data_7HAM
# 
_entry.id   7HAM 
# 
_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   7HAM         pdb_00007ham 10.2210/pdb7ham/pdb 
WWPDB D_1001407233 ?            ?                   
# 
_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                        7HAM 
_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 '(1P)-1-(3-fluorophenyl)-1H-imidazole' 162.164   1   ?        ? ? ? 
3 water       nat water                                  18.015    288 ?        ? ? ? 
# 
_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 '(1P)-1-(3-fluorophenyl)-1H-imidazole' A1AX5 
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 
A1AX5 non-polymer         . '(1P)-1-(3-fluorophenyl)-1H-imidazole' ? 'C9 H7 F N2'     162.164 
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        A1AX5 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1AX5 
_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 A1AX5 1   301 301 A1AX5 E8Y A . 
C 3 HOH   1   401 275 HOH   HOH A . 
C 3 HOH   2   402 239 HOH   HOH A . 
C 3 HOH   3   403 135 HOH   HOH A . 
C 3 HOH   4   404 160 HOH   HOH A . 
C 3 HOH   5   405 263 HOH   HOH A . 
C 3 HOH   6   406 238 HOH   HOH A . 
C 3 HOH   7   407 144 HOH   HOH A . 
C 3 HOH   8   408 42  HOH   HOH A . 
C 3 HOH   9   409 4   HOH   HOH A . 
C 3 HOH   10  410 249 HOH   HOH A . 
C 3 HOH   11  411 19  HOH   HOH A . 
C 3 HOH   12  412 55  HOH   HOH A . 
C 3 HOH   13  413 288 HOH   HOH A . 
C 3 HOH   14  414 228 HOH   HOH A . 
C 3 HOH   15  415 211 HOH   HOH A . 
C 3 HOH   16  416 92  HOH   HOH A . 
C 3 HOH   17  417 286 HOH   HOH A . 
C 3 HOH   18  418 73  HOH   HOH A . 
C 3 HOH   19  419 29  HOH   HOH A . 
C 3 HOH   20  420 111 HOH   HOH A . 
C 3 HOH   21  421 86  HOH   HOH A . 
C 3 HOH   22  422 8   HOH   HOH A . 
C 3 HOH   23  423 22  HOH   HOH A . 
C 3 HOH   24  424 251 HOH   HOH A . 
C 3 HOH   25  425 46  HOH   HOH A . 
C 3 HOH   26  426 283 HOH   HOH A . 
C 3 HOH   27  427 26  HOH   HOH A . 
C 3 HOH   28  428 83  HOH   HOH A . 
C 3 HOH   29  429 269 HOH   HOH A . 
C 3 HOH   30  430 3   HOH   HOH A . 
C 3 HOH   31  431 154 HOH   HOH A . 
C 3 HOH   32  432 75  HOH   HOH A . 
C 3 HOH   33  433 133 HOH   HOH A . 
C 3 HOH   34  434 125 HOH   HOH A . 
C 3 HOH   35  435 85  HOH   HOH A . 
C 3 HOH   36  436 21  HOH   HOH A . 
C 3 HOH   37  437 61  HOH   HOH A . 
C 3 HOH   38  438 24  HOH   HOH A . 
C 3 HOH   39  439 43  HOH   HOH A . 
C 3 HOH   40  440 2   HOH   HOH A . 
C 3 HOH   41  441 18  HOH   HOH A . 
C 3 HOH   42  442 57  HOH   HOH A . 
C 3 HOH   43  443 173 HOH   HOH A . 
C 3 HOH   44  444 129 HOH   HOH A . 
C 3 HOH   45  445 221 HOH   HOH A . 
C 3 HOH   46  446 247 HOH   HOH A . 
C 3 HOH   47  447 12  HOH   HOH A . 
C 3 HOH   48  448 188 HOH   HOH A . 
C 3 HOH   49  449 201 HOH   HOH A . 
C 3 HOH   50  450 30  HOH   HOH A . 
C 3 HOH   51  451 151 HOH   HOH A . 
C 3 HOH   52  452 103 HOH   HOH A . 
C 3 HOH   53  453 40  HOH   HOH A . 
C 3 HOH   54  454 51  HOH   HOH A . 
C 3 HOH   55  455 1   HOH   HOH A . 
C 3 HOH   56  456 116 HOH   HOH A . 
C 3 HOH   57  457 127 HOH   HOH A . 
C 3 HOH   58  458 74  HOH   HOH A . 
C 3 HOH   59  459 28  HOH   HOH A . 
C 3 HOH   60  460 172 HOH   HOH A . 
C 3 HOH   61  461 16  HOH   HOH A . 
C 3 HOH   62  462 53  HOH   HOH A . 
C 3 HOH   63  463 65  HOH   HOH A . 
C 3 HOH   64  464 181 HOH   HOH A . 
C 3 HOH   65  465 259 HOH   HOH A . 
C 3 HOH   66  466 17  HOH   HOH A . 
C 3 HOH   67  467 23  HOH   HOH A . 
C 3 HOH   68  468 6   HOH   HOH A . 
C 3 HOH   69  469 102 HOH   HOH A . 
C 3 HOH   70  470 176 HOH   HOH A . 
C 3 HOH   71  471 89  HOH   HOH A . 
C 3 HOH   72  472 237 HOH   HOH A . 
C 3 HOH   73  473 78  HOH   HOH A . 
C 3 HOH   74  474 142 HOH   HOH A . 
C 3 HOH   75  475 50  HOH   HOH A . 
C 3 HOH   76  476 13  HOH   HOH A . 
C 3 HOH   77  477 271 HOH   HOH A . 
C 3 HOH   78  478 5   HOH   HOH A . 
C 3 HOH   79  479 64  HOH   HOH A . 
C 3 HOH   80  480 225 HOH   HOH A . 
C 3 HOH   81  481 132 HOH   HOH A . 
C 3 HOH   82  482 38  HOH   HOH A . 
C 3 HOH   83  483 88  HOH   HOH A . 
C 3 HOH   84  484 227 HOH   HOH A . 
C 3 HOH   85  485 10  HOH   HOH A . 
C 3 HOH   86  486 71  HOH   HOH A . 
C 3 HOH   87  487 156 HOH   HOH A . 
C 3 HOH   88  488 60  HOH   HOH A . 
C 3 HOH   89  489 27  HOH   HOH A . 
C 3 HOH   90  490 37  HOH   HOH A . 
C 3 HOH   91  491 134 HOH   HOH A . 
C 3 HOH   92  492 93  HOH   HOH A . 
C 3 HOH   93  493 34  HOH   HOH A . 
C 3 HOH   94  494 81  HOH   HOH A . 
C 3 HOH   95  495 233 HOH   HOH A . 
C 3 HOH   96  496 47  HOH   HOH A . 
C 3 HOH   97  497 120 HOH   HOH A . 
C 3 HOH   98  498 171 HOH   HOH A . 
C 3 HOH   99  499 97  HOH   HOH A . 
C 3 HOH   100 500 62  HOH   HOH A . 
C 3 HOH   101 501 9   HOH   HOH A . 
C 3 HOH   102 502 226 HOH   HOH A . 
C 3 HOH   103 503 56  HOH   HOH A . 
C 3 HOH   104 504 232 HOH   HOH A . 
C 3 HOH   105 505 52  HOH   HOH A . 
C 3 HOH   106 506 122 HOH   HOH A . 
C 3 HOH   107 507 167 HOH   HOH A . 
C 3 HOH   108 508 189 HOH   HOH A . 
C 3 HOH   109 509 229 HOH   HOH A . 
C 3 HOH   110 510 39  HOH   HOH A . 
C 3 HOH   111 511 36  HOH   HOH A . 
C 3 HOH   112 512 109 HOH   HOH A . 
C 3 HOH   113 513 87  HOH   HOH A . 
C 3 HOH   114 514 48  HOH   HOH A . 
C 3 HOH   115 515 128 HOH   HOH A . 
C 3 HOH   116 516 14  HOH   HOH A . 
C 3 HOH   117 517 77  HOH   HOH A . 
C 3 HOH   118 518 119 HOH   HOH A . 
C 3 HOH   119 519 101 HOH   HOH A . 
C 3 HOH   120 520 118 HOH   HOH A . 
C 3 HOH   121 521 20  HOH   HOH A . 
C 3 HOH   122 522 141 HOH   HOH A . 
C 3 HOH   123 523 184 HOH   HOH A . 
C 3 HOH   124 524 82  HOH   HOH A . 
C 3 HOH   125 525 241 HOH   HOH A . 
C 3 HOH   126 526 49  HOH   HOH A . 
C 3 HOH   127 527 106 HOH   HOH A . 
C 3 HOH   128 528 197 HOH   HOH A . 
C 3 HOH   129 529 94  HOH   HOH A . 
C 3 HOH   130 530 68  HOH   HOH A . 
C 3 HOH   131 531 168 HOH   HOH A . 
C 3 HOH   132 532 25  HOH   HOH A . 
C 3 HOH   133 533 33  HOH   HOH A . 
C 3 HOH   134 534 35  HOH   HOH A . 
C 3 HOH   135 535 63  HOH   HOH A . 
C 3 HOH   136 536 273 HOH   HOH A . 
C 3 HOH   137 537 218 HOH   HOH A . 
C 3 HOH   138 538 177 HOH   HOH A . 
C 3 HOH   139 539 44  HOH   HOH A . 
C 3 HOH   140 540 45  HOH   HOH A . 
C 3 HOH   141 541 98  HOH   HOH A . 
C 3 HOH   142 542 216 HOH   HOH A . 
C 3 HOH   143 543 113 HOH   HOH A . 
C 3 HOH   144 544 255 HOH   HOH A . 
C 3 HOH   145 545 149 HOH   HOH A . 
C 3 HOH   146 546 126 HOH   HOH A . 
C 3 HOH   147 547 279 HOH   HOH A . 
C 3 HOH   148 548 145 HOH   HOH A . 
C 3 HOH   149 549 265 HOH   HOH A . 
C 3 HOH   150 550 112 HOH   HOH A . 
C 3 HOH   151 551 166 HOH   HOH A . 
C 3 HOH   152 552 84  HOH   HOH A . 
C 3 HOH   153 553 256 HOH   HOH A . 
C 3 HOH   154 554 15  HOH   HOH A . 
C 3 HOH   155 555 130 HOH   HOH A . 
C 3 HOH   156 556 41  HOH   HOH A . 
C 3 HOH   157 557 248 HOH   HOH A . 
C 3 HOH   158 558 230 HOH   HOH A . 
C 3 HOH   159 559 153 HOH   HOH A . 
C 3 HOH   160 560 163 HOH   HOH A . 
C 3 HOH   161 561 185 HOH   HOH A . 
C 3 HOH   162 562 157 HOH   HOH A . 
C 3 HOH   163 563 175 HOH   HOH A . 
C 3 HOH   164 564 69  HOH   HOH A . 
C 3 HOH   165 565 136 HOH   HOH A . 
C 3 HOH   166 566 210 HOH   HOH A . 
C 3 HOH   167 567 7   HOH   HOH A . 
C 3 HOH   168 568 11  HOH   HOH A . 
C 3 HOH   169 569 178 HOH   HOH A . 
C 3 HOH   170 570 280 HOH   HOH A . 
C 3 HOH   171 571 80  HOH   HOH A . 
C 3 HOH   172 572 66  HOH   HOH A . 
C 3 HOH   173 573 121 HOH   HOH A . 
C 3 HOH   174 574 182 HOH   HOH A . 
C 3 HOH   175 575 159 HOH   HOH A . 
C 3 HOH   176 576 108 HOH   HOH A . 
C 3 HOH   177 577 192 HOH   HOH A . 
C 3 HOH   178 578 203 HOH   HOH A . 
C 3 HOH   179 579 170 HOH   HOH A . 
C 3 HOH   180 580 222 HOH   HOH A . 
C 3 HOH   181 581 179 HOH   HOH A . 
C 3 HOH   182 582 114 HOH   HOH A . 
C 3 HOH   183 583 123 HOH   HOH A . 
C 3 HOH   184 584 138 HOH   HOH A . 
C 3 HOH   185 585 212 HOH   HOH A . 
C 3 HOH   186 586 140 HOH   HOH A . 
C 3 HOH   187 587 150 HOH   HOH A . 
C 3 HOH   188 588 32  HOH   HOH A . 
C 3 HOH   189 589 193 HOH   HOH A . 
C 3 HOH   190 590 217 HOH   HOH A . 
C 3 HOH   191 591 158 HOH   HOH A . 
C 3 HOH   192 592 155 HOH   HOH A . 
C 3 HOH   193 593 215 HOH   HOH A . 
C 3 HOH   194 594 31  HOH   HOH A . 
C 3 HOH   195 595 143 HOH   HOH A . 
C 3 HOH   196 596 205 HOH   HOH A . 
C 3 HOH   197 597 206 HOH   HOH A . 
C 3 HOH   198 598 180 HOH   HOH A . 
C 3 HOH   199 599 223 HOH   HOH A . 
C 3 HOH   200 600 194 HOH   HOH A . 
C 3 HOH   201 601 287 HOH   HOH A . 
C 3 HOH   202 602 58  HOH   HOH A . 
C 3 HOH   203 603 284 HOH   HOH A . 
C 3 HOH   204 604 191 HOH   HOH A . 
C 3 HOH   205 605 274 HOH   HOH A . 
C 3 HOH   206 606 242 HOH   HOH A . 
C 3 HOH   207 607 202 HOH   HOH A . 
C 3 HOH   208 608 183 HOH   HOH A . 
C 3 HOH   209 609 220 HOH   HOH A . 
C 3 HOH   210 610 196 HOH   HOH A . 
C 3 HOH   211 611 165 HOH   HOH A . 
C 3 HOH   212 612 199 HOH   HOH A . 
C 3 HOH   213 613 204 HOH   HOH A . 
C 3 HOH   214 614 243 HOH   HOH A . 
C 3 HOH   215 615 91  HOH   HOH A . 
C 3 HOH   216 616 254 HOH   HOH A . 
C 3 HOH   217 617 261 HOH   HOH A . 
C 3 HOH   218 618 59  HOH   HOH A . 
C 3 HOH   219 619 281 HOH   HOH A . 
C 3 HOH   220 620 213 HOH   HOH A . 
C 3 HOH   221 621 169 HOH   HOH A . 
C 3 HOH   222 622 148 HOH   HOH A . 
C 3 HOH   223 623 152 HOH   HOH A . 
C 3 HOH   224 624 162 HOH   HOH A . 
C 3 HOH   225 625 235 HOH   HOH A . 
C 3 HOH   226 626 131 HOH   HOH A . 
C 3 HOH   227 627 54  HOH   HOH A . 
C 3 HOH   228 628 276 HOH   HOH A . 
C 3 HOH   229 629 240 HOH   HOH A . 
C 3 HOH   230 630 67  HOH   HOH A . 
C 3 HOH   231 631 219 HOH   HOH A . 
C 3 HOH   232 632 272 HOH   HOH A . 
C 3 HOH   233 633 76  HOH   HOH A . 
C 3 HOH   234 634 214 HOH   HOH A . 
C 3 HOH   235 635 164 HOH   HOH A . 
C 3 HOH   236 636 110 HOH   HOH A . 
C 3 HOH   237 637 282 HOH   HOH A . 
C 3 HOH   238 638 146 HOH   HOH A . 
C 3 HOH   239 639 72  HOH   HOH A . 
C 3 HOH   240 640 264 HOH   HOH A . 
C 3 HOH   241 641 252 HOH   HOH A . 
C 3 HOH   242 642 198 HOH   HOH A . 
C 3 HOH   243 643 253 HOH   HOH A . 
C 3 HOH   244 644 79  HOH   HOH A . 
C 3 HOH   245 645 186 HOH   HOH A . 
C 3 HOH   246 646 139 HOH   HOH A . 
C 3 HOH   247 647 90  HOH   HOH A . 
C 3 HOH   248 648 245 HOH   HOH A . 
C 3 HOH   249 649 224 HOH   HOH A . 
C 3 HOH   250 650 161 HOH   HOH A . 
C 3 HOH   251 651 124 HOH   HOH A . 
C 3 HOH   252 652 270 HOH   HOH A . 
C 3 HOH   253 653 95  HOH   HOH A . 
C 3 HOH   254 654 70  HOH   HOH A . 
C 3 HOH   255 655 174 HOH   HOH A . 
C 3 HOH   256 656 268 HOH   HOH A . 
C 3 HOH   257 657 244 HOH   HOH A . 
C 3 HOH   258 658 99  HOH   HOH A . 
C 3 HOH   259 659 236 HOH   HOH A . 
C 3 HOH   260 660 209 HOH   HOH A . 
C 3 HOH   261 661 207 HOH   HOH A . 
C 3 HOH   262 662 267 HOH   HOH A . 
C 3 HOH   263 663 147 HOH   HOH A . 
C 3 HOH   264 664 257 HOH   HOH A . 
C 3 HOH   265 665 208 HOH   HOH A . 
C 3 HOH   266 666 187 HOH   HOH A . 
C 3 HOH   267 667 115 HOH   HOH A . 
C 3 HOH   268 668 100 HOH   HOH A . 
C 3 HOH   269 669 234 HOH   HOH A . 
C 3 HOH   270 670 137 HOH   HOH A . 
C 3 HOH   271 671 96  HOH   HOH A . 
C 3 HOH   272 672 260 HOH   HOH A . 
C 3 HOH   273 673 231 HOH   HOH A . 
C 3 HOH   274 674 104 HOH   HOH A . 
C 3 HOH   275 675 250 HOH   HOH A . 
C 3 HOH   276 676 285 HOH   HOH A . 
C 3 HOH   277 677 107 HOH   HOH A . 
C 3 HOH   278 678 200 HOH   HOH A . 
C 3 HOH   279 679 190 HOH   HOH A . 
C 3 HOH   280 680 266 HOH   HOH A . 
C 3 HOH   281 681 262 HOH   HOH A . 
C 3 HOH   282 682 195 HOH   HOH A . 
C 3 HOH   283 683 117 HOH   HOH A . 
C 3 HOH   284 684 278 HOH   HOH A . 
C 3 HOH   285 685 105 HOH   HOH A . 
C 3 HOH   286 686 246 HOH   HOH A . 
C 3 HOH   287 687 258 HOH   HOH A . 
C 3 HOH   288 688 277 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             607785.729 
_cell.length_a           67.120 
_cell.length_b           91.550 
_cell.length_c           98.910 
_cell.angle_beta         90.000 
_cell.angle_gamma        90.000 
_cell.angle_alpha        90.000 
_cell.entry_id           7HAM 
_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                         7HAM 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
# 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
_exptl.entry_id          7HAM 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_Matthews      2.88 
_exptl_crystal.density_percent_sol   57.23 
_exptl_crystal.density_meas          ? 
_exptl_crystal.description           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.pH              8.5 
_exptl_crystal_grow.temp            277 
_exptl_crystal_grow.pdbx_details    '100mM Tris-HCl pH 8.5, 22% PEG4000, 200mM MgCl2' 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_diffrn.id                     1 
_diffrn.crystal_id             1 
_diffrn.ambient_temp           100 
_diffrn.ambient_temp_details   ? 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               PIXEL 
_diffrn_detector.type                   'DECTRIS EIGER X 16M' 
_diffrn_detector.pdbx_collection_date   2024-01-13 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.pdbx_scattering_type             x-ray 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.monochromator                    Si111 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.97919 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.pdbx_synchrotron_beamline   BL10U2 
_diffrn_source.type                        'SSRF BEAMLINE BL10U2' 
_diffrn_source.pdbx_wavelength_list        0.97919 
_diffrn_source.pdbx_synchrotron_site       SSRF 
_diffrn_source.pdbx_wavelength             ? 
# 
_reflns.entry_id                     7HAM 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             30.020 
_reflns.d_resolution_high            1.770 
_reflns.number_obs                   29719 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         99.000 
_reflns.pdbx_Rmerge_I_obs            0.127 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        15.200 
_reflns.B_iso_Wilson_estimate        ? 
_reflns.pdbx_redundancy              13.100 
_reflns.pdbx_Rrim_I_all              0.132 
_reflns.pdbx_Rpim_I_all              0.036 
_reflns.pdbx_CC_half                 0.999 
_reflns.pdbx_netI_over_av_sigmaI     ? 
_reflns.pdbx_number_measured_all     390142 
_reflns.pdbx_scaling_rejects         18 
_reflns.pdbx_chi_squared             ? 
_reflns.Rmerge_F_all                 ? 
_reflns.Rmerge_F_obs                 ? 
_reflns.observed_criterion_F_max     ? 
_reflns.observed_criterion_F_min     ? 
_reflns.observed_criterion_I_max     ? 
_reflns.observed_criterion_I_min     ? 
_reflns.pdbx_d_res_high_opt          ? 
_reflns.pdbx_d_res_low_opt           ? 
_reflns.details                      ? 
# 
loop_
_reflns_shell.pdbx_diffrn_id 
_reflns_shell.pdbx_ordinal 
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_reflns_shell.number_measured_obs 
_reflns_shell.number_measured_all 
_reflns_shell.number_unique_obs 
_reflns_shell.pdbx_rejects 
_reflns_shell.Rmerge_I_obs 
_reflns_shell.meanI_over_sigI_obs 
_reflns_shell.pdbx_Rsym_value 
_reflns_shell.pdbx_chi_squared 
_reflns_shell.pdbx_redundancy 
_reflns_shell.percent_possible_obs 
_reflns_shell.pdbx_netI_over_sigmaI_obs 
_reflns_shell.number_possible 
_reflns_shell.number_unique_all 
_reflns_shell.Rmerge_F_all 
_reflns_shell.Rmerge_F_obs 
_reflns_shell.Rmerge_I_all 
_reflns_shell.meanI_over_sigI_all 
_reflns_shell.percent_possible_all 
_reflns_shell.pdbx_Rrim_I_all 
_reflns_shell.pdbx_Rpim_I_all 
_reflns_shell.pdbx_CC_half 
1 1 1.770 1.820  ? 28416 2144 ? 1.900 ? ? ? 13.300 ? 1.500  ? ? ? ? ? ? 98.300 1.975 0.536 0.544 
1 2 7.920 30.020 ? 3481  375  ? 0.037 ? ? ? 9.300  ? 42.900 ? ? ? ? ? ? 96.600 0.039 0.012 0.999 
# 
_refine.entry_id                                 7HAM 
_refine.pdbx_method_to_determine_struct          'FOURIER SYNTHESIS' 
_refine.ls_percent_reflns_R_free                 5.20 
_refine.pdbx_overall_phase_error                 22.8129 
_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                          0.1858 
_refine.B_iso_mean                               31.90 
_refine.ls_number_reflns_R_free                  1544 
_refine.ls_percent_reflns_obs                    98.77 
_refine.ls_R_factor_R_work                       0.1846 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_refine.ls_d_res_high                            1.77 
_refine.ls_number_reflns_obs                     29708 
_refine.pdbx_ls_sigma_F                          1.34 
_refine.ls_number_reflns_R_work                  28164 
_refine.ls_d_res_low                             29.59 
_refine.pdbx_stereochemistry_target_values       'GeoStd + Monomer Library + CDL v1.2' 
_refine.ls_R_factor_R_free                       0.2062 
_refine.overall_SU_ML                            0.2037 
_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         12 
_refine_hist.number_atoms_solvent             288 
_refine_hist.number_atoms_total               1944 
_refine_hist.d_res_high                       1.77 
_refine_hist.d_res_low                        29.59 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.type 
_refine_ls_restr.number 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
_refine_ls_restr.dev_ideal_target 
'X-RAY DIFFRACTION' f_bond_d           1683 0.0026 ? ? ? 
'X-RAY DIFFRACTION' f_angle_d          2268 0.5810 ? ? ? 
'X-RAY DIFFRACTION' f_chiral_restr     259  0.0429 ? ? ? 
'X-RAY DIFFRACTION' f_plane_restr      289  0.0037 ? ? ? 
'X-RAY DIFFRACTION' f_dihedral_angle_d 223  5.5201 ? ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.R_factor_R_free 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.R_factor_all 
'X-RAY DIFFRACTION' 1.77 1.83  2522 0.2968 98.19 0.3353 140 . . . . . 
'X-RAY DIFFRACTION' 1.83 1.89  2546 0.2622 98.36 0.2850 101 . . . . . 
'X-RAY DIFFRACTION' 1.89 1.97  2506 0.2647 98.36 0.3005 134 . . . . . 
'X-RAY DIFFRACTION' 1.97 2.06  2559 0.2078 98.56 0.2314 117 . . . . . 
'X-RAY DIFFRACTION' 2.06 2.17  2539 0.1876 98.74 0.2088 132 . . . . . 
'X-RAY DIFFRACTION' 2.17 2.30  2535 0.2033 98.67 0.2552 145 . . . . . 
'X-RAY DIFFRACTION' 2.30 2.48  2523 0.1889 99.01 0.1922 166 . . . . . 
'X-RAY DIFFRACTION' 2.48 2.73  2548 0.1887 99.23 0.2225 156 . . . . . 
'X-RAY DIFFRACTION' 2.73 3.12  2578 0.1878 99.13 0.2149 158 . . . . . 
'X-RAY DIFFRACTION' 3.12 3.93  2626 0.1624 99.28 0.1722 128 . . . . . 
'X-RAY DIFFRACTION' 3.93 29.59 2682 0.1589 98.92 0.1790 167 . . . . . 
# 
_struct.entry_id                  7HAM 
_struct.title                     'PanDDA analysis group deposition -- Crystal structure of HSP90N in complex with Fr14242' 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_details        ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HAM 
_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              7HAM 
_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 7HAM MET A 1   ? UNP P07900 ? ? 'initiating methionine' 8   1 
1 7HAM LEU A 230 ? UNP P07900 ? ? 'expression tag'        237 2 
1 7HAM GLU A 231 ? UNP P07900 ? ? 'expression tag'        238 3 
1 7HAM HIS A 232 ? UNP P07900 ? ? 'expression tag'        239 4 
1 7HAM HIS A 233 ? UNP P07900 ? ? 'expression tag'        240 5 
1 7HAM HIS A 234 ? UNP P07900 ? ? 'expression tag'        241 6 
1 7HAM HIS A 235 ? UNP P07900 ? ? 'expression tag'        242 7 
1 7HAM HIS A 236 ? UNP P07900 ? ? 'expression tag'        243 8 
1 7HAM HIS A 237 ? UNP P07900 ? ? 'expression tag'        244 9 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 AA1 GLN A 16  ? THR A 29  ? GLN A 23  THR A 36  1 ? 14 
HELX_P HELX_P2 AA2 GLU A 35  ? ASP A 59  ? GLU A 42  ASP A 66  1 ? 25 
HELX_P HELX_P3 AA3 PRO A 60  ? ASP A 64  ? PRO A 67  ASP A 71  5 ? 5  
HELX_P HELX_P4 AA4 THR A 92  ? ASN A 98  ? THR A 99  ASN A 105 1 ? 7  
HELX_P HELX_P5 AA5 ASN A 98  ? ALA A 117 ? ASN A 105 ALA A 124 1 ? 20 
HELX_P HELX_P6 AA6 ASP A 120 ? GLY A 128 ? ASP A 127 GLY A 135 5 ? 9  
HELX_P HELX_P7 AA7 VAL A 129 ? LEU A 136 ? VAL A 136 LEU A 143 5 ? 8  
HELX_P HELX_P8 AA8 GLU A 185 ? LEU A 191 ? GLU A 192 LEU A 198 5 ? 7  
HELX_P HELX_P9 AA9 GLU A 192 ? SER A 204 ? GLU A 199 SER A 211 1 ? 13 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
_struct_sheet.id               AA1 
_struct_sheet.type             ? 
_struct_sheet.number_strands   8 
_struct_sheet.details          ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA1 5 6 ? anti-parallel 
AA1 6 7 ? anti-parallel 
AA1 7 8 ? parallel      
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 GLU A 11  ? ALA A 14  ? GLU A 18  ALA A 21  
AA1 2 SER A 162 ? THR A 167 ? SER A 169 THR A 174 
AA1 3 GLN A 152 ? SER A 157 ? GLN A 159 SER A 164 
AA1 4 ALA A 138 ? LYS A 146 ? ALA A 145 LYS A 153 
AA1 5 GLY A 176 ? LEU A 183 ? GLY A 183 LEU A 190 
AA1 6 THR A 81  ? ASP A 86  ? THR A 88  ASP A 93  
AA1 7 ILE A 71  ? ASN A 76  ? ILE A 78  ASN A 83  
AA1 8 ILE A 211 ? LEU A 213 ? ILE A 218 LEU A 220 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N PHE A 13  ? N PHE A 20  O PHE A 163 ? O PHE A 170 
AA1 2 3 O ARG A 166 ? O ARG A 173 N ALA A 154 ? N ALA A 161 
AA1 3 4 O TRP A 155 ? O TRP A 162 N VAL A 143 ? N VAL A 150 
AA1 4 5 N THR A 142 ? N THR A 149 O ILE A 180 ? O ILE A 187 
AA1 5 6 O LEU A 181 ? O LEU A 188 N LEU A 82  ? N LEU A 89  
AA1 6 7 O VAL A 85  ? O VAL A 92  N ASN A 72  ? N ASN A 79  
AA1 7 8 N LEU A 73  ? N LEU A 80  O THR A 212 ? O THR A 219 
# 
_pdbx_entry_details.entry_id                   7HAM 
_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 604 ? ? O A HOH 686 ? ? 1.94 
2 1 O   A HOH 593 ? ? O A HOH 597 ? ? 1.95 
3 1 NH1 A ARG 201 ? ? O A HOH 401 ? ? 1.99 
4 1 O   A HOH 681 ? ? O A HOH 687 ? ? 2.05 
5 1 NZ  A LYS 84  ? ? O A HOH 402 ? ? 2.08 
6 1 O   A HOH 610 ? ? O A HOH 642 ? ? 2.14 
7 1 O   A HOH 598 ? ? O A HOH 614 ? ? 2.18 
8 1 O   A HOH 664 ? ? O A HOH 681 ? ? 2.18 
9 1 O   A HOH 464 ? ? O A HOH 551 ? ? 2.19 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 TYR A 38  ? ? -161.46 105.05  
2 1 THR A 94  ? ? -105.15 40.09   
3 1 ASN A 105 ? ? -126.55 -60.71  
4 1 ALA A 124 ? ? -79.19  -116.03 
5 1 ALA A 166 ? ? 62.11   -145.11 
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z               
2 x,-y,-z             
3 -x,y,-z             
4 -x,-y,z             
5 x+1/2,y+1/2,z+1/2   
6 x+1/2,-y+1/2,-z+1/2 
7 -x+1/2,y+1/2,-z+1/2 
8 -x+1/2,-y+1/2,z+1/2 
# 
loop_
_pdbx_refine_tls.id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][3] 
1 ? 'X-RAY DIFFRACTION' refined 13.2222248133  -18.3968370677 -18.0846344406 0.161850569441 0.223473783714 0.19700714723  
0.0180353466405   -0.0137150483416  -0.0361185938199 2.3181897421  1.53481566218 6.27878230192 -0.559851018189 -2.05676643938  
0.621597935393  0.0781822615604  -0.138992172113    -0.0687182128371 0.00465318147914 0.0504080890079   -0.0555072613154 
-0.0468477384889 0.365050172855    -0.107474227153  
2 ? 'X-RAY DIFFRACTION' refined -6.72017789563 -6.5935098811  -25.3396966677 0.178879848887 0.175888034814 0.194006668131 
0.00585712062426  -0.0122747105285  -0.0211319269018 1.93281332002 2.83923007591 4.45225526266 -0.878205376254 1.30979076811   
-2.16840465596  -0.0652966065802 0.169961756514     0.140215839183   -0.0754656593673 -0.032467941081   0.115442591905   
-0.301835530593  -0.0233979094932  0.126001792457   
3 ? 'X-RAY DIFFRACTION' refined -3.81477756924 -18.5755149314 -23.5456742667 0.197119438548 0.160549057125 0.182909119057 
-0.00661686246549 -0.0254819028427  -0.0472017228505 2.28495553425 1.73513887609 2.53833756527 -0.519091535112 -0.772919399512 
-0.820471828238 0.00156191329489 -0.000137455099552 -0.0685148781227 -0.127919009668  0.0359514699899   0.0210744841754  
0.187689122284   -0.0401872362983  -0.0428521367374 
4 ? 'X-RAY DIFFRACTION' refined 12.4902115189  -5.84599329589 -14.8285093006 0.247187570434 0.320506900197 0.277065444186 
-0.0470900091808  0.0133499273459   -0.0371679240203 4.87845768139 3.18581968954 2.60255198355 1.43364698376   -0.480244508797 
-0.380393785202 0.319352244899   -0.800474171475    0.352336931351   0.421391831383   -0.206085087879   -0.045103726338  
-0.245616202481  0.664600101695    0.0419115860578  
5 ? 'X-RAY DIFFRACTION' refined 1.52416305049  -20.1021387667 -26.8225547229 0.169134552911 0.173500108371 0.205038456942 
-0.00958080080755 -0.00546849927283 -0.037455830243  2.27458778063 2.04791560918 2.79272733985 -0.949157997982 0.232612177366  
-0.782140903704 0.0732320002959  0.14989185183      -0.199860033761  -0.193045656483  -0.00594895235571 0.137770116301   
0.208780040333   -0.00956012827466 -0.0850082956505 
6 ? 'X-RAY DIFFRACTION' refined -6.10313138054 -19.9149099839 -6.84207937659 0.21453882239  0.254377635516 0.150518586697 
-0.0327219553242  -0.0135769914266  0.0198762441168  6.26045839057 6.47552752588 4.75288776493 -2.31173877675  -1.3054848385   
0.555442623858  -0.106825891958  -0.338276159487    -0.347801034359  0.330662100521   -0.0247186442091  0.239023605992   
0.302133433035   -0.138564972381   0.115238487043   
7 ? 'X-RAY DIFFRACTION' refined -13.3477382151 -13.6849025114 -15.185559113  0.159323515254 0.251909604481 0.157040828008 
0.0392967655817   -0.00251014038207 -0.0111089324718 5.16821792917 4.18733602171 5.06644868024 1.21050765997   -0.324960377078 
-0.7893158239   -0.0293063818091 -0.29267628595     -0.206309186914  0.490385334411   0.0953606598849   -0.0872182296939 
-0.0614354926384 -0.136836880596   -0.0378188523195 
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
1 1 'X-RAY DIFFRACTION' A 16  A 1   A 40  A 25  . 
;chain 'A' and (resid 16 through 40 )
;
2 2 'X-RAY DIFFRACTION' A 41  A 26  A 76  A 61  . 
;chain 'A' and (resid 41 through 76 )
;
3 3 'X-RAY DIFFRACTION' A 77  A 62  A 105 A 90  . 
;chain 'A' and (resid 77 through 105 )
;
4 4 'X-RAY DIFFRACTION' A 106 A 91  A 136 A 121 . 
;chain 'A' and (resid 106 through 136 )
;
5 5 'X-RAY DIFFRACTION' A 137 A 122 A 190 A 175 . 
;chain 'A' and (resid 137 through 190 )
;
6 6 'X-RAY DIFFRACTION' A 191 A 176 A 210 A 195 . 
;chain 'A' and (resid 191 through 210 )
;
7 7 'X-RAY DIFFRACTION' A 211 A 196 A 224 A 209 . 
;chain 'A' and (resid 211 through 224 )
;
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A MET 8   ? A MET 1   
2  1 Y 1 A ASP 9   ? A ASP 2   
3  1 Y 1 A GLN 10  ? A GLN 3   
4  1 Y 1 A PRO 11  ? A PRO 4   
5  1 Y 1 A MET 12  ? A MET 5   
6  1 Y 1 A GLU 13  ? A GLU 6   
7  1 Y 1 A GLU 14  ? A GLU 7   
8  1 Y 1 A GLU 15  ? A GLU 8   
9  1 Y 1 A GLU 225 ? A GLU 218 
10 1 Y 1 A ARG 226 ? A ARG 219 
11 1 Y 1 A ASP 227 ? A ASP 220 
12 1 Y 1 A LYS 228 ? A LYS 221 
13 1 Y 1 A GLU 229 ? A GLU 222 
14 1 Y 1 A VAL 230 ? A VAL 223 
15 1 Y 1 A SER 231 ? A SER 224 
16 1 Y 1 A ASP 232 ? A ASP 225 
17 1 Y 1 A ASP 233 ? A ASP 226 
18 1 Y 1 A GLU 234 ? A GLU 227 
19 1 Y 1 A ALA 235 ? A ALA 228 
20 1 Y 1 A GLU 236 ? A GLU 229 
21 1 Y 1 A LEU 237 ? A LEU 230 
22 1 Y 1 A GLU 238 ? A GLU 231 
23 1 Y 1 A HIS 239 ? A HIS 232 
24 1 Y 1 A HIS 240 ? A HIS 233 
25 1 Y 1 A HIS 241 ? A HIS 234 
26 1 Y 1 A HIS 242 ? A HIS 235 
27 1 Y 1 A HIS 243 ? A HIS 236 
28 1 Y 1 A HIS 244 ? A HIS 237 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
A1AX5 N1   N Y N 1   
A1AX5 C4   C Y N 2   
A1AX5 C5   C Y N 3   
A1AX5 C6   C Y N 4   
A1AX5 C7   C Y N 5   
A1AX5 C8   C Y N 6   
A1AX5 C1   C Y N 7   
A1AX5 C2   C Y N 8   
A1AX5 C3   C Y N 9   
A1AX5 C9   C Y N 10  
A1AX5 F1   F N N 11  
A1AX5 N2   N Y N 12  
A1AX5 H3   H N N 13  
A1AX5 H4   H N N 14  
A1AX5 H5   H N N 15  
A1AX5 H6   H N N 16  
A1AX5 H1   H N N 17  
A1AX5 H2   H N N 18  
A1AX5 H7   H N N 19  
ALA   N    N N N 20  
ALA   CA   C N S 21  
ALA   C    C N N 22  
ALA   O    O N N 23  
ALA   CB   C N N 24  
ALA   OXT  O N N 25  
ALA   H    H N N 26  
ALA   H2   H N N 27  
ALA   HA   H N N 28  
ALA   HB1  H N N 29  
ALA   HB2  H N N 30  
ALA   HB3  H N N 31  
ALA   HXT  H N N 32  
ARG   N    N N N 33  
ARG   CA   C N S 34  
ARG   C    C N N 35  
ARG   O    O N N 36  
ARG   CB   C N N 37  
ARG   CG   C N N 38  
ARG   CD   C N N 39  
ARG   NE   N N N 40  
ARG   CZ   C N N 41  
ARG   NH1  N N N 42  
ARG   NH2  N N N 43  
ARG   OXT  O N N 44  
ARG   H    H N N 45  
ARG   H2   H N N 46  
ARG   HA   H N N 47  
ARG   HB2  H N N 48  
ARG   HB3  H N N 49  
ARG   HG2  H N N 50  
ARG   HG3  H N N 51  
ARG   HD2  H N N 52  
ARG   HD3  H N N 53  
ARG   HE   H N N 54  
ARG   HH11 H N N 55  
ARG   HH12 H N N 56  
ARG   HH21 H N N 57  
ARG   HH22 H N N 58  
ARG   HXT  H N N 59  
ASN   N    N N N 60  
ASN   CA   C N S 61  
ASN   C    C N N 62  
ASN   O    O N N 63  
ASN   CB   C N N 64  
ASN   CG   C N N 65  
ASN   OD1  O N N 66  
ASN   ND2  N N N 67  
ASN   OXT  O N N 68  
ASN   H    H N N 69  
ASN   H2   H N N 70  
ASN   HA   H N N 71  
ASN   HB2  H N N 72  
ASN   HB3  H N N 73  
ASN   HD21 H N N 74  
ASN   HD22 H N N 75  
ASN   HXT  H N N 76  
ASP   N    N N N 77  
ASP   CA   C N S 78  
ASP   C    C N N 79  
ASP   O    O N N 80  
ASP   CB   C N N 81  
ASP   CG   C N N 82  
ASP   OD1  O N N 83  
ASP   OD2  O N N 84  
ASP   OXT  O N N 85  
ASP   H    H N N 86  
ASP   H2   H N N 87  
ASP   HA   H N N 88  
ASP   HB2  H N N 89  
ASP   HB3  H N N 90  
ASP   HD2  H N N 91  
ASP   HXT  H N N 92  
GLN   N    N N N 93  
GLN   CA   C N S 94  
GLN   C    C N N 95  
GLN   O    O N N 96  
GLN   CB   C N N 97  
GLN   CG   C N N 98  
GLN   CD   C N N 99  
GLN   OE1  O N N 100 
GLN   NE2  N N N 101 
GLN   OXT  O N N 102 
GLN   H    H N N 103 
GLN   H2   H N N 104 
GLN   HA   H N N 105 
GLN   HB2  H N N 106 
GLN   HB3  H N N 107 
GLN   HG2  H N N 108 
GLN   HG3  H N N 109 
GLN   HE21 H N N 110 
GLN   HE22 H N N 111 
GLN   HXT  H N N 112 
GLU   N    N N N 113 
GLU   CA   C N S 114 
GLU   C    C N N 115 
GLU   O    O N N 116 
GLU   CB   C N N 117 
GLU   CG   C N N 118 
GLU   CD   C N N 119 
GLU   OE1  O N N 120 
GLU   OE2  O N N 121 
GLU   OXT  O N N 122 
GLU   H    H N N 123 
GLU   H2   H N N 124 
GLU   HA   H N N 125 
GLU   HB2  H N N 126 
GLU   HB3  H N N 127 
GLU   HG2  H N N 128 
GLU   HG3  H N N 129 
GLU   HE2  H N N 130 
GLU   HXT  H N N 131 
GLY   N    N N N 132 
GLY   CA   C N N 133 
GLY   C    C N N 134 
GLY   O    O N N 135 
GLY   OXT  O N N 136 
GLY   H    H N N 137 
GLY   H2   H N N 138 
GLY   HA2  H N N 139 
GLY   HA3  H N N 140 
GLY   HXT  H N N 141 
HIS   N    N N N 142 
HIS   CA   C N S 143 
HIS   C    C N N 144 
HIS   O    O N N 145 
HIS   CB   C N N 146 
HIS   CG   C Y N 147 
HIS   ND1  N Y N 148 
HIS   CD2  C Y N 149 
HIS   CE1  C Y N 150 
HIS   NE2  N Y N 151 
HIS   OXT  O N N 152 
HIS   H    H N N 153 
HIS   H2   H N N 154 
HIS   HA   H N N 155 
HIS   HB2  H N N 156 
HIS   HB3  H N N 157 
HIS   HD1  H N N 158 
HIS   HD2  H N N 159 
HIS   HE1  H N N 160 
HIS   HE2  H N N 161 
HIS   HXT  H N N 162 
HOH   O    O N N 163 
HOH   H1   H N N 164 
HOH   H2   H N N 165 
ILE   N    N N N 166 
ILE   CA   C N S 167 
ILE   C    C N N 168 
ILE   O    O N N 169 
ILE   CB   C N S 170 
ILE   CG1  C N N 171 
ILE   CG2  C N N 172 
ILE   CD1  C N N 173 
ILE   OXT  O N N 174 
ILE   H    H N N 175 
ILE   H2   H N N 176 
ILE   HA   H N N 177 
ILE   HB   H N N 178 
ILE   HG12 H N N 179 
ILE   HG13 H N N 180 
ILE   HG21 H N N 181 
ILE   HG22 H N N 182 
ILE   HG23 H N N 183 
ILE   HD11 H N N 184 
ILE   HD12 H N N 185 
ILE   HD13 H N N 186 
ILE   HXT  H N N 187 
LEU   N    N N N 188 
LEU   CA   C N S 189 
LEU   C    C N N 190 
LEU   O    O N N 191 
LEU   CB   C N N 192 
LEU   CG   C N N 193 
LEU   CD1  C N N 194 
LEU   CD2  C N N 195 
LEU   OXT  O N N 196 
LEU   H    H N N 197 
LEU   H2   H N N 198 
LEU   HA   H N N 199 
LEU   HB2  H N N 200 
LEU   HB3  H N N 201 
LEU   HG   H N N 202 
LEU   HD11 H N N 203 
LEU   HD12 H N N 204 
LEU   HD13 H N N 205 
LEU   HD21 H N N 206 
LEU   HD22 H N N 207 
LEU   HD23 H N N 208 
LEU   HXT  H N N 209 
LYS   N    N N N 210 
LYS   CA   C N S 211 
LYS   C    C N N 212 
LYS   O    O N N 213 
LYS   CB   C N N 214 
LYS   CG   C N N 215 
LYS   CD   C N N 216 
LYS   CE   C N N 217 
LYS   NZ   N N N 218 
LYS   OXT  O N N 219 
LYS   H    H N N 220 
LYS   H2   H N N 221 
LYS   HA   H N N 222 
LYS   HB2  H N N 223 
LYS   HB3  H N N 224 
LYS   HG2  H N N 225 
LYS   HG3  H N N 226 
LYS   HD2  H N N 227 
LYS   HD3  H N N 228 
LYS   HE2  H N N 229 
LYS   HE3  H N N 230 
LYS   HZ1  H N N 231 
LYS   HZ2  H N N 232 
LYS   HZ3  H N N 233 
LYS   HXT  H N N 234 
MET   N    N N N 235 
MET   CA   C N S 236 
MET   C    C N N 237 
MET   O    O N N 238 
MET   CB   C N N 239 
MET   CG   C N N 240 
MET   SD   S N N 241 
MET   CE   C N N 242 
MET   OXT  O N N 243 
MET   H    H N N 244 
MET   H2   H N N 245 
MET   HA   H N N 246 
MET   HB2  H N N 247 
MET   HB3  H N N 248 
MET   HG2  H N N 249 
MET   HG3  H N N 250 
MET   HE1  H N N 251 
MET   HE2  H N N 252 
MET   HE3  H N N 253 
MET   HXT  H N N 254 
PHE   N    N N N 255 
PHE   CA   C N S 256 
PHE   C    C N N 257 
PHE   O    O N N 258 
PHE   CB   C N N 259 
PHE   CG   C Y N 260 
PHE   CD1  C Y N 261 
PHE   CD2  C Y N 262 
PHE   CE1  C Y N 263 
PHE   CE2  C Y N 264 
PHE   CZ   C Y N 265 
PHE   OXT  O N N 266 
PHE   H    H N N 267 
PHE   H2   H N N 268 
PHE   HA   H N N 269 
PHE   HB2  H N N 270 
PHE   HB3  H N N 271 
PHE   HD1  H N N 272 
PHE   HD2  H N N 273 
PHE   HE1  H N N 274 
PHE   HE2  H N N 275 
PHE   HZ   H N N 276 
PHE   HXT  H N N 277 
PRO   N    N N N 278 
PRO   CA   C N S 279 
PRO   C    C N N 280 
PRO   O    O N N 281 
PRO   CB   C N N 282 
PRO   CG   C N N 283 
PRO   CD   C N N 284 
PRO   OXT  O N N 285 
PRO   H    H N N 286 
PRO   HA   H N N 287 
PRO   HB2  H N N 288 
PRO   HB3  H N N 289 
PRO   HG2  H N N 290 
PRO   HG3  H N N 291 
PRO   HD2  H N N 292 
PRO   HD3  H N N 293 
PRO   HXT  H N N 294 
SER   N    N N N 295 
SER   CA   C N S 296 
SER   C    C N N 297 
SER   O    O N N 298 
SER   CB   C N N 299 
SER   OG   O N N 300 
SER   OXT  O N N 301 
SER   H    H N N 302 
SER   H2   H N N 303 
SER   HA   H N N 304 
SER   HB2  H N N 305 
SER   HB3  H N N 306 
SER   HG   H N N 307 
SER   HXT  H N N 308 
THR   N    N N N 309 
THR   CA   C N S 310 
THR   C    C N N 311 
THR   O    O N N 312 
THR   CB   C N R 313 
THR   OG1  O N N 314 
THR   CG2  C N N 315 
THR   OXT  O N N 316 
THR   H    H N N 317 
THR   H2   H N N 318 
THR   HA   H N N 319 
THR   HB   H N N 320 
THR   HG1  H N N 321 
THR   HG21 H N N 322 
THR   HG22 H N N 323 
THR   HG23 H N N 324 
THR   HXT  H N N 325 
TRP   N    N N N 326 
TRP   CA   C N S 327 
TRP   C    C N N 328 
TRP   O    O N N 329 
TRP   CB   C N N 330 
TRP   CG   C Y N 331 
TRP   CD1  C Y N 332 
TRP   CD2  C Y N 333 
TRP   NE1  N Y N 334 
TRP   CE2  C Y N 335 
TRP   CE3  C Y N 336 
TRP   CZ2  C Y N 337 
TRP   CZ3  C Y N 338 
TRP   CH2  C Y N 339 
TRP   OXT  O N N 340 
TRP   H    H N N 341 
TRP   H2   H N N 342 
TRP   HA   H N N 343 
TRP   HB2  H N N 344 
TRP   HB3  H N N 345 
TRP   HD1  H N N 346 
TRP   HE1  H N N 347 
TRP   HE3  H N N 348 
TRP   HZ2  H N N 349 
TRP   HZ3  H N N 350 
TRP   HH2  H N N 351 
TRP   HXT  H N N 352 
TYR   N    N N N 353 
TYR   CA   C N S 354 
TYR   C    C N N 355 
TYR   O    O N N 356 
TYR   CB   C N N 357 
TYR   CG   C Y N 358 
TYR   CD1  C Y N 359 
TYR   CD2  C Y N 360 
TYR   CE1  C Y N 361 
TYR   CE2  C Y N 362 
TYR   CZ   C Y N 363 
TYR   OH   O N N 364 
TYR   OXT  O N N 365 
TYR   H    H N N 366 
TYR   H2   H N N 367 
TYR   HA   H N N 368 
TYR   HB2  H N N 369 
TYR   HB3  H N N 370 
TYR   HD1  H N N 371 
TYR   HD2  H N N 372 
TYR   HE1  H N N 373 
TYR   HE2  H N N 374 
TYR   HH   H N N 375 
TYR   HXT  H N N 376 
VAL   N    N N N 377 
VAL   CA   C N S 378 
VAL   C    C N N 379 
VAL   O    O N N 380 
VAL   CB   C N N 381 
VAL   CG1  C N N 382 
VAL   CG2  C N N 383 
VAL   OXT  O N N 384 
VAL   H    H N N 385 
VAL   H2   H N N 386 
VAL   HA   H N N 387 
VAL   HB   H N N 388 
VAL   HG11 H N N 389 
VAL   HG12 H N N 390 
VAL   HG13 H N N 391 
VAL   HG21 H N N 392 
VAL   HG22 H N N 393 
VAL   HG23 H N N 394 
VAL   HXT  H N N 395 
# 
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 
A1AX5 F1  C1   sing N N 1   
A1AX5 C1  C2   doub Y N 2   
A1AX5 C2  C3   sing Y N 3   
A1AX5 C3  C4   doub Y N 4   
A1AX5 C4  C5   sing Y N 5   
A1AX5 C5  N1   sing N N 6   
A1AX5 N1  C6   sing Y N 7   
A1AX5 C6  C7   doub Y N 8   
A1AX5 C7  N2   sing Y N 9   
A1AX5 N2  C8   doub Y N 10  
A1AX5 C5  C9   doub Y N 11  
A1AX5 C1  C9   sing Y N 12  
A1AX5 N1  C8   sing Y N 13  
A1AX5 C4  H3   sing N N 14  
A1AX5 C6  H4   sing N N 15  
A1AX5 C7  H5   sing N N 16  
A1AX5 C8  H6   sing N N 17  
A1AX5 C2  H1   sing N N 18  
A1AX5 C3  H2   sing N N 19  
A1AX5 C9  H7   sing N N 20  
ALA   N   CA   sing N N 21  
ALA   N   H    sing N N 22  
ALA   N   H2   sing N N 23  
ALA   CA  C    sing N N 24  
ALA   CA  CB   sing N N 25  
ALA   CA  HA   sing N N 26  
ALA   C   O    doub N N 27  
ALA   C   OXT  sing N N 28  
ALA   CB  HB1  sing N N 29  
ALA   CB  HB2  sing N N 30  
ALA   CB  HB3  sing N N 31  
ALA   OXT HXT  sing N N 32  
ARG   N   CA   sing N N 33  
ARG   N   H    sing N N 34  
ARG   N   H2   sing N N 35  
ARG   CA  C    sing N N 36  
ARG   CA  CB   sing N N 37  
ARG   CA  HA   sing N N 38  
ARG   C   O    doub N N 39  
ARG   C   OXT  sing N N 40  
ARG   CB  CG   sing N N 41  
ARG   CB  HB2  sing N N 42  
ARG   CB  HB3  sing N N 43  
ARG   CG  CD   sing N N 44  
ARG   CG  HG2  sing N N 45  
ARG   CG  HG3  sing N N 46  
ARG   CD  NE   sing N N 47  
ARG   CD  HD2  sing N N 48  
ARG   CD  HD3  sing N N 49  
ARG   NE  CZ   sing N N 50  
ARG   NE  HE   sing N N 51  
ARG   CZ  NH1  sing N N 52  
ARG   CZ  NH2  doub N N 53  
ARG   NH1 HH11 sing N N 54  
ARG   NH1 HH12 sing N N 55  
ARG   NH2 HH21 sing N N 56  
ARG   NH2 HH22 sing N N 57  
ARG   OXT HXT  sing N N 58  
ASN   N   CA   sing N N 59  
ASN   N   H    sing N N 60  
ASN   N   H2   sing N N 61  
ASN   CA  C    sing N N 62  
ASN   CA  CB   sing N N 63  
ASN   CA  HA   sing N N 64  
ASN   C   O    doub N N 65  
ASN   C   OXT  sing N N 66  
ASN   CB  CG   sing N N 67  
ASN   CB  HB2  sing N N 68  
ASN   CB  HB3  sing N N 69  
ASN   CG  OD1  doub N N 70  
ASN   CG  ND2  sing N N 71  
ASN   ND2 HD21 sing N N 72  
ASN   ND2 HD22 sing N N 73  
ASN   OXT HXT  sing N N 74  
ASP   N   CA   sing N N 75  
ASP   N   H    sing N N 76  
ASP   N   H2   sing N N 77  
ASP   CA  C    sing N N 78  
ASP   CA  CB   sing N N 79  
ASP   CA  HA   sing N N 80  
ASP   C   O    doub N N 81  
ASP   C   OXT  sing N N 82  
ASP   CB  CG   sing N N 83  
ASP   CB  HB2  sing N N 84  
ASP   CB  HB3  sing N N 85  
ASP   CG  OD1  doub N N 86  
ASP   CG  OD2  sing N N 87  
ASP   OD2 HD2  sing N N 88  
ASP   OXT HXT  sing N N 89  
GLN   N   CA   sing N N 90  
GLN   N   H    sing N N 91  
GLN   N   H2   sing N N 92  
GLN   CA  C    sing N N 93  
GLN   CA  CB   sing N N 94  
GLN   CA  HA   sing N N 95  
GLN   C   O    doub N N 96  
GLN   C   OXT  sing N N 97  
GLN   CB  CG   sing N N 98  
GLN   CB  HB2  sing N N 99  
GLN   CB  HB3  sing N N 100 
GLN   CG  CD   sing N N 101 
GLN   CG  HG2  sing N N 102 
GLN   CG  HG3  sing N N 103 
GLN   CD  OE1  doub N N 104 
GLN   CD  NE2  sing N N 105 
GLN   NE2 HE21 sing N N 106 
GLN   NE2 HE22 sing N N 107 
GLN   OXT HXT  sing N N 108 
GLU   N   CA   sing N N 109 
GLU   N   H    sing N N 110 
GLU   N   H2   sing N N 111 
GLU   CA  C    sing N N 112 
GLU   CA  CB   sing N N 113 
GLU   CA  HA   sing N N 114 
GLU   C   O    doub N N 115 
GLU   C   OXT  sing N N 116 
GLU   CB  CG   sing N N 117 
GLU   CB  HB2  sing N N 118 
GLU   CB  HB3  sing N N 119 
GLU   CG  CD   sing N N 120 
GLU   CG  HG2  sing N N 121 
GLU   CG  HG3  sing N N 122 
GLU   CD  OE1  doub N N 123 
GLU   CD  OE2  sing N N 124 
GLU   OE2 HE2  sing N N 125 
GLU   OXT HXT  sing N N 126 
GLY   N   CA   sing N N 127 
GLY   N   H    sing N N 128 
GLY   N   H2   sing N N 129 
GLY   CA  C    sing N N 130 
GLY   CA  HA2  sing N N 131 
GLY   CA  HA3  sing N N 132 
GLY   C   O    doub N N 133 
GLY   C   OXT  sing N N 134 
GLY   OXT HXT  sing N N 135 
HIS   N   CA   sing N N 136 
HIS   N   H    sing N N 137 
HIS   N   H2   sing N N 138 
HIS   CA  C    sing N N 139 
HIS   CA  CB   sing N N 140 
HIS   CA  HA   sing N N 141 
HIS   C   O    doub N N 142 
HIS   C   OXT  sing N N 143 
HIS   CB  CG   sing N N 144 
HIS   CB  HB2  sing N N 145 
HIS   CB  HB3  sing N N 146 
HIS   CG  ND1  sing Y N 147 
HIS   CG  CD2  doub Y N 148 
HIS   ND1 CE1  doub Y N 149 
HIS   ND1 HD1  sing N N 150 
HIS   CD2 NE2  sing Y N 151 
HIS   CD2 HD2  sing N N 152 
HIS   CE1 NE2  sing Y N 153 
HIS   CE1 HE1  sing N N 154 
HIS   NE2 HE2  sing N N 155 
HIS   OXT HXT  sing N N 156 
HOH   O   H1   sing N N 157 
HOH   O   H2   sing N N 158 
ILE   N   CA   sing N N 159 
ILE   N   H    sing N N 160 
ILE   N   H2   sing N N 161 
ILE   CA  C    sing N N 162 
ILE   CA  CB   sing N N 163 
ILE   CA  HA   sing N N 164 
ILE   C   O    doub N N 165 
ILE   C   OXT  sing N N 166 
ILE   CB  CG1  sing N N 167 
ILE   CB  CG2  sing N N 168 
ILE   CB  HB   sing N N 169 
ILE   CG1 CD1  sing N N 170 
ILE   CG1 HG12 sing N N 171 
ILE   CG1 HG13 sing N N 172 
ILE   CG2 HG21 sing N N 173 
ILE   CG2 HG22 sing N N 174 
ILE   CG2 HG23 sing N N 175 
ILE   CD1 HD11 sing N N 176 
ILE   CD1 HD12 sing N N 177 
ILE   CD1 HD13 sing N N 178 
ILE   OXT HXT  sing N N 179 
LEU   N   CA   sing N N 180 
LEU   N   H    sing N N 181 
LEU   N   H2   sing N N 182 
LEU   CA  C    sing N N 183 
LEU   CA  CB   sing N N 184 
LEU   CA  HA   sing N N 185 
LEU   C   O    doub N N 186 
LEU   C   OXT  sing N N 187 
LEU   CB  CG   sing N N 188 
LEU   CB  HB2  sing N N 189 
LEU   CB  HB3  sing N N 190 
LEU   CG  CD1  sing N N 191 
LEU   CG  CD2  sing N N 192 
LEU   CG  HG   sing N N 193 
LEU   CD1 HD11 sing N N 194 
LEU   CD1 HD12 sing N N 195 
LEU   CD1 HD13 sing N N 196 
LEU   CD2 HD21 sing N N 197 
LEU   CD2 HD22 sing N N 198 
LEU   CD2 HD23 sing N N 199 
LEU   OXT HXT  sing N N 200 
LYS   N   CA   sing N N 201 
LYS   N   H    sing N N 202 
LYS   N   H2   sing N N 203 
LYS   CA  C    sing N N 204 
LYS   CA  CB   sing N N 205 
LYS   CA  HA   sing N N 206 
LYS   C   O    doub N N 207 
LYS   C   OXT  sing N N 208 
LYS   CB  CG   sing N N 209 
LYS   CB  HB2  sing N N 210 
LYS   CB  HB3  sing N N 211 
LYS   CG  CD   sing N N 212 
LYS   CG  HG2  sing N N 213 
LYS   CG  HG3  sing N N 214 
LYS   CD  CE   sing N N 215 
LYS   CD  HD2  sing N N 216 
LYS   CD  HD3  sing N N 217 
LYS   CE  NZ   sing N N 218 
LYS   CE  HE2  sing N N 219 
LYS   CE  HE3  sing N N 220 
LYS   NZ  HZ1  sing N N 221 
LYS   NZ  HZ2  sing N N 222 
LYS   NZ  HZ3  sing N N 223 
LYS   OXT HXT  sing N N 224 
MET   N   CA   sing N N 225 
MET   N   H    sing N N 226 
MET   N   H2   sing N N 227 
MET   CA  C    sing N N 228 
MET   CA  CB   sing N N 229 
MET   CA  HA   sing N N 230 
MET   C   O    doub N N 231 
MET   C   OXT  sing N N 232 
MET   CB  CG   sing N N 233 
MET   CB  HB2  sing N N 234 
MET   CB  HB3  sing N N 235 
MET   CG  SD   sing N N 236 
MET   CG  HG2  sing N N 237 
MET   CG  HG3  sing N N 238 
MET   SD  CE   sing N N 239 
MET   CE  HE1  sing N N 240 
MET   CE  HE2  sing N N 241 
MET   CE  HE3  sing N N 242 
MET   OXT HXT  sing N N 243 
PHE   N   CA   sing N N 244 
PHE   N   H    sing N N 245 
PHE   N   H2   sing N N 246 
PHE   CA  C    sing N N 247 
PHE   CA  CB   sing N N 248 
PHE   CA  HA   sing N N 249 
PHE   C   O    doub N N 250 
PHE   C   OXT  sing N N 251 
PHE   CB  CG   sing N N 252 
PHE   CB  HB2  sing N N 253 
PHE   CB  HB3  sing N N 254 
PHE   CG  CD1  doub Y N 255 
PHE   CG  CD2  sing Y N 256 
PHE   CD1 CE1  sing Y N 257 
PHE   CD1 HD1  sing N N 258 
PHE   CD2 CE2  doub Y N 259 
PHE   CD2 HD2  sing N N 260 
PHE   CE1 CZ   doub Y N 261 
PHE   CE1 HE1  sing N N 262 
PHE   CE2 CZ   sing Y N 263 
PHE   CE2 HE2  sing N N 264 
PHE   CZ  HZ   sing N N 265 
PHE   OXT HXT  sing N N 266 
PRO   N   CA   sing N N 267 
PRO   N   CD   sing N N 268 
PRO   N   H    sing N N 269 
PRO   CA  C    sing N N 270 
PRO   CA  CB   sing N N 271 
PRO   CA  HA   sing N N 272 
PRO   C   O    doub N N 273 
PRO   C   OXT  sing N N 274 
PRO   CB  CG   sing N N 275 
PRO   CB  HB2  sing N N 276 
PRO   CB  HB3  sing N N 277 
PRO   CG  CD   sing N N 278 
PRO   CG  HG2  sing N N 279 
PRO   CG  HG3  sing N N 280 
PRO   CD  HD2  sing N N 281 
PRO   CD  HD3  sing N N 282 
PRO   OXT HXT  sing N N 283 
SER   N   CA   sing N N 284 
SER   N   H    sing N N 285 
SER   N   H2   sing N N 286 
SER   CA  C    sing N N 287 
SER   CA  CB   sing N N 288 
SER   CA  HA   sing N N 289 
SER   C   O    doub N N 290 
SER   C   OXT  sing N N 291 
SER   CB  OG   sing N N 292 
SER   CB  HB2  sing N N 293 
SER   CB  HB3  sing N N 294 
SER   OG  HG   sing N N 295 
SER   OXT HXT  sing N N 296 
THR   N   CA   sing N N 297 
THR   N   H    sing N N 298 
THR   N   H2   sing N N 299 
THR   CA  C    sing N N 300 
THR   CA  CB   sing N N 301 
THR   CA  HA   sing N N 302 
THR   C   O    doub N N 303 
THR   C   OXT  sing N N 304 
THR   CB  OG1  sing N N 305 
THR   CB  CG2  sing N N 306 
THR   CB  HB   sing N N 307 
THR   OG1 HG1  sing N N 308 
THR   CG2 HG21 sing N N 309 
THR   CG2 HG22 sing N N 310 
THR   CG2 HG23 sing N N 311 
THR   OXT HXT  sing N N 312 
TRP   N   CA   sing N N 313 
TRP   N   H    sing N N 314 
TRP   N   H2   sing N N 315 
TRP   CA  C    sing N N 316 
TRP   CA  CB   sing N N 317 
TRP   CA  HA   sing N N 318 
TRP   C   O    doub N N 319 
TRP   C   OXT  sing N N 320 
TRP   CB  CG   sing N N 321 
TRP   CB  HB2  sing N N 322 
TRP   CB  HB3  sing N N 323 
TRP   CG  CD1  doub Y N 324 
TRP   CG  CD2  sing Y N 325 
TRP   CD1 NE1  sing Y N 326 
TRP   CD1 HD1  sing N N 327 
TRP   CD2 CE2  doub Y N 328 
TRP   CD2 CE3  sing Y N 329 
TRP   NE1 CE2  sing Y N 330 
TRP   NE1 HE1  sing N N 331 
TRP   CE2 CZ2  sing Y N 332 
TRP   CE3 CZ3  doub Y N 333 
TRP   CE3 HE3  sing N N 334 
TRP   CZ2 CH2  doub Y N 335 
TRP   CZ2 HZ2  sing N N 336 
TRP   CZ3 CH2  sing Y N 337 
TRP   CZ3 HZ3  sing N N 338 
TRP   CH2 HH2  sing N N 339 
TRP   OXT HXT  sing N N 340 
TYR   N   CA   sing N N 341 
TYR   N   H    sing N N 342 
TYR   N   H2   sing N N 343 
TYR   CA  C    sing N N 344 
TYR   CA  CB   sing N N 345 
TYR   CA  HA   sing N N 346 
TYR   C   O    doub N N 347 
TYR   C   OXT  sing N N 348 
TYR   CB  CG   sing N N 349 
TYR   CB  HB2  sing N N 350 
TYR   CB  HB3  sing N N 351 
TYR   CG  CD1  doub Y N 352 
TYR   CG  CD2  sing Y N 353 
TYR   CD1 CE1  sing Y N 354 
TYR   CD1 HD1  sing N N 355 
TYR   CD2 CE2  doub Y N 356 
TYR   CD2 HD2  sing N N 357 
TYR   CE1 CZ   doub Y N 358 
TYR   CE1 HE1  sing N N 359 
TYR   CE2 CZ   sing Y N 360 
TYR   CE2 HE2  sing N N 361 
TYR   CZ  OH   sing N N 362 
TYR   OH  HH   sing N N 363 
TYR   OXT HXT  sing N N 364 
VAL   N   CA   sing N N 365 
VAL   N   H    sing N N 366 
VAL   N   H2   sing N N 367 
VAL   CA  C    sing N N 368 
VAL   CA  CB   sing N N 369 
VAL   CA  HA   sing N N 370 
VAL   C   O    doub N N 371 
VAL   C   OXT  sing N N 372 
VAL   CB  CG1  sing N N 373 
VAL   CB  CG2  sing N N 374 
VAL   CB  HB   sing N N 375 
VAL   CG1 HG11 sing N N 376 
VAL   CG1 HG12 sing N N 377 
VAL   CG1 HG13 sing N N 378 
VAL   CG2 HG21 sing N N 379 
VAL   CG2 HG22 sing N N 380 
VAL   CG2 HG23 sing N N 381 
VAL   OXT HXT  sing N N 382 
# 
_pdbx_audit_support.funding_organization   'National Natural Science Foundation of China (NSFC)' 
_pdbx_audit_support.country                China 
_pdbx_audit_support.grant_number           2021YFC2301405 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_deposit_group.group_title         'Crystallographic fragment screening of Human heat shock protein 90' 
_pdbx_deposit_group.group_description   
;Heat shock protein 90 (HSP90) is one of the most active molecular chaperones in cells. It plays a vital role in the cell maturation process and serves as a molecular chaperone involved in many oncogenic proteins folding, assembly and stabilization. Many HSP90 client proteins are kinases or transcription factors involved in signal transduction pathways and are key regulatory factors in tumor growth and maintenance. Therefore, HSP90 inhibitors can be used as drugs for cancer treatment.
;
_pdbx_deposit_group.group_type          'changed state' 
_pdbx_deposit_group.group_id            G_1002298 
# 
_space_group.name_H-M_alt     'I 2 2 2' 
_space_group.name_Hall        'I 2 2' 
_space_group.IT_number        23 
_space_group.crystal_system   orthorhombic 
_space_group.id               1 
# 
_atom_sites.entry_id                    7HAM 
_atom_sites.fract_transf_matrix[1][1]   0.014899 
_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]   0.010923 
_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]   0.010110 
_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.
;
? 
F ? ? 4.90428 4.07044 ? ? 12.99538 1.63651  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
N ? ? 4.01032 2.96436 ? ? 19.97189 1.75589  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O ? ? 4.49882 3.47563 ? ? 15.80542 1.70748  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
S ? ? 9.55732 6.39887 ? ? 1.23737  29.19336 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N   . GLU   A 1 9   ? 5.88843   -29.07721 -38.50093 1.000 54.52499 ? 16  GLU   A N   1 
ATOM   2    C CA  . GLU   A 1 9   ? 7.23767   -28.53323 -38.57912 1.000 57.37264 ? 16  GLU   A CA  1 
ATOM   3    C C   . GLU   A 1 9   ? 7.49736   -27.62159 -37.37832 1.000 49.94910 ? 16  GLU   A C   1 
ATOM   4    O O   . GLU   A 1 9   ? 7.02297   -26.48563 -37.32325 1.000 49.79404 ? 16  GLU   A O   1 
ATOM   5    C CB  . GLU   A 1 9   ? 7.43488   -27.77958 -39.89556 1.000 56.65568 ? 16  GLU   A CB  1 
ATOM   6    C CG  . GLU   A 1 9   ? 8.85893   -27.81305 -40.42640 1.000 74.51889 ? 16  GLU   A CG  1 
ATOM   7    C CD  . GLU   A 1 9   ? 9.70821   -26.68491 -39.88893 1.000 71.59767 ? 16  GLU   A CD  1 
ATOM   8    O OE1 . GLU   A 1 9   ? 9.15784   -25.81138 -39.18914 1.000 78.77795 ? 16  GLU   A OE1 1 
ATOM   9    O OE2 . GLU   A 1 9   ? 10.92753  -26.67471 -40.16027 1.000 76.92801 ? 16  GLU   A OE2 1 
ATOM   10   N N   . VAL   A 1 10  ? 8.25640   -28.13574 -36.41706 1.000 34.36810 ? 17  VAL   A N   1 
ATOM   11   C CA  . VAL   A 1 10  ? 8.49705   -27.46386 -35.14595 1.000 32.31868 ? 17  VAL   A CA  1 
ATOM   12   C C   . VAL   A 1 10  ? 9.87713   -26.82248 -35.18782 1.000 34.25194 ? 17  VAL   A C   1 
ATOM   13   O O   . VAL   A 1 10  ? 10.87688  -27.50033 -35.45027 1.000 33.82594 ? 17  VAL   A O   1 
ATOM   14   C CB  . VAL   A 1 10  ? 8.38645   -28.44877 -33.97301 1.000 39.17003 ? 17  VAL   A CB  1 
ATOM   15   C CG1 . VAL   A 1 10  ? 8.69503   -27.74912 -32.65487 1.000 30.14044 ? 17  VAL   A CG1 1 
ATOM   16   C CG2 . VAL   A 1 10  ? 7.01282   -29.10015 -33.95980 1.000 47.65976 ? 17  VAL   A CG2 1 
ATOM   17   N N   . GLU   A 1 11  ? 9.94045   -25.52140 -34.92440 1.000 27.77613 ? 18  GLU   A N   1 
ATOM   18   C CA  . GLU   A 1 11  ? 11.20510  -24.80195 -34.84144 1.000 24.58218 ? 18  GLU   A CA  1 
ATOM   19   C C   . GLU   A 1 11  ? 11.56837  -24.59448 -33.37815 1.000 27.00408 ? 18  GLU   A C   1 
ATOM   20   O O   . GLU   A 1 11  ? 10.72360  -24.18074 -32.57839 1.000 22.69703 ? 18  GLU   A O   1 
ATOM   21   C CB  . GLU   A 1 11  ? 11.12724  -23.45533 -35.56467 1.000 25.68721 ? 18  GLU   A CB  1 
ATOM   22   C CG  . GLU   A 1 11  ? 11.00041  -23.56502 -37.07741 1.000 28.36440 ? 18  GLU   A CG  1 
ATOM   23   C CD  . GLU   A 1 11  ? 10.91975  -22.20807 -37.75840 1.000 41.11092 ? 18  GLU   A CD  1 
ATOM   24   O OE1 . GLU   A 1 11  ? 9.92990   -21.48121 -37.53129 1.000 42.07933 ? 18  GLU   A OE1 1 
ATOM   25   O OE2 . GLU   A 1 11  ? 11.85151  -21.86757 -38.51821 1.000 48.89649 ? 18  GLU   A OE2 1 
ATOM   26   N N   . THR   A 1 12  ? 12.81742  -24.88690 -33.03026 1.000 22.39785 ? 19  THR   A N   1 
ATOM   27   C CA  . THR   A 1 12  ? 13.30637  -24.74279 -31.66613 1.000 21.26664 ? 19  THR   A CA  1 
ATOM   28   C C   . THR   A 1 12  ? 14.28169  -23.57789 -31.60176 1.000 20.51940 ? 19  THR   A C   1 
ATOM   29   O O   . THR   A 1 12  ? 15.18368  -23.47124 -32.43980 1.000 20.97943 ? 19  THR   A O   1 
ATOM   30   C CB  . THR   A 1 12  ? 13.98262  -26.02765 -31.18512 1.000 22.54075 ? 19  THR   A CB  1 
ATOM   31   O OG1 . THR   A 1 12  ? 13.07341  -27.12766 -31.32985 1.000 23.29502 ? 19  THR   A OG1 1 
ATOM   32   C CG2 . THR   A 1 12  ? 14.39547  -25.89934 -29.72341 1.000 21.14509 ? 19  THR   A CG2 1 
ATOM   33   N N   . PHE   A 1 13  ? 14.10144  -22.71460 -30.60644 1.000 19.34123 ? 20  PHE   A N   1 
ATOM   34   C CA  . PHE   A 1 13  ? 14.90156  -21.51179 -30.45064 1.000 21.91021 ? 20  PHE   A CA  1 
ATOM   35   C C   . PHE   A 1 13  ? 15.49758  -21.47501 -29.05461 1.000 25.23799 ? 20  PHE   A C   1 
ATOM   36   O O   . PHE   A 1 13  ? 14.90588  -21.98072 -28.09778 1.000 21.11051 ? 20  PHE   A O   1 
ATOM   37   C CB  . PHE   A 1 13  ? 14.06357  -20.25187 -30.65262 1.000 19.59802 ? 20  PHE   A CB  1 
ATOM   38   C CG  . PHE   A 1 13  ? 13.35980  -20.19305 -31.97385 1.000 20.75318 ? 20  PHE   A CG  1 
ATOM   39   C CD1 . PHE   A 1 13  ? 12.11379  -20.77896 -32.12955 1.000 23.96834 ? 20  PHE   A CD1 1 
ATOM   40   C CD2 . PHE   A 1 13  ? 13.92011  -19.52747 -33.04914 1.000 23.39735 ? 20  PHE   A CD2 1 
ATOM   41   C CE1 . PHE   A 1 13  ? 11.44800  -20.72290 -33.34161 1.000 21.29865 ? 20  PHE   A CE1 1 
ATOM   42   C CE2 . PHE   A 1 13  ? 13.25786  -19.46152 -34.26470 1.000 29.32919 ? 20  PHE   A CE2 1 
ATOM   43   C CZ  . PHE   A 1 13  ? 12.02153  -20.06363 -34.40980 1.000 26.40243 ? 20  PHE   A CZ  1 
ATOM   44   N N   . ALA   A 1 14  ? 16.66022  -20.84656 -28.93924 1.000 21.21643 ? 21  ALA   A N   1 
ATOM   45   C CA  . ALA   A 1 14  ? 17.24417  -20.56933 -27.63870 1.000 21.78294 ? 21  ALA   A CA  1 
ATOM   46   C C   . ALA   A 1 14  ? 16.75020  -19.22215 -27.13411 1.000 24.79931 ? 21  ALA   A C   1 
ATOM   47   O O   . ALA   A 1 14  ? 16.70931  -18.24027 -27.88438 1.000 24.07118 ? 21  ALA   A O   1 
ATOM   48   C CB  . ALA   A 1 14  ? 18.77137  -20.57418 -27.71284 1.000 25.28584 ? 21  ALA   A CB  1 
ATOM   49   N N   . PHE   A 1 15  ? 16.34927  -19.18696 -25.86510 1.000 21.40563 ? 22  PHE   A N   1 
ATOM   50   C CA  . PHE   A 1 15  ? 16.11485  -17.90843 -25.21755 1.000 22.18475 ? 22  PHE   A CA  1 
ATOM   51   C C   . PHE   A 1 15  ? 17.40021  -17.09450 -25.23470 1.000 23.44863 ? 22  PHE   A C   1 
ATOM   52   O O   . PHE   A 1 15  ? 18.50567  -17.64405 -25.21959 1.000 24.86552 ? 22  PHE   A O   1 
ATOM   53   C CB  . PHE   A 1 15  ? 15.66240  -18.10254 -23.76924 1.000 22.89924 ? 22  PHE   A CB  1 
ATOM   54   C CG  . PHE   A 1 15  ? 14.23159  -18.53808 -23.62202 1.000 23.27375 ? 22  PHE   A CG  1 
ATOM   55   C CD1 . PHE   A 1 15  ? 13.19437  -17.67952 -23.93956 1.000 22.53988 ? 22  PHE   A CD1 1 
ATOM   56   C CD2 . PHE   A 1 15  ? 13.92535  -19.79830 -23.13284 1.000 22.18592 ? 22  PHE   A CD2 1 
ATOM   57   C CE1 . PHE   A 1 15  ? 11.87362  -18.07745 -23.79424 1.000 21.53660 ? 22  PHE   A CE1 1 
ATOM   58   C CE2 . PHE   A 1 15  ? 12.61197  -20.20251 -22.98367 1.000 21.26184 ? 22  PHE   A CE2 1 
ATOM   59   C CZ  . PHE   A 1 15  ? 11.58444  -19.34114 -23.31505 1.000 20.04273 ? 22  PHE   A CZ  1 
ATOM   60   N N   . GLN   A 1 16  ? 17.25514  -15.77279 -25.26825 1.000 22.72035 ? 23  GLN   A N   1 
ATOM   61   C CA  . GLN   A 1 16  ? 18.39072  -14.92256 -24.95270 1.000 24.00396 ? 23  GLN   A CA  1 
ATOM   62   C C   . GLN   A 1 16  ? 18.92235  -15.29604 -23.57578 1.000 23.28743 ? 23  GLN   A C   1 
ATOM   63   O O   . GLN   A 1 16  ? 18.16336  -15.69810 -22.68921 1.000 26.04062 ? 23  GLN   A O   1 
ATOM   64   C CB  . GLN   A 1 16  ? 17.98793  -13.44913 -24.98111 1.000 27.21070 ? 23  GLN   A CB  1 
ATOM   65   C CG  . GLN   A 1 16  ? 17.75880  -12.88190 -26.37084 1.000 29.51178 ? 23  GLN   A CG  1 
ATOM   66   C CD  . GLN   A 1 16  ? 17.10923  -11.51389 -26.32879 1.000 36.59671 ? 23  GLN   A CD  1 
ATOM   67   O OE1 . GLN   A 1 16  ? 17.75740  -10.49796 -26.58124 1.000 39.15401 ? 23  GLN   A OE1 1 
ATOM   68   N NE2 . GLN   A 1 16  ? 15.82591  -11.47911 -25.99230 1.000 31.58985 ? 23  GLN   A NE2 1 
ATOM   69   N N   . ALA   A 1 17  ? 20.24221  -15.18477 -23.40377 1.000 23.87950 ? 24  ALA   A N   1 
ATOM   70   C CA  . ALA   A 1 17  ? 20.85111  -15.55972 -22.13029 1.000 29.02628 ? 24  ALA   A CA  1 
ATOM   71   C C   . ALA   A 1 17  ? 20.21908  -14.80198 -20.96808 1.000 26.81602 ? 24  ALA   A C   1 
ATOM   72   O O   . ALA   A 1 17  ? 19.97427  -15.37803 -19.90150 1.000 30.53718 ? 24  ALA   A O   1 
ATOM   73   C CB  . ALA   A 1 17  ? 22.35912  -15.31626 -22.17700 1.000 32.25559 ? 24  ALA   A CB  1 
ATOM   74   N N   . GLU   A 1 18  ? 19.92692  -13.51376 -21.16426 1.000 28.52363 ? 25  GLU   A N   1 
ATOM   75   C CA  . GLU   A 1 18  ? 19.34980  -12.71104 -20.08991 1.000 28.81873 ? 25  GLU   A CA  1 
ATOM   76   C C   . GLU   A 1 18  ? 17.93699  -13.16416 -19.74025 1.000 27.53146 ? 25  GLU   A C   1 
ATOM   77   O O   . GLU   A 1 18  ? 17.54376  -13.10646 -18.56787 1.000 26.59119 ? 25  GLU   A O   1 
ATOM   78   C CB  . GLU   A 1 18  ? 19.34829  -11.23123 -20.48032 1.000 32.10549 ? 25  GLU   A CB  1 
ATOM   79   C CG  . GLU   A 1 18  ? 20.73141  -10.63253 -20.71706 1.000 36.12327 ? 25  GLU   A CG  1 
ATOM   80   C CD  . GLU   A 1 18  ? 21.29660  -10.95857 -22.09034 1.000 45.66015 ? 25  GLU   A CD  1 
ATOM   81   O OE1 . GLU   A 1 18  ? 20.63576  -11.69431 -22.85616 1.000 37.28327 ? 25  GLU   A OE1 1 
ATOM   82   O OE2 . GLU   A 1 18  ? 22.40338  -10.47515 -22.40796 1.000 52.04920 ? 25  GLU   A OE2 1 
ATOM   83   N N   . ILE   A 1 19  ? 17.16096  -13.60905 -20.73218 1.000 23.66475 ? 26  ILE   A N   1 
ATOM   84   C CA  . ILE   A 1 19  ? 15.81378  -14.09649 -20.45192 1.000 24.15477 ? 26  ILE   A CA  1 
ATOM   85   C C   . ILE   A 1 19  ? 15.86991  -15.45587 -19.77097 1.000 25.38828 ? 26  ILE   A C   1 
ATOM   86   O O   . ILE   A 1 19  ? 15.14452  -15.70783 -18.80237 1.000 22.59122 ? 26  ILE   A O   1 
ATOM   87   C CB  . ILE   A 1 19  ? 14.97598  -14.14183 -21.74197 1.000 25.46375 ? 26  ILE   A CB  1 
ATOM   88   C CG1 . ILE   A 1 19  ? 14.78215  -12.72757 -22.28759 1.000 27.20307 ? 26  ILE   A CG1 1 
ATOM   89   C CG2 . ILE   A 1 19  ? 13.62746  -14.80832 -21.48796 1.000 24.87130 ? 26  ILE   A CG2 1 
ATOM   90   C CD1 . ILE   A 1 19  ? 14.11715  -11.79968 -21.30450 1.000 29.78944 ? 26  ILE   A CD1 1 
ATOM   91   N N   . ALA   A 1 20  ? 16.73364  -16.35141 -20.26077 1.000 23.13575 ? 27  ALA   A N   1 
ATOM   92   C CA  . ALA   A 1 20  ? 16.92998  -17.63482 -19.59314 1.000 23.41194 ? 27  ALA   A CA  1 
ATOM   93   C C   . ALA   A 1 20  ? 17.33987  -17.43927 -18.13945 1.000 24.64284 ? 27  ALA   A C   1 
ATOM   94   O O   . ALA   A 1 20  ? 16.91841  -18.19826 -17.25845 1.000 23.21379 ? 27  ALA   A O   1 
ATOM   95   C CB  . ALA   A 1 20  ? 17.97718  -18.46118 -20.34036 1.000 23.55443 ? 27  ALA   A CB  1 
ATOM   96   N N   . GLN   A 1 21  ? 18.15886  -16.41944 -17.87054 1.000 24.58400 ? 28  GLN   A N   1 
ATOM   97   C CA  . GLN   A 1 21  ? 18.53653  -16.10666 -16.49648 1.000 23.55087 ? 28  GLN   A CA  1 
ATOM   98   C C   . GLN   A 1 21  ? 17.33429  -15.64638 -15.68089 1.000 28.24921 ? 28  GLN   A C   1 
ATOM   99   O O   . GLN   A 1 21  ? 17.18480  -16.03387 -14.51539 1.000 26.80509 ? 28  GLN   A O   1 
ATOM   100  C CB  . GLN   A 1 21  ? 19.63005  -15.03910 -16.48736 1.000 25.12807 ? 28  GLN   A CB  1 
ATOM   101  C CG  . GLN   A 1 21  ? 20.30323  -14.83496 -15.14198 1.000 42.69261 ? 28  GLN   A CG  1 
ATOM   102  C CD  . GLN   A 1 21  ? 21.10374  -13.55086 -15.09166 1.000 62.89514 ? 28  GLN   A CD  1 
ATOM   103  O OE1 . GLN   A 1 21  ? 21.39256  -12.94613 -16.12482 1.000 59.37311 ? 28  GLN   A OE1 1 
ATOM   104  N NE2 . GLN   A 1 21  ? 21.46559  -13.12524 -13.88776 1.000 69.46915 ? 28  GLN   A NE2 1 
ATOM   105  N N   . LEU   A 1 22  ? 16.47157  -14.81504 -16.27197 1.000 23.92169 ? 29  LEU   A N   1 
ATOM   106  C CA  . LEU   A 1 22  ? 15.27413  -14.36569 -15.56777 1.000 23.39266 ? 29  LEU   A CA  1 
ATOM   107  C C   . LEU   A 1 22  ? 14.36484  -15.54056 -15.23705 1.000 24.22954 ? 29  LEU   A C   1 
ATOM   108  O O   . LEU   A 1 22  ? 13.81959  -15.62989 -14.13153 1.000 21.85414 ? 29  LEU   A O   1 
ATOM   109  C CB  . LEU   A 1 22  ? 14.52473  -13.33119 -16.40718 1.000 22.74048 ? 29  LEU   A CB  1 
ATOM   110  C CG  . LEU   A 1 22  ? 13.14116  -12.95198 -15.87319 1.000 22.11070 ? 29  LEU   A CG  1 
ATOM   111  C CD1 . LEU   A 1 22  ? 13.26599  -12.08251 -14.62883 1.000 27.25048 ? 29  LEU   A CD1 1 
ATOM   112  C CD2 . LEU   A 1 22  ? 12.31350  -12.25753 -16.94785 1.000 24.40056 ? 29  LEU   A CD2 1 
ATOM   113  N N   . MET   A 1 23  ? 14.19209  -16.45692 -16.19017 1.000 21.86599 ? 30  MET   A N   1 
ATOM   114  C CA  . MET   A 1 23  ? 13.31659  -17.60174 -15.96833 1.000 20.82755 ? 30  MET   A CA  1 
ATOM   115  C C   . MET   A 1 23  ? 13.87108  -18.51295 -14.88041 1.000 19.98009 ? 30  MET   A C   1 
ATOM   116  O O   . MET   A 1 23  ? 13.11089  -19.06587 -14.07716 1.000 22.10536 ? 30  MET   A O   1 
ATOM   117  C CB  . MET   A 1 23  ? 13.12921  -18.36458 -17.27953 1.000 21.08764 ? 30  MET   A CB  1 
ATOM   118  C CG  . MET   A 1 23  ? 12.58327  -17.48550 -18.39842 1.000 22.05362 ? 30  MET   A CG  1 
ATOM   119  S SD  . MET   A 1 23  ? 12.18824  -18.34995 -19.92982 1.000 24.14443 ? 30  MET   A SD  1 
ATOM   120  C CE  . MET   A 1 23  ? 11.29356  -19.76865 -19.30938 1.000 26.21865 ? 30  MET   A CE  1 
ATOM   121  N N   . SER   A 1 24  ? 15.19755  -18.67112 -14.82976 1.000 20.87905 ? 31  SER   A N   1 
ATOM   122  C CA  . SER   A 1 24  ? 15.80511  -19.48505 -13.78010 1.000 21.43212 ? 31  SER   A CA  1 
ATOM   123  C C   . SER   A 1 24  ? 15.59542  -18.86371 -12.40387 1.000 25.29548 ? 31  SER   A C   1 
ATOM   124  O O   . SER   A 1 24  ? 15.34789  -19.57833 -11.42329 1.000 26.70055 ? 31  SER   A O   1 
ATOM   125  C CB  . SER   A 1 24  ? 17.29608  -19.67585 -14.05665 1.000 30.14112 ? 31  SER   A CB  1 
ATOM   126  O OG  . SER   A 1 24  ? 17.50646  -20.18111 -15.36285 1.000 43.44208 ? 31  SER   A OG  1 
ATOM   127  N N   . LEU   A 1 25  ? 15.70321  -17.53413 -12.30577 1.000 22.30845 ? 32  LEU   A N   1 
ATOM   128  C CA  . LEU   A 1 25  ? 15.45601  -16.87585 -11.02494 1.000 22.34238 ? 32  LEU   A CA  1 
ATOM   129  C C   . LEU   A 1 25  ? 14.00122  -17.02955 -10.59631 1.000 27.81459 ? 32  LEU   A C   1 
ATOM   130  O O   . LEU   A 1 25  ? 13.71664  -17.23808 -9.41126  1.000 25.71780 ? 32  LEU   A O   1 
ATOM   131  C CB  . LEU   A 1 25  ? 15.83655  -15.39793 -11.10213 1.000 29.57588 ? 32  LEU   A CB  1 
ATOM   132  C CG  . LEU   A 1 25  ? 17.33015  -15.07311 -10.99909 1.000 47.16928 ? 32  LEU   A CG  1 
ATOM   133  C CD1 . LEU   A 1 25  ? 17.56071  -13.57046 -11.01341 1.000 48.83822 ? 32  LEU   A CD1 1 
ATOM   134  C CD2 . LEU   A 1 25  ? 17.94501  -15.70303 -9.75779  1.000 52.71045 ? 32  LEU   A CD2 1 
ATOM   135  N N   . ILE   A 1 26  ? 13.06809  -16.93497 -11.54686 1.000 24.95670 ? 33  ILE   A N   1 
ATOM   136  C CA  . ILE   A 1 26  ? 11.65260  -17.11112 -11.22945 1.000 21.55891 ? 33  ILE   A CA  1 
ATOM   137  C C   . ILE   A 1 26  ? 11.39032  -18.52766 -10.73149 1.000 25.79891 ? 33  ILE   A C   1 
ATOM   138  O O   . ILE   A 1 26  ? 10.61470  -18.74217 -9.79074  1.000 23.83277 ? 33  ILE   A O   1 
ATOM   139  C CB  . ILE   A 1 26  ? 10.79199  -16.77067 -12.46200 1.000 19.85357 ? 33  ILE   A CB  1 
ATOM   140  C CG1 . ILE   A 1 26  ? 10.78218  -15.25865 -12.70492 1.000 23.85750 ? 33  ILE   A CG1 1 
ATOM   141  C CG2 . ILE   A 1 26  ? 9.36862   -17.30086 -12.30152 1.000 17.17979 ? 33  ILE   A CG2 1 
ATOM   142  C CD1 . ILE   A 1 26  ? 10.22071  -14.86026 -14.05108 1.000 25.43625 ? 33  ILE   A CD1 1 
ATOM   143  N N   . ILE   A 1 27  ? 12.05161  -19.51319 -11.33591 1.000 22.84920 ? 34  ILE   A N   1 
ATOM   144  C CA  . ILE   A 1 27  ? 11.78746  -20.90741 -10.99734 1.000 26.61279 ? 34  ILE   A CA  1 
ATOM   145  C C   . ILE   A 1 27  ? 12.48741  -21.30516 -9.70066  1.000 27.30365 ? 34  ILE   A C   1 
ATOM   146  O O   . ILE   A 1 27  ? 11.94210  -22.07636 -8.90330  1.000 28.24263 ? 34  ILE   A O   1 
ATOM   147  C CB  . ILE   A 1 27  ? 12.20299  -21.80869 -12.17540 1.000 26.66582 ? 34  ILE   A CB  1 
ATOM   148  C CG1 . ILE   A 1 27  ? 11.24375  -21.61372 -13.35501 1.000 25.69085 ? 34  ILE   A CG1 1 
ATOM   149  C CG2 . ILE   A 1 27  ? 12.25772  -23.27648 -11.75770 1.000 34.18341 ? 34  ILE   A CG2 1 
ATOM   150  C CD1 . ILE   A 1 27  ? 11.76317  -22.17323 -14.65285 1.000 25.53891 ? 34  ILE   A CD1 1 
ATOM   151  N N   . ASN   A 1 28  ? 13.68676  -20.77449 -9.45018  1.000 26.54770 ? 35  ASN   A N   1 
ATOM   152  C CA  . ASN   A 1 28  ? 14.53108  -21.27698 -8.37271  1.000 28.23708 ? 35  ASN   A CA  1 
ATOM   153  C C   . ASN   A 1 28  ? 14.44552  -20.47379 -7.08035  1.000 29.56849 ? 35  ASN   A C   1 
ATOM   154  O O   . ASN   A 1 28  ? 14.74495  -21.02322 -6.01466  1.000 34.02897 ? 35  ASN   A O   1 
ATOM   155  C CB  . ASN   A 1 28  ? 15.99522  -21.32281 -8.82759  1.000 32.53961 ? 35  ASN   A CB  1 
ATOM   156  C CG  . ASN   A 1 28  ? 16.22118  -22.30266 -9.96205  1.000 45.10871 ? 35  ASN   A CG  1 
ATOM   157  O OD1 . ASN   A 1 28  ? 15.51145  -23.30090 -10.08750 1.000 41.21689 ? 35  ASN   A OD1 1 
ATOM   158  N ND2 . ASN   A 1 28  ? 17.21630  -22.02204 -10.79603 1.000 52.08513 ? 35  ASN   A ND2 1 
ATOM   159  N N   . THR   A 1 29  ? 14.05880  -19.20183 -7.13836  1.000 24.47394 ? 36  THR   A N   1 
ATOM   160  C CA  . THR   A 1 29  ? 14.04810  -18.36203 -5.94689  1.000 26.83399 ? 36  THR   A CA  1 
ATOM   161  C C   . THR   A 1 29  ? 12.86937  -18.72313 -5.05248  1.000 31.21956 ? 36  THR   A C   1 
ATOM   162  O O   . THR   A 1 29  ? 11.75452  -18.94706 -5.53267  1.000 29.77072 ? 36  THR   A O   1 
ATOM   163  C CB  . THR   A 1 29  ? 13.96977  -16.88372 -6.33431  1.000 31.65874 ? 36  THR   A CB  1 
ATOM   164  O OG1 . THR   A 1 29  ? 15.08695  -16.55064 -7.16434  1.000 31.84933 ? 36  THR   A OG1 1 
ATOM   165  C CG2 . THR   A 1 29  ? 13.99682  -15.99332 -5.09719  1.000 30.69720 ? 36  THR   A CG2 1 
ATOM   166  N N   . PHE   A 1 30  ? 13.11586  -18.78442 -3.74460  1.000 27.90734 ? 37  PHE   A N   1 
ATOM   167  C CA  . PHE   A 1 30  ? 12.01943  -19.01071 -2.81324  1.000 28.20958 ? 37  PHE   A CA  1 
ATOM   168  C C   . PHE   A 1 30  ? 11.16469  -17.75396 -2.73211  1.000 27.28446 ? 37  PHE   A C   1 
ATOM   169  O O   . PHE   A 1 30  ? 11.65979  -16.67649 -2.38418  1.000 27.48202 ? 37  PHE   A O   1 
ATOM   170  C CB  . PHE   A 1 30  ? 12.52950  -19.39301 -1.42856  1.000 25.73613 ? 37  PHE   A CB  1 
ATOM   171  C CG  . PHE   A 1 30  ? 11.42402  -19.65865 -0.44444  1.000 30.16250 ? 37  PHE   A CG  1 
ATOM   172  C CD1 . PHE   A 1 30  ? 10.66056  -20.81073 -0.54268  1.000 32.61318 ? 37  PHE   A CD1 1 
ATOM   173  C CD2 . PHE   A 1 30  ? 11.13338  -18.75328 0.56349   1.000 26.80006 ? 37  PHE   A CD2 1 
ATOM   174  C CE1 . PHE   A 1 30  ? 9.63510   -21.06268 0.34861   1.000 33.74218 ? 37  PHE   A CE1 1 
ATOM   175  C CE2 . PHE   A 1 30  ? 10.10585  -19.00074 1.46382   1.000 30.59998 ? 37  PHE   A CE2 1 
ATOM   176  C CZ  . PHE   A 1 30  ? 9.35810   -20.15783 1.35350   1.000 28.09064 ? 37  PHE   A CZ  1 
ATOM   177  N N   . TYR   A 1 31  ? 9.87778   -17.89462 -3.05010  1.000 23.39676 ? 38  TYR   A N   1 
ATOM   178  C CA  . TYR   A 1 31  ? 8.98545   -16.74259 -3.11321  1.000 23.55043 ? 38  TYR   A CA  1 
ATOM   179  C C   . TYR   A 1 31  ? 7.55799   -17.29057 -3.03258  1.000 23.21584 ? 38  TYR   A C   1 
ATOM   180  O O   . TYR   A 1 31  ? 7.05516   -17.84889 -4.00846  1.000 24.56780 ? 38  TYR   A O   1 
ATOM   181  C CB  . TYR   A 1 31  ? 9.21160   -15.94911 -4.38811  1.000 23.76989 ? 38  TYR   A CB  1 
ATOM   182  C CG  . TYR   A 1 31  ? 8.35805   -14.71353 -4.48789  1.000 27.98847 ? 38  TYR   A CG  1 
ATOM   183  C CD1 . TYR   A 1 31  ? 8.63646   -13.59384 -3.71580  1.000 28.71128 ? 38  TYR   A CD1 1 
ATOM   184  C CD2 . TYR   A 1 31  ? 7.25512   -14.67345 -5.32841  1.000 26.04637 ? 38  TYR   A CD2 1 
ATOM   185  C CE1 . TYR   A 1 31  ? 7.85380   -12.46052 -3.79433  1.000 33.73427 ? 38  TYR   A CE1 1 
ATOM   186  C CE2 . TYR   A 1 31  ? 6.46464   -13.54517 -5.41013  1.000 28.91284 ? 38  TYR   A CE2 1 
ATOM   187  C CZ  . TYR   A 1 31  ? 6.76846   -12.44298 -4.64201  1.000 30.55001 ? 38  TYR   A CZ  1 
ATOM   188  O OH  . TYR   A 1 31  ? 5.98283   -11.31708 -4.72184  1.000 37.54578 ? 38  TYR   A OH  1 
ATOM   189  N N   . SER   A 1 32  ? 6.93051   -17.12437 -1.87027  1.000 22.08043 ? 39  SER   A N   1 
ATOM   190  C CA  . SER   A 1 32  ? 5.64330   -17.75977 -1.61459  1.000 24.56724 ? 39  SER   A CA  1 
ATOM   191  C C   . SER   A 1 32  ? 4.48282   -17.08323 -2.33209  1.000 25.61738 ? 39  SER   A C   1 
ATOM   192  O O   . SER   A 1 32  ? 3.46526   -17.73847 -2.58193  1.000 29.58893 ? 39  SER   A O   1 
ATOM   193  C CB  . SER   A 1 32  ? 5.36721   -17.78278 -0.11093  1.000 28.15655 ? 39  SER   A CB  1 
ATOM   194  O OG  . SER   A 1 32  ? 6.41012   -18.45111 0.57453   1.000 25.12021 ? 39  SER   A OG  1 
ATOM   195  N N   . ASN   A 1 33  ? 4.61055   -15.80013 -2.67192  1.000 22.94461 ? 40  ASN   A N   1 
ATOM   196  C CA  . ASN   A 1 33  ? 3.50438   -15.01740 -3.22413  1.000 26.06686 ? 40  ASN   A CA  1 
ATOM   197  C C   . ASN   A 1 33  ? 3.34261   -15.28939 -4.72505  1.000 23.78661 ? 40  ASN   A C   1 
ATOM   198  O O   . ASN   A 1 33  ? 3.44282   -14.40233 -5.57141  1.000 23.58950 ? 40  ASN   A O   1 
ATOM   199  C CB  . ASN   A 1 33  ? 3.73747   -13.53868 -2.93256  1.000 24.03528 ? 40  ASN   A CB  1 
ATOM   200  C CG  . ASN   A 1 33  ? 2.60580   -12.65395 -3.41960  1.000 28.27824 ? 40  ASN   A CG  1 
ATOM   201  O OD1 . ASN   A 1 33  ? 1.43097   -12.99785 -3.28830  1.000 26.51304 ? 40  ASN   A OD1 1 
ATOM   202  N ND2 . ASN   A 1 33  ? 2.95644   -11.49784 -3.97265  1.000 31.72284 ? 40  ASN   A ND2 1 
ATOM   203  N N   . LYS   A 1 34  ? 3.06844   -16.55797 -5.04712  1.000 19.45532 ? 41  LYS   A N   1 
ATOM   204  C CA  . LYS   A 1 34  ? 3.01724   -16.98370 -6.44330  1.000 20.25522 ? 41  LYS   A CA  1 
ATOM   205  C C   . LYS   A 1 34  ? 1.77049   -16.50142 -7.17243  1.000 22.42360 ? 41  LYS   A C   1 
ATOM   206  O O   . LYS   A 1 34  ? 1.77529   -16.45959 -8.40683  1.000 24.44178 ? 41  LYS   A O   1 
ATOM   207  C CB  . LYS   A 1 34  ? 3.08918   -18.50847 -6.53995  1.000 21.02248 ? 41  LYS   A CB  1 
ATOM   208  C CG  . LYS   A 1 34  ? 4.44741   -19.10580 -6.19827  1.000 20.93165 ? 41  LYS   A CG  1 
ATOM   209  C CD  . LYS   A 1 34  ? 4.37730   -20.62451 -6.15936  1.000 21.17859 ? 41  LYS   A CD  1 
ATOM   210  C CE  . LYS   A 1 34  ? 5.72996   -21.23558 -5.81674  1.000 25.12517 ? 41  LYS   A CE  1 
ATOM   211  N NZ  . LYS   A 1 34  ? 6.65191   -21.21280 -6.98565  1.000 23.78047 ? 41  LYS   A NZ  1 
ATOM   212  N N   . GLU   A 1 35  ? 0.71160   -16.13286 -6.44737  1.000 21.35157 ? 42  GLU   A N   1 
ATOM   213  C CA  . GLU   A 1 35  ? -0.56075  -15.81505 -7.08805  1.000 19.06399 ? 42  GLU   A CA  1 
ATOM   214  C C   . GLU   A 1 35  ? -0.47044  -14.62161 -8.03177  1.000 23.36225 ? 42  GLU   A C   1 
ATOM   215  O O   . GLU   A 1 35  ? -1.39635  -14.40570 -8.82258  1.000 22.63851 ? 42  GLU   A O   1 
ATOM   216  C CB  . GLU   A 1 35  ? -1.62585  -15.54016 -6.02928  1.000 20.57228 ? 42  GLU   A CB  1 
ATOM   217  C CG  . GLU   A 1 35  ? -1.37491  -14.27551 -5.22181  1.000 22.74173 ? 42  GLU   A CG  1 
ATOM   218  C CD  . GLU   A 1 35  ? -2.35355  -14.11063 -4.07503  1.000 33.52920 ? 42  GLU   A CD  1 
ATOM   219  O OE1 . GLU   A 1 35  ? -2.56635  -15.09024 -3.33357  1.000 31.66853 ? 42  GLU   A OE1 1 
ATOM   220  O OE2 . GLU   A 1 35  ? -2.90565  -13.00082 -3.91293  1.000 46.02335 ? 42  GLU   A OE2 1 
ATOM   221  N N   . ILE   A 1 36  ? 0.61581   -13.84429 -7.97360  1.000 20.62843 ? 43  ILE   A N   1 
ATOM   222  C CA  . ILE   A 1 36  ? 0.73221   -12.65753 -8.81577  1.000 22.67551 ? 43  ILE   A CA  1 
ATOM   223  C C   . ILE   A 1 36  ? 0.80617   -12.99710 -10.29710 1.000 21.38088 ? 43  ILE   A C   1 
ATOM   224  O O   . ILE   A 1 36  ? 0.62268   -12.10967 -11.13772 1.000 20.98347 ? 43  ILE   A O   1 
ATOM   225  C CB  . ILE   A 1 36  ? 1.95085   -11.81479 -8.38455  1.000 25.40266 ? 43  ILE   A CB  1 
ATOM   226  C CG1 . ILE   A 1 36  ? 3.24080   -12.63696 -8.47954  1.000 31.53683 ? 43  ILE   A CG1 1 
ATOM   227  C CG2 . ILE   A 1 36  ? 1.74648   -11.25669 -6.99296  1.000 27.63228 ? 43  ILE   A CG2 1 
ATOM   228  C CD1 . ILE   A 1 36  ? 4.10353   -12.28760 -9.67154  1.000 43.13313 ? 43  ILE   A CD1 1 
ATOM   229  N N   . PHE   A 1 37  ? 1.07303   -14.26120 -10.64280 1.000 20.82774 ? 44  PHE   A N   1 
ATOM   230  C CA  . PHE   A 1 37  ? 1.12224   -14.64994 -12.04961 1.000 21.36678 ? 44  PHE   A CA  1 
ATOM   231  C C   . PHE   A 1 37  ? -0.19007  -14.32823 -12.75289 1.000 21.86417 ? 44  PHE   A C   1 
ATOM   232  O O   . PHE   A 1 37  ? -0.19573  -13.90243 -13.91428 1.000 18.93198 ? 44  PHE   A O   1 
ATOM   233  C CB  . PHE   A 1 37  ? 1.43442   -16.14588 -12.18334 1.000 19.79973 ? 44  PHE   A CB  1 
ATOM   234  C CG  . PHE   A 1 37  ? 0.22457   -17.03330 -12.01870 1.000 24.46740 ? 44  PHE   A CG  1 
ATOM   235  C CD1 . PHE   A 1 37  ? -0.19279  -17.43765 -10.76125 1.000 22.69270 ? 44  PHE   A CD1 1 
ATOM   236  C CD2 . PHE   A 1 37  ? -0.51917  -17.43270 -13.12151 1.000 20.16974 ? 44  PHE   A CD2 1 
ATOM   237  C CE1 . PHE   A 1 37  ? -1.31782  -18.23791 -10.60767 1.000 23.68693 ? 44  PHE   A CE1 1 
ATOM   238  C CE2 . PHE   A 1 37  ? -1.64957  -18.22496 -12.96853 1.000 17.20450 ? 44  PHE   A CE2 1 
ATOM   239  C CZ  . PHE   A 1 37  ? -2.04393  -18.63195 -11.71351 1.000 23.10366 ? 44  PHE   A CZ  1 
ATOM   240  N N   . LEU   A 1 38  ? -1.31647  -14.53479 -12.06339 1.000 20.54261 ? 45  LEU   A N   1 
ATOM   241  C CA  . LEU   A 1 38  ? -2.61403  -14.34976 -12.70099 1.000 22.03329 ? 45  LEU   A CA  1 
ATOM   242  C C   . LEU   A 1 38  ? -2.89103  -12.87607 -12.95740 1.000 22.41296 ? 45  LEU   A C   1 
ATOM   243  O O   . LEU   A 1 38  ? -3.44548  -12.51646 -14.00242 1.000 20.67584 ? 45  LEU   A O   1 
ATOM   244  C CB  . LEU   A 1 38  ? -3.71541  -14.96812 -11.84075 1.000 21.44021 ? 45  LEU   A CB  1 
ATOM   245  C CG  . LEU   A 1 38  ? -5.10798  -14.98709 -12.47363 1.000 20.59189 ? 45  LEU   A CG  1 
ATOM   246  C CD1 . LEU   A 1 38  ? -5.07665  -15.76988 -13.77952 1.000 21.53949 ? 45  LEU   A CD1 1 
ATOM   247  C CD2 . LEU   A 1 38  ? -6.13176  -15.57043 -11.51150 1.000 23.98771 ? 45  LEU   A CD2 1 
ATOM   248  N N   . ARG   A 1 39  ? -2.51843  -12.01030 -12.01172 1.000 19.04378 ? 46  ARG   A N   1 
ATOM   249  C CA  . ARG   A 1 39  ? -2.64861  -10.57438 -12.23242 1.000 18.67977 ? 46  ARG   A CA  1 
ATOM   250  C C   . ARG   A 1 39  ? -1.84877  -10.13359 -13.45251 1.000 22.37099 ? 46  ARG   A C   1 
ATOM   251  O O   . ARG   A 1 39  ? -2.30542  -9.29211  -14.23436 1.000 24.21656 ? 46  ARG   A O   1 
ATOM   252  C CB  . ARG   A 1 39  ? -2.19130  -9.81049  -10.98865 1.000 22.30365 ? 46  ARG   A CB  1 
ATOM   253  C CG  . ARG   A 1 39  ? -2.12800  -8.30442  -11.16913 1.000 31.89410 ? 46  ARG   A CG  1 
ATOM   254  C CD  . ARG   A 1 39  ? -1.37729  -7.64038  -10.02173 1.000 33.51276 ? 46  ARG   A CD  1 
ATOM   255  N NE  . ARG   A 1 39  ? 0.04823   -7.95218  -10.04446 1.000 36.66624 ? 46  ARG   A NE  1 
ATOM   256  C CZ  . ARG   A 1 39  ? 0.83332   -7.95709  -8.97490  1.000 45.86500 ? 46  ARG   A CZ  1 
ATOM   257  N NH1 . ARG   A 1 39  ? 0.36467   -7.67092  -7.77147  1.000 37.22104 ? 46  ARG   A NH1 1 
ATOM   258  N NH2 . ARG   A 1 39  ? 2.12276   -8.25203  -9.11661  1.000 37.60781 ? 46  ARG   A NH2 1 
ATOM   259  N N   . GLU   A 1 40  ? -0.65574  -10.70137 -13.63872 1.000 16.16475 ? 47  GLU   A N   1 
ATOM   260  C CA  . GLU   A 1 40  ? 0.20126   -10.27811 -14.74122 1.000 20.44255 ? 47  GLU   A CA  1 
ATOM   261  C C   . GLU   A 1 40  ? -0.35299  -10.72755 -16.08615 1.000 20.46391 ? 47  GLU   A C   1 
ATOM   262  O O   . GLU   A 1 40  ? -0.31644  -9.96809  -17.06145 1.000 21.40105 ? 47  GLU   A O   1 
ATOM   263  C CB  . GLU   A 1 40  ? 1.61809   -10.81345 -14.53814 1.000 23.44129 ? 47  GLU   A CB  1 
ATOM   264  C CG  . GLU   A 1 40  ? 2.28081   -10.32878 -13.25940 1.000 21.05450 ? 47  GLU   A CG  1 
ATOM   265  C CD  . GLU   A 1 40  ? 2.27829   -8.81534  -13.13876 1.000 35.07729 ? 47  GLU   A CD  1 
ATOM   266  O OE1 . GLU   A 1 40  ? 2.42305   -8.12951  -14.17205 1.000 29.38284 ? 47  GLU   A OE1 1 
ATOM   267  O OE2 . GLU   A 1 40  ? 2.13085   -8.30390  -12.00803 1.000 33.71543 ? 47  GLU   A OE2 1 
ATOM   268  N N   . LEU   A 1 41  ? -0.85981  -11.96046 -16.16265 1.000 17.87735 ? 48  LEU   A N   1 
ATOM   269  C CA  . LEU   A 1 41  ? -1.39571  -12.45411 -17.42760 1.000 19.45579 ? 48  LEU   A CA  1 
ATOM   270  C C   . LEU   A 1 41  ? -2.69991  -11.75220 -17.78521 1.000 20.80437 ? 48  LEU   A C   1 
ATOM   271  O O   . LEU   A 1 41  ? -2.94741  -11.45211 -18.96034 1.000 21.55670 ? 48  LEU   A O   1 
ATOM   272  C CB  . LEU   A 1 41  ? -1.59325  -13.96990 -17.36261 1.000 20.42545 ? 48  LEU   A CB  1 
ATOM   273  C CG  . LEU   A 1 41  ? -0.30741  -14.78782 -17.19480 1.000 19.40625 ? 48  LEU   A CG  1 
ATOM   274  C CD1 . LEU   A 1 41  ? -0.62313  -16.27256 -17.04356 1.000 19.83962 ? 48  LEU   A CD1 1 
ATOM   275  C CD2 . LEU   A 1 41  ? 0.63964   -14.54449 -18.36293 1.000 21.11423 ? 48  LEU   A CD2 1 
ATOM   276  N N   . ILE   A 1 42  ? -3.54645  -11.48578 -16.78685 1.000 19.43296 ? 49  ILE   A N   1 
ATOM   277  C CA  . ILE   A 1 42  ? -4.77583  -10.73944 -17.03565 1.000 18.45532 ? 49  ILE   A CA  1 
ATOM   278  C C   . ILE   A 1 42  ? -4.45211  -9.31453  -17.46804 1.000 19.00653 ? 49  ILE   A C   1 
ATOM   279  O O   . ILE   A 1 42  ? -5.08946  -8.76397  -18.37368 1.000 19.47871 ? 49  ILE   A O   1 
ATOM   280  C CB  . ILE   A 1 42  ? -5.67588  -10.77127 -15.78625 1.000 19.77296 ? 49  ILE   A CB  1 
ATOM   281  C CG1 . ILE   A 1 42  ? -6.29906  -12.16041 -15.60650 1.000 19.77254 ? 49  ILE   A CG1 1 
ATOM   282  C CG2 . ILE   A 1 42  ? -6.75304  -9.69439  -15.86228 1.000 22.90365 ? 49  ILE   A CG2 1 
ATOM   283  C CD1 . ILE   A 1 42  ? -7.04024  -12.33290 -14.29698 1.000 23.77502 ? 49  ILE   A CD1 1 
ATOM   284  N N   . SER   A 1 43  ? -3.44941  -8.69823  -16.83623 1.000 19.44133 ? 50  SER   A N   1 
ATOM   285  C CA  . SER   A 1 43  ? -3.02357  -7.36391  -17.24994 1.000 24.31901 ? 50  SER   A CA  1 
ATOM   286  C C   . SER   A 1 43  ? -2.49974  -7.37410  -18.68108 1.000 21.87560 ? 50  SER   A C   1 
ATOM   287  O O   . SER   A 1 43  ? -2.78144  -6.45440  -19.45913 1.000 21.00912 ? 50  SER   A O   1 
ATOM   288  C CB  . SER   A 1 43  ? -1.95847  -6.82697  -16.29057 1.000 24.85463 ? 50  SER   A CB  1 
ATOM   289  O OG  . SER   A 1 43  ? -1.34031  -5.66207  -16.81095 1.000 32.63338 ? 50  SER   A OG  1 
ATOM   290  N N   . ASN   A 1 44  ? -1.73159  -8.40642  -19.04485 1.000 17.51260 ? 51  ASN   A N   1 
ATOM   291  C CA  . ASN   A 1 44  ? -1.29054  -8.55197  -20.42866 1.000 19.89184 ? 51  ASN   A CA  1 
ATOM   292  C C   . ASN   A 1 44  ? -2.47725  -8.68486  -21.37300 1.000 22.15085 ? 51  ASN   A C   1 
ATOM   293  O O   . ASN   A 1 44  ? -2.48951  -8.08713  -22.45503 1.000 20.69864 ? 51  ASN   A O   1 
ATOM   294  C CB  . ASN   A 1 44  ? -0.37176  -9.76506  -20.56579 1.000 19.85703 ? 51  ASN   A CB  1 
ATOM   295  C CG  . ASN   A 1 44  ? 1.05042   -9.47393  -20.12973 1.000 26.14178 ? 51  ASN   A CG  1 
ATOM   296  O OD1 . ASN   A 1 44  ? 1.35944   -8.37723  -19.65611 1.000 23.05916 ? 51  ASN   A OD1 1 
ATOM   297  N ND2 . ASN   A 1 44  ? 1.92869   -10.45785 -20.29206 1.000 25.91299 ? 51  ASN   A ND2 1 
ATOM   298  N N   . SER   A 1 45  ? -3.48233  -9.47198  -20.98178 1.000 19.29468 ? 52  SER   A N   1 
ATOM   299  C CA  . SER   A 1 45  ? -4.66952  -9.63451  -21.81476 1.000 19.00288 ? 52  SER   A CA  1 
ATOM   300  C C   . SER   A 1 45  ? -5.41291  -8.31533  -21.97721 1.000 20.94483 ? 52  SER   A C   1 
ATOM   301  O O   . SER   A 1 45  ? -5.84078  -7.96776  -23.08417 1.000 20.62739 ? 52  SER   A O   1 
ATOM   302  C CB  . SER   A 1 45  ? -5.58821  -10.69859 -21.21317 1.000 18.60240 ? 52  SER   A CB  1 
ATOM   303  O OG  . SER   A 1 45  ? -5.01692  -11.99051 -21.32707 1.000 21.48868 ? 52  SER   A OG  1 
ATOM   304  N N   . SER   A 1 46  ? -5.56880  -7.56327  -20.88457 1.000 18.44738 ? 53  SER   A N   1 
ATOM   305  C CA  . SER   A 1 46  ? -6.23586  -6.26823  -20.96396 1.000 19.80529 ? 53  SER   A CA  1 
ATOM   306  C C   . SER   A 1 46  ? -5.48867  -5.31713  -21.89050 1.000 23.32872 ? 53  SER   A C   1 
ATOM   307  O O   . SER   A 1 46  ? -6.10950  -4.57503  -22.66313 1.000 24.14152 ? 53  SER   A O   1 
ATOM   308  C CB  . SER   A 1 46  ? -6.36763  -5.66439  -19.56666 1.000 22.10771 ? 53  SER   A CB  1 
ATOM   309  O OG  . SER   A 1 46  ? -6.96190  -4.38054  -19.62667 1.000 25.16418 ? 53  SER   A OG  1 
ATOM   310  N N   . ASP   A 1 47  ? -4.15285  -5.32628  -21.82823 1.000 22.10468 ? 54  ASP   A N   1 
ATOM   311  C CA  . ASP   A 1 47  ? -3.36605  -4.47754  -22.71708 1.000 20.44475 ? 54  ASP   A CA  1 
ATOM   312  C C   . ASP   A 1 47  ? -3.58692  -4.85404  -24.17754 1.000 18.79137 ? 54  ASP   A C   1 
ATOM   313  O O   . ASP   A 1 47  ? -3.72943  -3.97621  -25.03563 1.000 19.94329 ? 54  ASP   A O   1 
ATOM   314  C CB  . ASP   A 1 47  ? -1.88118  -4.57871  -22.37309 1.000 21.04505 ? 54  ASP   A CB  1 
ATOM   315  C CG  . ASP   A 1 47  ? -1.52886  -3.86907  -21.08953 1.000 29.69300 ? 54  ASP   A CG  1 
ATOM   316  O OD1 . ASP   A 1 47  ? -2.25548  -2.93261  -20.70104 1.000 31.39361 ? 54  ASP   A OD1 1 
ATOM   317  O OD2 . ASP   A 1 47  ? -0.50728  -4.23505  -20.47655 1.000 28.24959 ? 54  ASP   A OD2 1 
ATOM   318  N N   . ALA   A 1 48  ? -3.61542  -6.15444  -24.47960 1.000 19.54733 ? 55  ALA   A N   1 
ATOM   319  C CA  . ALA   A 1 48  ? -3.82990  -6.59168  -25.85579 1.000 17.70652 ? 55  ALA   A CA  1 
ATOM   320  C C   . ALA   A 1 48  ? -5.23177  -6.23977  -26.33556 1.000 19.33220 ? 55  ALA   A C   1 
ATOM   321  O O   . ALA   A 1 48  ? -5.43744  -5.96353  -27.52129 1.000 20.75954 ? 55  ALA   A O   1 
ATOM   322  C CB  . ALA   A 1 48  ? -3.58532  -8.09645  -25.97291 1.000 15.55756 ? 55  ALA   A CB  1 
ATOM   323  N N   . LEU   A 1 49  ? -6.21213  -6.25767  -25.43066 1.000 18.18145 ? 56  LEU   A N   1 
ATOM   324  C CA  . LEU   A 1 49  ? -7.56700  -5.85707  -25.79560 1.000 20.11456 ? 56  LEU   A CA  1 
ATOM   325  C C   . LEU   A 1 49  ? -7.65144  -4.35693  -26.04091 1.000 23.23438 ? 56  LEU   A C   1 
ATOM   326  O O   . LEU   A 1 49  ? -8.34793  -3.91459  -26.96425 1.000 20.53544 ? 56  LEU   A O   1 
ATOM   327  C CB  . LEU   A 1 49  ? -8.54853  -6.28992  -24.70690 1.000 21.73743 ? 56  LEU   A CB  1 
ATOM   328  C CG  . LEU   A 1 49  ? -8.78826  -7.79903  -24.63814 1.000 15.82077 ? 56  LEU   A CG  1 
ATOM   329  C CD1 . LEU   A 1 49  ? -9.32779  -8.20309  -23.27659 1.000 22.24152 ? 56  LEU   A CD1 1 
ATOM   330  C CD2 . LEU   A 1 49  ? -9.74774  -8.22503  -25.74339 1.000 18.75563 ? 56  LEU   A CD2 1 
ATOM   331  N N   . ASP   A 1 50  ? -6.95379  -3.55936  -25.22309 1.000 19.26293 ? 57  ASP   A N   1 
ATOM   332  C CA  . ASP   A 1 50  ? -6.86290  -2.12753  -25.48700 1.000 20.91686 ? 57  ASP   A CA  1 
ATOM   333  C C   . ASP   A 1 50  ? -6.31180  -1.85369  -26.87987 1.000 20.32356 ? 57  ASP   A C   1 
ATOM   334  O O   . ASP   A 1 50  ? -6.78305  -0.94920  -27.57638 1.000 20.45240 ? 57  ASP   A O   1 
ATOM   335  C CB  . ASP   A 1 50  ? -5.98313  -1.44466  -24.44074 1.000 20.39527 ? 57  ASP   A CB  1 
ATOM   336  C CG  . ASP   A 1 50  ? -6.62643  -1.38987  -23.06802 1.000 28.33025 ? 57  ASP   A CG  1 
ATOM   337  O OD1 . ASP   A 1 50  ? -7.83609  -1.67345  -22.95178 1.000 23.99002 ? 57  ASP   A OD1 1 
ATOM   338  O OD2 . ASP   A 1 50  ? -5.91324  -1.04787  -22.10304 1.000 27.11916 ? 57  ASP   A OD2 1 
ATOM   339  N N   . LYS   A 1 51  ? -5.31638  -2.63521  -27.30761 1.000 21.50495 ? 58  LYS   A N   1 
ATOM   340  C CA  . LYS   A 1 51  ? -4.64058  -2.35095  -28.57066 1.000 23.29280 ? 58  LYS   A CA  1 
ATOM   341  C C   . LYS   A 1 51  ? -5.55245  -2.58826  -29.76940 1.000 23.05506 ? 58  LYS   A C   1 
ATOM   342  O O   . LYS   A 1 51  ? -5.59196  -1.76516  -30.69148 1.000 21.35138 ? 58  LYS   A O   1 
ATOM   343  C CB  . LYS   A 1 51  ? -3.36847  -3.19108  -28.68874 1.000 25.26026 ? 58  LYS   A CB  1 
ATOM   344  C CG  . LYS   A 1 51  ? -2.22830  -2.71577  -27.79985 1.000 29.72100 ? 58  LYS   A CG  1 
ATOM   345  C CD  . LYS   A 1 51  ? -0.99656  -3.59010  -27.98154 1.000 33.97247 ? 58  LYS   A CD  1 
ATOM   346  C CE  . LYS   A 1 51  ? 0.01263   -3.36572  -26.86995 1.000 35.11391 ? 58  LYS   A CE  1 
ATOM   347  N NZ  . LYS   A 1 51  ? 0.98602   -4.49276  -26.78861 1.000 37.17180 ? 58  LYS   A NZ  1 
ATOM   348  N N   . ILE   A 1 52  ? -6.28206  -3.70761  -29.78821 1.000 21.07899 ? 59  ILE   A N   1 
ATOM   349  C CA  . ILE   A 1 52  ? -7.16827  -3.96423  -30.91971 1.000 22.60412 ? 59  ILE   A CA  1 
ATOM   350  C C   . ILE   A 1 52  ? -8.36539  -3.02517  -30.89243 1.000 22.59140 ? 59  ILE   A C   1 
ATOM   351  O O   . ILE   A 1 52  ? -8.88004  -2.63655  -31.94820 1.000 21.33673 ? 59  ILE   A O   1 
ATOM   352  C CB  . ILE   A 1 52  ? -7.59985  -5.44346  -30.95880 1.000 23.77960 ? 59  ILE   A CB  1 
ATOM   353  C CG1 . ILE   A 1 52  ? -8.29455  -5.74893  -32.29006 1.000 26.70495 ? 59  ILE   A CG1 1 
ATOM   354  C CG2 . ILE   A 1 52  ? -8.49923  -5.78908  -29.77749 1.000 21.83592 ? 59  ILE   A CG2 1 
ATOM   355  C CD1 . ILE   A 1 52  ? -7.43505  -5.47039  -33.50014 1.000 26.74100 ? 59  ILE   A CD1 1 
ATOM   356  N N   . ARG   A 1 53  ? -8.82103  -2.63223  -29.70081 1.000 22.79507 ? 60  ARG   A N   1 
ATOM   357  C CA  . ARG   A 1 53  ? -9.91609  -1.67287  -29.61316 1.000 23.06995 ? 60  ARG   A CA  1 
ATOM   358  C C   . ARG   A 1 53  ? -9.51145  -0.33211  -30.20564 1.000 24.22289 ? 60  ARG   A C   1 
ATOM   359  O O   . ARG   A 1 53  ? -10.26511 0.26866   -30.97995 1.000 25.55823 ? 60  ARG   A O   1 
ATOM   360  C CB  . ARG   A 1 53  ? -10.36983 -1.50884  -28.16114 1.000 23.52100 ? 60  ARG   A CB  1 
ATOM   361  C CG  . ARG   A 1 53  ? -11.49359 -0.49574  -27.98819 1.000 23.67991 ? 60  ARG   A CG  1 
ATOM   362  C CD  . ARG   A 1 53  ? -11.68973 -0.14024  -26.52298 1.000 33.86892 ? 60  ARG   A CD  1 
ATOM   363  N NE  . ARG   A 1 53  ? -10.46383 0.34264   -25.89701 1.000 67.18146 ? 60  ARG   A NE  1 
ATOM   364  C CZ  . ARG   A 1 53  ? -10.24665 0.34690   -24.58946 1.000 61.51753 ? 60  ARG   A CZ  1 
ATOM   365  N NH1 . ARG   A 1 53  ? -11.15121 -0.10550  -23.73946 1.000 56.51019 ? 60  ARG   A NH1 1 
ATOM   366  N NH2 . ARG   A 1 53  ? -9.10139  0.83582   -24.12288 1.000 33.87302 ? 60  ARG   A NH2 1 
ATOM   367  N N   . TYR   A 1 54  ? -8.31473  0.14888   -29.85668 1.000 21.40834 ? 61  TYR   A N   1 
ATOM   368  C CA  . TYR   A 1 54  ? -7.83929  1.42036   -30.39262 1.000 22.77433 ? 61  TYR   A CA  1 
ATOM   369  C C   . TYR   A 1 54  ? -7.64896  1.34791   -31.90245 1.000 24.38970 ? 61  TYR   A C   1 
ATOM   370  O O   . TYR   A 1 54  ? -8.01429  2.28272   -32.62420 1.000 26.22226 ? 61  TYR   A O   1 
ATOM   371  C CB  . TYR   A 1 54  ? -6.53606  1.82809   -29.70186 1.000 26.32704 ? 61  TYR   A CB  1 
ATOM   372  C CG  . TYR   A 1 54  ? -5.87697  3.04780   -30.31082 1.000 27.27267 ? 61  TYR   A CG  1 
ATOM   373  C CD1 . TYR   A 1 54  ? -6.31074  4.32729   -29.99147 1.000 33.86561 ? 61  TYR   A CD1 1 
ATOM   374  C CD2 . TYR   A 1 54  ? -4.81438  2.91882   -31.19853 1.000 39.01362 ? 61  TYR   A CD2 1 
ATOM   375  C CE1 . TYR   A 1 54  ? -5.71513  5.44411   -30.54648 1.000 28.48524 ? 61  TYR   A CE1 1 
ATOM   376  C CE2 . TYR   A 1 54  ? -4.21136  4.03034   -31.75766 1.000 43.06163 ? 61  TYR   A CE2 1 
ATOM   377  C CZ  . TYR   A 1 54  ? -4.66635  5.29002   -31.42739 1.000 39.18483 ? 61  TYR   A CZ  1 
ATOM   378  O OH  . TYR   A 1 54  ? -4.06974  6.40180   -31.98006 1.000 46.11996 ? 61  TYR   A OH  1 
ATOM   379  N N   . GLU   A 1 55  ? -7.08177  0.24630   -32.39967 1.000 24.26299 ? 62  GLU   A N   1 
ATOM   380  C CA  . GLU   A 1 55  ? -6.89076  0.10875   -33.83869 1.000 22.14084 ? 62  GLU   A CA  1 
ATOM   381  C C   . GLU   A 1 55  ? -8.22267  0.08729   -34.57631 1.000 24.39580 ? 62  GLU   A C   1 
ATOM   382  O O   . GLU   A 1 55  ? -8.32150  0.60597   -35.69346 1.000 25.74679 ? 62  GLU   A O   1 
ATOM   383  C CB  . GLU   A 1 55  ? -6.08547  -1.15635  -34.14480 1.000 26.57779 ? 62  GLU   A CB  1 
ATOM   384  C CG  . GLU   A 1 55  ? -4.60261  -1.05229  -33.81834 1.000 32.16694 ? 62  GLU   A CG  1 
ATOM   385  C CD  . GLU   A 1 55  ? -3.77658  -2.14150  -34.48257 1.000 49.28452 ? 62  GLU   A CD  1 
ATOM   386  O OE1 . GLU   A 1 55  ? -4.35987  -3.00303  -35.17359 1.000 44.45334 ? 62  GLU   A OE1 1 
ATOM   387  O OE2 . GLU   A 1 55  ? -2.53795  -2.12878  -34.32708 1.000 48.52450 ? 62  GLU   A OE2 1 
ATOM   388  N N   . SER   A 1 56  ? -9.26069  -0.48448  -33.96218 1.000 23.10231 ? 63  SER   A N   1 
ATOM   389  C CA  . SER   A 1 56  ? -10.56466 -0.55957  -34.61070 1.000 25.40491 ? 63  SER   A CA  1 
ATOM   390  C C   . SER   A 1 56  ? -11.24358 0.80064   -34.73102 1.000 26.36039 ? 63  SER   A C   1 
ATOM   391  O O   . SER   A 1 56  ? -12.18259 0.93845   -35.52290 1.000 29.28633 ? 63  SER   A O   1 
ATOM   392  C CB  . SER   A 1 56  ? -11.47485 -1.52529  -33.85016 1.000 23.92951 ? 63  SER   A CB  1 
ATOM   393  O OG  . SER   A 1 56  ? -11.86259 -0.98642  -32.60009 1.000 30.84336 ? 63  SER   A OG  1 
ATOM   394  N N   . LEU   A 1 57  ? -10.79733 1.80651   -33.97152 1.000 27.02905 ? 64  LEU   A N   1 
ATOM   395  C CA  . LEU   A 1 57  ? -11.42604 3.12319   -34.05608 1.000 28.88218 ? 64  LEU   A CA  1 
ATOM   396  C C   . LEU   A 1 57  ? -11.17269 3.79028   -35.40321 1.000 35.59344 ? 64  LEU   A C   1 
ATOM   397  O O   . LEU   A 1 57  ? -11.99604 4.59148   -35.85978 1.000 39.54105 ? 64  LEU   A O   1 
ATOM   398  C CB  . LEU   A 1 57  ? -10.93396 4.02221   -32.91916 1.000 31.16133 ? 64  LEU   A CB  1 
ATOM   399  C CG  . LEU   A 1 57  ? -11.17788 3.54985   -31.48227 1.000 34.39885 ? 64  LEU   A CG  1 
ATOM   400  C CD1 . LEU   A 1 57  ? -10.50186 4.48265   -30.48722 1.000 38.81504 ? 64  LEU   A CD1 1 
ATOM   401  C CD2 . LEU   A 1 57  ? -12.66783 3.46079   -31.19936 1.000 43.11721 ? 64  LEU   A CD2 1 
ATOM   402  N N   . THR   A 1 58  ? -10.04752 3.48433   -36.04856 1.000 30.84142 ? 65  THR   A N   1 
ATOM   403  C CA  . THR   A 1 58  ? -9.74052  4.02141   -37.36593 1.000 36.08552 ? 65  THR   A CA  1 
ATOM   404  C C   . THR   A 1 58  ? -9.88999  2.99586   -38.48131 1.000 40.33328 ? 65  THR   A C   1 
ATOM   405  O O   . THR   A 1 58  ? -9.82126  3.36992   -39.65719 1.000 43.03951 ? 65  THR   A O   1 
ATOM   406  C CB  . THR   A 1 58  ? -8.31425  4.59227   -37.39015 1.000 34.76483 ? 65  THR   A CB  1 
ATOM   407  O OG1 . THR   A 1 58  ? -7.38350  3.57950   -36.99321 1.000 37.06765 ? 65  THR   A OG1 1 
ATOM   408  C CG2 . THR   A 1 58  ? -8.19807  5.77108   -36.43557 1.000 48.14784 ? 65  THR   A CG2 1 
ATOM   409  N N   . ASP   A 1 59  ? -10.09413 1.72425   -38.14609 1.000 33.26152 ? 66  ASP   A N   1 
ATOM   410  C CA  . ASP   A 1 59  ? -10.28173 0.67081   -39.14541 1.000 34.25456 ? 66  ASP   A CA  1 
ATOM   411  C C   . ASP   A 1 59  ? -11.22541 -0.36319  -38.55447 1.000 37.30725 ? 66  ASP   A C   1 
ATOM   412  O O   . ASP   A 1 59  ? -10.79837 -1.35189  -37.94873 1.000 34.85910 ? 66  ASP   A O   1 
ATOM   413  C CB  . ASP   A 1 59  ? -8.94458  0.04024   -39.54464 1.000 34.29487 ? 66  ASP   A CB  1 
ATOM   414  C CG  . ASP   A 1 59  ? -9.06968  -0.92975  -40.71430 1.000 38.82972 ? 66  ASP   A CG  1 
ATOM   415  O OD1 . ASP   A 1 59  ? -10.20001 -1.33175  -41.06370 1.000 46.44010 ? 66  ASP   A OD1 1 
ATOM   416  O OD2 . ASP   A 1 59  ? -8.02272  -1.28704  -41.29428 1.000 47.55736 ? 66  ASP   A OD2 1 
ATOM   417  N N   . PRO   A 1 60  ? -12.53618 -0.15409  -38.70086 1.000 35.70349 ? 67  PRO   A N   1 
ATOM   418  C CA  . PRO   A 1 60  ? -13.50200 -1.10561  -38.12738 1.000 41.51695 ? 67  PRO   A CA  1 
ATOM   419  C C   . PRO   A 1 60  ? -13.32460 -2.53529  -38.60996 1.000 41.84084 ? 67  PRO   A C   1 
ATOM   420  O O   . PRO   A 1 60  ? -13.74704 -3.47023  -37.91686 1.000 36.77227 ? 67  PRO   A O   1 
ATOM   421  C CB  . PRO   A 1 60  ? -14.84628 -0.52757  -38.58473 1.000 43.63285 ? 67  PRO   A CB  1 
ATOM   422  C CG  . PRO   A 1 60  ? -14.59574 0.94002   -38.62483 1.000 48.05296 ? 67  PRO   A CG  1 
ATOM   423  C CD  . PRO   A 1 60  ? -13.20686 1.05286   -39.21419 1.000 46.77515 ? 67  PRO   A CD  1 
ATOM   424  N N   . SER   A 1 61  ? -12.71665 -2.73603  -39.78288 1.000 31.55671 ? 68  SER   A N   1 
ATOM   425  C CA  . SER   A 1 61  ? -12.53515 -4.08170  -40.31571 1.000 33.29348 ? 68  SER   A CA  1 
ATOM   426  C C   . SER   A 1 61  ? -11.55364 -4.90833  -39.49454 1.000 34.36806 ? 68  SER   A C   1 
ATOM   427  O O   . SER   A 1 61  ? -11.50890 -6.13253  -39.65556 1.000 32.43832 ? 68  SER   A O   1 
ATOM   428  C CB  . SER   A 1 61  ? -12.06222 -4.01290  -41.76777 1.000 37.54817 ? 68  SER   A CB  1 
ATOM   429  O OG  . SER   A 1 61  ? -10.67482 -3.73507  -41.83547 1.000 44.77902 ? 68  SER   A OG  1 
ATOM   430  N N   . LYS   A 1 62  ? -10.76638 -4.27371  -38.62245 1.000 27.75926 ? 69  LYS   A N   1 
ATOM   431  C CA  . LYS   A 1 62  ? -9.86490  -5.02645  -37.75816 1.000 31.10377 ? 69  LYS   A CA  1 
ATOM   432  C C   . LYS   A 1 62  ? -10.61414 -5.95433  -36.81336 1.000 26.47339 ? 69  LYS   A C   1 
ATOM   433  O O   . LYS   A 1 62  ? -10.00354 -6.86252  -36.24048 1.000 28.94052 ? 69  LYS   A O   1 
ATOM   434  C CB  . LYS   A 1 62  ? -8.98343  -4.07445  -36.95058 1.000 32.52654 ? 69  LYS   A CB  1 
ATOM   435  C CG  . LYS   A 1 62  ? -8.19597  -3.08621  -37.78853 1.000 40.50990 ? 69  LYS   A CG  1 
ATOM   436  C CD  . LYS   A 1 62  ? -6.76603  -2.98087  -37.29707 1.000 36.14772 ? 69  LYS   A CD  1 
ATOM   437  C CE  . LYS   A 1 62  ? -5.82221  -2.57729  -38.41549 1.000 38.13372 ? 69  LYS   A CE  1 
ATOM   438  N NZ  . LYS   A 1 62  ? -4.40011  -2.82311  -38.05116 1.000 43.28632 ? 69  LYS   A NZ  1 
ATOM   439  N N   . LEU   A 1 63  ? -11.91598 -5.74388  -36.63267 1.000 27.73727 ? 70  LEU   A N   1 
ATOM   440  C CA  . LEU   A 1 63  ? -12.74315 -6.58985  -35.78614 1.000 31.15524 ? 70  LEU   A CA  1 
ATOM   441  C C   . LEU   A 1 63  ? -13.51290 -7.63438  -36.58454 1.000 30.82467 ? 70  LEU   A C   1 
ATOM   442  O O   . LEU   A 1 63  ? -14.39457 -8.29929  -36.02987 1.000 30.09785 ? 70  LEU   A O   1 
ATOM   443  C CB  . LEU   A 1 63  ? -13.70802 -5.72726  -34.96927 1.000 24.59686 ? 70  LEU   A CB  1 
ATOM   444  C CG  . LEU   A 1 63  ? -13.05129 -4.87972  -33.87482 1.000 29.34134 ? 70  LEU   A CG  1 
ATOM   445  C CD1 . LEU   A 1 63  ? -14.09628 -4.13266  -33.05496 1.000 37.32983 ? 70  LEU   A CD1 1 
ATOM   446  C CD2 . LEU   A 1 63  ? -12.16092 -5.73344  -32.97949 1.000 26.53018 ? 70  LEU   A CD2 1 
ATOM   447  N N   . ASP   A 1 64  ? -13.20287 -7.78822  -37.87605 1.000 30.68112 ? 71  ASP   A N   1 
ATOM   448  C CA  . ASP   A 1 64  ? -13.82482 -8.84434  -38.66866 1.000 32.59798 ? 71  ASP   A CA  1 
ATOM   449  C C   . ASP   A 1 64  ? -13.48727 -10.22242 -38.11964 1.000 28.77853 ? 71  ASP   A C   1 
ATOM   450  O O   . ASP   A 1 64  ? -14.24744 -11.17600 -38.32196 1.000 30.77005 ? 71  ASP   A O   1 
ATOM   451  C CB  . ASP   A 1 64  ? -13.38367 -8.74185  -40.12790 1.000 34.37832 ? 71  ASP   A CB  1 
ATOM   452  C CG  . ASP   A 1 64  ? -13.95457 -7.52354  -40.82683 1.000 48.73660 ? 71  ASP   A CG  1 
ATOM   453  O OD1 . ASP   A 1 64  ? -14.78296 -6.81589  -40.21582 1.000 43.12138 ? 71  ASP   A OD1 1 
ATOM   454  O OD2 . ASP   A 1 64  ? -13.56660 -7.27133  -41.98674 1.000 45.45706 ? 71  ASP   A OD2 1 
ATOM   455  N N   . SER   A 1 65  ? -12.35819 -10.34375 -37.42441 1.000 26.49740 ? 72  SER   A N   1 
ATOM   456  C CA  . SER   A 1 65  ? -11.94959 -11.58620 -36.78478 1.000 32.48337 ? 72  SER   A CA  1 
ATOM   457  C C   . SER   A 1 65  ? -12.60874 -11.80167 -35.42844 1.000 38.21403 ? 72  SER   A C   1 
ATOM   458  O O   . SER   A 1 65  ? -12.25921 -12.76323 -34.73606 1.000 34.02053 ? 72  SER   A O   1 
ATOM   459  C CB  . SER   A 1 65  ? -10.42690 -11.61187 -36.62976 1.000 31.17946 ? 72  SER   A CB  1 
ATOM   460  O OG  . SER   A 1 65  ? -9.94211  -10.35809 -36.18194 1.000 31.11359 ? 72  SER   A OG  1 
ATOM   461  N N   . GLY   A 1 66  ? -13.54627 -10.94160 -35.03479 1.000 31.32981 ? 73  GLY   A N   1 
ATOM   462  C CA  . GLY   A 1 66  ? -14.20762 -11.06690 -33.74986 1.000 31.50150 ? 73  GLY   A CA  1 
ATOM   463  C C   . GLY   A 1 66  ? -14.48193 -9.73177  -33.08804 1.000 28.41429 ? 73  GLY   A C   1 
ATOM   464  O O   . GLY   A 1 66  ? -13.55133 -8.97645  -32.79197 1.000 28.69948 ? 73  GLY   A O   1 
ATOM   465  N N   . LYS   A 1 67  ? -15.75987 -9.43253  -32.84459 1.000 27.32970 ? 74  LYS   A N   1 
ATOM   466  C CA  . LYS   A 1 67  ? -16.12961 -8.15940  -32.23676 1.000 30.69232 ? 74  LYS   A CA  1 
ATOM   467  C C   . LYS   A 1 67  ? -16.02634 -8.18925  -30.71801 1.000 30.21299 ? 74  LYS   A C   1 
ATOM   468  O O   . LYS   A 1 67  ? -15.79230 -7.14556  -30.09888 1.000 32.42555 ? 74  LYS   A O   1 
ATOM   469  C CB  . LYS   A 1 67  ? -17.55284 -7.77608  -32.64278 1.000 33.31227 ? 74  LYS   A CB  1 
ATOM   470  C CG  . LYS   A 1 67  ? -17.63529 -6.75962  -33.77366 1.000 47.51699 ? 74  LYS   A CG  1 
ATOM   471  C CD  . LYS   A 1 67  ? -19.04176 -6.64932  -34.37328 1.000 65.86722 ? 74  LYS   A CD  1 
ATOM   472  C CE  . LYS   A 1 67  ? -20.17119 -6.98062  -33.39272 1.000 75.18795 ? 74  LYS   A CE  1 
ATOM   473  N NZ  . LYS   A 1 67  ? -20.12762 -6.21224  -32.11007 1.000 76.09128 ? 74  LYS   A NZ  1 
ATOM   474  N N   . GLU   A 1 68  ? -16.19779 -9.35546  -30.10280 1.000 26.07049 ? 75  GLU   A N   1 
ATOM   475  C CA  . GLU   A 1 68  ? -16.23206 -9.42644  -28.64898 1.000 24.81902 ? 75  GLU   A CA  1 
ATOM   476  C C   . GLU   A 1 68  ? -14.83657 -9.23469  -28.06767 1.000 26.65761 ? 75  GLU   A C   1 
ATOM   477  O O   . GLU   A 1 68  ? -13.85674 -9.80324  -28.55566 1.000 26.63231 ? 75  GLU   A O   1 
ATOM   478  C CB  . GLU   A 1 68  ? -16.81301 -10.76308 -28.18474 1.000 29.68093 ? 75  GLU   A CB  1 
ATOM   479  C CG  . GLU   A 1 68  ? -18.31313 -10.93267 -28.42843 1.000 32.81465 ? 75  GLU   A CG  1 
ATOM   480  C CD  . GLU   A 1 68  ? -18.67349 -10.95842 -29.89888 1.000 61.57481 ? 75  GLU   A CD  1 
ATOM   481  O OE1 . GLU   A 1 68  ? -18.06785 -11.76039 -30.64110 1.000 61.34801 ? 75  GLU   A OE1 1 
ATOM   482  O OE2 . GLU   A 1 68  ? -19.54916 -10.17220 -30.31848 1.000 70.60870 ? 75  GLU   A OE2 1 
ATOM   483  N N   . LEU   A 1 69  ? -14.75321 -8.42559  -27.01433 1.000 20.72557 ? 76  LEU   A N   1 
ATOM   484  C CA  . LEU   A 1 69  ? -13.49916 -8.11970  -26.33225 1.000 21.54908 ? 76  LEU   A CA  1 
ATOM   485  C C   . LEU   A 1 69  ? -13.63437 -8.60588  -24.89409 1.000 22.42269 ? 76  LEU   A C   1 
ATOM   486  O O   . LEU   A 1 69  ? -14.31759 -7.96838  -24.08543 1.000 22.22961 ? 76  LEU   A O   1 
ATOM   487  C CB  . LEU   A 1 69  ? -13.21139 -6.61836  -26.38150 1.000 22.40835 ? 76  LEU   A CB  1 
ATOM   488  C CG  . LEU   A 1 69  ? -13.07935 -5.99275  -27.77450 1.000 26.32967 ? 76  LEU   A CG  1 
ATOM   489  C CD1 . LEU   A 1 69  ? -12.69688 -4.51911  -27.67997 1.000 31.32789 ? 76  LEU   A CD1 1 
ATOM   490  C CD2 . LEU   A 1 69  ? -12.07837 -6.75670  -28.62139 1.000 25.64646 ? 76  LEU   A CD2 1 
ATOM   491  N N   . HIS   A 1 70  ? -12.99400 -9.72739  -24.56608 1.000 21.43158 ? 77  HIS   A N   1 
ATOM   492  C CA  . HIS   A 1 70  ? -13.23818 -10.34800 -23.26973 1.000 21.46312 ? 77  HIS   A CA  1 
ATOM   493  C C   . HIS   A 1 70  ? -12.04850 -11.20379 -22.85653 1.000 19.40703 ? 77  HIS   A C   1 
ATOM   494  O O   . HIS   A 1 70  ? -11.11809 -11.43842 -23.63027 1.000 19.51772 ? 77  HIS   A O   1 
ATOM   495  C CB  . HIS   A 1 70  ? -14.52982 -11.17597 -23.29278 1.000 22.56735 ? 77  HIS   A CB  1 
ATOM   496  C CG  . HIS   A 1 70  ? -14.49959 -12.33174 -24.24707 1.000 23.22821 ? 77  HIS   A CG  1 
ATOM   497  N ND1 . HIS   A 1 70  ? -15.40338 -12.46338 -25.27942 1.000 30.31963 ? 77  HIS   A ND1 1 
ATOM   498  C CD2 . HIS   A 1 70  ? -13.69272 -13.41756 -24.31546 1.000 27.42678 ? 77  HIS   A CD2 1 
ATOM   499  C CE1 . HIS   A 1 70  ? -15.14681 -13.57183 -25.95053 1.000 26.44799 ? 77  HIS   A CE1 1 
ATOM   500  N NE2 . HIS   A 1 70  ? -14.11377 -14.17016 -25.38551 1.000 25.48138 ? 77  HIS   A NE2 1 
ATOM   501  N N   . ILE   A 1 71  ? -12.10422 -11.66776 -21.60973 1.000 18.11580 ? 78  ILE   A N   1 
ATOM   502  C CA  . ILE   A 1 71  ? -11.10001 -12.53730 -21.01078 1.000 18.58643 ? 78  ILE   A CA  1 
ATOM   503  C C   . ILE   A 1 71  ? -11.82348 -13.71504 -20.37321 1.000 20.87269 ? 78  ILE   A C   1 
ATOM   504  O O   . ILE   A 1 71  ? -12.75694 -13.51719 -19.58591 1.000 21.26888 ? 78  ILE   A O   1 
ATOM   505  C CB  . ILE   A 1 71  ? -10.26112 -11.79815 -19.94988 1.000 18.97801 ? 78  ILE   A CB  1 
ATOM   506  C CG1 . ILE   A 1 71  ? -9.55414  -10.58578 -20.55750 1.000 19.27214 ? 78  ILE   A CG1 1 
ATOM   507  C CG2 . ILE   A 1 71  ? -9.26398  -12.75135 -19.29893 1.000 21.92178 ? 78  ILE   A CG2 1 
ATOM   508  C CD1 . ILE   A 1 71  ? -8.89298  -9.69366  -19.52613 1.000 18.74924 ? 78  ILE   A CD1 1 
ATOM   509  N N   . ASN   A 1 72  ? -11.40032 -14.93361 -20.70841 1.000 18.56527 ? 79  ASN   A N   1 
ATOM   510  C CA  . ASN   A 1 72  ? -11.94242 -16.14374 -20.10486 1.000 16.98660 ? 79  ASN   A CA  1 
ATOM   511  C C   . ASN   A 1 72  ? -10.85924 -16.86540 -19.31794 1.000 17.39978 ? 79  ASN   A C   1 
ATOM   512  O O   . ASN   A 1 72  ? -9.71763  -16.97551 -19.77246 1.000 19.42698 ? 79  ASN   A O   1 
ATOM   513  C CB  . ASN   A 1 72  ? -12.53611 -17.09155 -21.15894 1.000 16.98393 ? 79  ASN   A CB  1 
ATOM   514  C CG  . ASN   A 1 72  ? -13.74037 -16.49546 -21.86273 1.000 23.01855 ? 79  ASN   A CG  1 
ATOM   515  O OD1 . ASN   A 1 72  ? -14.46801 -15.68489 -21.28815 1.000 24.77846 ? 79  ASN   A OD1 1 
ATOM   516  N ND2 . ASN   A 1 72  ? -13.97143 -16.91192 -23.10161 1.000 22.17588 ? 79  ASN   A ND2 1 
ATOM   517  N N   . LEU   A 1 73  ? -11.22839 -17.35530 -18.13614 1.000 17.68864 ? 80  LEU   A N   1 
ATOM   518  C CA  . LEU   A 1 73  ? -10.34988 -18.14952 -17.28511 1.000 17.86215 ? 80  LEU   A CA  1 
ATOM   519  C C   . LEU   A 1 73  ? -10.91625 -19.55893 -17.20924 1.000 20.25972 ? 80  LEU   A C   1 
ATOM   520  O O   . LEU   A 1 73  ? -12.02773 -19.75509 -16.70915 1.000 19.54955 ? 80  LEU   A O   1 
ATOM   521  C CB  . LEU   A 1 73  ? -10.22952 -17.53827 -15.88649 1.000 17.08834 ? 80  LEU   A CB  1 
ATOM   522  C CG  . LEU   A 1 73  ? -9.76329  -16.08136 -15.83924 1.000 23.20200 ? 80  LEU   A CG  1 
ATOM   523  C CD1 . LEU   A 1 73  ? -9.74966  -15.56325 -14.40391 1.000 21.84890 ? 80  LEU   A CD1 1 
ATOM   524  C CD2 . LEU   A 1 73  ? -8.39690  -15.93381 -16.48804 1.000 21.61451 ? 80  LEU   A CD2 1 
ATOM   525  N N   . ILE   A 1 74  ? -10.16301 -20.53375 -17.70601 1.000 21.16476 ? 81  ILE   A N   1 
ATOM   526  C CA  . ILE   A 1 74  ? -10.67823 -21.89319 -17.85799 1.000 22.92347 ? 81  ILE   A CA  1 
ATOM   527  C C   . ILE   A 1 74  ? -9.78071  -22.88392 -17.12865 1.000 24.64424 ? 81  ILE   A C   1 
ATOM   528  O O   . ILE   A 1 74  ? -8.69513  -23.22540 -17.62378 1.000 21.60623 ? 81  ILE   A O   1 
ATOM   529  C CB  . ILE   A 1 74  ? -10.81362 -22.26955 -19.34222 1.000 19.99322 ? 81  ILE   A CB  1 
ATOM   530  C CG1 . ILE   A 1 74  ? -11.51280 -21.14817 -20.11206 1.000 24.22066 ? 81  ILE   A CG1 1 
ATOM   531  C CG2 . ILE   A 1 74  ? -11.57861 -23.57985 -19.49565 1.000 23.38365 ? 81  ILE   A CG2 1 
ATOM   532  C CD1 . ILE   A 1 74  ? -11.62254 -21.39850 -21.60029 1.000 26.87403 ? 81  ILE   A CD1 1 
ATOM   533  N N   . PRO   A 1 75  ? -10.18500 -23.37197 -15.96000 1.000 23.99172 ? 82  PRO   A N   1 
ATOM   534  C CA  . PRO   A 1 75  ? -9.44434  -24.44625 -15.29790 1.000 23.05452 ? 82  PRO   A CA  1 
ATOM   535  C C   . PRO   A 1 75  ? -9.90032  -25.81414 -15.77852 1.000 28.14629 ? 82  PRO   A C   1 
ATOM   536  O O   . PRO   A 1 75  ? -11.03954 -26.00975 -16.20748 1.000 27.09589 ? 82  PRO   A O   1 
ATOM   537  C CB  . PRO   A 1 75  ? -9.79031  -24.23855 -13.81635 1.000 26.10286 ? 82  PRO   A CB  1 
ATOM   538  C CG  . PRO   A 1 75  ? -11.14836 -23.58306 -13.83137 1.000 24.96555 ? 82  PRO   A CG  1 
ATOM   539  C CD  . PRO   A 1 75  ? -11.36156 -22.94355 -15.18442 1.000 22.50812 ? 82  PRO   A CD  1 
ATOM   540  N N   . ASN   A 1 76  ? -8.98293  -26.77739 -15.70334 1.000 25.28771 ? 83  ASN   A N   1 
ATOM   541  C CA  . ASN   A 1 76  ? -9.27792  -28.15060 -16.10702 1.000 23.46446 ? 83  ASN   A CA  1 
ATOM   542  C C   . ASN   A 1 76  ? -8.44350  -29.07424 -15.22627 1.000 27.39638 ? 83  ASN   A C   1 
ATOM   543  O O   . ASN   A 1 76  ? -7.23750  -29.21475 -15.44929 1.000 28.61222 ? 83  ASN   A O   1 
ATOM   544  C CB  . ASN   A 1 76  ? -8.97783  -28.35647 -17.59579 1.000 29.66316 ? 83  ASN   A CB  1 
ATOM   545  C CG  . ASN   A 1 76  ? -9.38360  -29.73434 -18.10482 1.000 28.91541 ? 83  ASN   A CG  1 
ATOM   546  O OD1 . ASN   A 1 76  ? -9.22997  -30.74267 -17.41930 1.000 34.15652 ? 83  ASN   A OD1 1 
ATOM   547  N ND2 . ASN   A 1 76  ? -9.90717  -29.77474 -19.32634 1.000 37.24449 ? 83  ASN   A ND2 1 
ATOM   548  N N   . LYS   A 1 77  ? -9.07839  -29.69472 -14.22017 1.000 31.32235 ? 84  LYS   A N   1 
ATOM   549  C CA  . LYS   A 1 77  ? -8.34168  -30.56812 -13.30494 1.000 35.27885 ? 84  LYS   A CA  1 
ATOM   550  C C   . LYS   A 1 77  ? -7.83169  -31.82471 -13.99396 1.000 31.86738 ? 84  LYS   A C   1 
ATOM   551  O O   . LYS   A 1 77  ? -6.79021  -32.35980 -13.59874 1.000 38.54223 ? 84  LYS   A O   1 
ATOM   552  C CB  . LYS   A 1 77  ? -9.19690  -30.98709 -12.10346 1.000 39.11380 ? 84  LYS   A CB  1 
ATOM   553  C CG  . LYS   A 1 77  ? -10.02601 -29.91130 -11.43510 1.000 43.57035 ? 84  LYS   A CG  1 
ATOM   554  C CD  . LYS   A 1 77  ? -9.66258  -29.77409 -9.96246  1.000 58.04505 ? 84  LYS   A CD  1 
ATOM   555  C CE  . LYS   A 1 77  ? -10.83729 -29.27465 -9.13136  1.000 66.94654 ? 84  LYS   A CE  1 
ATOM   556  N NZ  . LYS   A 1 77  ? -11.37715 -27.97516 -9.60550  1.000 62.89716 ? 84  LYS   A NZ  1 
ATOM   557  N N   . GLN   A 1 78  ? -8.55674  -32.33050 -14.99407 1.000 38.06349 ? 85  GLN   A N   1 
ATOM   558  C CA  . GLN   A 1 78  ? -8.11976  -33.55500 -15.65663 1.000 41.51472 ? 85  GLN   A CA  1 
ATOM   559  C C   . GLN   A 1 78  ? -6.79609  -33.33848 -16.37536 1.000 47.29155 ? 85  GLN   A C   1 
ATOM   560  O O   . GLN   A 1 78  ? -5.88611  -34.17114 -16.28225 1.000 44.98611 ? 85  GLN   A O   1 
ATOM   561  C CB  . GLN   A 1 78  ? -9.18749  -34.04411 -16.63624 1.000 53.16385 ? 85  GLN   A CB  1 
ATOM   562  C CG  . GLN   A 1 78  ? -10.11117 -35.10546 -16.05539 1.000 65.58974 ? 85  GLN   A CG  1 
ATOM   563  C CD  . GLN   A 1 78  ? -9.81783  -36.50030 -16.57752 1.000 74.69250 ? 85  GLN   A CD  1 
ATOM   564  O OE1 . GLN   A 1 78  ? -9.67616  -36.71374 -17.78219 1.000 81.40540 ? 85  GLN   A OE1 1 
ATOM   565  N NE2 . GLN   A 1 78  ? -9.72757  -37.46146 -15.66504 1.000 70.09349 ? 85  GLN   A NE2 1 
ATOM   566  N N   . ASP   A 1 79  ? -6.66726  -32.21884 -17.08247 1.000 29.84455 ? 86  ASP   A N   1 
ATOM   567  C CA  . ASP   A 1 79  ? -5.43336  -31.86005 -17.76161 1.000 36.65578 ? 86  ASP   A CA  1 
ATOM   568  C C   . ASP   A 1 79  ? -4.45018  -31.12592 -16.86033 1.000 35.73176 ? 86  ASP   A C   1 
ATOM   569  O O   . ASP   A 1 79  ? -3.29567  -30.93737 -17.25914 1.000 34.04266 ? 86  ASP   A O   1 
ATOM   570  C CB  . ASP   A 1 79  ? -5.74499  -30.99068 -18.98406 1.000 34.67911 ? 86  ASP   A CB  1 
ATOM   571  C CG  . ASP   A 1 79  ? -6.60536  -31.70937 -20.00402 1.000 51.34235 ? 86  ASP   A CG  1 
ATOM   572  O OD1 . ASP   A 1 79  ? -6.76345  -32.94266 -19.88476 1.000 55.32361 ? 86  ASP   A OD1 1 
ATOM   573  O OD2 . ASP   A 1 79  ? -7.13226  -31.04042 -20.91699 1.000 56.69544 ? 86  ASP   A OD2 1 
ATOM   574  N N   . ARG   A 1 80  ? -4.87602  -30.71839 -15.66295 1.000 27.35471 ? 87  ARG   A N   1 
ATOM   575  C CA  . ARG   A 1 80  ? -4.06776  -29.88694 -14.76867 1.000 26.81104 ? 87  ARG   A CA  1 
ATOM   576  C C   . ARG   A 1 80  ? -3.56245  -28.63538 -15.48259 1.000 23.53802 ? 87  ARG   A C   1 
ATOM   577  O O   . ARG   A 1 80  ? -2.37268  -28.31191 -15.46506 1.000 26.23568 ? 87  ARG   A O   1 
ATOM   578  C CB  . ARG   A 1 80  ? -2.91026  -30.68420 -14.16211 1.000 28.33052 ? 87  ARG   A CB  1 
ATOM   579  C CG  . ARG   A 1 80  ? -2.55495  -30.23312 -12.75351 1.000 33.40367 ? 87  ARG   A CG  1 
ATOM   580  C CD  . ARG   A 1 80  ? -1.63426  -31.21412 -12.04452 1.000 35.33227 ? 87  ARG   A CD  1 
ATOM   581  N NE  . ARG   A 1 80  ? -0.23260  -31.03745 -12.40029 1.000 47.65645 ? 87  ARG   A NE  1 
ATOM   582  C CZ  . ARG   A 1 80  ? 0.65895   -32.01886 -12.40919 1.000 51.58199 ? 87  ARG   A CZ  1 
ATOM   583  N NH1 . ARG   A 1 80  ? 0.33449   -33.24923 -12.04700 1.000 44.58142 ? 87  ARG   A NH1 1 
ATOM   584  N NH2 . ARG   A 1 80  ? 1.90838   -31.75869 -12.78349 1.000 49.22212 ? 87  ARG   A NH2 1 
ATOM   585  N N   . THR   A 1 81  ? -4.48978  -27.92041 -16.11638 1.000 22.31742 ? 88  THR   A N   1 
ATOM   586  C CA  . THR   A 1 81  ? -4.16651  -26.69934 -16.83620 1.000 18.86552 ? 88  THR   A CA  1 
ATOM   587  C C   . THR   A 1 81  ? -5.09675  -25.57389 -16.41065 1.000 22.93490 ? 88  THR   A C   1 
ATOM   588  O O   . THR   A 1 81  ? -6.28590  -25.78683 -16.16097 1.000 23.39036 ? 88  THR   A O   1 
ATOM   589  C CB  . THR   A 1 81  ? -4.27591  -26.87745 -18.35832 1.000 24.54149 ? 88  THR   A CB  1 
ATOM   590  O OG1 . THR   A 1 81  ? -5.60908  -27.28067 -18.69379 1.000 26.84889 ? 88  THR   A OG1 1 
ATOM   591  C CG2 . THR   A 1 81  ? -3.28998  -27.92806 -18.85918 1.000 30.01001 ? 88  THR   A CG2 1 
ATOM   592  N N   . LEU   A 1 82  ? -4.53691  -24.36935 -16.33313 1.000 22.70509 ? 89  LEU   A N   1 
ATOM   593  C CA  . LEU   A 1 82  ? -5.30933  -23.13808 -16.23146 1.000 19.56088 ? 89  LEU   A CA  1 
ATOM   594  C C   . LEU   A 1 82  ? -5.05275  -22.32989 -17.49305 1.000 22.41751 ? 89  LEU   A C   1 
ATOM   595  O O   . LEU   A 1 82  ? -3.89938  -22.02410 -17.81567 1.000 22.26002 ? 89  LEU   A O   1 
ATOM   596  C CB  . LEU   A 1 82  ? -4.94314  -22.33177 -14.98262 1.000 19.91057 ? 89  LEU   A CB  1 
ATOM   597  C CG  . LEU   A 1 82  ? -5.65163  -20.97761 -14.89551 1.000 19.33546 ? 89  LEU   A CG  1 
ATOM   598  C CD1 . LEU   A 1 82  ? -7.14898  -21.15968 -14.67062 1.000 22.13170 ? 89  LEU   A CD1 1 
ATOM   599  C CD2 . LEU   A 1 82  ? -5.04707  -20.11678 -13.80102 1.000 20.94130 ? 89  LEU   A CD2 1 
ATOM   600  N N   . THR   A 1 83  ? -6.12111  -22.00541 -18.21070 1.000 20.82162 ? 90  THR   A N   1 
ATOM   601  C CA  . THR   A 1 83  ? -6.03211  -21.32567 -19.49320 1.000 17.14633 ? 90  THR   A CA  1 
ATOM   602  C C   . THR   A 1 83  ? -6.59608  -19.91657 -19.37102 1.000 23.80000 ? 90  THR   A C   1 
ATOM   603  O O   . THR   A 1 83  ? -7.70960  -19.73009 -18.86826 1.000 23.51251 ? 90  THR   A O   1 
ATOM   604  C CB  . THR   A 1 83  ? -6.78165  -22.10772 -20.57319 1.000 20.75640 ? 90  THR   A CB  1 
ATOM   605  O OG1 . THR   A 1 83  ? -6.18779  -23.40107 -20.73787 1.000 22.57520 ? 90  THR   A OG1 1 
ATOM   606  C CG2 . THR   A 1 83  ? -6.72992  -21.37303 -21.87851 1.000 22.51707 ? 90  THR   A CG2 1 
ATOM   607  N N   . ILE   A 1 84  ? -5.82113  -18.93179 -19.82249 1.000 21.41886 ? 91  ILE   A N   1 
ATOM   608  C CA  . ILE   A 1 84  ? -6.23884  -17.53407 -19.85908 1.000 19.46044 ? 91  ILE   A CA  1 
ATOM   609  C C   . ILE   A 1 84  ? -6.42405  -17.16795 -21.32411 1.000 22.53639 ? 91  ILE   A C   1 
ATOM   610  O O   . ILE   A 1 84  ? -5.44522  -17.06971 -22.07514 1.000 22.07278 ? 91  ILE   A O   1 
ATOM   611  C CB  . ILE   A 1 84  ? -5.22048  -16.60059 -19.18723 1.000 22.94889 ? 91  ILE   A CB  1 
ATOM   612  C CG1 . ILE   A 1 84  ? -5.08734  -16.90379 -17.68993 1.000 26.10548 ? 91  ILE   A CG1 1 
ATOM   613  C CG2 . ILE   A 1 84  ? -5.62412  -15.14600 -19.39202 1.000 23.85389 ? 91  ILE   A CG2 1 
ATOM   614  C CD1 . ILE   A 1 84  ? -4.05537  -17.96257 -17.36233 1.000 30.71607 ? 91  ILE   A CD1 1 
ATOM   615  N N   . VAL   A 1 85  ? -7.67325  -16.96890 -21.73726 1.000 20.82247 ? 92  VAL   A N   1 
ATOM   616  C CA  . VAL   A 1 85  ? -8.00781  -16.65171 -23.12105 1.000 20.01976 ? 92  VAL   A CA  1 
ATOM   617  C C   . VAL   A 1 85  ? -8.43181  -15.19265 -23.19519 1.000 21.87744 ? 92  VAL   A C   1 
ATOM   618  O O   . VAL   A 1 85  ? -9.19702  -14.71825 -22.34832 1.000 22.55074 ? 92  VAL   A O   1 
ATOM   619  C CB  . VAL   A 1 85  ? -9.11980  -17.56681 -23.66714 1.000 23.08537 ? 92  VAL   A CB  1 
ATOM   620  C CG1 . VAL   A 1 85  ? -9.25457  -17.39852 -25.17754 1.000 25.86834 ? 92  VAL   A CG1 1 
ATOM   621  C CG2 . VAL   A 1 85  ? -8.84402  -19.01167 -23.32964 1.000 28.01988 ? 92  VAL   A CG2 1 
ATOM   622  N N   . ASP   A 1 86  ? -7.93572  -14.48488 -24.20761 1.000 17.61670 ? 93  ASP   A N   1 
ATOM   623  C CA  . ASP   A 1 86  ? -8.38675  -13.13780 -24.51723 1.000 17.35915 ? 93  ASP   A CA  1 
ATOM   624  C C   . ASP   A 1 86  ? -8.55105  -13.01007 -26.02327 1.000 19.36277 ? 93  ASP   A C   1 
ATOM   625  O O   . ASP   A 1 86  ? -7.94869  -13.75209 -26.80216 1.000 20.13664 ? 93  ASP   A O   1 
ATOM   626  C CB  . ASP   A 1 86  ? -7.42660  -12.06804 -23.95812 1.000 22.16063 ? 93  ASP   A CB  1 
ATOM   627  C CG  . ASP   A 1 86  ? -6.11797  -11.95962 -24.73843 1.000 26.68794 ? 93  ASP   A CG  1 
ATOM   628  O OD1 . ASP   A 1 86  ? -5.05472  -12.26398 -24.15499 1.000 22.80660 ? 93  ASP   A OD1 1 
ATOM   629  O OD2 . ASP   A 1 86  ? -6.13496  -11.52658 -25.91375 1.000 27.89970 ? 93  ASP   A OD2 1 
ATOM   630  N N   . THR   A 1 87  ? -9.40095  -12.07036 -26.42491 1.000 20.57447 ? 94  THR   A N   1 
ATOM   631  C CA  . THR   A 1 87  ? -9.62070  -11.75768 -27.83492 1.000 20.60827 ? 94  THR   A CA  1 
ATOM   632  C C   . THR   A 1 87  ? -8.94583  -10.44904 -28.22564 1.000 19.82479 ? 94  THR   A C   1 
ATOM   633  O O   . THR   A 1 87  ? -9.50012  -9.63928  -28.97462 1.000 21.16151 ? 94  THR   A O   1 
ATOM   634  C CB  . THR   A 1 87  ? -11.11372 -11.71365 -28.14325 1.000 24.84288 ? 94  THR   A CB  1 
ATOM   635  O OG1 . THR   A 1 87  ? -11.77577 -10.87402 -27.19245 1.000 23.08083 ? 94  THR   A OG1 1 
ATOM   636  C CG2 . THR   A 1 87  ? -11.71219 -13.11699 -28.07825 1.000 23.65175 ? 94  THR   A CG2 1 
ATOM   637  N N   . GLY   A 1 88  ? -7.74115  -10.21731 -27.71521 1.000 20.16963 ? 95  GLY   A N   1 
ATOM   638  C CA  . GLY   A 1 88  ? -6.99436  -9.01433  -28.01168 1.000 17.86000 ? 95  GLY   A CA  1 
ATOM   639  C C   . GLY   A 1 88  ? -6.32860  -9.07035  -29.37115 1.000 21.90534 ? 95  GLY   A C   1 
ATOM   640  O O   . GLY   A 1 88  ? -6.69736  -9.85109  -30.25258 1.000 21.55275 ? 95  GLY   A O   1 
ATOM   641  N N   . ILE   A 1 89  ? -5.30521  -8.22777  -29.52744 1.000 19.74930 ? 96  ILE   A N   1 
ATOM   642  C CA  . ILE   A 1 89  ? -4.67590  -8.04001  -30.82790 1.000 20.00291 ? 96  ILE   A CA  1 
ATOM   643  C C   . ILE   A 1 89  ? -3.86401  -9.25600  -31.25530 1.000 25.11346 ? 96  ILE   A C   1 
ATOM   644  O O   . ILE   A 1 89  ? -3.56571  -9.41076  -32.44445 1.000 22.90657 ? 96  ILE   A O   1 
ATOM   645  C CB  . ILE   A 1 89  ? -3.80293  -6.77048  -30.80412 1.000 22.00249 ? 96  ILE   A CB  1 
ATOM   646  C CG1 . ILE   A 1 89  ? -3.46147  -6.31832  -32.22603 1.000 27.42098 ? 96  ILE   A CG1 1 
ATOM   647  C CG2 . ILE   A 1 89  ? -2.54282  -6.99904  -29.97748 1.000 19.38044 ? 96  ILE   A CG2 1 
ATOM   648  C CD1 . ILE   A 1 89  ? -3.01131  -4.87456  -32.30986 1.000 30.85366 ? 96  ILE   A CD1 1 
ATOM   649  N N   . GLY   A 1 90  ? -3.50596  -10.13560 -30.32666 1.000 20.25622 ? 97  GLY   A N   1 
ATOM   650  C CA  . GLY   A 1 90  ? -2.73263  -11.30803 -30.67704 1.000 21.91382 ? 97  GLY   A CA  1 
ATOM   651  C C   . GLY   A 1 90  ? -1.27446  -10.97698 -30.92364 1.000 25.37098 ? 97  GLY   A C   1 
ATOM   652  O O   . GLY   A 1 90  ? -0.80780  -9.85438  -30.72519 1.000 21.94232 ? 97  GLY   A O   1 
ATOM   653  N N   . MET   A 1 91  ? -0.54486  -11.98660 -31.38935 1.000 20.46805 ? 98  MET   A N   1 
ATOM   654  C CA  . MET   A 1 91  ? 0.90290   -11.92059 -31.49707 1.000 22.47044 ? 98  MET   A CA  1 
ATOM   655  C C   . MET   A 1 91  ? 1.34790   -12.49844 -32.83136 1.000 21.52578 ? 98  MET   A C   1 
ATOM   656  O O   . MET   A 1 91  ? 0.91366   -13.58741 -33.22055 1.000 21.41816 ? 98  MET   A O   1 
ATOM   657  C CB  . MET   A 1 91  ? 1.55080   -12.69824 -30.34548 1.000 22.35771 ? 98  MET   A CB  1 
ATOM   658  C CG  . MET   A 1 91  ? 1.66822   -11.89559 -29.06190 1.000 24.90846 ? 98  MET   A CG  1 
ATOM   659  S SD  . MET   A 1 91  ? 2.48778   -12.82065 -27.74863 1.000 25.14860 ? 98  MET   A SD  1 
ATOM   660  C CE  . MET   A 1 91  ? 1.25482   -14.07340 -27.41443 1.000 26.50715 ? 98  MET   A CE  1 
ATOM   661  N N   . THR   A 1 92  ? 2.20644   -11.76423 -33.53310 1.000 21.15111 ? 99  THR   A N   1 
ATOM   662  C CA  . THR   A 1 92  ? 2.76840   -12.26880 -34.77482 1.000 22.48940 ? 99  THR   A CA  1 
ATOM   663  C C   . THR   A 1 92  ? 3.87070   -13.28158 -34.47662 1.000 19.32677 ? 99  THR   A C   1 
ATOM   664  O O   . THR   A 1 92  ? 4.31513   -13.43967 -33.33744 1.000 23.42599 ? 99  THR   A O   1 
ATOM   665  C CB  . THR   A 1 92  ? 3.32431   -11.12448 -35.62299 1.000 26.31075 ? 99  THR   A CB  1 
ATOM   666  O OG1 . THR   A 1 92  ? 4.41095   -10.50403 -34.92101 1.000 27.27543 ? 99  THR   A OG1 1 
ATOM   667  C CG2 . THR   A 1 92  ? 2.24341   -10.07838 -35.89051 1.000 26.35401 ? 99  THR   A CG2 1 
ATOM   668  N N   . LYS   A 1 93  ? 4.31241   -13.98309 -35.52237 1.000 22.84889 ? 100 LYS   A N   1 
ATOM   669  C CA  . LYS   A 1 93  ? 5.45412   -14.87557 -35.35926 1.000 23.31205 ? 100 LYS   A CA  1 
ATOM   670  C C   . LYS   A 1 93  ? 6.69887   -14.09501 -34.95966 1.000 22.89531 ? 100 LYS   A C   1 
ATOM   671  O O   . LYS   A 1 93  ? 7.50893   -14.56856 -34.15275 1.000 27.62991 ? 100 LYS   A O   1 
ATOM   672  C CB  . LYS   A 1 93  ? 5.70725   -15.65826 -36.64523 1.000 27.65592 ? 100 LYS   A CB  1 
ATOM   673  C CG  . LYS   A 1 93  ? 6.79756   -16.69759 -36.49191 1.000 26.12224 ? 100 LYS   A CG  1 
ATOM   674  C CD  . LYS   A 1 93  ? 7.20170   -17.32126 -37.81569 1.000 32.39484 ? 100 LYS   A CD  1 
ATOM   675  C CE  . LYS   A 1 93  ? 7.61786   -18.76855 -37.61590 1.000 37.48888 ? 100 LYS   A CE  1 
ATOM   676  N NZ  . LYS   A 1 93  ? 8.45285   -19.27431 -38.74296 1.000 45.06328 ? 100 LYS   A NZ  1 
ATOM   677  N N   . ALA   A 1 94  ? 6.86071   -12.88693 -35.50726 1.000 23.60086 ? 101 ALA   A N   1 
ATOM   678  C CA  . ALA   A 1 94  ? 7.98948   -12.04724 -35.12407 1.000 26.95493 ? 101 ALA   A CA  1 
ATOM   679  C C   . ALA   A 1 94  ? 7.88627   -11.59725 -33.67257 1.000 26.11712 ? 101 ALA   A C   1 
ATOM   680  O O   . ALA   A 1 94  ? 8.91320   -11.44367 -33.00238 1.000 26.80338 ? 101 ALA   A O   1 
ATOM   681  C CB  . ALA   A 1 94  ? 8.08724   -10.83670 -36.05012 1.000 27.56611 ? 101 ALA   A CB  1 
ATOM   682  N N   . ASP   A 1 95  ? 6.66672   -11.37047 -33.17522 1.000 22.36906 ? 102 ASP   A N   1 
ATOM   683  C CA  . ASP   A 1 95  ? 6.48568   -11.10588 -31.75027 1.000 22.64554 ? 102 ASP   A CA  1 
ATOM   684  C C   . ASP   A 1 95  ? 7.00176   -12.26908 -30.91560 1.000 28.93207 ? 102 ASP   A C   1 
ATOM   685  O O   . ASP   A 1 95  ? 7.75643   -12.07436 -29.95509 1.000 26.36584 ? 102 ASP   A O   1 
ATOM   686  C CB  . ASP   A 1 95  ? 5.00915   -10.85078 -31.43310 1.000 25.98214 ? 102 ASP   A CB  1 
ATOM   687  C CG  . ASP   A 1 95  ? 4.50681   -9.52334  -31.96601 1.000 29.16796 ? 102 ASP   A CG  1 
ATOM   688  O OD1 . ASP   A 1 95  ? 5.30041   -8.56341  -32.04359 1.000 29.90004 ? 102 ASP   A OD1 1 
ATOM   689  O OD2 . ASP   A 1 95  ? 3.30082   -9.43555  -32.28538 1.000 26.50408 ? 102 ASP   A OD2 1 
ATOM   690  N N   . LEU   A 1 96  ? 6.60554   -13.49268 -31.27903 1.000 20.20288 ? 103 LEU   A N   1 
ATOM   691  C CA  . LEU   A 1 96  ? 6.93023   -14.66020 -30.46617 1.000 22.48297 ? 103 LEU   A CA  1 
ATOM   692  C C   . LEU   A 1 96  ? 8.42748   -14.93718 -30.45442 1.000 23.45350 ? 103 LEU   A C   1 
ATOM   693  O O   . LEU   A 1 96  ? 8.99473   -15.27830 -29.40921 1.000 25.08076 ? 103 LEU   A O   1 
ATOM   694  C CB  . LEU   A 1 96  ? 6.16980   -15.88299 -30.98107 1.000 21.00562 ? 103 LEU   A CB  1 
ATOM   695  C CG  . LEU   A 1 96  ? 4.64124   -15.86182 -30.89597 1.000 20.85968 ? 103 LEU   A CG  1 
ATOM   696  C CD1 . LEU   A 1 96  ? 4.05271   -17.05556 -31.63633 1.000 21.37043 ? 103 LEU   A CD1 1 
ATOM   697  C CD2 . LEU   A 1 96  ? 4.16793   -15.84843 -29.45318 1.000 22.90396 ? 103 LEU   A CD2 1 
ATOM   698  N N   . ILE   A 1 97  ? 9.08362   -14.80260 -31.60352 1.000 21.77618 ? 104 ILE   A N   1 
ATOM   699  C CA  . ILE   A 1 97  ? 10.48967  -15.17819 -31.71166 1.000 23.29182 ? 104 ILE   A CA  1 
ATOM   700  C C   . ILE   A 1 97  ? 11.40944  -14.02962 -31.30933 1.000 32.08226 ? 104 ILE   A C   1 
ATOM   701  O O   . ILE   A 1 97  ? 12.44004  -14.25251 -30.66909 1.000 31.37922 ? 104 ILE   A O   1 
ATOM   702  C CB  . ILE   A 1 97  ? 10.79229  -15.66621 -33.14442 1.000 27.78154 ? 104 ILE   A CB  1 
ATOM   703  C CG1 . ILE   A 1 97  ? 9.97187   -16.91471 -33.47664 1.000 26.21998 ? 104 ILE   A CG1 1 
ATOM   704  C CG2 . ILE   A 1 97  ? 12.27900  -15.97824 -33.30977 1.000 29.17991 ? 104 ILE   A CG2 1 
ATOM   705  C CD1 . ILE   A 1 97  ? 9.94916   -17.23737 -34.95180 1.000 35.65829 ? 104 ILE   A CD1 1 
ATOM   706  N N   . ASN   A 1 98  ? 11.05190  -12.78762 -31.64606 1.000 24.86265 ? 105 ASN   A N   1 
ATOM   707  C CA  . ASN   A 1 98  ? 12.01419  -11.69329 -31.56005 1.000 29.08589 ? 105 ASN   A CA  1 
ATOM   708  C C   . ASN   A 1 98  ? 11.55283  -10.48888 -30.74338 1.000 30.92192 ? 105 ASN   A C   1 
ATOM   709  O O   . ASN   A 1 98  ? 12.20181  -10.13290 -29.75505 1.000 28.26404 ? 105 ASN   A O   1 
ATOM   710  C CB  . ASN   A 1 98  ? 12.38906  -11.23042 -32.96806 1.000 38.03844 ? 105 ASN   A CB  1 
ATOM   711  C CG  . ASN   A 1 98  ? 13.71528  -11.79060 -33.42459 1.000 55.23720 ? 105 ASN   A CG  1 
ATOM   712  O OD1 . ASN   A 1 98  ? 13.82276  -12.34801 -34.51528 1.000 64.55825 ? 105 ASN   A OD1 1 
ATOM   713  N ND2 . ASN   A 1 98  ? 14.74312  -11.62799 -32.59581 1.000 60.76949 ? 105 ASN   A ND2 1 
ATOM   714  N N   . ASN   A 1 99  ? 10.45744  -9.84040  -31.15318 1.000 26.77841 ? 106 ASN   A N   1 
ATOM   715  C CA  . ASN   A 1 99  ? 10.14668  -8.50628  -30.63721 1.000 24.33211 ? 106 ASN   A CA  1 
ATOM   716  C C   . ASN   A 1 99  ? 9.93182   -8.50881  -29.12680 1.000 24.83974 ? 106 ASN   A C   1 
ATOM   717  O O   . ASN   A 1 99  ? 10.48069  -7.66215  -28.41312 1.000 27.56485 ? 106 ASN   A O   1 
ATOM   718  C CB  . ASN   A 1 99  ? 8.92490   -7.92682  -31.35305 1.000 27.59848 ? 106 ASN   A CB  1 
ATOM   719  C CG  . ASN   A 1 99  ? 9.03546   -8.00796  -32.86080 1.000 36.41655 ? 106 ASN   A CG  1 
ATOM   720  O OD1 . ASN   A 1 99  ? 10.13304  -7.96839  -33.41745 1.000 36.05180 ? 106 ASN   A OD1 1 
ATOM   721  N ND2 . ASN   A 1 99  ? 7.89128   -8.09168  -33.53434 1.000 38.37205 ? 106 ASN   A ND2 1 
ATOM   722  N N   . LEU   A 1 100 ? 9.13461   -9.44808  -28.61644 1.000 24.14855 ? 107 LEU   A N   1 
ATOM   723  C CA  . LEU   A 1 100 ? 8.83870   -9.43417  -27.18738 1.000 22.66268 ? 107 LEU   A CA  1 
ATOM   724  C C   . LEU   A 1 100 ? 10.06823  -9.75969  -26.35379 1.000 23.97215 ? 107 LEU   A C   1 
ATOM   725  O O   . LEU   A 1 100 ? 10.25121  -9.18328  -25.27678 1.000 27.96384 ? 107 LEU   A O   1 
ATOM   726  C CB  . LEU   A 1 100 ? 7.70246   -10.40266 -26.87167 1.000 23.16744 ? 107 LEU   A CB  1 
ATOM   727  C CG  . LEU   A 1 100 ? 6.35201   -9.94533  -27.42224 1.000 24.25270 ? 107 LEU   A CG  1 
ATOM   728  C CD1 . LEU   A 1 100 ? 5.32417   -11.03132 -27.23304 1.000 29.88406 ? 107 LEU   A CD1 1 
ATOM   729  C CD2 . LEU   A 1 100 ? 5.89611   -8.64512  -26.76500 1.000 32.77898 ? 107 LEU   A CD2 1 
ATOM   730  N N   . GLY   A 1 101 ? 10.91748  -10.67178 -26.82812 1.000 24.79810 ? 108 GLY   A N   1 
ATOM   731  C CA  . GLY   A 1 101 ? 12.16691  -10.92956 -26.13662 1.000 25.32749 ? 108 GLY   A CA  1 
ATOM   732  C C   . GLY   A 1 101 ? 13.11500  -9.74992  -26.18063 1.000 26.22811 ? 108 GLY   A C   1 
ATOM   733  O O   . GLY   A 1 101 ? 13.86904  -9.52033  -25.22963 1.000 26.97816 ? 108 GLY   A O   1 
ATOM   734  N N   . THR   A 1 102 ? 13.08572  -8.98235  -27.27315 1.000 24.04525 ? 109 THR   A N   1 
ATOM   735  C CA  . THR   A 1 102 ? 13.93145  -7.79681  -27.37179 1.000 22.62326 ? 109 THR   A CA  1 
ATOM   736  C C   . THR   A 1 102 ? 13.54992  -6.76620  -26.31738 1.000 29.98507 ? 109 THR   A C   1 
ATOM   737  O O   . THR   A 1 102 ? 14.41689  -6.21836  -25.62644 1.000 30.00648 ? 109 THR   A O   1 
ATOM   738  C CB  . THR   A 1 102 ? 13.83221  -7.19069  -28.77186 1.000 30.26147 ? 109 THR   A CB  1 
ATOM   739  O OG1 . THR   A 1 102 ? 14.31879  -8.12921  -29.73729 1.000 30.80258 ? 109 THR   A OG1 1 
ATOM   740  C CG2 . THR   A 1 102 ? 14.65396  -5.90574  -28.85973 1.000 31.45474 ? 109 THR   A CG2 1 
ATOM   741  N N   . ILE   A 1 103 ? 12.25053  -6.48827  -26.17922 1.000 26.54366 ? 110 ILE   A N   1 
ATOM   742  C CA  . ILE   A 1 103 ? 11.79410  -5.57583  -25.13425 1.000 30.30479 ? 110 ILE   A CA  1 
ATOM   743  C C   . ILE   A 1 103 ? 12.09982  -6.15358  -23.75813 1.000 36.60780 ? 110 ILE   A C   1 
ATOM   744  O O   . ILE   A 1 103 ? 12.52981  -5.43699  -22.84525 1.000 39.58212 ? 110 ILE   A O   1 
ATOM   745  C CB  . ILE   A 1 103 ? 10.29124  -5.27425  -25.30181 1.000 39.09051 ? 110 ILE   A CB  1 
ATOM   746  C CG1 . ILE   A 1 103 ? 10.04524  -4.35737  -26.50259 1.000 36.63081 ? 110 ILE   A CG1 1 
ATOM   747  C CG2 . ILE   A 1 103 ? 9.71847   -4.65224  -24.03651 1.000 37.96163 ? 110 ILE   A CG2 1 
ATOM   748  C CD1 . ILE   A 1 103 ? 8.78404   -4.68972  -27.27778 1.000 45.77672 ? 110 ILE   A CD1 1 
ATOM   749  N N   . ALA   A 1 104 ? 11.90372  -7.46366  -23.59509 1.000 28.82552 ? 111 ALA   A N   1 
ATOM   750  C CA  . ALA   A 1 104 ? 12.10257  -8.10449  -22.30181 1.000 28.69216 ? 111 ALA   A CA  1 
ATOM   751  C C   . ALA   A 1 104 ? 13.55696  -8.08288  -21.84955 1.000 32.57138 ? 111 ALA   A C   1 
ATOM   752  O O   . ALA   A 1 104 ? 13.81494  -8.20974  -20.64818 1.000 30.86352 ? 111 ALA   A O   1 
ATOM   753  C CB  . ALA   A 1 104 ? 11.59194  -9.54479  -22.35240 1.000 28.04419 ? 111 ALA   A CB  1 
ATOM   754  N N   . LYS   A 1 105 ? 14.50782  -7.92812  -22.77559 1.000 30.34488 ? 112 LYS   A N   1 
ATOM   755  C CA  . LYS   A 1 105 ? 15.91584  -7.88040  -22.39186 1.000 28.28016 ? 112 LYS   A CA  1 
ATOM   756  C C   . LYS   A 1 105 ? 16.20964  -6.65487  -21.53485 1.000 30.28594 ? 112 LYS   A C   1 
ATOM   757  O O   . LYS   A 1 105 ? 16.79577  -6.76733  -20.45141 1.000 28.65197 ? 112 LYS   A O   1 
ATOM   758  C CB  . LYS   A 1 105 ? 16.80238  -7.88868  -23.63840 1.000 27.71330 ? 112 LYS   A CB  1 
ATOM   759  C CG  . LYS   A 1 105 ? 18.26152  -8.22631  -23.35590 1.000 31.07857 ? 112 LYS   A CG  1 
ATOM   760  C CD  . LYS   A 1 105 ? 19.10037  -8.25236  -24.62584 1.000 31.62351 ? 112 LYS   A CD  1 
ATOM   761  C CE  . LYS   A 1 105 ? 20.57538  -8.43749  -24.30055 1.000 50.33470 ? 112 LYS   A CE  1 
ATOM   762  N NZ  . LYS   A 1 105 ? 21.26707  -7.14380  -24.04307 1.000 56.19204 ? 112 LYS   A NZ  1 
ATOM   763  N N   . SER   A 1 106 ? 15.81000  -5.47177  -22.00605 1.000 28.49785 ? 113 SER   A N   1 
ATOM   764  C CA  . SER   A 1 106 ? 16.03802  -4.25723  -21.23098 1.000 27.11832 ? 113 SER   A CA  1 
ATOM   765  C C   . SER   A 1 106 ? 15.18303  -4.24102  -19.97141 1.000 26.12909 ? 113 SER   A C   1 
ATOM   766  O O   . SER   A 1 106 ? 15.63219  -3.78010  -18.91578 1.000 26.53083 ? 113 SER   A O   1 
ATOM   767  C CB  . SER   A 1 106 ? 15.75545  -3.02404  -22.08887 1.000 41.51444 ? 113 SER   A CB  1 
ATOM   768  O OG  . SER   A 1 106 ? 14.68886  -3.26041  -22.99244 1.000 41.14822 ? 113 SER   A OG  1 
ATOM   769  N N   . GLY   A 1 107 ? 13.94939  -4.73963  -20.06225 1.000 31.10293 ? 114 GLY   A N   1 
ATOM   770  C CA  . GLY   A 1 107 ? 13.09905  -4.79306  -18.88515 1.000 23.59540 ? 114 GLY   A CA  1 
ATOM   771  C C   . GLY   A 1 107 ? 13.65066  -5.71157  -17.81127 1.000 28.85756 ? 114 GLY   A C   1 
ATOM   772  O O   . GLY   A 1 107 ? 13.53347  -5.42704  -16.61691 1.000 26.42982 ? 114 GLY   A O   1 
ATOM   773  N N   . THR   A 1 108 ? 14.26045  -6.82542  -18.22300 1.000 22.26388 ? 115 THR   A N   1 
ATOM   774  C CA  . THR   A 1 108 ? 14.89197  -7.72208  -17.25948 1.000 20.99517 ? 115 THR   A CA  1 
ATOM   775  C C   . THR   A 1 108 ? 16.03267  -7.02116  -16.53398 1.000 26.77346 ? 115 THR   A C   1 
ATOM   776  O O   . THR   A 1 108 ? 16.11471  -7.06092  -15.30188 1.000 28.22591 ? 115 THR   A O   1 
ATOM   777  C CB  . THR   A 1 108 ? 15.39488  -8.98558  -17.96127 1.000 26.76081 ? 115 THR   A CB  1 
ATOM   778  O OG1 . THR   A 1 108 ? 14.27881  -9.72742  -18.46935 1.000 30.19147 ? 115 THR   A OG1 1 
ATOM   779  C CG2 . THR   A 1 108 ? 16.18117  -9.86289  -16.99287 1.000 30.79319 ? 115 THR   A CG2 1 
ATOM   780  N N   . LYS   A 1 109 ? 16.91368  -6.35389  -17.28519 1.000 26.23237 ? 116 LYS   A N   1 
ATOM   781  C CA  . LYS   A 1 109 ? 18.03095  -5.64427  -16.66837 1.000 26.67187 ? 116 LYS   A CA  1 
ATOM   782  C C   . LYS   A 1 109 ? 17.53962  -4.58471  -15.68821 1.000 27.66345 ? 116 LYS   A C   1 
ATOM   783  O O   . LYS   A 1 109 ? 18.09364  -4.43853  -14.59203 1.000 31.84025 ? 116 LYS   A O   1 
ATOM   784  C CB  . LYS   A 1 109 ? 18.90920  -5.01322  -17.74967 1.000 30.60773 ? 116 LYS   A CB  1 
ATOM   785  C CG  . LYS   A 1 109 ? 19.99538  -4.08140  -17.22435 1.000 34.58482 ? 116 LYS   A CG  1 
ATOM   786  C CD  . LYS   A 1 109 ? 21.27928  -4.21875  -18.03325 1.000 43.12604 ? 116 LYS   A CD  1 
ATOM   787  C CE  . LYS   A 1 109 ? 21.81139  -2.86292  -18.47506 1.000 55.87032 ? 116 LYS   A CE  1 
ATOM   788  N NZ  . LYS   A 1 109 ? 22.08867  -1.97298  -17.31299 1.000 46.40340 ? 116 LYS   A NZ  1 
ATOM   789  N N   . ALA   A 1 110 ? 16.49294  -3.84185  -16.06044 1.000 27.76246 ? 117 ALA   A N   1 
ATOM   790  C CA  . ALA   A 1 110 ? 15.94922  -2.82968  -15.15950 1.000 29.08307 ? 117 ALA   A CA  1 
ATOM   791  C C   . ALA   A 1 110 ? 15.29012  -3.46882  -13.94391 1.000 31.36226 ? 117 ALA   A C   1 
ATOM   792  O O   . ALA   A 1 110 ? 15.36192  -2.92831  -12.83515 1.000 31.70846 ? 117 ALA   A O   1 
ATOM   793  C CB  . ALA   A 1 110 ? 14.95160  -1.94476  -15.90455 1.000 29.85565 ? 117 ALA   A CB  1 
ATOM   794  N N   . PHE   A 1 111 ? 14.64441  -4.61962  -14.13591 1.000 25.38150 ? 118 PHE   A N   1 
ATOM   795  C CA  . PHE   A 1 111 ? 13.98991  -5.31454  -13.03198 1.000 26.58288 ? 118 PHE   A CA  1 
ATOM   796  C C   . PHE   A 1 111 ? 15.00879  -5.78393  -12.00014 1.000 31.12726 ? 118 PHE   A C   1 
ATOM   797  O O   . PHE   A 1 111 ? 14.80579  -5.61257  -10.79251 1.000 35.40050 ? 118 PHE   A O   1 
ATOM   798  C CB  . PHE   A 1 111 ? 13.17146  -6.48474  -13.58578 1.000 24.58786 ? 118 PHE   A CB  1 
ATOM   799  C CG  . PHE   A 1 111 ? 12.44109  -7.28333  -12.54044 1.000 25.08160 ? 118 PHE   A CG  1 
ATOM   800  C CD1 . PHE   A 1 111 ? 11.74815  -6.65797  -11.51557 1.000 26.75138 ? 118 PHE   A CD1 1 
ATOM   801  C CD2 . PHE   A 1 111 ? 12.40496  -8.66641  -12.61794 1.000 28.26783 ? 118 PHE   A CD2 1 
ATOM   802  C CE1 . PHE   A 1 111 ? 11.06470  -7.40215  -10.56768 1.000 28.45724 ? 118 PHE   A CE1 1 
ATOM   803  C CE2 . PHE   A 1 111 ? 11.72140  -9.41331  -11.67678 1.000 33.14923 ? 118 PHE   A CE2 1 
ATOM   804  C CZ  . PHE   A 1 111 ? 11.04947  -8.78083  -10.65048 1.000 27.16147 ? 118 PHE   A CZ  1 
ATOM   805  N N   . MET   A 1 112 ? 16.12472  -6.35990  -12.45996 1.000 31.12976 ? 119 MET   A N   1 
ATOM   806  C CA  . MET   A 1 112 ? 17.16643  -6.80211  -11.53593 1.000 41.13274 ? 119 MET   A CA  1 
ATOM   807  C C   . MET   A 1 112 ? 17.78522  -5.62515  -10.79320 1.000 43.59736 ? 119 MET   A C   1 
ATOM   808  O O   . MET   A 1 112 ? 18.04666  -5.71041  -9.58762  1.000 41.98472 ? 119 MET   A O   1 
ATOM   809  C CB  . MET   A 1 112 ? 18.24429  -7.58004  -12.28997 1.000 39.64400 ? 119 MET   A CB  1 
ATOM   810  C CG  . MET   A 1 112 ? 17.69573  -8.65391  -13.20820 1.000 41.12549 ? 119 MET   A CG  1 
ATOM   811  S SD  . MET   A 1 112 ? 17.58667  -10.27087 -12.42956 1.000 61.19529 ? 119 MET   A SD  1 
ATOM   812  C CE  . MET   A 1 112 ? 17.72050  -11.33826 -13.86516 1.000 47.81896 ? 119 MET   A CE  1 
ATOM   813  N N   . GLU   A 1 113 ? 18.04066  -4.52108  -11.49902 1.000 40.18935 ? 120 GLU   A N   1 
ATOM   814  C CA  . GLU   A 1 113 ? 18.61895  -3.34831  -10.85031 1.000 41.29390 ? 120 GLU   A CA  1 
ATOM   815  C C   . GLU   A 1 113 ? 17.62561  -2.69846  -9.89614  1.000 49.11116 ? 120 GLU   A C   1 
ATOM   816  O O   . GLU   A 1 113 ? 18.00526  -2.24688  -8.80974  1.000 44.86237 ? 120 GLU   A O   1 
ATOM   817  C CB  . GLU   A 1 113 ? 19.09188  -2.34745  -11.90388 1.000 49.73243 ? 120 GLU   A CB  1 
ATOM   818  C CG  . GLU   A 1 113 ? 20.23381  -2.86342  -12.76330 1.000 45.13587 ? 120 GLU   A CG  1 
ATOM   819  C CD  . GLU   A 1 113 ? 20.56012  -1.94580  -13.92627 1.000 59.17051 ? 120 GLU   A CD  1 
ATOM   820  O OE1 . GLU   A 1 113 ? 19.68040  -1.16032  -14.33779 1.000 64.97902 ? 120 GLU   A OE1 1 
ATOM   821  O OE2 . GLU   A 1 113 ? 21.70160  -2.00924  -14.42848 1.000 62.98702 ? 120 GLU   A OE2 1 
ATOM   822  N N   . ALA   A 1 114 ? 16.35059  -2.63864  -10.28601 1.000 38.16696 ? 121 ALA   A N   1 
ATOM   823  C CA  . ALA   A 1 114 ? 15.32768  -2.10775  -9.39217  1.000 42.70556 ? 121 ALA   A CA  1 
ATOM   824  C C   . ALA   A 1 114 ? 15.21712  -2.94703  -8.12857  1.000 48.95019 ? 121 ALA   A C   1 
ATOM   825  O O   . ALA   A 1 114 ? 15.02001  -2.40953  -7.03219  1.000 56.48644 ? 121 ALA   A O   1 
ATOM   826  C CB  . ALA   A 1 114 ? 13.98238  -2.05081  -10.11130 1.000 34.55440 ? 121 ALA   A CB  1 
ATOM   827  N N   . LEU   A 1 115 ? 15.33636  -4.27083  -8.26663  1.000 37.52113 ? 122 LEU   A N   1 
ATOM   828  C CA  . LEU   A 1 115 ? 15.30051  -5.15256  -7.10502  1.000 43.92683 ? 122 LEU   A CA  1 
ATOM   829  C C   . LEU   A 1 115 ? 16.38471  -4.78375  -6.10321  1.000 52.09872 ? 122 LEU   A C   1 
ATOM   830  O O   . LEU   A 1 115 ? 16.15194  -4.79707  -4.88894  1.000 60.88529 ? 122 LEU   A O   1 
ATOM   831  C CB  . LEU   A 1 115 ? 15.45558  -6.60772  -7.54970  1.000 40.14474 ? 122 LEU   A CB  1 
ATOM   832  C CG  . LEU   A 1 115 ? 14.21228  -7.25648  -8.16416  1.000 44.03829 ? 122 LEU   A CG  1 
ATOM   833  C CD1 . LEU   A 1 115 ? 14.44022  -8.73723  -8.41534  1.000 34.56079 ? 122 LEU   A CD1 1 
ATOM   834  C CD2 . LEU   A 1 115 ? 12.98802  -7.03720  -7.28818  1.000 42.89802 ? 122 LEU   A CD2 1 
ATOM   835  N N   . GLN   A 1 116 ? 17.57992  -4.45003  -6.59656  1.000 60.59601 ? 123 GLN   A N   1 
ATOM   836  C CA  . GLN   A 1 116 ? 18.65678  -4.00837  -5.71928  1.000 60.19194 ? 123 GLN   A CA  1 
ATOM   837  C C   . GLN   A 1 116 ? 18.37833  -2.64709  -5.10007  1.000 59.82106 ? 123 GLN   A C   1 
ATOM   838  O O   . GLN   A 1 116 ? 18.96674  -2.32122  -4.06362  1.000 64.76505 ? 123 GLN   A O   1 
ATOM   839  C CB  . GLN   A 1 116 ? 19.98057  -3.98300  -6.48427  1.000 70.74795 ? 123 GLN   A CB  1 
ATOM   840  C CG  . GLN   A 1 116 ? 20.50036  -5.36394  -6.83731  1.000 67.98334 ? 123 GLN   A CG  1 
ATOM   841  C CD  . GLN   A 1 116 ? 20.21708  -6.38026  -5.74710  1.000 73.41019 ? 123 GLN   A CD  1 
ATOM   842  O OE1 . GLN   A 1 116 ? 20.66033  -6.22510  -4.60831  1.000 82.15449 ? 123 GLN   A OE1 1 
ATOM   843  N NE2 . GLN   A 1 116 ? 19.46614  -7.42063  -6.08693  1.000 59.64013 ? 123 GLN   A NE2 1 
ATOM   844  N N   . ALA   A 1 117 ? 17.50311  -1.84710  -5.70600  1.000 57.53999 ? 124 ALA   A N   1 
ATOM   845  C CA  . ALA   A 1 117 ? 17.05115  -0.62003  -5.06623  1.000 66.46949 ? 124 ALA   A CA  1 
ATOM   846  C C   . ALA   A 1 117 ? 15.98749  -0.95230  -4.02758  1.000 75.81816 ? 124 ALA   A C   1 
ATOM   847  O O   . ALA   A 1 117 ? 16.26640  -1.65343  -3.04943  1.000 85.20065 ? 124 ALA   A O   1 
ATOM   848  C CB  . ALA   A 1 117 ? 16.51268  0.37085   -6.09994  1.000 57.93063 ? 124 ALA   A CB  1 
ATOM   849  N N   . GLY   A 1 118 ? 14.76415  -0.47313  -4.23650  1.000 62.95686 ? 125 GLY   A N   1 
ATOM   850  C CA  . GLY   A 1 118 ? 13.69847  -0.71310  -3.28314  1.000 65.01917 ? 125 GLY   A CA  1 
ATOM   851  C C   . GLY   A 1 118 ? 12.46802  -1.37797  -3.86696  1.000 52.68414 ? 125 GLY   A C   1 
ATOM   852  O O   . GLY   A 1 118 ? 11.39499  -1.34511  -3.25793  1.000 58.69925 ? 125 GLY   A O   1 
ATOM   853  N N   . ALA   A 1 119 ? 12.60632  -1.99439  -5.03697  1.000 55.99617 ? 126 ALA   A N   1 
ATOM   854  C CA  . ALA   A 1 119 ? 11.46673  -2.60728  -5.70402  1.000 62.41835 ? 126 ALA   A CA  1 
ATOM   855  C C   . ALA   A 1 119 ? 11.19681  -4.00583  -5.16102  1.000 58.05312 ? 126 ALA   A C   1 
ATOM   856  O O   . ALA   A 1 119 ? 12.08969  -4.67719  -4.63693  1.000 46.16475 ? 126 ALA   A O   1 
ATOM   857  C CB  . ALA   A 1 119 ? 11.69884  -2.67517  -7.21381  1.000 49.23441 ? 126 ALA   A CB  1 
ATOM   858  N N   . ASP   A 1 120 ? 9.94640   -4.44045  -5.29164  1.000 47.63665 ? 127 ASP   A N   1 
ATOM   859  C CA  . ASP   A 1 120 ? 9.53803   -5.77942  -4.89468  1.000 54.43068 ? 127 ASP   A CA  1 
ATOM   860  C C   . ASP   A 1 120 ? 9.40319   -6.68099  -6.11608  1.000 48.54342 ? 127 ASP   A C   1 
ATOM   861  O O   . ASP   A 1 120 ? 9.15746   -6.21477  -7.23173  1.000 41.45926 ? 127 ASP   A O   1 
ATOM   862  C CB  . ASP   A 1 120 ? 8.21342   -5.75207  -4.12525  1.000 45.67101 ? 127 ASP   A CB  1 
ATOM   863  C CG  . ASP   A 1 120 ? 8.15943   -4.64642  -3.08976  1.000 74.05993 ? 127 ASP   A CG  1 
ATOM   864  O OD1 . ASP   A 1 120 ? 7.04318   -4.19389  -2.75826  1.000 74.97435 ? 127 ASP   A OD1 1 
ATOM   865  O OD2 . ASP   A 1 120 ? 9.23240   -4.23807  -2.59775  1.000 80.94053 ? 127 ASP   A OD2 1 
ATOM   866  N N   . ILE   A 1 121 ? 9.56864   -7.98733  -5.88617  1.000 43.45248 ? 128 ILE   A N   1 
ATOM   867  C CA  . ILE   A 1 121 ? 9.40513   -8.97130  -6.95475  1.000 33.16683 ? 128 ILE   A CA  1 
ATOM   868  C C   . ILE   A 1 121 ? 8.02777   -8.84905  -7.59567  1.000 41.86084 ? 128 ILE   A C   1 
ATOM   869  O O   . ILE   A 1 121 ? 7.87724   -8.99162  -8.81626  1.000 37.74146 ? 128 ILE   A O   1 
ATOM   870  C CB  . ILE   A 1 121 ? 9.65567   -10.39158 -6.41162  1.000 33.34242 ? 128 ILE   A CB  1 
ATOM   871  C CG1 . ILE   A 1 121 ? 11.11649  -10.55002 -5.98227  1.000 36.58238 ? 128 ILE   A CG1 1 
ATOM   872  C CG2 . ILE   A 1 121 ? 9.26547   -11.44321 -7.44806  1.000 30.37388 ? 128 ILE   A CG2 1 
ATOM   873  C CD1 . ILE   A 1 121 ? 11.31974  -11.53090 -4.84936  1.000 43.19853 ? 128 ILE   A CD1 1 
ATOM   874  N N   . SER   A 1 122 ? 7.00357   -8.56279  -6.78756  1.000 39.17834 ? 129 SER   A N   1 
ATOM   875  C CA  . SER   A 1 122 ? 5.64677   -8.41838  -7.30432  1.000 30.69623 ? 129 SER   A CA  1 
ATOM   876  C C   . SER   A 1 122 ? 5.50463   -7.26304  -8.28804  1.000 34.13888 ? 129 SER   A C   1 
ATOM   877  O O   . SER   A 1 122 ? 4.46322   -7.15787  -8.94558  1.000 34.35993 ? 129 SER   A O   1 
ATOM   878  C CB  . SER   A 1 122 ? 4.66201   -8.23423  -6.14727  1.000 33.27108 ? 129 SER   A CB  1 
ATOM   879  O OG  . SER   A 1 122 ? 4.80526   -6.95930  -5.54732  1.000 40.23889 ? 129 SER   A OG  1 
ATOM   880  N N   . MET   A 1 123 ? 6.51129   -6.40017  -8.40405  1.000 32.61922 ? 130 MET   A N   1 
ATOM   881  C CA  . MET   A 1 123 ? 6.51075   -5.31196  -9.37010  1.000 31.85922 ? 130 MET   A CA  1 
ATOM   882  C C   . MET   A 1 123 ? 7.08774   -5.73081  -10.71630 1.000 33.19703 ? 130 MET   A C   1 
ATOM   883  O O   . MET   A 1 123 ? 7.42113   -4.86453  -11.53052 1.000 31.66944 ? 130 MET   A O   1 
ATOM   884  C CB  . MET   A 1 123 ? 7.28731   -4.11723  -8.80631  1.000 36.86606 ? 130 MET   A CB  1 
ATOM   885  C CG  . MET   A 1 123 ? 6.65203   -3.51696  -7.56062  1.000 46.59089 ? 130 MET   A CG  1 
ATOM   886  S SD  . MET   A 1 123 ? 7.59378   -2.16153  -6.83099  1.000 59.80708 ? 130 MET   A SD  1 
ATOM   887  C CE  . MET   A 1 123 ? 8.09768   -1.26765  -8.29537  1.000 52.30770 ? 130 MET   A CE  1 
ATOM   888  N N   . ILE   A 1 124 ? 7.20737   -7.03891  -10.96458 1.000 24.48646 ? 131 ILE   A N   1 
ATOM   889  C CA  . ILE   A 1 124 ? 7.74685   -7.53511  -12.22907 1.000 25.46268 ? 131 ILE   A CA  1 
ATOM   890  C C   . ILE   A 1 124 ? 6.98924   -6.95952  -13.41801 1.000 27.05781 ? 131 ILE   A C   1 
ATOM   891  O O   . ILE   A 1 124 ? 7.56803   -6.74183  -14.48947 1.000 24.25039 ? 131 ILE   A O   1 
ATOM   892  C CB  . ILE   A 1 124 ? 7.72541   -9.08038  -12.23600 1.000 24.92518 ? 131 ILE   A CB  1 
ATOM   893  C CG1 . ILE   A 1 124 ? 8.29919   -9.63080  -13.54626 1.000 21.34984 ? 131 ILE   A CG1 1 
ATOM   894  C CG2 . ILE   A 1 124 ? 6.31604   -9.60463  -12.00637 1.000 24.58132 ? 131 ILE   A CG2 1 
ATOM   895  C CD1 . ILE   A 1 124 ? 8.70900   -11.08620 -13.47273 1.000 28.14133 ? 131 ILE   A CD1 1 
ATOM   896  N N   . GLY   A 1 125 ? 5.69694   -6.67535  -13.24565 1.000 27.76210 ? 132 GLY   A N   1 
ATOM   897  C CA  . GLY   A 1 125 ? 4.88702   -6.23042  -14.36629 1.000 32.43223 ? 132 GLY   A CA  1 
ATOM   898  C C   . GLY   A 1 125 ? 5.26292   -4.86357  -14.90112 1.000 33.97644 ? 132 GLY   A C   1 
ATOM   899  O O   . GLY   A 1 125 ? 5.02440   -4.56928  -16.07582 1.000 39.14594 ? 132 GLY   A O   1 
ATOM   900  N N   . GLN   A 1 126 ? 5.85041   -4.01099  -14.06095 1.000 35.80674 ? 133 GLN   A N   1 
ATOM   901  C CA  . GLN   A 1 126 ? 6.23460   -2.67760  -14.50900 1.000 46.55441 ? 133 GLN   A CA  1 
ATOM   902  C C   . GLN   A 1 126 ? 7.41709   -2.69731  -15.46600 1.000 49.37710 ? 133 GLN   A C   1 
ATOM   903  O O   . GLN   A 1 126 ? 7.74321   -1.65312  -16.04123 1.000 44.39661 ? 133 GLN   A O   1 
ATOM   904  C CB  . GLN   A 1 126 ? 6.57210   -1.78936  -13.31027 1.000 40.93965 ? 133 GLN   A CB  1 
ATOM   905  C CG  . GLN   A 1 126 ? 5.92264   -2.22037  -12.00819 1.000 53.62953 ? 133 GLN   A CG  1 
ATOM   906  C CD  . GLN   A 1 126 ? 5.85523   -1.09825  -10.99678 1.000 67.15675 ? 133 GLN   A CD  1 
ATOM   907  O OE1 . GLN   A 1 126 ? 6.70857   -0.21058  -10.98190 1.000 66.80165 ? 133 GLN   A OE1 1 
ATOM   908  N NE2 . GLN   A 1 126 ? 4.84966   -1.14030  -10.13113 1.000 68.06569 ? 133 GLN   A NE2 1 
ATOM   909  N N   . PHE   A 1 127 ? 8.05860   -3.84957  -15.65252 1.000 32.21542 ? 134 PHE   A N   1 
ATOM   910  C CA  . PHE   A 1 127 ? 9.26361   -3.95621  -16.46163 1.000 27.62319 ? 134 PHE   A CA  1 
ATOM   911  C C   . PHE   A 1 127 ? 9.04030   -4.76478  -17.73367 1.000 32.78396 ? 134 PHE   A C   1 
ATOM   912  O O   . PHE   A 1 127 ? 10.01207  -5.15472  -18.38853 1.000 35.27175 ? 134 PHE   A O   1 
ATOM   913  C CB  . PHE   A 1 127 ? 10.38784  -4.56506  -15.62193 1.000 26.37608 ? 134 PHE   A CB  1 
ATOM   914  C CG  . PHE   A 1 127 ? 10.68313  -3.78581  -14.37315 1.000 25.00367 ? 134 PHE   A CG  1 
ATOM   915  C CD1 . PHE   A 1 127 ? 11.52905  -2.69053  -14.40112 1.000 31.60988 ? 134 PHE   A CD1 1 
ATOM   916  C CD2 . PHE   A 1 127 ? 10.08765  -4.13550  -13.17292 1.000 24.25876 ? 134 PHE   A CD2 1 
ATOM   917  C CE1 . PHE   A 1 127 ? 11.78576  -1.96922  -13.25138 1.000 32.74379 ? 134 PHE   A CE1 1 
ATOM   918  C CE2 . PHE   A 1 127 ? 10.34004  -3.41803  -12.02015 1.000 29.32494 ? 134 PHE   A CE2 1 
ATOM   919  C CZ  . PHE   A 1 127 ? 11.18807  -2.33292  -12.06028 1.000 29.55612 ? 134 PHE   A CZ  1 
ATOM   920  N N   . GLY   A 1 128 ? 7.78544   -5.03454  -18.09057 1.000 33.51770 ? 135 GLY   A N   1 
ATOM   921  C CA  . GLY   A 1 128 ? 7.47568   -5.70518  -19.33837 1.000 32.61399 ? 135 GLY   A CA  1 
ATOM   922  C C   . GLY   A 1 128 ? 7.84044   -7.16879  -19.39825 1.000 43.27523 ? 135 GLY   A C   1 
ATOM   923  O O   . GLY   A 1 128 ? 7.96973   -7.71985  -20.49388 1.000 38.63563 ? 135 GLY   A O   1 
ATOM   924  N N   . VAL   A 1 129 ? 8.01216   -7.82032  -18.25067 1.000 26.24526 ? 136 VAL   A N   1 
ATOM   925  C CA  . VAL   A 1 129 ? 8.40279   -9.22441  -18.21415 1.000 23.04137 ? 136 VAL   A CA  1 
ATOM   926  C C   . VAL   A 1 129 ? 7.48714   -9.99785  -17.27513 1.000 20.02216 ? 136 VAL   A C   1 
ATOM   927  O O   . VAL   A 1 129 ? 7.85523   -11.06530 -16.77156 1.000 21.67642 ? 136 VAL   A O   1 
ATOM   928  C CB  . VAL   A 1 129 ? 9.87581   -9.37603  -17.79593 1.000 23.99018 ? 136 VAL   A CB  1 
ATOM   929  C CG1 . VAL   A 1 129 ? 10.78571  -8.78966  -18.85704 1.000 27.99002 ? 136 VAL   A CG1 1 
ATOM   930  C CG2 . VAL   A 1 129 ? 10.12016  -8.69352  -16.46072 1.000 21.75432 ? 136 VAL   A CG2 1 
ATOM   931  N N   . GLY   A 1 130 ? 6.28368   -9.47013  -17.04266 1.000 23.69658 ? 137 GLY   A N   1 
ATOM   932  C CA  . GLY   A 1 130 ? 5.33406   -10.16595 -16.19078 1.000 17.64226 ? 137 GLY   A CA  1 
ATOM   933  C C   . GLY   A 1 130 ? 4.88050   -11.49844 -16.75531 1.000 22.49932 ? 137 GLY   A C   1 
ATOM   934  O O   . GLY   A 1 130 ? 4.47445   -12.38901 -16.00176 1.000 21.38296 ? 137 GLY   A O   1 
ATOM   935  N N   . PHE   A 1 131 ? 4.93882   -11.65549 -18.08257 1.000 19.04139 ? 138 PHE   A N   1 
ATOM   936  C CA  . PHE   A 1 131 ? 4.55967   -12.92276 -18.70349 1.000 18.38369 ? 138 PHE   A CA  1 
ATOM   937  C C   . PHE   A 1 131 ? 5.34672   -14.09314 -18.13040 1.000 19.93240 ? 138 PHE   A C   1 
ATOM   938  O O   . PHE   A 1 131 ? 4.79724   -15.18088 -17.92296 1.000 20.07551 ? 138 PHE   A O   1 
ATOM   939  C CB  . PHE   A 1 131 ? 4.76025   -12.85061 -20.21755 1.000 22.92325 ? 138 PHE   A CB  1 
ATOM   940  C CG  . PHE   A 1 131 ? 4.75124   -14.19528 -20.89277 1.000 21.06389 ? 138 PHE   A CG  1 
ATOM   941  C CD1 . PHE   A 1 131 ? 3.55852   -14.81976 -21.21118 1.000 18.11208 ? 138 PHE   A CD1 1 
ATOM   942  C CD2 . PHE   A 1 131 ? 5.94204   -14.83092 -21.21673 1.000 20.32396 ? 138 PHE   A CD2 1 
ATOM   943  C CE1 . PHE   A 1 131 ? 3.54982   -16.05748 -21.83275 1.000 16.14059 ? 138 PHE   A CE1 1 
ATOM   944  C CE2 . PHE   A 1 131 ? 5.94070   -16.06697 -21.83690 1.000 21.12783 ? 138 PHE   A CE2 1 
ATOM   945  C CZ  . PHE   A 1 131 ? 4.74413   -16.67934 -22.14575 1.000 20.95123 ? 138 PHE   A CZ  1 
ATOM   946  N N   . TYR   A 1 132 ? 6.63926   -13.89333 -17.87650 1.000 18.55558 ? 139 TYR   A N   1 
ATOM   947  C CA  . TYR   A 1 132 ? 7.47751   -14.98383 -17.39703 1.000 19.49434 ? 139 TYR   A CA  1 
ATOM   948  C C   . TYR   A 1 132 ? 7.15586   -15.38806 -15.96525 1.000 19.02844 ? 139 TYR   A C   1 
ATOM   949  O O   . TYR   A 1 132 ? 7.63153   -16.43667 -15.51665 1.000 20.01025 ? 139 TYR   A O   1 
ATOM   950  C CB  . TYR   A 1 132 ? 8.95306   -14.60233 -17.51955 1.000 21.31094 ? 139 TYR   A CB  1 
ATOM   951  C CG  . TYR   A 1 132 ? 9.34710   -14.23008 -18.92843 1.000 21.26849 ? 139 TYR   A CG  1 
ATOM   952  C CD1 . TYR   A 1 132 ? 9.64561   -15.20786 -19.86698 1.000 23.64888 ? 139 TYR   A CD1 1 
ATOM   953  C CD2 . TYR   A 1 132 ? 9.42050   -12.90041 -19.32150 1.000 22.61582 ? 139 TYR   A CD2 1 
ATOM   954  C CE1 . TYR   A 1 132 ? 10.00340  -14.87107 -21.16431 1.000 22.84987 ? 139 TYR   A CE1 1 
ATOM   955  C CE2 . TYR   A 1 132 ? 9.77861   -12.55298 -20.61489 1.000 23.55997 ? 139 TYR   A CE2 1 
ATOM   956  C CZ  . TYR   A 1 132 ? 10.06844  -13.54584 -21.52960 1.000 26.29227 ? 139 TYR   A CZ  1 
ATOM   957  O OH  . TYR   A 1 132 ? 10.42478  -13.21502 -22.81869 1.000 25.99216 ? 139 TYR   A OH  1 
ATOM   958  N N   . SER   A 1 133 ? 6.35600   -14.59738 -15.24349 1.000 19.54271 ? 140 SER   A N   1 
ATOM   959  C CA  . SER   A 1 133 ? 5.87616   -15.01986 -13.93167 1.000 20.10086 ? 140 SER   A CA  1 
ATOM   960  C C   . SER   A 1 133 ? 4.95202   -16.22904 -14.01303 1.000 19.47595 ? 140 SER   A C   1 
ATOM   961  O O   . SER   A 1 133 ? 4.62274   -16.80958 -12.97239 1.000 19.72805 ? 140 SER   A O   1 
ATOM   962  C CB  . SER   A 1 133 ? 5.15924   -13.86369 -13.23026 1.000 18.93648 ? 140 SER   A CB  1 
ATOM   963  O OG  . SER   A 1 133 ? 3.87772   -13.63933 -13.79065 1.000 22.69486 ? 140 SER   A OG  1 
ATOM   964  N N   . ALA   A 1 134 ? 4.52802   -16.62062 -15.21826 1.000 20.53839 ? 141 ALA   A N   1 
ATOM   965  C CA  . ALA   A 1 134 ? 3.77015   -17.85568 -15.38295 1.000 19.65488 ? 141 ALA   A CA  1 
ATOM   966  C C   . ALA   A 1 134 ? 4.53575   -19.05668 -14.84625 1.000 19.54726 ? 141 ALA   A C   1 
ATOM   967  O O   . ALA   A 1 134 ? 3.92810   -20.03507 -14.39680 1.000 17.74821 ? 141 ALA   A O   1 
ATOM   968  C CB  . ALA   A 1 134 ? 3.42699   -18.06521 -16.86027 1.000 20.60210 ? 141 ALA   A CB  1 
ATOM   969  N N   . TYR   A 1 135 ? 5.86500   -18.99725 -14.86734 1.000 16.09150 ? 142 TYR   A N   1 
ATOM   970  C CA  . TYR   A 1 135 ? 6.68522   -20.11058 -14.41423 1.000 21.73573 ? 142 TYR   A CA  1 
ATOM   971  C C   . TYR   A 1 135 ? 6.80335   -20.17867 -12.89829 1.000 20.57032 ? 142 TYR   A C   1 
ATOM   972  O O   . TYR   A 1 135 ? 7.48005   -21.07490 -12.38214 1.000 21.91778 ? 142 TYR   A O   1 
ATOM   973  C CB  . TYR   A 1 135 ? 8.05748   -20.02388 -15.08065 1.000 19.72449 ? 142 TYR   A CB  1 
ATOM   974  C CG  . TYR   A 1 135 ? 7.94111   -20.35389 -16.54519 1.000 21.75870 ? 142 TYR   A CG  1 
ATOM   975  C CD1 . TYR   A 1 135 ? 7.96616   -21.67006 -16.97997 1.000 19.13402 ? 142 TYR   A CD1 1 
ATOM   976  C CD2 . TYR   A 1 135 ? 7.72907   -19.35509 -17.48632 1.000 24.27267 ? 142 TYR   A CD2 1 
ATOM   977  C CE1 . TYR   A 1 135 ? 7.82719   -21.98538 -18.32296 1.000 18.09373 ? 142 TYR   A CE1 1 
ATOM   978  C CE2 . TYR   A 1 135 ? 7.58597   -19.65773 -18.83464 1.000 19.36411 ? 142 TYR   A CE2 1 
ATOM   979  C CZ  . TYR   A 1 135 ? 7.63684   -20.97395 -19.23983 1.000 22.81836 ? 142 TYR   A CZ  1 
ATOM   980  O OH  . TYR   A 1 135 ? 7.49250   -21.28495 -20.57655 1.000 21.82753 ? 142 TYR   A OH  1 
ATOM   981  N N   . LEU   A 1 136 ? 6.14666   -19.26983 -12.17553 1.000 18.58457 ? 143 LEU   A N   1 
ATOM   982  C CA  . LEU   A 1 136 ? 5.97651   -19.46092 -10.74158 1.000 18.99538 ? 143 LEU   A CA  1 
ATOM   983  C C   . LEU   A 1 136 ? 5.08320   -20.65822 -10.44930 1.000 24.06057 ? 143 LEU   A C   1 
ATOM   984  O O   . LEU   A 1 136 ? 5.22100   -21.29358 -9.39671  1.000 24.12407 ? 143 LEU   A O   1 
ATOM   985  C CB  . LEU   A 1 136 ? 5.38625   -18.20051 -10.10730 1.000 22.14277 ? 143 LEU   A CB  1 
ATOM   986  C CG  . LEU   A 1 136 ? 6.24232   -16.93420 -10.03147 1.000 23.30198 ? 143 LEU   A CG  1 
ATOM   987  C CD1 . LEU   A 1 136 ? 5.37940   -15.74229 -9.64357  1.000 22.24665 ? 143 LEU   A CD1 1 
ATOM   988  C CD2 . LEU   A 1 136 ? 7.36447   -17.12156 -9.02865  1.000 22.22211 ? 143 LEU   A CD2 1 
ATOM   989  N N   . VAL   A 1 137 ? 4.16622   -20.98118 -11.36024 1.000 21.86274 ? 144 VAL   A N   1 
ATOM   990  C CA  . VAL   A 1 137 ? 3.18410   -22.02780 -11.11136 1.000 20.72889 ? 144 VAL   A CA  1 
ATOM   991  C C   . VAL   A 1 137 ? 3.15237   -23.09886 -12.19218 1.000 21.21043 ? 144 VAL   A C   1 
ATOM   992  O O   . VAL   A 1 137 ? 2.59388   -24.18137 -11.94860 1.000 22.69072 ? 144 VAL   A O   1 
ATOM   993  C CB  . VAL   A 1 137 ? 1.77150   -21.43415 -10.92562 1.000 18.41920 ? 144 VAL   A CB  1 
ATOM   994  C CG1 . VAL   A 1 137 ? 1.72092   -20.56857 -9.67838  1.000 23.10560 ? 144 VAL   A CG1 1 
ATOM   995  C CG2 . VAL   A 1 137 ? 1.36563   -20.63841 -12.16173 1.000 18.71843 ? 144 VAL   A CG2 1 
ATOM   996  N N   . ALA   A 1 138 ? 3.70986   -22.85527 -13.37370 1.000 21.76203 ? 145 ALA   A N   1 
ATOM   997  C CA  . ALA   A 1 138 ? 3.61178   -23.78523 -14.48959 1.000 21.44920 ? 145 ALA   A CA  1 
ATOM   998  C C   . ALA   A 1 138 ? 4.95608   -24.43996 -14.76806 1.000 23.10833 ? 145 ALA   A C   1 
ATOM   999  O O   . ALA   A 1 138 ? 5.98992   -23.76777 -14.78693 1.000 24.08277 ? 145 ALA   A O   1 
ATOM   1000 C CB  . ALA   A 1 138 ? 3.11719   -23.07377 -15.75323 1.000 19.99905 ? 145 ALA   A CB  1 
ATOM   1001 N N   . GLU   A 1 139 ? 4.93426   -25.75764 -14.98412 1.000 24.16621 ? 146 GLU   A N   1 
ATOM   1002 C CA  . GLU   A 1 139 ? 6.11612   -26.45689 -15.47448 1.000 19.73079 ? 146 GLU   A CA  1 
ATOM   1003 C C   . GLU   A 1 139 ? 6.26777   -26.33280 -16.98392 1.000 25.96237 ? 146 GLU   A C   1 
ATOM   1004 O O   . GLU   A 1 139 ? 7.37033   -26.53094 -17.50678 1.000 22.08935 ? 146 GLU   A O   1 
ATOM   1005 C CB  . GLU   A 1 139 ? 6.06507   -27.93771 -15.08711 1.000 26.15786 ? 146 GLU   A CB  1 
ATOM   1006 C CG  . GLU   A 1 139 ? 5.01372   -28.75126 -15.82950 1.000 41.62839 ? 146 GLU   A CG  1 
ATOM   1007 C CD  . GLU   A 1 139 ? 4.77451   -30.10872 -15.19386 1.000 56.33076 ? 146 GLU   A CD  1 
ATOM   1008 O OE1 . GLU   A 1 139 ? 3.87555   -30.84159 -15.66061 1.000 60.08953 ? 146 GLU   A OE1 1 
ATOM   1009 O OE2 . GLU   A 1 139 ? 5.48586   -30.43995 -14.22299 1.000 59.15672 ? 146 GLU   A OE2 1 
ATOM   1010 N N   . LYS   A 1 140 ? 5.18245   -26.02029 -17.68693 1.000 23.26491 ? 147 LYS   A N   1 
ATOM   1011 C CA  . LYS   A 1 140 ? 5.19449   -25.79545 -19.12369 1.000 22.58704 ? 147 LYS   A CA  1 
ATOM   1012 C C   . LYS   A 1 140 ? 4.11919   -24.77292 -19.44941 1.000 20.61547 ? 147 LYS   A C   1 
ATOM   1013 O O   . LYS   A 1 140 ? 3.04514   -24.77929 -18.84245 1.000 21.43306 ? 147 LYS   A O   1 
ATOM   1014 C CB  . LYS   A 1 140 ? 4.94744   -27.09090 -19.90744 1.000 21.55487 ? 147 LYS   A CB  1 
ATOM   1015 C CG  . LYS   A 1 140 ? 5.06847   -26.93784 -21.41931 1.000 27.24287 ? 147 LYS   A CG  1 
ATOM   1016 C CD  . LYS   A 1 140 ? 5.00774   -28.28498 -22.12387 1.000 29.88484 ? 147 LYS   A CD  1 
ATOM   1017 C CE  . LYS   A 1 140 ? 3.56901   -28.74562 -22.30336 1.000 32.93530 ? 147 LYS   A CE  1 
ATOM   1018 N NZ  . LYS   A 1 140 ? 3.47143   -30.19340 -22.64343 1.000 36.73275 ? 147 LYS   A NZ  1 
ATOM   1019 N N   . VAL   A 1 141 ? 4.41861   -23.88931 -20.39517 1.000 20.02715 ? 148 VAL   A N   1 
ATOM   1020 C CA  . VAL   A 1 141 ? 3.47219   -22.88858 -20.86795 1.000 20.08836 ? 148 VAL   A CA  1 
ATOM   1021 C C   . VAL   A 1 141 ? 3.30860   -23.05106 -22.37018 1.000 20.48524 ? 148 VAL   A C   1 
ATOM   1022 O O   . VAL   A 1 141 ? 4.29880   -23.07935 -23.11076 1.000 21.24752 ? 148 VAL   A O   1 
ATOM   1023 C CB  . VAL   A 1 141 ? 3.92436   -21.45927 -20.52055 1.000 22.57466 ? 148 VAL   A CB  1 
ATOM   1024 C CG1 . VAL   A 1 141 ? 2.93827   -20.44680 -21.08316 1.000 21.24552 ? 148 VAL   A CG1 1 
ATOM   1025 C CG2 . VAL   A 1 141 ? 4.05322   -21.29473 -19.01091 1.000 21.40373 ? 148 VAL   A CG2 1 
ATOM   1026 N N   . THR   A 1 142 ? 2.06231   -23.16586 -22.81275 1.000 21.72946 ? 149 THR   A N   1 
ATOM   1027 C CA  . THR   A 1 142 ? 1.71891   -23.18525 -24.22646 1.000 20.20898 ? 149 THR   A CA  1 
ATOM   1028 C C   . THR   A 1 142 ? 0.90779   -21.93887 -24.54350 1.000 23.60965 ? 149 THR   A C   1 
ATOM   1029 O O   . THR   A 1 142 ? -0.04724  -21.61828 -23.82773 1.000 22.30842 ? 149 THR   A O   1 
ATOM   1030 C CB  . THR   A 1 142 ? 0.92459   -24.44253 -24.59155 1.000 23.60538 ? 149 THR   A CB  1 
ATOM   1031 O OG1 . THR   A 1 142 ? 1.62331   -25.60605 -24.12964 1.000 25.17686 ? 149 THR   A OG1 1 
ATOM   1032 C CG2 . THR   A 1 142 ? 0.73295   -24.53269 -26.09915 1.000 24.65311 ? 149 THR   A CG2 1 
ATOM   1033 N N   . VAL   A 1 143 ? 1.29528   -21.23186 -25.60110 1.000 19.10241 ? 150 VAL   A N   1 
ATOM   1034 C CA  . VAL   A 1 143 ? 0.61323   -20.01566 -26.02346 1.000 19.62560 ? 150 VAL   A CA  1 
ATOM   1035 C C   . VAL   A 1 143 ? 0.12704   -20.21266 -27.44998 1.000 19.63088 ? 150 VAL   A C   1 
ATOM   1036 O O   . VAL   A 1 143 ? 0.93514   -20.41812 -28.36437 1.000 23.24700 ? 150 VAL   A O   1 
ATOM   1037 C CB  . VAL   A 1 143 ? 1.52106   -18.78109 -25.92552 1.000 21.04672 ? 150 VAL   A CB  1 
ATOM   1038 C CG1 . VAL   A 1 143 ? 0.77521   -17.54761 -26.40201 1.000 23.03858 ? 150 VAL   A CG1 1 
ATOM   1039 C CG2 . VAL   A 1 143 ? 2.00923   -18.59449 -24.50132 1.000 19.77904 ? 150 VAL   A CG2 1 
ATOM   1040 N N   . ILE   A 1 144 ? -1.18793  -20.16494 -27.63739 1.000 18.49418 ? 151 ILE   A N   1 
ATOM   1041 C CA  . ILE   A 1 144 ? -1.80989  -20.15171 -28.95538 1.000 20.15322 ? 151 ILE   A CA  1 
ATOM   1042 C C   . ILE   A 1 144 ? -2.21210  -18.71341 -29.24161 1.000 19.45396 ? 151 ILE   A C   1 
ATOM   1043 O O   . ILE   A 1 144 ? -2.83571  -18.06236 -28.39438 1.000 21.33076 ? 151 ILE   A O   1 
ATOM   1044 C CB  . ILE   A 1 144 ? -3.03022  -21.08825 -29.02267 1.000 24.19442 ? 151 ILE   A CB  1 
ATOM   1045 C CG1 . ILE   A 1 144 ? -2.74788  -22.41876 -28.31976 1.000 29.23374 ? 151 ILE   A CG1 1 
ATOM   1046 C CG2 . ILE   A 1 144 ? -3.42326  -21.34102 -30.46733 1.000 26.15543 ? 151 ILE   A CG2 1 
ATOM   1047 C CD1 . ILE   A 1 144 ? -1.73636  -23.26326 -29.02718 1.000 25.32191 ? 151 ILE   A CD1 1 
ATOM   1048 N N   . THR   A 1 145 ? -1.84815  -18.20434 -30.41552 1.000 22.20883 ? 152 THR   A N   1 
ATOM   1049 C CA  . THR   A 1 145 ? -2.10142  -16.79751 -30.68515 1.000 17.85516 ? 152 THR   A CA  1 
ATOM   1050 C C   . THR   A 1 145 ? -2.37280  -16.58757 -32.16638 1.000 22.74695 ? 152 THR   A C   1 
ATOM   1051 O O   . THR   A 1 145 ? -1.87218  -17.32566 -33.02015 1.000 19.53651 ? 152 THR   A O   1 
ATOM   1052 C CB  . THR   A 1 145 ? -0.93095  -15.92026 -30.21360 1.000 18.91337 ? 152 THR   A CB  1 
ATOM   1053 O OG1 . THR   A 1 145 ? -1.30433  -14.53754 -30.28390 1.000 19.83028 ? 152 THR   A OG1 1 
ATOM   1054 C CG2 . THR   A 1 145 ? 0.31160   -16.16645 -31.06383 1.000 24.80325 ? 152 THR   A CG2 1 
ATOM   1055 N N   . LYS   A 1 146 ? -3.17905  -15.56843 -32.45577 1.000 19.99594 ? 153 LYS   A N   1 
ATOM   1056 C CA  . LYS   A 1 146 ? -3.54266  -15.23323 -33.82728 1.000 21.64348 ? 153 LYS   A CA  1 
ATOM   1057 C C   . LYS   A 1 146 ? -3.66772  -13.72339 -33.94488 1.000 25.28583 ? 153 LYS   A C   1 
ATOM   1058 O O   . LYS   A 1 146 ? -4.52818  -13.11917 -33.29780 1.000 22.16411 ? 153 LYS   A O   1 
ATOM   1059 C CB  . LYS   A 1 146 ? -4.85009  -15.91311 -34.23383 1.000 21.89757 ? 153 LYS   A CB  1 
ATOM   1060 C CG  . LYS   A 1 146 ? -5.40500  -15.43054 -35.56383 1.000 25.17847 ? 153 LYS   A CG  1 
ATOM   1061 C CD  . LYS   A 1 146 ? -4.55271  -15.91598 -36.72568 1.000 22.68137 ? 153 LYS   A CD  1 
ATOM   1062 C CE  . LYS   A 1 146 ? -5.25226  -15.68489 -38.05539 1.000 29.70387 ? 153 LYS   A CE  1 
ATOM   1063 N NZ  . LYS   A 1 146 ? -5.18661  -14.25961 -38.48248 1.000 26.40796 ? 153 LYS   A NZ  1 
ATOM   1064 N N   . HIS   A 1 147 ? -2.80963  -13.12822 -34.76553 1.000 20.40779 ? 154 HIS   A N   1 
ATOM   1065 C CA  . HIS   A 1 147 ? -2.83277  -11.71005 -35.08881 1.000 20.54387 ? 154 HIS   A CA  1 
ATOM   1066 C C   . HIS   A 1 147 ? -3.45145  -11.53974 -36.47247 1.000 23.93197 ? 154 HIS   A C   1 
ATOM   1067 O O   . HIS   A 1 147 ? -3.28823  -12.39841 -37.34273 1.000 24.03063 ? 154 HIS   A O   1 
ATOM   1068 C CB  . HIS   A 1 147 ? -1.40565  -11.14762 -35.04997 1.000 20.33587 ? 154 HIS   A CB  1 
ATOM   1069 C CG  . HIS   A 1 147 ? -1.31678  -9.65881  -35.16351 1.000 23.88565 ? 154 HIS   A CG  1 
ATOM   1070 N ND1 . HIS   A 1 147 ? -1.47549  -8.98755  -36.35764 1.000 24.23109 ? 154 HIS   A ND1 1 
ATOM   1071 C CD2 . HIS   A 1 147 ? -1.05163  -8.71176  -34.23331 1.000 26.91441 ? 154 HIS   A CD2 1 
ATOM   1072 C CE1 . HIS   A 1 147 ? -1.33003  -7.69145  -36.15330 1.000 29.76252 ? 154 HIS   A CE1 1 
ATOM   1073 N NE2 . HIS   A 1 147 ? -1.07111  -7.49686  -34.87205 1.000 29.33288 ? 154 HIS   A NE2 1 
ATOM   1074 N N   . ASN   A 1 148 ? -4.18503  -10.43567 -36.66737 1.000 22.64104 ? 155 ASN   A N   1 
ATOM   1075 C CA  . ASN   A 1 148 ? -4.85282  -10.21085 -37.95072 1.000 24.13288 ? 155 ASN   A CA  1 
ATOM   1076 C C   . ASN   A 1 148 ? -3.88944  -10.30706 -39.12809 1.000 29.14063 ? 155 ASN   A C   1 
ATOM   1077 O O   . ASN   A 1 148 ? -4.29365  -10.68308 -40.23451 1.000 28.74747 ? 155 ASN   A O   1 
ATOM   1078 C CB  . ASN   A 1 148 ? -5.54235  -8.84217  -37.97467 1.000 26.41635 ? 155 ASN   A CB  1 
ATOM   1079 C CG  . ASN   A 1 148 ? -6.85692  -8.82827  -37.22092 1.000 27.90115 ? 155 ASN   A CG  1 
ATOM   1080 O OD1 . ASN   A 1 148 ? -7.52585  -9.85459  -37.09520 1.000 25.73220 ? 155 ASN   A OD1 1 
ATOM   1081 N ND2 . ASN   A 1 148 ? -7.25158  -7.65162  -36.74330 1.000 28.78146 ? 155 ASN   A ND2 1 
ATOM   1082 N N   . ASP   A 1 149 ? -2.61573  -9.99178  -38.91155 1.000 25.34943 ? 156 ASP   A N   1 
ATOM   1083 C CA  . ASP   A 1 149 ? -1.64220  -9.90289  -39.98895 1.000 27.77955 ? 156 ASP   A CA  1 
ATOM   1084 C C   . ASP   A 1 149 ? -0.80325  -11.16257 -40.15404 1.000 34.87369 ? 156 ASP   A C   1 
ATOM   1085 O O   . ASP   A 1 149 ? 0.07154   -11.19456 -41.02392 1.000 35.00409 ? 156 ASP   A O   1 
ATOM   1086 C CB  . ASP   A 1 149 ? -0.72159  -8.70321  -39.75853 1.000 29.79714 ? 156 ASP   A CB  1 
ATOM   1087 C CG  . ASP   A 1 149 ? -1.44268  -7.38043  -39.92446 1.000 36.67318 ? 156 ASP   A CG  1 
ATOM   1088 O OD1 . ASP   A 1 149 ? -2.58989  -7.38738  -40.42165 1.000 32.98572 ? 156 ASP   A OD1 1 
ATOM   1089 O OD2 . ASP   A 1 149 ? -0.86698  -6.33621  -39.55619 1.000 39.66850 ? 156 ASP   A OD2 1 
ATOM   1090 N N   . ASP   A 1 150 ? -1.04396  -12.20038 -39.35441 1.000 29.71793 ? 157 ASP   A N   1 
ATOM   1091 C CA  . ASP   A 1 150 ? -0.22722  -13.40568 -39.40059 1.000 29.22866 ? 157 ASP   A CA  1 
ATOM   1092 C C   . ASP   A 1 150 ? -1.11033  -14.63560 -39.24610 1.000 31.60726 ? 157 ASP   A C   1 
ATOM   1093 O O   . ASP   A 1 150 ? -2.33085  -14.54137 -39.08421 1.000 26.00801 ? 157 ASP   A O   1 
ATOM   1094 C CB  . ASP   A 1 150 ? 0.86085   -13.38094 -38.32118 1.000 25.91864 ? 157 ASP   A CB  1 
ATOM   1095 C CG  . ASP   A 1 150 ? 2.16009   -14.00016 -38.79112 1.000 33.98386 ? 157 ASP   A CG  1 
ATOM   1096 O OD1 . ASP   A 1 150 ? 2.11473   -14.88839 -39.67031 1.000 28.13661 ? 157 ASP   A OD1 1 
ATOM   1097 O OD2 . ASP   A 1 150 ? 3.22742   -13.61208 -38.27242 1.000 28.45258 ? 157 ASP   A OD2 1 
ATOM   1098 N N   . GLU   A 1 151 ? -0.47135  -15.80022 -39.30271 1.000 26.64378 ? 158 GLU   A N   1 
ATOM   1099 C CA  . GLU   A 1 151 ? -1.14372  -17.07477 -39.12987 1.000 28.40527 ? 158 GLU   A CA  1 
ATOM   1100 C C   . GLU   A 1 151 ? -1.28369  -17.39704 -37.64294 1.000 24.84543 ? 158 GLU   A C   1 
ATOM   1101 O O   . GLU   A 1 151 ? -0.79127  -16.67594 -36.77160 1.000 24.88692 ? 158 GLU   A O   1 
ATOM   1102 C CB  . GLU   A 1 151 ? -0.37144  -18.18266 -39.84737 1.000 28.51815 ? 158 GLU   A CB  1 
ATOM   1103 C CG  . GLU   A 1 151 ? -0.31728  -18.02446 -41.35744 1.000 42.17632 ? 158 GLU   A CG  1 
ATOM   1104 C CD  . GLU   A 1 151 ? -1.65810  -18.27009 -42.02186 1.000 65.68897 ? 158 GLU   A CD  1 
ATOM   1105 O OE1 . GLU   A 1 151 ? -2.18665  -17.33776 -42.66406 1.000 71.92052 ? 158 GLU   A OE1 1 
ATOM   1106 O OE2 . GLU   A 1 151 ? -2.18008  -19.39934 -41.90835 1.000 83.60421 ? 158 GLU   A OE2 1 
ATOM   1107 N N   . GLN   A 1 152 ? -1.96705  -18.50154 -37.35508 1.000 23.13875 ? 159 GLN   A N   1 
ATOM   1108 C CA  . GLN   A 1 152 ? -2.11254  -18.96161 -35.98095 1.000 26.19566 ? 159 GLN   A CA  1 
ATOM   1109 C C   . GLN   A 1 152 ? -0.89658  -19.79200 -35.59032 1.000 22.36949 ? 159 GLN   A C   1 
ATOM   1110 O O   . GLN   A 1 152 ? -0.48796  -20.69397 -36.32887 1.000 27.00200 ? 159 GLN   A O   1 
ATOM   1111 C CB  . GLN   A 1 152 ? -3.39083  -19.78315 -35.82251 1.000 27.12557 ? 159 GLN   A CB  1 
ATOM   1112 C CG  . GLN   A 1 152 ? -3.70371  -20.16344 -34.38376 1.000 24.97878 ? 159 GLN   A CG  1 
ATOM   1113 C CD  . GLN   A 1 152 ? -5.13915  -20.61328 -34.19999 1.000 32.55946 ? 159 GLN   A CD  1 
ATOM   1114 O OE1 . GLN   A 1 152 ? -6.07580  -19.90644 -34.57247 1.000 33.15846 ? 159 GLN   A OE1 1 
ATOM   1115 N NE2 . GLN   A 1 152 ? -5.31999  -21.79041 -33.61294 1.000 30.26144 ? 159 GLN   A NE2 1 
ATOM   1116 N N   . TYR   A 1 153 ? -0.32218  -19.49321 -34.42749 1.000 19.44549 ? 160 TYR   A N   1 
ATOM   1117 C CA  . TYR   A 1 153 ? 0.90627   -20.13636 -33.99095 1.000 22.07969 ? 160 TYR   A CA  1 
ATOM   1118 C C   . TYR   A 1 153 ? 0.74555   -20.71069 -32.59271 1.000 25.69418 ? 160 TYR   A C   1 
ATOM   1119 O O   . TYR   A 1 153 ? -0.09487  -20.26997 -31.80332 1.000 21.36151 ? 160 TYR   A O   1 
ATOM   1120 C CB  . TYR   A 1 153 ? 2.08752   -19.16374 -33.99098 1.000 21.13668 ? 160 TYR   A CB  1 
ATOM   1121 C CG  . TYR   A 1 153 ? 2.47288   -18.67932 -35.35998 1.000 24.18042 ? 160 TYR   A CG  1 
ATOM   1122 C CD1 . TYR   A 1 153 ? 3.30897   -19.43039 -36.17044 1.000 24.64658 ? 160 TYR   A CD1 1 
ATOM   1123 C CD2 . TYR   A 1 153 ? 2.02040   -17.45867 -35.83455 1.000 31.37936 ? 160 TYR   A CD2 1 
ATOM   1124 C CE1 . TYR   A 1 153 ? 3.66491   -18.98832 -37.43120 1.000 30.09727 ? 160 TYR   A CE1 1 
ATOM   1125 C CE2 . TYR   A 1 153 ? 2.37204   -17.00451 -37.08927 1.000 27.47108 ? 160 TYR   A CE2 1 
ATOM   1126 C CZ  . TYR   A 1 153 ? 3.19317   -17.77186 -37.88176 1.000 29.41985 ? 160 TYR   A CZ  1 
ATOM   1127 O OH  . TYR   A 1 153 ? 3.54546   -17.31828 -39.13279 1.000 43.71790 ? 160 TYR   A OH  1 
ATOM   1128 N N   . ALA   A 1 154 ? 1.58416   -21.70089 -32.29768 1.000 21.05972 ? 161 ALA   A N   1 
ATOM   1129 C CA  . ALA   A 1 154 ? 1.71862   -22.26087 -30.96086 1.000 23.17532 ? 161 ALA   A CA  1 
ATOM   1130 C C   . ALA   A 1 154 ? 3.15603   -22.06184 -30.50502 1.000 21.27310 ? 161 ALA   A C   1 
ATOM   1131 O O   . ALA   A 1 154 ? 4.08934   -22.55862 -31.14573 1.000 22.58087 ? 161 ALA   A O   1 
ATOM   1132 C CB  . ALA   A 1 154 ? 1.34052   -23.74236 -30.93420 1.000 21.17529 ? 161 ALA   A CB  1 
ATOM   1133 N N   . TRP   A 1 155 ? 3.32631   -21.31027 -29.42357 1.000 18.30491 ? 162 TRP   A N   1 
ATOM   1134 C CA  . TRP   A 1 155 ? 4.60057   -21.13156 -28.74360 1.000 19.48927 ? 162 TRP   A CA  1 
ATOM   1135 C C   . TRP   A 1 155 ? 4.58549   -22.01432 -27.50272 1.000 19.48678 ? 162 TRP   A C   1 
ATOM   1136 O O   . TRP   A 1 155 ? 3.54132   -22.17159 -26.86383 1.000 21.81123 ? 162 TRP   A O   1 
ATOM   1137 C CB  . TRP   A 1 155 ? 4.78744   -19.65249 -28.38086 1.000 18.80067 ? 162 TRP   A CB  1 
ATOM   1138 C CG  . TRP   A 1 155 ? 6.01826   -19.25452 -27.59459 1.000 18.38603 ? 162 TRP   A CG  1 
ATOM   1139 C CD1 . TRP   A 1 155 ? 7.12079   -18.60815 -28.07811 1.000 17.93372 ? 162 TRP   A CD1 1 
ATOM   1140 C CD2 . TRP   A 1 155 ? 6.23027   -19.40058 -26.18219 1.000 21.79941 ? 162 TRP   A CD2 1 
ATOM   1141 N NE1 . TRP   A 1 155 ? 8.01741   -18.37509 -27.06485 1.000 20.17921 ? 162 TRP   A NE1 1 
ATOM   1142 C CE2 . TRP   A 1 155 ? 7.49578   -18.85126 -25.89078 1.000 19.81240 ? 162 TRP   A CE2 1 
ATOM   1143 C CE3 . TRP   A 1 155 ? 5.48197   -19.95737 -25.13988 1.000 20.36642 ? 162 TRP   A CE3 1 
ATOM   1144 C CZ2 . TRP   A 1 155 ? 8.02971   -18.84346 -24.60093 1.000 21.51241 ? 162 TRP   A CZ2 1 
ATOM   1145 C CZ3 . TRP   A 1 155 ? 6.01670   -19.95013 -23.85946 1.000 20.37351 ? 162 TRP   A CZ3 1 
ATOM   1146 C CH2 . TRP   A 1 155 ? 7.27539   -19.39445 -23.60298 1.000 16.53506 ? 162 TRP   A CH2 1 
ATOM   1147 N N   . GLU   A 1 156 ? 5.72814   -22.61481 -27.17422 1.000 20.86014 ? 163 GLU   A N   1 
ATOM   1148 C CA  . GLU   A 1 156 ? 5.76029   -23.53607 -26.04585 1.000 18.70839 ? 163 GLU   A CA  1 
ATOM   1149 C C   . GLU   A 1 156 ? 7.15349   -23.56524 -25.43784 1.000 21.45834 ? 163 GLU   A C   1 
ATOM   1150 O O   . GLU   A 1 156 ? 8.15320   -23.58748 -26.15984 1.000 22.05653 ? 163 GLU   A O   1 
ATOM   1151 C CB  . GLU   A 1 156 ? 5.34512   -24.95205 -26.46867 1.000 26.14643 ? 163 GLU   A CB  1 
ATOM   1152 C CG  . GLU   A 1 156 ? 5.04212   -25.88345 -25.30603 1.000 27.40553 ? 163 GLU   A CG  1 
ATOM   1153 C CD  . GLU   A 1 156 ? 4.33418   -27.15569 -25.73988 1.000 42.85630 ? 163 GLU   A CD  1 
ATOM   1154 O OE1 . GLU   A 1 156 ? 4.98289   -28.00608 -26.38510 1.000 38.87864 ? 163 GLU   A OE1 1 
ATOM   1155 O OE2 . GLU   A 1 156 ? 3.12823   -27.29911 -25.44507 1.000 36.35193 ? 163 GLU   A OE2 1 
ATOM   1156 N N   . SER   A 1 157 ? 7.21235   -23.58055 -24.10767 1.000 20.86961 ? 164 SER   A N   1 
ATOM   1157 C CA  . SER   A 1 157 ? 8.48886   -23.70034 -23.42048 1.000 17.61423 ? 164 SER   A CA  1 
ATOM   1158 C C   . SER   A 1 157 ? 8.28493   -24.33287 -22.05379 1.000 21.13997 ? 164 SER   A C   1 
ATOM   1159 O O   . SER   A 1 157 ? 7.34357   -23.98990 -21.33359 1.000 21.84186 ? 164 SER   A O   1 
ATOM   1160 C CB  . SER   A 1 157 ? 9.17980   -22.34171 -23.26139 1.000 18.70576 ? 164 SER   A CB  1 
ATOM   1161 O OG  . SER   A 1 157 ? 10.40328  -22.48463 -22.55867 1.000 22.14860 ? 164 SER   A OG  1 
ATOM   1162 N N   . SER   A 1 158 ? 9.17015   -25.27199 -21.71870 1.000 21.70366 ? 165 SER   A N   1 
ATOM   1163 C CA  . SER   A 1 158 ? 9.31215   -25.79830 -20.36789 1.000 22.49913 ? 165 SER   A CA  1 
ATOM   1164 C C   . SER   A 1 158 ? 10.52854  -25.20781 -19.66609 1.000 26.22628 ? 165 SER   A C   1 
ATOM   1165 O O   . SER   A 1 158 ? 11.12442  -25.85715 -18.79846 1.000 26.84645 ? 165 SER   A O   1 
ATOM   1166 C CB  . SER   A 1 158 ? 9.40296   -27.32398 -20.39730 1.000 27.88817 ? 165 SER   A CB  1 
ATOM   1167 O OG  . SER   A 1 158 ? 8.18984   -27.89739 -20.85131 1.000 25.32040 ? 165 SER   A OG  1 
ATOM   1168 N N   . ALA   A 1 159 ? 10.90566  -23.98940 -20.04058 1.000 23.12035 ? 166 ALA   A N   1 
ATOM   1169 C CA  . ALA   A 1 159 ? 12.13384  -23.32201 -19.59041 1.000 24.91986 ? 166 ALA   A CA  1 
ATOM   1170 C C   . ALA   A 1 159 ? 13.32724  -24.15563 -20.06490 1.000 29.44819 ? 166 ALA   A C   1 
ATOM   1171 O O   . ALA   A 1 159 ? 13.29237  -24.74924 -21.15048 1.000 30.46067 ? 166 ALA   A O   1 
ATOM   1172 C CB  . ALA   A 1 159 ? 12.08100  -23.07526 -18.09445 1.000 29.74462 ? 166 ALA   A CB  1 
ATOM   1173 N N   . GLY   A 1 160 ? 14.39255  -24.20837 -19.26962 1.000 24.08317 ? 167 GLY   A N   1 
ATOM   1174 C CA  . GLY   A 1 160 ? 15.57785  -24.93331 -19.67567 1.000 30.22807 ? 167 GLY   A CA  1 
ATOM   1175 C C   . GLY   A 1 160 ? 16.35231  -24.30314 -20.80883 1.000 25.83738 ? 167 GLY   A C   1 
ATOM   1176 O O   . GLY   A 1 160 ? 17.22499  -24.96014 -21.38459 1.000 29.18772 ? 167 GLY   A O   1 
ATOM   1177 N N   . GLY   A 1 161 ? 16.04646  -23.05682 -21.16403 1.000 24.60910 ? 168 GLY   A N   1 
ATOM   1178 C CA  . GLY   A 1 161 ? 16.82086  -22.31649 -22.13498 1.000 26.88927 ? 168 GLY   A CA  1 
ATOM   1179 C C   . GLY   A 1 161 ? 16.29478  -22.32539 -23.55364 1.000 25.62945 ? 168 GLY   A C   1 
ATOM   1180 O O   . GLY   A 1 161 ? 16.90873  -21.69194 -24.42049 1.000 22.43849 ? 168 GLY   A O   1 
ATOM   1181 N N   . SER   A 1 162 ? 15.18173  -23.00329 -23.82554 1.000 22.36662 ? 169 SER   A N   1 
ATOM   1182 C CA  . SER   A 1 162 ? 14.70050  -23.12007 -25.19390 1.000 21.77009 ? 169 SER   A CA  1 
ATOM   1183 C C   . SER   A 1 162 ? 13.18410  -23.00444 -25.23895 1.000 21.64152 ? 169 SER   A C   1 
ATOM   1184 O O   . SER   A 1 162 ? 12.48624  -23.25814 -24.25434 1.000 19.52043 ? 169 SER   A O   1 
ATOM   1185 C CB  . SER   A 1 162 ? 15.14705  -24.44300 -25.83386 1.000 23.59636 ? 169 SER   A CB  1 
ATOM   1186 O OG  . SER   A 1 162 ? 14.36725  -25.52783 -25.36467 1.000 25.08774 ? 169 SER   A OG  1 
ATOM   1187 N N   . PHE   A 1 163 ? 12.68530  -22.60748 -26.40806 1.000 19.38587 ? 170 PHE   A N   1 
ATOM   1188 C CA  . PHE   A 1 163 ? 11.25828  -22.59076 -26.68866 1.000 18.89350 ? 170 PHE   A CA  1 
ATOM   1189 C C   . PHE   A 1 163 ? 11.04146  -23.04541 -28.12455 1.000 21.44069 ? 170 PHE   A C   1 
ATOM   1190 O O   . PHE   A 1 163 ? 11.96991  -23.06361 -28.93603 1.000 21.29880 ? 170 PHE   A O   1 
ATOM   1191 C CB  . PHE   A 1 163 ? 10.63997  -21.20099 -26.45244 1.000 17.91679 ? 170 PHE   A CB  1 
ATOM   1192 C CG  . PHE   A 1 163 ? 11.17078  -20.11714 -27.36332 1.000 18.51948 ? 170 PHE   A CG  1 
ATOM   1193 C CD1 . PHE   A 1 163 ? 12.29141  -19.38187 -27.00660 1.000 20.50360 ? 170 PHE   A CD1 1 
ATOM   1194 C CD2 . PHE   A 1 163 ? 10.52158  -19.79896 -28.54847 1.000 18.48844 ? 170 PHE   A CD2 1 
ATOM   1195 C CE1 . PHE   A 1 163 ? 12.77257  -18.37221 -27.82745 1.000 22.60651 ? 170 PHE   A CE1 1 
ATOM   1196 C CE2 . PHE   A 1 163 ? 10.99946  -18.78992 -29.37354 1.000 20.62693 ? 170 PHE   A CE2 1 
ATOM   1197 C CZ  . PHE   A 1 163 ? 12.12301  -18.07462 -29.00746 1.000 21.09874 ? 170 PHE   A CZ  1 
ATOM   1198 N N   . THR   A 1 164 ? 9.80514   -23.43067 -28.43103 1.000 21.23289 ? 171 THR   A N   1 
ATOM   1199 C CA  . THR   A 1 164 ? 9.44615   -23.86828 -29.77073 1.000 19.98536 ? 171 THR   A CA  1 
ATOM   1200 C C   . THR   A 1 164 ? 8.30979   -23.01379 -30.31185 1.000 19.21560 ? 171 THR   A C   1 
ATOM   1201 O O   . THR   A 1 164 ? 7.48723   -22.48995 -29.55611 1.000 18.76922 ? 171 THR   A O   1 
ATOM   1202 C CB  . THR   A 1 164 ? 9.02410   -25.34629 -29.80534 1.000 23.52815 ? 171 THR   A CB  1 
ATOM   1203 O OG1 . THR   A 1 164 ? 7.81637   -25.52137 -29.05277 1.000 22.41076 ? 171 THR   A OG1 1 
ATOM   1204 C CG2 . THR   A 1 164 ? 10.11744  -26.23963 -29.23204 1.000 24.82427 ? 171 THR   A CG2 1 
ATOM   1205 N N   . VAL   A 1 165 ? 8.27708   -22.87640 -31.63341 1.000 21.49830 ? 172 VAL   A N   1 
ATOM   1206 C CA  . VAL   A 1 165 ? 7.18135   -22.22468 -32.33939 1.000 20.85762 ? 172 VAL   A CA  1 
ATOM   1207 C C   . VAL   A 1 165 ? 6.78576   -23.10941 -33.51248 1.000 22.25757 ? 172 VAL   A C   1 
ATOM   1208 O O   . VAL   A 1 165 ? 7.64843   -23.64726 -34.21631 1.000 21.56516 ? 172 VAL   A O   1 
ATOM   1209 C CB  . VAL   A 1 165 ? 7.55557   -20.80643 -32.82765 1.000 23.22248 ? 172 VAL   A CB  1 
ATOM   1210 C CG1 . VAL   A 1 165 ? 6.41978   -20.20612 -33.64836 1.000 21.63398 ? 172 VAL   A CG1 1 
ATOM   1211 C CG2 . VAL   A 1 165 ? 7.87342   -19.89824 -31.64909 1.000 18.73474 ? 172 VAL   A CG2 1 
ATOM   1212 N N   . ARG   A 1 166 ? 5.48011   -23.27373 -33.71001 1.000 20.79167 ? 173 ARG   A N   1 
ATOM   1213 C CA  . ARG   A 1 166 ? 4.95558   -24.03695 -34.82952 1.000 26.65239 ? 173 ARG   A CA  1 
ATOM   1214 C C   . ARG   A 1 166 ? 3.66437   -23.38911 -35.29919 1.000 23.76026 ? 173 ARG   A C   1 
ATOM   1215 O O   . ARG   A 1 166 ? 2.97374   -22.71956 -34.52565 1.000 22.17855 ? 173 ARG   A O   1 
ATOM   1216 C CB  . ARG   A 1 166 ? 4.68638   -25.49916 -34.44878 1.000 25.40909 ? 173 ARG   A CB  1 
ATOM   1217 C CG  . ARG   A 1 166 ? 3.62133   -25.65591 -33.37263 1.000 31.93847 ? 173 ARG   A CG  1 
ATOM   1218 C CD  . ARG   A 1 166 ? 3.32643   -27.11336 -33.05849 1.000 39.25535 ? 173 ARG   A CD  1 
ATOM   1219 N NE  . ARG   A 1 166 ? 4.47055   -27.80756 -32.48133 1.000 64.69946 ? 173 ARG   A NE  1 
ATOM   1220 C CZ  . ARG   A 1 166 ? 4.82477   -27.73426 -31.20531 1.000 55.60703 ? 173 ARG   A CZ  1 
ATOM   1221 N NH1 . ARG   A 1 166 ? 4.16562   -26.97264 -30.34727 1.000 54.87183 ? 173 ARG   A NH1 1 
ATOM   1222 N NH2 . ARG   A 1 166 ? 5.86509   -28.44433 -30.77816 1.000 55.66034 ? 173 ARG   A NH2 1 
ATOM   1223 N N   . THR   A 1 167 ? 3.34690   -23.58965 -36.57638 1.000 26.23903 ? 174 THR   A N   1 
ATOM   1224 C CA  . THR   A 1 167 ? 2.01745   -23.25304 -37.06473 1.000 32.27237 ? 174 THR   A CA  1 
ATOM   1225 C C   . THR   A 1 167 ? 0.99969   -24.17814 -36.40943 1.000 34.31597 ? 174 THR   A C   1 
ATOM   1226 O O   . THR   A 1 167 ? 1.19649   -25.39568 -36.36119 1.000 39.21261 ? 174 THR   A O   1 
ATOM   1227 C CB  . THR   A 1 167 ? 1.96257   -23.38359 -38.58764 1.000 38.96271 ? 174 THR   A CB  1 
ATOM   1228 O OG1 . THR   A 1 167 ? 2.87465   -22.44988 -39.18138 1.000 34.42057 ? 174 THR   A OG1 1 
ATOM   1229 C CG2 . THR   A 1 167 ? 0.55972   -23.10082 -39.10138 1.000 46.61649 ? 174 THR   A CG2 1 
ATOM   1230 N N   . ASP   A 1 168 ? -0.08261  -23.60366 -35.88906 1.000 31.32066 ? 175 ASP   A N   1 
ATOM   1231 C CA  . ASP   A 1 168 ? -1.03973  -24.36437 -35.09437 1.000 29.06150 ? 175 ASP   A CA  1 
ATOM   1232 C C   . ASP   A 1 168 ? -2.15315  -24.90320 -35.98421 1.000 49.66469 ? 175 ASP   A C   1 
ATOM   1233 O O   . ASP   A 1 168 ? -2.81354  -24.13887 -36.69628 1.000 47.62119 ? 175 ASP   A O   1 
ATOM   1234 C CB  . ASP   A 1 168 ? -1.62495  -23.50841 -33.97450 1.000 24.91780 ? 175 ASP   A CB  1 
ATOM   1235 C CG  . ASP   A 1 168 ? -2.58841  -24.28670 -33.09556 1.000 40.73329 ? 175 ASP   A CG  1 
ATOM   1236 O OD1 . ASP   A 1 168 ? -2.36456  -25.49912 -32.89673 1.000 43.45954 ? 175 ASP   A OD1 1 
ATOM   1237 O OD2 . ASP   A 1 168 ? -3.57175  -23.68981 -32.61401 1.000 38.98815 ? 175 ASP   A OD2 1 
ATOM   1238 N N   . THR   A 1 169 ? -2.36787  -26.21656 -35.92495 1.000 47.50494 ? 176 THR   A N   1 
ATOM   1239 C CA  . THR   A 1 169 ? -3.38888  -26.88749 -36.71670 1.000 64.67287 ? 176 THR   A CA  1 
ATOM   1240 C C   . THR   A 1 169 ? -4.72425  -27.02133 -35.99513 1.000 65.55716 ? 176 THR   A C   1 
ATOM   1241 O O   . THR   A 1 169 ? -5.71336  -27.40310 -36.62944 1.000 57.54178 ? 176 THR   A O   1 
ATOM   1242 C CB  . THR   A 1 169 ? -2.89904  -28.28119 -37.12608 1.000 69.96927 ? 176 THR   A CB  1 
ATOM   1243 O OG1 . THR   A 1 169 ? -2.45709  -28.99142 -35.96054 1.000 76.16220 ? 176 THR   A OG1 1 
ATOM   1244 C CG2 . THR   A 1 169 ? -1.74750  -28.16921 -38.10982 1.000 62.33355 ? 176 THR   A CG2 1 
ATOM   1245 N N   . GLY   A 1 170 ? -4.78195  -26.71411 -34.70069 1.000 58.39243 ? 177 GLY   A N   1 
ATOM   1246 C CA  . GLY   A 1 170 ? -5.98914  -26.91508 -33.92019 1.000 57.05399 ? 177 GLY   A CA  1 
ATOM   1247 C C   . GLY   A 1 170 ? -7.13971  -25.98481 -34.25389 1.000 55.96538 ? 177 GLY   A C   1 
ATOM   1248 O O   . GLY   A 1 170 ? -7.15055  -25.35070 -35.31368 1.000 49.02206 ? 177 GLY   A O   1 
ATOM   1249 N N   . GLU   A 1 171 ? -8.11794  -25.91394 -33.35115 1.000 50.13032 ? 178 GLU   A N   1 
ATOM   1250 C CA  . GLU   A 1 171 ? -9.27779  -25.05094 -33.52514 1.000 48.12785 ? 178 GLU   A CA  1 
ATOM   1251 C C   . GLU   A 1 171 ? -8.83887  -23.61323 -33.79755 1.000 41.79357 ? 178 GLU   A C   1 
ATOM   1252 O O   . GLU   A 1 171 ? -8.04490  -23.05600 -33.02560 1.000 40.46040 ? 178 GLU   A O   1 
ATOM   1253 C CB  . GLU   A 1 171 ? -10.15666 -25.09534 -32.27293 1.000 56.78384 ? 178 GLU   A CB  1 
ATOM   1254 C CG  . GLU   A 1 171 ? -11.55484 -24.49277 -32.42071 1.000 63.31133 ? 178 GLU   A CG  1 
ATOM   1255 C CD  . GLU   A 1 171 ? -12.56226 -25.44598 -33.03324 1.000 73.80473 ? 178 GLU   A CD  1 
ATOM   1256 O OE1 . GLU   A 1 171 ? -12.57783 -26.63130 -32.64166 1.000 65.48784 ? 178 GLU   A OE1 1 
ATOM   1257 O OE2 . GLU   A 1 171 ? -13.36555 -25.00422 -33.88164 1.000 57.16386 ? 178 GLU   A OE2 1 
ATOM   1258 N N   . PRO   A 1 172 ? -9.32035  -22.98661 -34.86947 1.000 38.40628 ? 179 PRO   A N   1 
ATOM   1259 C CA  . PRO   A 1 172 ? -8.95139  -21.58995 -35.13240 1.000 46.99040 ? 179 PRO   A CA  1 
ATOM   1260 C C   . PRO   A 1 172 ? -9.54114  -20.64176 -34.09715 1.000 41.90203 ? 179 PRO   A C   1 
ATOM   1261 O O   . PRO   A 1 172 ? -10.68031 -20.80174 -33.65142 1.000 44.46258 ? 179 PRO   A O   1 
ATOM   1262 C CB  . PRO   A 1 172 ? -9.52136  -21.32335 -36.53171 1.000 42.92667 ? 179 PRO   A CB  1 
ATOM   1263 C CG  . PRO   A 1 172 ? -9.77043  -22.68029 -37.12472 1.000 40.11714 ? 179 PRO   A CG  1 
ATOM   1264 C CD  . PRO   A 1 172 ? -10.08025 -23.58671 -35.97881 1.000 43.08503 ? 179 PRO   A CD  1 
ATOM   1265 N N   . MET   A 1 173 ? -8.74334  -19.63803 -33.72721 1.000 32.45925 ? 180 MET   A N   1 
ATOM   1266 C CA  . MET   A 1 173 ? -9.08005  -18.70407 -32.65974 1.000 33.40484 ? 180 MET   A CA  1 
ATOM   1267 C C   . MET   A 1 173 ? -9.86761  -17.49196 -33.13375 1.000 36.70500 ? 180 MET   A C   1 
ATOM   1268 O O   . MET   A 1 173 ? -10.54611 -16.85441 -32.31891 1.000 42.88945 ? 180 MET   A O   1 
ATOM   1269 C CB  . MET   A 1 173 ? -7.80395  -18.19925 -31.97646 1.000 28.91827 ? 180 MET   A CB  1 
ATOM   1270 C CG  . MET   A 1 173 ? -6.81000  -19.27035 -31.57041 1.000 54.79062 ? 180 MET   A CG  1 
ATOM   1271 S SD  . MET   A 1 173 ? -5.69586  -18.67473 -30.28618 1.000 52.67230 ? 180 MET   A SD  1 
ATOM   1272 C CE  . MET   A 1 173 ? -6.73357  -17.48883 -29.44547 1.000 38.69094 ? 180 MET   A CE  1 
ATOM   1273 N N   . GLY   A 1 174 ? -9.78567  -17.15040 -34.41534 1.000 29.60994 ? 181 GLY   A N   1 
ATOM   1274 C CA  . GLY   A 1 174 ? -10.28424 -15.87106 -34.87358 1.000 25.87543 ? 181 GLY   A CA  1 
ATOM   1275 C C   . GLY   A 1 174 ? -9.23833  -14.79392 -34.67332 1.000 23.31830 ? 181 GLY   A C   1 
ATOM   1276 O O   . GLY   A 1 174 ? -8.64215  -14.31182 -35.64123 1.000 28.42177 ? 181 GLY   A O   1 
ATOM   1277 N N   . ARG   A 1 175 ? -8.99357  -14.42574 -33.41630 1.000 23.94367 ? 182 ARG   A N   1 
ATOM   1278 C CA  . ARG   A 1 175 ? -7.99983  -13.41993 -33.06630 1.000 20.13343 ? 182 ARG   A CA  1 
ATOM   1279 C C   . ARG   A 1 175 ? -7.80870  -13.43281 -31.55866 1.000 21.56505 ? 182 ARG   A C   1 
ATOM   1280 O O   . ARG   A 1 175 ? -8.78246  -13.56363 -30.81369 1.000 22.15820 ? 182 ARG   A O   1 
ATOM   1281 C CB  . ARG   A 1 175 ? -8.43270  -12.01887 -33.52449 1.000 24.58384 ? 182 ARG   A CB  1 
ATOM   1282 C CG  . ARG   A 1 175 ? -7.36586  -10.94494 -33.34562 1.000 20.95908 ? 182 ARG   A CG  1 
ATOM   1283 C CD  . ARG   A 1 175 ? -7.96230  -9.54103  -33.24982 1.000 20.78794 ? 182 ARG   A CD  1 
ATOM   1284 N NE  . ARG   A 1 175 ? -8.91866  -9.40389  -32.15661 1.000 20.73609 ? 182 ARG   A NE  1 
ATOM   1285 C CZ  . ARG   A 1 175 ? -10.22670 -9.26116  -32.31637 1.000 21.91855 ? 182 ARG   A CZ  1 
ATOM   1286 N NH1 . ARG   A 1 175 ? -10.77729 -9.23086  -33.51915 1.000 23.08038 ? 182 ARG   A NH1 1 
ATOM   1287 N NH2 . ARG   A 1 175 ? -11.00179 -9.14376  -31.24221 1.000 22.12974 ? 182 ARG   A NH2 1 
ATOM   1288 N N   . GLY   A 1 176 ? -6.55651  -13.29954 -31.11434 1.000 21.59924 ? 183 GLY   A N   1 
ATOM   1289 C CA  . GLY   A 1 176 ? -6.28929  -13.15635 -29.70126 1.000 22.57556 ? 183 GLY   A CA  1 
ATOM   1290 C C   . GLY   A 1 176 ? -5.17573  -14.07463 -29.24332 1.000 25.84029 ? 183 GLY   A C   1 
ATOM   1291 O O   . GLY   A 1 176 ? -4.34921  -14.53545 -30.03889 1.000 22.41181 ? 183 GLY   A O   1 
ATOM   1292 N N   . THR   A 1 177 ? -5.15603  -14.33638 -27.93802 1.000 22.03154 ? 184 THR   A N   1 
ATOM   1293 C CA  . THR   A 1 177 ? -4.09906  -15.12020 -27.31914 1.000 24.01282 ? 184 THR   A CA  1 
ATOM   1294 C C   . THR   A 1 177 ? -4.69087  -16.04286 -26.26673 1.000 27.01288 ? 184 THR   A C   1 
ATOM   1295 O O   . THR   A 1 177 ? -5.57591  -15.64629 -25.50265 1.000 20.35816 ? 184 THR   A O   1 
ATOM   1296 C CB  . THR   A 1 177 ? -3.03361  -14.21885 -26.68393 1.000 22.28244 ? 184 THR   A CB  1 
ATOM   1297 O OG1 . THR   A 1 177 ? -2.40106  -13.43591 -27.70154 1.000 23.80598 ? 184 THR   A OG1 1 
ATOM   1298 C CG2 . THR   A 1 177 ? -1.98094  -15.04598 -25.94866 1.000 21.15496 ? 184 THR   A CG2 1 
ATOM   1299 N N   . LYS   A 1 178 ? -4.19112  -17.27524 -26.24169 1.000 20.70598 ? 185 LYS   A N   1 
ATOM   1300 C CA  . LYS   A 1 178 ? -4.56822  -18.28576 -25.26472 1.000 19.80404 ? 185 LYS   A CA  1 
ATOM   1301 C C   . LYS   A 1 178 ? -3.30450  -18.77327 -24.57142 1.000 24.13484 ? 185 LYS   A C   1 
ATOM   1302 O O   . LYS   A 1 178 ? -2.43140  -19.36351 -25.21544 1.000 20.82269 ? 185 LYS   A O   1 
ATOM   1303 C CB  . LYS   A 1 178 ? -5.30406  -19.43806 -25.94978 1.000 27.45068 ? 185 LYS   A CB  1 
ATOM   1304 C CG  . LYS   A 1 178 ? -5.78520  -20.51851 -25.02312 1.000 35.10572 ? 185 LYS   A CG  1 
ATOM   1305 C CD  . LYS   A 1 178 ? -6.29337  -21.72241 -25.80161 1.000 41.24298 ? 185 LYS   A CD  1 
ATOM   1306 C CE  . LYS   A 1 178 ? -7.16596  -21.28261 -26.96639 1.000 49.30164 ? 185 LYS   A CE  1 
ATOM   1307 N NZ  . LYS   A 1 178 ? -7.34280  -22.36900 -27.96651 1.000 68.13984 ? 185 LYS   A NZ  1 
ATOM   1308 N N   . VAL   A 1 179 ? -3.19927  -18.51427 -23.27078 1.000 20.23450 ? 186 VAL   A N   1 
ATOM   1309 C CA  . VAL   A 1 179 ? -2.06416  -18.96016 -22.46935 1.000 19.42664 ? 186 VAL   A CA  1 
ATOM   1310 C C   . VAL   A 1 179 ? -2.50160  -20.17757 -21.66901 1.000 22.59120 ? 186 VAL   A C   1 
ATOM   1311 O O   . VAL   A 1 179 ? -3.39980  -20.08418 -20.82423 1.000 22.50599 ? 186 VAL   A O   1 
ATOM   1312 C CB  . VAL   A 1 179 ? -1.54700  -17.84710 -21.54371 1.000 18.65614 ? 186 VAL   A CB  1 
ATOM   1313 C CG1 . VAL   A 1 179 ? -0.37114  -18.34954 -20.72736 1.000 16.66063 ? 186 VAL   A CG1 1 
ATOM   1314 C CG2 . VAL   A 1 179 ? -1.14310  -16.62548 -22.35025 1.000 23.04981 ? 186 VAL   A CG2 1 
ATOM   1315 N N   . ILE   A 1 180 ? -1.87264  -21.31792 -21.93298 1.000 17.23166 ? 187 ILE   A N   1 
ATOM   1316 C CA  . ILE   A 1 180 ? -2.20081  -22.57545 -21.27435 1.000 17.16576 ? 187 ILE   A CA  1 
ATOM   1317 C C   . ILE   A 1 180 ? -1.09986  -22.86855 -20.26774 1.000 22.74080 ? 187 ILE   A C   1 
ATOM   1318 O O   . ILE   A 1 180 ? 0.04810   -23.13154 -20.64406 1.000 20.51989 ? 187 ILE   A O   1 
ATOM   1319 C CB  . ILE   A 1 180 ? -2.35778  -23.72488 -22.27728 1.000 22.17967 ? 187 ILE   A CB  1 
ATOM   1320 C CG1 . ILE   A 1 180 ? -3.32792  -23.32903 -23.39190 1.000 19.84129 ? 187 ILE   A CG1 1 
ATOM   1321 C CG2 . ILE   A 1 180 ? -2.82822  -24.98999 -21.56835 1.000 22.96623 ? 187 ILE   A CG2 1 
ATOM   1322 C CD1 . ILE   A 1 180 ? -3.33949  -24.29110 -24.55947 1.000 25.96171 ? 187 ILE   A CD1 1 
ATOM   1323 N N   . LEU   A 1 181 ? -1.44763  -22.82211 -18.98751 1.000 20.30408 ? 188 LEU   A N   1 
ATOM   1324 C CA  . LEU   A 1 181 ? -0.50442  -23.08073 -17.90652 1.000 19.80923 ? 188 LEU   A CA  1 
ATOM   1325 C C   . LEU   A 1 181 ? -0.62456  -24.54219 -17.49425 1.000 23.79441 ? 188 LEU   A C   1 
ATOM   1326 O O   . LEU   A 1 181 ? -1.63644  -24.94433 -16.91401 1.000 20.60770 ? 188 LEU   A O   1 
ATOM   1327 C CB  . LEU   A 1 181 ? -0.78390  -22.15771 -16.72355 1.000 16.13039 ? 188 LEU   A CB  1 
ATOM   1328 C CG  . LEU   A 1 181 ? -0.77179  -20.67014 -17.05931 1.000 18.58440 ? 188 LEU   A CG  1 
ATOM   1329 C CD1 . LEU   A 1 181 ? -1.05457  -19.85949 -15.81546 1.000 22.35603 ? 188 LEU   A CD1 1 
ATOM   1330 C CD2 . LEU   A 1 181 ? 0.56891   -20.28598 -17.64398 1.000 17.00185 ? 188 LEU   A CD2 1 
ATOM   1331 N N   . HIS   A 1 182 ? 0.39842   -25.33837 -17.80163 1.000 20.99178 ? 189 HIS   A N   1 
ATOM   1332 C CA  . HIS   A 1 182 ? 0.47796   -26.71674 -17.31995 1.000 21.87660 ? 189 HIS   A CA  1 
ATOM   1333 C C   . HIS   A 1 182 ? 1.05100   -26.66667 -15.90884 1.000 25.05080 ? 189 HIS   A C   1 
ATOM   1334 O O   . HIS   A 1 182 ? 2.26028   -26.51995 -15.71861 1.000 22.86458 ? 189 HIS   A O   1 
ATOM   1335 C CB  . HIS   A 1 182 ? 1.32803   -27.56715 -18.25724 1.000 22.12952 ? 189 HIS   A CB  1 
ATOM   1336 C CG  . HIS   A 1 182 ? 0.88069   -27.51612 -19.68622 1.000 24.81840 ? 189 HIS   A CG  1 
ATOM   1337 N ND1 . HIS   A 1 182 ? 0.06501   -28.47544 -20.24671 1.000 30.03283 ? 189 HIS   A ND1 1 
ATOM   1338 C CD2 . HIS   A 1 182 ? 1.13817   -26.62040 -20.66938 1.000 25.76675 ? 189 HIS   A CD2 1 
ATOM   1339 C CE1 . HIS   A 1 182 ? -0.16665  -28.16875 -21.51101 1.000 29.87375 ? 189 HIS   A CE1 1 
ATOM   1340 N NE2 . HIS   A 1 182 ? 0.47524   -27.04919 -21.79337 1.000 28.42493 ? 189 HIS   A NE2 1 
ATOM   1341 N N   . LEU   A 1 183 ? 0.17728   -26.77983 -14.91186 1.000 22.84013 ? 190 LEU   A N   1 
ATOM   1342 C CA  . LEU   A 1 183 ? 0.54746   -26.42647 -13.54747 1.000 21.63195 ? 190 LEU   A CA  1 
ATOM   1343 C C   . LEU   A 1 183 ? 1.47358   -27.46074 -12.91985 1.000 27.79953 ? 190 LEU   A C   1 
ATOM   1344 O O   . LEU   A 1 183 ? 1.34776   -28.66617 -13.16037 1.000 28.70199 ? 190 LEU   A O   1 
ATOM   1345 C CB  . LEU   A 1 183 ? -0.70371  -26.26784 -12.68252 1.000 20.56536 ? 190 LEU   A CB  1 
ATOM   1346 C CG  . LEU   A 1 183 ? -1.63109  -25.09961 -13.02258 1.000 19.99676 ? 190 LEU   A CG  1 
ATOM   1347 C CD1 . LEU   A 1 183 ? -2.81395  -25.08675 -12.06818 1.000 24.97278 ? 190 LEU   A CD1 1 
ATOM   1348 C CD2 . LEU   A 1 183 ? -0.87240  -23.78097 -12.97833 1.000 24.25827 ? 190 LEU   A CD2 1 
ATOM   1349 N N   . LYS   A 1 184 ? 2.40197   -26.97327 -12.09618 1.000 25.02591 ? 191 LYS   A N   1 
ATOM   1350 C CA  . LYS   A 1 184 ? 3.21402   -27.85222 -11.26784 1.000 26.55046 ? 191 LYS   A CA  1 
ATOM   1351 C C   . LYS   A 1 184 ? 2.32531   -28.67450 -10.34262 1.000 30.26053 ? 191 LYS   A C   1 
ATOM   1352 O O   . LYS   A 1 184 ? 1.20270   -28.28216 -10.01211 1.000 30.18466 ? 191 LYS   A O   1 
ATOM   1353 C CB  . LYS   A 1 184 ? 4.21001   -27.04537 -10.43411 1.000 29.96867 ? 191 LYS   A CB  1 
ATOM   1354 C CG  . LYS   A 1 184 ? 5.26994   -26.29630 -11.22172 1.000 33.25083 ? 191 LYS   A CG  1 
ATOM   1355 C CD  . LYS   A 1 184 ? 6.08455   -25.41388 -10.28172 1.000 34.39321 ? 191 LYS   A CD  1 
ATOM   1356 C CE  . LYS   A 1 184 ? 7.28452   -24.79228 -10.96682 1.000 56.38101 ? 191 LYS   A CE  1 
ATOM   1357 N NZ  . LYS   A 1 184 ? 7.53873   -23.40346 -10.47938 1.000 47.85438 ? 191 LYS   A NZ  1 
ATOM   1358 N N   . GLU   A 1 185 ? 2.85686   -29.82033 -9.90780  1.000 29.94002 ? 192 GLU   A N   1 
ATOM   1359 C CA  . GLU   A 1 185 ? 2.08173   -30.76559 -9.10765  1.000 33.30929 ? 192 GLU   A CA  1 
ATOM   1360 C C   . GLU   A 1 185 ? 1.52318   -30.12634 -7.84027  1.000 39.70960 ? 192 GLU   A C   1 
ATOM   1361 O O   . GLU   A 1 185 ? 0.37986   -30.39464 -7.45364  1.000 36.19884 ? 192 GLU   A O   1 
ATOM   1362 C CB  . GLU   A 1 185 ? 2.95145   -31.97528 -8.75743  1.000 38.14551 ? 192 GLU   A CB  1 
ATOM   1363 C CG  . GLU   A 1 185 ? 2.27027   -33.01464 -7.88716  1.000 57.69744 ? 192 GLU   A CG  1 
ATOM   1364 C CD  . GLU   A 1 185 ? 2.86618   -34.39776 -8.06121  1.000 79.42362 ? 192 GLU   A CD  1 
ATOM   1365 O OE1 . GLU   A 1 185 ? 2.10873   -35.38766 -7.98322  1.000 84.69039 ? 192 GLU   A OE1 1 
ATOM   1366 O OE2 . GLU   A 1 185 ? 4.09092   -34.49412 -8.28935  1.000 87.82098 ? 192 GLU   A OE2 1 
ATOM   1367 N N   . ASP   A 1 186 ? 2.30898   -29.27740 -7.17900  1.000 32.81558 ? 193 ASP   A N   1 
ATOM   1368 C CA  . ASP   A 1 186 ? 1.90798   -28.69331 -5.90617  1.000 37.56230 ? 193 ASP   A CA  1 
ATOM   1369 C C   . ASP   A 1 186 ? 1.24086   -27.32942 -6.05923  1.000 33.39617 ? 193 ASP   A C   1 
ATOM   1370 O O   . ASP   A 1 186 ? 1.08933   -26.61226 -5.06334  1.000 31.10188 ? 193 ASP   A O   1 
ATOM   1371 C CB  . ASP   A 1 186 ? 3.11516   -28.57852 -4.97215  1.000 39.95737 ? 193 ASP   A CB  1 
ATOM   1372 C CG  . ASP   A 1 186 ? 4.21463   -27.70551 -5.54409  1.000 53.14169 ? 193 ASP   A CG  1 
ATOM   1373 O OD1 . ASP   A 1 186 ? 4.26384   -27.53575 -6.78124  1.000 49.89474 ? 193 ASP   A OD1 1 
ATOM   1374 O OD2 . ASP   A 1 186 ? 5.03069   -27.18471 -4.75481  1.000 49.42845 ? 193 ASP   A OD2 1 
ATOM   1375 N N   . GLN   A 1 187 ? 0.83243   -26.95717 -7.27480  1.000 25.06456 ? 194 GLN   A N   1 
ATOM   1376 C CA  . GLN   A 1 187 ? 0.21056   -25.66002 -7.51848  1.000 24.39157 ? 194 GLN   A CA  1 
ATOM   1377 C C   . GLN   A 1 187 ? -1.21844  -25.80036 -8.03480  1.000 30.06894 ? 194 GLN   A C   1 
ATOM   1378 O O   . GLN   A 1 187 ? -1.71299  -24.90991 -8.73521  1.000 28.42723 ? 194 GLN   A O   1 
ATOM   1379 C CB  . GLN   A 1 187 ? 1.05108   -24.83949 -8.50021  1.000 24.67913 ? 194 GLN   A CB  1 
ATOM   1380 C CG  . GLN   A 1 187 ? 2.45798   -24.52455 -8.00740  1.000 26.26597 ? 194 GLN   A CG  1 
ATOM   1381 C CD  . GLN   A 1 187 ? 2.47492   -23.81898 -6.66622  1.000 27.40356 ? 194 GLN   A CD  1 
ATOM   1382 O OE1 . GLN   A 1 187 ? 1.62032   -22.98148 -6.37930  1.000 29.97484 ? 194 GLN   A OE1 1 
ATOM   1383 N NE2 . GLN   A 1 187 ? 3.45230   -24.15879 -5.83322  1.000 30.04963 ? 194 GLN   A NE2 1 
ATOM   1384 N N   . THR   A 1 188 ? -1.89481  -26.90274 -7.70120  1.000 28.21724 ? 195 THR   A N   1 
ATOM   1385 C CA  . THR   A 1 188 ? -3.24541  -27.14445 -8.19763  1.000 26.92947 ? 195 THR   A CA  1 
ATOM   1386 C C   . THR   A 1 188 ? -4.29981  -26.28290 -7.51458  1.000 30.23672 ? 195 THR   A C   1 
ATOM   1387 O O   . THR   A 1 188 ? -5.46787  -26.34212 -7.91398  1.000 27.33915 ? 195 THR   A O   1 
ATOM   1388 C CB  . THR   A 1 188 ? -3.62046  -28.61911 -8.03168  1.000 33.36350 ? 195 THR   A CB  1 
ATOM   1389 O OG1 . THR   A 1 188 ? -3.48262  -28.99646 -6.65622  1.000 39.65378 ? 195 THR   A OG1 1 
ATOM   1390 C CG2 . THR   A 1 188 ? -2.72811  -29.50352 -8.89136  1.000 31.61462 ? 195 THR   A CG2 1 
ATOM   1391 N N   . GLU   A 1 189 ? -3.92810  -25.49340 -6.50156  1.000 25.87524 ? 196 GLU   A N   1 
ATOM   1392 C CA  . GLU   A 1 189 ? -4.89541  -24.59360 -5.87941  1.000 29.09545 ? 196 GLU   A CA  1 
ATOM   1393 C C   . GLU   A 1 189 ? -5.42794  -23.57173 -6.87455  1.000 28.80158 ? 196 GLU   A C   1 
ATOM   1394 O O   . GLU   A 1 189 ? -6.53457  -23.04906 -6.69854  1.000 27.23964 ? 196 GLU   A O   1 
ATOM   1395 C CB  . GLU   A 1 189 ? -4.26641  -23.88400 -4.67862  1.000 27.44090 ? 196 GLU   A CB  1 
ATOM   1396 C CG  . GLU   A 1 189 ? -3.24815  -22.81176 -5.04843  1.000 21.07309 ? 196 GLU   A CG  1 
ATOM   1397 C CD  . GLU   A 1 189 ? -2.46249  -22.30634 -3.85137  1.000 33.51621 ? 196 GLU   A CD  1 
ATOM   1398 O OE1 . GLU   A 1 189 ? -1.50499  -22.98904 -3.43212  1.000 41.09480 ? 196 GLU   A OE1 1 
ATOM   1399 O OE2 . GLU   A 1 189 ? -2.79905  -21.21862 -3.33647  1.000 31.38707 ? 196 GLU   A OE2 1 
ATOM   1400 N N   . TYR   A 1 190 ? -4.66565  -23.28213 -7.92449  1.000 23.15514 ? 197 TYR   A N   1 
ATOM   1401 C CA  . TYR   A 1 190 ? -5.07708  -22.32734 -8.94149  1.000 24.35509 ? 197 TYR   A CA  1 
ATOM   1402 C C   . TYR   A 1 190 ? -6.03019  -22.93416 -9.96268  1.000 26.39139 ? 197 TYR   A C   1 
ATOM   1403 O O   . TYR   A 1 190 ? -6.34608  -22.28464 -10.96506 1.000 29.18024 ? 197 TYR   A O   1 
ATOM   1404 C CB  . TYR   A 1 190 ? -3.83260  -21.73807 -9.60726  1.000 22.68344 ? 197 TYR   A CB  1 
ATOM   1405 C CG  . TYR   A 1 190 ? -2.95734  -21.06978 -8.57643  1.000 24.25588 ? 197 TYR   A CG  1 
ATOM   1406 C CD1 . TYR   A 1 190 ? -3.40543  -19.94902 -7.89411  1.000 24.93441 ? 197 TYR   A CD1 1 
ATOM   1407 C CD2 . TYR   A 1 190 ? -1.71469  -21.58970 -8.23856  1.000 21.95861 ? 197 TYR   A CD2 1 
ATOM   1408 C CE1 . TYR   A 1 190 ? -2.63058  -19.33956 -6.93127  1.000 25.94145 ? 197 TYR   A CE1 1 
ATOM   1409 C CE2 . TYR   A 1 190 ? -0.92755  -20.98293 -7.26884  1.000 24.32608 ? 197 TYR   A CE2 1 
ATOM   1410 C CZ  . TYR   A 1 190 ? -1.39440  -19.85731 -6.62109  1.000 27.62473 ? 197 TYR   A CZ  1 
ATOM   1411 O OH  . TYR   A 1 190 ? -0.62985  -19.24394 -5.65746  1.000 26.98929 ? 197 TYR   A OH  1 
ATOM   1412 N N   . LEU   A 1 191 ? -6.49491  -24.15895 -9.71975  1.000 25.98153 ? 198 LEU   A N   1 
ATOM   1413 C CA  . LEU   A 1 191 ? -7.62199  -24.72949 -10.44104 1.000 22.56900 ? 198 LEU   A CA  1 
ATOM   1414 C C   . LEU   A 1 191 ? -8.92596  -24.63203 -9.66071  1.000 28.23361 ? 198 LEU   A C   1 
ATOM   1415 O O   . LEU   A 1 191 ? -9.98444  -24.95085 -10.21249 1.000 28.26651 ? 198 LEU   A O   1 
ATOM   1416 C CB  . LEU   A 1 191 ? -7.35078  -26.19935 -10.78817 1.000 30.49072 ? 198 LEU   A CB  1 
ATOM   1417 C CG  . LEU   A 1 191 ? -6.12852  -26.47692 -11.66282 1.000 32.39727 ? 198 LEU   A CG  1 
ATOM   1418 C CD1 . LEU   A 1 191 ? -5.89496  -27.97363 -11.81775 1.000 35.90228 ? 198 LEU   A CD1 1 
ATOM   1419 C CD2 . LEU   A 1 191 ? -6.29891  -25.81300 -13.01742 1.000 32.81328 ? 198 LEU   A CD2 1 
ATOM   1420 N N   . GLU   A 1 192 ? -8.87927  -24.20213 -8.40090  1.000 24.23412 ? 199 GLU   A N   1 
ATOM   1421 C CA  . GLU   A 1 192 ? -10.07277 -24.11292 -7.56964  1.000 30.05800 ? 199 GLU   A CA  1 
ATOM   1422 C C   . GLU   A 1 192 ? -10.81007 -22.81137 -7.85413  1.000 25.63059 ? 199 GLU   A C   1 
ATOM   1423 O O   . GLU   A 1 192 ? -10.19413 -21.74220 -7.90666  1.000 25.58217 ? 199 GLU   A O   1 
ATOM   1424 C CB  . GLU   A 1 192 ? -9.71585  -24.19361 -6.08510  1.000 31.66712 ? 199 GLU   A CB  1 
ATOM   1425 C CG  . GLU   A 1 192 ? -9.18482  -25.54004 -5.63184  1.000 36.51150 ? 199 GLU   A CG  1 
ATOM   1426 C CD  . GLU   A 1 192 ? -8.48899  -25.46078 -4.28698  1.000 69.27952 ? 199 GLU   A CD  1 
ATOM   1427 O OE1 . GLU   A 1 192 ? -7.61389  -26.30908 -4.01507  1.000 64.27797 ? 199 GLU   A OE1 1 
ATOM   1428 O OE2 . GLU   A 1 192 ? -8.82405  -24.55192 -3.49566  1.000 65.74634 ? 199 GLU   A OE2 1 
ATOM   1429 N N   . GLU   A 1 193 ? -12.13245 -22.90700 -8.01669  1.000 27.78524 ? 200 GLU   A N   1 
ATOM   1430 C CA  . GLU   A 1 193 ? -12.93983 -21.73004 -8.32658  1.000 28.09105 ? 200 GLU   A CA  1 
ATOM   1431 C C   . GLU   A 1 193 ? -12.79490 -20.64974 -7.25978  1.000 27.79803 ? 200 GLU   A C   1 
ATOM   1432 O O   . GLU   A 1 193 ? -12.58273 -19.47402 -7.57752  1.000 22.72525 ? 200 GLU   A O   1 
ATOM   1433 C CB  . GLU   A 1 193 ? -14.40915 -22.12605 -8.48111  1.000 32.09372 ? 200 GLU   A CB  1 
ATOM   1434 C CG  . GLU   A 1 193 ? -15.31340 -20.96515 -8.86500  1.000 36.33239 ? 200 GLU   A CG  1 
ATOM   1435 C CD  . GLU   A 1 193 ? -16.78067 -21.34589 -8.89631  1.000 57.88852 ? 200 GLU   A CD  1 
ATOM   1436 O OE1 . GLU   A 1 193 ? -17.11666 -22.47701 -8.48538  1.000 61.02623 ? 200 GLU   A OE1 1 
ATOM   1437 O OE2 . GLU   A 1 193 ? -17.60125 -20.50939 -9.32724  1.000 57.11711 ? 200 GLU   A OE2 1 
ATOM   1438 N N   . ARG   A 1 194 ? -12.91601 -21.02951 -5.98319  1.000 24.89532 ? 201 ARG   A N   1 
ATOM   1439 C CA  . ARG   A 1 194 ? -12.86894 -20.03301 -4.91749  1.000 25.07686 ? 201 ARG   A CA  1 
ATOM   1440 C C   . ARG   A 1 194 ? -11.50432 -19.36166 -4.83363  1.000 24.87700 ? 201 ARG   A C   1 
ATOM   1441 O O   . ARG   A 1 194 ? -11.41131 -18.19366 -4.43964  1.000 23.09037 ? 201 ARG   A O   1 
ATOM   1442 C CB  . ARG   A 1 194 ? -13.22870 -20.66963 -3.57393  1.000 31.22343 ? 201 ARG   A CB  1 
ATOM   1443 C CG  . ARG   A 1 194 ? -12.24198 -21.71726 -3.08063  1.000 39.08228 ? 201 ARG   A CG  1 
ATOM   1444 C CD  . ARG   A 1 194 ? -12.80257 -22.48183 -1.88839  1.000 45.38109 ? 201 ARG   A CD  1 
ATOM   1445 N NE  . ARG   A 1 194 ? -11.82970 -23.40154 -1.31036  1.000 57.33397 ? 201 ARG   A NE  1 
ATOM   1446 C CZ  . ARG   A 1 194 ? -12.06599 -24.17542 -0.25899  1.000 45.94402 ? 201 ARG   A CZ  1 
ATOM   1447 N NH1 . ARG   A 1 194 ? -13.23431 -24.16126 0.36266   1.000 53.73614 ? 201 ARG   A NH1 1 
ATOM   1448 N NH2 . ARG   A 1 194 ? -11.10177 -24.97389 0.18899   1.000 64.20856 ? 201 ARG   A NH2 1 
ATOM   1449 N N   . ARG   A 1 195 ? -10.43693 -20.07545 -5.19880  1.000 24.08043 ? 202 ARG   A N   1 
ATOM   1450 C CA  . ARG   A 1 195 ? -9.10589  -19.47773 -5.15750  1.000 21.39381 ? 202 ARG   A CA  1 
ATOM   1451 C C   . ARG   A 1 195 ? -8.90502  -18.49328 -6.30380  1.000 26.50262 ? 202 ARG   A C   1 
ATOM   1452 O O   . ARG   A 1 195 ? -8.37785  -17.39342 -6.09886  1.000 22.66424 ? 202 ARG   A O   1 
ATOM   1453 C CB  . ARG   A 1 195 ? -8.03673  -20.57069 -5.18955  1.000 26.67612 ? 202 ARG   A CB  1 
ATOM   1454 C CG  . ARG   A 1 195 ? -6.60714  -20.04496 -5.19172  1.000 23.70558 ? 202 ARG   A CG  1 
ATOM   1455 C CD  . ARG   A 1 195 ? -6.23298  -19.39354 -3.86721  1.000 28.23170 ? 202 ARG   A CD  1 
ATOM   1456 N NE  . ARG   A 1 195 ? -4.79432  -19.17559 -3.76671  1.000 28.93428 ? 202 ARG   A NE  1 
ATOM   1457 C CZ  . ARG   A 1 195 ? -4.22773  -18.00456 -3.50778  1.000 28.39905 ? 202 ARG   A CZ  1 
ATOM   1458 N NH1 . ARG   A 1 195 ? -4.95166  -16.92000 -3.28470  1.000 25.15784 ? 202 ARG   A NH1 1 
ATOM   1459 N NH2 . ARG   A 1 195 ? -2.90091  -17.91976 -3.47022  1.000 28.96234 ? 202 ARG   A NH2 1 
ATOM   1460 N N   . ILE   A 1 196 ? -9.31720  -18.86771 -7.51772  1.000 22.44642 ? 203 ILE   A N   1 
ATOM   1461 C CA  . ILE   A 1 196 ? -9.21009  -17.95054 -8.65024  1.000 19.16701 ? 203 ILE   A CA  1 
ATOM   1462 C C   . ILE   A 1 196 ? -10.06769 -16.71357 -8.41298  1.000 20.52068 ? 203 ILE   A C   1 
ATOM   1463 O O   . ILE   A 1 196 ? -9.64403  -15.58367 -8.68332  1.000 21.72449 ? 203 ILE   A O   1 
ATOM   1464 C CB  . ILE   A 1 196 ? -9.59721  -18.66049 -9.96193  1.000 18.65431 ? 203 ILE   A CB  1 
ATOM   1465 C CG1 . ILE   A 1 196 ? -8.64906  -19.82674 -10.25480 1.000 21.67556 ? 203 ILE   A CG1 1 
ATOM   1466 C CG2 . ILE   A 1 196 ? -9.58566  -17.67433 -11.12295 1.000 20.42069 ? 203 ILE   A CG2 1 
ATOM   1467 C CD1 . ILE   A 1 196 ? -9.24602  -20.86093 -11.19129 1.000 25.86777 ? 203 ILE   A CD1 1 
ATOM   1468 N N   . LYS   A 1 197 ? -11.28732 -16.91032 -7.90555  1.000 22.06525 ? 204 LYS   A N   1 
ATOM   1469 C CA  . LYS   A 1 197 ? -12.17505 -15.78964 -7.60673  1.000 21.50615 ? 204 LYS   A CA  1 
ATOM   1470 C C   . LYS   A 1 197 ? -11.52163 -14.82048 -6.63372  1.000 23.21740 ? 204 LYS   A C   1 
ATOM   1471 O O   . LYS   A 1 197 ? -11.57393 -13.59923 -6.82202  1.000 22.13594 ? 204 LYS   A O   1 
ATOM   1472 C CB  . LYS   A 1 197 ? -13.49125 -16.31158 -7.02818  1.000 28.21861 ? 204 LYS   A CB  1 
ATOM   1473 C CG  . LYS   A 1 197 ? -14.72326 -15.53940 -7.45599  1.000 49.52165 ? 204 LYS   A CG  1 
ATOM   1474 C CD  . LYS   A 1 197 ? -15.98154 -16.17984 -6.89675  1.000 46.18747 ? 204 LYS   A CD  1 
ATOM   1475 C CE  . LYS   A 1 197 ? -16.16674 -17.58893 -7.43020  1.000 47.18204 ? 204 LYS   A CE  1 
ATOM   1476 N NZ  . LYS   A 1 197 ? -17.52471 -17.78271 -8.00781  1.000 56.25344 ? 204 LYS   A NZ  1 
ATOM   1477 N N   . GLU   A 1 198 ? -10.90320 -15.35806 -5.57965  1.000 21.31984 ? 205 GLU   A N   1 
ATOM   1478 C CA  . GLU   A 1 198 ? -10.23220 -14.52587 -4.58788  1.000 21.06043 ? 205 GLU   A CA  1 
ATOM   1479 C C   . GLU   A 1 198 ? -9.10630  -13.71190 -5.21641  1.000 24.28365 ? 205 GLU   A C   1 
ATOM   1480 O O   . GLU   A 1 198 ? -8.93184  -12.52939 -4.89794  1.000 23.76302 ? 205 GLU   A O   1 
ATOM   1481 C CB  . GLU   A 1 198 ? -9.70654  -15.41613 -3.46092  1.000 21.25451 ? 205 GLU   A CB  1 
ATOM   1482 C CG  . GLU   A 1 198 ? -8.83446  -14.73344 -2.42725  1.000 24.25007 ? 205 GLU   A CG  1 
ATOM   1483 C CD  . GLU   A 1 198 ? -8.18095  -15.74023 -1.50336  1.000 27.52822 ? 205 GLU   A CD  1 
ATOM   1484 O OE1 . GLU   A 1 198 ? -7.58198  -16.70627 -2.02200  1.000 29.13142 ? 205 GLU   A OE1 1 
ATOM   1485 O OE2 . GLU   A 1 198 ? -8.28239  -15.58308 -0.26694  1.000 27.95776 ? 205 GLU   A OE2 1 
ATOM   1486 N N   . ILE   A 1 199 ? -8.34680  -14.32016 -6.12987  1.000 19.17685 ? 206 ILE   A N   1 
ATOM   1487 C CA  . ILE   A 1 199 ? -7.20680  -13.63293 -6.73004  1.000 19.05545 ? 206 ILE   A CA  1 
ATOM   1488 C C   . ILE   A 1 199 ? -7.67517  -12.53676 -7.68029  1.000 22.29973 ? 206 ILE   A C   1 
ATOM   1489 O O   . ILE   A 1 199 ? -7.12054  -11.43068 -7.69503  1.000 24.19134 ? 206 ILE   A O   1 
ATOM   1490 C CB  . ILE   A 1 199 ? -6.29815  -14.65157 -7.44105  1.000 22.14209 ? 206 ILE   A CB  1 
ATOM   1491 C CG1 . ILE   A 1 199 ? -5.69138  -15.62536 -6.42725  1.000 24.99232 ? 206 ILE   A CG1 1 
ATOM   1492 C CG2 . ILE   A 1 199 ? -5.20536  -13.94493 -8.23811  1.000 23.07027 ? 206 ILE   A CG2 1 
ATOM   1493 C CD1 . ILE   A 1 199 ? -5.05434  -16.83546 -7.06491  1.000 25.65511 ? 206 ILE   A CD1 1 
ATOM   1494 N N   . VAL   A 1 200 ? -8.69921  -12.82232 -8.48898  1.000 20.55462 ? 207 VAL   A N   1 
ATOM   1495 C CA  . VAL   A 1 200 ? -9.21012  -11.81986 -9.42226  1.000 21.51367 ? 207 VAL   A CA  1 
ATOM   1496 C C   . VAL   A 1 200 ? -9.78457  -10.62839 -8.66465  1.000 24.75169 ? 207 VAL   A C   1 
ATOM   1497 O O   . VAL   A 1 200 ? -9.55668  -9.46748  -9.03333  1.000 24.25320 ? 207 VAL   A O   1 
ATOM   1498 C CB  . VAL   A 1 200 ? -10.25137 -12.45069 -10.36571 1.000 23.10656 ? 207 VAL   A CB  1 
ATOM   1499 C CG1 . VAL   A 1 200 ? -10.97762 -11.37174 -11.16403 1.000 21.97569 ? 207 VAL   A CG1 1 
ATOM   1500 C CG2 . VAL   A 1 200 ? -9.58095  -13.45048 -11.29775 1.000 20.47849 ? 207 VAL   A CG2 1 
ATOM   1501 N N   . LYS   A 1 201 ? -10.52246 -10.89643 -7.58371  1.000 23.23328 ? 208 LYS   A N   1 
ATOM   1502 C CA  . LYS   A 1 201 ? -11.09857 -9.81849  -6.78571  1.000 25.01913 ? 208 LYS   A CA  1 
ATOM   1503 C C   . LYS   A 1 201 ? -10.01384 -8.97595  -6.12383  1.000 27.10503 ? 208 LYS   A C   1 
ATOM   1504 O O   . LYS   A 1 201 ? -10.15496 -7.75407  -5.99261  1.000 28.38251 ? 208 LYS   A O   1 
ATOM   1505 C CB  . LYS   A 1 201 ? -12.03784 -10.40734 -5.73493  1.000 25.72014 ? 208 LYS   A CB  1 
ATOM   1506 C CG  . LYS   A 1 201 ? -12.70523 -9.38187  -4.83070  1.000 33.73653 ? 208 LYS   A CG  1 
ATOM   1507 C CD  . LYS   A 1 201 ? -13.73836 -10.04254 -3.92970  1.000 47.02707 ? 208 LYS   A CD  1 
ATOM   1508 C CE  . LYS   A 1 201 ? -14.42861 -9.02421  -3.03557  1.000 55.83364 ? 208 LYS   A CE  1 
ATOM   1509 N NZ  . LYS   A 1 201 ? -15.84243 -8.80534  -3.44902  1.000 59.55668 ? 208 LYS   A NZ  1 
ATOM   1510 N N   . LYS   A 1 202 ? -8.91776  -9.61190  -5.71295  1.000 24.62740 ? 209 LYS   A N   1 
ATOM   1511 C CA  . LYS   A 1 202 ? -7.86158  -8.91725  -4.98560  1.000 27.56265 ? 209 LYS   A CA  1 
ATOM   1512 C C   . LYS   A 1 202 ? -6.98493  -8.07769  -5.90860  1.000 29.00984 ? 209 LYS   A C   1 
ATOM   1513 O O   . LYS   A 1 202 ? -6.57325  -6.97198  -5.53968  1.000 29.20536 ? 209 LYS   A O   1 
ATOM   1514 C CB  . LYS   A 1 202 ? -7.00929  -9.93818  -4.23068  1.000 25.67569 ? 209 LYS   A CB  1 
ATOM   1515 C CG  . LYS   A 1 202 ? -5.80062  -9.36570  -3.51003  1.000 34.68567 ? 209 LYS   A CG  1 
ATOM   1516 C CD  . LYS   A 1 202 ? -5.33377  -10.31081 -2.41385  1.000 44.24632 ? 209 LYS   A CD  1 
ATOM   1517 C CE  . LYS   A 1 202 ? -3.85267  -10.13313 -2.11337  1.000 54.16811 ? 209 LYS   A CE  1 
ATOM   1518 N NZ  . LYS   A 1 202 ? -3.32933  -11.24346 -1.26687  1.000 49.42116 ? 209 LYS   A NZ  1 
ATOM   1519 N N   . HIS   A 1 203 ? -6.69509  -8.57976  -7.11151  1.000 23.51576 ? 210 HIS   A N   1 
ATOM   1520 C CA  . HIS   A 1 203 ? -5.65550  -8.01186  -7.95661  1.000 28.50393 ? 210 HIS   A CA  1 
ATOM   1521 C C   . HIS   A 1 203 ? -6.15159  -7.45621  -9.28240  1.000 25.95803 ? 210 HIS   A C   1 
ATOM   1522 O O   . HIS   A 1 203 ? -5.42615  -6.67567  -9.90737  1.000 30.35064 ? 210 HIS   A O   1 
ATOM   1523 C CB  . HIS   A 1 203 ? -4.58176  -9.07164  -8.25114  1.000 26.36269 ? 210 HIS   A CB  1 
ATOM   1524 C CG  . HIS   A 1 203 ? -3.77583  -9.46047  -7.05126  1.000 30.98297 ? 210 HIS   A CG  1 
ATOM   1525 N ND1 . HIS   A 1 203 ? -3.07001  -8.54740  -6.29864  1.000 35.97344 ? 210 HIS   A ND1 1 
ATOM   1526 C CD2 . HIS   A 1 203 ? -3.58115  -10.66482 -6.46233  1.000 32.59385 ? 210 HIS   A CD2 1 
ATOM   1527 C CE1 . HIS   A 1 203 ? -2.46497  -9.17412  -5.30486  1.000 37.43923 ? 210 HIS   A CE1 1 
ATOM   1528 N NE2 . HIS   A 1 203 ? -2.75986  -10.45944 -5.38077  1.000 33.51874 ? 210 HIS   A NE2 1 
ATOM   1529 N N   . SER   A 1 204 ? -7.35285  -7.82424  -9.72768  1.000 25.44182 ? 211 SER   A N   1 
ATOM   1530 C CA  . SER   A 1 204 ? -7.82545  -7.48597  -11.06547 1.000 23.30975 ? 211 SER   A CA  1 
ATOM   1531 C C   . SER   A 1 204 ? -9.25292  -6.95400  -11.03081 1.000 23.67548 ? 211 SER   A C   1 
ATOM   1532 O O   . SER   A 1 204 ? -10.01574 -7.14484  -11.98189 1.000 29.91850 ? 211 SER   A O   1 
ATOM   1533 C CB  . SER   A 1 204 ? -7.73423  -8.70063  -11.98908 1.000 29.04676 ? 211 SER   A CB  1 
ATOM   1534 O OG  . SER   A 1 204 ? -6.41717  -9.22792  -12.00182 1.000 29.64634 ? 211 SER   A OG  1 
ATOM   1535 N N   . GLN   A 1 205 ? -9.62166  -6.26829  -9.94685  1.000 30.54151 ? 212 GLN   A N   1 
ATOM   1536 C CA  . GLN   A 1 205 ? -11.02465 -5.93489  -9.72500  1.000 41.39766 ? 212 GLN   A CA  1 
ATOM   1537 C C   . GLN   A 1 205 ? -11.54101 -4.91093  -10.73195 1.000 37.92144 ? 212 GLN   A C   1 
ATOM   1538 O O   . GLN   A 1 205 ? -12.73963 -4.89776  -11.03504 1.000 36.92983 ? 212 GLN   A O   1 
ATOM   1539 C CB  . GLN   A 1 205 ? -11.21613 -5.42982  -8.29161  1.000 41.93597 ? 212 GLN   A CB  1 
ATOM   1540 C CG  . GLN   A 1 205 ? -12.65480 -5.09611  -7.92173  1.000 54.75350 ? 212 GLN   A CG  1 
ATOM   1541 C CD  . GLN   A 1 205 ? -12.76131 -4.29841  -6.63580  1.000 64.34447 ? 212 GLN   A CD  1 
ATOM   1542 O OE1 . GLN   A 1 205 ? -11.77592 -3.73796  -6.15525  1.000 57.62538 ? 212 GLN   A OE1 1 
ATOM   1543 N NE2 . GLN   A 1 205 ? -13.96213 -4.24639  -6.06943  1.000 63.31002 ? 212 GLN   A NE2 1 
ATOM   1544 N N   . PHE   A 1 206 ? -10.66630 -4.06390  -11.27878 1.000 36.70085 ? 213 PHE   A N   1 
ATOM   1545 C CA  . PHE   A 1 206 ? -11.10144 -2.95735  -12.12420 1.000 35.09905 ? 213 PHE   A CA  1 
ATOM   1546 C C   . PHE   A 1 206 ? -10.65315 -3.10002  -13.57608 1.000 32.49978 ? 213 PHE   A C   1 
ATOM   1547 O O   . PHE   A 1 206 ? -10.57637 -2.10016  -14.29558 1.000 37.10885 ? 213 PHE   A O   1 
ATOM   1548 C CB  . PHE   A 1 206 ? -10.61250 -1.63025  -11.54610 1.000 35.02785 ? 213 PHE   A CB  1 
ATOM   1549 C CG  . PHE   A 1 206 ? -11.14910 -1.34389  -10.17570 1.000 38.23386 ? 213 PHE   A CG  1 
ATOM   1550 C CD1 . PHE   A 1 206 ? -10.30071 -1.28956  -9.08423  1.000 45.18748 ? 213 PHE   A CD1 1 
ATOM   1551 C CD2 . PHE   A 1 206 ? -12.50770 -1.16845  -9.97081  1.000 40.71753 ? 213 PHE   A CD2 1 
ATOM   1552 C CE1 . PHE   A 1 206 ? -10.79305 -1.03804  -7.81598  1.000 51.37182 ? 213 PHE   A CE1 1 
ATOM   1553 C CE2 . PHE   A 1 206 ? -13.00589 -0.92228  -8.70515  1.000 55.74853 ? 213 PHE   A CE2 1 
ATOM   1554 C CZ  . PHE   A 1 206 ? -12.14721 -0.85547  -7.62757  1.000 49.81063 ? 213 PHE   A CZ  1 
ATOM   1555 N N   . ILE   A 1 207 ? -10.36107 -4.32152  -14.02665 1.000 25.73205 ? 214 ILE   A N   1 
ATOM   1556 C CA  . ILE   A 1 207 ? -10.08514 -4.53553  -15.44176 1.000 24.93869 ? 214 ILE   A CA  1 
ATOM   1557 C C   . ILE   A 1 207 ? -11.32541 -4.18445  -16.25445 1.000 31.28225 ? 214 ILE   A C   1 
ATOM   1558 O O   . ILE   A 1 207 ? -12.45140 -4.55887  -15.90217 1.000 28.38858 ? 214 ILE   A O   1 
ATOM   1559 C CB  . ILE   A 1 207 ? -9.63551  -5.98527  -15.68764 1.000 26.55960 ? 214 ILE   A CB  1 
ATOM   1560 C CG1 . ILE   A 1 207 ? -8.27584  -6.23638  -15.03116 1.000 30.14748 ? 214 ILE   A CG1 1 
ATOM   1561 C CG2 . ILE   A 1 207 ? -9.56977  -6.28033  -17.17423 1.000 24.88952 ? 214 ILE   A CG2 1 
ATOM   1562 C CD1 . ILE   A 1 207 ? -7.12910  -5.47283  -15.67435 1.000 27.69161 ? 214 ILE   A CD1 1 
ATOM   1563 N N   . GLY   A 1 208 ? -11.12384 -3.44704  -17.34580 1.000 26.91704 ? 215 GLY   A N   1 
ATOM   1564 C CA  . GLY   A 1 208 ? -12.23295 -2.91784  -18.11795 1.000 28.84734 ? 215 GLY   A CA  1 
ATOM   1565 C C   . GLY   A 1 208 ? -12.79573 -3.85181  -19.17002 1.000 26.06121 ? 215 GLY   A C   1 
ATOM   1566 O O   . GLY   A 1 208 ? -13.25255 -3.40262  -20.22528 1.000 28.45130 ? 215 GLY   A O   1 
ATOM   1567 N N   . TYR   A 1 209 ? -12.77723 -5.15211  -18.89298 1.000 24.34184 ? 216 TYR   A N   1 
ATOM   1568 C CA  . TYR   A 1 209 ? -13.28458 -6.16024  -19.81277 1.000 26.60750 ? 216 TYR   A CA  1 
ATOM   1569 C C   . TYR   A 1 209 ? -13.92774 -7.26425  -18.98860 1.000 24.01598 ? 216 TYR   A C   1 
ATOM   1570 O O   . TYR   A 1 209 ? -13.48362 -7.53353  -17.87016 1.000 26.41687 ? 216 TYR   A O   1 
ATOM   1571 C CB  . TYR   A 1 209 ? -12.16570 -6.73650  -20.69362 1.000 20.42203 ? 216 TYR   A CB  1 
ATOM   1572 C CG  . TYR   A 1 209 ? -11.52955 -5.70710  -21.59608 1.000 24.38327 ? 216 TYR   A CG  1 
ATOM   1573 C CD1 . TYR   A 1 209 ? -12.15955 -5.29114  -22.76097 1.000 23.58979 ? 216 TYR   A CD1 1 
ATOM   1574 C CD2 . TYR   A 1 209 ? -10.31328 -5.12466  -21.26460 1.000 21.38738 ? 216 TYR   A CD2 1 
ATOM   1575 C CE1 . TYR   A 1 209 ? -11.58360 -4.34005  -23.58425 1.000 27.43858 ? 216 TYR   A CE1 1 
ATOM   1576 C CE2 . TYR   A 1 209 ? -9.73315  -4.17251  -22.07705 1.000 21.66527 ? 216 TYR   A CE2 1 
ATOM   1577 C CZ  . TYR   A 1 209 ? -10.37121 -3.78211  -23.23413 1.000 24.23295 ? 216 TYR   A CZ  1 
ATOM   1578 O OH  . TYR   A 1 209 ? -9.79230  -2.83468  -24.04463 1.000 27.03822 ? 216 TYR   A OH  1 
ATOM   1579 N N   . PRO   A 1 210 ? -14.97680 -7.90182  -19.50636 1.000 25.70147 ? 217 PRO   A N   1 
ATOM   1580 C CA  . PRO   A 1 210 ? -15.59058 -9.00777  -18.75792 1.000 27.43861 ? 217 PRO   A CA  1 
ATOM   1581 C C   . PRO   A 1 210 ? -14.62419 -10.17197 -18.60354 1.000 24.87068 ? 217 PRO   A C   1 
ATOM   1582 O O   . PRO   A 1 210 ? -14.09021 -10.69783 -19.58223 1.000 24.49211 ? 217 PRO   A O   1 
ATOM   1583 C CB  . PRO   A 1 210 ? -16.80730 -9.38459  -19.61388 1.000 27.15894 ? 217 PRO   A CB  1 
ATOM   1584 C CG  . PRO   A 1 210 ? -16.50779 -8.85404  -20.97725 1.000 26.40105 ? 217 PRO   A CG  1 
ATOM   1585 C CD  . PRO   A 1 210 ? -15.66667 -7.63051  -20.77546 1.000 23.75605 ? 217 PRO   A CD  1 
ATOM   1586 N N   . ILE   A 1 211 ? -14.38829 -10.55783 -17.35442 1.000 22.68750 ? 218 ILE   A N   1 
ATOM   1587 C CA  . ILE   A 1 211 ? -13.58689 -11.72609 -17.01380 1.000 20.47116 ? 218 ILE   A CA  1 
ATOM   1588 C C   . ILE   A 1 211 ? -14.55529 -12.81883 -16.58789 1.000 26.74643 ? 218 ILE   A C   1 
ATOM   1589 O O   . ILE   A 1 211 ? -15.20677 -12.70970 -15.54198 1.000 25.42977 ? 218 ILE   A O   1 
ATOM   1590 C CB  . ILE   A 1 211 ? -12.56931 -11.42303 -15.90557 1.000 24.91613 ? 218 ILE   A CB  1 
ATOM   1591 C CG1 . ILE   A 1 211 ? -11.66818 -10.25256 -16.30547 1.000 24.40112 ? 218 ILE   A CG1 1 
ATOM   1592 C CG2 . ILE   A 1 211 ? -11.74585 -12.66276 -15.58012 1.000 24.32701 ? 218 ILE   A CG2 1 
ATOM   1593 C CD1 . ILE   A 1 211 ? -10.59503 -9.93773  -15.28278 1.000 21.85586 ? 218 ILE   A CD1 1 
ATOM   1594 N N   . THR   A 1 212 ? -14.66772 -13.86614 -17.39731 1.000 22.37244 ? 219 THR   A N   1 
ATOM   1595 C CA  . THR   A 1 212 ? -15.54508 -14.98835 -17.09407 1.000 21.73287 ? 219 THR   A CA  1 
ATOM   1596 C C   . THR   A 1 212 ? -14.70611 -16.14309 -16.56869 1.000 21.52098 ? 219 THR   A C   1 
ATOM   1597 O O   . THR   A 1 212 ? -13.82403 -16.64484 -17.27213 1.000 20.18792 ? 219 THR   A O   1 
ATOM   1598 C CB  . THR   A 1 212 ? -16.33769 -15.42643 -18.32477 1.000 24.05916 ? 219 THR   A CB  1 
ATOM   1599 O OG1 . THR   A 1 212 ? -17.07445 -14.31070 -18.84295 1.000 24.56517 ? 219 THR   A OG1 1 
ATOM   1600 C CG2 . THR   A 1 212 ? -17.30705 -16.54619 -17.95926 1.000 18.87230 ? 219 THR   A CG2 1 
ATOM   1601 N N   . LEU   A 1 213 ? -14.97499 -16.55633 -15.33573 1.000 20.76255 ? 220 LEU   A N   1 
ATOM   1602 C CA  . LEU   A 1 213 ? -14.31738 -17.71890 -14.75268 1.000 19.73112 ? 220 LEU   A CA  1 
ATOM   1603 C C   . LEU   A 1 213 ? -15.17501 -18.94741 -15.03789 1.000 24.18266 ? 220 LEU   A C   1 
ATOM   1604 O O   . LEU   A 1 213 ? -16.25069 -19.11570 -14.45086 1.000 23.09001 ? 220 LEU   A O   1 
ATOM   1605 C CB  . LEU   A 1 213 ? -14.09561 -17.52691 -13.25468 1.000 24.17622 ? 220 LEU   A CB  1 
ATOM   1606 C CG  . LEU   A 1 213 ? -13.61133 -18.75428 -12.48481 1.000 28.21219 ? 220 LEU   A CG  1 
ATOM   1607 C CD1 . LEU   A 1 213 ? -12.30787 -19.26852 -13.06914 1.000 27.60287 ? 220 LEU   A CD1 1 
ATOM   1608 C CD2 . LEU   A 1 213 ? -13.44542 -18.42674 -11.00308 1.000 29.56112 ? 220 LEU   A CD2 1 
ATOM   1609 N N   . PHE   A 1 214 ? -14.70699 -19.79259 -15.95328 1.000 21.19329 ? 221 PHE   A N   1 
ATOM   1610 C CA  . PHE   A 1 214 ? -15.40274 -21.03250 -16.25909 1.000 22.07637 ? 221 PHE   A CA  1 
ATOM   1611 C C   . PHE   A 1 214 ? -15.35228 -21.97533 -15.06132 1.000 25.66410 ? 221 PHE   A C   1 
ATOM   1612 O O   . PHE   A 1 214 ? -14.39454 -21.97704 -14.28237 1.000 24.87094 ? 221 PHE   A O   1 
ATOM   1613 C CB  . PHE   A 1 214 ? -14.77783 -21.72183 -17.47550 1.000 20.31590 ? 221 PHE   A CB  1 
ATOM   1614 C CG  . PHE   A 1 214 ? -15.12146 -21.08552 -18.80375 1.000 20.76374 ? 221 PHE   A CG  1 
ATOM   1615 C CD1 . PHE   A 1 214 ? -15.24605 -19.71132 -18.93862 1.000 21.51951 ? 221 PHE   A CD1 1 
ATOM   1616 C CD2 . PHE   A 1 214 ? -15.30136 -21.87737 -19.92629 1.000 24.94337 ? 221 PHE   A CD2 1 
ATOM   1617 C CE1 . PHE   A 1 214 ? -15.55215 -19.14154 -20.16637 1.000 22.16470 ? 221 PHE   A CE1 1 
ATOM   1618 C CE2 . PHE   A 1 214 ? -15.60759 -21.31678 -21.15420 1.000 23.74320 ? 221 PHE   A CE2 1 
ATOM   1619 C CZ  . PHE   A 1 214 ? -15.73356 -19.94597 -21.27414 1.000 19.50062 ? 221 PHE   A CZ  1 
ATOM   1620 N N   . VAL   A 1 215 ? -16.39313 -22.79091 -14.92507 1.000 23.41920 ? 222 VAL   A N   1 
ATOM   1621 C CA  . VAL   A 1 215 ? -16.45947 -23.81152 -13.88675 1.000 25.84068 ? 222 VAL   A CA  1 
ATOM   1622 C C   . VAL   A 1 215 ? -16.36002 -25.17259 -14.56481 1.000 28.50982 ? 222 VAL   A C   1 
ATOM   1623 O O   . VAL   A 1 215 ? -16.68898 -25.32490 -15.74615 1.000 31.57469 ? 222 VAL   A O   1 
ATOM   1624 C CB  . VAL   A 1 215 ? -17.75044 -23.66844 -13.04393 1.000 33.28717 ? 222 VAL   A CB  1 
ATOM   1625 C CG1 . VAL   A 1 215 ? -18.94201 -23.44793 -13.93885 1.000 35.53390 ? 222 VAL   A CG1 1 
ATOM   1626 C CG2 . VAL   A 1 215 ? -17.97382 -24.85263 -12.09140 1.000 37.85509 ? 222 VAL   A CG2 1 
ATOM   1627 N N   . GLU   A 1 216 ? -15.88367 -26.16005 -13.81384 1.000 31.98355 ? 223 GLU   A N   1 
ATOM   1628 C CA  . GLU   A 1 216 ? -15.60343 -27.49697 -14.31126 1.000 41.62244 ? 223 GLU   A CA  1 
ATOM   1629 C C   . GLU   A 1 216 ? -16.74688 -28.47519 -14.07137 1.000 42.20897 ? 223 GLU   A C   1 
ATOM   1630 O O   . GLU   A 1 216 ? -17.79153 -28.15318 -13.50299 1.000 54.56073 ? 223 GLU   A O   1 
ATOM   1631 C CB  . GLU   A 1 216 ? -14.33052 -28.03257 -13.66521 1.000 48.06053 ? 223 GLU   A CB  1 
ATOM   1632 C CG  . GLU   A 1 216 ? -13.10452 -27.26078 -14.05512 1.000 55.25656 ? 223 GLU   A CG  1 
ATOM   1633 C CD  . GLU   A 1 216 ? -11.83887 -28.04031 -13.80141 1.000 56.85845 ? 223 GLU   A CD  1 
ATOM   1634 O OE1 . GLU   A 1 216 ? -11.07597 -27.60933 -12.91578 1.000 67.55650 ? 223 GLU   A OE1 1 
ATOM   1635 O OE2 . GLU   A 1 216 ? -11.64608 -29.11352 -14.41490 1.000 67.30168 ? 223 GLU   A OE2 1 
ATOM   1636 N N   . LYS   A 1 217 ? -16.50756 -29.70008 -14.51860 1.000 68.38916 ? 224 LYS   A N   1 
ATOM   1637 C CA  . LYS   A 1 217 ? -17.43242 -30.81692 -14.41590 1.000 57.43806 ? 224 LYS   A CA  1 
ATOM   1638 C C   . LYS   A 1 217 ? -17.49049 -31.40781 -13.01578 1.000 73.17795 ? 224 LYS   A C   1 
ATOM   1639 O O   . LYS   A 1 217 ? -16.47511 -31.53640 -12.35072 1.000 83.66119 ? 224 LYS   A O   1 
ATOM   1640 C CB  . LYS   A 1 217 ? -17.03609 -31.86241 -15.47479 1.000 71.00444 ? 224 LYS   A CB  1 
ATOM   1641 C CG  . LYS   A 1 217 ? -15.94097 -32.89296 -15.12684 1.000 78.15422 ? 224 LYS   A CG  1 
ATOM   1642 C CD  . LYS   A 1 217 ? -16.36777 -34.04185 -14.23231 1.000 71.23377 ? 224 LYS   A CD  1 
ATOM   1643 C CE  . LYS   A 1 217 ? -15.24295 -35.06626 -14.10122 1.000 84.16483 ? 224 LYS   A CE  1 
ATOM   1644 N NZ  . LYS   A 1 217 ? -15.63844 -36.27615 -13.31186 1.000 79.98589 ? 224 LYS   A NZ  1 
HETATM 1645 N N1  . A1AX5 B 2 .   ? 6.29596   -12.13807 -23.71539 0.898 22.44983 ? 301 A1AX5 A N1  1 
HETATM 1646 C C4  . A1AX5 B 2 .   ? 7.29587   -13.88661 -25.08402 0.898 28.42910 ? 301 A1AX5 A C4  1 
HETATM 1647 C C5  . A1AX5 B 2 .   ? 6.17698   -13.33166 -24.49315 0.898 23.67147 ? 301 A1AX5 A C5  1 
HETATM 1648 C C6  . A1AX5 B 2 .   ? 5.28781   -11.27379 -23.37759 0.898 25.09518 ? 301 A1AX5 A C6  1 
HETATM 1649 C C7  . A1AX5 B 2 .   ? 5.85080   -10.30481 -22.64389 0.898 17.91856 ? 301 A1AX5 A C7  1 
HETATM 1650 C C8  . A1AX5 B 2 .   ? 7.42385   -11.64723 -23.15953 0.898 19.07141 ? 301 A1AX5 A C8  1 
HETATM 1651 C C1  . A1AX5 B 2 .   ? 4.84490   -15.08068 -25.39127 0.898 24.06286 ? 301 A1AX5 A C1  1 
HETATM 1652 C C2  . A1AX5 B 2 .   ? 5.93270   -15.65544 -25.99089 0.898 22.77773 ? 301 A1AX5 A C2  1 
HETATM 1653 C C3  . A1AX5 B 2 .   ? 7.16710   -15.04637 -25.83166 0.898 24.63603 ? 301 A1AX5 A C3  1 
HETATM 1654 C C9  . A1AX5 B 2 .   ? 4.94429   -13.93025 -24.64525 0.898 20.53357 ? 301 A1AX5 A C9  1 
HETATM 1655 F F1  . A1AX5 B 2 .   ? 3.62426   -15.66025 -25.53231 0.898 24.79218 ? 301 A1AX5 A F1  1 
HETATM 1656 N N2  . A1AX5 B 2 .   ? 7.19294   -10.53411 -22.50166 0.898 30.21566 ? 301 A1AX5 A N2  1 
HETATM 1657 O O   . HOH   C 3 .   ? -14.55442 -22.68569 0.60749   1.000 56.43468 ? 401 HOH   A O   1 
HETATM 1658 O O   . HOH   C 3 .   ? -12.05728 -26.49898 -10.89702 1.000 49.10483 ? 402 HOH   A O   1 
HETATM 1659 O O   . HOH   C 3 .   ? 8.01492   -22.38721 -36.75178 1.000 41.73738 ? 403 HOH   A O   1 
HETATM 1660 O O   . HOH   C 3 .   ? -7.03721  -23.25994 -30.02683 1.000 48.86899 ? 404 HOH   A O   1 
HETATM 1661 O O   . HOH   C 3 .   ? 13.09906  -6.64688  -4.07828  1.000 63.75809 ? 405 HOH   A O   1 
HETATM 1662 O O   . HOH   C 3 .   ? 18.76192  -7.83323  -8.25012  1.000 50.65182 ? 406 HOH   A O   1 
HETATM 1663 O O   . HOH   C 3 .   ? -5.27199  -24.59903 -31.28914 1.000 49.81877 ? 407 HOH   A O   1 
HETATM 1664 O O   . HOH   C 3 .   ? -1.42674  -29.03566 -5.51749  1.000 34.22610 ? 408 HOH   A O   1 
HETATM 1665 O O   . HOH   C 3 .   ? 5.42513   -24.88034 -30.33351 1.000 24.62855 ? 409 HOH   A O   1 
HETATM 1666 O O   . HOH   C 3 .   ? 10.32485  -8.52680  -3.53757  1.000 52.64719 ? 410 HOH   A O   1 
HETATM 1667 O O   . HOH   C 3 .   ? -7.88116  1.27138   -26.29511 1.000 25.09761 ? 411 HOH   A O   1 
HETATM 1668 O O   . HOH   C 3 .   ? 0.50611   -5.82450  -18.55435 1.000 28.48042 ? 412 HOH   A O   1 
HETATM 1669 O O   . HOH   C 3 .   ? 5.03341   -30.58401 -36.63552 1.000 67.35412 ? 413 HOH   A O   1 
HETATM 1670 O O   . HOH   C 3 .   ? 2.170     -3.926    -28.986   1.000 47.84285 ? 414 HOH   A O   1 
HETATM 1671 O O   . HOH   C 3 .   ? 13.50291  -23.26294 -39.89544 1.000 50.47532 ? 415 HOH   A O   1 
HETATM 1672 O O   . HOH   C 3 .   ? 6.00329   -25.64597 -6.71590  1.000 45.28552 ? 416 HOH   A O   1 
HETATM 1673 O O   . HOH   C 3 .   ? 4.50458   -18.46295 -41.22605 1.000 54.55993 ? 417 HOH   A O   1 
HETATM 1674 O O   . HOH   C 3 .   ? -5.52413  -31.53568 -11.51647 1.000 39.36916 ? 418 HOH   A O   1 
HETATM 1675 O O   . HOH   C 3 .   ? 2.36133   -8.21607  -16.74635 1.000 25.69338 ? 419 HOH   A O   1 
HETATM 1676 O O   . HOH   C 3 .   ? 9.72085   -26.73236 -16.45779 1.000 36.94493 ? 420 HOH   A O   1 
HETATM 1677 O O   . HOH   C 3 .   ? 8.50463   -28.38916 -23.39035 1.000 39.63759 ? 421 HOH   A O   1 
HETATM 1678 O O   . HOH   C 3 .   ? 8.00410   -18.93060 -6.18278  1.000 27.61727 ? 422 HOH   A O   1 
HETATM 1679 O O   . HOH   C 3 .   ? 8.33998   -23.61691 -13.66008 1.000 30.32184 ? 423 HOH   A O   1 
HETATM 1680 O O   . HOH   C 3 .   ? -12.34945 -27.39822 -35.13207 1.000 53.80668 ? 424 HOH   A O   1 
HETATM 1681 O O   . HOH   C 3 .   ? 12.59514  -28.91265 -29.47658 1.000 29.92216 ? 425 HOH   A O   1 
HETATM 1682 O O   . HOH   C 3 .   ? -3.70453  -8.12868  -42.67455 1.000 53.13355 ? 426 HOH   A O   1 
HETATM 1683 O O   . HOH   C 3 .   ? -15.48020 -13.17437 -20.58663 1.000 25.56062 ? 427 HOH   A O   1 
HETATM 1684 O O   . HOH   C 3 .   ? 2.97055   -20.32000 -2.50797  1.000 38.58648 ? 428 HOH   A O   1 
HETATM 1685 O O   . HOH   C 3 .   ? 2.32006   -27.41437 -37.62382 1.000 51.10131 ? 429 HOH   A O   1 
HETATM 1686 O O   . HOH   C 3 .   ? -7.44587  -25.13611 -19.20021 1.000 22.63804 ? 430 HOH   A O   1 
HETATM 1687 O O   . HOH   C 3 .   ? 12.50429  -2.54300  -21.69580 1.000 37.18014 ? 431 HOH   A O   1 
HETATM 1688 O O   . HOH   C 3 .   ? 0.77300   -2.14903  -19.47420 1.000 38.64721 ? 432 HOH   A O   1 
HETATM 1689 O O   . HOH   C 3 .   ? 4.94627   -25.13547 -38.25847 1.000 35.42563 ? 433 HOH   A O   1 
HETATM 1690 O O   . HOH   C 3 .   ? 18.99646  -20.27897 -23.59832 1.000 38.41017 ? 434 HOH   A O   1 
HETATM 1691 O O   . HOH   C 3 .   ? 19.15482  -11.62993 -16.68179 1.000 29.69361 ? 435 HOH   A O   1 
HETATM 1692 O O   . HOH   C 3 .   ? 11.25873  -14.76633 -24.80585 1.000 27.51999 ? 436 HOH   A O   1 
HETATM 1693 O O   . HOH   C 3 .   ? -13.82783 -22.40075 -11.72036 1.000 34.91756 ? 437 HOH   A O   1 
HETATM 1694 O O   . HOH   C 3 .   ? 3.65094   -6.22924  -11.30611 1.000 29.33382 ? 438 HOH   A O   1 
HETATM 1695 O O   . HOH   C 3 .   ? 11.81184  -26.14569 -25.86137 1.000 32.14240 ? 439 HOH   A O   1 
HETATM 1696 O O   . HOH   C 3 .   ? -0.39036  -14.36993 -35.47370 1.000 22.95327 ? 440 HOH   A O   1 
HETATM 1697 O O   . HOH   C 3 .   ? 10.09521  -17.79400 -7.28770  1.000 26.65395 ? 441 HOH   A O   1 
HETATM 1698 O O   . HOH   C 3 .   ? -13.38760 -16.89747 -3.18318  1.000 30.14027 ? 442 HOH   A O   1 
HETATM 1699 O O   . HOH   C 3 .   ? -3.320    -21.052   -0.707    1.000 43.89970 ? 443 HOH   A O   1 
HETATM 1700 O O   . HOH   C 3 .   ? -4.47894  -5.64364  -39.64521 1.000 47.13918 ? 444 HOH   A O   1 
HETATM 1701 O O   . HOH   C 3 .   ? 0.28173   -10.19412 -43.50780 1.000 59.67235 ? 445 HOH   A O   1 
HETATM 1702 O O   . HOH   C 3 .   ? -0.63549  -30.53674 -17.22401 1.000 49.60650 ? 446 HOH   A O   1 
HETATM 1703 O O   . HOH   C 3 .   ? -8.53401  -2.64701  -18.29687 1.000 25.82715 ? 447 HOH   A O   1 
HETATM 1704 O O   . HOH   C 3 .   ? -12.56033 -7.62261  -12.72254 1.000 42.46782 ? 448 HOH   A O   1 
HETATM 1705 O O   . HOH   C 3 .   ? -16.26652 -3.67489  -36.97950 1.000 45.92308 ? 449 HOH   A O   1 
HETATM 1706 O O   . HOH   C 3 .   ? -4.75746  -7.84082  -13.62478 1.000 26.14450 ? 450 HOH   A O   1 
HETATM 1707 O O   . HOH   C 3 .   ? 10.19058  -12.62435 -28.55517 1.000 26.89420 ? 451 HOH   A O   1 
HETATM 1708 O O   . HOH   C 3 .   ? 1.04297   -5.80438  -14.05313 1.000 42.67583 ? 452 HOH   A O   1 
HETATM 1709 O O   . HOH   C 3 .   ? 5.38153   -8.22380  -36.02219 1.000 33.18853 ? 453 HOH   A O   1 
HETATM 1710 O O   . HOH   C 3 .   ? -16.10448 -5.94869  -23.79819 1.000 30.92720 ? 454 HOH   A O   1 
HETATM 1711 O O   . HOH   C 3 .   ? -4.08566  -11.05266 -27.62902 1.000 22.06963 ? 455 HOH   A O   1 
HETATM 1712 O O   . HOH   C 3 .   ? 18.84697  -0.57088  -16.85277 1.000 41.79566 ? 456 HOH   A O   1 
HETATM 1713 O O   . HOH   C 3 .   ? -19.75086 -14.44206 -19.31411 1.000 45.50359 ? 457 HOH   A O   1 
HETATM 1714 O O   . HOH   C 3 .   ? 1.26879   -30.05776 -15.69155 1.000 40.24616 ? 458 HOH   A O   1 
HETATM 1715 O O   . HOH   C 3 .   ? -3.42042  -0.07780  -22.61261 1.000 24.10027 ? 459 HOH   A O   1 
HETATM 1716 O O   . HOH   C 3 .   ? 6.38100   -20.14210 -40.28372 1.000 39.17151 ? 460 HOH   A O   1 
HETATM 1717 O O   . HOH   C 3 .   ? -4.99018  -2.54025  -20.01796 1.000 24.48614 ? 461 HOH   A O   1 
HETATM 1718 O O   . HOH   C 3 .   ? -15.55296 -25.85442 -18.16657 1.000 27.84791 ? 462 HOH   A O   1 
HETATM 1719 O O   . HOH   C 3 .   ? -0.51822  -6.74740  -26.48147 1.000 28.37657 ? 463 HOH   A O   1 
HETATM 1720 O O   . HOH   C 3 .   ? -3.58314  -5.02050  -8.76036  1.000 40.21452 ? 464 HOH   A O   1 
HETATM 1721 O O   . HOH   C 3 .   ? -0.72305  -11.32750 -3.44251  1.000 46.03664 ? 465 HOH   A O   1 
HETATM 1722 O O   . HOH   C 3 .   ? 13.15749  -28.26428 -33.81326 1.000 29.56386 ? 466 HOH   A O   1 
HETATM 1723 O O   . HOH   C 3 .   ? 1.03469   -21.07684 -4.49433  1.000 31.05774 ? 467 HOH   A O   1 
HETATM 1724 O O   . HOH   C 3 .   ? -0.18773  -7.56908  -23.84318 1.000 21.24303 ? 468 HOH   A O   1 
HETATM 1725 O O   . HOH   C 3 .   ? 7.65097   -27.46284 -27.12847 1.000 37.09150 ? 469 HOH   A O   1 
HETATM 1726 O O   . HOH   C 3 .   ? 16.87285  -5.02200  -25.84368 1.000 41.05429 ? 470 HOH   A O   1 
HETATM 1727 O O   . HOH   C 3 .   ? 1.26641   -7.89001  -31.28946 1.000 30.75661 ? 471 HOH   A O   1 
HETATM 1728 O O   . HOH   C 3 .   ? 7.01916   -8.98853  -3.70322  1.000 40.29435 ? 472 HOH   A O   1 
HETATM 1729 O O   . HOH   C 3 .   ? -15.11426 -3.56391  -22.23600 1.000 34.47355 ? 473 HOH   A O   1 
HETATM 1730 O O   . HOH   C 3 .   ? -5.69690  -23.48730 -36.71011 1.000 39.93944 ? 474 HOH   A O   1 
HETATM 1731 O O   . HOH   C 3 .   ? 5.63038   -12.28770 -38.17906 1.000 29.32401 ? 475 HOH   A O   1 
HETATM 1732 O O   . HOH   C 3 .   ? -2.43492  -11.43739 -24.12362 1.000 24.49145 ? 476 HOH   A O   1 
HETATM 1733 O O   . HOH   C 3 .   ? -10.68927 -14.53909 0.55294   1.000 30.69974 ? 477 HOH   A O   1 
HETATM 1734 O O   . HOH   C 3 .   ? 10.15495  -16.27934 -27.12134 1.000 23.90990 ? 478 HOH   A O   1 
HETATM 1735 O O   . HOH   C 3 .   ? -11.88772 -1.22686  -21.22230 1.000 31.48762 ? 479 HOH   A O   1 
HETATM 1736 O O   . HOH   C 3 .   ? -11.79803 -28.18336 -30.50183 1.000 38.22984 ? 480 HOH   A O   1 
HETATM 1737 O O   . HOH   C 3 .   ? -1.37311  -11.15413 -26.52877 1.000 33.72457 ? 481 HOH   A O   1 
HETATM 1738 O O   . HOH   C 3 .   ? 17.39718  -1.65951  -19.10008 1.000 29.94211 ? 482 HOH   A O   1 
HETATM 1739 O O   . HOH   C 3 .   ? -6.33533  3.76014   -34.43454 1.000 41.23177 ? 483 HOH   A O   1 
HETATM 1740 O O   . HOH   C 3 .   ? 13.28037  -27.59289 -18.94637 1.000 48.08773 ? 484 HOH   A O   1 
HETATM 1741 O O   . HOH   C 3 .   ? 11.53254  -25.86513 -23.04166 1.000 24.58403 ? 485 HOH   A O   1 
HETATM 1742 O O   . HOH   C 3 .   ? -6.09858  0.82201   -37.33890 1.000 34.24341 ? 486 HOH   A O   1 
HETATM 1743 O O   . HOH   C 3 .   ? -8.85163  -15.64233 -28.63287 1.000 33.27188 ? 487 HOH   A O   1 
HETATM 1744 O O   . HOH   C 3 .   ? -17.89414 -11.34838 -24.73563 1.000 28.57186 ? 488 HOH   A O   1 
HETATM 1745 O O   . HOH   C 3 .   ? -12.92540 -26.74973 -18.11742 1.000 27.97050 ? 489 HOH   A O   1 
HETATM 1746 O O   . HOH   C 3 .   ? -6.88040  -12.58039 -36.93256 1.000 30.16498 ? 490 HOH   A O   1 
HETATM 1747 O O   . HOH   C 3 .   ? 5.92887   -21.18681 0.31789   1.000 32.60684 ? 491 HOH   A O   1 
HETATM 1748 O O   . HOH   C 3 .   ? -5.92586  -28.17108 -21.32105 1.000 38.66694 ? 492 HOH   A O   1 
HETATM 1749 O O   . HOH   C 3 .   ? -10.07004 -11.37453 -2.62326  1.000 26.57019 ? 493 HOH   A O   1 
HETATM 1750 O O   . HOH   C 3 .   ? 19.14774  -8.03818  -19.63812 1.000 30.00083 ? 494 HOH   A O   1 
HETATM 1751 O O   . HOH   C 3 .   ? -2.55854  -32.15066 -19.66741 1.000 57.19680 ? 495 HOH   A O   1 
HETATM 1752 O O   . HOH   C 3 .   ? 1.20847   -5.64402  -22.17859 1.000 27.27498 ? 496 HOH   A O   1 
HETATM 1753 O O   . HOH   C 3 .   ? -5.73049  -11.45252 -10.45038 1.000 33.34052 ? 497 HOH   A O   1 
HETATM 1754 O O   . HOH   C 3 .   ? 7.24212   -30.09995 -19.40639 1.000 36.19355 ? 498 HOH   A O   1 
HETATM 1755 O O   . HOH   C 3 .   ? -6.14271  -14.04746 0.69188   1.000 35.47857 ? 499 HOH   A O   1 
HETATM 1756 O O   . HOH   C 3 .   ? -1.67371  -25.53947 -4.58771  1.000 30.44274 ? 500 HOH   A O   1 
HETATM 1757 O O   . HOH   C 3 .   ? -4.84764  -8.48029  -34.76267 1.000 24.41351 ? 501 HOH   A O   1 
HETATM 1758 O O   . HOH   C 3 .   ? -1.03552  -4.12925  -35.60217 1.000 43.80838 ? 502 HOH   A O   1 
HETATM 1759 O O   . HOH   C 3 .   ? -9.19069  -15.02658 -38.30105 1.000 39.21503 ? 503 HOH   A O   1 
HETATM 1760 O O   . HOH   C 3 .   ? -10.31155 -6.32607  -3.57290  1.000 51.39461 ? 504 HOH   A O   1 
HETATM 1761 O O   . HOH   C 3 .   ? 16.11014  -20.81788 -17.89340 1.000 29.98977 ? 505 HOH   A O   1 
HETATM 1762 O O   . HOH   C 3 .   ? 20.59276  -17.03012 -27.00517 1.000 38.88492 ? 506 HOH   A O   1 
HETATM 1763 O O   . HOH   C 3 .   ? 19.99060  -0.28156  -8.45869  1.000 42.76352 ? 507 HOH   A O   1 
HETATM 1764 O O   . HOH   C 3 .   ? -5.63165  -35.53229 -19.97686 1.000 53.18403 ? 508 HOH   A O   1 
HETATM 1765 O O   . HOH   C 3 .   ? -6.475    1.006     -20.241   1.000 45.23023 ? 509 HOH   A O   1 
HETATM 1766 O O   . HOH   C 3 .   ? -13.64011 -12.63706 -8.50218  1.000 28.19046 ? 510 HOH   A O   1 
HETATM 1767 O O   . HOH   C 3 .   ? -2.31378  -13.28977 -21.02177 1.000 33.12372 ? 511 HOH   A O   1 
HETATM 1768 O O   . HOH   C 3 .   ? 10.52802  -21.41751 -6.53349  1.000 41.59060 ? 512 HOH   A O   1 
HETATM 1769 O O   . HOH   C 3 .   ? 19.34243  -16.82933 -12.85293 1.000 45.33045 ? 513 HOH   A O   1 
HETATM 1770 O O   . HOH   C 3 .   ? -2.33716  -1.54095  -24.59871 1.000 28.70051 ? 514 HOH   A O   1 
HETATM 1771 O O   . HOH   C 3 .   ? -2.64838  -3.34786  -17.81300 1.000 42.06183 ? 515 HOH   A O   1 
HETATM 1772 O O   . HOH   C 3 .   ? -19.06912 -19.52636 -14.52976 1.000 26.45712 ? 516 HOH   A O   1 
HETATM 1773 O O   . HOH   C 3 .   ? 8.06838   -23.68476 -6.92166  1.000 36.37124 ? 517 HOH   A O   1 
HETATM 1774 O O   . HOH   C 3 .   ? 14.13596  -15.62139 -1.44061  1.000 41.34199 ? 518 HOH   A O   1 
HETATM 1775 O O   . HOH   C 3 .   ? 15.82671  -18.62136 -2.85027  1.000 38.28347 ? 519 HOH   A O   1 
HETATM 1776 O O   . HOH   C 3 .   ? 8.37696   -7.71537  -23.68230 1.000 36.10616 ? 520 HOH   A O   1 
HETATM 1777 O O   . HOH   C 3 .   ? 4.89298   -9.47101  -19.93808 1.000 21.24331 ? 521 HOH   A O   1 
HETATM 1778 O O   . HOH   C 3 .   ? -17.04312 -18.64537 -11.73630 1.000 37.77107 ? 522 HOH   A O   1 
HETATM 1779 O O   . HOH   C 3 .   ? 10.20313  -24.35336 -8.75147  1.000 48.25050 ? 523 HOH   A O   1 
HETATM 1780 O O   . HOH   C 3 .   ? -7.45209  -28.36130 -7.43792  1.000 37.48698 ? 524 HOH   A O   1 
HETATM 1781 O O   . HOH   C 3 .   ? -6.95235  -11.26420 -41.14973 1.000 48.65940 ? 525 HOH   A O   1 
HETATM 1782 O O   . HOH   C 3 .   ? -13.91493 -11.79121 -30.62918 1.000 28.84305 ? 526 HOH   A O   1 
HETATM 1783 O O   . HOH   C 3 .   ? 10.33100  -17.14949 -39.20813 1.000 46.45553 ? 527 HOH   A O   1 
HETATM 1784 O O   . HOH   C 3 .   ? -14.54220 -0.50887  -31.67753 1.000 49.45420 ? 528 HOH   A O   1 
HETATM 1785 O O   . HOH   C 3 .   ? -16.91390 -6.60113  -26.49758 1.000 37.86460 ? 529 HOH   A O   1 
HETATM 1786 O O   . HOH   C 3 .   ? -6.69359  -24.85449 -23.16637 1.000 32.67649 ? 530 HOH   A O   1 
HETATM 1787 O O   . HOH   C 3 .   ? -8.03994  -5.48499  -7.67189  1.000 40.20993 ? 531 HOH   A O   1 
HETATM 1788 O O   . HOH   C 3 .   ? 4.68414   -7.29355  -18.04507 1.000 26.36845 ? 532 HOH   A O   1 
HETATM 1789 O O   . HOH   C 3 .   ? -9.15217  -1.02377  -20.46813 1.000 28.35431 ? 533 HOH   A O   1 
HETATM 1790 O O   . HOH   C 3 .   ? -4.06184  -14.61753 -22.80074 1.000 23.96222 ? 534 HOH   A O   1 
HETATM 1791 O O   . HOH   C 3 .   ? 8.85936   -20.86759 -8.82187  1.000 29.04416 ? 535 HOH   A O   1 
HETATM 1792 O O   . HOH   C 3 .   ? 5.15979   -30.91099 -11.28343 1.000 45.03051 ? 536 HOH   A O   1 
HETATM 1793 O O   . HOH   C 3 .   ? -1.36376  -32.70327 -7.26143  1.000 53.43973 ? 537 HOH   A O   1 
HETATM 1794 O O   . HOH   C 3 .   ? -18.00867 -11.01765 -33.76524 1.000 48.15982 ? 538 HOH   A O   1 
HETATM 1795 O O   . HOH   C 3 .   ? 8.91262   -20.52213 -3.82479  1.000 26.03040 ? 539 HOH   A O   1 
HETATM 1796 O O   . HOH   C 3 .   ? 0.13709   -16.68671 -3.64910  1.000 27.51411 ? 540 HOH   A O   1 
HETATM 1797 O O   . HOH   C 3 .   ? 10.26630  -3.51942  -20.78325 1.000 42.20644 ? 541 HOH   A O   1 
HETATM 1798 O O   . HOH   C 3 .   ? 22.86602  -13.63823 -18.54699 1.000 48.54795 ? 542 HOH   A O   1 
HETATM 1799 O O   . HOH   C 3 .   ? -3.14207  -0.17351  -30.72569 1.000 39.42099 ? 543 HOH   A O   1 
HETATM 1800 O O   . HOH   C 3 .   ? 13.52138  -22.72172 -3.96367  1.000 52.69802 ? 544 HOH   A O   1 
HETATM 1801 O O   . HOH   C 3 .   ? 3.72219   -30.42772 -18.56518 1.000 49.05870 ? 545 HOH   A O   1 
HETATM 1802 O O   . HOH   C 3 .   ? -16.41699 -25.20775 -9.31466  1.000 48.39158 ? 546 HOH   A O   1 
HETATM 1803 O O   . HOH   C 3 .   ? -14.77552 -12.30711 -12.66319 1.000 51.79813 ? 547 HOH   A O   1 
HETATM 1804 O O   . HOH   C 3 .   ? -3.76295  -19.63214 -39.39122 1.000 40.77575 ? 548 HOH   A O   1 
HETATM 1805 O O   . HOH   C 3 .   ? -11.10637 -8.34115  -43.20116 1.000 50.75260 ? 549 HOH   A O   1 
HETATM 1806 O O   . HOH   C 3 .   ? -7.73003  -3.85701  -11.43089 1.000 37.19599 ? 550 HOH   A O   1 
HETATM 1807 O O   . HOH   C 3 .   ? -2.51039  -5.73180  -6.98815  1.000 42.40926 ? 551 HOH   A O   1 
HETATM 1808 O O   . HOH   C 3 .   ? -17.10590 -15.21266 -13.79538 1.000 35.44939 ? 552 HOH   A O   1 
HETATM 1809 O O   . HOH   C 3 .   ? 21.96640  -14.87924 -25.78263 1.000 34.99030 ? 553 HOH   A O   1 
HETATM 1810 O O   . HOH   C 3 .   ? -4.49570  -5.83457  -36.02661 1.000 28.69985 ? 554 HOH   A O   1 
HETATM 1811 O O   . HOH   C 3 .   ? 2.01627   -3.84878  -24.08665 1.000 36.87170 ? 555 HOH   A O   1 
HETATM 1812 O O   . HOH   C 3 .   ? 3.38428   -6.62906  -20.94929 1.000 31.24927 ? 556 HOH   A O   1 
HETATM 1813 O O   . HOH   C 3 .   ? 16.71362  -26.62361 -23.86784 1.000 44.04731 ? 557 HOH   A O   1 
HETATM 1814 O O   . HOH   C 3 .   ? 0.53308   -5.48599  -33.34430 1.000 46.77487 ? 558 HOH   A O   1 
HETATM 1815 O O   . HOH   C 3 .   ? -8.165    2.442     -21.778   1.000 33.44239 ? 559 HOH   A O   1 
HETATM 1816 O O   . HOH   C 3 .   ? 0.32288   -26.80189 -32.65382 1.000 46.42756 ? 560 HOH   A O   1 
HETATM 1817 O O   . HOH   C 3 .   ? -6.56096  -19.06868 -37.41654 1.000 45.35931 ? 561 HOH   A O   1 
HETATM 1818 O O   . HOH   C 3 .   ? -6.783    -22.912   -2.015    1.000 38.86685 ? 562 HOH   A O   1 
HETATM 1819 O O   . HOH   C 3 .   ? -16.10657 -4.15502  -30.16958 1.000 46.08918 ? 563 HOH   A O   1 
HETATM 1820 O O   . HOH   C 3 .   ? 0.47563   -12.73746 -21.61334 1.000 31.85566 ? 564 HOH   A O   1 
HETATM 1821 O O   . HOH   C 3 .   ? -4.77692  5.92508   -34.88102 1.000 47.01521 ? 565 HOH   A O   1 
HETATM 1822 O O   . HOH   C 3 .   ? -5.22615  -14.26076 -41.50831 1.000 52.87504 ? 566 HOH   A O   1 
HETATM 1823 O O   . HOH   C 3 .   ? 14.39624  -20.79918 -20.00458 1.000 25.74320 ? 567 HOH   A O   1 
HETATM 1824 O O   . HOH   C 3 .   ? -12.78847 -19.09409 -24.84481 1.000 28.00091 ? 568 HOH   A O   1 
HETATM 1825 O O   . HOH   C 3 .   ? 4.15579   -22.89741 -3.16028  1.000 37.19729 ? 569 HOH   A O   1 
HETATM 1826 O O   . HOH   C 3 .   ? 13.98503  -13.13480 -28.27901 1.000 44.52777 ? 570 HOH   A O   1 
HETATM 1827 O O   . HOH   C 3 .   ? -11.63582 -12.87879 -31.68351 1.000 31.01116 ? 571 HOH   A O   1 
HETATM 1828 O O   . HOH   C 3 .   ? -0.54716  -9.18133  -27.74596 1.000 30.14426 ? 572 HOH   A O   1 
HETATM 1829 O O   . HOH   C 3 .   ? 9.19126   -1.22130  -18.70839 1.000 39.35148 ? 573 HOH   A O   1 
HETATM 1830 O O   . HOH   C 3 .   ? 5.78785   -21.96434 -38.34156 1.000 42.06618 ? 574 HOH   A O   1 
HETATM 1831 O O   . HOH   C 3 .   ? -13.08219 -16.84460 -26.50410 1.000 36.78302 ? 575 HOH   A O   1 
HETATM 1832 O O   . HOH   C 3 .   ? 1.79204   -6.52736  -38.01747 1.000 45.17816 ? 576 HOH   A O   1 
HETATM 1833 O O   . HOH   C 3 .   ? -13.64257 -23.91428 -5.18491  1.000 40.42170 ? 577 HOH   A O   1 
HETATM 1834 O O   . HOH   C 3 .   ? -4.66049  -31.83987 -6.84161  1.000 49.82640 ? 578 HOH   A O   1 
HETATM 1835 O O   . HOH   C 3 .   ? -1.053    -1.804    -31.635   1.000 46.83281 ? 579 HOH   A O   1 
HETATM 1836 O O   . HOH   C 3 .   ? 11.21979  -8.42455  -36.29199 1.000 53.79926 ? 580 HOH   A O   1 
HETATM 1837 O O   . HOH   C 3 .   ? -14.38130 -25.08569 -11.31134 1.000 43.79088 ? 581 HOH   A O   1 
HETATM 1838 O O   . HOH   C 3 .   ? -13.43045 -25.71000 -7.58895  1.000 38.42579 ? 582 HOH   A O   1 
HETATM 1839 O O   . HOH   C 3 .   ? 18.70350  -25.21145 -24.12669 1.000 36.70034 ? 583 HOH   A O   1 
HETATM 1840 O O   . HOH   C 3 .   ? 12.17905  -18.79115 -38.03146 1.000 40.44852 ? 584 HOH   A O   1 
HETATM 1841 O O   . HOH   C 3 .   ? 20.343    -24.427   -21.454   1.000 48.10011 ? 585 HOH   A O   1 
HETATM 1842 O O   . HOH   C 3 .   ? -3.60785  -3.69109  -15.76492 1.000 50.48414 ? 586 HOH   A O   1 
HETATM 1843 O O   . HOH   C 3 .   ? 14.37317  -14.44909 -25.73018 1.000 12.06970 ? 587 HOH   A O   1 
HETATM 1844 O O   . HOH   C 3 .   ? 15.13910  -23.00398 -16.33044 1.000 30.74992 ? 588 HOH   A O   1 
HETATM 1845 O O   . HOH   C 3 .   ? -1.12536  -27.62745 -24.60079 1.000 41.90198 ? 589 HOH   A O   1 
HETATM 1846 O O   . HOH   C 3 .   ? 6.892     1.885     -13.505   1.000 50.53809 ? 590 HOH   A O   1 
HETATM 1847 O O   . HOH   C 3 .   ? 7.088     1.547     -16.424   1.000 40.71415 ? 591 HOH   A O   1 
HETATM 1848 O O   . HOH   C 3 .   ? 9.46440   -26.47382 -25.27970 1.000 38.60050 ? 592 HOH   A O   1 
HETATM 1849 O O   . HOH   C 3 .   ? -16.37707 -5.08393  -18.54189 1.000 41.54517 ? 593 HOH   A O   1 
HETATM 1850 O O   . HOH   C 3 .   ? -11.65651 -27.16130 -20.32028 1.000 31.61505 ? 594 HOH   A O   1 
HETATM 1851 O O   . HOH   C 3 .   ? -5.76692  -11.08497 0.98016   1.000 39.15485 ? 595 HOH   A O   1 
HETATM 1852 O O   . HOH   C 3 .   ? -19.78359 -19.57746 -11.71648 1.000 39.92412 ? 596 HOH   A O   1 
HETATM 1853 O O   . HOH   C 3 .   ? -15.64553 -4.22354  -16.94865 1.000 47.76454 ? 597 HOH   A O   1 
HETATM 1854 O O   . HOH   C 3 .   ? -18.97962 -12.53399 -16.68057 1.000 50.59765 ? 598 HOH   A O   1 
HETATM 1855 O O   . HOH   C 3 .   ? 15.16367  0.45861   -12.86568 1.000 46.76538 ? 599 HOH   A O   1 
HETATM 1856 O O   . HOH   C 3 .   ? -4.11500  -5.42774  -12.82915 1.000 47.25587 ? 600 HOH   A O   1 
HETATM 1857 O O   . HOH   C 3 .   ? 22.14246  -9.77269  -13.39682 1.000 58.96565 ? 601 HOH   A O   1 
HETATM 1858 O O   . HOH   C 3 .   ? 18.50671  -22.14499 -18.88732 1.000 32.35213 ? 602 HOH   A O   1 
HETATM 1859 O O   . HOH   C 3 .   ? -12.89644 -25.33148 -37.31530 1.000 50.47141 ? 603 HOH   A O   1 
HETATM 1860 O O   . HOH   C 3 .   ? 20.15975  -22.82961 -24.94896 1.000 51.85033 ? 604 HOH   A O   1 
HETATM 1861 O O   . HOH   C 3 .   ? -8.92163  -17.49511 -37.81465 1.000 48.24460 ? 605 HOH   A O   1 
HETATM 1862 O O   . HOH   C 3 .   ? -3.45626  -13.30429 -42.44868 1.000 55.51309 ? 606 HOH   A O   1 
HETATM 1863 O O   . HOH   C 3 .   ? -11.913   -32.689   -19.251   1.000 56.44030 ? 607 HOH   A O   1 
HETATM 1864 O O   . HOH   C 3 .   ? 0.63532   -27.12980 -30.10935 1.000 49.75750 ? 608 HOH   A O   1 
HETATM 1865 O O   . HOH   C 3 .   ? 4.82745   -24.48644 -41.33444 1.000 51.68390 ? 609 HOH   A O   1 
HETATM 1866 O O   . HOH   C 3 .   ? 11.30600  -13.11132 -36.94107 1.000 62.90369 ? 610 HOH   A O   1 
HETATM 1867 O O   . HOH   C 3 .   ? 21.44561  -6.85631  -20.43454 1.000 45.52668 ? 611 HOH   A O   1 
HETATM 1868 O O   . HOH   C 3 .   ? -14.25913 -1.82458  -24.48243 1.000 46.80677 ? 612 HOH   A O   1 
HETATM 1869 O O   . HOH   C 3 .   ? -13.67780 -14.03560 -3.57725  1.000 41.54905 ? 613 HOH   A O   1 
HETATM 1870 O O   . HOH   C 3 .   ? -18.72964 -13.20220 -14.62580 1.000 53.78671 ? 614 HOH   A O   1 
HETATM 1871 O O   . HOH   C 3 .   ? -14.42978 -29.12708 -17.50973 1.000 37.82616 ? 615 HOH   A O   1 
HETATM 1872 O O   . HOH   C 3 .   ? -5.65850  1.28646   -40.11841 1.000 55.02223 ? 616 HOH   A O   1 
HETATM 1873 O O   . HOH   C 3 .   ? -16.77484 -15.63590 -10.92305 1.000 50.90190 ? 617 HOH   A O   1 
HETATM 1874 O O   . HOH   C 3 .   ? 19.68136  -4.54446  -21.87771 1.000 42.05073 ? 618 HOH   A O   1 
HETATM 1875 O O   . HOH   C 3 .   ? -2.44301  5.61201   -35.27199 1.000 58.25451 ? 619 HOH   A O   1 
HETATM 1876 O O   . HOH   C 3 .   ? -17.59319 -3.43630  -32.09164 1.000 49.48996 ? 620 HOH   A O   1 
HETATM 1877 O O   . HOH   C 3 .   ? -11.21898 -17.06461 -28.58717 1.000 38.61424 ? 621 HOH   A O   1 
HETATM 1878 O O   . HOH   C 3 .   ? 18.81916  -4.26319  -24.71348 1.000 40.09948 ? 622 HOH   A O   1 
HETATM 1879 O O   . HOH   C 3 .   ? 4.35648   -7.95342  -22.93195 1.000 31.53145 ? 623 HOH   A O   1 
HETATM 1880 O O   . HOH   C 3 .   ? 19.80882  -8.91203  -17.07556 1.000 38.99416 ? 624 HOH   A O   1 
HETATM 1881 O O   . HOH   C 3 .   ? 16.37487  1.23241   -10.51198 1.000 48.08976 ? 625 HOH   A O   1 
HETATM 1882 O O   . HOH   C 3 .   ? -13.82328 -9.74220  -9.31001  1.000 36.69609 ? 626 HOH   A O   1 
HETATM 1883 O O   . HOH   C 3 .   ? -5.50060  2.41102   -26.03356 1.000 30.70956 ? 627 HOH   A O   1 
HETATM 1884 O O   . HOH   C 3 .   ? -3.96600  2.35712   -35.52390 1.000 47.72297 ? 628 HOH   A O   1 
HETATM 1885 O O   . HOH   C 3 .   ? -2.33177  1.58697   -33.06278 1.000 47.94405 ? 629 HOH   A O   1 
HETATM 1886 O O   . HOH   C 3 .   ? -9.27315  -26.22965 -20.91229 1.000 33.12253 ? 630 HOH   A O   1 
HETATM 1887 O O   . HOH   C 3 .   ? -6.98397  -6.38195  -40.46156 1.000 40.83406 ? 631 HOH   A O   1 
HETATM 1888 O O   . HOH   C 3 .   ? -11.70055 -18.57602 -37.55428 1.000 47.94789 ? 632 HOH   A O   1 
HETATM 1889 O O   . HOH   C 3 .   ? -17.69276 -12.05729 -22.08951 1.000 30.56457 ? 633 HOH   A O   1 
HETATM 1890 O O   . HOH   C 3 .   ? -10.18932 -8.51654  -2.11444  1.000 47.20707 ? 634 HOH   A O   1 
HETATM 1891 O O   . HOH   C 3 .   ? -15.688   -0.446    -19.245   1.000 35.06091 ? 635 HOH   A O   1 
HETATM 1892 O O   . HOH   C 3 .   ? 13.20744  -0.78543  -19.80472 1.000 35.82081 ? 636 HOH   A O   1 
HETATM 1893 O O   . HOH   C 3 .   ? -3.26451  -33.08340 -10.38198 1.000 58.52373 ? 637 HOH   A O   1 
HETATM 1894 O O   . HOH   C 3 .   ? 7.23530   -30.62626 -24.36880 1.000 38.55881 ? 638 HOH   A O   1 
HETATM 1895 O O   . HOH   C 3 .   ? -13.369   -30.861   -21.014   1.000 40.86982 ? 639 HOH   A O   1 
HETATM 1896 O O   . HOH   C 3 .   ? 4.988     0.451     -18.083   1.000 49.94582 ? 640 HOH   A O   1 
HETATM 1897 O O   . HOH   C 3 .   ? -9.65189  -10.55371 -40.46748 1.000 49.67814 ? 641 HOH   A O   1 
HETATM 1898 O O   . HOH   C 3 .   ? 9.88915   -14.52823 -37.68446 1.000 48.14826 ? 642 HOH   A O   1 
HETATM 1899 O O   . HOH   C 3 .   ? 9.85046   -29.57729 -16.42178 1.000 52.53146 ? 643 HOH   A O   1 
HETATM 1900 O O   . HOH   C 3 .   ? 0.31195   -1.81433  -23.76962 1.000 39.02653 ? 644 HOH   A O   1 
HETATM 1901 O O   . HOH   C 3 .   ? -1.36508  -4.87601  -12.76620 1.000 55.57312 ? 645 HOH   A O   1 
HETATM 1902 O O   . HOH   C 3 .   ? 7.64520   -13.17867 -39.55179 1.000 38.11928 ? 646 HOH   A O   1 
HETATM 1903 O O   . HOH   C 3 .   ? 6.70461   -21.65150 -2.42715  1.000 37.66123 ? 647 HOH   A O   1 
HETATM 1904 O O   . HOH   C 3 .   ? -16.45643 -23.19394 -4.46425  1.000 52.65055 ? 648 HOH   A O   1 
HETATM 1905 O O   . HOH   C 3 .   ? 6.02334   -8.92398  -38.42438 1.000 46.14823 ? 649 HOH   A O   1 
HETATM 1906 O O   . HOH   C 3 .   ? -15.56964 -1.82983  -16.44310 1.000 37.17862 ? 650 HOH   A O   1 
HETATM 1907 O O   . HOH   C 3 .   ? 2.828     -1.268    -28.727   1.000 48.09712 ? 651 HOH   A O   1 
HETATM 1908 O O   . HOH   C 3 .   ? 12.40076  -28.56669 -22.65389 1.000 47.34587 ? 652 HOH   A O   1 
HETATM 1909 O O   . HOH   C 3 .   ? 2.12831   -8.98531  -24.24041 1.000 38.47933 ? 653 HOH   A O   1 
HETATM 1910 O O   . HOH   C 3 .   ? 5.99691   -6.28812  -23.94318 1.000 32.15687 ? 654 HOH   A O   1 
HETATM 1911 O O   . HOH   C 3 .   ? -4.18608  2.48500   -23.64584 1.000 38.01865 ? 655 HOH   A O   1 
HETATM 1912 O O   . HOH   C 3 .   ? -8.56835  -11.36369 -0.11275  1.000 50.50785 ? 656 HOH   A O   1 
HETATM 1913 O O   . HOH   C 3 .   ? 21.13009  0.79430   -6.03261  1.000 52.32529 ? 657 HOH   A O   1 
HETATM 1914 O O   . HOH   C 3 .   ? 10.59787  -22.74069 -3.91465  1.000 42.01832 ? 658 HOH   A O   1 
HETATM 1915 O O   . HOH   C 3 .   ? -15.52709 -8.05587  -7.67224  1.000 58.41370 ? 659 HOH   A O   1 
HETATM 1916 O O   . HOH   C 3 .   ? 20.21987  -21.95306 -20.63530 1.000 46.93485 ? 660 HOH   A O   1 
HETATM 1917 O O   . HOH   C 3 .   ? -14.23906 -10.04955 -12.28412 1.000 53.05295 ? 661 HOH   A O   1 
HETATM 1918 O O   . HOH   C 3 .   ? -12.12745 -14.93347 -38.49441 1.000 51.76234 ? 662 HOH   A O   1 
HETATM 1919 O O   . HOH   C 3 .   ? -9.50918  -24.33195 -23.35433 1.000 48.52054 ? 663 HOH   A O   1 
HETATM 1920 O O   . HOH   C 3 .   ? 10.76500  -14.41440 -7.88420  1.000 44.68689 ? 664 HOH   A O   1 
HETATM 1921 O O   . HOH   C 3 .   ? -6.61358  -31.02377 -8.93390  1.000 49.77528 ? 665 HOH   A O   1 
HETATM 1922 O O   . HOH   C 3 .   ? 2.14290   -8.69067  -27.18041 1.000 38.85627 ? 666 HOH   A O   1 
HETATM 1923 O O   . HOH   C 3 .   ? 1.83187   -11.59785 -24.55303 1.000 38.89800 ? 667 HOH   A O   1 
HETATM 1924 O O   . HOH   C 3 .   ? -3.43690  -28.72284 -23.05802 1.000 38.17931 ? 668 HOH   A O   1 
HETATM 1925 O O   . HOH   C 3 .   ? 14.41721  -13.17152 -2.31381  1.000 46.66300 ? 669 HOH   A O   1 
HETATM 1926 O O   . HOH   C 3 .   ? 6.19404   -4.12245  -22.46595 1.000 38.79436 ? 670 HOH   A O   1 
HETATM 1927 O O   . HOH   C 3 .   ? -12.31588 -12.74255 -1.96682  1.000 34.54694 ? 671 HOH   A O   1 
HETATM 1928 O O   . HOH   C 3 .   ? 13.53636  -12.76635 -9.67991  1.000 48.19316 ? 672 HOH   A O   1 
HETATM 1929 O O   . HOH   C 3 .   ? -18.71215 -9.03237  -24.92399 1.000 46.63905 ? 673 HOH   A O   1 
HETATM 1930 O O   . HOH   C 3 .   ? -11.998   0.977     -17.634   1.000 36.45543 ? 674 HOH   A O   1 
HETATM 1931 O O   . HOH   C 3 .   ? 8.98297   -29.72419 -27.60238 1.000 47.79795 ? 675 HOH   A O   1 
HETATM 1932 O O   . HOH   C 3 .   ? -19.88558 -11.92734 -25.65967 1.000 49.84338 ? 676 HOH   A O   1 
HETATM 1933 O O   . HOH   C 3 .   ? 0.739     -3.178    -31.348   1.000 36.88546 ? 677 HOH   A O   1 
HETATM 1934 O O   . HOH   C 3 .   ? -16.02727 -12.58391 -7.06245  1.000 47.91152 ? 678 HOH   A O   1 
HETATM 1935 O O   . HOH   C 3 .   ? -11.17250 -21.07110 -25.74992 1.000 49.12208 ? 679 HOH   A O   1 
HETATM 1936 O O   . HOH   C 3 .   ? 18.29843  -6.17880  -28.41400 1.000 47.78114 ? 680 HOH   A O   1 
HETATM 1937 O O   . HOH   C 3 .   ? 11.03216  -13.21384 -9.68066  1.000 49.06797 ? 681 HOH   A O   1 
HETATM 1938 O O   . HOH   C 3 .   ? 21.17561  -7.88421  -14.99268 1.000 47.84099 ? 682 HOH   A O   1 
HETATM 1939 O O   . HOH   C 3 .   ? 19.12314  -1.56204  -21.02359 1.000 38.66223 ? 683 HOH   A O   1 
HETATM 1940 O O   . HOH   C 3 .   ? -18.50673 -6.29361  -22.92417 1.000 47.75635 ? 684 HOH   A O   1 
HETATM 1941 O O   . HOH   C 3 .   ? -14.02485 -14.10361 -10.79590 1.000 38.22061 ? 685 HOH   A O   1 
HETATM 1942 O O   . HOH   C 3 .   ? 21.61821  -21.57259 -25.18701 1.000 48.33774 ? 686 HOH   A O   1 
HETATM 1943 O O   . HOH   C 3 .   ? 9.02125   -13.59234 -9.69493  1.000 40.51796 ? 687 HOH   A O   1 
HETATM 1944 O O   . HOH   C 3 .   ? -10.59098 -11.30715 1.61592   1.000 48.72125 ? 688 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   ? 0.68720 0.82003 0.56447 -0.07907 -0.04953 -0.23301 16  GLU A N   
2    C CA  . GLU A 9   ? 0.73567 0.84179 0.60244 -0.05229 -0.04569 -0.22287 16  GLU A CA  
3    C C   . GLU A 9   ? 0.63385 0.74170 0.52229 -0.03728 -0.04653 -0.20281 16  GLU A C   
4    O O   . GLU A 9   ? 0.61344 0.76414 0.51436 -0.02374 -0.05558 -0.18913 16  GLU A O   
5    C CB  . GLU A 9   ? 0.72002 0.85893 0.57371 -0.03262 -0.05242 -0.21850 16  GLU A CB  
6    C CG  . GLU A 9   ? 0.96558 1.06705 0.79875 -0.01417 -0.04303 -0.21647 16  GLU A CG  
7    C CD  . GLU A 9   ? 0.92593 1.02421 0.77024 0.01094  -0.04031 -0.19245 16  GLU A CD  
8    O OE1 . GLU A 9   ? 1.00247 1.12494 0.86579 0.01535  -0.04634 -0.17788 16  GLU A OE1 
9    O OE2 . GLU A 9   ? 1.00574 1.07612 0.84106 0.02523  -0.03034 -0.18593 16  GLU A OE2 
10   N N   . VAL A 10  ? 0.45267 0.50861 0.34455 -0.03677 -0.03513 -0.19554 17  VAL A N   
11   C CA  . VAL A 10  ? 0.42116 0.47193 0.33487 -0.02602 -0.03398 -0.17388 17  VAL A CA  
12   C C   . VAL A 10  ? 0.45157 0.48583 0.36402 -0.00073 -0.02879 -0.15704 17  VAL A C   
13   O O   . VAL A 10  ? 0.46209 0.46216 0.36099 0.00563  -0.01959 -0.16054 17  VAL A O   
14   C CB  . VAL A 10  ? 0.52030 0.53070 0.43728 -0.04170 -0.02486 -0.17645 17  VAL A CB  
15   C CG1 . VAL A 10  ? 0.40005 0.40778 0.33737 -0.02927 -0.02424 -0.15464 17  VAL A CG1 
16   C CG2 . VAL A 10  ? 0.62159 0.64979 0.53947 -0.07293 -0.02716 -0.19554 17  VAL A CG2 
17   N N   . GLU A 11  ? 0.35737 0.41573 0.28227 0.01321  -0.03292 -0.13962 18  GLU A N   
18   C CA  . GLU A 11  ? 0.32030 0.36743 0.24628 0.03095  -0.02639 -0.12480 18  GLU A CA  
19   C C   . GLU A 11  ? 0.34916 0.38330 0.29357 0.03198  -0.02311 -0.11245 18  GLU A C   
20   O O   . GLU A 11  ? 0.28629 0.33278 0.24331 0.02647  -0.02788 -0.10728 18  GLU A O   
21   C CB  . GLU A 11  ? 0.32775 0.40072 0.24752 0.04383  -0.02903 -0.11442 18  GLU A CB  
22   C CG  . GLU A 11  ? 0.36441 0.45159 0.26172 0.04803  -0.03135 -0.12406 18  GLU A CG  
23   C CD  . GLU A 11  ? 0.52375 0.62989 0.40839 0.06456  -0.03143 -0.11045 18  GLU A CD  
24   O OE1 . GLU A 11  ? 0.52741 0.65666 0.41475 0.06942  -0.03802 -0.10336 18  GLU A OE1 
25   O OE2 . GLU A 11  ? 0.63075 0.72691 0.50019 0.07415  -0.02308 -0.10612 18  GLU A OE2 
26   N N   . THR A 12  ? 0.29707 0.31144 0.24251 0.04040  -0.01511 -0.10824 19  THR A N   
27   C CA  . THR A 12  ? 0.27989 0.28749 0.24065 0.04325  -0.01250 -0.09761 19  THR A CA  
28   C C   . THR A 12  ? 0.26293 0.28612 0.23060 0.05180  -0.00887 -0.08686 19  THR A C   
29   O O   . THR A 12  ? 0.26987 0.29705 0.23020 0.05893  -0.00329 -0.08828 19  THR A O   
30   C CB  . THR A 12  ? 0.30761 0.28603 0.26281 0.04823  -0.00563 -0.10106 19  THR A CB  
31   O OG1 . THR A 12  ? 0.32945 0.28371 0.27194 0.03556  -0.00502 -0.11318 19  THR A OG1 
32   C CG2 . THR A 12  ? 0.28561 0.26314 0.25467 0.05316  -0.00452 -0.08962 19  THR A CG2 
33   N N   . PHE A 13  ? 0.24125 0.27233 0.22130 0.04894  -0.01035 -0.07748 20  PHE A N   
34   C CA  . PHE A 13  ? 0.26885 0.31087 0.25276 0.05052  -0.00488 -0.06956 20  PHE A CA  
35   C C   . PHE A 13  ? 0.30461 0.35082 0.30350 0.04914  -0.00386 -0.06510 20  PHE A C   
36   O O   . PHE A 13  ? 0.25263 0.29186 0.25762 0.04731  -0.00842 -0.06392 20  PHE A O   
37   C CB  . PHE A 13  ? 0.24107 0.28556 0.21801 0.04857  -0.00547 -0.06314 20  PHE A CB  
38   C CG  . PHE A 13  ? 0.26006 0.30819 0.22027 0.05348  -0.00814 -0.06599 20  PHE A CG  
39   C CD1 . PHE A 13  ? 0.29815 0.35442 0.25812 0.05150  -0.01754 -0.07189 20  PHE A CD1 
40   C CD2 . PHE A 13  ? 0.29931 0.34675 0.24294 0.05904  -0.00071 -0.06327 20  PHE A CD2 
41   C CE1 . PHE A 13  ? 0.26495 0.33480 0.20949 0.05640  -0.02172 -0.07609 20  PHE A CE1 
42   C CE2 . PHE A 13  ? 0.37848 0.43253 0.30337 0.06645  -0.00385 -0.06510 20  PHE A CE2 
43   C CZ  . PHE A 13  ? 0.33629 0.40469 0.26220 0.06584  -0.01550 -0.07199 20  PHE A CZ  
44   N N   . ALA A 14  ? 0.24706 0.30815 0.25092 0.04857  0.00276  -0.06331 21  ALA A N   
45   C CA  . ALA A 14  ? 0.24510 0.32012 0.26243 0.04522  0.00310  -0.06056 21  ALA A CA  
46   C C   . ALA A 14  ? 0.28552 0.35588 0.30086 0.03361  0.00532  -0.05635 21  ALA A C   
47   O O   . ALA A 14  ? 0.28293 0.34550 0.28616 0.02876  0.01242  -0.05488 21  ALA A O   
48   C CB  . ALA A 14  ? 0.27722 0.38090 0.30263 0.04771  0.00939  -0.06367 21  ALA A CB  
49   N N   . PHE A 15  ? 0.24019 0.31026 0.26286 0.03088  0.00097  -0.05380 22  PHE A N   
50   C CA  . PHE A 15  ? 0.25307 0.31782 0.27202 0.02027  0.00538  -0.05139 22  PHE A CA  
51   C C   . PHE A 15  ? 0.26355 0.34414 0.28325 0.00828  0.01522  -0.05595 22  PHE A C   
52   O O   . PHE A 15  ? 0.26798 0.37742 0.29938 0.00968  0.01513  -0.06056 22  PHE A O   
53   C CB  . PHE A 15  ? 0.25892 0.32542 0.28572 0.01948  -0.00038 -0.04930 22  PHE A CB  
54   C CG  . PHE A 15  ? 0.26936 0.32063 0.29431 0.02475  -0.00648 -0.04527 22  PHE A CG  
55   C CD1 . PHE A 15  ? 0.26768 0.30613 0.28260 0.02487  -0.00449 -0.04184 22  PHE A CD1 
56   C CD2 . PHE A 15  ? 0.25366 0.30436 0.28494 0.02996  -0.01244 -0.04484 22  PHE A CD2 
57   C CE1 . PHE A 15  ? 0.25477 0.29193 0.27160 0.02885  -0.01023 -0.03963 22  PHE A CE1 
58   C CE2 . PHE A 15  ? 0.24531 0.28644 0.27611 0.02942  -0.01609 -0.04322 22  PHE A CE2 
59   C CZ  . PHE A 15  ? 0.23159 0.27192 0.25802 0.02816  -0.01592 -0.04141 22  PHE A CZ  
60   N N   . GLN A 16  ? 0.26541 0.32726 0.27060 -0.00361 0.02546  -0.05516 23  GLN A N   
61   C CA  . GLN A 16  ? 0.27716 0.35250 0.28239 -0.02307 0.03669  -0.06234 23  GLN A CA  
62   C C   . GLN A 16  ? 0.25081 0.35953 0.27447 -0.02764 0.02924  -0.06790 23  GLN A C   
63   O O   . GLN A 16  ? 0.28636 0.38955 0.31351 -0.01938 0.01993  -0.06395 23  GLN A O   
64   C CB  . GLN A 16  ? 0.33953 0.37531 0.31905 -0.03587 0.05142  -0.06065 23  GLN A CB  
65   C CG  . GLN A 16  ? 0.38716 0.39189 0.34226 -0.03142 0.06301  -0.05450 23  GLN A CG  
66   C CD  . GLN A 16  ? 0.50479 0.45889 0.42682 -0.03510 0.07820  -0.04893 23  GLN A CD  
67   O OE1 . GLN A 16  ? 0.55221 0.48240 0.45306 -0.05333 0.09799  -0.05201 23  GLN A OE1 
68   N NE2 . GLN A 16  ? 0.44960 0.38586 0.36481 -0.01775 0.07105  -0.04095 23  GLN A NE2 
69   N N   . ALA A 17  ? 0.24106 0.38995 0.27631 -0.04026 0.03357  -0.07725 24  ALA A N   
70   C CA  . ALA A 17  ? 0.28627 0.47830 0.33830 -0.04158 0.02535  -0.08290 24  ALA A CA  
71   C C   . ALA A 17  ? 0.26769 0.44077 0.31043 -0.05321 0.02554  -0.08442 24  ALA A C   
72   O O   . ALA A 17  ? 0.30765 0.49496 0.35766 -0.04315 0.01463  -0.08215 24  ALA A O   
73   C CB  . ALA A 17  ? 0.30406 0.55177 0.36973 -0.05724 0.03153  -0.09521 24  ALA A CB  
74   N N   . GLU A 18  ? 0.30861 0.44431 0.33085 -0.07255 0.03970  -0.08749 25  GLU A N   
75   C CA  . GLU A 18  ? 0.32470 0.43693 0.33335 -0.08336 0.04279  -0.09025 25  GLU A CA  
76   C C   . GLU A 18  ? 0.31943 0.40255 0.32409 -0.06113 0.03334  -0.07774 25  GLU A C   
77   O O   . GLU A 18  ? 0.30732 0.39175 0.31127 -0.06145 0.02877  -0.07873 25  GLU A O   
78   C CB  . GLU A 18  ? 0.39106 0.45785 0.37096 -0.10647 0.06424  -0.09550 25  GLU A CB  
79   C CG  . GLU A 18  ? 0.43240 0.52636 0.41375 -0.13757 0.07778  -0.11097 25  GLU A CG  
80   C CD  . GLU A 18  ? 0.54785 0.65230 0.53472 -0.13361 0.08259  -0.10761 25  GLU A CD  
81   O OE1 . GLU A 18  ? 0.44557 0.53651 0.43451 -0.10623 0.07404  -0.09418 25  GLU A OE1 
82   O OE2 . GLU A 18  ? 0.62027 0.74861 0.60876 -0.15982 0.09580  -0.11978 25  GLU A OE2 
83   N N   . ILE A 19  ? 0.27870 0.33990 0.28055 -0.04331 0.03078  -0.06724 26  ILE A N   
84   C CA  . ILE A 19  ? 0.29087 0.33466 0.29224 -0.02548 0.02219  -0.05751 26  ILE A CA  
85   C C   . ILE A 19  ? 0.29031 0.36303 0.31130 -0.01420 0.00814  -0.05549 26  ILE A C   
86   O O   . ILE A 19  ? 0.25572 0.32498 0.27767 -0.00917 0.00301  -0.05185 26  ILE A O   
87   C CB  . ILE A 19  ? 0.31838 0.33876 0.31036 -0.01219 0.02345  -0.04948 26  ILE A CB  
88   C CG1 . ILE A 19  ? 0.36228 0.34495 0.32636 -0.01754 0.03963  -0.04784 26  ILE A CG1 
89   C CG2 . ILE A 19  ? 0.31031 0.32736 0.30732 0.00307  0.01357  -0.04225 26  ILE A CG2 
90   C CD1 . ILE A 19  ? 0.40928 0.36552 0.35706 -0.01993 0.04650  -0.04714 26  ILE A CD1 
91   N N   . ALA A 20  ? 0.24915 0.34742 0.28248 -0.00840 0.00380  -0.05705 27  ALA A N   
92   C CA  . ALA A 20  ? 0.24200 0.36084 0.28671 0.00553  -0.00609 -0.05397 27  ALA A CA  
93   C C   . ALA A 20  ? 0.24875 0.39139 0.29617 0.00104  -0.00911 -0.05698 27  ALA A C   
94   O O   . ALA A 20  ? 0.23064 0.37302 0.27836 0.01254  -0.01539 -0.05084 27  ALA A O   
95   C CB  . ALA A 20  ? 0.23301 0.37581 0.28614 0.01498  -0.00721 -0.05589 27  ALA A CB  
96   N N   . GLN A 21  ? 0.24143 0.40436 0.28829 -0.01743 -0.00346 -0.06729 28  GLN A N   
97   C CA  . GLN A 21  ? 0.21935 0.40894 0.26654 -0.02520 -0.00640 -0.07335 28  GLN A CA  
98   C C   . GLN A 21  ? 0.29478 0.44971 0.32885 -0.02693 -0.00532 -0.06940 28  GLN A C   
99   O O   . GLN A 21  ? 0.27214 0.44044 0.30590 -0.02033 -0.01175 -0.06716 28  GLN A O   
100  C CB  . GLN A 21  ? 0.22983 0.44754 0.27737 -0.05151 0.00177  -0.08915 28  GLN A CB  
101  C CG  . GLN A 21  ? 0.43594 0.69955 0.48663 -0.06126 -0.00309 -0.09960 28  GLN A CG  
102  C CD  . GLN A 21  ? 0.68835 0.96760 0.73378 -0.09688 0.00868  -0.11886 28  GLN A CD  
103  O OE1 . GLN A 21  ? 0.65084 0.91273 0.69233 -0.11251 0.02113  -0.12333 28  GLN A OE1 
104  N NE2 . GLN A 21  ? 0.76222 1.07269 0.80460 -0.11175 0.00627  -0.13124 28  GLN A NE2 
105  N N   . LEU A 22  ? 0.25864 0.37059 0.27969 -0.03297 0.00357  -0.06767 29  LEU A N   
106  C CA  . LEU A 22  ? 0.26617 0.34795 0.27470 -0.03066 0.00583  -0.06331 29  LEU A CA  
107  C C   . LEU A 22  ? 0.27440 0.35525 0.29096 -0.01182 -0.00344 -0.05179 29  LEU A C   
108  O O   . LEU A 22  ? 0.24580 0.32592 0.25864 -0.00890 -0.00547 -0.04919 29  LEU A O   
109  C CB  . LEU A 22  ? 0.27816 0.31676 0.26912 -0.03317 0.01769  -0.06129 29  LEU A CB  
110  C CG  . LEU A 22  ? 0.28340 0.29427 0.26244 -0.02356 0.02032  -0.05462 29  LEU A CG  
111  C CD1 . LEU A 22  ? 0.35613 0.35924 0.32002 -0.03604 0.02696  -0.06304 29  LEU A CD1 
112  C CD2 . LEU A 22  ? 0.32904 0.30553 0.29254 -0.01457 0.02926  -0.04822 29  LEU A CD2 
113  N N   . MET A 23  ? 0.24227 0.32111 0.26743 -0.00098 -0.00740 -0.04585 30  MET A N   
114  C CA  . MET A 23  ? 0.22985 0.30206 0.25945 0.01147  -0.01287 -0.03707 30  MET A CA  
115  C C   . MET A 23  ? 0.21226 0.30306 0.24383 0.01921  -0.01821 -0.03415 30  MET A C   
116  O O   . MET A 23  ? 0.24348 0.32499 0.27143 0.02464  -0.01904 -0.02742 30  MET A O   
117  C CB  . MET A 23  ? 0.23419 0.29843 0.26861 0.01760  -0.01434 -0.03495 30  MET A CB  
118  C CG  . MET A 23  ? 0.25298 0.30285 0.28211 0.01425  -0.00971 -0.03625 30  MET A CG  
119  S SD  . MET A 23  ? 0.28011 0.32504 0.31223 0.02057  -0.01256 -0.03565 30  MET A SD  
120  C CE  . MET A 23  ? 0.30590 0.34692 0.34336 0.02354  -0.01703 -0.03219 30  MET A CE  
121  N N   . SER A 24  ? 0.21247 0.33254 0.24829 0.02121  -0.02093 -0.03859 31  SER A N   
122  C CA  . SER A 24  ? 0.21220 0.35578 0.24635 0.03435  -0.02621 -0.03448 31  SER A CA  
123  C C   . SER A 24  ? 0.26043 0.41364 0.28704 0.02815  -0.02702 -0.03639 31  SER A C   
124  O O   . SER A 24  ? 0.28083 0.43403 0.29964 0.04058  -0.02948 -0.02804 31  SER A O   
125  C CB  . SER A 24  ? 0.30586 0.49147 0.34789 0.03997  -0.02932 -0.03995 31  SER A CB  
126  O OG  . SER A 24  ? 0.47603 0.65149 0.52308 0.04572  -0.02722 -0.03916 31  SER A OG  
127  N N   . LEU A 25  ? 0.22200 0.37910 0.24653 0.00890  -0.02308 -0.04750 32  LEU A N   
128  C CA  . LEU A 25  ? 0.22457 0.38611 0.23823 0.00136  -0.02236 -0.05167 32  LEU A CA  
129  C C   . LEU A 25  ? 0.30809 0.43467 0.31407 0.00727  -0.01920 -0.04190 32  LEU A C   
130  O O   . LEU A 25  ? 0.28269 0.41442 0.28005 0.01229  -0.02075 -0.03831 32  LEU A O   
131  C CB  . LEU A 25  ? 0.31851 0.47959 0.32565 -0.02294 -0.01486 -0.06729 32  LEU A CB  
132  C CG  . LEU A 25  ? 0.52291 0.73318 0.53613 -0.03673 -0.01704 -0.08186 32  LEU A CG  
133  C CD1 . LEU A 25  ? 0.55279 0.74971 0.55312 -0.06679 -0.00510 -0.09891 32  LEU A CD1 
134  C CD2 . LEU A 25  ? 0.57634 0.83589 0.59052 -0.02614 -0.02770 -0.08216 32  LEU A CD2 
135  N N   . ILE A 26  ? 0.28097 0.37741 0.28986 0.00722  -0.01462 -0.03778 33  ILE A N   
136  C CA  . ILE A 26  ? 0.24640 0.32069 0.25205 0.01212  -0.01141 -0.02970 33  ILE A CA  
137  C C   . ILE A 26  ? 0.29943 0.37445 0.30636 0.02362  -0.01464 -0.01907 33  ILE A C   
138  O O   . ILE A 26  ? 0.27881 0.34767 0.27906 0.02606  -0.01194 -0.01333 33  ILE A O   
139  C CB  . ILE A 26  ? 0.22999 0.28448 0.23987 0.01157  -0.00736 -0.02850 33  ILE A CB  
140  C CG1 . ILE A 26  ? 0.28947 0.32950 0.28751 0.00395  0.00057  -0.03567 33  ILE A CG1 
141  C CG2 . ILE A 26  ? 0.19773 0.24414 0.21088 0.01699  -0.00576 -0.02064 33  ILE A CG2 
142  C CD1 . ILE A 26  ? 0.31494 0.33887 0.31265 0.00785  0.00444  -0.03355 33  ILE A CD1 
143  N N   . ILE A 27  ? 0.25930 0.33783 0.27103 0.03133  -0.01818 -0.01607 34  ILE A N   
144  C CA  . ILE A 27  ? 0.31346 0.37853 0.31918 0.04267  -0.01711 -0.00539 34  ILE A CA  
145  C C   . ILE A 27  ? 0.32121 0.40221 0.31399 0.05511  -0.01953 0.00012  34  ILE A C   
146  O O   . ILE A 27  ? 0.34300 0.40722 0.32287 0.06238  -0.01515 0.01042  34  ILE A O   
147  C CB  . ILE A 27  ? 0.31624 0.37104 0.32590 0.04854  -0.01746 -0.00468 34  ILE A CB  
148  C CG1 . ILE A 27  ? 0.30597 0.34537 0.32480 0.03726  -0.01509 -0.00885 34  ILE A CG1 
149  C CG2 . ILE A 27  ? 0.42351 0.45694 0.41836 0.06286  -0.01345 0.00604  34  ILE A CG2 
150  C CD1 . ILE A 27  ? 0.30479 0.33852 0.32705 0.04027  -0.01602 -0.01213 34  ILE A CD1 
151  N N   . ASN A 28  ? 0.29920 0.41577 0.29372 0.05707  -0.02574 -0.00698 35  ASN A N   
152  C CA  . ASN A 28  ? 0.31551 0.45932 0.29806 0.07384  -0.03031 -0.00195 35  ASN A CA  
153  C C   . ASN A 28  ? 0.32869 0.49262 0.30216 0.06731  -0.03214 -0.00655 35  ASN A C   
154  O O   . ASN A 28  ? 0.38532 0.56428 0.34335 0.08351  -0.03463 0.00129  35  ASN A O   
155  C CB  . ASN A 28  ? 0.35317 0.53901 0.34418 0.08189  -0.03702 -0.00820 35  ASN A CB  
156  C CG  . ASN A 28  ? 0.51766 0.68425 0.51201 0.09468  -0.03456 -0.00239 35  ASN A CG  
157  O OD1 . ASN A 28  ? 0.48648 0.61017 0.46941 0.10395  -0.02828 0.00883  35  ASN A OD1 
158  N ND2 . ASN A 28  ? 0.59123 0.78838 0.59939 0.09315  -0.03780 -0.01132 35  ASN A ND2 
159  N N   . THR A 29  ? 0.26331 0.42507 0.24152 0.04615  -0.02979 -0.01870 36  THR A N   
160  C CA  . THR A 29  ? 0.29171 0.46990 0.25796 0.03796  -0.03017 -0.02638 36  THR A CA  
161  C C   . THR A 29  ? 0.36054 0.51250 0.31316 0.04462  -0.02453 -0.01490 36  THR A C   
162  O O   . THR A 29  ? 0.35197 0.47008 0.30910 0.04282  -0.01761 -0.00804 36  THR A O   
163  C CB  . THR A 29  ? 0.35436 0.52551 0.32302 0.01399  -0.02519 -0.04290 36  THR A CB  
164  O OG1 . THR A 29  ? 0.34490 0.54021 0.32502 0.00443  -0.02795 -0.05385 36  THR A OG1 
165  C CG2 . THR A 29  ? 0.34378 0.52703 0.29554 0.00335  -0.02374 -0.05383 36  THR A CG2 
166  N N   . PHE A 30  ? 0.31721 0.49015 0.25299 0.05182  -0.02723 -0.01349 37  PHE A N   
167  C CA  . PHE A 30  ? 0.33369 0.48374 0.25440 0.05628  -0.02007 -0.00354 37  PHE A CA  
168  C C   . PHE A 30  ? 0.32733 0.46138 0.24798 0.03874  -0.01301 -0.01439 37  PHE A C   
169  O O   . PHE A 30  ? 0.32669 0.47654 0.24096 0.02635  -0.01438 -0.03025 37  PHE A O   
170  C CB  . PHE A 30  ? 0.30081 0.47783 0.19922 0.07108  -0.02441 0.00160  37  PHE A CB  
171  C CG  . PHE A 30  ? 0.37099 0.52370 0.25134 0.07566  -0.01516 0.01281  37  PHE A CG  
172  C CD1 . PHE A 30  ? 0.41538 0.53306 0.29071 0.08568  -0.00616 0.03123  37  PHE A CD1 
173  C CD2 . PHE A 30  ? 0.32964 0.49244 0.19620 0.06765  -0.01333 0.00368  37  PHE A CD2 
174  C CE1 . PHE A 30  ? 0.44183 0.53918 0.30103 0.08694  0.00466  0.04121  37  PHE A CE1 
175  C CE2 . PHE A 30  ? 0.38995 0.53278 0.23994 0.07239  -0.00350 0.01424  37  PHE A CE2 
176  C CZ  . PHE A 30  ? 0.36921 0.48133 0.21677 0.08164  0.00560  0.03343  37  PHE A CZ  
177  N N   . TYR A 31  ? 0.28661 0.39000 0.21235 0.03779  -0.00414 -0.00668 38  TYR A N   
178  C CA  . TYR A 31  ? 0.29402 0.38164 0.21915 0.02781  0.00391  -0.01462 38  TYR A CA  
179  C C   . TYR A 31  ? 0.29409 0.36487 0.22313 0.03237  0.01276  -0.00242 38  TYR A C   
180  O O   . TYR A 31  ? 0.30882 0.37056 0.25408 0.03175  0.01395  0.00297  38  TYR A O   
181  C CB  . TYR A 31  ? 0.29575 0.37443 0.23297 0.01844  0.00403  -0.02430 38  TYR A CB  
182  C CG  . TYR A 31  ? 0.35892 0.41581 0.28870 0.01385  0.01429  -0.03089 38  TYR A CG  
183  C CD1 . TYR A 31  ? 0.37686 0.42851 0.28552 0.00584  0.01939  -0.04389 38  TYR A CD1 
184  C CD2 . TYR A 31  ? 0.33552 0.37786 0.27627 0.01908  0.01982  -0.02459 38  TYR A CD2 
185  C CE1 . TYR A 31  ? 0.45452 0.47749 0.34974 0.00578  0.03174  -0.04892 38  TYR A CE1 
186  C CE2 . TYR A 31  ? 0.38151 0.40515 0.31190 0.02186  0.03016  -0.02850 38  TYR A CE2 
187  C CZ  . TYR A 31  ? 0.41521 0.42448 0.32108 0.01660  0.03712  -0.03981 38  TYR A CZ  
188  O OH  . TYR A 31  ? 0.51841 0.50046 0.40770 0.02326  0.05027  -0.04277 38  TYR A OH  
189  N N   . SER A 32  ? 0.28477 0.35550 0.19869 0.03512  0.01936  0.00025  39  SER A N   
190  C CA  . SER A 32  ? 0.31791 0.38053 0.23501 0.03748  0.02915  0.01179  39  SER A CA  
191  C C   . SER A 32  ? 0.32738 0.38669 0.25928 0.03442  0.03622  0.00849  39  SER A C   
192  O O   . SER A 32  ? 0.37268 0.43452 0.31705 0.03254  0.04247  0.01595  39  SER A O   
193  C CB  . SER A 32  ? 0.36964 0.43610 0.26407 0.04250  0.03517  0.01611  39  SER A CB  
194  O OG  . SER A 32  ? 0.33402 0.40860 0.21183 0.05014  0.02824  0.02105  39  SER A OG  
195  N N   . ASN A 33  ? 0.29630 0.35069 0.22480 0.03414  0.03664  -0.00269 40  ASN A N   
196  C CA  . ASN A 33  ? 0.33457 0.38606 0.26979 0.03891  0.04476  -0.00428 40  ASN A CA  
197  C C   . ASN A 33  ? 0.29742 0.35185 0.25451 0.03799  0.04022  -0.00282 40  ASN A C   
198  O O   . ASN A 33  ? 0.29862 0.34313 0.25454 0.04145  0.04066  -0.00831 40  ASN A O   
199  C CB  . ASN A 33  ? 0.32224 0.35562 0.23537 0.04145  0.05061  -0.01574 40  ASN A CB  
200  C CG  . ASN A 33  ? 0.37854 0.40487 0.29103 0.05406  0.06121  -0.01536 40  ASN A CG  
201  O OD1 . ASN A 33  ? 0.34575 0.39173 0.26990 0.06212  0.06655  -0.00773 40  ASN A OD1 
202  N ND2 . ASN A 33  ? 0.43654 0.43564 0.33314 0.05663  0.06588  -0.02348 40  ASN A ND2 
203  N N   . LYS A 34  ? 0.25704 0.27432 0.20786 -0.00759 -0.02303 0.01219  41  LYS A N   
204  C CA  . LYS A 34  ? 0.25247 0.28481 0.23233 -0.00599 -0.01467 0.01257  41  LYS A CA  
205  C C   . LYS A 34  ? 0.28341 0.30616 0.26242 -0.00383 -0.00515 0.00308  41  LYS A C   
206  O O   . LYS A 34  ? 0.30038 0.33116 0.29713 -0.00452 -0.00209 0.00158  41  LYS A O   
207  C CB  . LYS A 34  ? 0.25426 0.29592 0.24858 0.00197  -0.00658 0.01929  41  LYS A CB  
208  C CG  . LYS A 34  ? 0.24455 0.30260 0.24815 0.00365  -0.01436 0.03075  41  LYS A CG  
209  C CD  . LYS A 34  ? 0.24617 0.30280 0.25572 0.01428  -0.00688 0.03626  41  LYS A CD  
210  C CE  . LYS A 34  ? 0.28702 0.36163 0.30599 0.02007  -0.01374 0.04889  41  LYS A CE  
211  N NZ  . LYS A 34  ? 0.25483 0.35267 0.29605 0.02604  -0.01271 0.05342  41  LYS A NZ  
212  N N   . GLU A 35  ? 0.28166 0.28978 0.23982 0.00062  0.00003  -0.00203 42  GLU A N   
213  C CA  . GLU A 35  ? 0.25227 0.25799 0.21408 0.00484  0.01024  -0.00773 42  GLU A CA  
214  C C   . GLU A 35  ? 0.30846 0.30796 0.27124 0.00087  0.00472  -0.01444 42  GLU A C   
215  O O   . GLU A 35  ? 0.29595 0.29707 0.26714 0.00391  0.01184  -0.01805 42  GLU A O   
216  C CB  . GLU A 35  ? 0.28218 0.27900 0.22047 0.01409  0.01811  -0.00899 42  GLU A CB  
217  C CG  . GLU A 35  ? 0.33002 0.30256 0.23151 0.01736  0.00908  -0.01629 42  GLU A CG  
218  C CD  . GLU A 35  ? 0.47947 0.44342 0.35107 0.03234  0.01931  -0.01677 42  GLU A CD  
219  O OE1 . GLU A 35  ? 0.45125 0.42765 0.32436 0.03555  0.02719  -0.00780 42  GLU A OE1 
220  O OE2 . GLU A 35  ? 0.65329 0.59745 0.49793 0.04263  0.01996  -0.02508 42  GLU A OE2 
221  N N   . ILE A 36  ? 0.27836 0.27159 0.23383 -0.00737 -0.00933 -0.01408 43  ILE A N   
222  C CA  . ILE A 36  ? 0.30746 0.29194 0.26216 -0.01340 -0.01643 -0.01791 43  ILE A CA  
223  C C   . ILE A 36  ? 0.27473 0.27908 0.25856 -0.01511 -0.01050 -0.01522 43  ILE A C   
224  O O   . ILE A 36  ? 0.27127 0.27000 0.25600 -0.01819 -0.01291 -0.01788 43  ILE A O   
225  C CB  . ILE A 36  ? 0.34947 0.32374 0.29198 -0.02636 -0.03627 -0.01401 43  ILE A CB  
226  C CG1 . ILE A 36  ? 0.40879 0.41286 0.37661 -0.03332 -0.04079 -0.00109 43  ILE A CG1 
227  C CG2 . ILE A 36  ? 0.40187 0.34443 0.30360 -0.02328 -0.04494 -0.02020 43  ILE A CG2 
228  C CD1 . ILE A 36  ? 0.53960 0.56575 0.53351 -0.04287 -0.04528 0.00819  43  ILE A CD1 
229  N N   . PHE A 37  ? 0.25492 0.27834 0.25811 -0.01170 -0.00348 -0.01015 44  PHE A N   
230  C CA  . PHE A 37  ? 0.25102 0.28756 0.27326 -0.00976 0.00210  -0.00915 44  PHE A CA  
231  C C   . PHE A 37  ? 0.26066 0.28828 0.28180 -0.00674 0.00815  -0.01669 44  PHE A C   
232  O O   . PHE A 37  ? 0.22012 0.25120 0.24801 -0.00791 0.00819  -0.01763 44  PHE A O   
233  C CB  . PHE A 37  ? 0.22424 0.27089 0.25718 -0.00252 0.00804  -0.00499 44  PHE A CB  
234  C CG  . PHE A 37  ? 0.28770 0.32359 0.31836 0.00185  0.01502  -0.00885 44  PHE A CG  
235  C CD1 . PHE A 37  ? 0.26989 0.30027 0.29206 0.00232  0.01639  -0.00662 44  PHE A CD1 
236  C CD2 . PHE A 37  ? 0.23266 0.26459 0.26911 0.00397  0.01878  -0.01280 44  PHE A CD2 
237  C CE1 . PHE A 37  ? 0.28338 0.30894 0.30767 0.00345  0.02217  -0.00556 44  PHE A CE1 
238  C CE2 . PHE A 37  ? 0.19748 0.22125 0.23496 0.00357  0.02165  -0.01299 44  PHE A CE2 
239  C CZ  . PHE A 37  ? 0.27376 0.29654 0.30754 0.00260  0.02374  -0.00804 44  PHE A CZ  
240  N N   . LEU A 38  ? 0.24892 0.26883 0.26278 -0.00235 0.01353  -0.01985 45  LEU A N   
241  C CA  . LEU A 38  ? 0.26662 0.28557 0.28497 0.00083  0.01905  -0.02347 45  LEU A CA  
242  C C   . LEU A 38  ? 0.27865 0.28684 0.28610 0.00150  0.01554  -0.02816 45  LEU A C   
243  O O   . LEU A 38  ? 0.25365 0.26355 0.26838 0.00206  0.01641  -0.03005 45  LEU A O   
244  C CB  . LEU A 38  ? 0.25816 0.28022 0.27625 0.00532  0.02652  -0.02055 45  LEU A CB  
245  C CG  . LEU A 38  ? 0.24067 0.27074 0.27098 0.00716  0.03144  -0.01950 45  LEU A CG  
246  C CD1 . LEU A 38  ? 0.24724 0.27900 0.29217 0.00141  0.02761  -0.01977 45  LEU A CD1 
247  C CD2 . LEU A 38  ? 0.27866 0.32004 0.31273 0.01043  0.03942  -0.01123 45  LEU A CD2 
248  N N   . ARG A 39  ? 0.24831 0.24078 0.23449 0.00174  0.00974  -0.03016 46  ARG A N   
249  C CA  . ARG A 39  ? 0.25597 0.22826 0.22552 0.00217  0.00301  -0.03484 46  ARG A CA  
250  C C   . ARG A 39  ? 0.29716 0.27383 0.27900 -0.00829 -0.00427 -0.03157 46  ARG A C   
251  O O   . ARG A 39  ? 0.32410 0.29228 0.30374 -0.00733 -0.00583 -0.03363 46  ARG A O   
252  C CB  . ARG A 39  ? 0.32128 0.26719 0.25897 0.00241  -0.00661 -0.03797 46  ARG A CB  
253  C CG  . ARG A 39  ? 0.46142 0.37525 0.37517 0.00080  -0.01858 -0.04279 46  ARG A CG  
254  C CD  . ARG A 39  ? 0.50430 0.38577 0.38326 -0.00404 -0.03463 -0.04541 46  ARG A CD  
255  N NE  . ARG A 39  ? 0.53457 0.42979 0.42879 -0.02321 -0.04731 -0.03608 46  ARG A NE  
256  C CZ  . ARG A 39  ? 0.66131 0.54429 0.53706 -0.03006 -0.06035 -0.03441 46  ARG A CZ  
257  N NH1 . ARG A 39  ? 0.57573 0.42732 0.41117 -0.01869 -0.06249 -0.04326 46  ARG A NH1 
258  N NH2 . ARG A 39  ? 0.54243 0.44690 0.43960 -0.04731 -0.07151 -0.02239 46  ARG A NH2 
259  N N   . GLU A 40  ? 0.20869 0.20150 0.20400 -0.01670 -0.00781 -0.02450 47  GLU A N   
260  C CA  . GLU A 40  ? 0.25505 0.25887 0.26280 -0.02544 -0.01289 -0.01743 47  GLU A CA  
261  C C   . GLU A 40  ? 0.24650 0.26302 0.26801 -0.01965 -0.00363 -0.01853 47  GLU A C   
262  O O   . GLU A 40  ? 0.25810 0.27398 0.28107 -0.02303 -0.00620 -0.01611 47  GLU A O   
263  C CB  . GLU A 40  ? 0.28154 0.30685 0.30228 -0.03235 -0.01708 -0.00650 47  GLU A CB  
264  C CG  . GLU A 40  ? 0.26026 0.27293 0.26678 -0.04135 -0.03078 -0.00374 47  GLU A CG  
265  C CD  . GLU A 40  ? 0.45453 0.43757 0.44068 -0.05186 -0.04598 -0.00503 47  GLU A CD  
266  O OE1 . GLU A 40  ? 0.37882 0.36463 0.37296 -0.05842 -0.04875 0.00016  47  GLU A OE1 
267  O OE2 . GLU A 40  ? 0.45666 0.40966 0.41471 -0.05279 -0.05601 -0.01115 47  GLU A OE2 
268  N N   . LEU A 41  ? 0.20846 0.23337 0.23742 -0.01194 0.00515  -0.02144 48  LEU A N   
269  C CA  . LEU A 41  ? 0.22418 0.25471 0.26034 -0.00731 0.01024  -0.02347 48  LEU A CA  
270  C C   . LEU A 41  ? 0.24583 0.26630 0.27834 -0.00532 0.01016  -0.02856 48  LEU A C   
271  O O   . LEU A 41  ? 0.25430 0.27617 0.28858 -0.00486 0.00954  -0.02868 48  LEU A O   
272  C CB  . LEU A 41  ? 0.23398 0.26759 0.27451 -0.00177 0.01518  -0.02490 48  LEU A CB  
273  C CG  . LEU A 41  ? 0.21651 0.26064 0.26020 0.00128  0.01650  -0.01928 48  LEU A CG  
274  C CD1 . LEU A 41  ? 0.22495 0.26167 0.26720 0.00754  0.01935  -0.02153 48  LEU A CD1 
275  C CD2 . LEU A 41  ? 0.23233 0.29068 0.27924 0.00417  0.01796  -0.01371 48  LEU A CD2 
276  N N   . ILE A 42  ? 0.23316 0.24553 0.25967 -0.00196 0.01148  -0.03153 49  ILE A N   
277  C CA  . ILE A 42  ? 0.22332 0.23041 0.24749 0.00366  0.01253  -0.03410 49  ILE A CA  
278  C C   . ILE A 42  ? 0.23939 0.23113 0.25164 0.00192  0.00573  -0.03454 49  ILE A C   
279  O O   . ILE A 42  ? 0.24529 0.23558 0.25923 0.00462  0.00476  -0.03470 49  ILE A O   
280  C CB  . ILE A 42  ? 0.24220 0.24823 0.26086 0.01194  0.01821  -0.03472 49  ILE A CB  
281  C CG1 . ILE A 42  ? 0.23082 0.25439 0.26606 0.01114  0.02387  -0.03052 49  ILE A CG1 
282  C CG2 . ILE A 42  ? 0.28634 0.28602 0.29788 0.02256  0.01983  -0.03617 49  ILE A CG2 
283  C CD1 . ILE A 42  ? 0.28058 0.31024 0.31252 0.01870  0.03154  -0.02685 49  ILE A CD1 
284  N N   . SER A 43  ? 0.25358 0.23203 0.25307 -0.00419 -0.00133 -0.03333 50  SER A N   
285  C CA  . SER A 43  ? 0.32573 0.28518 0.31309 -0.01017 -0.01147 -0.03125 50  SER A CA  
286  C C   . SER A 43  ? 0.28469 0.26004 0.28645 -0.01719 -0.01206 -0.02416 50  SER A C   
287  O O   . SER A 43  ? 0.27892 0.24375 0.27559 -0.01793 -0.01626 -0.02237 50  SER A O   
288  C CB  . SER A 43  ? 0.34337 0.28558 0.31541 -0.02003 -0.02310 -0.02890 50  SER A CB  
289  O OG  . SER A 43  ? 0.45002 0.37557 0.41432 -0.03169 -0.03612 -0.02285 50  SER A OG  
290  N N   . ASN A 44  ? 0.21632 0.21596 0.23312 -0.01999 -0.00731 -0.01943 51  ASN A N   
291  C CA  . ASN A 44  ? 0.23777 0.25432 0.26371 -0.02131 -0.00465 -0.01286 51  ASN A CA  
292  C C   . ASN A 44  ? 0.26746 0.28162 0.29255 -0.01326 -0.00096 -0.01867 51  ASN A C   
293  O O   . ASN A 44  ? 0.24960 0.26428 0.27258 -0.01437 -0.00276 -0.01443 51  ASN A O   
294  C CB  . ASN A 44  ? 0.22592 0.26596 0.26259 -0.01880 0.00186  -0.00840 51  ASN A CB  
295  C CG  . ASN A 44  ? 0.29825 0.35274 0.34227 -0.02838 -0.00287 0.00420  51  ASN A CG  
296  O OD1 . ASN A 44  ? 0.26476 0.30726 0.30412 -0.04037 -0.01386 0.00909  51  ASN A OD1 
297  N ND2 . ASN A 44  ? 0.28367 0.36278 0.33813 -0.02287 0.00386  0.01059  51  ASN A ND2 
298  N N   . SER A 45  ? 0.23069 0.24406 0.25836 -0.00648 0.00296  -0.02616 52  SER A N   
299  C CA  . SER A 45  ? 0.22608 0.23995 0.25600 -0.00144 0.00323  -0.02945 52  SER A CA  
300  C C   . SER A 45  ? 0.25640 0.25871 0.28070 0.00106  -0.00083 -0.02903 52  SER A C   
301  O O   . SER A 45  ? 0.25243 0.25535 0.27597 0.00241  -0.00350 -0.02741 52  SER A O   
302  C CB  . SER A 45  ? 0.21677 0.23533 0.25471 0.00160  0.00605  -0.03312 52  SER A CB  
303  O OG  . SER A 45  ? 0.25163 0.27401 0.29083 0.00060  0.00775  -0.03392 52  SER A OG  
304  N N   . SER A 46  ? 0.23220 0.22045 0.24827 0.00366  -0.00194 -0.03069 53  SER A N   
305  C CA  . SER A 46  ? 0.25927 0.22934 0.26390 0.01002  -0.00611 -0.03096 53  SER A CA  
306  C C   . SER A 46  ? 0.31033 0.26887 0.30718 0.00187  -0.01388 -0.02509 53  SER A C   
307  O O   . SER A 46  ? 0.32448 0.27546 0.31733 0.00632  -0.01712 -0.02319 53  SER A O   
308  C CB  . SER A 46  ? 0.30121 0.25019 0.28859 0.01695  -0.00658 -0.03519 53  SER A CB  
309  O OG  . SER A 46  ? 0.35417 0.27804 0.32391 0.02672  -0.01117 -0.03635 53  SER A OG  
310  N N   . ASP A 47  ? 0.29436 0.25462 0.29090 -0.01043 -0.01720 -0.01951 54  ASP A N   
311  C CA  . ASP A 47  ? 0.27572 0.23198 0.26911 -0.02083 -0.02416 -0.00901 54  ASP A CA  
312  C C   . ASP A 47  ? 0.24581 0.22136 0.24681 -0.01790 -0.01925 -0.00520 54  ASP A C   
313  O O   . ASP A 47  ? 0.26536 0.23239 0.26001 -0.01953 -0.02407 0.00101  54  ASP A O   
314  C CB  . ASP A 47  ? 0.27806 0.24457 0.27698 -0.03508 -0.02773 0.00058  54  ASP A CB  
315  C CG  . ASP A 47  ? 0.40176 0.34039 0.38605 -0.04225 -0.03911 -0.00093 54  ASP A CG  
316  O OD1 . ASP A 47  ? 0.44200 0.34545 0.40536 -0.03683 -0.04606 -0.00733 54  ASP A OD1 
317  O OD2 . ASP A 47  ? 0.37745 0.32751 0.36840 -0.05205 -0.04210 0.00459  54  ASP A OD2 
318  N N   . ALA A 48  ? 0.24518 0.24217 0.25536 -0.01309 -0.01109 -0.00890 55  ALA A N   
319  C CA  . ALA A 48  ? 0.21829 0.22707 0.22740 -0.00861 -0.00823 -0.00737 55  ALA A CA  
320  C C   . ALA A 48  ? 0.24292 0.24248 0.24914 -0.00202 -0.01235 -0.01199 55  ALA A C   
321  O O   . ALA A 48  ? 0.26264 0.26358 0.26255 -0.00042 -0.01468 -0.00804 55  ALA A O   
322  C CB  . ALA A 48  ? 0.18544 0.20829 0.19739 -0.00345 -0.00147 -0.01233 55  ALA A CB  
323  N N   . LEU A 49  ? 0.22866 0.22229 0.23987 0.00305  -0.01285 -0.01849 56  LEU A N   
324  C CA  . LEU A 49  ? 0.25306 0.24482 0.26638 0.01087  -0.01645 -0.01944 56  LEU A CA  
325  C C   . LEU A 49  ? 0.30287 0.27520 0.30473 0.01317  -0.02204 -0.01441 56  LEU A C   
326  O O   . LEU A 49  ? 0.26927 0.24151 0.26948 0.01773  -0.02642 -0.01104 56  LEU A O   
327  C CB  . LEU A 49  ? 0.26779 0.26597 0.29216 0.01768  -0.01299 -0.02375 56  LEU A CB  
328  C CG  . LEU A 49  ? 0.18311 0.19817 0.21983 0.01403  -0.01090 -0.02642 56  LEU A CG  
329  C CD1 . LEU A 49  ? 0.25853 0.28103 0.30552 0.01779  -0.00524 -0.02732 56  LEU A CD1 
330  C CD2 . LEU A 49  ? 0.21490 0.23984 0.25789 0.01371  -0.01799 -0.02455 56  LEU A CD2 
331  N N   . ASP A 50  ? 0.26285 0.21483 0.25423 0.00952  -0.02426 -0.01340 57  ASP A N   
332  C CA  . ASP A 50  ? 0.29834 0.22272 0.27368 0.00894  -0.03285 -0.00771 57  ASP A CA  
333  C C   . ASP A 50  ? 0.28897 0.22004 0.26319 0.00027  -0.03607 0.00297  57  ASP A C   
334  O O   . ASP A 50  ? 0.29826 0.21521 0.26362 0.00390  -0.04215 0.00820  57  ASP A O   
335  C CB  . ASP A 50  ? 0.30567 0.20278 0.26648 0.00107  -0.03904 -0.00741 57  ASP A CB  
336  C CG  . ASP A 50  ? 0.41498 0.29567 0.36577 0.01408  -0.03686 -0.01786 57  ASP A CG  
337  O OD1 . ASP A 50  ? 0.35405 0.24614 0.31132 0.03053  -0.02981 -0.02249 57  ASP A OD1 
338  O OD2 . ASP A 50  ? 0.41233 0.27005 0.34802 0.00790  -0.04276 -0.01982 57  ASP A OD2 
339  N N   . LYS A 51  ? 0.29401 0.24751 0.27556 -0.00883 -0.03110 0.00746  58  LYS A N   
340  C CA  . LYS A 51  ? 0.31456 0.27787 0.29259 -0.01542 -0.03165 0.02033  58  LYS A CA  
341  C C   . LYS A 51  ? 0.31043 0.28114 0.28442 -0.00595 -0.03133 0.01884  58  LYS A C   
342  O O   . LYS A 51  ? 0.29417 0.25819 0.25890 -0.00723 -0.03608 0.02870  58  LYS A O   
343  C CB  . LYS A 51  ? 0.32799 0.31791 0.31388 -0.02193 -0.02369 0.02646  58  LYS A CB  
344  C CG  . LYS A 51  ? 0.38356 0.37088 0.37483 -0.03614 -0.02775 0.03545  58  LYS A CG  
345  C CD  . LYS A 51  ? 0.42179 0.44401 0.42500 -0.03921 -0.01836 0.04447  58  LYS A CD  
346  C CE  . LYS A 51  ? 0.43236 0.45636 0.44545 -0.05318 -0.02396 0.05177  58  LYS A CE  
347  N NZ  . LYS A 51  ? 0.44162 0.50188 0.46886 -0.04995 -0.01301 0.05663  58  LYS A NZ  
348  N N   . ILE A 52  ? 0.27944 0.26237 0.25910 0.00192  -0.02791 0.00802  59  ILE A N   
349  C CA  . ILE A 52  ? 0.29900 0.28676 0.27309 0.00852  -0.03181 0.00694  59  ILE A CA  
350  C C   . ILE A 52  ? 0.30220 0.27804 0.27813 0.01507  -0.03959 0.00797  59  ILE A C   
351  O O   . ILE A 52  ? 0.28910 0.26417 0.25742 0.01848  -0.04565 0.01312  59  ILE A O   
352  C CB  . ILE A 52  ? 0.30884 0.30811 0.28656 0.01172  -0.03043 -0.00338 59  ILE A CB  
353  C CG1 . ILE A 52  ? 0.34967 0.35007 0.31493 0.01567  -0.03806 -0.00356 59  ILE A CG1 
354  C CG2 . ILE A 52  ? 0.27781 0.27882 0.27303 0.01359  -0.03103 -0.01042 59  ILE A CG2 
355  C CD1 . ILE A 52  ? 0.35719 0.35792 0.30093 0.01680  -0.03542 0.00440  59  ILE A CD1 
356  N N   . ARG A 53  ? 0.30544 0.27178 0.28889 0.01947  -0.03917 0.00383  60  ARG A N   
357  C CA  . ARG A 53  ? 0.31301 0.26773 0.29582 0.03106  -0.04456 0.00586  60  ARG A CA  
358  C C   . ARG A 53  ? 0.34181 0.27144 0.30711 0.02924  -0.05127 0.01548  60  ARG A C   
359  O O   . ARG A 53  ? 0.36138 0.28716 0.32255 0.03696  -0.05750 0.02100  60  ARG A O   
360  C CB  . ARG A 53  ? 0.31963 0.26689 0.30716 0.04032  -0.04036 -0.00035 60  ARG A CB  
361  C CG  . ARG A 53  ? 0.32690 0.26208 0.31075 0.05853  -0.04347 0.00215  60  ARG A CG  
362  C CD  . ARG A 53  ? 0.46371 0.38271 0.44045 0.07093  -0.03805 -0.00395 60  ARG A CD  
363  N NE  . ARG A 53  ? 0.90363 0.78957 0.85939 0.06047  -0.04088 -0.00709 60  ARG A NE  
364  C CZ  . ARG A 53  ? 0.84033 0.71124 0.78582 0.06487  -0.03732 -0.01430 60  ARG A CZ  
365  N NH1 . ARG A 53  ? 0.76847 0.65623 0.72243 0.08127  -0.02780 -0.01859 60  ARG A NH1 
366  N NH2 . ARG A 53  ? 0.50723 0.34669 0.43310 0.05204  -0.04435 -0.01534 60  ARG A NH2 
367  N N   . TYR A 54  ? 0.31495 0.22777 0.27071 0.01755  -0.05178 0.01969  61  TYR A N   
368  C CA  . TYR A 54  ? 0.34637 0.23306 0.28589 0.01123  -0.06049 0.03204  61  TYR A CA  
369  C C   . TYR A 54  ? 0.36215 0.26562 0.29893 0.00694  -0.06094 0.04306  61  TYR A C   
370  O O   . TYR A 54  ? 0.39455 0.28179 0.31999 0.00988  -0.06862 0.05215  61  TYR A O   
371  C CB  . TYR A 54  ? 0.39871 0.26900 0.33259 -0.00531 -0.06359 0.03743  61  TYR A CB  
372  C CG  . TYR A 54  ? 0.42352 0.26939 0.34333 -0.01826 -0.07463 0.05460  61  TYR A CG  
373  C CD1 . TYR A 54  ? 0.52988 0.32797 0.42889 -0.01379 -0.08749 0.05589  61  TYR A CD1 
374  C CD2 . TYR A 54  ? 0.56228 0.43210 0.48796 -0.03392 -0.07215 0.07119  61  TYR A CD2 
375  C CE1 . TYR A 54  ? 0.47550 0.24637 0.36044 -0.02821 -0.10021 0.07340  61  TYR A CE1 
376  C CE2 . TYR A 54  ? 0.62308 0.47429 0.53878 -0.04840 -0.08261 0.09103  61  TYR A CE2 
377  C CZ  . TYR A 54  ? 0.59784 0.39755 0.49345 -0.04739 -0.09795 0.09215  61  TYR A CZ  
378  O OH  . TYR A 54  ? 0.69725 0.47344 0.58165 -0.06432 -0.11097 0.11359  61  TYR A OH  
379  N N   . GLU A 55  ? 0.34856 0.28180 0.29152 0.00225  -0.05276 0.04246  62  GLU A N   
380  C CA  . GLU A 55  ? 0.32003 0.26786 0.25336 0.00181  -0.05188 0.05187  62  GLU A CA  
381  C C   . GLU A 55  ? 0.34999 0.29772 0.27921 0.01386  -0.05855 0.04798  62  GLU A C   
382  O O   . GLU A 55  ? 0.37237 0.31781 0.28809 0.01492  -0.06320 0.05847  62  GLU A O   
383  C CB  . GLU A 55  ? 0.36681 0.34181 0.30121 0.00034  -0.04109 0.04931  62  GLU A CB  
384  C CG  . GLU A 55  ? 0.43229 0.41814 0.37177 -0.01146 -0.03424 0.06098  62  GLU A CG  
385  C CD  . GLU A 55  ? 0.64095 0.65585 0.57579 -0.00694 -0.02189 0.06326  62  GLU A CD  
386  O OE1 . GLU A 55  ? 0.58296 0.60119 0.50488 0.00488  -0.02042 0.05301  62  GLU A OE1 
387  O OE2 . GLU A 55  ? 0.62258 0.65617 0.56496 -0.01440 -0.01463 0.07630  62  GLU A OE2 
388  N N   . SER A 56  ? 0.32760 0.28048 0.26971 0.02225  -0.05987 0.03554  63  SER A N   
389  C CA  . SER A 56  ? 0.35386 0.31341 0.29801 0.03185  -0.06826 0.03463  63  SER A CA  
390  C C   . SER A 56  ? 0.37351 0.31437 0.31370 0.04052  -0.07608 0.04319  63  SER A C   
391  O O   . SER A 56  ? 0.40850 0.35603 0.34821 0.04807  -0.08447 0.04729  63  SER A O   
392  C CB  . SER A 56  ? 0.32286 0.29894 0.28742 0.03622  -0.06790 0.02381  63  SER A CB  
393  O OG  . SER A 56  ? 0.40886 0.37760 0.38545 0.04338  -0.06453 0.02152  63  SER A OG  
394  N N   . LEU A 57  ? 0.39267 0.30696 0.32735 0.04003  -0.07551 0.04623  64  LEU A N   
395  C CA  . LEU A 57  ? 0.42843 0.31582 0.35314 0.05107  -0.08397 0.05360  64  LEU A CA  
396  C C   . LEU A 57  ? 0.52162 0.40104 0.42972 0.04629  -0.09125 0.06836  64  LEU A C   
397  O O   . LEU A 57  ? 0.57791 0.44476 0.47970 0.05822  -0.09971 0.07507  64  LEU A O   
398  C CB  . LEU A 57  ? 0.47347 0.32326 0.38726 0.05088  -0.08482 0.05204  64  LEU A CB  
399  C CG  . LEU A 57  ? 0.51070 0.36220 0.43410 0.05843  -0.07759 0.03830  64  LEU A CG  
400  C CD1 . LEU A 57  ? 0.58880 0.39466 0.49133 0.05564  -0.08201 0.03682  64  LEU A CD1 
401  C CD2 . LEU A 57  ? 0.61183 0.47851 0.54792 0.08170  -0.07574 0.03439  64  LEU A CD2 
402  N N   . THR A 58  ? 0.46089 0.34951 0.36144 0.03093  -0.08723 0.07535  65  THR A N   
403  C CA  . THR A 58  ? 0.53365 0.42024 0.41720 0.02646  -0.09174 0.09160  65  THR A CA  
404  C C   . THR A 58  ? 0.57932 0.49570 0.45747 0.02857  -0.08915 0.08983  65  THR A C   
405  O O   . THR A 58  ? 0.61941 0.53603 0.47987 0.02856  -0.09300 0.10255  65  THR A O   
406  C CB  . THR A 58  ? 0.52283 0.39943 0.39864 0.00848  -0.08919 0.10670  65  THR A CB  
407  O OG1 . THR A 58  ? 0.54006 0.44206 0.42628 -0.00010 -0.07739 0.10139  65  THR A OG1 
408  C CG2 . THR A 58  ? 0.70781 0.54214 0.57945 0.00448  -0.09818 0.10988  65  THR A CG2 
409  N N   . ASP A 59  ? 0.47939 0.41633 0.36807 0.03058  -0.08413 0.07469  66  ASP A N   
410  C CA  . ASP A 59  ? 0.48998 0.44516 0.36638 0.03326  -0.08512 0.07006  66  ASP A CA  
411  C C   . ASP A 59  ? 0.51905 0.48561 0.41285 0.03717  -0.08898 0.05420  66  ASP A C   
412  O O   . ASP A 59  ? 0.48322 0.45760 0.38366 0.03344  -0.08160 0.04362  66  ASP A O   
413  C CB  . ASP A 59  ? 0.49162 0.45799 0.35344 0.02767  -0.07264 0.07266  66  ASP A CB  
414  C CG  . ASP A 59  ? 0.55490 0.52979 0.39067 0.03442  -0.07442 0.06790  66  ASP A CG  
415  O OD1 . ASP A 59  ? 0.65302 0.62554 0.48595 0.03915  -0.08766 0.05981  66  ASP A OD1 
416  O OD2 . ASP A 59  ? 0.66894 0.65282 0.48520 0.03571  -0.06323 0.07334  66  ASP A OD2 
417  N N   . PRO A 60  ? 0.49430 0.46428 0.39799 0.04436  -0.10118 0.05472  67  PRO A N   
418  C CA  . PRO A 60  ? 0.55494 0.54173 0.48078 0.04544  -0.10626 0.04468  67  PRO A CA  
419  C C   . PRO A 60  ? 0.56115 0.55398 0.47463 0.03879  -0.10952 0.03475  67  PRO A C   
420  O O   . PRO A 60  ? 0.48772 0.49048 0.41897 0.03498  -0.11108 0.02628  67  PRO A O   
421  C CB  . PRO A 60  ? 0.57576 0.57065 0.51143 0.05419  -0.12064 0.05327  67  PRO A CB  
422  C CG  . PRO A 60  ? 0.64116 0.61619 0.56844 0.06145  -0.11803 0.06406  67  PRO A CG  
423  C CD  . PRO A 60  ? 0.63885 0.59932 0.53908 0.05219  -0.11056 0.06715  67  PRO A CD  
424  N N   . SER A 61  ? 0.44489 0.42927 0.32485 0.03849  -0.11091 0.03618  68  SER A N   
425  C CA  . SER A 61  ? 0.47583 0.45610 0.33307 0.03621  -0.11538 0.02511  68  SER A CA  
426  C C   . SER A 61  ? 0.48894 0.46826 0.34864 0.03384  -0.10050 0.01544  68  SER A C   
427  O O   . SER A 61  ? 0.47231 0.44383 0.31637 0.03297  -0.10489 0.00420  68  SER A O   
428  C CB  . SER A 61  ? 0.54785 0.51735 0.36146 0.04165  -0.11787 0.02942  68  SER A CB  
429  O OG  . SER A 61  ? 0.64400 0.61376 0.44364 0.04463  -0.09845 0.03486  68  SER A OG  
430  N N   . LYS A 62  ? 0.39818 0.38188 0.27466 0.03264  -0.08516 0.01989  69  LYS A N   
431  C CA  . LYS A 62  ? 0.43771 0.42378 0.32031 0.03033  -0.07219 0.01234  69  LYS A CA  
432  C C   . LYS A 62  ? 0.37086 0.35986 0.27515 0.02621  -0.07754 0.00138  69  LYS A C   
433  O O   . LYS A 62  ? 0.40253 0.39029 0.30679 0.02492  -0.07015 -0.00654 69  LYS A O   
434  C CB  . LYS A 62  ? 0.44949 0.43889 0.34749 0.02693  -0.05949 0.02091  69  LYS A CB  
435  C CG  . LYS A 62  ? 0.55618 0.54501 0.43800 0.02685  -0.05498 0.03655  69  LYS A CG  
436  C CD  . LYS A 62  ? 0.49628 0.49416 0.38301 0.02160  -0.04072 0.04396  69  LYS A CD  
437  C CE  . LYS A 62  ? 0.52497 0.53281 0.39112 0.02293  -0.03348 0.06085  69  LYS A CE  
438  N NZ  . LYS A 62  ? 0.58137 0.60894 0.45438 0.01961  -0.01868 0.06959  69  LYS A NZ  
439  N N   . LEU A 63  ? 0.37791 0.37374 0.30224 0.02462  -0.08984 0.00324  70  LEU A N   
440  C CA  . LEU A 63  ? 0.40987 0.41513 0.35876 0.01925  -0.09566 -0.00210 70  LEU A CA  
441  C C   . LEU A 63  ? 0.41134 0.41173 0.34812 0.01323  -0.11521 -0.00617 70  LEU A C   
442  O O   . LEU A 63  ? 0.39065 0.40198 0.35095 0.00537  -0.12471 -0.00603 70  LEU A O   
443  C CB  . LEU A 63  ? 0.31001 0.33229 0.29228 0.02275  -0.09561 0.00587  70  LEU A CB  
444  C CG  . LEU A 63  ? 0.36823 0.38697 0.35964 0.02769  -0.07952 0.00675  70  LEU A CG  
445  C CD1 . LEU A 63  ? 0.45669 0.48805 0.47363 0.03668  -0.07910 0.01293  70  LEU A CD1 
446  C CD2 . LEU A 63  ? 0.33303 0.34916 0.32584 0.02238  -0.06868 -0.00182 70  LEU A CD2 
447  N N   . ASP A 64  ? 0.42794 0.41121 0.32659 0.01617  -0.12265 -0.00844 71  ASP A N   
448  C CA  . ASP A 64  ? 0.46479 0.43262 0.34117 0.00999  -0.14459 -0.01461 71  ASP A CA  
449  C C   . ASP A 64  ? 0.42411 0.37591 0.29343 0.00447  -0.14529 -0.02640 71  ASP A C   
450  O O   . ASP A 64  ? 0.45517 0.39469 0.31927 -0.00631 -0.16690 -0.03004 71  ASP A O   
451  C CB  . ASP A 64  ? 0.51094 0.45778 0.33749 0.01828  -0.14976 -0.01649 71  ASP A CB  
452  C CG  . ASP A 64  ? 0.68745 0.64640 0.51791 0.02149  -0.15590 -0.00363 71  ASP A CG  
453  O OD1 . ASP A 64  ? 0.59514 0.57707 0.46621 0.01858  -0.15806 0.00591  71  ASP A OD1 
454  O OD2 . ASP A 64  ? 0.66372 0.60895 0.45449 0.02917  -0.15774 -0.00229 71  ASP A OD2 
455  N N   . SER A 65  ? 0.39577 0.34623 0.26477 0.01057  -0.12401 -0.03098 72  SER A N   
456  C CA  . SER A 65  ? 0.47826 0.41376 0.34219 0.00771  -0.12226 -0.04099 72  SER A CA  
457  C C   . SER A 65  ? 0.52896 0.48424 0.43876 -0.00367 -0.12205 -0.03696 72  SER A C   
458  O O   . SER A 65  ? 0.47915 0.42417 0.38931 -0.00684 -0.11923 -0.04318 72  SER A O   
459  C CB  . SER A 65  ? 0.46914 0.40034 0.31520 0.02070  -0.09931 -0.04487 72  SER A CB  
460  O OG  . SER A 65  ? 0.45224 0.40791 0.32203 0.02329  -0.08245 -0.03477 72  SER A OG  
461  N N   . GLY A 66  ? 0.42020 0.40368 0.36651 -0.00752 -0.12409 -0.02572 73  GLY A N   
462  C CA  . GLY A 66  ? 0.40032 0.40773 0.38887 -0.01443 -0.12099 -0.01944 73  GLY A CA  
463  C C   . GLY A 66  ? 0.34292 0.37655 0.36015 -0.00597 -0.10772 -0.01001 73  GLY A C   
464  O O   . GLY A 66  ? 0.35077 0.37922 0.36046 0.00284  -0.09130 -0.01225 73  GLY A O   
465  N N   . LYS A 67  ? 0.30938 0.37049 0.35854 -0.00803 -0.11577 0.00179  74  LYS A N   
466  C CA  . LYS A 67  ? 0.33793 0.41943 0.40880 0.00502  -0.10384 0.01036  74  LYS A CA  
467  C C   . LYS A 67  ? 0.32068 0.41459 0.41269 0.00911  -0.08724 0.01083  74  LYS A C   
468  O O   . LYS A 67  ? 0.34874 0.44171 0.44157 0.02249  -0.07372 0.01152  74  LYS A O   
469  C CB  . LYS A 67  ? 0.35313 0.46352 0.44907 0.00634  -0.11764 0.02498  74  LYS A CB  
470  C CG  . LYS A 67  ? 0.54163 0.64372 0.62008 0.01478  -0.12437 0.02817  74  LYS A CG  
471  C CD  . LYS A 67  ? 0.75653 0.88787 0.85825 0.01315  -0.14340 0.04329  74  LYS A CD  
472  C CE  . LYS A 67  ? 0.84407 1.01942 0.99331 0.01193  -0.14313 0.05763  74  LYS A CE  
473  N NZ  . LYS A 67  ? 0.84579 1.03398 1.01135 0.03097  -0.11916 0.06003  74  LYS A NZ  
474  N N   . GLU A 68  ? 0.26133 0.36270 0.36652 -0.00207 -0.08939 0.01074  75  GLU A N   
475  C CA  . GLU A 68  ? 0.23360 0.35044 0.35897 0.00225  -0.07414 0.01352  75  GLU A CA  
476  C C   . GLU A 68  ? 0.27303 0.36413 0.37571 0.00714  -0.05896 0.00116  75  GLU A C   
477  O O   . GLU A 68  ? 0.28834 0.35589 0.36767 0.00096  -0.06087 -0.00844 75  GLU A O   
478  C CB  . GLU A 68  ? 0.28300 0.41532 0.42943 -0.01345 -0.08218 0.01993  75  GLU A CB  
479  C CG  . GLU A 68  ? 0.29856 0.46876 0.47949 -0.02059 -0.09671 0.03858  75  GLU A CG  
480  C CD  . GLU A 68  ? 0.67028 0.83050 0.83879 -0.02883 -0.11930 0.03881  75  GLU A CD  
481  O OE1 . GLU A 68  ? 0.68949 0.81417 0.82728 -0.04032 -0.13194 0.02695  75  GLU A OE1 
482  O OE2 . GLU A 68  ? 0.77023 0.95634 0.95623 -0.02159 -0.12446 0.05073  75  GLU A OE2 
483  N N   . LEU A 69  ? 0.19454 0.29034 0.30259 0.01960  -0.04453 0.00236  76  LEU A N   
484  C CA  . LEU A 69  ? 0.21875 0.29218 0.30783 0.02277  -0.03285 -0.00685 76  LEU A CA  
485  C C   . LEU A 69  ? 0.22148 0.30680 0.32369 0.02457  -0.02266 -0.00543 76  LEU A C   
486  O O   . LEU A 69  ? 0.21137 0.31010 0.32315 0.03790  -0.01479 0.00031  76  LEU A O   
487  C CB  . LEU A 69  ? 0.23992 0.29734 0.31415 0.03506  -0.02882 -0.00734 76  LEU A CB  
488  C CG  . LEU A 69  ? 0.29793 0.34413 0.35834 0.03416  -0.03789 -0.00594 76  LEU A CG  
489  C CD1 . LEU A 69  ? 0.37408 0.39818 0.41806 0.04395  -0.03509 -0.00507 76  LEU A CD1 
490  C CD2 . LEU A 69  ? 0.29836 0.33348 0.34261 0.02243  -0.04142 -0.01147 76  LEU A CD2 
491  N N   . HIS A 70  ? 0.24310 0.28653 0.28467 0.03166  -0.00511 0.00831  77  HIS A N   
492  C CA  . HIS A 70  ? 0.24185 0.28761 0.28604 0.02853  -0.00448 0.00447  77  HIS A CA  
493  C C   . HIS A 70  ? 0.22350 0.25513 0.25875 0.01922  -0.00842 -0.00724 77  HIS A C   
494  O O   . HIS A 70  ? 0.23018 0.25268 0.25873 0.01471  -0.01216 -0.01203 77  HIS A O   
495  C CB  . HIS A 70  ? 0.24305 0.31536 0.29905 0.02518  -0.01042 0.01331  77  HIS A CB  
496  C CG  . HIS A 70  ? 0.24926 0.32938 0.30392 0.01316  -0.02275 0.01175  77  HIS A CG  
497  N ND1 . HIS A 70  ? 0.32947 0.43166 0.39087 0.01138  -0.03027 0.02001  77  HIS A ND1 
498  C CD2 . HIS A 70  ? 0.30925 0.37743 0.35541 0.00270  -0.02869 0.00247  77  HIS A CD2 
499  C CE1 . HIS A 70  ? 0.28287 0.38398 0.33805 -0.00089 -0.04069 0.01395  77  HIS A CE1 
500  N NE2 . HIS A 70  ? 0.28105 0.36012 0.32701 -0.00558 -0.03897 0.00363  77  HIS A NE2 
501  N N   . ILE A 71  ? 0.20720 0.23879 0.24233 0.01797  -0.00665 -0.01039 78  ILE A N   
502  C CA  . ILE A 71  ? 0.21874 0.24086 0.24661 0.01132  -0.00978 -0.01896 78  ILE A CA  
503  C C   . ILE A 71  ? 0.24208 0.27611 0.27488 0.00687  -0.01260 -0.01467 78  ILE A C   
504  O O   . ILE A 71  ? 0.24152 0.28631 0.28029 0.01160  -0.00766 -0.00872 78  ILE A O   
505  C CB  . ILE A 71  ? 0.23069 0.23932 0.25106 0.01506  -0.00380 -0.02728 78  ILE A CB  
506  C CG1 . ILE A 71  ? 0.23985 0.23463 0.25777 0.01751  0.00003  -0.03117 78  ILE A CG1 
507  C CG2 . ILE A 71  ? 0.27136 0.27607 0.28550 0.00952  -0.00787 -0.03381 78  ILE A CG2 
508  C CD1 . ILE A 71  ? 0.24006 0.22096 0.25137 0.01952  0.00571  -0.04046 78  ILE A CD1 
509  N N   . ASN A 72  ? 0.21469 0.24559 0.24511 -0.00163 -0.01912 -0.01700 79  ASN A N   
510  C CA  . ASN A 72  ? 0.19104 0.22832 0.22606 -0.00730 -0.02091 -0.01291 79  ASN A CA  
511  C C   . ASN A 72  ? 0.20338 0.22826 0.22948 -0.00807 -0.02019 -0.01820 79  ASN A C   
512  O O   . ASN A 72  ? 0.23564 0.24854 0.25396 -0.00887 -0.02240 -0.02487 79  ASN A O   
513  C CB  . ASN A 72  ? 0.18752 0.23007 0.22772 -0.01744 -0.02887 -0.01029 79  ASN A CB  
514  C CG  . ASN A 72  ? 0.25373 0.31592 0.30495 -0.01690 -0.03115 -0.00278 79  ASN A CG  
515  O OD1 . ASN A 72  ? 0.26904 0.34401 0.32842 -0.00904 -0.02512 0.00403  79  ASN A OD1 
516  N ND2 . ASN A 72  ? 0.24207 0.30779 0.29272 -0.02441 -0.03972 -0.00369 79  ASN A ND2 
517  N N   . LEU A 73  ? 0.20475 0.23481 0.23253 -0.00671 -0.01645 -0.01362 80  LEU A N   
518  C CA  . LEU A 73  ? 0.21217 0.23439 0.23212 -0.00602 -0.01554 -0.01539 80  LEU A CA  
519  C C   . LEU A 73  ? 0.24057 0.26274 0.26647 -0.01310 -0.01643 -0.00810 80  LEU A C   
520  O O   . LEU A 73  ? 0.22438 0.25866 0.25976 -0.01441 -0.01325 0.00058  80  LEU A O   
521  C CB  . LEU A 73  ? 0.20284 0.23000 0.21644 0.00252  -0.00965 -0.01573 80  LEU A CB  
522  C CG  . LEU A 73  ? 0.28341 0.30727 0.29089 0.00807  -0.00786 -0.02416 80  LEU A CG  
523  C CD1 . LEU A 73  ? 0.26836 0.29561 0.26619 0.01566  -0.00239 -0.02624 80  LEU A CD1 
524  C CD2 . LEU A 73  ? 0.26839 0.28173 0.27113 0.00539  -0.01250 -0.03266 80  LEU A CD2 
525  N N   . ILE A 74  ? 0.25846 0.26623 0.27947 -0.01754 -0.01964 -0.01111 81  ILE A N   
526  C CA  . ILE A 74  ? 0.28128 0.28241 0.30730 -0.02631 -0.02046 -0.00587 81  ILE A CA  
527  C C   . ILE A 74  ? 0.30993 0.29804 0.32840 -0.02262 -0.01683 -0.00373 81  ILE A C   
528  O O   . ILE A 74  ? 0.27904 0.25305 0.28885 -0.02061 -0.01832 -0.00951 81  ILE A O   
529  C CB  . ILE A 74  ? 0.24728 0.23931 0.27306 -0.03580 -0.02732 -0.01158 81  ILE A CB  
530  C CG1 . ILE A 74  ? 0.29386 0.30122 0.32520 -0.03634 -0.03118 -0.01274 81  ILE A CG1 
531  C CG2 . ILE A 74  ? 0.29036 0.27531 0.32280 -0.04795 -0.02873 -0.00740 81  ILE A CG2 
532  C CD1 . ILE A 74  ? 0.33050 0.33229 0.35830 -0.04436 -0.03886 -0.01859 81  ILE A CD1 
533  N N   . PRO A 75  ? 0.29886 0.29236 0.32036 -0.02018 -0.01111 0.00596  82  PRO A N   
534  C CA  . PRO A 75  ? 0.29317 0.27449 0.30830 -0.01602 -0.00697 0.01108  82  PRO A CA  
535  C C   . PRO A 75  ? 0.36186 0.32519 0.38238 -0.02644 -0.00595 0.01540  82  PRO A C   
536  O O   . PRO A 75  ? 0.34362 0.31023 0.37568 -0.03801 -0.00775 0.01761  82  PRO A O   
537  C CB  . PRO A 75  ? 0.32669 0.32372 0.34137 -0.00802 -0.00057 0.02061  82  PRO A CB  
538  C CG  . PRO A 75  ? 0.30307 0.31617 0.32934 -0.01254 0.00038  0.02375  82  PRO A CG  
539  C CD  . PRO A 75  ? 0.27068 0.28299 0.30154 -0.01945 -0.00685 0.01436  82  PRO A CD  
540  N N   . ASN A 76  ? 0.33478 0.27879 0.34725 -0.02237 -0.00289 0.01670  83  ASN A N   
541  C CA  . ASN A 76  ? 0.31907 0.23861 0.33386 -0.03154 -0.00022 0.01987  83  ASN A CA  
542  C C   . ASN A 76  ? 0.37541 0.28219 0.38334 -0.02059 0.00805  0.02950  83  ASN A C   
543  O O   . ASN A 76  ? 0.39744 0.29468 0.39502 -0.01102 0.00842  0.02559  83  ASN A O   
544  C CB  . ASN A 76  ? 0.40605 0.30644 0.41458 -0.03889 -0.00615 0.00669  83  ASN A CB  
545  C CG  . ASN A 76  ? 0.40619 0.27738 0.41508 -0.05092 -0.00412 0.00664  83  ASN A CG  
546  O OD1 . ASN A 76  ? 0.47804 0.33287 0.48689 -0.04838 0.00409  0.01604  83  ASN A OD1 
547  N ND2 . ASN A 76  ? 0.51440 0.37808 0.52265 -0.06429 -0.01163 -0.00415 83  ASN A ND2 
548  N N   . LYS A 77  ? 0.42228 0.33103 0.43680 -0.02088 0.01544  0.04381  84  LYS A N   
549  C CA  . LYS A 77  ? 0.47796 0.37671 0.48577 -0.00860 0.02422  0.05603  84  LYS A CA  
550  C C   . LYS A 77  ? 0.44851 0.31068 0.45163 -0.01067 0.02835  0.05506  84  LYS A C   
551  O O   . LYS A 77  ? 0.53910 0.39196 0.53338 0.00355  0.03394  0.06121  84  LYS A O   
552  C CB  . LYS A 77  ? 0.52086 0.42888 0.53641 -0.00821 0.03283  0.07351  84  LYS A CB  
553  C CG  . LYS A 77  ? 0.56470 0.50495 0.58582 -0.00777 0.03150  0.07578  84  LYS A CG  
554  C CD  . LYS A 77  ? 0.74523 0.70321 0.75701 0.00873  0.03802  0.08813  84  LYS A CD  
555  C CE  . LYS A 77  ? 0.84771 0.82917 0.86678 0.00789  0.04291  0.09705  84  LYS A CE  
556  N NZ  . LYS A 77  ? 0.78919 0.78826 0.81236 0.00335  0.03583  0.08462  84  LYS A NZ  
557  N N   . GLN A 78  ? 0.53224 0.37347 0.54053 -0.02771 0.02597  0.04769  85  GLN A N   
558  C CA  . GLN A 78  ? 0.59184 0.39277 0.59276 -0.03020 0.03094  0.04486  85  GLN A CA  
559  C C   . GLN A 78  ? 0.67266 0.46542 0.65878 -0.01807 0.02878  0.03415  85  GLN A C   
560  O O   . GLN A 78  ? 0.65390 0.42415 0.63122 -0.00619 0.03699  0.03887  85  GLN A O   
561  C CB  . GLN A 78  ? 0.74357 0.52533 0.75108 -0.05319 0.02660  0.03590  85  GLN A CB  
562  C CG  . GLN A 78  ? 0.90203 0.66793 0.92215 -0.06501 0.03477  0.04891  85  GLN A CG  
563  C CD  . GLN A 78  ? 1.03677 0.75263 1.04857 -0.07033 0.04207  0.04609  85  GLN A CD  
564  O OE1 . GLN A 78  ? 1.13297 0.82564 1.13443 -0.07898 0.03646  0.02891  85  GLN A OE1 
565  N NE2 . GLN A 78  ? 0.98377 0.68109 0.99837 -0.06434 0.05557  0.06326  85  GLN A NE2 
566  N N   . ASP A 79  ? 0.44601 0.25770 0.43024 -0.01977 0.01901  0.02138  86  ASP A N   
567  C CA  . ASP A 79  ? 0.53674 0.34643 0.50958 -0.00867 0.01725  0.01238  86  ASP A CA  
568  C C   . ASP A 79  ? 0.51564 0.35357 0.48844 0.00823  0.01760  0.01893  86  ASP A C   
569  O O   . ASP A 79  ? 0.49609 0.33495 0.46242 0.01888  0.01771  0.01483  86  ASP A O   
570  C CB  . ASP A 79  ? 0.51007 0.32661 0.48097 -0.01861 0.00733  -0.00314 86  ASP A CB  
571  C CG  . ASP A 79  ? 0.73076 0.52123 0.69879 -0.03578 0.00467  -0.01210 86  ASP A CG  
572  O OD1 . ASP A 79  ? 0.79195 0.55233 0.75776 -0.03971 0.01152  -0.00849 86  ASP A OD1 
573  O OD2 . ASP A 79  ? 0.79549 0.59545 0.76323 -0.04564 -0.00439 -0.02257 86  ASP A OD2 
574  N N   . ARG A 80  ? 0.39934 0.26112 0.37889 0.01061  0.01782  0.02881  87  ARG A N   
575  C CA  . ARG A 80  ? 0.38303 0.27454 0.36112 0.02379  0.01575  0.03244  87  ARG A CA  
576  C C   . ARG A 80  ? 0.33653 0.24393 0.31389 0.02283  0.00740  0.01889  87  ARG A C   
577  O O   . ARG A 80  ? 0.36819 0.28599 0.34266 0.03292  0.00618  0.01738  87  ARG A O   
578  C CB  . ARG A 80  ? 0.40543 0.29301 0.37799 0.04051  0.02247  0.04342  87  ARG A CB  
579  C CG  . ARG A 80  ? 0.45971 0.37818 0.43130 0.05181  0.02172  0.05339  87  ARG A CG  
580  C CD  . ARG A 80  ? 0.48651 0.40227 0.45368 0.06875  0.02922  0.06867  87  ARG A CD  
581  N NE  . ARG A 80  ? 0.63992 0.56537 0.60544 0.07995  0.02670  0.06564  87  ARG A NE  
582  C CZ  . ARG A 80  ? 0.69434 0.60800 0.65754 0.09420  0.03436  0.07590  87  ARG A CZ  
583  N NH1 . ARG A 80  ? 0.61484 0.50349 0.57556 0.09937  0.04538  0.08980  87  ARG A NH1 
584  N NH2 . ARG A 80  ? 0.65943 0.58683 0.62396 0.10401  0.03192  0.07333  87  ARG A NH2 
585  N N   . THR A 81  ? 0.31852 0.22930 0.30013 0.01053  0.00198  0.01031  88  THR A N   
586  C CA  . THR A 81  ? 0.27061 0.19404 0.25215 0.00889  -0.00465 -0.00104 88  THR A CA  
587  C C   . THR A 81  ? 0.31337 0.25722 0.30083 0.00371  -0.00847 -0.00251 88  THR A C   
588  O O   . THR A 81  ? 0.31706 0.26139 0.31028 -0.00339 -0.00734 0.00210  88  THR A O   
589  C CB  . THR A 81  ? 0.34992 0.25457 0.32798 0.00120  -0.00692 -0.01088 88  THR A CB  
590  O OG1 . THR A 81  ? 0.38089 0.27634 0.36291 -0.01192 -0.00842 -0.01118 88  THR A OG1 
591  C CG2 . THR A 81  ? 0.42966 0.31135 0.39923 0.00833  -0.00151 -0.01090 88  THR A CG2 
592  N N   . LEU A 82  ? 0.30518 0.26550 0.29201 0.00741  -0.01217 -0.00858 89  LEU A N   
593  C CA  . LEU A 82  ? 0.25936 0.23381 0.25006 0.00345  -0.01499 -0.01262 89  LEU A CA  
594  C C   . LEU A 82  ? 0.29620 0.26807 0.28749 -0.00025 -0.01887 -0.02208 89  LEU A C   
595  O O   . LEU A 82  ? 0.29482 0.26735 0.28361 0.00387  -0.01981 -0.02647 89  LEU A O   
596  C CB  . LEU A 82  ? 0.25882 0.25139 0.24630 0.01050  -0.01496 -0.01227 89  LEU A CB  
597  C CG  . LEU A 82  ? 0.24760 0.25012 0.23694 0.00816  -0.01610 -0.01772 89  LEU A CG  
598  C CD1 . LEU A 82  ? 0.28029 0.28529 0.27533 0.00456  -0.01274 -0.01092 89  LEU A CD1 
599  C CD2 . LEU A 82  ? 0.26588 0.28159 0.24821 0.01420  -0.01689 -0.02168 89  LEU A CD2 
600  N N   . THR A 83  ? 0.27480 0.24598 0.27035 -0.00761 -0.02082 -0.02371 90  THR A N   
601  C CA  . THR A 83  ? 0.22930 0.19798 0.22421 -0.01063 -0.02405 -0.03053 90  THR A CA  
602  C C   . THR A 83  ? 0.30754 0.28959 0.30716 -0.01007 -0.02456 -0.03185 90  THR A C   
603  O O   . THR A 83  ? 0.29915 0.28987 0.30436 -0.01157 -0.02357 -0.02724 90  THR A O   
604  C CB  . THR A 83  ? 0.27901 0.23649 0.27315 -0.01906 -0.02678 -0.03140 90  THR A CB  
605  O OG1 . THR A 83  ? 0.31045 0.24945 0.29786 -0.01884 -0.02475 -0.03159 90  THR A OG1 
606  C CG2 . THR A 83  ? 0.30227 0.25994 0.29334 -0.02068 -0.03017 -0.03725 90  THR A CG2 
607  N N   . ILE A 84  ? 0.27757 0.26060 0.27565 -0.00739 -0.02483 -0.03723 91  ILE A N   
608  C CA  . ILE A 84  ? 0.24931 0.23930 0.25080 -0.00618 -0.02382 -0.03888 91  ILE A CA  
609  C C   . ILE A 84  ? 0.28939 0.27590 0.29099 -0.00851 -0.02558 -0.03990 91  ILE A C   
610  O O   . ILE A 84  ? 0.28669 0.26727 0.28471 -0.00770 -0.02549 -0.04328 91  ILE A O   
611  C CB  . ILE A 84  ? 0.29320 0.28553 0.29322 -0.00257 -0.02218 -0.04407 91  ILE A CB  
612  C CG1 . ILE A 84  ? 0.33211 0.33089 0.32889 0.00053  -0.02145 -0.04330 91  ILE A CG1 
613  C CG2 . ILE A 84  ? 0.30370 0.29638 0.30626 -0.00159 -0.01961 -0.04637 91  ILE A CG2 
614  C CD1 . ILE A 84  ? 0.39137 0.39035 0.38535 0.00238  -0.02301 -0.04185 91  ILE A CD1 
615  N N   . VAL A 85  ? 0.26416 0.25693 0.27007 -0.01067 -0.02695 -0.03583 92  VAL A N   
616  C CA  . VAL A 85  ? 0.25420 0.24753 0.25893 -0.01223 -0.02968 -0.03532 92  VAL A CA  
617  C C   . VAL A 85  ? 0.27390 0.27383 0.28351 -0.00694 -0.02609 -0.03244 92  VAL A C   
618  O O   . VAL A 85  ? 0.27792 0.28531 0.29359 -0.00402 -0.02306 -0.02895 92  VAL A O   
619  C CB  . VAL A 85  ? 0.29079 0.28906 0.29729 -0.01935 -0.03543 -0.03227 92  VAL A CB  
620  C CG1 . VAL A 85  ? 0.32785 0.32672 0.32831 -0.02099 -0.03989 -0.03334 92  VAL A CG1 
621  C CG2 . VAL A 85  ? 0.35812 0.34567 0.36083 -0.02466 -0.03684 -0.03445 92  VAL A CG2 
622  N N   . ASP A 86  ? 0.22235 0.21830 0.22870 -0.00458 -0.02500 -0.03305 93  ASP A N   
623  C CA  . ASP A 86  ? 0.21659 0.21591 0.22707 0.00114  -0.02068 -0.02846 93  ASP A CA  
624  C C   . ASP A 86  ? 0.24242 0.24472 0.24856 0.00195  -0.02331 -0.02455 93  ASP A C   
625  O O   . ASP A 86  ? 0.25670 0.25417 0.25423 -0.00130 -0.02679 -0.02804 93  ASP A O   
626  C CB  . ASP A 86  ? 0.28073 0.26943 0.29185 0.00433  -0.01378 -0.03265 93  ASP A CB  
627  C CG  . ASP A 86  ? 0.34204 0.32245 0.34952 0.00294  -0.01264 -0.03572 93  ASP A CG  
628  O OD1 . ASP A 86  ? 0.29427 0.27079 0.30149 0.00021  -0.01263 -0.04157 93  ASP A OD1 
629  O OD2 . ASP A 86  ? 0.35823 0.33813 0.36370 0.00540  -0.01120 -0.03113 93  ASP A OD2 
630  N N   . THR A 87  ? 0.25339 0.26414 0.26421 0.00772  -0.02107 -0.01665 94  THR A N   
631  C CA  . THR A 87  ? 0.25351 0.27013 0.25938 0.01075  -0.02307 -0.01074 94  THR A CA  
632  C C   . THR A 87  ? 0.24716 0.25339 0.25270 0.01812  -0.01383 -0.00717 94  THR A C   
633  O O   . THR A 87  ? 0.26165 0.27430 0.26808 0.02542  -0.01122 0.00250  94  THR A O   
634  C CB  . THR A 87  ? 0.29783 0.33580 0.31029 0.01264  -0.02793 -0.00160 94  THR A CB  
635  O OG1 . THR A 87  ? 0.27040 0.31223 0.29434 0.01938  -0.02096 0.00386  94  THR A OG1 
636  C CG2 . THR A 87  ? 0.27940 0.32726 0.29201 0.00208  -0.03828 -0.00521 94  THR A CG2 
637  N N   . GLY A 88  ? 0.25664 0.24764 0.26208 0.01612  -0.00857 -0.01393 95  GLY A N   
638  C CA  . GLY A 88  ? 0.23070 0.20977 0.23813 0.02016  0.00067  -0.01133 95  GLY A CA  
639  C C   . GLY A 88  ? 0.28470 0.26318 0.28442 0.02154  0.00150  -0.00754 95  GLY A C   
640  O O   . GLY A 88  ? 0.28017 0.26828 0.27046 0.02154  -0.00519 -0.00588 95  GLY A O   
641  N N   . ILE A 89  ? 0.26016 0.22679 0.26344 0.02210  0.01019  -0.00661 96  ILE A N   
642  C CA  . ILE A 89  ? 0.26566 0.23170 0.26267 0.02548  0.01432  -0.00010 96  ILE A CA  
643  C C   . ILE A 89  ? 0.33246 0.30145 0.32028 0.02171  0.00965  -0.00632 96  ILE A C   
644  O O   . ILE A 89  ? 0.30724 0.27868 0.28442 0.02580  0.01132  -0.00159 96  ILE A O   
645  C CB  . ILE A 89  ? 0.29236 0.24453 0.29911 0.02576  0.02630  0.00370  96  ILE A CB  
646  C CG1 . ILE A 89  ? 0.36273 0.31545 0.36369 0.03231  0.03321  0.01549  96  ILE A CG1 
647  C CG2 . ILE A 89  ? 0.25830 0.20496 0.27311 0.01654  0.02686  -0.00650 96  ILE A CG2 
648  C CD1 . ILE A 89  ? 0.40756 0.34537 0.41937 0.03403  0.04659  0.02352  96  ILE A CD1 
649  N N   . GLY A 90  ? 0.27042 0.23872 0.26050 0.01550  0.00475  -0.01615 97  GLY A N   
650  C CA  . GLY A 90  ? 0.29423 0.26273 0.27567 0.01384  0.00201  -0.02140 97  GLY A CA  
651  C C   . GLY A 90  ? 0.33725 0.30258 0.32415 0.01417  0.01020  -0.02025 97  GLY A C   
652  O O   . GLY A 90  ? 0.29082 0.25302 0.28987 0.01305  0.01720  -0.01658 97  GLY A O   
653  N N   . MET A 91  ? 0.27793 0.24364 0.25613 0.01566  0.00999  -0.02316 98  MET A N   
654  C CA  . MET A 91  ? 0.30025 0.26746 0.28606 0.01629  0.01744  -0.02184 98  MET A CA  
655  C C   . MET A 91  ? 0.29389 0.26051 0.26349 0.02363  0.02189  -0.01881 98  MET A C   
656  O O   . MET A 91  ? 0.29980 0.26233 0.25166 0.02592  0.01669  -0.02399 98  MET A O   
657  C CB  . MET A 91  ? 0.29513 0.26524 0.28912 0.01246  0.01386  -0.02887 98  MET A CB  
658  C CG  . MET A 91  ? 0.32076 0.29362 0.33203 0.00545  0.01245  -0.03152 98  MET A CG  
659  S SD  . MET A 91  ? 0.31845 0.29964 0.33744 0.00261  0.00753  -0.03791 98  MET A SD  
660  C CE  . MET A 91  ? 0.34297 0.31767 0.34652 0.00455  -0.00033 -0.04206 98  MET A CE  
661  N N   . THR A 92  ? 0.28640 0.25592 0.26133 0.02700  0.03215  -0.01062 99  THR A N   
662  C CA  . THR A 92  ? 0.30865 0.27843 0.26741 0.03562  0.03865  -0.00705 99  THR A CA  
663  C C   . THR A 92  ? 0.26714 0.23900 0.22819 0.03777  0.04125  -0.01139 99  THR A C   
664  O O   . THR A 92  ? 0.31191 0.28824 0.28993 0.03235  0.03837  -0.01507 99  THR A O   
665  C CB  . THR A 92  ? 0.35373 0.32726 0.31870 0.03942  0.05067  0.00567  99  THR A CB  
666  O OG1 . THR A 92  ? 0.35507 0.33444 0.34683 0.03329  0.05692  0.00861  99  THR A OG1 
667  C CG2 . THR A 92  ? 0.35569 0.32640 0.31924 0.03946  0.04955  0.01214  99  THR A CG2 
668  N N   . LYS A 93  ? 0.31898 0.28800 0.26118 0.04714  0.04717  -0.01056 100 LYS A N   
669  C CA  . LYS A 93  ? 0.32316 0.29453 0.26806 0.05246  0.05283  -0.01209 100 LYS A CA  
670  C C   . LYS A 93  ? 0.30263 0.29046 0.27683 0.05033  0.06132  -0.00324 100 LYS A C   
671  O O   . LYS A 93  ? 0.35458 0.35122 0.34401 0.04965  0.06128  -0.00447 100 LYS A O   
672  C CB  . LYS A 93  ? 0.39022 0.35348 0.30710 0.06459  0.05998  -0.01264 100 LYS A CB  
673  C CG  . LYS A 93  ? 0.37085 0.33371 0.28796 0.07285  0.06704  -0.01419 100 LYS A CG  
674  C CD  . LYS A 93  ? 0.46264 0.41669 0.35153 0.08681  0.07756  -0.01400 100 LYS A CD  
675  C CE  . LYS A 93  ? 0.53598 0.47630 0.41212 0.09483  0.07989  -0.02195 100 LYS A CE  
676  N NZ  . LYS A 93  ? 0.64050 0.57578 0.49591 0.11120  0.09496  -0.01938 100 LYS A NZ  
677  N N   . ALA A 94  ? 0.30667 0.29987 0.29019 0.04877  0.06853  0.00653  101 ALA A N   
678  C CA  . ALA A 94  ? 0.33380 0.34235 0.34802 0.04325  0.07603  0.01471  101 ALA A CA  
679  C C   . ALA A 94  ? 0.31447 0.32685 0.35101 0.02986  0.06654  0.00859  101 ALA A C   
680  O O   . ALA A 94  ? 0.30990 0.33788 0.37062 0.02432  0.06789  0.01025  101 ALA A O   
681  C CB  . ALA A 94  ? 0.33988 0.34912 0.35838 0.04378  0.08681  0.02717  101 ALA A CB  
682  N N   . ASP A 95  ? 0.27363 0.27400 0.30229 0.02482  0.05696  0.00176  102 ASP A N   
683  C CA  . ASP A 95  ? 0.27145 0.27371 0.31526 0.01414  0.04786  -0.00582 102 ASP A CA  
684  C C   . ASP A 95  ? 0.34738 0.35851 0.39340 0.01553  0.04206  -0.01176 102 ASP A C   
685  O O   . ASP A 95  ? 0.30363 0.32841 0.36975 0.00868  0.03937  -0.01324 102 ASP A O   
686  C CB  . ASP A 95  ? 0.32225 0.31082 0.35414 0.01184  0.04002  -0.01114 102 ASP A CB  
687  C CG  . ASP A 95  ? 0.36440 0.34499 0.39885 0.01036  0.04573  -0.00426 102 ASP A CG  
688  O OD1 . ASP A 95  ? 0.36691 0.35005 0.41910 0.00541  0.05376  0.00167  102 ASP A OD1 
689  O OD2 . ASP A 95  ? 0.33826 0.31052 0.35825 0.01400  0.04234  -0.00402 102 ASP A OD2 
690  N N   . LEU A 96  ? 0.24648 0.24973 0.27141 0.02434  0.04006  -0.01505 103 LEU A N   
691  C CA  . LEU A 96  ? 0.27419 0.28123 0.29883 0.02718  0.03532  -0.01970 103 LEU A CA  
692  C C   . LEU A 96  ? 0.27495 0.30054 0.31564 0.03206  0.04245  -0.01333 103 LEU A C   
693  O O   . LEU A 96  ? 0.28631 0.32569 0.34095 0.03024  0.03797  -0.01425 103 LEU A O   
694  C CB  . LEU A 96  ? 0.27021 0.25983 0.26808 0.03474  0.03330  -0.02464 103 LEU A CB  
695  C CG  . LEU A 96  ? 0.27760 0.25344 0.26153 0.02961  0.02455  -0.03066 103 LEU A CG  
696  C CD1 . LEU A 96  ? 0.29817 0.25757 0.25624 0.03527  0.02329  -0.03569 103 LEU A CD1 
697  C CD2 . LEU A 96  ? 0.29895 0.27786 0.29344 0.02216  0.01581  -0.03504 103 LEU A CD2 
698  N N   . ILE A 97  ? 0.25316 0.28196 0.29228 0.03922  0.05385  -0.00567 104 ILE A N   
699  C CA  . ILE A 97  ? 0.26079 0.30923 0.31497 0.04642  0.06247  0.00216  104 ILE A CA  
700  C C   . ILE A 97  ? 0.35303 0.42550 0.44045 0.03565  0.06437  0.00887  104 ILE A C   
701  O O   . ILE A 97  ? 0.32898 0.42530 0.43799 0.03527  0.06404  0.01266  104 ILE A O   
702  C CB  . ILE A 97  ? 0.32652 0.36742 0.36163 0.06084  0.07548  0.00751  104 ILE A CB  
703  C CG1 . ILE A 97  ? 0.32624 0.34194 0.32806 0.06974  0.07268  -0.00152 104 ILE A CG1 
704  C CG2 . ILE A 97  ? 0.33058 0.39451 0.38362 0.07006  0.08684  0.01787  104 ILE A CG2 
705  C CD1 . ILE A 97  ? 0.45912 0.46162 0.43411 0.08173  0.08318  -0.00003 104 ILE A CD1 
706  N N   . ASN A 98  ? 0.26157 0.32857 0.35453 0.02626  0.06612  0.01069  105 ASN A N   
707  C CA  . ASN A 98  ? 0.29837 0.38456 0.42221 0.01587  0.07130  0.01833  105 ASN A CA  
708  C C   . ASN A 98  ? 0.31924 0.39964 0.45601 -0.00147 0.06370  0.01224  105 ASN A C   
709  O O   . ASN A 98  ? 0.27208 0.36967 0.43216 -0.01322 0.05759  0.00931  105 ASN A O   
710  C CB  . ASN A 98  ? 0.41248 0.49806 0.53475 0.02242  0.08684  0.03065  105 ASN A CB  
711  C CG  . ASN A 98  ? 0.61796 0.72742 0.75338 0.03217  0.09789  0.04133  105 ASN A CG  
712  O OD1 . ASN A 98  ? 0.74409 0.84829 0.86054 0.04748  0.10885  0.04708  105 ASN A OD1 
713  N ND2 . ASN A 98  ? 0.66787 0.80537 0.83572 0.02365  0.09521  0.04420  105 ASN A ND2 
714  N N   . ASN A 99  ? 0.35476 0.32178 0.34092 0.02146  0.00866  0.03261  106 ASN A N   
715  C CA  . ASN A 99  ? 0.32064 0.28191 0.32197 0.01426  0.00567  0.04682  106 ASN A CA  
716  C C   . ASN A 99  ? 0.32167 0.27612 0.34601 0.02140  0.00469  0.04297  106 ASN A C   
717  O O   . ASN A 99  ? 0.34961 0.31013 0.38759 0.01691  0.00945  0.04368  106 ASN A O   
718  C CB  . ASN A 99  ? 0.36888 0.31538 0.36436 0.00688  -0.00552 0.06276  106 ASN A CB  
719  C CG  . ASN A 99  ? 0.48754 0.44324 0.45288 -0.00268 -0.00698 0.06789  106 ASN A CG  
720  O OD1 . ASN A 99  ? 0.48164 0.45517 0.43299 -0.00762 0.00408  0.06339  106 ASN A OD1 
721  N ND2 . ASN A 99  ? 0.51862 0.46560 0.47374 -0.00689 -0.02066 0.07787  106 ASN A ND2 
722  N N   . LEU A 100 ? 0.31586 0.25846 0.34321 0.03029  -0.00103 0.03844  107 LEU A N   
723  C CA  . LEU A 100 ? 0.29291 0.23079 0.33738 0.03471  -0.00122 0.03648  107 LEU A CA  
724  C C   . LEU A 100 ? 0.30142 0.25831 0.35111 0.03903  0.00444  0.02891  107 LEU A C   
725  O O   . LEU A 100 ? 0.34697 0.30890 0.40662 0.03563  0.00613  0.02797  107 LEU A O   
726  C CB  . LEU A 100 ? 0.30368 0.22628 0.35030 0.04139  -0.00784 0.03589  107 LEU A CB  
727  C CG  . LEU A 100 ? 0.32085 0.22925 0.37139 0.03654  -0.01547 0.04533  107 LEU A CG  
728  C CD1 . LEU A 100 ? 0.39490 0.29213 0.44843 0.04117  -0.02188 0.04370  107 LEU A CD1 
729  C CD2 . LEU A 100 ? 0.42397 0.32737 0.49411 0.03225  -0.01268 0.05172  107 LEU A CD2 
730  N N   . GLY A 101 ? 0.30942 0.27869 0.35411 0.04611  0.00743  0.02286  108 GLY A N   
731  C CA  . GLY A 101 ? 0.30445 0.29750 0.36038 0.05098  0.01139  0.01881  108 GLY A CA  
732  C C   . GLY A 101 ? 0.30737 0.32077 0.36841 0.03961  0.01696  0.01964  108 GLY A C   
733  O O   . GLY A 101 ? 0.30640 0.33911 0.37954 0.03785  0.01682  0.01827  108 GLY A O   
734  N N   . THR A 102 ? 0.28383 0.29430 0.33547 0.02986  0.02098  0.02322  109 THR A N   
735  C CA  . THR A 102 ? 0.25838 0.28468 0.31652 0.01642  0.02701  0.02595  109 THR A CA  
736  C C   . THR A 102 ? 0.35139 0.36742 0.42049 0.00739  0.02432  0.02730  109 THR A C   
737  O O   . THR A 102 ? 0.34175 0.37601 0.42235 -0.00053 0.02692  0.02303  109 THR A O   
738  C CB  . THR A 102 ? 0.36142 0.38332 0.40506 0.00658  0.03112  0.03397  109 THR A CB  
739  O OG1 . THR A 102 ? 0.36820 0.40349 0.39866 0.01270  0.03697  0.02788  109 THR A OG1 
740  C CG2 . THR A 102 ? 0.36926 0.40376 0.42212 -0.00948 0.03788  0.03951  109 THR A CG2 
741  N N   . ILE A 103 ? 0.31755 0.30588 0.38511 0.00771  0.01978  0.03156  110 ILE A N   
742  C CA  . ILE A 103 ? 0.36516 0.34148 0.44480 0.00061  0.02048  0.02866  110 ILE A CA  
743  C C   . ILE A 103 ? 0.43970 0.42998 0.52125 0.00432  0.01874  0.01885  110 ILE A C   
744  O O   . ILE A 103 ? 0.47258 0.47090 0.56046 -0.00605 0.02136  0.01121  110 ILE A O   
745  C CB  . ILE A 103 ? 0.48488 0.43195 0.56843 0.00305  0.01731  0.03539  110 ILE A CB  
746  C CG1 . ILE A 103 ? 0.45708 0.39207 0.54266 -0.00421 0.01722  0.04938  110 ILE A CG1 
747  C CG2 . ILE A 103 ? 0.46991 0.40554 0.56691 -0.00037 0.02102  0.02714  110 ILE A CG2 
748  C CD1 . ILE A 103 ? 0.57921 0.49848 0.66161 0.00203  0.00877  0.06099  110 ILE A CD1 
749  N N   . ALA A 104 ? 0.34210 0.33572 0.41743 0.01760  0.01383  0.01946  111 ALA A N   
750  C CA  . ALA A 104 ? 0.33599 0.34260 0.41158 0.02141  0.01024  0.01579  111 ALA A CA  
751  C C   . ALA A 104 ? 0.37168 0.41254 0.45335 0.01761  0.00928  0.01286  111 ALA A C   
752  O O   . ALA A 104 ? 0.34512 0.40141 0.42614 0.01459  0.00501  0.01064  111 ALA A O   
753  C CB  . ALA A 104 ? 0.33169 0.33083 0.40303 0.03645  0.00516  0.02052  111 ALA A CB  
754  N N   . LYS A 105 ? 0.33621 0.39285 0.42390 0.01648  0.01295  0.01355  112 LYS A N   
755  C CA  . LYS A 105 ? 0.29326 0.38778 0.39347 0.01248  0.01202  0.01151  112 LYS A CA  
756  C C   . LYS A 105 ? 0.31496 0.41784 0.41793 -0.00731 0.01219  0.00449  112 LYS A C   
757  O O   . LYS A 105 ? 0.28460 0.41334 0.39070 -0.01191 0.00549  0.00171  112 LYS A O   
758  C CB  . LYS A 105 ? 0.27824 0.38870 0.38603 0.01377  0.01950  0.01264  112 LYS A CB  
759  C CG  . LYS A 105 ? 0.29908 0.45417 0.42759 0.01585  0.01869  0.01209  112 LYS A CG  
760  C CD  . LYS A 105 ? 0.29721 0.47000 0.43434 0.01708  0.03011  0.01148  112 LYS A CD  
761  C CE  . LYS A 105 ? 0.50805 0.73048 0.67397 0.01789  0.03023  0.01110  112 LYS A CE  
762  N NZ  . LYS A 105 ? 0.57224 0.81545 0.74735 -0.00559 0.03153  0.00935  112 LYS A NZ  
763  N N   . SER A 106 ? 0.29980 0.38079 0.40221 -0.02017 0.01924  0.00180  113 SER A N   
764  C CA  . SER A 106 ? 0.28036 0.36247 0.38754 -0.04026 0.02161  -0.00842 113 SER A CA  
765  C C   . SER A 106 ? 0.27552 0.34470 0.37256 -0.04225 0.01942  -0.01718 113 SER A C   
766  O O   . SER A 106 ? 0.27571 0.36138 0.37096 -0.05676 0.01771  -0.02867 113 SER A O   
767  C CB  . SER A 106 ? 0.46923 0.52516 0.58297 -0.05182 0.03051  -0.00667 113 SER A CB  
768  O OG  . SER A 106 ? 0.47638 0.50305 0.58401 -0.04008 0.03165  0.00373  113 SER A OG  
769  N N   . GLY A 107 ? 0.34995 0.39233 0.43949 -0.02969 0.01997  -0.01280 114 GLY A N   
770  C CA  . GLY A 107 ? 0.26120 0.29410 0.34122 -0.03150 0.02064  -0.02073 114 GLY A CA  
771  C C   . GLY A 107 ? 0.32113 0.38547 0.38985 -0.02982 0.01135  -0.01961 114 GLY A C   
772  O O   . GLY A 107 ? 0.29156 0.36383 0.34882 -0.04144 0.01171  -0.02997 114 GLY A O   
773  N N   . THR A 108 ? 0.23024 0.31324 0.30245 -0.01564 0.00323  -0.00669 115 THR A N   
774  C CA  . THR A 108 ? 0.20503 0.32005 0.27264 -0.01233 -0.00787 -0.00012 115 THR A CA  
775  C C   . THR A 108 ? 0.26550 0.41663 0.33515 -0.03057 -0.01281 -0.00808 115 THR A C   
776  O O   . THR A 108 ? 0.28230 0.45258 0.33758 -0.04069 -0.01947 -0.01085 115 THR A O   
777  C CB  . THR A 108 ? 0.27054 0.39570 0.35056 0.00816  -0.01363 0.01439  115 THR A CB  
778  O OG1 . THR A 108 ? 0.32657 0.41873 0.40183 0.02206  -0.01075 0.01989  115 THR A OG1 
779  C CG2 . THR A 108 ? 0.30861 0.46943 0.39197 0.01289  -0.02679 0.02558  115 THR A CG2 
780  N N   . LYS A 109 ? 0.24930 0.41204 0.33537 -0.03741 -0.00970 -0.01180 116 LYS A N   
781  C CA  . LYS A 109 ? 0.24080 0.43974 0.33287 -0.05744 -0.01482 -0.02020 116 LYS A CA  
782  C C   . LYS A 109 ? 0.26317 0.44976 0.33816 -0.08019 -0.01035 -0.03958 116 LYS A C   
783  O O   . LYS A 109 ? 0.30882 0.52686 0.37411 -0.09608 -0.01919 -0.04664 116 LYS A O   
784  C CB  . LYS A 109 ? 0.28026 0.48829 0.39440 -0.06291 -0.00866 -0.02102 116 LYS A CB  
785  C CG  . LYS A 109 ? 0.31614 0.55761 0.44032 -0.08806 -0.01211 -0.03191 116 LYS A CG  
786  C CD  . LYS A 109 ? 0.40262 0.68088 0.55509 -0.08605 -0.01269 -0.02365 116 LYS A CD  
787  C CE  . LYS A 109 ? 0.56024 0.83723 0.72536 -0.11053 -0.00349 -0.03400 116 LYS A CE  
788  N NZ  . LYS A 109 ? 0.43803 0.72752 0.59757 -0.13837 -0.00922 -0.05133 116 LYS A NZ  
789  N N   . ALA A 110 ? 0.28018 0.42230 0.35237 -0.08229 0.00338  -0.04891 117 ALA A N   
790  C CA  . ALA A 110 ? 0.30637 0.43192 0.36673 -0.10191 0.01174  -0.07083 117 ALA A CA  
791  C C   . ALA A 110 ? 0.34168 0.47366 0.37628 -0.10099 0.00858  -0.07339 117 ALA A C   
792  O O   . ALA A 110 ? 0.34799 0.49146 0.36532 -0.12142 0.00995  -0.09195 117 ALA A O   
793  C CB  . ALA A 110 ? 0.32870 0.40497 0.40071 -0.10022 0.02740  -0.07669 117 ALA A CB  
794  N N   . PHE A 111 ? 0.26975 0.39466 0.29997 -0.07950 0.00506  -0.05553 118 PHE A N   
795  C CA  . PHE A 111 ? 0.29093 0.42205 0.29705 -0.07865 0.00267  -0.05331 118 PHE A CA  
796  C C   . PHE A 111 ? 0.33739 0.51723 0.32808 -0.08901 -0.01379 -0.04779 118 PHE A C   
797  O O   . PHE A 111 ? 0.39591 0.58947 0.35968 -0.10550 -0.01381 -0.05827 118 PHE A O   
798  C CB  . PHE A 111 ? 0.27061 0.38292 0.28070 -0.05431 0.00148  -0.03312 118 PHE A CB  
799  C CG  . PHE A 111 ? 0.28286 0.39943 0.27070 -0.05304 0.00002  -0.02641 118 PHE A CG  
800  C CD1 . PHE A 111 ? 0.31222 0.42460 0.27961 -0.06946 0.01131  -0.04450 118 PHE A CD1 
801  C CD2 . PHE A 111 ? 0.32098 0.44336 0.30971 -0.03567 -0.01046 -0.00235 118 PHE A CD2 
802  C CE1 . PHE A 111 ? 0.33922 0.45801 0.28402 -0.07002 0.01183  -0.03683 118 PHE A CE1 
803  C CE2 . PHE A 111 ? 0.38845 0.51363 0.35744 -0.03591 -0.01143 0.00736  118 PHE A CE2 
804  C CZ  . PHE A 111 ? 0.32045 0.44569 0.26587 -0.05367 -0.00025 -0.00898 118 PHE A CZ  
805  N N   . MET A 112 ? 0.32171 0.53105 0.33003 -0.08022 -0.02776 -0.03129 119 MET A N   
806  C CA  . MET A 112 ? 0.43355 0.69455 0.43476 -0.08875 -0.04652 -0.02189 119 MET A CA  
807  C C   . MET A 112 ? 0.46077 0.74506 0.45066 -0.12000 -0.04758 -0.04541 119 MET A C   
808  O O   . MET A 112 ? 0.43777 0.75516 0.40230 -0.13662 -0.05865 -0.04716 119 MET A O   
809  C CB  . MET A 112 ? 0.39524 0.68298 0.42807 -0.07088 -0.05856 -0.00101 119 MET A CB  
810  C CG  . MET A 112 ? 0.41869 0.67839 0.46550 -0.04156 -0.05474 0.01625  119 MET A CG  
811  S SD  . MET A 112 ? 0.66945 0.94476 0.71093 -0.02411 -0.07046 0.04558  119 MET A SD  
812  C CE  . MET A 112 ? 0.49503 0.75048 0.57139 0.00792  -0.06680 0.05955  119 MET A CE  
813  N N   . GLU A 113 ? 0.41720 0.68512 0.42469 -0.13024 -0.03669 -0.06315 120 GLU A N   
814  C CA  . GLU A 113 ? 0.42812 0.71267 0.42818 -0.16214 -0.03618 -0.08860 120 GLU A CA  
815  C C   . GLU A 113 ? 0.54586 0.80601 0.51413 -0.17949 -0.02276 -0.11447 120 GLU A C   
816  O O   . GLU A 113 ? 0.49096 0.77822 0.43538 -0.20625 -0.02793 -0.13260 120 GLU A O   
817  C CB  . GLU A 113 ? 0.53056 0.79827 0.56078 -0.16857 -0.02624 -0.09844 120 GLU A CB  
818  C CG  . GLU A 113 ? 0.45096 0.75161 0.51238 -0.15675 -0.03691 -0.07759 120 GLU A CG  
819  C CD  . GLU A 113 ? 0.62646 0.90680 0.71495 -0.16186 -0.02421 -0.08324 120 GLU A CD  
820  O OE1 . GLU A 113 ? 0.71721 0.94786 0.80384 -0.16432 -0.00765 -0.09481 120 GLU A OE1 
821  O OE2 . GLU A 113 ? 0.65448 0.97030 0.76844 -0.16349 -0.03059 -0.07432 120 GLU A OE2 
822  N N   . ALA A 114 ? 0.42339 0.63493 0.39185 -0.16549 -0.00499 -0.11774 121 ALA A N   
823  C CA  . ALA A 114 ? 0.49670 0.68607 0.43985 -0.17855 0.01115  -0.14231 121 ALA A CA  
824  C C   . ALA A 114 ? 0.57726 0.80087 0.48176 -0.18468 0.00097  -0.13563 121 ALA A C   
825  O O   . ALA A 114 ? 0.68010 0.91243 0.55370 -0.20893 0.00783  -0.16075 121 ALA A O   
826  C CB  . ALA A 114 ? 0.40564 0.54319 0.36408 -0.15841 0.02976  -0.14088 121 ALA A CB  
827  N N   . LEU A 115 ? 0.42602 0.66841 0.33120 -0.16377 -0.01462 -0.10184 122 LEU A N   
828  C CA  . LEU A 115 ? 0.50735 0.78387 0.37780 -0.16890 -0.02704 -0.08765 122 LEU A CA  
829  C C   . LEU A 115 ? 0.60128 0.92947 0.44876 -0.19794 -0.04338 -0.09714 122 LEU A C   
830  O O   . LEU A 115 ? 0.71939 1.06912 0.52486 -0.21804 -0.04454 -0.10562 122 LEU A O   
831  C CB  . LEU A 115 ? 0.45117 0.73756 0.33659 -0.14075 -0.04296 -0.04747 122 LEU A CB  
832  C CG  . LEU A 115 ? 0.51191 0.75467 0.40667 -0.11665 -0.02988 -0.03597 122 LEU A CG  
833  C CD1 . LEU A 115 ? 0.38425 0.63801 0.29089 -0.09295 -0.04623 0.00123  122 LEU A CD1 
834  C CD2 . LEU A 115 ? 0.51318 0.73961 0.37714 -0.12804 -0.01253 -0.05099 122 LEU A CD2 
835  N N   . GLN A 116 ? 0.69221 1.04409 0.56607 -0.20236 -0.05620 -0.09586 123 GLN A N   
836  C CA  . GLN A 116 ? 0.67597 1.07548 0.53557 -0.22980 -0.07137 -0.10470 123 GLN A CA  
837  C C   . GLN A 116 ? 0.68510 1.06132 0.52651 -0.25626 -0.05048 -0.14467 123 GLN A C   
838  O O   . GLN A 116 ? 0.74530 1.14859 0.56689 -0.27574 -0.05581 -0.15086 123 GLN A O   
839  C CB  . GLN A 116 ? 0.78675 1.21331 0.68804 -0.22429 -0.08618 -0.09148 123 GLN A CB  
840  C CG  . GLN A 116 ? 0.73407 1.19107 0.65791 -0.19697 -0.10694 -0.05006 123 GLN A CG  
841  C CD  . GLN A 116 ? 0.80733 1.28107 0.70085 -0.19154 -0.11797 -0.02590 123 GLN A CD  
842  O OE1 . GLN A 116 ? 0.91754 1.41655 0.78741 -0.20953 -0.12490 -0.02689 123 GLN A OE1 
843  N NE2 . GLN A 116 ? 0.63750 1.09628 0.53227 -0.16770 -0.11916 -0.00313 123 GLN A NE2 
844  N N   . ALA A 117 ? 0.66976 0.99544 0.52106 -0.25630 -0.02651 -0.17083 124 ALA A N   
845  C CA  . ALA A 117 ? 0.79655 1.09381 0.63517 -0.27586 -0.00294 -0.20682 124 ALA A CA  
846  C C   . ALA A 117 ? 0.92890 1.22170 0.73014 -0.27853 0.00923  -0.21287 124 ALA A C   
847  O O   . ALA A 117 ? 1.04443 1.37675 0.81605 -0.28483 -0.00504 -0.19663 124 ALA A O   
848  C CB  . ALA A 117 ? 0.69578 0.93736 0.56796 -0.27072 0.01920  -0.22723 124 ALA A CB  
849  N N   . GLY A 118 ? 0.78003 1.02554 0.58650 -0.27269 0.03598  -0.23327 125 GLY A N   
850  C CA  . GLY A 118 ? 0.81752 1.05846 0.59445 -0.27515 0.05153  -0.24052 125 GLY A CA  
851  C C   . GLY A 118 ? 0.66935 0.88048 0.45193 -0.25243 0.06324  -0.23111 125 GLY A C   
852  O O   . GLY A 118 ? 0.75449 0.95125 0.52456 -0.25251 0.08354  -0.24181 125 GLY A O   
853  N N   . ALA A 119 ? 0.70575 0.90759 0.51426 -0.22993 0.05136  -0.20661 126 ALA A N   
854  C CA  . ALA A 119 ? 0.79118 0.95959 0.62084 -0.20092 0.06204  -0.18757 126 ALA A CA  
855  C C   . ALA A 119 ? 0.73584 0.93035 0.53956 -0.19163 0.04982  -0.15578 126 ALA A C   
856  O O   . ALA A 119 ? 0.57830 0.81581 0.35994 -0.19865 0.02652  -0.13622 126 ALA A O   
857  C CB  . ALA A 119 ? 0.61691 0.76051 0.49325 -0.17648 0.05527  -0.16765 126 ALA A CB  
858  N N   . ASP A 120 ? 0.61035 0.77905 0.42058 -0.17598 0.06526  -0.14881 127 ASP A N   
859  C CA  . ASP A 120 ? 0.69709 0.88186 0.48917 -0.16594 0.05652  -0.11672 127 ASP A CA  
860  C C   . ASP A 120 ? 0.61702 0.78113 0.44628 -0.13508 0.04562  -0.08429 127 ASP A C   
861  O O   . ASP A 120 ? 0.52597 0.65736 0.39193 -0.12103 0.05232  -0.08992 127 ASP A O   
862  C CB  . ASP A 120 ? 0.59589 0.77075 0.36865 -0.17256 0.08200  -0.13053 127 ASP A CB  
863  C CG  . ASP A 120 ? 0.96260 1.14714 0.70420 -0.20232 0.10132  -0.17332 127 ASP A CG  
864  O OD1 . ASP A 120 ? 0.98020 1.14514 0.72335 -0.20514 0.13010  -0.19652 127 ASP A OD1 
865  O OD2 . ASP A 120 ? 1.04755 1.25980 0.76802 -0.22239 0.08759  -0.18347 127 ASP A OD2 
866  N N   . ILE A 121 ? 0.54967 0.73306 0.36827 -0.12579 0.02857  -0.04985 128 ILE A N   
867  C CA  . ILE A 121 ? 0.41547 0.57857 0.26615 -0.09812 0.01938  -0.02127 128 ILE A CA  
868  C C   . ILE A 121 ? 0.53155 0.65400 0.40496 -0.08601 0.03940  -0.02839 128 ILE A C   
869  O O   . ILE A 121 ? 0.47688 0.57364 0.38348 -0.06727 0.03721  -0.02133 128 ILE A O   
870  C CB  . ILE A 121 ? 0.41496 0.60128 0.25062 -0.09219 0.00122  0.01547  128 ILE A CB  
871  C CG1 . ILE A 121 ? 0.44515 0.67438 0.27044 -0.09957 -0.02292 0.02773  128 ILE A CG1 
872  C CG2 . ILE A 121 ? 0.37589 0.53415 0.24403 -0.06532 -0.00346 0.03998  128 ILE A CG2 
873  C CD1 . ILE A 121 ? 0.52778 0.79128 0.32228 -0.10676 -0.03831 0.05738  128 ILE A CD1 
874  N N   . SER A 122 ? 0.50430 0.62353 0.36077 -0.09754 0.05949  -0.04304 129 SER A N   
875  C CA  . SER A 122 ? 0.39887 0.48554 0.28192 -0.08680 0.07878  -0.04946 129 SER A CA  
876  C C   . SER A 122 ? 0.44037 0.49826 0.35850 -0.08057 0.08832  -0.07088 129 SER A C   
877  O O   . SER A 122 ? 0.44175 0.47348 0.39029 -0.06827 0.09934  -0.07125 129 SER A O   
878  C CB  . SER A 122 ? 0.43651 0.53141 0.29623 -0.10227 0.10162  -0.06437 129 SER A CB  
879  O OG  . SER A 122 ? 0.52770 0.62688 0.37431 -0.12097 0.11805  -0.10134 129 SER A OG  
880  N N   . MET A 123 ? 0.41979 0.48313 0.33647 -0.08963 0.08346  -0.08644 130 MET A N   
881  C CA  . MET A 123 ? 0.40825 0.44375 0.35850 -0.08483 0.09042  -0.10186 130 MET A CA  
882  C C   . MET A 123 ? 0.42034 0.44699 0.39401 -0.06736 0.07256  -0.07975 130 MET A C   
883  O O   . MET A 123 ? 0.39903 0.40955 0.39471 -0.06633 0.07380  -0.08778 130 MET A O   
884  C CB  . MET A 123 ? 0.47297 0.51667 0.41111 -0.10667 0.09636  -0.13148 130 MET A CB  
885  C CG  . MET A 123 ? 0.60218 0.64989 0.51817 -0.12558 0.11909  -0.16160 130 MET A CG  
886  S SD  . MET A 123 ? 0.77257 0.82947 0.67036 -0.15558 0.12583  -0.20123 130 MET A SD  
887  C CE  . MET A 123 ? 0.67236 0.69634 0.61875 -0.14503 0.12139  -0.20023 130 MET A CE  
888  N N   . ILE A 124 ? 0.30835 0.34426 0.27777 -0.05452 0.05743  -0.05257 131 ILE A N   
889  C CA  . ILE A 124 ? 0.31656 0.34519 0.30572 -0.03823 0.04297  -0.03466 131 ILE A CA  
890  C C   . ILE A 124 ? 0.33747 0.33351 0.35710 -0.02812 0.05061  -0.03764 131 ILE A C   
891  O O   . ILE A 124 ? 0.29930 0.28881 0.33328 -0.02202 0.04361  -0.03283 131 ILE A O   
892  C CB  . ILE A 124 ? 0.30910 0.34541 0.29253 -0.02542 0.03000  -0.00820 131 ILE A CB  
893  C CG1 . ILE A 124 ? 0.25992 0.28839 0.26289 -0.00894 0.01794  0.00561  131 ILE A CG1 
894  C CG2 . ILE A 124 ? 0.30931 0.32946 0.29521 -0.02121 0.03981  -0.00284 131 ILE A CG2 
895  C CD1 . ILE A 124 ? 0.34340 0.38252 0.34332 0.00259  0.00412  0.02866  131 ILE A CD1 
896  N N   . GLY A 125 ? 0.34851 0.32678 0.37954 -0.02699 0.06511  -0.04454 132 GLY A N   
897  C CA  . GLY A 125 ? 0.40598 0.35716 0.46914 -0.01625 0.06902  -0.04196 132 GLY A CA  
898  C C   . GLY A 125 ? 0.42435 0.36144 0.50515 -0.02126 0.07440  -0.05473 132 GLY A C   
899  O O   . GLY A 125 ? 0.48809 0.40755 0.59172 -0.01243 0.07049  -0.04514 132 GLY A O   
900  N N   . GLN A 126 ? 0.44873 0.39320 0.51856 -0.03716 0.08290  -0.07571 133 GLN A N   
901  C CA  . GLN A 126 ? 0.58408 0.51164 0.67313 -0.04420 0.08918  -0.08848 133 GLN A CA  
902  C C   . GLN A 126 ? 0.61762 0.55199 0.70649 -0.04361 0.07422  -0.07574 133 GLN A C   
903  O O   . GLN A 126 ? 0.55369 0.47244 0.66074 -0.04904 0.07795  -0.08039 133 GLN A O   
904  C CB  . GLN A 126 ? 0.51543 0.44862 0.59147 -0.06453 0.10291  -0.11827 133 GLN A CB  
905  C CG  . GLN A 126 ? 0.67905 0.62633 0.73229 -0.07080 0.11393  -0.13061 133 GLN A CG  
906  C CD  . GLN A 126 ? 0.85372 0.79606 0.90187 -0.09001 0.13454  -0.16624 133 GLN A CD  
907  O OE1 . GLN A 126 ? 0.85008 0.78928 0.89880 -0.10417 0.13487  -0.18221 133 GLN A OE1 
908  N NE2 . GLN A 126 ? 0.86689 0.80925 0.91005 -0.09221 0.15327  -0.18067 133 GLN A NE2 
909  N N   . PHE A 127 ? 0.39854 0.35524 0.47027 -0.03716 0.05901  -0.05956 134 PHE A N   
910  C CA  . PHE A 127 ? 0.33599 0.30569 0.40788 -0.03669 0.04740  -0.04977 134 PHE A CA  
911  C C   . PHE A 127 ? 0.40139 0.36349 0.48076 -0.01963 0.03868  -0.02903 134 PHE A C   
912  O O   . PHE A 127 ? 0.42874 0.40571 0.50572 -0.01668 0.03023  -0.02048 134 PHE A O   
913  C CB  . PHE A 127 ? 0.31515 0.32146 0.36556 -0.04384 0.03760  -0.05045 134 PHE A CB  
914  C CG  . PHE A 127 ? 0.29815 0.31678 0.33510 -0.06460 0.04410  -0.07251 134 PHE A CG  
915  C CD1 . PHE A 127 ? 0.37837 0.40050 0.42216 -0.08132 0.04670  -0.08707 134 PHE A CD1 
916  C CD2 . PHE A 127 ? 0.29301 0.31968 0.30903 -0.06971 0.04863  -0.07981 134 PHE A CD2 
917  C CE1 . PHE A 127 ? 0.39401 0.42663 0.42347 -0.10319 0.05282  -0.11128 134 PHE A CE1 
918  C CE2 . PHE A 127 ? 0.35886 0.39836 0.35699 -0.09139 0.05559  -0.10331 134 PHE A CE2 
919  C CZ  . PHE A 127 ? 0.35882 0.40065 0.36353 -0.10837 0.05735  -0.12054 134 PHE A CZ  
920  N N   . GLY A 128 ? 0.41427 0.35594 0.50331 -0.00943 0.04114  -0.02231 135 GLY A N   
921  C CA  . GLY A 128 ? 0.40387 0.33715 0.49816 0.00328  0.03270  -0.00569 135 GLY A CA  
922  C C   . GLY A 128 ? 0.53887 0.48652 0.61887 0.01275  0.02272  0.00378  135 GLY A C   
923  O O   . GLY A 128 ? 0.48102 0.42557 0.56139 0.02073  0.01622  0.01306  135 GLY A O   
924  N N   . VAL A 129 ? 0.32235 0.28519 0.38967 0.01150  0.02170  0.00189  136 VAL A N   
925  C CA  . VAL A 129 ? 0.28078 0.25495 0.33973 0.02144  0.01220  0.01319  136 VAL A CA  
926  C C   . VAL A 129 ? 0.24578 0.21674 0.29823 0.02297  0.01339  0.01789  136 VAL A C   
927  O O   . VAL A 129 ? 0.26560 0.24810 0.30991 0.02778  0.00643  0.02800  136 VAL A O   
928  C CB  . VAL A 129 ? 0.28514 0.28873 0.33764 0.01868  0.00606  0.01343  136 VAL A CB  
929  C CG1 . VAL A 129 ? 0.33110 0.33987 0.39253 0.01771  0.00603  0.01095  136 VAL A CG1 
930  C CG2 . VAL A 129 ? 0.25497 0.27557 0.29603 0.00343  0.00924  0.00326  136 VAL A CG2 
931  N N   . GLY A 130 ? 0.31108 0.27964 0.30964 -0.02310 -0.01901 -0.05714 137 GLY A N   
932  C CA  . GLY A 130 ? 0.23730 0.20890 0.22413 -0.01042 -0.01453 -0.05722 137 GLY A CA  
933  C C   . GLY A 130 ? 0.28946 0.27812 0.28729 -0.00700 -0.00710 -0.04848 137 GLY A C   
934  O O   . GLY A 130 ? 0.27419 0.27066 0.26760 0.00031  -0.00428 -0.04606 137 GLY A O   
935  N N   . PHE A 131 ? 0.23986 0.23290 0.25073 -0.01214 -0.00412 -0.04348 138 PHE A N   
936  C CA  . PHE A 131 ? 0.22458 0.22976 0.24415 -0.00976 0.00082  -0.03738 138 PHE A CA  
937  C C   . PHE A 131 ? 0.23913 0.25644 0.26177 -0.00857 -0.00081 -0.03620 138 PHE A C   
938  O O   . PHE A 131 ? 0.23923 0.26076 0.26279 -0.00377 0.00264  -0.03212 138 PHE A O   
939  C CB  . PHE A 131 ? 0.27823 0.28565 0.30710 -0.01476 0.00260  -0.03412 138 PHE A CB  
940  C CG  . PHE A 131 ? 0.24910 0.26657 0.28467 -0.01316 0.00507  -0.03074 138 PHE A CG  
941  C CD1 . PHE A 131 ? 0.21171 0.22856 0.24791 -0.00970 0.00760  -0.02833 138 PHE A CD1 
942  C CD2 . PHE A 131 ? 0.23442 0.26172 0.27607 -0.01488 0.00431  -0.03018 138 PHE A CD2 
943  C CE1 . PHE A 131 ? 0.18391 0.20484 0.22452 -0.00917 0.00802  -0.02699 138 PHE A CE1 
944  C CE2 . PHE A 131 ? 0.24229 0.27385 0.28662 -0.01150 0.00634  -0.02863 138 PHE A CE2 
945  C CZ  . PHE A 131 ? 0.24248 0.26837 0.28520 -0.00925 0.00754  -0.02783 138 PHE A CZ  
946  N N   . TYR A 132 ? 0.21863 0.24205 0.24436 -0.01311 -0.00640 -0.03871 139 TYR A N   
947  C CA  . TYR A 132 ? 0.22473 0.26167 0.25430 -0.01025 -0.00826 -0.03661 139 TYR A CA  
948  C C   . TYR A 132 ? 0.22316 0.25952 0.24031 -0.00272 -0.00967 -0.03698 139 TYR A C   
949  O O   . TYR A 132 ? 0.23206 0.27772 0.25052 0.00206  -0.01006 -0.03317 139 TYR A O   
950  C CB  . TYR A 132 ? 0.24041 0.28941 0.27990 -0.01702 -0.01437 -0.03796 139 TYR A CB  
951  C CG  . TYR A 132 ? 0.23461 0.28724 0.28625 -0.02349 -0.01104 -0.03507 139 TYR A CG  
952  C CD1 . TYR A 132 ? 0.25890 0.32155 0.31809 -0.01966 -0.00563 -0.03047 139 TYR A CD1 
953  C CD2 . TYR A 132 ? 0.25388 0.29807 0.30735 -0.03237 -0.01296 -0.03657 139 TYR A CD2 
954  C CE1 . TYR A 132 ? 0.24461 0.31198 0.31160 -0.02344 -0.00146 -0.02722 139 TYR A CE1 
955  C CE2 . TYR A 132 ? 0.26103 0.30956 0.32459 -0.03758 -0.00862 -0.03153 139 TYR A CE2 
956  C CZ  . TYR A 132 ? 0.28918 0.35097 0.35884 -0.03254 -0.00251 -0.02674 139 TYR A CZ  
957  O OH  . TYR A 132 ? 0.28118 0.34876 0.35765 -0.03558 0.00287  -0.02119 139 TYR A OH  
958  N N   . SER A 133 ? 0.23787 0.26323 0.24143 0.00027  -0.00966 -0.04073 140 SER A N   
959  C CA  . SER A 133 ? 0.24962 0.27543 0.23869 0.00982  -0.00838 -0.03939 140 SER A CA  
960  C C   . SER A 133 ? 0.23899 0.26844 0.23257 0.01505  0.00042  -0.02964 140 SER A C   
961  O O   . SER A 133 ? 0.24429 0.27686 0.22843 0.02291  0.00319  -0.02484 140 SER A O   
962  C CB  . SER A 133 ? 0.24514 0.25771 0.21665 0.01428  -0.00874 -0.04590 140 SER A CB  
963  O OG  . SER A 133 ? 0.29386 0.30059 0.26785 0.01689  -0.00042 -0.04244 140 SER A OG  
964  N N   . ALA A 134 ? 0.24814 0.27683 0.25539 0.01050  0.00432  -0.02627 141 ALA A N   
965  C CA  . ALA A 134 ? 0.23405 0.26442 0.24833 0.01241  0.01010  -0.01775 141 ALA A CA  
966  C C   . ALA A 134 ? 0.23125 0.26589 0.24557 0.01610  0.00909  -0.01289 141 ALA A C   
967  O O   . ALA A 134 ? 0.20852 0.24223 0.22360 0.01946  0.01376  -0.00434 141 ALA A O   
968  C CB  . ALA A 134 ? 0.24279 0.27042 0.26957 0.00624  0.01098  -0.01782 141 ALA A CB  
969  N N   . TYR A 135 ? 0.18547 0.22566 0.20028 0.01572  0.00319  -0.01684 142 TYR A N   
970  C CA  . TYR A 135 ? 0.25501 0.30055 0.27030 0.02136  0.00183  -0.01182 142 TYR A CA  
971  C C   . TYR A 135 ? 0.24345 0.29365 0.24448 0.02921  0.00016  -0.00864 142 TYR A C   
972  O O   . TYR A 135 ? 0.25932 0.31463 0.25882 0.03574  -0.00134 -0.00310 142 TYR A O   
973  C CB  . TYR A 135 ? 0.22346 0.27842 0.24757 0.01923  -0.00327 -0.01590 142 TYR A CB  
974  C CG  . TYR A 135 ? 0.24747 0.29749 0.28177 0.01557  0.00023  -0.01671 142 TYR A CG  
975  C CD1 . TYR A 135 ? 0.21526 0.25915 0.25260 0.02043  0.00320  -0.01259 142 TYR A CD1 
976  C CD2 . TYR A 135 ? 0.27852 0.32709 0.31664 0.00820  0.00042  -0.02166 142 TYR A CD2 
977  C CE1 . TYR A 135 ? 0.20271 0.23986 0.24491 0.01841  0.00537  -0.01526 142 TYR A CE1 
978  C CE2 . TYR A 135 ? 0.21584 0.26040 0.25951 0.00641  0.00336  -0.02243 142 TYR A CE2 
979  C CZ  . TYR A 135 ? 0.26106 0.30015 0.30578 0.01171  0.00543  -0.02013 142 TYR A CZ  
980  O OH  . TYR A 135 ? 0.25004 0.28325 0.29606 0.01122  0.00722  -0.02282 142 TYR A OH  
981  N N   . LEU A 136 ? 0.22325 0.27120 0.21168 0.03065  0.00064  -0.01179 143 LEU A N   
982  C CA  . LEU A 136 ? 0.23329 0.28438 0.20407 0.04054  0.00142  -0.00737 143 LEU A CA  
983  C C   . LEU A 136 ? 0.29751 0.34641 0.27027 0.04533  0.01126  0.00673  143 LEU A C   
984  O O   . LEU A 136 ? 0.30079 0.35364 0.26218 0.05433  0.01273  0.01496  143 LEU A O   
985  C CB  . LEU A 136 ? 0.28017 0.32689 0.23426 0.04312  0.00093  -0.01492 143 LEU A CB  
986  C CG  . LEU A 136 ? 0.29795 0.34241 0.24501 0.03863  -0.01050 -0.02905 143 LEU A CG  
987  C CD1 . LEU A 136 ? 0.29403 0.32653 0.22471 0.04201  -0.00880 -0.03656 143 LEU A CD1 
988  C CD2 . LEU A 136 ? 0.28476 0.33902 0.22056 0.04334  -0.02064 -0.03128 143 LEU A CD2 
989  N N   . VAL A 137 ? 0.26683 0.30968 0.25417 0.03894  0.01740  0.01046  144 VAL A N   
990  C CA  . VAL A 137 ? 0.25143 0.29183 0.24434 0.04017  0.02616  0.02439  144 VAL A CA  
991  C C   . VAL A 137 ? 0.25482 0.28575 0.26533 0.03289  0.02619  0.02777  144 VAL A C   
992  O O   . VAL A 137 ? 0.27351 0.29894 0.28969 0.03267  0.03137  0.04001  144 VAL A O   
993  C CB  . VAL A 137 ? 0.22079 0.26484 0.21422 0.04004  0.03395  0.02777  144 VAL A CB  
994  C CG1 . VAL A 137 ? 0.28566 0.33586 0.25639 0.05106  0.03549  0.02548  144 VAL A CG1 
995  C CG2 . VAL A 137 ? 0.22165 0.26294 0.22662 0.03156  0.03162  0.01858  144 VAL A CG2 
996  N N   . ALA A 138 ? 0.26039 0.28780 0.27867 0.02713  0.02075  0.01778  145 ALA A N   
997  C CA  . ALA A 138 ? 0.25606 0.27213 0.28678 0.02153  0.02013  0.01822  145 ALA A CA  
998  C C   . ALA A 138 ? 0.27861 0.29148 0.30793 0.02666  0.01597  0.01559  145 ALA A C   
999  O O   . ALA A 138 ? 0.28863 0.31187 0.31453 0.02932  0.01170  0.00878  145 ALA A O   
1000 C CB  . ALA A 138 ? 0.23538 0.25051 0.27398 0.01335  0.01824  0.00964  145 ALA A CB  
1001 N N   . GLU A 139 ? 0.29559 0.29398 0.32864 0.02811  0.01712  0.02151  146 GLU A N   
1002 C CA  . GLU A 139 ? 0.24146 0.23452 0.27370 0.03494  0.01414  0.01844  146 GLU A CA  
1003 C C   . GLU A 139 ? 0.32059 0.30818 0.35768 0.03074  0.01179  0.00773  146 GLU A C   
1004 O O   . GLU A 139 ? 0.27098 0.26131 0.30701 0.03762  0.01023  0.00319  146 GLU A O   
1005 C CB  . GLU A 139 ? 0.32939 0.30390 0.36059 0.04032  0.01630  0.02882  146 GLU A CB  
1006 C CG  . GLU A 139 ? 0.53042 0.48208 0.56918 0.03124  0.01696  0.03008  146 GLU A CG  
1007 C CD  . GLU A 139 ? 0.72354 0.65465 0.76213 0.03404  0.01962  0.04336  146 GLU A CD  
1008 O OE1 . GLU A 139 ? 0.77530 0.68602 0.82181 0.02453  0.01909  0.04586  146 GLU A OE1 
1009 O OE2 . GLU A 139 ? 0.76060 0.69567 0.79141 0.04534  0.02153  0.05186  146 GLU A OE2 
1010 N N   . LYS A 140 ? 0.28659 0.26875 0.32862 0.02089  0.01177  0.00447  147 LYS A N   
1011 C CA  . LYS A 140 ? 0.27887 0.25698 0.32235 0.01728  0.00917  -0.00549 147 LYS A CA  
1012 C C   . LYS A 140 ? 0.25007 0.23526 0.29797 0.00794  0.00891  -0.00766 147 LYS A C   
1013 O O   . LYS A 140 ? 0.25863 0.24425 0.31148 0.00308  0.01074  -0.00108 147 LYS A O   
1014 C CB  . LYS A 140 ? 0.27402 0.22812 0.31685 0.01728  0.00700  -0.00754 147 LYS A CB  
1015 C CG  . LYS A 140 ? 0.34893 0.29827 0.38791 0.01660  0.00389  -0.01895 147 LYS A CG  
1016 C CD  . LYS A 140 ? 0.39354 0.31507 0.42687 0.01926  0.00045  -0.02342 147 LYS A CD  
1017 C CE  . LYS A 140 ? 0.43496 0.34117 0.47526 0.00615  -0.00446 -0.02236 147 LYS A CE  
1018 N NZ  . LYS A 140 ? 0.49559 0.36880 0.53128 0.00689  -0.00902 -0.02498 147 LYS A NZ  
1019 N N   . VAL A 141 ? 0.24072 0.23294 0.28728 0.00656  0.00748  -0.01534 148 VAL A N   
1020 C CA  . VAL A 141 ? 0.23866 0.23637 0.28824 -0.00025 0.00688  -0.01740 148 VAL A CA  
1021 C C   . VAL A 141 ? 0.24656 0.23736 0.29443 -0.00234 0.00350  -0.02436 148 VAL A C   
1022 O O   . VAL A 141 ? 0.25809 0.24919 0.30003 0.00268  0.00361  -0.02934 148 VAL A O   
1023 C CB  . VAL A 141 ? 0.26648 0.27765 0.31360 0.00027  0.00813  -0.01890 148 VAL A CB  
1024 C CG1 . VAL A 141 ? 0.24818 0.26187 0.29719 -0.00455 0.00787  -0.02039 148 VAL A CG1 
1025 C CG2 . VAL A 141 ? 0.25072 0.26740 0.29512 0.00348  0.00990  -0.01398 148 VAL A CG2 
1026 N N   . THR A 142 ? 0.26195 0.24877 0.31490 -0.00901 0.00041  -0.02422 149 THR A N   
1027 C CA  . THR A 142 ? 0.24556 0.22745 0.29484 -0.01120 -0.00466 -0.03131 149 THR A CA  
1028 C C   . THR A 142 ? 0.28322 0.27785 0.33599 -0.01471 -0.00499 -0.03017 149 THR A C   
1029 O O   . THR A 142 ? 0.26113 0.26307 0.32342 -0.01833 -0.00376 -0.02403 149 THR A O   
1030 C CB  . THR A 142 ? 0.29281 0.25853 0.34555 -0.01672 -0.01109 -0.03302 149 THR A CB  
1031 O OG1 . THR A 142 ? 0.31909 0.26913 0.36839 -0.01241 -0.01005 -0.03241 149 THR A OG1 
1032 C CG2 . THR A 142 ? 0.31136 0.27027 0.35508 -0.01712 -0.01820 -0.04289 149 THR A CG2 
1033 N N   . VAL A 143 ? 0.22780 0.22561 0.27239 -0.01211 -0.00565 -0.03484 150 VAL A N   
1034 C CA  . VAL A 143 ? 0.23088 0.23819 0.27661 -0.01356 -0.00595 -0.03311 150 VAL A CA  
1035 C C   . VAL A 143 ? 0.23397 0.23857 0.27335 -0.01404 -0.01256 -0.03826 150 VAL A C   
1036 O O   . VAL A 143 ? 0.28550 0.28545 0.31234 -0.00930 -0.01269 -0.04353 150 VAL A O   
1037 C CB  . VAL A 143 ? 0.24843 0.26178 0.28946 -0.01029 -0.00055 -0.03169 150 VAL A CB  
1038 C CG1 . VAL A 143 ? 0.27210 0.29044 0.31283 -0.01063 -0.00084 -0.02916 150 VAL A CG1 
1039 C CG2 . VAL A 143 ? 0.23038 0.24588 0.27525 -0.00985 0.00340  -0.02858 150 VAL A CG2 
1040 N N   . ILE A 144 ? 0.21515 0.22470 0.26284 -0.01882 -0.01815 -0.03647 151 ILE A N   
1041 C CA  . ILE A 144 ? 0.23781 0.24842 0.27950 -0.01930 -0.02646 -0.04093 151 ILE A CA  
1042 C C   . ILE A 144 ? 0.22492 0.24797 0.26628 -0.01591 -0.02404 -0.03559 151 ILE A C   
1043 O O   . ILE A 144 ? 0.24195 0.27362 0.29490 -0.01654 -0.02046 -0.02880 151 ILE A O   
1044 C CB  . ILE A 144 ? 0.28506 0.29515 0.33907 -0.02796 -0.03654 -0.04197 151 ILE A CB  
1045 C CG1 . ILE A 144 ? 0.35223 0.34744 0.41108 -0.03251 -0.03687 -0.04337 151 ILE A CG1 
1046 C CG2 . ILE A 144 ? 0.31456 0.32178 0.35744 -0.02813 -0.04806 -0.05019 151 ILE A CG2 
1047 C CD1 . ILE A 144 ? 0.31536 0.29099 0.35576 -0.02752 -0.03917 -0.05357 151 ILE A CD1 
1048 N N   . THR A 145 ? 0.26479 0.28773 0.29131 -0.01078 -0.02513 -0.03794 152 THR A N   
1049 C CA  . THR A 145 ? 0.20763 0.23849 0.23229 -0.00664 -0.02183 -0.03132 152 THR A CA  
1050 C C   . THR A 145 ? 0.27340 0.30701 0.28387 -0.00219 -0.02800 -0.03309 152 THR A C   
1051 O O   . THR A 145 ? 0.23956 0.26708 0.23566 -0.00004 -0.03146 -0.04026 152 THR A O   
1052 C CB  . THR A 145 ? 0.22355 0.25072 0.24435 -0.00407 -0.01153 -0.02759 152 THR A CB  
1053 O OG1 . THR A 145 ? 0.23437 0.26410 0.25499 -0.00102 -0.00866 -0.02064 152 THR A OG1 
1054 C CG2 . THR A 145 ? 0.30399 0.32760 0.31082 -0.00063 -0.00844 -0.03057 152 THR A CG2 
1055 N N   . LYS A 146 ? 0.23492 0.27735 0.24749 0.00102  -0.02926 -0.02642 153 LYS A N   
1056 C CA  . LYS A 146 ? 0.25895 0.30622 0.25718 0.00675  -0.03552 -0.02599 153 LYS A CA  
1057 C C   . LYS A 146 ? 0.30485 0.35494 0.30096 0.01322  -0.02937 -0.01519 153 LYS A C   
1058 O O   . LYS A 146 ? 0.25880 0.31489 0.26845 0.01401  -0.02907 -0.00956 153 LYS A O   
1059 C CB  . LYS A 146 ? 0.25635 0.31373 0.26193 0.00327  -0.04987 -0.02988 153 LYS A CB  
1060 C CG  . LYS A 146 ? 0.29977 0.36576 0.29113 0.01034  -0.05819 -0.02838 153 LYS A CG  
1061 C CD  . LYS A 146 ? 0.28049 0.33698 0.24432 0.01538  -0.06023 -0.03622 153 LYS A CD  
1062 C CE  . LYS A 146 ? 0.37177 0.43770 0.31913 0.02228  -0.07187 -0.03664 153 LYS A CE  
1063 N NZ  . LYS A 146 ? 0.33087 0.40253 0.26998 0.03225  -0.06398 -0.02313 153 LYS A NZ  
1064 N N   . HIS A 147 ? 0.25042 0.29557 0.22941 0.01859  -0.02377 -0.01152 154 HIS A N   
1065 C CA  . HIS A 147 ? 0.25445 0.29789 0.22823 0.02473  -0.01813 -0.00009 154 HIS A CA  
1066 C C   . HIS A 147 ? 0.29991 0.35149 0.25790 0.03293  -0.02555 0.00286  154 HIS A C   
1067 O O   . HIS A 147 ? 0.30490 0.35947 0.24868 0.03444  -0.03161 -0.00444 154 HIS A O   
1068 C CB  . HIS A 147 ? 0.25709 0.29075 0.22483 0.02353  -0.00633 0.00467  154 HIS A CB  
1069 C CG  . HIS A 147 ? 0.30542 0.33132 0.27081 0.02687  0.00026  0.01714  154 HIS A CG  
1070 N ND1 . HIS A 147 ? 0.31441 0.34170 0.26456 0.03485  0.00074  0.02651  154 HIS A ND1 
1071 C CD2 . HIS A 147 ? 0.34480 0.35846 0.31936 0.02348  0.00626  0.02172  154 HIS A CD2 
1072 C CE1 . HIS A 147 ? 0.38801 0.40304 0.33979 0.03574  0.00731  0.03749  154 HIS A CE1 
1073 N NE2 . HIS A 147 ? 0.38097 0.38637 0.34718 0.02859  0.01019  0.03377  154 HIS A NE2 
1074 N N   . ASN A 148 ? 0.28249 0.33669 0.24108 0.03967  -0.02569 0.01315  155 ASN A N   
1075 C CA  . ASN A 148 ? 0.30317 0.36729 0.24648 0.04897  -0.03380 0.01740  155 ASN A CA  
1076 C C   . ASN A 148 ? 0.37631 0.43709 0.29382 0.05381  -0.03015 0.01852  155 ASN A C   
1077 O O   . ASN A 148 ? 0.37427 0.44389 0.27411 0.06041  -0.03960 0.01578  155 ASN A O   
1078 C CB  . ASN A 148 ? 0.33141 0.39527 0.27703 0.05794  -0.03136 0.03115  155 ASN A CB  
1079 C CG  . ASN A 148 ? 0.33889 0.41516 0.30607 0.05870  -0.03803 0.03081  155 ASN A CG  
1080 O OD1 . ASN A 148 ? 0.30263 0.39384 0.28124 0.05315  -0.04843 0.02221  155 ASN A OD1 
1081 N ND2 . ASN A 148 ? 0.35018 0.42022 0.32316 0.06614  -0.03191 0.04092  155 ASN A ND2 
1082 N N   . ASP A 149 ? 0.33272 0.38280 0.24764 0.05100  -0.01684 0.02259  156 ASP A N   
1083 C CA  . ASP A 149 ? 0.37097 0.42097 0.26356 0.05693  -0.00964 0.02778  156 ASP A CA  
1084 C C   . ASP A 149 ? 0.46295 0.51445 0.34765 0.05510  -0.00905 0.01534  156 ASP A C   
1085 O O   . ASP A 149 ? 0.47010 0.52405 0.33584 0.06168  -0.00150 0.01914  156 ASP A O   
1086 C CB  . ASP A 149 ? 0.39840 0.43856 0.29519 0.05481  0.00522  0.04280  156 ASP A CB  
1087 C CG  . ASP A 149 ? 0.48773 0.52164 0.38404 0.06051  0.00570  0.05697  156 ASP A CG  
1088 O OD1 . ASP A 149 ? 0.44049 0.48250 0.33031 0.06873  -0.00475 0.05673  156 ASP A OD1 
1089 O OD2 . ASP A 149 ? 0.52799 0.54836 0.43087 0.05681  0.01572  0.06838  156 ASP A OD2 
1090 N N   . ASP A 150 ? 0.39375 0.44364 0.29176 0.04768  -0.01591 0.00169  157 ASP A N   
1091 C CA  . ASP A 150 ? 0.39073 0.43794 0.28188 0.04704  -0.01496 -0.01005 157 ASP A CA  
1092 C C   . ASP A 150 ? 0.42059 0.46583 0.31451 0.04317  -0.03028 -0.02544 157 ASP A C   
1093 O O   . ASP A 150 ? 0.34458 0.39479 0.24882 0.03986  -0.04116 -0.02595 157 ASP A O   
1094 C CB  . ASP A 150 ? 0.34437 0.38744 0.25298 0.03974  -0.00342 -0.00814 157 ASP A CB  
1095 C CG  . ASP A 150 ? 0.45002 0.49505 0.34617 0.04505  0.00516  -0.01075 157 ASP A CG  
1096 O OD1 . ASP A 150 ? 0.38331 0.42768 0.25807 0.05336  -0.00014 -0.02036 157 ASP A OD1 
1097 O OD2 . ASP A 150 ? 0.37520 0.42291 0.28296 0.04141  0.01669  -0.00364 157 ASP A OD2 
1098 N N   . GLU A 151 ? 0.36285 0.40088 0.24861 0.04371  -0.03093 -0.03726 158 GLU A N   
1099 C CA  . GLU A 151 ? 0.38678 0.41738 0.27511 0.03841  -0.04506 -0.05216 158 GLU A CA  
1100 C C   . GLU A 151 ? 0.33316 0.36008 0.25077 0.02659  -0.04351 -0.05228 158 GLU A C   
1101 O O   . GLU A 151 ? 0.32787 0.35738 0.26033 0.02377  -0.03225 -0.04305 158 GLU A O   
1102 C CB  . GLU A 151 ? 0.40022 0.41964 0.26371 0.04632  -0.04603 -0.06506 158 GLU A CB  
1103 C CG  . GLU A 151 ? 0.58353 0.60616 0.41282 0.05996  -0.04889 -0.06703 158 GLU A CG  
1104 C CD  . GLU A 151 ? 0.88365 0.90766 0.70457 0.05839  -0.06922 -0.07497 158 GLU A CD  
1105 O OE1 . GLU A 151 ? 0.96069 0.99765 0.77431 0.06343  -0.07139 -0.06561 158 GLU A OE1 
1106 O OE2 . GLU A 151 ? 1.11405 1.12615 0.93638 0.05184  -0.08371 -0.09000 158 GLU A OE2 
1107 N N   . GLN A 152 ? 0.31138 0.33138 0.23640 0.01939  -0.05555 -0.06271 159 GLN A N   
1108 C CA  . GLN A 152 ? 0.34290 0.35919 0.29323 0.00912  -0.05381 -0.06206 159 GLN A CA  
1109 C C   . GLN A 152 ? 0.30070 0.30343 0.24581 0.01138  -0.04623 -0.06755 159 GLN A C   
1110 O O   . GLN A 152 ? 0.37004 0.36044 0.29548 0.01708  -0.05043 -0.07839 159 GLN A O   
1111 C CB  . GLN A 152 ? 0.35025 0.36618 0.31423 -0.00099 -0.06929 -0.06791 159 GLN A CB  
1112 C CG  . GLN A 152 ? 0.31400 0.32965 0.30543 -0.01132 -0.06628 -0.06361 159 GLN A CG  
1113 C CD  . GLN A 152 ? 0.40029 0.42458 0.41224 -0.02236 -0.07950 -0.06340 159 GLN A CD  
1114 O OE1 . GLN A 152 ? 0.39963 0.44191 0.41834 -0.02204 -0.08518 -0.05816 159 GLN A OE1 
1115 N NE2 . GLN A 152 ? 0.37112 0.38380 0.39488 -0.03218 -0.08426 -0.06763 159 GLN A NE2 
1116 N N   . TYR A 153 ? 0.25760 0.26236 0.21887 0.00831  -0.03566 -0.06053 160 TYR A N   
1117 C CA  . TYR A 153 ? 0.29455 0.29120 0.25318 0.01187  -0.02771 -0.06325 160 TYR A CA  
1118 C C   . TYR A 153 ? 0.33528 0.32697 0.31401 0.00386  -0.02742 -0.06190 160 TYR A C   
1119 O O   . TYR A 153 ? 0.27236 0.27092 0.26835 -0.00355 -0.02865 -0.05580 160 TYR A O   
1120 C CB  . TYR A 153 ? 0.27978 0.28684 0.23647 0.01743  -0.01423 -0.05467 160 TYR A CB  
1121 C CG  . TYR A 153 ? 0.32353 0.33610 0.25912 0.02691  -0.01121 -0.05346 160 TYR A CG  
1122 C CD1 . TYR A 153 ? 0.33751 0.34581 0.25314 0.03773  -0.00838 -0.06020 160 TYR A CD1 
1123 C CD2 . TYR A 153 ? 0.41214 0.43389 0.34625 0.02687  -0.01011 -0.04456 160 TYR A CD2 
1124 C CE1 . TYR A 153 ? 0.41146 0.42671 0.30539 0.04815  -0.00411 -0.05782 160 TYR A CE1 
1125 C CE2 . TYR A 153 ? 0.36767 0.39498 0.28113 0.03628  -0.00638 -0.04116 160 TYR A CE2 
1126 C CZ  . TYR A 153 ? 0.39980 0.42503 0.29299 0.04680  -0.00307 -0.04759 160 TYR A CZ  
1127 O OH  . TYR A 153 ? 0.58599 0.61863 0.45646 0.05779  0.00211  -0.04297 160 TYR A OH  
1128 N N   . ALA A 154 ? 0.28169 0.26191 0.25658 0.00738  -0.02484 -0.06678 161 ALA A N   
1129 C CA  . ALA A 154 ? 0.30487 0.28031 0.29538 0.00262  -0.02237 -0.06372 161 ALA A CA  
1130 C C   . ALA A 154 ? 0.27900 0.26034 0.26894 0.00971  -0.01148 -0.06003 161 ALA A C   
1131 O O   . ALA A 154 ? 0.30138 0.27874 0.27784 0.01949  -0.00832 -0.06474 161 ALA A O   
1132 C CB  . ALA A 154 ? 0.28720 0.24159 0.27578 0.00002  -0.03080 -0.07166 161 ALA A CB  
1133 N N   . TRP A 155 ? 0.23305 0.22525 0.23720 0.00553  -0.00618 -0.05182 162 TRP A N   
1134 C CA  . TRP A 155 ? 0.24392 0.24416 0.25242 0.00942  0.00155  -0.04777 162 TRP A CA  
1135 C C   . TRP A 155 ? 0.24349 0.23645 0.26047 0.00790  0.00058  -0.04659 162 TRP A C   
1136 O O   . TRP A 155 ? 0.27190 0.26024 0.29659 0.00106  -0.00313 -0.04453 162 TRP A O   
1137 C CB  . TRP A 155 ? 0.22797 0.24228 0.24409 0.00515  0.00589  -0.04061 162 TRP A CB  
1138 C CG  . TRP A 155 ? 0.21644 0.24173 0.24042 0.00572  0.01129  -0.03620 162 TRP A CG  
1139 C CD1 . TRP A 155 ? 0.20608 0.24432 0.23100 0.00768  0.01681  -0.03253 162 TRP A CD1 
1140 C CD2 . TRP A 155 ? 0.25620 0.28289 0.28919 0.00342  0.01082  -0.03410 162 TRP A CD2 
1141 N NE1 . TRP A 155 ? 0.22749 0.27567 0.26355 0.00553  0.01828  -0.02915 162 TRP A NE1 
1142 C CE2 . TRP A 155 ? 0.22436 0.26498 0.26344 0.00375  0.01426  -0.03072 162 TRP A CE2 
1143 C CE3 . TRP A 155 ? 0.23943 0.25851 0.27590 0.00130  0.00790  -0.03377 162 TRP A CE3 
1144 C CZ2 . TRP A 155 ? 0.24153 0.28786 0.28799 0.00248  0.01299  -0.02883 162 TRP A CZ2 
1145 C CZ3 . TRP A 155 ? 0.23613 0.26023 0.27774 0.00154  0.00857  -0.03084 162 TRP A CZ3 
1146 C CH2 . TRP A 155 ? 0.18186 0.21903 0.22737 0.00233  0.01017  -0.02929 162 TRP A CH2 
1147 N N   . GLU A 156 ? 0.26102 0.25460 0.27697 0.01524  0.00442  -0.04648 163 GLU A N   
1148 C CA  . GLU A 156 ? 0.23471 0.21989 0.25623 0.01579  0.00360  -0.04412 163 GLU A CA  
1149 C C   . GLU A 156 ? 0.26438 0.26178 0.28916 0.02338  0.00865  -0.04047 163 GLU A C   
1150 O O   . GLU A 156 ? 0.27079 0.27610 0.29116 0.03165  0.01248  -0.04220 163 GLU A O   
1151 C CB  . GLU A 156 ? 0.33943 0.30076 0.35326 0.01840  -0.00124 -0.05004 163 GLU A CB  
1152 C CG  . GLU A 156 ? 0.35715 0.30616 0.37798 0.01625  -0.00246 -0.04502 163 GLU A CG  
1153 C CD  . GLU A 156 ? 0.56367 0.48500 0.57968 0.01392  -0.00919 -0.05025 163 GLU A CD  
1154 O OE1 . GLU A 156 ? 0.52313 0.42787 0.52621 0.02381  -0.01000 -0.05744 163 GLU A OE1 
1155 O OE2 . GLU A 156 ? 0.47985 0.39598 0.50538 0.00230  -0.01383 -0.04717 163 GLU A OE2 
1156 N N   . SER A 157 ? 0.25307 0.25432 0.28556 0.02143  0.00865  -0.03479 164 SER A N   
1157 C CA  . SER A 157 ? 0.20608 0.22055 0.24263 0.02865  0.01116  -0.03105 164 SER A CA  
1158 C C   . SER A 157 ? 0.25190 0.26063 0.29069 0.02956  0.00967  -0.02561 164 SER A C   
1159 O O   . SER A 157 ? 0.26104 0.26708 0.30177 0.02223  0.00837  -0.02269 164 SER A O   
1160 C CB  . SER A 157 ? 0.20978 0.24704 0.25391 0.02421  0.01242  -0.02870 164 SER A CB  
1161 O OG  . SER A 157 ? 0.24579 0.29922 0.29654 0.03000  0.01281  -0.02494 164 SER A OG  
1162 N N   . SER A 158 ? 0.25978 0.26744 0.29741 0.04036  0.01070  -0.02324 165 SER A N   
1163 C CA  . SER A 158 ? 0.26962 0.27686 0.30838 0.04413  0.00986  -0.01593 165 SER A CA  
1164 C C   . SER A 158 ? 0.30612 0.33966 0.35070 0.04846  0.00903  -0.01274 165 SER A C   
1165 O O   . SER A 158 ? 0.31293 0.35000 0.35711 0.05734  0.00817  -0.00703 165 SER A O   
1166 C CB  . SER A 158 ? 0.34720 0.33221 0.38021 0.05404  0.01051  -0.01410 165 SER A CB  
1167 O OG  . SER A 158 ? 0.32432 0.28375 0.35399 0.04689  0.00893  -0.01651 165 SER A OG  
1168 N N   . ALA A 159 ? 0.25868 0.31054 0.30925 0.04188  0.00846  -0.01576 166 ALA A N   
1169 C CA  . ALA A 159 ? 0.26930 0.34833 0.32921 0.04280  0.00604  -0.01366 166 ALA A CA  
1170 C C   . ALA A 159 ? 0.32125 0.41176 0.38588 0.05637  0.00900  -0.01140 166 ALA A C   
1171 O O   . ALA A 159 ? 0.33918 0.41906 0.39912 0.06274  0.01390  -0.01434 166 ALA A O   
1172 C CB  . ALA A 159 ? 0.32938 0.41356 0.38722 0.04126  0.00067  -0.01042 166 ALA A CB  
1173 N N   . GLY A 160 ? 0.24305 0.35604 0.31596 0.06228  0.00571  -0.00653 167 GLY A N   
1174 C CA  . GLY A 160 ? 0.31319 0.44233 0.39301 0.07710  0.00907  -0.00308 167 GLY A CA  
1175 C C   . GLY A 160 ? 0.24609 0.39788 0.33773 0.07585  0.01392  -0.00365 167 GLY A C   
1176 O O   . GLY A 160 ? 0.28310 0.44718 0.37872 0.09053  0.01947  -0.00106 167 GLY A O   
1177 N N   . GLY A 161 ? 0.22712 0.38415 0.32376 0.06002  0.01300  -0.00596 168 GLY A N   
1178 C CA  . GLY A 161 ? 0.24340 0.42478 0.35349 0.05666  0.01790  -0.00346 168 GLY A CA  
1179 C C   . GLY A 161 ? 0.23585 0.40276 0.33519 0.05836  0.02616  -0.00695 168 GLY A C   
1180 O O   . GLY A 161 ? 0.18539 0.37284 0.29433 0.05629  0.03194  -0.00309 168 GLY A O   
1181 N N   . SER A 162 ? 0.21200 0.34566 0.29217 0.06150  0.02646  -0.01339 169 SER A N   
1182 C CA  . SER A 162 ? 0.21339 0.33325 0.28052 0.06481  0.03230  -0.01803 169 SER A CA  
1183 C C   . SER A 162 ? 0.22606 0.31601 0.28020 0.05502  0.02778  -0.02417 169 SER A C   
1184 O O   . SER A 162 ? 0.20446 0.28012 0.25711 0.05034  0.02222  -0.02483 169 SER A O   
1185 C CB  . SER A 162 ? 0.24303 0.35476 0.29877 0.08505  0.03775  -0.02084 169 SER A CB  
1186 O OG  . SER A 162 ? 0.27709 0.35636 0.31977 0.08917  0.03313  -0.02588 169 SER A OG  
1187 N N   . PHE A 163 ? 0.20263 0.28613 0.24781 0.05276  0.03062  -0.02743 170 PHE A N   
1188 C CA  . PHE A 163 ? 0.20863 0.26712 0.24212 0.04557  0.02616  -0.03321 170 PHE A CA  
1189 C C   . PHE A 163 ? 0.25021 0.29772 0.26671 0.05395  0.02893  -0.03936 170 PHE A C   
1190 O O   . PHE A 163 ? 0.24460 0.30653 0.25813 0.06422  0.03609  -0.03791 170 PHE A O   
1191 C CB  . PHE A 163 ? 0.19244 0.25570 0.23262 0.03067  0.02375  -0.03040 170 PHE A CB  
1192 C CG  . PHE A 163 ? 0.19329 0.27343 0.23693 0.02777  0.02898  -0.02604 170 PHE A CG  
1193 C CD1 . PHE A 163 ? 0.20496 0.30924 0.26484 0.02390  0.03152  -0.01890 170 PHE A CD1 
1194 C CD2 . PHE A 163 ? 0.19950 0.27192 0.23106 0.02784  0.03062  -0.02798 170 PHE A CD2 
1195 C CE1 . PHE A 163 ? 0.22472 0.34402 0.29021 0.01939  0.03696  -0.01248 170 PHE A CE1 
1196 C CE2 . PHE A 163 ? 0.22080 0.30811 0.25482 0.02552  0.03650  -0.02148 170 PHE A CE2 
1197 C CZ  . PHE A 163 ? 0.21324 0.32334 0.26507 0.02070  0.04028  -0.01307 170 PHE A CZ  
1198 N N   . THR A 164 ? 0.25942 0.28277 0.26456 0.05001  0.02295  -0.04611 171 THR A N   
1199 C CA  . THR A 164 ? 0.25462 0.26440 0.24033 0.05698  0.02236  -0.05417 171 THR A CA  
1200 C C   . THR A 164 ? 0.24693 0.25387 0.22931 0.04617  0.01780  -0.05513 171 THR A C   
1201 O O   . THR A 164 ? 0.23794 0.24392 0.23128 0.03415  0.01346  -0.05197 171 THR A O   
1202 C CB  . THR A 164 ? 0.31364 0.29358 0.28674 0.06347  0.01662  -0.06336 171 THR A CB  
1203 O OG1 . THR A 164 ? 0.30214 0.26682 0.28255 0.05017  0.00838  -0.06345 171 THR A OG1 
1204 C CG2 . THR A 164 ? 0.32921 0.30941 0.30459 0.07657  0.02118  -0.06152 171 THR A CG2 
1205 N N   . VAL A 165 ? 0.28145 0.28819 0.24720 0.05253  0.01924  -0.05904 172 VAL A N   
1206 C CA  . VAL A 165 ? 0.27695 0.27999 0.23556 0.04558  0.01375  -0.06062 172 VAL A CA  
1207 C C   . VAL A 165 ? 0.30898 0.29395 0.24275 0.05455  0.00807  -0.07258 172 VAL A C   
1208 O O   . VAL A 165 ? 0.30577 0.29004 0.22356 0.06928  0.01364  -0.07675 172 VAL A O   
1209 C CB  . VAL A 165 ? 0.29873 0.32303 0.26059 0.04355  0.02103  -0.05079 172 VAL A CB  
1210 C CG1 . VAL A 165 ? 0.28357 0.30326 0.23516 0.03959  0.01512  -0.05193 172 VAL A CG1 
1211 C CG2 . VAL A 165 ? 0.22999 0.26713 0.21472 0.03313  0.02391  -0.04132 172 VAL A CG2 
1212 N N   . ARG A 166 ? 0.29618 0.26722 0.22658 0.04625  -0.00352 -0.07843 173 ARG A N   
1213 C CA  . ARG A 166 ? 0.38458 0.33721 0.29088 0.05213  -0.01266 -0.09139 173 ARG A CA  
1214 C C   . ARG A 166 ? 0.34681 0.30270 0.25326 0.04244  -0.02253 -0.09138 173 ARG A C   
1215 O O   . ARG A 166 ? 0.31661 0.28184 0.24423 0.03038  -0.02397 -0.08323 173 ARG A O   
1216 C CB  . ARG A 166 ? 0.37930 0.30333 0.28280 0.05158  -0.02124 -0.10193 173 ARG A CB  
1217 C CG  . ARG A 166 ? 0.45604 0.37444 0.38303 0.03435  -0.02913 -0.09809 173 ARG A CG  
1218 C CD  . ARG A 166 ? 0.55965 0.44732 0.48455 0.03220  -0.03769 -0.10665 173 ARG A CD  
1219 N NE  . ARG A 166 ? 0.88518 0.76456 0.80855 0.04332  -0.02905 -0.10544 173 ARG A NE  
1220 C CZ  . ARG A 166 ? 0.76046 0.64865 0.70370 0.04003  -0.02238 -0.09443 173 ARG A CZ  
1221 N NH1 . ARG A 166 ? 0.73864 0.64316 0.70307 0.02673  -0.02211 -0.08426 173 ARG A NH1 
1222 N NH2 . ARG A 166 ? 0.76465 0.64543 0.70477 0.05207  -0.01595 -0.09370 173 ARG A NH2 
1223 N N   . THR A 167 ? 0.38890 0.33791 0.27015 0.04952  -0.02943 -0.10064 174 THR A N   
1224 C CA  . THR A 167 ? 0.46522 0.41537 0.34562 0.04099  -0.04267 -0.10291 174 THR A CA  
1225 C C   . THR A 167 ? 0.49165 0.42516 0.38704 0.02740  -0.05641 -0.10931 174 THR A C   
1226 O O   . THR A 167 ? 0.56432 0.47388 0.45170 0.02919  -0.06144 -0.11997 174 THR A O   
1227 C CB  . THR A 167 ? 0.56286 0.50834 0.40920 0.05294  -0.04869 -0.11286 174 THR A CB  
1228 O OG1 . THR A 167 ? 0.50299 0.46713 0.33771 0.06492  -0.03401 -0.10322 174 THR A OG1 
1229 C CG2 . THR A 167 ? 0.65882 0.60748 0.50492 0.04429  -0.06496 -0.11561 174 THR A CG2 
1230 N N   . ASP A 168 ? 0.44203 0.38801 0.36000 0.01427  -0.06175 -0.10172 175 ASP A N   
1231 C CA  . ASP A 168 ? 0.40940 0.34616 0.34864 -0.00027 -0.07176 -0.10294 175 ASP A CA  
1232 C C   . ASP A 168 ? 0.67541 0.60417 0.60745 -0.00678 -0.09124 -0.11378 175 ASP A C   
1233 O O   . ASP A 168 ? 0.64520 0.59053 0.57365 -0.00650 -0.09729 -0.11209 175 ASP A O   
1234 C CB  . ASP A 168 ? 0.34027 0.29739 0.30910 -0.00972 -0.06610 -0.08821 175 ASP A CB  
1235 C CG  . ASP A 168 ? 0.53435 0.48619 0.52714 -0.02414 -0.07370 -0.08628 175 ASP A CG  
1236 O OD1 . ASP A 168 ? 0.57736 0.50621 0.56769 -0.02675 -0.07769 -0.09305 175 ASP A OD1 
1237 O OD2 . ASP A 168 ? 0.49887 0.46944 0.51306 -0.03216 -0.07505 -0.07704 175 ASP A OD2 
1238 N N   . THR A 169 ? 0.65728 0.55993 0.58776 -0.01299 -0.10198 -0.12455 176 THR A N   
1239 C CA  . THR A 169 ? 0.88054 0.77144 0.80530 -0.02182 -0.12339 -0.13692 176 THR A CA  
1240 C C   . THR A 169 ? 0.87589 0.77803 0.83695 -0.04244 -0.13334 -0.12904 176 THR A C   
1241 O O   . THR A 169 ? 0.77426 0.67474 0.73732 -0.05260 -0.15269 -0.13692 176 THR A O   
1242 C CB  . THR A 169 ? 0.96866 0.81982 0.87004 -0.01779 -0.13136 -0.15440 176 THR A CB  
1243 O OG1 . THR A 169 ? 1.04691 0.88222 0.96469 -0.02182 -0.12287 -0.14884 176 THR A OG1 
1244 C CG2 . THR A 169 ? 0.88765 0.73123 0.74951 0.00479  -0.12368 -0.16378 176 THR A CG2 
1245 N N   . GLY A 170 ? 0.77120 0.68668 0.76077 -0.04845 -0.12096 -0.11351 177 GLY A N   
1246 C CA  . GLY A 170 ? 0.73825 0.66619 0.76335 -0.06655 -0.12729 -0.10384 177 GLY A CA  
1247 C C   . GLY A 170 ? 0.70792 0.66938 0.74913 -0.07150 -0.13435 -0.09690 177 GLY A C   
1248 O O   . GLY A 170 ? 0.62368 0.59378 0.64516 -0.06261 -0.13962 -0.10254 177 GLY A O   
1249 N N   . GLU A 171 ? 0.61539 0.59708 0.69226 -0.08432 -0.13389 -0.08348 178 GLU A N   
1250 C CA  . GLU A 171 ? 0.57141 0.58868 0.66856 -0.08789 -0.13934 -0.07455 178 GLU A CA  
1251 C C   . GLU A 171 ? 0.49073 0.52478 0.57245 -0.07066 -0.12748 -0.06958 178 GLU A C   
1252 O O   . GLU A 171 ? 0.47536 0.50803 0.55392 -0.06213 -0.10955 -0.06262 178 GLU A O   
1253 C CB  . GLU A 171 ? 0.66058 0.69917 0.79778 -0.09971 -0.13342 -0.05765 178 GLU A CB  
1254 C CG  . GLU A 171 ? 0.72091 0.79840 0.88623 -0.10573 -0.14159 -0.04784 178 GLU A CG  
1255 C CD  . GLU A 171 ? 0.84834 0.92773 1.02818 -0.12292 -0.16201 -0.05325 178 GLU A CD  
1256 O OE1 . GLU A 171 ? 0.74847 0.80646 0.93331 -0.13437 -0.16168 -0.05463 178 GLU A OE1 
1257 O OE2 . GLU A 171 ? 0.62930 0.73158 0.81108 -0.12221 -0.17340 -0.05459 178 GLU A OE2 
1258 N N   . PRO A 172 ? 0.44626 0.49512 0.51788 -0.06549 -0.13762 -0.07254 179 PRO A N   
1259 C CA  . PRO A 172 ? 0.55498 0.61749 0.61295 -0.04967 -0.12614 -0.06561 179 PRO A CA  
1260 C C   . PRO A 172 ? 0.47326 0.56072 0.55810 -0.04862 -0.11436 -0.04880 179 PRO A C   
1261 O O   . PRO A 172 ? 0.48871 0.59719 0.60348 -0.05803 -0.12017 -0.04136 179 PRO A O   
1262 C CB  . PRO A 172 ? 0.50529 0.57800 0.54773 -0.04555 -0.14267 -0.07189 179 PRO A CB  
1263 C CG  . PRO A 172 ? 0.47763 0.53251 0.51413 -0.05686 -0.16229 -0.08764 179 PRO A CG  
1264 C CD  . PRO A 172 ? 0.50711 0.55592 0.57401 -0.07301 -0.16113 -0.08397 179 PRO A CD  
1265 N N   . MET A 173 ? 0.35820 0.44325 0.43186 -0.03665 -0.09771 -0.04283 180 MET A N   
1266 C CA  . MET A 173 ? 0.35885 0.45962 0.45076 -0.03278 -0.08467 -0.02931 180 MET A CA  
1267 C C   . MET A 173 ? 0.39242 0.51512 0.48708 -0.02342 -0.08611 -0.02101 180 MET A C   
1268 O O   . MET A 173 ? 0.45851 0.59845 0.57265 -0.02041 -0.07902 -0.01009 180 MET A O   
1269 C CB  . MET A 173 ? 0.31212 0.39634 0.39030 -0.02550 -0.06781 -0.02810 180 MET A CB  
1270 C CG  . MET A 173 ? 0.64938 0.71176 0.72066 -0.03054 -0.06487 -0.03557 180 MET A CG  
1271 S SD  . MET A 173 ? 0.62608 0.68030 0.69492 -0.02494 -0.04648 -0.03019 180 MET A SD  
1272 C CE  . MET A 173 ? 0.43609 0.51118 0.52281 -0.02091 -0.04006 -0.01772 180 MET A CE  
1273 N N   . GLY A 174 ? 0.30968 0.43179 0.38356 -0.01679 -0.09435 -0.02530 181 GLY A N   
1274 C CA  . GLY A 174 ? 0.25823 0.39587 0.32905 -0.00460 -0.09306 -0.01603 181 GLY A CA  
1275 C C   . GLY A 174 ? 0.23729 0.35881 0.28989 0.00627  -0.07664 -0.01144 181 GLY A C   
1276 O O   . GLY A 174 ? 0.31290 0.42597 0.34103 0.01411  -0.07624 -0.01227 181 GLY A O   
1277 N N   . ARG A 175 ? 0.24293 0.35995 0.30687 0.00634  -0.06334 -0.00634 182 ARG A N   
1278 C CA  . ARG A 175 ? 0.20494 0.30510 0.25495 0.01375  -0.04922 -0.00274 182 ARG A CA  
1279 C C   . ARG A 175 ? 0.22017 0.31571 0.28350 0.01074  -0.03871 -0.00109 182 ARG A C   
1280 O O   . ARG A 175 ? 0.21570 0.32685 0.29936 0.00975  -0.03885 0.00348  182 ARG A O   
1281 C CB  . ARG A 175 ? 0.26181 0.36652 0.30574 0.02647  -0.04673 0.00713  182 ARG A CB  
1282 C CG  . ARG A 175 ? 0.22819 0.31151 0.25665 0.03208  -0.03410 0.01095  182 ARG A CG  
1283 C CD  . ARG A 175 ? 0.22604 0.30909 0.25472 0.04433  -0.02943 0.02165  182 ARG A CD  
1284 N NE  . ARG A 175 ? 0.21504 0.30949 0.26335 0.04748  -0.02698 0.02460  182 ARG A NE  
1285 C CZ  . ARG A 175 ? 0.21758 0.33540 0.27983 0.05450  -0.03271 0.03079  182 ARG A CZ  
1286 N NH1 . ARG A 175 ? 0.22886 0.36078 0.28731 0.05861  -0.04321 0.03400  182 ARG A NH1 
1287 N NH2 . ARG A 175 ? 0.21032 0.33997 0.29054 0.05851  -0.02776 0.03441  182 ARG A NH2 
1288 N N   . GLY A 176 ? 0.23067 0.30730 0.28270 0.00980  -0.02971 -0.00412 183 GLY A N   
1289 C CA  . GLY A 176 ? 0.24234 0.31340 0.30203 0.00887  -0.02042 -0.00291 183 GLY A CA  
1290 C C   . GLY A 176 ? 0.28890 0.34812 0.34480 0.00151  -0.01793 -0.00971 183 GLY A C   
1291 O O   . GLY A 176 ? 0.25198 0.30358 0.29599 -0.00057 -0.02035 -0.01498 183 GLY A O   
1292 N N   . THR A 177 ? 0.23782 0.29653 0.30274 -0.00052 -0.01249 -0.00891 184 THR A N   
1293 C CA  . THR A 177 ? 0.26740 0.31579 0.32919 -0.00549 -0.00950 -0.01368 184 THR A CA  
1294 C C   . THR A 177 ? 0.29826 0.35340 0.37470 -0.00978 -0.00877 -0.01139 184 THR A C   
1295 O O   . THR A 177 ? 0.20707 0.27291 0.29353 -0.00647 -0.00501 -0.00519 184 THR A O   
1296 C CB  . THR A 177 ? 0.25252 0.28942 0.30470 -0.00237 -0.00197 -0.01404 184 THR A CB  
1297 O OG1 . THR A 177 ? 0.27774 0.30833 0.31845 -0.00031 -0.00183 -0.01400 184 THR A OG1 
1298 C CG2 . THR A 177 ? 0.24066 0.27145 0.29168 -0.00638 0.00027  -0.01793 184 THR A CG2 
1299 N N   . LYS A 178 ? 0.22044 0.26889 0.29740 -0.01599 -0.01152 -0.01546 185 LYS A N   
1300 C CA  . LYS A 178 ? 0.20397 0.25489 0.29361 -0.02105 -0.01029 -0.01191 185 LYS A CA  
1301 C C   . LYS A 178 ? 0.26616 0.30401 0.34684 -0.02034 -0.00575 -0.01479 185 LYS A C   
1302 O O   . LYS A 178 ? 0.23084 0.25769 0.30264 -0.02126 -0.00884 -0.02115 185 LYS A O   
1303 C CB  . LYS A 178 ? 0.29661 0.34932 0.39708 -0.03002 -0.02015 -0.01326 185 LYS A CB  
1304 C CG  . LYS A 178 ? 0.38773 0.44196 0.50418 -0.03734 -0.01911 -0.00718 185 LYS A CG  
1305 C CD  . LYS A 178 ? 0.46452 0.51297 0.58956 -0.04844 -0.03107 -0.01085 185 LYS A CD  
1306 C CE  . LYS A 178 ? 0.56097 0.62222 0.69005 -0.05025 -0.04136 -0.01350 185 LYS A CE  
1307 N NZ  . LYS A 178 ? 0.80402 0.85303 0.93196 -0.05964 -0.05588 -0.02246 185 LYS A NZ  
1308 N N   . VAL A 179 ? 0.21563 0.25589 0.29730 -0.01701 0.00149  -0.01013 186 VAL A N   
1309 C CA  . VAL A 179 ? 0.21086 0.24230 0.28497 -0.01544 0.00490  -0.01159 186 VAL A CA  
1310 C C   . VAL A 179 ? 0.24761 0.27927 0.33148 -0.01905 0.00616  -0.00522 186 VAL A C   
1311 O O   . VAL A 179 ? 0.24004 0.28246 0.33263 -0.01829 0.01082  0.00302  186 VAL A O   
1312 C CB  . VAL A 179 ? 0.20395 0.23598 0.26892 -0.00904 0.01037  -0.01166 186 VAL A CB  
1313 C CG1 . VAL A 179 ? 0.18277 0.20928 0.24098 -0.00754 0.01179  -0.01302 186 VAL A CG1 
1314 C CG2 . VAL A 179 ? 0.26326 0.29203 0.32050 -0.00728 0.00912  -0.01619 186 VAL A CG2 
1315 N N   . ILE A 180 ? 0.18441 0.20381 0.26650 -0.02198 0.00285  -0.00798 187 ILE A N   
1316 C CA  . ILE A 180 ? 0.18243 0.19657 0.27322 -0.02622 0.00349  -0.00114 187 ILE A CA  
1317 C C   . ILE A 180 ? 0.25825 0.26659 0.33920 -0.01960 0.00837  0.00067  187 ILE A C   
1318 O O   . ILE A 180 ? 0.23646 0.23544 0.30776 -0.01592 0.00637  -0.00581 187 ILE A O   
1319 C CB  . ILE A 180 ? 0.24957 0.24910 0.34406 -0.03357 -0.00502 -0.00583 187 ILE A CB  
1320 C CG1 . ILE A 180 ? 0.21508 0.22233 0.31646 -0.03928 -0.01236 -0.00954 187 ILE A CG1 
1321 C CG2 . ILE A 180 ? 0.25841 0.24970 0.36450 -0.04000 -0.00456 0.00317  187 ILE A CG2 
1322 C CD1 . ILE A 180 ? 0.29920 0.28970 0.39753 -0.04503 -0.02318 -0.01848 187 ILE A CD1 
1323 N N   . LEU A 181 ? 0.22406 0.24031 0.30708 -0.01678 0.01492  0.01012  188 LEU A N   
1324 C CA  . LEU A 181 ? 0.22223 0.23566 0.29477 -0.00952 0.01872  0.01306  188 LEU A CA  
1325 C C   . LEU A 181 ? 0.27437 0.27689 0.35282 -0.01216 0.01964  0.02204  188 LEU A C   
1326 O O   . LEU A 181 ? 0.22865 0.23634 0.31801 -0.01617 0.02393  0.03359  188 LEU A O   
1327 C CB  . LEU A 181 ? 0.17342 0.19996 0.23950 -0.00276 0.02511  0.01759  188 LEU A CB  
1328 C CG  . LEU A 181 ? 0.20469 0.23700 0.26442 -0.00014 0.02413  0.00924  188 LEU A CG  
1329 C CD1 . LEU A 181 ? 0.25322 0.29352 0.30269 0.00837  0.02998  0.01223  188 LEU A CD1 
1330 C CD2 . LEU A 181 ? 0.18967 0.21545 0.24087 0.00040  0.01885  -0.00096 188 LEU A CD2 
1331 N N   . HIS A 182 ? 0.24600 0.23349 0.31809 -0.00944 0.01623  0.01790  189 HIS A N   
1332 C CA  . HIS A 182 ? 0.26159 0.23372 0.33590 -0.00949 0.01726  0.02668  189 HIS A CA  
1333 C C   . HIS A 182 ? 0.30247 0.28222 0.36712 0.00047  0.02322  0.03535  189 HIS A C   
1334 O O   . HIS A 182 ? 0.27820 0.25901 0.33154 0.00936  0.02168  0.03051  189 HIS A O   
1335 C CB  . HIS A 182 ? 0.27349 0.22482 0.34251 -0.00754 0.01140  0.01800  189 HIS A CB  
1336 C CG  . HIS A 182 ? 0.30872 0.25299 0.38128 -0.01501 0.00447  0.00715  189 HIS A CG  
1337 N ND1 . HIS A 182 ? 0.37780 0.30429 0.45902 -0.02489 -0.00108 0.00744  189 HIS A ND1 
1338 C CD2 . HIS A 182 ? 0.31973 0.27203 0.38726 -0.01405 0.00151  -0.00394 189 HIS A CD2 
1339 C CE1 . HIS A 182 ? 0.37689 0.30175 0.45642 -0.02877 -0.00805 -0.00429 189 HIS A CE1 
1340 N NE2 . HIS A 182 ? 0.35617 0.29685 0.42700 -0.02162 -0.00571 -0.01045 189 HIS A NE2 
1341 N N   . LEU A 183 ? 0.27030 0.25797 0.33956 -0.00051 0.02996  0.04888  190 LEU A N   
1342 C CA  . LEU A 183 ? 0.25550 0.25490 0.31151 0.01030  0.03571  0.05594  190 LEU A CA  
1343 C C   . LEU A 183 ? 0.34035 0.32818 0.38773 0.01828  0.03584  0.06296  190 LEU A C   
1344 O O   . LEU A 183 ? 0.35552 0.32473 0.41030 0.01443  0.03556  0.06987  190 LEU A O   
1345 C CB  . LEU A 183 ? 0.23546 0.24863 0.29730 0.00918  0.04480  0.06979  190 LEU A CB  
1346 C CG  . LEU A 183 ? 0.22088 0.25007 0.28884 0.00615  0.04640  0.06485  190 LEU A CG  
1347 C CD1 . LEU A 183 ? 0.27631 0.32204 0.35051 0.00797  0.05745  0.08109  190 LEU A CD1 
1348 C CD2 . LEU A 183 ? 0.27870 0.31348 0.32952 0.01415  0.04309  0.05065  190 LEU A CD2 
1349 N N   . LYS A 184 ? 0.34806 0.27872 0.32409 0.07157  0.01647  0.02523  191 LYS A N   
1350 C CA  . LYS A 184 ? 0.36513 0.28729 0.35637 0.09079  0.01635  0.04205  191 LYS A CA  
1351 C C   . LYS A 184 ? 0.42951 0.31313 0.40712 0.08386  0.01425  0.05297  191 LYS A C   
1352 O O   . LYS A 184 ? 0.43340 0.31463 0.39885 0.06214  0.01035  0.05096  191 LYS A O   
1353 C CB  . LYS A 184 ? 0.38353 0.35606 0.39908 0.09837  0.00440  0.05679  191 LYS A CB  
1354 C CG  . LYS A 184 ? 0.40169 0.41495 0.44675 0.10458  0.01155  0.05074  191 LYS A CG  
1355 C CD  . LYS A 184 ? 0.38764 0.45318 0.46596 0.10407  -0.00533 0.05967  191 LYS A CD  
1356 C CE  . LYS A 184 ? 0.63581 0.74518 0.76123 0.10934  0.00542  0.05631  191 LYS A CE  
1357 N NZ  . LYS A 184 ? 0.50427 0.65615 0.65783 0.09034  -0.00724 0.05378  191 LYS A NZ  
1358 N N   . GLU A 185 ? 0.43394 0.28715 0.41649 0.10457  0.01994  0.06733  192 GLU A N   
1359 C CA  . GLU A 185 ? 0.49672 0.30170 0.46718 0.10023  0.02594  0.08267  192 GLU A CA  
1360 C C   . GLU A 185 ? 0.57622 0.40178 0.53078 0.08948  0.01686  0.10196  192 GLU A C   
1361 O O   . GLU A 185 ? 0.54401 0.34264 0.48875 0.07065  0.02554  0.10619  192 GLU A O   
1362 C CB  . GLU A 185 ? 0.56735 0.33759 0.54442 0.13168  0.03366  0.10186  192 GLU A CB  
1363 C CG  . GLU A 185 ? 0.83884 0.55040 0.80300 0.13091  0.04554  0.12552  192 GLU A CG  
1364 C CD  . GLU A 185 ? 1.13032 0.78368 1.10373 0.15805  0.06040  0.13452  192 GLU A CD  
1365 O OE1 . GLU A 185 ? 1.21968 0.80577 1.19240 0.14780  0.07840  0.13874  192 GLU A OE1 
1366 O OE2 . GLU A 185 ? 1.22509 0.89946 1.21225 0.18946  0.05583  0.13664  192 GLU A OE2 
1367 N N   . ASP A 186 ? 0.47260 0.34727 0.42697 0.10089  0.00032  0.11138  193 ASP A N   
1368 C CA  . ASP A 186 ? 0.53440 0.42763 0.46516 0.09660  -0.00964 0.12673  193 ASP A CA  
1369 C C   . ASP A 186 ? 0.47075 0.39814 0.40001 0.07174  -0.01645 0.10798  193 ASP A C   
1370 O O   . ASP A 186 ? 0.44010 0.39088 0.35074 0.07043  -0.02696 0.11394  193 ASP A O   
1371 C CB  . ASP A 186 ? 0.55431 0.48105 0.48284 0.12506  -0.02919 0.14366  193 ASP A CB  
1372 C CG  . ASP A 186 ? 0.69080 0.67229 0.65604 0.12856  -0.04406 0.12570  193 ASP A CG  
1373 O OD1 . ASP A 186 ? 0.64214 0.62334 0.63030 0.11828  -0.03264 0.10719  193 ASP A OD1 
1374 O OD2 . ASP A 186 ? 0.62684 0.65273 0.59849 0.14162  -0.06671 0.12962  193 ASP A OD2 
1375 N N   . GLN A 187 ? 0.36003 0.28841 0.30390 0.05533  -0.01088 0.08533  194 GLN A N   
1376 C CA  . GLN A 187 ? 0.34235 0.29869 0.28573 0.03628  -0.01626 0.07019  194 GLN A CA  
1377 C C   . GLN A 187 ? 0.42206 0.35793 0.36249 0.01594  -0.00680 0.05882  194 GLN A C   
1378 O O   . GLN A 187 ? 0.39422 0.34778 0.33811 0.00474  -0.01008 0.04313  194 GLN A O   
1379 C CB  . GLN A 187 ? 0.32987 0.31486 0.29296 0.03841  -0.01996 0.05653  194 GLN A CB  
1380 C CG  . GLN A 187 ? 0.33203 0.35068 0.31527 0.05387  -0.03100 0.06344  194 GLN A CG  
1381 C CD  . GLN A 187 ? 0.34176 0.38441 0.31505 0.05236  -0.04820 0.06850  194 GLN A CD  
1382 O OE1 . GLN A 187 ? 0.37824 0.42361 0.33706 0.03686  -0.04978 0.06137  194 GLN A OE1 
1383 N NE2 . GLN A 187 ? 0.36705 0.42846 0.34624 0.07161  -0.06256 0.07917  194 GLN A NE2 
1384 N N   . THR A 188 ? 0.41136 0.31097 0.34980 0.01144  0.00497  0.06719  195 THR A N   
1385 C CA  . THR A 188 ? 0.39584 0.28151 0.34585 -0.01043 0.01238  0.05300  195 THR A CA  
1386 C C   . THR A 188 ? 0.43012 0.34035 0.37839 -0.02454 0.01326  0.05501  195 THR A C   
1387 O O   . THR A 188 ? 0.38673 0.29792 0.35411 -0.04259 0.01725  0.04195  195 THR A O   
1388 C CB  . THR A 188 ? 0.49052 0.32653 0.45062 -0.01472 0.02835  0.06070  195 THR A CB  
1389 O OG1 . THR A 188 ? 0.58039 0.40217 0.52410 -0.00537 0.03886  0.09295  195 THR A OG1 
1390 C CG2 . THR A 188 ? 0.47696 0.28305 0.44120 -0.00022 0.02918  0.05159  195 THR A CG2 
1391 N N   . GLU A 189 ? 0.37413 0.30643 0.30258 -0.01573 0.00870  0.06794  196 GLU A N   
1392 C CA  . GLU A 189 ? 0.40899 0.36365 0.33286 -0.02547 0.01156  0.06641  196 GLU A CA  
1393 C C   . GLU A 189 ? 0.39162 0.37094 0.33177 -0.03453 0.00246  0.04380  196 GLU A C   
1394 O O   . GLU A 189 ? 0.36357 0.35833 0.31308 -0.04415 0.00712  0.03841  196 GLU A O   
1395 C CB  . GLU A 189 ? 0.39248 0.36417 0.28597 -0.01160 0.00460  0.07736  196 GLU A CB  
1396 C CG  . GLU A 189 ? 0.30224 0.29995 0.19849 -0.00493 -0.01502 0.06387  196 GLU A CG  
1397 C CD  . GLU A 189 ? 0.46258 0.47695 0.33393 0.00857  -0.02780 0.06927  196 GLU A CD  
1398 O OE1 . GLU A 189 ? 0.56248 0.57365 0.42529 0.02445  -0.03528 0.08226  196 GLU A OE1 
1399 O OE2 . GLU A 189 ? 0.43361 0.46486 0.29410 0.00524  -0.03228 0.05829  196 GLU A OE2 
1400 N N   . TYR A 190 ? 0.31766 0.30124 0.26089 -0.02872 -0.00819 0.03283  197 TYR A N   
1401 C CA  . TYR A 190 ? 0.32464 0.32632 0.27442 -0.03185 -0.01564 0.01684  197 TYR A CA  
1402 C C   . TYR A 190 ? 0.34756 0.34356 0.31163 -0.04072 -0.01705 0.00124  197 TYR A C   
1403 O O   . TYR A 190 ? 0.37873 0.38860 0.34138 -0.03822 -0.02604 -0.01140 197 TYR A O   
1404 C CB  . TYR A 190 ? 0.30325 0.31101 0.24760 -0.02081 -0.02118 0.01563  197 TYR A CB  
1405 C CG  . TYR A 190 ? 0.31991 0.34043 0.26127 -0.01575 -0.02490 0.02454  197 TYR A CG  
1406 C CD1 . TYR A 190 ? 0.32510 0.35947 0.26282 -0.01967 -0.02783 0.02178  197 TYR A CD1 
1407 C CD2 . TYR A 190 ? 0.29004 0.31023 0.23406 -0.00558 -0.02745 0.03278  197 TYR A CD2 
1408 C CE1 . TYR A 190 ? 0.33534 0.38114 0.26918 -0.01607 -0.03527 0.02289  197 TYR A CE1 
1409 C CE2 . TYR A 190 ? 0.31351 0.35246 0.25831 -0.00105 -0.03723 0.03606  197 TYR A CE2 
1410 C CZ  . TYR A 190 ? 0.35363 0.40428 0.29170 -0.00762 -0.04208 0.02910  197 TYR A CZ  
1411 O OH  . TYR A 190 ? 0.33971 0.40852 0.27725 -0.00409 -0.05556 0.02542  197 TYR A OH  
1412 N N   . LEU A 191 ? 0.34480 0.31964 0.32274 -0.05042 -0.00904 0.00162  198 LEU A N   
1413 C CA  . LEU A 191 ? 0.29308 0.26768 0.29676 -0.06496 -0.01232 -0.01788 198 LEU A CA  
1414 C C   . LEU A 191 ? 0.34901 0.34163 0.38211 -0.08068 -0.00338 -0.01468 198 LEU A C   
1415 O O   . LEU A 191 ? 0.33379 0.33889 0.40131 -0.09503 -0.00865 -0.03334 198 LEU A O   
1416 C CB  . LEU A 191 ? 0.40391 0.33881 0.41579 -0.06957 -0.00684 -0.02452 198 LEU A CB  
1417 C CG  . LEU A 191 ? 0.44246 0.35887 0.42962 -0.05207 -0.01161 -0.03119 198 LEU A CG  
1418 C CD1 . LEU A 191 ? 0.49921 0.36889 0.49601 -0.05450 -0.00266 -0.03726 198 LEU A CD1 
1419 C CD2 . LEU A 191 ? 0.44542 0.38284 0.41849 -0.04597 -0.02768 -0.05410 198 LEU A CD2 
1420 N N   . GLU A 192 ? 0.30040 0.29813 0.32225 -0.07741 0.00986  0.00633  199 GLU A N   
1421 C CA  . GLU A 192 ? 0.36002 0.37519 0.40685 -0.08933 0.02574  0.01227  199 GLU A CA  
1422 C C   . GLU A 192 ? 0.28671 0.34314 0.34399 -0.08538 0.01560  -0.00012 199 GLU A C   
1423 O O   . GLU A 192 ? 0.29323 0.35674 0.32204 -0.07030 0.00583  0.00046  199 GLU A O   
1424 C CB  . GLU A 192 ? 0.39461 0.39608 0.41251 -0.08219 0.04580  0.03963  199 GLU A CB  
1425 C CG  . GLU A 192 ? 0.47326 0.43157 0.48244 -0.08283 0.06033  0.05914  199 GLU A CG  
1426 C CD  . GLU A 192 ? 0.90785 0.85506 0.86940 -0.06501 0.07040  0.08671  199 GLU A CD  
1427 O OE1 . GLU A 192 ? 0.86220 0.77673 0.80334 -0.05399 0.07258  0.10392  199 GLU A OE1 
1428 O OE2 . GLU A 192 ? 0.86145 0.83280 0.80381 -0.05924 0.07495  0.08988  199 GLU A OE2 
1429 N N   . GLU A 193 ? 0.28929 0.37283 0.39360 -0.09878 0.01893  -0.01105 200 GLU A N   
1430 C CA  . GLU A 193 ? 0.27381 0.39892 0.39461 -0.09106 0.00873  -0.02219 200 GLU A CA  
1431 C C   . GLU A 193 ? 0.27747 0.40818 0.37054 -0.07703 0.02167  -0.00866 200 GLU A C   
1432 O O   . GLU A 193 ? 0.21605 0.35583 0.29158 -0.06143 0.00934  -0.01357 200 GLU A O   
1433 C CB  . GLU A 193 ? 0.29021 0.45115 0.47806 -0.10805 0.01237  -0.03515 200 GLU A CB  
1434 C CG  . GLU A 193 ? 0.31975 0.52901 0.53170 -0.09554 -0.00067 -0.04669 200 GLU A CG  
1435 C CD  . GLU A 193 ? 0.55077 0.80688 0.84185 -0.11204 0.00349  -0.05968 200 GLU A CD  
1436 O OE1 . GLU A 193 ? 0.58076 0.82816 0.90980 -0.13691 0.02251  -0.05753 200 GLU A OE1 
1437 O OE2 . GLU A 193 ? 0.51584 0.81808 0.83627 -0.09965 -0.01122 -0.07109 200 GLU A OE2 
1438 N N   . ARG A 194 ? 0.24618 0.36782 0.33191 -0.08120 0.04796  0.00816  201 ARG A N   
1439 C CA  . ARG A 194 ? 0.25698 0.38439 0.31143 -0.06659 0.05998  0.01534  201 ARG A CA  
1440 C C   . ARG A 194 ? 0.27891 0.38452 0.28179 -0.05210 0.04390  0.01584  201 ARG A C   
1441 O O   . ARG A 194 ? 0.26059 0.37227 0.24447 -0.03962 0.04179  0.00978  201 ARG A O   
1442 C CB  . ARG A 194 ? 0.34050 0.46034 0.38550 -0.07066 0.09313  0.03511  201 ARG A CB  
1443 C CG  . ARG A 194 ? 0.46576 0.54556 0.47363 -0.07133 0.09853  0.05502  201 ARG A CG  
1444 C CD  . ARG A 194 ? 0.55093 0.62055 0.55279 -0.07533 0.13638  0.08002  201 ARG A CD  
1445 N NE  . ARG A 194 ? 0.73102 0.75941 0.68800 -0.06847 0.14134  0.10402  201 ARG A NE  
1446 C CZ  . ARG A 194 ? 0.60090 0.60805 0.53672 -0.06679 0.17472  0.13374  201 ARG A CZ  
1447 N NH1 . ARG A 194 ? 0.68659 0.71096 0.64418 -0.07409 0.21049  0.14311  201 ARG A NH1 
1448 N NH2 . ARG A 194 ? 0.85984 0.82826 0.75154 -0.05484 0.17448  0.15709  201 ARG A NH2 
1449 N N   . ARG A 195 ? 0.28271 0.36348 0.26876 -0.05381 0.03332  0.02104  202 ARG A N   
1450 C CA  . ARG A 195 ? 0.26435 0.33259 0.21592 -0.04233 0.01827  0.02049  202 ARG A CA  
1451 C C   . ARG A 195 ? 0.32320 0.39921 0.28457 -0.03788 0.00149  0.00697  202 ARG A C   
1452 O O   . ARG A 195 ? 0.27967 0.35484 0.22662 -0.02989 -0.00427 0.00232  202 ARG A O   
1453 C CB  . ARG A 195 ? 0.34382 0.38824 0.28151 -0.04216 0.01466  0.03169  202 ARG A CB  
1454 C CG  . ARG A 195 ? 0.31448 0.35525 0.23098 -0.03156 -0.00143 0.03021  202 ARG A CG  
1455 C CD  . ARG A 195 ? 0.38054 0.42657 0.26557 -0.02223 -0.00282 0.03184  202 ARG A CD  
1456 N NE  . ARG A 195 ? 0.39224 0.43940 0.26773 -0.01459 -0.02054 0.02990  202 ARG A NE  
1457 C CZ  . ARG A 195 ? 0.38278 0.44079 0.25547 -0.01227 -0.03320 0.01538  202 ARG A CZ  
1458 N NH1 . ARG A 195 ? 0.34111 0.40288 0.21189 -0.01393 -0.02927 0.00213  202 ARG A NH1 
1459 N NH2 . ARG A 195 ? 0.38563 0.45112 0.26369 -0.00827 -0.04966 0.01259  202 ARG A NH2 
1460 N N   . ILE A 196 ? 0.26262 0.34370 0.24655 -0.04226 -0.00612 0.00024  203 ILE A N   
1461 C CA  . ILE A 196 ? 0.21917 0.30571 0.20338 -0.03344 -0.01944 -0.00756 203 ILE A CA  
1462 C C   . ILE A 196 ? 0.22766 0.33103 0.22101 -0.02497 -0.01738 -0.01178 203 ILE A C   
1463 O O   . ILE A 196 ? 0.24926 0.34467 0.23149 -0.01469 -0.02122 -0.01193 203 ILE A O   
1464 C CB  . ILE A 196 ? 0.20676 0.29801 0.20401 -0.03598 -0.03051 -0.01653 203 ILE A CB  
1465 C CG1 . ILE A 196 ? 0.25670 0.32430 0.24257 -0.04071 -0.03045 -0.01486 203 ILE A CG1 
1466 C CG2 . ILE A 196 ? 0.23077 0.32764 0.21749 -0.02126 -0.04264 -0.01999 203 ILE A CG2 
1467 C CD1 . ILE A 196 ? 0.30428 0.37222 0.30636 -0.04812 -0.03865 -0.02984 203 ILE A CD1 
1468 N N   . LYS A 197 ? 0.23145 0.35684 0.25008 -0.02877 -0.00827 -0.01460 204 LYS A N   
1469 C CA  . LYS A 197 ? 0.21379 0.35763 0.24572 -0.01714 -0.00330 -0.01921 204 LYS A CA  
1470 C C   . LYS A 197 ? 0.25201 0.37624 0.25391 -0.00929 0.00450  -0.01893 204 LYS A C   
1471 O O   . LYS A 197 ? 0.24085 0.35930 0.24091 0.00369  0.00195  -0.02370 204 LYS A O   
1472 C CB  . LYS A 197 ? 0.27590 0.45052 0.34577 -0.02417 0.01171  -0.02102 204 LYS A CB  
1473 C CG  . LYS A 197 ? 0.52078 0.73143 0.62938 -0.01164 0.00809  -0.02937 204 LYS A CG  
1474 C CD  . LYS A 197 ? 0.44885 0.69729 0.60878 -0.02226 0.02605  -0.03128 204 LYS A CD  
1475 C CE  . LYS A 197 ? 0.44854 0.70445 0.63971 -0.04533 0.01985  -0.03426 204 LYS A CE  
1476 N NZ  . LYS A 197 ? 0.52175 0.83096 0.78467 -0.05001 0.01178  -0.04796 204 LYS A NZ  
1477 N N   . GLU A 198 ? 0.24037 0.35214 0.21755 -0.01573 0.01289  -0.01436 205 GLU A N   
1478 C CA  . GLU A 198 ? 0.25280 0.34906 0.19834 -0.00884 0.01483  -0.02017 205 GLU A CA  
1479 C C   . GLU A 198 ? 0.30198 0.37890 0.24179 -0.00723 -0.00059 -0.02498 205 GLU A C   
1480 O O   . GLU A 198 ? 0.30131 0.36609 0.23549 -0.00072 -0.00097 -0.03620 205 GLU A O   
1481 C CB  . GLU A 198 ? 0.26775 0.35756 0.18227 -0.01259 0.02123  -0.01217 205 GLU A CB  
1482 C CG  . GLU A 198 ? 0.32259 0.40026 0.19855 -0.00519 0.01501  -0.02213 205 GLU A CG  
1483 C CD  . GLU A 198 ? 0.37736 0.45057 0.21802 -0.00404 0.01497  -0.01000 205 GLU A CD  
1484 O OE1 . GLU A 198 ? 0.39637 0.46479 0.24570 -0.00998 0.00818  0.00320  205 GLU A OE1 
1485 O OE2 . GLU A 198 ? 0.39631 0.46924 0.19672 0.00605  0.02248  -0.01301 205 GLU A OE2 
1486 N N   . ILE A 199 ? 0.23740 0.30930 0.18193 -0.01333 -0.01026 -0.01728 206 ILE A N   
1487 C CA  . ILE A 199 ? 0.24098 0.29721 0.18583 -0.01344 -0.01861 -0.01825 206 ILE A CA  
1488 C C   . ILE A 199 ? 0.28050 0.32921 0.23757 -0.00440 -0.01726 -0.01800 206 ILE A C   
1489 O O   . ILE A 199 ? 0.30994 0.33943 0.26979 -0.00276 -0.01601 -0.02172 206 ILE A O   
1490 C CB  . ILE A 199 ? 0.28017 0.33525 0.22588 -0.01887 -0.02401 -0.00903 206 ILE A CB  
1491 C CG1 . ILE A 199 ? 0.31987 0.37740 0.25232 -0.02270 -0.02604 -0.00605 206 ILE A CG1 
1492 C CG2 . ILE A 199 ? 0.29298 0.33669 0.24690 -0.01884 -0.02600 -0.00689 206 ILE A CG2 
1493 C CD1 . ILE A 199 ? 0.32817 0.38280 0.26381 -0.02447 -0.02811 0.00321  206 ILE A CD1 
1494 N N   . VAL A 200 ? 0.25051 0.31346 0.21701 0.00232  -0.01829 -0.01363 207 VAL A N   
1495 C CA  . VAL A 200 ? 0.26253 0.32006 0.23483 0.01754  -0.01939 -0.00950 207 VAL A CA  
1496 C C   . VAL A 200 ? 0.30412 0.35338 0.28296 0.02741  -0.01138 -0.01720 207 VAL A C   
1497 O O   . VAL A 200 ? 0.30637 0.32972 0.28542 0.03720  -0.00776 -0.01387 207 VAL A O   
1498 C CB  . VAL A 200 ? 0.27073 0.35458 0.25263 0.02491  -0.02878 -0.00763 207 VAL A CB  
1499 C CG1 . VAL A 200 ? 0.25518 0.33931 0.24049 0.04774  -0.03260 -0.00197 207 VAL A CG1 
1500 C CG2 . VAL A 200 ? 0.24252 0.32446 0.21112 0.01879  -0.03646 -0.00391 207 VAL A CG2 
1501 N N   . LYS A 201 ? 0.27746 0.34442 0.26089 0.02603  -0.00484 -0.02693 208 LYS A N   
1502 C CA  . LYS A 201 ? 0.30183 0.36084 0.28794 0.03818  0.00564  -0.03807 208 LYS A CA  
1503 C C   . LYS A 201 ? 0.34563 0.36922 0.31502 0.03284  0.00683  -0.04959 208 LYS A C   
1504 O O   . LYS A 201 ? 0.36885 0.36714 0.34242 0.04370  0.01275  -0.05828 208 LYS A O   
1505 C CB  . LYS A 201 ? 0.29985 0.38733 0.29007 0.03782  0.01769  -0.04469 208 LYS A CB  
1506 C CG  . LYS A 201 ? 0.40346 0.48568 0.39270 0.05368  0.03272  -0.05888 208 LYS A CG  
1507 C CD  . LYS A 201 ? 0.55782 0.67426 0.55474 0.05497  0.05119  -0.06062 208 LYS A CD  
1508 C CE  . LYS A 201 ? 0.67195 0.78443 0.66504 0.07480  0.07019  -0.07643 208 LYS A CE  
1509 N NZ  . LYS A 201 ? 0.69057 0.83994 0.73238 0.09183  0.07998  -0.07332 208 LYS A NZ  
1510 N N   . LYS A 202 ? 0.31975 0.34127 0.27471 0.01669  -0.00010 -0.05153 209 LYS A N   
1511 C CA  . LYS A 202 ? 0.36759 0.36587 0.31380 0.00902  -0.00455 -0.06805 209 LYS A CA  
1512 C C   . LYS A 202 ? 0.38829 0.35877 0.35518 0.00379  -0.00604 -0.06322 209 LYS A C   
1513 O O   . LYS A 202 ? 0.39748 0.33933 0.37287 0.00116  -0.00435 -0.07925 209 LYS A O   
1514 C CB  . LYS A 202 ? 0.34480 0.35850 0.27226 -0.00250 -0.01459 -0.07021 209 LYS A CB  
1515 C CG  . LYS A 202 ? 0.46415 0.46565 0.38810 -0.01145 -0.02726 -0.09038 209 LYS A CG  
1516 C CD  . LYS A 202 ? 0.58889 0.61060 0.48167 -0.01232 -0.03824 -0.09439 209 LYS A CD  
1517 C CE  . LYS A 202 ? 0.70994 0.73476 0.61344 -0.02314 -0.05932 -0.10835 209 LYS A CE  
1518 N NZ  . LYS A 202 ? 0.65208 0.70033 0.52537 -0.01868 -0.07298 -0.10387 209 LYS A NZ  
1519 N N   . HIS A 203 ? 0.31424 0.28999 0.28927 0.00219  -0.00665 -0.04198 210 HIS A N   
1520 C CA  . HIS A 203 ? 0.37925 0.33236 0.37141 -0.00482 -0.00276 -0.03245 210 HIS A CA  
1521 C C   . HIS A 203 ? 0.35256 0.28807 0.34565 0.01083  0.00749  -0.01049 210 HIS A C   
1522 O O   . HIS A 203 ? 0.41352 0.31979 0.41988 0.00790  0.01854  0.00016  210 HIS A O   
1523 C CB  . HIS A 203 ? 0.34470 0.31728 0.33968 -0.01727 -0.00881 -0.02485 210 HIS A CB  
1524 C CG  . HIS A 203 ? 0.39778 0.38503 0.39440 -0.02987 -0.02129 -0.04285 210 HIS A CG  
1525 N ND1 . HIS A 203 ? 0.45939 0.43421 0.47323 -0.04035 -0.02649 -0.06388 210 HIS A ND1 
1526 C CD2 . HIS A 203 ? 0.41481 0.42738 0.39622 -0.03142 -0.03142 -0.04328 210 HIS A CD2 
1527 C CE1 . HIS A 203 ? 0.47292 0.47087 0.47873 -0.04589 -0.04302 -0.07749 210 HIS A CE1 
1528 N NE2 . HIS A 203 ? 0.42346 0.44240 0.40770 -0.03906 -0.04458 -0.06221 210 HIS A NE2 
1529 N N   . SER A 204 ? 0.37171 0.38788 0.20709 -0.01750 -0.09336 -0.07141 211 SER A N   
1530 C CA  . SER A 204 ? 0.33638 0.34592 0.20336 -0.00995 -0.07610 -0.07137 211 SER A CA  
1531 C C   . SER A 204 ? 0.35848 0.33944 0.20164 0.00426  -0.05310 -0.07852 211 SER A C   
1532 O O   . SER A 204 ? 0.42729 0.41405 0.29543 0.01626  -0.03861 -0.07091 211 SER A O   
1533 C CB  . SER A 204 ? 0.38275 0.42501 0.29589 -0.00070 -0.07351 -0.05453 211 SER A CB  
1534 O OG  . SER A 204 ? 0.37080 0.44280 0.31282 -0.00868 -0.09219 -0.04765 211 SER A OG  
1535 N N   . GLN A 205 ? 0.47079 0.42344 0.26621 0.00310  -0.04939 -0.09400 212 GLN A N   
1536 C CA  . GLN A 205 ? 0.62102 0.55491 0.39699 0.02118  -0.02469 -0.10001 212 GLN A CA  
1537 C C   . GLN A 205 ? 0.57858 0.48794 0.37433 0.03042  -0.01117 -0.10432 212 GLN A C   
1538 O O   . GLN A 205 ? 0.56188 0.47359 0.36769 0.04985  0.00819  -0.09969 212 GLN A O   
1539 C CB  . GLN A 205 ? 0.65623 0.56493 0.37222 0.01788  -0.02120 -0.11928 212 GLN A CB  
1540 C CG  . GLN A 205 ? 0.82986 0.72424 0.52628 0.03884  0.00847  -0.12761 212 GLN A CG  
1541 C CD  . GLN A 205 ? 0.98050 0.84412 0.62017 0.03374  0.01616  -0.15309 212 GLN A CD  
1542 O OE1 . GLN A 205 ? 0.90752 0.75521 0.52677 0.01292  -0.00164 -0.16687 212 GLN A OE1 
1543 N NE2 . GLN A 205 ? 0.96769 0.83746 0.60035 0.04853  0.04297  -0.15640 212 GLN A NE2 
1544 N N   . PHE A 206 ? 0.56697 0.45596 0.37153 0.01622  -0.02178 -0.10988 213 PHE A N   
1545 C CA  . PHE A 206 ? 0.55365 0.40992 0.37003 0.02362  -0.01058 -0.11155 213 PHE A CA  
1546 C C   . PHE A 206 ? 0.49919 0.37683 0.35883 0.01749  -0.01625 -0.09327 213 PHE A C   
1547 O O   . PHE A 206 ? 0.56472 0.41358 0.43168 0.01447  -0.01393 -0.09154 213 PHE A O   
1548 C CB  . PHE A 206 ? 0.58247 0.38313 0.36529 0.01056  -0.01379 -0.13415 213 PHE A CB  
1549 C CG  . PHE A 206 ? 0.64895 0.42236 0.38140 0.01741  -0.00374 -0.15710 213 PHE A CG  
1550 C CD1 . PHE A 206 ? 0.75344 0.51843 0.44505 -0.00506 -0.01963 -0.17476 213 PHE A CD1 
1551 C CD2 . PHE A 206 ? 0.68615 0.44881 0.41211 0.04587  0.02185  -0.16065 213 PHE A CD2 
1552 C CE1 . PHE A 206 ? 0.84946 0.60223 0.50020 -0.00100 -0.00862 -0.19354 213 PHE A CE1 
1553 C CE2 . PHE A 206 ? 0.89553 0.64271 0.57995 0.05129  0.03519  -0.18141 213 PHE A CE2 
1554 C CZ  . PHE A 206 ? 0.83221 0.57824 0.48213 0.02654  0.02005  -0.19672 213 PHE A CZ  
1555 N N   . ILE A 207 ? 0.38904 0.31361 0.27505 0.01542  -0.02229 -0.07961 214 ILE A N   
1556 C CA  . ILE A 207 ? 0.35949 0.30685 0.28122 0.01143  -0.02287 -0.06497 214 ILE A CA  
1557 C C   . ILE A 207 ? 0.43873 0.38047 0.36938 0.02894  -0.00877 -0.05491 214 ILE A C   
1558 O O   . ILE A 207 ? 0.40053 0.35009 0.32802 0.04656  0.00145  -0.05339 214 ILE A O   
1559 C CB  . ILE A 207 ? 0.35682 0.34997 0.30235 0.00924  -0.02863 -0.05682 214 ILE A CB  
1560 C CG1 . ILE A 207 ? 0.39782 0.40283 0.34481 -0.00663 -0.04554 -0.06197 214 ILE A CG1 
1561 C CG2 . ILE A 207 ? 0.31792 0.33449 0.29328 0.00724  -0.02421 -0.04566 214 ILE A CG2 
1562 C CD1 . ILE A 207 ? 0.36095 0.36660 0.32460 -0.02660 -0.05293 -0.06290 214 ILE A CD1 
1563 N N   . GLY A 208 ? 0.38254 0.31441 0.32577 0.02315  -0.00882 -0.04547 215 GLY A N   
1564 C CA  . GLY A 208 ? 0.40678 0.33129 0.35800 0.03965  0.00044  -0.03220 215 GLY A CA  
1565 C C   . GLY A 208 ? 0.34859 0.31935 0.32227 0.04370  0.00176  -0.01683 215 GLY A C   
1566 O O   . GLY A 208 ? 0.37454 0.34866 0.35781 0.04715  0.00268  -0.00074 215 GLY A O   
1567 N N   . TYR A 209 ? 0.31359 0.31777 0.29352 0.04206  0.00079  -0.02103 216 TYR A N   
1568 C CA  . TYR A 209 ? 0.32318 0.36697 0.32081 0.04202  0.00184  -0.01172 216 TYR A CA  
1569 C C   . TYR A 209 ? 0.28416 0.34539 0.28295 0.04928  0.00552  -0.01626 216 TYR A C   
1570 O O   . TYR A 209 ? 0.32234 0.37271 0.30867 0.04847  0.00408  -0.02559 216 TYR A O   
1571 C CB  . TYR A 209 ? 0.23483 0.29870 0.24242 0.02413  -0.00279 -0.01239 216 TYR A CB  
1572 C CG  . TYR A 209 ? 0.28930 0.34177 0.29539 0.01278  -0.00438 -0.00449 216 TYR A CG  
1573 C CD1 . TYR A 209 ? 0.27639 0.33696 0.28295 0.01349  -0.00315 0.01153  216 TYR A CD1 
1574 C CD2 . TYR A 209 ? 0.25788 0.29310 0.26164 -0.00087 -0.00839 -0.01051 216 TYR A CD2 
1575 C CE1 . TYR A 209 ? 0.33091 0.37891 0.33272 0.00133  -0.00419 0.02316  216 TYR A CE1 
1576 C CE2 . TYR A 209 ? 0.26552 0.28930 0.26836 -0.01495 -0.00856 -0.00094 216 TYR A CE2 
1577 C CZ  . TYR A 209 ? 0.29750 0.32544 0.29780 -0.01349 -0.00559 0.01680  216 TYR A CZ  
1578 O OH  . TYR A 209 ? 0.33879 0.35352 0.33501 -0.02927 -0.00539 0.03049  216 TYR A OH  
1579 N N   . PRO A 210 ? 0.29168 0.38093 0.30392 0.05389  0.00910  -0.00811 217 PRO A N   
1580 C CA  . PRO A 210 ? 0.30742 0.41278 0.32234 0.05631  0.01343  -0.01004 217 PRO A CA  
1581 C C   . PRO A 210 ? 0.27350 0.38183 0.28964 0.04437  0.00818  -0.01642 217 PRO A C   
1582 O O   . PRO A 210 ? 0.26121 0.38110 0.28828 0.03447  0.00486  -0.01788 217 PRO A O   
1583 C CB  . PRO A 210 ? 0.28658 0.42501 0.32033 0.05757  0.01544  0.00071  217 PRO A CB  
1584 C CG  . PRO A 210 ? 0.27395 0.41774 0.31143 0.05118  0.00877  0.00697  217 PRO A CG  
1585 C CD  . PRO A 210 ? 0.25631 0.36547 0.28084 0.05446  0.00772  0.00511  217 PRO A CD  
1586 N N   . ILE A 211 ? 0.25357 0.35108 0.25737 0.04658  0.00807  -0.01987 218 ILE A N   
1587 C CA  . ILE A 211 ? 0.22357 0.32269 0.23155 0.03999  0.00219  -0.02116 218 ILE A CA  
1588 C C   . ILE A 211 ? 0.29893 0.40770 0.30961 0.04021  0.00823  -0.01419 218 ILE A C   
1589 O O   . ILE A 211 ? 0.28845 0.39449 0.28328 0.04547  0.01413  -0.01033 218 ILE A O   
1590 C CB  . ILE A 211 ? 0.29094 0.37379 0.28197 0.03968  -0.00643 -0.02512 218 ILE A CB  
1591 C CG1 . ILE A 211 ? 0.28810 0.36105 0.27798 0.03473  -0.01222 -0.03194 218 ILE A CG1 
1592 C CG2 . ILE A 211 ? 0.27817 0.36609 0.28005 0.03677  -0.01460 -0.02141 218 ILE A CG2 
1593 C CD1 . ILE A 211 ? 0.26427 0.32649 0.23967 0.02926  -0.02440 -0.03708 218 ILE A CD1 
1594 N N   . THR A 212 ? 0.23405 0.35308 0.26292 0.03255  0.00841  -0.01359 219 THR A N   
1595 C CA  . THR A 212 ? 0.22234 0.34694 0.25647 0.02737  0.01341  -0.00662 219 THR A CA  
1596 C C   . THR A 212 ? 0.22491 0.33164 0.26115 0.02523  0.00830  -0.00425 219 THR A C   
1597 O O   . THR A 212 ? 0.20515 0.30611 0.25579 0.02357  0.00438  -0.01160 219 THR A O   
1598 C CB  . THR A 212 ? 0.23983 0.38339 0.29092 0.01705  0.01583  -0.00860 219 THR A CB  
1599 O OG1 . THR A 212 ? 0.23910 0.40249 0.29177 0.02180  0.01749  -0.00605 219 THR A OG1 
1600 C CG2 . THR A 212 ? 0.16997 0.31896 0.22812 0.00693  0.02077  -0.00112 219 THR A CG2 
1601 N N   . LEU A 213 ? 0.22267 0.32143 0.24479 0.02654  0.00934  0.00719  220 LEU A N   
1602 C CA  . LEU A 213 ? 0.21506 0.29509 0.23954 0.02581  0.00310  0.01622  220 LEU A CA  
1603 C C   . LEU A 213 ? 0.26911 0.34343 0.30629 0.01430  0.01002  0.02243  220 LEU A C   
1604 O O   . LEU A 213 ? 0.25561 0.33778 0.28393 0.00742  0.01811  0.03342  220 LEU A O   
1605 C CB  . LEU A 213 ? 0.28296 0.35651 0.27912 0.03040  -0.00164 0.02857  220 LEU A CB  
1606 C CG  . LEU A 213 ? 0.34052 0.39566 0.33576 0.03012  -0.00953 0.04643  220 LEU A CG  
1607 C CD1 . LEU A 213 ? 0.32645 0.37245 0.34989 0.03740  -0.02090 0.04235  220 LEU A CD1 
1608 C CD2 . LEU A 213 ? 0.37037 0.42472 0.32810 0.03207  -0.01576 0.05948  220 LEU A CD2 
1609 N N   . PHE A 214 ? 0.22873 0.28961 0.28691 0.01075  0.00847  0.01378  221 PHE A N   
1610 C CA  . PHE A 214 ? 0.24129 0.28705 0.31046 -0.00342 0.01381  0.01626  221 PHE A CA  
1611 C C   . PHE A 214 ? 0.29767 0.31733 0.36012 -0.00357 0.01189  0.03819  221 PHE A C   
1612 O O   . PHE A 214 ? 0.29345 0.30182 0.34971 0.00985  0.00292  0.04830  221 PHE A O   
1613 C CB  . PHE A 214 ? 0.21812 0.24741 0.30639 -0.00563 0.01430  -0.00268 221 PHE A CB  
1614 C CG  . PHE A 214 ? 0.21484 0.26937 0.30471 -0.01363 0.01739  -0.02167 221 PHE A CG  
1615 C CD1 . PHE A 214 ? 0.21732 0.30205 0.29827 -0.00803 0.01568  -0.02174 221 PHE A CD1 
1616 C CD2 . PHE A 214 ? 0.26869 0.31307 0.36598 -0.02755 0.02148  -0.03922 221 PHE A CD2 
1617 C CE1 . PHE A 214 ? 0.21803 0.32529 0.29883 -0.01525 0.01651  -0.03372 221 PHE A CE1 
1618 C CE2 . PHE A 214 ? 0.24640 0.31674 0.33899 -0.03700 0.02223  -0.05447 221 PHE A CE2 
1619 C CZ  . PHE A 214 ? 0.18419 0.28752 0.26922 -0.03034 0.01898  -0.04910 221 PHE A CZ  
1620 N N   . VAL A 215 ? 0.27117 0.28338 0.33527 -0.02102 0.01900  0.04785  222 VAL A N   
1621 C CA  . VAL A 215 ? 0.31393 0.29684 0.37105 -0.02571 0.01853  0.07249  222 VAL A CA  
1622 C C   . VAL A 215 ? 0.35468 0.29552 0.43305 -0.03595 0.01946  0.06759  222 VAL A C   
1623 O O   . VAL A 215 ? 0.38824 0.33107 0.48039 -0.04737 0.02355  0.04500  222 VAL A O   
1624 C CB  . VAL A 215 ? 0.40595 0.41207 0.44674 -0.04031 0.02895  0.09050  222 VAL A CB  
1625 C CG1 . VAL A 215 ? 0.41843 0.45620 0.47549 -0.05729 0.03792  0.07772  222 VAL A CG1 
1626 C CG2 . VAL A 215 ? 0.47711 0.45158 0.50962 -0.05208 0.03065  0.11927  222 VAL A CG2 
1627 N N   . GLU A 216 ? 0.41226 0.31208 0.49089 -0.03178 0.01503  0.08877  223 GLU A N   
1628 C CA  . GLU A 216 ? 0.54540 0.39142 0.64464 -0.03606 0.01606  0.08537  223 GLU A CA  
1629 C C   . GLU A 216 ? 0.56194 0.38256 0.65925 -0.06546 0.02372  0.10038  223 GLU A C   
1630 O O   . GLU A 216 ? 0.71279 0.56450 0.79576 -0.08289 0.02951  0.11533  223 GLU A O   
1631 C CB  . GLU A 216 ? 0.63543 0.44766 0.74298 -0.01070 0.00523  0.10305  223 GLU A CB  
1632 C CG  . GLU A 216 ? 0.71444 0.55065 0.83441 0.01515  -0.00199 0.08623  223 GLU A CG  
1633 C CD  . GLU A 216 ? 0.73753 0.54015 0.88269 0.04059  -0.01112 0.09770  223 GLU A CD  
1634 O OE1 . GLU A 216 ? 0.86798 0.69040 1.00845 0.05735  -0.02577 0.11782  223 GLU A OE1 
1635 O OE2 . GLU A 216 ? 0.87746 0.63293 1.04676 0.04346  -0.00432 0.08818  223 GLU A OE2 
1636 N N   . LYS A 217 ? 0.90745 0.66929 1.02174 -0.07081 0.02522  0.09543  224 LYS A N   
1637 C CA  . LYS A 217 ? 0.78120 0.50340 0.89778 -0.10172 0.03167  0.10737  224 LYS A CA  
1638 C C   . LYS A 217 ? 0.99387 0.68912 1.09744 -0.10295 0.02900  0.15299  224 LYS A C   
1639 O O   . LYS A 217 ? 1.13416 0.80865 1.23593 -0.07580 0.01926  0.17232  224 LYS A O   
1640 C CB  . LYS A 217 ? 0.96702 0.62696 1.10387 -0.10507 0.03501  0.07984  224 LYS A CB  
1641 C CG  . LYS A 217 ? 1.07670 0.66394 1.22886 -0.08040 0.03160  0.09293  224 LYS A CG  
1642 C CD  . LYS A 217 ? 1.00972 0.53735 1.15949 -0.09661 0.03159  0.13041  224 LYS A CD  
1643 C CE  . LYS A 217 ? 1.19177 0.65215 1.35396 -0.06649 0.02692  0.13635  224 LYS A CE  
1644 N NZ  . LYS A 217 ? 1.16344 0.56905 1.30661 -0.08068 0.02558  0.16693  224 LYS A NZ  
# 
