 .   ? -13.72842 -16.93080 -2.71016  1.000 21.77633 ? 511 HOH   A O   1 
HETATM 2018 O  O   . HOH   C 3 .   ? -1.79257  -33.81410 -10.44139 1.000 55.60175 ? 512 HOH   A O   1 
HETATM 2019 O  O   . HOH   C 3 .   ? 4.69796   -30.63943 -11.59935 1.000 41.95045 ? 513 HOH   A O   1 
HETATM 2020 O  O   . HOH   C 3 .   ? 14.07227  -15.70702 -2.05748  1.000 36.27797 ? 514 HOH   A O   1 
HETATM 2021 O  O   . HOH   C 3 .   ? 10.59194  -25.40377 -23.71952 1.000 25.80229 ? 515 HOH   A O   1 
HETATM 2022 O  O   . HOH   C 3 .   ? 4.926     -9.547    -2.336    1.000 51.82092 ? 516 HOH   A O   1 
HETATM 2023 O  O   . HOH   C 3 .   ? -7.15333  -22.76692 -36.38334 1.000 52.71290 ? 517 HOH   A O   1 
HETATM 2024 O  O   . HOH   C 3 .   ? -15.16010 -11.09720 -29.81058 1.000 29.09009 ? 518 HOH   A O   1 
HETATM 2025 O  O   . HOH   C 3 .   ? -0.22318  -7.11212  -30.89301 1.000 33.56342 ? 519 HOH   A O   1 
HETATM 2026 O  O   . HOH   C 3 .   ? 10.51047  -21.43977 -6.93563  1.000 42.69297 ? 520 HOH   A O   1 
HETATM 2027 O  O   . HOH   C 3 .   ? -8.17638  -3.90434  -10.66196 1.000 28.95349 ? 521 HOH   A O   1 
HETATM 2028 O  O   . HOH   C 3 .   ? -6.10307  -14.00228 0.84190   1.000 29.83627 ? 522 HOH   A O   1 
HETATM 2029 O  O   . HOH   C 3 .   ? -2.43944  -10.54608 -26.43914 1.000 34.32515 ? 523 HOH   A O   1 
HETATM 2030 O  O   . HOH   C 3 .   ? -8.93406  -10.35159 -40.58285 1.000 45.48162 ? 524 HOH   A O   1 
HETATM 2031 O  O   . HOH   C 3 .   ? -3.379    -20.975   -0.554    1.000 36.75922 ? 525 HOH   A O   1 
HETATM 2032 O  O   . HOH   C 3 .   ? -14.38211 -21.87067 -33.45146 1.000 47.32581 ? 526 HOH   A O   1 
HETATM 2033 O  O   . HOH   C 3 .   ? -4.08423  -13.91260 -0.83024  1.000 40.08875 ? 527 HOH   A O   1 
HETATM 2034 O  O   . HOH   C 3 .   ? 8.42401   -20.54068 -9.30753  1.000 31.37109 ? 528 HOH   A O   1 
HETATM 2035 O  O   . HOH   C 3 .   ? 18.13182  -19.35390 -24.58210 1.000 32.89916 ? 529 HOH   A O   1 
HETATM 2036 O  O   . HOH   C 3 .   ? -6.22452  -11.40350 -10.08984 1.000 26.33706 ? 530 HOH   A O   1 
HETATM 2037 O  O   . HOH   C 3 .   ? -3.14940  -1.06056  -24.09516 1.000 28.99823 ? 531 HOH   A O   1 
HETATM 2038 O  O   . HOH   C 3 .   ? -11.88588 -7.59539  -38.26302 1.000 37.47712 ? 532 HOH   A O   1 
HETATM 2039 O  O   . HOH   C 3 .   ? -10.17501 -14.97594 -28.29456 1.000 28.10169 ? 533 HOH   A O   1 
HETATM 2040 O  O   . HOH   C 3 .   ? -9.927    -24.687   3.292     1.000 58.22199 ? 534 HOH   A O   1 
HETATM 2041 O  O   . HOH   C 3 .   ? -1.65799  -32.64841 -7.98211  1.000 45.84327 ? 535 HOH   A O   1 
HETATM 2042 O  O   . HOH   C 3 .   ? -4.65016  0.51528   -30.43329 1.000 31.77007 ? 536 HOH   A O   1 
HETATM 2043 O  O   . HOH   C 3 .   ? 0.93078   -9.52632  -40.64654 1.000 54.71415 ? 537 HOH   A O   1 
HETATM 2044 O  O   . HOH   C 3 .   ? -1.79954  -25.67018 -4.73909  1.000 25.26893 ? 538 HOH   A O   1 
HETATM 2045 O  O   . HOH   C 3 .   ? -5.81349  -31.19197 -11.45748 1.000 32.89789 ? 539 HOH   A O   1 
HETATM 2046 O  O   . HOH   C 3 .   ? -1.25951  -4.50217  -33.76880 1.000 40.11849 ? 540 HOH   A O   1 
HETATM 2047 O  O   . HOH   C 3 .   ? -18.09569 -3.73055  -28.99775 1.000 47.52482 ? 541 HOH   A O   1 
HETATM 2048 O  O   . HOH   C 3 .   ? 3.75825   -11.84960 -38.58301 1.000 27.33774 ? 542 HOH   A O   1 
HETATM 2049 O  O   . HOH   C 3 .   ? -19.93548 -12.92253 -16.40915 1.000 48.01900 ? 543 HOH   A O   1 
HETATM 2050 O  O   . HOH   C 3 .   ? -7.80924  -13.59598 -40.90428 1.000 53.55532 ? 544 HOH   A O   1 
HETATM 2051 O  O   . HOH   C 3 .   ? 5.27662   -29.36714 -8.39949  1.000 47.28283 ? 545 HOH   A O   1 
HETATM 2052 O  O   . HOH   C 3 .   ? -17.69790 -15.24034 -13.13086 1.000 23.74671 ? 546 HOH   A O   1 
HETATM 2053 O  O   . HOH   C 3 .   ? -14.75121 -7.12601  -14.23104 1.000 36.26629 ? 547 HOH   A O   1 
HETATM 2054 O  O   . HOH   C 3 .   ? 2.03251   -5.95559  -26.13758 1.000 40.81676 ? 548 HOH   A O   1 
HETATM 2055 O  O   . HOH   C 3 .   ? -3.19528  -31.74545 -20.07019 1.000 50.28534 ? 549 HOH   A O   1 
HETATM 2056 O  O   . HOH   C 3 .   ? -5.79675  -18.89808 -39.07827 1.000 37.67574 ? 550 HOH   A O   1 
HETATM 2057 O  O   . HOH   C 3 .   ? -8.83485  -18.10018 -36.71847 1.000 42.15746 ? 551 HOH   A O   1 
HETATM 2058 O  O   . HOH   C 3 .   ? 4.04186   -9.26496  -20.38680 1.000 20.78624 ? 552 HOH   A O   1 
HETATM 2059 O  O   . HOH   C 3 .   ? -13.53281 -26.48441 -18.13216 1.000 25.45781 ? 553 HOH   A O   1 
HETATM 2060 O  O   . HOH   C 3 .   ? 14.17807  0.68266   -13.75190 1.000 31.97663 ? 554 HOH   A O   1 
HETATM 2061 O  O   . HOH   C 3 .   ? -18.61148 -12.48528 -13.71043 1.000 54.44062 ? 555 HOH   A O   1 
HETATM 2062 O  O   . HOH   C 3 .   ? -17.26949 -28.63537 -17.35199 1.000 43.33666 ? 556 HOH   A O   1 
HETATM 2063 O  O   . HOH   C 3 .   ? 20.84725  -14.21553 -26.72263 1.000 32.71703 ? 557 HOH   A O   1 
HETATM 2064 O  O   . HOH   C 3 .   ? 8.80683   -20.47503 -4.29661  1.000 28.04423 ? 558 HOH   A O   1 
HETATM 2065 O  O   . HOH   C 3 .   ? -17.78852 -18.72251 -11.26255 1.000 37.76972 ? 559 HOH   A O   1 
HETATM 2066 O  O   . HOH   C 3 .   ? -0.03607  -28.59270 -25.57309 1.000 55.49682 ? 560 HOH   A O   1 
HETATM 2067 O  O   . HOH   C 3 .   ? 3.19411   -4.92549  -28.87419 1.000 46.88245 ? 561 HOH   A O   1 
HETATM 2068 O  O   . HOH   C 3 .   ? -6.27216  -24.37859 -30.38500 1.000 48.29706 ? 562 HOH   A O   1 
HETATM 2069 O  O   . HOH   C 3 .   ? -0.34479  -12.35201 -21.42484 1.000 31.58172 ? 563 HOH   A O   1 
HETATM 2070 O  O   . HOH   C 3 .   ? -3.42442  -13.09481 -20.71177 1.000 23.64927 ? 564 HOH   A O   1 
HETATM 2071 O  O   . HOH   C 3 .   ? 15.72700  -18.37903 -3.58432  1.000 35.43155 ? 565 HOH   A O   1 
HETATM 2072 O  O   . HOH   C 3 .   ? -7.33130  1.31998   -19.28113 1.000 37.16670 ? 566 HOH   A O   1 
HETATM 2073 O  O   . HOH   C 3 .   ? -16.43145 -9.03010  -14.24548 1.000 36.72672 ? 567 HOH   A O   1 
HETATM 2074 O  O   . HOH   C 3 .   ? -10.19728 -0.43112  -19.77905 1.000 39.75730 ? 568 HOH   A O   1 
HETATM 2075 O  O   . HOH   C 3 .   ? 20.13702  -5.21680  -14.93289 1.000 47.28275 ? 569 HOH   A O   1 
HETATM 2076 O  O   . HOH   C 3 .   ? 4.37174   -19.43439 -40.64418 1.000 36.50481 ? 570 HOH   A O   1 
HETATM 2077 O  O   . HOH   C 3 .   ? 1.36142   -3.11638  -24.22729 1.000 41.92692 ? 571 HOH   A O   1 
HETATM 2078 O  O   . HOH   C 3 .   ? -5.13940  -31.70852 -7.04660  1.000 45.16093 ? 572 HOH   A O   1 
HETATM 2079 O  O   . HOH   C 3 .   ? 6.41310   -23.22213 -40.79143 1.000 63.16896 ? 573 HOH   A O   1 
HETATM 2080 O  O   . HOH   C 3 .   ? -1.13239  -29.91102 -17.12586 1.000 43.81128 ? 574 HOH   A O   1 
HETATM 2081 O  O   . HOH   C 3 .   ? -4.09237  -3.34133  -15.45534 1.000 44.48615 ? 575 HOH   A O   1 
HETATM 2082 O  O   . HOH   C 3 .   ? 12.36585  -27.55907 -19.55496 1.000 44.36511 ? 576 HOH   A O   1 
HETATM 2083 O  O   . HOH   C 3 .   ? 13.68901  -20.43202 -20.69872 1.000 21.95333 ? 577 HOH   A O   1 
HETATM 2084 O  O   . HOH   C 3 .   ? -14.04546 -23.94400 -4.90215  1.000 31.78910 ? 578 HOH   A O   1 
HETATM 2085 O  O   . HOH   C 3 .   ? -13.53769 -25.79297 -7.80168  1.000 28.50253 ? 579 HOH   A O   1 
HETATM 2086 O  O   . HOH   C 3 .   ? -12.30217 -26.89369 -20.22425 1.000 29.67286 ? 580 HOH   A O   1 
HETATM 2087 O  O   . HOH   C 3 .   ? 17.07145  -24.87021 -25.31105 1.000 39.37968 ? 581 HOH   A O   1 
HETATM 2088 O  O   . HOH   C 3 .   ? 0.48575   -5.51489  -21.98898 1.000 41.96558 ? 582 HOH   A O   1 
HETATM 2089 O  O   . HOH   C 3 .   ? 8.38841   -19.85280 -41.34952 1.000 53.30896 ? 583 HOH   A O   1 
HETATM 2090 O  O   . HOH   C 3 .   ? 13.32674  -6.78863  -26.26267 1.000 25.00486 ? 584 HOH   A O   1 
HETATM 2091 O  O   . HOH   C 3 .   ? -2.36213  -15.63550 -0.23201  1.000 43.28472 ? 585 HOH   A O   1 
HETATM 2092 O  O   . HOH   C 3 .   ? 7.038     -4.557    -22.510   1.000 50.76998 ? 586 HOH   A O   1 
HETATM 2093 O  O   . HOH   C 3 .   ? 3.81780   -23.21957 -3.38607  1.000 37.68256 ? 587 HOH   A O   1 
HETATM 2094 O  O   . HOH   C 3 .   ? 0.00604   -16.61880 -3.42506  1.000 27.42386 ? 588 HOH   A O   1 
HETATM 2095 O  O   . HOH   C 3 .   ? -13.04871 -12.20072 -31.00860 1.000 25.72426 ? 589 HOH   A O   1 
HETATM 2096 O  O   . HOH   C 3 .   ? -15.964   -3.885    -15.109   1.000 52.14472 ? 590 HOH   A O   1 
HETATM 2097 O  O   . HOH   C 3 .   ? 1.48506   -4.08049  -16.73036 1.000 48.90254 ? 591 HOH   A O   1 
HETATM 2098 O  O   . HOH   C 3 .   ? -15.16049 -11.98480 -11.92717 1.000 35.03607 ? 592 HOH   A O   1 
HETATM 2099 O  O   . HOH   C 3 .   ? -1.24525  -27.52432 -34.58099 1.000 53.28246 ? 593 HOH   A O   1 
HETATM 2100 O  O   . HOH   C 3 .   ? 6.82455   -29.92253 -30.42209 1.000 48.75370 ? 594 HOH   A O   1 
HETATM 2101 O  O   . HOH   C 3 .   ? -17.76366 -33.92310 -10.79628 1.000 59.56382 ? 595 HOH   A O   1 
HETATM 2102 O  O   . HOH   C 3 .   ? -14.08727 -16.16057 -26.13282 1.000 33.15275 ? 596 HOH   A O   1 
HETATM 2103 O  O   . HOH   C 3 .   ? 11.550    -1.611    -20.285   1.000 43.65640 ? 597 HOH   A O   1 
HETATM 2104 O  O   . HOH   C 3 .   ? -16.22213 -25.40470 -10.83172 1.000 35.93152 ? 598 HOH   A O   1 
HETATM 2105 O  O   . HOH   C 3 .   ? -13.75903 -18.60444 -24.45970 1.000 22.15733 ? 599 HOH   A O   1 
HETATM 2106 O  O   . HOH   C 3 .   ? -7.60502  7.51594   -33.66948 1.000 38.62425 ? 600 HOH   A O   1 
HETATM 2107 O  O   . HOH   C 3 .   ? 15.46184  -7.21551  -27.80691 1.000 35.87070 ? 601 HOH   A O   1 
HETATM 2108 O  O   . HOH   C 3 .   ? -17.99438 -5.61804  -25.48556 1.000 38.38512 ? 602 HOH   A O   1 
HETATM 2109 O  O   . HOH   C 3 .   ? 17.43897  -15.35200 -29.89558 1.000 45.47292 ? 603 HOH   A O   1 
HETATM 2110 O  O   . HOH   C 3 .   ? 13.76064  -4.07071  -25.46738 1.000 17.93174 ? 604 HOH   A O   1 
HETATM 2111 O  O   . HOH   C 3 .   ? -3.05489  -8.24244  1.96903   1.000 48.22632 ? 605 HOH   A O   1 
HETATM 2112 O  O   . HOH   C 3 .   ? 1.13554   -8.71841  -27.12032 1.000 38.95199 ? 606 HOH   A O   1 
HETATM 2113 O  O   . HOH   C 3 .   ? 8.33661   -25.71212 -25.84002 1.000 43.21947 ? 607 HOH   A O   1 
HETATM 2114 O  O   . HOH   C 3 .   ? 3.68759   -30.31930 -19.51012 1.000 46.85934 ? 608 HOH   A O   1 
HETATM 2115 O  O   . HOH   C 3 .   ? -4.93865  -5.22040  -12.08393 1.000 42.33172 ? 609 HOH   A O   1 
HETATM 2116 O  O   . HOH   C 3 .   ? -1.49854  -8.45977  -27.70034 1.000 32.72209 ? 610 HOH   A O   1 
HETATM 2117 O  O   . HOH   C 3 .   ? 0.86782   -5.85271  -34.38787 1.000 45.99079 ? 611 HOH   A O   1 
HETATM 2118 O  O   . HOH   C 3 .   ? 6.73550   -27.89796 -8.19136  1.000 49.74812 ? 612 HOH   A O   1 
HETATM 2119 O  O   . HOH   C 3 .   ? 20.48901  -6.01449  -21.01401 1.000 40.31874 ? 613 HOH   A O   1 
HETATM 2120 O  O   . HOH   C 3 .   ? -3.88278  -32.93324 -10.91242 1.000 51.39348 ? 614 HOH   A O   1 
HETATM 2121 O  O   . HOH   C 3 .   ? 1.839     -18.343   0.203     1.000 39.54353 ? 615 HOH   A O   1 
HETATM 2122 O  O   . HOH   C 3 .   ? 3.03162   -6.26930  -20.50767 1.000 41.84174 ? 616 HOH   A O   1 
HETATM 2123 O  O   . HOH   C 3 .   ? 10.58053  -17.53918 -38.83464 1.000 52.31250 ? 617 HOH   A O   1 
HETATM 2124 O  O   . HOH   C 3 .   ? -0.95760  -5.80955  -12.54535 1.000 48.56548 ? 618 HOH   A O   1 
HETATM 2125 O  O   . HOH   C 3 .   ? 2.11493   -25.95187 -29.28832 1.000 41.01272 ? 619 HOH   A O   1 
HETATM 2126 O  O   . HOH   C 3 .   ? -5.67504  -12.38081 -41.99169 1.000 49.05852 ? 620 HOH   A O   1 
HETATM 2127 O  O   . HOH   C 3 .   ? -5.44622  -11.26012 1.28449   1.000 47.38251 ? 621 HOH   A O   1 
HETATM 2128 O  O   . HOH   C 3 .   ? 4.56017   -1.94747  -18.29380 1.000 40.17581 ? 622 HOH   A O   1 
HETATM 2129 O  O   . HOH   C 3 .   ? 2.71303   -10.07265 -23.08064 1.000 30.63260 ? 623 HOH   A O   1 
HETATM 2130 O  O   . HOH   C 3 .   ? 4.49785   -21.97356 -39.28593 1.000 53.25119 ? 624 HOH   A O   1 
HETATM 2131 O  O   . HOH   C 3 .   ? -17.383   -4.677    -17.592   1.000 41.98525 ? 625 HOH   A O   1 
HETATM 2132 O  O   . HOH   C 3 .   ? 0.74345   -4.78361  -30.01617 1.000 56.77341 ? 626 HOH   A O   1 
HETATM 2133 O  O   . HOH   C 3 .   ? 5.552     1.614     -16.682   1.000 39.43982 ? 627 HOH   A O   1 
HETATM 2134 O  O   . HOH   C 3 .   ? -10.49298 -6.65426  -40.03740 1.000 55.55410 ? 628 HOH   A O   1 
HETATM 2135 O  O   . HOH   C 3 .   ? -11.95471 -20.55798 -25.39786 1.000 53.15949 ? 629 HOH   A O   1 
HETATM 2136 O  O   . HOH   C 3 .   ? 1.54757   -7.57260  -22.75892 1.000 47.26102 ? 630 HOH   A O   1 
HETATM 2137 O  O   . HOH   C 3 .   ? -7.409    -1.980    -12.936   1.000 44.33423 ? 631 HOH   A O   1 
HETATM 2138 O  O   . HOH   C 3 .   ? 0.04393   -19.27666 -2.13463  1.000 42.76125 ? 632 HOH   A O   1 
HETATM 2139 O  O   . HOH   C 3 .   ? -0.39766  -1.30191  -22.92699 1.000 51.74803 ? 633 HOH   A O   1 
HETATM 2140 O  O   . HOH   C 3 .   ? 14.85916  -8.03710  -30.07221 1.000 41.88452 ? 634 HOH   A O   1 
HETATM 2141 O  O   . HOH   C 3 .   ? -12.29771 -16.34623 -28.19753 1.000 35.90282 ? 635 HOH   A O   1 
HETATM 2142 O  O   . HOH   C 3 .   ? 5.599     -2.759    -26.003   1.000 44.94121 ? 636 HOH   A O   1 
HETATM 2143 O  O   . HOH   C 3 .   ? 12.19906  -25.28653 -38.44078 1.000 34.55818 ? 637 HOH   A O   1 
HETATM 2144 O  O   . HOH   C 3 .   ? 17.70163  -21.45218 -19.79936 1.000 37.17335 ? 638 HOH   A O   1 
HETATM 2145 O  O   . HOH   C 3 .   ? -14.06517 -14.31084 -3.00928  1.000 37.87091 ? 639 HOH   A O   1 
HETATM 2146 O  O   . HOH   C 3 .   ? 14.50412  -22.01831 -16.92192 1.000 39.72156 ? 640 HOH   A O   1 
HETATM 2147 O  O   . HOH   C 3 .   ? -9.86645  -26.02779 -20.84434 1.000 34.01991 ? 641 HOH   A O   1 
HETATM 2148 O  O   . HOH   C 3 .   ? -6.24241  3.72682   -34.62385 1.000 40.78709 ? 642 HOH   A O   1 
HETATM 2149 O  O   . HOH   C 3 .   ? 2.62938   -4.60351  -30.99532 1.000 54.28940 ? 643 HOH   A O   1 
HETATM 2150 O  O   . HOH   C 3 .   ? -6.33889  6.71632   -36.11603 1.000 48.40139 ? 644 HOH   A O   1 
HETATM 2151 O  O   . HOH   C 3 .   ? -14.39693 -9.81951  -8.20871  1.000 41.78496 ? 645 HOH   A O   1 
HETATM 2152 O  O   . HOH   C 3 .   ? 7.75800   -29.20842 -28.74521 1.000 46.04096 ? 646 HOH   A O   1 
HETATM 2153 O  O   . HOH   C 3 .   ? 3.65675   -9.09428  -38.99593 1.000 43.74570 ? 647 HOH   A O   1 
HETATM 2154 O  O   . HOH   C 3 .   ? -15.91959 -20.33730 -32.54847 1.000 52.14007 ? 648 HOH   A O   1 
HETATM 2155 O  O   . HOH   C 3 .   ? -18.59280 -11.71716 -21.13451 1.000 31.85498 ? 649 HOH   A O   1 
HETATM 2156 O  O   . HOH   C 3 .   ? 3.53080   -0.00605  -16.39449 1.000 44.46249 ? 650 HOH   A O   1 
HETATM 2157 O  O   . HOH   C 3 .   ? -3.46003  -27.27971 -3.16761  1.000 49.78089 ? 651 HOH   A O   1 
HETATM 2158 O  O   . HOH   C 3 .   ? -8.83558  -5.65536  -40.01580 1.000 47.10054 ? 652 HOH   A O   1 
HETATM 2159 O  O   . HOH   C 3 .   ? 2.227     -0.889    -25.835   1.000 39.60900 ? 653 HOH   A O   1 
HETATM 2160 O  O   . HOH   C 3 .   ? 19.17703  -8.43474  -17.81965 1.000 38.73573 ? 654 HOH   A O   1 
HETATM 2161 O  O   . HOH   C 3 .   ? -2.058    -23.219   0.575     1.000 56.04934 ? 655 HOH   A O   1 
HETATM 2162 O  O   . HOH   C 3 .   ? 7.84338   -14.06589 -38.25839 1.000 36.81441 ? 656 HOH   A O   1 
HETATM 2163 O  O   . HOH   C 3 .   ? -2.27788  -0.85672  -30.94794 1.000 49.89653 ? 657 HOH   A O   1 
HETATM 2164 O  O   . HOH   C 3 .   ? -10.124   -29.086   -30.895   1.000 46.67544 ? 658 HOH   A O   1 
HETATM 2165 O  O   . HOH   C 3 .   ? 6.22926   -29.92992 -24.62802 1.000 53.45227 ? 659 HOH   A O   1 
HETATM 2166 O  O   . HOH   C 3 .   ? 13.91377  -11.52642 -5.02281  1.000 49.23832 ? 660 HOH   A O   1 
HETATM 2167 O  O   . HOH   C 3 .   ? -10.38838 -8.66564  -1.39769  1.000 43.25697 ? 661 HOH   A O   1 
HETATM 2168 O  O   . HOH   C 3 .   ? 5.86413   -12.88006 -39.83247 1.000 32.48031 ? 662 HOH   A O   1 
HETATM 2169 O  O   . HOH   C 3 .   ? -10.59829 -16.69677 -37.93715 1.000 45.82999 ? 663 HOH   A O   1 
HETATM 2170 O  O   . HOH   C 3 .   ? -7.86325  -21.49582 -37.53969 1.000 44.76979 ? 664 HOH   A O   1 
HETATM 2171 O  O   . HOH   C 3 .   ? -10.80512 -22.60794 -24.55110 1.000 48.04572 ? 665 HOH   A O   1 
HETATM 2172 O  O   . HOH   C 3 .   ? 6.70743   -21.58694 -2.73147  1.000 38.73545 ? 666 HOH   A O   1 
HETATM 2173 O  O   . HOH   C 3 .   ? -6.661    -23.262   -1.532    1.000 41.29052 ? 667 HOH   A O   1 
HETATM 2174 O  O   . HOH   C 3 .   ? -6.98869  -30.74583 -9.18479  1.000 34.82126 ? 668 HOH   A O   1 
HETATM 2175 O  O   . HOH   C 3 .   ? -4.754    -25.110   -1.079    1.000 51.12650 ? 669 HOH   A O   1 
HETATM 2176 O  O   . HOH   C 3 .   ? 5.73100   -23.64410 -42.57087 1.000 63.05486 ? 670 HOH   A O   1 
HETATM 2177 O  O   . HOH   C 3 .   ? 9.99531   -29.36611 -23.98882 1.000 46.60312 ? 671 HOH   A O   1 
HETATM 2178 O  O   . HOH   C 3 .   ? 4.78753   -14.88379 -41.49257 1.000 42.40361 ? 672 HOH   A O   1 
HETATM 2179 O  O   . HOH   C 3 .   ? -0.63220  -26.59732 -30.21533 1.000 49.85143 ? 673 HOH   A O   1 
HETATM 2180 O  O   . HOH   C 3 .   ? 5.408     -3.238    -23.506   1.000 51.70964 ? 674 HOH   A O   1 
HETATM 2181 O  O   . HOH   C 3 .   ? -13.88367 -13.76674 -38.19207 1.000 47.46880 ? 675 HOH   A O   1 
HETATM 2182 O  O   . HOH   C 3 .   ? -10.572   -22.728   4.543     1.000 44.56240 ? 676 HOH   A O   1 
HETATM 2183 O  O   . HOH   C 3 .   ? -0.00000  -0.00000  -18.26711 0.50  28.07422 ? 677 HOH   A O   1 
HETATM 2184 O  O   . HOH   C 3 .   ? 16.21306  -3.18261  -26.37440 1.000 40.56258 ? 678 HOH   A O   1 
HETATM 2185 O  O   . HOH   C 3 .   ? 10.92547  -28.14247 -27.89185 1.000 38.42107 ? 679 HOH   A O   1 
HETATM 2186 O  O   . HOH   C 3 .   ? 11.395    -30.174   -34.257   1.000 44.89311 ? 680 HOH   A O   1 
HETATM 2187 O  O   . HOH   C 3 .   ? 1.83757   -5.82633  -36.65331 1.000 50.64861 ? 681 HOH   A O   1 
HETATM 2188 O  O   . HOH   C 3 .   ? 3.05745   -2.17493  -20.38664 1.000 49.23126 ? 682 HOH   A O   1 
HETATM 2189 O  O   . HOH   C 3 .   ? 2.22669   -0.51036  -14.35731 1.000 46.94686 ? 683 HOH   A O   1 
HETATM 2190 O  O   . HOH   C 3 .   ? -16.30747 -12.59241 -6.21797  1.000 43.51827 ? 684 HOH   A O   1 
HETATM 2191 O  O   . HOH   C 3 .   ? 4.052     -2.027    -28.220   1.000 36.76359 ? 685 HOH   A O   1 
HETATM 2192 O  O   . HOH   C 3 .   ? 19.27406  -20.52030 -22.37261 1.000 40.69932 ? 686 HOH   A O   1 
HETATM 2193 O  O   . HOH   C 3 .   ? 18.43626  -18.41230 -7.08240  1.000 58.88728 ? 687 HOH   A O   1 
HETATM 2194 O  O   . HOH   C 3 .   ? 0.55338   -1.28013  -16.68836 1.000 37.37623 ? 688 HOH   A O   1 
HETATM 2195 O  O   . HOH   C 3 .   ? 14.60834  -13.21603 -2.87398  1.000 47.86101 ? 689 HOH   A O   1 
HETATM 2196 O  O   . HOH   C 3 .   ? 9.68931   -25.11629 -14.65257 1.000 40.60302 ? 690 HOH   A O   1 
HETATM 2197 O  O   . HOH   C 3 .   ? 9.54723   -12.61364 -37.12300 1.000 48.94277 ? 691 HOH   A O   1 
HETATM 2198 O  O   . HOH   C 3 .   ? -14.85371 -9.63062  -11.31999 1.000 37.74740 ? 692 HOH   A O   1 
HETATM 2199 O  O   . HOH   C 3 .   ? -0.90599  -2.54115  -31.34050 1.000 50.42288 ? 693 HOH   A O   1 
HETATM 2200 O  O   . HOH   C 3 .   ? 8.797     -10.711   -0.161    1.000 52.78637 ? 694 HOH   A O   1 
HETATM 2201 O  O   . HOH   C 3 .   ? -16.92579 -15.65408 -10.29653 1.000 39.56271 ? 695 HOH   A O   1 
HETATM 2202 O  O   . HOH   C 3 .   ? -16.09795 -13.65340 -3.74775  1.000 46.48625 ? 696 HOH   A O   1 
HETATM 2203 O  O   . HOH   C 3 .   ? -14.59376 -13.96709 -10.21093 1.000 35.68179 ? 697 HOH   A O   1 
HETATM 2204 O  O   . HOH   C 3 .   ? -19.51862 -5.93684  -21.64088 1.000 44.77564 ? 698 HOH   A O   1 
HETATM 2205 O  O   . HOH   C 3 .   ? 20.563    -20.690   -26.493   1.000 48.51485 ? 699 HOH   A O   1 
HETATM 2206 O  O   . HOH   C 3 .   ? 10.338    -11.568   -1.911    1.000 51.35248 ? 700 HOH   A O   1 
HETATM 2207 O  O   . HOH   C 3 .   ? -2.44228  -26.55753 -27.97841 1.000 51.33154 ? 701 HOH   A O   1 
HETATM 2208 O  O   . HOH   C 3 .   ? -15.42188 -7.48389  -6.94316  1.000 52.45148 ? 702 HOH   A O   1 
HETATM 2209 O  O   . HOH   C 3 .   ? -9.11205  -32.72836 -8.64591  1.000 49.25222 ? 703 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   ? 0.62203 0.78736 0.48443 -0.12695 -0.00022 -0.26192 16  GLU A N   
2    C CA  . GLU A 9   ? 0.79801 0.92773 0.64797 -0.09282 -0.00398 -0.24283 16  GLU A CA  
3    C C   . GLU A 9   ? 0.77674 0.90671 0.64898 -0.07505 -0.01056 -0.22275 16  GLU A C   
4    O O   . GLU A 9   ? 0.61889 0.81081 0.51430 -0.06609 -0.02402 -0.21532 16  GLU A O   
5    C CB  . GLU A 9   ? 0.76625 0.94743 0.60905 -0.07030 -0.01721 -0.23969 16  GLU A CB  
6    C CG  . GLU A 9   ? 0.95684 1.09233 0.77481 -0.04200 -0.01312 -0.22769 16  GLU A CG  
7    C CD  . GLU A 9   ? 1.06369 1.18205 0.89302 -0.01086 -0.01554 -0.20339 16  GLU A CD  
8    O OE1 . GLU A 9   ? 0.99627 1.12626 0.84902 -0.01128 -0.02034 -0.19565 16  GLU A OE1 
9    O OE2 . GLU A 9   ? 0.88450 0.97758 0.69936 0.01510  -0.01128 -0.19193 16  GLU A OE2 
10   N N   . VAL A 10  ? 0.48088 0.54220 0.34546 -0.06790 0.00101  -0.21331 17  VAL A N   
11   C CA  . VAL A 10  ? 0.42063 0.47413 0.30460 -0.05497 -0.00237 -0.19727 17  VAL A CA  
12   C C   . VAL A 10  ? 0.44198 0.46927 0.31990 -0.02290 -0.00179 -0.18200 17  VAL A C   
13   O O   . VAL A 10  ? 0.47867 0.45300 0.33725 -0.01737 0.01292  -0.17969 17  VAL A O   
14   C CB  . VAL A 10  ? 0.50789 0.51006 0.39436 -0.07473 0.01391  -0.19862 17  VAL A CB  
15   C CG1 . VAL A 10  ? 0.50984 0.51897 0.41903 -0.06467 0.00729  -0.18465 17  VAL A CG1 
16   C CG2 . VAL A 10  ? 0.70813 0.72871 0.59720 -0.10788 0.02014  -0.21672 17  VAL A CG2 
17   N N   . GLU A 11  ? 0.34192 0.40046 0.24107 0.00090  -0.01492 -0.16036 18  GLU A N   
18   C CA  . GLU A 11  ? 0.35689 0.39051 0.26162 0.03047  -0.01333 -0.13259 18  GLU A CA  
19   C C   . GLU A 11  ? 0.33476 0.34063 0.25884 0.03118  -0.01011 -0.11565 18  GLU A C   
20   O O   . GLU A 11  ? 0.28091 0.30859 0.22062 0.02317  -0.01669 -0.11603 18  GLU A O   
21   C CB  . GLU A 11  ? 0.30018 0.37987 0.20996 0.05578  -0.02426 -0.12002 18  GLU A CB  
22   C CG  . GLU A 11  ? 0.32334 0.43173 0.21099 0.06379  -0.02672 -0.13134 18  GLU A CG  
23   C CD  . GLU A 11  ? 0.46858 0.61717 0.35689 0.09577  -0.03245 -0.11398 18  GLU A CD  
24   O OE1 . GLU A 11  ? 0.45497 0.65224 0.35242 0.10071  -0.04052 -0.11218 18  GLU A OE1 
25   O OE2 . GLU A 11  ? 0.54646 0.67735 0.42415 0.11790  -0.02614 -0.10096 18  GLU A OE2 
26   N N   . THR A 12  ? 0.30249 0.26592 0.22476 0.04182  0.00020  -0.10063 19  THR A N   
27   C CA  . THR A 12  ? 0.28466 0.22990 0.22309 0.04446  0.00307  -0.08432 19  THR A CA  
28   C C   . THR A 12  ? 0.28821 0.24222 0.24008 0.06468  -0.00056 -0.06334 19  THR A C   
29   O O   . THR A 12  ? 0.27813 0.22407 0.22264 0.07853  0.00427  -0.05641 19  THR A O   
30   C CB  . THR A 12  ? 0.34251 0.23987 0.26759 0.04158  0.02071  -0.08241 19  THR A CB  
31   O OG1 . THR A 12  ? 0.36030 0.24031 0.26843 0.01840  0.02993  -0.10513 19  THR A OG1 
32   C CG2 . THR A 12  ? 0.34305 0.23367 0.28375 0.04634  0.02245  -0.06539 19  THR A CG2 
33   N N   . PHE A 13  ? 0.24924 0.21798 0.21925 0.06413  -0.00680 -0.05482 20  PHE A N   
34   C CA  . PHE A 13  ? 0.26421 0.24100 0.24628 0.07564  -0.00751 -0.03965 20  PHE A CA  
35   C C   . PHE A 13  ? 0.30555 0.27786 0.30153 0.07112  -0.00629 -0.03005 20  PHE A C   
36   O O   . PHE A 13  ? 0.26489 0.23446 0.26364 0.06123  -0.00804 -0.03373 20  PHE A O   
37   C CB  . PHE A 13  ? 0.23756 0.23679 0.22330 0.07894  -0.01272 -0.03971 20  PHE A CB  
38   C CG  . PHE A 13  ? 0.23945 0.25765 0.21140 0.08860  -0.01483 -0.04632 20  PHE A CG  
39   C CD1 . PHE A 13  ? 0.29104 0.33185 0.25729 0.07896  -0.02163 -0.06186 20  PHE A CD1 
40   C CD2 . PHE A 13  ? 0.28291 0.30178 0.24729 0.10714  -0.00899 -0.03719 20  PHE A CD2 
41   C CE1 . PHE A 13  ? 0.27227 0.34477 0.22557 0.08829  -0.02523 -0.06885 20  PHE A CE1 
42   C CE2 . PHE A 13  ? 0.30853 0.35154 0.25762 0.12043  -0.01086 -0.04145 20  PHE A CE2 
43   C CZ  . PHE A 13  ? 0.29032 0.36463 0.23398 0.11137  -0.02033 -0.05754 20  PHE A CZ  
44   N N   . ALA A 14  ? 0.24524 0.22202 0.25004 0.07764  -0.00279 -0.01832 21  ALA A N   
45   C CA  . ALA A 14  ? 0.19296 0.18118 0.21211 0.07186  -0.00367 -0.01098 21  ALA A CA  
46   C C   . ALA A 14  ? 0.22065 0.21814 0.24697 0.06292  -0.00665 -0.01369 21  ALA A C   
47   O O   . ALA A 14  ? 0.21990 0.21480 0.24290 0.06673  -0.00232 -0.01365 21  ALA A O   
48   C CB  . ALA A 14  ? 0.21434 0.21405 0.24122 0.07914  0.00218  0.00052  21  ALA A CB  
49   N N   . PHE A 15  ? 0.21768 0.22166 0.25006 0.05311  -0.01088 -0.01503 22  PHE A N   
50   C CA  . PHE A 15  ? 0.21618 0.22460 0.25254 0.04359  -0.00994 -0.01722 22  PHE A CA  
51   C C   . PHE A 15  ? 0.23052 0.24847 0.27413 0.03811  -0.00289 -0.01406 22  PHE A C   
52   O O   . PHE A 15  ? 0.22173 0.25797 0.27382 0.03922  -0.00326 -0.00863 22  PHE A O   
53   C CB  . PHE A 15  ? 0.19062 0.20623 0.23089 0.03382  -0.01524 -0.01921 22  PHE A CB  
54   C CG  . PHE A 15  ? 0.19883 0.20611 0.23380 0.03411  -0.01938 -0.02404 22  PHE A CG  
55   C CD1 . PHE A 15  ? 0.23153 0.23546 0.26132 0.03535  -0.01846 -0.02793 22  PHE A CD1 
56   C CD2 . PHE A 15  ? 0.22898 0.23327 0.26323 0.03393  -0.02119 -0.02366 22  PHE A CD2 
57   C CE1 . PHE A 15  ? 0.27020 0.27774 0.29841 0.03399  -0.02251 -0.03286 22  PHE A CE1 
58   C CE2 . PHE A 15  ? 0.26255 0.26094 0.29351 0.02949  -0.02265 -0.03027 22  PHE A CE2 
59   C CZ  . PHE A 15  ? 0.23295 0.23798 0.26310 0.02819  -0.02495 -0.03562 22  PHE A CZ  
60   N N   . GLN A 16  ? 0.21874 0.22489 0.25779 0.03214  0.00652  -0.01720 23  GLN A N   
61   C CA  . GLN A 16  ? 0.24240 0.25693 0.28821 0.01697  0.01619  -0.01928 23  GLN A CA  
62   C C   . GLN A 16  ? 0.22613 0.27169 0.28302 0.00158  0.00793  -0.02282 23  GLN A C   
63   O O   . GLN A 16  ? 0.24028 0.28657 0.29440 0.00025  -0.00009 -0.02488 23  GLN A O   
64   C CB  . GLN A 16  ? 0.27073 0.25579 0.30345 0.01033  0.03342  -0.02376 23  GLN A CB  
65   C CG  . GLN A 16  ? 0.34669 0.30627 0.36589 0.02996  0.04531  -0.01709 23  GLN A CG  
66   C CD  . GLN A 16  ? 0.52083 0.44480 0.52117 0.02948  0.06771  -0.01773 23  GLN A CD  
67   O OE1 . GLN A 16  ? 0.46516 0.37741 0.45262 0.04228  0.06846  -0.01500 23  GLN A OE1 
68   N NE2 . GLN A 16  ? 0.51095 0.41680 0.50801 0.01512  0.08927  -0.02090 23  GLN A NE2 
69   N N   A ALA A 17  ? 0.23132 0.30885 0.30099 -0.00903 0.01020  -0.02295 24  ALA A N   
70   N N   B ALA A 17  ? 0.23213 0.30919 0.30163 -0.00969 0.01056  -0.02331 24  ALA A N   
71   C CA  A ALA A 17  ? 0.23145 0.35415 0.31178 -0.01984 0.00109  -0.02466 24  ALA A CA  
72   C CA  B ALA A 17  ? 0.23300 0.35551 0.31328 -0.02080 0.00150  -0.02517 24  ALA A CA  
73   C C   A ALA A 17  ? 0.20783 0.32403 0.28032 -0.03814 0.00098  -0.03648 24  ALA A C   
74   C C   B ALA A 17  ? 0.20952 0.32538 0.28173 -0.03792 0.00067  -0.03645 24  ALA A C   
75   O O   A ALA A 17  ? 0.21546 0.35302 0.28862 -0.03682 -0.00972 -0.03536 24  ALA A O   
76   O O   B ALA A 17  ? 0.21616 0.35369 0.28932 -0.03560 -0.01025 -0.03471 24  ALA A O   
77   C CB  A ALA A 17  ? 0.20807 0.37693 0.30441 -0.03308 0.00542  -0.02596 24  ALA A CB  
78   C CB  B ALA A 17  ? 0.20820 0.37549 0.30408 -0.03578 0.00652  -0.02754 24  ALA A CB  
79   N N   A GLU A 18  ? 0.27014 0.35274 0.33166 -0.05329 0.01604  -0.04675 25  GLU A N   
80   N N   B GLU A 18  ? 0.27179 0.35377 0.33263 -0.05308 0.01531  -0.04687 25  GLU A N   
81   C CA  A GLU A 18  ? 0.26871 0.33815 0.31809 -0.07109 0.02030  -0.05866 25  GLU A CA  
82   C CA  B GLU A 18  ? 0.26831 0.34021 0.31779 -0.07102 0.01861  -0.05871 25  GLU A CA  
83   C C   A GLU A 18  ? 0.29538 0.34375 0.33567 -0.05390 0.01143  -0.05284 25  GLU A C   
84   C C   B GLU A 18  ? 0.29349 0.34626 0.33450 -0.05408 0.00917  -0.05283 25  GLU A C   
85   O O   A GLU A 18  ? 0.26258 0.31783 0.29778 -0.06286 0.00696  -0.05852 25  GLU A O   
86   O O   B GLU A 18  ? 0.27405 0.34065 0.31241 -0.06156 0.00231  -0.05722 25  GLU A O   
87   C CB  A GLU A 18  ? 0.35917 0.38397 0.39236 -0.08703 0.04564  -0.06869 25  GLU A CB  
88   C CB  B GLU A 18  ? 0.35605 0.38312 0.38888 -0.08746 0.04349  -0.06921 25  GLU A CB  
89   C CG  A GLU A 18  ? 0.42456 0.46675 0.46572 -0.11260 0.05974  -0.07889 25  GLU A CG  
90   C CG  B GLU A 18  ? 0.41665 0.46132 0.45652 -0.11493 0.05763  -0.08072 25  GLU A CG  
91   C CD  A GLU A 18  ? 0.47006 0.51366 0.52172 -0.09635 0.06298  -0.06713 25  GLU A CD  
92   C CD  B GLU A 18  ? 0.46517 0.50572 0.51372 -0.10126 0.06415  -0.07041 25  GLU A CD  
93   O OE1 A GLU A 18  ? 0.36678 0.40080 0.41876 -0.06577 0.05264  -0.05222 25  GLU A OE1 
94   O OE1 B GLU A 18  ? 0.40249 0.42762 0.44985 -0.07044 0.05656  -0.05536 25  GLU A OE1 
95   O OE2 A GLU A 18  ? 0.54438 0.59936 0.60313 -0.11655 0.07740  -0.07444 25  GLU A OE2 
96   O OE2 B GLU A 18  ? 0.51257 0.56696 0.56847 -0.12342 0.07800  -0.07887 25  GLU A OE2 
97   N N   A ILE A 19  ? 0.26769 0.29467 0.30575 -0.03090 0.00918  -0.04282 26  ILE A N   
98   N N   B ILE A 19  ? 0.26490 0.29046 0.30145 -0.03239 0.00919  -0.04386 26  ILE A N   
99   C CA  A ILE A 19  ? 0.20842 0.22243 0.24052 -0.01796 0.00181  -0.03911 26  ILE A CA  
100  C CA  B ILE A 19  ? 0.22439 0.23907 0.25579 -0.01963 0.00114  -0.03998 26  ILE A CA  
101  C C   A ILE A 19  ? 0.22511 0.26521 0.26674 -0.01175 -0.01299 -0.03390 26  ILE A C   
102  C C   B ILE A 19  ? 0.23153 0.27440 0.27286 -0.01442 -0.01353 -0.03496 26  ILE A C   
103  O O   A ILE A 19  ? 0.20425 0.24381 0.24265 -0.01153 -0.01796 -0.03423 26  ILE A O   
104  O O   B ILE A 19  ? 0.21979 0.26458 0.25802 -0.01532 -0.01854 -0.03552 26  ILE A O   
105  C CB  A ILE A 19  ? 0.21230 0.20356 0.23759 0.00108  0.00573  -0.03331 26  ILE A CB  
106  C CB  B ILE A 19  ? 0.23321 0.22643 0.25884 -0.00018 0.00387  -0.03386 26  ILE A CB  
107  C CG1 A ILE A 19  ? 0.32378 0.28328 0.33200 0.00268  0.02424  -0.03436 26  ILE A CG1 
108  C CG1 B ILE A 19  ? 0.31674 0.27865 0.32599 0.00208  0.02235  -0.03462 26  ILE A CG1 
109  C CG2 A ILE A 19  ? 0.24782 0.24272 0.27387 0.01171  -0.00515 -0.03081 26  ILE A CG2 
110  C CG2 B ILE A 19  ? 0.23913 0.23509 0.26510 0.00927  -0.00634 -0.03167 26  ILE A CG2 
111  C CD1 A ILE A 19  ? 0.33479 0.27845 0.33779 -0.00938 0.04267  -0.03820 26  ILE A CD1 
112  C CD1 B ILE A 19  ? 0.35983 0.30922 0.36618 0.00037  0.03724  -0.03403 26  ILE A CD1 
113  N N   A ALA A 20  ? 0.17874 0.23896 0.22977 -0.00448 -0.01685 -0.02739 27  ALA A N   
114  N N   B ALA A 20  ? 0.18909 0.25122 0.23982 -0.00646 -0.01734 -0.02822 27  ALA A N   
115  C CA  A ALA A 20  ? 0.19554 0.27671 0.25055 0.00467  -0.02449 -0.01960 27  ALA A CA  
116  C CA  B ALA A 20  ? 0.19715 0.28116 0.25219 0.00324  -0.02498 -0.02004 27  ALA A CA  
117  C C   A ALA A 20  ? 0.20245 0.31472 0.25881 -0.00627 -0.02869 -0.02241 27  ALA A C   
118  C C   B ALA A 20  ? 0.20737 0.32264 0.26339 -0.00707 -0.02939 -0.02262 27  ALA A C   
119  O O   A ALA A 20  ? 0.24028 0.35741 0.29294 0.00117  -0.03271 -0.01735 27  ALA A O   
120  O O   B ALA A 20  ? 0.22580 0.34360 0.27764 0.00061  -0.03316 -0.01763 27  ALA A O   
121  C CB  A ALA A 20  ? 0.21496 0.31301 0.27653 0.01719  -0.02349 -0.00990 27  ALA A CB  
122  C CB  B ALA A 20  ? 0.21851 0.32058 0.28067 0.01499  -0.02393 -0.01067 27  ALA A CB  
123  N N   A GLN A 21  ? 0.22051 0.35426 0.28027 -0.02548 -0.02595 -0.03179 28  GLN A N   
124  N N   B GLN A 21  ? 0.22591 0.36599 0.28577 -0.02602 -0.02728 -0.03170 28  GLN A N   
125  C CA  A GLN A 21  ? 0.20562 0.37661 0.26473 -0.03991 -0.03042 -0.03847 28  GLN A CA  
126  C CA  B GLN A 21  ? 0.20885 0.38775 0.26796 -0.03912 -0.03225 -0.03766 28  GLN A CA  
127  C C   A GLN A 21  ? 0.23889 0.38052 0.28407 -0.04631 -0.02928 -0.04550 28  GLN A C   
128  C C   B GLN A 21  ? 0.24120 0.39132 0.28655 -0.04433 -0.03171 -0.04391 28  GLN A C   
129  O O   A GLN A 21  ? 0.23887 0.40206 0.28012 -0.04491 -0.03560 -0.04422 28  GLN A O   
130  O O   B GLN A 21  ? 0.25627 0.42557 0.29784 -0.03880 -0.03806 -0.04009 28  GLN A O   
131  C CB  A GLN A 21  ? 0.21512 0.41573 0.27993 -0.06616 -0.02497 -0.05203 28  GLN A CB  
132  C CB  B GLN A 21  ? 0.23889 0.44845 0.30325 -0.06639 -0.02731 -0.05207 28  GLN A CB  
133  C CG  A GLN A 21  ? 0.36714 0.62786 0.43369 -0.08271 -0.03190 -0.06057 28  GLN A CG  
134  C CG  B GLN A 21  ? 0.33101 0.59716 0.39510 -0.08292 -0.03410 -0.06116 28  GLN A CG  
135  C CD  A GLN A 21  ? 0.52235 0.80448 0.59036 -0.11337 -0.02235 -0.07738 28  GLN A CD  
136  C CD  B GLN A 21  ? 0.48488 0.77728 0.55065 -0.11063 -0.02558 -0.07593 28  GLN A CD  
137  O OE1 A GLN A 21  ? 0.48563 0.74045 0.55663 -0.12676 -0.00988 -0.08482 28  GLN A OE1 
138  O OE1 B GLN A 21  ? 0.46640 0.72478 0.53018 -0.12937 -0.01175 -0.08751 28  GLN A OE1 
139  N NE2 A GLN A 21  ? 0.56200 0.88610 0.62370 -0.12224 -0.02433 -0.08234 28  GLN A NE2 
140  N NE2 B GLN A 21  ? 0.54011 0.88803 0.60553 -0.11115 -0.03012 -0.07456 28  GLN A NE2 
141  N N   A LEU A 22  ? 0.21291 0.30747 0.24884 -0.05014 -0.01966 -0.05101 29  LEU A N   
142  N N   B LEU A 22  ? 0.25119 0.35586 0.28711 -0.05176 -0.02206 -0.05149 29  LEU A N   
143  C CA  A LEU A 22  ? 0.28398 0.35013 0.30627 -0.05121 -0.01666 -0.05447 29  LEU A CA  
144  C CA  B LEU A 22  ? 0.25050 0.32756 0.27262 -0.05354 -0.01928 -0.05531 29  LEU A CA  
145  C C   A LEU A 22  ? 0.25420 0.32045 0.27901 -0.03295 -0.02550 -0.04364 29  LEU A C   
146  C C   B LEU A 22  ? 0.25478 0.32823 0.27908 -0.03389 -0.02716 -0.04366 29  LEU A C   
147  O O   A LEU A 22  ? 0.23179 0.30121 0.24989 -0.03423 -0.02787 -0.04432 29  LEU A O   
148  O O   B LEU A 22  ? 0.22522 0.30352 0.24316 -0.03392 -0.02998 -0.04349 29  LEU A O   
149  C CB  A LEU A 22  ? 0.24228 0.26263 0.25365 -0.04910 -0.00267 -0.05644 29  LEU A CB  
150  C CB  B LEU A 22  ? 0.31916 0.34897 0.32955 -0.05496 -0.00461 -0.05929 29  LEU A CB  
151  C CG  A LEU A 22  ? 0.30307 0.29633 0.30150 -0.04239 0.00162  -0.05524 29  LEU A CG  
152  C CG  B LEU A 22  ? 0.30015 0.30092 0.29618 -0.05026 0.00058  -0.05923 29  LEU A CG  
153  C CD1 A LEU A 22  ? 0.34193 0.32753 0.32424 -0.06115 0.00980  -0.06678 29  LEU A CD1 
154  C CD1 B LEU A 22  ? 0.31126 0.30455 0.29024 -0.07158 0.01009  -0.07270 29  LEU A CD1 
155  C CD2 A LEU A 22  ? 0.35542 0.31665 0.34560 -0.02837 0.01371  -0.05015 29  LEU A CD2 
156  C CD2 B LEU A 22  ? 0.37754 0.34391 0.36622 -0.03576 0.01200  -0.05363 29  LEU A CD2 
157  N N   A MET A 23  ? 0.19647 0.25650 0.22876 -0.01746 -0.02795 -0.03475 30  MET A N   
158  N N   B MET A 23  ? 0.21684 0.27997 0.24824 -0.01870 -0.02857 -0.03513 30  MET A N   
159  C CA  A MET A 23  ? 0.22619 0.27820 0.25849 -0.00494 -0.03085 -0.02749 30  MET A CA  
160  C CA  B MET A 23  ? 0.22863 0.28305 0.26032 -0.00541 -0.03126 -0.02736 30  MET A CA  
161  C C   A MET A 23  ? 0.24644 0.32394 0.27850 0.00149  -0.03434 -0.01973 30  MET A C   
162  C C   B MET A 23  ? 0.23293 0.31288 0.26410 0.00154  -0.03467 -0.01936 30  MET A C   
163  O O   A MET A 23  ? 0.22319 0.29389 0.24982 0.00611  -0.03348 -0.01621 30  MET A O   
164  O O   B MET A 23  ? 0.23677 0.30943 0.26235 0.00626  -0.03365 -0.01580 30  MET A O   
165  C CB  A MET A 23  ? 0.20462 0.24208 0.24094 0.00539  -0.02954 -0.02385 30  MET A CB  
166  C CB  B MET A 23  ? 0.20997 0.25026 0.24612 0.00487  -0.02989 -0.02352 30  MET A CB  
167  C CG  A MET A 23  ? 0.22939 0.24844 0.26346 0.00503  -0.02663 -0.02910 30  MET A CG  
168  C CG  B MET A 23  ? 0.22679 0.24726 0.26086 0.00456  -0.02703 -0.02875 30  MET A CG  
169  S SD  A MET A 23  ? 0.24009 0.25233 0.27635 0.01430  -0.02624 -0.02850 30  MET A SD  
170  S SD  B MET A 23  ? 0.27639 0.29020 0.31293 0.01359  -0.02629 -0.02798 30  MET A SD  
171  C CE  A MET A 23  ? 0.26476 0.26959 0.30026 0.01369  -0.02605 -0.03075 30  MET A CE  
172  C CE  B MET A 23  ? 0.26051 0.26646 0.29608 0.01385  -0.02644 -0.03146 30  MET A CE  
173  N N   A SER A 24  ? 0.22154 0.33220 0.25878 0.00435  -0.03674 -0.01526 31  SER A N   
174  N N   B SER A 24  ? 0.22858 0.34237 0.26484 0.00463  -0.03717 -0.01478 31  SER A N   
175  C CA  A SER A 24  ? 0.20722 0.35091 0.24180 0.01696  -0.03862 -0.00421 31  SER A CA  
176  C CA  B SER A 24  ? 0.20998 0.35562 0.24346 0.01887  -0.03857 -0.00275 31  SER A CA  
177  C C   A SER A 24  ? 0.25722 0.42568 0.28524 0.00550  -0.04326 -0.01125 31  SER A C   
178  C C   B SER A 24  ? 0.25773 0.42613 0.28375 0.01017  -0.04286 -0.00803 31  SER A C   
179  O O   A SER A 24  ? 0.29817 0.47982 0.31850 0.01831  -0.04323 -0.00205 31  SER A O   
180  O O   B SER A 24  ? 0.26827 0.44300 0.28614 0.02466  -0.04130 0.00226  31  SER A O   
181  C CB  A SER A 24  ? 0.26805 0.45223 0.31043 0.02656  -0.03960 0.00457  31  SER A CB  
182  C CB  B SER A 24  ? 0.27390 0.46341 0.31548 0.02649  -0.04027 0.00475  31  SER A CB  
183  O OG  A SER A 24  ? 0.40724 0.63189 0.45724 0.00681  -0.04489 -0.00679 31  SER A OG  
184  O OG  B SER A 24  ? 0.21476 0.45214 0.25247 0.04101  -0.04229 0.01648  31  SER A OG  
185  N N   A LEU A 25  ? 0.17669 0.34650 0.20380 -0.01809 -0.04414 -0.02768 32  LEU A N   
186  N N   B LEU A 25  ? 0.23239 0.40908 0.25756 -0.01335 -0.04523 -0.02431 32  LEU A N   
187  C CA  A LEU A 25  ? 0.17881 0.36330 0.19467 -0.03231 -0.04597 -0.03794 32  LEU A CA  
188  C CA  B LEU A 25  ? 0.19190 0.38606 0.20573 -0.02480 -0.04778 -0.03275 32  LEU A CA  
189  C C   A LEU A 25  ? 0.25345 0.39988 0.25904 -0.02470 -0.04267 -0.03459 32  LEU A C   
190  C C   B LEU A 25  ? 0.25311 0.40214 0.25681 -0.02111 -0.04319 -0.03211 32  LEU A C   
191  O O   A LEU A 25  ? 0.23395 0.39693 0.23003 -0.02067 -0.04486 -0.03213 32  LEU A O   
192  O O   B LEU A 25  ? 0.27464 0.43414 0.26847 -0.01547 -0.04438 -0.02862 32  LEU A O   
193  C CB  A LEU A 25  ? 0.24947 0.42707 0.26100 -0.06143 -0.04053 -0.05804 32  LEU A CB  
194  C CB  B LEU A 25  ? 0.31514 0.52181 0.32623 -0.05501 -0.04614 -0.05334 32  LEU A CB  
195  C CG  A LEU A 25  ? 0.38583 0.57258 0.38072 -0.08375 -0.03837 -0.07477 32  LEU A CG  
196  C CG  B LEU A 25  ? 0.44187 0.71743 0.45290 -0.06626 -0.05255 -0.05983 32  LEU A CG  
197  C CD1 A LEU A 25  ? 0.50199 0.69244 0.49456 -0.11263 -0.02859 -0.09275 32  LEU A CD1 
198  C CD1 B LEU A 25  ? 0.25249 0.55967 0.27885 -0.06740 -0.05145 -0.05697 32  LEU A CD1 
199  C CD2 A LEU A 25  ? 0.38881 0.52084 0.36758 -0.08175 -0.03015 -0.07634 32  LEU A CD2 
200  C CD2 B LEU A 25  ? 0.33852 0.60127 0.33385 -0.09370 -0.04424 -0.07963 32  LEU A CD2 
201  N N   A ILE A 26  ? 0.19643 0.29768 0.20388 -0.02202 -0.03712 -0.03419 33  ILE A N   
202  N N   B ILE A 26  ? 0.21856 0.32300 0.22447 -0.02253 -0.03751 -0.03447 33  ILE A N   
203  C CA  A ILE A 26  ? 0.24368 0.31605 0.24471 -0.01649 -0.03327 -0.03154 33  ILE A CA  
204  C CA  B ILE A 26  ? 0.24460 0.31644 0.24538 -0.01628 -0.03319 -0.03140 33  ILE A CA  
205  C C   A ILE A 26  ? 0.27149 0.34771 0.27350 0.00103  -0.03296 -0.01780 33  ILE A C   
206  C C   B ILE A 26  ? 0.27192 0.34632 0.27408 0.00127  -0.03267 -0.01767 33  ILE A C   
207  O O   A ILE A 26  ? 0.28740 0.35806 0.28130 0.00502  -0.03028 -0.01454 33  ILE A O   
208  O O   B ILE A 26  ? 0.27983 0.34610 0.27453 0.00542  -0.02954 -0.01427 33  ILE A O   
209  C CB  A ILE A 26  ? 0.21320 0.25200 0.21803 -0.01608 -0.02798 -0.03360 33  ILE A CB  
210  C CB  B ILE A 26  ? 0.21342 0.25339 0.21902 -0.01604 -0.02826 -0.03353 33  ILE A CB  
211  C CG1 A ILE A 26  ? 0.31305 0.33632 0.30820 -0.02877 -0.02087 -0.04415 33  ILE A CG1 
212  C CG1 B ILE A 26  ? 0.30145 0.32662 0.29802 -0.02890 -0.02135 -0.04413 33  ILE A CG1 
213  C CG2 A ILE A 26  ? 0.24632 0.26793 0.25076 -0.00880 -0.02473 -0.02897 33  ILE A CG2 
214  C CG2 B ILE A 26  ? 0.25189 0.27309 0.25761 -0.00881 -0.02486 -0.02924 33  ILE A CG2 
215  C CD1 A ILE A 26  ? 0.31874 0.31900 0.31619 -0.02251 -0.01453 -0.04289 33  ILE A CD1 
216  C CD1 B ILE A 26  ? 0.30883 0.31151 0.30810 -0.02267 -0.01534 -0.04285 33  ILE A CD1 
217  N N   . ILE A 27  ? 0.23932 0.32002 0.24821 0.01276  -0.03207 -0.00884 34  ILE A N   
218  C CA  . ILE A 27  ? 0.29626 0.36649 0.30093 0.03043  -0.02413 0.00491  34  ILE A CA  
219  C C   . ILE A 27  ? 0.34055 0.44542 0.33521 0.04440  -0.02449 0.01600  34  ILE A C   
220  O O   . ILE A 27  ? 0.31138 0.40418 0.29590 0.05756  -0.01559 0.02632  34  ILE A O   
221  C CB  . ILE A 27  ? 0.30950 0.36525 0.31895 0.03896  -0.01844 0.01031  34  ILE A CB  
222  C CG1 . ILE A 27  ? 0.28559 0.31099 0.30192 0.02708  -0.01732 -0.00059 34  ILE A CG1 
223  C CG2 . ILE A 27  ? 0.33814 0.38023 0.33664 0.05974  -0.00402 0.02643  34  ILE A CG2 
224  C CD1 . ILE A 27  ? 0.31643 0.33133 0.33588 0.03096  -0.01411 -0.00013 34  ILE A CD1 
225  N N   . ASN A 28  ? 0.27888 0.43164 0.27561 0.04162  -0.03363 0.01385  35  ASN A N   
226  C CA  . ASN A 28  ? 0.27266 0.47612 0.26109 0.05952  -0.03510 0.02660  35  ASN A CA  
227  C C   . ASN A 28  ? 0.38251 0.61721 0.36067 0.04947  -0.04238 0.01797  35  ASN A C   
228  O O   . ASN A 28  ? 0.36249 0.63146 0.32876 0.06922  -0.04124 0.03092  35  ASN A O   
229  C CB  . ASN A 28  ? 0.27970 0.53464 0.27779 0.06249  -0.04123 0.02928  35  ASN A CB  
230  C CG  . ASN A 28  ? 0.52829 0.75512 0.53206 0.07709  -0.03221 0.04030  35  ASN A CG  
231  O OD1 . ASN A 28  ? 0.63714 0.88293 0.65275 0.07080  -0.03645 0.03654  35  ASN A OD1 
232  N ND2 . ASN A 28  ? 0.36277 0.54262 0.35602 0.09570  -0.01713 0.05331  35  ASN A ND2 
233  N N   . THR A 29  ? 0.27260 0.49615 0.25138 0.02123  -0.04747 -0.00290 36  THR A N   
234  C CA  . THR A 29  ? 0.31892 0.56944 0.28377 0.00782  -0.05239 -0.01475 36  THR A CA  
235  C C   . THR A 29  ? 0.35315 0.57506 0.30411 0.02124  -0.04582 -0.00614 36  THR A C   
236  O O   . THR A 29  ? 0.35610 0.52375 0.31010 0.02316  -0.03768 -0.00333 36  THR A O   
237  C CB  . THR A 29  ? 0.32896 0.55955 0.29232 -0.02529 -0.05228 -0.03896 36  THR A CB  
238  O OG1 . THR A 29  ? 0.33150 0.58623 0.30785 -0.03873 -0.05535 -0.04672 36  THR A OG1 
239  C CG2 . THR A 29  ? 0.38770 0.64101 0.33158 -0.04318 -0.05423 -0.05489 36  THR A CG2 
240  N N   . PHE A 30  ? 0.28144 0.54565 0.21730 0.03063  -0.04898 -0.00201 37  PHE A N   
241  C CA  . PHE A 30  ? 0.26390 0.50174 0.18420 0.04105  -0.04179 0.00436  37  PHE A CA  
242  C C   . PHE A 30  ? 0.31119 0.51559 0.22386 0.01453  -0.04100 -0.01613 37  PHE A C   
243  O O   . PHE A 30  ? 0.30868 0.53872 0.21166 -0.00838 -0.04677 -0.03561 37  PHE A O   
244  C CB  . PHE A 30  ? 0.28435 0.58009 0.18703 0.06101  -0.04479 0.01500  37  PHE A CB  
245  C CG  . PHE A 30  ? 0.33740 0.60582 0.22217 0.07369  -0.03571 0.02292  37  PHE A CG  
246  C CD1 . PHE A 30  ? 0.42943 0.65434 0.31366 0.09895  -0.01951 0.04463  37  PHE A CD1 
247  C CD2 . PHE A 30  ? 0.33540 0.61761 0.20203 0.05824  -0.04050 0.00729  37  PHE A CD2 
248  C CE1 . PHE A 30  ? 0.37952 0.57832 0.24839 0.10960  -0.00881 0.05220  37  PHE A CE1 
249  C CE2 . PHE A 30  ? 0.42369 0.67982 0.27333 0.07134  -0.03113 0.01563  37  PHE A CE2 
250  C CZ  . PHE A 30  ? 0.34771 0.56374 0.19997 0.09758  -0.01557 0.03891  37  PHE A CZ  
251  N N   . TYR A 31  ? 0.28252 0.43058 0.19788 0.01724  -0.03130 -0.01208 38  TYR A N   
252  C CA  . TYR A 31  ? 0.28945 0.40100 0.19739 -0.00136 -0.02659 -0.02675 38  TYR A CA  
253  C C   . TYR A 31  ? 0.26714 0.33844 0.17727 0.01138  -0.01607 -0.01512 38  TYR A C   
254  O O   . TYR A 31  ? 0.28445 0.33342 0.21218 0.01600  -0.01203 -0.00843 38  TYR A O   
255  C CB  . TYR A 31  ? 0.33700 0.43021 0.25607 -0.01891 -0.02650 -0.03877 38  TYR A CB  
256  C CG  . TYR A 31  ? 0.38541 0.43664 0.29281 -0.03160 -0.01631 -0.04969 38  TYR A CG  
257  C CD1 . TYR A 31  ? 0.38164 0.43128 0.26467 -0.04968 -0.01181 -0.06643 38  TYR A CD1 
258  C CD2 . TYR A 31  ? 0.37723 0.39248 0.29522 -0.02447 -0.00893 -0.04316 38  TYR A CD2 
259  C CE1 . TYR A 31  ? 0.57194 0.57493 0.43847 -0.05727 0.00317  -0.07400 38  TYR A CE1 
260  C CE2 . TYR A 31  ? 0.36359 0.34394 0.26825 -0.02915 0.00335  -0.04875 38  TYR A CE2 
261  C CZ  . TYR A 31  ? 0.49858 0.46778 0.37606 -0.04397 0.01104  -0.06294 38  TYR A CZ  
262  O OH  . TYR A 31  ? 0.65778 0.58406 0.51627 -0.04508 0.02871  -0.06641 38  TYR A OH  
263  N N   . SER A 32  ? 0.29217 0.35809 0.18432 0.01524  -0.01111 -0.01410 39  SER A N   
264  C CA  . SER A 32  ? 0.30396 0.34124 0.19891 0.02864  0.00011  -0.00106 39  SER A CA  
265  C C   . SER A 32  ? 0.32285 0.32552 0.22654 0.02044  0.00724  -0.00554 39  SER A C   
266  O O   . SER A 32  ? 0.36900 0.35572 0.28550 0.02738  0.01546  0.00378  39  SER A O   
267  C CB  . SER A 32  ? 0.32865 0.37456 0.20003 0.03844  0.00403  0.00341  39  SER A CB  
268  O OG  . SER A 32  ? 0.32527 0.40996 0.18855 0.05417  -0.00044 0.01318  39  SER A OG  
269  N N   . ASN A 33  ? 0.30210 0.29494 0.19804 0.00643  0.00682  -0.01913 40  ASN A N   
270  C CA  . ASN A 33  ? 0.34439 0.30800 0.24101 0.00552  0.01702  -0.02001 40  ASN A CA  
271  C C   . ASN A 33  ? 0.34771 0.30968 0.26906 0.00588  0.01537  -0.01761 40  ASN A C   
272  O O   . ASN A 33  ? 0.30261 0.25282 0.22229 0.00150  0.01864  -0.02330 40  ASN A O   
273  C CB  . ASN A 33  ? 0.39441 0.33963 0.26404 -0.00650 0.02388  -0.03405 40  ASN A CB  
274  C CG  . ASN A 33  ? 0.48122 0.39374 0.34467 -0.00068 0.03933  -0.03115 40  ASN A CG  
275  O OD1 . ASN A 33  ? 0.44881 0.35925 0.32099 0.01270  0.04491  -0.01908 40  ASN A OD1 
276  N ND2 . ASN A 33  ? 0.46850 0.35640 0.31532 -0.00965 0.04917  -0.04134 40  ASN A ND2 
277  N N   . LYS A 34  ? 0.26268 0.26535 0.19989 0.00742  -0.03244 -0.01522 41  LYS A N   
278  C CA  . LYS A 34  ? 0.23079 0.26223 0.19747 0.01406  -0.02065 -0.01362 41  LYS A CA  
279  C C   . LYS A 34  ? 0.22771 0.24162 0.19227 0.01538  -0.01058 -0.02390 41  LYS A C   
280  O O   . LYS A 34  ? 0.23844 0.26677 0.21942 0.01731  -0.00664 -0.02334 41  LYS A O   
281  C CB  . LYS A 34  ? 0.23785 0.27714 0.20768 0.03120  -0.01167 -0.01268 41  LYS A CB  
282  C CG  . LYS A 34  ? 0.23543 0.30510 0.21312 0.03898  -0.01694 0.00213  41  LYS A CG  
283  C CD  . LYS A 34  ? 0.32150 0.37825 0.28425 0.06202  -0.00966 -0.00052 41  LYS A CD  
284  C CE  . LYS A 34  ? 0.29850 0.39021 0.26673 0.08007  -0.01034 0.01718  41  LYS A CE  
285  N NZ  . LYS A 34  ? 0.26121 0.40119 0.24699 0.09986  -0.00237 0.03624  41  LYS A NZ  
286  N N   . GLU A 35  ? 0.26162 0.24822 0.20444 0.01883  -0.00498 -0.02944 42  GLU A N   
287  C CA  . GLU A 35  ? 0.24822 0.23156 0.19721 0.02365  0.00696  -0.03088 42  GLU A CA  
288  C C   . GLU A 35  ? 0.29558 0.27610 0.24711 0.01728  0.00233  -0.03484 42  GLU A C   
289  O O   . GLU A 35  ? 0.27832 0.26402 0.24323 0.01989  0.01041  -0.03449 42  GLU A O   
290  C CB  . GLU A 35  ? 0.29409 0.26082 0.21771 0.03834  0.01896  -0.02691 42  GLU A CB  
291  C CG  . GLU A 35  ? 0.31867 0.24258 0.18957 0.04670  0.01146  -0.03456 42  GLU A CG  
292  C CD  . GLU A 35  ? 0.49322 0.39641 0.32179 0.07618  0.02846  -0.02852 42  GLU A CD  
293  O OE1 . GLU A 35  ? 0.48695 0.41039 0.32556 0.08270  0.03945  -0.01737 42  GLU A OE1 
294  O OE2 . GLU A 35  ? 0.61076 0.47467 0.38975 0.09705  0.03116  -0.03261 42  GLU A OE2 
295  N N   . ILE A 36  ? 0.29499 0.26844 0.23642 0.00553  -0.01443 -0.03394 43  ILE A N   
296  C CA  . ILE A 36  ? 0.25013 0.21697 0.19208 -0.00420 -0.02292 -0.03367 43  ILE A CA  
297  C C   . ILE A 36  ? 0.24724 0.25122 0.22624 -0.00454 -0.01450 -0.02960 43  ILE A C   
298  O O   . ILE A 36  ? 0.24827 0.24925 0.23056 -0.00948 -0.01643 -0.02971 43  ILE A O   
299  C CB  . ILE A 36  ? 0.33189 0.28330 0.25875 -0.02546 -0.05243 -0.02396 43  ILE A CB  
300  C CG1 . ILE A 36  ? 0.30732 0.31207 0.27263 -0.03509 -0.05854 -0.00471 43  ILE A CG1 
301  C CG2 . ILE A 36  ? 0.44730 0.33333 0.31154 -0.02124 -0.06755 -0.03231 43  ILE A CG2 
302  C CD1 . ILE A 36  ? 0.45274 0.50872 0.45954 -0.04414 -0.05988 0.01582  43  ILE A CD1 
303  N N   . PHE A 37  ? 0.19233 0.22160 0.18826 0.00460  -0.00679 -0.02640 44  PHE A N   
304  C CA  . PHE A 37  ? 0.20073 0.24679 0.20945 0.01347  -0.00036 -0.02452 44  PHE A CA  
305  C C   . PHE A 37  ? 0.23712 0.26353 0.24455 0.01283  0.00344  -0.03309 44  PHE A C   
306  O O   . PHE A 37  ? 0.19265 0.22475 0.20522 0.01368  0.00401  -0.03221 44  PHE A O   
307  C CB  . PHE A 37  ? 0.19825 0.24565 0.19908 0.03209  0.00389  -0.02397 44  PHE A CB  
308  C CG  . PHE A 37  ? 0.25005 0.26343 0.23877 0.03304  0.00204  -0.03250 44  PHE A CG  
309  C CD1 . PHE A 37  ? 0.24683 0.25218 0.23363 0.02835  0.00152  -0.03167 44  PHE A CD1 
310  C CD2 . PHE A 37  ? 0.30884 0.29911 0.28906 0.03547  -0.00311 -0.03587 44  PHE A CD2 
311  C CE1 . PHE A 37  ? 0.24709 0.23261 0.23300 0.02404  -0.00291 -0.02819 44  PHE A CE1 
312  C CE2 . PHE A 37  ? 0.23873 0.20182 0.21567 0.02705  -0.01375 -0.03332 44  PHE A CE2 
313  C CZ  . PHE A 37  ? 0.23572 0.20189 0.22027 0.02022  -0.01302 -0.02654 44  PHE A CZ  
314  N N   . LEU A 38  ? 0.20188 0.21215 0.20550 0.01267  0.00675  -0.03594 45  LEU A N   
315  C CA  . LEU A 38  ? 0.18161 0.18729 0.19449 0.01203  0.00932  -0.03421 45  LEU A CA  
316  C C   . LEU A 38  ? 0.21319 0.21447 0.22186 0.01125  0.01204  -0.03646 45  LEU A C   
317  O O   . LEU A 38  ? 0.22859 0.23188 0.24673 0.00974  0.01144  -0.03593 45  LEU A O   
318  C CB  . LEU A 38  ? 0.18050 0.18852 0.20122 0.01324  0.01346  -0.02325 45  LEU A CB  
319  C CG  . LEU A 38  ? 0.20461 0.22301 0.24822 0.00885  0.01227  -0.00877 45  LEU A CG  
320  C CD1 . LEU A 38  ? 0.21077 0.21156 0.25425 -0.00068 -0.00634 -0.01130 45  LEU A CD1 
321  C CD2 . LEU A 38  ? 0.27670 0.31564 0.33953 0.00829  0.01648  0.01570  45  LEU A CD2 
322  N N   . ARG A 39  ? 0.22845 0.21265 0.21332 0.01305  0.01070  -0.03929 46  ARG A N   
323  C CA  . ARG A 39  ? 0.25457 0.21404 0.21781 0.01296  0.00552  -0.04268 46  ARG A CA  
324  C C   . ARG A 39  ? 0.26753 0.23997 0.24739 -0.00199 -0.00436 -0.04051 46  ARG A C   
325  O O   . ARG A 39  ? 0.24368 0.20905 0.22339 -0.00213 -0.00445 -0.04122 46  ARG A O   
326  C CB  . ARG A 39  ? 0.30393 0.22035 0.21990 0.01473  -0.00669 -0.04657 46  ARG A CB  
327  C CG  . ARG A 39  ? 0.37634 0.24353 0.25180 0.01224  -0.02318 -0.05031 46  ARG A CG  
328  C CD  . ARG A 39  ? 0.53222 0.33518 0.34544 0.00814  -0.04960 -0.05356 46  ARG A CD  
329  N NE  . ARG A 39  ? 0.53005 0.35426 0.36891 -0.02475 -0.07415 -0.04172 46  ARG A NE  
330  C CZ  . ARG A 39  ? 0.60637 0.39534 0.41114 -0.03641 -0.10028 -0.03824 46  ARG A CZ  
331  N NH1 . ARG A 39  ? 0.57462 0.29057 0.30354 -0.01480 -0.10631 -0.05091 46  ARG A NH1 
332  N NH2 . ARG A 39  ? 0.58059 0.40965 0.42518 -0.06722 -0.12123 -0.01764 46  ARG A NH2 
333  N N   . GLU A 40  ? 0.21417 0.21204 0.20965 -0.01086 -0.01042 -0.03323 47  GLU A N   
334  C CA  . GLU A 40  ? 0.22447 0.24843 0.23826 -0.02021 -0.01608 -0.02095 47  GLU A CA  
335  C C   . GLU A 40  ? 0.21555 0.25186 0.24012 -0.00815 -0.00412 -0.02416 47  GLU A C   
336  O O   . GLU A 40  ? 0.18743 0.22926 0.21711 -0.01233 -0.00593 -0.01884 47  GLU A O   
337  C CB  . GLU A 40  ? 0.18255 0.24612 0.21450 -0.02412 -0.02045 -0.00260 47  GLU A CB  
338  C CG  . GLU A 40  ? 0.24600 0.29528 0.26769 -0.04423 -0.04288 0.00661  47  GLU A CG  
339  C CD  . GLU A 40  ? 0.35870 0.36470 0.35678 -0.06596 -0.06780 0.00934  47  GLU A CD  
340  O OE1 . GLU A 40  ? 0.33186 0.35248 0.34545 -0.07458 -0.07074 0.02044  47  GLU A OE1 
341  O OE2 . GLU A 40  ? 0.45859 0.40677 0.41282 -0.07180 -0.08657 0.00056  47  GLU A OE2 
342  N N   . LEU A 41  ? 0.18403 0.21657 0.20608 0.00502  0.00303  -0.03124 48  LEU A N   
343  C CA  . LEU A 41  ? 0.20893 0.23420 0.22628 0.01480  0.00443  -0.03430 48  LEU A CA  
344  C C   . LEU A 41  ? 0.19807 0.20862 0.22079 0.00790  0.00252  -0.03806 48  LEU A C   
345  O O   . LEU A 41  ? 0.20214 0.20917 0.22278 0.00989  0.00041  -0.03791 48  LEU A O   
346  C CB  . LEU A 41  ? 0.18775 0.19357 0.18849 0.02628  0.00081  -0.03842 48  LEU A CB  
347  C CG  . LEU A 41  ? 0.20523 0.22259 0.19132 0.04460  0.00529  -0.03364 48  LEU A CG  
348  C CD1 . LEU A 41  ? 0.25982 0.23668 0.21486 0.05640  -0.00426 -0.04009 48  LEU A CD1 
349  C CD2 . LEU A 41  ? 0.20694 0.24732 0.18428 0.06442  0.01380  -0.02291 48  LEU A CD2 
350  N N   . ILE A 42  ? 0.17122 0.17578 0.19819 0.00492  0.00510  -0.03819 49  ILE A N   
351  C CA  . ILE A 42  ? 0.19372 0.19495 0.22753 0.00624  0.00763  -0.03479 49  ILE A CA  
352  C C   . ILE A 42  ? 0.21988 0.21070 0.24227 0.00443  0.00631  -0.03794 49  ILE A C   
353  O O   . ILE A 42  ? 0.21342 0.20278 0.24068 0.00542  0.00576  -0.03620 49  ILE A O   
354  C CB  . ILE A 42  ? 0.20099 0.20652 0.23696 0.01509  0.01696  -0.02671 49  ILE A CB  
355  C CG1 . ILE A 42  ? 0.16553 0.18600 0.22318 0.00961  0.01261  -0.01422 49  ILE A CG1 
356  C CG2 . ILE A 42  ? 0.26289 0.27022 0.29883 0.02797  0.02556  -0.01850 49  ILE A CG2 
357  C CD1 . ILE A 42  ? 0.21926 0.25936 0.28623 0.01973  0.02509  0.00326  49  ILE A CD1 
358  N N   . SER A 43  ? 0.21225 0.19255 0.21861 -0.00189 0.00043  -0.03933 50  SER A N   
359  C CA  . SER A 43  ? 0.26266 0.22430 0.25492 -0.01088 -0.01023 -0.03718 50  SER A CA  
360  C C   . SER A 43  ? 0.23423 0.22282 0.24709 -0.01766 -0.01108 -0.02931 50  SER A C   
361  O O   . SER A 43  ? 0.23311 0.21166 0.24259 -0.02052 -0.01465 -0.02750 50  SER A O   
362  C CB  . SER A 43  ? 0.33744 0.27591 0.30677 -0.02428 -0.02775 -0.03336 50  SER A CB  
363  O OG  . SER A 43  ? 0.40381 0.32974 0.36741 -0.04390 -0.04755 -0.02218 50  SER A OG  
364  N N   . ASN A 44  ? 0.20105 0.22103 0.22809 -0.01397 -0.00603 -0.02344 51  ASN A N   
365  C CA  . ASN A 44  ? 0.21239 0.25532 0.24568 -0.00700 -0.00146 -0.01446 51  ASN A CA  
366  C C   . ASN A 44  ? 0.22686 0.24954 0.25242 0.00123  -0.00013 -0.02490 51  ASN A C   
367  O O   . ASN A 44  ? 0.20380 0.22899 0.22787 0.00183  -0.00056 -0.01991 51  ASN A O   
368  C CB  . ASN A 44  ? 0.19067 0.25863 0.22190 0.01058  0.00699  -0.00774 51  ASN A CB  
369  C CG  . ASN A 44  ? 0.32879 0.43835 0.37917 0.00319  0.00593  0.01546  51  ASN A CG  
370  O OD1 . ASN A 44  ? 0.22168 0.33560 0.28547 -0.02179 -0.00790 0.02824  51  ASN A OD1 
371  N ND2 . ASN A 44  ? 0.26911 0.40514 0.31700 0.02475  0.01626  0.02451  51  ASN A ND2 
372  N N   . SER A 45  ? 0.16929 0.17510 0.19282 0.00501  -0.00153 -0.03415 52  SER A N   
373  C CA  . SER A 45  ? 0.19169 0.18223 0.21502 0.00605  -0.00796 -0.03599 52  SER A CA  
374  C C   . SER A 45  ? 0.21860 0.20818 0.25093 0.00153  -0.00648 -0.03372 52  SER A C   
375  O O   . SER A 45  ? 0.21294 0.19740 0.24370 0.00206  -0.01094 -0.03210 52  SER A O   
376  C CB  . SER A 45  ? 0.17792 0.16073 0.20882 0.00309  -0.01523 -0.03400 52  SER A CB  
377  O OG  . SER A 45  ? 0.24121 0.20609 0.24981 0.00912  -0.02320 -0.03758 52  SER A OG  
378  N N   . SER A 46  ? 0.19091 0.17639 0.22221 0.00152  -0.00155 -0.03397 53  SER A N   
379  C CA  . SER A 46  ? 0.24890 0.21849 0.27095 0.00604  -0.00077 -0.03278 53  SER A CA  
380  C C   . SER A 46  ? 0.30417 0.26519 0.31725 -0.00361 -0.00844 -0.03153 53  SER A C   
381  O O   . SER A 46  ? 0.25365 0.20580 0.26433 -0.00077 -0.01015 -0.02979 53  SER A O   
382  C CB  . SER A 46  ? 0.25185 0.19729 0.24822 0.01611  0.00276  -0.03531 53  SER A CB  
383  O OG  . SER A 46  ? 0.29784 0.21083 0.26571 0.02935  0.00209  -0.03547 53  SER A OG  
384  N N   . ASP A 47  ? 0.24117 0.21196 0.25393 -0.01539 -0.01342 -0.02634 54  ASP A N   
385  C CA  . ASP A 47  ? 0.21878 0.19696 0.23318 -0.02741 -0.02096 -0.01337 54  ASP A CA  
386  C C   . ASP A 47  ? 0.28744 0.28321 0.30856 -0.01758 -0.01383 -0.01128 54  ASP A C   
387  O O   . ASP A 47  ? 0.23638 0.22702 0.25471 -0.02163 -0.01785 -0.00480 54  ASP A O   
388  C CB  . ASP A 47  ? 0.20787 0.21546 0.23455 -0.04092 -0.02632 0.00466  54  ASP A CB  
389  C CG  . ASP A 47  ? 0.34395 0.31876 0.35379 -0.05957 -0.04661 0.00770  54  ASP A CG  
390  O OD1 . ASP A 47  ? 0.35844 0.27760 0.33383 -0.05561 -0.05475 -0.00641 54  ASP A OD1 
391  O OD2 . ASP A 47  ? 0.30901 0.31028 0.33392 -0.07494 -0.05609 0.02666  54  ASP A OD2 
392  N N   . ALA A 48  ? 0.20224 0.20767 0.22222 -0.00368 -0.00715 -0.01683 55  ALA A N   
393  C CA  . ALA A 48  ? 0.24190 0.24331 0.24747 0.00981  -0.00666 -0.01711 55  ALA A CA  
394  C C   . ALA A 48  ? 0.21900 0.19778 0.22573 0.00691  -0.01513 -0.02365 55  ALA A C   
395  O O   . ALA A 48  ? 0.21688 0.18812 0.21223 0.01136  -0.01870 -0.02115 55  ALA A O   
396  C CB  . ALA A 48  ? 0.21456 0.20690 0.19806 0.02734  -0.00622 -0.02278 55  ALA A CB  
397  N N   . LEU A 49  ? 0.21841 0.19226 0.23989 0.00249  -0.01723 -0.02718 56  LEU A N   
398  C CA  . LEU A 49  ? 0.21255 0.18179 0.24537 0.00258  -0.02272 -0.02315 56  LEU A CA  
399  C C   . LEU A 49  ? 0.26556 0.22701 0.29306 0.00341  -0.01960 -0.02125 56  LEU A C   
400  O O   . LEU A 49  ? 0.23307 0.19047 0.26169 0.00525  -0.02481 -0.01723 56  LEU A O   
401  C CB  . LEU A 49  ? 0.19810 0.18018 0.25256 0.00425  -0.02024 -0.01641 56  LEU A CB  
402  C CG  . LEU A 49  ? 0.19106 0.17306 0.25120 -0.00296 -0.03308 -0.01290 56  LEU A CG  
403  C CD1 . LEU A 49  ? 0.18823 0.19033 0.26906 -0.00246 -0.02588 -0.00408 56  LEU A CD1 
404  C CD2 . LEU A 49  ? 0.23045 0.20501 0.29805 -0.01184 -0.05599 -0.00064 56  LEU A CD2 
405  N N   . ASP A 50  ? 0.21406 0.16440 0.22958 0.00047  -0.01658 -0.02295 57  ASP A N   
406  C CA  . ASP A 50  ? 0.25079 0.17546 0.24789 -0.00223 -0.02249 -0.02017 57  ASP A CA  
407  C C   . ASP A 50  ? 0.30926 0.24400 0.30892 -0.01026 -0.02667 -0.01251 57  ASP A C   
408  O O   . ASP A 50  ? 0.26583 0.18424 0.25710 -0.00911 -0.03143 -0.00948 57  ASP A O   
409  C CB  . ASP A 50  ? 0.26845 0.16554 0.24230 -0.01282 -0.03174 -0.01955 57  ASP A CB  
410  C CG  . ASP A 50  ? 0.35935 0.22876 0.30974 0.00310  -0.02817 -0.02796 57  ASP A CG  
411  O OD1 . ASP A 50  ? 0.33522 0.21700 0.29387 0.02501  -0.01424 -0.02867 57  ASP A OD1 
412  O OD2 . ASP A 50  ? 0.38092 0.21651 0.30250 -0.00602 -0.04143 -0.02900 57  ASP A OD2 
413  N N   . LYS A 51  ? 0.22617 0.18799 0.23241 -0.01285 -0.02285 -0.00686 58  LYS A N   
414  C CA  . LYS A 51  ? 0.24878 0.22648 0.25160 -0.01256 -0.02168 0.00668  58  LYS A CA  
415  C C   . LYS A 51  ? 0.24532 0.21000 0.23715 -0.00026 -0.02361 0.00020  58  LYS A C   
416  O O   . LYS A 51  ? 0.29293 0.25272 0.27875 -0.00164 -0.02656 0.00781  58  LYS A O   
417  C CB  . LYS A 51  ? 0.24727 0.26127 0.25206 -0.00456 -0.01140 0.01901  58  LYS A CB  
418  C CG  . LYS A 51  ? 0.23935 0.28022 0.26376 -0.02322 -0.01450 0.03956  58  LYS A CG  
419  C CD  . LYS A 51  ? 0.25212 0.34300 0.28390 -0.00738 0.00041  0.05822  58  LYS A CD  
420  C CE  . LYS A 51  ? 0.31240 0.42969 0.36967 -0.02810 -0.00697 0.07607  58  LYS A CE  
421  N NZ  . LYS A 51  ? 0.36967 0.54812 0.43919 -0.00720 0.01078  0.10150  58  LYS A NZ  
422  N N   . ILE A 52  ? 0.24843 0.20353 0.23594 0.00844  -0.02720 -0.01068 59  ILE A N   
423  C CA  . ILE A 52  ? 0.26161 0.19692 0.23576 0.01412  -0.03926 -0.01273 59  ILE A CA  
424  C C   . ILE A 52  ? 0.27098 0.20393 0.26570 0.00798  -0.04429 -0.00955 59  ILE A C   
425  O O   . ILE A 52  ? 0.28312 0.20603 0.27031 0.00982  -0.05234 -0.00571 59  ILE A O   
426  C CB  . ILE A 52  ? 0.31940 0.23380 0.27823 0.01804  -0.05372 -0.01914 59  ILE A CB  
427  C CG1 . ILE A 52  ? 0.34777 0.22661 0.27642 0.02161  -0.07630 -0.01867 59  ILE A CG1 
428  C CG2 . ILE A 52  ? 0.29114 0.21776 0.28535 0.00621  -0.05790 -0.01707 59  ILE A CG2 
429  C CD1 . ILE A 52  ? 0.37586 0.23952 0.25799 0.04203  -0.06981 -0.01849 59  ILE A CD1 
430  N N   . ARG A 53  ? 0.25259 0.19272 0.26656 0.00665  -0.03822 -0.00939 60  ARG A N   
431  C CA  . ARG A 53  ? 0.27614 0.21323 0.29884 0.01363  -0.03783 -0.00298 60  ARG A CA  
432  C C   . ARG A 53  ? 0.29606 0.21153 0.29790 0.01256  -0.03892 -0.00231 60  ARG A C   
433  O O   . ARG A 53  ? 0.28109 0.19071 0.28238 0.01805  -0.04374 0.00326  60  ARG A O   
434  C CB  . ARG A 53  ? 0.31763 0.25834 0.34627 0.02515  -0.02703 -0.00146 60  ARG A CB  
435  C CG  . ARG A 53  ? 0.48951 0.43511 0.52451 0.04566  -0.02250 0.01159  60  ARG A CG  
436  C CD  . ARG A 53  ? 0.59136 0.53393 0.61435 0.07184  -0.00675 0.01583  60  ARG A CD  
437  N NE  . ARG A 53  ? 0.65019 0.64630 0.71609 0.08087  0.00131  0.03774  60  ARG A NE  
438  C CZ  . ARG A 53  ? 0.71262 0.72075 0.77812 0.09419  0.01489  0.04178  60  ARG A CZ  
439  N NH1 . ARG A 53  ? 0.50202 0.46518 0.52186 0.09870  0.01883  0.02111  60  ARG A NH1 
440  N NH2 . ARG A 53  ? 0.38292 0.45097 0.49589 0.10119  0.02165  0.07214  60  ARG A NH2 
441  N N   . TYR A 54  ? 0.30999 0.21500 0.29712 0.00233  -0.03824 -0.00301 61  TYR A N   
442  C CA  . TYR A 54  ? 0.30168 0.18471 0.27110 -0.00621 -0.04611 0.00501  61  TYR A CA  
443  C C   . TYR A 54  ? 0.34965 0.24697 0.32054 -0.00621 -0.04699 0.01246  61  TYR A C   
444  O O   . TYR A 54  ? 0.35749 0.23658 0.31823 -0.00541 -0.05323 0.01746  61  TYR A O   
445  C CB  . TYR A 54  ? 0.31361 0.19315 0.27697 -0.02619 -0.05297 0.01449  61  TYR A CB  
446  C CG  . TYR A 54  ? 0.43537 0.28811 0.38209 -0.04279 -0.06950 0.03041  61  TYR A CG  
447  C CD1 . TYR A 54  ? 0.40331 0.19193 0.31249 -0.03945 -0.08483 0.02489  61  TYR A CD1 
448  C CD2 . TYR A 54  ? 0.36915 0.25808 0.33176 -0.05719 -0.06986 0.05448  61  TYR A CD2 
449  C CE1 . TYR A 54  ? 0.45054 0.20174 0.33732 -0.05763 -0.10675 0.04050  61  TYR A CE1 
450  C CE2 . TYR A 54  ? 0.47159 0.34004 0.42431 -0.07729 -0.08827 0.07605  61  TYR A CE2 
451  C CZ  . TYR A 54  ? 0.45594 0.25045 0.37019 -0.08110 -0.10995 0.06766  61  TYR A CZ  
452  O OH  . TYR A 54  ? 0.52056 0.28167 0.41767 -0.10427 -0.13504 0.09001  61  TYR A OH  
453  N N   . GLU A 55  ? 0.30023 0.22202 0.27313 -0.00223 -0.04133 0.01315  62  GLU A N   
454  C CA  . GLU A 55  ? 0.32602 0.25017 0.28232 0.00642  -0.04199 0.01943  62  GLU A CA  
455  C C   . GLU A 55  ? 0.36186 0.26596 0.31530 0.01221  -0.05381 0.01297  62  GLU A C   
456  O O   . GLU A 55  ? 0.39953 0.29407 0.33948 0.01508  -0.05859 0.01919  62  GLU A O   
457  C CB  . GLU A 55  ? 0.36694 0.30337 0.30431 0.02165  -0.03458 0.01902  62  GLU A CB  
458  C CG  . GLU A 55  ? 0.38352 0.35811 0.32770 0.02158  -0.01975 0.03837  62  GLU A CG  
459  C CD  . GLU A 55  ? 0.51881 0.50514 0.42834 0.05269  -0.00670 0.04489  62  GLU A CD  
460  O OE1 . GLU A 55  ? 0.51773 0.46307 0.38711 0.07121  -0.01563 0.02694  62  GLU A OE1 
461  O OE2 . GLU A 55  ? 0.51240 0.54615 0.43015 0.06063  0.01000  0.07186  62  GLU A OE2 
462  N N   . SER A 56  ? 0.35167 0.25571 0.32244 0.01265  -0.05986 0.00646  63  SER A N   
463  C CA  . SER A 56  ? 0.34546 0.24512 0.32660 0.01424  -0.07487 0.01144  63  SER A CA  
464  C C   . SER A 56  ? 0.40146 0.30031 0.39289 0.01935  -0.07157 0.01875  63  SER A C   
465  O O   . SER A 56  ? 0.34963 0.25115 0.35070 0.02258  -0.08296 0.02836  63  SER A O   
466  C CB  . SER A 56  ? 0.33700 0.25183 0.34553 0.01017  -0.08322 0.01538  63  SER A CB  
467  O OG  . SER A 56  ? 0.35528 0.29100 0.38957 0.01641  -0.06780 0.01963  63  SER A OG  
468  N N   . LEU A 57  ? 0.34559 0.23336 0.32867 0.02097  -0.06061 0.01618  64  LEU A N   
469  C CA  . LEU A 57  ? 0.45694 0.32365 0.42989 0.03271  -0.06051 0.02112  64  LEU A CA  
470  C C   . LEU A 57  ? 0.46828 0.32109 0.42707 0.02935  -0.06929 0.02693  64  LEU A C   
471  O O   . LEU A 57  ? 0.48334 0.32682 0.44024 0.04264  -0.07254 0.03363  64  LEU A O   
472  C CB  . LEU A 57  ? 0.44417 0.27529 0.38905 0.03268  -0.05797 0.01587  64  LEU A CB  
473  C CG  . LEU A 57  ? 0.43849 0.27249 0.38527 0.04450  -0.04840 0.01024  64  LEU A CG  
474  C CD1 . LEU A 57  ? 0.48570 0.25966 0.38357 0.04743  -0.05508 0.00448  64  LEU A CD1 
475  C CD2 . LEU A 57  ? 0.44569 0.30906 0.41554 0.07135  -0.03826 0.02039  64  LEU A CD2 
476  N N   . THR A 58  ? 0.44341 0.29857 0.39074 0.01658  -0.07083 0.02815  65  THR A N   
477  C CA  . THR A 58  ? 0.48447 0.33010 0.41548 0.01541  -0.07690 0.03678  65  THR A CA  
478  C C   . THR A 58  ? 0.58149 0.43459 0.50317 0.02104  -0.08311 0.03596  65  THR A C   
479  O O   . THR A 58  ? 0.58022 0.42202 0.48359 0.02463  -0.08953 0.04251  65  THR A O   
480  C CB  . THR A 58  ? 0.73093 0.57500 0.64950 0.00094  -0.07433 0.04962  65  THR A CB  
481  O OG1 . THR A 58  ? 0.64381 0.51877 0.56776 -0.00160 -0.06394 0.05265  65  THR A OG1 
482  C CG2 . THR A 58  ? 0.53638 0.34653 0.44620 -0.00946 -0.08233 0.05165  65  THR A CG2 
483  N N   . ASP A 59  ? 0.59032 0.42366 0.39550 0.14837  -0.01057 0.08853  66  ASP A N   
484  C CA  . ASP A 59  ? 0.56341 0.43910 0.38017 0.14148  -0.03011 0.08871  66  ASP A CA  
485  C C   . ASP A 59  ? 0.45773 0.37765 0.31111 0.13932  -0.04159 0.08483  66  ASP A C   
486  O O   . ASP A 59  ? 0.42590 0.35293 0.28969 0.12189  -0.04408 0.06823  66  ASP A O   
487  C CB  . ASP A 59  ? 0.53759 0.40357 0.33711 0.11954  -0.03181 0.07500  66  ASP A CB  
488  C CG  . ASP A 59  ? 0.68831 0.58452 0.48623 0.11335  -0.04994 0.07367  66  ASP A CG  
489  O OD1 . ASP A 59  ? 0.59628 0.52320 0.40727 0.12192  -0.06493 0.08374  66  ASP A OD1 
490  O OD2 . ASP A 59  ? 0.61820 0.50667 0.39984 0.09960  -0.04904 0.06359  66  ASP A OD2 
491  N N   . PRO A 60  ? 0.55174 0.50502 0.42711 0.15660  -0.04901 0.10232  67  PRO A N   
492  C CA  . PRO A 60  ? 0.42162 0.41993 0.33546 0.15289  -0.05934 0.10192  67  PRO A CA  
493  C C   . PRO A 60  ? 0.44711 0.46969 0.36497 0.12846  -0.08007 0.08920  67  PRO A C   
494  O O   . PRO A 60  ? 0.42527 0.47065 0.36812 0.11792  -0.08549 0.08181  67  PRO A O   
495  C CB  . PRO A 60  ? 0.47966 0.51438 0.41646 0.17669  -0.06423 0.12932  67  PRO A CB  
496  C CG  . PRO A 60  ? 0.77032 0.77419 0.67874 0.19256  -0.05515 0.14137  67  PRO A CG  
497  C CD  . PRO A 60  ? 0.61343 0.57148 0.48119 0.17811  -0.05114 0.12566  67  PRO A CD  
498  N N   . SER A 61  ? 0.50092 0.51415 0.39029 0.11970  -0.09031 0.08649  68  SER A N   
499  C CA  . SER A 61  ? 0.42744 0.45260 0.30978 0.09812  -0.10808 0.07351  68  SER A CA  
500  C C   . SER A 61  ? 0.49595 0.50176 0.37657 0.08324  -0.09827 0.05141  68  SER A C   
501  O O   . SER A 61  ? 0.40537 0.41838 0.28373 0.06729  -0.10993 0.03994  68  SER A O   
502  C CB  . SER A 61  ? 0.49044 0.50113 0.33336 0.09485  -0.11710 0.07517  68  SER A CB  
503  O OG  . SER A 61  ? 0.52225 0.49317 0.33749 0.09538  -0.09838 0.06706  68  SER A OG  
504  N N   . LYS A 62  ? 0.37291 0.35247 0.25215 0.08750  -0.07789 0.04625  69  LYS A N   
505  C CA  . LYS A 62  ? 0.37895 0.34734 0.26218 0.07435  -0.06975 0.02906  69  LYS A CA  
506  C C   . LYS A 62  ? 0.38143 0.37533 0.29501 0.06845  -0.07652 0.02438  69  LYS A C   
507  O O   . LYS A 62  ? 0.34548 0.33553 0.26151 0.05621  -0.07505 0.01066  69  LYS A O   
508  C CB  . LYS A 62  ? 0.44719 0.38603 0.32450 0.07759  -0.05047 0.02770  69  LYS A CB  
509  C CG  . LYS A 62  ? 0.57253 0.48350 0.42012 0.07847  -0.04234 0.03204  69  LYS A CG  
510  C CD  . LYS A 62  ? 0.53827 0.43858 0.37718 0.06333  -0.03543 0.02110  69  LYS A CD  
511  C CE  . LYS A 62  ? 0.55584 0.43518 0.36760 0.06269  -0.02757 0.02791  69  LYS A CE  
512  N NZ  . LYS A 62  ? 0.60099 0.47930 0.41097 0.04951  -0.01941 0.02115  69  LYS A NZ  
513  N N   . LEU A 63  ? 0.32440 0.34606 0.26262 0.07792  -0.08267 0.03775  70  LEU A N   
514  C CA  . LEU A 63  ? 0.30089 0.35103 0.27055 0.07164  -0.08887 0.03679  70  LEU A CA  
515  C C   . LEU A 63  ? 0.31916 0.39918 0.29574 0.05849  -0.11303 0.04037  70  LEU A C   
516  O O   . LEU A 63  ? 0.34022 0.44978 0.34614 0.05171  -0.12100 0.04437  70  LEU A O   
517  C CB  . LEU A 63  ? 0.36597 0.43122 0.36165 0.09018  -0.07783 0.05153  70  LEU A CB  
518  C CG  . LEU A 63  ? 0.36018 0.38741 0.34179 0.10067  -0.05472 0.04669  70  LEU A CG  
519  C CD1 . LEU A 63  ? 0.39681 0.43361 0.39761 0.12146  -0.04153 0.06075  70  LEU A CD1 
520  C CD2 . LEU A 63  ? 0.35005 0.35938 0.32613 0.08374  -0.05020 0.02729  70  LEU A CD2 
521  N N   . ASP A 64  ? 0.32540 0.39620 0.27247 0.05281  -0.12529 0.03945  71  ASP A N   
522  C CA  . ASP A 64  ? 0.36147 0.45166 0.30464 0.03558  -0.15083 0.04062  71  ASP A CA  
523  C C   . ASP A 64  ? 0.36971 0.44912 0.31074 0.01611  -0.15425 0.02297  71  ASP A C   
524  O O   . ASP A 64  ? 0.39344 0.49155 0.34187 -0.00108 -0.17442 0.02488  71  ASP A O   
525  C CB  . ASP A 64  ? 0.40835 0.47973 0.30837 0.03308  -0.16133 0.04023  71  ASP A CB  
526  C CG  . ASP A 64  ? 0.53428 0.62388 0.43800 0.05018  -0.16493 0.06227  71  ASP A CG  
527  O OD1 . ASP A 64  ? 0.52573 0.64598 0.46740 0.06433  -0.16082 0.07925  71  ASP A OD1 
528  O OD2 . ASP A 64  ? 0.56604 0.63800 0.43290 0.05145  -0.17026 0.06382  71  ASP A OD2 
529  N N   . SER A 65  ? 0.34577 0.39542 0.27679 0.01771  -0.13543 0.00755  72  SER A N   
530  C CA  . SER A 65  ? 0.36185 0.39838 0.29178 0.00429  -0.13391 -0.00764 72  SER A CA  
531  C C   . SER A 65  ? 0.42083 0.48093 0.39169 0.00364  -0.12950 -0.00389 72  SER A C   
532  O O   . SER A 65  ? 0.43700 0.48582 0.40955 -0.00523 -0.12554 -0.01498 72  SER A O   
533  C CB  . SER A 65  ? 0.41607 0.41839 0.32281 0.00885  -0.11494 -0.02100 72  SER A CB  
534  O OG  . SER A 65  ? 0.33348 0.33449 0.24957 0.02279  -0.09859 -0.01524 72  SER A OG  
535  N N   . GLY A 66  ? 0.32874 0.41952 0.33049 0.01510  -0.12796 0.01269  73  GLY A N   
536  C CA  . GLY A 66  ? 0.38663 0.50014 0.42493 0.01717  -0.12112 0.01843  73  GLY A CA  
537  C C   . GLY A 66  ? 0.33956 0.45962 0.39348 0.04003  -0.10336 0.03029  73  GLY A C   
538  O O   . GLY A 66  ? 0.27879 0.36752 0.31358 0.04916  -0.08723 0.02277  73  GLY A O   
539  N N   . LYS A 67  ? 0.29560 0.45487 0.38267 0.04930  -0.10553 0.05019  74  LYS A N   
540  C CA  . LYS A 67  ? 0.23505 0.39475 0.33129 0.07543  -0.08574 0.06302  74  LYS A CA  
541  C C   . LYS A 67  ? 0.25781 0.40580 0.36222 0.08094  -0.06607 0.05745  74  LYS A C   
542  O O   . LYS A 67  ? 0.32804 0.45001 0.41890 0.09940  -0.04616 0.05854  74  LYS A O   
543  C CB  . LYS A 67  ? 0.24233 0.45221 0.37213 0.08840  -0.09286 0.09075  74  LYS A CB  
544  C CG  . LYS A 67  ? 0.49247 0.71797 0.61368 0.08358  -0.11466 0.09998  74  LYS A CG  
545  C CD  . LYS A 67  ? 0.74929 0.98321 0.87600 0.10947  -0.10467 0.12019  74  LYS A CD  
546  C CE  . LYS A 67  ? 0.71157 0.94238 0.81537 0.10558  -0.12203 0.12393  74  LYS A CE  
547  N NZ  . LYS A 67  ? 0.80196 0.98842 0.86599 0.11993  -0.11086 0.11806  74  LYS A NZ  
548  N N   . GLU A 68  ? 0.21150 0.37326 0.33273 0.06474  -0.07126 0.05164  75  GLU A N   
549  C CA  . GLU A 68  ? 0.23165 0.38629 0.36094 0.06999  -0.05362 0.04885  75  GLU A CA  
550  C C   . GLU A 68  ? 0.23765 0.34370 0.33291 0.06594  -0.04331 0.02825  75  GLU A C   
551  O O   . GLU A 68  ? 0.30004 0.39057 0.37952 0.04993  -0.05281 0.01407  75  GLU A O   
552  C CB  . GLU A 68  ? 0.30230 0.48736 0.46029 0.05273  -0.06302 0.05122  75  GLU A CB  
553  C CG  . GLU A 68  ? 0.39378 0.63520 0.59521 0.05719  -0.06843 0.07684  75  GLU A CG  
554  C CD  . GLU A 68  ? 0.88434 1.15239 1.09236 0.04837  -0.09190 0.08698  75  GLU A CD  
555  O OE1 . GLU A 68  ? 0.83388 1.09222 1.02680 0.02369  -0.11217 0.07477  75  GLU A OE1 
556  O OE2 . GLU A 68  ? 0.85094 1.13583 1.06784 0.06485  -0.08686 0.10296  75  GLU A OE2 
557  N N   . LEU A 69  ? 0.21344 0.29557 0.29620 0.08041  -0.02367 0.02806  76  LEU A N   
558  C CA  . LEU A 69  ? 0.21409 0.25315 0.26539 0.07463  -0.01530 0.01184  76  LEU A CA  
559  C C   . LEU A 69  ? 0.20804 0.24561 0.26480 0.07288  -0.00581 0.00895  76  LEU A C   
560  O O   . LEU A 69  ? 0.22139 0.25375 0.27653 0.08939  0.01020  0.01715  76  LEU A O   
561  C CB  . LEU A 69  ? 0.29211 0.29420 0.31306 0.08914  -0.00243 0.01340  76  LEU A CB  
562  C CG  . LEU A 69  ? 0.36110 0.35894 0.37149 0.09162  -0.00986 0.01700  76  LEU A CG  
563  C CD1 . LEU A 69  ? 0.43905 0.38973 0.41334 0.10187  0.00399  0.01662  76  LEU A CD1 
564  C CD2 . LEU A 69  ? 0.29636 0.29742 0.30307 0.07161  -0.02497 0.00577  76  LEU A CD2 
565  N N   . HIS A 70  ? 0.20531 0.24515 0.26568 0.05514  -0.01390 -0.00154 77  HIS A N   
566  C CA  . HIS A 70  ? 0.21168 0.25562 0.28045 0.05266  -0.00698 -0.00193 77  HIS A CA  
567  C C   . HIS A 70  ? 0.19406 0.22436 0.25276 0.03597  -0.01302 -0.01523 77  HIS A C   
568  O O   . HIS A 70  ? 0.16934 0.19276 0.21977 0.02692  -0.02219 -0.02279 77  HIS A O   
569  C CB  . HIS A 70  ? 0.19954 0.28574 0.30566 0.05218  -0.01118 0.01117  77  HIS A CB  
570  C CG  . HIS A 70  ? 0.20742 0.31208 0.32771 0.03380  -0.03100 0.00831  77  HIS A CG  
571  N ND1 . HIS A 70  ? 0.30094 0.43832 0.44378 0.03125  -0.04350 0.02021  77  HIS A ND1 
572  C CD2 . HIS A 70  ? 0.27068 0.36233 0.38185 0.01741  -0.04015 -0.00421 77  HIS A CD2 
573  C CE1 . HIS A 70  ? 0.25774 0.39510 0.39865 0.01176  -0.06046 0.01280  77  HIS A CE1 
574  N NE2 . HIS A 70  ? 0.26978 0.37793 0.39118 0.00511  -0.05690 -0.00208 77  HIS A NE2 
575  N N   . ILE A 71  ? 0.17276 0.20044 0.23215 0.03422  -0.00613 -0.01586 78  ILE A N   
576  C CA  . ILE A 71  ? 0.15978 0.17835 0.21254 0.02145  -0.01019 -0.02450 78  ILE A CA  
577  C C   . ILE A 71  ? 0.20646 0.24469 0.28115 0.01709  -0.01027 -0.01943 78  ILE A C   
578  O O   . ILE A 71  ? 0.17082 0.21674 0.25253 0.02533  0.00048  -0.01106 78  ILE A O   
579  C CB  . ILE A 71  ? 0.22584 0.21503 0.24917 0.02147  -0.00247 -0.02954 78  ILE A CB  
580  C CG1 . ILE A 71  ? 0.24320 0.20880 0.24248 0.02324  -0.00183 -0.03286 78  ILE A CG1 
581  C CG2 . ILE A 71  ? 0.24250 0.23081 0.26441 0.00913  -0.00841 -0.03452 78  ILE A CG2 
582  C CD1 . ILE A 71  ? 0.25836 0.18933 0.22230 0.01862  0.00320  -0.03745 78  ILE A CD1 
583  N N   . ASN A 72  ? 0.17404 0.21703 0.25671 0.00507  -0.02041 -0.02357 79  ASN A N   
584  C CA  . ASN A 72  ? 0.14932 0.20380 0.24842 -0.00219 -0.02118 -0.01919 79  ASN A CA  
585  C C   . ASN A 72  ? 0.20545 0.24318 0.29185 -0.00733 -0.02041 -0.02512 79  ASN A C   
586  O O   . ASN A 72  ? 0.18684 0.21235 0.26094 -0.00955 -0.02500 -0.03217 79  ASN A O   
587  C CB  . ASN A 72  ? 0.13460 0.20308 0.24988 -0.01335 -0.03420 -0.01723 79  ASN A CB  
588  C CG  . ASN A 72  ? 0.20772 0.30223 0.34152 -0.00986 -0.03778 -0.00692 79  ASN A CG  
589  O OD1 . ASN A 72  ? 0.17839 0.28755 0.32297 0.00242  -0.02671 0.00326  79  ASN A OD1 
590  N ND2 . ASN A 72  ? 0.21332 0.31319 0.34897 -0.01966 -0.05282 -0.00804 79  ASN A ND2 
591  N N   . LEU A 73  ? 0.15865 0.19877 0.24959 -0.00799 -0.01379 -0.01980 80  LEU A N   
592  C CA  . LEU A 73  ? 0.14263 0.17055 0.22422 -0.01200 -0.01341 -0.02181 80  LEU A CA  
593  C C   . LEU A 73  ? 0.18053 0.21301 0.27722 -0.02067 -0.01632 -0.01735 80  LEU A C   
594  O O   . LEU A 73  ? 0.14516 0.19202 0.25759 -0.02263 -0.01177 -0.00836 80  LEU A O   
595  C CB  . LEU A 73  ? 0.17152 0.19182 0.23788 -0.00677 -0.00365 -0.01892 80  LEU A CB  
596  C CG  . LEU A 73  ? 0.22090 0.22774 0.26475 -0.00078 -0.00010 -0.02304 80  LEU A CG  
597  C CD1 . LEU A 73  ? 0.23259 0.22360 0.25209 0.00243  0.00915  -0.02096 80  LEU A CD1 
598  C CD2 . LEU A 73  ? 0.21029 0.20982 0.24449 -0.00583 -0.00939 -0.02976 80  LEU A CD2 
599  N N   . ILE A 74  ? 0.16079 0.17926 0.25124 -0.02546 -0.02244 -0.02222 81  ILE A N   
600  C CA  . ILE A 74  ? 0.17139 0.18308 0.26827 -0.03592 -0.02649 -0.01975 81  ILE A CA  
601  C C   . ILE A 74  ? 0.20417 0.19691 0.28999 -0.03428 -0.02270 -0.01874 81  ILE A C   
602  O O   . ILE A 74  ? 0.20937 0.18516 0.28180 -0.02994 -0.02413 -0.02384 81  ILE A O   
603  C CB  . ILE A 74  ? 0.18281 0.18531 0.27490 -0.04322 -0.03718 -0.02630 81  ILE A CB  
604  C CG1 . ILE A 74  ? 0.18903 0.21323 0.29169 -0.04233 -0.04172 -0.02532 81  ILE A CG1 
605  C CG2 . ILE A 74  ? 0.19192 0.18166 0.28536 -0.05881 -0.04321 -0.02368 81  ILE A CG2 
606  C CD1 . ILE A 74  ? 0.23044 0.24626 0.32385 -0.04975 -0.05390 -0.03134 81  ILE A CD1 
607  N N   . PRO A 75  ? 0.24212 0.23773 0.33274 -0.03556 -0.01637 -0.01036 82  PRO A N   
608  C CA  . PRO A 75  ? 0.22291 0.20001 0.30326 -0.03356 -0.01318 -0.00692 82  PRO A CA  
609  C C   . PRO A 75  ? 0.22846 0.18332 0.30683 -0.04441 -0.01643 -0.00636 82  PRO A C   
610  O O   . PRO A 75  ? 0.24406 0.20507 0.33447 -0.05823 -0.02077 -0.00381 82  PRO A O   
611  C CB  . PRO A 75  ? 0.26835 0.25600 0.35107 -0.03153 -0.00501 0.00246  82  PRO A CB  
612  C CG  . PRO A 75  ? 0.27263 0.28052 0.37248 -0.03657 -0.00240 0.00642  82  PRO A CG  
613  C CD  . PRO A 75  ? 0.26071 0.27658 0.36625 -0.03740 -0.01011 -0.00145 82  PRO A CD  
614  N N   . ASN A 76  ? 0.24924 0.17701 0.31095 -0.03835 -0.01433 -0.00730 83  ASN A N   
615  C CA  . ASN A 76  ? 0.29069 0.18294 0.33935 -0.04763 -0.01565 -0.00759 83  ASN A CA  
616  C C   . ASN A 76  ? 0.30851 0.18036 0.34558 -0.03687 -0.00688 0.00041  83  ASN A C   
617  O O   . ASN A 76  ? 0.34731 0.20930 0.37278 -0.02041 -0.00261 -0.00012 83  ASN A O   
618  C CB  . ASN A 76  ? 0.32151 0.18807 0.35080 -0.04813 -0.02099 -0.01910 83  ASN A CB  
619  C CG  . ASN A 76  ? 0.47964 0.30067 0.48683 -0.06265 -0.02440 -0.02149 83  ASN A CG  
620  O OD1 . ASN A 76  ? 0.47704 0.26951 0.47215 -0.06090 -0.01761 -0.01563 83  ASN A OD1 
621  N ND2 . ASN A 76  ? 0.51000 0.32111 0.50850 -0.07850 -0.03595 -0.02948 83  ASN A ND2 
622  N N   . LYS A 77  ? 0.34692 0.21505 0.38874 -0.04528 -0.00345 0.01026  84  LYS A N   
623  C CA  . LYS A 77  ? 0.37005 0.22120 0.40118 -0.03417 0.00490  0.02044  84  LYS A CA  
624  C C   . LYS A 77  ? 0.44875 0.24887 0.45401 -0.03022 0.00835  0.01884  84  LYS A C   
625  O O   . LYS A 77  ? 0.44926 0.23518 0.44349 -0.01233 0.01632  0.02671  84  LYS A O   
626  C CB  . LYS A 77  ? 0.38392 0.24347 0.42472 -0.04406 0.00915  0.03254  84  LYS A CB  
627  C CG  . LYS A 77  ? 0.46606 0.36613 0.52098 -0.03998 0.01147  0.03686  84  LYS A CG  
628  C CD  . LYS A 77  ? 0.46090 0.36543 0.52132 -0.04758 0.01909  0.05034  84  LYS A CD  
629  C CE  . LYS A 77  ? 0.48650 0.42286 0.55217 -0.04200 0.02424  0.05387  84  LYS A CE  
630  N NZ  . LYS A 77  ? 0.50401 0.46478 0.58557 -0.04587 0.02135  0.04629  84  LYS A NZ  
631  N N   . GLN A 78  ? 0.47339 0.24321 0.46558 -0.04627 0.00252  0.00986  85  GLN A N   
632  C CA  . GLN A 78  ? 0.57111 0.27925 0.52748 -0.04288 0.00718  0.00651  85  GLN A CA  
633  C C   . GLN A 78  ? 0.60690 0.30496 0.54733 -0.01782 0.01365  0.00064  85  GLN A C   
634  O O   . GLN A 78  ? 0.59327 0.25461 0.51064 0.00134  0.02548  0.00556  85  GLN A O   
635  C CB  . GLN A 78  ? 0.61400 0.28811 0.55379 -0.07118 -0.00357 -0.00218 85  GLN A CB  
636  C CG  . GLN A 78  ? 0.88454 0.56150 0.83825 -0.09796 -0.00838 0.00781  85  GLN A CG  
637  C CD  . GLN A 78  ? 0.94446 0.68992 0.94278 -0.10314 -0.01100 0.01612  85  GLN A CD  
638  O OE1 . GLN A 78  ? 0.98955 0.77398 1.00593 -0.10025 -0.01663 0.01021  85  GLN A OE1 
639  N NE2 . GLN A 78  ? 0.80979 0.56647 0.82249 -0.10882 -0.00484 0.03069  85  GLN A NE2 
640  N N   . ASP A 79  ? 0.45188 0.18257 0.40473 -0.01618 0.00770  -0.00776 86  ASP A N   
641  C CA  . ASP A 79  ? 0.54023 0.27218 0.48440 0.00665  0.01447  -0.01087 86  ASP A CA  
642  C C   . ASP A 79  ? 0.37405 0.15361 0.34401 0.02510  0.01899  0.00114  86  ASP A C   
643  O O   . ASP A 79  ? 0.43243 0.21802 0.40013 0.04578  0.02651  0.00454  86  ASP A O   
644  C CB  . ASP A 79  ? 0.54535 0.28904 0.48905 -0.00205 0.00543  -0.02424 86  ASP A CB  
645  C CG  . ASP A 79  ? 0.80927 0.50556 0.72240 -0.02188 -0.00230 -0.03590 86  ASP A CG  
646  O OD1 . ASP A 79  ? 0.72086 0.36599 0.60690 -0.02749 0.00114  -0.03512 86  ASP A OD1 
647  O OD2 . ASP A 79  ? 0.65104 0.35956 0.56497 -0.03329 -0.01295 -0.04513 86  ASP A OD2 
648  N N   . ARG A 80  ? 0.37666 0.18925 0.36890 0.01710  0.01454  0.00875  87  ARG A N   
649  C CA  . ARG A 80  ? 0.30976 0.16737 0.32210 0.02714  0.01388  0.01871  87  ARG A CA  
650  C C   . ARG A 80  ? 0.31392 0.20219 0.33682 0.02926  0.00909  0.01216  87  ARG A C   
651  O O   . ARG A 80  ? 0.29646 0.20675 0.32659 0.04331  0.01136  0.01995  87  ARG A O   
652  C CB  . ARG A 80  ? 0.36108 0.21440 0.36974 0.04838  0.02277  0.03468  87  ARG A CB  
653  C CG  . ARG A 80  ? 0.36409 0.25588 0.38837 0.04902  0.01819  0.04791  87  ARG A CG  
654  C CD  . ARG A 80  ? 0.51257 0.42540 0.54386 0.07023  0.02164  0.06548  87  ARG A CD  
655  N NE  . ARG A 80  ? 0.67756 0.55719 0.69562 0.08734  0.03333  0.07753  87  ARG A NE  
656  C CZ  . ARG A 80  ? 0.69461 0.57605 0.71399 0.11272  0.04292  0.09152  87  ARG A CZ  
657  N NH1 . ARG A 80  ? 0.52367 0.44430 0.56103 0.12225  0.04149  0.09676  87  ARG A NH1 
658  N NH2 . ARG A 80  ? 0.73201 0.57551 0.73476 0.12980  0.05549  0.10265  87  ARG A NH2 
659  N N   . THR A 81  ? 0.26469 0.15683 0.29021 0.01447  0.00210  0.00000  88  THR A N   
660  C CA  . THR A 81  ? 0.27839 0.19481 0.31128 0.01480  -0.00232 -0.00639 88  THR A CA  
661  C C   . THR A 81  ? 0.26047 0.20133 0.30599 0.00158  -0.00931 -0.00971 88  THR A C   
662  O O   . THR A 81  ? 0.27476 0.21095 0.32350 -0.00979 -0.01099 -0.01074 88  THR A O   
663  C CB  . THR A 81  ? 0.31170 0.20465 0.32936 0.01463  -0.00235 -0.01775 88  THR A CB  
664  O OG1 . THR A 81  ? 0.30774 0.17971 0.31822 -0.00245 -0.00846 -0.02516 88  THR A OG1 
665  C CG2 . THR A 81  ? 0.32570 0.19025 0.32467 0.03296  0.00882  -0.01448 88  THR A CG2 
666  N N   . LEU A 82  ? 0.22200 0.18791 0.27380 0.00354  -0.01220 -0.00975 89  LEU A N   
667  C CA  . LEU A 82  ? 0.20747 0.18837 0.26418 -0.00512 -0.01643 -0.01466 89  LEU A CA  
668  C C   . LEU A 82  ? 0.19605 0.18043 0.25162 -0.00434 -0.01930 -0.02235 89  LEU A C   
669  O O   . LEU A 82  ? 0.23655 0.22838 0.29118 0.00213  -0.01866 -0.02014 89  LEU A O   
670  C CB  . LEU A 82  ? 0.21229 0.20907 0.26744 -0.00580 -0.01750 -0.00868 89  LEU A CB  
671  C CG  . LEU A 82  ? 0.17521 0.17783 0.22722 -0.01139 -0.01851 -0.01391 89  LEU A CG  
672  C CD1 . LEU A 82  ? 0.22178 0.22133 0.28022 -0.01488 -0.01437 -0.01431 89  LEU A CD1 
673  C CD2 . LEU A 82  ? 0.19310 0.20002 0.23162 -0.01366 -0.02015 -0.00961 89  LEU A CD2 
674  N N   . THR A 83  ? 0.18777 0.16966 0.24500 -0.01084 -0.02243 -0.02894 90  THR A N   
675  C CA  . THR A 83  ? 0.20682 0.18972 0.26035 -0.01018 -0.02561 -0.03555 90  THR A CA  
676  C C   . THR A 83  ? 0.23494 0.23251 0.29323 -0.01275 -0.02732 -0.03636 90  THR A C   
677  O O   . THR A 83  ? 0.22311 0.22654 0.28902 -0.01636 -0.02677 -0.03413 90  THR A O   
678  C CB  . THR A 83  ? 0.24344 0.20881 0.29001 -0.01545 -0.02976 -0.04142 90  THR A CB  
679  O OG1 . THR A 83  ? 0.25687 0.19696 0.28980 -0.01128 -0.02577 -0.04169 90  THR A OG1 
680  C CG2 . THR A 83  ? 0.27832 0.24442 0.31745 -0.01405 -0.03331 -0.04728 90  THR A CG2 
681  N N   . ILE A 84  ? 0.16654 0.16885 0.21962 -0.00995 -0.02771 -0.03785 91  ILE A N   
682  C CA  . ILE A 84  ? 0.18225 0.18905 0.23268 -0.01070 -0.02795 -0.03905 91  ILE A CA  
683  C C   . ILE A 84  ? 0.23543 0.24090 0.28362 -0.00941 -0.03118 -0.04324 91  ILE A C   
684  O O   . ILE A 84  ? 0.24538 0.24855 0.28719 -0.00736 -0.03123 -0.04453 91  ILE A O   
685  C CB  . ILE A 84  ? 0.24285 0.25023 0.28345 -0.01237 -0.02738 -0.03676 91  ILE A CB  
686  C CG1 . ILE A 84  ? 0.32796 0.33529 0.36541 -0.01472 -0.02610 -0.03212 91  ILE A CG1 
687  C CG2 . ILE A 84  ? 0.20747 0.20785 0.23715 -0.01254 -0.02623 -0.03908 91  ILE A CG2 
688  C CD1 . ILE A 84  ? 0.39035 0.40552 0.43307 -0.01416 -0.02796 -0.02606 91  ILE A CD1 
689  N N   . VAL A 85  ? 0.17074 0.18060 0.22494 -0.01003 -0.03357 -0.04315 92  VAL A N   
690  C CA  . VAL A 85  ? 0.18917 0.19939 0.24023 -0.00951 -0.03891 -0.04545 92  VAL A CA  
691  C C   . VAL A 85  ? 0.26166 0.27584 0.31099 -0.00404 -0.03627 -0.04261 92  VAL A C   
692  O O   . VAL A 85  ? 0.21913 0.23833 0.27444 -0.00050 -0.03117 -0.03798 92  VAL A O   
693  C CB  . VAL A 85  ? 0.25022 0.26532 0.30975 -0.01616 -0.04688 -0.04451 92  VAL A CB  
694  C CG1 . VAL A 85  ? 0.24711 0.25848 0.29580 -0.01746 -0.05509 -0.04754 92  VAL A CG1 
695  C CG2 . VAL A 85  ? 0.26788 0.27116 0.32571 -0.02244 -0.04761 -0.04644 92  VAL A CG2 
696  N N   A ASP A 86  ? 0.20502 0.21373 0.24330 -0.00171 -0.03777 -0.04446 93  ASP A N   
697  N N   B ASP A 86  ? 0.20502 0.21373 0.24330 -0.00171 -0.03777 -0.04446 93  ASP A N   
698  C CA  A ASP A 86  ? 0.20836 0.21569 0.24176 0.00465  -0.03537 -0.04094 93  ASP A CA  
699  C CA  B ASP A 86  ? 0.20836 0.21569 0.24176 0.00465  -0.03537 -0.04094 93  ASP A CA  
700  C C   A ASP A 86  ? 0.26947 0.27886 0.29818 0.00601  -0.04215 -0.04079 93  ASP A C   
701  C C   B ASP A 86  ? 0.26947 0.27886 0.29818 0.00601  -0.04215 -0.04079 93  ASP A C   
702  O O   A ASP A 86  ? 0.23487 0.23971 0.25594 0.00203  -0.04647 -0.04534 93  ASP A O   
703  O O   B ASP A 86  ? 0.23487 0.23971 0.25594 0.00203  -0.04647 -0.04534 93  ASP A O   
704  C CB  A ASP A 86  ? 0.21835 0.20953 0.23536 0.00454  -0.02899 -0.04176 93  ASP A CB  
705  C CB  B ASP A 86  ? 0.21835 0.20953 0.23536 0.00454  -0.02899 -0.04176 93  ASP A CB  
706  C CG  A ASP A 86  ? 0.29766 0.28467 0.30587 -0.00011 -0.03063 -0.04369 93  ASP A CG  
707  C CG  B ASP A 86  ? 0.29766 0.28467 0.30587 -0.00011 -0.03063 -0.04369 93  ASP A CG  
708  O OD1 A ASP A 86  ? 0.28662 0.27186 0.28866 0.00266  -0.03233 -0.04319 93  ASP A OD1 
709  O OD1 B ASP A 86  ? 0.28662 0.27186 0.28866 0.00266  -0.03233 -0.04319 93  ASP A OD1 
710  O OD2 A ASP A 86  ? 0.28960 0.27780 0.29795 -0.00596 -0.02973 -0.04362 93  ASP A OD2 
711  O OD2 B ASP A 86  ? 0.28960 0.27780 0.29795 -0.00596 -0.02973 -0.04362 93  ASP A OD2 
712  N N   . THR A 87  ? 0.19546 0.20983 0.22582 0.01347  -0.04202 -0.03443 94  THR A N   
713  C CA  . THR A 87  ? 0.17349 0.19052 0.19712 0.01566  -0.04931 -0.03201 94  THR A CA  
714  C C   . THR A 87  ? 0.27477 0.27432 0.27978 0.02170  -0.04277 -0.03088 94  THR A C   
715  O O   . THR A 87  ? 0.23310 0.23365 0.23390 0.02966  -0.04401 -0.02408 94  THR A O   
716  C CB  . THR A 87  ? 0.21970 0.26055 0.26165 0.01984  -0.05591 -0.02157 94  THR A CB  
717  O OG1 . THR A 87  ? 0.20459 0.24959 0.25631 0.03158  -0.04458 -0.01357 94  THR A OG1 
718  C CG2 . THR A 87  ? 0.21987 0.27660 0.27742 0.00762  -0.06625 -0.02218 94  THR A CG2 
719  N N   . GLY A 88  ? 0.25752 0.24188 0.25178 0.01699  -0.03635 -0.03553 95  GLY A N   
720  C CA  . GLY A 88  ? 0.26535 0.23120 0.24131 0.01772  -0.03090 -0.03359 95  GLY A CA  
721  C C   . GLY A 88  ? 0.21955 0.18463 0.18508 0.01666  -0.03366 -0.03332 95  GLY A C   
722  O O   . GLY A 88  ? 0.25831 0.23280 0.22488 0.01777  -0.04061 -0.03476 95  GLY A O   
723  N N   . ILE A 89  ? 0.25668 0.20772 0.20845 0.01286  -0.02809 -0.03095 96  ILE A N   
724  C CA  . ILE A 89  ? 0.25679 0.20541 0.19600 0.01368  -0.02748 -0.02811 96  ILE A CA  
725  C C   . ILE A 89  ? 0.29858 0.25827 0.24058 0.01142  -0.02726 -0.03177 96  ILE A C   
726  O O   . ILE A 89  ? 0.28834 0.24544 0.21639 0.01530  -0.02686 -0.03097 96  ILE A O   
727  C CB  . ILE A 89  ? 0.28245 0.21357 0.20782 0.00785  -0.02076 -0.02229 96  ILE A CB  
728  C CG1 . ILE A 89  ? 0.32825 0.25395 0.23794 0.01162  -0.01868 -0.01658 96  ILE A CG1 
729  C CG2 . ILE A 89  ? 0.26037 0.19753 0.19351 -0.00554 -0.01796 -0.02184 96  ILE A CG2 
730  C CD1 . ILE A 89  ? 0.35835 0.26076 0.25137 0.00644  -0.01280 -0.00910 96  ILE A CD1 
731  N N   . GLY A 90  ? 0.26873 0.23747 0.22458 0.00726  -0.02635 -0.03514 97  GLY A N   
732  C CA  . GLY A 90  ? 0.27710 0.25187 0.23326 0.00911  -0.02296 -0.03712 97  GLY A CA  
733  C C   . GLY A 90  ? 0.26032 0.24075 0.21497 0.00790  -0.01329 -0.02920 97  GLY A C   
734  O O   . GLY A 90  ? 0.25883 0.23840 0.21304 0.00123  -0.01137 -0.02257 97  GLY A O   
735  N N   . MET A 91  ? 0.24252 0.22757 0.19534 0.01459  -0.00603 -0.02851 98  MET A N   
736  C CA  . MET A 91  ? 0.22417 0.22288 0.18147 0.01622  0.00595  -0.01716 98  MET A CA  
737  C C   . MET A 91  ? 0.24956 0.23740 0.18421 0.02981  0.01599  -0.01779 98  MET A C   
738  O O   . MET A 91  ? 0.29699 0.26818 0.21613 0.03733  0.01493  -0.02726 98  MET A O   
739  C CB  . MET A 91  ? 0.24943 0.27121 0.23179 0.01432  0.00985  -0.00986 98  MET A CB  
740  C CG  . MET A 91  ? 0.32038 0.35207 0.31923 -0.00151 0.00093  -0.00670 98  MET A CG  
741  S SD  . MET A 91  ? 0.26404 0.32362 0.28973 -0.00293 0.00160  0.00190  98  MET A SD  
742  C CE  . MET A 91  ? 0.22825 0.26958 0.24807 0.00584  -0.00269 -0.01268 98  MET A CE  
743  N N   . THR A 92  ? 0.26401 0.25795 0.19319 0.03198  0.02645  -0.00718 99  THR A N   
744  C CA  . THR A 92  ? 0.29321 0.27710 0.19831 0.04723  0.04093  -0.00506 99  THR A CA  
745  C C   . THR A 92  ? 0.29436 0.29466 0.21403 0.05900  0.05616  0.00305  99  THR A C   
746  O O   . THR A 92  ? 0.27637 0.30257 0.22882 0.05303  0.05404  0.01000  99  THR A O   
747  C CB  . THR A 92  ? 0.35085 0.33930 0.24789 0.04636  0.04963  0.00680  99  THR A CB  
748  O OG1 . THR A 92  ? 0.31033 0.33225 0.24099 0.03731  0.05583  0.02369  99  THR A OG1 
749  C CG2 . THR A 92  ? 0.33469 0.30694 0.21870 0.03690  0.03575  0.00180  99  THR A CG2 
750  N N   . LYS A 93  ? 0.28908 0.26385 0.23011 0.05710  -0.05451 0.01485  100 LYS A N   
751  C CA  . LYS A 93  ? 0.29287 0.25970 0.22667 0.04873  -0.03852 0.01005  100 LYS A CA  
752  C C   . LYS A 93  ? 0.27492 0.23109 0.21111 0.04912  -0.02511 0.01686  100 LYS A C   
753  O O   . LYS A 93  ? 0.28188 0.24280 0.23296 0.04692  -0.01465 0.01202  100 LYS A O   
754  C CB  . LYS A 93  ? 0.33341 0.29128 0.23376 0.04368  -0.03778 0.00750  100 LYS A CB  
755  C CG  . LYS A 93  ? 0.31992 0.27030 0.21415 0.03979  -0.02180 -0.00038 100 LYS A CG  
756  C CD  . LYS A 93  ? 0.40178 0.34105 0.26033 0.03569  -0.01918 -0.00521 100 LYS A CD  
757  C CE  . LYS A 93  ? 0.48607 0.41637 0.33998 0.03650  -0.00461 -0.01593 100 LYS A CE  
758  N NZ  . LYS A 93  ? 0.47220 0.39306 0.29405 0.03574  0.00560  -0.01944 100 LYS A NZ  
759  N N   . ALA A 94  ? 0.32406 0.26495 0.24338 0.05086  -0.02597 0.02811  101 ALA A N   
760  C CA  . ALA A 94  ? 0.36407 0.29542 0.28411 0.04586  -0.01227 0.03333  101 ALA A CA  
761  C C   . ALA A 94  ? 0.33707 0.27567 0.28872 0.04756  -0.01071 0.03024  101 ALA A C   
762  O O   . ALA A 94  ? 0.34730 0.29271 0.31071 0.04143  0.00107  0.02718  101 ALA A O   
763  C CB  . ALA A 94  ? 0.39375 0.29796 0.28268 0.04445  -0.01372 0.04691  101 ALA A CB  
764  N N   . ASP A 95  ? 0.30822 0.24942 0.27452 0.05612  -0.02263 0.02950  102 ASP A N   
765  C CA  . ASP A 95  ? 0.28485 0.23352 0.27900 0.05724  -0.02002 0.02425  102 ASP A CA  
766  C C   . ASP A 95  ? 0.25998 0.22744 0.27050 0.05149  -0.01344 0.01457  102 ASP A C   
767  O O   . ASP A 95  ? 0.26269 0.23348 0.28521 0.04724  -0.00560 0.01202  102 ASP A O   
768  C CB  . ASP A 95  ? 0.28813 0.24369 0.29767 0.06910  -0.03278 0.02180  102 ASP A CB  
769  C CG  . ASP A 95  ? 0.40224 0.33243 0.39599 0.08049  -0.04084 0.03215  102 ASP A CG  
770  O OD1 . ASP A 95  ? 0.47841 0.37982 0.45504 0.07548  -0.03260 0.03988  102 ASP A OD1 
771  O OD2 . ASP A 95  ? 0.42411 0.36315 0.42270 0.09468  -0.05590 0.03192  102 ASP A OD2 
772  N N   . LEU A 96  ? 0.27485 0.25166 0.28258 0.05085  -0.01758 0.00902  103 LEU A N   
773  C CA  . LEU A 96  ? 0.24562 0.22913 0.26010 0.04632  -0.01212 0.00144  103 LEU A CA  
774  C C   . LEU A 96  ? 0.25279 0.23383 0.26270 0.04563  -0.00176 0.00259  103 LEU A C   
775  O O   . LEU A 96  ? 0.25759 0.24413 0.27900 0.04500  0.00228  -0.00005 103 LEU A O   
776  C CB  . LEU A 96  ? 0.29561 0.27911 0.29794 0.04308  -0.01664 -0.00443 103 LEU A CB  
777  C CG  . LEU A 96  ? 0.31831 0.31615 0.33257 0.03912  -0.02521 -0.01108 103 LEU A CG  
778  C CD1 . LEU A 96  ? 0.28070 0.27436 0.27692 0.03086  -0.02772 -0.01800 103 LEU A CD1 
779  C CD2 . LEU A 96  ? 0.20983 0.21558 0.24351 0.03475  -0.02047 -0.01609 103 LEU A CD2 
780  N N   . ILE A 97  ? 0.27870 0.25511 0.27166 0.04590  0.00243  0.00568  104 ILE A N   
781  C CA  . ILE A 97  ? 0.27846 0.26229 0.27134 0.04634  0.01319  0.00406  104 ILE A CA  
782  C C   . ILE A 97  ? 0.28590 0.27903 0.29429 0.04136  0.01828  0.00664  104 ILE A C   
783  O O   . ILE A 97  ? 0.30057 0.30993 0.32200 0.04224  0.02309  0.00256  104 ILE A O   
784  C CB  . ILE A 97  ? 0.32430 0.30399 0.29460 0.04543  0.01893  0.00509  104 ILE A CB  
785  C CG1 . ILE A 97  ? 0.26973 0.23938 0.22271 0.04902  0.01494  -0.00084 104 ILE A CG1 
786  C CG2 . ILE A 97  ? 0.26832 0.26538 0.24415 0.04527  0.03227  0.00177  104 ILE A CG2 
787  C CD1 . ILE A 97  ? 0.34172 0.30373 0.26640 0.04641  0.01809  -0.00005 104 ILE A CD1 
788  N N   . ASN A 98  ? 0.21528 0.19672 0.22060 0.03655  0.01627  0.01288  105 ASN A N   
789  C CA  . ASN A 98  ? 0.26164 0.24364 0.27629 0.02836  0.02165  0.01427  105 ASN A CA  
790  C C   . ASN A 98  ? 0.24304 0.22862 0.27655 0.03016  0.01689  0.00970  105 ASN A C   
791  O O   . ASN A 98  ? 0.27987 0.25169 0.31555 0.02898  0.01471  0.01109  105 ASN A O   
792  C CB  . ASN A 98  ? 0.35356 0.30955 0.34856 0.02318  0.02217  0.02330  105 ASN A CB  
793  C CG  . ASN A 98  ? 0.61520 0.56757 0.60887 0.00794  0.03320  0.02428  105 ASN A CG  
794  O OD1 . ASN A 98  ? 0.69006 0.66885 0.70133 0.00100  0.04006  0.01703  105 ASN A OD1 
795  N ND2 . ASN A 98  ? 0.81950 0.73795 0.78998 0.00210  0.03428  0.03312  105 ASN A ND2 
796  N N   . ASN A 99  ? 0.25430 0.25520 0.29766 0.03397  0.01578  0.00392  106 ASN A N   
797  C CA  . ASN A 99  ? 0.22822 0.23410 0.28430 0.03326  0.01316  -0.00080 106 ASN A CA  
798  C C   . ASN A 99  ? 0.27285 0.26849 0.33236 0.03513  0.00808  -0.00193 106 ASN A C   
799  O O   . ASN A 99  ? 0.21515 0.20928 0.28334 0.03227  0.00904  -0.00537 106 ASN A O   
800  C CB  . ASN A 99  ? 0.25867 0.27446 0.32379 0.02449  0.01792  -0.00315 106 ASN A CB  
801  C CG  . ASN A 99  ? 0.21839 0.25740 0.28754 0.02364  0.02220  -0.00482 106 ASN A CG  
802  O OD1 . ASN A 99  ? 0.21976 0.26941 0.28968 0.03341  0.01931  -0.00675 106 ASN A OD1 
803  N ND2 . ASN A 99  ? 0.22420 0.27079 0.29514 0.01203  0.02962  -0.00485 106 ASN A ND2 
804  N N   . LEU A 100 ? 0.22055 0.21282 0.27416 0.03998  0.00282  -0.00108 107 LEU A N   
805  C CA  . LEU A 100 ? 0.25904 0.25345 0.32116 0.04295  -0.00297 -0.00462 107 LEU A CA  
806  C C   . LEU A 100 ? 0.27127 0.25706 0.33971 0.04743  -0.00406 -0.00320 107 LEU A C   
807  O O   . LEU A 100 ? 0.25900 0.25030 0.34163 0.04976  -0.00417 -0.00975 107 LEU A O   
808  C CB  . LEU A 100 ? 0.20250 0.20643 0.27259 0.03791  -0.00117 -0.01224 107 LEU A CB  
809  C CG  . LEU A 100 ? 0.33630 0.33625 0.39234 0.03493  -0.00035 -0.01242 107 LEU A CG  
810  C CD1 . LEU A 100 ? 0.46422 0.46244 0.51676 0.03330  0.00355  -0.01234 107 LEU A CD1 
811  C CD2 . LEU A 100 ? 0.30261 0.30507 0.35654 0.02874  -0.00247 -0.01833 107 LEU A CD2 
812  N N   . GLY A 101 ? 0.24262 0.21118 0.29704 0.04858  -0.00373 0.00500  108 GLY A N   
813  C CA  . GLY A 101 ? 0.27620 0.22377 0.32751 0.05468  -0.00570 0.00829  108 GLY A CA  
814  C C   . GLY A 101 ? 0.31063 0.24770 0.36683 0.04783  0.00244  0.00397  108 GLY A C   
815  O O   . GLY A 101 ? 0.33325 0.24833 0.38724 0.05474  0.00138  0.00378  108 GLY A O   
816  N N   . THR A 102 ? 0.25334 0.20428 0.31444 0.03565  0.00956  -0.00024 109 THR A N   
817  C CA  . THR A 102 ? 0.27735 0.22292 0.34179 0.02578  0.01638  -0.00621 109 THR A CA  
818  C C   . THR A 102 ? 0.28171 0.22062 0.33461 0.01119  0.02348  -0.00230 109 THR A C   
819  O O   . THR A 102 ? 0.29342 0.24057 0.33962 0.00883  0.02477  0.00346  109 THR A O   
820  C CB  . THR A 102 ? 0.23684 0.20710 0.31386 0.02142  0.01745  -0.01472 109 THR A CB  
821  O OG1 . THR A 102 ? 0.28826 0.27706 0.36390 0.01673  0.01783  -0.01220 109 THR A OG1 
822  C CG2 . THR A 102 ? 0.28619 0.26733 0.37244 0.03035  0.01311  -0.01884 109 THR A CG2 
823  N N   . ILE A 103 ? 0.27985 0.20527 0.33009 -0.00063 0.02950  -0.00742 110 ILE A N   
824  C CA  . ILE A 103 ? 0.24597 0.17588 0.29029 -0.02076 0.03772  -0.00790 110 ILE A CA  
825  C C   . ILE A 103 ? 0.27703 0.24663 0.33908 -0.02754 0.03717  -0.01701 110 ILE A C   
826  O O   . ILE A 103 ? 0.24857 0.22144 0.31218 -0.04253 0.04081  -0.02526 110 ILE A O   
827  C CB  . ILE A 103 ? 0.35779 0.24581 0.38359 -0.03364 0.04465  -0.00870 110 ILE A CB  
828  C CG1 . ILE A 103 ? 0.40035 0.27308 0.43052 -0.02911 0.04370  -0.01881 110 ILE A CG1 
829  C CG2 . ILE A 103 ? 0.41429 0.25973 0.41529 -0.02541 0.04352  0.00381  110 ILE A CG2 
830  C CD1 . ILE A 103 ? 0.52524 0.35568 0.53529 -0.04607 0.05235  -0.02347 110 ILE A CD1 
831  N N   A ALA A 104 ? 0.25809 0.25522 0.32994 -0.01634 0.03167  -0.01553 111 ALA A N   
832  N N   B ALA A 104 ? 0.25787 0.25502 0.32970 -0.01633 0.03168  -0.01549 111 ALA A N   
833  C CA  A ALA A 104 ? 0.24169 0.26814 0.32471 -0.01598 0.02742  -0.02193 111 ALA A CA  
834  C CA  B ALA A 104 ? 0.24327 0.26940 0.32623 -0.01556 0.02729  -0.02184 111 ALA A CA  
835  C C   A ALA A 104 ? 0.20713 0.26395 0.29823 -0.03007 0.02997  -0.02721 111 ALA A C   
836  C C   B ALA A 104 ? 0.20866 0.26583 0.29991 -0.02913 0.02954  -0.02711 111 ALA A C   
837  O O   A ALA A 104 ? 0.22313 0.29910 0.31982 -0.03447 0.02570  -0.03416 111 ALA A O   
838  O O   B ALA A 104 ? 0.22425 0.30172 0.32128 -0.03202 0.02472  -0.03359 111 ALA A O   
839  C CB  A ALA A 104 ? 0.22180 0.25977 0.30639 -0.00011 0.02132  -0.01797 111 ALA A CB  
840  C CB  B ALA A 104 ? 0.22122 0.25821 0.30555 0.00031  0.02122  -0.01782 111 ALA A CB  
841  N N   A LYS A 105 ? 0.19924 0.26458 0.29065 -0.03859 0.03686  -0.02499 112 LYS A N   
842  N N   B LYS A 105 ? 0.20294 0.26800 0.29439 -0.03853 0.03662  -0.02519 112 LYS A N   
843  C CA  A LYS A 105 ? 0.24847 0.35430 0.35341 -0.05353 0.03999  -0.03258 112 LYS A CA  
844  C CA  B LYS A 105 ? 0.24813 0.35298 0.35286 -0.05390 0.03969  -0.03291 112 LYS A CA  
845  C C   A LYS A 105 ? 0.33804 0.43750 0.44040 -0.07579 0.04275  -0.04139 112 LYS A C   
846  C C   B LYS A 105 ? 0.33130 0.42596 0.43185 -0.07672 0.04332  -0.04125 112 LYS A C   
847  O O   A LYS A 105 ? 0.25539 0.38869 0.36948 -0.08156 0.03699  -0.05019 112 LYS A O   
848  O O   B LYS A 105 ? 0.25373 0.37716 0.36415 -0.08295 0.03765  -0.05021 112 LYS A O   
849  C CB  A LYS A 105 ? 0.23602 0.35262 0.34040 -0.06252 0.05068  -0.03009 112 LYS A CB  
850  C CB  B LYS A 105 ? 0.23755 0.35644 0.34325 -0.06164 0.04978  -0.03057 112 LYS A CB  
851  C CG  A LYS A 105 ? 0.27149 0.44122 0.39565 -0.07986 0.05580  -0.04046 112 LYS A CG  
852  C CG  B LYS A 105 ? 0.37361 0.54680 0.50057 -0.05086 0.04751  -0.03501 112 LYS A CG  
853  C CD  A LYS A 105 ? 0.30922 0.49490 0.43334 -0.08786 0.06900  -0.03917 112 LYS A CD  
854  C CD  B LYS A 105 ? 0.27070 0.47611 0.40624 -0.06950 0.06103  -0.04007 112 LYS A CD  
855  C CE  A LYS A 105 ? 0.53629 0.79123 0.68901 -0.10091 0.07392  -0.05218 112 LYS A CE  
856  C CE  B LYS A 105 ? 0.29590 0.51001 0.43407 -0.10162 0.06752  -0.04853 112 LYS A CE  
857  N NZ  A LYS A 105 ? 0.42562 0.69301 0.58377 -0.12988 0.07533  -0.06218 112 LYS A NZ  
858  N NZ  B LYS A 105 ? 0.43903 0.72602 0.60921 -0.10802 0.06503  -0.06216 112 LYS A NZ  
859  N N   A SER A 106 ? 0.25955 0.31271 0.34324 -0.08785 0.05070  -0.03946 113 SER A N   
860  N N   B SER A 106 ? 0.27154 0.32132 0.35340 -0.08907 0.05204  -0.03856 113 SER A N   
861  C CA  A SER A 106 ? 0.31373 0.35107 0.38964 -0.10986 0.05480  -0.04941 113 SER A CA  
862  C CA  B SER A 106 ? 0.32215 0.34995 0.39397 -0.11065 0.05677  -0.04755 113 SER A CA  
863  C C   A SER A 106 ? 0.28212 0.30908 0.35696 -0.09971 0.04740  -0.05507 113 SER A C   
864  C C   B SER A 106 ? 0.30131 0.31813 0.37254 -0.10040 0.04947  -0.05339 113 SER A C   
865  O O   A SER A 106 ? 0.32040 0.35776 0.39515 -0.11534 0.04670  -0.06670 113 SER A O   
866  O O   B SER A 106 ? 0.34523 0.36122 0.41275 -0.11728 0.05077  -0.06490 113 SER A O   
867  C CB  A SER A 106 ? 0.40172 0.38193 0.45148 -0.12367 0.06587  -0.04514 113 SER A CB  
868  C CB  B SER A 106 ? 0.40362 0.37244 0.44829 -0.12120 0.06703  -0.04155 113 SER A CB  
869  O OG  A SER A 106 ? 0.42439 0.35980 0.46098 -0.10102 0.06243  -0.03626 113 SER A OG  
870  O OG  B SER A 106 ? 0.42445 0.34976 0.45748 -0.09866 0.06245  -0.03505 113 SER A OG  
871  N N   A GLY A 107 ? 0.28463 0.29411 0.35781 -0.07610 0.04259  -0.04843 114 GLY A N   
872  N N   B GLY A 107 ? 0.28249 0.29208 0.35574 -0.07565 0.04296  -0.04709 114 GLY A N   
873  C CA  A GLY A 107 ? 0.32098 0.32684 0.39358 -0.06817 0.03798  -0.05472 114 GLY A CA  
874  C CA  B GLY A 107 ? 0.32805 0.33134 0.40022 -0.06804 0.03868  -0.05349 114 GLY A CA  
875  C C   A GLY A 107 ? 0.30380 0.35213 0.38470 -0.06955 0.02957  -0.05946 114 GLY A C   
876  C C   B GLY A 107 ? 0.30153 0.34590 0.38166 -0.07113 0.03088  -0.05958 114 GLY A C   
877  O O   A GLY A 107 ? 0.27637 0.32672 0.35123 -0.07824 0.02806  -0.06918 114 GLY A O   
878  O O   B GLY A 107 ? 0.30672 0.35115 0.38065 -0.08245 0.03054  -0.07010 114 GLY A O   
879  N N   A THR A 108 ? 0.22875 0.30912 0.32043 -0.05937 0.02342  -0.05288 115 THR A N   
880  N N   B THR A 108 ? 0.23417 0.31117 0.32473 -0.05962 0.02380  -0.05321 115 THR A N   
881  C CA  A THR A 108 ? 0.23833 0.35716 0.33544 -0.05606 0.01276  -0.05572 115 THR A CA  
882  C CA  B THR A 108 ? 0.22853 0.34245 0.32343 -0.05795 0.01344  -0.05690 115 THR A CA  
883  C C   A THR A 108 ? 0.29425 0.44259 0.39724 -0.07792 0.01171  -0.06702 115 THR A C   
884  C C   B THR A 108 ? 0.29254 0.43398 0.39278 -0.08053 0.01303  -0.06820 115 THR A C   
885  O O   A THR A 108 ? 0.27527 0.44028 0.37327 -0.08197 0.00328  -0.07356 115 THR A O   
886  O O   B THR A 108 ? 0.29091 0.44896 0.38611 -0.08583 0.00512  -0.07533 115 THR A O   
887  C CB  A THR A 108 ? 0.21100 0.35457 0.31827 -0.03793 0.00726  -0.04766 115 THR A CB  
888  C CB  B THR A 108 ? 0.22494 0.36516 0.32948 -0.03938 0.00661  -0.04880 115 THR A CB  
889  O OG1 A THR A 108 ? 0.21782 0.33299 0.31640 -0.02116 0.00764  -0.03897 115 THR A OG1 
890  O OG1 B THR A 108 ? 0.23883 0.35135 0.33523 -0.02260 0.00716  -0.04009 115 THR A OG1 
891  C CG2 A THR A 108 ? 0.23818 0.41855 0.34895 -0.02943 -0.00615 -0.04959 115 THR A CG2 
892  C CG2 B THR A 108 ? 0.27223 0.44577 0.37752 -0.03216 -0.00691 -0.05088 115 THR A CG2 
893  N N   A LYS A 109 ? 0.24588 0.40125 0.35671 -0.09480 0.02039  -0.06991 116 LYS A N   
894  N N   B LYS A 109 ? 0.25775 0.40440 0.36532 -0.09671 0.02174  -0.07049 116 LYS A N   
895  C CA  A LYS A 109 ? 0.24121 0.42744 0.35859 -0.12140 0.02099  -0.08287 116 LYS A CA  
896  C CA  B LYS A 109 ? 0.25243 0.42695 0.36549 -0.12417 0.02317  -0.08335 116 LYS A CA  
897  C C   A LYS A 109 ? 0.36433 0.52276 0.46323 -0.13714 0.02194  -0.09331 116 LYS A C   
898  C C   B LYS A 109 ? 0.35622 0.49684 0.44980 -0.14133 0.02647  -0.09382 116 LYS A C   
899  O O   A LYS A 109 ? 0.36021 0.55017 0.45999 -0.14769 0.01312  -0.10350 116 LYS A O   
900  O O   B LYS A 109 ? 0.30884 0.47624 0.40176 -0.15482 0.01945  -0.10521 116 LYS A O   
901  C CB  A LYS A 109 ? 0.26451 0.44883 0.38576 -0.14232 0.03486  -0.08396 116 LYS A CB  
902  C CB  B LYS A 109 ? 0.26993 0.44740 0.38876 -0.14286 0.03595  -0.08354 116 LYS A CB  
903  C CG  A LYS A 109 ? 0.42590 0.63665 0.55092 -0.17628 0.03910  -0.09836 116 LYS A CG  
904  C CG  B LYS A 109 ? 0.43989 0.61447 0.55195 -0.18023 0.04453  -0.09710 116 LYS A CG  
905  C CD  A LYS A 109 ? 0.46431 0.64681 0.57709 -0.19493 0.05567  -0.09513 116 LYS A CD  
906  C CD  B LYS A 109 ? 0.47021 0.64355 0.58002 -0.19549 0.05754  -0.09389 116 LYS A CD  
907  C CE  A LYS A 109 ? 0.62452 0.79625 0.72032 -0.22307 0.06170  -0.10536 116 LYS A CE  
908  C CE  B LYS A 109 ? 0.41634 0.65250 0.54340 -0.20427 0.05399  -0.10204 116 LYS A CE  
909  N NZ  A LYS A 109 ? 0.49664 0.73178 0.61003 -0.22655 0.05062  -0.11623 116 LYS A NZ  
910  N NZ  B LYS A 109 ? 0.42806 0.69432 0.55933 -0.20572 0.04075  -0.11247 116 LYS A NZ  
911  N N   A ALA A 110 ? 0.33761 0.43770 0.41865 -0.13688 0.03184  -0.09175 117 ALA A N   
912  N N   B ALA A 110 ? 0.35559 0.43764 0.43214 -0.13940 0.03645  -0.09112 117 ALA A N   
913  C CA  A ALA A 110 ? 0.43157 0.50058 0.49384 -0.14918 0.03530  -0.10377 117 ALA A CA  
914  C CA  B ALA A 110 ? 0.38708 0.43189 0.44410 -0.15311 0.04190  -0.10313 117 ALA A CA  
915  C C   A ALA A 110 ? 0.38972 0.47240 0.44700 -0.13592 0.02530  -0.10569 117 ALA A C   
916  C C   B ALA A 110 ? 0.36249 0.41296 0.41376 -0.14054 0.03425  -0.10712 117 ALA A C   
917  O O   A ALA A 110 ? 0.36484 0.45826 0.41165 -0.15091 0.02162  -0.11807 117 ALA A O   
918  O O   B ALA A 110 ? 0.35071 0.39325 0.38781 -0.15585 0.03554  -0.12102 117 ALA A O   
919  C CB  A ALA A 110 ? 0.39655 0.40124 0.44314 -0.14400 0.04719  -0.10138 117 ALA A CB  
920  C CB  B ALA A 110 ? 0.32843 0.30876 0.36933 -0.14887 0.05365  -0.09920 117 ALA A CB  
921  N N   A PHE A 111 ? 0.36093 0.44113 0.42142 -0.11044 0.02135  -0.09386 118 PHE A N   
922  N N   B PHE A 111 ? 0.31398 0.37514 0.37184 -0.11556 0.02752  -0.09592 118 PHE A N   
923  C CA  A PHE A 111 ? 0.30264 0.38814 0.35192 -0.10037 0.01427  -0.09406 118 PHE A CA  
924  C CA  B PHE A 111 ? 0.33520 0.40577 0.38344 -0.10771 0.02037  -0.09828 118 PHE A CA  
925  C C   A PHE A 111 ? 0.34534 0.47456 0.39276 -0.10620 -0.00018 -0.09716 118 PHE A C   
926  C C   B PHE A 111 ? 0.31977 0.43309 0.36634 -0.11999 0.00824  -0.10474 118 PHE A C   
927  O O   A PHE A 111 ? 0.32598 0.45604 0.35465 -0.11400 -0.00426 -0.10505 118 PHE A O   
928  O O   B PHE A 111 ? 0.32258 0.43411 0.35170 -0.13198 0.00657  -0.11586 118 PHE A O   
929  C CB  A PHE A 111 ? 0.29424 0.37251 0.34710 -0.07630 0.01255  -0.08036 118 PHE A CB  
930  C CB  B PHE A 111 ? 0.31790 0.39086 0.37060 -0.08293 0.01570  -0.08433 118 PHE A CB  
931  C CG  A PHE A 111 ? 0.29977 0.37590 0.33584 -0.06903 0.00817  -0.07918 118 PHE A CG  
932  C CG  B PHE A 111 ? 0.30966 0.38346 0.34588 -0.07699 0.01088  -0.08473 118 PHE A CG  
933  C CD1 A PHE A 111 ? 0.30259 0.36349 0.32161 -0.07948 0.01418  -0.09069 118 PHE A CD1 
934  C CD1 B PHE A 111 ? 0.32880 0.39301 0.34706 -0.09016 0.01459  -0.09754 118 PHE A CD1 
935  C CD2 A PHE A 111 ? 0.27277 0.35710 0.30592 -0.05286 -0.00012 -0.06703 118 PHE A CD2 
936  C CD2 B PHE A 111 ? 0.30210 0.38072 0.33592 -0.05991 0.00441  -0.07266 118 PHE A CD2 
937  C CE1 A PHE A 111 ? 0.26437 0.32201 0.26337 -0.07639 0.01260  -0.08947 118 PHE A CE1 
938  C CE1 B PHE A 111 ? 0.36117 0.42392 0.35901 -0.08749 0.01225  -0.09742 118 PHE A CE1 
939  C CE2 A PHE A 111 ? 0.29058 0.36522 0.30116 -0.04977 -0.00251 -0.06475 118 PHE A CE2 
940  C CE2 B PHE A 111 ? 0.33556 0.40794 0.34743 -0.05795 0.00177  -0.07177 118 PHE A CE2 
941  C CZ  A PHE A 111 ? 0.29605 0.35899 0.28939 -0.06274 0.00424  -0.07565 118 PHE A CZ  
942  C CZ  B PHE A 111 ? 0.27028 0.33610 0.26390 -0.07223 0.00595  -0.08370 118 PHE A CZ  
943  N N   A MET A 112 ? 0.32498 0.49329 0.39115 -0.10140 -0.00854 -0.09182 119 MET A N   
944  N N   B MET A 112 ? 0.32917 0.48427 0.39392 -0.11652 -0.00070 -0.09917 119 MET A N   
945  C CA  A MET A 112 ? 0.44094 0.65579 0.50817 -0.09838 -0.02605 -0.09302 119 MET A CA  
946  C CA  B MET A 112 ? 0.32733 0.53246 0.39534 -0.12402 -0.01551 -0.10545 119 MET A CA  
947  C C   A MET A 112 ? 0.41558 0.65701 0.48188 -0.12609 -0.02935 -0.10950 119 MET A C   
948  C C   B MET A 112 ? 0.35745 0.56879 0.42070 -0.15679 -0.01158 -0.12329 119 MET A C   
949  O O   A MET A 112 ? 0.37418 0.64642 0.43140 -0.12657 -0.04517 -0.11325 119 MET A O   
950  O O   B MET A 112 ? 0.30060 0.52985 0.35009 -0.16721 -0.02136 -0.13283 119 MET A O   
951  C CB  A MET A 112 ? 0.41611 0.66850 0.50734 -0.08040 -0.03343 -0.08444 119 MET A CB  
952  C CB  B MET A 112 ? 0.27536 0.52838 0.36983 -0.11142 -0.02386 -0.09858 119 MET A CB  
953  C CG  A MET A 112 ? 0.21227 0.45422 0.29285 -0.05054 -0.04267 -0.07030 119 MET A CG  
954  C CG  B MET A 112 ? 0.41338 0.66548 0.50526 -0.07896 -0.03334 -0.08366 119 MET A CG  
955  S SD  A MET A 112 ? 0.68876 0.97204 0.79622 -0.02627 -0.05010 -0.06349 119 MET A SD  
956  S SD  B MET A 112 ? 0.45638 0.75281 0.57952 -0.06069 -0.03703 -0.07752 119 MET A SD  
957  C CE  A MET A 112 ? 0.40894 0.64204 0.49658 -0.00024 -0.04791 -0.04779 119 MET A CE  
958  C CE  B MET A 112 ? 0.54227 0.86370 0.65651 -0.03026 -0.06064 -0.06987 119 MET A CE  
959  N N   A GLU A 113 ? 0.34734 0.57442 0.41877 -0.15028 -0.01539 -0.11945 120 GLU A N   
960  N N   B GLU A 113 ? 0.30312 0.49578 0.37273 -0.17509 0.00274  -0.12800 120 GLU A N   
961  C CA  A GLU A 113 ? 0.40329 0.63748 0.46433 -0.17688 -0.01459 -0.13418 120 GLU A CA  
962  C CA  B GLU A 113 ? 0.34673 0.52360 0.40091 -0.19894 0.01050  -0.13877 120 GLU A CA  
963  C C   A GLU A 113 ? 0.50757 0.70606 0.53751 -0.18233 -0.01264 -0.14204 120 GLU A C   
964  C C   B GLU A 113 ? 0.42345 0.56426 0.44981 -0.20294 0.01303  -0.14782 120 GLU A C   
965  O O   A GLU A 113 ? 0.43766 0.65260 0.45322 -0.19149 -0.02041 -0.14891 120 GLU A O   
966  O O   B GLU A 113 ? 0.38523 0.53900 0.39869 -0.21628 0.00888  -0.15700 120 GLU A O   
967  C CB  A GLU A 113 ? 0.40402 0.61283 0.46711 -0.19634 0.00278  -0.13788 120 GLU A CB  
968  C CB  B GLU A 113 ? 0.44435 0.58152 0.49569 -0.21102 0.02770  -0.13710 120 GLU A CB  
969  C CG  A GLU A 113 ? 0.49880 0.74706 0.58761 -0.19677 0.00341  -0.13296 120 GLU A CG  
970  C CG  B GLU A 113 ? 0.57319 0.74853 0.64201 -0.22147 0.02935  -0.13497 120 GLU A CG  
971  C CD  A GLU A 113 ? 0.59506 0.80694 0.67710 -0.21618 0.02187  -0.13407 120 GLU A CD  
972  C CD  B GLU A 113 ? 0.52037 0.65713 0.58587 -0.22531 0.04422  -0.12702 120 GLU A CD  
973  O OE1 A GLU A 113 ? 0.72011 0.87821 0.77731 -0.22911 0.03220  -0.13949 120 GLU A OE1 
974  O OE1 B GLU A 113 ? 0.47218 0.55059 0.52203 -0.21839 0.05177  -0.12280 120 GLU A OE1 
975  O OE2 A GLU A 113 ? 0.82804 1.06270 0.92649 -0.21726 0.02629  -0.12939 120 GLU A OE2 
976  O OE2 B GLU A 113 ? 0.46952 0.63384 0.54623 -0.23445 0.04838  -0.12521 120 GLU A OE2 
977  N N   A ALA A 114 ? 0.39583 0.54558 0.41506 -0.17424 -0.00115 -0.14047 121 ALA A N   
978  N N   B ALA A 114 ? 0.35167 0.44883 0.36909 -0.19078 0.02076  -0.14619 121 ALA A N   
979  C CA  A ALA A 114 ? 0.37105 0.48862 0.36201 -0.17789 0.00413  -0.14984 121 ALA A CA  
980  C CA  B ALA A 114 ? 0.45927 0.52267 0.45154 -0.19141 0.02654  -0.15567 121 ALA A CA  
981  C C   A ALA A 114 ? 0.36485 0.50782 0.33912 -0.16828 -0.01140 -0.14530 121 ALA A C   
982  C C   B ALA A 114 ? 0.37378 0.46925 0.35439 -0.18816 0.01270  -0.15741 121 ALA A C   
983  O O   A ALA A 114 ? 0.51103 0.64806 0.45915 -0.17934 -0.01211 -0.15496 121 ALA A O   
984  O O   B ALA A 114 ? 0.40506 0.48998 0.36288 -0.19724 0.01490  -0.16691 121 ALA A O   
985  C CB  A ALA A 114 ? 0.38713 0.45494 0.37627 -0.16176 0.01972  -0.14530 121 ALA A CB  
986  C CB  B ALA A 114 ? 0.43115 0.44829 0.42188 -0.17487 0.03828  -0.15382 121 ALA A CB  
987  N N   A LEU A 115 ? 0.39247 0.55703 0.37718 -0.14501 -0.02299 -0.12801 122 LEU A N   
988  N N   B LEU A 115 ? 0.34253 0.47275 0.33457 -0.17242 -0.00141 -0.14589 122 LEU A N   
989  C CA  A LEU A 115 ? 0.34915 0.52649 0.31047 -0.13347 -0.03828 -0.12042 122 LEU A CA  
990  C CA  B LEU A 115 ? 0.37705 0.53008 0.35006 -0.16595 -0.01637 -0.14329 122 LEU A CA  
991  C C   A LEU A 115 ? 0.56836 0.78948 0.52095 -0.14683 -0.05697 -0.12906 122 LEU A C   
992  C C   B LEU A 115 ? 0.37271 0.56376 0.34121 -0.18107 -0.02924 -0.15033 122 LEU A C   
993  O O   A LEU A 115 ? 0.52016 0.73944 0.43877 -0.15017 -0.06597 -0.13096 122 LEU A O   
994  O O   B LEU A 115 ? 0.43063 0.61828 0.37188 -0.18743 -0.03333 -0.15566 122 LEU A O   
995  C CB  A LEU A 115 ? 0.33697 0.52114 0.30903 -0.10506 -0.04665 -0.10068 122 LEU A CB  
996  C CB  B LEU A 115 ? 0.36604 0.53594 0.34919 -0.13756 -0.02756 -0.12296 122 LEU A CB  
997  C CG  A LEU A 115 ? 0.33092 0.47360 0.30359 -0.09262 -0.03129 -0.09219 122 LEU A CG  
998  C CG  B LEU A 115 ? 0.30661 0.43824 0.28426 -0.11880 -0.01697 -0.11209 122 LEU A CG  
999  C CD1 A LEU A 115 ? 0.40346 0.54983 0.38244 -0.06755 -0.03968 -0.07467 122 LEU A CD1 
1000 C CD1 B LEU A 115 ? 0.31937 0.46423 0.30119 -0.09445 -0.02895 -0.09375 122 LEU A CD1 
1001 C CD2 A LEU A 115 ? 0.37493 0.48600 0.31582 -0.09927 -0.02226 -0.09682 122 LEU A CD2 
1002 C CD2 B LEU A 115 ? 0.33191 0.43605 0.27823 -0.12540 -0.00903 -0.11980 122 LEU A CD2 
1003 N N   A GLN A 116 ? 0.42881 0.68940 0.41079 -0.15405 -0.06207 -0.13322 123 GLN A N   
1004 N N   B GLN A 116 ? 0.37830 0.60533 0.37373 -0.18481 -0.03403 -0.14872 123 GLN A N   
1005 C CA  A GLN A 116 ? 0.42503 0.72121 0.40479 -0.16229 -0.07493 -0.13803 123 GLN A CA  
1006 C CA  B GLN A 116 ? 0.51977 0.78211 0.51566 -0.19894 -0.04271 -0.15577 123 GLN A CA  
1007 C C   A GLN A 116 ? 0.64674 0.91810 0.60898 -0.18936 -0.06180 -0.15331 123 GLN A C   
1008 C C   B GLN A 116 ? 0.49409 0.72194 0.46881 -0.22332 -0.02843 -0.17004 123 GLN A C   
1009 O O   A GLN A 116 ? 0.67540 0.96660 0.62339 -0.19805 -0.07253 -0.15880 123 GLN A O   
1010 O O   B GLN A 116 ? 0.51450 0.76651 0.48193 -0.23771 -0.03556 -0.17816 123 GLN A O   
1011 C CB  A GLN A 116 ? 0.60157 0.94791 0.62032 -0.15839 -0.08078 -0.13634 123 GLN A CB  
1012 C CB  B GLN A 116 ? 0.37639 0.68139 0.40679 -0.19993 -0.04471 -0.15341 123 GLN A CB  
1013 C CG  A GLN A 116 ? 0.49884 0.87809 0.53260 -0.12618 -0.09836 -0.12184 123 GLN A CG  
1014 C CG  B GLN A 116 ? 0.48130 0.83833 0.51963 -0.20999 -0.05706 -0.16022 123 GLN A CG  
1015 C CD  A GLN A 116 ? 0.76240 1.19980 0.81824 -0.11863 -0.11397 -0.12260 123 GLN A CD  
1016 C CD  B GLN A 116 ? 0.59920 0.98180 0.62207 -0.19586 -0.07996 -0.15683 123 GLN A CD  
1017 O OE1 A GLN A 116 ? 0.83394 1.29231 0.89436 -0.14064 -0.11244 -0.13463 123 GLN A OE1 
1018 O OE1 B GLN A 116 ? 0.57289 0.94366 0.56879 -0.20930 -0.08259 -0.16480 123 GLN A OE1 
1019 N NE2 A GLN A 116 ? 0.68775 1.14972 0.75647 -0.08649 -0.12847 -0.11051 123 GLN A NE2 
1020 N NE2 B GLN A 116 ? 0.59206 1.00504 0.62808 -0.16720 -0.09662 -0.14423 123 GLN A NE2 
1021 N N   A ALA A 117 ? 0.63551 0.86171 0.59692 -0.20047 -0.03959 -0.15994 124 ALA A N   
1022 N N   B ALA A 117 ? 0.49386 0.66574 0.45819 -0.22612 -0.00921 -0.17352 124 ALA A N   
1023 C CA  A ALA A 117 ? 0.63405 0.82792 0.57668 -0.22198 -0.02516 -0.17402 124 ALA A CA  
1024 C CA  B ALA A 117 ? 0.51020 0.64246 0.45352 -0.24468 0.00562  -0.18669 124 ALA A CA  
1025 C C   A ALA A 117 ? 0.78157 0.93266 0.69314 -0.21933 -0.01557 -0.17828 124 ALA A C   
1026 C C   B ALA A 117 ? 0.59062 0.68916 0.50597 -0.23993 0.01180  -0.19247 124 ALA A C   
1027 O O   A ALA A 117 ? 0.64625 0.75684 0.54676 -0.22921 0.00224  -0.18874 124 ALA A O   
1028 O O   B ALA A 117 ? 0.53316 0.59200 0.43179 -0.24976 0.02648  -0.20343 124 ALA A O   
1029 C CB  A ALA A 117 ? 0.55482 0.72051 0.51175 -0.23288 -0.00686 -0.17803 124 ALA A CB  
1030 C CB  B ALA A 117 ? 0.59462 0.68427 0.54446 -0.24910 0.02337  -0.18679 124 ALA A CB  
1031 N N   A GLY A 118 ? 0.64120 0.79899 0.53672 -0.20509 -0.02604 -0.17011 125 GLY A N   
1032 N N   B GLY A 118 ? 0.61236 0.72422 0.52018 -0.22497 0.00202  -0.18551 125 GLY A N   
1033 C CA  A GLY A 118 ? 0.65092 0.77564 0.51385 -0.20567 -0.01624 -0.17478 125 GLY A CA  
1034 C CA  B GLY A 118 ? 0.50695 0.59250 0.38630 -0.22252 0.00921  -0.19092 125 GLY A CA  
1035 C C   A GLY A 118 ? 0.68801 0.78679 0.54697 -0.19017 -0.00641 -0.16840 125 GLY A C   
1036 C C   B GLY A 118 ? 0.48011 0.53362 0.36142 -0.20551 0.02249  -0.18757 125 GLY A C   
1037 O O   A GLY A 118 ? 0.62588 0.71398 0.45557 -0.18743 -0.00540 -0.16613 125 GLY A O   
1038 O O   B GLY A 118 ? 0.49936 0.53232 0.36022 -0.20372 0.03258  -0.19343 125 GLY A O   
1039 N N   A ALA A 119 ? 0.47952 0.56765 0.36607 -0.18122 0.00166  -0.16539 126 ALA A N   
1040 N N   B ALA A 119 ? 0.44946 0.50101 0.35586 -0.19339 0.02350  -0.17902 126 ALA A N   
1041 C CA  A ALA A 119 ? 0.41380 0.47643 0.30098 -0.16765 0.01399  -0.16230 126 ALA A CA  
1042 C CA  B ALA A 119 ? 0.42524 0.45182 0.33651 -0.17649 0.03473  -0.17622 126 ALA A CA  
1043 C C   A ALA A 119 ? 0.40124 0.47626 0.27733 -0.15115 0.00178  -0.14275 126 ALA A C   
1044 C C   B ALA A 119 ? 0.51827 0.55997 0.41246 -0.16865 0.02694  -0.16922 126 ALA A C   
1045 O O   A ALA A 119 ? 0.52025 0.62285 0.38764 -0.14850 -0.01852 -0.13371 126 ALA A O   
1046 O O   B ALA A 119 ? 0.52757 0.59812 0.40773 -0.17172 0.00920  -0.16279 126 ALA A O   
1047 C CB  A ALA A 119 ? 0.46794 0.51670 0.39051 -0.15593 0.02291  -0.15681 126 ALA A CB  
1048 C CB  B ALA A 119 ? 0.39268 0.41456 0.33314 -0.16634 0.03580  -0.16812 126 ALA A CB  
1049 N N   A ASP A 120 ? 0.47284 0.52614 0.34838 -0.13961 0.01426  -0.13688 127 ASP A N   
1050 N N   B ASP A 120 ? 0.47942 0.50059 0.37376 -0.15688 0.04029  -0.16919 127 ASP A N   
1051 C CA  A ASP A 120 ? 0.46252 0.51520 0.32354 -0.12649 0.00672  -0.11867 127 ASP A CA  
1052 C CA  B ASP A 120 ? 0.40400 0.43121 0.28321 -0.14752 0.03740  -0.15699 127 ASP A CA  
1053 C C   A ASP A 120 ? 0.35357 0.39671 0.24423 -0.10962 0.01443  -0.10854 127 ASP A C   
1054 C C   B ASP A 120 ? 0.37106 0.40226 0.27679 -0.12676 0.03326  -0.13751 127 ASP A C   
1055 O O   A ASP A 120 ? 0.37049 0.40679 0.28938 -0.10706 0.02582  -0.11555 127 ASP A O   
1056 O O   B ASP A 120 ? 0.35429 0.37879 0.28965 -0.11787 0.03807  -0.13596 127 ASP A O   
1057 C CB  A ASP A 120 ? 0.46176 0.49772 0.28042 -0.13699 0.01515  -0.12286 127 ASP A CB  
1058 C CB  B ASP A 120 ? 0.51419 0.52244 0.37707 -0.15104 0.05744  -0.17030 127 ASP A CB  
1059 C CG  A ASP A 120 ? 0.55475 0.57335 0.38258 -0.14084 0.04075  -0.13684 127 ASP A CG  
1060 C CG  B ASP A 120 ? 0.62114 0.62507 0.46188 -0.16521 0.06175  -0.18114 127 ASP A CG  
1061 O OD1 A ASP A 120 ? 0.67559 0.68981 0.51417 -0.14833 0.05201  -0.15565 127 ASP A OD1 
1062 O OD1 B ASP A 120 ? 0.67893 0.67170 0.53074 -0.16932 0.06735  -0.19154 127 ASP A OD1 
1063 O OD2 A ASP A 120 ? 0.50719 0.51686 0.33153 -0.13615 0.04970  -0.13001 127 ASP A OD2 
1064 O OD2 B ASP A 120 ? 0.77867 0.78663 0.58736 -0.17291 0.05963  -0.17869 127 ASP A OD2 
1065 N N   A ILE A 121 ? 0.38777 0.42663 0.26717 -0.09803 0.00725  -0.09177 128 ILE A N   
1066 N N   B ILE A 121 ? 0.36398 0.40157 0.25342 -0.11965 0.02385  -0.12236 128 ILE A N   
1067 C CA  A ILE A 121 ? 0.32051 0.35297 0.22485 -0.08297 0.01100  -0.08151 128 ILE A CA  
1068 C CA  B ILE A 121 ? 0.36415 0.40066 0.27248 -0.10169 0.02116  -0.10566 128 ILE A CA  
1069 C C   A ILE A 121 ? 0.38848 0.40960 0.30934 -0.08539 0.03115  -0.09189 128 ILE A C   
1070 C C   B ILE A 121 ? 0.32080 0.34293 0.24816 -0.09645 0.03942  -0.11122 128 ILE A C   
1071 O O   A ILE A 121 ? 0.37182 0.39297 0.32280 -0.07458 0.03458  -0.08928 128 ILE A O   
1072 O O   B ILE A 121 ? 0.36745 0.38920 0.32279 -0.08348 0.03971  -0.10430 128 ILE A O   
1073 C CB  A ILE A 121 ? 0.36686 0.38734 0.24543 -0.07373 0.00152  -0.06410 128 ILE A CB  
1074 C CB  B ILE A 121 ? 0.37984 0.41381 0.25756 -0.09666 0.00981  -0.09001 128 ILE A CB  
1075 C CG1 A ILE A 121 ? 0.48704 0.52407 0.36073 -0.06177 -0.02090 -0.05359 128 ILE A CG1 
1076 C CG1 B ILE A 121 ? 0.53978 0.59511 0.41412 -0.08934 -0.01312 -0.08024 128 ILE A CG1 
1077 C CG2 A ILE A 121 ? 0.35646 0.36515 0.25282 -0.06379 0.00879  -0.05684 128 ILE A CG2 
1078 C CG2 B ILE A 121 ? 0.38923 0.41031 0.27671 -0.08421 0.01469  -0.07811 128 ILE A CG2 
1079 C CD1 A ILE A 121 ? 0.46459 0.48155 0.30671 -0.04825 -0.03254 -0.03597 128 ILE A CD1 
1080 C CD1 B ILE A 121 ? 0.53692 0.58339 0.36905 -0.08407 -0.02728 -0.06658 128 ILE A CD1 
1081 N N   A SER A 122 ? 0.39676 0.41105 0.29859 -0.09844 0.04443  -0.10480 129 SER A N   
1082 N N   B SER A 122 ? 0.37700 0.39084 0.28986 -0.10600 0.05468  -0.12506 129 SER A N   
1083 C CA  A SER A 122 ? 0.46117 0.47281 0.38231 -0.09769 0.06353  -0.11672 129 SER A CA  
1084 C CA  B SER A 122 ? 0.39875 0.40863 0.33372 -0.09930 0.07162  -0.13333 129 SER A CA  
1085 C C   A SER A 122 ? 0.37551 0.38673 0.33141 -0.08861 0.06796  -0.12608 129 SER A C   
1086 C C   B SER A 122 ? 0.45142 0.45592 0.42079 -0.08698 0.07372  -0.13767 129 SER A C   
1087 O O   A SER A 122 ? 0.34862 0.36038 0.32778 -0.08001 0.07922  -0.13307 129 SER A O   
1088 O O   B SER A 122 ? 0.37717 0.38217 0.37058 -0.07472 0.08187  -0.14017 129 SER A O   
1089 C CB  A SER A 122 ? 0.36186 0.37065 0.25660 -0.11385 0.07897  -0.13238 129 SER A CB  
1090 C CB  B SER A 122 ? 0.47594 0.48331 0.39260 -0.11189 0.08951  -0.15271 129 SER A CB  
1091 O OG  A SER A 122 ? 0.41675 0.42326 0.31021 -0.12019 0.08354  -0.14948 129 SER A OG  
1092 O OG  B SER A 122 ? 0.48197 0.48160 0.38683 -0.12139 0.09129  -0.16777 129 SER A OG  
1093 N N   A MET A 123 ? 0.32550 0.33541 0.28377 -0.09082 0.05920  -0.12670 130 MET A N   
1094 N N   B MET A 123 ? 0.32073 0.32010 0.29086 -0.09098 0.06616  -0.13862 130 MET A N   
1095 C CA  A MET A 123 ? 0.33951 0.33779 0.32043 -0.08565 0.06419  -0.13466 130 MET A CA  
1096 C CA  B MET A 123 ? 0.42716 0.41169 0.42015 -0.08254 0.06846  -0.14087 130 MET A CA  
1097 C C   A MET A 123 ? 0.28629 0.28564 0.29147 -0.07214 0.05600  -0.11981 130 MET A C   
1098 C C   B MET A 123 ? 0.32395 0.31420 0.33740 -0.06944 0.05877  -0.12265 130 MET A C   
1099 O O   A MET A 123 ? 0.34429 0.32897 0.36164 -0.06940 0.05813  -0.12258 130 MET A O   
1100 O O   B MET A 123 ? 0.29480 0.26955 0.32278 -0.06212 0.06023  -0.12149 130 MET A O   
1101 C CB  A MET A 123 ? 0.38374 0.37617 0.34970 -0.10181 0.06229  -0.14604 130 MET A CB  
1102 C CB  B MET A 123 ? 0.34504 0.31923 0.32620 -0.09837 0.06651  -0.15033 130 MET A CB  
1103 C CG  A MET A 123 ? 0.47958 0.46968 0.41609 -0.11681 0.07029  -0.16216 130 MET A CG  
1104 C CG  B MET A 123 ? 0.50849 0.48281 0.46086 -0.11619 0.07111  -0.16657 130 MET A CG  
1105 S SD  A MET A 123 ? 0.56635 0.55794 0.47818 -0.14061 0.06270  -0.17431 130 MET A SD  
1106 S SD  B MET A 123 ? 0.53072 0.47581 0.47374 -0.12849 0.08013  -0.18432 130 MET A SD  
1107 C CE  A MET A 123 ? 0.60497 0.56477 0.53404 -0.13838 0.07464  -0.18445 130 MET A CE  
1108 C CE  B MET A 123 ? 0.48601 0.43397 0.40319 -0.13624 0.08991  -0.19661 130 MET A CE  
1109 N N   A ILE A 124 ? 0.27685 0.28801 0.28460 -0.06438 0.04798  -0.10457 131 ILE A N   
1110 N N   B ILE A 124 ? 0.29852 0.30549 0.30880 -0.06620 0.04949  -0.10864 131 ILE A N   
1111 C CA  A ILE A 124 ? 0.28225 0.29645 0.30798 -0.05303 0.04003  -0.09093 131 ILE A CA  
1112 C CA  B ILE A 124 ? 0.27546 0.28802 0.30142 -0.05463 0.04083  -0.09308 131 ILE A CA  
1113 C C   A ILE A 124 ? 0.29913 0.29973 0.34582 -0.04172 0.04659  -0.09269 131 ILE A C   
1114 C C   B ILE A 124 ? 0.29844 0.29824 0.34543 -0.04178 0.04680  -0.09305 131 ILE A C   
1115 O O   A ILE A 124 ? 0.25435 0.24890 0.31048 -0.03750 0.04278  -0.08583 131 ILE A O   
1116 O O   B ILE A 124 ? 0.25814 0.25253 0.31505 -0.03669 0.04274  -0.08537 131 ILE A O   
1117 C CB  A ILE A 124 ? 0.22846 0.25069 0.24802 -0.04615 0.03288  -0.07741 131 ILE A CB  
1118 C CB  B ILE A 124 ? 0.25757 0.27958 0.27391 -0.04970 0.03391  -0.08086 131 ILE A CB  
1119 C CG1 A ILE A 124 ? 0.24784 0.27410 0.28260 -0.03469 0.02526  -0.06504 131 ILE A CG1 
1120 C CG1 B ILE A 124 ? 0.25779 0.28351 0.28875 -0.03718 0.02642  -0.06734 131 ILE A CG1 
1121 C CG2 A ILE A 124 ? 0.22259 0.24109 0.24137 -0.04499 0.04234  -0.08071 131 ILE A CG2 
1122 C CG2 B ILE A 124 ? 0.26572 0.28381 0.27684 -0.05062 0.04400  -0.08555 131 ILE A CG2 
1123 C CD1 A ILE A 124 ? 0.29232 0.32120 0.31571 -0.02753 0.01704  -0.05293 131 ILE A CD1 
1124 C CD1 B ILE A 124 ? 0.30633 0.33494 0.32283 -0.03159 0.01774  -0.05553 131 ILE A CD1 
1125 N N   . GLY A 125 ? 0.29491 0.29212 0.34812 -0.03619 0.05627  -0.10206 132 GLY A N   
1126 C CA  . GLY A 125 ? 0.28587 0.27464 0.35964 -0.02008 0.05883  -0.10246 132 GLY A CA  
1127 C C   . GLY A 125 ? 0.38135 0.34243 0.45483 -0.01753 0.06083  -0.10657 132 GLY A C   
1128 O O   . GLY A 125 ? 0.35270 0.29956 0.43560 -0.00402 0.05791  -0.10003 132 GLY A O   
1129 N N   . GLN A 126 ? 0.30136 0.25038 0.35932 -0.03181 0.06563  -0.11737 133 GLN A N   
1130 C CA  . GLN A 126 ? 0.38236 0.29660 0.43309 -0.03439 0.06921  -0.12254 133 GLN A CA  
1131 C C   . GLN A 126 ? 0.43081 0.33898 0.47948 -0.04087 0.06179  -0.10840 133 GLN A C   
1132 O O   . GLN A 126 ? 0.48172 0.35542 0.52077 -0.04510 0.06534  -0.10975 133 GLN A O   
1133 C CB  . GLN A 126 ? 0.49728 0.40158 0.52867 -0.05312 0.07627  -0.13949 133 GLN A CB  
1134 C CG  . GLN A 126 ? 0.59662 0.50730 0.62587 -0.04978 0.08676  -0.15607 133 GLN A CG  
1135 C CD  . GLN A 126 ? 0.74425 0.64613 0.74886 -0.07082 0.09307  -0.17317 133 GLN A CD  
1136 O OE1 . GLN A 126 ? 0.59364 0.47110 0.58567 -0.08131 0.09280  -0.17538 133 GLN A OE1 
1137 N NE2 . GLN A 126 ? 0.69148 0.61591 0.68605 -0.07783 0.09694  -0.18005 133 GLN A NE2 
1138 N N   . PHE A 127 ? 0.32236 0.26051 0.37735 -0.04221 0.05301  -0.09573 134 PHE A N   
1139 C CA  . PHE A 127 ? 0.35280 0.29507 0.40830 -0.04918 0.04786  -0.08460 134 PHE A CA  
1140 C C   . PHE A 127 ? 0.34062 0.28745 0.40645 -0.03292 0.04286  -0.06996 134 PHE A C   
1141 O O   . PHE A 127 ? 0.33248 0.28990 0.39969 -0.03693 0.03936  -0.06067 134 PHE A O   
1142 C CB  . PHE A 127 ? 0.26105 0.23782 0.31456 -0.06358 0.04147  -0.08519 134 PHE A CB  
1143 C CG  . PHE A 127 ? 0.33408 0.30883 0.37443 -0.08175 0.04456  -0.10032 134 PHE A CG  
1144 C CD1 . PHE A 127 ? 0.61176 0.56068 0.64271 -0.09817 0.05142  -0.10933 134 PHE A CD1 
1145 C CD2 . PHE A 127 ? 0.35636 0.34598 0.38801 -0.08316 0.04255  -0.10668 134 PHE A CD2 
1146 C CE1 . PHE A 127 ? 0.50648 0.45083 0.52233 -0.11682 0.05473  -0.12563 134 PHE A CE1 
1147 C CE2 . PHE A 127 ? 0.51469 0.50104 0.53003 -0.10045 0.04550  -0.12187 134 PHE A CE2 
1148 C CZ  . PHE A 127 ? 0.53512 0.50000 0.54373 -0.11720 0.05139  -0.13229 134 PHE A CZ  
1149 N N   . GLY A 128 ? 0.25711 0.20010 0.33082 -0.01563 0.04288  -0.06952 135 GLY A N   
1150 C CA  . GLY A 128 ? 0.26814 0.21218 0.34897 -0.00122 0.03749  -0.05766 135 GLY A CA  
1151 C C   . GLY A 128 ? 0.28778 0.25989 0.37295 -0.00003 0.03137  -0.04973 135 GLY A C   
1152 O O   . GLY A 128 ? 0.34236 0.31503 0.43011 0.00910  0.02696  -0.04058 135 GLY A O   
1153 N N   . VAL A 129 ? 0.22114 0.21218 0.30292 -0.00815 0.03044  -0.05294 136 VAL A N   
1154 C CA  . VAL A 129 ? 0.17098 0.17931 0.25090 -0.00511 0.02438  -0.04512 136 VAL A CA  
1155 C C   . VAL A 129 ? 0.21946 0.23348 0.29401 -0.00592 0.02554  -0.04928 136 VAL A C   
1156 O O   . VAL A 129 ? 0.20877 0.22900 0.27193 -0.00712 0.02117  -0.04463 136 VAL A O   
1157 C CB  . VAL A 129 ? 0.18337 0.20707 0.25929 -0.01190 0.02003  -0.04232 136 VAL A CB  
1158 C CG1 . VAL A 129 ? 0.25055 0.27294 0.33178 -0.01390 0.02144  -0.03785 136 VAL A CG1 
1159 C CG2 . VAL A 129 ? 0.22611 0.25495 0.29546 -0.02480 0.02105  -0.05185 136 VAL A CG2 
1160 N N   . GLY A 130 ? 0.26403 0.20214 0.26434 -0.00583 -0.02667 -0.05102 137 GLY A N   
1161 C CA  . GLY A 130 ? 0.24919 0.19383 0.23372 0.00637  -0.02207 -0.05038 137 GLY A CA  
1162 C C   . GLY A 130 ? 0.29207 0.24856 0.27995 0.00610  -0.01280 -0.03888 137 GLY A C   
1163 O O   . GLY A 130 ? 0.24246 0.20759 0.22223 0.01359  -0.00938 -0.03537 137 GLY A O   
1164 N N   . PHE A 131 ? 0.22204 0.17858 0.22149 -0.00185 -0.00912 -0.03277 138 PHE A N   
1165 C CA  . PHE A 131 ? 0.22172 0.18617 0.22475 -0.00235 -0.00296 -0.02487 138 PHE A CA  
1166 C C   . PHE A 131 ? 0.23236 0.20496 0.23488 -0.00031 -0.00377 -0.02354 138 PHE A C   
1167 O O   . PHE A 131 ? 0.22449 0.20038 0.22560 0.00317  0.00040  -0.01756 138 PHE A O   
1168 C CB  . PHE A 131 ? 0.26278 0.22717 0.27523 -0.00933 -0.00110 -0.02147 138 PHE A CB  
1169 C CG  . PHE A 131 ? 0.26439 0.23482 0.28023 -0.00971 0.00183  -0.01759 138 PHE A CG  
1170 C CD1 . PHE A 131 ? 0.24849 0.21881 0.26479 -0.00839 0.00473  -0.01404 138 PHE A CD1 
1171 C CD2 . PHE A 131 ? 0.25579 0.23194 0.27581 -0.01095 0.00086  -0.01804 138 PHE A CD2 
1172 C CE1 . PHE A 131 ? 0.22037 0.19173 0.24082 -0.00927 0.00517  -0.01247 138 PHE A CE1 
1173 C CE2 . PHE A 131 ? 0.22912 0.20674 0.25062 -0.00920 0.00252  -0.01651 138 PHE A CE2 
1174 C CZ  . PHE A 131 ? 0.24252 0.21549 0.26402 -0.00886 0.00394  -0.01448 138 PHE A CZ  
1175 N N   . TYR A 132 ? 0.22159 0.19798 0.22753 -0.00265 -0.00942 -0.02795 139 TYR A N   
1176 C CA  . TYR A 132 ? 0.21578 0.20150 0.22263 0.00044  -0.01039 -0.02591 139 TYR A CA  
1177 C C   . TYR A 132 ? 0.23620 0.22525 0.23030 0.01018  -0.01117 -0.02511 139 TYR A C   
1178 O O   . TYR A 132 ? 0.21935 0.21478 0.21264 0.01482  -0.01077 -0.02059 139 TYR A O   
1179 C CB  . TYR A 132 ? 0.19236 0.18637 0.20967 -0.00458 -0.01636 -0.02982 139 TYR A CB  
1180 C CG  . TYR A 132 ? 0.21581 0.21078 0.24516 -0.01230 -0.01294 -0.02681 139 TYR A CG  
1181 C CD1 . TYR A 132 ? 0.21078 0.21157 0.24373 -0.01064 -0.00799 -0.02236 139 TYR A CD1 
1182 C CD2 . TYR A 132 ? 0.21013 0.19912 0.24558 -0.01960 -0.01447 -0.02798 139 TYR A CD2 
1183 C CE1 . TYR A 132 ? 0.21897 0.22359 0.25914 -0.01476 -0.00414 -0.01942 139 TYR A CE1 
1184 C CE2 . TYR A 132 ? 0.23216 0.22435 0.27697 -0.02508 -0.00994 -0.02232 139 TYR A CE2 
1185 C CZ  . TYR A 132 ? 0.25207 0.25391 0.29796 -0.02195 -0.00448 -0.01816 139 TYR A CZ  
1186 O OH  . TYR A 132 ? 0.24054 0.24847 0.29212 -0.02459 0.00054  -0.01250 139 TYR A OH  
1187 N N   . SER A 133 ? 0.22622 0.21166 0.20911 0.01536  -0.01159 -0.02842 140 SER A N   
1188 C CA  . SER A 133 ? 0.22460 0.21645 0.19289 0.02710  -0.00969 -0.02491 140 SER A CA  
1189 C C   . SER A 133 ? 0.21739 0.21132 0.18858 0.02886  0.00001  -0.01094 140 SER A C   
1190 O O   . SER A 133 ? 0.23150 0.23267 0.19336 0.03815  0.00347  -0.00321 140 SER A O   
1191 C CB  . SER A 133 ? 0.24356 0.23245 0.19747 0.03493  -0.01120 -0.03208 140 SER A CB  
1192 O OG  . SER A 133 ? 0.26379 0.24772 0.22087 0.03367  -0.00398 -0.02786 140 SER A OG  
1193 N N   . ALA A 134 ? 0.21671 0.20476 0.20106 0.02026  0.00383  -0.00714 141 ALA A N   
1194 C CA  . ALA A 134 ? 0.22767 0.21518 0.21945 0.01928  0.01019  0.00470  141 ALA A CA  
1195 C C   . ALA A 134 ? 0.21364 0.20232 0.20506 0.02342  0.00962  0.01069  141 ALA A C   
1196 O O   . ALA A 134 ? 0.21185 0.20046 0.20549 0.02622  0.01487  0.02306  141 ALA A O   
1197 C CB  . ALA A 134 ? 0.22268 0.20304 0.22771 0.00964  0.01046  0.00346  141 ALA A CB  
1198 N N   . TYR A 135 ? 0.21579 0.20652 0.20631 0.02411  0.00344  0.00360  142 TYR A N   
1199 C CA  . TYR A 135 ? 0.24110 0.23391 0.23146 0.03005  0.00232  0.00901  142 TYR A CA  
1200 C C   . TYR A 135 ? 0.22707 0.22985 0.20292 0.04170  0.00175  0.01410  142 TYR A C   
1201 O O   . TYR A 135 ? 0.24065 0.24653 0.21454 0.04889  0.00068  0.02028  142 TYR A O   
1202 C CB  . TYR A 135 ? 0.20987 0.20630 0.20699 0.02762  -0.00348 0.00059  142 TYR A CB  
1203 C CG  . TYR A 135 ? 0.21427 0.20201 0.22227 0.02027  -0.00127 -0.00151 142 TYR A CG  
1204 C CD1 . TYR A 135 ? 0.23012 0.20855 0.24326 0.02244  0.00062  0.00291  142 TYR A CD1 
1205 C CD2 . TYR A 135 ? 0.21741 0.20456 0.22897 0.01243  -0.00151 -0.00788 142 TYR A CD2 
1206 C CE1 . TYR A 135 ? 0.21353 0.18397 0.23327 0.01774  0.00112  -0.00159 142 TYR A CE1 
1207 C CE2 . TYR A 135 ? 0.21744 0.19901 0.23546 0.00793  0.00023  -0.00975 142 TYR A CE2 
1208 C CZ  . TYR A 135 ? 0.26570 0.23962 0.28681 0.01096  0.00108  -0.00777 142 TYR A CZ  
1209 O OH  . TYR A 135 ? 0.23050 0.19924 0.25487 0.00843  0.00120  -0.01227 142 TYR A OH  
1210 N N   . LEU A 136 ? 0.24483 0.25304 0.20876 0.04590  0.00260  0.01194  143 LEU A N   
1211 C CA  . LEU A 136 ? 0.28447 0.30341 0.23149 0.05962  0.00451  0.01950  143 LEU A CA  
1212 C C   . LEU A 136 ? 0.26835 0.28581 0.21956 0.06227  0.01512  0.03977  143 LEU A C   
1213 O O   . LEU A 136 ? 0.27148 0.29682 0.21240 0.07368  0.01756  0.05139  143 LEU A O   
1214 C CB  . LEU A 136 ? 0.29428 0.31888 0.22586 0.06574  0.00360  0.01125  143 LEU A CB  
1215 C CG  . LEU A 136 ? 0.26271 0.28708 0.18826 0.06489  -0.00890 -0.00878 143 LEU A CG  
1216 C CD1 . LEU A 136 ? 0.29723 0.32025 0.20912 0.07092  -0.00873 -0.01715 143 LEU A CD1 
1217 C CD2 . LEU A 136 ? 0.27625 0.31218 0.19135 0.07384  -0.01866 -0.01340 143 LEU A CD2 
1218 N N   . VAL A 137 ? 0.24343 0.25144 0.21091 0.05172  0.02087  0.04517  144 VAL A N   
1219 C CA  . VAL A 137 ? 0.25008 0.25704 0.22646 0.05159  0.03036  0.06524  144 VAL A CA  
1220 C C   . VAL A 137 ? 0.24779 0.23707 0.24577 0.03984  0.02973  0.06870  144 VAL A C   
1221 O O   . VAL A 137 ? 0.31690 0.30045 0.32610 0.03827  0.03516  0.08556  144 VAL A O   
1222 C CB  . VAL A 137 ? 0.26300 0.28059 0.23952 0.05205  0.03845  0.07135  144 VAL A CB  
1223 C CG1 . VAL A 137 ? 0.30306 0.33705 0.25448 0.06757  0.03921  0.06752  144 VAL A CG1 
1224 C CG2 . VAL A 137 ? 0.23209 0.24327 0.22038 0.04039  0.03579  0.05938  144 VAL A CG2 
1225 N N   . ALA A 138 ? 0.22933 0.20950 0.23331 0.03216  0.02290  0.05328  145 ALA A N   
1226 C CA  . ALA A 138 ? 0.22704 0.19043 0.24798 0.02288  0.02084  0.05236  145 ALA A CA  
1227 C C   . ALA A 138 ? 0.25304 0.20790 0.27260 0.02727  0.01536  0.04662  145 ALA A C   
1228 O O   . ALA A 138 ? 0.31836 0.28202 0.32917 0.03146  0.01108  0.03625  145 ALA A O   
1229 C CB  . ALA A 138 ? 0.22921 0.19080 0.25687 0.01312  0.01816  0.04021  145 ALA A CB  
1230 N N   . GLU A 139 ? 0.24399 0.18184 0.27405 0.02653  0.01512  0.05363  146 GLU A N   
1231 C CA  . GLU A 139 ? 0.26660 0.19464 0.29635 0.03217  0.00997  0.04648  146 GLU A CA  
1232 C C   . GLU A 139 ? 0.30428 0.22560 0.33900 0.02609  0.00532  0.03036  146 GLU A C   
1233 O O   . GLU A 139 ? 0.31876 0.24082 0.35015 0.03223  0.00197  0.02128  146 GLU A O   
1234 C CB  . GLU A 139 ? 0.28799 0.19645 0.32552 0.03616  0.01081  0.05973  146 GLU A CB  
1235 C CG  . GLU A 139 ? 0.40072 0.29079 0.45614 0.02456  0.01155  0.06641  146 GLU A CG  
1236 C CD  . GLU A 139 ? 0.89404 0.76085 0.95976 0.02755  0.01179  0.08117  146 GLU A CD  
1237 O OE1 . GLU A 139 ? 0.67573 0.51965 0.75878 0.01820  0.00780  0.08045  146 GLU A OE1 
1238 O OE2 . GLU A 139 ? 0.64112 0.51167 0.69807 0.03942  0.01498  0.09342  146 GLU A OE2 
1239 N N   . LYS A 140 ? 0.25169 0.16965 0.29393 0.01561  0.00532  0.02743  147 LYS A N   
1240 C CA  . LYS A 140 ? 0.25329 0.16707 0.29760 0.01112  0.00080  0.01295  147 LYS A CA  
1241 C C   . LYS A 140 ? 0.25098 0.17458 0.29759 0.00227  0.00225  0.01166  147 LYS A C   
1242 O O   . LYS A 140 ? 0.24864 0.17484 0.30188 -0.00219 0.00580  0.02216  147 LYS A O   
1243 C CB  . LYS A 140 ? 0.26989 0.16006 0.32382 0.00961  -0.00444 0.00949  147 LYS A CB  
1244 C CG  . LYS A 140 ? 0.25863 0.14550 0.31117 0.00747  -0.01007 -0.00667 147 LYS A CG  
1245 C CD  . LYS A 140 ? 0.32641 0.18710 0.38569 0.00880  -0.01744 -0.01315 147 LYS A CD  
1246 C CE  . LYS A 140 ? 0.55824 0.40964 0.63026 -0.00313 -0.02381 -0.01713 147 LYS A CE  
1247 N NZ  . LYS A 140 ? 0.58710 0.40789 0.67128 -0.00452 -0.03196 -0.01937 147 LYS A NZ  
1248 N N   . VAL A 141 ? 0.20359 0.13462 0.24505 0.00104  0.00039  0.00059  148 VAL A N   
1249 C CA  . VAL A 141 ? 0.20774 0.14692 0.25067 -0.00554 0.00115  -0.00098 148 VAL A CA  
1250 C C   . VAL A 141 ? 0.28417 0.21898 0.32832 -0.00807 -0.00391 -0.01163 148 VAL A C   
1251 O O   . VAL A 141 ? 0.21338 0.14887 0.25040 -0.00285 -0.00545 -0.01960 148 VAL A O   
1252 C CB  . VAL A 141 ? 0.22533 0.17850 0.25898 -0.00363 0.00389  -0.00221 148 VAL A CB  
1253 C CG1 . VAL A 141 ? 0.24151 0.20002 0.27650 -0.00852 0.00449  -0.00360 148 VAL A CG1 
1254 C CG2 . VAL A 141 ? 0.19839 0.15703 0.22709 0.00115  0.00716  0.00576  148 VAL A CG2 
1255 N N   . THR A 142 ? 0.24510 0.17830 0.29835 -0.01494 -0.00656 -0.01134 149 THR A N   
1256 C CA  . THR A 142 ? 0.25191 0.18408 0.30461 -0.01662 -0.01276 -0.02185 149 THR A CA  
1257 C C   . THR A 142 ? 0.23623 0.18278 0.28772 -0.01941 -0.01075 -0.02013 149 THR A C   
1258 O O   . THR A 142 ? 0.25910 0.21186 0.31874 -0.02329 -0.00766 -0.01164 149 THR A O   
1259 C CB  . THR A 142 ? 0.25483 0.17322 0.32152 -0.02249 -0.02065 -0.02458 149 THR A CB  
1260 O OG1 . THR A 142 ? 0.31839 0.21904 0.38745 -0.01934 -0.02229 -0.02431 149 THR A OG1 
1261 C CG2 . THR A 142 ? 0.29666 0.21436 0.35870 -0.02157 -0.02938 -0.03877 149 THR A CG2 
1262 N N   . VAL A 143 ? 0.22571 0.17846 0.26686 -0.01594 -0.01166 -0.02674 150 VAL A N   
1263 C CA  . VAL A 143 ? 0.23817 0.20194 0.27749 -0.01707 -0.01038 -0.02467 150 VAL A CA  
1264 C C   . VAL A 143 ? 0.25570 0.22174 0.29312 -0.01640 -0.01767 -0.03265 150 VAL A C   
1265 O O   . VAL A 143 ? 0.26178 0.22731 0.28814 -0.01057 -0.01959 -0.03998 150 VAL A O   
1266 C CB  . VAL A 143 ? 0.21796 0.18758 0.24732 -0.01355 -0.00479 -0.02242 150 VAL A CB  
1267 C CG1 . VAL A 143 ? 0.19052 0.16726 0.21817 -0.01366 -0.00398 -0.01957 150 VAL A CG1 
1268 C CG2 . VAL A 143 ? 0.24227 0.21036 0.27226 -0.01345 -0.00035 -0.01736 150 VAL A CG2 
1269 N N   . ILE A 144 ? 0.19437 0.16558 0.24240 -0.02111 -0.02194 -0.03124 151 ILE A N   
1270 C CA  . ILE A 144 ? 0.20198 0.17929 0.24821 -0.01999 -0.03051 -0.03880 151 ILE A CA  
1271 C C   . ILE A 144 ? 0.24612 0.23676 0.28701 -0.01674 -0.02667 -0.03273 151 ILE A C   
1272 O O   . ILE A 144 ? 0.23101 0.22647 0.27971 -0.01882 -0.02154 -0.02398 151 ILE A O   
1273 C CB  . ILE A 144 ? 0.21908 0.19554 0.28497 -0.02823 -0.03996 -0.04124 151 ILE A CB  
1274 C CG1 . ILE A 144 ? 0.39116 0.35068 0.46805 -0.03347 -0.04171 -0.04176 151 ILE A CG1 
1275 C CG2 . ILE A 144 ? 0.29621 0.27762 0.35777 -0.02585 -0.05232 -0.05344 151 ILE A CG2 
1276 C CD1 . ILE A 144 ? 0.32955 0.27393 0.39409 -0.02752 -0.04743 -0.05487 151 ILE A CD1 
1277 N N   . THR A 145 ? 0.18887 0.18553 0.21562 -0.00999 -0.02885 -0.03666 152 THR A N   
1278 C CA  . THR A 145 ? 0.22126 0.22739 0.24264 -0.00598 -0.02451 -0.02866 152 THR A CA  
1279 C C   . THR A 145 ? 0.27431 0.29140 0.28540 0.00077  -0.03133 -0.03273 152 THR A C   
1280 O O   . THR A 145 ? 0.25825 0.27542 0.25889 0.00519  -0.03688 -0.04233 152 THR A O   
1281 C CB  . THR A 145 ? 0.28279 0.28429 0.29546 -0.00360 -0.01459 -0.02187 152 THR A CB  
1282 O OG1 . THR A 145 ? 0.25800 0.26245 0.26985 -0.00131 -0.01065 -0.01314 152 THR A OG1 
1283 C CG2 . THR A 145 ? 0.26491 0.26878 0.26370 0.00222  -0.01328 -0.02479 152 THR A CG2 
1284 N N   . LYS A 146 ? 0.23142 0.25836 0.24406 0.00354  -0.03117 -0.02566 153 LYS A N   
1285 C CA  . LYS A 146 ? 0.21521 0.25528 0.21685 0.01189  -0.03723 -0.02666 153 LYS A CA  
1286 C C   . LYS A 146 ? 0.23270 0.27559 0.22911 0.01769  -0.02951 -0.01304 153 LYS A C   
1287 O O   . LYS A 146 ? 0.24668 0.29027 0.25450 0.01622  -0.02751 -0.00700 153 LYS A O   
1288 C CB  . LYS A 146 ? 0.21325 0.26495 0.22783 0.00921  -0.05024 -0.03377 153 LYS A CB  
1289 C CG  . LYS A 146 ? 0.24689 0.31546 0.24949 0.01931  -0.05866 -0.03551 153 LYS A CG  
1290 C CD  . LYS A 146 ? 0.30906 0.37824 0.28983 0.02736  -0.06435 -0.04668 153 LYS A CD  
1291 C CE  . LYS A 146 ? 0.31122 0.39994 0.27818 0.03899  -0.07448 -0.04931 153 LYS A CE  
1292 N NZ  . LYS A 146 ? 0.26616 0.36273 0.22145 0.04870  -0.06447 -0.03166 153 LYS A NZ  
1293 N N   . HIS A 147 ? 0.21647 0.26094 0.19613 0.02514  -0.02488 -0.00751 154 HIS A N   
1294 C CA  . HIS A 147 ? 0.30180 0.34687 0.27557 0.03145  -0.01846 0.00691  154 HIS A CA  
1295 C C   . HIS A 147 ? 0.33193 0.39424 0.29332 0.04267  -0.02527 0.00840  154 HIS A C   
1296 O O   . HIS A 147 ? 0.28739 0.36000 0.23792 0.04706  -0.03257 -0.00161 154 HIS A O   
1297 C CB  . HIS A 147 ? 0.23558 0.27262 0.20238 0.03100  -0.00794 0.01550  154 HIS A CB  
1298 C CG  . HIS A 147 ? 0.27928 0.31037 0.24483 0.03433  -0.00082 0.03195  154 HIS A CG  
1299 N ND1 . HIS A 147 ? 0.29884 0.34011 0.25179 0.04477  0.00022  0.04300  154 HIS A ND1 
1300 C CD2 . HIS A 147 ? 0.28427 0.29828 0.25928 0.02900  0.00501  0.03925  154 HIS A CD2 
1301 C CE1 . HIS A 147 ? 0.34410 0.37305 0.30090 0.04490  0.00692  0.05800  154 HIS A CE1 
1302 N NE2 . HIS A 147 ? 0.31455 0.32577 0.28494 0.03510  0.00915  0.05463  154 HIS A NE2 
1303 N N   . ASN A 148 ? 0.26282 0.32796 0.22451 0.04900  -0.02377 0.02010  155 ASN A N   
1304 C CA  . ASN A 148 ? 0.27585 0.35954 0.22493 0.06152  -0.03068 0.02315  155 ASN A CA  
1305 C C   . ASN A 148 ? 0.30600 0.39806 0.23219 0.07050  -0.02824 0.02596  155 ASN A C   
1306 O O   . ASN A 148 ? 0.33076 0.44119 0.24256 0.08090  -0.03752 0.02047  155 ASN A O   
1307 C CB  . ASN A 148 ? 0.28267 0.36496 0.23364 0.06922  -0.02695 0.03892  155 ASN A CB  
1308 C CG  . ASN A 148 ? 0.33343 0.41974 0.30323 0.06716  -0.03227 0.03521  155 ASN A CG  
1309 O OD1 . ASN A 148 ? 0.31440 0.41265 0.29559 0.06149  -0.04157 0.02249  155 ASN A OD1 
1310 N ND2 . ASN A 148 ? 0.30889 0.38591 0.28316 0.07256  -0.02646 0.04707  155 ASN A ND2 
1311 N N   . ASP A 149 ? 0.31363 0.39528 0.23634 0.06754  -0.01620 0.03443  156 ASP A N   
1312 C CA  . ASP A 149 ? 0.34213 0.43529 0.24463 0.07744  -0.01013 0.04226  156 ASP A CA  
1313 C C   . ASP A 149 ? 0.42886 0.52696 0.32326 0.07733  -0.01196 0.02691  156 ASP A C   
1314 O O   . ASP A 149 ? 0.39821 0.50732 0.27680 0.08599  -0.00446 0.03353  156 ASP A O   
1315 C CB  . ASP A 149 ? 0.33663 0.41916 0.24363 0.07446  0.00480  0.06390  156 ASP A CB  
1316 C CG  . ASP A 149 ? 0.52543 0.60109 0.43576 0.07865  0.00694  0.08096  156 ASP A CG  
1317 O OD1 . ASP A 149 ? 0.41868 0.50480 0.32290 0.08790  -0.00186 0.07866  156 ASP A OD1 
1318 O OD2 . ASP A 149 ? 0.48712 0.54608 0.40778 0.07265  0.01642  0.09610  156 ASP A OD2 
1319 N N   . ASP A 150 ? 0.33930 0.42988 0.24449 0.06883  -0.02096 0.00798  157 ASP A N   
1320 C CA  . ASP A 150 ? 0.28664 0.37701 0.18508 0.06953  -0.02294 -0.00686 157 ASP A CA  
1321 C C   . ASP A 150 ? 0.37157 0.45802 0.27723 0.06504  -0.03907 -0.02834 157 ASP A C   
1322 O O   . ASP A 150 ? 0.35138 0.43930 0.26922 0.06057  -0.04767 -0.03016 157 ASP A O   
1323 C CB  . ASP A 150 ? 0.28725 0.36442 0.19832 0.05947  -0.01160 -0.00200 157 ASP A CB  
1324 C CG  . ASP A 150 ? 0.35866 0.44279 0.25701 0.06673  -0.00727 -0.00772 157 ASP A CG  
1325 O OD1 . ASP A 150 ? 0.35366 0.44758 0.23354 0.07871  -0.01523 -0.02114 157 ASP A OD1 
1326 O OD2 . ASP A 150 ? 0.39247 0.47307 0.29960 0.06130  0.00342  0.00032  157 ASP A OD2 
1327 N N   . GLU A 151 ? 0.35268 0.43449 0.25256 0.06650  -0.04319 -0.04393 158 GLU A N   
1328 C CA  . GLU A 151 ? 0.34935 0.42202 0.25885 0.06046  -0.05851 -0.06429 158 GLU A CA  
1329 C C   . GLU A 151 ? 0.28333 0.33736 0.21813 0.04425  -0.05470 -0.06296 158 GLU A C   
1330 O O   . GLU A 151 ? 0.30143 0.34991 0.24250 0.03950  -0.04141 -0.04984 158 GLU A O   
1331 C CB  . GLU A 151 ? 0.38092 0.45352 0.27023 0.07210  -0.06528 -0.08246 158 GLU A CB  
1332 C CG  . GLU A 151 ? 0.57090 0.66412 0.43052 0.09133  -0.07091 -0.08701 158 GLU A CG  
1333 C CD  . GLU A 151 ? 0.89175 0.99870 0.75325 0.09208  -0.08086 -0.08379 158 GLU A CD  
1334 O OE1 . GLU A 151 ? 0.99251 1.09378 0.87448 0.08076  -0.09483 -0.09392 158 GLU A OE1 
1335 O OE2 . GLU A 151 ? 0.93310 1.05815 0.77702 0.10435  -0.07451 -0.06967 158 GLU A OE2 
1336 N N   . GLN A 152 ? 0.28569 0.33044 0.23553 0.03583  -0.06726 -0.07647 159 GLN A N   
1337 C CA  . GLN A 152 ? 0.27498 0.30353 0.24771 0.02190  -0.06411 -0.07442 159 GLN A CA  
1338 C C   . GLN A 152 ? 0.26688 0.28125 0.23351 0.02404  -0.05958 -0.08043 159 GLN A C   
1339 O O   . GLN A 152 ? 0.31762 0.32762 0.27179 0.03193  -0.06795 -0.09591 159 GLN A O   
1340 C CB  . GLN A 152 ? 0.29465 0.31986 0.28905 0.01142  -0.07853 -0.08346 159 GLN A CB  
1341 C CG  . GLN A 152 ? 0.29832 0.31295 0.31838 -0.00259 -0.07316 -0.07512 159 GLN A CG  
1342 C CD  . GLN A 152 ? 0.32998 0.35121 0.37640 -0.01353 -0.08387 -0.07588 159 GLN A CD  
1343 O OE1 . GLN A 152 ? 0.34217 0.38187 0.39280 -0.01207 -0.08701 -0.07142 159 GLN A OE1 
1344 N NE2 . GLN A 152 ? 0.31654 0.32385 0.38293 -0.02449 -0.08919 -0.07984 159 GLN A NE2 
1345 N N   A TYR A 153 ? 0.25197 0.25944 0.22694 0.01837  -0.04738 -0.06931 160 TYR A N   
1346 N N   B TYR A 153 ? 0.25197 0.25944 0.22694 0.01837  -0.04738 -0.06931 160 TYR A N   
1347 C CA  A TYR A 153 ? 0.27451 0.27224 0.24526 0.02130  -0.04179 -0.07217 160 TYR A CA  
1348 C CA  B TYR A 153 ? 0.27451 0.27224 0.24526 0.02130  -0.04179 -0.07217 160 TYR A CA  
1349 C C   A TYR A 153 ? 0.32184 0.30506 0.31209 0.01006  -0.03950 -0.06811 160 TYR A C   
1350 C C   B TYR A 153 ? 0.32184 0.30506 0.31209 0.01006  -0.03950 -0.06811 160 TYR A C   
1351 O O   A TYR A 153 ? 0.25949 0.24392 0.26364 0.00132  -0.03686 -0.05865 160 TYR A O   
1352 O O   B TYR A 153 ? 0.25949 0.24392 0.26364 0.00132  -0.03686 -0.05865 160 TYR A O   
1353 C CB  A TYR A 153 ? 0.23889 0.24797 0.19828 0.02798  -0.02828 -0.06084 160 TYR A CB  
1354 C CB  B TYR A 153 ? 0.23889 0.24797 0.19828 0.02798  -0.02828 -0.06084 160 TYR A CB  
1355 C CG  A TYR A 153 ? 0.30181 0.32613 0.23877 0.04261  -0.02790 -0.06384 160 TYR A CG  
1356 C CG  B TYR A 153 ? 0.30181 0.32613 0.23877 0.04261  -0.02790 -0.06384 160 TYR A CG  
1357 C CD1 A TYR A 153 ? 0.35787 0.38285 0.28055 0.05456  -0.02884 -0.07498 160 TYR A CD1 
1358 C CD1 B TYR A 153 ? 0.35787 0.38285 0.28055 0.05456  -0.02884 -0.07498 160 TYR A CD1 
1359 C CD2 A TYR A 153 ? 0.32088 0.35984 0.24951 0.04664  -0.02602 -0.05472 160 TYR A CD2 
1360 C CD2 B TYR A 153 ? 0.32088 0.35984 0.24951 0.04664  -0.02602 -0.05472 160 TYR A CD2 
1361 C CE1 A TYR A 153 ? 0.36154 0.40381 0.26088 0.07071  -0.02737 -0.07727 160 TYR A CE1 
1362 C CE1 B TYR A 153 ? 0.36154 0.40381 0.26088 0.07071  -0.02737 -0.07727 160 TYR A CE1 
1363 C CE2 A TYR A 153 ? 0.35076 0.40638 0.25669 0.06187  -0.02464 -0.05524 160 TYR A CE2 
1364 C CE2 B TYR A 153 ? 0.35076 0.40638 0.25669 0.06187  -0.02464 -0.05524 160 TYR A CE2 
1365 C CZ  A TYR A 153 ? 0.40344 0.46188 0.29414 0.07412  -0.02500 -0.06664 160 TYR A CZ  
1366 C CZ  B TYR A 153 ? 0.40344 0.46188 0.29414 0.07412  -0.02500 -0.06664 160 TYR A CZ  
1367 O OH  A TYR A 153 ? 0.54534 0.62354 0.41075 0.09192  -0.02251 -0.06674 160 TYR A OH  
1368 O OH  B TYR A 153 ? 0.54534 0.62354 0.41075 0.09192  -0.02251 -0.06674 160 TYR A OH  
1369 N N   . ALA A 154 ? 0.23952 0.21009 0.22910 0.01255  -0.03999 -0.07472 161 ALA A N   
1370 C CA  . ALA A 154 ? 0.24891 0.20633 0.25358 0.00485  -0.03688 -0.06941 161 ALA A CA  
1371 C C   . ALA A 154 ? 0.29126 0.25063 0.28913 0.01098  -0.02711 -0.06496 161 ALA A C   
1372 O O   . ALA A 154 ? 0.27725 0.23628 0.26345 0.02160  -0.02755 -0.07305 161 ALA A O   
1373 C CB  . ALA A 154 ? 0.33367 0.27163 0.34785 0.00176  -0.04792 -0.07997 161 ALA A CB  
1374 N N   . TRP A 155 ? 0.21607 0.17894 0.22144 0.00532  -0.01910 -0.05299 162 TRP A N   
1375 C CA  . TRP A 155 ? 0.22770 0.19355 0.23221 0.00845  -0.01177 -0.04810 162 TRP A CA  
1376 C C   . TRP A 155 ? 0.25288 0.20504 0.26718 0.00527  -0.01295 -0.04628 162 TRP A C   
1377 O O   . TRP A 155 ? 0.25944 0.20440 0.28375 -0.00226 -0.01536 -0.04262 162 TRP A O   
1378 C CB  . TRP A 155 ? 0.23150 0.20905 0.23772 0.00427  -0.00463 -0.03755 162 TRP A CB  
1379 C CG  . TRP A 155 ? 0.24118 0.22469 0.25070 0.00446  0.00109  -0.03194 162 TRP A CG  
1380 C CD1 . TRP A 155 ? 0.22378 0.22158 0.23186 0.00714  0.00635  -0.02792 162 TRP A CD1 
1381 C CD2 . TRP A 155 ? 0.22836 0.20676 0.24475 0.00133  0.00155  -0.02856 162 TRP A CD2 
1382 N NE1 . TRP A 155 ? 0.20719 0.20883 0.22305 0.00472  0.00841  -0.02392 162 TRP A NE1 
1383 C CE2 . TRP A 155 ? 0.23397 0.22366 0.25274 0.00224  0.00516  -0.02503 162 TRP A CE2 
1384 C CE3 . TRP A 155 ? 0.21650 0.18408 0.23772 -0.00163 -0.00063 -0.02703 162 TRP A CE3 
1385 C CZ2 . TRP A 155 ? 0.24087 0.23090 0.26446 0.00117  0.00481  -0.02250 162 TRP A CZ2 
1386 C CZ3 . TRP A 155 ? 0.23538 0.20345 0.25907 -0.00131 0.00095  -0.02268 162 TRP A CZ3 
1387 C CH2 . TRP A 155 ? 0.23822 0.21723 0.26198 0.00049  0.00276  -0.02166 162 TRP A CH2 
1388 N N   . GLU A 156 ? 0.22208 0.17277 0.23424 0.01201  -0.01066 -0.04718 163 GLU A N   
1389 C CA  . GLU A 156 ? 0.21005 0.14747 0.22994 0.01105  -0.01164 -0.04373 163 GLU A CA  
1390 C C   . GLU A 156 ? 0.25565 0.20091 0.27369 0.01807  -0.00693 -0.04030 163 GLU A C   
1391 O O   . GLU A 156 ? 0.23020 0.18530 0.24202 0.02671  -0.00505 -0.04482 163 GLU A O   
1392 C CB  . GLU A 156 ? 0.28410 0.20080 0.30619 0.01354  -0.01960 -0.05237 163 GLU A CB  
1393 C CG  . GLU A 156 ? 0.35962 0.25977 0.39351 0.00951  -0.02073 -0.04486 163 GLU A CG  
1394 C CD  . GLU A 156 ? 0.57400 0.45020 0.61550 0.00746  -0.03043 -0.05252 163 GLU A CD  
1395 O OE1 . GLU A 156 ? 0.46150 0.32381 0.49658 0.01763  -0.03492 -0.06287 163 GLU A OE1 
1396 O OE2 . GLU A 156 ? 0.43875 0.31030 0.49393 -0.00404 -0.03411 -0.04855 163 GLU A OE2 
1397 N N   . SER A 157 ? 0.24215 0.18595 0.26566 0.01551  -0.00506 -0.03183 164 SER A N   
1398 C CA  . SER A 157 ? 0.20843 0.16017 0.23148 0.02288  -0.00279 -0.02895 164 SER A CA  
1399 C C   . SER A 157 ? 0.24000 0.18230 0.26671 0.02340  -0.00314 -0.02075 164 SER A C   
1400 O O   . SER A 157 ? 0.25142 0.19176 0.28065 0.01657  -0.00209 -0.01400 164 SER A O   
1401 C CB  . SER A 157 ? 0.20736 0.18055 0.23098 0.02039  0.00063  -0.02605 164 SER A CB  
1402 O OG  . SER A 157 ? 0.21433 0.19843 0.24034 0.02743  0.00113  -0.02397 164 SER A OG  
1403 N N   . SER A 158 ? 0.23270 0.17103 0.25899 0.03342  -0.00390 -0.02023 165 SER A N   
1404 C CA  . SER A 158 ? 0.27004 0.20509 0.29764 0.03725  -0.00339 -0.01020 165 SER A CA  
1405 C C   . SER A 158 ? 0.27437 0.23183 0.30000 0.04316  -0.00262 -0.00838 165 SER A C   
1406 O O   . SER A 158 ? 0.31401 0.27214 0.33889 0.05206  -0.00338 -0.00249 165 SER A O   
1407 C CB  . SER A 158 ? 0.34260 0.25486 0.37244 0.04516  -0.00592 -0.00921 165 SER A CB  
1408 O OG  . SER A 158 ? 0.35480 0.24552 0.39061 0.03712  -0.00868 -0.01028 165 SER A OG  
1409 N N   . ALA A 159 ? 0.23775 0.21366 0.26413 0.03810  -0.00189 -0.01269 166 ALA A N   
1410 C CA  . ALA A 159 ? 0.26497 0.26457 0.29467 0.04071  -0.00292 -0.01251 166 ALA A CA  
1411 C C   . ALA A 159 ? 0.28989 0.29678 0.32246 0.05318  -0.00259 -0.01446 166 ALA A C   
1412 O O   . ALA A 159 ? 0.34337 0.34145 0.37387 0.05769  -0.00086 -0.01974 166 ALA A O   
1413 C CB  . ALA A 159 ? 0.32812 0.33245 0.35474 0.04093  -0.00561 -0.00697 166 ALA A CB  
1414 N N   . GLY A 160 ? 0.27754 0.30171 0.31413 0.06059  -0.00480 -0.01132 167 GLY A N   
1415 C CA  . GLY A 160 ? 0.26751 0.30207 0.30794 0.07424  -0.00372 -0.01291 167 GLY A CA  
1416 C C   . GLY A 160 ? 0.32802 0.38437 0.37567 0.07354  0.00020  -0.01701 167 GLY A C   
1417 O O   . GLY A 160 ? 0.29551 0.36056 0.34438 0.08703  0.00287  -0.01918 167 GLY A O   
1418 N N   . GLY A 161 ? 0.20126 0.26676 0.25346 0.05959  0.00132  -0.01709 168 GLY A N   
1419 C CA  . GLY A 161 ? 0.20564 0.29690 0.26815 0.05753  0.00586  -0.01637 168 GLY A CA  
1420 C C   . GLY A 161 ? 0.23815 0.32252 0.29278 0.05765  0.01155  -0.01970 168 GLY A C   
1421 O O   . GLY A 161 ? 0.19934 0.30671 0.26157 0.05644  0.01700  -0.01638 168 GLY A O   
1422 N N   . SER A 162 ? 0.20635 0.26194 0.24710 0.05901  0.01016  -0.02526 169 SER A N   
1423 C CA  . SER A 162 ? 0.20313 0.25344 0.23438 0.06123  0.01340  -0.03043 169 SER A CA  
1424 C C   . SER A 162 ? 0.20177 0.22609 0.22552 0.05132  0.00961  -0.03339 169 SER A C   
1425 O O   . SER A 162 ? 0.23768 0.24481 0.26209 0.04643  0.00551  -0.03192 169 SER A O   
1426 C CB  . SER A 162 ? 0.28445 0.33015 0.30629 0.07986  0.01426  -0.03839 169 SER A CB  
1427 O OG  . SER A 162 ? 0.26066 0.27483 0.27642 0.08338  0.00801  -0.04365 169 SER A OG  
1428 N N   . PHE A 163 ? 0.20287 0.22792 0.21994 0.04939  0.01153  -0.03620 170 PHE A N   
1429 C CA  . PHE A 163 ? 0.22577 0.22986 0.23637 0.04243  0.00731  -0.04027 170 PHE A CA  
1430 C C   . PHE A 163 ? 0.23229 0.23413 0.23016 0.05173  0.00653  -0.04959 170 PHE A C   
1431 O O   . PHE A 163 ? 0.23137 0.25145 0.22406 0.06279  0.01152  -0.05067 170 PHE A O   
1432 C CB  . PHE A 163 ? 0.19593 0.20414 0.21115 0.02862  0.00848  -0.03345 170 PHE A CB  
1433 C CG  . PHE A 163 ? 0.18466 0.21365 0.20097 0.02735  0.01428  -0.02816 170 PHE A CG  
1434 C CD1 . PHE A 163 ? 0.21034 0.25910 0.23875 0.02423  0.01817  -0.02033 170 PHE A CD1 
1435 C CD2 . PHE A 163 ? 0.21609 0.24554 0.22300 0.02863  0.01528  -0.02969 170 PHE A CD2 
1436 C CE1 . PHE A 163 ? 0.21367 0.28116 0.24706 0.02133  0.02418  -0.01222 170 PHE A CE1 
1437 C CE2 . PHE A 163 ? 0.18908 0.23768 0.19704 0.02806  0.02180  -0.02142 170 PHE A CE2 
1438 C CZ  . PHE A 163 ? 0.23131 0.29826 0.25377 0.02364  0.02686  -0.01161 170 PHE A CZ  
1439 N N   . THR A 164 ? 0.23837 0.21972 0.23143 0.04809  -0.00018 -0.05650 171 THR A N   
1440 C CA  . THR A 164 ? 0.24629 0.22433 0.22572 0.05644  -0.00400 -0.06787 171 THR A CA  
1441 C C   . THR A 164 ? 0.23910 0.21924 0.21666 0.04701  -0.00596 -0.06610 171 THR A C   
1442 O O   . THR A 164 ? 0.22396 0.19926 0.21163 0.03408  -0.00654 -0.05889 171 THR A O   
1443 C CB  . THR A 164 ? 0.29118 0.24165 0.26741 0.06236  -0.01376 -0.08116 171 THR A CB  
1444 O OG1 . THR A 164 ? 0.31116 0.24252 0.29909 0.04804  -0.01982 -0.07847 171 THR A OG1 
1445 C CG2 . THR A 164 ? 0.28067 0.22631 0.25825 0.07401  -0.01207 -0.08230 171 THR A CG2 
1446 N N   . VAL A 165 ? 0.25361 0.24311 0.21667 0.05583  -0.00663 -0.07241 172 VAL A N   
1447 C CA  . VAL A 165 ? 0.26138 0.25341 0.21988 0.05052  -0.01020 -0.07234 172 VAL A CA  
1448 C C   . VAL A 165 ? 0.31535 0.30009 0.25805 0.06153  -0.02017 -0.08954 172 VAL A C   
1449 O O   . VAL A 165 ? 0.30237 0.29421 0.22986 0.07782  -0.01861 -0.09751 172 VAL A O   
1450 C CB  . VAL A 165 ? 0.29635 0.31249 0.25163 0.05053  -0.00032 -0.05906 172 VAL A CB  
1451 C CG1 . VAL A 165 ? 0.29079 0.30896 0.23941 0.04799  -0.00473 -0.05892 172 VAL A CG1 
1452 C CG2 . VAL A 165 ? 0.23696 0.25682 0.20889 0.03871  0.00652  -0.04498 172 VAL A CG2 
1453 N N   . ARG A 166 ? 0.28237 0.25460 0.22893 0.05357  -0.03104 -0.09596 173 ARG A N   
1454 C CA  . ARG A 166 ? 0.32686 0.29228 0.25932 0.06277  -0.04370 -0.11439 173 ARG A CA  
1455 C C   . ARG A 166 ? 0.31521 0.28602 0.25039 0.05448  -0.05104 -0.11373 173 ARG A C   
1456 O O   . ARG A 166 ? 0.28500 0.25713 0.23688 0.04044  -0.04807 -0.10115 173 ARG A O   
1457 C CB  . ARG A 166 ? 0.34981 0.28588 0.28926 0.06221  -0.05556 -0.12925 173 ARG A CB  
1458 C CG  . ARG A 166 ? 0.40731 0.32628 0.37191 0.04289  -0.06223 -0.12453 173 ARG A CG  
1459 C CD  . ARG A 166 ? 0.54789 0.43837 0.52468 0.04070  -0.06727 -0.12921 173 ARG A CD  
1460 N NE  . ARG A 166 ? 0.60152 0.49408 0.57824 0.04608  -0.05501 -0.11909 173 ARG A NE  
1461 C CZ  . ARG A 166 ? 0.75008 0.62080 0.73322 0.04897  -0.05685 -0.12098 173 ARG A CZ  
1462 N NH1 . ARG A 166 ? 0.58014 0.42163 0.57032 0.04699  -0.07027 -0.13306 173 ARG A NH1 
1463 N NH2 . ARG A 166 ? 0.78818 0.66611 0.77197 0.05394  -0.04590 -0.11029 173 ARG A NH2 
1464 N N   . THR A 167 ? 0.33399 0.30966 0.25126 0.06535  -0.06099 -0.12799 174 THR A N   
1465 C CA  . THR A 167 ? 0.41566 0.39547 0.33688 0.05856  -0.07218 -0.13109 174 THR A CA  
1466 C C   . THR A 167 ? 0.41671 0.37452 0.36370 0.04231  -0.08417 -0.13674 174 THR A C   
1467 O O   . THR A 167 ? 0.43191 0.36718 0.38296 0.04284  -0.09223 -0.14957 174 THR A O   
1468 C CB  . THR A 167 ? 0.47332 0.46220 0.36820 0.07541  -0.08323 -0.14847 174 THR A CB  
1469 O OG1 . THR A 167 ? 0.51727 0.53129 0.38984 0.09016  -0.06954 -0.13784 174 THR A OG1 
1470 C CG2 . THR A 167 ? 0.60984 0.60373 0.51124 0.06827  -0.09809 -0.15379 174 THR A CG2 
1471 N N   . ASP A 168 ? 0.32453 0.28904 0.29031 0.02839  -0.08460 -0.12566 175 ASP A N   
1472 C CA  . ASP A 168 ? 0.39108 0.34064 0.38547 0.01184  -0.09306 -0.12577 175 ASP A CA  
1473 C C   . ASP A 168 ? 0.50935 0.45897 0.50910 0.00903  -0.11330 -0.14173 175 ASP A C   
1474 O O   . ASP A 168 ? 0.49560 0.46601 0.49047 0.01120  -0.11699 -0.14044 175 ASP A O   
1475 C CB  . ASP A 168 ? 0.38316 0.34289 0.39623 -0.00016 -0.08201 -0.10500 175 ASP A CB  
1476 C CG  . ASP A 168 ? 0.46863 0.41698 0.51200 -0.01611 -0.08694 -0.10077 175 ASP A CG  
1477 O OD1 . ASP A 168 ? 0.67665 0.60327 0.72764 -0.01904 -0.09001 -0.10539 175 ASP A OD1 
1478 O OD2 . ASP A 168 ? 0.40381 0.36590 0.46412 -0.02485 -0.08732 -0.09160 175 ASP A OD2 
1479 N N   . THR A 169 ? 0.62693 0.55456 0.63771 0.00440  -0.12453 -0.15305 176 THR A N   
1480 C CA  . THR A 169 ? 0.94191 0.87000 0.96321 -0.00100 -0.13989 -0.16177 176 THR A CA  
1481 C C   . THR A 169 ? 0.80464 0.73194 0.86355 -0.02202 -0.14302 -0.15038 176 THR A C   
1482 O O   . THR A 169 ? 0.68865 0.61617 0.76189 -0.02932 -0.15576 -0.15624 176 THR A O   
1483 C CB  . THR A 169 ? 0.88407 0.79086 0.89566 0.00697  -0.14782 -0.17689 176 THR A CB  
1484 O OG1 . THR A 169 ? 0.86579 0.75011 0.88409 0.00488  -0.13982 -0.17156 176 THR A OG1 
1485 C CG2 . THR A 169 ? 0.62541 0.54259 0.60043 0.02949  -0.14779 -0.18921 176 THR A CG2 
1486 N N   . GLY A 170 ? 0.74040 0.66879 0.81583 -0.03125 -0.13125 -0.13365 177 GLY A N   
1487 C CA  . GLY A 170 ? 0.85310 0.78483 0.96383 -0.04925 -0.13061 -0.11912 177 GLY A CA  
1488 C C   . GLY A 170 ? 0.59083 0.55115 0.71586 -0.05513 -0.13581 -0.11457 177 GLY A C   
1489 O O   . GLY A 170 ? 0.53053 0.50547 0.63860 -0.04594 -0.14424 -0.12544 177 GLY A O   
1490 N N   . GLU A 171 ? 0.63200 0.60299 0.78760 -0.06868 -0.13003 -0.09715 178 GLU A N   
1491 C CA  . GLU A 171 ? 0.49550 0.49699 0.66968 -0.07403 -0.13373 -0.09022 178 GLU A CA  
1492 C C   . GLU A 171 ? 0.40693 0.42779 0.55712 -0.06014 -0.12685 -0.08818 178 GLU A C   
1493 O O   . GLU A 171 ? 0.31597 0.33326 0.45070 -0.05359 -0.10883 -0.07664 178 GLU A O   
1494 C CB  . GLU A 171 ? 0.52131 0.53273 0.72904 -0.08737 -0.12312 -0.06825 178 GLU A CB  
1495 C CG  . GLU A 171 ? 0.68587 0.72304 0.92239 -0.09716 -0.12975 -0.06203 178 GLU A CG  
1496 C CD  . GLU A 171 ? 0.53908 0.56636 0.78002 -0.10271 -0.14663 -0.07691 178 GLU A CD  
1497 O OE1 . GLU A 171 ? 0.53699 0.57833 0.76908 -0.09753 -0.15958 -0.08976 178 GLU A OE1 
1498 O OE2 . GLU A 171 ? 0.55522 0.56047 0.80786 -0.11130 -0.14742 -0.07571 178 GLU A OE2 
1499 N N   . PRO A 172 ? 0.38891 0.42926 0.53087 -0.05348 -0.13803 -0.09667 179 PRO A N   
1500 C CA  . PRO A 172 ? 0.35752 0.41460 0.47336 -0.03845 -0.12738 -0.08934 179 PRO A CA  
1501 C C   . PRO A 172 ? 0.44110 0.51290 0.57089 -0.04074 -0.11121 -0.06772 179 PRO A C   
1502 O O   . PRO A 172 ? 0.46212 0.54753 0.62396 -0.05169 -0.11289 -0.05927 179 PRO A O   
1503 C CB  . PRO A 172 ? 0.42870 0.50613 0.54040 -0.03275 -0.14547 -0.10133 179 PRO A CB  
1504 C CG  . PRO A 172 ? 0.64243 0.70388 0.75997 -0.03914 -0.16412 -0.12137 179 PRO A CG  
1505 C CD  . PRO A 172 ? 0.46918 0.51098 0.61446 -0.05560 -0.15796 -0.11324 179 PRO A CD  
1506 N N   . MET A 173 ? 0.27776 0.34758 0.38383 -0.02966 -0.09572 -0.05886 180 MET A N   
1507 C CA  . MET A 173 ? 0.27743 0.35490 0.39091 -0.02908 -0.08015 -0.04124 180 MET A CA  
1508 C C   . MET A 173 ? 0.39457 0.49352 0.50358 -0.01914 -0.07874 -0.03394 180 MET A C   
1509 O O   . MET A 173 ? 0.46051 0.57057 0.58238 -0.01860 -0.06990 -0.02136 180 MET A O   
1510 C CB  . MET A 173 ? 0.32430 0.38280 0.41792 -0.02438 -0.06503 -0.03631 180 MET A CB  
1511 C CG  . MET A 173 ? 0.67688 0.71649 0.77778 -0.03273 -0.06235 -0.03783 180 MET A CG  
1512 S SD  . MET A 173 ? 0.65597 0.68098 0.73673 -0.02650 -0.04555 -0.03063 180 MET A SD  
1513 C CE  . MET A 173 ? 0.45092 0.49033 0.53017 -0.01983 -0.03609 -0.01807 180 MET A CE  
1514 N N   . GLY A 174 ? 0.32593 0.43109 0.41524 -0.00913 -0.08644 -0.04074 181 GLY A N   
1515 C CA  . GLY A 174 ? 0.34223 0.46522 0.42498 0.00233  -0.08428 -0.03180 181 GLY A CA  
1516 C C   . GLY A 174 ? 0.25652 0.36585 0.31592 0.01207  -0.06891 -0.02202 181 GLY A C   
1517 O O   . GLY A 174 ? 0.26063 0.36983 0.29687 0.02264  -0.06912 -0.02177 181 GLY A O   
1518 N N   . ARG A 175 ? 0.19910 0.29745 0.26492 0.00867  -0.05599 -0.01355 182 ARG A N   
1519 C CA  . ARG A 175 ? 0.21713 0.29865 0.26506 0.01472  -0.04310 -0.00615 182 ARG A CA  
1520 C C   . ARG A 175 ? 0.25061 0.32053 0.30788 0.00868  -0.03318 -0.00229 182 ARG A C   
1521 O O   . ARG A 175 ? 0.20902 0.28981 0.28433 0.00649  -0.03180 0.00190  182 ARG A O   
1522 C CB  . ARG A 175 ? 0.20192 0.28977 0.24213 0.02701  -0.03971 0.00412  182 ARG A CB  
1523 C CG  . ARG A 175 ? 0.20442 0.27179 0.22780 0.03169  -0.02868 0.01149  182 ARG A CG  
1524 C CD  . ARG A 175 ? 0.21165 0.27865 0.23328 0.04264  -0.02432 0.02250  182 ARG A CD  
1525 N NE  . ARG A 175 ? 0.20428 0.27592 0.24170 0.04313  -0.02143 0.02389  182 ARG A NE  
1526 C CZ  . ARG A 175 ? 0.20574 0.29914 0.25580 0.04923  -0.02565 0.02676  182 ARG A CZ  
1527 N NH1 . ARG A 175 ? 0.21887 0.33077 0.26788 0.05486  -0.03476 0.02752  182 ARG A NH1 
1528 N NH2 . ARG A 175 ? 0.20096 0.30072 0.26491 0.05101  -0.02068 0.02920  182 ARG A NH2 
1529 N N   . GLY A 176 ? 0.37447 0.36175 0.16921 0.09124  -0.03387 0.02528  183 GLY A N   
1530 C CA  . GLY A 176 ? 0.32791 0.31639 0.16934 0.07323  -0.02521 0.02454  183 GLY A CA  
1531 C C   . GLY A 176 ? 0.32133 0.29859 0.17283 0.05948  -0.01449 0.01638  183 GLY A C   
1532 O O   . GLY A 176 ? 0.34723 0.30989 0.17022 0.06717  -0.00460 0.01653  183 GLY A O   
1533 N N   . THR A 177 ? 0.27262 0.25792 0.16293 0.04224  -0.01576 0.01027  184 THR A N   
1534 C CA  . THR A 177 ? 0.25615 0.23509 0.16173 0.03147  -0.00632 0.00498  184 THR A CA  
1535 C C   . THR A 177 ? 0.36130 0.35124 0.29100 0.01602  -0.02028 -0.00791 184 THR A C   
1536 O O   . THR A 177 ? 0.25945 0.26428 0.21030 0.00978  -0.02865 -0.00803 184 THR A O   
1537 C CB  . THR A 177 ? 0.29779 0.27223 0.22691 0.02708  0.01332  0.01730  184 THR A CB  
1538 O OG1 . THR A 177 ? 0.32007 0.28145 0.22669 0.03940  0.03021  0.03170  184 THR A OG1 
1539 C CG2 . THR A 177 ? 0.27170 0.25054 0.22308 0.01774  0.02005  0.01289  184 THR A CG2 
1540 N N   . LYS A 178 ? 0.23425 0.21412 0.15800 0.01209  -0.02023 -0.01727 185 LYS A N   
1541 C CA  . LYS A 178 ? 0.24091 0.22235 0.18259 -0.00204 -0.02938 -0.02700 185 LYS A CA  
1542 C C   . LYS A 178 ? 0.27189 0.24586 0.22643 -0.00190 -0.01596 -0.02422 185 LYS A C   
1543 O O   . LYS A 178 ? 0.29274 0.25258 0.22844 0.00865  -0.00611 -0.02489 185 LYS A O   
1544 C CB  . LYS A 178 ? 0.30609 0.27534 0.22225 -0.00584 -0.04414 -0.04175 185 LYS A CB  
1545 C CG  . LYS A 178 ? 0.45688 0.41846 0.38648 -0.02212 -0.05140 -0.05073 185 LYS A CG  
1546 C CD  . LYS A 178 ? 0.62231 0.55932 0.52134 -0.02854 -0.06429 -0.06769 185 LYS A CD  
1547 C CE  . LYS A 178 ? 0.68680 0.62739 0.55317 -0.02055 -0.07635 -0.07431 185 LYS A CE  
1548 N NZ  . LYS A 178 ? 0.84437 0.82493 0.73160 -0.02492 -0.09061 -0.06941 185 LYS A NZ  
1549 N N   . VAL A 179 ? 0.22897 0.21487 0.21369 -0.01076 -0.01536 -0.02059 186 VAL A N   
1550 C CA  . VAL A 179 ? 0.18664 0.17323 0.18658 -0.00996 -0.00698 -0.01756 186 VAL A CA  
1551 C C   . VAL A 179 ? 0.24108 0.21734 0.24117 -0.01637 -0.01465 -0.02398 186 VAL A C   
1552 O O   . VAL A 179 ? 0.22334 0.20762 0.23634 -0.02714 -0.02237 -0.02459 186 VAL A O   
1553 C CB  . VAL A 179 ? 0.18769 0.19269 0.21590 -0.01539 -0.00294 -0.00998 186 VAL A CB  
1554 C CG1 . VAL A 179 ? 0.18685 0.20140 0.23276 -0.01381 0.00144  -0.00706 186 VAL A CG1 
1555 C CG2 . VAL A 179 ? 0.20780 0.21502 0.23538 -0.01197 0.00718  -0.00210 186 VAL A CG2 
1556 N N   . ILE A 180 ? 0.23527 0.19063 0.21879 -0.00830 -0.01013 -0.02755 187 ILE A N   
1557 C CA  . ILE A 180 ? 0.23745 0.17144 0.21536 -0.01311 -0.01441 -0.03203 187 ILE A CA  
1558 C C   . ILE A 180 ? 0.23608 0.17685 0.22965 -0.00407 -0.00680 -0.02307 187 ILE A C   
1559 O O   . ILE A 180 ? 0.23348 0.17538 0.22485 0.01217  0.00369  -0.01927 187 ILE A O   
1560 C CB  . ILE A 180 ? 0.25828 0.15425 0.20036 -0.00862 -0.01515 -0.04354 187 ILE A CB  
1561 C CG1 . ILE A 180 ? 0.27051 0.16758 0.19566 -0.01593 -0.02624 -0.05294 187 ILE A CG1 
1562 C CG2 . ILE A 180 ? 0.30007 0.16448 0.23509 -0.01708 -0.01850 -0.04752 187 ILE A CG2 
1563 C CD1 . ILE A 180 ? 0.42848 0.28830 0.31030 -0.00940 -0.02814 -0.06704 187 ILE A CD1 
1564 N N   . LEU A 181 ? 0.21803 0.16720 0.22707 -0.01254 -0.01176 -0.01870 188 LEU A N   
1565 C CA  . LEU A 181 ? 0.22290 0.18310 0.24484 -0.00325 -0.00857 -0.00971 188 LEU A CA  
1566 C C   . LEU A 181 ? 0.25145 0.17657 0.25472 0.00201  -0.00659 -0.00837 188 LEU A C   
1567 O O   . LEU A 181 ? 0.27288 0.18345 0.27175 -0.01115 -0.01076 -0.00846 188 LEU A O   
1568 C CB  . LEU A 181 ? 0.17173 0.15845 0.21323 -0.01293 -0.01502 -0.00575 188 LEU A CB  
1569 C CG  . LEU A 181 ? 0.23923 0.24970 0.29544 -0.01984 -0.01661 -0.00762 188 LEU A CG  
1570 C CD1 . LEU A 181 ? 0.25704 0.28296 0.32334 -0.02745 -0.02276 -0.00660 188 LEU A CD1 
1571 C CD2 . LEU A 181 ? 0.22527 0.25278 0.29432 -0.01169 -0.01000 -0.00403 188 LEU A CD2 
1572 N N   . HIS A 182 ? 0.24562 0.15624 0.23825 0.02221  0.00190  -0.00552 189 HIS A N   
1573 C CA  . HIS A 182 ? 0.28285 0.15339 0.25469 0.03213  0.00610  -0.00173 189 HIS A CA  
1574 C C   . HIS A 182 ? 0.27972 0.17503 0.26787 0.04153  0.00432  0.01242  189 HIS A C   
1575 O O   . HIS A 182 ? 0.27436 0.19852 0.27702 0.06090  0.00709  0.01993  189 HIS A O   
1576 C CB  . HIS A 182 ? 0.32402 0.16424 0.27212 0.05495  0.01740  -0.00499 189 HIS A CB  
1577 C CG  . HIS A 182 ? 0.41023 0.23092 0.33705 0.04861  0.01778  -0.01998 189 HIS A CG  
1578 N ND1 . HIS A 182 ? 0.48742 0.25249 0.37874 0.04035  0.01556  -0.03330 189 HIS A ND1 
1579 C CD2 . HIS A 182 ? 0.36122 0.20958 0.29446 0.04871  0.01916  -0.02359 189 HIS A CD2 
1580 C CE1 . HIS A 182 ? 0.43180 0.19452 0.30666 0.03743  0.01335  -0.04576 189 HIS A CE1 
1581 N NE2 . HIS A 182 ? 0.45462 0.26659 0.35321 0.04408  0.01693  -0.03854 189 HIS A NE2 
1582 N N   . LEU A 183 ? 0.27890 0.16754 0.26530 0.02808  -0.00058 0.01664  190 LEU A N   
1583 C CA  . LEU A 183 ? 0.28904 0.20803 0.28762 0.03379  -0.00560 0.02793  190 LEU A CA  
1584 C C   . LEU A 183 ? 0.34020 0.24544 0.32635 0.06031  -0.00102 0.04133  190 LEU A C   
1585 O O   . LEU A 183 ? 0.34359 0.19818 0.30430 0.06924  0.00797  0.04393  190 LEU A O   
1586 C CB  . LEU A 183 ? 0.27882 0.19253 0.27341 0.01482  -0.00849 0.03001  190 LEU A CB  
1587 C CG  . LEU A 183 ? 0.27671 0.21471 0.28698 -0.00588 -0.01374 0.02002  190 LEU A CG  
1588 C CD1 . LEU A 183 ? 0.30281 0.24088 0.31033 -0.01912 -0.01309 0.02494  190 LEU A CD1 
1589 C CD2 . LEU A 183 ? 0.27639 0.25606 0.30676 -0.00248 -0.02000 0.01636  190 LEU A CD2 
1590 N N   . LYS A 184 ? 0.27319 0.22284 0.27612 0.07333  -0.00834 0.04959  191 LYS A N   
1591 C CA  . LYS A 184 ? 0.31243 0.25893 0.30450 0.10114  -0.00734 0.06536  191 LYS A CA  
1592 C C   . LYS A 184 ? 0.37608 0.27891 0.33755 0.09856  -0.00354 0.07564  191 LYS A C   
1593 O O   . LYS A 184 ? 0.38198 0.28010 0.34049 0.07499  -0.00514 0.07203  191 LYS A O   
1594 C CB  . LYS A 184 ? 0.32889 0.34033 0.34687 0.11054  -0.02135 0.07043  191 LYS A CB  
1595 C CG  . LYS A 184 ? 0.34440 0.40451 0.39859 0.11475  -0.02289 0.06540  191 LYS A CG  
1596 C CD  . LYS A 184 ? 0.40182 0.52648 0.48576 0.10855  -0.04104 0.06482  191 LYS A CD  
1597 C CE  . LYS A 184 ? 0.56744 0.74250 0.69395 0.10469  -0.04107 0.06045  191 LYS A CE  
1598 N NZ  . LYS A 184 ? 0.53555 0.77249 0.69382 0.09389  -0.06091 0.05799  191 LYS A NZ  
1599 N N   . GLU A 185 ? 0.41360 0.28529 0.35240 0.12544  0.00354  0.09082  192 GLU A N   
1600 C CA  . GLU A 185 ? 0.52913 0.34750 0.43463 0.12438  0.01199  0.10408  192 GLU A CA  
1601 C C   . GLU A 185 ? 0.52309 0.36935 0.42636 0.11555  0.00423  0.11190  192 GLU A C   
1602 O O   . GLU A 185 ? 0.57553 0.38815 0.46130 0.09859  0.01270  0.11746  192 GLU A O   
1603 C CB  . GLU A 185 ? 0.61905 0.40509 0.50108 0.15857  0.02040  0.11967  192 GLU A CB  
1604 C CG  . GLU A 185 ? 0.78445 0.50678 0.63470 0.14985  0.03312  0.12740  192 GLU A CG  
1605 C CD  . GLU A 185 ? 1.17644 0.87727 1.00886 0.17808  0.04059  0.13629  192 GLU A CD  
1606 O OE1 . GLU A 185 ? 1.06325 0.81117 0.90824 0.20530  0.03360  0.14153  192 GLU A OE1 
1607 O OE2 . GLU A 185 ? 1.31994 0.95906 1.12758 0.17192  0.05313  0.13783  192 GLU A OE2 
1608 N N   A ASP A 186 ? 0.43232 0.33965 0.35229 0.12589  -0.01129 0.11198  193 ASP A N   
1609 N N   B ASP A 186 ? 0.43232 0.33965 0.35229 0.12589  -0.01129 0.11198  193 ASP A N   
1610 C CA  A ASP A 186 ? 0.46626 0.39782 0.37543 0.12208  -0.01997 0.11740  193 ASP A CA  
1611 C CA  B ASP A 186 ? 0.46626 0.39782 0.37543 0.12208  -0.01997 0.11740  193 ASP A CA  
1612 C C   A ASP A 186 ? 0.39453 0.35708 0.32344 0.09311  -0.02724 0.09901  193 ASP A C   
1613 C C   B ASP A 186 ? 0.39453 0.35708 0.32344 0.09311  -0.02724 0.09901  193 ASP A C   
1614 O O   A ASP A 186 ? 0.40223 0.39134 0.32303 0.09160  -0.03678 0.09849  193 ASP A O   
1615 O O   B ASP A 186 ? 0.40223 0.39134 0.32303 0.09160  -0.03678 0.09849  193 ASP A O   
1616 C CB  A ASP A 186 ? 0.48679 0.46362 0.39552 0.15110  -0.03601 0.12725  193 ASP A CB  
1617 C CB  B ASP A 186 ? 0.48679 0.46362 0.39552 0.15110  -0.03601 0.12725  193 ASP A CB  
1618 C CG  A ASP A 186 ? 0.49964 0.53587 0.45028 0.15203  -0.05051 0.11403  193 ASP A CG  
1619 C CG  B ASP A 186 ? 0.49964 0.53587 0.45028 0.15203  -0.05051 0.11403  193 ASP A CG  
1620 O OD1 A ASP A 186 ? 0.60911 0.64517 0.58404 0.13383  -0.04531 0.09936  193 ASP A OD1 
1621 O OD1 B ASP A 186 ? 0.60911 0.64517 0.58404 0.13383  -0.04531 0.09936  193 ASP A OD1 
1622 O OD2 A ASP A 186 ? 0.64106 0.72342 0.60243 0.16508  -0.06562 0.11565  193 ASP A OD2 
1623 O OD2 B ASP A 186 ? 0.64106 0.72342 0.60243 0.16508  -0.06562 0.11565  193 ASP A OD2 
1624 N N   . GLN A 187 ? 0.31653 0.27288 0.26609 0.07267  -0.02275 0.08402  194 GLN A N   
1625 C CA  . GLN A 187 ? 0.29010 0.27207 0.25768 0.04931  -0.02822 0.06799  194 GLN A CA  
1626 C C   . GLN A 187 ? 0.30890 0.26126 0.27404 0.02699  -0.01648 0.06419  194 GLN A C   
1627 O O   . GLN A 187 ? 0.32051 0.28741 0.30331 0.01030  -0.01853 0.05083  194 GLN A O   
1628 C CB  . GLN A 187 ? 0.23919 0.25239 0.23746 0.04630  -0.03566 0.05468  194 GLN A CB  
1629 C CG  . GLN A 187 ? 0.25212 0.30854 0.26460 0.06330  -0.04899 0.05753  194 GLN A CG  
1630 C CD  . GLN A 187 ? 0.28777 0.37185 0.29097 0.06261  -0.06373 0.05650  194 GLN A CD  
1631 O OE1 . GLN A 187 ? 0.30711 0.39058 0.30517 0.04534  -0.06539 0.04639  194 GLN A OE1 
1632 N NE2 . GLN A 187 ? 0.31396 0.42252 0.31215 0.08388  -0.07502 0.06654  194 GLN A NE2 
1633 N N   . THR A 188 ? 0.37391 0.28616 0.31872 0.02606  -0.00422 0.07694  195 THR A N   
1634 C CA  . THR A 188 ? 0.45854 0.34893 0.40820 0.00135  0.00553  0.07355  195 THR A CA  
1635 C C   . THR A 188 ? 0.36542 0.28054 0.31944 -0.01158 0.00803  0.07379  195 THR A C   
1636 O O   . THR A 188 ? 0.38524 0.29625 0.35149 -0.03228 0.01512  0.07143  195 THR A O   
1637 C CB  . THR A 188 ? 0.45034 0.28558 0.37957 -0.00030 0.01905  0.08696  195 THR A CB  
1638 O OG1 . THR A 188 ? 0.49686 0.32222 0.40109 0.01383  0.02598  0.10741  195 THR A OG1 
1639 C CG2 . THR A 188 ? 0.45282 0.25607 0.37390 0.01452  0.01888  0.08399  195 THR A CG2 
1640 N N   . GLU A 189 ? 0.34103 0.28355 0.28517 0.00073  0.00193  0.07562  196 GLU A N   
1641 C CA  . GLU A 189 ? 0.31043 0.27459 0.25457 -0.00743 0.00564  0.07309  196 GLU A CA  
1642 C C   . GLU A 189 ? 0.27763 0.26209 0.24919 -0.02206 0.00159  0.05603  196 GLU A C   
1643 O O   . GLU A 189 ? 0.27673 0.27361 0.25503 -0.03117 0.00928  0.05537  196 GLU A O   
1644 C CB  . GLU A 189 ? 0.28924 0.27420 0.21113 0.00952  -0.00346 0.07302  196 GLU A CB  
1645 C CG  . GLU A 189 ? 0.28002 0.29156 0.21561 0.01234  -0.02203 0.05548  196 GLU A CG  
1646 C CD  . GLU A 189 ? 0.46749 0.49741 0.37903 0.02687  -0.03525 0.05394  196 GLU A CD  
1647 O OE1 . GLU A 189 ? 0.43763 0.46845 0.33604 0.04330  -0.04211 0.06452  196 GLU A OE1 
1648 O OE2 . GLU A 189 ? 0.38958 0.43178 0.29278 0.02334  -0.03957 0.04168  196 GLU A OE2 
1649 N N   . TYR A 190 ? 0.29769 0.28700 0.28466 -0.02206 -0.00863 0.04426  197 TYR A N   
1650 C CA  . TYR A 190 ? 0.27914 0.28416 0.28708 -0.03257 -0.01218 0.03046  197 TYR A CA  
1651 C C   . TYR A 190 ? 0.26882 0.26285 0.29040 -0.04788 -0.00676 0.02942  197 TYR A C   
1652 O O   . TYR A 190 ? 0.28388 0.29029 0.32062 -0.05428 -0.01075 0.01949  197 TYR A O   
1653 C CB  . TYR A 190 ? 0.23775 0.25294 0.25516 -0.02679 -0.02294 0.02078  197 TYR A CB  
1654 C CG  . TYR A 190 ? 0.19311 0.22558 0.20190 -0.01699 -0.03203 0.01924  197 TYR A CG  
1655 C CD1 . TYR A 190 ? 0.27788 0.32138 0.27937 -0.01904 -0.03431 0.01209  197 TYR A CD1 
1656 C CD2 . TYR A 190 ? 0.21553 0.25315 0.22101 -0.00434 -0.03899 0.02465  197 TYR A CD2 
1657 C CE1 . TYR A 190 ? 0.23360 0.28948 0.22234 -0.01257 -0.04556 0.00731  197 TYR A CE1 
1658 C CE2 . TYR A 190 ? 0.25967 0.31924 0.25847 0.00272  -0.05155 0.02193  197 TYR A CE2 
1659 C CZ  . TYR A 190 ? 0.23724 0.30393 0.22613 -0.00336 -0.05579 0.01185  197 TYR A CZ  
1660 O OH  . TYR A 190 ? 0.26046 0.34526 0.23784 0.00119  -0.07106 0.00561  197 TYR A OH  
1661 N N   . LEU A 191 ? 0.28590 0.25551 0.30075 -0.05449 0.00147  0.03963  198 LEU A N   
1662 C CA  . LEU A 191 ? 0.29570 0.25776 0.32476 -0.07476 0.00529  0.03823  198 LEU A CA  
1663 C C   . LEU A 191 ? 0.31137 0.29135 0.35056 -0.08599 0.01640  0.04814  198 LEU A C   
1664 O O   . LEU A 191 ? 0.30201 0.28795 0.36145 -0.10598 0.01842  0.04739  198 LEU A O   
1665 C CB  . LEU A 191 ? 0.30537 0.22213 0.32150 -0.07972 0.00840  0.04183  198 LEU A CB  
1666 C CG  . LEU A 191 ? 0.31963 0.21808 0.32553 -0.06622 0.00103  0.03272  198 LEU A CG  
1667 C CD1 . LEU A 191 ? 0.40238 0.24734 0.38902 -0.06809 0.00653  0.03566  198 LEU A CD1 
1668 C CD2 . LEU A 191 ? 0.34738 0.26625 0.36766 -0.07145 -0.00837 0.01695  198 LEU A CD2 
1669 N N   . GLU A 192 ? 0.25202 0.24273 0.27733 -0.07367 0.02373  0.05755  199 GLU A N   
1670 C CA  . GLU A 192 ? 0.26282 0.27065 0.29424 -0.08062 0.03916  0.07000  199 GLU A CA  
1671 C C   . GLU A 192 ? 0.28240 0.33105 0.33215 -0.07808 0.03846  0.06174  199 GLU A C   
1672 O O   . GLU A 192 ? 0.25267 0.30917 0.29306 -0.06340 0.02973  0.05065  199 GLU A O   
1673 C CB  . GLU A 192 ? 0.34215 0.33868 0.34116 -0.06489 0.04960  0.08522  199 GLU A CB  
1674 C CG  . GLU A 192 ? 0.41922 0.37285 0.39531 -0.06074 0.05131  0.09677  199 GLU A CG  
1675 C CD  . GLU A 192 ? 0.80881 0.75299 0.74913 -0.04306 0.06190  0.11503  199 GLU A CD  
1676 O OE1 . GLU A 192 ? 1.20450 1.16329 1.14181 -0.04564 0.07837  0.12661  199 GLU A OE1 
1677 O OE2 . GLU A 192 ? 0.99671 0.92187 0.91113 -0.02444 0.05419  0.11887  199 GLU A OE2 
1678 N N   . GLU A 193 ? 0.28511 0.35954 0.36225 -0.09254 0.04844  0.06808  200 GLU A N   
1679 C CA  . GLU A 193 ? 0.20566 0.32132 0.30438 -0.08759 0.04836  0.06182  200 GLU A CA  
1680 C C   . GLU A 193 ? 0.20260 0.32577 0.27620 -0.06344 0.05565  0.06140  200 GLU A C   
1681 O O   . GLU A 193 ? 0.23968 0.37014 0.31014 -0.05059 0.04789  0.04877  200 GLU A O   
1682 C CB  . GLU A 193 ? 0.21700 0.36479 0.35198 -0.10483 0.05897  0.07069  200 GLU A CB  
1683 C CG  . GLU A 193 ? 0.37477 0.56750 0.52990 -0.09215 0.06294  0.06792  200 GLU A CG  
1684 C CD  . GLU A 193 ? 0.82030 1.03819 1.01069 -0.10461 0.06508  0.06726  200 GLU A CD  
1685 O OE1 . GLU A 193 ? 0.63311 0.88227 0.84427 -0.09703 0.05778  0.06041  200 GLU A OE1 
1686 O OE2 . GLU A 193 ? 0.55002 0.75699 0.74726 -0.12192 0.07457  0.07447  200 GLU A OE2 
1687 N N   . ARG A 194 ? 0.24845 0.36464 0.29877 -0.05645 0.07089  0.07482  201 ARG A N   
1688 C CA  . ARG A 194 ? 0.26865 0.39009 0.28890 -0.03303 0.07762  0.07193  201 ARG A CA  
1689 C C   . ARG A 194 ? 0.28758 0.38420 0.27764 -0.02062 0.05895  0.05558  201 ARG A C   
1690 O O   . ARG A 194 ? 0.29672 0.39446 0.26803 -0.00545 0.05707  0.04400  201 ARG A O   
1691 C CB  . ARG A 194 ? 0.34026 0.45898 0.33509 -0.02611 0.09857  0.09065  201 ARG A CB  
1692 C CG  . ARG A 194 ? 0.44215 0.52646 0.41174 -0.02897 0.09621  0.10117  201 ARG A CG  
1693 C CD  . ARG A 194 ? 0.65134 0.73469 0.59529 -0.02131 0.12095  0.12356  201 ARG A CD  
1694 N NE  . ARG A 194 ? 0.60943 0.65678 0.51672 -0.01507 0.11891  0.13531  201 ARG A NE  
1695 C CZ  . ARG A 194 ? 0.53440 0.57118 0.40961 -0.00602 0.13937  0.15773  201 ARG A CZ  
1696 N NH1 . ARG A 194 ? 0.60415 0.66156 0.48462 -0.00508 0.15797  0.16249  201 ARG A NH1 
1697 N NH2 . ARG A 194 ? 0.86782 0.87030 0.70846 0.00321  0.13365  0.16728  201 ARG A NH2 
1698 N N   . ARG A 195 ? 0.23076 0.30477 0.21645 -0.02690 0.04573  0.05434  202 ARG A N   
1699 C CA  . ARG A 195 ? 0.25056 0.31115 0.21750 -0.01797 0.02764  0.04014  202 ARG A CA  
1700 C C   . ARG A 195 ? 0.23493 0.30133 0.22309 -0.02190 0.01688  0.02435  202 ARG A C   
1701 O O   . ARG A 195 ? 0.24894 0.31115 0.22350 -0.01421 0.00878  0.01119  202 ARG A O   
1702 C CB  . ARG A 195 ? 0.27835 0.31981 0.23856 -0.01959 0.01907  0.04612  202 ARG A CB  
1703 C CG  . ARG A 195 ? 0.28448 0.32302 0.23486 -0.01197 -0.00004 0.03381  202 ARG A CG  
1704 C CD  . ARG A 195 ? 0.33099 0.37172 0.24536 0.00234  -0.00471 0.03045  202 ARG A CD  
1705 N NE  . ARG A 195 ? 0.29939 0.34352 0.20886 0.00656  -0.02515 0.02124  202 ARG A NE  
1706 C CZ  . ARG A 195 ? 0.32347 0.37357 0.22488 0.00686  -0.03881 0.00375  202 ARG A CZ  
1707 N NH1 . ARG A 195 ? 0.31380 0.35908 0.20447 0.00674  -0.03340 -0.00744 202 ARG A NH1 
1708 N NH2 . ARG A 195 ? 0.32951 0.39043 0.23499 0.00710  -0.05804 -0.00267 202 ARG A NH2 
1709 N N   . ILE A 196 ? 0.23321 0.30660 0.25179 -0.03437 0.01662  0.02544  203 ILE A N   
1710 C CA  . ILE A 196 ? 0.18304 0.26108 0.21721 -0.03535 0.00803  0.01354  203 ILE A CA  
1711 C C   . ILE A 196 ? 0.19939 0.29047 0.23146 -0.02411 0.01512  0.00933  203 ILE A C   
1712 O O   . ILE A 196 ? 0.19809 0.27870 0.22176 -0.01721 0.00920  -0.00186 203 ILE A O   
1713 C CB  . ILE A 196 ? 0.24200 0.32556 0.30246 -0.04906 0.00479  0.01517  203 ILE A CB  
1714 C CG1 . ILE A 196 ? 0.21244 0.27326 0.26807 -0.05589 -0.00125 0.01668  203 ILE A CG1 
1715 C CG2 . ILE A 196 ? 0.21917 0.30892 0.29024 -0.04616 -0.00248 0.00574  203 ILE A CG2 
1716 C CD1 . ILE A 196 ? 0.31301 0.37063 0.38529 -0.07151 -0.00240 0.01823  203 ILE A CD1 
1717 N N   . LYS A 197 ? 0.20618 0.31864 0.24564 -0.02133 0.02983  0.01923  204 LYS A N   
1718 C CA  . LYS A 197 ? 0.17680 0.30280 0.21269 -0.00491 0.03988  0.01672  204 LYS A CA  
1719 C C   . LYS A 197 ? 0.26696 0.36654 0.26193 0.01017  0.03916  0.00550  204 LYS A C   
1720 O O   . LYS A 197 ? 0.27792 0.36643 0.26261 0.02221  0.03899  -0.00495 204 LYS A O   
1721 C CB  . LYS A 197 ? 0.18575 0.34488 0.23724 -0.00289 0.05919  0.03178  204 LYS A CB  
1722 C CG  . LYS A 197 ? 0.35538 0.54796 0.45221 -0.02028 0.05927  0.04120  204 LYS A CG  
1723 C CD  . LYS A 197 ? 0.31015 0.54680 0.42901 -0.01369 0.08009  0.05493  204 LYS A CD  
1724 C CE  . LYS A 197 ? 0.55736 0.82909 0.72363 -0.03680 0.07903  0.06431  204 LYS A CE  
1725 N NZ  . LYS A 197 ? 0.68230 0.95127 0.84917 -0.04916 0.09437  0.07750  204 LYS A NZ  
1726 N N   . GLU A 198 ? 0.22093 0.30759 0.18914 0.01023  0.03822  0.00736  205 GLU A N   
1727 C CA  . GLU A 198 ? 0.27093 0.33375 0.19682 0.02211  0.03306  -0.00585 205 GLU A CA  
1728 C C   . GLU A 198 ? 0.27413 0.31599 0.20004 0.01567  0.01467  -0.02267 205 GLU A C   
1729 O O   . GLU A 198 ? 0.27212 0.29261 0.17463 0.02361  0.01253  -0.03743 205 GLU A O   
1730 C CB  . GLU A 198 ? 0.31770 0.37525 0.21646 0.02303  0.03099  0.00104  205 GLU A CB  
1731 C CG  . GLU A 198 ? 0.31784 0.35414 0.17160 0.03221  0.01858  -0.01463 205 GLU A CG  
1732 C CD  . GLU A 198 ? 0.34974 0.38555 0.17825 0.03504  0.01261  -0.00570 205 GLU A CD  
1733 O OE1 . GLU A 198 ? 0.38136 0.42261 0.23225 0.02514  0.00565  0.00431  205 GLU A OE1 
1734 O OE2 . GLU A 198 ? 0.38116 0.40906 0.16360 0.04989  0.01547  -0.00820 205 GLU A OE2 
1735 N N   . ILE A 199 ? 0.22299 0.26788 0.17369 0.00111  0.00303  -0.02041 206 ILE A N   
1736 C CA  . ILE A 199 ? 0.26445 0.29459 0.21966 -0.00686 -0.01173 -0.03299 206 ILE A CA  
1737 C C   . ILE A 199 ? 0.29151 0.31267 0.25701 -0.00431 -0.00723 -0.03820 206 ILE A C   
1738 O O   . ILE A 199 ? 0.27485 0.27220 0.22790 -0.00516 -0.01248 -0.05090 206 ILE A O   
1739 C CB  . ILE A 199 ? 0.19388 0.23252 0.17237 -0.01866 -0.02100 -0.02686 206 ILE A CB  
1740 C CG1 . ILE A 199 ? 0.28115 0.32450 0.24505 -0.01638 -0.02578 -0.02037 206 ILE A CG1 
1741 C CG2 . ILE A 199 ? 0.24172 0.27219 0.23197 -0.02745 -0.03189 -0.03653 206 ILE A CG2 
1742 C CD1 . ILE A 199 ? 0.31517 0.36393 0.29888 -0.02194 -0.02858 -0.01024 206 ILE A CD1 
1743 N N   . VAL A 200 ? 0.21640 0.25561 0.20415 -0.00151 0.00188  -0.02807 207 VAL A N   
1744 C CA  . VAL A 200 ? 0.20082 0.23450 0.19634 0.00577  0.00578  -0.03001 207 VAL A CA  
1745 C C   . VAL A 200 ? 0.24426 0.25880 0.21216 0.02355  0.01523  -0.03771 207 VAL A C   
1746 O O   . VAL A 200 ? 0.30367 0.28855 0.25970 0.02831  0.01468  -0.04618 207 VAL A O   
1747 C CB  . VAL A 200 ? 0.22698 0.29256 0.25230 0.00605  0.01031  -0.01777 207 VAL A CB  
1748 C CG1 . VAL A 200 ? 0.22592 0.29184 0.25497 0.02125  0.01541  -0.01714 207 VAL A CG1 
1749 C CG2 . VAL A 200 ? 0.20100 0.27124 0.24470 -0.01015 -0.00007 -0.01488 207 VAL A CG2 
1750 N N   . LYS A 201 ? 0.24130 0.26748 0.19466 0.03457  0.02596  -0.03456 208 LYS A N   
1751 C CA  . LYS A 201 ? 0.28656 0.29163 0.20690 0.05578  0.03750  -0.04288 208 LYS A CA  
1752 C C   . LYS A 201 ? 0.37181 0.33161 0.25332 0.05161  0.02663  -0.06271 208 LYS A C   
1753 O O   . LYS A 201 ? 0.41771 0.34068 0.27204 0.06389  0.03120  -0.07494 208 LYS A O   
1754 C CB  . LYS A 201 ? 0.29974 0.33106 0.21208 0.06912  0.05418  -0.03306 208 LYS A CB  
1755 C CG  . LYS A 201 ? 0.38092 0.39110 0.25331 0.09595  0.06972  -0.04137 208 LYS A CG  
1756 C CD  . LYS A 201 ? 0.49946 0.53923 0.36345 0.10842  0.08886  -0.02889 208 LYS A CD  
1757 C CE  . LYS A 201 ? 0.60690 0.62366 0.42406 0.13929  0.10691  -0.03791 208 LYS A CE  
1758 N NZ  . LYS A 201 ? 0.81354 0.86693 0.63020 0.15263  0.13012  -0.02082 208 LYS A NZ  
1759 N N   . LYS A 202 ? 0.35598 0.31736 0.23480 0.03437  0.01139  -0.06641 209 LYS A N   
1760 C CA  . LYS A 202 ? 0.36201 0.29007 0.20862 0.02673  -0.00323 -0.08616 209 LYS A CA  
1761 C C   . LYS A 202 ? 0.37109 0.27235 0.23049 0.01185  -0.01256 -0.09563 209 LYS A C   
1762 O O   . LYS A 202 ? 0.42173 0.28076 0.25204 0.01081  -0.01604 -0.11345 209 LYS A O   
1763 C CB  . LYS A 202 ? 0.38401 0.33187 0.22938 0.01532  -0.01799 -0.08425 209 LYS A CB  
1764 C CG  . LYS A 202 ? 0.46707 0.39255 0.28231 0.00598  -0.03781 -0.10493 209 LYS A CG  
1765 C CD  . LYS A 202 ? 0.59715 0.55009 0.40993 0.00189  -0.05181 -0.09914 209 LYS A CD  
1766 C CE  . LYS A 202 ? 0.84247 0.78595 0.63591 -0.01092 -0.07729 -0.11938 209 LYS A CE  
1767 N NZ  . LYS A 202 ? 0.90466 0.81255 0.65396 -0.00543 -0.07475 -0.13794 209 LYS A NZ  
1768 N N   . HIS A 203 ? 0.35691 0.27808 0.25655 -0.00010 -0.01533 -0.08396 210 HIS A N   
1769 C CA  . HIS A 203 ? 0.43662 0.33891 0.35113 -0.01757 -0.02364 -0.08937 210 HIS A CA  
1770 C C   . HIS A 203 ? 0.39197 0.28337 0.32176 -0.01151 -0.01242 -0.08025 210 HIS A C   
1771 O O   . HIS A 203 ? 0.41155 0.27650 0.34551 -0.02327 -0.01438 -0.08395 210 HIS A O   
1772 C CB  . HIS A 203 ? 0.40967 0.34297 0.35438 -0.03545 -0.03637 -0.08330 210 HIS A CB  
1773 C CG  . HIS A 203 ? 0.33604 0.28148 0.26762 -0.04146 -0.05122 -0.09127 210 HIS A CG  
1774 N ND1 . HIS A 203 ? 0.37948 0.30445 0.29189 -0.05307 -0.06514 -0.10994 210 HIS A ND1 
1775 C CD2 . HIS A 203 ? 0.38330 0.35829 0.31611 -0.03697 -0.05541 -0.08264 210 HIS A CD2 
1776 C CE1 . HIS A 203 ? 0.45648 0.40388 0.35893 -0.05373 -0.07925 -0.11262 210 HIS A CE1 
1777 N NE2 . HIS A 203 ? 0.41616 0.39211 0.32947 -0.04238 -0.07224 -0.09481 210 HIS A NE2 
1778 N N   . SER A 204 ? 0.38983 0.35550 0.21208 -0.06972 -0.08348 -0.10270 211 SER A N   
1779 C CA  . SER A 204 ? 0.36714 0.30929 0.20878 -0.06836 -0.07471 -0.09955 211 SER A CA  
1780 C C   . SER A 204 ? 0.41391 0.31603 0.23362 -0.05155 -0.05575 -0.11659 211 SER A C   
1781 O O   . SER A 204 ? 0.40628 0.30510 0.25101 -0.03707 -0.04173 -0.10561 211 SER A O   
1782 C CB  . SER A 204 ? 0.40618 0.38379 0.27783 -0.05965 -0.07062 -0.07420 211 SER A CB  
1783 O OG  . SER A 204 ? 0.38531 0.39970 0.27724 -0.06973 -0.08528 -0.05763 211 SER A OG  
1784 N N   . GLN A 205 ? 0.45057 0.33979 0.24235 -0.04553 -0.05173 -0.13748 212 GLN A N   
1785 C CA  . GLN A 205 ? 0.72149 0.58769 0.49790 -0.02370 -0.02974 -0.14975 212 GLN A CA  
1786 C C   . GLN A 205 ? 0.70772 0.52472 0.49835 -0.01863 -0.02149 -0.15549 212 GLN A C   
1787 O O   . GLN A 205 ? 0.68678 0.49146 0.47653 0.00474  -0.00118 -0.15683 212 GLN A O   
1788 C CB  . GLN A 205 ? 0.62714 0.49820 0.37216 -0.01981 -0.02760 -0.17240 212 GLN A CB  
1789 C CG  . GLN A 205 ? 0.79107 0.63557 0.52880 -0.03604 -0.04401 -0.19573 212 GLN A CG  
1790 C CD  . GLN A 205 ? 1.22577 1.10336 0.95207 -0.04987 -0.06790 -0.19370 212 GLN A CD  
1791 O OE1 . GLN A 205 ? 0.73684 0.63521 0.48556 -0.06481 -0.08147 -0.17233 212 GLN A OE1 
1792 N NE2 . GLN A 205 ? 0.91340 0.79651 0.60450 -0.04315 -0.07211 -0.21235 212 GLN A NE2 
1793 N N   . PHE A 206 ? 0.61276 0.40732 0.42183 -0.03903 -0.03604 -0.15402 213 PHE A N   
1794 C CA  . PHE A 206 ? 0.61490 0.35859 0.43933 -0.03548 -0.02900 -0.15694 213 PHE A CA  
1795 C C   . PHE A 206 ? 0.51623 0.27093 0.38224 -0.03987 -0.03119 -0.12807 213 PHE A C   
1796 O O   . PHE A 206 ? 0.70199 0.42104 0.58920 -0.04236 -0.02922 -0.12227 213 PHE A O   
1797 C CB  . PHE A 206 ? 0.64012 0.35283 0.46190 -0.05542 -0.04140 -0.17726 213 PHE A CB  
1798 C CG  . PHE A 206 ? 0.67159 0.37834 0.46026 -0.04548 -0.03618 -0.20709 213 PHE A CG  
1799 C CD1 . PHE A 206 ? 0.89393 0.59999 0.66736 -0.01554 -0.01386 -0.21298 213 PHE A CD1 
1800 C CD2 . PHE A 206 ? 0.71369 0.42482 0.48776 -0.06565 -0.05388 -0.22768 213 PHE A CD2 
1801 C CE1 . PHE A 206 ? 1.01011 0.71774 0.75320 -0.00678 -0.00766 -0.23958 213 PHE A CE1 
1802 C CE2 . PHE A 206 ? 0.83459 0.54435 0.57525 -0.05577 -0.04990 -0.25740 213 PHE A CE2 
1803 C CZ  . PHE A 206 ? 0.88968 0.59813 0.61418 -0.02682 -0.02568 -0.26362 213 PHE A CZ  
1804 N N   . ILE A 207 ? 0.40535 0.21916 0.29212 -0.03869 -0.03350 -0.10632 214 ILE A N   
1805 C CA  . ILE A 207 ? 0.35357 0.19830 0.28482 -0.03721 -0.03224 -0.07804 214 ILE A CA  
1806 C C   . ILE A 207 ? 0.47458 0.31254 0.41958 -0.01154 -0.01146 -0.06954 214 ILE A C   
1807 O O   . ILE A 207 ? 0.39687 0.24170 0.32660 0.00802  0.00259  -0.07561 214 ILE A O   
1808 C CB  . ILE A 207 ? 0.33477 0.23772 0.27794 -0.03816 -0.03783 -0.06345 214 ILE A CB  
1809 C CG1 . ILE A 207 ? 0.31137 0.22977 0.24978 -0.06195 -0.05883 -0.06418 214 ILE A CG1 
1810 C CG2 . ILE A 207 ? 0.27978 0.21802 0.26133 -0.03040 -0.03279 -0.03974 214 ILE A CG2 
1811 C CD1 . ILE A 207 ? 0.35444 0.27039 0.31896 -0.08299 -0.07169 -0.05295 214 ILE A CD1 
1812 N N   . GLY A 208 ? 0.34401 0.17478 0.32010 -0.01157 -0.00937 -0.05174 215 GLY A N   
1813 C CA  . GLY A 208 ? 0.36288 0.18546 0.35299 0.01307  0.00945  -0.04103 215 GLY A CA  
1814 C C   . GLY A 208 ? 0.37802 0.26168 0.39306 0.02717  0.01723  -0.01940 215 GLY A C   
1815 O O   . GLY A 208 ? 0.39145 0.28553 0.43052 0.04158  0.02750  -0.00011 215 GLY A O   
1816 N N   . TYR A 209 ? 0.27553 0.19929 0.28467 0.02307  0.01212  -0.02243 216 TYR A N   
1817 C CA  . TYR A 209 ? 0.25604 0.23349 0.28406 0.03223  0.01696  -0.00881 216 TYR A CA  
1818 C C   . TYR A 209 ? 0.25753 0.24850 0.26629 0.03539  0.01989  -0.02067 216 TYR A C   
1819 O O   . TYR A 209 ? 0.27427 0.24811 0.25948 0.02628  0.01316  -0.03412 216 TYR A O   
1820 C CB  . TYR A 209 ? 0.20017 0.21441 0.24942 0.02021  0.00524  0.00400  216 TYR A CB  
1821 C CG  . TYR A 209 ? 0.23685 0.24784 0.30952 0.01569  0.00287  0.02237  216 TYR A CG  
1822 C CD1 . TYR A 209 ? 0.21761 0.25350 0.31319 0.02935  0.01235  0.04256  216 TYR A CD1 
1823 C CD2 . TYR A 209 ? 0.22170 0.20866 0.29545 -0.00379 -0.00939 0.02264  216 TYR A CD2 
1824 C CE1 . TYR A 209 ? 0.20722 0.24222 0.32674 0.02556  0.01124  0.06517  216 TYR A CE1 
1825 C CE2 . TYR A 209 ? 0.21577 0.19988 0.31529 -0.01093 -0.01151 0.04390  216 TYR A CE2 
1826 C CZ  . TYR A 209 ? 0.19782 0.20486 0.32035 0.00479  -0.00032 0.06637  216 TYR A CZ  
1827 O OH  . TYR A 209 ? 0.26084 0.26730 0.41131 -0.00160 -0.00126 0.09304  216 TYR A OH  
1828 N N   . PRO A 210 ? 0.25371 0.27882 0.27318 0.04645  0.02910  -0.01375 217 PRO A N   
1829 C CA  . PRO A 210 ? 0.21304 0.25173 0.21932 0.04631  0.03194  -0.02053 217 PRO A CA  
1830 C C   . PRO A 210 ? 0.29489 0.34416 0.30018 0.03191  0.01911  -0.02306 217 PRO A C   
1831 O O   . PRO A 210 ? 0.27146 0.34200 0.29477 0.02735  0.01224  -0.01733 217 PRO A O   
1832 C CB  . PRO A 210 ? 0.26388 0.34225 0.28997 0.05633  0.04171  -0.00947 217 PRO A CB  
1833 C CG  . PRO A 210 ? 0.26575 0.36301 0.31548 0.05889  0.03950  0.00300  217 PRO A CG  
1834 C CD  . PRO A 210 ? 0.24226 0.29931 0.28769 0.05777  0.03649  0.00296  217 PRO A CD  
1835 N N   . ILE A 211 ? 0.25795 0.29395 0.24103 0.02734  0.01686  -0.03063 218 ILE A N   
1836 C CA  . ILE A 211 ? 0.20357 0.24787 0.18561 0.01764  0.00673  -0.02948 218 ILE A CA  
1837 C C   . ILE A 211 ? 0.21907 0.27675 0.20039 0.01915  0.01360  -0.02579 218 ILE A C   
1838 O O   . ILE A 211 ? 0.27190 0.32490 0.23494 0.02310  0.02136  -0.02691 218 ILE A O   
1839 C CB  . ILE A 211 ? 0.24510 0.27060 0.20472 0.00948  -0.00320 -0.03546 218 ILE A CB  
1840 C CG1 . ILE A 211 ? 0.23529 0.24657 0.19939 0.00252  -0.01154 -0.03783 218 ILE A CG1 
1841 C CG2 . ILE A 211 ? 0.20980 0.24926 0.17165 0.00399  -0.01190 -0.02873 218 ILE A CG2 
1842 C CD1 . ILE A 211 ? 0.28902 0.28123 0.22820 -0.00938 -0.02273 -0.04752 218 ILE A CD1 
1843 N N   . THR A 212 ? 0.19224 0.26683 0.19320 0.01564  0.01121  -0.02164 219 THR A N   
1844 C CA  . THR A 212 ? 0.16656 0.25135 0.17331 0.01218  0.01631  -0.01664 219 THR A CA  
1845 C C   . THR A 212 ? 0.14548 0.21978 0.15165 0.00631  0.00896  -0.01299 219 THR A C   
1846 O O   . THR A 212 ? 0.19106 0.26380 0.20807 0.00594  0.00161  -0.01597 219 THR A O   
1847 C CB  . THR A 212 ? 0.21968 0.32807 0.24933 0.01019  0.01843  -0.01692 219 THR A CB  
1848 O OG1 . THR A 212 ? 0.21868 0.34175 0.25152 0.01911  0.02604  -0.01499 219 THR A OG1 
1849 C CG2 . THR A 212 ? 0.23479 0.35234 0.27341 0.00087  0.02188  -0.01122 219 THR A CG2 
1850 N N   . LEU A 213 ? 0.20127 0.27129 0.19504 0.00443  0.01225  -0.00445 220 LEU A N   
1851 C CA  . LEU A 213 ? 0.21347 0.27409 0.20944 0.00094  0.00716  0.00535  220 LEU A CA  
1852 C C   . LEU A 213 ? 0.23813 0.29843 0.25468 -0.00709 0.01123  0.01154  220 LEU A C   
1853 O O   . LEU A 213 ? 0.18926 0.26159 0.20660 -0.01180 0.01952  0.02061  220 LEU A O   
1854 C CB  . LEU A 213 ? 0.23986 0.30147 0.21126 0.00255  0.00776  0.01510  220 LEU A CB  
1855 C CG  . LEU A 213 ? 0.28740 0.34505 0.26120 0.00121  0.00439  0.03335  220 LEU A CG  
1856 C CD1 . LEU A 213 ? 0.26747 0.31492 0.25556 0.00476  -0.00526 0.03247  220 LEU A CD1 
1857 C CD2 . LEU A 213 ? 0.27551 0.34556 0.21952 0.00360  0.00363  0.04198  220 LEU A CD2 
1858 N N   . PHE A 214 ? 0.22482 0.27276 0.25831 -0.00909 0.00561  0.00555  221 PHE A N   
1859 C CA  . PHE A 214 ? 0.23706 0.27552 0.29008 -0.02046 0.00679  0.00676  221 PHE A CA  
1860 C C   . PHE A 214 ? 0.27718 0.29892 0.33192 -0.02461 0.00903  0.02796  221 PHE A C   
1861 O O   . PHE A 214 ? 0.25917 0.27376 0.30285 -0.01544 0.00679  0.03877  221 PHE A O   
1862 C CB  . PHE A 214 ? 0.20602 0.22914 0.27084 -0.01855 0.00040  -0.01004 221 PHE A CB  
1863 C CG  . PHE A 214 ? 0.18268 0.22952 0.25069 -0.01815 -0.00132 -0.02795 221 PHE A CG  
1864 C CD1 . PHE A 214 ? 0.17323 0.24536 0.23261 -0.01189 0.00101  -0.02712 221 PHE A CD1 
1865 C CD2 . PHE A 214 ? 0.21384 0.25633 0.29243 -0.02297 -0.00543 -0.04576 221 PHE A CD2 
1866 C CE1 . PHE A 214 ? 0.14913 0.24667 0.21398 -0.00989 -0.00005 -0.03760 221 PHE A CE1 
1867 C CE2 . PHE A 214 ? 0.21660 0.28976 0.29638 -0.02171 -0.00748 -0.05985 221 PHE A CE2 
1868 C CZ  . PHE A 214 ? 0.18038 0.28359 0.25503 -0.01475 -0.00448 -0.05270 221 PHE A CZ  
1869 N N   . VAL A 215 ? 0.23601 0.25570 0.30714 -0.03978 0.01279  0.03700  222 VAL A N   
1870 C CA  . VAL A 215 ? 0.25602 0.25836 0.33521 -0.04603 0.01545  0.06194  222 VAL A CA  
1871 C C   . VAL A 215 ? 0.28587 0.24640 0.38800 -0.05490 0.01057  0.05581  222 VAL A C   
1872 O O   . VAL A 215 ? 0.26807 0.22067 0.37764 -0.05942 0.00566  0.03026  222 VAL A O   
1873 C CB  . VAL A 215 ? 0.51236 0.54333 0.59558 -0.05809 0.02448  0.08295  222 VAL A CB  
1874 C CG1 . VAL A 215 ? 0.56074 0.62078 0.61488 -0.04397 0.03087  0.09308  222 VAL A CG1 
1875 C CG2 . VAL A 215 ? 0.30985 0.36534 0.40641 -0.07023 0.02576  0.07005  222 VAL A CG2 
1876 N N   . GLU A 216 ? 0.31164 0.24445 0.42373 -0.05635 0.01225  0.07945  223 GLU A N   
1877 C CA  . GLU A 216 ? 0.38134 0.26163 0.51480 -0.06217 0.00899  0.07487  223 GLU A CA  
1878 C C   . GLU A 216 ? 0.42108 0.28620 0.57937 -0.08813 0.01181  0.09612  223 GLU A C   
1879 O O   . GLU A 216 ? 0.51681 0.41409 0.67552 -0.09557 0.01820  0.12526  223 GLU A O   
1880 C CB  . GLU A 216 ? 0.44679 0.29854 0.57766 -0.03950 0.00884  0.08789  223 GLU A CB  
1881 C CG  . GLU A 216 ? 0.41694 0.28927 0.52806 -0.01654 0.00525  0.07199  223 GLU A CG  
1882 C CD  . GLU A 216 ? 0.63287 0.49032 0.74460 0.00597  0.00513  0.09125  223 GLU A CD  
1883 O OE1 . GLU A 216 ? 0.45051 0.26369 0.57729 0.01571  0.00577  0.08548  223 GLU A OE1 
1884 O OE2 . GLU A 216 ? 0.55375 0.44547 0.65007 0.01492  0.00424  0.11083  223 GLU A OE2 
1885 N N   . LYS A 217 ? 0.51298 0.32907 0.69178 -0.10247 0.00701  0.08058  224 LYS A N   
1886 C CA  . LYS A 217 ? 0.68653 0.48240 0.88744 -0.13019 0.00746  0.09611  224 LYS A CA  
1887 C C   . LYS A 217 ? 0.81360 0.60518 1.01536 -0.12332 0.01493  0.13833  224 LYS A C   
1888 O O   . LYS A 217 ? 0.70607 0.47331 0.90180 -0.09988 0.01660  0.14950  224 LYS A O   
1889 C CB  . LYS A 217 ? 0.67348 0.41062 0.87728 -0.13869 0.00070  0.06470  224 LYS A CB  
1890 C CG  . LYS A 217 ? 1.07940 0.78318 1.27115 -0.11149 -0.00204 0.03540  224 LYS A CG  
1891 C CD  . LYS A 217 ? 1.07593 0.72252 1.26176 -0.11756 -0.00698 0.00418  224 LYS A CD  
1892 C CE  . LYS A 217 ? 1.10366 0.72983 1.27305 -0.08616 -0.00741 -0.02615 224 LYS A CE  
1893 N NZ  . LYS A 217 ? 1.00031 0.55974 1.15952 -0.08197 -0.00808 -0.04580 224 LYS A NZ  
# 
