data_7HAZ
# 
_entry.id   7HAZ 
# 
_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   7HAZ         pdb_00007haz 10.2210/pdb7haz/pdb 
WWPDB D_1001407246 ?            ?                   
# 
_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                        7HAZ 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.recvd_initial_deposition_date   2024-07-10 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.pdb_format_compatible           N 
_pdbx_database_status.methods_development_category    ? 
# 
_pdbx_contact_author.id                 1 
_pdbx_contact_author.name_last          Yu 
_pdbx_contact_author.name_first         Feng 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.email              yufeng@sari.ac.cn 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-9502-3277 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Huang, L.' 1  ? 
'Wang, W.'  2  ? 
'Zhu, Z.'   3  ? 
'Li, Q.'    4  ? 
'Li, M.'    5  ? 
'Zhou, H.'  6  ? 
'Xu, Q.'    7  ? 
'Wen, W.'   8  ? 
'Wang, Q.'  9  ? 
'Yu, F.'    10 ? 
# 
_citation.id                        primary 
_citation.title                     
;Novel starting points for fragment-based drug design against human heat-shock protein 90 identified using crystallographic fragment screening.
;
_citation.journal_abbrev            Iucrj 
_citation.journal_volume            12 
_citation.page_first                177 
_citation.page_last                 187 
_citation.year                      2025 
_citation.journal_id_ASTM           ? 
_citation.country                   UK 
_citation.journal_id_ISSN           2052-2525 
_citation.journal_id_CSD            ? 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   39819741 
_citation.pdbx_database_id_DOI      10.1107/S2052252524012247 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.identifier_ORCID 
_citation_author.ordinal 
primary 'Huang, L.' 0009-0001-8431-0182 1  
primary 'Wang, W.'  ?                   2  
primary 'Zhu, Z.'   ?                   3  
primary 'Li, Q.'    ?                   4  
primary 'Li, M.'    ?                   5  
primary 'Zhou, H.'  ?                   6  
primary 'Xu, Q.'    0000-0002-7137-0768 7  
primary 'Wen, W.'   ?                   8  
primary 'Wang, Q.'  ?                   9  
primary 'Yu, F.'    0000-0002-9502-3277 10 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Heat shock protein HSP 90-alpha' 26859.117 1   3.6.4.10 ? ? ? 
2 non-polymer syn '(2-phenoxyphenyl)methanol'       200.233   1   ?        ? ? ? 
3 water       nat water                             18.015    268 ?        ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        
;Heat shock 86 kDa,HSP 86,HSP86,Heat shock protein family C member 1,Lipopolysaccharide-associated protein 2,LAP-2,LPS-associated protein 2,Renal carcinoma antigen NY-REN-38
;
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;MDQPMEEEEVETFAFQAEIAQLMSLIINTFYSNKEIFLRELISNSSDALDKIRYESLTDPSKLDSGKELHINLIPNKQDR
TLTIVDTGIGMTKADLINNLGTIAKSGTKAFMEALQAGADISMIGQFGVGFYSAYLVAEKVTVITKHNDDEQYAWESSAG
GSFTVRTDTGEPMGRGTKVILHLKEDQTEYLEERRIKEIVKKHSQFIGYPITLFVEKERDKEVSDDEAELEHHHHHH
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MDQPMEEEEVETFAFQAEIAQLMSLIINTFYSNKEIFLRELISNSSDALDKIRYESLTDPSKLDSGKELHINLIPNKQDR
TLTIVDTGIGMTKADLINNLGTIAKSGTKAFMEALQAGADISMIGQFGVGFYSAYLVAEKVTVITKHNDDEQYAWESSAG
GSFTVRTDTGEPMGRGTKVILHLKEDQTEYLEERRIKEIVKKHSQFIGYPITLFVEKERDKEVSDDEAELEHHHHHH
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 '(2-phenoxyphenyl)methanol' A1AYI 
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 
A1AYI non-polymer         . '(2-phenoxyphenyl)methanol' ? 'C13 H12 O2'     200.233 
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        A1AYI 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1AYI 
_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 A1AYI 1   301 301 A1AYI AB5 A . 
C 3 HOH   1   401 143 HOH   HOH A . 
C 3 HOH   2   402 206 HOH   HOH A . 
C 3 HOH   3   403 106 HOH   HOH A . 
C 3 HOH   4   404 129 HOH   HOH A . 
C 3 HOH   5   405 150 HOH   HOH A . 
C 3 HOH   6   406 261 HOH   HOH A . 
C 3 HOH   7   407 85  HOH   HOH A . 
C 3 HOH   8   408 203 HOH   HOH A . 
C 3 HOH   9   409 99  HOH   HOH A . 
C 3 HOH   10  410 165 HOH   HOH A . 
C 3 HOH   11  411 139 HOH   HOH A . 
C 3 HOH   12  412 145 HOH   HOH A . 
C 3 HOH   13  413 250 HOH   HOH A . 
C 3 HOH   14  414 73  HOH   HOH A . 
C 3 HOH   15  415 212 HOH   HOH A . 
C 3 HOH   16  416 42  HOH   HOH A . 
C 3 HOH   17  417 25  HOH   HOH A . 
C 3 HOH   18  418 59  HOH   HOH A . 
C 3 HOH   19  419 115 HOH   HOH A . 
C 3 HOH   20  420 31  HOH   HOH A . 
C 3 HOH   21  421 183 HOH   HOH A . 
C 3 HOH   22  422 257 HOH   HOH A . 
C 3 HOH   23  423 74  HOH   HOH A . 
C 3 HOH   24  424 40  HOH   HOH A . 
C 3 HOH   25  425 231 HOH   HOH A . 
C 3 HOH   26  426 21  HOH   HOH A . 
C 3 HOH   27  427 61  HOH   HOH A . 
C 3 HOH   28  428 148 HOH   HOH A . 
C 3 HOH   29  429 57  HOH   HOH A . 
C 3 HOH   30  430 80  HOH   HOH A . 
C 3 HOH   31  431 153 HOH   HOH A . 
C 3 HOH   32  432 134 HOH   HOH A . 
C 3 HOH   33  433 50  HOH   HOH A . 
C 3 HOH   34  434 191 HOH   HOH A . 
C 3 HOH   35  435 65  HOH   HOH A . 
C 3 HOH   36  436 72  HOH   HOH A . 
C 3 HOH   37  437 4   HOH   HOH A . 
C 3 HOH   38  438 93  HOH   HOH A . 
C 3 HOH   39  439 10  HOH   HOH A . 
C 3 HOH   40  440 78  HOH   HOH A . 
C 3 HOH   41  441 207 HOH   HOH A . 
C 3 HOH   42  442 7   HOH   HOH A . 
C 3 HOH   43  443 81  HOH   HOH A . 
C 3 HOH   44  444 124 HOH   HOH A . 
C 3 HOH   45  445 35  HOH   HOH A . 
C 3 HOH   46  446 30  HOH   HOH A . 
C 3 HOH   47  447 48  HOH   HOH A . 
C 3 HOH   48  448 15  HOH   HOH A . 
C 3 HOH   49  449 132 HOH   HOH A . 
C 3 HOH   50  450 13  HOH   HOH A . 
C 3 HOH   51  451 92  HOH   HOH A . 
C 3 HOH   52  452 83  HOH   HOH A . 
C 3 HOH   53  453 146 HOH   HOH A . 
C 3 HOH   54  454 141 HOH   HOH A . 
C 3 HOH   55  455 14  HOH   HOH A . 
C 3 HOH   56  456 140 HOH   HOH A . 
C 3 HOH   57  457 79  HOH   HOH A . 
C 3 HOH   58  458 225 HOH   HOH A . 
C 3 HOH   59  459 19  HOH   HOH A . 
C 3 HOH   60  460 102 HOH   HOH A . 
C 3 HOH   61  461 112 HOH   HOH A . 
C 3 HOH   62  462 64  HOH   HOH A . 
C 3 HOH   63  463 41  HOH   HOH A . 
C 3 HOH   64  464 11  HOH   HOH A . 
C 3 HOH   65  465 2   HOH   HOH A . 
C 3 HOH   66  466 116 HOH   HOH A . 
C 3 HOH   67  467 194 HOH   HOH A . 
C 3 HOH   68  468 5   HOH   HOH A . 
C 3 HOH   69  469 23  HOH   HOH A . 
C 3 HOH   70  470 26  HOH   HOH A . 
C 3 HOH   71  471 66  HOH   HOH A . 
C 3 HOH   72  472 55  HOH   HOH A . 
C 3 HOH   73  473 118 HOH   HOH A . 
C 3 HOH   74  474 3   HOH   HOH A . 
C 3 HOH   75  475 53  HOH   HOH A . 
C 3 HOH   76  476 91  HOH   HOH A . 
C 3 HOH   77  477 258 HOH   HOH A . 
C 3 HOH   78  478 97  HOH   HOH A . 
C 3 HOH   79  479 32  HOH   HOH A . 
C 3 HOH   80  480 68  HOH   HOH A . 
C 3 HOH   81  481 180 HOH   HOH A . 
C 3 HOH   82  482 111 HOH   HOH A . 
C 3 HOH   83  483 36  HOH   HOH A . 
C 3 HOH   84  484 236 HOH   HOH A . 
C 3 HOH   85  485 117 HOH   HOH A . 
C 3 HOH   86  486 147 HOH   HOH A . 
C 3 HOH   87  487 33  HOH   HOH A . 
C 3 HOH   88  488 12  HOH   HOH A . 
C 3 HOH   89  489 220 HOH   HOH A . 
C 3 HOH   90  490 46  HOH   HOH A . 
C 3 HOH   91  491 52  HOH   HOH A . 
C 3 HOH   92  492 87  HOH   HOH A . 
C 3 HOH   93  493 108 HOH   HOH A . 
C 3 HOH   94  494 201 HOH   HOH A . 
C 3 HOH   95  495 135 HOH   HOH A . 
C 3 HOH   96  496 8   HOH   HOH A . 
C 3 HOH   97  497 221 HOH   HOH A . 
C 3 HOH   98  498 67  HOH   HOH A . 
C 3 HOH   99  499 235 HOH   HOH A . 
C 3 HOH   100 500 20  HOH   HOH A . 
C 3 HOH   101 501 71  HOH   HOH A . 
C 3 HOH   102 502 256 HOH   HOH A . 
C 3 HOH   103 503 133 HOH   HOH A . 
C 3 HOH   104 504 109 HOH   HOH A . 
C 3 HOH   105 505 127 HOH   HOH A . 
C 3 HOH   106 506 224 HOH   HOH A . 
C 3 HOH   107 507 159 HOH   HOH A . 
C 3 HOH   108 508 88  HOH   HOH A . 
C 3 HOH   109 509 160 HOH   HOH A . 
C 3 HOH   110 510 24  HOH   HOH A . 
C 3 HOH   111 511 110 HOH   HOH A . 
C 3 HOH   112 512 167 HOH   HOH A . 
C 3 HOH   113 513 123 HOH   HOH A . 
C 3 HOH   114 514 70  HOH   HOH A . 
C 3 HOH   115 515 28  HOH   HOH A . 
C 3 HOH   116 516 38  HOH   HOH A . 
C 3 HOH   117 517 22  HOH   HOH A . 
C 3 HOH   118 518 63  HOH   HOH A . 
C 3 HOH   119 519 6   HOH   HOH A . 
C 3 HOH   120 520 18  HOH   HOH A . 
C 3 HOH   121 521 210 HOH   HOH A . 
C 3 HOH   122 522 253 HOH   HOH A . 
C 3 HOH   123 523 219 HOH   HOH A . 
C 3 HOH   124 524 45  HOH   HOH A . 
C 3 HOH   125 525 76  HOH   HOH A . 
C 3 HOH   126 526 185 HOH   HOH A . 
C 3 HOH   127 527 244 HOH   HOH A . 
C 3 HOH   128 528 162 HOH   HOH A . 
C 3 HOH   129 529 177 HOH   HOH A . 
C 3 HOH   130 530 142 HOH   HOH A . 
C 3 HOH   131 531 101 HOH   HOH A . 
C 3 HOH   132 532 75  HOH   HOH A . 
C 3 HOH   133 533 264 HOH   HOH A . 
C 3 HOH   134 534 16  HOH   HOH A . 
C 3 HOH   135 535 184 HOH   HOH A . 
C 3 HOH   136 536 178 HOH   HOH A . 
C 3 HOH   137 537 168 HOH   HOH A . 
C 3 HOH   138 538 62  HOH   HOH A . 
C 3 HOH   139 539 181 HOH   HOH A . 
C 3 HOH   140 540 1   HOH   HOH A . 
C 3 HOH   141 541 161 HOH   HOH A . 
C 3 HOH   142 542 234 HOH   HOH A . 
C 3 HOH   143 543 104 HOH   HOH A . 
C 3 HOH   144 544 154 HOH   HOH A . 
C 3 HOH   145 545 227 HOH   HOH A . 
C 3 HOH   146 546 268 HOH   HOH A . 
C 3 HOH   147 547 151 HOH   HOH A . 
C 3 HOH   148 548 86  HOH   HOH A . 
C 3 HOH   149 549 44  HOH   HOH A . 
C 3 HOH   150 550 47  HOH   HOH A . 
C 3 HOH   151 551 29  HOH   HOH A . 
C 3 HOH   152 552 43  HOH   HOH A . 
C 3 HOH   153 553 107 HOH   HOH A . 
C 3 HOH   154 554 9   HOH   HOH A . 
C 3 HOH   155 555 170 HOH   HOH A . 
C 3 HOH   156 556 89  HOH   HOH A . 
C 3 HOH   157 557 121 HOH   HOH A . 
C 3 HOH   158 558 158 HOH   HOH A . 
C 3 HOH   159 559 34  HOH   HOH A . 
C 3 HOH   160 560 130 HOH   HOH A . 
C 3 HOH   161 561 54  HOH   HOH A . 
C 3 HOH   162 562 251 HOH   HOH A . 
C 3 HOH   163 563 204 HOH   HOH A . 
C 3 HOH   164 564 171 HOH   HOH A . 
C 3 HOH   165 565 122 HOH   HOH A . 
C 3 HOH   166 566 136 HOH   HOH A . 
C 3 HOH   167 567 103 HOH   HOH A . 
C 3 HOH   168 568 241 HOH   HOH A . 
C 3 HOH   169 569 238 HOH   HOH A . 
C 3 HOH   170 570 119 HOH   HOH A . 
C 3 HOH   171 571 17  HOH   HOH A . 
C 3 HOH   172 572 94  HOH   HOH A . 
C 3 HOH   173 573 226 HOH   HOH A . 
C 3 HOH   174 574 166 HOH   HOH A . 
C 3 HOH   175 575 49  HOH   HOH A . 
C 3 HOH   176 576 211 HOH   HOH A . 
C 3 HOH   177 577 105 HOH   HOH A . 
C 3 HOH   178 578 265 HOH   HOH A . 
C 3 HOH   179 579 216 HOH   HOH A . 
C 3 HOH   180 580 120 HOH   HOH A . 
C 3 HOH   181 581 90  HOH   HOH A . 
C 3 HOH   182 582 27  HOH   HOH A . 
C 3 HOH   183 583 198 HOH   HOH A . 
C 3 HOH   184 584 125 HOH   HOH A . 
C 3 HOH   185 585 172 HOH   HOH A . 
C 3 HOH   186 586 215 HOH   HOH A . 
C 3 HOH   187 587 263 HOH   HOH A . 
C 3 HOH   188 588 164 HOH   HOH A . 
C 3 HOH   189 589 245 HOH   HOH A . 
C 3 HOH   190 590 209 HOH   HOH A . 
C 3 HOH   191 591 77  HOH   HOH A . 
C 3 HOH   192 592 247 HOH   HOH A . 
C 3 HOH   193 593 173 HOH   HOH A . 
C 3 HOH   194 594 196 HOH   HOH A . 
C 3 HOH   195 595 239 HOH   HOH A . 
C 3 HOH   196 596 51  HOH   HOH A . 
C 3 HOH   197 597 128 HOH   HOH A . 
C 3 HOH   198 598 260 HOH   HOH A . 
C 3 HOH   199 599 246 HOH   HOH A . 
C 3 HOH   200 600 232 HOH   HOH A . 
C 3 HOH   201 601 199 HOH   HOH A . 
C 3 HOH   202 602 175 HOH   HOH A . 
C 3 HOH   203 603 228 HOH   HOH A . 
C 3 HOH   204 604 95  HOH   HOH A . 
C 3 HOH   205 605 174 HOH   HOH A . 
C 3 HOH   206 606 56  HOH   HOH A . 
C 3 HOH   207 607 69  HOH   HOH A . 
C 3 HOH   208 608 195 HOH   HOH A . 
C 3 HOH   209 609 176 HOH   HOH A . 
C 3 HOH   210 610 193 HOH   HOH A . 
C 3 HOH   211 611 222 HOH   HOH A . 
C 3 HOH   212 612 163 HOH   HOH A . 
C 3 HOH   213 613 249 HOH   HOH A . 
C 3 HOH   214 614 217 HOH   HOH A . 
C 3 HOH   215 615 189 HOH   HOH A . 
C 3 HOH   216 616 96  HOH   HOH A . 
C 3 HOH   217 617 205 HOH   HOH A . 
C 3 HOH   218 618 155 HOH   HOH A . 
C 3 HOH   219 619 186 HOH   HOH A . 
C 3 HOH   220 620 218 HOH   HOH A . 
C 3 HOH   221 621 37  HOH   HOH A . 
C 3 HOH   222 622 60  HOH   HOH A . 
C 3 HOH   223 623 223 HOH   HOH A . 
C 3 HOH   224 624 187 HOH   HOH A . 
C 3 HOH   225 625 190 HOH   HOH A . 
C 3 HOH   226 626 182 HOH   HOH A . 
C 3 HOH   227 627 267 HOH   HOH A . 
C 3 HOH   228 628 248 HOH   HOH A . 
C 3 HOH   229 629 254 HOH   HOH A . 
C 3 HOH   230 630 156 HOH   HOH A . 
C 3 HOH   231 631 58  HOH   HOH A . 
C 3 HOH   232 632 252 HOH   HOH A . 
C 3 HOH   233 633 144 HOH   HOH A . 
C 3 HOH   234 634 137 HOH   HOH A . 
C 3 HOH   235 635 266 HOH   HOH A . 
C 3 HOH   236 636 188 HOH   HOH A . 
C 3 HOH   237 637 255 HOH   HOH A . 
C 3 HOH   238 638 126 HOH   HOH A . 
C 3 HOH   239 639 113 HOH   HOH A . 
C 3 HOH   240 640 240 HOH   HOH A . 
C 3 HOH   241 641 157 HOH   HOH A . 
C 3 HOH   242 642 149 HOH   HOH A . 
C 3 HOH   243 643 230 HOH   HOH A . 
C 3 HOH   244 644 214 HOH   HOH A . 
C 3 HOH   245 645 237 HOH   HOH A . 
C 3 HOH   246 646 84  HOH   HOH A . 
C 3 HOH   247 647 39  HOH   HOH A . 
C 3 HOH   248 648 169 HOH   HOH A . 
C 3 HOH   249 649 131 HOH   HOH A . 
C 3 HOH   250 650 114 HOH   HOH A . 
C 3 HOH   251 651 233 HOH   HOH A . 
C 3 HOH   252 652 229 HOH   HOH A . 
C 3 HOH   253 653 197 HOH   HOH A . 
C 3 HOH   254 654 259 HOH   HOH A . 
C 3 HOH   255 655 100 HOH   HOH A . 
C 3 HOH   256 656 192 HOH   HOH A . 
C 3 HOH   257 657 179 HOH   HOH A . 
C 3 HOH   258 658 213 HOH   HOH A . 
C 3 HOH   259 659 202 HOH   HOH A . 
C 3 HOH   260 660 98  HOH   HOH A . 
C 3 HOH   261 661 200 HOH   HOH A . 
C 3 HOH   262 662 152 HOH   HOH A . 
C 3 HOH   263 663 82  HOH   HOH A . 
C 3 HOH   264 664 242 HOH   HOH A . 
C 3 HOH   265 665 243 HOH   HOH A . 
C 3 HOH   266 666 262 HOH   HOH A . 
C 3 HOH   267 667 138 HOH   HOH A . 
C 3 HOH   268 668 208 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             587361.098 
_cell.length_a           65.582 
_cell.length_b           89.547 
_cell.length_c           100.016 
_cell.angle_beta         90.000 
_cell.angle_gamma        90.000 
_cell.angle_alpha        90.000 
_cell.entry_id           7HAZ 
_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                         7HAZ 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
# 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
_exptl.entry_id          7HAZ 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_Matthews      2.88 
_exptl_crystal.density_percent_sol   57.23 
_exptl_crystal.density_meas          ? 
_exptl_crystal.description           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.pH              8.5 
_exptl_crystal_grow.temp            277 
_exptl_crystal_grow.pdbx_details    '100mM Tris-HCl pH 8.5, 22% PEG4000, 200mM MgCl2' 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_diffrn.id                     1 
_diffrn.crystal_id             1 
_diffrn.ambient_temp           100 
_diffrn.ambient_temp_details   ? 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               PIXEL 
_diffrn_detector.type                   'DECTRIS EIGER X 16M' 
_diffrn_detector.pdbx_collection_date   2024-01-21 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.pdbx_scattering_type             x-ray 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.monochromator                    Si111 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.97918 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.pdbx_synchrotron_beamline   BL10U2 
_diffrn_source.type                        'SSRF BEAMLINE BL10U2' 
_diffrn_source.pdbx_wavelength_list        0.97918 
_diffrn_source.pdbx_synchrotron_site       SSRF 
_diffrn_source.pdbx_wavelength             ? 
# 
_reflns.entry_id                     7HAZ 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             66.710 
_reflns.d_resolution_high            1.680 
_reflns.number_obs                   32490 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         95.000 
_reflns.pdbx_Rmerge_I_obs            0.110 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        12.600 
_reflns.B_iso_Wilson_estimate        ? 
_reflns.pdbx_redundancy              12.500 
_reflns.pdbx_Rrim_I_all              0.116 
_reflns.pdbx_Rpim_I_all              0.033 
_reflns.pdbx_CC_half                 0.989 
_reflns.pdbx_netI_over_av_sigmaI     ? 
_reflns.pdbx_number_measured_all     405622 
_reflns.pdbx_scaling_rejects         1866 
_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 1.680 1.770  ? 50863 4704 ? 2.599 ? ? ? 10.800 ? 1.200  ? ? ? ? ? ? 95.400 2.732 0.822 0.397 
1 2 5.300 66.710 ? 13749 1183 ? 0.047 ? ? ? 11.600 ? 33.100 ? ? ? ? ? ? 99.900 0.050 0.015 0.998 
# 
_refine.entry_id                                 7HAZ 
_refine.pdbx_method_to_determine_struct          'FOURIER SYNTHESIS' 
_refine.ls_percent_reflns_R_free                 4.94 
_refine.pdbx_overall_phase_error                 21.3752 
_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                          0.1786 
_refine.B_iso_mean                               33.61 
_refine.ls_number_reflns_R_free                  1592 
_refine.ls_percent_reflns_obs                    94.37 
_refine.ls_R_factor_R_work                       0.1769 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_refine.ls_d_res_high                            1.68 
_refine.ls_number_reflns_obs                     32249 
_refine.pdbx_ls_sigma_F                          1.33 
_refine.ls_number_reflns_R_work                  30657 
_refine.ls_d_res_low                             27.42 
_refine.pdbx_stereochemistry_target_values       'GeoStd + Monomer Library + CDL v1.2' 
_refine.ls_R_factor_R_free                       0.2108 
_refine.overall_SU_ML                            0.1986 
_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         15 
_refine_hist.number_atoms_solvent             268 
_refine_hist.number_atoms_total               1927 
_refine_hist.d_res_high                       1.68 
_refine_hist.d_res_low                        27.42 
# 
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           1686 0.0035 ? ? ? 
'X-RAY DIFFRACTION' f_angle_d          2271 0.7097 ? ? ? 
'X-RAY DIFFRACTION' f_chiral_restr     259  0.0471 ? ? ? 
'X-RAY DIFFRACTION' f_plane_restr      289  0.0044 ? ? ? 
'X-RAY DIFFRACTION' f_dihedral_angle_d 225  8.0672 ? ? ? 
# 
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' 1.68 1.73  2605 0.2881 88.50  0.3159 126 . . . . . 
'X-RAY DIFFRACTION' 1.73 1.79  2899 0.2884 99.77  0.3258 145 . . . . . 
'X-RAY DIFFRACTION' 1.79 1.86  2925 0.2404 99.97  0.2744 158 . . . . . 
'X-RAY DIFFRACTION' 1.86 1.95  2197 0.2565 76.16  0.2931 132 . . . . . 
'X-RAY DIFFRACTION' 1.95 2.05  2915 0.1894 99.93  0.2019 152 . . . . . 
'X-RAY DIFFRACTION' 2.05 2.18  2735 0.1885 93.07  0.2193 141 . . . . . 
'X-RAY DIFFRACTION' 2.18 2.35  2749 0.1837 93.52  0.2124 152 . . . . . 
'X-RAY DIFFRACTION' 2.35 2.58  2965 0.1809 100.00 0.2330 139 . . . . . 
'X-RAY DIFFRACTION' 2.58 2.96  2791 0.1796 95.13  0.2491 159 . . . . . 
'X-RAY DIFFRACTION' 2.96 3.72  2854 0.1601 94.28  0.1982 131 . . . . . 
'X-RAY DIFFRACTION' 3.73 27.42 3022 0.1481 97.46  0.1647 157 . . . . . 
# 
_struct.entry_id                  7HAZ 
_struct.title                     'PanDDA analysis group deposition -- Crystal structure of HSP90N in complex with Fr12919' 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_details        ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HAZ 
_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              7HAZ 
_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 7HAZ MET A 1   ? UNP P07900 ? ? 'initiating methionine' 8   1 
1 7HAZ LEU A 230 ? UNP P07900 ? ? 'expression tag'        237 2 
1 7HAZ GLU A 231 ? UNP P07900 ? ? 'expression tag'        238 3 
1 7HAZ HIS A 232 ? UNP P07900 ? ? 'expression tag'        239 4 
1 7HAZ HIS A 233 ? UNP P07900 ? ? 'expression tag'        240 5 
1 7HAZ HIS A 234 ? UNP P07900 ? ? 'expression tag'        241 6 
1 7HAZ HIS A 235 ? UNP P07900 ? ? 'expression tag'        242 7 
1 7HAZ HIS A 236 ? UNP P07900 ? ? 'expression tag'        243 8 
1 7HAZ HIS A 237 ? UNP P07900 ? ? 'expression tag'        244 9 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 GLN A 16  ? THR A 29  ? GLN A 23  THR A 36  1 ? 14 
HELX_P HELX_P2  AA2 GLU A 35  ? ASP A 59  ? GLU A 42  ASP A 66  1 ? 25 
HELX_P HELX_P3  AA3 PRO A 60  ? ASP A 64  ? PRO A 67  ASP A 71  5 ? 5  
HELX_P HELX_P4  AA4 THR A 92  ? ASN A 98  ? THR A 99  ASN A 105 1 ? 7  
HELX_P HELX_P5  AA5 ASN A 99  ? THR A 102 ? ASN A 106 THR A 109 5 ? 4  
HELX_P HELX_P6  AA6 ILE A 103 ? GLN A 116 ? ILE A 110 GLN A 123 1 ? 14 
HELX_P HELX_P7  AA7 ASP A 120 ? GLY A 128 ? ASP A 127 GLY A 135 5 ? 9  
HELX_P HELX_P8  AA8 VAL A 129 ? LEU A 136 ? VAL A 136 LEU A 143 5 ? 8  
HELX_P HELX_P9  AA9 GLN A 187 ? LEU A 191 ? GLN A 194 LEU A 198 5 ? 5  
HELX_P HELX_P10 AB1 GLU A 192 ? SER A 204 ? GLU A 199 SER A 211 1 ? 13 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
_struct_sheet.id               AA1 
_struct_sheet.type             ? 
_struct_sheet.number_strands   8 
_struct_sheet.details          ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA1 5 6 ? anti-parallel 
AA1 6 7 ? anti-parallel 
AA1 7 8 ? parallel      
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 GLU A 11  ? ALA A 14  ? GLU A 18  ALA A 21  
AA1 2 SER A 162 ? THR A 167 ? SER A 169 THR A 174 
AA1 3 TYR A 153 ? SER A 157 ? TYR A 160 SER A 164 
AA1 4 ALA A 138 ? LYS A 146 ? ALA A 145 LYS A 153 
AA1 5 GLY A 176 ? LEU A 183 ? GLY A 183 LEU A 190 
AA1 6 THR A 81  ? ASP A 86  ? THR A 88  ASP A 93  
AA1 7 ILE A 71  ? ASN A 76  ? ILE A 78  ASN A 83  
AA1 8 ILE A 211 ? LEU A 213 ? ILE A 218 LEU A 220 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N PHE A 13  ? N PHE A 20  O PHE A 163 ? O PHE A 170 
AA1 2 3 O ARG A 166 ? O ARG A 173 N ALA A 154 ? N ALA A 161 
AA1 3 4 O TRP A 155 ? O TRP A 162 N VAL A 143 ? N VAL A 150 
AA1 4 5 N THR A 142 ? N THR A 149 O ILE A 180 ? O ILE A 187 
AA1 5 6 O LEU A 181 ? O LEU A 188 N LEU A 82  ? N LEU A 89  
AA1 6 7 O VAL A 85  ? O VAL A 92  N ASN A 72  ? N ASN A 79  
AA1 7 8 N LEU A 73  ? N LEU A 80  O THR A 212 ? O THR A 219 
# 
_pdbx_entry_details.entry_id                   7HAZ 
_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 591 ? ? O A HOH 634 ? ? 1.90 
2 1 O   A HOH 595 ? ? O A HOH 629 ? ? 1.90 
3 1 O   A HOH 481 ? ? O A HOH 611 ? ? 1.93 
4 1 OE1 A GLU 178 ? ? O A HOH 401 ? ? 1.97 
5 1 OE1 A GLU 199 ? ? O A HOH 402 ? ? 2.02 
6 1 O   A HOH 563 ? ? O A HOH 614 ? ? 2.05 
7 1 O   A HOH 454 ? ? O A HOH 543 ? ? 2.12 
8 1 O   A HOH 484 ? ? O A HOH 637 ? ? 2.16 
# 
_pdbx_validate_symm_contact.id                1 
_pdbx_validate_symm_contact.PDB_model_num     1 
_pdbx_validate_symm_contact.auth_atom_id_1    O 
_pdbx_validate_symm_contact.auth_asym_id_1    A 
_pdbx_validate_symm_contact.auth_comp_id_1    HOH 
_pdbx_validate_symm_contact.auth_seq_id_1     467 
_pdbx_validate_symm_contact.PDB_ins_code_1    ? 
_pdbx_validate_symm_contact.label_alt_id_1    ? 
_pdbx_validate_symm_contact.site_symmetry_1   1_555 
_pdbx_validate_symm_contact.auth_atom_id_2    O 
_pdbx_validate_symm_contact.auth_asym_id_2    A 
_pdbx_validate_symm_contact.auth_comp_id_2    HOH 
_pdbx_validate_symm_contact.auth_seq_id_2     558 
_pdbx_validate_symm_contact.PDB_ins_code_2    ? 
_pdbx_validate_symm_contact.label_alt_id_2    ? 
_pdbx_validate_symm_contact.site_symmetry_2   8_544 
_pdbx_validate_symm_contact.dist              2.01 
# 
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 THR A 94  ? ? -105.81 40.02   
2 1 ALA A 166 ? ? 65.27   -144.86 
3 1 ARG A 182 ? ? -172.43 134.49  
# 
_pdbx_struct_special_symmetry.id              1 
_pdbx_struct_special_symmetry.PDB_model_num   1 
_pdbx_struct_special_symmetry.auth_asym_id    A 
_pdbx_struct_special_symmetry.auth_comp_id    HOH 
_pdbx_struct_special_symmetry.auth_seq_id     647 
_pdbx_struct_special_symmetry.PDB_ins_code    ? 
_pdbx_struct_special_symmetry.label_asym_id   C 
_pdbx_struct_special_symmetry.label_comp_id   HOH 
_pdbx_struct_special_symmetry.label_seq_id    . 
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z               
2 x,-y,-z             
3 -x,y,-z             
4 -x,-y,z             
5 x+1/2,y+1/2,z+1/2   
6 x+1/2,-y+1/2,-z+1/2 
7 -x+1/2,y+1/2,-z+1/2 
8 -x+1/2,-y+1/2,z+1/2 
# 
loop_
_pdbx_refine_tls.id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][3] 
1 ? 'X-RAY DIFFRACTION' refined 12.2583876996  -17.8410422109 -18.8340068809 0.160827477388 0.210940469241 0.198567619258 
-0.00342705139492 -0.0333004139001 -0.0199967232304 3.30866027863 1.78604347689 5.29303142747 -1.22594308845  -3.75520326004   
0.998835412668  0.147765877464  -0.401627711255 0.0184988178631  0.0448793535162 -0.0311952730553 -0.106688177685  
-0.0289269141259 0.275613977993   -0.0788894068602 
2 ? 'X-RAY DIFFRACTION' refined -5.24603277756 -6.12281801842 -20.9559912455 0.210893279703 0.165042123908 0.231834193489 
-0.00863000543748 0.00454757604663 -0.030958240063  2.9042348633  4.8753897671  9.31236360203 -2.07218883047  3.47398224559    
-4.90944858372  -0.11516717516  0.154177606415  0.216031674404   0.161699890726  -0.10633114159   0.0198403073521  -0.620667148108 
0.329530781382   0.21245031244    
3 ? 'X-RAY DIFFRACTION' refined -10.2081956766 -14.8768403945 -25.1243761173 0.178099801633 0.184008289199 0.230580253442 
0.00307732317097  -0.0404895297092 -0.0349822829531 2.29079394018 2.59932841229 3.5580899314  -0.228088625668 -0.0471247097031 
-0.747462267183 0.0495647150227 0.115087792571  -0.0752684080996 -0.138945806116 0.0390294545931  0.240292693113   0.0477826049539 
-0.222746920107  -0.113623569174  
4 ? 'X-RAY DIFFRACTION' refined 10.645113507   -7.31708806927 -18.1222226883 0.222559281351 0.274203621204 0.318854016995 
-0.0417248289776  0.0201496353039  -0.0662751839856 3.75668806445 2.95875772465 5.46839951559 0.411611456138  -1.35954453541   
1.31256901511   0.207108446997  -0.53247859975  0.532126500362   0.0445914718596 -0.0491715476704 -0.156321460693  -0.568158489757 
0.658642791202   -0.0526139416068 
5 ? 'X-RAY DIFFRACTION' refined 0.727136772687 -19.3083559135 -27.8668973347 0.211075126177 0.18863167994  0.219375297123 
0.00412356378836  -0.013130167474  -0.0320734566071 3.51670173726 1.92815549733 2.35333056167 -1.01069035504  0.347506466799   
-0.336147528981 0.179446412201  0.311277392849  -0.271904944468  -0.245421072744 -0.0604448856473 0.150663836063   0.202922887847 
-0.0218700128693 -0.130425586098  
6 ? 'X-RAY DIFFRACTION' refined -2.67152918581 -23.5026158901 -13.6260777864 0.198960194939 0.183865574152 0.234190136899 
-0.00669317907388 -0.0155299053249 0.0163885139617  3.20005702083 3.84529499545 6.22952233865 -0.41107276763  -0.814490179467  
-1.53978999783  0.0150412378131 -0.278942538489 -0.329759430511  0.207563229101  -0.03118639378   -0.0217015321421 0.369029218066 
0.252358404415   -0.0367013015113 
7 ? 'X-RAY DIFFRACTION' refined -12.1379698796 -13.9607505478 -10.3224887585 0.175522938255 0.247376730613 0.186343138186 
0.00138251488254  0.019423477923   -0.0192388176534 3.71767613092 2.45289522508 5.17134773992 -1.13185362532  0.722774133638   
-1.18636449831  0.0247729595692 -0.43163194203  -0.0509522468998 0.236993848293  0.0594801877534  0.0633806210724  -0.137552972777 
-0.1957976471    -0.0711865800297 
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
1 1 'X-RAY DIFFRACTION' A 16  A 1   A 40  A 25  . 
;chain 'A' and (resid 16 through 40 )
;
2 2 'X-RAY DIFFRACTION' A 41  A 26  A 65  A 50  . 
;chain 'A' and (resid 41 through 65 )
;
3 3 'X-RAY DIFFRACTION' A 66  A 51  A 99  A 84  . 
;chain 'A' and (resid 66 through 99 )
;
4 4 'X-RAY DIFFRACTION' A 100 A 85  A 136 A 121 . 
;chain 'A' and (resid 100 through 136 )
;
5 5 'X-RAY DIFFRACTION' A 137 A 122 A 182 A 167 . 
;chain 'A' and (resid 137 through 182 )
;
6 6 'X-RAY DIFFRACTION' A 183 A 168 A 199 A 184 . 
;chain 'A' and (resid 183 through 199 )
;
7 7 'X-RAY DIFFRACTION' A 200 A 185 A 224 A 209 . 
;chain 'A' and (resid 200 through 224 )
;
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A MET 8   ? A MET 1   
2  1 Y 1 A ASP 9   ? A ASP 2   
3  1 Y 1 A GLN 10  ? A GLN 3   
4  1 Y 1 A PRO 11  ? A PRO 4   
5  1 Y 1 A MET 12  ? A MET 5   
6  1 Y 1 A GLU 13  ? A GLU 6   
7  1 Y 1 A GLU 14  ? A GLU 7   
8  1 Y 1 A GLU 15  ? A GLU 8   
9  1 Y 1 A GLU 225 ? A GLU 218 
10 1 Y 1 A ARG 226 ? A ARG 219 
11 1 Y 1 A ASP 227 ? A ASP 220 
12 1 Y 1 A LYS 228 ? A LYS 221 
13 1 Y 1 A GLU 229 ? A GLU 222 
14 1 Y 1 A VAL 230 ? A VAL 223 
15 1 Y 1 A SER 231 ? A SER 224 
16 1 Y 1 A ASP 232 ? A ASP 225 
17 1 Y 1 A ASP 233 ? A ASP 226 
18 1 Y 1 A GLU 234 ? A GLU 227 
19 1 Y 1 A ALA 235 ? A ALA 228 
20 1 Y 1 A GLU 236 ? A GLU 229 
21 1 Y 1 A LEU 237 ? A LEU 230 
22 1 Y 1 A GLU 238 ? A GLU 231 
23 1 Y 1 A HIS 239 ? A HIS 232 
24 1 Y 1 A HIS 240 ? A HIS 233 
25 1 Y 1 A HIS 241 ? A HIS 234 
26 1 Y 1 A HIS 242 ? A HIS 235 
27 1 Y 1 A HIS 243 ? A HIS 236 
28 1 Y 1 A HIS 244 ? A HIS 237 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
A1AYI O2   O N N 1   
A1AYI O1   O N N 2   
A1AYI C1   C N N 3   
A1AYI C10  C Y N 4   
A1AYI C11  C Y N 5   
A1AYI C12  C Y N 6   
A1AYI C13  C Y N 7   
A1AYI C2   C Y N 8   
A1AYI C3   C Y N 9   
A1AYI C4   C Y N 10  
A1AYI C5   C Y N 11  
A1AYI C6   C Y N 12  
A1AYI C7   C Y N 13  
A1AYI C8   C Y N 14  
A1AYI C9   C Y N 15  
A1AYI HO1  H N N 16  
A1AYI H13  H N N 17  
A1AYI H12  H N N 18  
A1AYI H10  H N N 19  
A1AYI H11  H N N 20  
A1AYI H121 H N N 21  
A1AYI H131 H N N 22  
A1AYI H3   H N N 23  
A1AYI H4   H N N 24  
A1AYI H5   H N N 25  
A1AYI H6   H N N 26  
A1AYI H9   H N N 27  
ALA   N    N N N 28  
ALA   CA   C N S 29  
ALA   C    C N N 30  
ALA   O    O N N 31  
ALA   CB   C N N 32  
ALA   OXT  O N N 33  
ALA   H    H N N 34  
ALA   H2   H N N 35  
ALA   HA   H N N 36  
ALA   HB1  H N N 37  
ALA   HB2  H N N 38  
ALA   HB3  H N N 39  
ALA   HXT  H N N 40  
ARG   N    N N N 41  
ARG   CA   C N S 42  
ARG   C    C N N 43  
ARG   O    O N N 44  
ARG   CB   C N N 45  
ARG   CG   C N N 46  
ARG   CD   C N N 47  
ARG   NE   N N N 48  
ARG   CZ   C N N 49  
ARG   NH1  N N N 50  
ARG   NH2  N N N 51  
ARG   OXT  O N N 52  
ARG   H    H N N 53  
ARG   H2   H N N 54  
ARG   HA   H N N 55  
ARG   HB2  H N N 56  
ARG   HB3  H N N 57  
ARG   HG2  H N N 58  
ARG   HG3  H N N 59  
ARG   HD2  H N N 60  
ARG   HD3  H N N 61  
ARG   HE   H N N 62  
ARG   HH11 H N N 63  
ARG   HH12 H N N 64  
ARG   HH21 H N N 65  
ARG   HH22 H N N 66  
ARG   HXT  H N N 67  
ASN   N    N N N 68  
ASN   CA   C N S 69  
ASN   C    C N N 70  
ASN   O    O N N 71  
ASN   CB   C N N 72  
ASN   CG   C N N 73  
ASN   OD1  O N N 74  
ASN   ND2  N N N 75  
ASN   OXT  O N N 76  
ASN   H    H N N 77  
ASN   H2   H N N 78  
ASN   HA   H N N 79  
ASN   HB2  H N N 80  
ASN   HB3  H N N 81  
ASN   HD21 H N N 82  
ASN   HD22 H N N 83  
ASN   HXT  H N N 84  
ASP   N    N N N 85  
ASP   CA   C N S 86  
ASP   C    C N N 87  
ASP   O    O N N 88  
ASP   CB   C N N 89  
ASP   CG   C N N 90  
ASP   OD1  O N N 91  
ASP   OD2  O N N 92  
ASP   OXT  O N N 93  
ASP   H    H N N 94  
ASP   H2   H N N 95  
ASP   HA   H N N 96  
ASP   HB2  H N N 97  
ASP   HB3  H N N 98  
ASP   HD2  H N N 99  
ASP   HXT  H N N 100 
GLN   N    N N N 101 
GLN   CA   C N S 102 
GLN   C    C N N 103 
GLN   O    O N N 104 
GLN   CB   C N N 105 
GLN   CG   C N N 106 
GLN   CD   C N N 107 
GLN   OE1  O N N 108 
GLN   NE2  N N N 109 
GLN   OXT  O N N 110 
GLN   H    H N N 111 
GLN   H2   H N N 112 
GLN   HA   H N N 113 
GLN   HB2  H N N 114 
GLN   HB3  H N N 115 
GLN   HG2  H N N 116 
GLN   HG3  H N N 117 
GLN   HE21 H N N 118 
GLN   HE22 H N N 119 
GLN   HXT  H N N 120 
GLU   N    N N N 121 
GLU   CA   C N S 122 
GLU   C    C N N 123 
GLU   O    O N N 124 
GLU   CB   C N N 125 
GLU   CG   C N N 126 
GLU   CD   C N N 127 
GLU   OE1  O N N 128 
GLU   OE2  O N N 129 
GLU   OXT  O N N 130 
GLU   H    H N N 131 
GLU   H2   H N N 132 
GLU   HA   H N N 133 
GLU   HB2  H N N 134 
GLU   HB3  H N N 135 
GLU   HG2  H N N 136 
GLU   HG3  H N N 137 
GLU   HE2  H N N 138 
GLU   HXT  H N N 139 
GLY   N    N N N 140 
GLY   CA   C N N 141 
GLY   C    C N N 142 
GLY   O    O N N 143 
GLY   OXT  O N N 144 
GLY   H    H N N 145 
GLY   H2   H N N 146 
GLY   HA2  H N N 147 
GLY   HA3  H N N 148 
GLY   HXT  H N N 149 
HIS   N    N N N 150 
HIS   CA   C N S 151 
HIS   C    C N N 152 
HIS   O    O N N 153 
HIS   CB   C N N 154 
HIS   CG   C Y N 155 
HIS   ND1  N Y N 156 
HIS   CD2  C Y N 157 
HIS   CE1  C Y N 158 
HIS   NE2  N Y N 159 
HIS   OXT  O N N 160 
HIS   H    H N N 161 
HIS   H2   H N N 162 
HIS   HA   H N N 163 
HIS   HB2  H N N 164 
HIS   HB3  H N N 165 
HIS   HD1  H N N 166 
HIS   HD2  H N N 167 
HIS   HE1  H N N 168 
HIS   HE2  H N N 169 
HIS   HXT  H N N 170 
HOH   O    O N N 171 
HOH   H1   H N N 172 
HOH   H2   H N N 173 
ILE   N    N N N 174 
ILE   CA   C N S 175 
ILE   C    C N N 176 
ILE   O    O N N 177 
ILE   CB   C N S 178 
ILE   CG1  C N N 179 
ILE   CG2  C N N 180 
ILE   CD1  C N N 181 
ILE   OXT  O N N 182 
ILE   H    H N N 183 
ILE   H2   H N N 184 
ILE   HA   H N N 185 
ILE   HB   H N N 186 
ILE   HG12 H N N 187 
ILE   HG13 H N N 188 
ILE   HG21 H N N 189 
ILE   HG22 H N N 190 
ILE   HG23 H N N 191 
ILE   HD11 H N N 192 
ILE   HD12 H N N 193 
ILE   HD13 H N N 194 
ILE   HXT  H N N 195 
LEU   N    N N N 196 
LEU   CA   C N S 197 
LEU   C    C N N 198 
LEU   O    O N N 199 
LEU   CB   C N N 200 
LEU   CG   C N N 201 
LEU   CD1  C N N 202 
LEU   CD2  C N N 203 
LEU   OXT  O N N 204 
LEU   H    H N N 205 
LEU   H2   H N N 206 
LEU   HA   H N N 207 
LEU   HB2  H N N 208 
LEU   HB3  H N N 209 
LEU   HG   H N N 210 
LEU   HD11 H N N 211 
LEU   HD12 H N N 212 
LEU   HD13 H N N 213 
LEU   HD21 H N N 214 
LEU   HD22 H N N 215 
LEU   HD23 H N N 216 
LEU   HXT  H N N 217 
LYS   N    N N N 218 
LYS   CA   C N S 219 
LYS   C    C N N 220 
LYS   O    O N N 221 
LYS   CB   C N N 222 
LYS   CG   C N N 223 
LYS   CD   C N N 224 
LYS   CE   C N N 225 
LYS   NZ   N N N 226 
LYS   OXT  O N N 227 
LYS   H    H N N 228 
LYS   H2   H N N 229 
LYS   HA   H N N 230 
LYS   HB2  H N N 231 
LYS   HB3  H N N 232 
LYS   HG2  H N N 233 
LYS   HG3  H N N 234 
LYS   HD2  H N N 235 
LYS   HD3  H N N 236 
LYS   HE2  H N N 237 
LYS   HE3  H N N 238 
LYS   HZ1  H N N 239 
LYS   HZ2  H N N 240 
LYS   HZ3  H N N 241 
LYS   HXT  H N N 242 
MET   N    N N N 243 
MET   CA   C N S 244 
MET   C    C N N 245 
MET   O    O N N 246 
MET   CB   C N N 247 
MET   CG   C N N 248 
MET   SD   S N N 249 
MET   CE   C N N 250 
MET   OXT  O N N 251 
MET   H    H N N 252 
MET   H2   H N N 253 
MET   HA   H N N 254 
MET   HB2  H N N 255 
MET   HB3  H N N 256 
MET   HG2  H N N 257 
MET   HG3  H N N 258 
MET   HE1  H N N 259 
MET   HE2  H N N 260 
MET   HE3  H N N 261 
MET   HXT  H N N 262 
PHE   N    N N N 263 
PHE   CA   C N S 264 
PHE   C    C N N 265 
PHE   O    O N N 266 
PHE   CB   C N N 267 
PHE   CG   C Y N 268 
PHE   CD1  C Y N 269 
PHE   CD2  C Y N 270 
PHE   CE1  C Y N 271 
PHE   CE2  C Y N 272 
PHE   CZ   C Y N 273 
PHE   OXT  O N N 274 
PHE   H    H N N 275 
PHE   H2   H N N 276 
PHE   HA   H N N 277 
PHE   HB2  H N N 278 
PHE   HB3  H N N 279 
PHE   HD1  H N N 280 
PHE   HD2  H N N 281 
PHE   HE1  H N N 282 
PHE   HE2  H N N 283 
PHE   HZ   H N N 284 
PHE   HXT  H N N 285 
PRO   N    N N N 286 
PRO   CA   C N S 287 
PRO   C    C N N 288 
PRO   O    O N N 289 
PRO   CB   C N N 290 
PRO   CG   C N N 291 
PRO   CD   C N N 292 
PRO   OXT  O N N 293 
PRO   H    H N N 294 
PRO   HA   H N N 295 
PRO   HB2  H N N 296 
PRO   HB3  H N N 297 
PRO   HG2  H N N 298 
PRO   HG3  H N N 299 
PRO   HD2  H N N 300 
PRO   HD3  H N N 301 
PRO   HXT  H N N 302 
SER   N    N N N 303 
SER   CA   C N S 304 
SER   C    C N N 305 
SER   O    O N N 306 
SER   CB   C N N 307 
SER   OG   O N N 308 
SER   OXT  O N N 309 
SER   H    H N N 310 
SER   H2   H N N 311 
SER   HA   H N N 312 
SER   HB2  H N N 313 
SER   HB3  H N N 314 
SER   HG   H N N 315 
SER   HXT  H N N 316 
THR   N    N N N 317 
THR   CA   C N S 318 
THR   C    C N N 319 
THR   O    O N N 320 
THR   CB   C N R 321 
THR   OG1  O N N 322 
THR   CG2  C N N 323 
THR   OXT  O N N 324 
THR   H    H N N 325 
THR   H2   H N N 326 
THR   HA   H N N 327 
THR   HB   H N N 328 
THR   HG1  H N N 329 
THR   HG21 H N N 330 
THR   HG22 H N N 331 
THR   HG23 H N N 332 
THR   HXT  H N N 333 
TRP   N    N N N 334 
TRP   CA   C N S 335 
TRP   C    C N N 336 
TRP   O    O N N 337 
TRP   CB   C N N 338 
TRP   CG   C Y N 339 
TRP   CD1  C Y N 340 
TRP   CD2  C Y N 341 
TRP   NE1  N Y N 342 
TRP   CE2  C Y N 343 
TRP   CE3  C Y N 344 
TRP   CZ2  C Y N 345 
TRP   CZ3  C Y N 346 
TRP   CH2  C Y N 347 
TRP   OXT  O N N 348 
TRP   H    H N N 349 
TRP   H2   H N N 350 
TRP   HA   H N N 351 
TRP   HB2  H N N 352 
TRP   HB3  H N N 353 
TRP   HD1  H N N 354 
TRP   HE1  H N N 355 
TRP   HE3  H N N 356 
TRP   HZ2  H N N 357 
TRP   HZ3  H N N 358 
TRP   HH2  H N N 359 
TRP   HXT  H N N 360 
TYR   N    N N N 361 
TYR   CA   C N S 362 
TYR   C    C N N 363 
TYR   O    O N N 364 
TYR   CB   C N N 365 
TYR   CG   C Y N 366 
TYR   CD1  C Y N 367 
TYR   CD2  C Y N 368 
TYR   CE1  C Y N 369 
TYR   CE2  C Y N 370 
TYR   CZ   C Y N 371 
TYR   OH   O N N 372 
TYR   OXT  O N N 373 
TYR   H    H N N 374 
TYR   H2   H N N 375 
TYR   HA   H N N 376 
TYR   HB2  H N N 377 
TYR   HB3  H N N 378 
TYR   HD1  H N N 379 
TYR   HD2  H N N 380 
TYR   HE1  H N N 381 
TYR   HE2  H N N 382 
TYR   HH   H N N 383 
TYR   HXT  H N N 384 
VAL   N    N N N 385 
VAL   CA   C N S 386 
VAL   C    C N N 387 
VAL   O    O N N 388 
VAL   CB   C N N 389 
VAL   CG1  C N N 390 
VAL   CG2  C N N 391 
VAL   OXT  O N N 392 
VAL   H    H N N 393 
VAL   H2   H N N 394 
VAL   HA   H N N 395 
VAL   HB   H N N 396 
VAL   HG11 H N N 397 
VAL   HG12 H N N 398 
VAL   HG13 H N N 399 
VAL   HG21 H N N 400 
VAL   HG22 H N N 401 
VAL   HG23 H N N 402 
VAL   HXT  H N N 403 
# 
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 
A1AYI O1  C1   sing N N 1   
A1AYI C1  C2   sing N N 2   
A1AYI C2  C3   doub Y N 3   
A1AYI C2  C7   sing Y N 4   
A1AYI C3  C4   sing Y N 5   
A1AYI C4  C5   doub Y N 6   
A1AYI C5  C6   sing Y N 7   
A1AYI C6  C7   doub Y N 8   
A1AYI C7  O2   sing N N 9   
A1AYI O2  C8   sing N N 10  
A1AYI C8  C9   doub Y N 11  
A1AYI C8  C13  sing Y N 12  
A1AYI C9  C10  sing Y N 13  
A1AYI C10 C11  doub Y N 14  
A1AYI C11 C12  sing Y N 15  
A1AYI C12 C13  doub Y N 16  
A1AYI O1  HO1  sing N N 17  
A1AYI C1  H13  sing N N 18  
A1AYI C1  H12  sing N N 19  
A1AYI C10 H10  sing N N 20  
A1AYI C11 H11  sing N N 21  
A1AYI C12 H121 sing N N 22  
A1AYI C13 H131 sing N N 23  
A1AYI C3  H3   sing N N 24  
A1AYI C4  H4   sing N N 25  
A1AYI C5  H5   sing N N 26  
A1AYI C6  H6   sing N N 27  
A1AYI C9  H9   sing N N 28  
ALA   N   CA   sing N N 29  
ALA   N   H    sing N N 30  
ALA   N   H2   sing N N 31  
ALA   CA  C    sing N N 32  
ALA   CA  CB   sing N N 33  
ALA   CA  HA   sing N N 34  
ALA   C   O    doub N N 35  
ALA   C   OXT  sing N N 36  
ALA   CB  HB1  sing N N 37  
ALA   CB  HB2  sing N N 38  
ALA   CB  HB3  sing N N 39  
ALA   OXT HXT  sing N N 40  
ARG   N   CA   sing N N 41  
ARG   N   H    sing N N 42  
ARG   N   H2   sing N N 43  
ARG   CA  C    sing N N 44  
ARG   CA  CB   sing N N 45  
ARG   CA  HA   sing N N 46  
ARG   C   O    doub N N 47  
ARG   C   OXT  sing N N 48  
ARG   CB  CG   sing N N 49  
ARG   CB  HB2  sing N N 50  
ARG   CB  HB3  sing N N 51  
ARG   CG  CD   sing N N 52  
ARG   CG  HG2  sing N N 53  
ARG   CG  HG3  sing N N 54  
ARG   CD  NE   sing N N 55  
ARG   CD  HD2  sing N N 56  
ARG   CD  HD3  sing N N 57  
ARG   NE  CZ   sing N N 58  
ARG   NE  HE   sing N N 59  
ARG   CZ  NH1  sing N N 60  
ARG   CZ  NH2  doub N N 61  
ARG   NH1 HH11 sing N N 62  
ARG   NH1 HH12 sing N N 63  
ARG   NH2 HH21 sing N N 64  
ARG   NH2 HH22 sing N N 65  
ARG   OXT HXT  sing N N 66  
ASN   N   CA   sing N N 67  
ASN   N   H    sing N N 68  
ASN   N   H2   sing N N 69  
ASN   CA  C    sing N N 70  
ASN   CA  CB   sing N N 71  
ASN   CA  HA   sing N N 72  
ASN   C   O    doub N N 73  
ASN   C   OXT  sing N N 74  
ASN   CB  CG   sing N N 75  
ASN   CB  HB2  sing N N 76  
ASN   CB  HB3  sing N N 77  
ASN   CG  OD1  doub N N 78  
ASN   CG  ND2  sing N N 79  
ASN   ND2 HD21 sing N N 80  
ASN   ND2 HD22 sing N N 81  
ASN   OXT HXT  sing N N 82  
ASP   N   CA   sing N N 83  
ASP   N   H    sing N N 84  
ASP   N   H2   sing N N 85  
ASP   CA  C    sing N N 86  
ASP   CA  CB   sing N N 87  
ASP   CA  HA   sing N N 88  
ASP   C   O    doub N N 89  
ASP   C   OXT  sing N N 90  
ASP   CB  CG   sing N N 91  
ASP   CB  HB2  sing N N 92  
ASP   CB  HB3  sing N N 93  
ASP   CG  OD1  doub N N 94  
ASP   CG  OD2  sing N N 95  
ASP   OD2 HD2  sing N N 96  
ASP   OXT HXT  sing N N 97  
GLN   N   CA   sing N N 98  
GLN   N   H    sing N N 99  
GLN   N   H2   sing N N 100 
GLN   CA  C    sing N N 101 
GLN   CA  CB   sing N N 102 
GLN   CA  HA   sing N N 103 
GLN   C   O    doub N N 104 
GLN   C   OXT  sing N N 105 
GLN   CB  CG   sing N N 106 
GLN   CB  HB2  sing N N 107 
GLN   CB  HB3  sing N N 108 
GLN   CG  CD   sing N N 109 
GLN   CG  HG2  sing N N 110 
GLN   CG  HG3  sing N N 111 
GLN   CD  OE1  doub N N 112 
GLN   CD  NE2  sing N N 113 
GLN   NE2 HE21 sing N N 114 
GLN   NE2 HE22 sing N N 115 
GLN   OXT HXT  sing N N 116 
GLU   N   CA   sing N N 117 
GLU   N   H    sing N N 118 
GLU   N   H2   sing N N 119 
GLU   CA  C    sing N N 120 
GLU   CA  CB   sing N N 121 
GLU   CA  HA   sing N N 122 
GLU   C   O    doub N N 123 
GLU   C   OXT  sing N N 124 
GLU   CB  CG   sing N N 125 
GLU   CB  HB2  sing N N 126 
GLU   CB  HB3  sing N N 127 
GLU   CG  CD   sing N N 128 
GLU   CG  HG2  sing N N 129 
GLU   CG  HG3  sing N N 130 
GLU   CD  OE1  doub N N 131 
GLU   CD  OE2  sing N N 132 
GLU   OE2 HE2  sing N N 133 
GLU   OXT HXT  sing N N 134 
GLY   N   CA   sing N N 135 
GLY   N   H    sing N N 136 
GLY   N   H2   sing N N 137 
GLY   CA  C    sing N N 138 
GLY   CA  HA2  sing N N 139 
GLY   CA  HA3  sing N N 140 
GLY   C   O    doub N N 141 
GLY   C   OXT  sing N N 142 
GLY   OXT HXT  sing N N 143 
HIS   N   CA   sing N N 144 
HIS   N   H    sing N N 145 
HIS   N   H2   sing N N 146 
HIS   CA  C    sing N N 147 
HIS   CA  CB   sing N N 148 
HIS   CA  HA   sing N N 149 
HIS   C   O    doub N N 150 
HIS   C   OXT  sing N N 151 
HIS   CB  CG   sing N N 152 
HIS   CB  HB2  sing N N 153 
HIS   CB  HB3  sing N N 154 
HIS   CG  ND1  sing Y N 155 
HIS   CG  CD2  doub Y N 156 
HIS   ND1 CE1  doub Y N 157 
HIS   ND1 HD1  sing N N 158 
HIS   CD2 NE2  sing Y N 159 
HIS   CD2 HD2  sing N N 160 
HIS   CE1 NE2  sing Y N 161 
HIS   CE1 HE1  sing N N 162 
HIS   NE2 HE2  sing N N 163 
HIS   OXT HXT  sing N N 164 
HOH   O   H1   sing N N 165 
HOH   O   H2   sing N N 166 
ILE   N   CA   sing N N 167 
ILE   N   H    sing N N 168 
ILE   N   H2   sing N N 169 
ILE   CA  C    sing N N 170 
ILE   CA  CB   sing N N 171 
ILE   CA  HA   sing N N 172 
ILE   C   O    doub N N 173 
ILE   C   OXT  sing N N 174 
ILE   CB  CG1  sing N N 175 
ILE   CB  CG2  sing N N 176 
ILE   CB  HB   sing N N 177 
ILE   CG1 CD1  sing N N 178 
ILE   CG1 HG12 sing N N 179 
ILE   CG1 HG13 sing N N 180 
ILE   CG2 HG21 sing N N 181 
ILE   CG2 HG22 sing N N 182 
ILE   CG2 HG23 sing N N 183 
ILE   CD1 HD11 sing N N 184 
ILE   CD1 HD12 sing N N 185 
ILE   CD1 HD13 sing N N 186 
ILE   OXT HXT  sing N N 187 
LEU   N   CA   sing N N 188 
LEU   N   H    sing N N 189 
LEU   N   H2   sing N N 190 
LEU   CA  C    sing N N 191 
LEU   CA  CB   sing N N 192 
LEU   CA  HA   sing N N 193 
LEU   C   O    doub N N 194 
LEU   C   OXT  sing N N 195 
LEU   CB  CG   sing N N 196 
LEU   CB  HB2  sing N N 197 
LEU   CB  HB3  sing N N 198 
LEU   CG  CD1  sing N N 199 
LEU   CG  CD2  sing N N 200 
LEU   CG  HG   sing N N 201 
LEU   CD1 HD11 sing N N 202 
LEU   CD1 HD12 sing N N 203 
LEU   CD1 HD13 sing N N 204 
LEU   CD2 HD21 sing N N 205 
LEU   CD2 HD22 sing N N 206 
LEU   CD2 HD23 sing N N 207 
LEU   OXT HXT  sing N N 208 
LYS   N   CA   sing N N 209 
LYS   N   H    sing N N 210 
LYS   N   H2   sing N N 211 
LYS   CA  C    sing N N 212 
LYS   CA  CB   sing N N 213 
LYS   CA  HA   sing N N 214 
LYS   C   O    doub N N 215 
LYS   C   OXT  sing N N 216 
LYS   CB  CG   sing N N 217 
LYS   CB  HB2  sing N N 218 
LYS   CB  HB3  sing N N 219 
LYS   CG  CD   sing N N 220 
LYS   CG  HG2  sing N N 221 
LYS   CG  HG3  sing N N 222 
LYS   CD  CE   sing N N 223 
LYS   CD  HD2  sing N N 224 
LYS   CD  HD3  sing N N 225 
LYS   CE  NZ   sing N N 226 
LYS   CE  HE2  sing N N 227 
LYS   CE  HE3  sing N N 228 
LYS   NZ  HZ1  sing N N 229 
LYS   NZ  HZ2  sing N N 230 
LYS   NZ  HZ3  sing N N 231 
LYS   OXT HXT  sing N N 232 
MET   N   CA   sing N N 233 
MET   N   H    sing N N 234 
MET   N   H2   sing N N 235 
MET   CA  C    sing N N 236 
MET   CA  CB   sing N N 237 
MET   CA  HA   sing N N 238 
MET   C   O    doub N N 239 
MET   C   OXT  sing N N 240 
MET   CB  CG   sing N N 241 
MET   CB  HB2  sing N N 242 
MET   CB  HB3  sing N N 243 
MET   CG  SD   sing N N 244 
MET   CG  HG2  sing N N 245 
MET   CG  HG3  sing N N 246 
MET   SD  CE   sing N N 247 
MET   CE  HE1  sing N N 248 
MET   CE  HE2  sing N N 249 
MET   CE  HE3  sing N N 250 
MET   OXT HXT  sing N N 251 
PHE   N   CA   sing N N 252 
PHE   N   H    sing N N 253 
PHE   N   H2   sing N N 254 
PHE   CA  C    sing N N 255 
PHE   CA  CB   sing N N 256 
PHE   CA  HA   sing N N 257 
PHE   C   O    doub N N 258 
PHE   C   OXT  sing N N 259 
PHE   CB  CG   sing N N 260 
PHE   CB  HB2  sing N N 261 
PHE   CB  HB3  sing N N 262 
PHE   CG  CD1  doub Y N 263 
PHE   CG  CD2  sing Y N 264 
PHE   CD1 CE1  sing Y N 265 
PHE   CD1 HD1  sing N N 266 
PHE   CD2 CE2  doub Y N 267 
PHE   CD2 HD2  sing N N 268 
PHE   CE1 CZ   doub Y N 269 
PHE   CE1 HE1  sing N N 270 
PHE   CE2 CZ   sing Y N 271 
PHE   CE2 HE2  sing N N 272 
PHE   CZ  HZ   sing N N 273 
PHE   OXT HXT  sing N N 274 
PRO   N   CA   sing N N 275 
PRO   N   CD   sing N N 276 
PRO   N   H    sing N N 277 
PRO   CA  C    sing N N 278 
PRO   CA  CB   sing N N 279 
PRO   CA  HA   sing N N 280 
PRO   C   O    doub N N 281 
PRO   C   OXT  sing N N 282 
PRO   CB  CG   sing N N 283 
PRO   CB  HB2  sing N N 284 
PRO   CB  HB3  sing N N 285 
PRO   CG  CD   sing N N 286 
PRO   CG  HG2  sing N N 287 
PRO   CG  HG3  sing N N 288 
PRO   CD  HD2  sing N N 289 
PRO   CD  HD3  sing N N 290 
PRO   OXT HXT  sing N N 291 
SER   N   CA   sing N N 292 
SER   N   H    sing N N 293 
SER   N   H2   sing N N 294 
SER   CA  C    sing N N 295 
SER   CA  CB   sing N N 296 
SER   CA  HA   sing N N 297 
SER   C   O    doub N N 298 
SER   C   OXT  sing N N 299 
SER   CB  OG   sing N N 300 
SER   CB  HB2  sing N N 301 
SER   CB  HB3  sing N N 302 
SER   OG  HG   sing N N 303 
SER   OXT HXT  sing N N 304 
THR   N   CA   sing N N 305 
THR   N   H    sing N N 306 
THR   N   H2   sing N N 307 
THR   CA  C    sing N N 308 
THR   CA  CB   sing N N 309 
THR   CA  HA   sing N N 310 
THR   C   O    doub N N 311 
THR   C   OXT  sing N N 312 
THR   CB  OG1  sing N N 313 
THR   CB  CG2  sing N N 314 
THR   CB  HB   sing N N 315 
THR   OG1 HG1  sing N N 316 
THR   CG2 HG21 sing N N 317 
THR   CG2 HG22 sing N N 318 
THR   CG2 HG23 sing N N 319 
THR   OXT HXT  sing N N 320 
TRP   N   CA   sing N N 321 
TRP   N   H    sing N N 322 
TRP   N   H2   sing N N 323 
TRP   CA  C    sing N N 324 
TRP   CA  CB   sing N N 325 
TRP   CA  HA   sing N N 326 
TRP   C   O    doub N N 327 
TRP   C   OXT  sing N N 328 
TRP   CB  CG   sing N N 329 
TRP   CB  HB2  sing N N 330 
TRP   CB  HB3  sing N N 331 
TRP   CG  CD1  doub Y N 332 
TRP   CG  CD2  sing Y N 333 
TRP   CD1 NE1  sing Y N 334 
TRP   CD1 HD1  sing N N 335 
TRP   CD2 CE2  doub Y N 336 
TRP   CD2 CE3  sing Y N 337 
TRP   NE1 CE2  sing Y N 338 
TRP   NE1 HE1  sing N N 339 
TRP   CE2 CZ2  sing Y N 340 
TRP   CE3 CZ3  doub Y N 341 
TRP   CE3 HE3  sing N N 342 
TRP   CZ2 CH2  doub Y N 343 
TRP   CZ2 HZ2  sing N N 344 
TRP   CZ3 CH2  sing Y N 345 
TRP   CZ3 HZ3  sing N N 346 
TRP   CH2 HH2  sing N N 347 
TRP   OXT HXT  sing N N 348 
TYR   N   CA   sing N N 349 
TYR   N   H    sing N N 350 
TYR   N   H2   sing N N 351 
TYR   CA  C    sing N N 352 
TYR   CA  CB   sing N N 353 
TYR   CA  HA   sing N N 354 
TYR   C   O    doub N N 355 
TYR   C   OXT  sing N N 356 
TYR   CB  CG   sing N N 357 
TYR   CB  HB2  sing N N 358 
TYR   CB  HB3  sing N N 359 
TYR   CG  CD1  doub Y N 360 
TYR   CG  CD2  sing Y N 361 
TYR   CD1 CE1  sing Y N 362 
TYR   CD1 HD1  sing N N 363 
TYR   CD2 CE2  doub Y N 364 
TYR   CD2 HD2  sing N N 365 
TYR   CE1 CZ   doub Y N 366 
TYR   CE1 HE1  sing N N 367 
TYR   CE2 CZ   sing Y N 368 
TYR   CE2 HE2  sing N N 369 
TYR   CZ  OH   sing N N 370 
TYR   OH  HH   sing N N 371 
TYR   OXT HXT  sing N N 372 
VAL   N   CA   sing N N 373 
VAL   N   H    sing N N 374 
VAL   N   H2   sing N N 375 
VAL   CA  C    sing N N 376 
VAL   CA  CB   sing N N 377 
VAL   CA  HA   sing N N 378 
VAL   C   O    doub N N 379 
VAL   C   OXT  sing N N 380 
VAL   CB  CG1  sing N N 381 
VAL   CB  CG2  sing N N 382 
VAL   CB  HB   sing N N 383 
VAL   CG1 HG11 sing N N 384 
VAL   CG1 HG12 sing N N 385 
VAL   CG1 HG13 sing N N 386 
VAL   CG2 HG21 sing N N 387 
VAL   CG2 HG22 sing N N 388 
VAL   CG2 HG23 sing N N 389 
VAL   OXT HXT  sing N N 390 
# 
_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                    7HAZ 
_atom_sites.fract_transf_matrix[1][1]   0.015248 
_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]   0.011167 
_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]   0.009998 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
_atom_type.scat_dispersion_real 
_atom_type.scat_dispersion_imag 
_atom_type.scat_Cromer_Mann_a1 
_atom_type.scat_Cromer_Mann_a2 
_atom_type.scat_Cromer_Mann_a3 
_atom_type.scat_Cromer_Mann_a4 
_atom_type.scat_Cromer_Mann_b1 
_atom_type.scat_Cromer_Mann_b2 
_atom_type.scat_Cromer_Mann_b3 
_atom_type.scat_Cromer_Mann_b4 
_atom_type.scat_Cromer_Mann_c 
_atom_type.scat_source 
_atom_type.scat_dispersion_source 
C ? ? 3.54356 2.42580 ? ? 25.62398 1.50364  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
N ? ? 4.01032 2.96436 ? ? 19.97189 1.75589  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O ? ? 4.49882 3.47563 ? ? 15.80542 1.70748  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
S ? ? 9.55732 6.39887 ? ? 1.23737  29.19336 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N   . GLU   A 1 9   ? 4.20733   -28.85336 -38.97767 1.000 54.80294  ? 16  GLU   A N   1 
ATOM   2    C CA  . GLU   A 1 9   ? 5.33526   -27.95504 -39.19887 1.000 50.39071  ? 16  GLU   A CA  1 
ATOM   3    C C   . GLU   A 1 9   ? 5.55959   -27.09816 -37.95672 1.000 44.77359  ? 16  GLU   A C   1 
ATOM   4    O O   . GLU   A 1 9   ? 4.86401   -26.10510 -37.74328 1.000 52.86019  ? 16  GLU   A O   1 
ATOM   5    C CB  . GLU   A 1 9   ? 5.08876   -27.07770 -40.42857 1.000 58.55315  ? 16  GLU   A CB  1 
ATOM   6    C CG  . GLU   A 1 9   ? 6.34061   -26.73414 -41.23406 1.000 76.16284  ? 16  GLU   A CG  1 
ATOM   7    C CD  . GLU   A 1 9   ? 7.27132   -25.76776 -40.52723 1.000 80.61246  ? 16  GLU   A CD  1 
ATOM   8    O OE1 . GLU   A 1 9   ? 6.81045   -25.03963 -39.62385 1.000 79.75544  ? 16  GLU   A OE1 1 
ATOM   9    O OE2 . GLU   A 1 9   ? 8.47045   -25.73224 -40.88022 1.000 78.87055  ? 16  GLU   A OE2 1 
ATOM   10   N N   . VAL   A 1 10  ? 6.53830   -27.48786 -37.14378 1.000 37.64081  ? 17  VAL   A N   1 
ATOM   11   C CA  . VAL   A 1 10  ? 6.82935   -26.83905 -35.87069 1.000 32.33989  ? 17  VAL   A CA  1 
ATOM   12   C C   . VAL   A 1 10  ? 8.18914   -26.16402 -35.97131 1.000 36.02522  ? 17  VAL   A C   1 
ATOM   13   O O   . VAL   A 1 10  ? 9.18152   -26.80802 -36.32959 1.000 39.47942  ? 17  VAL   A O   1 
ATOM   14   C CB  . VAL   A 1 10  ? 6.80581   -27.85035 -34.71201 1.000 40.77780  ? 17  VAL   A CB  1 
ATOM   15   C CG1 . VAL   A 1 10  ? 6.96731   -27.14191 -33.38154 1.000 35.10636  ? 17  VAL   A CG1 1 
ATOM   16   C CG2 . VAL   A 1 10  ? 5.52169   -28.66222 -34.74338 1.000 54.62530  ? 17  VAL   A CG2 1 
ATOM   17   N N   . GLU   A 1 11  ? 8.23580   -24.87224 -35.66041 1.000 27.64067  ? 18  GLU   A N   1 
ATOM   18   C CA  . GLU   A 1 11  ? 9.48677   -24.12474 -35.61605 1.000 26.90986  ? 18  GLU   A CA  1 
ATOM   19   C C   . GLU   A 1 11  ? 9.92670   -23.96201 -34.16616 1.000 29.65198  ? 18  GLU   A C   1 
ATOM   20   O O   . GLU   A 1 11  ? 9.12703   -23.57028 -33.31271 1.000 25.70996  ? 18  GLU   A O   1 
ATOM   21   C CB  . GLU   A 1 11  ? 9.33051   -22.75473 -36.27959 1.000 29.40623  ? 18  GLU   A CB  1 
ATOM   22   C CG  . GLU   A 1 11  ? 9.13433   -22.79150 -37.79049 1.000 31.05093  ? 18  GLU   A CG  1 
ATOM   23   C CD  . GLU   A 1 11  ? 8.87884   -21.41147 -38.36654 1.000 42.68976  ? 18  GLU   A CD  1 
ATOM   24   O OE1 . GLU   A 1 11  ? 7.81410   -20.83030 -38.07089 1.000 47.13555  ? 18  GLU   A OE1 1 
ATOM   25   O OE2 . GLU   A 1 11  ? 9.74622   -20.90273 -39.10547 1.000 50.42170  ? 18  GLU   A OE2 1 
ATOM   26   N N   . THR   A 1 12  ? 11.19137  -24.25949 -33.88768 1.000 25.37004  ? 19  THR   A N   1 
ATOM   27   C CA  . THR   A 1 12  ? 11.73601  -24.14157 -32.54187 1.000 22.18153  ? 19  THR   A CA  1 
ATOM   28   C C   . THR   A 1 12  ? 12.73014  -22.99060 -32.49805 1.000 24.45499  ? 19  THR   A C   1 
ATOM   29   O O   . THR   A 1 12  ? 13.59718  -22.88216 -33.36961 1.000 22.18977  ? 19  THR   A O   1 
ATOM   30   C CB  . THR   A 1 12  ? 12.40091  -25.44465 -32.10020 1.000 21.42726  ? 19  THR   A CB  1 
ATOM   31   O OG1 . THR   A 1 12  ? 11.44852  -26.51145 -32.18159 1.000 26.55347  ? 19  THR   A OG1 1 
ATOM   32   C CG2 . THR   A 1 12  ? 12.89445  -25.33317 -30.65758 1.000 22.71450  ? 19  THR   A CG2 1 
ATOM   33   N N   . PHE   A 1 13  ? 12.59957  -22.14159 -31.47966 1.000 22.65108  ? 20  PHE   A N   1 
ATOM   34   C CA  . PHE   A 1 13  ? 13.38390  -20.92343 -31.33981 1.000 22.11021  ? 20  PHE   A CA  1 
ATOM   35   C C   . PHE   A 1 13  ? 14.07741  -20.91387 -29.98868 1.000 24.24224  ? 20  PHE   A C   1 
ATOM   36   O O   . PHE   A 1 13  ? 13.55823  -21.45220 -29.00996 1.000 23.47191  ? 20  PHE   A O   1 
ATOM   37   C CB  . PHE   A 1 13  ? 12.50875  -19.66208 -31.41662 1.000 20.74506  ? 20  PHE   A CB  1 
ATOM   38   C CG  . PHE   A 1 13  ? 11.77849  -19.48923 -32.71589 1.000 24.23363  ? 20  PHE   A CG  1 
ATOM   39   C CD1 . PHE   A 1 13  ? 10.57046  -20.13597 -32.93614 1.000 27.42247  ? 20  PHE   A CD1 1 
ATOM   40   C CD2 . PHE   A 1 13  ? 12.28318  -18.66073 -33.70545 1.000 28.74472  ? 20  PHE   A CD2 1 
ATOM   41   C CE1 . PHE   A 1 13  ? 9.88863   -19.97411 -34.12964 1.000 27.64270  ? 20  PHE   A CE1 1 
ATOM   42   C CE2 . PHE   A 1 13  ? 11.60943  -18.49668 -34.90157 1.000 33.52424  ? 20  PHE   A CE2 1 
ATOM   43   C CZ  . PHE   A 1 13  ? 10.41004  -19.15479 -35.11303 1.000 29.92894  ? 20  PHE   A CZ  1 
ATOM   44   N N   . ALA   A 1 14  ? 15.23490  -20.26117 -29.92871 1.000 21.46696  ? 21  ALA   A N   1 
ATOM   45   C CA  . ALA   A 1 14  ? 15.88826  -20.00354 -28.65460 1.000 21.44444  ? 21  ALA   A CA  1 
ATOM   46   C C   . ALA   A 1 14  ? 15.44027  -18.65335 -28.10443 1.000 21.35068  ? 21  ALA   A C   1 
ATOM   47   O O   . ALA   A 1 14  ? 15.34498  -17.66902 -28.84115 1.000 24.01468  ? 21  ALA   A O   1 
ATOM   48   C CB  . ALA   A 1 14  ? 17.40999  -20.02890 -28.80888 1.000 25.01965  ? 21  ALA   A CB  1 
ATOM   49   N N   . PHE   A 1 15  ? 15.14499  -18.61527 -26.80573 1.000 23.51401  ? 22  PHE   A N   1 
ATOM   50   C CA  . PHE   A 1 15  ? 14.95938  -17.33381 -26.14028 1.000 21.09970  ? 22  PHE   A CA  1 
ATOM   51   C C   . PHE   A 1 15  ? 16.25149  -16.52694 -26.20607 1.000 19.38207  ? 22  PHE   A C   1 
ATOM   52   O O   . PHE   A 1 15  ? 17.35459  -17.08121 -26.14123 1.000 24.68618  ? 22  PHE   A O   1 
ATOM   53   C CB  . PHE   A 1 15  ? 14.57210  -17.53126 -24.67027 1.000 22.29228  ? 22  PHE   A CB  1 
ATOM   54   C CG  . PHE   A 1 15  ? 13.15966  -18.01986 -24.45165 1.000 22.37701  ? 22  PHE   A CG  1 
ATOM   55   C CD1 . PHE   A 1 15  ? 12.07166  -17.21907 -24.76289 1.000 21.83264  ? 22  PHE   A CD1 1 
ATOM   56   C CD2 . PHE   A 1 15  ? 12.92967  -19.26738 -23.89556 1.000 21.46693  ? 22  PHE   A CD2 1 
ATOM   57   C CE1 . PHE   A 1 15  ? 10.77150  -17.65604 -24.53810 1.000 19.97454  ? 22  PHE   A CE1 1 
ATOM   58   C CE2 . PHE   A 1 15  ? 11.62931  -19.72452 -23.67873 1.000 21.52456  ? 22  PHE   A CE2 1 
ATOM   59   C CZ  . PHE   A 1 15  ? 10.54944  -18.91600 -23.99571 1.000 20.39459  ? 22  PHE   A CZ  1 
ATOM   60   N N   . GLN   A 1 16  ? 16.11741  -15.20805 -26.33544 1.000 23.58241  ? 23  GLN   A N   1 
ATOM   61   C CA  . GLN   A 1 16  ? 17.26270  -14.34923 -26.06142 1.000 24.07340  ? 23  GLN   A CA  1 
ATOM   62   C C   . GLN   A 1 16  ? 17.77216  -14.62137 -24.65196 1.000 26.38185  ? 23  GLN   A C   1 
ATOM   63   O O   . GLN   A 1 16  ? 17.00195  -14.93721 -23.74149 1.000 25.92064  ? 23  GLN   A O   1 
ATOM   64   C CB  . GLN   A 1 16  ? 16.90993  -12.86859 -26.20086 1.000 25.87489  ? 23  GLN   A CB  1 
ATOM   65   C CG  . GLN   A 1 16  ? 16.53872  -12.40807 -27.59103 1.000 34.28434  ? 23  GLN   A CG  1 
ATOM   66   C CD  . GLN   A 1 16  ? 15.89238  -11.03459 -27.56907 1.000 44.20184  ? 23  GLN   A CD  1 
ATOM   67   O OE1 . GLN   A 1 16  ? 14.67214  -10.91192 -27.51692 1.000 42.93841  ? 23  GLN   A OE1 1 
ATOM   68   N NE2 . GLN   A 1 16  ? 16.71663  -9.99102  -27.60555 1.000 44.04609  ? 23  GLN   A NE2 1 
ATOM   69   N N   . ALA   A 1 17  ? 19.08957  -14.49934 -24.48118 1.000 27.62421  ? 24  ALA   A N   1 
ATOM   70   C CA  . ALA   A 1 17  ? 19.71757  -14.87097 -23.21569 1.000 27.45457  ? 24  ALA   A CA  1 
ATOM   71   C C   . ALA   A 1 17  ? 19.07948  -14.15242 -22.03086 1.000 29.54325  ? 24  ALA   A C   1 
ATOM   72   O O   . ALA   A 1 17  ? 18.90794  -14.74576 -20.95952 1.000 31.45557  ? 24  ALA   A O   1 
ATOM   73   C CB  . ALA   A 1 17  ? 21.21774  -14.58234 -23.27416 1.000 33.93774  ? 24  ALA   A CB  1 
ATOM   74   N N   . GLU   A 1 18  ? 18.71276  -12.87856 -22.20205 1.000 26.36874  ? 25  GLU   A N   1 
ATOM   75   C CA  . GLU   A 1 18  ? 18.15387  -12.12367 -21.08340 1.000 30.32423  ? 25  GLU   A CA  1 
ATOM   76   C C   . GLU   A 1 18  ? 16.76911  -12.63271 -20.70357 1.000 29.72571  ? 25  GLU   A C   1 
ATOM   77   O O   . GLU   A 1 18  ? 16.40756  -12.62934 -19.51977 1.000 28.64002  ? 25  GLU   A O   1 
ATOM   78   C CB  . GLU   A 1 18  ? 18.10590  -10.62887 -21.40950 1.000 34.09537  ? 25  GLU   A CB  1 
ATOM   79   C CG  . GLU   A 1 18  ? 19.46849  -9.97218  -21.64697 1.000 39.37105  ? 25  GLU   A CG  1 
ATOM   80   C CD  . GLU   A 1 18  ? 19.99599  -10.14168 -23.06135 1.000 49.61692  ? 25  GLU   A CD  1 
ATOM   81   O OE1 . GLU   A 1 18  ? 19.35572  -10.84581 -23.87111 1.000 42.61339  ? 25  GLU   A OE1 1 
ATOM   82   O OE2 . GLU   A 1 18  ? 21.05714  -9.55437  -23.36528 1.000 60.05067  ? 25  GLU   A OE2 1 
ATOM   83   N N   . ILE   A 1 19  ? 15.98109  -13.07530 -21.68907 1.000 23.30920  ? 26  ILE   A N   1 
ATOM   84   C CA  . ILE   A 1 19  ? 14.65913  -13.61912 -21.38667 1.000 25.06705  ? 26  ILE   A CA  1 
ATOM   85   C C   . ILE   A 1 19  ? 14.79550  -14.98017 -20.71819 1.000 24.00970  ? 26  ILE   A C   1 
ATOM   86   O O   . ILE   A 1 19  ? 14.07300  -15.29510 -19.76510 1.000 24.09299  ? 26  ILE   A O   1 
ATOM   87   C CB  . ILE   A 1 19  ? 13.78121  -13.70029 -22.65455 1.000 24.94072  ? 26  ILE   A CB  1 
ATOM   88   C CG1 . ILE   A 1 19  ? 13.27395  -12.32142 -23.10946 1.000 28.80212  ? 26  ILE   A CG1 1 
ATOM   89   C CG2 . ILE   A 1 19  ? 12.56407  -14.60478 -22.41120 1.000 24.16287  ? 26  ILE   A CG2 1 
ATOM   90   C CD1 . ILE   A 1 19  ? 14.32374  -11.26240 -23.40949 1.000 38.29933  ? 26  ILE   A CD1 1 
ATOM   91   N N   . ALA   A 1 20  ? 15.72253  -15.81162 -21.20507 1.000 25.08152  ? 27  ALA   A N   1 
ATOM   92   C CA  . ALA   A 1 20  ? 15.99224  -17.07377 -20.52699 1.000 29.30599  ? 27  ALA   A CA  1 
ATOM   93   C C   . ALA   A 1 20  ? 16.38835  -16.83100 -19.07502 1.000 26.18652  ? 27  ALA   A C   1 
ATOM   94   O O   . ALA   A 1 20  ? 15.94940  -17.55389 -18.17146 1.000 28.19405  ? 27  ALA   A O   1 
ATOM   95   C CB  . ALA   A 1 20  ? 17.08517  -17.84440 -21.26879 1.000 24.74404  ? 27  ALA   A CB  1 
ATOM   96   N N   . GLN   A 1 21  ? 17.20124  -15.79749 -18.83405 1.000 24.87960  ? 28  GLN   A N   1 
ATOM   97   C CA  . GLN   A 1 21  ? 17.61627  -15.46377 -17.47477 1.000 25.87581  ? 28  GLN   A CA  1 
ATOM   98   C C   . GLN   A 1 21  ? 16.42941  -15.02982 -16.62027 1.000 27.53900  ? 28  GLN   A C   1 
ATOM   99   O O   . GLN   A 1 21  ? 16.31624  -15.43906 -15.45922 1.000 31.25778  ? 28  GLN   A O   1 
ATOM   100  C CB  . GLN   A 1 21  ? 18.67858  -14.36677 -17.51749 1.000 34.86759  ? 28  GLN   A CB  1 
ATOM   101  C CG  . GLN   A 1 21  ? 19.13998  -13.88097 -16.15704 1.000 56.54995  ? 28  GLN   A CG  1 
ATOM   102  C CD  . GLN   A 1 21  ? 20.38589  -13.01887 -16.24227 1.000 66.37119  ? 28  GLN   A CD  1 
ATOM   103  O OE1 . GLN   A 1 21  ? 20.48729  -12.13762 -17.09759 1.000 64.74165  ? 28  GLN   A OE1 1 
ATOM   104  N NE2 . GLN   A 1 21  ? 21.33585  -13.26016 -15.34653 1.000 67.25598  ? 28  GLN   A NE2 1 
ATOM   105  N N   . LEU   A 1 22  ? 15.54516  -14.19204 -17.17263 1.000 29.86811  ? 29  LEU   A N   1 
ATOM   106  C CA  . LEU   A 1 22  ? 14.33749  -13.78956 -16.45363 1.000 25.65911  ? 29  LEU   A CA  1 
ATOM   107  C C   . LEU   A 1 22  ? 13.49477  -14.99957 -16.08167 1.000 27.54625  ? 29  LEU   A C   1 
ATOM   108  O O   . LEU   A 1 22  ? 12.99769  -15.10917 -14.95534 1.000 26.17168  ? 29  LEU   A O   1 
ATOM   109  C CB  . LEU   A 1 22  ? 13.51694  -12.82076 -17.30687 1.000 27.34518  ? 29  LEU   A CB  1 
ATOM   110  C CG  . LEU   A 1 22  ? 12.11491  -12.47915 -16.79588 1.000 27.00932  ? 29  LEU   A CG  1 
ATOM   111  C CD1 . LEU   A 1 22  ? 12.19240  -11.61315 -15.54552 1.000 33.73665  ? 29  LEU   A CD1 1 
ATOM   112  C CD2 . LEU   A 1 22  ? 11.29634  -11.79842 -17.87841 1.000 31.80033  ? 29  LEU   A CD2 1 
ATOM   113  N N   . MET   A 1 23  ? 13.33023  -15.92238 -17.02630 1.000 25.84123  ? 30  MET   A N   1 
ATOM   114  C CA  . MET   A 1 23  ? 12.47468  -17.08366 -16.81558 1.000 23.30361  ? 30  MET   A CA  1 
ATOM   115  C C   . MET   A 1 23  ? 13.05181  -17.99939 -15.74093 1.000 24.38390  ? 30  MET   A C   1 
ATOM   116  O O   . MET   A 1 23  ? 12.31901  -18.50699 -14.88424 1.000 26.16335  ? 30  MET   A O   1 
ATOM   117  C CB  . MET   A 1 23  ? 12.33236  -17.81812 -18.14533 1.000 20.65042  ? 30  MET   A CB  1 
ATOM   118  C CG  . MET   A 1 23  ? 11.51975  -17.02630 -19.14796 1.000 25.54074  ? 30  MET   A CG  1 
ATOM   119  S SD  . MET   A 1 23  ? 11.15761  -17.90297 -20.67541 1.000 25.10804  ? 30  MET   A SD  1 
ATOM   120  C CE  . MET   A 1 23  ? 10.24191  -19.31624 -20.06982 1.000 27.56897  ? 30  MET   A CE  1 
ATOM   121  N N   . SER   A 1 24  ? 14.36917  -18.21670 -15.76466 1.000 24.50943  ? 31  SER   A N   1 
ATOM   122  C CA  . SER   A 1 24  ? 14.99951  -19.02790 -14.72689 1.000 26.89805  ? 31  SER   A CA  1 
ATOM   123  C C   . SER   A 1 24  ? 14.91869  -18.35708 -13.35780 1.000 31.36117  ? 31  SER   A C   1 
ATOM   124  O O   . SER   A 1 24  ? 14.76472  -19.04745 -12.34293 1.000 30.82619  ? 31  SER   A O   1 
ATOM   125  C CB  . SER   A 1 24  ? 16.45031  -19.32621 -15.11375 1.000 35.31662  ? 31  SER   A CB  1 
ATOM   126  O OG  . SER   A 1 24  ? 17.34813  -18.46563 -14.44203 1.000 61.36442  ? 31  SER   A OG  1 
ATOM   127  N N   . LEU   A 1 25  ? 15.01073  -17.02307 -13.30142 1.000 25.23964  ? 32  LEU   A N   1 
ATOM   128  C CA  . LEU   A 1 25  ? 14.83381  -16.32459 -12.02710 1.000 28.52014  ? 32  LEU   A CA  1 
ATOM   129  C C   . LEU   A 1 25  ? 13.42096  -16.52156 -11.48297 1.000 31.26117  ? 32  LEU   A C   1 
ATOM   130  O O   . LEU   A 1 25  ? 13.22989  -16.73058 -10.27863 1.000 32.51181  ? 32  LEU   A O   1 
ATOM   131  C CB  . LEU   A 1 25  ? 15.15602  -14.83530 -12.20665 1.000 33.41463  ? 32  LEU   A CB  1 
ATOM   132  C CG  . LEU   A 1 25  ? 15.25666  -13.84080 -11.03591 1.000 54.79766  ? 32  LEU   A CG  1 
ATOM   133  C CD1 . LEU   A 1 25  ? 15.80066  -12.51327 -11.53743 1.000 45.02715  ? 32  LEU   A CD1 1 
ATOM   134  C CD2 . LEU   A 1 25  ? 13.92674  -13.58581 -10.33581 1.000 51.34694  ? 32  LEU   A CD2 1 
ATOM   135  N N   . ILE   A 1 26  ? 12.41743  -16.44202 -12.35410 1.000 26.94457  ? 33  ILE   A N   1 
ATOM   136  C CA  . ILE   A 1 26  ? 11.03210  -16.60135 -11.92032 1.000 29.41594  ? 33  ILE   A CA  1 
ATOM   137  C C   . ILE   A 1 26  ? 10.78140  -18.02278 -11.42641 1.000 32.28977  ? 33  ILE   A C   1 
ATOM   138  O O   . ILE   A 1 26  ? 10.03628  -18.24323 -10.45939 1.000 30.93914  ? 33  ILE   A O   1 
ATOM   139  C CB  . ILE   A 1 26  ? 10.08608  -16.21163 -13.07044 1.000 24.97521  ? 33  ILE   A CB  1 
ATOM   140  C CG1 . ILE   A 1 26  ? 10.09110  -14.68934 -13.25307 1.000 27.35732  ? 33  ILE   A CG1 1 
ATOM   141  C CG2 . ILE   A 1 26  ? 8.67167   -16.74686 -12.82903 1.000 26.82461  ? 33  ILE   A CG2 1 
ATOM   142  C CD1 . ILE   A 1 26  ? 9.48483   -14.22140 -14.55895 1.000 27.56034  ? 33  ILE   A CD1 1 
ATOM   143  N N   . ILE   A 1 27  ? 11.42100  -19.00439 -12.05686 1.000 29.73863  ? 34  ILE   A N   1 
ATOM   144  C CA  . ILE   A 1 27  ? 11.18393  -20.39749 -11.69947 1.000 32.64393  ? 34  ILE   A CA  1 
ATOM   145  C C   . ILE   A 1 27  ? 11.94634  -20.77820 -10.43370 1.000 34.12646  ? 34  ILE   A C   1 
ATOM   146  O O   . ILE   A 1 27  ? 11.44114  -21.53470 -9.59591  1.000 37.87464  ? 34  ILE   A O   1 
ATOM   147  C CB  . ILE   A 1 27  ? 11.55168  -21.30265 -12.89124 1.000 29.11633  ? 34  ILE   A CB  1 
ATOM   148  C CG1 . ILE   A 1 27  ? 10.49218  -21.17697 -13.98733 1.000 28.44289  ? 34  ILE   A CG1 1 
ATOM   149  C CG2 . ILE   A 1 27  ? 11.69326  -22.75267 -12.45481 1.000 34.32223  ? 34  ILE   A CG2 1 
ATOM   150  C CD1 . ILE   A 1 27  ? 10.97084  -21.61134 -15.35425 1.000 34.07764  ? 34  ILE   A CD1 1 
ATOM   151  N N   . ASN   A 1 28  ? 13.15359  -20.24025 -10.24981 1.000 30.81389  ? 35  ASN   A N   1 
ATOM   152  C CA  . ASN   A 1 28  ? 14.05352  -20.74108 -9.21645  1.000 36.20189  ? 35  ASN   A CA  1 
ATOM   153  C C   . ASN   A 1 28  ? 14.08261  -19.90552 -7.94259  1.000 34.90258  ? 35  ASN   A C   1 
ATOM   154  O O   . ASN   A 1 28  ? 14.53967  -20.40877 -6.90935  1.000 41.66064  ? 35  ASN   A O   1 
ATOM   155  C CB  . ASN   A 1 28  ? 15.47970  -20.85124 -9.77170  1.000 44.27945  ? 35  ASN   A CB  1 
ATOM   156  C CG  . ASN   A 1 28  ? 15.60094  -21.91373 -10.84422 1.000 42.44519  ? 35  ASN   A CG  1 
ATOM   157  O OD1 . ASN   A 1 28  ? 15.00905  -22.98791 -10.73656 1.000 53.57030  ? 35  ASN   A OD1 1 
ATOM   158  N ND2 . ASN   A 1 28  ? 16.36053  -21.61645 -11.89204 1.000 50.15924  ? 35  ASN   A ND2 1 
ATOM   159  N N   . THR   A 1 29  ? 13.62091  -18.65775 -7.97547  1.000 34.04787  ? 36  THR   A N   1 
ATOM   160  C CA  . THR   A 1 29  ? 13.65206  -17.82744 -6.77557  1.000 35.54311  ? 36  THR   A CA  1 
ATOM   161  C C   . THR   A 1 29  ? 12.55068  -18.24337 -5.80778  1.000 33.75262  ? 36  THR   A C   1 
ATOM   162  O O   . THR   A 1 29  ? 11.39266  -18.40312 -6.20414  1.000 35.45924  ? 36  THR   A O   1 
ATOM   163  C CB  . THR   A 1 29  ? 13.49383  -16.35113 -7.14105  1.000 40.35495  ? 36  THR   A CB  1 
ATOM   164  O OG1 . THR   A 1 29  ? 14.55083  -15.95944 -8.02441  1.000 38.52669  ? 36  THR   A OG1 1 
ATOM   165  C CG2 . THR   A 1 29  ? 13.53081  -15.47842 -5.89205  1.000 43.82624  ? 36  THR   A CG2 1 
ATOM   166  N N   . PHE   A 1 30  ? 12.90665  -18.41710 -4.53449  1.000 36.20246  ? 37  PHE   A N   1 
ATOM   167  C CA  . PHE   A 1 30  ? 11.89123  -18.68774 -3.52450  1.000 39.43960  ? 37  PHE   A CA  1 
ATOM   168  C C   . PHE   A 1 30  ? 11.05032  -17.43638 -3.30273  1.000 36.35526  ? 37  PHE   A C   1 
ATOM   169  O O   . PHE   A 1 30  ? 11.56262  -16.40422 -2.85725  1.000 36.29771  ? 37  PHE   A O   1 
ATOM   170  C CB  . PHE   A 1 30  ? 12.52391  -19.14479 -2.21287  1.000 39.64406  ? 37  PHE   A CB  1 
ATOM   171  C CG  . PHE   A 1 30  ? 11.51761  -19.39075 -1.12393  1.000 34.62778  ? 37  PHE   A CG  1 
ATOM   172  C CD1 . PHE   A 1 30  ? 10.68718  -20.49930 -1.17194  1.000 41.10773  ? 37  PHE   A CD1 1 
ATOM   173  C CD2 . PHE   A 1 30  ? 11.38524  -18.50541 -0.06270  1.000 36.06553  ? 37  PHE   A CD2 1 
ATOM   174  C CE1 . PHE   A 1 30  ? 9.74664   -20.72740 -0.17756  1.000 35.50474  ? 37  PHE   A CE1 1 
ATOM   175  C CE2 . PHE   A 1 30  ? 10.44527  -18.72788 0.93167   1.000 42.43375  ? 37  PHE   A CE2 1 
ATOM   176  C CZ  . PHE   A 1 30  ? 9.62795   -19.84152 0.87488   1.000 38.34259  ? 37  PHE   A CZ  1 
ATOM   177  N N   . TYR   A 1 31  ? 9.75671   -17.52712 -3.60339  1.000 29.35703  ? 38  TYR   A N   1 
ATOM   178  C CA  . TYR   A 1 31  ? 8.88511   -16.35942 -3.51397  1.000 27.93696  ? 38  TYR   A CA  1 
ATOM   179  C C   . TYR   A 1 31  ? 7.45799   -16.87115 -3.36779  1.000 27.69615  ? 38  TYR   A C   1 
ATOM   180  O O   . TYR   A 1 31  ? 6.91564   -17.46178 -4.30646  1.000 30.43045  ? 38  TYR   A O   1 
ATOM   181  C CB  . TYR   A 1 31  ? 9.04505   -15.47700 -4.75139  1.000 28.10507  ? 38  TYR   A CB  1 
ATOM   182  C CG  . TYR   A 1 31  ? 8.11022   -14.29276 -4.78097  1.000 31.91505  ? 38  TYR   A CG  1 
ATOM   183  C CD1 . TYR   A 1 31  ? 8.35352   -13.18368 -3.98440  1.000 40.83967  ? 38  TYR   A CD1 1 
ATOM   184  C CD2 . TYR   A 1 31  ? 6.98746   -14.28204 -5.59846  1.000 38.81339  ? 38  TYR   A CD2 1 
ATOM   185  C CE1 . TYR   A 1 31  ? 7.50987   -12.09797 -3.99493  1.000 47.56338  ? 38  TYR   A CE1 1 
ATOM   186  C CE2 . TYR   A 1 31  ? 6.13333   -13.19329 -5.61706  1.000 37.76435  ? 38  TYR   A CE2 1 
ATOM   187  C CZ  . TYR   A 1 31  ? 6.40480   -12.10633 -4.81209  1.000 41.15077  ? 38  TYR   A CZ  1 
ATOM   188  O OH  . TYR   A 1 31  ? 5.57267   -11.01638 -4.81140  1.000 53.39494  ? 38  TYR   A OH  1 
ATOM   189  N N   . SER   A 1 32  ? 6.85482   -16.63982 -2.20201  1.000 27.67318  ? 39  SER   A N   1 
ATOM   190  C CA  . SER   A 1 32  ? 5.60639   -17.30748 -1.86008  1.000 28.59396  ? 39  SER   A CA  1 
ATOM   191  C C   . SER   A 1 32  ? 4.38673   -16.68674 -2.53035  1.000 33.62453  ? 39  SER   A C   1 
ATOM   192  O O   . SER   A 1 32  ? 3.38077   -17.38017 -2.71134  1.000 32.25589  ? 39  SER   A O   1 
ATOM   193  C CB  . SER   A 1 32  ? 5.41590   -17.29931 -0.34212  1.000 30.17478  ? 39  SER   A CB  1 
ATOM   194  O OG  . SER   A 1 32  ? 6.38032   -18.11951 0.29653   1.000 33.28451  ? 39  SER   A OG  1 
ATOM   195  N N   . ASN   A 1 33  ? 4.45912   -15.41700 -2.92129  1.000 30.63563  ? 40  ASN   A N   1 
ATOM   196  C CA  . ASN   A 1 33  ? 3.28195   -14.65167 -3.34352  1.000 27.17827  ? 40  ASN   A CA  1 
ATOM   197  C C   . ASN   A 1 33  ? 2.99834   -14.87995 -4.83426  1.000 25.99098  ? 40  ASN   A C   1 
ATOM   198  O O   . ASN   A 1 33  ? 2.96707   -13.96095 -5.65209  1.000 28.26745  ? 40  ASN   A O   1 
ATOM   199  C CB  . ASN   A 1 33  ? 3.50129   -13.17670 -3.01119  1.000 32.12406  ? 40  ASN   A CB  1 
ATOM   200  C CG  . ASN   A 1 33  ? 2.31765   -12.29629 -3.36352  1.000 30.69362  ? 40  ASN   A CG  1 
ATOM   201  O OD1 . ASN   A 1 33  ? 1.16322   -12.70427 -3.24682  1.000 33.40346  ? 40  ASN   A OD1 1 
ATOM   202  N ND2 . ASN   A 1 33  ? 2.60445   -11.06243 -3.76573  1.000 32.18980  ? 40  ASN   A ND2 1 
ATOM   203  N N   . LYS   A 1 34  ? 2.78296   -16.15649 -5.17782  1.000 25.93470  ? 41  LYS   A N   1 
ATOM   204  C CA  . LYS   A 1 34  ? 2.66088   -16.56660 -6.57599  1.000 20.10895  ? 41  LYS   A CA  1 
ATOM   205  C C   . LYS   A 1 34  ? 1.36826   -16.08549 -7.22230  1.000 23.46588  ? 41  LYS   A C   1 
ATOM   206  O O   . LYS   A 1 34  ? 1.29992   -16.01183 -8.45776  1.000 23.95436  ? 41  LYS   A O   1 
ATOM   207  C CB  . LYS   A 1 34  ? 2.73012   -18.09384 -6.67950  1.000 24.83468  ? 41  LYS   A CB  1 
ATOM   208  C CG  . LYS   A 1 34  ? 4.10557   -18.70823 -6.40611  1.000 24.99840  ? 41  LYS   A CG  1 
ATOM   209  C CD  . LYS   A 1 34  ? 4.04102   -20.22954 -6.51833  1.000 27.44120  ? 41  LYS   A CD  1 
ATOM   210  C CE  . LYS   A 1 34  ? 5.39169   -20.89130 -6.25284  1.000 27.46587  ? 41  LYS   A CE  1 
ATOM   211  N NZ  . LYS   A 1 34  ? 6.32926   -20.79560 -7.40799  1.000 27.52276  ? 41  LYS   A NZ  1 
ATOM   212  N N   . GLU   A 1 35  ? 0.35085   -15.76141 -6.41845  1.000 25.11772  ? 42  GLU   A N   1 
ATOM   213  C CA  . GLU   A 1 35  ? -0.98145  -15.47048 -6.94054  1.000 25.18379  ? 42  GLU   A CA  1 
ATOM   214  C C   . GLU   A 1 35  ? -1.00997  -14.24896 -7.84726  1.000 26.25295  ? 42  GLU   A C   1 
ATOM   215  O O   . GLU   A 1 35  ? -1.99391  -14.05314 -8.56938  1.000 26.83206  ? 42  GLU   A O   1 
ATOM   216  C CB  . GLU   A 1 35  ? -1.96384  -15.26227 -5.78486  1.000 23.69601  ? 42  GLU   A CB  1 
ATOM   217  C CG  . GLU   A 1 35  ? -1.80721  -13.92596 -5.07551  1.000 25.59657  ? 42  GLU   A CG  1 
ATOM   218  C CD  . GLU   A 1 35  ? -2.69752  -13.79528 -3.84540  1.000 40.13984  ? 42  GLU   A CD  1 
ATOM   219  O OE1 . GLU   A 1 35  ? -2.86279  -14.79414 -3.11911  1.000 38.16713  ? 42  GLU   A OE1 1 
ATOM   220  O OE2 . GLU   A 1 35  ? -3.22043  -12.68883 -3.59766  1.000 45.93929  ? 42  GLU   A OE2 1 
ATOM   221  N N   . ILE   A 1 36  ? 0.03254   -13.41559 -7.82451  1.000 23.76182  ? 43  ILE   A N   1 
ATOM   222  C CA  . ILE   A 1 36  ? 0.03905   -12.22810 -8.66707  1.000 24.46929  ? 43  ILE   A CA  1 
ATOM   223  C C   . ILE   A 1 36  ? 0.13549   -12.56543 -10.14592 1.000 21.78640  ? 43  ILE   A C   1 
ATOM   224  O O   . ILE   A 1 36  ? -0.07323  -11.67830 -10.98134 1.000 21.64780  ? 43  ILE   A O   1 
ATOM   225  C CB  . ILE   A 1 36  ? 1.17555   -11.27410 -8.24350  1.000 27.74143  ? 43  ILE   A CB  1 
ATOM   226  C CG1 . ILE   A 1 36  ? 2.55060   -11.93356 -8.39511  1.000 30.96010  ? 43  ILE   A CG1 1 
ATOM   227  C CG2 . ILE   A 1 36  ? 0.95391   -10.79662 -6.80741  1.000 26.09802  ? 43  ILE   A CG2 1 
ATOM   228  C CD1 . ILE   A 1 36  ? 3.23868   -11.66820 -9.72845  1.000 31.13518  ? 43  ILE   A CD1 1 
ATOM   229  N N   . PHE   A 1 37  ? 0.43924   -13.82257 -10.49539 1.000 19.26341  ? 44  PHE   A N   1 
ATOM   230  C CA  . PHE   A 1 37  ? 0.45181   -14.19981 -11.90728 1.000 21.58864  ? 44  PHE   A CA  1 
ATOM   231  C C   . PHE   A 1 37  ? -0.88070  -13.86380 -12.56142 1.000 24.04419  ? 44  PHE   A C   1 
ATOM   232  O O   . PHE   A 1 37  ? -0.92402  -13.42946 -13.71780 1.000 22.23564  ? 44  PHE   A O   1 
ATOM   233  C CB  . PHE   A 1 37  ? 0.74915   -15.69684 -12.08026 1.000 24.86162  ? 44  PHE   A CB  1 
ATOM   234  C CG  . PHE   A 1 37  ? -0.46443  -16.58182 -11.90693 1.000 23.66437  ? 44  PHE   A CG  1 
ATOM   235  C CD1 . PHE   A 1 37  ? -0.82946  -17.04012 -10.65174 1.000 21.71100  ? 44  PHE   A CD1 1 
ATOM   236  C CD2 . PHE   A 1 37  ? -1.25947  -16.92709 -12.99646 1.000 24.03232  ? 44  PHE   A CD2 1 
ATOM   237  C CE1 . PHE   A 1 37  ? -1.95171  -17.83627 -10.48308 1.000 25.46677  ? 44  PHE   A CE1 1 
ATOM   238  C CE2 . PHE   A 1 37  ? -2.39134  -17.71475 -12.83012 1.000 22.12545  ? 44  PHE   A CE2 1 
ATOM   239  C CZ  . PHE   A 1 37  ? -2.73425  -18.17549 -11.57443 1.000 20.56054  ? 44  PHE   A CZ  1 
ATOM   240  N N   . LEU   A 1 38  ? -1.98577  -14.06548 -11.83814 1.000 21.60556  ? 45  LEU   A N   1 
ATOM   241  C CA  . LEU   A 1 38  ? -3.29078  -13.90339 -12.46979 1.000 21.26133  ? 45  LEU   A CA  1 
ATOM   242  C C   . LEU   A 1 38  ? -3.58716  -12.43418 -12.72847 1.000 23.11653  ? 45  LEU   A C   1 
ATOM   243  O O   . LEU   A 1 38  ? -4.10525  -12.07843 -13.79490 1.000 21.52243  ? 45  LEU   A O   1 
ATOM   244  C CB  . LEU   A 1 38  ? -4.38066  -14.54310 -11.61015 1.000 22.26087  ? 45  LEU   A CB  1 
ATOM   245  C CG  . LEU   A 1 38  ? -5.76858  -14.54574 -12.25375 1.000 25.36450  ? 45  LEU   A CG  1 
ATOM   246  C CD1 . LEU   A 1 38  ? -5.77402  -15.37858 -13.52773 1.000 22.59983  ? 45  LEU   A CD1 1 
ATOM   247  C CD2 . LEU   A 1 38  ? -6.80714  -15.06841 -11.28247 1.000 25.45687  ? 45  LEU   A CD2 1 
ATOM   248  N N   . ARG   A 1 39  ? -3.25009  -11.56815 -11.76794 1.000 21.97864  ? 46  ARG   A N   1 
ATOM   249  C CA  . ARG   A 1 39  ? -3.35342  -10.12626 -11.97607 1.000 19.92834  ? 46  ARG   A CA  1 
ATOM   250  C C   . ARG   A 1 39  ? -2.58318  -9.69263  -13.21579 1.000 22.41925  ? 46  ARG   A C   1 
ATOM   251  O O   . ARG   A 1 39  ? -3.07446  -8.88481  -14.01401 1.000 24.87623  ? 46  ARG   A O   1 
ATOM   252  C CB  . ARG   A 1 39  ? -2.82334  -9.38994  -10.74246 1.000 24.65886  ? 46  ARG   A CB  1 
ATOM   253  C CG  . ARG   A 1 39  ? -2.72610  -7.88319  -10.87542 1.000 31.42411  ? 46  ARG   A CG  1 
ATOM   254  C CD  . ARG   A 1 39  ? -2.05652  -7.28340  -9.64382  1.000 35.38045  ? 46  ARG   A CD  1 
ATOM   255  N NE  . ARG   A 1 39  ? -0.61178  -7.49233  -9.64911  1.000 36.67161  ? 46  ARG   A NE  1 
ATOM   256  C CZ  . ARG   A 1 39  ? 0.17545   -7.34158  -8.59229  1.000 42.04107  ? 46  ARG   A CZ  1 
ATOM   257  N NH1 . ARG   A 1 39  ? -0.31222  -7.01437  -7.40581  1.000 39.97972  ? 46  ARG   A NH1 1 
ATOM   258  N NH2 . ARG   A 1 39  ? 1.48536   -7.52875  -8.72744  1.000 41.67398  ? 46  ARG   A NH2 1 
ATOM   259  N N   . GLU   A 1 40  ? -1.36800  -10.21655 -13.39115 1.000 20.80462  ? 47  GLU   A N   1 
ATOM   260  C CA  . GLU   A 1 40  ? -0.54120  -9.78670  -14.51474 1.000 21.88315  ? 47  GLU   A CA  1 
ATOM   261  C C   . GLU   A 1 40  ? -1.14322  -10.21899 -15.84395 1.000 21.37144  ? 47  GLU   A C   1 
ATOM   262  O O   . GLU   A 1 40  ? -1.11728  -9.45589  -16.81876 1.000 22.49703  ? 47  GLU   A O   1 
ATOM   263  C CB  . GLU   A 1 40  ? 0.88520   -10.32945 -14.37583 1.000 21.77747  ? 47  GLU   A CB  1 
ATOM   264  C CG  . GLU   A 1 40  ? 1.64475   -9.81815  -13.15548 1.000 26.01624  ? 47  GLU   A CG  1 
ATOM   265  C CD  . GLU   A 1 40  ? 1.56134   -8.30838  -13.00561 1.000 36.76566  ? 47  GLU   A CD  1 
ATOM   266  O OE1 . GLU   A 1 40  ? 1.65873   -7.60482  -14.02970 1.000 33.10856  ? 47  GLU   A OE1 1 
ATOM   267  O OE2 . GLU   A 1 40  ? 1.39738   -7.82221  -11.86309 1.000 38.93825  ? 47  GLU   A OE2 1 
ATOM   268  N N   . LEU   A 1 41  ? -1.67866  -11.44241 -15.90970 1.000 19.66431  ? 48  LEU   A N   1 
ATOM   269  C CA  . LEU   A 1 41  ? -2.24615  -11.92323 -17.16638 1.000 22.66307  ? 48  LEU   A CA  1 
ATOM   270  C C   . LEU   A 1 41  ? -3.56386  -11.22823 -17.47801 1.000 22.68425  ? 48  LEU   A C   1 
ATOM   271  O O   . LEU   A 1 41  ? -3.85678  -10.93623 -18.64418 1.000 23.49026  ? 48  LEU   A O   1 
ATOM   272  C CB  . LEU   A 1 41  ? -2.44177  -13.43929 -17.12752 1.000 22.10266  ? 48  LEU   A CB  1 
ATOM   273  C CG  . LEU   A 1 41  ? -1.18023  -14.30073 -17.02411 1.000 22.23209  ? 48  LEU   A CG  1 
ATOM   274  C CD1 . LEU   A 1 41  ? -1.55341  -15.77179 -16.85696 1.000 23.72453  ? 48  LEU   A CD1 1 
ATOM   275  C CD2 . LEU   A 1 41  ? -0.24727  -14.10182 -18.21659 1.000 23.35881  ? 48  LEU   A CD2 1 
ATOM   276  N N   . ILE   A 1 42  ? -4.37539  -10.95965 -16.45184 1.000 20.75574  ? 49  ILE   A N   1 
ATOM   277  C CA  . ILE   A 1 42  ? -5.60603  -10.20947 -16.66973 1.000 21.05489  ? 49  ILE   A CA  1 
ATOM   278  C C   . ILE   A 1 42  ? -5.28803  -8.78344  -17.10115 1.000 22.60595  ? 49  ILE   A C   1 
ATOM   279  O O   . ILE   A 1 42  ? -5.98099  -8.21244  -17.94785 1.000 21.89081  ? 49  ILE   A O   1 
ATOM   280  C CB  . ILE   A 1 42  ? -6.49037  -10.24915 -15.41003 1.000 20.99125  ? 49  ILE   A CB  1 
ATOM   281  C CG1 . ILE   A 1 42  ? -7.06653  -11.65806 -15.22116 1.000 19.47648  ? 49  ILE   A CG1 1 
ATOM   282  C CG2 . ILE   A 1 42  ? -7.61249  -9.20112  -15.48670 1.000 22.91965  ? 49  ILE   A CG2 1 
ATOM   283  C CD1 . ILE   A 1 42  ? -7.73562  -11.86610 -13.87842 1.000 26.01235  ? 49  ILE   A CD1 1 
ATOM   284  N N   . SER   A 1 43  ? -4.22061  -8.19394  -16.55134 1.000 20.59192  ? 50  SER   A N   1 
ATOM   285  C CA  . SER   A 1 43  ? -3.84372  -6.84387  -16.96052 1.000 21.61302  ? 50  SER   A CA  1 
ATOM   286  C C   . SER   A 1 43  ? -3.36493  -6.82780  -18.40986 1.000 25.67176  ? 50  SER   A C   1 
ATOM   287  O O   . SER   A 1 43  ? -3.68846  -5.90615  -19.16913 1.000 23.71864  ? 50  SER   A O   1 
ATOM   288  C CB  . SER   A 1 43  ? -2.77387  -6.29157  -16.01390 1.000 28.31626  ? 50  SER   A CB  1 
ATOM   289  O OG  . SER   A 1 43  ? -2.17482  -5.11443  -16.53080 1.000 34.43420  ? 50  SER   A OG  1 
ATOM   290  N N   . ASN   A 1 44  ? -2.61132  -7.85136  -18.81953 1.000 20.51270  ? 51  ASN   A N   1 
ATOM   291  C CA  . ASN   A 1 44  ? -2.22055  -7.96956  -20.22101 1.000 22.91323  ? 51  ASN   A CA  1 
ATOM   292  C C   . ASN   A 1 44  ? -3.44698  -8.07925  -21.12063 1.000 20.02275  ? 51  ASN   A C   1 
ATOM   293  O O   . ASN   A 1 44  ? -3.52240  -7.42995  -22.16955 1.000 19.94531  ? 51  ASN   A O   1 
ATOM   294  C CB  . ASN   A 1 44  ? -1.31650  -9.18636  -20.39904 1.000 20.84840  ? 51  ASN   A CB  1 
ATOM   295  C CG  . ASN   A 1 44  ? 0.06802   -8.96978  -19.83082 1.000 30.26793  ? 51  ASN   A CG  1 
ATOM   296  O OD1 . ASN   A 1 44  ? 0.41763   -7.86563  -19.40021 1.000 28.30530  ? 51  ASN   A OD1 1 
ATOM   297  N ND2 . ASN   A 1 44  ? 0.86241   -10.03204 -19.80698 1.000 29.24291  ? 51  ASN   A ND2 1 
ATOM   298  N N   . SER   A 1 45  ? -4.40793  -8.91969  -20.73432 1.000 19.63707  ? 52  SER   A N   1 
ATOM   299  C CA  . SER   A 1 45  ? -5.63808  -9.05075  -21.51167 1.000 22.34639  ? 52  SER   A CA  1 
ATOM   300  C C   . SER   A 1 45  ? -6.36475  -7.71443  -21.61001 1.000 21.41034  ? 52  SER   A C   1 
ATOM   301  O O   . SER   A 1 45  ? -6.85868  -7.34361  -22.68376 1.000 20.15381  ? 52  SER   A O   1 
ATOM   302  C CB  . SER   A 1 45  ? -6.54807  -10.11187 -20.88520 1.000 20.24084  ? 52  SER   A CB  1 
ATOM   303  O OG  . SER   A 1 45  ? -6.00648  -11.41631 -21.02606 1.000 23.17284  ? 52  SER   A OG  1 
ATOM   304  N N   . SER   A 1 46  ? -6.43330  -6.97220  -20.49924 1.000 20.87984  ? 53  SER   A N   1 
ATOM   305  C CA  . SER   A 1 46  ? -7.07410  -5.66204  -20.52750 1.000 20.01662  ? 53  SER   A CA  1 
ATOM   306  C C   . SER   A 1 46  ? -6.35231  -4.71593  -21.48466 1.000 21.50089  ? 53  SER   A C   1 
ATOM   307  O O   . SER   A 1 46  ? -6.99704  -3.96618  -22.22858 1.000 21.47225  ? 53  SER   A O   1 
ATOM   308  C CB  . SER   A 1 46  ? -7.12905  -5.06857  -19.11614 1.000 21.38652  ? 53  SER   A CB  1 
ATOM   309  O OG  . SER   A 1 46  ? -7.69140  -3.76729  -19.13433 1.000 24.99650  ? 53  SER   A OG  1 
ATOM   310  N N   . ASP   A 1 47  ? -5.01258  -4.73818  -21.48719 1.000 21.22568  ? 54  ASP   A N   1 
ATOM   311  C CA  . ASP   A 1 47  ? -4.27163  -3.90096  -22.42676 1.000 21.33104  ? 54  ASP   A CA  1 
ATOM   312  C C   . ASP   A 1 47  ? -4.57049  -4.28413  -23.87266 1.000 26.13320  ? 54  ASP   A C   1 
ATOM   313  O O   . ASP   A 1 47  ? -4.67276  -3.41273  -24.74346 1.000 24.17318  ? 54  ASP   A O   1 
ATOM   314  C CB  . ASP   A 1 47  ? -2.76208  -3.98104  -22.17448 1.000 21.14099  ? 54  ASP   A CB  1 
ATOM   315  C CG  . ASP   A 1 47  ? -2.34327  -3.35891  -20.85184 1.000 37.72211  ? 54  ASP   A CG  1 
ATOM   316  O OD1 . ASP   A 1 47  ? -3.04468  -2.44850  -20.35938 1.000 33.18593  ? 54  ASP   A OD1 1 
ATOM   317  O OD2 . ASP   A 1 47  ? -1.25754  -3.72268  -20.34738 1.000 33.86219  ? 54  ASP   A OD2 1 
ATOM   318  N N   . ALA   A 1 48  ? -4.70068  -5.58465  -24.15190 1.000 21.25772  ? 55  ALA   A N   1 
ATOM   319  C CA  . ALA   A 1 48  ? -5.00001  -6.02341  -25.51328 1.000 21.13728  ? 55  ALA   A CA  1 
ATOM   320  C C   . ALA   A 1 48  ? -6.41329  -5.63867  -25.92393 1.000 21.22081  ? 55  ALA   A C   1 
ATOM   321  O O   . ALA   A 1 48  ? -6.66164  -5.32569  -27.09601 1.000 21.09985  ? 55  ALA   A O   1 
ATOM   322  C CB  . ALA   A 1 48  ? -4.81347  -7.53607  -25.63120 1.000 21.07301  ? 55  ALA   A CB  1 
ATOM   323  N N   . LEU   A 1 49  ? -7.34576  -5.66591  -24.97546 1.000 21.55927  ? 56  LEU   A N   1 
ATOM   324  C CA  . LEU   A 1 49  ? -8.70800  -5.23006  -25.25302 1.000 20.27944  ? 56  LEU   A CA  1 
ATOM   325  C C   . LEU   A 1 49  ? -8.76820  -3.72165  -25.47537 1.000 21.90225  ? 56  LEU   A C   1 
ATOM   326  O O   . LEU   A 1 49  ? -9.51009  -3.25013  -26.34621 1.000 23.10830  ? 56  LEU   A O   1 
ATOM   327  C CB  . LEU   A 1 49  ? -9.62105  -5.66826  -24.10493 1.000 22.53416  ? 56  LEU   A CB  1 
ATOM   328  C CG  . LEU   A 1 49  ? -9.90585  -7.17630  -24.07588 1.000 22.57924  ? 56  LEU   A CG  1 
ATOM   329  C CD1 . LEU   A 1 49  ? -10.33023 -7.62838  -22.68230 1.000 22.96000  ? 56  LEU   A CD1 1 
ATOM   330  C CD2 . LEU   A 1 49  ? -10.96434 -7.56507  -25.09335 1.000 22.84885  ? 56  LEU   A CD2 1 
ATOM   331  N N   . ASP   A 1 50  ? -7.98823  -2.94650  -24.71030 1.000 23.00194  ? 57  ASP   A N   1 
ATOM   332  C CA  . ASP   A 1 50  ? -7.90793  -1.50728  -24.95767 1.000 23.29565  ? 57  ASP   A CA  1 
ATOM   333  C C   . ASP   A 1 50  ? -7.44281  -1.21263  -26.37915 1.000 24.57161  ? 57  ASP   A C   1 
ATOM   334  O O   . ASP   A 1 50  ? -7.94138  -0.27922  -27.01969 1.000 23.70963  ? 57  ASP   A O   1 
ATOM   335  C CB  . ASP   A 1 50  ? -6.96138  -0.82666  -23.96330 1.000 22.65850  ? 57  ASP   A CB  1 
ATOM   336  C CG  . ASP   A 1 50  ? -7.50918  -0.77807  -22.54563 1.000 33.34093  ? 57  ASP   A CG  1 
ATOM   337  O OD1 . ASP   A 1 50  ? -8.70060  -1.08796  -22.32736 1.000 30.49842  ? 57  ASP   A OD1 1 
ATOM   338  O OD2 . ASP   A 1 50  ? -6.73371  -0.39943  -21.64332 1.000 30.95267  ? 57  ASP   A OD2 1 
ATOM   339  N N   . LYS   A 1 51  ? -6.47598  -1.98917  -26.88351 1.000 22.71624  ? 58  LYS   A N   1 
ATOM   340  C CA  . LYS   A 1 51  ? -5.90970  -1.70459  -28.20128 1.000 21.50416  ? 58  LYS   A CA  1 
ATOM   341  C C   . LYS   A 1 51  ? -6.92812  -1.93024  -29.30958 1.000 25.01008  ? 58  LYS   A C   1 
ATOM   342  O O   . LYS   A 1 51  ? -7.05854  -1.10174  -30.21921 1.000 27.23817  ? 58  LYS   A O   1 
ATOM   343  C CB  . LYS   A 1 51  ? -4.65522  -2.54706  -28.45219 1.000 24.37372  ? 58  LYS   A CB  1 
ATOM   344  C CG  . LYS   A 1 51  ? -3.49678  -2.27808  -27.50530 1.000 33.17808  ? 58  LYS   A CG  1 
ATOM   345  C CD  . LYS   A 1 51  ? -2.38110  -3.30010  -27.71517 1.000 36.58493  ? 58  LYS   A CD  1 
ATOM   346  C CE  . LYS   A 1 51  ? -1.06661  -2.84729  -27.09241 1.000 49.34033  ? 58  LYS   A CE  1 
ATOM   347  N NZ  . LYS   A 1 51  ? -1.22800  -2.45388  -25.66574 1.000 66.46978  ? 58  LYS   A NZ  1 
ATOM   348  N N   . ILE   A 1 52  ? -7.64651  -3.05402  -29.27235 1.000 22.00772  ? 59  ILE   A N   1 
ATOM   349  C CA  . ILE   A 1 52  ? -8.62036  -3.28136  -30.33310 1.000 23.51662  ? 59  ILE   A CA  1 
ATOM   350  C C   . ILE   A 1 52  ? -9.78777  -2.31492  -30.19213 1.000 28.38794  ? 59  ILE   A C   1 
ATOM   351  O O   . ILE   A 1 52  ? -10.37056 -1.89090  -31.19702 1.000 27.96971  ? 59  ILE   A O   1 
ATOM   352  C CB  . ILE   A 1 52  ? -9.08549  -4.75118  -30.36647 1.000 21.93913  ? 59  ILE   A CB  1 
ATOM   353  C CG1 . ILE   A 1 52  ? -9.93964  -5.01532  -31.61427 1.000 28.91377  ? 59  ILE   A CG1 1 
ATOM   354  C CG2 . ILE   A 1 52  ? -9.85507  -5.12533  -29.10608 1.000 22.07412  ? 59  ILE   A CG2 1 
ATOM   355  C CD1 . ILE   A 1 52  ? -9.21793  -4.75132  -32.93591 1.000 28.55513  ? 59  ILE   A CD1 1 
ATOM   356  N N   . ARG   A 1 53  ? -10.13315 -1.92289  -28.96196 1.000 24.79913  ? 60  ARG   A N   1 
ATOM   357  C CA  . ARG   A 1 53  ? -11.17790 -0.91751  -28.79480 1.000 25.09538  ? 60  ARG   A CA  1 
ATOM   358  C C   . ARG   A 1 53  ? -10.76765 0.40022   -29.43821 1.000 26.42775  ? 60  ARG   A C   1 
ATOM   359  O O   . ARG   A 1 53  ? -11.54219 1.00543   -30.18748 1.000 28.58126  ? 60  ARG   A O   1 
ATOM   360  C CB  . ARG   A 1 53  ? -11.50943 -0.70265  -27.31733 1.000 25.47879  ? 60  ARG   A CB  1 
ATOM   361  C CG  . ARG   A 1 53  ? -12.57383 0.37495   -27.16748 1.000 31.37955  ? 60  ARG   A CG  1 
ATOM   362  C CD  . ARG   A 1 53  ? -12.89081 0.74167   -25.74016 1.000 47.18034  ? 60  ARG   A CD  1 
ATOM   363  N NE  . ARG   A 1 53  ? -13.95963 -0.07209  -25.17949 1.000 55.82699  ? 60  ARG   A NE  1 
ATOM   364  C CZ  . ARG   A 1 53  ? -13.91131 -0.64864  -23.98785 1.000 55.60071  ? 60  ARG   A CZ  1 
ATOM   365  N NH1 . ARG   A 1 53  ? -12.85758 -0.51279  -23.19871 1.000 50.34754  ? 60  ARG   A NH1 1 
ATOM   366  N NH2 . ARG   A 1 53  ? -14.94905 -1.37342  -23.57490 1.000 43.35859  ? 60  ARG   A NH2 1 
ATOM   367  N N   . TYR   A 1 54  ? -9.53816  0.85300   -29.17280 1.000 25.16913  ? 61  TYR   A N   1 
ATOM   368  C CA  . TYR   A 1 54  ? -9.09287  2.12076   -29.74114 1.000 28.48228  ? 61  TYR   A CA  1 
ATOM   369  C C   . TYR   A 1 54  ? -9.08018  2.07260   -31.26369 1.000 26.49566  ? 61  TYR   A C   1 
ATOM   370  O O   . TYR   A 1 54  ? -9.49003  3.03307   -31.92759 1.000 30.24606  ? 61  TYR   A O   1 
ATOM   371  C CB  . TYR   A 1 54  ? -7.70428  2.48873   -29.22177 1.000 30.20502  ? 61  TYR   A CB  1 
ATOM   372  C CG  . TYR   A 1 54  ? -7.31420  3.88330   -29.63128 1.000 33.40643  ? 61  TYR   A CG  1 
ATOM   373  C CD1 . TYR   A 1 54  ? -7.88528  4.99152   -29.01430 1.000 34.15994  ? 61  TYR   A CD1 1 
ATOM   374  C CD2 . TYR   A 1 54  ? -6.42925  4.09799   -30.67907 1.000 34.68466  ? 61  TYR   A CD2 1 
ATOM   375  C CE1 . TYR   A 1 54  ? -7.54940  6.27110   -29.39932 1.000 34.97816  ? 61  TYR   A CE1 1 
ATOM   376  C CE2 . TYR   A 1 54  ? -6.09375  5.37385   -31.07758 1.000 33.97692  ? 61  TYR   A CE2 1 
ATOM   377  C CZ  . TYR   A 1 54  ? -6.65526  6.45765   -30.43388 1.000 43.08942  ? 61  TYR   A CZ  1 
ATOM   378  O OH  . TYR   A 1 54  ? -6.32331  7.73184   -30.82226 1.000 45.97050  ? 61  TYR   A OH  1 
ATOM   379  N N   . GLU   A 1 55  ? -8.60611  0.96424   -31.83598 1.000 26.79301  ? 62  GLU   A N   1 
ATOM   380  C CA  . GLU   A 1 55  ? -8.56400  0.85427   -33.29072 1.000 26.60243  ? 62  GLU   A CA  1 
ATOM   381  C C   . GLU   A 1 55  ? -9.96928  0.88805   -33.87921 1.000 32.57958  ? 62  GLU   A C   1 
ATOM   382  O O   . GLU   A 1 55  ? -10.19398 1.48407   -34.93911 1.000 34.13357  ? 62  GLU   A O   1 
ATOM   383  C CB  . GLU   A 1 55  ? -7.83164  -0.42634  -33.69111 1.000 31.70444  ? 62  GLU   A CB  1 
ATOM   384  C CG  . GLU   A 1 55  ? -6.31678  -0.27095  -33.70708 1.000 33.24712  ? 62  GLU   A CG  1 
ATOM   385  C CD  . GLU   A 1 55  ? -5.60886  -1.42073  -34.40200 1.000 58.77762  ? 62  GLU   A CD  1 
ATOM   386  O OE1 . GLU   A 1 55  ? -4.36375  -1.38333  -34.49728 1.000 54.95515  ? 62  GLU   A OE1 1 
ATOM   387  O OE2 . GLU   A 1 55  ? -6.29358  -2.36542  -34.84541 1.000 46.06000  ? 62  GLU   A OE2 1 
ATOM   388  N N   . SER   A 1 56  ? -10.93546 0.28007   -33.18581 1.000 29.79135  ? 63  SER   A N   1 
ATOM   389  C CA  . SER   A 1 56  ? -12.31000 0.24459   -33.67376 1.000 29.25584  ? 63  SER   A CA  1 
ATOM   390  C C   . SER   A 1 56  ? -12.99546 1.60419   -33.61214 1.000 31.73956  ? 63  SER   A C   1 
ATOM   391  O O   . SER   A 1 56  ? -14.05097 1.77514   -34.23038 1.000 32.80892  ? 63  SER   A O   1 
ATOM   392  C CB  . SER   A 1 56  ? -13.12591 -0.77371  -32.87430 1.000 32.77354  ? 63  SER   A CB  1 
ATOM   393  O OG  . SER   A 1 56  ? -13.45118 -0.26906  -31.58825 1.000 34.02796  ? 63  SER   A OG  1 
ATOM   394  N N   . LEU   A 1 57  ? -12.43146 2.57315   -32.88464 1.000 30.28442  ? 64  LEU   A N   1 
ATOM   395  C CA  . LEU   A 1 57  ? -13.07213 3.88102   -32.79465 1.000 34.03766  ? 64  LEU   A CA  1 
ATOM   396  C C   . LEU   A 1 57  ? -13.06285 4.60318   -34.13345 1.000 40.66906  ? 64  LEU   A C   1 
ATOM   397  O O   . LEU   A 1 57  ? -13.97570 5.38525   -34.42124 1.000 44.55213  ? 64  LEU   A O   1 
ATOM   398  C CB  . LEU   A 1 57  ? -12.38603 4.73903   -31.73104 1.000 34.48264  ? 64  LEU   A CB  1 
ATOM   399  C CG  . LEU   A 1 57  ? -12.53137 4.26519   -30.28421 1.000 32.49766  ? 64  LEU   A CG  1 
ATOM   400  C CD1 . LEU   A 1 57  ? -11.90096 5.27532   -29.33242 1.000 35.29679  ? 64  LEU   A CD1 1 
ATOM   401  C CD2 . LEU   A 1 57  ? -13.99290 4.03118   -29.93478 1.000 42.56202  ? 64  LEU   A CD2 1 
ATOM   402  N N   . THR   A 1 58  ? -12.04863 4.36002   -34.96048 1.000 34.09423  ? 65  THR   A N   1 
ATOM   403  C CA  . THR   A 1 58  ? -11.96247 4.98040   -36.27375 1.000 37.04876  ? 65  THR   A CA  1 
ATOM   404  C C   . THR   A 1 58  ? -12.20629 4.00552   -37.41497 1.000 50.24634  ? 65  THR   A C   1 
ATOM   405  O O   . THR   A 1 58  ? -12.36120 4.44599   -38.55901 1.000 42.08258  ? 65  THR   A O   1 
ATOM   406  C CB  . THR   A 1 58  ? -10.59062 5.64592   -36.46497 1.000 47.77414  ? 65  THR   A CB  1 
ATOM   407  O OG1 . THR   A 1 58  ? -9.55569  4.66233   -36.34107 1.000 46.71341  ? 65  THR   A OG1 1 
ATOM   408  C CG2 . THR   A 1 58  ? -10.38026 6.73476   -35.42490 1.000 47.07320  ? 65  THR   A CG2 1 
ATOM   409  N N   . ASP   A 1 59  ? -12.24626 2.70354   -37.13688 1.000 39.69767  ? 66  ASP   A N   1 
ATOM   410  C CA  . ASP   A 1 59  ? -12.48015 1.68346   -38.15642 1.000 43.91895  ? 66  ASP   A CA  1 
ATOM   411  C C   . ASP   A 1 59  ? -13.31600 0.58226   -37.51987 1.000 35.65963  ? 66  ASP   A C   1 
ATOM   412  O O   . ASP   A 1 59  ? -12.77920 -0.39581  -36.98489 1.000 33.26186  ? 66  ASP   A O   1 
ATOM   413  C CB  . ASP   A 1 59  ? -11.16112 1.13826   -38.70673 1.000 38.31569  ? 66  ASP   A CB  1 
ATOM   414  C CG  . ASP   A 1 59  ? -11.35962 0.10008   -39.80281 1.000 47.32912  ? 66  ASP   A CG  1 
ATOM   415  O OD1 . ASP   A 1 59  ? -12.51851 -0.16707  -40.18785 1.000 53.18828  ? 66  ASP   A OD1 1 
ATOM   416  O OD2 . ASP   A 1 59  ? -10.34606 -0.44404  -40.29236 1.000 45.99919  ? 66  ASP   A OD2 1 
ATOM   417  N N   . PRO   A 1 60  ? -14.64561 0.71249   -37.55405 1.000 46.64903  ? 67  PRO   A N   1 
ATOM   418  C CA  . PRO   A 1 60  ? -15.49651 -0.31532  -36.92999 1.000 42.52157  ? 67  PRO   A CA  1 
ATOM   419  C C   . PRO   A 1 60  ? -15.30184 -1.70700  -37.50854 1.000 38.73157  ? 67  PRO   A C   1 
ATOM   420  O O   . PRO   A 1 60  ? -15.55760 -2.69232  -36.80580 1.000 37.36447  ? 67  PRO   A O   1 
ATOM   421  C CB  . PRO   A 1 60  ? -16.92183 0.19314   -37.18379 1.000 41.80638  ? 67  PRO   A CB  1 
ATOM   422  C CG  . PRO   A 1 60  ? -16.79656 1.62736   -37.51038 1.000 45.88476  ? 67  PRO   A CG  1 
ATOM   423  C CD  . PRO   A 1 60  ? -15.39194 1.92344   -37.93115 1.000 43.51172  ? 67  PRO   A CD  1 
ATOM   424  N N   . SER   A 1 61  ? -14.85717 -1.82486  -38.76510 1.000 42.20029  ? 68  SER   A N   1 
ATOM   425  C CA  . SER   A 1 61  ? -14.66744 -3.14489  -39.35875 1.000 38.20401  ? 68  SER   A CA  1 
ATOM   426  C C   . SER   A 1 61  ? -13.61516 -3.96295  -38.62097 1.000 39.62485  ? 68  SER   A C   1 
ATOM   427  O O   . SER   A 1 61  ? -13.54444 -5.18200  -38.81129 1.000 34.64150  ? 68  SER   A O   1 
ATOM   428  C CB  . SER   A 1 61  ? -14.28181 -3.02057  -40.83406 1.000 41.95083  ? 68  SER   A CB  1 
ATOM   429  O OG  . SER   A 1 61  ? -12.97677 -2.48968  -40.98135 1.000 40.64989  ? 68  SER   A OG  1 
ATOM   430  N N   . LYS   A 1 62  ? -12.79858 -3.32775  -37.77832 1.000 32.46051  ? 69  LYS   A N   1 
ATOM   431  C CA  . LYS   A 1 62  ? -11.83414 -4.08249  -36.99142 1.000 27.54896  ? 69  LYS   A CA  1 
ATOM   432  C C   . LYS   A 1 62  ? -12.51181 -5.03905  -36.01876 1.000 29.48360  ? 69  LYS   A C   1 
ATOM   433  O O   . LYS   A 1 62  ? -11.86521 -5.97245  -35.53227 1.000 29.29798  ? 69  LYS   A O   1 
ATOM   434  C CB  . LYS   A 1 62  ? -10.91107 -3.12339  -36.24024 1.000 32.17244  ? 69  LYS   A CB  1 
ATOM   435  C CG  . LYS   A 1 62  ? -10.09006 -2.24358  -37.16806 1.000 44.54368  ? 69  LYS   A CG  1 
ATOM   436  C CD  . LYS   A 1 62  ? -8.60660  -2.43695  -36.94342 1.000 39.67417  ? 69  LYS   A CD  1 
ATOM   437  C CE  . LYS   A 1 62  ? -7.78965  -1.76308  -38.03232 1.000 41.97110  ? 69  LYS   A CE  1 
ATOM   438  N NZ  . LYS   A 1 62  ? -6.34598  -2.11092  -37.92015 1.000 60.34518  ? 69  LYS   A NZ  1 
ATOM   439  N N   . LEU   A 1 63  ? -13.79242 -4.82720  -35.71633 1.000 29.41434  ? 70  LEU   A N   1 
ATOM   440  C CA  . LEU   A 1 63  ? -14.55028 -5.72742  -34.85853 1.000 29.33472  ? 70  LEU   A CA  1 
ATOM   441  C C   . LEU   A 1 63  ? -15.38494 -6.72747  -35.64781 1.000 33.13112  ? 70  LEU   A C   1 
ATOM   442  O O   . LEU   A 1 63  ? -16.23649 -7.40257  -35.06169 1.000 35.03237  ? 70  LEU   A O   1 
ATOM   443  C CB  . LEU   A 1 63  ? -15.45419 -4.93286  -33.91227 1.000 33.66935  ? 70  LEU   A CB  1 
ATOM   444  C CG  . LEU   A 1 63  ? -14.75276 -4.00125  -32.92563 1.000 31.14345  ? 70  LEU   A CG  1 
ATOM   445  C CD1 . LEU   A 1 63  ? -15.77584 -3.25517  -32.07709 1.000 31.63539  ? 70  LEU   A CD1 1 
ATOM   446  C CD2 . LEU   A 1 63  ? -13.79537 -4.79877  -32.04834 1.000 29.77741  ? 70  LEU   A CD2 1 
ATOM   447  N N   . ASP   A 1 64  ? -15.16119 -6.84118  -36.95961 1.000 30.73092  ? 71  ASP   A N   1 
ATOM   448  C CA  . ASP   A 1 64  ? -15.87871 -7.84680  -37.73723 1.000 35.30345  ? 71  ASP   A CA  1 
ATOM   449  C C   . ASP   A 1 64  ? -15.54608 -9.25270  -37.25720 1.000 36.17678  ? 71  ASP   A C   1 
ATOM   450  O O   . ASP   A 1 64  ? -16.35114 -10.17622 -37.42475 1.000 35.29170  ? 71  ASP   A O   1 
ATOM   451  C CB  . ASP   A 1 64  ? -15.54488 -7.70174  -39.22147 1.000 32.95666  ? 71  ASP   A CB  1 
ATOM   452  C CG  . ASP   A 1 64  ? -16.25292 -6.52573  -39.86802 1.000 52.56413  ? 71  ASP   A CG  1 
ATOM   453  O OD1 . ASP   A 1 64  ? -17.15340 -5.93874  -39.23093 1.000 49.21518  ? 71  ASP   A OD1 1 
ATOM   454  O OD2 . ASP   A 1 64  ? -15.90204 -6.18327  -41.01590 1.000 45.57965  ? 71  ASP   A OD2 1 
ATOM   455  N N   . SER   A 1 65  ? -14.37062 -9.42799  -36.65769 1.000 35.52506  ? 72  SER   A N   1 
ATOM   456  C CA  . SER   A 1 65  ? -13.92504 -10.68956 -36.08707 1.000 27.50892  ? 72  SER   A CA  1 
ATOM   457  C C   . SER   A 1 65  ? -14.46996 -10.92997 -34.68684 1.000 37.12964  ? 72  SER   A C   1 
ATOM   458  O O   . SER   A 1 65  ? -14.01445 -11.85960 -34.01270 1.000 37.18621  ? 72  SER   A O   1 
ATOM   459  C CB  . SER   A 1 65  ? -12.39623 -10.72708 -36.05268 1.000 31.20937  ? 72  SER   A CB  1 
ATOM   460  O OG  . SER   A 1 65  ? -11.87395 -9.50365  -35.55181 1.000 29.85082  ? 72  SER   A OG  1 
ATOM   461  N N   . GLY   A 1 66  ? -15.41327 -10.11146 -34.22890 1.000 34.15345  ? 73  GLY   A N   1 
ATOM   462  C CA  . GLY   A 1 66  ? -15.95954 -10.26370 -32.89495 1.000 36.33443  ? 73  GLY   A CA  1 
ATOM   463  C C   . GLY   A 1 66  ? -16.19666 -8.93682  -32.20431 1.000 38.35134  ? 73  GLY   A C   1 
ATOM   464  O O   . GLY   A 1 66  ? -15.25502 -8.17463  -31.97226 1.000 29.87749  ? 73  GLY   A O   1 
ATOM   465  N N   . LYS   A 1 67  ? -17.45886 -8.64793  -31.88067 1.000 29.67263  ? 74  LYS   A N   1 
ATOM   466  C CA  . LYS   A 1 67  ? -17.81281 -7.38549  -31.24146 1.000 30.79406  ? 74  LYS   A CA  1 
ATOM   467  C C   . LYS   A 1 67  ? -17.56774 -7.40866  -29.73827 1.000 33.18328  ? 74  LYS   A C   1 
ATOM   468  O O   . LYS   A 1 67  ? -17.35034 -6.35219  -29.13485 1.000 35.72952  ? 74  LYS   A O   1 
ATOM   469  C CB  . LYS   A 1 67  ? -19.28429 -7.06662  -31.50591 1.000 31.25692  ? 74  LYS   A CB  1 
ATOM   470  C CG  . LYS   A 1 67  ? -19.62668 -6.82061  -32.96374 1.000 44.09947  ? 74  LYS   A CG  1 
ATOM   471  C CD  . LYS   A 1 67  ? -20.05150 -5.38270  -33.20271 1.000 53.30518  ? 74  LYS   A CD  1 
ATOM   472  C CE  . LYS   A 1 67  ? -20.41851 -5.15194  -34.65752 1.000 65.12383  ? 74  LYS   A CE  1 
ATOM   473  N NZ  . LYS   A 1 67  ? -19.28726 -4.56699  -35.42265 1.000 64.66587  ? 74  LYS   A NZ  1 
ATOM   474  N N   . GLU   A 1 68  ? -17.60337 -8.58834  -29.12392 1.000 26.87968  ? 75  GLU   A N   1 
ATOM   475  C CA  . GLU   A 1 68  ? -17.57163 -8.69725  -27.67220 1.000 29.52117  ? 75  GLU   A CA  1 
ATOM   476  C C   . GLU   A 1 68  ? -16.15005 -8.52283  -27.15466 1.000 26.46880  ? 75  GLU   A C   1 
ATOM   477  O O   . GLU   A 1 68  ? -15.20995 -9.11230  -27.69081 1.000 31.36751  ? 75  GLU   A O   1 
ATOM   478  C CB  . GLU   A 1 68  ? -18.12877 -10.05037 -27.23336 1.000 33.83049  ? 75  GLU   A CB  1 
ATOM   479  C CG  . GLU   A 1 68  ? -19.63947 -10.07779 -27.09607 1.000 43.95482  ? 75  GLU   A CG  1 
ATOM   480  C CD  . GLU   A 1 68  ? -20.31371 -10.77872 -28.25901 1.000 83.63096  ? 75  GLU   A CD  1 
ATOM   481  O OE1 . GLU   A 1 68  ? -21.43921 -11.29145 -28.07790 1.000 96.95740  ? 75  GLU   A OE1 1 
ATOM   482  O OE2 . GLU   A 1 68  ? -19.71628 -10.81642 -29.35551 1.000 72.31795  ? 75  GLU   A OE2 1 
ATOM   483  N N   . LEU   A 1 69  ? -15.99894 -7.71708  -26.10761 1.000 25.01291  ? 76  LEU   A N   1 
ATOM   484  C CA  . LEU   A 1 69  ? -14.70169 -7.43428  -25.49353 1.000 25.04087  ? 76  LEU   A CA  1 
ATOM   485  C C   . LEU   A 1 69  ? -14.75654 -7.96500  -24.06421 1.000 22.30930  ? 76  LEU   A C   1 
ATOM   486  O O   . LEU   A 1 69  ? -15.37118 -7.33841  -23.19425 1.000 24.68701  ? 76  LEU   A O   1 
ATOM   487  C CB  . LEU   A 1 69  ? -14.41241 -5.93615  -25.52708 1.000 26.42466  ? 76  LEU   A CB  1 
ATOM   488  C CG  . LEU   A 1 69  ? -14.28278 -5.28388  -26.90802 1.000 29.90549  ? 76  LEU   A CG  1 
ATOM   489  C CD1 . LEU   A 1 69  ? -13.83187 -3.83519  -26.77075 1.000 35.44189  ? 76  LEU   A CD1 1 
ATOM   490  C CD2 . LEU   A 1 69  ? -13.31839 -6.06039  -27.78918 1.000 27.97806  ? 76  LEU   A CD2 1 
ATOM   491  N N   . HIS   A 1 70  ? -14.12222 -9.11168  -23.80858 1.000 23.48468  ? 77  HIS   A N   1 
ATOM   492  C CA  . HIS   A 1 70  ? -14.27616 -9.74629  -22.50395 1.000 21.81204  ? 77  HIS   A CA  1 
ATOM   493  C C   . HIS   A 1 70  ? -13.07089 -10.62378 -22.19092 1.000 19.53666  ? 77  HIS   A C   1 
ATOM   494  O O   . HIS   A 1 70  ? -12.22848 -10.90253 -23.04951 1.000 21.30901  ? 77  HIS   A O   1 
ATOM   495  C CB  . HIS   A 1 70  ? -15.56485 -10.57610 -22.43858 1.000 21.43957  ? 77  HIS   A CB  1 
ATOM   496  C CG  . HIS   A 1 70  ? -15.61665 -11.69297 -23.43540 1.000 29.33018  ? 77  HIS   A CG  1 
ATOM   497  N ND1 . HIS   A 1 70  ? -16.62538 -11.81281 -24.36654 1.000 34.82918  ? 77  HIS   A ND1 1 
ATOM   498  C CD2 . HIS   A 1 70  ? -14.79408 -12.75038 -23.63447 1.000 29.05332  ? 77  HIS   A CD2 1 
ATOM   499  C CE1 . HIS   A 1 70  ? -16.41619 -12.88998 -25.10190 1.000 26.92592  ? 77  HIS   A CE1 1 
ATOM   500  N NE2 . HIS   A 1 70  ? -15.31140 -13.47625 -24.67940 1.000 29.11834  ? 77  HIS   A NE2 1 
ATOM   501  N N   . ILE   A 1 71  ? -13.02741 -11.07374 -20.93553 1.000 18.69124  ? 78  ILE   A N   1 
ATOM   502  C CA  . ILE   A 1 71  ? -12.00582 -11.96793 -20.40101 1.000 16.88653  ? 78  ILE   A CA  1 
ATOM   503  C C   . ILE   A 1 71  ? -12.71107 -13.14439 -19.74058 1.000 22.64822  ? 78  ILE   A C   1 
ATOM   504  O O   . ILE   A 1 71  ? -13.59394 -12.94410 -18.89948 1.000 21.31432  ? 78  ILE   A O   1 
ATOM   505  C CB  . ILE   A 1 71  ? -11.10177 -11.26043 -19.36854 1.000 19.50429  ? 78  ILE   A CB  1 
ATOM   506  C CG1 . ILE   A 1 71  ? -10.47098 -9.99448  -19.95416 1.000 22.23471  ? 78  ILE   A CG1 1 
ATOM   507  C CG2 . ILE   A 1 71  ? -10.05424 -12.23014 -18.81309 1.000 20.77541  ? 78  ILE   A CG2 1 
ATOM   508  C CD1 . ILE   A 1 71  ? -9.80859  -9.10827  -18.90378 1.000 22.35221  ? 78  ILE   A CD1 1 
ATOM   509  N N   . ASN   A 1 72  ? -12.31543 -14.36379 -20.10344 1.000 20.85911  ? 79  ASN   A N   1 
ATOM   510  C CA  . ASN   A 1 72  ? -12.85366 -15.57307 -19.49379 1.000 19.41199  ? 79  ASN   A CA  1 
ATOM   511  C C   . ASN   A 1 72  ? -11.73951 -16.31990 -18.76965 1.000 22.92994  ? 79  ASN   A C   1 
ATOM   512  O O   . ASN   A 1 72  ? -10.61977 -16.42574 -19.27797 1.000 23.82006  ? 79  ASN   A O   1 
ATOM   513  C CB  . ASN   A 1 72  ? -13.49424 -16.49505 -20.54223 1.000 21.45208  ? 79  ASN   A CB  1 
ATOM   514  C CG  . ASN   A 1 72  ? -14.69601 -15.86950 -21.22033 1.000 22.81814  ? 79  ASN   A CG  1 
ATOM   515  O OD1 . ASN   A 1 72  ? -15.41505 -15.07042 -20.62421 1.000 25.11599  ? 79  ASN   A OD1 1 
ATOM   516  N ND2 . ASN   A 1 72  ? -14.93365 -16.25192 -22.47301 1.000 27.34426  ? 79  ASN   A ND2 1 
ATOM   517  N N   . LEU   A 1 73  ? -12.05092 -16.83661 -17.58291 1.000 20.56991  ? 80  LEU   A N   1 
ATOM   518  C CA  . LEU   A 1 73  ? -11.14159 -17.67222 -16.80518 1.000 19.33573  ? 80  LEU   A CA  1 
ATOM   519  C C   . LEU   A 1 73  ? -11.72302 -19.07901 -16.76638 1.000 22.99285  ? 80  LEU   A C   1 
ATOM   520  O O   . LEU   A 1 73  ? -12.83364 -19.27261 -16.26536 1.000 20.57613  ? 80  LEU   A O   1 
ATOM   521  C CB  . LEU   A 1 73  ? -10.97765 -17.12580 -15.38472 1.000 17.97561  ? 80  LEU   A CB  1 
ATOM   522  C CG  . LEU   A 1 73  ? -10.59719 -15.64639 -15.29983 1.000 19.20635  ? 80  LEU   A CG  1 
ATOM   523  C CD1 . LEU   A 1 73  ? -10.45221 -15.21270 -13.85106 1.000 18.91065  ? 80  LEU   A CD1 1 
ATOM   524  C CD2 . LEU   A 1 73  ? -9.31266  -15.37334 -16.07580 1.000 22.22559  ? 80  LEU   A CD2 1 
ATOM   525  N N   . ILE   A 1 74  ? -10.99257 -20.05243 -17.29528 1.000 21.93310  ? 81  ILE   A N   1 
ATOM   526  C CA  . ILE   A 1 74  ? -11.50728 -21.40503 -17.47027 1.000 20.86731  ? 81  ILE   A CA  1 
ATOM   527  C C   . ILE   A 1 74  ? -10.58487 -22.38475 -16.75487 1.000 20.46749  ? 81  ILE   A C   1 
ATOM   528  O O   . ILE   A 1 74  ? -9.53589  -22.76115 -17.27515 1.000 23.50465  ? 81  ILE   A O   1 
ATOM   529  C CB  . ILE   A 1 74  ? -11.65450 -21.76922 -18.95921 1.000 20.12056  ? 81  ILE   A CB  1 
ATOM   530  C CG1 . ILE   A 1 74  ? -12.34584 -20.63030 -19.71450 1.000 23.77409  ? 81  ILE   A CG1 1 
ATOM   531  C CG2 . ILE   A 1 74  ? -12.42673 -23.08066 -19.11011 1.000 20.80378  ? 81  ILE   A CG2 1 
ATOM   532  C CD1 . ILE   A 1 74  ? -12.46526 -20.84965 -21.21000 1.000 28.97705  ? 81  ILE   A CD1 1 
ATOM   533  N N   . PRO   A 1 75  ? -10.96625 -22.85352 -15.56761 1.000 23.13274  ? 82  PRO   A N   1 
ATOM   534  C CA  . PRO   A 1 75  ? -10.20966 -23.93338 -14.92792 1.000 23.08582  ? 82  PRO   A CA  1 
ATOM   535  C C   . PRO   A 1 75  ? -10.66649 -25.29018 -15.44018 1.000 24.30389  ? 82  PRO   A C   1 
ATOM   536  O O   . PRO   A 1 75  ? -11.84719 -25.50252 -15.73188 1.000 26.72514  ? 82  PRO   A O   1 
ATOM   537  C CB  . PRO   A 1 75  ? -10.53830 -23.75762 -13.44021 1.000 26.53466  ? 82  PRO   A CB  1 
ATOM   538  C CG  . PRO   A 1 75  ? -11.92339 -23.17898 -13.43831 1.000 24.41619  ? 82  PRO   A CG  1 
ATOM   539  C CD  . PRO   A 1 75  ? -12.10072 -22.40414 -14.73974 1.000 26.91677  ? 82  PRO   A CD  1 
ATOM   540  N N   . ASN   A 1 76  ? -9.71232  -26.21534 -15.55284 1.000 25.97289  ? 83  ASN   A N   1 
ATOM   541  C CA  . ASN   A 1 76  ? -10.00281 -27.59483 -15.94363 1.000 25.97338  ? 83  ASN   A CA  1 
ATOM   542  C C   . ASN   A 1 76  ? -9.18757  -28.52204 -15.05403 1.000 32.65566  ? 83  ASN   A C   1 
ATOM   543  O O   . ASN   A 1 76  ? -7.97482  -28.65836 -15.24067 1.000 28.08111  ? 83  ASN   A O   1 
ATOM   544  C CB  . ASN   A 1 76  ? -9.68628  -27.84395 -17.41695 1.000 30.97383  ? 83  ASN   A CB  1 
ATOM   545  C CG  . ASN   A 1 76  ? -10.21636 -29.18433 -17.90856 1.000 33.57238  ? 83  ASN   A CG  1 
ATOM   546  O OD1 . ASN   A 1 76  ? -9.92367  -30.23258 -17.33082 1.000 33.35609  ? 83  ASN   A OD1 1 
ATOM   547  N ND2 . ASN   A 1 76  ? -10.99302 -29.15475 -18.98392 1.000 37.30364  ? 83  ASN   A ND2 1 
ATOM   548  N N   . LYS   A 1 77  ? -9.85640  -29.18174 -14.10859 1.000 31.13851  ? 84  LYS   A N   1 
ATOM   549  C CA  . LYS   A 1 77  ? -9.13823  -30.01517 -13.14919 1.000 37.12713  ? 84  LYS   A CA  1 
ATOM   550  C C   . LYS   A 1 77  ? -8.64298  -31.31374 -13.77400 1.000 36.86373  ? 84  LYS   A C   1 
ATOM   551  O O   . LYS   A 1 77  ? -7.63935  -31.87045 -13.31645 1.000 37.35943  ? 84  LYS   A O   1 
ATOM   552  C CB  . LYS   A 1 77  ? -10.02664 -30.30931 -11.94380 1.000 35.38296  ? 84  LYS   A CB  1 
ATOM   553  C CG  . LYS   A 1 77  ? -10.22648 -29.10885 -11.03099 1.000 39.74619  ? 84  LYS   A CG  1 
ATOM   554  C CD  . LYS   A 1 77  ? -10.92191 -29.50148 -9.73721  1.000 38.68731  ? 84  LYS   A CD  1 
ATOM   555  C CE  . LYS   A 1 77  ? -11.12940 -28.29317 -8.83790  1.000 39.23322  ? 84  LYS   A CE  1 
ATOM   556  N NZ  . LYS   A 1 77  ? -11.95461 -27.25586 -9.50841  1.000 53.47659  ? 84  LYS   A NZ  1 
ATOM   557  N N   . GLN   A 1 78  ? -9.32197  -31.81090 -14.81138 1.000 35.18129  ? 85  GLN   A N   1 
ATOM   558  C CA  . GLN   A 1 78  ? -8.88489  -33.05053 -15.44986 1.000 40.66385  ? 85  GLN   A CA  1 
ATOM   559  C C   . GLN   A 1 78  ? -7.57989  -32.85133 -16.21184 1.000 37.14136  ? 85  GLN   A C   1 
ATOM   560  O O   . GLN   A 1 78  ? -6.68585  -33.70455 -16.15713 1.000 43.14798  ? 85  GLN   A O   1 
ATOM   561  C CB  . GLN   A 1 78  ? -9.97137  -33.57848 -16.38829 1.000 46.84923  ? 85  GLN   A CB  1 
ATOM   562  C CG  . GLN   A 1 78  ? -11.15683 -34.22284 -15.68599 1.000 55.57348  ? 85  GLN   A CG  1 
ATOM   563  C CD  . GLN   A 1 78  ? -12.11522 -33.19958 -15.10616 1.000 82.02326  ? 85  GLN   A CD  1 
ATOM   564  O OE1 . GLN   A 1 78  ? -12.71354 -32.40795 -15.83659 1.000 75.39249  ? 85  GLN   A OE1 1 
ATOM   565  N NE2 . GLN   A 1 78  ? -12.26542 -33.21041 -13.78557 1.000 67.18999  ? 85  GLN   A NE2 1 
ATOM   566  N N   . ASP   A 1 79  ? -7.45952  -31.74095 -16.93691 1.000 36.89353  ? 86  ASP   A N   1 
ATOM   567  C CA  . ASP   A 1 79  ? -6.24405  -31.40071 -17.66313 1.000 37.79253  ? 86  ASP   A CA  1 
ATOM   568  C C   . ASP   A 1 79  ? -5.22430  -30.68182 -16.79126 1.000 33.46376  ? 86  ASP   A C   1 
ATOM   569  O O   . ASP   A 1 79  ? -4.07708  -30.51557 -17.21613 1.000 31.64381  ? 86  ASP   A O   1 
ATOM   570  C CB  . ASP   A 1 79  ? -6.58177  -30.51385 -18.86673 1.000 35.18599  ? 86  ASP   A CB  1 
ATOM   571  C CG  . ASP   A 1 79  ? -7.49692  -31.19956 -19.86127 1.000 51.04888  ? 86  ASP   A CG  1 
ATOM   572  O OD1 . ASP   A 1 79  ? -7.68173  -32.43225 -19.75680 1.000 47.59940  ? 86  ASP   A OD1 1 
ATOM   573  O OD2 . ASP   A 1 79  ? -8.04172  -30.49937 -20.74114 1.000 46.81990  ? 86  ASP   A OD2 1 
ATOM   574  N N   . ARG   A 1 80  ? -5.62554  -30.26838 -15.58995 1.000 32.22431  ? 87  ARG   A N   1 
ATOM   575  C CA  . ARG   A 1 80  ? -4.83384  -29.43411 -14.68738 1.000 26.09146  ? 87  ARG   A CA  1 
ATOM   576  C C   . ARG   A 1 80  ? -4.33590  -28.18070 -15.41151 1.000 26.13186  ? 87  ARG   A C   1 
ATOM   577  O O   . ARG   A 1 80  ? -3.14620  -27.84857 -15.41200 1.000 27.56816  ? 87  ARG   A O   1 
ATOM   578  C CB  . ARG   A 1 80  ? -3.68045  -30.22364 -14.06461 1.000 29.70732  ? 87  ARG   A CB  1 
ATOM   579  C CG  . ARG   A 1 80  ? -3.04903  -29.49652 -12.88536 1.000 31.39839  ? 87  ARG   A CG  1 
ATOM   580  C CD  . ARG   A 1 80  ? -1.59592  -29.82523 -12.70061 1.000 42.97547  ? 87  ARG   A CD  1 
ATOM   581  N NE  . ARG   A 1 80  ? -1.38044  -31.18217 -12.22729 1.000 46.13043  ? 87  ARG   A NE  1 
ATOM   582  C CZ  . ARG   A 1 80  ? -0.22875  -31.83016 -12.33158 1.000 54.66175  ? 87  ARG   A CZ  1 
ATOM   583  N NH1 . ARG   A 1 80  ? 0.83794   -31.26287 -12.87238 1.000 40.76023  ? 87  ARG   A NH1 1 
ATOM   584  N NH2 . ARG   A 1 80  ? -0.14157  -33.07380 -11.87270 1.000 46.62768  ? 87  ARG   A NH2 1 
ATOM   585  N N   . THR   A 1 81  ? -5.27348  -27.47648 -16.03893 1.000 24.97585  ? 88  THR   A N   1 
ATOM   586  C CA  . THR   A 1 81  ? -4.97131  -26.24859 -16.75839 1.000 21.54111  ? 88  THR   A CA  1 
ATOM   587  C C   . THR   A 1 81  ? -5.87431  -25.12393 -16.28049 1.000 26.64447  ? 88  THR   A C   1 
ATOM   588  O O   . THR   A 1 81  ? -7.03700  -25.34147 -15.92666 1.000 24.78037  ? 88  THR   A O   1 
ATOM   589  C CB  . THR   A 1 81  ? -5.13971  -26.40465 -18.28002 1.000 25.16983  ? 88  THR   A CB  1 
ATOM   590  O OG1 . THR   A 1 81  ? -6.48809  -26.79195 -18.57082 1.000 26.32540  ? 88  THR   A OG1 1 
ATOM   591  C CG2 . THR   A 1 81  ? -4.18602  -27.44675 -18.82284 1.000 26.63553  ? 88  THR   A CG2 1 
ATOM   592  N N   . LEU   A 1 82  ? -5.31936  -23.91381 -16.28059 1.000 20.74473  ? 89  LEU   A N   1 
ATOM   593  C CA  . LEU   A 1 82  ? -6.07913  -22.68177 -16.10731 1.000 19.70461  ? 89  LEU   A CA  1 
ATOM   594  C C   . LEU   A 1 82  ? -5.87963  -21.85010 -17.36459 1.000 23.73507  ? 89  LEU   A C   1 
ATOM   595  O O   . LEU   A 1 82  ? -4.74274  -21.53280 -17.72755 1.000 22.20101  ? 89  LEU   A O   1 
ATOM   596  C CB  . LEU   A 1 82  ? -5.63213  -21.90660 -14.86356 1.000 24.53198  ? 89  LEU   A CB  1 
ATOM   597  C CG  . LEU   A 1 82  ? -6.31295  -20.55023 -14.63012 1.000 22.01965  ? 89  LEU   A CG  1 
ATOM   598  C CD1 . LEU   A 1 82  ? -7.80641  -20.74323 -14.39953 1.000 22.85358  ? 89  LEU   A CD1 1 
ATOM   599  C CD2 . LEU   A 1 82  ? -5.67892  -19.85126 -13.43408 1.000 24.57534  ? 89  LEU   A CD2 1 
ATOM   600  N N   . THR   A 1 83  ? -6.97125  -21.52278 -18.04151 1.000 19.77365  ? 90  THR   A N   1 
ATOM   601  C CA  . THR   A 1 83  ? -6.90220  -20.79737 -19.30228 1.000 18.70086  ? 90  THR   A CA  1 
ATOM   602  C C   . THR   A 1 83  ? -7.48504  -19.40189 -19.12991 1.000 22.11003  ? 90  THR   A C   1 
ATOM   603  O O   . THR   A 1 83  ? -8.58621  -19.24659 -18.59005 1.000 23.07785  ? 90  THR   A O   1 
ATOM   604  C CB  . THR   A 1 83  ? -7.63917  -21.55166 -20.40748 1.000 22.48164  ? 90  THR   A CB  1 
ATOM   605  O OG1 . THR   A 1 83  ? -7.05746  -22.85000 -20.57141 1.000 27.29204  ? 90  THR   A OG1 1 
ATOM   606  C CG2 . THR   A 1 83  ? -7.52087  -20.79834 -21.70928 1.000 21.81205  ? 90  THR   A CG2 1 
ATOM   607  N N   . ILE   A 1 84  ? -6.73781  -18.39155 -19.57536 1.000 20.55555  ? 91  ILE   A N   1 
ATOM   608  C CA  . ILE   A 1 84  ? -7.18727  -17.00204 -19.57182 1.000 19.31860  ? 91  ILE   A CA  1 
ATOM   609  C C   . ILE   A 1 84  ? -7.42750  -16.62004 -21.02776 1.000 24.71398  ? 91  ILE   A C   1 
ATOM   610  O O   . ILE   A 1 84  ? -6.48268  -16.58151 -21.82674 1.000 22.42415  ? 91  ILE   A O   1 
ATOM   611  C CB  . ILE   A 1 84  ? -6.16795  -16.05728 -18.91347 1.000 20.46843  ? 91  ILE   A CB  1 
ATOM   612  C CG1 . ILE   A 1 84  ? -5.94955  -16.39471 -17.43164 1.000 24.83972  ? 91  ILE   A CG1 1 
ATOM   613  C CG2 . ILE   A 1 84  ? -6.62668  -14.60579 -19.05064 1.000 22.57554  ? 91  ILE   A CG2 1 
ATOM   614  C CD1 . ILE   A 1 84  ? -4.92608  -17.48422 -17.17583 1.000 28.85919  ? 91  ILE   A CD1 1 
ATOM   615  N N   . VAL   A 1 85  ? -8.68586  -16.35065 -21.37902 1.000 19.48540  ? 92  VAL   A N   1 
ATOM   616  C CA  . VAL   A 1 85  ? -9.09519  -16.03240 -22.74773 1.000 17.28220  ? 92  VAL   A CA  1 
ATOM   617  C C   . VAL   A 1 85  ? -9.51385  -14.57380 -22.80104 1.000 22.18575  ? 92  VAL   A C   1 
ATOM   618  O O   . VAL   A 1 85  ? -10.26959 -14.10967 -21.93805 1.000 23.10436  ? 92  VAL   A O   1 
ATOM   619  C CB  . VAL   A 1 85  ? -10.25826 -16.92308 -23.22656 1.000 21.78905  ? 92  VAL   A CB  1 
ATOM   620  C CG1 . VAL   A 1 85  ? -10.52825 -16.70552 -24.71356 1.000 28.74860  ? 92  VAL   A CG1 1 
ATOM   621  C CG2 . VAL   A 1 85  ? -9.98738  -18.38723 -22.94999 1.000 26.63105  ? 92  VAL   A CG2 1 
ATOM   622  N N   . ASP   A 1 86  ? -9.05443  -13.85775 -23.82620 1.000 21.92108  ? 93  ASP   A N   1 
ATOM   623  C CA  . ASP   A 1 86  ? -9.54640  -12.51218 -24.08707 1.000 19.49616  ? 93  ASP   A CA  1 
ATOM   624  C C   . ASP   A 1 86  ? -9.83347  -12.35349 -25.57343 1.000 23.86925  ? 93  ASP   A C   1 
ATOM   625  O O   . ASP   A 1 86  ? -9.31028  -13.08756 -26.41734 1.000 22.45658  ? 93  ASP   A O   1 
ATOM   626  C CB  . ASP   A 1 86  ? -8.56683  -11.42491 -23.60955 1.000 23.70142  ? 93  ASP   A CB  1 
ATOM   627  C CG  . ASP   A 1 86  ? -7.26587  -11.39756 -24.40194 1.000 25.50034  ? 93  ASP   A CG  1 
ATOM   628  O OD1 . ASP   A 1 86  ? -7.28443  -11.03781 -25.60250 1.000 26.43896  ? 93  ASP   A OD1 1 
ATOM   629  O OD2 . ASP   A 1 86  ? -6.21070  -11.69674 -23.80262 1.000 23.65934  ? 93  ASP   A OD2 1 
ATOM   630  N N   . THR   A 1 87  ? -10.68891 -11.38598 -25.88574 1.000 22.26829  ? 94  THR   A N   1 
ATOM   631  C CA  . THR   A 1 87  ? -11.01115 -11.04971 -27.26617 1.000 20.18257  ? 94  THR   A CA  1 
ATOM   632  C C   . THR   A 1 87  ? -10.33789 -9.74035  -27.66854 1.000 20.80977  ? 94  THR   A C   1 
ATOM   633  O O   . THR   A 1 87  ? -10.92068 -8.90498  -28.36572 1.000 22.99169  ? 94  THR   A O   1 
ATOM   634  C CB  . THR   A 1 87  ? -12.52467 -10.97747 -27.47310 1.000 23.78939  ? 94  THR   A CB  1 
ATOM   635  O OG1 . THR   A 1 87  ? -13.12303 -10.14886 -26.46761 1.000 24.22263  ? 94  THR   A OG1 1 
ATOM   636  C CG2 . THR   A 1 87  ? -13.13280 -12.37221 -27.38125 1.000 24.21267  ? 94  THR   A CG2 1 
ATOM   637  N N   . GLY   A 1 88  ? -9.09440  -9.55858  -27.22713 1.000 20.51467  ? 95  GLY   A N   1 
ATOM   638  C CA  . GLY   A 1 88  ? -8.32023  -8.37445  -27.53240 1.000 22.70569  ? 95  GLY   A CA  1 
ATOM   639  C C   . GLY   A 1 88  ? -7.75130  -8.39747  -28.93973 1.000 21.47662  ? 95  GLY   A C   1 
ATOM   640  O O   . GLY   A 1 88  ? -8.17651  -9.16465  -29.80769 1.000 22.89581  ? 95  GLY   A O   1 
ATOM   641  N N   . ILE   A 1 89  ? -6.76091  -7.52872  -29.16040 1.000 21.29670  ? 96  ILE   A N   1 
ATOM   642  C CA  . ILE   A 1 89  ? -6.21793  -7.33198  -30.50287 1.000 21.97255  ? 96  ILE   A CA  1 
ATOM   643  C C   . ILE   A 1 89  ? -5.47770  -8.56176  -31.02052 1.000 25.78926  ? 96  ILE   A C   1 
ATOM   644  O O   . ILE   A 1 89  ? -5.33183  -8.72384  -32.23679 1.000 25.05610  ? 96  ILE   A O   1 
ATOM   645  C CB  . ILE   A 1 89  ? -5.31145  -6.08272  -30.52753 1.000 23.25854  ? 96  ILE   A CB  1 
ATOM   646  C CG1 . ILE   A 1 89  ? -5.00602  -5.66124  -31.96930 1.000 27.11448  ? 96  ILE   A CG1 1 
ATOM   647  C CG2 . ILE   A 1 89  ? -4.03357  -6.30315  -29.71610 1.000 24.38626  ? 96  ILE   A CG2 1 
ATOM   648  C CD1 . ILE   A 1 89  ? -4.64507  -4.21358  -32.10643 1.000 26.27705  ? 96  ILE   A CD1 1 
ATOM   649  N N   . GLY   A 1 90  ? -5.02253  -9.44478  -30.14350 1.000 25.37997  ? 97  GLY   A N   1 
ATOM   650  C CA  . GLY   A 1 90  ? -4.26604  -10.60096 -30.58162 1.000 23.23240  ? 97  GLY   A CA  1 
ATOM   651  C C   . GLY   A 1 90  ? -2.85305  -10.22191 -30.99320 1.000 23.13356  ? 97  GLY   A C   1 
ATOM   652  O O   . GLY   A 1 90  ? -2.40349  -9.08440  -30.86353 1.000 24.77630  ? 97  GLY   A O   1 
ATOM   653  N N   . MET   A 1 91  ? -2.14120  -11.22148 -31.49901 1.000 22.33292  ? 98  MET   A N   1 
ATOM   654  C CA  . MET   A 1 91  ? -0.73717  -11.07002 -31.83980 1.000 24.04255  ? 98  MET   A CA  1 
ATOM   655  C C   . MET   A 1 91  ? -0.47589  -11.71237 -33.19059 1.000 23.86374  ? 98  MET   A C   1 
ATOM   656  O O   . MET   A 1 91  ? -1.00174  -12.78888 -33.48072 1.000 22.96489  ? 98  MET   A O   1 
ATOM   657  C CB  . MET   A 1 91  ? 0.15547   -11.71669 -30.76754 1.000 27.12027  ? 98  MET   A CB  1 
ATOM   658  C CG  . MET   A 1 91  ? 0.43281   -10.82784 -29.56944 1.000 27.39279  ? 98  MET   A CG  1 
ATOM   659  S SD  . MET   A 1 91  ? 1.26761   -11.67752 -28.20650 1.000 29.36314  ? 98  MET   A SD  1 
ATOM   660  C CE  . MET   A 1 91  ? 0.16661   -13.04893 -27.87838 1.000 26.64260  ? 98  MET   A CE  1 
ATOM   661  N N   . THR   A 1 92  ? 0.32738   -11.04422 -34.01651 1.000 24.59489  ? 99  THR   A N   1 
ATOM   662  C CA  . THR   A 1 92  ? 0.82090   -11.66814 -35.23344 1.000 23.93992  ? 99  THR   A CA  1 
ATOM   663  C C   . THR   A 1 92  ? 1.90641   -12.68978 -34.89941 1.000 27.43530  ? 99  THR   A C   1 
ATOM   664  O O   . THR   A 1 92  ? 2.45080   -12.72279 -33.79219 1.000 27.08620  ? 99  THR   A O   1 
ATOM   665  C CB  . THR   A 1 92  ? 1.39342   -10.62716 -36.19626 1.000 28.74656  ? 99  THR   A CB  1 
ATOM   666  O OG1 . THR   A 1 92  ? 2.55306   -10.02697 -35.60737 1.000 29.15690  ? 99  THR   A OG1 1 
ATOM   667  C CG2 . THR   A 1 92  ? 0.36940   -9.54476  -36.51086 1.000 28.58265  ? 99  THR   A CG2 1 
ATOM   668  N N   . LYS   A 1 93  ? 2.22833   -13.52708 -35.89022 1.000 27.07214  ? 100 LYS   A N   1 
ATOM   669  C CA  . LYS   A 1 93  ? 3.33301   -14.46779 -35.73009 1.000 24.16630  ? 100 LYS   A CA  1 
ATOM   670  C C   . LYS   A 1 93  ? 4.61805   -13.73994 -35.36662 1.000 25.20848  ? 100 LYS   A C   1 
ATOM   671  O O   . LYS   A 1 93  ? 5.36933   -14.18543 -34.48779 1.000 24.70989  ? 100 LYS   A O   1 
ATOM   672  C CB  . LYS   A 1 93  ? 3.52901   -15.27463 -37.01394 1.000 25.34922  ? 100 LYS   A CB  1 
ATOM   673  C CG  . LYS   A 1 93  ? 4.56065   -16.38702 -36.86461 1.000 28.43566  ? 100 LYS   A CG  1 
ATOM   674  C CD  . LYS   A 1 93  ? 4.78846   -17.11780 -38.18423 1.000 27.51223  ? 100 LYS   A CD  1 
ATOM   675  C CE  . LYS   A 1 93  ? 5.69574   -18.31754 -37.98095 1.000 36.58146  ? 100 LYS   A CE  1 
ATOM   676  N NZ  . LYS   A 1 93  ? 6.37143   -18.73491 -39.23728 1.000 36.35940  ? 100 LYS   A NZ  1 
ATOM   677  N N   . ALA   A 1 94  ? 4.87829   -12.61021 -36.03141 1.000 27.02781  ? 101 ALA   A N   1 
ATOM   678  C CA  . ALA   A 1 94  ? 6.06533   -11.81606 -35.73307 1.000 28.34192  ? 101 ALA   A CA  1 
ATOM   679  C C   . ALA   A 1 94  ? 6.06584   -11.34310 -34.28553 1.000 30.17037  ? 101 ALA   A C   1 
ATOM   680  O O   . ALA   A 1 94  ? 7.10089   -11.40077 -33.61153 1.000 28.07914  ? 101 ALA   A O   1 
ATOM   681  C CB  . ALA   A 1 94  ? 6.15100   -10.62454 -36.68677 1.000 28.60781  ? 101 ALA   A CB  1 
ATOM   682  N N   . ASP   A 1 95  ? 4.91587   -10.86571 -33.79293 1.000 27.21312  ? 102 ASP   A N   1 
ATOM   683  C CA  . ASP   A 1 95  ? 4.82141   -10.46229 -32.39015 1.000 29.14268  ? 102 ASP   A CA  1 
ATOM   684  C C   . ASP   A 1 95  ? 5.08541   -11.62850 -31.45081 1.000 28.72965  ? 102 ASP   A C   1 
ATOM   685  O O   . ASP   A 1 95  ? 5.80657   -11.47597 -30.45665 1.000 25.89398  ? 102 ASP   A O   1 
ATOM   686  C CB  . ASP   A 1 95  ? 3.45003   -9.85390  -32.08242 1.000 28.31575  ? 102 ASP   A CB  1 
ATOM   687  C CG  . ASP   A 1 95  ? 3.14106   -8.63346  -32.91790 1.000 50.52036  ? 102 ASP   A CG  1 
ATOM   688  O OD1 . ASP   A 1 95  ? 1.96417   -8.47971  -33.32119 1.000 58.09845  ? 102 ASP   A OD1 1 
ATOM   689  O OD2 . ASP   A 1 95  ? 4.06514   -7.82412  -33.15523 1.000 50.28496  ? 102 ASP   A OD2 1 
ATOM   690  N N   . LEU   A 1 96  ? 4.49616   -12.79610 -31.73102 1.000 25.54559  ? 103 LEU   A N   1 
ATOM   691  C CA  . LEU   A 1 96  ? 4.72142   -13.95571 -30.87165 1.000 27.49574  ? 103 LEU   A CA  1 
ATOM   692  C C   . LEU   A 1 96  ? 6.20428   -14.25531 -30.73677 1.000 29.59406  ? 103 LEU   A C   1 
ATOM   693  O O   . LEU   A 1 96  ? 6.71794   -14.44131 -29.62621 1.000 25.62640  ? 103 LEU   A O   1 
ATOM   694  C CB  . LEU   A 1 96  ? 4.00405   -15.18594 -31.42102 1.000 31.90450  ? 103 LEU   A CB  1 
ATOM   695  C CG  . LEU   A 1 96  ? 2.53976   -15.42228 -31.09396 1.000 32.34099  ? 103 LEU   A CG  1 
ATOM   696  C CD1 . LEU   A 1 96  ? 2.08709   -16.68335 -31.81411 1.000 27.57663  ? 103 LEU   A CD1 1 
ATOM   697  C CD2 . LEU   A 1 96  ? 2.32861   -15.53564 -29.58383 1.000 21.98109  ? 103 LEU   A CD2 1 
ATOM   698  N N   . ILE   A 1 97  ? 6.90802   -14.31184 -31.86751 1.000 24.79313  ? 104 ILE   A N   1 
ATOM   699  C CA  . ILE   A 1 97  ? 8.32618   -14.64251 -31.84495 1.000 25.68611  ? 104 ILE   A CA  1 
ATOM   700  C C   . ILE   A 1 97  ? 9.11417   -13.56401 -31.11249 1.000 29.01106  ? 104 ILE   A C   1 
ATOM   701  O O   . ILE   A 1 97  ? 10.05448  -13.85805 -30.36353 1.000 27.76156  ? 104 ILE   A O   1 
ATOM   702  C CB  . ILE   A 1 97  ? 8.83222   -14.84204 -33.28266 1.000 27.54043  ? 104 ILE   A CB  1 
ATOM   703  C CG1 . ILE   A 1 97  ? 8.19741   -16.09592 -33.89216 1.000 25.42514  ? 104 ILE   A CG1 1 
ATOM   704  C CG2 . ILE   A 1 97  ? 10.35958  -14.92796 -33.29701 1.000 24.65661  ? 104 ILE   A CG2 1 
ATOM   705  C CD1 . ILE   A 1 97  ? 8.38711   -16.21600 -35.40137 1.000 27.94438  ? 104 ILE   A CD1 1 
ATOM   706  N N   . ASN   A 1 98  ? 8.73774   -12.30250 -31.30841 1.000 24.67714  ? 105 ASN   A N   1 
ATOM   707  C CA  . ASN   A 1 98  ? 9.39841   -11.16859 -30.66674 1.000 25.19251  ? 105 ASN   A CA  1 
ATOM   708  C C   . ASN   A 1 98  ? 8.85171   -10.96854 -29.24839 1.000 24.06432  ? 105 ASN   A C   1 
ATOM   709  O O   . ASN   A 1 98  ? 8.29340   -9.93068  -28.89393 1.000 24.34441  ? 105 ASN   A O   1 
ATOM   710  C CB  . ASN   A 1 98  ? 9.22339   -9.92189  -31.52493 1.000 32.37634  ? 105 ASN   A CB  1 
ATOM   711  C CG  . ASN   A 1 98  ? 10.10237  -8.77109  -31.07625 1.000 48.15769  ? 105 ASN   A CG  1 
ATOM   712  O OD1 . ASN   A 1 98  ? 10.99350  -8.93664  -30.24015 1.000 41.85762  ? 105 ASN   A OD1 1 
ATOM   713  N ND2 . ASN   A 1 98  ? 9.85126   -7.59143  -31.62980 1.000 40.89956  ? 105 ASN   A ND2 1 
ATOM   714  N N   . ASN   A 1 99  ? 9.00203   -12.02080 -28.44235 1.000 22.73574  ? 106 ASN   A N   1 
ATOM   715  C CA  . ASN   A 1 99  ? 8.69345   -11.98582 -27.01079 1.000 23.92238  ? 106 ASN   A CA  1 
ATOM   716  C C   . ASN   A 1 99  ? 7.25200   -11.55788 -26.73556 1.000 24.85081  ? 106 ASN   A C   1 
ATOM   717  O O   . ASN   A 1 99  ? 6.98137   -10.78456 -25.81398 1.000 22.84684  ? 106 ASN   A O   1 
ATOM   718  C CB  . ASN   A 1 99  ? 9.69355   -11.09508 -26.26925 1.000 26.12719  ? 106 ASN   A CB  1 
ATOM   719  C CG  . ASN   A 1 99  ? 11.12616  -11.57229 -26.44355 1.000 22.03091  ? 106 ASN   A CG  1 
ATOM   720  O OD1 . ASN   A 1 99  ? 11.42447  -12.74683 -26.22904 1.000 28.25436  ? 106 ASN   A OD1 1 
ATOM   721  N ND2 . ASN   A 1 99  ? 12.01668  -10.66862 -26.84156 1.000 25.89296  ? 106 ASN   A ND2 1 
ATOM   722  N N   . LEU   A 1 100 ? 6.31953   -12.08785 -27.53263 1.000 23.96833  ? 107 LEU   A N   1 
ATOM   723  C CA  . LEU   A 1 100 ? 4.88128   -11.90674 -27.32255 1.000 25.31581  ? 107 LEU   A CA  1 
ATOM   724  C C   . LEU   A 1 100 ? 4.50896   -10.42902 -27.19948 1.000 29.33924  ? 107 LEU   A C   1 
ATOM   725  O O   . LEU   A 1 100 ? 3.73710   -10.02249 -26.32857 1.000 24.85208  ? 107 LEU   A O   1 
ATOM   726  C CB  . LEU   A 1 100 ? 4.40628   -12.70999 -26.10630 1.000 21.56596  ? 107 LEU   A CB  1 
ATOM   727  C CG  . LEU   A 1 100 ? 4.74253   -14.20564 -26.19366 1.000 25.69417  ? 107 LEU   A CG  1 
ATOM   728  C CD1 . LEU   A 1 100 ? 5.95952   -14.56180 -25.34203 1.000 28.12923  ? 107 LEU   A CD1 1 
ATOM   729  C CD2 . LEU   A 1 100 ? 3.55013   -15.05781 -25.80587 1.000 32.90770  ? 107 LEU   A CD2 1 
ATOM   730  N N   . GLY   A 1 101 ? 5.06348   -9.61917  -28.10171 1.000 22.16970  ? 108 GLY   A N   1 
ATOM   731  C CA  . GLY   A 1 101 ? 4.72860   -8.20902  -28.16576 1.000 26.05406  ? 108 GLY   A CA  1 
ATOM   732  C C   . GLY   A 1 101 ? 5.30906   -7.34138  -27.07059 1.000 29.68497  ? 108 GLY   A C   1 
ATOM   733  O O   . GLY   A 1 101 ? 4.89016   -6.18710  -26.92996 1.000 31.02689  ? 108 GLY   A O   1 
ATOM   734  N N   . THR   A 1 102 ? 6.25820   -7.85045  -26.29283 1.000 25.37943  ? 109 THR   A N   1 
ATOM   735  C CA  . THR   A 1 102 ? 6.83283   -7.11368  -25.17765 1.000 27.80799  ? 109 THR   A CA  1 
ATOM   736  C C   . THR   A 1 102 ? 8.22248   -6.60097  -25.52952 1.000 29.83803  ? 109 THR   A C   1 
ATOM   737  O O   . THR   A 1 102 ? 8.88921   -7.10762  -26.43519 1.000 30.18396  ? 109 THR   A O   1 
ATOM   738  C CB  . THR   A 1 102 ? 6.92597   -7.99094  -23.92615 1.000 27.18408  ? 109 THR   A CB  1 
ATOM   739  O OG1 . THR   A 1 102 ? 7.93803   -8.98934  -24.11793 1.000 27.29602  ? 109 THR   A OG1 1 
ATOM   740  C CG2 . THR   A 1 102 ? 5.59529   -8.67690  -23.65131 1.000 29.11704  ? 109 THR   A CG2 1 
ATOM   741  N N   . ILE   A 1 103 ? 8.65271   -5.58200  -24.78518 1.000 23.63604  ? 110 ILE   A N   1 
ATOM   742  C CA  . ILE   A 1 103 ? 10.02268  -5.08356  -24.83391 1.000 23.42394  ? 110 ILE   A CA  1 
ATOM   743  C C   . ILE   A 1 103 ? 10.85497  -5.84404  -23.80723 1.000 25.58923  ? 110 ILE   A C   1 
ATOM   744  O O   . ILE   A 1 103 ? 11.47029  -5.25289  -22.91353 1.000 27.07850  ? 110 ILE   A O   1 
ATOM   745  C CB  . ILE   A 1 103 ? 10.05653  -3.55505  -24.62125 1.000 31.35271  ? 110 ILE   A CB  1 
ATOM   746  C CG1 . ILE   A 1 103 ? 9.03072   -3.09729  -23.57171 1.000 35.41276  ? 110 ILE   A CG1 1 
ATOM   747  C CG2 . ILE   A 1 103 ? 9.78349   -2.84260  -25.93455 1.000 36.04447  ? 110 ILE   A CG2 1 
ATOM   748  C CD1 . ILE   A 1 103 ? 9.39482   -3.29748  -22.11230 1.000 45.07653  ? 110 ILE   A CD1 1 
ATOM   749  N N   . ALA   A 1 104 ? 10.89718  -7.16945  -23.95418 1.000 27.76978  ? 111 ALA   A N   1 
ATOM   750  C CA  . ALA   A 1 104 ? 11.35575  -8.02448  -22.86599 1.000 32.70128  ? 111 ALA   A CA  1 
ATOM   751  C C   . ALA   A 1 104 ? 12.83278  -7.82598  -22.54192 1.000 24.41941  ? 111 ALA   A C   1 
ATOM   752  O O   . ALA   A 1 104 ? 13.22258  -7.97144  -21.37882 1.000 27.31198  ? 111 ALA   A O   1 
ATOM   753  C CB  . ALA   A 1 104 ? 11.07195  -9.48989  -23.19837 1.000 30.51139  ? 111 ALA   A CB  1 
ATOM   754  N N   . LYS   A 1 105 ? 13.66709  -7.49798  -23.53247 1.000 25.67229  ? 112 LYS   A N   1 
ATOM   755  C CA  . LYS   A 1 105 ? 15.09023  -7.31194  -23.24927 1.000 27.21453  ? 112 LYS   A CA  1 
ATOM   756  C C   . LYS   A 1 105 ? 15.32266  -6.09630  -22.35824 1.000 34.45695  ? 112 LYS   A C   1 
ATOM   757  O O   . LYS   A 1 105 ? 15.96470  -6.19882  -21.30627 1.000 29.50286  ? 112 LYS   A O   1 
ATOM   758  C CB  . LYS   A 1 105 ? 15.88865  -7.18306  -24.54600 1.000 29.74805  ? 112 LYS   A CB  1 
ATOM   759  C CG  . LYS   A 1 105 ? 17.39501  -7.15466  -24.32228 1.000 47.26369  ? 112 LYS   A CG  1 
ATOM   760  C CD  . LYS   A 1 105 ? 18.16452  -7.05776  -25.63045 1.000 38.30701  ? 112 LYS   A CD  1 
ATOM   761  C CE  . LYS   A 1 105 ? 19.57846  -6.54956  -25.39737 1.000 58.31926  ? 112 LYS   A CE  1 
ATOM   762  N NZ  . LYS   A 1 105 ? 20.57684  -7.29299  -26.21516 1.000 63.16535  ? 112 LYS   A NZ  1 
ATOM   763  N N   . SER   A 1 106 ? 14.81872  -4.92956  -22.76577 1.000 31.67784  ? 113 SER   A N   1 
ATOM   764  C CA  . SER   A 1 106 ? 14.99173  -3.74489  -21.93384 1.000 32.84637  ? 113 SER   A CA  1 
ATOM   765  C C   . SER   A 1 106 ? 14.15287  -3.82835  -20.66667 1.000 29.54043  ? 113 SER   A C   1 
ATOM   766  O O   . SER   A 1 106 ? 14.56019  -3.30508  -19.62351 1.000 37.59413  ? 113 SER   A O   1 
ATOM   767  C CB  . SER   A 1 106 ? 14.64279  -2.48232  -22.72021 1.000 36.24623  ? 113 SER   A CB  1 
ATOM   768  O OG  . SER   A 1 106 ? 13.31280  -2.53450  -23.19993 1.000 37.33223  ? 113 SER   A OG  1 
ATOM   769  N N   . GLY   A 1 107 ? 12.98709  -4.47687  -20.73665 1.000 26.99985  ? 114 GLY   A N   1 
ATOM   770  C CA  . GLY   A 1 107 ? 12.16123  -4.62518  -19.54942 1.000 33.37173  ? 114 GLY   A CA  1 
ATOM   771  C C   . GLY   A 1 107 ? 12.81108  -5.49852  -18.49424 1.000 31.24481  ? 114 GLY   A C   1 
ATOM   772  O O   . GLY   A 1 107 ? 12.77826  -5.17623  -17.30419 1.000 33.37873  ? 114 GLY   A O   1 
ATOM   773  N N   . THR   A 1 108 ? 13.40735  -6.61846  -18.91276 1.000 28.80580  ? 115 THR   A N   1 
ATOM   774  C CA  . THR   A 1 108 ? 14.15267  -7.45238  -17.97361 1.000 31.46836  ? 115 THR   A CA  1 
ATOM   775  C C   . THR   A 1 108 ? 15.30326  -6.68424  -17.33983 1.000 33.88082  ? 115 THR   A C   1 
ATOM   776  O O   . THR   A 1 108 ? 15.53392  -6.78703  -16.12907 1.000 33.66686  ? 115 THR   A O   1 
ATOM   777  C CB  . THR   A 1 108 ? 14.67227  -8.70330  -18.67834 1.000 33.59999  ? 115 THR   A CB  1 
ATOM   778  O OG1 . THR   A 1 108 ? 13.56280  -9.44468  -19.19810 1.000 28.41840  ? 115 THR   A OG1 1 
ATOM   779  C CG2 . THR   A 1 108 ? 15.46571  -9.57381  -17.71935 1.000 30.92622  ? 115 THR   A CG2 1 
ATOM   780  N N   . LYS   A 1 109 ? 16.03998  -5.91246  -18.14255 1.000 33.61883  ? 116 LYS   A N   1 
ATOM   781  C CA  . LYS   A 1 109 ? 17.13364  -5.11051  -17.60383 1.000 35.77360  ? 116 LYS   A CA  1 
ATOM   782  C C   . LYS   A 1 109 ? 16.62825  -4.16029  -16.52285 1.000 42.35138  ? 116 LYS   A C   1 
ATOM   783  O O   . LYS   A 1 109 ? 17.19180  -4.09417  -15.42540 1.000 39.82107  ? 116 LYS   A O   1 
ATOM   784  C CB  . LYS   A 1 109 ? 17.81965  -4.34890  -18.74116 1.000 33.46136  ? 116 LYS   A CB  1 
ATOM   785  C CG  . LYS   A 1 109 ? 18.85767  -3.32311  -18.31485 1.000 49.59426  ? 116 LYS   A CG  1 
ATOM   786  C CD  . LYS   A 1 109 ? 19.27036  -2.46363  -19.50389 1.000 60.90681  ? 116 LYS   A CD  1 
ATOM   787  C CE  . LYS   A 1 109 ? 20.62041  -1.79330  -19.28878 1.000 60.17523  ? 116 LYS   A CE  1 
ATOM   788  N NZ  . LYS   A 1 109 ? 21.03614  -1.80311  -17.86240 1.000 65.12141  ? 116 LYS   A NZ  1 
ATOM   789  N N   . ALA   A 1 110 ? 15.54169  -3.43840  -16.80449 1.000 36.93853  ? 117 ALA   A N   1 
ATOM   790  C CA  . ALA   A 1 110 ? 14.98654  -2.52080  -15.81224 1.000 37.27111  ? 117 ALA   A CA  1 
ATOM   791  C C   . ALA   A 1 110 ? 14.46052  -3.26957  -14.59147 1.000 35.33192  ? 117 ALA   A C   1 
ATOM   792  O O   . ALA   A 1 110 ? 14.63441  -2.81304  -13.45373 1.000 42.04331  ? 117 ALA   A O   1 
ATOM   793  C CB  . ALA   A 1 110 ? 13.87912  -1.67610  -16.44213 1.000 40.76895  ? 117 ALA   A CB  1 
ATOM   794  N N   . PHE   A 1 111 ? 13.81208  -4.41658  -14.81023 1.000 33.36852  ? 118 PHE   A N   1 
ATOM   795  C CA  . PHE   A 1 111 ? 13.28188  -5.21131  -13.70399 1.000 34.91658  ? 118 PHE   A CA  1 
ATOM   796  C C   . PHE   A 1 111 ? 14.39304  -5.66070  -12.76305 1.000 43.21094  ? 118 PHE   A C   1 
ATOM   797  O O   . PHE   A 1 111 ? 14.26883  -5.54024  -11.53867 1.000 36.95150  ? 118 PHE   A O   1 
ATOM   798  C CB  . PHE   A 1 111 ? 12.51716  -6.41241  -14.26778 1.000 28.28324  ? 118 PHE   A CB  1 
ATOM   799  C CG  . PHE   A 1 111 ? 11.89558  -7.30897  -13.22764 1.000 29.13494  ? 118 PHE   A CG  1 
ATOM   800  C CD1 . PHE   A 1 111 ? 11.30911  -6.78658  -12.08340 1.000 33.19875  ? 118 PHE   A CD1 1 
ATOM   801  C CD2 . PHE   A 1 111 ? 11.85592  -8.68083  -13.42382 1.000 30.59922  ? 118 PHE   A CD2 1 
ATOM   802  C CE1 . PHE   A 1 111 ? 10.71767  -7.61585  -11.14383 1.000 31.95371  ? 118 PHE   A CE1 1 
ATOM   803  C CE2 . PHE   A 1 111 ? 11.26410  -9.51602  -12.49180 1.000 32.48049  ? 118 PHE   A CE2 1 
ATOM   804  C CZ  . PHE   A 1 111 ? 10.69671  -8.98037  -11.34403 1.000 34.45395  ? 118 PHE   A CZ  1 
ATOM   805  N N   . MET   A 1 112 ? 15.50174  -6.15411  -13.31247 1.000 40.95882  ? 119 MET   A N   1 
ATOM   806  C CA  . MET   A 1 112 ? 16.54298  -6.69533  -12.44971 1.000 44.59644  ? 119 MET   A CA  1 
ATOM   807  C C   . MET   A 1 112 ? 17.35017  -5.60057  -11.75885 1.000 44.77648  ? 119 MET   A C   1 
ATOM   808  O O   . MET   A 1 112 ? 17.85509  -5.82309  -10.65255 1.000 48.28331  ? 119 MET   A O   1 
ATOM   809  C CB  . MET   A 1 112 ? 17.43929  -7.63903  -13.25157 1.000 50.29080  ? 119 MET   A CB  1 
ATOM   810  C CG  . MET   A 1 112 ? 16.85331  -9.05272  -13.33810 1.000 31.84867  ? 119 MET   A CG  1 
ATOM   811  S SD  . MET   A 1 112 ? 18.05096  -10.30594 -13.81612 1.000 87.56452  ? 119 MET   A SD  1 
ATOM   812  C CE  . MET   A 1 112 ? 17.07518  -11.28776 -14.95092 1.000 41.66888  ? 119 MET   A CE  1 
ATOM   813  N N   . GLU   A 1 113 ? 17.46896  -4.41345  -12.36344 1.000 47.14362  ? 120 GLU   A N   1 
ATOM   814  C CA  . GLU   A 1 113 ? 18.02059  -3.28718  -11.61324 1.000 44.78960  ? 120 GLU   A CA  1 
ATOM   815  C C   . GLU   A 1 113 ? 17.09805  -2.86992  -10.47679 1.000 45.89402  ? 120 GLU   A C   1 
ATOM   816  O O   . GLU   A 1 113 ? 17.57277  -2.39476  -9.43882  1.000 49.97374  ? 120 GLU   A O   1 
ATOM   817  C CB  . GLU   A 1 113 ? 18.29077  -2.08593  -12.52203 1.000 58.86285  ? 120 GLU   A CB  1 
ATOM   818  C CG  . GLU   A 1 113 ? 19.02578  -2.38597  -13.81227 1.000 65.15506  ? 120 GLU   A CG  1 
ATOM   819  C CD  . GLU   A 1 113 ? 19.28512  -1.13345  -14.63073 1.000 72.04559  ? 120 GLU   A CD  1 
ATOM   820  O OE1 . GLU   A 1 113 ? 19.29638  -0.03294  -14.04149 1.000 89.24208  ? 120 GLU   A OE1 1 
ATOM   821  O OE2 . GLU   A 1 113 ? 19.47594  -1.24619  -15.86000 1.000 71.98776  ? 120 GLU   A OE2 1 
ATOM   822  N N   . ALA   A 1 114 ? 15.78504  -3.02828  -10.65320 1.000 42.40534  ? 121 ALA   A N   1 
ATOM   823  C CA  . ALA   A 1 114 ? 14.85574  -2.69030  -9.58068  1.000 50.26010  ? 121 ALA   A CA  1 
ATOM   824  C C   . ALA   A 1 114 ? 14.93368  -3.70295  -8.44730  1.000 41.57952  ? 121 ALA   A C   1 
ATOM   825  O O   . ALA   A 1 114 ? 14.82580  -3.33589  -7.27107  1.000 44.41552  ? 121 ALA   A O   1 
ATOM   826  C CB  . ALA   A 1 114 ? 13.43136  -2.60415  -10.12476 1.000 41.90272  ? 121 ALA   A CB  1 
ATOM   827  N N   . LEU   A 1 115 ? 15.13127  -4.98090  -8.78190  1.000 43.15092  ? 122 LEU   A N   1 
ATOM   828  C CA  . LEU   A 1 115 ? 15.17289  -6.01841  -7.75654  1.000 46.62619  ? 122 LEU   A CA  1 
ATOM   829  C C   . LEU   A 1 115 ? 16.36204  -5.83067  -6.82778  1.000 53.10384  ? 122 LEU   A C   1 
ATOM   830  O O   . LEU   A 1 115 ? 16.26523  -6.08383  -5.62143  1.000 54.05868  ? 122 LEU   A O   1 
ATOM   831  C CB  . LEU   A 1 115 ? 15.22327  -7.39775  -8.40655  1.000 39.87102  ? 122 LEU   A CB  1 
ATOM   832  C CG  . LEU   A 1 115 ? 13.91924  -7.88557  -9.03852  1.000 42.82452  ? 122 LEU   A CG  1 
ATOM   833  C CD1 . LEU   A 1 115 ? 14.13583  -9.23088  -9.70428  1.000 41.13531  ? 122 LEU   A CD1 1 
ATOM   834  C CD2 . LEU   A 1 115 ? 12.81189  -7.96596  -7.99682  1.000 40.34818  ? 122 LEU   A CD2 1 
ATOM   835  N N   . GLN   A 1 116 ? 17.49490  -5.39678  -7.36714  1.000 54.24775  ? 123 GLN   A N   1 
ATOM   836  C CA  . GLN   A 1 116 ? 18.64779  -5.13879  -6.51990  1.000 50.06392  ? 123 GLN   A CA  1 
ATOM   837  C C   . GLN   A 1 116 ? 18.57560  -3.77352  -5.85017  1.000 62.88559  ? 123 GLN   A C   1 
ATOM   838  O O   . GLN   A 1 116 ? 19.47491  -3.42944  -5.07569  1.000 75.52941  ? 123 GLN   A O   1 
ATOM   839  C CB  . GLN   A 1 116 ? 19.93229  -5.27519  -7.33884  1.000 74.79274  ? 123 GLN   A CB  1 
ATOM   840  C CG  . GLN   A 1 116 ? 20.24768  -6.72299  -7.69323  1.000 69.86446  ? 123 GLN   A CG  1 
ATOM   841  C CD  . GLN   A 1 116 ? 21.65865  -7.13273  -7.32527  1.000 98.33006  ? 123 GLN   A CD  1 
ATOM   842  O OE1 . GLN   A 1 116 ? 22.37966  -6.39247  -6.65617  1.000 104.54624 ? 123 GLN   A OE1 1 
ATOM   843  N NE2 . GLN   A 1 116 ? 22.05951  -8.32367  -7.75890  1.000 98.97601  ? 123 GLN   A NE2 1 
ATOM   844  N N   . ALA   A 1 117 ? 17.52175  -3.00033  -6.12157  1.000 69.28433  ? 124 ALA   A N   1 
ATOM   845  C CA  . ALA   A 1 117 ? 17.29976  -1.70268  -5.49845  1.000 65.26236  ? 124 ALA   A CA  1 
ATOM   846  C C   . ALA   A 1 117 ? 16.05591  -1.68936  -4.61536  1.000 64.71940  ? 124 ALA   A C   1 
ATOM   847  O O   . ALA   A 1 117 ? 15.53125  -0.61518  -4.30660  1.000 61.69674  ? 124 ALA   A O   1 
ATOM   848  C CB  . ALA   A 1 117 ? 17.20375  -0.61132  -6.56476  1.000 63.90531  ? 124 ALA   A CB  1 
ATOM   849  N N   . GLY   A 1 118 ? 15.56285  -2.85814  -4.21576  1.000 61.85216  ? 125 GLY   A N   1 
ATOM   850  C CA  . GLY   A 1 118 ? 14.48227  -2.94428  -3.25705  1.000 55.35716  ? 125 GLY   A CA  1 
ATOM   851  C C   . GLY   A 1 118 ? 13.13637  -3.39542  -3.78768  1.000 53.69880  ? 125 GLY   A C   1 
ATOM   852  O O   . GLY   A 1 118 ? 12.16125  -3.38222  -3.02835  1.000 54.52269  ? 125 GLY   A O   1 
ATOM   853  N N   . ALA   A 1 119 ? 13.04121  -3.78551  -5.05248  1.000 51.35262  ? 126 ALA   A N   1 
ATOM   854  C CA  . ALA   A 1 119 ? 11.78808  -4.29176  -5.58719  1.000 48.39395  ? 126 ALA   A CA  1 
ATOM   855  C C   . ALA   A 1 119 ? 11.67411  -5.79186  -5.34156  1.000 42.31576  ? 126 ALA   A C   1 
ATOM   856  O O   . ALA   A 1 119 ? 12.64641  -6.46798  -5.00031  1.000 46.15932  ? 126 ALA   A O   1 
ATOM   857  C CB  . ALA   A 1 119 ? 11.67438  -3.99473  -7.08266  1.000 44.43198  ? 126 ALA   A CB  1 
ATOM   858  N N   . ASP   A 1 120 ? 10.45974  -6.30786  -5.50943  1.000 48.30520  ? 127 ASP   A N   1 
ATOM   859  C CA  . ASP   A 1 120 ? 10.21143  -7.73732  -5.41980  1.000 49.14354  ? 127 ASP   A CA  1 
ATOM   860  C C   . ASP   A 1 120 ? 9.49294   -8.19759  -6.67899  1.000 35.00405  ? 127 ASP   A C   1 
ATOM   861  O O   . ASP   A 1 120 ? 9.09411   -7.39422  -7.52804  1.000 36.75289  ? 127 ASP   A O   1 
ATOM   862  C CB  . ASP   A 1 120 ? 9.39892   -8.10339  -4.17128  1.000 50.81968  ? 127 ASP   A CB  1 
ATOM   863  C CG  . ASP   A 1 120 ? 8.01642   -7.50205  -4.18315  1.000 56.14166  ? 127 ASP   A CG  1 
ATOM   864  O OD1 . ASP   A 1 120 ? 7.90418   -6.26538  -4.04919  1.000 65.61106  ? 127 ASP   A OD1 1 
ATOM   865  O OD2 . ASP   A 1 120 ? 7.04357   -8.26723  -4.34320  1.000 55.43650  ? 127 ASP   A OD2 1 
ATOM   866  N N   . ILE   A 1 121 ? 9.33138   -9.51791  -6.78979  1.000 34.09609  ? 128 ILE   A N   1 
ATOM   867  C CA  . ILE   A 1 121 ? 8.84537   -10.11755 -8.02933  1.000 36.36668  ? 128 ILE   A CA  1 
ATOM   868  C C   . ILE   A 1 121 ? 7.44033   -9.63384  -8.37032  1.000 33.68290  ? 128 ILE   A C   1 
ATOM   869  O O   . ILE   A 1 121 ? 7.07480   -9.55638  -9.55001  1.000 34.79594  ? 128 ILE   A O   1 
ATOM   870  C CB  . ILE   A 1 121 ? 8.93170   -11.65561 -7.92155  1.000 33.57038  ? 128 ILE   A CB  1 
ATOM   871  C CG1 . ILE   A 1 121 ? 10.39584  -12.09648 -8.01436  1.000 44.01435  ? 128 ILE   A CG1 1 
ATOM   872  C CG2 . ILE   A 1 121 ? 8.10709   -12.34729 -8.99829  1.000 37.27591  ? 128 ILE   A CG2 1 
ATOM   873  C CD1 . ILE   A 1 121 ? 10.62559  -13.55576 -7.69715  1.000 54.70492  ? 128 ILE   A CD1 1 
ATOM   874  N N   . SER   A 1 122 ? 6.64516   -9.25767  -7.36260  1.000 35.79814  ? 129 SER   A N   1 
ATOM   875  C CA  . SER   A 1 122 ? 5.27379   -8.82833  -7.63143  1.000 36.67289  ? 129 SER   A CA  1 
ATOM   876  C C   . SER   A 1 122 ? 5.20952   -7.56004  -8.47344  1.000 42.11422  ? 129 SER   A C   1 
ATOM   877  O O   . SER   A 1 122 ? 4.14996   -7.25466  -9.02902  1.000 35.61199  ? 129 SER   A O   1 
ATOM   878  C CB  . SER   A 1 122 ? 4.50806   -8.60293  -6.32696  1.000 33.61707  ? 129 SER   A CB  1 
ATOM   879  O OG  . SER   A 1 122 ? 4.96788   -7.44690  -5.64987  1.000 39.86892  ? 129 SER   A OG  1 
ATOM   880  N N   . MET   A 1 123 ? 6.30435   -6.81298  -8.57768  1.000 33.43402  ? 130 MET   A N   1 
ATOM   881  C CA  . MET   A 1 123 ? 6.32517   -5.58177  -9.35430  1.000 29.16045  ? 130 MET   A CA  1 
ATOM   882  C C   . MET   A 1 123 ? 6.69845   -5.81216  -10.81758 1.000 36.50539  ? 130 MET   A C   1 
ATOM   883  O O   . MET   A 1 123 ? 6.88337   -4.84044  -11.55772 1.000 30.08049  ? 130 MET   A O   1 
ATOM   884  C CB  . MET   A 1 123 ? 7.28636   -4.58649  -8.70832  1.000 35.78578  ? 130 MET   A CB  1 
ATOM   885  C CG  . MET   A 1 123 ? 6.74187   -4.00850  -7.41067  1.000 41.14717  ? 130 MET   A CG  1 
ATOM   886  S SD  . MET   A 1 123 ? 8.05460   -3.33969  -6.38567  1.000 52.63813  ? 130 MET   A SD  1 
ATOM   887  C CE  . MET   A 1 123 ? 8.61961   -2.05909  -7.48990  1.000 50.55931  ? 130 MET   A CE  1 
ATOM   888  N N   . ILE   A 1 124 ? 6.77577   -7.07637  -11.24747 1.000 30.74377  ? 131 ILE   A N   1 
ATOM   889  C CA  . ILE   A 1 124 ? 7.23512   -7.43024  -12.59494 1.000 29.55064  ? 131 ILE   A CA  1 
ATOM   890  C C   . ILE   A 1 124 ? 6.44321   -6.70354  -13.67984 1.000 26.78939  ? 131 ILE   A C   1 
ATOM   891  O O   . ILE   A 1 124 ? 6.99774   -6.31558  -14.71694 1.000 26.71680  ? 131 ILE   A O   1 
ATOM   892  C CB  . ILE   A 1 124 ? 7.16845   -8.95961  -12.78161 1.000 28.40511  ? 131 ILE   A CB  1 
ATOM   893  C CG1 . ILE   A 1 124 ? 7.70611   -9.37286  -14.15424 1.000 28.59201  ? 131 ILE   A CG1 1 
ATOM   894  C CG2 . ILE   A 1 124 ? 5.75086   -9.46901  -12.55782 1.000 26.49020  ? 131 ILE   A CG2 1 
ATOM   895  C CD1 . ILE   A 1 124 ? 7.89553   -10.86954 -14.30834 1.000 27.26752  ? 131 ILE   A CD1 1 
ATOM   896  N N   . GLY   A 1 125 ? 5.14179   -6.50309  -13.46178 1.000 27.90555  ? 132 GLY   A N   1 
ATOM   897  C CA  . GLY   A 1 125 ? 4.29762   -5.89588  -14.47938 1.000 31.10179  ? 132 GLY   A CA  1 
ATOM   898  C C   . GLY   A 1 125 ? 4.64772   -4.45832  -14.81206 1.000 30.74851  ? 132 GLY   A C   1 
ATOM   899  O O   . GLY   A 1 125 ? 4.33559   -3.99413  -15.91404 1.000 36.07842  ? 132 GLY   A O   1 
ATOM   900  N N   . GLN   A 1 126 ? 5.28805   -3.74259  -13.88775 1.000 27.10313  ? 133 GLN   A N   1 
ATOM   901  C CA  . GLN   A 1 126 ? 5.70582   -2.37107  -14.15866 1.000 33.20012  ? 133 GLN   A CA  1 
ATOM   902  C C   . GLN   A 1 126 ? 6.80789   -2.29084  -15.20248 1.000 36.49356  ? 133 GLN   A C   1 
ATOM   903  O O   . GLN   A 1 126 ? 7.14509   -1.18741  -15.64388 1.000 37.67500  ? 133 GLN   A O   1 
ATOM   904  C CB  . GLN   A 1 126 ? 6.18436   -1.70700  -12.87283 1.000 34.08155  ? 133 GLN   A CB  1 
ATOM   905  C CG  . GLN   A 1 126 ? 5.15156   -1.72062  -11.76743 1.000 43.62112  ? 133 GLN   A CG  1 
ATOM   906  C CD  . GLN   A 1 126 ? 5.67229   -1.11363  -10.48642 1.000 48.29998  ? 133 GLN   A CD  1 
ATOM   907  O OE1 . GLN   A 1 126 ? 6.56267   -0.26023  -10.50413 1.000 46.23438  ? 133 GLN   A OE1 1 
ATOM   908  N NE2 . GLN   A 1 126 ? 5.12483   -1.55589  -9.36055  1.000 50.50647  ? 133 GLN   A NE2 1 
ATOM   909  N N   . PHE   A 1 127 ? 7.37649   -3.42430  -15.59861 1.000 30.97699  ? 134 PHE   A N   1 
ATOM   910  C CA  . PHE   A 1 127 ? 8.50934   -3.44974  -16.51118 1.000 33.81101  ? 134 PHE   A CA  1 
ATOM   911  C C   . PHE   A 1 127 ? 8.15538   -4.12512  -17.82614 1.000 27.97674  ? 134 PHE   A C   1 
ATOM   912  O O   . PHE   A 1 127 ? 9.05303   -4.43076  -18.62245 1.000 33.64203  ? 134 PHE   A O   1 
ATOM   913  C CB  . PHE   A 1 127 ? 9.68804   -4.13859  -15.82535 1.000 29.15603  ? 134 PHE   A CB  1 
ATOM   914  C CG  . PHE   A 1 127 ? 10.03266  -3.52100  -14.50496 1.000 33.81195  ? 134 PHE   A CG  1 
ATOM   915  C CD1 . PHE   A 1 127 ? 10.57398  -2.24670  -14.44065 1.000 40.23983  ? 134 PHE   A CD1 1 
ATOM   916  C CD2 . PHE   A 1 127 ? 9.73250   -4.17643  -13.32401 1.000 32.72807  ? 134 PHE   A CD2 1 
ATOM   917  C CE1 . PHE   A 1 127 ? 10.86365  -1.66287  -13.22073 1.000 38.30037  ? 134 PHE   A CE1 1 
ATOM   918  C CE2 . PHE   A 1 127 ? 10.01588  -3.59626  -12.09986 1.000 36.37786  ? 134 PHE   A CE2 1 
ATOM   919  C CZ  . PHE   A 1 127 ? 10.58168  -2.33818  -12.05076 1.000 40.92751  ? 134 PHE   A CZ  1 
ATOM   920  N N   . GLY   A 1 128 ? 6.86919   -4.37199  -18.06447 1.000 30.25783  ? 135 GLY   A N   1 
ATOM   921  C CA  . GLY   A 1 128 ? 6.39161   -4.87671  -19.33251 1.000 25.15248  ? 135 GLY   A CA  1 
ATOM   922  C C   . GLY   A 1 128 ? 6.58501   -6.35615  -19.57402 1.000 24.81191  ? 135 GLY   A C   1 
ATOM   923  O O   . GLY   A 1 128 ? 6.31927   -6.81631  -20.68798 1.000 29.78635  ? 135 GLY   A O   1 
ATOM   924  N N   . VAL   A 1 129 ? 7.02489   -7.12142  -18.57441 1.000 23.21689  ? 136 VAL   A N   1 
ATOM   925  C CA  . VAL   A 1 129 ? 7.29402   -8.54160  -18.78022 1.000 21.83651  ? 136 VAL   A CA  1 
ATOM   926  C C   . VAL   A 1 129 ? 6.42729   -9.38564  -17.85524 1.000 27.64632  ? 136 VAL   A C   1 
ATOM   927  O O   . VAL   A 1 129 ? 6.79517   -10.50998 -17.49549 1.000 22.89032  ? 136 VAL   A O   1 
ATOM   928  C CB  . VAL   A 1 129 ? 8.78560   -8.85454  -18.57512 1.000 24.87579  ? 136 VAL   A CB  1 
ATOM   929  C CG1 . VAL   A 1 129 ? 9.58265   -8.38478  -19.78069 1.000 25.13381  ? 136 VAL   A CG1 1 
ATOM   930  C CG2 . VAL   A 1 129 ? 9.29792   -8.19401  -17.30691 1.000 24.17657  ? 136 VAL   A CG2 1 
ATOM   931  N N   . GLY   A 1 130 ? 5.25721   -8.85862  -17.49245 1.000 24.42300  ? 137 GLY   A N   1 
ATOM   932  C CA  . GLY   A 1 130 ? 4.37544   -9.57065  -16.57980 1.000 21.87630  ? 137 GLY   A CA  1 
ATOM   933  C C   . GLY   A 1 130 ? 3.90031   -10.91646 -17.09830 1.000 21.59636  ? 137 GLY   A C   1 
ATOM   934  O O   . GLY   A 1 130 ? 3.55258   -11.79929 -16.30829 1.000 23.58734  ? 137 GLY   A O   1 
ATOM   935  N N   . PHE   A 1 131 ? 3.86718   -11.09634 -18.42260 1.000 20.32160  ? 138 PHE   A N   1 
ATOM   936  C CA  . PHE   A 1 131 ? 3.45793   -12.38816 -18.97272 1.000 18.62807  ? 138 PHE   A CA  1 
ATOM   937  C C   . PHE   A 1 131 ? 4.25778   -13.53619 -18.37110 1.000 22.97903  ? 138 PHE   A C   1 
ATOM   938  O O   . PHE   A 1 131 ? 3.70537   -14.60009 -18.06786 1.000 21.25916  ? 138 PHE   A O   1 
ATOM   939  C CB  . PHE   A 1 131 ? 3.61431   -12.40846 -20.49604 1.000 22.90402  ? 138 PHE   A CB  1 
ATOM   940  C CG  . PHE   A 1 131 ? 3.59288   -13.79550 -21.07457 1.000 25.18070  ? 138 PHE   A CG  1 
ATOM   941  C CD1 . PHE   A 1 131 ? 2.39779   -14.48663 -21.19389 1.000 23.34824  ? 138 PHE   A CD1 1 
ATOM   942  C CD2 . PHE   A 1 131 ? 4.77228   -14.42677 -21.46003 1.000 24.66815  ? 138 PHE   A CD2 1 
ATOM   943  C CE1 . PHE   A 1 131 ? 2.36696   -15.77739 -21.70419 1.000 22.41688  ? 138 PHE   A CE1 1 
ATOM   944  C CE2 . PHE   A 1 131 ? 4.74862   -15.72052 -21.97699 1.000 21.94209  ? 138 PHE   A CE2 1 
ATOM   945  C CZ  . PHE   A 1 131 ? 3.54641   -16.39243 -22.09864 1.000 21.54333  ? 138 PHE   A CZ  1 
ATOM   946  N N   . TYR   A 1 132 ? 5.56222   -13.33763 -18.19084 1.000 21.35464  ? 139 TYR   A N   1 
ATOM   947  C CA  . TYR   A 1 132 ? 6.43673   -14.41983 -17.76160 1.000 21.71740  ? 139 TYR   A CA  1 
ATOM   948  C C   . TYR   A 1 132 ? 6.19458   -14.83434 -16.31549 1.000 21.07263  ? 139 TYR   A C   1 
ATOM   949  O O   . TYR   A 1 132 ? 6.67603   -15.89697 -15.90668 1.000 22.25501  ? 139 TYR   A O   1 
ATOM   950  C CB  . TYR   A 1 132 ? 7.89216   -14.00740 -17.98688 1.000 20.99260  ? 139 TYR   A CB  1 
ATOM   951  C CG  . TYR   A 1 132 ? 8.17406   -13.76715 -19.45630 1.000 20.61217  ? 139 TYR   A CG  1 
ATOM   952  C CD1 . TYR   A 1 132 ? 8.42252   -14.82529 -20.32397 1.000 23.96256  ? 139 TYR   A CD1 1 
ATOM   953  C CD2 . TYR   A 1 132 ? 8.13315   -12.48261 -19.98214 1.000 21.61926  ? 139 TYR   A CD2 1 
ATOM   954  C CE1 . TYR   A 1 132 ? 8.65507   -14.60087 -21.68010 1.000 20.98685  ? 139 TYR   A CE1 1 
ATOM   955  C CE2 . TYR   A 1 132 ? 8.36303   -12.24789 -21.32566 1.000 28.05562  ? 139 TYR   A CE2 1 
ATOM   956  C CZ  . TYR   A 1 132 ? 8.62093   -13.30845 -22.17054 1.000 25.33396  ? 139 TYR   A CZ  1 
ATOM   957  O OH  . TYR   A 1 132 ? 8.84598   -13.06117 -23.50468 1.000 25.32977  ? 139 TYR   A OH  1 
ATOM   958  N N   . SER   A 1 133 ? 5.43343   -14.05061 -15.54736 1.000 22.97449  ? 140 SER   A N   1 
ATOM   959  C CA  . SER   A 1 133 ? 5.01081   -14.49697 -14.22388 1.000 22.59528  ? 140 SER   A CA  1 
ATOM   960  C C   . SER   A 1 133 ? 4.13943   -15.74446 -14.28722 1.000 20.55411  ? 140 SER   A C   1 
ATOM   961  O O   . SER   A 1 133 ? 3.93888   -16.39149 -13.25370 1.000 21.65895  ? 140 SER   A O   1 
ATOM   962  C CB  . SER   A 1 133 ? 4.27479   -13.37015 -13.48859 1.000 24.99135  ? 140 SER   A CB  1 
ATOM   963  O OG  . SER   A 1 133 ? 2.96881   -13.16895 -14.00048 1.000 22.85678  ? 140 SER   A OG  1 
ATOM   964  N N   . ALA   A 1 134 ? 3.63193   -16.10504 -15.47358 1.000 20.42529  ? 141 ALA   A N   1 
ATOM   965  C CA  . ALA   A 1 134 ? 2.93646   -17.37963 -15.62805 1.000 21.27581  ? 141 ALA   A CA  1 
ATOM   966  C C   . ALA   A 1 134 ? 3.76807   -18.54167 -15.09802 1.000 19.68237  ? 141 ALA   A C   1 
ATOM   967  O O   . ALA   A 1 134 ? 3.21411   -19.50929 -14.56102 1.000 21.03691  ? 141 ALA   A O   1 
ATOM   968  C CB  . ALA   A 1 134 ? 2.58647   -17.61747 -17.10278 1.000 18.34223  ? 141 ALA   A CB  1 
ATOM   969  N N   . TYR   A 1 135 ? 5.09617   -18.45401 -15.21114 1.000 19.33730  ? 142 TYR   A N   1 
ATOM   970  C CA  . TYR   A 1 135 ? 5.95728   -19.55136 -14.79054 1.000 20.26889  ? 142 TYR   A CA  1 
ATOM   971  C C   . TYR   A 1 135 ? 6.16485   -19.60649 -13.28243 1.000 22.89851  ? 142 TYR   A C   1 
ATOM   972  O O   . TYR   A 1 135 ? 6.90187   -20.47668 -12.81048 1.000 25.00955  ? 142 TYR   A O   1 
ATOM   973  C CB  . TYR   A 1 135 ? 7.29526   -19.46514 -15.52341 1.000 20.35405  ? 142 TYR   A CB  1 
ATOM   974  C CG  . TYR   A 1 135 ? 7.10057   -19.80689 -16.97667 1.000 22.44388  ? 142 TYR   A CG  1 
ATOM   975  C CD1 . TYR   A 1 135 ? 7.13671   -21.12637 -17.41413 1.000 21.68488  ? 142 TYR   A CD1 1 
ATOM   976  C CD2 . TYR   A 1 135 ? 6.80691   -18.81381 -17.89994 1.000 20.44596  ? 142 TYR   A CD2 1 
ATOM   977  C CE1 . TYR   A 1 135 ? 6.92349   -21.44189 -18.75174 1.000 21.57527  ? 142 TYR   A CE1 1 
ATOM   978  C CE2 . TYR   A 1 135 ? 6.59100   -19.11718 -19.23564 1.000 23.40743  ? 142 TYR   A CE2 1 
ATOM   979  C CZ  . TYR   A 1 135 ? 6.65028   -20.43085 -19.65278 1.000 24.02265  ? 142 TYR   A CZ  1 
ATOM   980  O OH  . TYR   A 1 135 ? 6.43351   -20.72902 -20.98056 1.000 21.41433  ? 142 TYR   A OH  1 
ATOM   981  N N   . LEU   A 1 136 ? 5.53187   -18.70974 -12.52245 1.000 22.62696  ? 143 LEU   A N   1 
ATOM   982  C CA  . LEU   A 1 136 ? 5.41742   -18.91035 -11.08200 1.000 21.09066  ? 143 LEU   A CA  1 
ATOM   983  C C   . LEU   A 1 136 ? 4.56469   -20.12936 -10.76193 1.000 22.62669  ? 143 LEU   A C   1 
ATOM   984  O O   . LEU   A 1 136 ? 4.78915   -20.79586 -9.74718  1.000 24.71355  ? 143 LEU   A O   1 
ATOM   985  C CB  . LEU   A 1 136 ? 4.80139   -17.67710 -10.42166 1.000 25.15678  ? 143 LEU   A CB  1 
ATOM   986  C CG  . LEU   A 1 136 ? 5.62969   -16.39344 -10.43043 1.000 23.76556  ? 143 LEU   A CG  1 
ATOM   987  C CD1 . LEU   A 1 136 ? 4.77712   -15.20518 -9.98916  1.000 24.83566  ? 143 LEU   A CD1 1 
ATOM   988  C CD2 . LEU   A 1 136 ? 6.85459   -16.55394 -9.54892  1.000 25.64558  ? 143 LEU   A CD2 1 
ATOM   989  N N   . VAL   A 1 137 ? 3.58909   -20.43851 -11.61321 1.000 23.98605  ? 144 VAL   A N   1 
ATOM   990  C CA  . VAL   A 1 137 ? 2.63946   -21.50720 -11.33105 1.000 23.51610  ? 144 VAL   A CA  1 
ATOM   991  C C   . VAL   A 1 137 ? 2.57246   -22.56819 -12.41815 1.000 25.17335  ? 144 VAL   A C   1 
ATOM   992  O O   . VAL   A 1 137 ? 2.05741   -23.67001 -12.16163 1.000 25.07420  ? 144 VAL   A O   1 
ATOM   993  C CB  . VAL   A 1 137 ? 1.23196   -20.92107 -11.07122 1.000 23.55395  ? 144 VAL   A CB  1 
ATOM   994  C CG1 . VAL   A 1 137 ? 1.23715   -20.03099 -9.82452  1.000 24.66695  ? 144 VAL   A CG1 1 
ATOM   995  C CG2 . VAL   A 1 137 ? 0.74004   -20.13515 -12.28679 1.000 23.06761  ? 144 VAL   A CG2 1 
ATOM   996  N N   . ALA   A 1 138 ? 3.07519   -22.32353 -13.62632 1.000 25.26539  ? 145 ALA   A N   1 
ATOM   997  C CA  . ALA   A 1 138 ? 2.90695   -23.24619 -14.74116 1.000 24.92630  ? 145 ALA   A CA  1 
ATOM   998  C C   . ALA   A 1 138 ? 4.23209   -23.90358 -15.09123 1.000 26.08504  ? 145 ALA   A C   1 
ATOM   999  O O   . ALA   A 1 138 ? 5.26360   -23.22883 -15.17685 1.000 25.58260  ? 145 ALA   A O   1 
ATOM   1000 C CB  . ALA   A 1 138 ? 2.34757   -22.52666 -15.96854 1.000 22.47757  ? 145 ALA   A CB  1 
ATOM   1001 N N   . GLU   A 1 139 ? 4.19439   -25.21726 -15.30535 1.000 24.19925  ? 146 GLU   A N   1 
ATOM   1002 C CA  . GLU   A 1 139 ? 5.34206   -25.92916 -15.85196 1.000 23.89495  ? 146 GLU   A CA  1 
ATOM   1003 C C   . GLU   A 1 139 ? 5.45064   -25.76265 -17.36367 1.000 28.80164  ? 146 GLU   A C   1 
ATOM   1004 O O   . GLU   A 1 139 ? 6.55159   -25.86723 -17.91526 1.000 26.82126  ? 146 GLU   A O   1 
ATOM   1005 C CB  . GLU   A 1 139 ? 5.25279   -27.40588 -15.45021 1.000 32.36920  ? 146 GLU   A CB  1 
ATOM   1006 C CG  . GLU   A 1 139 ? 4.50826   -28.30025 -16.41597 1.000 44.30266  ? 146 GLU   A CG  1 
ATOM   1007 C CD  . GLU   A 1 139 ? 4.17334   -29.65150 -15.80359 1.000 62.77208  ? 146 GLU   A CD  1 
ATOM   1008 O OE1 . GLU   A 1 139 ? 4.92044   -30.10579 -14.91093 1.000 54.24891  ? 146 GLU   A OE1 1 
ATOM   1009 O OE2 . GLU   A 1 139 ? 3.15793   -30.25623 -16.21159 1.000 58.68980  ? 146 GLU   A OE2 1 
ATOM   1010 N N   . LYS   A 1 140 ? 4.33990   -25.47295 -18.03412 1.000 22.55107  ? 147 LYS   A N   1 
ATOM   1011 C CA  . LYS   A 1 140 ? 4.32252   -25.23015 -19.46746 1.000 26.47676  ? 147 LYS   A CA  1 
ATOM   1012 C C   . LYS   A 1 140 ? 3.22038   -24.22052 -19.75090 1.000 24.13427  ? 147 LYS   A C   1 
ATOM   1013 O O   . LYS   A 1 140 ? 2.18890   -24.21808 -19.07247 1.000 24.00808  ? 147 LYS   A O   1 
ATOM   1014 C CB  . LYS   A 1 140 ? 4.10661   -26.54045 -20.23097 1.000 24.35915  ? 147 LYS   A CB  1 
ATOM   1015 C CG  . LYS   A 1 140 ? 3.75996   -26.41395 -21.70231 1.000 28.12701  ? 147 LYS   A CG  1 
ATOM   1016 C CD  . LYS   A 1 140 ? 3.83168   -27.78718 -22.35022 1.000 29.19779  ? 147 LYS   A CD  1 
ATOM   1017 C CE  . LYS   A 1 140 ? 2.59369   -28.09957 -23.15412 1.000 42.33291  ? 147 LYS   A CE  1 
ATOM   1018 N NZ  . LYS   A 1 140 ? 2.28663   -29.55767 -23.12139 1.000 43.84588  ? 147 LYS   A NZ  1 
ATOM   1019 N N   . VAL   A 1 141 ? 3.45715   -23.33733 -20.71912 1.000 18.72468  ? 148 VAL   A N   1 
ATOM   1020 C CA  . VAL   A 1 141 ? 2.47278   -22.33584 -21.11496 1.000 17.91933  ? 148 VAL   A CA  1 
ATOM   1021 C C   . VAL   A 1 141 ? 2.26698   -22.43214 -22.62201 1.000 20.58072  ? 148 VAL   A C   1 
ATOM   1022 O O   . VAL   A 1 141 ? 3.24140   -22.46063 -23.38321 1.000 20.37961  ? 148 VAL   A O   1 
ATOM   1023 C CB  . VAL   A 1 141 ? 2.90456   -20.91148 -20.72136 1.000 21.16097  ? 148 VAL   A CB  1 
ATOM   1024 C CG1 . VAL   A 1 141 ? 1.86660   -19.89776 -21.19262 1.000 20.86922  ? 148 VAL   A CG1 1 
ATOM   1025 C CG2 . VAL   A 1 141 ? 3.12678   -20.80618 -19.20418 1.000 22.26494  ? 148 VAL   A CG2 1 
ATOM   1026 N N   . THR   A 1 142 ? 1.00394   -22.51004 -23.04245 1.000 20.27817  ? 149 THR   A N   1 
ATOM   1027 C CA  . THR   A 1 142 ? 0.61036   -22.45745 -24.44823 1.000 20.84518  ? 149 THR   A CA  1 
ATOM   1028 C C   . THR   A 1 142 ? -0.14215  -21.15443 -24.68959 1.000 21.35831  ? 149 THR   A C   1 
ATOM   1029 O O   . THR   A 1 142 ? -1.01427  -20.78311 -23.89567 1.000 22.89916  ? 149 THR   A O   1 
ATOM   1030 C CB  . THR   A 1 142 ? -0.27435  -23.65125 -24.83562 1.000 23.25161  ? 149 THR   A CB  1 
ATOM   1031 O OG1 . THR   A 1 142 ? 0.31629   -24.87598 -24.38372 1.000 26.15592  ? 149 THR   A OG1 1 
ATOM   1032 C CG2 . THR   A 1 142 ? -0.46770  -23.71441 -26.34951 1.000 22.46724  ? 149 THR   A CG2 1 
ATOM   1033 N N   . VAL   A 1 143 ? 0.19646   -20.45712 -25.77220 1.000 20.35235  ? 150 VAL   A N   1 
ATOM   1034 C CA  . VAL   A 1 143 ? -0.46745  -19.20729 -26.14254 1.000 22.42906  ? 150 VAL   A CA  1 
ATOM   1035 C C   . VAL   A 1 143 ? -1.03156  -19.38128 -27.54559 1.000 25.02162  ? 150 VAL   A C   1 
ATOM   1036 O O   . VAL   A 1 143 ? -0.27183  -19.54137 -28.51055 1.000 22.84484  ? 150 VAL   A O   1 
ATOM   1037 C CB  . VAL   A 1 143 ? 0.48073   -18.00242 -26.07687 1.000 23.45170  ? 150 VAL   A CB  1 
ATOM   1038 C CG1 . VAL   A 1 143 ? -0.22750  -16.74700 -26.57574 1.000 20.63225  ? 150 VAL   A CG1 1 
ATOM   1039 C CG2 . VAL   A 1 143 ? 0.99383   -17.80501 -24.65641 1.000 19.60832  ? 150 VAL   A CG2 1 
ATOM   1040 N N   . ILE   A 1 144 ? -2.36112  -19.36679 -27.65753 1.000 18.96332  ? 151 ILE   A N   1 
ATOM   1041 C CA  . ILE   A 1 144 ? -3.06464  -19.42026 -28.93911 1.000 20.74216  ? 151 ILE   A CA  1 
ATOM   1042 C C   . ILE   A 1 144 ? -3.54383  -18.00706 -29.23641 1.000 23.49950  ? 151 ILE   A C   1 
ATOM   1043 O O   . ILE   A 1 144 ? -4.15546  -17.36887 -28.37321 1.000 22.00173  ? 151 ILE   A O   1 
ATOM   1044 C CB  . ILE   A 1 144 ? -4.25877  -20.39245 -28.89208 1.000 22.37321  ? 151 ILE   A CB  1 
ATOM   1045 C CG1 . ILE   A 1 144 ? -3.91759  -21.70142 -28.17749 1.000 30.60521  ? 151 ILE   A CG1 1 
ATOM   1046 C CG2 . ILE   A 1 144 ? -4.75578  -20.70198 -30.30456 1.000 24.91433  ? 151 ILE   A CG2 1 
ATOM   1047 C CD1 . ILE   A 1 144 ? -2.90788  -22.53588 -28.87989 1.000 31.97774  ? 151 ILE   A CD1 1 
ATOM   1048 N N   . THR   A 1 145 ? -3.27696  -17.50640 -30.44304 1.000 20.19310  ? 152 THR   A N   1 
ATOM   1049 C CA  . THR   A 1 145 ? -3.60272  -16.11039 -30.70594 1.000 21.96105  ? 152 THR   A CA  1 
ATOM   1050 C C   . THR   A 1 145 ? -4.03837  -15.92512 -32.15481 1.000 22.53090  ? 152 THR   A C   1 
ATOM   1051 O O   . THR   A 1 145 ? -3.59487  -16.64640 -33.05510 1.000 23.51776  ? 152 THR   A O   1 
ATOM   1052 C CB  . THR   A 1 145 ? -2.41181  -15.19695 -30.35790 1.000 25.08386  ? 152 THR   A CB  1 
ATOM   1053 O OG1 . THR   A 1 145 ? -2.83454  -13.82861 -30.31908 1.000 23.49078  ? 152 THR   A OG1 1 
ATOM   1054 C CG2 . THR   A 1 145 ? -1.28108  -15.34971 -31.36440 1.000 26.19848  ? 152 THR   A CG2 1 
ATOM   1055 N N   . LYS   A 1 146 ? -4.93386  -14.95623 -32.36057 1.000 24.30769  ? 153 LYS   A N   1 
ATOM   1056 C CA  . LYS   A 1 146 ? -5.40029  -14.57688 -33.69248 1.000 21.26549  ? 153 LYS   A CA  1 
ATOM   1057 C C   . LYS   A 1 146 ? -5.50337  -13.06132 -33.76106 1.000 26.49150  ? 153 LYS   A C   1 
ATOM   1058 O O   . LYS   A 1 146 ? -6.29655  -12.45568 -33.03441 1.000 25.04626  ? 153 LYS   A O   1 
ATOM   1059 C CB  . LYS   A 1 146 ? -6.75328  -15.21758 -34.01696 1.000 22.46725  ? 153 LYS   A CB  1 
ATOM   1060 C CG  . LYS   A 1 146 ? -7.37418  -14.78427 -35.34723 1.000 25.33524  ? 153 LYS   A CG  1 
ATOM   1061 C CD  . LYS   A 1 146 ? -6.67317  -15.42505 -36.54156 1.000 26.96826  ? 153 LYS   A CD  1 
ATOM   1062 C CE  . LYS   A 1 146 ? -7.35976  -15.06588 -37.86566 1.000 27.05944  ? 153 LYS   A CE  1 
ATOM   1063 N NZ  . LYS   A 1 146 ? -7.39491  -13.60282 -38.15856 1.000 29.80763  ? 153 LYS   A NZ  1 
ATOM   1064 N N   . HIS   A 1 147 ? -4.70730  -12.46239 -34.63526 1.000 25.24083  ? 154 HIS   A N   1 
ATOM   1065 C CA  . HIS   A 1 147 ? -4.73162  -11.03908 -34.93360 1.000 22.85438  ? 154 HIS   A CA  1 
ATOM   1066 C C   . HIS   A 1 147 ? -5.44618  -10.83691 -36.26659 1.000 30.22218  ? 154 HIS   A C   1 
ATOM   1067 O O   . HIS   A 1 147 ? -5.41875  -11.71444 -37.13328 1.000 27.89303  ? 154 HIS   A O   1 
ATOM   1068 C CB  . HIS   A 1 147 ? -3.29254  -10.50281 -34.97946 1.000 25.78553  ? 154 HIS   A CB  1 
ATOM   1069 C CG  . HIS   A 1 147 ? -3.17908  -9.01488  -35.12065 1.000 31.69958  ? 154 HIS   A CG  1 
ATOM   1070 N ND1 . HIS   A 1 147 ? -3.37650  -8.36039  -36.31627 1.000 29.81840  ? 154 HIS   A ND1 1 
ATOM   1071 C CD2 . HIS   A 1 147 ? -2.85077  -8.05858  -34.21979 1.000 27.61530  ? 154 HIS   A CD2 1 
ATOM   1072 C CE1 . HIS   A 1 147 ? -3.19535  -7.06305  -36.14371 1.000 29.54662  ? 154 HIS   A CE1 1 
ATOM   1073 N NE2 . HIS   A 1 147 ? -2.87531  -6.85358  -34.87894 1.000 28.20733  ? 154 HIS   A NE2 1 
ATOM   1074 N N   . ASN   A 1 148 ? -6.11179  -9.68487  -36.42398 1.000 27.33265  ? 155 ASN   A N   1 
ATOM   1075 C CA  . ASN   A 1 148 ? -6.84406  -9.43663  -37.66981 1.000 26.80338  ? 155 ASN   A CA  1 
ATOM   1076 C C   . ASN   A 1 148 ? -5.95261  -9.54707  -38.90351 1.000 31.92943  ? 155 ASN   A C   1 
ATOM   1077 O O   . ASN   A 1 148 ? -6.44266  -9.87369  -39.98987 1.000 34.22154  ? 155 ASN   A O   1 
ATOM   1078 C CB  . ASN   A 1 148 ? -7.51318  -8.05727  -37.65654 1.000 28.28697  ? 155 ASN   A CB  1 
ATOM   1079 C CG  . ASN   A 1 148 ? -8.78062  -8.02266  -36.82730 1.000 33.60117  ? 155 ASN   A CG  1 
ATOM   1080 O OD1 . ASN   A 1 148 ? -9.40595  -9.05390  -36.58215 1.000 34.84334  ? 155 ASN   A OD1 1 
ATOM   1081 N ND2 . ASN   A 1 148 ? -9.18827  -6.82240  -36.41996 1.000 33.12911  ? 155 ASN   A ND2 1 
ATOM   1082 N N   . ASP   A 1 149 ? -4.65334  -9.28646  -38.76670 1.000 34.44681  ? 156 ASP   A N   1 
ATOM   1083 C CA  . ASP   A 1 149 ? -3.75004  -9.22145  -39.90994 1.000 36.78298  ? 156 ASP   A CA  1 
ATOM   1084 C C   . ASP   A 1 149 ? -2.96210  -10.50704 -40.14291 1.000 34.98990  ? 156 ASP   A C   1 
ATOM   1085 O O   . ASP   A 1 149 ? -2.07016  -10.51941 -40.99726 1.000 34.90662  ? 156 ASP   A O   1 
ATOM   1086 C CB  . ASP   A 1 149 ? -2.77407  -8.05140  -39.74607 1.000 34.58429  ? 156 ASP   A CB  1 
ATOM   1087 C CG  . ASP   A 1 149 ? -3.47301  -6.70545  -39.70362 1.000 42.40089  ? 156 ASP   A CG  1 
ATOM   1088 O OD1 . ASP   A 1 149 ? -4.64399  -6.62907  -40.12729 1.000 39.02900  ? 156 ASP   A OD1 1 
ATOM   1089 O OD2 . ASP   A 1 149 ? -2.84880  -5.72526  -39.24313 1.000 45.28674  ? 156 ASP   A OD2 1 
ATOM   1090 N N   . ASP   A 1 150 ? -3.26028  -11.58352 -39.41855 1.000 31.32280  ? 157 ASP   A N   1 
ATOM   1091 C CA  . ASP   A 1 150 ? -2.47026  -12.80547 -39.52478 1.000 32.14996  ? 157 ASP   A CA  1 
ATOM   1092 C C   . ASP   A 1 150 ? -3.37187  -14.00580 -39.25183 1.000 38.93381  ? 157 ASP   A C   1 
ATOM   1093 O O   . ASP   A 1 150 ? -4.55829  -13.86299 -38.94350 1.000 33.50582  ? 157 ASP   A O   1 
ATOM   1094 C CB  . ASP   A 1 150 ? -1.27108  -12.75898 -38.56513 1.000 28.08246  ? 157 ASP   A CB  1 
ATOM   1095 C CG  . ASP   A 1 150 ? -0.07139  -13.54062 -39.07832 1.000 34.70547  ? 157 ASP   A CG  1 
ATOM   1096 O OD1 . ASP   A 1 150 ? -0.21393  -14.28453 -40.07194 1.000 33.64593  ? 157 ASP   A OD1 1 
ATOM   1097 O OD2 . ASP   A 1 150 ? 1.02623   -13.39404 -38.49681 1.000 35.24133  ? 157 ASP   A OD2 1 
ATOM   1098 N N   . GLU   A 1 151 ? -2.80056  -15.19875 -39.38056 1.000 32.18471  ? 158 GLU   A N   1 
ATOM   1099 C CA  . GLU   A 1 151 ? -3.51474  -16.43549 -39.10395 1.000 35.86337  ? 158 GLU   A CA  1 
ATOM   1100 C C   . GLU   A 1 151 ? -3.37530  -16.82069 -37.63314 1.000 26.73919  ? 158 GLU   A C   1 
ATOM   1101 O O   . GLU   A 1 151 ? -2.64262  -16.19639 -36.86235 1.000 29.73650  ? 158 GLU   A O   1 
ATOM   1102 C CB  . GLU   A 1 151 ? -3.00437  -17.56514 -39.99835 1.000 34.74127  ? 158 GLU   A CB  1 
ATOM   1103 C CG  . GLU   A 1 151 ? -2.53018  -17.10797 -41.36397 1.000 48.58385  ? 158 GLU   A CG  1 
ATOM   1104 C CD  . GLU   A 1 151 ? -3.68071  -16.86869 -42.32231 1.000 77.52765  ? 158 GLU   A CD  1 
ATOM   1105 O OE1 . GLU   A 1 151 ? -3.49698  -16.11255 -43.30091 1.000 89.41777  ? 158 GLU   A OE1 1 
ATOM   1106 O OE2 . GLU   A 1 151 ? -4.77052  -17.43592 -42.09351 1.000 83.14847  ? 158 GLU   A OE2 1 
ATOM   1107 N N   . GLN   A 1 152 ? -4.09360  -17.87263 -37.24650 1.000 25.67943  ? 159 GLN   A N   1 
ATOM   1108 C CA  . GLN   A 1 152 ? -4.08320  -18.32367 -35.86083 1.000 24.24785  ? 159 GLN   A CA  1 
ATOM   1109 C C   . GLN   A 1 152 ? -2.83589  -19.15745 -35.59451 1.000 27.88444  ? 159 GLN   A C   1 
ATOM   1110 O O   . GLN   A 1 152 ? -2.54738  -20.10743 -36.33034 1.000 27.30933  ? 159 GLN   A O   1 
ATOM   1111 C CB  . GLN   A 1 152 ? -5.34043  -19.13425 -35.54921 1.000 28.45354  ? 159 GLN   A CB  1 
ATOM   1112 C CG  . GLN   A 1 152 ? -5.54724  -19.41933 -34.06035 1.000 25.78305  ? 159 GLN   A CG  1 
ATOM   1113 C CD  . GLN   A 1 152 ? -6.97193  -19.85239 -33.76121 1.000 35.75716  ? 159 GLN   A CD  1 
ATOM   1114 O OE1 . GLN   A 1 152 ? -7.92253  -19.14389 -34.08699 1.000 36.75413  ? 159 GLN   A OE1 1 
ATOM   1115 N NE2 . GLN   A 1 152 ? -7.12662  -21.01874 -33.14433 1.000 32.38502  ? 159 GLN   A NE2 1 
ATOM   1116 N N   . TYR   A 1 153 ? -2.09613  -18.79513 -34.54406 1.000 25.09133  ? 160 TYR   A N   1 
ATOM   1117 C CA  . TYR   A 1 153 ? -0.83288  -19.44045 -34.20553 1.000 25.81756  ? 160 TYR   A CA  1 
ATOM   1118 C C   . TYR   A 1 153 ? -0.82428  -19.92128 -32.76168 1.000 26.67646  ? 160 TYR   A C   1 
ATOM   1119 O O   . TYR   A 1 153 ? -1.51450  -19.37057 -31.89897 1.000 21.89079  ? 160 TYR   A O   1 
ATOM   1120 C CB  . TYR   A 1 153 ? 0.35301   -18.49720 -34.42128 1.000 25.20847  ? 160 TYR   A CB  1 
ATOM   1121 C CG  . TYR   A 1 153 ? 0.71307   -18.34788 -35.87273 1.000 27.17983  ? 160 TYR   A CG  1 
ATOM   1122 C CD1 . TYR   A 1 153 ? 1.48804   -19.30582 -36.51076 1.000 29.93232  ? 160 TYR   A CD1 1 
ATOM   1123 C CD2 . TYR   A 1 153 ? 0.25827   -17.26647 -36.61572 1.000 33.32477  ? 160 TYR   A CD2 1 
ATOM   1124 C CE1 . TYR   A 1 153 ? 1.81272   -19.18547 -37.84986 1.000 34.59119  ? 160 TYR   A CE1 1 
ATOM   1125 C CE2 . TYR   A 1 153 ? 0.57672   -17.13914 -37.95822 1.000 33.07650  ? 160 TYR   A CE2 1 
ATOM   1126 C CZ  . TYR   A 1 153 ? 1.35697   -18.10108 -38.56582 1.000 37.48319  ? 160 TYR   A CZ  1 
ATOM   1127 O OH  . TYR   A 1 153 ? 1.68166   -17.98488 -39.89774 1.000 45.35332  ? 160 TYR   A OH  1 
ATOM   1128 N N   . ALA   A 1 154 ? -0.00388  -20.94335 -32.50640 1.000 21.84072  ? 161 ALA   A N   1 
ATOM   1129 C CA  . ALA   A 1 154 ? 0.19872   -21.49282 -31.17037 1.000 22.22233  ? 161 ALA   A CA  1 
ATOM   1130 C C   . ALA   A 1 154 ? 1.66704   -21.35964 -30.79150 1.000 25.35958  ? 161 ALA   A C   1 
ATOM   1131 O O   . ALA   A 1 154 ? 2.54457   -21.86381 -31.50268 1.000 26.60427  ? 161 ALA   A O   1 
ATOM   1132 C CB  . ALA   A 1 154 ? -0.23562  -22.95732 -31.10176 1.000 25.41454  ? 161 ALA   A CB  1 
ATOM   1133 N N   . TRP   A 1 155 ? 1.91951   -20.68368 -29.67740 1.000 20.77649  ? 162 TRP   A N   1 
ATOM   1134 C CA  . TRP   A 1 155 ? 3.23291   -20.55691 -29.05873 1.000 23.09147  ? 162 TRP   A CA  1 
ATOM   1135 C C   . TRP   A 1 155 ? 3.27257   -21.47669 -27.84619 1.000 23.25109  ? 162 TRP   A C   1 
ATOM   1136 O O   . TRP   A 1 155 ? 2.25504   -21.65545 -27.17290 1.000 21.93963  ? 162 TRP   A O   1 
ATOM   1137 C CB  . TRP   A 1 155 ? 3.44589   -19.09388 -28.65602 1.000 20.91741  ? 162 TRP   A CB  1 
ATOM   1138 C CG  . TRP   A 1 155 ? 4.70413   -18.71495 -27.92686 1.000 20.18226  ? 162 TRP   A CG  1 
ATOM   1139 C CD1 . TRP   A 1 155 ? 5.77347   -18.04796 -28.45062 1.000 20.86023  ? 162 TRP   A CD1 1 
ATOM   1140 C CD2 . TRP   A 1 155 ? 4.98635   -18.88703 -26.52572 1.000 21.30588  ? 162 TRP   A CD2 1 
ATOM   1141 N NE1 . TRP   A 1 155 ? 6.71569   -17.82320 -27.47435 1.000 19.70856  ? 162 TRP   A NE1 1 
ATOM   1142 C CE2 . TRP   A 1 155 ? 6.25677   -18.32820 -26.28592 1.000 20.40969  ? 162 TRP   A CE2 1 
ATOM   1143 C CE3 . TRP   A 1 155 ? 4.29556   -19.47520 -25.45805 1.000 19.64500  ? 162 TRP   A CE3 1 
ATOM   1144 C CZ2 . TRP   A 1 155 ? 6.85839   -18.34500 -25.02372 1.000 24.06415  ? 162 TRP   A CZ2 1 
ATOM   1145 C CZ3 . TRP   A 1 155 ? 4.89355   -19.48504 -24.20300 1.000 22.66400  ? 162 TRP   A CZ3 1 
ATOM   1146 C CH2 . TRP   A 1 155 ? 6.15962   -18.91973 -23.99823 1.000 20.47379  ? 162 TRP   A CH2 1 
ATOM   1147 N N   . GLU   A 1 156 ? 4.43119   -22.07991 -27.57169 1.000 20.33984  ? 163 GLU   A N   1 
ATOM   1148 C CA  . GLU   A 1 156 ? 4.51356   -22.97789 -26.42604 1.000 21.69226  ? 163 GLU   A CA  1 
ATOM   1149 C C   . GLU   A 1 156 ? 5.92385   -22.99776 -25.85846 1.000 21.87289  ? 163 GLU   A C   1 
ATOM   1150 O O   . GLU   A 1 156 ? 6.89863   -22.98640 -26.61202 1.000 21.16618  ? 163 GLU   A O   1 
ATOM   1151 C CB  . GLU   A 1 156 ? 4.10601   -24.40075 -26.81147 1.000 28.46764  ? 163 GLU   A CB  1 
ATOM   1152 C CG  . GLU   A 1 156 ? 3.69610   -25.27303 -25.64206 1.000 31.50108  ? 163 GLU   A CG  1 
ATOM   1153 C CD  . GLU   A 1 156 ? 2.93917   -26.50696 -26.09752 1.000 38.57098  ? 163 GLU   A CD  1 
ATOM   1154 O OE1 . GLU   A 1 156 ? 3.56021   -27.37742 -26.74543 1.000 41.50064  ? 163 GLU   A OE1 1 
ATOM   1155 O OE2 . GLU   A 1 156 ? 1.72192   -26.60114 -25.82342 1.000 37.40292  ? 163 GLU   A OE2 1 
ATOM   1156 N N   . SER   A 1 157 ? 6.02702   -23.06529 -24.53099 1.000 23.48942  ? 164 SER   A N   1 
ATOM   1157 C CA  . SER   A 1 157 ? 7.33551   -23.21885 -23.90900 1.000 20.84435  ? 164 SER   A CA  1 
ATOM   1158 C C   . SER   A 1 157 ? 7.19271   -23.86041 -22.53461 1.000 21.21969  ? 164 SER   A C   1 
ATOM   1159 O O   . SER   A 1 157 ? 6.29702   -23.50497 -21.75942 1.000 21.43902  ? 164 SER   A O   1 
ATOM   1160 C CB  . SER   A 1 157 ? 8.06263   -21.87467 -23.78931 1.000 19.77356  ? 164 SER   A CB  1 
ATOM   1161 O OG  . SER   A 1 157 ? 9.33537   -22.04747 -23.17640 1.000 22.45075  ? 164 SER   A OG  1 
ATOM   1162 N N   . SER   A 1 158 ? 8.07839   -24.81651 -22.25313 1.000 22.16415  ? 165 SER   A N   1 
ATOM   1163 C CA  . SER   A 1 158 ? 8.30431   -25.32768 -20.90593 1.000 21.93861  ? 165 SER   A CA  1 
ATOM   1164 C C   . SER   A 1 158 ? 9.55352   -24.71682 -20.28062 1.000 23.12499  ? 165 SER   A C   1 
ATOM   1165 O O   . SER   A 1 158 ? 10.17645  -25.32800 -19.39943 1.000 25.87818  ? 165 SER   A O   1 
ATOM   1166 C CB  . SER   A 1 158 ? 8.41219   -26.85163 -20.92757 1.000 27.34873  ? 165 SER   A CB  1 
ATOM   1167 O OG  . SER   A 1 158 ? 7.19278   -27.44291 -21.34036 1.000 30.90095  ? 165 SER   A OG  1 
ATOM   1168 N N   . ALA   A 1 159 ? 9.93037   -23.52696 -20.73505 1.000 22.04835  ? 166 ALA   A N   1 
ATOM   1169 C CA  . ALA   A 1 159 ? 11.15448  -22.82551 -20.31808 1.000 24.66706  ? 166 ALA   A CA  1 
ATOM   1170 C C   . ALA   A 1 159 ? 12.33675  -23.66911 -20.80380 1.000 25.06035  ? 166 ALA   A C   1 
ATOM   1171 O O   . ALA   A 1 159 ? 12.26198  -24.26806 -21.88672 1.000 31.44987  ? 166 ALA   A O   1 
ATOM   1172 C CB  . ALA   A 1 159 ? 11.12600  -22.53950 -18.83232 1.000 27.28564  ? 166 ALA   A CB  1 
ATOM   1173 N N   . GLY   A 1 160 ? 13.43671  -23.73153 -20.06001 1.000 29.24769  ? 167 GLY   A N   1 
ATOM   1174 C CA  . GLY   A 1 160 ? 14.57929  -24.48111 -20.54314 1.000 25.97691  ? 167 GLY   A CA  1 
ATOM   1175 C C   . GLY   A 1 160 ? 15.25596  -23.89501 -21.76310 1.000 25.32391  ? 167 GLY   A C   1 
ATOM   1176 O O   . GLY   A 1 160 ? 16.07466  -24.57164 -22.38830 1.000 31.06074  ? 167 GLY   A O   1 
ATOM   1177 N N   . GLY   A 1 161 ? 14.92876  -22.65706 -22.13145 1.000 23.20307  ? 168 GLY   A N   1 
ATOM   1178 C CA  . GLY   A 1 161 ? 15.67868  -21.92997 -23.13667 1.000 25.62345  ? 168 GLY   A CA  1 
ATOM   1179 C C   . GLY   A 1 161 ? 15.09468  -21.90061 -24.53541 1.000 22.76540  ? 168 GLY   A C   1 
ATOM   1180 O O   . GLY   A 1 161 ? 15.70004  -21.28040 -25.41694 1.000 24.95276  ? 168 GLY   A O   1 
ATOM   1181 N N   . SER   A 1 162 ? 13.95209  -22.54273 -24.77600 1.000 21.70917  ? 169 SER   A N   1 
ATOM   1182 C CA  . SER   A 1 162 ? 13.40127  -22.61004 -26.12347 1.000 20.16060  ? 169 SER   A CA  1 
ATOM   1183 C C   . SER   A 1 162 ? 11.88416  -22.49664 -26.07758 1.000 21.41356  ? 169 SER   A C   1 
ATOM   1184 O O   . SER   A 1 162 ? 11.24574  -22.80024 -25.06612 1.000 21.48950  ? 169 SER   A O   1 
ATOM   1185 C CB  . SER   A 1 162 ? 13.80152  -23.90980 -26.83465 1.000 24.19679  ? 169 SER   A CB  1 
ATOM   1186 O OG  . SER   A 1 162 ? 13.26008  -25.03856 -26.17223 1.000 26.78164  ? 169 SER   A OG  1 
ATOM   1187 N N   . PHE   A 1 163 ? 11.31682  -22.05170 -27.20152 1.000 23.52007  ? 170 PHE   A N   1 
ATOM   1188 C CA  . PHE   A 1 163 ? 9.87639   -22.04328 -27.41519 1.000 22.46463  ? 170 PHE   A CA  1 
ATOM   1189 C C   . PHE   A 1 163 ? 9.59239   -22.51202 -28.83649 1.000 22.84511  ? 170 PHE   A C   1 
ATOM   1190 O O   . PHE   A 1 163 ? 10.46890  -22.48713 -29.70398 1.000 23.33685  ? 170 PHE   A O   1 
ATOM   1191 C CB  . PHE   A 1 163 ? 9.24880   -20.65545 -27.17282 1.000 21.47990  ? 170 PHE   A CB  1 
ATOM   1192 C CG  . PHE   A 1 163 ? 9.74349   -19.56714 -28.09851 1.000 21.96587  ? 170 PHE   A CG  1 
ATOM   1193 C CD1 . PHE   A 1 163 ? 10.88455  -18.84244 -27.79679 1.000 24.56179  ? 170 PHE   A CD1 1 
ATOM   1194 C CD2 . PHE   A 1 163 ? 9.04086   -19.24436 -29.25258 1.000 21.19585  ? 170 PHE   A CD2 1 
ATOM   1195 C CE1 . PHE   A 1 163 ? 11.32543  -17.82698 -28.63686 1.000 22.86869  ? 170 PHE   A CE1 1 
ATOM   1196 C CE2 . PHE   A 1 163 ? 9.47707   -18.23269 -30.09508 1.000 25.62482  ? 170 PHE   A CE2 1 
ATOM   1197 C CZ  . PHE   A 1 163 ? 10.61692  -17.52024 -29.78551 1.000 22.42921  ? 170 PHE   A CZ  1 
ATOM   1198 N N   . THR   A 1 164 ? 8.35805   -22.95798 -29.06863 1.000 21.28824  ? 171 THR   A N   1 
ATOM   1199 C CA  . THR   A 1 164 ? 7.93410   -23.38440 -30.39567 1.000 20.74766  ? 171 THR   A CA  1 
ATOM   1200 C C   . THR   A 1 164 ? 6.77674   -22.52743 -30.88972 1.000 20.64792  ? 171 THR   A C   1 
ATOM   1201 O O   . THR   A 1 164 ? 5.99894   -21.97831 -30.09897 1.000 21.23628  ? 171 THR   A O   1 
ATOM   1202 C CB  . THR   A 1 164 ? 7.51825   -24.87227 -30.43338 1.000 24.94143  ? 171 THR   A CB  1 
ATOM   1203 O OG1 . THR   A 1 164 ? 6.36603   -25.07948 -29.60436 1.000 29.11413  ? 171 THR   A OG1 1 
ATOM   1204 C CG2 . THR   A 1 164 ? 8.66037   -25.78460 -29.98778 1.000 26.24855  ? 171 THR   A CG2 1 
ATOM   1205 N N   . VAL   A 1 165 ? 6.67334   -22.41715 -32.21417 1.000 22.66408  ? 172 VAL   A N   1 
ATOM   1206 C CA  . VAL   A 1 165 ? 5.55902   -21.73508 -32.86200 1.000 27.47744  ? 172 VAL   A CA  1 
ATOM   1207 C C   . VAL   A 1 165 ? 5.08095   -22.60873 -34.01205 1.000 27.35190  ? 172 VAL   A C   1 
ATOM   1208 O O   . VAL   A 1 165 ? 5.89250   -23.11705 -34.79512 1.000 27.34969  ? 172 VAL   A O   1 
ATOM   1209 C CB  . VAL   A 1 165 ? 5.94137   -20.32924 -33.37106 1.000 25.37754  ? 172 VAL   A CB  1 
ATOM   1210 C CG1 . VAL   A 1 165 ? 4.78143   -19.70455 -34.14622 1.000 29.17948  ? 172 VAL   A CG1 1 
ATOM   1211 C CG2 . VAL   A 1 165 ? 6.35361   -19.42946 -32.22379 1.000 22.38829  ? 172 VAL   A CG2 1 
ATOM   1212 N N   . ARG   A 1 166 ? 3.76612   -22.78806 -34.10585 1.000 23.35154  ? 173 ARG   A N   1 
ATOM   1213 C CA  . ARG   A 1 166 ? 3.15469   -23.53906 -35.19045 1.000 26.10465  ? 173 ARG   A CA  1 
ATOM   1214 C C   . ARG   A 1 166 ? 1.82301   -22.89188 -35.53326 1.000 26.55523  ? 173 ARG   A C   1 
ATOM   1215 O O   . ARG   A 1 166 ? 1.23391   -22.17449 -34.71973 1.000 26.11944  ? 173 ARG   A O   1 
ATOM   1216 C CB  . ARG   A 1 166 ? 2.94150   -25.00857 -34.81002 1.000 30.72985  ? 173 ARG   A CB  1 
ATOM   1217 C CG  . ARG   A 1 166 ? 1.99880   -25.19767 -33.62290 1.000 30.90334  ? 173 ARG   A CG  1 
ATOM   1218 C CD  . ARG   A 1 166 ? 2.16733   -26.57367 -33.00200 1.000 47.85370  ? 173 ARG   A CD  1 
ATOM   1219 N NE  . ARG   A 1 166 ? 3.27963   -26.60376 -32.05993 1.000 44.02105  ? 173 ARG   A NE  1 
ATOM   1220 C CZ  . ARG   A 1 166 ? 3.83690   -27.71172 -31.59038 1.000 52.40686  ? 173 ARG   A CZ  1 
ATOM   1221 N NH1 . ARG   A 1 166 ? 3.41743   -28.90931 -31.96551 1.000 46.35959  ? 173 ARG   A NH1 1 
ATOM   1222 N NH2 . ARG   A 1 166 ? 4.84521   -27.61537 -30.72767 1.000 43.67165  ? 173 ARG   A NH2 1 
ATOM   1223 N N   . THR   A 1 167 ? 1.35879   -23.14363 -36.75328 1.000 29.09553  ? 174 THR   A N   1 
ATOM   1224 C CA  . THR   A 1 167 ? -0.01704  -22.80877 -37.09567 1.000 31.01653  ? 174 THR   A CA  1 
ATOM   1225 C C   . THR   A 1 167 ? -0.95417  -23.62030 -36.21068 1.000 36.50718  ? 174 THR   A C   1 
ATOM   1226 O O   . THR   A 1 167 ? -0.73926  -24.81551 -35.99434 1.000 34.23328  ? 174 THR   A O   1 
ATOM   1227 C CB  . THR   A 1 167 ? -0.28929  -23.09683 -38.57302 1.000 38.04706  ? 174 THR   A CB  1 
ATOM   1228 O OG1 . THR   A 1 167 ? 0.55260   -22.27273 -39.38821 1.000 39.52893  ? 174 THR   A OG1 1 
ATOM   1229 C CG2 . THR   A 1 167 ? -1.74509  -22.80852 -38.91911 1.000 46.37993  ? 174 THR   A CG2 1 
ATOM   1230 N N   . ASP   A 1 168 ? -1.97690  -22.96800 -35.66875 1.000 32.23956  ? 175 ASP   A N   1 
ATOM   1231 C CA  . ASP   A 1 168 ? -2.89419  -23.65325 -34.76881 1.000 35.69126  ? 175 ASP   A CA  1 
ATOM   1232 C C   . ASP   A 1 168 ? -3.95126  -24.38949 -35.57670 1.000 45.55931  ? 175 ASP   A C   1 
ATOM   1233 O O   . ASP   A 1 168 ? -4.65457  -23.78326 -36.39191 1.000 44.00186  ? 175 ASP   A O   1 
ATOM   1234 C CB  . ASP   A 1 168 ? -3.55535  -22.67759 -33.80018 1.000 34.60554  ? 175 ASP   A CB  1 
ATOM   1235 C CG  . ASP   A 1 168 ? -4.46055  -23.38252 -32.80742 1.000 43.89782  ? 175 ASP   A CG  1 
ATOM   1236 O OD1 . ASP   A 1 168 ? -4.08923  -24.48244 -32.34599 1.000 50.18810  ? 175 ASP   A OD1 1 
ATOM   1237 O OD2 . ASP   A 1 168 ? -5.54968  -22.85403 -32.50409 1.000 43.25021  ? 175 ASP   A OD2 1 
ATOM   1238 N N   . THR   A 1 169 ? -4.06097  -25.69439 -35.34566 1.000 62.16006  ? 176 THR   A N   1 
ATOM   1239 C CA  . THR   A 1 169 ? -5.08302  -26.51875 -35.97070 1.000 66.04041  ? 176 THR   A CA  1 
ATOM   1240 C C   . THR   A 1 169 ? -6.38086  -26.55562 -35.17536 1.000 69.00732  ? 176 THR   A C   1 
ATOM   1241 O O   . THR   A 1 169 ? -7.39745  -27.02345 -35.69930 1.000 66.26133  ? 176 THR   A O   1 
ATOM   1242 C CB  . THR   A 1 169 ? -4.56273  -27.94901 -36.15200 1.000 68.42527  ? 176 THR   A CB  1 
ATOM   1243 O OG1 . THR   A 1 169 ? -3.90887  -28.37302 -34.94823 1.000 63.99794  ? 176 THR   A OG1 1 
ATOM   1244 C CG2 . THR   A 1 169 ? -3.57511  -28.01227 -37.30558 1.000 63.91771  ? 176 THR   A CG2 1 
ATOM   1245 N N   . GLY   A 1 170 ? -6.37336  -26.06673 -33.93731 1.000 59.75838  ? 177 GLY   A N   1 
ATOM   1246 C CA  . GLY   A 1 170 ? -7.51715  -26.18991 -33.05555 1.000 67.85766  ? 177 GLY   A CA  1 
ATOM   1247 C C   . GLY   A 1 170 ? -8.70224  -25.31032 -33.39675 1.000 55.13746  ? 177 GLY   A C   1 
ATOM   1248 O O   . GLY   A 1 170 ? -8.86999  -24.88625 -34.54470 1.000 49.31501  ? 177 GLY   A O   1 
ATOM   1249 N N   . GLU   A 1 171 ? -9.52882  -25.03380 -32.39301 1.000 53.41634  ? 178 GLU   A N   1 
ATOM   1250 C CA  . GLU   A 1 171 ? -10.75950 -24.28504 -32.60703 1.000 54.00791  ? 178 GLU   A CA  1 
ATOM   1251 C C   . GLU   A 1 171 ? -10.46085 -22.86947 -33.08863 1.000 47.49698  ? 178 GLU   A C   1 
ATOM   1252 O O   . GLU   A 1 171 ? -9.60773  -22.18887 -32.50354 1.000 42.31599  ? 178 GLU   A O   1 
ATOM   1253 C CB  . GLU   A 1 171 ? -11.57809 -24.24170 -31.31723 1.000 51.70285  ? 178 GLU   A CB  1 
ATOM   1254 C CG  . GLU   A 1 171 ? -13.01564 -24.67599 -31.49178 1.000 64.80316  ? 178 GLU   A CG  1 
ATOM   1255 C CD  . GLU   A 1 171 ? -13.14421 -26.07951 -32.04342 1.000 53.89823  ? 178 GLU   A CD  1 
ATOM   1256 O OE1 . GLU   A 1 171 ? -13.55453 -26.21691 -33.21325 1.000 66.76339  ? 178 GLU   A OE1 1 
ATOM   1257 O OE2 . GLU   A 1 171 ? -12.83339 -27.04353 -31.31567 1.000 68.67354  ? 178 GLU   A OE2 1 
ATOM   1258 N N   . PRO   A 1 172 ? -11.11392 -22.40362 -34.15281 1.000 42.40521  ? 179 PRO   A N   1 
ATOM   1259 C CA  . PRO   A 1 172 ? -10.96214 -21.00133 -34.54695 1.000 44.43371  ? 179 PRO   A CA  1 
ATOM   1260 C C   . PRO   A 1 172 ? -11.39547 -20.07757 -33.41900 1.000 53.90979  ? 179 PRO   A C   1 
ATOM   1261 O O   . PRO   A 1 172 ? -12.35084 -20.35856 -32.69279 1.000 53.45811  ? 179 PRO   A O   1 
ATOM   1262 C CB  . PRO   A 1 172 ? -11.87702 -20.87734 -35.76705 1.000 46.80212  ? 179 PRO   A CB  1 
ATOM   1263 C CG  . PRO   A 1 172 ? -11.91013 -22.25971 -36.34777 1.000 54.07228  ? 179 PRO   A CG  1 
ATOM   1264 C CD  . PRO   A 1 172 ? -11.83395 -23.19528 -35.16735 1.000 53.50124  ? 179 PRO   A CD  1 
ATOM   1265 N N   . MET   A 1 173 ? -10.67040 -18.96543 -33.27966 1.000 37.90695  ? 180 MET   A N   1 
ATOM   1266 C CA  . MET   A 1 173 ? -10.86927 -18.00644 -32.19940 1.000 41.82368  ? 180 MET   A CA  1 
ATOM   1267 C C   . MET   A 1 173 ? -11.57781 -16.71882 -32.61837 1.000 44.34553  ? 180 MET   A C   1 
ATOM   1268 O O   . MET   A 1 173 ? -12.19520 -16.07962 -31.76229 1.000 54.37891  ? 180 MET   A O   1 
ATOM   1269 C CB  . MET   A 1 173 ? -9.50738  -17.66451 -31.56680 1.000 39.08678  ? 180 MET   A CB  1 
ATOM   1270 C CG  . MET   A 1 173 ? -9.00838  -18.68498 -30.54944 1.000 51.26328  ? 180 MET   A CG  1 
ATOM   1271 S SD  . MET   A 1 173 ? -7.29191  -18.33779 -30.20771 1.000 51.47163  ? 180 MET   A SD  1 
ATOM   1272 C CE  . MET   A 1 173 ? -7.26093  -16.60922 -30.61580 1.000 43.79108  ? 180 MET   A CE  1 
ATOM   1273 N N   . GLY   A 1 174 ? -11.51322 -16.32763 -33.88666 1.000 35.16478  ? 181 GLY   A N   1 
ATOM   1274 C CA  . GLY   A 1 174 ? -12.07439 -15.06444 -34.30899 1.000 35.00156  ? 181 GLY   A CA  1 
ATOM   1275 C C   . GLY   A 1 174 ? -11.05674 -13.95112 -34.18487 1.000 26.97509  ? 181 GLY   A C   1 
ATOM   1276 O O   . GLY   A 1 174 ? -10.58628 -13.40694 -35.19034 1.000 32.25100  ? 181 GLY   A O   1 
ATOM   1277 N N   . ARG   A 1 175 ? -10.69095 -13.62912 -32.94172 1.000 24.09716  ? 182 ARG   A N   1 
ATOM   1278 C CA  . ARG   A 1 175 ? -9.70733  -12.59844 -32.63274 1.000 25.69122  ? 182 ARG   A CA  1 
ATOM   1279 C C   . ARG   A 1 175 ? -9.39914  -12.62737 -31.14373 1.000 26.65783  ? 182 ARG   A C   1 
ATOM   1280 O O   . ARG   A 1 175 ? -10.32098 -12.69250 -30.32806 1.000 25.36003  ? 182 ARG   A O   1 
ATOM   1281 C CB  . ARG   A 1 175 ? -10.21220 -11.20079 -33.00964 1.000 23.57794  ? 182 ARG   A CB  1 
ATOM   1282 C CG  . ARG   A 1 175 ? -9.12716  -10.13442 -32.85787 1.000 28.83711  ? 182 ARG   A CG  1 
ATOM   1283 C CD  . ARG   A 1 175 ? -9.69105  -8.71783  -32.72196 1.000 26.62579  ? 182 ARG   A CD  1 
ATOM   1284 N NE  . ARG   A 1 175 ? -10.59738 -8.58293  -31.58255 1.000 23.67701  ? 182 ARG   A NE  1 
ATOM   1285 C CZ  . ARG   A 1 175 ? -11.91797 -8.49280  -31.66719 1.000 25.14027  ? 182 ARG   A CZ  1 
ATOM   1286 N NH1 . ARG   A 1 175 ? -12.54137 -8.49899  -32.83467 1.000 27.03602  ? 182 ARG   A NH1 1 
ATOM   1287 N NH2 . ARG   A 1 175 ? -12.63473 -8.39360  -30.54919 1.000 25.60856  ? 182 ARG   A NH2 1 
ATOM   1288 N N   . GLY   A 1 176 ? -8.12287  -12.56540 -30.77142 1.000 24.42773  ? 183 GLY   A N   1 
ATOM   1289 C CA  . GLY   A 1 176 ? -7.79830  -12.48567 -29.36535 1.000 22.53260  ? 183 GLY   A CA  1 
ATOM   1290 C C   . GLY   A 1 176 ? -6.70237  -13.45586 -29.00839 1.000 23.37495  ? 183 GLY   A C   1 
ATOM   1291 O O   . GLY   A 1 176 ? -5.98462  -13.96238 -29.87753 1.000 24.51638  ? 183 GLY   A O   1 
ATOM   1292 N N   . THR   A 1 177 ? -6.57751  -13.72311 -27.71127 1.000 19.41648  ? 184 THR   A N   1 
ATOM   1293 C CA  . THR   A 1 177 ? -5.49234  -14.55472 -27.21456 1.000 22.38404  ? 184 THR   A CA  1 
ATOM   1294 C C   . THR   A 1 177 ? -5.98981  -15.45984 -26.10065 1.000 25.09251  ? 184 THR   A C   1 
ATOM   1295 O O   . THR   A 1 177 ? -6.81455  -15.05793 -25.27391 1.000 22.51134  ? 184 THR   A O   1 
ATOM   1296 C CB  . THR   A 1 177 ? -4.32009  -13.69835 -26.71588 1.000 25.99026  ? 184 THR   A CB  1 
ATOM   1297 O OG1 . THR   A 1 177 ? -3.84625  -12.88215 -27.78975 1.000 24.99263  ? 184 THR   A OG1 1 
ATOM   1298 C CG2 . THR   A 1 177 ? -3.17011  -14.57695 -26.23697 1.000 28.79895  ? 184 THR   A CG2 1 
ATOM   1299 N N   . LYS   A 1 178 ? -5.46818  -16.68274 -26.09275 1.000 21.24226  ? 185 LYS   A N   1 
ATOM   1300 C CA  . LYS   A 1 178 ? -5.75210  -17.69396 -25.08436 1.000 22.62705  ? 185 LYS   A CA  1 
ATOM   1301 C C   . LYS   A 1 178 ? -4.43216  -18.10411 -24.44097 1.000 19.93796  ? 185 LYS   A C   1 
ATOM   1302 O O   . LYS   A 1 178 ? -3.53642  -18.59831 -25.13328 1.000 23.67828  ? 185 LYS   A O   1 
ATOM   1303 C CB  . LYS   A 1 178 ? -6.43645  -18.89058 -25.75027 1.000 28.13462  ? 185 LYS   A CB  1 
ATOM   1304 C CG  . LYS   A 1 178 ? -6.58732  -20.13497 -24.92380 1.000 30.64862  ? 185 LYS   A CG  1 
ATOM   1305 C CD  . LYS   A 1 178 ? -7.40092  -21.17246 -25.69852 1.000 46.09053  ? 185 LYS   A CD  1 
ATOM   1306 C CE  . LYS   A 1 178 ? -8.60124  -20.52915 -26.37759 1.000 40.21656  ? 185 LYS   A CE  1 
ATOM   1307 N NZ  . LYS   A 1 178 ? -9.45855  -21.51830 -27.09333 1.000 60.78381  ? 185 LYS   A NZ  1 
ATOM   1308 N N   . VAL   A 1 179 ? -4.29958  -17.89178 -23.13139 1.000 21.25786  ? 186 VAL   A N   1 
ATOM   1309 C CA  . VAL   A 1 179 ? -3.11325  -18.32246 -22.38816 1.000 20.77651  ? 186 VAL   A CA  1 
ATOM   1310 C C   . VAL   A 1 179 ? -3.48507  -19.56170 -21.58309 1.000 23.39295  ? 186 VAL   A C   1 
ATOM   1311 O O   . VAL   A 1 179 ? -4.28980  -19.48938 -20.64974 1.000 22.21855  ? 186 VAL   A O   1 
ATOM   1312 C CB  . VAL   A 1 179 ? -2.56605  -17.21349 -21.47734 1.000 20.40238  ? 186 VAL   A CB  1 
ATOM   1313 C CG1 . VAL   A 1 179 ? -1.37403  -17.72246 -20.67807 1.000 19.87831  ? 186 VAL   A CG1 1 
ATOM   1314 C CG2 . VAL   A 1 179 ? -2.14502  -16.00430 -22.29863 1.000 21.63088  ? 186 VAL   A CG2 1 
ATOM   1315 N N   . ILE   A 1 180 ? -2.88902  -20.69937 -21.92488 1.000 21.73151  ? 187 ILE   A N   1 
ATOM   1316 C CA  . ILE   A 1 180 ? -3.17651  -21.96810 -21.26407 1.000 21.71099  ? 187 ILE   A CA  1 
ATOM   1317 C C   . ILE   A 1 180 ? -2.03161  -22.26420 -20.30367 1.000 20.36155  ? 187 ILE   A C   1 
ATOM   1318 O O   . ILE   A 1 180 ? -0.89294  -22.48442 -20.72673 1.000 21.05234  ? 187 ILE   A O   1 
ATOM   1319 C CB  . ILE   A 1 180 ? -3.36459  -23.10553 -22.27474 1.000 21.09606  ? 187 ILE   A CB  1 
ATOM   1320 C CG1 . ILE   A 1 180 ? -4.44244  -22.73458 -23.29653 1.000 26.15404  ? 187 ILE   A CG1 1 
ATOM   1321 C CG2 . ILE   A 1 180 ? -3.70863  -24.40656 -21.54546 1.000 24.00159  ? 187 ILE   A CG2 1 
ATOM   1322 C CD1 . ILE   A 1 180 ? -4.49929  -23.66406 -24.49075 1.000 30.33797  ? 187 ILE   A CD1 1 
ATOM   1323 N N   . LEU   A 1 181 ? -2.33036  -22.27205 -19.00684 1.000 19.22571  ? 188 LEU   A N   1 
ATOM   1324 C CA  . LEU   A 1 181 ? -1.34045  -22.55081 -17.97064 1.000 22.26459  ? 188 LEU   A CA  1 
ATOM   1325 C C   . LEU   A 1 181 ? -1.45200  -24.01682 -17.57964 1.000 24.20587  ? 188 LEU   A C   1 
ATOM   1326 O O   . LEU   A 1 181 ? -2.44086  -24.42321 -16.96466 1.000 22.56827  ? 188 LEU   A O   1 
ATOM   1327 C CB  . LEU   A 1 181 ? -1.55378  -21.65572 -16.75124 1.000 18.50543  ? 188 LEU   A CB  1 
ATOM   1328 C CG  . LEU   A 1 181 ? -1.64501  -20.15935 -17.02606 1.000 19.51868  ? 188 LEU   A CG  1 
ATOM   1329 C CD1 . LEU   A 1 181 ? -1.95884  -19.42303 -15.74599 1.000 26.59878  ? 188 LEU   A CD1 1 
ATOM   1330 C CD2 . LEU   A 1 181 ? -0.34261  -19.66752 -17.61586 1.000 24.29098  ? 188 LEU   A CD2 1 
ATOM   1331 N N   . HIS   A 1 182 ? -0.44076  -24.80752 -17.93063 1.000 22.38490  ? 189 HIS   A N   1 
ATOM   1332 C CA  . HIS   A 1 182 ? -0.35244  -26.19132 -17.46481 1.000 24.66481  ? 189 HIS   A CA  1 
ATOM   1333 C C   . HIS   A 1 182 ? 0.30269   -26.15583 -16.08915 1.000 23.21869  ? 189 HIS   A C   1 
ATOM   1334 O O   . HIS   A 1 182 ? 1.51746   -26.00305 -15.96777 1.000 23.83853  ? 189 HIS   A O   1 
ATOM   1335 C CB  . HIS   A 1 182 ? 0.41776   -27.05095 -18.46167 1.000 24.82119  ? 189 HIS   A CB  1 
ATOM   1336 C CG  . HIS   A 1 182 ? -0.10281  -26.95717 -19.86572 1.000 25.67188  ? 189 HIS   A CG  1 
ATOM   1337 N ND1 . HIS   A 1 182 ? -0.89274  -27.93499 -20.43308 1.000 35.24382  ? 189 HIS   A ND1 1 
ATOM   1338 C CD2 . HIS   A 1 182 ? 0.04058   -25.99608 -20.81043 1.000 32.48774  ? 189 HIS   A CD2 1 
ATOM   1339 C CE1 . HIS   A 1 182 ? -1.20942  -27.58341 -21.66695 1.000 32.41842  ? 189 HIS   A CE1 1 
ATOM   1340 N NE2 . HIS   A 1 182 ? -0.65524  -26.41045 -21.92121 1.000 33.11443  ? 189 HIS   A NE2 1 
ATOM   1341 N N   . LEU   A 1 183 ? -0.51242  -26.28061 -15.04501 1.000 22.63499  ? 190 LEU   A N   1 
ATOM   1342 C CA  . LEU   A 1 183 ? -0.07361  -25.93760 -13.69946 1.000 22.93394  ? 190 LEU   A CA  1 
ATOM   1343 C C   . LEU   A 1 183 ? 0.89885   -26.96776 -13.13539 1.000 28.18363  ? 190 LEU   A C   1 
ATOM   1344 O O   . LEU   A 1 183 ? 0.83067   -28.16249 -13.44170 1.000 26.39745  ? 190 LEU   A O   1 
ATOM   1345 C CB  . LEU   A 1 183 ? -1.27948  -25.81516 -12.76909 1.000 22.74213  ? 190 LEU   A CB  1 
ATOM   1346 C CG  . LEU   A 1 183 ? -2.25276  -24.68246 -13.09726 1.000 23.33691  ? 190 LEU   A CG  1 
ATOM   1347 C CD1 . LEU   A 1 183 ? -3.40467  -24.65409 -12.10333 1.000 25.96244  ? 190 LEU   A CD1 1 
ATOM   1348 C CD2 . LEU   A 1 183 ? -1.54213  -23.34284 -13.12798 1.000 27.52221  ? 190 LEU   A CD2 1 
ATOM   1349 N N   . LYS   A 1 184 ? 1.81795   -26.48553 -12.29976 1.000 27.71519  ? 191 LYS   A N   1 
ATOM   1350 C CA  . LYS   A 1 184 ? 2.66076   -27.38140 -11.52361 1.000 29.84056  ? 191 LYS   A CA  1 
ATOM   1351 C C   . LYS   A 1 184 ? 1.80656   -28.19090 -10.55709 1.000 31.86801  ? 191 LYS   A C   1 
ATOM   1352 O O   . LYS   A 1 184 ? 0.74254   -27.74990 -10.11475 1.000 29.24447  ? 191 LYS   A O   1 
ATOM   1353 C CB  . LYS   A 1 184 ? 3.72763   -26.60223 -10.74996 1.000 30.23538  ? 191 LYS   A CB  1 
ATOM   1354 C CG  . LYS   A 1 184 ? 4.68797   -25.79009 -11.61172 1.000 33.41996  ? 191 LYS   A CG  1 
ATOM   1355 C CD  . LYS   A 1 184 ? 5.35982   -24.69073 -10.78636 1.000 31.25431  ? 191 LYS   A CD  1 
ATOM   1356 C CE  . LYS   A 1 184 ? 6.55117   -24.09059 -11.51179 1.000 52.36623  ? 191 LYS   A CE  1 
ATOM   1357 N NZ  . LYS   A 1 184 ? 7.11585   -22.90671 -10.79770 1.000 51.96776  ? 191 LYS   A NZ  1 
ATOM   1358 N N   . GLU   A 1 185 ? 2.29591   -29.38662 -10.22392 1.000 31.11703  ? 192 GLU   A N   1 
ATOM   1359 C CA  . GLU   A 1 185 ? 1.50479   -30.33730 -9.44674  1.000 37.46649  ? 192 GLU   A CA  1 
ATOM   1360 C C   . GLU   A 1 185 ? 1.09621   -29.77879 -8.08597  1.000 38.00927  ? 192 GLU   A C   1 
ATOM   1361 O O   . GLU   A 1 185 ? 0.03348   -30.13747 -7.56501  1.000 41.98869  ? 192 GLU   A O   1 
ATOM   1362 C CB  . GLU   A 1 185 ? 2.28842   -31.64495 -9.29275  1.000 41.91226  ? 192 GLU   A CB  1 
ATOM   1363 C CG  . GLU   A 1 185 ? 2.20981   -32.29753 -7.92659  1.000 61.54865  ? 192 GLU   A CG  1 
ATOM   1364 C CD  . GLU   A 1 185 ? 2.85701   -33.66956 -7.90451  1.000 81.21309  ? 192 GLU   A CD  1 
ATOM   1365 O OE1 . GLU   A 1 185 ? 2.50684   -34.48025 -7.01958  1.000 81.11646  ? 192 GLU   A OE1 1 
ATOM   1366 O OE2 . GLU   A 1 185 ? 3.71112   -33.93877 -8.77616  1.000 80.68850  ? 192 GLU   A OE2 1 
ATOM   1367 N N   . ASP   A 1 186 ? 1.90270   -28.89323 -7.50042  1.000 37.13495  ? 193 ASP   A N   1 
ATOM   1368 C CA  . ASP   A 1 186 ? 1.59872   -28.33366 -6.18939  1.000 40.58725  ? 193 ASP   A CA  1 
ATOM   1369 C C   . ASP   A 1 186 ? 0.96231   -26.94734 -6.27059  1.000 35.26915  ? 193 ASP   A C   1 
ATOM   1370 O O   . ASP   A 1 186 ? 0.94298   -26.22156 -5.26918  1.000 33.19380  ? 193 ASP   A O   1 
ATOM   1371 C CB  . ASP   A 1 186 ? 2.85934   -28.29323 -5.32286  1.000 39.58654  ? 193 ASP   A CB  1 
ATOM   1372 C CG  . ASP   A 1 186 ? 3.92830   -27.36991 -5.87726  1.000 51.08636  ? 193 ASP   A CG  1 
ATOM   1373 O OD1 . ASP   A 1 186 ? 3.82057   -26.94819 -7.04918  1.000 50.36411  ? 193 ASP   A OD1 1 
ATOM   1374 O OD2 . ASP   A 1 186 ? 4.88641   -27.06612 -5.13511  1.000 66.81131  ? 193 ASP   A OD2 1 
ATOM   1375 N N   . GLN   A 1 187 ? 0.43237   -26.56953 -7.43511  1.000 29.27195  ? 194 GLN   A N   1 
ATOM   1376 C CA  . GLN   A 1 187 ? -0.19188  -25.26561 -7.62998  1.000 26.47653  ? 194 GLN   A CA  1 
ATOM   1377 C C   . GLN   A 1 187 ? -1.64590  -25.39696 -8.07936  1.000 24.12153  ? 194 GLN   A C   1 
ATOM   1378 O O   . GLN   A 1 187 ? -2.18309  -24.49935 -8.73471  1.000 26.61715  ? 194 GLN   A O   1 
ATOM   1379 C CB  . GLN   A 1 187 ? 0.60270   -24.43271 -8.63661  1.000 29.07733  ? 194 GLN   A CB  1 
ATOM   1380 C CG  . GLN   A 1 187 ? 2.03917   -24.13017 -8.21797  1.000 27.73608  ? 194 GLN   A CG  1 
ATOM   1381 C CD  . GLN   A 1 187 ? 2.12753   -23.38303 -6.90142  1.000 30.02955  ? 194 GLN   A CD  1 
ATOM   1382 O OE1 . GLN   A 1 187 ? 1.30502   -22.51640 -6.61094  1.000 34.25127  ? 194 GLN   A OE1 1 
ATOM   1383 N NE2 . GLN   A 1 187 ? 3.13973   -23.70303 -6.10547  1.000 29.25060  ? 194 GLN   A NE2 1 
ATOM   1384 N N   . THR   A 1 188 ? -2.30259  -26.50303 -7.72158  1.000 31.86847  ? 195 THR   A N   1 
ATOM   1385 C CA  . THR   A 1 188 ? -3.67001  -26.74469 -8.16884  1.000 30.32776  ? 195 THR   A CA  1 
ATOM   1386 C C   . THR   A 1 188 ? -4.70894  -25.93786 -7.40142  1.000 31.52815  ? 195 THR   A C   1 
ATOM   1387 O O   . THR   A 1 188 ? -5.89270  -26.00206 -7.74971  1.000 30.00970  ? 195 THR   A O   1 
ATOM   1388 C CB  . THR   A 1 188 ? -4.01677  -28.23233 -8.06210  1.000 34.16071  ? 195 THR   A CB  1 
ATOM   1389 O OG1 . THR   A 1 188 ? -3.75832  -28.69561 -6.73198  1.000 37.10381  ? 195 THR   A OG1 1 
ATOM   1390 C CG2 . THR   A 1 188 ? -3.17960  -29.03580 -9.04462  1.000 33.99639  ? 195 THR   A CG2 1 
ATOM   1391 N N   . GLU   A 1 189 ? -4.30824  -25.19051 -6.37037  1.000 30.80733  ? 196 GLU   A N   1 
ATOM   1392 C CA  . GLU   A 1 189 ? -5.25135  -24.29145 -5.71154  1.000 32.58964  ? 196 GLU   A CA  1 
ATOM   1393 C C   . GLU   A 1 189 ? -5.81510  -23.26684 -6.68750  1.000 28.61040  ? 196 GLU   A C   1 
ATOM   1394 O O   . GLU   A 1 189 ? -6.93100  -22.76981 -6.49560  1.000 29.52542  ? 196 GLU   A O   1 
ATOM   1395 C CB  . GLU   A 1 189 ? -4.57378  -23.59374 -4.53065  1.000 30.87438  ? 196 GLU   A CB  1 
ATOM   1396 C CG  . GLU   A 1 189 ? -3.51857  -22.57944 -4.93993  1.000 32.34976  ? 196 GLU   A CG  1 
ATOM   1397 C CD  . GLU   A 1 189 ? -2.71607  -22.06414 -3.76565  1.000 42.48090  ? 196 GLU   A CD  1 
ATOM   1398 O OE1 . GLU   A 1 189 ? -1.75203  -22.75049 -3.36348  1.000 40.36711  ? 196 GLU   A OE1 1 
ATOM   1399 O OE2 . GLU   A 1 189 ? -3.04049  -20.97244 -3.25024  1.000 35.46807  ? 196 GLU   A OE2 1 
ATOM   1400 N N   . TYR   A 1 190 ? -5.07488  -22.95419 -7.74643  1.000 24.22314  ? 197 TYR   A N   1 
ATOM   1401 C CA  . TYR   A 1 190 ? -5.51839  -21.97210 -8.72549  1.000 25.00630  ? 197 TYR   A CA  1 
ATOM   1402 C C   . TYR   A 1 190 ? -6.52963  -22.54081 -9.71481  1.000 25.59278  ? 197 TYR   A C   1 
ATOM   1403 O O   . TYR   A 1 190 ? -6.89717  -21.85222 -10.67391 1.000 27.68611  ? 197 TYR   A O   1 
ATOM   1404 C CB  . TYR   A 1 190 ? -4.29652  -21.38337 -9.43691  1.000 24.25298  ? 197 TYR   A CB  1 
ATOM   1405 C CG  . TYR   A 1 190 ? -3.37753  -20.70352 -8.44349  1.000 22.63774  ? 197 TYR   A CG  1 
ATOM   1406 C CD1 . TYR   A 1 190 ? -3.79716  -19.57079 -7.75636  1.000 27.85560  ? 197 TYR   A CD1 1 
ATOM   1407 C CD2 . TYR   A 1 190 ? -2.12474  -21.22312 -8.14580  1.000 28.61852  ? 197 TYR   A CD2 1 
ATOM   1408 C CE1 . TYR   A 1 190 ? -2.98734  -18.95571 -6.82696  1.000 28.63751  ? 197 TYR   A CE1 1 
ATOM   1409 C CE2 . TYR   A 1 190 ? -1.29875  -20.60946 -7.21102  1.000 25.67510  ? 197 TYR   A CE2 1 
ATOM   1410 C CZ  . TYR   A 1 190 ? -1.74026  -19.47280 -6.55539  1.000 25.54629  ? 197 TYR   A CZ  1 
ATOM   1411 O OH  . TYR   A 1 190 ? -0.94056  -18.85013 -5.62225  1.000 30.49764  ? 197 TYR   A OH  1 
ATOM   1412 N N   . LEU   A 1 191 ? -6.98189  -23.77603 -9.49684  1.000 24.48743  ? 198 LEU   A N   1 
ATOM   1413 C CA  . LEU   A 1 191 ? -8.12959  -24.33317 -10.19534 1.000 24.98989  ? 198 LEU   A CA  1 
ATOM   1414 C C   . LEU   A 1 191 ? -9.41302  -24.23026 -9.38645  1.000 28.97106  ? 198 LEU   A C   1 
ATOM   1415 O O   . LEU   A 1 191 ? -10.48554 -24.52800 -9.91891  1.000 30.87943  ? 198 LEU   A O   1 
ATOM   1416 C CB  . LEU   A 1 191 ? -7.87588  -25.80500 -10.53890 1.000 29.91147  ? 198 LEU   A CB  1 
ATOM   1417 C CG  . LEU   A 1 191 ? -6.66658  -26.06186 -11.43243 1.000 27.39878  ? 198 LEU   A CG  1 
ATOM   1418 C CD1 . LEU   A 1 191 ? -6.43445  -27.55651 -11.61048 1.000 32.45920  ? 198 LEU   A CD1 1 
ATOM   1419 C CD2 . LEU   A 1 191 ? -6.86644  -25.37591 -12.77035 1.000 32.38076  ? 198 LEU   A CD2 1 
ATOM   1420 N N   . GLU   A 1 192 ? -9.32607  -23.83317 -8.11827  1.000 26.72111  ? 199 GLU   A N   1 
ATOM   1421 C CA  . GLU   A 1 192 ? -10.46148 -23.84942 -7.20643  1.000 30.44911  ? 199 GLU   A CA  1 
ATOM   1422 C C   . GLU   A 1 192 ? -11.24492 -22.55203 -7.36286  1.000 29.55784  ? 199 GLU   A C   1 
ATOM   1423 O O   . GLU   A 1 192 ? -10.65591 -21.46555 -7.35897  1.000 27.32308  ? 199 GLU   A O   1 
ATOM   1424 C CB  . GLU   A 1 192 ? -9.97628  -24.00736 -5.76433  1.000 32.95416  ? 199 GLU   A CB  1 
ATOM   1425 C CG  . GLU   A 1 192 ? -9.31745  -25.35141 -5.46795  1.000 31.99856  ? 199 GLU   A CG  1 
ATOM   1426 C CD  . GLU   A 1 192 ? -10.25387 -26.53870 -5.59407  1.000 73.10406  ? 199 GLU   A CD  1 
ATOM   1427 O OE1 . GLU   A 1 192 ? -11.47820 -26.36125 -5.43727  1.000 74.60873  ? 199 GLU   A OE1 1 
ATOM   1428 O OE2 . GLU   A 1 192 ? -9.76103  -27.65826 -5.84637  1.000 71.66680  ? 199 GLU   A OE2 1 
ATOM   1429 N N   . GLU   A 1 193 ? -12.56821 -22.66858 -7.51317  1.000 30.70027  ? 200 GLU   A N   1 
ATOM   1430 C CA  . GLU   A 1 193 ? -13.38916 -21.49276 -7.79558  1.000 27.43494  ? 200 GLU   A CA  1 
ATOM   1431 C C   . GLU   A 1 193 ? -13.21381 -20.41791 -6.72848  1.000 25.55712  ? 200 GLU   A C   1 
ATOM   1432 O O   . GLU   A 1 193 ? -13.03850 -19.23615 -7.04670  1.000 27.03577  ? 200 GLU   A O   1 
ATOM   1433 C CB  . GLU   A 1 193 ? -14.86748 -21.88019 -7.91464  1.000 27.57104  ? 200 GLU   A CB  1 
ATOM   1434 C CG  . GLU   A 1 193 ? -15.76211 -20.68601 -8.24161  1.000 39.85959  ? 200 GLU   A CG  1 
ATOM   1435 C CD  . GLU   A 1 193 ? -17.24520 -21.00517 -8.18570  1.000 60.38303  ? 200 GLU   A CD  1 
ATOM   1436 O OE1 . GLU   A 1 193 ? -18.03188 -20.27751 -8.82810  1.000 48.19475  ? 200 GLU   A OE1 1 
ATOM   1437 O OE2 . GLU   A 1 193 ? -17.62562 -21.97639 -7.49913  1.000 44.79253  ? 200 GLU   A OE2 1 
ATOM   1438 N N   . ARG   A 1 194 ? -13.26017 -20.80548 -5.45260  1.000 31.07586  ? 201 ARG   A N   1 
ATOM   1439 C CA  . ARG   A 1 194 ? -13.19288 -19.79732 -4.40076  1.000 29.40481  ? 201 ARG   A CA  1 
ATOM   1440 C C   . ARG   A 1 194 ? -11.83003 -19.11339 -4.36368  1.000 29.76060  ? 201 ARG   A C   1 
ATOM   1441 O O   . ARG   A 1 194 ? -11.73843 -17.94028 -3.98584  1.000 27.92261  ? 201 ARG   A O   1 
ATOM   1442 C CB  . ARG   A 1 194 ? -13.53392 -20.41918 -3.04655  1.000 35.48867  ? 201 ARG   A CB  1 
ATOM   1443 C CG  . ARG   A 1 194 ? -12.49020 -21.35527 -2.48313  1.000 33.62708  ? 201 ARG   A CG  1 
ATOM   1444 C CD  . ARG   A 1 194 ? -13.00991 -21.99202 -1.20029  1.000 38.50896  ? 201 ARG   A CD  1 
ATOM   1445 N NE  . ARG   A 1 194 ? -12.12302 -23.03001 -0.69610  1.000 52.21964  ? 201 ARG   A NE  1 
ATOM   1446 C CZ  . ARG   A 1 194 ? -12.25888 -23.60604 0.48973   1.000 49.80242  ? 201 ARG   A CZ  1 
ATOM   1447 N NH1 . ARG   A 1 194 ? -13.25653 -23.29000 1.29942   1.000 52.78656  ? 201 ARG   A NH1 1 
ATOM   1448 N NH2 . ARG   A 1 194 ? -11.36929 -24.51605 0.87498   1.000 53.95556  ? 201 ARG   A NH2 1 
ATOM   1449 N N   . ARG   A 1 195 ? -10.76773 -19.81573 -4.76540  1.000 25.12906  ? 202 ARG   A N   1 
ATOM   1450 C CA  . ARG   A 1 195 ? -9.44448  -19.20037 -4.78301  1.000 25.55522  ? 202 ARG   A CA  1 
ATOM   1451 C C   . ARG   A 1 195 ? -9.31349  -18.20258 -5.93040  1.000 23.45079  ? 202 ARG   A C   1 
ATOM   1452 O O   . ARG   A 1 195 ? -8.77194  -17.10667 -5.74706  1.000 25.57731  ? 202 ARG   A O   1 
ATOM   1453 C CB  . ARG   A 1 195 ? -8.37351  -20.28367 -4.87976  1.000 24.43528  ? 202 ARG   A CB  1 
ATOM   1454 C CG  . ARG   A 1 195 ? -6.92959  -19.77870 -4.88801  1.000 25.42946  ? 202 ARG   A CG  1 
ATOM   1455 C CD  . ARG   A 1 195 ? -6.51427  -19.20472 -3.52702  1.000 29.56715  ? 202 ARG   A CD  1 
ATOM   1456 N NE  . ARG   A 1 195 ? -5.07851  -18.94864 -3.47204  1.000 28.22896  ? 202 ARG   A NE  1 
ATOM   1457 C CZ  . ARG   A 1 195 ? -4.52365  -17.76431 -3.24485  1.000 30.98328  ? 202 ARG   A CZ  1 
ATOM   1458 N NH1 . ARG   A 1 195 ? -5.25707  -16.68442 -3.03316  1.000 29.86570  ? 202 ARG   A NH1 1 
ATOM   1459 N NH2 . ARG   A 1 195 ? -3.19680  -17.66201 -3.23052  1.000 32.74700  ? 202 ARG   A NH2 1 
ATOM   1460 N N   . ILE   A 1 196 ? -9.78617  -18.56686 -7.12533  1.000 24.61147  ? 203 ILE   A N   1 
ATOM   1461 C CA  . ILE   A 1 196 ? -9.74880  -17.63562 -8.25134  1.000 25.08228  ? 203 ILE   A CA  1 
ATOM   1462 C C   . ILE   A 1 196 ? -10.59422 -16.40497 -7.94999  1.000 24.59785  ? 203 ILE   A C   1 
ATOM   1463 O O   . ILE   A 1 196 ? -10.17166 -15.26973 -8.20073  1.000 24.93624  ? 203 ILE   A O   1 
ATOM   1464 C CB  . ILE   A 1 196 ? -10.21310 -18.33264 -9.54490  1.000 24.30346  ? 203 ILE   A CB  1 
ATOM   1465 C CG1 . ILE   A 1 196 ? -9.29764  -19.51115 -9.88524  1.000 23.11883  ? 203 ILE   A CG1 1 
ATOM   1466 C CG2 . ILE   A 1 196 ? -10.24439 -17.34570 -10.71080 1.000 20.31068  ? 203 ILE   A CG2 1 
ATOM   1467 C CD1 . ILE   A 1 196 ? -9.93391  -20.51425 -10.84952 1.000 25.62404  ? 203 ILE   A CD1 1 
ATOM   1468 N N   . LYS   A 1 197 ? -11.80033 -16.61160 -7.41039  1.000 24.18990  ? 204 LYS   A N   1 
ATOM   1469 C CA  . LYS   A 1 197 ? -12.66836 -15.49430 -7.04621  1.000 24.66632  ? 204 LYS   A CA  1 
ATOM   1470 C C   . LYS   A 1 197 ? -11.96345 -14.54386 -6.09071  1.000 30.61733  ? 204 LYS   A C   1 
ATOM   1471 O O   . LYS   A 1 197 ? -12.01622 -13.32132 -6.26052  1.000 25.68543  ? 204 LYS   A O   1 
ATOM   1472 C CB  . LYS   A 1 197 ? -13.94918 -16.01069 -6.39085  1.000 29.31273  ? 204 LYS   A CB  1 
ATOM   1473 C CG  . LYS   A 1 197 ? -15.06501 -16.38430 -7.32680  1.000 35.43889  ? 204 LYS   A CG  1 
ATOM   1474 C CD  . LYS   A 1 197 ? -16.28569 -16.77920 -6.51205  1.000 38.19626  ? 204 LYS   A CD  1 
ATOM   1475 C CE  . LYS   A 1 197 ? -17.41091 -17.28869 -7.38814  1.000 53.90686  ? 204 LYS   A CE  1 
ATOM   1476 N NZ  . LYS   A 1 197 ? -18.15088 -18.39086 -6.71482  1.000 61.96541  ? 204 LYS   A NZ  1 
ATOM   1477 N N   . GLU   A 1 198 ? -11.31877 -15.10018 -5.05988  1.000 24.85946  ? 205 GLU   A N   1 
ATOM   1478 C CA  . GLU   A 1 198 ? -10.59298 -14.29076 -4.08620  1.000 22.72453  ? 205 GLU   A CA  1 
ATOM   1479 C C   . GLU   A 1 198 ? -9.51166  -13.45575 -4.75566  1.000 23.98050  ? 205 GLU   A C   1 
ATOM   1480 O O   . GLU   A 1 198 ? -9.35346  -12.26953 -4.44776  1.000 24.01676  ? 205 GLU   A O   1 
ATOM   1481 C CB  . GLU   A 1 198 ? -9.98106  -15.20493 -3.02265  1.000 22.53312  ? 205 GLU   A CB  1 
ATOM   1482 C CG  . GLU   A 1 198 ? -9.07144  -14.52180 -2.01911  1.000 29.41191  ? 205 GLU   A CG  1 
ATOM   1483 C CD  . GLU   A 1 198 ? -8.40034  -15.51948 -1.08536  1.000 27.85350  ? 205 GLU   A CD  1 
ATOM   1484 O OE1 . GLU   A 1 198 ? -7.87861  -16.53660 -1.58959  1.000 35.46272  ? 205 GLU   A OE1 1 
ATOM   1485 O OE2 . GLU   A 1 198 ? -8.39568  -15.29147 0.14370   1.000 31.85014  ? 205 GLU   A OE2 1 
ATOM   1486 N N   . ILE   A 1 199 ? -8.75587  -14.06194 -5.67461  1.000 22.78317  ? 206 ILE   A N   1 
ATOM   1487 C CA  . ILE   A 1 199 ? -7.64506  -13.36270 -6.31171  1.000 22.53993  ? 206 ILE   A CA  1 
ATOM   1488 C C   . ILE   A 1 199 ? -8.15689  -12.25948 -7.22797  1.000 23.25775  ? 206 ILE   A C   1 
ATOM   1489 O O   . ILE   A 1 199 ? -7.60643  -11.15183 -7.25262  1.000 23.80390  ? 206 ILE   A O   1 
ATOM   1490 C CB  . ILE   A 1 199 ? -6.76037  -14.36547 -7.07246  1.000 24.48194  ? 206 ILE   A CB  1 
ATOM   1491 C CG1 . ILE   A 1 199 ? -6.11162  -15.34093 -6.08915  1.000 26.77362  ? 206 ILE   A CG1 1 
ATOM   1492 C CG2 . ILE   A 1 199 ? -5.70484  -13.64636 -7.88844  1.000 26.67867  ? 206 ILE   A CG2 1 
ATOM   1493 C CD1 . ILE   A 1 199 ? -5.59502  -16.59906 -6.73839  1.000 28.48158  ? 206 ILE   A CD1 1 
ATOM   1494 N N   . VAL   A 1 200 ? -9.20159  -12.54812 -8.00868  1.000 23.24762  ? 207 VAL   A N   1 
ATOM   1495 C CA  . VAL   A 1 200 ? -9.76903  -11.53672 -8.89702  1.000 24.77758  ? 207 VAL   A CA  1 
ATOM   1496 C C   . VAL   A 1 200 ? -10.28700 -10.34816 -8.09376  1.000 28.63810  ? 207 VAL   A C   1 
ATOM   1497 O O   . VAL   A 1 200 ? -10.05794 -9.18721  -8.45427  1.000 26.79348  ? 207 VAL   A O   1 
ATOM   1498 C CB  . VAL   A 1 200 ? -10.87254 -12.15913 -9.77351  1.000 24.63259  ? 207 VAL   A CB  1 
ATOM   1499 C CG1 . VAL   A 1 200 ? -11.66350 -11.07281 -10.48478 1.000 28.85080  ? 207 VAL   A CG1 1 
ATOM   1500 C CG2 . VAL   A 1 200 ? -10.26529 -13.13548 -10.78197 1.000 22.27759  ? 207 VAL   A CG2 1 
ATOM   1501 N N   . LYS   A 1 201 ? -10.97576 -10.61609 -6.98121  1.000 24.89093  ? 208 LYS   A N   1 
ATOM   1502 C CA  . LYS   A 1 201 ? -11.49490 -9.53235  -6.15242  1.000 30.22982  ? 208 LYS   A CA  1 
ATOM   1503 C C   . LYS   A 1 201 ? -10.36974 -8.73879  -5.49885  1.000 27.01064  ? 208 LYS   A C   1 
ATOM   1504 O O   . LYS   A 1 201 ? -10.49395 -7.52269  -5.31141  1.000 32.65028  ? 208 LYS   A O   1 
ATOM   1505 C CB  . LYS   A 1 201 ? -12.43984 -10.10204 -5.09164  1.000 30.35799  ? 208 LYS   A CB  1 
ATOM   1506 C CG  . LYS   A 1 201 ? -12.93101 -9.09227  -4.06593  1.000 37.04484  ? 208 LYS   A CG  1 
ATOM   1507 C CD  . LYS   A 1 201 ? -14.10326 -9.64507  -3.27176  1.000 49.44092  ? 208 LYS   A CD  1 
ATOM   1508 C CE  . LYS   A 1 201 ? -14.48909 -8.71612  -2.13217  1.000 51.93021  ? 208 LYS   A CE  1 
ATOM   1509 N NZ  . LYS   A 1 201 ? -15.39124 -9.38584  -1.15146  1.000 58.47525  ? 208 LYS   A NZ  1 
ATOM   1510 N N   . LYS   A 1 202 ? -9.26692  -9.40622  -5.15153  1.000 28.41834  ? 209 LYS   A N   1 
ATOM   1511 C CA  . LYS   A 1 202 ? -8.17306  -8.73623  -4.45362  1.000 31.08496  ? 209 LYS   A CA  1 
ATOM   1512 C C   . LYS   A 1 202 ? -7.38603  -7.82370  -5.38729  1.000 31.94562  ? 209 LYS   A C   1 
ATOM   1513 O O   . LYS   A 1 202 ? -7.00642  -6.71125  -5.00162  1.000 29.97057  ? 209 LYS   A O   1 
ATOM   1514 C CB  . LYS   A 1 202 ? -7.24464  -9.78057  -3.83240  1.000 29.42341  ? 209 LYS   A CB  1 
ATOM   1515 C CG  . LYS   A 1 202 ? -5.92304  -9.22925  -3.29711  1.000 37.12260  ? 209 LYS   A CG  1 
ATOM   1516 C CD  . LYS   A 1 202 ? -5.31183  -10.16717 -2.27276  1.000 41.23539  ? 209 LYS   A CD  1 
ATOM   1517 C CE  . LYS   A 1 202 ? -4.12833  -9.52240  -1.56928  1.000 43.14245  ? 209 LYS   A CE  1 
ATOM   1518 N NZ  . LYS   A 1 202 ? -4.54884  -8.64372  -0.44446  1.000 69.93829  ? 209 LYS   A NZ  1 
ATOM   1519 N N   . HIS   A 1 203 ? -7.13388  -8.27582  -6.61818  1.000 27.12366  ? 210 HIS   A N   1 
ATOM   1520 C CA  . HIS   A 1 203 ? -6.15530  -7.64629  -7.49616  1.000 31.13424  ? 210 HIS   A CA  1 
ATOM   1521 C C   . HIS   A 1 203 ? -6.71928  -7.09294  -8.79818  1.000 31.27200  ? 210 HIS   A C   1 
ATOM   1522 O O   . HIS   A 1 203 ? -6.02458  -6.31020  -9.45869  1.000 28.75127  ? 210 HIS   A O   1 
ATOM   1523 C CB  . HIS   A 1 203 ? -5.04209  -8.64691  -7.85600  1.000 26.11324  ? 210 HIS   A CB  1 
ATOM   1524 C CG  . HIS   A 1 203 ? -4.17988  -9.03810  -6.69508  1.000 33.76017  ? 210 HIS   A CG  1 
ATOM   1525 N ND1 . HIS   A 1 203 ? -3.39889  -8.13516  -6.00699  1.000 36.03760  ? 210 HIS   A ND1 1 
ATOM   1526 C CD2 . HIS   A 1 203 ? -3.97745  -10.23911 -6.10223  1.000 39.00522  ? 210 HIS   A CD2 1 
ATOM   1527 C CE1 . HIS   A 1 203 ? -2.75052  -8.76247  -5.04112  1.000 39.20331  ? 210 HIS   A CE1 1 
ATOM   1528 N NE2 . HIS   A 1 203 ? -3.08624  -10.03978 -5.07558  1.000 39.14333  ? 210 HIS   A NE2 1 
ATOM   1529 N N   . SER   A 1 204 ? -7.93733  -7.47158  -9.19420  1.000 26.52317  ? 211 SER   A N   1 
ATOM   1530 C CA  . SER   A 1 204 ? -8.45546  -7.14387  -10.51899 1.000 28.94300  ? 211 SER   A CA  1 
ATOM   1531 C C   . SER   A 1 204 ? -9.88094  -6.60523  -10.44778 1.000 25.61260  ? 211 SER   A C   1 
ATOM   1532 O O   . SER   A 1 204 ? -10.63855 -6.71088  -11.41668 1.000 29.44201  ? 211 SER   A O   1 
ATOM   1533 C CB  . SER   A 1 204 ? -8.39842  -8.36727  -11.43735 1.000 24.94113  ? 211 SER   A CB  1 
ATOM   1534 O OG  . SER   A 1 204 ? -7.08908  -8.90581  -11.48865 1.000 27.50212  ? 211 SER   A OG  1 
ATOM   1535 N N   . GLN   A 1 205 ? -10.25597 -6.00611  -9.31601  1.000 30.71606  ? 212 GLN   A N   1 
ATOM   1536 C CA  . GLN   A 1 205 ? -11.65192 -5.64210  -9.09566  1.000 37.86776  ? 212 GLN   A CA  1 
ATOM   1537 C C   . GLN   A 1 205 ? -12.10748 -4.46096  -9.94851  1.000 34.66460  ? 212 GLN   A C   1 
ATOM   1538 O O   . GLN   A 1 205 ? -13.31699 -4.25250  -10.09256 1.000 36.76605  ? 212 GLN   A O   1 
ATOM   1539 C CB  . GLN   A 1 205 ? -11.88651 -5.33415  -7.61400  1.000 34.42288  ? 212 GLN   A CB  1 
ATOM   1540 C CG  . GLN   A 1 205 ? -11.15027 -4.10388  -7.10667  1.000 44.11837  ? 212 GLN   A CG  1 
ATOM   1541 C CD  . GLN   A 1 205 ? -9.83239  -4.43964  -6.42720  1.000 62.19282  ? 212 GLN   A CD  1 
ATOM   1542 O OE1 . GLN   A 1 205 ? -8.91223  -4.97589  -7.05067  1.000 46.19992  ? 212 GLN   A OE1 1 
ATOM   1543 N NE2 . GLN   A 1 205 ? -9.73433  -4.11728  -5.14000  1.000 53.31413  ? 212 GLN   A NE2 1 
ATOM   1544 N N   . PHE   A 1 206 ? -11.18207 -3.69478  -10.52544 1.000 27.90388  ? 213 PHE   A N   1 
ATOM   1545 C CA  . PHE   A 1 206 ? -11.52259 -2.49843  -11.28757 1.000 29.28634  ? 213 PHE   A CA  1 
ATOM   1546 C C   . PHE   A 1 206 ? -11.20616 -2.61870  -12.77500 1.000 33.70501  ? 213 PHE   A C   1 
ATOM   1547 O O   . PHE   A 1 206 ? -11.28900 -1.61926  -13.49503 1.000 36.66192  ? 213 PHE   A O   1 
ATOM   1548 C CB  . PHE   A 1 206 ? -10.80975 -1.28835  -10.68526 1.000 34.93343  ? 213 PHE   A CB  1 
ATOM   1549 C CG  . PHE   A 1 206 ? -11.19305 -1.02263  -9.25990  1.000 40.57743  ? 213 PHE   A CG  1 
ATOM   1550 C CD1 . PHE   A 1 206 ? -12.52624 -1.01708  -8.88147  1.000 39.11082  ? 213 PHE   A CD1 1 
ATOM   1551 C CD2 . PHE   A 1 206 ? -10.22659 -0.85777  -8.28582  1.000 37.54821  ? 213 PHE   A CD2 1 
ATOM   1552 C CE1 . PHE   A 1 206 ? -12.88895 -0.78969  -7.56749  1.000 47.27622  ? 213 PHE   A CE1 1 
ATOM   1553 C CE2 . PHE   A 1 206 ? -10.58619 -0.63904  -6.96645  1.000 46.15735  ? 213 PHE   A CE2 1 
ATOM   1554 C CZ  . PHE   A 1 206 ? -11.91766 -0.60448  -6.61062  1.000 43.59036  ? 213 PHE   A CZ  1 
ATOM   1555 N N   . ILE   A 1 207 ? -10.85732 -3.81637  -13.25124 1.000 25.23478  ? 214 ILE   A N   1 
ATOM   1556 C CA  . ILE   A 1 207 ? -10.64542 -4.03323  -14.67820 1.000 25.06961  ? 214 ILE   A CA  1 
ATOM   1557 C C   . ILE   A 1 207 ? -11.92184 -3.69178  -15.43625 1.000 30.60045  ? 214 ILE   A C   1 
ATOM   1558 O O   . ILE   A 1 207 ? -13.02159 -4.10348  -15.04822 1.000 29.72212  ? 214 ILE   A O   1 
ATOM   1559 C CB  . ILE   A 1 207 ? -10.21365 -5.48716  -14.92721 1.000 24.15569  ? 214 ILE   A CB  1 
ATOM   1560 C CG1 . ILE   A 1 207 ? -8.81209  -5.74423  -14.35802 1.000 24.47783  ? 214 ILE   A CG1 1 
ATOM   1561 C CG2 . ILE   A 1 207 ? -10.25751 -5.81441  -16.41463 1.000 22.44186  ? 214 ILE   A CG2 1 
ATOM   1562 C CD1 . ILE   A 1 207 ? -7.69503  -5.07874  -15.13917 1.000 27.45341  ? 214 ILE   A CD1 1 
ATOM   1563 N N   . GLY   A 1 208 ? -11.78053 -2.94221  -16.52902 1.000 27.70719  ? 215 GLY   A N   1 
ATOM   1564 C CA  . GLY   A 1 208 ? -12.92573 -2.39377  -17.23596 1.000 26.78651  ? 215 GLY   A CA  1 
ATOM   1565 C C   . GLY   A 1 208 ? -13.56877 -3.29175  -18.27698 1.000 29.99591  ? 215 GLY   A C   1 
ATOM   1566 O O   . GLY   A 1 208 ? -14.17925 -2.79871  -19.23026 1.000 28.15458  ? 215 GLY   A O   1 
ATOM   1567 N N   . TYR   A 1 209 ? -13.45158 -4.60401  -18.10800 1.000 23.97282  ? 216 TYR   A N   1 
ATOM   1568 C CA  . TYR   A 1 209 ? -14.05250 -5.57549  -19.01047 1.000 25.37279  ? 216 TYR   A CA  1 
ATOM   1569 C C   . TYR   A 1 209 ? -14.65213 -6.69586  -18.17476 1.000 26.38674  ? 216 TYR   A C   1 
ATOM   1570 O O   . TYR   A 1 209 ? -14.13350 -7.00739  -17.09787 1.000 25.38123  ? 216 TYR   A O   1 
ATOM   1571 C CB  . TYR   A 1 209 ? -13.01794 -6.15127  -19.99237 1.000 25.00694  ? 216 TYR   A CB  1 
ATOM   1572 C CG  . TYR   A 1 209 ? -12.41666 -5.09498  -20.88300 1.000 25.55772  ? 216 TYR   A CG  1 
ATOM   1573 C CD1 . TYR   A 1 209 ? -13.05746 -4.68870  -22.04384 1.000 25.21924  ? 216 TYR   A CD1 1 
ATOM   1574 C CD2 . TYR   A 1 209 ? -11.21757 -4.47835  -20.54555 1.000 26.24868  ? 216 TYR   A CD2 1 
ATOM   1575 C CE1 . TYR   A 1 209 ? -12.51781 -3.71210  -22.85224 1.000 26.64299  ? 216 TYR   A CE1 1 
ATOM   1576 C CE2 . TYR   A 1 209 ? -10.67074 -3.49390  -21.34744 1.000 22.76855  ? 216 TYR   A CE2 1 
ATOM   1577 C CZ  . TYR   A 1 209 ? -11.32675 -3.11628  -22.50023 1.000 26.87963  ? 216 TYR   A CZ  1 
ATOM   1578 O OH  . TYR   A 1 209 ? -10.79893 -2.14015  -23.31033 1.000 30.19230  ? 216 TYR   A OH  1 
ATOM   1579 N N   . PRO   A 1 210 ? -15.73795 -7.31240  -18.63813 1.000 23.06975  ? 217 PRO   A N   1 
ATOM   1580 C CA  . PRO   A 1 210 ? -16.33050 -8.41642  -17.87013 1.000 24.91136  ? 217 PRO   A CA  1 
ATOM   1581 C C   . PRO   A 1 210 ? -15.37654 -9.59818  -17.76176 1.000 23.82171  ? 217 PRO   A C   1 
ATOM   1582 O O   . PRO   A 1 210 ? -14.83002 -10.07914 -18.75955 1.000 24.98746  ? 217 PRO   A O   1 
ATOM   1583 C CB  . PRO   A 1 210 ? -17.59338 -8.76790  -18.66926 1.000 26.04857  ? 217 PRO   A CB  1 
ATOM   1584 C CG  . PRO   A 1 210 ? -17.32448 -8.26800  -20.04912 1.000 30.41699  ? 217 PRO   A CG  1 
ATOM   1585 C CD  . PRO   A 1 210 ? -16.49611 -7.02604  -19.86866 1.000 29.51208  ? 217 PRO   A CD  1 
ATOM   1586 N N   . ILE   A 1 211 ? -15.16164 -10.05182 -16.52959 1.000 23.91803  ? 218 ILE   A N   1 
ATOM   1587 C CA  . ILE   A 1 211 ? -14.37427 -11.24937 -16.25245 1.000 22.96834  ? 218 ILE   A CA  1 
ATOM   1588 C C   . ILE   A 1 211 ? -15.34144 -12.32907 -15.79685 1.000 25.23327  ? 218 ILE   A C   1 
ATOM   1589 O O   . ILE   A 1 211 ? -16.00384 -12.18096 -14.76125 1.000 25.08324  ? 218 ILE   A O   1 
ATOM   1590 C CB  . ILE   A 1 211 ? -13.28838 -11.00066 -15.19402 1.000 26.87639  ? 218 ILE   A CB  1 
ATOM   1591 C CG1 . ILE   A 1 211 ? -12.30821 -9.92063  -15.66290 1.000 26.03378  ? 218 ILE   A CG1 1 
ATOM   1592 C CG2 . ILE   A 1 211 ? -12.55144 -12.29753 -14.86986 1.000 21.92782  ? 218 ILE   A CG2 1 
ATOM   1593 C CD1 . ILE   A 1 211 ? -11.54886 -9.25042  -14.52896 1.000 24.03577  ? 218 ILE   A CD1 1 
ATOM   1594 N N   . THR   A 1 212 ? -15.42883 -13.40673 -16.56890 1.000 22.35713  ? 219 THR   A N   1 
ATOM   1595 C CA  . THR   A 1 212 ? -16.34865 -14.50194 -16.29463 1.000 18.82617  ? 219 THR   A CA  1 
ATOM   1596 C C   . THR   A 1 212 ? -15.53584 -15.70857 -15.84956 1.000 19.94119  ? 219 THR   A C   1 
ATOM   1597 O O   . THR   A 1 212 ? -14.69856 -16.21089 -16.60799 1.000 23.16439  ? 219 THR   A O   1 
ATOM   1598 C CB  . THR   A 1 212 ? -17.18433 -14.84258 -17.52995 1.000 22.77134  ? 219 THR   A CB  1 
ATOM   1599 O OG1 . THR   A 1 212 ? -17.93460 -13.69033 -17.94175 1.000 24.11153  ? 219 THR   A OG1 1 
ATOM   1600 C CG2 . THR   A 1 212 ? -18.15238 -15.98747 -17.22043 1.000 25.69753  ? 219 THR   A CG2 1 
ATOM   1601 N N   . LEU   A 1 213 ? -15.77280 -16.16335 -14.62326 1.000 21.40773  ? 220 LEU   A N   1 
ATOM   1602 C CA  . LEU   A 1 213 ? -15.12012 -17.36127 -14.10628 1.000 19.82999  ? 220 LEU   A CA  1 
ATOM   1603 C C   . LEU   A 1 213 ? -16.01989 -18.55144 -14.42632 1.000 22.38991  ? 220 LEU   A C   1 
ATOM   1604 O O   . LEU   A 1 213 ? -17.12523 -18.66827 -13.88176 1.000 22.20410  ? 220 LEU   A O   1 
ATOM   1605 C CB  . LEU   A 1 213 ? -14.85610 -17.23237 -12.60437 1.000 22.27290  ? 220 LEU   A CB  1 
ATOM   1606 C CG  . LEU   A 1 213 ? -14.34628 -18.46214 -11.84953 1.000 24.87719  ? 220 LEU   A CG  1 
ATOM   1607 C CD1 . LEU   A 1 213 ? -13.13031 -19.07745 -12.53223 1.000 25.02359  ? 220 LEU   A CD1 1 
ATOM   1608 C CD2 . LEU   A 1 213 ? -14.01645 -18.10579 -10.38918 1.000 23.97270  ? 220 LEU   A CD2 1 
ATOM   1609 N N   . PHE   A 1 214 ? -15.55933 -19.41414 -15.33268 1.000 20.81964  ? 221 PHE   A N   1 
ATOM   1610 C CA  . PHE   A 1 214 ? -16.30783 -20.60909 -15.69679 1.000 21.27664  ? 221 PHE   A CA  1 
ATOM   1611 C C   . PHE   A 1 214 ? -16.29223 -21.59401 -14.53263 1.000 24.27439  ? 221 PHE   A C   1 
ATOM   1612 O O   . PHE   A 1 214 ? -15.34723 -21.63420 -13.73939 1.000 25.10090  ? 221 PHE   A O   1 
ATOM   1613 C CB  . PHE   A 1 214 ? -15.69078 -21.29162 -16.92688 1.000 23.13458  ? 221 PHE   A CB  1 
ATOM   1614 C CG  . PHE   A 1 214 ? -15.97292 -20.60740 -18.24641 1.000 20.63196  ? 221 PHE   A CG  1 
ATOM   1615 C CD1 . PHE   A 1 214 ? -16.08249 -19.22522 -18.34159 1.000 22.43015  ? 221 PHE   A CD1 1 
ATOM   1616 C CD2 . PHE   A 1 214 ? -16.08742 -21.36238 -19.40945 1.000 21.14100  ? 221 PHE   A CD2 1 
ATOM   1617 C CE1 . PHE   A 1 214 ? -16.32141 -18.61197 -19.56927 1.000 23.14490  ? 221 PHE   A CE1 1 
ATOM   1618 C CE2 . PHE   A 1 214 ? -16.32915 -20.75566 -20.64299 1.000 22.56878  ? 221 PHE   A CE2 1 
ATOM   1619 C CZ  . PHE   A 1 214 ? -16.44175 -19.37870 -20.72183 1.000 22.84237  ? 221 PHE   A CZ  1 
ATOM   1620 N N   . VAL   A 1 215 ? -17.33843 -22.40478 -14.43781 1.000 25.93535  ? 222 VAL   A N   1 
ATOM   1621 C CA  . VAL   A 1 215 ? -17.39952 -23.45975 -13.43855 1.000 29.90619  ? 222 VAL   A CA  1 
ATOM   1622 C C   . VAL   A 1 215 ? -17.27631 -24.80766 -14.14175 1.000 33.30269  ? 222 VAL   A C   1 
ATOM   1623 O O   . VAL   A 1 215 ? -17.37272 -24.90871 -15.36386 1.000 32.25848  ? 222 VAL   A O   1 
ATOM   1624 C CB  . VAL   A 1 215 ? -18.67755 -23.37539 -12.58475 1.000 39.35558  ? 222 VAL   A CB  1 
ATOM   1625 C CG1 . VAL   A 1 215 ? -18.62108 -22.14685 -11.68654 1.000 45.96141  ? 222 VAL   A CG1 1 
ATOM   1626 C CG2 . VAL   A 1 215 ? -19.89541 -23.32172 -13.47062 1.000 32.97720  ? 222 VAL   A CG2 1 
ATOM   1627 N N   . GLU   A 1 216 ? -17.04972 -25.85377 -13.35362 1.000 35.32018  ? 223 GLU   A N   1 
ATOM   1628 C CA  . GLU   A 1 216 ? -16.80192 -27.17808 -13.90188 1.000 43.86389  ? 223 GLU   A CA  1 
ATOM   1629 C C   . GLU   A 1 216 ? -17.89055 -28.15817 -13.48513 1.000 45.17930  ? 223 GLU   A C   1 
ATOM   1630 O O   . GLU   A 1 216 ? -18.60501 -27.94920 -12.50042 1.000 49.58726  ? 223 GLU   A O   1 
ATOM   1631 C CB  . GLU   A 1 216 ? -15.43818 -27.72061 -13.45623 1.000 40.71002  ? 223 GLU   A CB  1 
ATOM   1632 C CG  . GLU   A 1 216 ? -14.26348 -26.81658 -13.78531 1.000 36.26940  ? 223 GLU   A CG  1 
ATOM   1633 C CD  . GLU   A 1 216 ? -12.93894 -27.41996 -13.36046 1.000 46.76741  ? 223 GLU   A CD  1 
ATOM   1634 O OE1 . GLU   A 1 216 ? -12.63438 -28.55468 -13.79385 1.000 42.82185  ? 223 GLU   A OE1 1 
ATOM   1635 O OE2 . GLU   A 1 216 ? -12.21882 -26.77164 -12.57097 1.000 45.75179  ? 223 GLU   A OE2 1 
ATOM   1636 N N   . LYS   A 1 217 ? -17.99640 -29.23755 -14.26123 1.000 53.94411  ? 224 LYS   A N   1 
ATOM   1637 C CA  . LYS   A 1 217 ? -18.83668 -30.39285 -13.94135 1.000 64.07039  ? 224 LYS   A CA  1 
ATOM   1638 C C   . LYS   A 1 217 ? -20.29836 -30.02357 -13.71878 1.000 74.10277  ? 224 LYS   A C   1 
ATOM   1639 O O   . LYS   A 1 217 ? -20.98302 -30.64480 -12.90381 1.000 74.51083  ? 224 LYS   A O   1 
ATOM   1640 C CB  . LYS   A 1 217 ? -18.29804 -31.11573 -12.70324 1.000 58.42714  ? 224 LYS   A CB  1 
ATOM   1641 C CG  . LYS   A 1 217 ? -16.85918 -31.58626 -12.83561 1.000 62.87507  ? 224 LYS   A CG  1 
ATOM   1642 C CD  . LYS   A 1 217 ? -16.21454 -31.76220 -11.47148 1.000 73.99663  ? 224 LYS   A CD  1 
ATOM   1643 C CE  . LYS   A 1 217 ? -17.08242 -32.62473 -10.56612 1.000 75.82594  ? 224 LYS   A CE  1 
ATOM   1644 N NZ  . LYS   A 1 217 ? -16.42030 -33.91362 -10.22060 1.000 73.94245  ? 224 LYS   A NZ  1 
HETATM 1645 O O2  . A1AYI B 2 .   ? -0.52980  -9.07085  -23.88857 0.747 30.88840  ? 301 A1AYI A O2  1 
HETATM 1646 O O1  . A1AYI B 2 .   ? -3.76605  -10.76329 -24.71069 1.000 29.68111  ? 301 A1AYI A O1  1 
HETATM 1647 C C1  . A1AYI B 2 .   ? -2.91765  -10.65788 -23.57745 0.694 23.00092  ? 301 A1AYI A C1  1 
HETATM 1648 C C10 . A1AYI B 2 .   ? -1.36964  -8.25890  -27.35149 0.990 33.51137  ? 301 A1AYI A C10 1 
HETATM 1649 C C11 . A1AYI B 2 .   ? -1.53172  -6.89512  -27.26663 0.726 29.44214  ? 301 A1AYI A C11 1 
HETATM 1650 C C12 . A1AYI B 2 .   ? -1.36132  -6.26149  -26.05913 1.000 22.83740  ? 301 A1AYI A C12 1 
HETATM 1651 C C13 . A1AYI B 2 .   ? -1.02364  -6.98286  -24.92486 1.000 35.64444  ? 301 A1AYI A C13 1 
HETATM 1652 C C2  . A1AYI B 2 .   ? -1.55739  -11.26248 -23.81946 1.000 27.73858  ? 301 A1AYI A C2  1 
HETATM 1653 C C3  . A1AYI B 2 .   ? -1.40078  -12.64552 -23.88281 0.664 24.69253  ? 301 A1AYI A C3  1 
HETATM 1654 C C4  . A1AYI B 2 .   ? -0.15843  -13.21577 -24.09384 0.840 26.61582  ? 301 A1AYI A C4  1 
HETATM 1655 C C5  . A1AYI B 2 .   ? 0.94735   -12.40958 -24.23259 1.000 26.10078  ? 301 A1AYI A C5  1 
HETATM 1656 C C6  . A1AYI B 2 .   ? 0.82556   -11.03374 -24.16866 1.000 32.90249  ? 301 A1AYI A C6  1 
HETATM 1657 C C7  . A1AYI B 2 .   ? -0.41241  -10.46420 -23.96205 0.742 26.45265  ? 301 A1AYI A C7  1 
HETATM 1658 C C8  . A1AYI B 2 .   ? -0.86537  -8.34558  -25.02900 0.579 34.20723  ? 301 A1AYI A C8  1 
HETATM 1659 C C9  . A1AYI B 2 .   ? -1.03309  -8.99865  -26.22879 1.000 33.57418  ? 301 A1AYI A C9  1 
HETATM 1660 O O   . HOH   C 3 .   ? -12.53932 -27.35520 -34.45283 1.000 49.96606  ? 401 HOH   A O   1 
HETATM 1661 O O   . HOH   C 3 .   ? -13.49044 -26.19286 -5.32596  1.000 62.83143  ? 402 HOH   A O   1 
HETATM 1662 O O   . HOH   C 3 .   ? -11.92977 -28.25309 -29.69162 1.000 45.22116  ? 403 HOH   A O   1 
HETATM 1663 O O   . HOH   C 3 .   ? -17.71010 -4.38295  -37.09138 1.000 55.60652  ? 404 HOH   A O   1 
HETATM 1664 O O   . HOH   C 3 .   ? -17.93482 -2.64586  -35.57713 1.000 50.27513  ? 405 HOH   A O   1 
HETATM 1665 O O   . HOH   C 3 .   ? -14.25917 -7.22861  -42.34679 1.000 57.19261  ? 406 HOH   A O   1 
HETATM 1666 O O   . HOH   C 3 .   ? -1.63697  -28.76588 -5.68980  1.000 39.01601  ? 407 HOH   A O   1 
HETATM 1667 O O   . HOH   C 3 .   ? -23.262   -31.550   -12.893   1.000 54.86686  ? 408 HOH   A O   1 
HETATM 1668 O O   . HOH   C 3 .   ? 3.29208   -29.51848 -25.52885 1.000 55.49674  ? 409 HOH   A O   1 
HETATM 1669 O O   . HOH   C 3 .   ? -14.29542 -10.97313 0.42395   1.000 51.29079  ? 410 HOH   A O   1 
HETATM 1670 O O   . HOH   C 3 .   ? 2.87754   -29.97798 -18.67746 1.000 52.24519  ? 411 HOH   A O   1 
HETATM 1671 O O   . HOH   C 3 .   ? 1.84464   -15.70635 -40.93018 1.000 46.94624  ? 412 HOH   A O   1 
HETATM 1672 O O   . HOH   C 3 .   ? 11.42444  -21.98888 -40.67549 1.000 50.03399  ? 413 HOH   A O   1 
HETATM 1673 O O   . HOH   C 3 .   ? 7.64462   -23.00834 -14.26768 1.000 35.28423  ? 414 HOH   A O   1 
HETATM 1674 O O   . HOH   C 3 .   ? 5.97774   -25.61525 -7.40106  1.000 45.66332  ? 415 HOH   A O   1 
HETATM 1675 O O   . HOH   C 3 .   ? -16.26108 -25.38410 -17.62236 1.000 30.03724  ? 416 HOH   A O   1 
HETATM 1676 O O   . HOH   C 3 .   ? 3.35574   -6.06986  -11.16086 1.000 31.94717  ? 417 HOH   A O   1 
HETATM 1677 O O   . HOH   C 3 .   ? -7.75811  -28.12765 -7.38145  1.000 41.40174  ? 418 HOH   A O   1 
HETATM 1678 O O   . HOH   C 3 .   ? 0.69193   -29.56309 -15.98354 1.000 43.98406  ? 419 HOH   A O   1 
HETATM 1679 O O   . HOH   C 3 .   ? -0.34876  -5.21774  -18.46159 1.000 30.91125  ? 420 HOH   A O   1 
HETATM 1680 O O   . HOH   C 3 .   ? -0.41525  -5.57235  -38.41730 1.000 44.52325  ? 421 HOH   A O   1 
HETATM 1681 O O   . HOH   C 3 .   ? -17.32130 -24.40241 -8.31364  1.000 55.15274  ? 422 HOH   A O   1 
HETATM 1682 O O   . HOH   C 3 .   ? -18.88768 -10.73860 -23.72107 1.000 36.70486  ? 423 HOH   A O   1 
HETATM 1683 O O   . HOH   C 3 .   ? 7.61003   -18.44838 -6.59675  1.000 28.14275  ? 424 HOH   A O   1 
HETATM 1684 O O   . HOH   C 3 .   ? 7.47515   -30.53192 -15.04560 1.000 53.17098  ? 425 HOH   A O   1 
HETATM 1685 O O   . HOH   C 3 .   ? 1.50518   -7.68664  -16.62348 1.000 26.83833  ? 426 HOH   A O   1 
HETATM 1686 O O   . HOH   C 3 .   ? 7.42037   -27.90229 -23.88988 1.000 33.52652  ? 427 HOH   A O   1 
HETATM 1687 O O   . HOH   C 3 .   ? -13.42548 -0.67404  -20.66394 1.000 43.28168  ? 428 HOH   A O   1 
HETATM 1688 O O   . HOH   C 3 .   ? 10.90478  -28.52887 -30.62434 1.000 34.10184  ? 429 HOH   A O   1 
HETATM 1689 O O   . HOH   C 3 .   ? 8.90127   -26.31637 -16.88008 1.000 33.96145  ? 430 HOH   A O   1 
HETATM 1690 O O   . HOH   C 3 .   ? 3.36081   -7.95863  -36.97686 1.000 42.36553  ? 431 HOH   A O   1 
HETATM 1691 O O   . HOH   C 3 .   ? -8.30454  1.95067   -36.67663 1.000 42.09307  ? 432 HOH   A O   1 
HETATM 1692 O O   . HOH   C 3 .   ? -14.70694 -22.28994 -11.28801 1.000 35.11579  ? 433 HOH   A O   1 
HETATM 1693 O O   . HOH   C 3 .   ? 20.53406  -10.89190 -26.21542 1.000 47.03191  ? 434 HOH   A O   1 
HETATM 1694 O O   . HOH   C 3 .   ? -14.43707 -6.70700  -14.49874 1.000 36.59496  ? 435 HOH   A O   1 
HETATM 1695 O O   . HOH   C 3 .   ? 2.71899   -24.82532 -38.58208 1.000 41.56957  ? 436 HOH   A O   1 
HETATM 1696 O O   . HOH   C 3 .   ? -16.37557 -12.49472 -19.69778 1.000 23.75734  ? 437 HOH   A O   1 
HETATM 1697 O O   . HOH   C 3 .   ? 6.19490   -29.56034 -20.12746 1.000 39.53286  ? 438 HOH   A O   1 
HETATM 1698 O O   . HOH   C 3 .   ? -5.85208  -1.91152  -19.66391 1.000 29.54020  ? 439 HOH   A O   1 
HETATM 1699 O O   . HOH   C 3 .   ? -3.09655  -1.10767  -24.36968 1.000 38.23945  ? 440 HOH   A O   1 
HETATM 1700 O O   . HOH   C 3 .   ? -0.26933  -28.35190 -25.72757 1.000 54.51461  ? 441 HOH   A O   1 
HETATM 1701 O O   . HOH   C 3 .   ? -9.22642  -2.22677  -17.60926 1.000 26.21415  ? 442 HOH   A O   1 
HETATM 1702 O O   . HOH   C 3 .   ? -10.57781 -14.11094 1.09873   1.000 36.53064  ? 443 HOH   A O   1 
HETATM 1703 O O   . HOH   C 3 .   ? -13.17697 -7.05872  -12.18685 1.000 37.11850  ? 444 HOH   A O   1 
HETATM 1704 O O   . HOH   C 3 .   ? 5.57693   -22.16901 -37.28079 1.000 36.71187  ? 445 HOH   A O   1 
HETATM 1705 O O   . HOH   C 3 .   ? 0.80240   -20.64178 -4.65636  1.000 33.96052  ? 446 HOH   A O   1 
HETATM 1706 O O   . HOH   C 3 .   ? -8.78346  -11.87540 -36.45797 1.000 31.49845  ? 447 HOH   A O   1 
HETATM 1707 O O   . HOH   C 3 .   ? 10.30189  -25.42371 -23.63191 1.000 25.91054  ? 448 HOH   A O   1 
HETATM 1708 O O   . HOH   C 3 .   ? 19.63985  -16.85693 -27.53908 1.000 43.05543  ? 449 HOH   A O   1 
HETATM 1709 O O   . HOH   C 3 .   ? -6.55292  -7.76172  -34.43784 1.000 25.30040  ? 450 HOH   A O   1 
HETATM 1710 O O   . HOH   C 3 .   ? -3.38119  -11.70564 -9.07950  1.000 36.71434  ? 451 HOH   A O   1 
HETATM 1711 O O   . HOH   C 3 .   ? 7.85301   -23.01216 -7.23683  1.000 42.37001  ? 452 HOH   A O   1 
HETATM 1712 O O   . HOH   C 3 .   ? -0.92891  -11.00222 -3.21640  1.000 43.93154  ? 453 HOH   A O   1 
HETATM 1713 O O   . HOH   C 3 .   ? 13.64030  -11.94423 -29.79109 1.000 46.84701  ? 454 HOH   A O   1 
HETATM 1714 O O   . HOH   C 3 .   ? 9.65357   -14.78204 -25.42791 1.000 24.52684  ? 455 HOH   A O   1 
HETATM 1715 O O   . HOH   C 3 .   ? 18.30368  -7.33329  -20.54458 1.000 41.11258  ? 456 HOH   A O   1 
HETATM 1716 O O   . HOH   C 3 .   ? -0.53549  -7.13199  -31.06487 1.000 32.58775  ? 457 HOH   A O   1 
HETATM 1717 O O   . HOH   C 3 .   ? 0.51655   -22.35295 -1.93602  1.000 47.80994  ? 458 HOH   A O   1 
HETATM 1718 O O   . HOH   C 3 .   ? 11.09993  -8.08858  -27.66698 1.000 27.76600  ? 459 HOH   A O   1 
HETATM 1719 O O   . HOH   C 3 .   ? 9.44385   -11.28109 -34.97538 1.000 47.99855  ? 460 HOH   A O   1 
HETATM 1720 O O   . HOH   C 3 .   ? -11.33445 -14.05612 -37.71803 1.000 41.86736  ? 461 HOH   A O   1 
HETATM 1721 O O   . HOH   C 3 .   ? -8.44122  4.81749   -33.68790 1.000 34.78543  ? 462 HOH   A O   1 
HETATM 1722 O O   . HOH   C 3 .   ? 9.68085   -17.15398 -7.90623  1.000 28.66604  ? 463 HOH   A O   1 
HETATM 1723 O O   . HOH   C 3 .   ? 8.61011   -15.42100 -27.93109 1.000 25.18302  ? 464 HOH   A O   1 
HETATM 1724 O O   . HOH   C 3 .   ? -5.24138  -10.43805 -27.30337 1.000 23.46579  ? 465 HOH   A O   1 
HETATM 1725 O O   . HOH   C 3 .   ? -15.89234 0.17690   -30.45818 1.000 44.25905  ? 466 HOH   A O   1 
HETATM 1726 O O   . HOH   C 3 .   ? 10.495    -18.281   -39.213   1.000 49.45679  ? 467 HOH   A O   1 
HETATM 1727 O O   . HOH   C 3 .   ? -8.28513  -24.64055 -18.91787 1.000 22.55335  ? 468 HOH   A O   1 
HETATM 1728 O O   . HOH   C 3 .   ? -13.73797 -16.67173 -2.61235  1.000 30.24190  ? 469 HOH   A O   1 
HETATM 1729 O O   . HOH   C 3 .   ? 13.48784  -14.35330 -27.05200 1.000 27.91622  ? 470 HOH   A O   1 
HETATM 1730 O O   . HOH   C 3 .   ? 6.25414   -26.82777 -27.49379 1.000 38.11527  ? 471 HOH   A O   1 
HETATM 1731 O O   . HOH   C 3 .   ? 6.05828   -20.80782 -0.16184  1.000 34.13574  ? 472 HOH   A O   1 
HETATM 1732 O O   . HOH   C 3 .   ? -13.11987 -24.52327 -10.70238 1.000 36.32042  ? 473 HOH   A O   1 
HETATM 1733 O O   . HOH   C 3 .   ? -2.43515  -13.65111 -35.66191 1.000 24.69809  ? 474 HOH   A O   1 
HETATM 1734 O O   . HOH   C 3 .   ? -17.04532 -5.19797  -22.74947 1.000 32.13659  ? 475 HOH   A O   1 
HETATM 1735 O O   . HOH   C 3 .   ? 0.35824   -1.55664  -19.80456 1.000 42.79394  ? 476 HOH   A O   1 
HETATM 1736 O O   . HOH   C 3 .   ? -4.89709  0.56177   -30.62608 1.000 40.27984  ? 477 HOH   A O   1 
HETATM 1737 O O   . HOH   C 3 .   ? 15.77740  -0.82982  -19.67915 1.000 34.95228  ? 478 HOH   A O   1 
HETATM 1738 O O   . HOH   C 3 .   ? -13.56813 -26.27221 -17.74921 1.000 32.35320  ? 479 HOH   A O   1 
HETATM 1739 O O   . HOH   C 3 .   ? -7.84612  -24.28077 -22.80404 1.000 37.97446  ? 480 HOH   A O   1 
HETATM 1740 O O   . HOH   C 3 .   ? -17.99820 -18.56001 -10.99755 1.000 43.52984  ? 481 HOH   A O   1 
HETATM 1741 O O   . HOH   C 3 .   ? 7.97668   1.31725   -14.81038 1.000 40.74298  ? 482 HOH   A O   1 
HETATM 1742 O O   . HOH   C 3 .   ? 11.24760  -27.67573 -34.70500 1.000 34.69622  ? 483 HOH   A O   1 
HETATM 1743 O O   . HOH   C 3 .   ? -7.63404  -27.76203 -20.92446 1.000 46.67326  ? 484 HOH   A O   1 
HETATM 1744 O O   . HOH   C 3 .   ? -2.15033  -0.57661  -18.51621 1.000 43.21402  ? 485 HOH   A O   1 
HETATM 1745 O O   . HOH   C 3 .   ? 14.06871  -15.50363 -2.07547  1.000 42.02612  ? 486 HOH   A O   1 
HETATM 1746 O O   . HOH   C 3 .   ? -19.83618 -19.24081 -14.10674 1.000 25.90182  ? 487 HOH   A O   1 
HETATM 1747 O O   . HOH   C 3 .   ? 3.78900   -24.29666 -30.59303 1.000 26.89897  ? 488 HOH   A O   1 
HETATM 1748 O O   . HOH   C 3 .   ? -9.01177  -30.52976 -23.34802 1.000 60.34166  ? 489 HOH   A O   1 
HETATM 1749 O O   . HOH   C 3 .   ? -14.11850 -12.26068 -7.74607  1.000 30.79269  ? 490 HOH   A O   1 
HETATM 1750 O O   . HOH   C 3 .   ? 17.78487  -19.53897 -24.77638 1.000 31.77492  ? 491 HOH   A O   1 
HETATM 1751 O O   . HOH   C 3 .   ? -6.16698  -11.13663 -10.08530 1.000 29.85938  ? 492 HOH   A O   1 
HETATM 1752 O O   . HOH   C 3 .   ? -6.21894  -13.70042 0.88562   1.000 35.84524  ? 493 HOH   A O   1 
HETATM 1753 O O   . HOH   C 3 .   ? 5.18225   -9.47010  -2.51421  1.000 54.26164  ? 494 HOH   A O   1 
HETATM 1754 O O   . HOH   C 3 .   ? -6.65481  -4.99470  -39.05530 1.000 47.26780  ? 495 HOH   A O   1 
HETATM 1755 O O   . HOH   C 3 .   ? -5.18154  -14.06887 -22.71074 1.000 24.73596  ? 496 HOH   A O   1 
HETATM 1756 O O   . HOH   C 3 .   ? -9.86898  -33.71799 -20.95803 1.000 54.16422  ? 497 HOH   A O   1 
HETATM 1757 O O   . HOH   C 3 .   ? 8.89734   -20.07773 -4.42342  1.000 32.04043  ? 498 HOH   A O   1 
HETATM 1758 O O   . HOH   C 3 .   ? -14.71196 -4.20854  -12.53779 1.000 42.21719  ? 499 HOH   A O   1 
HETATM 1759 O O   . HOH   C 3 .   ? 15.43063  -20.25564 -18.77146 1.000 30.68982  ? 500 HOH   A O   1 
HETATM 1760 O O   . HOH   C 3 .   ? -15.31652 -10.99272 -29.78396 1.000 30.72784  ? 501 HOH   A O   1 
HETATM 1761 O O   . HOH   C 3 .   ? 6.39083   -22.93927 -41.46145 1.000 60.06135  ? 502 HOH   A O   1 
HETATM 1762 O O   . HOH   C 3 .   ? -4.00437  -13.58091 -0.83844  1.000 46.98248  ? 503 HOH   A O   1 
HETATM 1763 O O   . HOH   C 3 .   ? -3.30397  -20.83122 -0.43683  1.000 41.33072  ? 504 HOH   A O   1 
HETATM 1764 O O   . HOH   C 3 .   ? 2.88729   -20.16595 -2.56502  1.000 42.99073  ? 505 HOH   A O   1 
HETATM 1765 O O   . HOH   C 3 .   ? -6.64904  1.59484   -19.63019 1.000 53.23683  ? 506 HOH   A O   1 
HETATM 1766 O O   . HOH   C 3 .   ? -8.97242  -18.16374 -36.53268 1.000 50.20481  ? 507 HOH   A O   1 
HETATM 1767 O O   . HOH   C 3 .   ? 15.35988  -7.53612  -28.06073 1.000 38.23709  ? 508 HOH   A O   1 
HETATM 1768 O O   . HOH   C 3 .   ? 0.54155   -14.69886 -1.31991  1.000 47.80987  ? 509 HOH   A O   1 
HETATM 1769 O O   . HOH   C 3 .   ? -6.51613  -5.02898  -35.81289 1.000 29.53862  ? 510 HOH   A O   1 
HETATM 1770 O O   . HOH   C 3 .   ? 0.61691   -4.96444  -14.19534 1.000 44.43461  ? 511 HOH   A O   1 
HETATM 1771 O O   . HOH   C 3 .   ? -17.96849 -3.58505  -28.91090 1.000 53.93884  ? 512 HOH   A O   1 
HETATM 1772 O O   . HOH   C 3 .   ? 14.18999  -16.18326 -30.97753 1.000 40.27416  ? 513 HOH   A O   1 
HETATM 1773 O O   . HOH   C 3 .   ? -5.86391  -31.01182 -11.26281 1.000 41.08207  ? 514 HOH   A O   1 
HETATM 1774 O O   . HOH   C 3 .   ? 3.64527   -6.58882  -18.11641 1.000 29.87083  ? 515 HOH   A O   1 
HETATM 1775 O O   . HOH   C 3 .   ? 10.53058  -25.70188 -26.67373 1.000 32.93800  ? 516 HOH   A O   1 
HETATM 1776 O O   . HOH   C 3 .   ? 3.89583   -9.03820  -20.40407 1.000 25.94361  ? 517 HOH   A O   1 
HETATM 1777 O O   . HOH   C 3 .   ? -8.32747  -3.79489  -10.67039 1.000 30.71878  ? 518 HOH   A O   1 
HETATM 1778 O O   . HOH   C 3 .   ? -5.45877  -7.33957  -13.24115 1.000 24.34143  ? 519 HOH   A O   1 
HETATM 1779 O O   . HOH   C 3 .   ? -10.34984 -11.11399 -2.02338  1.000 30.48019  ? 520 HOH   A O   1 
HETATM 1780 O O   . HOH   C 3 .   ? 18.520    -15.878   -13.681   1.000 43.53367  ? 521 HOH   A O   1 
HETATM 1781 O O   . HOH   C 3 .   ? -8.00204  -13.57003 -40.96289 1.000 49.88947  ? 522 HOH   A O   1 
HETATM 1782 O O   . HOH   C 3 .   ? -9.02708  -25.40448 -29.58873 1.000 52.19374  ? 523 HOH   A O   1 
HETATM 1783 O O   . HOH   C 3 .   ? -16.24313 -2.96230  -21.22463 1.000 35.66001  ? 524 HOH   A O   1 
HETATM 1784 O O   . HOH   C 3 .   ? -10.41587 -15.01538 -28.24340 1.000 36.88529  ? 525 HOH   A O   1 
HETATM 1785 O O   . HOH   C 3 .   ? -3.996    0.380     -22.063   1.000 49.46272  ? 526 HOH   A O   1 
HETATM 1786 O O   . HOH   C 3 .   ? -4.94832  -26.03263 -30.07490 1.000 55.57779  ? 527 HOH   A O   1 
HETATM 1787 O O   . HOH   C 3 .   ? -1.27636  -29.85829 -17.39355 1.000 41.10296  ? 528 HOH   A O   1 
HETATM 1788 O O   . HOH   C 3 .   ? 5.63899   -3.46854  -26.32395 1.000 45.74192  ? 529 HOH   A O   1 
HETATM 1789 O O   . HOH   C 3 .   ? 1.66031   -3.90324  -16.99043 1.000 37.43788  ? 530 HOH   A O   1 
HETATM 1790 O O   . HOH   C 3 .   ? 4.01414   -19.55714 -40.68589 1.000 40.50251  ? 531 HOH   A O   1 
HETATM 1791 O O   . HOH   C 3 .   ? 8.15443   -16.48541 -39.54603 1.000 41.34420  ? 532 HOH   A O   1 
HETATM 1792 O O   . HOH   C 3 .   ? -12.51365 -20.61297 -29.81692 1.000 48.99408  ? 533 HOH   A O   1 
HETATM 1793 O O   . HOH   C 3 .   ? 13.56980  -20.47646 -20.79022 1.000 25.66982  ? 534 HOH   A O   1 
HETATM 1794 O O   . HOH   C 3 .   ? -1.75064  -4.39240  -33.83910 1.000 43.06438  ? 535 HOH   A O   1 
HETATM 1795 O O   . HOH   C 3 .   ? -15.91201 -4.00446  -15.25575 1.000 46.30433  ? 536 HOH   A O   1 
HETATM 1796 O O   . HOH   C 3 .   ? 0.44667   -27.05825 -37.41021 1.000 46.86907  ? 537 HOH   A O   1 
HETATM 1797 O O   . HOH   C 3 .   ? 8.30614   -20.38379 -9.51388  1.000 35.77622  ? 538 HOH   A O   1 
HETATM 1798 O O   . HOH   C 3 .   ? -17.405   -28.534   -17.031   1.000 51.20790  ? 539 HOH   A O   1 
HETATM 1799 O O   . HOH   C 3 .   ? 13.58474  -4.09218  -25.65676 1.000 21.34564  ? 540 HOH   A O   1 
HETATM 1800 O O   . HOH   C 3 .   ? -7.77679  -4.78004  -2.94866  1.000 49.13902  ? 541 HOH   A O   1 
HETATM 1801 O O   . HOH   C 3 .   ? -11.50423 -29.84443 -4.98185  1.000 65.76564  ? 542 HOH   A O   1 
HETATM 1802 O O   . HOH   C 3 .   ? 12.93727  -13.93956 -29.86409 1.000 37.16596  ? 543 HOH   A O   1 
HETATM 1803 O O   . HOH   C 3 .   ? -16.47100 -8.82000  -14.21562 1.000 39.45418  ? 544 HOH   A O   1 
HETATM 1804 O O   . HOH   C 3 .   ? 2.01067   -6.05364  -26.39021 1.000 47.85945  ? 545 HOH   A O   1 
HETATM 1805 O O   . HOH   C 3 .   ? -17.47999 -22.39950 -4.59791  1.000 55.64006  ? 546 HOH   A O   1 
HETATM 1806 O O   . HOH   C 3 .   ? 4.81491   -30.30229 -11.42999 1.000 44.93635  ? 547 HOH   A O   1 
HETATM 1807 O O   . HOH   C 3 .   ? 20.81619  -14.18063 -26.84171 1.000 40.76605  ? 548 HOH   A O   1 
HETATM 1808 O O   . HOH   C 3 .   ? -17.85297 -14.81370 -13.03785 1.000 27.50654  ? 549 HOH   A O   1 
HETATM 1809 O O   . HOH   C 3 .   ? -1.82420  -25.43055 -4.62285  1.000 30.16403  ? 550 HOH   A O   1 
HETATM 1810 O O   . HOH   C 3 .   ? -0.53644  -12.33830 -21.00150 1.000 29.91136  ? 551 HOH   A O   1 
HETATM 1811 O O   . HOH   C 3 .   ? 3.58107   -11.92266 -38.66668 1.000 32.22984  ? 552 HOH   A O   1 
HETATM 1812 O O   . HOH   C 3 .   ? -15.16091 -11.90646 -11.94336 1.000 39.17193  ? 553 HOH   A O   1 
HETATM 1813 O O   . HOH   C 3 .   ? -3.36174  -13.00536 -20.69634 1.000 26.24757  ? 554 HOH   A O   1 
HETATM 1814 O O   . HOH   C 3 .   ? -2.48570  -15.42913 -0.24843  1.000 44.00268  ? 555 HOH   A O   1 
HETATM 1815 O O   . HOH   C 3 .   ? 6.22104   -4.91608  -22.96673 1.000 38.85539  ? 556 HOH   A O   1 
HETATM 1816 O O   . HOH   C 3 .   ? 13.95471  -8.69493  -30.30113 1.000 51.47468  ? 557 HOH   A O   1 
HETATM 1817 O O   . HOH   C 3 .   ? -21.31415 -28.19072 -11.25180 1.000 70.42234  ? 558 HOH   A O   1 
HETATM 1818 O O   . HOH   C 3 .   ? -12.30369 -26.71017 -20.07218 1.000 33.53645  ? 559 HOH   A O   1 
HETATM 1819 O O   . HOH   C 3 .   ? 7.34857   1.86592   -12.44181 1.000 38.99153  ? 560 HOH   A O   1 
HETATM 1820 O O   . HOH   C 3 .   ? -13.63108 -25.45816 -7.53060  1.000 35.99860  ? 561 HOH   A O   1 
HETATM 1821 O O   . HOH   C 3 .   ? 3.06605   -3.72529  -9.21937  1.000 54.40366  ? 562 HOH   A O   1 
HETATM 1822 O O   . HOH   C 3 .   ? -11.83866 -7.64039  -38.66190 1.000 46.61031  ? 563 HOH   A O   1 
HETATM 1823 O O   . HOH   C 3 .   ? 2.49941   -7.67042  -24.94546 1.000 44.44245  ? 564 HOH   A O   1 
HETATM 1824 O O   . HOH   C 3 .   ? 0.62960   -5.36652  -21.99662 1.000 38.69220  ? 565 HOH   A O   1 
HETATM 1825 O O   . HOH   C 3 .   ? -6.27543  -18.69246 -39.13167 1.000 40.17129  ? 566 HOH   A O   1 
HETATM 1826 O O   . HOH   C 3 .   ? -9.50192  -0.18649  -19.57564 1.000 47.52391  ? 567 HOH   A O   1 
HETATM 1827 O O   . HOH   C 3 .   ? 2.99888   -5.43372  -6.71664  1.000 55.32252  ? 568 HOH   A O   1 
HETATM 1828 O O   . HOH   C 3 .   ? -19.77406 -10.52580 -32.35531 1.000 49.10479  ? 569 HOH   A O   1 
HETATM 1829 O O   . HOH   C 3 .   ? -14.07997 -0.47891  -13.47539 1.000 38.92293  ? 570 HOH   A O   1 
HETATM 1830 O O   . HOH   C 3 .   ? 13.26167  -6.90958  -26.46240 1.000 28.03104  ? 571 HOH   A O   1 
HETATM 1831 O O   . HOH   C 3 .   ? -14.21258 -16.00594 -25.91621 1.000 35.84695  ? 572 HOH   A O   1 
HETATM 1832 O O   . HOH   C 3 .   ? -5.553    -11.179   0.863     1.000 59.04858  ? 573 HOH   A O   1 
HETATM 1833 O O   . HOH   C 3 .   ? 11.15403  -10.83657 -4.76922  1.000 44.74934  ? 574 HOH   A O   1 
HETATM 1834 O O   . HOH   C 3 .   ? -13.27279 -12.28321 -30.91877 1.000 31.19101  ? 575 HOH   A O   1 
HETATM 1835 O O   . HOH   C 3 .   ? 4.228     -1.809    -18.037   1.000 55.80052  ? 576 HOH   A O   1 
HETATM 1836 O O   . HOH   C 3 .   ? 3.94738   -22.57363 -3.38304  1.000 40.34052  ? 577 HOH   A O   1 
HETATM 1837 O O   . HOH   C 3 .   ? 16.598    -25.376   -25.294   1.000 46.17869  ? 578 HOH   A O   1 
HETATM 1838 O O   . HOH   C 3 .   ? -6.26064  -7.24203  -42.70720 1.000 55.06570  ? 579 HOH   A O   1 
HETATM 1839 O O   . HOH   C 3 .   ? -5.08335  -4.98858  -12.10847 1.000 41.51665  ? 580 HOH   A O   1 
HETATM 1840 O O   . HOH   C 3 .   ? -14.06700 -23.69331 -4.63268  1.000 35.34910  ? 581 HOH   A O   1 
HETATM 1841 O O   . HOH   C 3 .   ? -0.02015  -16.43890 -3.40316  1.000 33.67497  ? 582 HOH   A O   1 
HETATM 1842 O O   . HOH   C 3 .   ? -16.50946 -24.98201 -10.41220 1.000 42.93860  ? 583 HOH   A O   1 
HETATM 1843 O O   . HOH   C 3 .   ? 1.91194   -7.84334  -22.38497 1.000 46.37653  ? 584 HOH   A O   1 
HETATM 1844 O O   . HOH   C 3 .   ? -14.01066 -18.61660 -24.29128 1.000 29.45029  ? 585 HOH   A O   1 
HETATM 1845 O O   . HOH   C 3 .   ? 1.97831   -24.83370 -2.64344  1.000 52.19963  ? 586 HOH   A O   1 
HETATM 1846 O O   . HOH   C 3 .   ? 17.72094  -15.74098 -29.63292 1.000 50.08991  ? 587 HOH   A O   1 
HETATM 1847 O O   . HOH   C 3 .   ? -18.37456 -5.79530  -25.26859 1.000 40.96216  ? 588 HOH   A O   1 
HETATM 1848 O O   . HOH   C 3 .   ? 0.99985   -8.33782  -3.98585  1.000 42.70370  ? 589 HOH   A O   1 
HETATM 1849 O O   . HOH   C 3 .   ? 7.550     -7.680    -33.808   1.000 38.06580  ? 590 HOH   A O   1 
HETATM 1850 O O   . HOH   C 3 .   ? -1.47544  -26.30326 -32.29898 1.000 45.45870  ? 591 HOH   A O   1 
HETATM 1851 O O   . HOH   C 3 .   ? 21.930    -13.561   -19.579   1.000 51.35770  ? 592 HOH   A O   1 
HETATM 1852 O O   . HOH   C 3 .   ? 1.595     -17.805   -0.002    1.000 39.39614  ? 593 HOH   A O   1 
HETATM 1853 O O   . HOH   C 3 .   ? -4.01658  -32.68865 -10.94359 1.000 50.42625  ? 594 HOH   A O   1 
HETATM 1854 O O   . HOH   C 3 .   ? 6.71546   -30.00812 -29.41542 1.000 58.90035  ? 595 HOH   A O   1 
HETATM 1855 O O   . HOH   C 3 .   ? 14.35191  -22.39107 -17.16244 1.000 36.71630  ? 596 HOH   A O   1 
HETATM 1856 O O   . HOH   C 3 .   ? 1.77909   -25.91384 -29.17052 1.000 40.82519  ? 597 HOH   A O   1 
HETATM 1857 O O   . HOH   C 3 .   ? -7.64731  -7.74418  0.41297   1.000 52.63817  ? 598 HOH   A O   1 
HETATM 1858 O O   . HOH   C 3 .   ? -4.84805  -3.21788  -15.82926 1.000 47.48505  ? 599 HOH   A O   1 
HETATM 1859 O O   . HOH   C 3 .   ? 19.765    -14.072   -12.483   1.000 56.81781  ? 600 HOH   A O   1 
HETATM 1860 O O   . HOH   C 3 .   ? -14.15738 -28.98742 -16.81050 1.000 50.23670  ? 601 HOH   A O   1 
HETATM 1861 O O   . HOH   C 3 .   ? 8.08491   -26.21849 -25.86711 1.000 44.11650  ? 602 HOH   A O   1 
HETATM 1862 O O   . HOH   C 3 .   ? 1.81241   -3.08259  -13.22908 1.000 47.53021  ? 603 HOH   A O   1 
HETATM 1863 O O   . HOH   C 3 .   ? 11.851    -25.510   -38.368   1.000 37.24013  ? 604 HOH   A O   1 
HETATM 1864 O O   . HOH   C 3 .   ? 17.57343  -21.63776 -19.89734 1.000 40.36910  ? 605 HOH   A O   1 
HETATM 1865 O O   . HOH   C 3 .   ? -12.50185 -16.32131 -28.15864 1.000 40.55394  ? 606 HOH   A O   1 
HETATM 1866 O O   . HOH   C 3 .   ? -14.16764 -9.49333  -8.31174  1.000 37.27870  ? 607 HOH   A O   1 
HETATM 1867 O O   . HOH   C 3 .   ? -17.38081 -4.34772  -17.29584 1.000 51.79681  ? 608 HOH   A O   1 
HETATM 1868 O O   . HOH   C 3 .   ? 16.91742  0.55660   -17.74631 1.000 46.03239  ? 609 HOH   A O   1 
HETATM 1869 O O   . HOH   C 3 .   ? -2.27163  1.00213   -26.28393 1.000 43.98769  ? 610 HOH   A O   1 
HETATM 1870 O O   . HOH   C 3 .   ? -18.77580 -16.79617 -11.14953 1.000 60.47906  ? 611 HOH   A O   1 
HETATM 1871 O O   . HOH   C 3 .   ? 3.55702   -9.36553  -39.11408 1.000 45.07590  ? 612 HOH   A O   1 
HETATM 1872 O O   . HOH   C 3 .   ? -9.82440  -29.10253 -30.58492 1.000 53.64766  ? 613 HOH   A O   1 
HETATM 1873 O O   . HOH   C 3 .   ? -12.06877 -9.46269  -39.57968 1.000 52.25600  ? 614 HOH   A O   1 
HETATM 1874 O O   . HOH   C 3 .   ? 2.82858   -5.18662  -20.39843 1.000 47.68568  ? 615 HOH   A O   1 
HETATM 1875 O O   . HOH   C 3 .   ? -13.98682 -13.82442 -2.68998  1.000 41.22366  ? 616 HOH   A O   1 
HETATM 1876 O O   . HOH   C 3 .   ? -11.84660 -26.62881 -27.65455 1.000 49.75869  ? 617 HOH   A O   1 
HETATM 1877 O O   . HOH   C 3 .   ? 1.94321   -6.72340  -29.92221 1.000 52.54876  ? 618 HOH   A O   1 
HETATM 1878 O O   . HOH   C 3 .   ? 3.569     0.022     -16.421   1.000 48.39783  ? 619 HOH   A O   1 
HETATM 1879 O O   . HOH   C 3 .   ? 12.268    -18.912   -41.257   1.000 58.10345  ? 620 HOH   A O   1 
HETATM 1880 O O   . HOH   C 3 .   ? -9.96008  -25.78950 -20.59489 1.000 34.18453  ? 621 HOH   A O   1 
HETATM 1881 O O   . HOH   C 3 .   ? -18.75592 -11.34470 -20.98403 1.000 33.96711  ? 622 HOH   A O   1 
HETATM 1882 O O   . HOH   C 3 .   ? -0.75506  -29.06365 -3.09798  1.000 58.33479  ? 623 HOH   A O   1 
HETATM 1883 O O   . HOH   C 3 .   ? 7.78542   -13.86131 -38.42163 1.000 42.19115  ? 624 HOH   A O   1 
HETATM 1884 O O   . HOH   C 3 .   ? 18.09024  -3.27428  -24.30100 1.000 47.82049  ? 625 HOH   A O   1 
HETATM 1885 O O   . HOH   C 3 .   ? 19.13586  -8.41175  -18.02493 1.000 44.54411  ? 626 HOH   A O   1 
HETATM 1886 O O   . HOH   C 3 .   ? 6.92484   -28.97091 -11.60247 1.000 66.63355  ? 627 HOH   A O   1 
HETATM 1887 O O   . HOH   C 3 .   ? 5.70179   -23.94557 -43.34716 1.000 66.08698  ? 628 HOH   A O   1 
HETATM 1888 O O   . HOH   C 3 .   ? 7.54135   -28.97880 -28.04764 1.000 53.68229  ? 629 HOH   A O   1 
HETATM 1889 O O   . HOH   C 3 .   ? 4.63907   -3.29438  -24.09090 1.000 50.32078  ? 630 HOH   A O   1 
HETATM 1890 O O   . HOH   C 3 .   ? 5.53093   -13.30516 -40.00321 1.000 35.54418  ? 631 HOH   A O   1 
HETATM 1891 O O   . HOH   C 3 .   ? 5.191     2.786     -12.901   1.000 47.43200  ? 632 HOH   A O   1 
HETATM 1892 O O   . HOH   C 3 .   ? 6.61056   -21.33684 -2.79415  1.000 36.06641  ? 633 HOH   A O   1 
HETATM 1893 O O   . HOH   C 3 .   ? -0.97468  -26.62917 -30.49708 1.000 46.87361  ? 634 HOH   A O   1 
HETATM 1894 O O   . HOH   C 3 .   ? 20.41840  -6.49390  -16.70284 1.000 51.74500  ? 635 HOH   A O   1 
HETATM 1895 O O   . HOH   C 3 .   ? -16.291   3.198     -26.579   1.000 43.28237  ? 636 HOH   A O   1 
HETATM 1896 O O   . HOH   C 3 .   ? -7.35375  -26.72820 -22.80227 1.000 58.80275  ? 637 HOH   A O   1 
HETATM 1897 O O   . HOH   C 3 .   ? 10.80852  -28.14570 -27.90956 1.000 41.88769  ? 638 HOH   A O   1 
HETATM 1898 O O   . HOH   C 3 .   ? -10.222   -22.316   4.418     1.000 53.43038  ? 639 HOH   A O   1 
HETATM 1899 O O   . HOH   C 3 .   ? -9.96657  -8.31518  -1.01766  1.000 52.47262  ? 640 HOH   A O   1 
HETATM 1900 O O   . HOH   C 3 .   ? 9.52064   -25.44915 -14.78606 1.000 48.84652  ? 641 HOH   A O   1 
HETATM 1901 O O   . HOH   C 3 .   ? -3.010    1.893     -20.246   1.000 48.97756  ? 642 HOH   A O   1 
HETATM 1902 O O   . HOH   C 3 .   ? 4.19422   -14.93201 -41.73009 1.000 53.61442  ? 643 HOH   A O   1 
HETATM 1903 O O   . HOH   C 3 .   ? 20.23665  -5.49589  -21.94221 1.000 51.04710  ? 644 HOH   A O   1 
HETATM 1904 O O   . HOH   C 3 .   ? 11.27329  -30.24758 -34.45469 1.000 48.69373  ? 645 HOH   A O   1 
HETATM 1905 O O   . HOH   C 3 .   ? -7.20164  -30.41863 -8.82943  1.000 41.66980  ? 646 HOH   A O   1 
HETATM 1906 O O   . HOH   C 3 .   ? -0.00000  -0.00000  -18.26189 0.50  28.14723  ? 647 HOH   A O   1 
HETATM 1907 O O   . HOH   C 3 .   ? 4.051     -2.027    -28.285   1.000 45.54886  ? 648 HOH   A O   1 
HETATM 1908 O O   . HOH   C 3 .   ? -8.75193  -10.84214 0.10540   1.000 48.19042  ? 649 HOH   A O   1 
HETATM 1909 O O   . HOH   C 3 .   ? -12.37444 -12.72510 -0.92940  1.000 37.00852  ? 650 HOH   A O   1 
HETATM 1910 O O   . HOH   C 3 .   ? -16.41256 -12.34702 -6.09760  1.000 47.87846  ? 651 HOH   A O   1 
HETATM 1911 O O   . HOH   C 3 .   ? 21.760    -18.046   -25.360   1.000 51.21220  ? 652 HOH   A O   1 
HETATM 1912 O O   . HOH   C 3 .   ? -13.521   -24.551   -27.596   1.000 45.52707  ? 653 HOH   A O   1 
HETATM 1913 O O   . HOH   C 3 .   ? -14.12959 -14.20796 -37.92768 1.000 53.60839  ? 654 HOH   A O   1 
HETATM 1914 O O   . HOH   C 3 .   ? 0.72685   -1.35506  -16.77801 1.000 39.01477  ? 655 HOH   A O   1 
HETATM 1915 O O   . HOH   C 3 .   ? -6.961    -22.672   -1.621    1.000 44.51784  ? 656 HOH   A O   1 
HETATM 1916 O O   . HOH   C 3 .   ? -10.45624 -11.67621 2.03648   1.000 43.36366  ? 657 HOH   A O   1 
HETATM 1917 O O   . HOH   C 3 .   ? -16.11063 -17.39478 -2.58015  1.000 51.35177  ? 658 HOH   A O   1 
HETATM 1918 O O   . HOH   C 3 .   ? -20.70710 -10.22897 -19.53182 1.000 47.91242  ? 659 HOH   A O   1 
HETATM 1919 O O   . HOH   C 3 .   ? -17.16406 -15.13952 -10.23840 1.000 46.19431  ? 660 HOH   A O   1 
HETATM 1920 O O   . HOH   C 3 .   ? -19.53710 -5.88517  -21.53729 1.000 50.81234  ? 661 HOH   A O   1 
HETATM 1921 O O   . HOH   C 3 .   ? -14.86764 -9.21129  -11.20811 1.000 37.31466  ? 662 HOH   A O   1 
HETATM 1922 O O   . HOH   C 3 .   ? -14.58265 -13.78973 -10.27484 1.000 33.16616  ? 663 HOH   A O   1 
HETATM 1923 O O   . HOH   C 3 .   ? 15.00333  -13.03399 -2.94366  1.000 49.78393  ? 664 HOH   A O   1 
HETATM 1924 O O   . HOH   C 3 .   ? -19.37593 -4.17817  -19.05769 1.000 59.68873  ? 665 HOH   A O   1 
HETATM 1925 O O   . HOH   C 3 .   ? 4.30328   -20.26015 -43.37402 1.000 56.04039  ? 666 HOH   A O   1 
HETATM 1926 O O   . HOH   C 3 .   ? 13.90226  -11.17686 -5.14797  1.000 46.82099  ? 667 HOH   A O   1 
HETATM 1927 O O   . HOH   C 3 .   ? -18.20263 -13.50761 -8.37727  1.000 56.98586  ? 668 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   ? 0.59247 0.89421 0.59559 -0.06546 -0.03293 -0.27980 16  GLU A N   
2    C CA  . GLU A 9   ? 0.55569 0.82558 0.53335 -0.03268 -0.04333 -0.25500 16  GLU A CA  
3    C C   . GLU A 9   ? 0.49050 0.73888 0.47181 -0.02006 -0.04861 -0.23200 16  GLU A C   
4    O O   . GLU A 9   ? 0.57622 0.86900 0.56323 0.00002  -0.06008 -0.22171 16  GLU A O   
5    C CB  . GLU A 9   ? 0.64490 0.97125 0.60860 0.00143  -0.05831 -0.25080 16  GLU A CB  
6    C CG  . GLU A 9   ? 0.89159 1.17891 0.82333 0.02663  -0.05960 -0.23605 16  GLU A CG  
7    C CD  . GLU A 9   ? 0.96788 1.20956 0.88546 0.05187  -0.06156 -0.20693 16  GLU A CD  
8    O OE1 . GLU A 9   ? 0.94888 1.20388 0.87759 0.05927  -0.06701 -0.19482 16  GLU A OE1 
9    O OE2 . GLU A 9   ? 0.96983 1.16176 0.86513 0.06493  -0.05566 -0.19662 16  GLU A OE2 
10   N N   . VAL A 10  ? 0.42419 0.60387 0.40212 -0.03017 -0.03794 -0.22384 17  VAL A N   
11   C CA  . VAL A 10  ? 0.36367 0.51498 0.35011 -0.02178 -0.03893 -0.19723 17  VAL A CA  
12   C C   . VAL A 10  ? 0.43112 0.53464 0.40303 0.00532  -0.03826 -0.16364 17  VAL A C   
13   O O   . VAL A 10  ? 0.49303 0.55094 0.45607 0.00265  -0.02718 -0.15957 17  VAL A O   
14   C CB  . VAL A 10  ? 0.47978 0.58793 0.48166 -0.05223 -0.02089 -0.20057 17  VAL A CB  
15   C CG1 . VAL A 10  ? 0.41103 0.50072 0.42213 -0.04225 -0.02346 -0.17215 17  VAL A CG1 
16   C CG2 . VAL A 10  ? 0.63710 0.78317 0.65525 -0.08202 -0.01330 -0.23013 17  VAL A CG2 
17   N N   . GLU A 11  ? 0.32234 0.43586 0.29202 0.03037  -0.04711 -0.14108 18  GLU A N   
18   C CA  . GLU A 11  ? 0.33048 0.40123 0.29074 0.05124  -0.04309 -0.11231 18  GLU A CA  
19   C C   . GLU A 11  ? 0.37064 0.40986 0.34613 0.04338  -0.03846 -0.09458 18  GLU A C   
20   O O   . GLU A 11  ? 0.31030 0.37009 0.29647 0.03920  -0.04296 -0.09454 18  GLU A O   
21   C CB  . GLU A 11  ? 0.35974 0.45447 0.30309 0.08412  -0.04900 -0.10010 18  GLU A CB  
22   C CG  . GLU A 11  ? 0.37802 0.50250 0.29927 0.10111  -0.05292 -0.11188 18  GLU A CG  
23   C CD  . GLU A 11  ? 0.52544 0.67169 0.42489 0.13979  -0.05446 -0.09584 18  GLU A CD  
24   O OE1 . GLU A 11  ? 0.56637 0.75685 0.46771 0.15029  -0.06151 -0.09730 18  GLU A OE1 
25   O OE2 . GLU A 11  ? 0.64010 0.75663 0.51906 0.16144  -0.04553 -0.08054 18  GLU A OE2 
26   N N   . THR A 12  ? 0.33100 0.32593 0.30702 0.04295  -0.02966 -0.08012 19  THR A N   
27   C CA  . THR A 12  ? 0.29367 0.26695 0.28217 0.03821  -0.02617 -0.06420 19  THR A CA  
28   C C   . THR A 12  ? 0.32697 0.28894 0.31327 0.05498  -0.02516 -0.04599 19  THR A C   
29   O O   . THR A 12  ? 0.30617 0.25323 0.28371 0.06559  -0.02030 -0.04137 19  THR A O   
30   C CB  . THR A 12  ? 0.29432 0.23378 0.28603 0.02602  -0.01463 -0.06235 19  THR A CB  
31   O OG1 . THR A 12  ? 0.35799 0.30049 0.35044 0.00650  -0.00878 -0.08261 19  THR A OG1 
32   C CG2 . THR A 12  ? 0.31095 0.23920 0.31289 0.02549  -0.01258 -0.04575 19  THR A CG2 
33   N N   . PHE A 13  ? 0.29945 0.26747 0.29372 0.05515  -0.02711 -0.03783 20  PHE A N   
34   C CA  . PHE A 13  ? 0.29596 0.25480 0.28933 0.06551  -0.02204 -0.02604 20  PHE A CA  
35   C C   . PHE A 13  ? 0.31961 0.27368 0.32780 0.05537  -0.02079 -0.01915 20  PHE A C   
36   O O   . PHE A 13  ? 0.30502 0.26639 0.32041 0.04525  -0.02507 -0.02058 20  PHE A O   
37   C CB  . PHE A 13  ? 0.27703 0.24962 0.26157 0.07720  -0.02166 -0.02496 20  PHE A CB  
38   C CG  . PHE A 13  ? 0.32183 0.31066 0.28828 0.09465  -0.02350 -0.02977 20  PHE A CG  
39   C CD1 . PHE A 13  ? 0.35057 0.37364 0.31771 0.09076  -0.03414 -0.04365 20  PHE A CD1 
40   C CD2 . PHE A 13  ? 0.39000 0.36406 0.33810 0.11552  -0.01300 -0.02161 20  PHE A CD2 
41   C CE1 . PHE A 13  ? 0.34933 0.40133 0.29963 0.10873  -0.03797 -0.05049 20  PHE A CE1 
42   C CE2 . PHE A 13  ? 0.45079 0.44522 0.37776 0.13709  -0.01488 -0.02437 20  PHE A CE2 
43   C CZ  . PHE A 13  ? 0.39014 0.42857 0.31845 0.13441  -0.02925 -0.03939 20  PHE A CZ  
44   N N   . ALA A 14  ? 0.28585 0.23160 0.29820 0.05819  -0.01369 -0.01307 21  ALA A N   
45   C CA  . ALA A 14  ? 0.27790 0.23263 0.30426 0.04935  -0.01341 -0.01020 21  ALA A CA  
46   C C   . ALA A 14  ? 0.27583 0.23415 0.30124 0.04650  -0.00907 -0.01275 21  ALA A C   
47   O O   . ALA A 14  ? 0.31750 0.26257 0.33238 0.05456  0.00135  -0.01281 21  ALA A O   
48   C CB  . ALA A 14  ? 0.32013 0.27474 0.35576 0.05038  -0.00700 -0.00710 21  ALA A CB  
49   N N   . PHE A 15  ? 0.29601 0.26846 0.32895 0.03701  -0.01407 -0.01390 22  PHE A N   
50   C CA  . PHE A 15  ? 0.26526 0.23857 0.29786 0.03155  -0.00664 -0.01790 22  PHE A CA  
51   C C   . PHE A 15  ? 0.24212 0.21241 0.28189 0.02522  0.00657  -0.02287 22  PHE A C   
52   O O   . PHE A 15  ? 0.30044 0.28495 0.35257 0.02189  0.00399  -0.02339 22  PHE A O   
53   C CB  . PHE A 15  ? 0.27207 0.26373 0.31121 0.02167  -0.01447 -0.01932 22  PHE A CB  
54   C CG  . PHE A 15  ? 0.27420 0.26813 0.30790 0.02388  -0.02200 -0.01746 22  PHE A CG  
55   C CD1 . PHE A 15  ? 0.27174 0.26162 0.29618 0.03006  -0.01806 -0.01874 22  PHE A CD1 
56   C CD2 . PHE A 15  ? 0.25909 0.26002 0.29653 0.02072  -0.02979 -0.01441 22  PHE A CD2 
57   C CE1 . PHE A 15  ? 0.24443 0.24638 0.26813 0.03063  -0.02493 -0.01970 22  PHE A CE1 
58   C CE2 . PHE A 15  ? 0.25949 0.26345 0.29490 0.01843  -0.03312 -0.01610 22  PHE A CE2 
59   C CZ  . PHE A 15  ? 0.24489 0.25413 0.27589 0.02205  -0.03230 -0.02013 22  PHE A CZ  
60   N N   . GLN A 16  ? 0.30413 0.25599 0.33590 0.02381  0.02394  -0.02722 23  GLN A N   
61   C CA  . GLN A 16  ? 0.30705 0.25862 0.34901 0.00902  0.04071  -0.03826 23  GLN A CA  
62   C C   . GLN A 16  ? 0.31726 0.30793 0.37720 -0.00784 0.02978  -0.04760 23  GLN A C   
63   O O   . GLN A 16  ? 0.30785 0.31148 0.36554 -0.00846 0.01734  -0.04538 23  GLN A O   
64   C CB  . GLN A 16  ? 0.34615 0.26376 0.37322 0.00777  0.06736  -0.04273 23  GLN A CB  
65   C CG  . GLN A 16  ? 0.47295 0.35251 0.47719 0.02979  0.08372  -0.03186 23  GLN A CG  
66   C CD  . GLN A 16  ? 0.61814 0.46075 0.60058 0.03625  0.11151  -0.03084 23  GLN A CD  
67   O OE1 . GLN A 16  ? 0.60802 0.44861 0.57483 0.05278  0.10683  -0.02180 23  GLN A OE1 
68   N NE2 . GLN A 16  ? 0.62651 0.43936 0.60768 0.02313  0.14389  -0.04091 23  GLN A NE2 
69   N N   . ALA A 17  ? 0.31917 0.33359 0.39683 -0.02036 0.03504  -0.05866 24  ALA A N   
70   C CA  . ALA A 17  ? 0.29424 0.36025 0.38866 -0.03140 0.02219  -0.06747 24  ALA A CA  
71   C C   . ALA A 17  ? 0.31987 0.39283 0.40982 -0.04453 0.02381  -0.07789 24  ALA A C   
72   O O   . ALA A 17  ? 0.33240 0.43849 0.42428 -0.04331 0.00710  -0.07600 24  ALA A O   
73   C CB  . ALA A 17  ? 0.35791 0.45726 0.47431 -0.04502 0.03106  -0.08314 24  ALA A CB  
74   N N   . GLU A 18  ? 0.29440 0.33248 0.37501 -0.05494 0.04679  -0.08766 25  GLU A N   
75   C CA  . GLU A 18  ? 0.34558 0.38614 0.42046 -0.06866 0.05231  -0.09935 25  GLU A CA  
76   C C   . GLU A 18  ? 0.34635 0.37679 0.40631 -0.05292 0.03708  -0.08272 25  GLU A C   
77   O O   . GLU A 18  ? 0.32581 0.37753 0.38485 -0.05992 0.02930  -0.08780 25  GLU A O   
78   C CB  . GLU A 18  ? 0.41173 0.40733 0.47641 -0.08188 0.08765  -0.11273 25  GLU A CB  
79   C CG  . GLU A 18  ? 0.47001 0.47430 0.55160 -0.10551 0.10999  -0.13582 25  GLU A CG  
80   C CD  . GLU A 18  ? 0.60813 0.58687 0.69021 -0.09327 0.11992  -0.12548 25  GLU A CD  
81   O OE1 . GLU A 18  ? 0.53016 0.48962 0.59934 -0.06607 0.10648  -0.10124 25  GLU A OE1 
82   O OE2 . GLU A 18  ? 0.73549 0.71503 0.83113 -0.11265 0.14293  -0.14396 25  GLU A OE2 
83   N N   . ILE A 19  ? 0.27816 0.28063 0.32685 -0.03254 0.03333  -0.06486 26  ILE A N   
84   C CA  . ILE A 19  ? 0.30444 0.30459 0.34341 -0.02042 0.01988  -0.05254 26  ILE A CA  
85   C C   . ILE A 19  ? 0.27720 0.30999 0.32507 -0.01825 -0.00240 -0.04627 26  ILE A C   
86   O O   . ILE A 19  ? 0.27588 0.31923 0.32032 -0.01861 -0.01062 -0.04351 26  ILE A O   
87   C CB  . ILE A 19  ? 0.31626 0.28919 0.34219 -0.00057 0.02233  -0.03986 26  ILE A CB  
88   C CG1 . ILE A 19  ? 0.38277 0.32057 0.39101 0.00632  0.04706  -0.04014 26  ILE A CG1 
89   C CG2 . ILE A 19  ? 0.30314 0.28804 0.32690 0.00812  0.00525  -0.03107 26  ILE A CG2 
90   C CD1 . ILE A 19  ? 0.51172 0.42495 0.51853 -0.00436 0.07398  -0.05069 26  ILE A CD1 
91   N N   . ALA A 20  ? 0.28353 0.32900 0.34045 -0.01376 -0.00912 -0.04239 27  ALA A N   
92   C CA  . ALA A 20  ? 0.32689 0.39868 0.38793 -0.00770 -0.02406 -0.03424 27  ALA A CA  
93   C C   . ALA A 20  ? 0.27365 0.38293 0.33838 -0.01635 -0.02836 -0.04250 27  ALA A C   
94   O O   . ALA A 20  ? 0.29718 0.41851 0.35555 -0.00976 -0.03709 -0.03419 27  ALA A O   
95   C CB  . ALA A 20  ? 0.26384 0.34351 0.33281 0.00041  -0.02618 -0.02907 27  ALA A CB  
96   N N   . GLN A 21  ? 0.24778 0.37604 0.32149 -0.03204 -0.01989 -0.06067 28  GLN A N   
97   C CA  . GLN A 21  ? 0.24431 0.41716 0.32169 -0.04314 -0.02389 -0.07436 28  GLN A CA  
98   C C   . GLN A 21  ? 0.27518 0.43264 0.33853 -0.04736 -0.02246 -0.07506 28  GLN A C   
99   O O   . GLN A 21  ? 0.31398 0.50152 0.37215 -0.04414 -0.03259 -0.07341 28  GLN A O   
100  C CB  . GLN A 21  ? 0.34606 0.54074 0.43801 -0.06547 -0.01046 -0.10017 28  GLN A CB  
101  C CG  . GLN A 21  ? 0.60102 0.84967 0.69795 -0.08210 -0.01316 -0.12202 28  GLN A CG  
102  C CD  . GLN A 21  ? 0.70814 0.98955 0.82411 -0.10634 0.00053  -0.15107 28  GLN A CD  
103  O OE1 . GLN A 21  ? 0.69923 0.94122 0.81944 -0.12197 0.02335  -0.16241 28  GLN A OE1 
104  N NE2 . GLN A 21  ? 0.69933 1.03866 0.81743 -0.10301 -0.00781 -0.15764 28  GLN A NE2 
105  N N   . LEU A 22  ? 0.32256 0.43471 0.37758 -0.05141 -0.00849 -0.07616 29  LEU A N   
106  C CA  . LEU A 22  ? 0.27905 0.37504 0.32084 -0.05239 -0.00562 -0.07478 29  LEU A CA  
107  C C   . LEU A 22  ? 0.30383 0.40275 0.34005 -0.03706 -0.02075 -0.05628 29  LEU A C   
108  O O   . LEU A 22  ? 0.28461 0.39621 0.31359 -0.03794 -0.02486 -0.05573 29  LEU A O   
109  C CB  . LEU A 22  ? 0.31960 0.36783 0.35155 -0.05048 0.01288  -0.07371 29  LEU A CB  
110  C CG  . LEU A 22  ? 0.32581 0.35610 0.34432 -0.04531 0.01649  -0.06806 29  LEU A CG  
111  C CD1 . LEU A 22  ? 0.41011 0.44871 0.42302 -0.06242 0.02607  -0.08471 29  LEU A CD1 
112  C CD2 . LEU A 22  ? 0.40320 0.39431 0.41076 -0.03216 0.03189  -0.06034 29  LEU A CD2 
113  N N   . MET A 23  ? 0.28613 0.37111 0.32460 -0.02432 -0.02617 -0.04255 30  MET A N   
114  C CA  . MET A 23  ? 0.25742 0.33696 0.29105 -0.01384 -0.03384 -0.02819 30  MET A CA  
115  C C   . MET A 23  ? 0.26290 0.37005 0.29353 -0.00764 -0.04157 -0.02154 30  MET A C   
116  O O   . MET A 23  ? 0.28881 0.39484 0.31044 -0.00362 -0.04243 -0.01409 30  MET A O   
117  C CB  . MET A 23  ? 0.22940 0.28913 0.26609 -0.00555 -0.03457 -0.02053 30  MET A CB  
118  C CG  . MET A 23  ? 0.29917 0.33767 0.33359 -0.00462 -0.02783 -0.02381 30  MET A CG  
119  S SD  . MET A 23  ? 0.29788 0.32276 0.33336 0.00482  -0.03042 -0.01865 30  MET A SD  
120  C CE  . MET A 23  ? 0.32801 0.35538 0.36411 0.00299  -0.03487 -0.01366 30  MET A CE  
121  N N   . SER A 24  ? 0.25331 0.38778 0.29016 -0.00419 -0.04558 -0.02321 31  SER A N   
122  C CA  . SER A 24  ? 0.27404 0.44332 0.30465 0.00862  -0.05225 -0.01494 31  SER A CA  
123  C C   . SER A 24  ? 0.32226 0.52318 0.34614 0.00169  -0.05495 -0.02529 31  SER A C   
124  O O   . SER A 24  ? 0.31509 0.53114 0.32502 0.01535  -0.05810 -0.01401 31  SER A O   
125  C CB  . SER A 24  ? 0.36645 0.56823 0.40720 0.01625  -0.05616 -0.01551 31  SER A CB  
126  O OG  . SER A 24  ? 0.67608 0.93004 0.72544 0.00556  -0.06001 -0.03445 31  SER A OG  
127  N N   . LEU A 25  ? 0.24029 0.44788 0.27082 -0.01877 -0.05051 -0.04675 32  LEU A N   
128  C CA  . LEU A 25  ? 0.27611 0.50910 0.29843 -0.02875 -0.05057 -0.06010 32  LEU A CA  
129  C C   . LEU A 25  ? 0.32633 0.52772 0.33373 -0.02411 -0.04763 -0.04849 32  LEU A C   
130  O O   . LEU A 25  ? 0.33935 0.56251 0.33344 -0.01873 -0.05120 -0.04619 32  LEU A O   
131  C CB  . LEU A 25  ? 0.33528 0.56816 0.36617 -0.05463 -0.03895 -0.08729 32  LEU A CB  
132  C CG  . LEU A 25  ? 0.59845 0.85985 0.62376 -0.07374 -0.03413 -0.11165 32  LEU A CG  
133  C CD1 . LEU A 25  ? 0.47440 0.72602 0.51041 -0.10079 -0.01545 -0.13922 32  LEU A CD1 
134  C CD2 . LEU A 25  ? 0.57078 0.80171 0.57846 -0.07281 -0.02915 -0.10576 32  LEU A CD2 
135  N N   . ILE A 26  ? 0.28642 0.44158 0.29576 -0.02521 -0.04068 -0.04192 33  ILE A N   
136  C CA  . ILE A 26  ? 0.32891 0.46000 0.32876 -0.02245 -0.03679 -0.03328 33  ILE A CA  
137  C C   . ILE A 26  ? 0.36802 0.49942 0.35942 -0.00667 -0.04020 -0.01444 33  ILE A C   
138  O O   . ILE A 26  ? 0.35566 0.48469 0.33520 -0.00359 -0.03717 -0.00875 33  ILE A O   
139  C CB  . ILE A 26  ? 0.28260 0.37775 0.28859 -0.02461 -0.02955 -0.03222 33  ILE A CB  
140  C CG1 . ILE A 26  ? 0.31662 0.40123 0.32160 -0.03608 -0.01816 -0.04749 33  ILE A CG1 
141  C CG2 . ILE A 26  ? 0.31246 0.39200 0.31476 -0.01991 -0.02718 -0.02226 33  ILE A CG2 
142  C CD1 . ILE A 26  ? 0.32816 0.38321 0.33579 -0.03109 -0.00978 -0.04464 33  ILE A CD1 
143  N N   . ILE A 27  ? 0.33497 0.46506 0.32990 0.00430  -0.04275 -0.00404 34  ILE A N   
144  C CA  . ILE A 27  ? 0.37980 0.49730 0.36323 0.02024  -0.03824 0.01497  34  ILE A CA  
145  C C   . ILE A 27  ? 0.39247 0.54512 0.35907 0.03692  -0.04146 0.02311  34  ILE A C   
146  O O   . ILE A 27  ? 0.44956 0.59120 0.39830 0.04964  -0.03353 0.03768  34  ILE A O   
147  C CB  . ILE A 27  ? 0.33985 0.43640 0.33003 0.02652  -0.03536 0.02275  34  ILE A CB  
148  C CG1 . ILE A 27  ? 0.33792 0.40332 0.33946 0.01354  -0.03111 0.01626  34  ILE A CG1 
149  C CG2 . ILE A 27  ? 0.41598 0.49824 0.38987 0.04603  -0.02529 0.04287  34  ILE A CG2 
150  C CD1 . ILE A 27  ? 0.41085 0.46286 0.42108 0.01483  -0.03109 0.01607  34  ILE A CD1 
151  N N   . ASN A 28  ? 0.33343 0.53271 0.30465 0.03773  -0.05161 0.01282  35  ASN A N   
152  C CA  . ASN A 28  ? 0.39082 0.63796 0.34672 0.05967  -0.05694 0.02119  35  ASN A CA  
153  C C   . ASN A 28  ? 0.36302 0.65368 0.30944 0.05370  -0.06322 0.00678  35  ASN A C   
154  O O   . ASN A 28  ? 0.44183 0.77229 0.36879 0.07638  -0.06674 0.01657  35  ASN A O   
155  C CB  . ASN A 28  ? 0.47558 0.76298 0.44386 0.06751  -0.06487 0.01791  35  ASN A CB  
156  C CG  . ASN A 28  ? 0.46472 0.71278 0.43523 0.08066  -0.05713 0.03599  35  ASN A CG  
157  O OD1 . ASN A 28  ? 0.62455 0.83266 0.57822 0.09641  -0.04484 0.05695  35  ASN A OD1 
158  N ND2 . ASN A 28  ? 0.55332 0.80886 0.54364 0.07259  -0.06097 0.02649  35  ASN A ND2 
159  N N   . THR A 29  ? 0.35100 0.63533 0.30733 0.02637  -0.06267 -0.01569 36  THR A N   
160  C CA  . THR A 29  ? 0.36053 0.68332 0.30663 0.01734  -0.06598 -0.03312 36  THR A CA  
161  C C   . THR A 29  ? 0.35329 0.65294 0.27622 0.02838  -0.05961 -0.01785 36  THR A C   
162  O O   . THR A 29  ? 0.39263 0.63761 0.31704 0.02384  -0.04962 -0.00839 36  THR A O   
163  C CB  . THR A 29  ? 0.42023 0.73228 0.38079 -0.01518 -0.06043 -0.06158 36  THR A CB  
164  O OG1 . THR A 29  ? 0.38384 0.71475 0.36525 -0.02644 -0.06226 -0.07638 36  THR A OG1 
165  C CG2 . THR A 29  ? 0.45604 0.80444 0.40471 -0.02809 -0.06047 -0.08344 36  THR A CG2 
166  N N   . PHE A 30  ? 0.37597 0.72214 0.27742 0.04356  -0.06479 -0.01640 37  PHE A N   
167  C CA  . PHE A 30  ? 0.43208 0.75719 0.30925 0.05316  -0.05661 -0.00369 37  PHE A CA  
168  C C   . PHE A 30  ? 0.39776 0.70413 0.27944 0.02470  -0.05151 -0.02526 37  PHE A C   
169  O O   . PHE A 30  ? 0.38363 0.72893 0.26659 0.00740  -0.05634 -0.05218 37  PHE A O   
170  C CB  . PHE A 30  ? 0.42570 0.79885 0.28174 0.07853  -0.05963 0.00357  37  PHE A CB  
171  C CG  . PHE A 30  ? 0.37844 0.73218 0.20507 0.08995  -0.05035 0.01673  37  PHE A CG  
172  C CD1 . PHE A 30  ? 0.48399 0.78683 0.29108 0.11001  -0.03524 0.04743  37  PHE A CD1 
173  C CD2 . PHE A 30  ? 0.39013 0.76927 0.21093 0.07828  -0.05214 -0.00247 37  PHE A CD2 
174  C CE1 . PHE A 30  ? 0.42925 0.70864 0.21113 0.11909  -0.02205 0.05952  37  PHE A CE1 
175  C CE2 . PHE A 30  ? 0.48668 0.84568 0.27992 0.08917  -0.04242 0.01006  37  PHE A CE2 
176  C CZ  . PHE A 30  ? 0.45789 0.76839 0.23057 0.11041  -0.02736 0.04179  37  PHE A CZ  
177  N N   . TYR A 31  ? 0.32762 0.57628 0.21153 0.01959  -0.03943 -0.01498 38  TYR A N   
178  C CA  . TYR A 31  ? 0.31580 0.54199 0.20369 -0.00268 -0.03172 -0.03163 38  TYR A CA  
179  C C   . TYR A 31  ? 0.32939 0.51079 0.21215 0.00311  -0.01941 -0.01371 38  TYR A C   
180  O O   . TYR A 31  ? 0.37004 0.51874 0.26744 0.00423  -0.01470 -0.00232 38  TYR A O   
181  C CB  . TYR A 31  ? 0.31585 0.52438 0.22763 -0.02270 -0.02983 -0.04743 38  TYR A CB  
182  C CG  . TYR A 31  ? 0.37411 0.55176 0.28676 -0.03959 -0.01683 -0.06011 38  TYR A CG  
183  C CD1 . TYR A 31  ? 0.48523 0.67931 0.38718 -0.05533 -0.01141 -0.08351 38  TYR A CD1 
184  C CD2 . TYR A 31  ? 0.47218 0.60749 0.39506 -0.03867 -0.00825 -0.04978 38  TYR A CD2 
185  C CE1 . TYR A 31  ? 0.58302 0.74240 0.48176 -0.06773 0.00523  -0.09321 38  TYR A CE1 
186  C CE2 . TYR A 31  ? 0.46799 0.57793 0.38895 -0.04774 0.00548  -0.05825 38  TYR A CE2 
187  C CZ  . TYR A 31  ? 0.51294 0.63013 0.42048 -0.06126 0.01366  -0.07842 38  TYR A CZ  
188  O OH  . TYR A 31  ? 0.68053 0.76598 0.58226 -0.06768 0.03197  -0.08525 38  TYR A OH  
189  N N   . SER A 32  ? 0.33496 0.51859 0.19791 0.00514  -0.01339 -0.01377 39  SER A N   
190  C CA  . SER A 32  ? 0.36053 0.50919 0.21672 0.01295  0.00006  0.00433  39  SER A CA  
191  C C   . SER A 32  ? 0.42901 0.54414 0.30443 -0.00259 0.00939  -0.00112 39  SER A C   
192  O O   . SER A 32  ? 0.41805 0.50743 0.30010 0.00010  0.01985  0.01146  39  SER A O   
193  C CB  . SER A 32  ? 0.38553 0.54978 0.21120 0.02338  0.00443  0.00758  39  SER A CB  
194  O OG  . SER A 32  ? 0.42139 0.61828 0.22499 0.04704  -0.00185 0.01952  39  SER A OG  
195  N N   . ASN A 33  ? 0.38787 0.50425 0.27189 -0.01769 0.00845  -0.01992 40  ASN A N   
196  C CA  . ASN A 33  ? 0.34925 0.43944 0.24396 -0.02567 0.01973  -0.02361 40  ASN A CA  
197  C C   . ASN A 33  ? 0.33060 0.40663 0.25031 -0.02618 0.01828  -0.01957 40  ASN A C   
198  O O   . ASN A 33  ? 0.35935 0.42674 0.28795 -0.03133 0.02112  -0.02845 40  ASN A O   
199  C CB  . ASN A 33  ? 0.41479 0.50558 0.30020 -0.03809 0.02590  -0.04400 40  ASN A CB  
200  C CG  . ASN A 33  ? 0.40437 0.46702 0.29483 -0.04007 0.04129  -0.04509 40  ASN A CG  
201  O OD1 . ASN A 33  ? 0.44002 0.49401 0.33515 -0.03281 0.04710  -0.03288 40  ASN A OD1 
202  N ND2 . ASN A 33  ? 0.42860 0.47748 0.31699 -0.04902 0.05113  -0.06011 40  ASN A ND2 
203  N N   . LYS A 34  ? 0.32431 0.36742 0.29366 -0.00678 -0.02796 -0.00026 41  LYS A N   
204  C CA  . LYS A 34  ? 0.23311 0.29825 0.23270 0.00381  -0.01741 -0.00084 41  LYS A CA  
205  C C   . LYS A 34  ? 0.28465 0.32558 0.28137 0.00448  -0.00585 -0.01231 41  LYS A C   
206  O O   . LYS A 34  ? 0.28105 0.33381 0.29530 0.00835  -0.00166 -0.01396 41  LYS A O   
207  C CB  . LYS A 34  ? 0.28914 0.35872 0.29574 0.02438  -0.01277 0.00205  41  LYS A CB  
208  C CG  . LYS A 34  ? 0.27633 0.38166 0.29184 0.03492  -0.02095 0.01617  41  LYS A CG  
209  C CD  . LYS A 34  ? 0.31624 0.40404 0.32236 0.06129  -0.01901 0.01567  41  LYS A CD  
210  C CE  . LYS A 34  ? 0.30224 0.42753 0.31381 0.08176  -0.02469 0.03108  41  LYS A CE  
211  N NZ  . LYS A 34  ? 0.27937 0.45700 0.30937 0.10522  -0.01846 0.04223  41  LYS A NZ  
212  N N   . GLU A 35  ? 0.32284 0.33522 0.29630 0.00489  0.00040  -0.01732 42  GLU A N   
213  C CA  . GLU A 35  ? 0.32580 0.32812 0.30295 0.01014  0.01337  -0.02137 42  GLU A CA  
214  C C   . GLU A 35  ? 0.34171 0.33759 0.31820 0.00459  0.01125  -0.02842 42  GLU A C   
215  O O   . GLU A 35  ? 0.34585 0.34067 0.33297 0.00948  0.02045  -0.03039 42  GLU A O   
216  C CB  . GLU A 35  ? 0.32096 0.30833 0.27106 0.01990  0.02428  -0.01837 42  GLU A CB  
217  C CG  . GLU A 35  ? 0.37346 0.32557 0.27353 0.02395  0.01900  -0.02771 42  GLU A CG  
218  C CD  . GLU A 35  ? 0.57641 0.51344 0.43528 0.04666  0.03342  -0.02390 42  GLU A CD  
219  O OE1 . GLU A 35  ? 0.54207 0.49926 0.40885 0.05038  0.04078  -0.01128 42  GLU A OE1 
220  O OE2 . GLU A 35  ? 0.67647 0.57968 0.48933 0.06460  0.03742  -0.03179 42  GLU A OE2 
221  N N   . ILE A 36  ? 0.31497 0.30741 0.28045 -0.00880 -0.00416 -0.02799 43  ILE A N   
222  C CA  . ILE A 36  ? 0.32866 0.31014 0.29092 -0.01854 -0.01053 -0.03048 43  ILE A CA  
223  C C   . ILE A 36  ? 0.27058 0.28645 0.27075 -0.01679 -0.00355 -0.02675 43  ILE A C   
224  O O   . ILE A 36  ? 0.27087 0.28005 0.27159 -0.02266 -0.00529 -0.02786 43  ILE A O   
225  C CB  . ILE A 36  ? 0.38193 0.34914 0.32297 -0.04214 -0.03742 -0.02294 43  ILE A CB  
226  C CG1 . ILE A 36  ? 0.39143 0.41561 0.36931 -0.05332 -0.04631 -0.00363 43  ILE A CG1 
227  C CG2 . ILE A 36  ? 0.40024 0.30997 0.28140 -0.03933 -0.04890 -0.03146 43  ILE A CG2 
228  C CD1 . ILE A 36  ? 0.36416 0.43815 0.38068 -0.06223 -0.04728 0.01315  43  ILE A CD1 
229  N N   . PHE A 37  ? 0.22198 0.26585 0.24410 -0.00524 0.00261  -0.02286 44  PHE A N   
230  C CA  . PHE A 37  ? 0.23941 0.30167 0.27919 0.00528  0.00841  -0.02225 44  PHE A CA  
231  C C   . PHE A 37  ? 0.27908 0.31716 0.31733 0.00667  0.01434  -0.03137 44  PHE A C   
232  O O   . PHE A 37  ? 0.25203 0.29645 0.29637 0.00759  0.01544  -0.03162 44  PHE A O   
233  C CB  . PHE A 37  ? 0.27823 0.34708 0.31931 0.02590  0.01041  -0.02128 44  PHE A CB  
234  C CG  . PHE A 37  ? 0.27775 0.31060 0.31079 0.02981  0.01015  -0.02818 44  PHE A CG  
235  C CD1 . PHE A 37  ? 0.25843 0.27992 0.28657 0.02460  0.00920  -0.02498 44  PHE A CD1 
236  C CD2 . PHE A 37  ? 0.29016 0.30245 0.32051 0.03527  0.00758  -0.03300 44  PHE A CD2 
237  C CE1 . PHE A 37  ? 0.31302 0.31298 0.34162 0.02195  0.00641  -0.02097 44  PHE A CE1 
238  C CE2 . PHE A 37  ? 0.27622 0.25969 0.30475 0.02955  -0.00028 -0.03060 44  PHE A CE2 
239  C CZ  . PHE A 37  ? 0.25587 0.23790 0.28744 0.02146  -0.00055 -0.02183 44  PHE A CZ  
240  N N   . LEU A 38  ? 0.25675 0.27492 0.28925 0.00798  0.01871  -0.03426 45  LEU A N   
241  C CA  . LEU A 38  ? 0.25251 0.26239 0.29293 0.01017  0.02341  -0.03515 45  LEU A CA  
242  C C   . LEU A 38  ? 0.28270 0.28254 0.31309 0.00803  0.02581  -0.03911 45  LEU A C   
243  O O   . LEU A 38  ? 0.25949 0.25939 0.29887 0.00866  0.02622  -0.04013 45  LEU A O   
244  C CB  . LEU A 38  ? 0.26328 0.27357 0.30897 0.01230  0.02835  -0.02598 45  LEU A CB  
245  C CG  . LEU A 38  ? 0.29359 0.31117 0.35898 0.01137  0.02989  -0.01664 45  LEU A CG  
246  C CD1 . LEU A 38  ? 0.26008 0.26537 0.33324 0.00554  0.01425  -0.01800 45  LEU A CD1 
247  C CD2 . LEU A 38  ? 0.28358 0.32143 0.36224 0.01169  0.03635  0.00408  45  LEU A CD2 
248  N N   . ARG A 39  ? 0.28360 0.26470 0.28679 0.00623  0.02331  -0.04169 46  ARG A N   
249  C CA  . ARG A 39  ? 0.27599 0.22747 0.25372 0.00421  0.01766  -0.04635 46  ARG A CA  
250  C C   . ARG A 39  ? 0.29830 0.26208 0.29145 -0.01103 0.00825  -0.04253 46  ARG A C   
251  O O   . ARG A 39  ? 0.33498 0.28564 0.32456 -0.01060 0.00766  -0.04399 46  ARG A O   
252  C CB  . ARG A 39  ? 0.36501 0.27637 0.29554 0.00147  0.00530  -0.05009 46  ARG A CB  
253  C CG  . ARG A 39  ? 0.48308 0.34072 0.37018 -0.00429 -0.01190 -0.05482 46  ARG A CG  
254  C CD  . ARG A 39  ? 0.57121 0.37357 0.39952 -0.01134 -0.03490 -0.05835 46  ARG A CD  
255  N NE  . ARG A 39  ? 0.57224 0.39895 0.42217 -0.04526 -0.05711 -0.04473 46  ARG A NE  
256  C CZ  . ARG A 39  ? 0.66171 0.45888 0.47678 -0.05940 -0.08104 -0.04185 46  ARG A CZ  
257  N NH1 . ARG A 39  ? 0.68030 0.41230 0.42644 -0.03925 -0.08537 -0.05598 46  ARG A NH1 
258  N NH2 . ARG A 39  ? 0.63264 0.47019 0.48059 -0.09164 -0.10129 -0.02133 46  ARG A NH2 
259  N N   . GLU A 40  ? 0.26152 0.25685 0.27211 -0.02142 0.00226  -0.03374 47  GLU A N   
260  C CA  . GLU A 40  ? 0.26054 0.28342 0.28750 -0.03274 -0.00351 -0.02157 47  GLU A CA  
261  C C   . GLU A 40  ? 0.24455 0.28097 0.28650 -0.01808 0.00825  -0.02511 47  GLU A C   
262  O O   . GLU A 40  ? 0.25700 0.29689 0.30089 -0.02384 0.00607  -0.01956 47  GLU A O   
263  C CB  . GLU A 40  ? 0.23672 0.30782 0.28290 -0.03897 -0.00836 -0.00406 47  GLU A CB  
264  C CG  . GLU A 40  ? 0.29909 0.35843 0.33099 -0.06107 -0.02849 0.00475  47  GLU A CG  
265  C CD  . GLU A 40  ? 0.46212 0.47164 0.46316 -0.08580 -0.05128 0.00690  47  GLU A CD  
266  O OE1 . GLU A 40  ? 0.40931 0.42831 0.42036 -0.09691 -0.05540 0.01781  47  GLU A OE1 
267  O OE2 . GLU A 40  ? 0.52284 0.47569 0.48094 -0.09190 -0.06720 -0.00221 47  GLU A OE2 
268  N N   . LEU A 41  ? 0.22078 0.25830 0.26808 -0.00132 0.01613  -0.03255 48  LEU A N   
269  C CA  . LEU A 41  ? 0.25862 0.29431 0.30816 0.01098  0.01889  -0.03638 48  LEU A CA  
270  C C   . LEU A 41  ? 0.26623 0.27955 0.31612 0.00750  0.01878  -0.04103 48  LEU A C   
271  O O   . LEU A 41  ? 0.27704 0.28899 0.32650 0.01012  0.01745  -0.04105 48  LEU A O   
272  C CB  . LEU A 41  ? 0.25678 0.28220 0.30081 0.02542  0.01672  -0.04098 48  LEU A CB  
273  C CG  . LEU A 41  ? 0.25435 0.29933 0.29103 0.04111  0.01799  -0.03663 48  LEU A CG  
274  C CD1 . LEU A 41  ? 0.29060 0.30182 0.30901 0.05468  0.00949  -0.04313 48  LEU A CD1 
275  C CD2 . LEU A 41  ? 0.25987 0.33636 0.29130 0.05780  0.02401  -0.02830 48  LEU A CD2 
276  N N   . ILE A 42  ? 0.24682 0.24658 0.29523 0.00628  0.02154  -0.04250 49  ILE A N   
277  C CA  . ILE A 42  ? 0.25394 0.24284 0.30321 0.01063  0.02454  -0.04195 49  ILE A CA  
278  C C   . ILE A 42  ? 0.28546 0.25628 0.31718 0.00617  0.02069  -0.04360 49  ILE A C   
279  O O   . ILE A 42  ? 0.27773 0.24272 0.31130 0.00982  0.02028  -0.04274 49  ILE A O   
280  C CB  . ILE A 42  ? 0.25391 0.24267 0.30100 0.02039  0.03322  -0.03774 49  ILE A CB  
281  C CG1 . ILE A 42  ? 0.21946 0.22914 0.29141 0.01801  0.03225  -0.02760 49  ILE A CG1 
282  C CG2 . ILE A 42  ? 0.28287 0.26497 0.32300 0.03531  0.04014  -0.03426 49  ILE A CG2 
283  C CD1 . ILE A 42  ? 0.29658 0.32129 0.37047 0.02686  0.04331  -0.01586 49  ILE A CD1 
284  N N   . SER A 43  ? 0.26989 0.22903 0.28349 -0.00528 0.01304  -0.04273 50  SER A N   
285  C CA  . SER A 43  ? 0.29831 0.23143 0.29145 -0.01754 0.00067  -0.03906 50  SER A CA  
286  C C   . SER A 43  ? 0.33296 0.29591 0.34654 -0.02577 -0.00026 -0.02924 50  SER A C   
287  O O   . SER A 43  ? 0.31700 0.26245 0.32175 -0.02917 -0.00543 -0.02631 50  SER A O   
288  C CB  . SER A 43  ? 0.39883 0.30980 0.36726 -0.03623 -0.01675 -0.03418 50  SER A CB  
289  O OG  . SER A 43  ? 0.48880 0.37764 0.44190 -0.05904 -0.03722 -0.02250 50  SER A OG  
290  N N   . ASN A 44  ? 0.24632 0.25228 0.28079 -0.02343 0.00563  -0.02331 51  ASN A N   
291  C CA  . ASN A 44  ? 0.26350 0.29968 0.30742 -0.01924 0.00942  -0.01381 51  ASN A CA  
292  C C   . ASN A 44  ? 0.23454 0.25155 0.27468 -0.00611 0.01236  -0.02429 51  ASN A C   
293  O O   . ASN A 44  ? 0.23447 0.25253 0.27083 -0.00784 0.01061  -0.01806 51  ASN A O   
294  C CB  . ASN A 44  ? 0.22090 0.29794 0.27330 -0.00423 0.01755  -0.00834 51  ASN A CB  
295  C CG  . ASN A 44  ? 0.32212 0.43995 0.38796 -0.01826 0.01386  0.01283  51  ASN A CG  
296  O OD1 . ASN A 44  ? 0.29952 0.40981 0.36614 -0.04624 -0.00048 0.02525  51  ASN A OD1 
297  N ND2 . ASN A 44  ? 0.29401 0.45073 0.36636 0.00118  0.02263  0.01922  51  ASN A ND2 
298  N N   . SER A 45  ? 0.23325 0.23642 0.27645 0.00416  0.01404  -0.03552 52  SER A N   
299  C CA  . SER A 45  ? 0.27131 0.26112 0.31663 0.01071  0.01053  -0.03912 52  SER A CA  
300  C C   . SER A 45  ? 0.26526 0.23968 0.30856 0.00777  0.00974  -0.03680 52  SER A C   
301  O O   . SER A 45  ? 0.25125 0.22150 0.29300 0.00996  0.00568  -0.03461 52  SER A O   
302  C CB  . SER A 45  ? 0.24230 0.22782 0.29894 0.01354  0.00739  -0.04107 52  SER A CB  
303  O OG  . SER A 45  ? 0.28397 0.26576 0.33073 0.01894  0.00179  -0.04453 52  SER A OG  
304  N N   . SER A 46  ? 0.26712 0.22511 0.30111 0.00686  0.01183  -0.03790 53  SER A N   
305  C CA  . SER A 46  ? 0.27213 0.20038 0.28803 0.01247  0.00922  -0.03737 53  SER A CA  
306  C C   . SER A 46  ? 0.29962 0.21507 0.30224 -0.00189 -0.00095 -0.03104 53  SER A C   
307  O O   . SER A 46  ? 0.30704 0.20638 0.30243 0.00324  -0.00448 -0.02876 53  SER A O   
308  C CB  . SER A 46  ? 0.31003 0.20580 0.29676 0.02099  0.01002  -0.04216 53  SER A CB  
309  O OG  . SER A 46  ? 0.38231 0.23304 0.33441 0.03423  0.00489  -0.04362 53  SER A OG  
310  N N   . ASP A 47  ? 0.29134 0.22104 0.29409 -0.02054 -0.00630 -0.02274 54  ASP A N   
311  C CA  . ASP A 47  ? 0.29286 0.22650 0.29112 -0.03828 -0.01604 -0.00635 54  ASP A CA  
312  C C   . ASP A 47  ? 0.34062 0.30167 0.35064 -0.02786 -0.00830 -0.00316 54  ASP A C   
313  O O   . ASP A 47  ? 0.32225 0.27282 0.32340 -0.03398 -0.01470 0.00648  54  ASP A O   
314  C CB  . ASP A 47  ? 0.27577 0.24334 0.28415 -0.06043 -0.02214 0.01269  54  ASP A CB  
315  C CG  . ASP A 47  ? 0.50663 0.43386 0.49278 -0.07885 -0.04056 0.01334  54  ASP A CG  
316  O OD1 . ASP A 47  ? 0.48454 0.34372 0.43266 -0.07588 -0.05277 0.00231  54  ASP A OD1 
317  O OD2 . ASP A 47  ? 0.44195 0.40232 0.44234 -0.09455 -0.04554 0.02712  54  ASP A OD2 
318  N N   . ALA A 48  ? 0.26658 0.25331 0.28781 -0.01172 0.00167  -0.01096 55  ALA A N   
319  C CA  . ALA A 48  ? 0.26365 0.26012 0.27935 0.00167  0.00360  -0.01088 55  ALA A CA  
320  C C   . ALA A 48  ? 0.27455 0.24286 0.28889 0.00643  -0.00322 -0.01770 55  ALA A C   
321  O O   . ALA A 48  ? 0.27721 0.24300 0.28149 0.00999  -0.00707 -0.01312 55  ALA A O   
322  C CB  . ALA A 48  ? 0.26092 0.26847 0.27129 0.01964  0.00765  -0.01959 55  ALA A CB  
323  N N   . LEU A 49  ? 0.27995 0.23421 0.30500 0.00922  -0.00376 -0.02471 56  LEU A N   
324  C CA  . LEU A 49  ? 0.26538 0.20839 0.29676 0.01719  -0.00831 -0.02351 56  LEU A CA  
325  C C   . LEU A 49  ? 0.30060 0.21739 0.31419 0.01661  -0.01143 -0.01845 56  LEU A C   
326  O O   . LEU A 49  ? 0.31833 0.22902 0.33067 0.02254  -0.01694 -0.01388 56  LEU A O   
327  C CB  . LEU A 49  ? 0.28474 0.23632 0.33513 0.02545  -0.00367 -0.02380 56  LEU A CB  
328  C CG  . LEU A 49  ? 0.27316 0.24294 0.34181 0.02138  -0.00937 -0.02311 56  LEU A CG  
329  C CD1 . LEU A 49  ? 0.26647 0.25254 0.35337 0.02463  -0.00138 -0.01867 56  LEU A CD1 
330  C CD2 . LEU A 49  ? 0.27133 0.24523 0.35160 0.01931  -0.02571 -0.01454 56  LEU A CD2 
331  N N   . ASP A 50  ? 0.32876 0.22207 0.32314 0.00782  -0.01309 -0.01787 57  ASP A N   
332  C CA  . ASP A 50  ? 0.35655 0.20696 0.32162 0.00253  -0.02478 -0.01147 57  ASP A CA  
333  C C   . ASP A 50  ? 0.36769 0.23206 0.33386 -0.01074 -0.03025 0.00197  57  ASP A C   
334  O O   . ASP A 50  ? 0.37143 0.20788 0.32155 -0.00803 -0.03877 0.00744  57  ASP A O   
335  C CB  . ASP A 50  ? 0.37045 0.18336 0.30711 -0.01406 -0.03648 -0.00956 57  ASP A CB  
336  C CG  . ASP A 50  ? 0.52432 0.30394 0.43854 0.00644  -0.03314 -0.02343 57  ASP A CG  
337  O OD1 . ASP A 50  ? 0.48094 0.27283 0.40504 0.03576  -0.01925 -0.02945 57  ASP A OD1 
338  O OD2 . ASP A 50  ? 0.51603 0.25932 0.40070 -0.00678 -0.04609 -0.02434 57  ASP A OD2 
339  N N   . LYS A 51  ? 0.32476 0.23314 0.30521 -0.02023 -0.02416 0.00943  58  LYS A N   
340  C CA  . LYS A 51  ? 0.30331 0.23392 0.27983 -0.02758 -0.02526 0.02729  58  LYS A CA  
341  C C   . LYS A 51  ? 0.35026 0.27761 0.32240 -0.00983 -0.02505 0.02108  58  LYS A C   
342  O O   . LYS A 51  ? 0.38633 0.30285 0.34575 -0.01365 -0.03169 0.03294  58  LYS A O   
343  C CB  . LYS A 51  ? 0.31738 0.30404 0.30467 -0.02902 -0.01392 0.03958  58  LYS A CB  
344  C CG  . LYS A 51  ? 0.41956 0.42330 0.41775 -0.05222 -0.01804 0.05529  58  LYS A CG  
345  C CD  . LYS A 51  ? 0.43499 0.50677 0.44830 -0.04227 -0.00219 0.06845  58  LYS A CD  
346  C CE  . LYS A 51  ? 0.57733 0.68715 0.61022 -0.07167 -0.00967 0.09949  58  LYS A CE  
347  N NZ  . LYS A 51  ? 0.81291 0.87175 0.84089 -0.09179 -0.02726 0.08664  58  LYS A NZ  
348  N N   . ILE A 52  ? 0.30719 0.24112 0.28788 0.00613  -0.02208 0.00572  59  ILE A N   
349  C CA  . ILE A 52  ? 0.33094 0.25743 0.30516 0.01732  -0.03025 0.00322  59  ILE A CA  
350  C C   . ILE A 52  ? 0.39779 0.30160 0.37922 0.02020  -0.03779 0.00531  59  ILE A C   
351  O O   . ILE A 52  ? 0.39799 0.29369 0.37104 0.02434  -0.04651 0.01126  59  ILE A O   
352  C CB  . ILE A 52  ? 0.30937 0.23884 0.28537 0.02677  -0.03556 -0.00867 59  ILE A CB  
353  C CG1 . ILE A 52  ? 0.40854 0.32245 0.36760 0.03335  -0.05277 -0.00834 59  ILE A CG1 
354  C CG2 . ILE A 52  ? 0.30048 0.23223 0.30600 0.02449  -0.03596 -0.01353 59  ILE A CG2 
355  C CD1 . ILE A 52  ? 0.41721 0.32973 0.33803 0.04216  -0.05059 -0.00250 59  ILE A CD1 
356  N N   . ARG A 53  ? 0.35312 0.24532 0.34382 0.02351  -0.03396 0.00161  60  ARG A N   
357  C CA  . ARG A 53  ? 0.36577 0.23503 0.35271 0.03814  -0.03781 0.00536  60  ARG A CA  
358  C C   . ARG A 53  ? 0.40548 0.23727 0.36138 0.03135  -0.04693 0.01385  60  ARG A C   
359  O O   . ARG A 53  ? 0.43864 0.25867 0.38865 0.04170  -0.05420 0.02032  60  ARG A O   
360  C CB  . ARG A 53  ? 0.37503 0.23230 0.36075 0.05284  -0.02955 -0.00013 60  ARG A CB  
361  C CG  . ARG A 53  ? 0.46367 0.29501 0.43360 0.08106  -0.03070 0.00491  60  ARG A CG  
362  C CD  . ARG A 53  ? 0.67804 0.48748 0.62712 0.10783  -0.02084 -0.00035 60  ARG A CD  
363  N NE  . ARG A 53  ? 0.75413 0.62289 0.74416 0.12905  -0.00630 0.00852  60  ARG A NE  
364  C CZ  . ARG A 53  ? 0.74363 0.62945 0.73949 0.13680  0.00647  0.00582  60  ARG A CZ  
365  N NH1 . ARG A 53  ? 0.70305 0.54638 0.66354 0.12667  0.00543  -0.00915 60  ARG A NH1 
366  N NH2 . ARG A 53  ? 0.55218 0.50308 0.59217 0.15265  0.01828  0.02317  60  ARG A NH2 
367  N N   . TYR A 54  ? 0.40136 0.21608 0.33887 0.01063  -0.05009 0.01855  61  TYR A N   
368  C CA  . TYR A 54  ? 0.46601 0.24213 0.37405 -0.00423 -0.06504 0.03365  61  TYR A CA  
369  C C   . TYR A 54  ? 0.43074 0.23328 0.34269 -0.00812 -0.06581 0.04654  61  TYR A C   
370  O O   . TYR A 54  ? 0.49537 0.26624 0.38760 -0.00674 -0.07742 0.05606  61  TYR A O   
371  C CB  . TYR A 54  ? 0.49499 0.26108 0.39158 -0.03534 -0.07404 0.04610  61  TYR A CB  
372  C CG  . TYR A 54  ? 0.56427 0.27809 0.42693 -0.05760 -0.09827 0.06681  61  TYR A CG  
373  C CD1 . TYR A 54  ? 0.61932 0.24439 0.43421 -0.04759 -0.11801 0.05942  61  TYR A CD1 
374  C CD2 . TYR A 54  ? 0.56526 0.31533 0.43727 -0.08449 -0.10236 0.09639  61  TYR A CD2 
375  C CE1 . TYR A 54  ? 0.66473 0.22530 0.43898 -0.07011 -0.14739 0.07907  61  TYR A CE1 
376  C CE2 . TYR A 54  ? 0.58188 0.28428 0.42481 -0.11079 -0.12870 0.12158  61  TYR A CE2 
377  C CZ  . TYR A 54  ? 0.74788 0.34887 0.54045 -0.10634 -0.15422 0.11183  61  TYR A CZ  
378  O OH  . TYR A 54  ? 0.80712 0.36849 0.57106 -0.12934 -0.18144 0.12936  61  TYR A OH  
379  N N   . GLU A 55  ? 0.41210 0.26575 0.34017 -0.00867 -0.05454 0.04673  62  GLU A N   
380  C CA  . GLU A 55  ? 0.40650 0.27990 0.32437 -0.00529 -0.05471 0.05761  62  GLU A CA  
381  C C   . GLU A 55  ? 0.48853 0.34433 0.40501 0.01241  -0.06375 0.04955  62  GLU A C   
382  O O   . GLU A 55  ? 0.51707 0.36329 0.41657 0.01322  -0.07158 0.06113  62  GLU A O   
383  C CB  . GLU A 55  ? 0.45604 0.37428 0.37431 0.00279  -0.04146 0.05540  62  GLU A CB  
384  C CG  . GLU A 55  ? 0.46172 0.42014 0.38138 -0.01163 -0.03128 0.07922  62  GLU A CG  
385  C CD  . GLU A 55  ? 0.77430 0.77853 0.68045 0.01094  -0.01490 0.08156  62  GLU A CD  
386  O OE1 . GLU A 55  ? 0.70648 0.76304 0.61853 0.00630  -0.00225 0.10781  62  GLU A OE1 
387  O OE2 . GLU A 55  ? 0.62601 0.61238 0.51169 0.03492  -0.01710 0.05999  62  GLU A OE2 
388  N N   . SER A 56  ? 0.44561 0.30311 0.38322 0.02511  -0.06407 0.03504  63  SER A N   
389  C CA  . SER A 56  ? 0.43569 0.29235 0.38355 0.03895  -0.07528 0.03567  63  SER A CA  
390  C C   . SER A 56  ? 0.47960 0.30648 0.41987 0.04973  -0.08093 0.04426  63  SER A C   
391  O O   . SER A 56  ? 0.48907 0.32057 0.43695 0.06203  -0.09102 0.05129  63  SER A O   
392  C CB  . SER A 56  ? 0.46121 0.34184 0.44220 0.04544  -0.07525 0.02866  63  SER A CB  
393  O OG  . SER A 56  ? 0.47354 0.35114 0.46823 0.05622  -0.06508 0.02778  63  SER A OG  
394  N N   . LEU A 57  ? 0.48038 0.27037 0.39992 0.04647  -0.07880 0.04506  64  LEU A N   
395  C CA  . LEU A 57  ? 0.55226 0.29402 0.44700 0.06345  -0.08791 0.05086  64  LEU A CA  
396  C C   . LEU A 57  ? 0.64874 0.37334 0.52316 0.05616  -0.10110 0.06554  64  LEU A C   
397  O O   . LEU A 57  ? 0.71036 0.40957 0.57285 0.07733  -0.10976 0.07138  64  LEU A O   
398  C CB  . LEU A 57  ? 0.58960 0.27256 0.44802 0.05896  -0.09211 0.04719  64  LEU A CB  
399  C CG  . LEU A 57  ? 0.56109 0.24743 0.42624 0.07454  -0.07994 0.03260  64  LEU A CG  
400  C CD1 . LEU A 57  ? 0.64198 0.24754 0.45159 0.07168  -0.09311 0.02846  64  LEU A CD1 
401  C CD2 . LEU A 57  ? 0.67151 0.38668 0.55897 0.11524  -0.06891 0.03168  64  LEU A CD2 
402  N N   . THR A 58  ? 0.56144 0.30389 0.43009 0.03087  -0.10116 0.07461  65  THR A N   
403  C CA  . THR A 58  ? 0.60882 0.34238 0.45649 0.02372  -0.11141 0.09231  65  THR A CA  
404  C C   . THR A 58  ? 0.75950 0.53554 0.61409 0.02922  -0.10906 0.09154  65  THR A C   
405  O O   . THR A 58  ? 0.66501 0.43450 0.49944 0.02967  -0.11789 0.10480  65  THR A O   
406  C CB  . THR A 58  ? 0.75499 0.47790 0.58231 -0.00767 -0.11528 0.11391  65  THR A CB  
407  O OG1 . THR A 58  ? 0.71758 0.49469 0.56262 -0.01984 -0.09930 0.11495  65  THR A OG1 
408  C CG2 . THR A 58  ? 0.77666 0.43205 0.57985 -0.01775 -0.13064 0.11607  65  THR A CG2 
409  N N   . ASP A 59  ? 0.61969 0.41359 0.47505 0.11825  -0.04554 0.13622  66  ASP A N   
410  C CA  . ASP A 59  ? 0.66254 0.49440 0.51178 0.11690  -0.05667 0.13648  66  ASP A CA  
411  C C   . ASP A 59  ? 0.53536 0.40627 0.41327 0.11959  -0.06555 0.12064  66  ASP A C   
412  O O   . ASP A 59  ? 0.49644 0.38236 0.38500 0.10506  -0.06227 0.10402  66  ASP A O   
413  C CB  . ASP A 59  ? 0.59674 0.43054 0.42854 0.09658  -0.04912 0.13278  66  ASP A CB  
414  C CG  . ASP A 59  ? 0.70462 0.57090 0.52277 0.09601  -0.05969 0.13116  66  ASP A CG  
415  O OD1 . ASP A 59  ? 0.77044 0.65814 0.59233 0.10896  -0.07511 0.13383  66  ASP A OD1 
416  O OD2 . ASP A 59  ? 0.69130 0.56209 0.49437 0.08267  -0.05264 0.12704  66  ASP A OD2 
417  N N   . PRO A 60  ? 0.66354 0.55284 0.55607 0.13820  -0.07676 0.12675  67  PRO A N   
418  C CA  . PRO A 60  ? 0.58785 0.51680 0.51097 0.13885  -0.08463 0.11363  67  PRO A CA  
419  C C   . PRO A 60  ? 0.53102 0.48998 0.45062 0.12365  -0.09387 0.10285  67  PRO A C   
420  O O   . PRO A 60  ? 0.49854 0.48053 0.44061 0.11608  -0.09569 0.08849  67  PRO A O   
421  C CB  . PRO A 60  ? 0.56791 0.51523 0.50532 0.16222  -0.09619 0.12731  67  PRO A CB  
422  C CG  . PRO A 60  ? 0.63956 0.54674 0.55712 0.17689  -0.09036 0.14500  67  PRO A CG  
423  C CD  . PRO A 60  ? 0.63198 0.50323 0.51804 0.16018  -0.08000 0.14638  67  PRO A CD  
424  N N   . SER A 61  ? 0.58577 0.54243 0.47522 0.11926  -0.09908 0.10929  68  SER A N   
425  C CA  . SER A 61  ? 0.53051 0.51001 0.41106 0.10631  -0.10748 0.09722  68  SER A CA  
426  C C   . SER A 61  ? 0.54848 0.52260 0.43449 0.08975  -0.09504 0.07957  68  SER A C   
427  O O   . SER A 61  ? 0.48012 0.47107 0.36503 0.08008  -0.10083 0.06636  68  SER A O   
428  C CB  . SER A 61  ? 0.59331 0.56667 0.43396 0.10626  -0.11238 0.10727  68  SER A CB  
429  O OG  . SER A 61  ? 0.59374 0.53770 0.41307 0.09931  -0.09494 0.11149  68  SER A OG  
430  N N   . LYS A 62  ? 0.46408 0.41400 0.35527 0.08633  -0.07907 0.07902  69  LYS A N   
431  C CA  . LYS A 62  ? 0.39938 0.34828 0.29908 0.07212  -0.06888 0.06363  69  LYS A CA  
432  C C   . LYS A 62  ? 0.40727 0.37765 0.33532 0.07004  -0.07392 0.05018  69  LYS A C   
433  O O   . LYS A 62  ? 0.40178 0.37632 0.33509 0.05915  -0.06940 0.03723  69  LYS A O   
434  C CB  . LYS A 62  ? 0.46700 0.38764 0.36776 0.06786  -0.05372 0.06645  69  LYS A CB  
435  C CG  . LYS A 62  ? 0.63993 0.53860 0.51393 0.06547  -0.04660 0.08056  69  LYS A CG  
436  C CD  . LYS A 62  ? 0.58118 0.47388 0.45238 0.04948  -0.03329 0.07512  69  LYS A CD  
437  C CE  . LYS A 62  ? 0.62373 0.50243 0.46855 0.04519  -0.02541 0.09018  69  LYS A CE  
438  N NZ  . LYS A 62  ? 0.85432 0.73794 0.70058 0.02981  -0.01241 0.08536  69  LYS A NZ  
439  N N   . LEU A 63  ? 0.39502 0.38022 0.34237 0.08083  -0.08238 0.05436  70  LEU A N   
440  C CA  . LEU A 63  ? 0.37655 0.38595 0.35209 0.07811  -0.08681 0.04436  70  LEU A CA  
441  C C   . LEU A 63  ? 0.41415 0.45241 0.39228 0.07462  -0.10414 0.04186  70  LEU A C   
442  O O   . LEU A 63  ? 0.42158 0.48365 0.42584 0.07206  -0.10997 0.03699  70  LEU A O   
443  C CB  . LEU A 63  ? 0.42249 0.43497 0.42182 0.09164  -0.08322 0.04992  70  LEU A CB  
444  C CG  . LEU A 63  ? 0.40190 0.38291 0.39850 0.09395  -0.06723 0.04889  70  LEU A CG  
445  C CD1 . LEU A 63  ? 0.40080 0.38416 0.41704 0.11073  -0.06349 0.05331  70  LEU A CD1 
446  C CD2 . LEU A 63  ? 0.38521 0.36190 0.38430 0.07840  -0.05905 0.03457  70  LEU A CD2 
447  N N   . ASP A 64  ? 0.39365 0.43005 0.34393 0.07325  -0.11258 0.04509  71  ASP A N   
448  C CA  . ASP A 64  ? 0.44467 0.50465 0.39205 0.06725  -0.13087 0.04000  71  ASP A CA  
449  C C   . ASP A 64  ? 0.45282 0.51521 0.40653 0.05172  -0.13001 0.02230  71  ASP A C   
450  O O   . ASP A 64  ? 0.43157 0.51407 0.39528 0.04393  -0.14456 0.01609  71  ASP A O   
451  C CB  . ASP A 64  ? 0.43064 0.48288 0.33869 0.06875  -0.13833 0.04519  71  ASP A CB  
452  C CG  . ASP A 64  ? 0.67927 0.73604 0.58188 0.08451  -0.14636 0.06466  71  ASP A CG  
453  O OD1 . ASP A 64  ? 0.62245 0.69274 0.55477 0.09524  -0.14847 0.07296  71  ASP A OD1 
454  O OD2 . ASP A 64  ? 0.60600 0.65244 0.47338 0.08763  -0.14967 0.07250  71  ASP A OD2 
455  N N   . SER A 65  ? 0.45310 0.49495 0.40173 0.04671  -0.11387 0.01487  72  SER A N   
456  C CA  . SER A 65  ? 0.35053 0.38994 0.30475 0.03487  -0.11066 -0.00012 72  SER A CA  
457  C C   . SER A 65  ? 0.45722 0.50745 0.44609 0.03247  -0.10700 -0.00224 72  SER A C   
458  O O   . SER A 65  ? 0.45792 0.50265 0.45234 0.02389  -0.10190 -0.01229 72  SER A O   
459  C CB  . SER A 65  ? 0.41087 0.42825 0.34669 0.03274  -0.09509 -0.00492 72  SER A CB  
460  O OG  . SER A 65  ? 0.39587 0.40251 0.33582 0.03860  -0.08271 0.00447  72  SER A OG  
461  N N   . GLY A 66  ? 0.40736 0.47218 0.41813 0.04141  -0.10834 0.00773  73  GLY A N   
462  C CA  . GLY A 66  ? 0.42085 0.49742 0.46226 0.04093  -0.10245 0.00671  73  GLY A CA  
463  C C   . GLY A 66  ? 0.44415 0.51691 0.49611 0.05547  -0.09242 0.01606  73  GLY A C   
464  O O   . GLY A 66  ? 0.35037 0.39740 0.38744 0.05889  -0.08112 0.01664  73  GLY A O   
465  N N   . LYS A 67  ? 0.31707 0.41533 0.39502 0.06406  -0.09641 0.02339  74  LYS A N   
466  C CA  . LYS A 67  ? 0.33007 0.42304 0.41692 0.08140  -0.08639 0.03170  74  LYS A CA  
467  C C   . LYS A 67  ? 0.35964 0.44431 0.45686 0.08064  -0.07086 0.02516  74  LYS A C   
468  O O   . LYS A 67  ? 0.40079 0.46451 0.49226 0.09208  -0.05947 0.02714  74  LYS A O   
469  C CB  . LYS A 67  ? 0.31576 0.44365 0.42820 0.09423  -0.09581 0.04307  74  LYS A CB  
470  C CG  . LYS A 67  ? 0.47939 0.61634 0.57985 0.09859  -0.11265 0.05211  74  LYS A CG  
471  C CD  . LYS A 67  ? 0.59882 0.72877 0.69776 0.12208  -0.11041 0.06680  74  LYS A CD  
472  C CE  . LYS A 67  ? 0.74961 0.89014 0.83466 0.12723  -0.12845 0.07786  74  LYS A CE  
473  N NZ  . LYS A 67  ? 0.77076 0.87109 0.81516 0.12654  -0.12465 0.08013  74  LYS A NZ  
474  N N   . GLU A 68  ? 0.27136 0.36914 0.38080 0.06724  -0.07055 0.01748  75  GLU A N   
475  C CA  . GLU A 68  ? 0.30200 0.39782 0.42185 0.06715  -0.05698 0.01317  75  GLU A CA  
476  C C   . GLU A 68  ? 0.28274 0.34410 0.37885 0.06184  -0.04757 0.00509  75  GLU A C   
477  O O   . GLU A 68  ? 0.35367 0.40353 0.43462 0.05079  -0.05158 -0.00009 75  GLU A O   
478  C CB  . GLU A 68  ? 0.34121 0.46244 0.48175 0.05371  -0.06038 0.01036  75  GLU A CB  
479  C CG  . GLU A 68  ? 0.44489 0.60641 0.61879 0.05946  -0.06349 0.01929  75  GLU A CG  
480  C CD  . GLU A 68  ? 0.93526 1.12228 1.12006 0.04970  -0.08278 0.02225  75  GLU A CD  
481  O OE1 . GLU A 68  ? 1.08110 1.30559 1.29725 0.04504  -0.08764 0.02774  75  GLU A OE1 
482  O OE2 . GLU A 68  ? 0.80531 0.97581 0.96663 0.04589  -0.09313 0.01913  75  GLU A OE2 
483  N N   . LEU A 69  ? 0.27047 0.31659 0.36332 0.07007  -0.03523 0.00375  76  LEU A N   
484  C CA  . LEU A 69  ? 0.28767 0.30376 0.36001 0.06425  -0.02770 -0.00363 76  LEU A CA  
485  C C   . LEU A 69  ? 0.24947 0.27022 0.32796 0.06110  -0.01925 -0.00919 76  LEU A C   
486  O O   . LEU A 69  ? 0.27854 0.29881 0.36064 0.07223  -0.01018 -0.00864 76  LEU A O   
487  C CB  . LEU A 69  ? 0.32000 0.30737 0.37664 0.07482  -0.02220 -0.00123 76  LEU A CB  
488  C CG  . LEU A 69  ? 0.37065 0.34871 0.41691 0.07848  -0.02906 0.00680  76  LEU A CG  
489  C CD1 . LEU A 69  ? 0.45901 0.40042 0.48721 0.08574  -0.02216 0.00894  76  LEU A CD1 
490  C CD2 . LEU A 69  ? 0.34928 0.32837 0.38539 0.06391  -0.03552 0.00457  76  LEU A CD2 
491  N N   . HIS A 70  ? 0.26365 0.28752 0.34115 0.04763  -0.02140 -0.01408 77  HIS A N   
492  C CA  . HIS A 70  ? 0.23843 0.26904 0.32130 0.04448  -0.01436 -0.01675 77  HIS A CA  
493  C C   . HIS A 70  ? 0.21670 0.23695 0.28866 0.03221  -0.01606 -0.02229 77  HIS A C   
494  O O   . HIS A 70  ? 0.24404 0.25704 0.30857 0.02630  -0.02230 -0.02419 77  HIS A O   
495  C CB  . HIS A 70  ? 0.21507 0.27674 0.32279 0.04342  -0.01575 -0.01108 77  HIS A CB  
496  C CG  . HIS A 70  ? 0.30896 0.38137 0.42409 0.03150  -0.02792 -0.01053 77  HIS A CG  
497  N ND1 . HIS A 70  ? 0.36561 0.46036 0.49739 0.03192  -0.03718 -0.00516 77  HIS A ND1 
498  C CD2 . HIS A 70  ? 0.31167 0.37407 0.41815 0.01948  -0.03276 -0.01535 77  HIS A CD2 
499  C CE1 . HIS A 70  ? 0.26602 0.36100 0.39604 0.01902  -0.04769 -0.00820 77  HIS A CE1 
500  N NE2 . HIS A 70  ? 0.30594 0.37996 0.42047 0.01245  -0.04421 -0.01446 77  HIS A NE2 
501  N N   . ILE A 71  ? 0.20599 0.22734 0.27685 0.03004  -0.00970 -0.02389 78  ILE A N   
502  C CA  . ILE A 71  ? 0.18830 0.20270 0.25062 0.02097  -0.01094 -0.02712 78  ILE A CA  
503  C C   . ILE A 71  ? 0.25256 0.28148 0.32649 0.01638  -0.00875 -0.02294 78  ILE A C   
504  O O   . ILE A 71  ? 0.23026 0.26955 0.31004 0.02103  -0.00054 -0.01961 78  ILE A O   
505  C CB  . ILE A 71  ? 0.23320 0.23083 0.27704 0.02201  -0.00625 -0.03211 78  ILE A CB  
506  C CG1 . ILE A 71  ? 0.27704 0.25764 0.31013 0.02408  -0.00771 -0.03528 78  ILE A CG1 
507  C CG2 . ILE A 71  ? 0.25213 0.24762 0.28962 0.01420  -0.00919 -0.03344 78  ILE A CG2 
508  C CD1 . ILE A 71  ? 0.29103 0.25283 0.30542 0.02380  -0.00403 -0.04132 78  ILE A CD1 
509  N N   . ASN A 72  ? 0.22946 0.25748 0.30561 0.00769  -0.01486 -0.02270 79  ASN A N   
510  C CA  . ASN A 72  ? 0.20573 0.24117 0.29067 0.00078  -0.01332 -0.01775 79  ASN A CA  
511  C C   . ASN A 72  ? 0.25969 0.28077 0.33078 -0.00222 -0.01316 -0.01854 79  ASN A C   
512  O O   . ASN A 72  ? 0.27770 0.28752 0.33983 -0.00200 -0.01828 -0.02298 79  ASN A O   
513  C CB  . ASN A 72  ? 0.22461 0.26702 0.32346 -0.00757 -0.02188 -0.01629 79  ASN A CB  
514  C CG  . ASN A 72  ? 0.22937 0.29236 0.34526 -0.00497 -0.02425 -0.01341 79  ASN A CG  
515  O OD1 . ASN A 72  ? 0.25106 0.32805 0.37518 0.00282  -0.01633 -0.00947 79  ASN A OD1 
516  N ND2 . ASN A 72  ? 0.28445 0.34981 0.40470 -0.01035 -0.03542 -0.01533 79  ASN A ND2 
517  N N   . LEU A 73  ? 0.22934 0.25309 0.29914 -0.00405 -0.00679 -0.01291 80  LEU A N   
518  C CA  . LEU A 73  ? 0.22191 0.23368 0.27908 -0.00602 -0.00732 -0.01066 80  LEU A CA  
519  C C   . LEU A 73  ? 0.26575 0.27580 0.33207 -0.01472 -0.00797 -0.00325 80  LEU A C   
520  O O   . LEU A 73  ? 0.22744 0.25003 0.30432 -0.01903 -0.00153 0.00387  80  LEU A O   
521  C CB  . LEU A 73  ? 0.20959 0.22185 0.25155 -0.00136 0.00020  -0.00908 80  LEU A CB  
522  C CG  . LEU A 73  ? 0.22969 0.23930 0.26077 0.00532  0.00141  -0.01718 80  LEU A CG  
523  C CD1 . LEU A 73  ? 0.23387 0.24015 0.24451 0.00892  0.00781  -0.01746 80  LEU A CD1 
524  C CD2 . LEU A 73  ? 0.27220 0.27304 0.29923 0.00462  -0.00757 -0.02333 80  LEU A CD2 
525  N N   . ILE A 74  ? 0.25890 0.25294 0.32152 -0.01730 -0.01490 -0.00456 81  ILE A N   
526  C CA  . ILE A 74  ? 0.24652 0.23062 0.31572 -0.02693 -0.01726 0.00067  81  ILE A CA  
527  C C   . ILE A 74  ? 0.25269 0.21697 0.30802 -0.02454 -0.01738 0.00583  81  ILE A C   
528  O O   . ILE A 74  ? 0.29862 0.24834 0.34611 -0.01874 -0.02273 0.00099  81  ILE A O   
529  C CB  . ILE A 74  ? 0.23744 0.21453 0.31252 -0.03158 -0.02634 -0.00690 81  ILE A CB  
530  C CG1 . ILE A 74  ? 0.27333 0.27093 0.35905 -0.03028 -0.02786 -0.01128 81  ILE A CG1 
531  C CG2 . ILE A 74  ? 0.24750 0.21305 0.32990 -0.04524 -0.02961 -0.00240 81  ILE A CG2 
532  C CD1 . ILE A 74  ? 0.34055 0.33312 0.42733 -0.03394 -0.03789 -0.01891 81  ILE A CD1 
533  N N   . PRO A 75  ? 0.28764 0.25168 0.33962 -0.02779 -0.01091 0.01698  82  PRO A N   
534  C CA  . PRO A 75  ? 0.29859 0.24128 0.33729 -0.02547 -0.01197 0.02466  82  PRO A CA  
535  C C   . PRO A 75  ? 0.31989 0.23974 0.36381 -0.03577 -0.01511 0.02850  82  PRO A C   
536  O O   . PRO A 75  ? 0.34363 0.26964 0.40217 -0.04913 -0.01392 0.03074  82  PRO A O   
537  C CB  . PRO A 75  ? 0.34207 0.29441 0.37171 -0.02520 -0.00297 0.03592  82  PRO A CB  
538  C CG  . PRO A 75  ? 0.30269 0.27707 0.34795 -0.03277 0.00470  0.03707  82  PRO A CG  
539  C CD  . PRO A 75  ? 0.32651 0.31060 0.38561 -0.03202 -0.00112 0.02428  82  PRO A CD  
540  N N   . ASN A 76  ? 0.35386 0.24684 0.38615 -0.02941 -0.01958 0.02925  83  ASN A N   
541  C CA  . ASN A 76  ? 0.36498 0.22576 0.39613 -0.03795 -0.02262 0.03247  83  ASN A CA  
542  C C   . ASN A 76  ? 0.46312 0.29938 0.47826 -0.02920 -0.02143 0.04418  83  ASN A C   
543  O O   . ASN A 76  ? 0.41140 0.23822 0.41734 -0.01338 -0.02513 0.04044  83  ASN A O   
544  C CB  . ASN A 76  ? 0.43379 0.27852 0.46455 -0.03634 -0.03045 0.01756  83  ASN A CB  
545  C CG  . ASN A 76  ? 0.47973 0.28809 0.50778 -0.04889 -0.03462 0.01782  83  ASN A CG  
546  O OD1 . ASN A 76  ? 0.49066 0.26860 0.50812 -0.04765 -0.03320 0.02722  83  ASN A OD1 
547  N ND2 . ASN A 76  ? 0.52405 0.33331 0.56001 -0.06138 -0.04079 0.00765  83  ASN A ND2 
548  N N   . LYS A 77  ? 0.44769 0.27498 0.46045 -0.03900 -0.01597 0.05976  84  LYS A N   
549  C CA  . LYS A 77  ? 0.53692 0.34153 0.53222 -0.02988 -0.01475 0.07406  84  LYS A CA  
550  C C   . LYS A 77  ? 0.55150 0.31046 0.53869 -0.02614 -0.02009 0.07331  84  LYS A C   
551  O O   . LYS A 77  ? 0.56853 0.30926 0.54170 -0.01004 -0.02171 0.08072  84  LYS A O   
552  C CB  . LYS A 77  ? 0.51464 0.32265 0.50710 -0.04171 -0.00569 0.09275  84  LYS A CB  
553  C CG  . LYS A 77  ? 0.55748 0.40466 0.54804 -0.03840 0.00124  0.09497  84  LYS A CG  
554  C CD  . LYS A 77  ? 0.54667 0.39519 0.52809 -0.04633 0.01207  0.11521  84  LYS A CD  
555  C CE  . LYS A 77  ? 0.54400 0.42823 0.51845 -0.04126 0.02006  0.11505  84  LYS A CE  
556  N NZ  . LYS A 77  ? 0.70751 0.62090 0.70346 -0.04688 0.02322  0.10173  84  LYS A NZ  
557  N N   . GLN A 78  ? 0.53436 0.27355 0.52882 -0.03983 -0.02349 0.06420  85  GLN A N   
558  C CA  . GLN A 78  ? 0.62463 0.31355 0.60687 -0.03607 -0.02823 0.06082  85  GLN A CA  
559  C C   . GLN A 78  ? 0.58322 0.26961 0.55837 -0.01256 -0.03210 0.04718  85  GLN A C   
560  O O   . GLN A 78  ? 0.67463 0.32869 0.63610 0.00387  -0.03283 0.05053  85  GLN A O   
561  C CB  . GLN A 78  ? 0.70748 0.37590 0.69667 -0.05906 -0.03263 0.05234  85  GLN A CB  
562  C CG  . GLN A 78  ? 0.81888 0.47760 0.81505 -0.08370 -0.02889 0.06865  85  GLN A CG  
563  C CD  . GLN A 78  ? 1.12914 0.84133 1.14604 -0.09550 -0.02254 0.07537  85  GLN A CD  
564  O OE1 . GLN A 78  ? 1.02933 0.77228 1.06296 -0.10285 -0.02574 0.06362  85  GLN A OE1 
565  N NE2 . GLN A 78  ? 0.93864 0.66160 0.95266 -0.09565 -0.01298 0.09478  85  GLN A NE2 
566  N N   . ASP A 79  ? 0.56551 0.28590 0.55038 -0.00994 -0.03374 0.03295  86  ASP A N   
567  C CA  . ASP A 79  ? 0.57603 0.30262 0.55730 0.01067  -0.03545 0.02129  86  ASP A CA  
568  C C   . ASP A 79  ? 0.50979 0.26835 0.49333 0.02689  -0.03378 0.02892  86  ASP A C   
569  O O   . ASP A 79  ? 0.48428 0.25052 0.46752 0.04494  -0.03462 0.02321  86  ASP A O   
570  C CB  . ASP A 79  ? 0.53340 0.28100 0.52251 0.00458  -0.03791 0.00426  86  ASP A CB  
571  C CG  . ASP A 79  ? 0.74553 0.46364 0.73046 -0.01121 -0.04263 -0.00563 86  ASP A CG  
572  O OD1 . ASP A 79  ? 0.71982 0.39475 0.69400 -0.01571 -0.04385 -0.00192 86  ASP A OD1 
573  O OD2 . ASP A 79  ? 0.68359 0.42045 0.67491 -0.01982 -0.04608 -0.01675 86  ASP A OD2 
574  N N   . ARG A 80  ? 0.48701 0.26509 0.47228 0.02023  -0.03144 0.04158  87  ARG A N   
575  C CA  . ARG A 80  ? 0.39851 0.20922 0.38362 0.03082  -0.03179 0.04734  87  ARG A CA  
576  C C   . ARG A 80  ? 0.38474 0.22804 0.38011 0.03457  -0.03345 0.03316  87  ARG A C   
577  O O   . ARG A 80  ? 0.39686 0.25646 0.39414 0.04878  -0.03619 0.03181  87  ARG A O   
578  C CB  . ARG A 80  ? 0.45192 0.24947 0.42735 0.04990  -0.03446 0.05875  87  ARG A CB  
579  C CG  . ARG A 80  ? 0.46364 0.29350 0.43586 0.05643  -0.03710 0.06773  87  ARG A CG  
580  C CD  . ARG A 80  ? 0.60847 0.44416 0.58024 0.07842  -0.04284 0.07303  87  ARG A CD  
581  N NE  . ARG A 80  ? 0.66416 0.46467 0.62391 0.08934  -0.04326 0.08819  87  ARG A NE  
582  C CZ  . ARG A 80  ? 0.77403 0.56819 0.73468 0.11193  -0.04689 0.09312  87  ARG A CZ  
583  N NH1 . ARG A 80  ? 0.58268 0.40800 0.55802 0.12501  -0.04997 0.08467  87  ARG A NH1 
584  N NH2 . ARG A 80  ? 0.68925 0.44565 0.63674 0.12212  -0.04679 0.10816  87  ARG A NH2 
585  N N   . THR A 81  ? 0.36384 0.21792 0.36721 0.02110  -0.03191 0.02386  88  THR A N   
586  C CA  . THR A 81  ? 0.30875 0.18950 0.32021 0.02250  -0.03279 0.01194  88  THR A CA  
587  C C   . THR A 81  ? 0.36399 0.26804 0.38034 0.01137  -0.03003 0.01189  88  THR A C   
588  O O   . THR A 81  ? 0.34090 0.24128 0.35936 -0.00007 -0.02674 0.01692  88  THR A O   
589  C CB  . THR A 81  ? 0.35768 0.22699 0.37167 0.02105  -0.03407 -0.00110 88  THR A CB  
590  O OG1 . THR A 81  ? 0.37610 0.23201 0.39214 0.00525  -0.03446 -0.00201 88  THR A OG1 
591  C CG2 . THR A 81  ? 0.38692 0.23177 0.39334 0.03537  -0.03481 -0.00339 88  THR A CG2 
592  N N   . LEU A 82  ? 0.28053 0.20839 0.29929 0.01502  -0.03078 0.00644  89  LEU A N   
593  C CA  . LEU A 82  ? 0.26007 0.20630 0.28232 0.00763  -0.02786 0.00286  89  LEU A CA  
594  C C   . LEU A 82  ? 0.30595 0.26059 0.33529 0.00818  -0.02953 -0.00831 89  LEU A C   
595  O O   . LEU A 82  ? 0.28426 0.24553 0.31375 0.01513  -0.03193 -0.01194 89  LEU A O   
596  C CB  . LEU A 82  ? 0.31947 0.28005 0.33259 0.01020  -0.02744 0.00649  89  LEU A CB  
597  C CG  . LEU A 82  ? 0.28322 0.25762 0.29580 0.00549  -0.02345 0.00121  89  LEU A CG  
598  C CD1 . LEU A 82  ? 0.29251 0.26643 0.30939 -0.00140 -0.01615 0.00560  89  LEU A CD1 
599  C CD2 . LEU A 82  ? 0.31775 0.30045 0.31554 0.00806  -0.02487 0.00219  89  LEU A CD2 
600  N N   . THR A 83  ? 0.25295 0.20937 0.28898 0.00089  -0.02831 -0.01229 90  THR A N   
601  C CA  . THR A 83  ? 0.23617 0.19827 0.27610 0.00143  -0.03022 -0.02110 90  THR A CA  
602  C C   . THR A 83  ? 0.27313 0.25060 0.31634 -0.00082 -0.02760 -0.02260 90  THR A C   
603  O O   . THR A 83  ? 0.28209 0.26499 0.32977 -0.00511 -0.02421 -0.01890 90  THR A O   
604  C CB  . THR A 83  ? 0.28715 0.23733 0.32972 -0.00377 -0.03344 -0.02504 90  THR A CB  
605  O OG1 . THR A 83  ? 0.35750 0.28625 0.39323 -0.00021 -0.03518 -0.02508 90  THR A OG1 
606  C CG2 . THR A 83  ? 0.27682 0.23300 0.31895 -0.00207 -0.03566 -0.03303 90  THR A CG2 
607  N N   . ILE A 84  ? 0.25197 0.23585 0.29320 0.00254  -0.02821 -0.02729 91  ILE A N   
608  C CA  . ILE A 84  ? 0.23363 0.22509 0.27530 0.00176  -0.02594 -0.02945 91  ILE A CA  
609  C C   . ILE A 84  ? 0.30073 0.29261 0.34567 0.00179  -0.02815 -0.03327 91  ILE A C   
610  O O   . ILE A 84  ? 0.27320 0.26383 0.31499 0.00387  -0.02958 -0.03605 91  ILE A O   
611  C CB  . ILE A 84  ? 0.24968 0.24399 0.28404 0.00296  -0.02574 -0.03104 91  ILE A CB  
612  C CG1 . ILE A 84  ? 0.30757 0.30210 0.33413 0.00314  -0.02518 -0.02732 91  ILE A CG1 
613  C CG2 . ILE A 84  ? 0.27734 0.27114 0.30928 0.00254  -0.02324 -0.03419 91  ILE A CG2 
614  C CD1 . ILE A 84  ? 0.35855 0.35323 0.38474 0.00594  -0.02920 -0.02345 91  ILE A CD1 
615  N N   . VAL A 85  ? 0.23091 0.22716 0.28229 0.00012  -0.02823 -0.03240 92  VAL A N   
616  C CA  . VAL A 85  ? 0.20193 0.19993 0.25478 0.00030  -0.03220 -0.03463 92  VAL A CA  
617  C C   . VAL A 85  ? 0.26232 0.26491 0.31573 0.00418  -0.02970 -0.03336 92  VAL A C   
618  O O   . VAL A 85  ? 0.27064 0.27825 0.32897 0.00619  -0.02542 -0.03081 92  VAL A O   
619  C CB  . VAL A 85  ? 0.25505 0.25640 0.31643 -0.00505 -0.03720 -0.03377 92  VAL A CB  
620  C CG1 . VAL A 85  ? 0.34394 0.34644 0.40193 -0.00496 -0.04388 -0.03685 92  VAL A CG1 
621  C CG2 . VAL A 85  ? 0.32084 0.31073 0.38029 -0.00962 -0.03880 -0.03435 92  VAL A CG2 
622  N N   . ASP A 86  ? 0.26219 0.26151 0.30920 0.00625  -0.03132 -0.03454 93  ASP A N   
623  C CA  . ASP A 86  ? 0.23195 0.23074 0.27808 0.01082  -0.02982 -0.03203 93  ASP A CA  
624  C C   . ASP A 86  ? 0.28782 0.28840 0.33070 0.01233  -0.03529 -0.03052 93  ASP A C   
625  O O   . ASP A 86  ? 0.27261 0.27171 0.30893 0.00969  -0.03866 -0.03323 93  ASP A O   
626  C CB  . ASP A 86  ? 0.29201 0.27966 0.32888 0.01096  -0.02528 -0.03300 93  ASP A CB  
627  C CG  . ASP A 86  ? 0.31811 0.30267 0.34812 0.00735  -0.02595 -0.03368 93  ASP A CG  
628  O OD1 . ASP A 86  ? 0.33202 0.31527 0.35727 0.00872  -0.02726 -0.03125 93  ASP A OD1 
629  O OD2 . ASP A 86  ? 0.29459 0.28025 0.32411 0.00361  -0.02481 -0.03561 93  ASP A OD2 
630  N N   . THR A 87  ? 0.26586 0.26890 0.31133 0.01820  -0.03598 -0.02599 94  THR A N   
631  C CA  . THR A 87  ? 0.24074 0.24567 0.28043 0.02106  -0.04207 -0.02253 94  THR A CA  
632  C C   . THR A 87  ? 0.25789 0.24803 0.28475 0.02469  -0.03791 -0.01861 94  THR A C   
633  O O   . THR A 87  ? 0.28718 0.27568 0.31072 0.03139  -0.04041 -0.01213 94  THR A O   
634  C CB  . THR A 87  ? 0.27619 0.29780 0.32989 0.02580  -0.04795 -0.01771 94  THR A CB  
635  O OG1 . THR A 87  ? 0.27789 0.30104 0.34141 0.03354  -0.04099 -0.01447 94  THR A OG1 
636  C CG2 . THR A 87  ? 0.27291 0.30861 0.33845 0.01766  -0.05408 -0.02086 94  THR A CG2 
637  N N   . GLY A 88  ? 0.25983 0.23949 0.28014 0.01965  -0.03209 -0.02138 95  GLY A N   
638  C CA  . GLY A 88  ? 0.29623 0.26079 0.30570 0.01873  -0.02783 -0.01741 95  GLY A CA  
639  C C   . GLY A 88  ? 0.28442 0.24951 0.28208 0.01726  -0.02879 -0.01340 95  GLY A C   
640  O O   . GLY A 88  ? 0.30030 0.27499 0.29464 0.01934  -0.03421 -0.01408 95  GLY A O   
641  N N   . ILE A 89  ? 0.28854 0.24247 0.27817 0.01253  -0.02325 -0.00920 96  ILE A N   
642  C CA  . ILE A 89  ? 0.30170 0.25539 0.27777 0.01157  -0.02140 -0.00278 96  ILE A CA  
643  C C   . ILE A 89  ? 0.34572 0.31439 0.31977 0.00958  -0.02008 -0.00799 96  ILE A C   
644  O O   . ILE A 89  ? 0.34044 0.31169 0.29988 0.01189  -0.01944 -0.00490 96  ILE A O   
645  C CB  . ILE A 89  ? 0.32500 0.26331 0.29541 0.00440  -0.01451 0.00451  96  ILE A CB  
646  C CG1 . ILE A 89  ? 0.38026 0.31597 0.33400 0.00481  -0.01148 0.01492  96  ILE A CG1 
647  C CG2 . ILE A 89  ? 0.33361 0.27876 0.31420 -0.00649 -0.00991 -0.00018 96  ILE A CG2 
648  C CD1 . ILE A 89  ? 0.37980 0.29293 0.32568 -0.00054 -0.00651 0.02572  96  ILE A CD1 
649  N N   . GLY A 90  ? 0.33389 0.31083 0.31961 0.00698  -0.01935 -0.01566 97  GLY A N   
650  C CA  . GLY A 90  ? 0.30385 0.29149 0.28739 0.00791  -0.01688 -0.02059 97  GLY A CA  
651  C C   . GLY A 90  ? 0.30067 0.29538 0.28292 0.00389  -0.00745 -0.01584 97  GLY A C   
652  O O   . GLY A 90  ? 0.32221 0.31273 0.30645 -0.00287 -0.00370 -0.00874 97  GLY A O   
653  N N   . MET A 91  ? 0.28797 0.29331 0.26727 0.00809  -0.00303 -0.01976 98  MET A N   
654  C CA  . MET A 91  ? 0.30340 0.32352 0.28659 0.00591  0.00763  -0.01509 98  MET A CA  
655  C C   . MET A 91  ? 0.30622 0.33007 0.27042 0.01436  0.01398  -0.01651 98  MET A C   
656  O O   . MET A 91  ? 0.30064 0.31780 0.25412 0.02219  0.00964  -0.02573 98  MET A O   
657  C CB  . MET A 91  ? 0.33057 0.36551 0.33437 0.00533  0.00883  -0.01864 98  MET A CB  
658  C CG  . MET A 91  ? 0.32833 0.36449 0.34798 -0.00579 0.00556  -0.01538 98  MET A CG  
659  S SD  . MET A 91  ? 0.34046 0.39414 0.38106 -0.00529 0.00261  -0.01937 98  MET A SD  
660  C CE  . MET A 91  ? 0.31310 0.35289 0.34630 0.00589  -0.00377 -0.02830 98  MET A CE  
661  N N   . THR A 92  ? 0.31456 0.34732 0.27261 0.01195  0.02457  -0.00745 99  THR A N   
662  C CA  . THR A 92  ? 0.31030 0.35003 0.24927 0.02120  0.03422  -0.00881 99  THR A CA  
663  C C   . THR A 92  ? 0.34349 0.40195 0.29697 0.02867  0.04245  -0.01423 99  THR A C   
664  O O   . THR A 92  ? 0.32609 0.39689 0.30618 0.02452  0.04109  -0.01349 99  THR A O   
665  C CB  . THR A 92  ? 0.37264 0.41874 0.30085 0.01631  0.04547  0.00486  99  THR A CB  
666  O OG1 . THR A 92  ? 0.36241 0.42845 0.31696 0.00625  0.05389  0.01353  99  THR A OG1 
667  C CG2 . THR A 92  ? 0.38221 0.40774 0.29606 0.01089  0.03742  0.01261  99  THR A CG2 
668  N N   . LYS A 93  ? 0.36238 0.38369 0.28255 0.08005  -0.04847 0.01495  100 LYS A N   
669  C CA  . LYS A 93  ? 0.32790 0.33995 0.25036 0.06511  -0.02985 0.00662  100 LYS A CA  
670  C C   . LYS A 93  ? 0.35063 0.33614 0.27104 0.06293  -0.01626 0.02074  100 LYS A C   
671  O O   . LYS A 93  ? 0.33840 0.32054 0.27992 0.05678  -0.00455 0.01562  100 LYS A O   
672  C CB  . LYS A 93  ? 0.34933 0.37064 0.24318 0.05723  -0.02692 -0.00223 100 LYS A CB  
673  C CG  . LYS A 93  ? 0.38931 0.40216 0.28895 0.04593  -0.00710 -0.01426 100 LYS A CG  
674  C CD  . LYS A 93  ? 0.38577 0.40499 0.25458 0.03822  -0.00151 -0.02551 100 LYS A CD  
675  C CE  . LYS A 93  ? 0.50077 0.50977 0.37938 0.03132  0.01878  -0.04022 100 LYS A CE  
676  N NZ  . LYS A 93  ? 0.50823 0.51763 0.35563 0.02540  0.03074  -0.04803 100 LYS A NZ  
677  N N   . ALA A 94  ? 0.38869 0.35576 0.28249 0.06739  -0.01761 0.03872  101 ALA A N   
678  C CA  . ALA A 94  ? 0.41435 0.35677 0.30574 0.06041  -0.00304 0.05031  101 ALA A CA  
679  C C   . ALA A 94  ? 0.42890 0.36461 0.35283 0.06144  -0.00231 0.04874  101 ALA A C   
680  O O   . ALA A 94  ? 0.39749 0.33236 0.33703 0.05121  0.01030  0.04574  101 ALA A O   
681  C CB  . ALA A 94  ? 0.43991 0.35506 0.29199 0.06386  -0.00380 0.07137  101 ALA A CB  
682  N N   . ASP A 95  ? 0.38779 0.32344 0.32274 0.07418  -0.01585 0.04920  102 ASP A N   
683  C CA  . ASP A 95  ? 0.40401 0.33536 0.36792 0.07460  -0.01427 0.04444  102 ASP A CA  
684  C C   . ASP A 95  ? 0.38270 0.33607 0.37282 0.06621  -0.00893 0.02938  102 ASP A C   
685  O O   . ASP A 95  ? 0.34272 0.29316 0.34798 0.05926  -0.00108 0.02720  102 ASP A O   
686  C CB  . ASP A 95  ? 0.38978 0.32296 0.36313 0.09188  -0.02845 0.04442  102 ASP A CB  
687  C CG  . ASP A 95  ? 0.68965 0.59456 0.63533 0.10642  -0.03499 0.06264  102 ASP A CG  
688  O OD1 . ASP A 95  ? 0.78123 0.70035 0.72589 0.12537  -0.05114 0.06418  102 ASP A OD1 
689  O OD2 . ASP A 95  ? 0.70555 0.57460 0.63044 0.09909  -0.02370 0.07553  102 ASP A OD2 
690  N N   . LEU A 96  ? 0.33434 0.30844 0.32784 0.06634  -0.01301 0.01880  103 LEU A N   
691  C CA  . LEU A 96  ? 0.34927 0.33404 0.36140 0.05961  -0.00623 0.00737  103 LEU A CA  
692  C C   . LEU A 96  ? 0.37748 0.35753 0.38943 0.05337  0.00656  0.01001  103 LEU A C   
693  O O   . LEU A 96  ? 0.32076 0.30376 0.34917 0.05149  0.01097  0.00835  103 LEU A O   
694  C CB  . LEU A 96  ? 0.40142 0.40010 0.41071 0.05682  -0.00847 -0.00498 103 LEU A CB  
695  C CG  . LEU A 96  ? 0.39609 0.41328 0.41944 0.05781  -0.01790 -0.01570 103 LEU A CG  
696  C CD1 . LEU A 96  ? 0.33428 0.36278 0.35072 0.04876  -0.01666 -0.03036 103 LEU A CD1 
697  C CD2 . LEU A 96  ? 0.25735 0.27449 0.30334 0.05526  -0.01327 -0.01946 103 LEU A CD2 
698  N N   . ILE A 97  ? 0.32378 0.30125 0.31699 0.05071  0.01247  0.01349  104 ILE A N   
699  C CA  . ILE A 97  ? 0.33216 0.31415 0.32964 0.04604  0.02566  0.01342  104 ILE A CA  
700  C C   . ILE A 97  ? 0.37124 0.35163 0.37942 0.04063  0.02922  0.02006  104 ILE A C   
701  O O   . ILE A 97  ? 0.34446 0.33953 0.37082 0.03858  0.03512  0.01686  104 ILE A O   
702  C CB  . ILE A 97  ? 0.36361 0.34563 0.33717 0.04277  0.03342  0.01383  104 ILE A CB  
703  C CG1 . ILE A 97  ? 0.33850 0.32413 0.30341 0.04513  0.03223  0.00154  104 ILE A CG1 
704  C CG2 . ILE A 97  ? 0.32054 0.31369 0.30261 0.03788  0.04872  0.01338  104 ILE A CG2 
705  C CD1 . ILE A 97  ? 0.38040 0.36677 0.31459 0.04126  0.03730  -0.00024 104 ILE A CD1 
706  N N   . ASN A 98  ? 0.32624 0.28866 0.32272 0.03867  0.02552  0.02868  105 ASN A N   
707  C CA  . ASN A 98  ? 0.33354 0.28699 0.33667 0.02954  0.03083  0.03245  105 ASN A CA  
708  C C   . ASN A 98  ? 0.31170 0.26730 0.33534 0.03252  0.02389  0.02641  105 ASN A C   
709  O O   . ASN A 98  ? 0.32272 0.25821 0.34405 0.03350  0.02070  0.02872  105 ASN A O   
710  C CB  . ASN A 98  ? 0.44411 0.36590 0.42015 0.02673  0.03272  0.04520  105 ASN A CB  
711  C CG  . ASN A 98  ? 0.64854 0.55458 0.62665 0.01097  0.04387  0.04746  105 ASN A CG  
712  O OD1 . ASN A 98  ? 0.55332 0.48244 0.55464 0.00035  0.04975  0.03786  105 ASN A OD1 
713  N ND2 . ASN A 98  ? 0.57859 0.44450 0.53091 0.00923  0.04679  0.05999  105 ASN A ND2 
714  N N   . ASN A 99  ? 0.28166 0.25945 0.32275 0.03525  0.02267  0.01870  106 ASN A N   
715  C CA  . ASN A 99  ? 0.28902 0.27380 0.34613 0.03572  0.01841  0.01276  106 ASN A CA  
716  C C   . ASN A 99  ? 0.30541 0.27713 0.36167 0.04249  0.01071  0.01087  106 ASN A C   
717  O O   . ASN A 99  ? 0.27941 0.24597 0.34269 0.04051  0.00990  0.00673  106 ASN A O   
718  C CB  . ASN A 99  ? 0.31202 0.30287 0.37782 0.02362  0.02327  0.01021  106 ASN A CB  
719  C CG  . ASN A 99  ? 0.24841 0.26584 0.32282 0.01810  0.03010  0.00937  106 ASN A CG  
720  O OD1 . ASN A 99  ? 0.31810 0.35513 0.40030 0.02728  0.02880  0.00834  106 ASN A OD1 
721  N ND2 . ASN A 99  ? 0.29763 0.31515 0.37104 0.00344  0.03877  0.00946  106 ASN A ND2 
722  N N   . LEU A 100 ? 0.29683 0.26778 0.34608 0.05031  0.00541  0.01137  107 LEU A N   
723  C CA  . LEU A 100 ? 0.31172 0.28370 0.36646 0.05838  -0.00270 0.00686  107 LEU A CA  
724  C C   . LEU A 100 ? 0.36948 0.32252 0.42276 0.06393  -0.00515 0.01029  107 LEU A C   
725  O O   . LEU A 100 ? 0.30761 0.26271 0.37395 0.06848  -0.00713 0.00308  107 LEU A O   
726  C CB  . LEU A 100 ? 0.25424 0.24101 0.32416 0.05589  -0.00157 -0.00269 107 LEU A CB  
727  C CG  . LEU A 100 ? 0.30497 0.29881 0.37249 0.05222  0.00282  -0.00451 107 LEU A CG  
728  C CD1 . LEU A 100 ? 0.33422 0.33052 0.40405 0.04910  0.00871  -0.00145 107 LEU A CD1 
729  C CD2 . LEU A 100 ? 0.39136 0.39365 0.46534 0.05026  0.00241  -0.01361 107 LEU A CD2 
730  N N   . GLY A 101 ? 0.29219 0.22299 0.32716 0.06359  -0.00294 0.02131  108 GLY A N   
731  C CA  . GLY A 101 ? 0.35432 0.25447 0.38115 0.07073  -0.00352 0.02754  108 GLY A CA  
732  C C   . GLY A 101 ? 0.40315 0.28682 0.43792 0.06024  0.00561  0.02149  108 GLY A C   
733  O O   . GLY A 101 ? 0.43197 0.28482 0.46209 0.06724  0.00685  0.02314  108 GLY A O   
734  N N   . THR A 102 ? 0.33848 0.24168 0.38415 0.04471  0.01175  0.01374  109 THR A N   
735  C CA  . THR A 102 ? 0.36864 0.26582 0.42212 0.03170  0.01895  0.00412  109 THR A CA  
736  C C   . THR A 102 ? 0.39992 0.28840 0.44539 0.01258  0.02949  0.00715  109 THR A C   
737  O O   . THR A 102 ? 0.40340 0.30150 0.44196 0.00897  0.03203  0.01506  109 THR A O   
738  C CB  . THR A 102 ? 0.34349 0.27563 0.41375 0.02747  0.01681  -0.00739 109 THR A CB  
739  O OG1 . THR A 102 ? 0.33544 0.29365 0.40803 0.02145  0.01756  -0.00415 109 THR A OG1 
740  C CG2 . THR A 102 ? 0.36139 0.30571 0.43921 0.04149  0.00979  -0.01084 109 THR A CG2 
741  N N   . ILE A 103 ? 0.32625 0.19834 0.37348 -0.00182 0.03738  -0.00200 110 ILE A N   
742  C CA  . ILE A 103 ? 0.32349 0.19698 0.36953 -0.02666 0.04904  -0.00542 110 ILE A CA  
743  C C   . ILE A 103 ? 0.32592 0.25299 0.39336 -0.03689 0.04593  -0.01828 110 ILE A C   
744  O O   . ILE A 103 ? 0.33911 0.27562 0.41413 -0.05541 0.05050  -0.03268 110 ILE A O   
745  C CB  . ILE A 103 ? 0.44441 0.26811 0.47874 -0.04002 0.06077  -0.01052 110 ILE A CB  
746  C CG1 . ILE A 103 ? 0.49881 0.30763 0.53908 -0.02918 0.05700  -0.02262 110 ILE A CG1 
747  C CG2 . ILE A 103 ? 0.53092 0.30131 0.53729 -0.03374 0.06694  0.00848  110 ILE A CG2 
748  C CD1 . ILE A 103 ? 0.60297 0.44906 0.66067 -0.04267 0.05579  -0.04377 110 ILE A CD1 
749  N N   . ALA A 104 ? 0.33942 0.30104 0.41467 -0.02439 0.03805  -0.01320 111 ALA A N   
750  C CA  . ALA A 104 ? 0.38158 0.38817 0.47275 -0.02414 0.03150  -0.02125 111 ALA A CA  
751  C C   . ALA A 104 ? 0.26019 0.30304 0.36460 -0.04319 0.03592  -0.02989 111 ALA A C   
752  O O   . ALA A 104 ? 0.28235 0.35845 0.39693 -0.04795 0.03020  -0.04029 111 ALA A O   
753  C CB  . ALA A 104 ? 0.34756 0.37139 0.44035 -0.00539 0.02474  -0.01233 111 ALA A CB  
754  N N   . LYS A 105 ? 0.27639 0.31847 0.38057 -0.05511 0.04606  -0.02668 112 LYS A N   
755  C CA  . LYS A 105 ? 0.27486 0.36169 0.39748 -0.07537 0.05126  -0.03788 112 LYS A CA  
756  C C   . LYS A 105 ? 0.36817 0.44878 0.49225 -0.10074 0.05595  -0.05484 112 LYS A C   
757  O O   . LYS A 105 ? 0.28418 0.41237 0.42443 -0.10957 0.04954  -0.06902 112 LYS A O   
758  C CB  . LYS A 105 ? 0.30716 0.39451 0.42861 -0.08598 0.06499  -0.03234 112 LYS A CB  
759  C CG  . LYS A 105 ? 0.50005 0.64780 0.64795 -0.10576 0.07089  -0.04578 112 LYS A CG  
760  C CD  . LYS A 105 ? 0.38592 0.53689 0.53268 -0.11777 0.08788  -0.04149 112 LYS A CD  
761  C CE  . LYS A 105 ? 0.61277 0.81720 0.78590 -0.14832 0.09880  -0.05931 112 LYS A CE  
762  N NZ  . LYS A 105 ? 0.65070 0.90588 0.84341 -0.14496 0.10717  -0.05958 112 LYS A NZ  
763  N N   . SER A 106 ? 0.35913 0.38014 0.46435 -0.11225 0.06720  -0.05409 113 SER A N   
764  C CA  . SER A 106 ? 0.37970 0.38466 0.48365 -0.13751 0.07464  -0.07281 113 SER A CA  
765  C C   . SER A 106 ? 0.33719 0.34427 0.44094 -0.12632 0.06345  -0.08267 113 SER A C   
766  O O   . SER A 106 ? 0.43091 0.45701 0.54049 -0.14626 0.06425  -0.10353 113 SER A O   
767  C CB  . SER A 106 ? 0.45609 0.38528 0.53582 -0.14937 0.09157  -0.06735 113 SER A CB  
768  O OG  . SER A 106 ? 0.49202 0.37305 0.55339 -0.12029 0.08614  -0.05067 113 SER A OG  
769  N N   . GLY A 107 ? 0.31278 0.30377 0.40932 -0.09721 0.05414  -0.07005 114 GLY A N   
770  C CA  . GLY A 107 ? 0.39200 0.38820 0.48777 -0.08765 0.04612  -0.07940 114 GLY A CA  
771  C C   . GLY A 107 ? 0.33991 0.40008 0.44717 -0.08907 0.03465  -0.08667 114 GLY A C   
772  O O   . GLY A 107 ? 0.36260 0.43771 0.46793 -0.09887 0.03227  -0.10331 114 GLY A O   
773  N N   . THR A 108 ? 0.29334 0.39097 0.41019 -0.07755 0.02748  -0.07416 115 THR A N   
774  C CA  . THR A 108 ? 0.30358 0.46196 0.43011 -0.07461 0.01550  -0.07769 115 THR A CA  
775  C C   . THR A 108 ? 0.31687 0.51542 0.45502 -0.10243 0.01654  -0.09827 115 THR A C   
776  O O   . THR A 108 ? 0.30176 0.53846 0.43897 -0.10657 0.00679  -0.10961 115 THR A O   
777  C CB  . THR A 108 ? 0.31850 0.50341 0.45473 -0.05519 0.01038  -0.06121 115 THR A CB  
778  O OG1 . THR A 108 ? 0.26893 0.41768 0.39315 -0.03339 0.00977  -0.04589 115 THR A OG1 
779  C CG2 . THR A 108 ? 0.26162 0.50686 0.40657 -0.04613 -0.00318 -0.06170 115 THR A CG2 
780  N N   . LYS A 109 ? 0.31251 0.50507 0.45979 -0.12393 0.02890  -0.10414 116 LYS A N   
781  C CA  . LYS A 109 ? 0.32232 0.55399 0.48292 -0.15676 0.03260  -0.12756 116 LYS A CA  
782  C C   . LYS A 109 ? 0.41772 0.62717 0.56427 -0.17455 0.03493  -0.14854 116 LYS A C   
783  O O   . LYS A 109 ? 0.36645 0.62805 0.51853 -0.18835 0.02615  -0.16731 116 LYS A O   
784  C CB  . LYS A 109 ? 0.29695 0.51015 0.46427 -0.18076 0.05110  -0.12959 116 LYS A CB  
785  C CG  . LYS A 109 ? 0.49041 0.72777 0.66618 -0.21888 0.06010  -0.15465 116 LYS A CG  
786  C CD  . LYS A 109 ? 0.65127 0.84363 0.81928 -0.23897 0.08218  -0.15091 116 LYS A CD  
787  C CE  . LYS A 109 ? 0.62774 0.85611 0.80254 -0.26461 0.08888  -0.16849 116 LYS A CE  
788  N NZ  . LYS A 109 ? 0.67045 0.95242 0.85144 -0.26797 0.07466  -0.18810 116 LYS A NZ  
789  N N   . ALA A 110 ? 0.38047 0.51494 0.50808 -0.17215 0.04611  -0.14635 117 ALA A N   
790  C CA  . ALA A 110 ? 0.39825 0.50546 0.51242 -0.18618 0.05123  -0.16813 117 ALA A CA  
791  C C   . ALA A 110 ? 0.36441 0.50621 0.47183 -0.16970 0.03594  -0.17081 117 ALA A C   
792  O O   . ALA A 110 ? 0.44403 0.60783 0.54559 -0.18787 0.03444  -0.19460 117 ALA A O   
793  C CB  . ALA A 110 ? 0.47720 0.49711 0.57472 -0.17865 0.06575  -0.16234 117 ALA A CB  
794  N N   . PHE A 111 ? 0.33929 0.48436 0.44421 -0.13775 0.02604  -0.14750 118 PHE A N   
795  C CA  . PHE A 111 ? 0.35378 0.52555 0.44734 -0.12273 0.01418  -0.14615 118 PHE A CA  
796  C C   . PHE A 111 ? 0.43295 0.67872 0.53015 -0.13149 -0.00021 -0.15438 118 PHE A C   
797  O O   . PHE A 111 ? 0.35115 0.61925 0.43359 -0.13900 -0.00547 -0.16912 118 PHE A O   
798  C CB  . PHE A 111 ? 0.27477 0.43401 0.36585 -0.09117 0.00889  -0.11922 118 PHE A CB  
799  C CG  . PHE A 111 ? 0.28485 0.46197 0.36018 -0.07670 0.00037  -0.11409 118 PHE A CG  
800  C CD1 . PHE A 111 ? 0.34248 0.51673 0.40219 -0.08630 0.00358  -0.13204 118 PHE A CD1 
801  C CD2 . PHE A 111 ? 0.29958 0.49042 0.37263 -0.05416 -0.00812 -0.09139 118 PHE A CD2 
802  C CE1 . PHE A 111 ? 0.32832 0.51685 0.36893 -0.07523 -0.00154 -0.12599 118 PHE A CE1 
803  C CE2 . PHE A 111 ? 0.32736 0.52601 0.38073 -0.04296 -0.01294 -0.08429 118 PHE A CE2 
804  C CZ  . PHE A 111 ? 0.35791 0.55700 0.39418 -0.05424 -0.00960 -0.10089 118 PHE A CZ  
805  N N   . MET A 112 ? 0.38367 0.67230 0.50028 -0.13005 -0.00688 -0.14621 119 MET A N   
806  C CA  . MET A 112 ? 0.40146 0.76863 0.52437 -0.13096 -0.02404 -0.15120 119 MET A CA  
807  C C   . MET A 112 ? 0.39355 0.78904 0.51871 -0.16401 -0.02106 -0.18021 119 MET A C   
808  O O   . MET A 112 ? 0.42588 0.86804 0.54062 -0.16200 -0.03302 -0.18510 119 MET A O   
809  C CB  . MET A 112 ? 0.45311 0.85894 0.59877 -0.11263 -0.03133 -0.13302 119 MET A CB  
810  C CG  . MET A 112 ? 0.22787 0.62085 0.36138 -0.07434 -0.03966 -0.10408 119 MET A CG  
811  S SD  . MET A 112 ? 0.90611 1.35775 1.06320 -0.04744 -0.05191 -0.08658 119 MET A SD  
812  C CE  . MET A 112 ? 0.35046 0.73457 0.49821 -0.01939 -0.04244 -0.06002 119 MET A CE  
813  N N   . GLU A 113 ? 0.43589 0.78951 0.56584 -0.18886 -0.00211 -0.19389 120 GLU A N   
814  C CA  . GLU A 113 ? 0.40753 0.76507 0.52920 -0.21566 0.00622  -0.21826 120 GLU A CA  
815  C C   . GLU A 113 ? 0.43754 0.77211 0.53412 -0.21889 0.00792  -0.23219 120 GLU A C   
816  O O   . GLU A 113 ? 0.48248 0.84641 0.56989 -0.23341 0.00690  -0.24994 120 GLU A O   
817  C CB  . GLU A 113 ? 0.60076 0.90834 0.72742 -0.24015 0.02848  -0.22722 120 GLU A CB  
818  C CG  . GLU A 113 ? 0.67050 0.98720 0.81789 -0.23919 0.03235  -0.21330 120 GLU A CG  
819  C CD  . GLU A 113 ? 0.77709 1.03941 0.92090 -0.26528 0.05599  -0.22091 120 GLU A CD  
820  O OE1 . GLU A 113 ? 1.00798 1.24464 1.13818 -0.28654 0.06740  -0.24046 120 GLU A OE1 
821  O OE2 . GLU A 113 ? 0.77989 1.02337 0.93195 -0.26420 0.06429  -0.20658 120 GLU A OE2 
822  N N   . ALA A 114 ? 0.41359 0.69810 0.49953 -0.20584 0.01173  -0.22598 121 ALA A N   
823  C CA  . ALA A 114 ? 0.52774 0.79184 0.59008 -0.20624 0.01537  -0.23949 121 ALA A CA  
824  C C   . ALA A 114 ? 0.40303 0.72654 0.45026 -0.19332 -0.00366 -0.23390 121 ALA A C   
825  O O   . ALA A 114 ? 0.44111 0.77721 0.46926 -0.20212 -0.00262 -0.24890 121 ALA A O   
826  C CB  . ALA A 114 ? 0.44618 0.64272 0.50321 -0.19281 0.02586  -0.23502 121 ALA A CB  
827  N N   . LEU A 115 ? 0.40926 0.76758 0.46270 -0.17120 -0.02038 -0.21054 122 LEU A N   
828  C CA  . LEU A 115 ? 0.44456 0.84984 0.47719 -0.15395 -0.03823 -0.19856 122 LEU A CA  
829  C C   . LEU A 115 ? 0.50790 0.97126 0.53854 -0.16338 -0.04721 -0.20720 122 LEU A C   
830  O O   . LEU A 115 ? 0.52009 1.00878 0.52512 -0.16066 -0.05508 -0.20863 122 LEU A O   
831  C CB  . LEU A 115 ? 0.35245 0.77048 0.39199 -0.12276 -0.05077 -0.16620 122 LEU A CB  
832  C CG  . LEU A 115 ? 0.41472 0.76550 0.44692 -0.10150 -0.03887 -0.14545 122 LEU A CG  
833  C CD1 . LEU A 115 ? 0.38941 0.74550 0.42805 -0.07133 -0.04739 -0.11328 122 LEU A CD1 
834  C CD2 . LEU A 115 ? 0.40048 0.73221 0.40036 -0.10006 -0.03428 -0.14942 122 LEU A CD2 
835  N N   . GLN A 116 ? 0.50606 0.99269 0.56241 -0.17508 -0.04550 -0.21342 123 GLN A N   
836  C CA  . GLN A 116 ? 0.43294 0.97866 0.49060 -0.18639 -0.05306 -0.22585 123 GLN A CA  
837  C C   . GLN A 116 ? 0.60419 1.13279 0.65238 -0.21875 -0.03767 -0.25701 123 GLN A C   
838  O O   . GLN A 116 ? 0.74778 1.32592 0.79607 -0.23287 -0.04236 -0.27209 123 GLN A O   
839  C CB  . GLN A 116 ? 0.72300 1.30662 0.81217 -0.18587 -0.05630 -0.22185 123 GLN A CB  
840  C CG  . GLN A 116 ? 0.64742 1.26225 0.74486 -0.14958 -0.07381 -0.19189 123 GLN A CG  
841  C CD  . GLN A 116 ? 0.97863 1.66693 1.09053 -0.14131 -0.08790 -0.19084 123 GLN A CD  
842  O OE1 . GLN A 116 ? 1.04450 1.76963 1.15815 -0.16363 -0.08731 -0.21315 123 GLN A OE1 
843  N NE2 . GLN A 116 ? 0.97606 1.68571 1.09886 -0.10817 -0.09998 -0.16575 123 GLN A NE2 
844  N N   . ALA A 117 ? 0.71084 1.17042 0.75123 -0.22900 -0.01915 -0.26710 124 ALA A N   
845  C CA  . ALA A 117 ? 0.67280 1.10431 0.70256 -0.25549 -0.00187 -0.29528 124 ALA A CA  
846  C C   . ALA A 117 ? 0.68442 1.08755 0.68708 -0.24947 0.00235  -0.30017 124 ALA A C   
847  O O   . ALA A 117 ? 0.66285 1.02329 0.65806 -0.26543 0.02056  -0.32104 124 ALA A O   
848  C CB  . ALA A 117 ? 0.67223 1.04007 0.71581 -0.27190 0.02015  -0.30417 124 ALA A CB  
849  N N   . GLY A 118 ? 0.64659 1.07011 0.63340 -0.22605 -0.01243 -0.28086 125 GLY A N   
850  C CA  . GLY A 118 ? 0.57940 0.98638 0.53754 -0.22163 -0.00825 -0.28533 125 GLY A CA  
851  C C   . GLY A 118 ? 0.57731 0.93349 0.52950 -0.20312 -0.00097 -0.27306 125 GLY A C   
852  O O   . GLY A 118 ? 0.60065 0.94009 0.53087 -0.20056 0.00681  -0.27898 125 GLY A O   
853  N N   . ALA A 119 ? 0.54865 0.88225 0.52027 -0.19089 -0.00213 -0.25755 126 ALA A N   
854  C CA  . ALA A 119 ? 0.52663 0.81822 0.49390 -0.17293 0.00379  -0.24683 126 ALA A CA  
855  C C   . ALA A 119 ? 0.44456 0.77029 0.39295 -0.15185 -0.01327 -0.22175 126 ALA A C   
856  O O   . ALA A 119 ? 0.47738 0.85466 0.42181 -0.14599 -0.03136 -0.20775 126 ALA A O   
857  C CB  . ALA A 119 ? 0.48181 0.72974 0.47666 -0.16976 0.01113  -0.24203 126 ALA A CB  
858  N N   . ASP A 120 ? 0.53574 0.82318 0.47646 -0.13375 -0.00364 -0.20724 127 ASP A N   
859  C CA  . ASP A 120 ? 0.54849 0.84523 0.47351 -0.10994 -0.01240 -0.17425 127 ASP A CA  
860  C C   . ASP A 120 ? 0.37699 0.62826 0.32475 -0.09057 -0.00444 -0.15326 127 ASP A C   
861  O O   . ASP A 120 ? 0.40324 0.61820 0.37500 -0.09335 0.00672  -0.16314 127 ASP A O   
862  C CB  . ASP A 120 ? 0.58121 0.88308 0.46662 -0.11117 -0.00701 -0.17682 127 ASP A CB  
863  C CG  . ASP A 120 ? 0.66173 0.92027 0.55113 -0.11463 0.01590  -0.19363 127 ASP A CG  
864  O OD1 . ASP A 120 ? 0.78281 1.02894 0.68117 -0.13117 0.02651  -0.22513 127 ASP A OD1 
865  O OD2 . ASP A 120 ? 0.66138 0.89841 0.54654 -0.10065 0.02413  -0.17642 127 ASP A OD2 
866  N N   . ILE A 121 ? 0.36893 0.62076 0.30580 -0.07063 -0.01032 -0.12379 128 ILE A N   
867  C CA  . ILE A 121 ? 0.40240 0.61953 0.35984 -0.05356 -0.00574 -0.10388 128 ILE A CA  
868  C C   . ILE A 121 ? 0.37837 0.55569 0.34573 -0.05436 0.01180  -0.11448 128 ILE A C   
869  O O   . ILE A 121 ? 0.39350 0.54350 0.38508 -0.04574 0.01572  -0.10858 128 ILE A O   
870  C CB  . ILE A 121 ? 0.37207 0.59305 0.31039 -0.03458 -0.01302 -0.07324 128 ILE A CB  
871  C CG1 . ILE A 121 ? 0.49033 0.74934 0.43267 -0.02532 -0.03153 -0.06081 128 ILE A CG1 
872  C CG2 . ILE A 121 ? 0.42756 0.60894 0.37982 -0.02150 -0.00412 -0.05769 128 ILE A CG2 
873  C CD1 . ILE A 121 ? 0.63305 0.89492 0.55057 -0.00342 -0.03983 -0.03073 128 ILE A CD1 
874  N N   . SER A 122 ? 0.41098 0.58857 0.36062 -0.06389 0.02238  -0.13169 129 SER A N   
875  C CA  . SER A 122 ? 0.42717 0.57561 0.39063 -0.06130 0.03907  -0.14329 129 SER A CA  
876  C C   . SER A 122 ? 0.49517 0.61741 0.48757 -0.06206 0.04404  -0.15956 129 SER A C   
877  O O   . SER A 122 ? 0.41486 0.51270 0.42553 -0.05225 0.05394  -0.16373 129 SER A O   
878  C CB  . SER A 122 ? 0.39300 0.55165 0.33265 -0.07210 0.05173  -0.16227 129 SER A CB  
879  O OG  . SER A 122 ? 0.47126 0.63889 0.40468 -0.08810 0.05363  -0.19034 129 SER A OG  
880  N N   . MET A 123 ? 0.38235 0.50938 0.37861 -0.07350 0.03787  -0.16869 130 MET A N   
881  C CA  . MET A 123 ? 0.33276 0.42554 0.34966 -0.07665 0.04494  -0.18215 130 MET A CA  
882  C C   . MET A 123 ? 0.42499 0.50051 0.46154 -0.06544 0.03880  -0.16057 130 MET A C   
883  O O   . MET A 123 ? 0.35007 0.39429 0.39856 -0.06875 0.04406  -0.16662 130 MET A O   
884  C CB  . MET A 123 ? 0.41589 0.51877 0.42504 -0.10104 0.04562  -0.20680 130 MET A CB  
885  C CG  . MET A 123 ? 0.48853 0.59599 0.47889 -0.11323 0.05654  -0.23564 130 MET A CG  
886  S SD  . MET A 123 ? 0.62789 0.77121 0.60091 -0.14519 0.05114  -0.26159 130 MET A SD  
887  C CE  . MET A 123 ? 0.60848 0.70543 0.60711 -0.15439 0.05957  -0.26730 130 MET A CE  
888  N N   . ILE A 124 ? 0.34697 0.43758 0.38357 -0.05257 0.02977  -0.13584 131 ILE A N   
889  C CA  . ILE A 124 ? 0.33031 0.41060 0.38188 -0.04308 0.02407  -0.11654 131 ILE A CA  
890  C C   . ILE A 124 ? 0.30420 0.34303 0.37064 -0.03375 0.03150  -0.11671 131 ILE A C   
891  O O   . ILE A 124 ? 0.30632 0.32799 0.38081 -0.03405 0.03066  -0.10955 131 ILE A O   
892  C CB  . ILE A 124 ? 0.31248 0.40790 0.35889 -0.02914 0.01685  -0.09350 131 ILE A CB  
893  C CG1 . ILE A 124 ? 0.31298 0.40039 0.37300 -0.02002 0.01217  -0.07653 131 ILE A CG1 
894  C CG2 . ILE A 124 ? 0.29323 0.37737 0.33591 -0.02070 0.02424  -0.09232 131 ILE A CG2 
895  C CD1 . ILE A 124 ? 0.29432 0.39374 0.34798 -0.00736 0.00614  -0.05634 131 ILE A CD1 
896  N N   . GLY A 125 ? 0.32200 0.34676 0.39152 -0.02444 0.03898  -0.12449 132 GLY A N   
897  C CA  . GLY A 125 ? 0.36877 0.36029 0.45267 -0.00944 0.04292  -0.12246 132 GLY A CA  
898  C C   . GLY A 125 ? 0.37660 0.33013 0.46157 -0.01459 0.04961  -0.13280 132 GLY A C   
899  O O   . GLY A 125 ? 0.45266 0.37438 0.54377 -0.00153 0.04987  -0.12307 132 GLY A O   
900  N N   . GLN A 126 ? 0.33332 0.28722 0.40925 -0.03432 0.05552  -0.15236 133 GLN A N   
901  C CA  . GLN A 126 ? 0.42565 0.33632 0.49948 -0.04455 0.06516  -0.16420 133 GLN A CA  
902  C C   . GLN A 126 ? 0.47089 0.37133 0.54437 -0.05401 0.06188  -0.14892 133 GLN A C   
903  O O   . GLN A 126 ? 0.50211 0.35820 0.57118 -0.06336 0.07187  -0.15410 133 GLN A O   
904  C CB  . GLN A 126 ? 0.43764 0.35643 0.50088 -0.06879 0.07287  -0.19293 133 GLN A CB  
905  C CG  . GLN A 126 ? 0.55579 0.48581 0.61580 -0.06255 0.07935  -0.21129 133 GLN A CG  
906  C CD  . GLN A 126 ? 0.61610 0.55821 0.66087 -0.08854 0.08643  -0.24129 133 GLN A CD  
907  O OE1 . GLN A 126 ? 0.59629 0.52366 0.63674 -0.10771 0.08960  -0.24792 133 GLN A OE1 
908  N NE2 . GLN A 126 ? 0.63644 0.61132 0.67126 -0.08868 0.08765  -0.25138 133 GLN A NE2 
909  N N   . PHE A 127 ? 0.38764 0.32504 0.46431 -0.05232 0.05046  -0.13096 134 PHE A N   
910  C CA  . PHE A 127 ? 0.42255 0.36127 0.50084 -0.06273 0.04883  -0.11909 134 PHE A CA  
911  C C   . PHE A 127 ? 0.35072 0.28038 0.43189 -0.04251 0.04344  -0.09432 134 PHE A C   
912  O O   . PHE A 127 ? 0.41886 0.35805 0.50133 -0.04834 0.04186  -0.08279 134 PHE A O   
913  C CB  . PHE A 127 ? 0.34373 0.33944 0.42463 -0.07854 0.04074  -0.12307 134 PHE A CB  
914  C CG  . PHE A 127 ? 0.39891 0.41174 0.47405 -0.09981 0.04370  -0.14916 134 PHE A CG  
915  C CD1 . PHE A 127 ? 0.48946 0.47680 0.56266 -0.12471 0.05554  -0.16870 134 PHE A CD1 
916  C CD2 . PHE A 127 ? 0.37564 0.42471 0.44317 -0.09634 0.03655  -0.15523 134 PHE A CD2 
917  C CE1 . PHE A 127 ? 0.46173 0.46545 0.52805 -0.14693 0.05887  -0.19687 134 PHE A CE1 
918  C CE2 . PHE A 127 ? 0.41910 0.48624 0.47686 -0.11664 0.03894  -0.18090 134 PHE A CE2 
919  C CZ  . PHE A 127 ? 0.48345 0.52982 0.54179 -0.14226 0.04963  -0.20333 134 PHE A CZ  
920  N N   . GLY A 128 ? 0.38328 0.29995 0.46643 -0.02003 0.04106  -0.08833 135 GLY A N   
921  C CA  . GLY A 128 ? 0.32145 0.22876 0.40547 -0.00180 0.03562  -0.06855 135 GLY A CA  
922  C C   . GLY A 128 ? 0.30350 0.24821 0.39103 0.00315  0.02673  -0.05665 135 GLY A C   
923  O O   . GLY A 128 ? 0.36876 0.30785 0.45514 0.01464  0.02278  -0.04261 135 GLY A O   
924  N N   . VAL A 129 ? 0.27116 0.25110 0.35988 -0.00421 0.02369  -0.06166 136 VAL A N   
925  C CA  . VAL A 129 ? 0.24470 0.25116 0.33383 0.00218  0.01713  -0.04926 136 VAL A CA  
926  C C   . VAL A 129 ? 0.31416 0.33555 0.40073 0.00792  0.01573  -0.05176 136 VAL A C   
927  O O   . VAL A 129 ? 0.24902 0.29035 0.33035 0.00969  0.01215  -0.04414 136 VAL A O   
928  C CB  . VAL A 129 ? 0.27335 0.30815 0.36367 -0.00833 0.01449  -0.04751 136 VAL A CB  
929  C CG1 . VAL A 129 ? 0.27927 0.30294 0.37276 -0.01376 0.01826  -0.04166 136 VAL A CG1 
930  C CG2 . VAL A 129 ? 0.25923 0.31160 0.34777 -0.02413 0.01508  -0.06367 136 VAL A CG2 
931  N N   . GLY A 130 ? 0.30155 0.28218 0.34422 -0.01342 0.01060  -0.05419 137 GLY A N   
932  C CA  . GLY A 130 ? 0.27103 0.26082 0.29935 -0.00532 0.01120  -0.05463 137 GLY A CA  
933  C C   . GLY A 130 ? 0.26644 0.26337 0.29075 -0.00384 0.01442  -0.04210 137 GLY A C   
934  O O   . GLY A 130 ? 0.29102 0.29830 0.30689 0.00037  0.01444  -0.03928 137 GLY A O   
935  N N   . PHE A 131 ? 0.25019 0.24153 0.28041 -0.00701 0.01686  -0.03432 138 PHE A N   
936  C CA  . PHE A 131 ? 0.22827 0.22386 0.25566 -0.00597 0.01778  -0.02571 138 PHE A CA  
937  C C   . PHE A 131 ? 0.28138 0.28566 0.30605 -0.00541 0.01485  -0.02486 138 PHE A C   
938  O O   . PHE A 131 ? 0.25975 0.26716 0.28085 -0.00315 0.01479  -0.01905 138 PHE A O   
939  C CB  . PHE A 131 ? 0.28280 0.27330 0.31415 -0.00823 0.01932  -0.02063 138 PHE A CB  
940  C CG  . PHE A 131 ? 0.31154 0.30498 0.34024 -0.00721 0.01793  -0.01641 138 PHE A CG  
941  C CD1 . PHE A 131 ? 0.28898 0.28201 0.31614 -0.00586 0.01695  -0.01268 138 PHE A CD1 
942  C CD2 . PHE A 131 ? 0.30349 0.30043 0.33335 -0.00737 0.01708  -0.01700 138 PHE A CD2 
943  C CE1 . PHE A 131 ? 0.27768 0.26960 0.30445 -0.00571 0.01394  -0.01085 138 PHE A CE1 
944  C CE2 . PHE A 131 ? 0.27011 0.26628 0.29732 -0.00478 0.01501  -0.01549 138 PHE A CE2 
945  C CZ  . PHE A 131 ? 0.26710 0.25872 0.29273 -0.00446 0.01283  -0.01308 138 PHE A CZ  
946  N N   . TYR A 132 ? 0.25800 0.26668 0.28670 -0.00753 0.01213  -0.02950 139 TYR A N   
947  C CA  . TYR A 132 ? 0.25982 0.27774 0.28760 -0.00535 0.00888  -0.02778 139 TYR A CA  
948  C C   . TYR A 132 ? 0.25199 0.27820 0.27048 -0.00062 0.00634  -0.02769 139 TYR A C   
949  O O   . TYR A 132 ? 0.26559 0.29811 0.28189 0.00294  0.00391  -0.02270 139 TYR A O   
950  C CB  . TYR A 132 ? 0.24486 0.26997 0.28279 -0.00872 0.00659  -0.03233 139 TYR A CB  
951  C CG  . TYR A 132 ? 0.23887 0.25982 0.28448 -0.01188 0.01114  -0.02883 139 TYR A CG  
952  C CD1 . TYR A 132 ? 0.28118 0.30364 0.32564 -0.00807 0.01285  -0.02417 139 TYR A CD1 
953  C CD2 . TYR A 132 ? 0.25130 0.26605 0.30408 -0.01743 0.01391  -0.02981 139 TYR A CD2 
954  C CE1 . TYR A 132 ? 0.24262 0.26459 0.29019 -0.00881 0.01768  -0.02115 139 TYR A CE1 
955  C CE2 . TYR A 132 ? 0.33162 0.34505 0.38932 -0.01923 0.01920  -0.02365 139 TYR A CE2 
956  C CZ  . TYR A 132 ? 0.29667 0.31565 0.35026 -0.01443 0.02132  -0.01957 139 TYR A CZ  
957  O OH  . TYR A 132 ? 0.29549 0.31648 0.35044 -0.01424 0.02714  -0.01371 139 TYR A OH  
958  N N   . SER A 133 ? 0.27800 0.30485 0.29007 0.00113  0.00735  -0.03221 140 SER A N   
959  C CA  . SER A 133 ? 0.27358 0.31139 0.27355 0.00750  0.00706  -0.02982 140 SER A CA  
960  C C   . SER A 133 ? 0.24817 0.28591 0.24688 0.00915  0.01105  -0.01539 140 SER A C   
961  O O   . SER A 133 ? 0.26151 0.30965 0.25178 0.01416  0.01170  -0.00822 140 SER A O   
962  C CB  . SER A 133 ? 0.30591 0.34527 0.29838 0.01112  0.00867  -0.03885 140 SER A CB  
963  O OG  . SER A 133 ? 0.28015 0.31322 0.27508 0.01151  0.01505  -0.03400 140 SER A OG  
964  N N   . ALA A 134 ? 0.24727 0.27407 0.25473 0.00488  0.01318  -0.01059 141 ALA A N   
965  C CA  . ALA A 134 ? 0.25778 0.28194 0.26866 0.00423  0.01458  0.00157  141 ALA A CA  
966  C C   . ALA A 134 ? 0.23750 0.26369 0.24665 0.00731  0.01134  0.00833  141 ALA A C   
967  O O   . ALA A 134 ? 0.25415 0.28142 0.26374 0.00834  0.01290  0.02069  141 ALA A O   
968  C CB  . ALA A 134 ? 0.22172 0.23362 0.24158 -0.00042 0.01396  0.00132  141 ALA A CB  
969  N N   . TYR A 135 ? 0.23255 0.26047 0.24171 0.00905  0.00705  0.00191  142 TYR A N   
970  C CA  . TYR A 135 ? 0.24365 0.27391 0.25257 0.01402  0.00332  0.00833  142 TYR A CA  
971  C C   . TYR A 135 ? 0.27546 0.32139 0.27318 0.02027  0.00187  0.01306  142 TYR A C   
972  O O   . TYR A 135 ? 0.30127 0.35120 0.29778 0.02609  -0.00177 0.02008  142 TYR A O   
973  C CB  . TYR A 135 ? 0.24231 0.27324 0.25781 0.01478  -0.00027 0.00036  142 TYR A CB  
974  C CG  . TYR A 135 ? 0.27106 0.28793 0.29378 0.01202  0.00141  -0.00134 142 TYR A CG  
975  C CD1 . TYR A 135 ? 0.26405 0.26947 0.29041 0.01549  -0.00032 0.00381  142 TYR A CD1 
976  C CD2 . TYR A 135 ? 0.24599 0.26005 0.27081 0.00686  0.00425  -0.00813 142 TYR A CD2 
977  C CE1 . TYR A 135 ? 0.26546 0.25871 0.29560 0.01431  -0.00005 -0.00076 142 TYR A CE1 
978  C CE2 . TYR A 135 ? 0.28581 0.29002 0.31355 0.00595  0.00533  -0.00978 142 TYR A CE2 
979  C CZ  . TYR A 135 ? 0.29621 0.29089 0.32565 0.00986  0.00280  -0.00746 142 TYR A CZ  
980  O OH  . TYR A 135 ? 0.26604 0.25187 0.29574 0.01031  0.00257  -0.01209 142 TYR A OH  
981  N N   . LEU A 136 ? 0.27193 0.32753 0.26026 0.02097  0.00445  0.00922  143 LEU A N   
982  C CA  . LEU A 136 ? 0.25181 0.32397 0.22556 0.02866  0.00467  0.01601  143 LEU A CA  
983  C C   . LEU A 136 ? 0.27166 0.34178 0.24627 0.02991  0.01003  0.03673  143 LEU A C   
984  O O   . LEU A 136 ? 0.29750 0.37882 0.26268 0.03710  0.00962  0.04895  143 LEU A O   
985  C CB  . LEU A 136 ? 0.30365 0.38594 0.26625 0.03080  0.00722  0.00545  143 LEU A CB  
986  C CG  . LEU A 136 ? 0.28568 0.36981 0.24750 0.02958  0.00068  -0.01529 143 LEU A CG  
987  C CD1 . LEU A 136 ? 0.30128 0.38771 0.25464 0.03202  0.00401  -0.02651 143 LEU A CD1 
988  C CD2 . LEU A 136 ? 0.30677 0.40680 0.26085 0.03524  -0.00836 -0.01942 143 LEU A CD2 
989  N N   . VAL A 137 ? 0.28919 0.34590 0.27627 0.02272  0.01451  0.04185  144 VAL A N   
990  C CA  . VAL A 137 ? 0.28182 0.33655 0.27513 0.02093  0.01963  0.06164  144 VAL A CA  
991  C C   . VAL A 137 ? 0.30445 0.33658 0.31544 0.01427  0.01667  0.06653  144 VAL A C   
992  O O   . VAL A 137 ? 0.30229 0.32842 0.32200 0.01212  0.01855  0.08392  144 VAL A O   
993  C CB  . VAL A 137 ? 0.27846 0.34418 0.27231 0.01867  0.02796  0.06470  144 VAL A CB  
994  C CG1 . VAL A 137 ? 0.29170 0.38033 0.26521 0.02828  0.03133  0.06022  144 VAL A CG1 
995  C CG2 . VAL A 137 ? 0.27234 0.32778 0.27634 0.01198  0.02736  0.05110  144 VAL A CG2 
996  N N   . ALA A 138 ? 0.30801 0.32696 0.32500 0.01121  0.01201  0.05224  145 ALA A N   
997  C CA  . ALA A 138 ? 0.30597 0.30398 0.33713 0.00618  0.00856  0.05273  145 ALA A CA  
998  C C   . ALA A 138 ? 0.32388 0.31204 0.35520 0.01229  0.00273  0.04866  145 ALA A C   
999  O O   . ALA A 138 ? 0.31681 0.31362 0.34159 0.01673  0.00095  0.03801  145 ALA A O   
1000 C CB  . ALA A 138 ? 0.27500 0.26789 0.31115 0.00011  0.00824  0.04005  145 ALA A CB  
1001 N N   . GLU A 139 ? 0.30270 0.27281 0.34395 0.01250  -0.00035 0.05706  146 GLU A N   
1002 C CA  . GLU A 139 ? 0.30217 0.25993 0.34580 0.01988  -0.00584 0.05135  146 GLU A CA  
1003 C C   . GLU A 139 ? 0.36673 0.31371 0.41389 0.01798  -0.00845 0.03428  146 GLU A C   
1004 O O   . GLU A 139 ? 0.34242 0.28869 0.38798 0.02561  -0.01077 0.02507  146 GLU A O   
1005 C CB  . GLU A 139 ? 0.41253 0.35171 0.46564 0.02241  -0.00851 0.06686  146 GLU A CB  
1006 C CG  . GLU A 139 ? 0.56755 0.47986 0.63590 0.01555  -0.01247 0.06439  146 GLU A CG  
1007 C CD  . GLU A 139 ? 0.80356 0.69648 0.88501 0.01476  -0.01420 0.08377  146 GLU A CD  
1008 O OE1 . GLU A 139 ? 0.69622 0.59171 0.77328 0.02437  -0.01389 0.09660  146 GLU A OE1 
1009 O OE2 . GLU A 139 ? 0.75226 0.62780 0.84989 0.00425  -0.01641 0.08703  146 GLU A OE2 
1010 N N   . LYS A 140 ? 0.28770 0.23002 0.33912 0.00907  -0.00786 0.03038  147 LYS A N   
1011 C CA  . LYS A 140 ? 0.33970 0.27532 0.39097 0.00806  -0.01044 0.01500  147 LYS A CA  
1012 C C   . LYS A 140 ? 0.30707 0.25218 0.35775 -0.00014 -0.00761 0.01302  147 LYS A C   
1013 O O   . LYS A 140 ? 0.30213 0.25137 0.35870 -0.00633 -0.00539 0.02325  147 LYS A O   
1014 C CB  . LYS A 140 ? 0.31799 0.22894 0.37860 0.00835  -0.01744 0.01122  147 LYS A CB  
1015 C CG  . LYS A 140 ? 0.36840 0.27294 0.42735 0.00694  -0.02157 -0.00469 147 LYS A CG  
1016 C CD  . LYS A 140 ? 0.38820 0.26670 0.45448 0.01032  -0.03006 -0.01209 147 LYS A CD  
1017 C CE  . LYS A 140 ? 0.55539 0.42288 0.63019 0.00096  -0.03745 -0.01908 147 LYS A CE  
1018 N NZ  . LYS A 140 ? 0.57879 0.41738 0.66977 -0.00165 -0.04621 -0.01845 147 LYS A NZ  
1019 N N   . VAL A 141 ? 0.23888 0.18957 0.28300 0.00090  -0.00681 0.00161  148 VAL A N   
1020 C CA  . VAL A 141 ? 0.22626 0.18488 0.26971 -0.00467 -0.00473 -0.00024 148 VAL A CA  
1021 C C   . VAL A 141 ? 0.26279 0.21465 0.30453 -0.00422 -0.00925 -0.01093 148 VAL A C   
1022 O O   . VAL A 141 ? 0.26306 0.21370 0.29758 0.00227  -0.00950 -0.01901 148 VAL A O   
1023 C CB  . VAL A 141 ? 0.26492 0.23835 0.30075 -0.00328 0.00111  -0.00150 148 VAL A CB  
1024 C CG1 . VAL A 141 ? 0.25944 0.23804 0.29546 -0.00701 0.00301  -0.00283 148 VAL A CG1 
1025 C CG2 . VAL A 141 ? 0.27654 0.25883 0.31059 -0.00204 0.00404  0.00616  148 VAL A CG2 
1026 N N   . THR A 142 ? 0.25718 0.20761 0.30569 -0.01029 -0.01296 -0.01081 149 THR A N   
1027 C CA  . THR A 142 ? 0.26627 0.21460 0.31115 -0.00957 -0.01858 -0.02114 149 THR A CA  
1028 C C   . THR A 142 ? 0.26882 0.23143 0.31127 -0.01134 -0.01521 -0.01876 149 THR A C   
1029 O O   . THR A 142 ? 0.28291 0.25313 0.33401 -0.01613 -0.01246 -0.01047 149 THR A O   
1030 C CB  . THR A 142 ? 0.29688 0.23245 0.35412 -0.01514 -0.02868 -0.02466 149 THR A CB  
1031 O OG1 . THR A 142 ? 0.33743 0.25590 0.40048 -0.01385 -0.03144 -0.02390 149 THR A OG1 
1032 C CG2 . THR A 142 ? 0.29025 0.22399 0.33942 -0.01173 -0.03668 -0.03916 149 THR A CG2 
1033 N N   . VAL A 143 ? 0.25848 0.22560 0.28921 -0.00619 -0.01469 -0.02482 150 VAL A N   
1034 C CA  . VAL A 143 ? 0.28201 0.26009 0.31011 -0.00606 -0.01202 -0.02154 150 VAL A CA  
1035 C C   . VAL A 143 ? 0.31612 0.29615 0.33844 -0.00348 -0.01987 -0.02862 150 VAL A C   
1036 O O   . VAL A 143 ? 0.29336 0.27221 0.30243 0.00310  -0.02077 -0.03560 150 VAL A O   
1037 C CB  . VAL A 143 ? 0.29611 0.27897 0.31598 -0.00224 -0.00328 -0.01863 150 VAL A CB  
1038 C CG1 . VAL A 143 ? 0.25874 0.24854 0.27665 -0.00094 -0.00122 -0.01438 150 VAL A CG1 
1039 C CG2 . VAL A 143 ? 0.24578 0.22865 0.27060 -0.00449 0.00202  -0.01433 150 VAL A CG2 
1040 N N   . ILE A 144 ? 0.23411 0.22013 0.26628 -0.00776 -0.02575 -0.02703 151 ILE A N   
1041 C CA  . ILE A 144 ? 0.25623 0.24832 0.28356 -0.00521 -0.03524 -0.03376 151 ILE A CA  
1042 C C   . ILE A 144 ? 0.28825 0.29333 0.31130 -0.00100 -0.03074 -0.02575 151 ILE A C   
1043 O O   . ILE A 144 ? 0.26369 0.27407 0.29821 -0.00380 -0.02585 -0.01722 151 ILE A O   
1044 C CB  . ILE A 144 ? 0.27067 0.26289 0.31652 -0.01361 -0.04685 -0.03738 151 ILE A CB  
1045 C CG1 . ILE A 144 ? 0.37663 0.35244 0.43379 -0.01995 -0.04913 -0.03966 151 ILE A CG1 
1046 C CG2 . ILE A 144 ? 0.30373 0.30071 0.34220 -0.01028 -0.06017 -0.04948 151 ILE A CG2 
1047 C CD1 . ILE A 144 ? 0.40341 0.36426 0.44733 -0.01387 -0.05365 -0.05274 151 ILE A CD1 
1048 N N   . THR A 145 ? 0.25022 0.26067 0.25635 0.00708  -0.03190 -0.02774 152 THR A N   
1049 C CA  . THR A 145 ? 0.27094 0.29025 0.27323 0.01208  -0.02657 -0.01735 152 THR A CA  
1050 C C   . THR A 145 ? 0.27911 0.30974 0.26723 0.02008  -0.03429 -0.01930 152 THR A C   
1051 O O   . THR A 145 ? 0.29631 0.32736 0.26990 0.02433  -0.03991 -0.02923 152 THR A O   
1052 C CB  . THR A 145 ? 0.31468 0.32787 0.31053 0.01428  -0.01362 -0.01014 152 THR A CB  
1053 O OG1 . THR A 145 ? 0.29277 0.30888 0.29089 0.01739  -0.00846 0.00064  152 THR A OG1 
1054 C CG2 . THR A 145 ? 0.33443 0.34852 0.31247 0.02045  -0.01102 -0.01287 152 THR A CG2 
1055 N N   . LYS A 146 ? 0.29705 0.33787 0.28866 0.02375  -0.03493 -0.01018 153 LYS A N   
1056 C CA  . LYS A 146 ? 0.25880 0.31332 0.23587 0.03328  -0.04193 -0.00844 153 LYS A CA  
1057 C C   . LYS A 146 ? 0.32489 0.38144 0.30023 0.04006  -0.03316 0.00825  153 LYS A C   
1058 O O   . LYS A 146 ? 0.30070 0.35823 0.29272 0.03876  -0.03157 0.01453  153 LYS A O   
1059 C CB  . LYS A 146 ? 0.26581 0.33403 0.25381 0.03115  -0.05795 -0.01611 153 LYS A CB  
1060 C CG  . LYS A 146 ? 0.30095 0.38749 0.27418 0.04219  -0.06752 -0.01428 153 LYS A CG  
1061 C CD  . LYS A 146 ? 0.32993 0.41875 0.27600 0.04935  -0.07340 -0.02569 153 LYS A CD  
1062 C CE  . LYS A 146 ? 0.32962 0.44031 0.25821 0.06157  -0.08479 -0.02460 153 LYS A CE  
1063 N NZ  . LYS A 146 ? 0.36484 0.48220 0.28551 0.07168  -0.07498 -0.00260 153 LYS A NZ  
1064 N N   . HIS A 147 ? 0.31526 0.37246 0.27131 0.04793  -0.02704 0.01595  154 HIS A N   
1065 C CA  . HIS A 147 ? 0.28613 0.34298 0.23926 0.05513  -0.01930 0.03389  154 HIS A CA  
1066 C C   . HIS A 147 ? 0.37865 0.45385 0.31581 0.06703  -0.02832 0.03903  154 HIS A C   
1067 O O   . HIS A 147 ? 0.35067 0.43765 0.27149 0.07067  -0.03738 0.02826  154 HIS A O   
1068 C CB  . HIS A 147 ? 0.32918 0.37578 0.27477 0.05442  -0.00528 0.04232  154 HIS A CB  
1069 C CG  . HIS A 147 ? 0.40551 0.44537 0.35356 0.05881  0.00393  0.06199  154 HIS A CG  
1070 N ND1 . HIS A 147 ? 0.38338 0.43334 0.31623 0.06999  0.00413  0.07689  154 HIS A ND1 
1071 C CD2 . HIS A 147 ? 0.35425 0.37663 0.31837 0.05373  0.01282  0.06917  154 HIS A CD2 
1072 C CE1 . HIS A 147 ? 0.38136 0.41825 0.32302 0.07103  0.01327  0.09425  154 HIS A CE1 
1073 N NE2 . HIS A 147 ? 0.36384 0.38292 0.32500 0.06095  0.01810  0.08835  154 HIS A NE2 
1074 N N   . ASN A 148 ? 0.33982 0.41748 0.28123 0.07442  -0.02688 0.05461  155 ASN A N   
1075 C CA  . ASN A 148 ? 0.33161 0.42925 0.25754 0.08744  -0.03638 0.06155  155 ASN A CA  
1076 C C   . ASN A 148 ? 0.40373 0.50998 0.29946 0.09569  -0.03346 0.06579  155 ASN A C   
1077 O O   . ASN A 148 ? 0.43224 0.55915 0.30887 0.10582  -0.04491 0.06285  155 ASN A O   
1078 C CB  . ASN A 148 ? 0.34811 0.44395 0.28272 0.09627  -0.03294 0.08131  155 ASN A CB  
1079 C CG  . ASN A 148 ? 0.40541 0.50579 0.36549 0.09449  -0.04003 0.07643  155 ASN A CG  
1080 O OD1 . ASN A 148 ? 0.41394 0.52649 0.38346 0.08801  -0.05088 0.06070  155 ASN A OD1 
1081 N ND2 . ASN A 148 ? 0.39824 0.48950 0.37101 0.10087  -0.03381 0.09056  155 ASN A ND2 
1082 N N   . ASP A 149 ? 0.44128 0.53519 0.33235 0.09219  -0.01856 0.07237  156 ASP A N   
1083 C CA  . ASP A 149 ? 0.47610 0.58128 0.34020 0.10119  -0.01185 0.08095  156 ASP A CA  
1084 C C   . ASP A 149 ? 0.45614 0.56677 0.30655 0.09941  -0.01358 0.06101  156 ASP A C   
1085 O O   . ASP A 149 ? 0.45869 0.58034 0.28726 0.10727  -0.00556 0.06674  156 ASP A O   
1086 C CB  . ASP A 149 ? 0.45059 0.54268 0.32077 0.09904  0.00663  0.10382  156 ASP A CB  
1087 C CG  . ASP A 149 ? 0.54875 0.63260 0.42970 0.10382  0.00873  0.12522  156 ASP A CG  
1088 O OD1 . ASP A 149 ? 0.50356 0.59928 0.38008 0.11317  -0.00319 0.12612  156 ASP A OD1 
1089 O OD2 . ASP A 149 ? 0.58664 0.65185 0.48220 0.09842  0.02151  0.14057  156 ASP A OD2 
1090 N N   . ASP A 150 ? 0.40780 0.51139 0.27093 0.09032  -0.02309 0.03893  157 ASP A N   
1091 C CA  . ASP A 150 ? 0.42160 0.52487 0.27508 0.08900  -0.02451 0.01978  157 ASP A CA  
1092 C C   . ASP A 150 ? 0.50519 0.60670 0.36742 0.08362  -0.04258 -0.00338 157 ASP A C   
1093 O O   . ASP A 150 ? 0.43059 0.53431 0.30817 0.07989  -0.05254 -0.00325 157 ASP A O   
1094 C CB  . ASP A 150 ? 0.37054 0.45793 0.23854 0.07935  -0.00989 0.02228  157 ASP A CB  
1095 C CG  . ASP A 150 ? 0.45792 0.55150 0.30923 0.08468  -0.00439 0.01297  157 ASP A CG  
1096 O OD1 . ASP A 150 ? 0.44784 0.55451 0.27605 0.09539  -0.01314 -0.00000 157 ASP A OD1 
1097 O OD2 . ASP A 150 ? 0.46356 0.55043 0.32502 0.07914  0.00834  0.01783  157 ASP A OD2 
1098 N N   . GLU A 151 ? 0.42349 0.52137 0.27801 0.08344  -0.04670 -0.02286 158 GLU A N   
1099 C CA  . GLU A 151 ? 0.46840 0.55998 0.33426 0.07656  -0.06357 -0.04500 158 GLU A CA  
1100 C C   . GLU A 151 ? 0.34999 0.42102 0.24496 0.06144  -0.05909 -0.04638 158 GLU A C   
1101 O O   . GLU A 151 ? 0.38800 0.45053 0.29132 0.05740  -0.04415 -0.03370 158 GLU A O   
1102 C CB  . GLU A 151 ? 0.46089 0.55530 0.30383 0.08547  -0.07167 -0.06691 158 GLU A CB  
1103 C CG  . GLU A 151 ? 0.64104 0.75676 0.44816 0.10352  -0.06757 -0.06224 158 GLU A CG  
1104 C CD  . GLU A 151 ? 1.00553 1.14147 0.79869 0.11175  -0.08341 -0.06390 158 GLU A CD  
1105 O OE1 . GLU A 151 ? 1.15832 1.31425 0.92490 0.12612  -0.07797 -0.05047 158 GLU A OE1 
1106 O OE2 . GLU A 151 ? 1.07183 1.20554 0.88189 0.10380  -0.10139 -0.07733 158 GLU A OE2 
1107 N N   . GLN A 152 ? 0.33358 0.39749 0.24463 0.05286  -0.07289 -0.06171 159 GLN A N   
1108 C CA  . GLN A 152 ? 0.31220 0.35907 0.25004 0.03923  -0.06941 -0.06128 159 GLN A CA  
1109 C C   . GLN A 152 ? 0.36507 0.39657 0.29784 0.03974  -0.06369 -0.07027 159 GLN A C   
1110 O O   . GLN A 152 ? 0.36317 0.39166 0.28279 0.04571  -0.07227 -0.08763 159 GLN A O   
1111 C CB  . GLN A 152 ? 0.35804 0.40445 0.31861 0.02888  -0.08528 -0.07064 159 GLN A CB  
1112 C CG  . GLN A 152 ? 0.31868 0.35289 0.30807 0.01519  -0.07998 -0.06425 159 GLN A CG  
1113 C CD  . GLN A 152 ? 0.43354 0.47549 0.44958 0.00471  -0.09254 -0.06603 159 GLN A CD  
1114 O OE1 . GLN A 152 ? 0.43835 0.49913 0.45902 0.00691  -0.09682 -0.05982 159 GLN A OE1 
1115 N NE2 . GLN A 152 ? 0.38870 0.41724 0.42454 -0.00659 -0.09837 -0.07308 159 GLN A NE2 
1116 N N   . TYR A 153 ? 0.32925 0.35175 0.27236 0.03475  -0.05000 -0.05956 160 TYR A N   
1117 C CA  . TYR A 153 ? 0.34311 0.35441 0.28343 0.03639  -0.04326 -0.06495 160 TYR A CA  
1118 C C   . TYR A 153 ? 0.35122 0.34770 0.31467 0.02512  -0.04136 -0.06225 160 TYR A C   
1119 O O   . TYR A 153 ? 0.28501 0.28260 0.26414 0.01705  -0.03906 -0.05178 160 TYR A O   
1120 C CB  . TYR A 153 ? 0.33667 0.35631 0.26482 0.04318  -0.02758 -0.05347 160 TYR A CB  
1121 C CG  . TYR A 153 ? 0.36544 0.40011 0.26716 0.05688  -0.02703 -0.05663 160 TYR A CG  
1122 C CD1 . TYR A 153 ? 0.40525 0.44008 0.29196 0.06668  -0.02872 -0.07175 160 TYR A CD1 
1123 C CD2 . TYR A 153 ? 0.44203 0.49152 0.33265 0.06181  -0.02476 -0.04422 160 TYR A CD2 
1124 C CE1 . TYR A 153 ? 0.46763 0.51978 0.32690 0.08138  -0.02736 -0.07511 160 TYR A CE1 
1125 C CE2 . TYR A 153 ? 0.44229 0.50861 0.30586 0.07578  -0.02363 -0.04507 160 TYR A CE2 
1126 C CZ  . TYR A 153 ? 0.50274 0.57166 0.34979 0.08563  -0.02458 -0.06090 160 TYR A CZ  
1127 O OH  . TYR A 153 ? 0.60567 0.69466 0.42288 0.10153  -0.02245 -0.06213 160 TYR A OH  
1128 N N   . ALA A 154 ? 0.29397 0.27778 0.25810 0.02656  -0.04171 -0.07122 161 ALA A N   
1129 C CA  . ALA A 154 ? 0.29711 0.26741 0.27983 0.01837  -0.03933 -0.06720 161 ALA A CA  
1130 C C   . ALA A 154 ? 0.33853 0.30867 0.31634 0.02385  -0.02796 -0.06375 161 ALA A C   
1131 O O   . ALA A 154 ? 0.35845 0.32846 0.32393 0.03387  -0.02741 -0.07314 161 ALA A O   
1132 C CB  . ALA A 154 ? 0.33978 0.29277 0.33308 0.01450  -0.05200 -0.07940 161 ALA A CB  
1133 N N   . TRP A 155 ? 0.27642 0.24868 0.26431 0.01807  -0.01948 -0.05139 162 TRP A N   
1134 C CA  . TRP A 155 ? 0.30478 0.27872 0.29387 0.02066  -0.01058 -0.04744 162 TRP A CA  
1135 C C   . TRP A 155 ? 0.30652 0.26800 0.30891 0.01617  -0.01342 -0.04625 162 TRP A C   
1136 O O   . TRP A 155 ? 0.28811 0.24435 0.30114 0.00817  -0.01732 -0.04181 162 TRP A O   
1137 C CB  . TRP A 155 ? 0.27293 0.25780 0.26404 0.01711  -0.00119 -0.03577 162 TRP A CB  
1138 C CG  . TRP A 155 ? 0.26017 0.25018 0.25649 0.01702  0.00671  -0.03122 162 TRP A CG  
1139 C CD1 . TRP A 155 ? 0.26582 0.26785 0.25893 0.02069  0.01465  -0.02818 162 TRP A CD1 
1140 C CD2 . TRP A 155 ? 0.27196 0.25859 0.27898 0.01250  0.00710  -0.02809 162 TRP A CD2 
1141 N NE1 . TRP A 155 ? 0.24631 0.25250 0.25002 0.01775  0.01859  -0.02500 162 TRP A NE1 
1142 C CE2 . TRP A 155 ? 0.25610 0.25302 0.26636 0.01362  0.01355  -0.02554 162 TRP A CE2 
1143 C CE3 . TRP A 155 ? 0.25125 0.22955 0.26562 0.00790  0.00275  -0.02617 162 TRP A CE3 
1144 C CZ2 . TRP A 155 ? 0.29880 0.29790 0.31763 0.01106  0.01384  -0.02344 162 TRP A CZ2 
1145 C CZ3 . TRP A 155 ? 0.28680 0.26732 0.30701 0.00650  0.00474  -0.02221 162 TRP A CZ3 
1146 C CH2 . TRP A 155 ? 0.25519 0.24600 0.27672 0.00842  0.00930  -0.02199 162 TRP A CH2 
1147 N N   . GLU A 156 ? 0.27050 0.22922 0.27310 0.02214  -0.01108 -0.04866 163 GLU A N   
1148 C CA  . GLU A 156 ? 0.28774 0.23466 0.30181 0.01958  -0.01382 -0.04506 163 GLU A CA  
1149 C C   . GLU A 156 ? 0.28743 0.24113 0.30252 0.02584  -0.00813 -0.04244 163 GLU A C   
1150 O O   . GLU A 156 ? 0.27799 0.23957 0.28665 0.03480  -0.00479 -0.04835 163 GLU A O   
1151 C CB  . GLU A 156 ? 0.37903 0.30599 0.39661 0.02147  -0.02383 -0.05418 163 GLU A CB  
1152 C CG  . GLU A 156 ? 0.41721 0.32967 0.45001 0.01518  -0.02738 -0.04574 163 GLU A CG  
1153 C CD  . GLU A 156 ? 0.51123 0.40170 0.55259 0.01243  -0.03873 -0.05379 163 GLU A CD  
1154 O OE1 . GLU A 156 ? 0.55435 0.43088 0.59161 0.02187  -0.04371 -0.06637 163 GLU A OE1 
1155 O OE2 . GLU A 156 ? 0.49326 0.38093 0.54696 0.00101  -0.04298 -0.04834 163 GLU A OE2 
1156 N N   . SER A 157 ? 0.30524 0.25869 0.32856 0.02206  -0.00721 -0.03332 164 SER A N   
1157 C CA  . SER A 157 ? 0.26824 0.22951 0.29424 0.02850  -0.00436 -0.03103 164 SER A CA  
1158 C C   . SER A 157 ? 0.27287 0.22753 0.30585 0.02671  -0.00708 -0.02155 164 SER A C   
1159 O O   . SER A 157 ? 0.27483 0.23008 0.30967 0.01872  -0.00663 -0.01390 164 SER A O   
1160 C CB  . SER A 157 ? 0.24788 0.22999 0.27344 0.02649  0.00253  -0.02864 164 SER A CB  
1161 O OG  . SER A 157 ? 0.27619 0.26946 0.30737 0.03211  0.00367  -0.02707 164 SER A OG  
1162 N N   . SER A 158 ? 0.28530 0.23516 0.32168 0.03578  -0.00936 -0.02120 165 SER A N   
1163 C CA  . SER A 158 ? 0.28107 0.23025 0.32225 0.03729  -0.01097 -0.00979 165 SER A CA  
1164 C C   . SER A 158 ? 0.28847 0.26049 0.32969 0.04230  -0.00845 -0.00821 165 SER A C   
1165 O O   . SER A 158 ? 0.32152 0.29598 0.36575 0.04910  -0.01106 -0.00116 165 SER A O   
1166 C CB  . SER A 158 ? 0.35515 0.28174 0.40224 0.04479  -0.01655 -0.00841 165 SER A CB  
1167 O OG  . SER A 158 ? 0.40592 0.31100 0.45718 0.03747  -0.02070 -0.00931 165 SER A OG  
1168 N N   . ALA A 159 ? 0.26968 0.25878 0.30927 0.03883  -0.00413 -0.01397 166 ALA A N   
1169 C CA  . ALA A 159 ? 0.29342 0.30617 0.33765 0.04107  -0.00255 -0.01456 166 ALA A CA  
1170 C C   . ALA A 159 ? 0.29485 0.31249 0.34484 0.05400  -0.00305 -0.01792 166 ALA A C   
1171 O O   . ALA A 159 ? 0.38035 0.38674 0.42786 0.05986  -0.00196 -0.02432 166 ALA A O   
1172 C CB  . ALA A 159 ? 0.32393 0.34551 0.36728 0.03840  -0.00552 -0.00752 166 ALA A CB  
1173 N N   . GLY A 160 ? 0.33930 0.37521 0.39676 0.06001  -0.00516 -0.01501 167 GLY A N   
1174 C CA  . GLY A 160 ? 0.29264 0.33676 0.35761 0.07403  -0.00490 -0.01816 167 GLY A CA  
1175 C C   . GLY A 160 ? 0.27718 0.33835 0.34666 0.07547  0.00239  -0.02563 167 GLY A C   
1176 O O   . GLY A 160 ? 0.34623 0.41382 0.42012 0.08902  0.00443  -0.02978 167 GLY A O   
1177 N N   . GLY A 161 ? 0.24803 0.31699 0.31660 0.06298  0.00709  -0.02645 168 GLY A N   
1178 C CA  . GLY A 161 ? 0.26922 0.35964 0.34472 0.06270  0.01526  -0.02890 168 GLY A CA  
1179 C C   . GLY A 161 ? 0.24026 0.32100 0.30372 0.06437  0.02132  -0.03332 168 GLY A C   
1180 O O   . GLY A 161 ? 0.25996 0.36054 0.32759 0.06489  0.02973  -0.03275 168 GLY A O   
1181 N N   . SER A 162 ? 0.24065 0.29399 0.29020 0.06515  0.01714  -0.03699 169 SER A N   
1182 C CA  . SER A 162 ? 0.22795 0.27374 0.26432 0.06851  0.02047  -0.04331 169 SER A CA  
1183 C C   . SER A 162 ? 0.25470 0.27748 0.28143 0.05877  0.01535  -0.04336 169 SER A C   
1184 O O   . SER A 162 ? 0.25952 0.26800 0.28898 0.05301  0.00928  -0.03965 169 SER A O   
1185 C CB  . SER A 162 ? 0.28337 0.32197 0.31404 0.08592  0.01907  -0.05347 169 SER A CB  
1186 O OG  . SER A 162 ? 0.32515 0.33660 0.35583 0.08839  0.00955  -0.05563 169 SER A OG  
1187 N N   . PHE A 163 ? 0.28513 0.30773 0.30080 0.05784  0.01829  -0.04645 170 PHE A N   
1188 C CA  . PHE A 163 ? 0.28070 0.28498 0.28788 0.05104  0.01273  -0.04817 170 PHE A CA  
1189 C C   . PHE A 163 ? 0.29162 0.29257 0.28383 0.06022  0.01152  -0.05878 170 PHE A C   
1190 O O   . PHE A 163 ? 0.29460 0.31144 0.28066 0.07079  0.01802  -0.06232 170 PHE A O   
1191 C CB  . PHE A 163 ? 0.26583 0.27567 0.27464 0.03856  0.01598  -0.03941 170 PHE A CB  
1192 C CG  . PHE A 163 ? 0.26691 0.29497 0.27272 0.03884  0.02497  -0.03514 170 PHE A CG  
1193 C CD1 . PHE A 163 ? 0.28957 0.33616 0.30751 0.03652  0.03205  -0.02878 170 PHE A CD1 
1194 C CD2 . PHE A 163 ? 0.26173 0.28951 0.25410 0.04077  0.02591  -0.03602 170 PHE A CD2 
1195 C CE1 . PHE A 163 ? 0.26243 0.32535 0.28113 0.03509  0.04126  -0.02161 170 PHE A CE1 
1196 C CE2 . PHE A 163 ? 0.31319 0.35789 0.30255 0.04138  0.03520  -0.02834 170 PHE A CE2 
1197 C CZ  . PHE A 163 ? 0.26241 0.32382 0.26597 0.03790  0.04355  -0.02017 170 PHE A CZ  
1198 N N   . THR A 164 ? 0.27986 0.26244 0.26655 0.05660  0.00286  -0.06426 171 THR A N   
1199 C CA  . THR A 164 ? 0.27939 0.25855 0.25038 0.06466  -0.00136 -0.07681 171 THR A CA  
1200 C C   . THR A 164 ? 0.27939 0.26159 0.24355 0.05665  -0.00329 -0.07320 171 THR A C   
1201 O O   . THR A 164 ? 0.28491 0.26315 0.25882 0.04458  -0.00456 -0.06396 171 THR A O   
1202 C CB  . THR A 164 ? 0.34066 0.29434 0.31266 0.06921  -0.01334 -0.09063 171 THR A CB  
1203 O OG1 . THR A 164 ? 0.39506 0.33182 0.37933 0.05549  -0.02113 -0.08535 171 THR A OG1 
1204 C CG2 . THR A 164 ? 0.35670 0.30518 0.33544 0.08002  -0.01199 -0.09396 171 THR A CG2 
1205 N N   . VAL A 165 ? 0.30789 0.29915 0.25410 0.06535  -0.00339 -0.08053 172 VAL A N   
1206 C CA  . VAL A 165 ? 0.37042 0.36580 0.30780 0.06107  -0.00719 -0.07831 172 VAL A CA  
1207 C C   . VAL A 165 ? 0.37606 0.36661 0.29658 0.07083  -0.01804 -0.09669 172 VAL A C   
1208 O O   . VAL A 165 ? 0.37881 0.37550 0.28486 0.08531  -0.01569 -0.10752 172 VAL A O   
1209 C CB  . VAL A 165 ? 0.33887 0.35620 0.26917 0.06192  0.00497  -0.06403 172 VAL A CB  
1210 C CG1 . VAL A 165 ? 0.38926 0.41098 0.30845 0.06078  -0.00000 -0.06148 172 VAL A CG1 
1211 C CG2 . VAL A 165 ? 0.29423 0.31360 0.24283 0.05115  0.01319  -0.04901 172 VAL A CG2 
1212 N N   . ARG A 166 ? 0.32761 0.30889 0.25076 0.06348  -0.03039 -0.10128 173 ARG A N   
1213 C CA  . ARG A 166 ? 0.36864 0.34597 0.27725 0.07074  -0.04397 -0.12050 173 ARG A CA  
1214 C C   . ARG A 166 ? 0.37186 0.35707 0.28004 0.06341  -0.05174 -0.11618 173 ARG A C   
1215 O O   . ARG A 166 ? 0.36056 0.34691 0.28495 0.05145  -0.04864 -0.10078 173 ARG A O   
1216 C CB  . ARG A 166 ? 0.43211 0.38226 0.35322 0.06851  -0.05690 -0.13675 173 ARG A CB  
1217 C CG  . ARG A 166 ? 0.43015 0.36518 0.37886 0.05039  -0.06254 -0.12737 173 ARG A CG  
1218 C CD  . ARG A 166 ? 0.64884 0.55597 0.61342 0.04828  -0.06997 -0.13597 173 ARG A CD  
1219 N NE  . ARG A 166 ? 0.59895 0.50355 0.57010 0.05103  -0.05808 -0.12499 173 ARG A NE  
1220 C CZ  . ARG A 166 ? 0.70920 0.59248 0.68954 0.05502  -0.06100 -0.13031 173 ARG A CZ  
1221 N NH1 . ARG A 166 ? 0.63926 0.49769 0.62450 0.05613  -0.07515 -0.14719 173 ARG A NH1 
1222 N NH2 . ARG A 166 ? 0.59569 0.48212 0.58151 0.05828  -0.05048 -0.11870 173 ARG A NH2 
1223 N N   . THR A 167 ? 0.40811 0.40061 0.29679 0.07233  -0.06227 -0.13072 174 THR A N   
1224 C CA  . THR A 167 ? 0.42932 0.42863 0.32054 0.06586  -0.07436 -0.13051 174 THR A CA  
1225 C C   . THR A 167 ? 0.49569 0.47522 0.41619 0.05007  -0.08676 -0.13518 174 THR A C   
1226 O O   . THR A 167 ? 0.47121 0.42963 0.39987 0.04892  -0.09429 -0.14961 174 THR A O   
1227 C CB  . THR A 167 ? 0.52357 0.53499 0.38706 0.07961  -0.08616 -0.14871 174 THR A CB  
1228 O OG1 . THR A 167 ? 0.54402 0.57773 0.38017 0.09452  -0.07229 -0.13982 174 THR A OG1 
1229 C CG2 . THR A 167 ? 0.62418 0.64523 0.49282 0.07301  -0.10116 -0.14932 174 THR A CG2 
1230 N N   . ASP A 168 ? 0.43350 0.41992 0.37154 0.03832  -0.08790 -0.12150 175 ASP A N   
1231 C CA  . ASP A 168 ? 0.47152 0.44442 0.44016 0.02254  -0.09695 -0.12154 175 ASP A CA  
1232 C C   . ASP A 168 ? 0.59503 0.56818 0.56783 0.01961  -0.11832 -0.13980 175 ASP A C   
1233 O O   . ASP A 168 ? 0.57182 0.56544 0.53461 0.02350  -0.12519 -0.14082 175 ASP A O   
1234 C CB  . ASP A 168 ? 0.44822 0.43139 0.43524 0.01252  -0.08838 -0.09999 175 ASP A CB  
1235 C CG  . ASP A 168 ? 0.55831 0.53198 0.57762 -0.00325 -0.09474 -0.09681 175 ASP A CG  
1236 O OD1 . ASP A 168 ? 0.64152 0.59423 0.67117 -0.00760 -0.09768 -0.10297 175 ASP A OD1 
1237 O OD2 . ASP A 168 ? 0.53996 0.52796 0.57539 -0.01062 -0.09645 -0.08711 175 ASP A OD2 
1238 N N   . THR A 169 ? 0.80761 0.75768 0.79651 0.01273  -0.12975 -0.15397 176 THR A N   
1239 C CA  . THR A 169 ? 0.85420 0.80052 0.85451 0.00627  -0.15232 -0.17297 176 THR A CA  
1240 C C   . THR A 169 ? 0.87755 0.82856 0.91586 -0.01341 -0.15820 -0.16097 176 THR A C   
1241 O O   . THR A 169 ? 0.83649 0.79209 0.88905 -0.02097 -0.17741 -0.17378 176 THR A O   
1242 C CB  . THR A 169 ? 0.89415 0.80952 0.89618 0.00824  -0.16274 -0.19515 176 THR A CB  
1243 O OG1 . THR A 169 ? 0.83964 0.73348 0.85851 0.00264  -0.15087 -0.18241 176 THR A OG1 
1244 C CG2 . THR A 169 ? 0.84847 0.76787 0.81224 0.02985  -0.15943 -0.20991 176 THR A CG2 
1245 N N   . GLY A 170 ? 0.75419 0.70695 0.80940 -0.02131 -0.14241 -0.13732 177 GLY A N   
1246 C CA  . GLY A 170 ? 0.84251 0.80098 0.93480 -0.03896 -0.14487 -0.12411 177 GLY A CA  
1247 C C   . GLY A 170 ? 0.66836 0.65819 0.76841 -0.04139 -0.14978 -0.11780 177 GLY A C   
1248 O O   . GLY A 170 ? 0.59655 0.60138 0.67581 -0.03130 -0.15874 -0.12879 177 GLY A O   
1249 N N   . GLU A 171 ? 0.63273 0.63465 0.76220 -0.05323 -0.14351 -0.09924 178 GLU A N   
1250 C CA  . GLU A 171 ? 0.62507 0.65838 0.76860 -0.05575 -0.14844 -0.09234 178 GLU A CA  
1251 C C   . GLU A 171 ? 0.54681 0.59734 0.66051 -0.03918 -0.13879 -0.08564 178 GLU A C   
1252 O O   . GLU A 171 ? 0.48849 0.53233 0.58700 -0.03238 -0.12078 -0.07414 178 GLU A O   
1253 C CB  . GLU A 171 ? 0.58012 0.62444 0.75992 -0.06929 -0.13958 -0.07205 178 GLU A CB  
1254 C CG  . GLU A 171 ? 0.72667 0.79159 0.94397 -0.08330 -0.15534 -0.07342 178 GLU A CG  
1255 C CD  . GLU A 171 ? 0.58994 0.63517 0.82277 -0.09500 -0.17600 -0.09299 178 GLU A CD  
1256 O OE1 . GLU A 171 ? 0.75301 0.80646 0.97724 -0.09158 -0.19314 -0.11069 178 GLU A OE1 
1257 O OE2 . GLU A 171 ? 0.78044 0.80071 1.02813 -0.10506 -0.17172 -0.08886 178 GLU A OE2 
1258 N N   . PRO A 172 ? 0.47792 0.55006 0.58322 -0.03235 -0.15098 -0.09214 179 PRO A N   
1259 C CA  . PRO A 172 ? 0.50608 0.59457 0.58763 -0.01720 -0.14126 -0.08109 179 PRO A CA  
1260 C C   . PRO A 172 ? 0.61662 0.71546 0.71625 -0.01949 -0.12553 -0.05947 179 PRO A C   
1261 O O   . PRO A 172 ? 0.59614 0.70603 0.72900 -0.03099 -0.12746 -0.05321 179 PRO A O   
1262 C CB  . PRO A 172 ? 0.52916 0.64209 0.60701 -0.01188 -0.16065 -0.09078 179 PRO A CB  
1263 C CG  . PRO A 172 ? 0.62393 0.72495 0.70562 -0.01917 -0.18033 -0.11495 179 PRO A CG  
1264 C CD  . PRO A 172 ? 0.61380 0.69304 0.72596 -0.03626 -0.17557 -0.11230 179 PRO A CD  
1265 N N   . MET A 173 ? 0.42216 0.51782 0.50031 -0.00814 -0.10967 -0.04837 180 MET A N   
1266 C CA  . MET A 173 ? 0.46642 0.56680 0.55588 -0.00745 -0.09382 -0.03096 180 MET A CA  
1267 C C   . MET A 173 ? 0.49230 0.61331 0.57932 0.00393  -0.09284 -0.02067 180 MET A C   
1268 O O   . MET A 173 ? 0.61018 0.74092 0.71504 0.00399  -0.08443 -0.00915 180 MET A O   
1269 C CB  . MET A 173 ? 0.44493 0.52346 0.51673 -0.00425 -0.07707 -0.02644 180 MET A CB  
1270 C CG  . MET A 173 ? 0.60101 0.66254 0.68422 -0.01517 -0.07288 -0.02865 180 MET A CG  
1271 S SD  . MET A 173 ? 0.61885 0.65935 0.67749 -0.00900 -0.05821 -0.02730 180 MET A SD  
1272 C CE  . MET A 173 ? 0.52320 0.57334 0.56733 0.00312  -0.04969 -0.01685 180 MET A CE  
1273 N N   . GLY A 174 ? 0.38087 0.50937 0.44587 0.01498  -0.10082 -0.02392 181 GLY A N   
1274 C CA  . GLY A 174 ? 0.37476 0.51975 0.43539 0.02776  -0.09916 -0.01158 181 GLY A CA  
1275 C C   . GLY A 174 ? 0.28562 0.41410 0.32521 0.03722  -0.08220 -0.00003 181 GLY A C   
1276 O O   . GLY A 174 ? 0.36063 0.48951 0.37524 0.04829  -0.08232 0.00362  181 GLY A O   
1277 N N   . ARG A 175 ? 0.25031 0.36491 0.30036 0.03253  -0.06774 0.00589  182 ARG A N   
1278 C CA  . ARG A 175 ? 0.28105 0.37785 0.31725 0.03839  -0.05237 0.01511  182 ARG A CA  
1279 C C   . ARG A 175 ? 0.29287 0.37718 0.34283 0.03062  -0.04087 0.01560  182 ARG A C   
1280 O O   . ARG A 175 ? 0.26569 0.36083 0.33705 0.02758  -0.04057 0.01731  182 ARG A O   
1281 C CB  . ARG A 175 ? 0.25279 0.35604 0.28702 0.05155  -0.04936 0.02896  182 ARG A CB  
1282 C CG  . ARG A 175 ? 0.33087 0.41271 0.35210 0.05621  -0.03512 0.03843  182 ARG A CG  
1283 C CD  . ARG A 175 ? 0.30103 0.38135 0.32927 0.06733  -0.02981 0.05201  182 ARG A CD  
1284 N NE  . ARG A 175 ? 0.25398 0.34010 0.30554 0.06646  -0.02773 0.05015  182 ARG A NE  
1285 C CZ  . ARG A 175 ? 0.25979 0.36835 0.32708 0.07259  -0.03490 0.05271  182 ARG A CZ  
1286 N NH1 . ARG A 175 ? 0.27922 0.40632 0.34171 0.08004  -0.04659 0.05671  182 ARG A NH1 
1287 N NH2 . ARG A 175 ? 0.25631 0.37202 0.34467 0.07219  -0.03028 0.05132  182 ARG A NH2 
1288 N N   . GLY A 176 ? 0.32927 0.35823 0.24065 0.07649  -0.01785 0.05978  183 GLY A N   
1289 C CA  . GLY A 176 ? 0.30084 0.31685 0.23845 0.06784  -0.00741 0.05320  183 GLY A CA  
1290 C C   . GLY A 176 ? 0.31272 0.32174 0.25368 0.05124  -0.00453 0.03617  183 GLY A C   
1291 O O   . GLY A 176 ? 0.33482 0.34130 0.25539 0.04932  -0.00380 0.03105  183 GLY A O   
1292 N N   . THR A 177 ? 0.25559 0.26196 0.22019 0.04214  -0.00178 0.02850  184 THR A N   
1293 C CA  . THR A 177 ? 0.29279 0.29421 0.26349 0.02990  0.00169  0.01601  184 THR A CA  
1294 C C   . THR A 177 ? 0.31683 0.32725 0.30932 0.02218  -0.00630 0.00710  184 THR A C   
1295 O O   . THR A 177 ? 0.27780 0.29277 0.28475 0.02398  -0.00638 0.01139  184 THR A O   
1296 C CB  . THR A 177 ? 0.34363 0.32787 0.31601 0.02391  0.01743  0.01964  184 THR A CB  
1297 O OG1 . THR A 177 ? 0.34099 0.31558 0.29304 0.02870  0.02707  0.03049  184 THR A OG1 
1298 C CG2 . THR A 177 ? 0.37333 0.36415 0.35675 0.01429  0.01946  0.01010  184 THR A CG2 
1299 N N   . LYS A 178 ? 0.26833 0.27848 0.26029 0.01571  -0.01051 -0.00396 185 LYS A N   
1300 C CA  . LYS A 178 ? 0.27984 0.29201 0.28787 0.00748  -0.01639 -0.01103 185 LYS A CA  
1301 C C   . LYS A 178 ? 0.24733 0.25112 0.25910 0.00515  -0.00846 -0.01525 185 LYS A C   
1302 O O   . LYS A 178 ? 0.30004 0.29946 0.30017 0.00938  -0.00477 -0.01926 185 LYS A O   
1303 C CB  . LYS A 178 ? 0.35195 0.36564 0.35139 0.00235  -0.03043 -0.01921 185 LYS A CB  
1304 C CG  . LYS A 178 ? 0.38321 0.38898 0.39232 -0.00794 -0.03519 -0.02625 185 LYS A CG  
1305 C CD  . LYS A 178 ? 0.58447 0.58587 0.58089 -0.01832 -0.05071 -0.03485 185 LYS A CD  
1306 C CE  . LYS A 178 ? 0.49895 0.52923 0.49987 -0.01993 -0.06263 -0.02802 185 LYS A CE  
1307 N NZ  . LYS A 178 ? 0.76257 0.79441 0.75253 -0.03626 -0.08230 -0.03684 185 LYS A NZ  
1308 N N   . VAL A 179 ? 0.25893 0.26333 0.28545 0.00040  -0.00549 -0.01342 186 VAL A N   
1309 C CA  . VAL A 179 ? 0.25054 0.25531 0.28356 -0.00188 -0.00183 -0.01521 186 VAL A CA  
1310 C C   . VAL A 179 ? 0.28321 0.28385 0.32177 -0.00411 -0.00794 -0.01840 186 VAL A C   
1311 O O   . VAL A 179 ? 0.26564 0.26728 0.31127 -0.00896 -0.00983 -0.01602 186 VAL A O   
1312 C CB  . VAL A 179 ? 0.24351 0.24956 0.28212 -0.00828 0.00360  -0.01125 186 VAL A CB  
1313 C CG1 . VAL A 179 ? 0.23004 0.24698 0.27827 -0.01170 0.00292  -0.01146 186 VAL A CG1 
1314 C CG2 . VAL A 179 ? 0.26283 0.26514 0.29390 -0.00913 0.01129  -0.00648 186 VAL A CG2 
1315 N N   . ILE A 180 ? 0.26669 0.25947 0.29953 0.00096  -0.00862 -0.02258 187 ILE A N   
1316 C CA  . ILE A 180 ? 0.27113 0.24978 0.30401 -0.00067 -0.01294 -0.02420 187 ILE A CA  
1317 C C   . ILE A 180 ? 0.24949 0.23409 0.29007 0.00550  -0.00929 -0.01895 187 ILE A C   
1318 O O   . ILE A 180 ? 0.25630 0.24694 0.29665 0.01660  -0.00420 -0.01830 187 ILE A O   
1319 C CB  . ILE A 180 ? 0.27774 0.23221 0.29160 0.00200  -0.01617 -0.03300 187 ILE A CB  
1320 C CG1 . ILE A 180 ? 0.34383 0.30085 0.34905 -0.00558 -0.02381 -0.03757 187 ILE A CG1 
1321 C CG2 . ILE A 180 ? 0.32363 0.25355 0.33478 -0.00256 -0.01951 -0.03338 187 ILE A CG2 
1322 C CD1 . ILE A 180 ? 0.41512 0.34607 0.39151 -0.00452 -0.02840 -0.04957 187 ILE A CD1 
1323 N N   . LEU A 181 ? 0.23196 0.21927 0.27926 -0.00024 -0.01159 -0.01365 188 LEU A N   
1324 C CA  . LEU A 181 ? 0.26553 0.26254 0.31788 0.00489  -0.01180 -0.00688 188 LEU A CA  
1325 C C   . LEU A 181 ? 0.30012 0.27425 0.34534 0.01152  -0.01269 -0.00338 188 LEU A C   
1326 O O   . LEU A 181 ? 0.28536 0.24516 0.32698 0.00294  -0.01426 -0.00098 188 LEU A O   
1327 C CB  . LEU A 181 ? 0.21355 0.22196 0.26761 -0.00473 -0.01374 -0.00353 188 LEU A CB  
1328 C CG  . LEU A 181 ? 0.22383 0.23983 0.27796 -0.01267 -0.01135 -0.00745 188 LEU A CG  
1329 C CD1 . LEU A 181 ? 0.31693 0.33124 0.36246 -0.02046 -0.01177 -0.00695 188 LEU A CD1 
1330 C CD2 . LEU A 181 ? 0.27573 0.30961 0.33761 -0.01217 -0.01027 -0.00691 188 LEU A CD2 
1331 N N   . HIS A 182 ? 0.27936 0.24892 0.32224 0.02785  -0.00962 -0.00141 189 HIS A N   
1332 C CA  . HIS A 182 ? 0.32143 0.26206 0.35367 0.03848  -0.00857 0.00442  189 HIS A CA  
1333 C C   . HIS A 182 ? 0.29287 0.25613 0.33321 0.04369  -0.01211 0.01824  189 HIS A C   
1334 O O   . HIS A 182 ? 0.28660 0.28036 0.33879 0.05690  -0.01255 0.02490  189 HIS A O   
1335 C CB  . HIS A 182 ? 0.33385 0.25432 0.35492 0.05921  -0.00121 0.00073  189 HIS A CB  
1336 C CG  . HIS A 182 ? 0.35585 0.25739 0.36217 0.05399  0.00079  -0.01429 189 HIS A CG  
1337 N ND1 . HIS A 182 ? 0.50215 0.35397 0.48299 0.04874  -0.00033 -0.02419 189 HIS A ND1 
1338 C CD2 . HIS A 182 ? 0.43341 0.35773 0.44325 0.05154  0.00271  -0.02048 189 HIS A CD2 
1339 C CE1 . HIS A 182 ? 0.47177 0.32008 0.43990 0.04398  -0.00111 -0.03685 189 HIS A CE1 
1340 N NE2 . HIS A 182 ? 0.46043 0.35219 0.44557 0.04740  0.00178  -0.03359 189 HIS A NE2 
1341 N N   . LEU A 183 ? 0.29090 0.24410 0.32502 0.03269  -0.01494 0.02375  190 LEU A N   
1342 C CA  . LEU A 183 ? 0.28626 0.26380 0.32133 0.03287  -0.02023 0.03455  190 LEU A CA  
1343 C C   . LEU A 183 ? 0.35413 0.33089 0.38583 0.05428  -0.02164 0.04952  190 LEU A C   
1344 O O   . LEU A 183 ? 0.34748 0.28686 0.36865 0.06712  -0.01580 0.05359  190 LEU A O   
1345 C CB  . LEU A 183 ? 0.29144 0.25679 0.31587 0.01790  -0.01917 0.03722  190 LEU A CB  
1346 C CG  . LEU A 183 ? 0.29483 0.26788 0.32399 0.00180  -0.01683 0.02631  190 LEU A CG  
1347 C CD1 . LEU A 183 ? 0.33310 0.29965 0.35371 -0.00793 -0.01197 0.03204  190 LEU A CD1 
1348 C CD2 . LEU A 183 ? 0.33706 0.33775 0.37091 -0.00112 -0.02056 0.01982  190 LEU A CD2 
1349 N N   . LYS A 184 ? 0.33247 0.34949 0.37110 0.05811  -0.03023 0.05814  191 LYS A N   
1350 C CA  . LYS A 184 ? 0.35782 0.38273 0.39326 0.07961  -0.03425 0.07679  191 LYS A CA  
1351 C C   . LYS A 184 ? 0.40468 0.39110 0.41506 0.07847  -0.03182 0.08750  191 LYS A C   
1352 O O   . LYS A 184 ? 0.37909 0.35351 0.37856 0.05831  -0.03004 0.08220  191 LYS A O   
1353 C CB  . LYS A 184 ? 0.33905 0.42291 0.38685 0.07811  -0.04850 0.08383  191 LYS A CB  
1354 C CG  . LYS A 184 ? 0.35458 0.48360 0.43162 0.07580  -0.05050 0.07741  191 LYS A CG  
1355 C CD  . LYS A 184 ? 0.30760 0.48764 0.39229 0.05723  -0.06714 0.07821  191 LYS A CD  
1356 C CE  . LYS A 184 ? 0.54505 0.77961 0.66502 0.05560  -0.06979 0.07905  191 LYS A CE  
1357 N NZ  . LYS A 184 ? 0.52388 0.80142 0.64924 0.02797  -0.08735 0.07623  191 LYS A NZ  
1358 N N   . GLU A 185 ? 0.40460 0.37197 0.40574 0.10243  -0.02969 0.10494  192 GLU A N   
1359 C CA  . GLU A 185 ? 0.50925 0.42980 0.48451 0.10219  -0.02400 0.11809  192 GLU A CA  
1360 C C   . GLU A 185 ? 0.51454 0.45473 0.47491 0.08830  -0.03039 0.12575  192 GLU A C   
1361 O O   . GLU A 185 ? 0.58187 0.48923 0.52428 0.07601  -0.02233 0.13084  192 GLU A O   
1362 C CB  . GLU A 185 ? 0.57732 0.47278 0.54238 0.13528  -0.02035 0.13833  192 GLU A CB  
1363 C CG  . GLU A 185 ? 0.83885 0.72054 0.77918 0.14381  -0.02219 0.16325  192 GLU A CG  
1364 C CD  . GLU A 185 ? 1.10552 0.94810 1.03211 0.17944  -0.01529 0.18441  192 GLU A CD  
1365 O OE1 . GLU A 185 ? 1.12439 0.93190 1.02577 0.18095  -0.01166 0.20126  192 GLU A OE1 
1366 O OE2 . GLU A 185 ? 1.09137 0.94087 1.03356 0.20075  -0.01228 0.17887  192 GLU A OE2 
1367 N N   . ASP A 186 ? 0.48413 0.47723 0.44960 0.08811  -0.04423 0.12628  193 ASP A N   
1368 C CA  . ASP A 186 ? 0.53096 0.53868 0.47249 0.07618  -0.05096 0.13095  193 ASP A CA  
1369 C C   . ASP A 186 ? 0.45950 0.47931 0.40125 0.05023  -0.05073 0.10915  193 ASP A C   
1370 O O   . ASP A 186 ? 0.43537 0.47125 0.35459 0.04068  -0.05783 0.10764  193 ASP A O   
1371 C CB  . ASP A 186 ? 0.50439 0.55805 0.44166 0.09057  -0.06931 0.14602  193 ASP A CB  
1372 C CG  . ASP A 186 ? 0.62172 0.73022 0.58911 0.08600  -0.08277 0.13484  193 ASP A CG  
1373 O OD1 . ASP A 186 ? 0.60565 0.71114 0.59682 0.07845  -0.07521 0.11844  193 ASP A OD1 
1374 O OD2 . ASP A 186 ? 0.80483 0.96193 0.77177 0.08837  -0.10166 0.14378  193 ASP A OD2 
1375 N N   . GLN A 187 ? 0.38071 0.38912 0.34237 0.04037  -0.04239 0.09250  194 GLN A N   
1376 C CA  . GLN A 187 ? 0.34291 0.35788 0.30520 0.02065  -0.04002 0.07394  194 GLN A CA  
1377 C C   . GLN A 187 ? 0.32229 0.30746 0.28676 0.01126  -0.02486 0.06889  194 GLN A C   
1378 O O   . GLN A 187 ? 0.34952 0.33770 0.32411 0.00091  -0.02085 0.05448  194 GLN A O   
1379 C CB  . GLN A 187 ? 0.35929 0.39976 0.34576 0.01685  -0.04617 0.06060  194 GLN A CB  
1380 C CG  . GLN A 187 ? 0.32601 0.40925 0.31858 0.02021  -0.06256 0.06572  194 GLN A CG  
1381 C CD  . GLN A 187 ? 0.36059 0.45611 0.32428 0.00750  -0.07363 0.06431  194 GLN A CD  
1382 O OE1 . GLN A 187 ? 0.42740 0.50336 0.37064 -0.00717 -0.06775 0.05145  194 GLN A OE1 
1383 N NE2 . GLN A 187 ? 0.34129 0.46954 0.30055 0.01472  -0.08987 0.07757  194 GLN A NE2 
1384 N N   . THR A 188 ? 0.43221 0.39045 0.38819 0.01397  -0.01663 0.08262  195 THR A N   
1385 C CA  . THR A 188 ? 0.41663 0.35457 0.38112 0.00128  -0.00423 0.08035  195 THR A CA  
1386 C C   . THR A 188 ? 0.43173 0.37976 0.38644 -0.00897 0.00544  0.07947  195 THR A C   
1387 O O   . THR A 188 ? 0.40910 0.35351 0.37762 -0.01960 0.01575  0.07927  195 THR A O   
1388 C CB  . THR A 188 ? 0.47906 0.38092 0.43797 0.00283  0.00196  0.09619  195 THR A CB  
1389 O OG1 . THR A 188 ? 0.52647 0.42368 0.45963 0.01126  0.00320  0.11544  195 THR A OG1 
1390 C CG2 . THR A 188 ? 0.48141 0.36287 0.44742 0.01538  -0.00314 0.09370  195 THR A CG2 
1391 N N   . GLU A 189 ? 0.42622 0.38797 0.35635 -0.00570 0.00254  0.07901  196 GLU A N   
1392 C CA  . GLU A 189 ? 0.45220 0.41880 0.36726 -0.01111 0.01473  0.07491  196 GLU A CA  
1393 C C   . GLU A 189 ? 0.39213 0.36649 0.32844 -0.01632 0.01893  0.05853  196 GLU A C   
1394 O O   . GLU A 189 ? 0.40231 0.38035 0.33917 -0.01787 0.03370  0.05833  196 GLU A O   
1395 C CB  . GLU A 189 ? 0.44158 0.41400 0.31750 -0.00753 0.00821  0.07224  196 GLU A CB  
1396 C CG  . GLU A 189 ? 0.45585 0.44057 0.33273 -0.01083 -0.00758 0.05482  196 GLU A CG  
1397 C CD  . GLU A 189 ? 0.59547 0.58653 0.43208 -0.01229 -0.01985 0.05234  196 GLU A CD  
1398 O OE1 . GLU A 189 ? 0.56520 0.57073 0.39783 -0.00683 -0.03497 0.06407  196 GLU A OE1 
1399 O OE2 . GLU A 189 ? 0.52019 0.50071 0.32672 -0.01805 -0.01495 0.03867  196 GLU A OE2 
1400 N N   . TYR A 190 ? 0.32905 0.30806 0.28325 -0.01667 0.00778  0.04724  197 TYR A N   
1401 C CA  . TYR A 190 ? 0.33179 0.31580 0.30253 -0.01977 0.01093  0.03411  197 TYR A CA  
1402 C C   . TYR A 190 ? 0.32913 0.31465 0.32862 -0.02383 0.01612  0.03715  197 TYR A C   
1403 O O   . TYR A 190 ? 0.34821 0.34075 0.36299 -0.02459 0.01658  0.02877  197 TYR A O   
1404 C CB  . TYR A 190 ? 0.31870 0.30836 0.29445 -0.02015 -0.00168 0.02313  197 TYR A CB  
1405 C CG  . TYR A 190 ? 0.30611 0.29914 0.25488 -0.02252 -0.00965 0.01905  197 TYR A CG  
1406 C CD1 . TYR A 190 ? 0.38514 0.36677 0.30648 -0.02591 -0.00299 0.01012  197 TYR A CD1 
1407 C CD2 . TYR A 190 ? 0.37734 0.38466 0.32537 -0.02074 -0.02400 0.02456  197 TYR A CD2 
1408 C CE1 . TYR A 190 ? 0.40639 0.38583 0.29588 -0.03239 -0.01260 0.00366  197 TYR A CE1 
1409 C CE2 . TYR A 190 ? 0.34503 0.36185 0.26865 -0.02689 -0.03541 0.02106  197 TYR A CE2 
1410 C CZ  . TYR A 190 ? 0.35952 0.35970 0.25143 -0.03517 -0.03067 0.00911  197 TYR A CZ  
1411 O OH  . TYR A 190 ? 0.43142 0.43541 0.29193 -0.04549 -0.04422 0.00261  197 TYR A OH  
1412 N N   . LEU A 191 ? 0.31599 0.29368 0.32074 -0.02806 0.01898  0.04968  198 LEU A N   
1413 C CA  . LEU A 191 ? 0.31305 0.29402 0.34243 -0.03860 0.02329  0.05364  198 LEU A CA  
1414 C C   . LEU A 191 ? 0.35647 0.35360 0.39070 -0.04322 0.03900  0.06545  198 LEU A C   
1415 O O   . LEU A 191 ? 0.36658 0.37904 0.42765 -0.05445 0.04230  0.07025  198 LEU A O   
1416 C CB  . LEU A 191 ? 0.38338 0.33864 0.41448 -0.04481 0.01760  0.05974  198 LEU A CB  
1417 C CG  . LEU A 191 ? 0.35778 0.29782 0.38542 -0.03622 0.00596  0.04969  198 LEU A CG  
1418 C CD1 . LEU A 191 ? 0.43653 0.33988 0.45690 -0.03755 0.00425  0.05639  198 LEU A CD1 
1419 C CD2 . LEU A 191 ? 0.41159 0.36386 0.45487 -0.03889 0.00097  0.03528  198 LEU A CD2 
1420 N N   . GLU A 192 ? 0.33661 0.33374 0.34493 -0.03527 0.04865  0.07079  199 GLU A N   
1421 C CA  . GLU A 192 ? 0.37907 0.39098 0.38687 -0.03648 0.06788  0.08481  199 GLU A CA  
1422 C C   . GLU A 192 ? 0.35722 0.39228 0.37357 -0.02707 0.07934  0.07814  199 GLU A C   
1423 O O   . GLU A 192 ? 0.33927 0.36427 0.33462 -0.01606 0.07665  0.06370  199 GLU A O   
1424 C CB  . GLU A 192 ? 0.42935 0.42685 0.39591 -0.02920 0.07406  0.09323  199 GLU A CB  
1425 C CG  . GLU A 192 ? 0.42834 0.40271 0.38475 -0.03375 0.06597  0.10601  199 GLU A CG  
1426 C CD  . GLU A 192 ? 0.94266 0.91326 0.92170 -0.04963 0.07483  0.12379  199 GLU A CD  
1427 O OE1 . GLU A 192 ? 0.94696 0.94253 0.94530 -0.05717 0.09095  0.13214  199 GLU A OE1 
1428 O OE2 . GLU A 192 ? 0.93450 0.87647 0.91204 -0.05477 0.06641  0.13023  199 GLU A OE2 
1429 N N   . GLU A 193 ? 0.36731 0.40510 0.39407 -0.03377 -0.00097 0.07895  200 GLU A N   
1430 C CA  . GLU A 193 ? 0.31473 0.37917 0.34850 -0.03551 0.00609  0.06817  200 GLU A CA  
1431 C C   . GLU A 193 ? 0.28552 0.37974 0.30579 -0.02613 0.01476  0.06486  200 GLU A C   
1432 O O   . GLU A 193 ? 0.30327 0.40423 0.31973 -0.01902 0.01705  0.04760  200 GLU A O   
1433 C CB  . GLU A 193 ? 0.30654 0.38329 0.35774 -0.05155 0.00817  0.08072  200 GLU A CB  
1434 C CG  . GLU A 193 ? 0.44918 0.55678 0.50853 -0.04890 0.01561  0.07093  200 GLU A CG  
1435 C CD  . GLU A 193 ? 0.69274 0.82821 0.77333 -0.06361 0.01892  0.08670  200 GLU A CD  
1436 O OE1 . GLU A 193 ? 0.52765 0.68370 0.61983 -0.06192 0.02103  0.07894  200 GLU A OE1 
1437 O OE2 . GLU A 193 ? 0.49176 0.63126 0.57889 -0.07705 0.01933  0.10896  200 GLU A OE2 
1438 N N   . ARG A 194 ? 0.35384 0.46314 0.36376 -0.02565 0.01891  0.08125  201 ARG A N   
1439 C CA  . ARG A 194 ? 0.32975 0.46640 0.32109 -0.01540 0.02609  0.07570  201 ARG A CA  
1440 C C   . ARG A 194 ? 0.34159 0.46996 0.31922 -0.00604 0.01888  0.05793  201 ARG A C   
1441 O O   . ARG A 194 ? 0.31928 0.45844 0.28321 0.00054  0.02110  0.04277  201 ARG A O   
1442 C CB  . ARG A 194 ? 0.40352 0.56155 0.38334 -0.01555 0.03231  0.09879  201 ARG A CB  
1443 C CG  . ARG A 194 ? 0.38825 0.53213 0.35730 -0.01297 0.02455  0.11154  201 ARG A CG  
1444 C CD  . ARG A 194 ? 0.44632 0.61278 0.40406 -0.01404 0.03231  0.13909  201 ARG A CD  
1445 N NE  . ARG A 194 ? 0.62869 0.77856 0.57686 -0.01092 0.02469  0.15640  201 ARG A NE  
1446 C CZ  . ARG A 194 ? 0.59753 0.76445 0.53029 -0.00876 0.02956  0.18216  201 ARG A CZ  
1447 N NH1 . ARG A 194 ? 0.62528 0.82953 0.55085 -0.00982 0.04332  0.19420  201 ARG A NH1 
1448 N NH2 . ARG A 194 ? 0.65938 0.80811 0.58258 -0.00287 0.02127  0.19762  201 ARG A NH2 
1449 N N   . ARG A 195 ? 0.28798 0.39735 0.26946 -0.00518 0.00964  0.05951  202 ARG A N   
1450 C CA  . ARG A 195 ? 0.29508 0.40573 0.27017 0.00140  0.00235  0.04564  202 ARG A CA  
1451 C C   . ARG A 195 ? 0.26789 0.37031 0.25282 -0.00029 0.00205  0.02660  202 ARG A C   
1452 O O   . ARG A 195 ? 0.29502 0.40401 0.27279 0.00049  -0.00032 0.01284  202 ARG A O   
1453 C CB  . ARG A 195 ? 0.28336 0.38343 0.26164 0.00676  -0.00580 0.05558  202 ARG A CB  
1454 C CG  . ARG A 195 ? 0.29204 0.40433 0.26983 0.01302  -0.01393 0.04554  202 ARG A CG  
1455 C CD  . ARG A 195 ? 0.34213 0.48012 0.30117 0.01480  -0.01796 0.04432  202 ARG A CD  
1456 N NE  . ARG A 195 ? 0.31825 0.47315 0.28117 0.01819  -0.02880 0.03900  202 ARG A NE  
1457 C CZ  . ARG A 195 ? 0.34936 0.51909 0.30878 0.01188  -0.03518 0.02309  202 ARG A CZ  
1458 N NH1 . ARG A 195 ? 0.34156 0.50462 0.28859 0.00532  -0.03165 0.00868  202 ARG A NH1 
1459 N NH2 . ARG A 195 ? 0.36126 0.55275 0.33023 0.01234  -0.04614 0.02199  202 ARG A NH2 
1460 N N   . ILE A 196 ? 0.28306 0.36924 0.28282 -0.00344 0.00317  0.02610  203 ILE A N   
1461 C CA  . ILE A 196 ? 0.28866 0.36859 0.29576 -0.00381 0.00397  0.01134  203 ILE A CA  
1462 C C   . ILE A 196 ? 0.28199 0.37024 0.28237 -0.00395 0.01032  0.00275  203 ILE A C   
1463 O O   . ILE A 196 ? 0.28884 0.37325 0.28537 -0.00304 0.00954  -0.00989 203 ILE A O   
1464 C CB  . ILE A 196 ? 0.28043 0.34316 0.29983 -0.00553 0.00289  0.01238  203 ILE A CB  
1465 C CG1 . ILE A 196 ? 0.27011 0.31763 0.29067 -0.00022 -0.00358 0.01760  203 ILE A CG1 
1466 C CG2 . ILE A 196 ? 0.22931 0.28886 0.25354 -0.00426 0.00461  -0.00018 203 ILE A CG2 
1467 C CD1 . ILE A 196 ? 0.30848 0.33127 0.33385 -0.00259 -0.00731 0.01920  203 ILE A CD1 
1468 N N   . LYS A 197 ? 0.27350 0.37308 0.27252 -0.00444 0.01691  0.01072  204 LYS A N   
1469 C CA  . LYS A 197 ? 0.27884 0.38921 0.26916 0.00134  0.02454  0.00313  204 LYS A CA  
1470 C C   . LYS A 197 ? 0.36192 0.47201 0.32939 0.00706  0.02253  -0.00899 204 LYS A C   
1471 O O   . LYS A 197 ? 0.30611 0.40530 0.26453 0.01170  0.02325  -0.02384 204 LYS A O   
1472 C CB  . LYS A 197 ? 0.32876 0.46301 0.32198 0.00139  0.03320  0.01783  204 LYS A CB  
1473 C CG  . LYS A 197 ? 0.39672 0.53738 0.41242 -0.00457 0.03543  0.02493  204 LYS A CG  
1474 C CD  . LYS A 197 ? 0.41848 0.59300 0.43981 -0.00605 0.04497  0.04219  204 LYS A CD  
1475 C CE  . LYS A 197 ? 0.60405 0.79140 0.65276 -0.01679 0.04430  0.05197  204 LYS A CE  
1476 N NZ  . LYS A 197 ? 0.69386 0.90474 0.75580 -0.03029 0.04763  0.07694  204 LYS A NZ  
1477 N N   . GLU A 198 ? 0.28968 0.40928 0.24558 0.00685  0.01859  -0.00269 205 GLU A N   
1478 C CA  . GLU A 198 ? 0.27019 0.39126 0.20198 0.01060  0.01297  -0.01532 205 GLU A CA  
1479 C C   . GLU A 198 ? 0.29050 0.39374 0.22691 0.00411  0.00325  -0.03012 205 GLU A C   
1480 O O   . GLU A 198 ? 0.30052 0.39175 0.22026 0.00479  -0.00036 -0.04679 205 GLU A O   
1481 C CB  . GLU A 198 ? 0.26563 0.40336 0.18716 0.01128  0.00821  -0.00284 205 GLU A CB  
1482 C CG  . GLU A 198 ? 0.35930 0.50234 0.25589 0.01339  -0.00201 -0.01580 205 GLU A CG  
1483 C CD  . GLU A 198 ? 0.33570 0.49851 0.22409 0.01563  -0.00805 -0.00049 205 GLU A CD  
1484 O OE1 . GLU A 198 ? 0.42572 0.58755 0.33415 0.01283  -0.01097 0.01404  205 GLU A OE1 
1485 O OE2 . GLU A 198 ? 0.39097 0.56904 0.25015 0.02258  -0.01006 -0.00306 205 GLU A OE2 
1486 N N   . ILE A 199 ? 0.26902 0.36956 0.22708 -0.00206 -0.00108 -0.02366 206 ILE A N   
1487 C CA  . ILE A 199 ? 0.26545 0.35873 0.23223 -0.00960 -0.00893 -0.03249 206 ILE A CA  
1488 C C   . ILE A 199 ? 0.28061 0.35298 0.25010 -0.01115 -0.00449 -0.04228 206 ILE A C   
1489 O O   . ILE A 199 ? 0.29358 0.35302 0.25784 -0.01797 -0.01028 -0.05338 206 ILE A O   
1490 C CB  . ILE A 199 ? 0.28022 0.38197 0.26801 -0.01048 -0.01185 -0.02135 206 ILE A CB  
1491 C CG1 . ILE A 199 ? 0.30473 0.42488 0.28766 -0.00646 -0.01791 -0.01108 206 ILE A CG1 
1492 C CG2 . ILE A 199 ? 0.30307 0.40585 0.30475 -0.01815 -0.01661 -0.02645 206 ILE A CG2 
1493 C CD1 . ILE A 199 ? 0.32060 0.44268 0.31889 -0.00010 -0.01825 0.00170  206 ILE A CD1 
1494 N N   . VAL A 200 ? 0.27916 0.34703 0.25711 -0.00586 0.00438  -0.03720 207 VAL A N   
1495 C CA  . VAL A 200 ? 0.30399 0.35408 0.28336 -0.00396 0.00873  -0.04396 207 VAL A CA  
1496 C C   . VAL A 200 ? 0.36521 0.40132 0.32159 0.00210  0.00996  -0.05695 207 VAL A C   
1497 O O   . VAL A 200 ? 0.35207 0.36359 0.30236 -0.00005 0.00739  -0.06645 207 VAL A O   
1498 C CB  . VAL A 200 ? 0.29637 0.35116 0.28839 0.00131  0.01583  -0.03578 207 VAL A CB  
1499 C CG1 . VAL A 200 ? 0.35504 0.39628 0.34489 0.00779  0.02066  -0.04139 207 VAL A CG1 
1500 C CG2 . VAL A 200 ? 0.26025 0.31740 0.26880 -0.00271 0.01280  -0.02823 207 VAL A CG2 
1501 N N   . LYS A 201 ? 0.31842 0.36799 0.25933 0.01083  0.01405  -0.05703 208 LYS A N   
1502 C CA  . LYS A 201 ? 0.39971 0.43617 0.31272 0.02210  0.01609  -0.07157 208 LYS A CA  
1503 C C   . LYS A 201 ? 0.37205 0.38849 0.26573 0.01384  0.00298  -0.08703 208 LYS A C   
1504 O O   . LYS A 201 ? 0.46096 0.44640 0.33320 0.01858  0.00019  -0.10348 208 LYS A O   
1505 C CB  . LYS A 201 ? 0.39625 0.46051 0.29671 0.03475  0.02516  -0.06544 208 LYS A CB  
1506 C CG  . LYS A 201 ? 0.49580 0.55111 0.36063 0.05179  0.02827  -0.08177 208 LYS A CG  
1507 C CD  . LYS A 201 ? 0.64265 0.73513 0.50075 0.06733  0.04239  -0.07070 208 LYS A CD  
1508 C CE  . LYS A 201 ? 0.69001 0.77705 0.50605 0.08888  0.04617  -0.08829 208 LYS A CE  
1509 N NZ  . LYS A 201 ? 0.76040 0.89375 0.56765 0.10285  0.06033  -0.07407 208 LYS A NZ  
1510 N N   . LYS A 202 ? 0.38217 0.41472 0.28288 0.00163  -0.00657 -0.08209 209 LYS A N   
1511 C CA  . LYS A 202 ? 0.42458 0.44675 0.30975 -0.00914 -0.02200 -0.09583 209 LYS A CA  
1512 C C   . LYS A 202 ? 0.43921 0.43606 0.33852 -0.02541 -0.02989 -0.10081 209 LYS A C   
1513 O O   . LYS A 202 ? 0.43005 0.39787 0.31082 -0.03316 -0.04084 -0.11738 209 LYS A O   
1514 C CB  . LYS A 202 ? 0.39024 0.44550 0.28221 -0.01535 -0.03001 -0.08575 209 LYS A CB  
1515 C CG  . LYS A 202 ? 0.48954 0.54527 0.37568 -0.03088 -0.04915 -0.09649 209 LYS A CG  
1516 C CD  . LYS A 202 ? 0.53189 0.62300 0.41187 -0.02875 -0.05680 -0.08877 209 LYS A CD  
1517 C CE  . LYS A 202 ? 0.55782 0.65369 0.42770 -0.04374 -0.07854 -0.10214 209 LYS A CE  
1518 N NZ  . LYS A 202 ? 0.91939 0.99377 0.74418 -0.03813 -0.08585 -0.12518 209 LYS A NZ  
1519 N N   . HIS A 203 ? 0.36479 0.37075 0.29503 -0.03110 -0.02487 -0.08625 210 HIS A N   
1520 C CA  . HIS A 203 ? 0.41263 0.40878 0.36155 -0.04863 -0.03140 -0.08409 210 HIS A CA  
1521 C C   . HIS A 203 ? 0.41864 0.39248 0.37708 -0.04574 -0.02185 -0.07911 210 HIS A C   
1522 O O   . HIS A 203 ? 0.38821 0.34727 0.35694 -0.06050 -0.02636 -0.07694 210 HIS A O   
1523 C CB  . HIS A 203 ? 0.32691 0.36151 0.30376 -0.05674 -0.03453 -0.06926 210 HIS A CB  
1524 C CG  . HIS A 203 ? 0.41718 0.47669 0.38886 -0.06238 -0.04733 -0.07172 210 HIS A CG  
1525 N ND1 . HIS A 203 ? 0.45135 0.50406 0.41385 -0.07895 -0.06358 -0.08388 210 HIS A ND1 
1526 C CD2 . HIS A 203 ? 0.47281 0.56313 0.44608 -0.05362 -0.04775 -0.06290 210 HIS A CD2 
1527 C CE1 . HIS A 203 ? 0.48220 0.56614 0.44120 -0.07932 -0.07377 -0.08285 210 HIS A CE1 
1528 N NE2 . HIS A 203 ? 0.47192 0.57840 0.43695 -0.06282 -0.06354 -0.06907 210 HIS A NE2 
1529 N N   . SER A 204 ? 0.35898 0.33321 0.31557 -0.02845 -0.00954 -0.07521 211 SER A N   
1530 C CA  . SER A 204 ? 0.39012 0.35220 0.35737 -0.02385 -0.00136 -0.06781 211 SER A CA  
1531 C C   . SER A 204 ? 0.35963 0.30348 0.31005 -0.00522 0.00656  -0.07379 211 SER A C   
1532 O O   . SER A 204 ? 0.40402 0.35104 0.36361 0.00403  0.01427  -0.06583 211 SER A O   
1533 C CB  . SER A 204 ? 0.32222 0.31365 0.31178 -0.02154 0.00418  -0.05359 211 SER A CB  
1534 O OG  . SER A 204 ? 0.34264 0.35507 0.34725 -0.03308 -0.00155 -0.04749 211 SER A OG  
1535 N N   . GLN A 205 ? 0.43846 0.36576 0.36285 0.00250  0.00437  -0.08813 212 GLN A N   
1536 C CA  . GLN A 205 ? 0.53630 0.45753 0.44498 0.02557  0.01394  -0.09282 212 GLN A CA  
1537 C C   . GLN A 205 ? 0.51016 0.39406 0.41288 0.03437  0.01658  -0.09451 212 GLN A C   
1538 O O   . GLN A 205 ? 0.53748 0.42458 0.43488 0.05617  0.02585  -0.09366 212 GLN A O   
1539 C CB  . GLN A 205 ? 0.50499 0.42062 0.38231 0.03591  0.01206  -0.10864 212 GLN A CB  
1540 C CG  . GLN A 205 ? 0.65252 0.52030 0.50347 0.02870  -0.00056 -0.12761 212 GLN A CG  
1541 C CD  . GLN A 205 ? 0.87796 0.75546 0.72963 0.00631  -0.01508 -0.13163 212 GLN A CD  
1542 O OE1 . GLN A 205 ? 0.65959 0.55594 0.53986 -0.01298 -0.01947 -0.11890 212 GLN A OE1 
1543 N NE2 . GLN A 205 ? 0.77974 0.64757 0.59838 0.01111  -0.02283 -0.14958 212 GLN A NE2 
1544 N N   . PHE A 206 ? 0.43448 0.28616 0.33957 0.01821  0.00889  -0.09424 213 PHE A N   
1545 C CA  . PHE A 206 ? 0.46939 0.27769 0.36567 0.02548  0.01040  -0.09357 213 PHE A CA  
1546 C C   . PHE A 206 ? 0.51438 0.33089 0.43537 0.01655  0.01359  -0.07427 213 PHE A C   
1547 O O   . PHE A 206 ? 0.56604 0.34584 0.48111 0.01892  0.01408  -0.06933 213 PHE A O   
1548 C CB  . PHE A 206 ? 0.56731 0.32016 0.43984 0.01397  -0.00185 -0.10864 213 PHE A CB  
1549 C CG  . PHE A 206 ? 0.65483 0.39309 0.49383 0.02777  -0.00545 -0.13103 213 PHE A CG  
1550 C CD1 . PHE A 206 ? 0.63933 0.38536 0.46134 0.06036  0.00617  -0.13648 213 PHE A CD1 
1551 C CD2 . PHE A 206 ? 0.62531 0.35092 0.45042 0.00925  -0.02026 -0.14566 213 PHE A CD2 
1552 C CE1 . PHE A 206 ? 0.75690 0.49458 0.54480 0.07680  0.00506  -0.15648 213 PHE A CE1 
1553 C CE2 . PHE A 206 ? 0.75034 0.46439 0.53904 0.02449  -0.02378 -0.16751 213 PHE A CE2 
1554 C CZ  . PHE A 206 ? 0.72265 0.44226 0.49133 0.05948  -0.01001 -0.17287 213 PHE A CZ  
1555 N N   . ILE A 207 ? 0.38409 0.24549 0.32923 0.00851  0.01588  -0.06309 214 ILE A N   
1556 C CA  . ILE A 207 ? 0.37164 0.24571 0.33518 0.00511  0.02003  -0.04637 214 ILE A CA  
1557 C C   . ILE A 207 ? 0.44517 0.31397 0.40353 0.02722  0.02733  -0.04133 214 ILE A C   
1558 O O   . ILE A 207 ? 0.42890 0.31596 0.38444 0.04398  0.03130  -0.04581 214 ILE A O   
1559 C CB  . ILE A 207 ? 0.33820 0.25793 0.32168 -0.00083 0.02087  -0.03983 214 ILE A CB  
1560 C CG1 . ILE A 207 ? 0.33626 0.26574 0.32805 -0.02085 0.01356  -0.04088 214 ILE A CG1 
1561 C CG2 . ILE A 207 ? 0.30751 0.24225 0.30292 0.00289  0.02593  -0.02594 214 ILE A CG2 
1562 C CD1 . ILE A 207 ? 0.37263 0.29485 0.37563 -0.03770 0.01173  -0.02993 214 ILE A CD1 
1563 N N   . GLY A 208 ? 0.41522 0.26375 0.37378 0.02724  0.02913  -0.02954 215 GLY A N   
1564 C CA  . GLY A 208 ? 0.40945 0.24820 0.36011 0.04987  0.03438  -0.02365 215 GLY A CA  
1565 C C   . GLY A 208 ? 0.43149 0.31247 0.39574 0.05952  0.03806  -0.01353 215 GLY A C   
1566 O O   . GLY A 208 ? 0.41098 0.28740 0.37137 0.07382  0.04075  -0.00331 215 GLY A O   
1567 N N   . TYR A 209 ? 0.33786 0.25717 0.31583 0.05232  0.03669  -0.01647 216 TYR A N   
1568 C CA  . TYR A 209 ? 0.34015 0.29522 0.32869 0.05863  0.03670  -0.01077 216 TYR A CA  
1569 C C   . TYR A 209 ? 0.34040 0.32432 0.33786 0.05783  0.03486  -0.01859 216 TYR A C   
1570 O O   . TYR A 209 ? 0.32837 0.31034 0.32565 0.04826  0.03392  -0.02557 216 TYR A O   
1571 C CB  . TYR A 209 ? 0.32952 0.29619 0.32444 0.04769  0.03596  -0.00311 216 TYR A CB  
1572 C CG  . TYR A 209 ? 0.34588 0.29096 0.33423 0.04662  0.03943  0.00978  216 TYR A CG  
1573 C CD1 . TYR A 209 ? 0.34340 0.29003 0.32479 0.06115  0.04148  0.02058  216 TYR A CD1 
1574 C CD2 . TYR A 209 ? 0.36094 0.28568 0.35071 0.02973  0.03985  0.01318  216 TYR A CD2 
1575 C CE1 . TYR A 209 ? 0.37064 0.29673 0.34494 0.06000  0.04564  0.03634  216 TYR A CE1 
1576 C CE2 . TYR A 209 ? 0.32470 0.22953 0.31087 0.02511  0.04328  0.02884  216 TYR A CE2 
1577 C CZ  . TYR A 209 ? 0.37985 0.28407 0.35739 0.04088  0.04707  0.04134  216 TYR A CZ  
1578 O OH  . TYR A 209 ? 0.43010 0.31414 0.40293 0.03640  0.05145  0.06079  216 TYR A OH  
1579 N N   . PRO A 210 ? 0.28619 0.29844 0.29192 0.06626  0.03338  -0.01599 217 PRO A N   
1580 C CA  . PRO A 210 ? 0.29639 0.33652 0.31361 0.06143  0.03138  -0.01949 217 PRO A CA  
1581 C C   . PRO A 210 ? 0.27977 0.32298 0.30236 0.04504  0.02699  -0.02147 217 PRO A C   
1582 O O   . PRO A 210 ? 0.29443 0.33750 0.31748 0.04158  0.02339  -0.01966 217 PRO A O   
1583 C CB  . PRO A 210 ? 0.29730 0.36732 0.32511 0.06982  0.02786  -0.01419 217 PRO A CB  
1584 C CG  . PRO A 210 ? 0.35874 0.41820 0.37876 0.07610  0.02588  -0.00923 217 PRO A CG  
1585 C CD  . PRO A 210 ? 0.36447 0.38676 0.37009 0.07918  0.03216  -0.00820 217 PRO A CD  
1586 N N   . ILE A 211 ? 0.27965 0.32568 0.30345 0.03802  0.02775  -0.02491 218 ILE A N   
1587 C CA  . ILE A 211 ? 0.26487 0.31433 0.29350 0.02577  0.02348  -0.02522 218 ILE A CA  
1588 C C   . ILE A 211 ? 0.28279 0.35376 0.32220 0.02160  0.02100  -0.02174 218 ILE A C   
1589 O O   . ILE A 211 ? 0.27626 0.36013 0.31665 0.02375  0.02558  -0.01998 218 ILE A O   
1590 C CB  . ILE A 211 ? 0.32059 0.35837 0.34222 0.01966  0.02451  -0.02886 218 ILE A CB  
1591 C CG1 . ILE A 211 ? 0.31864 0.33649 0.33404 0.01820  0.02532  -0.03002 218 ILE A CG1 
1592 C CG2 . ILE A 211 ? 0.25400 0.29831 0.28085 0.01117  0.02011  -0.02695 218 ILE A CG2 
1593 C CD1 . ILE A 211 ? 0.30067 0.30513 0.30744 0.01178  0.02409  -0.03591 218 ILE A CD1 
1594 N N   . THR A 212 ? 0.24300 0.31730 0.28917 0.01553  0.01361  -0.02037 219 THR A N   
1595 C CA  . THR A 212 ? 0.18868 0.27914 0.24749 0.00636  0.00841  -0.01533 219 THR A CA  
1596 C C   . THR A 212 ? 0.20825 0.28406 0.26537 -0.00326 0.00386  -0.01440 219 THR A C   
1597 O O   . THR A 212 ? 0.25742 0.31513 0.30759 -0.00212 -0.00132 -0.01938 219 THR A O   
1598 C CB  . THR A 212 ? 0.23318 0.33309 0.29894 0.00527  -0.00050 -0.01590 219 THR A CB  
1599 O OG1 . THR A 212 ? 0.24450 0.36013 0.31150 0.01768  0.00375  -0.01461 219 THR A OG1 
1600 C CG2 . THR A 212 ? 0.25920 0.37550 0.34169 -0.00999 -0.00831 -0.00940 219 THR A CG2 
1601 N N   . LEU A 213 ? 0.22242 0.30704 0.28393 -0.00982 0.00660  -0.00693 220 LEU A N   
1602 C CA  . LEU A 213 ? 0.20798 0.27788 0.26759 -0.01765 0.00202  -0.00252 220 LEU A CA  
1603 C C   . LEU A 213 ? 0.23673 0.30567 0.30831 -0.03135 -0.00727 0.00398  220 LEU A C   
1604 O O   . LEU A 213 ? 0.22147 0.31506 0.30713 -0.04023 -0.00525 0.01463  220 LEU A O   
1605 C CB  . LEU A 213 ? 0.23737 0.31666 0.29224 -0.01747 0.00914  0.00423  220 LEU A CB  
1606 C CG  . LEU A 213 ? 0.27468 0.34308 0.32746 -0.02418 0.00536  0.01386  220 LEU A CG  
1607 C CD1 . LEU A 213 ? 0.28792 0.32916 0.33370 -0.01968 -0.00179 0.00775  220 LEU A CD1 
1608 C CD2 . LEU A 213 ? 0.26182 0.34421 0.30482 -0.02056 0.01245  0.01927  220 LEU A CD2 
1609 N N   . PHE A 214 ? 0.22801 0.26936 0.29367 -0.03299 -0.01786 -0.00254 221 PHE A N   
1610 C CA  . PHE A 214 ? 0.23536 0.26432 0.30874 -0.04853 -0.03074 0.00072  221 PHE A CA  
1611 C C   . PHE A 214 ? 0.27506 0.29465 0.35261 -0.06037 -0.03101 0.01574  221 PHE A C   
1612 O O   . PHE A 214 ? 0.29150 0.30311 0.35911 -0.05216 -0.02478 0.01925  221 PHE A O   
1613 C CB  . PHE A 214 ? 0.27609 0.26926 0.33366 -0.04295 -0.04261 -0.01360 221 PHE A CB  
1614 C CG  . PHE A 214 ? 0.24295 0.24541 0.29556 -0.03482 -0.04593 -0.02579 221 PHE A CG  
1615 C CD1 . PHE A 214 ? 0.25527 0.28606 0.31091 -0.02467 -0.03495 -0.02534 221 PHE A CD1 
1616 C CD2 . PHE A 214 ? 0.26142 0.23974 0.30210 -0.03567 -0.06101 -0.03812 221 PHE A CD2 
1617 C CE1 . PHE A 214 ? 0.26401 0.30227 0.31312 -0.01575 -0.03788 -0.03336 221 PHE A CE1 
1618 C CE2 . PHE A 214 ? 0.27868 0.26793 0.31091 -0.02636 -0.06454 -0.04843 221 PHE A CE2 
1619 C CZ  . PHE A 214 ? 0.26990 0.29070 0.30731 -0.01631 -0.05235 -0.04429 221 PHE A CZ  
1620 N N   . VAL A 215 ? 0.29003 0.31228 0.38311 -0.08090 -0.03923 0.02647  222 VAL A N   
1621 C CA  . VAL A 215 ? 0.34339 0.35224 0.44067 -0.09513 -0.04072 0.04458  222 VAL A CA  
1622 C C   . VAL A 215 ? 0.40619 0.36259 0.49657 -0.10640 -0.05918 0.04010  222 VAL A C   
1623 O O   . VAL A 215 ? 0.40097 0.33955 0.48515 -0.10542 -0.07118 0.02280  222 VAL A O   
1624 C CB  . VAL A 215 ? 0.43975 0.49394 0.56164 -0.11234 -0.03411 0.06587  222 VAL A CB  
1625 C CG1 . VAL A 215 ? 0.51051 0.60612 0.62969 -0.09555 -0.01524 0.06866  222 VAL A CG1 
1626 C CG2 . VAL A 215 ? 0.34429 0.42125 0.48745 -0.12720 -0.04373 0.06388  222 VAL A CG2 
1627 N N   . GLU A 216 ? 0.44206 0.37011 0.52983 -0.11560 -0.06205 0.05560  223 GLU A N   
1628 C CA  . GLU A 216 ? 0.57531 0.44065 0.65067 -0.12306 -0.07992 0.05095  223 GLU A CA  
1629 C C   . GLU A 216 ? 0.58859 0.44444 0.68358 -0.15714 -0.09027 0.07215  223 GLU A C   
1630 O O   . GLU A 216 ? 0.62261 0.52227 0.73921 -0.17147 -0.07966 0.09610  223 GLU A O   
1631 C CB  . GLU A 216 ? 0.55632 0.38247 0.60801 -0.10201 -0.07727 0.05145  223 GLU A CB  
1632 C CG  . GLU A 216 ? 0.50029 0.34084 0.53695 -0.07131 -0.06719 0.03456  223 GLU A CG  
1633 C CD  . GLU A 216 ? 0.64984 0.45973 0.66738 -0.05021 -0.06593 0.03692  223 GLU A CD  
1634 O OE1 . GLU A 216 ? 0.62375 0.37763 0.62566 -0.04613 -0.07840 0.03258  223 GLU A OE1 
1635 O OE2 . GLU A 216 ? 0.62662 0.46778 0.64396 -0.03718 -0.05368 0.04302  223 GLU A OE2 
1636 N N   . LYS A 217 ? 0.72219 0.51943 0.80801 -0.16987 -0.11149 0.06305  224 LYS A N   
1637 C CA  . LYS A 217 ? 0.85403 0.62770 0.95266 -0.20099 -0.12320 0.08106  224 LYS A CA  
1638 C C   . LYS A 217 ? 0.94694 0.78795 1.08068 -0.22507 -0.11873 0.09588  224 LYS A C   
1639 O O   . LYS A 217 ? 0.94265 0.79654 1.09188 -0.24344 -0.11493 0.11986  224 LYS A O   
1640 C CB  . LYS A 217 ? 0.79288 0.54268 0.88440 -0.19893 -0.11496 0.10588  224 LYS A CB  
1641 C CG  . LYS A 217 ? 0.88203 0.56769 0.93925 -0.17082 -0.11875 0.09433  224 LYS A CG  
1642 C CD  . LYS A 217 ? 1.02355 0.71158 1.07640 -0.16141 -0.10541 0.12128  224 LYS A CD  
1643 C CE  . LYS A 217 ? 1.03987 0.73368 1.10749 -0.18659 -0.10302 0.14987  224 LYS A CE  
1644 N NZ  . LYS A 217 ? 1.04546 0.67361 1.09041 -0.17785 -0.10856 0.15758  224 LYS A NZ  
# 
