data_7HB4
# 
_entry.id   7HB4 
# 
_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   7HB4         pdb_00007hb4 10.2210/pdb7hb4/pdb 
WWPDB D_1001407251 ?            ?                   
# 
_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                        7HB4 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.recvd_initial_deposition_date   2024-07-10 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.pdb_format_compatible           N 
_pdbx_database_status.methods_development_category    ? 
# 
_pdbx_contact_author.id                 1 
_pdbx_contact_author.name_last          Yu 
_pdbx_contact_author.name_first         Feng 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.email              yufeng@sari.ac.cn 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-9502-3277 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Huang, L.' 1  ? 
'Wang, W.'  2  ? 
'Zhu, Z.'   3  ? 
'Li, Q.'    4  ? 
'Li, M.'    5  ? 
'Zhou, H.'  6  ? 
'Xu, Q.'    7  ? 
'Wen, W.'   8  ? 
'Wang, Q.'  9  ? 
'Yu, F.'    10 ? 
# 
_citation.id                        primary 
_citation.title                     
;Novel starting points for fragment-based drug design against human heat-shock protein 90 identified using crystallographic fragment screening.
;
_citation.journal_abbrev            Iucrj 
_citation.journal_volume            12 
_citation.page_first                177 
_citation.page_last                 187 
_citation.year                      2025 
_citation.journal_id_ASTM           ? 
_citation.country                   UK 
_citation.journal_id_ISSN           2052-2525 
_citation.journal_id_CSD            ? 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   39819741 
_citation.pdbx_database_id_DOI      10.1107/S2052252524012247 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.identifier_ORCID 
_citation_author.ordinal 
primary 'Huang, L.' 0009-0001-8431-0182 1  
primary 'Wang, W.'  ?                   2  
primary 'Zhu, Z.'   ?                   3  
primary 'Li, Q.'    ?                   4  
primary 'Li, M.'    ?                   5  
primary 'Zhou, H.'  ?                   6  
primary 'Xu, Q.'    0000-0002-7137-0768 7  
primary 'Wen, W.'   ?                   8  
primary 'Wang, Q.'  ?                   9  
primary 'Yu, F.'    0000-0002-9502-3277 10 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Heat shock protein HSP 90-alpha' 26859.117 1   3.6.4.10 ? ? ? 
2 non-polymer syn 'N-(3-methylphenyl)thiourea'      166.243   1   ?        ? ? ? 
3 water       nat water                             18.015    305 ?        ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        
;Heat shock 86 kDa,HSP 86,HSP86,Heat shock protein family C member 1,Lipopolysaccharide-associated protein 2,LAP-2,LPS-associated protein 2,Renal carcinoma antigen NY-REN-38
;
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;MDQPMEEEEVETFAFQAEIAQLMSLIINTFYSNKEIFLRELISNSSDALDKIRYESLTDPSKLDSGKELHINLIPNKQDR
TLTIVDTGIGMTKADLINNLGTIAKSGTKAFMEALQAGADISMIGQFGVGFYSAYLVAEKVTVITKHNDDEQYAWESSAG
GSFTVRTDTGEPMGRGTKVILHLKEDQTEYLEERRIKEIVKKHSQFIGYPITLFVEKERDKEVSDDEAELEHHHHHH
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MDQPMEEEEVETFAFQAEIAQLMSLIINTFYSNKEIFLRELISNSSDALDKIRYESLTDPSKLDSGKELHINLIPNKQDR
TLTIVDTGIGMTKADLINNLGTIAKSGTKAFMEALQAGADISMIGQFGVGFYSAYLVAEKVTVITKHNDDEQYAWESSAG
GSFTVRTDTGEPMGRGTKVILHLKEDQTEYLEERRIKEIVKKHSQFIGYPITLFVEKERDKEVSDDEAELEHHHHHH
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'N-(3-methylphenyl)thiourea' A1AXV 
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 
A1AXV non-polymer         . 'N-(3-methylphenyl)thiourea' ? 'C8 H10 N2 S'    166.243 
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        A1AXV 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1AXV 
_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 A1AXV 1   301 301 A1AXV AJW A . 
C 3 HOH   1   401 99  HOH   HOH A . 
C 3 HOH   2   402 179 HOH   HOH A . 
C 3 HOH   3   403 277 HOH   HOH A . 
C 3 HOH   4   404 194 HOH   HOH A . 
C 3 HOH   5   405 209 HOH   HOH A . 
C 3 HOH   6   406 292 HOH   HOH A . 
C 3 HOH   7   407 269 HOH   HOH A . 
C 3 HOH   8   408 110 HOH   HOH A . 
C 3 HOH   9   409 91  HOH   HOH A . 
C 3 HOH   10  410 107 HOH   HOH A . 
C 3 HOH   11  411 188 HOH   HOH A . 
C 3 HOH   12  412 210 HOH   HOH A . 
C 3 HOH   13  413 177 HOH   HOH A . 
C 3 HOH   14  414 162 HOH   HOH A . 
C 3 HOH   15  415 106 HOH   HOH A . 
C 3 HOH   16  416 257 HOH   HOH A . 
C 3 HOH   17  417 298 HOH   HOH A . 
C 3 HOH   18  418 125 HOH   HOH A . 
C 3 HOH   19  419 68  HOH   HOH A . 
C 3 HOH   20  420 80  HOH   HOH A . 
C 3 HOH   21  421 139 HOH   HOH A . 
C 3 HOH   22  422 23  HOH   HOH A . 
C 3 HOH   23  423 2   HOH   HOH A . 
C 3 HOH   24  424 66  HOH   HOH A . 
C 3 HOH   25  425 26  HOH   HOH A . 
C 3 HOH   26  426 262 HOH   HOH A . 
C 3 HOH   27  427 92  HOH   HOH A . 
C 3 HOH   28  428 17  HOH   HOH A . 
C 3 HOH   29  429 195 HOH   HOH A . 
C 3 HOH   30  430 183 HOH   HOH A . 
C 3 HOH   31  431 103 HOH   HOH A . 
C 3 HOH   32  432 228 HOH   HOH A . 
C 3 HOH   33  433 276 HOH   HOH A . 
C 3 HOH   34  434 38  HOH   HOH A . 
C 3 HOH   35  435 13  HOH   HOH A . 
C 3 HOH   36  436 97  HOH   HOH A . 
C 3 HOH   37  437 18  HOH   HOH A . 
C 3 HOH   38  438 83  HOH   HOH A . 
C 3 HOH   39  439 59  HOH   HOH A . 
C 3 HOH   40  440 159 HOH   HOH A . 
C 3 HOH   41  441 71  HOH   HOH A . 
C 3 HOH   42  442 178 HOH   HOH A . 
C 3 HOH   43  443 130 HOH   HOH A . 
C 3 HOH   44  444 5   HOH   HOH A . 
C 3 HOH   45  445 102 HOH   HOH A . 
C 3 HOH   46  446 265 HOH   HOH A . 
C 3 HOH   47  447 303 HOH   HOH A . 
C 3 HOH   48  448 87  HOH   HOH A . 
C 3 HOH   49  449 96  HOH   HOH A . 
C 3 HOH   50  450 8   HOH   HOH A . 
C 3 HOH   51  451 27  HOH   HOH A . 
C 3 HOH   52  452 43  HOH   HOH A . 
C 3 HOH   53  453 205 HOH   HOH A . 
C 3 HOH   54  454 69  HOH   HOH A . 
C 3 HOH   55  455 134 HOH   HOH A . 
C 3 HOH   56  456 198 HOH   HOH A . 
C 3 HOH   57  457 98  HOH   HOH A . 
C 3 HOH   58  458 100 HOH   HOH A . 
C 3 HOH   59  459 161 HOH   HOH A . 
C 3 HOH   60  460 55  HOH   HOH A . 
C 3 HOH   61  461 10  HOH   HOH A . 
C 3 HOH   62  462 264 HOH   HOH A . 
C 3 HOH   63  463 3   HOH   HOH A . 
C 3 HOH   64  464 25  HOH   HOH A . 
C 3 HOH   65  465 131 HOH   HOH A . 
C 3 HOH   66  466 111 HOH   HOH A . 
C 3 HOH   67  467 4   HOH   HOH A . 
C 3 HOH   68  468 167 HOH   HOH A . 
C 3 HOH   69  469 267 HOH   HOH A . 
C 3 HOH   70  470 213 HOH   HOH A . 
C 3 HOH   71  471 147 HOH   HOH A . 
C 3 HOH   72  472 141 HOH   HOH A . 
C 3 HOH   73  473 7   HOH   HOH A . 
C 3 HOH   74  474 185 HOH   HOH A . 
C 3 HOH   75  475 30  HOH   HOH A . 
C 3 HOH   76  476 54  HOH   HOH A . 
C 3 HOH   77  477 1   HOH   HOH A . 
C 3 HOH   78  478 101 HOH   HOH A . 
C 3 HOH   79  479 72  HOH   HOH A . 
C 3 HOH   80  480 48  HOH   HOH A . 
C 3 HOH   81  481 81  HOH   HOH A . 
C 3 HOH   82  482 240 HOH   HOH A . 
C 3 HOH   83  483 253 HOH   HOH A . 
C 3 HOH   84  484 90  HOH   HOH A . 
C 3 HOH   85  485 40  HOH   HOH A . 
C 3 HOH   86  486 153 HOH   HOH A . 
C 3 HOH   87  487 221 HOH   HOH A . 
C 3 HOH   88  488 16  HOH   HOH A . 
C 3 HOH   89  489 109 HOH   HOH A . 
C 3 HOH   90  490 122 HOH   HOH A . 
C 3 HOH   91  491 20  HOH   HOH A . 
C 3 HOH   92  492 53  HOH   HOH A . 
C 3 HOH   93  493 28  HOH   HOH A . 
C 3 HOH   94  494 33  HOH   HOH A . 
C 3 HOH   95  495 89  HOH   HOH A . 
C 3 HOH   96  496 62  HOH   HOH A . 
C 3 HOH   97  497 169 HOH   HOH A . 
C 3 HOH   98  498 281 HOH   HOH A . 
C 3 HOH   99  499 52  HOH   HOH A . 
C 3 HOH   100 500 77  HOH   HOH A . 
C 3 HOH   101 501 61  HOH   HOH A . 
C 3 HOH   102 502 252 HOH   HOH A . 
C 3 HOH   103 503 22  HOH   HOH A . 
C 3 HOH   104 504 70  HOH   HOH A . 
C 3 HOH   105 505 127 HOH   HOH A . 
C 3 HOH   106 506 36  HOH   HOH A . 
C 3 HOH   107 507 143 HOH   HOH A . 
C 3 HOH   108 508 231 HOH   HOH A . 
C 3 HOH   109 509 291 HOH   HOH A . 
C 3 HOH   110 510 32  HOH   HOH A . 
C 3 HOH   111 511 6   HOH   HOH A . 
C 3 HOH   112 512 172 HOH   HOH A . 
C 3 HOH   113 513 216 HOH   HOH A . 
C 3 HOH   114 514 64  HOH   HOH A . 
C 3 HOH   115 515 263 HOH   HOH A . 
C 3 HOH   116 516 151 HOH   HOH A . 
C 3 HOH   117 517 73  HOH   HOH A . 
C 3 HOH   118 518 31  HOH   HOH A . 
C 3 HOH   119 519 174 HOH   HOH A . 
C 3 HOH   120 520 208 HOH   HOH A . 
C 3 HOH   121 521 11  HOH   HOH A . 
C 3 HOH   122 522 238 HOH   HOH A . 
C 3 HOH   123 523 42  HOH   HOH A . 
C 3 HOH   124 524 9   HOH   HOH A . 
C 3 HOH   125 525 19  HOH   HOH A . 
C 3 HOH   126 526 229 HOH   HOH A . 
C 3 HOH   127 527 193 HOH   HOH A . 
C 3 HOH   128 528 93  HOH   HOH A . 
C 3 HOH   129 529 44  HOH   HOH A . 
C 3 HOH   130 530 206 HOH   HOH A . 
C 3 HOH   131 531 41  HOH   HOH A . 
C 3 HOH   132 532 121 HOH   HOH A . 
C 3 HOH   133 533 123 HOH   HOH A . 
C 3 HOH   134 534 65  HOH   HOH A . 
C 3 HOH   135 535 79  HOH   HOH A . 
C 3 HOH   136 536 45  HOH   HOH A . 
C 3 HOH   137 537 112 HOH   HOH A . 
C 3 HOH   138 538 15  HOH   HOH A . 
C 3 HOH   139 539 137 HOH   HOH A . 
C 3 HOH   140 540 135 HOH   HOH A . 
C 3 HOH   141 541 249 HOH   HOH A . 
C 3 HOH   142 542 165 HOH   HOH A . 
C 3 HOH   143 543 39  HOH   HOH A . 
C 3 HOH   144 544 74  HOH   HOH A . 
C 3 HOH   145 545 12  HOH   HOH A . 
C 3 HOH   146 546 245 HOH   HOH A . 
C 3 HOH   147 547 215 HOH   HOH A . 
C 3 HOH   148 548 75  HOH   HOH A . 
C 3 HOH   149 549 273 HOH   HOH A . 
C 3 HOH   150 550 119 HOH   HOH A . 
C 3 HOH   151 551 266 HOH   HOH A . 
C 3 HOH   152 552 37  HOH   HOH A . 
C 3 HOH   153 553 250 HOH   HOH A . 
C 3 HOH   154 554 56  HOH   HOH A . 
C 3 HOH   155 555 46  HOH   HOH A . 
C 3 HOH   156 556 129 HOH   HOH A . 
C 3 HOH   157 557 35  HOH   HOH A . 
C 3 HOH   158 558 218 HOH   HOH A . 
C 3 HOH   159 559 29  HOH   HOH A . 
C 3 HOH   160 560 78  HOH   HOH A . 
C 3 HOH   161 561 95  HOH   HOH A . 
C 3 HOH   162 562 86  HOH   HOH A . 
C 3 HOH   163 563 304 HOH   HOH A . 
C 3 HOH   164 564 128 HOH   HOH A . 
C 3 HOH   165 565 288 HOH   HOH A . 
C 3 HOH   166 566 132 HOH   HOH A . 
C 3 HOH   167 567 140 HOH   HOH A . 
C 3 HOH   168 568 254 HOH   HOH A . 
C 3 HOH   169 569 294 HOH   HOH A . 
C 3 HOH   170 570 51  HOH   HOH A . 
C 3 HOH   171 571 271 HOH   HOH A . 
C 3 HOH   172 572 67  HOH   HOH A . 
C 3 HOH   173 573 152 HOH   HOH A . 
C 3 HOH   174 574 58  HOH   HOH A . 
C 3 HOH   175 575 150 HOH   HOH A . 
C 3 HOH   176 576 227 HOH   HOH A . 
C 3 HOH   177 577 275 HOH   HOH A . 
C 3 HOH   178 578 225 HOH   HOH A . 
C 3 HOH   179 579 239 HOH   HOH A . 
C 3 HOH   180 580 126 HOH   HOH A . 
C 3 HOH   181 581 138 HOH   HOH A . 
C 3 HOH   182 582 255 HOH   HOH A . 
C 3 HOH   183 583 21  HOH   HOH A . 
C 3 HOH   184 584 180 HOH   HOH A . 
C 3 HOH   185 585 234 HOH   HOH A . 
C 3 HOH   186 586 300 HOH   HOH A . 
C 3 HOH   187 587 191 HOH   HOH A . 
C 3 HOH   188 588 295 HOH   HOH A . 
C 3 HOH   189 589 120 HOH   HOH A . 
C 3 HOH   190 590 219 HOH   HOH A . 
C 3 HOH   191 591 280 HOH   HOH A . 
C 3 HOH   192 592 243 HOH   HOH A . 
C 3 HOH   193 593 203 HOH   HOH A . 
C 3 HOH   194 594 63  HOH   HOH A . 
C 3 HOH   195 595 146 HOH   HOH A . 
C 3 HOH   196 596 124 HOH   HOH A . 
C 3 HOH   197 597 289 HOH   HOH A . 
C 3 HOH   198 598 187 HOH   HOH A . 
C 3 HOH   199 599 24  HOH   HOH A . 
C 3 HOH   200 600 293 HOH   HOH A . 
C 3 HOH   201 601 268 HOH   HOH A . 
C 3 HOH   202 602 285 HOH   HOH A . 
C 3 HOH   203 603 84  HOH   HOH A . 
C 3 HOH   204 604 155 HOH   HOH A . 
C 3 HOH   205 605 192 HOH   HOH A . 
C 3 HOH   206 606 117 HOH   HOH A . 
C 3 HOH   207 607 230 HOH   HOH A . 
C 3 HOH   208 608 283 HOH   HOH A . 
C 3 HOH   209 609 241 HOH   HOH A . 
C 3 HOH   210 610 163 HOH   HOH A . 
C 3 HOH   211 611 242 HOH   HOH A . 
C 3 HOH   212 612 201 HOH   HOH A . 
C 3 HOH   213 613 256 HOH   HOH A . 
C 3 HOH   214 614 259 HOH   HOH A . 
C 3 HOH   215 615 156 HOH   HOH A . 
C 3 HOH   216 616 118 HOH   HOH A . 
C 3 HOH   217 617 244 HOH   HOH A . 
C 3 HOH   218 618 14  HOH   HOH A . 
C 3 HOH   219 619 226 HOH   HOH A . 
C 3 HOH   220 620 211 HOH   HOH A . 
C 3 HOH   221 621 34  HOH   HOH A . 
C 3 HOH   222 622 305 HOH   HOH A . 
C 3 HOH   223 623 258 HOH   HOH A . 
C 3 HOH   224 624 246 HOH   HOH A . 
C 3 HOH   225 625 175 HOH   HOH A . 
C 3 HOH   226 626 105 HOH   HOH A . 
C 3 HOH   227 627 57  HOH   HOH A . 
C 3 HOH   228 628 200 HOH   HOH A . 
C 3 HOH   229 629 108 HOH   HOH A . 
C 3 HOH   230 630 220 HOH   HOH A . 
C 3 HOH   231 631 260 HOH   HOH A . 
C 3 HOH   232 632 50  HOH   HOH A . 
C 3 HOH   233 633 247 HOH   HOH A . 
C 3 HOH   234 634 181 HOH   HOH A . 
C 3 HOH   235 635 113 HOH   HOH A . 
C 3 HOH   236 636 232 HOH   HOH A . 
C 3 HOH   237 637 290 HOH   HOH A . 
C 3 HOH   238 638 170 HOH   HOH A . 
C 3 HOH   239 639 261 HOH   HOH A . 
C 3 HOH   240 640 202 HOH   HOH A . 
C 3 HOH   241 641 189 HOH   HOH A . 
C 3 HOH   242 642 145 HOH   HOH A . 
C 3 HOH   243 643 164 HOH   HOH A . 
C 3 HOH   244 644 299 HOH   HOH A . 
C 3 HOH   245 645 157 HOH   HOH A . 
C 3 HOH   246 646 278 HOH   HOH A . 
C 3 HOH   247 647 296 HOH   HOH A . 
C 3 HOH   248 648 160 HOH   HOH A . 
C 3 HOH   249 649 184 HOH   HOH A . 
C 3 HOH   250 650 274 HOH   HOH A . 
C 3 HOH   251 651 223 HOH   HOH A . 
C 3 HOH   252 652 49  HOH   HOH A . 
C 3 HOH   253 653 190 HOH   HOH A . 
C 3 HOH   254 654 282 HOH   HOH A . 
C 3 HOH   255 655 76  HOH   HOH A . 
C 3 HOH   256 656 217 HOH   HOH A . 
C 3 HOH   257 657 85  HOH   HOH A . 
C 3 HOH   258 658 142 HOH   HOH A . 
C 3 HOH   259 659 204 HOH   HOH A . 
C 3 HOH   260 660 148 HOH   HOH A . 
C 3 HOH   261 661 286 HOH   HOH A . 
C 3 HOH   262 662 115 HOH   HOH A . 
C 3 HOH   263 663 207 HOH   HOH A . 
C 3 HOH   264 664 173 HOH   HOH A . 
C 3 HOH   265 665 136 HOH   HOH A . 
C 3 HOH   266 666 279 HOH   HOH A . 
C 3 HOH   267 667 248 HOH   HOH A . 
C 3 HOH   268 668 236 HOH   HOH A . 
C 3 HOH   269 669 301 HOH   HOH A . 
C 3 HOH   270 670 196 HOH   HOH A . 
C 3 HOH   271 671 233 HOH   HOH A . 
C 3 HOH   272 672 154 HOH   HOH A . 
C 3 HOH   273 673 158 HOH   HOH A . 
C 3 HOH   274 674 88  HOH   HOH A . 
C 3 HOH   275 675 297 HOH   HOH A . 
C 3 HOH   276 676 214 HOH   HOH A . 
C 3 HOH   277 677 60  HOH   HOH A . 
C 3 HOH   278 678 287 HOH   HOH A . 
C 3 HOH   279 679 212 HOH   HOH A . 
C 3 HOH   280 680 94  HOH   HOH A . 
C 3 HOH   281 681 182 HOH   HOH A . 
C 3 HOH   282 682 171 HOH   HOH A . 
C 3 HOH   283 683 133 HOH   HOH A . 
C 3 HOH   284 684 302 HOH   HOH A . 
C 3 HOH   285 685 104 HOH   HOH A . 
C 3 HOH   286 686 197 HOH   HOH A . 
C 3 HOH   287 687 224 HOH   HOH A . 
C 3 HOH   288 688 186 HOH   HOH A . 
C 3 HOH   289 689 82  HOH   HOH A . 
C 3 HOH   290 690 222 HOH   HOH A . 
C 3 HOH   291 691 270 HOH   HOH A . 
C 3 HOH   292 692 144 HOH   HOH A . 
C 3 HOH   293 693 47  HOH   HOH A . 
C 3 HOH   294 694 149 HOH   HOH A . 
C 3 HOH   295 695 114 HOH   HOH A . 
C 3 HOH   296 696 116 HOH   HOH A . 
C 3 HOH   297 697 168 HOH   HOH A . 
C 3 HOH   298 698 272 HOH   HOH A . 
C 3 HOH   299 699 251 HOH   HOH A . 
C 3 HOH   300 700 166 HOH   HOH A . 
C 3 HOH   301 701 235 HOH   HOH A . 
C 3 HOH   302 702 237 HOH   HOH A . 
C 3 HOH   303 703 176 HOH   HOH A . 
C 3 HOH   304 704 199 HOH   HOH A . 
C 3 HOH   305 705 284 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             609572.309 
_cell.length_a           68.200 
_cell.length_b           90.640 
_cell.length_c           98.610 
_cell.angle_beta         90.000 
_cell.angle_gamma        90.000 
_cell.angle_alpha        90.000 
_cell.entry_id           7HB4 
_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                         7HB4 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
# 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
_exptl.entry_id          7HB4 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_Matthews      2.88 
_exptl_crystal.density_percent_sol   57.23 
_exptl_crystal.density_meas          ? 
_exptl_crystal.description           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.pH              8.5 
_exptl_crystal_grow.temp            277 
_exptl_crystal_grow.pdbx_details    '100mM Tris-HCl pH 8.5, 22% PEG4000, 200mM MgCl2' 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_diffrn.id                     1 
_diffrn.crystal_id             1 
_diffrn.ambient_temp           100 
_diffrn.ambient_temp_details   ? 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               PIXEL 
_diffrn_detector.type                   'DECTRIS EIGER2 S 9M' 
_diffrn_detector.pdbx_collection_date   2023-07-22 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.pdbx_scattering_type             x-ray 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.monochromator                    Si111 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.97918 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.pdbx_synchrotron_beamline   BL02U1 
_diffrn_source.type                        'SSRF BEAMLINE BL02U1' 
_diffrn_source.pdbx_wavelength_list        0.97918 
_diffrn_source.pdbx_synchrotron_site       SSRF 
_diffrn_source.pdbx_wavelength             ? 
# 
_reflns.entry_id                     7HB4 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             29.610 
_reflns.d_resolution_high            1.870 
_reflns.number_obs                   25385 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         99.100 
_reflns.pdbx_Rmerge_I_obs            0.121 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        19.000 
_reflns.B_iso_Wilson_estimate        ? 
_reflns.pdbx_redundancy              11.200 
_reflns.pdbx_Rrim_I_all              0.127 
_reflns.pdbx_Rpim_I_all              0.037 
_reflns.pdbx_CC_half                 0.998 
_reflns.pdbx_netI_over_av_sigmaI     ? 
_reflns.pdbx_number_measured_all     284683 
_reflns.pdbx_scaling_rejects         2113 
_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 1.870 1.920  ? 9345 1694 ? 0.859 ? ? ? 5.500  ? 2.500  ? ? ? ? ? ? 91.600 0.952 0.395 0.740 
1 2 8.360 29.610 ? 3550 321  ? 0.044 ? ? ? 11.100 ? 41.900 ? ? ? ? ? ? 97.200 0.046 0.014 0.998 
# 
_refine.entry_id                                 7HB4 
_refine.pdbx_method_to_determine_struct          'FOURIER SYNTHESIS' 
_refine.ls_percent_reflns_R_free                 5.13 
_refine.pdbx_overall_phase_error                 18.6183 
_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                          0.1643 
_refine.B_iso_mean                               28.69 
_refine.ls_number_reflns_R_free                  1302 
_refine.ls_percent_reflns_obs                    98.99 
_refine.ls_R_factor_R_work                       0.1630 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_refine.ls_d_res_high                            1.87 
_refine.ls_number_reflns_obs                     25378 
_refine.pdbx_ls_sigma_F                          1.34 
_refine.ls_number_reflns_R_work                  24076 
_refine.ls_d_res_low                             29.61 
_refine.pdbx_stereochemistry_target_values       'GeoStd + Monomer Library + CDL v1.2' 
_refine.ls_R_factor_R_free                       0.1884 
_refine.overall_SU_ML                            0.2069 
_refine.pdbx_solvent_vdw_probe_radii             1.1000 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.solvent_model_param_ksol                 ? 
_refine.solvent_model_param_bsol                 ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.details                                  ? 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.overall_SU_B                             ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        1644 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         11 
_refine_hist.number_atoms_solvent             305 
_refine_hist.number_atoms_total               1960 
_refine_hist.d_res_high                       1.87 
_refine_hist.d_res_low                        29.61 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.type 
_refine_ls_restr.number 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
_refine_ls_restr.dev_ideal_target 
'X-RAY DIFFRACTION' f_bond_d           1681 0.0114 ? ? ? 
'X-RAY DIFFRACTION' f_angle_d          2265 1.1099 ? ? ? 
'X-RAY DIFFRACTION' f_chiral_restr     259  0.0683 ? ? ? 
'X-RAY DIFFRACTION' f_plane_restr      289  0.0085 ? ? ? 
'X-RAY DIFFRACTION' f_dihedral_angle_d 224  6.7599 ? ? ? 
# 
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' 1.87 1.94  2429 0.2787 92.16  0.3162 146 . . . . . 
'X-RAY DIFFRACTION' 1.94 2.03  2672 0.2097 99.05  0.2336 140 . . . . . 
'X-RAY DIFFRACTION' 2.03 2.14  2642 0.1750 99.93  0.2135 151 . . . . . 
'X-RAY DIFFRACTION' 2.14 2.27  2689 0.1563 100.00 0.1643 141 . . . . . 
'X-RAY DIFFRACTION' 2.27 2.45  2686 0.1632 100.00 0.1744 128 . . . . . 
'X-RAY DIFFRACTION' 2.45 2.70  2691 0.1691 99.93  0.2094 137 . . . . . 
'X-RAY DIFFRACTION' 2.70 3.09  2681 0.1701 100.00 0.2125 169 . . . . . 
'X-RAY DIFFRACTION' 3.09 3.89  2748 0.1467 99.97  0.1841 135 . . . . . 
'X-RAY DIFFRACTION' 3.89 29.61 2838 0.1436 99.77  0.1487 155 . . . . . 
# 
_struct.entry_id                  7HB4 
_struct.title                     'PanDDA analysis group deposition -- Crystal structure of HSP90N in complex with Fr14472' 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_details        ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HB4 
_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              7HB4 
_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 7HB4 MET A 1   ? UNP P07900 ? ? 'initiating methionine' 8   1 
1 7HB4 LEU A 230 ? UNP P07900 ? ? 'expression tag'        237 2 
1 7HB4 GLU A 231 ? UNP P07900 ? ? 'expression tag'        238 3 
1 7HB4 HIS A 232 ? UNP P07900 ? ? 'expression tag'        239 4 
1 7HB4 HIS A 233 ? UNP P07900 ? ? 'expression tag'        240 5 
1 7HB4 HIS A 234 ? UNP P07900 ? ? 'expression tag'        241 6 
1 7HB4 HIS A 235 ? UNP P07900 ? ? 'expression tag'        242 7 
1 7HB4 HIS A 236 ? UNP P07900 ? ? 'expression tag'        243 8 
1 7HB4 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 VAL A 10  ? ALA A 14  ? VAL A 17  ALA A 21  
AA1 2 SER A 162 ? THR A 167 ? SER A 169 THR A 174 
AA1 3 TYR A 153 ? SER A 157 ? TYR A 160 SER A 164 
AA1 4 ALA A 138 ? LYS A 146 ? ALA A 145 LYS A 153 
AA1 5 GLY A 176 ? LEU A 183 ? GLY A 183 LEU A 190 
AA1 6 THR A 81  ? ASP A 86  ? THR A 88  ASP A 93  
AA1 7 ILE A 71  ? ASN A 76  ? ILE A 78  ASN A 83  
AA1 8 ILE A 211 ? LEU A 213 ? ILE A 218 LEU A 220 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N PHE A 13  ? N PHE A 20  O PHE A 163 ? O PHE A 170 
AA1 2 3 O ARG A 166 ? O ARG A 173 N ALA A 154 ? N ALA A 161 
AA1 3 4 O TRP A 155 ? O TRP A 162 N VAL A 143 ? N VAL A 150 
AA1 4 5 N THR A 142 ? N THR A 149 O ILE A 180 ? O ILE A 187 
AA1 5 6 O VAL A 179 ? O VAL A 186 N ILE A 84  ? N ILE A 91  
AA1 6 7 O THR A 83  ? O THR A 90  N ILE A 74  ? N ILE A 81  
AA1 7 8 N LEU A 73  ? N LEU A 80  O THR A 212 ? O THR A 219 
# 
_pdbx_entry_details.entry_id                   7HB4 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1  1 O   A HOH 620 ? ? O A HOH 640 ? ? 1.91 
2  1 O   A HOH 536 ? ? O A HOH 604 ? ? 2.05 
3  1 O   A HOH 577 ? ? O A HOH 698 ? ? 2.06 
4  1 OG  A SER 113 ? ? O A HOH 401 ? ? 2.06 
5  1 O   A HOH 609 ? ? O A HOH 611 ? ? 2.07 
6  1 O   A HOH 674 ? ? O A HOH 685 ? ? 2.12 
7  1 O   A HOH 598 ? ? O A HOH 670 ? ? 2.13 
8  1 O   A HOH 469 ? ? O A HOH 591 ? ? 2.15 
9  1 O   A HOH 666 ? ? O A HOH 678 ? ? 2.18 
10 1 OH  A TYR 160 ? ? O A HOH 402 ? ? 2.19 
11 1 O   A LYS 224 ? ? O A HOH 403 ? ? 2.19 
12 1 OE1 A GLU 178 ? ? O A HOH 404 ? ? 2.19 
# 
_pdbx_validate_rmsd_bond.id                        1 
_pdbx_validate_rmsd_bond.PDB_model_num             1 
_pdbx_validate_rmsd_bond.auth_atom_id_1            CB 
_pdbx_validate_rmsd_bond.auth_asym_id_1            A 
_pdbx_validate_rmsd_bond.auth_comp_id_1            VAL 
_pdbx_validate_rmsd_bond.auth_seq_id_1             222 
_pdbx_validate_rmsd_bond.PDB_ins_code_1            ? 
_pdbx_validate_rmsd_bond.label_alt_id_1            ? 
_pdbx_validate_rmsd_bond.auth_atom_id_2            CG2 
_pdbx_validate_rmsd_bond.auth_asym_id_2            A 
_pdbx_validate_rmsd_bond.auth_comp_id_2            VAL 
_pdbx_validate_rmsd_bond.auth_seq_id_2             222 
_pdbx_validate_rmsd_bond.PDB_ins_code_2            ? 
_pdbx_validate_rmsd_bond.label_alt_id_2            ? 
_pdbx_validate_rmsd_bond.bond_value                1.396 
_pdbx_validate_rmsd_bond.bond_target_value         1.524 
_pdbx_validate_rmsd_bond.bond_deviation            -0.128 
_pdbx_validate_rmsd_bond.bond_standard_deviation   0.021 
_pdbx_validate_rmsd_bond.linker_flag               N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ALA A 166 ? ? 65.01   -142.27 
2 1 ARG A 182 ? ? -172.57 137.55  
# 
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 13.5232908552  -17.8545234825 -17.9148139573 0.175138815662 0.200215667507 0.22325466902  
0.0138264521354  -0.0455159855687  -0.00332372899145 2.13036721866 1.82325043351 7.24427551441 -1.14017447028 -2.27057576284  
0.970629121296  -0.0548709293243   -0.199458966095   0.0012099835712  0.146184686501  -0.00439923874382 -0.073284973121   
0.0612709871204  0.48517532328    -0.0189656350769 
2  ? 'X-RAY DIFFRACTION' refined -4.06112218602 -6.60178741228 -21.5775753179 0.128124110363 0.136428570032 0.150119811291 
-0.013527436178  -0.010147859164   -0.0216034948967  2.37454131334 4.1461635973  7.84893958684 -2.32465093878 2.88087984842   
-4.22905488243  -0.135917232287    0.109489233425    0.108487696163   0.199411292518  -0.0776541740335  -0.0524596333234  
-0.432590416705  0.0790209162643  0.237132235699   
3  ? 'X-RAY DIFFRACTION' refined -9.68223385122 -16.4854309989 -24.7542054514 0.170384578768 0.16813908877  0.181771145893 
-0.022005713001  -0.0333466837569  -0.0522771580023  2.02429356801 4.57028262903 5.37021406855 -1.3818926505  0.846128325933  
-3.08956848015  0.0793442781928    0.147650568576    -0.189081594703  -0.290073296155 0.0102710231566   0.355985752116    
0.255894238424   -0.108062881589  -0.161440310275  
4  ? 'X-RAY DIFFRACTION' refined 3.5980965672   -12.1661592546 -32.1591028004 0.197094625601 0.166375869186 0.157087807023 
0.0115554803575  -0.0105188050778  -0.0346709997814  8.28350105385 4.58319815518 3.67271888496 -2.35823173933 -2.0109359738   
0.660004942385  0.165799592707     0.215665070105    0.212360044684   -0.265622597797 0.00387965116378  -0.349942519009   
-0.0710164487425 0.18036482439    -0.191239276227  
5  ? 'X-RAY DIFFRACTION' refined 15.2209911659  -6.42076413941 -18.1219166337 0.138364851284 0.237449334263 0.262021362219 
0.0191841148131  -0.0156538492629  -0.0079616163448  2.98427102208 3.18432479998 2.11671228984 0.768529667414 -0.466070502708 
1.37755456376   0.0126406620802    -0.00060503868329 0.0798276991141  0.204115723182  -0.0109346673737  -0.382443650223   
0.228986741331   1.00292675231    0.0136124401567  
6  ? 'X-RAY DIFFRACTION' refined 6.07978775355  -13.7556756372 -16.1898031456 0.120706166297 0.154723914388 0.125600779556 
0.0226413219919  -0.00219165841053 -0.0166191021162  2.62396575654 1.86309698152 2.5502239186  0.254480987761 0.352881300624  
-0.363080406751 0.0662001699459    -0.215782777552   0.0682991177012  0.189455012126  -0.103285734169   -0.00544317453364 
0.144029256153   0.117871097543   -0.0110528501678 
7  ? 'X-RAY DIFFRACTION' refined 1.54839805289  -17.2294952515 -33.7677049918 0.236221968892 0.234828323076 0.180626272282 
0.00651025019152 0.000486676751558 -0.0432046773516  4.44315769094 3.52365574035 4.67345582644 -2.14024322118 1.78453991906   
-1.54759606558  0.288339437619     0.408745454035    -0.18670161215   -0.474063982822 -0.141117916578   0.0899840199631   
0.277356878663   0.0375538349851  -0.0697600364778 
8  ? 'X-RAY DIFFRACTION' refined 0.949771207793 -21.9620282342 -27.7201931638 0.230699883264 0.190359721797 0.222659973563 
-0.0143986418071 -0.0270433038673  -0.0528023059733  2.1092350285  1.95073761224 2.09002232413 -1.00500497559 -0.821691093498 
-0.571083070163 -0.000539228071564 0.255683635639    -0.338310990617  -0.175426015268 -0.0411879359712  0.210036067535    
0.284455877931   -0.0714188216966 -0.0288472087397 
9  ? 'X-RAY DIFFRACTION' refined -5.92358802763 -19.6362121799 -6.93878579231 0.236299094559 0.222225305007 0.193630986805 
-0.030425221181  -0.00636306619992 0.030329829098    5.22319500906 3.75265475158 3.88816623157 -1.76960232527 -0.513697207312 
-0.131605635341 -0.0317295059225   -0.2661087        -0.364021932145  0.189168633627  -0.0654923503486  0.112909217816    
0.322409939247   -0.149990931544  0.0565877951365  
10 ? 'X-RAY DIFFRACTION' refined -13.273714349  -13.5133963431 -15.7039533202 0.130213584449 0.215496403319 0.155315278605 
0.0170553566836  0.00639584938677  0.00521836952302  3.47777386945 5.87596247844 3.34079575777 1.24378493047  0.441735748453  
-0.689797166359 0.0550712858178    -0.264501606478   -0.0717188674977 0.231087604766  -0.0729994297111  0.282536737424    
-0.0430619325519 -0.16689304983   -0.0309327269264 
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
1  1  'X-RAY DIFFRACTION' A 16  A 1   A 40  A 25  . 
;chain 'A' and (resid 16 through 40 )
;
2  2  'X-RAY DIFFRACTION' A 41  A 26  A 65  A 50  . 
;chain 'A' and (resid 41 through 65 )
;
3  3  'X-RAY DIFFRACTION' A 66  A 51  A 93  A 78  . 
;chain 'A' and (resid 66 through 93 )
;
4  4  'X-RAY DIFFRACTION' A 94  A 79  A 105 A 90  . 
;chain 'A' and (resid 94 through 105 )
;
5  5  'X-RAY DIFFRACTION' A 106 A 91  A 123 A 108 . 
;chain 'A' and (resid 106 through 123 )
;
6  6  'X-RAY DIFFRACTION' A 124 A 109 A 153 A 138 . 
;chain 'A' and (resid 124 through 153 )
;
7  7  'X-RAY DIFFRACTION' A 154 A 139 A 164 A 149 . 
;chain 'A' and (resid 154 through 164 )
;
8  8  'X-RAY DIFFRACTION' A 165 A 150 A 190 A 175 . 
;chain 'A' and (resid 165 through 190 )
;
9  9  'X-RAY DIFFRACTION' A 191 A 176 A 210 A 195 . 
;chain 'A' and (resid 191 through 210 )
;
10 10 '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 
A1AXV N1   N N N 1   
A1AXV C4   C Y N 2   
A1AXV C5   C Y N 3   
A1AXV C6   C Y N 4   
A1AXV C7   C N N 5   
A1AXV C8   C Y N 6   
A1AXV C1   C N N 7   
A1AXV C2   C Y N 8   
A1AXV C3   C Y N 9   
A1AXV N2   N N N 10  
A1AXV S1   S N N 11  
A1AXV H7   H N N 12  
A1AXV H5   H N N 13  
A1AXV H6   H N N 14  
A1AXV H10  H N N 15  
A1AXV H3   H N N 16  
A1AXV H2   H N N 17  
A1AXV H1   H N N 18  
A1AXV H4   H N N 19  
A1AXV H9   H N N 20  
A1AXV H8   H N N 21  
ALA   N    N N N 22  
ALA   CA   C N S 23  
ALA   C    C N N 24  
ALA   O    O N N 25  
ALA   CB   C N N 26  
ALA   OXT  O N N 27  
ALA   H    H N N 28  
ALA   H2   H N N 29  
ALA   HA   H N N 30  
ALA   HB1  H N N 31  
ALA   HB2  H N N 32  
ALA   HB3  H N N 33  
ALA   HXT  H N N 34  
ARG   N    N N N 35  
ARG   CA   C N S 36  
ARG   C    C N N 37  
ARG   O    O N N 38  
ARG   CB   C N N 39  
ARG   CG   C N N 40  
ARG   CD   C N N 41  
ARG   NE   N N N 42  
ARG   CZ   C N N 43  
ARG   NH1  N N N 44  
ARG   NH2  N N N 45  
ARG   OXT  O N N 46  
ARG   H    H N N 47  
ARG   H2   H N N 48  
ARG   HA   H N N 49  
ARG   HB2  H N N 50  
ARG   HB3  H N N 51  
ARG   HG2  H N N 52  
ARG   HG3  H N N 53  
ARG   HD2  H N N 54  
ARG   HD3  H N N 55  
ARG   HE   H N N 56  
ARG   HH11 H N N 57  
ARG   HH12 H N N 58  
ARG   HH21 H N N 59  
ARG   HH22 H N N 60  
ARG   HXT  H N N 61  
ASN   N    N N N 62  
ASN   CA   C N S 63  
ASN   C    C N N 64  
ASN   O    O N N 65  
ASN   CB   C N N 66  
ASN   CG   C N N 67  
ASN   OD1  O N N 68  
ASN   ND2  N N N 69  
ASN   OXT  O N N 70  
ASN   H    H N N 71  
ASN   H2   H N N 72  
ASN   HA   H N N 73  
ASN   HB2  H N N 74  
ASN   HB3  H N N 75  
ASN   HD21 H N N 76  
ASN   HD22 H N N 77  
ASN   HXT  H N N 78  
ASP   N    N N N 79  
ASP   CA   C N S 80  
ASP   C    C N N 81  
ASP   O    O N N 82  
ASP   CB   C N N 83  
ASP   CG   C N N 84  
ASP   OD1  O N N 85  
ASP   OD2  O N N 86  
ASP   OXT  O N N 87  
ASP   H    H N N 88  
ASP   H2   H N N 89  
ASP   HA   H N N 90  
ASP   HB2  H N N 91  
ASP   HB3  H N N 92  
ASP   HD2  H N N 93  
ASP   HXT  H N N 94  
GLN   N    N N N 95  
GLN   CA   C N S 96  
GLN   C    C N N 97  
GLN   O    O N N 98  
GLN   CB   C N N 99  
GLN   CG   C N N 100 
GLN   CD   C N N 101 
GLN   OE1  O N N 102 
GLN   NE2  N N N 103 
GLN   OXT  O N N 104 
GLN   H    H N N 105 
GLN   H2   H N N 106 
GLN   HA   H N N 107 
GLN   HB2  H N N 108 
GLN   HB3  H N N 109 
GLN   HG2  H N N 110 
GLN   HG3  H N N 111 
GLN   HE21 H N N 112 
GLN   HE22 H N N 113 
GLN   HXT  H N N 114 
GLU   N    N N N 115 
GLU   CA   C N S 116 
GLU   C    C N N 117 
GLU   O    O N N 118 
GLU   CB   C N N 119 
GLU   CG   C N N 120 
GLU   CD   C N N 121 
GLU   OE1  O N N 122 
GLU   OE2  O N N 123 
GLU   OXT  O N N 124 
GLU   H    H N N 125 
GLU   H2   H N N 126 
GLU   HA   H N N 127 
GLU   HB2  H N N 128 
GLU   HB3  H N N 129 
GLU   HG2  H N N 130 
GLU   HG3  H N N 131 
GLU   HE2  H N N 132 
GLU   HXT  H N N 133 
GLY   N    N N N 134 
GLY   CA   C N N 135 
GLY   C    C N N 136 
GLY   O    O N N 137 
GLY   OXT  O N N 138 
GLY   H    H N N 139 
GLY   H2   H N N 140 
GLY   HA2  H N N 141 
GLY   HA3  H N N 142 
GLY   HXT  H N N 143 
HIS   N    N N N 144 
HIS   CA   C N S 145 
HIS   C    C N N 146 
HIS   O    O N N 147 
HIS   CB   C N N 148 
HIS   CG   C Y N 149 
HIS   ND1  N Y N 150 
HIS   CD2  C Y N 151 
HIS   CE1  C Y N 152 
HIS   NE2  N Y N 153 
HIS   OXT  O N N 154 
HIS   H    H N N 155 
HIS   H2   H N N 156 
HIS   HA   H N N 157 
HIS   HB2  H N N 158 
HIS   HB3  H N N 159 
HIS   HD1  H N N 160 
HIS   HD2  H N N 161 
HIS   HE1  H N N 162 
HIS   HE2  H N N 163 
HIS   HXT  H N N 164 
HOH   O    O N N 165 
HOH   H1   H N N 166 
HOH   H2   H N N 167 
ILE   N    N N N 168 
ILE   CA   C N S 169 
ILE   C    C N N 170 
ILE   O    O N N 171 
ILE   CB   C N S 172 
ILE   CG1  C N N 173 
ILE   CG2  C N N 174 
ILE   CD1  C N N 175 
ILE   OXT  O N N 176 
ILE   H    H N N 177 
ILE   H2   H N N 178 
ILE   HA   H N N 179 
ILE   HB   H N N 180 
ILE   HG12 H N N 181 
ILE   HG13 H N N 182 
ILE   HG21 H N N 183 
ILE   HG22 H N N 184 
ILE   HG23 H N N 185 
ILE   HD11 H N N 186 
ILE   HD12 H N N 187 
ILE   HD13 H N N 188 
ILE   HXT  H N N 189 
LEU   N    N N N 190 
LEU   CA   C N S 191 
LEU   C    C N N 192 
LEU   O    O N N 193 
LEU   CB   C N N 194 
LEU   CG   C N N 195 
LEU   CD1  C N N 196 
LEU   CD2  C N N 197 
LEU   OXT  O N N 198 
LEU   H    H N N 199 
LEU   H2   H N N 200 
LEU   HA   H N N 201 
LEU   HB2  H N N 202 
LEU   HB3  H N N 203 
LEU   HG   H N N 204 
LEU   HD11 H N N 205 
LEU   HD12 H N N 206 
LEU   HD13 H N N 207 
LEU   HD21 H N N 208 
LEU   HD22 H N N 209 
LEU   HD23 H N N 210 
LEU   HXT  H N N 211 
LYS   N    N N N 212 
LYS   CA   C N S 213 
LYS   C    C N N 214 
LYS   O    O N N 215 
LYS   CB   C N N 216 
LYS   CG   C N N 217 
LYS   CD   C N N 218 
LYS   CE   C N N 219 
LYS   NZ   N N N 220 
LYS   OXT  O N N 221 
LYS   H    H N N 222 
LYS   H2   H N N 223 
LYS   HA   H N N 224 
LYS   HB2  H N N 225 
LYS   HB3  H N N 226 
LYS   HG2  H N N 227 
LYS   HG3  H N N 228 
LYS   HD2  H N N 229 
LYS   HD3  H N N 230 
LYS   HE2  H N N 231 
LYS   HE3  H N N 232 
LYS   HZ1  H N N 233 
LYS   HZ2  H N N 234 
LYS   HZ3  H N N 235 
LYS   HXT  H N N 236 
MET   N    N N N 237 
MET   CA   C N S 238 
MET   C    C N N 239 
MET   O    O N N 240 
MET   CB   C N N 241 
MET   CG   C N N 242 
MET   SD   S N N 243 
MET   CE   C N N 244 
MET   OXT  O N N 245 
MET   H    H N N 246 
MET   H2   H N N 247 
MET   HA   H N N 248 
MET   HB2  H N N 249 
MET   HB3  H N N 250 
MET   HG2  H N N 251 
MET   HG3  H N N 252 
MET   HE1  H N N 253 
MET   HE2  H N N 254 
MET   HE3  H N N 255 
MET   HXT  H N N 256 
PHE   N    N N N 257 
PHE   CA   C N S 258 
PHE   C    C N N 259 
PHE   O    O N N 260 
PHE   CB   C N N 261 
PHE   CG   C Y N 262 
PHE   CD1  C Y N 263 
PHE   CD2  C Y N 264 
PHE   CE1  C Y N 265 
PHE   CE2  C Y N 266 
PHE   CZ   C Y N 267 
PHE   OXT  O N N 268 
PHE   H    H N N 269 
PHE   H2   H N N 270 
PHE   HA   H N N 271 
PHE   HB2  H N N 272 
PHE   HB3  H N N 273 
PHE   HD1  H N N 274 
PHE   HD2  H N N 275 
PHE   HE1  H N N 276 
PHE   HE2  H N N 277 
PHE   HZ   H N N 278 
PHE   HXT  H N N 279 
PRO   N    N N N 280 
PRO   CA   C N S 281 
PRO   C    C N N 282 
PRO   O    O N N 283 
PRO   CB   C N N 284 
PRO   CG   C N N 285 
PRO   CD   C N N 286 
PRO   OXT  O N N 287 
PRO   H    H N N 288 
PRO   HA   H N N 289 
PRO   HB2  H N N 290 
PRO   HB3  H N N 291 
PRO   HG2  H N N 292 
PRO   HG3  H N N 293 
PRO   HD2  H N N 294 
PRO   HD3  H N N 295 
PRO   HXT  H N N 296 
SER   N    N N N 297 
SER   CA   C N S 298 
SER   C    C N N 299 
SER   O    O N N 300 
SER   CB   C N N 301 
SER   OG   O N N 302 
SER   OXT  O N N 303 
SER   H    H N N 304 
SER   H2   H N N 305 
SER   HA   H N N 306 
SER   HB2  H N N 307 
SER   HB3  H N N 308 
SER   HG   H N N 309 
SER   HXT  H N N 310 
THR   N    N N N 311 
THR   CA   C N S 312 
THR   C    C N N 313 
THR   O    O N N 314 
THR   CB   C N R 315 
THR   OG1  O N N 316 
THR   CG2  C N N 317 
THR   OXT  O N N 318 
THR   H    H N N 319 
THR   H2   H N N 320 
THR   HA   H N N 321 
THR   HB   H N N 322 
THR   HG1  H N N 323 
THR   HG21 H N N 324 
THR   HG22 H N N 325 
THR   HG23 H N N 326 
THR   HXT  H N N 327 
TRP   N    N N N 328 
TRP   CA   C N S 329 
TRP   C    C N N 330 
TRP   O    O N N 331 
TRP   CB   C N N 332 
TRP   CG   C Y N 333 
TRP   CD1  C Y N 334 
TRP   CD2  C Y N 335 
TRP   NE1  N Y N 336 
TRP   CE2  C Y N 337 
TRP   CE3  C Y N 338 
TRP   CZ2  C Y N 339 
TRP   CZ3  C Y N 340 
TRP   CH2  C Y N 341 
TRP   OXT  O N N 342 
TRP   H    H N N 343 
TRP   H2   H N N 344 
TRP   HA   H N N 345 
TRP   HB2  H N N 346 
TRP   HB3  H N N 347 
TRP   HD1  H N N 348 
TRP   HE1  H N N 349 
TRP   HE3  H N N 350 
TRP   HZ2  H N N 351 
TRP   HZ3  H N N 352 
TRP   HH2  H N N 353 
TRP   HXT  H N N 354 
TYR   N    N N N 355 
TYR   CA   C N S 356 
TYR   C    C N N 357 
TYR   O    O N N 358 
TYR   CB   C N N 359 
TYR   CG   C Y N 360 
TYR   CD1  C Y N 361 
TYR   CD2  C Y N 362 
TYR   CE1  C Y N 363 
TYR   CE2  C Y N 364 
TYR   CZ   C Y N 365 
TYR   OH   O N N 366 
TYR   OXT  O N N 367 
TYR   H    H N N 368 
TYR   H2   H N N 369 
TYR   HA   H N N 370 
TYR   HB2  H N N 371 
TYR   HB3  H N N 372 
TYR   HD1  H N N 373 
TYR   HD2  H N N 374 
TYR   HE1  H N N 375 
TYR   HE2  H N N 376 
TYR   HH   H N N 377 
TYR   HXT  H N N 378 
VAL   N    N N N 379 
VAL   CA   C N S 380 
VAL   C    C N N 381 
VAL   O    O N N 382 
VAL   CB   C N N 383 
VAL   CG1  C N N 384 
VAL   CG2  C N N 385 
VAL   OXT  O N N 386 
VAL   H    H N N 387 
VAL   H2   H N N 388 
VAL   HA   H N N 389 
VAL   HB   H N N 390 
VAL   HG11 H N N 391 
VAL   HG12 H N N 392 
VAL   HG13 H N N 393 
VAL   HG21 H N N 394 
VAL   HG22 H N N 395 
VAL   HG23 H N N 396 
VAL   HXT  H N N 397 
# 
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 
A1AXV C1  C2   sing N N 1   
A1AXV C2  C3   doub Y N 2   
A1AXV C3  C4   sing Y N 3   
A1AXV C4  C5   doub Y N 4   
A1AXV C5  C6   sing Y N 5   
A1AXV C6  N1   sing N N 6   
A1AXV N1  C7   sing N N 7   
A1AXV C7  N2   sing N N 8   
A1AXV C7  S1   doub N N 9   
A1AXV C6  C8   doub Y N 10  
A1AXV C2  C8   sing Y N 11  
A1AXV N1  H7   sing N N 12  
A1AXV C4  H5   sing N N 13  
A1AXV C5  H6   sing N N 14  
A1AXV C8  H10  sing N N 15  
A1AXV C1  H3   sing N N 16  
A1AXV C1  H2   sing N N 17  
A1AXV C1  H1   sing N N 18  
A1AXV C3  H4   sing N N 19  
A1AXV N2  H9   sing N N 20  
A1AXV N2  H8   sing N N 21  
ALA   N   CA   sing N N 22  
ALA   N   H    sing N N 23  
ALA   N   H2   sing N N 24  
ALA   CA  C    sing N N 25  
ALA   CA  CB   sing N N 26  
ALA   CA  HA   sing N N 27  
ALA   C   O    doub N N 28  
ALA   C   OXT  sing N N 29  
ALA   CB  HB1  sing N N 30  
ALA   CB  HB2  sing N N 31  
ALA   CB  HB3  sing N N 32  
ALA   OXT HXT  sing N N 33  
ARG   N   CA   sing N N 34  
ARG   N   H    sing N N 35  
ARG   N   H2   sing N N 36  
ARG   CA  C    sing N N 37  
ARG   CA  CB   sing N N 38  
ARG   CA  HA   sing N N 39  
ARG   C   O    doub N N 40  
ARG   C   OXT  sing N N 41  
ARG   CB  CG   sing N N 42  
ARG   CB  HB2  sing N N 43  
ARG   CB  HB3  sing N N 44  
ARG   CG  CD   sing N N 45  
ARG   CG  HG2  sing N N 46  
ARG   CG  HG3  sing N N 47  
ARG   CD  NE   sing N N 48  
ARG   CD  HD2  sing N N 49  
ARG   CD  HD3  sing N N 50  
ARG   NE  CZ   sing N N 51  
ARG   NE  HE   sing N N 52  
ARG   CZ  NH1  sing N N 53  
ARG   CZ  NH2  doub N N 54  
ARG   NH1 HH11 sing N N 55  
ARG   NH1 HH12 sing N N 56  
ARG   NH2 HH21 sing N N 57  
ARG   NH2 HH22 sing N N 58  
ARG   OXT HXT  sing N N 59  
ASN   N   CA   sing N N 60  
ASN   N   H    sing N N 61  
ASN   N   H2   sing N N 62  
ASN   CA  C    sing N N 63  
ASN   CA  CB   sing N N 64  
ASN   CA  HA   sing N N 65  
ASN   C   O    doub N N 66  
ASN   C   OXT  sing N N 67  
ASN   CB  CG   sing N N 68  
ASN   CB  HB2  sing N N 69  
ASN   CB  HB3  sing N N 70  
ASN   CG  OD1  doub N N 71  
ASN   CG  ND2  sing N N 72  
ASN   ND2 HD21 sing N N 73  
ASN   ND2 HD22 sing N N 74  
ASN   OXT HXT  sing N N 75  
ASP   N   CA   sing N N 76  
ASP   N   H    sing N N 77  
ASP   N   H2   sing N N 78  
ASP   CA  C    sing N N 79  
ASP   CA  CB   sing N N 80  
ASP   CA  HA   sing N N 81  
ASP   C   O    doub N N 82  
ASP   C   OXT  sing N N 83  
ASP   CB  CG   sing N N 84  
ASP   CB  HB2  sing N N 85  
ASP   CB  HB3  sing N N 86  
ASP   CG  OD1  doub N N 87  
ASP   CG  OD2  sing N N 88  
ASP   OD2 HD2  sing N N 89  
ASP   OXT HXT  sing N N 90  
GLN   N   CA   sing N N 91  
GLN   N   H    sing N N 92  
GLN   N   H2   sing N N 93  
GLN   CA  C    sing N N 94  
GLN   CA  CB   sing N N 95  
GLN   CA  HA   sing N N 96  
GLN   C   O    doub N N 97  
GLN   C   OXT  sing N N 98  
GLN   CB  CG   sing N N 99  
GLN   CB  HB2  sing N N 100 
GLN   CB  HB3  sing N N 101 
GLN   CG  CD   sing N N 102 
GLN   CG  HG2  sing N N 103 
GLN   CG  HG3  sing N N 104 
GLN   CD  OE1  doub N N 105 
GLN   CD  NE2  sing N N 106 
GLN   NE2 HE21 sing N N 107 
GLN   NE2 HE22 sing N N 108 
GLN   OXT HXT  sing N N 109 
GLU   N   CA   sing N N 110 
GLU   N   H    sing N N 111 
GLU   N   H2   sing N N 112 
GLU   CA  C    sing N N 113 
GLU   CA  CB   sing N N 114 
GLU   CA  HA   sing N N 115 
GLU   C   O    doub N N 116 
GLU   C   OXT  sing N N 117 
GLU   CB  CG   sing N N 118 
GLU   CB  HB2  sing N N 119 
GLU   CB  HB3  sing N N 120 
GLU   CG  CD   sing N N 121 
GLU   CG  HG2  sing N N 122 
GLU   CG  HG3  sing N N 123 
GLU   CD  OE1  doub N N 124 
GLU   CD  OE2  sing N N 125 
GLU   OE2 HE2  sing N N 126 
GLU   OXT HXT  sing N N 127 
GLY   N   CA   sing N N 128 
GLY   N   H    sing N N 129 
GLY   N   H2   sing N N 130 
GLY   CA  C    sing N N 131 
GLY   CA  HA2  sing N N 132 
GLY   CA  HA3  sing N N 133 
GLY   C   O    doub N N 134 
GLY   C   OXT  sing N N 135 
GLY   OXT HXT  sing N N 136 
HIS   N   CA   sing N N 137 
HIS   N   H    sing N N 138 
HIS   N   H2   sing N N 139 
HIS   CA  C    sing N N 140 
HIS   CA  CB   sing N N 141 
HIS   CA  HA   sing N N 142 
HIS   C   O    doub N N 143 
HIS   C   OXT  sing N N 144 
HIS   CB  CG   sing N N 145 
HIS   CB  HB2  sing N N 146 
HIS   CB  HB3  sing N N 147 
HIS   CG  ND1  sing Y N 148 
HIS   CG  CD2  doub Y N 149 
HIS   ND1 CE1  doub Y N 150 
HIS   ND1 HD1  sing N N 151 
HIS   CD2 NE2  sing Y N 152 
HIS   CD2 HD2  sing N N 153 
HIS   CE1 NE2  sing Y N 154 
HIS   CE1 HE1  sing N N 155 
HIS   NE2 HE2  sing N N 156 
HIS   OXT HXT  sing N N 157 
HOH   O   H1   sing N N 158 
HOH   O   H2   sing N N 159 
ILE   N   CA   sing N N 160 
ILE   N   H    sing N N 161 
ILE   N   H2   sing N N 162 
ILE   CA  C    sing N N 163 
ILE   CA  CB   sing N N 164 
ILE   CA  HA   sing N N 165 
ILE   C   O    doub N N 166 
ILE   C   OXT  sing N N 167 
ILE   CB  CG1  sing N N 168 
ILE   CB  CG2  sing N N 169 
ILE   CB  HB   sing N N 170 
ILE   CG1 CD1  sing N N 171 
ILE   CG1 HG12 sing N N 172 
ILE   CG1 HG13 sing N N 173 
ILE   CG2 HG21 sing N N 174 
ILE   CG2 HG22 sing N N 175 
ILE   CG2 HG23 sing N N 176 
ILE   CD1 HD11 sing N N 177 
ILE   CD1 HD12 sing N N 178 
ILE   CD1 HD13 sing N N 179 
ILE   OXT HXT  sing N N 180 
LEU   N   CA   sing N N 181 
LEU   N   H    sing N N 182 
LEU   N   H2   sing N N 183 
LEU   CA  C    sing N N 184 
LEU   CA  CB   sing N N 185 
LEU   CA  HA   sing N N 186 
LEU   C   O    doub N N 187 
LEU   C   OXT  sing N N 188 
LEU   CB  CG   sing N N 189 
LEU   CB  HB2  sing N N 190 
LEU   CB  HB3  sing N N 191 
LEU   CG  CD1  sing N N 192 
LEU   CG  CD2  sing N N 193 
LEU   CG  HG   sing N N 194 
LEU   CD1 HD11 sing N N 195 
LEU   CD1 HD12 sing N N 196 
LEU   CD1 HD13 sing N N 197 
LEU   CD2 HD21 sing N N 198 
LEU   CD2 HD22 sing N N 199 
LEU   CD2 HD23 sing N N 200 
LEU   OXT HXT  sing N N 201 
LYS   N   CA   sing N N 202 
LYS   N   H    sing N N 203 
LYS   N   H2   sing N N 204 
LYS   CA  C    sing N N 205 
LYS   CA  CB   sing N N 206 
LYS   CA  HA   sing N N 207 
LYS   C   O    doub N N 208 
LYS   C   OXT  sing N N 209 
LYS   CB  CG   sing N N 210 
LYS   CB  HB2  sing N N 211 
LYS   CB  HB3  sing N N 212 
LYS   CG  CD   sing N N 213 
LYS   CG  HG2  sing N N 214 
LYS   CG  HG3  sing N N 215 
LYS   CD  CE   sing N N 216 
LYS   CD  HD2  sing N N 217 
LYS   CD  HD3  sing N N 218 
LYS   CE  NZ   sing N N 219 
LYS   CE  HE2  sing N N 220 
LYS   CE  HE3  sing N N 221 
LYS   NZ  HZ1  sing N N 222 
LYS   NZ  HZ2  sing N N 223 
LYS   NZ  HZ3  sing N N 224 
LYS   OXT HXT  sing N N 225 
MET   N   CA   sing N N 226 
MET   N   H    sing N N 227 
MET   N   H2   sing N N 228 
MET   CA  C    sing N N 229 
MET   CA  CB   sing N N 230 
MET   CA  HA   sing N N 231 
MET   C   O    doub N N 232 
MET   C   OXT  sing N N 233 
MET   CB  CG   sing N N 234 
MET   CB  HB2  sing N N 235 
MET   CB  HB3  sing N N 236 
MET   CG  SD   sing N N 237 
MET   CG  HG2  sing N N 238 
MET   CG  HG3  sing N N 239 
MET   SD  CE   sing N N 240 
MET   CE  HE1  sing N N 241 
MET   CE  HE2  sing N N 242 
MET   CE  HE3  sing N N 243 
MET   OXT HXT  sing N N 244 
PHE   N   CA   sing N N 245 
PHE   N   H    sing N N 246 
PHE   N   H2   sing N N 247 
PHE   CA  C    sing N N 248 
PHE   CA  CB   sing N N 249 
PHE   CA  HA   sing N N 250 
PHE   C   O    doub N N 251 
PHE   C   OXT  sing N N 252 
PHE   CB  CG   sing N N 253 
PHE   CB  HB2  sing N N 254 
PHE   CB  HB3  sing N N 255 
PHE   CG  CD1  doub Y N 256 
PHE   CG  CD2  sing Y N 257 
PHE   CD1 CE1  sing Y N 258 
PHE   CD1 HD1  sing N N 259 
PHE   CD2 CE2  doub Y N 260 
PHE   CD2 HD2  sing N N 261 
PHE   CE1 CZ   doub Y N 262 
PHE   CE1 HE1  sing N N 263 
PHE   CE2 CZ   sing Y N 264 
PHE   CE2 HE2  sing N N 265 
PHE   CZ  HZ   sing N N 266 
PHE   OXT HXT  sing N N 267 
PRO   N   CA   sing N N 268 
PRO   N   CD   sing N N 269 
PRO   N   H    sing N N 270 
PRO   CA  C    sing N N 271 
PRO   CA  CB   sing N N 272 
PRO   CA  HA   sing N N 273 
PRO   C   O    doub N N 274 
PRO   C   OXT  sing N N 275 
PRO   CB  CG   sing N N 276 
PRO   CB  HB2  sing N N 277 
PRO   CB  HB3  sing N N 278 
PRO   CG  CD   sing N N 279 
PRO   CG  HG2  sing N N 280 
PRO   CG  HG3  sing N N 281 
PRO   CD  HD2  sing N N 282 
PRO   CD  HD3  sing N N 283 
PRO   OXT HXT  sing N N 284 
SER   N   CA   sing N N 285 
SER   N   H    sing N N 286 
SER   N   H2   sing N N 287 
SER   CA  C    sing N N 288 
SER   CA  CB   sing N N 289 
SER   CA  HA   sing N N 290 
SER   C   O    doub N N 291 
SER   C   OXT  sing N N 292 
SER   CB  OG   sing N N 293 
SER   CB  HB2  sing N N 294 
SER   CB  HB3  sing N N 295 
SER   OG  HG   sing N N 296 
SER   OXT HXT  sing N N 297 
THR   N   CA   sing N N 298 
THR   N   H    sing N N 299 
THR   N   H2   sing N N 300 
THR   CA  C    sing N N 301 
THR   CA  CB   sing N N 302 
THR   CA  HA   sing N N 303 
THR   C   O    doub N N 304 
THR   C   OXT  sing N N 305 
THR   CB  OG1  sing N N 306 
THR   CB  CG2  sing N N 307 
THR   CB  HB   sing N N 308 
THR   OG1 HG1  sing N N 309 
THR   CG2 HG21 sing N N 310 
THR   CG2 HG22 sing N N 311 
THR   CG2 HG23 sing N N 312 
THR   OXT HXT  sing N N 313 
TRP   N   CA   sing N N 314 
TRP   N   H    sing N N 315 
TRP   N   H2   sing N N 316 
TRP   CA  C    sing N N 317 
TRP   CA  CB   sing N N 318 
TRP   CA  HA   sing N N 319 
TRP   C   O    doub N N 320 
TRP   C   OXT  sing N N 321 
TRP   CB  CG   sing N N 322 
TRP   CB  HB2  sing N N 323 
TRP   CB  HB3  sing N N 324 
TRP   CG  CD1  doub Y N 325 
TRP   CG  CD2  sing Y N 326 
TRP   CD1 NE1  sing Y N 327 
TRP   CD1 HD1  sing N N 328 
TRP   CD2 CE2  doub Y N 329 
TRP   CD2 CE3  sing Y N 330 
TRP   NE1 CE2  sing Y N 331 
TRP   NE1 HE1  sing N N 332 
TRP   CE2 CZ2  sing Y N 333 
TRP   CE3 CZ3  doub Y N 334 
TRP   CE3 HE3  sing N N 335 
TRP   CZ2 CH2  doub Y N 336 
TRP   CZ2 HZ2  sing N N 337 
TRP   CZ3 CH2  sing Y N 338 
TRP   CZ3 HZ3  sing N N 339 
TRP   CH2 HH2  sing N N 340 
TRP   OXT HXT  sing N N 341 
TYR   N   CA   sing N N 342 
TYR   N   H    sing N N 343 
TYR   N   H2   sing N N 344 
TYR   CA  C    sing N N 345 
TYR   CA  CB   sing N N 346 
TYR   CA  HA   sing N N 347 
TYR   C   O    doub N N 348 
TYR   C   OXT  sing N N 349 
TYR   CB  CG   sing N N 350 
TYR   CB  HB2  sing N N 351 
TYR   CB  HB3  sing N N 352 
TYR   CG  CD1  doub Y N 353 
TYR   CG  CD2  sing Y N 354 
TYR   CD1 CE1  sing Y N 355 
TYR   CD1 HD1  sing N N 356 
TYR   CD2 CE2  doub Y N 357 
TYR   CD2 HD2  sing N N 358 
TYR   CE1 CZ   doub Y N 359 
TYR   CE1 HE1  sing N N 360 
TYR   CE2 CZ   sing Y N 361 
TYR   CE2 HE2  sing N N 362 
TYR   CZ  OH   sing N N 363 
TYR   OH  HH   sing N N 364 
TYR   OXT HXT  sing N N 365 
VAL   N   CA   sing N N 366 
VAL   N   H    sing N N 367 
VAL   N   H2   sing N N 368 
VAL   CA  C    sing N N 369 
VAL   CA  CB   sing N N 370 
VAL   CA  HA   sing N N 371 
VAL   C   O    doub N N 372 
VAL   C   OXT  sing N N 373 
VAL   CB  CG1  sing N N 374 
VAL   CB  CG2  sing N N 375 
VAL   CB  HB   sing N N 376 
VAL   CG1 HG11 sing N N 377 
VAL   CG1 HG12 sing N N 378 
VAL   CG1 HG13 sing N N 379 
VAL   CG2 HG21 sing N N 380 
VAL   CG2 HG22 sing N N 381 
VAL   CG2 HG23 sing N N 382 
VAL   OXT HXT  sing N N 383 
# 
_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                    7HB4 
_atom_sites.fract_transf_matrix[1][1]   0.014663 
_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]   0.011033 
_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]   0.010141 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
_atom_type.scat_dispersion_real 
_atom_type.scat_dispersion_imag 
_atom_type.scat_Cromer_Mann_a1 
_atom_type.scat_Cromer_Mann_a2 
_atom_type.scat_Cromer_Mann_a3 
_atom_type.scat_Cromer_Mann_a4 
_atom_type.scat_Cromer_Mann_b1 
_atom_type.scat_Cromer_Mann_b2 
_atom_type.scat_Cromer_Mann_b3 
_atom_type.scat_Cromer_Mann_b4 
_atom_type.scat_Cromer_Mann_c 
_atom_type.scat_source 
_atom_type.scat_dispersion_source 
C ? ? 3.54356 2.42580 ? ? 25.62398 1.50364  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
N ? ? 4.01032 2.96436 ? ? 19.97189 1.75589  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O ? ? 4.49882 3.47563 ? ? 15.80542 1.70748  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
S ? ? 9.55732 6.39887 ? ? 1.23737  29.19336 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N   . GLU   A 1 9   ? 6.83082   -29.01268 -38.45658 1.000 52.49291 ? 16  GLU   A N   1 
ATOM   2    C CA  . GLU   A 1 9   ? 8.15082   -28.39743 -38.41304 1.000 47.09265 ? 16  GLU   A CA  1 
ATOM   3    C C   . GLU   A 1 9   ? 8.27506   -27.48710 -37.18435 1.000 48.23934 ? 16  GLU   A C   1 
ATOM   4    O O   . GLU   A 1 9   ? 7.57072   -26.48239 -37.04719 1.000 45.61838 ? 16  GLU   A O   1 
ATOM   5    C CB  . GLU   A 1 9   ? 8.42122   -27.61263 -39.69826 1.000 53.40640 ? 16  GLU   A CB  1 
ATOM   6    C CG  . GLU   A 1 9   ? 9.30102   -26.36629 -39.52198 1.000 74.42325 ? 16  GLU   A CG  1 
ATOM   7    C CD  . GLU   A 1 9   ? 10.79079  -26.65160 -39.60581 1.000 84.85920 ? 16  GLU   A CD  1 
ATOM   8    O OE1 . GLU   A 1 9   ? 11.19947  -27.80897 -39.35115 1.000 90.65788 ? 16  GLU   A OE1 1 
ATOM   9    O OE2 . GLU   A 1 9   ? 11.55150  -25.70329 -39.91363 1.000 79.12629 ? 16  GLU   A OE2 1 
ATOM   10   N N   . VAL   A 1 10  ? 9.18089   -27.84648 -36.28656 1.000 40.28885 ? 17  VAL   A N   1 
ATOM   11   C CA  . VAL   A 1 10  ? 9.35682   -27.14830 -35.01527 1.000 35.86852 ? 17  VAL   A CA  1 
ATOM   12   C C   . VAL   A 1 10  ? 10.72912  -26.49620 -35.02661 1.000 33.58447 ? 17  VAL   A C   1 
ATOM   13   O O   . VAL   A 1 10  ? 11.72631  -27.17219 -35.30445 1.000 34.45379 ? 17  VAL   A O   1 
ATOM   14   C CB  . VAL   A 1 10  ? 9.24789   -28.12213 -33.83718 1.000 32.64590 ? 17  VAL   A CB  1 
ATOM   15   C CG1 . VAL   A 1 10  ? 9.52688   -27.36264 -32.50589 1.000 27.27804 ? 17  VAL   A CG1 1 
ATOM   16   C CG2 . VAL   A 1 10  ? 7.92561   -28.88123 -33.89312 1.000 38.25174 ? 17  VAL   A CG2 1 
ATOM   17   N N   . GLU   A 1 11  ? 10.79314  -25.19999 -34.72161 1.000 23.79297 ? 18  GLU   A N   1 
ATOM   18   C CA  . GLU   A 1 11  ? 12.07333  -24.51563 -34.63134 1.000 22.44552 ? 18  GLU   A CA  1 
ATOM   19   C C   . GLU   A 1 11  ? 12.39347  -24.24714 -33.17231 1.000 21.17173 ? 18  GLU   A C   1 
ATOM   20   O O   . GLU   A 1 11  ? 11.51734  -23.84910 -32.40456 1.000 20.73384 ? 18  GLU   A O   1 
ATOM   21   C CB  . GLU   A 1 11  ? 12.10608  -23.19662 -35.40598 1.000 22.04736 ? 18  GLU   A CB  1 
ATOM   22   C CG  . GLU   A 1 11  ? 11.85640  -23.35389 -36.90717 1.000 24.39048 ? 18  GLU   A CG  1 
ATOM   23   C CD  . GLU   A 1 11  ? 11.79779  -22.00416 -37.61288 1.000 38.91062 ? 18  GLU   A CD  1 
ATOM   24   O OE1 . GLU   A 1 11  ? 10.79231  -21.28260 -37.44297 1.000 35.59947 ? 18  GLU   A OE1 1 
ATOM   25   O OE2 . GLU   A 1 11  ? 12.72873  -21.69917 -38.38759 1.000 46.50064 ? 18  GLU   A OE2 1 
ATOM   26   N N   . THR   A 1 12  ? 13.64105  -24.49218 -32.80498 1.000 20.88114 ? 19  THR   A N   1 
ATOM   27   C CA  . THR   A 1 12  ? 14.09885  -24.27211 -31.43966 1.000 20.79138 ? 19  THR   A CA  1 
ATOM   28   C C   . THR   A 1 12  ? 15.05267  -23.08719 -31.40642 1.000 22.23901 ? 19  THR   A C   1 
ATOM   29   O O   . THR   A 1 12  ? 15.96834  -22.99613 -32.23195 1.000 21.28626 ? 19  THR   A O   1 
ATOM   30   C CB  . THR   A 1 12  ? 14.78618  -25.51855 -30.89135 1.000 20.95578 ? 19  THR   A CB  1 
ATOM   31   O OG1 . THR   A 1 12  ? 13.92921  -26.65791 -31.07293 1.000 22.23674 ? 19  THR   A OG1 1 
ATOM   32   C CG2 . THR   A 1 12  ? 15.09081  -25.35136 -29.40912 1.000 20.40549 ? 19  THR   A CG2 1 
ATOM   33   N N   . PHE   A 1 13  ? 14.87284  -22.22687 -30.40711 1.000 20.43704 ? 20  PHE   A N   1 
ATOM   34   C CA  . PHE   A 1 13  ? 15.63848  -20.99964 -30.26302 1.000 22.19999 ? 20  PHE   A CA  1 
ATOM   35   C C   . PHE   A 1 13  ? 16.19443  -20.90564 -28.85005 1.000 22.06408 ? 20  PHE   A C   1 
ATOM   36   O O   . PHE   A 1 13  ? 15.56362  -21.36281 -27.89818 1.000 23.09706 ? 20  PHE   A O   1 
ATOM   37   C CB  . PHE   A 1 13  ? 14.78535  -19.75291 -30.49894 1.000 18.91760 ? 20  PHE   A CB  1 
ATOM   38   C CG  . PHE   A 1 13  ? 14.02368  -19.75577 -31.79685 1.000 18.12962 ? 20  PHE   A CG  1 
ATOM   39   C CD1 . PHE   A 1 13  ? 12.82277  -20.43147 -31.90978 1.000 19.08428 ? 20  PHE   A CD1 1 
ATOM   40   C CD2 . PHE   A 1 13  ? 14.49763  -19.05980 -32.89055 1.000 26.80832 ? 20  PHE   A CD2 1 
ATOM   41   C CE1 . PHE   A 1 13  ? 12.09662  -20.42502 -33.11262 1.000 22.41784 ? 20  PHE   A CE1 1 
ATOM   42   C CE2 . PHE   A 1 13  ? 13.76760  -19.03206 -34.08419 1.000 22.39104 ? 20  PHE   A CE2 1 
ATOM   43   C CZ  . PHE   A 1 13  ? 12.57585  -19.72980 -34.18735 1.000 22.39258 ? 20  PHE   A CZ  1 
ATOM   44   N N   . ALA   A 1 14  ? 17.34959  -20.26599 -28.71840 1.000 18.24635 ? 21  ALA   A N   1 
ATOM   45   C CA  . ALA   A 1 14  ? 17.85447  -19.88458 -27.39485 1.000 19.79549 ? 21  ALA   A CA  1 
ATOM   46   C C   . ALA   A 1 14  ? 17.22489  -18.56419 -26.96491 1.000 20.47851 ? 21  ALA   A C   1 
ATOM   47   O O   . ALA   A 1 14  ? 17.12246  -17.62720 -27.76180 1.000 20.84450 ? 21  ALA   A O   1 
ATOM   48   C CB  . ALA   A 1 14  ? 19.38138  -19.76252 -27.41213 1.000 20.93011 ? 21  ALA   A CB  1 
ATOM   49   N N   . PHE   A 1 15  ? 16.77596  -18.49644 -25.70768 1.000 19.41149 ? 22  PHE   A N   1 
ATOM   50   C CA  . PHE   A 1 15  ? 16.45675  -17.20797 -25.10923 1.000 21.90513 ? 22  PHE   A CA  1 
ATOM   51   C C   . PHE   A 1 15  ? 17.70049  -16.33586 -25.11921 1.000 21.57292 ? 22  PHE   A C   1 
ATOM   52   O O   . PHE   A 1 15  ? 18.82882  -16.82609 -25.02628 1.000 26.15578 ? 22  PHE   A O   1 
ATOM   53   C CB  . PHE   A 1 15  ? 16.01113  -17.37928 -23.64813 1.000 23.25476 ? 22  PHE   A CB  1 
ATOM   54   C CG  . PHE   A 1 15  ? 14.61953  -17.89151 -23.48626 1.000 21.15899 ? 22  PHE   A CG  1 
ATOM   55   C CD1 . PHE   A 1 15  ? 13.53227  -17.08815 -23.80090 1.000 22.83543 ? 22  PHE   A CD1 1 
ATOM   56   C CD2 . PHE   A 1 15  ? 14.39971  -19.17047 -23.01063 1.000 20.71320 ? 22  PHE   A CD2 1 
ATOM   57   C CE1 . PHE   A 1 15  ? 12.23013  -17.55458 -23.64022 1.000 18.22339 ? 22  PHE   A CE1 1 
ATOM   58   C CE2 . PHE   A 1 15  ? 13.12214  -19.64551 -22.84062 1.000 23.83493 ? 22  PHE   A CE2 1 
ATOM   59   C CZ  . PHE   A 1 15  ? 12.03264  -18.85132 -23.16370 1.000 19.33501 ? 22  PHE   A CZ  1 
ATOM   60   N N   . GLN   A 1 16  ? 17.49988  -15.03149 -25.21758 1.000 22.10849 ? 23  GLN   A N   1 
ATOM   61   C CA  . GLN   A 1 16  ? 18.58506  -14.12656 -24.88160 1.000 29.71177 ? 23  GLN   A CA  1 
ATOM   62   C C   . GLN   A 1 16  ? 19.11152  -14.42520 -23.47839 1.000 29.81079 ? 23  GLN   A C   1 
ATOM   63   O O   . GLN   A 1 16  ? 18.35676  -14.82881 -22.59055 1.000 23.79487 ? 23  GLN   A O   1 
ATOM   64   C CB  . GLN   A 1 16  ? 18.08676  -12.70502 -24.93781 1.000 27.90174 ? 23  GLN   A CB  1 
ATOM   65   C CG  . GLN   A 1 16  ? 18.39944  -12.06695 -26.23504 1.000 51.34171 ? 23  GLN   A CG  1 
ATOM   66   C CD  . GLN   A 1 16  ? 17.60073  -10.85223 -26.35449 1.000 43.80677 ? 23  GLN   A CD  1 
ATOM   67   O OE1 . GLN   A 1 16  ? 18.12595  -9.76019  -26.52916 1.000 55.88624 ? 23  GLN   A OE1 1 
ATOM   68   N NE2 . GLN   A 1 16  ? 16.30750  -11.00218 -26.11700 1.000 40.98512 ? 23  GLN   A NE2 1 
ATOM   69   N N   . ALA   A 1 17  ? 20.41314  -14.19701 -23.27027 1.000 28.92697 ? 24  ALA   A N   1 
ATOM   70   C CA  . ALA   A 1 17  ? 21.02795  -14.58960 -22.00577 1.000 32.52699 ? 24  ALA   A CA  1 
ATOM   71   C C   . ALA   A 1 17  ? 20.33915  -13.92162 -20.82024 1.000 35.49302 ? 24  ALA   A C   1 
ATOM   72   O O   . ALA   A 1 17  ? 20.10627  -14.56188 -19.78330 1.000 31.80209 ? 24  ALA   A O   1 
ATOM   73   C CB  . ALA   A 1 17  ? 22.51819  -14.25280 -22.01640 1.000 35.84022 ? 24  ALA   A CB  1 
ATOM   74   N N   . GLU   A 1 18  ? 19.99720  -12.63461 -20.95958 1.000 25.73703 ? 25  GLU   A N   1 
ATOM   75   C CA  . GLU   A 1 18  ? 19.38369  -11.89498 -19.86009 1.000 25.08980 ? 25  GLU   A CA  1 
ATOM   76   C C   . GLU   A 1 18  ? 18.02700  -12.47183 -19.50130 1.000 24.35343 ? 25  GLU   A C   1 
ATOM   77   O O   . GLU   A 1 18  ? 17.62978  -12.47345 -18.32789 1.000 24.15961 ? 25  GLU   A O   1 
ATOM   78   C CB  . GLU   A 1 18  ? 19.23858  -10.42201 -20.24360 1.000 36.64046 ? 25  GLU   A CB  1 
ATOM   79   C CG  . GLU   A 1 18  ? 20.55250  -9.68815  -20.41437 1.000 43.83296 ? 25  GLU   A CG  1 
ATOM   80   C CD  . GLU   A 1 18  ? 21.16928  -9.90864  -21.78898 1.000 56.23193 ? 25  GLU   A CD  1 
ATOM   81   O OE1 . GLU   A 1 18  ? 20.61275  -10.70238 -22.59413 1.000 47.06969 ? 25  GLU   A OE1 1 
ATOM   82   O OE2 . GLU   A 1 18  ? 22.21829  -9.28799  -22.05951 1.000 55.24653 ? 25  GLU   A OE2 1 
ATOM   83   N N   . ILE   A 1 19  ? 17.28353  -12.94493 -20.50359 1.000 23.61807 ? 26  ILE   A N   1 
ATOM   84   C CA  . ILE   A 1 19  ? 15.95311  -13.47615 -20.23438 1.000 21.41484 ? 26  ILE   A CA  1 
ATOM   85   C C   . ILE   A 1 19  ? 16.05444  -14.85270 -19.59709 1.000 25.01948 ? 26  ILE   A C   1 
ATOM   86   O O   . ILE   A 1 19  ? 15.27514  -15.17966 -18.69331 1.000 20.22603 ? 26  ILE   A O   1 
ATOM   87   C CB  . ILE   A 1 19  ? 15.09154  -13.50496 -21.52127 1.000 24.24725 ? 26  ILE   A CB  1 
ATOM   88   C CG1 . ILE   A 1 19  ? 14.61448  -12.10267 -21.93571 1.000 28.60795 ? 26  ILE   A CG1 1 
ATOM   89   C CG2 . ILE   A 1 19  ? 13.82586  -14.30905 -21.30149 1.000 19.04993 ? 26  ILE   A CG2 1 
ATOM   90   C CD1 . ILE   A 1 19  ? 15.67543  -11.17303 -22.38830 1.000 44.88690 ? 26  ILE   A CD1 1 
ATOM   91   N N   . ALA   A 1 20  ? 16.99550  -15.69413 -20.06311 1.000 20.60072 ? 27  ALA   A N   1 
ATOM   92   C CA  . ALA   A 1 20  ? 17.20694  -16.98803 -19.39592 1.000 23.46266 ? 27  ALA   A CA  1 
ATOM   93   C C   . ALA   A 1 20  ? 17.60592  -16.79210 -17.93697 1.000 23.91364 ? 27  ALA   A C   1 
ATOM   94   O O   . ALA   A 1 20  ? 17.16520  -17.53312 -17.04769 1.000 21.33171 ? 27  ALA   A O   1 
ATOM   95   C CB  . ALA   A 1 20  ? 18.27359  -17.81712 -20.13061 1.000 24.79222 ? 27  ALA   A CB  1 
ATOM   96   N N   . GLN   A 1 21  ? 18.44966  -15.80650 -17.67865 1.000 21.24906 ? 28  GLN   A N   1 
ATOM   97   C CA  . GLN   A 1 21  ? 18.81274  -15.46347 -16.30824 1.000 22.57725 ? 28  GLN   A CA  1 
ATOM   98   C C   . GLN   A 1 21  ? 17.59477  -15.04429 -15.49051 1.000 24.34084 ? 28  GLN   A C   1 
ATOM   99   O O   . GLN   A 1 21  ? 17.45125  -15.42462 -14.31779 1.000 22.01076 ? 28  GLN   A O   1 
ATOM   100  C CB  . GLN   A 1 21  ? 19.84966  -14.35578 -16.37942 1.000 27.50832 ? 28  GLN   A CB  1 
ATOM   101  C CG  . GLN   A 1 21  ? 20.56090  -14.02500 -15.12862 1.000 50.25523 ? 28  GLN   A CG  1 
ATOM   102  C CD  . GLN   A 1 21  ? 21.77622  -13.21274 -15.46329 1.000 62.65904 ? 28  GLN   A CD  1 
ATOM   103  O OE1 . GLN   A 1 21  ? 21.87312  -12.65727 -16.56966 1.000 46.60473 ? 28  GLN   A OE1 1 
ATOM   104  N NE2 . GLN   A 1 21  ? 22.72099  -13.14120 -14.52805 1.000 58.77219 ? 28  GLN   A NE2 1 
ATOM   105  N N   . LEU   A 1 22  ? 16.70528  -14.24926 -16.08446 1.000 22.88649 ? 29  LEU   A N   1 
ATOM   106  C CA  . LEU   A 1 22  ? 15.50477  -13.84582 -15.35564 1.000 21.73167 ? 29  LEU   A CA  1 
ATOM   107  C C   . LEU   A 1 22  ? 14.61521  -15.04510 -15.06951 1.000 21.15914 ? 29  LEU   A C   1 
ATOM   108  O O   . LEU   A 1 22  ? 14.06415  -15.16962 -13.97482 1.000 21.24687 ? 29  LEU   A O   1 
ATOM   109  C CB  . LEU   A 1 22  ? 14.72166  -12.80261 -16.15210 1.000 22.43546 ? 29  LEU   A CB  1 
ATOM   110  C CG  . LEU   A 1 22  ? 13.33513  -12.50316 -15.58260 1.000 26.50611 ? 29  LEU   A CG  1 
ATOM   111  C CD1 . LEU   A 1 22  ? 13.43045  -11.82184 -14.22908 1.000 25.92519 ? 29  LEU   A CD1 1 
ATOM   112  C CD2 . LEU   A 1 22  ? 12.49145  -11.68182 -16.58779 1.000 25.51875 ? 29  LEU   A CD2 1 
ATOM   113  N N   . MET   A 1 23  ? 14.41583  -15.93037 -16.05720 1.000 17.88229 ? 30  MET   A N   1 
ATOM   114  C CA  . MET   A 1 23  ? 13.53212  -17.05713 -15.76540 1.000 21.56366 ? 30  MET   A CA  1 
ATOM   115  C C   . MET   A 1 23  ? 14.13536  -17.99410 -14.73373 1.000 18.49444 ? 30  MET   A C   1 
ATOM   116  O O   . MET   A 1 23  ? 13.40357  -18.54992 -13.90153 1.000 21.99714 ? 30  MET   A O   1 
ATOM   117  C CB  . MET   A 1 23  ? 13.10472  -17.88750 -16.99666 1.000 24.57017 ? 30  MET   A CB  1 
ATOM   118  C CG  . MET   A 1 23  ? 12.33662  -17.15708 -18.06262 1.000 21.17280 ? 30  MET   A CG  1 
ATOM   119  S SD  . MET   A 1 23  ? 12.60765  -17.75127 -19.76776 1.000 20.98021 ? 30  MET   A SD  1 
ATOM   120  C CE  . MET   A 1 23  ? 11.55270  -19.18298 -19.52831 1.000 18.64827 ? 30  MET   A CE  1 
ATOM   121  N N   . SER   A 1 24  ? 15.45835  -18.16065 -14.73313 1.000 19.90859 ? 31  SER   A N   1 
ATOM   122  C CA  . SER   A 1 24  ? 16.07354  -18.95160 -13.67330 1.000 22.91152 ? 31  SER   A CA  1 
ATOM   123  C C   . SER   A 1 24  ? 15.85647  -18.29929 -12.31192 1.000 26.44114 ? 31  SER   A C   1 
ATOM   124  O O   . SER   A 1 24  ? 15.59402  -18.98777 -11.31050 1.000 23.38193 ? 31  SER   A O   1 
ATOM   125  C CB  . SER   A 1 24  ? 17.55611  -19.13971 -13.97956 1.000 26.06790 ? 31  SER   A CB  1 
ATOM   126  O OG  . SER   A 1 24  ? 18.17334  -19.76381 -12.88454 1.000 42.16753 ? 31  SER   A OG  1 
ATOM   127  N N   . LEU   A 1 25  ? 15.97185  -16.97226 -12.24235 1.000 21.86355 ? 32  LEU   A N   1 
ATOM   128  C CA  . LEU   A 1 25  ? 15.72810  -16.31179 -10.96180 1.000 22.23095 ? 32  LEU   A CA  1 
ATOM   129  C C   . LEU   A 1 25  ? 14.28014  -16.51852 -10.51216 1.000 24.53278 ? 32  LEU   A C   1 
ATOM   130  O O   . LEU   A 1 25  ? 14.00858  -16.76581 -9.32808  1.000 24.77505 ? 32  LEU   A O   1 
ATOM   131  C CB  . LEU   A 1 25  ? 16.05758  -14.82518 -11.09015 1.000 22.84042 ? 32  LEU   A CB  1 
ATOM   132  C CG  . LEU   A 1 25  ? 15.83833  -13.91725 -9.88801  1.000 35.25235 ? 32  LEU   A CG  1 
ATOM   133  C CD1 . LEU   A 1 25  ? 16.79920  -12.72945 -9.99381  1.000 34.40095 ? 32  LEU   A CD1 1 
ATOM   134  C CD2 . LEU   A 1 25  ? 14.38397  -13.46251 -9.80874  1.000 27.15233 ? 32  LEU   A CD2 1 
ATOM   135  N N   . ILE   A 1 26  ? 13.33212  -16.40249 -11.43681 1.000 19.63254 ? 33  ILE   A N   1 
ATOM   136  C CA  . ILE   A 1 26  ? 11.91969  -16.57115 -11.08473 1.000 18.95087 ? 33  ILE   A CA  1 
ATOM   137  C C   . ILE   A 1 26  ? 11.64688  -17.99252 -10.59373 1.000 27.33306 ? 33  ILE   A C   1 
ATOM   138  O O   . ILE   A 1 26  ? 10.87451  -18.20312 -9.64601  1.000 24.00276 ? 33  ILE   A O   1 
ATOM   139  C CB  . ILE   A 1 26  ? 11.02805  -16.20350 -12.28664 1.000 20.33922 ? 33  ILE   A CB  1 
ATOM   140  C CG1 . ILE   A 1 26  ? 11.03448  -14.68178 -12.48589 1.000 22.11327 ? 33  ILE   A CG1 1 
ATOM   141  C CG2 . ILE   A 1 26  ? 9.57540   -16.75676 -12.10566 1.000 22.58528 ? 33  ILE   A CG2 1 
ATOM   142  C CD1 . ILE   A 1 26  ? 10.40987  -14.26116 -13.81240 1.000 21.65481 ? 33  ILE   A CD1 1 
ATOM   143  N N   . ILE   A 1 27  ? 12.28651  -18.98908 -11.21227 1.000 23.78238 ? 34  ILE   A N   1 
ATOM   144  C CA  . ILE   A 1 27  ? 12.02984  -20.38194 -10.85336 1.000 23.74768 ? 34  ILE   A CA  1 
ATOM   145  C C   . ILE   A 1 27  ? 12.73844  -20.76220 -9.56067  1.000 25.72952 ? 34  ILE   A C   1 
ATOM   146  O O   . ILE   A 1 27  ? 12.22052  -21.55569 -8.76239  1.000 28.83825 ? 34  ILE   A O   1 
ATOM   147  C CB  . ILE   A 1 27  ? 12.46155  -21.28291 -12.01841 1.000 31.25362 ? 34  ILE   A CB  1 
ATOM   148  C CG1 . ILE   A 1 27  ? 11.47214  -21.13384 -13.17202 1.000 22.17351 ? 34  ILE   A CG1 1 
ATOM   149  C CG2 . ILE   A 1 27  ? 12.56716  -22.75421 -11.58583 1.000 31.93485 ? 34  ILE   A CG2 1 
ATOM   150  C CD1 . ILE   A 1 27  ? 12.07825  -21.50829 -14.49193 1.000 25.37303 ? 34  ILE   A CD1 1 
ATOM   151  N N   . ASN   A 1 28  ? 13.90991  -20.19192 -9.30626  1.000 23.34641 ? 35  ASN   A N   1 
ATOM   152  C CA  . ASN   A 1 28  ? 14.74324  -20.64382 -8.19734  1.000 26.71365 ? 35  ASN   A CA  1 
ATOM   153  C C   . ASN   A 1 28  ? 14.64853  -19.78365 -6.94487  1.000 30.71266 ? 35  ASN   A C   1 
ATOM   154  O O   . ASN   A 1 28  ? 15.07304  -20.23216 -5.87296  1.000 31.86450 ? 35  ASN   A O   1 
ATOM   155  C CB  . ASN   A 1 28  ? 16.18658  -20.71895 -8.68348  1.000 28.67200 ? 35  ASN   A CB  1 
ATOM   156  C CG  . ASN   A 1 28  ? 16.36656  -21.82323 -9.69290  1.000 43.05666 ? 35  ASN   A CG  1 
ATOM   157  O OD1 . ASN   A 1 28  ? 15.67052  -22.83826 -9.63578  1.000 44.03962 ? 35  ASN   A OD1 1 
ATOM   158  N ND2 . ASN   A 1 28  ? 17.16493  -21.56498 -10.70912 1.000 40.72820 ? 35  ASN   A ND2 1 
ATOM   159  N N   . THR   A 1 29  ? 14.09400  -18.58215 -7.02521  1.000 28.78118 ? 36  THR   A N   1 
ATOM   160  C CA  . THR   A 1 29  ? 14.02590  -17.74080 -5.83654  1.000 30.97185 ? 36  THR   A CA  1 
ATOM   161  C C   . THR   A 1 29  ? 12.86936  -18.17651 -4.94131  1.000 30.25632 ? 36  THR   A C   1 
ATOM   162  O O   . THR   A 1 29  ? 11.74851  -18.41625 -5.40378  1.000 29.66354 ? 36  THR   A O   1 
ATOM   163  C CB  . THR   A 1 29  ? 13.86848  -16.26212 -6.22414  1.000 34.45002 ? 36  THR   A CB  1 
ATOM   164  O OG1 . THR   A 1 29  ? 14.99901  -15.85838 -7.00777  1.000 29.47042 ? 36  THR   A OG1 1 
ATOM   165  C CG2 . THR   A 1 29  ? 13.80184  -15.37436 -4.98188  1.000 27.81569 ? 36  THR   A CG2 1 
ATOM   166  N N   . PHE   A 1 30  ? 13.13807  -18.25597 -3.64742  1.000 27.18098 ? 37  PHE   A N   1 
ATOM   167  C CA  . PHE   A 1 30  ? 12.05348  -18.50385 -2.71369  1.000 29.55619 ? 37  PHE   A CA  1 
ATOM   168  C C   . PHE   A 1 30  ? 11.18419  -17.25772 -2.60048  1.000 27.89299 ? 37  PHE   A C   1 
ATOM   169  O O   . PHE   A 1 30  ? 11.65510  -16.18671 -2.20084  1.000 28.51963 ? 37  PHE   A O   1 
ATOM   170  C CB  . PHE   A 1 30  ? 12.59820  -18.89276 -1.35491  1.000 29.86306 ? 37  PHE   A CB  1 
ATOM   171  C CG  . PHE   A 1 30  ? 11.53254  -19.23393 -0.37526  1.000 35.27827 ? 37  PHE   A CG  1 
ATOM   172  C CD1 . PHE   A 1 30  ? 10.91306  -20.48123 -0.41390  1.000 34.03564 ? 37  PHE   A CD1 1 
ATOM   173  C CD2 . PHE   A 1 30  ? 11.11632  -18.30495 0.56080   1.000 30.90217 ? 37  PHE   A CD2 1 
ATOM   174  C CE1 . PHE   A 1 30  ? 9.92189   -20.80579 0.49543   1.000 41.27948 ? 37  PHE   A CE1 1 
ATOM   175  C CE2 . PHE   A 1 30  ? 10.11370  -18.61795 1.47053   1.000 32.30988 ? 37  PHE   A CE2 1 
ATOM   176  C CZ  . PHE   A 1 30  ? 9.51525   -19.87178 1.43928   1.000 31.93770 ? 37  PHE   A CZ  1 
ATOM   177  N N   . TYR   A 1 31  ? 9.91420   -17.39491 -2.94347  1.000 25.29876 ? 38  TYR   A N   1 
ATOM   178  C CA  . TYR   A 1 31  ? 9.02459   -16.23593 -2.99775  1.000 24.78834 ? 38  TYR   A CA  1 
ATOM   179  C C   . TYR   A 1 31  ? 7.59885   -16.76266 -2.89507  1.000 24.55148 ? 38  TYR   A C   1 
ATOM   180  O O   . TYR   A 1 31  ? 7.10541   -17.37687 -3.84242  1.000 23.44816 ? 38  TYR   A O   1 
ATOM   181  C CB  . TYR   A 1 31  ? 9.23746   -15.45073 -4.29148  1.000 25.04683 ? 38  TYR   A CB  1 
ATOM   182  C CG  . TYR   A 1 31  ? 8.37476   -14.21567 -4.31719  1.000 23.76800 ? 38  TYR   A CG  1 
ATOM   183  C CD1 . TYR   A 1 31  ? 8.70500   -13.15130 -3.51868  1.000 25.34832 ? 38  TYR   A CD1 1 
ATOM   184  C CD2 . TYR   A 1 31  ? 7.24288   -14.11513 -5.13365  1.000 24.73938 ? 38  TYR   A CD2 1 
ATOM   185  C CE1 . TYR   A 1 31  ? 7.95777   -12.02144 -3.47220  1.000 36.28171 ? 38  TYR   A CE1 1 
ATOM   186  C CE2 . TYR   A 1 31  ? 6.46526   -12.94751 -5.10572  1.000 28.00715 ? 38  TYR   A CE2 1 
ATOM   187  C CZ  . TYR   A 1 31  ? 6.85457   -11.90407 -4.25153  1.000 31.13693 ? 38  TYR   A CZ  1 
ATOM   188  O OH  . TYR   A 1 31  ? 6.15931   -10.72085 -4.16064  1.000 35.87559 ? 38  TYR   A OH  1 
ATOM   189  N N   . SER   A 1 32  ? 6.94260   -16.55048 -1.74889  1.000 25.34558 ? 39  SER   A N   1 
ATOM   190  C CA  . SER   A 1 32  ? 5.67332   -17.22369 -1.52177  1.000 25.69322 ? 39  SER   A CA  1 
ATOM   191  C C   . SER   A 1 32  ? 4.49293   -16.54735 -2.22718  1.000 25.24646 ? 39  SER   A C   1 
ATOM   192  O O   . SER   A 1 32  ? 3.48969   -17.21889 -2.48755  1.000 28.96960 ? 39  SER   A O   1 
ATOM   193  C CB  . SER   A 1 32  ? 5.40460   -17.32431 -0.01115  1.000 27.40410 ? 39  SER   A CB  1 
ATOM   194  O OG  . SER   A 1 32  ? 6.40573   -18.11368 0.62110   1.000 28.59103 ? 39  SER   A OG  1 
ATOM   195  N N   . ASN   A 1 33  ? 4.59770   -15.26316 -2.57111  1.000 24.33974 ? 40  ASN   A N   1 
ATOM   196  C CA  . ASN   A 1 33  ? 3.47048   -14.48918 -3.11557  1.000 24.72528 ? 40  ASN   A CA  1 
ATOM   197  C C   . ASN   A 1 33  ? 3.28863   -14.75186 -4.62063  1.000 23.02245 ? 40  ASN   A C   1 
ATOM   198  O O   . ASN   A 1 33  ? 3.26651   -13.84266 -5.46171  1.000 23.82699 ? 40  ASN   A O   1 
ATOM   199  C CB  . ASN   A 1 33  ? 3.67381   -13.00599 -2.81825  1.000 24.54933 ? 40  ASN   A CB  1 
ATOM   200  C CG  . ASN   A 1 33  ? 2.53011   -12.13232 -3.31917  1.000 25.76444 ? 40  ASN   A CG  1 
ATOM   201  O OD1 . ASN   A 1 33  ? 1.35527   -12.50380 -3.22967  1.000 27.40302 ? 40  ASN   A OD1 1 
ATOM   202  N ND2 . ASN   A 1 33  ? 2.87357   -10.94780 -3.82714  1.000 28.51022 ? 40  ASN   A ND2 1 
ATOM   203  N N   . LYS   A 1 34  ? 3.14014   -16.03737 -4.95149  1.000 17.20502 ? 41  LYS   A N   1 
ATOM   204  C CA  . LYS   A 1 34  ? 3.10664   -16.43561 -6.36946  1.000 17.62821 ? 41  LYS   A CA  1 
ATOM   205  C C   . LYS   A 1 34  ? 1.85093   -15.96331 -7.08664  1.000 20.37790 ? 41  LYS   A C   1 
ATOM   206  O O   . LYS   A 1 34  ? 1.86312   -15.87857 -8.32146  1.000 18.15230 ? 41  LYS   A O   1 
ATOM   207  C CB  . LYS   A 1 34  ? 3.21172   -17.96832 -6.51623  1.000 17.30103 ? 41  LYS   A CB  1 
ATOM   208  C CG  . LYS   A 1 34  ? 4.62176   -18.53159 -6.16618  1.000 21.10682 ? 41  LYS   A CG  1 
ATOM   209  C CD  . LYS   A 1 34  ? 4.62871   -20.04255 -6.04488  1.000 28.79353 ? 41  LYS   A CD  1 
ATOM   210  C CE  . LYS   A 1 34  ? 6.01198   -20.57329 -5.66890  1.000 26.60658 ? 41  LYS   A CE  1 
ATOM   211  N NZ  . LYS   A 1 34  ? 6.94576   -20.57362 -6.83662  1.000 28.75239 ? 41  LYS   A NZ  1 
ATOM   212  N N   . GLU   A 1 35  ? 0.76908   -15.64912 -6.35882  1.000 18.44647 ? 42  GLU   A N   1 
ATOM   213  C CA  . GLU   A 1 35  ? -0.50102  -15.38065 -7.04975  1.000 17.01109 ? 42  GLU   A CA  1 
ATOM   214  C C   . GLU   A 1 35  ? -0.44083  -14.21667 -8.03226  1.000 23.17420 ? 42  GLU   A C   1 
ATOM   215  O O   . GLU   A 1 35  ? -1.34036  -14.10793 -8.88193  1.000 20.93964 ? 42  GLU   A O   1 
ATOM   216  C CB  . GLU   A 1 35  ? -1.59488  -15.12143 -6.03050  1.000 19.37046 ? 42  GLU   A CB  1 
ATOM   217  C CG  . GLU   A 1 35  ? -1.44975  -13.75810 -5.35832  1.000 20.92669 ? 42  GLU   A CG  1 
ATOM   218  C CD  . GLU   A 1 35  ? -2.43386  -13.57564 -4.20594  1.000 34.10806 ? 42  GLU   A CD  1 
ATOM   219  O OE1 . GLU   A 1 35  ? -2.63347  -14.53412 -3.43360  1.000 30.08317 ? 42  GLU   A OE1 1 
ATOM   220  O OE2 . GLU   A 1 35  ? -2.99469  -12.46980 -4.06832  1.000 41.12325 ? 42  GLU   A OE2 1 
ATOM   221  N N   . ILE   A 1 36  ? 0.57716   -13.34862 -7.95083  1.000 18.53904 ? 43  ILE   A N   1 
ATOM   222  C CA  . ILE   A 1 36  ? 0.64332   -12.19461 -8.84421  1.000 15.73205 ? 43  ILE   A CA  1 
ATOM   223  C C   . ILE   A 1 36  ? 0.81495   -12.57684 -10.29993 1.000 18.92905 ? 43  ILE   A C   1 
ATOM   224  O O   . ILE   A 1 36  ? 0.59935   -11.72205 -11.16902 1.000 18.46854 ? 43  ILE   A O   1 
ATOM   225  C CB  . ILE   A 1 36  ? 1.76447   -11.22412 -8.39916  1.000 18.07415 ? 43  ILE   A CB  1 
ATOM   226  C CG1 . ILE   A 1 36  ? 3.15181   -11.87418 -8.47578  1.000 25.43070 ? 43  ILE   A CG1 1 
ATOM   227  C CG2 . ILE   A 1 36  ? 1.48337   -10.77206 -6.97657  1.000 25.75087 ? 43  ILE   A CG2 1 
ATOM   228  C CD1 . ILE   A 1 36  ? 3.89992   -11.62991 -9.79453  1.000 25.20980 ? 43  ILE   A CD1 1 
ATOM   229  N N   . PHE   A 1 37  ? 1.17582   -13.83524 -10.59927 1.000 18.06078 ? 44  PHE   A N   1 
ATOM   230  C CA  . PHE   A 1 37  ? 1.28728   -14.20936 -12.00701 1.000 17.92686 ? 44  PHE   A CA  1 
ATOM   231  C C   . PHE   A 1 37  ? -0.03128  -13.95680 -12.72262 1.000 16.12326 ? 44  PHE   A C   1 
ATOM   232  O O   . PHE   A 1 37  ? -0.04815  -13.56381 -13.88993 1.000 16.79882 ? 44  PHE   A O   1 
ATOM   233  C CB  . PHE   A 1 37  ? 1.68658   -15.68328 -12.16812 1.000 16.82820 ? 44  PHE   A CB  1 
ATOM   234  C CG  . PHE   A 1 37  ? 0.51256   -16.63650 -12.00500 1.000 15.54938 ? 44  PHE   A CG  1 
ATOM   235  C CD1 . PHE   A 1 37  ? 0.15325   -17.10022 -10.74502 1.000 16.24124 ? 44  PHE   A CD1 1 
ATOM   236  C CD2 . PHE   A 1 37  ? -0.28692  -16.97946 -13.10016 1.000 19.99894 ? 44  PHE   A CD2 1 
ATOM   237  C CE1 . PHE   A 1 37  ? -0.96448  -17.94108 -10.59094 1.000 17.78283 ? 44  PHE   A CE1 1 
ATOM   238  C CE2 . PHE   A 1 37  ? -1.40406  -17.81017 -12.96263 1.000 20.08911 ? 44  PHE   A CE2 1 
ATOM   239  C CZ  . PHE   A 1 37  ? -1.73810  -18.29771 -11.71862 1.000 20.30803 ? 44  PHE   A CZ  1 
ATOM   240  N N   . LEU   A 1 38  ? -1.15343  -14.21033 -12.04300 1.000 17.70480 ? 45  LEU   A N   1 
ATOM   241  C CA  . LEU   A 1 38  ? -2.44707  -14.07896 -12.71143 1.000 18.86966 ? 45  LEU   A CA  1 
ATOM   242  C C   . LEU   A 1 38  ? -2.74465  -12.61987 -13.04392 1.000 18.69360 ? 45  LEU   A C   1 
ATOM   243  O O   . LEU   A 1 38  ? -3.25465  -12.32114 -14.12968 1.000 17.22748 ? 45  LEU   A O   1 
ATOM   244  C CB  . LEU   A 1 38  ? -3.56471  -14.67688 -11.83499 1.000 14.12606 ? 45  LEU   A CB  1 
ATOM   245  C CG  . LEU   A 1 38  ? -4.94133  -14.70987 -12.54663 1.000 16.04572 ? 45  LEU   A CG  1 
ATOM   246  C CD1 . LEU   A 1 38  ? -4.83297  -15.46043 -13.85126 1.000 17.29802 ? 45  LEU   A CD1 1 
ATOM   247  C CD2 . LEU   A 1 38  ? -6.01518  -15.34164 -11.63680 1.000 23.46880 ? 45  LEU   A CD2 1 
ATOM   248  N N   . ARG   A 1 39  ? -2.47981  -11.71040 -12.09354 1.000 14.70605 ? 46  ARG   A N   1 
ATOM   249  C CA  . ARG   A 1 39  ? -2.56655  -10.27230 -12.34813 1.000 19.83911 ? 46  ARG   A CA  1 
ATOM   250  C C   . ARG   A 1 39  ? -1.72164  -9.87792  -13.55555 1.000 19.66816 ? 46  ARG   A C   1 
ATOM   251  O O   . ARG   A 1 39  ? -2.15968  -9.08779  -14.41068 1.000 15.43107 ? 46  ARG   A O   1 
ATOM   252  C CB  . ARG   A 1 39  ? -2.11973  -9.49072  -11.08385 1.000 18.88781 ? 46  ARG   A CB  1 
ATOM   253  C CG  . ARG   A 1 39  ? -2.15305  -7.96662  -11.24966 1.000 27.33856 ? 46  ARG   A CG  1 
ATOM   254  C CD  . ARG   A 1 39  ? -1.44282  -7.18105  -10.14123 1.000 27.08506 ? 46  ARG   A CD  1 
ATOM   255  N NE  . ARG   A 1 39  ? -0.02152  -7.50536  -10.07878 1.000 28.14707 ? 46  ARG   A NE  1 
ATOM   256  C CZ  . ARG   A 1 39  ? 0.73788   -7.38715  -8.99726  1.000 35.73591 ? 46  ARG   A CZ  1 
ATOM   257  N NH1 . ARG   A 1 39  ? 0.23877   -6.97878  -7.83621  1.000 29.13737 ? 46  ARG   A NH1 1 
ATOM   258  N NH2 . ARG   A 1 39  ? 2.03742   -7.66886  -9.08336  1.000 30.92011 ? 46  ARG   A NH2 1 
ATOM   259  N N   . GLU   A 1 40  ? -0.51162  -10.42220 -13.66349 1.000 14.96615 ? 47  GLU   A N   1 
ATOM   260  C CA  . GLU   A 1 40  ? 0.36085   -9.96955  -14.75553 1.000 15.07324 ? 47  GLU   A CA  1 
ATOM   261  C C   . GLU   A 1 40  ? -0.17664  -10.42638 -16.09355 1.000 16.72016 ? 47  GLU   A C   1 
ATOM   262  O O   . GLU   A 1 40  ? -0.09574  -9.70053  -17.09313 1.000 16.07319 ? 47  GLU   A O   1 
ATOM   263  C CB  . GLU   A 1 40  ? 1.78166   -10.49883 -14.58526 1.000 14.38617 ? 47  GLU   A CB  1 
ATOM   264  C CG  . GLU   A 1 40  ? 2.53532   -9.92196  -13.34117 1.000 15.83773 ? 47  GLU   A CG  1 
ATOM   265  C CD  . GLU   A 1 40  ? 2.46009   -8.39029  -13.21564 1.000 27.57704 ? 47  GLU   A CD  1 
ATOM   266  O OE1 . GLU   A 1 40  ? 2.62397   -7.69622  -14.24726 1.000 22.16688 ? 47  GLU   A OE1 1 
ATOM   267  O OE2 . GLU   A 1 40  ? 2.30148   -7.86582  -12.07432 1.000 29.14191 ? 47  GLU   A OE2 1 
ATOM   268  N N   . LEU   A 1 41  ? -0.71126  -11.63590 -16.13368 1.000 18.58604 ? 48  LEU   A N   1 
ATOM   269  C CA  . LEU   A 1 41  ? -1.15839  -12.14334 -17.41586 1.000 14.89829 ? 48  LEU   A CA  1 
ATOM   270  C C   . LEU   A 1 41  ? -2.47980  -11.51379 -17.80872 1.000 15.20471 ? 48  LEU   A C   1 
ATOM   271  O O   . LEU   A 1 41  ? -2.71451  -11.26985 -18.99585 1.000 17.35488 ? 48  LEU   A O   1 
ATOM   272  C CB  . LEU   A 1 41  ? -1.24835  -13.66812 -17.35893 1.000 15.10342 ? 48  LEU   A CB  1 
ATOM   273  C CG  . LEU   A 1 41  ? 0.09060   -14.39966 -17.15390 1.000 15.73577 ? 48  LEU   A CG  1 
ATOM   274  C CD1 . LEU   A 1 41  ? -0.13058  -15.92520 -16.98423 1.000 20.32346 ? 48  LEU   A CD1 1 
ATOM   275  C CD2 . LEU   A 1 41  ? 1.04410   -14.17934 -18.33094 1.000 16.68028 ? 48  LEU   A CD2 1 
ATOM   276  N N   . ILE   A 1 42  ? -3.35026  -11.23472 -16.83758 1.000 13.31421 ? 49  ILE   A N   1 
ATOM   277  C CA  . ILE   A 1 42  ? -4.59058  -10.55132 -17.17866 1.000 16.96957 ? 49  ILE   A CA  1 
ATOM   278  C C   . ILE   A 1 42  ? -4.28523  -9.13769  -17.65430 1.000 20.45141 ? 49  ILE   A C   1 
ATOM   279  O O   . ILE   A 1 42  ? -4.91018  -8.62688  -18.60573 1.000 15.14825 ? 49  ILE   A O   1 
ATOM   280  C CB  . ILE   A 1 42  ? -5.54219  -10.59445 -15.96429 1.000 14.82693 ? 49  ILE   A CB  1 
ATOM   281  C CG1 . ILE   A 1 42  ? -6.05240  -12.03684 -15.79105 1.000 14.90493 ? 49  ILE   A CG1 1 
ATOM   282  C CG2 . ILE   A 1 42  ? -6.70243  -9.60093  -16.12251 1.000 15.05403 ? 49  ILE   A CG2 1 
ATOM   283  C CD1 . ILE   A 1 42  ? -6.96170  -12.28619 -14.52069 1.000 16.63757 ? 49  ILE   A CD1 1 
ATOM   284  N N   . SER   A 1 43  ? -3.28714  -8.49589  -17.02540 1.000 13.07931 ? 50  SER   A N   1 
ATOM   285  C CA  . SER   A 1 43  ? -2.86008  -7.16803  -17.46122 1.000 18.41140 ? 50  SER   A CA  1 
ATOM   286  C C   . SER   A 1 43  ? -2.35474  -7.20075  -18.90276 1.000 20.14101 ? 50  SER   A C   1 
ATOM   287  O O   . SER   A 1 43  ? -2.69273  -6.31883  -19.71799 1.000 15.84851 ? 50  SER   A O   1 
ATOM   288  C CB  . SER   A 1 43  ? -1.78834  -6.64392  -16.47830 1.000 16.99526 ? 50  SER   A CB  1 
ATOM   289  O OG  . SER   A 1 43  ? -1.23700  -5.41526  -16.93032 1.000 31.66102 ? 50  SER   A OG  1 
ATOM   290  N N   . ASN   A 1 44  ? -1.58944  -8.24641  -19.25021 1.000 15.48645 ? 51  ASN   A N   1 
ATOM   291  C CA  . ASN   A 1 44  ? -1.12051  -8.38975  -20.62849 1.000 19.06239 ? 51  ASN   A CA  1 
ATOM   292  C C   . ASN   A 1 44  ? -2.28986  -8.59343  -21.58470 1.000 17.78199 ? 51  ASN   A C   1 
ATOM   293  O O   . ASN   A 1 44  ? -2.30360  -8.01892  -22.67824 1.000 18.60037 ? 51  ASN   A O   1 
ATOM   294  C CB  . ASN   A 1 44  ? -0.12033  -9.54585  -20.74306 1.000 18.05166 ? 51  ASN   A CB  1 
ATOM   295  C CG  . ASN   A 1 44  ? 1.26953   -9.15855  -20.23856 1.000 24.69380 ? 51  ASN   A CG  1 
ATOM   296  O OD1 . ASN   A 1 44  ? 1.47300   -8.04540  -19.73335 1.000 21.51099 ? 51  ASN   A OD1 1 
ATOM   297  N ND2 . ASN   A 1 44  ? 2.22679   -10.07218 -20.36794 1.000 23.04318 ? 51  ASN   A ND2 1 
ATOM   298  N N   . SER   A 1 45  ? -3.28818  -9.38446  -21.18430 1.000 16.19676 ? 52  SER   A N   1 
ATOM   299  C CA  . SER   A 1 45  ? -4.47259  -9.58155  -22.03544 1.000 14.80177 ? 52  SER   A CA  1 
ATOM   300  C C   . SER   A 1 45  ? -5.22981  -8.27537  -22.22332 1.000 20.18123 ? 52  SER   A C   1 
ATOM   301  O O   . SER   A 1 45  ? -5.66154  -7.93134  -23.33323 1.000 16.28662 ? 52  SER   A O   1 
ATOM   302  C CB  . SER   A 1 45  ? -5.39294  -10.61761 -21.38703 1.000 18.78884 ? 52  SER   A CB  1 
ATOM   303  O OG  . SER   A 1 45  ? -4.83560  -11.91158 -21.48971 1.000 19.72968 ? 52  SER   A OG  1 
ATOM   304  N N   . SER   A 1 46  ? -5.41595  -7.53968  -21.13308 1.000 12.72254 ? 53  SER   A N   1 
ATOM   305  C CA  . SER   A 1 46  ? -6.07167  -6.23984  -21.20722 1.000 14.79881 ? 53  SER   A CA  1 
ATOM   306  C C   . SER   A 1 46  ? -5.33730  -5.30249  -22.16472 1.000 18.41272 ? 53  SER   A C   1 
ATOM   307  O O   . SER   A 1 46  ? -5.97370  -4.65602  -23.00590 1.000 18.45465 ? 53  SER   A O   1 
ATOM   308  C CB  . SER   A 1 46  ? -6.15764  -5.64016  -19.80531 1.000 17.87590 ? 53  SER   A CB  1 
ATOM   309  O OG  . SER   A 1 46  ? -6.86756  -4.41643  -19.82425 1.000 19.68881 ? 53  SER   A OG  1 
ATOM   310  N N   . ASP   A 1 47  ? -3.99622  -5.24439  -22.08261 1.000 14.82350 ? 54  ASP   A N   1 
ATOM   311  C CA  . ASP   A 1 47  ? -3.23922  -4.40323  -23.02076 1.000 15.64352 ? 54  ASP   A CA  1 
ATOM   312  C C   . ASP   A 1 47  ? -3.48668  -4.81762  -24.47695 1.000 19.76334 ? 54  ASP   A C   1 
ATOM   313  O O   . ASP   A 1 47  ? -3.62356  -3.95774  -25.37009 1.000 16.24950 ? 54  ASP   A O   1 
ATOM   314  C CB  . ASP   A 1 47  ? -1.74720  -4.49041  -22.71278 1.000 15.41533 ? 54  ASP   A CB  1 
ATOM   315  C CG  . ASP   A 1 47  ? -1.37087  -3.82200  -21.39305 1.000 24.79635 ? 54  ASP   A CG  1 
ATOM   316  O OD1 . ASP   A 1 47  ? -2.24737  -3.15363  -20.79466 1.000 23.48104 ? 54  ASP   A OD1 1 
ATOM   317  O OD2 . ASP   A 1 47  ? -0.19999  -3.98890  -20.94883 1.000 22.30320 ? 54  ASP   A OD2 1 
ATOM   318  N N   . ALA   A 1 48  ? -3.49781  -6.12832  -24.74108 1.000 15.52819 ? 55  ALA   A N   1 
ATOM   319  C CA  . ALA   A 1 48  ? -3.70533  -6.62471  -26.10712 1.000 14.05921 ? 55  ALA   A CA  1 
ATOM   320  C C   . ALA   A 1 48  ? -5.10033  -6.29581  -26.59786 1.000 18.95593 ? 55  ALA   A C   1 
ATOM   321  O O   . ALA   A 1 48  ? -5.29748  -6.01161  -27.78161 1.000 17.50454 ? 55  ALA   A O   1 
ATOM   322  C CB  . ALA   A 1 48  ? -3.49766  -8.14767  -26.16526 1.000 13.32313 ? 55  ALA   A CB  1 
ATOM   323  N N   . LEU   A 1 49  ? -6.08798  -6.37790  -25.71196 1.000 15.36108 ? 56  LEU   A N   1 
ATOM   324  C CA  . LEU   A 1 49  ? -7.44245  -5.95653  -26.05694 1.000 17.03032 ? 56  LEU   A CA  1 
ATOM   325  C C   . LEU   A 1 49  ? -7.50541  -4.45434  -26.32862 1.000 18.42000 ? 56  LEU   A C   1 
ATOM   326  O O   . LEU   A 1 49  ? -8.13004  -4.02287  -27.30273 1.000 16.19900 ? 56  LEU   A O   1 
ATOM   327  C CB  . LEU   A 1 49  ? -8.40516  -6.35050  -24.92971 1.000 15.55594 ? 56  LEU   A CB  1 
ATOM   328  C CG  . LEU   A 1 49  ? -8.60744  -7.88102  -24.84732 1.000 14.74309 ? 56  LEU   A CG  1 
ATOM   329  C CD1 . LEU   A 1 49  ? -9.13274  -8.23194  -23.47449 1.000 16.92076 ? 56  LEU   A CD1 1 
ATOM   330  C CD2 . LEU   A 1 49  ? -9.62130  -8.29768  -25.89475 1.000 13.66894 ? 56  LEU   A CD2 1 
ATOM   331  N N   . ASP   A 1 50  ? -6.87716  -3.63921  -25.47298 1.000 17.55501 ? 57  ASP   A N   1 
ATOM   332  C CA  . ASP   A 1 50  ? -6.78331  -2.20046  -25.75102 1.000 17.58535 ? 57  ASP   A CA  1 
ATOM   333  C C   . ASP   A 1 50  ? -6.25399  -1.93474  -27.15948 1.000 17.74156 ? 57  ASP   A C   1 
ATOM   334  O O   . ASP   A 1 50  ? -6.70660  -1.00537  -27.84039 1.000 17.10456 ? 57  ASP   A O   1 
ATOM   335  C CB  . ASP   A 1 50  ? -5.86046  -1.51631  -24.75303 1.000 15.04377 ? 57  ASP   A CB  1 
ATOM   336  C CG  . ASP   A 1 50  ? -6.46861  -1.38188  -23.38618 1.000 24.74845 ? 57  ASP   A CG  1 
ATOM   337  O OD1 . ASP   A 1 50  ? -7.69811  -1.56934  -23.22485 1.000 21.95705 ? 57  ASP   A OD1 1 
ATOM   338  O OD2 . ASP   A 1 50  ? -5.69677  -1.07174  -22.46353 1.000 23.05301 ? 57  ASP   A OD2 1 
ATOM   339  N N   . LYS   A 1 51  ? -5.25948  -2.71191  -27.59286 1.000 16.67217 ? 58  LYS   A N   1 
ATOM   340  C CA  . LYS   A 1 51  ? -4.59250  -2.39458  -28.85710 1.000 16.71972 ? 58  LYS   A CA  1 
ATOM   341  C C   . LYS   A 1 51  ? -5.50090  -2.66023  -30.04470 1.000 18.99222 ? 58  LYS   A C   1 
ATOM   342  O O   . LYS   A 1 51  ? -5.54855  -1.86296  -30.99887 1.000 18.16742 ? 58  LYS   A O   1 
ATOM   343  C CB  . LYS   A 1 51  ? -3.29413  -3.20334  -29.00083 1.000 18.78639 ? 58  LYS   A CB  1 
ATOM   344  C CG  . LYS   A 1 51  ? -2.17942  -2.74629  -28.05932 1.000 32.30360 ? 58  LYS   A CG  1 
ATOM   345  C CD  . LYS   A 1 51  ? -0.89306  -3.57194  -28.22051 1.000 40.67303 ? 58  LYS   A CD  1 
ATOM   346  C CE  . LYS   A 1 51  ? -0.11951  -3.65112  -26.89957 1.000 42.27350 ? 58  LYS   A CE  1 
ATOM   347  N NZ  . LYS   A 1 51  ? 1.19774   -4.29375  -27.08245 1.000 38.03012 ? 58  LYS   A NZ  1 
ATOM   348  N N   . ILE   A 1 52  ? -6.18699  -3.79784  -30.04101 1.000 16.83041 ? 59  ILE   A N   1 
ATOM   349  C CA  . ILE   A 1 52  ? -7.05932  -4.09068  -31.18101 1.000 18.88824 ? 59  ILE   A CA  1 
ATOM   350  C C   . ILE   A 1 52  ? -8.28000  -3.17611  -31.13787 1.000 17.45279 ? 59  ILE   A C   1 
ATOM   351  O O   . ILE   A 1 52  ? -8.80561  -2.75861  -32.18464 1.000 19.10739 ? 59  ILE   A O   1 
ATOM   352  C CB  . ILE   A 1 52  ? -7.44545  -5.59474  -31.22692 1.000 20.09656 ? 59  ILE   A CB  1 
ATOM   353  C CG1 . ILE   A 1 52  ? -8.13252  -5.97371  -32.55315 1.000 23.73121 ? 59  ILE   A CG1 1 
ATOM   354  C CG2 . ILE   A 1 52  ? -8.36245  -6.03441  -30.05288 1.000 16.07683 ? 59  ILE   A CG2 1 
ATOM   355  C CD1 . ILE   A 1 52  ? -7.22149  -5.73734  -33.80115 1.000 20.63534 ? 59  ILE   A CD1 1 
ATOM   356  N N   . ARG   A 1 53  ? -8.77336  -2.86751  -29.93661 1.000 16.09462 ? 60  ARG   A N   1 
ATOM   357  C CA  . ARG   A 1 53  ? -9.86927  -1.91053  -29.83732 1.000 18.49275 ? 60  ARG   A CA  1 
ATOM   358  C C   . ARG   A 1 53  ? -9.50532  -0.57108  -30.46832 1.000 21.74765 ? 60  ARG   A C   1 
ATOM   359  O O   . ARG   A 1 53  ? -10.29185 0.00481   -31.22423 1.000 21.48531 ? 60  ARG   A O   1 
ATOM   360  C CB  . ARG   A 1 53  ? -10.27271 -1.70323  -28.38155 1.000 17.51471 ? 60  ARG   A CB  1 
ATOM   361  C CG  . ARG   A 1 53  ? -11.58992 -0.96426  -28.30433 1.000 25.66826 ? 60  ARG   A CG  1 
ATOM   362  C CD  . ARG   A 1 53  ? -11.93077 -0.44651  -26.92985 1.000 28.55085 ? 60  ARG   A CD  1 
ATOM   363  N NE  . ARG   A 1 53  ? -10.75517 -0.13735  -26.12646 1.000 50.83679 ? 60  ARG   A NE  1 
ATOM   364  C CZ  . ARG   A 1 53  ? -10.80547 0.13499   -24.82822 1.000 54.07625 ? 60  ARG   A CZ  1 
ATOM   365  N NH1 . ARG   A 1 53  ? -11.94851 0.06268   -24.15998 1.000 41.08922 ? 60  ARG   A NH1 1 
ATOM   366  N NH2 . ARG   A 1 53  ? -9.68392  0.49418   -24.18756 1.000 30.12230 ? 60  ARG   A NH2 1 
ATOM   367  N N   . TYR   A 1 54  ? -8.32110  -0.05229  -30.15478 1.000 19.37386 ? 61  TYR   A N   1 
ATOM   368  C CA  . TYR   A 1 54  ? -7.93760  1.24106   -30.70034 1.000 17.98961 ? 61  TYR   A CA  1 
ATOM   369  C C   . TYR   A 1 54  ? -7.74276  1.14948   -32.21215 1.000 20.49589 ? 61  TYR   A C   1 
ATOM   370  O O   . TYR   A 1 54  ? -8.25697  1.99191   -32.95860 1.000 19.28986 ? 61  TYR   A O   1 
ATOM   371  C CB  . TYR   A 1 54  ? -6.67226  1.75065   -29.99227 1.000 20.24773 ? 61  TYR   A CB  1 
ATOM   372  C CG  . TYR   A 1 54  ? -6.00532  2.94391   -30.65383 1.000 25.79938 ? 61  TYR   A CG  1 
ATOM   373  C CD1 . TYR   A 1 54  ? -4.98825  2.77290   -31.58826 1.000 34.86362 ? 61  TYR   A CD1 1 
ATOM   374  C CD2 . TYR   A 1 54  ? -6.40499  4.24018   -30.35362 1.000 34.31335 ? 61  TYR   A CD2 1 
ATOM   375  C CE1 . TYR   A 1 54  ? -4.38508  3.87277   -32.20436 1.000 43.52323 ? 61  TYR   A CE1 1 
ATOM   376  C CE2 . TYR   A 1 54  ? -5.81553  5.34050   -30.95325 1.000 34.18306 ? 61  TYR   A CE2 1 
ATOM   377  C CZ  . TYR   A 1 54  ? -4.80004  5.15423   -31.87252 1.000 42.97035 ? 61  TYR   A CZ  1 
ATOM   378  O OH  . TYR   A 1 54  ? -4.19354  6.24913   -32.48715 1.000 47.94997 ? 61  TYR   A OH  1 
ATOM   379  N N   . GLU   A 1 55  ? -7.06320  0.10233   -32.69116 1.000 21.97348 ? 62  GLU   A N   1 
ATOM   380  C CA  . GLU   A 1 55  ? -6.84072  -0.00744  -34.13670 1.000 23.09612 ? 62  GLU   A CA  1 
ATOM   381  C C   . GLU   A 1 55  ? -8.15715  -0.07488  -34.90115 1.000 24.38934 ? 62  GLU   A C   1 
ATOM   382  O O   . GLU   A 1 55  ? -8.25393  0.44214   -36.02992 1.000 21.26497 ? 62  GLU   A O   1 
ATOM   383  C CB  . GLU   A 1 55  ? -5.97750  -1.23686  -34.45080 1.000 24.00830 ? 62  GLU   A CB  1 
ATOM   384  C CG  . GLU   A 1 55  ? -4.49005  -1.04655  -34.12262 1.000 26.41249 ? 62  GLU   A CG  1 
ATOM   385  C CD  . GLU   A 1 55  ? -3.56197  -2.10755  -34.73910 1.000 39.07765 ? 62  GLU   A CD  1 
ATOM   386  O OE1 . GLU   A 1 55  ? -4.03472  -2.97252  -35.51847 1.000 33.73038 ? 62  GLU   A OE1 1 
ATOM   387  O OE2 . GLU   A 1 55  ? -2.35512  -2.09363  -34.40332 1.000 49.11902 ? 62  GLU   A OE2 1 
ATOM   388  N N   . SER   A 1 56  ? -9.18529  -0.68849  -34.30451 1.000 20.30568 ? 63  SER   A N   1 
ATOM   389  C CA  . SER   A 1 56  ? -10.46725 -0.85942  -35.00124 1.000 27.83613 ? 63  SER   A CA  1 
ATOM   390  C C   . SER   A 1 56  ? -11.22935 0.45050   -35.17537 1.000 29.08057 ? 63  SER   A C   1 
ATOM   391  O O   . SER   A 1 56  ? -12.11122 0.53146   -36.04707 1.000 26.64691 ? 63  SER   A O   1 
ATOM   392  C CB  . SER   A 1 56  ? -11.34817 -1.86285  -34.24693 1.000 25.17805 ? 63  SER   A CB  1 
ATOM   393  O OG  . SER   A 1 56  ? -11.82530 -1.28286  -33.04970 1.000 27.18130 ? 63  SER   A OG  1 
ATOM   394  N N   . LEU   A 1 57  ? -10.90708 1.47940   -34.38571 1.000 24.12633 ? 64  LEU   A N   1 
ATOM   395  C CA  . LEU   A 1 57  ? -11.56294 2.78287   -34.55292 1.000 26.54662 ? 64  LEU   A CA  1 
ATOM   396  C C   . LEU   A 1 57  ? -11.25694 3.39795   -35.91472 1.000 33.22834 ? 64  LEU   A C   1 
ATOM   397  O O   . LEU   A 1 57  ? -12.08934 4.12432   -36.47226 1.000 34.46738 ? 64  LEU   A O   1 
ATOM   398  C CB  . LEU   A 1 57  ? -11.11964 3.74505   -33.44922 1.000 23.88357 ? 64  LEU   A CB  1 
ATOM   399  C CG  . LEU   A 1 57  ? -11.49279 3.27312   -32.03726 1.000 26.00422 ? 64  LEU   A CG  1 
ATOM   400  C CD1 . LEU   A 1 57  ? -11.10903 4.31230   -30.97363 1.000 31.60741 ? 64  LEU   A CD1 1 
ATOM   401  C CD2 . LEU   A 1 57  ? -12.96889 2.90407   -31.95316 1.000 34.19098 ? 64  LEU   A CD2 1 
ATOM   402  N N   . THR   A 1 58  ? -10.06733 3.15047   -36.46409 1.000 26.90085 ? 65  THR   A N   1 
ATOM   403  C CA  . THR   A 1 58  ? -9.76479  3.67962   -37.79034 1.000 31.02683 ? 65  THR   A CA  1 
ATOM   404  C C   . THR   A 1 58  ? -9.83494  2.63438   -38.89330 1.000 33.91722 ? 65  THR   A C   1 
ATOM   405  O O   . THR   A 1 58  ? -9.86175  3.00756   -40.07412 1.000 35.46853 ? 65  THR   A O   1 
ATOM   406  C CB  . THR   A 1 58  ? -8.39818  4.38773   -37.78801 1.000 40.14190 ? 65  THR   A CB  1 
ATOM   407  O OG1 . THR   A 1 58  ? -7.35889  3.43426   -37.60459 1.000 41.83352 ? 65  THR   A OG1 1 
ATOM   408  C CG2 . THR   A 1 58  ? -8.31979  5.41132   -36.68741 1.000 33.01925 ? 65  THR   A CG2 1 
ATOM   409  N N   . ASP   A 1 59  ? -9.92717  1.34982   -38.55385 1.000 34.51784 ? 66  ASP   A N   1 
ATOM   410  C CA  . ASP   A 1 59  ? -10.08579 0.30245   -39.56338 1.000 32.10611 ? 66  ASP   A CA  1 
ATOM   411  C C   . ASP   A 1 59  ? -11.02742 -0.75004  -38.99060 1.000 32.64412 ? 66  ASP   A C   1 
ATOM   412  O O   . ASP   A 1 59  ? -10.58400 -1.74480  -38.40474 1.000 27.72522 ? 66  ASP   A O   1 
ATOM   413  C CB  . ASP   A 1 59  ? -8.73282  -0.30751  -39.94457 1.000 33.27405 ? 66  ASP   A CB  1 
ATOM   414  C CG  . ASP   A 1 59  ? -8.84515  -1.32693  -41.06501 1.000 45.91258 ? 66  ASP   A CG  1 
ATOM   415  O OD1 . ASP   A 1 59  ? -9.98660  -1.66212  -41.44925 1.000 38.29820 ? 66  ASP   A OD1 1 
ATOM   416  O OD2 . ASP   A 1 59  ? -7.79380  -1.78167  -41.56683 1.000 44.22655 ? 66  ASP   A OD2 1 
ATOM   417  N N   . PRO   A 1 60  ? -12.34312 -0.55750  -39.13743 1.000 35.47195 ? 67  PRO   A N   1 
ATOM   418  C CA  . PRO   A 1 60  ? -13.30205 -1.50634  -38.53714 1.000 33.62813 ? 67  PRO   A CA  1 
ATOM   419  C C   . PRO   A 1 60  ? -13.07887 -2.94303  -38.96681 1.000 31.46905 ? 67  PRO   A C   1 
ATOM   420  O O   . PRO   A 1 60  ? -13.40117 -3.87373  -38.22343 1.000 31.75907 ? 67  PRO   A O   1 
ATOM   421  C CB  . PRO   A 1 60  ? -14.65531 -0.98959  -39.04840 1.000 37.99954 ? 67  PRO   A CB  1 
ATOM   422  C CG  . PRO   A 1 60  ? -14.45175 0.46715   -39.19874 1.000 45.52753 ? 67  PRO   A CG  1 
ATOM   423  C CD  . PRO   A 1 60  ? -13.00645 0.67037   -39.60917 1.000 37.38128 ? 67  PRO   A CD  1 
ATOM   424  N N   . SER   A 1 61  ? -12.53081 -3.14682  -40.15424 1.000 29.25744 ? 68  SER   A N   1 
ATOM   425  C CA  . SER   A 1 61  ? -12.32943 -4.49080  -40.66616 1.000 28.76559 ? 68  SER   A CA  1 
ATOM   426  C C   . SER   A 1 61  ? -11.35983 -5.30513  -39.81422 1.000 39.16839 ? 68  SER   A C   1 
ATOM   427  O O   . SER   A 1 61  ? -11.36234 -6.53485  -39.91945 1.000 28.05710 ? 68  SER   A O   1 
ATOM   428  C CB  . SER   A 1 61  ? -11.90893 -4.37231  -42.14210 1.000 36.61851 ? 68  SER   A CB  1 
ATOM   429  O OG  . SER   A 1 61  ? -10.51807 -4.17620  -42.30848 1.000 38.34298 ? 68  SER   A OG  1 
ATOM   430  N N   . LYS   A 1 62  ? -10.59354 -4.66752  -38.92006 1.000 25.89998 ? 69  LYS   A N   1 
ATOM   431  C CA  . LYS   A 1 62  ? -9.72277  -5.40920  -38.01942 1.000 27.00794 ? 69  LYS   A CA  1 
ATOM   432  C C   . LYS   A 1 62  ? -10.49424 -6.30239  -37.05831 1.000 27.90706 ? 69  LYS   A C   1 
ATOM   433  O O   . LYS   A 1 62  ? -9.90769  -7.21687  -36.47464 1.000 25.62222 ? 69  LYS   A O   1 
ATOM   434  C CB  . LYS   A 1 62  ? -8.82495  -4.43873  -37.24997 1.000 26.87364 ? 69  LYS   A CB  1 
ATOM   435  C CG  . LYS   A 1 62  ? -7.88180  -3.73396  -38.20410 1.000 30.82200 ? 69  LYS   A CG  1 
ATOM   436  C CD  . LYS   A 1 62  ? -6.55330  -3.43630  -37.60850 1.000 28.86023 ? 69  LYS   A CD  1 
ATOM   437  C CE  . LYS   A 1 62  ? -5.68605  -2.72623  -38.61239 1.000 34.93512 ? 69  LYS   A CE  1 
ATOM   438  N NZ  . LYS   A 1 62  ? -4.42623  -2.35330  -37.96455 1.000 43.56707 ? 69  LYS   A NZ  1 
ATOM   439  N N   . LEU   A 1 63  ? -11.79137 -6.06828  -36.89298 1.000 24.84635 ? 70  LEU   A N   1 
ATOM   440  C CA  . LEU   A 1 63  ? -12.62637 -6.89537  -36.04253 1.000 22.71267 ? 70  LEU   A CA  1 
ATOM   441  C C   . LEU   A 1 63  ? -13.38556 -7.95707  -36.84711 1.000 33.25349 ? 70  LEU   A C   1 
ATOM   442  O O   . LEU   A 1 63  ? -14.25637 -8.62609  -36.29309 1.000 24.13868 ? 70  LEU   A O   1 
ATOM   443  C CB  . LEU   A 1 63  ? -13.60128 -6.00529  -35.26574 1.000 24.34373 ? 70  LEU   A CB  1 
ATOM   444  C CG  . LEU   A 1 63  ? -12.96792 -5.11007  -34.18019 1.000 23.95760 ? 70  LEU   A CG  1 
ATOM   445  C CD1 . LEU   A 1 63  ? -14.04302 -4.29332  -33.45352 1.000 27.87675 ? 70  LEU   A CD1 1 
ATOM   446  C CD2 . LEU   A 1 63  ? -12.19397 -5.95930  -33.18101 1.000 25.69098 ? 70  LEU   A CD2 1 
ATOM   447  N N   . ASP   A 1 64  ? -13.07525 -8.11674  -38.14145 1.000 27.97194 ? 71  ASP   A N   1 
ATOM   448  C CA  . ASP   A 1 64  ? -13.68456 -9.18971  -38.93413 1.000 30.03133 ? 71  ASP   A CA  1 
ATOM   449  C C   . ASP   A 1 64  ? -13.36887 -10.56124 -38.35637 1.000 28.92233 ? 71  ASP   A C   1 
ATOM   450  O O   . ASP   A 1 64  ? -14.14878 -11.50392 -38.52324 1.000 31.87392 ? 71  ASP   A O   1 
ATOM   451  C CB  . ASP   A 1 64  ? -13.20059 -9.13016  -40.38266 1.000 30.03492 ? 71  ASP   A CB  1 
ATOM   452  C CG  . ASP   A 1 64  ? -13.79385 -7.97541  -41.13686 1.000 45.57274 ? 71  ASP   A CG  1 
ATOM   453  O OD1 . ASP   A 1 64  ? -14.68624 -7.30688  -40.57152 1.000 38.39033 ? 71  ASP   A OD1 1 
ATOM   454  O OD2 . ASP   A 1 64  ? -13.36124 -7.72889  -42.28572 1.000 45.03227 ? 71  ASP   A OD2 1 
ATOM   455  N N   . SER   A 1 65  ? -12.22899 -10.69029 -37.68501 1.000 26.93687 ? 72  SER   A N   1 
ATOM   456  C CA  . SER   A 1 65  ? -11.79469 -11.93027 -37.05445 1.000 27.76945 ? 72  SER   A CA  1 
ATOM   457  C C   . SER   A 1 65  ? -12.37736 -12.11431 -35.64626 1.000 34.85485 ? 72  SER   A C   1 
ATOM   458  O O   . SER   A 1 65  ? -11.93083 -12.99723 -34.90734 1.000 35.82092 ? 72  SER   A O   1 
ATOM   459  C CB  . SER   A 1 65  ? -10.26509 -11.95065 -36.99407 1.000 34.34922 ? 72  SER   A CB  1 
ATOM   460  O OG  . SER   A 1 65  ? -9.77988  -10.72763 -36.42024 1.000 25.94484 ? 72  SER   A OG  1 
ATOM   461  N N   . GLY   A 1 66  ? -13.33171 -11.27256 -35.24552 1.000 30.44324 ? 73  GLY   A N   1 
ATOM   462  C CA  . GLY   A 1 66  ? -14.02488 -11.44738 -33.98519 1.000 27.94514 ? 73  GLY   A CA  1 
ATOM   463  C C   . GLY   A 1 66  ? -14.27753 -10.11373 -33.30448 1.000 29.06903 ? 73  GLY   A C   1 
ATOM   464  O O   . GLY   A 1 66  ? -13.33778 -9.35731  -33.04444 1.000 28.63410 ? 73  GLY   A O   1 
ATOM   465  N N   . LYS   A 1 67  ? -15.54404 -9.79273  -33.04352 1.000 25.28347 ? 74  LYS   A N   1 
ATOM   466  C CA  . LYS   A 1 67  ? -15.89180 -8.48604  -32.50388 1.000 28.81948 ? 74  LYS   A CA  1 
ATOM   467  C C   . LYS   A 1 67  ? -15.84054 -8.45868  -30.98153 1.000 30.02469 ? 74  LYS   A C   1 
ATOM   468  O O   . LYS   A 1 67  ? -15.65903 -7.38826  -30.39677 1.000 27.79273 ? 74  LYS   A O   1 
ATOM   469  C CB  . LYS   A 1 67  ? -17.29307 -8.08348  -32.98495 1.000 37.23545 ? 74  LYS   A CB  1 
ATOM   470  C CG  . LYS   A 1 67  ? -17.28988 -7.40878  -34.36806 1.000 49.89712 ? 74  LYS   A CG  1 
ATOM   471  C CD  . LYS   A 1 67  ? -18.47324 -6.45930  -34.59697 1.000 61.94979 ? 74  LYS   A CD  1 
ATOM   472  C CE  . LYS   A 1 67  ? -18.09945 -4.97044  -34.39977 1.000 63.12081 ? 74  LYS   A CE  1 
ATOM   473  N NZ  . LYS   A 1 67  ? -17.75279 -4.59753  -32.97546 1.000 54.82876 ? 74  LYS   A NZ  1 
ATOM   474  N N   . GLU   A 1 68  ? -15.96086 -9.60849  -30.33518 1.000 21.91044 ? 75  GLU   A N   1 
ATOM   475  C CA  . GLU   A 1 68  ? -16.01536 -9.66290  -28.87287 1.000 23.39791 ? 75  GLU   A CA  1 
ATOM   476  C C   . GLU   A 1 68  ? -14.62943 -9.48742  -28.27839 1.000 21.21835 ? 75  GLU   A C   1 
ATOM   477  O O   . GLU   A 1 68  ? -13.66943 -10.12237 -28.72756 1.000 23.69302 ? 75  GLU   A O   1 
ATOM   478  C CB  . GLU   A 1 68  ? -16.62516 -11.00123 -28.46827 1.000 26.32468 ? 75  GLU   A CB  1 
ATOM   479  C CG  . GLU   A 1 68  ? -18.06524 -11.08302 -28.93997 1.000 35.27612 ? 75  GLU   A CG  1 
ATOM   480  C CD  . GLU   A 1 68  ? -18.23068 -12.00938 -30.13935 1.000 64.81161 ? 75  GLU   A CD  1 
ATOM   481  O OE1 . GLU   A 1 68  ? -17.26371 -12.16085 -30.92629 1.000 57.30887 ? 75  GLU   A OE1 1 
ATOM   482  O OE2 . GLU   A 1 68  ? -19.33123 -12.57328 -30.30731 1.000 82.78946 ? 75  GLU   A OE2 1 
ATOM   483  N N   . LEU   A 1 69  ? -14.52356 -8.62839  -27.25572 1.000 19.85668 ? 76  LEU   A N   1 
ATOM   484  C CA  . LEU   A 1 69  ? -13.26007 -8.31222  -26.59969 1.000 17.72063 ? 76  LEU   A CA  1 
ATOM   485  C C   . LEU   A 1 69  ? -13.39165 -8.81620  -25.17127 1.000 18.94131 ? 76  LEU   A C   1 
ATOM   486  O O   . LEU   A 1 69  ? -14.12259 -8.21400  -24.37531 1.000 19.38209 ? 76  LEU   A O   1 
ATOM   487  C CB  . LEU   A 1 69  ? -12.99104 -6.80166  -26.61358 1.000 18.67623 ? 76  LEU   A CB  1 
ATOM   488  C CG  . LEU   A 1 69  ? -12.92906 -6.14823  -28.01810 1.000 18.17906 ? 76  LEU   A CG  1 
ATOM   489  C CD1 . LEU   A 1 69  ? -12.56411 -4.65603  -27.89735 1.000 21.47881 ? 76  LEU   A CD1 1 
ATOM   490  C CD2 . LEU   A 1 69  ? -11.94803 -6.89048  -28.90127 1.000 17.30485 ? 76  LEU   A CD2 1 
ATOM   491  N N   . HIS   A 1 70  ? -12.74222 -9.93486  -24.84783 1.000 16.74686 ? 77  HIS   A N   1 
ATOM   492  C CA  . HIS   A 1 70  ? -12.99792 -10.52074 -23.53479 1.000 18.01165 ? 77  HIS   A CA  1 
ATOM   493  C C   . HIS   A 1 70  ? -11.80108 -11.35739 -23.10946 1.000 20.75147 ? 77  HIS   A C   1 
ATOM   494  O O   . HIS   A 1 70  ? -10.86662 -11.58822 -23.87860 1.000 16.22654 ? 77  HIS   A O   1 
ATOM   495  C CB  . HIS   A 1 70  ? -14.28516 -11.36375 -23.51746 1.000 17.45231 ? 77  HIS   A CB  1 
ATOM   496  C CG  . HIS   A 1 70  ? -14.24722 -12.52809 -24.45121 1.000 19.23436 ? 77  HIS   A CG  1 
ATOM   497  N ND1 . HIS   A 1 70  ? -15.14411 -12.68121 -25.48528 1.000 24.91927 ? 77  HIS   A ND1 1 
ATOM   498  C CD2 . HIS   A 1 70  ? -13.40176 -13.58582 -24.52866 1.000 28.88764 ? 77  HIS   A CD2 1 
ATOM   499  C CE1 . HIS   A 1 70  ? -14.86700 -13.79038 -26.14890 1.000 25.87880 ? 77  HIS   A CE1 1 
ATOM   500  N NE2 . HIS   A 1 70  ? -13.80256 -14.34831 -25.60166 1.000 27.72235 ? 77  HIS   A NE2 1 
ATOM   501  N N   . ILE   A 1 71  ? -11.84096 -11.78731 -21.84591 1.000 18.23031 ? 78  ILE   A N   1 
ATOM   502  C CA  . ILE   A 1 71  ? -10.81193 -12.63375 -21.24511 1.000 14.15290 ? 78  ILE   A CA  1 
ATOM   503  C C   . ILE   A 1 71  ? -11.51705 -13.80698 -20.58344 1.000 19.56603 ? 78  ILE   A C   1 
ATOM   504  O O   . ILE   A 1 71  ? -12.48006 -13.60122 -19.84083 1.000 17.75102 ? 78  ILE   A O   1 
ATOM   505  C CB  . ILE   A 1 71  ? -9.99618  -11.85841 -20.18173 1.000 14.21921 ? 78  ILE   A CB  1 
ATOM   506  C CG1 . ILE   A 1 71  ? -9.30730  -10.62777 -20.80319 1.000 17.40610 ? 78  ILE   A CG1 1 
ATOM   507  C CG2 . ILE   A 1 71  ? -9.01979  -12.79956 -19.47452 1.000 20.35148 ? 78  ILE   A CG2 1 
ATOM   508  C CD1 . ILE   A 1 71  ? -8.69332  -9.69012  -19.78167 1.000 17.24879 ? 78  ILE   A CD1 1 
ATOM   509  N N   . ASN   A 1 72  ? -11.05035 -15.02462 -20.84436 1.000 18.18984 ? 79  ASN   A N   1 
ATOM   510  C CA  . ASN   A 1 72  ? -11.60564 -16.22468 -20.22644 1.000 15.43389 ? 79  ASN   A CA  1 
ATOM   511  C C   . ASN   A 1 72  ? -10.51555 -16.93916 -19.44772 1.000 17.71664 ? 79  ASN   A C   1 
ATOM   512  O O   . ASN   A 1 72  ? -9.40100  -17.10638 -19.95121 1.000 17.94094 ? 79  ASN   A O   1 
ATOM   513  C CB  . ASN   A 1 72  ? -12.18463 -17.20336 -21.25770 1.000 17.33010 ? 79  ASN   A CB  1 
ATOM   514  C CG  . ASN   A 1 72  ? -13.36150 -16.62456 -22.00237 1.000 19.72872 ? 79  ASN   A CG  1 
ATOM   515  O OD1 . ASN   A 1 72  ? -14.08810 -15.80629 -21.46981 1.000 18.96752 ? 79  ASN   A OD1 1 
ATOM   516  N ND2 . ASN   A 1 72  ? -13.59843 -17.11162 -23.21367 1.000 19.61708 ? 79  ASN   A ND2 1 
ATOM   517  N N   . LEU   A 1 73  ? -10.86208 -17.39207 -18.23668 1.000 18.68790 ? 80  LEU   A N   1 
ATOM   518  C CA  . LEU   A 1 73  ? -9.97153  -18.17174 -17.37579 1.000 16.13183 ? 80  LEU   A CA  1 
ATOM   519  C C   . LEU   A 1 73  ? -10.52186 -19.58109 -17.30922 1.000 17.81082 ? 80  LEU   A C   1 
ATOM   520  O O   . LEU   A 1 73  ? -11.66838 -19.76201 -16.89453 1.000 16.72043 ? 80  LEU   A O   1 
ATOM   521  C CB  . LEU   A 1 73  ? -9.92596  -17.55654 -15.96588 1.000 18.23147 ? 80  LEU   A CB  1 
ATOM   522  C CG  . LEU   A 1 73  ? -9.56740  -16.06589 -15.99675 1.000 16.33118 ? 80  LEU   A CG  1 
ATOM   523  C CD1 . LEU   A 1 73  ? -9.59323  -15.52567 -14.56874 1.000 16.59209 ? 80  LEU   A CD1 1 
ATOM   524  C CD2 . LEU   A 1 73  ? -8.18752  -15.78398 -16.65814 1.000 14.95903 ? 80  LEU   A CD2 1 
ATOM   525  N N   . ILE   A 1 74  ? -9.71716  -20.56748 -17.71524 1.000 16.66548 ? 81  ILE   A N   1 
ATOM   526  C CA  . ILE   A 1 74  ? -10.17500 -21.94285 -17.90313 1.000 16.92162 ? 81  ILE   A CA  1 
ATOM   527  C C   . ILE   A 1 74  ? -9.27950  -22.90656 -17.13303 1.000 17.67688 ? 81  ILE   A C   1 
ATOM   528  O O   . ILE   A 1 74  ? -8.24617  -23.34465 -17.66149 1.000 20.62986 ? 81  ILE   A O   1 
ATOM   529  C CB  . ILE   A 1 74  ? -10.19422 -22.30189 -19.40315 1.000 19.19906 ? 81  ILE   A CB  1 
ATOM   530  C CG1 . ILE   A 1 74  ? -10.90281 -21.18889 -20.16225 1.000 21.45680 ? 81  ILE   A CG1 1 
ATOM   531  C CG2 . ILE   A 1 74  ? -10.88127 -23.63358 -19.61188 1.000 23.39690 ? 81  ILE   A CG2 1 
ATOM   532  C CD1 . ILE   A 1 74  ? -11.06281 -21.45974 -21.66580 1.000 33.76705 ? 81  ILE   A CD1 1 
ATOM   533  N N   . PRO   A 1 75  ? -9.61765  -23.25533 -15.89294 1.000 20.78954 ? 82  PRO   A N   1 
ATOM   534  C CA  . PRO   A 1 75  ? -8.84782  -24.27922 -15.17849 1.000 22.20496 ? 82  PRO   A CA  1 
ATOM   535  C C   . PRO   A 1 75  ? -9.24563  -25.67184 -15.63936 1.000 29.99853 ? 82  PRO   A C   1 
ATOM   536  O O   . PRO   A 1 75  ? -10.39664 -25.92883 -15.99395 1.000 25.87565 ? 82  PRO   A O   1 
ATOM   537  C CB  . PRO   A 1 75  ? -9.24980  -24.05137 -13.71674 1.000 26.45271 ? 82  PRO   A CB  1 
ATOM   538  C CG  . PRO   A 1 75  ? -10.67738 -23.57995 -13.81434 1.000 23.88669 ? 82  PRO   A CG  1 
ATOM   539  C CD  . PRO   A 1 75  ? -10.75592 -22.75991 -15.08876 1.000 18.18442 ? 82  PRO   A CD  1 
ATOM   540  N N   . ASN   A 1 76  ? -8.27423  -26.58781 -15.62116 1.000 22.32661 ? 83  ASN   A N   1 
ATOM   541  C CA  . ASN   A 1 76  ? -8.52270  -27.97590 -16.02057 1.000 24.61580 ? 83  ASN   A CA  1 
ATOM   542  C C   . ASN   A 1 76  ? -7.75232  -28.86222 -15.05473 1.000 26.51540 ? 83  ASN   A C   1 
ATOM   543  O O   . ASN   A 1 76  ? -6.53940  -29.02466 -15.20298 1.000 26.70224 ? 83  ASN   A O   1 
ATOM   544  C CB  . ASN   A 1 76  ? -8.09912  -28.24428 -17.46031 1.000 24.82846 ? 83  ASN   A CB  1 
ATOM   545  C CG  . ASN   A 1 76  ? -8.55280  -29.60252 -17.95458 1.000 33.87393 ? 83  ASN   A CG  1 
ATOM   546  O OD1 . ASN   A 1 76  ? -8.44004  -30.61091 -17.26116 1.000 34.94674 ? 83  ASN   A OD1 1 
ATOM   547  N ND2 . ASN   A 1 76  ? -9.07842  -29.62867 -19.16289 1.000 39.05546 ? 83  ASN   A ND2 1 
ATOM   548  N N   . LYS   A 1 77  ? -8.46384  -29.45857 -14.08644 1.000 27.53510 ? 84  LYS   A N   1 
ATOM   549  C CA  . LYS   A 1 77  ? -7.78688  -30.25426 -13.06772 1.000 28.24929 ? 84  LYS   A CA  1 
ATOM   550  C C   . LYS   A 1 77  ? -7.24459  -31.55843 -13.62625 1.000 36.73237 ? 84  LYS   A C   1 
ATOM   551  O O   . LYS   A 1 77  ? -6.26284  -32.08342 -13.09469 1.000 33.31104 ? 84  LYS   A O   1 
ATOM   552  C CB  . LYS   A 1 77  ? -8.71287  -30.56422 -11.89015 1.000 33.25476 ? 84  LYS   A CB  1 
ATOM   553  C CG  . LYS   A 1 77  ? -8.75447  -29.46856 -10.80738 1.000 40.71850 ? 84  LYS   A CG  1 
ATOM   554  C CD  . LYS   A 1 77  ? -9.89693  -29.71969 -9.81234  1.000 45.94791 ? 84  LYS   A CD  1 
ATOM   555  C CE  . LYS   A 1 77  ? -10.13453 -28.54859 -8.86563  1.000 54.22631 ? 84  LYS   A CE  1 
ATOM   556  N NZ  . LYS   A 1 77  ? -11.58833 -28.36898 -8.56244  1.000 57.06346 ? 84  LYS   A NZ  1 
ATOM   557  N N   . GLN   A 1 78  ? -7.88320  -32.11108 -14.65771 1.000 39.84868 ? 85  GLN   A N   1 
ATOM   558  C CA  . GLN   A 1 78  ? -7.39582  -33.35719 -15.25383 1.000 42.86210 ? 85  GLN   A CA  1 
ATOM   559  C C   . GLN   A 1 78  ? -6.06177  -33.14790 -15.95478 1.000 46.40576 ? 85  GLN   A C   1 
ATOM   560  O O   . GLN   A 1 78  ? -5.13330  -33.94195 -15.78727 1.000 36.55592 ? 85  GLN   A O   1 
ATOM   561  C CB  . GLN   A 1 78  ? -8.41632  -33.92038 -16.24003 1.000 49.73761 ? 85  GLN   A CB  1 
ATOM   562  C CG  . GLN   A 1 78  ? -9.50409  -34.80810 -15.64686 1.000 76.97755 ? 85  GLN   A CG  1 
ATOM   563  C CD  . GLN   A 1 78  ? -10.53250 -34.03486 -14.84010 1.000 95.97230 ? 85  GLN   A CD  1 
ATOM   564  O OE1 . GLN   A 1 78  ? -11.06369 -33.01367 -15.29365 1.000 92.30681 ? 85  GLN   A OE1 1 
ATOM   565  N NE2 . GLN   A 1 78  ? -10.84997 -34.54340 -13.64856 1.000 83.74965 ? 85  GLN   A NE2 1 
ATOM   566  N N   . ASP   A 1 79  ? -5.95454  -32.09573 -16.76686 1.000 30.15459 ? 86  ASP   A N   1 
ATOM   567  C CA  . ASP   A 1 79  ? -4.68847  -31.77397 -17.41102 1.000 41.60303 ? 86  ASP   A CA  1 
ATOM   568  C C   . ASP   A 1 79  ? -3.73567  -30.99068 -16.52318 1.000 36.41301 ? 86  ASP   A C   1 
ATOM   569  O O   . ASP   A 1 79  ? -2.57420  -30.82132 -16.91082 1.000 27.08125 ? 86  ASP   A O   1 
ATOM   570  C CB  . ASP   A 1 79  ? -4.92209  -30.97558 -18.68845 1.000 29.54071 ? 86  ASP   A CB  1 
ATOM   571  C CG  . ASP   A 1 79  ? -5.80988  -31.70678 -19.66948 1.000 50.71892 ? 86  ASP   A CG  1 
ATOM   572  O OD1 . ASP   A 1 79  ? -5.88671  -32.94765 -19.57779 1.000 48.72426 ? 86  ASP   A OD1 1 
ATOM   573  O OD2 . ASP   A 1 79  ? -6.38954  -31.04765 -20.55692 1.000 53.03432 ? 86  ASP   A OD2 1 
ATOM   574  N N   . ARG   A 1 80  ? -4.19474  -30.52766 -15.35980 1.000 27.75022 ? 87  ARG   A N   1 
ATOM   575  C CA  . ARG   A 1 80  ? -3.43434  -29.63586 -14.48877 1.000 25.17074 ? 87  ARG   A CA  1 
ATOM   576  C C   . ARG   A 1 80  ? -2.94680  -28.39547 -15.25637 1.000 24.10384 ? 87  ARG   A C   1 
ATOM   577  O O   . ARG   A 1 80  ? -1.79345  -27.98598 -15.18969 1.000 25.00430 ? 87  ARG   A O   1 
ATOM   578  C CB  . ARG   A 1 80  ? -2.27557  -30.36603 -13.81320 1.000 30.19083 ? 87  ARG   A CB  1 
ATOM   579  C CG  . ARG   A 1 80  ? -1.79784  -29.61396 -12.58494 1.000 33.51135 ? 87  ARG   A CG  1 
ATOM   580  C CD  . ARG   A 1 80  ? -0.36907  -29.86962 -12.34771 1.000 47.06521 ? 87  ARG   A CD  1 
ATOM   581  N NE  . ARG   A 1 80  ? -0.18260  -31.23659 -11.92123 1.000 35.15700 ? 87  ARG   A NE  1 
ATOM   582  C CZ  . ARG   A 1 80  ? 0.98735   -31.86206 -11.87942 1.000 55.26147 ? 87  ARG   A CZ  1 
ATOM   583  N NH1 . ARG   A 1 80  ? 2.11239   -31.27426 -12.26781 1.000 38.60374 ? 87  ARG   A NH1 1 
ATOM   584  N NH2 . ARG   A 1 80  ? 1.02874   -33.11492 -11.44791 1.000 43.62716 ? 87  ARG   A NH2 1 
ATOM   585  N N   . THR   A 1 81  ? -3.85363  -27.78030 -15.98018 1.000 24.24706 ? 88  THR   A N   1 
ATOM   586  C CA  . THR   A 1 81  ? -3.54434  -26.56228 -16.69629 1.000 21.29566 ? 88  THR   A CA  1 
ATOM   587  C C   . THR   A 1 81  ? -4.50675  -25.46127 -16.29255 1.000 22.56943 ? 88  THR   A C   1 
ATOM   588  O O   . THR   A 1 81  ? -5.66726  -25.71845 -15.93980 1.000 22.56769 ? 88  THR   A O   1 
ATOM   589  C CB  . THR   A 1 81  ? -3.63149  -26.75397 -18.21508 1.000 24.62407 ? 88  THR   A CB  1 
ATOM   590  O OG1 . THR   A 1 81  ? -4.95818  -27.16500 -18.57444 1.000 24.88795 ? 88  THR   A OG1 1 
ATOM   591  C CG2 . THR   A 1 81  ? -2.61983  -27.74316 -18.69885 1.000 22.10707 ? 88  THR   A CG2 1 
ATOM   592  N N   . LEU   A 1 82  ? -3.99919  -24.22799 -16.34141 1.000 18.73935 ? 89  LEU   A N   1 
ATOM   593  C CA  . LEU   A 1 82  ? -4.81577  -23.03039 -16.27575 1.000 15.80207 ? 89  LEU   A CA  1 
ATOM   594  C C   . LEU   A 1 82  ? -4.57131  -22.25388 -17.55935 1.000 18.84390 ? 89  LEU   A C   1 
ATOM   595  O O   . LEU   A 1 82  ? -3.42568  -21.90892 -17.86876 1.000 20.52424 ? 89  LEU   A O   1 
ATOM   596  C CB  . LEU   A 1 82  ? -4.47414  -22.18924 -15.04438 1.000 18.49438 ? 89  LEU   A CB  1 
ATOM   597  C CG  . LEU   A 1 82  ? -5.16391  -20.82356 -15.01138 1.000 17.55863 ? 89  LEU   A CG  1 
ATOM   598  C CD1 . LEU   A 1 82  ? -6.65087  -21.02791 -14.82750 1.000 17.82794 ? 89  LEU   A CD1 1 
ATOM   599  C CD2 . LEU   A 1 82  ? -4.60963  -20.02106 -13.81055 1.000 17.58666 ? 89  LEU   A CD2 1 
ATOM   600  N N   . THR   A 1 83  ? -5.63637  -22.01937 -18.32062 1.000 20.06897 ? 90  THR   A N   1 
ATOM   601  C CA  . THR   A 1 83  ? -5.56581  -21.32017 -19.59593 1.000 18.44275 ? 90  THR   A CA  1 
ATOM   602  C C   . THR   A 1 83  ? -6.16231  -19.92139 -19.44985 1.000 15.55179 ? 90  THR   A C   1 
ATOM   603  O O   . THR   A 1 83  ? -7.26030  -19.76761 -18.89629 1.000 22.97157 ? 90  THR   A O   1 
ATOM   604  C CB  . THR   A 1 83  ? -6.30876  -22.11773 -20.67495 1.000 17.37148 ? 90  THR   A CB  1 
ATOM   605  O OG1 . THR   A 1 83  ? -5.65926  -23.38318 -20.85800 1.000 20.75075 ? 90  THR   A OG1 1 
ATOM   606  C CG2 . THR   A 1 83  ? -6.26454  -21.39944 -22.00233 1.000 23.31582 ? 90  THR   A CG2 1 
ATOM   607  N N   . ILE   A 1 84  ? -5.45047  -18.91614 -19.95106 1.000 14.06475 ? 91  ILE   A N   1 
ATOM   608  C CA  . ILE   A 1 84  ? -5.91221  -17.52390 -19.98809 1.000 13.44687 ? 91  ILE   A CA  1 
ATOM   609  C C   . ILE   A 1 84  ? -6.06119  -17.17425 -21.45760 1.000 16.95594 ? 91  ILE   A C   1 
ATOM   610  O O   . ILE   A 1 84  ? -5.05988  -17.16186 -22.18147 1.000 18.76373 ? 91  ILE   A O   1 
ATOM   611  C CB  . ILE   A 1 84  ? -4.93006  -16.56143 -19.30311 1.000 14.28712 ? 91  ILE   A CB  1 
ATOM   612  C CG1 . ILE   A 1 84  ? -4.83843  -16.86709 -17.80704 1.000 30.21279 ? 91  ILE   A CG1 1 
ATOM   613  C CG2 . ILE   A 1 84  ? -5.38311  -15.11781 -19.44095 1.000 21.24263 ? 91  ILE   A CG2 1 
ATOM   614  C CD1 . ILE   A 1 84  ? -3.74148  -17.80063 -17.50560 1.000 26.53169 ? 91  ILE   A CD1 1 
ATOM   615  N N   . VAL   A 1 85  ? -7.29731  -16.95110 -21.90686 1.000 15.95413 ? 92  VAL   A N   1 
ATOM   616  C CA  . VAL   A 1 85  ? -7.60193  -16.65478 -23.31037 1.000 17.66249 ? 92  VAL   A CA  1 
ATOM   617  C C   . VAL   A 1 85  ? -8.02642  -15.20054 -23.42462 1.000 25.76024 ? 92  VAL   A C   1 
ATOM   618  O O   . VAL   A 1 85  ? -8.88846  -14.75355 -22.66435 1.000 17.90687 ? 92  VAL   A O   1 
ATOM   619  C CB  . VAL   A 1 85  ? -8.74953  -17.51028 -23.87656 1.000 19.60149 ? 92  VAL   A CB  1 
ATOM   620  C CG1 . VAL   A 1 85  ? -8.92209  -17.23583 -25.41433 1.000 17.33794 ? 92  VAL   A CG1 1 
ATOM   621  C CG2 . VAL   A 1 85  ? -8.58989  -18.98256 -23.55264 1.000 31.67426 ? 92  VAL   A CG2 1 
ATOM   622  N N   . ASP   A 1 86  ? -7.52402  -14.49007 -24.43817 1.000 17.73577 ? 93  ASP   A N   1 
ATOM   623  C CA  . ASP   A 1 86  ? -8.09306  -13.18373 -24.74607 1.000 14.95660 ? 93  ASP   A CA  1 
ATOM   624  C C   . ASP   A 1 86  ? -8.30069  -13.08902 -26.25015 1.000 15.14113 ? 93  ASP   A C   1 
ATOM   625  O O   . ASP   A 1 86  ? -7.73005  -13.86787 -27.02130 1.000 18.03328 ? 93  ASP   A O   1 
ATOM   626  C CB  . ASP   A 1 86  ? -7.20913  -12.05300 -24.20980 1.000 15.66792 ? 93  ASP   A CB  1 
ATOM   627  C CG  . ASP   A 1 86  ? -5.81856  -12.01490 -24.89031 1.000 21.88478 ? 93  ASP   A CG  1 
ATOM   628  O OD1 . ASP   A 1 86  ? -5.75508  -11.64504 -26.07913 1.000 20.27509 ? 93  ASP   A OD1 1 
ATOM   629  O OD2 . ASP   A 1 86  ? -4.78254  -12.35583 -24.24564 1.000 19.09130 ? 93  ASP   A OD2 1 
ATOM   630  N N   . THR   A 1 87  ? -9.17967  -12.17697 -26.65316 1.000 17.41355 ? 94  THR   A N   1 
ATOM   631  C CA  . THR   A 1 87  ? -9.41847  -11.91574 -28.07111 1.000 17.41538 ? 94  THR   A CA  1 
ATOM   632  C C   . THR   A 1 87  ? -8.74681  -10.61232 -28.48668 1.000 17.14937 ? 94  THR   A C   1 
ATOM   633  O O   . THR   A 1 87  ? -9.29977  -9.80469  -29.24713 1.000 21.50255 ? 94  THR   A O   1 
ATOM   634  C CB  . THR   A 1 87  ? -10.91472 -11.89998 -28.36243 1.000 19.22599 ? 94  THR   A CB  1 
ATOM   635  O OG1 . THR   A 1 87  ? -11.57167 -11.04487 -27.42373 1.000 19.86188 ? 94  THR   A OG1 1 
ATOM   636  C CG2 . THR   A 1 87  ? -11.48439 -13.30395 -28.19906 1.000 20.57879 ? 94  THR   A CG2 1 
ATOM   637  N N   . GLY   A 1 88  ? -7.54782  -10.37400 -27.95327 1.000 16.57054 ? 95  GLY   A N   1 
ATOM   638  C CA  . GLY   A 1 88  ? -6.84037  -9.13522  -28.21386 1.000 15.41134 ? 95  GLY   A CA  1 
ATOM   639  C C   . GLY   A 1 88  ? -6.16879  -9.18964  -29.57660 1.000 15.51451 ? 95  GLY   A C   1 
ATOM   640  O O   . GLY   A 1 88  ? -6.49223  -10.02080 -30.43294 1.000 19.52305 ? 95  GLY   A O   1 
ATOM   641  N N   . ILE   A 1 89  ? -5.17586  -8.31539  -29.75022 1.000 20.34414 ? 96  ILE   A N   1 
ATOM   642  C CA  . ILE   A 1 89  ? -4.52329  -8.16576  -31.05471 1.000 18.42021 ? 96  ILE   A CA  1 
ATOM   643  C C   . ILE   A 1 89  ? -3.67400  -9.36772  -31.48109 1.000 19.20741 ? 96  ILE   A C   1 
ATOM   644  O O   . ILE   A 1 89  ? -3.42241  -9.52777  -32.68883 1.000 19.85012 ? 96  ILE   A O   1 
ATOM   645  C CB  . ILE   A 1 89  ? -3.66315  -6.89015  -31.06347 1.000 17.03362 ? 96  ILE   A CB  1 
ATOM   646  C CG1 . ILE   A 1 89  ? -3.33194  -6.47105  -32.51876 1.000 20.76872 ? 96  ILE   A CG1 1 
ATOM   647  C CG2 . ILE   A 1 89  ? -2.40221  -7.11049  -30.20197 1.000 19.66670 ? 96  ILE   A CG2 1 
ATOM   648  C CD1 . ILE   A 1 89  ? -3.05084  -4.95424  -32.68905 1.000 21.93158 ? 96  ILE   A CD1 1 
ATOM   649  N N   . GLY   A 1 90  ? -3.22495  -10.23753 -30.55191 1.000 16.56745 ? 97  GLY   A N   1 
ATOM   650  C CA  . GLY   A 1 90  ? -2.43273  -11.39488 -30.95045 1.000 19.42404 ? 97  GLY   A CA  1 
ATOM   651  C C   . GLY   A 1 90  ? -0.97245  -11.03888 -31.20926 1.000 18.96697 ? 97  GLY   A C   1 
ATOM   652  O O   . GLY   A 1 90  ? -0.54063  -9.89444  -31.06665 1.000 20.29925 ? 97  GLY   A O   1 
ATOM   653  N N   . MET   A 1 91  ? -0.19585  -12.04710 -31.60305 1.000 18.75346 ? 98  MET   A N   1 
ATOM   654  C CA  . MET   A 1 91  ? 1.23526   -11.87614 -31.83541 1.000 13.52282 ? 98  MET   A CA  1 
ATOM   655  C C   . MET   A 1 91  ? 1.62853   -12.46509 -33.17750 1.000 14.88131 ? 98  MET   A C   1 
ATOM   656  O O   . MET   A 1 91  ? 1.14365   -13.53424 -33.55624 1.000 18.65029 ? 98  MET   A O   1 
ATOM   657  C CB  . MET   A 1 91  ? 2.01874   -12.55302 -30.70089 1.000 15.46820 ? 98  MET   A CB  1 
ATOM   658  C CG  . MET   A 1 91  ? 1.86853   -11.79433 -29.38455 1.000 17.21129 ? 98  MET   A CG  1 
ATOM   659  S SD  . MET   A 1 91  ? 2.72745   -12.70875 -28.07654 1.000 23.26565 ? 98  MET   A SD  1 
ATOM   660  C CE  . MET   A 1 91  ? 1.53825   -14.01826 -27.81979 1.000 21.27232 ? 98  MET   A CE  1 
ATOM   661  N N   . THR   A 1 92  ? 2.50125   -11.75944 -33.89707 1.000 17.95146 ? 99  THR   A N   1 
ATOM   662  C CA  . THR   A 1 92  ? 3.04969   -12.29095 -35.13827 1.000 18.69419 ? 99  THR   A CA  1 
ATOM   663  C C   . THR   A 1 92  ? 4.18724   -13.27567 -34.84587 1.000 20.06157 ? 99  THR   A C   1 
ATOM   664  O O   . THR   A 1 92  ? 4.70811   -13.35475 -33.73867 1.000 21.07904 ? 99  THR   A O   1 
ATOM   665  C CB  . THR   A 1 92  ? 3.59462   -11.16616 -36.00094 1.000 22.29086 ? 99  THR   A CB  1 
ATOM   666  O OG1 . THR   A 1 92  ? 4.67967   -10.56145 -35.28358 1.000 21.63268 ? 99  THR   A OG1 1 
ATOM   667  C CG2 . THR   A 1 92  ? 2.51494   -10.13779 -36.27657 1.000 20.81075 ? 99  THR   A CG2 1 
ATOM   668  N N   . LYS   A 1 93  ? 4.60668   -14.01983 -35.87243 1.000 17.61023 ? 100 LYS   A N   1 
ATOM   669  C CA  . LYS   A 1 93  ? 5.77993   -14.85987 -35.67942 1.000 18.04175 ? 100 LYS   A CA  1 
ATOM   670  C C   . LYS   A 1 93  ? 6.98631   -14.02269 -35.26426 1.000 20.97511 ? 100 LYS   A C   1 
ATOM   671  O O   . LYS   A 1 93  ? 7.75801   -14.42909 -34.38738 1.000 21.56468 ? 100 LYS   A O   1 
ATOM   672  C CB  . LYS   A 1 93  ? 6.09627   -15.63941 -36.96955 1.000 20.66504 ? 100 LYS   A CB  1 
ATOM   673  C CG  . LYS   A 1 93  ? 7.09535   -16.78594 -36.76945 1.000 22.32516 ? 100 LYS   A CG  1 
ATOM   674  C CD  . LYS   A 1 93  ? 7.44903   -17.43351 -38.12852 1.000 26.07494 ? 100 LYS   A CD  1 
ATOM   675  C CE  . LYS   A 1 93  ? 8.46571   -18.56443 -37.98076 1.000 36.13573 ? 100 LYS   A CE  1 
ATOM   676  N NZ  . LYS   A 1 93  ? 8.80665   -19.16026 -39.33292 1.000 38.07364 ? 100 LYS   A NZ  1 
ATOM   677  N N   . ALA   A 1 94  ? 7.15423   -12.83723 -35.87192 1.000 19.36412 ? 101 ALA   A N   1 
ATOM   678  C CA  . ALA   A 1 94  ? 8.29815   -11.99509 -35.52427 1.000 20.38673 ? 101 ALA   A CA  1 
ATOM   679  C C   . ALA   A 1 94  ? 8.20191   -11.51373 -34.07961 1.000 23.15212 ? 101 ALA   A C   1 
ATOM   680  O O   . ALA   A 1 94  ? 9.21783   -11.40271 -33.38049 1.000 21.06010 ? 101 ALA   A O   1 
ATOM   681  C CB  . ALA   A 1 94  ? 8.40380   -10.80953 -36.48386 1.000 22.28437 ? 101 ALA   A CB  1 
ATOM   682  N N   . ASP   A 1 95  ? 6.98856   -11.21776 -33.61790 1.000 21.74458 ? 102 ASP   A N   1 
ATOM   683  C CA  . ASP   A 1 95  ? 6.78395   -10.91051 -32.20453 1.000 17.27423 ? 102 ASP   A CA  1 
ATOM   684  C C   . ASP   A 1 95  ? 7.35404   -12.01626 -31.31355 1.000 18.45599 ? 102 ASP   A C   1 
ATOM   685  O O   . ASP   A 1 95  ? 8.10137   -11.74470 -30.35588 1.000 22.88611 ? 102 ASP   A O   1 
ATOM   686  C CB  . ASP   A 1 95  ? 5.28414   -10.77389 -31.93902 1.000 22.25033 ? 102 ASP   A CB  1 
ATOM   687  C CG  . ASP   A 1 95  ? 4.72184   -9.40674  -32.31666 1.000 22.65307 ? 102 ASP   A CG  1 
ATOM   688  O OD1 . ASP   A 1 95  ? 5.48469   -8.42713  -32.50774 1.000 24.39425 ? 102 ASP   A OD1 1 
ATOM   689  O OD2 . ASP   A 1 95  ? 3.48936   -9.34373  -32.48898 1.000 24.51633 ? 102 ASP   A OD2 1 
ATOM   690  N N   . LEU   A 1 96  ? 6.94401   -13.27263 -31.58765 1.000 17.73059 ? 103 LEU   A N   1 
ATOM   691  C CA  . LEU   A 1 96  ? 7.28022   -14.42180 -30.74371 1.000 16.46515 ? 103 LEU   A CA  1 
ATOM   692  C C   . LEU   A 1 96  ? 8.76236   -14.71257 -30.75295 1.000 21.73403 ? 103 LEU   A C   1 
ATOM   693  O O   . LEU   A 1 96  ? 9.32709   -15.12731 -29.73909 1.000 19.17336 ? 103 LEU   A O   1 
ATOM   694  C CB  . LEU   A 1 96  ? 6.53336   -15.67560 -31.21709 1.000 16.08166 ? 103 LEU   A CB  1 
ATOM   695  C CG  . LEU   A 1 96  ? 5.02292   -15.67262 -31.06279 1.000 20.36970 ? 103 LEU   A CG  1 
ATOM   696  C CD1 . LEU   A 1 96  ? 4.44241   -16.88339 -31.73620 1.000 18.88023 ? 103 LEU   A CD1 1 
ATOM   697  C CD2 . LEU   A 1 96  ? 4.63483   -15.66483 -29.57654 1.000 18.81708 ? 103 LEU   A CD2 1 
ATOM   698  N N   . ILE   A 1 97  ? 9.40389   -14.57485 -31.90747 1.000 20.84320 ? 104 ILE   A N   1 
ATOM   699  C CA  . ILE   A 1 97  ? 10.79106  -14.99581 -32.00658 1.000 21.47969 ? 104 ILE   A CA  1 
ATOM   700  C C   . ILE   A 1 97  ? 11.74425  -13.87032 -31.64838 1.000 23.09519 ? 104 ILE   A C   1 
ATOM   701  O O   . ILE   A 1 97  ? 12.77748  -14.10428 -31.00960 1.000 27.54136 ? 104 ILE   A O   1 
ATOM   702  C CB  . ILE   A 1 97  ? 11.08534  -15.53665 -33.41729 1.000 21.39124 ? 104 ILE   A CB  1 
ATOM   703  C CG1 . ILE   A 1 97  ? 10.26884  -16.80269 -33.69232 1.000 24.24878 ? 104 ILE   A CG1 1 
ATOM   704  C CG2 . ILE   A 1 97  ? 12.58664  -15.75075 -33.60182 1.000 30.43634 ? 104 ILE   A CG2 1 
ATOM   705  C CD1 . ILE   A 1 97  ? 10.33097  -17.23734 -35.19627 1.000 26.43431 ? 104 ILE   A CD1 1 
ATOM   706  N N   . ASN   A 1 98  ? 11.44138  -12.63935 -32.06399 1.000 22.51196 ? 105 ASN   A N   1 
ATOM   707  C CA  . ASN   A 1 98  ? 12.46731  -11.60609 -31.95058 1.000 24.70013 ? 105 ASN   A CA  1 
ATOM   708  C C   . ASN   A 1 98  ? 11.97842  -10.32544 -31.25598 1.000 30.16041 ? 105 ASN   A C   1 
ATOM   709  O O   . ASN   A 1 98  ? 12.68594  -9.80291  -30.39751 1.000 26.27488 ? 105 ASN   A O   1 
ATOM   710  C CB  . ASN   A 1 98  ? 13.00698  -11.28485 -33.34496 1.000 36.10853 ? 105 ASN   A CB  1 
ATOM   711  C CG  . ASN   A 1 98  ? 14.41068  -10.69185 -33.31100 1.000 62.71738 ? 105 ASN   A CG  1 
ATOM   712  O OD1 . ASN   A 1 98  ? 14.99355  -10.48924 -32.24589 1.000 62.22339 ? 105 ASN   A OD1 1 
ATOM   713  N ND2 . ASN   A 1 98  ? 14.98048  -10.46275 -34.48957 1.000 76.92600 ? 105 ASN   A ND2 1 
ATOM   714  N N   . ASN   A 1 99  ? 10.79756  -9.79143  -31.60418 1.000 20.92122 ? 106 ASN   A N   1 
ATOM   715  C CA  . ASN   A 1 99  ? 10.46942  -8.41691  -31.19698 1.000 22.02516 ? 106 ASN   A CA  1 
ATOM   716  C C   . ASN   A 1 99  ? 10.21986  -8.29979  -29.69764 1.000 20.98150 ? 106 ASN   A C   1 
ATOM   717  O O   . ASN   A 1 99  ? 10.70118  -7.35948  -29.05657 1.000 22.05408 ? 106 ASN   A O   1 
ATOM   718  C CB  . ASN   A 1 99  ? 9.22921   -7.88331  -31.93707 1.000 22.06267 ? 106 ASN   A CB  1 
ATOM   719  C CG  . ASN   A 1 99  ? 9.36841   -7.88633  -33.42458 1.000 33.94415 ? 106 ASN   A CG  1 
ATOM   720  O OD1 . ASN   A 1 99  ? 10.45873  -7.75781  -33.95010 1.000 29.57872 ? 106 ASN   A OD1 1 
ATOM   721  N ND2 . ASN   A 1 99  ? 8.23515   -7.98833  -34.12167 1.000 40.11806 ? 106 ASN   A ND2 1 
ATOM   722  N N   . LEU   A 1 100 ? 9.38774   -9.18535  -29.13739 1.000 17.18561 ? 107 LEU   A N   1 
ATOM   723  C CA  . LEU   A 1 100 ? 9.03344   -9.06374  -27.72343 1.000 22.10094 ? 107 LEU   A CA  1 
ATOM   724  C C   . LEU   A 1 100 ? 10.24319  -9.28703  -26.82690 1.000 20.26340 ? 107 LEU   A C   1 
ATOM   725  O O   . LEU   A 1 100 ? 10.38909  -8.63473  -25.77641 1.000 20.78703 ? 107 LEU   A O   1 
ATOM   726  C CB  . LEU   A 1 100 ? 7.92535   -10.05163 -27.38196 1.000 21.48689 ? 107 LEU   A CB  1 
ATOM   727  C CG  . LEU   A 1 100 ? 6.59177   -9.72777  -28.06287 1.000 24.36443 ? 107 LEU   A CG  1 
ATOM   728  C CD1 . LEU   A 1 100 ? 5.53356   -10.75154 -27.70301 1.000 25.15270 ? 107 LEU   A CD1 1 
ATOM   729  C CD2 . LEU   A 1 100 ? 6.12776   -8.34381  -27.63978 1.000 26.67532 ? 107 LEU   A CD2 1 
ATOM   730  N N   . GLY   A 1 101 ? 11.11676  -10.20867 -27.21513 1.000 21.01009 ? 108 GLY   A N   1 
ATOM   731  C CA  . GLY   A 1 101 ? 12.31767  -10.44785 -26.42978 1.000 26.01478 ? 108 GLY   A CA  1 
ATOM   732  C C   . GLY   A 1 101 ? 13.30418  -9.29723  -26.51801 1.000 27.21954 ? 108 GLY   A C   1 
ATOM   733  O O   . GLY   A 1 101 ? 13.99911  -8.98824  -25.55221 1.000 25.44992 ? 108 GLY   A O   1 
ATOM   734  N N   . THR   A 1 102 ? 13.40752  -8.66572  -27.68552 1.000 21.70603 ? 109 THR   A N   1 
ATOM   735  C CA  . THR   A 1 102 ? 14.26606  -7.49342  -27.78669 1.000 20.28837 ? 109 THR   A CA  1 
ATOM   736  C C   . THR   A 1 102 ? 13.81721  -6.42106  -26.80463 1.000 25.59794 ? 109 THR   A C   1 
ATOM   737  O O   . THR   A 1 102 ? 14.63462  -5.85493  -26.07503 1.000 24.18432 ? 109 THR   A O   1 
ATOM   738  C CB  . THR   A 1 102 ? 14.23406  -6.96073  -29.21221 1.000 24.42743 ? 109 THR   A CB  1 
ATOM   739  O OG1 . THR   A 1 102 ? 14.81598  -7.94843  -30.06570 1.000 31.09412 ? 109 THR   A OG1 1 
ATOM   740  C CG2 . THR   A 1 102 ? 15.02401  -5.67385  -29.31185 1.000 30.85021 ? 109 THR   A CG2 1 
ATOM   741  N N   . ILE   A 1 103 ? 12.51169  -6.15659  -26.75361 1.000 21.98831 ? 110 ILE   A N   1 
ATOM   742  C CA  . ILE   A 1 103 ? 11.97010  -5.22670  -25.76150 1.000 25.19967 ? 110 ILE   A CA  1 
ATOM   743  C C   . ILE   A 1 103 ? 12.23640  -5.74211  -24.34806 1.000 31.53244 ? 110 ILE   A C   1 
ATOM   744  O O   . ILE   A 1 103 ? 12.62761  -4.98372  -23.45260 1.000 29.15045 ? 110 ILE   A O   1 
ATOM   745  C CB  . ILE   A 1 103 ? 10.46681  -5.00755  -26.01184 1.000 21.99812 ? 110 ILE   A CB  1 
ATOM   746  C CG1 . ILE   A 1 103 ? 10.21688  -4.39603  -27.39412 1.000 26.94878 ? 110 ILE   A CG1 1 
ATOM   747  C CG2 . ILE   A 1 103 ? 9.88729   -4.09494  -24.94150 1.000 32.34337 ? 110 ILE   A CG2 1 
ATOM   748  C CD1 . ILE   A 1 103 ? 10.87566  -3.02705  -27.58078 1.000 35.25319 ? 110 ILE   A CD1 1 
ATOM   749  N N   . ALA   A 1 104 ? 12.05600  -7.04349  -24.12624 1.000 20.55241 ? 111 ALA   A N   1 
ATOM   750  C CA  . ALA   A 1 104 ? 12.19668  -7.57738  -22.77331 1.000 18.70077 ? 111 ALA   A CA  1 
ATOM   751  C C   . ALA   A 1 104 ? 13.62566  -7.48443  -22.24094 1.000 29.89591 ? 111 ALA   A C   1 
ATOM   752  O O   . ALA   A 1 104 ? 13.81993  -7.48651  -21.01790 1.000 27.76740 ? 111 ALA   A O   1 
ATOM   753  C CB  . ALA   A 1 104 ? 11.70671  -9.03761  -22.73210 1.000 17.72846 ? 111 ALA   A CB  1 
ATOM   754  N N   . LYS   A 1 105 ? 14.62745  -7.39378  -23.12258 1.000 23.04759 ? 112 LYS   A N   1 
ATOM   755  C CA  . LYS   A 1 105 ? 16.01563  -7.36810  -22.67446 1.000 25.10045 ? 112 LYS   A CA  1 
ATOM   756  C C   . LYS   A 1 105 ? 16.27531  -6.17718  -21.75612 1.000 27.18175 ? 112 LYS   A C   1 
ATOM   757  O O   . LYS   A 1 105 ? 16.90829  -6.31711  -20.69887 1.000 25.69656 ? 112 LYS   A O   1 
ATOM   758  C CB  . LYS   A 1 105 ? 16.94184  -7.35157  -23.90099 1.000 25.62408 ? 112 LYS   A CB  1 
ATOM   759  C CG  . LYS   A 1 105 ? 18.38177  -7.73488  -23.68440 1.000 35.61320 ? 112 LYS   A CG  1 
ATOM   760  C CD  . LYS   A 1 105 ? 19.18995  -7.46421  -24.97604 1.000 39.52902 ? 112 LYS   A CD  1 
ATOM   761  C CE  . LYS   A 1 105 ? 20.60578  -8.00781  -24.89888 1.000 55.57346 ? 112 LYS   A CE  1 
ATOM   762  N NZ  . LYS   A 1 105 ? 21.51295  -7.14452  -24.08913 1.000 57.17108 ? 112 LYS   A NZ  1 
ATOM   763  N N   . SER   A 1 106 ? 15.78563  -4.99188  -22.12155 1.000 26.06394 ? 113 SER   A N   1 
ATOM   764  C CA  . SER   A 1 106 ? 16.09267  -3.85895  -21.25509 1.000 23.02261 ? 113 SER   A CA  1 
ATOM   765  C C   . SER   A 1 106 ? 15.21597  -3.85513  -20.01116 1.000 23.26468 ? 113 SER   A C   1 
ATOM   766  O O   . SER   A 1 106 ? 15.67917  -3.44896  -18.94046 1.000 22.75536 ? 113 SER   A O   1 
ATOM   767  C CB  . SER   A 1 106 ? 15.96345  -2.52749  -22.00345 1.000 31.31474 ? 113 SER   A CB  1 
ATOM   768  O OG  . SER   A 1 106 ? 14.68592  -2.36893  -22.56414 1.000 39.79595 ? 113 SER   A OG  1 
ATOM   769  N N   . GLY   A 1 107 ? 13.97260  -4.32425  -20.11453 1.000 23.71743 ? 114 GLY   A N   1 
ATOM   770  C CA  . GLY   A 1 107 ? 13.14132  -4.41513  -18.92582 1.000 23.11829 ? 114 GLY   A CA  1 
ATOM   771  C C   . GLY   A 1 107 ? 13.69072  -5.41519  -17.92784 1.000 24.92612 ? 114 GLY   A C   1 
ATOM   772  O O   . GLY   A 1 107 ? 13.64709  -5.19213  -16.71459 1.000 18.85415 ? 114 GLY   A O   1 
ATOM   773  N N   . THR   A 1 108 ? 14.22535  -6.52947  -18.42763 1.000 19.84945 ? 115 THR   A N   1 
ATOM   774  C CA  . THR   A 1 108 ? 14.86438  -7.52077  -17.56436 1.000 20.24731 ? 115 THR   A CA  1 
ATOM   775  C C   . THR   A 1 108 ? 16.06176  -6.93838  -16.83677 1.000 19.69857 ? 115 THR   A C   1 
ATOM   776  O O   . THR   A 1 108 ? 16.20916  -7.11628  -15.62020 1.000 25.02900 ? 115 THR   A O   1 
ATOM   777  C CB  . THR   A 1 108 ? 15.30190  -8.72473  -18.40928 1.000 20.13205 ? 115 THR   A CB  1 
ATOM   778  O OG1 . THR   A 1 108 ? 14.13419  -9.35825  -18.92214 1.000 31.22577 ? 115 THR   A OG1 1 
ATOM   779  C CG2 . THR   A 1 108 ? 16.10105  -9.68276  -17.55052 1.000 27.74365 ? 115 THR   A CG2 1 
ATOM   780  N N   . LYS   A 1 109 ? 16.95803  -6.27022  -17.57520 1.000 19.93039 ? 116 LYS   A N   1 
ATOM   781  C CA  . LYS   A 1 109 ? 18.11915  -5.63427  -16.96046 1.000 26.17267 ? 116 LYS   A CA  1 
ATOM   782  C C   . LYS   A 1 109 ? 17.69956  -4.68541  -15.84329 1.000 28.28565 ? 116 LYS   A C   1 
ATOM   783  O O   . LYS   A 1 109 ? 18.29009  -4.68524  -14.76024 1.000 27.01120 ? 116 LYS   A O   1 
ATOM   784  C CB  . LYS   A 1 109 ? 18.92556  -4.89128  -18.03657 1.000 24.25764 ? 116 LYS   A CB  1 
ATOM   785  C CG  . LYS   A 1 109 ? 20.11045  -4.03903  -17.53156 1.000 33.82073 ? 116 LYS   A CG  1 
ATOM   786  C CD  . LYS   A 1 109 ? 20.98930  -3.58443  -18.70336 1.000 44.14070 ? 116 LYS   A CD  1 
ATOM   787  C CE  . LYS   A 1 109 ? 22.14284  -2.65687  -18.26342 1.000 58.50265 ? 116 LYS   A CE  1 
ATOM   788  N NZ  . LYS   A 1 109 ? 22.67996  -2.98458  -16.91942 1.000 72.02832 ? 116 LYS   A NZ  1 
ATOM   789  N N   . ALA   A 1 110 ? 16.67894  -3.86938  -16.08757 1.000 21.65571 ? 117 ALA   A N   1 
ATOM   790  C CA  . ALA   A 1 110 ? 16.25743  -2.90741  -15.07382 1.000 25.21425 ? 117 ALA   A CA  1 
ATOM   791  C C   . ALA   A 1 110 ? 15.60934  -3.60994  -13.87917 1.000 24.22142 ? 117 ALA   A C   1 
ATOM   792  O O   . ALA   A 1 110 ? 15.83267  -3.22555  -12.72220 1.000 23.31931 ? 117 ALA   A O   1 
ATOM   793  C CB  . ALA   A 1 110 ? 15.29425  -1.89528  -15.69642 1.000 20.07984 ? 117 ALA   A CB  1 
ATOM   794  N N   . PHE   A 1 111 ? 14.80899  -4.64143  -14.13858 1.000 18.64081 ? 118 PHE   A N   1 
ATOM   795  C CA  . PHE   A 1 111 ? 14.16829  -5.37860  -13.05017 1.000 18.18313 ? 118 PHE   A CA  1 
ATOM   796  C C   . PHE   A 1 111 ? 15.21195  -6.06230  -12.17016 1.000 22.67906 ? 118 PHE   A C   1 
ATOM   797  O O   . PHE   A 1 111 ? 15.15430  -5.98312  -10.93145 1.000 21.19114 ? 118 PHE   A O   1 
ATOM   798  C CB  . PHE   A 1 111 ? 13.18453  -6.38758  -13.64130 1.000 16.83614 ? 118 PHE   A CB  1 
ATOM   799  C CG  . PHE   A 1 111 ? 12.45963  -7.23567  -12.60314 1.000 16.94168 ? 118 PHE   A CG  1 
ATOM   800  C CD1 . PHE   A 1 111 ? 11.86187  -6.64115  -11.49191 1.000 18.45791 ? 118 PHE   A CD1 1 
ATOM   801  C CD2 . PHE   A 1 111 ? 12.36047  -8.60585  -12.76063 1.000 22.27568 ? 118 PHE   A CD2 1 
ATOM   802  C CE1 . PHE   A 1 111 ? 11.17721  -7.43685  -10.53967 1.000 20.87300 ? 118 PHE   A CE1 1 
ATOM   803  C CE2 . PHE   A 1 111 ? 11.69769  -9.39456  -11.84014 1.000 25.36370 ? 118 PHE   A CE2 1 
ATOM   804  C CZ  . PHE   A 1 111 ? 11.08560  -8.79451  -10.71937 1.000 21.32785 ? 118 PHE   A CZ  1 
ATOM   805  N N   . MET   A 1 112 ? 16.20687  -6.70538  -12.79018 1.000 21.31470 ? 119 MET   A N   1 
ATOM   806  C CA  . MET   A 1 112 ? 17.22005  -7.38800  -11.98271 1.000 26.88028 ? 119 MET   A CA  1 
ATOM   807  C C   . MET   A 1 112 ? 18.05956  -6.40449  -11.18781 1.000 27.19514 ? 119 MET   A C   1 
ATOM   808  O O   . MET   A 1 112 ? 18.43245  -6.69164  -10.04546 1.000 28.60627 ? 119 MET   A O   1 
ATOM   809  C CB  . MET   A 1 112 ? 18.09149  -8.29933  -12.86185 1.000 27.25727 ? 119 MET   A CB  1 
ATOM   810  C CG  . MET   A 1 112 ? 17.24507  -9.20732  -13.73118 1.000 36.03944 ? 119 MET   A CG  1 
ATOM   811  S SD  . MET   A 1 112 ? 17.80242  -10.91804 -13.87060 1.000 49.67713 ? 119 MET   A SD  1 
ATOM   812  C CE  . MET   A 1 112 ? 18.71857  -10.79734 -15.42638 1.000 43.26646 ? 119 MET   A CE  1 
ATOM   813  N N   . GLU   A 1 113 ? 18.34985  -5.23094  -11.74745 1.000 25.79979 ? 120 GLU   A N   1 
ATOM   814  C CA  . GLU   A 1 113 ? 19.04907  -4.22806  -10.94793 1.000 31.99270 ? 120 GLU   A CA  1 
ATOM   815  C C   . GLU   A 1 113 ? 18.18361  -3.73857  -9.78817  1.000 27.37253 ? 120 GLU   A C   1 
ATOM   816  O O   . GLU   A 1 113 ? 18.67917  -3.57402  -8.67179  1.000 32.32486 ? 120 GLU   A O   1 
ATOM   817  C CB  . GLU   A 1 113 ? 19.51432  -3.07873  -11.83779 1.000 31.09227 ? 120 GLU   A CB  1 
ATOM   818  C CG  . GLU   A 1 113 ? 20.52590  -3.56159  -12.89242 1.000 43.17230 ? 120 GLU   A CG  1 
ATOM   819  C CD  . GLU   A 1 113 ? 21.06059  -2.45821  -13.79787 1.000 61.42896 ? 120 GLU   A CD  1 
ATOM   820  O OE1 . GLU   A 1 113 ? 20.48354  -1.35041  -13.80779 1.000 66.98540 ? 120 GLU   A OE1 1 
ATOM   821  O OE2 . GLU   A 1 113 ? 22.07120  -2.70749  -14.49729 1.000 61.66461 ? 120 GLU   A OE2 1 
ATOM   822  N N   . ALA   A 1 114 ? 16.88656  -3.53525  -10.02833 1.000 23.96539 ? 121 ALA   A N   1 
ATOM   823  C CA  . ALA   A 1 114 ? 15.96555  -3.13555  -8.96298  1.000 24.40754 ? 121 ALA   A CA  1 
ATOM   824  C C   . ALA   A 1 114 ? 15.87206  -4.19175  -7.87379  1.000 28.46333 ? 121 ALA   A C   1 
ATOM   825  O O   . ALA   A 1 114 ? 15.78284  -3.85565  -6.68317  1.000 29.53448 ? 121 ALA   A O   1 
ATOM   826  C CB  . ALA   A 1 114 ? 14.57359  -2.88162  -9.54525  1.000 24.11360 ? 121 ALA   A CB  1 
ATOM   827  N N   . LEU   A 1 115 ? 15.84370  -5.47730  -8.25947  1.000 24.70593 ? 122 LEU   A N   1 
ATOM   828  C CA  . LEU   A 1 115 ? 15.81540  -6.53834  -7.25264  1.000 28.10702 ? 122 LEU   A CA  1 
ATOM   829  C C   . LEU   A 1 115 ? 17.05059  -6.47300  -6.37764  1.000 36.88034 ? 122 LEU   A C   1 
ATOM   830  O O   . LEU   A 1 115 ? 16.96758  -6.65417  -5.15550  1.000 30.87277 ? 122 LEU   A O   1 
ATOM   831  C CB  . LEU   A 1 115 ? 15.71103  -7.91313  -7.91016  1.000 29.04335 ? 122 LEU   A CB  1 
ATOM   832  C CG  . LEU   A 1 115 ? 14.34534  -8.21089  -8.53473  1.000 27.30170 ? 122 LEU   A CG  1 
ATOM   833  C CD1 . LEU   A 1 115 ? 14.39595  -9.45763  -9.39565  1.000 30.89965 ? 122 LEU   A CD1 1 
ATOM   834  C CD2 . LEU   A 1 115 ? 13.22654  -8.31347  -7.48624  1.000 26.41066 ? 122 LEU   A CD2 1 
ATOM   835  N N   . GLN   A 1 116 ? 18.20865  -6.21386  -6.99398  1.000 31.01413 ? 123 GLN   A N   1 
ATOM   836  C CA  . GLN   A 1 116 ? 19.45372  -6.08619  -6.23975  1.000 36.63328 ? 123 GLN   A CA  1 
ATOM   837  C C   . GLN   A 1 116 ? 19.37571  -4.95153  -5.22909  1.000 44.84420 ? 123 GLN   A C   1 
ATOM   838  O O   . GLN   A 1 116 ? 19.99450  -5.01656  -4.15915  1.000 46.51549 ? 123 GLN   A O   1 
ATOM   839  C CB  . GLN   A 1 116 ? 20.60515  -5.85075  -7.21686  1.000 37.64262 ? 123 GLN   A CB  1 
ATOM   840  C CG  . GLN   A 1 116 ? 21.09697  -7.11594  -7.86640  1.000 50.96008 ? 123 GLN   A CG  1 
ATOM   841  C CD  . GLN   A 1 116 ? 21.40332  -8.18670  -6.84162  1.000 74.83310 ? 123 GLN   A CD  1 
ATOM   842  O OE1 . GLN   A 1 116 ? 22.29627  -8.02605  -6.00147  1.000 75.41126 ? 123 GLN   A OE1 1 
ATOM   843  N NE2 . GLN   A 1 116 ? 20.64304  -9.27953  -6.88466  1.000 79.38078 ? 123 GLN   A NE2 1 
ATOM   844  N N   . ALA   A 1 117 ? 18.62485  -3.90308  -5.54889  1.000 34.02087 ? 124 ALA   A N   1 
ATOM   845  C CA  . ALA   A 1 117 ? 18.51800  -2.72578  -4.70032  1.000 35.88426 ? 124 ALA   A CA  1 
ATOM   846  C C   . ALA   A 1 117 ? 17.29566  -2.77353  -3.77995  1.000 45.43585 ? 124 ALA   A C   1 
ATOM   847  O O   . ALA   A 1 117 ? 16.93091  -1.75147  -3.19128  1.000 45.94353 ? 124 ALA   A O   1 
ATOM   848  C CB  . ALA   A 1 117 ? 18.48791  -1.46593  -5.56837  1.000 36.22312 ? 124 ALA   A CB  1 
ATOM   849  N N   . GLY   A 1 118 ? 16.63713  -3.92798  -3.66366  1.000 41.17811 ? 125 GLY   A N   1 
ATOM   850  C CA  . GLY   A 1 118 ? 15.59997  -4.10279  -2.66303  1.000 40.89135 ? 125 GLY   A CA  1 
ATOM   851  C C   . GLY   A 1 118 ? 14.18795  -4.29290  -3.17748  1.000 41.89870 ? 125 GLY   A C   1 
ATOM   852  O O   . GLY   A 1 118 ? 13.28786  -4.53310  -2.36178  1.000 37.76374 ? 125 GLY   A O   1 
ATOM   853  N N   . ALA   A 1 119 ? 13.95120  -4.20332  -4.48958  1.000 29.21812 ? 126 ALA   A N   1 
ATOM   854  C CA  . ALA   A 1 119 ? 12.61545  -4.43739  -5.02224  1.000 28.96863 ? 126 ALA   A CA  1 
ATOM   855  C C   . ALA   A 1 119 ? 12.20510  -5.89154  -4.79272  1.000 35.36153 ? 126 ALA   A C   1 
ATOM   856  O O   . ALA   A 1 119 ? 13.02153  -6.74769  -4.44092  1.000 32.20904 ? 126 ALA   A O   1 
ATOM   857  C CB  . ALA   A 1 119 ? 12.56919  -4.09462  -6.51572  1.000 25.36431 ? 126 ALA   A CB  1 
ATOM   858  N N   . ASP   A 1 120 ? 10.92347  -6.18846  -4.97948  1.000 30.98501 ? 127 ASP   A N   1 
ATOM   859  C CA  . ASP   A 1 120 ? 10.53759  -7.58824  -4.90121  1.000 36.73135 ? 127 ASP   A CA  1 
ATOM   860  C C   . ASP   A 1 120 ? 9.87646   -8.02748  -6.19818  1.000 26.74618 ? 127 ASP   A C   1 
ATOM   861  O O   . ASP   A 1 120 ? 9.50557   -7.21451  -7.05739  1.000 25.56990 ? 127 ASP   A O   1 
ATOM   862  C CB  . ASP   A 1 120 ? 9.62258   -7.88098  -3.70532  1.000 40.26766 ? 127 ASP   A CB  1 
ATOM   863  C CG  . ASP   A 1 120 ? 8.26120   -7.28003  -3.86407  1.000 41.22341 ? 127 ASP   A CG  1 
ATOM   864  O OD1 . ASP   A 1 120 ? 8.17220   -6.03695  -3.76381  1.000 49.86343 ? 127 ASP   A OD1 1 
ATOM   865  O OD2 . ASP   A 1 120 ? 7.29617   -8.03990  -4.14197  1.000 35.39003 ? 127 ASP   A OD2 1 
ATOM   866  N N   . ILE   A 1 121 ? 9.74802   -9.35058  -6.31548  1.000 24.52309 ? 128 ILE   A N   1 
ATOM   867  C CA  . ILE   A 1 121 ? 9.30848   -9.97843  -7.55667  1.000 24.63342 ? 128 ILE   A CA  1 
ATOM   868  C C   . ILE   A 1 121 ? 7.93218   -9.47494  -7.96147  1.000 28.35918 ? 128 ILE   A C   1 
ATOM   869  O O   . ILE   A 1 121 ? 7.60906   -9.41994  -9.15619  1.000 24.80490 ? 128 ILE   A O   1 
ATOM   870  C CB  . ILE   A 1 121 ? 9.37627   -11.51670 -7.39466  1.000 28.91466 ? 128 ILE   A CB  1 
ATOM   871  C CG1 . ILE   A 1 121 ? 10.84272  -11.95968 -7.47343  1.000 33.18827 ? 128 ILE   A CG1 1 
ATOM   872  C CG2 . ILE   A 1 121 ? 8.53723   -12.25888 -8.46998  1.000 22.46279 ? 128 ILE   A CG2 1 
ATOM   873  C CD1 . ILE   A 1 121 ? 11.15982  -13.30523 -6.85388  1.000 36.89063 ? 128 ILE   A CD1 1 
ATOM   874  N N   . SER   A 1 122 ? 7.12258   -9.02768  -6.99727  1.000 24.95972 ? 129 SER   A N   1 
ATOM   875  C CA  . SER   A 1 122 ? 5.79022   -8.57043  -7.37756  1.000 24.53875 ? 129 SER   A CA  1 
ATOM   876  C C   . SER   A 1 122 ? 5.81401   -7.27756  -8.19808  1.000 27.73142 ? 129 SER   A C   1 
ATOM   877  O O   . SER   A 1 122 ? 4.78727   -6.94464  -8.80443  1.000 27.39020 ? 129 SER   A O   1 
ATOM   878  C CB  . SER   A 1 122 ? 4.91833   -8.36747  -6.14668  1.000 26.24288 ? 129 SER   A CB  1 
ATOM   879  O OG  . SER   A 1 122 ? 5.30688   -7.18416  -5.45963  1.000 34.20078 ? 129 SER   A OG  1 
ATOM   880  N N   . MET   A 1 123 ? 6.93338   -6.50664  -8.20871  1.000 22.69744 ? 130 MET   A N   1 
ATOM   881  C CA  . MET   A 1 123 ? 6.95582   -5.31787  -9.06158  1.000 21.96494 ? 130 MET   A CA  1 
ATOM   882  C C   . MET   A 1 123 ? 7.34365   -5.60239  -10.50744 1.000 21.06302 ? 130 MET   A C   1 
ATOM   883  O O   . MET   A 1 123 ? 7.53172   -4.64193  -11.26831 1.000 23.36474 ? 130 MET   A O   1 
ATOM   884  C CB  . MET   A 1 123 ? 7.85084   -4.19678  -8.51782  1.000 22.21976 ? 130 MET   A CB  1 
ATOM   885  C CG  . MET   A 1 123 ? 7.50301   -3.74187  -7.09391  1.000 32.76291 ? 130 MET   A CG  1 
ATOM   886  S SD  . MET   A 1 123 ? 8.87015   -3.47069  -5.97017  1.000 40.23467 ? 130 MET   A SD  1 
ATOM   887  C CE  . MET   A 1 123 ? 9.15549   -1.74309  -6.33602  1.000 42.91524 ? 130 MET   A CE  1 
ATOM   888  N N   . ILE   A 1 124 ? 7.41132   -6.87657  -10.89878 1.000 19.64587 ? 131 ILE   A N   1 
ATOM   889  C CA  . ILE   A 1 124 ? 7.94640   -7.25919  -12.20181 1.000 17.56163 ? 131 ILE   A CA  1 
ATOM   890  C C   . ILE   A 1 124 ? 7.21822   -6.55490  -13.35028 1.000 21.22006 ? 131 ILE   A C   1 
ATOM   891  O O   . ILE   A 1 124 ? 7.84534   -6.19413  -14.35539 1.000 17.97618 ? 131 ILE   A O   1 
ATOM   892  C CB  . ILE   A 1 124 ? 7.88621   -8.79265  -12.34427 1.000 17.89118 ? 131 ILE   A CB  1 
ATOM   893  C CG1 . ILE   A 1 124 ? 8.51291   -9.22252  -13.67849 1.000 15.38639 ? 131 ILE   A CG1 1 
ATOM   894  C CG2 . ILE   A 1 124 ? 6.43744   -9.27860  -12.22223 1.000 19.62471 ? 131 ILE   A CG2 1 
ATOM   895  C CD1 . ILE   A 1 124 ? 8.59294   -10.80066 -13.88370 1.000 19.88162 ? 131 ILE   A CD1 1 
ATOM   896  N N   . GLY   A 1 125 ? 5.90930   -6.31494  -13.21889 1.000 20.74554 ? 132 GLY   A N   1 
ATOM   897  C CA  . GLY   A 1 125 ? 5.16526   -5.64848  -14.28668 1.000 22.75876 ? 132 GLY   A CA  1 
ATOM   898  C C   . GLY   A 1 125 ? 5.53846   -4.18638  -14.47592 1.000 28.71236 ? 132 GLY   A C   1 
ATOM   899  O O   . GLY   A 1 125 ? 5.30005   -3.62057  -15.55111 1.000 25.77344 ? 132 GLY   A O   1 
ATOM   900  N N   . GLN   A 1 126 ? 6.13387   -3.56047  -13.46717 1.000 19.01503 ? 133 GLN   A N   1 
ATOM   901  C CA  . GLN   A 1 126 ? 6.56805   -2.18809  -13.67646 1.000 24.06067 ? 133 GLN   A CA  1 
ATOM   902  C C   . GLN   A 1 126 ? 7.72007   -2.12068  -14.66147 1.000 29.54272 ? 133 GLN   A C   1 
ATOM   903  O O   . GLN   A 1 126 ? 8.03738   -1.03907  -15.16129 1.000 28.44402 ? 133 GLN   A O   1 
ATOM   904  C CB  . GLN   A 1 126 ? 6.92907   -1.52084  -12.33899 1.000 28.05996 ? 133 GLN   A CB  1 
ATOM   905  C CG  . GLN   A 1 126 ? 5.71121   -1.40818  -11.37560 1.000 30.87917 ? 133 GLN   A CG  1 
ATOM   906  C CD  . GLN   A 1 126 ? 6.06094   -1.01761  -9.93938  1.000 51.73322 ? 133 GLN   A CD  1 
ATOM   907  O OE1 . GLN   A 1 126 ? 6.72127   -0.00325  -9.70270  1.000 37.45704 ? 133 GLN   A OE1 1 
ATOM   908  N NE2 . GLN   A 1 126 ? 5.58716   -1.81419  -8.96556  1.000 42.67735 ? 133 GLN   A NE2 1 
ATOM   909  N N   . PHE   A 1 127 ? 8.29218   -3.26093  -15.02641 1.000 16.71095 ? 134 PHE   A N   1 
ATOM   910  C CA  . PHE   A 1 127 ? 9.40742   -3.29935  -15.96256 1.000 18.68577 ? 134 PHE   A CA  1 
ATOM   911  C C   . PHE   A 1 127 ? 9.04074   -3.91556  -17.29660 1.000 20.72941 ? 134 PHE   A C   1 
ATOM   912  O O   . PHE   A 1 127 ? 9.93029   -4.16369  -18.11610 1.000 20.09601 ? 134 PHE   A O   1 
ATOM   913  C CB  . PHE   A 1 127 ? 10.56708  -4.05563  -15.32299 1.000 18.16777 ? 134 PHE   A CB  1 
ATOM   914  C CG  . PHE   A 1 127 ? 10.97062  -3.46367  -14.00244 1.000 18.91272 ? 134 PHE   A CG  1 
ATOM   915  C CD1 . PHE   A 1 127 ? 11.91040  -2.43706  -13.93476 1.000 18.99230 ? 134 PHE   A CD1 1 
ATOM   916  C CD2 . PHE   A 1 127 ? 10.34115  -3.87922  -12.83265 1.000 17.97707 ? 134 PHE   A CD2 1 
ATOM   917  C CE1 . PHE   A 1 127 ? 12.25615  -1.87988  -12.70230 1.000 20.61607 ? 134 PHE   A CE1 1 
ATOM   918  C CE2 . PHE   A 1 127 ? 10.68620  -3.34172  -11.61465 1.000 18.72453 ? 134 PHE   A CE2 1 
ATOM   919  C CZ  . PHE   A 1 127 ? 11.63437  -2.33167  -11.54471 1.000 21.33988 ? 134 PHE   A CZ  1 
ATOM   920  N N   . GLY   A 1 128 ? 7.76357   -4.19186  -17.51333 1.000 22.09626 ? 135 GLY   A N   1 
ATOM   921  C CA  . GLY   A 1 128 ? 7.26319   -4.68910  -18.76883 1.000 21.52920 ? 135 GLY   A CA  1 
ATOM   922  C C   . GLY   A 1 128 ? 7.50338   -6.15302  -19.03891 1.000 22.71872 ? 135 GLY   A C   1 
ATOM   923  O O   . GLY   A 1 128 ? 7.29869   -6.58484  -20.17936 1.000 21.36795 ? 135 GLY   A O   1 
ATOM   924  N N   . VAL   A 1 129 ? 7.94988   -6.93395  -18.04783 1.000 17.52029 ? 136 VAL   A N   1 
ATOM   925  C CA  . VAL   A 1 129 ? 8.28557   -8.32532  -18.31048 1.000 16.39363 ? 136 VAL   A CA  1 
ATOM   926  C C   . VAL   A 1 129 ? 7.46109   -9.24410  -17.40445 1.000 13.51592 ? 136 VAL   A C   1 
ATOM   927  O O   . VAL   A 1 129 ? 7.92570   -10.32037 -17.01847 1.000 16.99604 ? 136 VAL   A O   1 
ATOM   928  C CB  . VAL   A 1 129 ? 9.79484   -8.57399  -18.14185 1.000 13.39087 ? 136 VAL   A CB  1 
ATOM   929  C CG1 . VAL   A 1 129 ? 10.55719  -7.84181  -19.23830 1.000 15.92547 ? 136 VAL   A CG1 1 
ATOM   930  C CG2 . VAL   A 1 129 ? 10.32263  -8.11097  -16.76520 1.000 15.03353 ? 136 VAL   A CG2 1 
ATOM   931  N N   . GLY   A 1 130 ? 6.23851   -8.82911  -17.06002 1.000 14.28536 ? 137 GLY   A N   1 
ATOM   932  C CA  . GLY   A 1 130 ? 5.41717   -9.65987  -16.18583 1.000 14.33748 ? 137 GLY   A CA  1 
ATOM   933  C C   . GLY   A 1 130 ? 5.06862   -11.01610 -16.76624 1.000 17.62961 ? 137 GLY   A C   1 
ATOM   934  O O   . GLY   A 1 130 ? 4.73619   -11.94062 -16.00924 1.000 17.72198 ? 137 GLY   A O   1 
ATOM   935  N N   . PHE   A 1 131 ? 5.09636   -11.15273 -18.09679 1.000 13.51293 ? 138 PHE   A N   1 
ATOM   936  C CA  . PHE   A 1 131 ? 4.83599   -12.45963 -18.70043 1.000 14.68469 ? 138 PHE   A CA  1 
ATOM   937  C C   . PHE   A 1 131 ? 5.63632   -13.57996 -18.02870 1.000 16.35171 ? 138 PHE   A C   1 
ATOM   938  O O   . PHE   A 1 131 ? 5.10170   -14.66582 -17.76648 1.000 17.45454 ? 138 PHE   A O   1 
ATOM   939  C CB  . PHE   A 1 131 ? 5.17963   -12.45038 -20.18814 1.000 17.81108 ? 138 PHE   A CB  1 
ATOM   940  C CG  . PHE   A 1 131 ? 5.15890   -13.84140 -20.80310 1.000 16.22779 ? 138 PHE   A CG  1 
ATOM   941  C CD1 . PHE   A 1 131 ? 3.94646   -14.45202 -21.09477 1.000 18.79874 ? 138 PHE   A CD1 1 
ATOM   942  C CD2 . PHE   A 1 131 ? 6.33892   -14.52012 -21.08815 1.000 14.98006 ? 138 PHE   A CD2 1 
ATOM   943  C CE1 . PHE   A 1 131 ? 3.89675   -15.74459 -21.62375 1.000 19.04518 ? 138 PHE   A CE1 1 
ATOM   944  C CE2 . PHE   A 1 131 ? 6.30346   -15.81178 -21.65186 1.000 20.79124 ? 138 PHE   A CE2 1 
ATOM   945  C CZ  . PHE   A 1 131 ? 5.07477   -16.41060 -21.92996 1.000 16.78238 ? 138 PHE   A CZ  1 
ATOM   946  N N   . TYR   A 1 132 ? 6.93068   -13.33294 -17.74405 1.000 14.76830 ? 139 TYR   A N   1 
ATOM   947  C CA  . TYR   A 1 132 ? 7.78364   -14.41317 -17.25508 1.000 13.23795 ? 139 TYR   A CA  1 
ATOM   948  C C   . TYR   A 1 132 ? 7.37972   -14.85181 -15.84522 1.000 14.55153 ? 139 TYR   A C   1 
ATOM   949  O O   . TYR   A 1 132 ? 7.82204   -15.92088 -15.39799 1.000 16.38612 ? 139 TYR   A O   1 
ATOM   950  C CB  . TYR   A 1 132 ? 9.25852   -13.98730 -17.32134 1.000 16.30525 ? 139 TYR   A CB  1 
ATOM   951  C CG  . TYR   A 1 132 ? 9.64696   -13.65351 -18.75001 1.000 17.61058 ? 139 TYR   A CG  1 
ATOM   952  C CD1 . TYR   A 1 132 ? 9.96219   -14.67471 -19.67639 1.000 17.25413 ? 139 TYR   A CD1 1 
ATOM   953  C CD2 . TYR   A 1 132 ? 9.60891   -12.34663 -19.19582 1.000 14.08838 ? 139 TYR   A CD2 1 
ATOM   954  C CE1 . TYR   A 1 132 ? 10.26124  -14.37589 -20.99901 1.000 15.40022 ? 139 TYR   A CE1 1 
ATOM   955  C CE2 . TYR   A 1 132 ? 9.88835   -12.03039 -20.53603 1.000 18.38121 ? 139 TYR   A CE2 1 
ATOM   956  C CZ  . TYR   A 1 132 ? 10.23448  -13.04585 -21.42311 1.000 15.78926 ? 139 TYR   A CZ  1 
ATOM   957  O OH  . TYR   A 1 132 ? 10.51867  -12.70731 -22.73661 1.000 17.89206 ? 139 TYR   A OH  1 
ATOM   958  N N   . SER   A 1 133 ? 6.51577   -14.08925 -15.16378 1.000 19.12681 ? 140 SER   A N   1 
ATOM   959  C CA  . SER   A 1 133 ? 6.04617   -14.53242 -13.84395 1.000 15.85029 ? 140 SER   A CA  1 
ATOM   960  C C   . SER   A 1 133 ? 5.16212   -15.77036 -13.93986 1.000 16.95023 ? 140 SER   A C   1 
ATOM   961  O O   . SER   A 1 133 ? 4.87584   -16.38945 -12.91674 1.000 16.80656 ? 140 SER   A O   1 
ATOM   962  C CB  . SER   A 1 133 ? 5.28051   -13.41298 -13.11580 1.000 17.81271 ? 140 SER   A CB  1 
ATOM   963  O OG  . SER   A 1 133 ? 3.97730   -13.21329 -13.68241 1.000 18.30957 ? 140 SER   A OG  1 
ATOM   964  N N   . ALA   A 1 134 ? 4.73231   -16.14138 -15.14071 1.000 16.24114 ? 141 ALA   A N   1 
ATOM   965  C CA  . ALA   A 1 134 ? 4.09972   -17.44205 -15.35009 1.000 13.86839 ? 141 ALA   A CA  1 
ATOM   966  C C   . ALA   A 1 134 ? 4.92869   -18.58029 -14.75454 1.000 14.84022 ? 141 ALA   A C   1 
ATOM   967  O O   . ALA   A 1 134 ? 4.36138   -19.54863 -14.25543 1.000 18.22867 ? 141 ALA   A O   1 
ATOM   968  C CB  . ALA   A 1 134 ? 3.87903   -17.68023 -16.86819 1.000 11.82875 ? 141 ALA   A CB  1 
ATOM   969  N N   . TYR   A 1 135 ? 6.27508   -18.47154 -14.78098 1.000 16.41305 ? 142 TYR   A N   1 
ATOM   970  C CA  . TYR   A 1 135 ? 7.12193   -19.54827 -14.28216 1.000 16.24738 ? 142 TYR   A CA  1 
ATOM   971  C C   . TYR   A 1 135 ? 7.20198   -19.59138 -12.76327 1.000 20.67459 ? 142 TYR   A C   1 
ATOM   972  O O   . TYR   A 1 135 ? 7.92745   -20.43187 -12.22427 1.000 20.33562 ? 142 TYR   A O   1 
ATOM   973  C CB  . TYR   A 1 135 ? 8.51966   -19.44680 -14.90851 1.000 14.01809 ? 142 TYR   A CB  1 
ATOM   974  C CG  . TYR   A 1 135 ? 8.39519   -19.79045 -16.39150 1.000 14.00049 ? 142 TYR   A CG  1 
ATOM   975  C CD1 . TYR   A 1 135 ? 8.49692   -21.11825 -16.82915 1.000 16.81596 ? 142 TYR   A CD1 1 
ATOM   976  C CD2 . TYR   A 1 135 ? 8.12147   -18.79666 -17.33225 1.000 19.91461 ? 142 TYR   A CD2 1 
ATOM   977  C CE1 . TYR   A 1 135 ? 8.33617   -21.45975 -18.19212 1.000 17.24428 ? 142 TYR   A CE1 1 
ATOM   978  C CE2 . TYR   A 1 135 ? 7.96560   -19.12002 -18.68450 1.000 18.86372 ? 142 TYR   A CE2 1 
ATOM   979  C CZ  . TYR   A 1 135 ? 8.07139   -20.44914 -19.10702 1.000 22.03890 ? 142 TYR   A CZ  1 
ATOM   980  O OH  . TYR   A 1 135 ? 7.89735   -20.74781 -20.45933 1.000 18.71889 ? 142 TYR   A OH  1 
ATOM   981  N N   . LEU   A 1 136 ? 6.48020   -18.71460 -12.06790 1.000 15.95486 ? 143 LEU   A N   1 
ATOM   982  C CA  . LEU   A 1 136 ? 6.29843   -18.89956 -10.63455 1.000 17.22154 ? 143 LEU   A CA  1 
ATOM   983  C C   . LEU   A 1 136 ? 5.47037   -20.13971 -10.35728 1.000 22.88650 ? 143 LEU   A C   1 
ATOM   984  O O   . LEU   A 1 136 ? 5.64326   -20.78572 -9.31560  1.000 20.69797 ? 143 LEU   A O   1 
ATOM   985  C CB  . LEU   A 1 136 ? 5.58591   -17.67520 -10.04581 1.000 19.57685 ? 143 LEU   A CB  1 
ATOM   986  C CG  . LEU   A 1 136 ? 6.40124   -16.37393 -9.97181  1.000 18.29232 ? 143 LEU   A CG  1 
ATOM   987  C CD1 . LEU   A 1 136 ? 5.42773   -15.25842 -9.61708  1.000 17.55058 ? 143 LEU   A CD1 1 
ATOM   988  C CD2 . LEU   A 1 136 ? 7.57333   -16.50188 -8.92821  1.000 18.46168 ? 143 LEU   A CD2 1 
ATOM   989  N N   . VAL   A 1 137 ? 4.51563   -20.44432 -11.23894 1.000 19.00747 ? 144 VAL   A N   1 
ATOM   990  C CA  . VAL   A 1 137 ? 3.57706   -21.53268 -10.99546 1.000 17.87946 ? 144 VAL   A CA  1 
ATOM   991  C C   . VAL   A 1 137 ? 3.58492   -22.60153 -12.08031 1.000 18.05834 ? 144 VAL   A C   1 
ATOM   992  O O   . VAL   A 1 137 ? 3.01877   -23.68884 -11.84968 1.000 19.10021 ? 144 VAL   A O   1 
ATOM   993  C CB  . VAL   A 1 137 ? 2.14285   -21.01593 -10.81546 1.000 16.86886 ? 144 VAL   A CB  1 
ATOM   994  C CG1 . VAL   A 1 137 ? 2.03178   -20.08255 -9.55881  1.000 18.67722 ? 144 VAL   A CG1 1 
ATOM   995  C CG2 . VAL   A 1 137 ? 1.67994   -20.34425 -12.12298 1.000 17.46022 ? 144 VAL   A CG2 1 
ATOM   996  N N   . ALA   A 1 138 ? 4.16025   -22.35011 -13.25250 1.000 16.56545 ? 145 ALA   A N   1 
ATOM   997  C CA  . ALA   A 1 138 ? 4.08690   -23.30687 -14.34407 1.000 16.27267 ? 145 ALA   A CA  1 
ATOM   998  C C   . ALA   A 1 138 ? 5.45116   -23.92338 -14.59721 1.000 21.70395 ? 145 ALA   A C   1 
ATOM   999  O O   . ALA   A 1 138 ? 6.46274   -23.22135 -14.61140 1.000 22.93696 ? 145 ALA   A O   1 
ATOM   1000 C CB  . ALA   A 1 138 ? 3.61761   -22.64326 -15.63913 1.000 16.55786 ? 145 ALA   A CB  1 
ATOM   1001 N N   . GLU   A 1 139 ? 5.47542   -25.22706 -14.83572 1.000 19.60334 ? 146 GLU   A N   1 
ATOM   1002 C CA  . GLU   A 1 139 ? 6.71837   -25.84355 -15.27421 1.000 23.55962 ? 146 GLU   A CA  1 
ATOM   1003 C C   . GLU   A 1 139 ? 6.86994   -25.75867 -16.78617 1.000 32.42043 ? 146 GLU   A C   1 
ATOM   1004 O O   . GLU   A 1 139 ? 7.98943   -25.89259 -17.30894 1.000 24.75838 ? 146 GLU   A O   1 
ATOM   1005 C CB  . GLU   A 1 139 ? 6.77698   -27.29562 -14.78606 1.000 25.42819 ? 146 GLU   A CB  1 
ATOM   1006 C CG  . GLU   A 1 139 ? 5.75359   -28.16817 -15.43014 1.000 31.41214 ? 146 GLU   A CG  1 
ATOM   1007 C CD  . GLU   A 1 139 ? 5.71317   -29.57818 -14.85203 1.000 62.89624 ? 146 GLU   A CD  1 
ATOM   1008 O OE1 . GLU   A 1 139 ? 6.43525   -29.84698 -13.86203 1.000 57.64059 ? 146 GLU   A OE1 1 
ATOM   1009 O OE2 . GLU   A 1 139 ? 4.94418   -30.41155 -15.38841 1.000 49.76512 ? 146 GLU   A OE2 1 
ATOM   1010 N N   . LYS   A 1 140 ? 5.76909   -25.52562 -17.49106 1.000 18.96448 ? 147 LYS   A N   1 
ATOM   1011 C CA  . LYS   A 1 140 ? 5.81205   -25.35315 -18.93410 1.000 17.03518 ? 147 LYS   A CA  1 
ATOM   1012 C C   . LYS   A 1 140 ? 4.72378   -24.36273 -19.29546 1.000 22.80084 ? 147 LYS   A C   1 
ATOM   1013 O O   . LYS   A 1 140 ? 3.66929   -24.32071 -18.65265 1.000 18.06262 ? 147 LYS   A O   1 
ATOM   1014 C CB  . LYS   A 1 140 ? 5.65406   -26.71459 -19.65597 1.000 18.45742 ? 147 LYS   A CB  1 
ATOM   1015 C CG  . LYS   A 1 140 ? 5.48709   -26.61900 -21.14470 1.000 24.15591 ? 147 LYS   A CG  1 
ATOM   1016 C CD  . LYS   A 1 140 ? 5.58187   -28.03484 -21.73873 1.000 31.00098 ? 147 LYS   A CD  1 
ATOM   1017 C CE  . LYS   A 1 140 ? 4.32396   -28.46162 -22.42665 1.000 39.80054 ? 147 LYS   A CE  1 
ATOM   1018 N NZ  . LYS   A 1 140 ? 4.32868   -29.95940 -22.51644 1.000 43.04258 ? 147 LYS   A NZ  1 
ATOM   1019 N N   . VAL   A 1 141 ? 5.00031   -23.53092 -20.29529 1.000 15.89931 ? 148 VAL   A N   1 
ATOM   1020 C CA  . VAL   A 1 141 ? 4.03228   -22.56200 -20.77351 1.000 18.01084 ? 148 VAL   A CA  1 
ATOM   1021 C C   . VAL   A 1 141 ? 3.91242   -22.72789 -22.28031 1.000 18.16519 ? 148 VAL   A C   1 
ATOM   1022 O O   . VAL   A 1 141 ? 4.93057   -22.74931 -22.98500 1.000 17.85943 ? 148 VAL   A O   1 
ATOM   1023 C CB  . VAL   A 1 141 ? 4.43839   -21.11027 -20.43479 1.000 15.33018 ? 148 VAL   A CB  1 
ATOM   1024 C CG1 . VAL   A 1 141 ? 3.34906   -20.14065 -20.93075 1.000 15.29317 ? 148 VAL   A CG1 1 
ATOM   1025 C CG2 . VAL   A 1 141 ? 4.66725   -20.93825 -18.93275 1.000 19.35857 ? 148 VAL   A CG2 1 
ATOM   1026 N N   . THR   A 1 142 ? 2.67974   -22.89936 -22.76216 1.000 18.21627 ? 149 THR   A N   1 
ATOM   1027 C CA  . THR   A 1 142 ? 2.37635   -22.92200 -24.19333 1.000 16.82362 ? 149 THR   A CA  1 
ATOM   1028 C C   . THR   A 1 142 ? 1.54106   -21.69175 -24.51756 1.000 19.24631 ? 149 THR   A C   1 
ATOM   1029 O O   . THR   A 1 142 ? 0.60809   -21.35270 -23.77508 1.000 19.30077 ? 149 THR   A O   1 
ATOM   1030 C CB  . THR   A 1 142 ? 1.59426   -24.17908 -24.58477 1.000 20.30707 ? 149 THR   A CB  1 
ATOM   1031 O OG1 . THR   A 1 142 ? 2.23192   -25.32274 -24.02730 1.000 20.48553 ? 149 THR   A OG1 1 
ATOM   1032 C CG2 . THR   A 1 142 ? 1.51993   -24.33365 -26.14625 1.000 21.60426 ? 149 THR   A CG2 1 
ATOM   1033 N N   . VAL   A 1 143 ? 1.88040   -20.99957 -25.60096 1.000 17.10330 ? 150 VAL   A N   1 
ATOM   1034 C CA  . VAL   A 1 143 ? 1.15583   -19.78963 -25.97971 1.000 14.46780 ? 150 VAL   A CA  1 
ATOM   1035 C C   . VAL   A 1 143 ? 0.71247   -19.96920 -27.41435 1.000 20.71554 ? 150 VAL   A C   1 
ATOM   1036 O O   . VAL   A 1 143 ? 1.56000   -20.13617 -28.30252 1.000 20.82646 ? 150 VAL   A O   1 
ATOM   1037 C CB  . VAL   A 1 143 ? 2.02291   -18.52251 -25.84901 1.000 18.24843 ? 150 VAL   A CB  1 
ATOM   1038 C CG1 . VAL   A 1 143 ? 1.24977   -17.30510 -26.29165 1.000 19.56962 ? 150 VAL   A CG1 1 
ATOM   1039 C CG2 . VAL   A 1 143 ? 2.50763   -18.32929 -24.41804 1.000 17.74689 ? 150 VAL   A CG2 1 
ATOM   1040 N N   . ILE   A 1 144 ? -0.60292  -19.97005 -27.63773 1.000 17.94611 ? 151 ILE   A N   1 
ATOM   1041 C CA  . ILE   A 1 144 ? -1.18814  -20.09959 -28.97164 1.000 15.29231 ? 151 ILE   A CA  1 
ATOM   1042 C C   . ILE   A 1 144 ? -1.68579  -18.71899 -29.32837 1.000 19.93244 ? 151 ILE   A C   1 
ATOM   1043 O O   . ILE   A 1 144 ? -2.33604  -18.06867 -28.50331 1.000 20.25184 ? 151 ILE   A O   1 
ATOM   1044 C CB  . ILE   A 1 144 ? -2.35822  -21.10788 -29.01443 1.000 18.60684 ? 151 ILE   A CB  1 
ATOM   1045 C CG1 . ILE   A 1 144 ? -2.03335  -22.41924 -28.29579 1.000 27.55935 ? 151 ILE   A CG1 1 
ATOM   1046 C CG2 . ILE   A 1 144 ? -2.79022  -21.37352 -30.43916 1.000 20.47773 ? 151 ILE   A CG2 1 
ATOM   1047 C CD1 . ILE   A 1 144 ? -0.96791  -23.17245 -28.95057 1.000 24.36207 ? 151 ILE   A CD1 1 
ATOM   1048 N N   . THR   A 1 145 ? -1.39858  -18.26829 -30.54671 1.000 18.28250 ? 152 THR   A N   1 
ATOM   1049 C CA  . THR   A 1 145 ? -1.71153  -16.88725 -30.83597 1.000 19.99222 ? 152 THR   A CA  1 
ATOM   1050 C C   . THR   A 1 145 ? -1.96554  -16.70267 -32.31483 1.000 20.91093 ? 152 THR   A C   1 
ATOM   1051 O O   . THR   A 1 145 ? -1.38255  -17.39457 -33.15271 1.000 20.56603 ? 152 THR   A O   1 
ATOM   1052 C CB  . THR   A 1 145 ? -0.57835  -15.97646 -30.35145 1.000 21.55726 ? 152 THR   A CB  1 
ATOM   1053 O OG1 . THR   A 1 145 ? -0.98200  -14.60945 -30.46462 1.000 16.87709 ? 152 THR   A OG1 1 
ATOM   1054 C CG2 . THR   A 1 145 ? 0.67821   -16.22399 -31.15434 1.000 17.69970 ? 152 THR   A CG2 1 
ATOM   1055 N N   . LYS   A 1 146 ? -2.83031  -15.73972 -32.62362 1.000 16.60689 ? 153 LYS   A N   1 
ATOM   1056 C CA  . LYS   A 1 146 ? -3.18610  -15.43872 -34.00371 1.000 17.44230 ? 153 LYS   A CA  1 
ATOM   1057 C C   . LYS   A 1 146 ? -3.32951  -13.92740 -34.11698 1.000 21.41002 ? 153 LYS   A C   1 
ATOM   1058 O O   . LYS   A 1 146 ? -4.16707  -13.34274 -33.43096 1.000 17.04238 ? 153 LYS   A O   1 
ATOM   1059 C CB  . LYS   A 1 146 ? -4.49087  -16.14371 -34.38389 1.000 21.63569 ? 153 LYS   A CB  1 
ATOM   1060 C CG  . LYS   A 1 146 ? -5.03707  -15.76414 -35.76774 1.000 27.53011 ? 153 LYS   A CG  1 
ATOM   1061 C CD  . LYS   A 1 146 ? -4.18602  -16.36893 -36.86381 1.000 23.42778 ? 153 LYS   A CD  1 
ATOM   1062 C CE  . LYS   A 1 146 ? -4.83726  -16.14186 -38.23814 1.000 30.37125 ? 153 LYS   A CE  1 
ATOM   1063 N NZ  . LYS   A 1 146 ? -4.87149  -14.67633 -38.64773 1.000 23.86762 ? 153 LYS   A NZ  1 
ATOM   1064 N N   . HIS   A 1 147 ? -2.51764  -13.30852 -34.96222 1.000 22.24808 ? 154 HIS   A N   1 
ATOM   1065 C CA  . HIS   A 1 147 ? -2.59536  -11.89126 -35.28577 1.000 19.22884 ? 154 HIS   A CA  1 
ATOM   1066 C C   . HIS   A 1 147 ? -3.23872  -11.78197 -36.66686 1.000 20.64301 ? 154 HIS   A C   1 
ATOM   1067 O O   . HIS   A 1 147 ? -3.02843  -12.65513 -37.51544 1.000 21.33390 ? 154 HIS   A O   1 
ATOM   1068 C CB  . HIS   A 1 147 ? -1.18140  -11.29386 -35.26658 1.000 20.48306 ? 154 HIS   A CB  1 
ATOM   1069 C CG  . HIS   A 1 147 ? -1.09852  -9.80595  -35.46869 1.000 24.30801 ? 154 HIS   A CG  1 
ATOM   1070 N ND1 . HIS   A 1 147 ? -1.27875  -9.20505  -36.69283 1.000 21.12367 ? 154 HIS   A ND1 1 
ATOM   1071 C CD2 . HIS   A 1 147 ? -0.84895  -8.79897  -34.58902 1.000 19.73685 ? 154 HIS   A CD2 1 
ATOM   1072 C CE1 . HIS   A 1 147 ? -1.13481  -7.89411  -36.57086 1.000 22.27128 ? 154 HIS   A CE1 1 
ATOM   1073 N NE2 . HIS   A 1 147 ? -0.87411  -7.62459  -35.30086 1.000 25.05468 ? 154 HIS   A NE2 1 
ATOM   1074 N N   . ASN   A 1 148 ? -4.04506  -10.72953 -36.87832 1.000 21.39163 ? 155 ASN   A N   1 
ATOM   1075 C CA  . ASN   A 1 148 ? -4.70592  -10.53461 -38.17480 1.000 23.00639 ? 155 ASN   A CA  1 
ATOM   1076 C C   . ASN   A 1 148 ? -3.73096  -10.62346 -39.34179 1.000 28.14532 ? 155 ASN   A C   1 
ATOM   1077 O O   . ASN   A 1 148 ? -4.12682  -10.97022 -40.46498 1.000 25.67944 ? 155 ASN   A O   1 
ATOM   1078 C CB  . ASN   A 1 148 ? -5.39952  -9.16632  -38.26149 1.000 23.89647 ? 155 ASN   A CB  1 
ATOM   1079 C CG  . ASN   A 1 148 ? -6.74205  -9.11191  -37.53543 1.000 27.52686 ? 155 ASN   A CG  1 
ATOM   1080 O OD1 . ASN   A 1 148 ? -7.41590  -10.12230 -37.35170 1.000 24.21974 ? 155 ASN   A OD1 1 
ATOM   1081 N ND2 . ASN   A 1 148 ? -7.13647  -7.90505  -37.12735 1.000 28.34428 ? 155 ASN   A ND2 1 
ATOM   1082 N N   . ASP   A 1 149 ? -2.47966  -10.24231 -39.12558 1.000 23.37203 ? 156 ASP   A N   1 
ATOM   1083 C CA  . ASP   A 1 149 ? -1.52677  -10.15086 -40.22060 1.000 30.29772 ? 156 ASP   A CA  1 
ATOM   1084 C C   . ASP   A 1 149 ? -0.66582  -11.40254 -40.38588 1.000 28.74876 ? 156 ASP   A C   1 
ATOM   1085 O O   . ASP   A 1 149 ? 0.26953   -11.38547 -41.19549 1.000 28.62593 ? 156 ASP   A O   1 
ATOM   1086 C CB  . ASP   A 1 149 ? -0.62730  -8.92589  -40.03206 1.000 27.86875 ? 156 ASP   A CB  1 
ATOM   1087 C CG  . ASP   A 1 149 ? -1.39072  -7.61442  -40.15705 1.000 33.98604 ? 156 ASP   A CG  1 
ATOM   1088 O OD1 . ASP   A 1 149 ? -2.53329  -7.61293  -40.67030 1.000 36.96236 ? 156 ASP   A OD1 1 
ATOM   1089 O OD2 . ASP   A 1 149 ? -0.82887  -6.57920  -39.76982 1.000 30.90216 ? 156 ASP   A OD2 1 
ATOM   1090 N N   . ASP   A 1 150 ? -0.95099  -12.48526 -39.66443 1.000 25.10288 ? 157 ASP   A N   1 
ATOM   1091 C CA  . ASP   A 1 150 ? -0.06460  -13.64560 -39.69309 1.000 23.56463 ? 157 ASP   A CA  1 
ATOM   1092 C C   . ASP   A 1 150 ? -0.88007  -14.91539 -39.43704 1.000 32.81575 ? 157 ASP   A C   1 
ATOM   1093 O O   . ASP   A 1 150 ? -2.09750  -14.86428 -39.23898 1.000 26.14286 ? 157 ASP   A O   1 
ATOM   1094 C CB  . ASP   A 1 150 ? 1.08180   -13.44957 -38.68427 1.000 22.26937 ? 157 ASP   A CB  1 
ATOM   1095 C CG  . ASP   A 1 150 ? 2.36238   -14.19578 -39.08135 1.000 32.70338 ? 157 ASP   A CG  1 
ATOM   1096 O OD1 . ASP   A 1 150 ? 2.30432   -15.06089 -39.98321 1.000 30.51776 ? 157 ASP   A OD1 1 
ATOM   1097 O OD2 . ASP   A 1 150 ? 3.43678   -13.89534 -38.51763 1.000 27.02692 ? 157 ASP   A OD2 1 
ATOM   1098 N N   . GLU   A 1 151 ? -0.20371  -16.06951 -39.48135 1.000 25.75381 ? 158 GLU   A N   1 
ATOM   1099 C CA  . GLU   A 1 151 ? -0.84722  -17.36255 -39.25789 1.000 24.77062 ? 158 GLU   A CA  1 
ATOM   1100 C C   . GLU   A 1 151 ? -0.93915  -17.65791 -37.76278 1.000 24.48957 ? 158 GLU   A C   1 
ATOM   1101 O O   . GLU   A 1 151 ? -0.38908  -16.93777 -36.93245 1.000 21.53916 ? 158 GLU   A O   1 
ATOM   1102 C CB  . GLU   A 1 151 ? -0.06266  -18.47766 -39.94367 1.000 26.17061 ? 158 GLU   A CB  1 
ATOM   1103 C CG  . GLU   A 1 151 ? 0.09664   -18.31294 -41.45009 1.000 42.45414 ? 158 GLU   A CG  1 
ATOM   1104 C CD  . GLU   A 1 151 ? 1.04629   -19.35818 -42.01830 1.000 76.47040 ? 158 GLU   A CD  1 
ATOM   1105 O OE1 . GLU   A 1 151 ? 1.82546   -19.02604 -42.93807 1.000 86.33417 ? 158 GLU   A OE1 1 
ATOM   1106 O OE2 . GLU   A 1 151 ? 1.04635   -20.50374 -41.51115 1.000 78.65407 ? 158 GLU   A OE2 1 
ATOM   1107 N N   . GLN   A 1 152 ? -1.61075  -18.75912 -37.41927 1.000 23.27442 ? 159 GLN   A N   1 
ATOM   1108 C CA  . GLN   A 1 152 ? -1.69482  -19.17010 -36.02216 1.000 24.32350 ? 159 GLN   A CA  1 
ATOM   1109 C C   . GLN   A 1 152 ? -0.43017  -19.93617 -35.62438 1.000 24.36610 ? 159 GLN   A C   1 
ATOM   1110 O O   . GLN   A 1 152 ? -0.04128  -20.90440 -36.29271 1.000 23.42309 ? 159 GLN   A O   1 
ATOM   1111 C CB  . GLN   A 1 152 ? -2.93491  -20.02954 -35.80110 1.000 27.26728 ? 159 GLN   A CB  1 
ATOM   1112 C CG  . GLN   A 1 152 ? -3.23803  -20.29843 -34.31900 1.000 23.64420 ? 159 GLN   A CG  1 
ATOM   1113 C CD  . GLN   A 1 152 ? -4.64876  -20.78986 -34.15552 1.000 27.38045 ? 159 GLN   A CD  1 
ATOM   1114 O OE1 . GLN   A 1 152 ? -5.60397  -20.16091 -34.64410 1.000 26.88946 ? 159 GLN   A OE1 1 
ATOM   1115 N NE2 . GLN   A 1 152 ? -4.79756  -21.94767 -33.53034 1.000 26.52891 ? 159 GLN   A NE2 1 
ATOM   1116 N N   . TYR   A 1 153 ? 0.20181   -19.51790 -34.52349 1.000 22.21990 ? 160 TYR   A N   1 
ATOM   1117 C CA  . TYR   A 1 153 ? 1.45428   -20.11267 -34.06678 1.000 23.58596 ? 160 TYR   A CA  1 
ATOM   1118 C C   . TYR   A 1 153 ? 1.32403   -20.63751 -32.64849 1.000 22.05446 ? 160 TYR   A C   1 
ATOM   1119 O O   . TYR   A 1 153 ? 0.53726   -20.11357 -31.85517 1.000 18.51010 ? 160 TYR   A O   1 
ATOM   1120 C CB  . TYR   A 1 153 ? 2.59108   -19.09642 -34.07202 1.000 19.13666 ? 160 TYR   A CB  1 
ATOM   1121 C CG  . TYR   A 1 153 ? 3.02857   -18.77402 -35.45983 1.000 22.87638 ? 160 TYR   A CG  1 
ATOM   1122 C CD1 . TYR   A 1 153 ? 3.85648   -19.64530 -36.16603 1.000 23.34599 ? 160 TYR   A CD1 1 
ATOM   1123 C CD2 . TYR   A 1 153 ? 2.59287   -17.61717 -36.08733 1.000 34.56137 ? 160 TYR   A CD2 1 
ATOM   1124 C CE1 . TYR   A 1 153 ? 4.25556   -19.35926 -37.43583 1.000 35.92725 ? 160 TYR   A CE1 1 
ATOM   1125 C CE2 . TYR   A 1 153 ? 2.96886   -17.33595 -37.38351 1.000 32.44425 ? 160 TYR   A CE2 1 
ATOM   1126 C CZ  . TYR   A 1 153 ? 3.80324   -18.20049 -38.04649 1.000 39.09635 ? 160 TYR   A CZ  1 
ATOM   1127 O OH  . TYR   A 1 153 ? 4.19152   -17.91451 -39.33342 1.000 50.56981 ? 160 TYR   A OH  1 
ATOM   1128 N N   . ALA   A 1 154 ? 2.14989   -21.62873 -32.32150 1.000 20.76753 ? 161 ALA   A N   1 
ATOM   1129 C CA  . ALA   A 1 154 ? 2.34249   -22.07012 -30.93890 1.000 19.31602 ? 161 ALA   A CA  1 
ATOM   1130 C C   . ALA   A 1 154 ? 3.77049   -21.79337 -30.48790 1.000 19.86352 ? 161 ALA   A C   1 
ATOM   1131 O O   . ALA   A 1 154 ? 4.72302   -22.31140 -31.08119 1.000 22.94824 ? 161 ALA   A O   1 
ATOM   1132 C CB  . ALA   A 1 154 ? 2.04163   -23.56504 -30.79455 1.000 23.11533 ? 161 ALA   A CB  1 
ATOM   1133 N N   . TRP   A 1 155 ? 3.90873   -21.05728 -29.38422 1.000 17.46053 ? 162 TRP   A N   1 
ATOM   1134 C CA  . TRP   A 1 155 ? 5.17786   -20.82637 -28.70585 1.000 19.20454 ? 162 TRP   A CA  1 
ATOM   1135 C C   . TRP   A 1 155 ? 5.16659   -21.67652 -27.43910 1.000 18.31378 ? 162 TRP   A C   1 
ATOM   1136 O O   . TRP   A 1 155 ? 4.11302   -21.85598 -26.82579 1.000 17.76664 ? 162 TRP   A O   1 
ATOM   1137 C CB  . TRP   A 1 155 ? 5.31711   -19.34456 -28.34981 1.000 16.67329 ? 162 TRP   A CB  1 
ATOM   1138 C CG  . TRP   A 1 155 ? 6.52105   -18.88019 -27.56377 1.000 16.15220 ? 162 TRP   A CG  1 
ATOM   1139 C CD1 . TRP   A 1 155 ? 7.58492   -18.16363 -28.03977 1.000 17.49586 ? 162 TRP   A CD1 1 
ATOM   1140 C CD2 . TRP   A 1 155 ? 6.73936   -19.02381 -26.14532 1.000 16.99069 ? 162 TRP   A CD2 1 
ATOM   1141 N NE1 . TRP   A 1 155 ? 8.44850   -17.83817 -26.99211 1.000 16.79153 ? 162 TRP   A NE1 1 
ATOM   1142 C CE2 . TRP   A 1 155 ? 7.95247   -18.36977 -25.83427 1.000 20.59235 ? 162 TRP   A CE2 1 
ATOM   1143 C CE3 . TRP   A 1 155 ? 6.01870   -19.63380 -25.11184 1.000 16.91942 ? 162 TRP   A CE3 1 
ATOM   1144 C CZ2 . TRP   A 1 155 ? 8.47865   -18.33480 -24.54094 1.000 20.16743 ? 162 TRP   A CZ2 1 
ATOM   1145 C CZ3 . TRP   A 1 155 ? 6.55093   -19.58303 -23.79485 1.000 16.51767 ? 162 TRP   A CZ3 1 
ATOM   1146 C CH2 . TRP   A 1 155 ? 7.75051   -18.93284 -23.53790 1.000 19.93464 ? 162 TRP   A CH2 1 
ATOM   1147 N N   . GLU   A 1 156 ? 6.31473   -22.22617 -27.05690 1.000 17.94320 ? 163 GLU   A N   1 
ATOM   1148 C CA  . GLU   A 1 156 ? 6.33173   -23.11291 -25.90405 1.000 18.54891 ? 163 GLU   A CA  1 
ATOM   1149 C C   . GLU   A 1 156 ? 7.69321   -23.08438 -25.23342 1.000 18.79795 ? 163 GLU   A C   1 
ATOM   1150 O O   . GLU   A 1 156 ? 8.72522   -23.09341 -25.91690 1.000 19.27867 ? 163 GLU   A O   1 
ATOM   1151 C CB  . GLU   A 1 156 ? 6.01455   -24.54191 -26.31044 1.000 22.35474 ? 163 GLU   A CB  1 
ATOM   1152 C CG  . GLU   A 1 156 ? 5.78682   -25.47726 -25.15314 1.000 23.34144 ? 163 GLU   A CG  1 
ATOM   1153 C CD  . GLU   A 1 156 ? 5.06910   -26.72302 -25.61058 1.000 49.00039 ? 163 GLU   A CD  1 
ATOM   1154 O OE1 . GLU   A 1 156 ? 5.77635   -27.59777 -26.14185 1.000 37.62391 ? 163 GLU   A OE1 1 
ATOM   1155 O OE2 . GLU   A 1 156 ? 3.83055   -26.84106 -25.43298 1.000 37.28286 ? 163 GLU   A OE2 1 
ATOM   1156 N N   . SER   A 1 157 ? 7.70109   -23.12834 -23.90176 1.000 18.89399 ? 164 SER   A N   1 
ATOM   1157 C CA  . SER   A 1 157 ? 8.98647   -23.22409 -23.22533 1.000 19.52175 ? 164 SER   A CA  1 
ATOM   1158 C C   . SER   A 1 157 ? 8.82212   -23.81585 -21.83443 1.000 20.29989 ? 164 SER   A C   1 
ATOM   1159 O O   . SER   A 1 157 ? 7.93541   -23.41181 -21.07722 1.000 20.03085 ? 164 SER   A O   1 
ATOM   1160 C CB  . SER   A 1 157 ? 9.67690   -21.86748 -23.09796 1.000 18.97016 ? 164 SER   A CB  1 
ATOM   1161 O OG  . SER   A 1 157 ? 10.95005  -22.05115 -22.46887 1.000 20.00963 ? 164 SER   A OG  1 
ATOM   1162 N N   . SER   A 1 158 ? 9.72828   -24.73004 -21.50480 1.000 18.67997 ? 165 SER   A N   1 
ATOM   1163 C CA  . SER   A 1 158 ? 9.89696   -25.24808 -20.15527 1.000 19.22660 ? 165 SER   A CA  1 
ATOM   1164 C C   . SER   A 1 158 ? 11.09989  -24.61638 -19.47942 1.000 24.91248 ? 165 SER   A C   1 
ATOM   1165 O O   . SER   A 1 158 ? 11.68533  -25.22948 -18.57248 1.000 24.07769 ? 165 SER   A O   1 
ATOM   1166 C CB  . SER   A 1 158 ? 10.06360  -26.77312 -20.20176 1.000 26.93386 ? 165 SER   A CB  1 
ATOM   1167 O OG  . SER   A 1 158 ? 8.85717   -27.41073 -20.59202 1.000 26.52583 ? 165 SER   A OG  1 
ATOM   1168 N N   . ALA   A 1 159 ? 11.51195  -23.43510 -19.95209 1.000 19.05804 ? 166 ALA   A N   1 
ATOM   1169 C CA  . ALA   A 1 159 ? 12.71224  -22.74644 -19.48765 1.000 24.72354 ? 166 ALA   A CA  1 
ATOM   1170 C C   . ALA   A 1 159 ? 13.94661  -23.57740 -19.85301 1.000 24.35393 ? 166 ALA   A C   1 
ATOM   1171 O O   . ALA   A 1 159 ? 14.00053  -24.16255 -20.94007 1.000 26.36109 ? 166 ALA   A O   1 
ATOM   1172 C CB  . ALA   A 1 159 ? 12.63388  -22.45097 -17.97796 1.000 23.18597 ? 166 ALA   A CB  1 
ATOM   1173 N N   . GLY   A 1 160 ? 14.95706  -23.62767 -18.99094 1.000 24.60700 ? 167 GLY   A N   1 
ATOM   1174 C CA  . GLY   A 1 160 ? 16.17926  -24.30620 -19.40618 1.000 26.69612 ? 167 GLY   A CA  1 
ATOM   1175 C C   . GLY   A 1 160 ? 16.92751  -23.67305 -20.56715 1.000 27.18203 ? 167 GLY   A C   1 
ATOM   1176 O O   . GLY   A 1 160 ? 17.79736  -24.33280 -21.16578 1.000 29.26564 ? 167 GLY   A O   1 
ATOM   1177 N N   . GLY   A 1 161 ? 16.59870  -22.43031 -20.93689 1.000 22.85932 ? 168 GLY   A N   1 
ATOM   1178 C CA  . GLY   A 1 161 ? 17.36241  -21.68481 -21.91830 1.000 22.95864 ? 168 GLY   A CA  1 
ATOM   1179 C C   . GLY   A 1 161 ? 16.82609  -21.70394 -23.33799 1.000 23.63008 ? 168 GLY   A C   1 
ATOM   1180 O O   . GLY   A 1 161 ? 17.41919  -21.05795 -24.20817 1.000 22.76948 ? 168 GLY   A O   1 
ATOM   1181 N N   . SER   A 1 162 ? 15.74056  -22.41873 -23.61264 1.000 20.77390 ? 169 SER   A N   1 
ATOM   1182 C CA  . SER   A 1 162 ? 15.27961  -22.53509 -24.99404 1.000 22.10875 ? 169 SER   A CA  1 
ATOM   1183 C C   . SER   A 1 162 ? 13.76034  -22.49006 -25.06717 1.000 22.50218 ? 169 SER   A C   1 
ATOM   1184 O O   . SER   A 1 162 ? 13.05372  -22.76155 -24.09619 1.000 19.12918 ? 169 SER   A O   1 
ATOM   1185 C CB  . SER   A 1 162 ? 15.81183  -23.81916 -25.64074 1.000 22.08452 ? 169 SER   A CB  1 
ATOM   1186 O OG  . SER   A 1 162 ? 15.21582  -24.98009 -25.07528 1.000 23.01239 ? 169 SER   A OG  1 
ATOM   1187 N N   . PHE   A 1 163 ? 13.26744  -22.15431 -26.25691 1.000 19.17457 ? 170 PHE   A N   1 
ATOM   1188 C CA  . PHE   A 1 163 ? 11.84661  -22.14867 -26.54061 1.000 18.95867 ? 170 PHE   A CA  1 
ATOM   1189 C C   . PHE   A 1 163 ? 11.67199  -22.63318 -27.96848 1.000 19.75893 ? 170 PHE   A C   1 
ATOM   1190 O O   . PHE   A 1 163 ? 12.64083  -22.70136 -28.73199 1.000 20.71405 ? 170 PHE   A O   1 
ATOM   1191 C CB  . PHE   A 1 163 ? 11.20411  -20.74828 -26.36348 1.000 17.67786 ? 170 PHE   A CB  1 
ATOM   1192 C CG  . PHE   A 1 163 ? 11.74315  -19.68004 -27.28956 1.000 17.80167 ? 170 PHE   A CG  1 
ATOM   1193 C CD1 . PHE   A 1 163 ? 12.87707  -18.96060 -26.94678 1.000 19.50115 ? 170 PHE   A CD1 1 
ATOM   1194 C CD2 . PHE   A 1 163 ? 11.06426  -19.34121 -28.45753 1.000 17.69778 ? 170 PHE   A CD2 1 
ATOM   1195 C CE1 . PHE   A 1 163 ? 13.38004  -17.94921 -27.74889 1.000 19.82112 ? 170 PHE   A CE1 1 
ATOM   1196 C CE2 . PHE   A 1 163 ? 11.56253  -18.31652 -29.30144 1.000 19.13720 ? 170 PHE   A CE2 1 
ATOM   1197 C CZ  . PHE   A 1 163 ? 12.71696  -17.60451 -28.93636 1.000 18.37284 ? 170 PHE   A CZ  1 
ATOM   1198 N N   . THR   A 1 164 ? 10.44054  -23.01687 -28.30550 1.000 18.76528 ? 171 THR   A N   1 
ATOM   1199 C CA  . THR   A 1 164 ? 10.13240  -23.49951 -29.64836 1.000 19.41376 ? 171 THR   A CA  1 
ATOM   1200 C C   . THR   A 1 164 ? 8.99806   -22.67982 -30.22782 1.000 22.42849 ? 171 THR   A C   1 
ATOM   1201 O O   . THR   A 1 164 ? 8.14871   -22.16169 -29.50137 1.000 18.19913 ? 171 THR   A O   1 
ATOM   1202 C CB  . THR   A 1 164 ? 9.74725   -24.97820 -29.65383 1.000 23.00094 ? 171 THR   A CB  1 
ATOM   1203 O OG1 . THR   A 1 164 ? 8.51369   -25.17688 -28.92948 1.000 21.01807 ? 171 THR   A OG1 1 
ATOM   1204 C CG2 . THR   A 1 164 ? 10.86568  -25.80674 -29.03670 1.000 22.24577 ? 171 THR   A CG2 1 
ATOM   1205 N N   . VAL   A 1 165 ? 8.98436   -22.57064 -31.55256 1.000 19.55346 ? 172 VAL   A N   1 
ATOM   1206 C CA  . VAL   A 1 165 ? 7.88058   -21.93589 -32.24634 1.000 19.44332 ? 172 VAL   A CA  1 
ATOM   1207 C C   . VAL   A 1 165 ? 7.49909   -22.85293 -33.40411 1.000 23.93291 ? 172 VAL   A C   1 
ATOM   1208 O O   . VAL   A 1 165 ? 8.37492   -23.36322 -34.11444 1.000 21.53233 ? 172 VAL   A O   1 
ATOM   1209 C CB  . VAL   A 1 165 ? 8.24667   -20.51594 -32.74716 1.000 19.58108 ? 172 VAL   A CB  1 
ATOM   1210 C CG1 . VAL   A 1 165 ? 7.16302   -19.99107 -33.66378 1.000 19.63417 ? 172 VAL   A CG1 1 
ATOM   1211 C CG2 . VAL   A 1 165 ? 8.47890   -19.56068 -31.56515 1.000 18.18551 ? 172 VAL   A CG2 1 
ATOM   1212 N N   . ARG   A 1 166 ? 6.20480   -23.11897 -33.54501 1.000 20.86083 ? 173 ARG   A N   1 
ATOM   1213 C CA  . ARG   A 1 166 ? 5.71241   -23.90810 -34.66765 1.000 24.80384 ? 173 ARG   A CA  1 
ATOM   1214 C C   . ARG   A 1 166 ? 4.39272   -23.33272 -35.14911 1.000 25.77784 ? 173 ARG   A C   1 
ATOM   1215 O O   . ARG   A 1 166 ? 3.71504   -22.58023 -34.44344 1.000 21.44519 ? 173 ARG   A O   1 
ATOM   1216 C CB  . ARG   A 1 166 ? 5.55080   -25.38755 -34.26823 1.000 26.30974 ? 173 ARG   A CB  1 
ATOM   1217 C CG  . ARG   A 1 166 ? 4.33908   -25.65723 -33.35315 1.000 33.36664 ? 173 ARG   A CG  1 
ATOM   1218 C CD  . ARG   A 1 166 ? 4.41493   -27.05730 -32.71927 1.000 37.24410 ? 173 ARG   A CD  1 
ATOM   1219 N NE  . ARG   A 1 166 ? 5.44438   -27.06093 -31.67574 1.000 47.52105 ? 173 ARG   A NE  1 
ATOM   1220 C CZ  . ARG   A 1 166 ? 5.92464   -28.14314 -31.06701 1.000 55.18288 ? 173 ARG   A CZ  1 
ATOM   1221 N NH1 . ARG   A 1 166 ? 5.50261   -29.35933 -31.37237 1.000 41.19776 ? 173 ARG   A NH1 1 
ATOM   1222 N NH2 . ARG   A 1 166 ? 6.87403   -28.00355 -30.14411 1.000 48.19182 ? 173 ARG   A NH2 1 
ATOM   1223 N N   . THR   A 1 167 ? 4.04307   -23.68578 -36.38039 1.000 26.02250 ? 174 THR   A N   1 
ATOM   1224 C CA  . THR   A 1 167 ? 2.72406   -23.37118 -36.88727 1.000 24.39228 ? 174 THR   A CA  1 
ATOM   1225 C C   . THR   A 1 167 ? 1.72003   -24.20379 -36.10898 1.000 35.65786 ? 174 THR   A C   1 
ATOM   1226 O O   . THR   A 1 167 ? 1.96188   -25.38450 -35.85839 1.000 31.91760 ? 174 THR   A O   1 
ATOM   1227 C CB  . THR   A 1 167 ? 2.68058   -23.69179 -38.38882 1.000 30.37237 ? 174 THR   A CB  1 
ATOM   1228 O OG1 . THR   A 1 167 ? 3.27238   -22.59598 -39.09245 1.000 36.07729 ? 174 THR   A OG1 1 
ATOM   1229 C CG2 . THR   A 1 167 ? 1.25814   -23.86600 -38.86523 1.000 53.94416 ? 174 THR   A CG2 1 
ATOM   1230 N N   . ASP   A 1 168 ? 0.62298   -23.59405 -35.66372 1.000 29.24555 ? 175 ASP   A N   1 
ATOM   1231 C CA  . ASP   A 1 168 ? -0.36508  -24.33906 -34.89041 1.000 27.91183 ? 175 ASP   A CA  1 
ATOM   1232 C C   . ASP   A 1 168 ? -1.41955  -24.93999 -35.81450 1.000 51.15292 ? 175 ASP   A C   1 
ATOM   1233 O O   . ASP   A 1 168 ? -1.96502  -24.24926 -36.68166 1.000 46.27570 ? 175 ASP   A O   1 
ATOM   1234 C CB  . ASP   A 1 168 ? -1.04481  -23.46613 -33.83095 1.000 27.05455 ? 175 ASP   A CB  1 
ATOM   1235 C CG  . ASP   A 1 168 ? -1.93213  -24.28666 -32.92170 1.000 37.57729 ? 175 ASP   A CG  1 
ATOM   1236 O OD1 . ASP   A 1 168 ? -1.50590  -25.39185 -32.54698 1.000 50.99885 ? 175 ASP   A OD1 1 
ATOM   1237 O OD2 . ASP   A 1 168 ? -3.06326  -23.86626 -32.62464 1.000 41.12374 ? 175 ASP   A OD2 1 
ATOM   1238 N N   . THR   A 1 169 ? -1.69897  -26.22892 -35.61915 1.000 53.94217 ? 176 THR   A N   1 
ATOM   1239 C CA  . THR   A 1 169 ? -2.73801  -26.94073 -36.35178 1.000 75.20788 ? 176 THR   A CA  1 
ATOM   1240 C C   . THR   A 1 169 ? -3.94667  -27.30539 -35.49507 1.000 70.25006 ? 176 THR   A C   1 
ATOM   1241 O O   . THR   A 1 169 ? -4.84236  -28.00013 -35.98364 1.000 63.84645 ? 176 THR   A O   1 
ATOM   1242 C CB  . THR   A 1 169 ? -2.15130  -28.20246 -37.00897 1.000 72.31641 ? 176 THR   A CB  1 
ATOM   1243 O OG1 . THR   A 1 169 ? -1.49976  -29.01486 -36.01488 1.000 62.92635 ? 176 THR   A OG1 1 
ATOM   1244 C CG2 . THR   A 1 169 ? -1.18574  -27.83125 -38.14120 1.000 46.39938 ? 176 THR   A CG2 1 
ATOM   1245 N N   . GLY   A 1 170 ? -4.01279  -26.84396 -34.24618 1.000 56.79311 ? 177 GLY   A N   1 
ATOM   1246 C CA  . GLY   A 1 170 ? -5.20248  -27.04955 -33.43812 1.000 50.42780 ? 177 GLY   A CA  1 
ATOM   1247 C C   . GLY   A 1 170 ? -6.40019  -26.25223 -33.92089 1.000 60.35206 ? 177 GLY   A C   1 
ATOM   1248 O O   . GLY   A 1 170 ? -6.41601  -25.77667 -35.06317 1.000 48.02321 ? 177 GLY   A O   1 
ATOM   1249 N N   . GLU   A 1 171 ? -7.40936  -26.10931 -33.06057 1.000 57.24468 ? 178 GLU   A N   1 
ATOM   1250 C CA  . GLU   A 1 171 ? -8.59605  -25.33274 -33.39361 1.000 63.48421 ? 178 GLU   A CA  1 
ATOM   1251 C C   . GLU   A 1 171 ? -8.20243  -23.91624 -33.81594 1.000 44.82500 ? 178 GLU   A C   1 
ATOM   1252 O O   . GLU   A 1 171 ? -7.40683  -23.26576 -33.11869 1.000 38.24288 ? 178 GLU   A O   1 
ATOM   1253 C CB  . GLU   A 1 171 ? -9.54375  -25.27128 -32.18764 1.000 66.95754 ? 178 GLU   A CB  1 
ATOM   1254 C CG  . GLU   A 1 171 ? -11.01990 -24.89653 -32.46689 1.000 71.02830 ? 178 GLU   A CG  1 
ATOM   1255 C CD  . GLU   A 1 171 ? -11.83298 -25.97963 -33.19025 1.000 95.08917 ? 178 GLU   A CD  1 
ATOM   1256 O OE1 . GLU   A 1 171 ? -11.23506 -26.97074 -33.67215 1.000 89.64542 ? 178 GLU   A OE1 1 
ATOM   1257 O OE2 . GLU   A 1 171 ? -13.08535 -25.84469 -33.25779 1.000 73.01507 ? 178 GLU   A OE2 1 
ATOM   1258 N N   . PRO   A 1 172 ? -8.71327  -23.41557 -34.94436 1.000 47.77363 ? 179 PRO   A N   1 
ATOM   1259 C CA  . PRO   A 1 172 ? -8.51478  -22.00296 -35.28985 1.000 44.64073 ? 179 PRO   A CA  1 
ATOM   1260 C C   . PRO   A 1 172 ? -9.08987  -21.09606 -34.21184 1.000 48.66617 ? 179 PRO   A C   1 
ATOM   1261 O O   . PRO   A 1 172 ? -10.12177 -21.39549 -33.61095 1.000 46.80884 ? 179 PRO   A O   1 
ATOM   1262 C CB  . PRO   A 1 172 ? -9.27404  -21.83586 -36.60907 1.000 40.97529 ? 179 PRO   A CB  1 
ATOM   1263 C CG  . PRO   A 1 172 ? -9.65637  -23.19192 -37.06036 1.000 45.63604 ? 179 PRO   A CG  1 
ATOM   1264 C CD  . PRO   A 1 172 ? -9.23954  -24.21622 -36.06651 1.000 43.65127 ? 179 PRO   A CD  1 
ATOM   1265 N N   . MET   A 1 173 ? -8.42295  -19.95428 -34.00361 1.000 34.76598 ? 180 MET   A N   1 
ATOM   1266 C CA  . MET   A 1 173 ? -8.64168  -19.10962 -32.84561 1.000 38.71463 ? 180 MET   A CA  1 
ATOM   1267 C C   . MET   A 1 173 ? -9.33692  -17.79761 -33.18108 1.000 38.00629 ? 180 MET   A C   1 
ATOM   1268 O O   . MET   A 1 173 ? -9.79835  -17.10439 -32.26549 1.000 52.78414 ? 180 MET   A O   1 
ATOM   1269 C CB  . MET   A 1 173 ? -7.27534  -18.81827 -32.21543 1.000 30.35928 ? 180 MET   A CB  1 
ATOM   1270 C CG  . MET   A 1 173 ? -7.00394  -19.46843 -30.90488 1.000 51.25328 ? 180 MET   A CG  1 
ATOM   1271 S SD  . MET   A 1 173 ? -5.51527  -18.67964 -30.29486 1.000 44.57524 ? 180 MET   A SD  1 
ATOM   1272 C CE  . MET   A 1 173 ? -6.20014  -17.15172 -29.67083 1.000 26.99596 ? 180 MET   A CE  1 
ATOM   1273 N N   . GLY   A 1 174 ? -9.39107  -17.42546 -34.45515 1.000 35.59049 ? 181 GLY   A N   1 
ATOM   1274 C CA  . GLY   A 1 174 ? -9.97666  -16.15776 -34.85067 1.000 31.89237 ? 181 GLY   A CA  1 
ATOM   1275 C C   . GLY   A 1 174 ? -8.95529  -15.04117 -34.75966 1.000 24.80754 ? 181 GLY   A C   1 
ATOM   1276 O O   . GLY   A 1 174 ? -8.39398  -14.60260 -35.76749 1.000 28.96125 ? 181 GLY   A O   1 
ATOM   1277 N N   . ARG   A 1 175 ? -8.64876  -14.64196 -33.53365 1.000 23.34452 ? 182 ARG   A N   1 
ATOM   1278 C CA  . ARG   A 1 175 ? -7.66734  -13.60503 -33.25184 1.000 22.08091 ? 182 ARG   A CA  1 
ATOM   1279 C C   . ARG   A 1 175 ? -7.49180  -13.59479 -31.74705 1.000 20.83112 ? 182 ARG   A C   1 
ATOM   1280 O O   . ARG   A 1 175 ? -8.48632  -13.71063 -31.02003 1.000 21.71956 ? 182 ARG   A O   1 
ATOM   1281 C CB  . ARG   A 1 175 ? -8.12275  -12.21424 -33.73657 1.000 22.59858 ? 182 ARG   A CB  1 
ATOM   1282 C CG  . ARG   A 1 175 ? -7.11456  -11.08047 -33.45369 1.000 21.56349 ? 182 ARG   A CG  1 
ATOM   1283 C CD  . ARG   A 1 175 ? -7.77929  -9.68087  -33.46878 1.000 22.06259 ? 182 ARG   A CD  1 
ATOM   1284 N NE  . ARG   A 1 175 ? -8.75168  -9.50650  -32.39385 1.000 22.29285 ? 182 ARG   A NE  1 
ATOM   1285 C CZ  . ARG   A 1 175 ? -10.07161 -9.52682  -32.55044 1.000 23.13784 ? 182 ARG   A CZ  1 
ATOM   1286 N NH1 . ARG   A 1 175 ? -10.62748 -9.64781  -33.74757 1.000 24.55367 ? 182 ARG   A NH1 1 
ATOM   1287 N NH2 . ARG   A 1 175 ? -10.85586 -9.40977  -31.47890 1.000 23.04990 ? 182 ARG   A NH2 1 
ATOM   1288 N N   . GLY   A 1 176 ? -6.24952  -13.48292 -31.28989 1.000 19.66240 ? 183 GLY   A N   1 
ATOM   1289 C CA  . GLY   A 1 176 ? -5.98375  -13.28708 -29.87377 1.000 18.62703 ? 183 GLY   A CA  1 
ATOM   1290 C C   . GLY   A 1 176 ? -4.88083  -14.19932 -29.37686 1.000 22.56434 ? 183 GLY   A C   1 
ATOM   1291 O O   . GLY   A 1 176 ? -4.04428  -14.68161 -30.14571 1.000 21.24840 ? 183 GLY   A O   1 
ATOM   1292 N N   . THR   A 1 177 ? -4.87659  -14.45920 -28.06965 1.000 17.29576 ? 184 THR   A N   1 
ATOM   1293 C CA  . THR   A 1 177 ? -3.78923  -15.21245 -27.46010 1.000 16.65478 ? 184 THR   A CA  1 
ATOM   1294 C C   . THR   A 1 177 ? -4.37687  -16.11755 -26.39327 1.000 18.77157 ? 184 THR   A C   1 
ATOM   1295 O O   . THR   A 1 177 ? -5.31689  -15.72521 -25.68636 1.000 19.41355 ? 184 THR   A O   1 
ATOM   1296 C CB  . THR   A 1 177 ? -2.73683  -14.27915 -26.83899 1.000 18.59150 ? 184 THR   A CB  1 
ATOM   1297 O OG1 . THR   A 1 177 ? -2.11270  -13.50063 -27.86143 1.000 19.18980 ? 184 THR   A OG1 1 
ATOM   1298 C CG2 . THR   A 1 177 ? -1.65429  -15.07538 -26.06703 1.000 15.93576 ? 184 THR   A CG2 1 
ATOM   1299 N N   . LYS   A 1 178 ? -3.84176  -17.33653 -26.31443 1.000 17.36737 ? 185 LYS   A N   1 
ATOM   1300 C CA  . LYS   A 1 178 ? -4.21582  -18.30651 -25.30214 1.000 17.45303 ? 185 LYS   A CA  1 
ATOM   1301 C C   . LYS   A 1 178 ? -2.93996  -18.73914 -24.58908 1.000 20.51401 ? 185 LYS   A C   1 
ATOM   1302 O O   . LYS   A 1 178 ? -2.01758  -19.25563 -25.22337 1.000 18.94267 ? 185 LYS   A O   1 
ATOM   1303 C CB  . LYS   A 1 178 ? -4.98030  -19.46827 -25.94759 1.000 20.17092 ? 185 LYS   A CB  1 
ATOM   1304 C CG  . LYS   A 1 178 ? -5.07235  -20.72357 -25.14444 1.000 34.87221 ? 185 LYS   A CG  1 
ATOM   1305 C CD  . LYS   A 1 178 ? -6.15889  -21.65300 -25.73218 1.000 41.22785 ? 185 LYS   A CD  1 
ATOM   1306 C CE  . LYS   A 1 178 ? -6.10636  -21.80389 -27.23061 1.000 44.90873 ? 185 LYS   A CE  1 
ATOM   1307 N NZ  . LYS   A 1 178 ? -6.91591  -23.01164 -27.63302 1.000 49.02591 ? 185 LYS   A NZ  1 
ATOM   1308 N N   . VAL   A 1 179 ? -2.84451  -18.44455 -23.29134 1.000 18.04145 ? 186 VAL   A N   1 
ATOM   1309 C CA  . VAL   A 1 179 ? -1.68353  -18.82692 -22.49252 1.000 17.19710 ? 186 VAL   A CA  1 
ATOM   1310 C C   . VAL   A 1 179 ? -2.05586  -20.06090 -21.67794 1.000 19.68790 ? 186 VAL   A C   1 
ATOM   1311 O O   . VAL   A 1 179 ? -2.94131  -19.99587 -20.81977 1.000 20.93494 ? 186 VAL   A O   1 
ATOM   1312 C CB  . VAL   A 1 179 ? -1.22036  -17.67693 -21.58408 1.000 15.23720 ? 186 VAL   A CB  1 
ATOM   1313 C CG1 . VAL   A 1 179 ? -0.06377  -18.16392 -20.70055 1.000 16.06478 ? 186 VAL   A CG1 1 
ATOM   1314 C CG2 . VAL   A 1 179 ? -0.77860  -16.52108 -22.44615 1.000 16.46571 ? 186 VAL   A CG2 1 
ATOM   1315 N N   . ILE   A 1 180 ? -1.38470  -21.18548 -21.93325 1.000 17.57996 ? 187 ILE   A N   1 
ATOM   1316 C CA  . ILE   A 1 180 ? -1.68057  -22.44944 -21.26962 1.000 17.40526 ? 187 ILE   A CA  1 
ATOM   1317 C C   . ILE   A 1 180 ? -0.58148  -22.68852 -20.24377 1.000 19.13507 ? 187 ILE   A C   1 
ATOM   1318 O O   . ILE   A 1 180 ? 0.57528   -22.92610 -20.61097 1.000 19.43644 ? 187 ILE   A O   1 
ATOM   1319 C CB  . ILE   A 1 180 ? -1.77502  -23.61047 -22.26378 1.000 19.56085 ? 187 ILE   A CB  1 
ATOM   1320 C CG1 . ILE   A 1 180 ? -2.78748  -23.29181 -23.35723 1.000 22.68927 ? 187 ILE   A CG1 1 
ATOM   1321 C CG2 . ILE   A 1 180 ? -2.15878  -24.93713 -21.55644 1.000 20.81895 ? 187 ILE   A CG2 1 
ATOM   1322 C CD1 . ILE   A 1 180 ? -2.57692  -24.12098 -24.58675 1.000 28.27902 ? 187 ILE   A CD1 1 
ATOM   1323 N N   . LEU   A 1 181 ? -0.94082  -22.63820 -18.95590 1.000 17.43020 ? 188 LEU   A N   1 
ATOM   1324 C CA  . LEU   A 1 181 ? 0.00919   -22.80840 -17.87088 1.000 21.54640 ? 188 LEU   A CA  1 
ATOM   1325 C C   . LEU   A 1 181 ? -0.05452  -24.26019 -17.42503 1.000 19.51688 ? 188 LEU   A C   1 
ATOM   1326 O O   . LEU   A 1 181 ? -1.06586  -24.68745 -16.86965 1.000 19.17273 ? 188 LEU   A O   1 
ATOM   1327 C CB  . LEU   A 1 181 ? -0.33350  -21.86859 -16.71207 1.000 17.38403 ? 188 LEU   A CB  1 
ATOM   1328 C CG  . LEU   A 1 181 ? -0.39858  -20.38588 -17.09448 1.000 18.66215 ? 188 LEU   A CG  1 
ATOM   1329 C CD1 . LEU   A 1 181 ? -0.94611  -19.56944 -15.89140 1.000 20.81984 ? 188 LEU   A CD1 1 
ATOM   1330 C CD2 . LEU   A 1 181 ? 0.98041   -19.91480 -17.52218 1.000 21.22516 ? 188 LEU   A CD2 1 
ATOM   1331 N N   . HIS   A 1 182 ? 1.00809   -25.02872 -17.67596 1.000 19.96980 ? 189 HIS   A N   1 
ATOM   1332 C CA  . HIS   A 1 182 ? 1.10737   -26.39572 -17.16092 1.000 22.84703 ? 189 HIS   A CA  1 
ATOM   1333 C C   . HIS   A 1 182 ? 1.66869   -26.28893 -15.74124 1.000 24.64988 ? 189 HIS   A C   1 
ATOM   1334 O O   . HIS   A 1 182 ? 2.87429   -26.08707 -15.55105 1.000 20.02503 ? 189 HIS   A O   1 
ATOM   1335 C CB  . HIS   A 1 182 ? 1.97973   -27.26374 -18.07178 1.000 20.17715 ? 189 HIS   A CB  1 
ATOM   1336 C CG  . HIS   A 1 182 ? 1.54969   -27.24331 -19.52260 1.000 20.86078 ? 189 HIS   A CG  1 
ATOM   1337 N ND1 . HIS   A 1 182 ? 0.78031   -28.23184 -20.09784 1.000 29.87229 ? 189 HIS   A ND1 1 
ATOM   1338 C CD2 . HIS   A 1 182 ? 1.76326   -26.32147 -20.49703 1.000 27.95014 ? 189 HIS   A CD2 1 
ATOM   1339 C CE1 . HIS   A 1 182 ? 0.55668   -27.93184 -21.37110 1.000 27.21348 ? 189 HIS   A CE1 1 
ATOM   1340 N NE2 . HIS   A 1 182 ? 1.13520   -26.77232 -21.63414 1.000 29.96243 ? 189 HIS   A NE2 1 
ATOM   1341 N N   . LEU   A 1 183 ? 0.79822   -26.43969 -14.73910 1.000 20.71935 ? 190 LEU   A N   1 
ATOM   1342 C CA  . LEU   A 1 183 ? 1.15760   -26.03191 -13.38766 1.000 20.98138 ? 190 LEU   A CA  1 
ATOM   1343 C C   . LEU   A 1 183 ? 2.10805   -27.03501 -12.73479 1.000 25.43188 ? 190 LEU   A C   1 
ATOM   1344 O O   . LEU   A 1 183 ? 2.04365   -28.24603 -12.97427 1.000 24.48142 ? 190 LEU   A O   1 
ATOM   1345 C CB  . LEU   A 1 183 ? -0.09728  -25.89726 -12.52857 1.000 21.52990 ? 190 LEU   A CB  1 
ATOM   1346 C CG  . LEU   A 1 183 ? -1.08994  -24.81752 -12.94595 1.000 20.78054 ? 190 LEU   A CG  1 
ATOM   1347 C CD1 . LEU   A 1 183 ? -2.22291  -24.74587 -11.93097 1.000 21.73682 ? 190 LEU   A CD1 1 
ATOM   1348 C CD2 . LEU   A 1 183 ? -0.42431  -23.42670 -13.10033 1.000 19.71140 ? 190 LEU   A CD2 1 
ATOM   1349 N N   . LYS   A 1 184 ? 2.99517   -26.51560 -11.89585 1.000 26.04401 ? 191 LYS   A N   1 
ATOM   1350 C CA  . LYS   A 1 184 ? 3.80442   -27.36589 -11.03200 1.000 30.44981 ? 191 LYS   A CA  1 
ATOM   1351 C C   . LYS   A 1 184 ? 2.89487   -28.17910 -10.11016 1.000 28.92947 ? 191 LYS   A C   1 
ATOM   1352 O O   . LYS   A 1 184 ? 1.77985   -27.76154 -9.76463  1.000 27.07542 ? 191 LYS   A O   1 
ATOM   1353 C CB  . LYS   A 1 184 ? 4.75045   -26.50505 -10.19067 1.000 31.20346 ? 191 LYS   A CB  1 
ATOM   1354 C CG  . LYS   A 1 184 ? 5.88443   -25.80933 -10.97395 1.000 27.30982 ? 191 LYS   A CG  1 
ATOM   1355 C CD  . LYS   A 1 184 ? 6.56884   -24.72977 -10.10375 1.000 37.46268 ? 191 LYS   A CD  1 
ATOM   1356 C CE  . LYS   A 1 184 ? 7.23093   -23.64207 -10.94642 1.000 40.54394 ? 191 LYS   A CE  1 
ATOM   1357 N NZ  . LYS   A 1 184 ? 8.01590   -22.60878 -10.16651 1.000 35.26181 ? 191 LYS   A NZ  1 
ATOM   1358 N N   . GLU   A 1 185 ? 3.41495   -29.32125 -9.64465  1.000 30.59044 ? 192 GLU   A N   1 
ATOM   1359 C CA  . GLU   A 1 185 ? 2.59553   -30.22491 -8.84153  1.000 31.93827 ? 192 GLU   A CA  1 
ATOM   1360 C C   . GLU   A 1 185 ? 2.08910   -29.57211 -7.55658  1.000 33.80770 ? 192 GLU   A C   1 
ATOM   1361 O O   . GLU   A 1 185 ? 0.98893   -29.88963 -7.09126  1.000 31.19299 ? 192 GLU   A O   1 
ATOM   1362 C CB  . GLU   A 1 185 ? 3.38048   -31.50175 -8.51063  1.000 34.99787 ? 192 GLU   A CB  1 
ATOM   1363 C CG  . GLU   A 1 185 ? 2.50284   -32.73797 -8.60623  1.000 65.08210 ? 192 GLU   A CG  1 
ATOM   1364 C CD  . GLU   A 1 185 ? 3.22063   -34.03518 -8.25486  1.000 79.17114 ? 192 GLU   A CD  1 
ATOM   1365 O OE1 . GLU   A 1 185 ? 2.52338   -35.06941 -8.11729  1.000 73.58334 ? 192 GLU   A OE1 1 
ATOM   1366 O OE2 . GLU   A 1 185 ? 4.46742   -34.02224 -8.14031  1.000 72.67701 ? 192 GLU   A OE2 1 
ATOM   1367 N N   . ASP   A 1 186 ? 2.86112   -28.67718 -6.96011  1.000 29.88261 ? 193 ASP   A N   1 
ATOM   1368 C CA  . ASP   A 1 186 ? 2.43752   -28.07470 -5.70413  1.000 36.66698 ? 193 ASP   A CA  1 
ATOM   1369 C C   . ASP   A 1 186 ? 1.68766   -26.76493 -5.89701  1.000 33.34856 ? 193 ASP   A C   1 
ATOM   1370 O O   . ASP   A 1 186 ? 1.39395   -26.07899 -4.90919  1.000 29.81950 ? 193 ASP   A O   1 
ATOM   1371 C CB  . ASP   A 1 186 ? 3.63913   -27.87396 -4.76966  1.000 32.00095 ? 193 ASP   A CB  1 
ATOM   1372 C CG  . ASP   A 1 186 ? 4.69848   -26.95233 -5.33721  1.000 43.29549 ? 193 ASP   A CG  1 
ATOM   1373 O OD1 . ASP   A 1 186 ? 4.68546   -26.64922 -6.55370  1.000 44.24577 ? 193 ASP   A OD1 1 
ATOM   1374 O OD2 . ASP   A 1 186 ? 5.56618   -26.53227 -4.54666  1.000 61.64259 ? 193 ASP   A OD2 1 
ATOM   1375 N N   . GLN   A 1 187 ? 1.31282   -26.42023 -7.13202  1.000 25.48850 ? 194 GLN   A N   1 
ATOM   1376 C CA  . GLN   A 1 187 ? 0.62399   -25.16560 -7.37800  1.000 25.12427 ? 194 GLN   A CA  1 
ATOM   1377 C C   . GLN   A 1 187 ? -0.80456  -25.37862 -7.88824  1.000 23.07234 ? 194 GLN   A C   1 
ATOM   1378 O O   . GLN   A 1 187 ? -1.34688  -24.52646 -8.59556  1.000 22.91610 ? 194 GLN   A O   1 
ATOM   1379 C CB  . GLN   A 1 187 ? 1.45330   -24.31276 -8.34362  1.000 23.20413 ? 194 GLN   A CB  1 
ATOM   1380 C CG  . GLN   A 1 187 ? 2.89089   -24.11031 -7.84340  1.000 23.28687 ? 194 GLN   A CG  1 
ATOM   1381 C CD  . GLN   A 1 187 ? 2.94652   -23.32575 -6.51955  1.000 28.85759 ? 194 GLN   A CD  1 
ATOM   1382 O OE1 . GLN   A 1 187 ? 2.09003   -22.49419 -6.25349  1.000 25.30366 ? 194 GLN   A OE1 1 
ATOM   1383 N NE2 . GLN   A 1 187 ? 3.96212   -23.57727 -5.71637  1.000 24.68980 ? 194 GLN   A NE2 1 
ATOM   1384 N N   . THR   A 1 188 ? -1.44942  -26.49135 -7.51760  1.000 25.84828 ? 195 THR   A N   1 
ATOM   1385 C CA  . THR   A 1 188 ? -2.79425  -26.73437 -8.04134  1.000 26.39122 ? 195 THR   A CA  1 
ATOM   1386 C C   . THR   A 1 188 ? -3.86781  -25.90091 -7.34779  1.000 25.17111 ? 195 THR   A C   1 
ATOM   1387 O O   . THR   A 1 188 ? -5.02877  -25.96288 -7.75867  1.000 24.16453 ? 195 THR   A O   1 
ATOM   1388 C CB  . THR   A 1 188 ? -3.17386  -28.20668 -7.93618  1.000 33.56417 ? 195 THR   A CB  1 
ATOM   1389 O OG1 . THR   A 1 188 ? -3.12350  -28.61773 -6.55665  1.000 34.53189 ? 195 THR   A OG1 1 
ATOM   1390 C CG2 . THR   A 1 188 ? -2.19630  -29.06031 -8.75796  1.000 39.72935 ? 195 THR   A CG2 1 
ATOM   1391 N N   . GLU   A 1 189 ? -3.52138  -25.10497 -6.32942  1.000 23.18884 ? 196 GLU   A N   1 
ATOM   1392 C CA  . GLU   A 1 189 ? -4.52194  -24.18844 -5.78488  1.000 25.05251 ? 196 GLU   A CA  1 
ATOM   1393 C C   . GLU   A 1 189 ? -5.04818  -23.22882 -6.84786  1.000 20.86154 ? 196 GLU   A C   1 
ATOM   1394 O O   . GLU   A 1 189 ? -6.17763  -22.75069 -6.74484  1.000 23.21081 ? 196 GLU   A O   1 
ATOM   1395 C CB  . GLU   A 1 189 ? -3.93235  -23.40366 -4.61861  1.000 26.61545 ? 196 GLU   A CB  1 
ATOM   1396 C CG  . GLU   A 1 189 ? -2.84476  -22.42150 -5.05041  1.000 21.48099 ? 196 GLU   A CG  1 
ATOM   1397 C CD  . GLU   A 1 189 ? -2.23917  -21.70161 -3.84315  1.000 37.86774 ? 196 GLU   A CD  1 
ATOM   1398 O OE1 . GLU   A 1 189 ? -1.30072  -22.27673 -3.25764  1.000 33.80303 ? 196 GLU   A OE1 1 
ATOM   1399 O OE2 . GLU   A 1 189 ? -2.73602  -20.62369 -3.43648  1.000 26.36785 ? 196 GLU   A OE2 1 
ATOM   1400 N N   . TYR   A 1 190 ? -4.25613  -22.91696 -7.86545  1.000 20.00368 ? 197 TYR   A N   1 
ATOM   1401 C CA  . TYR   A 1 190 ? -4.70997  -21.99316 -8.89596  1.000 20.89354 ? 197 TYR   A CA  1 
ATOM   1402 C C   . TYR   A 1 190 ? -5.66132  -22.65225 -9.89645  1.000 25.18020 ? 197 TYR   A C   1 
ATOM   1403 O O   . TYR   A 1 190 ? -6.01000  -22.04234 -10.90869 1.000 23.27947 ? 197 TYR   A O   1 
ATOM   1404 C CB  . TYR   A 1 190 ? -3.48980  -21.36707 -9.59379  1.000 18.18736 ? 197 TYR   A CB  1 
ATOM   1405 C CG  . TYR   A 1 190 ? -2.62439  -20.67722 -8.54037  1.000 17.85108 ? 197 TYR   A CG  1 
ATOM   1406 C CD1 . TYR   A 1 190 ? -3.07754  -19.52135 -7.91097  1.000 20.28157 ? 197 TYR   A CD1 1 
ATOM   1407 C CD2 . TYR   A 1 190 ? -1.43245  -21.22737 -8.11906  1.000 22.65672 ? 197 TYR   A CD2 1 
ATOM   1408 C CE1 . TYR   A 1 190 ? -2.32595  -18.90021 -6.93020  1.000 21.40370 ? 197 TYR   A CE1 1 
ATOM   1409 C CE2 . TYR   A 1 190 ? -0.67738  -20.63439 -7.12325  1.000 23.11777 ? 197 TYR   A CE2 1 
ATOM   1410 C CZ  . TYR   A 1 190 ? -1.13219  -19.46027 -6.54262  1.000 24.19486 ? 197 TYR   A CZ  1 
ATOM   1411 O OH  . TYR   A 1 190 ? -0.39967  -18.85535 -5.55470  1.000 21.64428 ? 197 TYR   A OH  1 
ATOM   1412 N N   . LEU   A 1 191 ? -6.09847  -23.87425 -9.63354  1.000 21.34145 ? 198 LEU   A N   1 
ATOM   1413 C CA  . LEU   A 1 191 ? -7.17197  -24.48919 -10.40243 1.000 22.70363 ? 198 LEU   A CA  1 
ATOM   1414 C C   . LEU   A 1 191 ? -8.49263  -24.45533 -9.65587  1.000 27.40263 ? 198 LEU   A C   1 
ATOM   1415 O O   . LEU   A 1 191 ? -9.49563  -24.93046 -10.18959 1.000 26.76240 ? 198 LEU   A O   1 
ATOM   1416 C CB  . LEU   A 1 191 ? -6.82514  -25.95299 -10.74107 1.000 24.72457 ? 198 LEU   A CB  1 
ATOM   1417 C CG  . LEU   A 1 191 ? -5.56670  -26.12852 -11.59367 1.000 32.47909 ? 198 LEU   A CG  1 
ATOM   1418 C CD1 . LEU   A 1 191 ? -5.36873  -27.56740 -11.94399 1.000 33.65873 ? 198 LEU   A CD1 1 
ATOM   1419 C CD2 . LEU   A 1 191 ? -5.70121  -25.31075 -12.83730 1.000 26.69755 ? 198 LEU   A CD2 1 
ATOM   1420 N N   . GLU   A 1 192 ? -8.50476  -23.95448 -8.41850  1.000 22.88505 ? 199 GLU   A N   1 
ATOM   1421 C CA  . GLU   A 1 192 ? -9.69729  -23.97644 -7.57801  1.000 27.30059 ? 199 GLU   A CA  1 
ATOM   1422 C C   . GLU   A 1 192 ? -10.50877 -22.72371 -7.85568  1.000 24.66751 ? 199 GLU   A C   1 
ATOM   1423 O O   . GLU   A 1 192 ? -9.96835  -21.61453 -7.83167  1.000 21.32528 ? 199 GLU   A O   1 
ATOM   1424 C CB  . GLU   A 1 192 ? -9.33081  -24.02680 -6.08682  1.000 27.87519 ? 199 GLU   A CB  1 
ATOM   1425 C CG  . GLU   A 1 192 ? -8.55105  -25.26153 -5.62740  1.000 29.74612 ? 199 GLU   A CG  1 
ATOM   1426 C CD  . GLU   A 1 192 ? -9.31838  -26.56797 -5.81897  1.000 68.05154 ? 199 GLU   A CD  1 
ATOM   1427 O OE1 . GLU   A 1 192 ? -10.57737 -26.52334 -5.84024  1.000 65.28768 ? 199 GLU   A OE1 1 
ATOM   1428 O OE2 . GLU   A 1 192 ? -8.66350  -27.63864 -5.92295  1.000 54.23507 ? 199 GLU   A OE2 1 
ATOM   1429 N N   . GLU   A 1 193 ? -11.80797 -22.90542 -8.07586  1.000 24.57201 ? 200 GLU   A N   1 
ATOM   1430 C CA  . GLU   A 1 193 ? -12.66215 -21.78040 -8.44106  1.000 24.27311 ? 200 GLU   A CA  1 
ATOM   1431 C C   . GLU   A 1 193 ? -12.58624 -20.65479 -7.40080  1.000 28.31324 ? 200 GLU   A C   1 
ATOM   1432 O O   . GLU   A 1 193 ? -12.46181 -19.47792 -7.75325  1.000 23.36970 ? 200 GLU   A O   1 
ATOM   1433 C CB  . GLU   A 1 193 ? -14.09633 -22.27726 -8.61049  1.000 31.57678 ? 200 GLU   A CB  1 
ATOM   1434 C CG  . GLU   A 1 193 ? -15.15992 -21.19029 -8.54824  1.000 46.60955 ? 200 GLU   A CG  1 
ATOM   1435 C CD  . GLU   A 1 193 ? -16.50792 -21.66579 -9.09331  1.000 63.17606 ? 200 GLU   A CD  1 
ATOM   1436 O OE1 . GLU   A 1 193 ? -16.78942 -22.89309 -9.04805  1.000 56.02621 ? 200 GLU   A OE1 1 
ATOM   1437 O OE2 . GLU   A 1 193 ? -17.26985 -20.81216 -9.60081  1.000 67.08778 ? 200 GLU   A OE2 1 
ATOM   1438 N N   . ARG   A 1 194 ? -12.65297 -20.98450 -6.10402  1.000 24.51702 ? 201 ARG   A N   1 
ATOM   1439 C CA  . ARG   A 1 194 ? -12.70511 -19.87473 -5.15278  1.000 23.39976 ? 201 ARG   A CA  1 
ATOM   1440 C C   . ARG   A 1 194 ? -11.35817 -19.15864 -5.03330  1.000 21.60685 ? 201 ARG   A C   1 
ATOM   1441 O O   . ARG   A 1 194 ? -11.32444 -17.95749 -4.73754  1.000 21.02877 ? 201 ARG   A O   1 
ATOM   1442 C CB  . ARG   A 1 194 ? -13.18559 -20.34434 -3.77822  1.000 34.95886 ? 201 ARG   A CB  1 
ATOM   1443 C CG  . ARG   A 1 194 ? -12.38854 -21.43728 -3.19138  1.000 44.03295 ? 201 ARG   A CG  1 
ATOM   1444 C CD  . ARG   A 1 194 ? -13.20498 -22.14996 -2.13265  1.000 54.39137 ? 201 ARG   A CD  1 
ATOM   1445 N NE  . ARG   A 1 194 ? -12.33398 -23.03119 -1.37035  1.000 69.44446 ? 201 ARG   A NE  1 
ATOM   1446 C CZ  . ARG   A 1 194 ? -12.54747 -23.38943 -0.11180  1.000 68.24079 ? 201 ARG   A CZ  1 
ATOM   1447 N NH1 . ARG   A 1 194 ? -13.64010 -23.00763 0.54212   1.000 47.16392 ? 201 ARG   A NH1 1 
ATOM   1448 N NH2 . ARG   A 1 194 ? -11.62360 -24.11268 0.51837   1.000 56.34858 ? 201 ARG   A NH2 1 
ATOM   1449 N N   . ARG   A 1 195 ? -10.24052 -19.86460 -5.25550  1.000 21.07562 ? 202 ARG   A N   1 
ATOM   1450 C CA  . ARG   A 1 195 ? -8.93211  -19.21521 -5.22330  1.000 19.74919 ? 202 ARG   A CA  1 
ATOM   1451 C C   . ARG   A 1 195 ? -8.79597  -18.25612 -6.38852  1.000 22.73893 ? 202 ARG   A C   1 
ATOM   1452 O O   . ARG   A 1 195 ? -8.30406  -17.13908 -6.23475  1.000 18.36629 ? 202 ARG   A O   1 
ATOM   1453 C CB  . ARG   A 1 195 ? -7.80120  -20.25920 -5.28044  1.000 21.89930 ? 202 ARG   A CB  1 
ATOM   1454 C CG  . ARG   A 1 195 ? -6.38454  -19.65025 -5.22864  1.000 19.74556 ? 202 ARG   A CG  1 
ATOM   1455 C CD  . ARG   A 1 195 ? -6.09282  -19.05802 -3.84165  1.000 26.70943 ? 202 ARG   A CD  1 
ATOM   1456 N NE  . ARG   A 1 195 ? -4.67485  -18.75342 -3.70209  1.000 19.54752 ? 202 ARG   A NE  1 
ATOM   1457 C CZ  . ARG   A 1 195 ? -4.18490  -17.53741 -3.51240  1.000 25.23083 ? 202 ARG   A CZ  1 
ATOM   1458 N NH1 . ARG   A 1 195 ? -4.97824  -16.49319 -3.34420  1.000 20.39460 ? 202 ARG   A NH1 1 
ATOM   1459 N NH2 . ARG   A 1 195 ? -2.86472  -17.36856 -3.47479  1.000 24.52650 ? 202 ARG   A NH2 1 
ATOM   1460 N N   . ILE   A 1 196 ? -9.23461  -18.68284 -7.56408  1.000 18.49753 ? 203 ILE   A N   1 
ATOM   1461 C CA  . ILE   A 1 196 ? -9.10829  -17.81711 -8.72686  1.000 18.73184 ? 203 ILE   A CA  1 
ATOM   1462 C C   . ILE   A 1 196 ? -9.96966  -16.57650 -8.55047  1.000 17.80750 ? 203 ILE   A C   1 
ATOM   1463 O O   . ILE   A 1 196 ? -9.52196  -15.46499 -8.83183  1.000 19.65819 ? 203 ILE   A O   1 
ATOM   1464 C CB  . ILE   A 1 196 ? -9.46466  -18.58746 -10.00095 1.000 18.28176 ? 203 ILE   A CB  1 
ATOM   1465 C CG1 . ILE   A 1 196 ? -8.46724  -19.71943 -10.21349 1.000 18.40915 ? 203 ILE   A CG1 1 
ATOM   1466 C CG2 . ILE   A 1 196 ? -9.41848  -17.67186 -11.21720 1.000 18.25366 ? 203 ILE   A CG2 1 
ATOM   1467 C CD1 . ILE   A 1 196 ? -8.97818  -20.74081 -11.29290 1.000 22.25075 ? 203 ILE   A CD1 1 
ATOM   1468 N N   . LYS   A 1 197 ? -11.20947 -16.74743 -8.07370  1.000 18.87159 ? 204 LYS   A N   1 
ATOM   1469 C CA  . LYS   A 1 197 ? -12.07835 -15.59230 -7.86007  1.000 21.70678 ? 204 LYS   A CA  1 
ATOM   1470 C C   . LYS   A 1 197 ? -11.45252 -14.62467 -6.87562  1.000 20.84730 ? 204 LYS   A C   1 
ATOM   1471 O O   . LYS   A 1 197 ? -11.48571 -13.41204 -7.08564  1.000 20.79113 ? 204 LYS   A O   1 
ATOM   1472 C CB  . LYS   A 1 197 ? -13.45131 -16.00812 -7.32309  1.000 22.55301 ? 204 LYS   A CB  1 
ATOM   1473 C CG  . LYS   A 1 197 ? -14.33433 -16.72139 -8.31862  1.000 32.57183 ? 204 LYS   A CG  1 
ATOM   1474 C CD  . LYS   A 1 197 ? -15.63385 -17.14183 -7.62416  1.000 38.74247 ? 204 LYS   A CD  1 
ATOM   1475 C CE  . LYS   A 1 197 ? -16.65902 -17.69887 -8.60764  1.000 52.78137 ? 204 LYS   A CE  1 
ATOM   1476 N NZ  . LYS   A 1 197 ? -17.69715 -18.50724 -7.90886  1.000 48.94182 ? 204 LYS   A NZ  1 
ATOM   1477 N N   . GLU   A 1 198 ? -10.90449 -15.15099 -5.77478  1.000 19.14579 ? 205 GLU   A N   1 
ATOM   1478 C CA  . GLU   A 1 198 ? -10.21031 -14.29885 -4.80668  1.000 19.26279 ? 205 GLU   A CA  1 
ATOM   1479 C C   . GLU   A 1 198 ? -9.12315  -13.45948 -5.47137  1.000 20.03255 ? 205 GLU   A C   1 
ATOM   1480 O O   . GLU   A 1 198 ? -8.97300  -12.26316 -5.18098  1.000 18.79859 ? 205 GLU   A O   1 
ATOM   1481 C CB  . GLU   A 1 198 ? -9.59894  -15.17647 -3.71496  1.000 19.78784 ? 205 GLU   A CB  1 
ATOM   1482 C CG  . GLU   A 1 198 ? -8.84979  -14.42649 -2.65280  1.000 20.42259 ? 205 GLU   A CG  1 
ATOM   1483 C CD  . GLU   A 1 198 ? -8.21677  -15.38262 -1.65179  1.000 23.30559 ? 205 GLU   A CD  1 
ATOM   1484 O OE1 . GLU   A 1 198 ? -7.71147  -16.41177 -2.11384  1.000 24.33915 ? 205 GLU   A OE1 1 
ATOM   1485 O OE2 . GLU   A 1 198 ? -8.27310  -15.13077 -0.41222  1.000 22.84591 ? 205 GLU   A OE2 1 
ATOM   1486 N N   . ILE   A 1 199 ? -8.32789  -14.08279 -6.34089  1.000 17.44587 ? 206 ILE   A N   1 
ATOM   1487 C CA  . ILE   A 1 199 ? -7.18760  -13.37467 -6.91508  1.000 17.69870 ? 206 ILE   A CA  1 
ATOM   1488 C C   . ILE   A 1 199 ? -7.65885  -12.30167 -7.88113  1.000 17.08360 ? 206 ILE   A C   1 
ATOM   1489 O O   . ILE   A 1 199 ? -7.11721  -11.18387 -7.90975  1.000 18.76122 ? 206 ILE   A O   1 
ATOM   1490 C CB  . ILE   A 1 199 ? -6.24519  -14.36743 -7.60607  1.000 19.03454 ? 206 ILE   A CB  1 
ATOM   1491 C CG1 . ILE   A 1 199 ? -5.66038  -15.31916 -6.54337  1.000 22.29864 ? 206 ILE   A CG1 1 
ATOM   1492 C CG2 . ILE   A 1 199 ? -5.11342  -13.64475 -8.32828  1.000 16.79405 ? 206 ILE   A CG2 1 
ATOM   1493 C CD1 . ILE   A 1 199 ? -5.04609  -16.54665 -7.18756  1.000 19.03219 ? 206 ILE   A CD1 1 
ATOM   1494 N N   . VAL   A 1 200 ? -8.63359  -12.64398 -8.71878  1.000 18.27389 ? 207 VAL   A N   1 
ATOM   1495 C CA  . VAL   A 1 200 ? -9.14595  -11.67908 -9.68548  1.000 17.58301 ? 207 VAL   A CA  1 
ATOM   1496 C C   . VAL   A 1 200 ? -9.76451  -10.49197 -8.95440  1.000 20.35395 ? 207 VAL   A C   1 
ATOM   1497 O O   . VAL   A 1 200 ? -9.47953  -9.33358  -9.26838  1.000 20.77829 ? 207 VAL   A O   1 
ATOM   1498 C CB  . VAL   A 1 200 ? -10.14958 -12.36038 -10.62832 1.000 17.89731 ? 207 VAL   A CB  1 
ATOM   1499 C CG1 . VAL   A 1 200 ? -10.88695 -11.30803 -11.47282 1.000 18.90635 ? 207 VAL   A CG1 1 
ATOM   1500 C CG2 . VAL   A 1 200 ? -9.45404  -13.41353 -11.51477 1.000 17.73205 ? 207 VAL   A CG2 1 
ATOM   1501 N N   . LYS   A 1 201 ? -10.58386 -10.76699 -7.92971  1.000 18.98011 ? 208 LYS   A N   1 
ATOM   1502 C CA  . LYS   A 1 201 ? -11.16942 -9.68050  -7.15294  1.000 20.21947 ? 208 LYS   A CA  1 
ATOM   1503 C C   . LYS   A 1 201 ? -10.09149 -8.79907  -6.52309  1.000 27.26414 ? 208 LYS   A C   1 
ATOM   1504 O O   . LYS   A 1 201 ? -10.23790 -7.57357  -6.46610  1.000 25.97978 ? 208 LYS   A O   1 
ATOM   1505 C CB  . LYS   A 1 201 ? -12.10704 -10.24041 -6.07188  1.000 20.96861 ? 208 LYS   A CB  1 
ATOM   1506 C CG  . LYS   A 1 201 ? -13.08719 -9.20436  -5.47970  1.000 36.36543 ? 208 LYS   A CG  1 
ATOM   1507 C CD  . LYS   A 1 201 ? -13.66822 -9.67749  -4.13376  1.000 50.81743 ? 208 LYS   A CD  1 
ATOM   1508 C CE  . LYS   A 1 201 ? -14.10479 -8.51546  -3.23402  1.000 71.78304 ? 208 LYS   A CE  1 
ATOM   1509 N NZ  . LYS   A 1 201 ? -12.99910 -7.96923  -2.36521  1.000 56.53593 ? 208 LYS   A NZ  1 
ATOM   1510 N N   . LYS   A 1 202 ? -9.01299  -9.40086  -6.02637  1.000 21.09981 ? 209 LYS   A N   1 
ATOM   1511 C CA  . LYS   A 1 202 ? -8.01605  -8.63125  -5.28015  1.000 20.79682 ? 209 LYS   A CA  1 
ATOM   1512 C C   . LYS   A 1 202 ? -7.16981  -7.76749  -6.21222  1.000 21.00256 ? 209 LYS   A C   1 
ATOM   1513 O O   . LYS   A 1 202 ? -6.82634  -6.62266  -5.88142  1.000 22.51087 ? 209 LYS   A O   1 
ATOM   1514 C CB  . LYS   A 1 202 ? -7.13210  -9.59097  -4.47448  1.000 24.34563 ? 209 LYS   A CB  1 
ATOM   1515 C CG  . LYS   A 1 202 ? -5.88862  -8.98352  -3.80165  1.000 25.96818 ? 209 LYS   A CG  1 
ATOM   1516 C CD  . LYS   A 1 202 ? -5.25173  -10.03636 -2.85385  1.000 29.05880 ? 209 LYS   A CD  1 
ATOM   1517 C CE  . LYS   A 1 202 ? -4.07383  -9.47999  -2.05545  1.000 49.51166 ? 209 LYS   A CE  1 
ATOM   1518 N NZ  . LYS   A 1 202 ? -3.31794  -10.56525 -1.30731  1.000 45.07777 ? 209 LYS   A NZ  1 
ATOM   1519 N N   . HIS   A 1 203 ? -6.85111  -8.28018  -7.39233  1.000 19.92257 ? 210 HIS   A N   1 
ATOM   1520 C CA  . HIS   A 1 203 ? -5.81933  -7.68846  -8.23038  1.000 20.52657 ? 210 HIS   A CA  1 
ATOM   1521 C C   . HIS   A 1 203 ? -6.31346  -7.17058  -9.55410  1.000 21.53753 ? 210 HIS   A C   1 
ATOM   1522 O O   . HIS   A 1 203 ? -5.59705  -6.38013  -10.18999 1.000 22.59177 ? 210 HIS   A O   1 
ATOM   1523 C CB  . HIS   A 1 203 ? -4.72013  -8.71153  -8.54003  1.000 19.33008 ? 210 HIS   A CB  1 
ATOM   1524 C CG  . HIS   A 1 203 ? -3.92815  -9.10924  -7.34742  1.000 19.50790 ? 210 HIS   A CG  1 
ATOM   1525 N ND1 . HIS   A 1 203 ? -3.11930  -8.22278  -6.67114  1.000 22.67048 ? 210 HIS   A ND1 1 
ATOM   1526 C CD2 . HIS   A 1 203 ? -3.79951  -10.30103 -6.71753  1.000 24.16575 ? 210 HIS   A CD2 1 
ATOM   1527 C CE1 . HIS   A 1 203 ? -2.53332  -8.85102  -5.66782  1.000 27.83657 ? 210 HIS   A CE1 1 
ATOM   1528 N NE2 . HIS   A 1 203 ? -2.93298  -10.11106 -5.67128  1.000 24.46648 ? 210 HIS   A NE2 1 
ATOM   1529 N N   . SER   A 1 204 ? -7.47388  -7.62660  -10.02426 1.000 20.18166 ? 211 SER   A N   1 
ATOM   1530 C CA  . SER   A 1 204 ? -7.87824  -7.33045  -11.39414 1.000 18.56095 ? 211 SER   A CA  1 
ATOM   1531 C C   . SER   A 1 204 ? -9.30274  -6.78883  -11.46138 1.000 18.78323 ? 211 SER   A C   1 
ATOM   1532 O O   . SER   A 1 204 ? -9.92362  -6.82485  -12.52627 1.000 22.23384 ? 211 SER   A O   1 
ATOM   1533 C CB  . SER   A 1 204 ? -7.71640  -8.60036  -12.24889 1.000 19.73936 ? 211 SER   A CB  1 
ATOM   1534 O OG  . SER   A 1 204 ? -6.37047  -9.04969  -12.19147 1.000 20.94766 ? 211 SER   A OG  1 
ATOM   1535 N N   . GLN   A 1 205 ? -9.82057  -6.25821  -10.33824 1.000 21.37419 ? 212 GLN   A N   1 
ATOM   1536 C CA  . GLN   A 1 205 ? -11.22640 -5.87575  -10.25806 1.000 29.67403 ? 212 GLN   A CA  1 
ATOM   1537 C C   . GLN   A 1 205 ? -11.61395 -4.81996  -11.29080 1.000 33.22100 ? 212 GLN   A C   1 
ATOM   1538 O O   . GLN   A 1 205 ? -12.74574 -4.84001  -11.78245 1.000 29.69372 ? 212 GLN   A O   1 
ATOM   1539 C CB  . GLN   A 1 205 ? -11.55544 -5.37243  -8.84655  1.000 33.54428 ? 212 GLN   A CB  1 
ATOM   1540 C CG  . GLN   A 1 205 ? -13.01164 -5.02000  -8.65541  1.000 55.08279 ? 212 GLN   A CG  1 
ATOM   1541 C CD  . GLN   A 1 205 ? -13.25512 -4.20371  -7.39065  1.000 61.97415 ? 212 GLN   A CD  1 
ATOM   1542 O OE1 . GLN   A 1 205 ? -12.37283 -4.09122  -6.53751  1.000 47.22486 ? 212 GLN   A OE1 1 
ATOM   1543 N NE2 . GLN   A 1 205 ? -14.45210 -3.61808  -7.27407  1.000 57.22624 ? 212 GLN   A NE2 1 
ATOM   1544 N N   . PHE   A 1 206 ? -10.69350 -3.92595  -11.66673 1.000 21.01111 ? 213 PHE   A N   1 
ATOM   1545 C CA  . PHE   A 1 206 ? -11.02929 -2.80151  -12.53779 1.000 21.64645 ? 213 PHE   A CA  1 
ATOM   1546 C C   . PHE   A 1 206 ? -10.58630 -2.99647  -13.98113 1.000 19.69513 ? 213 PHE   A C   1 
ATOM   1547 O O   . PHE   A 1 206 ? -10.66193 -2.04300  -14.77818 1.000 21.82694 ? 213 PHE   A O   1 
ATOM   1548 C CB  . PHE   A 1 206 ? -10.44571 -1.51594  -11.97442 1.000 23.35133 ? 213 PHE   A CB  1 
ATOM   1549 C CG  . PHE   A 1 206 ? -11.00549 -1.17152  -10.63134 1.000 25.62804 ? 213 PHE   A CG  1 
ATOM   1550 C CD1 . PHE   A 1 206 ? -12.37742 -1.09449  -10.45324 1.000 26.60814 ? 213 PHE   A CD1 1 
ATOM   1551 C CD2 . PHE   A 1 206 ? -10.16801 -0.92051  -9.55380  1.000 29.31993 ? 213 PHE   A CD2 1 
ATOM   1552 C CE1 . PHE   A 1 206 ? -12.93839 -0.76644  -9.20553  1.000 29.24840 ? 213 PHE   A CE1 1 
ATOM   1553 C CE2 . PHE   A 1 206 ? -10.71233 -0.59344  -8.29251  1.000 39.43684 ? 213 PHE   A CE2 1 
ATOM   1554 C CZ  . PHE   A 1 206 ? -12.09517 -0.50996  -8.12400  1.000 34.00590 ? 213 PHE   A CZ  1 
ATOM   1555 N N   . ILE   A 1 207 ? -10.18909 -4.21305  -14.35292 1.000 21.28015 ? 214 ILE   A N   1 
ATOM   1556 C CA  . ILE   A 1 207 ? -9.91653  -4.49758  -15.75359 1.000 19.01817 ? 214 ILE   A CA  1 
ATOM   1557 C C   . ILE   A 1 207 ? -11.16599 -4.20444  -16.57208 1.000 24.10101 ? 214 ILE   A C   1 
ATOM   1558 O O   . ILE   A 1 207 ? -12.28346 -4.54696  -16.17522 1.000 23.25615 ? 214 ILE   A O   1 
ATOM   1559 C CB  . ILE   A 1 207 ? -9.45638  -5.95016  -15.94234 1.000 16.05853 ? 214 ILE   A CB  1 
ATOM   1560 C CG1 . ILE   A 1 207 ? -8.11336  -6.16365  -15.23411 1.000 21.70600 ? 214 ILE   A CG1 1 
ATOM   1561 C CG2 . ILE   A 1 207 ? -9.45135  -6.33207  -17.44566 1.000 16.62716 ? 214 ILE   A CG2 1 
ATOM   1562 C CD1 . ILE   A 1 207 ? -6.94516  -5.44501  -15.85089 1.000 21.20629 ? 214 ILE   A CD1 1 
ATOM   1563 N N   . GLY   A 1 208 ? -10.97971 -3.53743  -17.71240 1.000 18.92665 ? 215 GLY   A N   1 
ATOM   1564 C CA  . GLY   A 1 208 ? -12.10594 -2.97092  -18.43355 1.000 18.57357 ? 215 GLY   A CA  1 
ATOM   1565 C C   . GLY   A 1 208 ? -12.68945 -3.89240  -19.48763 1.000 21.84866 ? 215 GLY   A C   1 
ATOM   1566 O O   . GLY   A 1 208 ? -13.24498 -3.42350  -20.48592 1.000 22.64915 ? 215 GLY   A O   1 
ATOM   1567 N N   . TYR   A 1 209 ? -12.56725 -5.20388  -19.28427 1.000 19.25944 ? 216 TYR   A N   1 
ATOM   1568 C CA  . TYR   A 1 209 ? -13.12281 -6.18839  -20.19703 1.000 17.64650 ? 216 TYR   A CA  1 
ATOM   1569 C C   . TYR   A 1 209 ? -13.72541 -7.29447  -19.35435 1.000 17.96699 ? 216 TYR   A C   1 
ATOM   1570 O O   . TYR   A 1 209 ? -13.24911 -7.55211  -18.23989 1.000 17.97567 ? 216 TYR   A O   1 
ATOM   1571 C CB  . TYR   A 1 209 ? -12.05084 -6.78684  -21.12032 1.000 16.69559 ? 216 TYR   A CB  1 
ATOM   1572 C CG  . TYR   A 1 209 ? -11.42104 -5.75668  -21.98251 1.000 18.94115 ? 216 TYR   A CG  1 
ATOM   1573 C CD1 . TYR   A 1 209 ? -12.04022 -5.33897  -23.15940 1.000 20.69253 ? 216 TYR   A CD1 1 
ATOM   1574 C CD2 . TYR   A 1 209 ? -10.23368 -5.13239  -21.57874 1.000 15.92469 ? 216 TYR   A CD2 1 
ATOM   1575 C CE1 . TYR   A 1 209 ? -11.46674 -4.34275  -23.94322 1.000 23.80273 ? 216 TYR   A CE1 1 
ATOM   1576 C CE2 . TYR   A 1 209 ? -9.64696  -4.13563  -22.35671 1.000 17.01831 ? 216 TYR   A CE2 1 
ATOM   1577 C CZ  . TYR   A 1 209 ? -10.27778 -3.74207  -23.52812 1.000 18.04410 ? 216 TYR   A CZ  1 
ATOM   1578 O OH  . TYR   A 1 209 ? -9.70591  -2.76224  -24.31832 1.000 19.80558 ? 216 TYR   A OH  1 
ATOM   1579 N N   . PRO   A 1 210 ? -14.74208 -7.97708  -19.86387 1.000 19.04236 ? 217 PRO   A N   1 
ATOM   1580 C CA  . PRO   A 1 210 ? -15.36112 -9.05247  -19.07436 1.000 19.78510 ? 217 PRO   A CA  1 
ATOM   1581 C C   . PRO   A 1 210 ? -14.39694 -10.21857 -18.90450 1.000 23.28940 ? 217 PRO   A C   1 
ATOM   1582 O O   . PRO   A 1 210 ? -13.84948 -10.74309 -19.88013 1.000 21.42777 ? 217 PRO   A O   1 
ATOM   1583 C CB  . PRO   A 1 210 ? -16.60054 -9.44127  -19.90528 1.000 23.11111 ? 217 PRO   A CB  1 
ATOM   1584 C CG  . PRO   A 1 210 ? -16.32676 -8.96419  -21.25185 1.000 25.71212 ? 217 PRO   A CG  1 
ATOM   1585 C CD  . PRO   A 1 210 ? -15.45436 -7.72981  -21.13117 1.000 19.28636 ? 217 PRO   A CD  1 
ATOM   1586 N N   . ILE   A 1 211 ? -14.19841 -10.61909 -17.65744 1.000 19.73667 ? 218 ILE   A N   1 
ATOM   1587 C CA  . ILE   A 1 211 ? -13.37801 -11.77372 -17.29522 1.000 18.99869 ? 218 ILE   A CA  1 
ATOM   1588 C C   . ILE   A 1 211 ? -14.32376 -12.88737 -16.84771 1.000 22.53676 ? 218 ILE   A C   1 
ATOM   1589 O O   . ILE   A 1 211 ? -15.02509 -12.74934 -15.83196 1.000 22.31152 ? 218 ILE   A O   1 
ATOM   1590 C CB  . ILE   A 1 211 ? -12.38106 -11.41508 -16.17792 1.000 22.48739 ? 218 ILE   A CB  1 
ATOM   1591 C CG1 . ILE   A 1 211 ? -11.39742 -10.30744 -16.63773 1.000 15.81623 ? 218 ILE   A CG1 1 
ATOM   1592 C CG2 . ILE   A 1 211 ? -11.66597 -12.68128 -15.67870 1.000 17.54698 ? 218 ILE   A CG2 1 
ATOM   1593 C CD1 . ILE   A 1 211 ? -10.62102 -9.61440  -15.40999 1.000 16.21242 ? 218 ILE   A CD1 1 
ATOM   1594 N N   . THR   A 1 212 ? -14.33680 -13.99890 -17.58400 1.000 18.34283 ? 219 THR   A N   1 
ATOM   1595 C CA  . THR   A 1 212 ? -15.24806 -15.10438 -17.28263 1.000 22.03522 ? 219 THR   A CA  1 
ATOM   1596 C C   . THR   A 1 212 ? -14.43211 -16.27159 -16.75653 1.000 21.73841 ? 219 THR   A C   1 
ATOM   1597 O O   . THR   A 1 212 ? -13.52050 -16.76121 -17.43627 1.000 15.51296 ? 219 THR   A O   1 
ATOM   1598 C CB  . THR   A 1 212 ? -16.05429 -15.51859 -18.52196 1.000 18.72969 ? 219 THR   A CB  1 
ATOM   1599 O OG1 . THR   A 1 212 ? -16.79419 -14.38143 -18.97679 1.000 21.62380 ? 219 THR   A OG1 1 
ATOM   1600 C CG2 . THR   A 1 212 ? -17.02109 -16.64471 -18.19660 1.000 20.99681 ? 219 THR   A CG2 1 
ATOM   1601 N N   . LEU   A 1 213 ? -14.71691 -16.69036 -15.53243 1.000 19.23471 ? 220 LEU   A N   1 
ATOM   1602 C CA  . LEU   A 1 213 ? -14.03648 -17.85205 -14.96730 1.000 24.47031 ? 220 LEU   A CA  1 
ATOM   1603 C C   . LEU   A 1 213 ? -14.88033 -19.08204 -15.30075 1.000 29.31549 ? 220 LEU   A C   1 
ATOM   1604 O O   . LEU   A 1 213 ? -16.00527 -19.20972 -14.81737 1.000 22.92089 ? 220 LEU   A O   1 
ATOM   1605 C CB  . LEU   A 1 213 ? -13.84668 -17.68110 -13.46197 1.000 22.30632 ? 220 LEU   A CB  1 
ATOM   1606 C CG  . LEU   A 1 213 ? -13.39491 -18.92484 -12.67651 1.000 29.71051 ? 220 LEU   A CG  1 
ATOM   1607 C CD1 . LEU   A 1 213 ? -12.08736 -19.50280 -13.22388 1.000 28.78586 ? 220 LEU   A CD1 1 
ATOM   1608 C CD2 . LEU   A 1 213 ? -13.24526 -18.57441 -11.17872 1.000 22.48459 ? 220 LEU   A CD2 1 
ATOM   1609 N N   . PHE   A 1 214 ? -14.36148 -19.96143 -16.16122 1.000 22.96047 ? 221 PHE   A N   1 
ATOM   1610 C CA  . PHE   A 1 214 ? -15.06545 -21.19125 -16.50094 1.000 20.35011 ? 221 PHE   A CA  1 
ATOM   1611 C C   . PHE   A 1 214 ? -15.00082 -22.17775 -15.34054 1.000 27.01632 ? 221 PHE   A C   1 
ATOM   1612 O O   . PHE   A 1 214 ? -13.95906 -22.34007 -14.71013 1.000 31.14543 ? 221 PHE   A O   1 
ATOM   1613 C CB  . PHE   A 1 214 ? -14.45621 -21.86793 -17.73604 1.000 22.01479 ? 221 PHE   A CB  1 
ATOM   1614 C CG  . PHE   A 1 214 ? -14.80412 -21.20376 -19.04909 1.000 22.02587 ? 221 PHE   A CG  1 
ATOM   1615 C CD1 . PHE   A 1 214 ? -14.95690 -19.82655 -19.14546 1.000 18.90535 ? 221 PHE   A CD1 1 
ATOM   1616 C CD2 . PHE   A 1 214 ? -14.97533 -21.97481 -20.18727 1.000 25.83799 ? 221 PHE   A CD2 1 
ATOM   1617 C CE1 . PHE   A 1 214 ? -15.25023 -19.21863 -20.37225 1.000 21.17960 ? 221 PHE   A CE1 1 
ATOM   1618 C CE2 . PHE   A 1 214 ? -15.27869 -21.38182 -21.42370 1.000 29.51079 ? 221 PHE   A CE2 1 
ATOM   1619 C CZ  . PHE   A 1 214 ? -15.42338 -19.99868 -21.50904 1.000 20.81927 ? 221 PHE   A CZ  1 
ATOM   1620 N N   . VAL   A 1 215 ? -16.10999 -22.84305 -15.07147 1.000 20.39774 ? 222 VAL   A N   1 
ATOM   1621 C CA  . VAL   A 1 215 ? -16.15148 -23.84610 -14.01801 1.000 22.02869 ? 222 VAL   A CA  1 
ATOM   1622 C C   . VAL   A 1 215 ? -16.01268 -25.21697 -14.67407 1.000 26.68447 ? 222 VAL   A C   1 
ATOM   1623 O O   . VAL   A 1 215 ? -16.30977 -25.38701 -15.85665 1.000 26.21643 ? 222 VAL   A O   1 
ATOM   1624 C CB  . VAL   A 1 215 ? -17.43705 -23.71348 -13.17093 1.000 32.62561 ? 222 VAL   A CB  1 
ATOM   1625 C CG1 . VAL   A 1 215 ? -17.74235 -22.26311 -12.85334 1.000 37.13181 ? 222 VAL   A CG1 1 
ATOM   1626 C CG2 . VAL   A 1 215 ? -18.53538 -24.17644 -13.89827 1.000 34.89157 ? 222 VAL   A CG2 1 
ATOM   1627 N N   . GLU   A 1 216 ? -15.48962 -26.19408 -13.94457 1.000 25.77295 ? 223 GLU   A N   1 
ATOM   1628 C CA  . GLU   A 1 216 ? -15.30930 -27.50210 -14.57901 1.000 32.46018 ? 223 GLU   A CA  1 
ATOM   1629 C C   . GLU   A 1 216 ? -16.53678 -28.38608 -14.41675 1.000 37.13262 ? 223 GLU   A C   1 
ATOM   1630 O O   . GLU   A 1 216 ? -17.27802 -28.27486 -13.43725 1.000 30.79396 ? 223 GLU   A O   1 
ATOM   1631 C CB  . GLU   A 1 216 ? -14.08472 -28.23776 -14.04603 1.000 33.17817 ? 223 GLU   A CB  1 
ATOM   1632 C CG  . GLU   A 1 216 ? -12.80987 -27.43128 -14.08652 1.000 42.74344 ? 223 GLU   A CG  1 
ATOM   1633 C CD  . GLU   A 1 216 ? -11.60683 -28.32880 -13.87698 1.000 48.07216 ? 223 GLU   A CD  1 
ATOM   1634 O OE1 . GLU   A 1 216 ? -11.48078 -29.33306 -14.61366 1.000 51.80125 ? 223 GLU   A OE1 1 
ATOM   1635 O OE2 . GLU   A 1 216 ? -10.81019 -28.05001 -12.96569 1.000 53.64513 ? 223 GLU   A OE2 1 
ATOM   1636 N N   . LYS   A 1 217 ? -16.73498 -29.28690 -15.38680 1.000 31.61082 ? 224 LYS   A N   1 
ATOM   1637 C CA  . LYS   A 1 217 ? -17.94111 -30.11327 -15.43117 1.000 31.47161 ? 224 LYS   A CA  1 
ATOM   1638 C C   . LYS   A 1 217 ? -17.90020 -31.31184 -14.45851 1.000 41.58707 ? 224 LYS   A C   1 
ATOM   1639 O O   . LYS   A 1 217 ? -16.82861 -31.81507 -14.11071 1.000 50.55451 ? 224 LYS   A O   1 
ATOM   1640 C CB  . LYS   A 1 217 ? -18.19944 -30.61400 -16.87063 1.000 32.22447 ? 224 LYS   A CB  1 
ATOM   1641 C CG  . LYS   A 1 217 ? -17.88144 -29.56602 -17.95665 1.000 30.07750 ? 224 LYS   A CG  1 
ATOM   1642 C CD  . LYS   A 1 217 ? -18.23579 -30.05729 -19.34803 1.000 31.39473 ? 224 LYS   A CD  1 
ATOM   1643 C CE  . LYS   A 1 217 ? -16.98722 -30.59987 -20.02259 1.000 31.72185 ? 224 LYS   A CE  1 
ATOM   1644 N NZ  . LYS   A 1 217 ? -15.92712 -29.57710 -20.05650 1.000 29.31597 ? 224 LYS   A NZ  1 
HETATM 1645 N N1  . A1AXV B 2 .   ? 7.75659   -11.90087 -23.51903 0.934 15.16402 ? 301 A1AXV A N1  1 
HETATM 1646 C C4  . A1AXV B 2 .   ? 8.22780   -13.94968 -26.54770 0.934 19.20799 ? 301 A1AXV A C4  1 
HETATM 1647 C C5  . A1AXV B 2 .   ? 8.42804   -13.02022 -25.54151 0.934 15.93448 ? 301 A1AXV A C5  1 
HETATM 1648 C C6  . A1AXV B 2 .   ? 7.48313   -12.86775 -24.53766 0.934 24.30976 ? 301 A1AXV A C6  1 
HETATM 1649 C C7  . A1AXV B 2 .   ? 6.98207   -10.88768 -23.11004 0.934 16.27907 ? 301 A1AXV A C7  1 
HETATM 1650 C C8  . A1AXV B 2 .   ? 6.33787   -13.65226 -24.55141 0.934 18.30779 ? 301 A1AXV A C8  1 
HETATM 1651 C C1  . A1AXV B 2 .   ? 4.89801   -15.45015 -25.57635 0.934 19.61781 ? 301 A1AXV A C1  1 
HETATM 1652 C C2  . A1AXV B 2 .   ? 6.13114   -14.59177 -25.56425 0.934 20.94195 ? 301 A1AXV A C2  1 
HETATM 1653 C C3  . A1AXV B 2 .   ? 7.08666   -14.72421 -26.55562 0.934 19.68659 ? 301 A1AXV A C3  1 
HETATM 1654 N N2  . A1AXV B 2 .   ? 5.75024   -10.81232 -23.59314 0.934 17.69884 ? 301 A1AXV A N2  1 
HETATM 1655 S S1  . A1AXV B 2 .   ? 7.63004   -9.67225  -22.11278 0.934 18.18144 ? 301 A1AXV A S1  1 
HETATM 1656 O O   . HOH   C 3 .   ? 12.72671  -2.31520  -21.91794 1.000 36.99961 ? 401 HOH   A O   1 
HETATM 1657 O O   . HOH   C 3 .   ? 4.57980   -16.42286 -40.89065 1.000 57.40657 ? 402 HOH   A O   1 
HETATM 1658 O O   . HOH   C 3 .   ? -16.67660 -32.70502 -12.11354 1.000 63.19569 ? 403 HOH   A O   1 
HETATM 1659 O O   . HOH   C 3 .   ? -12.77890 -27.59488 -35.10188 1.000 53.57813 ? 404 HOH   A O   1 
HETATM 1660 O O   . HOH   C 3 .   ? 6.88731   1.47093   -11.34952 1.000 47.37658 ? 405 HOH   A O   1 
HETATM 1661 O O   . HOH   C 3 .   ? -13.44633 1.15132   -25.46531 1.000 51.99145 ? 406 HOH   A O   1 
HETATM 1662 O O   . HOH   C 3 .   ? 18.76996  0.25309   -13.35645 1.000 48.64120 ? 407 HOH   A O   1 
HETATM 1663 O O   . HOH   C 3 .   ? -11.54001 -26.32747 -11.44140 1.000 43.02609 ? 408 HOH   A O   1 
HETATM 1664 O O   . HOH   C 3 .   ? -6.86208  -28.00231 -7.50355  1.000 32.56710 ? 409 HOH   A O   1 
HETATM 1665 O O   . HOH   C 3 .   ? 6.85032   -20.33843 -40.15707 1.000 36.57043 ? 410 HOH   A O   1 
HETATM 1666 O O   . HOH   C 3 .   ? -15.87776 -25.09975 -9.50257  1.000 48.12484 ? 411 HOH   A O   1 
HETATM 1667 O O   . HOH   C 3 .   ? -15.62221 -33.92062 -13.66355 1.000 53.65248 ? 412 HOH   A O   1 
HETATM 1668 O O   . HOH   C 3 .   ? 5.90094   -25.04459 -38.17321 1.000 41.83267 ? 413 HOH   A O   1 
HETATM 1669 O O   . HOH   C 3 .   ? -10.54015 -8.27229  -2.41283  1.000 36.16304 ? 414 HOH   A O   1 
HETATM 1670 O O   . HOH   C 3 .   ? 9.97972   -23.49981 -8.94136  1.000 47.54316 ? 415 HOH   A O   1 
HETATM 1671 O O   . HOH   C 3 .   ? -9.92617  -4.25355  -6.14564  1.000 51.45381 ? 416 HOH   A O   1 
HETATM 1672 O O   . HOH   C 3 .   ? 6.47553   -24.90327 -6.66241  1.000 51.89790 ? 417 HOH   A O   1 
HETATM 1673 O O   . HOH   C 3 .   ? 0.37434   -14.03016 -1.49511  1.000 49.80087 ? 418 HOH   A O   1 
HETATM 1674 O O   . HOH   C 3 .   ? 18.74226  -26.44095 -20.09957 1.000 48.62492 ? 419 HOH   A O   1 
HETATM 1675 O O   . HOH   C 3 .   ? 10.31141  -26.19392 -16.26157 1.000 33.05665 ? 420 HOH   A O   1 
HETATM 1676 O O   . HOH   C 3 .   ? 8.50925   -22.07797 -36.56443 1.000 39.84745 ? 421 HOH   A O   1 
HETATM 1677 O O   . HOH   C 3 .   ? 10.36640  -17.08202 -7.12587  1.000 22.77192 ? 422 HOH   A O   1 
HETATM 1678 O O   . HOH   C 3 .   ? -3.91544  -11.05029 -27.81096 1.000 16.64881 ? 423 HOH   A O   1 
HETATM 1679 O O   . HOH   C 3 .   ? 8.82085   -23.01837 -13.52131 1.000 32.51478 ? 424 HOH   A O   1 
HETATM 1680 O O   . HOH   C 3 .   ? 0.56802   -5.57938  -18.80623 1.000 23.05677 ? 425 HOH   A O   1 
HETATM 1681 O O   . HOH   C 3 .   ? 19.22715  -18.89489 -23.48792 1.000 43.37587 ? 426 HOH   A O   1 
HETATM 1682 O O   . HOH   C 3 .   ? -2.53774  -5.71663  -7.10685  1.000 31.29946 ? 427 HOH   A O   1 
HETATM 1683 O O   . HOH   C 3 .   ? -15.25108 -13.29588 -20.78265 1.000 19.86216 ? 428 HOH   A O   1 
HETATM 1684 O O   . HOH   C 3 .   ? 14.23131  -23.33035 -39.77435 1.000 47.06213 ? 429 HOH   A O   1 
HETATM 1685 O O   . HOH   C 3 .   ? -1.00489  -21.62618 -38.61704 1.000 48.63716 ? 430 HOH   A O   1 
HETATM 1686 O O   . HOH   C 3 .   ? 8.17573   -29.62823 -19.37146 1.000 35.44219 ? 431 HOH   A O   1 
HETATM 1687 O O   . HOH   C 3 .   ? -10.07583 -23.88366 -2.39541  1.000 43.47315 ? 432 HOH   A O   1 
HETATM 1688 O O   . HOH   C 3 .   ? 20.97791  -2.41459  -8.16933  1.000 43.75478 ? 433 HOH   A O   1 
HETATM 1689 O O   . HOH   C 3 .   ? -15.42864 -26.14685 -18.21660 1.000 30.84483 ? 434 HOH   A O   1 
HETATM 1690 O O   . HOH   C 3 .   ? -4.97502  -2.48622  -20.36219 1.000 17.29809 ? 435 HOH   A O   1 
HETATM 1691 O O   . HOH   C 3 .   ? -17.49347 -11.64198 -24.89662 1.000 30.44089 ? 436 HOH   A O   1 
HETATM 1692 O O   . HOH   C 3 .   ? 13.92298  -27.88462 -33.41086 1.000 24.88125 ? 437 HOH   A O   1 
HETATM 1693 O O   . HOH   C 3 .   ? 19.43838  -16.09046 -12.71175 1.000 32.28434 ? 438 HOH   A O   1 
HETATM 1694 O O   . HOH   C 3 .   ? 1.21270   -20.63606 -4.45141  1.000 32.92649 ? 439 HOH   A O   1 
HETATM 1695 O O   . HOH   C 3 .   ? 1.64375   -6.37864  -5.67807  1.000 41.93458 ? 440 HOH   A O   1 
HETATM 1696 O O   . HOH   C 3 .   ? 6.20618   -20.72941 0.28854   1.000 29.63549 ? 441 HOH   A O   1 
HETATM 1697 O O   . HOH   C 3 .   ? -12.61402 -24.57738 -16.50902 1.000 37.79723 ? 442 HOH   A O   1 
HETATM 1698 O O   . HOH   C 3 .   ? -4.42504  -6.01319  -39.73042 1.000 38.86230 ? 443 HOH   A O   1 
HETATM 1699 O O   . HOH   C 3 .   ? 11.63701  -14.23481 -24.59113 1.000 17.42295 ? 444 HOH   A O   1 
HETATM 1700 O O   . HOH   C 3 .   ? 1.75678   -2.24387  -20.51106 1.000 40.03302 ? 445 HOH   A O   1 
HETATM 1701 O O   . HOH   C 3 .   ? -3.91057  -13.88906 -1.18977  1.000 45.63746 ? 446 HOH   A O   1 
HETATM 1702 O O   . HOH   C 3 .   ? 6.15157   -28.68121 -7.45818  1.000 45.54761 ? 447 HOH   A O   1 
HETATM 1703 O O   . HOH   C 3 .   ? 5.51657   -8.24509  -36.30236 1.000 29.76004 ? 448 HOH   A O   1 
HETATM 1704 O O   . HOH   C 3 .   ? -0.76716  -28.53914 -5.30971  1.000 33.81287 ? 449 HOH   A O   1 
HETATM 1705 O O   . HOH   C 3 .   ? 2.41168   -7.94707  -16.89451 1.000 22.75336 ? 450 HOH   A O   1 
HETATM 1706 O O   . HOH   C 3 .   ? 3.98260   -5.97130  -11.22408 1.000 25.98966 ? 451 HOH   A O   1 
HETATM 1707 O O   . HOH   C 3 .   ? 8.52327   -26.89066 -26.87752 1.000 27.07174 ? 452 HOH   A O   1 
HETATM 1708 O O   . HOH   C 3 .   ? -7.93448  -4.70587  -41.85010 1.000 45.50895 ? 453 HOH   A O   1 
HETATM 1709 O O   . HOH   C 3 .   ? 1.52665   -5.25768  -14.41286 1.000 28.14145 ? 454 HOH   A O   1 
HETATM 1710 O O   . HOH   C 3 .   ? 2.45644   -3.92533  -24.74212 1.000 36.43901 ? 455 HOH   A O   1 
HETATM 1711 O O   . HOH   C 3 .   ? 13.98670  -15.38755 -1.13496  1.000 38.85690 ? 456 HOH   A O   1 
HETATM 1712 O O   . HOH   C 3 .   ? 5.70092   -5.33346  -21.93994 1.000 31.83740 ? 457 HOH   A O   1 
HETATM 1713 O O   . HOH   C 3 .   ? -4.57521  -31.13910 -11.22857 1.000 36.69962 ? 458 HOH   A O   1 
HETATM 1714 O O   . HOH   C 3 .   ? -5.10340  -28.31780 -21.00153 1.000 41.78495 ? 459 HOH   A O   1 
HETATM 1715 O O   . HOH   C 3 .   ? -10.65463 -14.16494 0.38794   1.000 29.77281 ? 460 HOH   A O   1 
HETATM 1716 O O   . HOH   C 3 .   ? 12.30542  -25.28918 -22.70540 1.000 24.06656 ? 461 HOH   A O   1 
HETATM 1717 O O   . HOH   C 3 .   ? -11.01256 -8.61620  -43.26833 1.000 50.20671 ? 462 HOH   A O   1 
HETATM 1718 O O   . HOH   C 3 .   ? -0.12160  -14.50992 -35.78304 1.000 21.00692 ? 463 HOH   A O   1 
HETATM 1719 O O   . HOH   C 3 .   ? 8.42200   -7.47736  -24.33230 1.000 17.38947 ? 464 HOH   A O   1 
HETATM 1720 O O   . HOH   C 3 .   ? -3.79060  -4.69962  -9.07408  1.000 33.28892 ? 465 HOH   A O   1 
HETATM 1721 O O   . HOH   C 3 .   ? 3.75727   -5.05202  -6.08751  1.000 39.75077 ? 466 HOH   A O   1 
HETATM 1722 O O   . HOH   C 3 .   ? -6.83929  -25.15631 -19.10407 1.000 18.68988 ? 467 HOH   A O   1 
HETATM 1723 O O   . HOH   C 3 .   ? -8.67214  -15.22612 -38.39068 1.000 41.12043 ? 468 HOH   A O   1 
HETATM 1724 O O   . HOH   C 3 .   ? 2.10078   -29.54748 -15.35406 1.000 36.44406 ? 469 HOH   A O   1 
HETATM 1725 O O   . HOH   C 3 .   ? 10.663    -17.177   -39.379   1.000 45.92674 ? 470 HOH   A O   1 
HETATM 1726 O O   . HOH   C 3 .   ? 3.07518   -19.90939 -2.42254  1.000 31.93982 ? 471 HOH   A O   1 
HETATM 1727 O O   . HOH   C 3 .   ? -15.07153 -3.57255  -12.42509 1.000 38.48423 ? 472 HOH   A O   1 
HETATM 1728 O O   . HOH   C 3 .   ? -8.45562  -2.58860  -18.57131 1.000 18.99351 ? 473 HOH   A O   1 
HETATM 1729 O O   . HOH   C 3 .   ? -10.078   -0.378    -16.862   1.000 40.39660 ? 474 HOH   A O   1 
HETATM 1730 O O   . HOH   C 3 .   ? -6.68307  -12.88947 -37.03733 1.000 27.31043 ? 475 HOH   A O   1 
HETATM 1731 O O   . HOH   C 3 .   ? 9.31457   -27.96271 -23.23138 1.000 30.63225 ? 476 HOH   A O   1 
HETATM 1732 O O   . HOH   C 3 .   ? -4.69807  -7.62321  -13.82241 1.000 14.24423 ? 477 HOH   A O   1 
HETATM 1733 O O   . HOH   C 3 .   ? -6.18150  -13.62149 0.50475   1.000 32.90380 ? 478 HOH   A O   1 
HETATM 1734 O O   . HOH   C 3 .   ? -6.07693  0.67560   -37.67860 1.000 26.35747 ? 479 HOH   A O   1 
HETATM 1735 O O   . HOH   C 3 .   ? -6.30806  -24.89395 -23.05754 1.000 32.05400 ? 480 HOH   A O   1 
HETATM 1736 O O   . HOH   C 3 .   ? -3.17312  -0.09455  -22.95809 1.000 30.60310 ? 481 HOH   A O   1 
HETATM 1737 O O   . HOH   C 3 .   ? 10.50474  -12.19736 -29.01793 1.000 20.90928 ? 482 HOH   A O   1 
HETATM 1738 O O   . HOH   C 3 .   ? 3.80786   -3.88371  -8.59889  1.000 47.69505 ? 483 HOH   A O   1 
HETATM 1739 O O   . HOH   C 3 .   ? -13.08090 -0.90371  -15.44710 1.000 28.83830 ? 484 HOH   A O   1 
HETATM 1740 O O   . HOH   C 3 .   ? -16.93718 -15.72003 -14.21589 1.000 31.97695 ? 485 HOH   A O   1 
HETATM 1741 O O   . HOH   C 3 .   ? 10.65448  -20.80442 -6.24351  1.000 44.66649 ? 486 HOH   A O   1 
HETATM 1742 O O   . HOH   C 3 .   ? -7.09416  -5.14616  -3.56544  1.000 42.29661 ? 487 HOH   A O   1 
HETATM 1743 O O   . HOH   C 3 .   ? 17.45940  -1.33853  -18.89723 1.000 24.46537 ? 488 HOH   A O   1 
HETATM 1744 O O   . HOH   C 3 .   ? 16.47779  -0.60484  -12.13512 1.000 31.90071 ? 489 HOH   A O   1 
HETATM 1745 O O   . HOH   C 3 .   ? 14.72206  -8.82452  -3.78604  1.000 47.01557 ? 490 HOH   A O   1 
HETATM 1746 O O   . HOH   C 3 .   ? 6.09719   -24.57090 -30.13098 1.000 20.24388 ? 491 HOH   A O   1 
HETATM 1747 O O   . HOH   C 3 .   ? 0.01182   -7.60068  -24.13459 1.000 23.97489 ? 492 HOH   A O   1 
HETATM 1748 O O   . HOH   C 3 .   ? -18.73828 -19.52812 -14.51839 1.000 22.54384 ? 493 HOH   A O   1 
HETATM 1749 O O   . HOH   C 3 .   ? -1.18053  -25.14739 -4.49469  1.000 27.58955 ? 494 HOH   A O   1 
HETATM 1750 O O   . HOH   C 3 .   ? 9.16981   -5.92634  -22.11274 1.000 28.00611 ? 495 HOH   A O   1 
HETATM 1751 O O   . HOH   C 3 .   ? 1.42426   -7.77817  -31.50134 1.000 36.17975 ? 496 HOH   A O   1 
HETATM 1752 O O   . HOH   C 3 .   ? 4.09200   -8.61080  -23.28292 1.000 40.04185 ? 497 HOH   A O   1 
HETATM 1753 O O   . HOH   C 3 .   ? 2.99881   -29.47540 -25.17452 1.000 55.39200 ? 498 HOH   A O   1 
HETATM 1754 O O   . HOH   C 3 .   ? 13.24482  -28.47467 -29.09013 1.000 31.59275 ? 499 HOH   A O   1 
HETATM 1755 O O   . HOH   C 3 .   ? 16.64578  -20.16808 -17.76743 1.000 26.08183 ? 500 HOH   A O   1 
HETATM 1756 O O   . HOH   C 3 .   ? -8.63877  -15.85365 -28.74638 1.000 32.13227 ? 501 HOH   A O   1 
HETATM 1757 O O   . HOH   C 3 .   ? -19.02474 -13.39620 -17.63068 1.000 54.04915 ? 502 HOH   A O   1 
HETATM 1758 O O   . HOH   C 3 .   ? -3.85664  -14.62496 -22.90853 1.000 19.89938 ? 503 HOH   A O   1 
HETATM 1759 O O   . HOH   C 3 .   ? -8.02474  1.09580   -26.55690 1.000 22.07559 ? 504 HOH   A O   1 
HETATM 1760 O O   . HOH   C 3 .   ? -5.55800  -11.27263 -10.70453 1.000 26.14605 ? 505 HOH   A O   1 
HETATM 1761 O O   . HOH   C 3 .   ? -0.95298  -11.15287 -26.87409 1.000 28.03491 ? 506 HOH   A O   1 
HETATM 1762 O O   . HOH   C 3 .   ? -19.68310 -28.76226 -12.09152 1.000 44.70774 ? 507 HOH   A O   1 
HETATM 1763 O O   . HOH   C 3 .   ? 5.92651   -4.67165  -2.79858  1.000 44.61276 ? 508 HOH   A O   1 
HETATM 1764 O O   . HOH   C 3 .   ? -4.99962  -14.73266 -41.44810 1.000 48.09986 ? 509 HOH   A O   1 
HETATM 1765 O O   . HOH   C 3 .   ? -13.56020 -12.00550 -30.80365 1.000 24.71991 ? 510 HOH   A O   1 
HETATM 1766 O O   . HOH   C 3 .   ? 5.02900   -9.14917  -20.05956 1.000 18.02792 ? 511 HOH   A O   1 
HETATM 1767 O O   . HOH   C 3 .   ? -16.02700 -4.60668  -30.47987 1.000 34.77818 ? 512 HOH   A O   1 
HETATM 1768 O O   . HOH   C 3 .   ? 3.79044   -30.39440 -33.34334 1.000 50.59460 ? 513 HOH   A O   1 
HETATM 1769 O O   . HOH   C 3 .   ? -15.02970 -4.32950  -16.73468 1.000 31.81068 ? 514 HOH   A O   1 
HETATM 1770 O O   . HOH   C 3 .   ? -10.78474 5.17446   -41.61117 1.000 52.31958 ? 515 HOH   A O   1 
HETATM 1771 O O   . HOH   C 3 .   ? 1.87530   -6.77324  -39.01444 1.000 43.00347 ? 516 HOH   A O   1 
HETATM 1772 O O   . HOH   C 3 .   ? 9.19701   -20.19186 -8.48443  1.000 27.30230 ? 517 HOH   A O   1 
HETATM 1773 O O   . HOH   C 3 .   ? -8.91317  -1.02807  -20.74241 1.000 21.93757 ? 518 HOH   A O   1 
HETATM 1774 O O   . HOH   C 3 .   ? -0.59609  -10.46987 -3.30810  1.000 41.90487 ? 519 HOH   A O   1 
HETATM 1775 O O   . HOH   C 3 .   ? -14.52386 -29.38028 -17.61814 1.000 33.20838 ? 520 HOH   A O   1 
HETATM 1776 O O   . HOH   C 3 .   ? -2.14654  -11.36356 -24.40795 1.000 22.05760 ? 521 HOH   A O   1 
HETATM 1777 O O   . HOH   C 3 .   ? -15.74889 -21.16527 0.88826   1.000 49.45145 ? 522 HOH   A O   1 
HETATM 1778 O O   . HOH   C 3 .   ? -13.41241 -16.61176 -3.39808  1.000 26.74848 ? 523 HOH   A O   1 
HETATM 1779 O O   . HOH   C 3 .   ? -4.60945  -8.61303  -35.09054 1.000 20.12394 ? 524 HOH   A O   1 
HETATM 1780 O O   . HOH   C 3 .   ? 9.10085   -19.99697 -3.71608  1.000 24.87816 ? 525 HOH   A O   1 
HETATM 1781 O O   . HOH   C 3 .   ? -12.15181 -29.03295 -17.35302 1.000 44.13786 ? 526 HOH   A O   1 
HETATM 1782 O O   . HOH   C 3 .   ? -3.25865  -8.33877  -43.31456 1.000 45.37608 ? 527 HOH   A O   1 
HETATM 1783 O O   . HOH   C 3 .   ? -3.12200  -19.98983 -39.48074 1.000 39.69738 ? 528 HOH   A O   1 
HETATM 1784 O O   . HOH   C 3 .   ? -15.00224 -3.60909  -22.70604 1.000 34.03677 ? 529 HOH   A O   1 
HETATM 1785 O O   . HOH   C 3 .   ? 0.01950   -10.33931 -43.82735 1.000 45.40544 ? 530 HOH   A O   1 
HETATM 1786 O O   . HOH   C 3 .   ? -10.19417 -10.98169 -2.94147  1.000 20.11014 ? 531 HOH   A O   1 
HETATM 1787 O O   . HOH   C 3 .   ? 5.81062   -30.25012 -10.89303 1.000 42.32030 ? 532 HOH   A O   1 
HETATM 1788 O O   . HOH   C 3 .   ? 0.35221   -5.19724  -34.42090 1.000 43.20850 ? 533 HOH   A O   1 
HETATM 1789 O O   . HOH   C 3 .   ? 11.85580  -14.43192 -28.32333 1.000 25.94366 ? 534 HOH   A O   1 
HETATM 1790 O O   . HOH   C 3 .   ? 12.52382  -25.68283 -25.75266 1.000 30.76958 ? 535 HOH   A O   1 
HETATM 1791 O O   . HOH   C 3 .   ? -13.72205 -7.35832  -15.41308 1.000 32.31923 ? 536 HOH   A O   1 
HETATM 1792 O O   . HOH   C 3 .   ? -16.83022 -6.97875  -26.79155 1.000 34.97610 ? 537 HOH   A O   1 
HETATM 1793 O O   . HOH   C 3 .   ? 14.96102  -20.36162 -19.79240 1.000 25.06416 ? 538 HOH   A O   1 
HETATM 1794 O O   . HOH   C 3 .   ? 15.78030  -17.75663 -2.62030  1.000 35.42925 ? 539 HOH   A O   1 
HETATM 1795 O O   . HOH   C 3 .   ? -0.57727  -32.27113 -7.52298  1.000 42.41243 ? 540 HOH   A O   1 
HETATM 1796 O O   . HOH   C 3 .   ? -15.75747 -2.99935  -9.77542  1.000 47.75705 ? 541 HOH   A O   1 
HETATM 1797 O O   . HOH   C 3 .   ? 13.78171  -27.22305 -18.50333 1.000 40.77124 ? 542 HOH   A O   1 
HETATM 1798 O O   . HOH   C 3 .   ? -13.71910 -12.55252 -8.71271  1.000 28.32151 ? 543 HOH   A O   1 
HETATM 1799 O O   . HOH   C 3 .   ? -11.82430 -1.04046  -21.32739 1.000 26.03217 ? 544 HOH   A O   1 
HETATM 1800 O O   . HOH   C 3 .   ? 4.45553   -6.83741  -18.18293 1.000 17.03713 ? 545 HOH   A O   1 
HETATM 1801 O O   . HOH   C 3 .   ? -6.70104  3.88295   -34.51356 1.000 33.85409 ? 546 HOH   A O   1 
HETATM 1802 O O   . HOH   C 3 .   ? 8.59712   -22.95626 -6.65193  1.000 43.36825 ? 547 HOH   A O   1 
HETATM 1803 O O   . HOH   C 3 .   ? 1.54253   -5.55715  -22.66416 1.000 28.42860 ? 548 HOH   A O   1 
HETATM 1804 O O   . HOH   C 3 .   ? 4.81307   -1.15117  -17.00692 1.000 46.50479 ? 549 HOH   A O   1 
HETATM 1805 O O   . HOH   C 3 .   ? -13.57023 -22.51883 -11.83363 1.000 35.98462 ? 550 HOH   A O   1 
HETATM 1806 O O   . HOH   C 3 .   ? -4.93978  -5.02682  -12.67934 1.000 33.28997 ? 551 HOH   A O   1 
HETATM 1807 O O   . HOH   C 3 .   ? 10.79073  -16.15179 -26.61919 1.000 23.81864 ? 552 HOH   A O   1 
HETATM 1808 O O   . HOH   C 3 .   ? 21.97785  -13.02896 -25.43226 1.000 45.06493 ? 553 HOH   A O   1 
HETATM 1809 O O   . HOH   C 3 .   ? 5.92724   -12.32151 -38.46636 1.000 26.76753 ? 554 HOH   A O   1 
HETATM 1810 O O   . HOH   C 3 .   ? -15.99102 -5.98531  -24.16354 1.000 25.84639 ? 555 HOH   A O   1 
HETATM 1811 O O   . HOH   C 3 .   ? -7.86466  -3.82675  -10.93935 1.000 30.79051 ? 556 HOH   A O   1 
HETATM 1812 O O   . HOH   C 3 .   ? -0.29186  -6.79821  -26.77978 1.000 30.19143 ? 557 HOH   A O   1 
HETATM 1813 O O   . HOH   C 3 .   ? 11.23718  -7.89974  -36.78772 1.000 43.11688 ? 558 HOH   A O   1 
HETATM 1814 O O   . HOH   C 3 .   ? -11.27192 -13.17784 -31.85362 1.000 27.13186 ? 559 HOH   A O   1 
HETATM 1815 O O   . HOH   C 3 .   ? 4.45902   -22.20705 -3.13380  1.000 34.45928 ? 560 HOH   A O   1 
HETATM 1816 O O   . HOH   C 3 .   ? -6.37014  1.26878   -20.75192 1.000 41.21882 ? 561 HOH   A O   1 
HETATM 1817 O O   . HOH   C 3 .   ? 3.54378   -6.59747  -21.30940 1.000 30.70416 ? 562 HOH   A O   1 
HETATM 1818 O O   . HOH   C 3 .   ? 20.47554  -3.37919  -1.71641  1.000 57.10615 ? 563 HOH   A O   1 
HETATM 1819 O O   . HOH   C 3 .   ? -1.95966  -1.50116  -25.07613 1.000 30.52247 ? 564 HOH   A O   1 
HETATM 1820 O O   . HOH   C 3 .   ? 3.93874   -17.05584 -43.67783 1.000 53.73814 ? 565 HOH   A O   1 
HETATM 1821 O O   . HOH   C 3 .   ? -14.46177 -25.35108 -11.27051 1.000 41.43112 ? 566 HOH   A O   1 
HETATM 1822 O O   . HOH   C 3 .   ? -19.65740 -14.47624 -19.82027 1.000 42.42488 ? 567 HOH   A O   1 
HETATM 1823 O O   . HOH   C 3 .   ? 20.74056  -24.39415 -20.65992 1.000 49.32218 ? 568 HOH   A O   1 
HETATM 1824 O O   . HOH   C 3 .   ? 19.19309  -18.33308 -10.46338 1.000 45.43474 ? 569 HOH   A O   1 
HETATM 1825 O O   . HOH   C 3 .   ? -2.23663  -13.35022 -21.10044 1.000 25.49858 ? 570 HOH   A O   1 
HETATM 1826 O O   . HOH   C 3 .   ? 20.65892  -6.52194  -14.66355 1.000 41.46637 ? 571 HOH   A O   1 
HETATM 1827 O O   . HOH   C 3 .   ? 11.20983  -10.83504 -4.15183  1.000 34.55653 ? 572 HOH   A O   1 
HETATM 1828 O O   . HOH   C 3 .   ? -0.44981  -9.09637  -28.16756 1.000 33.83594 ? 573 HOH   A O   1 
HETATM 1829 O O   . HOH   C 3 .   ? 0.24310   -16.34484 -3.47913  1.000 27.52588 ? 574 HOH   A O   1 
HETATM 1830 O O   . HOH   C 3 .   ? -12.75025 -16.88590 -26.86050 1.000 37.63429 ? 575 HOH   A O   1 
HETATM 1831 O O   . HOH   C 3 .   ? -13.24499 -23.78459 -5.12463  1.000 36.93286 ? 576 HOH   A O   1 
HETATM 1832 O O   . HOH   C 3 .   ? -14.90835 -12.97223 -12.79880 1.000 47.33636 ? 577 HOH   A O   1 
HETATM 1833 O O   . HOH   C 3 .   ? -7.97980  -4.69231  -7.93379  1.000 28.99972 ? 578 HOH   A O   1 
HETATM 1834 O O   . HOH   C 3 .   ? -12.92526 -1.37403  -42.59886 1.000 48.03772 ? 579 HOH   A O   1 
HETATM 1835 O O   . HOH   C 3 .   ? 3.75258   -4.14342  -18.12405 1.000 39.19181 ? 580 HOH   A O   1 
HETATM 1836 O O   . HOH   C 3 .   ? -3.51192  -3.61345  -15.99521 1.000 40.07198 ? 581 HOH   A O   1 
HETATM 1837 O O   . HOH   C 3 .   ? 2.99871   -10.08234 -40.79160 1.000 53.89597 ? 582 HOH   A O   1 
HETATM 1838 O O   . HOH   C 3 .   ? -12.36732 -19.30868 -24.94090 1.000 23.42393 ? 583 HOH   A O   1 
HETATM 1839 O O   . HOH   C 3 .   ? 18.86890  -9.69037  -9.61547  1.000 43.07844 ? 584 HOH   A O   1 
HETATM 1840 O O   . HOH   C 3 .   ? -14.65944 -0.59323  -32.11926 1.000 50.07265 ? 585 HOH   A O   1 
HETATM 1841 O O   . HOH   C 3 .   ? -0.566    -18.943   -2.081    1.000 52.79415 ? 586 HOH   A O   1 
HETATM 1842 O O   . HOH   C 3 .   ? 11.27274  -20.48735 -40.79399 1.000 51.52329 ? 587 HOH   A O   1 
HETATM 1843 O O   . HOH   C 3 .   ? -17.07255 -18.65268 -11.77025 1.000 49.61152 ? 588 HOH   A O   1 
HETATM 1844 O O   . HOH   C 3 .   ? 1.60465   -17.34394 -0.06684  1.000 41.48531 ? 589 HOH   A O   1 
HETATM 1845 O O   . HOH   C 3 .   ? -2.20159  -32.98573 -10.36749 1.000 55.46788 ? 590 HOH   A O   1 
HETATM 1846 O O   . HOH   C 3 .   ? 0.33277   -29.81385 -16.53910 1.000 41.62943 ? 591 HOH   A O   1 
HETATM 1847 O O   . HOH   C 3 .   ? 1.30546   -8.27154  -4.14246  1.000 31.62222 ? 592 HOH   A O   1 
HETATM 1848 O O   . HOH   C 3 .   ? -10.53835 -5.83657  -3.89217  1.000 44.75563 ? 593 HOH   A O   1 
HETATM 1849 O O   . HOH   C 3 .   ? 10.68690  -3.79248  -21.12572 1.000 27.51414 ? 594 HOH   A O   1 
HETATM 1850 O O   . HOH   C 3 .   ? 14.72269  -0.95792  -6.10615  1.000 37.29139 ? 595 HOH   A O   1 
HETATM 1851 O O   . HOH   C 3 .   ? 1.65810   -4.22688  -16.67343 1.000 35.27827 ? 596 HOH   A O   1 
HETATM 1852 O O   . HOH   C 3 .   ? -3.25424  -13.16534 -42.54893 1.000 47.99960 ? 597 HOH   A O   1 
HETATM 1853 O O   . HOH   C 3 .   ? 1.26221   -26.76821 -31.91928 1.000 41.86113 ? 598 HOH   A O   1 
HETATM 1854 O O   . HOH   C 3 .   ? -4.65512  -6.06589  -36.45644 1.000 23.30014 ? 599 HOH   A O   1 
HETATM 1855 O O   . HOH   C 3 .   ? 21.99760  -16.99735 -19.08621 1.000 48.07859 ? 600 HOH   A O   1 
HETATM 1856 O O   . HOH   C 3 .   ? 14.41714  -11.93028 -28.80759 1.000 34.91761 ? 601 HOH   A O   1 
HETATM 1857 O O   . HOH   C 3 .   ? 3.55885   -27.71432 -37.29817 1.000 52.46886 ? 602 HOH   A O   1 
HETATM 1858 O O   . HOH   C 3 .   ? 3.07200   -11.98940 -24.85038 1.000 40.16039 ? 603 HOH   A O   1 
HETATM 1859 O O   . HOH   C 3 .   ? -13.65273 -7.46276  -13.37083 1.000 48.13764 ? 604 HOH   A O   1 
HETATM 1860 O O   . HOH   C 3 .   ? 12.854    -18.512   -38.153   1.000 39.34328 ? 605 HOH   A O   1 
HETATM 1861 O O   . HOH   C 3 .   ? 19.12140  -0.87330  -16.66599 1.000 40.54710 ? 606 HOH   A O   1 
HETATM 1862 O O   . HOH   C 3 .   ? 13.54524  -21.88356 -3.58374  1.000 45.89528 ? 607 HOH   A O   1 
HETATM 1863 O O   . HOH   C 3 .   ? -15.06897 -14.39922 -30.22337 1.000 48.75089 ? 608 HOH   A O   1 
HETATM 1864 O O   . HOH   C 3 .   ? 0.72702   -12.61105 -21.70245 1.000 31.19758 ? 609 HOH   A O   1 
HETATM 1865 O O   . HOH   C 3 .   ? -16.23409 -5.35647  -18.67291 1.000 37.37526 ? 610 HOH   A O   1 
HETATM 1866 O O   . HOH   C 3 .   ? 1.54636   -11.48330 -23.23453 1.000 42.03085 ? 611 HOH   A O   1 
HETATM 1867 O O   . HOH   C 3 .   ? 6.34375   -21.85549 -38.21734 1.000 49.82878 ? 612 HOH   A O   1 
HETATM 1868 O O   . HOH   C 3 .   ? 14.47898  -14.00795 -25.97752 1.000 12.62353 ? 613 HOH   A O   1 
HETATM 1869 O O   . HOH   C 3 .   ? 6.88034   1.90135   -14.19977 1.000 47.41557 ? 614 HOH   A O   1 
HETATM 1870 O O   . HOH   C 3 .   ? 10.32897  -25.87788 -25.15258 1.000 38.15674 ? 615 HOH   A O   1 
HETATM 1871 O O   . HOH   C 3 .   ? 4.05824   -26.39731 -28.74943 1.000 40.68246 ? 616 HOH   A O   1 
HETATM 1872 O O   . HOH   C 3 .   ? -8.05540  2.68741   -22.30781 1.000 36.76502 ? 617 HOH   A O   1 
HETATM 1873 O O   . HOH   C 3 .   ? -15.01900 -9.10479  -14.79725 1.000 23.92098 ? 618 HOH   A O   1 
HETATM 1874 O O   . HOH   C 3 .   ? -14.15442 -31.89631 -16.11352 1.000 50.90681 ? 619 HOH   A O   1 
HETATM 1875 O O   . HOH   C 3 .   ? -8.61514  -8.05716  -41.12496 1.000 52.23170 ? 620 HOH   A O   1 
HETATM 1876 O O   . HOH   C 3 .   ? 15.71267  -22.12393 -16.05996 1.000 28.69770 ? 621 HOH   A O   1 
HETATM 1877 O O   . HOH   C 3 .   ? -17.46819 -14.80846 -28.58222 1.000 56.28177 ? 622 HOH   A O   1 
HETATM 1878 O O   . HOH   C 3 .   ? 6.811     1.812     -16.514   1.000 39.12570 ? 623 HOH   A O   1 
HETATM 1879 O O   . HOH   C 3 .   ? 20.755    -21.468   -24.628   1.000 51.65708 ? 624 HOH   A O   1 
HETATM 1880 O O   . HOH   C 3 .   ? -0.49505  -27.48007 -24.52356 1.000 42.49717 ? 625 HOH   A O   1 
HETATM 1881 O O   . HOH   C 3 .   ? -8.66941  -26.60971 -20.65698 1.000 35.66403 ? 626 HOH   A O   1 
HETATM 1882 O O   . HOH   C 3 .   ? -12.70452 -26.56690 -18.45041 1.000 28.55283 ? 627 HOH   A O   1 
HETATM 1883 O O   . HOH   C 3 .   ? -6.11831  -10.70177 0.70342   1.000 47.94312 ? 628 HOH   A O   1 
HETATM 1884 O O   . HOH   C 3 .   ? 18.98124  -21.31002 -18.66948 1.000 35.87208 ? 629 HOH   A O   1 
HETATM 1885 O O   . HOH   C 3 .   ? -4.70281  -35.14263 -12.46846 1.000 54.05932 ? 630 HOH   A O   1 
HETATM 1886 O O   . HOH   C 3 .   ? -15.08023 -7.18078  -10.65638 1.000 52.65243 ? 631 HOH   A O   1 
HETATM 1887 O O   . HOH   C 3 .   ? 13.29505  -0.62322  -19.87283 1.000 26.81966 ? 632 HOH   A O   1 
HETATM 1888 O O   . HOH   C 3 .   ? 3.08643   -3.32036  -10.94712 1.000 49.78973 ? 633 HOH   A O   1 
HETATM 1889 O O   . HOH   C 3 .   ? -19.34716 -19.07573 -11.88594 1.000 36.03364 ? 634 HOH   A O   1 
HETATM 1890 O O   . HOH   C 3 .   ? -14.70330 -2.19128  -24.64696 1.000 41.51931 ? 635 HOH   A O   1 
HETATM 1891 O O   . HOH   C 3 .   ? -2.65783  -34.31336 -13.20608 1.000 56.38774 ? 636 HOH   A O   1 
HETATM 1892 O O   . HOH   C 3 .   ? 12.56514  -0.87578  -4.30590  1.000 42.01481 ? 637 HOH   A O   1 
HETATM 1893 O O   . HOH   C 3 .   ? -13.70183 -13.98736 -3.78486  1.000 42.43082 ? 638 HOH   A O   1 
HETATM 1894 O O   . HOH   C 3 .   ? -18.42897 -11.48713 -16.24585 1.000 53.78895 ? 639 HOH   A O   1 
HETATM 1895 O O   . HOH   C 3 .   ? -7.04882  -7.04870  -40.68757 1.000 48.27809 ? 640 HOH   A O   1 
HETATM 1896 O O   . HOH   C 3 .   ? 5.60985   -24.84050 -40.83437 1.000 43.40257 ? 641 HOH   A O   1 
HETATM 1897 O O   . HOH   C 3 .   ? -0.84202  -5.05520  -12.71881 1.000 47.22010 ? 642 HOH   A O   1 
HETATM 1898 O O   . HOH   C 3 .   ? 7.83596   -30.02498 -24.25883 1.000 42.69610 ? 643 HOH   A O   1 
HETATM 1899 O O   . HOH   C 3 .   ? 5.43731   -31.09534 -5.79173  1.000 47.79088 ? 644 HOH   A O   1 
HETATM 1900 O O   . HOH   C 3 .   ? -15.619   -0.788    -19.353   1.000 29.02136 ? 645 HOH   A O   1 
HETATM 1901 O O   . HOH   C 3 .   ? 22.17127  -2.29365  -5.51969  1.000 49.09990 ? 646 HOH   A O   1 
HETATM 1902 O O   . HOH   C 3 .   ? 17.18755  0.14935   -9.39742  1.000 46.65337 ? 647 HOH   A O   1 
HETATM 1903 O O   . HOH   C 3 .   ? -10.67456 -17.37465 -28.62508 1.000 39.65356 ? 648 HOH   A O   1 
HETATM 1904 O O   . HOH   C 3 .   ? 2.35347   -2.71503  -13.38295 1.000 42.78972 ? 649 HOH   A O   1 
HETATM 1905 O O   . HOH   C 3 .   ? 20.10901  -8.27382  -17.02204 1.000 39.67634 ? 650 HOH   A O   1 
HETATM 1906 O O   . HOH   C 3 .   ? -4.17083  2.37905   -35.69794 1.000 49.46114 ? 651 HOH   A O   1 
HETATM 1907 O O   . HOH   C 3 .   ? -11.36516 -26.88393 -20.67740 1.000 30.98908 ? 652 HOH   A O   1 
HETATM 1908 O O   . HOH   C 3 .   ? 9.93844   -14.54011 -38.00829 1.000 37.25789 ? 653 HOH   A O   1 
HETATM 1909 O O   . HOH   C 3 .   ? 20.58670  -13.94614 -11.35728 1.000 48.16176 ? 654 HOH   A O   1 
HETATM 1910 O O   . HOH   C 3 .   ? 12.16456  -0.98059  -17.62587 1.000 25.02720 ? 655 HOH   A O   1 
HETATM 1911 O O   . HOH   C 3 .   ? -8.52068  -18.11181 -38.22271 1.000 51.57354 ? 656 HOH   A O   1 
HETATM 1912 O O   . HOH   C 3 .   ? -17.52290 -12.28127 -22.38131 1.000 29.19329 ? 657 HOH   A O   1 
HETATM 1913 O O   . HOH   C 3 .   ? 19.58172  -3.82494  -22.35755 1.000 44.92425 ? 658 HOH   A O   1 
HETATM 1914 O O   . HOH   C 3 .   ? -10.753   -22.197   3.921     1.000 39.69850 ? 659 HOH   A O   1 
HETATM 1915 O O   . HOH   C 3 .   ? 9.44262   -29.36009 -27.32467 1.000 50.02796 ? 660 HOH   A O   1 
HETATM 1916 O O   . HOH   C 3 .   ? -17.15038 -12.83437 -12.37154 1.000 65.92597 ? 661 HOH   A O   1 
HETATM 1917 O O   . HOH   C 3 .   ? 8.28146   -13.31988 -39.79218 1.000 37.17628 ? 662 HOH   A O   1 
HETATM 1918 O O   . HOH   C 3 .   ? -2.84443  -26.52121 -2.52367  1.000 40.40655 ? 663 HOH   A O   1 
HETATM 1919 O O   . HOH   C 3 .   ? 18.51018  -3.49849  -24.82798 1.000 42.57096 ? 664 HOH   A O   1 
HETATM 1920 O O   . HOH   C 3 .   ? -6.11396  -30.57743 -8.60595  1.000 38.34267 ? 665 HOH   A O   1 
HETATM 1921 O O   . HOH   C 3 .   ? -12.65326 -16.23392 -37.40284 1.000 49.95100 ? 666 HOH   A O   1 
HETATM 1922 O O   . HOH   C 3 .   ? -6.45429  2.86301   -25.29465 1.000 48.30598 ? 667 HOH   A O   1 
HETATM 1923 O O   . HOH   C 3 .   ? 6.26551   -9.01404  -38.80146 1.000 43.71314 ? 668 HOH   A O   1 
HETATM 1924 O O   . HOH   C 3 .   ? 10.52523  -28.91909 -15.96467 1.000 50.87182 ? 669 HOH   A O   1 
HETATM 1925 O O   . HOH   C 3 .   ? 1.63326   -27.13311 -29.85754 1.000 43.10114 ? 670 HOH   A O   1 
HETATM 1926 O O   . HOH   C 3 .   ? 14.86409  -27.00536 -16.41917 1.000 52.11774 ? 671 HOH   A O   1 
HETATM 1927 O O   . HOH   C 3 .   ? -15.50836 -1.83296  -16.71192 1.000 32.35004 ? 672 HOH   A O   1 
HETATM 1928 O O   . HOH   C 3 .   ? 7.01495   -21.32271 -2.24495  1.000 36.53040 ? 673 HOH   A O   1 
HETATM 1929 O O   . HOH   C 3 .   ? -14.20677 -9.73204  -9.93702  1.000 34.26598 ? 674 HOH   A O   1 
HETATM 1930 O O   . HOH   C 3 .   ? -19.78834 -12.12345 -21.05509 1.000 48.16308 ? 675 HOH   A O   1 
HETATM 1931 O O   . HOH   C 3 .   ? -4.59995  -17.79022 -41.60908 1.000 56.13419 ? 676 HOH   A O   1 
HETATM 1932 O O   . HOH   C 3 .   ? -14.67828 -1.24342  -13.41534 1.000 32.78851 ? 677 HOH   A O   1 
HETATM 1933 O O   . HOH   C 3 .   ? -11.65808 -15.02272 -38.91713 1.000 56.10771 ? 678 HOH   A O   1 
HETATM 1934 O O   . HOH   C 3 .   ? 17.755    1.558     -15.538   1.000 49.96083 ? 679 HOH   A O   1 
HETATM 1935 O O   . HOH   C 3 .   ? 13.96332  -11.05815 -4.45998  1.000 43.30819 ? 680 HOH   A O   1 
HETATM 1936 O O   . HOH   C 3 .   ? -8.72399  -10.73912 -0.71326  1.000 48.24441 ? 681 HOH   A O   1 
HETATM 1937 O O   . HOH   C 3 .   ? -10.53885 -21.27878 -25.68992 1.000 37.75088 ? 682 HOH   A O   1 
HETATM 1938 O O   . HOH   C 3 .   ? -19.69144 -13.41274 -25.93786 1.000 49.48938 ? 683 HOH   A O   1 
HETATM 1939 O O   . HOH   C 3 .   ? 1.01758   -1.54075  -16.74940 1.000 56.55455 ? 684 HOH   A O   1 
HETATM 1940 O O   . HOH   C 3 .   ? -14.21343 -9.08274  -11.95663 1.000 44.27318 ? 685 HOH   A O   1 
HETATM 1941 O O   . HOH   C 3 .   ? 10.75609  -25.21117 -13.82763 1.000 44.79053 ? 686 HOH   A O   1 
HETATM 1942 O O   . HOH   C 3 .   ? 14.01501  -24.90794 -14.72371 1.000 40.16279 ? 687 HOH   A O   1 
HETATM 1943 O O   . HOH   C 3 .   ? 10.87018  -30.04885 -29.50578 1.000 47.06052 ? 688 HOH   A O   1 
HETATM 1944 O O   . HOH   C 3 .   ? 19.11599  -1.39229  -21.06798 1.000 36.77003 ? 689 HOH   A O   1 
HETATM 1945 O O   . HOH   C 3 .   ? -15.87654 -12.21136 -7.17117  1.000 41.45424 ? 690 HOH   A O   1 
HETATM 1946 O O   . HOH   C 3 .   ? -6.848    -22.658   -2.225    1.000 41.99262 ? 691 HOH   A O   1 
HETATM 1947 O O   . HOH   C 3 .   ? -16.66712 -4.85675  -14.13984 1.000 43.04624 ? 692 HOH   A O   1 
HETATM 1948 O O   . HOH   C 3 .   ? 6.28500   -6.07699  -24.62285 1.000 26.35051 ? 693 HOH   A O   1 
HETATM 1949 O O   . HOH   C 3 .   ? 4.17476   -2.66598  -20.09719 1.000 45.07539 ? 694 HOH   A O   1 
HETATM 1950 O O   . HOH   C 3 .   ? -12.24853 -12.63702 -1.88741  1.000 34.37389 ? 695 HOH   A O   1 
HETATM 1951 O O   . HOH   C 3 .   ? 14.63399  -12.57218 -2.04701  1.000 47.82182 ? 696 HOH   A O   1 
HETATM 1952 O O   . HOH   C 3 .   ? 18.48034  0.40401   -22.89407 1.000 43.45828 ? 697 HOH   A O   1 
HETATM 1953 O O   . HOH   C 3 .   ? -13.80198 -14.06852 -11.44848 1.000 43.25321 ? 698 HOH   A O   1 
HETATM 1954 O O   . HOH   C 3 .   ? -16.14602 -19.05002 -0.49670  1.000 53.72223 ? 699 HOH   A O   1 
HETATM 1955 O O   . HOH   C 3 .   ? -10.634   -11.324   1.320     1.000 39.59781 ? 700 HOH   A O   1 
HETATM 1956 O O   . HOH   C 3 .   ? -18.33268 -5.89096  -22.93753 1.000 44.27325 ? 701 HOH   A O   1 
HETATM 1957 O O   . HOH   C 3 .   ? -7.60314  -32.64146 -8.15066  1.000 47.95566 ? 702 HOH   A O   1 
HETATM 1958 O O   . HOH   C 3 .   ? -1.68534  -26.88183 -27.05328 1.000 46.09792 ? 703 HOH   A O   1 
HETATM 1959 O O   . HOH   C 3 .   ? 22.558    -20.304   -26.024   1.000 43.82948 ? 704 HOH   A O   1 
HETATM 1960 O O   . HOH   C 3 .   ? 8.51882   -8.46030  -39.48330 1.000 45.57402 ? 705 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   ? 0.68669 0.72564 0.58216 -0.05306 -0.02771 -0.23287 16  GLU A N   
2    C CA  . GLU A 9   ? 0.62847 0.63974 0.52110 -0.01667 -0.02718 -0.19836 16  GLU A CA  
3    C C   . GLU A 9   ? 0.63043 0.65061 0.55184 -0.00827 -0.02980 -0.17390 16  GLU A C   
4    O O   . GLU A 9   ? 0.57144 0.64500 0.51685 -0.00303 -0.04258 -0.17218 16  GLU A O   
5    C CB  . GLU A 9   ? 0.69765 0.74609 0.58545 0.01259  -0.04017 -0.19324 16  GLU A CB  
6    C CG  . GLU A 9   ? 0.95800 1.01128 0.85847 0.04497  -0.04396 -0.15909 16  GLU A CG  
7    C CD  . GLU A 9   ? 1.11188 1.11607 0.99632 0.06220  -0.03183 -0.13853 16  GLU A CD  
8    O OE1 . GLU A 9   ? 1.20772 1.16362 1.07324 0.05244  -0.01874 -0.14417 16  GLU A OE1 
9    O OE2 . GLU A 9   ? 1.03465 1.04866 0.92313 0.08613  -0.03359 -0.11670 16  GLU A OE2 
10   N N   . VAL A 10  ? 0.54929 0.51707 0.46443 -0.00429 -0.01721 -0.15540 17  VAL A N   
11   C CA  . VAL A 10  ? 0.48480 0.45524 0.42280 0.00026  -0.01808 -0.13504 17  VAL A CA  
12   C C   . VAL A 10  ? 0.45872 0.41958 0.39775 0.02921  -0.01841 -0.10756 17  VAL A C   
13   O O   . VAL A 10  ? 0.48862 0.41387 0.40660 0.04074  -0.00876 -0.10105 17  VAL A O   
14   C CB  . VAL A 10  ? 0.46291 0.38626 0.39123 -0.01959 -0.00248 -0.13750 17  VAL A CB  
15   C CG1 . VAL A 10  ? 0.38610 0.31439 0.33594 -0.01141 -0.00452 -0.11564 17  VAL A CG1 
16   C CG2 . VAL A 10  ? 0.53308 0.46269 0.45762 -0.05581 0.00265  -0.16818 17  VAL A CG2 
17   N N   . GLU A 11  ? 0.31695 0.30911 0.27796 0.04033  -0.02753 -0.09256 18  GLU A N   
18   C CA  . GLU A 11  ? 0.30027 0.28770 0.26485 0.05985  -0.02576 -0.06937 18  GLU A CA  
19   C C   . GLU A 11  ? 0.28167 0.26150 0.26126 0.05586  -0.02343 -0.05666 18  GLU A C   
20   O O   . GLU A 11  ? 0.26748 0.25961 0.26070 0.04458  -0.02782 -0.06035 18  GLU A O   
21   C CB  . GLU A 11  ? 0.28387 0.30061 0.25322 0.07439  -0.03313 -0.06101 18  GLU A CB  
22   C CG  . GLU A 11  ? 0.31576 0.34422 0.26675 0.08405  -0.03625 -0.07157 18  GLU A CG  
23   C CD  . GLU A 11  ? 0.49335 0.54392 0.44115 0.10224  -0.04089 -0.06106 18  GLU A CD  
24   O OE1 . GLU A 11  ? 0.44148 0.51622 0.39491 0.10399  -0.04872 -0.06466 18  GLU A OE1 
25   O OE2 . GLU A 11  ? 0.59636 0.63872 0.53173 0.11670  -0.03489 -0.04942 18  GLU A OE2 
26   N N   . THR A 12  ? 0.28419 0.24894 0.26025 0.06689  -0.01666 -0.04277 19  THR A N   
27   C CA  . THR A 12  ? 0.27957 0.24304 0.26737 0.06622  -0.01533 -0.03122 19  THR A CA  
28   C C   . THR A 12  ? 0.28404 0.27371 0.28724 0.07384  -0.01822 -0.01693 19  THR A C   
29   O O   . THR A 12  ? 0.27049 0.26849 0.26980 0.08504  -0.01476 -0.01109 19  THR A O   
30   C CB  . THR A 12  ? 0.29856 0.23030 0.26736 0.07486  -0.00455 -0.02759 19  THR A CB  
31   O OG1 . THR A 12  ? 0.33442 0.22973 0.28074 0.06354  0.00310  -0.04284 19  THR A OG1 
32   C CG2 . THR A 12  ? 0.28788 0.22189 0.26554 0.07575  -0.00440 -0.01750 19  THR A CG2 
33   N N   . PHE A 13  ? 0.25241 0.25317 0.27094 0.06575  -0.02240 -0.01239 20  PHE A N   
34   C CA  . PHE A 13  ? 0.26424 0.28460 0.29466 0.06490  -0.02296 -0.00262 20  PHE A CA  
35   C C   . PHE A 13  ? 0.25599 0.28515 0.29720 0.06069  -0.02360 0.00252  20  PHE A C   
36   O O   . PHE A 13  ? 0.27333 0.29078 0.31348 0.05709  -0.02542 -0.00057 20  PHE A O   
37   C CB  . PHE A 13  ? 0.22202 0.24354 0.25322 0.05924  -0.02655 -0.00385 20  PHE A CB  
38   C CG  . PHE A 13  ? 0.21669 0.23696 0.23520 0.06695  -0.02834 -0.00999 20  PHE A CG  
39   C CD1 . PHE A 13  ? 0.22932 0.25063 0.24516 0.06457  -0.03354 -0.02304 20  PHE A CD1 
40   C CD2 . PHE A 13  ? 0.32971 0.35122 0.33767 0.07557  -0.02395 -0.00384 20  PHE A CD2 
41   C CE1 . PHE A 13  ? 0.27180 0.30357 0.27641 0.07220  -0.03727 -0.03166 20  PHE A CE1 
42   C CE2 . PHE A 13  ? 0.27813 0.30209 0.27054 0.08692  -0.02666 -0.00941 20  PHE A CE2 
43   C CZ  . PHE A 13  ? 0.27527 0.30840 0.26714 0.08586  -0.03475 -0.02416 20  PHE A CZ  
44   N N   . ALA A 14  ? 0.19634 0.24959 0.24736 0.05948  -0.02145 0.00905  21  ALA A N   
45   C CA  . ALA A 14  ? 0.20596 0.27771 0.26846 0.05246  -0.02403 0.01106  21  ALA A CA  
46   C C   . ALA A 14  ? 0.21630 0.27996 0.28183 0.03572  -0.02602 0.00868  21  ALA A C   
47   O O   . ALA A 14  ? 0.22534 0.28074 0.28591 0.03002  -0.02182 0.00946  21  ALA A O   
48   C CB  . ALA A 14  ? 0.20306 0.31549 0.27670 0.05489  -0.02069 0.01518  21  ALA A CB  
49   N N   . PHE A 15  ? 0.20314 0.26345 0.27096 0.03062  -0.03056 0.00656  22  PHE A N   
50   C CA  . PHE A 15  ? 0.23696 0.29069 0.30465 0.01592  -0.03090 0.00433  22  PHE A CA  
51   C C   . PHE A 15  ? 0.22325 0.29909 0.29733 0.00178  -0.02600 0.00419  22  PHE A C   
52   O O   . PHE A 15  ? 0.26544 0.37734 0.35102 0.00395  -0.02617 0.00490  22  PHE A O   
53   C CB  . PHE A 15  ? 0.25410 0.30656 0.32291 0.01389  -0.03610 0.00198  22  PHE A CB  
54   C CG  . PHE A 15  ? 0.23691 0.26734 0.29970 0.01933  -0.03780 -0.00020 22  PHE A CG  
55   C CD1 . PHE A 15  ? 0.26516 0.28029 0.32219 0.01728  -0.03753 -0.00292 22  PHE A CD1 
56   C CD2 . PHE A 15  ? 0.23378 0.25949 0.29374 0.02702  -0.03760 0.00011  22  PHE A CD2 
57   C CE1 . PHE A 15  ? 0.20916 0.21811 0.26513 0.02048  -0.03906 -0.00737 22  PHE A CE1 
58   C CE2 . PHE A 15  ? 0.28039 0.28918 0.33604 0.02555  -0.03635 -0.00439 22  PHE A CE2 
59   C CZ  . PHE A 15  ? 0.22336 0.23050 0.28078 0.02103  -0.03805 -0.00920 22  PHE A CZ  
60   N N   . GLN A 16  ? 0.24038 0.29520 0.30445 -0.01284 -0.01982 0.00245  23  GLN A N   
61   C CA  . GLN A 16  ? 0.32957 0.40166 0.39769 -0.03571 -0.01315 -0.00205 23  GLN A CA  
62   C C   . GLN A 16  ? 0.31409 0.42236 0.39623 -0.04167 -0.02180 -0.00824 23  GLN A C   
63   O O   . GLN A 16  ? 0.24210 0.34058 0.32141 -0.03232 -0.02977 -0.00838 23  GLN A O   
64   C CB  . GLN A 16  ? 0.32961 0.35626 0.37427 -0.05027 -0.00279 -0.00384 23  GLN A CB  
65   C CG  . GLN A 16  ? 0.63879 0.64379 0.66817 -0.05422 0.01192  0.00091  23  GLN A CG  
66   C CD  . GLN A 16  ? 0.57446 0.52047 0.56952 -0.05611 0.02292  0.00265  23  GLN A CD  
67   O OE1 . GLN A 16  ? 0.74381 0.66116 0.71845 -0.07732 0.04020  0.00078  23  GLN A OE1 
68   N NE2 . GLN A 16  ? 0.54827 0.47486 0.53412 -0.03506 0.01454  0.00501  23  GLN A NE2 
69   N N   . ALA A 17  ? 0.28254 0.43745 0.37910 -0.05750 -0.01953 -0.01423 24  ALA A N   
70   C CA  . ALA A 17  ? 0.30752 0.51103 0.41733 -0.05750 -0.02963 -0.02053 24  ALA A CA  
71   C C   . ALA A 17  ? 0.35740 0.53594 0.45524 -0.06892 -0.03343 -0.02736 24  ALA A C   
72   O O   . ALA A 17  ? 0.30616 0.49768 0.40449 -0.05466 -0.04361 -0.02697 24  ALA A O   
73   C CB  . ALA A 17  ? 0.32116 0.59037 0.45023 -0.07701 -0.02622 -0.02971 24  ALA A CB  
74   N N   . GLU A 18  ? 0.25325 0.39003 0.33461 -0.09232 -0.02323 -0.03284 25  GLU A N   
75   C CA  . GLU A 18  ? 0.25987 0.36847 0.32496 -0.10319 -0.02460 -0.04034 25  GLU A CA  
76   C C   . GLU A 18  ? 0.26443 0.34047 0.32042 -0.07716 -0.03156 -0.03176 25  GLU A C   
77   O O   . GLU A 18  ? 0.26409 0.33912 0.31475 -0.07538 -0.03791 -0.03572 25  GLU A O   
78   C CB  . GLU A 18  ? 0.43251 0.48798 0.47168 -0.12887 -0.00775 -0.04598 25  GLU A CB  
79   C CG  . GLU A 18  ? 0.51263 0.59565 0.55718 -0.16559 0.00342  -0.05885 25  GLU A CG  
80   C CD  . GLU A 18  ? 0.66191 0.75818 0.71647 -0.16502 0.01288  -0.05145 25  GLU A CD  
81   O OE1 . GLU A 18  ? 0.54836 0.63449 0.60558 -0.13423 0.00855  -0.03694 25  GLU A OE1 
82   O OE2 . GLU A 18  ? 0.64048 0.75908 0.69955 -0.19757 0.02566  -0.06171 25  GLU A OE2 
83   N N   . ILE A 19  ? 0.26391 0.31601 0.31745 -0.05851 -0.02963 -0.02150 26  ILE A N   
84   C CA  . ILE A 19  ? 0.24581 0.27452 0.29334 -0.03894 -0.03441 -0.01637 26  ILE A CA  
85   C C   . ILE A 19  ? 0.27793 0.33481 0.33789 -0.02392 -0.04320 -0.01332 26  ILE A C   
86   O O   . ILE A 19  ? 0.22230 0.26924 0.27695 -0.01673 -0.04650 -0.01300 26  ILE A O   
87   C CB  . ILE A 19  ? 0.29304 0.29506 0.33319 -0.02586 -0.02988 -0.00995 26  ILE A CB  
88   C CG1 . ILE A 19  ? 0.37080 0.33057 0.38560 -0.03079 -0.01941 -0.01021 26  ILE A CG1 
89   C CG2 . ILE A 19  ? 0.22855 0.22506 0.27020 -0.00924 -0.03527 -0.00788 26  ILE A CG2 
90   C CD1 . ILE A 19  ? 0.58339 0.53347 0.58864 -0.05135 -0.00774 -0.01267 26  ILE A CD1 
91   N N   . ALA A 20  ? 0.20752 0.29570 0.27952 -0.01659 -0.04473 -0.01009 27  ALA A N   
92   C CA  . ALA A 20  ? 0.23704 0.34379 0.31064 0.00212  -0.04981 -0.00571 27  ALA A CA  
93   C C   . ALA A 20  ? 0.23551 0.36611 0.30699 -0.00041 -0.05590 -0.01037 27  ALA A C   
94   O O   . ALA A 20  ? 0.20878 0.33148 0.27025 0.01418  -0.05799 -0.00642 27  ALA A O   
95   C CB  . ALA A 20  ? 0.24111 0.37824 0.32264 0.01490  -0.04895 -0.00121 27  ALA A CB  
96   N N   . GLN A 21  ? 0.18988 0.34941 0.26807 -0.02028 -0.05740 -0.01986 28  GLN A N   
97   C CA  . GLN A 21  ? 0.19892 0.38507 0.27384 -0.02651 -0.06419 -0.02827 28  GLN A CA  
98   C C   . GLN A 21  ? 0.24167 0.38360 0.29957 -0.02848 -0.06361 -0.02930 28  GLN A C   
99   O O   . GLN A 21  ? 0.21226 0.36269 0.26136 -0.01782 -0.06896 -0.02924 28  GLN A O   
100  C CB  . GLN A 21  ? 0.24667 0.46736 0.33116 -0.05655 -0.06284 -0.04251 28  GLN A CB  
101  C CG  . GLN A 21  ? 0.51837 0.78710 0.60400 -0.06698 -0.07115 -0.05591 28  GLN A CG  
102  C CD  . GLN A 21  ? 0.65409 0.97146 0.75520 -0.09883 -0.06792 -0.07141 28  GLN A CD  
103  O OE1 . GLN A 21  ? 0.45757 0.75176 0.56143 -0.11672 -0.05605 -0.07123 28  GLN A OE1 
104  N NE2 . GLN A 21  ? 0.58600 0.95664 0.69043 -0.10173 -0.07319 -0.08183 28  GLN A NE2 
105  N N   . LEU A 22  ? 0.24113 0.33715 0.29130 -0.03868 -0.05630 -0.02961 29  LEU A N   
106  C CA  . LEU A 22  ? 0.24429 0.30316 0.27826 -0.03660 -0.05475 -0.03020 29  LEU A CA  
107  C C   . LEU A 22  ? 0.24028 0.29014 0.27353 -0.01486 -0.05567 -0.02069 29  LEU A C   
108  O O   . LEU A 22  ? 0.24725 0.28995 0.27008 -0.00936 -0.05673 -0.02085 29  LEU A O   
109  C CB  . LEU A 22  ? 0.27189 0.28667 0.29388 -0.04393 -0.04572 -0.03074 29  LEU A CB  
110  C CG  . LEU A 22  ? 0.33960 0.32144 0.34607 -0.03429 -0.04326 -0.02947 29  LEU A CG  
111  C CD1 . LEU A 22  ? 0.33912 0.31604 0.32988 -0.04364 -0.04454 -0.03843 29  LEU A CD1 
112  C CD2 . LEU A 22  ? 0.34403 0.28869 0.33688 -0.02978 -0.03449 -0.02674 29  LEU A CD2 
113  N N   . MET A 23  ? 0.19739 0.24347 0.23858 -0.00445 -0.05310 -0.01339 30  MET A N   
114  C CA  . MET A 23  ? 0.25065 0.28165 0.28702 0.00939  -0.05004 -0.00726 30  MET A CA  
115  C C   . MET A 23  ? 0.21003 0.25526 0.23741 0.02305  -0.05181 -0.00266 30  MET A C   
116  O O   . MET A 23  ? 0.26469 0.29187 0.27922 0.03032  -0.04736 0.00080  30  MET A O   
117  C CB  . MET A 23  ? 0.29070 0.31024 0.33261 0.01464  -0.04533 -0.00360 30  MET A CB  
118  C CG  . MET A 23  ? 0.24977 0.25819 0.29651 0.00848  -0.04366 -0.00691 30  MET A CG  
119  S SD  . MET A 23  ? 0.24420 0.25493 0.29802 0.01238  -0.04191 -0.00531 30  MET A SD  
120  C CE  . MET A 23  ? 0.22088 0.21733 0.27034 0.01613  -0.03629 -0.00631 30  MET A CE  
121  N N   . SER A 24  ? 0.21496 0.29502 0.24645 0.02861  -0.05710 -0.00238 31  SER A N   
122  C CA  . SER A 24  ? 0.25116 0.35056 0.26881 0.04842  -0.05965 0.00251  31  SER A CA  
123  C C   . SER A 24  ? 0.29728 0.40247 0.30489 0.04381  -0.06431 -0.00312 31  SER A C   
124  O O   . SER A 24  ? 0.26862 0.36383 0.25596 0.06100  -0.06179 0.00325  31  SER A O   
125  C CB  . SER A 24  ? 0.27101 0.42162 0.29783 0.05749  -0.06573 0.00209  31  SER A CB  
126  O OG  . SER A 24  ? 0.47125 0.64907 0.48186 0.08134  -0.06977 0.00624  31  SER A OG  
127  N N   . LEU A 25  ? 0.23299 0.34867 0.24906 0.02102  -0.06905 -0.01513 32  LEU A N   
128  C CA  . LEU A 25  ? 0.24200 0.35819 0.24449 0.01564  -0.07270 -0.02247 32  LEU A CA  
129  C C   . LEU A 25  ? 0.29091 0.36148 0.27975 0.02146  -0.06459 -0.01652 32  LEU A C   
130  O O   . LEU A 25  ? 0.30084 0.36852 0.27198 0.03190  -0.06449 -0.01470 32  LEU A O   
131  C CB  . LEU A 25  ? 0.24630 0.36789 0.25364 -0.01305 -0.07492 -0.03783 32  LEU A CB  
132  C CG  . LEU A 25  ? 0.41134 0.52701 0.40107 -0.02407 -0.07741 -0.04948 32  LEU A CG  
133  C CD1 . LEU A 25  ? 0.39207 0.52981 0.38519 -0.05476 -0.07960 -0.06783 32  LEU A CD1 
134  C CD2 . LEU A 25  ? 0.33185 0.39189 0.30793 -0.02339 -0.06861 -0.04619 32  LEU A CD2 
135  N N   . ILE A 26  ? 0.23641 0.27660 0.23294 0.01535  -0.05741 -0.01422 33  ILE A N   
136  C CA  . ILE A 26  ? 0.24053 0.25033 0.22919 0.01870  -0.04915 -0.01094 33  ILE A CA  
137  C C   . ILE A 26  ? 0.35379 0.35355 0.33119 0.03412  -0.04175 -0.00088 33  ILE A C   
138  O O   . ILE A 26  ? 0.32149 0.30595 0.28455 0.03846  -0.03512 0.00154  33  ILE A O   
139  C CB  . ILE A 26  ? 0.25945 0.25302 0.26032 0.01165  -0.04440 -0.01211 33  ILE A CB  
140  C CG1 . ILE A 26  ? 0.28588 0.27139 0.28293 0.00083  -0.04628 -0.02010 33  ILE A CG1 
141  C CG2 . ILE A 26  ? 0.29342 0.27173 0.29299 0.01552  -0.03499 -0.00944 33  ILE A CG2 
142  C CD1 . ILE A 26  ? 0.28189 0.25508 0.28582 0.00024  -0.04238 -0.01964 33  ILE A CD1 
143  N N   . ILE A 27  ? 0.30734 0.31029 0.28599 0.04333  -0.04012 0.00550  34  ILE A N   
144  C CA  . ILE A 27  ? 0.32201 0.29987 0.28042 0.05807  -0.02811 0.01564  34  ILE A CA  
145  C C   . ILE A 27  ? 0.35265 0.33954 0.28541 0.07903  -0.02981 0.02203  34  ILE A C   
146  O O   . ILE A 27  ? 0.41079 0.36774 0.31720 0.09019  -0.01724 0.03021  34  ILE A O   
147  C CB  . ILE A 27  ? 0.41872 0.38864 0.38014 0.06309  -0.02382 0.01975  34  ILE A CB  
148  C CG1 . ILE A 27  ? 0.30175 0.25890 0.28184 0.04443  -0.01958 0.01329  34  ILE A CG1 
149  C CG2 . ILE A 27  ? 0.44955 0.38581 0.37802 0.08310  -0.00929 0.03125  34  ILE A CG2 
150  C CD1 . ILE A 27  ? 0.33793 0.29909 0.32704 0.04584  -0.02104 0.01328  34  ILE A CD1 
151  N N   . ASN A 28  ? 0.30618 0.33673 0.24415 0.08425  -0.04421 0.01754  35  ASN A N   
152  C CA  . ASN A 28  ? 0.34947 0.40263 0.26290 0.10987  -0.04830 0.02292  35  ASN A CA  
153  C C   . ASN A 28  ? 0.39709 0.46790 0.30195 0.10590  -0.05615 0.01498  35  ASN A C   
154  O O   . ASN A 28  ? 0.41628 0.50019 0.29423 0.13004  -0.05774 0.02036  35  ASN A O   
155  C CB  . ASN A 28  ? 0.35327 0.45839 0.27774 0.12105  -0.05946 0.02121  35  ASN A CB  
156  C CG  . ASN A 28  ? 0.54447 0.62695 0.46453 0.13558  -0.04947 0.03195  35  ASN A CG  
157  O OD1 . ASN A 28  ? 0.58357 0.61171 0.47803 0.14683  -0.03318 0.04288  35  ASN A OD1 
158  N ND2 . ASN A 28  ? 0.49553 0.61197 0.43998 0.12959  -0.05639 0.02715  35  ASN A ND2 
159  N N   . THR A 29  ? 0.36821 0.43620 0.28915 0.07961  -0.05991 0.00279  36  THR A N   
160  C CA  . THR A 29  ? 0.39638 0.47606 0.30435 0.07543  -0.06630 -0.00653 36  THR A CA  
161  C C   . THR A 29  ? 0.40870 0.44839 0.29251 0.08566  -0.05350 0.00218  36  THR A C   
162  O O   . THR A 29  ? 0.41153 0.41464 0.30090 0.07817  -0.04059 0.00705  36  THR A O   
163  C CB  . THR A 29  ? 0.43480 0.51492 0.35922 0.04558  -0.07131 -0.02263 36  THR A CB  
164  O OG1 . THR A 29  ? 0.35280 0.46970 0.29724 0.03263  -0.08008 -0.03126 36  THR A OG1 
165  C CG2 . THR A 29  ? 0.35542 0.44077 0.26068 0.03996  -0.07639 -0.03449 36  THR A CG2 
166  N N   . PHE A 30  ? 0.37452 0.42677 0.23147 0.10208  -0.05678 0.00282  37  PHE A N   
167  C CA  . PHE A 30  ? 0.42494 0.44072 0.25734 0.10951  -0.04350 0.00985  37  PHE A CA  
168  C C   . PHE A 30  ? 0.40452 0.40882 0.24647 0.08739  -0.04377 -0.00247 37  PHE A C   
169  O O   . PHE A 30  ? 0.40575 0.43153 0.24634 0.07738  -0.05597 -0.01723 37  PHE A O   
170  C CB  . PHE A 30  ? 0.43563 0.46742 0.23161 0.13670  -0.04676 0.01447  37  PHE A CB  
171  C CG  . PHE A 30  ? 0.52739 0.51914 0.29388 0.14603  -0.03020 0.02365  37  PHE A CG  
172  C CD1 . PHE A 30  ? 0.53347 0.47935 0.28038 0.15823  -0.00787 0.04149  37  PHE A CD1 
173  C CD2 . PHE A 30  ? 0.47425 0.46979 0.23010 0.14011  -0.03406 0.01356  37  PHE A CD2 
174  C CE1 . PHE A 30  ? 0.64666 0.55594 0.36583 0.16342  0.01087  0.04966  37  PHE A CE1 
175  C CE2 . PHE A 30  ? 0.51261 0.47370 0.24131 0.14919  -0.01707 0.02246  37  PHE A CE2 
176  C CZ  . PHE A 30  ? 0.52724 0.44723 0.23901 0.16000  0.00582  0.04077  37  PHE A CZ  
177  N N   . TYR A 31  ? 0.38035 0.35170 0.22918 0.08004  -0.02910 0.00235  38  TYR A N   
178  C CA  . TYR A 31  ? 0.37460 0.33583 0.23141 0.06526  -0.02780 -0.00758 38  TYR A CA  
179  C C   . TYR A 31  ? 0.37969 0.31723 0.23593 0.06645  -0.00915 0.00033  38  TYR A C   
180  O O   . TYR A 31  ? 0.36136 0.29289 0.23667 0.05951  -0.00102 0.00453  38  TYR A O   
181  C CB  . TYR A 31  ? 0.36725 0.33396 0.25046 0.04817  -0.03479 -0.01602 38  TYR A CB  
182  C CG  . TYR A 31  ? 0.35733 0.30727 0.23848 0.04012  -0.03171 -0.02467 38  TYR A CG  
183  C CD1 . TYR A 31  ? 0.38557 0.33177 0.24578 0.03618  -0.03740 -0.03639 38  TYR A CD1 
184  C CD2 . TYR A 31  ? 0.36816 0.30733 0.26449 0.03848  -0.02258 -0.02215 38  TYR A CD2 
185  C CE1 . TYR A 31  ? 0.53615 0.45772 0.38467 0.03325  -0.03209 -0.04358 38  TYR A CE1 
186  C CE2 . TYR A 31  ? 0.41750 0.34161 0.30504 0.03922  -0.01887 -0.02868 38  TYR A CE2 
187  C CZ  . TYR A 31  ? 0.47087 0.38064 0.33155 0.03758  -0.02271 -0.03856 38  TYR A CZ  
188  O OH  . TYR A 31  ? 0.54566 0.42983 0.38762 0.04148  -0.01669 -0.04483 38  TYR A OH  
189  N N   . SER A 32  ? 0.40019 0.32824 0.23459 0.07366  -0.00160 0.00088  39  SER A N   
190  C CA  . SER A 32  ? 0.41037 0.32269 0.24316 0.07359  0.01898  0.00860  39  SER A CA  
191  C C   . SER A 32  ? 0.39403 0.31350 0.25172 0.06237  0.02410  0.00171  39  SER A C   
192  O O   . SER A 32  ? 0.43691 0.35731 0.30649 0.05549  0.04004  0.00503  39  SER A O   
193  C CB  . SER A 32  ? 0.44732 0.34869 0.24523 0.08771  0.02760  0.01324  39  SER A CB  
194  O OG  . SER A 32  ? 0.47301 0.36990 0.24342 0.10431  0.02499  0.02196  39  SER A OG  
195  N N   . ASN A 33  ? 0.37887 0.30394 0.24199 0.06067  0.01253  -0.00838 40  ASN A N   
196  C CA  . ASN A 33  ? 0.37691 0.30861 0.25393 0.05990  0.01766  -0.01365 40  ASN A CA  
197  C C   . ASN A 33  ? 0.34027 0.28599 0.24849 0.05102  0.01592  -0.01430 40  ASN A C   
198  O O   . ASN A 33  ? 0.34765 0.29475 0.26292 0.05220  0.00929  -0.01965 40  ASN A O   
199  C CB  . ASN A 33  ? 0.38589 0.30372 0.24315 0.06548  0.00995  -0.02298 40  ASN A CB  
200  C CG  . ASN A 33  ? 0.39913 0.31920 0.26061 0.07407  0.01662  -0.02646 40  ASN A CG  
201  O OD1 . ASN A 33  ? 0.40920 0.34996 0.28202 0.07984  0.02859  -0.02346 40  ASN A OD1 
202  N ND2 . ASN A 33  ? 0.44502 0.34428 0.29396 0.07595  0.01066  -0.03319 40  ASN A ND2 
203  N N   . LYS A 34  ? 0.26809 0.21546 0.17016 0.02832  -0.02360 0.00135  41  LYS A N   
204  C CA  . LYS A 34  ? 0.25296 0.22635 0.19048 0.02202  -0.01487 0.00255  41  LYS A CA  
205  C C   . LYS A 34  ? 0.28763 0.25722 0.22942 0.02109  -0.00464 -0.00297 41  LYS A C   
206  O O   . LYS A 34  ? 0.24739 0.23151 0.21080 0.01477  -0.00315 -0.00400 41  LYS A O   
207  C CB  . LYS A 34  ? 0.24262 0.22419 0.19055 0.02949  -0.00392 0.00698  41  LYS A CB  
208  C CG  . LYS A 34  ? 0.28487 0.28173 0.23536 0.03516  -0.01198 0.01500  41  LYS A CG  
209  C CD  . LYS A 34  ? 0.38771 0.37487 0.33144 0.04820  -0.00334 0.01768  41  LYS A CD  
210  C CE  . LYS A 34  ? 0.35353 0.35977 0.29763 0.06008  -0.00955 0.02728  41  LYS A CE  
211  N NZ  . LYS A 34  ? 0.36225 0.40448 0.32574 0.06943  -0.00900 0.03493  41  LYS A NZ  
212  N N   . GLU A 35  ? 0.27512 0.23008 0.19569 0.03092  0.00342  -0.00391 42  GLU A N   
213  C CA  . GLU A 35  ? 0.25013 0.21412 0.18209 0.03210  0.01533  -0.00326 42  GLU A CA  
214  C C   . GLU A 35  ? 0.32820 0.28879 0.26353 0.02556  0.00703  -0.01083 42  GLU A C   
215  O O   . GLU A 35  ? 0.29016 0.26333 0.24212 0.02403  0.01526  -0.01007 42  GLU A O   
216  C CB  . GLU A 35  ? 0.28926 0.24991 0.19681 0.05118  0.02774  0.00327  42  GLU A CB  
217  C CG  . GLU A 35  ? 0.33715 0.26244 0.19554 0.06766  0.01740  -0.00637 42  GLU A CG  
218  C CD  . GLU A 35  ? 0.51844 0.43894 0.33856 0.09957  0.03285  0.00151  42  GLU A CD  
219  O OE1 . GLU A 35  ? 0.45994 0.39845 0.28464 0.10561  0.04523  0.01459  42  GLU A OE1 
220  O OE2 . GLU A 35  ? 0.62781 0.52576 0.40893 0.12216  0.03292  -0.00348 42  GLU A OE2 
221  N N   . ILE A 36  ? 0.27959 0.22397 0.20085 0.01882  -0.01197 -0.01473 43  ILE A N   
222  C CA  . ILE A 36  ? 0.24595 0.18336 0.16843 0.00967  -0.02285 -0.01798 43  ILE A CA  
223  C C   . ILE A 36  ? 0.26222 0.23255 0.22445 -0.00089 -0.01653 -0.01473 43  ILE A C   
224  O O   . ILE A 36  ? 0.25537 0.22457 0.22178 -0.00656 -0.02046 -0.01617 43  ILE A O   
225  C CB  . ILE A 36  ? 0.29207 0.20268 0.19199 -0.00273 -0.05218 -0.01599 43  ILE A CB  
226  C CG1 . ILE A 36  ? 0.36399 0.30794 0.29432 -0.01727 -0.06093 -0.00313 43  ILE A CG1 
227  C CG2 . ILE A 36  ? 0.42507 0.28587 0.26747 0.01373  -0.06198 -0.02301 43  ILE A CG2 
228  C CD1 . ILE A 36  ? 0.33488 0.31818 0.30480 -0.03353 -0.06511 0.00989  43  ILE A CD1 
229  N N   . PHE A 37  ? 0.23679 0.22952 0.21991 0.00024  -0.00780 -0.01078 44  PHE A N   
230  C CA  . PHE A 37  ? 0.22098 0.23405 0.22611 -0.00138 -0.00258 -0.00952 44  PHE A CA  
231  C C   . PHE A 37  ? 0.19907 0.20642 0.20711 -0.00154 0.00434  -0.01519 44  PHE A C   
232  O O   . PHE A 37  ? 0.20147 0.21755 0.21926 -0.00447 0.00371  -0.01597 44  PHE A O   
233  C CB  . PHE A 37  ? 0.20398 0.22307 0.21235 0.00801  0.00370  -0.00730 44  PHE A CB  
234  C CG  . PHE A 37  ? 0.19620 0.19588 0.19872 0.00944  0.00986  -0.01051 44  PHE A CG  
235  C CD1 . PHE A 37  ? 0.21103 0.20118 0.20489 0.01042  0.01245  -0.00677 44  PHE A CD1 
236  C CD2 . PHE A 37  ? 0.25381 0.24612 0.25994 0.00702  0.01009  -0.01335 44  PHE A CD2 
237  C CE1 . PHE A 37  ? 0.23282 0.21406 0.22879 0.00618  0.01583  -0.00078 44  PHE A CE1 
238  C CE2 . PHE A 37  ? 0.26008 0.23714 0.26607 0.00016  0.00867  -0.00923 44  PHE A CE2 
239  C CZ  . PHE A 37  ? 0.26394 0.23924 0.26843 -0.00182 0.01177  -0.00052 44  PHE A CZ  
240  N N   . LEU A 38  ? 0.22379 0.22319 0.22572 0.00260  0.01147  -0.01510 45  LEU A N   
241  C CA  . LEU A 38  ? 0.23292 0.23881 0.24524 0.00152  0.01708  -0.01389 45  LEU A CA  
242  C C   . LEU A 38  ? 0.23487 0.23652 0.23888 0.00448  0.01477  -0.01810 45  LEU A C   
243  O O   . LEU A 38  ? 0.20987 0.21907 0.22563 0.00103  0.01493  -0.01919 45  LEU A O   
244  C CB  . LEU A 38  ? 0.16911 0.18334 0.18427 0.00530  0.02600  -0.00268 45  LEU A CB  
245  C CG  . LEU A 38  ? 0.17970 0.21390 0.21606 0.00016  0.02911  0.00718  45  LEU A CG  
246  C CD1 . LEU A 38  ? 0.19489 0.21992 0.24244 -0.01408 0.01782  0.00341  45  LEU A CD1 
247  C CD2 . LEU A 38  ? 0.26138 0.32019 0.31014 0.00131  0.03788  0.02945  45  LEU A CD2 
248  N N   . ARG A 39  ? 0.20052 0.18162 0.17662 0.01239  0.00970  -0.02073 46  ARG A N   
249  C CA  . ARG A 39  ? 0.28031 0.23888 0.23461 0.01557  0.00040  -0.02570 46  ARG A CA  
250  C C   . ARG A 39  ? 0.27000 0.23520 0.24210 -0.00186 -0.01029 -0.02512 46  ARG A C   
251  O O   . ARG A 39  ? 0.21735 0.17930 0.18966 -0.00268 -0.01209 -0.02651 46  ARG A O   
252  C CB  . ARG A 39  ? 0.29814 0.21425 0.20526 0.02501  -0.01325 -0.02969 46  ARG A CB  
253  C CG  . ARG A 39  ? 0.43302 0.30425 0.30147 0.02845  -0.03111 -0.03542 46  ARG A CG  
254  C CD  . ARG A 39  ? 0.46902 0.27950 0.28059 0.03099  -0.05767 -0.03997 46  ARG A CD  
255  N NE  . ARG A 39  ? 0.47199 0.29205 0.30542 0.00231  -0.07655 -0.03213 46  ARG A NE  
256  C CZ  . ARG A 39  ? 0.59066 0.37609 0.39105 -0.00125 -0.09852 -0.03178 46  ARG A CZ  
257  N NH1 . ARG A 39  ? 0.54775 0.27722 0.28212 0.02543  -0.10431 -0.04211 46  ARG A NH1 
258  N NH2 . ARG A 39  ? 0.51147 0.32056 0.34279 -0.02915 -0.11571 -0.01841 46  ARG A NH2 
259  N N   . GLU A 40  ? 0.20013 0.18060 0.18792 -0.01296 -0.01585 -0.01954 47  GLU A N   
260  C CA  . GLU A 40  ? 0.18945 0.18801 0.19526 -0.02579 -0.02384 -0.01110 47  GLU A CA  
261  C C   . GLU A 40  ? 0.19741 0.21658 0.22130 -0.02104 -0.01111 -0.01306 47  GLU A C   
262  O O   . GLU A 40  ? 0.18490 0.21096 0.21485 -0.02612 -0.01437 -0.00893 47  GLU A O   
263  C CB  . GLU A 40  ? 0.16640 0.19170 0.18851 -0.03264 -0.02941 0.00218  47  GLU A CB  
264  C CG  . GLU A 40  ? 0.19771 0.20170 0.20235 -0.04396 -0.05111 0.00813  47  GLU A CG  
265  C CD  . GLU A 40  ? 0.36917 0.33142 0.34721 -0.05777 -0.07565 0.00904  47  GLU A CD  
266  O OE1 . GLU A 40  ? 0.29196 0.26584 0.28444 -0.06966 -0.08129 0.01866  47  GLU A OE1 
267  O OE2 . GLU A 40  ? 0.41999 0.33152 0.35575 -0.05541 -0.09219 0.00129  47  GLU A OE2 
268  N N   . LEU A 41  ? 0.21803 0.24173 0.24642 -0.01258 -0.00023 -0.01794 48  LEU A N   
269  C CA  . LEU A 41  ? 0.16671 0.19742 0.20194 -0.00865 0.00459  -0.02045 48  LEU A CA  
270  C C   . LEU A 41  ? 0.17258 0.19664 0.20849 -0.01015 0.00527  -0.02451 48  LEU A C   
271  O O   . LEU A 41  ? 0.19739 0.22565 0.23637 -0.00994 0.00439  -0.02549 48  LEU A O   
272  C CB  . LEU A 41  ? 0.17335 0.19653 0.20398 -0.00205 0.00721  -0.02289 48  LEU A CB  
273  C CG  . LEU A 41  ? 0.18016 0.21187 0.20586 0.00771  0.00849  -0.01804 48  LEU A CG  
274  C CD1 . LEU A 41  ? 0.25213 0.25890 0.26117 0.01604  0.00729  -0.02220 48  LEU A CD1 
275  C CD2 . LEU A 41  ? 0.18380 0.23924 0.21073 0.01870  0.01127  -0.01060 48  LEU A CD2 
276  N N   . ILE A 42  ? 0.15241 0.16996 0.18351 -0.00751 0.00800  -0.02456 49  ILE A N   
277  C CA  . ILE A 42  ? 0.19707 0.21791 0.22979 -0.00315 0.01062  -0.02376 49  ILE A CA  
278  C C   . ILE A 42  ? 0.25016 0.25745 0.26946 -0.00241 0.00429  -0.02663 49  ILE A C   
279  O O   . ILE A 42  ? 0.18015 0.19174 0.20368 -0.00119 0.00407  -0.02684 49  ILE A O   
280  C CB  . ILE A 42  ? 0.16967 0.19612 0.19756 0.00809  0.01898  -0.01728 49  ILE A CB  
281  C CG1 . ILE A 42  ? 0.15747 0.20200 0.20685 -0.00003 0.02160  -0.00755 49  ILE A CG1 
282  C CG2 . ILE A 42  ? 0.17174 0.20578 0.19446 0.02243  0.02403  -0.01311 49  ILE A CG2 
283  C CD1 . ILE A 42  ? 0.17147 0.23678 0.22390 0.01040  0.03282  0.00825  49  ILE A CD1 
284  N N   . SER A 43  ? 0.16913 0.15679 0.17103 -0.00606 -0.00506 -0.02668 50  SER A N   
285  C CA  . SER A 43  ? 0.24867 0.21532 0.23555 -0.01242 -0.01864 -0.02493 50  SER A CA  
286  C C   . SER A 43  ? 0.25456 0.24614 0.26457 -0.02264 -0.01851 -0.01836 50  SER A C   
287  O O   . SER A 43  ? 0.20414 0.18849 0.20955 -0.02365 -0.02249 -0.01706 50  SER A O   
288  C CB  . SER A 43  ? 0.24725 0.18600 0.21249 -0.02192 -0.03683 -0.02127 50  SER A CB  
289  O OG  . SER A 43  ? 0.44524 0.36011 0.39762 -0.03655 -0.05750 -0.01385 50  SER A OG  
290  N N   . ASN A 44  ? 0.17972 0.19957 0.20912 -0.02477 -0.01254 -0.01359 51  ASN A N   
291  C CA  . ASN A 44  ? 0.21223 0.25743 0.25462 -0.02417 -0.00870 -0.00609 51  ASN A CA  
292  C C   . ASN A 44  ? 0.19805 0.23940 0.23819 -0.01570 -0.00309 -0.01545 51  ASN A C   
293  O O   . ASN A 44  ? 0.20621 0.25393 0.24659 -0.01529 -0.00383 -0.01126 51  ASN A O   
294  C CB  . ASN A 44  ? 0.18792 0.25914 0.23881 -0.01653 -0.00174 0.00049  51  ASN A CB  
295  C CG  . ASN A 44  ? 0.25994 0.35476 0.32355 -0.02723 -0.00910 0.02014  51  ASN A CG  
296  O OD1 . ASN A 44  ? 0.22480 0.30564 0.28688 -0.04542 -0.02483 0.02742  51  ASN A OD1 
297  N ND2 . ASN A 44  ? 0.22528 0.35270 0.29755 -0.01526 -0.00106 0.03087  51  ASN A ND2 
298  N N   . SER A 45  ? 0.18083 0.21416 0.22041 -0.01123 0.00014  -0.02428 52  SER A N   
299  C CA  . SER A 45  ? 0.16286 0.19518 0.20436 -0.00861 -0.00070 -0.02835 52  SER A CA  
300  C C   . SER A 45  ? 0.23248 0.26203 0.27228 -0.00746 -0.00198 -0.02736 52  SER A C   
301  O O   . SER A 45  ? 0.18230 0.21449 0.22202 -0.00587 -0.00435 -0.02747 52  SER A O   
302  C CB  . SER A 45  ? 0.21136 0.24266 0.25987 -0.01085 -0.00137 -0.02870 52  SER A CB  
303  O OG  . SER A 45  ? 0.22937 0.25011 0.27016 -0.01042 -0.00477 -0.03109 52  SER A OG  
304  N N   . SER A 46  ? 0.14488 0.16313 0.17539 -0.00404 -0.00147 -0.02692 53  SER A N   
305  C CA  . SER A 46  ? 0.18126 0.18480 0.19624 0.00444  -0.00403 -0.02683 53  SER A CA  
306  C C   . SER A 46  ? 0.23344 0.22525 0.24091 -0.00371 -0.01285 -0.02383 53  SER A C   
307  O O   . SER A 46  ? 0.23571 0.22572 0.23976 0.00116  -0.01406 -0.02338 53  SER A O   
308  C CB  . SER A 46  ? 0.23795 0.21557 0.22568 0.01610  -0.00507 -0.02849 53  SER A CB  
309  O OG  . SER A 46  ? 0.27848 0.23166 0.23795 0.03297  -0.00810 -0.02953 53  SER A OG  
310  N N   . ASP A 47  ? 0.18791 0.17863 0.19668 -0.01699 -0.01939 -0.01712 54  ASP A N   
311  C CA  . ASP A 47  ? 0.19756 0.18969 0.20713 -0.02833 -0.02792 -0.00490 54  ASP A CA  
312  C C   . ASP A 47  ? 0.23650 0.25560 0.25881 -0.02217 -0.01872 -0.00354 54  ASP A C   
313  O O   . ASP A 47  ? 0.19501 0.21022 0.21218 -0.02358 -0.02276 0.00254  54  ASP A O   
314  C CB  . ASP A 47  ? 0.18580 0.19308 0.20684 -0.04455 -0.03523 0.01112  54  ASP A CB  
315  C CG  . ASP A 47  ? 0.32470 0.29308 0.32437 -0.05553 -0.05404 0.01220  54  ASP A CG  
316  O OD1 . ASP A 47  ? 0.33447 0.25692 0.30078 -0.04516 -0.06041 -0.00051 54  ASP A OD1 
317  O OD2 . ASP A 47  ? 0.28399 0.26732 0.29611 -0.07117 -0.06332 0.02698  54  ASP A OD2 
318  N N   . ALA A 48  ? 0.17335 0.21198 0.20467 -0.01422 -0.00933 -0.00886 55  ALA A N   
319  C CA  . ALA A 48  ? 0.15184 0.20210 0.18024 -0.00407 -0.00513 -0.01004 55  ALA A CA  
320  C C   . ALA A 48  ? 0.21909 0.25760 0.24355 -0.00067 -0.00897 -0.01827 55  ALA A C   
321  O O   . ALA A 48  ? 0.20227 0.24317 0.21965 0.00459  -0.01022 -0.01647 55  ALA A O   
322  C CB  . ALA A 48  ? 0.14361 0.19623 0.16638 0.00623  -0.00121 -0.01666 55  ALA A CB  
323  N N   . LEU A 49  ? 0.17393 0.20600 0.20372 -0.00116 -0.01006 -0.02402 56  LEU A N   
324  C CA  . LEU A 49  ? 0.19357 0.22748 0.22602 0.00393  -0.01285 -0.02490 56  LEU A CA  
325  C C   . LEU A 49  ? 0.22016 0.24049 0.23922 0.00832  -0.01487 -0.02143 56  LEU A C   
326  O O   . LEU A 49  ? 0.19188 0.21490 0.20870 0.01315  -0.01776 -0.02021 56  LEU A O   
327  C CB  . LEU A 49  ? 0.16739 0.21158 0.21208 0.00658  -0.00994 -0.02321 56  LEU A CB  
328  C CG  . LEU A 49  ? 0.14958 0.20278 0.20781 -0.00258 -0.01419 -0.02279 56  LEU A CG  
329  C CD1 . LEU A 49  ? 0.16786 0.23559 0.23946 -0.00182 -0.00814 -0.01556 56  LEU A CD1 
330  C CD2 . LEU A 49  ? 0.13066 0.19178 0.19692 -0.00744 -0.02667 -0.01912 56  LEU A CD2 
331  N N   . ASP A 50  ? 0.22146 0.21953 0.22603 0.00612  -0.01749 -0.01941 57  ASP A N   
332  C CA  . ASP A 50  ? 0.23925 0.20798 0.22093 0.00694  -0.02661 -0.01485 57  ASP A CA  
333  C C   . ASP A 50  ? 0.23561 0.21582 0.22267 -0.00118 -0.02882 -0.00587 57  ASP A C   
334  O O   . ASP A 50  ? 0.23671 0.20264 0.21055 0.00343  -0.03386 -0.00285 57  ASP A O   
335  C CB  . ASP A 50  ? 0.22621 0.15904 0.18635 -0.00270 -0.03869 -0.01124 57  ASP A CB  
336  C CG  . ASP A 50  ? 0.36632 0.27229 0.30172 0.01408  -0.03849 -0.02026 57  ASP A CG  
337  O OD1 . ASP A 50  ? 0.32581 0.24630 0.26216 0.03601  -0.02702 -0.02462 57  ASP A OD1 
338  O OD2 . ASP A 50  ? 0.36311 0.23588 0.27692 0.00631  -0.05092 -0.01965 57  ASP A OD2 
339  N N   . LYS A 51  ? 0.20825 0.21474 0.21048 -0.00901 -0.02401 0.00071  58  LYS A N   
340  C CA  . LYS A 51  ? 0.20262 0.22629 0.20637 -0.01171 -0.02315 0.01533  58  LYS A CA  
341  C C   . LYS A 51  ? 0.23133 0.26115 0.22914 0.00264  -0.01951 0.00784  58  LYS A C   
342  O O   . LYS A 51  ? 0.22413 0.25249 0.21366 0.00406  -0.02196 0.01677  58  LYS A O   
343  C CB  . LYS A 51  ? 0.21280 0.27099 0.23000 -0.01357 -0.01519 0.02817  58  LYS A CB  
344  C CG  . LYS A 51  ? 0.37932 0.44053 0.40754 -0.03346 -0.02357 0.04524  58  LYS A CG  
345  C CD  . LYS A 51  ? 0.46287 0.57281 0.50971 -0.03063 -0.01316 0.06368  58  LYS A CD  
346  C CE  . LYS A 51  ? 0.47891 0.58924 0.53805 -0.04728 -0.02200 0.07058  58  LYS A CE  
347  N NZ  . LYS A 51  ? 0.39852 0.56641 0.48005 -0.04343 -0.01224 0.09593  58  LYS A NZ  
348  N N   . ILE A 52  ? 0.20169 0.23597 0.20182 0.01102  -0.01724 -0.00601 59  ILE A N   
349  C CA  . ILE A 52  ? 0.23100 0.26490 0.22177 0.02093  -0.02136 -0.01183 59  ILE A CA  
350  C C   . ILE A 52  ? 0.21430 0.24108 0.20774 0.02246  -0.02704 -0.01302 59  ILE A C   
351  O O   . ILE A 52  ? 0.23846 0.26451 0.22303 0.02887  -0.03153 -0.01144 59  ILE A O   
352  C CB  . ILE A 52  ? 0.24879 0.27903 0.23575 0.02431  -0.02654 -0.02294 59  ILE A CB  
353  C CG1 . ILE A 52  ? 0.30554 0.32449 0.27165 0.03299  -0.03837 -0.02786 59  ILE A CG1 
354  C CG2 . ILE A 52  ? 0.19025 0.22261 0.19798 0.01506  -0.03065 -0.02698 59  ILE A CG2 
355  C CD1 . ILE A 52  ? 0.27577 0.29499 0.21330 0.05001  -0.03167 -0.02211 59  ILE A CD1 
356  N N   . ARG A 53  ? 0.19593 0.21831 0.19728 0.02182  -0.02609 -0.01474 60  ARG A N   
357  C CA  . ARG A 53  ? 0.22950 0.24687 0.22627 0.03311  -0.02835 -0.01292 60  ARG A CA  
358  C C   . ARG A 53  ? 0.28650 0.27903 0.26078 0.03528  -0.03263 -0.00704 60  ARG A C   
359  O O   . ARG A 53  ? 0.28547 0.27780 0.25308 0.04555  -0.03599 -0.00496 60  ARG A O   
360  C CB  . ARG A 53  ? 0.21924 0.23140 0.21483 0.04153  -0.02382 -0.01375 60  ARG A CB  
361  C CG  . ARG A 53  ? 0.32204 0.34091 0.31233 0.06370  -0.02250 -0.00902 60  ARG A CG  
362  C CD  . ARG A 53  ? 0.37004 0.37438 0.34038 0.08489  -0.01612 -0.00843 60  ARG A CD  
363  N NE  . ARG A 53  ? 0.67613 0.63578 0.61965 0.07655  -0.02068 -0.01520 60  ARG A NE  
364  C CZ  . ARG A 53  ? 0.73420 0.66971 0.65075 0.09345  -0.01827 -0.01781 60  ARG A CZ  
365  N NH1 . ARG A 53  ? 0.56126 0.52256 0.47737 0.12327  -0.00578 -0.01203 60  ARG A NH1 
366  N NH2 . ARG A 53  ? 0.45636 0.34363 0.34452 0.08155  -0.02968 -0.02296 60  ARG A NH2 
367  N N   . TYR A 54  ? 0.26692 0.23879 0.23041 0.02332  -0.03549 -0.00085 61  TYR A N   
368  C CA  . TYR A 54  ? 0.26583 0.20961 0.20808 0.01893  -0.04496 0.01034  61  TYR A CA  
369  C C   . TYR A 54  ? 0.28798 0.25514 0.23563 0.01830  -0.04192 0.01895  61  TYR A C   
370  O O   . TYR A 54  ? 0.28224 0.23572 0.21497 0.02531  -0.04696 0.02301  61  TYR A O   
371  C CB  . TYR A 54  ? 0.30515 0.22468 0.23949 -0.00159 -0.05541 0.02194  61  TYR A CB  
372  C CG  . TYR A 54  ? 0.38843 0.28407 0.30777 -0.01730 -0.07029 0.04270  61  TYR A CG  
373  C CD1 . TYR A 54  ? 0.48260 0.41809 0.42397 -0.03220 -0.06613 0.06534  61  TYR A CD1 
374  C CD2 . TYR A 54  ? 0.53083 0.36315 0.40977 -0.01441 -0.08911 0.04285  61  TYR A CD2 
375  C CE1 . TYR A 54  ? 0.59958 0.52114 0.53297 -0.05037 -0.08062 0.09212  61  TYR A CE1 
376  C CE2 . TYR A 54  ? 0.54442 0.34719 0.40720 -0.03339 -0.10796 0.06497  61  TYR A CE2 
377  C CZ  . TYR A 54  ? 0.62853 0.48043 0.52372 -0.05482 -0.10386 0.09183  61  TYR A CZ  
378  O OH  . TYR A 54  ? 0.70177 0.53293 0.58718 -0.07789 -0.12337 0.12185  61  TYR A OH  
379  N N   . GLU A 55  ? 0.29117 0.29064 0.25308 0.01581  -0.03331 0.02121  62  GLU A N   
380  C CA  . GLU A 55  ? 0.30147 0.31944 0.25664 0.02346  -0.02919 0.02970  62  GLU A CA  
381  C C   . GLU A 55  ? 0.32277 0.33561 0.26830 0.03785  -0.03380 0.01769  62  GLU A C   
382  O O   . GLU A 55  ? 0.28793 0.30076 0.21928 0.04484  -0.03523 0.02537  62  GLU A O   
383  C CB  . GLU A 55  ? 0.30270 0.34869 0.26082 0.03000  -0.01868 0.03148  62  GLU A CB  
384  C CG  . GLU A 55  ? 0.32045 0.39079 0.29232 0.01834  -0.01251 0.05533  62  GLU A CG  
385  C CD  . GLU A 55  ? 0.47039 0.57688 0.43750 0.03698  0.00232  0.06417  62  GLU A CD  
386  O OE1 . GLU A 55  ? 0.41399 0.51252 0.35509 0.06056  0.00500  0.04881  62  GLU A OE1 
387  O OE2 . GLU A 55  ? 0.58027 0.72047 0.56555 0.02988  0.00900  0.08778  62  GLU A OE2 
388  N N   . SER A 56  ? 0.26755 0.28086 0.22312 0.04115  -0.03746 0.00324  63  SER A N   
389  C CA  . SER A 56  ? 0.36159 0.37996 0.31609 0.05040  -0.04616 -0.00233 63  SER A CA  
390  C C   . SER A 56  ? 0.38282 0.39164 0.33047 0.05912  -0.04949 0.00336  63  SER A C   
391  O O   . SER A 56  ? 0.35061 0.36680 0.29505 0.06762  -0.05710 0.00377  63  SER A O   
392  C CB  . SER A 56  ? 0.31607 0.34862 0.29197 0.04668  -0.05140 -0.00944 63  SER A CB  
393  O OG  . SER A 56  ? 0.33574 0.37236 0.32466 0.04973  -0.04598 -0.00670 63  SER A OG  
394  N N   . LEU A 57  ? 0.33080 0.31647 0.26942 0.05864  -0.04738 0.00790  64  LEU A N   
395  C CA  . LEU A 57  ? 0.37627 0.33810 0.29428 0.07226  -0.05271 0.01263  64  LEU A CA  
396  C C   . LEU A 57  ? 0.46879 0.42295 0.37079 0.07131  -0.05680 0.02228  64  LEU A C   
397  O O   . LEU A 57  ? 0.49170 0.43755 0.38035 0.08589  -0.06192 0.02464  64  LEU A O   
398  C CB  . LEU A 57  ? 0.36542 0.28253 0.25951 0.07210  -0.05654 0.01437  64  LEU A CB  
399  C CG  . LEU A 57  ? 0.38880 0.30982 0.28942 0.08048  -0.05101 0.00571  64  LEU A CG  
400  C CD1 . LEU A 57  ? 0.49412 0.35380 0.35301 0.08620  -0.06005 0.00499  64  LEU A CD1 
401  C CD2 . LEU A 57  ? 0.47381 0.43335 0.39193 0.10314  -0.04473 0.00474  64  LEU A CD2 
402  N N   . THR A 58  ? 0.38609 0.34747 0.28855 0.05762  -0.05323 0.03146  65  THR A N   
403  C CA  . THR A 58  ? 0.44301 0.40551 0.33035 0.05980  -0.05414 0.04529  65  THR A CA  
404  C C   . THR A 58  ? 0.47114 0.46127 0.35629 0.07040  -0.04972 0.04052  65  THR A C   
405  O O   . THR A 58  ? 0.49650 0.48782 0.36333 0.07955  -0.05051 0.04932  65  THR A O   
406  C CB  . THR A 58  ? 0.56183 0.51702 0.44636 0.04071  -0.05447 0.06952  65  THR A CB  
407  O OG1 . THR A 58  ? 0.56597 0.55466 0.46885 0.03301  -0.04382 0.07504  65  THR A OG1 
408  C CG2 . THR A 58  ? 0.49136 0.39928 0.36394 0.02850  -0.06824 0.07251  65  THR A CG2 
409  N N   . ASP A 59  ? 0.54731 0.43026 0.33395 0.04786  -0.04671 0.09785  66  ASP A N   
410  C CA  . ASP A 59  ? 0.51158 0.42121 0.28709 0.05941  -0.04783 0.09201  66  ASP A CA  
411  C C   . ASP A 59  ? 0.50757 0.43270 0.30006 0.06301  -0.05847 0.06996  66  ASP A C   
412  O O   . ASP A 59  ? 0.43605 0.37478 0.24261 0.05496  -0.05519 0.05847  66  ASP A O   
413  C CB  . ASP A 59  ? 0.52149 0.44902 0.29375 0.05330  -0.03360 0.10004  66  ASP A CB  
414  C CG  . ASP A 59  ? 0.68685 0.62712 0.43050 0.07034  -0.03383 0.09364  66  ASP A CG  
415  O OD1 . ASP A 59  ? 0.59609 0.53213 0.32694 0.08086  -0.05019 0.08075  66  ASP A OD1 
416  O OD2 . ASP A 59  ? 0.66522 0.61822 0.39697 0.07416  -0.01848 0.10315  66  ASP A OD2 
417  N N   . PRO A 60  ? 0.54228 0.46845 0.33705 0.07484  -0.07156 0.06684  67  PRO A N   
418  C CA  . PRO A 60  ? 0.50377 0.45040 0.32355 0.07519  -0.08249 0.05181  67  PRO A CA  
419  C C   . PRO A 60  ? 0.47415 0.43463 0.28690 0.07074  -0.08908 0.03901  67  PRO A C   
420  O O   . PRO A 60  ? 0.46604 0.43916 0.30150 0.06358  -0.09375 0.02685  67  PRO A O   
421  C CB  . PRO A 60  ? 0.55620 0.50954 0.37807 0.09032  -0.09673 0.05923  67  PRO A CB  
422  C CG  . PRO A 60  ? 0.66625 0.59228 0.47131 0.09822  -0.08806 0.07462  67  PRO A CG  
423  C CD  . PRO A 60  ? 0.57625 0.48565 0.35842 0.08744  -0.07554 0.08077  67  PRO A CD  
424  N N   . SER A 61  ? 0.46061 0.41402 0.23701 0.07675  -0.08882 0.04228  68  SER A N   
425  C CA  . SER A 61  ? 0.46187 0.41493 0.21616 0.07766  -0.09574 0.02911  68  SER A CA  
426  C C   . SER A 61  ? 0.58776 0.54497 0.35548 0.06872  -0.08130 0.02076  68  SER A C   
427  O O   . SER A 61  ? 0.45285 0.40562 0.20757 0.06883  -0.08847 0.00692  68  SER A O   
428  C CB  . SER A 61  ? 0.58397 0.52197 0.28540 0.09252  -0.09461 0.03673  68  SER A CB  
429  O OG  . SER A 61  ? 0.61050 0.54753 0.29883 0.09568  -0.06918 0.04804  68  SER A OG  
430  N N   . LYS A 62  ? 0.40991 0.37195 0.20222 0.06008  -0.06449 0.02882  69  LYS A N   
431  C CA  . LYS A 62  ? 0.41553 0.38555 0.22510 0.05113  -0.05341 0.02282  69  LYS A CA  
432  C C   . LYS A 62  ? 0.41701 0.39234 0.25099 0.04396  -0.06399 0.00632  69  LYS A C   
433  O O   . LYS A 62  ? 0.38439 0.36364 0.22550 0.03936  -0.05810 -0.00129 69  LYS A O   
434  C CB  . LYS A 62  ? 0.40648 0.37805 0.23655 0.03973  -0.03996 0.03672  69  LYS A CB  
435  C CG  . LYS A 62  ? 0.46237 0.43469 0.27403 0.04348  -0.02780 0.05798  69  LYS A CG  
436  C CD  . LYS A 62  ? 0.42642 0.41080 0.25934 0.02946  -0.01460 0.07358  69  LYS A CD  
437  C CE  . LYS A 62  ? 0.50505 0.49668 0.32565 0.03237  -0.00182 0.10057  69  LYS A CE  
438  N NZ  . LYS A 62  ? 0.59846 0.60728 0.44961 0.01323  0.00673  0.12087  69  LYS A NZ  
439  N N   . LEU A 63  ? 0.37213 0.35084 0.22108 0.04414  -0.07843 0.00391  70  LEU A N   
440  C CA  . LEU A 63  ? 0.33202 0.32197 0.20899 0.03719  -0.08794 -0.00604 70  LEU A CA  
441  C C   . LEU A 63  ? 0.47029 0.45915 0.33404 0.03661  -0.11004 -0.01424 70  LEU A C   
442  O O   . LEU A 63  ? 0.34165 0.34290 0.23261 0.02811  -0.12241 -0.01800 70  LEU A O   
443  C CB  . LEU A 63  ? 0.33957 0.33934 0.24605 0.03947  -0.08823 0.00133  70  LEU A CB  
444  C CG  . LEU A 63  ? 0.33645 0.32428 0.24956 0.03790  -0.07116 0.00527  70  LEU A CG  
445  C CD1 . LEU A 63  ? 0.37986 0.36905 0.31027 0.04779  -0.06996 0.01166  70  LEU A CD1 
446  C CD2 . LEU A 63  ? 0.35441 0.34381 0.27792 0.02715  -0.06318 -0.00367 70  LEU A CD2 
447  N N   . ASP A 64  ? 0.42390 0.39538 0.24352 0.04503  -0.11643 -0.01550 71  ASP A N   
448  C CA  . ASP A 64  ? 0.46402 0.42020 0.25684 0.04330  -0.14190 -0.02584 71  ASP A CA  
449  C C   . ASP A 64  ? 0.45422 0.39833 0.24637 0.03475  -0.14344 -0.03973 71  ASP A C   
450  O O   . ASP A 64  ? 0.49474 0.42953 0.28679 0.02407  -0.16577 -0.04672 71  ASP A O   
451  C CB  . ASP A 64  ? 0.49372 0.42310 0.22437 0.05877  -0.14432 -0.02605 71  ASP A CB  
452  C CG  . ASP A 64  ? 0.68984 0.62640 0.41532 0.06632  -0.15168 -0.01274 71  ASP A CG  
453  O OD1 . ASP A 64  ? 0.57566 0.53723 0.34577 0.06057  -0.15746 -0.00417 71  ASP A OD1 
454  O OD2 . ASP A 64  ? 0.70268 0.62223 0.38611 0.07857  -0.14568 -0.00880 71  ASP A OD2 
455  N N   . SER A 65  ? 0.42744 0.37235 0.22370 0.03736  -0.11856 -0.04093 72  SER A N   
456  C CA  . SER A 65  ? 0.44209 0.37543 0.23759 0.03251  -0.11591 -0.05212 72  SER A CA  
457  C C   . SER A 65  ? 0.50615 0.46207 0.35611 0.01665  -0.11644 -0.05146 72  SER A C   
458  O O   . SER A 65  ? 0.51832 0.46855 0.37416 0.01238  -0.11016 -0.05791 72  SER A O   
459  C CB  . SER A 65  ? 0.53184 0.46297 0.31030 0.04507  -0.08835 -0.04911 72  SER A CB  
460  O OG  . SER A 65  ? 0.40584 0.36348 0.21646 0.04231  -0.07067 -0.03496 72  SER A OG  
461  N N   . GLY A 66  ? 0.42947 0.41057 0.31667 0.01150  -0.12102 -0.04187 73  GLY A N   
462  C CA  . GLY A 66  ? 0.37464 0.37800 0.30914 0.00118  -0.12001 -0.03827 73  GLY A CA  
463  C C   . GLY A 66  ? 0.37345 0.39667 0.33436 0.00745  -0.10562 -0.02668 73  GLY A C   
464  O O   . GLY A 66  ? 0.37433 0.38938 0.32425 0.01291  -0.08823 -0.02535 73  GLY A O   
465  N N   . LYS A 67  ? 0.30646 0.35392 0.30028 0.00750  -0.11371 -0.01618 74  LYS A N   
466  C CA  . LYS A 67  ? 0.34292 0.40072 0.35137 0.01996  -0.09999 -0.00496 74  LYS A CA  
467  C C   . LYS A 67  ? 0.34967 0.41228 0.37886 0.02135  -0.08198 -0.00378 74  LYS A C   
468  O O   . LYS A 67  ? 0.32775 0.37886 0.34939 0.03264  -0.06734 0.00003  74  LYS A O   
469  C CB  . LYS A 67  ? 0.43222 0.51742 0.46514 0.02612  -0.11435 0.00979  74  LYS A CB  
470  C CG  . LYS A 67  ? 0.60586 0.68036 0.60965 0.03327  -0.12617 0.01234  74  LYS A CG  
471  C CD  . LYS A 67  ? 0.74271 0.84224 0.76886 0.04760  -0.13132 0.03085  74  LYS A CD  
472  C CE  . LYS A 67  ? 0.77108 0.84954 0.77768 0.06643  -0.11117 0.03625  74  LYS A CE  
473  N NZ  . LYS A 67  ? 0.66838 0.73460 0.68026 0.07205  -0.08759 0.03420  74  LYS A NZ  
474  N N   . GLU A 68  ? 0.23736 0.30963 0.28551 0.01052  -0.08371 -0.00714 75  GLU A N   
475  C CA  . GLU A 68  ? 0.24852 0.32639 0.31411 0.01357  -0.06670 -0.00429 75  GLU A CA  
476  C C   . GLU A 68  ? 0.23981 0.28894 0.27745 0.01244  -0.05358 -0.01527 75  GLU A C   
477  O O   . GLU A 68  ? 0.28091 0.31774 0.30157 0.00370  -0.05743 -0.02470 75  GLU A O   
478  C CB  . GLU A 68  ? 0.26846 0.36693 0.36483 0.00038  -0.07464 -0.00104 75  GLU A CB  
479  C CG  . GLU A 68  ? 0.35717 0.49209 0.49107 -0.00160 -0.09009 0.01608  75  GLU A CG  
480  C CD  . GLU A 68  ? 0.73527 0.86439 0.86289 -0.01999 -0.11998 0.01079  75  GLU A CD  
481  O OE1 . GLU A 68  ? 0.66647 0.76078 0.75022 -0.02152 -0.12520 -0.00588 75  GLU A OE1 
482  O OE2 . GLU A 68  ? 0.94104 1.09915 1.10542 -0.03232 -0.13903 0.02503  75  GLU A OE2 
483  N N   . LEU A 69  ? 0.22898 0.26600 0.25949 0.02260  -0.03893 -0.01257 76  LEU A N   
484  C CA  . LEU A 69  ? 0.21974 0.22883 0.22473 0.01882  -0.03136 -0.02004 76  LEU A CA  
485  C C   . LEU A 69  ? 0.23265 0.24221 0.24483 0.02072  -0.02130 -0.02048 76  LEU A C   
486  O O   . LEU A 69  ? 0.24019 0.24566 0.25058 0.03584  -0.01113 -0.01410 76  LEU A O   
487  C CB  . LEU A 69  ? 0.25052 0.23055 0.22854 0.02716  -0.02809 -0.01713 76  LEU A CB  
488  C CG  . LEU A 69  ? 0.24780 0.22614 0.21678 0.02764  -0.03609 -0.01313 76  LEU A CG  
489  C CD1 . LEU A 69  ? 0.31189 0.25288 0.25132 0.03304  -0.03352 -0.00900 76  LEU A CD1 
490  C CD2 . LEU A 69  ? 0.23524 0.22114 0.20113 0.01468  -0.04189 -0.01748 76  LEU A CD2 
491  N N   . HIS A 70  ? 0.20184 0.21531 0.21915 0.00916  -0.02244 -0.02647 77  HIS A N   
492  C CA  . HIS A 70  ? 0.21408 0.23071 0.23956 0.01162  -0.01296 -0.02464 77  HIS A CA  
493  C C   . HIS A 70  ? 0.25453 0.26241 0.27152 0.00059  -0.01398 -0.03225 77  HIS A C   
494  O O   . HIS A 70  ? 0.20047 0.20572 0.21035 -0.00722 -0.02055 -0.03709 77  HIS A O   
495  C CB  . HIS A 70  ? 0.18420 0.23279 0.24611 0.01180  -0.01318 -0.01462 77  HIS A CB  
496  C CG  . HIS A 70  ? 0.19876 0.25744 0.27462 -0.00409 -0.02852 -0.01832 77  HIS A CG  
497  N ND1 . HIS A 70  ? 0.25857 0.33517 0.35308 -0.00860 -0.04289 -0.01261 77  HIS A ND1 
498  C CD2 . HIS A 70  ? 0.32793 0.37478 0.39489 -0.01480 -0.03335 -0.02739 77  HIS A CD2 
499  C CE1 . HIS A 70  ? 0.27476 0.34315 0.36537 -0.02249 -0.05752 -0.01992 77  HIS A CE1 
500  N NE2 . HIS A 70  ? 0.31028 0.35980 0.38324 -0.02440 -0.05016 -0.02903 77  HIS A NE2 
501  N N   . ILE A 71  ? 0.22377 0.22856 0.24034 0.00329  -0.00551 -0.03082 78  ILE A N   
502  C CA  . ILE A 71  ? 0.17622 0.17496 0.18657 -0.00450 -0.00580 -0.03539 78  ILE A CA  
503  C C   . ILE A 71  ? 0.23341 0.24594 0.26407 -0.00473 -0.00010 -0.03018 78  ILE A C   
504  O O   . ILE A 71  ? 0.20570 0.22508 0.24367 0.00497  0.01014  -0.02142 78  ILE A O   
505  C CB  . ILE A 71  ? 0.19563 0.16847 0.17617 -0.00221 -0.00394 -0.03744 78  ILE A CB  
506  C CG1 . ILE A 71  ? 0.24774 0.20371 0.20991 -0.00650 -0.01234 -0.03899 78  ILE A CG1 
507  C CG2 . ILE A 71  ? 0.27393 0.24680 0.25253 -0.00900 -0.00518 -0.03894 78  ILE A CG2 
508  C CD1 . ILE A 71  ? 0.26932 0.18951 0.19654 -0.00727 -0.01670 -0.04033 78  ILE A CD1 
509  N N   . ASN A 72  ? 0.21264 0.22776 0.25073 -0.01386 -0.00530 -0.03325 79  ASN A N   
510  C CA  . ASN A 72  ? 0.16954 0.19170 0.22518 -0.01761 -0.00210 -0.02702 79  ASN A CA  
511  C C   . ASN A 72  ? 0.20778 0.21678 0.24860 -0.01820 0.00083  -0.03038 79  ASN A C   
512  O O   . ASN A 72  ? 0.21733 0.21888 0.24547 -0.01975 -0.00447 -0.03722 79  ASN A O   
513  C CB  . ASN A 72  ? 0.18584 0.21316 0.25946 -0.02896 -0.01499 -0.02664 79  ASN A CB  
514  C CG  . ASN A 72  ? 0.20309 0.24934 0.29717 -0.03024 -0.02152 -0.01977 79  ASN A CG  
515  O OD1 . ASN A 72  ? 0.18407 0.24674 0.28987 -0.02073 -0.01134 -0.00979 79  ASN A OD1 
516  N ND2 . ASN A 72  ? 0.20251 0.24463 0.29822 -0.04012 -0.03905 -0.02378 79  ASN A ND2 
517  N N   . LEU A 73  ? 0.21885 0.22844 0.26277 -0.01500 0.01047  -0.02258 80  LEU A N   
518  C CA  . LEU A 73  ? 0.19456 0.19281 0.22557 -0.01445 0.01308  -0.02299 80  LEU A CA  
519  C C   . LEU A 73  ? 0.20925 0.20863 0.25885 -0.02155 0.01302  -0.01605 80  LEU A C   
520  O O   . LEU A 73  ? 0.18408 0.19663 0.25459 -0.02312 0.01945  -0.00348 80  LEU A O   
521  C CB  . LEU A 73  ? 0.23085 0.22079 0.24108 -0.00403 0.02327  -0.01878 80  LEU A CB  
522  C CG  . LEU A 73  ? 0.21909 0.19652 0.20490 0.00095  0.01985  -0.02516 80  LEU A CG  
523  C CD1 . LEU A 73  ? 0.24088 0.19669 0.19285 0.01312  0.02752  -0.02273 80  LEU A CD1 
524  C CD2 . LEU A 73  ? 0.20556 0.17928 0.18354 -0.00782 0.00624  -0.03258 80  LEU A CD2 
525  N N   . ILE A 74  ? 0.20215 0.18710 0.24397 -0.02490 0.00618  -0.02165 81  ILE A N   
526  C CA  . ILE A 74  ? 0.20640 0.17872 0.25783 -0.03386 0.00086  -0.01747 81  ILE A CA  
527  C C   . ILE A 74  ? 0.22691 0.18198 0.26276 -0.02833 0.00524  -0.01601 81  ILE A C   
528  O O   . ILE A 74  ? 0.27542 0.21547 0.29295 -0.02191 0.00121  -0.02394 81  ILE A O   
529  C CB  . ILE A 74  ? 0.24226 0.19947 0.28774 -0.03998 -0.01445 -0.02735 81  ILE A CB  
530  C CG1 . ILE A 74  ? 0.26030 0.23692 0.31804 -0.04267 -0.01908 -0.02856 81  ILE A CG1 
531  C CG2 . ILE A 74  ? 0.30105 0.23567 0.35225 -0.05360 -0.02573 -0.02281 81  ILE A CG2 
532  C CD1 . ILE A 74  ? 0.42523 0.38547 0.47229 -0.04844 -0.03625 -0.03767 81  ILE A CD1 
533  N N   . PRO A 75  ? 0.26367 0.22152 0.30472 -0.02740 0.01513  -0.00395 82  PRO A N   
534  C CA  . PRO A 75  ? 0.29262 0.23223 0.31883 -0.02204 0.01815  -0.00058 82  PRO A CA  
535  C C   . PRO A 75  ? 0.39914 0.31189 0.42879 -0.03216 0.01014  0.00247  82  PRO A C   
536  O O   . PRO A 75  ? 0.33927 0.25330 0.39059 -0.04773 0.00382  0.00941  82  PRO A O   
537  C CB  . PRO A 75  ? 0.34263 0.29295 0.36950 -0.01703 0.03194  0.01271  82  PRO A CB  
538  C CG  . PRO A 75  ? 0.29447 0.26516 0.34795 -0.02395 0.03688  0.02247  82  PRO A CG  
539  C CD  . PRO A 75  ? 0.21779 0.19613 0.27700 -0.02785 0.02626  0.00991  82  PRO A CD  
540  N N   . ASN A 76  ? 0.31832 0.20456 0.32543 -0.02328 0.00875  -0.00095 83  ASN A N   
541  C CA  . ASN A 76  ? 0.36433 0.20923 0.36173 -0.03052 -0.00044 0.00036  83  ASN A CA  
542  C C   . ASN A 76  ? 0.39993 0.22692 0.38061 -0.01830 0.00766  0.00797  83  ASN A C   
543  O O   . ASN A 76  ? 0.41216 0.23169 0.37071 0.00062  0.01012  0.00180  83  ASN A O   
544  C CB  . ASN A 76  ? 0.38527 0.20042 0.35768 -0.02603 -0.01278 -0.01568 83  ASN A CB  
545  C CG  . ASN A 76  ? 0.52506 0.28388 0.47812 -0.03642 -0.02761 -0.01646 83  ASN A CG  
546  O OD1 . ASN A 76  ? 0.55091 0.28206 0.49485 -0.03583 -0.02548 -0.00784 83  ASN A OD1 
547  N ND2 . ASN A 76  ? 0.60177 0.33799 0.54417 -0.04681 -0.04513 -0.02656 83  ASN A ND2 
548  N N   . LYS A 77  ? 0.40999 0.23294 0.40328 -0.02803 0.01250  0.02456  84  LYS A N   
549  C CA  . LYS A 77  ? 0.42992 0.23692 0.40651 -0.01574 0.02085  0.03406  84  LYS A CA  
550  C C   . LYS A 77  ? 0.56498 0.31798 0.51270 -0.00949 0.01255  0.02949  84  LYS A C   
551  O O   . LYS A 77  ? 0.53256 0.27351 0.45959 0.00987  0.01895  0.03266  84  LYS A O   
552  C CB  . LYS A 77  ? 0.48425 0.29996 0.47932 -0.02617 0.03060  0.05600  84  LYS A CB  
553  C CG  . LYS A 77  ? 0.56348 0.42007 0.56356 -0.01643 0.04582  0.06259  84  LYS A CG  
554  C CD  . LYS A 77  ? 0.61903 0.48794 0.63884 -0.02455 0.05926  0.08736  84  LYS A CD  
555  C CE  . LYS A 77  ? 0.71435 0.61602 0.72998 -0.01123 0.07555  0.09267  84  LYS A CE  
556  N NZ  . LYS A 77  ? 0.73016 0.65914 0.77885 -0.01969 0.08881  0.11476  84  LYS A NZ  
557  N N   . GLN A 78  ? 0.61874 0.33474 0.56058 -0.02447 -0.00294 0.02308  85  GLN A N   
558  C CA  . GLN A 78  ? 0.69299 0.34205 0.59353 -0.01573 -0.01233 0.01628  85  GLN A CA  
559  C C   . GLN A 78  ? 0.74938 0.39515 0.61868 0.01563  -0.00690 0.00130  85  GLN A C   
560  O O   . GLN A 78  ? 0.64470 0.26055 0.48371 0.03959  -0.00079 0.00276  85  GLN A O   
561  C CB  . GLN A 78  ? 0.79791 0.40047 0.69143 -0.04128 -0.03555 0.01150  85  GLN A CB  
562  C CG  . GLN A 78  ? 1.14464 0.72312 1.05704 -0.07103 -0.04536 0.03165  85  GLN A CG  
563  C CD  . GLN A 78  ? 1.34277 0.98924 1.31450 -0.09080 -0.03625 0.05206  85  GLN A CD  
564  O OE1 . GLN A 78  ? 1.27268 0.96292 1.27164 -0.09843 -0.03818 0.04836  85  GLN A OE1 
565  N NE2 . GLN A 78  ? 1.17981 0.83319 1.16911 -0.09673 -0.02493 0.07571  85  GLN A NE2 
566  N N   . ASP A 79  ? 0.53014 0.20807 0.40753 0.01746  -0.00789 -0.01021 86  ASP A N   
567  C CA  . ASP A 79  ? 0.67879 0.36667 0.53527 0.04675  0.00029  -0.01857 86  ASP A CA  
568  C C   . ASP A 79  ? 0.58555 0.33284 0.46513 0.06006  0.01419  -0.00879 86  ASP A C   
569  O O   . ASP A 79  ? 0.46510 0.22863 0.33523 0.08439  0.02174  -0.00858 86  ASP A O   
570  C CB  . ASP A 79  ? 0.52424 0.22038 0.37779 0.04311  -0.00669 -0.03231 86  ASP A CB  
571  C CG  . ASP A 79  ? 0.82319 0.45665 0.64724 0.02928  -0.02611 -0.04312 86  ASP A CG  
572  O OD1 . ASP A 79  ? 0.82855 0.40122 0.62153 0.03064  -0.03298 -0.04243 86  ASP A OD1 
573  O OD2 . ASP A 79  ? 0.84857 0.48980 0.67669 0.01727  -0.03658 -0.05198 86  ASP A OD2 
574  N N   . ARG A 80  ? 0.45633 0.23464 0.36341 0.04538  0.01685  0.00110  87  ARG A N   
575  C CA  . ARG A 80  ? 0.40167 0.22970 0.32500 0.05233  0.02357  0.00862  87  ARG A CA  
576  C C   . ARG A 80  ? 0.37201 0.23735 0.30648 0.05400  0.02214  0.00148  87  ARG A C   
577  O O   . ARG A 80  ? 0.37202 0.26748 0.31054 0.06757  0.02466  0.00715  87  ARG A O   
578  C CB  . ARG A 80  ? 0.47023 0.29625 0.38063 0.07487  0.02940  0.01981  87  ARG A CB  
579  C CG  . ARG A 80  ? 0.49387 0.36126 0.41816 0.07397  0.03013  0.03026  87  ARG A CG  
580  C CD  . ARG A 80  ? 0.65983 0.54704 0.58139 0.09655  0.03160  0.04120  87  ARG A CD  
581  N NE  . ARG A 80  ? 0.52754 0.37892 0.42934 0.11216  0.03674  0.04972  87  ARG A NE  
582  C CZ  . ARG A 80  ? 0.78275 0.63963 0.67730 0.13898  0.04088  0.06109  87  ARG A CZ  
583  N NH1 . ARG A 80  ? 0.55060 0.45438 0.46179 0.15250  0.04083  0.06810  87  ARG A NH1 
584  N NH2 . ARG A 80  ? 0.65650 0.47248 0.52865 0.15317  0.04560  0.06862  87  ARG A NH2 
585  N N   . THR A 81  ? 0.37092 0.23677 0.31359 0.03857  0.01696  -0.00800 88  THR A N   
586  C CA  . THR A 81  ? 0.31982 0.21697 0.27235 0.03772  0.01544  -0.01359 88  THR A CA  
587  C C   . THR A 81  ? 0.32312 0.24012 0.29429 0.01932  0.01292  -0.01487 88  THR A C   
588  O O   . THR A 81  ? 0.32444 0.23000 0.30302 0.00695  0.01242  -0.01308 88  THR A O   
589  C CB  . THR A 81  ? 0.37438 0.25033 0.31089 0.04286  0.01211  -0.02452 88  THR A CB  
590  O OG1 . THR A 81  ? 0.38904 0.23379 0.32280 0.02562  0.00270  -0.03123 88  THR A OG1 
591  C CG2 . THR A 81  ? 0.35931 0.21207 0.26859 0.06868  0.01815  -0.02313 88  THR A CG2 
592  N N   . LEU A 82  ? 0.26214 0.20895 0.24092 0.01862  0.01168  -0.01528 89  LEU A N   
593  C CA  . LEU A 82  ? 0.21762 0.17680 0.20599 0.00639  0.00952  -0.01872 89  LEU A CA  
594  C C   . LEU A 82  ? 0.25166 0.22170 0.24262 0.00598  0.00567  -0.02521 89  LEU A C   
595  O O   . LEU A 82  ? 0.26724 0.25441 0.25818 0.01270  0.00521  -0.02145 89  LEU A O   
596  C CB  . LEU A 82  ? 0.24893 0.22057 0.23320 0.00521  0.00901  -0.01328 89  LEU A CB  
597  C CG  . LEU A 82  ? 0.23566 0.21191 0.21958 -0.00206 0.00737  -0.01749 89  LEU A CG  
598  C CD1 . LEU A 82  ? 0.23886 0.20817 0.23035 -0.00494 0.01501  -0.01627 89  LEU A CD1 
599  C CD2 . LEU A 82  ? 0.24293 0.21735 0.20793 -0.00168 0.00256  -0.01403 89  LEU A CD2 
600  N N   . THR A 83  ? 0.26795 0.23117 0.26341 -0.00175 0.00272  -0.03173 90  THR A N   
601  C CA  . THR A 83  ? 0.24570 0.21523 0.23980 -0.00161 -0.00107 -0.03763 90  THR A CA  
602  C C   . THR A 83  ? 0.20114 0.18511 0.20465 -0.00980 -0.00268 -0.03784 90  THR A C   
603  O O   . THR A 83  ? 0.29276 0.27542 0.30463 -0.01530 -0.00132 -0.03627 90  THR A O   
604  C CB  . THR A 83  ? 0.24328 0.18825 0.22851 -0.00327 -0.00731 -0.04502 90  THR A CB  
605  O OG1 . THR A 83  ? 0.30128 0.22099 0.26617 0.00836  -0.00577 -0.04615 90  THR A OG1 
606  C CG2 . THR A 83  ? 0.31972 0.26871 0.29746 -0.00100 -0.01126 -0.05077 90  THR A CG2 
607  N N   . ILE A 84  ? 0.17844 0.17564 0.18032 -0.00908 -0.00447 -0.03722 91  ILE A N   
608  C CA  . ILE A 84  ? 0.16853 0.17040 0.17199 -0.01509 -0.00724 -0.03794 91  ILE A CA  
609  C C   . ILE A 84  ? 0.21219 0.21689 0.21517 -0.01427 -0.01000 -0.04141 91  ILE A C   
610  O O   . ILE A 84  ? 0.23351 0.24679 0.23264 -0.00948 -0.00895 -0.03822 91  ILE A O   
611  C CB  . ILE A 84  ? 0.17913 0.18669 0.17702 -0.01888 -0.01119 -0.03226 91  ILE A CB  
612  C CG1 . ILE A 84  ? 0.38652 0.38549 0.37593 -0.01848 -0.01082 -0.02970 91  ILE A CG1 
613  C CG2 . ILE A 84  ? 0.27213 0.27212 0.26287 -0.02399 -0.01541 -0.03390 91  ILE A CG2 
614  C CD1 . ILE A 84  ? 0.33502 0.34456 0.32850 -0.01478 -0.01114 -0.02315 91  ILE A CD1 
615  N N   . VAL A 85  ? 0.19944 0.19985 0.20690 -0.01717 -0.01286 -0.04521 92  VAL A N   
616  C CA  . VAL A 85  ? 0.22273 0.22263 0.22574 -0.01621 -0.01810 -0.04871 92  VAL A CA  
617  C C   . VAL A 85  ? 0.32253 0.32819 0.32805 -0.01816 -0.01913 -0.04632 92  VAL A C   
618  O O   . VAL A 85  ? 0.22063 0.22632 0.23344 -0.01875 -0.01714 -0.04428 92  VAL A O   
619  C CB  . VAL A 85  ? 0.24956 0.23939 0.25581 -0.01995 -0.02633 -0.05287 92  VAL A CB  
620  C CG1 . VAL A 85  ? 0.22771 0.21162 0.21943 -0.01751 -0.03493 -0.05741 92  VAL A CG1 
621  C CG2 . VAL A 85  ? 0.40992 0.38283 0.41073 -0.02022 -0.02732 -0.05493 92  VAL A CG2 
622  N N   . ASP A 86  ? 0.22274 0.23124 0.21989 -0.01647 -0.02087 -0.04504 93  ASP A N   
623  C CA  . ASP A 86  ? 0.18819 0.19572 0.18438 -0.01728 -0.02329 -0.04281 93  ASP A CA  
624  C C   . ASP A 86  ? 0.19280 0.20139 0.18110 -0.01372 -0.02800 -0.04386 93  ASP A C   
625  O O   . ASP A 86  ? 0.23376 0.24075 0.21067 -0.00918 -0.02775 -0.04599 93  ASP A O   
626  C CB  . ASP A 86  ? 0.20097 0.20410 0.19024 -0.02171 -0.02264 -0.03684 93  ASP A CB  
627  C CG  . ASP A 86  ? 0.27582 0.29138 0.26432 -0.02406 -0.02187 -0.02884 93  ASP A CG  
628  O OD1 . ASP A 86  ? 0.25560 0.27548 0.23928 -0.02085 -0.02141 -0.02546 93  ASP A OD1 
629  O OD2 . ASP A 86  ? 0.23557 0.26020 0.22962 -0.02774 -0.02099 -0.02303 93  ASP A OD2 
630  N N   . THR A 87  ? 0.19728 0.22636 0.23799 0.01938  -0.00516 0.00137  94  THR A N   
631  C CA  . THR A 87  ? 0.19172 0.22910 0.24088 0.01967  -0.02143 -0.00588 94  THR A CA  
632  C C   . THR A 87  ? 0.20159 0.22545 0.22456 0.03013  -0.02426 -0.00576 94  THR A C   
633  O O   . THR A 87  ? 0.25172 0.28521 0.28007 0.04028  -0.02948 -0.00266 94  THR A O   
634  C CB  . THR A 87  ? 0.19127 0.25985 0.27938 0.02096  -0.02396 -0.00673 94  THR A CB  
635  O OG1 . THR A 87  ? 0.19546 0.27017 0.28903 0.03089  -0.00938 0.00031  94  THR A OG1 
636  C CG2 . THR A 87  ? 0.19163 0.27142 0.31885 0.00546  -0.02042 -0.00992 94  THR A CG2 
637  N N   . GLY A 88  ? 0.20913 0.21207 0.20841 0.02886  -0.01940 -0.00784 95  GLY A N   
638  C CA  . GLY A 88  ? 0.20415 0.19060 0.19081 0.03478  -0.01709 -0.00938 95  GLY A CA  
639  C C   . GLY A 88  ? 0.21037 0.19180 0.18732 0.03453  -0.02487 -0.00610 95  GLY A C   
640  O O   . GLY A 88  ? 0.25597 0.25168 0.23413 0.03302  -0.03515 -0.00647 95  GLY A O   
641  N N   . ILE A 89  ? 0.28028 0.24289 0.24982 0.03554  -0.01823 -0.00553 96  ILE A N   
642  C CA  . ILE A 89  ? 0.26098 0.21919 0.21971 0.03862  -0.01887 0.00283  96  ILE A CA  
643  C C   . ILE A 89  ? 0.27315 0.23653 0.22012 0.03079  -0.02576 -0.00403 96  ILE A C   
644  O O   . ILE A 89  ? 0.28386 0.25314 0.21722 0.03598  -0.02803 0.00078  96  ILE A O   
645  C CB  . ILE A 89  ? 0.24908 0.18325 0.21488 0.03943  -0.00368 0.00712  96  ILE A CB  
646  C CG1 . ILE A 89  ? 0.30113 0.23185 0.25613 0.04924  0.00282  0.02699  96  ILE A CG1 
647  C CG2 . ILE A 89  ? 0.28276 0.21073 0.25376 0.02581  -0.00184 -0.00991 96  ILE A CG2 
648  C CD1 . ILE A 89  ? 0.31897 0.22196 0.29237 0.05549  0.02417  0.04218  96  ILE A CD1 
649  N N   . GLY A 90  ? 0.23883 0.20182 0.18884 0.02187  -0.02796 -0.01394 97  GLY A N   
650  C CA  . GLY A 90  ? 0.27627 0.24089 0.22087 0.01740  -0.03241 -0.01956 97  GLY A CA  
651  C C   . GLY A 90  ? 0.27399 0.23143 0.21524 0.01587  -0.02587 -0.02073 97  GLY A C   
652  O O   . GLY A 90  ? 0.29128 0.24097 0.23904 0.01539  -0.01728 -0.01833 97  GLY A O   
653  N N   . MET A 91  ? 0.27138 0.23133 0.20984 0.01457  -0.02799 -0.02606 98  MET A N   
654  C CA  . MET A 91  ? 0.20393 0.16356 0.14632 0.01329  -0.02084 -0.02801 98  MET A CA  
655  C C   . MET A 91  ? 0.22384 0.18767 0.15391 0.01812  -0.01803 -0.02941 98  MET A C   
656  O O   . MET A 91  ? 0.27260 0.23920 0.19682 0.02002  -0.02571 -0.03776 98  MET A O   
657  C CB  . MET A 91  ? 0.22307 0.18789 0.17676 0.01134  -0.02518 -0.03455 98  MET A CB  
658  C CG  . MET A 91  ? 0.24190 0.21061 0.20144 0.00934  -0.02739 -0.03768 98  MET A CG  
659  S SD  . MET A 91  ? 0.31171 0.29804 0.27424 0.01489  -0.03584 -0.04151 98  MET A SD  
660  C CE  . MET A 91  ? 0.29307 0.26949 0.24570 0.02006  -0.03630 -0.02798 98  MET A CE  
661  N N   . THR A 92  ? 0.26262 0.22757 0.19188 0.02003  -0.00475 -0.02293 99  THR A N   
662  C CA  . THR A 92  ? 0.27451 0.24792 0.18786 0.02745  0.00188  -0.02465 99  THR A CA  
663  C C   . THR A 92  ? 0.28520 0.26266 0.21439 0.02568  0.00282  -0.03673 99  THR A C   
664  O O   . THR A 92  ? 0.29037 0.26805 0.24249 0.02015  -0.00099 -0.03957 99  THR A O   
665  C CB  . THR A 92  ? 0.32146 0.29553 0.22997 0.03223  0.02214  -0.00697 99  THR A CB  
666  O OG1 . THR A 92  ? 0.30258 0.27252 0.24683 0.02146  0.03322  -0.00655 99  THR A OG1 
667  C CG2 . THR A 92  ? 0.30890 0.27708 0.20473 0.03880  0.02334  0.01049  99  THR A CG2 
668  N N   . LYS A 93  ? 0.25618 0.24094 0.17199 0.03366  0.00800  -0.04468 100 LYS A N   
669  C CA  . LYS A 93  ? 0.25358 0.24272 0.18920 0.03540  0.01250  -0.05414 100 LYS A CA  
670  C C   . LYS A 93  ? 0.27792 0.27700 0.24204 0.03029  0.02468  -0.04586 100 LYS A C   
671  O O   . LYS A 93  ? 0.27345 0.28055 0.26536 0.02897  0.01969  -0.05131 100 LYS A O   
672  C CB  . LYS A 93  ? 0.29067 0.28747 0.20704 0.04667  0.02053  -0.06695 100 LYS A CB  
673  C CG  . LYS A 93  ? 0.30369 0.30098 0.24359 0.05185  0.02384  -0.08029 100 LYS A CG  
674  C CD  . LYS A 93  ? 0.35508 0.36145 0.27420 0.06464  0.03538  -0.09742 100 LYS A CD  
675  C CE  . LYS A 93  ? 0.47360 0.47840 0.42100 0.07279  0.04176  -0.11124 100 LYS A CE  
676  N NZ  . LYS A 93  ? 0.50218 0.51711 0.42734 0.08687  0.05526  -0.13309 100 LYS A NZ  
677  N N   . ALA A 94  ? 0.25752 0.25839 0.21983 0.02814  0.04115  -0.03209 101 ALA A N   
678  C CA  . ALA A 94  ? 0.25371 0.26413 0.25676 0.01911  0.05550  -0.02791 101 ALA A CA  
679  C C   . ALA A 94  ? 0.27994 0.28930 0.31043 0.00750  0.04048  -0.03563 101 ALA A C   
680  O O   . ALA A 94  ? 0.23409 0.26231 0.30379 0.00110  0.03894  -0.04599 101 ALA A O   
681  C CB  . ALA A 94  ? 0.28001 0.28568 0.28102 0.01911  0.08179  -0.00700 101 ALA A CB  
682  N N   . ASP A 95  ? 0.27395 0.26732 0.28492 0.00627  0.02876  -0.03320 102 ASP A N   
683  C CA  . ASP A 95  ? 0.21134 0.20688 0.23813 -0.00069 0.01389  -0.04367 102 ASP A CA  
684  C C   . ASP A 95  ? 0.21756 0.23209 0.25160 0.00448  -0.00179 -0.05440 102 ASP A C   
685  O O   . ASP A 95  ? 0.25752 0.29367 0.31838 0.00093  -0.00958 -0.06640 102 ASP A O   
686  C CB  . ASP A 95  ? 0.28911 0.26758 0.28872 0.00176  0.00503  -0.03840 102 ASP A CB  
687  C CG  . ASP A 95  ? 0.29879 0.26056 0.30137 -0.00130 0.01766  -0.02803 102 ASP A CG  
688  O OD1 . ASP A 95  ? 0.31205 0.27048 0.34435 -0.00871 0.03409  -0.02629 102 ASP A OD1 
689  O OD2 . ASP A 95  ? 0.33327 0.28519 0.31304 0.00474  0.01295  -0.01999 102 ASP A OD2 
690  N N   . LEU A 96  ? 0.21799 0.22568 0.23001 0.01442  -0.00719 -0.05085 103 LEU A N   
691  C CA  . LEU A 96  ? 0.19707 0.21443 0.21410 0.02383  -0.01884 -0.05289 103 LEU A CA  
692  C C   . LEU A 96  ? 0.24539 0.28822 0.29219 0.02898  -0.01631 -0.05860 103 LEU A C   
693  O O   . LEU A 96  ? 0.20115 0.26568 0.26166 0.03730  -0.02833 -0.06022 103 LEU A O   
694  C CB  . LEU A 96  ? 0.20493 0.20195 0.20415 0.03105  -0.01923 -0.04933 103 LEU A CB  
695  C CG  . LEU A 96  ? 0.27163 0.25073 0.25160 0.02685  -0.02403 -0.04502 103 LEU A CG  
696  C CD1 . LEU A 96  ? 0.25939 0.22216 0.23582 0.03004  -0.02304 -0.04948 103 LEU A CD1 
697  C CD2 . LEU A 96  ? 0.25048 0.23413 0.23035 0.02891  -0.03245 -0.03767 103 LEU A CD2 
698  N N   . ILE A 97  ? 0.23024 0.27532 0.28639 0.02759  -0.00011 -0.05999 104 ILE A N   
699  C CA  . ILE A 97  ? 0.21827 0.29024 0.30761 0.03439  0.00492  -0.06531 104 ILE A CA  
700  C C   . ILE A 97  ? 0.21463 0.31635 0.34653 0.02247  0.00795  -0.07328 104 ILE A C   
701  O O   . ILE A 97  ? 0.24705 0.38452 0.41488 0.02737  -0.00074 -0.08203 104 ILE A O   
702  C CB  . ILE A 97  ? 0.22254 0.28708 0.30315 0.04132  0.02413  -0.06512 104 ILE A CB  
703  C CG1 . ILE A 97  ? 0.27690 0.31571 0.32874 0.05210  0.01875  -0.06724 104 ILE A CG1 
704  C CG2 . ILE A 97  ? 0.31240 0.40919 0.43485 0.04754  0.03476  -0.07028 104 ILE A CG2 
705  C CD1 . ILE A 97  ? 0.31308 0.34550 0.34580 0.05904  0.03593  -0.07527 104 ILE A CD1 
706  N N   . ASN A 98  ? 0.21023 0.29971 0.34541 0.00739  0.02087  -0.07108 105 ASN A N   
707  C CA  . ASN A 98  ? 0.21132 0.32543 0.40174 -0.00702 0.03113  -0.08068 105 ASN A CA  
708  C C   . ASN A 98  ? 0.27898 0.38368 0.48330 -0.02335 0.02701  -0.08968 105 ASN A C   
709  O O   . ASN A 98  ? 0.20445 0.33909 0.45479 -0.03326 0.01709  -0.11160 105 ASN A O   
710  C CB  . ASN A 98  ? 0.35318 0.46311 0.55567 -0.00940 0.06397  -0.06769 105 ASN A CB  
711  C CG  . ASN A 98  ? 0.65402 0.79963 0.92933 -0.02158 0.07842  -0.07764 105 ASN A CG  
712  O OD1 . ASN A 98  ? 0.62244 0.80003 0.94173 -0.02909 0.05971  -0.09929 105 ASN A OD1 
713  N ND2 . ASN A 98  ? 0.82900 0.97538 1.11846 -0.02202 0.11202  -0.06295 105 ASN A ND2 
714  N N   . ASN A 99  ? 0.24380 0.30615 0.24496 0.03246  0.04991  -0.02753 106 ASN A N   
715  C CA  . ASN A 99  ? 0.25987 0.31065 0.26633 0.01674  0.03844  -0.01049 106 ASN A CA  
716  C C   . ASN A 99  ? 0.24581 0.27740 0.27399 0.02063  0.03234  -0.01067 106 ASN A C   
717  O O   . ASN A 99  ? 0.25239 0.29138 0.29419 0.01061  0.02957  -0.00038 106 ASN A O   
718  C CB  . ASN A 99  ? 0.27415 0.30053 0.26360 0.00806  0.02596  -0.00496 106 ASN A CB  
719  C CG  . ASN A 99  ? 0.42921 0.47108 0.38943 0.00179  0.02925  -0.00258 106 ASN A CG  
720  O OD1 . ASN A 99  ? 0.36656 0.43805 0.31924 -0.00406 0.04139  0.00133  106 ASN A OD1 
721  N ND2 . ASN A 99  ? 0.51950 0.54222 0.46259 0.00164  0.01803  -0.00545 106 ASN A ND2 
722  N N   . LEU A 100 ? 0.20624 0.21069 0.23604 0.03263  0.03062  -0.02273 107 LEU A N   
723  C CA  . LEU A 100 ? 0.27109 0.25337 0.31527 0.03387  0.02598  -0.02310 107 LEU A CA  
724  C C   . LEU A 100 ? 0.23719 0.24024 0.29248 0.04075  0.03043  -0.02157 107 LEU A C   
725  O O   . LEU A 100 ? 0.24134 0.24099 0.30748 0.03428  0.02537  -0.01611 107 LEU A O   
726  C CB  . LEU A 100 ? 0.27571 0.22414 0.31656 0.04381  0.02656  -0.03704 107 LEU A CB  
727  C CG  . LEU A 100 ? 0.32018 0.24824 0.35731 0.03647  0.01863  -0.04057 107 LEU A CG  
728  C CD1 . LEU A 100 ? 0.34218 0.25243 0.36109 0.03915  0.01695  -0.04503 107 LEU A CD1 
729  C CD2 . LEU A 100 ? 0.34846 0.26679 0.39829 0.02166  0.00799  -0.02970 107 LEU A CD2 
730  N N   . GLY A 101 ? 0.23937 0.26517 0.29375 0.05422  0.03914  -0.02776 108 GLY A N   
731  C CA  . GLY A 101 ? 0.28989 0.33986 0.35869 0.06317  0.04078  -0.02678 108 GLY A CA  
732  C C   . GLY A 101 ? 0.28869 0.37490 0.37063 0.04860  0.04003  -0.01705 108 GLY A C   
733  O O   . GLY A 101 ? 0.25656 0.35707 0.35335 0.04845  0.03556  -0.01407 108 GLY A O   
734  N N   . THR A 102 ? 0.21587 0.31770 0.29117 0.03536  0.04471  -0.01232 109 THR A N   
735  C CA  . THR A 102 ? 0.18421 0.31543 0.27123 0.01799  0.04606  -0.00243 109 THR A CA  
736  C C   . THR A 102 ? 0.25509 0.36685 0.35066 0.00462  0.03548  0.00593  109 THR A C   
737  O O   . THR A 102 ? 0.22386 0.35714 0.33789 -0.00179 0.03399  0.00810  109 THR A O   
738  C CB  . THR A 102 ? 0.23929 0.37937 0.30947 0.00386  0.05280  0.00397  109 THR A CB  
739  O OG1 . THR A 102 ? 0.31766 0.48180 0.38197 0.01486  0.06530  -0.00698 109 THR A OG1 
740  C CG2 . THR A 102 ? 0.30943 0.47272 0.39002 -0.01718 0.05585  0.01571  109 THR A CG2 
741  N N   . ILE A 103 ? 0.22593 0.29847 0.31106 0.00044  0.02817  0.00819  110 ILE A N   
742  C CA  . ILE A 103 ? 0.27030 0.32113 0.36604 -0.01101 0.01957  0.01237  110 ILE A CA  
743  C C   . ILE A 103 ? 0.34832 0.39739 0.45238 -0.00143 0.01691  0.00497  110 ILE A C   
744  O O   . ILE A 103 ? 0.31128 0.36770 0.42861 -0.01150 0.01305  0.00694  110 ILE A O   
745  C CB  . ILE A 103 ? 0.24585 0.25663 0.33335 -0.01423 0.01277  0.01264  110 ILE A CB  
746  C CG1 . ILE A 103 ? 0.31220 0.32383 0.38791 -0.02390 0.01150  0.02299  110 ILE A CG1 
747  C CG2 . ILE A 103 ? 0.37932 0.36775 0.48184 -0.02541 0.00602  0.01341  110 ILE A CG2 
748  C CD1 . ILE A 103 ? 0.41000 0.43530 0.49416 -0.04333 0.01188  0.03746  110 ILE A CD1 
749  N N   . ALA A 104 ? 0.21595 0.25446 0.31049 0.01764  0.01887  -0.00353 111 ALA A N   
750  C CA  . ALA A 104 ? 0.19541 0.22464 0.29049 0.02708  0.01515  -0.00789 111 ALA A CA  
751  C C   . ALA A 104 ? 0.31902 0.38843 0.42845 0.03019  0.01278  -0.00622 111 ALA A C   
752  O O   . ALA A 104 ? 0.29304 0.35889 0.40310 0.03177  0.00598  -0.00703 111 ALA A O   
753  C CB  . ALA A 104 ? 0.19612 0.20099 0.27649 0.04702  0.01892  -0.01574 111 ALA A CB  
754  N N   . LYS A 105 ? 0.21520 0.32427 0.33623 0.03023  0.01823  -0.00504 112 LYS A N   
755  C CA  . LYS A 105 ? 0.21989 0.37272 0.36110 0.03432  0.01600  -0.00641 112 LYS A CA  
756  C C   . LYS A 105 ? 0.23910 0.40091 0.39277 0.01589  0.00853  -0.00333 112 LYS A C   
757  O O   . LYS A 105 ? 0.21247 0.38973 0.37415 0.02172  -0.00021 -0.00610 112 LYS A O   
758  C CB  . LYS A 105 ? 0.20864 0.40259 0.36238 0.03301  0.02691  -0.00786 112 LYS A CB  
759  C CG  . LYS A 105 ? 0.31009 0.55343 0.48962 0.04413  0.02715  -0.01405 112 LYS A CG  
760  C CD  . LYS A 105 ? 0.34217 0.62542 0.53434 0.03537  0.04217  -0.01665 112 LYS A CD  
761  C CE  . LYS A 105 ? 0.51718 0.85318 0.74117 0.04919  0.04469  -0.02691 112 LYS A CE  
762  N NZ  . LYS A 105 ? 0.52006 0.88405 0.76813 0.03692  0.03662  -0.02648 112 LYS A NZ  
763  N N   . SER A 106 ? 0.22797 0.37913 0.38322 -0.00633 0.01087  0.00211  113 SER A N   
764  C CA  . SER A 106 ? 0.18129 0.34177 0.35169 -0.02463 0.00543  0.00254  113 SER A CA  
765  C C   . SER A 106 ? 0.20024 0.32455 0.35916 -0.02510 -0.00260 -0.00095 113 SER A C   
766  O O   . SER A 106 ? 0.18694 0.32388 0.35378 -0.03151 -0.00946 -0.00494 113 SER A O   
767  C CB  . SER A 106 ? 0.28360 0.44353 0.46268 -0.04886 0.01121  0.00995  113 SER A CB  
768  O OG  . SER A 106 ? 0.41019 0.52845 0.57342 -0.05172 0.01182  0.01521  113 SER A OG  
769  N N   . GLY A 107 ? 0.22647 0.30789 0.36680 -0.01929 -0.00125 -0.00131 114 GLY A N   
770  C CA  . GLY A 107 ? 0.23421 0.28150 0.36268 -0.02044 -0.00556 -0.00656 114 GLY A CA  
771  C C   . GLY A 107 ? 0.25930 0.31241 0.37537 -0.00378 -0.01141 -0.00950 114 GLY A C   
772  O O   . GLY A 107 ? 0.18738 0.23251 0.29648 -0.00958 -0.01718 -0.01304 114 GLY A O   
773  N N   . THR A 108 ? 0.19190 0.25817 0.30412 0.01726  -0.01033 -0.00809 115 THR A N   
774  C CA  . THR A 108 ? 0.19808 0.27064 0.30059 0.03646  -0.01799 -0.00838 115 THR A CA  
775  C C   . THR A 108 ? 0.17144 0.28663 0.29039 0.03152  -0.02871 -0.00899 115 THR A C   
776  O O   . THR A 108 ? 0.24536 0.35488 0.35075 0.03454  -0.03907 -0.00943 115 THR A O   
777  C CB  . THR A 108 ? 0.19278 0.27545 0.29670 0.05995  -0.01375 -0.00811 115 THR A CB  
778  O OG1 . THR A 108 ? 0.35312 0.39374 0.43958 0.06441  -0.00490 -0.00987 115 THR A OG1 
779  C CG2 . THR A 108 ? 0.28766 0.37962 0.38686 0.08182  -0.02404 -0.00669 115 THR A CG2 
780  N N   . LYS A 109 ? 0.15021 0.30968 0.29737 0.02341  -0.02624 -0.00960 116 LYS A N   
781  C CA  . LYS A 109 ? 0.20665 0.41189 0.37590 0.01602  -0.03554 -0.01301 116 LYS A CA  
782  C C   . LYS A 109 ? 0.24077 0.43094 0.40301 -0.00440 -0.04158 -0.01622 116 LYS A C   
783  O O   . LYS A 109 ? 0.21925 0.42704 0.38001 -0.00289 -0.05457 -0.01977 116 LYS A O   
784  C CB  . LYS A 109 ? 0.15779 0.40573 0.35816 0.00364  -0.02660 -0.01411 116 LYS A CB  
785  C CG  . LYS A 109 ? 0.25191 0.55074 0.48238 -0.00979 -0.03320 -0.02031 116 LYS A CG  
786  C CD  . LYS A 109 ? 0.35911 0.69933 0.61870 -0.01890 -0.02068 -0.02164 116 LYS A CD  
787  C CE  . LYS A 109 ? 0.52634 0.89078 0.80572 -0.03360 -0.02355 -0.02638 116 LYS A CE  
788  N NZ  . LYS A 109 ? 0.69128 1.07263 0.97284 -0.02366 -0.04229 -0.03248 116 LYS A NZ  
789  N N   . ALA A 110 ? 0.16871 0.32689 0.32722 -0.02335 -0.03296 -0.01603 117 ALA A N   
790  C CA  . ALA A 110 ? 0.21932 0.36317 0.37554 -0.04414 -0.03609 -0.02204 117 ALA A CA  
791  C C   . ALA A 110 ? 0.22924 0.33863 0.35243 -0.03613 -0.04188 -0.02451 117 ALA A C   
792  O O   . ALA A 110 ? 0.21830 0.33328 0.33444 -0.04567 -0.04997 -0.03077 117 ALA A O   
793  C CB  . ALA A 110 ? 0.16058 0.27688 0.32549 -0.06381 -0.02553 -0.02136 117 ALA A CB  
794  N N   . PHE A 111 ? 0.17808 0.25125 0.27894 -0.02018 -0.03694 -0.02039 118 PHE A N   
795  C CA  . PHE A 111 ? 0.19631 0.23220 0.26237 -0.01366 -0.03939 -0.02157 118 PHE A CA  
796  C C   . PHE A 111 ? 0.25012 0.30900 0.30258 0.00181  -0.05469 -0.01821 118 PHE A C   
797  O O   . PHE A 111 ? 0.24265 0.29105 0.27146 -0.00443 -0.06209 -0.02097 118 PHE A O   
798  C CB  . PHE A 111 ? 0.19829 0.19350 0.24790 0.00011  -0.02944 -0.01853 118 PHE A CB  
799  C CG  . PHE A 111 ? 0.22686 0.17809 0.23875 0.00580  -0.02809 -0.01909 118 PHE A CG  
800  C CD1 . PHE A 111 ? 0.25858 0.18822 0.25452 -0.01302 -0.02642 -0.02646 118 PHE A CD1 
801  C CD2 . PHE A 111 ? 0.30815 0.23780 0.30043 0.02826  -0.02636 -0.01313 118 PHE A CD2 
802  C CE1 . PHE A 111 ? 0.31656 0.20329 0.27323 -0.01019 -0.02230 -0.02679 118 PHE A CE1 
803  C CE2 . PHE A 111 ? 0.37437 0.25965 0.32969 0.03194  -0.02303 -0.01215 118 PHE A CE2 
804  C CZ  . PHE A 111 ? 0.33710 0.20046 0.27280 0.01165  -0.02043 -0.01868 118 PHE A CZ  
805  N N   . MET A 112 ? 0.21645 0.30896 0.28446 0.02186  -0.06039 -0.01299 119 MET A N   
806  C CA  . MET A 112 ? 0.28192 0.39782 0.34158 0.03999  -0.07797 -0.00931 119 MET A CA  
807  C C   . MET A 112 ? 0.26748 0.42476 0.34105 0.02435  -0.09109 -0.01605 119 MET A C   
808  O O   . MET A 112 ? 0.29180 0.45193 0.34318 0.02992  -0.10710 -0.01484 119 MET A O   
809  C CB  . MET A 112 ? 0.27018 0.41472 0.35075 0.06611  -0.08018 -0.00498 119 MET A CB  
810  C CG  . MET A 112 ? 0.39836 0.50356 0.46742 0.07883  -0.06562 -0.00144 119 MET A CG  
811  S SD  . MET A 112 ? 0.57465 0.67519 0.63767 0.11705  -0.07147 0.00538  119 MET A SD  
812  C CE  . MET A 112 ? 0.45918 0.61445 0.57029 0.12246  -0.06281 -0.00114 119 MET A CE  
813  N N   . GLU A 113 ? 0.22819 0.41599 0.33610 0.00362  -0.08486 -0.02321 120 GLU A N   
814  C CA  . GLU A 113 ? 0.28986 0.51374 0.41198 -0.01502 -0.09538 -0.03258 120 GLU A CA  
815  C C   . GLU A 113 ? 0.25387 0.44147 0.34470 -0.03355 -0.09552 -0.03847 120 GLU A C   
816  O O   . GLU A 113 ? 0.31509 0.51976 0.39335 -0.03807 -0.11046 -0.04382 120 GLU A O   
817  C CB  . GLU A 113 ? 0.25223 0.51125 0.41788 -0.03490 -0.08570 -0.03861 120 GLU A CB  
818  C CG  . GLU A 113 ? 0.38060 0.68274 0.57701 -0.01848 -0.08463 -0.03548 120 GLU A CG  
819  C CD  . GLU A 113 ? 0.58829 0.92256 0.82318 -0.03952 -0.07252 -0.03989 120 GLU A CD  
820  O OE1 . GLU A 113 ? 0.66850 0.97503 0.90160 -0.06336 -0.06261 -0.04075 120 GLU A OE1 
821  O OE2 . GLU A 113 ? 0.57449 0.93821 0.83027 -0.02975 -0.06927 -0.03865 120 GLU A OE2 
822  N N   . ALA A 114 ? 0.23124 0.37006 0.30927 -0.04409 -0.07930 -0.03892 121 ALA A N   
823  C CA  . ALA A 114 ? 0.25856 0.36038 0.30844 -0.06174 -0.07563 -0.04697 121 ALA A CA  
824  C C   . ALA A 114 ? 0.33372 0.41234 0.33542 -0.04741 -0.08563 -0.04175 121 ALA A C   
825  O O   . ALA A 114 ? 0.35779 0.43022 0.33417 -0.06121 -0.09119 -0.04934 121 ALA A O   
826  C CB  . ALA A 114 ? 0.26995 0.32534 0.32092 -0.07127 -0.05640 -0.04880 121 ALA A CB  
827  N N   . LEU A 115 ? 0.29713 0.35879 0.28279 -0.02079 -0.08687 -0.02888 122 LEU A N   
828  C CA  . LEU A 115 ? 0.36494 0.40046 0.30253 -0.00557 -0.09695 -0.02047 122 LEU A CA  
829  C C   . LEU A 115 ? 0.46328 0.54190 0.39610 -0.00055 -0.12160 -0.01983 122 LEU A C   
830  O O   . LEU A 115 ? 0.40719 0.46902 0.29681 -0.00425 -0.13132 -0.01891 122 LEU A O   
831  C CB  . LEU A 115 ? 0.38739 0.40016 0.31597 0.02339  -0.09435 -0.00707 122 LEU A CB  
832  C CG  . LEU A 115 ? 0.38454 0.34660 0.30620 0.01946  -0.07174 -0.00835 122 LEU A CG  
833  C CD1 . LEU A 115 ? 0.43366 0.38317 0.35722 0.04675  -0.06858 0.00154  122 LEU A CD1 
834  C CD2 . LEU A 115 ? 0.40573 0.31475 0.28300 0.00501  -0.06206 -0.01195 122 LEU A CD2 
835  N N   . GLN A 116 ? 0.35529 0.49113 0.33197 0.00716  -0.13197 -0.02113 123 GLN A N   
836  C CA  . GLN A 116 ? 0.40788 0.59390 0.39012 0.01193  -0.15721 -0.02340 123 GLN A CA  
837  C C   . GLN A 116 ? 0.51209 0.70749 0.48430 -0.01830 -0.16080 -0.03806 123 GLN A C   
838  O O   . GLN A 116 ? 0.53412 0.74927 0.48398 -0.01684 -0.18248 -0.03939 123 GLN A O   
839  C CB  . GLN A 116 ? 0.38062 0.62840 0.42123 0.02017  -0.16165 -0.02680 123 GLN A CB  
840  C CG  . GLN A 116 ? 0.54471 0.79777 0.59377 0.05493  -0.16698 -0.01462 123 GLN A CG  
841  C CD  . GLN A 116 ? 0.86481 1.10405 0.87446 0.07951  -0.18986 -0.00272 123 GLN A CD  
842  O OE1 . GLN A 116 ? 0.85919 1.13672 0.86937 0.08225  -0.21430 -0.00532 123 GLN A OE1 
843  N NE2 . GLN A 116 ? 0.95330 1.13586 0.92695 0.09683  -0.18266 0.01062  123 GLN A NE2 
844  N N   . ALA A 117 ? 0.37944 0.53811 0.37509 -0.10153 -0.12847 -0.07613 124 ALA A N   
845  C CA  . ALA A 117 ? 0.41506 0.55167 0.39670 -0.11331 -0.13340 -0.09460 124 ALA A CA  
846  C C   . ALA A 117 ? 0.55479 0.66972 0.50185 -0.10880 -0.12540 -0.10973 124 ALA A C   
847  O O   . ALA A 117 ? 0.57355 0.66440 0.50770 -0.11521 -0.12565 -0.12727 124 ALA A O   
848  C CB  . ALA A 117 ? 0.41811 0.53631 0.42189 -0.12269 -0.13186 -0.10103 124 ALA A CB  
849  N N   . GLY A 118 ? 0.50326 0.62549 0.43583 -0.09715 -0.11745 -0.10289 125 GLY A N   
850  C CA  . GLY A 118 ? 0.51529 0.62334 0.41506 -0.09297 -0.10946 -0.11393 125 GLY A CA  
851  C C   . GLY A 118 ? 0.53392 0.62759 0.43045 -0.08369 -0.09243 -0.11951 125 GLY A C   
852  O O   . GLY A 118 ? 0.49264 0.57829 0.36392 -0.07928 -0.08378 -0.12636 125 GLY A O   
853  N N   . ALA A 119 ? 0.36586 0.45549 0.28881 -0.07903 -0.08621 -0.11452 126 ALA A N   
854  C CA  . ALA A 119 ? 0.36748 0.44142 0.29178 -0.06700 -0.06955 -0.11526 126 ALA A CA  
855  C C   . ALA A 119 ? 0.44911 0.53472 0.35975 -0.05743 -0.06418 -0.10172 126 ALA A C   
856  O O   . ALA A 119 ? 0.40495 0.50909 0.30976 -0.05774 -0.07326 -0.08894 126 ALA A O   
857  C CB  . ALA A 119 ? 0.31386 0.37977 0.27010 -0.06239 -0.06501 -0.10708 126 ALA A CB  
858  N N   . ASP A 120 ? 0.39866 0.47338 0.30525 -0.04901 -0.04988 -0.10368 127 ASP A N   
859  C CA  . ASP A 120 ? 0.47191 0.55486 0.36886 -0.04155 -0.04516 -0.08898 127 ASP A CA  
860  C C   . ASP A 120 ? 0.34079 0.41644 0.25901 -0.03183 -0.03581 -0.07968 127 ASP A C   
861  O O   . ASP A 120 ? 0.32322 0.38788 0.26045 -0.03013 -0.03127 -0.08536 127 ASP A O   
862  C CB  . ASP A 120 ? 0.52684 0.60977 0.39338 -0.04273 -0.03754 -0.09652 127 ASP A CB  
863  C CG  . ASP A 120 ? 0.54239 0.61216 0.41175 -0.03880 -0.02243 -0.11002 127 ASP A CG  
864  O OD1 . ASP A 120 ? 0.65428 0.71323 0.52708 -0.04182 -0.02188 -0.12780 127 ASP A OD1 
865  O OD2 . ASP A 120 ? 0.46803 0.53789 0.33873 -0.03257 -0.01171 -0.10252 127 ASP A OD2 
866  N N   . ILE A 121 ? 0.31244 0.39334 0.22599 -0.02585 -0.03408 -0.06473 128 ILE A N   
867  C CA  . ILE A 121 ? 0.30980 0.38511 0.24105 -0.01738 -0.02794 -0.05467 128 ILE A CA  
868  C C   . ILE A 121 ? 0.35876 0.42253 0.29623 -0.01516 -0.01569 -0.06375 128 ILE A C   
869  O O   . ILE A 121 ? 0.30919 0.36739 0.26590 -0.01014 -0.01221 -0.06016 128 ILE A O   
870  C CB  . ILE A 121 ? 0.36633 0.44514 0.28716 -0.01251 -0.02907 -0.03896 128 ILE A CB  
871  C CG1 . ILE A 121 ? 0.41450 0.50549 0.34101 -0.01031 -0.04150 -0.02797 128 ILE A CG1 
872  C CG2 . ILE A 121 ? 0.28422 0.35310 0.21616 -0.00543 -0.02081 -0.03214 128 ILE A CG2 
873  C CD1 . ILE A 121 ? 0.46520 0.55993 0.37655 -0.00646 -0.04651 -0.01358 128 ILE A CD1 
874  N N   . SER A 122 ? 0.32144 0.38335 0.24356 -0.01843 -0.00913 -0.07617 129 SER A N   
875  C CA  . SER A 122 ? 0.31535 0.36996 0.24705 -0.01448 0.00283  -0.08423 129 SER A CA  
876  C C   . SER A 122 ? 0.35200 0.39610 0.30556 -0.01281 0.00212  -0.09292 129 SER A C   
877  O O   . SER A 122 ? 0.34486 0.38342 0.31242 -0.00739 0.01015  -0.09595 129 SER A O   
878  C CB  . SER A 122 ? 0.34259 0.40056 0.25396 -0.01692 0.01182  -0.09641 129 SER A CB  
879  O OG  . SER A 122 ? 0.44743 0.50096 0.35108 -0.02104 0.00878  -0.11354 129 SER A OG  
880  N N   . MET A 123 ? 0.28772 0.32927 0.24541 -0.01801 -0.00780 -0.09631 130 MET A N   
881  C CA  . MET A 123 ? 0.27545 0.30446 0.25466 -0.01751 -0.00883 -0.10146 130 MET A CA  
882  C C   . MET A 123 ? 0.25645 0.28718 0.25667 -0.01409 -0.01154 -0.08619 130 MET A C   
883  O O   . MET A 123 ? 0.28288 0.30448 0.30039 -0.01514 -0.01380 -0.08689 130 MET A O   
884  C CB  . MET A 123 ? 0.28165 0.30402 0.25858 -0.02660 -0.01764 -0.11282 130 MET A CB  
885  C CG  . MET A 123 ? 0.42434 0.44284 0.37766 -0.03041 -0.01531 -0.13173 130 MET A CG  
886  S SD  . MET A 123 ? 0.52318 0.54848 0.45707 -0.04398 -0.02974 -0.13856 130 MET A SD  
887  C CE  . MET A 123 ? 0.55949 0.56067 0.51043 -0.05035 -0.03482 -0.15332 130 MET A CE  
888  N N   . ILE A 124 ? 0.23604 0.27652 0.23389 -0.00997 -0.01088 -0.07294 131 ILE A N   
889  C CA  . ILE A 124 ? 0.20322 0.24752 0.21653 -0.00652 -0.01354 -0.05971 131 ILE A CA  
890  C C   . ILE A 124 ? 0.24671 0.28161 0.27795 -0.00286 -0.00930 -0.05940 131 ILE A C   
891  O O   . ILE A 124 ? 0.20062 0.23662 0.24577 -0.00340 -0.01275 -0.05201 131 ILE A O   
892  C CB  . ILE A 124 ? 0.20791 0.25896 0.21291 -0.00123 -0.01211 -0.04886 131 ILE A CB  
893  C CG1 . ILE A 124 ? 0.17029 0.22568 0.18865 0.00349  -0.01419 -0.03751 131 ILE A CG1 
894  C CG2 . ILE A 124 ? 0.23358 0.27917 0.23290 0.00188  -0.00324 -0.05124 131 ILE A CG2 
895  C CD1 . ILE A 124 ? 0.22912 0.28705 0.23924 0.00997  -0.01374 -0.02784 131 ILE A CD1 
896  N N   . GLY A 125 ? 0.24286 0.27059 0.27478 0.00085  -0.00194 -0.06644 132 GLY A N   
897  C CA  . GLY A 125 ? 0.26491 0.28506 0.31476 0.00536  0.00071  -0.06483 132 GLY A CA  
898  C C   . GLY A 125 ? 0.34034 0.34815 0.40245 0.00219  -0.00317 -0.06973 132 GLY A C   
899  O O   . GLY A 125 ? 0.29987 0.30167 0.37773 0.00480  -0.00391 -0.06346 132 GLY A O   
900  N N   . GLN A 126 ? 0.22177 0.22457 0.27614 -0.00429 -0.00661 -0.08024 133 GLN A N   
901  C CA  . GLN A 126 ? 0.28678 0.27428 0.35313 -0.00925 -0.01162 -0.08449 133 GLN A CA  
902  C C   . GLN A 126 ? 0.35038 0.34404 0.42806 -0.01506 -0.01856 -0.06991 133 GLN A C   
903  O O   . GLN A 126 ? 0.33612 0.31734 0.42729 -0.01988 -0.02257 -0.06814 133 GLN A O   
904  C CB  . GLN A 126 ? 0.34447 0.32362 0.39806 -0.01630 -0.01459 -0.10141 133 GLN A CB  
905  C CG  . GLN A 126 ? 0.38586 0.35914 0.42827 -0.00960 -0.00543 -0.11789 133 GLN A CG  
906  C CD  . GLN A 126 ? 0.65821 0.62735 0.68007 -0.01637 -0.00743 -0.13576 133 GLN A CD  
907  O OE1 . GLN A 126 ? 0.48179 0.43607 0.50533 -0.02421 -0.01469 -0.14457 133 GLN A OE1 
908  N NE2 . GLN A 126 ? 0.54620 0.52806 0.54728 -0.01434 -0.00115 -0.14125 133 GLN A NE2 
909  N N   . PHE A 127 ? 0.18303 0.19529 0.25662 -0.01394 -0.01921 -0.05863 134 PHE A N   
910  C CA  . PHE A 127 ? 0.20073 0.22421 0.28504 -0.01804 -0.02375 -0.04499 134 PHE A CA  
911  C C   . PHE A 127 ? 0.22264 0.25228 0.31270 -0.01042 -0.01949 -0.03255 134 PHE A C   
912  O O   . PHE A 127 ? 0.20815 0.25105 0.30435 -0.01186 -0.02106 -0.02121 134 PHE A O   
913  C CB  . PHE A 127 ? 0.19060 0.23267 0.26702 -0.02200 -0.02867 -0.04270 134 PHE A CB  
914  C CG  . PHE A 127 ? 0.20416 0.24218 0.27226 -0.03095 -0.03462 -0.05511 134 PHE A CG  
915  C CD1 . PHE A 127 ? 0.20222 0.23880 0.28061 -0.04303 -0.04249 -0.05618 134 PHE A CD1 
916  C CD2 . PHE A 127 ? 0.19976 0.23458 0.24870 -0.02848 -0.03227 -0.06624 134 PHE A CD2 
917  C CE1 . PHE A 127 ? 0.22782 0.25926 0.29623 -0.05243 -0.04920 -0.06970 134 PHE A CE1 
918  C CE2 . PHE A 127 ? 0.21419 0.24574 0.25151 -0.03683 -0.03780 -0.07895 134 PHE A CE2 
919  C CZ  . PHE A 127 ? 0.24514 0.27402 0.29166 -0.04876 -0.04677 -0.08175 134 PHE A CZ  
920  N N   . GLY A 128 ? 0.24303 0.26567 0.33085 -0.00265 -0.01410 -0.03495 135 GLY A N   
921  C CA  . GLY A 128 ? 0.23319 0.25989 0.32494 0.00357  -0.01136 -0.02503 135 GLY A CA  
922  C C   . GLY A 128 ? 0.24740 0.28710 0.32871 0.00809  -0.00955 -0.01998 135 GLY A C   
923  O O   . GLY A 128 ? 0.22853 0.27222 0.31113 0.01219  -0.00815 -0.01229 135 GLY A O   
924  N N   . VAL A 129 ? 0.18349 0.22871 0.25349 0.00765  -0.01016 -0.02389 136 VAL A N   
925  C CA  . VAL A 129 ? 0.16927 0.22319 0.23042 0.01291  -0.00926 -0.01847 136 VAL A CA  
926  C C   . VAL A 129 ? 0.13904 0.18789 0.18661 0.01507  -0.00670 -0.02365 136 VAL A C   
927  O O   . VAL A 129 ? 0.18514 0.23786 0.22278 0.01755  -0.00779 -0.02083 136 VAL A O   
928  C CB  . VAL A 129 ? 0.12608 0.19419 0.18852 0.01156  -0.01334 -0.01359 136 VAL A CB  
929  C CG1 . VAL A 129 ? 0.15058 0.22743 0.22709 0.00903  -0.01404 -0.00587 136 VAL A CG1 
930  C CG2 . VAL A 129 ? 0.14741 0.21729 0.20650 0.00469  -0.01824 -0.01982 136 VAL A CG2 
931  N N   . GLY A 130 ? 0.15122 0.19218 0.19937 0.01437  -0.00308 -0.03024 137 GLY A N   
932  C CA  . GLY A 130 ? 0.15647 0.19567 0.19262 0.01465  0.00058  -0.03393 137 GLY A CA  
933  C C   . GLY A 130 ? 0.20044 0.23881 0.23060 0.01806  0.00165  -0.02760 137 GLY A C   
934  O O   . GLY A 130 ? 0.20615 0.24276 0.22444 0.01695  0.00323  -0.02731 137 GLY A O   
935  N N   . PHE A 131 ? 0.14612 0.18445 0.18286 0.02142  0.00067  -0.02261 138 PHE A N   
936  C CA  . PHE A 131 ? 0.16475 0.19927 0.19393 0.02434  0.00079  -0.01871 138 PHE A CA  
937  C C   . PHE A 131 ? 0.19085 0.22304 0.20740 0.02628  -0.00094 -0.01584 138 PHE A C   
938  O O   . PHE A 131 ? 0.21070 0.23470 0.21779 0.02582  -0.00022 -0.01453 138 PHE A O   
939  C CB  . PHE A 131 ? 0.20218 0.23878 0.23578 0.02824  -0.00067 -0.01456 138 PHE A CB  
940  C CG  . PHE A 131 ? 0.18785 0.21799 0.21074 0.03201  -0.00114 -0.01294 138 PHE A CG  
941  C CD1 . PHE A 131 ? 0.22386 0.24682 0.24358 0.02941  -0.00092 -0.01463 138 PHE A CD1 
942  C CD2 . PHE A 131 ? 0.17351 0.20485 0.19082 0.03819  -0.00200 -0.01037 138 PHE A CD2 
943  C CE1 . PHE A 131 ? 0.23414 0.24671 0.24278 0.03151  -0.00227 -0.01472 138 PHE A CE1 
944  C CE2 . PHE A 131 ? 0.25411 0.27514 0.26071 0.04298  -0.00230 -0.01093 138 PHE A CE2 
945  C CZ  . PHE A 131 ? 0.20894 0.21854 0.21018 0.03893  -0.00282 -0.01358 138 PHE A CZ  
946  N N   . TYR A 132 ? 0.16797 0.20759 0.18557 0.02812  -0.00400 -0.01373 139 TYR A N   
947  C CA  . TYR A 132 ? 0.15180 0.19096 0.16022 0.03249  -0.00690 -0.00920 139 TYR A CA  
948  C C   . TYR A 132 ? 0.17412 0.20869 0.17008 0.02815  -0.00733 -0.00935 139 TYR A C   
949  O O   . TYR A 132 ? 0.20208 0.23205 0.18846 0.03168  -0.01013 -0.00373 139 TYR A O   
950  C CB  . TYR A 132 ? 0.18316 0.23687 0.19949 0.03535  -0.01058 -0.00606 139 TYR A CB  
951  C CG  . TYR A 132 ? 0.19403 0.25430 0.22079 0.03916  -0.00857 -0.00426 139 TYR A CG  
952  C CD1 . TYR A 132 ? 0.19131 0.24955 0.21471 0.04828  -0.00693 -0.00182 139 TYR A CD1 
953  C CD2 . TYR A 132 ? 0.14365 0.20995 0.18169 0.03366  -0.00793 -0.00522 139 TYR A CD2 
954  C CE1 . TYR A 132 ? 0.16323 0.22923 0.19268 0.05142  -0.00399 -0.00059 139 TYR A CE1 
955  C CE2 . TYR A 132 ? 0.19337 0.26629 0.23874 0.03598  -0.00573 -0.00158 139 TYR A CE2 
956  C CZ  . TYR A 132 ? 0.16167 0.23640 0.20185 0.04470  -0.00340 0.00063  139 TYR A CZ  
957  O OH  . TYR A 132 ? 0.18388 0.26757 0.22836 0.04655  -0.00039 0.00402  139 TYR A OH  
958  N N   . SER A 133 ? 0.23201 0.26738 0.22734 0.02133  -0.00418 -0.01520 140 SER A N   
959  C CA  . SER A 133 ? 0.19599 0.22935 0.17690 0.01658  -0.00286 -0.01512 140 SER A CA  
960  C C   . SER A 133 ? 0.21614 0.23844 0.18946 0.01574  -0.00022 -0.01021 140 SER A C   
961  O O   . SER A 133 ? 0.21965 0.23946 0.17946 0.01157  0.00061  -0.00647 140 SER A O   
962  C CB  . SER A 133 ? 0.21896 0.25712 0.20072 0.01070  0.00183  -0.02452 140 SER A CB  
963  O OG  . SER A 133 ? 0.22301 0.25890 0.21377 0.00995  0.00799  -0.02793 140 SER A OG  
964  N N   . ALA A 134 ? 0.20698 0.22252 0.18759 0.01836  0.00059  -0.00975 141 ALA A N   
965  C CA  . ALA A 134 ? 0.18394 0.18574 0.15726 0.01689  0.00084  -0.00502 141 ALA A CA  
966  C C   . ALA A 134 ? 0.20400 0.19566 0.16420 0.02039  -0.00369 0.00317  141 ALA A C   
967  O O   . ALA A 134 ? 0.25421 0.23410 0.20429 0.01566  -0.00333 0.00878  141 ALA A O   
968  C CB  . ALA A 134 ? 0.15768 0.15329 0.13847 0.02057  -0.00010 -0.00697 141 ALA A CB  
969  N N   . TYR A 135 ? 0.22164 0.21867 0.18331 0.02848  -0.00833 0.00518  142 TYR A N   
970  C CA  . TYR A 135 ? 0.22551 0.21408 0.17774 0.03453  -0.01369 0.01393  142 TYR A CA  
971  C C   . TYR A 135 ? 0.28427 0.27755 0.22372 0.02893  -0.01586 0.01974  142 TYR A C   
972  O O   . TYR A 135 ? 0.28456 0.27221 0.21588 0.03400  -0.02171 0.02910  142 TYR A O   
973  C CB  . TYR A 135 ? 0.19119 0.18860 0.15284 0.04622  -0.01756 0.01450  142 TYR A CB  
974  C CG  . TYR A 135 ? 0.19185 0.18058 0.15952 0.05251  -0.01491 0.01010  142 TYR A CG  
975  C CD1 . TYR A 135 ? 0.23657 0.20475 0.19761 0.06023  -0.01648 0.01264  142 TYR A CD1 
976  C CD2 . TYR A 135 ? 0.25987 0.25892 0.23787 0.05029  -0.01122 0.00330  142 TYR A CD2 
977  C CE1 . TYR A 135 ? 0.24448 0.20355 0.20718 0.06544  -0.01407 0.00632  142 TYR A CE1 
978  C CE2 . TYR A 135 ? 0.24820 0.24061 0.22793 0.05513  -0.00918 -0.00058 142 TYR A CE2 
979  C CZ  . TYR A 135 ? 0.29773 0.27079 0.26886 0.06248  -0.01043 -0.00011 142 TYR A CZ  
980  O OH  . TYR A 135 ? 0.25843 0.22473 0.22808 0.06675  -0.00848 -0.00621 142 TYR A OH  
981  N N   . LEU A 136 ? 0.22193 0.22557 0.15871 0.01950  -0.01137 0.01439  143 LEU A N   
982  C CA  . LEU A 136 ? 0.24260 0.24946 0.16228 0.01262  -0.01168 0.01949  143 LEU A CA  
983  C C   . LEU A 136 ? 0.32365 0.31394 0.23199 0.00772  -0.00966 0.02892  143 LEU A C   
984  O O   . LEU A 136 ? 0.30244 0.28968 0.19430 0.00476  -0.01267 0.03934  143 LEU A O   
985  C CB  . LEU A 136 ? 0.26791 0.28882 0.18711 0.00461  -0.00514 0.00886  143 LEU A CB  
986  C CG  . LEU A 136 ? 0.24461 0.27938 0.17104 0.00613  -0.00822 -0.00029 143 LEU A CG  
987  C CD1 . LEU A 136 ? 0.23245 0.27397 0.16042 -0.00005 -0.00011 -0.01268 143 LEU A CD1 
988  C CD2 . LEU A 136 ? 0.24830 0.29150 0.16166 0.00632  -0.01727 0.00531  143 LEU A CD2 
989  N N   . VAL A 137 ? 0.27514 0.25546 0.19160 0.00509  -0.00503 0.02610  144 VAL A N   
990  C CA  . VAL A 137 ? 0.26871 0.23397 0.17666 -0.00313 -0.00277 0.03441  144 VAL A CA  
991  C C   . VAL A 137 ? 0.27762 0.21889 0.18963 0.00118  -0.00668 0.03701  144 VAL A C   
992  O O   . VAL A 137 ? 0.29974 0.22260 0.20339 -0.00570 -0.00730 0.04585  144 VAL A O   
993  C CB  . VAL A 137 ? 0.25038 0.22760 0.16296 -0.01451 0.00678  0.02901  144 VAL A CB  
994  C CG1 . VAL A 137 ? 0.26906 0.26759 0.17300 -0.01898 0.01219  0.02541  144 VAL A CG1 
995  C CG2 . VAL A 137 ? 0.24987 0.23132 0.18221 -0.01160 0.00883  0.01785  144 VAL A CG2 
996  N N   . ALA A 138 ? 0.25541 0.19530 0.17870 0.01123  -0.00901 0.02947  145 ALA A N   
997  C CA  . ALA A 138 ? 0.25875 0.17594 0.18359 0.01528  -0.01182 0.02856  145 ALA A CA  
998  C C   . ALA A 138 ? 0.33197 0.23813 0.25455 0.03048  -0.01794 0.03183  145 ALA A C   
999  O O   . ALA A 138 ? 0.33962 0.26334 0.26854 0.03936  -0.01915 0.02970  145 ALA A O   
1000 C CB  . ALA A 138 ? 0.25566 0.18016 0.19330 0.01571  -0.00914 0.01699  145 ALA A CB  
1001 N N   . GLU A 139 ? 0.31745 0.19465 0.23274 0.03361  -0.02180 0.03663  146 GLU A N   
1002 C CA  . GLU A 139 ? 0.37102 0.23706 0.28708 0.05108  -0.02658 0.03749  146 GLU A CA  
1003 C C   . GLU A 139 ? 0.48166 0.34520 0.40496 0.05925  -0.02446 0.02452  146 GLU A C   
1004 O O   . GLU A 139 ? 0.38226 0.24823 0.31022 0.07533  -0.02557 0.02199  146 GLU A O   
1005 C CB  . GLU A 139 ? 0.40977 0.24228 0.31410 0.05313  -0.03220 0.04872  146 GLU A CB  
1006 C CG  . GLU A 139 ? 0.49740 0.29964 0.39648 0.04438  -0.03207 0.04520  146 GLU A CG  
1007 C CD  . GLU A 139 ? 0.91253 0.67754 0.79970 0.04345  -0.03806 0.05800  146 GLU A CD  
1008 O OE1 . GLU A 139 ? 0.84759 0.61262 0.72988 0.04966  -0.04234 0.07148  146 GLU A OE1 
1009 O OE2 . GLU A 139 ? 0.75772 0.49285 0.64027 0.03560  -0.03941 0.05515  146 GLU A OE2 
1010 N N   . LYS A 140 ? 0.31145 0.17320 0.23591 0.04855  -0.02136 0.01669  147 LYS A N   
1011 C CA  . LYS A 140 ? 0.28558 0.14779 0.21389 0.05429  -0.01969 0.00463  147 LYS A CA  
1012 C C   . LYS A 140 ? 0.35029 0.23061 0.28543 0.04139  -0.01632 -0.00055 147 LYS A C   
1013 O O   . LYS A 140 ? 0.29011 0.17100 0.22519 0.02749  -0.01552 0.00324  147 LYS A O   
1014 C CB  . LYS A 140 ? 0.31907 0.14521 0.23702 0.05793  -0.02306 0.00010  147 LYS A CB  
1015 C CG  . LYS A 140 ? 0.39195 0.21700 0.30886 0.06097  -0.02165 -0.01358 147 LYS A CG  
1016 C CD  . LYS A 140 ? 0.49591 0.28180 0.40019 0.06748  -0.02540 -0.01977 147 LYS A CD  
1017 C CE  . LYS A 140 ? 0.61577 0.38366 0.51282 0.05250  -0.02847 -0.02745 147 LYS A CE  
1018 N NZ  . LYS A 140 ? 0.67637 0.39853 0.56052 0.05494  -0.03374 -0.03004 147 LYS A NZ  
1019 N N   . VAL A 141 ? 0.25486 0.15227 0.19698 0.04650  -0.01404 -0.00803 148 VAL A N   
1020 C CA  . VAL A 141 ? 0.27342 0.18746 0.22344 0.03684  -0.01199 -0.01214 148 VAL A CA  
1021 C C   . VAL A 141 ? 0.27814 0.18732 0.22473 0.04010  -0.01307 -0.02092 148 VAL A C   
1022 O O   . VAL A 141 ? 0.27429 0.18581 0.21848 0.05245  -0.01185 -0.02445 148 VAL A O   
1023 C CB  . VAL A 141 ? 0.22612 0.16835 0.18800 0.03801  -0.00878 -0.01070 148 VAL A CB  
1024 C CG1 . VAL A 141 ? 0.21783 0.17401 0.18923 0.02947  -0.00727 -0.01410 148 VAL A CG1 
1025 C CG2 . VAL A 141 ? 0.27544 0.22304 0.23706 0.03521  -0.00825 -0.00390 148 VAL A CG2 
1026 N N   . THR A 142 ? 0.28081 0.18477 0.22656 0.02884  -0.01542 -0.02436 149 THR A N   
1027 C CA  . THR A 142 ? 0.26508 0.16805 0.20609 0.02913  -0.01776 -0.03281 149 THR A CA  
1028 C C   . THR A 142 ? 0.28308 0.21128 0.23691 0.02176  -0.01751 -0.03167 149 THR A C   
1029 O O   . THR A 142 ? 0.27759 0.21401 0.24174 0.01180  -0.01713 -0.02743 149 THR A O   
1030 C CB  . THR A 142 ? 0.32215 0.19771 0.25172 0.02110  -0.02330 -0.03812 149 THR A CB  
1031 O OG1 . THR A 142 ? 0.33680 0.18489 0.25666 0.02702  -0.02399 -0.03684 149 THR A OG1 
1032 C CG2 . THR A 142 ? 0.34335 0.21542 0.26210 0.02354  -0.02651 -0.04926 149 THR A CG2 
1033 N N   . VAL A 143 ? 0.25151 0.19306 0.20528 0.02729  -0.01724 -0.03461 150 VAL A N   
1034 C CA  . VAL A 143 ? 0.20649 0.17025 0.17298 0.02214  -0.01802 -0.03189 150 VAL A CA  
1035 C C   . VAL A 143 ? 0.28878 0.25237 0.24595 0.02029  -0.02316 -0.03729 150 VAL A C   
1036 O O   . VAL A 143 ? 0.29506 0.25666 0.23959 0.02871  -0.02198 -0.04139 150 VAL A O   
1037 C CB  . VAL A 143 ? 0.24478 0.22741 0.22117 0.02918  -0.01353 -0.02696 150 VAL A CB  
1038 C CG1 . VAL A 143 ? 0.25116 0.25174 0.24065 0.02491  -0.01523 -0.02350 150 VAL A CG1 
1039 C CG2 . VAL A 143 ? 0.23589 0.21936 0.21905 0.03026  -0.00974 -0.02297 150 VAL A CG2 
1040 N N   . ILE A 144 ? 0.25043 0.21807 0.21337 0.00926  -0.02881 -0.03747 151 ILE A N   
1041 C CA  . ILE A 144 ? 0.21891 0.18911 0.17301 0.00519  -0.03603 -0.04211 151 ILE A CA  
1042 C C   . ILE A 144 ? 0.26367 0.26007 0.23360 0.00460  -0.03755 -0.03469 151 ILE A C   
1043 O O   . ILE A 144 ? 0.25715 0.26523 0.24710 0.00108  -0.03610 -0.02900 151 ILE A O   
1044 C CB  . ILE A 144 ? 0.26590 0.22376 0.21731 -0.00828 -0.04359 -0.04675 151 ILE A CB  
1045 C CG1 . ILE A 144 ? 0.39257 0.32101 0.33355 -0.00967 -0.04207 -0.05082 151 ILE A CG1 
1046 C CG2 . ILE A 144 ? 0.29427 0.25231 0.23148 -0.01238 -0.05241 -0.05368 151 ILE A CG2 
1047 C CD1 . ILE A 144 ? 0.36638 0.27385 0.28542 0.00084  -0.04106 -0.05966 151 ILE A CD1 
1048 N N   . THR A 145 ? 0.24289 0.24824 0.20352 0.00849  -0.04023 -0.03448 152 THR A N   
1049 C CA  . THR A 145 ? 0.25207 0.27941 0.22814 0.00955  -0.04159 -0.02493 152 THR A CA  
1050 C C   . THR A 145 ? 0.26483 0.30151 0.22817 0.00836  -0.04905 -0.02423 152 THR A C   
1051 O O   . THR A 145 ? 0.27126 0.29948 0.21068 0.01078  -0.04924 -0.03142 152 THR A O   
1052 C CB  . THR A 145 ? 0.26792 0.30022 0.25094 0.01828  -0.03320 -0.01902 152 THR A CB  
1053 O OG1 . THR A 145 ? 0.19733 0.24592 0.19800 0.01855  -0.03493 -0.00945 152 THR A OG1 
1054 C CG2 . THR A 145 ? 0.22623 0.25615 0.19013 0.02572  -0.02930 -0.02132 152 THR A CG2 
1055 N N   . LYS A 146 ? 0.19903 0.25383 0.17813 0.00558  -0.05513 -0.01542 153 LYS A N   
1056 C CA  . LYS A 146 ? 0.20921 0.27620 0.17732 0.00376  -0.06410 -0.01174 153 LYS A CA  
1057 C C   . LYS A 146 ? 0.24730 0.33157 0.23461 0.00788  -0.06514 0.00293  153 LYS A C   
1058 O O   . LYS A 146 ? 0.18079 0.27280 0.19394 0.00697  -0.06683 0.00782  153 LYS A O   
1059 C CB  . LYS A 146 ? 0.26149 0.33142 0.22915 -0.00707 -0.07591 -0.01658 153 LYS A CB  
1060 C CG  . LYS A 146 ? 0.33390 0.42031 0.29181 -0.01016 -0.08797 -0.01144 153 LYS A CG  
1061 C CD  . LYS A 146 ? 0.29696 0.37465 0.21854 -0.00827 -0.08757 -0.01948 153 LYS A CD  
1062 C CE  . LYS A 146 ? 0.38418 0.47847 0.29132 -0.01356 -0.10123 -0.01551 153 LYS A CE  
1063 N NZ  . LYS A 146 ? 0.29033 0.40598 0.21055 -0.00847 -0.10350 0.00368  153 LYS A NZ  
1064 N N   . HIS A 147 ? 0.28902 0.31871 0.23760 0.01200  -0.00823 -0.01639 154 HIS A N   
1065 C CA  . HIS A 147 ? 0.25398 0.28070 0.19593 0.01995  -0.00213 -0.00669 154 HIS A CA  
1066 C C   . HIS A 147 ? 0.27675 0.30775 0.19984 0.02897  -0.01070 -0.00432 154 HIS A C   
1067 O O   . HIS A 147 ? 0.29157 0.32140 0.19762 0.03100  -0.01723 -0.01178 154 HIS A O   
1068 C CB  . HIS A 147 ? 0.27561 0.28971 0.21294 0.01841  0.01056  -0.00137 154 HIS A CB  
1069 C CG  . HIS A 147 ? 0.32874 0.33121 0.26364 0.02245  0.01505  0.01127  154 HIS A CG  
1070 N ND1 . HIS A 147 ? 0.29458 0.29575 0.21228 0.03071  0.01562  0.02262  154 HIS A ND1 
1071 C CD2 . HIS A 147 ? 0.27249 0.25928 0.21814 0.02006  0.01674  0.01433  154 HIS A CD2 
1072 C CE1 . HIS A 147 ? 0.31369 0.29765 0.23487 0.03143  0.01827  0.03484  154 HIS A CE1 
1073 N NE2 . HIS A 147 ? 0.34721 0.31966 0.28510 0.02488  0.01748  0.02821  154 HIS A NE2 
1074 N N   . ASN A 148 ? 0.28515 0.31952 0.20811 0.03736  -0.01259 0.00463  155 ASN A N   
1075 C CA  . ASN A 148 ? 0.31009 0.35044 0.21361 0.04812  -0.02226 0.00850  155 ASN A CA  
1076 C C   . ASN A 148 ? 0.38836 0.42027 0.26076 0.05442  -0.01659 0.01115  155 ASN A C   
1077 O O   . ASN A 148 ? 0.36342 0.40076 0.21152 0.06424  -0.02742 0.00806  155 ASN A O   
1078 C CB  . ASN A 148 ? 0.32151 0.36087 0.22558 0.05978  -0.02158 0.02140  155 ASN A CB  
1079 C CG  . ASN A 148 ? 0.35216 0.41279 0.28094 0.06301  -0.03000 0.02016  155 ASN A CG  
1080 O OD1 . ASN A 148 ? 0.29732 0.37999 0.24293 0.05540  -0.04059 0.01355  155 ASN A OD1 
1081 N ND2 . ASN A 148 ? 0.36342 0.41783 0.29570 0.07540  -0.02575 0.02821  155 ASN A ND2 
1082 N N   . ASP A 149 ? 0.33117 0.35340 0.20346 0.05085  -0.00017 0.01856  156 ASP A N   
1083 C CA  . ASP A 149 ? 0.42706 0.45074 0.27337 0.05930  0.01022  0.02811  156 ASP A CA  
1084 C C   . ASP A 149 ? 0.40942 0.43779 0.24511 0.06063  0.01311  0.01497  156 ASP A C   
1085 O O   . ASP A 149 ? 0.41200 0.44833 0.22732 0.07070  0.02573  0.02369  156 ASP A O   
1086 C CB  . ASP A 149 ? 0.39525 0.41092 0.25272 0.05409  0.02609  0.04978  156 ASP A CB  
1087 C CG  . ASP A 149 ? 0.47668 0.47958 0.33505 0.05847  0.02219  0.06450  156 ASP A CG  
1088 O OD1 . ASP A 149 ? 0.51711 0.52509 0.36220 0.06976  0.01025  0.06133  156 ASP A OD1 
1089 O OD2 . ASP A 149 ? 0.43829 0.42462 0.31124 0.05107  0.02899  0.07959  156 ASP A OD2 
1090 N N   . ASP A 150 ? 0.36021 0.38497 0.20862 0.05290  0.00239  -0.00355 157 ASP A N   
1091 C CA  . ASP A 150 ? 0.34445 0.36701 0.18389 0.05584  0.00441  -0.01618 157 ASP A CA  
1092 C C   . ASP A 150 ? 0.46425 0.47632 0.30628 0.05106  -0.01740 -0.03641 157 ASP A C   
1093 O O   . ASP A 150 ? 0.37457 0.38867 0.23007 0.04367  -0.03224 -0.03768 157 ASP A O   
1094 C CB  . ASP A 150 ? 0.31867 0.34382 0.18365 0.04571  0.02036  -0.00941 157 ASP A CB  
1095 C CG  . ASP A 150 ? 0.45277 0.48535 0.30446 0.05646  0.03092  -0.01267 157 ASP A CG  
1096 O OD1 . ASP A 150 ? 0.43689 0.46606 0.25659 0.07308  0.02397  -0.02560 157 ASP A OD1 
1097 O OD2 . ASP A 150 ? 0.37057 0.41336 0.24297 0.05043  0.04494  -0.00271 157 ASP A OD2 
1098 N N   . GLU A 151 ? 0.38209 0.38356 0.21288 0.05595  -0.02036 -0.05057 158 GLU A N   
1099 C CA  . GLU A 151 ? 0.37457 0.35783 0.20876 0.04955  -0.04372 -0.06847 158 GLU A CA  
1100 C C   . GLU A 151 ? 0.35793 0.34061 0.23195 0.02983  -0.04201 -0.06431 158 GLU A C   
1101 O O   . GLU A 151 ? 0.31068 0.30459 0.20313 0.02460  -0.02406 -0.05252 158 GLU A O   
1102 C CB  . GLU A 151 ? 0.40985 0.37426 0.21026 0.06733  -0.04953 -0.08667 158 GLU A CB  
1103 C CG  . GLU A 151 ? 0.63168 0.59826 0.38312 0.09328  -0.05060 -0.09250 158 GLU A CG  
1104 C CD  . GLU A 151 ? 1.08022 1.03066 0.79465 0.11777  -0.05167 -0.11099 158 GLU A CD  
1105 O OE1 . GLU A 151 ? 1.20866 1.17638 0.89526 0.14085  -0.03425 -0.10442 158 GLU A OE1 
1106 O OE2 . GLU A 151 ? 1.11509 1.03744 0.83597 0.11297  -0.06802 -0.12758 158 GLU A OE2 
1107 N N   . GLN A 152 ? 0.34329 0.31142 0.22962 0.01900  -0.06259 -0.07343 159 GLN A N   
1108 C CA  . GLN A 152 ? 0.34467 0.31405 0.26546 0.00227  -0.06036 -0.06636 159 GLN A CA  
1109 C C   . GLN A 152 ? 0.35310 0.30605 0.26666 0.00825  -0.05310 -0.07279 159 GLN A C   
1110 O O   . GLN A 152 ? 0.35732 0.28555 0.24710 0.01914  -0.06502 -0.08829 159 GLN A O   
1111 C CB  . GLN A 152 ? 0.37605 0.34037 0.31962 -0.01449 -0.08476 -0.06668 159 GLN A CB  
1112 C CG  . GLN A 152 ? 0.31347 0.28966 0.29524 -0.03155 -0.07929 -0.05161 159 GLN A CG  
1113 C CD  . GLN A 152 ? 0.34621 0.33409 0.36003 -0.04994 -0.09924 -0.04254 159 GLN A CD  
1114 O OE1 . GLN A 152 ? 0.32992 0.34034 0.35141 -0.05053 -0.10531 -0.03826 159 GLN A OE1 
1115 N NE2 . GLN A 152 ? 0.33315 0.30665 0.36818 -0.06538 -0.11138 -0.03766 159 GLN A NE2 
1116 N N   . TYR A 153 ? 0.31550 0.28101 0.24774 0.00360  -0.03576 -0.06232 160 TYR A N   
1117 C CA  . TYR A 153 ? 0.33647 0.29372 0.26597 0.01031  -0.02792 -0.06577 160 TYR A CA  
1118 C C   . TYR A 153 ? 0.30900 0.26463 0.26434 -0.00296 -0.02944 -0.05808 160 TYR A C   
1119 O O   . TYR A 153 ? 0.25198 0.22364 0.22768 -0.01468 -0.02703 -0.04665 160 TYR A O   
1120 C CB  . TYR A 153 ? 0.27385 0.25147 0.20178 0.01835  -0.00656 -0.05873 160 TYR A CB  
1121 C CG  . TYR A 153 ? 0.32872 0.31123 0.22925 0.03509  -0.00090 -0.06201 160 TYR A CG  
1122 C CD1 . TYR A 153 ? 0.34553 0.31975 0.22176 0.05469  -0.00093 -0.07325 160 TYR A CD1 
1123 C CD2 . TYR A 153 ? 0.47403 0.46959 0.36955 0.03492  0.00466  -0.05298 160 TYR A CD2 
1124 C CE1 . TYR A 153 ? 0.51135 0.49569 0.35803 0.07441  0.00675  -0.07442 160 TYR A CE1 
1125 C CE2 . TYR A 153 ? 0.45415 0.45709 0.32150 0.05193  0.01108  -0.05220 160 TYR A CE2 
1126 C CZ  . TYR A 153 ? 0.54769 0.54769 0.39010 0.07199  0.01321  -0.06244 160 TYR A CZ  
1127 O OH  . TYR A 153 ? 0.69941 0.71251 0.50950 0.09325  0.02231  -0.05977 160 TYR A OH  
1128 N N   . ALA A 154 ? 0.29950 0.23821 0.25136 0.00273  -0.03177 -0.06316 161 ALA A N   
1129 C CA  . ALA A 154 ? 0.27423 0.21371 0.24598 -0.00549 -0.02971 -0.05333 161 ALA A CA  
1130 C C   . ALA A 154 ? 0.27763 0.22902 0.24807 0.00555  -0.01528 -0.05299 161 ALA A C   
1131 O O   . ALA A 154 ? 0.32438 0.26727 0.28028 0.02130  -0.01435 -0.06214 161 ALA A O   
1132 C CB  . ALA A 154 ? 0.33270 0.23924 0.30635 -0.00995 -0.04857 -0.05581 161 ALA A CB  
1133 N N   . TRP A 155 ? 0.23533 0.20699 0.22111 -0.00102 -0.00607 -0.04280 162 TRP A N   
1134 C CA  . TRP A 155 ? 0.25121 0.23600 0.24247 0.00523  0.00239  -0.04098 162 TRP A CA  
1135 C C   . TRP A 155 ? 0.23962 0.21768 0.23854 0.00243  -0.00284 -0.03411 162 TRP A C   
1136 O O   . TRP A 155 ? 0.23117 0.20749 0.23639 -0.00762 -0.00677 -0.02535 162 TRP A O   
1137 C CB  . TRP A 155 ? 0.20935 0.21545 0.20871 0.00016  0.01098  -0.03648 162 TRP A CB  
1138 C CG  . TRP A 155 ? 0.19400 0.21550 0.20421 0.00183  0.01478  -0.03435 162 TRP A CG  
1139 C CD1 . TRP A 155 ? 0.20272 0.24053 0.22152 0.00362  0.02089  -0.03303 162 TRP A CD1 
1140 C CD2 . TRP A 155 ? 0.20153 0.22687 0.21717 0.00073  0.01085  -0.03137 162 TRP A CD2 
1141 N NE1 . TRP A 155 ? 0.18483 0.23521 0.21797 0.00115  0.01788  -0.03094 162 TRP A NE1 
1142 C CE2 . TRP A 155 ? 0.23786 0.27936 0.26520 0.00135  0.01136  -0.03169 162 TRP A CE2 
1143 C CE3 . TRP A 155 ? 0.20365 0.22334 0.21587 -0.00056 0.00675  -0.02611 162 TRP A CE3 
1144 C CZ2 . TRP A 155 ? 0.22871 0.27731 0.26025 0.00234  0.00488  -0.03117 162 TRP A CZ2 
1145 C CZ3 . TRP A 155 ? 0.19541 0.22401 0.20818 0.00284  0.00394  -0.02339 162 TRP A CZ3 
1146 C CH2 . TRP A 155 ? 0.23208 0.27304 0.25231 0.00486  0.00158  -0.02807 162 TRP A CH2 
1147 N N   . GLU A 156 ? 0.23473 0.21277 0.23426 0.01252  -0.00234 -0.03520 163 GLU A N   
1148 C CA  . GLU A 156 ? 0.24400 0.21319 0.24758 0.01208  -0.00807 -0.02648 163 GLU A CA  
1149 C C   . GLU A 156 ? 0.24047 0.22535 0.24842 0.02294  -0.00516 -0.02614 163 GLU A C   
1150 O O   . GLU A 156 ? 0.24370 0.23663 0.25217 0.03476  -0.00170 -0.03324 163 GLU A O   
1151 C CB  . GLU A 156 ? 0.30607 0.23980 0.30351 0.01443  -0.02031 -0.02781 163 GLU A CB  
1152 C CG  . GLU A 156 ? 0.32077 0.24153 0.32457 0.01018  -0.02698 -0.01260 163 GLU A CG  
1153 C CD  . GLU A 156 ? 0.65961 0.53929 0.66289 0.00396  -0.04332 -0.01096 163 GLU A CD  
1154 O OE1 . GLU A 156 ? 0.52969 0.37904 0.52081 0.01875  -0.05221 -0.02218 163 GLU A OE1 
1155 O OE2 . GLU A 156 ? 0.50754 0.38529 0.52375 -0.01461 -0.04867 0.00170  163 GLU A OE2 
1156 N N   . SER A 157 ? 0.23813 0.23068 0.24907 0.02109  -0.00697 -0.01648 164 SER A N   
1157 C CA  . SER A 157 ? 0.23959 0.24701 0.25513 0.03204  -0.00847 -0.01615 164 SER A CA  
1158 C C   . SER A 157 ? 0.25194 0.25671 0.26266 0.03399  -0.01358 -0.00339 164 SER A C   
1159 O O   . SER A 157 ? 0.24830 0.25898 0.25380 0.02671  -0.01175 0.00447  164 SER A O   
1160 C CB  . SER A 157 ? 0.21964 0.25602 0.24512 0.02903  -0.00551 -0.02130 164 SER A CB  
1161 O OG  . SER A 157 ? 0.22361 0.27799 0.25867 0.03856  -0.01040 -0.02028 164 SER A OG  
1162 N N   . SER A 158 ? 0.25089 0.22312 0.23574 0.04344  0.00365  -0.00191 165 SER A N   
1163 C CA  . SER A 158 ? 0.25816 0.23107 0.24129 0.05124  0.00571  0.00669  165 SER A CA  
1164 C C   . SER A 158 ? 0.32092 0.31970 0.30594 0.05571  -0.00036 0.01181  165 SER A C   
1165 O O   . SER A 158 ? 0.30889 0.31390 0.29205 0.06669  0.00134  0.02014  165 SER A O   
1166 C CB  . SER A 158 ? 0.36188 0.31774 0.34374 0.06187  0.01575  0.01100  165 SER A CB  
1167 O OG  . SER A 158 ? 0.36492 0.29588 0.34706 0.05591  0.02064  0.00578  165 SER A OG  
1168 N N   . ALA A 159 ? 0.23994 0.25449 0.22970 0.04766  -0.00714 0.00731  166 ALA A N   
1169 C CA  . ALA A 159 ? 0.30069 0.34186 0.29684 0.04857  -0.01408 0.01021  166 ALA A CA  
1170 C C   . ALA A 159 ? 0.28954 0.34320 0.29260 0.06024  -0.00978 0.01675  166 ALA A C   
1171 O O   . ALA A 159 ? 0.31827 0.36161 0.32173 0.06354  -0.00241 0.01561  166 ALA A O   
1172 C CB  . ALA A 159 ? 0.28094 0.32931 0.27070 0.05017  -0.02032 0.01284  166 ALA A CB  
1173 N N   . GLY A 160 ? 0.28339 0.36023 0.29134 0.06742  -0.01438 0.02346  167 GLY A N   
1174 C CA  . GLY A 160 ? 0.30140 0.39420 0.31873 0.07913  -0.00989 0.03091  167 GLY A CA  
1175 C C   . GLY A 160 ? 0.29824 0.40565 0.32891 0.07397  -0.00932 0.02905  167 GLY A C   
1176 O O   . GLY A 160 ? 0.31972 0.43537 0.35687 0.08490  -0.00219 0.03525  167 GLY A O   
1177 N N   . GLY A 161 ? 0.24163 0.35086 0.27607 0.05898  -0.01469 0.02179  168 GLY A N   
1178 C CA  . GLY A 161 ? 0.23266 0.35808 0.28158 0.05376  -0.01358 0.02198  168 GLY A CA  
1179 C C   . GLY A 161 ? 0.24976 0.35592 0.29215 0.05252  -0.00494 0.01800  168 GLY A C   
1180 O O   . GLY A 161 ? 0.23130 0.34965 0.28418 0.04944  -0.00214 0.01951  168 GLY A O   
1181 N N   . SER A 162 ? 0.22851 0.30628 0.25453 0.05492  -0.00066 0.01317  169 SER A N   
1182 C CA  . SER A 162 ? 0.25355 0.31514 0.27134 0.05519  0.00602  0.00830  169 SER A CA  
1183 C C   . SER A 162 ? 0.27094 0.30814 0.27590 0.04756  0.00377  -0.00022 169 SER A C   
1184 O O   . SER A 162 ? 0.23257 0.26043 0.23382 0.04540  0.00056  -0.00111 169 SER A O   
1185 C CB  . SER A 162 ? 0.25765 0.31144 0.27002 0.07008  0.01594  0.01105  169 SER A CB  
1186 O OG  . SER A 162 ? 0.27980 0.31229 0.28228 0.07578  0.01835  0.00975  169 SER A OG  
1187 N N   . PHE A 163 ? 0.23377 0.26251 0.23227 0.04458  0.00597  -0.00554 170 PHE A N   
1188 C CA  . PHE A 163 ? 0.24088 0.25037 0.22909 0.03817  0.00357  -0.01353 170 PHE A CA  
1189 C C   . PHE A 163 ? 0.25845 0.25693 0.23536 0.04320  0.00827  -0.01924 170 PHE A C   
1190 O O   . PHE A 163 ? 0.26800 0.27454 0.24450 0.05113  0.01403  -0.01608 170 PHE A O   
1191 C CB  . PHE A 163 ? 0.22186 0.23670 0.21312 0.02687  -0.00214 -0.01468 170 PHE A CB  
1192 C CG  . PHE A 163 ? 0.21809 0.24514 0.21315 0.02505  -0.00015 -0.01241 170 PHE A CG  
1193 C CD1 . PHE A 163 ? 0.22859 0.27483 0.23754 0.02321  -0.00007 -0.00611 170 PHE A CD1 
1194 C CD2 . PHE A 163 ? 0.22213 0.24239 0.20791 0.02468  0.00142  -0.01614 170 PHE A CD2 
1195 C CE1 . PHE A 163 ? 0.22698 0.28356 0.24258 0.02067  0.00355  -0.00250 170 PHE A CE1 
1196 C CE2 . PHE A 163 ? 0.23583 0.26663 0.22466 0.02445  0.00530  -0.01176 170 PHE A CE2 
1197 C CZ  . PHE A 163 ? 0.21516 0.26297 0.21996 0.02194  0.00727  -0.00447 170 PHE A CZ  
1198 N N   . THR A 164 ? 0.25480 0.23563 0.22256 0.03911  0.00578  -0.02775 171 THR A N   
1199 C CA  . THR A 164 ? 0.27144 0.24080 0.22539 0.04311  0.00780  -0.03604 171 THR A CA  
1200 C C   . THR A 164 ? 0.31089 0.28087 0.26043 0.03511  0.00151  -0.04143 171 THR A C   
1201 O O   . THR A 164 ? 0.25454 0.22584 0.21110 0.02638  -0.00361 -0.04072 171 THR A O   
1202 C CB  . THR A 164 ? 0.32693 0.27324 0.27376 0.04643  0.01025  -0.04338 171 THR A CB  
1203 O OG1 . THR A 164 ? 0.30342 0.23967 0.25551 0.03655  0.00512  -0.04700 171 THR A OG1 
1204 C CG2 . THR A 164 ? 0.31633 0.26176 0.26714 0.05678  0.01787  -0.03599 171 THR A CG2 
1205 N N   . VAL A 165 ? 0.27890 0.24857 0.21546 0.03983  0.00248  -0.04614 172 VAL A N   
1206 C CA  . VAL A 165 ? 0.27921 0.25044 0.20911 0.03490  -0.00379 -0.05139 172 VAL A CA  
1207 C C   . VAL A 165 ? 0.34640 0.30477 0.25817 0.03985  -0.00539 -0.06380 172 VAL A C   
1208 O O   . VAL A 165 ? 0.32135 0.27544 0.22134 0.05041  0.00106  -0.06509 172 VAL A O   
1209 C CB  . VAL A 165 ? 0.27518 0.26304 0.20577 0.03642  -0.00149 -0.04295 172 VAL A CB  
1210 C CG1 . VAL A 165 ? 0.27879 0.26858 0.19864 0.03550  -0.00689 -0.04763 172 VAL A CG1 
1211 C CG2 . VAL A 165 ? 0.24856 0.24592 0.19648 0.02906  -0.00153 -0.03376 172 VAL A CG2 
1212 N N   . ARG A 166 ? 0.31013 0.26222 0.22026 0.03228  -0.01393 -0.07339 173 ARG A N   
1213 C CA  . ARG A 166 ? 0.36961 0.31062 0.26220 0.03480  -0.01841 -0.08791 173 ARG A CA  
1214 C C   . ARG A 166 ? 0.37895 0.32990 0.27059 0.02806  -0.02935 -0.09327 173 ARG A C   
1215 O O   . ARG A 166 ? 0.31548 0.27699 0.22235 0.02045  -0.03260 -0.08648 173 ARG A O   
1216 C CB  . ARG A 166 ? 0.39588 0.31360 0.29017 0.03161  -0.01772 -0.09765 173 ARG A CB  
1217 C CG  . ARG A 166 ? 0.48047 0.39413 0.39318 0.01762  -0.02402 -0.10004 173 ARG A CG  
1218 C CD  . ARG A 166 ? 0.53587 0.42509 0.45415 0.01553  -0.01894 -0.10460 173 ARG A CD  
1219 N NE  . ARG A 166 ? 0.66312 0.55317 0.58930 0.02179  -0.00914 -0.09067 173 ARG A NE  
1220 C CZ  . ARG A 166 ? 0.76538 0.63708 0.69424 0.02569  -0.00105 -0.08914 173 ARG A CZ  
1221 N NH1 . ARG A 166 ? 0.59805 0.44442 0.52286 0.02323  0.00013  -0.10102 173 ARG A NH1 
1222 N NH2 . ARG A 166 ? 0.67222 0.55102 0.60783 0.03262  0.00608  -0.07545 173 ARG A NH2 
1223 N N   . THR A 167 ? 0.38942 0.33773 0.26159 0.03223  -0.03503 -0.10554 174 THR A N   
1224 C CA  . THR A 167 ? 0.36544 0.32453 0.23683 0.02607  -0.04753 -0.11280 174 THR A CA  
1225 C C   . THR A 167 ? 0.50498 0.45476 0.39510 0.01164  -0.05414 -0.12079 174 THR A C   
1226 O O   . THR A 167 ? 0.46451 0.39305 0.35516 0.00908  -0.05135 -0.12899 174 THR A O   
1227 C CB  . THR A 167 ? 0.45101 0.40890 0.29411 0.03495  -0.05298 -0.12594 174 THR A CB  
1228 O OG1 . THR A 167 ? 0.52274 0.49586 0.35217 0.04773  -0.04731 -0.11466 174 THR A OG1 
1229 C CG2 . THR A 167 ? 0.74674 0.71260 0.59030 0.02635  -0.06899 -0.13908 174 THR A CG2 
1230 N N   . ASP A 168 ? 0.41310 0.37783 0.32028 0.00286  -0.06090 -0.11670 175 ASP A N   
1231 C CA  . ASP A 168 ? 0.39122 0.34942 0.31988 -0.01096 -0.06555 -0.12197 175 ASP A CA  
1232 C C   . ASP A 168 ? 0.68562 0.64659 0.61137 -0.01794 -0.07956 -0.13946 175 ASP A C   
1233 O O   . ASP A 168 ? 0.61999 0.60122 0.53706 -0.01470 -0.08878 -0.14150 175 ASP A O   
1234 C CB  . ASP A 168 ? 0.36817 0.34079 0.31899 -0.01674 -0.06445 -0.10818 175 ASP A CB  
1235 C CG  . ASP A 168 ? 0.49620 0.46098 0.47059 -0.02953 -0.06564 -0.11065 175 ASP A CG  
1236 O OD1 . ASP A 168 ? 0.67292 0.61582 0.64898 -0.03188 -0.06036 -0.11549 175 ASP A OD1 
1237 O OD2 . ASP A 168 ? 0.53022 0.51042 0.52187 -0.03648 -0.07088 -0.10720 175 ASP A OD2 
1238 N N   . THR A 169 ? 0.72516 0.66582 0.65858 -0.02743 -0.08112 -0.15199 176 THR A N   
1239 C CA  . THR A 169 ? 0.99358 0.93464 0.92933 -0.03796 -0.09536 -0.17091 176 THR A CA  
1240 C C   . THR A 169 ? 0.91788 0.86308 0.88823 -0.05502 -0.09934 -0.17037 176 THR A C   
1241 O O   . THR A 169 ? 0.83420 0.77958 0.81209 -0.06665 -0.10958 -0.18353 176 THR A O   
1242 C CB  . THR A 169 ? 0.97353 0.88473 0.88943 -0.03641 -0.09447 -0.18922 176 THR A CB  
1243 O OG1 . THR A 169 ? 0.86036 0.74462 0.78594 -0.03758 -0.08029 -0.18389 176 THR A OG1 
1244 C CG2 . THR A 169 ? 0.65702 0.56914 0.53681 -0.01892 -0.09258 -0.19139 176 THR A CG2 
1245 N N   . GLY A 170 ? 0.73919 0.68872 0.72997 -0.05649 -0.08981 -0.15247 177 GLY A N   
1246 C CA  . GLY A 170 ? 0.64499 0.60218 0.66886 -0.07055 -0.09186 -0.14888 177 GLY A CA  
1247 C C   . GLY A 170 ? 0.75563 0.74648 0.79099 -0.07473 -0.10522 -0.14874 177 GLY A C   
1248 O O   . GLY A 170 ? 0.60094 0.60687 0.61685 -0.06831 -0.11566 -0.15599 177 GLY A O   
1249 N N   . GLU A 171 ? 0.70156 0.70539 0.76809 -0.08393 -0.10419 -0.13936 178 GLU A N   
1250 C CA  . GLU A 171 ? 0.76392 0.80259 0.84560 -0.08681 -0.11537 -0.13623 178 GLU A CA  
1251 C C   . GLU A 171 ? 0.52886 0.58549 0.58879 -0.07065 -0.11492 -0.12540 178 GLU A C   
1252 O O   . GLU A 171 ? 0.45148 0.49907 0.50251 -0.06131 -0.10189 -0.11150 178 GLU A O   
1253 C CB  . GLU A 171 ? 0.79289 0.84079 0.91040 -0.09531 -0.10879 -0.12252 178 GLU A CB  
1254 C CG  . GLU A 171 ? 0.82335 0.90743 0.96798 -0.10295 -0.12091 -0.12146 178 GLU A CG  
1255 C CD  . GLU A 171 ? 1.12190 1.20983 1.28122 -0.11910 -0.13447 -0.13875 178 GLU A CD  
1256 O OE1 . GLU A 171 ? 1.06863 1.12863 1.20885 -0.12226 -0.13424 -0.15165 178 GLU A OE1 
1257 O OE2 . GLU A 171 ? 0.82425 0.94076 1.00923 -0.12693 -0.14182 -0.13466 178 GLU A OE2 
1258 N N   . PRO A 172 ? 0.56099 0.64246 0.61173 -0.06680 -0.12865 -0.13132 179 PRO A N   
1259 C CA  . PRO A 172 ? 0.52072 0.62033 0.55510 -0.05131 -0.12647 -0.11802 179 PRO A CA  
1260 C C   . PRO A 172 ? 0.56054 0.67233 0.61622 -0.05005 -0.11753 -0.09843 179 PRO A C   
1261 O O   . PRO A 172 ? 0.52342 0.64614 0.60896 -0.06037 -0.11952 -0.09601 179 PRO A O   
1262 C CB  . PRO A 172 ? 0.46744 0.59498 0.49445 -0.04921 -0.14445 -0.12811 179 PRO A CB  
1263 C CG  . PRO A 172 ? 0.52740 0.64625 0.56031 -0.06344 -0.15554 -0.14818 179 PRO A CG  
1264 C CD  . PRO A 172 ? 0.50776 0.59571 0.55507 -0.07458 -0.14577 -0.15213 179 PRO A CD  
1265 N N   . MET A 173 ? 0.39040 0.50010 0.43045 -0.03699 -0.10711 -0.08444 180 MET A N   
1266 C CA  . MET A 173 ? 0.43580 0.54641 0.48877 -0.03426 -0.09524 -0.06702 180 MET A CA  
1267 C C   . MET A 173 ? 0.41842 0.55417 0.47147 -0.02408 -0.09625 -0.05480 180 MET A C   
1268 O O   . MET A 173 ? 0.60015 0.73923 0.66617 -0.02189 -0.08748 -0.04112 180 MET A O   
1269 C CB  . MET A 173 ? 0.34407 0.42922 0.38023 -0.02837 -0.08170 -0.06122 180 MET A CB  
1270 C CG  . MET A 173 ? 0.61122 0.67664 0.65953 -0.03521 -0.07252 -0.05867 180 MET A CG  
1271 S SD  . MET A 173 ? 0.53947 0.58639 0.56780 -0.02582 -0.05961 -0.04980 180 MET A SD  
1272 C CE  . MET A 173 ? 0.31097 0.36993 0.34482 -0.01953 -0.05327 -0.03394 180 MET A CE  
1273 N N   . GLY A 174 ? 0.38788 0.53989 0.42450 -0.01602 -0.10546 -0.05864 181 GLY A N   
1274 C CA  . GLY A 174 ? 0.33428 0.50921 0.36827 -0.00360 -0.10508 -0.04543 181 GLY A CA  
1275 C C   . GLY A 174 ? 0.25700 0.41601 0.26957 0.00893  -0.09089 -0.03363 181 GLY A C   
1276 O O   . GLY A 174 ? 0.31659 0.47764 0.30616 0.01944  -0.09161 -0.03357 181 GLY A O   
1277 N N   . ARG A 175 ? 0.24193 0.38340 0.26166 0.00722  -0.07764 -0.02448 182 ARG A N   
1278 C CA  . ARG A 175 ? 0.23708 0.36093 0.24097 0.01566  -0.06403 -0.01459 182 ARG A CA  
1279 C C   . ARG A 175 ? 0.22368 0.32907 0.23874 0.00943  -0.05390 -0.01014 182 ARG A C   
1280 O O   . ARG A 175 ? 0.22597 0.33925 0.26003 0.00568  -0.05370 -0.00618 182 ARG A O   
1281 C CB  . ARG A 175 ? 0.24127 0.37858 0.23879 0.02955  -0.05938 -0.00053 182 ARG A CB  
1282 C CG  . ARG A 175 ? 0.23989 0.35623 0.22319 0.03670  -0.04425 0.00944  182 ARG A CG  
1283 C CD  . ARG A 175 ? 0.24398 0.36721 0.22709 0.04896  -0.03571 0.02551  182 ARG A CD  
1284 N NE  . ARG A 175 ? 0.24003 0.36580 0.24120 0.04658  -0.03234 0.03129  182 ARG A NE  
1285 C CZ  . ARG A 175 ? 0.23714 0.38884 0.25315 0.04998  -0.03837 0.03595  182 ARG A CZ  
1286 N NH1 . ARG A 175 ? 0.24656 0.42554 0.26082 0.05608  -0.04966 0.03513  182 ARG A NH1 
1287 N NH2 . ARG A 175 ? 0.23029 0.38228 0.26322 0.04806  -0.03294 0.04200  182 ARG A NH2 
1288 N N   . GLY A 176 ? 0.22010 0.30314 0.22385 0.00883  -0.04582 -0.01058 183 GLY A N   
1289 C CA  . GLY A 176 ? 0.21084 0.27685 0.22006 0.00531  -0.03642 -0.00599 183 GLY A CA  
1290 C C   . GLY A 176 ? 0.26768 0.31632 0.27334 -0.00130 -0.03554 -0.01383 183 GLY A C   
1291 O O   . GLY A 176 ? 0.25532 0.30114 0.25088 -0.00113 -0.03880 -0.02079 183 GLY A O   
1292 N N   . THR A 177 ? 0.20226 0.23963 0.21527 -0.00555 -0.03041 -0.01191 184 THR A N   
1293 C CA  . THR A 177 ? 0.20066 0.22250 0.20965 -0.00954 -0.02842 -0.01684 184 THR A CA  
1294 C C   . THR A 177 ? 0.22447 0.24189 0.24688 -0.01485 -0.02701 -0.01669 184 THR A C   
1295 O O   . THR A 177 ? 0.22836 0.24951 0.25975 -0.01399 -0.02315 -0.00966 184 THR A O   
1296 C CB  . THR A 177 ? 0.23280 0.24259 0.23100 -0.00661 -0.02121 -0.01255 184 THR A CB  
1297 O OG1 . THR A 177 ? 0.24274 0.25547 0.23091 -0.00223 -0.02064 -0.01156 184 THR A OG1 
1298 C CG2 . THR A 177 ? 0.20383 0.20186 0.19980 -0.00976 -0.01997 -0.01641 184 THR A CG2 
1299 N N   . LYS A 178 ? 0.20902 0.21807 0.23279 -0.01916 -0.02875 -0.02337 185 LYS A N   
1300 C CA  . LYS A 178 ? 0.20868 0.21018 0.24427 -0.02343 -0.02535 -0.02217 185 LYS A CA  
1301 C C   . LYS A 178 ? 0.25578 0.24225 0.28141 -0.02134 -0.02092 -0.02255 185 LYS A C   
1302 O O   . LYS A 178 ? 0.23980 0.22192 0.25802 -0.02091 -0.02341 -0.02881 185 LYS A O   
1303 C CB  . LYS A 178 ? 0.23677 0.24279 0.28685 -0.03089 -0.03152 -0.02959 185 LYS A CB  
1304 C CG  . LYS A 178 ? 0.42339 0.41670 0.48489 -0.03590 -0.02703 -0.02991 185 LYS A CG  
1305 C CD  . LYS A 178 ? 0.49493 0.49482 0.57672 -0.04580 -0.03313 -0.03670 185 LYS A CD  
1306 C CE  . LYS A 178 ? 0.54127 0.54866 0.61640 -0.04822 -0.04474 -0.04947 185 LYS A CE  
1307 N NZ  . LYS A 178 ? 0.58726 0.59424 0.68125 -0.05993 -0.05076 -0.05939 185 LYS A NZ  
1308 N N   . VAL A 179 ? 0.22726 0.20730 0.25093 -0.01847 -0.01438 -0.01547 186 VAL A N   
1309 C CA  . VAL A 179 ? 0.22308 0.19268 0.23765 -0.01536 -0.01120 -0.01480 186 VAL A CA  
1310 C C   . VAL A 179 ? 0.25440 0.21563 0.27802 -0.01614 -0.00632 -0.01181 186 VAL A C   
1311 O O   . VAL A 179 ? 0.26807 0.22893 0.29843 -0.01544 -0.00101 -0.00486 186 VAL A O   
1312 C CB  . VAL A 179 ? 0.20271 0.17045 0.20579 -0.01100 -0.00828 -0.01026 186 VAL A CB  
1313 C CG1 . VAL A 179 ? 0.21804 0.17929 0.21306 -0.00758 -0.00687 -0.00968 186 VAL A CG1 
1314 C CG2 . VAL A 179 ? 0.21873 0.19179 0.21510 -0.01103 -0.01134 -0.01266 186 VAL A CG2 
1315 N N   . ILE A 180 ? 0.23029 0.18365 0.25402 -0.01649 -0.00643 -0.01590 187 ILE A N   
1316 C CA  . ILE A 180 ? 0.22874 0.17091 0.26167 -0.01698 -0.00021 -0.01260 187 ILE A CA  
1317 C C   . ILE A 180 ? 0.25688 0.19221 0.27796 -0.00846 0.00462  -0.00699 187 ILE A C   
1318 O O   . ILE A 180 ? 0.26390 0.19799 0.27661 -0.00508 0.00243  -0.01052 187 ILE A O   
1319 C CB  . ILE A 180 ? 0.25575 0.19067 0.29681 -0.02276 -0.00268 -0.02139 187 ILE A CB  
1320 C CG1 . ILE A 180 ? 0.28845 0.23454 0.33909 -0.03075 -0.01047 -0.02848 187 ILE A CG1 
1321 C CG2 . ILE A 180 ? 0.27265 0.19239 0.32599 -0.02425 0.00584  -0.01717 187 ILE A CG2 
1322 C CD1 . ILE A 180 ? 0.36144 0.30193 0.41110 -0.03505 -0.01628 -0.04105 187 ILE A CD1 
1323 N N   . LEU A 181 ? 0.23654 0.16910 0.25663 -0.00378 0.01135  0.00238  188 LEU A N   
1324 C CA  . LEU A 181 ? 0.29419 0.22325 0.30122 0.00578  0.01490  0.00836  188 LEU A CA  
1325 C C   . LEU A 181 ? 0.27054 0.18649 0.28452 0.00915  0.02363  0.01424  188 LEU A C   
1326 O O   . LEU A 181 ? 0.26464 0.17475 0.28909 0.00825  0.03153  0.02121  188 LEU A O   
1327 C CB  . LEU A 181 ? 0.24365 0.17607 0.24079 0.01091  0.01742  0.01474  188 LEU A CB  
1328 C CG  . LEU A 181 ? 0.25911 0.20004 0.24993 0.00755  0.01100  0.00949  188 LEU A CG  
1329 C CD1 . LEU A 181 ? 0.29051 0.22984 0.27071 0.01332  0.01563  0.01542  188 LEU A CD1 
1330 C CD2 . LEU A 181 ? 0.29285 0.23943 0.27418 0.00759  0.00339  0.00307  188 LEU A CD2 
1331 N N   . HIS A 182 ? 0.27947 0.19029 0.28899 0.01355  0.02368  0.01256  189 HIS A N   
1332 C CA  . HIS A 182 ? 0.31963 0.21529 0.33316 0.01937  0.03380  0.01974  189 HIS A CA  
1333 C C   . HIS A 182 ? 0.34603 0.24506 0.34549 0.03266  0.03824  0.03120  189 HIS A C   
1334 O O   . HIS A 182 ? 0.28872 0.19639 0.27575 0.04026  0.03359  0.03114  189 HIS A O   
1335 C CB  . HIS A 182 ? 0.28860 0.17606 0.30198 0.02031  0.03313  0.01338  189 HIS A CB  
1336 C CG  . HIS A 182 ? 0.29512 0.18112 0.31638 0.00875  0.02660  0.00007  189 HIS A CG  
1337 N ND1 . HIS A 182 ? 0.41003 0.28028 0.44470 0.00083  0.03006  -0.00518 189 HIS A ND1 
1338 C CD2 . HIS A 182 ? 0.38214 0.28099 0.39885 0.00417  0.01666  -0.00899 189 HIS A CD2 
1339 C CE1 . HIS A 182 ? 0.37440 0.24927 0.41032 -0.00753 0.02103  -0.01797 189 HIS A CE1 
1340 N NE2 . HIS A 182 ? 0.40718 0.29939 0.43187 -0.00475 0.01362  -0.01937 189 HIS A NE2 
1341 N N   . LEU A 183 ? 0.29726 0.19110 0.29888 0.03610  0.04725  0.04143  190 LEU A N   
1342 C CA  . LEU A 183 ? 0.30458 0.20435 0.28827 0.04890  0.04952  0.05075  190 LEU A CA  
1343 C C   . LEU A 183 ? 0.36543 0.26030 0.34056 0.06289  0.05560  0.05995  190 LEU A C   
1344 O O   . LEU A 183 ? 0.35490 0.23456 0.34072 0.06407  0.06486  0.06434  190 LEU A O   
1345 C CB  . LEU A 183 ? 0.31187 0.20732 0.29885 0.05048  0.05926  0.06026  190 LEU A CB  
1346 C CG  . LEU A 183 ? 0.29772 0.20031 0.29153 0.04035  0.05483  0.05434  190 LEU A CG  
1347 C CD1 . LEU A 183 ? 0.31025 0.20967 0.30598 0.04559  0.06680  0.06653  190 LEU A CD1 
1348 C CD2 . LEU A 183 ? 0.28556 0.20070 0.26268 0.03959  0.04210  0.04473  190 LEU A CD2 
1349 N N   . LYS A 184 ? 0.37678 0.25788 0.35489 0.08703  0.01193  0.03848  191 LYS A N   
1350 C CA  . LYS A 184 ? 0.43305 0.30389 0.42002 0.10123  0.01168  0.05454  191 LYS A CA  
1351 C C   . LYS A 184 ? 0.42841 0.26275 0.40802 0.09023  0.00930  0.06178  191 LYS A C   
1352 O O   . LYS A 184 ? 0.40717 0.24074 0.38083 0.06904  0.00627  0.05937  191 LYS A O   
1353 C CB  . LYS A 184 ? 0.42241 0.33756 0.42563 0.10401  0.00541  0.07110  191 LYS A CB  
1354 C CG  . LYS A 184 ? 0.35379 0.30797 0.37588 0.11536  0.01052  0.06994  191 LYS A CG  
1355 C CD  . LYS A 184 ? 0.45993 0.45956 0.50393 0.10823  0.00074  0.08123  191 LYS A CD  
1356 C CE  . LYS A 184 ? 0.47943 0.51599 0.54507 0.10614  0.00756  0.07889  191 LYS A CE  
1357 N NZ  . LYS A 184 ? 0.38770 0.46801 0.48408 0.09713  -0.00275 0.08648  191 LYS A NZ  
1358 N N   . GLU A 185 ? 0.45792 0.26415 0.44023 0.10635  0.01233  0.07421  192 GLU A N   
1359 C CA  . GLU A 185 ? 0.49037 0.25551 0.46762 0.09720  0.01442  0.08532  192 GLU A CA  
1360 C C   . GLU A 185 ? 0.50859 0.29632 0.47963 0.08275  0.00932  0.10324  192 GLU A C   
1361 O O   . GLU A 185 ? 0.48428 0.24984 0.45108 0.06548  0.01325  0.10770  192 GLU A O   
1362 C CB  . GLU A 185 ? 0.53945 0.26971 0.52060 0.12155  0.01965  0.10083  192 GLU A CB  
1363 C CG  . GLU A 185 ? 0.94196 0.60772 0.92314 0.11308  0.02759  0.09745  192 GLU A CG  
1364 C CD  . GLU A 185 ? 1.13379 0.75522 1.11914 0.13851  0.03452  0.11510  192 GLU A CD  
1365 O OE1 . GLU A 185 ? 1.08005 0.64643 1.06936 0.12902  0.04125  0.11722  192 GLU A OE1 
1366 O OE2 . GLU A 185 ? 1.04276 0.68727 1.03136 0.16672  0.03267  0.12597  192 GLU A OE2 
1367 N N   . ASP A 186 ? 0.44365 0.27630 0.41545 0.08940  0.00102  0.11245  193 ASP A N   
1368 C CA  . ASP A 186 ? 0.52636 0.38007 0.48675 0.07941  -0.00476 0.12597  193 ASP A CA  
1369 C C   . ASP A 186 ? 0.47597 0.35660 0.43452 0.05882  -0.00833 0.11003  193 ASP A C   
1370 O O   . ASP A 186 ? 0.42753 0.32989 0.37558 0.05220  -0.01357 0.11625  193 ASP A O   
1371 C CB  . ASP A 186 ? 0.45614 0.34308 0.41668 0.09834  -0.01542 0.14277  193 ASP A CB  
1372 C CG  . ASP A 186 ? 0.57821 0.50813 0.55869 0.10383  -0.02345 0.13081  193 ASP A CG  
1373 O OD1 . ASP A 186 ? 0.58679 0.51590 0.57845 0.09915  -0.01738 0.11373  193 ASP A OD1 
1374 O OD2 . ASP A 186 ? 0.79639 0.76349 0.78226 0.11318  -0.03597 0.13931  193 ASP A OD2 
1375 N N   . GLN A 187 ? 0.37495 0.25311 0.34039 0.05067  -0.00531 0.08961  194 GLN A N   
1376 C CA  . GLN A 187 ? 0.36279 0.26458 0.32724 0.03492  -0.00819 0.07688  194 GLN A CA  
1377 C C   . GLN A 187 ? 0.34410 0.22647 0.30607 0.01855  -0.00326 0.06510  194 GLN A C   
1378 O O   . GLN A 187 ? 0.33682 0.23399 0.29991 0.01053  -0.00479 0.05105  194 GLN A O   
1379 C CB  . GLN A 187 ? 0.32655 0.25311 0.30200 0.04098  -0.00985 0.06679  194 GLN A CB  
1380 C CG  . GLN A 187 ? 0.31457 0.26742 0.30281 0.05483  -0.01553 0.07754  194 GLN A CG  
1381 C CD  . GLN A 187 ? 0.37795 0.35547 0.36303 0.04853  -0.02649 0.08405  194 GLN A CD  
1382 O OE1 . GLN A 187 ? 0.33409 0.31621 0.31112 0.03425  -0.02806 0.07703  194 GLN A OE1 
1383 N NE2 . GLN A 187 ? 0.31736 0.31265 0.30809 0.06138  -0.03495 0.09564  194 GLN A NE2 
1384 N N   . THR A 188 ? 0.38985 0.24072 0.35155 0.01314  0.00256  0.07188  195 THR A N   
1385 C CA  . THR A 188 ? 0.39899 0.23645 0.36730 -0.00487 0.00561  0.05846  195 THR A CA  
1386 C C   . THR A 188 ? 0.37572 0.23741 0.34326 -0.02004 0.00638  0.06123  195 THR A C   
1387 O O   . THR A 188 ? 0.35960 0.22063 0.33791 -0.03518 0.00784  0.05011  195 THR A O   
1388 C CB  . THR A 188 ? 0.50174 0.29499 0.47855 -0.00958 0.01285  0.06348  195 THR A CB  
1389 O OG1 . THR A 188 ? 0.51828 0.30391 0.48986 -0.00805 0.01962  0.09156  195 THR A OG1 
1390 C CG2 . THR A 188 ? 0.58917 0.35388 0.56648 0.00793  0.01277  0.05556  195 THR A CG2 
1391 N N   . GLU A 189 ? 0.34637 0.23211 0.30259 -0.01536 0.00454  0.07322  196 GLU A N   
1392 C CA  . GLU A 189 ? 0.36288 0.27264 0.31637 -0.02610 0.00601  0.07135  196 GLU A CA  
1393 C C   . GLU A 189 ? 0.30152 0.22835 0.26277 -0.03118 0.00124  0.05108  196 GLU A C   
1394 O O   . GLU A 189 ? 0.32470 0.26606 0.29115 -0.04094 0.00374  0.04617  196 GLU A O   
1395 C CB  . GLU A 189 ? 0.38103 0.31281 0.31743 -0.01748 0.00207  0.08097  196 GLU A CB  
1396 C CG  . GLU A 189 ? 0.30964 0.25904 0.24750 -0.00884 -0.00879 0.07096  196 GLU A CG  
1397 C CD  . GLU A 189 ? 0.51457 0.48568 0.43855 -0.00220 -0.01640 0.07581  196 GLU A CD  
1398 O OE1 . GLU A 189 ? 0.46507 0.43619 0.38310 0.00911  -0.02106 0.08817  196 GLU A OE1 
1399 O OE2 . GLU A 189 ? 0.36541 0.35309 0.28336 -0.00670 -0.01838 0.06660  196 GLU A OE2 
1400 N N   . TYR A 190 ? 0.28999 0.21798 0.25207 -0.02256 -0.00428 0.04138  197 TYR A N   
1401 C CA  . TYR A 190 ? 0.29510 0.23866 0.26010 -0.02379 -0.00771 0.02674  197 TYR A CA  
1402 C C   . TYR A 190 ? 0.34979 0.28473 0.32221 -0.03081 -0.00874 0.01264  197 TYR A C   
1403 O O   . TYR A 190 ? 0.32171 0.26990 0.29290 -0.02813 -0.01313 0.00062  197 TYR A O   
1404 C CB  . TYR A 190 ? 0.25914 0.20995 0.22195 -0.01137 -0.01019 0.02548  197 TYR A CB  
1405 C CG  . TYR A 190 ? 0.25071 0.21431 0.21324 -0.00824 -0.01262 0.03553  197 TYR A CG  
1406 C CD1 . TYR A 190 ? 0.27695 0.25580 0.23786 -0.01329 -0.01472 0.03364  197 TYR A CD1 
1407 C CD2 . TYR A 190 ? 0.31181 0.27285 0.27619 0.00051  -0.01421 0.04477  197 TYR A CD2 
1408 C CE1 . TYR A 190 ? 0.28775 0.27784 0.24765 -0.01140 -0.01994 0.03726  197 TYR A CE1 
1409 C CE2 . TYR A 190 ? 0.31168 0.28952 0.27717 0.00282  -0.02043 0.05084  197 TYR A CE2 
1410 C CZ  . TYR A 190 ? 0.32168 0.31338 0.28424 -0.00424 -0.02403 0.04529  197 TYR A CZ  
1411 O OH  . TYR A 190 ? 0.28383 0.29193 0.24662 -0.00266 -0.03303 0.04589  197 TYR A OH  
1412 N N   . LEU A 191 ? 0.30561 0.21877 0.28650 -0.03969 -0.00547 0.01386  198 LEU A N   
1413 C CA  . LEU A 191 ? 0.31992 0.22779 0.31492 -0.05163 -0.00871 -0.00264 198 LEU A CA  
1414 C C   . LEU A 191 ? 0.36844 0.29104 0.38169 -0.06891 -0.00429 0.00188  198 LEU A C   
1415 O O   . LEU A 191 ? 0.35272 0.27794 0.38620 -0.08233 -0.00798 -0.01197 198 LEU A O   
1416 C CB  . LEU A 191 ? 0.35691 0.22558 0.35692 -0.05264 -0.00751 -0.00797 198 LEU A CB  
1417 C CG  . LEU A 191 ? 0.46496 0.32044 0.44865 -0.03291 -0.00981 -0.01490 198 LEU A CG  
1418 C CD1 . LEU A 191 ? 0.49215 0.30550 0.48123 -0.03250 -0.00841 -0.02402 198 LEU A CD1 
1419 C CD2 . LEU A 191 ? 0.38731 0.26678 0.36029 -0.02549 -0.01740 -0.03251 198 LEU A CD2 
1420 N N   . GLU A 192 ? 0.30915 0.24348 0.31690 -0.06856 0.00362  0.01995  199 GLU A N   
1421 C CA  . GLU A 192 ? 0.35442 0.30481 0.37806 -0.08236 0.01264  0.02800  199 GLU A CA  
1422 C C   . GLU A 192 ? 0.30718 0.29497 0.33510 -0.08069 0.00851  0.01768  199 GLU A C   
1423 O O   . GLU A 192 ? 0.26728 0.26580 0.27719 -0.06731 0.00490  0.01700  199 GLU A O   
1424 C CB  . GLU A 192 ? 0.36788 0.31515 0.37610 -0.07822 0.02420  0.05210  199 GLU A CB  
1425 C CG  . GLU A 192 ? 0.40561 0.31648 0.40813 -0.07600 0.02983  0.06889  199 GLU A CG  
1426 C CD  . GLU A 192 ? 0.88985 0.77528 0.92051 -0.09416 0.03776  0.07118  199 GLU A CD  
1427 O OE1 . GLU A 192 ? 0.83988 0.74463 0.89613 -0.11121 0.04273  0.06673  199 GLU A OE1 
1428 O OE2 . GLU A 192 ? 0.72789 0.57412 0.75867 -0.09142 0.03940  0.07747  199 GLU A OE2 
1429 N N   . GLU A 193 ? 0.29011 0.29773 0.34578 -0.09436 0.00943  0.01043  200 GLU A N   
1430 C CA  . GLU A 193 ? 0.27118 0.31647 0.33462 -0.08988 0.00458  0.00058  200 GLU A CA  
1431 C C   . GLU A 193 ? 0.32299 0.38347 0.36931 -0.07843 0.01313  0.01151  200 GLU A C   
1432 O O   . GLU A 193 ? 0.26012 0.33245 0.29538 -0.06493 0.00729  0.00506  200 GLU A O   
1433 C CB  . GLU A 193 ? 0.34197 0.41250 0.44530 -0.10764 0.00550  -0.00632 200 GLU A CB  
1434 C CG  . GLU A 193 ? 0.51242 0.62868 0.62985 -0.10211 0.00592  -0.00973 200 GLU A CG  
1435 C CD  . GLU A 193 ? 0.69585 0.84524 0.85931 -0.11857 0.00026  -0.02211 200 GLU A CD  
1436 O OE1 . GLU A 193 ? 0.60058 0.73697 0.79119 -0.14036 0.00302  -0.02289 200 GLU A OE1 
1437 O OE2 . GLU A 193 ? 0.72859 0.91675 0.90369 -0.10947 -0.00803 -0.03153 200 GLU A OE2 
1438 N N   . ARG A 194 ? 0.27710 0.33545 0.31898 -0.08228 0.02748  0.02800  201 ARG A N   
1439 C CA  . ARG A 194 ? 0.26338 0.33899 0.28671 -0.06991 0.03410  0.03232  201 ARG A CA  
1440 C C   . ARG A 194 ? 0.25692 0.31482 0.24923 -0.05557 0.02575  0.03051  201 ARG A C   
1441 O O   . ARG A 194 ? 0.25003 0.31841 0.23056 -0.04447 0.02443  0.02430  201 ARG A O   
1442 C CB  . ARG A 194 ? 0.40786 0.49166 0.42876 -0.07444 0.05275  0.05032  201 ARG A CB  
1443 C CG  . ARG A 194 ? 0.53725 0.59173 0.54407 -0.07792 0.05779  0.06780  201 ARG A CG  
1444 C CD  . ARG A 194 ? 0.66229 0.72663 0.67771 -0.08675 0.07958  0.08921  201 ARG A CD  
1445 N NE  . ARG A 194 ? 0.87038 0.90587 0.86233 -0.08334 0.08534  0.11083  201 ARG A NE  
1446 C CZ  . ARG A 194 ? 0.85893 0.89970 0.83421 -0.08005 0.10412  0.13534  201 ARG A CZ  
1447 N NH1 . ARG A 194 ? 0.57847 0.65304 0.56050 -0.08147 0.12176  0.14117  201 ARG A NH1 
1448 N NH2 . ARG A 194 ? 0.72586 0.74031 0.67482 -0.07193 0.10592  0.15565  201 ARG A NH2 
1449 N N   . ARG A 195 ? 0.26217 0.29369 0.24492 -0.05560 0.02020  0.03495  202 ARG A N   
1450 C CA  . ARG A 195 ? 0.25544 0.27662 0.21832 -0.04408 0.01159  0.03292  202 ARG A CA  
1451 C C   . ARG A 195 ? 0.29012 0.31519 0.25866 -0.03850 0.00295  0.01985  202 ARG A C   
1452 O O   . ARG A 195 ? 0.23674 0.26401 0.19708 -0.03060 -0.00055 0.01571  202 ARG A O   
1453 C CB  . ARG A 195 ? 0.29258 0.28984 0.24966 -0.04322 0.00864  0.04171  202 ARG A CB  
1454 C CG  . ARG A 195 ? 0.27045 0.26455 0.21524 -0.03246 -0.00053 0.04042  202 ARG A CG  
1455 C CD  . ARG A 195 ? 0.36130 0.36657 0.28697 -0.02666 -0.00131 0.04429  202 ARG A CD  
1456 N NE  . ARG A 195 ? 0.27240 0.27707 0.19324 -0.01926 -0.01218 0.04351  202 ARG A NE  
1457 C CZ  . ARG A 195 ? 0.34137 0.35593 0.26136 -0.01652 -0.02022 0.03219  202 ARG A CZ  
1458 N NH1 . ARG A 195 ? 0.27857 0.29988 0.19645 -0.01745 -0.01802 0.02102  202 ARG A NH1 
1459 N NH2 . ARG A 195 ? 0.32969 0.34748 0.25472 -0.01272 -0.03056 0.03157  202 ARG A NH2 
1460 N N   . ILE A 196 ? 0.23184 0.25693 0.21406 -0.04223 -0.00059 0.01329  203 ILE A N   
1461 C CA  . ILE A 196 ? 0.23318 0.26302 0.21553 -0.03366 -0.00747 0.00490  203 ILE A CA  
1462 C C   . ILE A 196 ? 0.21380 0.26292 0.19988 -0.02766 -0.00590 0.00131  203 ILE A C   
1463 O O   . ILE A 196 ? 0.24034 0.28606 0.22052 -0.01797 -0.00781 0.00047  203 ILE A O   
1464 C CB  . ILE A 196 ? 0.22496 0.25440 0.21526 -0.03628 -0.01341 -0.00370 203 ILE A CB  
1465 C CG1 . ILE A 196 ? 0.23682 0.24138 0.22127 -0.03787 -0.01391 -0.00201 203 ILE A CG1 
1466 C CG2 . ILE A 196 ? 0.22363 0.26192 0.20801 -0.02371 -0.01936 -0.00903 203 ILE A CG2 
1467 C CD1 . ILE A 196 ? 0.28443 0.28410 0.27690 -0.04300 -0.02011 -0.01585 203 ILE A CD1 
1468 N N   . LYS A 197 ? 0.21631 0.28530 0.21543 -0.03289 -0.00082 0.00018  204 LYS A N   
1469 C CA  . LYS A 197 ? 0.24379 0.33293 0.24804 -0.02364 0.00212  -0.00350 204 LYS A CA  
1470 C C   . LYS A 197 ? 0.24255 0.32032 0.22923 -0.01567 0.00601  -0.00300 204 LYS A C   
1471 O O   . LYS A 197 ? 0.24305 0.31885 0.22808 -0.00422 0.00471  -0.00764 204 LYS A O   
1472 C CB  . LYS A 197 ? 0.23809 0.35584 0.26299 -0.03053 0.01017  -0.00314 204 LYS A CB  
1473 C CG  . LYS A 197 ? 0.34953 0.48712 0.40093 -0.03908 0.00334  -0.00904 204 LYS A CG  
1474 C CD  . LYS A 197 ? 0.40733 0.57707 0.48764 -0.04919 0.01399  -0.00648 204 LYS A CD  
1475 C CE  . LYS A 197 ? 0.56368 0.76231 0.67946 -0.05886 0.00412  -0.01640 204 LYS A CE  
1476 N NZ  . LYS A 197 ? 0.49433 0.71875 0.64649 -0.07719 0.01632  -0.01129 204 LYS A NZ  
1477 N N   . GLU A 198 ? 0.22822 0.29776 0.20147 -0.02079 0.01014  0.00206  205 GLU A N   
1478 C CA  . GLU A 198 ? 0.23908 0.29953 0.19329 -0.01370 0.00967  -0.00195 205 GLU A CA  
1479 C C   . GLU A 198 ? 0.25510 0.29694 0.20910 -0.00979 0.00043  -0.00651 205 GLU A C   
1480 O O   . GLU A 198 ? 0.24280 0.27769 0.19377 -0.00284 -0.00088 -0.01525 205 GLU A O   
1481 C CB  . GLU A 198 ? 0.25291 0.30916 0.18978 -0.01809 0.01165  0.00628  205 GLU A CB  
1482 C CG  . GLU A 198 ? 0.26982 0.32172 0.18442 -0.01081 0.00718  -0.00098 205 GLU A CG  
1483 C CD  . GLU A 198 ? 0.31313 0.36486 0.20751 -0.01172 0.00701  0.01014  205 GLU A CD  
1484 O OE1 . GLU A 198 ? 0.32688 0.36937 0.22852 -0.01760 0.00512  0.02186  205 GLU A OE1 
1485 O OE2 . GLU A 198 ? 0.31270 0.37358 0.18176 -0.00419 0.00939  0.00756  205 GLU A OE2 
1486 N N   . ILE A 199 ? 0.22387 0.25625 0.18274 -0.01422 -0.00453 -0.00068 206 ILE A N   
1487 C CA  . ILE A 199 ? 0.23056 0.24907 0.19284 -0.01181 -0.00983 -0.00111 206 ILE A CA  
1488 C C   . ILE A 199 ? 0.22063 0.23697 0.19150 -0.00386 -0.00821 -0.00242 206 ILE A C   
1489 O O   . ILE A 199 ? 0.24469 0.24790 0.22025 -0.00075 -0.00868 -0.00442 206 ILE A O   
1490 C CB  . ILE A 199 ? 0.24854 0.26144 0.21324 -0.01526 -0.01241 0.00645  206 ILE A CB  
1491 C CG1 . ILE A 199 ? 0.29303 0.30520 0.24901 -0.01941 -0.01434 0.01059  206 ILE A CG1 
1492 C CG2 . ILE A 199 ? 0.21987 0.22470 0.19353 -0.01272 -0.01406 0.00909  206 ILE A CG2 
1493 C CD1 . ILE A 199 ? 0.25312 0.25819 0.21183 -0.02030 -0.01466 0.01784  206 ILE A CD1 
1494 N N   . VAL A 200 ? 0.23025 0.25899 0.20508 -0.00042 -0.00706 -0.00069 207 VAL A N   
1495 C CA  . VAL A 200 ? 0.21939 0.24957 0.19911 0.01139  -0.00645 0.00120  207 VAL A CA  
1496 C C   . VAL A 200 ? 0.25444 0.28214 0.23678 0.01945  -0.00266 -0.00461 207 VAL A C   
1497 O O   . VAL A 200 ? 0.26448 0.27492 0.25009 0.02765  -0.00085 -0.00246 207 VAL A O   
1498 C CB  . VAL A 200 ? 0.21508 0.26669 0.19825 0.01435  -0.00989 0.00093  207 VAL A CB  
1499 C CG1 . VAL A 200 ? 0.22417 0.28394 0.21024 0.03117  -0.01051 0.00415  207 VAL A CG1 
1500 C CG2 . VAL A 200 ? 0.21629 0.26407 0.19338 0.00981  -0.01391 0.00286  207 VAL A CG2 
1501 N N   . LYS A 201 ? 0.23245 0.27507 0.21364 0.01783  0.00053  -0.01156 208 LYS A N   
1502 C CA  . LYS A 201 ? 0.24904 0.28964 0.22957 0.02841  0.00560  -0.02011 208 LYS A CA  
1503 C C   . LYS A 201 ? 0.35027 0.36174 0.32390 0.02720  0.00357  -0.02767 208 LYS A C   
1504 O O   . LYS A 201 ? 0.33851 0.33276 0.31584 0.03755  0.00578  -0.03403 208 LYS A O   
1505 C CB  . LYS A 201 ? 0.25127 0.31638 0.22906 0.02702  0.01249  -0.02481 208 LYS A CB  
1506 C CG  . LYS A 201 ? 0.44305 0.51615 0.42252 0.04341  0.02045  -0.03403 208 LYS A CG  
1507 C CD  . LYS A 201 ? 0.62243 0.71658 0.59181 0.04250  0.03071  -0.03836 208 LYS A CD  
1508 C CE  . LYS A 201 ? 0.89291 0.98293 0.85159 0.06039  0.03836  -0.05331 208 LYS A CE  
1509 N NZ  . LYS A 201 ? 0.71835 0.77794 0.65182 0.05960  0.03259  -0.06742 208 LYS A NZ  
1510 N N   . LYS A 202 ? 0.27655 0.28226 0.24289 0.01500  -0.00155 -0.02819 209 LYS A N   
1511 C CA  . LYS A 202 ? 0.28037 0.26598 0.24383 0.01167  -0.00695 -0.03958 209 LYS A CA  
1512 C C   . LYS A 202 ? 0.28458 0.24681 0.26661 0.00969  -0.00851 -0.03457 209 LYS A C   
1513 O O   . LYS A 202 ? 0.30871 0.24814 0.29847 0.01034  -0.00994 -0.04546 209 LYS A O   
1514 C CB  . LYS A 202 ? 0.32639 0.32033 0.27831 0.00152  -0.01379 -0.03992 209 LYS A CB  
1515 C CG  . LYS A 202 ? 0.35054 0.33196 0.30417 -0.00456 -0.02467 -0.05241 209 LYS A CG  
1516 C CD  . LYS A 202 ? 0.38987 0.38786 0.32637 -0.00881 -0.03225 -0.05126 209 LYS A CD  
1517 C CE  . LYS A 202 ? 0.64941 0.64448 0.58733 -0.01383 -0.04738 -0.06714 209 LYS A CE  
1518 N NZ  . LYS A 202 ? 0.59164 0.60642 0.51469 -0.01482 -0.05667 -0.06123 209 LYS A NZ  
1519 N N   . HIS A 203 ? 0.26698 0.23327 0.25672 0.00773  -0.00686 -0.01828 210 HIS A N   
1520 C CA  . HIS A 203 ? 0.27461 0.22387 0.28144 0.00404  -0.00538 -0.00864 210 HIS A CA  
1521 C C   . HIS A 203 ? 0.28800 0.23137 0.29896 0.01606  0.00263  0.00680  210 HIS A C   
1522 O O   . HIS A 203 ? 0.30266 0.22719 0.32854 0.01539  0.00809  0.01751  210 HIS A O   
1523 C CB  . HIS A 203 ? 0.25458 0.21516 0.26471 -0.00549 -0.00830 -0.00029 210 HIS A CB  
1524 C CG  . HIS A 203 ? 0.25515 0.22163 0.26444 -0.01548 -0.01770 -0.01134 210 HIS A CG  
1525 N ND1 . HIS A 203 ? 0.29395 0.24941 0.31802 -0.02330 -0.02419 -0.02297 210 HIS A ND1 
1526 C CD2 . HIS A 203 ? 0.31330 0.29589 0.30899 -0.01797 -0.02276 -0.01205 210 HIS A CD2 
1527 C CE1 . HIS A 203 ? 0.35702 0.32680 0.37385 -0.02862 -0.03490 -0.03145 210 HIS A CE1 
1528 N NE2 . HIS A 203 ? 0.31544 0.30038 0.31380 -0.02432 -0.03296 -0.02272 210 HIS A NE2 
1529 N N   . SER A 204 ? 0.30085 0.30261 0.16335 -0.03224 -0.04330 -0.01692 211 SER A N   
1530 C CA  . SER A 204 ? 0.26654 0.27582 0.16287 -0.02091 -0.03378 -0.01818 211 SER A CA  
1531 C C   . SER A 204 ? 0.27530 0.27264 0.16574 -0.00952 -0.01538 -0.03115 211 SER A C   
1532 O O   . SER A 204 ? 0.30701 0.31315 0.22462 0.00091  -0.00884 -0.02947 211 SER A O   
1533 C CB  . SER A 204 ? 0.26159 0.29699 0.19143 -0.01459 -0.03272 -0.00486 211 SER A CB  
1534 O OG  . SER A 204 ? 0.26749 0.31603 0.21240 -0.02200 -0.04785 0.00670  211 SER A OG  
1535 N N   . GLN A 205 ? 0.32669 0.30339 0.18204 -0.01146 -0.00713 -0.04442 212 GLN A N   
1536 C CA  . GLN A 205 ? 0.43286 0.40385 0.29077 0.00170  0.01461  -0.05683 212 GLN A CA  
1537 C C   . GLN A 205 ? 0.47217 0.43343 0.35664 0.01283  0.01532  -0.06210 212 GLN A C   
1538 O O   . GLN A 205 ? 0.41499 0.38638 0.32685 0.02681  0.02732  -0.06365 212 GLN A O   
1539 C CB  . GLN A 205 ? 0.50629 0.45190 0.31634 -0.00287 0.02676  -0.07323 212 GLN A CB  
1540 C CG  . GLN A 205 ? 0.77666 0.72058 0.59565 0.01242  0.05480  -0.08716 212 GLN A CG  
1541 C CD  . GLN A 205 ? 0.89243 0.80205 0.66025 0.00960  0.07070  -0.10923 212 GLN A CD  
1542 O OE1 . GLN A 205 ? 0.73021 0.61735 0.44677 -0.00725 0.05828  -0.11243 212 GLN A OE1 
1543 N NE2 . GLN A 205 ? 0.82918 0.73375 0.61141 0.02618  0.09779  -0.12519 212 GLN A NE2 
1544 N N   . PHE A 206 ? 0.32509 0.26790 0.20533 0.00569  0.00057  -0.06222 213 PHE A N   
1545 C CA  . PHE A 206 ? 0.33330 0.25797 0.23120 0.01430  -0.00046 -0.06565 213 PHE A CA  
1546 C C   . PHE A 206 ? 0.29432 0.23391 0.22009 0.01340  -0.01137 -0.04903 213 PHE A C   
1547 O O   . PHE A 206 ? 0.32440 0.24561 0.25932 0.01654  -0.01644 -0.04730 213 PHE A O   
1548 C CB  . PHE A 206 ? 0.37743 0.26241 0.24740 0.00555  -0.00726 -0.07817 213 PHE A CB  
1549 C CG  . PHE A 206 ? 0.42598 0.28744 0.26033 0.00773  0.00701  -0.09892 213 PHE A CG  
1550 C CD1 . PHE A 206 ? 0.43386 0.29643 0.28070 0.02683  0.02991  -0.10975 213 PHE A CD1 
1551 C CD2 . PHE A 206 ? 0.49569 0.33424 0.28409 -0.01007 -0.00204 -0.10781 213 PHE A CD2 
1552 C CE1 . PHE A 206 ? 0.48647 0.32673 0.29811 0.02975  0.05007  -0.13129 213 PHE A CE1 
1553 C CE2 . PHE A 206 ? 0.64805 0.45896 0.39141 -0.00940 0.01387  -0.12950 213 PHE A CE2 
1554 C CZ  . PHE A 206 ? 0.57564 0.38689 0.32954 0.01112  0.04283  -0.14213 213 PHE A CZ  
1555 N N   . ILE A 207 ? 0.30095 0.26978 0.23782 0.00974  -0.01372 -0.03700 214 ILE A N   
1556 C CA  . ILE A 207 ? 0.26148 0.24257 0.21856 0.01008  -0.01871 -0.02428 214 ILE A CA  
1557 C C   . ILE A 207 ? 0.32176 0.29943 0.29453 0.02357  -0.01592 -0.02406 214 ILE A C   
1558 O O   . ILE A 207 ? 0.30475 0.29116 0.28772 0.03389  -0.00756 -0.02949 214 ILE A O   
1559 C CB  . ILE A 207 ? 0.21162 0.22059 0.17794 0.00730  -0.01809 -0.01542 214 ILE A CB  
1560 C CG1 . ILE A 207 ? 0.28328 0.29786 0.24358 -0.00519 -0.02561 -0.01197 214 ILE A CG1 
1561 C CG2 . ILE A 207 ? 0.21145 0.22885 0.19146 0.00963  -0.01848 -0.00656 214 ILE A CG2 
1562 C CD1 . ILE A 207 ? 0.27556 0.28691 0.24327 -0.01581 -0.03290 -0.00598 214 ILE A CD1 
1563 N N   . GLY A 208 ? 0.25921 0.22458 0.23534 0.02233  -0.02384 -0.01604 215 GLY A N   
1564 C CA  . GLY A 208 ? 0.25353 0.20877 0.24340 0.03443  -0.02768 -0.01379 215 GLY A CA  
1565 C C   . GLY A 208 ? 0.28479 0.25937 0.28599 0.03752  -0.03185 -0.00445 215 GLY A C   
1566 O O   . GLY A 208 ? 0.29662 0.26099 0.30296 0.04169  -0.04255 0.00380  215 GLY A O   
1567 N N   . TYR A 209 ? 0.24353 0.24209 0.24614 0.03443  -0.02599 -0.00505 216 TYR A N   
1568 C CA  . TYR A 209 ? 0.21600 0.22884 0.22565 0.03526  -0.03033 0.00078  216 TYR A CA  
1569 C C   . TYR A 209 ? 0.20809 0.24261 0.23197 0.03808  -0.02192 -0.00444 216 TYR A C   
1570 O O   . TYR A 209 ? 0.20887 0.24760 0.22652 0.03546  -0.01277 -0.00943 216 TYR A O   
1571 C CB  . TYR A 209 ? 0.21019 0.22306 0.20110 0.02484  -0.03065 0.00684  216 TYR A CB  
1572 C CG  . TYR A 209 ? 0.25101 0.24358 0.22508 0.01862  -0.03576 0.01433  216 TYR A CG  
1573 C CD1 . TYR A 209 ? 0.28125 0.25940 0.24557 0.01901  -0.04778 0.02286  216 TYR A CD1 
1574 C CD2 . TYR A 209 ? 0.21691 0.20324 0.18492 0.01044  -0.03089 0.01476  216 TYR A CD2 
1575 C CE1 . TYR A 209 ? 0.33503 0.29030 0.27907 0.01120  -0.05235 0.03276  216 TYR A CE1 
1576 C CE2 . TYR A 209 ? 0.24206 0.20863 0.19593 0.00181  -0.03439 0.02365  216 TYR A CE2 
1577 C CZ  . TYR A 209 ? 0.26532 0.21502 0.20526 0.00241  -0.04394 0.03301  216 TYR A CZ  
1578 O OH  . TYR A 209 ? 0.30165 0.22825 0.22262 -0.00821 -0.04719 0.04477  216 TYR A OH  
1579 N N   . PRO A 210 ? 0.21184 0.25889 0.25279 0.04092  -0.02668 -0.00181 217 PRO A N   
1580 C CA  . PRO A 210 ? 0.20932 0.27643 0.26599 0.04082  -0.01792 -0.00465 217 PRO A CA  
1581 C C   . PRO A 210 ? 0.25838 0.32773 0.29878 0.03236  -0.01383 -0.00348 217 PRO A C   
1582 O O   . PRO A 210 ? 0.24047 0.30408 0.26961 0.02785  -0.01946 -0.00069 217 PRO A O   
1583 C CB  . PRO A 210 ? 0.23923 0.31780 0.32108 0.04267  -0.02915 -0.00020 217 PRO A CB  
1584 C CG  . PRO A 210 ? 0.28329 0.34504 0.34861 0.04052  -0.04545 0.00567  217 PRO A CG  
1585 C CD  . PRO A 210 ? 0.21447 0.25672 0.26161 0.04264  -0.04275 0.00530  217 PRO A CD  
1586 N N   . ILE A 211 ? 0.21219 0.28768 0.25003 0.03068  -0.00357 -0.00556 218 ILE A N   
1587 C CA  . ILE A 211 ? 0.20511 0.28273 0.23402 0.02458  -0.00162 -0.00200 218 ILE A CA  
1588 C C   . ILE A 211 ? 0.24160 0.33047 0.28422 0.02205  0.00306  0.00059  218 ILE A C   
1589 O O   . ILE A 211 ? 0.23472 0.33141 0.28161 0.02218  0.01309  -0.00060 218 ILE A O   
1590 C CB  . ILE A 211 ? 0.25647 0.32955 0.26840 0.02152  0.00121  -0.00233 218 ILE A CB  
1591 C CG1 . ILE A 211 ? 0.17838 0.24104 0.18153 0.02058  -0.00434 -0.00372 218 ILE A CG1 
1592 C CG2 . ILE A 211 ? 0.19359 0.27019 0.20293 0.01685  0.00014  0.00468  218 ILE A CG2 
1593 C CD1 . ILE A 211 ? 0.19168 0.24693 0.17739 0.01519  -0.00551 -0.00625 218 ILE A CD1 
1594 N N   . THR A 212 ? 0.18730 0.27472 0.23493 0.01848  -0.00227 0.00352  219 THR A N   
1595 C CA  . THR A 212 ? 0.22645 0.32146 0.28932 0.01298  -0.00009 0.00722  219 THR A CA  
1596 C C   . THR A 212 ? 0.22886 0.31508 0.28202 0.00871  0.00131  0.01289  219 THR A C   
1597 O O   . THR A 212 ? 0.15615 0.23039 0.20288 0.01037  -0.00348 0.01197  219 THR A O   
1598 C CB  . THR A 212 ? 0.18015 0.27485 0.25664 0.01003  -0.01118 0.00589  219 THR A CB  
1599 O OG1 . THR A 212 ? 0.20979 0.31279 0.29902 0.01528  -0.01640 0.00391  219 THR A OG1 
1600 C CG2 . THR A 212 ? 0.19931 0.30220 0.29627 0.00111  -0.01036 0.01041  219 THR A CG2 
1601 N N   . LEU A 213 ? 0.19617 0.28696 0.24770 0.00380  0.00892  0.01935  220 LEU A N   
1602 C CA  . LEU A 213 ? 0.26879 0.34843 0.31254 -0.00054 0.00686  0.02870  220 LEU A CA  
1603 C C   . LEU A 213 ? 0.32617 0.40172 0.38596 -0.00819 0.00551  0.03276  220 LEU A C   
1604 O O   . LEU A 213 ? 0.23733 0.32489 0.30867 -0.01577 0.01288  0.03638  220 LEU A O   
1605 C CB  . LEU A 213 ? 0.24766 0.32842 0.27146 -0.00499 0.01298  0.03616  220 LEU A CB  
1606 C CG  . LEU A 213 ? 0.34864 0.41680 0.36343 -0.01165 0.00868  0.05111  220 LEU A CG  
1607 C CD1 . LEU A 213 ? 0.33852 0.39467 0.36054 -0.00454 -0.00427 0.05405  220 LEU A CD1 
1608 C CD2 . LEU A 213 ? 0.26833 0.33490 0.25108 -0.01854 0.01299  0.05858  220 LEU A CD2 
1609 N N   . PHE A 214 ? 0.25066 0.30880 0.31293 -0.00681 -0.00249 0.03094  221 PHE A N   
1610 C CA  . PHE A 214 ? 0.21766 0.26385 0.29170 -0.01590 -0.00635 0.03341  221 PHE A CA  
1611 C C   . PHE A 214 ? 0.30584 0.34267 0.37798 -0.02327 -0.00378 0.04867  221 PHE A C   
1612 O O   . PHE A 214 ? 0.36490 0.39294 0.42554 -0.01793 -0.00552 0.05607  221 PHE A O   
1613 C CB  . PHE A 214 ? 0.24816 0.27011 0.31819 -0.01169 -0.01361 0.02391  221 PHE A CB  
1614 C CG  . PHE A 214 ? 0.24943 0.27312 0.31433 -0.01055 -0.01876 0.01087  221 PHE A CG  
1615 C CD1 . PHE A 214 ? 0.20389 0.24743 0.26700 -0.00597 -0.01761 0.00859  221 PHE A CD1 
1616 C CD2 . PHE A 214 ? 0.30811 0.30821 0.36540 -0.01506 -0.02628 0.00122  221 PHE A CD2 
1617 C CE1 . PHE A 214 ? 0.23628 0.27746 0.29099 -0.00573 -0.02553 0.00019  221 PHE A CE1 
1618 C CE2 . PHE A 214 ? 0.36036 0.35766 0.40325 -0.01638 -0.03394 -0.00916 221 PHE A CE2 
1619 C CZ  . PHE A 214 ? 0.24324 0.26212 0.28567 -0.01176 -0.03443 -0.00783 221 PHE A CZ  
1620 N N   . VAL A 215 ? 0.21703 0.25587 0.30212 -0.03690 -0.00139 0.05540  222 VAL A N   
1621 C CA  . VAL A 215 ? 0.24362 0.26949 0.32388 -0.04731 0.00109  0.07282  222 VAL A CA  
1622 C C   . VAL A 215 ? 0.31062 0.30394 0.39933 -0.05133 -0.00975 0.07378  222 VAL A C   
1623 O O   . VAL A 215 ? 0.30412 0.28976 0.40223 -0.05146 -0.01650 0.06007  222 VAL A O   
1624 C CB  . VAL A 215 ? 0.36729 0.41588 0.45645 -0.06210 0.01523  0.08160  222 VAL A CB  
1625 C CG1 . VAL A 215 ? 0.41539 0.49357 0.50187 -0.05499 0.02764  0.07314  222 VAL A CG1 
1626 C CG2 . VAL A 215 ? 0.38391 0.43871 0.50310 -0.07301 0.01223  0.07852  222 VAL A CG2 
1627 N N   . GLU A 216 ? 0.30961 0.27843 0.39122 -0.05410 -0.01323 0.08941  223 GLU A N   
1628 C CA  . GLU A 216 ? 0.40399 0.33485 0.49449 -0.05577 -0.02309 0.08848  223 GLU A CA  
1629 C C   . GLU A 216 ? 0.46198 0.38383 0.56506 -0.07840 -0.02343 0.09777  223 GLU A C   
1630 O O   . GLU A 216 ? 0.37532 0.31608 0.47864 -0.09269 -0.01402 0.11318  223 GLU A O   
1631 C CB  . GLU A 216 ? 0.42422 0.32694 0.50946 -0.04513 -0.03023 0.10108  223 GLU A CB  
1632 C CG  . GLU A 216 ? 0.54228 0.45811 0.62366 -0.02506 -0.03110 0.09554  223 GLU A CG  
1633 C CD  . GLU A 216 ? 0.61582 0.50336 0.70735 -0.01185 -0.04097 0.10563  223 GLU A CD  
1634 O OE1 . GLU A 216 ? 0.66969 0.52402 0.77450 -0.00713 -0.04346 0.09833  223 GLU A OE1 
1635 O OE2 . GLU A 216 ? 0.68488 0.58142 0.77197 -0.00643 -0.04753 0.12084  223 GLU A OE2 
1636 N N   . LYS A 217 ? 0.39932 0.29017 0.51158 -0.08304 -0.03319 0.08769  224 LYS A N   
1637 C CA  . LYS A 217 ? 0.39503 0.27672 0.52403 -0.10762 -0.03699 0.09410  224 LYS A CA  
1638 C C   . LYS A 217 ? 0.53429 0.38387 0.66196 -0.12025 -0.03836 0.11848  224 LYS A C   
1639 O O   . LYS A 217 ? 0.66197 0.48125 0.77762 -0.10705 -0.04293 0.12621  224 LYS A O   
1640 C CB  . LYS A 217 ? 0.41243 0.26693 0.54502 -0.11121 -0.05035 0.07236  224 LYS A CB  
1641 C CG  . LYS A 217 ? 0.38335 0.25465 0.50481 -0.09572 -0.05163 0.04923  224 LYS A CG  
1642 C CD  . LYS A 217 ? 0.41251 0.25394 0.52641 -0.10352 -0.06589 0.02836  224 LYS A CD  
1643 C CE  . LYS A 217 ? 0.44011 0.23565 0.52952 -0.08535 -0.06436 0.01214  224 LYS A CE  
1644 N NZ  . LYS A 217 ? 0.40577 0.22381 0.48429 -0.06159 -0.05264 0.00724  224 LYS A NZ  
# 
