data_7HAD
# 
_entry.id   7HAD 
# 
_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   7HAD         pdb_00007had 10.2210/pdb7had/pdb 
WWPDB D_1001407224 ?            ?                   
# 
_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                        7HAD 
_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 2,3-dimethylbenzamide             149.190   1   ?        ? ? ? 
3 water       nat water                             18.015    310 ?        ? ? ? 
# 
_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 2,3-dimethylbenzamide A1AX3 
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 
A1AX3 non-polymer         . 2,3-dimethylbenzamide ? 'C9 H11 N O'     149.190 
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        A1AX3 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1AX3 
_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 A1AX3 1   301 301 A1AX3 E25 A . 
C 3 HOH   1   401 247 HOH   HOH A . 
C 3 HOH   2   402 239 HOH   HOH A . 
C 3 HOH   3   403 270 HOH   HOH A . 
C 3 HOH   4   404 151 HOH   HOH A . 
C 3 HOH   5   405 272 HOH   HOH A . 
C 3 HOH   6   406 137 HOH   HOH A . 
C 3 HOH   7   407 275 HOH   HOH A . 
C 3 HOH   8   408 70  HOH   HOH A . 
C 3 HOH   9   409 172 HOH   HOH A . 
C 3 HOH   10  410 302 HOH   HOH A . 
C 3 HOH   11  411 38  HOH   HOH A . 
C 3 HOH   12  412 258 HOH   HOH A . 
C 3 HOH   13  413 279 HOH   HOH A . 
C 3 HOH   14  414 113 HOH   HOH A . 
C 3 HOH   15  415 209 HOH   HOH A . 
C 3 HOH   16  416 179 HOH   HOH A . 
C 3 HOH   17  417 198 HOH   HOH A . 
C 3 HOH   18  418 111 HOH   HOH A . 
C 3 HOH   19  419 62  HOH   HOH A . 
C 3 HOH   20  420 180 HOH   HOH A . 
C 3 HOH   21  421 43  HOH   HOH A . 
C 3 HOH   22  422 50  HOH   HOH A . 
C 3 HOH   23  423 64  HOH   HOH A . 
C 3 HOH   24  424 73  HOH   HOH A . 
C 3 HOH   25  425 164 HOH   HOH A . 
C 3 HOH   26  426 136 HOH   HOH A . 
C 3 HOH   27  427 20  HOH   HOH A . 
C 3 HOH   28  428 202 HOH   HOH A . 
C 3 HOH   29  429 139 HOH   HOH A . 
C 3 HOH   30  430 57  HOH   HOH A . 
C 3 HOH   31  431 199 HOH   HOH A . 
C 3 HOH   32  432 23  HOH   HOH A . 
C 3 HOH   33  433 90  HOH   HOH A . 
C 3 HOH   34  434 61  HOH   HOH A . 
C 3 HOH   35  435 76  HOH   HOH A . 
C 3 HOH   36  436 156 HOH   HOH A . 
C 3 HOH   37  437 109 HOH   HOH A . 
C 3 HOH   38  438 95  HOH   HOH A . 
C 3 HOH   39  439 218 HOH   HOH A . 
C 3 HOH   40  440 27  HOH   HOH A . 
C 3 HOH   41  441 178 HOH   HOH A . 
C 3 HOH   42  442 217 HOH   HOH A . 
C 3 HOH   43  443 167 HOH   HOH A . 
C 3 HOH   44  444 32  HOH   HOH A . 
C 3 HOH   45  445 7   HOH   HOH A . 
C 3 HOH   46  446 82  HOH   HOH A . 
C 3 HOH   47  447 30  HOH   HOH A . 
C 3 HOH   48  448 84  HOH   HOH A . 
C 3 HOH   49  449 143 HOH   HOH A . 
C 3 HOH   50  450 91  HOH   HOH A . 
C 3 HOH   51  451 83  HOH   HOH A . 
C 3 HOH   52  452 24  HOH   HOH A . 
C 3 HOH   53  453 48  HOH   HOH A . 
C 3 HOH   54  454 10  HOH   HOH A . 
C 3 HOH   55  455 105 HOH   HOH A . 
C 3 HOH   56  456 153 HOH   HOH A . 
C 3 HOH   57  457 17  HOH   HOH A . 
C 3 HOH   58  458 68  HOH   HOH A . 
C 3 HOH   59  459 60  HOH   HOH A . 
C 3 HOH   60  460 49  HOH   HOH A . 
C 3 HOH   61  461 88  HOH   HOH A . 
C 3 HOH   62  462 282 HOH   HOH A . 
C 3 HOH   63  463 135 HOH   HOH A . 
C 3 HOH   64  464 8   HOH   HOH A . 
C 3 HOH   65  465 81  HOH   HOH A . 
C 3 HOH   66  466 125 HOH   HOH A . 
C 3 HOH   67  467 9   HOH   HOH A . 
C 3 HOH   68  468 13  HOH   HOH A . 
C 3 HOH   69  469 267 HOH   HOH A . 
C 3 HOH   70  470 65  HOH   HOH A . 
C 3 HOH   71  471 87  HOH   HOH A . 
C 3 HOH   72  472 1   HOH   HOH A . 
C 3 HOH   73  473 115 HOH   HOH A . 
C 3 HOH   74  474 107 HOH   HOH A . 
C 3 HOH   75  475 40  HOH   HOH A . 
C 3 HOH   76  476 110 HOH   HOH A . 
C 3 HOH   77  477 241 HOH   HOH A . 
C 3 HOH   78  478 118 HOH   HOH A . 
C 3 HOH   79  479 26  HOH   HOH A . 
C 3 HOH   80  480 126 HOH   HOH A . 
C 3 HOH   81  481 42  HOH   HOH A . 
C 3 HOH   82  482 185 HOH   HOH A . 
C 3 HOH   83  483 117 HOH   HOH A . 
C 3 HOH   84  484 28  HOH   HOH A . 
C 3 HOH   85  485 5   HOH   HOH A . 
C 3 HOH   86  486 121 HOH   HOH A . 
C 3 HOH   87  487 15  HOH   HOH A . 
C 3 HOH   88  488 206 HOH   HOH A . 
C 3 HOH   89  489 47  HOH   HOH A . 
C 3 HOH   90  490 89  HOH   HOH A . 
C 3 HOH   91  491 19  HOH   HOH A . 
C 3 HOH   92  492 74  HOH   HOH A . 
C 3 HOH   93  493 25  HOH   HOH A . 
C 3 HOH   94  494 72  HOH   HOH A . 
C 3 HOH   95  495 18  HOH   HOH A . 
C 3 HOH   96  496 29  HOH   HOH A . 
C 3 HOH   97  497 55  HOH   HOH A . 
C 3 HOH   98  498 286 HOH   HOH A . 
C 3 HOH   99  499 79  HOH   HOH A . 
C 3 HOH   100 500 51  HOH   HOH A . 
C 3 HOH   101 501 256 HOH   HOH A . 
C 3 HOH   102 502 229 HOH   HOH A . 
C 3 HOH   103 503 14  HOH   HOH A . 
C 3 HOH   104 504 34  HOH   HOH A . 
C 3 HOH   105 505 168 HOH   HOH A . 
C 3 HOH   106 506 77  HOH   HOH A . 
C 3 HOH   107 507 12  HOH   HOH A . 
C 3 HOH   108 508 98  HOH   HOH A . 
C 3 HOH   109 509 187 HOH   HOH A . 
C 3 HOH   110 510 46  HOH   HOH A . 
C 3 HOH   111 511 222 HOH   HOH A . 
C 3 HOH   112 512 85  HOH   HOH A . 
C 3 HOH   113 513 75  HOH   HOH A . 
C 3 HOH   114 514 112 HOH   HOH A . 
C 3 HOH   115 515 297 HOH   HOH A . 
C 3 HOH   116 516 134 HOH   HOH A . 
C 3 HOH   117 517 119 HOH   HOH A . 
C 3 HOH   118 518 212 HOH   HOH A . 
C 3 HOH   119 519 165 HOH   HOH A . 
C 3 HOH   120 520 33  HOH   HOH A . 
C 3 HOH   121 521 41  HOH   HOH A . 
C 3 HOH   122 522 228 HOH   HOH A . 
C 3 HOH   123 523 97  HOH   HOH A . 
C 3 HOH   124 524 230 HOH   HOH A . 
C 3 HOH   125 525 225 HOH   HOH A . 
C 3 HOH   126 526 262 HOH   HOH A . 
C 3 HOH   127 527 254 HOH   HOH A . 
C 3 HOH   128 528 53  HOH   HOH A . 
C 3 HOH   129 529 196 HOH   HOH A . 
C 3 HOH   130 530 310 HOH   HOH A . 
C 3 HOH   131 531 294 HOH   HOH A . 
C 3 HOH   132 532 54  HOH   HOH A . 
C 3 HOH   133 533 35  HOH   HOH A . 
C 3 HOH   134 534 293 HOH   HOH A . 
C 3 HOH   135 535 120 HOH   HOH A . 
C 3 HOH   136 536 200 HOH   HOH A . 
C 3 HOH   137 537 252 HOH   HOH A . 
C 3 HOH   138 538 106 HOH   HOH A . 
C 3 HOH   139 539 103 HOH   HOH A . 
C 3 HOH   140 540 86  HOH   HOH A . 
C 3 HOH   141 541 285 HOH   HOH A . 
C 3 HOH   142 542 129 HOH   HOH A . 
C 3 HOH   143 543 308 HOH   HOH A . 
C 3 HOH   144 544 45  HOH   HOH A . 
C 3 HOH   145 545 66  HOH   HOH A . 
C 3 HOH   146 546 56  HOH   HOH A . 
C 3 HOH   147 547 3   HOH   HOH A . 
C 3 HOH   148 548 6   HOH   HOH A . 
C 3 HOH   149 549 224 HOH   HOH A . 
C 3 HOH   150 550 22  HOH   HOH A . 
C 3 HOH   151 551 155 HOH   HOH A . 
C 3 HOH   152 552 251 HOH   HOH A . 
C 3 HOH   153 553 114 HOH   HOH A . 
C 3 HOH   154 554 281 HOH   HOH A . 
C 3 HOH   155 555 16  HOH   HOH A . 
C 3 HOH   156 556 280 HOH   HOH A . 
C 3 HOH   157 557 102 HOH   HOH A . 
C 3 HOH   158 558 37  HOH   HOH A . 
C 3 HOH   159 559 227 HOH   HOH A . 
C 3 HOH   160 560 44  HOH   HOH A . 
C 3 HOH   161 561 31  HOH   HOH A . 
C 3 HOH   162 562 232 HOH   HOH A . 
C 3 HOH   163 563 80  HOH   HOH A . 
C 3 HOH   164 564 93  HOH   HOH A . 
C 3 HOH   165 565 150 HOH   HOH A . 
C 3 HOH   166 566 174 HOH   HOH A . 
C 3 HOH   167 567 78  HOH   HOH A . 
C 3 HOH   168 568 186 HOH   HOH A . 
C 3 HOH   169 569 152 HOH   HOH A . 
C 3 HOH   170 570 271 HOH   HOH A . 
C 3 HOH   171 571 184 HOH   HOH A . 
C 3 HOH   172 572 309 HOH   HOH A . 
C 3 HOH   173 573 144 HOH   HOH A . 
C 3 HOH   174 574 39  HOH   HOH A . 
C 3 HOH   175 575 305 HOH   HOH A . 
C 3 HOH   176 576 4   HOH   HOH A . 
C 3 HOH   177 577 238 HOH   HOH A . 
C 3 HOH   178 578 128 HOH   HOH A . 
C 3 HOH   179 579 163 HOH   HOH A . 
C 3 HOH   180 580 58  HOH   HOH A . 
C 3 HOH   181 581 220 HOH   HOH A . 
C 3 HOH   182 582 21  HOH   HOH A . 
C 3 HOH   183 583 67  HOH   HOH A . 
C 3 HOH   184 584 52  HOH   HOH A . 
C 3 HOH   185 585 195 HOH   HOH A . 
C 3 HOH   186 586 92  HOH   HOH A . 
C 3 HOH   187 587 2   HOH   HOH A . 
C 3 HOH   188 588 234 HOH   HOH A . 
C 3 HOH   189 589 257 HOH   HOH A . 
C 3 HOH   190 590 215 HOH   HOH A . 
C 3 HOH   191 591 273 HOH   HOH A . 
C 3 HOH   192 592 296 HOH   HOH A . 
C 3 HOH   193 593 123 HOH   HOH A . 
C 3 HOH   194 594 160 HOH   HOH A . 
C 3 HOH   195 595 36  HOH   HOH A . 
C 3 HOH   196 596 291 HOH   HOH A . 
C 3 HOH   197 597 162 HOH   HOH A . 
C 3 HOH   198 598 190 HOH   HOH A . 
C 3 HOH   199 599 253 HOH   HOH A . 
C 3 HOH   200 600 300 HOH   HOH A . 
C 3 HOH   201 601 11  HOH   HOH A . 
C 3 HOH   202 602 250 HOH   HOH A . 
C 3 HOH   203 603 146 HOH   HOH A . 
C 3 HOH   204 604 193 HOH   HOH A . 
C 3 HOH   205 605 292 HOH   HOH A . 
C 3 HOH   206 606 138 HOH   HOH A . 
C 3 HOH   207 607 147 HOH   HOH A . 
C 3 HOH   208 608 131 HOH   HOH A . 
C 3 HOH   209 609 142 HOH   HOH A . 
C 3 HOH   210 610 295 HOH   HOH A . 
C 3 HOH   211 611 249 HOH   HOH A . 
C 3 HOH   212 612 288 HOH   HOH A . 
C 3 HOH   213 613 290 HOH   HOH A . 
C 3 HOH   214 614 94  HOH   HOH A . 
C 3 HOH   215 615 298 HOH   HOH A . 
C 3 HOH   216 616 161 HOH   HOH A . 
C 3 HOH   217 617 259 HOH   HOH A . 
C 3 HOH   218 618 221 HOH   HOH A . 
C 3 HOH   219 619 240 HOH   HOH A . 
C 3 HOH   220 620 242 HOH   HOH A . 
C 3 HOH   221 621 226 HOH   HOH A . 
C 3 HOH   222 622 264 HOH   HOH A . 
C 3 HOH   223 623 71  HOH   HOH A . 
C 3 HOH   224 624 277 HOH   HOH A . 
C 3 HOH   225 625 197 HOH   HOH A . 
C 3 HOH   226 626 208 HOH   HOH A . 
C 3 HOH   227 627 133 HOH   HOH A . 
C 3 HOH   228 628 266 HOH   HOH A . 
C 3 HOH   229 629 223 HOH   HOH A . 
C 3 HOH   230 630 191 HOH   HOH A . 
C 3 HOH   231 631 255 HOH   HOH A . 
C 3 HOH   232 632 171 HOH   HOH A . 
C 3 HOH   233 633 237 HOH   HOH A . 
C 3 HOH   234 634 192 HOH   HOH A . 
C 3 HOH   235 635 245 HOH   HOH A . 
C 3 HOH   236 636 127 HOH   HOH A . 
C 3 HOH   237 637 301 HOH   HOH A . 
C 3 HOH   238 638 175 HOH   HOH A . 
C 3 HOH   239 639 303 HOH   HOH A . 
C 3 HOH   240 640 101 HOH   HOH A . 
C 3 HOH   241 641 104 HOH   HOH A . 
C 3 HOH   242 642 207 HOH   HOH A . 
C 3 HOH   243 643 169 HOH   HOH A . 
C 3 HOH   244 644 235 HOH   HOH A . 
C 3 HOH   245 645 130 HOH   HOH A . 
C 3 HOH   246 646 157 HOH   HOH A . 
C 3 HOH   247 647 265 HOH   HOH A . 
C 3 HOH   248 648 173 HOH   HOH A . 
C 3 HOH   249 649 69  HOH   HOH A . 
C 3 HOH   250 650 170 HOH   HOH A . 
C 3 HOH   251 651 261 HOH   HOH A . 
C 3 HOH   252 652 188 HOH   HOH A . 
C 3 HOH   253 653 96  HOH   HOH A . 
C 3 HOH   254 654 149 HOH   HOH A . 
C 3 HOH   255 655 260 HOH   HOH A . 
C 3 HOH   256 656 204 HOH   HOH A . 
C 3 HOH   257 657 59  HOH   HOH A . 
C 3 HOH   258 658 108 HOH   HOH A . 
C 3 HOH   259 659 203 HOH   HOH A . 
C 3 HOH   260 660 219 HOH   HOH A . 
C 3 HOH   261 661 154 HOH   HOH A . 
C 3 HOH   262 662 148 HOH   HOH A . 
C 3 HOH   263 663 63  HOH   HOH A . 
C 3 HOH   264 664 233 HOH   HOH A . 
C 3 HOH   265 665 287 HOH   HOH A . 
C 3 HOH   266 666 299 HOH   HOH A . 
C 3 HOH   267 667 141 HOH   HOH A . 
C 3 HOH   268 668 159 HOH   HOH A . 
C 3 HOH   269 669 205 HOH   HOH A . 
C 3 HOH   270 670 176 HOH   HOH A . 
C 3 HOH   271 671 236 HOH   HOH A . 
C 3 HOH   272 672 276 HOH   HOH A . 
C 3 HOH   273 673 210 HOH   HOH A . 
C 3 HOH   274 674 278 HOH   HOH A . 
C 3 HOH   275 675 304 HOH   HOH A . 
C 3 HOH   276 676 100 HOH   HOH A . 
C 3 HOH   277 677 284 HOH   HOH A . 
C 3 HOH   278 678 201 HOH   HOH A . 
C 3 HOH   279 679 243 HOH   HOH A . 
C 3 HOH   280 680 283 HOH   HOH A . 
C 3 HOH   281 681 182 HOH   HOH A . 
C 3 HOH   282 682 211 HOH   HOH A . 
C 3 HOH   283 683 116 HOH   HOH A . 
C 3 HOH   284 684 124 HOH   HOH A . 
C 3 HOH   285 685 213 HOH   HOH A . 
C 3 HOH   286 686 269 HOH   HOH A . 
C 3 HOH   287 687 246 HOH   HOH A . 
C 3 HOH   288 688 189 HOH   HOH A . 
C 3 HOH   289 689 181 HOH   HOH A . 
C 3 HOH   290 690 99  HOH   HOH A . 
C 3 HOH   291 691 231 HOH   HOH A . 
C 3 HOH   292 692 268 HOH   HOH A . 
C 3 HOH   293 693 214 HOH   HOH A . 
C 3 HOH   294 694 248 HOH   HOH A . 
C 3 HOH   295 695 263 HOH   HOH A . 
C 3 HOH   296 696 140 HOH   HOH A . 
C 3 HOH   297 697 177 HOH   HOH A . 
C 3 HOH   298 698 194 HOH   HOH A . 
C 3 HOH   299 699 145 HOH   HOH A . 
C 3 HOH   300 700 306 HOH   HOH A . 
C 3 HOH   301 701 122 HOH   HOH A . 
C 3 HOH   302 702 158 HOH   HOH A . 
C 3 HOH   303 703 183 HOH   HOH A . 
C 3 HOH   304 704 244 HOH   HOH A . 
C 3 HOH   305 705 274 HOH   HOH A . 
C 3 HOH   306 706 289 HOH   HOH A . 
C 3 HOH   307 707 216 HOH   HOH A . 
C 3 HOH   308 708 132 HOH   HOH A . 
C 3 HOH   309 709 166 HOH   HOH A . 
C 3 HOH   310 710 307 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             588709.776 
_cell.length_a           65.866 
_cell.length_b           89.430 
_cell.length_c           99.944 
_cell.angle_beta         90.000 
_cell.angle_gamma        90.000 
_cell.angle_alpha        90.000 
_cell.entry_id           7HAD 
_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                         7HAD 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
# 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
_exptl.entry_id          7HAD 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_Matthews      2.88 
_exptl_crystal.density_percent_sol   57.23 
_exptl_crystal.density_meas          ? 
_exptl_crystal.description           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.pH              8.5 
_exptl_crystal_grow.temp            277 
_exptl_crystal_grow.pdbx_details    '100mM Tris-HCl pH 8.5, 22% PEG4000, 200mM MgCl2' 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_diffrn.id                     1 
_diffrn.crystal_id             1 
_diffrn.ambient_temp           100 
_diffrn.ambient_temp_details   ? 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               PIXEL 
_diffrn_detector.type                   'DECTRIS EIGER2 S 9M' 
_diffrn_detector.pdbx_collection_date   2023-07-04 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.pdbx_scattering_type             x-ray 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.monochromator                    Si111 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.97918 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.pdbx_synchrotron_beamline   BL02U1 
_diffrn_source.type                        'SSRF BEAMLINE BL02U1' 
_diffrn_source.pdbx_wavelength_list        0.97918 
_diffrn_source.pdbx_synchrotron_site       SSRF 
_diffrn_source.pdbx_wavelength             ? 
# 
_reflns.entry_id                     7HAD 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             53.030 
_reflns.d_resolution_high            1.590 
_reflns.number_obs                   39938 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         100.000 
_reflns.pdbx_Rmerge_I_obs            0.053 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        24.400 
_reflns.B_iso_Wilson_estimate        ? 
_reflns.pdbx_redundancy              12.300 
_reflns.pdbx_Rrim_I_all              0.056 
_reflns.pdbx_Rpim_I_all              0.016 
_reflns.pdbx_CC_half                 1.000 
_reflns.pdbx_netI_over_av_sigmaI     ? 
_reflns.pdbx_number_measured_all     490603 
_reflns.pdbx_scaling_rejects         61 
_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                      ? 
_reflns.pdbx_CC_star                 ? 
# 
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 
_reflns_shell.pdbx_CC_star 
1 1 1.590 1.680  ? 54909 5742 ? 0.760 ? ? ? 9.600  ? 2.700  ? ? ? ? ? ? 100.000 0.803 0.256 0.896 ? 
1 2 5.030 53.030 ? 16174 1372 ? 0.029 ? ? ? 11.800 ? 63.900 ? ? ? ? ? ? 99.600  0.031 0.009 0.999 ? 
# 
_refine.entry_id                                 7HAD 
_refine.pdbx_method_to_determine_struct          'FOURIER SYNTHESIS' 
_refine.ls_percent_reflns_R_free                 4.75 
_refine.pdbx_overall_phase_error                 18.9135 
_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                          0.1664 
_refine.B_iso_mean                               31.18 
_refine.ls_number_reflns_R_free                  1897 
_refine.ls_percent_reflns_obs                    99.96 
_refine.ls_R_factor_R_work                       0.1653 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_refine.ls_d_res_high                            1.59 
_refine.ls_number_reflns_obs                     39923 
_refine.pdbx_ls_sigma_F                          1.34 
_refine.ls_number_reflns_R_work                  38026 
_refine.ls_d_res_low                             31.22 
_refine.pdbx_stereochemistry_target_values       'GeoStd + Monomer Library + CDL v1.2' 
_refine.ls_R_factor_R_free                       0.1906 
_refine.overall_SU_ML                            0.1691 
_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         11 
_refine_hist.number_atoms_solvent             310 
_refine_hist.number_atoms_total               1965 
_refine_hist.d_res_high                       1.59 
_refine_hist.d_res_low                        31.22 
# 
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           1681 0.0113 ? ? ? 
'X-RAY DIFFRACTION' f_angle_d          2266 1.1302 ? ? ? 
'X-RAY DIFFRACTION' f_chiral_restr     259  0.0719 ? ? ? 
'X-RAY DIFFRACTION' f_plane_restr      289  0.0082 ? ? ? 
'X-RAY DIFFRACTION' f_dihedral_angle_d 223  7.1213 ? ? ? 
# 
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 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.number_reflns_obs 
'X-RAY DIFFRACTION' 1.59 1.63  2695 0.2570 99.93  0.2684 129 . . . . . . . 
'X-RAY DIFFRACTION' 1.63 1.67  2649 0.2229 100.00 0.2511 136 . . . . . . . 
'X-RAY DIFFRACTION' 1.67 1.72  2668 0.2025 99.86  0.2295 160 . . . . . . . 
'X-RAY DIFFRACTION' 1.72 1.78  2718 0.1823 99.96  0.2176 124 . . . . . . . 
'X-RAY DIFFRACTION' 1.78 1.84  2660 0.1777 99.96  0.2106 136 . . . . . . . 
'X-RAY DIFFRACTION' 1.84 1.92  2711 0.1819 99.89  0.2049 128 . . . . . . . 
'X-RAY DIFFRACTION' 1.92 2.00  2673 0.1803 99.93  0.2203 141 . . . . . . . 
'X-RAY DIFFRACTION' 2.00 2.11  2689 0.1692 100.00 0.2102 141 . . . . . . . 
'X-RAY DIFFRACTION' 2.11 2.24  2712 0.1608 100.00 0.1715 145 . . . . . . . 
'X-RAY DIFFRACTION' 2.24 2.42  2710 0.1666 100.00 0.2176 142 . . . . . . . 
'X-RAY DIFFRACTION' 2.42 2.66  2747 0.1751 99.97  0.1844 120 . . . . . . . 
'X-RAY DIFFRACTION' 2.66 3.04  2731 0.1665 100.00 0.1926 125 . . . . . . . 
'X-RAY DIFFRACTION' 3.04 3.83  2764 0.1510 100.00 0.1789 146 . . . . . . . 
'X-RAY DIFFRACTION' 3.83 31.22 2899 0.1515 99.90  0.1671 124 . . . . . . . 
# 
_struct.entry_id                  7HAD 
_struct.title                     'PanDDA analysis group deposition -- Crystal structure of HSP90N in complex with Fr14363' 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_details        ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HAD 
_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              7HAD 
_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 7HAD MET A 1   ? UNP P07900 ? ? 'initiating methionine' 8   1 
1 7HAD LEU A 230 ? UNP P07900 ? ? 'expression tag'        237 2 
1 7HAD GLU A 231 ? UNP P07900 ? ? 'expression tag'        238 3 
1 7HAD HIS A 232 ? UNP P07900 ? ? 'expression tag'        239 4 
1 7HAD HIS A 233 ? UNP P07900 ? ? 'expression tag'        240 5 
1 7HAD HIS A 234 ? UNP P07900 ? ? 'expression tag'        241 6 
1 7HAD HIS A 235 ? UNP P07900 ? ? 'expression tag'        242 7 
1 7HAD HIS A 236 ? UNP P07900 ? ? 'expression tag'        243 8 
1 7HAD HIS A 237 ? UNP P07900 ? ? 'expression tag'        244 9 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 GLN A 16  ? THR A 29  ? GLN A 23  THR A 36  1 ? 14 
HELX_P HELX_P2  AA2 GLU A 35  ? ASP A 59  ? GLU A 42  ASP A 66  1 ? 25 
HELX_P HELX_P3  AA3 PRO A 60  ? ASP A 64  ? PRO A 67  ASP A 71  5 ? 5  
HELX_P HELX_P4  AA4 THR A 92  ? ASN A 98  ? THR A 99  ASN A 105 1 ? 7  
HELX_P HELX_P5  AA5 ASN A 99  ? THR A 102 ? ASN A 106 THR A 109 5 ? 4  
HELX_P HELX_P6  AA6 ILE A 103 ? GLN A 116 ? ILE A 110 GLN A 123 1 ? 14 
HELX_P HELX_P7  AA7 ASP A 120 ? GLY A 128 ? ASP A 127 GLY A 135 5 ? 9  
HELX_P HELX_P8  AA8 VAL A 129 ? LEU A 136 ? VAL A 136 LEU A 143 5 ? 8  
HELX_P HELX_P9  AA9 GLU A 185 ? LEU A 191 ? GLU A 192 LEU A 198 5 ? 7  
HELX_P HELX_P10 AB1 GLU A 192 ? SER A 204 ? GLU A 199 SER A 211 1 ? 13 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
_struct_sheet.id               AA1 
_struct_sheet.type             ? 
_struct_sheet.number_strands   8 
_struct_sheet.details          ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA1 5 6 ? anti-parallel 
AA1 6 7 ? anti-parallel 
AA1 7 8 ? parallel      
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 VAL A 10  ? ALA A 14  ? VAL A 17  ALA A 21  
AA1 2 SER A 162 ? THR A 167 ? SER A 169 THR A 174 
AA1 3 TYR A 153 ? SER A 157 ? TYR A 160 SER A 164 
AA1 4 ALA A 138 ? LYS A 146 ? ALA A 145 LYS A 153 
AA1 5 GLY A 176 ? LEU A 183 ? GLY A 183 LEU A 190 
AA1 6 THR A 81  ? ASP A 86  ? THR A 88  ASP A 93  
AA1 7 ILE A 71  ? ASN A 76  ? ILE A 78  ASN A 83  
AA1 8 ILE A 211 ? LEU A 213 ? ILE A 218 LEU A 220 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N PHE A 13  ? N PHE A 20  O PHE A 163 ? O PHE A 170 
AA1 2 3 O ARG A 166 ? O ARG A 173 N ALA A 154 ? N ALA A 161 
AA1 3 4 O TRP A 155 ? O TRP A 162 N VAL A 143 ? N VAL A 150 
AA1 4 5 N THR A 142 ? N THR A 149 O ILE A 180 ? O ILE A 187 
AA1 5 6 O LEU A 181 ? O LEU A 188 N LEU A 82  ? N LEU A 89  
AA1 6 7 O VAL A 85  ? O VAL A 92  N ASN A 72  ? N ASN A 79  
AA1 7 8 N LEU A 73  ? N LEU A 80  O THR A 212 ? O THR A 219 
# 
_pdbx_entry_details.entry_id                   7HAD 
_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 620 ? ? O A HOH 633 ? ? 1.85 
2 1 OE2 A GLU 199 ? ? O A HOH 401 ? ? 1.86 
3 1 O   A HOH 679 ? ? O A HOH 705 ? ? 1.94 
4 1 O   A HOH 462 ? ? O A HOH 677 ? ? 1.96 
5 1 O   A HOH 642 ? ? O A HOH 655 ? ? 1.98 
6 1 O   A HOH 401 ? ? O A HOH 626 ? ? 2.07 
7 1 OD1 A ASP 102 ? ? O A HOH 402 ? ? 2.11 
8 1 O   A HOH 567 ? ? O A HOH 637 ? ? 2.14 
9 1 O   A HOH 415 ? ? O A HOH 573 ? ? 2.16 
# 
_pdbx_validate_symm_contact.id                1 
_pdbx_validate_symm_contact.PDB_model_num     1 
_pdbx_validate_symm_contact.auth_atom_id_1    O 
_pdbx_validate_symm_contact.auth_asym_id_1    A 
_pdbx_validate_symm_contact.auth_comp_id_1    HOH 
_pdbx_validate_symm_contact.auth_seq_id_1     402 
_pdbx_validate_symm_contact.PDB_ins_code_1    ? 
_pdbx_validate_symm_contact.label_alt_id_1    ? 
_pdbx_validate_symm_contact.site_symmetry_1   1_555 
_pdbx_validate_symm_contact.auth_atom_id_2    O 
_pdbx_validate_symm_contact.auth_asym_id_2    A 
_pdbx_validate_symm_contact.auth_comp_id_2    HOH 
_pdbx_validate_symm_contact.auth_seq_id_2     606 
_pdbx_validate_symm_contact.PDB_ins_code_2    ? 
_pdbx_validate_symm_contact.label_alt_id_2    ? 
_pdbx_validate_symm_contact.site_symmetry_2   2_555 
_pdbx_validate_symm_contact.dist              2.12 
# 
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  ? ? -162.43 110.08  
2 1 THR A 94  ? ? -106.83 40.18   
3 1 ALA A 166 ? ? 61.39   -145.37 
# 
_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     671 
_pdbx_struct_special_symmetry.PDB_ins_code    ? 
_pdbx_struct_special_symmetry.label_asym_id   C 
_pdbx_struct_special_symmetry.label_comp_id   HOH 
_pdbx_struct_special_symmetry.label_seq_id    . 
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z               
2 x,-y,-z             
3 -x,y,-z             
4 -x,-y,z             
5 x+1/2,y+1/2,z+1/2   
6 x+1/2,-y+1/2,-z+1/2 
7 -x+1/2,y+1/2,-z+1/2 
8 -x+1/2,-y+1/2,z+1/2 
# 
loop_
_pdbx_refine_tls.id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][3] 
1 ? 'X-RAY DIFFRACTION' refined 12.2983456218  -17.8820987963 -18.8301801277 0.137717231104 0.189559575916 0.19341293287  
0.010835385197    -0.0377223781317 -0.0165438665732  3.59638789957 1.71414235195 6.56859166288 -1.19620990057  -3.85520783579  
0.665288047745  0.141735989412   -0.371737214406 -0.00882526663678 -0.0428224292103 -0.111263110626  -0.101002494131  
0.0458414307157 0.423769754571  -0.0466351178724  
2 ? 'X-RAY DIFFRACTION' refined -5.23128743802 -6.27372103015 -21.0328155888 0.177723169203 0.168841695191 0.212047458107 
-0.0115129625188  0.00233247597794 -0.0459581412246  3.55678848875 8.80357009278 7.91228699745 -4.15939319207  4.12913398041   
-7.19315133343  -0.0513754075073 0.104005071642  0.193773060338    0.106946869523   -0.127426015031  -0.0502275382292 
-0.386024968648 0.320236563033  0.142477589745    
3 ? 'X-RAY DIFFRACTION' refined -10.1878101232 -14.9732486967 -25.1846258683 0.157625748717 0.142198956427 0.209241360936 
-0.005811567912   -0.059025294987  -0.0542940875147  2.26905665442 3.74829961341 4.87629607641 -0.521118756592 -0.216482997403 
-2.238640723    0.0877569824079  0.0813880265063 -0.1518649396     -0.226145070663  0.047918887153   0.320644215341   
0.154447381468  -0.251000655782 -0.180823179707   
4 ? 'X-RAY DIFFRACTION' refined 10.642063468   -7.40910862308 -18.1159749254 0.188912335628 0.293134689379 0.275171335846 
-0.0496222710399  0.0277485162861  -0.0706482458628  4.02255343307 3.15521248978 6.74712323024 0.801118193371  -0.739047979837 
1.35047192791   0.239172726417   -0.651046780165 0.500593593348    0.132160337474   -0.161246221044  -0.206764207449  
-0.458530621762 0.756079590322  -0.00741487327634 
5 ? 'X-RAY DIFFRACTION' refined 0.762328381197 -19.3276898328 -27.8539153798 0.169975467837 0.140600313446 0.187944934141 
0.00501391302128  -0.0193989635913 -0.0354742737972  3.7839257639  2.28608481392 3.08058362386 -1.5904514792   0.9131298752    
-0.543034146507 0.232177110024   0.260263462655  -0.303151145984   -0.264143631043  -0.0933328728363 0.165394439497   
0.231869763919  0.0126620797439 -0.162490216185   
6 ? 'X-RAY DIFFRACTION' refined -2.59682099349 -23.5971321909 -13.6732375047 0.189811220873 0.15353930583  0.198930735979 
-0.0119724394745  -0.0277827404222 -0.00078581137156 5.11252185408 6.37719365684 8.98848773439 -1.35260878222  0.333228828454  
-3.76027265404  0.0862797896369  -0.358915440737 -0.374652513623   0.134106226875   -0.120972085208  -0.0168727369495 
0.607239137886  0.401762656269  -0.0191339687334  
7 ? 'X-RAY DIFFRACTION' refined -12.1309132461 -14.1657024802 -10.4543033951 0.148997271858 0.205360951449 0.172700883907 
-0.00558296690734 0.00777434625038 -0.0188948554689  3.95349206955 2.38787987538 6.16364307593 -1.12780061658  0.134374831788  
-1.31669864489  -0.0151575784047 -0.473851281962 -0.146360723221   0.254582773514   0.0607957900938  0.15628465902    
-0.169765419307 -0.176755078198 -0.0025408299019  
# 
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 199 A 184 . 
;chain 'A' and (resid 183 through 199 )
;
7 7 'X-RAY DIFFRACTION' A 200 A 185 A 224 A 209 . 
;chain 'A' and (resid 200 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 
A1AX3 C1   C N N 1   
A1AX3 C2   C Y N 2   
A1AX3 C3   C Y N 3   
A1AX3 N1   N N N 4   
A1AX3 C4   C Y N 5   
A1AX3 C5   C Y N 6   
A1AX3 C6   C Y N 7   
A1AX3 C7   C N N 8   
A1AX3 C8   C Y N 9   
A1AX3 C9   C N N 10  
A1AX3 O1   O N N 11  
A1AX3 H12  H N N 12  
A1AX3 H11  H N N 13  
A1AX3 H13  H N N 14  
A1AX3 H3   H N N 15  
A1AX3 HN11 H N N 16  
A1AX3 HN12 H N N 17  
A1AX3 H4   H N N 18  
A1AX3 H5   H N N 19  
A1AX3 H92  H N N 20  
A1AX3 H91  H N N 21  
A1AX3 H93  H N N 22  
ALA   N    N N N 23  
ALA   CA   C N S 24  
ALA   C    C N N 25  
ALA   O    O N N 26  
ALA   CB   C N N 27  
ALA   OXT  O N N 28  
ALA   H    H N N 29  
ALA   H2   H N N 30  
ALA   HA   H N N 31  
ALA   HB1  H N N 32  
ALA   HB2  H N N 33  
ALA   HB3  H N N 34  
ALA   HXT  H N N 35  
ARG   N    N N N 36  
ARG   CA   C N S 37  
ARG   C    C N N 38  
ARG   O    O N N 39  
ARG   CB   C N N 40  
ARG   CG   C N N 41  
ARG   CD   C N N 42  
ARG   NE   N N N 43  
ARG   CZ   C N N 44  
ARG   NH1  N N N 45  
ARG   NH2  N N N 46  
ARG   OXT  O N N 47  
ARG   H    H N N 48  
ARG   H2   H N N 49  
ARG   HA   H N N 50  
ARG   HB2  H N N 51  
ARG   HB3  H N N 52  
ARG   HG2  H N N 53  
ARG   HG3  H N N 54  
ARG   HD2  H N N 55  
ARG   HD3  H N N 56  
ARG   HE   H N N 57  
ARG   HH11 H N N 58  
ARG   HH12 H N N 59  
ARG   HH21 H N N 60  
ARG   HH22 H N N 61  
ARG   HXT  H N N 62  
ASN   N    N N N 63  
ASN   CA   C N S 64  
ASN   C    C N N 65  
ASN   O    O N N 66  
ASN   CB   C N N 67  
ASN   CG   C N N 68  
ASN   OD1  O N N 69  
ASN   ND2  N N N 70  
ASN   OXT  O N N 71  
ASN   H    H N N 72  
ASN   H2   H N N 73  
ASN   HA   H N N 74  
ASN   HB2  H N N 75  
ASN   HB3  H N N 76  
ASN   HD21 H N N 77  
ASN   HD22 H N N 78  
ASN   HXT  H N N 79  
ASP   N    N N N 80  
ASP   CA   C N S 81  
ASP   C    C N N 82  
ASP   O    O N N 83  
ASP   CB   C N N 84  
ASP   CG   C N N 85  
ASP   OD1  O N N 86  
ASP   OD2  O N N 87  
ASP   OXT  O N N 88  
ASP   H    H N N 89  
ASP   H2   H N N 90  
ASP   HA   H N N 91  
ASP   HB2  H N N 92  
ASP   HB3  H N N 93  
ASP   HD2  H N N 94  
ASP   HXT  H N N 95  
GLN   N    N N N 96  
GLN   CA   C N S 97  
GLN   C    C N N 98  
GLN   O    O N N 99  
GLN   CB   C N N 100 
GLN   CG   C N N 101 
GLN   CD   C N N 102 
GLN   OE1  O N N 103 
GLN   NE2  N N N 104 
GLN   OXT  O N N 105 
GLN   H    H N N 106 
GLN   H2   H N N 107 
GLN   HA   H N N 108 
GLN   HB2  H N N 109 
GLN   HB3  H N N 110 
GLN   HG2  H N N 111 
GLN   HG3  H N N 112 
GLN   HE21 H N N 113 
GLN   HE22 H N N 114 
GLN   HXT  H N N 115 
GLU   N    N N N 116 
GLU   CA   C N S 117 
GLU   C    C N N 118 
GLU   O    O N N 119 
GLU   CB   C N N 120 
GLU   CG   C N N 121 
GLU   CD   C N N 122 
GLU   OE1  O N N 123 
GLU   OE2  O N N 124 
GLU   OXT  O N N 125 
GLU   H    H N N 126 
GLU   H2   H N N 127 
GLU   HA   H N N 128 
GLU   HB2  H N N 129 
GLU   HB3  H N N 130 
GLU   HG2  H N N 131 
GLU   HG3  H N N 132 
GLU   HE2  H N N 133 
GLU   HXT  H N N 134 
GLY   N    N N N 135 
GLY   CA   C N N 136 
GLY   C    C N N 137 
GLY   O    O N N 138 
GLY   OXT  O N N 139 
GLY   H    H N N 140 
GLY   H2   H N N 141 
GLY   HA2  H N N 142 
GLY   HA3  H N N 143 
GLY   HXT  H N N 144 
HIS   N    N N N 145 
HIS   CA   C N S 146 
HIS   C    C N N 147 
HIS   O    O N N 148 
HIS   CB   C N N 149 
HIS   CG   C Y N 150 
HIS   ND1  N Y N 151 
HIS   CD2  C Y N 152 
HIS   CE1  C Y N 153 
HIS   NE2  N Y N 154 
HIS   OXT  O N N 155 
HIS   H    H N N 156 
HIS   H2   H N N 157 
HIS   HA   H N N 158 
HIS   HB2  H N N 159 
HIS   HB3  H N N 160 
HIS   HD1  H N N 161 
HIS   HD2  H N N 162 
HIS   HE1  H N N 163 
HIS   HE2  H N N 164 
HIS   HXT  H N N 165 
HOH   O    O N N 166 
HOH   H1   H N N 167 
HOH   H2   H N N 168 
ILE   N    N N N 169 
ILE   CA   C N S 170 
ILE   C    C N N 171 
ILE   O    O N N 172 
ILE   CB   C N S 173 
ILE   CG1  C N N 174 
ILE   CG2  C N N 175 
ILE   CD1  C N N 176 
ILE   OXT  O N N 177 
ILE   H    H N N 178 
ILE   H2   H N N 179 
ILE   HA   H N N 180 
ILE   HB   H N N 181 
ILE   HG12 H N N 182 
ILE   HG13 H N N 183 
ILE   HG21 H N N 184 
ILE   HG22 H N N 185 
ILE   HG23 H N N 186 
ILE   HD11 H N N 187 
ILE   HD12 H N N 188 
ILE   HD13 H N N 189 
ILE   HXT  H N N 190 
LEU   N    N N N 191 
LEU   CA   C N S 192 
LEU   C    C N N 193 
LEU   O    O N N 194 
LEU   CB   C N N 195 
LEU   CG   C N N 196 
LEU   CD1  C N N 197 
LEU   CD2  C N N 198 
LEU   OXT  O N N 199 
LEU   H    H N N 200 
LEU   H2   H N N 201 
LEU   HA   H N N 202 
LEU   HB2  H N N 203 
LEU   HB3  H N N 204 
LEU   HG   H N N 205 
LEU   HD11 H N N 206 
LEU   HD12 H N N 207 
LEU   HD13 H N N 208 
LEU   HD21 H N N 209 
LEU   HD22 H N N 210 
LEU   HD23 H N N 211 
LEU   HXT  H N N 212 
LYS   N    N N N 213 
LYS   CA   C N S 214 
LYS   C    C N N 215 
LYS   O    O N N 216 
LYS   CB   C N N 217 
LYS   CG   C N N 218 
LYS   CD   C N N 219 
LYS   CE   C N N 220 
LYS   NZ   N N N 221 
LYS   OXT  O N N 222 
LYS   H    H N N 223 
LYS   H2   H N N 224 
LYS   HA   H N N 225 
LYS   HB2  H N N 226 
LYS   HB3  H N N 227 
LYS   HG2  H N N 228 
LYS   HG3  H N N 229 
LYS   HD2  H N N 230 
LYS   HD3  H N N 231 
LYS   HE2  H N N 232 
LYS   HE3  H N N 233 
LYS   HZ1  H N N 234 
LYS   HZ2  H N N 235 
LYS   HZ3  H N N 236 
LYS   HXT  H N N 237 
MET   N    N N N 238 
MET   CA   C N S 239 
MET   C    C N N 240 
MET   O    O N N 241 
MET   CB   C N N 242 
MET   CG   C N N 243 
MET   SD   S N N 244 
MET   CE   C N N 245 
MET   OXT  O N N 246 
MET   H    H N N 247 
MET   H2   H N N 248 
MET   HA   H N N 249 
MET   HB2  H N N 250 
MET   HB3  H N N 251 
MET   HG2  H N N 252 
MET   HG3  H N N 253 
MET   HE1  H N N 254 
MET   HE2  H N N 255 
MET   HE3  H N N 256 
MET   HXT  H N N 257 
PHE   N    N N N 258 
PHE   CA   C N S 259 
PHE   C    C N N 260 
PHE   O    O N N 261 
PHE   CB   C N N 262 
PHE   CG   C Y N 263 
PHE   CD1  C Y N 264 
PHE   CD2  C Y N 265 
PHE   CE1  C Y N 266 
PHE   CE2  C Y N 267 
PHE   CZ   C Y N 268 
PHE   OXT  O N N 269 
PHE   H    H N N 270 
PHE   H2   H N N 271 
PHE   HA   H N N 272 
PHE   HB2  H N N 273 
PHE   HB3  H N N 274 
PHE   HD1  H N N 275 
PHE   HD2  H N N 276 
PHE   HE1  H N N 277 
PHE   HE2  H N N 278 
PHE   HZ   H N N 279 
PHE   HXT  H N N 280 
PRO   N    N N N 281 
PRO   CA   C N S 282 
PRO   C    C N N 283 
PRO   O    O N N 284 
PRO   CB   C N N 285 
PRO   CG   C N N 286 
PRO   CD   C N N 287 
PRO   OXT  O N N 288 
PRO   H    H N N 289 
PRO   HA   H N N 290 
PRO   HB2  H N N 291 
PRO   HB3  H N N 292 
PRO   HG2  H N N 293 
PRO   HG3  H N N 294 
PRO   HD2  H N N 295 
PRO   HD3  H N N 296 
PRO   HXT  H N N 297 
SER   N    N N N 298 
SER   CA   C N S 299 
SER   C    C N N 300 
SER   O    O N N 301 
SER   CB   C N N 302 
SER   OG   O N N 303 
SER   OXT  O N N 304 
SER   H    H N N 305 
SER   H2   H N N 306 
SER   HA   H N N 307 
SER   HB2  H N N 308 
SER   HB3  H N N 309 
SER   HG   H N N 310 
SER   HXT  H N N 311 
THR   N    N N N 312 
THR   CA   C N S 313 
THR   C    C N N 314 
THR   O    O N N 315 
THR   CB   C N R 316 
THR   OG1  O N N 317 
THR   CG2  C N N 318 
THR   OXT  O N N 319 
THR   H    H N N 320 
THR   H2   H N N 321 
THR   HA   H N N 322 
THR   HB   H N N 323 
THR   HG1  H N N 324 
THR   HG21 H N N 325 
THR   HG22 H N N 326 
THR   HG23 H N N 327 
THR   HXT  H N N 328 
TRP   N    N N N 329 
TRP   CA   C N S 330 
TRP   C    C N N 331 
TRP   O    O N N 332 
TRP   CB   C N N 333 
TRP   CG   C Y N 334 
TRP   CD1  C Y N 335 
TRP   CD2  C Y N 336 
TRP   NE1  N Y N 337 
TRP   CE2  C Y N 338 
TRP   CE3  C Y N 339 
TRP   CZ2  C Y N 340 
TRP   CZ3  C Y N 341 
TRP   CH2  C Y N 342 
TRP   OXT  O N N 343 
TRP   H    H N N 344 
TRP   H2   H N N 345 
TRP   HA   H N N 346 
TRP   HB2  H N N 347 
TRP   HB3  H N N 348 
TRP   HD1  H N N 349 
TRP   HE1  H N N 350 
TRP   HE3  H N N 351 
TRP   HZ2  H N N 352 
TRP   HZ3  H N N 353 
TRP   HH2  H N N 354 
TRP   HXT  H N N 355 
TYR   N    N N N 356 
TYR   CA   C N S 357 
TYR   C    C N N 358 
TYR   O    O N N 359 
TYR   CB   C N N 360 
TYR   CG   C Y N 361 
TYR   CD1  C Y N 362 
TYR   CD2  C Y N 363 
TYR   CE1  C Y N 364 
TYR   CE2  C Y N 365 
TYR   CZ   C Y N 366 
TYR   OH   O N N 367 
TYR   OXT  O N N 368 
TYR   H    H N N 369 
TYR   H2   H N N 370 
TYR   HA   H N N 371 
TYR   HB2  H N N 372 
TYR   HB3  H N N 373 
TYR   HD1  H N N 374 
TYR   HD2  H N N 375 
TYR   HE1  H N N 376 
TYR   HE2  H N N 377 
TYR   HH   H N N 378 
TYR   HXT  H N N 379 
VAL   N    N N N 380 
VAL   CA   C N S 381 
VAL   C    C N N 382 
VAL   O    O N N 383 
VAL   CB   C N N 384 
VAL   CG1  C N N 385 
VAL   CG2  C N N 386 
VAL   OXT  O N N 387 
VAL   H    H N N 388 
VAL   H2   H N N 389 
VAL   HA   H N N 390 
VAL   HB   H N N 391 
VAL   HG11 H N N 392 
VAL   HG12 H N N 393 
VAL   HG13 H N N 394 
VAL   HG21 H N N 395 
VAL   HG22 H N N 396 
VAL   HG23 H N N 397 
VAL   HXT  H N N 398 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
A1AX3 C1  C2   sing N N 1   
A1AX3 C2  C3   doub Y N 2   
A1AX3 C2  C8   sing Y N 3   
A1AX3 C3  C4   sing Y N 4   
A1AX3 C4  C5   doub Y N 5   
A1AX3 C5  C6   sing Y N 6   
A1AX3 C6  C7   sing N N 7   
A1AX3 C6  C8   doub Y N 8   
A1AX3 C7  N1   sing N N 9   
A1AX3 C7  O1   doub N N 10  
A1AX3 C8  C9   sing N N 11  
A1AX3 C1  H12  sing N N 12  
A1AX3 C1  H11  sing N N 13  
A1AX3 C1  H13  sing N N 14  
A1AX3 C3  H3   sing N N 15  
A1AX3 N1  HN11 sing N N 16  
A1AX3 N1  HN12 sing N N 17  
A1AX3 C4  H4   sing N N 18  
A1AX3 C5  H5   sing N N 19  
A1AX3 C9  H92  sing N N 20  
A1AX3 C9  H91  sing N N 21  
A1AX3 C9  H93  sing N N 22  
ALA   N   CA   sing N N 23  
ALA   N   H    sing N N 24  
ALA   N   H2   sing N N 25  
ALA   CA  C    sing N N 26  
ALA   CA  CB   sing N N 27  
ALA   CA  HA   sing N N 28  
ALA   C   O    doub N N 29  
ALA   C   OXT  sing N N 30  
ALA   CB  HB1  sing N N 31  
ALA   CB  HB2  sing N N 32  
ALA   CB  HB3  sing N N 33  
ALA   OXT HXT  sing N N 34  
ARG   N   CA   sing N N 35  
ARG   N   H    sing N N 36  
ARG   N   H2   sing N N 37  
ARG   CA  C    sing N N 38  
ARG   CA  CB   sing N N 39  
ARG   CA  HA   sing N N 40  
ARG   C   O    doub N N 41  
ARG   C   OXT  sing N N 42  
ARG   CB  CG   sing N N 43  
ARG   CB  HB2  sing N N 44  
ARG   CB  HB3  sing N N 45  
ARG   CG  CD   sing N N 46  
ARG   CG  HG2  sing N N 47  
ARG   CG  HG3  sing N N 48  
ARG   CD  NE   sing N N 49  
ARG   CD  HD2  sing N N 50  
ARG   CD  HD3  sing N N 51  
ARG   NE  CZ   sing N N 52  
ARG   NE  HE   sing N N 53  
ARG   CZ  NH1  sing N N 54  
ARG   CZ  NH2  doub N N 55  
ARG   NH1 HH11 sing N N 56  
ARG   NH1 HH12 sing N N 57  
ARG   NH2 HH21 sing N N 58  
ARG   NH2 HH22 sing N N 59  
ARG   OXT HXT  sing N N 60  
ASN   N   CA   sing N N 61  
ASN   N   H    sing N N 62  
ASN   N   H2   sing N N 63  
ASN   CA  C    sing N N 64  
ASN   CA  CB   sing N N 65  
ASN   CA  HA   sing N N 66  
ASN   C   O    doub N N 67  
ASN   C   OXT  sing N N 68  
ASN   CB  CG   sing N N 69  
ASN   CB  HB2  sing N N 70  
ASN   CB  HB3  sing N N 71  
ASN   CG  OD1  doub N N 72  
ASN   CG  ND2  sing N N 73  
ASN   ND2 HD21 sing N N 74  
ASN   ND2 HD22 sing N N 75  
ASN   OXT HXT  sing N N 76  
ASP   N   CA   sing N N 77  
ASP   N   H    sing N N 78  
ASP   N   H2   sing N N 79  
ASP   CA  C    sing N N 80  
ASP   CA  CB   sing N N 81  
ASP   CA  HA   sing N N 82  
ASP   C   O    doub N N 83  
ASP   C   OXT  sing N N 84  
ASP   CB  CG   sing N N 85  
ASP   CB  HB2  sing N N 86  
ASP   CB  HB3  sing N N 87  
ASP   CG  OD1  doub N N 88  
ASP   CG  OD2  sing N N 89  
ASP   OD2 HD2  sing N N 90  
ASP   OXT HXT  sing N N 91  
GLN   N   CA   sing N N 92  
GLN   N   H    sing N N 93  
GLN   N   H2   sing N N 94  
GLN   CA  C    sing N N 95  
GLN   CA  CB   sing N N 96  
GLN   CA  HA   sing N N 97  
GLN   C   O    doub N N 98  
GLN   C   OXT  sing N N 99  
GLN   CB  CG   sing N N 100 
GLN   CB  HB2  sing N N 101 
GLN   CB  HB3  sing N N 102 
GLN   CG  CD   sing N N 103 
GLN   CG  HG2  sing N N 104 
GLN   CG  HG3  sing N N 105 
GLN   CD  OE1  doub N N 106 
GLN   CD  NE2  sing N N 107 
GLN   NE2 HE21 sing N N 108 
GLN   NE2 HE22 sing N N 109 
GLN   OXT HXT  sing N N 110 
GLU   N   CA   sing N N 111 
GLU   N   H    sing N N 112 
GLU   N   H2   sing N N 113 
GLU   CA  C    sing N N 114 
GLU   CA  CB   sing N N 115 
GLU   CA  HA   sing N N 116 
GLU   C   O    doub N N 117 
GLU   C   OXT  sing N N 118 
GLU   CB  CG   sing N N 119 
GLU   CB  HB2  sing N N 120 
GLU   CB  HB3  sing N N 121 
GLU   CG  CD   sing N N 122 
GLU   CG  HG2  sing N N 123 
GLU   CG  HG3  sing N N 124 
GLU   CD  OE1  doub N N 125 
GLU   CD  OE2  sing N N 126 
GLU   OE2 HE2  sing N N 127 
GLU   OXT HXT  sing N N 128 
GLY   N   CA   sing N N 129 
GLY   N   H    sing N N 130 
GLY   N   H2   sing N N 131 
GLY   CA  C    sing N N 132 
GLY   CA  HA2  sing N N 133 
GLY   CA  HA3  sing N N 134 
GLY   C   O    doub N N 135 
GLY   C   OXT  sing N N 136 
GLY   OXT HXT  sing N N 137 
HIS   N   CA   sing N N 138 
HIS   N   H    sing N N 139 
HIS   N   H2   sing N N 140 
HIS   CA  C    sing N N 141 
HIS   CA  CB   sing N N 142 
HIS   CA  HA   sing N N 143 
HIS   C   O    doub N N 144 
HIS   C   OXT  sing N N 145 
HIS   CB  CG   sing N N 146 
HIS   CB  HB2  sing N N 147 
HIS   CB  HB3  sing N N 148 
HIS   CG  ND1  sing Y N 149 
HIS   CG  CD2  doub Y N 150 
HIS   ND1 CE1  doub Y N 151 
HIS   ND1 HD1  sing N N 152 
HIS   CD2 NE2  sing Y N 153 
HIS   CD2 HD2  sing N N 154 
HIS   CE1 NE2  sing Y N 155 
HIS   CE1 HE1  sing N N 156 
HIS   NE2 HE2  sing N N 157 
HIS   OXT HXT  sing N N 158 
HOH   O   H1   sing N N 159 
HOH   O   H2   sing N N 160 
ILE   N   CA   sing N N 161 
ILE   N   H    sing N N 162 
ILE   N   H2   sing N N 163 
ILE   CA  C    sing N N 164 
ILE   CA  CB   sing N N 165 
ILE   CA  HA   sing N N 166 
ILE   C   O    doub N N 167 
ILE   C   OXT  sing N N 168 
ILE   CB  CG1  sing N N 169 
ILE   CB  CG2  sing N N 170 
ILE   CB  HB   sing N N 171 
ILE   CG1 CD1  sing N N 172 
ILE   CG1 HG12 sing N N 173 
ILE   CG1 HG13 sing N N 174 
ILE   CG2 HG21 sing N N 175 
ILE   CG2 HG22 sing N N 176 
ILE   CG2 HG23 sing N N 177 
ILE   CD1 HD11 sing N N 178 
ILE   CD1 HD12 sing N N 179 
ILE   CD1 HD13 sing N N 180 
ILE   OXT HXT  sing N N 181 
LEU   N   CA   sing N N 182 
LEU   N   H    sing N N 183 
LEU   N   H2   sing N N 184 
LEU   CA  C    sing N N 185 
LEU   CA  CB   sing N N 186 
LEU   CA  HA   sing N N 187 
LEU   C   O    doub N N 188 
LEU   C   OXT  sing N N 189 
LEU   CB  CG   sing N N 190 
LEU   CB  HB2  sing N N 191 
LEU   CB  HB3  sing N N 192 
LEU   CG  CD1  sing N N 193 
LEU   CG  CD2  sing N N 194 
LEU   CG  HG   sing N N 195 
LEU   CD1 HD11 sing N N 196 
LEU   CD1 HD12 sing N N 197 
LEU   CD1 HD13 sing N N 198 
LEU   CD2 HD21 sing N N 199 
LEU   CD2 HD22 sing N N 200 
LEU   CD2 HD23 sing N N 201 
LEU   OXT HXT  sing N N 202 
LYS   N   CA   sing N N 203 
LYS   N   H    sing N N 204 
LYS   N   H2   sing N N 205 
LYS   CA  C    sing N N 206 
LYS   CA  CB   sing N N 207 
LYS   CA  HA   sing N N 208 
LYS   C   O    doub N N 209 
LYS   C   OXT  sing N N 210 
LYS   CB  CG   sing N N 211 
LYS   CB  HB2  sing N N 212 
LYS   CB  HB3  sing N N 213 
LYS   CG  CD   sing N N 214 
LYS   CG  HG2  sing N N 215 
LYS   CG  HG3  sing N N 216 
LYS   CD  CE   sing N N 217 
LYS   CD  HD2  sing N N 218 
LYS   CD  HD3  sing N N 219 
LYS   CE  NZ   sing N N 220 
LYS   CE  HE2  sing N N 221 
LYS   CE  HE3  sing N N 222 
LYS   NZ  HZ1  sing N N 223 
LYS   NZ  HZ2  sing N N 224 
LYS   NZ  HZ3  sing N N 225 
LYS   OXT HXT  sing N N 226 
MET   N   CA   sing N N 227 
MET   N   H    sing N N 228 
MET   N   H2   sing N N 229 
MET   CA  C    sing N N 230 
MET   CA  CB   sing N N 231 
MET   CA  HA   sing N N 232 
MET   C   O    doub N N 233 
MET   C   OXT  sing N N 234 
MET   CB  CG   sing N N 235 
MET   CB  HB2  sing N N 236 
MET   CB  HB3  sing N N 237 
MET   CG  SD   sing N N 238 
MET   CG  HG2  sing N N 239 
MET   CG  HG3  sing N N 240 
MET   SD  CE   sing N N 241 
MET   CE  HE1  sing N N 242 
MET   CE  HE2  sing N N 243 
MET   CE  HE3  sing N N 244 
MET   OXT HXT  sing N N 245 
PHE   N   CA   sing N N 246 
PHE   N   H    sing N N 247 
PHE   N   H2   sing N N 248 
PHE   CA  C    sing N N 249 
PHE   CA  CB   sing N N 250 
PHE   CA  HA   sing N N 251 
PHE   C   O    doub N N 252 
PHE   C   OXT  sing N N 253 
PHE   CB  CG   sing N N 254 
PHE   CB  HB2  sing N N 255 
PHE   CB  HB3  sing N N 256 
PHE   CG  CD1  doub Y N 257 
PHE   CG  CD2  sing Y N 258 
PHE   CD1 CE1  sing Y N 259 
PHE   CD1 HD1  sing N N 260 
PHE   CD2 CE2  doub Y N 261 
PHE   CD2 HD2  sing N N 262 
PHE   CE1 CZ   doub Y N 263 
PHE   CE1 HE1  sing N N 264 
PHE   CE2 CZ   sing Y N 265 
PHE   CE2 HE2  sing N N 266 
PHE   CZ  HZ   sing N N 267 
PHE   OXT HXT  sing N N 268 
PRO   N   CA   sing N N 269 
PRO   N   CD   sing N N 270 
PRO   N   H    sing N N 271 
PRO   CA  C    sing N N 272 
PRO   CA  CB   sing N N 273 
PRO   CA  HA   sing N N 274 
PRO   C   O    doub N N 275 
PRO   C   OXT  sing N N 276 
PRO   CB  CG   sing N N 277 
PRO   CB  HB2  sing N N 278 
PRO   CB  HB3  sing N N 279 
PRO   CG  CD   sing N N 280 
PRO   CG  HG2  sing N N 281 
PRO   CG  HG3  sing N N 282 
PRO   CD  HD2  sing N N 283 
PRO   CD  HD3  sing N N 284 
PRO   OXT HXT  sing N N 285 
SER   N   CA   sing N N 286 
SER   N   H    sing N N 287 
SER   N   H2   sing N N 288 
SER   CA  C    sing N N 289 
SER   CA  CB   sing N N 290 
SER   CA  HA   sing N N 291 
SER   C   O    doub N N 292 
SER   C   OXT  sing N N 293 
SER   CB  OG   sing N N 294 
SER   CB  HB2  sing N N 295 
SER   CB  HB3  sing N N 296 
SER   OG  HG   sing N N 297 
SER   OXT HXT  sing N N 298 
THR   N   CA   sing N N 299 
THR   N   H    sing N N 300 
THR   N   H2   sing N N 301 
THR   CA  C    sing N N 302 
THR   CA  CB   sing N N 303 
THR   CA  HA   sing N N 304 
THR   C   O    doub N N 305 
THR   C   OXT  sing N N 306 
THR   CB  OG1  sing N N 307 
THR   CB  CG2  sing N N 308 
THR   CB  HB   sing N N 309 
THR   OG1 HG1  sing N N 310 
THR   CG2 HG21 sing N N 311 
THR   CG2 HG22 sing N N 312 
THR   CG2 HG23 sing N N 313 
THR   OXT HXT  sing N N 314 
TRP   N   CA   sing N N 315 
TRP   N   H    sing N N 316 
TRP   N   H2   sing N N 317 
TRP   CA  C    sing N N 318 
TRP   CA  CB   sing N N 319 
TRP   CA  HA   sing N N 320 
TRP   C   O    doub N N 321 
TRP   C   OXT  sing N N 322 
TRP   CB  CG   sing N N 323 
TRP   CB  HB2  sing N N 324 
TRP   CB  HB3  sing N N 325 
TRP   CG  CD1  doub Y N 326 
TRP   CG  CD2  sing Y N 327 
TRP   CD1 NE1  sing Y N 328 
TRP   CD1 HD1  sing N N 329 
TRP   CD2 CE2  doub Y N 330 
TRP   CD2 CE3  sing Y N 331 
TRP   NE1 CE2  sing Y N 332 
TRP   NE1 HE1  sing N N 333 
TRP   CE2 CZ2  sing Y N 334 
TRP   CE3 CZ3  doub Y N 335 
TRP   CE3 HE3  sing N N 336 
TRP   CZ2 CH2  doub Y N 337 
TRP   CZ2 HZ2  sing N N 338 
TRP   CZ3 CH2  sing Y N 339 
TRP   CZ3 HZ3  sing N N 340 
TRP   CH2 HH2  sing N N 341 
TRP   OXT HXT  sing N N 342 
TYR   N   CA   sing N N 343 
TYR   N   H    sing N N 344 
TYR   N   H2   sing N N 345 
TYR   CA  C    sing N N 346 
TYR   CA  CB   sing N N 347 
TYR   CA  HA   sing N N 348 
TYR   C   O    doub N N 349 
TYR   C   OXT  sing N N 350 
TYR   CB  CG   sing N N 351 
TYR   CB  HB2  sing N N 352 
TYR   CB  HB3  sing N N 353 
TYR   CG  CD1  doub Y N 354 
TYR   CG  CD2  sing Y N 355 
TYR   CD1 CE1  sing Y N 356 
TYR   CD1 HD1  sing N N 357 
TYR   CD2 CE2  doub Y N 358 
TYR   CD2 HD2  sing N N 359 
TYR   CE1 CZ   doub Y N 360 
TYR   CE1 HE1  sing N N 361 
TYR   CE2 CZ   sing Y N 362 
TYR   CE2 HE2  sing N N 363 
TYR   CZ  OH   sing N N 364 
TYR   OH  HH   sing N N 365 
TYR   OXT HXT  sing N N 366 
VAL   N   CA   sing N N 367 
VAL   N   H    sing N N 368 
VAL   N   H2   sing N N 369 
VAL   CA  C    sing N N 370 
VAL   CA  CB   sing N N 371 
VAL   CA  HA   sing N N 372 
VAL   C   O    doub N N 373 
VAL   C   OXT  sing N N 374 
VAL   CB  CG1  sing N N 375 
VAL   CB  CG2  sing N N 376 
VAL   CB  HB   sing N N 377 
VAL   CG1 HG11 sing N N 378 
VAL   CG1 HG12 sing N N 379 
VAL   CG1 HG13 sing N N 380 
VAL   CG2 HG21 sing N N 381 
VAL   CG2 HG22 sing N N 382 
VAL   CG2 HG23 sing N N 383 
VAL   OXT HXT  sing N N 384 
# 
_pdbx_audit_support.funding_organization   'National Natural Science Foundation of China (NSFC)' 
_pdbx_audit_support.country                China 
_pdbx_audit_support.grant_number           2021YFC2301405 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_deposit_group.group_title         'Crystallographic fragment screening of Human heat shock protein 90' 
_pdbx_deposit_group.group_description   
;Heat shock protein 90 (HSP90) is one of the most active molecular chaperones in cells. It plays a vital role in the cell maturation process and serves as a molecular chaperone involved in many oncogenic proteins folding, assembly and stabilization. Many HSP90 client proteins are kinases or transcription factors involved in signal transduction pathways and are key regulatory factors in tumor growth and maintenance. Therefore, HSP90 inhibitors can be used as drugs for cancer treatment.
;
_pdbx_deposit_group.group_type          'changed state' 
_pdbx_deposit_group.group_id            G_1002298 
# 
_space_group.name_H-M_alt     'I 2 2 2' 
_space_group.name_Hall        'I 2 2' 
_space_group.IT_number        23 
_space_group.crystal_system   orthorhombic 
_space_group.id               1 
# 
_atom_sites.entry_id                    7HAD 
_atom_sites.fract_transf_matrix[1][1]   0.015182 
_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]   0.011182 
_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]   0.010006 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
_atom_type.scat_dispersion_real 
_atom_type.scat_dispersion_imag 
_atom_type.scat_Cromer_Mann_a1 
_atom_type.scat_Cromer_Mann_a2 
_atom_type.scat_Cromer_Mann_a3 
_atom_type.scat_Cromer_Mann_a4 
_atom_type.scat_Cromer_Mann_b1 
_atom_type.scat_Cromer_Mann_b2 
_atom_type.scat_Cromer_Mann_b3 
_atom_type.scat_Cromer_Mann_b4 
_atom_type.scat_Cromer_Mann_c 
_atom_type.scat_source 
_atom_type.scat_dispersion_source 
C ? ? 3.54356 2.42580 ? ? 25.62398 1.50364  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
N ? ? 4.01032 2.96436 ? ? 19.97189 1.75589  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O ? ? 4.49882 3.47563 ? ? 15.80542 1.70748  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
S ? ? 9.55732 6.39887 ? ? 1.23737  29.19336 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N   . GLU   A 1 9   ? 4.50543   -28.82917 -38.96547 1.000 54.96044  ? 16  GLU   A N   1 
ATOM   2    C CA  . GLU   A 1 9   ? 5.59841   -27.88310 -39.16889 1.000 63.63094  ? 16  GLU   A CA  1 
ATOM   3    C C   . GLU   A 1 9   ? 5.79387   -27.01288 -37.92023 1.000 48.47693  ? 16  GLU   A C   1 
ATOM   4    O O   . GLU   A 1 9   ? 5.07936   -26.02712 -37.72317 1.000 51.76722  ? 16  GLU   A O   1 
ATOM   5    C CB  . GLU   A 1 9   ? 5.31927   -27.00465 -40.38600 1.000 70.40502  ? 16  GLU   A CB  1 
ATOM   6    C CG  . GLU   A 1 9   ? 6.32129   -25.87750 -40.60039 1.000 75.85078  ? 16  GLU   A CG  1 
ATOM   7    C CD  . GLU   A 1 9   ? 5.97596   -25.01844 -41.81037 1.000 101.69327 ? 16  GLU   A CD  1 
ATOM   8    O OE1 . GLU   A 1 9   ? 6.02238   -23.77470 -41.68181 1.000 88.97778  ? 16  GLU   A OE1 1 
ATOM   9    O OE2 . GLU   A 1 9   ? 5.64240   -25.58186 -42.87908 1.000 99.99136  ? 16  GLU   A OE2 1 
ATOM   10   N N   . VAL   A 1 10  ? 6.75245   -27.39249 -37.07605 1.000 40.55171  ? 17  VAL   A N   1 
ATOM   11   C CA  . VAL   A 1 10  ? 7.02862   -26.72653 -35.80747 1.000 34.01810  ? 17  VAL   A CA  1 
ATOM   12   C C   . VAL   A 1 10  ? 8.38342   -26.04461 -35.90115 1.000 35.38043  ? 17  VAL   A C   1 
ATOM   13   O O   . VAL   A 1 10  ? 9.37740   -26.68095 -36.25906 1.000 36.42327  ? 17  VAL   A O   1 
ATOM   14   C CB  . VAL   A 1 10  ? 7.01930   -27.72119 -34.63512 1.000 43.43822  ? 17  VAL   A CB  1 
ATOM   15   C CG1 . VAL   A 1 10  ? 7.04907   -26.98661 -33.30455 1.000 36.11766  ? 17  VAL   A CG1 1 
ATOM   16   C CG2 . VAL   A 1 10  ? 5.81659   -28.63169 -34.72824 1.000 50.30752  ? 17  VAL   A CG2 1 
ATOM   17   N N   . GLU   A 1 11  ? 8.42351   -24.76029 -35.59708 1.000 27.42390  ? 18  GLU   A N   1 
ATOM   18   C CA  . GLU   A 1 11  ? 9.67568   -24.01225 -35.53999 1.000 28.57462  ? 18  GLU   A CA  1 
ATOM   19   C C   . GLU   A 1 11  ? 10.09034  -23.83567 -34.08312 1.000 22.84606  ? 18  GLU   A C   1 
ATOM   20   O O   . GLU   A 1 11  ? 9.29335   -23.40863 -33.22937 1.000 22.27599  ? 18  GLU   A O   1 
ATOM   21   C CB  . GLU   A 1 11  ? 9.54034   -22.64332 -36.20237 1.000 27.31975  ? 18  GLU   A CB  1 
ATOM   22   C CG  . GLU   A 1 11  ? 9.34078   -22.73221 -37.68712 1.000 28.27744  ? 18  GLU   A CG  1 
ATOM   23   C CD  . GLU   A 1 11  ? 9.07887   -21.38884 -38.32616 1.000 39.47685  ? 18  GLU   A CD  1 
ATOM   24   O OE1 . GLU   A 1 11  ? 8.00936   -20.79953 -38.07983 1.000 41.94643  ? 18  GLU   A OE1 1 
ATOM   25   O OE2 . GLU   A 1 11  ? 9.93124   -20.95257 -39.12989 1.000 40.86231  ? 18  GLU   A OE2 1 
ATOM   26   N N   . THR   A 1 12  ? 11.35916  -24.11934 -33.80305 1.000 24.88323  ? 19  THR   A N   1 
ATOM   27   C CA  . THR   A 1 12  ? 11.90030  -23.99778 -32.46413 1.000 20.19849  ? 19  THR   A CA  1 
ATOM   28   C C   . THR   A 1 12  ? 12.90064  -22.85032 -32.41880 1.000 22.58583  ? 19  THR   A C   1 
ATOM   29   O O   . THR   A 1 12  ? 13.78212  -22.76224 -33.28106 1.000 21.57589  ? 19  THR   A O   1 
ATOM   30   C CB  . THR   A 1 12  ? 12.56989  -25.30100 -32.02798 1.000 21.69098  ? 19  THR   A CB  1 
ATOM   31   O OG1 . THR   A 1 12  ? 11.65204  -26.39724 -32.14414 1.000 24.98602  ? 19  THR   A OG1 1 
ATOM   32   C CG2 . THR   A 1 12  ? 13.09958  -25.17681 -30.57779 1.000 21.00432  ? 19  THR   A CG2 1 
ATOM   33   N N   . PHE   A 1 13  ? 12.76268  -21.99222 -31.41568 1.000 20.38377  ? 20  PHE   A N   1 
ATOM   34   C CA  . PHE   A 1 13  ? 13.54444  -20.77129 -31.27609 1.000 22.64317  ? 20  PHE   A CA  1 
ATOM   35   C C   . PHE   A 1 13  ? 14.22992  -20.75484 -29.92064 1.000 23.93423  ? 20  PHE   A C   1 
ATOM   36   O O   . PHE   A 1 13  ? 13.68958  -21.24799 -28.92477 1.000 22.20160  ? 20  PHE   A O   1 
ATOM   37   C CB  . PHE   A 1 13  ? 12.66250  -19.51385 -31.36728 1.000 21.57286  ? 20  PHE   A CB  1 
ATOM   38   C CG  . PHE   A 1 13  ? 11.92308  -19.36451 -32.65238 1.000 23.05181  ? 20  PHE   A CG  1 
ATOM   39   C CD1 . PHE   A 1 13  ? 10.69036  -20.00102 -32.87068 1.000 23.50552  ? 20  PHE   A CD1 1 
ATOM   40   C CD2 . PHE   A 1 13  ? 12.44656  -18.55079 -33.65245 1.000 25.19277  ? 20  PHE   A CD2 1 
ATOM   41   C CE1 . PHE   A 1 13  ? 10.01365  -19.83656 -34.09281 1.000 26.65554  ? 20  PHE   A CE1 1 
ATOM   42   C CE2 . PHE   A 1 13  ? 11.76583  -18.37048 -34.87614 1.000 28.69559  ? 20  PHE   A CE2 1 
ATOM   43   C CZ  . PHE   A 1 13  ? 10.54681  -19.01933 -35.08802 1.000 28.55031  ? 20  PHE   A CZ  1 
ATOM   44   N N   . ALA   A 1 14  ? 15.42896  -20.17573 -29.86831 1.000 20.31309  ? 21  ALA   A N   1 
ATOM   45   C CA  . ALA   A 1 14  ? 16.04775  -19.85857 -28.57903 1.000 19.59641  ? 21  ALA   A CA  1 
ATOM   46   C C   . ALA   A 1 14  ? 15.53117  -18.53807 -28.01648 1.000 18.80582  ? 21  ALA   A C   1 
ATOM   47   O O   . ALA   A 1 14  ? 15.45192  -17.52501 -28.71407 1.000 21.77946  ? 21  ALA   A O   1 
ATOM   48   C CB  . ALA   A 1 14  ? 17.56691  -19.75799 -28.73221 1.000 20.79430  ? 21  ALA   A CB  1 
ATOM   49   N N   . PHE   A 1 15  ? 15.22106  -18.52674 -26.71178 1.000 19.03740  ? 22  PHE   A N   1 
ATOM   50   C CA  . PHE   A 1 15  ? 15.02630  -17.22896 -26.08112 1.000 19.49981  ? 22  PHE   A CA  1 
ATOM   51   C C   . PHE   A 1 15  ? 16.31719  -16.42345 -26.13338 1.000 19.11132  ? 22  PHE   A C   1 
ATOM   52   O O   . PHE   A 1 15  ? 17.42835  -16.97570 -26.01207 1.000 22.54422  ? 22  PHE   A O   1 
ATOM   53   C CB  . PHE   A 1 15  ? 14.64572  -17.38908 -24.59629 1.000 19.21836  ? 22  PHE   A CB  1 
ATOM   54   C CG  . PHE   A 1 15  ? 13.23554  -17.92026 -24.36721 1.000 17.94294  ? 22  PHE   A CG  1 
ATOM   55   C CD1 . PHE   A 1 15  ? 12.10715  -17.13170 -24.66589 1.000 18.68534  ? 22  PHE   A CD1 1 
ATOM   56   C CD2 . PHE   A 1 15  ? 13.04954  -19.20219 -23.82133 1.000 18.72009  ? 22  PHE   A CD2 1 
ATOM   57   C CE1 . PHE   A 1 15  ? 10.80940  -17.60106 -24.42309 1.000 19.15101  ? 22  PHE   A CE1 1 
ATOM   58   C CE2 . PHE   A 1 15  ? 11.74444  -19.69349 -23.60184 1.000 18.68915  ? 22  PHE   A CE2 1 
ATOM   59   C CZ  . PHE   A 1 15  ? 10.63170  -18.89127 -23.89231 1.000 16.47211  ? 22  PHE   A CZ  1 
ATOM   60   N N   . GLN   A 1 16  ? 16.15683  -15.10156 -26.25014 1.000 20.29325  ? 23  GLN   A N   1 
ATOM   61   C CA  . GLN   A 1 16  ? 17.26296  -14.20834 -25.94459 1.000 22.53433  ? 23  GLN   A CA  1 
ATOM   62   C C   . GLN   A 1 16  ? 17.77840  -14.51863 -24.54993 1.000 20.16292  ? 23  GLN   A C   1 
ATOM   63   O O   . GLN   A 1 16  ? 17.01299  -14.89450 -23.65567 1.000 22.78389  ? 23  GLN   A O   1 
ATOM   64   C CB  . GLN   A 1 16  ? 16.84313  -12.74090 -26.02976 1.000 24.45086  ? 23  GLN   A CB  1 
ATOM   65   C CG  . GLN   A 1 16  ? 16.54639  -12.27068 -27.42902 1.000 28.04948  ? 23  GLN   A CG  1 
ATOM   66   C CD  . GLN   A 1 16  ? 15.91509  -10.90577 -27.42090 1.000 39.13762  ? 23  GLN   A CD  1 
ATOM   67   O OE1 . GLN   A 1 16  ? 14.75151  -10.78567 -27.11474 1.000 39.46955  ? 23  GLN   A OE1 1 
ATOM   68   N NE2 . GLN   A 1 16  ? 16.69816  -9.86069  -27.71523 1.000 37.80553  ? 23  GLN   A NE2 1 
ATOM   69   N N   . ALA   A 1 17  ? 19.09298  -14.38549 -24.39024 1.000 24.12974  ? 24  ALA   A N   1 
ATOM   70   C CA  . ALA   A 1 17  ? 19.73071  -14.78419 -23.13964 1.000 24.90783  ? 24  ALA   A CA  1 
ATOM   71   C C   . ALA   A 1 17  ? 19.09374  -14.09855 -21.94435 1.000 23.20540  ? 24  ALA   A C   1 
ATOM   72   O O   . ALA   A 1 17  ? 18.88372  -14.72252 -20.90155 1.000 24.29010  ? 24  ALA   A O   1 
ATOM   73   C CB  . ALA   A 1 17  ? 21.22650  -14.46198 -23.20664 1.000 26.68403  ? 24  ALA   A CB  1 
ATOM   74   N N   . GLU   A 1 18  ? 18.74904  -12.82184 -22.09167 1.000 25.68201  ? 25  GLU   A N   1 
ATOM   75   C CA  . GLU   A 1 18  ? 18.17318  -12.08111 -20.97181 1.000 24.88017  ? 25  GLU   A CA  1 
ATOM   76   C C   . GLU   A 1 18  ? 16.80254  -12.62885 -20.58107 1.000 24.45439  ? 25  GLU   A C   1 
ATOM   77   O O   . GLU   A 1 18  ? 16.43102  -12.62461 -19.39493 1.000 24.50416  ? 25  GLU   A O   1 
ATOM   78   C CB  . GLU   A 1 18  ? 18.09504  -10.59891 -21.33657 1.000 31.21177  ? 25  GLU   A CB  1 
ATOM   79   C CG  . GLU   A 1 18  ? 19.46438  -9.93384  -21.55372 1.000 35.34762  ? 25  GLU   A CG  1 
ATOM   80   C CD  . GLU   A 1 18  ? 20.05011  -10.11495 -22.95716 1.000 41.59677  ? 25  GLU   A CD  1 
ATOM   81   O OE1 . GLU   A 1 18  ? 19.51384  -10.89811 -23.78076 1.000 35.41301  ? 25  GLU   A OE1 1 
ATOM   82   O OE2 . GLU   A 1 18  ? 21.08379  -9.47032  -23.24736 1.000 51.20936  ? 25  GLU   A OE2 1 
ATOM   83   N N   . ILE   A 1 19  ? 16.01576  -13.08163 -21.56339 1.000 22.14393  ? 26  ILE   A N   1 
ATOM   84   C CA  . ILE   A 1 19  ? 14.69035  -13.61088 -21.23740 1.000 21.24511  ? 26  ILE   A CA  1 
ATOM   85   C C   . ILE   A 1 19  ? 14.82373  -14.99462 -20.59568 1.000 19.70727  ? 26  ILE   A C   1 
ATOM   86   O O   . ILE   A 1 19  ? 14.09731  -15.33278 -19.64554 1.000 22.04240  ? 26  ILE   A O   1 
ATOM   87   C CB  . ILE   A 1 19  ? 13.78117  -13.64089 -22.49274 1.000 20.30181  ? 26  ILE   A CB  1 
ATOM   88   C CG1 . ILE   A 1 19  ? 13.26046  -12.24444 -22.86629 1.000 26.74233  ? 26  ILE   A CG1 1 
ATOM   89   C CG2 . ILE   A 1 19  ? 12.49382  -14.48649 -22.20512 1.000 20.02854  ? 26  ILE   A CG2 1 
ATOM   90   C CD1 . ILE   A 1 19  ? 14.29243  -11.18959 -23.16688 1.000 37.36271  ? 26  ILE   A CD1 1 
ATOM   91   N N   . ALA   A 1 20  ? 15.77620  -15.80177 -21.07392 1.000 19.54628  ? 27  ALA   A N   1 
ATOM   92   C CA  . ALA   A 1 20  ? 16.02086  -17.08510 -20.42781 1.000 21.25899  ? 27  ALA   A CA  1 
ATOM   93   C C   . ALA   A 1 20  ? 16.42412  -16.86020 -18.97363 1.000 22.52551  ? 27  ALA   A C   1 
ATOM   94   O O   . ALA   A 1 20  ? 15.98685  -17.60194 -18.08154 1.000 25.37933  ? 27  ALA   A O   1 
ATOM   95   C CB  . ALA   A 1 20  ? 17.11535  -17.86965 -21.16091 1.000 22.96914  ? 27  ALA   A CB  1 
ATOM   96   N N   . GLN   A 1 21  ? 17.24553  -15.83387 -18.72325 1.000 22.62565  ? 28  GLN   A N   1 
ATOM   97   C CA  . GLN   A 1 21  ? 17.65830  -15.55496 -17.34360 1.000 22.89801  ? 28  GLN   A CA  1 
ATOM   98   C C   . GLN   A 1 21  ? 16.47915  -15.12925 -16.49208 1.000 27.66602  ? 28  GLN   A C   1 
ATOM   99   O O   . GLN   A 1 21  ? 16.37331  -15.55284 -15.33579 1.000 28.50908  ? 28  GLN   A O   1 
ATOM   100  C CB  . GLN   A 1 21  ? 18.74637  -14.47994 -17.28536 1.000 27.83567  ? 28  GLN   A CB  1 
ATOM   101  C CG  . GLN   A 1 21  ? 20.04723  -14.73173 -18.05605 1.000 47.02982  ? 28  GLN   A CG  1 
ATOM   102  C CD  . GLN   A 1 21  ? 20.78313  -13.44846 -18.48709 1.000 59.46567  ? 28  GLN   A CD  1 
ATOM   103  O OE1 . GLN   A 1 21  ? 21.56130  -13.46202 -19.44719 1.000 54.56632  ? 28  GLN   A OE1 1 
ATOM   104  N NE2 . GLN   A 1 21  ? 20.58152  -12.35596 -17.73958 1.000 50.63461  ? 28  GLN   A NE2 1 
ATOM   105  N N   . LEU   A 1 22  ? 15.59841  -14.28560 -17.04337 1.000 23.01532  ? 29  LEU   A N   1 
ATOM   106  C CA  . LEU   A 1 22  ? 14.38126  -13.88837 -16.32932 1.000 25.15543  ? 29  LEU   A CA  1 
ATOM   107  C C   . LEU   A 1 22  ? 13.51445  -15.09502 -15.99054 1.000 27.21839  ? 29  LEU   A C   1 
ATOM   108  O O   . LEU   A 1 22  ? 13.03451  -15.23923 -14.85500 1.000 25.44628  ? 29  LEU   A O   1 
ATOM   109  C CB  . LEU   A 1 22  ? 13.58594  -12.88148 -17.17047 1.000 26.55087  ? 29  LEU   A CB  1 
ATOM   110  C CG  . LEU   A 1 22  ? 12.18728  -12.55874 -16.64784 1.000 29.60452  ? 29  LEU   A CG  1 
ATOM   111  C CD1 . LEU   A 1 22  ? 12.35010  -11.78122 -15.34065 1.000 31.21164  ? 29  LEU   A CD1 1 
ATOM   112  C CD2 . LEU   A 1 22  ? 11.42645  -11.74992 -17.69036 1.000 29.33551  ? 29  LEU   A CD2 1 
ATOM   113  N N   . MET   A 1 23  ? 13.30122  -15.98667 -16.96682 1.000 22.28350  ? 30  MET   A N   1 
ATOM   114  C CA  . MET   A 1 23  ? 12.50537  -17.17271 -16.67452 1.000 20.61626  ? 30  MET   A CA  1 
ATOM   115  C C   . MET   A 1 23  ? 13.15849  -18.06639 -15.62208 1.000 24.22041  ? 30  MET   A C   1 
ATOM   116  O O   . MET   A 1 23  ? 12.46000  -18.59758 -14.74810 1.000 23.48794  ? 30  MET   A O   1 
ATOM   117  C CB  . MET   A 1 23  ? 12.14270  -17.96549 -17.94357 1.000 20.14167  ? 30  MET   A CB  1 
ATOM   118  C CG  . MET   A 1 23  ? 11.31686  -17.14562 -18.93614 1.000 19.58626  ? 30  MET   A CG  1 
ATOM   119  S SD  . MET   A 1 23  ? 11.25848  -17.91678 -20.57349 1.000 20.55183  ? 30  MET   A SD  1 
ATOM   120  C CE  . MET   A 1 23  ? 10.15875  -19.30106 -20.23822 1.000 22.05977  ? 30  MET   A CE  1 
ATOM   121  N N   . SER   A 1 24  ? 14.48295  -18.22599 -15.66500 1.000 22.37915  ? 31  SER   A N   1 
ATOM   122  C CA  . SER   A 1 24  ? 15.18120  -19.01376 -14.65065 1.000 24.71349  ? 31  SER   A CA  1 
ATOM   123  C C   . SER   A 1 24  ? 14.97914  -18.42099 -13.26934 1.000 29.15504  ? 31  SER   A C   1 
ATOM   124  O O   . SER   A 1 24  ? 14.73923  -19.14837 -12.29448 1.000 30.17195  ? 31  SER   A O   1 
ATOM   125  C CB  . SER   A 1 24  ? 16.66985  -19.09458 -14.99848 1.000 33.73832  ? 31  SER   A CB  1 
ATOM   126  O OG  . SER   A 1 24  ? 17.27733  -20.23293 -14.39542 1.000 55.37864  ? 31  SER   A OG  1 
ATOM   127  N N   . LEU   A 1 25  ? 15.07251  -17.09650 -13.16705 1.000 26.93965  ? 32  LEU   A N   1 
ATOM   128  C CA  . LEU   A 1 25  ? 14.87616  -16.43567 -11.87866 1.000 26.59165  ? 32  LEU   A CA  1 
ATOM   129  C C   . LEU   A 1 25  ? 13.46177  -16.66449 -11.34959 1.000 29.47161  ? 32  LEU   A C   1 
ATOM   130  O O   . LEU   A 1 25  ? 13.25136  -16.88742 -10.15092 1.000 30.70388  ? 32  LEU   A O   1 
ATOM   131  C CB  . LEU   A 1 25  ? 15.16833  -14.94762 -12.04787 1.000 31.80928  ? 32  LEU   A CB  1 
ATOM   132  C CG  . LEU   A 1 25  ? 15.10717  -14.03546 -10.81754 1.000 43.12280  ? 32  LEU   A CG  1 
ATOM   133  C CD1 . LEU   A 1 25  ? 16.06172  -12.86619 -11.00728 1.000 45.16952  ? 32  LEU   A CD1 1 
ATOM   134  C CD2 . LEU   A 1 25  ? 13.69884  -13.53088 -10.57339 1.000 43.57586  ? 32  LEU   A CD2 1 
ATOM   135  N N   . ILE   A 1 26  ? 12.47857  -16.59082 -12.22856 1.000 23.58582  ? 33  ILE   A N   1 
ATOM   136  C CA  . ILE   A 1 26  ? 11.09651  -16.76925 -11.80675 1.000 26.38864  ? 33  ILE   A CA  1 
ATOM   137  C C   . ILE   A 1 26  ? 10.86736  -18.19634 -11.32521 1.000 27.05907  ? 33  ILE   A C   1 
ATOM   138  O O   . ILE   A 1 26  ? 10.15420  -18.43626 -10.33040 1.000 27.35291  ? 33  ILE   A O   1 
ATOM   139  C CB  . ILE   A 1 26  ? 10.15419  -16.38311 -12.95993 1.000 22.96001  ? 33  ILE   A CB  1 
ATOM   140  C CG1 . ILE   A 1 26  ? 10.15883  -14.85753 -13.14603 1.000 25.27579  ? 33  ILE   A CG1 1 
ATOM   141  C CG2 . ILE   A 1 26  ? 8.74906   -16.96022 -12.72846 1.000 22.90047  ? 33  ILE   A CG2 1 
ATOM   142  C CD1 . ILE   A 1 26  ? 9.47780   -14.38654 -14.45185 1.000 26.40573  ? 33  ILE   A CD1 1 
ATOM   143  N N   . ILE   A 1 27  ? 11.49755  -19.16144 -11.98725 1.000 25.53034  ? 34  ILE   A N   1 
ATOM   144  C CA  . ILE   A 1 27  ? 11.28887  -20.56432 -11.65943 1.000 25.84942  ? 34  ILE   A CA  1 
ATOM   145  C C   . ILE   A 1 27  ? 12.05278  -20.95837 -10.39659 1.000 29.52004  ? 34  ILE   A C   1 
ATOM   146  O O   . ILE   A 1 27  ? 11.55909  -21.75548 -9.59877  1.000 33.66406  ? 34  ILE   A O   1 
ATOM   147  C CB  . ILE   A 1 27  ? 11.66467  -21.43916 -12.87734 1.000 26.80306  ? 34  ILE   A CB  1 
ATOM   148  C CG1 . ILE   A 1 27  ? 10.61313  -21.25916 -13.97663 1.000 25.34171  ? 34  ILE   A CG1 1 
ATOM   149  C CG2 . ILE   A 1 27  ? 11.78478  -22.91699 -12.49054 1.000 29.54460  ? 34  ILE   A CG2 1 
ATOM   150  C CD1 . ILE   A 1 27  ? 11.12615  -21.65866 -15.35926 1.000 26.86502  ? 34  ILE   A CD1 1 
ATOM   151  N N   . ASN   A 1 28  ? 13.26134  -20.41425 -10.18030 1.000 29.90240  ? 35  ASN   A N   1 
ATOM   152  C CA  . ASN   A 1 28  ? 14.11680  -20.89901 -9.10551  1.000 35.13419  ? 35  ASN   A CA  1 
ATOM   153  C C   . ASN   A 1 28  ? 14.10908  -20.04275 -7.85175  1.000 34.62084  ? 35  ASN   A C   1 
ATOM   154  O O   . ASN   A 1 28  ? 14.53802  -20.53339 -6.80059  1.000 40.80396  ? 35  ASN   A O   1 
ATOM   155  C CB  . ASN   A 1 28  ? 15.55901  -21.03287 -9.60912  1.000 38.31949  ? 35  ASN   A CB  1 
ATOM   156  C CG  . ASN   A 1 28  ? 15.66275  -22.01040 -10.73969 1.000 43.75099  ? 35  ASN   A CG  1 
ATOM   157  O OD1 . ASN   A 1 28  ? 15.05536  -23.08435 -10.69000 1.000 44.62303  ? 35  ASN   A OD1 1 
ATOM   158  N ND2 . ASN   A 1 28  ? 16.39386  -21.64051 -11.78862 1.000 56.48592  ? 35  ASN   A ND2 1 
ATOM   159  N N   . THR   A 1 29  ? 13.63966  -18.79762 -7.90808  1.000 30.80935  ? 36  THR   A N   1 
ATOM   160  C CA  . THR   A 1 29  ? 13.66536  -17.96523 -6.69905  1.000 31.31294  ? 36  THR   A CA  1 
ATOM   161  C C   . THR   A 1 29  ? 12.58392  -18.38690 -5.71594  1.000 29.87474  ? 36  THR   A C   1 
ATOM   162  O O   . THR   A 1 29  ? 11.41743  -18.54833 -6.10269  1.000 29.87992  ? 36  THR   A O   1 
ATOM   163  C CB  . THR   A 1 29  ? 13.48221  -16.49188 -7.06613  1.000 37.27035  ? 36  THR   A CB  1 
ATOM   164  O OG1 . THR   A 1 29  ? 14.55887  -16.08637 -7.91928  1.000 37.37981  ? 36  THR   A OG1 1 
ATOM   165  C CG2 . THR   A 1 29  ? 13.48180  -15.61118 -5.82172  1.000 38.62323  ? 36  THR   A CG2 1 
ATOM   166  N N   . PHE   A 1 30  ? 12.96221  -18.54682 -4.43910  1.000 33.05164  ? 37  PHE   A N   1 
ATOM   167  C CA  . PHE   A 1 30  ? 11.94800  -18.81748 -3.43201  1.000 32.85034  ? 37  PHE   A CA  1 
ATOM   168  C C   . PHE   A 1 30  ? 11.08613  -17.56823 -3.23785  1.000 33.63852  ? 37  PHE   A C   1 
ATOM   169  O O   . PHE   A 1 30  ? 11.59148  -16.50057 -2.86811  1.000 34.64824  ? 37  PHE   A O   1 
ATOM   170  C CB  . PHE   A 1 30  ? 12.57199  -19.26526 -2.10987  1.000 32.05710  ? 37  PHE   A CB  1 
ATOM   171  C CG  . PHE   A 1 30  ? 11.54954  -19.51554 -1.05609  1.000 32.44256  ? 37  PHE   A CG  1 
ATOM   172  C CD1 . PHE   A 1 30  ? 10.73352  -20.62961 -1.13490  1.000 37.05232  ? 37  PHE   A CD1 1 
ATOM   173  C CD2 . PHE   A 1 30  ? 11.37118  -18.64036 0.02056   1.000 34.37780  ? 37  PHE   A CD2 1 
ATOM   174  C CE1 . PHE   A 1 30  ? 9.74706   -20.87067 -0.18126  1.000 34.31580  ? 37  PHE   A CE1 1 
ATOM   175  C CE2 . PHE   A 1 30  ? 10.37811  -18.87615 0.97861   1.000 41.84789  ? 37  PHE   A CE2 1 
ATOM   176  C CZ  . PHE   A 1 30  ? 9.57383   -19.99285 0.89058   1.000 33.74530  ? 37  PHE   A CZ  1 
ATOM   177  N N   . TYR   A 1 31  ? 9.78330   -17.70819 -3.45681  1.000 27.93042  ? 38  TYR   A N   1 
ATOM   178  C CA  . TYR   A 1 31  ? 8.87657   -16.56191 -3.42727  1.000 25.89634  ? 38  TYR   A CA  1 
ATOM   179  C C   . TYR   A 1 31  ? 7.45100   -17.09212 -3.27323  1.000 25.67935  ? 38  TYR   A C   1 
ATOM   180  O O   . TYR   A 1 31  ? 6.90175   -17.67595 -4.20833  1.000 26.97829  ? 38  TYR   A O   1 
ATOM   181  C CB  . TYR   A 1 31  ? 9.04530   -15.73300 -4.71096  1.000 30.22617  ? 38  TYR   A CB  1 
ATOM   182  C CG  . TYR   A 1 31  ? 8.06125   -14.60755 -4.81789  1.000 26.98254  ? 38  TYR   A CG  1 
ATOM   183  C CD1 . TYR   A 1 31  ? 8.23550   -13.45157 -4.07487  1.000 33.31533  ? 38  TYR   A CD1 1 
ATOM   184  C CD2 . TYR   A 1 31  ? 6.97130   -14.67987 -5.69757  1.000 35.40708  ? 38  TYR   A CD2 1 
ATOM   185  C CE1 . TYR   A 1 31  ? 7.33003   -12.41075 -4.15158  1.000 40.09904  ? 38  TYR   A CE1 1 
ATOM   186  C CE2 . TYR   A 1 31  ? 6.05839   -13.62911 -5.77506  1.000 31.62837  ? 38  TYR   A CE2 1 
ATOM   187  C CZ  . TYR   A 1 31  ? 6.26478   -12.50318 -5.00540  1.000 38.56525  ? 38  TYR   A CZ  1 
ATOM   188  O OH  . TYR   A 1 31  ? 5.38437   -11.45485 -5.07710  1.000 56.93598  ? 38  TYR   A OH  1 
ATOM   189  N N   . SER   A 1 32  ? 6.83889   -16.87418 -2.11414  1.000 26.28802  ? 39  SER   A N   1 
ATOM   190  C CA  . SER   A 1 32  ? 5.58602   -17.55318 -1.82172  1.000 25.56757  ? 39  SER   A CA  1 
ATOM   191  C C   . SER   A 1 32  ? 4.37582   -16.90792 -2.48519  1.000 25.05818  ? 39  SER   A C   1 
ATOM   192  O O   . SER   A 1 32  ? 3.37281   -17.59060 -2.66888  1.000 28.23713  ? 39  SER   A O   1 
ATOM   193  C CB  . SER   A 1 32  ? 5.36420   -17.62071 -0.31192  1.000 27.89932  ? 39  SER   A CB  1 
ATOM   194  O OG  . SER   A 1 32  ? 6.42867   -18.34643 0.28659   1.000 30.39496  ? 39  SER   A OG  1 
ATOM   195  N N   . ASN   A 1 33  ? 4.45191   -15.62733 -2.85700  1.000 25.92764  ? 40  ASN   A N   1 
ATOM   196  C CA  . ASN   A 1 33  ? 3.27037   -14.86206 -3.27738  1.000 25.81958  ? 40  ASN   A CA  1 
ATOM   197  C C   . ASN   A 1 33  ? 2.98758   -15.09112 -4.76388  1.000 23.79336  ? 40  ASN   A C   1 
ATOM   198  O O   . ASN   A 1 33  ? 2.93048   -14.15784 -5.56624  1.000 25.13190  ? 40  ASN   A O   1 
ATOM   199  C CB  . ASN   A 1 33  ? 3.50931   -13.38736 -2.96481  1.000 28.59283  ? 40  ASN   A CB  1 
ATOM   200  C CG  . ASN   A 1 33  ? 2.33356   -12.47785 -3.32408  1.000 27.98415  ? 40  ASN   A CG  1 
ATOM   201  O OD1 . ASN   A 1 33  ? 1.17420   -12.85994 -3.20992  1.000 28.86943  ? 40  ASN   A OD1 1 
ATOM   202  N ND2 . ASN   A 1 33  ? 2.64877   -11.23786 -3.70446  1.000 29.17403  ? 40  ASN   A ND2 1 
ATOM   203  N N   . LYS   A 1 34  ? 2.80112   -16.36927 -5.11826  1.000 22.92921  ? 41  LYS   A N   1 
ATOM   204  C CA  . LYS   A 1 34  ? 2.67801   -16.74041 -6.52615  1.000 20.57220  ? 41  LYS   A CA  1 
ATOM   205  C C   . LYS   A 1 34  ? 1.38534   -16.25400 -7.16260  1.000 22.08206  ? 41  LYS   A C   1 
ATOM   206  O O   . LYS   A 1 34  ? 1.33328   -16.14836 -8.39582  1.000 22.37619  ? 41  LYS   A O   1 
ATOM   207  C CB  . LYS   A 1 34  ? 2.74675   -18.25716 -6.67427  1.000 22.33779  ? 41  LYS   A CB  1 
ATOM   208  C CG  . LYS   A 1 34  ? 4.09691   -18.88482 -6.35516  1.000 20.79827  ? 41  LYS   A CG  1 
ATOM   209  C CD  . LYS   A 1 34  ? 4.00848   -20.41502 -6.49168  1.000 25.35344  ? 41  LYS   A CD  1 
ATOM   210  C CE  . LYS   A 1 34  ? 5.36414   -21.10856 -6.26799  1.000 24.80553  ? 41  LYS   A CE  1 
ATOM   211  N NZ  . LYS   A 1 34  ? 6.37515   -20.89030 -7.34797  1.000 26.13599  ? 41  LYS   A NZ  1 
ATOM   212  N N   . GLU   A 1 35  ? 0.35838   -15.94296 -6.36661  1.000 22.01677  ? 42  GLU   A N   1 
ATOM   213  C CA  . GLU   A 1 35  ? -0.96270  -15.66505 -6.92243  1.000 21.55467  ? 42  GLU   A CA  1 
ATOM   214  C C   . GLU   A 1 35  ? -0.97258  -14.45950 -7.86347  1.000 23.32014  ? 42  GLU   A C   1 
ATOM   215  O O   . GLU   A 1 35  ? -1.94065  -14.27708 -8.60665  1.000 23.34697  ? 42  GLU   A O   1 
ATOM   216  C CB  . GLU   A 1 35  ? -1.96764  -15.47259 -5.77724  1.000 25.21340  ? 42  GLU   A CB  1 
ATOM   217  C CG  . GLU   A 1 35  ? -1.85384  -14.16464 -5.02185  1.000 24.45304  ? 42  GLU   A CG  1 
ATOM   218  C CD  . GLU   A 1 35  ? -2.73854  -14.10638 -3.75640  1.000 30.75021  ? 42  GLU   A CD  1 
ATOM   219  O OE1 . GLU   A 1 35  ? -2.88610  -15.13914 -3.08830  1.000 40.66071  ? 42  GLU   A OE1 1 
ATOM   220  O OE2 . GLU   A 1 35  ? -3.23819  -13.02334 -3.42985  1.000 46.38939  ? 42  GLU   A OE2 1 
ATOM   221  N N   . ILE   A 1 36  ? 0.04294   -13.59422 -7.80208  1.000 22.40587  ? 43  ILE   A N   1 
ATOM   222  C CA  . ILE   A 1 36  ? 0.04624   -12.40881 -8.63157  1.000 21.25495  ? 43  ILE   A CA  1 
ATOM   223  C C   . ILE   A 1 36  ? 0.15085   -12.74394 -10.10695 1.000 20.09417  ? 43  ILE   A C   1 
ATOM   224  O O   . ILE   A 1 36  ? -0.10519  -11.85382 -10.93401 1.000 20.78055  ? 43  ILE   A O   1 
ATOM   225  C CB  . ILE   A 1 36  ? 1.17879   -11.44206 -8.21595  1.000 24.13792  ? 43  ILE   A CB  1 
ATOM   226  C CG1 . ILE   A 1 36  ? 2.53717   -12.12746 -8.35394  1.000 28.33144  ? 43  ILE   A CG1 1 
ATOM   227  C CG2 . ILE   A 1 36  ? 0.95850   -10.93269 -6.77489  1.000 27.12796  ? 43  ILE   A CG2 1 
ATOM   228  C CD1 . ILE   A 1 36  ? 3.21684   -11.86340 -9.68226  1.000 30.73859  ? 43  ILE   A CD1 1 
ATOM   229  N N   . PHE   A 1 37  ? 0.48985   -13.99739 -10.47123 1.000 19.18153  ? 44  PHE   A N   1 
ATOM   230  C CA  . PHE   A 1 37  ? 0.50733   -14.31282 -11.90168 1.000 19.68900  ? 44  PHE   A CA  1 
ATOM   231  C C   . PHE   A 1 37  ? -0.83548  -13.98070 -12.54756 1.000 20.13788  ? 44  PHE   A C   1 
ATOM   232  O O   . PHE   A 1 37  ? -0.87787  -13.55712 -13.71326 1.000 19.39703  ? 44  PHE   A O   1 
ATOM   233  C CB  . PHE   A 1 37  ? 0.83228   -15.79994 -12.16298 1.000 19.74365  ? 44  PHE   A CB  1 
ATOM   234  C CG  . PHE   A 1 37  ? -0.36556  -16.71033 -11.93653 1.000 18.46698  ? 44  PHE   A CG  1 
ATOM   235  C CD1 . PHE   A 1 37  ? -0.66802  -17.18433 -10.67224 1.000 20.34561  ? 44  PHE   A CD1 1 
ATOM   236  C CD2 . PHE   A 1 37  ? -1.24214  -17.03697 -13.00525 1.000 19.95277  ? 44  PHE   A CD2 1 
ATOM   237  C CE1 . PHE   A 1 37  ? -1.80776  -17.99274 -10.46096 1.000 19.03100  ? 44  PHE   A CE1 1 
ATOM   238  C CE2 . PHE   A 1 37  ? -2.38435  -17.81438 -12.80483 1.000 19.81039  ? 44  PHE   A CE2 1 
ATOM   239  C CZ  . PHE   A 1 37  ? -2.67519  -18.31002 -11.52618 1.000 20.77587  ? 44  PHE   A CZ  1 
ATOM   240  N N   . LEU   A 1 38  ? -1.94765  -14.16415 -11.82210 1.000 18.71106  ? 45  LEU   A N   1 
ATOM   241  C CA  . LEU   A 1 38  ? -3.23110  -14.05003 -12.50209 1.000 17.71637  ? 45  LEU   A CA  1 
ATOM   242  C C   . LEU   A 1 38  ? -3.53800  -12.59459 -12.80856 1.000 19.72471  ? 45  LEU   A C   1 
ATOM   243  O O   . LEU   A 1 38  ? -4.03282  -12.27349 -13.91085 1.000 19.90576  ? 45  LEU   A O   1 
ATOM   244  C CB  . LEU   A 1 38  ? -4.32993  -14.67235 -11.65652 1.000 17.91186  ? 45  LEU   A CB  1 
ATOM   245  C CG  . LEU   A 1 38  ? -5.72900  -14.70914 -12.28259 1.000 18.32696  ? 45  LEU   A CG  1 
ATOM   246  C CD1 . LEU   A 1 38  ? -5.66496  -15.48696 -13.58636 1.000 19.48739  ? 45  LEU   A CD1 1 
ATOM   247  C CD2 . LEU   A 1 38  ? -6.73647  -15.34191 -11.37189 1.000 23.55088  ? 45  LEU   A CD2 1 
ATOM   248  N N   . ARG   A 1 39  ? -3.24876  -11.69946 -11.84567 1.000 19.90904  ? 46  ARG   A N   1 
ATOM   249  C CA  . ARG   A 1 39  ? -3.40112  -10.27040 -12.08244 1.000 20.10094  ? 46  ARG   A CA  1 
ATOM   250  C C   . ARG   A 1 39  ? -2.58084  -9.84276  -13.29577 1.000 21.26966  ? 46  ARG   A C   1 
ATOM   251  O O   . ARG   A 1 39  ? -3.02454  -9.00480  -14.09601 1.000 21.67536  ? 46  ARG   A O   1 
ATOM   252  C CB  . ARG   A 1 39  ? -2.99520  -9.48890  -10.83778 1.000 24.64778  ? 46  ARG   A CB  1 
ATOM   253  C CG  . ARG   A 1 39  ? -2.63917  -8.04367  -11.06649 1.000 37.12453  ? 46  ARG   A CG  1 
ATOM   254  C CD  . ARG   A 1 39  ? -1.98712  -7.43803  -9.82703  1.000 39.41596  ? 46  ARG   A CD  1 
ATOM   255  N NE  . ARG   A 1 39  ? -0.55644  -7.72786  -9.74905  1.000 43.28640  ? 46  ARG   A NE  1 
ATOM   256  C CZ  . ARG   A 1 39  ? 0.18333   -7.51798  -8.66856  1.000 41.71282  ? 46  ARG   A CZ  1 
ATOM   257  N NH1 . ARG   A 1 39  ? -0.34662  -7.06690  -7.54046  1.000 42.61971  ? 46  ARG   A NH1 1 
ATOM   258  N NH2 . ARG   A 1 39  ? 1.48832   -7.77169  -8.71591  1.000 44.29550  ? 46  ARG   A NH2 1 
ATOM   259  N N   . GLU   A 1 40  ? -1.37482  -10.40454 -13.45503 1.000 18.71587  ? 47  GLU   A N   1 
ATOM   260  C CA  . GLU   A 1 40  ? -0.52990  -9.97683  -14.57550 1.000 16.96645  ? 47  GLU   A CA  1 
ATOM   261  C C   . GLU   A 1 40  ? -1.12474  -10.40616 -15.90559 1.000 18.73619  ? 47  GLU   A C   1 
ATOM   262  O O   . GLU   A 1 40  ? -1.05630  -9.65953  -16.89813 1.000 20.32526  ? 47  GLU   A O   1 
ATOM   263  C CB  . GLU   A 1 40  ? 0.90223   -10.53845 -14.42343 1.000 18.01840  ? 47  GLU   A CB  1 
ATOM   264  C CG  . GLU   A 1 40  ? 1.65669   -10.03206 -13.19770 1.000 21.42714  ? 47  GLU   A CG  1 
ATOM   265  C CD  . GLU   A 1 40  ? 1.66555   -8.52063  -13.06854 1.000 24.54973  ? 47  GLU   A CD  1 
ATOM   266  O OE1 . GLU   A 1 40  ? 1.76365   -7.82860  -14.09937 1.000 27.65015  ? 47  GLU   A OE1 1 
ATOM   267  O OE2 . GLU   A 1 40  ? 1.64694   -8.01494  -11.91731 1.000 32.43671  ? 47  GLU   A OE2 1 
ATOM   268  N N   . LEU   A 1 41  ? -1.66282  -11.62716 -15.96216 1.000 17.57319  ? 48  LEU   A N   1 
ATOM   269  C CA  . LEU   A 1 41  ? -2.22626  -12.10567 -17.22163 1.000 18.22305  ? 48  LEU   A CA  1 
ATOM   270  C C   . LEU   A 1 41  ? -3.52808  -11.39139 -17.54703 1.000 18.70256  ? 48  LEU   A C   1 
ATOM   271  O O   . LEU   A 1 41  ? -3.79311  -11.07291 -18.71825 1.000 18.55249  ? 48  LEU   A O   1 
ATOM   272  C CB  . LEU   A 1 41  ? -2.44440  -13.61946 -17.18423 1.000 18.75399  ? 48  LEU   A CB  1 
ATOM   273  C CG  . LEU   A 1 41  ? -1.17199  -14.44907 -16.97198 1.000 19.92334  ? 48  LEU   A CG  1 
ATOM   274  C CD1 . LEU   A 1 41  ? -1.50658  -15.95305 -16.89533 1.000 20.29513  ? 48  LEU   A CD1 1 
ATOM   275  C CD2 . LEU   A 1 41  ? -0.10110  -14.20719 -18.06678 1.000 20.69595  ? 48  LEU   A CD2 1 
ATOM   276  N N   . ILE   A 1 42  ? -4.35859  -11.13387 -16.52194 1.000 17.45323  ? 49  ILE   A N   1 
ATOM   277  C CA  . ILE   A 1 42  ? -5.58144  -10.36474 -16.73518 1.000 17.80804  ? 49  ILE   A CA  1 
ATOM   278  C C   . ILE   A 1 42  ? -5.25385  -8.94111  -17.18354 1.000 18.86675  ? 49  ILE   A C   1 
ATOM   279  O O   . ILE   A 1 42  ? -5.93302  -8.38681  -18.05896 1.000 18.87727  ? 49  ILE   A O   1 
ATOM   280  C CB  . ILE   A 1 42  ? -6.47053  -10.40013 -15.47468 1.000 17.42466  ? 49  ILE   A CB  1 
ATOM   281  C CG1 . ILE   A 1 42  ? -7.02006  -11.82781 -15.31007 1.000 17.04751  ? 49  ILE   A CG1 1 
ATOM   282  C CG2 . ILE   A 1 42  ? -7.59762  -9.33388  -15.55560 1.000 19.71068  ? 49  ILE   A CG2 1 
ATOM   283  C CD1 . ILE   A 1 42  ? -7.79209  -12.01621 -13.95519 1.000 20.21545  ? 49  ILE   A CD1 1 
ATOM   284  N N   . SER   A 1 43  ? -4.20336  -8.32757  -16.61408 1.000 18.38047  ? 50  SER   A N   1 
ATOM   285  C CA  . SER   A 1 43  ? -3.83856  -6.98626  -17.02966 1.000 17.55328  ? 50  SER   A CA  1 
ATOM   286  C C   . SER   A 1 43  ? -3.36360  -6.98125  -18.48738 1.000 20.28072  ? 50  SER   A C   1 
ATOM   287  O O   . SER   A 1 43  ? -3.67696  -6.05540  -19.25911 1.000 18.66010  ? 50  SER   A O   1 
ATOM   288  C CB  . SER   A 1 43  ? -2.74128  -6.45333  -16.10698 1.000 25.87847  ? 50  SER   A CB  1 
ATOM   289  O OG  . SER   A 1 43  ? -2.19433  -5.24485  -16.59899 1.000 32.49300  ? 50  SER   A OG  1 
ATOM   290  N N   . ASN   A 1 44  ? -2.61824  -8.01372  -18.87978 1.000 19.02062  ? 51  ASN   A N   1 
ATOM   291  C CA  . ASN   A 1 44  ? -2.21597  -8.12734  -20.27995 1.000 18.35207  ? 51  ASN   A CA  1 
ATOM   292  C C   . ASN   A 1 44  ? -3.42948  -8.24286  -21.19285 1.000 17.64870  ? 51  ASN   A C   1 
ATOM   293  O O   . ASN   A 1 44  ? -3.47232  -7.59943  -22.25435 1.000 17.89845  ? 51  ASN   A O   1 
ATOM   294  C CB  . ASN   A 1 44  ? -1.31676  -9.34798  -20.47339 1.000 18.79633  ? 51  ASN   A CB  1 
ATOM   295  C CG  . ASN   A 1 44  ? 0.08764   -9.10780  -20.01022 1.000 25.44340  ? 51  ASN   A CG  1 
ATOM   296  O OD1 . ASN   A 1 44  ? 0.48003   -7.96976  -19.73871 1.000 26.36944  ? 51  ASN   A OD1 1 
ATOM   297  N ND2 . ASN   A 1 44  ? 0.88616   -10.16609 -19.98710 1.000 22.22674  ? 51  ASN   A ND2 1 
ATOM   298  N N   . SER   A 1 45  ? -4.42111  -9.04831  -20.78956 1.000 16.21714  ? 52  SER   A N   1 
ATOM   299  C CA  . SER   A 1 45  ? -5.64817  -9.16816  -21.58209 1.000 17.54250  ? 52  SER   A CA  1 
ATOM   300  C C   . SER   A 1 45  ? -6.35546  -7.82442  -21.68157 1.000 17.49966  ? 52  SER   A C   1 
ATOM   301  O O   . SER   A 1 45  ? -6.83196  -7.44479  -22.76396 1.000 18.34635  ? 52  SER   A O   1 
ATOM   302  C CB  . SER   A 1 45  ? -6.58938  -10.20350 -20.95874 1.000 16.98354  ? 52  SER   A CB  1 
ATOM   303  O OG  . SER   A 1 45  ? -6.06686  -11.52020 -21.11797 1.000 17.72748  ? 52  SER   A OG  1 
ATOM   304  N N   . SER   A 1 46  ? -6.44339  -7.09317  -20.56473 1.000 18.17747  ? 53  SER   A N   1 
ATOM   305  C CA  . SER   A 1 46  ? -7.09588  -5.78612  -20.57541 1.000 17.69548  ? 53  SER   A CA  1 
ATOM   306  C C   . SER   A 1 46  ? -6.37939  -4.83744  -21.54069 1.000 19.34144  ? 53  SER   A C   1 
ATOM   307  O O   . SER   A 1 46  ? -7.02775  -4.13973  -22.32652 1.000 18.58765  ? 53  SER   A O   1 
ATOM   308  C CB  . SER   A 1 46  ? -7.13337  -5.22241  -19.13980 1.000 17.68349  ? 53  SER   A CB  1 
ATOM   309  O OG  . SER   A 1 46  ? -7.70143  -3.91843  -19.16294 1.000 20.65198  ? 53  SER   A OG  1 
ATOM   310  N N   . ASP   A 1 47  ? -5.03788  -4.86759  -21.55433 1.000 18.19153  ? 54  ASP   A N   1 
ATOM   311  C CA  . ASP   A 1 47  ? -4.27027  -4.01798  -22.46182 1.000 19.52979  ? 54  ASP   A CA  1 
ATOM   312  C C   . ASP   A 1 47  ? -4.55104  -4.38120  -23.91209 1.000 21.45793  ? 54  ASP   A C   1 
ATOM   313  O O   . ASP   A 1 47  ? -4.63692  -3.49924  -24.78369 1.000 20.92353  ? 54  ASP   A O   1 
ATOM   314  C CB  . ASP   A 1 47  ? -2.78475  -4.18653  -22.17337 1.000 18.99777  ? 54  ASP   A CB  1 
ATOM   315  C CG  . ASP   A 1 47  ? -2.33722  -3.50792  -20.88066 1.000 24.74490  ? 54  ASP   A CG  1 
ATOM   316  O OD1 . ASP   A 1 47  ? -3.13028  -2.73079  -20.27194 1.000 27.86440  ? 54  ASP   A OD1 1 
ATOM   317  O OD2 . ASP   A 1 47  ? -1.15794  -3.71570  -20.47319 1.000 26.41114  ? 54  ASP   A OD2 1 
ATOM   318  N N   . ALA   A 1 48  ? -4.69409  -5.67547  -24.19920 1.000 17.46292  ? 55  ALA   A N   1 
ATOM   319  C CA  . ALA   A 1 48  ? -4.95387  -6.10340  -25.57410 1.000 18.80153  ? 55  ALA   A CA  1 
ATOM   320  C C   . ALA   A 1 48  ? -6.37046  -5.72792  -26.01581 1.000 17.53041  ? 55  ALA   A C   1 
ATOM   321  O O   . ALA   A 1 48  ? -6.62151  -5.42789  -27.19310 1.000 18.56739  ? 55  ALA   A O   1 
ATOM   322  C CB  . ALA   A 1 48  ? -4.74718  -7.62251  -25.68419 1.000 20.00572  ? 55  ALA   A CB  1 
ATOM   323  N N   . LEU   A 1 49  ? -7.30686  -5.79115  -25.07697 1.000 18.58157  ? 56  LEU   A N   1 
ATOM   324  C CA  . LEU   A 1 49  ? -8.67057  -5.35180  -25.34632 1.000 18.17731  ? 56  LEU   A CA  1 
ATOM   325  C C   . LEU   A 1 49  ? -8.71703  -3.85292  -25.59225 1.000 19.23162  ? 56  LEU   A C   1 
ATOM   326  O O   . LEU   A 1 49  ? -9.42004  -3.39134  -26.51319 1.000 19.17833  ? 56  LEU   A O   1 
ATOM   327  C CB  . LEU   A 1 49  ? -9.57269  -5.75489  -24.16700 1.000 17.00756  ? 56  LEU   A CB  1 
ATOM   328  C CG  . LEU   A 1 49  ? -9.87993  -7.26316  -24.18460 1.000 17.67459  ? 56  LEU   A CG  1 
ATOM   329  C CD1 . LEU   A 1 49  ? -10.25067 -7.73792  -22.76545 1.000 20.87736  ? 56  LEU   A CD1 1 
ATOM   330  C CD2 . LEU   A 1 49  ? -11.00189 -7.63030  -25.17266 1.000 19.39962  ? 56  LEU   A CD2 1 
ATOM   331  N N   . ASP   A 1 50  ? -7.99315  -3.06996  -24.78136 1.000 17.47600  ? 57  ASP   A N   1 
ATOM   332  C CA  . ASP   A 1 50  ? -7.92417  -1.62692  -25.01419 1.000 17.13352  ? 57  ASP   A CA  1 
ATOM   333  C C   . ASP   A 1 50  ? -7.45928  -1.32734  -26.43247 1.000 21.20706  ? 57  ASP   A C   1 
ATOM   334  O O   . ASP   A 1 50  ? -7.96467  -0.39541  -27.07263 1.000 20.24974  ? 57  ASP   A O   1 
ATOM   335  C CB  . ASP   A 1 50  ? -6.95807  -0.95169  -24.04993 1.000 18.89097  ? 57  ASP   A CB  1 
ATOM   336  C CG  . ASP   A 1 50  ? -7.43603  -0.90477  -22.61063 1.000 23.35106  ? 57  ASP   A CG  1 
ATOM   337  O OD1 . ASP   A 1 50  ? -8.60790  -1.21330  -22.31465 1.000 25.54192  ? 57  ASP   A OD1 1 
ATOM   338  O OD2 . ASP   A 1 50  ? -6.60776  -0.46475  -21.78235 1.000 25.11781  ? 57  ASP   A OD2 1 
ATOM   339  N N   . LYS   A 1 51  ? -6.45568  -2.07724  -26.91985 1.000 18.90384  ? 58  LYS   A N   1 
ATOM   340  C CA  . LYS   A 1 51  ? -5.90043  -1.80864  -28.24876 1.000 19.68490  ? 58  LYS   A CA  1 
ATOM   341  C C   . LYS   A 1 51  ? -6.91931  -2.04932  -29.36124 1.000 20.84727  ? 58  LYS   A C   1 
ATOM   342  O O   . LYS   A 1 51  ? -7.02024  -1.24670  -30.30129 1.000 21.75955  ? 58  LYS   A O   1 
ATOM   343  C CB  . LYS   A 1 51  ? -4.65865  -2.67944  -28.46864 1.000 20.87269  ? 58  LYS   A CB  1 
ATOM   344  C CG  . LYS   A 1 51  ? -3.42325  -2.18302  -27.70853 1.000 25.37822  ? 58  LYS   A CG  1 
ATOM   345  C CD  . LYS   A 1 51  ? -2.27351  -3.19216  -27.93255 1.000 26.51105  ? 58  LYS   A CD  1 
ATOM   346  C CE  . LYS   A 1 51  ? -1.12700  -3.08167  -26.93994 1.000 43.67996  ? 58  LYS   A CE  1 
ATOM   347  N NZ  . LYS   A 1 51  ? 0.02383   -3.90912  -27.49176 1.000 45.91066  ? 58  LYS   A NZ  1 
ATOM   348  N N   . ILE   A 1 52  ? -7.63532  -3.18073  -29.32466 1.000 20.81966  ? 59  ILE   A N   1 
ATOM   349  C CA  . ILE   A 1 52  ? -8.61952  -3.39531  -30.39179 1.000 21.33283  ? 59  ILE   A CA  1 
ATOM   350  C C   . ILE   A 1 52  ? -9.78628  -2.42762  -30.22898 1.000 20.86699  ? 59  ILE   A C   1 
ATOM   351  O O   . ILE   A 1 52  ? -10.33659 -1.95969  -31.23659 1.000 22.36074  ? 59  ILE   A O   1 
ATOM   352  C CB  . ILE   A 1 52  ? -9.09355  -4.85899  -30.48102 1.000 21.07318  ? 59  ILE   A CB  1 
ATOM   353  C CG1 . ILE   A 1 52  ? -9.88418  -5.09219  -31.77497 1.000 25.15463  ? 59  ILE   A CG1 1 
ATOM   354  C CG2 . ILE   A 1 52  ? -9.94735  -5.29504  -29.25287 1.000 20.78063  ? 59  ILE   A CG2 1 
ATOM   355  C CD1 . ILE   A 1 52  ? -9.06734  -4.85570  -33.07948 1.000 26.56195  ? 59  ILE   A CD1 1 
ATOM   356  N N   . ARG   A 1 53  ? -10.13406 -2.05278  -28.99173 1.000 20.13984  ? 60  ARG   A N   1 
ATOM   357  C CA  . ARG   A 1 53  ? -11.16135 -1.01721  -28.84782 1.000 20.36889  ? 60  ARG   A CA  1 
ATOM   358  C C   . ARG   A 1 53  ? -10.74059 0.28117   -29.52294 1.000 21.39146  ? 60  ARG   A C   1 
ATOM   359  O O   . ARG   A 1 53  ? -11.50638 0.85928   -30.31612 1.000 23.34841  ? 60  ARG   A O   1 
ATOM   360  C CB  . ARG   A 1 53  ? -11.49730 -0.75773  -27.38283 1.000 20.56558  ? 60  ARG   A CB  1 
ATOM   361  C CG  . ARG   A 1 53  ? -12.71632 0.16502   -27.28529 1.000 27.54363  ? 60  ARG   A CG  1 
ATOM   362  C CD  . ARG   A 1 53  ? -12.99578 0.54854   -25.88886 1.000 42.33378  ? 60  ARG   A CD  1 
ATOM   363  N NE  . ARG   A 1 53  ? -14.13912 -0.19418  -25.37938 1.000 53.53061  ? 60  ARG   A NE  1 
ATOM   364  C CZ  . ARG   A 1 53  ? -14.12567 -0.77298  -24.19184 1.000 46.43959  ? 60  ARG   A CZ  1 
ATOM   365  N NH1 . ARG   A 1 53  ? -13.07296 -0.66869  -23.40243 1.000 40.23629  ? 60  ARG   A NH1 1 
ATOM   366  N NH2 . ARG   A 1 53  ? -15.18720 -1.47362  -23.78890 1.000 40.63023  ? 60  ARG   A NH2 1 
ATOM   367  N N   . TYR   A 1 54  ? -9.50329  0.72765   -29.27835 1.000 21.72499  ? 61  TYR   A N   1 
ATOM   368  C CA  . TYR   A 1 54  ? -9.07605  1.98982   -29.86547 1.000 21.65541  ? 61  TYR   A CA  1 
ATOM   369  C C   . TYR   A 1 54  ? -9.10297  1.90998   -31.39294 1.000 22.59812  ? 61  TYR   A C   1 
ATOM   370  O O   . TYR   A 1 54  ? -9.58524  2.83741   -32.05964 1.000 23.32166  ? 61  TYR   A O   1 
ATOM   371  C CB  . TYR   A 1 54  ? -7.68586  2.38515   -29.35970 1.000 22.49274  ? 61  TYR   A CB  1 
ATOM   372  C CG  . TYR   A 1 54  ? -7.27953  3.76400   -29.87524 1.000 25.63705  ? 61  TYR   A CG  1 
ATOM   373  C CD1 . TYR   A 1 54  ? -7.78446  4.93180   -29.29066 1.000 26.88190  ? 61  TYR   A CD1 1 
ATOM   374  C CD2 . TYR   A 1 54  ? -6.41948  3.89781   -30.93947 1.000 28.64466  ? 61  TYR   A CD2 1 
ATOM   375  C CE1 . TYR   A 1 54  ? -7.42892  6.17028   -29.76131 1.000 28.82690  ? 61  TYR   A CE1 1 
ATOM   376  C CE2 . TYR   A 1 54  ? -6.06552  5.11536   -31.42475 1.000 29.39862  ? 61  TYR   A CE2 1 
ATOM   377  C CZ  . TYR   A 1 54  ? -6.56315  6.26139   -30.84103 1.000 31.23968  ? 61  TYR   A CZ  1 
ATOM   378  O OH  . TYR   A 1 54  ? -6.20940  7.49513   -31.33197 1.000 38.29417  ? 61  TYR   A OH  1 
ATOM   379  N N   . GLU   A 1 55  ? -8.60188  0.80430   -31.96405 1.000 24.00048  ? 62  GLU   A N   1 
ATOM   380  C CA  . GLU   A 1 55  ? -8.60906  0.67432   -33.43129 1.000 24.18096  ? 62  GLU   A CA  1 
ATOM   381  C C   . GLU   A 1 55  ? -10.02746 0.75358   -33.97695 1.000 25.40691  ? 62  GLU   A C   1 
ATOM   382  O O   . GLU   A 1 55  ? -10.26262 1.34572   -35.04368 1.000 29.13882  ? 62  GLU   A O   1 
ATOM   383  C CB  . GLU   A 1 55  ? -7.95676  -0.64879  -33.83900 1.000 25.99882  ? 62  GLU   A CB  1 
ATOM   384  C CG  . GLU   A 1 55  ? -6.46963  -0.63374  -33.58336 1.000 31.11490  ? 62  GLU   A CG  1 
ATOM   385  C CD  . GLU   A 1 55  ? -5.70334  -1.68057  -34.34956 1.000 41.63021  ? 62  GLU   A CD  1 
ATOM   386  O OE1 . GLU   A 1 55  ? -4.44603  -1.61454  -34.34729 1.000 45.67224  ? 62  GLU   A OE1 1 
ATOM   387  O OE2 . GLU   A 1 55  ? -6.35251  -2.58617  -34.91857 1.000 40.09165  ? 62  GLU   A OE2 1 
ATOM   388  N N   . SER   A 1 56  ? -10.99326 0.16458   -33.25484 1.000 24.08117  ? 63  SER   A N   1 
ATOM   389  C CA  . SER   A 1 56  ? -12.37781 0.15337   -33.73069 1.000 27.19364  ? 63  SER   A CA  1 
ATOM   390  C C   . SER   A 1 56  ? -13.02478 1.53834   -33.69893 1.000 26.76120  ? 63  SER   A C   1 
ATOM   391  O O   . SER   A 1 56  ? -14.03600 1.74162   -34.37565 1.000 28.46298  ? 63  SER   A O   1 
ATOM   392  C CB  . SER   A 1 56  ? -13.20751 -0.84247  -32.90115 1.000 27.42779  ? 63  SER   A CB  1 
ATOM   393  O OG  . SER   A 1 56  ? -13.52927 -0.29738  -31.60350 1.000 27.86037  ? 63  SER   A OG  1 
ATOM   394  N N   . LEU   A 1 57  ? -12.46268 2.49828   -32.96249 1.000 25.15006  ? 64  LEU   A N   1 
ATOM   395  C CA  . LEU   A 1 57  ? -13.09497 3.81439   -32.87466 1.000 27.45944  ? 64  LEU   A CA  1 
ATOM   396  C C   . LEU   A 1 57  ? -13.09590 4.51072   -34.21984 1.000 35.22983  ? 64  LEU   A C   1 
ATOM   397  O O   . LEU   A 1 57  ? -14.00915 5.28368   -34.51670 1.000 37.10604  ? 64  LEU   A O   1 
ATOM   398  C CB  . LEU   A 1 57  ? -12.38814 4.70155   -31.84906 1.000 27.08521  ? 64  LEU   A CB  1 
ATOM   399  C CG  . LEU   A 1 57  ? -12.48168 4.15306   -30.42945 1.000 27.27171  ? 64  LEU   A CG  1 
ATOM   400  C CD1 . LEU   A 1 57  ? -11.80222 5.12872   -29.47955 1.000 26.93742  ? 64  LEU   A CD1 1 
ATOM   401  C CD2 . LEU   A 1 57  ? -13.91987 3.91596   -29.99257 1.000 30.43574  ? 64  LEU   A CD2 1 
ATOM   402  N N   . THR   A 1 58  ? -12.08951 4.25452   -35.04033 1.000 28.31994  ? 65  THR   A N   1 
ATOM   403  C CA  . THR   A 1 58  ? -12.01154 4.86785   -36.35414 1.000 34.39491  ? 65  THR   A CA  1 
ATOM   404  C C   . THR   A 1 58  ? -12.26836 3.88338   -37.48489 1.000 30.37015  ? 65  THR   A C   1 
ATOM   405  O O   . THR   A 1 58  ? -12.46049 4.31208   -38.62849 1.000 38.20627  ? 65  THR   A O   1 
ATOM   406  C CB  . THR   A 1 58  ? -10.64134 5.52657   -36.53971 1.000 42.10188  ? 65  THR   A CB  1 
ATOM   407  O OG1 . THR   A 1 58  ? -9.61772  4.54293   -36.36885 1.000 41.63344  ? 65  THR   A OG1 1 
ATOM   408  C CG2 . THR   A 1 58  ? -10.44121 6.64900   -35.51871 1.000 40.77501  ? 65  THR   A CG2 1 
ATOM   409  N N   . ASP   A 1 59  ? -12.32302 2.58717   -37.18892 1.000 35.45185  ? 66  ASP   A N   1 
ATOM   410  C CA  . ASP   A 1 59  ? -12.54489 1.56193   -38.20609 1.000 34.01732  ? 66  ASP   A CA  1 
ATOM   411  C C   . ASP   A 1 59  ? -13.37700 0.46604   -37.56505 1.000 33.79525  ? 66  ASP   A C   1 
ATOM   412  O O   . ASP   A 1 59  ? -12.84054 -0.49483  -36.99751 1.000 32.28706  ? 66  ASP   A O   1 
ATOM   413  C CB  . ASP   A 1 59  ? -11.22125 1.01953   -38.74176 1.000 34.54769  ? 66  ASP   A CB  1 
ATOM   414  C CG  . ASP   A 1 59  ? -11.40720 -0.00659  -39.83852 1.000 42.07755  ? 66  ASP   A CG  1 
ATOM   415  O OD1 . ASP   A 1 59  ? -12.56600 -0.27361  -40.21081 1.000 41.85958  ? 66  ASP   A OD1 1 
ATOM   416  O OD2 . ASP   A 1 59  ? -10.38972 -0.54247  -40.32711 1.000 40.34703  ? 66  ASP   A OD2 1 
ATOM   417  N N   . PRO   A 1 60  ? -14.70909 0.56547   -37.63795 1.000 37.77607  ? 67  PRO   A N   1 
ATOM   418  C CA  . PRO   A 1 60  ? -15.54615 -0.46476  -37.00065 1.000 39.27712  ? 67  PRO   A CA  1 
ATOM   419  C C   . PRO   A 1 60  ? -15.35102 -1.85795  -37.59242 1.000 34.04456  ? 67  PRO   A C   1 
ATOM   420  O O   . PRO   A 1 60  ? -15.63869 -2.84773  -36.90404 1.000 33.55112  ? 67  PRO   A O   1 
ATOM   421  C CB  . PRO   A 1 60  ? -16.97465 0.04711   -37.22561 1.000 41.63984  ? 67  PRO   A CB  1 
ATOM   422  C CG  . PRO   A 1 60  ? -16.82177 1.51915   -37.48788 1.000 50.15501  ? 67  PRO   A CG  1 
ATOM   423  C CD  . PRO   A 1 60  ? -15.50738 1.67443   -38.18825 1.000 38.26167  ? 67  PRO   A CD  1 
ATOM   424  N N   . SER   A 1 61  ? -14.87545 -1.97774  -38.83965 1.000 37.17123  ? 68  SER   A N   1 
ATOM   425  C CA  . SER   A 1 61  ? -14.65869 -3.31372  -39.38247 1.000 33.34653  ? 68  SER   A CA  1 
ATOM   426  C C   . SER   A 1 61  ? -13.59479 -4.08792  -38.61534 1.000 33.56395  ? 68  SER   A C   1 
ATOM   427  O O   . SER   A 1 61  ? -13.50905 -5.31249  -38.76230 1.000 30.89397  ? 68  SER   A O   1 
ATOM   428  C CB  . SER   A 1 61  ? -14.27584 -3.25261  -40.85609 1.000 33.63466  ? 68  SER   A CB  1 
ATOM   429  O OG  . SER   A 1 61  ? -12.98027 -2.70762  -41.01268 1.000 40.11228  ? 68  SER   A OG  1 
ATOM   430  N N   . LYS   A 1 62  ? -12.78653 -3.41681  -37.78329 1.000 31.07978  ? 69  LYS   A N   1 
ATOM   431  C CA  . LYS   A 1 62  ? -11.83096 -4.14738  -36.96567 1.000 27.49120  ? 69  LYS   A CA  1 
ATOM   432  C C   . LYS   A 1 62  ? -12.51355 -5.14881  -36.03422 1.000 27.30665  ? 69  LYS   A C   1 
ATOM   433  O O   . LYS   A 1 62  ? -11.86078 -6.06046  -35.51531 1.000 25.53965  ? 69  LYS   A O   1 
ATOM   434  C CB  . LYS   A 1 62  ? -11.02083 -3.14701  -36.14823 1.000 28.48104  ? 69  LYS   A CB  1 
ATOM   435  C CG  . LYS   A 1 62  ? -10.14670 -2.21422  -36.96351 1.000 34.61728  ? 69  LYS   A CG  1 
ATOM   436  C CD  . LYS   A 1 62  ? -8.75074  -2.77067  -37.07021 1.000 36.55084  ? 69  LYS   A CD  1 
ATOM   437  C CE  . LYS   A 1 62  ? -7.86887  -1.97830  -37.99904 1.000 36.56510  ? 69  LYS   A CE  1 
ATOM   438  N NZ  . LYS   A 1 62  ? -6.44047  -2.39323  -37.72045 1.000 44.99331  ? 69  LYS   A NZ  1 
ATOM   439  N N   . LEU   A 1 63  ? -13.79443 -4.96094  -35.73185 1.000 26.57889  ? 70  LEU   A N   1 
ATOM   440  C CA  . LEU   A 1 63  ? -14.51551 -5.89285  -34.87851 1.000 28.77301  ? 70  LEU   A CA  1 
ATOM   441  C C   . LEU   A 1 63  ? -15.34044 -6.88439  -35.69121 1.000 28.60008  ? 70  LEU   A C   1 
ATOM   442  O O   . LEU   A 1 63  ? -16.15656 -7.60799  -35.10923 1.000 32.64509  ? 70  LEU   A O   1 
ATOM   443  C CB  . LEU   A 1 63  ? -15.44179 -5.14060  -33.90877 1.000 27.95915  ? 70  LEU   A CB  1 
ATOM   444  C CG  . LEU   A 1 63  ? -14.72011 -4.17845  -32.95604 1.000 30.36693  ? 70  LEU   A CG  1 
ATOM   445  C CD1 . LEU   A 1 63  ? -15.72116 -3.39427  -32.09354 1.000 31.73764  ? 70  LEU   A CD1 1 
ATOM   446  C CD2 . LEU   A 1 63  ? -13.74068 -4.95741  -32.11576 1.000 29.50685  ? 70  LEU   A CD2 1 
ATOM   447  N N   . ASP   A 1 64  ? -15.12293 -6.96798  -37.00723 1.000 27.70906  ? 71  ASP   A N   1 
ATOM   448  C CA  . ASP   A 1 64  ? -15.84265 -7.97845  -37.78071 1.000 33.52555  ? 71  ASP   A CA  1 
ATOM   449  C C   . ASP   A 1 64  ? -15.50585 -9.37674  -37.28434 1.000 31.56965  ? 71  ASP   A C   1 
ATOM   450  O O   . ASP   A 1 64  ? -16.30376 -10.30664 -37.43989 1.000 34.41650  ? 71  ASP   A O   1 
ATOM   451  C CB  . ASP   A 1 64  ? -15.50907 -7.83410  -39.26202 1.000 31.01893  ? 71  ASP   A CB  1 
ATOM   452  C CG  . ASP   A 1 64  ? -16.22668 -6.65113  -39.91032 1.000 38.32400  ? 71  ASP   A CG  1 
ATOM   453  O OD1 . ASP   A 1 64  ? -17.06849 -6.00638  -39.23922 1.000 44.96823  ? 71  ASP   A OD1 1 
ATOM   454  O OD2 . ASP   A 1 64  ? -15.94939 -6.34853  -41.09347 1.000 41.15059  ? 71  ASP   A OD2 1 
ATOM   455  N N   . SER   A 1 65  ? -14.32964 -9.53563  -36.70756 1.000 28.91657  ? 72  SER   A N   1 
ATOM   456  C CA  . SER   A 1 65  ? -13.83794 -10.77352 -36.12424 1.000 27.77955  ? 72  SER   A CA  1 
ATOM   457  C C   . SER   A 1 65  ? -14.39415 -11.03364 -34.73290 1.000 32.13427  ? 72  SER   A C   1 
ATOM   458  O O   . SER   A 1 65  ? -13.95042 -11.96152 -34.04905 1.000 34.61094  ? 72  SER   A O   1 
ATOM   459  C CB  . SER   A 1 65  ? -12.31259 -10.73320 -36.10105 1.000 27.00416  ? 72  SER   A CB  1 
ATOM   460  O OG  . SER   A 1 65  ? -11.84716 -9.50215  -35.51599 1.000 26.50798  ? 72  SER   A OG  1 
ATOM   461  N N   . GLY   A 1 66  ? -15.34891 -10.22302 -34.28594 1.000 29.67491  ? 73  GLY   A N   1 
ATOM   462  C CA  . GLY   A 1 66  ? -15.94805 -10.41769 -32.98308 1.000 31.93502  ? 73  GLY   A CA  1 
ATOM   463  C C   . GLY   A 1 66  ? -16.16912 -9.09301  -32.27969 1.000 32.24376  ? 73  GLY   A C   1 
ATOM   464  O O   . GLY   A 1 66  ? -15.20735 -8.37188  -32.00218 1.000 27.69851  ? 73  GLY   A O   1 
ATOM   465  N N   . LYS   A 1 67  ? -17.42299 -8.78537  -31.94329 1.000 29.43816  ? 74  LYS   A N   1 
ATOM   466  C CA  . LYS   A 1 67  ? -17.75558 -7.51100  -31.31057 1.000 30.79025  ? 74  LYS   A CA  1 
ATOM   467  C C   . LYS   A 1 67  ? -17.55048 -7.53192  -29.79862 1.000 29.32064  ? 74  LYS   A C   1 
ATOM   468  O O   . LYS   A 1 67  ? -17.33700 -6.47567  -29.19437 1.000 31.19400  ? 74  LYS   A O   1 
ATOM   469  C CB  . LYS   A 1 67  ? -19.21364 -7.15233  -31.61252 1.000 30.92582  ? 74  LYS   A CB  1 
ATOM   470  C CG  . LYS   A 1 67  ? -19.44921 -6.75752  -33.08042 1.000 43.41063  ? 74  LYS   A CG  1 
ATOM   471  C CD  . LYS   A 1 67  ? -20.48871 -5.64651  -33.27403 1.000 47.24313  ? 74  LYS   A CD  1 
ATOM   472  C CE  . LYS   A 1 67  ? -20.85877 -5.50674  -34.74750 1.000 55.58453  ? 74  LYS   A CE  1 
ATOM   473  N NZ  . LYS   A 1 67  ? -21.62703 -4.25140  -35.02138 1.000 75.50350  ? 74  LYS   A NZ  1 
ATOM   474  N N   . GLU   A 1 68  ? -17.63957 -8.69412  -29.17287 1.000 25.68788  ? 75  GLU   A N   1 
ATOM   475  C CA  . GLU   A 1 68  ? -17.60181 -8.75250  -27.71545 1.000 27.26729  ? 75  GLU   A CA  1 
ATOM   476  C C   . GLU   A 1 68  ? -16.17803 -8.60569  -27.20562 1.000 24.23247  ? 75  GLU   A C   1 
ATOM   477  O O   . GLU   A 1 68  ? -15.26009 -9.20980  -27.74711 1.000 26.36429  ? 75  GLU   A O   1 
ATOM   478  C CB  . GLU   A 1 68  ? -18.18277 -10.07346 -27.21823 1.000 30.66335  ? 75  GLU   A CB  1 
ATOM   479  C CG  . GLU   A 1 68  ? -19.67627 -10.20004 -27.38728 1.000 36.58327  ? 75  GLU   A CG  1 
ATOM   480  C CD  . GLU   A 1 68  ? -20.08941 -10.52139 -28.81542 1.000 63.62623  ? 75  GLU   A CD  1 
ATOM   481  O OE1 . GLU   A 1 68  ? -19.27188 -11.14137 -29.53118 1.000 52.65454  ? 75  GLU   A OE1 1 
ATOM   482  O OE2 . GLU   A 1 68  ? -21.21315 -10.12842 -29.22883 1.000 57.36045  ? 75  GLU   A OE2 1 
ATOM   483  N N   . LEU   A 1 69  ? -16.01234 -7.80643  -26.15550 1.000 23.95620  ? 76  LEU   A N   1 
ATOM   484  C CA  . LEU   A 1 69  ? -14.70963 -7.53731  -25.54111 1.000 19.60585  ? 76  LEU   A CA  1 
ATOM   485  C C   . LEU   A 1 69  ? -14.75834 -8.05563  -24.11136 1.000 17.80876  ? 76  LEU   A C   1 
ATOM   486  O O   . LEU   A 1 69  ? -15.37808 -7.42793  -23.24231 1.000 21.37882  ? 76  LEU   A O   1 
ATOM   487  C CB  . LEU   A 1 69  ? -14.44929 -6.03220  -25.57039 1.000 21.60114  ? 76  LEU   A CB  1 
ATOM   488  C CG  . LEU   A 1 69  ? -14.35517 -5.38174  -26.96566 1.000 25.71103  ? 76  LEU   A CG  1 
ATOM   489  C CD1 . LEU   A 1 69  ? -13.92531 -3.91223  -26.82896 1.000 34.60912  ? 76  LEU   A CD1 1 
ATOM   490  C CD2 . LEU   A 1 69  ? -13.39028 -6.14124  -27.88411 1.000 25.66045  ? 76  LEU   A CD2 1 
ATOM   491  N N   . HIS   A 1 70  ? -14.10727 -9.19684  -23.86115 1.000 19.78332  ? 77  HIS   A N   1 
ATOM   492  C CA  . HIS   A 1 70  ? -14.26411 -9.82656  -22.55468 1.000 19.66205  ? 77  HIS   A CA  1 
ATOM   493  C C   . HIS   A 1 70  ? -13.07290 -10.69560 -22.23169 1.000 17.80173  ? 77  HIS   A C   1 
ATOM   494  O O   . HIS   A 1 70  ? -12.20656 -10.95465 -23.08360 1.000 17.85278  ? 77  HIS   A O   1 
ATOM   495  C CB  . HIS   A 1 70  ? -15.55393 -10.65986 -22.51061 1.000 21.54806  ? 77  HIS   A CB  1 
ATOM   496  C CG  . HIS   A 1 70  ? -15.56213 -11.79561 -23.49224 1.000 19.12884  ? 77  HIS   A CG  1 
ATOM   497  N ND1 . HIS   A 1 70  ? -16.54491 -11.94441 -24.44164 1.000 30.42680  ? 77  HIS   A ND1 1 
ATOM   498  C CD2 . HIS   A 1 70  ? -14.72290 -12.84772 -23.64936 1.000 20.03345  ? 77  HIS   A CD2 1 
ATOM   499  C CE1 . HIS   A 1 70  ? -16.30019 -13.03031 -25.15427 1.000 26.06686  ? 77  HIS   A CE1 1 
ATOM   500  N NE2 . HIS   A 1 70  ? -15.20338 -13.59618 -24.69556 1.000 24.86213  ? 77  HIS   A NE2 1 
ATOM   501  N N   . ILE   A 1 71  ? -13.04853 -11.15018 -20.96790 1.000 16.69196  ? 78  ILE   A N   1 
ATOM   502  C CA  . ILE   A 1 71  ? -12.02415 -12.03678 -20.44685 1.000 15.94360  ? 78  ILE   A CA  1 
ATOM   503  C C   . ILE   A 1 71  ? -12.70482 -13.22938 -19.78494 1.000 18.31422  ? 78  ILE   A C   1 
ATOM   504  O O   . ILE   A 1 71  ? -13.59481 -13.03737 -18.94816 1.000 18.86671  ? 78  ILE   A O   1 
ATOM   505  C CB  . ILE   A 1 71  ? -11.15654 -11.31234 -19.39802 1.000 17.66176  ? 78  ILE   A CB  1 
ATOM   506  C CG1 . ILE   A 1 71  ? -10.47046 -10.09328 -20.03607 1.000 18.21213  ? 78  ILE   A CG1 1 
ATOM   507  C CG2 . ILE   A 1 71  ? -10.15319 -12.31868 -18.80202 1.000 17.85979  ? 78  ILE   A CG2 1 
ATOM   508  C CD1 . ILE   A 1 71  ? -9.81004  -9.17743  -19.02549 1.000 19.77642  ? 78  ILE   A CD1 1 
ATOM   509  N N   . ASN   A 1 72  ? -12.29840 -14.46076 -20.15558 1.000 18.32843  ? 79  ASN   A N   1 
ATOM   510  C CA  . ASN   A 1 72  ? -12.84123 -15.66436 -19.51562 1.000 16.44855  ? 79  ASN   A CA  1 
ATOM   511  C C   . ASN   A 1 72  ? -11.71955 -16.40451 -18.80222 1.000 19.32776  ? 79  ASN   A C   1 
ATOM   512  O O   . ASN   A 1 72  ? -10.59397 -16.47035 -19.29516 1.000 18.53118  ? 79  ASN   A O   1 
ATOM   513  C CB  . ASN   A 1 72  ? -13.50469 -16.60246 -20.53343 1.000 17.61471  ? 79  ASN   A CB  1 
ATOM   514  C CG  . ASN   A 1 72  ? -14.68256 -15.97532 -21.20988 1.000 20.77277  ? 79  ASN   A CG  1 
ATOM   515  O OD1 . ASN   A 1 72  ? -15.38472 -15.15837 -20.62223 1.000 21.47647  ? 79  ASN   A OD1 1 
ATOM   516  N ND2 . ASN   A 1 72  ? -14.94013 -16.38546 -22.45882 1.000 21.93795  ? 79  ASN   A ND2 1 
ATOM   517  N N   . LEU   A 1 73  ? -12.00795 -16.95172 -17.61593 1.000 17.54927  ? 80  LEU   A N   1 
ATOM   518  C CA  . LEU   A 1 73  ? -11.06001 -17.77426 -16.87490 1.000 16.16471  ? 80  LEU   A CA  1 
ATOM   519  C C   . LEU   A 1 73  ? -11.63938 -19.17347 -16.84188 1.000 18.46326  ? 80  LEU   A C   1 
ATOM   520  O O   . LEU   A 1 73  ? -12.76135 -19.36857 -16.36382 1.000 18.99777  ? 80  LEU   A O   1 
ATOM   521  C CB  . LEU   A 1 73  ? -10.88308 -17.25063 -15.44595 1.000 19.15404  ? 80  LEU   A CB  1 
ATOM   522  C CG  . LEU   A 1 73  ? -10.54438 -15.76542 -15.35984 1.000 17.87177  ? 80  LEU   A CG  1 
ATOM   523  C CD1 . LEU   A 1 73  ? -10.49104 -15.36621 -13.89332 1.000 18.13125  ? 80  LEU   A CD1 1 
ATOM   524  C CD2 . LEU   A 1 73  ? -9.21457  -15.44832 -16.07343 1.000 18.50186  ? 80  LEU   A CD2 1 
ATOM   525  N N   . ILE   A 1 74  ? -10.91199 -20.13978 -17.39002 1.000 17.57117  ? 81  ILE   A N   1 
ATOM   526  C CA  . ILE   A 1 74  ? -11.43960 -21.48928 -17.55782 1.000 20.50531  ? 81  ILE   A CA  1 
ATOM   527  C C   . ILE   A 1 74  ? -10.50676 -22.46886 -16.86872 1.000 18.98674  ? 81  ILE   A C   1 
ATOM   528  O O   . ILE   A 1 74  ? -9.46926  -22.84925 -17.40766 1.000 20.38485  ? 81  ILE   A O   1 
ATOM   529  C CB  . ILE   A 1 74  ? -11.60046 -21.85609 -19.04564 1.000 19.86535  ? 81  ILE   A CB  1 
ATOM   530  C CG1 . ILE   A 1 74  ? -12.34048 -20.71035 -19.75795 1.000 21.89310  ? 81  ILE   A CG1 1 
ATOM   531  C CG2 . ILE   A 1 74  ? -12.32205 -23.20050 -19.17989 1.000 19.43220  ? 81  ILE   A CG2 1 
ATOM   532  C CD1 . ILE   A 1 74  ? -12.49556 -20.91039 -21.31400 1.000 21.18444  ? 81  ILE   A CD1 1 
ATOM   533  N N   . PRO   A 1 75  ? -10.89063 -22.94491 -15.68991 1.000 20.46060  ? 82  PRO   A N   1 
ATOM   534  C CA  . PRO   A 1 75  ? -10.15185 -24.02745 -15.04024 1.000 20.50358  ? 82  PRO   A CA  1 
ATOM   535  C C   . PRO   A 1 75  ? -10.60990 -25.37178 -15.57115 1.000 22.43676  ? 82  PRO   A C   1 
ATOM   536  O O   . PRO   A 1 75  ? -11.78843 -25.56881 -15.88393 1.000 25.48219  ? 82  PRO   A O   1 
ATOM   537  C CB  . PRO   A 1 75  ? -10.54062 -23.87961 -13.56157 1.000 21.50090  ? 82  PRO   A CB  1 
ATOM   538  C CG  . PRO   A 1 75  ? -11.95541 -23.32077 -13.60880 1.000 24.88395  ? 82  PRO   A CG  1 
ATOM   539  C CD  . PRO   A 1 75  ? -12.10484 -22.56172 -14.94952 1.000 23.39770  ? 82  PRO   A CD  1 
ATOM   540  N N   . ASN   A 1 76  ? -9.66532  -26.31021 -15.65193 1.000 23.20046  ? 83  ASN   A N   1 
ATOM   541  C CA  . ASN   A 1 76  ? -9.96110  -27.68273 -16.06184 1.000 24.43267  ? 83  ASN   A CA  1 
ATOM   542  C C   . ASN   A 1 76  ? -9.13638  -28.63086 -15.20234 1.000 26.08046  ? 83  ASN   A C   1 
ATOM   543  O O   . ASN   A 1 76  ? -7.93582  -28.78376 -15.43003 1.000 28.28907  ? 83  ASN   A O   1 
ATOM   544  C CB  . ASN   A 1 76  ? -9.66532  -27.91390 -17.54435 1.000 26.67713  ? 83  ASN   A CB  1 
ATOM   545  C CG  . ASN   A 1 76  ? -10.18500 -29.27091 -18.02381 1.000 30.42593  ? 83  ASN   A CG  1 
ATOM   546  O OD1 . ASN   A 1 76  ? -9.79219  -30.30469 -17.49801 1.000 34.74551  ? 83  ASN   A OD1 1 
ATOM   547  N ND2 . ASN   A 1 76  ? -11.07873 -29.26210 -19.01056 1.000 39.07739  ? 83  ASN   A ND2 1 
ATOM   548  N N   . LYS   A 1 77  ? -9.77535  -29.29687 -14.24739 1.000 27.84393  ? 84  LYS   A N   1 
ATOM   549  C CA  . LYS   A 1 77  ? -9.04518  -30.15336 -13.31324 1.000 31.06607  ? 84  LYS   A CA  1 
ATOM   550  C C   . LYS   A 1 77  ? -8.58256  -31.45107 -13.94781 1.000 32.84482  ? 84  LYS   A C   1 
ATOM   551  O O   . LYS   A 1 77  ? -7.60632  -32.03993 -13.47944 1.000 37.05030  ? 84  LYS   A O   1 
ATOM   552  C CB  . LYS   A 1 77  ? -9.91561  -30.48209 -12.10501 1.000 32.02417  ? 84  LYS   A CB  1 
ATOM   553  C CG  . LYS   A 1 77  ? -10.14010 -29.27128 -11.20763 1.000 33.76808  ? 84  LYS   A CG  1 
ATOM   554  C CD  . LYS   A 1 77  ? -10.88924 -29.66511 -9.94962  1.000 34.10155  ? 84  LYS   A CD  1 
ATOM   555  C CE  . LYS   A 1 77  ? -11.12574 -28.45348 -9.07742  1.000 38.38379  ? 84  LYS   A CE  1 
ATOM   556  N NZ  . LYS   A 1 77  ? -12.05710 -27.51954 -9.77979  1.000 45.95300  ? 84  LYS   A NZ  1 
ATOM   557  N N   . GLN   A 1 78  ? -9.27106  -31.91996 -14.99251 1.000 36.30845  ? 85  GLN   A N   1 
ATOM   558  C CA  . GLN   A 1 78  ? -8.85766  -33.16149 -15.64020 1.000 39.17303  ? 85  GLN   A CA  1 
ATOM   559  C C   . GLN   A 1 78  ? -7.55708  -32.96388 -16.40640 1.000 34.96504  ? 85  GLN   A C   1 
ATOM   560  O O   . GLN   A 1 78  ? -6.69040  -33.84711 -16.40007 1.000 41.42581  ? 85  GLN   A O   1 
ATOM   561  C CB  . GLN   A 1 78  ? -9.95159  -33.67674 -16.58238 1.000 41.83084  ? 85  GLN   A CB  1 
ATOM   562  C CG  . GLN   A 1 78  ? -11.15708 -34.32435 -15.91344 1.000 59.82573  ? 85  GLN   A CG  1 
ATOM   563  C CD  . GLN   A 1 78  ? -11.80376 -33.43615 -14.86091 1.000 71.87404  ? 85  GLN   A CD  1 
ATOM   564  O OE1 . GLN   A 1 78  ? -11.75517 -33.73103 -13.66118 1.000 68.42804  ? 85  GLN   A OE1 1 
ATOM   565  N NE2 . GLN   A 1 78  ? -12.38060 -32.31785 -15.30455 1.000 68.29769  ? 85  GLN   A NE2 1 
ATOM   566  N N   . ASP   A 1 79  ? -7.41138  -31.81728 -17.05983 1.000 30.37157  ? 86  ASP   A N   1 
ATOM   567  C CA  . ASP   A 1 79  ? -6.22316  -31.46035 -17.82466 1.000 34.03951  ? 86  ASP   A CA  1 
ATOM   568  C C   . ASP   A 1 79  ? -5.18096  -30.75149 -16.97483 1.000 29.95171  ? 86  ASP   A C   1 
ATOM   569  O O   . ASP   A 1 79  ? -4.05757  -30.56729 -17.44648 1.000 29.99194  ? 86  ASP   A O   1 
ATOM   570  C CB  . ASP   A 1 79  ? -6.58157  -30.53777 -18.99885 1.000 36.61497  ? 86  ASP   A CB  1 
ATOM   571  C CG  . ASP   A 1 79  ? -7.55501  -31.17301 -19.97626 1.000 44.41875  ? 86  ASP   A CG  1 
ATOM   572  O OD1 . ASP   A 1 79  ? -7.69650  -32.41971 -19.96562 1.000 46.92285  ? 86  ASP   A OD1 1 
ATOM   573  O OD2 . ASP   A 1 79  ? -8.17639  -30.41320 -20.75239 1.000 40.63712  ? 86  ASP   A OD2 1 
ATOM   574  N N   . ARG   A 1 80  ? -5.53675  -30.38346 -15.74132 1.000 27.11755  ? 87  ARG   A N   1 
ATOM   575  C CA  . ARG   A 1 80  ? -4.72576  -29.52839 -14.85215 1.000 25.22260  ? 87  ARG   A CA  1 
ATOM   576  C C   . ARG   A 1 80  ? -4.25961  -28.25179 -15.54925 1.000 23.83811  ? 87  ARG   A C   1 
ATOM   577  O O   . ARG   A 1 80  ? -3.06506  -27.90622 -15.54693 1.000 27.08382  ? 87  ARG   A O   1 
ATOM   578  C CB  . ARG   A 1 80  ? -3.52790  -30.27652 -14.26207 1.000 28.02813  ? 87  ARG   A CB  1 
ATOM   579  C CG  . ARG   A 1 80  ? -3.11990  -29.63503 -12.94606 1.000 29.97205  ? 87  ARG   A CG  1 
ATOM   580  C CD  . ARG   A 1 80  ? -1.70958  -29.93146 -12.53671 1.000 40.25528  ? 87  ARG   A CD  1 
ATOM   581  N NE  . ARG   A 1 80  ? -1.48336  -31.34617 -12.33481 1.000 45.74646  ? 87  ARG   A NE  1 
ATOM   582  C CZ  . ARG   A 1 80  ? -0.31747  -31.95585 -12.50738 1.000 55.41437  ? 87  ARG   A CZ  1 
ATOM   583  N NH1 . ARG   A 1 80  ? 0.75777   -31.30130 -12.91883 1.000 43.78415  ? 87  ARG   A NH1 1 
ATOM   584  N NH2 . ARG   A 1 80  ? -0.22091  -33.24829 -12.23140 1.000 47.21928  ? 87  ARG   A NH2 1 
ATOM   585  N N   . THR   A 1 81  ? -5.20778  -27.53790 -16.14049 1.000 22.75245  ? 88  THR   A N   1 
ATOM   586  C CA  . THR   A 1 81  ? -4.91475  -26.30341 -16.84988 1.000 20.63901  ? 88  THR   A CA  1 
ATOM   587  C C   . THR   A 1 81  ? -5.81844  -25.19047 -16.36037 1.000 21.35674  ? 88  THR   A C   1 
ATOM   588  O O   . THR   A 1 81  ? -6.98714  -25.41385 -16.03786 1.000 21.98596  ? 88  THR   A O   1 
ATOM   589  C CB  . THR   A 1 81  ? -5.08132  -26.40694 -18.39674 1.000 23.25950  ? 88  THR   A CB  1 
ATOM   590  O OG1 . THR   A 1 81  ? -6.43004  -26.79388 -18.72799 1.000 25.47634  ? 88  THR   A OG1 1 
ATOM   591  C CG2 . THR   A 1 81  ? -4.09323  -27.40812 -18.96270 1.000 26.47718  ? 88  THR   A CG2 1 
ATOM   592  N N   . LEU   A 1 82  ? -5.26899  -23.97511 -16.32783 1.000 18.59962  ? 89  LEU   A N   1 
ATOM   593  C CA  . LEU   A 1 82  ? -6.04027  -22.75210 -16.15964 1.000 19.28868  ? 89  LEU   A CA  1 
ATOM   594  C C   . LEU   A 1 82  ? -5.81526  -21.90657 -17.40470 1.000 19.92495  ? 89  LEU   A C   1 
ATOM   595  O O   . LEU   A 1 82  ? -4.66751  -21.60411 -17.74963 1.000 19.31184  ? 89  LEU   A O   1 
ATOM   596  C CB  . LEU   A 1 82  ? -5.61209  -21.97824 -14.89754 1.000 19.30362  ? 89  LEU   A CB  1 
ATOM   597  C CG  . LEU   A 1 82  ? -6.34144  -20.64064 -14.71797 1.000 18.10594  ? 89  LEU   A CG  1 
ATOM   598  C CD1 . LEU   A 1 82  ? -7.84535  -20.90597 -14.44669 1.000 19.96209  ? 89  LEU   A CD1 1 
ATOM   599  C CD2 . LEU   A 1 82  ? -5.69542  -19.93356 -13.50795 1.000 20.23408  ? 89  LEU   A CD2 1 
ATOM   600  N N   . THR   A 1 83  ? -6.89468  -21.57226 -18.10327 1.000 18.32237  ? 90  THR   A N   1 
ATOM   601  C CA  . THR   A 1 83  ? -6.80506  -20.82426 -19.35583 1.000 18.85461  ? 90  THR   A CA  1 
ATOM   602  C C   . THR   A 1 83  ? -7.40087  -19.43107 -19.17836 1.000 20.61568  ? 90  THR   A C   1 
ATOM   603  O O   . THR   A 1 83  ? -8.52546  -19.28258 -18.66151 1.000 19.69278  ? 90  THR   A O   1 
ATOM   604  C CB  . THR   A 1 83  ? -7.52047  -21.55691 -20.49154 1.000 20.59829  ? 90  THR   A CB  1 
ATOM   605  O OG1 . THR   A 1 83  ? -6.98297  -22.87792 -20.62911 1.000 22.08499  ? 90  THR   A OG1 1 
ATOM   606  C CG2 . THR   A 1 83  ? -7.34725  -20.77221 -21.79475 1.000 20.55926  ? 90  THR   A CG2 1 
ATOM   607  N N   . ILE   A 1 84  ? -6.64204  -18.41050 -19.58701 1.000 17.67625  ? 91  ILE   A N   1 
ATOM   608  C CA  . ILE   A 1 84  ? -7.08189  -17.02152 -19.54538 1.000 16.81442  ? 91  ILE   A CA  1 
ATOM   609  C C   . ILE   A 1 84  ? -7.35615  -16.64821 -21.00526 1.000 19.27594  ? 91  ILE   A C   1 
ATOM   610  O O   . ILE   A 1 84  ? -6.43172  -16.64710 -21.83238 1.000 18.86100  ? 91  ILE   A O   1 
ATOM   611  C CB  . ILE   A 1 84  ? -6.04333  -16.07618 -18.90205 1.000 17.96195  ? 91  ILE   A CB  1 
ATOM   612  C CG1 . ILE   A 1 84  ? -5.74977  -16.38173 -17.40900 1.000 21.22909  ? 91  ILE   A CG1 1 
ATOM   613  C CG2 . ILE   A 1 84  ? -6.53771  -14.63309 -19.05560 1.000 18.64959  ? 91  ILE   A CG2 1 
ATOM   614  C CD1 . ILE   A 1 84  ? -4.84896  -17.55988 -17.17024 1.000 28.27235  ? 91  ILE   A CD1 1 
ATOM   615  N N   . VAL   A 1 85  ? -8.61782  -16.38310 -21.34438 1.000 16.65621  ? 92  VAL   A N   1 
ATOM   616  C CA  . VAL   A 1 85  ? -9.03549  -16.10546 -22.72300 1.000 17.28231  ? 92  VAL   A CA  1 
ATOM   617  C C   . VAL   A 1 85  ? -9.42418  -14.64774 -22.83069 1.000 20.07900  ? 92  VAL   A C   1 
ATOM   618  O O   . VAL   A 1 85  ? -10.17352 -14.14696 -21.98178 1.000 19.74902  ? 92  VAL   A O   1 
ATOM   619  C CB  . VAL   A 1 85  ? -10.25125 -16.95208 -23.16200 1.000 18.47740  ? 92  VAL   A CB  1 
ATOM   620  C CG1 . VAL   A 1 85  ? -10.59008 -16.63163 -24.64416 1.000 21.98521  ? 92  VAL   A CG1 1 
ATOM   621  C CG2 . VAL   A 1 85  ? -10.01744 -18.44614 -22.91749 1.000 22.65890  ? 92  VAL   A CG2 1 
ATOM   622  N N   . ASP   A 1 86  ? -8.99504  -13.97172 -23.90883 1.000 20.33002  ? 93  ASP   A N   1 
ATOM   623  C CA  . ASP   A 1 86  ? -9.53339  -12.63676 -24.16860 1.000 16.87532  ? 93  ASP   A CA  1 
ATOM   624  C C   . ASP   A 1 86  ? -9.81228  -12.48686 -25.65591 1.000 18.95218  ? 93  ASP   A C   1 
ATOM   625  O O   . ASP   A 1 86  ? -9.31467  -13.25229 -26.49558 1.000 19.73925  ? 93  ASP   A O   1 
ATOM   626  C CB  . ASP   A 1 86  ? -8.58501  -11.52941 -23.69328 1.000 17.99723  ? 93  ASP   A CB  1 
ATOM   627  C CG  . ASP   A 1 86  ? -7.27716  -11.48949 -24.47735 1.000 22.06991  ? 93  ASP   A CG  1 
ATOM   628  O OD1 . ASP   A 1 86  ? -7.27088  -11.13649 -25.66544 1.000 20.24380  ? 93  ASP   A OD1 1 
ATOM   629  O OD2 . ASP   A 1 86  ? -6.21939  -11.77019 -23.89245 1.000 19.64677  ? 93  ASP   A OD2 1 
ATOM   630  N N   . THR   A 1 87  ? -10.67377 -11.51139 -25.96758 1.000 17.80003  ? 94  THR   A N   1 
ATOM   631  C CA  . THR   A 1 87  ? -10.98697 -11.15711 -27.34678 1.000 17.73416  ? 94  THR   A CA  1 
ATOM   632  C C   . THR   A 1 87  ? -10.33113 -9.82502  -27.71181 1.000 19.83787  ? 94  THR   A C   1 
ATOM   633  O O   . THR   A 1 87  ? -10.88394 -9.00068  -28.46408 1.000 19.97687  ? 94  THR   A O   1 
ATOM   634  C CB  . THR   A 1 87  ? -12.49802 -11.10833 -27.55290 1.000 18.03201  ? 94  THR   A CB  1 
ATOM   635  O OG1 . THR   A 1 87  ? -13.08376 -10.27544 -26.54905 1.000 20.14330  ? 94  THR   A OG1 1 
ATOM   636  C CG2 . THR   A 1 87  ? -13.07942 -12.52188 -27.40734 1.000 20.52176  ? 94  THR   A CG2 1 
ATOM   637  N N   . GLY   A 1 88  ? -9.10482  -9.63632  -27.25307 1.000 18.02558  ? 95  GLY   A N   1 
ATOM   638  C CA  . GLY   A 1 88  ? -8.34679  -8.44333  -27.54443 1.000 18.42740  ? 95  GLY   A CA  1 
ATOM   639  C C   . GLY   A 1 88  ? -7.72793  -8.52318  -28.94518 1.000 18.31194  ? 95  GLY   A C   1 
ATOM   640  O O   . GLY   A 1 88  ? -8.14135  -9.28742  -29.81791 1.000 19.83091  ? 95  GLY   A O   1 
ATOM   641  N N   . ILE   A 1 89  ? -6.70501  -7.68638  -29.14062 1.000 18.61865  ? 96  ILE   A N   1 
ATOM   642  C CA  . ILE   A 1 89  ? -6.14312  -7.50939  -30.49823 1.000 18.55257  ? 96  ILE   A CA  1 
ATOM   643  C C   . ILE   A 1 89  ? -5.37697  -8.73098  -30.98973 1.000 22.01062  ? 96  ILE   A C   1 
ATOM   644  O O   . ILE   A 1 89  ? -5.19024  -8.89041  -32.20608 1.000 20.29089  ? 96  ILE   A O   1 
ATOM   645  C CB  . ILE   A 1 89  ? -5.26471  -6.23323  -30.51517 1.000 19.26980  ? 96  ILE   A CB  1 
ATOM   646  C CG1 . ILE   A 1 89  ? -4.96461  -5.80045  -31.97516 1.000 22.50687  ? 96  ILE   A CG1 1 
ATOM   647  C CG2 . ILE   A 1 89  ? -3.94130  -6.43092  -29.70645 1.000 20.04262  ? 96  ILE   A CG2 1 
ATOM   648  C CD1 . ILE   A 1 89  ? -4.60852  -4.37232  -32.09344 1.000 27.77506  ? 96  ILE   A CD1 1 
ATOM   649  N N   . GLY   A 1 90  ? -4.92885  -9.61848  -30.09636 1.000 20.69029  ? 97  GLY   A N   1 
ATOM   650  C CA  . GLY   A 1 90  ? -4.17422  -10.75694 -30.56302 1.000 20.75193  ? 97  GLY   A CA  1 
ATOM   651  C C   . GLY   A 1 90  ? -2.77166  -10.34466 -30.94896 1.000 20.55404  ? 97  GLY   A C   1 
ATOM   652  O O   . GLY   A 1 90  ? -2.30918  -9.23535  -30.68375 1.000 23.21141  ? 97  GLY   A O   1 
ATOM   653  N N   . MET   A 1 91  ? -2.05062  -11.31857 -31.47930 1.000 18.91527  ? 98  MET   A N   1 
ATOM   654  C CA  . MET   A 1 91  ? -0.66919  -11.11277 -31.91244 1.000 21.10985  ? 98  MET   A CA  1 
ATOM   655  C C   . MET   A 1 91  ? -0.42444  -11.79200 -33.23587 1.000 20.56591  ? 98  MET   A C   1 
ATOM   656  O O   . MET   A 1 91  ? -0.94636  -12.88188 -33.49589 1.000 22.16160  ? 98  MET   A O   1 
ATOM   657  C CB  . MET   A 1 91  ? 0.40356   -11.64002 -30.91567 1.000 22.29523  ? 98  MET   A CB  1 
ATOM   658  C CG  . MET   A 1 91  ? 0.27303   -11.06829 -29.53465 1.000 23.84898  ? 98  MET   A CG  1 
ATOM   659  S SD  . MET   A 1 91  ? 1.29015   -11.88524 -28.25255 1.000 25.30408  ? 98  MET   A SD  1 
ATOM   660  C CE  . MET   A 1 91  ? 0.06334   -13.04554 -27.68102 1.000 24.59973  ? 98  MET   A CE  1 
ATOM   661  N N   . THR   A 1 92  ? 0.38916   -11.13350 -34.06114 1.000 20.64410  ? 99  THR   A N   1 
ATOM   662  C CA  . THR   A 1 92  ? 0.89993   -11.75697 -35.27756 1.000 22.30706  ? 99  THR   A CA  1 
ATOM   663  C C   . THR   A 1 92  ? 1.99942   -12.77101 -34.93777 1.000 23.80769  ? 99  THR   A C   1 
ATOM   664  O O   . THR   A 1 92  ? 2.50910   -12.82695 -33.82229 1.000 24.14337  ? 99  THR   A O   1 
ATOM   665  C CB  . THR   A 1 92  ? 1.47455   -10.71879 -36.22645 1.000 29.25196  ? 99  THR   A CB  1 
ATOM   666  O OG1 . THR   A 1 92  ? 2.62554   -10.13299 -35.60625 1.000 26.17121  ? 99  THR   A OG1 1 
ATOM   667  C CG2 . THR   A 1 92  ? 0.43558   -9.62514  -36.53741 1.000 30.65303  ? 99  THR   A CG2 1 
ATOM   668  N N   . LYS   A 1 93  ? 2.32707   -13.61687 -35.91689 1.000 21.93738  ? 100 LYS   A N   1 
ATOM   669  C CA  . LYS   A 1 93  ? 3.44167   -14.54997 -35.75969 1.000 20.94705  ? 100 LYS   A CA  1 
ATOM   670  C C   . LYS   A 1 93  ? 4.71847   -13.80374 -35.41257 1.000 21.77423  ? 100 LYS   A C   1 
ATOM   671  O O   . LYS   A 1 93  ? 5.44722   -14.21272 -34.50198 1.000 21.70057  ? 100 LYS   A O   1 
ATOM   672  C CB  . LYS   A 1 93  ? 3.63021   -15.35728 -37.05094 1.000 24.15232  ? 100 LYS   A CB  1 
ATOM   673  C CG  . LYS   A 1 93  ? 4.73352   -16.41390 -36.90012 1.000 25.38478  ? 100 LYS   A CG  1 
ATOM   674  C CD  . LYS   A 1 93  ? 5.05684   -17.09409 -38.23826 1.000 26.68074  ? 100 LYS   A CD  1 
ATOM   675  C CE  . LYS   A 1 93  ? 5.87627   -18.34182 -37.95504 1.000 29.37472  ? 100 LYS   A CE  1 
ATOM   676  N NZ  . LYS   A 1 93  ? 6.53074   -18.85260 -39.17451 1.000 33.41410  ? 100 LYS   A NZ  1 
ATOM   677  N N   . ALA   A 1 94  ? 4.95827   -12.66718 -36.08000 1.000 23.34428  ? 101 ALA   A N   1 
ATOM   678  C CA  . ALA   A 1 94  ? 6.14823   -11.86986 -35.78441 1.000 24.38016  ? 101 ALA   A CA  1 
ATOM   679  C C   . ALA   A 1 94  ? 6.14415   -11.38855 -34.33850 1.000 23.58076  ? 101 ALA   A C   1 
ATOM   680  O O   . ALA   A 1 94  ? 7.18131   -11.45498 -33.66227 1.000 26.50155  ? 101 ALA   A O   1 
ATOM   681  C CB  . ALA   A 1 94  ? 6.23406   -10.68545 -36.73409 1.000 26.49865  ? 101 ALA   A CB  1 
ATOM   682  N N   . ASP   A 1 95  ? 4.98208   -10.92551 -33.85456 1.000 24.12620  ? 102 ASP   A N   1 
ATOM   683  C CA  . ASP   A 1 95  ? 4.85264   -10.51509 -32.44837 1.000 23.95493  ? 102 ASP   A CA  1 
ATOM   684  C C   . ASP   A 1 95  ? 5.17654   -11.66010 -31.51660 1.000 20.91534  ? 102 ASP   A C   1 
ATOM   685  O O   . ASP   A 1 95  ? 5.90125   -11.49715 -30.51661 1.000 22.99740  ? 102 ASP   A O   1 
ATOM   686  C CB  . ASP   A 1 95  ? 3.42152   -10.05386 -32.13071 1.000 24.32723  ? 102 ASP   A CB  1 
ATOM   687  C CG  . ASP   A 1 95  ? 3.03360   -8.74790  -32.77203 1.000 35.35505  ? 102 ASP   A CG  1 
ATOM   688  O OD1 . ASP   A 1 95  ? 3.88316   -7.83402  -32.87585 1.000 37.30045  ? 102 ASP   A OD1 1 
ATOM   689  O OD2 . ASP   A 1 95  ? 1.82367   -8.61295  -33.10285 1.000 38.78766  ? 102 ASP   A OD2 1 
ATOM   690  N N   . LEU   A 1 96  ? 4.61326   -12.84288 -31.78963 1.000 20.80949  ? 103 LEU   A N   1 
ATOM   691  C CA  . LEU   A 1 96  ? 4.86834   -13.98197 -30.91384 1.000 22.57721  ? 103 LEU   A CA  1 
ATOM   692  C C   . LEU   A 1 96  ? 6.34893   -14.24025 -30.78227 1.000 24.24353  ? 103 LEU   A C   1 
ATOM   693  O O   . LEU   A 1 96  ? 6.85686   -14.45472 -29.68270 1.000 21.99764  ? 103 LEU   A O   1 
ATOM   694  C CB  . LEU   A 1 96  ? 4.22202   -15.25336 -31.45168 1.000 25.21008  ? 103 LEU   A CB  1 
ATOM   695  C CG  . LEU   A 1 96  ? 2.76178   -15.45647 -31.20057 1.000 23.79384  ? 103 LEU   A CG  1 
ATOM   696  C CD1 . LEU   A 1 96  ? 2.30739   -16.74769 -31.90078 1.000 22.23901  ? 103 LEU   A CD1 1 
ATOM   697  C CD2 . LEU   A 1 96  ? 2.41605   -15.44599 -29.66147 1.000 20.12649  ? 103 LEU   A CD2 1 
ATOM   698  N N   . ILE   A 1 97  ? 7.04654   -14.31048 -31.91780 1.000 20.74290  ? 104 ILE   A N   1 
ATOM   699  C CA  . ILE   A 1 97  ? 8.46764   -14.60569 -31.89237 1.000 22.81138  ? 104 ILE   A CA  1 
ATOM   700  C C   . ILE   A 1 97  ? 9.21992   -13.51237 -31.14353 1.000 22.72092  ? 104 ILE   A C   1 
ATOM   701  O O   . ILE   A 1 97  ? 10.13938  -13.80210 -30.35938 1.000 24.23453  ? 104 ILE   A O   1 
ATOM   702  C CB  . ILE   A 1 97  ? 8.98316   -14.78351 -33.32939 1.000 25.05717  ? 104 ILE   A CB  1 
ATOM   703  C CG1 . ILE   A 1 97  ? 8.35116   -16.03688 -33.91323 1.000 25.83551  ? 104 ILE   A CG1 1 
ATOM   704  C CG2 . ILE   A 1 97  ? 10.53147  -14.85965 -33.35940 1.000 26.42043  ? 104 ILE   A CG2 1 
ATOM   705  C CD1 . ILE   A 1 97  ? 8.50586   -16.12999 -35.44700 1.000 25.51706  ? 104 ILE   A CD1 1 
ATOM   706  N N   . ASN   A 1 98  ? 8.81588   -12.26485 -31.34312 1.000 21.58878  ? 105 ASN   A N   1 
ATOM   707  C CA  . ASN   A 1 98  ? 9.45347   -11.10015 -30.72493 1.000 23.78598  ? 105 ASN   A CA  1 
ATOM   708  C C   . ASN   A 1 98  ? 8.90601   -10.88269 -29.30439 1.000 21.75780  ? 105 ASN   A C   1 
ATOM   709  O O   . ASN   A 1 98  ? 8.32872   -9.85203  -28.96859 1.000 21.77359  ? 105 ASN   A O   1 
ATOM   710  C CB  . ASN   A 1 98  ? 9.23556   -9.87595  -31.61315 1.000 26.46537  ? 105 ASN   A CB  1 
ATOM   711  C CG  . ASN   A 1 98  ? 10.13960  -8.69824  -31.25428 1.000 44.19056  ? 105 ASN   A CG  1 
ATOM   712  O OD1 . ASN   A 1 98  ? 11.07219  -8.81094  -30.42716 1.000 36.53006  ? 105 ASN   A OD1 1 
ATOM   713  N ND2 . ASN   A 1 98  ? 9.86655   -7.54767  -31.88447 1.000 41.18182  ? 105 ASN   A ND2 1 
ATOM   714  N N   . ASN   A 1 99  ? 9.08781   -11.91182 -28.47566 1.000 22.47384  ? 106 ASN   A N   1 
ATOM   715  C CA  . ASN   A 1 99  ? 8.69631   -11.87906 -27.05997 1.000 20.39526  ? 106 ASN   A CA  1 
ATOM   716  C C   . ASN   A 1 99  ? 7.24453   -11.47382 -26.83471 1.000 20.65915  ? 106 ASN   A C   1 
ATOM   717  O O   . ASN   A 1 99  ? 6.91463   -10.67521 -25.94721 1.000 20.28380  ? 106 ASN   A O   1 
ATOM   718  C CB  . ASN   A 1 99  ? 9.64336   -10.97297 -26.26343 1.000 19.48390  ? 106 ASN   A CB  1 
ATOM   719  C CG  . ASN   A 1 99  ? 11.08686  -11.44888 -26.37286 1.000 19.47232  ? 106 ASN   A CG  1 
ATOM   720  O OD1 . ASN   A 1 99  ? 11.37500  -12.63453 -26.14946 1.000 23.08721  ? 106 ASN   A OD1 1 
ATOM   721  N ND2 . ASN   A 1 99  ? 12.01097  -10.53402 -26.71926 1.000 24.41388  ? 106 ASN   A ND2 1 
ATOM   722  N N   . LEU   A 1 100 ? 6.34378   -12.09063 -27.59864 1.000 19.05956  ? 107 LEU   A N   1 
ATOM   723  C CA  . LEU   A 1 100 ? 4.90508   -11.87955 -27.41664 1.000 21.44892  ? 107 LEU   A CA  1 
ATOM   724  C C   . LEU   A 1 100 ? 4.54446   -10.38397 -27.42193 1.000 20.45671  ? 107 LEU   A C   1 
ATOM   725  O O   . LEU   A 1 100 ? 3.70631   -9.89654  -26.65374 1.000 20.23315  ? 107 LEU   A O   1 
ATOM   726  C CB  . LEU   A 1 100 ? 4.41166   -12.59004 -26.14290 1.000 18.24743  ? 107 LEU   A CB  1 
ATOM   727  C CG  . LEU   A 1 100 ? 4.74833   -14.09381 -26.23326 1.000 22.51700  ? 107 LEU   A CG  1 
ATOM   728  C CD1 . LEU   A 1 100 ? 5.98155   -14.45452 -25.39785 1.000 20.62981  ? 107 LEU   A CD1 1 
ATOM   729  C CD2 . LEU   A 1 100 ? 3.62072   -15.01154 -25.89460 1.000 28.81444  ? 107 LEU   A CD2 1 
ATOM   730  N N   . GLY   A 1 101 ? 5.15146   -9.64860  -28.35691 1.000 19.69287  ? 108 GLY   A N   1 
ATOM   731  C CA  . GLY   A 1 101 ? 4.81700   -8.26217  -28.56262 1.000 20.94930  ? 108 GLY   A CA  1 
ATOM   732  C C   . GLY   A 1 101 ? 5.30678   -7.28054  -27.51481 1.000 23.64443  ? 108 GLY   A C   1 
ATOM   733  O O   . GLY   A 1 101 ? 4.82104   -6.13914  -27.48117 1.000 29.19985  ? 108 GLY   A O   1 
ATOM   734  N N   . THR   A 1 102 ? 6.28715   -7.67430  -26.68904 1.000 22.44224  ? 109 THR   A N   1 
ATOM   735  C CA  . THR   A 1 102 ? 6.78338   -6.88215  -25.57007 1.000 23.01056  ? 109 THR   A CA  1 
ATOM   736  C C   . THR   A 1 102 ? 8.21866   -6.45096  -25.82313 1.000 21.93526  ? 109 THR   A C   1 
ATOM   737  O O   . THR   A 1 102 ? 8.91168   -7.00098  -26.68914 1.000 25.35127  ? 109 THR   A O   1 
ATOM   738  C CB  . THR   A 1 102 ? 6.75047   -7.66110  -24.25739 1.000 23.04874  ? 109 THR   A CB  1 
ATOM   739  O OG1 . THR   A 1 102 ? 7.75427   -8.67901  -24.27869 1.000 24.29542  ? 109 THR   A OG1 1 
ATOM   740  C CG2 . THR   A 1 102 ? 5.37539   -8.27638  -24.03447 1.000 31.71473  ? 109 THR   A CG2 1 
ATOM   741  N N   . ILE   A 1 103 ? 8.66432   -5.46772  -25.04384 1.000 20.65639  ? 110 ILE   A N   1 
ATOM   742  C CA  . ILE   A 1 103 ? 10.06640  -5.05632  -25.10571 1.000 22.03472  ? 110 ILE   A CA  1 
ATOM   743  C C   . ILE   A 1 103 ? 10.78965  -5.77043  -23.97516 1.000 24.54689  ? 110 ILE   A C   1 
ATOM   744  O O   . ILE   A 1 103 ? 11.38210  -5.15578  -23.07069 1.000 24.31774  ? 110 ILE   A O   1 
ATOM   745  C CB  . ILE   A 1 103 ? 10.22453  -3.52956  -25.05958 1.000 27.66015  ? 110 ILE   A CB  1 
ATOM   746  C CG1 . ILE   A 1 103 ? 9.49699   -2.91815  -23.88814 1.000 27.99118  ? 110 ILE   A CG1 1 
ATOM   747  C CG2 . ILE   A 1 103 ? 9.71521   -2.89428  -26.36015 1.000 29.53519  ? 110 ILE   A CG2 1 
ATOM   748  C CD1 . ILE   A 1 103 ? 9.91911   -1.45853  -23.65485 1.000 35.58788  ? 110 ILE   A CD1 1 
ATOM   749  N N   . ALA   A 1 104 ? 10.77565  -7.09579  -24.06289 1.000 22.42048  ? 111 ALA   A N   1 
ATOM   750  C CA  . ALA   A 1 104 ? 11.16337  -7.89297  -22.91591 1.000 21.05155  ? 111 ALA   A CA  1 
ATOM   751  C C   . ALA   A 1 104 ? 12.64608  -7.77808  -22.58396 1.000 22.23866  ? 111 ALA   A C   1 
ATOM   752  O O   . ALA   A 1 104 ? 12.99425  -7.90621  -21.41265 1.000 25.28827  ? 111 ALA   A O   1 
ATOM   753  C CB  . ALA   A 1 104 ? 10.77148  -9.35324  -23.14159 1.000 22.95759  ? 111 ALA   A CB  1 
ATOM   754  N N   . LYS   A 1 105 ? 13.53107  -7.52216  -23.55297 1.000 21.81395  ? 112 LYS   A N   1 
ATOM   755  C CA  . LYS   A 1 105 ? 14.95037  -7.37027  -23.21988 1.000 23.63260  ? 112 LYS   A CA  1 
ATOM   756  C C   . LYS   A 1 105 ? 15.16385  -6.16072  -22.31636 1.000 29.82937  ? 112 LYS   A C   1 
ATOM   757  O O   . LYS   A 1 105 ? 15.76783  -6.27015  -21.24980 1.000 29.35527  ? 112 LYS   A O   1 
ATOM   758  C CB  . LYS   A 1 105 ? 15.82018  -7.24210  -24.48276 1.000 25.54748  ? 112 LYS   A CB  1 
ATOM   759  C CG  . LYS   A 1 105 ? 17.29608  -7.06401  -24.19489 1.000 35.86796  ? 112 LYS   A CG  1 
ATOM   760  C CD  . LYS   A 1 105 ? 18.18092  -7.35054  -25.43591 1.000 35.65851  ? 112 LYS   A CD  1 
ATOM   761  C CE  . LYS   A 1 105 ? 19.60509  -6.87904  -25.21986 1.000 54.53078  ? 112 LYS   A CE  1 
ATOM   762  N NZ  . LYS   A 1 105 ? 20.50768  -7.14462  -26.39977 1.000 51.94558  ? 112 LYS   A NZ  1 
ATOM   763  N N   . SER   A 1 106 ? 14.66996  -4.99032  -22.72370 1.000 27.71664  ? 113 SER   A N   1 
ATOM   764  C CA  . SER   A 1 106 ? 14.88142  -3.81128  -21.90096 1.000 29.37036  ? 113 SER   A CA  1 
ATOM   765  C C   . SER   A 1 106 ? 14.02913  -3.86867  -20.64017 1.000 28.14550  ? 113 SER   A C   1 
ATOM   766  O O   . SER   A 1 106 ? 14.47248  -3.38545  -19.59500 1.000 32.30512  ? 113 SER   A O   1 
ATOM   767  C CB  . SER   A 1 106 ? 14.61093  -2.53260  -22.70521 1.000 34.90544  ? 113 SER   A CB  1 
ATOM   768  O OG  . SER   A 1 106 ? 13.27200  -2.49160  -23.15601 1.000 36.11511  ? 113 SER   A OG  1 
ATOM   769  N N   . GLY   A 1 107 ? 12.83482  -4.47257  -20.71513 1.000 26.75048  ? 114 GLY   A N   1 
ATOM   770  C CA  . GLY   A 1 107 ? 12.02308  -4.62826  -19.51438 1.000 27.54771  ? 114 GLY   A CA  1 
ATOM   771  C C   . GLY   A 1 107 ? 12.69807  -5.50353  -18.47831 1.000 32.28106  ? 114 GLY   A C   1 
ATOM   772  O O   . GLY   A 1 107 ? 12.69979  -5.19532  -17.28202 1.000 30.94102  ? 114 GLY   A O   1 
ATOM   773  N N   . THR   A 1 108 ? 13.27723  -6.61949  -18.92499 1.000 27.89989  ? 115 THR   A N   1 
ATOM   774  C CA  . THR   A 1 108 ? 14.04943  -7.46525  -18.01604 1.000 33.00447  ? 115 THR   A CA  1 
ATOM   775  C C   . THR   A 1 108 ? 15.19685  -6.70347  -17.36928 1.000 37.14302  ? 115 THR   A C   1 
ATOM   776  O O   . THR   A 1 108 ? 15.41205  -6.81889  -16.15907 1.000 33.81286  ? 115 THR   A O   1 
ATOM   777  C CB  . THR   A 1 108 ? 14.57423  -8.68244  -18.75220 1.000 34.06334  ? 115 THR   A CB  1 
ATOM   778  O OG1 . THR   A 1 108 ? 13.45234  -9.45517  -19.18561 1.000 27.22168  ? 115 THR   A OG1 1 
ATOM   779  C CG2 . THR   A 1 108 ? 15.46819  -9.50652  -17.83897 1.000 32.32338  ? 115 THR   A CG2 1 
ATOM   780  N N   . LYS   A 1 109 ? 15.96600  -5.94247  -18.15927 1.000 32.65713  ? 116 LYS   A N   1 
ATOM   781  C CA  . LYS   A 1 109 ? 17.07297  -5.16786  -17.59204 1.000 35.74721  ? 116 LYS   A CA  1 
ATOM   782  C C   . LYS   A 1 109 ? 16.57771  -4.23485  -16.48509 1.000 42.68762  ? 116 LYS   A C   1 
ATOM   783  O O   . LYS   A 1 109 ? 17.17581  -4.14448  -15.40112 1.000 42.10633  ? 116 LYS   A O   1 
ATOM   784  C CB  . LYS   A 1 109 ? 17.77765  -4.38322  -18.71361 1.000 35.02352  ? 116 LYS   A CB  1 
ATOM   785  C CG  . LYS   A 1 109 ? 18.68582  -3.22014  -18.27018 1.000 49.41374  ? 116 LYS   A CG  1 
ATOM   786  C CD  . LYS   A 1 109 ? 19.38926  -2.59949  -19.47895 1.000 56.07241  ? 116 LYS   A CD  1 
ATOM   787  C CE  . LYS   A 1 109 ? 20.68364  -1.87334  -19.10775 1.000 62.24614  ? 116 LYS   A CE  1 
ATOM   788  N NZ  . LYS   A 1 109 ? 20.88875  -1.79361  -17.64266 1.000 63.45514  ? 116 LYS   A NZ  1 
ATOM   789  N N   . ALA   A 1 110 ? 15.49899  -3.50689  -16.75382 1.000 34.13555  ? 117 ALA   A N   1 
ATOM   790  C CA  . ALA   A 1 110 ? 14.95507  -2.60410  -15.74116 1.000 39.60242  ? 117 ALA   A CA  1 
ATOM   791  C C   . ALA   A 1 110 ? 14.45867  -3.37553  -14.51493 1.000 39.01635  ? 117 ALA   A C   1 
ATOM   792  O O   . ALA   A 1 110 ? 14.69903  -2.96263  -13.37016 1.000 42.40735  ? 117 ALA   A O   1 
ATOM   793  C CB  . ALA   A 1 110 ? 13.83041  -1.76717  -16.34991 1.000 35.75660  ? 117 ALA   A CB  1 
ATOM   794  N N   . PHE   A 1 111 ? 13.75256  -4.48851  -14.73650 1.000 34.72271  ? 118 PHE   A N   1 
ATOM   795  C CA  . PHE   A 1 111 ? 13.24504  -5.30120  -13.62944 1.000 33.36150  ? 118 PHE   A CA  1 
ATOM   796  C C   . PHE   A 1 111 ? 14.38430  -5.80439  -12.74623 1.000 42.00007  ? 118 PHE   A C   1 
ATOM   797  O O   . PHE   A 1 111 ? 14.36293  -5.64923  -11.51649 1.000 41.42296  ? 118 PHE   A O   1 
ATOM   798  C CB  . PHE   A 1 111 ? 12.42056  -6.45883  -14.21300 1.000 29.36155  ? 118 PHE   A CB  1 
ATOM   799  C CG  . PHE   A 1 111 ? 11.80774  -7.39159  -13.18674 1.000 29.63229  ? 118 PHE   A CG  1 
ATOM   800  C CD1 . PHE   A 1 111 ? 11.22724  -6.91827  -12.00920 1.000 28.86235  ? 118 PHE   A CD1 1 
ATOM   801  C CD2 . PHE   A 1 111 ? 11.75291  -8.75543  -13.43866 1.000 33.85621  ? 118 PHE   A CD2 1 
ATOM   802  C CE1 . PHE   A 1 111 ? 10.63161  -7.80060  -11.10490 1.000 28.95182  ? 118 PHE   A CE1 1 
ATOM   803  C CE2 . PHE   A 1 111 ? 11.14333  -9.63314  -12.55745 1.000 32.02993  ? 118 PHE   A CE2 1 
ATOM   804  C CZ  . PHE   A 1 111 ? 10.59253  -9.14239  -11.36303 1.000 30.34787  ? 118 PHE   A CZ  1 
ATOM   805  N N   . MET   A 1 112 ? 15.42445  -6.36418  -13.35793 1.000 40.45939  ? 119 MET   A N   1 
ATOM   806  C CA  . MET   A 1 112 ? 16.44405  -6.98603  -12.52650 1.000 58.39783  ? 119 MET   A CA  1 
ATOM   807  C C   . MET   A 1 112 ? 17.29481  -5.91967  -11.83637 1.000 61.24041  ? 119 MET   A C   1 
ATOM   808  O O   . MET   A 1 112 ? 17.82272  -6.14966  -10.73815 1.000 52.73186  ? 119 MET   A O   1 
ATOM   809  C CB  . MET   A 1 112 ? 17.25034  -7.96163  -13.38256 1.000 58.04306  ? 119 MET   A CB  1 
ATOM   810  C CG  . MET   A 1 112 ? 16.77756  -9.43871  -13.20724 1.000 32.68186  ? 119 MET   A CG  1 
ATOM   811  S SD  . MET   A 1 112 ? 18.01557  -10.43986 -14.03630 1.000 85.33276  ? 119 MET   A SD  1 
ATOM   812  C CE  . MET   A 1 112 ? 17.09049  -11.70130 -14.90170 1.000 34.12449  ? 119 MET   A CE  1 
ATOM   813  N N   . GLU   A 1 113 ? 17.35546  -4.71466  -12.41128 1.000 49.25065  ? 120 GLU   A N   1 
ATOM   814  C CA  . GLU   A 1 113 ? 17.94496  -3.58309  -11.70417 1.000 61.45637  ? 120 GLU   A CA  1 
ATOM   815  C C   . GLU   A 1 113 ? 17.05745  -3.07206  -10.57629 1.000 50.21110  ? 120 GLU   A C   1 
ATOM   816  O O   . GLU   A 1 113 ? 17.54755  -2.37280  -9.67949  1.000 51.78005  ? 120 GLU   A O   1 
ATOM   817  C CB  . GLU   A 1 113 ? 18.22736  -2.44797  -12.68259 1.000 61.23053  ? 120 GLU   A CB  1 
ATOM   818  C CG  . GLU   A 1 113 ? 19.36921  -2.70210  -13.64359 1.000 68.79362  ? 120 GLU   A CG  1 
ATOM   819  C CD  . GLU   A 1 113 ? 19.48655  -1.60060  -14.68555 1.000 80.83867  ? 120 GLU   A CD  1 
ATOM   820  O OE1 . GLU   A 1 113 ? 18.64393  -0.67922  -14.67135 1.000 69.30428  ? 120 GLU   A OE1 1 
ATOM   821  O OE2 . GLU   A 1 113 ? 20.43671  -1.63453  -15.49727 1.000 88.89523  ? 120 GLU   A OE2 1 
ATOM   822  N N   . ALA   A 1 114 ? 15.77372  -3.39738  -10.59102 1.000 47.03908  ? 121 ALA   A N   1 
ATOM   823  C CA  . ALA   A 1 114 ? 14.90926  -3.01974  -9.48031  1.000 44.24685  ? 121 ALA   A CA  1 
ATOM   824  C C   . ALA   A 1 114 ? 14.96488  -4.04104  -8.36024  1.000 50.02570  ? 121 ALA   A C   1 
ATOM   825  O O   . ALA   A 1 114 ? 14.81729  -3.67285  -7.18905  1.000 54.78214  ? 121 ALA   A O   1 
ATOM   826  C CB  . ALA   A 1 114 ? 13.47398  -2.83430  -9.96527  1.000 48.98935  ? 121 ALA   A CB  1 
ATOM   827  N N   . LEU   A 1 115 ? 15.23576  -5.30718  -8.69050  1.000 47.27031  ? 122 LEU   A N   1 
ATOM   828  C CA  . LEU   A 1 115 ? 15.16996  -6.36593  -7.68721  1.000 48.23316  ? 122 LEU   A CA  1 
ATOM   829  C C   . LEU   A 1 115 ? 16.27852  -6.22326  -6.65217  1.000 59.36279  ? 122 LEU   A C   1 
ATOM   830  O O   . LEU   A 1 115 ? 16.02027  -6.23100  -5.44251  1.000 64.19180  ? 122 LEU   A O   1 
ATOM   831  C CB  . LEU   A 1 115 ? 15.23750  -7.72865  -8.36493  1.000 46.33505  ? 122 LEU   A CB  1 
ATOM   832  C CG  . LEU   A 1 115 ? 13.92327  -8.15437  -9.02008  1.000 45.44630  ? 122 LEU   A CG  1 
ATOM   833  C CD1 . LEU   A 1 115 ? 14.07766  -9.49966  -9.67016  1.000 43.47350  ? 122 LEU   A CD1 1 
ATOM   834  C CD2 . LEU   A 1 115 ? 12.79292  -8.17857  -7.96893  1.000 41.84027  ? 122 LEU   A CD2 1 
ATOM   835  N N   . GLN   A 1 116 ? 17.52221  -6.10341  -7.10285  1.000 67.44067  ? 123 GLN   A N   1 
ATOM   836  C CA  . GLN   A 1 116 ? 18.60802  -5.88542  -6.15770  1.000 63.17466  ? 123 GLN   A CA  1 
ATOM   837  C C   . GLN   A 1 116 ? 18.50189  -4.52911  -5.46268  1.000 71.61799  ? 123 GLN   A C   1 
ATOM   838  O O   . GLN   A 1 116 ? 19.26963  -4.26823  -4.53090  1.000 77.59191  ? 123 GLN   A O   1 
ATOM   839  C CB  . GLN   A 1 116 ? 19.93530  -6.00173  -6.89876  1.000 78.80852  ? 123 GLN   A CB  1 
ATOM   840  C CG  . GLN   A 1 116 ? 20.20156  -7.39564  -7.44810  1.000 68.81123  ? 123 GLN   A CG  1 
ATOM   841  C CD  . GLN   A 1 116 ? 21.67862  -7.74973  -7.44560  1.000 99.92919  ? 123 GLN   A CD  1 
ATOM   842  O OE1 . GLN   A 1 116 ? 22.53520  -6.90319  -7.17824  1.000 106.00223 ? 123 GLN   A OE1 1 
ATOM   843  N NE2 . GLN   A 1 116 ? 21.98326  -9.01099  -7.73552  1.000 95.15717  ? 123 GLN   A NE2 1 
ATOM   844  N N   . ALA   A 1 117 ? 17.56967  -3.66906  -5.89721  1.000 74.67256  ? 124 ALA   A N   1 
ATOM   845  C CA  . ALA   A 1 117 ? 17.38976  -2.31523  -5.38197  1.000 67.67608  ? 124 ALA   A CA  1 
ATOM   846  C C   . ALA   A 1 117 ? 16.06358  -2.14367  -4.63760  1.000 75.53213  ? 124 ALA   A C   1 
ATOM   847  O O   . ALA   A 1 117 ? 15.50579  -1.04223  -4.58562  1.000 67.95132  ? 124 ALA   A O   1 
ATOM   848  C CB  . ALA   A 1 117 ? 17.48928  -1.29747  -6.51663  1.000 55.65470  ? 124 ALA   A CB  1 
ATOM   849  N N   . GLY   A 1 118 ? 15.53646  -3.22459  -4.06033  1.000 60.23488  ? 125 GLY   A N   1 
ATOM   850  C CA  . GLY   A 1 118 ? 14.41327  -3.15691  -3.14278  1.000 61.13302  ? 125 GLY   A CA  1 
ATOM   851  C C   . GLY   A 1 118 ? 13.16369  -3.84350  -3.65019  1.000 56.72943  ? 125 GLY   A C   1 
ATOM   852  O O   . GLY   A 1 118 ? 12.34538  -4.30225  -2.84621  1.000 57.71532  ? 125 GLY   A O   1 
ATOM   853  N N   . ALA   A 1 119 ? 13.01051  -3.94103  -4.96489  1.000 50.42297  ? 126 ALA   A N   1 
ATOM   854  C CA  . ALA   A 1 119 ? 11.78657  -4.47700  -5.53900  1.000 42.02468  ? 126 ALA   A CA  1 
ATOM   855  C C   . ALA   A 1 119 ? 11.67674  -5.98320  -5.30530  1.000 55.73521  ? 126 ALA   A C   1 
ATOM   856  O O   . ALA   A 1 119 ? 12.65065  -6.66855  -4.98136  1.000 49.08902  ? 126 ALA   A O   1 
ATOM   857  C CB  . ALA   A 1 119 ? 11.74307  -4.16988  -7.03209  1.000 44.39442  ? 126 ALA   A CB  1 
ATOM   858  N N   . ASP   A 1 120 ? 10.45839  -6.49759  -5.46681  1.000 46.00819  ? 127 ASP   A N   1 
ATOM   859  C CA  . ASP   A 1 120 ? 10.19685  -7.92814  -5.39903  1.000 41.89980  ? 127 ASP   A CA  1 
ATOM   860  C C   . ASP   A 1 120 ? 9.45445   -8.35740  -6.64979  1.000 37.34454  ? 127 ASP   A C   1 
ATOM   861  O O   . ASP   A 1 120 ? 9.03766   -7.53274  -7.46789  1.000 39.46723  ? 127 ASP   A O   1 
ATOM   862  C CB  . ASP   A 1 120 ? 9.38093   -8.31228  -4.16639  1.000 44.32095  ? 127 ASP   A CB  1 
ATOM   863  C CG  . ASP   A 1 120 ? 8.02422   -7.66353  -4.16235  1.000 45.54097  ? 127 ASP   A CG  1 
ATOM   864  O OD1 . ASP   A 1 120 ? 7.95592   -6.44188  -3.89875  1.000 61.94395  ? 127 ASP   A OD1 1 
ATOM   865  O OD2 . ASP   A 1 120 ? 7.04783   -8.35489  -4.51080  1.000 43.71154  ? 127 ASP   A OD2 1 
ATOM   866  N N   . ILE   A 1 121 ? 9.28684   -9.67949  -6.77971  1.000 35.92932  ? 128 ILE   A N   1 
ATOM   867  C CA  . ILE   A 1 121 ? 8.75159   -10.25786 -8.00747  1.000 31.87674  ? 128 ILE   A CA  1 
ATOM   868  C C   . ILE   A 1 121 ? 7.35098   -9.74269  -8.30201  1.000 35.08486  ? 128 ILE   A C   1 
ATOM   869  O O   . ILE   A 1 121 ? 6.95061   -9.66356  -9.47281  1.000 33.26687  ? 128 ILE   A O   1 
ATOM   870  C CB  . ILE   A 1 121 ? 8.84497   -11.80189 -7.92480  1.000 33.90048  ? 128 ILE   A CB  1 
ATOM   871  C CG1 . ILE   A 1 121 ? 10.32074  -12.21366 -8.11940  1.000 42.74183  ? 128 ILE   A CG1 1 
ATOM   872  C CG2 . ILE   A 1 121 ? 7.96722   -12.51305 -8.95230  1.000 34.13617  ? 128 ILE   A CG2 1 
ATOM   873  C CD1 . ILE   A 1 121 ? 10.65108  -13.67227 -7.79273  1.000 44.63168  ? 128 ILE   A CD1 1 
ATOM   874  N N   . SER   A 1 122 ? 6.60638   -9.31839  -7.27478  1.000 39.42531  ? 129 SER   A N   1 
ATOM   875  C CA  . SER   A 1 122 ? 5.24492   -8.85646  -7.53941  1.000 35.82638  ? 129 SER   A CA  1 
ATOM   876  C C   . SER   A 1 122 ? 5.19898   -7.56991  -8.37087  1.000 42.46084  ? 129 SER   A C   1 
ATOM   877  O O   . SER   A 1 122 ? 4.14621   -7.25168  -8.92631  1.000 37.97530  ? 129 SER   A O   1 
ATOM   878  C CB  . SER   A 1 122 ? 4.47347   -8.66831  -6.22989  1.000 34.94104  ? 129 SER   A CB  1 
ATOM   879  O OG  . SER   A 1 122 ? 4.84729   -7.47591  -5.56997  1.000 38.40081  ? 129 SER   A OG  1 
ATOM   880  N N   . MET   A 1 123 ? 6.29670   -6.82725  -8.48404  1.000 33.10303  ? 130 MET   A N   1 
ATOM   881  C CA  . MET   A 1 123 ? 6.30661   -5.61308  -9.29100  1.000 32.49053  ? 130 MET   A CA  1 
ATOM   882  C C   . MET   A 1 123 ? 6.67383   -5.85899  -10.75118 1.000 29.39028  ? 130 MET   A C   1 
ATOM   883  O O   . MET   A 1 123 ? 6.80394   -4.89877  -11.52326 1.000 31.03936  ? 130 MET   A O   1 
ATOM   884  C CB  . MET   A 1 123 ? 7.20914   -4.56827  -8.62647  1.000 38.77320  ? 130 MET   A CB  1 
ATOM   885  C CG  . MET   A 1 123 ? 7.05626   -4.62948  -7.08846  1.000 38.77332  ? 130 MET   A CG  1 
ATOM   886  S SD  . MET   A 1 123 ? 8.27752   -3.69407  -6.19034  1.000 48.77121  ? 130 MET   A SD  1 
ATOM   887  C CE  . MET   A 1 123 ? 8.10807   -2.13826  -7.08298  1.000 44.46744  ? 130 MET   A CE  1 
ATOM   888  N N   . ILE   A 1 124 ? 6.72846   -7.12465  -11.17242 1.000 27.28627  ? 131 ILE   A N   1 
ATOM   889  C CA  . ILE   A 1 124 ? 7.17730   -7.47156  -12.51958 1.000 26.33528  ? 131 ILE   A CA  1 
ATOM   890  C C   . ILE   A 1 124 ? 6.37888   -6.73575  -13.60494 1.000 25.87643  ? 131 ILE   A C   1 
ATOM   891  O O   . ILE   A 1 124 ? 6.92960   -6.34892  -14.63479 1.000 23.78410  ? 131 ILE   A O   1 
ATOM   892  C CB  . ILE   A 1 124 ? 7.09262   -8.99903  -12.69521 1.000 26.20198  ? 131 ILE   A CB  1 
ATOM   893  C CG1 . ILE   A 1 124 ? 7.70726   -9.43390  -14.04294 1.000 24.93384  ? 131 ILE   A CG1 1 
ATOM   894  C CG2 . ILE   A 1 124 ? 5.63856   -9.47507  -12.51504 1.000 25.09330  ? 131 ILE   A CG2 1 
ATOM   895  C CD1 . ILE   A 1 124 ? 7.82704   -10.93497 -14.18373 1.000 25.31399  ? 131 ILE   A CD1 1 
ATOM   896  N N   . GLY   A 1 125 ? 5.08168   -6.53697  -13.40192 1.000 27.31908  ? 132 GLY   A N   1 
ATOM   897  C CA  . GLY   A 1 125 ? 4.28059   -5.90045  -14.43747 1.000 30.85813  ? 132 GLY   A CA  1 
ATOM   898  C C   . GLY   A 1 125 ? 4.63014   -4.44023  -14.69733 1.000 30.95729  ? 132 GLY   A C   1 
ATOM   899  O O   . GLY   A 1 125 ? 4.31782   -3.93255  -15.77967 1.000 32.39667  ? 132 GLY   A O   1 
ATOM   900  N N   . GLN   A 1 126 ? 5.27192   -3.77363  -13.74642 1.000 31.00833  ? 133 GLN   A N   1 
ATOM   901  C CA  . GLN   A 1 126 ? 5.72858   -2.40088  -13.97022 1.000 31.08644  ? 133 GLN   A CA  1 
ATOM   902  C C   . GLN   A 1 126 ? 6.81838   -2.32253  -15.02334 1.000 37.81279  ? 133 GLN   A C   1 
ATOM   903  O O   . GLN   A 1 126 ? 7.11773   -1.22597  -15.51256 1.000 36.44131  ? 133 GLN   A O   1 
ATOM   904  C CB  . GLN   A 1 126 ? 6.24244   -1.78056  -12.68888 1.000 35.22708  ? 133 GLN   A CB  1 
ATOM   905  C CG  . GLN   A 1 126 ? 5.17627   -1.70405  -11.63270 1.000 38.23813  ? 133 GLN   A CG  1 
ATOM   906  C CD  . GLN   A 1 126 ? 5.67998   -1.07203  -10.37210 1.000 51.78897  ? 133 GLN   A CD  1 
ATOM   907  O OE1 . GLN   A 1 126 ? 6.42578   -0.08056  -10.40570 1.000 51.64236  ? 133 GLN   A OE1 1 
ATOM   908  N NE2 . GLN   A 1 126 ? 5.27653   -1.63350  -9.23957  1.000 50.44198  ? 133 GLN   A NE2 1 
ATOM   909  N N   . PHE   A 1 127 ? 7.42300   -3.45384  -15.36392 1.000 31.09736  ? 134 PHE   A N   1 
ATOM   910  C CA  . PHE   A 1 127 ? 8.50957   -3.50753  -16.33033 1.000 30.91342  ? 134 PHE   A CA  1 
ATOM   911  C C   . PHE   A 1 127 ? 8.11006   -4.17728  -17.62796 1.000 29.93056  ? 134 PHE   A C   1 
ATOM   912  O O   . PHE   A 1 127 ? 8.97211   -4.44712  -18.46957 1.000 28.88842  ? 134 PHE   A O   1 
ATOM   913  C CB  . PHE   A 1 127 ? 9.71704   -4.19156  -15.69019 1.000 27.40866  ? 134 PHE   A CB  1 
ATOM   914  C CG  . PHE   A 1 127 ? 10.06246  -3.61442  -14.35058 1.000 32.23715  ? 134 PHE   A CG  1 
ATOM   915  C CD1 . PHE   A 1 127 ? 10.78294  -2.42768  -14.28035 1.000 41.78495  ? 134 PHE   A CD1 1 
ATOM   916  C CD2 . PHE   A 1 127 ? 9.61310   -4.18972  -13.18029 1.000 30.17696  ? 134 PHE   A CD2 1 
ATOM   917  C CE1 . PHE   A 1 127 ? 11.08019  -1.85631  -13.04802 1.000 39.07120  ? 134 PHE   A CE1 1 
ATOM   918  C CE2 . PHE   A 1 127 ? 9.90904   -3.63303  -11.96360 1.000 35.75939  ? 134 PHE   A CE2 1 
ATOM   919  C CZ  . PHE   A 1 127 ? 10.65106  -2.46365  -11.89102 1.000 41.00688  ? 134 PHE   A CZ  1 
ATOM   920  N N   . GLY   A 1 128 ? 6.82361   -4.43324  -17.82375 1.000 26.58182  ? 135 GLY   A N   1 
ATOM   921  C CA  . GLY   A 1 128 ? 6.37772   -4.89217  -19.10713 1.000 25.81702  ? 135 GLY   A CA  1 
ATOM   922  C C   . GLY   A 1 128 ? 6.64700   -6.34592  -19.39706 1.000 23.05235  ? 135 GLY   A C   1 
ATOM   923  O O   . GLY   A 1 128 ? 6.54547   -6.74582  -20.56015 1.000 25.87803  ? 135 GLY   A O   1 
ATOM   924  N N   . VAL   A 1 129 ? 6.97649   -7.15155  -18.37813 1.000 21.46653  ? 136 VAL   A N   1 
ATOM   925  C CA  . VAL   A 1 129 ? 7.31268   -8.55696  -18.58911 1.000 18.11768  ? 136 VAL   A CA  1 
ATOM   926  C C   . VAL   A 1 129 ? 6.47190   -9.43380  -17.65503 1.000 21.58962  ? 136 VAL   A C   1 
ATOM   927  O O   . VAL   A 1 129 ? 6.84123   -10.57125 -17.34769 1.000 20.41124  ? 136 VAL   A O   1 
ATOM   928  C CB  . VAL   A 1 129 ? 8.82699   -8.79902  -18.42786 1.000 19.88992  ? 136 VAL   A CB  1 
ATOM   929  C CG1 . VAL   A 1 129 ? 9.59912   -8.21388  -19.63264 1.000 22.92297  ? 136 VAL   A CG1 1 
ATOM   930  C CG2 . VAL   A 1 129 ? 9.35693   -8.19520  -17.16166 1.000 22.38736  ? 136 VAL   A CG2 1 
ATOM   931  N N   . GLY   A 1 130 ? 5.29363   -8.93944  -17.27538 1.000 20.22195  ? 137 GLY   A N   1 
ATOM   932  C CA  . GLY   A 1 130 ? 4.40827   -9.71362  -16.41701 1.000 20.91634  ? 137 GLY   A CA  1 
ATOM   933  C C   . GLY   A 1 130 ? 3.96904   -11.04972 -16.98228 1.000 20.59905  ? 137 GLY   A C   1 
ATOM   934  O O   . GLY   A 1 130 ? 3.68129   -11.97029 -16.19814 1.000 20.59066  ? 137 GLY   A O   1 
ATOM   935  N N   . PHE   A 1 131 ? 3.96103   -11.21258 -18.31954 1.000 17.97972  ? 138 PHE   A N   1 
ATOM   936  C CA  . PHE   A 1 131 ? 3.59237   -12.51038 -18.86175 1.000 18.30853  ? 138 PHE   A CA  1 
ATOM   937  C C   . PHE   A 1 131 ? 4.40971   -13.64610 -18.24445 1.000 18.96256  ? 138 PHE   A C   1 
ATOM   938  O O   . PHE   A 1 131 ? 3.86549   -14.72243 -17.96100 1.000 18.55480  ? 138 PHE   A O   1 
ATOM   939  C CB  . PHE   A 1 131 ? 3.77073   -12.51411 -20.38305 1.000 19.46411  ? 138 PHE   A CB  1 
ATOM   940  C CG  . PHE   A 1 131 ? 3.75226   -13.87822 -20.96422 1.000 18.27186  ? 138 PHE   A CG  1 
ATOM   941  C CD1 . PHE   A 1 131 ? 2.55646   -14.59115 -21.07471 1.000 19.07835  ? 138 PHE   A CD1 1 
ATOM   942  C CD2 . PHE   A 1 131 ? 4.95182   -14.47773 -21.39816 1.000 19.44727  ? 138 PHE   A CD2 1 
ATOM   943  C CE1 . PHE   A 1 131 ? 2.51911   -15.90072 -21.59742 1.000 15.95489  ? 138 PHE   A CE1 1 
ATOM   944  C CE2 . PHE   A 1 131 ? 4.91589   -15.78413 -21.94872 1.000 19.01558  ? 138 PHE   A CE2 1 
ATOM   945  C CZ  . PHE   A 1 131 ? 3.69014   -16.48629 -22.04626 1.000 19.74919  ? 138 PHE   A CZ  1 
ATOM   946  N N   . TYR   A 1 132 ? 5.72982   -13.43560 -18.06576 1.000 18.74271  ? 139 TYR   A N   1 
ATOM   947  C CA  . TYR   A 1 132 ? 6.62236   -14.50434 -17.62437 1.000 18.55952  ? 139 TYR   A CA  1 
ATOM   948  C C   . TYR   A 1 132 ? 6.35278   -14.93396 -16.18336 1.000 17.40079  ? 139 TYR   A C   1 
ATOM   949  O O   . TYR   A 1 132 ? 6.78934   -16.02282 -15.79641 1.000 19.92523  ? 139 TYR   A O   1 
ATOM   950  C CB  . TYR   A 1 132 ? 8.10530   -14.08144 -17.82285 1.000 18.62470  ? 139 TYR   A CB  1 
ATOM   951  C CG  . TYR   A 1 132 ? 8.36326   -13.81909 -19.30018 1.000 18.21429  ? 139 TYR   A CG  1 
ATOM   952  C CD1 . TYR   A 1 132 ? 8.59537   -14.86975 -20.19598 1.000 17.90034  ? 139 TYR   A CD1 1 
ATOM   953  C CD2 . TYR   A 1 132 ? 8.33306   -12.51863 -19.79790 1.000 20.79589  ? 139 TYR   A CD2 1 
ATOM   954  C CE1 . TYR   A 1 132 ? 8.77523   -14.59784 -21.58542 1.000 16.76394  ? 139 TYR   A CE1 1 
ATOM   955  C CE2 . TYR   A 1 132 ? 8.50589   -12.24930 -21.15030 1.000 22.58477  ? 139 TYR   A CE2 1 
ATOM   956  C CZ  . TYR   A 1 132 ? 8.73366   -13.28127 -22.03596 1.000 20.07843  ? 139 TYR   A CZ  1 
ATOM   957  O OH  . TYR   A 1 132 ? 8.89414   -12.96070 -23.36574 1.000 21.12497  ? 139 TYR   A OH  1 
ATOM   958  N N   . SER   A 1 133 ? 5.58541   -14.16151 -15.42308 1.000 18.49532  ? 140 SER   A N   1 
ATOM   959  C CA  . SER   A 1 133 ? 5.12242   -14.63055 -14.12092 1.000 19.05488  ? 140 SER   A CA  1 
ATOM   960  C C   . SER   A 1 133 ? 4.24340   -15.87204 -14.21139 1.000 19.22336  ? 140 SER   A C   1 
ATOM   961  O O   . SER   A 1 133 ? 4.03689   -16.54149 -13.18196 1.000 19.72777  ? 140 SER   A O   1 
ATOM   962  C CB  . SER   A 1 133 ? 4.38465   -13.49985 -13.37852 1.000 22.04438  ? 140 SER   A CB  1 
ATOM   963  O OG  . SER   A 1 133 ? 3.07457   -13.26283 -13.89495 1.000 20.70475  ? 140 SER   A OG  1 
ATOM   964  N N   . ALA   A 1 134 ? 3.73865   -16.19986 -15.41697 1.000 19.69425  ? 141 ALA   A N   1 
ATOM   965  C CA  . ALA   A 1 134 ? 3.04807   -17.48104 -15.58005 1.000 18.98229  ? 141 ALA   A CA  1 
ATOM   966  C C   . ALA   A 1 134 ? 3.87269   -18.63662 -15.03388 1.000 19.11801  ? 141 ALA   A C   1 
ATOM   967  O O   . ALA   A 1 134 ? 3.30838   -19.62168 -14.53008 1.000 19.59091  ? 141 ALA   A O   1 
ATOM   968  C CB  . ALA   A 1 134 ? 2.73141   -17.73375 -17.05876 1.000 16.85822  ? 141 ALA   A CB  1 
ATOM   969  N N   . TYR   A 1 135 ? 5.21796   -18.55298 -15.15193 1.000 18.27674  ? 142 TYR   A N   1 
ATOM   970  C CA  . TYR   A 1 135 ? 6.07853   -19.66333 -14.75909 1.000 19.36594  ? 142 TYR   A CA  1 
ATOM   971  C C   . TYR   A 1 135 ? 6.25432   -19.75940 -13.23277 1.000 20.52484  ? 142 TYR   A C   1 
ATOM   972  O O   . TYR   A 1 135 ? 6.92539   -20.67595 -12.75053 1.000 22.69108  ? 142 TYR   A O   1 
ATOM   973  C CB  . TYR   A 1 135 ? 7.42828   -19.56509 -15.50915 1.000 17.85757  ? 142 TYR   A CB  1 
ATOM   974  C CG  . TYR   A 1 135 ? 7.22326   -19.87646 -16.98538 1.000 18.25176  ? 142 TYR   A CG  1 
ATOM   975  C CD1 . TYR   A 1 135 ? 7.19301   -21.20212 -17.44459 1.000 20.20915  ? 142 TYR   A CD1 1 
ATOM   976  C CD2 . TYR   A 1 135 ? 6.97284   -18.84513 -17.90114 1.000 17.90188  ? 142 TYR   A CD2 1 
ATOM   977  C CE1 . TYR   A 1 135 ? 6.95901   -21.48777 -18.79735 1.000 19.92326  ? 142 TYR   A CE1 1 
ATOM   978  C CE2 . TYR   A 1 135 ? 6.72195   -19.12306 -19.24758 1.000 18.40980  ? 142 TYR   A CE2 1 
ATOM   979  C CZ  . TYR   A 1 135 ? 6.71253   -20.44059 -19.67578 1.000 19.53554  ? 142 TYR   A CZ  1 
ATOM   980  O OH  . TYR   A 1 135 ? 6.46571   -20.69894 -21.01345 1.000 18.74663  ? 142 TYR   A OH  1 
ATOM   981  N N   . LEU   A 1 136 ? 5.58953   -18.88686 -12.46927 1.000 20.86917  ? 143 LEU   A N   1 
ATOM   982  C CA  . LEU   A 1 136 ? 5.45805   -19.11866 -11.03188 1.000 21.25474  ? 143 LEU   A CA  1 
ATOM   983  C C   . LEU   A 1 136 ? 4.59728   -20.34061 -10.74658 1.000 21.74571  ? 143 LEU   A C   1 
ATOM   984  O O   . LEU   A 1 136 ? 4.81357   -21.04100 -9.75503  1.000 24.22499  ? 143 LEU   A O   1 
ATOM   985  C CB  . LEU   A 1 136 ? 4.82249   -17.89953 -10.35759 1.000 22.89149  ? 143 LEU   A CB  1 
ATOM   986  C CG  . LEU   A 1 136 ? 5.65270   -16.60316 -10.33732 1.000 22.65339  ? 143 LEU   A CG  1 
ATOM   987  C CD1 . LEU   A 1 136 ? 4.80925   -15.43809 -9.91300  1.000 22.07133  ? 143 LEU   A CD1 1 
ATOM   988  C CD2 . LEU   A 1 136 ? 6.89890   -16.75664 -9.47449  1.000 24.42455  ? 143 LEU   A CD2 1 
ATOM   989  N N   . VAL   A 1 137 ? 3.63878   -20.63646 -11.64056 1.000 21.77093  ? 144 VAL   A N   1 
ATOM   990  C CA  . VAL   A 1 137 ? 2.65924   -21.67220 -11.33000 1.000 23.89745  ? 144 VAL   A CA  1 
ATOM   991  C C   . VAL   A 1 137 ? 2.58875   -22.73178 -12.42544 1.000 23.39122  ? 144 VAL   A C   1 
ATOM   992  O O   . VAL   A 1 137 ? 2.04780   -23.81624 -12.18154 1.000 24.78501  ? 144 VAL   A O   1 
ATOM   993  C CB  . VAL   A 1 137 ? 1.25222   -21.09147 -11.06717 1.000 22.47615  ? 144 VAL   A CB  1 
ATOM   994  C CG1 . VAL   A 1 137 ? 1.25001   -20.20057 -9.80247  1.000 22.51901  ? 144 VAL   A CG1 1 
ATOM   995  C CG2 . VAL   A 1 137 ? 0.70537   -20.31250 -12.26469 1.000 22.55590  ? 144 VAL   A CG2 1 
ATOM   996  N N   . ALA   A 1 138 ? 3.14477   -22.45443 -13.60507 1.000 23.03817  ? 145 ALA   A N   1 
ATOM   997  C CA  . ALA   A 1 138 ? 2.97859   -23.34318 -14.76226 1.000 21.60569  ? 145 ALA   A CA  1 
ATOM   998  C C   . ALA   A 1 138 ? 4.29599   -23.99338 -15.12991 1.000 22.55105  ? 145 ALA   A C   1 
ATOM   999  O O   . ALA   A 1 138 ? 5.33123   -23.31577 -15.18038 1.000 25.19361  ? 145 ALA   A O   1 
ATOM   1000 C CB  . ALA   A 1 138 ? 2.43005   -22.59189 -15.98440 1.000 21.10833  ? 145 ALA   A CB  1 
ATOM   1001 N N   . GLU   A 1 139 ? 4.24948   -25.30482 -15.39000 1.000 22.08570  ? 146 GLU   A N   1 
ATOM   1002 C CA  . GLU   A 1 139 ? 5.41224   -25.99102 -15.95193 1.000 23.48992  ? 146 GLU   A CA  1 
ATOM   1003 C C   . GLU   A 1 139 ? 5.50531   -25.78537 -17.45679 1.000 23.16930  ? 146 GLU   A C   1 
ATOM   1004 O O   . GLU   A 1 139 ? 6.60212   -25.87037 -18.01779 1.000 24.56083  ? 146 GLU   A O   1 
ATOM   1005 C CB  . GLU   A 1 139 ? 5.35265   -27.47975 -15.61698 1.000 26.25801  ? 146 GLU   A CB  1 
ATOM   1006 C CG  . GLU   A 1 139 ? 4.24163   -28.24717 -16.26840 1.000 34.32882  ? 146 GLU   A CG  1 
ATOM   1007 C CD  . GLU   A 1 139 ? 4.08205   -29.66369 -15.70134 1.000 58.13046  ? 146 GLU   A CD  1 
ATOM   1008 O OE1 . GLU   A 1 139 ? 4.70487   -29.97965 -14.66044 1.000 51.44533  ? 146 GLU   A OE1 1 
ATOM   1009 O OE2 . GLU   A 1 139 ? 3.33337   -30.46488 -16.31266 1.000 51.33986  ? 146 GLU   A OE2 1 
ATOM   1010 N N   . LYS   A 1 140 ? 4.38808   -25.47925 -18.10746 1.000 20.51146  ? 147 LYS   A N   1 
ATOM   1011 C CA  . LYS   A 1 140 ? 4.36401   -25.28243 -19.54830 1.000 19.66006  ? 147 LYS   A CA  1 
ATOM   1012 C C   . LYS   A 1 140 ? 3.30013   -24.22406 -19.79281 1.000 20.01145  ? 147 LYS   A C   1 
ATOM   1013 O O   . LYS   A 1 140 ? 2.30188   -24.18993 -19.07021 1.000 20.66174  ? 147 LYS   A O   1 
ATOM   1014 C CB  . LYS   A 1 140 ? 4.03380   -26.58294 -20.28830 1.000 20.34172  ? 147 LYS   A CB  1 
ATOM   1015 C CG  . LYS   A 1 140 ? 3.96223   -26.42193 -21.80159 1.000 21.93059  ? 147 LYS   A CG  1 
ATOM   1016 C CD  . LYS   A 1 140 ? 3.93640   -27.79427 -22.44095 1.000 25.48427  ? 147 LYS   A CD  1 
ATOM   1017 C CE  . LYS   A 1 140 ? 2.52777   -28.27276 -22.60186 1.000 30.39718  ? 147 LYS   A CE  1 
ATOM   1018 N NZ  . LYS   A 1 140 ? 2.44568   -29.67269 -23.15521 1.000 37.30378  ? 147 LYS   A NZ  1 
ATOM   1019 N N   . VAL   A 1 141 ? 3.53796   -23.32728 -20.73868 1.000 16.73100  ? 148 VAL   A N   1 
ATOM   1020 C CA  . VAL   A 1 141 ? 2.54212   -22.32906 -21.11239 1.000 16.75050  ? 148 VAL   A CA  1 
ATOM   1021 C C   . VAL   A 1 141 ? 2.33848   -22.42536 -22.61415 1.000 19.94740  ? 148 VAL   A C   1 
ATOM   1022 O O   . VAL   A 1 141 ? 3.31505   -22.44348 -23.37074 1.000 19.77068  ? 148 VAL   A O   1 
ATOM   1023 C CB  . VAL   A 1 141 ? 2.98239   -20.91374 -20.72590 1.000 18.04278  ? 148 VAL   A CB  1 
ATOM   1024 C CG1 . VAL   A 1 141 ? 1.94268   -19.86951 -21.22037 1.000 18.97766  ? 148 VAL   A CG1 1 
ATOM   1025 C CG2 . VAL   A 1 141 ? 3.21587   -20.81391 -19.15072 1.000 18.00564  ? 148 VAL   A CG2 1 
ATOM   1026 N N   . THR   A 1 142 ? 1.07688   -22.48043 -23.03753 1.000 18.04588  ? 149 THR   A N   1 
ATOM   1027 C CA  . THR   A 1 142 ? 0.71661   -22.45274 -24.45721 1.000 20.25565  ? 149 THR   A CA  1 
ATOM   1028 C C   . THR   A 1 142 ? -0.05350  -21.16211 -24.71140 1.000 22.19492  ? 149 THR   A C   1 
ATOM   1029 O O   . THR   A 1 142 ? -0.98348  -20.83086 -23.96818 1.000 21.03705  ? 149 THR   A O   1 
ATOM   1030 C CB  . THR   A 1 142 ? -0.13271  -23.65867 -24.85498 1.000 18.76835  ? 149 THR   A CB  1 
ATOM   1031 O OG1 . THR   A 1 142 ? 0.49814   -24.86839 -24.42990 1.000 23.69163  ? 149 THR   A OG1 1 
ATOM   1032 C CG2 . THR   A 1 142 ? -0.31950  -23.69855 -26.38072 1.000 20.66819  ? 149 THR   A CG2 1 
ATOM   1033 N N   . VAL   A 1 143 ? 0.30374   -20.44103 -25.76900 1.000 17.97714  ? 150 VAL   A N   1 
ATOM   1034 C CA  . VAL   A 1 143 ? -0.36164  -19.18442 -26.10830 1.000 17.84012  ? 150 VAL   A CA  1 
ATOM   1035 C C   . VAL   A 1 143 ? -0.94596  -19.35716 -27.49761 1.000 22.05649  ? 150 VAL   A C   1 
ATOM   1036 O O   . VAL   A 1 143 ? -0.18736  -19.52533 -28.46779 1.000 20.64626  ? 150 VAL   A O   1 
ATOM   1037 C CB  . VAL   A 1 143 ? 0.60010   -17.99403 -26.06572 1.000 18.02750  ? 150 VAL   A CB  1 
ATOM   1038 C CG1 . VAL   A 1 143 ? -0.14173  -16.72839 -26.51366 1.000 19.88693  ? 150 VAL   A CG1 1 
ATOM   1039 C CG2 . VAL   A 1 143 ? 1.14776   -17.76671 -24.63749 1.000 18.15656  ? 150 VAL   A CG2 1 
ATOM   1040 N N   . ILE   A 1 144 ? -2.27208  -19.35864 -27.60005 1.000 17.69269  ? 151 ILE   A N   1 
ATOM   1041 C CA  . ILE   A 1 144 ? -2.94830  -19.47724 -28.89530 1.000 18.76045  ? 151 ILE   A CA  1 
ATOM   1042 C C   . ILE   A 1 144 ? -3.45599  -18.09072 -29.23539 1.000 19.91941  ? 151 ILE   A C   1 
ATOM   1043 O O   . ILE   A 1 144 ? -4.12878  -17.47325 -28.41150 1.000 20.51619  ? 151 ILE   A O   1 
ATOM   1044 C CB  . ILE   A 1 144 ? -4.12979  -20.46013 -28.86378 1.000 20.73472  ? 151 ILE   A CB  1 
ATOM   1045 C CG1 . ILE   A 1 144 ? -3.80206  -21.77085 -28.15332 1.000 30.58853  ? 151 ILE   A CG1 1 
ATOM   1046 C CG2 . ILE   A 1 144 ? -4.69150  -20.65536 -30.29808 1.000 22.63291  ? 151 ILE   A CG2 1 
ATOM   1047 C CD1 . ILE   A 1 144 ? -2.94708  -22.65279 -28.90510 1.000 30.30692  ? 151 ILE   A CD1 1 
ATOM   1048 N N   . THR   A 1 145 ? -3.16515  -17.59365 -30.42842 1.000 18.34480  ? 152 THR   A N   1 
ATOM   1049 C CA  . THR   A 1 145 ? -3.54685  -16.20967 -30.70547 1.000 19.67228  ? 152 THR   A CA  1 
ATOM   1050 C C   . THR   A 1 145 ? -3.98257  -16.03342 -32.15322 1.000 20.09986  ? 152 THR   A C   1 
ATOM   1051 O O   . THR   A 1 145 ? -3.53088  -16.73979 -33.07180 1.000 21.00666  ? 152 THR   A O   1 
ATOM   1052 C CB  . THR   A 1 145 ? -2.38635  -15.24704 -30.34203 1.000 19.12288  ? 152 THR   A CB  1 
ATOM   1053 O OG1 . THR   A 1 145 ? -2.85420  -13.88868 -30.32337 1.000 20.38493  ? 152 THR   A OG1 1 
ATOM   1054 C CG2 . THR   A 1 145 ? -1.18825  -15.41067 -31.30166 1.000 20.85012  ? 152 THR   A CG2 1 
ATOM   1055 N N   . LYS   A 1 146 ? -4.89730  -15.07423 -32.33996 1.000 19.12540  ? 153 LYS   A N   1 
ATOM   1056 C CA  . LYS   A 1 146 ? -5.33903  -14.69562 -33.68124 1.000 21.08292  ? 153 LYS   A CA  1 
ATOM   1057 C C   . LYS   A 1 146 ? -5.45481  -13.18262 -33.74505 1.000 22.84552  ? 153 LYS   A C   1 
ATOM   1058 O O   . LYS   A 1 146 ? -6.24485  -12.58974 -32.99539 1.000 20.87496  ? 153 LYS   A O   1 
ATOM   1059 C CB  . LYS   A 1 146 ? -6.68480  -15.34078 -33.99173 1.000 20.23534  ? 153 LYS   A CB  1 
ATOM   1060 C CG  . LYS   A 1 146 ? -7.35361  -14.91848 -35.32338 1.000 24.83170  ? 153 LYS   A CG  1 
ATOM   1061 C CD  . LYS   A 1 146 ? -6.56848  -15.43853 -36.54563 1.000 25.61726  ? 153 LYS   A CD  1 
ATOM   1062 C CE  . LYS   A 1 146 ? -7.29896  -15.12821 -37.82350 1.000 28.59496  ? 153 LYS   A CE  1 
ATOM   1063 N NZ  . LYS   A 1 146 ? -7.20950  -13.69092 -38.18755 1.000 27.89615  ? 153 LYS   A NZ  1 
ATOM   1064 N N   . HIS   A 1 147 ? -4.68445  -12.57779 -34.63535 1.000 22.27447  ? 154 HIS   A N   1 
ATOM   1065 C CA  . HIS   A 1 147 ? -4.69905  -11.14996 -34.92328 1.000 19.91007  ? 154 HIS   A CA  1 
ATOM   1066 C C   . HIS   A 1 147 ? -5.40288  -10.94037 -36.25980 1.000 21.78482  ? 154 HIS   A C   1 
ATOM   1067 O O   . HIS   A 1 147 ? -5.30006  -11.77971 -37.15904 1.000 25.26051  ? 154 HIS   A O   1 
ATOM   1068 C CB  . HIS   A 1 147 ? -3.25344  -10.63461 -34.95959 1.000 23.11836  ? 154 HIS   A CB  1 
ATOM   1069 C CG  . HIS   A 1 147 ? -3.11517  -9.14930  -35.08629 1.000 21.05012  ? 154 HIS   A CG  1 
ATOM   1070 N ND1 . HIS   A 1 147 ? -3.33608  -8.47193  -36.26350 1.000 24.30363  ? 154 HIS   A ND1 1 
ATOM   1071 C CD2 . HIS   A 1 147 ? -2.77919  -8.21291  -34.16666 1.000 22.87794  ? 154 HIS   A CD2 1 
ATOM   1072 C CE1 . HIS   A 1 147 ? -3.12718  -7.18177  -36.07121 1.000 29.01007  ? 154 HIS   A CE1 1 
ATOM   1073 N NE2 . HIS   A 1 147 ? -2.78543  -7.00144  -34.80563 1.000 24.08841  ? 154 HIS   A NE2 1 
ATOM   1074 N N   . ASN   A 1 148 ? -6.14522  -9.83115  -36.39449 1.000 22.48858  ? 155 ASN   A N   1 
ATOM   1075 C CA  . ASN   A 1 148 ? -6.84765  -9.57009  -37.65587 1.000 23.03827  ? 155 ASN   A CA  1 
ATOM   1076 C C   . ASN   A 1 148 ? -5.92897  -9.67687  -38.87123 1.000 27.96869  ? 155 ASN   A C   1 
ATOM   1077 O O   . ASN   A 1 148 ? -6.37955  -10.01022 -39.97245 1.000 30.34900  ? 155 ASN   A O   1 
ATOM   1078 C CB  . ASN   A 1 148 ? -7.48059  -8.17399  -37.63711 1.000 26.08001  ? 155 ASN   A CB  1 
ATOM   1079 C CG  . ASN   A 1 148 ? -8.77611  -8.11609  -36.85329 1.000 29.89002  ? 155 ASN   A CG  1 
ATOM   1080 O OD1 . ASN   A 1 148 ? -9.46554  -9.11787  -36.68940 1.000 32.25630  ? 155 ASN   A OD1 1 
ATOM   1081 N ND2 . ASN   A 1 148 ? -9.09477  -6.92781  -36.32675 1.000 28.06627  ? 155 ASN   A ND2 1 
ATOM   1082 N N   . ASP   A 1 149 ? -4.63971  -9.39892  -38.70801 1.000 30.21507  ? 156 ASP   A N   1 
ATOM   1083 C CA  . ASP   A 1 149 ? -3.77045  -9.32667  -39.87711 1.000 28.24427  ? 156 ASP   A CA  1 
ATOM   1084 C C   . ASP   A 1 149 ? -2.97795  -10.60379 -40.11025 1.000 33.43816  ? 156 ASP   A C   1 
ATOM   1085 O O   . ASP   A 1 149 ? -2.08468  -10.60034 -40.96410 1.000 35.64935  ? 156 ASP   A O   1 
ATOM   1086 C CB  . ASP   A 1 149 ? -2.81044  -8.14262  -39.74733 1.000 33.82299  ? 156 ASP   A CB  1 
ATOM   1087 C CG  . ASP   A 1 149 ? -3.53100  -6.80302  -39.74231 1.000 40.88081  ? 156 ASP   A CG  1 
ATOM   1088 O OD1 . ASP   A 1 149 ? -4.70107  -6.75501  -40.15516 1.000 38.04368  ? 156 ASP   A OD1 1 
ATOM   1089 O OD2 . ASP   A 1 149 ? -2.93699  -5.80756  -39.28902 1.000 38.37264  ? 156 ASP   A OD2 1 
ATOM   1090 N N   . ASP   A 1 150 ? -3.27742  -11.69379 -39.39638 1.000 27.99415  ? 157 ASP   A N   1 
ATOM   1091 C CA  . ASP   A 1 150 ? -2.46067  -12.90278 -39.53023 1.000 25.60737  ? 157 ASP   A CA  1 
ATOM   1092 C C   . ASP   A 1 150 ? -3.33019  -14.13050 -39.26463 1.000 33.28931  ? 157 ASP   A C   1 
ATOM   1093 O O   . ASP   A 1 150 ? -4.52453  -14.02540 -38.96642 1.000 29.93653  ? 157 ASP   A O   1 
ATOM   1094 C CB  . ASP   A 1 150 ? -1.23628  -12.84616 -38.58939 1.000 26.80189  ? 157 ASP   A CB  1 
ATOM   1095 C CG  . ASP   A 1 150 ? -0.02624  -13.65895 -39.10147 1.000 30.35750  ? 157 ASP   A CG  1 
ATOM   1096 O OD1 . ASP   A 1 150 ? -0.13485  -14.42637 -40.08693 1.000 32.01365  ? 157 ASP   A OD1 1 
ATOM   1097 O OD2 . ASP   A 1 150 ? 1.07674   -13.48948 -38.54069 1.000 28.55159  ? 157 ASP   A OD2 1 
ATOM   1098 N N   . GLU   A 1 151 ? -2.72059  -15.31100 -39.38464 1.000 29.02530  ? 158 GLU   A N   1 
ATOM   1099 C CA  . GLU   A 1 151 ? -3.42921  -16.55800 -39.15127 1.000 30.84509  ? 158 GLU   A CA  1 
ATOM   1100 C C   . GLU   A 1 151 ? -3.29610  -16.95223 -37.67760 1.000 24.27922  ? 158 GLU   A C   1 
ATOM   1101 O O   . GLU   A 1 151 ? -2.60397  -16.30205 -36.89220 1.000 25.91619  ? 158 GLU   A O   1 
ATOM   1102 C CB  . GLU   A 1 151 ? -2.89092  -17.65327 -40.06654 1.000 33.98627  ? 158 GLU   A CB  1 
ATOM   1103 C CG  . GLU   A 1 151 ? -3.12233  -17.39080 -41.54317 1.000 40.47653  ? 158 GLU   A CG  1 
ATOM   1104 C CD  . GLU   A 1 151 ? -4.52102  -16.86553 -41.85479 1.000 60.23601  ? 158 GLU   A CD  1 
ATOM   1105 O OE1 . GLU   A 1 151 ? -4.62782  -15.84927 -42.58005 1.000 71.18849  ? 158 GLU   A OE1 1 
ATOM   1106 O OE2 . GLU   A 1 151 ? -5.51838  -17.45614 -41.37588 1.000 60.52668  ? 158 GLU   A OE2 1 
ATOM   1107 N N   . GLN   A 1 152 ? -3.97848  -18.02012 -37.28126 1.000 26.60917  ? 159 GLN   A N   1 
ATOM   1108 C CA  . GLN   A 1 152 ? -3.96229  -18.44679 -35.89096 1.000 25.58909  ? 159 GLN   A CA  1 
ATOM   1109 C C   . GLN   A 1 152 ? -2.70486  -19.26964 -35.59715 1.000 23.50141  ? 159 GLN   A C   1 
ATOM   1110 O O   . GLN   A 1 152 ? -2.40237  -20.23317 -36.31049 1.000 25.57817  ? 159 GLN   A O   1 
ATOM   1111 C CB  . GLN   A 1 152 ? -5.21058  -19.25990 -35.55809 1.000 24.54804  ? 159 GLN   A CB  1 
ATOM   1112 C CG  . GLN   A 1 152 ? -5.42869  -19.50317 -34.05269 1.000 24.93626  ? 159 GLN   A CG  1 
ATOM   1113 C CD  . GLN   A 1 152 ? -6.85593  -19.94804 -33.77058 1.000 31.63492  ? 159 GLN   A CD  1 
ATOM   1114 O OE1 . GLN   A 1 152 ? -7.79034  -19.26116 -34.14577 1.000 33.56366  ? 159 GLN   A OE1 1 
ATOM   1115 N NE2 . GLN   A 1 152 ? -7.02654  -21.09315 -33.11419 1.000 31.33940  ? 159 GLN   A NE2 1 
ATOM   1116 N N   . TYR   A 1 153 ? -1.99614  -18.89301 -34.54237 1.000 20.98007  ? 160 TYR   A N   1 
ATOM   1117 C CA  . TYR   A 1 153 ? -0.72871  -19.50513 -34.18122 1.000 22.24651  ? 160 TYR   A CA  1 
ATOM   1118 C C   . TYR   A 1 153 ? -0.75336  -19.98298 -32.73728 1.000 22.14176  ? 160 TYR   A C   1 
ATOM   1119 O O   . TYR   A 1 153 ? -1.45025  -19.40739 -31.88787 1.000 21.80086  ? 160 TYR   A O   1 
ATOM   1120 C CB  . TYR   A 1 153 ? 0.43177   -18.51241 -34.34567 1.000 23.30595  ? 160 TYR   A CB  1 
ATOM   1121 C CG  . TYR   A 1 153 ? 0.84151   -18.37498 -35.78223 1.000 26.09078  ? 160 TYR   A CG  1 
ATOM   1122 C CD1 . TYR   A 1 153 ? 1.65433   -19.31961 -36.36082 1.000 25.62067  ? 160 TYR   A CD1 1 
ATOM   1123 C CD2 . TYR   A 1 153 ? 0.35297   -17.34448 -36.58294 1.000 29.36691  ? 160 TYR   A CD2 1 
ATOM   1124 C CE1 . TYR   A 1 153 ? 2.03346   -19.22883 -37.69478 1.000 32.69170  ? 160 TYR   A CE1 1 
ATOM   1125 C CE2 . TYR   A 1 153 ? 0.71424   -17.25849 -37.93752 1.000 34.37458  ? 160 TYR   A CE2 1 
ATOM   1126 C CZ  . TYR   A 1 153 ? 1.55609   -18.21037 -38.47514 1.000 33.70803  ? 160 TYR   A CZ  1 
ATOM   1127 O OH  . TYR   A 1 153 ? 1.94841   -18.16171 -39.80063 1.000 43.48998  ? 160 TYR   A OH  1 
ATOM   1128 N N   . ALA   A 1 154 ? 0.07592   -20.99228 -32.45276 1.000 21.21625  ? 161 ALA   A N   1 
ATOM   1129 C CA  . ALA   A 1 154 ? 0.33692   -21.47668 -31.09542 1.000 20.57353  ? 161 ALA   A CA  1 
ATOM   1130 C C   . ALA   A 1 154 ? 1.81920   -21.33315 -30.76345 1.000 21.82978  ? 161 ALA   A C   1 
ATOM   1131 O O   . ALA   A 1 154 ? 2.67651   -21.87498 -31.48733 1.000 21.96947  ? 161 ALA   A O   1 
ATOM   1132 C CB  . ALA   A 1 154 ? -0.08598  -22.94228 -30.96174 1.000 24.58811  ? 161 ALA   A CB  1 
ATOM   1133 N N   . TRP   A 1 155 ? 2.09663   -20.58409 -29.70637 1.000 18.45082  ? 162 TRP   A N   1 
ATOM   1134 C CA  . TRP   A 1 155 ? 3.41485   -20.47184 -29.08625 1.000 17.68692  ? 162 TRP   A CA  1 
ATOM   1135 C C   . TRP   A 1 155 ? 3.41981   -21.40612 -27.89408 1.000 21.02523  ? 162 TRP   A C   1 
ATOM   1136 O O   . TRP   A 1 155 ? 2.39918   -21.53569 -27.20734 1.000 18.87927  ? 162 TRP   A O   1 
ATOM   1137 C CB  . TRP   A 1 155 ? 3.60477   -19.01220 -28.65453 1.000 18.81442  ? 162 TRP   A CB  1 
ATOM   1138 C CG  . TRP   A 1 155 ? 4.85499   -18.61432 -27.89806 1.000 17.14171  ? 162 TRP   A CG  1 
ATOM   1139 C CD1 . TRP   A 1 155 ? 5.92732   -17.91384 -28.40830 1.000 18.03790  ? 162 TRP   A CD1 1 
ATOM   1140 C CD2 . TRP   A 1 155 ? 5.11428   -18.80999 -26.50646 1.000 17.25545  ? 162 TRP   A CD2 1 
ATOM   1141 N NE1 . TRP   A 1 155 ? 6.84332   -17.67576 -27.39369 1.000 18.56998  ? 162 TRP   A NE1 1 
ATOM   1142 C CE2 . TRP   A 1 155 ? 6.36080   -18.20948 -26.22704 1.000 16.71164  ? 162 TRP   A CE2 1 
ATOM   1143 C CE3 . TRP   A 1 155 ? 4.40618   -19.43435 -25.45967 1.000 16.74641  ? 162 TRP   A CE3 1 
ATOM   1144 C CZ2 . TRP   A 1 155 ? 6.93694   -18.22453 -24.94601 1.000 17.13067  ? 162 TRP   A CZ2 1 
ATOM   1145 C CZ3 . TRP   A 1 155 ? 4.98010   -19.41916 -24.16578 1.000 17.74029  ? 162 TRP   A CZ3 1 
ATOM   1146 C CH2 . TRP   A 1 155 ? 6.23843   -18.82857 -23.93708 1.000 17.15270  ? 162 TRP   A CH2 1 
ATOM   1147 N N   . GLU   A 1 156 ? 4.55788   -22.04248 -27.62988 1.000 17.71488  ? 163 GLU   A N   1 
ATOM   1148 C CA  . GLU   A 1 156 ? 4.64028   -22.87587 -26.42944 1.000 19.09886  ? 163 GLU   A CA  1 
ATOM   1149 C C   . GLU   A 1 156 ? 6.03832   -22.86155 -25.84137 1.000 17.03008  ? 163 GLU   A C   1 
ATOM   1150 O O   . GLU   A 1 156 ? 7.02515   -22.85763 -26.57539 1.000 20.41091  ? 163 GLU   A O   1 
ATOM   1151 C CB  . GLU   A 1 156 ? 4.31980   -24.34028 -26.73683 1.000 22.76240  ? 163 GLU   A CB  1 
ATOM   1152 C CG  . GLU   A 1 156 ? 3.67968   -25.09949 -25.60072 1.000 29.25422  ? 163 GLU   A CG  1 
ATOM   1153 C CD  . GLU   A 1 156 ? 3.09657   -26.41263 -26.04046 1.000 38.56222  ? 163 GLU   A CD  1 
ATOM   1154 O OE1 . GLU   A 1 156 ? 3.74813   -27.16113 -26.82585 1.000 36.21048  ? 163 GLU   A OE1 1 
ATOM   1155 O OE2 . GLU   A 1 156 ? 1.89521   -26.61723 -25.73929 1.000 30.24491  ? 163 GLU   A OE2 1 
ATOM   1156 N N   . SER   A 1 157 ? 6.12141   -22.93273 -24.50734 1.000 17.30147  ? 164 SER   A N   1 
ATOM   1157 C CA  . SER   A 1 157 ? 7.43484   -23.11828 -23.87667 1.000 17.93301  ? 164 SER   A CA  1 
ATOM   1158 C C   . SER   A 1 157 ? 7.28370   -23.79171 -22.52045 1.000 17.24052  ? 164 SER   A C   1 
ATOM   1159 O O   . SER   A 1 157 ? 6.39117   -23.43637 -21.71607 1.000 19.12354  ? 164 SER   A O   1 
ATOM   1160 C CB  . SER   A 1 157 ? 8.18061   -21.79988 -23.69425 1.000 17.78580  ? 164 SER   A CB  1 
ATOM   1161 O OG  . SER   A 1 157 ? 9.46241   -22.04024 -23.11994 1.000 19.50998  ? 164 SER   A OG  1 
ATOM   1162 N N   . SER   A 1 158 ? 8.17937   -24.75315 -22.28082 1.000 18.66728  ? 165 SER   A N   1 
ATOM   1163 C CA  . SER   A 1 158 ? 8.40673   -25.29351 -20.93826 1.000 20.62104  ? 165 SER   A CA  1 
ATOM   1164 C C   . SER   A 1 158 ? 9.67279   -24.72791 -20.32876 1.000 21.98519  ? 165 SER   A C   1 
ATOM   1165 O O   . SER   A 1 158 ? 10.30142  -25.37147 -19.47057 1.000 24.40083  ? 165 SER   A O   1 
ATOM   1166 C CB  . SER   A 1 158 ? 8.46376   -26.81695 -20.96756 1.000 25.54449  ? 165 SER   A CB  1 
ATOM   1167 O OG  . SER   A 1 158 ? 7.21675   -27.37258 -21.36215 1.000 26.41411  ? 165 SER   A OG  1 
ATOM   1168 N N   . ALA   A 1 159 ? 10.03462  -23.51896 -20.73008 1.000 19.13163  ? 166 ALA   A N   1 
ATOM   1169 C CA  . ALA   A 1 159 ? 11.28762  -22.84635 -20.32883 1.000 21.58600  ? 166 ALA   A CA  1 
ATOM   1170 C C   . ALA   A 1 159 ? 12.46311  -23.69896 -20.82181 1.000 22.11785  ? 166 ALA   A C   1 
ATOM   1171 O O   . ALA   A 1 159 ? 12.41307  -24.26739 -21.92315 1.000 26.54298  ? 166 ALA   A O   1 
ATOM   1172 C CB  . ALA   A 1 159 ? 11.26496  -22.53293 -18.82887 1.000 25.18038  ? 166 ALA   A CB  1 
ATOM   1173 N N   . GLY   A 1 160 ? 13.56768  -23.75915 -20.08442 1.000 23.42095  ? 167 GLY   A N   1 
ATOM   1174 C CA  . GLY   A 1 160 ? 14.69173  -24.50586 -20.60208 1.000 26.71100  ? 167 GLY   A CA  1 
ATOM   1175 C C   . GLY   A 1 160 ? 15.34565  -23.88122 -21.81713 1.000 28.22938  ? 167 GLY   A C   1 
ATOM   1176 O O   . GLY   A 1 160 ? 16.13030  -24.54947 -22.50834 1.000 27.28689  ? 167 GLY   A O   1 
ATOM   1177 N N   . GLY   A 1 161 ? 15.04067  -22.62063 -22.09730 1.000 22.65343  ? 168 GLY   A N   1 
ATOM   1178 C CA  . GLY   A 1 161 ? 15.78822  -21.85132 -23.07236 1.000 20.75556  ? 168 GLY   A CA  1 
ATOM   1179 C C   . GLY   A 1 161 ? 15.15869  -21.75376 -24.45248 1.000 19.17953  ? 168 GLY   A C   1 
ATOM   1180 O O   . GLY   A 1 161 ? 15.75753  -21.11864 -25.33544 1.000 22.48267  ? 168 GLY   A O   1 
ATOM   1181 N N   . SER   A 1 162 ? 14.03207  -22.41326 -24.69158 1.000 19.06128  ? 169 SER   A N   1 
ATOM   1182 C CA  . SER   A 1 162 ? 13.51549  -22.46033 -26.05878 1.000 18.33142  ? 169 SER   A CA  1 
ATOM   1183 C C   . SER   A 1 162 ? 11.99925  -22.39258 -26.01436 1.000 17.44567  ? 169 SER   A C   1 
ATOM   1184 O O   . SER   A 1 162 ? 11.36434  -22.65354 -24.99351 1.000 20.93069  ? 169 SER   A O   1 
ATOM   1185 C CB  . SER   A 1 162 ? 13.94814  -23.71264 -26.84507 1.000 23.16213  ? 169 SER   A CB  1 
ATOM   1186 O OG  . SER   A 1 162 ? 13.33167  -24.87391 -26.30960 1.000 26.88549  ? 169 SER   A OG  1 
ATOM   1187 N N   . PHE   A 1 163 ? 11.44637  -21.99780 -27.15361 1.000 19.62240  ? 170 PHE   A N   1 
ATOM   1188 C CA  . PHE   A 1 163 ? 10.00023  -21.94908 -27.36316 1.000 18.90790  ? 170 PHE   A CA  1 
ATOM   1189 C C   . PHE   A 1 163 ? 9.72140   -22.41056 -28.78976 1.000 19.74815  ? 170 PHE   A C   1 
ATOM   1190 O O   . PHE   A 1 163 ? 10.61006  -22.43664 -29.64530 1.000 21.05988  ? 170 PHE   A O   1 
ATOM   1191 C CB  . PHE   A 1 163 ? 9.38662   -20.55287 -27.12196 1.000 19.65525  ? 170 PHE   A CB  1 
ATOM   1192 C CG  . PHE   A 1 163 ? 9.87922   -19.47792 -28.05962 1.000 20.13993  ? 170 PHE   A CG  1 
ATOM   1193 C CD1 . PHE   A 1 163 ? 10.99926  -18.73919 -27.74125 1.000 21.13133  ? 170 PHE   A CD1 1 
ATOM   1194 C CD2 . PHE   A 1 163 ? 9.17561   -19.15430 -29.21166 1.000 19.23567  ? 170 PHE   A CD2 1 
ATOM   1195 C CE1 . PHE   A 1 163 ? 11.43865  -17.70187 -28.59233 1.000 22.45421  ? 170 PHE   A CE1 1 
ATOM   1196 C CE2 . PHE   A 1 163 ? 9.59495   -18.15382 -30.04666 1.000 19.10928  ? 170 PHE   A CE2 1 
ATOM   1197 C CZ  . PHE   A 1 163 ? 10.72719  -17.40557 -29.74518 1.000 21.75268  ? 170 PHE   A CZ  1 
ATOM   1198 N N   . THR   A 1 164 ? 8.47827   -22.82377 -29.03285 1.000 19.74187  ? 171 THR   A N   1 
ATOM   1199 C CA  . THR   A 1 164 ? 8.08073   -23.26969 -30.35815 1.000 18.88588  ? 171 THR   A CA  1 
ATOM   1200 C C   . THR   A 1 164 ? 6.93401   -22.41279 -30.85579 1.000 18.04556  ? 171 THR   A C   1 
ATOM   1201 O O   . THR   A 1 164 ? 6.16128   -21.86085 -30.06373 1.000 20.06802  ? 171 THR   A O   1 
ATOM   1202 C CB  . THR   A 1 164 ? 7.63530   -24.74821 -30.40299 1.000 22.28432  ? 171 THR   A CB  1 
ATOM   1203 O OG1 . THR   A 1 164 ? 6.50509   -24.93907 -29.55071 1.000 23.78758  ? 171 THR   A OG1 1 
ATOM   1204 C CG2 . THR   A 1 164 ? 8.76507   -25.69447 -29.94444 1.000 22.97769  ? 171 THR   A CG2 1 
ATOM   1205 N N   . VAL   A 1 165 ? 6.83777   -22.31720 -32.17565 1.000 21.34822  ? 172 VAL   A N   1 
ATOM   1206 C CA  . VAL   A 1 165 ? 5.71700   -21.64782 -32.81631 1.000 23.37085  ? 172 VAL   A CA  1 
ATOM   1207 C C   . VAL   A 1 165 ? 5.25463   -22.55524 -33.93803 1.000 24.40352  ? 172 VAL   A C   1 
ATOM   1208 O O   . VAL   A 1 165 ? 6.07714   -23.06401 -34.71138 1.000 24.10125  ? 172 VAL   A O   1 
ATOM   1209 C CB  . VAL   A 1 165 ? 6.08722   -20.25434 -33.36734 1.000 22.74361  ? 172 VAL   A CB  1 
ATOM   1210 C CG1 . VAL   A 1 165 ? 4.88764   -19.64687 -34.12113 1.000 24.72669  ? 172 VAL   A CG1 1 
ATOM   1211 C CG2 . VAL   A 1 165 ? 6.50496   -19.33196 -32.25434 1.000 22.98086  ? 172 VAL   A CG2 1 
ATOM   1212 N N   . ARG   A 1 166 ? 3.93752   -22.74973 -34.03734 1.000 23.66536  ? 173 ARG   A N   1 
ATOM   1213 C CA  . ARG   A 1 166 ? 3.36485   -23.48816 -35.14793 1.000 24.50091  ? 173 ARG   A CA  1 
ATOM   1214 C C   . ARG   A 1 166 ? 2.03157   -22.86268 -35.51319 1.000 23.53881  ? 173 ARG   A C   1 
ATOM   1215 O O   . ARG   A 1 166 ? 1.41057   -22.19390 -34.68540 1.000 24.25409  ? 173 ARG   A O   1 
ATOM   1216 C CB  . ARG   A 1 166 ? 3.12130   -24.96475 -34.83235 1.000 30.51669  ? 173 ARG   A CB  1 
ATOM   1217 C CG  . ARG   A 1 166 ? 2.52069   -25.26220 -33.51156 1.000 32.77928  ? 173 ARG   A CG  1 
ATOM   1218 C CD  . ARG   A 1 166 ? 1.57293   -26.44282 -33.45621 1.000 47.41307  ? 173 ARG   A CD  1 
ATOM   1219 N NE  . ARG   A 1 166 ? 1.03314   -26.62469 -32.10717 1.000 62.80360  ? 173 ARG   A NE  1 
ATOM   1220 C CZ  . ARG   A 1 166 ? -0.22454  -26.41372 -31.72699 1.000 66.60657  ? 173 ARG   A CZ  1 
ATOM   1221 N NH1 . ARG   A 1 166 ? -1.15158  -26.01278 -32.58106 1.000 41.62487  ? 173 ARG   A NH1 1 
ATOM   1222 N NH2 . ARG   A 1 166 ? -0.55787  -26.59756 -30.44652 1.000 46.20258  ? 173 ARG   A NH2 1 
ATOM   1223 N N   . THR   A 1 167 ? 1.58676   -23.10229 -36.75333 1.000 26.86039  ? 174 THR   A N   1 
ATOM   1224 C CA  . THR   A 1 167 ? 0.20147   -22.75264 -37.08582 1.000 28.16351  ? 174 THR   A CA  1 
ATOM   1225 C C   . THR   A 1 167 ? -0.73052  -23.60672 -36.23774 1.000 35.10905  ? 174 THR   A C   1 
ATOM   1226 O O   . THR   A 1 167 ? -0.44126  -24.76931 -35.94956 1.000 35.52119  ? 174 THR   A O   1 
ATOM   1227 C CB  . THR   A 1 167 ? -0.09589  -22.93144 -38.57125 1.000 34.32061  ? 174 THR   A CB  1 
ATOM   1228 O OG1 . THR   A 1 167 ? -0.03137  -24.32203 -38.90377 1.000 47.21669  ? 174 THR   A OG1 1 
ATOM   1229 C CG2 . THR   A 1 167 ? 0.87613   -22.14597 -39.41736 1.000 32.00559  ? 174 THR   A CG2 1 
ATOM   1230 N N   . ASP   A 1 168 ? -1.83156  -23.01357 -35.78106 1.000 29.97038  ? 175 ASP   A N   1 
ATOM   1231 C CA  . ASP   A 1 168 ? -2.74681  -23.71212 -34.89392 1.000 33.20467  ? 175 ASP   A CA  1 
ATOM   1232 C C   . ASP   A 1 168 ? -3.90196  -24.23153 -35.72130 1.000 43.76735  ? 175 ASP   A C   1 
ATOM   1233 O O   . ASP   A 1 168 ? -4.68477  -23.44492 -36.25720 1.000 44.15599  ? 175 ASP   A O   1 
ATOM   1234 C CB  . ASP   A 1 168 ? -3.28051  -22.81517 -33.78180 1.000 30.57546  ? 175 ASP   A CB  1 
ATOM   1235 C CG  . ASP   A 1 168 ? -4.11929  -23.58487 -32.77183 1.000 41.02124  ? 175 ASP   A CG  1 
ATOM   1236 O OD1 . ASP   A 1 168 ? -3.70726  -24.68863 -32.35772 1.000 51.41745  ? 175 ASP   A OD1 1 
ATOM   1237 O OD2 . ASP   A 1 168 ? -5.23996  -23.13611 -32.46965 1.000 36.19787  ? 175 ASP   A OD2 1 
ATOM   1238 N N   . THR   A 1 169 ? -3.99935  -25.55376 -35.80826 1.000 55.30780  ? 176 THR   A N   1 
ATOM   1239 C CA  . THR   A 1 169 ? -5.13932  -26.25712 -36.36987 1.000 69.45938  ? 176 THR   A CA  1 
ATOM   1240 C C   . THR   A 1 169 ? -6.29619  -26.38819 -35.38449 1.000 64.11124  ? 176 THR   A C   1 
ATOM   1241 O O   . THR   A 1 169 ? -7.37828  -26.83160 -35.78531 1.000 56.53203  ? 176 THR   A O   1 
ATOM   1242 C CB  . THR   A 1 169 ? -4.68225  -27.64244 -36.83468 1.000 73.82318  ? 176 THR   A CB  1 
ATOM   1243 O OG1 . THR   A 1 169 ? -3.84129  -28.22569 -35.82014 1.000 56.62662  ? 176 THR   A OG1 1 
ATOM   1244 C CG2 . THR   A 1 169 ? -3.90332  -27.52609 -38.14068 1.000 58.18179  ? 176 THR   A CG2 1 
ATOM   1245 N N   . GLY   A 1 170 ? -6.09422  -26.01296 -34.11674 1.000 60.35173  ? 177 GLY   A N   1 
ATOM   1246 C CA  . GLY   A 1 170 ? -7.13596  -26.07058 -33.10559 1.000 59.23535  ? 177 GLY   A CA  1 
ATOM   1247 C C   . GLY   A 1 170 ? -8.38278  -25.25462 -33.40944 1.000 52.20709  ? 177 GLY   A C   1 
ATOM   1248 O O   . GLY   A 1 170 ? -8.52982  -24.68313 -34.49284 1.000 45.39760  ? 177 GLY   A O   1 
ATOM   1249 N N   . GLU   A 1 171 ? -9.28951  -25.19620 -32.44531 1.000 51.62764  ? 178 GLU   A N   1 
ATOM   1250 C CA  . GLU   A 1 171 ? -10.55373 -24.48648 -32.58012 1.000 52.91934  ? 178 GLU   A CA  1 
ATOM   1251 C C   . GLU   A 1 171 ? -10.31321 -23.03506 -33.01353 1.000 37.35663  ? 178 GLU   A C   1 
ATOM   1252 O O   . GLU   A 1 171 ? -9.57148  -22.32461 -32.33819 1.000 33.33583  ? 178 GLU   A O   1 
ATOM   1253 C CB  . GLU   A 1 171 ? -11.25980 -24.53913 -31.22725 1.000 50.46081  ? 178 GLU   A CB  1 
ATOM   1254 C CG  . GLU   A 1 171 ? -12.74975 -24.48632 -31.27918 1.000 46.52101  ? 178 GLU   A CG  1 
ATOM   1255 C CD  . GLU   A 1 171 ? -13.31993 -25.47352 -32.27087 1.000 52.11492  ? 178 GLU   A CD  1 
ATOM   1256 O OE1 . GLU   A 1 171 ? -13.92696 -25.02342 -33.25175 1.000 51.38704  ? 178 GLU   A OE1 1 
ATOM   1257 O OE2 . GLU   A 1 171 ? -13.11276 -26.68950 -32.10448 1.000 48.74102  ? 178 GLU   A OE2 1 
ATOM   1258 N N   . PRO   A 1 172 ? -10.88149 -22.58450 -34.13755 1.000 40.58241  ? 179 PRO   A N   1 
ATOM   1259 C CA  . PRO   A 1 172 ? -10.69061 -21.18131 -34.54130 1.000 38.77823  ? 179 PRO   A CA  1 
ATOM   1260 C C   . PRO   A 1 172 ? -11.23191 -20.23476 -33.48158 1.000 38.75775  ? 179 PRO   A C   1 
ATOM   1261 O O   . PRO   A 1 172 ? -12.34572 -20.41470 -32.98948 1.000 49.33300  ? 179 PRO   A O   1 
ATOM   1262 C CB  . PRO   A 1 172 ? -11.50648 -21.07450 -35.83487 1.000 46.26333  ? 179 PRO   A CB  1 
ATOM   1263 C CG  . PRO   A 1 172 ? -11.54915 -22.45539 -36.37372 1.000 47.76396  ? 179 PRO   A CG  1 
ATOM   1264 C CD  . PRO   A 1 172 ? -11.58928 -23.36540 -35.17033 1.000 50.80360  ? 179 PRO   A CD  1 
ATOM   1265 N N   . MET   A 1 173 ? -10.45850 -19.20018 -33.14381 1.000 34.00024  ? 180 MET   A N   1 
ATOM   1266 C CA  . MET   A 1 173 ? -10.95104 -18.26966 -32.13465 1.000 41.50861  ? 180 MET   A CA  1 
ATOM   1267 C C   . MET   A 1 173 ? -11.49202 -16.95251 -32.66827 1.000 52.17573  ? 180 MET   A C   1 
ATOM   1268 O O   . MET   A 1 173 ? -12.15168 -16.23427 -31.91259 1.000 57.99333  ? 180 MET   A O   1 
ATOM   1269 C CB  . MET   A 1 173 ? -9.88864  -17.92818 -31.09070 1.000 38.21411  ? 180 MET   A CB  1 
ATOM   1270 C CG  . MET   A 1 173 ? -8.87716  -18.97971 -30.70825 1.000 51.39733  ? 180 MET   A CG  1 
ATOM   1271 S SD  . MET   A 1 173 ? -7.39500  -18.07976 -30.24739 1.000 44.11427  ? 180 MET   A SD  1 
ATOM   1272 C CE  . MET   A 1 173 ? -8.18758  -17.07039 -29.02165 1.000 38.86271  ? 180 MET   A CE  1 
ATOM   1273 N N   . GLY   A 1 174 ? -11.20990 -16.57881 -33.89861 1.000 33.94422  ? 181 GLY   A N   1 
ATOM   1274 C CA  . GLY   A 1 174 ? -11.85494 -15.36160 -34.37257 1.000 32.65581  ? 181 GLY   A CA  1 
ATOM   1275 C C   . GLY   A 1 174 ? -10.98168 -14.13837 -34.23086 1.000 28.23005  ? 181 GLY   A C   1 
ATOM   1276 O O   . GLY   A 1 174 ? -10.55182 -13.54892 -35.23183 1.000 30.72968  ? 181 GLY   A O   1 
ATOM   1277 N N   . ARG   A 1 175 ? -10.72257 -13.75672 -32.97733 1.000 22.09050  ? 182 ARG   A N   1 
ATOM   1278 C CA  . ARG   A 1 175 ? -9.72288  -12.73887 -32.67007 1.000 21.49084  ? 182 ARG   A CA  1 
ATOM   1279 C C   . ARG   A 1 175 ? -9.44359  -12.77185 -31.17955 1.000 19.74047  ? 182 ARG   A C   1 
ATOM   1280 O O   . ARG   A 1 175 ? -10.38928 -12.85878 -30.39481 1.000 23.46405  ? 182 ARG   A O   1 
ATOM   1281 C CB  . ARG   A 1 175 ? -10.21122 -11.32289 -33.06275 1.000 21.27770  ? 182 ARG   A CB  1 
ATOM   1282 C CG  . ARG   A 1 175 ? -9.07494  -10.26273 -32.89292 1.000 22.22042  ? 182 ARG   A CG  1 
ATOM   1283 C CD  . ARG   A 1 175 ? -9.62330  -8.84748  -32.74500 1.000 21.85289  ? 182 ARG   A CD  1 
ATOM   1284 N NE  . ARG   A 1 175 ? -10.55239 -8.74522  -31.61337 1.000 20.88697  ? 182 ARG   A NE  1 
ATOM   1285 C CZ  . ARG   A 1 175 ? -11.87099 -8.59056  -31.70343 1.000 20.90548  ? 182 ARG   A CZ  1 
ATOM   1286 N NH1 . ARG   A 1 175 ? -12.51598 -8.53212  -32.88752 1.000 23.12216  ? 182 ARG   A NH1 1 
ATOM   1287 N NH2 . ARG   A 1 175 ? -12.58683 -8.49198  -30.57885 1.000 21.63785  ? 182 ARG   A NH2 1 
ATOM   1288 N N   . GLY   A 1 176 ? -8.16977  -12.72821 -30.79315 1.000 25.74043  ? 183 GLY   A N   1 
ATOM   1289 C CA  . GLY   A 1 176 ? -7.82093  -12.64580 -29.38101 1.000 22.90055  ? 183 GLY   A CA  1 
ATOM   1290 C C   . GLY   A 1 176 ? -6.73647  -13.63270 -29.02330 1.000 22.17392  ? 183 GLY   A C   1 
ATOM   1291 O O   . GLY   A 1 176 ? -6.02450  -14.14008 -29.89755 1.000 22.84113  ? 183 GLY   A O   1 
ATOM   1292 N N   . THR   A 1 177 ? -6.60953  -13.90963 -27.73008 1.000 19.09659  ? 184 THR   A N   1 
ATOM   1293 C CA  . THR   A 1 177 ? -5.52399  -14.75428 -27.24894 1.000 17.91494  ? 184 THR   A CA  1 
ATOM   1294 C C   . THR   A 1 177 ? -6.03133  -15.64777 -26.14159 1.000 20.67361  ? 184 THR   A C   1 
ATOM   1295 O O   . THR   A 1 177 ? -6.81668  -15.19734 -25.29159 1.000 19.30418  ? 184 THR   A O   1 
ATOM   1296 C CB  . THR   A 1 177 ? -4.37217  -13.88651 -26.73898 1.000 20.34068  ? 184 THR   A CB  1 
ATOM   1297 O OG1 . THR   A 1 177 ? -3.94610  -13.02066 -27.79339 1.000 21.04850  ? 184 THR   A OG1 1 
ATOM   1298 C CG2 . THR   A 1 177 ? -3.17554  -14.75392 -26.25303 1.000 22.69242  ? 184 THR   A CG2 1 
ATOM   1299 N N   . LYS   A 1 178 ? -5.54997  -16.89624 -26.12144 1.000 18.74468  ? 185 LYS   A N   1 
ATOM   1300 C CA  . LYS   A 1 178 ? -5.75193  -17.79690 -24.97777 1.000 18.04527  ? 185 LYS   A CA  1 
ATOM   1301 C C   . LYS   A 1 178 ? -4.39054  -18.12793 -24.39440 1.000 18.39168  ? 185 LYS   A C   1 
ATOM   1302 O O   . LYS   A 1 178 ? -3.51275  -18.59333 -25.12821 1.000 20.97235  ? 185 LYS   A O   1 
ATOM   1303 C CB  . LYS   A 1 178 ? -6.43224  -19.11219 -25.43666 1.000 25.08457  ? 185 LYS   A CB  1 
ATOM   1304 C CG  . LYS   A 1 178 ? -7.82818  -18.89310 -26.04778 1.000 30.95145  ? 185 LYS   A CG  1 
ATOM   1305 C CD  . LYS   A 1 178 ? -8.53755  -20.17129 -26.41523 1.000 41.93612  ? 185 LYS   A CD  1 
ATOM   1306 C CE  . LYS   A 1 178 ? -7.59242  -21.33119 -26.48927 1.000 44.57662  ? 185 LYS   A CE  1 
ATOM   1307 N NZ  . LYS   A 1 178 ? -8.11009  -22.34192 -27.46809 1.000 55.27541  ? 185 LYS   A NZ  1 
ATOM   1308 N N   . VAL   A 1 179 ? -4.22090  -17.92140 -23.08933 1.000 18.12375  ? 186 VAL   A N   1 
ATOM   1309 C CA  . VAL   A 1 179 ? -2.99919  -18.32172 -22.38486 1.000 18.73466  ? 186 VAL   A CA  1 
ATOM   1310 C C   . VAL   A 1 179 ? -3.36432  -19.55849 -21.57322 1.000 18.91857  ? 186 VAL   A C   1 
ATOM   1311 O O   . VAL   A 1 179 ? -4.20715  -19.48581 -20.66118 1.000 19.02600  ? 186 VAL   A O   1 
ATOM   1312 C CB  . VAL   A 1 179 ? -2.45392  -17.19746 -21.48733 1.000 17.44636  ? 186 VAL   A CB  1 
ATOM   1313 C CG1 . VAL   A 1 179 ? -1.24780  -17.72513 -20.66580 1.000 19.04021  ? 186 VAL   A CG1 1 
ATOM   1314 C CG2 . VAL   A 1 179 ? -2.01543  -16.02356 -22.34132 1.000 18.10457  ? 186 VAL   A CG2 1 
ATOM   1315 N N   . ILE   A 1 180 ? -2.77388  -20.69930 -21.92688 1.000 19.17418  ? 187 ILE   A N   1 
ATOM   1316 C CA  . ILE   A 1 180 ? -3.08395  -21.97310 -21.28580 1.000 18.59822  ? 187 ILE   A CA  1 
ATOM   1317 C C   . ILE   A 1 180 ? -1.95036  -22.28773 -20.32976 1.000 16.02463  ? 187 ILE   A C   1 
ATOM   1318 O O   . ILE   A 1 180 ? -0.82271  -22.53930 -20.76792 1.000 18.73908  ? 187 ILE   A O   1 
ATOM   1319 C CB  . ILE   A 1 180 ? -3.24928  -23.09317 -22.32013 1.000 20.10493  ? 187 ILE   A CB  1 
ATOM   1320 C CG1 . ILE   A 1 180 ? -4.27297  -22.70217 -23.39421 1.000 23.13990  ? 187 ILE   A CG1 1 
ATOM   1321 C CG2 . ILE   A 1 180 ? -3.62470  -24.43394 -21.61346 1.000 22.79938  ? 187 ILE   A CG2 1 
ATOM   1322 C CD1 . ILE   A 1 180 ? -4.32793  -23.70366 -24.54416 1.000 27.33364  ? 187 ILE   A CD1 1 
ATOM   1323 N N   . LEU   A 1 181 ? -2.25530  -22.30632 -19.04481 1.000 16.92724  ? 188 LEU   A N   1 
ATOM   1324 C CA  . LEU   A 1 181 ? -1.25893  -22.60748 -18.01689 1.000 17.85820  ? 188 LEU   A CA  1 
ATOM   1325 C C   . LEU   A 1 181 ? -1.37845  -24.08506 -17.66476 1.000 21.02811  ? 188 LEU   A C   1 
ATOM   1326 O O   . LEU   A 1 181 ? -2.38848  -24.50582 -17.08470 1.000 21.33508  ? 188 LEU   A O   1 
ATOM   1327 C CB  . LEU   A 1 181 ? -1.45569  -21.74087 -16.77463 1.000 18.03560  ? 188 LEU   A CB  1 
ATOM   1328 C CG  . LEU   A 1 181 ? -1.55223  -20.24732 -17.01242 1.000 19.41001  ? 188 LEU   A CG  1 
ATOM   1329 C CD1 . LEU   A 1 181 ? -1.89242  -19.57247 -15.66550 1.000 22.73783  ? 188 LEU   A CD1 1 
ATOM   1330 C CD2 . LEU   A 1 181 ? -0.26092  -19.74013 -17.54574 1.000 20.87941  ? 188 LEU   A CD2 1 
ATOM   1331 N N   . HIS   A 1 182 ? -0.33576  -24.86731 -17.97307 1.000 21.28581  ? 189 HIS   A N   1 
ATOM   1332 C CA  . HIS   A 1 182 ? -0.26640  -26.27450 -17.57196 1.000 21.56439  ? 189 HIS   A CA  1 
ATOM   1333 C C   . HIS   A 1 182 ? 0.35576   -26.26686 -16.18307 1.000 22.29116  ? 189 HIS   A C   1 
ATOM   1334 O O   . HIS   A 1 182 ? 1.56357   -26.11619 -16.03635 1.000 23.69814  ? 189 HIS   A O   1 
ATOM   1335 C CB  . HIS   A 1 182 ? 0.53509   -27.09701 -18.57607 1.000 23.23796  ? 189 HIS   A CB  1 
ATOM   1336 C CG  . HIS   A 1 182 ? 0.03468   -26.96790 -19.99127 1.000 25.99548  ? 189 HIS   A CG  1 
ATOM   1337 N ND1 . HIS   A 1 182 ? -0.75611  -27.92981 -20.58884 1.000 34.00072  ? 189 HIS   A ND1 1 
ATOM   1338 C CD2 . HIS   A 1 182 ? 0.15196   -25.96384 -20.89876 1.000 26.08583  ? 189 HIS   A CD2 1 
ATOM   1339 C CE1 . HIS   A 1 182 ? -1.06410  -27.54349 -21.81653 1.000 30.64253  ? 189 HIS   A CE1 1 
ATOM   1340 N NE2 . HIS   A 1 182 ? -0.51644  -26.36133 -22.03536 1.000 30.19902  ? 189 HIS   A NE2 1 
ATOM   1341 N N   . LEU   A 1 183 ? -0.47868  -26.38482 -15.15129 1.000 21.97752  ? 190 LEU   A N   1 
ATOM   1342 C CA  . LEU   A 1 183 ? -0.03562  -26.06390 -13.79588 1.000 24.37157  ? 190 LEU   A CA  1 
ATOM   1343 C C   . LEU   A 1 183 ? 0.92458   -27.10593 -13.23034 1.000 26.99654  ? 190 LEU   A C   1 
ATOM   1344 O O   . LEU   A 1 183 ? 0.83563   -28.30339 -13.52505 1.000 26.39311  ? 190 LEU   A O   1 
ATOM   1345 C CB  . LEU   A 1 183 ? -1.25309  -25.94061 -12.87467 1.000 22.25378  ? 190 LEU   A CB  1 
ATOM   1346 C CG  . LEU   A 1 183 ? -2.17461  -24.75078 -13.17278 1.000 20.09664  ? 190 LEU   A CG  1 
ATOM   1347 C CD1 . LEU   A 1 183 ? -3.39237  -24.77823 -12.21947 1.000 23.80441  ? 190 LEU   A CD1 1 
ATOM   1348 C CD2 . LEU   A 1 183 ? -1.44647  -23.43386 -13.02042 1.000 23.64385  ? 190 LEU   A CD2 1 
ATOM   1349 N N   . LYS   A 1 184 ? 1.86822   -26.63101 -12.40162 1.000 25.45822  ? 191 LYS   A N   1 
ATOM   1350 C CA  . LYS   A 1 184 ? 2.71423   -27.50693 -11.60878 1.000 25.91651  ? 191 LYS   A CA  1 
ATOM   1351 C C   . LYS   A 1 184 ? 1.85386   -28.33174 -10.64958 1.000 30.34257  ? 191 LYS   A C   1 
ATOM   1352 O O   . LYS   A 1 184 ? 0.77566   -27.89515 -10.22488 1.000 28.65423  ? 191 LYS   A O   1 
ATOM   1353 C CB  . LYS   A 1 184 ? 3.73557   -26.68237 -10.80924 1.000 28.62723  ? 191 LYS   A CB  1 
ATOM   1354 C CG  . LYS   A 1 184 ? 4.72271   -25.84998 -11.66867 1.000 33.68319  ? 191 LYS   A CG  1 
ATOM   1355 C CD  . LYS   A 1 184 ? 5.48759   -24.81270 -10.78352 1.000 36.18559  ? 191 LYS   A CD  1 
ATOM   1356 C CE  . LYS   A 1 184 ? 6.45421   -23.93542 -11.58605 1.000 43.78313  ? 191 LYS   A CE  1 
ATOM   1357 N NZ  . LYS   A 1 184 ? 7.35607   -23.00587 -10.77324 1.000 44.15173  ? 191 LYS   A NZ  1 
ATOM   1358 N N   . GLU   A 1 185 ? 2.32391   -29.54737 -10.34211 1.000 33.51002  ? 192 GLU   A N   1 
ATOM   1359 C CA  . GLU   A 1 185 ? 1.53736   -30.47852 -9.53302  1.000 35.57194  ? 192 GLU   A CA  1 
ATOM   1360 C C   . GLU   A 1 185 ? 1.13065   -29.88836 -8.18704  1.000 36.96458  ? 192 GLU   A C   1 
ATOM   1361 O O   . GLU   A 1 185 ? 0.06952   -30.23030 -7.65625  1.000 40.08575  ? 192 GLU   A O   1 
ATOM   1362 C CB  . GLU   A 1 185 ? 2.32592   -31.77809 -9.32997  1.000 44.93235  ? 192 GLU   A CB  1 
ATOM   1363 C CG  . GLU   A 1 185 ? 1.59019   -32.87503 -8.59114  1.000 64.04611  ? 192 GLU   A CG  1 
ATOM   1364 C CD  . GLU   A 1 185 ? 2.51533   -34.01987 -8.20944  1.000 84.74538  ? 192 GLU   A CD  1 
ATOM   1365 O OE1 . GLU   A 1 185 ? 3.60094   -34.12891 -8.82690  1.000 75.05807  ? 192 GLU   A OE1 1 
ATOM   1366 O OE2 . GLU   A 1 185 ? 2.17050   -34.79221 -7.28284  1.000 84.46447  ? 192 GLU   A OE2 1 
ATOM   1367 N N   . ASP   A 1 186 ? 1.95310   -29.01935 -7.61052  1.000 33.44391  ? 193 ASP   A N   1 
ATOM   1368 C CA  . ASP   A 1 186 ? 1.67340   -28.46899 -6.29302  1.000 31.80391  ? 193 ASP   A CA  1 
ATOM   1369 C C   . ASP   A 1 186 ? 0.98320   -27.11007 -6.35105  1.000 28.31803  ? 193 ASP   A C   1 
ATOM   1370 O O   . ASP   A 1 186 ? 0.87031   -26.44311 -5.30620  1.000 32.59642  ? 193 ASP   A O   1 
ATOM   1371 C CB  . ASP   A 1 186 ? 2.95424   -28.39217 -5.47184  1.000 38.21996  ? 193 ASP   A CB  1 
ATOM   1372 C CG  . ASP   A 1 186 ? 3.95920   -27.40346 -6.01758  1.000 35.86052  ? 193 ASP   A CG  1 
ATOM   1373 O OD1 . ASP   A 1 186 ? 3.87178   -27.01437 -7.19531  1.000 42.10109  ? 193 ASP   A OD1 1 
ATOM   1374 O OD2 . ASP   A 1 186 ? 4.90483   -27.07958 -5.26297  1.000 46.53869  ? 193 ASP   A OD2 1 
ATOM   1375 N N   . GLN   A 1 187 ? 0.48794   -26.71097 -7.52422  1.000 30.10374  ? 194 GLN   A N   1 
ATOM   1376 C CA  . GLN   A 1 187 ? -0.15881  -25.41837 -7.69757  1.000 24.94752  ? 194 GLN   A CA  1 
ATOM   1377 C C   . GLN   A 1 187 ? -1.61541  -25.56839 -8.12630  1.000 23.06989  ? 194 GLN   A C   1 
ATOM   1378 O O   . GLN   A 1 187 ? -2.16897  -24.66206 -8.74327  1.000 25.65604  ? 194 GLN   A O   1 
ATOM   1379 C CB  . GLN   A 1 187 ? 0.62060   -24.56884 -8.70854  1.000 24.48129  ? 194 GLN   A CB  1 
ATOM   1380 C CG  . GLN   A 1 187 ? 2.06424   -24.32647 -8.26381  1.000 25.64434  ? 194 GLN   A CG  1 
ATOM   1381 C CD  . GLN   A 1 187 ? 2.18135   -23.61496 -6.92691  1.000 32.55843  ? 194 GLN   A CD  1 
ATOM   1382 O OE1 . GLN   A 1 187 ? 1.39328   -22.73641 -6.62181  1.000 33.09014  ? 194 GLN   A OE1 1 
ATOM   1383 N NE2 . GLN   A 1 187 ? 3.19889   -23.96169 -6.14696  1.000 31.41559  ? 194 GLN   A NE2 1 
ATOM   1384 N N   . THR   A 1 188 ? -2.25804  -26.68061 -7.79429  1.000 28.18440  ? 195 THR   A N   1 
ATOM   1385 C CA  . THR   A 1 188 ? -3.62131  -26.87909 -8.27817  1.000 28.67857  ? 195 THR   A CA  1 
ATOM   1386 C C   . THR   A 1 188 ? -4.66035  -26.05609 -7.52497  1.000 28.44689  ? 195 THR   A C   1 
ATOM   1387 O O   . THR   A 1 188 ? -5.84530  -26.10440 -7.90025  1.000 29.99800  ? 195 THR   A O   1 
ATOM   1388 C CB  . THR   A 1 188 ? -4.00500  -28.35956 -8.20939  1.000 32.78356  ? 195 THR   A CB  1 
ATOM   1389 O OG1 . THR   A 1 188 ? -3.90633  -28.83348 -6.85934  1.000 37.39552  ? 195 THR   A OG1 1 
ATOM   1390 C CG2 . THR   A 1 188 ? -3.09648  -29.16671 -9.16513  1.000 33.98780  ? 195 THR   A CG2 1 
ATOM   1391 N N   . GLU   A 1 189 ? -4.27025  -25.32651 -6.47649  1.000 26.67384  ? 196 GLU   A N   1 
ATOM   1392 C CA  . GLU   A 1 189 ? -5.22818  -24.43964 -5.81381  1.000 26.67069  ? 196 GLU   A CA  1 
ATOM   1393 C C   . GLU   A 1 189 ? -5.82417  -23.44629 -6.79705  1.000 28.77041  ? 196 GLU   A C   1 
ATOM   1394 O O   . GLU   A 1 189 ? -6.94597  -22.97460 -6.58782  1.000 27.15495  ? 196 GLU   A O   1 
ATOM   1395 C CB  . GLU   A 1 189 ? -4.57990  -23.68880 -4.63942  1.000 30.05834  ? 196 GLU   A CB  1 
ATOM   1396 C CG  . GLU   A 1 189 ? -3.50404  -22.69205 -5.06800  1.000 29.62407  ? 196 GLU   A CG  1 
ATOM   1397 C CD  . GLU   A 1 189 ? -2.72077  -22.20369 -3.87986  1.000 34.45072  ? 196 GLU   A CD  1 
ATOM   1398 O OE1 . GLU   A 1 189 ? -1.81536  -22.96120 -3.43626  1.000 40.62275  ? 196 GLU   A OE1 1 
ATOM   1399 O OE2 . GLU   A 1 189 ? -3.03081  -21.12038 -3.30375  1.000 34.62324  ? 196 GLU   A OE2 1 
ATOM   1400 N N   . TYR   A 1 190 ? -5.08641  -23.11673 -7.85518  1.000 24.04252  ? 197 TYR   A N   1 
ATOM   1401 C CA  . TYR   A 1 190 ? -5.49635  -22.12033 -8.84461  1.000 20.15136  ? 197 TYR   A CA  1 
ATOM   1402 C C   . TYR   A 1 190 ? -6.51445  -22.66746 -9.82009  1.000 24.55176  ? 197 TYR   A C   1 
ATOM   1403 O O   . TYR   A 1 190 ? -6.88817  -21.95069 -10.75319 1.000 25.16938  ? 197 TYR   A O   1 
ATOM   1404 C CB  . TYR   A 1 190 ? -4.26072  -21.52157 -9.55997  1.000 21.61148  ? 197 TYR   A CB  1 
ATOM   1405 C CG  . TYR   A 1 190 ? -3.35298  -20.87811 -8.54901  1.000 22.52928  ? 197 TYR   A CG  1 
ATOM   1406 C CD1 . TYR   A 1 190 ? -3.77349  -19.76984 -7.81421  1.000 21.87849  ? 197 TYR   A CD1 1 
ATOM   1407 C CD2 . TYR   A 1 190 ? -2.09445  -21.41418 -8.24957  1.000 24.26260  ? 197 TYR   A CD2 1 
ATOM   1408 C CE1 . TYR   A 1 190 ? -2.98765  -19.20429 -6.83367  1.000 25.78898  ? 197 TYR   A CE1 1 
ATOM   1409 C CE2 . TYR   A 1 190 ? -1.28897  -20.84645 -7.27123  1.000 25.32420  ? 197 TYR   A CE2 1 
ATOM   1410 C CZ  . TYR   A 1 190 ? -1.74143  -19.72215 -6.53501  1.000 23.75964  ? 197 TYR   A CZ  1 
ATOM   1411 O OH  . TYR   A 1 190 ? -1.00313  -19.13248 -5.52543  1.000 27.78490  ? 197 TYR   A OH  1 
ATOM   1412 N N   . LEU   A 1 191 ? -6.97672  -23.89669 -9.60570  1.000 23.21334  ? 198 LEU   A N   1 
ATOM   1413 C CA  . LEU   A 1 191 ? -8.13105  -24.44431 -10.30984 1.000 24.04963  ? 198 LEU   A CA  1 
ATOM   1414 C C   . LEU   A 1 191 ? -9.39535  -24.38742 -9.48073  1.000 26.05940  ? 198 LEU   A C   1 
ATOM   1415 O O   . LEU   A 1 191 ? -10.46557 -24.75215 -9.98428  1.000 31.02826  ? 198 LEU   A O   1 
ATOM   1416 C CB  . LEU   A 1 191 ? -7.88640  -25.90784 -10.71243 1.000 28.47455  ? 198 LEU   A CB  1 
ATOM   1417 C CG  . LEU   A 1 191 ? -6.64299  -26.08037 -11.58994 1.000 24.26437  ? 198 LEU   A CG  1 
ATOM   1418 C CD1 . LEU   A 1 191 ? -6.31772  -27.54423 -11.82874 1.000 32.77002  ? 198 LEU   A CD1 1 
ATOM   1419 C CD2 . LEU   A 1 191 ? -6.77664  -25.27916 -12.91067 1.000 28.45460  ? 198 LEU   A CD2 1 
ATOM   1420 N N   . GLU   A 1 192 ? -9.29765  -24.04495 -8.19291  1.000 25.92463  ? 199 GLU   A N   1 
ATOM   1421 C CA  . GLU   A 1 192 ? -10.45688 -24.06970 -7.32425  1.000 26.10038  ? 199 GLU   A CA  1 
ATOM   1422 C C   . GLU   A 1 192 ? -11.22110 -22.75583 -7.41488  1.000 29.06379  ? 199 GLU   A C   1 
ATOM   1423 O O   . GLU   A 1 192 ? -10.62023 -21.67379 -7.42511  1.000 26.48819  ? 199 GLU   A O   1 
ATOM   1424 C CB  . GLU   A 1 192 ? -10.02932 -24.36225 -5.88527  1.000 33.61341  ? 199 GLU   A CB  1 
ATOM   1425 C CG  . GLU   A 1 192 ? -9.36126  -25.73294 -5.76087  1.000 40.87479  ? 199 GLU   A CG  1 
ATOM   1426 C CD  . GLU   A 1 192 ? -8.64193  -25.94276 -4.44651  1.000 66.89464  ? 199 GLU   A CD  1 
ATOM   1427 O OE1 . GLU   A 1 192 ? -7.98367  -26.99622 -4.28182  1.000 74.98359  ? 199 GLU   A OE1 1 
ATOM   1428 O OE2 . GLU   A 1 192 ? -8.75721  -25.06879 -3.56609  1.000 75.34279  ? 199 GLU   A OE2 1 
ATOM   1429 N N   . GLU   A 1 193 ? -12.54049 -22.86212 -7.59500  1.000 26.08903  ? 200 GLU   A N   1 
ATOM   1430 C CA  . GLU   A 1 193 ? -13.36067 -21.67796 -7.85486  1.000 27.27188  ? 200 GLU   A CA  1 
ATOM   1431 C C   . GLU   A 1 193 ? -13.17793 -20.60747 -6.77864  1.000 24.78048  ? 200 GLU   A C   1 
ATOM   1432 O O   . GLU   A 1 193 ? -13.00726 -19.42179 -7.09674  1.000 25.48129  ? 200 GLU   A O   1 
ATOM   1433 C CB  . GLU   A 1 193 ? -14.84243 -22.06952 -7.94590  1.000 28.78488  ? 200 GLU   A CB  1 
ATOM   1434 C CG  . GLU   A 1 193 ? -15.73502 -20.87864 -8.24702  1.000 30.98015  ? 200 GLU   A CG  1 
ATOM   1435 C CD  . GLU   A 1 193 ? -17.20390 -21.22829 -8.37081  1.000 54.01696  ? 200 GLU   A CD  1 
ATOM   1436 O OE1 . GLU   A 1 193 ? -17.60134 -22.29716 -7.87303  1.000 43.62254  ? 200 GLU   A OE1 1 
ATOM   1437 O OE2 . GLU   A 1 193 ? -17.95909 -20.42127 -8.95376  1.000 46.17202  ? 200 GLU   A OE2 1 
ATOM   1438 N N   . ARG   A 1 194 ? -13.22773 -21.00622 -5.49929  1.000 29.55615  ? 201 ARG   A N   1 
ATOM   1439 C CA  . ARG   A 1 194 ? -13.15659 -20.00021 -4.43876  1.000 24.94629  ? 201 ARG   A CA  1 
ATOM   1440 C C   . ARG   A 1 194 ? -11.80093 -19.30661 -4.43976  1.000 25.15810  ? 201 ARG   A C   1 
ATOM   1441 O O   . ARG   A 1 194 ? -11.71213 -18.11941 -4.10177  1.000 26.02725  ? 201 ARG   A O   1 
ATOM   1442 C CB  . ARG   A 1 194 ? -13.42610 -20.61100 -3.06055  1.000 30.52965  ? 201 ARG   A CB  1 
ATOM   1443 C CG  . ARG   A 1 194 ? -12.60249 -21.81537 -2.73385  1.000 33.38853  ? 201 ARG   A CG  1 
ATOM   1444 C CD  . ARG   A 1 194 ? -13.09943 -22.38178 -1.40182  1.000 39.68382  ? 201 ARG   A CD  1 
ATOM   1445 N NE  . ARG   A 1 194 ? -12.11939 -23.24465 -0.77701  1.000 50.51417  ? 201 ARG   A NE  1 
ATOM   1446 C CZ  . ARG   A 1 194 ? -12.26233 -23.71478 0.45160   1.000 41.81678  ? 201 ARG   A CZ  1 
ATOM   1447 N NH1 . ARG   A 1 194 ? -13.36198 -23.47291 1.15576   1.000 49.75514  ? 201 ARG   A NH1 1 
ATOM   1448 N NH2 . ARG   A 1 194 ? -11.29537 -24.46133 0.97313   1.000 47.55378  ? 201 ARG   A NH2 1 
ATOM   1449 N N   . ARG   A 1 195 ? -10.73512 -20.03075 -4.80345  1.000 24.73233  ? 202 ARG   A N   1 
ATOM   1450 C CA  . ARG   A 1 195 ? -9.41271  -19.41343 -4.83420  1.000 23.17016  ? 202 ARG   A CA  1 
ATOM   1451 C C   . ARG   A 1 195 ? -9.30505  -18.41875 -5.98334  1.000 23.10479  ? 202 ARG   A C   1 
ATOM   1452 O O   . ARG   A 1 195 ? -8.78994  -17.31000 -5.80204  1.000 22.83805  ? 202 ARG   A O   1 
ATOM   1453 C CB  . ARG   A 1 195 ? -8.32449  -20.48655 -4.95500  1.000 25.23906  ? 202 ARG   A CB  1 
ATOM   1454 C CG  . ARG   A 1 195 ? -6.84942  -20.00951 -4.90904  1.000 23.44327  ? 202 ARG   A CG  1 
ATOM   1455 C CD  . ARG   A 1 195 ? -6.47694  -19.40761 -3.53842  1.000 26.55352  ? 202 ARG   A CD  1 
ATOM   1456 N NE  . ARG   A 1 195 ? -5.03838  -19.19810 -3.47340  1.000 26.59321  ? 202 ARG   A NE  1 
ATOM   1457 C CZ  . ARG   A 1 195 ? -4.44151  -18.01915 -3.32228  1.000 29.78722  ? 202 ARG   A CZ  1 
ATOM   1458 N NH1 . ARG   A 1 195 ? -5.13309  -16.91333 -3.12035  1.000 27.91936  ? 202 ARG   A NH1 1 
ATOM   1459 N NH2 . ARG   A 1 195 ? -3.11047  -17.95092 -3.38411  1.000 31.19662  ? 202 ARG   A NH2 1 
ATOM   1460 N N   . ILE   A 1 196 ? -9.77739  -18.79500 -7.17629  1.000 21.87870  ? 203 ILE   A N   1 
ATOM   1461 C CA  . ILE   A 1 196 ? -9.72845  -17.86152 -8.30136  1.000 20.26301  ? 203 ILE   A CA  1 
ATOM   1462 C C   . ILE   A 1 196 ? -10.54659 -16.61340 -7.99643  1.000 20.17344  ? 203 ILE   A C   1 
ATOM   1463 O O   . ILE   A 1 196 ? -10.07570 -15.48330 -8.20729  1.000 21.70419  ? 203 ILE   A O   1 
ATOM   1464 C CB  . ILE   A 1 196 ? -10.20623 -18.54398 -9.59403  1.000 20.49838  ? 203 ILE   A CB  1 
ATOM   1465 C CG1 . ILE   A 1 196 ? -9.28064  -19.71539 -9.93482  1.000 23.05179  ? 203 ILE   A CG1 1 
ATOM   1466 C CG2 . ILE   A 1 196 ? -10.22157 -17.51886 -10.71522 1.000 19.79861  ? 203 ILE   A CG2 1 
ATOM   1467 C CD1 . ILE   A 1 196 ? -9.95756  -20.76679 -10.90043 1.000 25.47378  ? 203 ILE   A CD1 1 
ATOM   1468 N N   . LYS   A 1 197 ? -11.76939 -16.79461 -7.46636  1.000 21.61051  ? 204 LYS   A N   1 
ATOM   1469 C CA  . LYS   A 1 197 ? -12.61291 -15.64877 -7.12490  1.000 20.49978  ? 204 LYS   A CA  1 
ATOM   1470 C C   . LYS   A 1 197 ? -11.90818 -14.71243 -6.16473  1.000 22.96497  ? 204 LYS   A C   1 
ATOM   1471 O O   . LYS   A 1 197 ? -12.01382 -13.48702 -6.28870  1.000 24.21351  ? 204 LYS   A O   1 
ATOM   1472 C CB  . LYS   A 1 197 ? -13.94265 -16.06713 -6.48388  1.000 25.08626  ? 204 LYS   A CB  1 
ATOM   1473 C CG  . LYS   A 1 197 ? -14.94210 -16.63026 -7.43031  1.000 27.97176  ? 204 LYS   A CG  1 
ATOM   1474 C CD  . LYS   A 1 197 ? -16.21527 -16.99878 -6.65051  1.000 33.78863  ? 204 LYS   A CD  1 
ATOM   1475 C CE  . LYS   A 1 197 ? -17.22886 -17.66949 -7.56478  1.000 51.70714  ? 204 LYS   A CE  1 
ATOM   1476 N NZ  . LYS   A 1 197 ? -18.16331 -18.54979 -6.79834  1.000 54.51111  ? 204 LYS   A NZ  1 
ATOM   1477 N N   . GLU   A 1 198 ? -11.25871 -15.28082 -5.14128  1.000 22.38646  ? 205 GLU   A N   1 
ATOM   1478 C CA  . GLU   A 1 198 ? -10.57595 -14.46597 -4.14322  1.000 21.70312  ? 205 GLU   A CA  1 
ATOM   1479 C C   . GLU   A 1 198 ? -9.50481  -13.60778 -4.80376  1.000 21.38029  ? 205 GLU   A C   1 
ATOM   1480 O O   . GLU   A 1 198 ? -9.35353  -12.42317 -4.47817  1.000 25.10319  ? 205 GLU   A O   1 
ATOM   1481 C CB  . GLU   A 1 198 ? -9.96421  -15.37871 -3.07097  1.000 22.27694  ? 205 GLU   A CB  1 
ATOM   1482 C CG  . GLU   A 1 198 ? -9.01678  -14.70511 -2.06762  1.000 27.57741  ? 205 GLU   A CG  1 
ATOM   1483 C CD  . GLU   A 1 198 ? -8.34479  -15.71373 -1.15417  1.000 27.05869  ? 205 GLU   A CD  1 
ATOM   1484 O OE1 . GLU   A 1 198 ? -7.74500  -16.67757 -1.70152  1.000 29.91560  ? 205 GLU   A OE1 1 
ATOM   1485 O OE2 . GLU   A 1 198 ? -8.37213  -15.51360 0.08420   1.000 29.01719  ? 205 GLU   A OE2 1 
ATOM   1486 N N   . ILE   A 1 199 ? -8.71789  -14.21672 -5.68835  1.000 20.52845  ? 206 ILE   A N   1 
ATOM   1487 C CA  . ILE   A 1 199 ? -7.61058  -13.50979 -6.33037  1.000 21.17921  ? 206 ILE   A CA  1 
ATOM   1488 C C   . ILE   A 1 199 ? -8.12668  -12.42075 -7.26551  1.000 21.03163  ? 206 ILE   A C   1 
ATOM   1489 O O   . ILE   A 1 199 ? -7.57139  -11.32398 -7.31916  1.000 23.94755  ? 206 ILE   A O   1 
ATOM   1490 C CB  . ILE   A 1 199 ? -6.73169  -14.52390 -7.08619  1.000 22.15649  ? 206 ILE   A CB  1 
ATOM   1491 C CG1 . ILE   A 1 199 ? -6.12601  -15.51333 -6.07553  1.000 23.81527  ? 206 ILE   A CG1 1 
ATOM   1492 C CG2 . ILE   A 1 199 ? -5.67586  -13.82374 -7.93504  1.000 24.29268  ? 206 ILE   A CG2 1 
ATOM   1493 C CD1 . ILE   A 1 199 ? -5.54711  -16.74795 -6.82308  1.000 26.76963  ? 206 ILE   A CD1 1 
ATOM   1494 N N   . VAL   A 1 200 ? -9.15592  -12.72370 -8.05890  1.000 21.18367  ? 207 VAL   A N   1 
ATOM   1495 C CA  . VAL   A 1 200 ? -9.72256  -11.70565 -8.93916  1.000 20.31391  ? 207 VAL   A CA  1 
ATOM   1496 C C   . VAL   A 1 200 ? -10.25102 -10.53687 -8.12306  1.000 22.35855  ? 207 VAL   A C   1 
ATOM   1497 O O   . VAL   A 1 200 ? -10.03196 -9.36379  -8.45946  1.000 25.21342  ? 207 VAL   A O   1 
ATOM   1498 C CB  . VAL   A 1 200 ? -10.82548 -12.34063 -9.79033  1.000 21.32572  ? 207 VAL   A CB  1 
ATOM   1499 C CG1 . VAL   A 1 200 ? -11.62931 -11.24147 -10.52494 1.000 24.13331  ? 207 VAL   A CG1 1 
ATOM   1500 C CG2 . VAL   A 1 200 ? -10.19243 -13.34196 -10.74780 1.000 22.01281  ? 207 VAL   A CG2 1 
ATOM   1501 N N   . LYS   A 1 201 ? -10.90909 -10.82612 -6.99619  1.000 21.58687  ? 208 LYS   A N   1 
ATOM   1502 C CA  . LYS   A 1 201 ? -11.44050 -9.74090  -6.19496  1.000 23.86775  ? 208 LYS   A CA  1 
ATOM   1503 C C   . LYS   A 1 201 ? -10.31779 -8.91276  -5.57484  1.000 26.15043  ? 208 LYS   A C   1 
ATOM   1504 O O   . LYS   A 1 201 ? -10.43401 -7.69077  -5.45914  1.000 32.76284  ? 208 LYS   A O   1 
ATOM   1505 C CB  . LYS   A 1 201 ? -12.35863 -10.31074 -5.11109  1.000 23.31610  ? 208 LYS   A CB  1 
ATOM   1506 C CG  . LYS   A 1 201 ? -13.05761 -9.27461  -4.25351  1.000 34.05628  ? 208 LYS   A CG  1 
ATOM   1507 C CD  . LYS   A 1 201 ? -13.76719 -9.95609  -3.09483  1.000 40.96833  ? 208 LYS   A CD  1 
ATOM   1508 C CE  . LYS   A 1 201 ? -14.46235 -8.95926  -2.19066  1.000 46.81629  ? 208 LYS   A CE  1 
ATOM   1509 N NZ  . LYS   A 1 201 ? -15.26837 -9.66883  -1.14811  1.000 54.88014  ? 208 LYS   A NZ  1 
ATOM   1510 N N   . LYS   A 1 202 ? -9.22306  -9.57328  -5.15989  1.000 26.72005  ? 209 LYS   A N   1 
ATOM   1511 C CA  . LYS   A 1 202 ? -8.12040  -8.88769  -4.48925  1.000 29.67543  ? 209 LYS   A CA  1 
ATOM   1512 C C   . LYS   A 1 202 ? -7.32763  -7.99067  -5.42935  1.000 25.32636  ? 209 LYS   A C   1 
ATOM   1513 O O   . LYS   A 1 202 ? -6.93500  -6.88344  -5.03558  1.000 28.83598  ? 209 LYS   A O   1 
ATOM   1514 C CB  . LYS   A 1 202 ? -7.18738  -9.91125  -3.86095  1.000 26.95494  ? 209 LYS   A CB  1 
ATOM   1515 C CG  . LYS   A 1 202 ? -6.03276  -9.31653  -3.09906  1.000 30.53414  ? 209 LYS   A CG  1 
ATOM   1516 C CD  . LYS   A 1 202 ? -5.04533  -10.38752 -2.70832  1.000 46.30469  ? 209 LYS   A CD  1 
ATOM   1517 C CE  . LYS   A 1 202 ? -5.69043  -11.41355 -1.80467  1.000 54.83232  ? 209 LYS   A CE  1 
ATOM   1518 N NZ  . LYS   A 1 202 ? -6.24726  -12.59297 -2.56543  1.000 57.61657  ? 209 LYS   A NZ  1 
ATOM   1519 N N   . HIS   A 1 203 ? -7.06179  -8.46387  -6.65850  1.000 27.09725  ? 210 HIS   A N   1 
ATOM   1520 C CA  . HIS   A 1 203 ? -6.06939  -7.82843  -7.52113  1.000 30.78838  ? 210 HIS   A CA  1 
ATOM   1521 C C   . HIS   A 1 203 ? -6.60564  -7.29321  -8.84473  1.000 28.52695  ? 210 HIS   A C   1 
ATOM   1522 O O   . HIS   A 1 203 ? -5.90630  -6.49176  -9.48479  1.000 29.64742  ? 210 HIS   A O   1 
ATOM   1523 C CB  . HIS   A 1 203 ? -4.92313  -8.81101  -7.83693  1.000 29.62146  ? 210 HIS   A CB  1 
ATOM   1524 C CG  . HIS   A 1 203 ? -4.08314  -9.16873  -6.65028  1.000 32.70525  ? 210 HIS   A CG  1 
ATOM   1525 N ND1 . HIS   A 1 203 ? -3.41393  -8.22932  -5.89668  1.000 33.72172  ? 210 HIS   A ND1 1 
ATOM   1526 C CD2 . HIS   A 1 203 ? -3.77399  -10.37242 -6.10942  1.000 38.82855  ? 210 HIS   A CD2 1 
ATOM   1527 C CE1 . HIS   A 1 203 ? -2.75081  -8.83384  -4.92665  1.000 40.48273  ? 210 HIS   A CE1 1 
ATOM   1528 N NE2 . HIS   A 1 203 ? -2.95036  -10.13528 -5.03644  1.000 41.19039  ? 210 HIS   A NE2 1 
ATOM   1529 N N   . SER   A 1 204 ? -7.81458  -7.67685  -9.25607  1.000 25.69001  ? 211 SER   A N   1 
ATOM   1530 C CA  . SER   A 1 204 ? -8.34715  -7.35309  -10.57541 1.000 27.05857  ? 211 SER   A CA  1 
ATOM   1531 C C   . SER   A 1 204 ? -9.74852  -6.76633  -10.48173 1.000 25.36254  ? 211 SER   A C   1 
ATOM   1532 O O   . SER   A 1 204 ? -10.54023 -6.88130  -11.41176 1.000 26.43653  ? 211 SER   A O   1 
ATOM   1533 C CB  . SER   A 1 204 ? -8.31947  -8.58941  -11.48607 1.000 25.90186  ? 211 SER   A CB  1 
ATOM   1534 O OG  . SER   A 1 204 ? -6.97773  -9.05358  -11.59835 1.000 26.28294  ? 211 SER   A OG  1 
ATOM   1535 N N   . GLN   A 1 205 ? -10.05714 -6.11563  -9.36463  1.000 30.39739  ? 212 GLN   A N   1 
ATOM   1536 C CA  . GLN   A 1 205 ? -11.44042 -5.73197  -9.11729  1.000 36.20492  ? 212 GLN   A CA  1 
ATOM   1537 C C   . GLN   A 1 205 ? -11.87922 -4.53469  -9.95649  1.000 32.96221  ? 212 GLN   A C   1 
ATOM   1538 O O   . GLN   A 1 205 ? -13.08555 -4.32759  -10.12225 1.000 42.09390  ? 212 GLN   A O   1 
ATOM   1539 C CB  . GLN   A 1 205 ? -11.64850 -5.46866  -7.62537  1.000 37.54649  ? 212 GLN   A CB  1 
ATOM   1540 C CG  . GLN   A 1 205 ? -10.95087 -4.24445  -7.11575  1.000 38.48237  ? 212 GLN   A CG  1 
ATOM   1541 C CD  . GLN   A 1 205 ? -9.58132  -4.51893  -6.46211  1.000 61.83434  ? 212 GLN   A CD  1 
ATOM   1542 O OE1 . GLN   A 1 205 ? -8.69779  -5.19413  -7.02887  1.000 40.86939  ? 212 GLN   A OE1 1 
ATOM   1543 N NE2 . GLN   A 1 205 ? -9.40446  -3.97632  -5.25452  1.000 50.38434  ? 212 GLN   A NE2 1 
ATOM   1544 N N   . PHE   A 1 206 ? -10.94449 -3.76720  -10.52326 1.000 28.19002  ? 213 PHE   A N   1 
ATOM   1545 C CA  . PHE   A 1 206 ? -11.29126 -2.58985  -11.31624 1.000 32.02687  ? 213 PHE   A CA  1 
ATOM   1546 C C   . PHE   A 1 206 ? -11.02226 -2.74087  -12.82236 1.000 33.25064  ? 213 PHE   A C   1 
ATOM   1547 O O   . PHE   A 1 206 ? -11.06350 -1.74058  -13.54135 1.000 41.29425  ? 213 PHE   A O   1 
ATOM   1548 C CB  . PHE   A 1 206 ? -10.56745 -1.36018  -10.78128 1.000 35.98455  ? 213 PHE   A CB  1 
ATOM   1549 C CG  . PHE   A 1 206 ? -10.92443 -1.03469  -9.35301  1.000 38.34734  ? 213 PHE   A CG  1 
ATOM   1550 C CD1 . PHE   A 1 206 ? -12.22192 -0.68922  -9.02034  1.000 43.76949  ? 213 PHE   A CD1 1 
ATOM   1551 C CD2 . PHE   A 1 206 ? -9.96892  -1.08357  -8.35175  1.000 42.92174  ? 213 PHE   A CD2 1 
ATOM   1552 C CE1 . PHE   A 1 206 ? -12.56370 -0.38934  -7.70761  1.000 46.09796  ? 213 PHE   A CE1 1 
ATOM   1553 C CE2 . PHE   A 1 206 ? -10.30366 -0.78475  -7.04282  1.000 50.25748  ? 213 PHE   A CE2 1 
ATOM   1554 C CZ  . PHE   A 1 206 ? -11.60542 -0.44246  -6.72428  1.000 43.66647  ? 213 PHE   A CZ  1 
ATOM   1555 N N   . ILE   A 1 207 ? -10.77220 -3.95611  -13.32080 1.000 24.52144  ? 214 ILE   A N   1 
ATOM   1556 C CA  . ILE   A 1 207 ? -10.58624 -4.18264  -14.75950 1.000 22.35389  ? 214 ILE   A CA  1 
ATOM   1557 C C   . ILE   A 1 207 ? -11.87288 -3.83713  -15.51243 1.000 28.13410  ? 214 ILE   A C   1 
ATOM   1558 O O   . ILE   A 1 207 ? -12.97076 -4.23159  -15.10274 1.000 27.49901  ? 214 ILE   A O   1 
ATOM   1559 C CB  . ILE   A 1 207 ? -10.16595 -5.64810  -14.99447 1.000 22.33584  ? 214 ILE   A CB  1 
ATOM   1560 C CG1 . ILE   A 1 207 ? -8.75893  -5.89395  -14.40812 1.000 22.68197  ? 214 ILE   A CG1 1 
ATOM   1561 C CG2 . ILE   A 1 207 ? -10.20797 -6.05759  -16.48394 1.000 23.02581  ? 214 ILE   A CG2 1 
ATOM   1562 C CD1 . ILE   A 1 207 ? -7.64431  -5.20562  -15.14781 1.000 26.32091  ? 214 ILE   A CD1 1 
ATOM   1563 N N   . GLY   A 1 208 ? -11.74287 -3.10244  -16.62138 1.000 24.42565  ? 215 GLY   A N   1 
ATOM   1564 C CA  . GLY   A 1 208 ? -12.89367 -2.52733  -17.29930 1.000 24.96262  ? 215 GLY   A CA  1 
ATOM   1565 C C   . GLY   A 1 208 ? -13.53027 -3.39784  -18.36893 1.000 22.22129  ? 215 GLY   A C   1 
ATOM   1566 O O   . GLY   A 1 208 ? -14.12395 -2.88367  -19.32842 1.000 28.00045  ? 215 GLY   A O   1 
ATOM   1567 N N   . TYR   A 1 209 ? -13.42467 -4.70442  -18.20990 1.000 21.09581  ? 216 TYR   A N   1 
ATOM   1568 C CA  . TYR   A 1 209 ? -14.01830 -5.67937  -19.11781 1.000 21.76213  ? 216 TYR   A CA  1 
ATOM   1569 C C   . TYR   A 1 209 ? -14.60326 -6.77918  -18.24768 1.000 23.90289  ? 216 TYR   A C   1 
ATOM   1570 O O   . TYR   A 1 209 ? -14.06799 -7.07391  -17.17283 1.000 23.69642  ? 216 TYR   A O   1 
ATOM   1571 C CB  . TYR   A 1 209 ? -12.97354 -6.28217  -20.07682 1.000 20.18528  ? 216 TYR   A CB  1 
ATOM   1572 C CG  . TYR   A 1 209 ? -12.36822 -5.21831  -20.94422 1.000 21.03745  ? 216 TYR   A CG  1 
ATOM   1573 C CD1 . TYR   A 1 209 ? -13.00311 -4.80450  -22.11543 1.000 21.19577  ? 216 TYR   A CD1 1 
ATOM   1574 C CD2 . TYR   A 1 209 ? -11.14214 -4.61267  -20.61502 1.000 21.18005  ? 216 TYR   A CD2 1 
ATOM   1575 C CE1 . TYR   A 1 209 ? -12.48527 -3.80875  -22.89039 1.000 22.16132  ? 216 TYR   A CE1 1 
ATOM   1576 C CE2 . TYR   A 1 209 ? -10.61079 -3.61023  -21.39327 1.000 20.39533  ? 216 TYR   A CE2 1 
ATOM   1577 C CZ  . TYR   A 1 209 ? -11.27804 -3.20341  -22.55734 1.000 20.41511  ? 216 TYR   A CZ  1 
ATOM   1578 O OH  . TYR   A 1 209 ? -10.82327 -2.19333  -23.36602 1.000 23.15851  ? 216 TYR   A OH  1 
ATOM   1579 N N   . PRO   A 1 210 ? -15.67645 -7.42755  -18.69351 1.000 21.62561  ? 217 PRO   A N   1 
ATOM   1580 C CA  . PRO   A 1 210 ? -16.25238 -8.52435  -17.89993 1.000 19.74114  ? 217 PRO   A CA  1 
ATOM   1581 C C   . PRO   A 1 210 ? -15.31439 -9.71145  -17.77550 1.000 22.13760  ? 217 PRO   A C   1 
ATOM   1582 O O   . PRO   A 1 210 ? -14.77667 -10.20810 -18.76640 1.000 22.01749  ? 217 PRO   A O   1 
ATOM   1583 C CB  . PRO   A 1 210 ? -17.53493 -8.89339  -18.67081 1.000 23.40620  ? 217 PRO   A CB  1 
ATOM   1584 C CG  . PRO   A 1 210 ? -17.37820 -8.34641  -20.00238 1.000 28.51893  ? 217 PRO   A CG  1 
ATOM   1585 C CD  . PRO   A 1 210 ? -16.46155 -7.13385  -19.90303 1.000 23.91385  ? 217 PRO   A CD  1 
ATOM   1586 N N   . ILE   A 1 211 ? -15.13468 -10.18954 -16.54446 1.000 20.85914  ? 218 ILE   A N   1 
ATOM   1587 C CA  . ILE   A 1 211 ? -14.32027 -11.36882 -16.28660 1.000 18.71573  ? 218 ILE   A CA  1 
ATOM   1588 C C   . ILE   A 1 211 ? -15.26584 -12.46388 -15.83506 1.000 20.39430  ? 218 ILE   A C   1 
ATOM   1589 O O   . ILE   A 1 211 ? -15.91822 -12.33098 -14.78891 1.000 24.66284  ? 218 ILE   A O   1 
ATOM   1590 C CB  . ILE   A 1 211 ? -13.25855 -11.10096 -15.20998 1.000 19.12606  ? 218 ILE   A CB  1 
ATOM   1591 C CG1 . ILE   A 1 211 ? -12.26353 -10.02224 -15.68875 1.000 20.07910  ? 218 ILE   A CG1 1 
ATOM   1592 C CG2 . ILE   A 1 211 ? -12.54411 -12.38280 -14.86043 1.000 21.77038  ? 218 ILE   A CG2 1 
ATOM   1593 C CD1 . ILE   A 1 211 ? -11.37334 -9.48887  -14.51882 1.000 19.88308  ? 218 ILE   A CD1 1 
ATOM   1594 N N   . THR   A 1 212 ? -15.35628 -13.52946 -16.62255 1.000 19.60120  ? 219 THR   A N   1 
ATOM   1595 C CA  . THR   A 1 212 ? -16.29339 -14.61110 -16.33756 1.000 18.23153  ? 219 THR   A CA  1 
ATOM   1596 C C   . THR   A 1 212 ? -15.46768 -15.80912 -15.90815 1.000 18.64666  ? 219 THR   A C   1 
ATOM   1597 O O   . THR   A 1 212 ? -14.62212 -16.28673 -16.66726 1.000 19.39194  ? 219 THR   A O   1 
ATOM   1598 C CB  . THR   A 1 212 ? -17.13954 -14.96682 -17.55889 1.000 19.19868  ? 219 THR   A CB  1 
ATOM   1599 O OG1 . THR   A 1 212 ? -17.89805 -13.82089 -17.97008 1.000 22.23491  ? 219 THR   A OG1 1 
ATOM   1600 C CG2 . THR   A 1 212 ? -18.14114 -16.14070 -17.20439 1.000 19.92091  ? 219 THR   A CG2 1 
ATOM   1601 N N   . LEU   A 1 213 ? -15.69024 -16.27648 -14.68263 1.000 20.25968  ? 220 LEU   A N   1 
ATOM   1602 C CA  . LEU   A 1 213 ? -15.05559 -17.49107 -14.18598 1.000 19.33303  ? 220 LEU   A CA  1 
ATOM   1603 C C   . LEU   A 1 213 ? -15.97171 -18.67234 -14.50620 1.000 19.67110  ? 220 LEU   A C   1 
ATOM   1604 O O   . LEU   A 1 213 ? -17.07490 -18.78381 -13.96247 1.000 21.93073  ? 220 LEU   A O   1 
ATOM   1605 C CB  . LEU   A 1 213 ? -14.78349 -17.38631 -12.68071 1.000 19.47886  ? 220 LEU   A CB  1 
ATOM   1606 C CG  . LEU   A 1 213 ? -14.29278 -18.65497 -11.98534 1.000 23.57548  ? 220 LEU   A CG  1 
ATOM   1607 C CD1 . LEU   A 1 213 ? -13.02583 -19.23063 -12.61692 1.000 23.33975  ? 220 LEU   A CD1 1 
ATOM   1608 C CD2 . LEU   A 1 213 ? -14.03755 -18.32023 -10.46361 1.000 25.01015  ? 220 LEU   A CD2 1 
ATOM   1609 N N   . PHE   A 1 214 ? -15.52160 -19.54186 -15.41816 1.000 18.07001  ? 221 PHE   A N   1 
ATOM   1610 C CA  . PHE   A 1 214 ? -16.27407 -20.71642 -15.77902 1.000 19.96112  ? 221 PHE   A CA  1 
ATOM   1611 C C   . PHE   A 1 214 ? -16.24294 -21.72002 -14.62652 1.000 23.39703  ? 221 PHE   A C   1 
ATOM   1612 O O   . PHE   A 1 214 ? -15.28004 -21.73965 -13.83189 1.000 24.29337  ? 221 PHE   A O   1 
ATOM   1613 C CB  . PHE   A 1 214 ? -15.69054 -21.39508 -17.03497 1.000 22.70743  ? 221 PHE   A CB  1 
ATOM   1614 C CG  . PHE   A 1 214 ? -15.94868 -20.68135 -18.35349 1.000 19.02422  ? 221 PHE   A CG  1 
ATOM   1615 C CD1 . PHE   A 1 214 ? -16.02728 -19.29768 -18.44499 1.000 20.47160  ? 221 PHE   A CD1 1 
ATOM   1616 C CD2 . PHE   A 1 214 ? -16.06930 -21.45159 -19.51632 1.000 20.26931  ? 221 PHE   A CD2 1 
ATOM   1617 C CE1 . PHE   A 1 214 ? -16.25525 -18.68543 -19.69322 1.000 19.22859  ? 221 PHE   A CE1 1 
ATOM   1618 C CE2 . PHE   A 1 214 ? -16.26821 -20.85086 -20.76578 1.000 22.09274  ? 221 PHE   A CE2 1 
ATOM   1619 C CZ  . PHE   A 1 214 ? -16.37225 -19.47398 -20.84730 1.000 19.47820  ? 221 PHE   A CZ  1 
ATOM   1620 N N   . VAL   A 1 215 ? -17.29465 -22.52134 -14.52094 1.000 24.35419  ? 222 VAL   A N   1 
ATOM   1621 C CA  . VAL   A 1 215 ? -17.33416 -23.59387 -13.53330 1.000 27.91008  ? 222 VAL   A CA  1 
ATOM   1622 C C   . VAL   A 1 215 ? -17.19910 -24.94026 -14.22321 1.000 30.80302  ? 222 VAL   A C   1 
ATOM   1623 O O   . VAL   A 1 215 ? -17.31220 -25.06118 -15.44474 1.000 31.07375  ? 222 VAL   A O   1 
ATOM   1624 C CB  . VAL   A 1 215 ? -18.58068 -23.52689 -12.64151 1.000 40.83846  ? 222 VAL   A CB  1 
ATOM   1625 C CG1 . VAL   A 1 215 ? -18.33367 -22.50514 -11.51431 1.000 43.37575  ? 222 VAL   A CG1 1 
ATOM   1626 C CG2 . VAL   A 1 215 ? -19.77394 -23.16140 -13.42199 1.000 32.83977  ? 222 VAL   A CG2 1 
ATOM   1627 N N   . GLU   A 1 216 ? -16.93446 -25.96689 -13.42805 1.000 30.79863  ? 223 GLU   A N   1 
ATOM   1628 C CA  . GLU   A 1 216 ? -16.76089 -27.30944 -13.97256 1.000 36.24667  ? 223 GLU   A CA  1 
ATOM   1629 C C   . GLU   A 1 216 ? -17.88116 -28.24990 -13.55206 1.000 42.87320  ? 223 GLU   A C   1 
ATOM   1630 O O   . GLU   A 1 216 ? -18.46866 -28.08913 -12.48162 1.000 47.32731  ? 223 GLU   A O   1 
ATOM   1631 C CB  . GLU   A 1 216 ? -15.41146 -27.87889 -13.53315 1.000 38.05278  ? 223 GLU   A CB  1 
ATOM   1632 C CG  . GLU   A 1 216 ? -14.25809 -26.97637 -13.92488 1.000 34.02044  ? 223 GLU   A CG  1 
ATOM   1633 C CD  . GLU   A 1 216 ? -12.92376 -27.51223 -13.45672 1.000 36.86068  ? 223 GLU   A CD  1 
ATOM   1634 O OE1 . GLU   A 1 216 ? -12.52042 -28.59375 -13.93623 1.000 35.79863  ? 223 GLU   A OE1 1 
ATOM   1635 O OE2 . GLU   A 1 216 ? -12.29360 -26.84448 -12.59653 1.000 38.53035  ? 223 GLU   A OE2 1 
ATOM   1636 N N   . LYS   A 1 217 ? -18.16587 -29.24662 -14.40670 1.000 45.20340  ? 224 LYS   A N   1 
ATOM   1637 C CA  . LYS   A 1 217 ? -19.07527 -30.33576 -14.04763 1.000 57.06662  ? 224 LYS   A CA  1 
ATOM   1638 C C   . LYS   A 1 217 ? -18.64754 -31.00773 -12.74053 1.000 65.57376  ? 224 LYS   A C   1 
ATOM   1639 O O   . LYS   A 1 217 ? -17.45562 -31.18883 -12.49015 1.000 58.98898  ? 224 LYS   A O   1 
ATOM   1640 C CB  . LYS   A 1 217 ? -19.15721 -31.39738 -15.15619 1.000 50.85883  ? 224 LYS   A CB  1 
ATOM   1641 C CG  . LYS   A 1 217 ? -20.14974 -32.50780 -14.81526 1.000 64.43910  ? 224 LYS   A CG  1 
ATOM   1642 C CD  . LYS   A 1 217 ? -19.93256 -33.78935 -15.61936 1.000 67.09291  ? 224 LYS   A CD  1 
ATOM   1643 C CE  . LYS   A 1 217 ? -20.00179 -35.01057 -14.70152 1.000 77.37491  ? 224 LYS   A CE  1 
ATOM   1644 N NZ  . LYS   A 1 217 ? -21.23727 -35.03355 -13.86104 1.000 80.03982  ? 224 LYS   A NZ  1 
HETATM 1645 C C1  . A1AX3 B 2 .   ? 2.30209   -9.79230  -23.54113 1.000 23.08590  ? 301 A1AX3 A C1  1 
HETATM 1646 C C2  . A1AX3 B 2 .   ? 1.21777   -10.82017 -23.79986 1.000 18.12836  ? 301 A1AX3 A C2  1 
HETATM 1647 C C3  . A1AX3 B 2 .   ? 1.51801   -12.17336 -23.71429 0.794 15.99037  ? 301 A1AX3 A C3  1 
HETATM 1648 N N1  . A1AX3 B 2 .   ? -3.43479  -11.47926 -23.83871 1.000 20.81472  ? 301 A1AX3 A N1  1 
HETATM 1649 C C4  . A1AX3 B 2 .   ? 0.56223   -13.14402 -23.92248 1.000 19.95084  ? 301 A1AX3 A C4  1 
HETATM 1650 C C5  . A1AX3 B 2 .   ? -0.73304  -12.75579 -24.21271 0.884 18.42863  ? 301 A1AX3 A C5  1 
HETATM 1651 C C6  . A1AX3 B 2 .   ? -1.07229  -11.40821 -24.27466 0.836 17.43642  ? 301 A1AX3 A C6  1 
HETATM 1652 C C7  . A1AX3 B 2 .   ? -2.47274  -11.04663 -24.64206 0.770 16.83142  ? 301 A1AX3 A C7  1 
HETATM 1653 C C8  . A1AX3 B 2 .   ? -0.09498  -10.41537 -24.09535 1.000 21.37730  ? 301 A1AX3 A C8  1 
HETATM 1654 C C9  . A1AX3 B 2 .   ? -0.42979  -8.93933  -24.18077 1.000 23.27193  ? 301 A1AX3 A C9  1 
HETATM 1655 O O1  . A1AX3 B 2 .   ? -2.71020  -10.44447 -25.69797 0.888 19.76509  ? 301 A1AX3 A O1  1 
HETATM 1656 O O   . HOH   C 3 .   ? -8.63993  -23.47491 -2.60586  1.000 55.02436  ? 401 HOH   A O   1 
HETATM 1657 O O   . HOH   C 3 .   ? 5.52661   -7.52126  -34.16898 1.000 52.49398  ? 402 HOH   A O   1 
HETATM 1658 O O   . HOH   C 3 .   ? 17.79066  -3.98030  -8.18342  1.000 58.83183  ? 403 HOH   A O   1 
HETATM 1659 O O   . HOH   C 3 .   ? -7.69373  -24.13964 -26.00414 1.000 50.27955  ? 404 HOH   A O   1 
HETATM 1660 O O   . HOH   C 3 .   ? 11.46665  -22.04677 -40.58591 1.000 47.58356  ? 405 HOH   A O   1 
HETATM 1661 O O   . HOH   C 3 .   ? 9.28204   -3.33422  -20.56636 1.000 39.71687  ? 406 HOH   A O   1 
HETATM 1662 O O   . HOH   C 3 .   ? -20.36470 -20.38598 -9.30422  1.000 51.13990  ? 407 HOH   A O   1 
HETATM 1663 O O   . HOH   C 3 .   ? -1.63174  -28.94450 -5.88296  1.000 35.80126  ? 408 HOH   A O   1 
HETATM 1664 O O   . HOH   C 3 .   ? 13.56219  -8.80062  -30.61975 1.000 46.52556  ? 409 HOH   A O   1 
HETATM 1665 O O   . HOH   C 3 .   ? -4.02514  -13.41450 -42.94469 1.000 54.55900  ? 410 HOH   A O   1 
HETATM 1666 O O   . HOH   C 3 .   ? -16.18527 -25.41236 -17.69276 1.000 27.05014  ? 411 HOH   A O   1 
HETATM 1667 O O   . HOH   C 3 .   ? -5.91567  -28.34493 -4.99500  1.000 52.59308  ? 412 HOH   A O   1 
HETATM 1668 O O   . HOH   C 3 .   ? 2.98273   -24.75784 -38.50301 1.000 36.26224  ? 413 HOH   A O   1 
HETATM 1669 O O   . HOH   C 3 .   ? -13.36470 -0.76353  -20.58897 1.000 37.37089  ? 414 HOH   A O   1 
HETATM 1670 O O   . HOH   C 3 .   ? -17.86072 -4.75046  -37.11738 1.000 50.71660  ? 415 HOH   A O   1 
HETATM 1671 O O   . HOH   C 3 .   ? -2.94298  -2.94044  -17.52044 1.000 44.32677  ? 416 HOH   A O   1 
HETATM 1672 O O   . HOH   C 3 .   ? 20.35458  -10.91113 -26.23457 1.000 41.56415  ? 417 HOH   A O   1 
HETATM 1673 O O   . HOH   C 3 .   ? -13.03542 -7.13857  -12.07254 1.000 35.13767  ? 418 HOH   A O   1 
HETATM 1674 O O   . HOH   C 3 .   ? 7.74794   -23.19993 -14.22084 1.000 31.75973  ? 419 HOH   A O   1 
HETATM 1675 O O   . HOH   C 3 .   ? -14.02870 -15.20751 -30.42650 1.000 49.23856  ? 420 HOH   A O   1 
HETATM 1676 O O   . HOH   C 3 .   ? -8.91292  -11.95672 -36.49075 1.000 28.98227  ? 421 HOH   A O   1 
HETATM 1677 O O   . HOH   C 3 .   ? 7.71831   -18.80586 -6.52904  1.000 27.41093  ? 422 HOH   A O   1 
HETATM 1678 O O   . HOH   C 3 .   ? 5.80831   -21.95399 -37.25785 1.000 32.20517  ? 423 HOH   A O   1 
HETATM 1679 O O   . HOH   C 3 .   ? 6.47333   -26.73385 -27.64218 1.000 32.55835  ? 424 HOH   A O   1 
HETATM 1680 O O   . HOH   C 3 .   ? 0.49370   -14.69284 -1.45894  1.000 43.98014  ? 425 HOH   A O   1 
HETATM 1681 O O   . HOH   C 3 .   ? 1.81305   -15.93048 -41.18113 1.000 40.29686  ? 426 HOH   A O   1 
HETATM 1682 O O   . HOH   C 3 .   ? 1.41813   -7.87289  -16.71029 1.000 23.77277  ? 427 HOH   A O   1 
HETATM 1683 O O   . HOH   C 3 .   ? -0.37492  -5.79327  -38.67703 1.000 46.85215  ? 428 HOH   A O   1 
HETATM 1684 O O   . HOH   C 3 .   ? -17.99615 -3.93302  -28.98379 1.000 44.98526  ? 429 HOH   A O   1 
HETATM 1685 O O   . HOH   C 3 .   ? 7.48838   -27.87892 -23.93930 1.000 32.50087  ? 430 HOH   A O   1 
HETATM 1686 O O   . HOH   C 3 .   ? -6.75615  -5.35217  -39.26987 1.000 45.80246  ? 431 HOH   A O   1 
HETATM 1687 O O   . HOH   C 3 .   ? 11.07335  -8.07763  -27.77837 1.000 24.61239  ? 432 HOH   A O   1 
HETATM 1688 O O   . HOH   C 3 .   ? -12.99700 -24.81932 -10.77355 1.000 33.57186  ? 433 HOH   A O   1 
HETATM 1689 O O   . HOH   C 3 .   ? -14.71470 -22.40928 -11.32363 1.000 32.70037  ? 434 HOH   A O   1 
HETATM 1690 O O   . HOH   C 3 .   ? -10.59347 -14.39093 1.02399   1.000 30.48035  ? 435 HOH   A O   1 
HETATM 1691 O O   . HOH   C 3 .   ? -8.22047  1.70029   -36.71165 1.000 39.09081  ? 436 HOH   A O   1 
HETATM 1692 O O   . HOH   C 3 .   ? 3.47479   -8.06461  -37.04925 1.000 40.27452  ? 437 HOH   A O   1 
HETATM 1693 O O   . HOH   C 3 .   ? -2.90644  -3.42401  -35.54628 1.000 46.41431  ? 438 HOH   A O   1 
HETATM 1694 O O   . HOH   C 3 .   ? 0.35938   -1.70974  -19.60239 1.000 48.74298  ? 439 HOH   A O   1 
HETATM 1695 O O   . HOH   C 3 .   ? 3.23452   -5.97453  -11.27672 1.000 26.51820  ? 440 HOH   A O   1 
HETATM 1696 O O   . HOH   C 3 .   ? -14.15517 -11.46850 0.47412   1.000 46.14638  ? 441 HOH   A O   1 
HETATM 1697 O O   . HOH   C 3 .   ? 1.05347   -6.78804  -5.28662  1.000 47.52644  ? 442 HOH   A O   1 
HETATM 1698 O O   . HOH   C 3 .   ? -12.29415 -27.80258 -29.82204 1.000 43.49065  ? 443 HOH   A O   1 
HETATM 1699 O O   . HOH   C 3 .   ? 9.73746   -17.37210 -7.81960  1.000 27.76449  ? 444 HOH   A O   1 
HETATM 1700 O O   . HOH   C 3 .   ? -16.33347 -12.58796 -19.75819 1.000 22.39967  ? 445 HOH   A O   1 
HETATM 1701 O O   . HOH   C 3 .   ? -14.39744 -6.82622  -14.52165 1.000 34.13571  ? 446 HOH   A O   1 
HETATM 1702 O O   . HOH   C 3 .   ? 0.91700   -20.81169 -4.68939  1.000 29.87660  ? 447 HOH   A O   1 
HETATM 1703 O O   . HOH   C 3 .   ? 11.11172  -28.41965 -30.46356 1.000 35.72494  ? 448 HOH   A O   1 
HETATM 1704 O O   . HOH   C 3 .   ? -15.93006 0.10074   -30.46800 1.000 40.08439  ? 449 HOH   A O   1 
HETATM 1705 O O   . HOH   C 3 .   ? 6.38281   -29.60401 -20.11757 1.000 36.88089  ? 450 HOH   A O   1 
HETATM 1706 O O   . HOH   C 3 .   ? 14.40898  -16.11913 -30.75360 1.000 38.08588  ? 451 HOH   A O   1 
HETATM 1707 O O   . HOH   C 3 .   ? -9.22108  -2.33593  -17.60964 1.000 24.23428  ? 452 HOH   A O   1 
HETATM 1708 O O   . HOH   C 3 .   ? -3.29691  -12.00814 -9.10623  1.000 28.64197  ? 453 HOH   A O   1 
HETATM 1709 O O   . HOH   C 3 .   ? -5.79928  -2.07430  -19.66005 1.000 25.21239  ? 454 HOH   A O   1 
HETATM 1710 O O   . HOH   C 3 .   ? 9.517     -11.293   -34.999   1.000 38.83278  ? 455 HOH   A O   1 
HETATM 1711 O O   . HOH   C 3 .   ? 18.20893  -7.20464  -20.58697 1.000 36.89876  ? 456 HOH   A O   1 
HETATM 1712 O O   . HOH   C 3 .   ? -5.45537  -7.58090  -13.26919 1.000 23.38099  ? 457 HOH   A O   1 
HETATM 1713 O O   . HOH   C 3 .   ? 9.05435   -26.39710 -17.01466 1.000 32.95918  ? 458 HOH   A O   1 
HETATM 1714 O O   . HOH   C 3 .   ? 6.07528   -20.99598 -0.11052  1.000 32.03705  ? 459 HOH   A O   1 
HETATM 1715 O O   . HOH   C 3 .   ? 11.41370  -27.53374 -34.58711 1.000 28.39477  ? 460 HOH   A O   1 
HETATM 1716 O O   . HOH   C 3 .   ? 8.01751   -23.02794 -7.09706  1.000 41.32843  ? 461 HOH   A O   1 
HETATM 1717 O O   . HOH   C 3 .   ? 0.33595   -22.11474 -2.02638  1.000 44.83385  ? 462 HOH   A O   1 
HETATM 1718 O O   . HOH   C 3 .   ? -7.33819  -27.84317 -21.05347 1.000 47.84565  ? 463 HOH   A O   1 
HETATM 1719 O O   . HOH   C 3 .   ? 9.73503   -14.64629 -25.31704 1.000 20.88139  ? 464 HOH   A O   1 
HETATM 1720 O O   . HOH   C 3 .   ? -18.89715 -10.77307 -23.76819 1.000 32.09317  ? 465 HOH   A O   1 
HETATM 1721 O O   . HOH   C 3 .   ? -20.59230 -14.03682 -18.20098 1.000 42.05824  ? 466 HOH   A O   1 
HETATM 1722 O O   . HOH   C 3 .   ? -8.24431  -24.68448 -18.98808 1.000 22.00376  ? 467 HOH   A O   1 
HETATM 1723 O O   . HOH   C 3 .   ? -2.30540  -13.79248 -35.67219 1.000 21.68651  ? 468 HOH   A O   1 
HETATM 1724 O O   . HOH   C 3 .   ? -19.79783 -12.73653 -16.34698 1.000 49.93093  ? 469 HOH   A O   1 
HETATM 1725 O O   . HOH   C 3 .   ? -8.59138  4.70449   -33.84866 1.000 32.36291  ? 470 HOH   A O   1 
HETATM 1726 O O   . HOH   C 3 .   ? 17.98894  -19.30363 -24.70838 1.000 32.85321  ? 471 HOH   A O   1 
HETATM 1727 O O   . HOH   C 3 .   ? -5.12101  -10.60614 -27.26040 1.000 18.39142  ? 472 HOH   A O   1 
HETATM 1728 O O   . HOH   C 3 .   ? -11.13779 -14.33354 -37.78625 1.000 42.65786  ? 473 HOH   A O   1 
HETATM 1729 O O   . HOH   C 3 .   ? 3.23009   -4.88778  -29.32288 1.000 35.27388  ? 474 HOH   A O   1 
HETATM 1730 O O   . HOH   C 3 .   ? -13.55474 -26.36341 -17.81743 1.000 31.27544  ? 475 HOH   A O   1 
HETATM 1731 O O   . HOH   C 3 .   ? -10.42271 -15.08864 -28.20514 1.000 35.51062  ? 476 HOH   A O   1 
HETATM 1732 O O   . HOH   C 3 .   ? -19.64192 -10.20709 -32.71876 1.000 47.39286  ? 477 HOH   A O   1 
HETATM 1733 O O   . HOH   C 3 .   ? 7.65280   1.43706   -15.09772 1.000 37.74486  ? 478 HOH   A O   1 
HETATM 1734 O O   . HOH   C 3 .   ? -0.23409  -5.48094  -18.58078 1.000 26.52791  ? 479 HOH   A O   1 
HETATM 1735 O O   . HOH   C 3 .   ? 14.06042  -15.53681 -2.13618  1.000 39.29132  ? 480 HOH   A O   1 
HETATM 1736 O O   . HOH   C 3 .   ? -17.06526 -5.29734  -22.81403 1.000 28.81636  ? 481 HOH   A O   1 
HETATM 1737 O O   . HOH   C 3 .   ? 18.22835  -10.96035 -17.39627 1.000 45.83829  ? 482 HOH   A O   1 
HETATM 1738 O O   . HOH   C 3 .   ? -1.09151  -11.28968 -3.10766  1.000 36.54982  ? 483 HOH   A O   1 
HETATM 1739 O O   . HOH   C 3 .   ? -6.45919  -5.23864  -35.69266 1.000 24.37750  ? 484 HOH   A O   1 
HETATM 1740 O O   . HOH   C 3 .   ? 8.70499   -15.42767 -27.86766 1.000 21.63012  ? 485 HOH   A O   1 
HETATM 1741 O O   . HOH   C 3 .   ? -3.95811  0.14583   -22.29819 1.000 35.21184  ? 486 HOH   A O   1 
HETATM 1742 O O   . HOH   C 3 .   ? -1.49829  -8.87732  -27.63070 1.000 23.19402  ? 487 HOH   A O   1 
HETATM 1743 O O   . HOH   C 3 .   ? -6.03523  -18.92708 -39.08874 1.000 37.78813  ? 488 HOH   A O   1 
HETATM 1744 O O   . HOH   C 3 .   ? -14.07774 -12.43085 -7.80188  1.000 28.26892  ? 489 HOH   A O   1 
HETATM 1745 O O   . HOH   C 3 .   ? 0.59931   -5.31692  -13.99003 1.000 39.45900  ? 490 HOH   A O   1 
HETATM 1746 O O   . HOH   C 3 .   ? 10.49769  -25.33846 -23.68048 1.000 25.88610  ? 491 HOH   A O   1 
HETATM 1747 O O   . HOH   C 3 .   ? -3.27247  -20.89021 -0.55153  1.000 34.70215  ? 492 HOH   A O   1 
HETATM 1748 O O   . HOH   C 3 .   ? 13.53585  -14.20421 -26.90986 1.000 23.76591  ? 493 HOH   A O   1 
HETATM 1749 O O   . HOH   C 3 .   ? -8.19166  -3.93332  -10.85617 1.000 31.02503  ? 494 HOH   A O   1 
HETATM 1750 O O   . HOH   C 3 .   ? 15.45150  -20.24406 -18.75435 1.000 26.57571  ? 495 HOH   A O   1 
HETATM 1751 O O   . HOH   C 3 .   ? -10.30087 -11.33152 -2.09914  1.000 26.81285  ? 496 HOH   A O   1 
HETATM 1752 O O   . HOH   C 3 .   ? -7.71595  -24.21857 -22.95600 1.000 30.81411  ? 497 HOH   A O   1 
HETATM 1753 O O   . HOH   C 3 .   ? -9.537    -30.651   -23.171   1.000 54.14469  ? 498 HOH   A O   1 
HETATM 1754 O O   . HOH   C 3 .   ? 8.39887   -20.49592 -9.22122  1.000 33.12358  ? 499 HOH   A O   1 
HETATM 1755 O O   . HOH   C 3 .   ? -3.10685  -1.20546  -24.38387 1.000 30.65559  ? 500 HOH   A O   1 
HETATM 1756 O O   . HOH   C 3 .   ? -4.33689  -4.31190  -37.39901 1.000 50.33843  ? 501 HOH   A O   1 
HETATM 1757 O O   . HOH   C 3 .   ? 1.76624   -25.65732 -2.78324  1.000 44.98106  ? 502 HOH   A O   1 
HETATM 1758 O O   . HOH   C 3 .   ? -6.51852  -7.85012  -34.42851 1.000 22.59075  ? 503 HOH   A O   1 
HETATM 1759 O O   . HOH   C 3 .   ? -19.810   -19.310   -14.163   1.000 25.49708  ? 504 HOH   A O   1 
HETATM 1760 O O   . HOH   C 3 .   ? 0.60345   -29.64572 -15.96699 1.000 40.74448  ? 505 HOH   A O   1 
HETATM 1761 O O   . HOH   C 3 .   ? 12.87560  -13.97510 -29.79451 1.000 31.84047  ? 506 HOH   A O   1 
HETATM 1762 O O   . HOH   C 3 .   ? 3.98695   -24.18388 -30.58818 1.000 23.02348  ? 507 HOH   A O   1 
HETATM 1763 O O   . HOH   C 3 .   ? 3.13907   -20.38063 -2.85103  1.000 38.31437  ? 508 HOH   A O   1 
HETATM 1764 O O   . HOH   C 3 .   ? -12.61884 -27.11396 -34.83925 1.000 48.25677  ? 509 HOH   A O   1 
HETATM 1765 O O   . HOH   C 3 .   ? -16.11666 -3.01818  -21.31471 1.000 32.35770  ? 510 HOH   A O   1 
HETATM 1766 O O   . HOH   C 3 .   ? -17.245   -28.690   -17.012   1.000 47.41769  ? 511 HOH   A O   1 
HETATM 1767 O O   . HOH   C 3 .   ? -0.41381  -7.21809  -31.21721 1.000 32.13749  ? 512 HOH   A O   1 
HETATM 1768 O O   . HOH   C 3 .   ? -6.18981  -13.89185 0.83358   1.000 31.06826  ? 513 HOH   A O   1 
HETATM 1769 O O   . HOH   C 3 .   ? -9.70732  -0.42529  -19.83762 1.000 46.11130  ? 514 HOH   A O   1 
HETATM 1770 O O   . HOH   C 3 .   ? -7.68620  -13.79152 -40.97005 1.000 46.92584  ? 515 HOH   A O   1 
HETATM 1771 O O   . HOH   C 3 .   ? 4.73548   -30.40475 -11.53848 1.000 44.47966  ? 516 HOH   A O   1 
HETATM 1772 O O   . HOH   C 3 .   ? -9.12297  -10.44550 -40.50132 1.000 42.38009  ? 517 HOH   A O   1 
HETATM 1773 O O   . HOH   C 3 .   ? -3.56113  -21.25850 -38.67878 1.000 40.06499  ? 518 HOH   A O   1 
HETATM 1774 O O   . HOH   C 3 .   ? -17.79311 -18.62540 -11.13584 1.000 36.11019  ? 519 HOH   A O   1 
HETATM 1775 O O   . HOH   C 3 .   ? 4.03907   -9.14993  -20.26075 1.000 25.33853  ? 520 HOH   A O   1 
HETATM 1776 O O   . HOH   C 3 .   ? -13.72773 -16.79982 -2.60564  1.000 28.18840  ? 521 HOH   A O   1 
HETATM 1777 O O   . HOH   C 3 .   ? -4.24201  -26.13624 -29.97601 1.000 55.48655  ? 522 HOH   A O   1 
HETATM 1778 O O   . HOH   C 3 .   ? -7.70901  -28.24565 -7.86942  1.000 34.11849  ? 523 HOH   A O   1 
HETATM 1779 O O   . HOH   C 3 .   ? 0.58216   -27.08632 -37.23179 1.000 47.15792  ? 524 HOH   A O   1 
HETATM 1780 O O   . HOH   C 3 .   ? -14.57664 -3.97965  -12.77415 1.000 47.89493  ? 525 HOH   A O   1 
HETATM 1781 O O   . HOH   C 3 .   ? 12.39737  -27.29342 -19.39349 1.000 45.08523  ? 526 HOH   A O   1 
HETATM 1782 O O   . HOH   C 3 .   ? -12.16452 -7.79299  -38.39724 1.000 35.47598  ? 527 HOH   A O   1 
HETATM 1783 O O   . HOH   C 3 .   ? 3.55210   -12.09495 -38.71712 1.000 28.24660  ? 528 HOH   A O   1 
HETATM 1784 O O   . HOH   C 3 .   ? 19.570    -16.559   -27.848   1.000 41.15609  ? 529 HOH   A O   1 
HETATM 1785 O O   . HOH   C 3 .   ? -6.55593  -34.98963 -19.47693 1.000 58.52129  ? 530 HOH   A O   1 
HETATM 1786 O O   . HOH   C 3 .   ? -4.27499  -13.63216 -0.78212  1.000 49.48034  ? 531 HOH   A O   1 
HETATM 1787 O O   . HOH   C 3 .   ? -5.81254  -31.08919 -11.47167 1.000 34.92527  ? 532 HOH   A O   1 
HETATM 1788 O O   . HOH   C 3 .   ? -15.34044 -11.13613 -29.85389 1.000 27.61375  ? 533 HOH   A O   1 
HETATM 1789 O O   . HOH   C 3 .   ? 3.63764   -29.81533 -25.77714 1.000 42.38520  ? 534 HOH   A O   1 
HETATM 1790 O O   . HOH   C 3 .   ? -16.37627 -8.95031  -14.29007 1.000 37.96611  ? 535 HOH   A O   1 
HETATM 1791 O O   . HOH   C 3 .   ? 1.96692   -25.97008 -29.25354 1.000 39.53518  ? 536 HOH   A O   1 
HETATM 1792 O O   . HOH   C 3 .   ? -13.51718 -31.01503 -12.77320 1.000 54.56117  ? 537 HOH   A O   1 
HETATM 1793 O O   . HOH   C 3 .   ? 15.78547  -0.84474  -19.77919 1.000 38.99261  ? 538 HOH   A O   1 
HETATM 1794 O O   . HOH   C 3 .   ? 4.18017   -19.75047 -40.64737 1.000 36.99088  ? 539 HOH   A O   1 
HETATM 1795 O O   . HOH   C 3 .   ? -6.21307  -11.33556 -10.03346 1.000 26.04750  ? 540 HOH   A O   1 
HETATM 1796 O O   . HOH   C 3 .   ? 5.02109   -0.72007  -6.52869  1.000 54.11966  ? 541 HOH   A O   1 
HETATM 1797 O O   . HOH   C 3 .   ? -4.73899  0.44908   -30.71298 1.000 36.38745  ? 542 HOH   A O   1 
HETATM 1798 O O   . HOH   C 3 .   ? 20.40889  -4.41677  -27.31149 1.000 56.37597  ? 543 HOH   A O   1 
HETATM 1799 O O   . HOH   C 3 .   ? -1.85744  -25.55679 -4.67960  1.000 27.17284  ? 544 HOH   A O   1 
HETATM 1800 O O   . HOH   C 3 .   ? -15.16316 -11.93683 -12.03876 1.000 35.23877  ? 545 HOH   A O   1 
HETATM 1801 O O   . HOH   C 3 .   ? 10.56725  -25.62117 -26.67287 1.000 31.70039  ? 546 HOH   A O   1 
HETATM 1802 O O   . HOH   C 3 .   ? -5.09312  -14.25227 -22.73852 1.000 19.13014  ? 547 HOH   A O   1 
HETATM 1803 O O   . HOH   C 3 .   ? -0.48193  -12.54265 -20.90188 1.000 20.85121  ? 548 HOH   A O   1 
HETATM 1804 O O   . HOH   C 3 .   ? 5.22478   -9.72612  -2.73032  1.000 41.03736  ? 549 HOH   A O   1 
HETATM 1805 O O   . HOH   C 3 .   ? 3.53863   -6.80248  -18.12933 1.000 27.44328  ? 550 HOH   A O   1 
HETATM 1806 O O   . HOH   C 3 .   ? 0.25381   -5.73231  -21.99813 1.000 37.91701  ? 551 HOH   A O   1 
HETATM 1807 O O   . HOH   C 3 .   ? -3.18982  -31.31016 -20.10900 1.000 52.93499  ? 552 HOH   A O   1 
HETATM 1808 O O   . HOH   C 3 .   ? -9.21538  -17.92453 -36.28620 1.000 41.91196  ? 553 HOH   A O   1 
HETATM 1809 O O   . HOH   C 3 .   ? 15.71491  -18.15218 -3.61104  1.000 37.73732  ? 554 HOH   A O   1 
HETATM 1810 O O   . HOH   C 3 .   ? 13.64565  -20.47367 -20.72311 1.000 22.02288  ? 555 HOH   A O   1 
HETATM 1811 O O   . HOH   C 3 .   ? -2.304    -0.030    -19.581   1.000 47.65537  ? 556 HOH   A O   1 
HETATM 1812 O O   . HOH   C 3 .   ? -5.22123  -5.21137  -12.00359 1.000 39.64987  ? 557 HOH   A O   1 
HETATM 1813 O O   . HOH   C 3 .   ? 1.31874   -8.35219  -27.28247 1.000 25.88220  ? 558 HOH   A O   1 
HETATM 1814 O O   . HOH   C 3 .   ? -6.26304  -7.53335  -42.49001 1.000 53.15495  ? 559 HOH   A O   1 
HETATM 1815 O O   . HOH   C 3 .   ? -17.75916 -14.99789 -13.07355 1.000 29.86390  ? 560 HOH   A O   1 
HETATM 1816 O O   . HOH   C 3 .   ? -1.57716  -6.20075  -26.65170 1.000 27.07488  ? 561 HOH   A O   1 
HETATM 1817 O O   . HOH   C 3 .   ? -10.53958 -6.23865  -2.92082  1.000 44.91693  ? 562 HOH   A O   1 
HETATM 1818 O O   . HOH   C 3 .   ? 8.77598   -20.34200 -4.23865  1.000 30.13151  ? 563 HOH   A O   1 
HETATM 1819 O O   . HOH   C 3 .   ? 8.28907   -16.55182 -39.61746 1.000 39.71759  ? 564 HOH   A O   1 
HETATM 1820 O O   . HOH   C 3 .   ? -1.21715  -29.85341 -17.32495 1.000 44.38137  ? 565 HOH   A O   1 
HETATM 1821 O O   . HOH   C 3 .   ? -16.19161 -25.29883 -10.67067 1.000 39.09233  ? 566 HOH   A O   1 
HETATM 1822 O O   . HOH   C 3 .   ? 15.31337  -7.30924  -28.13358 1.000 33.05745  ? 567 HOH   A O   1 
HETATM 1823 O O   . HOH   C 3 .   ? -7.26222  1.28575   -19.51599 1.000 43.81291  ? 568 HOH   A O   1 
HETATM 1824 O O   . HOH   C 3 .   ? 10.34018  -21.16220 -6.93307  1.000 40.87520  ? 569 HOH   A O   1 
HETATM 1825 O O   . HOH   C 3 .   ? -1.35442  -4.59911  -33.87520 1.000 46.72030  ? 570 HOH   A O   1 
HETATM 1826 O O   . HOH   C 3 .   ? 18.64670  -16.01592 -13.51824 1.000 35.81810  ? 571 HOH   A O   1 
HETATM 1827 O O   . HOH   C 3 .   ? 9.95476   -5.58621  -1.68566  1.000 62.02711  ? 572 HOH   A O   1 
HETATM 1828 O O   . HOH   C 3 .   ? -18.27831 -3.23413  -35.63899 1.000 53.00029  ? 573 HOH   A O   1 
HETATM 1829 O O   . HOH   C 3 .   ? -12.26827 -26.84999 -20.24587 1.000 31.06073  ? 574 HOH   A O   1 
HETATM 1830 O O   . HOH   C 3 .   ? 9.92626   -26.65081 -39.17107 1.000 50.30300  ? 575 HOH   A O   1 
HETATM 1831 O O   . HOH   C 3 .   ? -3.32794  -12.89276 -21.01472 1.000 21.09064  ? 576 HOH   A O   1 
HETATM 1832 O O   . HOH   C 3 .   ? -2.481    -15.726   -0.206    1.000 37.00081  ? 577 HOH   A O   1 
HETATM 1833 O O   . HOH   C 3 .   ? 16.97736  -24.86343 -25.34706 1.000 37.02555  ? 578 HOH   A O   1 
HETATM 1834 O O   . HOH   C 3 .   ? 3.03936   -6.75741  -20.68098 1.000 40.07719  ? 579 HOH   A O   1 
HETATM 1835 O O   . HOH   C 3 .   ? 20.82019  -14.20017 -26.82485 1.000 34.66460  ? 580 HOH   A O   1 
HETATM 1836 O O   . HOH   C 3 .   ? -2.26313  -24.69227 -1.03445  1.000 50.03164  ? 581 HOH   A O   1 
HETATM 1837 O O   . HOH   C 3 .   ? 0.09234   -16.61654 -3.45859  1.000 26.92967  ? 582 HOH   A O   1 
HETATM 1838 O O   . HOH   C 3 .   ? -13.60764 -25.66164 -7.71345  1.000 32.68530  ? 583 HOH   A O   1 
HETATM 1839 O O   . HOH   C 3 .   ? -13.27057 -12.28337 -30.99804 1.000 28.32014  ? 584 HOH   A O   1 
HETATM 1840 O O   . HOH   C 3 .   ? -15.93069 -3.96096  -15.52351 1.000 47.44376  ? 585 HOH   A O   1 
HETATM 1841 O O   . HOH   C 3 .   ? -14.22212 -16.11755 -25.99968 1.000 27.97508  ? 586 HOH   A O   1 
HETATM 1842 O O   . HOH   C 3 .   ? 13.63731  -4.05221  -25.70683 1.000 20.72496  ? 587 HOH   A O   1 
HETATM 1843 O O   . HOH   C 3 .   ? 18.60596  -19.31644 -11.84582 1.000 47.24962  ? 588 HOH   A O   1 
HETATM 1844 O O   . HOH   C 3 .   ? 3.14793   -3.76811  -9.07345  1.000 52.06123  ? 589 HOH   A O   1 
HETATM 1845 O O   . HOH   C 3 .   ? -5.40113  -31.45576 -7.01721  1.000 51.33727  ? 590 HOH   A O   1 
HETATM 1846 O O   . HOH   C 3 .   ? -16.98285 -20.17017 -4.52698  1.000 48.96615  ? 591 HOH   A O   1 
HETATM 1847 O O   . HOH   C 3 .   ? -5.63741  -12.10796 -42.03311 1.000 48.74260  ? 592 HOH   A O   1 
HETATM 1848 O O   . HOH   C 3 .   ? 3.91059   -22.78312 -3.43906  1.000 38.59321  ? 593 HOH   A O   1 
HETATM 1849 O O   . HOH   C 3 .   ? 6.44313   -9.64191  -21.51747 1.000 34.12628  ? 594 HOH   A O   1 
HETATM 1850 O O   . HOH   C 3 .   ? 13.13870  -6.88495  -26.51279 1.000 25.50273  ? 595 HOH   A O   1 
HETATM 1851 O O   . HOH   C 3 .   ? -14.57430 -29.23860 -9.60704  1.000 51.92000  ? 596 HOH   A O   1 
HETATM 1852 O O   . HOH   C 3 .   ? -18.22012 -5.81917  -25.43338 1.000 37.92704  ? 597 HOH   A O   1 
HETATM 1853 O O   . HOH   C 3 .   ? 0.73956   -4.35885  -16.58337 1.000 44.14891  ? 598 HOH   A O   1 
HETATM 1854 O O   . HOH   C 3 .   ? -13.927   -0.640    -13.562   1.000 40.40925  ? 599 HOH   A O   1 
HETATM 1855 O O   . HOH   C 3 .   ? -18.59034 -10.82466 -14.63843 1.000 60.60294  ? 600 HOH   A O   1 
HETATM 1856 O O   . HOH   C 3 .   ? -13.83844 -18.55635 -24.33344 1.000 24.98081  ? 601 HOH   A O   1 
HETATM 1857 O O   . HOH   C 3 .   ? -1.09869  -14.05195 -42.98260 1.000 43.75822  ? 602 HOH   A O   1 
HETATM 1858 O O   . HOH   C 3 .   ? 11.01983  -11.43772 -4.93551  1.000 39.53125  ? 603 HOH   A O   1 
HETATM 1859 O O   . HOH   C 3 .   ? -14.16710 -23.87276 -4.84968  1.000 35.18700  ? 604 HOH   A O   1 
HETATM 1860 O O   . HOH   C 3 .   ? -12.12736 -32.11106 -19.58438 1.000 59.25375  ? 605 HOH   A O   1 
HETATM 1861 O O   . HOH   C 3 .   ? -7.632    7.721     -34.066   1.000 41.44807  ? 606 HOH   A O   1 
HETATM 1862 O O   . HOH   C 3 .   ? 7.17585   2.05979   -12.52077 1.000 41.82730  ? 607 HOH   A O   1 
HETATM 1863 O O   . HOH   C 3 .   ? 1.13191   -8.52675  -3.90570  1.000 42.27931  ? 608 HOH   A O   1 
HETATM 1864 O O   . HOH   C 3 .   ? 13.69600  -11.53398 -29.95276 1.000 45.09597  ? 609 HOH   A O   1 
HETATM 1865 O O   . HOH   C 3 .   ? 5.54400   -3.24723  -26.55226 1.000 44.86080  ? 610 HOH   A O   1 
HETATM 1866 O O   . HOH   C 3 .   ? 16.228    -27.676   -22.555   1.000 45.79086  ? 611 HOH   A O   1 
HETATM 1867 O O   . HOH   C 3 .   ? -2.39556  -26.70878 -27.91534 1.000 57.43274  ? 612 HOH   A O   1 
HETATM 1868 O O   . HOH   C 3 .   ? -2.00125  -32.58447 -7.58749  1.000 57.63997  ? 613 HOH   A O   1 
HETATM 1869 O O   . HOH   C 3 .   ? 2.11923   -6.04626  -25.86113 1.000 34.53676  ? 614 HOH   A O   1 
HETATM 1870 O O   . HOH   C 3 .   ? -19.03662 -13.52713 -27.47624 1.000 49.84939  ? 615 HOH   A O   1 
HETATM 1871 O O   . HOH   C 3 .   ? 1.90375   -18.21898 0.07851   1.000 35.45038  ? 616 HOH   A O   1 
HETATM 1872 O O   . HOH   C 3 .   ? -4.63075  -3.32793  -15.78129 1.000 43.20983  ? 617 HOH   A O   1 
HETATM 1873 O O   . HOH   C 3 .   ? -3.93475  -32.94125 -10.92723 1.000 51.16416  ? 618 HOH   A O   1 
HETATM 1874 O O   . HOH   C 3 .   ? 10.46353  -17.75000 -38.85359 1.000 50.26703  ? 619 HOH   A O   1 
HETATM 1875 O O   . HOH   C 3 .   ? -18.79195 -15.04374 -20.95875 1.000 47.93185  ? 620 HOH   A O   1 
HETATM 1876 O O   . HOH   C 3 .   ? -2.70761  -1.04915  -31.53282 1.000 43.70276  ? 621 HOH   A O   1 
HETATM 1877 O O   . HOH   C 3 .   ? -2.29065  -26.85048 -24.85472 1.000 45.70488  ? 622 HOH   A O   1 
HETATM 1878 O O   . HOH   C 3 .   ? 14.38960  -22.45487 -17.07831 1.000 35.32900  ? 623 HOH   A O   1 
HETATM 1879 O O   . HOH   C 3 .   ? -6.54327  -25.36566 -27.46648 1.000 50.59329  ? 624 HOH   A O   1 
HETATM 1880 O O   . HOH   C 3 .   ? 4.27995   -22.37160 -39.11366 1.000 49.77658  ? 625 HOH   A O   1 
HETATM 1881 O O   . HOH   C 3 .   ? -6.869    -22.923   -1.697    1.000 46.64594  ? 626 HOH   A O   1 
HETATM 1882 O O   . HOH   C 3 .   ? 5.88042   -3.82411  -23.91757 1.000 42.31658  ? 627 HOH   A O   1 
HETATM 1883 O O   . HOH   C 3 .   ? 5.362     1.397     -17.006   1.000 47.77383  ? 628 HOH   A O   1 
HETATM 1884 O O   . HOH   C 3 .   ? 15.94680  1.50644   -15.25475 1.000 50.03263  ? 629 HOH   A O   1 
HETATM 1885 O O   . HOH   C 3 .   ? -17.27841 -4.54955  -17.41137 1.000 40.94957  ? 630 HOH   A O   1 
HETATM 1886 O O   . HOH   C 3 .   ? 4.718     -1.713    -18.658   1.000 49.08937  ? 631 HOH   A O   1 
HETATM 1887 O O   . HOH   C 3 .   ? 0.00544   -19.00914 -2.04137  1.000 36.17736  ? 632 HOH   A O   1 
HETATM 1888 O O   . HOH   C 3 .   ? -18.26447 -14.63724 -22.68830 1.000 31.02022  ? 633 HOH   A O   1 
HETATM 1889 O O   . HOH   C 3 .   ? 17.70102  -21.56282 -19.94205 1.000 35.00502  ? 634 HOH   A O   1 
HETATM 1890 O O   . HOH   C 3 .   ? -12.24727 -25.82000 -3.90256  1.000 55.30912  ? 635 HOH   A O   1 
HETATM 1891 O O   . HOH   C 3 .   ? 12.03166  -25.50017 -38.36895 1.000 35.33635  ? 636 HOH   A O   1 
HETATM 1892 O O   . HOH   C 3 .   ? 16.86693  -6.73349  -29.48051 1.000 60.53155  ? 637 HOH   A O   1 
HETATM 1893 O O   . HOH   C 3 .   ? 1.77758   -3.04788  -12.96721 1.000 49.83608  ? 638 HOH   A O   1 
HETATM 1894 O O   . HOH   C 3 .   ? 3.61568   -8.05695  -2.08774  1.000 53.76697  ? 639 HOH   A O   1 
HETATM 1895 O O   . HOH   C 3 .   ? -14.10342 -9.54721  -8.36579  1.000 38.01553  ? 640 HOH   A O   1 
HETATM 1896 O O   . HOH   C 3 .   ? -13.93464 -14.13911 -2.84663  1.000 36.29689  ? 641 HOH   A O   1 
HETATM 1897 O O   . HOH   C 3 .   ? -9.16685  -5.90045  -39.89016 1.000 42.74536  ? 642 HOH   A O   1 
HETATM 1898 O O   . HOH   C 3 .   ? -3.34497  -27.12044 -3.32236  1.000 47.31237  ? 643 HOH   A O   1 
HETATM 1899 O O   . HOH   C 3 .   ? -6.33766  3.52241   -34.78590 1.000 47.28956  ? 644 HOH   A O   1 
HETATM 1900 O O   . HOH   C 3 .   ? 18.92421  -8.30394  -17.87765 1.000 42.68900  ? 645 HOH   A O   1 
HETATM 1901 O O   . HOH   C 3 .   ? 16.84617  0.48151   -17.81067 1.000 44.90484  ? 646 HOH   A O   1 
HETATM 1902 O O   . HOH   C 3 .   ? 0.31341   -2.34060  -24.04184 1.000 46.35086  ? 647 HOH   A O   1 
HETATM 1903 O O   . HOH   C 3 .   ? 7.52513   -14.26858 -38.39779 1.000 32.88298  ? 648 HOH   A O   1 
HETATM 1904 O O   . HOH   C 3 .   ? -12.46619 -16.42470 -28.08659 1.000 41.87948  ? 649 HOH   A O   1 
HETATM 1905 O O   . HOH   C 3 .   ? -1.47833  -5.35196  -12.65563 1.000 51.96227  ? 650 HOH   A O   1 
HETATM 1906 O O   . HOH   C 3 .   ? -5.651    -11.069   0.960     1.000 52.36201  ? 651 HOH   A O   1 
HETATM 1907 O O   . HOH   C 3 .   ? 3.43712   -9.45788  -39.35270 1.000 41.62998  ? 652 HOH   A O   1 
HETATM 1908 O O   . HOH   C 3 .   ? -18.75258 -11.59850 -21.06501 1.000 31.53690  ? 653 HOH   A O   1 
HETATM 1909 O O   . HOH   C 3 .   ? -8.69512  -10.72918 -0.11972  1.000 47.90784  ? 654 HOH   A O   1 
HETATM 1910 O O   . HOH   C 3 .   ? -10.46403 -7.37660  -40.16271 1.000 53.30864  ? 655 HOH   A O   1 
HETATM 1911 O O   . HOH   C 3 .   ? -11.83911 -9.79446  -39.77347 1.000 48.07915  ? 656 HOH   A O   1 
HETATM 1912 O O   . HOH   C 3 .   ? -9.86326  -25.92920 -20.76888 1.000 31.52035  ? 657 HOH   A O   1 
HETATM 1913 O O   . HOH   C 3 .   ? -10.602   -22.447   4.314     1.000 43.22084  ? 658 HOH   A O   1 
HETATM 1914 O O   . HOH   C 3 .   ? 11.54068  -27.82422 -23.46121 1.000 50.60784  ? 659 HOH   A O   1 
HETATM 1915 O O   . HOH   C 3 .   ? -10.46748 -8.55977  -1.51447  1.000 46.25188  ? 660 HOH   A O   1 
HETATM 1916 O O   . HOH   C 3 .   ? 6.05084   -29.97940 -24.82678 1.000 44.95879  ? 661 HOH   A O   1 
HETATM 1917 O O   . HOH   C 3 .   ? 6.51108   -21.35929 -2.70970  1.000 33.04502  ? 662 HOH   A O   1 
HETATM 1918 O O   . HOH   C 3 .   ? 5.65130   -13.32771 -39.98246 1.000 33.56954  ? 663 HOH   A O   1 
HETATM 1919 O O   . HOH   C 3 .   ? -23.098   -31.658   -12.699   1.000 49.43252  ? 664 HOH   A O   1 
HETATM 1920 O O   . HOH   C 3 .   ? -4.31935  2.27666   -33.06790 1.000 54.06474  ? 665 HOH   A O   1 
HETATM 1921 O O   . HOH   C 3 .   ? 17.30189  -17.17313 -5.01733  1.000 56.38871  ? 666 HOH   A O   1 
HETATM 1922 O O   . HOH   C 3 .   ? 20.15572  -5.79670  -21.52643 1.000 47.77665  ? 667 HOH   A O   1 
HETATM 1923 O O   . HOH   C 3 .   ? 6.13426   -7.05397  -36.28873 1.000 48.25339  ? 668 HOH   A O   1 
HETATM 1924 O O   . HOH   C 3 .   ? 4.32712   -15.34101 -41.73874 1.000 45.65622  ? 669 HOH   A O   1 
HETATM 1925 O O   . HOH   C 3 .   ? 9.96653   -29.44591 -23.89354 1.000 49.14290  ? 670 HOH   A O   1 
HETATM 1926 O O   . HOH   C 3 .   ? -0.00000  -0.00000  -18.69763 0.50  50.29352  ? 671 HOH   A O   1 
HETATM 1927 O O   . HOH   C 3 .   ? 20.48334  -6.67249  -16.51918 1.000 51.20493  ? 672 HOH   A O   1 
HETATM 1928 O O   . HOH   C 3 .   ? -16.208   3.370     -26.653   1.000 45.45853  ? 673 HOH   A O   1 
HETATM 1929 O O   . HOH   C 3 .   ? -14.18454 -14.40972 -37.59986 1.000 59.06149  ? 674 HOH   A O   1 
HETATM 1930 O O   . HOH   C 3 .   ? -0.23989  -27.13559 -1.18240  1.000 54.76658  ? 675 HOH   A O   1 
HETATM 1931 O O   . HOH   C 3 .   ? -7.04383  -30.73372 -9.17759  1.000 42.79904  ? 676 HOH   A O   1 
HETATM 1932 O O   . HOH   C 3 .   ? 1.812     -22.947   -1.051    1.000 51.24564  ? 677 HOH   A O   1 
HETATM 1933 O O   . HOH   C 3 .   ? -4.36486  -28.02129 -23.17708 1.000 43.79971  ? 678 HOH   A O   1 
HETATM 1934 O O   . HOH   C 3 .   ? 7.57975   -28.93475 -28.19835 1.000 51.99210  ? 679 HOH   A O   1 
HETATM 1935 O O   . HOH   C 3 .   ? 2.643     -1.628    -20.988   1.000 54.01676  ? 680 HOH   A O   1 
HETATM 1936 O O   . HOH   C 3 .   ? -16.28343 -12.50397 -6.21603  1.000 45.13403  ? 681 HOH   A O   1 
HETATM 1937 O O   . HOH   C 3 .   ? -16.07267 -13.26767 -3.52333  1.000 45.56020  ? 682 HOH   A O   1 
HETATM 1938 O O   . HOH   C 3 .   ? 10.75860  -28.08538 -27.89712 1.000 38.73549  ? 683 HOH   A O   1 
HETATM 1939 O O   . HOH   C 3 .   ? 11.396    -30.183   -34.410   1.000 40.55898  ? 684 HOH   A O   1 
HETATM 1940 O O   . HOH   C 3 .   ? -6.95952  -26.75111 -23.12118 1.000 45.46944  ? 685 HOH   A O   1 
HETATM 1941 O O   . HOH   C 3 .   ? -19.84874 -8.30874  -23.99605 1.000 54.20554  ? 686 HOH   A O   1 
HETATM 1942 O O   . HOH   C 3 .   ? 21.713    -17.898   -25.223   1.000 42.71062  ? 687 HOH   A O   1 
HETATM 1943 O O   . HOH   C 3 .   ? 9.67786   -25.19988 -14.82772 1.000 50.37475  ? 688 HOH   A O   1 
HETATM 1944 O O   . HOH   C 3 .   ? 4.011     -1.844    -28.511   1.000 43.49001  ? 689 HOH   A O   1 
HETATM 1945 O O   . HOH   C 3 .   ? -12.24897 -13.01020 -0.94960  1.000 32.84203  ? 690 HOH   A O   1 
HETATM 1946 O O   . HOH   C 3 .   ? -16.25507 -17.90978 -2.72335  1.000 52.30087  ? 691 HOH   A O   1 
HETATM 1947 O O   . HOH   C 3 .   ? -19.21205 -4.54154  -18.60486 1.000 56.96146  ? 692 HOH   A O   1 
HETATM 1948 O O   . HOH   C 3 .   ? 14.55636  -13.02085 -2.92988  1.000 49.04328  ? 693 HOH   A O   1 
HETATM 1949 O O   . HOH   C 3 .   ? -8.90556  -28.35350 -24.77024 1.000 46.65712  ? 694 HOH   A O   1 
HETATM 1950 O O   . HOH   C 3 .   ? 14.163    -28.612   -23.517   1.000 56.63905  ? 695 HOH   A O   1 
HETATM 1951 O O   . HOH   C 3 .   ? -14.44009 -14.05213 -10.19989 1.000 31.24178  ? 696 HOH   A O   1 
HETATM 1952 O O   . HOH   C 3 .   ? -14.70431 -9.42049  -11.29053 1.000 42.05703  ? 697 HOH   A O   1 
HETATM 1953 O O   . HOH   C 3 .   ? 19.29356  -20.54408 -22.19254 1.000 39.20094  ? 698 HOH   A O   1 
HETATM 1954 O O   . HOH   C 3 .   ? -10.445   -11.703   2.003     1.000 39.34495  ? 699 HOH   A O   1 
HETATM 1955 O O   . HOH   C 3 .   ? -20.37557 -10.12204 -16.33060 1.000 61.98491  ? 700 HOH   A O   1 
HETATM 1956 O O   . HOH   C 3 .   ? -17.01186 -15.43886 -10.19551 1.000 40.43179  ? 701 HOH   A O   1 
HETATM 1957 O O   . HOH   C 3 .   ? -19.60743 -5.83356  -21.74930 1.000 44.82225  ? 702 HOH   A O   1 
HETATM 1958 O O   . HOH   C 3 .   ? -20.79674 -10.35540 -19.66795 1.000 49.86797  ? 703 HOH   A O   1 
HETATM 1959 O O   . HOH   C 3 .   ? -18.30496 -1.79123  -30.36526 1.000 53.40900  ? 704 HOH   A O   1 
HETATM 1960 O O   . HOH   C 3 .   ? 6.74892   -29.88537 -29.66762 1.000 55.27805  ? 705 HOH   A O   1 
HETATM 1961 O O   . HOH   C 3 .   ? 24.861    -15.435   -22.793   1.000 56.03042  ? 706 HOH   A O   1 
HETATM 1962 O O   . HOH   C 3 .   ? -12.27413 -20.65569 -25.01601 1.000 45.27413  ? 707 HOH   A O   1 
HETATM 1963 O O   . HOH   C 3 .   ? -9.32004  -32.74274 -8.68910  1.000 51.46902  ? 708 HOH   A O   1 
HETATM 1964 O O   . HOH   C 3 .   ? 13.76182  -11.70151 -5.18621  1.000 46.95832  ? 709 HOH   A O   1 
HETATM 1965 O O   . HOH   C 3 .   ? -10.27985 -31.38620 -6.42361  1.000 56.81766  ? 710 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   ? 0.68281 0.84506 0.56037 -0.06093 -0.03623 -0.29918 16  GLU A N   
2    C CA  . GLU A 9   ? 0.80435 0.94742 0.66592 -0.02143 -0.04318 -0.27279 16  GLU A CA  
3    C C   . GLU A 9   ? 0.60929 0.74366 0.48895 -0.00713 -0.04795 -0.24838 16  GLU A C   
4    O O   . GLU A 9   ? 0.62520 0.81839 0.52332 0.00792  -0.06172 -0.23855 16  GLU A O   
5    C CB  . GLU A 9   ? 0.86843 1.08185 0.72479 0.00855  -0.05903 -0.26920 16  GLU A CB  
6    C CG  . GLU A 9   ? 0.94640 1.14628 0.78931 0.05320  -0.06380 -0.23837 16  GLU A CG  
7    C CD  . GLU A 9   ? 1.25409 1.51944 1.09035 0.08700  -0.07505 -0.23118 16  GLU A CD  
8    O OE1 . GLU A 9   ? 1.08533 1.37004 0.92538 0.12298  -0.08040 -0.20451 16  GLU A OE1 
9    O OE2 . GLU A 9   ? 1.22615 1.52112 1.05194 0.07890  -0.07613 -0.25181 16  GLU A OE2 
10   N N   . VAL A 10  ? 0.53529 0.59625 0.40924 -0.00967 -0.03448 -0.23850 17  VAL A N   
11   C CA  . VAL A 10  ? 0.45163 0.49817 0.34273 0.00037  -0.03713 -0.21875 17  VAL A CA  
12   C C   . VAL A 10  ? 0.48382 0.49555 0.36493 0.03561  -0.03604 -0.18937 17  VAL A C   
13   O O   . VAL A 10  ? 0.51964 0.48004 0.38425 0.04002  -0.02196 -0.18472 17  VAL A O   
14   C CB  . VAL A 10  ? 0.58633 0.57824 0.48589 -0.02854 -0.01901 -0.22252 17  VAL A CB  
15   C CG1 . VAL A 10  ? 0.48630 0.47774 0.40827 -0.02076 -0.02416 -0.20087 17  VAL A CG1 
16   C CG2 . VAL A 10  ? 0.66410 0.67606 0.57130 -0.06414 -0.01278 -0.24515 17  VAL A CG2 
17   N N   . GLU A 11  ? 0.37091 0.40770 0.26337 0.05949  -0.04672 -0.16432 18  GLU A N   
18   C CA  . GLU A 11  ? 0.39687 0.40141 0.28742 0.08602  -0.04147 -0.13151 18  GLU A CA  
19   C C   . GLU A 11  ? 0.32607 0.30313 0.23885 0.07911  -0.03676 -0.11156 18  GLU A C   
20   O O   . GLU A 11  ? 0.30563 0.30553 0.23523 0.07053  -0.04355 -0.11142 18  GLU A O   
21   C CB  . GLU A 11  ? 0.37141 0.41240 0.25422 0.11682  -0.04934 -0.11725 18  GLU A CB  
22   C CG  . GLU A 11  ? 0.38288 0.45271 0.23882 0.13237  -0.05318 -0.13129 18  GLU A CG  
23   C CD  . GLU A 11  ? 0.51728 0.62296 0.35970 0.16863  -0.05726 -0.11446 18  GLU A CD  
24   O OE1 . GLU A 11  ? 0.53045 0.68454 0.37878 0.17475  -0.06681 -0.11666 18  GLU A OE1 
25   O OE2 . GLU A 11  ? 0.54829 0.63319 0.37111 0.19344  -0.04819 -0.09855 18  GLU A OE2 
26   N N   . THR A 12  ? 0.36619 0.30083 0.27843 0.08548  -0.02528 -0.09420 19  THR A N   
27   C CA  . THR A 12  ? 0.30641 0.22389 0.23715 0.08200  -0.02117 -0.07574 19  THR A CA  
28   C C   . THR A 12  ? 0.33298 0.25450 0.27068 0.10040  -0.02020 -0.05309 19  THR A C   
29   O O   . THR A 12  ? 0.32711 0.23869 0.25399 0.11535  -0.01381 -0.04640 19  THR A O   
30   C CB  . THR A 12  ? 0.34173 0.21589 0.26654 0.07599  -0.00613 -0.07367 19  THR A CB  
31   O OG1 . THR A 12  ? 0.39177 0.25132 0.30626 0.05427  0.00013  -0.09814 19  THR A OG1 
32   C CG2 . THR A 12  ? 0.32912 0.19771 0.27123 0.07674  -0.00334 -0.05361 19  THR A CG2 
33   N N   . PHE A 13  ? 0.29497 0.22966 0.24986 0.09678  -0.02389 -0.04350 20  PHE A N   
34   C CA  . PHE A 13  ? 0.31978 0.25870 0.28186 0.10643  -0.01947 -0.02779 20  PHE A CA  
35   C C   . PHE A 13  ? 0.32955 0.26895 0.31089 0.09677  -0.01722 -0.01823 20  PHE A C   
36   O O   . PHE A 13  ? 0.30437 0.24575 0.29344 0.08517  -0.02170 -0.02130 20  PHE A O   
37   C CB  . PHE A 13  ? 0.30142 0.25725 0.26100 0.11207  -0.02232 -0.02745 20  PHE A CB  
38   C CG  . PHE A 13  ? 0.32241 0.29222 0.26124 0.12803  -0.02557 -0.03460 20  PHE A CG  
39   C CD1 . PHE A 13  ? 0.32071 0.31650 0.25590 0.12187  -0.03721 -0.05257 20  PHE A CD1 
40   C CD2 . PHE A 13  ? 0.35758 0.32003 0.27961 0.14952  -0.01545 -0.02423 20  PHE A CD2 
41   C CE1 . PHE A 13  ? 0.35770 0.38211 0.27298 0.13884  -0.04209 -0.06112 20  PHE A CE1 
42   C CE2 . PHE A 13  ? 0.40335 0.38546 0.30149 0.16938  -0.01827 -0.02844 20  PHE A CE2 
43   C CZ  . PHE A 13  ? 0.39045 0.40877 0.28556 0.16602  -0.03347 -0.04773 20  PHE A CZ  
44   N N   . ALA A 14  ? 0.27999 0.22279 0.26903 0.10107  -0.00928 -0.00765 21  ALA A N   
45   C CA  . ALA A 14  ? 0.25879 0.21862 0.26716 0.09092  -0.00852 -0.00187 21  ALA A CA  
46   C C   . ALA A 14  ? 0.24444 0.21124 0.25885 0.08074  -0.00770 -0.00455 21  ALA A C   
47   O O   . ALA A 14  ? 0.28817 0.24522 0.29413 0.08553  0.00107  -0.00405 21  ALA A O   
48   C CB  . ALA A 14  ? 0.26647 0.23967 0.28395 0.09577  0.00063  0.00617  21  ALA A CB  
49   N N   . PHE A 15  ? 0.23926 0.21909 0.26498 0.06851  -0.01330 -0.00614 22  PHE A N   
50   C CA  . PHE A 15  ? 0.24201 0.22613 0.27276 0.05735  -0.00802 -0.00926 22  PHE A CA  
51   C C   . PHE A 15  ? 0.23112 0.22445 0.27057 0.04978  0.00543  -0.00926 22  PHE A C   
52   O O   . PHE A 15  ? 0.26296 0.27962 0.31399 0.04962  0.00501  -0.00653 22  PHE A O   
53   C CB  . PHE A 15  ? 0.22955 0.23013 0.27053 0.04492  -0.01570 -0.01175 22  PHE A CB  
54   C CG  . PHE A 15  ? 0.21794 0.21069 0.25312 0.04626  -0.02475 -0.01430 22  PHE A CG  
55   C CD1 . PHE A 15  ? 0.23259 0.21767 0.25970 0.04897  -0.02368 -0.01803 22  PHE A CD1 
56   C CD2 . PHE A 15  ? 0.22668 0.22108 0.26351 0.04580  -0.03093 -0.01249 22  PHE A CD2 
57   C CE1 . PHE A 15  ? 0.23697 0.22744 0.26323 0.04803  -0.03190 -0.02260 22  PHE A CE1 
58   C CE2 . PHE A 15  ? 0.22926 0.21778 0.26307 0.04153  -0.03564 -0.01798 22  PHE A CE2 
59   C CZ  . PHE A 15  ? 0.20068 0.19310 0.23208 0.04100  -0.03781 -0.02433 22  PHE A CZ  
60   N N   . GLN A 16  ? 0.25383 0.23011 0.28711 0.04314  0.02032  -0.01287 23  GLN A N   
61   C CA  . GLN A 16  ? 0.27533 0.26132 0.31956 0.02454  0.03708  -0.01939 23  GLN A CA  
62   C C   . GLN A 16  ? 0.22366 0.25397 0.28846 0.00688  0.02696  -0.02675 23  GLN A C   
63   O O   . GLN A 16  ? 0.25457 0.29179 0.31932 0.00644  0.01376  -0.02699 23  GLN A O   
64   C CB  . GLN A 16  ? 0.31673 0.26615 0.34614 0.01721  0.06017  -0.02375 23  GLN A CB  
65   C CG  . GLN A 16  ? 0.38373 0.29310 0.38892 0.03921  0.07594  -0.01377 23  GLN A CG  
66   C CD  . GLN A 16  ? 0.54603 0.41205 0.52897 0.04056  0.10142  -0.01333 23  GLN A CD  
67   O OE1 . GLN A 16  ? 0.55643 0.41510 0.52813 0.05199  0.09475  -0.01025 23  GLN A OE1 
68   N NE2 . GLN A 16  ? 0.54165 0.37738 0.51740 0.02819  0.13444  -0.01680 23  GLN A NE2 
69   N N   . ALA A 17  ? 0.25604 0.32255 0.33823 -0.00614 0.03365  -0.03270 24  ALA A N   
70   C CA  . ALA A 17  ? 0.23979 0.36551 0.34108 -0.01722 0.02227  -0.03876 24  ALA A CA  
71   C C   . ALA A 17  ? 0.21786 0.34605 0.31780 -0.03632 0.02158  -0.05092 24  ALA A C   
72   O O   . ALA A 17  ? 0.22008 0.37898 0.32385 -0.03327 0.00580  -0.04916 24  ALA A O   
73   C CB  . ALA A 17  ? 0.23877 0.41406 0.36104 -0.03245 0.03273  -0.04820 24  ALA A CB  
74   N N   . GLU A 18  ? 0.26514 0.35533 0.35533 -0.05335 0.04174  -0.06180 25  GLU A N   
75   C CA  . GLU A 18  ? 0.25762 0.34443 0.34328 -0.07239 0.04540  -0.07505 25  GLU A CA  
76   C C   . GLU A 18  ? 0.26315 0.32958 0.33642 -0.05371 0.02919  -0.06349 25  GLU A C   
77   O O   . GLU A 18  ? 0.25697 0.34254 0.33154 -0.06259 0.02133  -0.06979 25  GLU A O   
78   C CB  . GLU A 18  ? 0.35945 0.39560 0.43086 -0.09102 0.07801  -0.08711 25  GLU A CB  
79   C CG  . GLU A 18  ? 0.40009 0.45723 0.48573 -0.11999 0.10014  -0.10490 25  GLU A CG  
80   C CD  . GLU A 18  ? 0.48482 0.52520 0.57047 -0.10529 0.11013  -0.09275 25  GLU A CD  
81   O OE1 . GLU A 18  ? 0.41634 0.43717 0.49203 -0.07172 0.09613  -0.07128 25  GLU A OE1 
82   O OE2 . GLU A 18  ? 0.60025 0.64943 0.69604 -0.12984 0.13379  -0.10699 25  GLU A OE2 
83   N N   . ILE A 19  ? 0.24957 0.28117 0.31063 -0.02926 0.02507  -0.04855 26  ILE A N   
84   C CA  . ILE A 19  ? 0.24488 0.26468 0.29765 -0.01564 0.01139  -0.04105 26  ILE A CA  
85   C C   . ILE A 19  ? 0.21070 0.26430 0.27379 -0.00908 -0.00859 -0.03464 26  ILE A C   
86   O O   . ILE A 19  ? 0.23838 0.29868 0.30045 -0.00977 -0.01719 -0.03390 26  ILE A O   
87   C CB  . ILE A 19  ? 0.24990 0.23451 0.28697 0.00627  0.01348  -0.03137 26  ILE A CB  
88   C CG1 . ILE A 19  ? 0.35062 0.29657 0.36889 0.00875  0.03580  -0.03260 26  ILE A CG1 
89   C CG2 . ILE A 19  ? 0.24571 0.23438 0.28091 0.01693  -0.00323 -0.02681 26  ILE A CG2 
90   C CD1 . ILE A 19  ? 0.49291 0.41924 0.50746 -0.00544 0.06192  -0.03935 26  ILE A CD1 
91   N N   . ALA A 20  ? 0.19996 0.27231 0.27040 -0.00060 -0.01259 -0.02847 27  ALA A N   
92   C CA  . ALA A 20  ? 0.21160 0.31010 0.28604 0.01026  -0.02481 -0.01944 27  ALA A CA  
93   C C   . ALA A 20  ? 0.21020 0.35317 0.29250 -0.00116 -0.02887 -0.02540 27  ALA A C   
94   O O   . ALA A 20  ? 0.24497 0.39661 0.32272 0.00686  -0.03666 -0.01825 27  ALA A O   
95   C CB  . ALA A 20  ? 0.22722 0.33977 0.30574 0.02451  -0.02409 -0.01084 27  ALA A CB  
96   N N   . GLN A 21  ? 0.19851 0.37027 0.29090 -0.02125 -0.02143 -0.04013 28  GLN A N   
97   C CA  . GLN A 21  ? 0.18212 0.40652 0.28138 -0.03525 -0.02588 -0.05102 28  GLN A CA  
98   C C   . GLN A 21  ? 0.25428 0.45472 0.34218 -0.04312 -0.02666 -0.05582 28  GLN A C   
99   O O   . GLN A 21  ? 0.25493 0.48746 0.34082 -0.03978 -0.03594 -0.05399 28  GLN A O   
100  C CB  . GLN A 21  ? 0.22748 0.48943 0.34072 -0.06317 -0.01448 -0.07286 28  GLN A CB  
101  C CG  . GLN A 21  ? 0.45314 0.75156 0.58222 -0.05996 -0.01125 -0.07163 28  GLN A CG  
102  C CD  . GLN A 21  ? 0.60605 0.90770 0.74567 -0.09311 0.00997  -0.09479 28  GLN A CD  
103  O OE1 . GLN A 21  ? 0.53973 0.84502 0.68852 -0.09146 0.01879  -0.09266 28  GLN A OE1 
104  N NE2 . GLN A 21  ? 0.50030 0.79169 0.63189 -0.12107 0.02139  -0.11567 28  GLN A NE2 
105  N N   . LEU A 22  ? 0.21660 0.36306 0.29481 -0.04995 -0.01542 -0.06028 29  LEU A N   
106  C CA  . LEU A 22  ? 0.25577 0.37764 0.32238 -0.05312 -0.01451 -0.06262 29  LEU A CA  
107  C C   . LEU A 22  ? 0.28413 0.40287 0.34717 -0.03378 -0.02832 -0.04668 29  LEU A C   
108  O O   . LEU A 22  ? 0.25867 0.39046 0.31771 -0.03556 -0.03300 -0.04701 29  LEU A O   
109  C CB  . LEU A 22  ? 0.29621 0.36237 0.35023 -0.05364 0.00188  -0.06469 29  LEU A CB  
110  C CG  . LEU A 22  ? 0.34759 0.38808 0.38917 -0.04904 0.00340  -0.06285 29  LEU A CG  
111  C CD1 . LEU A 22  ? 0.36456 0.41899 0.40234 -0.07081 0.01042  -0.07928 29  LEU A CD1 
112  C CD2 . LEU A 22  ? 0.36499 0.35777 0.39185 -0.03749 0.01910  -0.05855 29  LEU A CD2 
113  N N   . MET A 23  ? 0.22821 0.32752 0.29095 -0.01692 -0.03222 -0.03413 30  MET A N   
114  C CA  . MET A 23  ? 0.21142 0.30206 0.26985 -0.00407 -0.03941 -0.02254 30  MET A CA  
115  C C   . MET A 23  ? 0.24603 0.37028 0.30395 0.00404  -0.04451 -0.01396 30  MET A C   
116  O O   . MET A 23  ? 0.24010 0.36121 0.29112 0.00810  -0.04565 -0.00796 30  MET A O   
117  C CB  . MET A 23  ? 0.21566 0.27803 0.27160 0.00773  -0.03954 -0.01597 30  MET A CB  
118  C CG  . MET A 23  ? 0.21789 0.25592 0.27037 0.00663  -0.03559 -0.02202 30  MET A CG  
119  S SD  . MET A 23  ? 0.23770 0.25707 0.28611 0.01929  -0.03649 -0.01904 30  MET A SD  
120  C CE  . MET A 23  ? 0.25990 0.27160 0.30667 0.01875  -0.04043 -0.01835 30  MET A CE  
121  N N   . SER A 24  ? 0.20873 0.36900 0.27258 0.00898  -0.04593 -0.01216 31  SER A N   
122  C CA  . SER A 24  ? 0.22499 0.42861 0.28540 0.02395  -0.05006 -0.00155 31  SER A CA  
123  C C   . SER A 24  ? 0.27116 0.50760 0.32900 0.01311  -0.05379 -0.01032 31  SER A C   
124  O O   . SER A 24  ? 0.28413 0.53195 0.33031 0.02800  -0.05528 0.00180  31  SER A O   
125  C CB  . SER A 24  ? 0.32007 0.57126 0.39057 0.03119  -0.05126 -0.00059 31  SER A CB  
126  O OG  . SER A 24  ? 0.58634 0.86970 0.64810 0.05993  -0.05250 0.01851  31  SER A OG  
127  N N   . LEU A 25  ? 0.23706 0.48440 0.30212 -0.01248 -0.05193 -0.03157 32  LEU A N   
128  C CA  . LEU A 25  ? 0.22477 0.50064 0.28495 -0.02652 -0.05351 -0.04449 32  LEU A CA  
129  C C   . LEU A 25  ? 0.27905 0.51426 0.32647 -0.02165 -0.05222 -0.03674 32  LEU A C   
130  O O   . LEU A 25  ? 0.28993 0.54901 0.32767 -0.01699 -0.05543 -0.03409 32  LEU A O   
131  C CB  . LEU A 25  ? 0.29054 0.56255 0.35551 -0.05698 -0.04319 -0.06982 32  LEU A CB  
132  C CG  . LEU A 25  ? 0.43330 0.71747 0.48769 -0.07465 -0.03648 -0.08658 32  LEU A CG  
133  C CD1 . LEU A 25  ? 0.45503 0.74815 0.51305 -0.09977 -0.02171 -0.10878 32  LEU A CD1 
134  C CD2 . LEU A 25  ? 0.45711 0.69712 0.50145 -0.08160 -0.03222 -0.09038 32  LEU A CD2 
135  N N   . ILE A 26  ? 0.22295 0.40302 0.27019 -0.02208 -0.04707 -0.03370 33  ILE A N   
136  C CA  . ILE A 26  ? 0.27122 0.42074 0.31069 -0.01961 -0.04491 -0.02859 33  ILE A CA  
137  C C   . ILE A 26  ? 0.28231 0.43110 0.31471 -0.00091 -0.04629 -0.00981 33  ILE A C   
138  O O   . ILE A 26  ? 0.28942 0.43696 0.31291 0.00147  -0.04414 -0.00519 33  ILE A O   
139  C CB  . ILE A 26  ? 0.24133 0.34727 0.28378 -0.02178 -0.03981 -0.03060 33  ILE A CB  
140  C CG1 . ILE A 26  ? 0.27508 0.37015 0.31513 -0.03628 -0.03073 -0.04604 33  ILE A CG1 
141  C CG2 . ILE A 26  ? 0.24833 0.33370 0.28808 -0.01665 -0.03877 -0.02357 33  ILE A CG2 
142  C CD1 . ILE A 26  ? 0.30188 0.36062 0.34080 -0.03037 -0.02382 -0.04483 33  ILE A CD1 
143  N N   . ILE A 27  ? 0.26386 0.40927 0.29691 0.01362  -0.04605 0.00194  34  ILE A N   
144  C CA  . ILE A 27  ? 0.27757 0.40628 0.29831 0.03264  -0.03939 0.02086  34  ILE A CA  
145  C C   . ILE A 27  ? 0.31396 0.48588 0.32178 0.05061  -0.04022 0.03265  34  ILE A C   
146  O O   . ILE A 27  ? 0.37656 0.53427 0.36824 0.06406  -0.03140 0.04715  34  ILE A O   
147  C CB  . ILE A 27  ? 0.29868 0.39996 0.31975 0.04286  -0.03438 0.02840  34  ILE A CB  
148  C CG1 . ILE A 27  ? 0.29053 0.35279 0.31954 0.02782  -0.03290 0.01742  34  ILE A CG1 
149  C CG2 . ILE A 27  ? 0.34679 0.42698 0.34879 0.06597  -0.02079 0.04944  34  ILE A CG2 
150  C CD1 . ILE A 27  ? 0.31484 0.35977 0.34614 0.03260  -0.03152 0.01721  34  ILE A CD1 
151  N N   . ASN A 28  ? 0.29754 0.52736 0.31125 0.05169  -0.04919 0.02621  35  ASN A N   
152  C CA  . ASN A 28  ? 0.34902 0.63593 0.34998 0.07514  -0.05154 0.03856  35  ASN A CA  
153  C C   . ASN A 28  ? 0.32762 0.66244 0.32537 0.06291  -0.05838 0.02413  35  ASN A C   
154  O O   . ASN A 28  ? 0.40072 0.76630 0.38334 0.08224  -0.05413 0.03423  35  ASN A O   
155  C CB  . ASN A 28  ? 0.37341 0.70033 0.38223 0.08490  -0.05317 0.03910  35  ASN A CB  
156  C CG  . ASN A 28  ? 0.45620 0.74314 0.46299 0.10409  -0.04621 0.05654  35  ASN A CG  
157  O OD1 . ASN A 28  ? 0.49022 0.72692 0.47833 0.12270  -0.03306 0.07587  35  ASN A OD1 
158  N ND2 . ASN A 28  ? 0.60963 0.90385 0.63273 0.09497  -0.04889 0.04697  35  ASN A ND2 
159  N N   . THR A 29  ? 0.27772 0.60667 0.28623 0.03109  -0.06200 -0.00034 36  THR A N   
160  C CA  . THR A 29  ? 0.27594 0.63586 0.27796 0.01684  -0.06187 -0.01686 36  THR A CA  
161  C C   . THR A 29  ? 0.26766 0.61688 0.25056 0.02836  -0.06135 -0.00481 36  THR A C   
162  O O   . THR A 29  ? 0.28881 0.57451 0.27198 0.02440  -0.05324 0.00103  36  THR A O   
163  C CB  . THR A 29  ? 0.35336 0.69651 0.36623 -0.01849 -0.05871 -0.04511 36  THR A CB  
164  O OG1 . THR A 29  ? 0.34651 0.70029 0.37346 -0.02844 -0.05592 -0.05488 36  THR A OG1 
165  C CG2 . THR A 29  ? 0.36524 0.73311 0.36916 -0.03395 -0.05472 -0.06322 36  THR A CG2 
166  N N   . PHE A 30  ? 0.29930 0.68802 0.26849 0.04051  -0.05942 -0.00191 37  PHE A N   
167  C CA  . PHE A 30  ? 0.30748 0.68514 0.25554 0.05021  -0.05651 0.00842  37  PHE A CA  
168  C C   . PHE A 30  ? 0.32259 0.68236 0.27316 0.01847  -0.05705 -0.01621 37  PHE A C   
169  O O   . PHE A 30  ? 0.32485 0.70989 0.28173 -0.00338 -0.05691 -0.04118 37  PHE A O   
170  C CB  . PHE A 30  ? 0.28629 0.71167 0.22006 0.07319  -0.05269 0.01712  37  PHE A CB  
171  C CG  . PHE A 30  ? 0.30400 0.71445 0.21421 0.08388  -0.04707 0.02845  37  PHE A CG  
172  C CD1 . PHE A 30  ? 0.38544 0.74673 0.27564 0.10756  -0.03522 0.05862  37  PHE A CD1 
173  C CD2 . PHE A 30  ? 0.32058 0.75950 0.22612 0.06930  -0.04926 0.00939  37  PHE A CD2 
174  C CE1 . PHE A 30  ? 0.36568 0.70509 0.23308 0.11583  -0.02430 0.07024  37  PHE A CE1 
175  C CE2 . PHE A 30  ? 0.42886 0.85043 0.31074 0.07987  -0.04244 0.02076  37  PHE A CE2 
176  C CZ  . PHE A 30  ? 0.34874 0.72225 0.21118 0.10364  -0.02968 0.05190  37  PHE A CZ  
177  N N   . TYR A 31  ? 0.27160 0.56736 0.22227 0.01567  -0.04702 -0.00846 38  TYR A N   
178  C CA  . TYR A 31  ? 0.25444 0.52110 0.20841 -0.00875 -0.04222 -0.02770 38  TYR A CA  
179  C C   . TYR A 31  ? 0.26879 0.48771 0.21919 -0.00144 -0.03154 -0.01236 38  TYR A C   
180  O O   . TYR A 31  ? 0.29391 0.47450 0.25664 0.00103  -0.02698 -0.00238 38  TYR A O   
181  C CB  . TYR A 31  ? 0.31125 0.55339 0.28382 -0.02832 -0.04165 -0.04334 38  TYR A CB  
182  C CG  . TYR A 31  ? 0.28343 0.48680 0.25499 -0.04526 -0.03169 -0.05758 38  TYR A CG  
183  C CD1 . TYR A 31  ? 0.36317 0.57980 0.32286 -0.06391 -0.02657 -0.08073 38  TYR A CD1 
184  C CD2 . TYR A 31  ? 0.40281 0.55890 0.38359 -0.04169 -0.02544 -0.04911 38  TYR A CD2 
185  C CE1 . TYR A 31  ? 0.46552 0.63933 0.41873 -0.07461 -0.01240 -0.09128 38  TYR A CE1 
186  C CE2 . TYR A 31  ? 0.36634 0.49222 0.34317 -0.04977 -0.01445 -0.05879 38  TYR A CE2 
187  C CZ  . TYR A 31  ? 0.45791 0.58793 0.41946 -0.06447 -0.00658 -0.07816 38  TYR A CZ  
188  O OH  . TYR A 31  ? 0.70603 0.79883 0.65845 -0.06820 0.00913  -0.08557 38  TYR A OH  
189  N N   . SER A 32  ? 0.27988 0.50477 0.21417 -0.00025 -0.02665 -0.01299 39  SER A N   
190  C CA  . SER A 32  ? 0.28380 0.47293 0.21472 0.00805  -0.01448 0.00341  39  SER A CA  
191  C C   . SER A 32  ? 0.28449 0.43641 0.23119 -0.00703 -0.00816 -0.00543 39  SER A C   
192  O O   . SER A 32  ? 0.33091 0.45715 0.28482 -0.00421 0.00117  0.00578  39  SER A O   
193  C CB  . SER A 32  ? 0.31448 0.52520 0.22037 0.01846  -0.00977 0.00871  39  SER A CB  
194  O OG  . SER A 32  ? 0.33824 0.59005 0.22658 0.04056  -0.01457 0.02157  39  SER A OG  
195  N N   . ASN A 33  ? 0.29474 0.44480 0.24559 -0.02198 -0.01026 -0.02526 40  ASN A N   
196  C CA  . ASN A 33  ? 0.30063 0.42159 0.25881 -0.02832 -0.00142 -0.03126 40  ASN A CA  
197  C C   . ASN A 33  ? 0.27430 0.37606 0.25368 -0.02792 -0.00313 -0.02795 40  ASN A C   
198  O O   . ASN A 33  ? 0.29451 0.38257 0.27781 -0.03205 -0.00081 -0.03753 40  ASN A O   
199  C CB  . ASN A 33  ? 0.34099 0.45946 0.28595 -0.04074 0.00380  -0.05223 40  ASN A CB  
200  C CG  . ASN A 33  ? 0.34378 0.43041 0.28908 -0.03994 0.01727  -0.05565 40  ASN A CG  
201  O OD1 . ASN A 33  ? 0.35435 0.43643 0.30613 -0.03083 0.02197  -0.04450 40  ASN A OD1 
202  N ND2 . ASN A 33  ? 0.36891 0.43460 0.30497 -0.04877 0.02681  -0.07142 40  ASN A ND2 
203  N N   . LYS A 34  ? 0.32331 0.31064 0.23725 0.00384  -0.07581 -0.02369 41  LYS A N   
204  C CA  . LYS A 34  ? 0.25427 0.29516 0.23222 -0.00178 -0.05481 -0.01967 41  LYS A CA  
205  C C   . LYS A 34  ? 0.27936 0.31053 0.24912 0.00899  -0.03339 -0.02905 41  LYS A C   
206  O O   . LYS A 34  ? 0.26282 0.31910 0.26827 0.00252  -0.02630 -0.02855 41  LYS A O   
207  C CB  . LYS A 34  ? 0.25162 0.33132 0.26580 0.00687  -0.03733 -0.01313 41  LYS A CB  
208  C CG  . LYS A 34  ? 0.21532 0.32140 0.25352 0.00031  -0.05220 0.00114  41  LYS A CG  
209  C CD  . LYS A 34  ? 0.25956 0.38643 0.31733 0.01576  -0.03585 0.00386  41  LYS A CD  
210  C CE  . LYS A 34  ? 0.23344 0.39224 0.31681 0.01719  -0.04520 0.02119  41  LYS A CE  
211  N NZ  . LYS A 34  ? 0.22154 0.42603 0.34548 0.02037  -0.04212 0.04052  41  LYS A NZ  
212  N N   . GLU A 35  ? 0.30585 0.30316 0.22753 0.03020  -0.02145 -0.03298 42  GLU A N   
213  C CA  . GLU A 35  ? 0.29532 0.29913 0.22453 0.04372  0.00300  -0.03115 42  GLU A CA  
214  C C   . GLU A 35  ? 0.32379 0.31220 0.25007 0.03335  -0.00599 -0.04096 42  GLU A C   
215  O O   . GLU A 35  ? 0.31282 0.31496 0.25930 0.03899  0.01094  -0.03838 42  GLU A O   
216  C CB  . GLU A 35  ? 0.36779 0.34650 0.24370 0.07929  0.02346  -0.02227 42  GLU A CB  
217  C CG  . GLU A 35  ? 0.41546 0.31810 0.19554 0.10022  0.00883  -0.03654 42  GLU A CG  
218  C CD  . GLU A 35  ? 0.53039 0.40245 0.23553 0.15320  0.03558  -0.02418 42  GLU A CD  
219  O OE1 . GLU A 35  ? 0.63914 0.54427 0.36151 0.16421  0.05325  -0.00526 42  GLU A OE1 
220  O OE2 . GLU A 35  ? 0.77589 0.58757 0.39913 0.18812  0.03892  -0.03103 42  GLU A OE2 
221  N N   . ILE A 36  ? 0.32968 0.28798 0.23366 0.01643  -0.03692 -0.04689 43  ILE A N   
222  C CA  . ILE A 36  ? 0.32153 0.26238 0.22368 0.00455  -0.04925 -0.05102 43  ILE A CA  
223  C C   . ILE A 36  ? 0.26517 0.26318 0.23513 -0.00870 -0.03578 -0.04413 43  ILE A C   
224  O O   . ILE A 36  ? 0.27504 0.26630 0.24823 -0.01442 -0.03759 -0.04578 43  ILE A O   
225  C CB  . ILE A 36  ? 0.38347 0.27723 0.25643 -0.01818 -0.09750 -0.04839 43  ILE A CB  
226  C CG1 . ILE A 36  ? 0.39813 0.34502 0.33332 -0.04385 -0.11332 -0.02729 43  ILE A CG1 
227  C CG2 . ILE A 36  ? 0.48613 0.28845 0.25616 0.00405  -0.11962 -0.06172 43  ILE A CG2 
228  C CD1 . ILE A 36  ? 0.38531 0.39022 0.39240 -0.06512 -0.11352 -0.00511 43  ILE A CD1 
229  N N   . PHE A 37  ? 0.22446 0.26814 0.23622 -0.00808 -0.02347 -0.03716 44  PHE A N   
230  C CA  . PHE A 37  ? 0.20784 0.28441 0.25584 -0.00768 -0.01181 -0.03349 44  PHE A CA  
231  C C   . PHE A 37  ? 0.21990 0.28261 0.26264 -0.00042 0.00000  -0.04183 44  PHE A C   
232  O O   . PHE A 37  ? 0.20459 0.27427 0.25814 -0.00242 0.00190  -0.04163 44  PHE A O   
233  C CB  . PHE A 37  ? 0.19406 0.29515 0.26096 0.00388  -0.00324 -0.02953 44  PHE A CB  
234  C CG  . PHE A 37  ? 0.18405 0.27019 0.24742 0.01280  0.00306  -0.03488 44  PHE A CG  
235  C CD1 . PHE A 37  ? 0.21197 0.29298 0.26809 0.01520  0.00436  -0.03084 44  PHE A CD1 
236  C CD2 . PHE A 37  ? 0.20422 0.28008 0.27381 0.01740  0.00305  -0.03742 44  PHE A CD2 
237  C CE1 . PHE A 37  ? 0.19096 0.27091 0.26123 0.02006  0.00884  -0.02109 44  PHE A CE1 
238  C CE2 . PHE A 37  ? 0.20164 0.26703 0.28404 0.01709  -0.00187 -0.02988 44  PHE A CE2 
239  C CZ  . PHE A 37  ? 0.20818 0.28250 0.29870 0.01741  0.00259  -0.01749 44  PHE A CZ  
240  N N   . LEU A 38  ? 0.21053 0.25959 0.24081 0.01049  0.00926  -0.04242 45  LEU A N   
241  C CA  . LEU A 38  ? 0.19251 0.24332 0.23731 0.01602  0.01867  -0.03878 45  LEU A CA  
242  C C   . LEU A 38  ? 0.23217 0.26212 0.25516 0.01709  0.01907  -0.04470 45  LEU A C   
243  O O   . LEU A 38  ? 0.22760 0.26193 0.26680 0.01364  0.01968  -0.04495 45  LEU A O   
244  C CB  . LEU A 38  ? 0.18799 0.24858 0.24400 0.02898  0.03115  -0.02123 45  LEU A CB  
245  C CG  . LEU A 38  ? 0.17599 0.25193 0.26842 0.03097  0.03598  -0.00221 45  LEU A CG  
246  C CD1 . LEU A 38  ? 0.18376 0.25536 0.30131 0.01443  0.01369  -0.00632 45  LEU A CD1 
247  C CD2 . LEU A 38  ? 0.22307 0.32701 0.34474 0.04352  0.04976  0.03234  45  LEU A CD2 
248  N N   . ARG A 39  ? 0.26174 0.25673 0.23798 0.02352  0.01323  -0.05027 46  ARG A N   
249  C CA  . ARG A 39  ? 0.28833 0.24495 0.23046 0.02486  0.00446  -0.05756 46  ARG A CA  
250  C C   . ARG A 39  ? 0.28794 0.25979 0.26043 -0.00071 -0.01036 -0.05701 46  ARG A C   
251  O O   . ARG A 39  ? 0.29606 0.25894 0.26856 -0.00220 -0.01012 -0.05836 46  ARG A O   
252  C CB  . ARG A 39  ? 0.39222 0.28390 0.26037 0.03570  -0.01472 -0.06578 46  ARG A CB  
253  C CG  . ARG A 39  ? 0.58370 0.41646 0.41041 0.02580  -0.04495 -0.07369 46  ARG A CG  
254  C CD  . ARG A 39  ? 0.66889 0.41657 0.41217 0.03040  -0.08326 -0.08225 46  ARG A CD  
255  N NE  . ARG A 39  ? 0.70078 0.46394 0.47997 -0.00837 -0.11888 -0.07150 46  ARG A NE  
256  C CZ  . ARG A 39  ? 0.71734 0.42168 0.44588 -0.01285 -0.15768 -0.07115 46  ARG A CZ  
257  N NH1 . ARG A 39  ? 0.78158 0.41362 0.42415 0.02489  -0.15754 -0.07865 46  ARG A NH1 
258  N NH2 . ARG A 39  ? 0.72117 0.45729 0.50456 -0.05059 -0.18845 -0.05013 46  ARG A NH2 
259  N N   . GLU A 40  ? 0.23661 0.23731 0.23719 -0.01672 -0.02018 -0.04903 47  GLU A N   
260  C CA  . GLU A 40  ? 0.19446 0.22248 0.22771 -0.03287 -0.02744 -0.03541 47  GLU A CA  
261  C C   . GLU A 40  ? 0.20252 0.25482 0.25455 -0.02146 -0.00714 -0.03697 47  GLU A C   
262  O O   . GLU A 40  ? 0.21806 0.27600 0.27821 -0.02591 -0.00748 -0.03006 47  GLU A O   
263  C CB  . GLU A 40  ? 0.18390 0.25094 0.24977 -0.04366 -0.03634 -0.01456 47  GLU A CB  
264  C CG  . GLU A 40  ? 0.24264 0.27918 0.29232 -0.06243 -0.07076 -0.00754 47  GLU A CG  
265  C CD  . GLU A 40  ? 0.30997 0.29116 0.33165 -0.08114 -0.10552 -0.00558 47  GLU A CD  
266  O OE1 . GLU A 40  ? 0.33365 0.33337 0.38356 -0.09186 -0.10617 0.00892  47  GLU A OE1 
267  O OE2 . GLU A 40  ? 0.45303 0.36312 0.41630 -0.08342 -0.13710 -0.01683 47  GLU A OE2 
268  N N   . LEU A 41  ? 0.18421 0.24398 0.23951 -0.00753 0.00441  -0.04339 48  LEU A N   
269  C CA  . LEU A 41  ? 0.19145 0.25185 0.24909 0.00337  0.00988  -0.04606 48  LEU A CA  
270  C C   . LEU A 41  ? 0.20477 0.24590 0.25994 0.00195  0.00949  -0.05074 48  LEU A C   
271  O O   . LEU A 41  ? 0.20555 0.24159 0.25777 0.00471  0.00820  -0.05114 48  LEU A O   
272  C CB  . LEU A 41  ? 0.20069 0.25551 0.25636 0.01471  0.00731  -0.04910 48  LEU A CB  
273  C CG  . LEU A 41  ? 0.21004 0.28308 0.26387 0.02444  0.01055  -0.04339 48  LEU A CG  
274  C CD1 . LEU A 41  ? 0.22663 0.27635 0.26814 0.03644  0.00121  -0.04870 48  LEU A CD1 
275  C CD2 . LEU A 41  ? 0.21379 0.30983 0.26274 0.04063  0.02105  -0.03028 48  LEU A CD2 
276  N N   . ILE A 42  ? 0.19278 0.22448 0.24588 0.00359  0.01308  -0.05027 49  ILE A N   
277  C CA  . ILE A 42  ? 0.20009 0.22205 0.25448 0.00914  0.01778  -0.04676 49  ILE A CA  
278  C C   . ILE A 42  ? 0.22674 0.22959 0.26053 0.00434  0.01388  -0.05263 49  ILE A C   
279  O O   . ILE A 42  ? 0.22639 0.22532 0.26554 0.00538  0.01422  -0.05121 49  ILE A O   
280  C CB  . ILE A 42  ? 0.19592 0.21898 0.24716 0.02558  0.03126  -0.03550 49  ILE A CB  
281  C CG1 . ILE A 42  ? 0.16882 0.21870 0.26021 0.02399  0.03012  -0.01804 49  ILE A CG1 
282  C CG2 . ILE A 42  ? 0.23003 0.24464 0.27424 0.04214  0.04259  -0.02672 49  ILE A CG2 
283  C CD1 . ILE A 42  ? 0.20118 0.26891 0.29801 0.04506  0.05038  0.00586  49  ILE A CD1 
284  N N   . SER A 43  ? 0.23280 0.22006 0.24551 -0.00436 0.00343  -0.05540 50  SER A N   
285  C CA  . SER A 43  ? 0.23523 0.19835 0.23337 -0.01534 -0.01072 -0.05432 50  SER A CA  
286  C C   . SER A 43  ? 0.24877 0.24433 0.27747 -0.02481 -0.00874 -0.04396 50  SER A C   
287  O O   . SER A 43  ? 0.23279 0.21732 0.25889 -0.02795 -0.01169 -0.04145 50  SER A O   
288  C CB  . SER A 43  ? 0.35776 0.29197 0.33353 -0.02999 -0.03674 -0.05119 50  SER A CB  
289  O OG  . SER A 43  ? 0.44897 0.36192 0.42370 -0.05000 -0.06142 -0.04072 50  SER A OG  
290  N N   . ASN A 44  ? 0.21382 0.24576 0.26312 -0.02246 -0.00163 -0.03626 51  ASN A N   
291  C CA  . ASN A 44  ? 0.19347 0.25086 0.25297 -0.01501 0.00710  -0.02423 51  ASN A CA  
292  C C   . ASN A 44  ? 0.19647 0.23322 0.24088 -0.00282 0.01029  -0.03669 51  ASN A C   
293  O O   . ASN A 44  ? 0.20115 0.23794 0.24097 -0.00008 0.01206  -0.03002 51  ASN A O   
294  C CB  . ASN A 44  ? 0.18727 0.27514 0.25176 0.00099  0.01767  -0.01498 51  ASN A CB  
295  C CG  . ASN A 44  ? 0.24785 0.37526 0.34362 -0.01077 0.01491  0.01314  51  ASN A CG  
296  O OD1 . ASN A 44  ? 0.25282 0.38114 0.36795 -0.03572 -0.00208 0.02941  51  ASN A OD1 
297  N ND2 . ASN A 44  ? 0.19483 0.35276 0.29692 0.00728  0.02675  0.02449  51  ASN A ND2 
298  N N   . SER A 45  ? 0.18430 0.20547 0.22641 0.00243  0.00732  -0.04839 52  SER A N   
299  C CA  . SER A 45  ? 0.20838 0.21008 0.24808 0.00717  -0.00059 -0.05170 52  SER A CA  
300  C C   . SER A 45  ? 0.20870 0.20325 0.25296 0.00159  0.00115  -0.04964 52  SER A C   
301  O O   . SER A 45  ? 0.22479 0.20877 0.26351 0.00387  -0.00429 -0.04852 52  SER A O   
302  C CB  . SER A 45  ? 0.19698 0.19406 0.25426 0.00650  -0.00989 -0.04940 52  SER A CB  
303  O OG  . SER A 45  ? 0.21480 0.20109 0.25767 0.01340  -0.01994 -0.05319 52  SER A OG  
304  N N   . SER A 46  ? 0.21940 0.20925 0.26201 -0.00074 0.00646  -0.04990 53  SER A N   
305  C CA  . SER A 46  ? 0.22404 0.19302 0.25528 0.00232  0.00715  -0.04927 53  SER A CA  
306  C C   . SER A 46  ? 0.24967 0.21186 0.27336 -0.00903 -0.00047 -0.04690 53  SER A C   
307  O O   . SER A 46  ? 0.24396 0.19614 0.26615 -0.00682 -0.00182 -0.04501 53  SER A O   
308  C CB  . SER A 46  ? 0.24259 0.18501 0.24429 0.01267  0.01013  -0.05280 53  SER A CB  
309  O OG  . SER A 46  ? 0.30194 0.20801 0.27473 0.02360  0.00842  -0.05408 53  SER A OG  
310  N N   . ASP A 47  ? 0.22895 0.20548 0.25677 -0.02100 -0.00510 -0.03926 54  ASP A N   
311  C CA  . ASP A 47  ? 0.23990 0.22617 0.27598 -0.03238 -0.01065 -0.02191 54  ASP A CA  
312  C C   . ASP A 47  ? 0.25929 0.26175 0.29426 -0.01801 0.00081  -0.01813 54  ASP A C   
313  O O   . ASP A 47  ? 0.25415 0.25317 0.28768 -0.02040 -0.00077 -0.00811 54  ASP A O   
314  C CB  . ASP A 47  ? 0.21492 0.23296 0.27394 -0.04569 -0.01579 0.00042  54  ASP A CB  
315  C CG  . ASP A 47  ? 0.30180 0.28564 0.35276 -0.06637 -0.04319 0.00142  54  ASP A CG  
316  O OD1 . ASP A 47  ? 0.37392 0.29881 0.38599 -0.06380 -0.05629 -0.01678 54  ASP A OD1 
317  O OD2 . ASP A 47  ? 0.30547 0.31524 0.38279 -0.08191 -0.05503 0.02359  54  ASP A OD2 
318  N N   . ALA A 48  ? 0.20971 0.21848 0.23531 -0.00100 0.00751  -0.02605 55  ALA A N   
319  C CA  . ALA A 48  ? 0.23877 0.23785 0.23776 0.01950  0.00933  -0.02615 55  ALA A CA  
320  C C   . ALA A 48  ? 0.23463 0.20271 0.22873 0.01683  -0.00415 -0.03639 55  ALA A C   
321  O O   . ALA A 48  ? 0.26028 0.21339 0.23181 0.02690  -0.00776 -0.03347 55  ALA A O   
322  C CB  . ALA A 48  ? 0.26625 0.25498 0.23889 0.04075  0.00816  -0.03434 55  ALA A CB  
323  N N   . LEU A 49  ? 0.24259 0.20490 0.25853 0.00743  -0.01032 -0.04284 56  LEU A N   
324  C CA  . LEU A 49  ? 0.23784 0.18668 0.26614 0.00594  -0.02004 -0.04064 56  LEU A CA  
325  C C   . LEU A 49  ? 0.25408 0.19751 0.27912 0.00246  -0.01441 -0.03694 56  LEU A C   
326  O O   . LEU A 49  ? 0.25831 0.18986 0.28052 0.00486  -0.02217 -0.03329 56  LEU A O   
327  C CB  . LEU A 49  ? 0.20845 0.16911 0.26865 0.00501  -0.01873 -0.03463 56  LEU A CB  
328  C CG  . LEU A 49  ? 0.21332 0.17234 0.28590 0.00284  -0.03680 -0.03075 56  LEU A CG  
329  C CD1 . LEU A 49  ? 0.23400 0.21926 0.33999 0.00301  -0.02623 -0.01890 56  LEU A CD1 
330  C CD2 . LEU A 49  ? 0.23770 0.17680 0.32259 -0.00199 -0.06847 -0.01880 56  LEU A CD2 
331  N N   . ASP A 50  ? 0.23341 0.17586 0.25474 -0.00450 -0.00817 -0.03675 57  ASP A N   
332  C CA  . ASP A 50  ? 0.23938 0.16130 0.25032 -0.01058 -0.01287 -0.03184 57  ASP A CA  
333  C C   . ASP A 50  ? 0.28804 0.22054 0.29720 -0.01343 -0.01369 -0.01992 57  ASP A C   
334  O O   . ASP A 50  ? 0.28307 0.19938 0.28694 -0.01382 -0.01843 -0.01576 57  ASP A O   
335  C CB  . ASP A 50  ? 0.27130 0.17525 0.27123 -0.02355 -0.02230 -0.02955 57  ASP A CB  
336  C CG  . ASP A 50  ? 0.34643 0.21881 0.32199 -0.01117 -0.02265 -0.04213 57  ASP A CG  
337  O OD1 . ASP A 50  ? 0.37288 0.24817 0.34943 0.01028  -0.00873 -0.04545 57  ASP A OD1 
338  O OD2 . ASP A 50  ? 0.38640 0.22820 0.33975 -0.02147 -0.03995 -0.04273 57  ASP A OD2 
339  N N   . LYS A 51  ? 0.24972 0.20987 0.25867 -0.00948 -0.00600 -0.01052 58  LYS A N   
340  C CA  . LYS A 51  ? 0.25787 0.23333 0.25673 -0.00031 0.00131  0.00899  58  LYS A CA  
341  C C   . LYS A 51  ? 0.29182 0.24029 0.25999 0.01732  -0.00413 -0.00156 58  LYS A C   
342  O O   . LYS A 51  ? 0.30834 0.25195 0.26647 0.02033  -0.00391 0.01013  58  LYS A O   
343  C CB  . LYS A 51  ? 0.26111 0.27407 0.25788 0.01522  0.01787  0.02643  58  LYS A CB  
344  C CG  . LYS A 51  ? 0.29070 0.34242 0.33113 -0.00696 0.01809  0.05505  58  LYS A CG  
345  C CD  . LYS A 51  ? 0.28772 0.38781 0.33177 0.01682  0.04023  0.07831  58  LYS A CD  
346  C CE  . LYS A 51  ? 0.47407 0.61544 0.57013 -0.00712 0.03441  0.10629  58  LYS A CE  
347  N NZ  . LYS A 51  ? 0.47838 0.68267 0.58335 0.02651  0.06480  0.14396  58  LYS A NZ  
348  N N   . ILE A 52  ? 0.30397 0.23083 0.25625 0.02750  -0.01504 -0.01931 59  ILE A N   
349  C CA  . ILE A 52  ? 0.33298 0.22234 0.25523 0.03877  -0.03466 -0.02529 59  ILE A CA  
350  C C   . ILE A 52  ? 0.31775 0.20266 0.27244 0.02299  -0.04429 -0.02355 59  ILE A C   
351  O O   . ILE A 52  ? 0.34918 0.21365 0.28678 0.02781  -0.05560 -0.01981 59  ILE A O   
352  C CB  . ILE A 52  ? 0.35033 0.20402 0.24634 0.04865  -0.05933 -0.03802 59  ILE A CB  
353  C CG1 . ILE A 52  ? 0.43747 0.23403 0.28425 0.06146  -0.09198 -0.04141 59  ILE A CG1 
354  C CG2 . ILE A 52  ? 0.32396 0.19074 0.27487 0.02738  -0.07045 -0.03906 59  ILE A CG2 
355  C CD1 . ILE A 52  ? 0.48745 0.26258 0.25920 0.09664  -0.07854 -0.03779 59  ILE A CD1 
356  N N   . ARG A 53  ? 0.29051 0.19136 0.28335 0.01087  -0.03764 -0.02399 60  ARG A N   
357  C CA  . ARG A 53  ? 0.28856 0.18409 0.30128 0.00873  -0.03955 -0.01804 60  ARG A CA  
358  C C   . ARG A 53  ? 0.31087 0.19521 0.30670 0.00612  -0.03611 -0.01268 60  ARG A C   
359  O O   . ARG A 53  ? 0.34063 0.21202 0.33448 0.00936  -0.04471 -0.00724 60  ARG A O   
360  C CB  . ARG A 53  ? 0.28164 0.18540 0.31436 0.01146  -0.02743 -0.01787 60  ARG A CB  
361  C CG  . ARG A 53  ? 0.36748 0.26553 0.41352 0.02374  -0.02512 -0.00667 60  ARG A CG  
362  C CD  . ARG A 53  ? 0.55796 0.45188 0.59865 0.04238  -0.00794 -0.00506 60  ARG A CD  
363  N NE  . ARG A 53  ? 0.67204 0.60404 0.75784 0.05668  0.00017  0.01749  60  ARG A NE  
364  C CZ  . ARG A 53  ? 0.57512 0.52322 0.66615 0.06900  0.01542  0.02220  60  ARG A CZ  
365  N NH1 . ARG A 53  ? 0.52055 0.44090 0.56734 0.06877  0.02032  0.00062  60  ARG A NH1 
366  N NH2 . ARG A 53  ? 0.46715 0.46277 0.61384 0.08044  0.02296  0.05551  60  ARG A NH2 
367  N N   . TYR A 54  ? 0.31492 0.20621 0.30432 -0.00248 -0.02803 -0.00791 61  TYR A N   
368  C CA  . TYR A 54  ? 0.31864 0.20125 0.30292 -0.01086 -0.03081 0.00685  61  TYR A CA  
369  C C   . TYR A 54  ? 0.33497 0.22263 0.30103 0.00041  -0.02919 0.01727  61  TYR A C   
370  O O   . TYR A 54  ? 0.35112 0.22278 0.31222 -0.00036 -0.03542 0.02427  61  TYR A O   
371  C CB  . TYR A 54  ? 0.32097 0.21684 0.31682 -0.02872 -0.03176 0.02349  61  TYR A CB  
372  C CG  . TYR A 54  ? 0.36306 0.24684 0.36420 -0.04478 -0.04421 0.04777  61  TYR A CG  
373  C CD1 . TYR A 54  ? 0.40198 0.23093 0.38848 -0.05321 -0.06522 0.04051  61  TYR A CD1 
374  C CD2 . TYR A 54  ? 0.38341 0.30629 0.39866 -0.04627 -0.03517 0.08181  61  TYR A CD2 
375  C CE1 . TYR A 54  ? 0.43278 0.24031 0.42221 -0.07088 -0.08458 0.06397  61  TYR A CE1 
376  C CE2 . TYR A 54  ? 0.38963 0.30778 0.41961 -0.06389 -0.04838 0.11222  61  TYR A CE2 
377  C CZ  . TYR A 54  ? 0.43680 0.29409 0.45607 -0.08072 -0.07725 0.10239  61  TYR A CZ  
378  O OH  . TYR A 54  ? 0.52667 0.36911 0.55923 -0.10179 -0.09842 0.13468  61  TYR A OH  
379  N N   . GLU A 55  ? 0.35581 0.25640 0.29970 0.01699  -0.02174 0.01788  62  GLU A N   
380  C CA  . GLU A 55  ? 0.37657 0.26522 0.27698 0.04008  -0.02086 0.02629  62  GLU A CA  
381  C C   . GLU A 55  ? 0.40967 0.25887 0.29681 0.04178  -0.04510 0.01285  62  GLU A C   
382  O O   . GLU A 55  ? 0.47071 0.30393 0.33250 0.05078  -0.04941 0.02196  62  GLU A O   
383  C CB  . GLU A 55  ? 0.41557 0.30213 0.27014 0.07007  -0.01249 0.02381  62  GLU A CB  
384  C CG  . GLU A 55  ? 0.45633 0.39641 0.32949 0.07529  0.01629  0.05168  62  GLU A CG  
385  C CD  . GLU A 55  ? 0.60976 0.55026 0.42174 0.12288  0.03529  0.06096  62  GLU A CD  
386  O OE1 . GLU A 55  ? 0.63449 0.63364 0.46721 0.13550  0.06514  0.09814  62  GLU A OE1 
387  O OE2 . GLU A 55  ? 0.63441 0.51287 0.37603 0.14961  0.01687  0.03501  62  GLU A OE2 
388  N N   . SER A 56  ? 0.38835 0.22735 0.29927 0.03294  -0.06207 -0.00162 63  SER A N   
389  C CA  . SER A 56  ? 0.43427 0.24760 0.35136 0.03107  -0.09028 -0.00196 63  SER A CA  
390  C C   . SER A 56  ? 0.41669 0.23688 0.36323 0.02340  -0.08611 0.00805  63  SER A C   
391  O O   . SER A 56  ? 0.44265 0.24619 0.39262 0.02445  -0.10745 0.01478  63  SER A O   
392  C CB  . SER A 56  ? 0.42329 0.24091 0.37793 0.02200  -0.10857 -0.00378 63  SER A CB  
393  O OG  . SER A 56  ? 0.39917 0.25231 0.40709 0.01447  -0.08837 0.00210  63  SER A OG  
394  N N   . LEU A 57  ? 0.38644 0.22106 0.34809 0.01657  -0.06550 0.01053  64  LEU A N   
395  C CA  . LEU A 57  ? 0.41522 0.23860 0.38951 0.01538  -0.06568 0.01753  64  LEU A CA  
396  C C   . LEU A 57  ? 0.52650 0.33465 0.47742 0.01733  -0.07313 0.02771  64  LEU A C   
397  O O   . LEU A 57  ? 0.55185 0.34677 0.51125 0.02045  -0.08157 0.03382  64  LEU A O   
398  C CB  . LEU A 57  ? 0.41370 0.22822 0.38719 0.00834  -0.05550 0.01627  64  LEU A CB  
399  C CG  . LEU A 57  ? 0.41048 0.23077 0.39494 0.01310  -0.04745 0.00593  64  LEU A CG  
400  C CD1 . LEU A 57  ? 0.42539 0.21073 0.38738 0.00846  -0.04998 0.00258  64  LEU A CD1 
401  C CD2 . LEU A 57  ? 0.43893 0.26925 0.44824 0.03166  -0.04423 0.01074  64  LEU A CD2 
402  N N   . THR A 58  ? 0.44764 0.26060 0.36778 0.02108  -0.06686 0.03418  65  THR A N   
403  C CA  . THR A 58  ? 0.53836 0.33955 0.42894 0.02940  -0.06925 0.04889  65  THR A CA  
404  C C   . THR A 58  ? 0.51385 0.28975 0.35033 0.05232  -0.08281 0.04348  65  THR A C   
405  O O   . THR A 58  ? 0.63243 0.38698 0.43226 0.06510  -0.08966 0.05303  65  THR A O   
406  C CB  . THR A 58  ? 0.62661 0.45390 0.51917 0.02412  -0.04977 0.07479  65  THR A CB  
407  O OG1 . THR A 58  ? 0.61425 0.46972 0.49791 0.03424  -0.03291 0.07908  65  THR A OG1 
408  C CG2 . THR A 58  ? 0.59834 0.42180 0.52912 -0.00209 -0.05489 0.08063  65  THR A CG2 
409  N N   . ASP A 59  ? 0.56045 0.37242 0.41414 0.14870  -0.01605 0.09289  66  ASP A N   
410  C CA  . ASP A 59  ? 0.52898 0.38097 0.38255 0.14740  -0.03298 0.09254  66  ASP A CA  
411  C C   . ASP A 59  ? 0.50323 0.39429 0.38655 0.14499  -0.04613 0.08108  66  ASP A C   
412  O O   . ASP A 59  ? 0.47811 0.37789 0.37076 0.12779  -0.04776 0.06404  66  ASP A O   
413  C CB  . ASP A 59  ? 0.54287 0.39062 0.37916 0.12936  -0.03005 0.08526  66  ASP A CB  
414  C CG  . ASP A 59  ? 0.63326 0.50936 0.45613 0.13013  -0.04585 0.08301  66  ASP A CG  
415  O OD1 . ASP A 59  ? 0.62065 0.52104 0.44879 0.14059  -0.06283 0.08754  66  ASP A OD1 
416  O OD2 . ASP A 59  ? 0.61798 0.49145 0.42357 0.12044  -0.04137 0.07749  66  ASP A OD2 
417  N N   . PRO A 60  ? 0.53856 0.45677 0.43999 0.16207  -0.05571 0.09265  67  PRO A N   
418  C CA  . PRO A 60  ? 0.53272 0.49198 0.46766 0.15729  -0.06791 0.08531  67  PRO A CA  
419  C C   . PRO A 60  ? 0.45982 0.44276 0.39095 0.13842  -0.08749 0.07295  67  PRO A C   
420  O O   . PRO A 60  ? 0.43862 0.44319 0.39298 0.12655  -0.09445 0.06203  67  PRO A O   
421  C CB  . PRO A 60  ? 0.54550 0.53508 0.50155 0.18070  -0.07483 0.10704  67  PRO A CB  
422  C CG  . PRO A 60  ? 0.67398 0.62407 0.60761 0.20138  -0.05818 0.12230  67  PRO A CG  
423  C CD  . PRO A 60  ? 0.54791 0.46168 0.44418 0.18731  -0.05382 0.11572  67  PRO A CD  
424  N N   . SER A 61  ? 0.51307 0.48800 0.41127 0.13612  -0.09551 0.07449  68  SER A N   
425  C CA  . SER A 61  ? 0.46551 0.45145 0.35006 0.12015  -0.11235 0.06037  68  SER A CA  
426  C C   . SER A 61  ? 0.47305 0.44367 0.35856 0.10419  -0.10112 0.04064  68  SER A C   
427  O O   . SER A 61  ? 0.43933 0.41600 0.31850 0.09182  -0.11308 0.02723  68  SER A O   
428  C CB  . SER A 61  ? 0.48831 0.46177 0.32789 0.12399  -0.11942 0.06526  68  SER A CB  
429  O OG  . SER A 61  ? 0.58892 0.52994 0.40522 0.12471  -0.09716 0.06487  68  SER A OG  
430  N N   . LYS A 62  ? 0.44672 0.39572 0.33845 0.10365  -0.07971 0.03908  69  LYS A N   
431  C CA  . LYS A 62  ? 0.40168 0.34337 0.29949 0.08904  -0.07122 0.02322  69  LYS A CA  
432  C C   . LYS A 62  ? 0.38266 0.34608 0.30878 0.08095  -0.08056 0.01322  69  LYS A C   
433  O O   . LYS A 62  ? 0.36023 0.32124 0.28892 0.06928  -0.07840 0.00014  69  LYS A O   
434  C CB  . LYS A 62  ? 0.42104 0.33843 0.32268 0.08741  -0.05146 0.02541  69  LYS A CB  
435  C CG  . LYS A 62  ? 0.51483 0.40889 0.39158 0.08987  -0.04024 0.03640  69  LYS A CG  
436  C CD  . LYS A 62  ? 0.54276 0.43426 0.41174 0.07737  -0.03190 0.03014  69  LYS A CD  
437  C CE  . LYS A 62  ? 0.55550 0.43142 0.40239 0.07883  -0.01996 0.04427  69  LYS A CE  
438  N NZ  . LYS A 62  ? 0.65888 0.53896 0.51170 0.06547  -0.00837 0.04127  69  LYS A NZ  
439  N N   . LEU A 63  ? 0.35776 0.34395 0.30817 0.08798  -0.08868 0.02173  70  LEU A N   
440  C CA  . LEU A 63  ? 0.36722 0.37827 0.34775 0.07953  -0.09664 0.01632  70  LEU A CA  
441  C C   . LEU A 63  ? 0.35627 0.39207 0.33834 0.07116  -0.12220 0.01686  70  LEU A C   
442  O O   . LEU A 63  ? 0.38896 0.45085 0.40056 0.06263  -0.13188 0.01730  70  LEU A O   
443  C CB  . LEU A 63  ? 0.34193 0.36760 0.35279 0.09238  -0.08736 0.02763  70  LEU A CB  
444  C CG  . LEU A 63  ? 0.38617 0.37866 0.38898 0.09844  -0.06416 0.02459  70  LEU A CG  
445  C CD1 . LEU A 63  ? 0.39452 0.39405 0.41731 0.11676  -0.05279 0.03590  70  LEU A CD1 
446  C CD2 . LEU A 63  ? 0.37986 0.36056 0.38070 0.08158  -0.05899 0.00798  70  LEU A CD2 
447  N N   . ASP A 64  ? 0.35957 0.38558 0.30767 0.07150  -0.13388 0.01692  71  ASP A N   
448  C CA  . ASP A 64  ? 0.43085 0.47192 0.37105 0.05952  -0.16170 0.01438  71  ASP A CA  
449  C C   . ASP A 64  ? 0.40989 0.44044 0.34917 0.04082  -0.16626 -0.00354 71  ASP A C   
450  O O   . ASP A 64  ? 0.43875 0.48356 0.38536 0.02556  -0.18915 -0.00553 71  ASP A O   
451  C CB  . ASP A 64  ? 0.42158 0.44414 0.31286 0.06434  -0.17128 0.01497  71  ASP A CB  
452  C CG  . ASP A 64  ? 0.50727 0.54766 0.40121 0.08112  -0.17606 0.03662  71  ASP A CG  
453  O OD1 . ASP A 64  ? 0.56815 0.63685 0.50359 0.09006  -0.17291 0.05135  71  ASP A OD1 
454  O OD2 . ASP A 64  ? 0.56196 0.58712 0.41446 0.08803  -0.18125 0.04045  71  ASP A OD2 
455  N N   . SER A 65  ? 0.38765 0.39309 0.31796 0.04097  -0.14589 -0.01492 72  SER A N   
456  C CA  . SER A 65  ? 0.37838 0.36989 0.30723 0.02792  -0.14496 -0.03011 72  SER A CA  
457  C C   . SER A 65  ? 0.41143 0.42460 0.38493 0.02093  -0.14126 -0.02774 72  SER A C   
458  O O   . SER A 65  ? 0.44568 0.44762 0.42176 0.01173  -0.13726 -0.03789 72  SER A O   
459  C CB  . SER A 65  ? 0.38599 0.34937 0.29067 0.03416  -0.12378 -0.03841 72  SER A CB  
460  O OG  . SER A 65  ? 0.37302 0.34031 0.29385 0.04333  -0.10449 -0.02977 72  SER A OG  
461  N N   . GLY A 66  ? 0.35905 0.40235 0.36611 0.02780  -0.14037 -0.01292 73  GLY A N   
462  C CA  . GLY A 66  ? 0.36691 0.43254 0.41393 0.02438  -0.13403 -0.00825 73  GLY A CA  
463  C C   . GLY A 66  ? 0.36199 0.43641 0.42672 0.04281  -0.11498 0.00324  73  GLY A C   
464  O O   . GLY A 66  ? 0.31952 0.36686 0.36604 0.05055  -0.09771 -0.00186 73  GLY A O   
465  N N   . LYS A 67  ? 0.30258 0.41354 0.40241 0.04966  -0.11742 0.01956  74  LYS A N   
466  C CA  . LYS A 67  ? 0.31482 0.42888 0.42619 0.07198  -0.09757 0.03133  74  LYS A CA  
467  C C   . LYS A 67  ? 0.29562 0.40149 0.41694 0.07401  -0.07721 0.02656  74  LYS A C   
468  O O   . LYS A 67  ? 0.33007 0.41450 0.44065 0.09042  -0.05768 0.02792  74  LYS A O   
469  C CB  . LYS A 67  ? 0.28931 0.45040 0.43533 0.08376  -0.10622 0.05445  74  LYS A CB  
470  C CG  . LYS A 67  ? 0.45032 0.61761 0.58147 0.08804  -0.12459 0.06286  74  LYS A CG  
471  C CD  . LYS A 67  ? 0.48145 0.67849 0.63509 0.11415  -0.12050 0.08814  74  LYS A CD  
472  C CE  . LYS A 67  ? 0.58599 0.79800 0.72797 0.11433  -0.14494 0.09841  74  LYS A CE  
473  N NZ  . LYS A 67  ? 0.83395 1.05190 0.98294 0.13900  -0.13444 0.11636  74  LYS A NZ  
474  N N   . GLU A 68  ? 0.24010 0.35849 0.37743 0.05779  -0.08172 0.02148  75  GLU A N   
475  C CA  . GLU A 68  ? 0.25793 0.37344 0.40466 0.06098  -0.06311 0.02002  75  GLU A CA  
476  C C   . GLU A 68  ? 0.24545 0.31700 0.35828 0.05724  -0.05224 0.00255  75  GLU A C   
477  O O   . GLU A 68  ? 0.28392 0.33884 0.37896 0.04412  -0.06128 -0.00903 75  GLU A O   
478  C CB  . GLU A 68  ? 0.28177 0.42569 0.45761 0.04393  -0.07154 0.02337  75  GLU A CB  
479  C CG  . GLU A 68  ? 0.32430 0.52141 0.54428 0.04554  -0.08000 0.04538  75  GLU A CG  
480  C CD  . GLU A 68  ? 0.66003 0.87406 0.88342 0.03364  -0.10818 0.04936  75  GLU A CD  
481  O OE1 . GLU A 68  ? 0.54187 0.72491 0.73385 0.01839  -0.12200 0.03255  75  GLU A OE1 
482  O OE2 . GLU A 68  ? 0.55563 0.81341 0.81040 0.04133  -0.11611 0.07008  75  GLU A OE2 
483  N N   . LEU A 69  ? 0.25136 0.30461 0.35426 0.06932  -0.03300 0.00178  76  LEU A N   
484  C CA  . LEU A 69  ? 0.21938 0.23387 0.29169 0.06386  -0.02471 -0.01245 76  LEU A CA  
485  C C   . LEU A 69  ? 0.19481 0.21080 0.27104 0.06143  -0.01494 -0.01500 76  LEU A C   
486  O O   . LEU A 69  ? 0.24160 0.25457 0.31613 0.07658  0.00043  -0.00937 76  LEU A O   
487  C CB  . LEU A 69  ? 0.26425 0.24549 0.31100 0.07787  -0.01321 -0.01194 76  LEU A CB  
488  C CG  . LEU A 69  ? 0.32077 0.29655 0.35958 0.08215  -0.02048 -0.00693 76  LEU A CG  
489  C CD1 . LEU A 69  ? 0.45803 0.39009 0.46687 0.09256  -0.00772 -0.00712 76  LEU A CD1 
490  C CD2 . LEU A 69  ? 0.32224 0.29858 0.35416 0.06497  -0.03399 -0.01468 76  LEU A CD2 
491  N N   . HIS A 70  ? 0.21857 0.23667 0.29644 0.04495  -0.02221 -0.02251 77  HIS A N   
492  C CA  . HIS A 70  ? 0.21334 0.23701 0.29672 0.04260  -0.01418 -0.02189 77  HIS A CA  
493  C C   . HIS A 70  ? 0.19806 0.20880 0.26953 0.02779  -0.01986 -0.03203 77  HIS A C   
494  O O   . HIS A 70  ? 0.20398 0.20652 0.26783 0.01998  -0.02946 -0.03840 77  HIS A O   
495  C CB  . HIS A 70  ? 0.21202 0.27466 0.33205 0.04130  -0.01686 -0.00842 77  HIS A CB  
496  C CG  . HIS A 70  ? 0.17235 0.24777 0.30669 0.02411  -0.03653 -0.00952 77  HIS A CG  
497  N ND1 . HIS A 70  ? 0.29844 0.40125 0.45639 0.02157  -0.04938 0.00037  77  HIS A ND1 
498  C CD2 . HIS A 70  ? 0.19196 0.25289 0.31633 0.00943  -0.04574 -0.01916 77  HIS A CD2 
499  C CE1 . HIS A 70  ? 0.24521 0.34375 0.40146 0.00397  -0.06685 -0.00562 77  HIS A CE1 
500  N NE2 . HIS A 70  ? 0.24582 0.31743 0.38139 -0.00171 -0.06319 -0.01744 77  HIS A NE2 
501  N N   . ILE A 71  ? 0.18486 0.19527 0.25410 0.02652  -0.01217 -0.03145 78  ILE A N   
502  C CA  . ILE A 71  ? 0.18096 0.18335 0.24148 0.01540  -0.01634 -0.03726 78  ILE A CA  
503  C C   . ILE A 71  ? 0.19852 0.21895 0.27838 0.01108  -0.01472 -0.02918 78  ILE A C   
504  O O   . ILE A 71  ? 0.19971 0.23097 0.28617 0.01881  -0.00293 -0.02072 78  ILE A O   
505  C CB  . ILE A 71  ? 0.22054 0.19934 0.25118 0.01660  -0.00985 -0.04353 78  ILE A CB  
506  C CG1 . ILE A 71  ? 0.24073 0.19845 0.25280 0.01682  -0.01211 -0.04980 78  ILE A CG1 
507  C CG2 . ILE A 71  ? 0.22433 0.20326 0.25100 0.00654  -0.01536 -0.04547 78  ILE A CG2 
508  C CD1 . ILE A 71  ? 0.28141 0.20988 0.26012 0.01514  -0.00807 -0.05604 78  ILE A CD1 
509  N N   . ASN A 72  ? 0.19604 0.21719 0.28316 -0.00006 -0.02475 -0.03046 79  ASN A N   
510  C CA  . ASN A 72  ? 0.16357 0.19494 0.26646 -0.00704 -0.02389 -0.02197 79  ASN A CA  
511  C C   . ASN A 72  ? 0.21062 0.22641 0.29733 -0.01017 -0.02368 -0.02518 79  ASN A C   
512  O O   . ASN A 72  ? 0.20925 0.21206 0.28279 -0.01074 -0.02964 -0.03296 79  ASN A O   
513  C CB  . ASN A 72  ? 0.16895 0.20826 0.29207 -0.01870 -0.03713 -0.01882 79  ASN A CB  
514  C CG  . ASN A 72  ? 0.19395 0.25706 0.33826 -0.01682 -0.04040 -0.01171 79  ASN A CG  
515  O OD1 . ASN A 72  ? 0.19362 0.27449 0.34790 -0.00570 -0.02817 -0.00311 79  ASN A OD1 
516  N ND2 . ASN A 72  ? 0.20703 0.27018 0.35633 -0.02641 -0.05708 -0.01417 79  ASN A ND2 
517  N N   . LEU A 73  ? 0.18614 0.20613 0.27452 -0.01052 -0.01566 -0.01665 80  LEU A N   
518  C CA  . LEU A 73  ? 0.17697 0.18522 0.25200 -0.01240 -0.01607 -0.01586 80  LEU A CA  
519  C C   . LEU A 73  ? 0.20032 0.20888 0.29231 -0.02136 -0.01805 -0.00632 80  LEU A C   
520  O O   . LEU A 73  ? 0.19612 0.22008 0.30562 -0.02455 -0.01132 0.00526  80  LEU A O   
521  C CB  . LEU A 73  ? 0.22186 0.22909 0.27682 -0.00565 -0.00564 -0.01286 80  LEU A CB  
522  C CG  . LEU A 73  ? 0.21561 0.21460 0.24884 0.00073  -0.00346 -0.02223 80  LEU A CG  
523  C CD1 . LEU A 73  ? 0.23136 0.22158 0.23596 0.00649  0.00598  -0.02029 80  LEU A CD1 
524  C CD2 . LEU A 73  ? 0.22942 0.21968 0.25389 -0.00350 -0.01516 -0.03168 80  LEU A CD2 
525  N N   . ILE A 74  ? 0.19677 0.18715 0.28370 -0.02522 -0.02636 -0.00981 81  ILE A N   
526  C CA  . ILE A 74  ? 0.23444 0.21296 0.33171 -0.03613 -0.03067 -0.00293 81  ILE A CA  
527  C C   . ILE A 74  ? 0.22659 0.18577 0.30905 -0.03194 -0.02798 0.00154  81  ILE A C   
528  O O   . ILE A 74  ? 0.25517 0.19593 0.32343 -0.02555 -0.03209 -0.00500 81  ILE A O   
529  C CB  . ILE A 74  ? 0.23141 0.19437 0.32901 -0.04380 -0.04398 -0.01197 81  ILE A CB  
530  C CG1 . ILE A 74  ? 0.24544 0.23101 0.35538 -0.04417 -0.04750 -0.01544 81  ILE A CG1 
531  C CG2 . ILE A 74  ? 0.22934 0.17426 0.33473 -0.06014 -0.05096 -0.00510 81  ILE A CG2 
532  C CD1 . ILE A 74  ? 0.24316 0.21446 0.34729 -0.05110 -0.06280 -0.02504 81  ILE A CD1 
533  N N   . PRO A 75  ? 0.24258 0.20637 0.32846 -0.03370 -0.01975 0.01514  82  PRO A N   
534  C CA  . PRO A 75  ? 0.25404 0.19792 0.32708 -0.02980 -0.01763 0.02307  82  PRO A CA  
535  C C   . PRO A 75  ? 0.28669 0.20129 0.36452 -0.04168 -0.02280 0.02734  82  PRO A C   
536  O O   . PRO A 75  ? 0.31748 0.23646 0.41426 -0.05782 -0.02613 0.03154  82  PRO A O   
537  C CB  . PRO A 75  ? 0.26161 0.22212 0.33320 -0.02746 -0.00590 0.03707  82  PRO A CB  
538  C CG  . PRO A 75  ? 0.28945 0.27285 0.38318 -0.03551 -0.00054 0.04139  82  PRO A CG  
539  C CD  . PRO A 75  ? 0.26606 0.25430 0.36864 -0.03782 -0.01030 0.02654  82  PRO A CD  
540  N N   . ASN A 76  ? 0.31263 0.19627 0.37262 -0.03374 -0.02384 0.02768  83  ASN A N   
541  C CA  . ASN A 76  ? 0.34440 0.18561 0.39831 -0.04349 -0.02798 0.03114  83  ASN A CA  
542  C C   . ASN A 76  ? 0.37788 0.19704 0.41602 -0.03077 -0.02052 0.04366  83  ASN A C   
543  O O   . ASN A 76  ? 0.41517 0.22282 0.43686 -0.01182 -0.01931 0.03986  83  ASN A O   
544  C CB  . ASN A 76  ? 0.38859 0.19815 0.42686 -0.04330 -0.03788 0.01424  83  ASN A CB  
545  C CG  . ASN A 76  ? 0.45799 0.21452 0.48353 -0.05848 -0.04496 0.01513  83  ASN A CG  
546  O OD1 . ASN A 76  ? 0.52866 0.25154 0.53998 -0.05317 -0.03936 0.02451  83  ASN A OD1 
547  N ND2 . ASN A 76  ? 0.56976 0.31662 0.59838 -0.07839 -0.05864 0.00618  83  ASN A ND2 
548  N N   . LYS A 77  ? 0.39953 0.21439 0.44403 -0.04003 -0.01477 0.06110  84  LYS A N   
549  C CA  . LYS A 77  ? 0.45165 0.24807 0.48065 -0.02672 -0.00713 0.07639  84  LYS A CA  
550  C C   . LYS A 77  ? 0.50095 0.23793 0.50908 -0.02224 -0.00932 0.07556  84  LYS A C   
551  O O   . LYS A 77  ? 0.56494 0.28598 0.55683 -0.00200 -0.00342 0.08495  84  LYS A O   
552  C CB  . LYS A 77  ? 0.45659 0.26413 0.49605 -0.03774 0.00164  0.09744  84  LYS A CB  
553  C CG  . LYS A 77  ? 0.45911 0.31776 0.50616 -0.03329 0.00853  0.10036  84  LYS A CG  
554  C CD  . LYS A 77  ? 0.45892 0.32680 0.50999 -0.03907 0.02111  0.12353  84  LYS A CD  
555  C CE  . LYS A 77  ? 0.49988 0.41000 0.54853 -0.03157 0.02992  0.12450  84  LYS A CE  
556  N NZ  . LYS A 77  ? 0.57951 0.51491 0.65158 -0.04131 0.02883  0.11370  84  LYS A NZ  
557  N N   . GLN A 78  ? 0.55768 0.25901 0.56286 -0.04008 -0.01817 0.06521  85  GLN A N   
558  C CA  . GLN A 78  ? 0.62730 0.25901 0.60208 -0.03535 -0.01991 0.06168  85  GLN A CA  
559  C C   . GLN A 78  ? 0.58444 0.20655 0.53751 -0.00644 -0.01735 0.04832  85  GLN A C   
560  O O   . GLN A 78  ? 0.68825 0.26926 0.61648 0.01511  -0.00992 0.05339  85  GLN A O   
561  C CB  . GLN A 78  ? 0.67453 0.26884 0.64601 -0.06512 -0.03294 0.05207  85  GLN A CB  
562  C CG  . GLN A 78  ? 0.89471 0.49228 0.88611 -0.09269 -0.03205 0.06826  85  GLN A CG  
563  C CD  . GLN A 78  ? 1.01424 0.67287 1.04377 -0.10168 -0.02819 0.08623  85  GLN A CD  
564  O OE1 . GLN A 78  ? 0.96555 0.63454 0.99986 -0.09624 -0.01578 0.10663  85  GLN A OE1 
565  N NE2 . GLN A 78  ? 0.94472 0.65208 0.99821 -0.10950 -0.03418 0.07694  85  GLN A NE2 
566  N N   . ASP A 79  ? 0.51018 0.17056 0.47324 -0.00418 -0.02171 0.03377  86  ASP A N   
567  C CA  . ASP A 79  ? 0.56063 0.22328 0.50944 0.02133  -0.01804 0.02336  86  ASP A CA  
568  C C   . ASP A 79  ? 0.48575 0.20204 0.45024 0.04141  -0.01093 0.03432  86  ASP A C   
569  O O   . ASP A 79  ? 0.48563 0.20998 0.44394 0.06413  -0.00612 0.03223  86  ASP A O   
570  C CB  . ASP A 79  ? 0.58782 0.26463 0.53875 0.01201  -0.02681 0.00401  86  ASP A CB  
571  C CG  . ASP A 79  ? 0.71008 0.33570 0.64193 -0.00943 -0.03853 -0.00826 86  ASP A CG  
572  O OD1 . ASP A 79  ? 0.76180 0.34440 0.67665 -0.01265 -0.03583 -0.00516 86  ASP A OD1 
573  O OD2 . ASP A 79  ? 0.65378 0.29744 0.59281 -0.02343 -0.04891 -0.02023 86  ASP A OD2 
574  N N   . ARG A 80  ? 0.43190 0.18383 0.41461 0.03292  -0.01043 0.04703  87  ARG A N   
575  C CA  . ARG A 80  ? 0.38643 0.19097 0.38095 0.04443  -0.00878 0.05549  87  ARG A CA  
576  C C   . ARG A 80  ? 0.35393 0.19416 0.35765 0.04645  -0.01309 0.04191  87  ARG A C   
577  O O   . ARG A 80  ? 0.38574 0.25099 0.39233 0.06302  -0.01216 0.04598  87  ARG A O   
578  C CB  . ARG A 80  ? 0.42608 0.22682 0.41204 0.06925  -0.00287 0.07253  87  ARG A CB  
579  C CG  . ARG A 80  ? 0.43164 0.28061 0.42655 0.07105  -0.00525 0.08587  87  ARG A CG  
580  C CD  . ARG A 80  ? 0.55559 0.42365 0.55028 0.09584  -0.00428 0.10194  87  ARG A CD  
581  N NE  . ARG A 80  ? 0.64354 0.47015 0.62446 0.11250  0.00395  0.11735  87  ARG A NE  
582  C CZ  . ARG A 80  ? 0.76737 0.59199 0.74614 0.14095  0.00928  0.12999  87  ARG A CZ  
583  N NH1 . ARG A 80  ? 0.60061 0.46824 0.59475 0.15464  0.00710  0.13055  87  ARG A NH1 
584  N NH2 . ARG A 80  ? 0.68397 0.46389 0.64626 0.15676  0.01794  0.14502  87  ARG A NH2 
585  N N   . THR A 81  ? 0.33613 0.18143 0.34693 0.02899  -0.01806 0.02831  88  THR A N   
586  C CA  . THR A 81  ? 0.29774 0.17105 0.31541 0.02900  -0.02174 0.01600  88  THR A CA  
587  C C   . THR A 81  ? 0.29306 0.19511 0.32328 0.01340  -0.02462 0.01274  88  THR A C   
588  O O   . THR A 81  ? 0.30097 0.19714 0.33726 -0.00003 -0.02421 0.01541  88  THR A O   
589  C CB  . THR A 81  ? 0.34313 0.18983 0.35080 0.02867  -0.02429 0.00087  88  THR A CB  
590  O OG1 . THR A 81  ? 0.37950 0.20198 0.38650 0.00913  -0.03024 -0.00455 88  THR A OG1 
591  C CG2 . THR A 81  ? 0.40120 0.21535 0.38946 0.04978  -0.01778 0.00279  88  THR A CG2 
592  N N   . LEU A 82  ? 0.24675 0.17916 0.28080 0.01563  -0.02670 0.00824  89  LEU A N   
593  C CA  . LEU A 82  ? 0.24717 0.19872 0.28699 0.00497  -0.02809 0.00173  89  LEU A CA  
594  C C   . LEU A 82  ? 0.25305 0.20902 0.29500 0.00519  -0.03170 -0.01061 89  LEU A C   
595  O O   . LEU A 82  ? 0.24258 0.20830 0.28288 0.01326  -0.03266 -0.01094 89  LEU A O   
596  C CB  . LEU A 82  ? 0.24218 0.21590 0.27537 0.00575  -0.02792 0.00709  89  LEU A CB  
597  C CG  . LEU A 82  ? 0.22422 0.20854 0.25518 -0.00132 -0.02694 -0.00079 89  LEU A CG  
598  C CD1 . LEU A 82  ? 0.24642 0.22686 0.28518 -0.00696 -0.01963 0.00293  89  LEU A CD1 
599  C CD2 . LEU A 82  ? 0.25354 0.24892 0.26635 -0.00076 -0.02917 0.00215  89  LEU A CD2 
600  N N   . THR A 83  ? 0.23239 0.18395 0.27983 -0.00335 -0.03365 -0.01802 90  THR A N   
601  C CA  . THR A 83  ? 0.23901 0.19181 0.28557 -0.00278 -0.03722 -0.02844 90  THR A CA  
602  C C   . THR A 83  ? 0.25348 0.22444 0.30538 -0.00747 -0.03688 -0.03167 90  THR A C   
603  O O   . THR A 83  ? 0.23713 0.21398 0.29713 -0.01289 -0.03457 -0.02839 90  THR A O   
604  C CB  . THR A 83  ? 0.26995 0.19942 0.31328 -0.00764 -0.04246 -0.03438 90  THR A CB  
605  O OG1 . THR A 83  ? 0.30254 0.20357 0.33301 -0.00163 -0.04126 -0.03247 90  THR A OG1 
606  C CG2 . THR A 83  ? 0.27122 0.20170 0.30824 -0.00489 -0.04588 -0.04400 90  THR A CG2 
607  N N   . ILE A 84  ? 0.21504 0.19416 0.26241 -0.00439 -0.03763 -0.03618 91  ILE A N   
608  C CA  . ILE A 84  ? 0.20198 0.18862 0.24827 -0.00702 -0.03675 -0.04001 91  ILE A CA  
609  C C   . ILE A 84  ? 0.23393 0.21676 0.28171 -0.00621 -0.03997 -0.04593 91  ILE A C   
610  O O   . ILE A 84  ? 0.23114 0.21176 0.27373 -0.00244 -0.04098 -0.04791 91  ILE A O   
611  C CB  . ILE A 84  ? 0.21777 0.21064 0.25407 -0.00808 -0.03724 -0.03982 91  ILE A CB  
612  C CG1 . ILE A 84  ? 0.26088 0.25682 0.28891 -0.00935 -0.03676 -0.03397 91  ILE A CG1 
613  C CG2 . ILE A 84  ? 0.23048 0.21868 0.25944 -0.01002 -0.03571 -0.04525 91  ILE A CG2 
614  C CD1 . ILE A 84  ? 0.34661 0.34833 0.37928 -0.00543 -0.03889 -0.02595 91  ILE A CD1 
615  N N   . VAL A 85  ? 0.19756 0.18243 0.25287 -0.00855 -0.04122 -0.04654 92  VAL A N   
616  C CA  . VAL A 85  ? 0.20644 0.18876 0.26145 -0.00823 -0.04694 -0.05060 92  VAL A CA  
617  C C   . VAL A 85  ? 0.23967 0.22860 0.29464 -0.00473 -0.04391 -0.05047 92  VAL A C   
618  O O   . VAL A 85  ? 0.23119 0.22704 0.29214 -0.00298 -0.03826 -0.04651 92  VAL A O   
619  C CB  . VAL A 85  ? 0.21792 0.20039 0.28375 -0.01524 -0.05472 -0.04876 92  VAL A CB  
620  C CG1 . VAL A 85  ? 0.26563 0.24474 0.32497 -0.01527 -0.06394 -0.05321 92  VAL A CG1 
621  C CG2 . VAL A 85  ? 0.27736 0.24378 0.33979 -0.02019 -0.05720 -0.04832 92  VAL A CG2 
622  N N   . ASP A 86  ? 0.24737 0.23168 0.29340 -0.00173 -0.04596 -0.05355 93  ASP A N   
623  C CA  . ASP A 86  ? 0.20365 0.18913 0.24840 0.00276  -0.04346 -0.05193 93  ASP A CA  
624  C C   . ASP A 86  ? 0.23149 0.21630 0.27230 0.00527  -0.05033 -0.05234 93  ASP A C   
625  O O   . ASP A 86  ? 0.24659 0.22506 0.27835 0.00396  -0.05537 -0.05596 93  ASP A O   
626  C CB  . ASP A 86  ? 0.22573 0.20087 0.25721 0.00274  -0.03745 -0.05313 93  ASP A CB  
627  C CG  . ASP A 86  ? 0.28054 0.25321 0.30480 0.00026  -0.03885 -0.05372 93  ASP A CG  
628  O OD1 . ASP A 86  ? 0.25985 0.23012 0.27920 0.00368  -0.04001 -0.05290 93  ASP A OD1 
629  O OD2 . ASP A 86  ? 0.24882 0.22485 0.27282 -0.00437 -0.03814 -0.05281 93  ASP A OD2 
630  N N   . THR A 87  ? 0.21412 0.20368 0.25852 0.01110  -0.04989 -0.04781 94  THR A N   
631  C CA  . THR A 87  ? 0.21532 0.20523 0.25327 0.01489  -0.05702 -0.04598 94  THR A CA  
632  C C   . THR A 87  ? 0.25148 0.22787 0.27440 0.02083  -0.04975 -0.04422 94  THR A C   
633  O O   . THR A 87  ? 0.25448 0.23068 0.27387 0.02837  -0.05114 -0.03849 94  THR A O   
634  C CB  . THR A 87  ? 0.20614 0.21625 0.26275 0.01756  -0.06405 -0.03799 94  THR A CB  
635  O OG1 . THR A 87  ? 0.22695 0.24343 0.29498 0.02614  -0.05253 -0.03154 94  THR A OG1 
636  C CG2 . THR A 87  ? 0.22911 0.25055 0.30008 0.00597  -0.07456 -0.03852 94  THR A CG2 
637  N N   . GLY A 88  ? 0.23495 0.20062 0.24932 0.01628  -0.04327 -0.04726 95  GLY A N   
638  C CA  . GLY A 88  ? 0.24912 0.20047 0.25057 0.01640  -0.03748 -0.04431 95  GLY A CA  
639  C C   . GLY A 88  ? 0.25116 0.20263 0.24198 0.01828  -0.03887 -0.04167 95  GLY A C   
640  O O   . GLY A 88  ? 0.26984 0.22693 0.25671 0.02216  -0.04550 -0.04325 95  GLY A O   
641  N N   . ILE A 89  ? 0.26041 0.20336 0.24366 0.01433  -0.03250 -0.03688 96  ILE A N   
642  C CA  . ILE A 89  ? 0.26379 0.20640 0.23473 0.01839  -0.02977 -0.03075 96  ILE A CA  
643  C C   . ILE A 89  ? 0.30468 0.25848 0.27315 0.02072  -0.02845 -0.03295 96  ILE A C   
644  O O   . ILE A 89  ? 0.28926 0.24090 0.24080 0.02861  -0.02632 -0.03016 96  ILE A O   
645  C CB  . ILE A 89  ? 0.27792 0.20935 0.24490 0.01102  -0.02229 -0.02172 96  ILE A CB  
646  C CG1 . ILE A 89  ? 0.32465 0.25364 0.27687 0.01762  -0.01738 -0.01187 96  ILE A CG1 
647  C CG2 . ILE A 89  ? 0.27984 0.22220 0.25949 -0.00261 -0.01956 -0.01989 96  ILE A CG2 
648  C CD1 . ILE A 89  ? 0.39958 0.31012 0.34562 0.01131  -0.01161 -0.00136 96  ILE A CD1 
649  N N   . GLY A 90  ? 0.28099 0.24362 0.26153 0.01659  -0.02852 -0.03728 97  GLY A N   
650  C CA  . GLY A 90  ? 0.28158 0.24996 0.25694 0.02309  -0.02454 -0.03803 97  GLY A CA  
651  C C   . GLY A 90  ? 0.27374 0.25482 0.25240 0.02366  -0.01291 -0.02629 97  GLY A C   
652  O O   . GLY A 90  ? 0.30271 0.28839 0.29083 0.01366  -0.01051 -0.01793 97  GLY A O   
653  N N   . MET A 91  ? 0.25350 0.23995 0.22525 0.03507  -0.00515 -0.02464 98  MET A N   
654  C CA  . MET A 91  ? 0.27191 0.27893 0.25125 0.03942  0.00912  -0.00966 98  MET A CA  
655  C C   . MET A 91  ? 0.27778 0.27520 0.22843 0.05949  0.02017  -0.00926 98  MET A C   
656  O O   . MET A 91  ? 0.31286 0.28855 0.24063 0.06982  0.01666  -0.02179 98  MET A O   
657  C CB  . MET A 91  ? 0.26860 0.30276 0.27575 0.03675  0.01270  -0.00168 98  MET A CB  
658  C CG  . MET A 91  ? 0.27924 0.31977 0.30715 0.01700  0.00095  -0.00290 98  MET A CG  
659  S SD  . MET A 91  ? 0.27841 0.34913 0.33390 0.01427  -0.00068 0.00482  98  MET A SD  
660  C CE  . MET A 91  ? 0.28369 0.32719 0.32380 0.02141  -0.00826 -0.01327 98  MET A CE  
661  N N   . THR A 92  ? 0.27494 0.28556 0.22388 0.06415  0.03391  0.00581  99  THR A N   
662  C CA  . THR A 92  ? 0.30779 0.31242 0.22736 0.08684  0.05009  0.00968  99  THR A CA  
663  C C   . THR A 92  ? 0.31556 0.34012 0.24891 0.10118  0.06423  0.01716  99  THR A C   
664  O O   . THR A 92  ? 0.29853 0.34961 0.26920 0.09120  0.06101  0.02354  99  THR A O   
665  C CB  . THR A 92  ? 0.39293 0.40975 0.30876 0.08851  0.06365  0.02750  99  THR A CB  
666  O OG1 . THR A 92  ? 0.32587 0.38294 0.28558 0.07668  0.07183  0.04783  99  THR A OG1 
667  C CG2 . THR A 92  ? 0.42144 0.41838 0.32485 0.07646  0.05071  0.02350  99  THR A CG2 
668  N N   . LYS A 93  ? 0.32425 0.29014 0.21914 0.07584  -0.00857 0.00398  100 LYS A N   
669  C CA  . LYS A 93  ? 0.31668 0.27046 0.20876 0.06779  0.00978  -0.00211 100 LYS A CA  
670  C C   . LYS A 93  ? 0.32915 0.27035 0.22782 0.06943  0.02174  0.01103  100 LYS A C   
671  O O   . LYS A 93  ? 0.32189 0.26244 0.24019 0.06800  0.03156  0.00738  100 LYS A O   
672  C CB  . LYS A 93  ? 0.36884 0.32181 0.22703 0.06241  0.01453  -0.00988 100 LYS A CB  
673  C CG  . LYS A 93  ? 0.38916 0.32880 0.24654 0.05989  0.03407  -0.01932 100 LYS A CG  
674  C CD  . LYS A 93  ? 0.41855 0.35517 0.24002 0.05588  0.04255  -0.02930 100 LYS A CD  
675  C CE  . LYS A 93  ? 0.45709 0.37722 0.28179 0.05836  0.06023  -0.04379 100 LYS A CE  
676  N NZ  . LYS A 93  ? 0.51951 0.43698 0.31309 0.05791  0.07432  -0.05431 100 LYS A NZ  
677  N N   . ALA A 94  ? 0.35800 0.28952 0.23946 0.07136  0.02002  0.02694  101 ALA A N   
678  C CA  . ALA A 94  ? 0.37298 0.29366 0.25969 0.06622  0.03283  0.03785  101 ALA A CA  
679  C C   . ALA A 94  ? 0.35184 0.27175 0.27237 0.06673  0.03119  0.03612  101 ALA A C   
680  O O   . ALA A 94  ? 0.38082 0.30768 0.31843 0.06033  0.04253  0.03410  101 ALA A O   
681  C CB  . ALA A 94  ? 0.41729 0.31699 0.27255 0.06476  0.03134  0.05688  101 ALA A CB  
682  N N   . ASP A 95  ? 0.35600 0.27357 0.28712 0.07490  0.01700  0.03485  102 ASP A N   
683  C CA  . ASP A 95  ? 0.34355 0.26242 0.30421 0.07489  0.01632  0.02931  102 ASP A CA  
684  C C   . ASP A 95  ? 0.29294 0.22978 0.27197 0.06960  0.02232  0.01734  102 ASP A C   
685  O O   . ASP A 95  ? 0.31260 0.25318 0.30803 0.06434  0.02841  0.01587  102 ASP A O   
686  C CB  . ASP A 95  ? 0.34328 0.26615 0.31489 0.08711  0.00156  0.02488  102 ASP A CB  
687  C CG  . ASP A 95  ? 0.49656 0.39435 0.45242 0.09946  -0.00702 0.03861  102 ASP A CG  
688  O OD1 . ASP A 95  ? 0.53590 0.40236 0.47898 0.09379  0.00112  0.05053  102 ASP A OD1 
689  O OD2 . ASP A 95  ? 0.53553 0.44538 0.49284 0.11525  -0.02242 0.03691  102 ASP A OD2 
690  N N   . LEU A 96  ? 0.29029 0.23637 0.26401 0.07012  0.01995  0.00854  103 LEU A N   
691  C CA  . LEU A 96  ? 0.30790 0.25861 0.29132 0.06625  0.02572  0.00016  103 LEU A CA  
692  C C   . LEU A 96  ? 0.32831 0.27918 0.31365 0.06686  0.03697  0.00446  103 LEU A C   
693  O O   . LEU A 96  ? 0.29291 0.25003 0.29288 0.06668  0.03918  0.00389  103 LEU A O   
694  C CB  . LEU A 96  ? 0.34673 0.29537 0.31576 0.06323  0.02508  -0.00992 103 LEU A CB  
695  C CG  . LEU A 96  ? 0.32273 0.28360 0.29773 0.05767  0.01587  -0.02003 103 LEU A CG  
696  C CD1 . LEU A 96  ? 0.31130 0.26673 0.26696 0.04859  0.01768  -0.03202 103 LEU A CD1 
697  C CD2 . LEU A 96  ? 0.26723 0.23451 0.26297 0.05272  0.01701  -0.02366 103 LEU A CD2 
698  N N   . ILE A 97  ? 0.28957 0.23909 0.25948 0.06816  0.04413  0.00762  104 ILE A N   
699  C CA  . ILE A 97  ? 0.30971 0.27068 0.28634 0.07055  0.05615  0.00869  104 ILE A CA  
700  C C   . ILE A 97  ? 0.29749 0.27210 0.29371 0.06381  0.05782  0.01476  104 ILE A C   
701  O O   . ILE A 97  ? 0.30373 0.29854 0.31853 0.06605  0.06142  0.01300  104 ILE A O   
702  C CB  . ILE A 97  ? 0.34513 0.30676 0.30017 0.07079  0.06606  0.00846  104 ILE A CB  
703  C CG1 . ILE A 97  ? 0.36597 0.31386 0.30180 0.07565  0.06566  -0.00271 104 ILE A CG1 
704  C CG2 . ILE A 97  ? 0.34979 0.33578 0.31829 0.07284  0.08071  0.00809  104 ILE A CG2 
705  C CD1 . ILE A 97  ? 0.37225 0.31921 0.27807 0.07329  0.07304  -0.00548 104 ILE A CD1 
706  N N   . ASN A 98  ? 0.28893 0.25144 0.27990 0.05607  0.05423  0.02126  105 ASN A N   
707  C CA  . ASN A 98  ? 0.31148 0.27698 0.31530 0.04459  0.05739  0.02479  105 ASN A CA  
708  C C   . ASN A 98  ? 0.27944 0.24598 0.30128 0.04460  0.04892  0.01857  105 ASN A C   
709  O O   . ASN A 98  ? 0.28551 0.23418 0.30760 0.04098  0.04474  0.01873  105 ASN A O   
710  C CB  . ASN A 98  ? 0.36187 0.29962 0.34408 0.03724  0.05872  0.03550  105 ASN A CB  
711  C CG  . ASN A 98  ? 0.58596 0.51920 0.57388 0.01868  0.06761  0.03867  105 ASN A CG  
712  O OD1 . ASN A 98  ? 0.47109 0.43432 0.48256 0.00966  0.07292  0.03109  105 ASN A OD1 
713  N ND2 . ASN A 98  ? 0.56887 0.46312 0.53273 0.01212  0.06871  0.05009  105 ASN A ND2 
714  N N   . ASN A 99  ? 0.27849 0.26340 0.31202 0.05018  0.04715  0.01297  106 ASN A N   
715  C CA  . ASN A 99  ? 0.24607 0.23706 0.29180 0.04820  0.04088  0.00720  106 ASN A CA  
716  C C   . ASN A 99  ? 0.25606 0.23010 0.29879 0.04941  0.03413  0.00272  106 ASN A C   
717  O O   . ASN A 99  ? 0.24868 0.22198 0.30003 0.04430  0.03213  -0.00321 106 ASN A O   
718  C CB  . ASN A 99  ? 0.22392 0.23229 0.28409 0.03563  0.04332  0.00477  106 ASN A CB  
719  C CG  . ASN A 99  ? 0.20902 0.25075 0.28009 0.03587  0.04877  0.00660  106 ASN A CG  
720  O OD1 . ASN A 99  ? 0.24947 0.30509 0.32264 0.04986  0.04660  0.00775  106 ASN A OD1 
721  N ND2 . ASN A 99  ? 0.26497 0.31967 0.34298 0.02062  0.05666  0.00639  106 ASN A ND2 
722  N N   . LEU A 100 ? 0.24223 0.20775 0.27419 0.05630  0.03084  0.00257  107 LEU A N   
723  C CA  . LEU A 100 ? 0.27220 0.23576 0.30699 0.05905  0.02372  -0.00417 107 LEU A CA  
724  C C   . LEU A 100 ? 0.26186 0.21365 0.30175 0.06216  0.02060  -0.00386 107 LEU A C   
725  O O   . LEU A 100 ? 0.25362 0.20951 0.30564 0.06471  0.01755  -0.01312 107 LEU A O   
726  C CB  . LEU A 100 ? 0.22511 0.20081 0.26739 0.05385  0.02382  -0.01270 107 LEU A CB  
727  C CG  . LEU A 100 ? 0.28467 0.25646 0.31441 0.05290  0.02717  -0.01031 107 LEU A CG  
728  C CD1 . LEU A 100 ? 0.25895 0.23517 0.28972 0.05352  0.03037  -0.00466 107 LEU A CD1 
729  C CD2 . LEU A 100 ? 0.36639 0.33787 0.39056 0.04593  0.02685  -0.01794 107 LEU A CD2 
730  N N   . GLY A 101 ? 0.26252 0.19574 0.28999 0.06254  0.02272  0.00674  108 GLY A N   
731  C CA  . GLY A 101 ? 0.28869 0.19542 0.31187 0.06744  0.02006  0.01070  108 GLY A CA  
732  C C   . GLY A 101 ? 0.32360 0.21811 0.35668 0.05782  0.02591  0.00441  108 GLY A C   
733  O O   . GLY A 101 ? 0.40483 0.26973 0.43490 0.06455  0.02402  0.00388  108 GLY A O   
734  N N   . THR A 102 ? 0.29823 0.21342 0.34106 0.04318  0.03243  -0.00080 109 THR A N   
735  C CA  . THR A 102 ? 0.30297 0.21634 0.35498 0.02973  0.03709  -0.01096 109 THR A CA  
736  C C   . THR A 102 ? 0.29044 0.20398 0.33902 0.01061  0.04595  -0.00601 109 THR A C   
737  O O   . THR A 102 ? 0.33133 0.25710 0.37481 0.00916  0.04957  0.00394  109 THR A O   
738  C CB  . THR A 102 ? 0.28775 0.23506 0.35293 0.02603  0.03532  -0.02230 109 THR A CB  
739  O OG1 . THR A 102 ? 0.29376 0.26878 0.36057 0.02207  0.03630  -0.01608 109 THR A OG1 
740  C CG2 . THR A 102 ? 0.39383 0.34871 0.46247 0.03906  0.02980  -0.02786 109 THR A CG2 
741  N N   . ILE A 103 ? 0.27640 0.17995 0.32850 -0.00615 0.05087  -0.01598 110 ILE A N   
742  C CA  . ILE A 103 ? 0.28942 0.20468 0.34312 -0.03100 0.06013  -0.01585 110 ILE A CA  
743  C C   . ILE A 103 ? 0.29602 0.26709 0.36956 -0.03855 0.05681  -0.02637 110 ILE A C   
744  O O   . ILE A 103 ? 0.28640 0.27068 0.36688 -0.05907 0.05902  -0.03970 110 ILE A O   
745  C CB  . ILE A 103 ? 0.38113 0.24777 0.42206 -0.05013 0.06860  -0.02066 110 ILE A CB  
746  C CG1 . ILE A 103 ? 0.38979 0.23906 0.43469 -0.04839 0.06582  -0.03892 110 ILE A CG1 
747  C CG2 . ILE A 103 ? 0.43305 0.24187 0.44728 -0.04063 0.07106  -0.00321 110 ILE A CG2 
748  C CD1 . ILE A 103 ? 0.50652 0.30719 0.53846 -0.07323 0.07665  -0.04881 110 ILE A CD1 
749  N N   . ALA A 104 ? 0.25669 0.25899 0.33620 -0.02189 0.05098  -0.01998 111 ALA A N   
750  C CA  . ALA A 104 ? 0.22091 0.26664 0.31232 -0.02052 0.04411  -0.02597 111 ALA A CA  
751  C C   . ALA A 104 ? 0.21508 0.30774 0.32215 -0.03697 0.04594  -0.03020 111 ALA A C   
752  O O   . ALA A 104 ? 0.24013 0.36627 0.35443 -0.04266 0.03890  -0.03869 111 ALA A O   
753  C CB  . ALA A 104 ? 0.24319 0.29761 0.33148 0.00201  0.03858  -0.01654 111 ALA A CB  
754  N N   . LYS A 105 ? 0.20479 0.30696 0.31708 -0.04640 0.05520  -0.02561 112 LYS A N   
755  C CA  . LYS A 105 ? 0.20153 0.36136 0.33504 -0.06465 0.05760  -0.03303 112 LYS A CA  
756  C C   . LYS A 105 ? 0.28028 0.43839 0.41471 -0.09547 0.05903  -0.04945 112 LYS A C   
757  O O   . LYS A 105 ? 0.25292 0.46119 0.40125 -0.10397 0.05080  -0.06042 112 LYS A O   
758  C CB  . LYS A 105 ? 0.21967 0.39261 0.35841 -0.07376 0.07149  -0.02736 112 LYS A CB  
759  C CG  . LYS A 105 ? 0.31703 0.56182 0.48396 -0.09485 0.07558  -0.03781 112 LYS A CG  
760  C CD  . LYS A 105 ? 0.30078 0.57621 0.47786 -0.09616 0.09022  -0.03282 112 LYS A CD  
761  C CE  . LYS A 105 ? 0.50882 0.85088 0.71222 -0.12329 0.09585  -0.04536 112 LYS A CE  
762  N NZ  . LYS A 105 ? 0.46596 0.83279 0.67494 -0.12152 0.10899  -0.04137 112 LYS A NZ  
763  N N   . SER A 106 ? 0.27960 0.37736 0.39615 -0.11190 0.06892  -0.05176 113 SER A N   
764  C CA  . SER A 106 ? 0.30552 0.39118 0.41924 -0.14295 0.07283  -0.07035 113 SER A CA  
765  C C   . SER A 106 ? 0.29368 0.37320 0.40252 -0.13351 0.06243  -0.08245 113 SER A C   
766  O O   . SER A 106 ? 0.33684 0.44098 0.44962 -0.15624 0.06050  -0.10147 113 SER A O   
767  C CB  . SER A 106 ? 0.40849 0.41873 0.49903 -0.16104 0.08750  -0.06805 113 SER A CB  
768  O OG  . SER A 106 ? 0.45085 0.39935 0.52202 -0.13299 0.08454  -0.05729 113 SER A OG  
769  N N   . GLY A 107 ? 0.28778 0.34090 0.38772 -0.10327 0.05653  -0.07358 114 GLY A N   
770  C CA  . GLY A 107 ? 0.29872 0.35403 0.39394 -0.09589 0.04923  -0.08538 114 GLY A CA  
771  C C   . GLY A 107 ? 0.33358 0.45536 0.43759 -0.09693 0.03784  -0.08810 114 GLY A C   
772  O O   . GLY A 107 ? 0.31239 0.45170 0.41153 -0.11037 0.03402  -0.10471 114 GLY A O   
773  N N   . THR A 108 ? 0.26259 0.42074 0.37674 -0.08065 0.03185  -0.07178 115 THR A N   
774  C CA  . THR A 108 ? 0.30387 0.52474 0.42541 -0.07632 0.01881  -0.07057 115 THR A CA  
775  C C   . THR A 108 ? 0.33543 0.60582 0.47001 -0.10607 0.01675  -0.08764 115 THR A C   
776  O O   . THR A 108 ? 0.28214 0.59046 0.41214 -0.11240 0.00550  -0.09665 115 THR A O   
777  C CB  . THR A 108 ? 0.30579 0.55074 0.43773 -0.05086 0.01483  -0.05174 115 THR A CB  
778  O OG1 . THR A 108 ? 0.23935 0.43950 0.35545 -0.02783 0.01580  -0.03934 115 THR A OG1 
779  C CG2 . THR A 108 ? 0.25971 0.56886 0.39957 -0.04104 -0.00059 -0.04848 115 THR A CG2 
780  N N   . LYS A 109 ? 0.27268 0.54683 0.42131 -0.12741 0.02764  -0.09259 116 LYS A N   
781  C CA  . LYS A 109 ? 0.29103 0.61435 0.45285 -0.16214 0.02748  -0.11180 116 LYS A CA  
782  C C   . LYS A 109 ? 0.39616 0.69002 0.53575 -0.18254 0.02766  -0.13250 116 LYS A C   
783  O O   . LYS A 109 ? 0.37688 0.71192 0.51105 -0.19114 0.01820  -0.14297 116 LYS A O   
784  C CB  . LYS A 109 ? 0.28610 0.59172 0.45291 -0.18218 0.04374  -0.11108 116 LYS A CB  
785  C CG  . LYS A 109 ? 0.46847 0.78046 0.62857 -0.21631 0.04879  -0.12879 116 LYS A CG  
786  C CD  . LYS A 109 ? 0.55711 0.85375 0.71963 -0.23513 0.06537  -0.12449 116 LYS A CD  
787  C CE  . LYS A 109 ? 0.62053 0.95753 0.78702 -0.26498 0.06800  -0.14008 116 LYS A CE  
788  N NZ  . LYS A 109 ? 0.62435 0.99842 0.78823 -0.27055 0.05479  -0.15683 116 LYS A NZ  
789  N N   . ALA A 110 ? 0.31774 0.53739 0.44187 -0.18739 0.03939  -0.13870 117 ALA A N   
790  C CA  . ALA A 110 ? 0.40531 0.59164 0.50776 -0.20134 0.04241  -0.16017 117 ALA A CA  
791  C C   . ALA A 110 ? 0.38926 0.61025 0.48294 -0.18826 0.02883  -0.16433 117 ALA A C   
792  O O   . ALA A 110 ? 0.43088 0.67024 0.51016 -0.20107 0.02606  -0.17938 117 ALA A O   
793  C CB  . ALA A 110 ? 0.39114 0.48780 0.47965 -0.19840 0.05673  -0.16379 117 ALA A CB  
794  N N   . PHE A 111 ? 0.33599 0.55499 0.42832 -0.15603 0.02250  -0.14439 118 PHE A N   
795  C CA  . PHE A 111 ? 0.31599 0.55958 0.39201 -0.14314 0.01156  -0.14277 118 PHE A CA  
796  C C   . PHE A 111 ? 0.39846 0.72027 0.47708 -0.15133 -0.00554 -0.14312 118 PHE A C   
797  O O   . PHE A 111 ? 0.39100 0.73331 0.44957 -0.16211 -0.01091 -0.15557 118 PHE A O   
798  C CB  . PHE A 111 ? 0.27392 0.49541 0.34628 -0.10884 0.00995  -0.11749 118 PHE A CB  
799  C CG  . PHE A 111 ? 0.28002 0.51588 0.32999 -0.09726 0.00188  -0.11149 118 PHE A CG  
800  C CD1 . PHE A 111 ? 0.27681 0.51337 0.30646 -0.11236 0.00455  -0.13174 118 PHE A CD1 
801  C CD2 . PHE A 111 ? 0.33330 0.57486 0.37823 -0.07214 -0.00588 -0.08579 118 PHE A CD2 
802  C CE1 . PHE A 111 ? 0.28294 0.53052 0.28657 -0.10479 -0.00026 -0.12413 118 PHE A CE1 
803  C CE2 . PHE A 111 ? 0.31863 0.56195 0.33641 -0.06445 -0.01082 -0.07724 118 PHE A CE2 
804  C CZ  . PHE A 111 ? 0.30260 0.55167 0.29881 -0.08235 -0.00792 -0.09579 118 PHE A CZ  
805  N N   . MET A 112 ? 0.35699 0.72197 0.45832 -0.14249 -0.01303 -0.12821 119 MET A N   
806  C CA  . MET A 112 ? 0.56194 0.99440 0.66252 -0.13602 -0.03051 -0.12182 119 MET A CA  
807  C C   . MET A 112 ? 0.59214 1.04533 0.68938 -0.16503 -0.02737 -0.14246 119 MET A C   
808  O O   . MET A 112 ? 0.47302 0.97167 0.55888 -0.16593 -0.03986 -0.14420 119 MET A O   
809  C CB  . MET A 112 ? 0.53756 1.00478 0.66303 -0.10950 -0.03760 -0.09995 119 MET A CB  
810  C CG  . MET A 112 ? 0.22039 0.68857 0.33279 -0.07190 -0.05092 -0.07468 119 MET A CG  
811  S SD  . MET A 112 ? 0.86316 1.37463 1.00446 -0.03924 -0.05798 -0.05501 119 MET A SD  
812  C CE  . MET A 112 ? 0.23945 0.68909 0.36803 -0.00105 -0.05301 -0.02949 119 MET A CE  
813  N N   . GLU A 113 ? 0.45115 0.86634 0.55380 -0.18975 -0.01018 -0.15810 120 GLU A N   
814  C CA  . GLU A 113 ? 0.60641 1.02842 0.70023 -0.22046 -0.00418 -0.18059 120 GLU A CA  
815  C C   . GLU A 113 ? 0.48287 0.87638 0.54855 -0.22988 -0.00038 -0.19756 120 GLU A C   
816  O O   . GLU A 113 ? 0.49971 0.91260 0.55509 -0.25192 0.00092  -0.21552 120 GLU A O   
817  C CB  . GLU A 113 ? 0.61521 0.99437 0.71691 -0.24344 0.01425  -0.18959 120 GLU A CB  
818  C CG  . GLU A 113 ? 0.68963 1.10728 0.81694 -0.24376 0.01418  -0.17894 120 GLU A CG  
819  C CD  . GLU A 113 ? 0.86022 1.22395 0.98734 -0.26742 0.03438  -0.18415 120 GLU A CD  
820  O OE1 . GLU A 113 ? 0.74481 1.03647 0.85196 -0.27885 0.04676  -0.19388 120 GLU A OE1 
821  O OE2 . GLU A 113 ? 0.94700 1.33894 1.09168 -0.27377 0.03842  -0.17832 120 GLU A OE2 
822  N N   . ALA A 114 ? 0.46073 0.81209 0.51446 -0.21436 0.00265  -0.19392 121 ALA A N   
823  C CA  . ALA A 114 ? 0.44069 0.77185 0.46864 -0.21998 0.00763  -0.20989 121 ALA A CA  
824  C C   . ALA A 114 ? 0.50212 0.88581 0.51282 -0.20962 -0.00892 -0.20029 121 ALA A C   
825  O O   . ALA A 114 ? 0.56601 0.95963 0.55583 -0.22225 -0.00739 -0.21458 121 ALA A O   
826  C CB  . ALA A 114 ? 0.52470 0.78886 0.54782 -0.20761 0.02053  -0.21274 121 ALA A CB  
827  N N   . LEU A 115 ? 0.45403 0.87059 0.47144 -0.18649 -0.02477 -0.17499 122 LEU A N   
828  C CA  . LEU A 115 ? 0.46217 0.91463 0.45584 -0.17233 -0.04092 -0.15987 122 LEU A CA  
829  C C   . LEU A 115 ? 0.58550 1.09618 0.57383 -0.18357 -0.05269 -0.16437 122 LEU A C   
830  O O   . LEU A 115 ? 0.65209 1.17451 0.61240 -0.19102 -0.05580 -0.16979 122 LEU A O   
831  C CB  . LEU A 115 ? 0.43183 0.89639 0.43230 -0.14117 -0.05477 -0.12961 122 LEU A CB  
832  C CG  . LEU A 115 ? 0.43990 0.85397 0.43288 -0.12943 -0.04659 -0.12366 122 LEU A CG  
833  C CD1 . LEU A 115 ? 0.41355 0.82754 0.41071 -0.09529 -0.05639 -0.09021 122 LEU A CD1 
834  C CD2 . LEU A 115 ? 0.41488 0.80532 0.36954 -0.13623 -0.03952 -0.13155 122 LEU A CD2 
835  N N   . GLN A 116 ? 0.66552 1.21638 0.68054 -0.18544 -0.05882 -0.16284 123 GLN A N   
836  C CA  . GLN A 116 ? 0.59187 1.20332 0.60516 -0.19802 -0.06969 -0.17064 123 GLN A CA  
837  C C   . GLN A 116 ? 0.70753 1.30499 0.70864 -0.23413 -0.05513 -0.20244 123 GLN A C   
838  O O   . GLN A 116 ? 0.76873 1.41581 0.76360 -0.24905 -0.06318 -0.21279 123 GLN A O   
839  C CB  . GLN A 116 ? 0.76255 1.42121 0.81061 -0.19297 -0.07612 -0.16516 123 GLN A CB  
840  C CG  . GLN A 116 ? 0.62497 1.30382 0.68573 -0.15279 -0.09145 -0.13431 123 GLN A CG  
841  C CD  . GLN A 116 ? 0.98633 1.73805 1.07247 -0.14218 -0.10534 -0.12907 123 GLN A CD  
842  O OE1 . GLN A 116 ? 1.04640 1.83718 1.14402 -0.16878 -0.10249 -0.14954 123 GLN A OE1 
843  N NE2 . GLN A 116 ? 0.91737 1.68647 1.01169 -0.10243 -0.11975 -0.10254 123 GLN A NE2 
844  N N   . ALA A 117 ? 0.76981 1.30000 0.76741 -0.24642 -0.03422 -0.21808 124 ALA A N   
845  C CA  . ALA A 117 ? 0.69411 1.19634 0.68093 -0.27685 -0.01746 -0.24831 124 ALA A CA  
846  C C   . ALA A 117 ? 0.81624 1.27714 0.77650 -0.27567 -0.00737 -0.25828 124 ALA A C   
847  O O   . ALA A 117 ? 0.73830 1.14995 0.69360 -0.29080 0.01117  -0.28091 124 ALA A O   
848  C CB  . ALA A 117 ? 0.55253 1.00475 0.55734 -0.29074 0.00009  -0.25908 124 ALA A CB  
849  N N   . GLY A 118 ? 0.62272 1.10110 0.56483 -0.25685 -0.01855 -0.24111 125 GLY A N   
850  C CA  . GLY A 118 ? 0.65079 1.10648 0.56550 -0.25869 -0.00959 -0.25071 125 GLY A CA  
851  C C   . GLY A 118 ? 0.60996 1.02493 0.52057 -0.23639 -0.00369 -0.23694 125 GLY A C   
852  O O   . GLY A 118 ? 0.63114 1.04505 0.51673 -0.23276 -0.00174 -0.23455 125 GLY A O   
853  N N   . ALA A 119 ? 0.53276 0.91660 0.46648 -0.22311 -0.00038 -0.22800 126 ALA A N   
854  C CA  . ALA A 119 ? 0.43999 0.78427 0.37249 -0.20401 0.00697  -0.21891 126 ALA A CA  
855  C C   . ALA A 119 ? 0.61119 0.98184 0.52466 -0.18635 -0.00866 -0.19067 126 ALA A C   
856  O O   . ALA A 119 ? 0.51397 0.92954 0.42165 -0.18172 -0.02785 -0.17325 126 ALA A O   
857  C CB  . ALA A 119 ? 0.47329 0.77918 0.43432 -0.19561 0.01303  -0.21656 126 ALA A CB  
858  N N   . ASP A 120 ? 0.50181 0.84176 0.40453 -0.17488 0.00025  -0.18535 127 ASP A N   
859  C CA  . ASP A 120 ? 0.45500 0.80291 0.33410 -0.15870 -0.01058 -0.15685 127 ASP A CA  
860  C C   . ASP A 120 ? 0.40479 0.71706 0.29707 -0.14285 -0.00385 -0.14928 127 ASP A C   
861  O O   . ASP A 120 ? 0.43291 0.71447 0.35220 -0.14324 0.00898  -0.16659 127 ASP A O   
862  C CB  . ASP A 120 ? 0.49759 0.84602 0.34039 -0.16535 -0.00427 -0.15579 127 ASP A CB  
863  C CG  . ASP A 120 ? 0.52121 0.83684 0.37230 -0.17051 0.01995  -0.17814 127 ASP A CG  
864  O OD1 . ASP A 120 ? 0.72575 1.03576 0.59208 -0.18209 0.03098  -0.20526 127 ASP A OD1 
865  O OD2 . ASP A 120 ? 0.50688 0.80153 0.35243 -0.16113 0.02811  -0.16826 127 ASP A OD2 
866  N N   . ILE A 121 ? 0.39462 0.70378 0.26676 -0.12625 -0.01169 -0.11953 128 ILE A N   
867  C CA  . ILE A 121 ? 0.34961 0.61799 0.24357 -0.10493 -0.00475 -0.10141 128 ILE A CA  
868  C C   . ILE A 121 ? 0.39764 0.63324 0.30218 -0.10850 0.01685  -0.12067 128 ILE A C   
869  O O   . ILE A 121 ? 0.37475 0.58108 0.30816 -0.09481 0.02307  -0.11730 128 ILE A O   
870  C CB  . ILE A 121 ? 0.38688 0.64791 0.25328 -0.08752 -0.01493 -0.06511 128 ILE A CB  
871  C CG1 . ILE A 121 ? 0.48556 0.77748 0.36095 -0.07158 -0.03698 -0.04618 128 ILE A CG1 
872  C CG2 . ILE A 121 ? 0.40177 0.61690 0.27835 -0.07301 -0.00377 -0.05129 128 ILE A CG2 
873  C CD1 . ILE A 121 ? 0.52279 0.80886 0.36415 -0.05049 -0.05125 -0.01040 128 ILE A CD1 
874  N N   . SER A 122 ? 0.45662 0.70156 0.33981 -0.12575 0.02836  -0.14329 129 SER A N   
875  C CA  . SER A 122 ? 0.41296 0.63594 0.31234 -0.12439 0.04875  -0.16285 129 SER A CA  
876  C C   . SER A 122 ? 0.49168 0.69150 0.43013 -0.11796 0.05502  -0.18400 129 SER A C   
877  O O   . SER A 122 ? 0.43431 0.61298 0.39560 -0.10610 0.06683  -0.19187 129 SER A O   
878  C CB  . SER A 122 ? 0.40248 0.63799 0.28713 -0.13808 0.05969  -0.17405 129 SER A CB  
879  O OG  . SER A 122 ? 0.44085 0.68493 0.33328 -0.14861 0.06172  -0.19668 129 SER A OG  
880  N N   . MET A 123 ? 0.36943 0.57191 0.31642 -0.12512 0.04682  -0.19063 130 MET A N   
881  C CA  . MET A 123 ? 0.36322 0.53160 0.33967 -0.12102 0.05382  -0.20556 130 MET A CA  
882  C C   . MET A 123 ? 0.32377 0.46984 0.32309 -0.10498 0.04779  -0.18459 130 MET A C   
883  O O   . MET A 123 ? 0.34962 0.46281 0.36692 -0.10305 0.05252  -0.19270 130 MET A O   
884  C CB  . MET A 123 ? 0.44110 0.61651 0.41560 -0.14018 0.05289  -0.22030 130 MET A CB  
885  C CG  . MET A 123 ? 0.43893 0.64554 0.38874 -0.15401 0.05480  -0.22863 130 MET A CG  
886  S SD  . MET A 123 ? 0.56098 0.78955 0.50256 -0.17899 0.05068  -0.24397 130 MET A SD  
887  C CE  . MET A 123 ? 0.51805 0.68702 0.48449 -0.17754 0.06489  -0.26308 130 MET A CE  
888  N N   . ILE A 124 ? 0.29476 0.45035 0.29164 -0.09168 0.03945  -0.15534 131 ILE A N   
889  C CA  . ILE A 124 ? 0.28172 0.42079 0.29811 -0.07617 0.03384  -0.13316 131 ILE A CA  
890  C C   . ILE A 124 ? 0.28260 0.38088 0.31970 -0.06358 0.04318  -0.13916 131 ILE A C   
891  O O   . ILE A 124 ? 0.25811 0.33688 0.30870 -0.05925 0.04157  -0.13097 131 ILE A O   
892  C CB  . ILE A 124 ? 0.28115 0.42803 0.28637 -0.06286 0.02685  -0.10569 131 ILE A CB  
893  C CG1 . ILE A 124 ? 0.26346 0.39790 0.28602 -0.04720 0.02146  -0.08519 131 ILE A CG1 
894  C CG2 . ILE A 124 ? 0.27361 0.40913 0.27069 -0.05928 0.03697  -0.10867 131 ILE A CG2 
895  C CD1 . ILE A 124 ? 0.27233 0.40835 0.28114 -0.03365 0.01468  -0.06024 131 ILE A CD1 
896  N N   . GLY A 125 ? 0.30351 0.39184 0.34265 -0.05674 0.05276  -0.15289 132 GLY A N   
897  C CA  . GLY A 125 ? 0.35291 0.40782 0.41175 -0.03878 0.05791  -0.15618 132 GLY A CA  
898  C C   . GLY A 125 ? 0.36441 0.38272 0.42911 -0.04149 0.06258  -0.17130 132 GLY A C   
899  O O   . GLY A 125 ? 0.39086 0.37368 0.46638 -0.02526 0.06301  -0.16482 132 GLY A O   
900  N N   . GLN A 126 ? 0.36713 0.39024 0.42081 -0.06292 0.06586  -0.19060 133 GLN A N   
901  C CA  . GLN A 126 ? 0.38195 0.36320 0.43599 -0.07113 0.07124  -0.20252 133 GLN A CA  
902  C C   . GLN A 126 ? 0.47137 0.43629 0.52905 -0.07852 0.06659  -0.18482 133 GLN A C   
903  O O   . GLN A 126 ? 0.47041 0.38846 0.52574 -0.08496 0.07276  -0.18971 133 GLN A O   
904  C CB  . GLN A 126 ? 0.43357 0.43106 0.47384 -0.09487 0.07420  -0.22089 133 GLN A CB  
905  C CG  . GLN A 126 ? 0.46808 0.48075 0.50405 -0.08846 0.08055  -0.23482 133 GLN A CG  
906  C CD  . GLN A 126 ? 0.63997 0.66728 0.66050 -0.11173 0.08424  -0.25367 133 GLN A CD  
907  O OE1 . GLN A 126 ? 0.64811 0.64971 0.66436 -0.12614 0.08660  -0.26202 133 GLN A OE1 
908  N NE2 . GLN A 126 ? 0.61302 0.68101 0.62254 -0.11765 0.08553  -0.26010 133 GLN A NE2 
909  N N   . PHE A 127 ? 0.37288 0.37480 0.43388 -0.07706 0.05659  -0.16121 134 PHE A N   
910  C CA  . PHE A 127 ? 0.36900 0.36975 0.43582 -0.08333 0.05318  -0.14315 134 PHE A CA  
911  C C   . PHE A 127 ? 0.35906 0.34608 0.43209 -0.05952 0.05027  -0.11835 134 PHE A C   
912  O O   . PHE A 127 ? 0.34238 0.33585 0.41940 -0.06226 0.04839  -0.10225 134 PHE A O   
913  C CB  . PHE A 127 ? 0.30472 0.36441 0.37228 -0.09963 0.04410  -0.13954 134 PHE A CB  
914  C CG  . PHE A 127 ? 0.36167 0.44367 0.41952 -0.12443 0.04442  -0.16519 134 PHE A CG  
915  C CD1 . PHE A 127 ? 0.48784 0.55441 0.54539 -0.15240 0.05117  -0.18401 134 PHE A CD1 
916  C CD2 . PHE A 127 ? 0.32969 0.44272 0.37417 -0.12317 0.03986  -0.17225 134 PHE A CD2 
917  C CE1 . PHE A 127 ? 0.45118 0.53711 0.49624 -0.17281 0.05199  -0.20552 134 PHE A CE1 
918  C CE2 . PHE A 127 ? 0.39768 0.53244 0.42858 -0.14722 0.04021  -0.19754 134 PHE A CE2 
919  C CZ  . PHE A 127 ? 0.46804 0.58967 0.50037 -0.16852 0.04619  -0.21112 134 PHE A CZ  
920  N N   . GLY A 128 ? 0.32077 0.29388 0.39534 -0.03770 0.05058  -0.11735 135 GLY A N   
921  C CA  . GLY A 128 ? 0.31494 0.27284 0.39315 -0.01766 0.04743  -0.09777 135 GLY A CA  
922  C C   . GLY A 128 ? 0.26885 0.25951 0.34752 -0.01199 0.04073  -0.08004 135 GLY A C   
923  O O   . GLY A 128 ? 0.30824 0.28780 0.38720 0.00010  0.03865  -0.06465 135 GLY A O   
924  N N   . VAL A 129 ? 0.23819 0.26467 0.31277 -0.01952 0.03726  -0.08161 136 VAL A N   
925  C CA  . VAL A 129 ? 0.19010 0.23754 0.26075 -0.01191 0.03127  -0.06401 136 VAL A CA  
926  C C   . VAL A 129 ? 0.23346 0.29411 0.29274 -0.01074 0.03051  -0.06611 136 VAL A C   
927  O O   . VAL A 129 ? 0.21777 0.29219 0.26557 -0.00835 0.02565  -0.05334 136 VAL A O   
928  C CB  . VAL A 129 ? 0.20207 0.27843 0.27523 -0.01965 0.02640  -0.05709 136 VAL A CB  
929  C CG1 . VAL A 129 ? 0.24073 0.30607 0.32417 -0.02197 0.03044  -0.05152 136 VAL A CG1 
930  C CG2 . VAL A 129 ? 0.22624 0.32761 0.29676 -0.03827 0.02447  -0.07221 136 VAL A CG2 
931  N N   . GLY A 130 ? 0.25731 0.22148 0.28955 -0.00636 -0.02513 -0.06932 137 GLY A N   
932  C CA  . GLY A 130 ? 0.26776 0.24520 0.28177 0.00683  -0.02114 -0.06918 137 GLY A CA  
933  C C   . GLY A 130 ? 0.25916 0.24978 0.27374 0.00602  -0.01096 -0.05444 137 GLY A C   
934  O O   . GLY A 130 ? 0.25726 0.26219 0.26290 0.01287  -0.00850 -0.05065 137 GLY A O   
935  N N   . PHE A 131 ? 0.22424 0.20997 0.24894 -0.00184 -0.00592 -0.04575 138 PHE A N   
936  C CA  . PHE A 131 ? 0.22526 0.21989 0.25048 -0.00221 0.00021  -0.03548 138 PHE A CA  
937  C C   . PHE A 131 ? 0.22964 0.23593 0.25491 -0.00139 -0.00132 -0.03367 138 PHE A C   
938  O O   . PHE A 131 ? 0.22369 0.23594 0.24537 0.00195  0.00157  -0.02650 138 PHE A O   
939  C CB  . PHE A 131 ? 0.23915 0.22831 0.27208 -0.00851 0.00354  -0.02975 138 PHE A CB  
940  C CG  . PHE A 131 ? 0.22180 0.21708 0.25537 -0.00849 0.00607  -0.02389 138 PHE A CG  
941  C CD1 . PHE A 131 ? 0.23256 0.22878 0.26355 -0.00608 0.00744  -0.01952 138 PHE A CD1 
942  C CD2 . PHE A 131 ? 0.23316 0.23378 0.27197 -0.01042 0.00605  -0.02325 138 PHE A CD2 
943  C CE1 . PHE A 131 ? 0.19219 0.18870 0.22532 -0.00672 0.00665  -0.01605 138 PHE A CE1 
944  C CE2 . PHE A 131 ? 0.22781 0.22950 0.26519 -0.00766 0.00660  -0.02049 138 PHE A CE2 
945  C CZ  . PHE A 131 ? 0.23979 0.23644 0.27415 -0.00645 0.00581  -0.01769 138 PHE A CZ  
946  N N   . TYR A 132 ? 0.22336 0.23336 0.25542 -0.00484 -0.00639 -0.03868 139 TYR A N   
947  C CA  . TYR A 132 ? 0.21651 0.23861 0.25005 -0.00247 -0.00842 -0.03647 139 TYR A CA  
948  C C   . TYR A 132 ? 0.20352 0.23386 0.22378 0.00677  -0.01120 -0.03692 139 TYR A C   
949  O O   . TYR A 132 ? 0.23340 0.27163 0.25204 0.01098  -0.01165 -0.03104 139 TYR A O   
950  C CB  . TYR A 132 ? 0.20979 0.23977 0.25809 -0.00836 -0.01344 -0.04111 139 TYR A CB  
951  C CG  . TYR A 132 ? 0.20165 0.22874 0.26166 -0.01553 -0.00747 -0.03584 139 TYR A CG  
952  C CD1 . TYR A 132 ? 0.19565 0.22788 0.25660 -0.01256 -0.00193 -0.02948 139 TYR A CD1 
953  C CD2 . TYR A 132 ? 0.23470 0.25269 0.30276 -0.02338 -0.00762 -0.03689 139 TYR A CD2 
954  C CE1 . TYR A 132 ? 0.17914 0.21188 0.24594 -0.01581 0.00443  -0.02453 139 TYR A CE1 
955  C CE2 . TYR A 132 ? 0.25487 0.27230 0.33094 -0.02835 -0.00065 -0.02868 139 TYR A CE2 
956  C CZ  . TYR A 132 ? 0.22052 0.24772 0.29464 -0.02383 0.00582  -0.02266 139 TYR A CZ  
957  O OH  . TYR A 132 ? 0.23162 0.26143 0.30960 -0.02590 0.01317  -0.01455 139 TYR A OH  
958  N N   . SER A 133 ? 0.22157 0.25051 0.23066 0.01220  -0.01224 -0.04236 140 SER A N   
959  C CA  . SER A 133 ? 0.23006 0.27102 0.22292 0.02379  -0.01171 -0.03946 140 SER A CA  
960  C C   . SER A 133 ? 0.23095 0.27600 0.22346 0.02497  -0.00282 -0.02236 140 SER A C   
961  O O   . SER A 133 ? 0.23675 0.29411 0.21870 0.03345  -0.00084 -0.01387 140 SER A O   
962  C CB  . SER A 133 ? 0.27273 0.31306 0.25180 0.03265  -0.01350 -0.04989 140 SER A CB  
963  O OG  . SER A 133 ? 0.25696 0.29303 0.23669 0.03318  -0.00521 -0.04434 140 SER A OG  
964  N N   . ALA A 134 ? 0.23624 0.27143 0.24062 0.01661  0.00159  -0.01654 141 ALA A N   
965  C CA  . ALA A 134 ? 0.22542 0.26100 0.23482 0.01481  0.00636  -0.00164 141 ALA A CA  
966  C C   . ALA A 134 ? 0.22684 0.26468 0.23488 0.01809  0.00387  0.00569  141 ALA A C   
967  O O   . ALA A 134 ? 0.23181 0.27241 0.24014 0.01970  0.00727  0.02061  141 ALA A O   
968  C CB  . ALA A 134 ? 0.19872 0.22149 0.22033 0.00608  0.00680  -0.00130 141 ALA A CB  
969  N N   . TYR A 135 ? 0.21593 0.25345 0.22505 0.01901  -0.00209 -0.00281 142 TYR A N   
970  C CA  . TYR A 135 ? 0.22918 0.26859 0.23805 0.02422  -0.00535 0.00358  142 TYR A CA  
971  C C   . TYR A 135 ? 0.24370 0.29833 0.23782 0.03503  -0.00719 0.00826  142 TYR A C   
972  O O   . TYR A 135 ? 0.27101 0.32846 0.26268 0.04170  -0.01021 0.01576  142 TYR A O   
973  C CB  . TYR A 135 ? 0.20688 0.24657 0.22505 0.02280  -0.01021 -0.00611 142 TYR A CB  
974  C CG  . TYR A 135 ? 0.21321 0.23941 0.24086 0.01682  -0.00730 -0.00682 142 TYR A CG  
975  C CD1 . TYR A 135 ? 0.24121 0.25508 0.27157 0.01962  -0.00799 -0.00047 142 TYR A CD1 
976  C CD2 . TYR A 135 ? 0.20815 0.23197 0.24007 0.00979  -0.00484 -0.01382 142 TYR A CD2 
977  C CE1 . TYR A 135 ? 0.24012 0.24156 0.27532 0.01669  -0.00736 -0.00430 142 TYR A CE1 
978  C CE2 . TYR A 135 ? 0.21642 0.23047 0.25259 0.00694  -0.00254 -0.01441 142 TYR A CE2 
979  C CZ  . TYR A 135 ? 0.23389 0.23776 0.27062 0.01091  -0.00429 -0.01106 142 TYR A CZ  
980  O OH  . TYR A 135 ? 0.22676 0.22124 0.26428 0.01048  -0.00409 -0.01492 142 TYR A OH  
981  N N   . LEU A 136 ? 0.24876 0.31329 0.23088 0.03932  -0.00529 0.00474  143 LEU A N   
982  C CA  . LEU A 136 ? 0.25424 0.33557 0.21777 0.05249  -0.00472 0.01235  143 LEU A CA  
983  C C   . LEU A 136 ? 0.25983 0.34187 0.22454 0.05333  0.00417  0.03693  143 LEU A C   
984  O O   . LEU A 136 ? 0.29155 0.38413 0.24475 0.06342  0.00472  0.05029  143 LEU A O   
985  C CB  . LEU A 136 ? 0.27653 0.36832 0.22492 0.05980  -0.00403 0.00148  143 LEU A CB  
986  C CG  . LEU A 136 ? 0.27511 0.36435 0.22127 0.05994  -0.01569 -0.02315 143 LEU A CG  
987  C CD1 . LEU A 136 ? 0.27157 0.36245 0.20458 0.06718  -0.01495 -0.03462 143 LEU A CD1 
988  C CD2 . LEU A 136 ? 0.29628 0.39780 0.23394 0.06820  -0.02729 -0.02992 143 LEU A CD2 
989  N N   . VAL A 137 ? 0.25866 0.32933 0.23921 0.04210  0.01014  0.04427  144 VAL A N   
990  C CA  . VAL A 137 ? 0.28261 0.35551 0.26987 0.03983  0.01801  0.06862  144 VAL A CA  
991  C C   . VAL A 137 ? 0.27723 0.32576 0.28577 0.02739  0.01514  0.07495  144 VAL A C   
992  O O   . VAL A 137 ? 0.29321 0.33698 0.31153 0.02368  0.01810  0.09603  144 VAL A O   
993  C CB  . VAL A 137 ? 0.25873 0.34867 0.24659 0.03976  0.02779  0.07489  144 VAL A CB  
994  C CG1 . VAL A 137 ? 0.25964 0.37436 0.22162 0.05706  0.03067  0.06950  144 VAL A CG1 
995  C CG2 . VAL A 137 ? 0.25871 0.33900 0.25931 0.03000  0.02674  0.06072  144 VAL A CG2 
996  N N   . ALA A 138 ? 0.27562 0.30856 0.29117 0.02174  0.00893  0.05759  145 ALA A N   
997  C CA  . ALA A 138 ? 0.25965 0.26946 0.29181 0.01246  0.00486  0.05867  145 ALA A CA  
998  C C   . ALA A 138 ? 0.27671 0.27264 0.30749 0.01802  -0.00247 0.05197  145 ALA A C   
999  O O   . ALA A 138 ? 0.30972 0.31426 0.33325 0.02366  -0.00482 0.03843  145 ALA A O   
1000 C CB  . ALA A 138 ? 0.25240 0.25765 0.29196 0.00436  0.00434  0.04519  145 ALA A CB  
1001 N N   . GLU A 139 ? 0.27481 0.24952 0.31483 0.01655  -0.00671 0.06158  146 GLU A N   
1002 C CA  . GLU A 139 ? 0.29795 0.25702 0.33753 0.02418  -0.01410 0.05310  146 GLU A CA  
1003 C C   . GLU A 139 ? 0.29600 0.24395 0.34038 0.02085  -0.01768 0.03514  146 GLU A C   
1004 O O   . GLU A 139 ? 0.31509 0.26198 0.35613 0.02954  -0.02086 0.02357  146 GLU A O   
1005 C CB  . GLU A 139 ? 0.33864 0.27445 0.38459 0.02649  -0.01878 0.06944  146 GLU A CB  
1006 C CG  . GLU A 139 ? 0.44336 0.35461 0.50638 0.01398  -0.02268 0.07550  146 GLU A CG  
1007 C CD  . GLU A 139 ? 0.74981 0.63648 0.82241 0.01383  -0.02722 0.09675  146 GLU A CD  
1008 O OE1 . GLU A 139 ? 0.66619 0.55922 0.72927 0.02441  -0.02486 0.11049  146 GLU A OE1 
1009 O OE2 . GLU A 139 ? 0.66682 0.52660 0.75727 0.00305  -0.03450 0.09987  146 GLU A OE2 
1010 N N   . LYS A 140 ? 0.26123 0.20533 0.31278 0.01010  -0.01678 0.03323  147 LYS A N   
1011 C CA  . LYS A 140 ? 0.25300 0.18824 0.30575 0.00856  -0.02056 0.01726  147 LYS A CA  
1012 C C   . LYS A 140 ? 0.25235 0.20043 0.30756 -0.00065 -0.01587 0.01611  147 LYS A C   
1013 O O   . LYS A 140 ? 0.25601 0.21100 0.31804 -0.00730 -0.01249 0.02868  147 LYS A O   
1014 C CB  . LYS A 140 ? 0.26881 0.17434 0.32974 0.00752  -0.03082 0.01545  147 LYS A CB  
1015 C CG  . LYS A 140 ? 0.29258 0.19054 0.35014 0.00905  -0.03604 -0.00273 147 LYS A CG  
1016 C CD  . LYS A 140 ? 0.34706 0.21245 0.40877 0.01280  -0.04922 -0.00912 147 LYS A CD  
1017 C CE  . LYS A 140 ? 0.40854 0.25907 0.48735 -0.00212 -0.05736 -0.00394 147 LYS A CE  
1018 N NZ  . LYS A 140 ? 0.50635 0.31862 0.59240 -0.00037 -0.07391 -0.01112 147 LYS A NZ  
1019 N N   . VAL A 141 ? 0.21061 0.16479 0.26030 0.00047  -0.01454 0.00322  148 VAL A N   
1020 C CA  . VAL A 141 ? 0.20727 0.17058 0.25860 -0.00600 -0.01134 0.00170  148 VAL A CA  
1021 C C   . VAL A 141 ? 0.25138 0.20496 0.30157 -0.00569 -0.01682 -0.00931 148 VAL A C   
1022 O O   . VAL A 141 ? 0.25259 0.20416 0.29445 0.00199  -0.01745 -0.01851 148 VAL A O   
1023 C CB  . VAL A 141 ? 0.22056 0.20068 0.26430 -0.00399 -0.00452 -0.00153 148 VAL A CB  
1024 C CG1 . VAL A 141 ? 0.23028 0.21588 0.27490 -0.00815 -0.00200 -0.00337 148 VAL A CG1 
1025 C CG2 . VAL A 141 ? 0.21744 0.20884 0.25785 -0.00118 -0.00120 0.00642  148 VAL A CG2 
1026 N N   . THR A 142 ? 0.22524 0.17667 0.28375 -0.01268 -0.02076 -0.00805 149 THR A N   
1027 C CA  . THR A 142 ? 0.25637 0.20184 0.31141 -0.01125 -0.02753 -0.01931 149 THR A CA  
1028 C C   . THR A 142 ? 0.27609 0.23724 0.32997 -0.01353 -0.02257 -0.01812 149 THR A C   
1029 O O   . THR A 142 ? 0.25453 0.22608 0.31871 -0.01944 -0.01947 -0.00910 149 THR A O   
1030 C CB  . THR A 142 ? 0.23885 0.16748 0.30678 -0.01714 -0.04061 -0.02109 149 THR A CB  
1031 O OG1 . THR A 142 ? 0.30655 0.21606 0.37756 -0.01510 -0.04557 -0.01959 149 THR A OG1 
1032 C CG2 . THR A 142 ? 0.26812 0.19027 0.32691 -0.01168 -0.05030 -0.03697 149 THR A CG2 
1033 N N   . VAL A 143 ? 0.22593 0.18994 0.26719 -0.00730 -0.02134 -0.02582 150 VAL A N   
1034 C CA  . VAL A 143 ? 0.22134 0.19643 0.26007 -0.00746 -0.01735 -0.02387 150 VAL A CA  
1035 C C   . VAL A 143 ? 0.27735 0.25016 0.31053 -0.00381 -0.02602 -0.03156 150 VAL A C   
1036 O O   . VAL A 143 ? 0.26551 0.23465 0.28431 0.00465  -0.02734 -0.03909 150 VAL A O   
1037 C CB  . VAL A 143 ? 0.22498 0.20576 0.25423 -0.00363 -0.00776 -0.02249 150 VAL A CB  
1038 C CG1 . VAL A 143 ? 0.24766 0.23387 0.27408 -0.00259 -0.00520 -0.01980 150 VAL A CG1 
1039 C CG2 . VAL A 143 ? 0.22397 0.20806 0.25783 -0.00641 -0.00230 -0.01787 150 VAL A CG2 
1040 N N   . ILE A 144 ? 0.21657 0.19474 0.26094 -0.00863 -0.03233 -0.02993 151 ILE A N   
1041 C CA  . ILE A 144 ? 0.23150 0.21033 0.27099 -0.00464 -0.04334 -0.03834 151 ILE A CA  
1042 C C   . ILE A 144 ? 0.24380 0.23584 0.27721 -0.00010 -0.03762 -0.03318 151 ILE A C   
1043 O O   . ILE A 144 ? 0.24425 0.24584 0.28944 -0.00410 -0.03240 -0.02481 151 ILE A O   
1044 C CB  . ILE A 144 ? 0.24971 0.22746 0.31065 -0.01400 -0.05747 -0.04029 151 ILE A CB  
1045 C CG1 . ILE A 144 ? 0.37551 0.33729 0.44943 -0.02166 -0.06194 -0.03949 151 ILE A CG1 
1046 C CG2 . ILE A 144 ? 0.27641 0.25404 0.32950 -0.00808 -0.07274 -0.05337 151 ILE A CG2 
1047 C CD1 . ILE A 144 ? 0.38331 0.32496 0.44325 -0.01400 -0.07059 -0.05340 151 ILE A CD1 
1048 N N   . THR A 145 ? 0.22989 0.22300 0.24413 0.01005  -0.03830 -0.03720 152 THR A N   
1049 C CA  . THR A 145 ? 0.24590 0.24759 0.25397 0.01513  -0.03204 -0.02935 152 THR A CA  
1050 C C   . THR A 145 ? 0.25473 0.26205 0.24692 0.02582  -0.04013 -0.03367 152 THR A C   
1051 O O   . THR A 145 ? 0.27218 0.27658 0.24940 0.03287  -0.04658 -0.04325 152 THR A O   
1052 C CB  . THR A 145 ? 0.24301 0.24044 0.24313 0.01644  -0.01772 -0.02163 152 THR A CB  
1053 O OG1 . THR A 145 ? 0.25864 0.25812 0.25777 0.01941  -0.01267 -0.01311 152 THR A OG1 
1054 C CG2 . THR A 145 ? 0.27116 0.26748 0.25357 0.02390  -0.01412 -0.02356 152 THR A CG2 
1055 N N   . LYS A 146 ? 0.23881 0.25520 0.23266 0.02949  -0.04038 -0.02710 153 LYS A N   
1056 C CA  . LYS A 146 ? 0.26687 0.29095 0.24323 0.04199  -0.04733 -0.02823 153 LYS A CA  
1057 C C   . LYS A 146 ? 0.29096 0.31605 0.26101 0.04850  -0.03742 -0.01404 153 LYS A C   
1058 O O   . LYS A 146 ? 0.25979 0.28811 0.24526 0.04589  -0.03604 -0.00904 153 LYS A O   
1059 C CB  . LYS A 146 ? 0.24784 0.28360 0.23741 0.04061  -0.06512 -0.03695 153 LYS A CB  
1060 C CG  . LYS A 146 ? 0.30773 0.35564 0.28012 0.05505  -0.07557 -0.03899 153 LYS A CG  
1061 C CD  . LYS A 146 ? 0.32904 0.37317 0.27113 0.06728  -0.08059 -0.04892 153 LYS A CD  
1062 C CE  . LYS A 146 ? 0.36828 0.42691 0.29129 0.08308  -0.09314 -0.05209 153 LYS A CE  
1063 N NZ  . LYS A 146 ? 0.36317 0.42648 0.27029 0.09429  -0.08003 -0.03297 153 LYS A NZ  
1064 N N   . HIS A 147 ? 0.29191 0.31450 0.23992 0.05794  -0.03051 -0.00682 154 HIS A N   
1065 C CA  . HIS A 147 ? 0.26575 0.28488 0.20587 0.06492  -0.02212 0.00905  154 HIS A CA  
1066 C C   . HIS A 147 ? 0.29198 0.32302 0.21273 0.08054  -0.03072 0.01111  154 HIS A C   
1067 O O   . HIS A 147 ? 0.33828 0.37844 0.24307 0.08770  -0.03887 0.00137  154 HIS A O   
1068 C CB  . HIS A 147 ? 0.31182 0.32188 0.24469 0.06253  -0.00732 0.01994  154 HIS A CB  
1069 C CG  . HIS A 147 ? 0.28976 0.28959 0.22046 0.06542  0.00161  0.03835  154 HIS A CG  
1070 N ND1 . HIS A 147 ? 0.33585 0.33986 0.24772 0.07872  0.00254  0.05153  154 HIS A ND1 
1071 C CD2 . HIS A 147 ? 0.31374 0.29670 0.25882 0.05712  0.00860  0.04560  154 HIS A CD2 
1072 C CE1 . HIS A 147 ? 0.39918 0.38709 0.31598 0.07727  0.01048  0.06823  154 HIS A CE1 
1073 N NE2 . HIS A 147 ? 0.33471 0.30850 0.27203 0.06396  0.01331  0.06329  154 HIS A NE2 
1074 N N   . ASN A 148 ? 0.30108 0.33180 0.22158 0.08806  -0.03043 0.02251  155 ASN A N   
1075 C CA  . ASN A 148 ? 0.31023 0.35412 0.21099 0.10503  -0.03940 0.02606  155 ASN A CA  
1076 C C   . ASN A 148 ? 0.38134 0.42979 0.25155 0.11603  -0.03461 0.03167  155 ASN A C   
1077 O O   . ASN A 148 ? 0.41342 0.47727 0.26243 0.13077  -0.04568 0.02655  155 ASN A O   
1078 C CB  . ASN A 148 ? 0.35038 0.38823 0.25231 0.11373  -0.03610 0.04235  155 ASN A CB  
1079 C CG  . ASN A 148 ? 0.38798 0.43391 0.31379 0.11239  -0.04492 0.03543  155 ASN A CG  
1080 O OD1 . ASN A 148 ? 0.40763 0.47071 0.34726 0.10734  -0.05689 0.02073  155 ASN A OD1 
1081 N ND2 . ASN A 148 ? 0.36671 0.40013 0.29955 0.11696  -0.03881 0.04656  155 ASN A ND2 
1082 N N   . ASP A 149 ? 0.41393 0.45272 0.28139 0.11036  -0.01851 0.04221  156 ASP A N   
1083 C CA  . ASP A 149 ? 0.39502 0.44380 0.23434 0.12288  -0.01026 0.05293  156 ASP A CA  
1084 C C   . ASP A 149 ? 0.46080 0.51885 0.29085 0.12365  -0.01142 0.03655  156 ASP A C   
1085 O O   . ASP A 149 ? 0.49226 0.56213 0.30012 0.13463  -0.00149 0.04529  156 ASP A O   
1086 C CB  . ASP A 149 ? 0.46803 0.50548 0.31161 0.11765  0.00890  0.07899  156 ASP A CB  
1087 C CG  . ASP A 149 ? 0.56073 0.58467 0.40789 0.12149  0.00945  0.09692  156 ASP A CG  
1088 O OD1 . ASP A 149 ? 0.52533 0.55613 0.36402 0.13365  -0.00316 0.09243  156 ASP A OD1 
1089 O OD2 . ASP A 149 ? 0.53065 0.53611 0.39122 0.11230  0.02096  0.11444  156 ASP A OD2 
1090 N N   . ASP A 150 ? 0.38792 0.44161 0.23413 0.11382  -0.02280 0.01444  157 ASP A N   
1091 C CA  . ASP A 150 ? 0.35914 0.41586 0.19796 0.11528  -0.02428 -0.00131 157 ASP A CA  
1092 C C   . ASP A 150 ? 0.45428 0.50704 0.30352 0.11095  -0.04533 -0.02640 157 ASP A C   
1093 O O   . ASP A 150 ? 0.40670 0.45940 0.27136 0.10560  -0.05706 -0.02971 157 ASP A O   
1094 C CB  . ASP A 150 ? 0.37107 0.41982 0.22746 0.10157  -0.00840 0.00562  157 ASP A CB  
1095 C CG  . ASP A 150 ? 0.41794 0.47688 0.25863 0.11075  -0.00228 -0.00055 157 ASP A CG  
1096 O OD1 . ASP A 150 ? 0.44423 0.51269 0.25946 0.12793  -0.01166 -0.01452 157 ASP A OD1 
1097 O OD2 . ASP A 150 ? 0.39073 0.45002 0.24408 0.10252  0.01179  0.00832  157 ASP A OD2 
1098 N N   . GLU A 151 ? 0.40335 0.45328 0.24620 0.11356  -0.05043 -0.04343 158 GLU A N   
1099 C CA  . GLU A 151 ? 0.42519 0.46638 0.28040 0.10781  -0.07143 -0.06654 158 GLU A CA  
1100 C C   . GLU A 151 ? 0.33576 0.36222 0.22452 0.08659  -0.06752 -0.06581 158 GLU A C   
1101 O O   . GLU A 151 ? 0.35406 0.37790 0.25274 0.07857  -0.05022 -0.05106 158 GLU A O   
1102 C CB  . GLU A 151 ? 0.47379 0.51459 0.30295 0.12417  -0.08158 -0.08712 158 GLU A CB  
1103 C CG  . GLU A 151 ? 0.56274 0.62080 0.35439 0.14831  -0.08827 -0.09082 158 GLU A CG  
1104 C CD  . GLU A 151 ? 0.80863 0.87515 0.60491 0.14798  -0.10257 -0.08928 158 GLU A CD  
1105 O OE1 . GLU A 151 ? 0.94870 1.03024 0.72589 0.16060  -0.09418 -0.07272 158 GLU A OE1 
1106 O OE2 . GLU A 151 ? 0.80584 0.86529 0.62861 0.13453  -0.12118 -0.10225 158 GLU A OE2 
1107 N N   . GLN A 152 ? 0.36219 0.37928 0.26955 0.07715  -0.08460 -0.08110 159 GLN A N   
1108 C CA  . GLN A 152 ? 0.34293 0.34842 0.28092 0.05831  -0.08122 -0.07795 159 GLN A CA  
1109 C C   . GLN A 152 ? 0.32252 0.31488 0.25554 0.05963  -0.07581 -0.08398 159 GLN A C   
1110 O O   . GLN A 152 ? 0.35638 0.34097 0.27450 0.07011  -0.08731 -0.10116 159 GLN A O   
1111 C CB  . GLN A 152 ? 0.32185 0.32447 0.28639 0.04598  -0.10046 -0.08709 159 GLN A CB  
1112 C CG  . GLN A 152 ? 0.31748 0.31487 0.31511 0.02677  -0.09441 -0.07736 159 GLN A CG  
1113 C CD  . GLN A 152 ? 0.38945 0.39466 0.41787 0.01402  -0.10967 -0.07870 159 GLN A CD  
1114 O OE1 . GLN A 152 ? 0.40657 0.43000 0.43870 0.01683  -0.11374 -0.07532 159 GLN A OE1 
1115 N NE2 . GLN A 152 ? 0.38169 0.37464 0.43442 0.00008  -0.11810 -0.08183 159 GLN A NE2 
1116 N N   . TYR A 153 ? 0.28731 0.27740 0.23244 0.05069  -0.05990 -0.07136 160 TYR A N   
1117 C CA  . TYR A 153 ? 0.30688 0.28926 0.24912 0.05287  -0.05285 -0.07400 160 TYR A CA  
1118 C C   . TYR A 153 ? 0.30051 0.27196 0.26882 0.03706  -0.05172 -0.06970 160 TYR A C   
1119 O O   . TYR A 153 ? 0.28902 0.26441 0.27491 0.02533  -0.04816 -0.05926 160 TYR A O   
1120 C CB  . TYR A 153 ? 0.31990 0.31536 0.25026 0.05922  -0.03345 -0.06085 160 TYR A CB  
1121 C CG  . TYR A 153 ? 0.36077 0.36875 0.26181 0.07855  -0.03192 -0.06413 160 TYR A CG  
1122 C CD1 . TYR A 153 ? 0.36033 0.36827 0.24488 0.09324  -0.03447 -0.07727 160 TYR A CD1 
1123 C CD2 . TYR A 153 ? 0.40259 0.42288 0.29034 0.08478  -0.02870 -0.05430 160 TYR A CD2 
1124 C CE1 . TYR A 153 ? 0.45491 0.47854 0.30869 0.11464  -0.03215 -0.08062 160 TYR A CE1 
1125 C CE2 . TYR A 153 ? 0.47135 0.50634 0.32839 0.10512  -0.02673 -0.05560 160 TYR A CE2 
1126 C CZ  . TYR A 153 ? 0.46769 0.50577 0.30729 0.12024  -0.02804 -0.06911 160 TYR A CZ  
1127 O OH  . TYR A 153 ? 0.59663 0.65326 0.40253 0.14375  -0.02486 -0.07079 160 TYR A OH  
1128 N N   . ALA A 154 ? 0.29275 0.25218 0.26119 0.03951  -0.05348 -0.07678 161 ALA A N   
1129 C CA  . ALA A 154 ? 0.28109 0.23125 0.26936 0.02813  -0.05040 -0.07046 161 ALA A CA  
1130 C C   . ALA A 154 ? 0.29742 0.25280 0.27921 0.03449  -0.03737 -0.06646 161 ALA A C   
1131 O O   . ALA A 154 ? 0.30449 0.25904 0.27121 0.04866  -0.03820 -0.07584 161 ALA A O   
1132 C CB  . ALA A 154 ? 0.33566 0.26388 0.33470 0.02453  -0.06711 -0.08092 161 ALA A CB  
1133 N N   . TRP A 155 ? 0.24826 0.21142 0.24137 0.02551  -0.02630 -0.05370 162 TRP A N   
1134 C CA  . TRP A 155 ? 0.23579 0.20558 0.23065 0.02752  -0.01641 -0.04902 162 TRP A CA  
1135 C C   . TRP A 155 ? 0.27780 0.23538 0.28569 0.02168  -0.02098 -0.04765 162 TRP A C   
1136 O O   . TRP A 155 ? 0.24873 0.20031 0.26829 0.01147  -0.02509 -0.04281 162 TRP A O   
1137 C CB  . TRP A 155 ? 0.24395 0.22741 0.24350 0.02077  -0.00503 -0.03756 162 TRP A CB  
1138 C CG  . TRP A 155 ? 0.21699 0.21055 0.22376 0.01895  0.00348  -0.03201 162 TRP A CG  
1139 C CD1 . TRP A 155 ? 0.22343 0.23285 0.22908 0.02231  0.01258  -0.02735 162 TRP A CD1 
1140 C CD2 . TRP A 155 ? 0.21531 0.20709 0.23323 0.01285  0.00304  -0.02934 162 TRP A CD2 
1141 N NE1 . TRP A 155 ? 0.22325 0.24042 0.24191 0.01707  0.01592  -0.02369 162 TRP A NE1 
1142 C CE2 . TRP A 155 ? 0.20175 0.20789 0.22533 0.01259  0.00974  -0.02582 162 TRP A CE2 
1143 C CE3 . TRP A 155 ? 0.21002 0.19201 0.23426 0.00781  -0.00227 -0.02803 162 TRP A CE3 
1144 C CZ2 . TRP A 155 ? 0.20264 0.21276 0.23549 0.00886  0.00908  -0.02418 162 TRP A CZ2 
1145 C CZ3 . TRP A 155 ? 0.21898 0.20558 0.24949 0.00543  -0.00051 -0.02404 162 TRP A CZ3 
1146 C CH2 . TRP A 155 ? 0.20610 0.20604 0.23958 0.00668  0.00398  -0.02376 162 TRP A CH2 
1147 N N   . GLU A 156 ? 0.23657 0.19328 0.24324 0.02909  -0.01948 -0.04983 163 GLU A N   
1148 C CA  . GLU A 156 ? 0.25413 0.19977 0.27177 0.02497  -0.02301 -0.04533 163 GLU A CA  
1149 C C   . GLU A 156 ? 0.22379 0.18111 0.24217 0.03144  -0.01649 -0.04260 163 GLU A C   
1150 O O   . GLU A 156 ? 0.26544 0.23334 0.27674 0.04283  -0.01289 -0.04806 163 GLU A O   
1151 C CB  . GLU A 156 ? 0.30883 0.22911 0.32693 0.02930  -0.03633 -0.05350 163 GLU A CB  
1152 C CG  . GLU A 156 ? 0.39085 0.29604 0.42463 0.01885  -0.04158 -0.04356 163 GLU A CG  
1153 C CD  . GLU A 156 ? 0.51663 0.39260 0.55596 0.01856  -0.05723 -0.05086 163 GLU A CD  
1154 O OE1 . GLU A 156 ? 0.49554 0.35644 0.52386 0.03270  -0.06483 -0.06523 163 GLU A OE1 
1155 O OE2 . GLU A 156 ? 0.40809 0.27765 0.46342 0.00443  -0.06289 -0.04378 163 GLU A OE2 
1156 N N   . SER A 157 ? 0.22404 0.18219 0.25115 0.02572  -0.01544 -0.03381 164 SER A N   
1157 C CA  . SER A 157 ? 0.22770 0.19687 0.25680 0.03307  -0.01269 -0.03210 164 SER A CA  
1158 C C   . SER A 157 ? 0.21997 0.18078 0.25431 0.03081  -0.01626 -0.02318 164 SER A C   
1159 O O   . SER A 157 ? 0.24268 0.20357 0.28035 0.02106  -0.01505 -0.01500 164 SER A O   
1160 C CB  . SER A 157 ? 0.21614 0.21064 0.24900 0.02958  -0.00437 -0.02968 164 SER A CB  
1161 O OG  . SER A 157 ? 0.23142 0.24026 0.26962 0.03655  -0.00379 -0.02886 164 SER A OG  
1162 N N   . SER A 158 ? 0.23977 0.19570 0.27380 0.04213  -0.01992 -0.02379 165 SER A N   
1163 C CA  . SER A 158 ? 0.26414 0.21830 0.30106 0.04372  -0.02201 -0.01313 165 SER A CA  
1164 C C   . SER A 158 ? 0.27202 0.25302 0.31029 0.04971  -0.01873 -0.01316 165 SER A C   
1165 O O   . SER A 158 ? 0.30207 0.28459 0.34046 0.05815  -0.02212 -0.00748 165 SER A O   
1166 C CB  . SER A 158 ? 0.33563 0.26220 0.37274 0.05269  -0.03052 -0.01166 165 SER A CB  
1167 O OG  . SER A 158 ? 0.35391 0.25471 0.39499 0.04372  -0.03629 -0.01045 165 SER A OG  
1168 N N   . ALA A 159 ? 0.22787 0.23011 0.26893 0.04482  -0.01322 -0.01836 166 ALA A N   
1169 C CA  . ALA A 159 ? 0.24697 0.27766 0.29555 0.04736  -0.01158 -0.01983 166 ALA A CA  
1170 C C   . ALA A 159 ? 0.24992 0.28879 0.30166 0.06317  -0.01272 -0.02343 166 ALA A C   
1171 O O   . ALA A 159 ? 0.31109 0.33947 0.35796 0.07103  -0.01175 -0.02905 166 ALA A O   
1172 C CB  . ALA A 159 ? 0.29018 0.32860 0.33795 0.04428  -0.01497 -0.01432 166 ALA A CB  
1173 N N   . GLY A 160 ? 0.25664 0.31714 0.31611 0.07014  -0.01531 -0.02184 167 GLY A N   
1174 C CA  . GLY A 160 ? 0.29261 0.36560 0.35668 0.08734  -0.01546 -0.02531 167 GLY A CA  
1175 C C   . GLY A 160 ? 0.30067 0.39856 0.37335 0.08850  -0.00700 -0.03006 167 GLY A C   
1176 O O   . GLY A 160 ? 0.28496 0.39345 0.35837 0.10579  -0.00493 -0.03400 167 GLY A O   
1177 N N   . GLY A 161 ? 0.22471 0.33257 0.30345 0.07213  -0.00157 -0.02864 168 GLY A N   
1178 C CA  . GLY A 161 ? 0.18643 0.32426 0.27793 0.07063  0.00765  -0.02767 168 GLY A CA  
1179 C C   . GLY A 161 ? 0.17417 0.30172 0.25285 0.07247  0.01512  -0.02958 168 GLY A C   
1180 O O   . GLY A 161 ? 0.20412 0.35859 0.29152 0.07256  0.02484  -0.02557 168 GLY A O   
1181 N N   . SER A 162 ? 0.19070 0.28340 0.25015 0.07504  0.01055  -0.03464 169 SER A N   
1182 C CA  . SER A 162 ? 0.18880 0.27396 0.23375 0.08082  0.01495  -0.03915 169 SER A CA  
1183 C C   . SER A 162 ? 0.19216 0.24478 0.22592 0.06969  0.00929  -0.04080 169 SER A C   
1184 O O   . SER A 162 ? 0.24201 0.27590 0.27735 0.06179  0.00245  -0.03881 169 SER A O   
1185 C CB  . SER A 162 ? 0.25578 0.33652 0.28776 0.10493  0.01300  -0.04920 169 SER A CB  
1186 O OG  . SER A 162 ? 0.31795 0.36196 0.34162 0.10931  0.00070  -0.05527 169 SER A OG  
1187 N N   . PHE A 163 ? 0.22386 0.27480 0.24690 0.07011  0.01302  -0.04291 170 PHE A N   
1188 C CA  . PHE A 163 ? 0.22661 0.25182 0.23999 0.06192  0.00719  -0.04546 170 PHE A CA  
1189 C C   . PHE A 163 ? 0.24514 0.26516 0.24004 0.07580  0.00561  -0.05521 170 PHE A C   
1190 O O   . PHE A 163 ? 0.25701 0.29796 0.24521 0.09048  0.01266  -0.05724 170 PHE A O   
1191 C CB  . PHE A 163 ? 0.23233 0.26237 0.25211 0.04491  0.01191  -0.03668 170 PHE A CB  
1192 C CG  . PHE A 163 ? 0.23082 0.28326 0.25115 0.04474  0.02258  -0.03025 170 PHE A CG  
1193 C CD1 . PHE A 163 ? 0.22944 0.30672 0.26674 0.03985  0.03000  -0.02196 170 PHE A CD1 
1194 C CD2 . PHE A 163 ? 0.22523 0.27446 0.23118 0.04809  0.02441  -0.03063 170 PHE A CD2 
1195 C CE1 . PHE A 163 ? 0.23766 0.33558 0.27992 0.03700  0.04068  -0.01159 170 PHE A CE1 
1196 C CE2 . PHE A 163 ? 0.21686 0.28633 0.22287 0.04804  0.03523  -0.02062 170 PHE A CE2 
1197 C CZ  . PHE A 163 ? 0.23590 0.32927 0.26133 0.04153  0.04422  -0.00959 170 PHE A CZ  
1198 N N   . THR A 164 ? 0.25631 0.25062 0.24317 0.07235  -0.00447 -0.06172 171 THR A N   
1199 C CA  . THR A 164 ? 0.25434 0.24142 0.22182 0.08562  -0.00999 -0.07411 171 THR A CA  
1200 C C   . THR A 164 ? 0.24547 0.23161 0.20858 0.07560  -0.01067 -0.07097 171 THR A C   
1201 O O   . THR A 164 ? 0.26868 0.24923 0.24458 0.05871  -0.01122 -0.06262 171 THR A O   
1202 C CB  . THR A 164 ? 0.31003 0.26437 0.27230 0.09336  -0.02668 -0.08903 171 THR A CB  
1203 O OG1 . THR A 164 ? 0.33162 0.26412 0.30808 0.07503  -0.03541 -0.08427 171 THR A OG1 
1204 C CG2 . THR A 164 ? 0.31898 0.27029 0.28378 0.10708  -0.02741 -0.09263 171 THR A CG2 
1205 N N   . VAL A 165 ? 0.29143 0.28506 0.23465 0.08884  -0.01068 -0.07786 172 VAL A N   
1206 C CA  . VAL A 165 ? 0.32000 0.31245 0.25553 0.08376  -0.01396 -0.07670 172 VAL A CA  
1207 C C   . VAL A 165 ? 0.34429 0.32471 0.25822 0.10000  -0.02813 -0.09598 172 VAL A C   
1208 O O   . VAL A 165 ? 0.34391 0.33237 0.23946 0.12088  -0.02652 -0.10568 172 VAL A O   
1209 C CB  . VAL A 165 ? 0.30471 0.32375 0.23569 0.08373  0.00178  -0.06143 172 VAL A CB  
1210 C CG1 . VAL A 165 ? 0.33441 0.35094 0.25415 0.08248  -0.00331 -0.06069 172 VAL A CG1 
1211 C CG2 . VAL A 165 ? 0.29770 0.32407 0.25140 0.06684  0.01194  -0.04567 172 VAL A CG2 
1212 N N   . ARG A 166 ? 0.33978 0.30311 0.25629 0.09160  -0.04281 -0.10249 173 ARG A N   
1213 C CA  . ARG A 166 ? 0.36067 0.31269 0.25756 0.10542  -0.05990 -0.12271 173 ARG A CA  
1214 C C   . ARG A 166 ? 0.34712 0.30166 0.24558 0.09622  -0.06763 -0.12055 173 ARG A C   
1215 O O   . ARG A 166 ? 0.34838 0.30513 0.26803 0.07761  -0.06307 -0.10603 173 ARG A O   
1216 C CB  . ARG A 166 ? 0.44459 0.36440 0.35050 0.10448  -0.07897 -0.13871 173 ARG A CB  
1217 C CG  . ARG A 166 ? 0.46912 0.37061 0.40573 0.08187  -0.08346 -0.13003 173 ARG A CG  
1218 C CD  . ARG A 166 ? 0.65797 0.53292 0.61058 0.07230  -0.10432 -0.13791 173 ARG A CD  
1219 N NE  . ARG A 166 ? 0.84712 0.70939 0.82973 0.05083  -0.10514 -0.12508 173 ARG A NE  
1220 C CZ  . ARG A 166 ? 0.88784 0.75068 0.89223 0.03220  -0.11145 -0.11787 173 ARG A CZ  
1221 N NH1 . ARG A 166 ? 0.56906 0.44249 0.57001 0.03157  -0.11978 -0.12397 173 ARG A NH1 
1222 N NH2 . ARG A 166 ? 0.62232 0.48014 0.65302 0.01493  -0.10785 -0.10159 173 ARG A NH2 
1223 N N   . THR A 167 ? 0.39673 0.35233 0.27152 0.11159  -0.08034 -0.13628 174 THR A N   
1224 C CA  . THR A 167 ? 0.41149 0.36772 0.29088 0.10338  -0.09332 -0.13780 174 THR A CA  
1225 C C   . THR A 167 ? 0.49695 0.42930 0.40773 0.08352  -0.11044 -0.14335 174 THR A C   
1226 O O   . THR A 167 ? 0.50518 0.41772 0.42675 0.08182  -0.11749 -0.14950 174 THR A O   
1227 C CB  . THR A 167 ? 0.49461 0.45988 0.34953 0.12193  -0.10343 -0.14891 174 THR A CB  
1228 O OG1 . THR A 167 ? 0.66282 0.60937 0.52184 0.12715  -0.11854 -0.16440 174 THR A OG1 
1229 C CG2 . THR A 167 ? 0.46631 0.45792 0.29183 0.14193  -0.08484 -0.13955 174 THR A CG2 
1230 N N   . ASP A 168 ? 0.42219 0.36190 0.35465 0.06657  -0.11194 -0.13197 175 ASP A N   
1231 C CA  . ASP A 168 ? 0.45657 0.38138 0.42367 0.04585  -0.12434 -0.13108 175 ASP A CA  
1232 C C   . ASP A 168 ? 0.58887 0.51216 0.56192 0.04476  -0.14588 -0.14322 175 ASP A C   
1233 O O   . ASP A 168 ? 0.58894 0.53105 0.55774 0.04660  -0.14980 -0.14241 175 ASP A O   
1234 C CB  . ASP A 168 ? 0.41015 0.34975 0.40182 0.02868  -0.11015 -0.10828 175 ASP A CB  
1235 C CG  . ASP A 168 ? 0.53364 0.46309 0.56189 0.00821  -0.11901 -0.10300 175 ASP A CG  
1236 O OD1 . ASP A 168 ? 0.67012 0.57662 0.70688 0.00443  -0.12539 -0.10772 175 ASP A OD1 
1237 O OD2 . ASP A 168 ? 0.46030 0.40551 0.50954 -0.00303 -0.12068 -0.09379 175 ASP A OD2 
1238 N N   . THR A 169 ? 0.73808 0.64075 0.72261 0.04213  -0.15801 -0.15122 176 THR A N   
1239 C CA  . THR A 169 ? 0.91364 0.81192 0.91358 0.03626  -0.17760 -0.15951 176 THR A CA  
1240 C C   . THR A 169 ? 0.83101 0.73207 0.87285 0.01057  -0.18141 -0.14588 176 THR A C   
1241 O O   . THR A 169 ? 0.72856 0.63149 0.78791 0.00298  -0.19676 -0.15035 176 THR A O   
1242 C CB  . THR A 169 ? 0.97907 0.85208 0.97379 0.04493  -0.18956 -0.17377 176 THR A CB  
1243 O OG1 . THR A 169 ? 0.76412 0.61955 0.76789 0.03969  -0.18098 -0.16591 176 THR A OG1 
1244 C CG2 . THR A 169 ? 0.79231 0.67131 0.74702 0.07287  -0.18969 -0.18887 176 THR A CG2 
1245 N N   . GLY A 170 ? 0.77673 0.68087 0.83548 -0.00218 -0.16729 -0.12872 177 GLY A N   
1246 C CA  . GLY A 170 ? 0.74636 0.65987 0.84445 -0.02453 -0.16660 -0.11171 177 GLY A CA  
1247 C C   . GLY A 170 ? 0.64316 0.58567 0.75481 -0.02990 -0.17137 -0.10819 177 GLY A C   
1248 O O   . GLY A 170 ? 0.56066 0.51403 0.65021 -0.01621 -0.17783 -0.11987 177 GLY A O   
1249 N N   . GLU A 171 ? 0.61859 0.57698 0.76605 -0.04804 -0.16713 -0.09038 178 GLU A N   
1250 C CA  . GLU A 171 ? 0.61769 0.60850 0.78450 -0.05355 -0.17054 -0.08423 178 GLU A CA  
1251 C C   . GLU A 171 ? 0.42176 0.43255 0.56508 -0.03830 -0.16488 -0.08662 178 GLU A C   
1252 O O   . GLU A 171 ? 0.37437 0.38629 0.50595 -0.03391 -0.14579 -0.07627 178 GLU A O   
1253 C CB  . GLU A 171 ? 0.56788 0.57630 0.77310 -0.07181 -0.15936 -0.06064 178 GLU A CB  
1254 C CG  . GLU A 171 ? 0.49762 0.53580 0.73417 -0.08213 -0.16575 -0.05339 178 GLU A CG  
1255 C CD  . GLU A 171 ? 0.57111 0.59652 0.81250 -0.08553 -0.18716 -0.06862 178 GLU A CD  
1256 O OE1 . GLU A 171 ? 0.55863 0.60016 0.79368 -0.07833 -0.19880 -0.07966 178 GLU A OE1 
1257 O OE2 . GLU A 171 ? 0.53466 0.53288 0.78440 -0.09359 -0.19330 -0.07022 178 GLU A OE2 
1258 N N   . PRO A 172 ? 0.46236 0.48728 0.59231 -0.02735 -0.17605 -0.09682 179 PRO A N   
1259 C CA  . PRO A 172 ? 0.44191 0.48513 0.54636 -0.01041 -0.16732 -0.09397 179 PRO A CA  
1260 C C   . PRO A 172 ? 0.42707 0.49373 0.55181 -0.01596 -0.14832 -0.07161 179 PRO A C   
1261 O O   . PRO A 172 ? 0.54124 0.62945 0.70374 -0.02879 -0.15396 -0.06383 179 PRO A O   
1262 C CB  . PRO A 172 ? 0.53539 0.59231 0.63010 -0.00038 -0.18537 -0.10612 179 PRO A CB  
1263 C CG  . PRO A 172 ? 0.56152 0.59555 0.65774 -0.00543 -0.19929 -0.12068 179 PRO A CG  
1264 C CD  . PRO A 172 ? 0.59288 0.61378 0.72365 -0.02681 -0.19497 -0.11080 179 PRO A CD  
1265 N N   . MET A 173 ? 0.37569 0.43978 0.47638 -0.00548 -0.12635 -0.06152 180 MET A N   
1266 C CA  . MET A 173 ? 0.45934 0.54244 0.57535 -0.00735 -0.10989 -0.04384 180 MET A CA  
1267 C C   . MET A 173 ? 0.59262 0.69356 0.69626 0.00785  -0.10671 -0.03908 180 MET A C   
1268 O O   . MET A 173 ? 0.65483 0.77426 0.77439 0.00843  -0.09709 -0.02709 180 MET A O   
1269 C CB  . MET A 173 ? 0.42604 0.49457 0.53136 -0.00791 -0.08867 -0.03464 180 MET A CB  
1270 C CG  . MET A 173 ? 0.60189 0.64651 0.70447 -0.01559 -0.08798 -0.03909 180 MET A CG  
1271 S SD  . MET A 173 ? 0.52398 0.55449 0.59767 -0.00641 -0.06673 -0.03383 180 MET A SD  
1272 C CE  . MET A 173 ? 0.44509 0.49594 0.53557 -0.00791 -0.05349 -0.01868 180 MET A CE  
1273 N N   . GLY A 174 ? 0.37318 0.46926 0.44729 0.02229  -0.11325 -0.04681 181 GLY A N   
1274 C CA  . GLY A 174 ? 0.35405 0.46713 0.41959 0.03686  -0.11155 -0.03956 181 GLY A CA  
1275 C C   . GLY A 174 ? 0.31153 0.41010 0.35099 0.04787  -0.09188 -0.02859 181 GLY A C   
1276 O O   . GLY A 174 ? 0.35496 0.44764 0.36499 0.06192  -0.09138 -0.02758 181 GLY A O   
1277 N N   . ARG A 175 ? 0.23174 0.32502 0.28258 0.04150  -0.07626 -0.01974 182 ARG A N   
1278 C CA  . ARG A 175 ? 0.23717 0.31125 0.26814 0.04737  -0.05941 -0.01162 182 ARG A CA  
1279 C C   . ARG A 175 ? 0.21140 0.28091 0.25774 0.03762  -0.04756 -0.00788 182 ARG A C   
1280 O O   . ARG A 175 ? 0.24478 0.33254 0.31421 0.03445  -0.04773 -0.00495 182 ARG A O   
1281 C CB  . ARG A 175 ? 0.23687 0.31397 0.25762 0.06295  -0.05609 -0.00210 182 ARG A CB  
1282 C CG  . ARG A 175 ? 0.26357 0.31536 0.26534 0.06691  -0.04109 0.00669  182 ARG A CG  
1283 C CD  . ARG A 175 ? 0.26071 0.30866 0.26094 0.07952  -0.03662 0.01654  182 ARG A CD  
1284 N NE  . ARG A 175 ? 0.23637 0.29813 0.25911 0.07935  -0.03558 0.01481  182 ARG A NE  
1285 C CZ  . ARG A 175 ? 0.22382 0.31021 0.26028 0.08831  -0.04270 0.01572  182 ARG A CZ  
1286 N NH1 . ARG A 175 ? 0.24937 0.34926 0.27991 0.09811  -0.05416 0.01703  182 ARG A NH1 
1287 N NH2 . ARG A 175 ? 0.22116 0.32318 0.27780 0.08918  -0.03840 0.01559  182 ARG A NH2 
1288 N N   . GLY A 176 ? 0.34625 0.38344 0.24833 0.07311  -0.05119 0.08394  183 GLY A N   
1289 C CA  . GLY A 176 ? 0.29818 0.32623 0.24571 0.05954  -0.03624 0.07325  183 GLY A CA  
1290 C C   . GLY A 176 ? 0.29670 0.31492 0.23088 0.05152  -0.02785 0.05264  183 GLY A C   
1291 O O   . GLY A 176 ? 0.32082 0.33572 0.21132 0.06201  -0.02323 0.05078  183 GLY A O   
1292 N N   . THR A 177 ? 0.24794 0.26194 0.21570 0.03784  -0.02399 0.03904  184 THR A N   
1293 C CA  . THR A 177 ? 0.23636 0.24525 0.19908 0.03321  -0.01499 0.02487  184 THR A CA  
1294 C C   . THR A 177 ? 0.26689 0.27086 0.24776 0.02068  -0.02641 0.00601  184 THR A C   
1295 O O   . THR A 177 ? 0.23741 0.24602 0.25005 0.01304  -0.02851 0.00774  184 THR A O   
1296 C CB  . THR A 177 ? 0.25747 0.27023 0.24516 0.02648  0.00635  0.03802  184 THR A CB  
1297 O OG1 . THR A 177 ? 0.26887 0.28720 0.24367 0.03488  0.01857  0.06233  184 THR A OG1 
1298 C CG2 . THR A 177 ? 0.28256 0.30610 0.27355 0.02497  0.01486  0.03010  184 THR A CG2 
1299 N N   . LYS A 178 ? 0.25431 0.24584 0.21206 0.02222  -0.03011 -0.00944 185 LYS A N   
1300 C CA  . LYS A 178 ? 0.24309 0.22569 0.21686 0.01006  -0.03657 -0.02265 185 LYS A CA  
1301 C C   . LYS A 178 ? 0.24628 0.22970 0.22282 0.01569  -0.02050 -0.02394 185 LYS A C   
1302 O O   . LYS A 178 ? 0.28997 0.26939 0.23749 0.03345  -0.01182 -0.02408 185 LYS A O   
1303 C CB  . LYS A 178 ? 0.35192 0.30821 0.29296 0.00556  -0.05955 -0.03754 185 LYS A CB  
1304 C CG  . LYS A 178 ? 0.42089 0.38942 0.36569 -0.00523 -0.08349 -0.03255 185 LYS A CG  
1305 C CD  . LYS A 178 ? 0.57938 0.51900 0.49500 -0.02138 -0.11398 -0.04655 185 LYS A CD  
1306 C CE  . LYS A 178 ? 0.64765 0.53330 0.51276 -0.01206 -0.11024 -0.06607 185 LYS A CE  
1307 N NZ  . LYS A 178 ? 0.81464 0.65816 0.62742 -0.01971 -0.13485 -0.07956 185 LYS A NZ  
1308 N N   . VAL A 179 ? 0.22968 0.22124 0.23769 0.00391  -0.01650 -0.02331 186 VAL A N   
1309 C CA  . VAL A 179 ? 0.23155 0.23267 0.24761 0.00669  -0.00779 -0.02179 186 VAL A CA  
1310 C C   . VAL A 179 ? 0.24262 0.22396 0.25224 0.00417  -0.01676 -0.03228 186 VAL A C   
1311 O O   . VAL A 179 ? 0.23969 0.21868 0.26453 -0.01015 -0.02241 -0.03420 186 VAL A O   
1312 C CB  . VAL A 179 ? 0.19917 0.21842 0.24529 -0.00821 -0.00249 -0.01313 186 VAL A CB  
1313 C CG1 . VAL A 179 ? 0.20824 0.24820 0.26700 -0.00846 -0.00092 -0.00891 186 VAL A CG1 
1314 C CG2 . VAL A 179 ? 0.20154 0.23228 0.25407 -0.00955 0.00620  0.00182  186 VAL A CG2 
1315 N N   . ILE A 180 ? 0.26064 0.22389 0.24400 0.02106  -0.01558 -0.03676 187 ILE A N   
1316 C CA  . ILE A 180 ? 0.26877 0.19902 0.23886 0.01955  -0.02441 -0.04414 187 ILE A CA  
1317 C C   . ILE A 180 ? 0.22522 0.17375 0.20989 0.02976  -0.01535 -0.03485 187 ILE A C   
1318 O O   . ILE A 180 ? 0.25767 0.21894 0.23539 0.05433  -0.00361 -0.02831 187 ILE A O   
1319 C CB  . ILE A 180 ? 0.32256 0.20047 0.24086 0.03366  -0.03207 -0.05734 187 ILE A CB  
1320 C CG1 . ILE A 180 ? 0.37002 0.23864 0.27055 0.02265  -0.04662 -0.06461 187 ILE A CG1 
1321 C CG2 . ILE A 180 ? 0.37802 0.20710 0.28115 0.02667  -0.04344 -0.06267 187 ILE A CG2 
1322 C CD1 . ILE A 180 ? 0.46621 0.27427 0.29807 0.03650  -0.05787 -0.08201 187 ILE A CD1 
1323 N N   . LEU A 181 ? 0.22838 0.18300 0.23178 0.01410  -0.02009 -0.03134 188 LEU A N   
1324 C CA  . LEU A 181 ? 0.22943 0.20479 0.24431 0.02135  -0.01730 -0.02048 188 LEU A CA  
1325 C C   . LEU A 181 ? 0.29159 0.22454 0.28285 0.03276  -0.02060 -0.01991 188 LEU A C   
1326 O O   . LEU A 181 ? 0.30551 0.21254 0.29259 0.01539  -0.02785 -0.02134 188 LEU A O   
1327 C CB  . LEU A 181 ? 0.21737 0.21644 0.25146 -0.00004 -0.02140 -0.01746 188 LEU A CB  
1328 C CG  . LEU A 181 ? 0.22391 0.24139 0.27219 -0.01444 -0.01999 -0.02030 188 LEU A CG  
1329 C CD1 . LEU A 181 ? 0.26672 0.28413 0.31309 -0.03086 -0.02408 -0.02319 188 LEU A CD1 
1330 C CD2 . LEU A 181 ? 0.22517 0.27751 0.29065 -0.00990 -0.01674 -0.00977 188 LEU A CD2 
1331 N N   . HIS A 182 ? 0.30152 0.22822 0.27902 0.06362  -0.01319 -0.01374 189 HIS A N   
1332 C CA  . HIS A 182 ? 0.33082 0.20720 0.28133 0.08042  -0.01473 -0.01010 189 HIS A CA  
1333 C C   . HIS A 182 ? 0.31822 0.23515 0.29359 0.08047  -0.01642 0.00935  189 HIS A C   
1334 O O   . HIS A 182 ? 0.31296 0.27932 0.30815 0.10119  -0.01109 0.02439  189 HIS A O   
1335 C CB  . HIS A 182 ? 0.37501 0.21786 0.29006 0.12274  -0.00275 -0.01269 189 HIS A CB  
1336 C CG  . HIS A 182 ? 0.43392 0.24059 0.31320 0.12435  -0.00259 -0.03312 189 HIS A CG  
1337 N ND1 . HIS A 182 ? 0.58000 0.30415 0.40773 0.11897  -0.01410 -0.05075 189 HIS A ND1 
1338 C CD2 . HIS A 182 ? 0.41939 0.26490 0.30685 0.12370  0.00420  -0.03619 189 HIS A CD2 
1339 C CE1 . HIS A 182 ? 0.54617 0.26722 0.35089 0.11622  -0.01573 -0.06376 189 HIS A CE1 
1340 N NE2 . HIS A 182 ? 0.51042 0.29368 0.34332 0.12654  -0.00260 -0.05695 189 HIS A NE2 
1341 N N   . LEU A 183 ? 0.31843 0.22254 0.29408 0.05644  -0.02446 0.01218  190 LEU A N   
1342 C CA  . LEU A 183 ? 0.32938 0.27644 0.32019 0.05061  -0.02886 0.02735  190 LEU A CA  
1343 C C   . LEU A 183 ? 0.36565 0.31127 0.34883 0.08032  -0.02880 0.04838  190 LEU A C   
1344 O O   . LEU A 183 ? 0.38641 0.27278 0.34363 0.10046  -0.02454 0.05172  190 LEU A O   
1345 C CB  . LEU A 183 ? 0.30934 0.24224 0.29396 0.02328  -0.03154 0.02699  190 LEU A CB  
1346 C CG  . LEU A 183 ? 0.27319 0.22034 0.27006 -0.00008 -0.02971 0.01183  190 LEU A CG  
1347 C CD1 . LEU A 183 ? 0.32394 0.26415 0.31638 -0.01793 -0.02568 0.01793  190 LEU A CD1 
1348 C CD2 . LEU A 183 ? 0.29908 0.29051 0.30877 -0.00447 -0.03224 0.00664  190 LEU A CD2 
1349 N N   . LYS A 184 ? 0.31842 0.32689 0.32198 0.08289  -0.03620 0.06380  191 LYS A N   
1350 C CA  . LYS A 184 ? 0.32083 0.34237 0.32152 0.10950  -0.04008 0.08989  191 LYS A CA  
1351 C C   . LYS A 184 ? 0.40504 0.37396 0.37388 0.10206  -0.04174 0.09804  191 LYS A C   
1352 O O   . LYS A 184 ? 0.39164 0.34619 0.35090 0.07120  -0.04232 0.08770  191 LYS A O   
1353 C CB  . LYS A 184 ? 0.31723 0.42398 0.34649 0.10162  -0.05640 0.10471  191 LYS A CB  
1354 C CG  . LYS A 184 ? 0.34468 0.51765 0.41747 0.10369  -0.05580 0.10700  191 LYS A CG  
1355 C CD  . LYS A 184 ? 0.34215 0.59116 0.44158 0.07501  -0.08148 0.11740  191 LYS A CD  
1356 C CE  . LYS A 184 ? 0.40186 0.71266 0.54904 0.06529  -0.08037 0.12282  191 LYS A CE  
1357 N NZ  . LYS A 184 ? 0.38489 0.74279 0.54988 0.02993  -0.10354 0.12775  191 LYS A NZ  
1358 N N   . GLU A 185 ? 0.46008 0.39999 0.41315 0.13381  -0.03937 0.12052  192 GLU A N   
1359 C CA  . GLU A 185 ? 0.51626 0.39693 0.43838 0.12758  -0.03861 0.13463  192 GLU A CA  
1360 C C   . GLU A 185 ? 0.52323 0.44193 0.43932 0.10148  -0.04645 0.14349  192 GLU A C   
1361 O O   . GLU A 185 ? 0.58168 0.46265 0.47874 0.08195  -0.04070 0.14925  192 GLU A O   
1362 C CB  . GLU A 185 ? 0.65179 0.49844 0.55699 0.17134  -0.03552 0.16207  192 GLU A CB  
1363 C CG  . GLU A 185 ? 0.92638 0.70459 0.80249 0.16101  -0.03413 0.17778  192 GLU A CG  
1364 C CD  . GLU A 185 ? 1.19353 0.96119 1.06522 0.19244  -0.03360 0.19647  192 GLU A CD  
1365 O OE1 . GLU A 185 ? 1.05632 0.85180 0.94374 0.22409  -0.02885 0.19212  192 GLU A OE1 
1366 O OE2 . GLU A 185 ? 1.20696 0.94239 1.05991 0.18645  -0.03587 0.21818  192 GLU A OE2 
1367 N N   . ASP A 186 ? 0.45011 0.44202 0.37858 0.10010  -0.05987 0.14622  193 ASP A N   
1368 C CA  . ASP A 186 ? 0.42862 0.44681 0.33297 0.08041  -0.06932 0.15138  193 ASP A CA  
1369 C C   . ASP A 186 ? 0.38053 0.41172 0.28370 0.04800  -0.06865 0.12149  193 ASP A C   
1370 O O   . ASP A 186 ? 0.43843 0.48855 0.31153 0.03468  -0.07699 0.11907  193 ASP A O   
1371 C CB  . ASP A 186 ? 0.48875 0.56940 0.39403 0.09527  -0.09159 0.17304  193 ASP A CB  
1372 C CG  . ASP A 186 ? 0.42350 0.57057 0.36847 0.08853  -0.10719 0.16233  193 ASP A CG  
1373 O OD1 . ASP A 186 ? 0.49495 0.63642 0.46828 0.08468  -0.09605 0.14345  193 ASP A OD1 
1374 O OD2 . ASP A 186 ? 0.53995 0.73849 0.48981 0.08387  -0.12863 0.17031  193 ASP A OD2 
1375 N N   . GLN A 187 ? 0.40107 0.41526 0.32747 0.03852  -0.05856 0.09924  194 GLN A N   
1376 C CA  . GLN A 187 ? 0.33298 0.35460 0.26031 0.01410  -0.05596 0.07362  194 GLN A CA  
1377 C C   . GLN A 187 ? 0.32151 0.30484 0.25020 0.00282  -0.03774 0.06619  194 GLN A C   
1378 O O   . GLN A 187 ? 0.34941 0.33489 0.29051 -0.00949 -0.03272 0.04675  194 GLN A O   
1379 C CB  . GLN A 187 ? 0.30647 0.35776 0.26595 0.01091  -0.06321 0.05898  194 GLN A CB  
1380 C CG  . GLN A 187 ? 0.29867 0.40543 0.27026 0.01506  -0.08446 0.07211  194 GLN A CG  
1381 C CD  . GLN A 187 ? 0.39290 0.51491 0.32925 -0.00356 -0.10344 0.06947  194 GLN A CD  
1382 O OE1 . GLN A 187 ? 0.41779 0.51385 0.32563 -0.02175 -0.09959 0.04831  194 GLN A OE1 
1383 N NE2 . GLN A 187 ? 0.36538 0.52894 0.29933 0.00367  -0.12509 0.09102  194 GLN A NE2 
1384 N N   . THR A 188 ? 0.40008 0.35143 0.31937 0.00495  -0.02925 0.08533  195 THR A N   
1385 C CA  . THR A 188 ? 0.41031 0.33630 0.34304 -0.01201 -0.01684 0.08366  195 THR A CA  
1386 C C   . THR A 188 ? 0.40217 0.35084 0.32785 -0.02416 -0.00253 0.08338  195 THR A C   
1387 O O   . THR A 188 ? 0.41521 0.36134 0.36324 -0.03826 0.00829  0.08703  195 THR A O   
1388 C CB  . THR A 188 ? 0.47948 0.35839 0.40775 -0.01316 -0.01470 0.10760  195 THR A CB  
1389 O OG1 . THR A 188 ? 0.54521 0.42834 0.44731 -0.00683 -0.01004 0.13492  195 THR A OG1 
1390 C CG2 . THR A 188 ? 0.50825 0.34819 0.43495 0.00626  -0.02457 0.10282  195 THR A CG2 
1391 N N   . GLU A 189 ? 0.38344 0.35400 0.27604 -0.01767 -0.00264 0.08041  196 GLU A N   
1392 C CA  . GLU A 189 ? 0.38553 0.36876 0.25908 -0.01998 0.01560  0.07572  196 GLU A CA  
1393 C C   . GLU A 189 ? 0.40111 0.38910 0.30294 -0.02577 0.02112  0.05387  196 GLU A C   
1394 O O   . GLU A 189 ? 0.37594 0.37501 0.28081 -0.02422 0.04198  0.05705  196 GLU A O   
1395 C CB  . GLU A 189 ? 0.44544 0.43514 0.26150 -0.01146 0.00905  0.06667  196 GLU A CB  
1396 C CG  . GLU A 189 ? 0.43957 0.43252 0.25349 -0.01657 -0.01456 0.03930  196 GLU A CG  
1397 C CD  . GLU A 189 ? 0.51977 0.51491 0.27430 -0.01572 -0.03239 0.03343  196 GLU A CD  
1398 O OE1 . GLU A 189 ? 0.59396 0.60611 0.34341 -0.01186 -0.05089 0.05161  196 GLU A OE1 
1399 O OE2 . GLU A 189 ? 0.54490 0.52078 0.24985 -0.01644 -0.02882 0.01229  196 GLU A OE2 
1400 N N   . TYR A 190 ? 0.33536 0.31985 0.25830 -0.02867 0.00510  0.03608  197 TYR A N   
1401 C CA  . TYR A 190 ? 0.27781 0.26464 0.22321 -0.03243 0.00785  0.01752  197 TYR A CA  
1402 C C   . TYR A 190 ? 0.32009 0.30761 0.30516 -0.04021 0.01302  0.02579  197 TYR A C   
1403 O O   . TYR A 190 ? 0.31942 0.31202 0.32488 -0.04186 0.01306  0.01439  197 TYR A O   
1404 C CB  . TYR A 190 ? 0.29421 0.28197 0.24496 -0.03391 -0.00993 0.00093  197 TYR A CB  
1405 C CG  . TYR A 190 ? 0.31681 0.30786 0.23134 -0.03529 -0.02168 -0.00602 197 TYR A CG  
1406 C CD1 . TYR A 190 ? 0.32692 0.30174 0.20262 -0.03583 -0.01548 -0.02060 197 TYR A CD1 
1407 C CD2 . TYR A 190 ? 0.33346 0.34170 0.24671 -0.03438 -0.04050 0.00321  197 TYR A CD2 
1408 C CE1 . TYR A 190 ? 0.39488 0.36118 0.22381 -0.04157 -0.03211 -0.03033 197 TYR A CE1 
1409 C CE2 . TYR A 190 ? 0.35527 0.37202 0.23492 -0.04132 -0.05866 -0.00115 197 TYR A CE2 
1410 C CZ  . TYR A 190 ? 0.36016 0.35069 0.19190 -0.04817 -0.05698 -0.02048 197 TYR A CZ  
1411 O OH  . TYR A 190 ? 0.42903 0.41451 0.21216 -0.05917 -0.08028 -0.02952 197 TYR A OH  
1412 N N   . LEU A 191 ? 0.30262 0.28281 0.29658 -0.04750 0.01460  0.04713  198 LEU A N   
1413 C CA  . LEU A 191 ? 0.30036 0.28275 0.33066 -0.06400 0.01531  0.05914  198 LEU A CA  
1414 C C   . LEU A 191 ? 0.30939 0.32537 0.35538 -0.06881 0.03670  0.08350  198 LEU A C   
1415 O O   . LEU A 191 ? 0.35248 0.38661 0.43984 -0.08707 0.03611  0.09963  198 LEU A O   
1416 C CB  . LEU A 191 ? 0.37016 0.31143 0.40031 -0.07515 0.00035  0.06908  198 LEU A CB  
1417 C CG  . LEU A 191 ? 0.33279 0.24332 0.34583 -0.06157 -0.01479 0.04870  198 LEU A CG  
1418 C CD1 . LEU A 191 ? 0.46461 0.31897 0.46153 -0.06209 -0.02524 0.05741  198 LEU A CD1 
1419 C CD2 . LEU A 191 ? 0.37821 0.29710 0.40584 -0.06273 -0.02136 0.02742  198 LEU A CD2 
1420 N N   . GLU A 192 ? 0.31508 0.34224 0.32770 -0.05370 0.05478  0.09034  199 GLU A N   
1421 C CA  . GLU A 192 ? 0.30202 0.36534 0.32433 -0.05163 0.08222  0.11871  199 GLU A CA  
1422 C C   . GLU A 192 ? 0.32598 0.42123 0.35708 -0.03355 0.10224  0.10993  199 GLU A C   
1423 O O   . GLU A 192 ? 0.31211 0.38685 0.30747 -0.01611 0.10062  0.08034  199 GLU A O   
1424 C CB  . GLU A 192 ? 0.41729 0.47337 0.38650 -0.03843 0.09496  0.13172  199 GLU A CB  
1425 C CG  . GLU A 192 ? 0.52195 0.54589 0.48521 -0.05148 0.07772  0.14820  199 GLU A CG  
1426 C CD  . GLU A 192 ? 0.87442 0.88915 0.77812 -0.03502 0.08201  0.15780  199 GLU A CD  
1427 O OE1 . GLU A 192 ? 0.98932 0.97639 0.88332 -0.03829 0.06828  0.17294  199 GLU A OE1 
1428 O OE2 . GLU A 192 ? 0.99046 1.02126 0.85096 -0.01643 0.09881  0.15100  199 GLU A OE2 
1429 N N   . GLU A 193 ? 0.30485 0.31942 0.36699 -0.03183 0.01764  0.09165  200 GLU A N   
1430 C CA  . GLU A 193 ? 0.30713 0.35153 0.37755 -0.03621 0.01935  0.07776  200 GLU A CA  
1431 C C   . GLU A 193 ? 0.26934 0.34837 0.32384 -0.02493 0.02556  0.07627  200 GLU A C   
1432 O O   . GLU A 193 ? 0.27749 0.36546 0.32522 -0.01907 0.02326  0.05754  200 GLU A O   
1433 C CB  . GLU A 193 ? 0.31528 0.37038 0.40804 -0.05477 0.02307  0.08796  200 GLU A CB  
1434 C CG  . GLU A 193 ? 0.32843 0.41834 0.43033 -0.05385 0.02557  0.07573  200 GLU A CG  
1435 C CD  . GLU A 193 ? 0.60278 0.71765 0.73198 -0.07172 0.02857  0.08740  200 GLU A CD  
1436 O OE1 . GLU A 193 ? 0.46868 0.57995 0.60882 -0.08746 0.03173  0.10906  200 GLU A OE1 
1437 O OE2 . GLU A 193 ? 0.49111 0.63161 0.63161 -0.07018 0.02780  0.07693  200 GLU A OE2 
1438 N N   . ARG A 194 ? 0.32755 0.42289 0.37255 -0.02173 0.03320  0.09585  201 ARG A N   
1439 C CA  . ARG A 194 ? 0.26551 0.39280 0.28953 -0.01033 0.03839  0.09168  201 ARG A CA  
1440 C C   . ARG A 194 ? 0.27593 0.39924 0.28073 -0.00090 0.02876  0.07490  201 ARG A C   
1441 O O   . ARG A 194 ? 0.28836 0.42434 0.27621 0.00428  0.02786  0.05859  201 ARG A O   
1442 C CB  . ARG A 194 ? 0.33232 0.48170 0.34596 -0.00683 0.04856  0.11740  201 ARG A CB  
1443 C CG  . ARG A 194 ? 0.37631 0.50665 0.38565 -0.00480 0.04595  0.13758  201 ARG A CG  
1444 C CD  . ARG A 194 ? 0.45102 0.60581 0.45098 -0.00237 0.05837  0.16726  201 ARG A CD  
1445 N NE  . ARG A 194 ? 0.59672 0.74125 0.58134 0.00793  0.05606  0.18666  201 ARG A NE  
1446 C CZ  . ARG A 194 ? 0.48434 0.65078 0.45373 0.01462  0.06561  0.21415  201 ARG A CZ  
1447 N NH1 . ARG A 194 ? 0.57364 0.77395 0.54288 0.01085  0.07934  0.22614  201 ARG A NH1 
1448 N NH2 . ARG A 194 ? 0.56505 0.72290 0.51888 0.02770  0.06234  0.23223  201 ARG A NH2 
1449 N N   . ARG A 195 ? 0.27571 0.38171 0.28229 0.00150  0.02139  0.07910  202 ARG A N   
1450 C CA  . ARG A 195 ? 0.25749 0.37083 0.25204 0.00792  0.01185  0.06646  202 ARG A CA  
1451 C C   . ARG A 195 ? 0.25772 0.36086 0.25930 0.00244  0.00657  0.04372  202 ARG A C   
1452 O O   . ARG A 195 ? 0.25517 0.36834 0.24424 0.00131  0.00147  0.02911  202 ARG A O   
1453 C CB  . ARG A 195 ? 0.28565 0.39086 0.28246 0.01667  0.00723  0.07985  202 ARG A CB  
1454 C CG  . ARG A 195 ? 0.25785 0.38522 0.24767 0.02353  -0.00287 0.07268  202 ARG A CG  
1455 C CD  . ARG A 195 ? 0.29280 0.45539 0.26072 0.02557  -0.00650 0.07345  202 ARG A CD  
1456 N NE  . ARG A 195 ? 0.28468 0.47480 0.25094 0.02959  -0.01804 0.07140  202 ARG A NE  
1457 C CZ  . ARG A 195 ? 0.32063 0.53192 0.27923 0.01919  -0.02816 0.05367  202 ARG A CZ  
1458 N NH1 . ARG A 195 ? 0.30493 0.50591 0.24997 0.00810  -0.02778 0.03505  202 ARG A NH1 
1459 N NH2 . ARG A 195 ? 0.32583 0.56904 0.29045 0.01999  -0.03912 0.05527  202 ARG A NH2 
1460 N N   . ILE A 196 ? 0.24360 0.32480 0.26289 -0.00206 0.00689  0.04079  203 ILE A N   
1461 C CA  . ILE A 196 ? 0.22415 0.29743 0.24831 -0.00539 0.00298  0.02246  203 ILE A CA  
1462 C C   . ILE A 196 ? 0.22332 0.30408 0.23911 -0.00702 0.00668  0.01144  203 ILE A C   
1463 O O   . ILE A 196 ? 0.24703 0.32479 0.25284 -0.00791 0.00274  -0.00251 203 ILE A O   
1464 C CB  . ILE A 196 ? 0.22909 0.28031 0.26944 -0.00839 0.00192  0.02104  203 ILE A CB  
1465 C CG1 . ILE A 196 ? 0.26643 0.30181 0.30763 -0.00138 -0.00143 0.02861  203 ILE A CG1 
1466 C CG2 . ILE A 196 ? 0.22072 0.26828 0.26326 -0.00965 -0.00104 0.00494  203 ILE A CG2 
1467 C CD1 . ILE A 196 ? 0.30466 0.30818 0.35505 -0.00546 -0.00295 0.02861  203 ILE A CD1 
1468 N N   . LYS A 197 ? 0.23733 0.32765 0.25612 -0.00671 0.01493  0.01891  204 LYS A N   
1469 C CA  . LYS A 197 ? 0.22380 0.32310 0.23199 -0.00141 0.02070  0.00939  204 LYS A CA  
1470 C C   . LYS A 197 ? 0.26425 0.36542 0.24290 0.00383  0.01834  -0.00132 204 LYS A C   
1471 O O   . LYS A 197 ? 0.28932 0.37795 0.25274 0.00742  0.01760  -0.01765 204 LYS A O   
1472 C CB  . LYS A 197 ? 0.27141 0.39415 0.28761 0.00071  0.03194  0.02336  204 LYS A CB  
1473 C CG  . LYS A 197 ? 0.29725 0.42318 0.34236 -0.00761 0.03292  0.02978  204 LYS A CG  
1474 C CD  . LYS A 197 ? 0.35568 0.51621 0.41192 -0.00814 0.04482  0.04732  204 LYS A CD  
1475 C CE  . LYS A 197 ? 0.56847 0.73823 0.65794 -0.02263 0.04297  0.05534  204 LYS A CE  
1476 N NZ  . LYS A 197 ? 0.58767 0.78849 0.69501 -0.03326 0.05237  0.08047  204 LYS A NZ  
1477 N N   . GLU A 198 ? 0.25603 0.37122 0.22334 0.00486  0.01680  0.00809  205 GLU A N   
1478 C CA  . GLU A 198 ? 0.25577 0.37671 0.19214 0.00780  0.01162  -0.00332 205 GLU A CA  
1479 C C   . GLU A 198 ? 0.25845 0.36240 0.19151 -0.00176 -0.00066 -0.02002 205 GLU A C   
1480 O O   . GLU A 198 ? 0.31810 0.40884 0.22687 -0.00356 -0.00505 -0.03815 205 GLU A O   
1481 C CB  . GLU A 198 ? 0.25800 0.40262 0.18580 0.01092  0.01008  0.01304  205 GLU A CB  
1482 C CG  . GLU A 198 ? 0.33142 0.48866 0.22773 0.01130  -0.00025 0.00150  205 GLU A CG  
1483 C CD  . GLU A 198 ? 0.31717 0.50286 0.20808 0.01676  -0.00292 0.02138  205 GLU A CD  
1484 O OE1 . GLU A 198 ? 0.34546 0.53194 0.25926 0.01598  -0.00539 0.03664  205 GLU A OE1 
1485 O OE2 . GLU A 198 ? 0.34529 0.55134 0.20589 0.02429  -0.00287 0.02115  205 GLU A OE2 
1486 N N   . ILE A 199 ? 0.24034 0.34399 0.19566 -0.00794 -0.00610 -0.01327 206 ILE A N   
1487 C CA  . ILE A 199 ? 0.24979 0.34791 0.20702 -0.01858 -0.01641 -0.02353 206 ILE A CA  
1488 C C   . ILE A 199 ? 0.25761 0.32706 0.21443 -0.02236 -0.01452 -0.03699 206 ILE A C   
1489 O O   . ILE A 199 ? 0.30346 0.35908 0.24736 -0.03249 -0.02141 -0.04963 206 ILE A O   
1490 C CB  . ILE A 199 ? 0.25024 0.36058 0.23102 -0.01804 -0.01926 -0.01054 206 ILE A CB  
1491 C CG1 . ILE A 199 ? 0.26363 0.40047 0.24077 -0.01073 -0.02161 0.00449  206 ILE A CG1 
1492 C CG2 . ILE A 199 ? 0.27381 0.38662 0.26258 -0.02877 -0.02687 -0.01710 206 ILE A CG2 
1493 C CD1 . ILE A 199 ? 0.29342 0.43298 0.29072 -0.00177 -0.02057 0.01928  206 ILE A CD1 
1494 N N   . VAL A 200 ? 0.25789 0.31778 0.22921 -0.01557 -0.00632 -0.03311 207 VAL A N   
1495 C CA  . VAL A 200 ? 0.25549 0.29135 0.22500 -0.01477 -0.00404 -0.04302 207 VAL A CA  
1496 C C   . VAL A 200 ? 0.29691 0.31537 0.23725 -0.00922 -0.00166 -0.05644 207 VAL A C   
1497 O O   . VAL A 200 ? 0.34779 0.33686 0.27335 -0.01319 -0.00488 -0.06821 207 VAL A O   
1498 C CB  . VAL A 200 ? 0.26057 0.29926 0.25045 -0.00756 0.00262  -0.03569 207 VAL A CB  
1499 C CG1 . VAL A 200 ? 0.30402 0.32400 0.28894 -0.00089 0.00607  -0.04377 207 VAL A CG1 
1500 C CG2 . VAL A 200 ? 0.26097 0.30430 0.27112 -0.01192 -0.00137 -0.02800 207 VAL A CG2 
1501 N N   . LYS A 201 ? 0.28629 0.31975 0.21416 0.00091  0.00442  -0.05454 208 LYS A N   
1502 C CA  . LYS A 201 ? 0.33225 0.34816 0.22646 0.01176  0.00804  -0.06928 208 LYS A CA  
1503 C C   . LYS A 201 ? 0.37760 0.37343 0.24256 -0.00048 -0.00437 -0.08544 208 LYS A C   
1504 O O   . LYS A 201 ? 0.48373 0.44144 0.31966 0.00185  -0.00610 -0.10309 208 LYS A O   
1505 C CB  . LYS A 201 ? 0.31788 0.36309 0.20494 0.02685  0.01896  -0.06111 208 LYS A CB  
1506 C CG  . LYS A 201 ? 0.47115 0.50289 0.31994 0.04574  0.02601  -0.07618 208 LYS A CG  
1507 C CD  . LYS A 201 ? 0.54775 0.61931 0.38956 0.05965  0.03751  -0.06425 208 LYS A CD  
1508 C CE  . LYS A 201 ? 0.63934 0.70142 0.43805 0.08408  0.04644  -0.08003 208 LYS A CE  
1509 N NZ  . LYS A 201 ? 0.72616 0.83710 0.52194 0.09959  0.06118  -0.06348 208 LYS A NZ  
1510 N N   . LYS A 202 ? 0.37443 0.39504 0.24577 -0.01364 -0.01403 -0.07939 209 LYS A N   
1511 C CA  . LYS A 202 ? 0.42232 0.43597 0.26924 -0.02910 -0.02881 -0.09357 209 LYS A CA  
1512 C C   . LYS A 202 ? 0.37462 0.36011 0.22755 -0.04953 -0.03825 -0.10124 209 LYS A C   
1513 O O   . LYS A 202 ? 0.43936 0.39315 0.26313 -0.06196 -0.04804 -0.11975 209 LYS A O   
1514 C CB  . LYS A 202 ? 0.36949 0.42807 0.22660 -0.03484 -0.03647 -0.08074 209 LYS A CB  
1515 C CG  . LYS A 202 ? 0.41984 0.48533 0.25498 -0.05241 -0.05438 -0.09378 209 LYS A CG  
1516 C CD  . LYS A 202 ? 0.59634 0.71399 0.44904 -0.05512 -0.06187 -0.07638 209 LYS A CD  
1517 C CE  . LYS A 202 ? 0.69870 0.84091 0.54377 -0.03366 -0.05190 -0.06197 209 LYS A CE  
1518 N NZ  . LYS A 202 ? 0.72099 0.86839 0.59979 -0.02181 -0.03785 -0.03930 209 LYS A NZ  
1519 N N   . HIS A 203 ? 0.38195 0.37744 0.27017 -0.05413 -0.03572 -0.08696 210 HIS A N   
1520 C CA  . HIS A 203 ? 0.42836 0.41354 0.32791 -0.07564 -0.04416 -0.08726 210 HIS A CA  
1521 C C   . HIS A 203 ? 0.40686 0.36100 0.31602 -0.07214 -0.03616 -0.08446 210 HIS A C   
1522 O O   . HIS A 203 ? 0.42641 0.36248 0.33757 -0.09055 -0.04167 -0.08498 210 HIS A O   
1523 C CB  . HIS A 203 ? 0.38676 0.42114 0.31757 -0.08406 -0.04946 -0.07083 210 HIS A CB  
1524 C CG  . HIS A 203 ? 0.41652 0.48660 0.33953 -0.09100 -0.06090 -0.07124 210 HIS A CG  
1525 N ND1 . HIS A 203 ? 0.43904 0.50277 0.33946 -0.11191 -0.07576 -0.08618 210 HIS A ND1 
1526 C CD2 . HIS A 203 ? 0.47641 0.58891 0.40999 -0.07980 -0.06087 -0.05771 210 HIS A CD2 
1527 C CE1 . HIS A 203 ? 0.51093 0.61720 0.41003 -0.11117 -0.08427 -0.08139 210 HIS A CE1 
1528 N NE2 . HIS A 203 ? 0.50322 0.64068 0.42115 -0.09161 -0.07528 -0.06351 210 HIS A NE2 
1529 N N   . SER A 204 ? 0.37021 0.32061 0.28528 -0.05062 -0.02407 -0.08004 211 SER A N   
1530 C CA  . SER A 204 ? 0.38981 0.32198 0.31631 -0.04418 -0.01737 -0.07463 211 SER A CA  
1531 C C   . SER A 204 ? 0.38306 0.28870 0.29190 -0.02293 -0.00814 -0.08132 211 SER A C   
1532 O O   . SER A 204 ? 0.39166 0.29899 0.31382 -0.01021 -0.00135 -0.07413 211 SER A O   
1533 C CB  . SER A 204 ? 0.35310 0.31934 0.31172 -0.03924 -0.01397 -0.05975 211 SER A CB  
1534 O OG  . SER A 204 ? 0.34454 0.33665 0.31745 -0.05348 -0.02086 -0.05287 211 SER A OG  
1535 N N   . GLN A 205 ? 0.46469 0.34864 0.34163 -0.01693 -0.00819 -0.09547 212 GLN A N   
1536 C CA  . GLN A 205 ? 0.54769 0.41913 0.40880 0.00993  0.00305  -0.09998 212 GLN A CA  
1537 C C   . GLN A 205 ? 0.52726 0.35103 0.37412 0.01972  0.00663  -0.10343 212 GLN A C   
1538 O O   . GLN A 205 ? 0.64390 0.46784 0.48764 0.04597  0.01707  -0.10148 212 GLN A O   
1539 C CB  . GLN A 205 ? 0.57806 0.44395 0.40459 0.01890  0.00375  -0.11433 212 GLN A CB  
1540 C CG  . GLN A 205 ? 0.62129 0.43336 0.40751 0.00758  -0.00605 -0.13482 212 GLN A CG  
1541 C CD  . GLN A 205 ? 0.91256 0.73994 0.69692 -0.02130 -0.02184 -0.13948 212 GLN A CD  
1542 O OE1 . GLN A 205 ? 0.62524 0.48447 0.44314 -0.04079 -0.02812 -0.12578 212 GLN A OE1 
1543 N NE2 . GLN A 205 ? 0.78233 0.59775 0.53429 -0.02113 -0.02773 -0.15663 212 GLN A NE2 
1544 N N   . PHE A 206 ? 0.48121 0.26831 0.32158 -0.00027 -0.00122 -0.10531 213 PHE A N   
1545 C CA  . PHE A 206 ? 0.55309 0.28722 0.37657 0.00839  0.00242  -0.10545 213 PHE A CA  
1546 C C   . PHE A 206 ? 0.55529 0.30082 0.40726 0.00133  0.00325  -0.08699 213 PHE A C   
1547 O O   . PHE A 206 ? 0.67686 0.37724 0.51490 0.00362  0.00516  -0.08320 213 PHE A O   
1548 C CB  . PHE A 206 ? 0.62717 0.31400 0.42608 -0.00822 -0.00585 -0.11670 213 PHE A CB  
1549 C CG  . PHE A 206 ? 0.66748 0.34890 0.44064 0.00302  -0.00604 -0.13383 213 PHE A CG  
1550 C CD1 . PHE A 206 ? 0.74331 0.41857 0.50117 0.03689  0.00586  -0.13697 213 PHE A CD1 
1551 C CD2 . PHE A 206 ? 0.72560 0.41452 0.49071 -0.01904 -0.01797 -0.14543 213 PHE A CD2 
1552 C CE1 . PHE A 206 ? 0.78256 0.45466 0.51429 0.04870  0.00738  -0.15198 213 PHE A CE1 
1553 C CE2 . PHE A 206 ? 0.82932 0.51348 0.56676 -0.00732 -0.01780 -0.16211 213 PHE A CE2 
1554 C CZ  . PHE A 206 ? 0.75519 0.42925 0.47469 0.02668  -0.00423 -0.16549 213 PHE A CZ  
1555 N N   . ILE A 207 ? 0.41446 0.21548 0.30176 -0.00477 0.00241  -0.07529 214 ILE A N   
1556 C CA  . ILE A 207 ? 0.37460 0.19054 0.28420 -0.00675 0.00382  -0.05969 214 ILE A CA  
1557 C C   . ILE A 207 ? 0.45115 0.26004 0.35778 0.02098  0.01179  -0.05421 214 ILE A C   
1558 O O   . ILE A 207 ? 0.43501 0.26517 0.34465 0.04102  0.01644  -0.05715 214 ILE A O   
1559 C CB  . ILE A 207 ? 0.34540 0.21703 0.28623 -0.01349 0.00128  -0.05272 214 ILE A CB  
1560 C CG1 . ILE A 207 ? 0.34416 0.22810 0.28956 -0.03829 -0.00665 -0.05400 214 ILE A CG1 
1561 C CG2 . ILE A 207 ? 0.34144 0.23276 0.30068 -0.00839 0.00338  -0.03994 214 ILE A CG2 
1562 C CD1 . ILE A 207 ? 0.39313 0.26582 0.34112 -0.05864 -0.00984 -0.04572 214 ILE A CD1 
1563 N N   . GLY A 208 ? 0.41376 0.19851 0.31579 0.02239  0.01356  -0.04364 215 GLY A N   
1564 C CA  . GLY A 208 ? 0.42765 0.19995 0.32087 0.05092  0.02027  -0.03720 215 GLY A CA  
1565 C C   . GLY A 208 ? 0.36724 0.19116 0.28590 0.06317  0.02065  -0.02657 215 GLY A C   
1566 O O   . GLY A 208 ? 0.44380 0.26258 0.35752 0.08144  0.02377  -0.01600 215 GLY A O   
1567 N N   . TYR A 209 ? 0.32930 0.20002 0.27223 0.05378  0.01656  -0.02946 216 TYR A N   
1568 C CA  . TYR A 209 ? 0.31524 0.23156 0.28007 0.06100  0.01388  -0.02401 216 TYR A CA  
1569 C C   . TYR A 209 ? 0.32510 0.27590 0.30720 0.05927  0.01228  -0.03089 216 TYR A C   
1570 O O   . TYR A 209 ? 0.32455 0.27072 0.30509 0.04726  0.01218  -0.03726 216 TYR A O   
1571 C CB  . TYR A 209 ? 0.28744 0.21763 0.26187 0.04640  0.00975  -0.01852 216 TYR A CB  
1572 C CG  . TYR A 209 ? 0.31268 0.21456 0.27210 0.04577  0.01298  -0.00713 216 TYR A CG  
1573 C CD1 . TYR A 209 ? 0.31548 0.22098 0.26888 0.06392  0.01461  0.00346  216 TYR A CD1 
1574 C CD2 . TYR A 209 ? 0.32624 0.20054 0.27796 0.02528  0.01388  -0.00457 216 TYR A CD2 
1575 C CE1 . TYR A 209 ? 0.34215 0.21969 0.28019 0.06391  0.01906  0.01784  216 TYR A CE1 
1576 C CE2 . TYR A 209 ? 0.32953 0.17644 0.26895 0.02090  0.01756  0.00939  216 TYR A CE2 
1577 C CZ  . TYR A 209 ? 0.33258 0.17896 0.26415 0.04114  0.02122  0.02195  216 TYR A CZ  
1578 O OH  . TYR A 209 ? 0.38166 0.19916 0.29910 0.03868  0.02636  0.03997  216 TYR A OH  
1579 N N   . PRO A 210 ? 0.27811 0.26623 0.27734 0.06897  0.01019  -0.02819 217 PRO A N   
1580 C CA  . PRO A 210 ? 0.23684 0.25797 0.25526 0.06283  0.00891  -0.03101 217 PRO A CA  
1581 C C   . PRO A 210 ? 0.26251 0.28768 0.29094 0.04224  0.00344  -0.03377 217 PRO A C   
1582 O O   . PRO A 210 ? 0.25929 0.28618 0.29110 0.03668  -0.00217 -0.03350 217 PRO A O   
1583 C CB  . PRO A 210 ? 0.26373 0.32526 0.30035 0.07291  0.00505  -0.02599 217 PRO A CB  
1584 C CG  . PRO A 210 ? 0.33429 0.38753 0.36176 0.08154  0.00165  -0.02217 217 PRO A CG  
1585 C CD  . PRO A 210 ? 0.30105 0.30504 0.30253 0.08513  0.00824  -0.02091 217 PRO A CD  
1586 N N   . ILE A 211 ? 0.24482 0.27242 0.27532 0.03435  0.00578  -0.03575 218 ILE A N   
1587 C CA  . ILE A 211 ? 0.21364 0.24487 0.25261 0.01919  0.00153  -0.03593 218 ILE A CA  
1588 C C   . ILE A 211 ? 0.22000 0.27723 0.27766 0.01465  0.00083  -0.03193 218 ILE A C   
1589 O O   . ILE A 211 ? 0.26935 0.33964 0.32809 0.01814  0.00720  -0.02870 218 ILE A O   
1590 C CB  . ILE A 211 ? 0.22846 0.24401 0.25423 0.01242  0.00355  -0.03822 218 ILE A CB  
1591 C CG1 . ILE A 211 ? 0.25379 0.24456 0.26456 0.00993  0.00275  -0.04042 218 ILE A CG1 
1592 C CG2 . ILE A 211 ? 0.25590 0.28028 0.29099 0.00230  0.00008  -0.03525 218 ILE A CG2 
1593 C CD1 . ILE A 211 ? 0.26126 0.23751 0.25670 0.00069  0.00226  -0.04504 218 ILE A CD1 
1594 N N   . THR A 212 ? 0.20353 0.26725 0.27398 0.00654  -0.00670 -0.03194 219 THR A N   
1595 C CA  . THR A 212 ? 0.17281 0.25702 0.26288 -0.00373 -0.00948 -0.02705 219 THR A CA  
1596 C C   . THR A 212 ? 0.18416 0.25044 0.27389 -0.01501 -0.01178 -0.02539 219 THR A C   
1597 O O   . THR A 212 ? 0.20263 0.24916 0.28501 -0.01531 -0.01732 -0.03108 219 THR A O   
1598 C CB  . THR A 212 ? 0.17568 0.27581 0.27798 -0.00686 -0.01925 -0.02997 219 THR A CB  
1599 O OG1 . THR A 212 ? 0.20762 0.32769 0.30951 0.00825  -0.01676 -0.02874 219 THR A OG1 
1600 C CG2 . THR A 212 ? 0.16966 0.29135 0.29589 -0.02518 -0.02399 -0.02366 219 THR A CG2 
1601 N N   . LEU A 213 ? 0.20018 0.27421 0.29538 -0.02079 -0.00628 -0.01616 220 LEU A N   
1602 C CA  . LEU A 213 ? 0.19434 0.25099 0.28924 -0.02947 -0.00773 -0.01036 220 LEU A CA  
1603 C C   . LEU A 213 ? 0.19248 0.24970 0.30523 -0.04583 -0.01398 -0.00555 220 LEU A C   
1604 O O   . LEU A 213 ? 0.20620 0.29089 0.33617 -0.05476 -0.01050 0.00479  220 LEU A O   
1605 C CB  . LEU A 213 ? 0.19577 0.26041 0.28392 -0.02702 0.00116  -0.00051 220 LEU A CB  
1606 C CG  . LEU A 213 ? 0.25233 0.30318 0.34025 -0.03352 0.00133  0.01119  220 LEU A CG  
1607 C CD1 . LEU A 213 ? 0.26230 0.28427 0.34023 -0.02865 -0.00488 0.00578  220 LEU A CD1 
1608 C CD2 . LEU A 213 ? 0.26891 0.33598 0.34538 -0.02764 0.01010  0.02071  220 LEU A CD2 
1609 N N   . PHE A 214 ? 0.18380 0.21124 0.29154 -0.05012 -0.02346 -0.01338 221 PHE A N   
1610 C CA  . PHE A 214 ? 0.20783 0.22322 0.32738 -0.06921 -0.03250 -0.01221 221 PHE A CA  
1611 C C   . PHE A 214 ? 0.25478 0.25556 0.37863 -0.08017 -0.02746 0.00476  221 PHE A C   
1612 O O   . PHE A 214 ? 0.27420 0.26399 0.38484 -0.06818 -0.01992 0.01146  221 PHE A O   
1613 C CB  . PHE A 214 ? 0.26077 0.23781 0.36420 -0.06695 -0.04405 -0.02851 221 PHE A CB  
1614 C CG  . PHE A 214 ? 0.21068 0.20241 0.30974 -0.06010 -0.05161 -0.04357 221 PHE A CG  
1615 C CD1 . PHE A 214 ? 0.21793 0.24165 0.31824 -0.04688 -0.04527 -0.04280 221 PHE A CD1 
1616 C CD2 . PHE A 214 ? 0.23808 0.20529 0.32676 -0.06568 -0.06565 -0.05885 221 PHE A CD2 
1617 C CE1 . PHE A 214 ? 0.20034 0.23590 0.29436 -0.03880 -0.05188 -0.05325 221 PHE A CE1 
1618 C CE2 . PHE A 214 ? 0.25876 0.24149 0.33917 -0.05731 -0.07316 -0.07194 221 PHE A CE2 
1619 C CZ  . PHE A 214 ? 0.21220 0.23116 0.29673 -0.04375 -0.06575 -0.06711 221 PHE A CZ  
1620 N N   . VAL A 215 ? 0.25929 0.26380 0.40226 -0.10381 -0.03193 0.01374  222 VAL A N   
1621 C CA  . VAL A 215 ? 0.30965 0.29429 0.45652 -0.11742 -0.02746 0.03328  222 VAL A CA  
1622 C C   . VAL A 215 ? 0.36865 0.29419 0.50753 -0.13245 -0.04022 0.02707  222 VAL A C   
1623 O O   . VAL A 215 ? 0.37970 0.28806 0.51291 -0.13604 -0.05360 0.00680  222 VAL A O   
1624 C CB  . VAL A 215 ? 0.44801 0.48118 0.62248 -0.13479 -0.01961 0.05457  222 VAL A CB  
1625 C CG1 . VAL A 215 ? 0.46993 0.54044 0.63771 -0.11335 -0.00341 0.06353  222 VAL A CG1 
1626 C CG2 . VAL A 215 ? 0.32550 0.39829 0.52397 -0.14869 -0.02771 0.04842  222 VAL A CG2 
1627 N N   . GLU A 216 ? 0.38212 0.27203 0.51606 -0.13939 -0.03616 0.04444  223 GLU A N   
1628 C CA  . GLU A 216 ? 0.47921 0.29909 0.59891 -0.15118 -0.04709 0.03897  223 GLU A CA  
1629 C C   . GLU A 216 ? 0.55892 0.37867 0.69140 -0.17936 -0.04471 0.05273  223 GLU A C   
1630 O O   . GLU A 216 ? 0.59538 0.45559 0.74725 -0.18849 -0.03358 0.07662  223 GLU A O   
1631 C CB  . GLU A 216 ? 0.52764 0.29890 0.61929 -0.12578 -0.04094 0.04459  223 GLU A CB  
1632 C CG  . GLU A 216 ? 0.47644 0.26512 0.55106 -0.09157 -0.03735 0.02899  223 GLU A CG  
1633 C CD  . GLU A 216 ? 0.53113 0.28719 0.58222 -0.06447 -0.03103 0.03690  223 GLU A CD  
1634 O OE1 . GLU A 216 ? 0.54569 0.23812 0.57638 -0.05843 -0.03669 0.03158  223 GLU A OE1 
1635 O OE2 . GLU A 216 ? 0.53922 0.33392 0.59084 -0.04838 -0.02108 0.04806  223 GLU A OE2 
1636 N N   . LYS A 217 ? 0.60727 0.38210 0.72814 -0.19221 -0.05449 0.03703  224 LYS A N   
1637 C CA  . LYS A 217 ? 0.75891 0.51860 0.89076 -0.22059 -0.05321 0.04925  224 LYS A CA  
1638 C C   . LYS A 217 ? 0.87789 0.61064 1.00297 -0.21763 -0.03952 0.07818  224 LYS A C   
1639 O O   . LYS A 217 ? 0.81652 0.50841 0.91638 -0.19255 -0.03559 0.08088  224 LYS A O   
1640 C CB  . LYS A 217 ? 0.70600 0.40611 0.82030 -0.23108 -0.06575 0.02599  224 LYS A CB  
1641 C CG  . LYS A 217 ? 0.87836 0.56178 1.00825 -0.26494 -0.06580 0.03821  224 LYS A CG  
1642 C CD  . LYS A 217 ? 0.94685 0.54968 1.05270 -0.27172 -0.07513 0.01924  224 LYS A CD  
1643 C CE  . LYS A 217 ? 1.09474 0.64615 1.19901 -0.28630 -0.06580 0.04266  224 LYS A CE  
1644 N NZ  . LYS A 217 ? 1.09897 0.70185 1.24033 -0.31915 -0.06021 0.06844  224 LYS A NZ  
# 
