data_7HBB
# 
_entry.id   7HBB 
# 
_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   7HBB         pdb_00007hbb 10.2210/pdb7hbb/pdb 
WWPDB D_1001407258 ?            ?                   
# 
_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                        7HBB 
_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 3-methyl-2-oxo-2,3-dihydro-1,3-benzoxazole-6-sulfonamide 228.225   1   ?        ? ? ? 
3 water       nat water                                                    18.015    289 ?        ? ? ? 
# 
_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 3-methyl-2-oxo-2,3-dihydro-1,3-benzoxazole-6-sulfonamide A1AY4 
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 
A1AY4 non-polymer         . 3-methyl-2-oxo-2,3-dihydro-1,3-benzoxazole-6-sulfonamide ? 'C8 H8 N2 O4 S'  228.225 
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        A1AY4 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1AY4 
_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 A1AY4 1   301 301 A1AY4 BF8 A . 
C 3 HOH   1   401 230 HOH   HOH A . 
C 3 HOH   2   402 233 HOH   HOH A . 
C 3 HOH   3   403 224 HOH   HOH A . 
C 3 HOH   4   404 42  HOH   HOH A . 
C 3 HOH   5   405 181 HOH   HOH A . 
C 3 HOH   6   406 171 HOH   HOH A . 
C 3 HOH   7   407 277 HOH   HOH A . 
C 3 HOH   8   408 169 HOH   HOH A . 
C 3 HOH   9   409 162 HOH   HOH A . 
C 3 HOH   10  410 137 HOH   HOH A . 
C 3 HOH   11  411 283 HOH   HOH A . 
C 3 HOH   12  412 204 HOH   HOH A . 
C 3 HOH   13  413 223 HOH   HOH A . 
C 3 HOH   14  414 108 HOH   HOH A . 
C 3 HOH   15  415 229 HOH   HOH A . 
C 3 HOH   16  416 54  HOH   HOH A . 
C 3 HOH   17  417 35  HOH   HOH A . 
C 3 HOH   18  418 110 HOH   HOH A . 
C 3 HOH   19  419 114 HOH   HOH A . 
C 3 HOH   20  420 158 HOH   HOH A . 
C 3 HOH   21  421 11  HOH   HOH A . 
C 3 HOH   22  422 246 HOH   HOH A . 
C 3 HOH   23  423 78  HOH   HOH A . 
C 3 HOH   24  424 52  HOH   HOH A . 
C 3 HOH   25  425 127 HOH   HOH A . 
C 3 HOH   26  426 53  HOH   HOH A . 
C 3 HOH   27  427 27  HOH   HOH A . 
C 3 HOH   28  428 13  HOH   HOH A . 
C 3 HOH   29  429 268 HOH   HOH A . 
C 3 HOH   30  430 89  HOH   HOH A . 
C 3 HOH   31  431 91  HOH   HOH A . 
C 3 HOH   32  432 95  HOH   HOH A . 
C 3 HOH   33  433 47  HOH   HOH A . 
C 3 HOH   34  434 36  HOH   HOH A . 
C 3 HOH   35  435 180 HOH   HOH A . 
C 3 HOH   36  436 186 HOH   HOH A . 
C 3 HOH   37  437 172 HOH   HOH A . 
C 3 HOH   38  438 92  HOH   HOH A . 
C 3 HOH   39  439 80  HOH   HOH A . 
C 3 HOH   40  440 175 HOH   HOH A . 
C 3 HOH   41  441 182 HOH   HOH A . 
C 3 HOH   42  442 116 HOH   HOH A . 
C 3 HOH   43  443 12  HOH   HOH A . 
C 3 HOH   44  444 84  HOH   HOH A . 
C 3 HOH   45  445 1   HOH   HOH A . 
C 3 HOH   46  446 156 HOH   HOH A . 
C 3 HOH   47  447 187 HOH   HOH A . 
C 3 HOH   48  448 14  HOH   HOH A . 
C 3 HOH   49  449 63  HOH   HOH A . 
C 3 HOH   50  450 43  HOH   HOH A . 
C 3 HOH   51  451 3   HOH   HOH A . 
C 3 HOH   52  452 32  HOH   HOH A . 
C 3 HOH   53  453 55  HOH   HOH A . 
C 3 HOH   54  454 75  HOH   HOH A . 
C 3 HOH   55  455 19  HOH   HOH A . 
C 3 HOH   56  456 155 HOH   HOH A . 
C 3 HOH   57  457 98  HOH   HOH A . 
C 3 HOH   58  458 129 HOH   HOH A . 
C 3 HOH   59  459 49  HOH   HOH A . 
C 3 HOH   60  460 57  HOH   HOH A . 
C 3 HOH   61  461 107 HOH   HOH A . 
C 3 HOH   62  462 28  HOH   HOH A . 
C 3 HOH   63  463 196 HOH   HOH A . 
C 3 HOH   64  464 23  HOH   HOH A . 
C 3 HOH   65  465 56  HOH   HOH A . 
C 3 HOH   66  466 256 HOH   HOH A . 
C 3 HOH   67  467 103 HOH   HOH A . 
C 3 HOH   68  468 65  HOH   HOH A . 
C 3 HOH   69  469 71  HOH   HOH A . 
C 3 HOH   70  470 67  HOH   HOH A . 
C 3 HOH   71  471 68  HOH   HOH A . 
C 3 HOH   72  472 115 HOH   HOH A . 
C 3 HOH   73  473 50  HOH   HOH A . 
C 3 HOH   74  474 15  HOH   HOH A . 
C 3 HOH   75  475 209 HOH   HOH A . 
C 3 HOH   76  476 40  HOH   HOH A . 
C 3 HOH   77  477 247 HOH   HOH A . 
C 3 HOH   78  478 193 HOH   HOH A . 
C 3 HOH   79  479 215 HOH   HOH A . 
C 3 HOH   80  480 2   HOH   HOH A . 
C 3 HOH   81  481 77  HOH   HOH A . 
C 3 HOH   82  482 64  HOH   HOH A . 
C 3 HOH   83  483 16  HOH   HOH A . 
C 3 HOH   84  484 152 HOH   HOH A . 
C 3 HOH   85  485 139 HOH   HOH A . 
C 3 HOH   86  486 29  HOH   HOH A . 
C 3 HOH   87  487 69  HOH   HOH A . 
C 3 HOH   88  488 136 HOH   HOH A . 
C 3 HOH   89  489 241 HOH   HOH A . 
C 3 HOH   90  490 165 HOH   HOH A . 
C 3 HOH   91  491 17  HOH   HOH A . 
C 3 HOH   92  492 86  HOH   HOH A . 
C 3 HOH   93  493 26  HOH   HOH A . 
C 3 HOH   94  494 30  HOH   HOH A . 
C 3 HOH   95  495 102 HOH   HOH A . 
C 3 HOH   96  496 99  HOH   HOH A . 
C 3 HOH   97  497 101 HOH   HOH A . 
C 3 HOH   98  498 258 HOH   HOH A . 
C 3 HOH   99  499 37  HOH   HOH A . 
C 3 HOH   100 500 278 HOH   HOH A . 
C 3 HOH   101 501 225 HOH   HOH A . 
C 3 HOH   102 502 254 HOH   HOH A . 
C 3 HOH   103 503 10  HOH   HOH A . 
C 3 HOH   104 504 79  HOH   HOH A . 
C 3 HOH   105 505 7   HOH   HOH A . 
C 3 HOH   106 506 138 HOH   HOH A . 
C 3 HOH   107 507 62  HOH   HOH A . 
C 3 HOH   108 508 149 HOH   HOH A . 
C 3 HOH   109 509 5   HOH   HOH A . 
C 3 HOH   110 510 128 HOH   HOH A . 
C 3 HOH   111 511 134 HOH   HOH A . 
C 3 HOH   112 512 189 HOH   HOH A . 
C 3 HOH   113 513 207 HOH   HOH A . 
C 3 HOH   114 514 168 HOH   HOH A . 
C 3 HOH   115 515 33  HOH   HOH A . 
C 3 HOH   116 516 58  HOH   HOH A . 
C 3 HOH   117 517 82  HOH   HOH A . 
C 3 HOH   118 518 6   HOH   HOH A . 
C 3 HOH   119 519 222 HOH   HOH A . 
C 3 HOH   120 520 22  HOH   HOH A . 
C 3 HOH   121 521 44  HOH   HOH A . 
C 3 HOH   122 522 197 HOH   HOH A . 
C 3 HOH   123 523 61  HOH   HOH A . 
C 3 HOH   124 524 151 HOH   HOH A . 
C 3 HOH   125 525 87  HOH   HOH A . 
C 3 HOH   126 526 20  HOH   HOH A . 
C 3 HOH   127 527 9   HOH   HOH A . 
C 3 HOH   128 528 123 HOH   HOH A . 
C 3 HOH   129 529 142 HOH   HOH A . 
C 3 HOH   130 530 109 HOH   HOH A . 
C 3 HOH   131 531 76  HOH   HOH A . 
C 3 HOH   132 532 120 HOH   HOH A . 
C 3 HOH   133 533 31  HOH   HOH A . 
C 3 HOH   134 534 260 HOH   HOH A . 
C 3 HOH   135 535 240 HOH   HOH A . 
C 3 HOH   136 536 201 HOH   HOH A . 
C 3 HOH   137 537 34  HOH   HOH A . 
C 3 HOH   138 538 279 HOH   HOH A . 
C 3 HOH   139 539 25  HOH   HOH A . 
C 3 HOH   140 540 219 HOH   HOH A . 
C 3 HOH   141 541 81  HOH   HOH A . 
C 3 HOH   142 542 88  HOH   HOH A . 
C 3 HOH   143 543 8   HOH   HOH A . 
C 3 HOH   144 544 111 HOH   HOH A . 
C 3 HOH   145 545 60  HOH   HOH A . 
C 3 HOH   146 546 48  HOH   HOH A . 
C 3 HOH   147 547 238 HOH   HOH A . 
C 3 HOH   148 548 216 HOH   HOH A . 
C 3 HOH   149 549 18  HOH   HOH A . 
C 3 HOH   150 550 143 HOH   HOH A . 
C 3 HOH   151 551 21  HOH   HOH A . 
C 3 HOH   152 552 226 HOH   HOH A . 
C 3 HOH   153 553 117 HOH   HOH A . 
C 3 HOH   154 554 121 HOH   HOH A . 
C 3 HOH   155 555 96  HOH   HOH A . 
C 3 HOH   156 556 288 HOH   HOH A . 
C 3 HOH   157 557 39  HOH   HOH A . 
C 3 HOH   158 558 147 HOH   HOH A . 
C 3 HOH   159 559 90  HOH   HOH A . 
C 3 HOH   160 560 198 HOH   HOH A . 
C 3 HOH   161 561 140 HOH   HOH A . 
C 3 HOH   162 562 214 HOH   HOH A . 
C 3 HOH   163 563 271 HOH   HOH A . 
C 3 HOH   164 564 237 HOH   HOH A . 
C 3 HOH   165 565 100 HOH   HOH A . 
C 3 HOH   166 566 161 HOH   HOH A . 
C 3 HOH   167 567 93  HOH   HOH A . 
C 3 HOH   168 568 94  HOH   HOH A . 
C 3 HOH   169 569 157 HOH   HOH A . 
C 3 HOH   170 570 167 HOH   HOH A . 
C 3 HOH   171 571 73  HOH   HOH A . 
C 3 HOH   172 572 38  HOH   HOH A . 
C 3 HOH   173 573 183 HOH   HOH A . 
C 3 HOH   174 574 232 HOH   HOH A . 
C 3 HOH   175 575 227 HOH   HOH A . 
C 3 HOH   176 576 41  HOH   HOH A . 
C 3 HOH   177 577 51  HOH   HOH A . 
C 3 HOH   178 578 45  HOH   HOH A . 
C 3 HOH   179 579 267 HOH   HOH A . 
C 3 HOH   180 580 4   HOH   HOH A . 
C 3 HOH   181 581 105 HOH   HOH A . 
C 3 HOH   182 582 119 HOH   HOH A . 
C 3 HOH   183 583 287 HOH   HOH A . 
C 3 HOH   184 584 276 HOH   HOH A . 
C 3 HOH   185 585 112 HOH   HOH A . 
C 3 HOH   186 586 195 HOH   HOH A . 
C 3 HOH   187 587 184 HOH   HOH A . 
C 3 HOH   188 588 59  HOH   HOH A . 
C 3 HOH   189 589 272 HOH   HOH A . 
C 3 HOH   190 590 173 HOH   HOH A . 
C 3 HOH   191 591 163 HOH   HOH A . 
C 3 HOH   192 592 236 HOH   HOH A . 
C 3 HOH   193 593 194 HOH   HOH A . 
C 3 HOH   194 594 245 HOH   HOH A . 
C 3 HOH   195 595 211 HOH   HOH A . 
C 3 HOH   196 596 213 HOH   HOH A . 
C 3 HOH   197 597 24  HOH   HOH A . 
C 3 HOH   198 598 154 HOH   HOH A . 
C 3 HOH   199 599 97  HOH   HOH A . 
C 3 HOH   200 600 270 HOH   HOH A . 
C 3 HOH   201 601 118 HOH   HOH A . 
C 3 HOH   202 602 243 HOH   HOH A . 
C 3 HOH   203 603 251 HOH   HOH A . 
C 3 HOH   204 604 217 HOH   HOH A . 
C 3 HOH   205 605 285 HOH   HOH A . 
C 3 HOH   206 606 166 HOH   HOH A . 
C 3 HOH   207 607 104 HOH   HOH A . 
C 3 HOH   208 608 148 HOH   HOH A . 
C 3 HOH   209 609 264 HOH   HOH A . 
C 3 HOH   210 610 289 HOH   HOH A . 
C 3 HOH   211 611 208 HOH   HOH A . 
C 3 HOH   212 612 130 HOH   HOH A . 
C 3 HOH   213 613 133 HOH   HOH A . 
C 3 HOH   214 614 265 HOH   HOH A . 
C 3 HOH   215 615 242 HOH   HOH A . 
C 3 HOH   216 616 179 HOH   HOH A . 
C 3 HOH   217 617 253 HOH   HOH A . 
C 3 HOH   218 618 252 HOH   HOH A . 
C 3 HOH   219 619 72  HOH   HOH A . 
C 3 HOH   220 620 203 HOH   HOH A . 
C 3 HOH   221 621 124 HOH   HOH A . 
C 3 HOH   222 622 125 HOH   HOH A . 
C 3 HOH   223 623 220 HOH   HOH A . 
C 3 HOH   224 624 244 HOH   HOH A . 
C 3 HOH   225 625 145 HOH   HOH A . 
C 3 HOH   226 626 249 HOH   HOH A . 
C 3 HOH   227 627 191 HOH   HOH A . 
C 3 HOH   228 628 66  HOH   HOH A . 
C 3 HOH   229 629 132 HOH   HOH A . 
C 3 HOH   230 630 153 HOH   HOH A . 
C 3 HOH   231 631 70  HOH   HOH A . 
C 3 HOH   232 632 178 HOH   HOH A . 
C 3 HOH   233 633 188 HOH   HOH A . 
C 3 HOH   234 634 141 HOH   HOH A . 
C 3 HOH   235 635 284 HOH   HOH A . 
C 3 HOH   236 636 212 HOH   HOH A . 
C 3 HOH   237 637 113 HOH   HOH A . 
C 3 HOH   238 638 135 HOH   HOH A . 
C 3 HOH   239 639 199 HOH   HOH A . 
C 3 HOH   240 640 202 HOH   HOH A . 
C 3 HOH   241 641 266 HOH   HOH A . 
C 3 HOH   242 642 74  HOH   HOH A . 
C 3 HOH   243 643 281 HOH   HOH A . 
C 3 HOH   244 644 231 HOH   HOH A . 
C 3 HOH   245 645 174 HOH   HOH A . 
C 3 HOH   246 646 126 HOH   HOH A . 
C 3 HOH   247 647 269 HOH   HOH A . 
C 3 HOH   248 648 257 HOH   HOH A . 
C 3 HOH   249 649 280 HOH   HOH A . 
C 3 HOH   250 650 273 HOH   HOH A . 
C 3 HOH   251 651 46  HOH   HOH A . 
C 3 HOH   252 652 144 HOH   HOH A . 
C 3 HOH   253 653 206 HOH   HOH A . 
C 3 HOH   254 654 192 HOH   HOH A . 
C 3 HOH   255 655 146 HOH   HOH A . 
C 3 HOH   256 656 218 HOH   HOH A . 
C 3 HOH   257 657 150 HOH   HOH A . 
C 3 HOH   258 658 274 HOH   HOH A . 
C 3 HOH   259 659 122 HOH   HOH A . 
C 3 HOH   260 660 234 HOH   HOH A . 
C 3 HOH   261 661 164 HOH   HOH A . 
C 3 HOH   262 662 255 HOH   HOH A . 
C 3 HOH   263 663 177 HOH   HOH A . 
C 3 HOH   264 664 170 HOH   HOH A . 
C 3 HOH   265 665 210 HOH   HOH A . 
C 3 HOH   266 666 263 HOH   HOH A . 
C 3 HOH   267 667 262 HOH   HOH A . 
C 3 HOH   268 668 228 HOH   HOH A . 
C 3 HOH   269 669 275 HOH   HOH A . 
C 3 HOH   270 670 185 HOH   HOH A . 
C 3 HOH   271 671 131 HOH   HOH A . 
C 3 HOH   272 672 259 HOH   HOH A . 
C 3 HOH   273 673 221 HOH   HOH A . 
C 3 HOH   274 674 248 HOH   HOH A . 
C 3 HOH   275 675 85  HOH   HOH A . 
C 3 HOH   276 676 250 HOH   HOH A . 
C 3 HOH   277 677 282 HOH   HOH A . 
C 3 HOH   278 678 176 HOH   HOH A . 
C 3 HOH   279 679 286 HOH   HOH A . 
C 3 HOH   280 680 106 HOH   HOH A . 
C 3 HOH   281 681 239 HOH   HOH A . 
C 3 HOH   282 682 190 HOH   HOH A . 
C 3 HOH   283 683 160 HOH   HOH A . 
C 3 HOH   284 684 261 HOH   HOH A . 
C 3 HOH   285 685 83  HOH   HOH A . 
C 3 HOH   286 686 205 HOH   HOH A . 
C 3 HOH   287 687 159 HOH   HOH A . 
C 3 HOH   288 688 200 HOH   HOH A . 
C 3 HOH   289 689 235 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             596801.392 
_cell.length_a           66.060 
_cell.length_b           90.180 
_cell.length_c           100.180 
_cell.angle_beta         90.000 
_cell.angle_gamma        90.000 
_cell.angle_alpha        90.000 
_cell.entry_id           7HBB 
_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                         7HBB 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
# 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
_exptl.entry_id          7HBB 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_Matthews      2.88 
_exptl_crystal.density_percent_sol   57.23 
_exptl_crystal.density_meas          ? 
_exptl_crystal.description           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.pH              8.5 
_exptl_crystal_grow.temp            277 
_exptl_crystal_grow.pdbx_details    '100mM Tris-HCl pH 8.5, 22% PEG4000, 200mM MgCl2' 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_diffrn.id                     1 
_diffrn.crystal_id             1 
_diffrn.ambient_temp           100 
_diffrn.ambient_temp_details   ? 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               PIXEL 
_diffrn_detector.type                   'DECTRIS EIGER X 16M' 
_diffrn_detector.pdbx_collection_date   2023-07-19 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.pdbx_scattering_type             x-ray 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.monochromator                    Si111 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.97918 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.pdbx_synchrotron_beamline   BL10U2 
_diffrn_source.type                        'SSRF BEAMLINE BL10U2' 
_diffrn_source.pdbx_wavelength_list        0.97918 
_diffrn_source.pdbx_synchrotron_site       SSRF 
_diffrn_source.pdbx_wavelength             ? 
# 
_reflns.entry_id                     7HBB 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             33.510 
_reflns.d_resolution_high            1.840 
_reflns.number_obs                   25888 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         98.400 
_reflns.pdbx_Rmerge_I_obs            0.076 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        21.000 
_reflns.B_iso_Wilson_estimate        ? 
_reflns.pdbx_redundancy              10.200 
_reflns.pdbx_Rrim_I_all              0.080 
_reflns.pdbx_Rpim_I_all              0.024 
_reflns.pdbx_CC_half                 0.999 
_reflns.pdbx_netI_over_av_sigmaI     ? 
_reflns.pdbx_number_measured_all     263307 
_reflns.pdbx_scaling_rejects         703 
_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 1.840 1.890  ? 7980 1666 ? 0.554 ? ? ? 4.800 ? 3.000  ? ? ? ? ? ? 87.500 0.626 0.277 0.714 
1 2 8.230 33.510 ? 3174 329  ? 0.038 ? ? ? 9.600 ? 42.300 ? ? ? ? ? ? 97.200 0.041 0.013 0.998 
# 
_refine.entry_id                                 7HBB 
_refine.pdbx_method_to_determine_struct          'FOURIER SYNTHESIS' 
_refine.ls_percent_reflns_R_free                 4.87 
_refine.pdbx_overall_phase_error                 21.4291 
_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                          0.1706 
_refine.B_iso_mean                               31.19 
_refine.ls_number_reflns_R_free                  1260 
_refine.ls_percent_reflns_obs                    98.17 
_refine.ls_R_factor_R_work                       0.1692 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_refine.ls_d_res_high                            1.84 
_refine.ls_number_reflns_obs                     25856 
_refine.pdbx_ls_sigma_F                          1.34 
_refine.ls_number_reflns_R_work                  24596 
_refine.ls_d_res_low                             33.51 
_refine.pdbx_stereochemistry_target_values       'GeoStd + Monomer Library + CDL v1.2' 
_refine.ls_R_factor_R_free                       0.1978 
_refine.overall_SU_ML                            0.2063 
_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             289 
_refine_hist.number_atoms_total               1948 
_refine_hist.d_res_high                       1.84 
_refine_hist.d_res_low                        33.51 
# 
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 0.0039 ? ? ? 
'X-RAY DIFFRACTION' f_angle_d          2276 0.6902 ? ? ? 
'X-RAY DIFFRACTION' f_chiral_restr     260  0.0472 ? ? ? 
'X-RAY DIFFRACTION' f_plane_restr      289  0.0046 ? ? ? 
'X-RAY DIFFRACTION' f_dihedral_angle_d 223  5.4588 ? ? ? 
# 
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' 1.84 1.91  2428 0.2786 88.70  0.3205 123 . . . . . 
'X-RAY DIFFRACTION' 1.91 2.00  2623 0.2311 95.89  0.2736 151 . . . . . 
'X-RAY DIFFRACTION' 2.00 2.11  2760 0.1877 99.83  0.2062 127 . . . . . 
'X-RAY DIFFRACTION' 2.11 2.24  2739 0.1674 99.97  0.2050 135 . . . . . 
'X-RAY DIFFRACTION' 2.24 2.41  2771 0.1897 99.52  0.2348 130 . . . . . 
'X-RAY DIFFRACTION' 2.41 2.65  2769 0.1725 100.00 0.2056 149 . . . . . 
'X-RAY DIFFRACTION' 2.65 3.04  2787 0.1755 100.00 0.2176 136 . . . . . 
'X-RAY DIFFRACTION' 3.04 3.82  2803 0.1519 99.97  0.1721 155 . . . . . 
'X-RAY DIFFRACTION' 3.83 33.51 2916 0.1469 99.45  0.1680 154 . . . . . 
# 
_struct.entry_id                  7HBB 
_struct.title                     'PanDDA analysis group deposition -- Crystal structure of HSP90N in complex with Fr13430' 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_details        ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HBB 
_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              7HBB 
_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 7HBB MET A 1   ? UNP P07900 ? ? 'initiating methionine' 8   1 
1 7HBB LEU A 230 ? UNP P07900 ? ? 'expression tag'        237 2 
1 7HBB GLU A 231 ? UNP P07900 ? ? 'expression tag'        238 3 
1 7HBB HIS A 232 ? UNP P07900 ? ? 'expression tag'        239 4 
1 7HBB HIS A 233 ? UNP P07900 ? ? 'expression tag'        240 5 
1 7HBB HIS A 234 ? UNP P07900 ? ? 'expression tag'        241 6 
1 7HBB HIS A 235 ? UNP P07900 ? ? 'expression tag'        242 7 
1 7HBB HIS A 236 ? UNP P07900 ? ? 'expression tag'        243 8 
1 7HBB 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 VAL A 10  ? ALA A 14  ? VAL A 17  ALA A 21  
AA1 2 SER A 162 ? THR A 167 ? SER A 169 THR A 174 
AA1 3 TYR A 153 ? SER A 157 ? TYR A 160 SER A 164 
AA1 4 ALA A 138 ? LYS A 146 ? ALA A 145 LYS A 153 
AA1 5 GLY A 176 ? LEU A 183 ? GLY A 183 LEU A 190 
AA1 6 THR A 81  ? ASP A 86  ? THR A 88  ASP A 93  
AA1 7 ILE A 71  ? ASN A 76  ? ILE A 78  ASN A 83  
AA1 8 ILE A 211 ? LEU A 213 ? ILE A 218 LEU A 220 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N PHE A 13  ? N PHE A 20  O PHE A 163 ? O PHE A 170 
AA1 2 3 O ARG A 166 ? O ARG A 173 N ALA A 154 ? N ALA A 161 
AA1 3 4 O TRP A 155 ? O TRP A 162 N VAL A 143 ? N VAL A 150 
AA1 4 5 N THR A 142 ? N THR A 149 O ILE A 180 ? O ILE A 187 
AA1 5 6 O LEU A 181 ? O LEU A 188 N LEU A 82  ? N LEU A 89  
AA1 6 7 O THR A 83  ? O THR A 90  N ILE A 74  ? N ILE A 81  
AA1 7 8 N LEU A 73  ? N LEU A 80  O THR A 212 ? O THR A 219 
# 
_pdbx_entry_details.entry_id                   7HBB 
_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 OE2 A GLU 200 ? ? O A HOH 401 ? ? 2.07 
2 1 OE1 A GLU 178 ? ? O A HOH 402 ? ? 2.17 
3 1 O   A HOH 589 ? ? O A HOH 647 ? ? 2.18 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 TYR A 38  ? ? -161.07 109.15  
2 1 ALA A 166 ? ? 63.03   -146.20 
# 
_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     651 
_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 12.3895097661   -17.947569725  -18.7893826342 0.137588913873 0.174235003457 0.197531885263 
0.0153748005042   -0.0258234219951 -0.0244873609757 3.80816326309 1.73630398134 8.57489930971 -1.07588996598   -3.63494307439  
0.565504342537  0.172993223068   -0.255878722278 -0.0363005574798 0.0350350445222  -0.0069060272388 -0.13476843342   
-0.0073232841049 0.432777110314   -0.204399191527  
2 ? 'X-RAY DIFFRACTION' refined -8.60249266517  -8.11668466197 -23.7830083284 0.153436256372 0.160942453252 0.204643820702 
0.0127085351779   -0.0041862609598 -0.0332166914258 1.73928220434 4.80349145922 4.95698166735 -1.37827858882   1.21904636724   
-3.44946386473  -0.0894840907144 0.155303383095  0.13791315663    -0.0584053481481 0.0376065050681  0.170725053587   
-0.290425199884  -0.0115117385357 0.0369940009256  
3 ? 'X-RAY DIFFRACTION' refined -0.838744239006 -16.3895635995 -25.057115913  0.155874664819 0.092741528355 0.169134563017 
0.0153742503802   -0.0300116956796 -0.0483124324926 3.21501116118 1.80538611509 4.01055109629 -0.451813389638  -0.346513113369 
-1.40055577463  -0.0583591447196 0.113829373136  -0.0163712256875 -0.113467912154  0.0612003133993  -0.0273731352359 
0.218980195163   0.0586441377583  0.0153233037203  
4 ? 'X-RAY DIFFRACTION' refined 12.3490275149   -5.93954289127 -12.6559630465 0.257167778084 0.454596272642 0.370426163328 
-0.114105090557   0.0334884837862  -0.143074238803  2.01112143077 4.50347922669 6.30682826791 1.6712793044     1.05432310311   
0.625982713039  0.697941661469   -1.07966183677  0.933793196783   0.354019552795   -0.193494183636  -0.201777574806  
-0.72780706597   1.32228097684    -0.268549052385  
5 ? 'X-RAY DIFFRACTION' refined 0.926813911007  -19.3456719023 -27.8575771085 0.157762199778 0.137689850279 0.199494946684 
-0.00822028942999 -0.0124603632243 -0.0387254309991 3.67463761699 2.32933810398 3.14988518746 -1.40524441267   0.852429553311  
-0.428999946312 0.158288591907   0.288117429793  -0.309897011296  -0.203579910617  -0.0457608197504 0.198999433011   
0.190128785663   0.0580659163537  -0.114833970634  
6 ? 'X-RAY DIFFRACTION' refined -5.61391728211  -20.21104019   -10.3573460692 0.112756558145 0.153202984994 0.166231751858 
-0.0395567057796  -0.0341735213252 0.00239207978969 3.80695838351 4.43555326089 6.40594156328 -1.27273164335   -0.883587427032 
-0.809532139486 -0.173243385631  -0.431066043243 -0.198201716345  0.342729315205   0.129904131224   0.0316177056002  
0.391507107397   -0.0665333672737 0.0418010463262  
7 ? 'X-RAY DIFFRACTION' refined -13.9646188778  -13.3903677315 -14.7585234353 0.150971412018 0.171740171573 0.118996966088 
0.0232746315269   -0.0121134862627 -0.028464745981  6.09493530143 1.60164421642 5.72657356547 -0.0453998335122 -0.289086000007 
-1.00515763004  0.0588608032215  -0.250155088996 -0.033462004565  0.429564354661   -0.0407751528756 -0.0821167276103 
-0.212239700251  -0.295350548467  0.00971886348657 
# 
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 83  A 68  . 
;chain 'A' and (resid 41 through 83 )
;
3 3 'X-RAY DIFFRACTION' A 84  A 69  A 110 A 95  . 
;chain 'A' and (resid 84 through 110 )
;
4 4 'X-RAY DIFFRACTION' A 111 A 96  A 136 A 121 . 
;chain 'A' and (resid 111 through 136 )
;
5 5 'X-RAY DIFFRACTION' A 137 A 122 A 182 A 167 . 
;chain 'A' and (resid 137 through 182 )
;
6 6 'X-RAY DIFFRACTION' A 183 A 168 A 210 A 195 . 
;chain 'A' and (resid 183 through 210 )
;
7 7 'X-RAY DIFFRACTION' A 211 A 196 A 224 A 209 . 
;chain 'A' and (resid 211 through 224 )
;
# 
_pdbx_distant_solvent_atoms.id                                1 
_pdbx_distant_solvent_atoms.PDB_model_num                     1 
_pdbx_distant_solvent_atoms.auth_atom_id                      O 
_pdbx_distant_solvent_atoms.label_alt_id                      ? 
_pdbx_distant_solvent_atoms.auth_asym_id                      A 
_pdbx_distant_solvent_atoms.auth_comp_id                      HOH 
_pdbx_distant_solvent_atoms.auth_seq_id                       689 
_pdbx_distant_solvent_atoms.PDB_ins_code                      ? 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance   5.92 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance          . 
# 
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 
A1AY4 S1   S N N 1   
A1AY4 C1   C N N 2   
A1AY4 C2   C Y N 3   
A1AY4 C3   C Y N 4   
A1AY4 C4   C Y N 5   
A1AY4 C5   C Y N 6   
A1AY4 C6   C Y N 7   
A1AY4 C7   C Y N 8   
A1AY4 C8   C N N 9   
A1AY4 N1   N N N 10  
A1AY4 N2   N N N 11  
A1AY4 O1   O N N 12  
A1AY4 O2   O N N 13  
A1AY4 O3   O N N 14  
A1AY4 O4   O N N 15  
A1AY4 H12  H N N 16  
A1AY4 H11  H N N 17  
A1AY4 H13  H N N 18  
A1AY4 H3   H N N 19  
A1AY4 H4   H N N 20  
A1AY4 H6   H N N 21  
A1AY4 H22  H N N 22  
A1AY4 H21  H N N 23  
ALA   N    N N N 24  
ALA   CA   C N S 25  
ALA   C    C N N 26  
ALA   O    O N N 27  
ALA   CB   C N N 28  
ALA   OXT  O N N 29  
ALA   H    H N N 30  
ALA   H2   H N N 31  
ALA   HA   H N N 32  
ALA   HB1  H N N 33  
ALA   HB2  H N N 34  
ALA   HB3  H N N 35  
ALA   HXT  H N N 36  
ARG   N    N N N 37  
ARG   CA   C N S 38  
ARG   C    C N N 39  
ARG   O    O N N 40  
ARG   CB   C N N 41  
ARG   CG   C N N 42  
ARG   CD   C N N 43  
ARG   NE   N N N 44  
ARG   CZ   C N N 45  
ARG   NH1  N N N 46  
ARG   NH2  N N N 47  
ARG   OXT  O N N 48  
ARG   H    H N N 49  
ARG   H2   H N N 50  
ARG   HA   H N N 51  
ARG   HB2  H N N 52  
ARG   HB3  H N N 53  
ARG   HG2  H N N 54  
ARG   HG3  H N N 55  
ARG   HD2  H N N 56  
ARG   HD3  H N N 57  
ARG   HE   H N N 58  
ARG   HH11 H N N 59  
ARG   HH12 H N N 60  
ARG   HH21 H N N 61  
ARG   HH22 H N N 62  
ARG   HXT  H N N 63  
ASN   N    N N N 64  
ASN   CA   C N S 65  
ASN   C    C N N 66  
ASN   O    O N N 67  
ASN   CB   C N N 68  
ASN   CG   C N N 69  
ASN   OD1  O N N 70  
ASN   ND2  N N N 71  
ASN   OXT  O N N 72  
ASN   H    H N N 73  
ASN   H2   H N N 74  
ASN   HA   H N N 75  
ASN   HB2  H N N 76  
ASN   HB3  H N N 77  
ASN   HD21 H N N 78  
ASN   HD22 H N N 79  
ASN   HXT  H N N 80  
ASP   N    N N N 81  
ASP   CA   C N S 82  
ASP   C    C N N 83  
ASP   O    O N N 84  
ASP   CB   C N N 85  
ASP   CG   C N N 86  
ASP   OD1  O N N 87  
ASP   OD2  O N N 88  
ASP   OXT  O N N 89  
ASP   H    H N N 90  
ASP   H2   H N N 91  
ASP   HA   H N N 92  
ASP   HB2  H N N 93  
ASP   HB3  H N N 94  
ASP   HD2  H N N 95  
ASP   HXT  H N N 96  
GLN   N    N N N 97  
GLN   CA   C N S 98  
GLN   C    C N N 99  
GLN   O    O N N 100 
GLN   CB   C N N 101 
GLN   CG   C N N 102 
GLN   CD   C N N 103 
GLN   OE1  O N N 104 
GLN   NE2  N N N 105 
GLN   OXT  O N N 106 
GLN   H    H N N 107 
GLN   H2   H N N 108 
GLN   HA   H N N 109 
GLN   HB2  H N N 110 
GLN   HB3  H N N 111 
GLN   HG2  H N N 112 
GLN   HG3  H N N 113 
GLN   HE21 H N N 114 
GLN   HE22 H N N 115 
GLN   HXT  H N N 116 
GLU   N    N N N 117 
GLU   CA   C N S 118 
GLU   C    C N N 119 
GLU   O    O N N 120 
GLU   CB   C N N 121 
GLU   CG   C N N 122 
GLU   CD   C N N 123 
GLU   OE1  O N N 124 
GLU   OE2  O N N 125 
GLU   OXT  O N N 126 
GLU   H    H N N 127 
GLU   H2   H N N 128 
GLU   HA   H N N 129 
GLU   HB2  H N N 130 
GLU   HB3  H N N 131 
GLU   HG2  H N N 132 
GLU   HG3  H N N 133 
GLU   HE2  H N N 134 
GLU   HXT  H N N 135 
GLY   N    N N N 136 
GLY   CA   C N N 137 
GLY   C    C N N 138 
GLY   O    O N N 139 
GLY   OXT  O N N 140 
GLY   H    H N N 141 
GLY   H2   H N N 142 
GLY   HA2  H N N 143 
GLY   HA3  H N N 144 
GLY   HXT  H N N 145 
HIS   N    N N N 146 
HIS   CA   C N S 147 
HIS   C    C N N 148 
HIS   O    O N N 149 
HIS   CB   C N N 150 
HIS   CG   C Y N 151 
HIS   ND1  N Y N 152 
HIS   CD2  C Y N 153 
HIS   CE1  C Y N 154 
HIS   NE2  N Y N 155 
HIS   OXT  O N N 156 
HIS   H    H N N 157 
HIS   H2   H N N 158 
HIS   HA   H N N 159 
HIS   HB2  H N N 160 
HIS   HB3  H N N 161 
HIS   HD1  H N N 162 
HIS   HD2  H N N 163 
HIS   HE1  H N N 164 
HIS   HE2  H N N 165 
HIS   HXT  H N N 166 
HOH   O    O N N 167 
HOH   H1   H N N 168 
HOH   H2   H N N 169 
ILE   N    N N N 170 
ILE   CA   C N S 171 
ILE   C    C N N 172 
ILE   O    O N N 173 
ILE   CB   C N S 174 
ILE   CG1  C N N 175 
ILE   CG2  C N N 176 
ILE   CD1  C N N 177 
ILE   OXT  O N N 178 
ILE   H    H N N 179 
ILE   H2   H N N 180 
ILE   HA   H N N 181 
ILE   HB   H N N 182 
ILE   HG12 H N N 183 
ILE   HG13 H N N 184 
ILE   HG21 H N N 185 
ILE   HG22 H N N 186 
ILE   HG23 H N N 187 
ILE   HD11 H N N 188 
ILE   HD12 H N N 189 
ILE   HD13 H N N 190 
ILE   HXT  H N N 191 
LEU   N    N N N 192 
LEU   CA   C N S 193 
LEU   C    C N N 194 
LEU   O    O N N 195 
LEU   CB   C N N 196 
LEU   CG   C N N 197 
LEU   CD1  C N N 198 
LEU   CD2  C N N 199 
LEU   OXT  O N N 200 
LEU   H    H N N 201 
LEU   H2   H N N 202 
LEU   HA   H N N 203 
LEU   HB2  H N N 204 
LEU   HB3  H N N 205 
LEU   HG   H N N 206 
LEU   HD11 H N N 207 
LEU   HD12 H N N 208 
LEU   HD13 H N N 209 
LEU   HD21 H N N 210 
LEU   HD22 H N N 211 
LEU   HD23 H N N 212 
LEU   HXT  H N N 213 
LYS   N    N N N 214 
LYS   CA   C N S 215 
LYS   C    C N N 216 
LYS   O    O N N 217 
LYS   CB   C N N 218 
LYS   CG   C N N 219 
LYS   CD   C N N 220 
LYS   CE   C N N 221 
LYS   NZ   N N N 222 
LYS   OXT  O N N 223 
LYS   H    H N N 224 
LYS   H2   H N N 225 
LYS   HA   H N N 226 
LYS   HB2  H N N 227 
LYS   HB3  H N N 228 
LYS   HG2  H N N 229 
LYS   HG3  H N N 230 
LYS   HD2  H N N 231 
LYS   HD3  H N N 232 
LYS   HE2  H N N 233 
LYS   HE3  H N N 234 
LYS   HZ1  H N N 235 
LYS   HZ2  H N N 236 
LYS   HZ3  H N N 237 
LYS   HXT  H N N 238 
MET   N    N N N 239 
MET   CA   C N S 240 
MET   C    C N N 241 
MET   O    O N N 242 
MET   CB   C N N 243 
MET   CG   C N N 244 
MET   SD   S N N 245 
MET   CE   C N N 246 
MET   OXT  O N N 247 
MET   H    H N N 248 
MET   H2   H N N 249 
MET   HA   H N N 250 
MET   HB2  H N N 251 
MET   HB3  H N N 252 
MET   HG2  H N N 253 
MET   HG3  H N N 254 
MET   HE1  H N N 255 
MET   HE2  H N N 256 
MET   HE3  H N N 257 
MET   HXT  H N N 258 
PHE   N    N N N 259 
PHE   CA   C N S 260 
PHE   C    C N N 261 
PHE   O    O N N 262 
PHE   CB   C N N 263 
PHE   CG   C Y N 264 
PHE   CD1  C Y N 265 
PHE   CD2  C Y N 266 
PHE   CE1  C Y N 267 
PHE   CE2  C Y N 268 
PHE   CZ   C Y N 269 
PHE   OXT  O N N 270 
PHE   H    H N N 271 
PHE   H2   H N N 272 
PHE   HA   H N N 273 
PHE   HB2  H N N 274 
PHE   HB3  H N N 275 
PHE   HD1  H N N 276 
PHE   HD2  H N N 277 
PHE   HE1  H N N 278 
PHE   HE2  H N N 279 
PHE   HZ   H N N 280 
PHE   HXT  H N N 281 
PRO   N    N N N 282 
PRO   CA   C N S 283 
PRO   C    C N N 284 
PRO   O    O N N 285 
PRO   CB   C N N 286 
PRO   CG   C N N 287 
PRO   CD   C N N 288 
PRO   OXT  O N N 289 
PRO   H    H N N 290 
PRO   HA   H N N 291 
PRO   HB2  H N N 292 
PRO   HB3  H N N 293 
PRO   HG2  H N N 294 
PRO   HG3  H N N 295 
PRO   HD2  H N N 296 
PRO   HD3  H N N 297 
PRO   HXT  H N N 298 
SER   N    N N N 299 
SER   CA   C N S 300 
SER   C    C N N 301 
SER   O    O N N 302 
SER   CB   C N N 303 
SER   OG   O N N 304 
SER   OXT  O N N 305 
SER   H    H N N 306 
SER   H2   H N N 307 
SER   HA   H N N 308 
SER   HB2  H N N 309 
SER   HB3  H N N 310 
SER   HG   H N N 311 
SER   HXT  H N N 312 
THR   N    N N N 313 
THR   CA   C N S 314 
THR   C    C N N 315 
THR   O    O N N 316 
THR   CB   C N R 317 
THR   OG1  O N N 318 
THR   CG2  C N N 319 
THR   OXT  O N N 320 
THR   H    H N N 321 
THR   H2   H N N 322 
THR   HA   H N N 323 
THR   HB   H N N 324 
THR   HG1  H N N 325 
THR   HG21 H N N 326 
THR   HG22 H N N 327 
THR   HG23 H N N 328 
THR   HXT  H N N 329 
TRP   N    N N N 330 
TRP   CA   C N S 331 
TRP   C    C N N 332 
TRP   O    O N N 333 
TRP   CB   C N N 334 
TRP   CG   C Y N 335 
TRP   CD1  C Y N 336 
TRP   CD2  C Y N 337 
TRP   NE1  N Y N 338 
TRP   CE2  C Y N 339 
TRP   CE3  C Y N 340 
TRP   CZ2  C Y N 341 
TRP   CZ3  C Y N 342 
TRP   CH2  C Y N 343 
TRP   OXT  O N N 344 
TRP   H    H N N 345 
TRP   H2   H N N 346 
TRP   HA   H N N 347 
TRP   HB2  H N N 348 
TRP   HB3  H N N 349 
TRP   HD1  H N N 350 
TRP   HE1  H N N 351 
TRP   HE3  H N N 352 
TRP   HZ2  H N N 353 
TRP   HZ3  H N N 354 
TRP   HH2  H N N 355 
TRP   HXT  H N N 356 
TYR   N    N N N 357 
TYR   CA   C N S 358 
TYR   C    C N N 359 
TYR   O    O N N 360 
TYR   CB   C N N 361 
TYR   CG   C Y N 362 
TYR   CD1  C Y N 363 
TYR   CD2  C Y N 364 
TYR   CE1  C Y N 365 
TYR   CE2  C Y N 366 
TYR   CZ   C Y N 367 
TYR   OH   O N N 368 
TYR   OXT  O N N 369 
TYR   H    H N N 370 
TYR   H2   H N N 371 
TYR   HA   H N N 372 
TYR   HB2  H N N 373 
TYR   HB3  H N N 374 
TYR   HD1  H N N 375 
TYR   HD2  H N N 376 
TYR   HE1  H N N 377 
TYR   HE2  H N N 378 
TYR   HH   H N N 379 
TYR   HXT  H N N 380 
VAL   N    N N N 381 
VAL   CA   C N S 382 
VAL   C    C N N 383 
VAL   O    O N N 384 
VAL   CB   C N N 385 
VAL   CG1  C N N 386 
VAL   CG2  C N N 387 
VAL   OXT  O N N 388 
VAL   H    H N N 389 
VAL   H2   H N N 390 
VAL   HA   H N N 391 
VAL   HB   H N N 392 
VAL   HG11 H N N 393 
VAL   HG12 H N N 394 
VAL   HG13 H N N 395 
VAL   HG21 H N N 396 
VAL   HG22 H N N 397 
VAL   HG23 H N N 398 
VAL   HXT  H N N 399 
# 
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 
A1AY4 C1  N1   sing N N 1   
A1AY4 N1  C2   sing N N 2   
A1AY4 N1  C8   sing N N 3   
A1AY4 C2  C3   doub Y N 4   
A1AY4 C2  C7   sing Y N 5   
A1AY4 C3  C4   sing Y N 6   
A1AY4 C4  C5   doub Y N 7   
A1AY4 C5  C6   sing Y N 8   
A1AY4 C5  S1   sing N N 9   
A1AY4 C6  C7   doub Y N 10  
A1AY4 C7  O1   sing N N 11  
A1AY4 O1  C8   sing N N 12  
A1AY4 C8  O2   doub N N 13  
A1AY4 S1  N2   sing N N 14  
A1AY4 S1  O3   doub N N 15  
A1AY4 S1  O4   doub N N 16  
A1AY4 C1  H12  sing N N 17  
A1AY4 C1  H11  sing N N 18  
A1AY4 C1  H13  sing N N 19  
A1AY4 C3  H3   sing N N 20  
A1AY4 C4  H4   sing N N 21  
A1AY4 C6  H6   sing N N 22  
A1AY4 N2  H22  sing N N 23  
A1AY4 N2  H21  sing N N 24  
ALA   N   CA   sing N N 25  
ALA   N   H    sing N N 26  
ALA   N   H2   sing N N 27  
ALA   CA  C    sing N N 28  
ALA   CA  CB   sing N N 29  
ALA   CA  HA   sing N N 30  
ALA   C   O    doub N N 31  
ALA   C   OXT  sing N N 32  
ALA   CB  HB1  sing N N 33  
ALA   CB  HB2  sing N N 34  
ALA   CB  HB3  sing N N 35  
ALA   OXT HXT  sing N N 36  
ARG   N   CA   sing N N 37  
ARG   N   H    sing N N 38  
ARG   N   H2   sing N N 39  
ARG   CA  C    sing N N 40  
ARG   CA  CB   sing N N 41  
ARG   CA  HA   sing N N 42  
ARG   C   O    doub N N 43  
ARG   C   OXT  sing N N 44  
ARG   CB  CG   sing N N 45  
ARG   CB  HB2  sing N N 46  
ARG   CB  HB3  sing N N 47  
ARG   CG  CD   sing N N 48  
ARG   CG  HG2  sing N N 49  
ARG   CG  HG3  sing N N 50  
ARG   CD  NE   sing N N 51  
ARG   CD  HD2  sing N N 52  
ARG   CD  HD3  sing N N 53  
ARG   NE  CZ   sing N N 54  
ARG   NE  HE   sing N N 55  
ARG   CZ  NH1  sing N N 56  
ARG   CZ  NH2  doub N N 57  
ARG   NH1 HH11 sing N N 58  
ARG   NH1 HH12 sing N N 59  
ARG   NH2 HH21 sing N N 60  
ARG   NH2 HH22 sing N N 61  
ARG   OXT HXT  sing N N 62  
ASN   N   CA   sing N N 63  
ASN   N   H    sing N N 64  
ASN   N   H2   sing N N 65  
ASN   CA  C    sing N N 66  
ASN   CA  CB   sing N N 67  
ASN   CA  HA   sing N N 68  
ASN   C   O    doub N N 69  
ASN   C   OXT  sing N N 70  
ASN   CB  CG   sing N N 71  
ASN   CB  HB2  sing N N 72  
ASN   CB  HB3  sing N N 73  
ASN   CG  OD1  doub N N 74  
ASN   CG  ND2  sing N N 75  
ASN   ND2 HD21 sing N N 76  
ASN   ND2 HD22 sing N N 77  
ASN   OXT HXT  sing N N 78  
ASP   N   CA   sing N N 79  
ASP   N   H    sing N N 80  
ASP   N   H2   sing N N 81  
ASP   CA  C    sing N N 82  
ASP   CA  CB   sing N N 83  
ASP   CA  HA   sing N N 84  
ASP   C   O    doub N N 85  
ASP   C   OXT  sing N N 86  
ASP   CB  CG   sing N N 87  
ASP   CB  HB2  sing N N 88  
ASP   CB  HB3  sing N N 89  
ASP   CG  OD1  doub N N 90  
ASP   CG  OD2  sing N N 91  
ASP   OD2 HD2  sing N N 92  
ASP   OXT HXT  sing N N 93  
GLN   N   CA   sing N N 94  
GLN   N   H    sing N N 95  
GLN   N   H2   sing N N 96  
GLN   CA  C    sing N N 97  
GLN   CA  CB   sing N N 98  
GLN   CA  HA   sing N N 99  
GLN   C   O    doub N N 100 
GLN   C   OXT  sing N N 101 
GLN   CB  CG   sing N N 102 
GLN   CB  HB2  sing N N 103 
GLN   CB  HB3  sing N N 104 
GLN   CG  CD   sing N N 105 
GLN   CG  HG2  sing N N 106 
GLN   CG  HG3  sing N N 107 
GLN   CD  OE1  doub N N 108 
GLN   CD  NE2  sing N N 109 
GLN   NE2 HE21 sing N N 110 
GLN   NE2 HE22 sing N N 111 
GLN   OXT HXT  sing N N 112 
GLU   N   CA   sing N N 113 
GLU   N   H    sing N N 114 
GLU   N   H2   sing N N 115 
GLU   CA  C    sing N N 116 
GLU   CA  CB   sing N N 117 
GLU   CA  HA   sing N N 118 
GLU   C   O    doub N N 119 
GLU   C   OXT  sing N N 120 
GLU   CB  CG   sing N N 121 
GLU   CB  HB2  sing N N 122 
GLU   CB  HB3  sing N N 123 
GLU   CG  CD   sing N N 124 
GLU   CG  HG2  sing N N 125 
GLU   CG  HG3  sing N N 126 
GLU   CD  OE1  doub N N 127 
GLU   CD  OE2  sing N N 128 
GLU   OE2 HE2  sing N N 129 
GLU   OXT HXT  sing N N 130 
GLY   N   CA   sing N N 131 
GLY   N   H    sing N N 132 
GLY   N   H2   sing N N 133 
GLY   CA  C    sing N N 134 
GLY   CA  HA2  sing N N 135 
GLY   CA  HA3  sing N N 136 
GLY   C   O    doub N N 137 
GLY   C   OXT  sing N N 138 
GLY   OXT HXT  sing N N 139 
HIS   N   CA   sing N N 140 
HIS   N   H    sing N N 141 
HIS   N   H2   sing N N 142 
HIS   CA  C    sing N N 143 
HIS   CA  CB   sing N N 144 
HIS   CA  HA   sing N N 145 
HIS   C   O    doub N N 146 
HIS   C   OXT  sing N N 147 
HIS   CB  CG   sing N N 148 
HIS   CB  HB2  sing N N 149 
HIS   CB  HB3  sing N N 150 
HIS   CG  ND1  sing Y N 151 
HIS   CG  CD2  doub Y N 152 
HIS   ND1 CE1  doub Y N 153 
HIS   ND1 HD1  sing N N 154 
HIS   CD2 NE2  sing Y N 155 
HIS   CD2 HD2  sing N N 156 
HIS   CE1 NE2  sing Y N 157 
HIS   CE1 HE1  sing N N 158 
HIS   NE2 HE2  sing N N 159 
HIS   OXT HXT  sing N N 160 
HOH   O   H1   sing N N 161 
HOH   O   H2   sing N N 162 
ILE   N   CA   sing N N 163 
ILE   N   H    sing N N 164 
ILE   N   H2   sing N N 165 
ILE   CA  C    sing N N 166 
ILE   CA  CB   sing N N 167 
ILE   CA  HA   sing N N 168 
ILE   C   O    doub N N 169 
ILE   C   OXT  sing N N 170 
ILE   CB  CG1  sing N N 171 
ILE   CB  CG2  sing N N 172 
ILE   CB  HB   sing N N 173 
ILE   CG1 CD1  sing N N 174 
ILE   CG1 HG12 sing N N 175 
ILE   CG1 HG13 sing N N 176 
ILE   CG2 HG21 sing N N 177 
ILE   CG2 HG22 sing N N 178 
ILE   CG2 HG23 sing N N 179 
ILE   CD1 HD11 sing N N 180 
ILE   CD1 HD12 sing N N 181 
ILE   CD1 HD13 sing N N 182 
ILE   OXT HXT  sing N N 183 
LEU   N   CA   sing N N 184 
LEU   N   H    sing N N 185 
LEU   N   H2   sing N N 186 
LEU   CA  C    sing N N 187 
LEU   CA  CB   sing N N 188 
LEU   CA  HA   sing N N 189 
LEU   C   O    doub N N 190 
LEU   C   OXT  sing N N 191 
LEU   CB  CG   sing N N 192 
LEU   CB  HB2  sing N N 193 
LEU   CB  HB3  sing N N 194 
LEU   CG  CD1  sing N N 195 
LEU   CG  CD2  sing N N 196 
LEU   CG  HG   sing N N 197 
LEU   CD1 HD11 sing N N 198 
LEU   CD1 HD12 sing N N 199 
LEU   CD1 HD13 sing N N 200 
LEU   CD2 HD21 sing N N 201 
LEU   CD2 HD22 sing N N 202 
LEU   CD2 HD23 sing N N 203 
LEU   OXT HXT  sing N N 204 
LYS   N   CA   sing N N 205 
LYS   N   H    sing N N 206 
LYS   N   H2   sing N N 207 
LYS   CA  C    sing N N 208 
LYS   CA  CB   sing N N 209 
LYS   CA  HA   sing N N 210 
LYS   C   O    doub N N 211 
LYS   C   OXT  sing N N 212 
LYS   CB  CG   sing N N 213 
LYS   CB  HB2  sing N N 214 
LYS   CB  HB3  sing N N 215 
LYS   CG  CD   sing N N 216 
LYS   CG  HG2  sing N N 217 
LYS   CG  HG3  sing N N 218 
LYS   CD  CE   sing N N 219 
LYS   CD  HD2  sing N N 220 
LYS   CD  HD3  sing N N 221 
LYS   CE  NZ   sing N N 222 
LYS   CE  HE2  sing N N 223 
LYS   CE  HE3  sing N N 224 
LYS   NZ  HZ1  sing N N 225 
LYS   NZ  HZ2  sing N N 226 
LYS   NZ  HZ3  sing N N 227 
LYS   OXT HXT  sing N N 228 
MET   N   CA   sing N N 229 
MET   N   H    sing N N 230 
MET   N   H2   sing N N 231 
MET   CA  C    sing N N 232 
MET   CA  CB   sing N N 233 
MET   CA  HA   sing N N 234 
MET   C   O    doub N N 235 
MET   C   OXT  sing N N 236 
MET   CB  CG   sing N N 237 
MET   CB  HB2  sing N N 238 
MET   CB  HB3  sing N N 239 
MET   CG  SD   sing N N 240 
MET   CG  HG2  sing N N 241 
MET   CG  HG3  sing N N 242 
MET   SD  CE   sing N N 243 
MET   CE  HE1  sing N N 244 
MET   CE  HE2  sing N N 245 
MET   CE  HE3  sing N N 246 
MET   OXT HXT  sing N N 247 
PHE   N   CA   sing N N 248 
PHE   N   H    sing N N 249 
PHE   N   H2   sing N N 250 
PHE   CA  C    sing N N 251 
PHE   CA  CB   sing N N 252 
PHE   CA  HA   sing N N 253 
PHE   C   O    doub N N 254 
PHE   C   OXT  sing N N 255 
PHE   CB  CG   sing N N 256 
PHE   CB  HB2  sing N N 257 
PHE   CB  HB3  sing N N 258 
PHE   CG  CD1  doub Y N 259 
PHE   CG  CD2  sing Y N 260 
PHE   CD1 CE1  sing Y N 261 
PHE   CD1 HD1  sing N N 262 
PHE   CD2 CE2  doub Y N 263 
PHE   CD2 HD2  sing N N 264 
PHE   CE1 CZ   doub Y N 265 
PHE   CE1 HE1  sing N N 266 
PHE   CE2 CZ   sing Y N 267 
PHE   CE2 HE2  sing N N 268 
PHE   CZ  HZ   sing N N 269 
PHE   OXT HXT  sing N N 270 
PRO   N   CA   sing N N 271 
PRO   N   CD   sing N N 272 
PRO   N   H    sing N N 273 
PRO   CA  C    sing N N 274 
PRO   CA  CB   sing N N 275 
PRO   CA  HA   sing N N 276 
PRO   C   O    doub N N 277 
PRO   C   OXT  sing N N 278 
PRO   CB  CG   sing N N 279 
PRO   CB  HB2  sing N N 280 
PRO   CB  HB3  sing N N 281 
PRO   CG  CD   sing N N 282 
PRO   CG  HG2  sing N N 283 
PRO   CG  HG3  sing N N 284 
PRO   CD  HD2  sing N N 285 
PRO   CD  HD3  sing N N 286 
PRO   OXT HXT  sing N N 287 
SER   N   CA   sing N N 288 
SER   N   H    sing N N 289 
SER   N   H2   sing N N 290 
SER   CA  C    sing N N 291 
SER   CA  CB   sing N N 292 
SER   CA  HA   sing N N 293 
SER   C   O    doub N N 294 
SER   C   OXT  sing N N 295 
SER   CB  OG   sing N N 296 
SER   CB  HB2  sing N N 297 
SER   CB  HB3  sing N N 298 
SER   OG  HG   sing N N 299 
SER   OXT HXT  sing N N 300 
THR   N   CA   sing N N 301 
THR   N   H    sing N N 302 
THR   N   H2   sing N N 303 
THR   CA  C    sing N N 304 
THR   CA  CB   sing N N 305 
THR   CA  HA   sing N N 306 
THR   C   O    doub N N 307 
THR   C   OXT  sing N N 308 
THR   CB  OG1  sing N N 309 
THR   CB  CG2  sing N N 310 
THR   CB  HB   sing N N 311 
THR   OG1 HG1  sing N N 312 
THR   CG2 HG21 sing N N 313 
THR   CG2 HG22 sing N N 314 
THR   CG2 HG23 sing N N 315 
THR   OXT HXT  sing N N 316 
TRP   N   CA   sing N N 317 
TRP   N   H    sing N N 318 
TRP   N   H2   sing N N 319 
TRP   CA  C    sing N N 320 
TRP   CA  CB   sing N N 321 
TRP   CA  HA   sing N N 322 
TRP   C   O    doub N N 323 
TRP   C   OXT  sing N N 324 
TRP   CB  CG   sing N N 325 
TRP   CB  HB2  sing N N 326 
TRP   CB  HB3  sing N N 327 
TRP   CG  CD1  doub Y N 328 
TRP   CG  CD2  sing Y N 329 
TRP   CD1 NE1  sing Y N 330 
TRP   CD1 HD1  sing N N 331 
TRP   CD2 CE2  doub Y N 332 
TRP   CD2 CE3  sing Y N 333 
TRP   NE1 CE2  sing Y N 334 
TRP   NE1 HE1  sing N N 335 
TRP   CE2 CZ2  sing Y N 336 
TRP   CE3 CZ3  doub Y N 337 
TRP   CE3 HE3  sing N N 338 
TRP   CZ2 CH2  doub Y N 339 
TRP   CZ2 HZ2  sing N N 340 
TRP   CZ3 CH2  sing Y N 341 
TRP   CZ3 HZ3  sing N N 342 
TRP   CH2 HH2  sing N N 343 
TRP   OXT HXT  sing N N 344 
TYR   N   CA   sing N N 345 
TYR   N   H    sing N N 346 
TYR   N   H2   sing N N 347 
TYR   CA  C    sing N N 348 
TYR   CA  CB   sing N N 349 
TYR   CA  HA   sing N N 350 
TYR   C   O    doub N N 351 
TYR   C   OXT  sing N N 352 
TYR   CB  CG   sing N N 353 
TYR   CB  HB2  sing N N 354 
TYR   CB  HB3  sing N N 355 
TYR   CG  CD1  doub Y N 356 
TYR   CG  CD2  sing Y N 357 
TYR   CD1 CE1  sing Y N 358 
TYR   CD1 HD1  sing N N 359 
TYR   CD2 CE2  doub Y N 360 
TYR   CD2 HD2  sing N N 361 
TYR   CE1 CZ   doub Y N 362 
TYR   CE1 HE1  sing N N 363 
TYR   CE2 CZ   sing Y N 364 
TYR   CE2 HE2  sing N N 365 
TYR   CZ  OH   sing N N 366 
TYR   OH  HH   sing N N 367 
TYR   OXT HXT  sing N N 368 
VAL   N   CA   sing N N 369 
VAL   N   H    sing N N 370 
VAL   N   H2   sing N N 371 
VAL   CA  C    sing N N 372 
VAL   CA  CB   sing N N 373 
VAL   CA  HA   sing N N 374 
VAL   C   O    doub N N 375 
VAL   C   OXT  sing N N 376 
VAL   CB  CG1  sing N N 377 
VAL   CB  CG2  sing N N 378 
VAL   CB  HB   sing N N 379 
VAL   CG1 HG11 sing N N 380 
VAL   CG1 HG12 sing N N 381 
VAL   CG1 HG13 sing N N 382 
VAL   CG2 HG21 sing N N 383 
VAL   CG2 HG22 sing N N 384 
VAL   CG2 HG23 sing N N 385 
VAL   OXT HXT  sing N N 386 
# 
_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                    7HBB 
_atom_sites.fract_transf_matrix[1][1]   0.015138 
_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]   0.011089 
_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]   0.009982 
_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   ? 4.30445   -28.43330 -39.07243 1.000 53.75435  ? 16  GLU   A N   1 
ATOM   2    C CA  . GLU   A 1 9   ? 5.58006   -27.73957 -39.19518 1.000 62.42066  ? 16  GLU   A CA  1 
ATOM   3    C C   . GLU   A 1 9   ? 5.87001   -26.90279 -37.95004 1.000 51.08350  ? 16  GLU   A C   1 
ATOM   4    O O   . GLU   A 1 9   ? 5.22828   -25.87661 -37.71591 1.000 54.84406  ? 16  GLU   A O   1 
ATOM   5    C CB  . GLU   A 1 9   ? 5.58828   -26.85357 -40.44017 1.000 76.94978  ? 16  GLU   A CB  1 
ATOM   6    C CG  . GLU   A 1 9   ? 6.76090   -25.89087 -40.50994 1.000 82.76201  ? 16  GLU   A CG  1 
ATOM   7    C CD  . GLU   A 1 9   ? 8.08151   -26.61092 -40.65318 1.000 90.03382  ? 16  GLU   A CD  1 
ATOM   8    O OE1 . GLU   A 1 9   ? 8.44263   -26.99301 -41.78855 1.000 97.99016  ? 16  GLU   A OE1 1 
ATOM   9    O OE2 . GLU   A 1 9   ? 8.75468   -26.80042 -39.61833 1.000 81.81620  ? 16  GLU   A OE2 1 
ATOM   10   N N   . VAL   A 1 10  ? 6.84849   -27.34026 -37.16090 1.000 38.01175  ? 17  VAL   A N   1 
ATOM   11   C CA  . VAL   A 1 10  ? 7.14869   -26.75065 -35.86049 1.000 34.43122  ? 17  VAL   A CA  1 
ATOM   12   C C   . VAL   A 1 10  ? 8.51119   -26.07725 -35.93083 1.000 37.88654  ? 17  VAL   A C   1 
ATOM   13   O O   . VAL   A 1 10  ? 9.51042   -26.71763 -36.27541 1.000 37.75322  ? 17  VAL   A O   1 
ATOM   14   C CB  . VAL   A 1 10  ? 7.11966   -27.80652 -34.74803 1.000 39.38272  ? 17  VAL   A CB  1 
ATOM   15   C CG1 . VAL   A 1 10  ? 7.34069   -27.15004 -33.40618 1.000 36.23409  ? 17  VAL   A CG1 1 
ATOM   16   C CG2 . VAL   A 1 10  ? 5.80030   -28.56558 -34.77383 1.000 54.86447  ? 17  VAL   A CG2 1 
ATOM   17   N N   . GLU   A 1 11  ? 8.55404   -24.79251 -35.59109 1.000 29.27917  ? 18  GLU   A N   1 
ATOM   18   C CA  . GLU   A 1 11  ? 9.79397   -24.02888 -35.54719 1.000 26.85068  ? 18  GLU   A CA  1 
ATOM   19   C C   . GLU   A 1 11  ? 10.22743  -23.86677 -34.09661 1.000 25.63543  ? 18  GLU   A C   1 
ATOM   20   O O   . GLU   A 1 11  ? 9.43514   -23.43356 -33.25733 1.000 23.73020  ? 18  GLU   A O   1 
ATOM   21   C CB  . GLU   A 1 11  ? 9.60824   -22.65870 -36.19917 1.000 26.74933  ? 18  GLU   A CB  1 
ATOM   22   C CG  . GLU   A 1 11  ? 9.39977   -22.70500 -37.70774 1.000 29.72431  ? 18  GLU   A CG  1 
ATOM   23   C CD  . GLU   A 1 11  ? 9.19544   -21.32284 -38.30562 1.000 46.26691  ? 18  GLU   A CD  1 
ATOM   24   O OE1 . GLU   A 1 11  ? 8.11039   -20.73864 -38.09125 1.000 43.90448  ? 18  GLU   A OE1 1 
ATOM   25   O OE2 . GLU   A 1 11  ? 10.10927  -20.82038 -38.99046 1.000 44.49221  ? 18  GLU   A OE2 1 
ATOM   26   N N   . THR   A 1 12  ? 11.47917  -24.20885 -33.80512 1.000 23.63062  ? 19  THR   A N   1 
ATOM   27   C CA  . THR   A 1 12  ? 12.03287  -24.08132 -32.46310 1.000 21.86715  ? 19  THR   A CA  1 
ATOM   28   C C   . THR   A 1 12  ? 13.01913  -22.92305 -32.42732 1.000 22.39846  ? 19  THR   A C   1 
ATOM   29   O O   . THR   A 1 12  ? 13.90322  -22.82884 -33.28611 1.000 21.23529  ? 19  THR   A O   1 
ATOM   30   C CB  . THR   A 1 12  ? 12.72413  -25.37561 -32.03363 1.000 22.84959  ? 19  THR   A CB  1 
ATOM   31   O OG1 . THR   A 1 12  ? 11.82730  -26.47463 -32.22394 1.000 25.02118  ? 19  THR   A OG1 1 
ATOM   32   C CG2 . THR   A 1 12  ? 13.14224  -25.30717 -30.56313 1.000 21.55601  ? 19  THR   A CG2 1 
ATOM   33   N N   . PHE   A 1 13  ? 12.86985  -22.05776 -31.42582 1.000 19.14125  ? 20  PHE   A N   1 
ATOM   34   C CA  . PHE   A 1 13  ? 13.68189  -20.86412 -31.25822 1.000 18.92526  ? 20  PHE   A CA  1 
ATOM   35   C C   . PHE   A 1 13  ? 14.36405  -20.88804 -29.90001 1.000 25.57925  ? 20  PHE   A C   1 
ATOM   36   O O   . PHE   A 1 13  ? 13.83644  -21.44639 -28.93236 1.000 20.27229  ? 20  PHE   A O   1 
ATOM   37   C CB  . PHE   A 1 13  ? 12.83222  -19.58879 -31.32379 1.000 18.68535  ? 20  PHE   A CB  1 
ATOM   38   C CG  . PHE   A 1 13  ? 12.09656  -19.40365 -32.61353 1.000 20.77539  ? 20  PHE   A CG  1 
ATOM   39   C CD1 . PHE   A 1 13  ? 10.85356  -19.98912 -32.80228 1.000 23.05715  ? 20  PHE   A CD1 1 
ATOM   40   C CD2 . PHE   A 1 13  ? 12.62412  -18.61183 -33.62424 1.000 25.96029  ? 20  PHE   A CD2 1 
ATOM   41   C CE1 . PHE   A 1 13  ? 10.15960  -19.80889 -33.98831 1.000 23.92650  ? 20  PHE   A CE1 1 
ATOM   42   C CE2 . PHE   A 1 13  ? 11.93142  -18.42300 -34.80674 1.000 28.66887  ? 20  PHE   A CE2 1 
ATOM   43   C CZ  . PHE   A 1 13  ? 10.70234  -19.02706 -34.98942 1.000 25.77688  ? 20  PHE   A CZ  1 
ATOM   44   N N   . ALA   A 1 14  ? 15.52002  -20.23835 -29.82139 1.000 18.62697  ? 21  ALA   A N   1 
ATOM   45   C CA  . ALA   A 1 14  ? 16.15687  -19.98502 -28.53786 1.000 17.57122  ? 21  ALA   A CA  1 
ATOM   46   C C   . ALA   A 1 14  ? 15.68541  -18.64513 -27.98845 1.000 19.11685  ? 21  ALA   A C   1 
ATOM   47   O O   . ALA   A 1 14  ? 15.58247  -17.66267 -28.72998 1.000 18.64059  ? 21  ALA   A O   1 
ATOM   48   C CB  . ALA   A 1 14  ? 17.68138  -19.99156 -28.67492 1.000 20.13763  ? 21  ALA   A CB  1 
ATOM   49   N N   . PHE   A 1 15  ? 15.36566  -18.61755 -26.69145 1.000 16.52170  ? 22  PHE   A N   1 
ATOM   50   C CA  . PHE   A 1 15  ? 15.15190  -17.34381 -26.01912 1.000 19.69866  ? 22  PHE   A CA  1 
ATOM   51   C C   . PHE   A 1 15  ? 16.42751  -16.51723 -26.07660 1.000 22.71655  ? 22  PHE   A C   1 
ATOM   52   O O   . PHE   A 1 15  ? 17.53806  -17.05124 -26.01262 1.000 18.45668  ? 22  PHE   A O   1 
ATOM   53   C CB  . PHE   A 1 15  ? 14.76096  -17.54459 -24.54724 1.000 17.47447  ? 22  PHE   A CB  1 
ATOM   54   C CG  . PHE   A 1 15  ? 13.35944  -18.05433 -24.34125 1.000 17.13227  ? 22  PHE   A CG  1 
ATOM   55   C CD1 . PHE   A 1 15  ? 12.26982  -17.26392 -24.66171 1.000 19.50231  ? 22  PHE   A CD1 1 
ATOM   56   C CD2 . PHE   A 1 15  ? 13.13568  -19.31453 -23.80984 1.000 16.39100  ? 22  PHE   A CD2 1 
ATOM   57   C CE1 . PHE   A 1 15  ? 10.97178  -17.71940 -24.46056 1.000 19.00516  ? 22  PHE   A CE1 1 
ATOM   58   C CE2 . PHE   A 1 15  ? 11.84832  -19.78361 -23.61033 1.000 17.36713  ? 22  PHE   A CE2 1 
ATOM   59   C CZ  . PHE   A 1 15  ? 10.76117  -18.98259 -23.93433 1.000 18.54115  ? 22  PHE   A CZ  1 
ATOM   60   N N   . GLN   A 1 16  ? 16.26786  -15.20054 -26.18468 1.000 19.82924  ? 23  GLN   A N   1 
ATOM   61   C CA  . GLN   A 1 16  ? 17.39224  -14.32417 -25.89057 1.000 25.77203  ? 23  GLN   A CA  1 
ATOM   62   C C   . GLN   A 1 16  ? 17.92120  -14.63179 -24.49598 1.000 22.22596  ? 23  GLN   A C   1 
ATOM   63   O O   . GLN   A 1 16  ? 17.16945  -15.02225 -23.59848 1.000 21.85739  ? 23  GLN   A O   1 
ATOM   64   C CB  . GLN   A 1 16  ? 16.98217  -12.85716 -25.97320 1.000 30.79676  ? 23  GLN   A CB  1 
ATOM   65   C CG  . GLN   A 1 16  ? 16.62256  -12.37460 -27.35791 1.000 30.75611  ? 23  GLN   A CG  1 
ATOM   66   C CD  . GLN   A 1 16  ? 16.08907  -10.95780 -27.33327 1.000 44.66244  ? 23  GLN   A CD  1 
ATOM   67   O OE1 . GLN   A 1 16  ? 14.88318  -10.74620 -27.26672 1.000 33.85237  ? 23  GLN   A OE1 1 
ATOM   68   N NE2 . GLN   A 1 16  ? 16.98768  -9.97857  -27.38498 1.000 38.21001  ? 23  GLN   A NE2 1 
ATOM   69   N N   . ALA   A 1 17  ? 19.23525  -14.46658 -24.32599 1.000 23.28600  ? 24  ALA   A N   1 
ATOM   70   C CA  . ALA   A 1 17  ? 19.87116  -14.81098 -23.05848 1.000 24.65913  ? 24  ALA   A CA  1 
ATOM   71   C C   . ALA   A 1 17  ? 19.19376  -14.11567 -21.88431 1.000 23.59351  ? 24  ALA   A C   1 
ATOM   72   O O   . ALA   A 1 17  ? 18.94297  -14.73653 -20.84399 1.000 25.33729  ? 24  ALA   A O   1 
ATOM   73   C CB  . ALA   A 1 17  ? 21.35702  -14.45610 -23.10942 1.000 26.51050  ? 24  ALA   A CB  1 
ATOM   74   N N   . GLU   A 1 18  ? 18.86786  -12.83078 -22.04080 1.000 25.13954  ? 25  GLU   A N   1 
ATOM   75   C CA  . GLU   A 1 18  ? 18.25770  -12.08270 -20.94552 1.000 27.56295  ? 25  GLU   A CA  1 
ATOM   76   C C   . GLU   A 1 18  ? 16.88679  -12.63488 -20.57004 1.000 27.67532  ? 25  GLU   A C   1 
ATOM   77   O O   . GLU   A 1 18  ? 16.51795  -12.62422 -19.38672 1.000 24.23211  ? 25  GLU   A O   1 
ATOM   78   C CB  . GLU   A 1 18  ? 18.15871  -10.60061 -21.31565 1.000 31.55436  ? 25  GLU   A CB  1 
ATOM   79   C CG  . GLU   A 1 18  ? 19.50510  -9.90901  -21.52473 1.000 38.06147  ? 25  GLU   A CG  1 
ATOM   80   C CD  . GLU   A 1 18  ? 20.10417  -10.12772 -22.90379 1.000 48.08288  ? 25  GLU   A CD  1 
ATOM   81   O OE1 . GLU   A 1 18  ? 19.52254  -10.88114 -23.71376 1.000 36.35125  ? 25  GLU   A OE1 1 
ATOM   82   O OE2 . GLU   A 1 18  ? 21.16758  -9.53505  -23.18220 1.000 54.14622  ? 25  GLU   A OE2 1 
ATOM   83   N N   . ILE   A 1 19  ? 16.12554  -13.12895 -21.54760 1.000 23.94213  ? 26  ILE   A N   1 
ATOM   84   C CA  . ILE   A 1 19  ? 14.80342  -13.67618 -21.25054 1.000 21.35293  ? 26  ILE   A CA  1 
ATOM   85   C C   . ILE   A 1 19  ? 14.92982  -15.04354 -20.58893 1.000 19.96353  ? 26  ILE   A C   1 
ATOM   86   O O   . ILE   A 1 19  ? 14.17013  -15.37574 -19.67348 1.000 20.70560  ? 26  ILE   A O   1 
ATOM   87   C CB  . ILE   A 1 19  ? 13.93497  -13.73767 -22.52632 1.000 21.75458  ? 26  ILE   A CB  1 
ATOM   88   C CG1 . ILE   A 1 19  ? 13.36760  -12.35914 -22.90329 1.000 25.30500  ? 26  ILE   A CG1 1 
ATOM   89   C CG2 . ILE   A 1 19  ? 12.77412  -14.71349 -22.34583 1.000 20.55274  ? 26  ILE   A CG2 1 
ATOM   90   C CD1 . ILE   A 1 19  ? 14.38927  -11.26824 -23.20036 1.000 34.31961  ? 26  ILE   A CD1 1 
ATOM   91   N N   . ALA   A 1 20  ? 15.89786  -15.85318 -21.02746 1.000 17.75663  ? 27  ALA   A N   1 
ATOM   92   C CA  . ALA   A 1 20  ? 16.16376  -17.11314 -20.34202 1.000 23.21376  ? 27  ALA   A CA  1 
ATOM   93   C C   . ALA   A 1 20  ? 16.53439  -16.87267 -18.88345 1.000 25.20917  ? 27  ALA   A C   1 
ATOM   94   O O   . ALA   A 1 20  ? 16.09566  -17.61345 -17.99385 1.000 24.61413  ? 27  ALA   A O   1 
ATOM   95   C CB  . ALA   A 1 20  ? 17.27364  -17.88247 -21.06226 1.000 21.59307  ? 27  ALA   A CB  1 
ATOM   96   N N   . GLN   A 1 21  ? 17.32996  -15.83203 -18.61681 1.000 26.65329  ? 28  GLN   A N   1 
ATOM   97   C CA  . GLN   A 1 21  ? 17.68099  -15.51050 -17.23659 1.000 27.84178  ? 28  GLN   A CA  1 
ATOM   98   C C   . GLN   A 1 21  ? 16.45438  -15.09638 -16.44041 1.000 25.82545  ? 28  GLN   A C   1 
ATOM   99   O O   . GLN   A 1 21  ? 16.33098  -15.44475 -15.26134 1.000 27.63006  ? 28  GLN   A O   1 
ATOM   100  C CB  . GLN   A 1 21  ? 18.73511  -14.39919 -17.17854 1.000 32.12894  ? 28  GLN   A CB  1 
ATOM   101  C CG  . GLN   A 1 21  ? 20.05007  -14.71453 -17.86326 1.000 59.69505  ? 28  GLN   A CG  1 
ATOM   102  C CD  . GLN   A 1 21  ? 20.76964  -13.46795 -18.35157 1.000 67.09578  ? 28  GLN   A CD  1 
ATOM   103  O OE1 . GLN   A 1 21  ? 20.63733  -12.38971 -17.76749 1.000 52.91964  ? 28  GLN   A OE1 1 
ATOM   104  N NE2 . GLN   A 1 21  ? 21.54732  -13.61363 -19.42013 1.000 51.71721  ? 28  GLN   A NE2 1 
ATOM   105  N N   . LEU   A 1 22  ? 15.54698  -14.33705 -17.06074 1.000 23.33257  ? 29  LEU   A N   1 
ATOM   106  C CA  . LEU   A 1 22  ? 14.32347  -13.93018 -16.37269 1.000 22.87317  ? 29  LEU   A CA  1 
ATOM   107  C C   . LEU   A 1 22  ? 13.48299  -15.14122 -15.98481 1.000 27.65263  ? 29  LEU   A C   1 
ATOM   108  O O   . LEU   A 1 22  ? 13.00132  -15.23856 -14.85047 1.000 22.71589  ? 29  LEU   A O   1 
ATOM   109  C CB  . LEU   A 1 22  ? 13.51543  -12.97475 -17.25277 1.000 25.27811  ? 29  LEU   A CB  1 
ATOM   110  C CG  . LEU   A 1 22  ? 12.12068  -12.61660 -16.72890 1.000 26.47016  ? 29  LEU   A CG  1 
ATOM   111  C CD1 . LEU   A 1 22  ? 12.22045  -11.72672 -15.49352 1.000 24.92796  ? 29  LEU   A CD1 1 
ATOM   112  C CD2 . LEU   A 1 22  ? 11.29568  -11.94081 -17.81354 1.000 26.77233  ? 29  LEU   A CD2 1 
ATOM   113  N N   . MET   A 1 23  ? 13.29408  -16.08398 -16.91198 1.000 21.93452  ? 30  MET   A N   1 
ATOM   114  C CA  . MET   A 1 23  ? 12.48122  -17.24877 -16.57416 1.000 23.29065  ? 30  MET   A CA  1 
ATOM   115  C C   . MET   A 1 23  ? 13.17875  -18.15227 -15.56477 1.000 21.87697  ? 30  MET   A C   1 
ATOM   116  O O   . MET   A 1 23  ? 12.51257  -18.75745 -14.71669 1.000 23.38925  ? 30  MET   A O   1 
ATOM   117  C CB  . MET   A 1 23  ? 12.05981  -18.02506 -17.82913 1.000 23.06560  ? 30  MET   A CB  1 
ATOM   118  C CG  . MET   A 1 23  ? 11.65679  -17.14751 -19.01457 1.000 26.41120  ? 30  MET   A CG  1 
ATOM   119  S SD  . MET   A 1 23  ? 11.37396  -18.03055 -20.58042 1.000 22.85989  ? 30  MET   A SD  1 
ATOM   120  C CE  . MET   A 1 23  ? 10.24773  -19.32489 -20.05477 1.000 21.12730  ? 30  MET   A CE  1 
ATOM   121  N N   . SER   A 1 24  ? 14.51239  -18.24246 -15.61602 1.000 21.69115  ? 31  SER   A N   1 
ATOM   122  C CA  . SER   A 1 24  ? 15.22483  -18.98428 -14.57721 1.000 19.51139  ? 31  SER   A CA  1 
ATOM   123  C C   . SER   A 1 24  ? 15.01811  -18.35345 -13.20412 1.000 26.39859  ? 31  SER   A C   1 
ATOM   124  O O   . SER   A 1 24  ? 14.82312  -19.06307 -12.20840 1.000 29.01591  ? 31  SER   A O   1 
ATOM   125  C CB  . SER   A 1 24  ? 16.71657  -19.06259 -14.90283 1.000 28.56857  ? 31  SER   A CB  1 
ATOM   126  O OG  . SER   A 1 24  ? 16.94133  -19.89767 -16.02059 1.000 44.38216  ? 31  SER   A OG  1 
ATOM   127  N N   . LEU   A 1 25  ? 15.07291  -17.02167 -13.12555 1.000 24.99157  ? 32  LEU   A N   1 
ATOM   128  C CA  . LEU   A 1 25  ? 14.87799  -16.35166 -11.84091 1.000 23.64064  ? 32  LEU   A CA  1 
ATOM   129  C C   . LEU   A 1 25  ? 13.46365  -16.57461 -11.31547 1.000 27.98181  ? 32  LEU   A C   1 
ATOM   130  O O   . LEU   A 1 25  ? 13.26439  -16.80496 -10.11606 1.000 25.61936  ? 32  LEU   A O   1 
ATOM   131  C CB  . LEU   A 1 25  ? 15.17977  -14.85685 -11.98522 1.000 31.72678  ? 32  LEU   A CB  1 
ATOM   132  C CG  . LEU   A 1 25  ? 15.03899  -13.91852 -10.77750 1.000 44.01712  ? 32  LEU   A CG  1 
ATOM   133  C CD1 . LEU   A 1 25  ? 15.98500  -12.73688 -10.93762 1.000 42.95483  ? 32  LEU   A CD1 1 
ATOM   134  C CD2 . LEU   A 1 25  ? 13.60551  -13.41415 -10.59608 1.000 36.23524  ? 32  LEU   A CD2 1 
ATOM   135  N N   . ILE   A 1 26  ? 12.46885  -16.50517 -12.19951 1.000 22.50296  ? 33  ILE   A N   1 
ATOM   136  C CA  . ILE   A 1 26  ? 11.08503  -16.72198 -11.78484 1.000 26.10976  ? 33  ILE   A CA  1 
ATOM   137  C C   . ILE   A 1 26  ? 10.89456  -18.14837 -11.28179 1.000 26.21855  ? 33  ILE   A C   1 
ATOM   138  O O   . ILE   A 1 26  ? 10.19777  -18.38808 -10.28596 1.000 26.81241  ? 33  ILE   A O   1 
ATOM   139  C CB  . ILE   A 1 26  ? 10.13065  -16.39893 -12.94880 1.000 21.42969  ? 33  ILE   A CB  1 
ATOM   140  C CG1 . ILE   A 1 26  ? 10.06417  -14.88736 -13.18190 1.000 24.42521  ? 33  ILE   A CG1 1 
ATOM   141  C CG2 . ILE   A 1 26  ? 8.73665   -16.97608 -12.68042 1.000 22.87347  ? 33  ILE   A CG2 1 
ATOM   142  C CD1 . ILE   A 1 26  ? 9.55084   -14.49675 -14.55929 1.000 26.59939  ? 33  ILE   A CD1 1 
ATOM   143  N N   . ILE   A 1 27  ? 11.52937  -19.11391 -11.94738 1.000 22.14648  ? 34  ILE   A N   1 
ATOM   144  C CA  . ILE   A 1 27  ? 11.30461  -20.51882 -11.62274 1.000 25.94124  ? 34  ILE   A CA  1 
ATOM   145  C C   . ILE   A 1 27  ? 12.04438  -20.90804 -10.34950 1.000 31.21571  ? 34  ILE   A C   1 
ATOM   146  O O   . ILE   A 1 27  ? 11.54540  -21.70602 -9.54609  1.000 31.80534  ? 34  ILE   A O   1 
ATOM   147  C CB  . ILE   A 1 27  ? 11.71606  -21.39714 -12.81950 1.000 29.55099  ? 34  ILE   A CB  1 
ATOM   148  C CG1 . ILE   A 1 27  ? 10.68211  -21.26953 -13.94195 1.000 23.85425  ? 34  ILE   A CG1 1 
ATOM   149  C CG2 . ILE   A 1 27  ? 11.90217  -22.85407 -12.40407 1.000 28.15005  ? 34  ILE   A CG2 1 
ATOM   150  C CD1 . ILE   A 1 27  ? 11.19368  -21.72602 -15.29573 1.000 26.24810  ? 34  ILE   A CD1 1 
ATOM   151  N N   . ASN   A 1 28  ? 13.23096  -20.34094 -10.12878 1.000 25.92185  ? 35  ASN   A N   1 
ATOM   152  C CA  . ASN   A 1 28  ? 14.11621  -20.83873 -9.08077  1.000 26.99423  ? 35  ASN   A CA  1 
ATOM   153  C C   . ASN   A 1 28  ? 14.10692  -20.01210 -7.80038  1.000 37.66551  ? 35  ASN   A C   1 
ATOM   154  O O   . ASN   A 1 28  ? 14.51921  -20.52715 -6.75393  1.000 38.88218  ? 35  ASN   A O   1 
ATOM   155  C CB  . ASN   A 1 28  ? 15.55100  -20.92489 -9.60887  1.000 34.38364  ? 35  ASN   A CB  1 
ATOM   156  C CG  . ASN   A 1 28  ? 15.69173  -21.94006 -10.71864 1.000 43.20355  ? 35  ASN   A CG  1 
ATOM   157  O OD1 . ASN   A 1 28  ? 15.04061  -22.98521 -10.70063 1.000 41.77677  ? 35  ASN   A OD1 1 
ATOM   158  N ND2 . ASN   A 1 28  ? 16.52959  -21.63340 -11.70118 1.000 46.64708  ? 35  ASN   A ND2 1 
ATOM   159  N N   . THR   A 1 29  ? 13.66376  -18.75808 -7.84469  1.000 28.73502  ? 36  THR   A N   1 
ATOM   160  C CA  . THR   A 1 29  ? 13.66683  -17.93238 -6.64111  1.000 28.18080  ? 36  THR   A CA  1 
ATOM   161  C C   . THR   A 1 29  ? 12.58749  -18.41011 -5.67804  1.000 30.69908  ? 36  THR   A C   1 
ATOM   162  O O   . THR   A 1 29  ? 11.44158  -18.63512 -6.07916  1.000 31.04949  ? 36  THR   A O   1 
ATOM   163  C CB  . THR   A 1 29  ? 13.43422  -16.45933 -6.99209  1.000 33.02035  ? 36  THR   A CB  1 
ATOM   164  O OG1 . THR   A 1 29  ? 14.47169  -15.99625 -7.86679  1.000 31.18089  ? 36  THR   A OG1 1 
ATOM   165  C CG2 . THR   A 1 29  ? 13.41976  -15.59505 -5.73052  1.000 33.53898  ? 36  THR   A CG2 1 
ATOM   166  N N   . PHE   A 1 30  ? 12.94684  -18.57398 -4.40756  1.000 27.87879  ? 37  PHE   A N   1 
ATOM   167  C CA  . PHE   A 1 30  ? 11.92908  -18.86052 -3.40664  1.000 29.22487  ? 37  PHE   A CA  1 
ATOM   168  C C   . PHE   A 1 30  ? 11.06427  -17.62436 -3.19839  1.000 29.22041  ? 37  PHE   A C   1 
ATOM   169  O O   . PHE   A 1 30  ? 11.56340  -16.56869 -2.78817  1.000 30.04770  ? 37  PHE   A O   1 
ATOM   170  C CB  . PHE   A 1 30  ? 12.54908  -19.29875 -2.08479  1.000 31.45333  ? 37  PHE   A CB  1 
ATOM   171  C CG  . PHE   A 1 30  ? 11.52364  -19.62223 -1.03554  1.000 34.47824  ? 37  PHE   A CG  1 
ATOM   172  C CD1 . PHE   A 1 30  ? 10.75525  -20.77195 -1.13192  1.000 37.12416  ? 37  PHE   A CD1 1 
ATOM   173  C CD2 . PHE   A 1 30  ? 11.30072  -18.75948 0.03009   1.000 33.27620  ? 37  PHE   A CD2 1 
ATOM   174  C CE1 . PHE   A 1 30  ? 9.79407   -21.06907 -0.17663  1.000 32.73648  ? 37  PHE   A CE1 1 
ATOM   175  C CE2 . PHE   A 1 30  ? 10.33922  -19.05132 0.99036   1.000 39.17843  ? 37  PHE   A CE2 1 
ATOM   176  C CZ  . PHE   A 1 30  ? 9.58706   -20.20733 0.88780   1.000 34.27074  ? 37  PHE   A CZ  1 
ATOM   177  N N   . TYR   A 1 31  ? 9.76511   -17.76080 -3.46130  1.000 25.51282  ? 38  TYR   A N   1 
ATOM   178  C CA  . TYR   A 1 31  ? 8.86541   -16.61254 -3.42563  1.000 24.43254  ? 38  TYR   A CA  1 
ATOM   179  C C   . TYR   A 1 31  ? 7.44253   -17.14634 -3.29406  1.000 23.57781  ? 38  TYR   A C   1 
ATOM   180  O O   . TYR   A 1 31  ? 6.91426   -17.73094 -4.24294  1.000 24.51625  ? 38  TYR   A O   1 
ATOM   181  C CB  . TYR   A 1 31  ? 9.03842   -15.76798 -4.68256  1.000 24.64954  ? 38  TYR   A CB  1 
ATOM   182  C CG  . TYR   A 1 31  ? 8.04533   -14.64582 -4.78508  1.000 28.41988  ? 38  TYR   A CG  1 
ATOM   183  C CD1 . TYR   A 1 31  ? 8.15763   -13.52759 -3.97224  1.000 32.14342  ? 38  TYR   A CD1 1 
ATOM   184  C CD2 . TYR   A 1 31  ? 6.99273   -14.70371 -5.68506  1.000 32.12187  ? 38  TYR   A CD2 1 
ATOM   185  C CE1 . TYR   A 1 31  ? 7.25015   -12.49849 -4.04796  1.000 37.56583  ? 38  TYR   A CE1 1 
ATOM   186  C CE2 . TYR   A 1 31  ? 6.07747   -13.67560 -5.77019  1.000 28.21628  ? 38  TYR   A CE2 1 
ATOM   187  C CZ  . TYR   A 1 31  ? 6.21374   -12.57969 -4.95001  1.000 39.48846  ? 38  TYR   A CZ  1 
ATOM   188  O OH  . TYR   A 1 31  ? 5.30545   -11.55535 -5.02818  1.000 49.14079  ? 38  TYR   A OH  1 
ATOM   189  N N   . SER   A 1 32  ? 6.83201   -16.95648 -2.12253  1.000 25.15109  ? 39  SER   A N   1 
ATOM   190  C CA  . SER   A 1 32  ? 5.58043   -17.64189 -1.81041  1.000 24.74095  ? 39  SER   A CA  1 
ATOM   191  C C   . SER   A 1 32  ? 4.34952   -17.00647 -2.45369  1.000 29.53964  ? 39  SER   A C   1 
ATOM   192  O O   . SER   A 1 32  ? 3.33364   -17.68999 -2.61096  1.000 30.53555  ? 39  SER   A O   1 
ATOM   193  C CB  . SER   A 1 32  ? 5.38415   -17.70407 -0.29370  1.000 26.85726  ? 39  SER   A CB  1 
ATOM   194  O OG  . SER   A 1 32  ? 6.42433   -18.45302 0.31641   1.000 28.62558  ? 39  SER   A OG  1 
ATOM   195  N N   . ASN   A 1 33  ? 4.40810   -15.73123 -2.83266  1.000 25.83943  ? 40  ASN   A N   1 
ATOM   196  C CA  . ASN   A 1 33  ? 3.21935   -14.99434 -3.27013  1.000 25.42059  ? 40  ASN   A CA  1 
ATOM   197  C C   . ASN   A 1 33  ? 2.95723   -15.22309 -4.76783  1.000 21.01583  ? 40  ASN   A C   1 
ATOM   198  O O   . ASN   A 1 33  ? 2.91271   -14.30168 -5.58810  1.000 21.38846  ? 40  ASN   A O   1 
ATOM   199  C CB  . ASN   A 1 33  ? 3.39204   -13.51832 -2.92826  1.000 29.60570  ? 40  ASN   A CB  1 
ATOM   200  C CG  . ASN   A 1 33  ? 2.17148   -12.67677 -3.27169  1.000 35.40559  ? 40  ASN   A CG  1 
ATOM   201  O OD1 . ASN   A 1 33  ? 1.02967   -13.10354 -3.08970  1.000 33.42242  ? 40  ASN   A OD1 1 
ATOM   202  N ND2 . ASN   A 1 33  ? 2.41346   -11.45282 -3.72643  1.000 31.72879  ? 40  ASN   A ND2 1 
ATOM   203  N N   . LYS   A 1 34  ? 2.75172   -16.49982 -5.11475  1.000 22.55442  ? 41  LYS   A N   1 
ATOM   204  C CA  . LYS   A 1 34  ? 2.63670   -16.89166 -6.51772  1.000 20.75859  ? 41  LYS   A CA  1 
ATOM   205  C C   . LYS   A 1 34  ? 1.34215   -16.41474 -7.16533  1.000 23.94673  ? 41  LYS   A C   1 
ATOM   206  O O   . LYS   A 1 34  ? 1.26725   -16.35978 -8.40032  1.000 20.17619  ? 41  LYS   A O   1 
ATOM   207  C CB  . LYS   A 1 34  ? 2.73730   -18.41491 -6.64357  1.000 21.91963  ? 41  LYS   A CB  1 
ATOM   208  C CG  . LYS   A 1 34  ? 4.11376   -19.00357 -6.33039  1.000 23.36764  ? 41  LYS   A CG  1 
ATOM   209  C CD  . LYS   A 1 34  ? 4.07689   -20.52907 -6.40608  1.000 26.75727  ? 41  LYS   A CD  1 
ATOM   210  C CE  . LYS   A 1 34  ? 5.46054   -21.15874 -6.22463  1.000 23.62873  ? 41  LYS   A CE  1 
ATOM   211  N NZ  . LYS   A 1 34  ? 6.37389   -20.91181 -7.37936  1.000 23.52921  ? 41  LYS   A NZ  1 
ATOM   212  N N   . GLU   A 1 35  ? 0.32374   -16.06912 -6.37215  1.000 19.40468  ? 42  GLU   A N   1 
ATOM   213  C CA  . GLU   A 1 35  ? -0.99389  -15.78523 -6.93789  1.000 20.11808  ? 42  GLU   A CA  1 
ATOM   214  C C   . GLU   A 1 35  ? -0.99573  -14.58921 -7.88284  1.000 21.83173  ? 42  GLU   A C   1 
ATOM   215  O O   . GLU   A 1 35  ? -1.92628  -14.45610 -8.68744  1.000 22.66037  ? 42  GLU   A O   1 
ATOM   216  C CB  . GLU   A 1 35  ? -2.01552  -15.54419 -5.82339  1.000 20.68025  ? 42  GLU   A CB  1 
ATOM   217  C CG  . GLU   A 1 35  ? -1.81782  -14.25053 -5.06867  1.000 25.37632  ? 42  GLU   A CG  1 
ATOM   218  C CD  . GLU   A 1 35  ? -2.71778  -14.14370 -3.84619  1.000 39.36104  ? 42  GLU   A CD  1 
ATOM   219  O OE1 . GLU   A 1 35  ? -2.88000  -15.15648 -3.13689  1.000 34.21807  ? 42  GLU   A OE1 1 
ATOM   220  O OE2 . GLU   A 1 35  ? -3.25914  -13.04733 -3.59524  1.000 41.87233  ? 42  GLU   A OE2 1 
ATOM   221  N N   . ILE   A 1 36  ? 0.01381   -13.71792 -7.81355  1.000 21.06656  ? 43  ILE   A N   1 
ATOM   222  C CA  . ILE   A 1 36  ? 0.03985   -12.53699 -8.66656  1.000 19.81253  ? 43  ILE   A CA  1 
ATOM   223  C C   . ILE   A 1 36  ? 0.14942   -12.86896 -10.14796 1.000 18.48075  ? 43  ILE   A C   1 
ATOM   224  O O   . ILE   A 1 36  ? -0.05773  -11.97760 -10.97807 1.000 18.87664  ? 43  ILE   A O   1 
ATOM   225  C CB  . ILE   A 1 36  ? 1.18581   -11.57977 -8.25264  1.000 24.84348  ? 43  ILE   A CB  1 
ATOM   226  C CG1 . ILE   A 1 36  ? 2.55676   -12.25493 -8.38281  1.000 24.53106  ? 43  ILE   A CG1 1 
ATOM   227  C CG2 . ILE   A 1 36  ? 0.96188   -11.05631 -6.83469  1.000 30.03335  ? 43  ILE   A CG2 1 
ATOM   228  C CD1 . ILE   A 1 36  ? 3.28209   -11.93720 -9.69698  1.000 30.21027  ? 43  ILE   A CD1 1 
ATOM   229  N N   . PHE   A 1 37  ? 0.46879   -14.11877 -10.50961 1.000 17.34548  ? 44  PHE   A N   1 
ATOM   230  C CA  . PHE   A 1 37  ? 0.48258   -14.47783 -11.92976 1.000 18.74858  ? 44  PHE   A CA  1 
ATOM   231  C C   . PHE   A 1 37  ? -0.85904  -14.15465 -12.58032 1.000 21.53954  ? 44  PHE   A C   1 
ATOM   232  O O   . PHE   A 1 37  ? -0.91317  -13.70408 -13.73087 1.000 18.94357  ? 44  PHE   A O   1 
ATOM   233  C CB  . PHE   A 1 37  ? 0.80410   -15.96914 -12.11604 1.000 16.15825  ? 44  PHE   A CB  1 
ATOM   234  C CG  . PHE   A 1 37  ? -0.39594  -16.86902 -11.93818 1.000 18.56639  ? 44  PHE   A CG  1 
ATOM   235  C CD1 . PHE   A 1 37  ? -0.75955  -17.32262 -10.68098 1.000 18.14375  ? 44  PHE   A CD1 1 
ATOM   236  C CD2 . PHE   A 1 37  ? -1.17695  -17.23830 -13.02792 1.000 22.13731  ? 44  PHE   A CD2 1 
ATOM   237  C CE1 . PHE   A 1 37  ? -1.88229  -18.13432 -10.50923 1.000 22.17801  ? 44  PHE   A CE1 1 
ATOM   238  C CE2 . PHE   A 1 37  ? -2.30137  -18.04041 -12.86065 1.000 17.64180  ? 44  PHE   A CE2 1 
ATOM   239  C CZ  . PHE   A 1 37  ? -2.65047  -18.49026 -11.59958 1.000 19.33182  ? 44  PHE   A CZ  1 
ATOM   240  N N   . LEU   A 1 38  ? -1.95935  -14.37879 -11.85608 1.000 19.28918  ? 45  LEU   A N   1 
ATOM   241  C CA  . LEU   A 1 38  ? -3.27203  -14.20431 -12.46734 1.000 16.04883  ? 45  LEU   A CA  1 
ATOM   242  C C   . LEU   A 1 38  ? -3.57314  -12.72886 -12.68979 1.000 20.51722  ? 45  LEU   A C   1 
ATOM   243  O O   . LEU   A 1 38  ? -4.12749  -12.35122 -13.73109 1.000 18.24911  ? 45  LEU   A O   1 
ATOM   244  C CB  . LEU   A 1 38  ? -4.34695  -14.86294 -11.60298 1.000 16.00346  ? 45  LEU   A CB  1 
ATOM   245  C CG  . LEU   A 1 38  ? -5.75872  -14.80274 -12.19431 1.000 17.76045  ? 45  LEU   A CG  1 
ATOM   246  C CD1 . LEU   A 1 38  ? -5.79247  -15.49204 -13.54768 1.000 17.57965  ? 45  LEU   A CD1 1 
ATOM   247  C CD2 . LEU   A 1 38  ? -6.75360  -15.45051 -11.23917 1.000 22.40872  ? 45  LEU   A CD2 1 
ATOM   248  N N   . ARG   A 1 39  ? -3.20954  -11.88214 -11.72167 1.000 19.62779  ? 46  ARG   A N   1 
ATOM   249  C CA  . ARG   A 1 39  ? -3.32599  -10.43892 -11.90433 1.000 19.15456  ? 46  ARG   A CA  1 
ATOM   250  C C   . ARG   A 1 39  ? -2.55272  -9.97907  -13.13235 1.000 24.80871  ? 46  ARG   A C   1 
ATOM   251  O O   . ARG   A 1 39  ? -3.04907  -9.16865  -13.92611 1.000 19.99276  ? 46  ARG   A O   1 
ATOM   252  C CB  . ARG   A 1 39  ? -2.81415  -9.71434  -10.65995 1.000 18.94980  ? 46  ARG   A CB  1 
ATOM   253  C CG  . ARG   A 1 39  ? -2.73915  -8.20440  -10.80754 1.000 25.43016  ? 46  ARG   A CG  1 
ATOM   254  C CD  . ARG   A 1 39  ? -2.08428  -7.55367  -9.59937  1.000 34.08749  ? 46  ARG   A CD  1 
ATOM   255  N NE  . ARG   A 1 39  ? -0.63669  -7.73602  -9.59921  1.000 34.72128  ? 46  ARG   A NE  1 
ATOM   256  C CZ  . ARG   A 1 39  ? 0.14108   -7.60111  -8.53293  1.000 41.66455  ? 46  ARG   A CZ  1 
ATOM   257  N NH1 . ARG   A 1 39  ? -0.35250  -7.25649  -7.35382  1.000 35.18232  ? 46  ARG   A NH1 1 
ATOM   258  N NH2 . ARG   A 1 39  ? 1.44903   -7.81156  -8.65336  1.000 37.30814  ? 46  ARG   A NH2 1 
ATOM   259  N N   . GLU   A 1 40  ? -1.33352  -10.49144 -13.30759 1.000 17.72668  ? 47  GLU   A N   1 
ATOM   260  C CA  . GLU   A 1 40  ? -0.50318  -10.04209 -14.42029 1.000 20.02556  ? 47  GLU   A CA  1 
ATOM   261  C C   . GLU   A 1 40  ? -1.09371  -10.46718 -15.76100 1.000 17.37337  ? 47  GLU   A C   1 
ATOM   262  O O   . GLU   A 1 40  ? -1.06552  -9.69692  -16.72967 1.000 18.42773  ? 47  GLU   A O   1 
ATOM   263  C CB  . GLU   A 1 40  ? 0.91979   -10.57901 -14.25883 1.000 18.33849  ? 47  GLU   A CB  1 
ATOM   264  C CG  . GLU   A 1 40  ? 1.67884   -10.00919 -13.06426 1.000 24.69656  ? 47  GLU   A CG  1 
ATOM   265  C CD  . GLU   A 1 40  ? 1.55492   -8.49713  -12.92943 1.000 32.88547  ? 47  GLU   A CD  1 
ATOM   266  O OE1 . GLU   A 1 40  ? 1.66564   -7.78601  -13.95168 1.000 26.89882  ? 47  GLU   A OE1 1 
ATOM   267  O OE2 . GLU   A 1 40  ? 1.34938   -8.01661  -11.79170 1.000 36.64548  ? 47  GLU   A OE2 1 
ATOM   268  N N   . LEU   A 1 41  ? -1.63662  -11.68569 -15.84563 1.000 16.13227  ? 48  LEU   A N   1 
ATOM   269  C CA  . LEU   A 1 41  ? -2.19682  -12.13154 -17.12386 1.000 17.15781  ? 48  LEU   A CA  1 
ATOM   270  C C   . LEU   A 1 41  ? -3.51440  -11.43155 -17.43319 1.000 17.06226  ? 48  LEU   A C   1 
ATOM   271  O O   . LEU   A 1 41  ? -3.79747  -11.11920 -18.59610 1.000 19.52469  ? 48  LEU   A O   1 
ATOM   272  C CB  . LEU   A 1 41  ? -2.38392  -13.64980 -17.13534 1.000 14.51488  ? 48  LEU   A CB  1 
ATOM   273  C CG  . LEU   A 1 41  ? -1.08048  -14.45210 -17.07030 1.000 21.35930  ? 48  LEU   A CG  1 
ATOM   274  C CD1 . LEU   A 1 41  ? -1.37812  -15.94379 -16.97155 1.000 17.69741  ? 48  LEU   A CD1 1 
ATOM   275  C CD2 . LEU   A 1 41  ? -0.17290  -14.14954 -18.26337 1.000 17.92741  ? 48  LEU   A CD2 1 
ATOM   276  N N   . ILE   A 1 42  ? -4.33620  -11.17828 -16.41358 1.000 16.25015  ? 49  ILE   A N   1 
ATOM   277  C CA  . ILE   A 1 42  ? -5.57538  -10.44223 -16.64591 1.000 18.92586  ? 49  ILE   A CA  1 
ATOM   278  C C   . ILE   A 1 42  ? -5.26729  -9.00726  -17.05859 1.000 16.73711  ? 49  ILE   A C   1 
ATOM   279  O O   . ILE   A 1 42  ? -5.94065  -8.43245  -17.92528 1.000 19.59873  ? 49  ILE   A O   1 
ATOM   280  C CB  . ILE   A 1 42  ? -6.47183  -10.50465 -15.39555 1.000 20.03026  ? 49  ILE   A CB  1 
ATOM   281  C CG1 . ILE   A 1 42  ? -7.04463  -11.91958 -15.23795 1.000 16.38784  ? 49  ILE   A CG1 1 
ATOM   282  C CG2 . ILE   A 1 42  ? -7.59513  -9.46537  -15.47731 1.000 19.36479  ? 49  ILE   A CG2 1 
ATOM   283  C CD1 . ILE   A 1 42  ? -7.78184  -12.13751 -13.91953 1.000 21.92090  ? 49  ILE   A CD1 1 
ATOM   284  N N   . SER   A 1 43  ? -4.22831  -8.41432  -16.46586 1.000 17.68275  ? 50  SER   A N   1 
ATOM   285  C CA  . SER   A 1 43  ? -3.83997  -7.06444  -16.85116 1.000 17.92967  ? 50  SER   A CA  1 
ATOM   286  C C   . SER   A 1 43  ? -3.33996  -7.03541  -18.29310 1.000 20.81160  ? 50  SER   A C   1 
ATOM   287  O O   . SER   A 1 43  ? -3.62333  -6.08808  -19.03901 1.000 16.84911  ? 50  SER   A O   1 
ATOM   288  C CB  . SER   A 1 43  ? -2.77945  -6.53445  -15.87984 1.000 22.41704  ? 50  SER   A CB  1 
ATOM   289  O OG  . SER   A 1 43  ? -2.12628  -5.39788  -16.40986 1.000 33.27125  ? 50  SER   A OG  1 
ATOM   290  N N   . ASN   A 1 44  ? -2.59754  -8.06952  -18.70180 1.000 19.01071  ? 51  ASN   A N   1 
ATOM   291  C CA  . ASN   A 1 44  ? -2.19458  -8.19577  -20.09895 1.000 22.39095  ? 51  ASN   A CA  1 
ATOM   292  C C   . ASN   A 1 44  ? -3.40688  -8.28133  -21.01477 1.000 18.53000  ? 51  ASN   A C   1 
ATOM   293  O O   . ASN   A 1 44  ? -3.43241  -7.66408  -22.08501 1.000 16.83458  ? 51  ASN   A O   1 
ATOM   294  C CB  . ASN   A 1 44  ? -1.32630  -9.43681  -20.28309 1.000 17.33041  ? 51  ASN   A CB  1 
ATOM   295  C CG  . ASN   A 1 44  ? 0.08742   -9.22700  -19.81410 1.000 30.06381  ? 51  ASN   A CG  1 
ATOM   296  O OD1 . ASN   A 1 44  ? 0.46255   -8.12729  -19.40456 1.000 24.61897  ? 51  ASN   A OD1 1 
ATOM   297  N ND2 . ASN   A 1 44  ? 0.88528   -10.28176 -19.87129 1.000 29.52022  ? 51  ASN   A ND2 1 
ATOM   298  N N   . SER   A 1 45  ? -4.41373  -9.06330  -20.61844 1.000 14.44199  ? 52  SER   A N   1 
ATOM   299  C CA  . SER   A 1 45  ? -5.62490  -9.17924  -21.42590 1.000 17.76725  ? 52  SER   A CA  1 
ATOM   300  C C   . SER   A 1 45  ? -6.34557  -7.83997  -21.53107 1.000 18.33786  ? 52  SER   A C   1 
ATOM   301  O O   . SER   A 1 45  ? -6.81598  -7.46378  -22.61256 1.000 17.46834  ? 52  SER   A O   1 
ATOM   302  C CB  . SER   A 1 45  ? -6.55083  -10.24291 -20.82914 1.000 16.88850  ? 52  SER   A CB  1 
ATOM   303  O OG  . SER   A 1 45  ? -5.99153  -11.53975 -20.94098 1.000 19.36131  ? 52  SER   A OG  1 
ATOM   304  N N   . SER   A 1 46  ? -6.44470  -7.10954  -20.41349 1.000 17.00883  ? 53  SER   A N   1 
ATOM   305  C CA  . SER   A 1 46  ? -7.07076  -5.78914  -20.43397 1.000 18.93369  ? 53  SER   A CA  1 
ATOM   306  C C   . SER   A 1 46  ? -6.33072  -4.84340  -21.37493 1.000 24.58654  ? 53  SER   A C   1 
ATOM   307  O O   . SER   A 1 46  ? -6.95696  -4.08141  -22.12326 1.000 19.33873  ? 53  SER   A O   1 
ATOM   308  C CB  . SER   A 1 46  ? -7.11616  -5.21543  -19.01750 1.000 18.31237  ? 53  SER   A CB  1 
ATOM   309  O OG  . SER   A 1 46  ? -7.70658  -3.92199  -18.99857 1.000 21.48040  ? 53  SER   A OG  1 
ATOM   310  N N   . ASP   A 1 47  ? -4.99422  -4.87852  -21.34601 1.000 18.32043  ? 54  ASP   A N   1 
ATOM   311  C CA  . ASP   A 1 47  ? -4.20002  -4.05264  -22.24943 1.000 17.87655  ? 54  ASP   A CA  1 
ATOM   312  C C   . ASP   A 1 47  ? -4.49779  -4.38982  -23.70828 1.000 18.82810  ? 54  ASP   A C   1 
ATOM   313  O O   . ASP   A 1 47  ? -4.61473  -3.49189  -24.55103 1.000 20.10902  ? 54  ASP   A O   1 
ATOM   314  C CB  . ASP   A 1 47  ? -2.71701  -4.24976  -21.94297 1.000 18.89644  ? 54  ASP   A CB  1 
ATOM   315  C CG  . ASP   A 1 47  ? -2.26202  -3.47821  -20.70595 1.000 35.58930  ? 54  ASP   A CG  1 
ATOM   316  O OD1 . ASP   A 1 47  ? -3.10499  -2.82281  -20.05197 1.000 27.44033  ? 54  ASP   A OD1 1 
ATOM   317  O OD2 . ASP   A 1 47  ? -1.06752  -3.57900  -20.35259 1.000 30.26416  ? 54  ASP   A OD2 1 
ATOM   318  N N   . ALA   A 1 48  ? -4.63241  -5.68282  -24.02305 1.000 18.41523  ? 55  ALA   A N   1 
ATOM   319  C CA  . ALA   A 1 48  ? -4.89483  -6.09538  -25.39961 1.000 19.44345  ? 55  ALA   A CA  1 
ATOM   320  C C   . ALA   A 1 48  ? -6.31228  -5.74597  -25.82707 1.000 16.41514  ? 55  ALA   A C   1 
ATOM   321  O O   . ALA   A 1 48  ? -6.55829  -5.47319  -27.00831 1.000 16.53637  ? 55  ALA   A O   1 
ATOM   322  C CB  . ALA   A 1 48  ? -4.65989  -7.59874  -25.55631 1.000 15.59918  ? 55  ALA   A CB  1 
ATOM   323  N N   . LEU   A 1 49  ? -7.25686  -5.76418  -24.88809 1.000 18.23218  ? 56  LEU   A N   1 
ATOM   324  C CA  . LEU   A 1 49  ? -8.61459  -5.34229  -25.20284 1.000 18.37170  ? 56  LEU   A CA  1 
ATOM   325  C C   . LEU   A 1 49  ? -8.68760  -3.83278  -25.40177 1.000 18.33426  ? 56  LEU   A C   1 
ATOM   326  O O   . LEU   A 1 49  ? -9.41962  -3.35212  -26.27687 1.000 19.37338  ? 56  LEU   A O   1 
ATOM   327  C CB  . LEU   A 1 49  ? -9.56442  -5.80292  -24.09757 1.000 19.70023  ? 56  LEU   A CB  1 
ATOM   328  C CG  . LEU   A 1 49  ? -9.81196  -7.31620  -24.07389 1.000 16.57425  ? 56  LEU   A CG  1 
ATOM   329  C CD1 . LEU   A 1 49  ? -10.21632 -7.76278  -22.67125 1.000 17.50597  ? 56  LEU   A CD1 1 
ATOM   330  C CD2 . LEU   A 1 49  ? -10.87552 -7.72030  -25.08971 1.000 18.68514  ? 56  LEU   A CD2 1 
ATOM   331  N N   . ASP   A 1 50  ? -7.93938  -3.06722  -24.59782 1.000 18.20715  ? 57  ASP   A N   1 
ATOM   332  C CA  . ASP   A 1 50  ? -7.84837  -1.62652  -24.82551 1.000 22.41853  ? 57  ASP   A CA  1 
ATOM   333  C C   . ASP   A 1 50  ? -7.37357  -1.32347  -26.24366 1.000 21.04100  ? 57  ASP   A C   1 
ATOM   334  O O   . ASP   A 1 50  ? -7.87374  -0.39649  -26.89171 1.000 20.29634  ? 57  ASP   A O   1 
ATOM   335  C CB  . ASP   A 1 50  ? -6.89612  -0.98278  -23.81395 1.000 19.92621  ? 57  ASP   A CB  1 
ATOM   336  C CG  . ASP   A 1 50  ? -7.47858  -0.90002  -22.40191 1.000 27.80479  ? 57  ASP   A CG  1 
ATOM   337  O OD1 . ASP   A 1 50  ? -8.65845  -1.25939  -22.18933 1.000 26.74555  ? 57  ASP   A OD1 1 
ATOM   338  O OD2 . ASP   A 1 50  ? -6.73405  -0.47377  -21.49808 1.000 26.96809  ? 57  ASP   A OD2 1 
ATOM   339  N N   . LYS   A 1 51  ? -6.41179  -2.10638  -26.74296 1.000 19.78198  ? 58  LYS   A N   1 
ATOM   340  C CA  . LYS   A 1 51  ? -5.80746  -1.82335  -28.04298 1.000 22.30274  ? 58  LYS   A CA  1 
ATOM   341  C C   . LYS   A 1 51  ? -6.79970  -2.03100  -29.17770 1.000 22.77790  ? 58  LYS   A C   1 
ATOM   342  O O   . LYS   A 1 51  ? -6.88399  -1.20949  -30.09927 1.000 21.28173  ? 58  LYS   A O   1 
ATOM   343  C CB  . LYS   A 1 51  ? -4.57358  -2.70196  -28.25232 1.000 22.22790  ? 58  LYS   A CB  1 
ATOM   344  C CG  . LYS   A 1 51  ? -3.34325  -2.25385  -27.48024 1.000 25.87195  ? 58  LYS   A CG  1 
ATOM   345  C CD  . LYS   A 1 51  ? -2.22867  -3.28398  -27.62499 1.000 27.41247  ? 58  LYS   A CD  1 
ATOM   346  C CE  . LYS   A 1 51  ? -1.19031  -3.14918  -26.51490 1.000 38.06907  ? 58  LYS   A CE  1 
ATOM   347  N NZ  . LYS   A 1 51  ? -0.01114  -4.03360  -26.75112 1.000 36.04416  ? 58  LYS   A NZ  1 
ATOM   348  N N   . ILE   A 1 52  ? -7.54536  -3.13725  -29.14832 1.000 19.01408  ? 59  ILE   A N   1 
ATOM   349  C CA  . ILE   A 1 52  ? -8.50968  -3.35295  -30.22345 1.000 20.19570  ? 59  ILE   A CA  1 
ATOM   350  C C   . ILE   A 1 52  ? -9.67612  -2.37976  -30.10059 1.000 21.03468  ? 59  ILE   A C   1 
ATOM   351  O O   . ILE   A 1 52  ? -10.21612 -1.92363  -31.11545 1.000 20.96904  ? 59  ILE   A O   1 
ATOM   352  C CB  . ILE   A 1 52  ? -8.97822  -4.82394  -30.27051 1.000 18.91280  ? 59  ILE   A CB  1 
ATOM   353  C CG1 . ILE   A 1 52  ? -9.75767  -5.09893  -31.56588 1.000 20.27757  ? 59  ILE   A CG1 1 
ATOM   354  C CG2 . ILE   A 1 52  ? -9.82157  -5.19323  -29.05236 1.000 17.54489  ? 59  ILE   A CG2 1 
ATOM   355  C CD1 . ILE   A 1 52  ? -8.94640  -4.88207  -32.83533 1.000 22.37392  ? 59  ILE   A CD1 1 
ATOM   356  N N   . ARG   A 1 53  ? -10.07057 -2.01509  -28.87801 1.000 20.54472  ? 60  ARG   A N   1 
ATOM   357  C CA  . ARG   A 1 53  ? -11.13528 -1.02504  -28.73565 1.000 20.27146  ? 60  ARG   A CA  1 
ATOM   358  C C   . ARG   A 1 53  ? -10.71606 0.31925   -29.32021 1.000 24.55159  ? 60  ARG   A C   1 
ATOM   359  O O   . ARG   A 1 53  ? -11.48395 0.95777   -30.05200 1.000 22.69164  ? 60  ARG   A O   1 
ATOM   360  C CB  . ARG   A 1 53  ? -11.54577 -0.86872  -27.27147 1.000 24.04790  ? 60  ARG   A CB  1 
ATOM   361  C CG  . ARG   A 1 53  ? -12.69704 0.12752   -27.13827 1.000 35.39576  ? 60  ARG   A CG  1 
ATOM   362  C CD  . ARG   A 1 53  ? -13.08909 0.41822   -25.70900 1.000 48.93942  ? 60  ARG   A CD  1 
ATOM   363  N NE  . ARG   A 1 53  ? -14.15051 -0.46414  -25.24129 1.000 54.39404  ? 60  ARG   A NE  1 
ATOM   364  C CZ  . ARG   A 1 53  ? -14.23155 -0.95031  -24.01097 1.000 50.73834  ? 60  ARG   A CZ  1 
ATOM   365  N NH1 . ARG   A 1 53  ? -13.32068 -0.66611  -23.09466 1.000 44.50007  ? 60  ARG   A NH1 1 
ATOM   366  N NH2 . ARG   A 1 53  ? -15.26075 -1.72831  -23.68730 1.000 44.53890  ? 60  ARG   A NH2 1 
ATOM   367  N N   . TYR   A 1 54  ? -9.48826  0.75935   -29.02369 1.000 21.74495  ? 61  TYR   A N   1 
ATOM   368  C CA  . TYR   A 1 54  ? -9.01851  2.02530   -29.57458 1.000 23.28427  ? 61  TYR   A CA  1 
ATOM   369  C C   . TYR   A 1 54  ? -9.00851  1.99879   -31.09916 1.000 24.29363  ? 61  TYR   A C   1 
ATOM   370  O O   . TYR   A 1 54  ? -9.43567  2.96360   -31.74609 1.000 25.66113  ? 61  TYR   A O   1 
ATOM   371  C CB  . TYR   A 1 54  ? -7.62508  2.36779   -29.04709 1.000 23.88031  ? 61  TYR   A CB  1 
ATOM   372  C CG  . TYR   A 1 54  ? -7.18147  3.72534   -29.54259 1.000 30.60575  ? 61  TYR   A CG  1 
ATOM   373  C CD1 . TYR   A 1 54  ? -7.77081  4.88468   -29.06089 1.000 27.31326  ? 61  TYR   A CD1 1 
ATOM   374  C CD2 . TYR   A 1 54  ? -6.21921  3.84319   -30.53728 1.000 26.80724  ? 61  TYR   A CD2 1 
ATOM   375  C CE1 . TYR   A 1 54  ? -7.39431  6.12649   -29.53252 1.000 29.43798  ? 61  TYR   A CE1 1 
ATOM   376  C CE2 . TYR   A 1 54  ? -5.83372  5.07966   -31.01483 1.000 28.94247  ? 61  TYR   A CE2 1 
ATOM   377  C CZ  . TYR   A 1 54  ? -6.42301  6.21570   -30.51140 1.000 31.31445  ? 61  TYR   A CZ  1 
ATOM   378  O OH  . TYR   A 1 54  ? -6.03799  7.44917   -30.98494 1.000 33.81684  ? 61  TYR   A OH  1 
ATOM   379  N N   . GLU   A 1 55  ? -8.52529  0.90361   -31.69461 1.000 23.27390  ? 62  GLU   A N   1 
ATOM   380  C CA  . GLU   A 1 55  ? -8.48978  0.82212   -33.15379 1.000 27.85953  ? 62  GLU   A CA  1 
ATOM   381  C C   . GLU   A 1 55  ? -9.89376  0.84973   -33.74137 1.000 25.71742  ? 62  GLU   A C   1 
ATOM   382  O O   . GLU   A 1 55  ? -10.12336 1.45090   -34.79901 1.000 30.86239  ? 62  GLU   A O   1 
ATOM   383  C CB  . GLU   A 1 55  ? -7.74591  -0.43863  -33.59349 1.000 29.91674  ? 62  GLU   A CB  1 
ATOM   384  C CG  . GLU   A 1 55  ? -6.23731  -0.35837  -33.40803 1.000 34.49736  ? 62  GLU   A CG  1 
ATOM   385  C CD  . GLU   A 1 55  ? -5.49348  -1.42236  -34.20062 1.000 46.36884  ? 62  GLU   A CD  1 
ATOM   386  O OE1 . GLU   A 1 55  ? -6.15418  -2.33865  -34.73318 1.000 38.22855  ? 62  GLU   A OE1 1 
ATOM   387  O OE2 . GLU   A 1 55  ? -4.25063  -1.33991  -34.29791 1.000 46.12197  ? 62  GLU   A OE2 1 
ATOM   388  N N   . SER   A 1 56  ? -10.85253 0.22282   -33.05976 1.000 26.62762  ? 63  SER   A N   1 
ATOM   389  C CA  . SER   A 1 56  ? -12.22908 0.20850   -33.53806 1.000 26.07723  ? 63  SER   A CA  1 
ATOM   390  C C   . SER   A 1 56  ? -12.89600 1.57615   -33.47025 1.000 30.69908  ? 63  SER   A C   1 
ATOM   391  O O   . SER   A 1 56  ? -13.94692 1.76099   -34.09129 1.000 26.89224  ? 63  SER   A O   1 
ATOM   392  C CB  . SER   A 1 56  ? -13.05185 -0.80049  -32.73508 1.000 24.08950  ? 63  SER   A CB  1 
ATOM   393  O OG  . SER   A 1 56  ? -13.36112 -0.29833  -31.44205 1.000 27.92121  ? 63  SER   A OG  1 
ATOM   394  N N   . LEU   A 1 57  ? -12.32211 2.53165   -32.73416 1.000 28.25963  ? 64  LEU   A N   1 
ATOM   395  C CA  . LEU   A 1 57  ? -12.94734 3.84566   -32.61229 1.000 34.37385  ? 64  LEU   A CA  1 
ATOM   396  C C   . LEU   A 1 57  ? -12.98388 4.57601   -33.94679 1.000 34.57370  ? 64  LEU   A C   1 
ATOM   397  O O   . LEU   A 1 57  ? -13.92170 5.33517   -34.21392 1.000 35.39653  ? 64  LEU   A O   1 
ATOM   398  C CB  . LEU   A 1 57  ? -12.20299 4.68564   -31.57401 1.000 32.05843  ? 64  LEU   A CB  1 
ATOM   399  C CG  . LEU   A 1 57  ? -12.36225 4.23768   -30.12129 1.000 34.11962  ? 64  LEU   A CG  1 
ATOM   400  C CD1 . LEU   A 1 57  ? -11.66995 5.21413   -29.18067 1.000 35.80495  ? 64  LEU   A CD1 1 
ATOM   401  C CD2 . LEU   A 1 57  ? -13.83239 4.09391   -29.76529 1.000 33.61223  ? 64  LEU   A CD2 1 
ATOM   402  N N   . THR   A 1 58  ? -11.97396 4.37131   -34.78721 1.000 32.85494  ? 65  THR   A N   1 
ATOM   403  C CA  . THR   A 1 58  ? -11.91614 4.99728   -36.09858 1.000 41.02586  ? 65  THR   A CA  1 
ATOM   404  C C   . THR   A 1 58  ? -12.17515 4.02643   -37.24054 1.000 42.71464  ? 65  THR   A C   1 
ATOM   405  O O   . THR   A 1 58  ? -12.39215 4.47317   -38.37193 1.000 40.50991  ? 65  THR   A O   1 
ATOM   406  C CB  . THR   A 1 58  ? -10.54952 5.66782   -36.30636 1.000 50.62439  ? 65  THR   A CB  1 
ATOM   407  O OG1 . THR   A 1 58  ? -9.51515  4.67936   -36.22178 1.000 44.51504  ? 65  THR   A OG1 1 
ATOM   408  C CG2 . THR   A 1 58  ? -10.31230 6.73824   -35.24787 1.000 38.75170  ? 65  THR   A CG2 1 
ATOM   409  N N   . ASP   A 1 59  ? -12.16591 2.72040   -36.97801 1.000 38.98113  ? 66  ASP   A N   1 
ATOM   410  C CA  . ASP   A 1 59  ? -12.38092 1.71046   -38.01244 1.000 38.93587  ? 66  ASP   A CA  1 
ATOM   411  C C   . ASP   A 1 59  ? -13.21885 0.58994   -37.41007 1.000 35.23933  ? 66  ASP   A C   1 
ATOM   412  O O   . ASP   A 1 59  ? -12.68523 -0.36396  -36.82917 1.000 29.52708  ? 66  ASP   A O   1 
ATOM   413  C CB  . ASP   A 1 59  ? -11.05056 1.18697   -38.55676 1.000 34.73703  ? 66  ASP   A CB  1 
ATOM   414  C CG  . ASP   A 1 59  ? -11.22788 0.18939   -39.68645 1.000 48.36062  ? 66  ASP   A CG  1 
ATOM   415  O OD1 . ASP   A 1 59  ? -12.38126 -0.06735  -40.08882 1.000 38.94247  ? 66  ASP   A OD1 1 
ATOM   416  O OD2 . ASP   A 1 59  ? -10.20635 -0.33631  -40.17690 1.000 45.75575  ? 66  ASP   A OD2 1 
ATOM   417  N N   . PRO   A 1 60  ? -14.54681 0.67321   -37.53206 1.000 40.09116  ? 67  PRO   A N   1 
ATOM   418  C CA  . PRO   A 1 60  ? -15.40235 -0.35210  -36.90611 1.000 39.12169  ? 67  PRO   A CA  1 
ATOM   419  C C   . PRO   A 1 60  ? -15.19954 -1.74517  -37.47789 1.000 39.74538  ? 67  PRO   A C   1 
ATOM   420  O O   . PRO   A 1 60  ? -15.48294 -2.73161  -36.78596 1.000 34.18846  ? 67  PRO   A O   1 
ATOM   421  C CB  . PRO   A 1 60  ? -16.83086 0.14922   -37.16553 1.000 42.85607  ? 67  PRO   A CB  1 
ATOM   422  C CG  . PRO   A 1 60  ? -16.72258 1.45501   -37.84833 1.000 50.50297  ? 67  PRO   A CG  1 
ATOM   423  C CD  . PRO   A 1 60  ? -15.30122 1.79845   -38.10920 1.000 43.06002  ? 67  PRO   A CD  1 
ATOM   424  N N   . SER   A 1 61  ? -14.71881 -1.86035  -38.72139 1.000 33.93303  ? 68  SER   A N   1 
ATOM   425  C CA  . SER   A 1 61  ? -14.50031 -3.17582  -39.31164 1.000 34.87651  ? 68  SER   A CA  1 
ATOM   426  C C   . SER   A 1 61  ? -13.44566 -3.97672  -38.55905 1.000 36.74331  ? 68  SER   A C   1 
ATOM   427  O O   . SER   A 1 61  ? -13.37672 -5.19897  -38.72382 1.000 29.95743  ? 68  SER   A O   1 
ATOM   428  C CB  . SER   A 1 61  ? -14.10112 -3.03901  -40.78371 1.000 34.86468  ? 68  SER   A CB  1 
ATOM   429  O OG  . SER   A 1 61  ? -12.78673 -2.52641  -40.91144 1.000 35.51411  ? 68  SER   A OG  1 
ATOM   430  N N   . LYS   A 1 62  ? -12.63037 -3.32241  -37.72747 1.000 27.53404  ? 69  LYS   A N   1 
ATOM   431  C CA  . LYS   A 1 62  ? -11.66289 -4.05132  -36.91828 1.000 31.40209  ? 69  LYS   A CA  1 
ATOM   432  C C   . LYS   A 1 62  ? -12.33036 -5.02523  -35.95565 1.000 30.57061  ? 69  LYS   A C   1 
ATOM   433  O O   . LYS   A 1 62  ? -11.65838 -5.92346  -35.43550 1.000 26.50466  ? 69  LYS   A O   1 
ATOM   434  C CB  . LYS   A 1 62  ? -10.78853 -3.06730  -36.14738 1.000 34.44975  ? 69  LYS   A CB  1 
ATOM   435  C CG  . LYS   A 1 62  ? -9.98358  -2.15358  -37.05237 1.000 41.56775  ? 69  LYS   A CG  1 
ATOM   436  C CD  . LYS   A 1 62  ? -8.49949  -2.36477  -36.84923 1.000 36.91252  ? 69  LYS   A CD  1 
ATOM   437  C CE  . LYS   A 1 62  ? -7.67965  -1.69754  -37.93909 1.000 38.69150  ? 69  LYS   A CE  1 
ATOM   438  N NZ  . LYS   A 1 62  ? -6.25196  -2.12365  -37.86534 1.000 47.72933  ? 69  LYS   A NZ  1 
ATOM   439  N N   . LEU   A 1 63  ? -13.62997 -4.87057  -35.70335 1.000 28.71456  ? 70  LEU   A N   1 
ATOM   440  C CA  . LEU   A 1 63  ? -14.37446 -5.79154  -34.85462 1.000 26.25006  ? 70  LEU   A CA  1 
ATOM   441  C C   . LEU   A 1 63  ? -15.18280 -6.80243  -35.65493 1.000 27.72501  ? 70  LEU   A C   1 
ATOM   442  O O   . LEU   A 1 63  ? -16.01645 -7.50905  -35.07719 1.000 29.78789  ? 70  LEU   A O   1 
ATOM   443  C CB  . LEU   A 1 63  ? -15.29417 -5.01852  -33.90681 1.000 30.78747  ? 70  LEU   A CB  1 
ATOM   444  C CG  . LEU   A 1 63  ? -14.60570 -4.09053  -32.90756 1.000 31.46764  ? 70  LEU   A CG  1 
ATOM   445  C CD1 . LEU   A 1 63  ? -15.63914 -3.39879  -32.03099 1.000 31.11016  ? 70  LEU   A CD1 1 
ATOM   446  C CD2 . LEU   A 1 63  ? -13.61642 -4.86745  -32.05080 1.000 27.14217  ? 70  LEU   A CD2 1 
ATOM   447  N N   . ASP   A 1 64  ? -14.95252 -6.89227  -36.96857 1.000 27.96848  ? 71  ASP   A N   1 
ATOM   448  C CA  . ASP   A 1 64  ? -15.62783 -7.90998  -37.76784 1.000 30.19473  ? 71  ASP   A CA  1 
ATOM   449  C C   . ASP   A 1 64  ? -15.29433 -9.31124  -37.27575 1.000 33.38181  ? 71  ASP   A C   1 
ATOM   450  O O   . ASP   A 1 64  ? -16.09479 -10.23848 -37.44290 1.000 35.06285  ? 71  ASP   A O   1 
ATOM   451  C CB  . ASP   A 1 64  ? -15.23976 -7.77025  -39.23982 1.000 40.15386  ? 71  ASP   A CB  1 
ATOM   452  C CG  . ASP   A 1 64  ? -15.95763 -6.62603  -39.92827 1.000 54.21591  ? 71  ASP   A CG  1 
ATOM   453  O OD1 . ASP   A 1 64  ? -16.87504 -6.03857  -39.31486 1.000 44.96891  ? 71  ASP   A OD1 1 
ATOM   454  O OD2 . ASP   A 1 64  ? -15.60877 -6.31991  -41.08778 1.000 46.12868  ? 71  ASP   A OD2 1 
ATOM   455  N N   . SER   A 1 65  ? -14.12026 -9.48147  -36.67361 1.000 28.04610  ? 72  SER   A N   1 
ATOM   456  C CA  . SER   A 1 65  ? -13.67044 -10.74398 -36.10493 1.000 29.86140  ? 72  SER   A CA  1 
ATOM   457  C C   . SER   A 1 65  ? -14.26559 -11.02153 -34.72830 1.000 41.84981  ? 72  SER   A C   1 
ATOM   458  O O   . SER   A 1 65  ? -13.86652 -11.99763 -34.08600 1.000 37.27168  ? 72  SER   A O   1 
ATOM   459  C CB  . SER   A 1 65  ? -12.14221 -10.74562 -36.00760 1.000 30.94294  ? 72  SER   A CB  1 
ATOM   460  O OG  . SER   A 1 65  ? -11.67819 -9.47443  -35.56938 1.000 26.12277  ? 72  SER   A OG  1 
ATOM   461  N N   . GLY   A 1 66  ? -15.19025 -10.18609 -34.25744 1.000 31.41980  ? 73  GLY   A N   1 
ATOM   462  C CA  . GLY   A 1 66  ? -15.80655 -10.38373 -32.95898 1.000 34.33091  ? 73  GLY   A CA  1 
ATOM   463  C C   . GLY   A 1 66  ? -16.03928 -9.08013  -32.22240 1.000 27.93685  ? 73  GLY   A C   1 
ATOM   464  O O   . GLY   A 1 66  ? -15.09107 -8.34428  -31.94433 1.000 26.42402  ? 73  GLY   A O   1 
ATOM   465  N N   . LYS   A 1 67  ? -17.29902 -8.77460  -31.90721 1.000 27.39620  ? 74  LYS   A N   1 
ATOM   466  C CA  . LYS   A 1 67  ? -17.61646 -7.51174  -31.25160 1.000 30.93366  ? 74  LYS   A CA  1 
ATOM   467  C C   . LYS   A 1 67  ? -17.45606 -7.56560  -29.73504 1.000 29.26597  ? 74  LYS   A C   1 
ATOM   468  O O   . LYS   A 1 67  ? -17.22698 -6.52015  -29.11617 1.000 30.68727  ? 74  LYS   A O   1 
ATOM   469  C CB  . LYS   A 1 67  ? -19.04437 -7.08838  -31.61003 1.000 28.65478  ? 74  LYS   A CB  1 
ATOM   470  C CG  . LYS   A 1 67  ? -19.27657 -6.94530  -33.10925 1.000 45.17551  ? 74  LYS   A CG  1 
ATOM   471  C CD  . LYS   A 1 67  ? -20.25248 -5.82604  -33.43924 1.000 51.69548  ? 74  LYS   A CD  1 
ATOM   472  C CE  . LYS   A 1 67  ? -20.82080 -6.00313  -34.84172 1.000 63.12174  ? 74  LYS   A CE  1 
ATOM   473  N NZ  . LYS   A 1 67  ? -21.53653 -4.78959  -35.33148 1.000 78.97135  ? 74  LYS   A NZ  1 
ATOM   474  N N   . GLU   A 1 68  ? -17.56122 -8.74486  -29.12488 1.000 25.71926  ? 75  GLU   A N   1 
ATOM   475  C CA  . GLU   A 1 68  ? -17.52089 -8.85001  -27.66901 1.000 27.40109  ? 75  GLU   A CA  1 
ATOM   476  C C   . GLU   A 1 68  ? -16.09398 -8.69209  -27.15219 1.000 28.85577  ? 75  GLU   A C   1 
ATOM   477  O O   . GLU   A 1 68  ? -15.16394 -9.32366  -27.66003 1.000 28.76061  ? 75  GLU   A O   1 
ATOM   478  C CB  . GLU   A 1 68  ? -18.09604 -10.19071 -27.20708 1.000 34.19398  ? 75  GLU   A CB  1 
ATOM   479  C CG  . GLU   A 1 68  ? -19.61826 -10.27739 -27.24433 1.000 41.81007  ? 75  GLU   A CG  1 
ATOM   480  C CD  . GLU   A 1 68  ? -20.16726 -10.40281 -28.65270 1.000 72.20005  ? 75  GLU   A CD  1 
ATOM   481  O OE1 . GLU   A 1 68  ? -19.67000 -11.26989 -29.40115 1.000 70.50955  ? 75  GLU   A OE1 1 
ATOM   482  O OE2 . GLU   A 1 68  ? -21.09472 -9.64159  -29.01142 1.000 65.23628  ? 75  GLU   A OE2 1 
ATOM   483  N N   . LEU   A 1 69  ? -15.92812 -7.85667  -26.13136 1.000 22.78790  ? 76  LEU   A N   1 
ATOM   484  C CA  . LEU   A 1 69  ? -14.63382 -7.59760  -25.50754 1.000 21.12034  ? 76  LEU   A CA  1 
ATOM   485  C C   . LEU   A 1 69  ? -14.69863 -8.13776  -24.08420 1.000 21.98120  ? 76  LEU   A C   1 
ATOM   486  O O   . LEU   A 1 69  ? -15.34076 -7.53053  -23.22159 1.000 19.99777  ? 76  LEU   A O   1 
ATOM   487  C CB  . LEU   A 1 69  ? -14.33059 -6.10021  -25.52283 1.000 24.96837  ? 76  LEU   A CB  1 
ATOM   488  C CG  . LEU   A 1 69  ? -14.21570 -5.45063  -26.90745 1.000 27.15551  ? 76  LEU   A CG  1 
ATOM   489  C CD1 . LEU   A 1 69  ? -13.69706 -4.02359  -26.79690 1.000 31.37842  ? 76  LEU   A CD1 1 
ATOM   490  C CD2 . LEU   A 1 69  ? -13.30870 -6.27486  -27.80526 1.000 23.99853  ? 76  LEU   A CD2 1 
ATOM   491  N N   . HIS   A 1 70  ? -14.05712 -9.27950  -23.83311 1.000 19.91173  ? 77  HIS   A N   1 
ATOM   492  C CA  . HIS   A 1 70  ? -14.20721 -9.91165  -22.52747 1.000 17.47594  ? 77  HIS   A CA  1 
ATOM   493  C C   . HIS   A 1 70  ? -13.00649 -10.79363 -22.21711 1.000 15.75157  ? 77  HIS   A C   1 
ATOM   494  O O   . HIS   A 1 70  ? -12.13238 -11.02729 -23.05859 1.000 15.51575  ? 77  HIS   A O   1 
ATOM   495  C CB  . HIS   A 1 70  ? -15.49198 -10.74312 -22.45724 1.000 23.07985  ? 77  HIS   A CB  1 
ATOM   496  C CG  . HIS   A 1 70  ? -15.55787 -11.82844 -23.48459 1.000 25.80231  ? 77  HIS   A CG  1 
ATOM   497  N ND1 . HIS   A 1 70  ? -16.54653 -11.88807 -24.44140 1.000 32.27275  ? 77  HIS   A ND1 1 
ATOM   498  C CD2 . HIS   A 1 70  ? -14.75434 -12.89554 -23.70705 1.000 28.61589  ? 77  HIS   A CD2 1 
ATOM   499  C CE1 . HIS   A 1 70  ? -16.34899 -12.94415 -25.21007 1.000 30.41612  ? 77  HIS   A CE1 1 
ATOM   500  N NE2 . HIS   A 1 70  ? -15.26753 -13.57196 -24.78600 1.000 31.45995  ? 77  HIS   A NE2 1 
ATOM   501  N N   . ILE   A 1 71  ? -13.00970 -11.30895 -20.98720 1.000 15.77341  ? 78  ILE   A N   1 
ATOM   502  C CA  . ILE   A 1 71  ? -11.97843 -12.18694 -20.44698 1.000 14.85766  ? 78  ILE   A CA  1 
ATOM   503  C C   . ILE   A 1 71  ? -12.67267 -13.38433 -19.80920 1.000 18.55824  ? 78  ILE   A C   1 
ATOM   504  O O   . ILE   A 1 71  ? -13.55673 -13.20682 -18.96504 1.000 17.26651  ? 78  ILE   A O   1 
ATOM   505  C CB  . ILE   A 1 71  ? -11.12118 -11.46431 -19.38893 1.000 19.68712  ? 78  ILE   A CB  1 
ATOM   506  C CG1 . ILE   A 1 71  ? -10.45172 -10.22263 -19.98035 1.000 19.01190  ? 78  ILE   A CG1 1 
ATOM   507  C CG2 . ILE   A 1 71  ? -10.09537 -12.42806 -18.78835 1.000 18.87630  ? 78  ILE   A CG2 1 
ATOM   508  C CD1 . ILE   A 1 71  ? -9.74793  -9.36580  -18.94325 1.000 19.79114  ? 78  ILE   A CD1 1 
ATOM   509  N N   . ASN   A 1 72  ? -12.27503 -14.59537 -20.19840 1.000 15.29717  ? 79  ASN   A N   1 
ATOM   510  C CA  . ASN   A 1 72  ? -12.81258 -15.81362 -19.60392 1.000 17.02936  ? 79  ASN   A CA  1 
ATOM   511  C C   . ASN   A 1 72  ? -11.70030 -16.57591 -18.90118 1.000 19.73953  ? 79  ASN   A C   1 
ATOM   512  O O   . ASN   A 1 72  ? -10.58831 -16.69032 -19.42345 1.000 17.10150  ? 79  ASN   A O   1 
ATOM   513  C CB  . ASN   A 1 72  ? -13.47278 -16.73648 -20.64547 1.000 17.07989  ? 79  ASN   A CB  1 
ATOM   514  C CG  . ASN   A 1 72  ? -14.67188 -16.10585 -21.31017 1.000 25.04804  ? 79  ASN   A CG  1 
ATOM   515  O OD1 . ASN   A 1 72  ? -15.39488 -15.32218 -20.69458 1.000 24.59708  ? 79  ASN   A OD1 1 
ATOM   516  N ND2 . ASN   A 1 72  ? -14.91253 -16.47131 -22.56739 1.000 21.85025  ? 79  ASN   A ND2 1 
ATOM   517  N N   . LEU   A 1 73  ? -12.01667 -17.11993 -17.72774 1.000 16.77730  ? 80  LEU   A N   1 
ATOM   518  C CA  . LEU   A 1 73  ? -11.09315 -17.95088 -16.96231 1.000 14.66960  ? 80  LEU   A CA  1 
ATOM   519  C C   . LEU   A 1 73  ? -11.64188 -19.36920 -16.94515 1.000 15.79827  ? 80  LEU   A C   1 
ATOM   520  O O   . LEU   A 1 73  ? -12.75272 -19.59806 -16.45906 1.000 17.15402  ? 80  LEU   A O   1 
ATOM   521  C CB  . LEU   A 1 73  ? -10.93090 -17.42454 -15.53418 1.000 17.40384  ? 80  LEU   A CB  1 
ATOM   522  C CG  . LEU   A 1 73  ? -10.54255 -15.94999 -15.38145 1.000 19.30699  ? 80  LEU   A CG  1 
ATOM   523  C CD1 . LEU   A 1 73  ? -10.40531 -15.59581 -13.90898 1.000 17.97010  ? 80  LEU   A CD1 1 
ATOM   524  C CD2 . LEU   A 1 73  ? -9.25445  -15.66012 -16.12546 1.000 17.02702  ? 80  LEU   A CD2 1 
ATOM   525  N N   . ILE   A 1 74  ? -10.87167 -20.31609 -17.47211 1.000 15.63601  ? 81  ILE   A N   1 
ATOM   526  C CA  . ILE   A 1 74  ? -11.37851 -21.67169 -17.67163 1.000 17.11889  ? 81  ILE   A CA  1 
ATOM   527  C C   . ILE   A 1 74  ? -10.48435 -22.68699 -16.97092 1.000 21.92271  ? 81  ILE   A C   1 
ATOM   528  O O   . ILE   A 1 74  ? -9.46205  -23.10799 -17.53204 1.000 18.34554  ? 81  ILE   A O   1 
ATOM   529  C CB  . ILE   A 1 74  ? -11.50978 -22.00834 -19.16582 1.000 18.04129  ? 81  ILE   A CB  1 
ATOM   530  C CG1 . ILE   A 1 74  ? -12.24529 -20.88467 -19.90245 1.000 19.03473  ? 81  ILE   A CG1 1 
ATOM   531  C CG2 . ILE   A 1 74  ? -12.22049 -23.34517 -19.34139 1.000 20.22134  ? 81  ILE   A CG2 1 
ATOM   532  C CD1 . ILE   A 1 74  ? -12.41135 -21.13426 -21.38855 1.000 23.87919  ? 81  ILE   A CD1 1 
ATOM   533  N N   . PRO   A 1 75  ? -10.84026 -23.11935 -15.76394 1.000 20.93517  ? 82  PRO   A N   1 
ATOM   534  C CA  . PRO   A 1 75  ? -10.09057 -24.19491 -15.11238 1.000 20.99163  ? 82  PRO   A CA  1 
ATOM   535  C C   . PRO   A 1 75  ? -10.53769 -25.55705 -15.61921 1.000 23.75393  ? 82  PRO   A C   1 
ATOM   536  O O   . PRO   A 1 75  ? -11.71776 -25.78196 -15.90456 1.000 22.54274  ? 82  PRO   A O   1 
ATOM   537  C CB  . PRO   A 1 75  ? -10.43900 -24.00785 -13.63147 1.000 20.87451  ? 82  PRO   A CB  1 
ATOM   538  C CG  . PRO   A 1 75  ? -11.82906 -23.43915 -13.65279 1.000 22.99024  ? 82  PRO   A CG  1 
ATOM   539  C CD  . PRO   A 1 75  ? -12.01774 -22.70787 -14.97712 1.000 19.33776  ? 82  PRO   A CD  1 
ATOM   540  N N   . ASN   A 1 76  ? -9.57465  -26.47197 -15.73363 1.000 19.47528  ? 83  ASN   A N   1 
ATOM   541  C CA  . ASN   A 1 76  ? -9.84851  -27.85045 -16.13724 1.000 23.07347  ? 83  ASN   A CA  1 
ATOM   542  C C   . ASN   A 1 76  ? -9.02048  -28.77632 -15.25617 1.000 22.94388  ? 83  ASN   A C   1 
ATOM   543  O O   . ASN   A 1 76  ? -7.80480  -28.88648 -15.44168 1.000 25.91362  ? 83  ASN   A O   1 
ATOM   544  C CB  . ASN   A 1 76  ? -9.52847  -28.07060 -17.61636 1.000 25.34482  ? 83  ASN   A CB  1 
ATOM   545  C CG  . ASN   A 1 76  ? -10.01741 -29.41827 -18.12889 1.000 29.84142  ? 83  ASN   A CG  1 
ATOM   546  O OD1 . ASN   A 1 76  ? -9.79407  -30.45733 -17.50320 1.000 33.21428  ? 83  ASN   A OD1 1 
ATOM   547  N ND2 . ASN   A 1 76  ? -10.68874 -29.40531 -19.27408 1.000 34.66147  ? 83  ASN   A ND2 1 
ATOM   548  N N   . LYS   A 1 77  ? -9.67862  -29.45773 -14.31563 1.000 29.05803  ? 84  LYS   A N   1 
ATOM   549  C CA  . LYS   A 1 77  ? -8.95817  -30.29392 -13.36118 1.000 29.63462  ? 84  LYS   A CA  1 
ATOM   550  C C   . LYS   A 1 77  ? -8.46146  -31.59428 -13.97964 1.000 37.48125  ? 84  LYS   A C   1 
ATOM   551  O O   . LYS   A 1 77  ? -7.47073  -32.15833 -13.50319 1.000 33.26618  ? 84  LYS   A O   1 
ATOM   552  C CB  . LYS   A 1 77  ? -9.84632  -30.60717 -12.15867 1.000 32.20976  ? 84  LYS   A CB  1 
ATOM   553  C CG  . LYS   A 1 77  ? -10.03623 -29.43838 -11.21066 1.000 36.92442  ? 84  LYS   A CG  1 
ATOM   554  C CD  . LYS   A 1 77  ? -10.78002 -29.88007 -9.95911  1.000 42.75637  ? 84  LYS   A CD  1 
ATOM   555  C CE  . LYS   A 1 77  ? -11.08003 -28.70198 -9.05140  1.000 43.70124  ? 84  LYS   A CE  1 
ATOM   556  N NZ  . LYS   A 1 77  ? -11.99626 -27.73442 -9.71194  1.000 45.97306  ? 84  LYS   A NZ  1 
ATOM   557  N N   . GLN   A 1 78  ? -9.13542  -32.09565 -15.01663 1.000 33.83896  ? 85  GLN   A N   1 
ATOM   558  C CA  . GLN   A 1 78  ? -8.68049  -33.32251 -15.66328 1.000 42.27367  ? 85  GLN   A CA  1 
ATOM   559  C C   . GLN   A 1 78  ? -7.37961  -33.08673 -16.41794 1.000 35.55864  ? 85  GLN   A C   1 
ATOM   560  O O   . GLN   A 1 78  ? -6.43870  -33.88258 -16.31992 1.000 40.62234  ? 85  GLN   A O   1 
ATOM   561  C CB  . GLN   A 1 78  ? -9.75949  -33.85591 -16.60498 1.000 40.37839  ? 85  GLN   A CB  1 
ATOM   562  C CG  . GLN   A 1 78  ? -10.89615 -34.58319 -15.91056 1.000 55.53755  ? 85  GLN   A CG  1 
ATOM   563  C CD  . GLN   A 1 78  ? -11.76440 -33.65491 -15.08636 1.000 75.75754  ? 85  GLN   A CD  1 
ATOM   564  O OE1 . GLN   A 1 78  ? -11.89707 -33.82325 -13.87312 1.000 72.33749  ? 85  GLN   A OE1 1 
ATOM   565  N NE2 . GLN   A 1 78  ? -12.35439 -32.65962 -15.74173 1.000 70.37985  ? 85  GLN   A NE2 1 
ATOM   566  N N   . ASP   A 1 79  ? -7.31215  -31.99340 -17.17609 1.000 29.37831  ? 86  ASP   A N   1 
ATOM   567  C CA  . ASP   A 1 79  ? -6.11054  -31.61308 -17.90300 1.000 35.84886  ? 86  ASP   A CA  1 
ATOM   568  C C   . ASP   A 1 79  ? -5.09897  -30.89463 -17.02313 1.000 30.69535  ? 86  ASP   A C   1 
ATOM   569  O O   . ASP   A 1 79  ? -3.95120  -30.71958 -17.44698 1.000 30.75610  ? 86  ASP   A O   1 
ATOM   570  C CB  . ASP   A 1 79  ? -6.48261  -30.71319 -19.08304 1.000 31.68704  ? 86  ASP   A CB  1 
ATOM   571  C CG  . ASP   A 1 79  ? -7.32568  -31.43218 -20.12108 1.000 47.49482  ? 86  ASP   A CG  1 
ATOM   572  O OD1 . ASP   A 1 79  ? -7.48419  -32.66636 -20.01022 1.000 46.05038  ? 86  ASP   A OD1 1 
ATOM   573  O OD2 . ASP   A 1 79  ? -7.84084  -30.76053 -21.03938 1.000 52.06880  ? 86  ASP   A OD2 1 
ATOM   574  N N   . ARG   A 1 80  ? -5.50234  -30.49417 -15.81713 1.000 31.59048  ? 87  ARG   A N   1 
ATOM   575  C CA  . ARG   A 1 80  ? -4.69549  -29.67098 -14.91707 1.000 24.14455  ? 87  ARG   A CA  1 
ATOM   576  C C   . ARG   A 1 80  ? -4.20916  -28.40110 -15.61578 1.000 25.45479  ? 87  ARG   A C   1 
ATOM   577  O O   . ARG   A 1 80  ? -3.02521  -28.05655 -15.60034 1.000 22.81728  ? 87  ARG   A O   1 
ATOM   578  C CB  . ARG   A 1 80  ? -3.52965  -30.46848 -14.32699 1.000 26.99973  ? 87  ARG   A CB  1 
ATOM   579  C CG  . ARG   A 1 80  ? -3.14498  -29.98360 -12.93971 1.000 28.06348  ? 87  ARG   A CG  1 
ATOM   580  C CD  . ARG   A 1 80  ? -1.67783  -30.20293 -12.62894 1.000 38.11161  ? 87  ARG   A CD  1 
ATOM   581  N NE  . ARG   A 1 80  ? -1.35484  -31.61247 -12.47158 1.000 46.76958  ? 87  ARG   A NE  1 
ATOM   582  C CZ  . ARG   A 1 80  ? -0.13983  -32.12206 -12.61716 1.000 54.04780  ? 87  ARG   A CZ  1 
ATOM   583  N NH1 . ARG   A 1 80  ? 0.89050   -31.36701 -12.96389 1.000 40.28364  ? 87  ARG   A NH1 1 
ATOM   584  N NH2 . ARG   A 1 80  ? 0.04738   -33.42005 -12.40304 1.000 48.66994  ? 87  ARG   A NH2 1 
ATOM   585  N N   . THR   A 1 81  ? -5.14695  -27.69159 -16.23350 1.000 21.07664  ? 88  THR   A N   1 
ATOM   586  C CA  . THR   A 1 81  ? -4.84015  -26.45442 -16.93047 1.000 19.22548  ? 88  THR   A CA  1 
ATOM   587  C C   . THR   A 1 81  ? -5.76122  -25.34485 -16.45182 1.000 21.08786  ? 88  THR   A C   1 
ATOM   588  O O   . THR   A 1 81  ? -6.93132  -25.57532 -16.14019 1.000 20.92534  ? 88  THR   A O   1 
ATOM   589  C CB  . THR   A 1 81  ? -4.98996  -26.59459 -18.45058 1.000 24.69588  ? 88  THR   A CB  1 
ATOM   590  O OG1 . THR   A 1 81  ? -6.32356  -27.02642 -18.75112 1.000 22.55441  ? 88  THR   A OG1 1 
ATOM   591  C CG2 . THR   A 1 81  ? -3.98308  -27.59867 -19.00859 1.000 23.70142  ? 88  THR   A CG2 1 
ATOM   592  N N   . LEU   A 1 82  ? -5.21139  -24.13801 -16.39672 1.000 16.95294  ? 89  LEU   A N   1 
ATOM   593  C CA  . LEU   A 1 82  ? -5.98256  -22.91424 -16.23409 1.000 16.53011  ? 89  LEU   A CA  1 
ATOM   594  C C   . LEU   A 1 82  ? -5.78147  -22.08431 -17.49474 1.000 19.27806  ? 89  LEU   A C   1 
ATOM   595  O O   . LEU   A 1 82  ? -4.64364  -21.76409 -17.85349 1.000 18.48915  ? 89  LEU   A O   1 
ATOM   596  C CB  . LEU   A 1 82  ? -5.54418  -22.13446 -14.99019 1.000 19.72197  ? 89  LEU   A CB  1 
ATOM   597  C CG  . LEU   A 1 82  ? -6.24725  -20.78547 -14.79202 1.000 19.93534  ? 89  LEU   A CG  1 
ATOM   598  C CD1 . LEU   A 1 82  ? -7.74227  -20.98477 -14.66542 1.000 18.03258  ? 89  LEU   A CD1 1 
ATOM   599  C CD2 . LEU   A 1 82  ? -5.70688  -20.07006 -13.55558 1.000 19.64559  ? 89  LEU   A CD2 1 
ATOM   600  N N   . THR   A 1 83  ? -6.87519  -21.74823 -18.17015 1.000 17.99560  ? 90  THR   A N   1 
ATOM   601  C CA  . THR   A 1 83  ? -6.82009  -21.02726 -19.43364 1.000 17.07944  ? 90  THR   A CA  1 
ATOM   602  C C   . THR   A 1 83  ? -7.41343  -19.63341 -19.26867 1.000 20.05917  ? 90  THR   A C   1 
ATOM   603  O O   . THR   A 1 83  ? -8.51708  -19.48193 -18.73198 1.000 18.36833  ? 90  THR   A O   1 
ATOM   604  C CB  . THR   A 1 83  ? -7.56571  -21.79198 -20.52775 1.000 19.79331  ? 90  THR   A CB  1 
ATOM   605  O OG1 . THR   A 1 83  ? -6.94666  -23.06771 -20.74360 1.000 20.39790  ? 90  THR   A OG1 1 
ATOM   606  C CG2 . THR   A 1 83  ? -7.54171  -21.00965 -21.81073 1.000 22.58189  ? 90  THR   A CG2 1 
ATOM   607  N N   . ILE   A 1 84  ? -6.67776  -18.62158 -19.72253 1.000 15.29721  ? 91  ILE   A N   1 
ATOM   608  C CA  . ILE   A 1 84  ? -7.12936  -17.23197 -19.69618 1.000 18.11146  ? 91  ILE   A CA  1 
ATOM   609  C C   . ILE   A 1 84  ? -7.36330  -16.81685 -21.14310 1.000 20.37875  ? 91  ILE   A C   1 
ATOM   610  O O   . ILE   A 1 84  ? -6.41371  -16.73092 -21.93325 1.000 18.51796  ? 91  ILE   A O   1 
ATOM   611  C CB  . ILE   A 1 84  ? -6.11522  -16.30581 -19.00459 1.000 18.00351  ? 91  ILE   A CB  1 
ATOM   612  C CG1 . ILE   A 1 84  ? -5.94299  -16.69801 -17.53517 1.000 26.20365  ? 91  ILE   A CG1 1 
ATOM   613  C CG2 . ILE   A 1 84  ? -6.56391  -14.84460 -19.09687 1.000 14.78856  ? 91  ILE   A CG2 1 
ATOM   614  C CD1 . ILE   A 1 84  ? -4.71642  -17.53807 -17.26266 1.000 30.80921  ? 91  ILE   A CD1 1 
ATOM   615  N N   . VAL   A 1 85  ? -8.62491  -16.56865 -21.49674 1.000 16.31926  ? 92  VAL   A N   1 
ATOM   616  C CA  . VAL   A 1 85  ? -9.01778  -16.21110 -22.85639 1.000 18.15641  ? 92  VAL   A CA  1 
ATOM   617  C C   . VAL   A 1 85  ? -9.43370  -14.75101 -22.88426 1.000 23.68115  ? 92  VAL   A C   1 
ATOM   618  O O   . VAL   A 1 85  ? -10.20318 -14.30361 -22.02827 1.000 19.83929  ? 92  VAL   A O   1 
ATOM   619  C CB  . VAL   A 1 85  ? -10.17158 -17.09388 -23.37234 1.000 19.74954  ? 92  VAL   A CB  1 
ATOM   620  C CG1 . VAL   A 1 85  ? -10.38903 -16.86182 -24.86796 1.000 20.52553  ? 92  VAL   A CG1 1 
ATOM   621  C CG2 . VAL   A 1 85  ? -9.90166  -18.55994 -23.07834 1.000 22.04683  ? 92  VAL   A CG2 1 
ATOM   622  N N   . ASP   A 1 86  ? -8.95002  -14.01422 -23.88444 1.000 18.09083  ? 93  ASP   A N   1 
ATOM   623  C CA  . ASP   A 1 86  ? -9.41930  -12.65524 -24.10888 1.000 18.59533  ? 93  ASP   A CA  1 
ATOM   624  C C   . ASP   A 1 86  ? -9.66984  -12.45987 -25.59573 1.000 20.72185  ? 93  ASP   A C   1 
ATOM   625  O O   . ASP   A 1 86  ? -9.08119  -13.14362 -26.43806 1.000 20.97469  ? 93  ASP   A O   1 
ATOM   626  C CB  . ASP   A 1 86  ? -8.41979  -11.60473 -23.56021 1.000 18.50003  ? 93  ASP   A CB  1 
ATOM   627  C CG  . ASP   A 1 86  ? -7.11537  -11.54285 -24.34647 1.000 26.87263  ? 93  ASP   A CG  1 
ATOM   628  O OD1 . ASP   A 1 86  ? -6.04253  -11.77615 -23.74295 1.000 21.90731  ? 93  ASP   A OD1 1 
ATOM   629  O OD2 . ASP   A 1 86  ? -7.14486  -11.18333 -25.54615 1.000 24.41849  ? 93  ASP   A OD2 1 
ATOM   630  N N   . THR   A 1 87  ? -10.56852 -11.53224 -25.91109 1.000 17.05754  ? 94  THR   A N   1 
ATOM   631  C CA  . THR   A 1 87  ? -10.84828 -11.16104 -27.29677 1.000 19.10800  ? 94  THR   A CA  1 
ATOM   632  C C   . THR   A 1 87  ? -10.17075 -9.84574  -27.66596 1.000 26.65764  ? 94  THR   A C   1 
ATOM   633  O O   . THR   A 1 87  ? -10.72994 -9.01587  -28.38937 1.000 20.10750  ? 94  THR   A O   1 
ATOM   634  C CB  . THR   A 1 87  ? -12.35288 -11.09351 -27.53451 1.000 20.22557  ? 94  THR   A CB  1 
ATOM   635  O OG1 . THR   A 1 87  ? -12.95966 -10.20996 -26.58399 1.000 21.30277  ? 94  THR   A OG1 1 
ATOM   636  C CG2 . THR   A 1 87  ? -12.97266 -12.48463 -27.40265 1.000 23.20594  ? 94  THR   A CG2 1 
ATOM   637  N N   . GLY   A 1 88  ? -8.95170  -9.63566  -27.16703 1.000 16.93183  ? 95  GLY   A N   1 
ATOM   638  C CA  . GLY   A 1 88  ? -8.20047  -8.43572  -27.47474 1.000 20.24879  ? 95  GLY   A CA  1 
ATOM   639  C C   . GLY   A 1 88  ? -7.61809  -8.42862  -28.87512 1.000 22.47467  ? 95  GLY   A C   1 
ATOM   640  O O   . GLY   A 1 88  ? -8.05438  -9.18256  -29.75159 1.000 21.05647  ? 95  GLY   A O   1 
ATOM   641  N N   . ILE   A 1 89  ? -6.61381  -7.57757  -29.09284 1.000 21.28686  ? 96  ILE   A N   1 
ATOM   642  C CA  . ILE   A 1 89  ? -6.08313  -7.37147  -30.43769 1.000 19.54970  ? 96  ILE   A CA  1 
ATOM   643  C C   . ILE   A 1 89  ? -5.29878  -8.58169  -30.94781 1.000 23.29205  ? 96  ILE   A C   1 
ATOM   644  O O   . ILE   A 1 89  ? -5.10691  -8.72517  -32.16093 1.000 22.12173  ? 96  ILE   A O   1 
ATOM   645  C CB  . ILE   A 1 89  ? -5.22190  -6.09224  -30.44760 1.000 22.46210  ? 96  ILE   A CB  1 
ATOM   646  C CG1 . ILE   A 1 89  ? -4.93383  -5.62356  -31.88001 1.000 24.10873  ? 96  ILE   A CG1 1 
ATOM   647  C CG2 . ILE   A 1 89  ? -3.93177  -6.31813  -29.66650 1.000 16.80543  ? 96  ILE   A CG2 1 
ATOM   648  C CD1 . ILE   A 1 89  ? -4.49095  -4.18629  -31.95330 1.000 26.05188  ? 96  ILE   A CD1 1 
ATOM   649  N N   . GLY   A 1 90  ? -4.84764  -9.46669  -30.06082 1.000 18.97048  ? 97  GLY   A N   1 
ATOM   650  C CA  . GLY   A 1 90  ? -4.06471  -10.61571 -30.48307 1.000 20.76938  ? 97  GLY   A CA  1 
ATOM   651  C C   . GLY   A 1 90  ? -2.62829  -10.24735 -30.82689 1.000 19.00253  ? 97  GLY   A C   1 
ATOM   652  O O   . GLY   A 1 90  ? -2.18241  -9.11119  -30.66924 1.000 21.26648  ? 97  GLY   A O   1 
ATOM   653  N N   . MET   A 1 91  ? -1.89511  -11.25126 -31.30451 1.000 18.00094  ? 98  MET   A N   1 
ATOM   654  C CA  . MET   A 1 91  ? -0.51273  -11.04712 -31.71265 1.000 17.25530  ? 98  MET   A CA  1 
ATOM   655  C C   . MET   A 1 91  ? -0.25533  -11.73191 -33.04460 1.000 19.07467  ? 98  MET   A C   1 
ATOM   656  O O   . MET   A 1 91  ? -0.79588  -12.80735 -33.31868 1.000 20.39462  ? 98  MET   A O   1 
ATOM   657  C CB  . MET   A 1 91  ? 0.50799   -11.58662 -30.69006 1.000 18.94697  ? 98  MET   A CB  1 
ATOM   658  C CG  . MET   A 1 91  ? 0.47837   -10.93624 -29.31823 1.000 22.28319  ? 98  MET   A CG  1 
ATOM   659  S SD  . MET   A 1 91  ? 1.45949   -11.89837 -28.14514 1.000 24.57162  ? 98  MET   A SD  1 
ATOM   660  C CE  . MET   A 1 91  ? 0.25009   -13.11484 -27.61593 1.000 20.67976  ? 98  MET   A CE  1 
ATOM   661  N N   . THR   A 1 92  ? 0.58501   -11.10397 -33.85848 1.000 22.23264  ? 99  THR   A N   1 
ATOM   662  C CA  . THR   A 1 92  ? 1.07437   -11.70523 -35.08766 1.000 23.06147  ? 99  THR   A CA  1 
ATOM   663  C C   . THR   A 1 92  ? 2.15551   -12.73815 -34.77358 1.000 19.47817  ? 99  THR   A C   1 
ATOM   664  O O   . THR   A 1 92  ? 2.64413   -12.84013 -33.64674 1.000 21.65747  ? 99  THR   A O   1 
ATOM   665  C CB  . THR   A 1 92  ? 1.64592   -10.63267 -36.00915 1.000 20.34250  ? 99  THR   A CB  1 
ATOM   666  O OG1 . THR   A 1 92  ? 2.79107   -10.04533 -35.37196 1.000 23.76216  ? 99  THR   A OG1 1 
ATOM   667  C CG2 . THR   A 1 92  ? 0.61478   -9.54595  -36.27731 1.000 21.39627  ? 99  THR   A CG2 1 
ATOM   668  N N   . LYS   A 1 93  ? 2.53742   -13.50991 -35.79796 1.000 20.60202  ? 100 LYS   A N   1 
ATOM   669  C CA  . LYS   A 1 93  ? 3.67447   -14.41576 -35.64726 1.000 25.66406  ? 100 LYS   A CA  1 
ATOM   670  C C   . LYS   A 1 93  ? 4.92583   -13.66228 -35.22074 1.000 25.37961  ? 100 LYS   A C   1 
ATOM   671  O O   . LYS   A 1 93  ? 5.66907   -14.12105 -34.34344 1.000 22.77229  ? 100 LYS   A O   1 
ATOM   672  C CB  . LYS   A 1 93  ? 3.93867   -15.16817 -36.95085 1.000 24.46041  ? 100 LYS   A CB  1 
ATOM   673  C CG  . LYS   A 1 93  ? 4.91105   -16.33789 -36.78797 1.000 24.61523  ? 100 LYS   A CG  1 
ATOM   674  C CD  . LYS   A 1 93  ? 5.21863   -16.98708 -38.13639 1.000 30.03172  ? 100 LYS   A CD  1 
ATOM   675  C CE  . LYS   A 1 93  ? 6.10075   -18.20626 -37.96526 1.000 34.62482  ? 100 LYS   A CE  1 
ATOM   676  N NZ  . LYS   A 1 93  ? 6.89346   -18.48306 -39.19398 1.000 35.70931  ? 100 LYS   A NZ  1 
ATOM   677  N N   . ALA   A 1 94  ? 5.18132   -12.50662 -35.84085 1.000 24.02287  ? 101 ALA   A N   1 
ATOM   678  C CA  . ALA   A 1 94  ? 6.34980   -11.71742 -35.46943 1.000 29.40216  ? 101 ALA   A CA  1 
ATOM   679  C C   . ALA   A 1 94  ? 6.27275   -11.27987 -34.01237 1.000 25.10139  ? 101 ALA   A C   1 
ATOM   680  O O   . ALA   A 1 94  ? 7.27753   -11.32453 -33.29398 1.000 29.07255  ? 101 ALA   A O   1 
ATOM   681  C CB  . ALA   A 1 94  ? 6.48481   -10.50509 -36.39079 1.000 27.66860  ? 101 ALA   A CB  1 
ATOM   682  N N   . ASP   A 1 95  ? 5.08413   -10.86367 -33.55579 1.000 20.31460  ? 102 ASP   A N   1 
ATOM   683  C CA  . ASP   A 1 95  ? 4.91552   -10.47188 -32.15500 1.000 22.80926  ? 102 ASP   A CA  1 
ATOM   684  C C   . ASP   A 1 95  ? 5.24918   -11.62593 -31.21862 1.000 21.62396  ? 102 ASP   A C   1 
ATOM   685  O O   . ASP   A 1 95  ? 5.97199   -11.45008 -30.23172 1.000 23.98921  ? 102 ASP   A O   1 
ATOM   686  C CB  . ASP   A 1 95  ? 3.48209   -10.00291 -31.88673 1.000 22.37352  ? 102 ASP   A CB  1 
ATOM   687  C CG  . ASP   A 1 95  ? 3.16317   -8.66053  -32.50479 1.000 27.23043  ? 102 ASP   A CG  1 
ATOM   688  O OD1 . ASP   A 1 95  ? 4.04656   -7.78238  -32.53732 1.000 28.16834  ? 102 ASP   A OD1 1 
ATOM   689  O OD2 . ASP   A 1 95  ? 1.99336   -8.46580  -32.90851 1.000 35.24308  ? 102 ASP   A OD2 1 
ATOM   690  N N   . LEU   A 1 96  ? 4.69892   -12.81209 -31.49971 1.000 22.65398  ? 103 LEU   A N   1 
ATOM   691  C CA  . LEU   A 1 96  ? 4.97394   -13.99321 -30.68533 1.000 24.20598  ? 103 LEU   A CA  1 
ATOM   692  C C   . LEU   A 1 96  ? 6.47006   -14.23255 -30.55588 1.000 23.75562  ? 103 LEU   A C   1 
ATOM   693  O O   . LEU   A 1 96  ? 6.99038   -14.42121 -29.44956 1.000 23.92251  ? 103 LEU   A O   1 
ATOM   694  C CB  . LEU   A 1 96  ? 4.30715   -15.22384 -31.30282 1.000 20.73379  ? 103 LEU   A CB  1 
ATOM   695  C CG  . LEU   A 1 96  ? 2.82652   -15.48835 -31.06490 1.000 21.31858  ? 103 LEU   A CG  1 
ATOM   696  C CD1 . LEU   A 1 96  ? 2.42998   -16.79502 -31.75369 1.000 21.35495  ? 103 LEU   A CD1 1 
ATOM   697  C CD2 . LEU   A 1 96  ? 2.50978   -15.54812 -29.57820 1.000 19.17711  ? 103 LEU   A CD2 1 
ATOM   698  N N   . ILE   A 1 97  ? 7.17771   -14.22471 -31.68814 1.000 21.94209  ? 104 ILE   A N   1 
ATOM   699  C CA  . ILE   A 1 97  ? 8.60819   -14.50575 -31.67441 1.000 24.33175  ? 104 ILE   A CA  1 
ATOM   700  C C   . ILE   A 1 97  ? 9.36269   -13.41385 -30.92334 1.000 26.52965  ? 104 ILE   A C   1 
ATOM   701  O O   . ILE   A 1 97  ? 10.29836  -13.69518 -30.16490 1.000 26.21842  ? 104 ILE   A O   1 
ATOM   702  C CB  . ILE   A 1 97  ? 9.11876   -14.67029 -33.11639 1.000 28.37841  ? 104 ILE   A CB  1 
ATOM   703  C CG1 . ILE   A 1 97  ? 8.49678   -15.91827 -33.74957 1.000 24.61730  ? 104 ILE   A CG1 1 
ATOM   704  C CG2 . ILE   A 1 97  ? 10.64216  -14.76364 -33.13714 1.000 22.25757  ? 104 ILE   A CG2 1 
ATOM   705  C CD1 . ILE   A 1 97  ? 8.63241   -15.98306 -35.26924 1.000 23.81018  ? 104 ILE   A CD1 1 
ATOM   706  N N   . ASN   A 1 98  ? 8.96627   -12.15388 -31.11153 1.000 21.78473  ? 105 ASN   A N   1 
ATOM   707  C CA  . ASN   A 1 98  ? 9.58528   -11.03277 -30.40246 1.000 29.56512  ? 105 ASN   A CA  1 
ATOM   708  C C   . ASN   A 1 98  ? 8.98940   -10.88740 -28.99922 1.000 24.88394  ? 105 ASN   A C   1 
ATOM   709  O O   . ASN   A 1 98  ? 8.40145   -9.86992  -28.63141 1.000 25.24020  ? 105 ASN   A O   1 
ATOM   710  C CB  . ASN   A 1 98  ? 9.45845   -9.74256  -31.20763 1.000 27.89727  ? 105 ASN   A CB  1 
ATOM   711  C CG  . ASN   A 1 98  ? 10.20343  -9.80025  -32.52718 1.000 54.79162  ? 105 ASN   A CG  1 
ATOM   712  O OD1 . ASN   A 1 98  ? 9.66586   -10.22487 -33.55169 1.000 63.03500  ? 105 ASN   A OD1 1 
ATOM   713  N ND2 . ASN   A 1 98  ? 11.45995  -9.37061  -32.50540 1.000 55.06008  ? 105 ASN   A ND2 1 
ATOM   714  N N   . ASN   A 1 99  ? 9.15212   -11.95943 -28.21927 1.000 23.82730  ? 106 ASN   A N   1 
ATOM   715  C CA  . ASN   A 1 99  ? 8.82522   -11.98158 -26.79304 1.000 22.53266  ? 106 ASN   A CA  1 
ATOM   716  C C   . ASN   A 1 99  ? 7.37201   -11.59433 -26.52143 1.000 23.33650  ? 106 ASN   A C   1 
ATOM   717  O O   . ASN   A 1 99  ? 7.07134   -10.81686 -25.61288 1.000 22.03213  ? 106 ASN   A O   1 
ATOM   718  C CB  . ASN   A 1 99  ? 9.79940   -11.09736 -26.01631 1.000 19.36684  ? 106 ASN   A CB  1 
ATOM   719  C CG  . ASN   A 1 99  ? 11.23158  -11.57635 -26.16668 1.000 20.07149  ? 106 ASN   A CG  1 
ATOM   720  O OD1 . ASN   A 1 99  ? 11.50689  -12.76052 -25.98983 1.000 23.24940  ? 106 ASN   A OD1 1 
ATOM   721  N ND2 . ASN   A 1 99  ? 12.14155  -10.67080 -26.50833 1.000 22.22421  ? 106 ASN   A ND2 1 
ATOM   722  N N   . LEU   A 1 100 ? 6.46459   -12.17413 -27.30937 1.000 20.71360  ? 107 LEU   A N   1 
ATOM   723  C CA  . LEU   A 1 100 ? 5.02407   -11.98844 -27.12756 1.000 24.75377  ? 107 LEU   A CA  1 
ATOM   724  C C   . LEU   A 1 100 ? 4.65664   -10.50749 -27.06582 1.000 25.97211  ? 107 LEU   A C   1 
ATOM   725  O O   . LEU   A 1 100 ? 3.87902   -10.07018 -26.21573 1.000 21.43142  ? 107 LEU   A O   1 
ATOM   726  C CB  . LEU   A 1 100 ? 4.53863   -12.73864 -25.88403 1.000 21.27977  ? 107 LEU   A CB  1 
ATOM   727  C CG  . LEU   A 1 100 ? 4.89712   -14.22877 -25.97578 1.000 26.50693  ? 107 LEU   A CG  1 
ATOM   728  C CD1 . LEU   A 1 100 ? 6.00412   -14.59087 -24.99921 1.000 27.96785  ? 107 LEU   A CD1 1 
ATOM   729  C CD2 . LEU   A 1 100 ? 3.68516   -15.10756 -25.75902 1.000 27.15868  ? 107 LEU   A CD2 1 
ATOM   730  N N   . GLY   A 1 101 ? 5.23827   -9.72339  -27.97239 1.000 22.14766  ? 108 GLY   A N   1 
ATOM   731  C CA  . GLY   A 1 101 ? 4.87795   -8.32228  -28.08755 1.000 26.36710  ? 108 GLY   A CA  1 
ATOM   732  C C   . GLY   A 1 101 ? 5.37854   -7.42364  -26.98242 1.000 30.15888  ? 108 GLY   A C   1 
ATOM   733  O O   . GLY   A 1 101 ? 4.84624   -6.32319  -26.80732 1.000 29.77015  ? 108 GLY   A O   1 
ATOM   734  N N   . THR   A 1 102 ? 6.38852   -7.85238  -26.23014 1.000 22.62579  ? 109 THR   A N   1 
ATOM   735  C CA  . THR   A 1 102 ? 6.94708   -7.06232  -25.14383 1.000 24.79026  ? 109 THR   A CA  1 
ATOM   736  C C   . THR   A 1 102 ? 8.32428   -6.54416  -25.53214 1.000 27.37391  ? 109 THR   A C   1 
ATOM   737  O O   . THR   A 1 102 ? 8.94834   -7.02788  -26.47946 1.000 27.75488  ? 109 THR   A O   1 
ATOM   738  C CB  . THR   A 1 102 ? 7.05333   -7.89043  -23.85609 1.000 27.52235  ? 109 THR   A CB  1 
ATOM   739  O OG1 . THR   A 1 102 ? 8.08366   -8.87804  -24.01426 1.000 25.29605  ? 109 THR   A OG1 1 
ATOM   740  C CG2 . THR   A 1 102 ? 5.73628   -8.59120  -23.55729 1.000 25.38959  ? 109 THR   A CG2 1 
ATOM   741  N N   . ILE   A 1 103 ? 8.79032   -5.53785  -24.79403 1.000 21.85778  ? 110 ILE   A N   1 
ATOM   742  C CA  . ILE   A 1 103 ? 10.18045  -5.10875  -24.89517 1.000 23.89908  ? 110 ILE   A CA  1 
ATOM   743  C C   . ILE   A 1 103 ? 10.94962  -5.80424  -23.77851 1.000 24.21904  ? 110 ILE   A C   1 
ATOM   744  O O   . ILE   A 1 103 ? 11.52398  -5.16274  -22.88916 1.000 25.93005  ? 110 ILE   A O   1 
ATOM   745  C CB  . ILE   A 1 103 ? 10.31216  -3.57262  -24.85850 1.000 32.51633  ? 110 ILE   A CB  1 
ATOM   746  C CG1 . ILE   A 1 103 ? 9.60596   -2.96413  -23.64289 1.000 31.31027  ? 110 ILE   A CG1 1 
ATOM   747  C CG2 . ILE   A 1 103 ? 9.74413   -2.97202  -26.13348 1.000 33.72928  ? 110 ILE   A CG2 1 
ATOM   748  C CD1 . ILE   A 1 103 ? 9.94626   -1.50580  -23.41659 1.000 37.06285  ? 110 ILE   A CD1 1 
ATOM   749  N N   . ALA   A 1 104 ? 10.98146  -7.13779  -23.84350 1.000 21.72077  ? 111 ALA   A N   1 
ATOM   750  C CA  . ALA   A 1 104 ? 11.39789  -7.93781  -22.69745 1.000 21.59058  ? 111 ALA   A CA  1 
ATOM   751  C C   . ALA   A 1 104 ? 12.86860  -7.73998  -22.34571 1.000 22.11208  ? 111 ALA   A C   1 
ATOM   752  O O   . ALA   A 1 104 ? 13.23910  -7.87906  -21.17470 1.000 23.39261  ? 111 ALA   A O   1 
ATOM   753  C CB  . ALA   A 1 104 ? 11.11170  -9.41662  -22.96358 1.000 25.91379  ? 111 ALA   A CB  1 
ATOM   754  N N   . LYS   A 1 105 ? 13.71845  -7.42472  -23.32637 1.000 26.31019  ? 112 LYS   A N   1 
ATOM   755  C CA  . LYS   A 1 105 ? 15.14043  -7.25388  -23.03538 1.000 26.50486  ? 112 LYS   A CA  1 
ATOM   756  C C   . LYS   A 1 105 ? 15.36998  -6.08248  -22.08530 1.000 32.14243  ? 112 LYS   A C   1 
ATOM   757  O O   . LYS   A 1 105 ? 16.00549  -6.23560  -21.03710 1.000 30.97800  ? 112 LYS   A O   1 
ATOM   758  C CB  . LYS   A 1 105 ? 15.92933  -7.06971  -24.33504 1.000 28.29355  ? 112 LYS   A CB  1 
ATOM   759  C CG  . LYS   A 1 105 ? 17.43696  -7.27669  -24.20724 1.000 46.33162  ? 112 LYS   A CG  1 
ATOM   760  C CD  . LYS   A 1 105 ? 18.18510  -6.54293  -25.32000 1.000 39.80548  ? 112 LYS   A CD  1 
ATOM   761  C CE  . LYS   A 1 105 ? 19.61845  -6.18114  -24.93607 1.000 57.63328  ? 112 LYS   A CE  1 
ATOM   762  N NZ  . LYS   A 1 105 ? 20.18792  -7.03881  -23.85981 1.000 65.68358  ? 112 LYS   A NZ  1 
ATOM   763  N N   . SER   A 1 106 ? 14.85132  -4.90110  -22.42902 1.000 27.34034  ? 113 SER   A N   1 
ATOM   764  C CA  . SER   A 1 106 ? 15.03867  -3.75004  -21.55273 1.000 29.91556  ? 113 SER   A CA  1 
ATOM   765  C C   . SER   A 1 106 ? 14.17273  -3.85187  -20.30325 1.000 28.59773  ? 113 SER   A C   1 
ATOM   766  O O   . SER   A 1 106 ? 14.54105  -3.31608  -19.25308 1.000 31.07866  ? 113 SER   A O   1 
ATOM   767  C CB  . SER   A 1 106 ? 14.74564  -2.44924  -22.30496 1.000 38.19594  ? 113 SER   A CB  1 
ATOM   768  O OG  . SER   A 1 106 ? 13.41888  -2.42534  -22.79968 1.000 39.32167  ? 113 SER   A OG  1 
ATOM   769  N N   . GLY   A 1 107 ? 13.02600  -4.52930  -20.39168 1.000 26.53271  ? 114 GLY   A N   1 
ATOM   770  C CA  . GLY   A 1 107 ? 12.20767  -4.72740  -19.20511 1.000 27.66496  ? 114 GLY   A CA  1 
ATOM   771  C C   . GLY   A 1 107 ? 12.87195  -5.63156  -18.18344 1.000 30.83568  ? 114 GLY   A C   1 
ATOM   772  O O   . GLY   A 1 107 ? 12.83000  -5.35866  -16.97965 1.000 27.37313  ? 114 GLY   A O   1 
ATOM   773  N N   . THR   A 1 108 ? 13.49131  -6.72207  -18.64737 1.000 23.63731  ? 115 THR   A N   1 
ATOM   774  C CA  . THR   A 1 108 ? 14.22598  -7.60567  -17.74551 1.000 25.41971  ? 115 THR   A CA  1 
ATOM   775  C C   . THR   A 1 108 ? 15.38299  -6.87217  -17.08245 1.000 29.00886  ? 115 THR   A C   1 
ATOM   776  O O   . THR   A 1 108 ? 15.62460  -7.03491  -15.88011 1.000 31.78667  ? 115 THR   A O   1 
ATOM   777  C CB  . THR   A 1 108 ? 14.73674  -8.82883  -18.51355 1.000 23.86889  ? 115 THR   A CB  1 
ATOM   778  O OG1 . THR   A 1 108 ? 13.62042  -9.56261  -19.03490 1.000 27.39730  ? 115 THR   A OG1 1 
ATOM   779  C CG2 . THR   A 1 108 ? 15.55826  -9.73180  -17.61688 1.000 28.45262  ? 115 THR   A CG2 1 
ATOM   780  N N   . LYS   A 1 109 ? 16.11323  -6.06798  -17.85765 1.000 30.20525  ? 116 LYS   A N   1 
ATOM   781  C CA  . LYS   A 1 109 ? 17.20293  -5.26630  -17.30919 1.000 34.22636  ? 116 LYS   A CA  1 
ATOM   782  C C   . LYS   A 1 109 ? 16.72345  -4.40101  -16.14990 1.000 35.45996  ? 116 LYS   A C   1 
ATOM   783  O O   . LYS   A 1 109 ? 17.32439  -4.39267  -15.06924 1.000 39.73802  ? 116 LYS   A O   1 
ATOM   784  C CB  . LYS   A 1 109 ? 17.79890  -4.39831  -18.41552 1.000 36.25966  ? 116 LYS   A CB  1 
ATOM   785  C CG  . LYS   A 1 109 ? 19.09051  -3.69647  -18.05061 1.000 50.55360  ? 116 LYS   A CG  1 
ATOM   786  C CD  . LYS   A 1 109 ? 19.45866  -2.67346  -19.11294 1.000 52.89494  ? 116 LYS   A CD  1 
ATOM   787  C CE  . LYS   A 1 109 ? 20.92911  -2.29996  -19.03665 1.000 63.45101  ? 116 LYS   A CE  1 
ATOM   788  N NZ  . LYS   A 1 109 ? 21.28072  -1.77958  -17.68965 1.000 59.90946  ? 116 LYS   A NZ  1 
ATOM   789  N N   . ALA   A 1 110 ? 15.63403  -3.66191  -16.36251 1.000 34.28577  ? 117 ALA   A N   1 
ATOM   790  C CA  . ALA   A 1 110 ? 15.11605  -2.78844  -15.31621 1.000 39.13464  ? 117 ALA   A CA  1 
ATOM   791  C C   . ALA   A 1 110 ? 14.59255  -3.59364  -14.13432 1.000 36.32267  ? 117 ALA   A C   1 
ATOM   792  O O   . ALA   A 1 110 ? 14.82276  -3.23102  -12.97410 1.000 37.04903  ? 117 ALA   A O   1 
ATOM   793  C CB  . ALA   A 1 110 ? 14.01893  -1.89296  -15.88797 1.000 35.80209  ? 117 ALA   A CB  1 
ATOM   794  N N   . PHE   A 1 111 ? 13.88905  -4.69348  -14.41238 1.000 33.42562  ? 118 PHE   A N   1 
ATOM   795  C CA  . PHE   A 1 111 ? 13.31548  -5.51315  -13.34917 1.000 30.21503  ? 118 PHE   A CA  1 
ATOM   796  C C   . PHE   A 1 111 ? 14.40124  -6.05642  -12.42648 1.000 36.51748  ? 118 PHE   A C   1 
ATOM   797  O O   . PHE   A 1 111 ? 14.28091  -5.99131  -11.19851 1.000 34.77788  ? 118 PHE   A O   1 
ATOM   798  C CB  . PHE   A 1 111 ? 12.50317  -6.64620  -13.97556 1.000 26.52487  ? 118 PHE   A CB  1 
ATOM   799  C CG  . PHE   A 1 111 ? 11.83658  -7.55693  -12.98503 1.000 27.75351  ? 118 PHE   A CG  1 
ATOM   800  C CD1 . PHE   A 1 111 ? 11.22512  -7.05182  -11.84616 1.000 32.36025  ? 118 PHE   A CD1 1 
ATOM   801  C CD2 . PHE   A 1 111 ? 11.78243  -8.92408  -13.21831 1.000 29.40817  ? 118 PHE   A CD2 1 
ATOM   802  C CE1 . PHE   A 1 111 ? 10.59702  -7.89642  -10.94824 1.000 32.65153  ? 118 PHE   A CE1 1 
ATOM   803  C CE2 . PHE   A 1 111 ? 11.15446  -9.77247  -12.32252 1.000 27.87800  ? 118 PHE   A CE2 1 
ATOM   804  C CZ  . PHE   A 1 111 ? 10.56231  -9.25599  -11.18573 1.000 29.61445  ? 118 PHE   A CZ  1 
ATOM   805  N N   . MET   A 1 112 ? 15.48553  -6.57677  -13.00236 1.000 35.58935  ? 119 MET   A N   1 
ATOM   806  C CA  . MET   A 1 112 ? 16.51068  -7.21396  -12.18438 1.000 49.72080  ? 119 MET   A CA  1 
ATOM   807  C C   . MET   A 1 112 ? 17.34267  -6.19357  -11.41754 1.000 47.33471  ? 119 MET   A C   1 
ATOM   808  O O   . MET   A 1 112 ? 17.88066  -6.51177  -10.34919 1.000 45.47135  ? 119 MET   A O   1 
ATOM   809  C CB  . MET   A 1 112 ? 17.40118  -8.09429  -13.05774 1.000 55.04236  ? 119 MET   A CB  1 
ATOM   810  C CG  . MET   A 1 112 ? 16.94954  -9.54608  -13.10694 1.000 32.52028  ? 119 MET   A CG  1 
ATOM   811  S SD  . MET   A 1 112 ? 17.94305  -10.48646 -14.27462 1.000 75.94929  ? 119 MET   A SD  1 
ATOM   812  C CE  . MET   A 1 112 ? 16.77146  -11.72624 -14.80626 1.000 44.25552  ? 119 MET   A CE  1 
ATOM   813  N N   . GLU   A 1 113 ? 17.46861  -4.97315  -11.94176 1.000 40.74590  ? 120 GLU   A N   1 
ATOM   814  C CA  . GLU   A 1 113 ? 18.07107  -3.90259  -11.15543 1.000 53.01871  ? 120 GLU   A CA  1 
ATOM   815  C C   . GLU   A 1 113 ? 17.18054  -3.53244  -9.97867  1.000 54.50474  ? 120 GLU   A C   1 
ATOM   816  O O   . GLU   A 1 113 ? 17.67090  -3.27393  -8.87264  1.000 51.74136  ? 120 GLU   A O   1 
ATOM   817  C CB  . GLU   A 1 113 ? 18.32738  -2.67905  -12.03432 1.000 53.03076  ? 120 GLU   A CB  1 
ATOM   818  C CG  . GLU   A 1 113 ? 19.44106  -2.85767  -13.05099 1.000 70.44920  ? 120 GLU   A CG  1 
ATOM   819  C CD  . GLU   A 1 113 ? 19.51905  -1.70846  -14.04019 1.000 85.69162  ? 120 GLU   A CD  1 
ATOM   820  O OE1 . GLU   A 1 113 ? 18.90270  -0.65289  -13.78110 1.000 84.19260  ? 120 GLU   A OE1 1 
ATOM   821  O OE2 . GLU   A 1 113 ? 20.20327  -1.85919  -15.07502 1.000 92.08553  ? 120 GLU   A OE2 1 
ATOM   822  N N   . ALA   A 1 114 ? 15.86648  -3.50714  -10.20116 1.000 42.22036  ? 121 ALA   A N   1 
ATOM   823  C CA  . ALA   A 1 114 ? 14.93647  -3.19152  -9.12478  1.000 42.76401  ? 121 ALA   A CA  1 
ATOM   824  C C   . ALA   A 1 114 ? 14.96927  -4.25714  -8.03758  1.000 47.96023  ? 121 ALA   A C   1 
ATOM   825  O O   . ALA   A 1 114 ? 14.87368  -3.93951  -6.84619  1.000 50.12166  ? 121 ALA   A O   1 
ATOM   826  C CB  . ALA   A 1 114 ? 13.52525  -3.03603  -9.68825  1.000 39.89567  ? 121 ALA   A CB  1 
ATOM   827  N N   . LEU   A 1 115 ? 15.10796  -5.52874  -8.42804  1.000 41.05767  ? 122 LEU   A N   1 
ATOM   828  C CA  . LEU   A 1 115 ? 15.11393  -6.60758  -7.44376  1.000 42.70273  ? 122 LEU   A CA  1 
ATOM   829  C C   . LEU   A 1 115 ? 16.30395  -6.49092  -6.50284  1.000 59.84623  ? 122 LEU   A C   1 
ATOM   830  O O   . LEU   A 1 115 ? 16.17559  -6.71827  -5.29515  1.000 49.57789  ? 122 LEU   A O   1 
ATOM   831  C CB  . LEU   A 1 115 ? 15.12393  -7.96545  -8.14212  1.000 39.53485  ? 122 LEU   A CB  1 
ATOM   832  C CG  . LEU   A 1 115 ? 13.81695  -8.39279  -8.80639  1.000 34.62016  ? 122 LEU   A CG  1 
ATOM   833  C CD1 . LEU   A 1 115 ? 14.03698  -9.65696  -9.61723  1.000 34.31900  ? 122 LEU   A CD1 1 
ATOM   834  C CD2 . LEU   A 1 115 ? 12.72887  -8.59035  -7.76266  1.000 35.39507  ? 122 LEU   A CD2 1 
ATOM   835  N N   . GLN   A 1 116 ? 17.47046  -6.14285  -7.03275  1.000 52.32726  ? 123 GLN   A N   1 
ATOM   836  C CA  . GLN   A 1 116 ? 18.62822  -5.92449  -6.17901  1.000 61.74734  ? 123 GLN   A CA  1 
ATOM   837  C C   . GLN   A 1 116 ? 18.56950  -4.59112  -5.44072  1.000 61.57731  ? 123 GLN   A C   1 
ATOM   838  O O   . GLN   A 1 116 ? 19.51533  -4.26119  -4.71807  1.000 70.63157  ? 123 GLN   A O   1 
ATOM   839  C CB  . GLN   A 1 116 ? 19.91117  -6.01652  -7.01161  1.000 67.03857  ? 123 GLN   A CB  1 
ATOM   840  C CG  . GLN   A 1 116 ? 20.26188  -7.44182  -7.43806  1.000 69.60513  ? 123 GLN   A CG  1 
ATOM   841  C CD  . GLN   A 1 116 ? 21.71489  -7.80881  -7.17301  1.000 99.36948  ? 123 GLN   A CD  1 
ATOM   842  O OE1 . GLN   A 1 116 ? 22.47928  -7.01749  -6.62009  1.000 105.22751 ? 123 GLN   A OE1 1 
ATOM   843  N NE2 . GLN   A 1 116 ? 22.09959  -9.01960  -7.56629  1.000 88.26428  ? 123 GLN   A NE2 1 
ATOM   844  N N   . ALA   A 1 117 ? 17.48151  -3.82861  -5.58690  1.000 70.70836  ? 124 ALA   A N   1 
ATOM   845  C CA  . ALA   A 1 117 ? 17.35748  -2.49832  -5.00079  1.000 65.70277  ? 124 ALA   A CA  1 
ATOM   846  C C   . ALA   A 1 117 ? 16.05866  -2.33620  -4.21254  1.000 76.41304  ? 124 ALA   A C   1 
ATOM   847  O O   . ALA   A 1 117 ? 15.52049  -1.23107  -4.11003  1.000 68.87519  ? 124 ALA   A O   1 
ATOM   848  C CB  . ALA   A 1 117 ? 17.46494  -1.42627  -6.08457  1.000 59.10892  ? 124 ALA   A CB  1 
ATOM   849  N N   . GLY   A 1 118 ? 15.53931  -3.43072  -3.65536  1.000 62.74628  ? 125 GLY   A N   1 
ATOM   850  C CA  . GLY   A 1 118 ? 14.38631  -3.39613  -2.78029  1.000 66.28062  ? 125 GLY   A CA  1 
ATOM   851  C C   . GLY   A 1 118 ? 13.15950  -4.11773  -3.30289  1.000 54.81666  ? 125 GLY   A C   1 
ATOM   852  O O   . GLY   A 1 118 ? 12.35841  -4.60520  -2.49548  1.000 51.56202  ? 125 GLY   A O   1 
ATOM   853  N N   . ALA   A 1 119 ? 12.99120  -4.21146  -4.62009  1.000 48.21944  ? 126 ALA   A N   1 
ATOM   854  C CA  . ALA   A 1 119 ? 11.75549  -4.72969  -5.19024  1.000 44.79736  ? 126 ALA   A CA  1 
ATOM   855  C C   . ALA   A 1 119 ? 11.62957  -6.23675  -4.96492  1.000 40.92257  ? 126 ALA   A C   1 
ATOM   856  O O   . ALA   A 1 119 ? 12.58530  -6.92873  -4.60560  1.000 44.65606  ? 126 ALA   A O   1 
ATOM   857  C CB  . ALA   A 1 119 ? 11.68652  -4.41930  -6.68541  1.000 40.85351  ? 126 ALA   A CB  1 
ATOM   858  N N   . ASP   A 1 120 ? 10.41860  -6.74580  -5.19075  1.000 43.39770  ? 127 ASP   A N   1 
ATOM   859  C CA  . ASP   A 1 120 ? 10.15602  -8.17633  -5.17685  1.000 37.54926  ? 127 ASP   A CA  1 
ATOM   860  C C   . ASP   A 1 120 ? 9.46359   -8.56411  -6.47439  1.000 32.53610  ? 127 ASP   A C   1 
ATOM   861  O O   . ASP   A 1 120 ? 9.10807   -7.71473  -7.29420  1.000 35.51761  ? 127 ASP   A O   1 
ATOM   862  C CB  . ASP   A 1 120 ? 9.30024   -8.59683  -3.97313  1.000 45.08714  ? 127 ASP   A CB  1 
ATOM   863  C CG  . ASP   A 1 120 ? 7.94120   -7.94123  -3.96840  1.000 49.20786  ? 127 ASP   A CG  1 
ATOM   864  O OD1 . ASP   A 1 120 ? 7.86910   -6.70894  -3.78546  1.000 66.70149  ? 127 ASP   A OD1 1 
ATOM   865  O OD2 . ASP   A 1 120 ? 6.94196   -8.66427  -4.15544  1.000 54.69090  ? 127 ASP   A OD2 1 
ATOM   866  N N   . ILE   A 1 121 ? 9.26028   -9.87303  -6.64155  1.000 30.89650  ? 128 ILE   A N   1 
ATOM   867  C CA  . ILE   A 1 121 ? 8.77141   -10.41457 -7.90769  1.000 31.92858  ? 128 ILE   A CA  1 
ATOM   868  C C   . ILE   A 1 121 ? 7.36170   -9.92224  -8.21896  1.000 29.67023  ? 128 ILE   A C   1 
ATOM   869  O O   . ILE   A 1 121 ? 6.97495   -9.82692  -9.39071  1.000 27.47354  ? 128 ILE   A O   1 
ATOM   870  C CB  . ILE   A 1 121 ? 8.87869   -11.95544 -7.86026  1.000 31.28972  ? 128 ILE   A CB  1 
ATOM   871  C CG1 . ILE   A 1 121 ? 10.35273  -12.36997 -7.98836  1.000 38.36143  ? 128 ILE   A CG1 1 
ATOM   872  C CG2 . ILE   A 1 121 ? 8.01824   -12.62817 -8.91944  1.000 29.16388  ? 128 ILE   A CG2 1 
ATOM   873  C CD1 . ILE   A 1 121 ? 10.61702  -13.83550 -7.71290  1.000 42.80195  ? 128 ILE   A CD1 1 
ATOM   874  N N   . SER   A 1 122 ? 6.58628   -9.55270  -7.19358  1.000 32.94530  ? 129 SER   A N   1 
ATOM   875  C CA  . SER   A 1 122 ? 5.21534   -9.10724  -7.43721  1.000 38.94850  ? 129 SER   A CA  1 
ATOM   876  C C   . SER   A 1 122 ? 5.14383   -7.84110  -8.28516  1.000 37.31854  ? 129 SER   A C   1 
ATOM   877  O O   . SER   A 1 122 ? 4.08614   -7.55405  -8.85466  1.000 35.29871  ? 129 SER   A O   1 
ATOM   878  C CB  . SER   A 1 122 ? 4.47847   -8.86651  -6.11743  1.000 30.74425  ? 129 SER   A CB  1 
ATOM   879  O OG  . SER   A 1 122 ? 4.90402   -7.66308  -5.50936  1.000 39.11353  ? 129 SER   A OG  1 
ATOM   880  N N   . MET   A 1 123 ? 6.22681   -7.07453  -8.38130  1.000 29.69338  ? 130 MET   A N   1 
ATOM   881  C CA  . MET   A 1 123 ? 6.22529   -5.85183  -9.17424  1.000 30.53361  ? 130 MET   A CA  1 
ATOM   882  C C   . MET   A 1 123 ? 6.67740   -6.07044  -10.61508 1.000 27.53037  ? 130 MET   A C   1 
ATOM   883  O O   . MET   A 1 123 ? 6.91854   -5.09135  -11.32930 1.000 27.37088  ? 130 MET   A O   1 
ATOM   884  C CB  . MET   A 1 123 ? 7.07265   -4.77807  -8.47627  1.000 37.95688  ? 130 MET   A CB  1 
ATOM   885  C CG  . MET   A 1 123 ? 6.90737   -4.80214  -6.94564  1.000 45.57183  ? 130 MET   A CG  1 
ATOM   886  S SD  . MET   A 1 123 ? 8.19986   -4.00459  -5.96917  1.000 49.39420  ? 130 MET   A SD  1 
ATOM   887  C CE  . MET   A 1 123 ? 8.25283   -2.39168  -6.74329  1.000 46.20650  ? 130 MET   A CE  1 
ATOM   888  N N   . ILE   A 1 124 ? 6.74275   -7.32966  -11.06201 1.000 25.39275  ? 131 ILE   A N   1 
ATOM   889  C CA  . ILE   A 1 124 ? 7.18327   -7.65855  -12.41893 1.000 23.86592  ? 131 ILE   A CA  1 
ATOM   890  C C   . ILE   A 1 124 ? 6.38151   -6.89834  -13.47484 1.000 22.81201  ? 131 ILE   A C   1 
ATOM   891  O O   . ILE   A 1 124 ? 6.91572   -6.51167  -14.51957 1.000 21.87063  ? 131 ILE   A O   1 
ATOM   892  C CB  . ILE   A 1 124 ? 7.09615   -9.18220  -12.63695 1.000 24.08037  ? 131 ILE   A CB  1 
ATOM   893  C CG1 . ILE   A 1 124 ? 7.66629   -9.56952  -14.00706 1.000 25.17164  ? 131 ILE   A CG1 1 
ATOM   894  C CG2 . ILE   A 1 124 ? 5.65623   -9.67042  -12.47129 1.000 21.41051  ? 131 ILE   A CG2 1 
ATOM   895  C CD1 . ILE   A 1 124 ? 7.86642   -11.06271 -14.18570 1.000 22.88000  ? 131 ILE   A CD1 1 
ATOM   896  N N   . GLY   A 1 125 ? 5.09005   -6.68005  -13.22829 1.000 25.13117  ? 132 GLY   A N   1 
ATOM   897  C CA  . GLY   A 1 125 ? 4.24018   -6.02042  -14.20536 1.000 28.87694  ? 132 GLY   A CA  1 
ATOM   898  C C   . GLY   A 1 125 ? 4.61768   -4.58194  -14.49410 1.000 33.26502  ? 132 GLY   A C   1 
ATOM   899  O O   . GLY   A 1 125 ? 4.33615   -4.08757  -15.59029 1.000 32.45305  ? 132 GLY   A O   1 
ATOM   900  N N   . GLN   A 1 126 ? 5.24867   -3.89616  -13.53923 1.000 26.59809  ? 133 GLN   A N   1 
ATOM   901  C CA  . GLN   A 1 126 ? 5.68965   -2.52766  -13.77589 1.000 28.61805  ? 133 GLN   A CA  1 
ATOM   902  C C   . GLN   A 1 126 ? 6.83148   -2.44423  -14.77734 1.000 29.03685  ? 133 GLN   A C   1 
ATOM   903  O O   . GLN   A 1 126 ? 7.20758   -1.33583  -15.17009 1.000 31.43721  ? 133 GLN   A O   1 
ATOM   904  C CB  . GLN   A 1 126 ? 6.11875   -1.87806  -12.46189 1.000 33.90708  ? 133 GLN   A CB  1 
ATOM   905  C CG  . GLN   A 1 126 ? 5.01529   -1.80017  -11.42581 1.000 35.80845  ? 133 GLN   A CG  1 
ATOM   906  C CD  . GLN   A 1 126 ? 5.52610   -1.32563  -10.08244 1.000 45.28906  ? 133 GLN   A CD  1 
ATOM   907  O OE1 . GLN   A 1 126 ? 6.37710   -0.43788  -10.00986 1.000 48.58919  ? 133 GLN   A OE1 1 
ATOM   908  N NE2 . GLN   A 1 126 ? 5.00739   -1.91331  -9.00806  1.000 52.08677  ? 133 GLN   A NE2 1 
ATOM   909  N N   . PHE   A 1 127 ? 7.39159   -3.57885  -15.18789 1.000 26.77757  ? 134 PHE   A N   1 
ATOM   910  C CA  . PHE   A 1 127 ? 8.50608   -3.61512  -16.12458 1.000 30.71346  ? 134 PHE   A CA  1 
ATOM   911  C C   . PHE   A 1 127 ? 8.11923   -4.25497  -17.45198 1.000 30.28257  ? 134 PHE   A C   1 
ATOM   912  O O   . PHE   A 1 127 ? 8.99502   -4.53755  -18.27710 1.000 30.69283  ? 134 PHE   A O   1 
ATOM   913  C CB  . PHE   A 1 127 ? 9.69029   -4.33996  -15.47923 1.000 25.23507  ? 134 PHE   A CB  1 
ATOM   914  C CG  . PHE   A 1 127 ? 10.08153  -3.75924  -14.14903 1.000 28.17639  ? 134 PHE   A CG  1 
ATOM   915  C CD1 . PHE   A 1 127 ? 10.85126  -2.61042  -14.08161 1.000 37.37417  ? 134 PHE   A CD1 1 
ATOM   916  C CD2 . PHE   A 1 127 ? 9.62391   -4.32218  -12.97013 1.000 30.46834  ? 134 PHE   A CD2 1 
ATOM   917  C CE1 . PHE   A 1 127 ? 11.19245  -2.05646  -12.85742 1.000 40.50206  ? 134 PHE   A CE1 1 
ATOM   918  C CE2 . PHE   A 1 127 ? 9.95932   -3.77618  -11.74403 1.000 33.50537  ? 134 PHE   A CE2 1 
ATOM   919  C CZ  . PHE   A 1 127 ? 10.74465  -2.63955  -11.68776 1.000 34.92643  ? 134 PHE   A CZ  1 
ATOM   920  N N   . GLY   A 1 128 ? 6.82717   -4.48747  -17.67448 1.000 27.08213  ? 135 GLY   A N   1 
ATOM   921  C CA  . GLY   A 1 128 ? 6.33776   -4.91740  -18.96539 1.000 28.81552  ? 135 GLY   A CA  1 
ATOM   922  C C   . GLY   A 1 128 ? 6.58367   -6.36519  -19.31636 1.000 26.04753  ? 135 GLY   A C   1 
ATOM   923  O O   . GLY   A 1 128 ? 6.37869   -6.73985  -20.47560 1.000 28.86784  ? 135 GLY   A O   1 
ATOM   924  N N   . VAL   A 1 129 ? 7.00412   -7.19418  -18.36067 1.000 20.93985  ? 136 VAL   A N   1 
ATOM   925  C CA  . VAL   A 1 129 ? 7.30285   -8.59654  -18.62778 1.000 19.64685  ? 136 VAL   A CA  1 
ATOM   926  C C   . VAL   A 1 129 ? 6.46791   -9.48108  -17.71122 1.000 20.40641  ? 136 VAL   A C   1 
ATOM   927  O O   . VAL   A 1 129 ? 6.88608   -10.58209 -17.34025 1.000 18.43386  ? 136 VAL   A O   1 
ATOM   928  C CB  . VAL   A 1 129 ? 8.80672   -8.88683  -18.46663 1.000 21.06258  ? 136 VAL   A CB  1 
ATOM   929  C CG1 . VAL   A 1 129 ? 9.58311   -8.24757  -19.60792 1.000 25.73116  ? 136 VAL   A CG1 1 
ATOM   930  C CG2 . VAL   A 1 129 ? 9.31448   -8.35891  -17.12999 1.000 23.72717  ? 136 VAL   A CG2 1 
ATOM   931  N N   . GLY   A 1 130 ? 5.27352   -9.00571  -17.35094 1.000 21.40329  ? 137 GLY   A N   1 
ATOM   932  C CA  . GLY   A 1 130 ? 4.41288   -9.74196  -16.44301 1.000 19.11588  ? 137 GLY   A CA  1 
ATOM   933  C C   . GLY   A 1 130 ? 3.95222   -11.08168 -16.97145 1.000 19.32311  ? 137 GLY   A C   1 
ATOM   934  O O   . GLY   A 1 130 ? 3.59860   -11.95715 -16.17400 1.000 20.55096  ? 137 GLY   A O   1 
ATOM   935  N N   . PHE   A 1 131 ? 3.96169   -11.26905 -18.29606 1.000 16.45906  ? 138 PHE   A N   1 
ATOM   936  C CA  . PHE   A 1 131 ? 3.56570   -12.55618 -18.85920 1.000 17.68865  ? 138 PHE   A CA  1 
ATOM   937  C C   . PHE   A 1 131 ? 4.38075   -13.69616 -18.26553 1.000 18.93155  ? 138 PHE   A C   1 
ATOM   938  O O   . PHE   A 1 131 ? 3.84207   -14.77002 -17.97681 1.000 17.07868  ? 138 PHE   A O   1 
ATOM   939  C CB  . PHE   A 1 131 ? 3.72758   -12.55971 -20.37947 1.000 19.54275  ? 138 PHE   A CB  1 
ATOM   940  C CG  . PHE   A 1 131 ? 3.73480   -13.94581 -20.97168 1.000 22.80599  ? 138 PHE   A CG  1 
ATOM   941  C CD1 . PHE   A 1 131 ? 2.54587   -14.63265 -21.16937 1.000 20.53967  ? 138 PHE   A CD1 1 
ATOM   942  C CD2 . PHE   A 1 131 ? 4.93136   -14.57537 -21.29820 1.000 17.51110  ? 138 PHE   A CD2 1 
ATOM   943  C CE1 . PHE   A 1 131 ? 2.54484   -15.91737 -21.70271 1.000 20.94063  ? 138 PHE   A CE1 1 
ATOM   944  C CE2 . PHE   A 1 131 ? 4.93723   -15.85935 -21.82579 1.000 18.80471  ? 138 PHE   A CE2 1 
ATOM   945  C CZ  . PHE   A 1 131 ? 3.74275   -16.52745 -22.03030 1.000 21.95637  ? 138 PHE   A CZ  1 
ATOM   946  N N   . TYR   A 1 132 ? 5.68751   -13.48391 -18.08472 1.000 17.17823  ? 139 TYR   A N   1 
ATOM   947  C CA  . TYR   A 1 132 ? 6.56226   -14.56798 -17.65366 1.000 18.39980  ? 139 TYR   A CA  1 
ATOM   948  C C   . TYR   A 1 132 ? 6.31542   -14.99103 -16.21416 1.000 21.18477  ? 139 TYR   A C   1 
ATOM   949  O O   . TYR   A 1 132 ? 6.83715   -16.03316 -15.80080 1.000 18.81415  ? 139 TYR   A O   1 
ATOM   950  C CB  . TYR   A 1 132 ? 8.02102   -14.16358 -17.85927 1.000 16.59683  ? 139 TYR   A CB  1 
ATOM   951  C CG  . TYR   A 1 132 ? 8.30950   -13.89738 -19.32222 1.000 17.85648  ? 139 TYR   A CG  1 
ATOM   952  C CD1 . TYR   A 1 132 ? 8.60840   -14.94128 -20.18991 1.000 19.41393  ? 139 TYR   A CD1 1 
ATOM   953  C CD2 . TYR   A 1 132 ? 8.23839   -12.60976 -19.84407 1.000 18.18960  ? 139 TYR   A CD2 1 
ATOM   954  C CE1 . TYR   A 1 132 ? 8.85839   -14.70742 -21.54825 1.000 18.85719  ? 139 TYR   A CE1 1 
ATOM   955  C CE2 . TYR   A 1 132 ? 8.48386   -12.36489 -21.19603 1.000 25.31751  ? 139 TYR   A CE2 1 
ATOM   956  C CZ  . TYR   A 1 132 ? 8.79062   -13.41439 -22.03903 1.000 25.60950  ? 139 TYR   A CZ  1 
ATOM   957  O OH  . TYR   A 1 132 ? 9.02990   -13.16554 -23.38057 1.000 23.20958  ? 139 TYR   A OH  1 
ATOM   958  N N   . SER   A 1 133 ? 5.52249   -14.22985 -15.45496 1.000 19.08076  ? 140 SER   A N   1 
ATOM   959  C CA  . SER   A 1 133 ? 5.09592   -14.68664 -14.13658 1.000 21.88869  ? 140 SER   A CA  1 
ATOM   960  C C   . SER   A 1 133 ? 4.22933   -15.93519 -14.21237 1.000 20.63290  ? 140 SER   A C   1 
ATOM   961  O O   . SER   A 1 133 ? 3.99607   -16.57366 -13.17894 1.000 16.74330  ? 140 SER   A O   1 
ATOM   962  C CB  . SER   A 1 133 ? 4.34072   -13.57263 -13.40317 1.000 19.62371  ? 140 SER   A CB  1 
ATOM   963  O OG  . SER   A 1 133 ? 3.03965   -13.39308 -13.93643 1.000 20.67311  ? 140 SER   A OG  1 
ATOM   964  N N   . ALA   A 1 134 ? 3.75084   -16.29873 -15.40503 1.000 19.06342  ? 141 ALA   A N   1 
ATOM   965  C CA  . ALA   A 1 134 ? 3.04712   -17.56550 -15.56849 1.000 19.52060  ? 141 ALA   A CA  1 
ATOM   966  C C   . ALA   A 1 134 ? 3.87754   -18.73637 -15.05864 1.000 17.13175  ? 141 ALA   A C   1 
ATOM   967  O O   . ALA   A 1 134 ? 3.32269   -19.71277 -14.54442 1.000 18.15764  ? 141 ALA   A O   1 
ATOM   968  C CB  . ALA   A 1 134 ? 2.68358   -17.77422 -17.04132 1.000 17.69772  ? 141 ALA   A CB  1 
ATOM   969  N N   . TYR   A 1 135 ? 5.20848   -18.64766 -15.16209 1.000 17.02686  ? 142 TYR   A N   1 
ATOM   970  C CA  . TYR   A 1 135 ? 6.06178   -19.75476 -14.74773 1.000 18.54874  ? 142 TYR   A CA  1 
ATOM   971  C C   . TYR   A 1 135 ? 6.24908   -19.83166 -13.23553 1.000 21.03361  ? 142 TYR   A C   1 
ATOM   972  O O   . TYR   A 1 135 ? 7.00733   -20.68527 -12.76560 1.000 19.38368  ? 142 TYR   A O   1 
ATOM   973  C CB  . TYR   A 1 135 ? 7.40988   -19.66810 -15.47498 1.000 15.87090  ? 142 TYR   A CB  1 
ATOM   974  C CG  . TYR   A 1 135 ? 7.22932   -19.97205 -16.94774 1.000 19.91842  ? 142 TYR   A CG  1 
ATOM   975  C CD1 . TYR   A 1 135 ? 7.29552   -21.27701 -17.42134 1.000 18.95003  ? 142 TYR   A CD1 1 
ATOM   976  C CD2 . TYR   A 1 135 ? 6.93048   -18.96101 -17.85184 1.000 19.78259  ? 142 TYR   A CD2 1 
ATOM   977  C CE1 . TYR   A 1 135 ? 7.09116   -21.56761 -18.76826 1.000 22.32847  ? 142 TYR   A CE1 1 
ATOM   978  C CE2 . TYR   A 1 135 ? 6.72884   -19.23751 -19.19985 1.000 17.05307  ? 142 TYR   A CE2 1 
ATOM   979  C CZ  . TYR   A 1 135 ? 6.80966   -20.53622 -19.64895 1.000 20.69977  ? 142 TYR   A CZ  1 
ATOM   980  O OH  . TYR   A 1 135 ? 6.61364   -20.80065 -20.98805 1.000 19.21191  ? 142 TYR   A OH  1 
ATOM   981  N N   . LEU   A 1 136 ? 5.56704   -18.97853 -12.46560 1.000 21.56744  ? 143 LEU   A N   1 
ATOM   982  C CA  . LEU   A 1 136 ? 5.46979   -19.19246 -11.02651 1.000 19.89521  ? 143 LEU   A CA  1 
ATOM   983  C C   . LEU   A 1 136 ? 4.63636   -20.42684 -10.71085 1.000 23.49376  ? 143 LEU   A C   1 
ATOM   984  O O   . LEU   A 1 136 ? 4.88124   -21.10353 -9.70609  1.000 21.00117  ? 143 LEU   A O   1 
ATOM   985  C CB  . LEU   A 1 136 ? 4.85004   -17.96522 -10.34946 1.000 20.95726  ? 143 LEU   A CB  1 
ATOM   986  C CG  . LEU   A 1 136 ? 5.66181   -16.66804 -10.31402 1.000 19.44440  ? 143 LEU   A CG  1 
ATOM   987  C CD1 . LEU   A 1 136 ? 4.80814   -15.52078 -9.78349  1.000 22.44269  ? 143 LEU   A CD1 1 
ATOM   988  C CD2 . LEU   A 1 136 ? 6.92875   -16.84375 -9.46666  1.000 21.07774  ? 143 LEU   A CD2 1 
ATOM   989  N N   . VAL   A 1 137 ? 3.64993   -20.73299 -11.55696 1.000 20.11969  ? 144 VAL   A N   1 
ATOM   990  C CA  . VAL   A 1 137 ? 2.71678   -21.82236 -11.29176 1.000 19.86822  ? 144 VAL   A CA  1 
ATOM   991  C C   . VAL   A 1 137 ? 2.65085   -22.85188 -12.40936 1.000 20.70354  ? 144 VAL   A C   1 
ATOM   992  O O   . VAL   A 1 137 ? 2.09826   -23.94644 -12.19719 1.000 23.82379  ? 144 VAL   A O   1 
ATOM   993  C CB  . VAL   A 1 137 ? 1.30076   -21.26751 -11.00573 1.000 20.34695  ? 144 VAL   A CB  1 
ATOM   994  C CG1 . VAL   A 1 137 ? 1.29941   -20.38928 -9.75803  1.000 22.35468  ? 144 VAL   A CG1 1 
ATOM   995  C CG2 . VAL   A 1 137 ? 0.76497   -20.50470 -12.21300 1.000 18.80325  ? 144 VAL   A CG2 1 
ATOM   996  N N   . ALA   A 1 138 ? 3.17294   -22.58024 -13.60130 1.000 23.55919  ? 145 ALA   A N   1 
ATOM   997  C CA  . ALA   A 1 138 ? 3.02658   -23.47504 -14.73974 1.000 20.22966  ? 145 ALA   A CA  1 
ATOM   998  C C   . ALA   A 1 138 ? 4.36387   -24.09916 -15.10824 1.000 18.66424  ? 145 ALA   A C   1 
ATOM   999  O O   . ALA   A 1 138 ? 5.38706   -23.41123 -15.17021 1.000 24.61474  ? 145 ALA   A O   1 
ATOM   1000 C CB  . ALA   A 1 138 ? 2.45696   -22.73405 -15.95496 1.000 16.43591  ? 145 ALA   A CB  1 
ATOM   1001 N N   . GLU   A 1 139 ? 4.34417   -25.40394 -15.36440 1.000 18.70739  ? 146 GLU   A N   1 
ATOM   1002 C CA  . GLU   A 1 139 ? 5.51348   -26.07561 -15.91993 1.000 25.23097  ? 146 GLU   A CA  1 
ATOM   1003 C C   . GLU   A 1 139 ? 5.60724   -25.90042 -17.42936 1.000 25.68570  ? 146 GLU   A C   1 
ATOM   1004 O O   . GLU   A 1 139 ? 6.69891   -26.01612 -17.99547 1.000 22.84065  ? 146 GLU   A O   1 
ATOM   1005 C CB  . GLU   A 1 139 ? 5.48204   -27.56200 -15.55187 1.000 26.15759  ? 146 GLU   A CB  1 
ATOM   1006 C CG  . GLU   A 1 139 ? 4.24494   -28.30131 -16.02575 1.000 38.83777  ? 146 GLU   A CG  1 
ATOM   1007 C CD  . GLU   A 1 139 ? 4.30060   -29.79077 -15.73000 1.000 68.05350  ? 146 GLU   A CD  1 
ATOM   1008 O OE1 . GLU   A 1 139 ? 3.63832   -30.56545 -16.45487 1.000 61.70515  ? 146 GLU   A OE1 1 
ATOM   1009 O OE2 . GLU   A 1 139 ? 4.99433   -30.18559 -14.76506 1.000 56.22300  ? 146 GLU   A OE2 1 
ATOM   1010 N N   . LYS   A 1 140 ? 4.49030   -25.61039 -18.08601 1.000 20.90388  ? 147 LYS   A N   1 
ATOM   1011 C CA  . LYS   A 1 140 ? 4.46465   -25.37668 -19.51884 1.000 22.83523  ? 147 LYS   A CA  1 
ATOM   1012 C C   . LYS   A 1 140 ? 3.37110   -24.35779 -19.78457 1.000 20.95097  ? 147 LYS   A C   1 
ATOM   1013 O O   . LYS   A 1 140 ? 2.34030   -24.36319 -19.10646 1.000 18.50430  ? 147 LYS   A O   1 
ATOM   1014 C CB  . LYS   A 1 140 ? 4.21433   -26.68321 -20.28322 1.000 21.75524  ? 147 LYS   A CB  1 
ATOM   1015 C CG  . LYS   A 1 140 ? 4.07413   -26.55133 -21.79373 1.000 24.94765  ? 147 LYS   A CG  1 
ATOM   1016 C CD  . LYS   A 1 140 ? 4.18662   -27.93767 -22.42131 1.000 27.61438  ? 147 LYS   A CD  1 
ATOM   1017 C CE  . LYS   A 1 140 ? 2.83297   -28.53124 -22.75812 1.000 39.94425  ? 147 LYS   A CE  1 
ATOM   1018 N NZ  . LYS   A 1 140 ? 2.71414   -28.90228 -24.19563 1.000 57.37241  ? 147 LYS   A NZ  1 
ATOM   1019 N N   . VAL   A 1 141 ? 3.61239   -23.46589 -20.74009 1.000 15.78183  ? 148 VAL   A N   1 
ATOM   1020 C CA  . VAL   A 1 141 ? 2.63300   -22.45475 -21.12759 1.000 15.08443  ? 148 VAL   A CA  1 
ATOM   1021 C C   . VAL   A 1 141 ? 2.44340   -22.52992 -22.63439 1.000 20.69419  ? 148 VAL   A C   1 
ATOM   1022 O O   . VAL   A 1 141 ? 3.42395   -22.50453 -23.38807 1.000 15.84290  ? 148 VAL   A O   1 
ATOM   1023 C CB  . VAL   A 1 141 ? 3.06706   -21.03490 -20.71451 1.000 17.29702  ? 148 VAL   A CB  1 
ATOM   1024 C CG1 . VAL   A 1 141 ? 2.04218   -20.00473 -21.20119 1.000 17.72456  ? 148 VAL   A CG1 1 
ATOM   1025 C CG2 . VAL   A 1 141 ? 3.25330   -20.93835 -19.19104 1.000 15.39709  ? 148 VAL   A CG2 1 
ATOM   1026 N N   . THR   A 1 142 ? 1.18766   -22.61649 -23.06874 1.000 19.08117  ? 149 THR   A N   1 
ATOM   1027 C CA  . THR   A 1 142 ? 0.82112   -22.53979 -24.47576 1.000 18.52738  ? 149 THR   A CA  1 
ATOM   1028 C C   . THR   A 1 142 ? 0.03747   -21.25317 -24.70961 1.000 19.17994  ? 149 THR   A C   1 
ATOM   1029 O O   . THR   A 1 142 ? -0.88112  -20.93424 -23.94802 1.000 19.71576  ? 149 THR   A O   1 
ATOM   1030 C CB  . THR   A 1 142 ? -0.01573  -23.75211 -24.89723 1.000 20.77037  ? 149 THR   A CB  1 
ATOM   1031 O OG1 . THR   A 1 142 ? 0.64311   -24.96251 -24.50166 1.000 25.19049  ? 149 THR   A OG1 1 
ATOM   1032 C CG2 . THR   A 1 142 ? -0.21903  -23.76249 -26.41559 1.000 22.50883  ? 149 THR   A CG2 1 
ATOM   1033 N N   . VAL   A 1 143 ? 0.40189   -20.51296 -25.75142 1.000 19.60292  ? 150 VAL   A N   1 
ATOM   1034 C CA  . VAL   A 1 143 ? -0.29653  -19.28655 -26.12233 1.000 16.83082  ? 150 VAL   A CA  1 
ATOM   1035 C C   . VAL   A 1 143 ? -0.85099  -19.46804 -27.52728 1.000 22.59546  ? 150 VAL   A C   1 
ATOM   1036 O O   . VAL   A 1 143 ? -0.08630  -19.64078 -28.48480 1.000 20.93473  ? 150 VAL   A O   1 
ATOM   1037 C CB  . VAL   A 1 143 ? 0.61878   -18.05358 -26.05160 1.000 15.91425  ? 150 VAL   A CB  1 
ATOM   1038 C CG1 . VAL   A 1 143 ? -0.13871  -16.79795 -26.51153 1.000 17.45613  ? 150 VAL   A CG1 1 
ATOM   1039 C CG2 . VAL   A 1 143 ? 1.16408   -17.87315 -24.63683 1.000 20.88396  ? 150 VAL   A CG2 1 
ATOM   1040 N N   . ILE   A 1 144 ? -2.17292  -19.44398 -27.64692 1.000 19.68640  ? 151 ILE   A N   1 
ATOM   1041 C CA  . ILE   A 1 144 ? -2.85256  -19.45514 -28.93782 1.000 15.48628  ? 151 ILE   A CA  1 
ATOM   1042 C C   . ILE   A 1 144 ? -3.31588  -18.03644 -29.21147 1.000 18.75162  ? 151 ILE   A C   1 
ATOM   1043 O O   . ILE   A 1 144 ? -3.89383  -17.38845 -28.33252 1.000 18.68637  ? 151 ILE   A O   1 
ATOM   1044 C CB  . ILE   A 1 144 ? -4.04811  -20.42751 -28.94241 1.000 21.18335  ? 151 ILE   A CB  1 
ATOM   1045 C CG1 . ILE   A 1 144 ? -3.71161  -21.73164 -28.21947 1.000 32.21277  ? 151 ILE   A CG1 1 
ATOM   1046 C CG2 . ILE   A 1 144 ? -4.52472  -20.68637 -30.37202 1.000 23.89482  ? 151 ILE   A CG2 1 
ATOM   1047 C CD1 . ILE   A 1 144 ? -2.79325  -22.62390 -28.98315 1.000 27.70828  ? 151 ILE   A CD1 1 
ATOM   1048 N N   . THR   A 1 145 ? -3.07993  -17.54224 -30.42419 1.000 17.45043  ? 152 THR   A N   1 
ATOM   1049 C CA  . THR   A 1 145 ? -3.40541  -16.14695 -30.66728 1.000 21.85306  ? 152 THR   A CA  1 
ATOM   1050 C C   . THR   A 1 145 ? -3.79608  -15.94158 -32.12246 1.000 23.83692  ? 152 THR   A C   1 
ATOM   1051 O O   . THR   A 1 145 ? -3.34476  -16.66248 -33.01599 1.000 20.67289  ? 152 THR   A O   1 
ATOM   1052 C CB  . THR   A 1 145 ? -2.23537  -15.23243 -30.26459 1.000 23.44280  ? 152 THR   A CB  1 
ATOM   1053 O OG1 . THR   A 1 145 ? -2.68247  -13.87155 -30.20900 1.000 20.25231  ? 152 THR   A OG1 1 
ATOM   1054 C CG2 . THR   A 1 145 ? -1.06709  -15.36076 -31.23877 1.000 21.95203  ? 152 THR   A CG2 1 
ATOM   1055 N N   . LYS   A 1 146 ? -4.65607  -14.94956 -32.34111 1.000 18.93156  ? 153 LYS   A N   1 
ATOM   1056 C CA  . LYS   A 1 146 ? -5.12002  -14.58022 -33.67422 1.000 22.03363  ? 153 LYS   A CA  1 
ATOM   1057 C C   . LYS   A 1 146 ? -5.24376  -13.06746 -33.73855 1.000 21.69742  ? 153 LYS   A C   1 
ATOM   1058 O O   . LYS   A 1 146 ? -6.04837  -12.47432 -33.01344 1.000 20.78163  ? 153 LYS   A O   1 
ATOM   1059 C CB  . LYS   A 1 146 ? -6.46132  -15.23978 -34.00438 1.000 21.36578  ? 153 LYS   A CB  1 
ATOM   1060 C CG  . LYS   A 1 146 ? -7.09648  -14.77472 -35.31810 1.000 23.71350  ? 153 LYS   A CG  1 
ATOM   1061 C CD  . LYS   A 1 146 ? -6.39852  -15.35101 -36.53897 1.000 21.67290  ? 153 LYS   A CD  1 
ATOM   1062 C CE  . LYS   A 1 146 ? -7.12833  -14.97063 -37.82960 1.000 23.57679  ? 153 LYS   A CE  1 
ATOM   1063 N NZ  . LYS   A 1 146 ? -7.07879  -13.50858 -38.11453 1.000 23.69186  ? 153 LYS   A NZ  1 
ATOM   1064 N N   . HIS   A 1 147 ? -4.44362  -12.45568 -34.59951 1.000 20.98720  ? 154 HIS   A N   1 
ATOM   1065 C CA  . HIS   A 1 147 ? -4.48080  -11.03058 -34.87988 1.000 22.31978  ? 154 HIS   A CA  1 
ATOM   1066 C C   . HIS   A 1 147 ? -5.18731  -10.81466 -36.21715 1.000 21.65402  ? 154 HIS   A C   1 
ATOM   1067 O O   . HIS   A 1 147 ? -5.12745  -11.66991 -37.10595 1.000 21.63259  ? 154 HIS   A O   1 
ATOM   1068 C CB  . HIS   A 1 147 ? -3.04794  -10.48148 -34.91030 1.000 24.02448  ? 154 HIS   A CB  1 
ATOM   1069 C CG  . HIS   A 1 147 ? -2.95290  -8.99087  -35.00725 1.000 19.90060  ? 154 HIS   A CG  1 
ATOM   1070 N ND1 . HIS   A 1 147 ? -3.19264  -8.30352  -36.17682 1.000 21.38861  ? 154 HIS   A ND1 1 
ATOM   1071 C CD2 . HIS   A 1 147 ? -2.60668  -8.05932  -34.08779 1.000 22.26637  ? 154 HIS   A CD2 1 
ATOM   1072 C CE1 . HIS   A 1 147 ? -3.01856  -7.01080  -35.97005 1.000 28.67538  ? 154 HIS   A CE1 1 
ATOM   1073 N NE2 . HIS   A 1 147 ? -2.66367  -6.83580  -34.70973 1.000 28.25359  ? 154 HIS   A NE2 1 
ATOM   1074 N N   . ASN   A 1 148 ? -5.87844  -9.67311  -36.35226 1.000 22.07840  ? 155 ASN   A N   1 
ATOM   1075 C CA  . ASN   A 1 148 ? -6.59234  -9.39741  -37.60194 1.000 24.67511  ? 155 ASN   A CA  1 
ATOM   1076 C C   . ASN   A 1 148 ? -5.68381  -9.49063  -38.82457 1.000 27.43010  ? 155 ASN   A C   1 
ATOM   1077 O O   . ASN   A 1 148 ? -6.14638  -9.84870  -39.91451 1.000 26.31093  ? 155 ASN   A O   1 
ATOM   1078 C CB  . ASN   A 1 148 ? -7.24787  -8.01197  -37.56613 1.000 25.04340  ? 155 ASN   A CB  1 
ATOM   1079 C CG  . ASN   A 1 148 ? -8.55902  -7.99551  -36.80329 1.000 31.00233  ? 155 ASN   A CG  1 
ATOM   1080 O OD1 . ASN   A 1 148 ? -9.22637  -9.02168  -36.66565 1.000 29.94269  ? 155 ASN   A OD1 1 
ATOM   1081 N ND2 . ASN   A 1 148 ? -8.95125  -6.81538  -36.32729 1.000 29.20645  ? 155 ASN   A ND2 1 
ATOM   1082 N N   . ASP   A 1 149 ? -4.39964  -9.16811  -38.67719 1.000 25.27252  ? 156 ASP   A N   1 
ATOM   1083 C CA  . ASP   A 1 149 ? -3.49274  -9.09224  -39.81718 1.000 31.53546  ? 156 ASP   A CA  1 
ATOM   1084 C C   . ASP   A 1 149 ? -2.68396  -10.36605 -40.03497 1.000 37.83322  ? 156 ASP   A C   1 
ATOM   1085 O O   . ASP   A 1 149 ? -1.75394  -10.35763 -40.84980 1.000 32.08848  ? 156 ASP   A O   1 
ATOM   1086 C CB  . ASP   A 1 149 ? -2.53104  -7.91111  -39.65861 1.000 30.66778  ? 156 ASP   A CB  1 
ATOM   1087 C CG  . ASP   A 1 149 ? -3.24425  -6.58172  -39.58931 1.000 40.40581  ? 156 ASP   A CG  1 
ATOM   1088 O OD1 . ASP   A 1 149 ? -4.40457  -6.50081  -40.04317 1.000 31.30143  ? 156 ASP   A OD1 1 
ATOM   1089 O OD2 . ASP   A 1 149 ? -2.64028  -5.61499  -39.08211 1.000 36.81074  ? 156 ASP   A OD2 1 
ATOM   1090 N N   . ASP   A 1 150 ? -3.00045  -11.45423 -39.33490 1.000 25.61398  ? 157 ASP   A N   1 
ATOM   1091 C CA  . ASP   A 1 150 ? -2.20859  -12.67261 -39.45428 1.000 25.20137  ? 157 ASP   A CA  1 
ATOM   1092 C C   . ASP   A 1 150 ? -3.09963  -13.88879 -39.21546 1.000 34.59990  ? 157 ASP   A C   1 
ATOM   1093 O O   . ASP   A 1 150 ? -4.30383  -13.77046 -38.96476 1.000 30.50374  ? 157 ASP   A O   1 
ATOM   1094 C CB  . ASP   A 1 150 ? -1.02107  -12.64565 -38.48365 1.000 27.42426  ? 157 ASP   A CB  1 
ATOM   1095 C CG  . ASP   A 1 150 ? 0.17489   -13.42515 -38.99855 1.000 31.13727  ? 157 ASP   A CG  1 
ATOM   1096 O OD1 . ASP   A 1 150 ? 0.01584   -14.19012 -39.97265 1.000 29.68195  ? 157 ASP   A OD1 1 
ATOM   1097 O OD2 . ASP   A 1 150 ? 1.27832   -13.26945 -38.42828 1.000 30.91469  ? 157 ASP   A OD2 1 
ATOM   1098 N N   . GLU   A 1 151 ? -2.48981  -15.06851 -39.30143 1.000 26.01069  ? 158 GLU   A N   1 
ATOM   1099 C CA  . GLU   A 1 151 ? -3.17295  -16.33429 -39.08820 1.000 29.53075  ? 158 GLU   A CA  1 
ATOM   1100 C C   . GLU   A 1 151 ? -3.09908  -16.73257 -37.61319 1.000 23.64862  ? 158 GLU   A C   1 
ATOM   1101 O O   . GLU   A 1 151 ? -2.43026  -16.09176 -36.80138 1.000 23.89111  ? 158 GLU   A O   1 
ATOM   1102 C CB  . GLU   A 1 151 ? -2.55191  -17.42407 -39.96214 1.000 28.87175  ? 158 GLU   A CB  1 
ATOM   1103 C CG  . GLU   A 1 151 ? -2.71391  -17.18476 -41.45804 1.000 45.70808  ? 158 GLU   A CG  1 
ATOM   1104 C CD  . GLU   A 1 151 ? -4.16323  -17.13787 -41.90438 1.000 71.60187  ? 158 GLU   A CD  1 
ATOM   1105 O OE1 . GLU   A 1 151 ? -4.50594  -16.24813 -42.71203 1.000 84.72291  ? 158 GLU   A OE1 1 
ATOM   1106 O OE2 . GLU   A 1 151 ? -4.95879  -17.98820 -41.45218 1.000 82.95470  ? 158 GLU   A OE2 1 
ATOM   1107 N N   . GLN   A 1 152 ? -3.78903  -17.81884 -37.27113 1.000 22.27631  ? 159 GLN   A N   1 
ATOM   1108 C CA  . GLN   A 1 152 ? -3.79086  -18.31461 -35.89799 1.000 21.98370  ? 159 GLN   A CA  1 
ATOM   1109 C C   . GLN   A 1 152 ? -2.53872  -19.14586 -35.63574 1.000 22.25962  ? 159 GLN   A C   1 
ATOM   1110 O O   . GLN   A 1 152 ? -2.24010  -20.08593 -36.37806 1.000 25.14664  ? 159 GLN   A O   1 
ATOM   1111 C CB  . GLN   A 1 152 ? -5.04976  -19.14024 -35.63764 1.000 27.44876  ? 159 GLN   A CB  1 
ATOM   1112 C CG  . GLN   A 1 152 ? -5.30795  -19.46090 -34.16552 1.000 26.36192  ? 159 GLN   A CG  1 
ATOM   1113 C CD  . GLN   A 1 152 ? -6.74714  -19.89136 -33.91179 1.000 30.62885  ? 159 GLN   A CD  1 
ATOM   1114 O OE1 . GLN   A 1 152 ? -7.68451  -19.16611 -34.23340 1.000 30.85384  ? 159 GLN   A OE1 1 
ATOM   1115 N NE2 . GLN   A 1 152 ? -6.92492  -21.06528 -33.32385 1.000 26.88077  ? 159 GLN   A NE2 1 
ATOM   1116 N N   . TYR   A 1 153 ? -1.80550  -18.79303 -34.57876 1.000 18.89150  ? 160 TYR   A N   1 
ATOM   1117 C CA  . TYR   A 1 153 ? -0.54409  -19.43869 -34.24774 1.000 20.02521  ? 160 TYR   A CA  1 
ATOM   1118 C C   . TYR   A 1 153 ? -0.56624  -19.93956 -32.81010 1.000 23.27797  ? 160 TYR   A C   1 
ATOM   1119 O O   . TYR   A 1 153 ? -1.31726  -19.43651 -31.96974 1.000 19.78507  ? 160 TYR   A O   1 
ATOM   1120 C CB  . TYR   A 1 153 ? 0.63305   -18.48025 -34.44213 1.000 23.40929  ? 160 TYR   A CB  1 
ATOM   1121 C CG  . TYR   A 1 153 ? 1.01946   -18.30043 -35.88888 1.000 26.84207  ? 160 TYR   A CG  1 
ATOM   1122 C CD1 . TYR   A 1 153 ? 1.87989   -19.19657 -36.51067 1.000 25.92709  ? 160 TYR   A CD1 1 
ATOM   1123 C CD2 . TYR   A 1 153 ? 0.51195   -17.24854 -36.63929 1.000 28.78045  ? 160 TYR   A CD2 1 
ATOM   1124 C CE1 . TYR   A 1 153 ? 2.23179   -19.04729 -37.84008 1.000 28.34409  ? 160 TYR   A CE1 1 
ATOM   1125 C CE2 . TYR   A 1 153 ? 0.85537   -17.09188 -37.97824 1.000 29.32714  ? 160 TYR   A CE2 1 
ATOM   1126 C CZ  . TYR   A 1 153 ? 1.71683   -17.99451 -38.56770 1.000 32.64171  ? 160 TYR   A CZ  1 
ATOM   1127 O OH  . TYR   A 1 153 ? 2.07076   -17.84671 -39.88827 1.000 44.24250  ? 160 TYR   A OH  1 
ATOM   1128 N N   . ALA   A 1 154 ? 0.27254   -20.93920 -32.53809 1.000 18.24675  ? 161 ALA   A N   1 
ATOM   1129 C CA  . ALA   A 1 154 ? 0.45758   -21.48767 -31.19802 1.000 17.88473  ? 161 ALA   A CA  1 
ATOM   1130 C C   . ALA   A 1 154 ? 1.92085   -21.35257 -30.80200 1.000 20.41897  ? 161 ALA   A C   1 
ATOM   1131 O O   . ALA   A 1 154 ? 2.80466   -21.85301 -31.50574 1.000 22.33233  ? 161 ALA   A O   1 
ATOM   1132 C CB  . ALA   A 1 154 ? 0.02832   -22.95369 -31.13607 1.000 22.73723  ? 161 ALA   A CB  1 
ATOM   1133 N N   . TRP   A 1 155 ? 2.16512   -20.67908 -29.68166 1.000 17.89618  ? 162 TRP   A N   1 
ATOM   1134 C CA  . TRP   A 1 155 ? 3.48018   -20.55296 -29.06369 1.000 17.33273  ? 162 TRP   A CA  1 
ATOM   1135 C C   . TRP   A 1 155 ? 3.51300   -21.46947 -27.84635 1.000 18.45859  ? 162 TRP   A C   1 
ATOM   1136 O O   . TRP   A 1 155 ? 2.49347   -21.64274 -27.17242 1.000 20.01880  ? 162 TRP   A O   1 
ATOM   1137 C CB  . TRP   A 1 155 ? 3.71649   -19.08719 -28.67010 1.000 18.53154  ? 162 TRP   A CB  1 
ATOM   1138 C CG  . TRP   A 1 155 ? 4.96775   -18.71883 -27.89495 1.000 19.99550  ? 162 TRP   A CG  1 
ATOM   1139 C CD1 . TRP   A 1 155 ? 6.06648   -18.06573 -28.38649 1.000 15.00152  ? 162 TRP   A CD1 1 
ATOM   1140 C CD2 . TRP   A 1 155 ? 5.20572   -18.89488 -26.48603 1.000 21.17340  ? 162 TRP   A CD2 1 
ATOM   1141 N NE1 . TRP   A 1 155 ? 6.98605   -17.86069 -27.37948 1.000 18.91197  ? 162 TRP   A NE1 1 
ATOM   1142 C CE2 . TRP   A 1 155 ? 6.47861   -18.35623 -26.20598 1.000 23.95313  ? 162 TRP   A CE2 1 
ATOM   1143 C CE3 . TRP   A 1 155 ? 4.47042   -19.46445 -25.43889 1.000 16.58133  ? 162 TRP   A CE3 1 
ATOM   1144 C CZ2 . TRP   A 1 155 ? 7.03587   -18.37983 -24.92688 1.000 22.67683  ? 162 TRP   A CZ2 1 
ATOM   1145 C CZ3 . TRP   A 1 155 ? 5.02876   -19.48650 -24.16993 1.000 17.39250  ? 162 TRP   A CZ3 1 
ATOM   1146 C CH2 . TRP   A 1 155 ? 6.29759   -18.94238 -23.92601 1.000 18.70558  ? 162 TRP   A CH2 1 
ATOM   1147 N N   . GLU   A 1 156 ? 4.66575   -22.08415 -27.57479 1.000 17.55386  ? 163 GLU   A N   1 
ATOM   1148 C CA  . GLU   A 1 156 ? 4.71938   -22.98669 -26.43346 1.000 15.11935  ? 163 GLU   A CA  1 
ATOM   1149 C C   . GLU   A 1 156 ? 6.12841   -23.03945 -25.85716 1.000 17.34118  ? 163 GLU   A C   1 
ATOM   1150 O O   . GLU   A 1 156 ? 7.11029   -23.00246 -26.60066 1.000 16.76254  ? 163 GLU   A O   1 
ATOM   1151 C CB  . GLU   A 1 156 ? 4.24514   -24.38696 -26.83473 1.000 23.29788  ? 163 GLU   A CB  1 
ATOM   1152 C CG  . GLU   A 1 156 ? 4.09369   -25.35276 -25.67921 1.000 25.71549  ? 163 GLU   A CG  1 
ATOM   1153 C CD  . GLU   A 1 156 ? 3.38592   -26.62823 -26.09707 1.000 52.13917  ? 163 GLU   A CD  1 
ATOM   1154 O OE1 . GLU   A 1 156 ? 2.16941   -26.75211 -25.82884 1.000 39.57379  ? 163 GLU   A OE1 1 
ATOM   1155 O OE2 . GLU   A 1 156 ? 4.04572   -27.50256 -26.69948 1.000 43.81139  ? 163 GLU   A OE2 1 
ATOM   1156 N N   . SER   A 1 157 ? 6.22210   -23.12233 -24.52790 1.000 20.11036  ? 164 SER   A N   1 
ATOM   1157 C CA  . SER   A 1 157 ? 7.52291   -23.27296 -23.89129 1.000 18.74927  ? 164 SER   A CA  1 
ATOM   1158 C C   . SER   A 1 157 ? 7.37891   -23.90967 -22.51782 1.000 18.85692  ? 164 SER   A C   1 
ATOM   1159 O O   . SER   A 1 157 ? 6.50448   -23.53006 -21.73113 1.000 18.68745  ? 164 SER   A O   1 
ATOM   1160 C CB  . SER   A 1 157 ? 8.24884   -21.93121 -23.75117 1.000 16.71270  ? 164 SER   A CB  1 
ATOM   1161 O OG  . SER   A 1 157 ? 9.52453   -22.12566 -23.15209 1.000 20.41085  ? 164 SER   A OG  1 
ATOM   1162 N N   . SER   A 1 158 ? 8.25935   -24.87090 -22.23812 1.000 20.72613  ? 165 SER   A N   1 
ATOM   1163 C CA  . SER   A 1 158 ? 8.47701   -25.38780 -20.89229 1.000 20.77953  ? 165 SER   A CA  1 
ATOM   1164 C C   . SER   A 1 158 ? 9.73309   -24.79686 -20.26090 1.000 22.77989  ? 165 SER   A C   1 
ATOM   1165 O O   . SER   A 1 158 ? 10.38042  -25.44820 -19.42995 1.000 22.11070  ? 165 SER   A O   1 
ATOM   1166 C CB  . SER   A 1 158 ? 8.56362   -26.91170 -20.92353 1.000 21.73200  ? 165 SER   A CB  1 
ATOM   1167 O OG  . SER   A 1 158 ? 7.34241   -27.47003 -21.37625 1.000 27.59067  ? 165 SER   A OG  1 
ATOM   1168 N N   . ALA   A 1 159 ? 10.09032  -23.57840 -20.65459 1.000 19.90223  ? 166 ALA   A N   1 
ATOM   1169 C CA  . ALA   A 1 159 ? 11.32663  -22.90061 -20.24317 1.000 22.54673  ? 166 ALA   A CA  1 
ATOM   1170 C C   . ALA   A 1 159 ? 12.50353  -23.72665 -20.77099 1.000 25.59340  ? 166 ALA   A C   1 
ATOM   1171 O O   . ALA   A 1 159 ? 12.41834  -24.32608 -21.85028 1.000 27.80135  ? 166 ALA   A O   1 
ATOM   1172 C CB  . ALA   A 1 159 ? 11.33335  -22.66438 -18.73910 1.000 24.24203  ? 166 ALA   A CB  1 
ATOM   1173 N N   . GLY   A 1 160 ? 13.61259  -23.76787 -20.03455 1.000 27.09513  ? 167 GLY   A N   1 
ATOM   1174 C CA  . GLY   A 1 160 ? 14.76880  -24.50286 -20.51535 1.000 25.58184  ? 167 GLY   A CA  1 
ATOM   1175 C C   . GLY   A 1 160 ? 15.46147  -23.89126 -21.71371 1.000 32.71552  ? 167 GLY   A C   1 
ATOM   1176 O O   . GLY   A 1 160 ? 16.26901  -24.56350 -22.36494 1.000 31.12209  ? 167 GLY   A O   1 
ATOM   1177 N N   . GLY   A 1 161 ? 15.15793  -22.63788 -22.04025 1.000 21.52767  ? 168 GLY   A N   1 
ATOM   1178 C CA  . GLY   A 1 161 ? 15.91299  -21.90223 -23.03091 1.000 23.77181  ? 168 GLY   A CA  1 
ATOM   1179 C C   . GLY   A 1 161 ? 15.34011  -21.88679 -24.43181 1.000 23.96631  ? 168 GLY   A C   1 
ATOM   1180 O O   . GLY   A 1 161 ? 15.93453  -21.25195 -25.31254 1.000 20.64188  ? 168 GLY   A O   1 
ATOM   1181 N N   . SER   A 1 162 ? 14.20748  -22.54365 -24.67469 1.000 19.86474  ? 169 SER   A N   1 
ATOM   1182 C CA  . SER   A 1 162 ? 13.67318  -22.60835 -26.02782 1.000 19.15250  ? 169 SER   A CA  1 
ATOM   1183 C C   . SER   A 1 162 ? 12.15256  -22.50829 -26.01163 1.000 19.62895  ? 169 SER   A C   1 
ATOM   1184 O O   . SER   A 1 162 ? 11.49404  -22.77883 -25.00285 1.000 19.13951  ? 169 SER   A O   1 
ATOM   1185 C CB  . SER   A 1 162 ? 14.12122  -23.89765 -26.73865 1.000 23.88875  ? 169 SER   A CB  1 
ATOM   1186 O OG  . SER   A 1 162 ? 13.41010  -25.02077 -26.25442 1.000 25.22470  ? 169 SER   A OG  1 
ATOM   1187 N N   . PHE   A 1 163 ? 11.60123  -22.10054 -27.15449 1.000 22.25904  ? 170 PHE   A N   1 
ATOM   1188 C CA  . PHE   A 1 163 ? 10.16161  -22.10019 -27.36936 1.000 16.92489  ? 170 PHE   A CA  1 
ATOM   1189 C C   . PHE   A 1 163 ? 9.88564   -22.52449 -28.80555 1.000 18.85884  ? 170 PHE   A C   1 
ATOM   1190 O O   . PHE   A 1 163 ? 10.76961  -22.49282 -29.66784 1.000 19.86148  ? 170 PHE   A O   1 
ATOM   1191 C CB  . PHE   A 1 163 ? 9.52884   -20.72491 -27.07139 1.000 18.38724  ? 170 PHE   A CB  1 
ATOM   1192 C CG  . PHE   A 1 163 ? 9.99973   -19.61582 -27.98202 1.000 18.55031  ? 170 PHE   A CG  1 
ATOM   1193 C CD1 . PHE   A 1 163 ? 11.13852  -18.88783 -27.67950 1.000 21.93795  ? 170 PHE   A CD1 1 
ATOM   1194 C CD2 . PHE   A 1 163 ? 9.28696   -19.28781 -29.12927 1.000 20.76580  ? 170 PHE   A CD2 1 
ATOM   1195 C CE1 . PHE   A 1 163 ? 11.56902  -17.85885 -28.50985 1.000 22.84530  ? 170 PHE   A CE1 1 
ATOM   1196 C CE2 . PHE   A 1 163 ? 9.71256   -18.26694 -29.96458 1.000 19.32650  ? 170 PHE   A CE2 1 
ATOM   1197 C CZ  . PHE   A 1 163 ? 10.85040  -17.54319 -29.65128 1.000 22.41776  ? 170 PHE   A CZ  1 
ATOM   1198 N N   . THR   A 1 164 ? 8.64848   -22.94655 -29.05520 1.000 17.66952  ? 171 THR   A N   1 
ATOM   1199 C CA  . THR   A 1 164 ? 8.24496   -23.36411 -30.38619 1.000 18.79169  ? 171 THR   A CA  1 
ATOM   1200 C C   . THR   A 1 164 ? 7.09251   -22.49684 -30.85979 1.000 18.07979  ? 171 THR   A C   1 
ATOM   1201 O O   . THR   A 1 164 ? 6.33810   -21.94197 -30.05470 1.000 17.00230  ? 171 THR   A O   1 
ATOM   1202 C CB  . THR   A 1 164 ? 7.83124   -24.84668 -30.43677 1.000 22.20429  ? 171 THR   A CB  1 
ATOM   1203 O OG1 . THR   A 1 164 ? 6.66824   -25.05389 -29.62586 1.000 21.48790  ? 171 THR   A OG1 1 
ATOM   1204 C CG2 . THR   A 1 164 ? 8.95973   -25.74738 -29.95209 1.000 22.83903  ? 171 THR   A CG2 1 
ATOM   1205 N N   . VAL   A 1 165 ? 6.98117   -22.37039 -32.17848 1.000 19.58541  ? 172 VAL   A N   1 
ATOM   1206 C CA  . VAL   A 1 165 ? 5.86783   -21.67893 -32.81055 1.000 20.32426  ? 172 VAL   A CA  1 
ATOM   1207 C C   . VAL   A 1 165 ? 5.39140   -22.54939 -33.96090 1.000 22.72283  ? 172 VAL   A C   1 
ATOM   1208 O O   . VAL   A 1 165 ? 6.20655   -23.03948 -34.75007 1.000 23.74472  ? 172 VAL   A O   1 
ATOM   1209 C CB  . VAL   A 1 165 ? 6.26221   -20.27489 -33.31457 1.000 23.63407  ? 172 VAL   A CB  1 
ATOM   1210 C CG1 . VAL   A 1 165 ? 5.11958   -19.65510 -34.11802 1.000 21.62423  ? 172 VAL   A CG1 1 
ATOM   1211 C CG2 . VAL   A 1 165 ? 6.66629   -19.36637 -32.15073 1.000 20.05069  ? 172 VAL   A CG2 1 
ATOM   1212 N N   . ARG   A 1 166 ? 4.08113   -22.75682 -34.04847 1.000 20.59044  ? 173 ARG   A N   1 
ATOM   1213 C CA  . ARG   A 1 166 ? 3.50692   -23.48034 -35.17401 1.000 23.25660  ? 173 ARG   A CA  1 
ATOM   1214 C C   . ARG   A 1 166 ? 2.16542   -22.86509 -35.53416 1.000 22.27027  ? 173 ARG   A C   1 
ATOM   1215 O O   . ARG   A 1 166 ? 1.54649   -22.15853 -34.73741 1.000 20.82470  ? 173 ARG   A O   1 
ATOM   1216 C CB  . ARG   A 1 166 ? 3.30787   -24.97443 -34.87709 1.000 27.32163  ? 173 ARG   A CB  1 
ATOM   1217 C CG  . ARG   A 1 166 ? 2.29852   -25.25772 -33.76815 1.000 33.46230  ? 173 ARG   A CG  1 
ATOM   1218 C CD  . ARG   A 1 166 ? 2.49122   -26.64869 -33.17732 1.000 42.23201  ? 173 ARG   A CD  1 
ATOM   1219 N NE  . ARG   A 1 166 ? 3.54664   -26.67716 -32.17058 1.000 39.87602  ? 173 ARG   A NE  1 
ATOM   1220 C CZ  . ARG   A 1 166 ? 4.06360   -27.78494 -31.65563 1.000 47.56391  ? 173 ARG   A CZ  1 
ATOM   1221 N NH1 . ARG   A 1 166 ? 3.64291   -28.98283 -32.02799 1.000 42.74039  ? 173 ARG   A NH1 1 
ATOM   1222 N NH2 . ARG   A 1 166 ? 5.03340   -27.68848 -30.75032 1.000 51.60093  ? 173 ARG   A NH2 1 
ATOM   1223 N N   . THR   A 1 167 ? 1.72836   -23.13867 -36.75629 1.000 24.09356  ? 174 THR   A N   1 
ATOM   1224 C CA  . THR   A 1 167 ? 0.36202   -22.82819 -37.14118 1.000 27.15682  ? 174 THR   A CA  1 
ATOM   1225 C C   . THR   A 1 167 ? -0.59545  -23.64828 -36.28716 1.000 32.50206  ? 174 THR   A C   1 
ATOM   1226 O O   . THR   A 1 167 ? -0.37710  -24.84122 -36.05426 1.000 32.93406  ? 174 THR   A O   1 
ATOM   1227 C CB  . THR   A 1 167 ? 0.15526   -23.12947 -38.62675 1.000 33.07815  ? 174 THR   A CB  1 
ATOM   1228 O OG1 . THR   A 1 167 ? 0.96842   -22.24342 -39.40537 1.000 39.90361  ? 174 THR   A OG1 1 
ATOM   1229 C CG2 . THR   A 1 167 ? -1.29966  -22.94696 -39.01311 1.000 41.47309  ? 174 THR   A CG2 1 
ATOM   1230 N N   . ASP   A 1 168 ? -1.64264  -23.00406 -35.79036 1.000 27.94569  ? 175 ASP   A N   1 
ATOM   1231 C CA  . ASP   A 1 168 ? -2.59646  -23.68153 -34.92416 1.000 34.34719  ? 175 ASP   A CA  1 
ATOM   1232 C C   . ASP   A 1 168 ? -3.75892  -24.21728 -35.74887 1.000 44.67251  ? 175 ASP   A C   1 
ATOM   1233 O O   . ASP   A 1 168 ? -4.37700  -23.47600 -36.51985 1.000 40.74113  ? 175 ASP   A O   1 
ATOM   1234 C CB  . ASP   A 1 168 ? -3.10058  -22.73805 -33.83131 1.000 30.50565  ? 175 ASP   A CB  1 
ATOM   1235 C CG  . ASP   A 1 168 ? -4.01478  -23.43078 -32.84064 1.000 46.96745  ? 175 ASP   A CG  1 
ATOM   1236 O OD1 . ASP   A 1 168 ? -3.61385  -24.47859 -32.28719 1.000 54.14815  ? 175 ASP   A OD1 1 
ATOM   1237 O OD2 . ASP   A 1 168 ? -5.13213  -22.92951 -32.61572 1.000 41.83776  ? 175 ASP   A OD2 1 
ATOM   1238 N N   . THR   A 1 169 ? -4.04483  -25.50599 -35.58603 1.000 53.54140  ? 176 THR   A N   1 
ATOM   1239 C CA  . THR   A 1 169 ? -5.14746  -26.15053 -36.27582 1.000 69.34639  ? 176 THR   A CA  1 
ATOM   1240 C C   . THR   A 1 169 ? -6.32200  -26.42640 -35.35182 1.000 66.25313  ? 176 THR   A C   1 
ATOM   1241 O O   . THR   A 1 169 ? -7.27444  -27.10345 -35.75626 1.000 64.54376  ? 176 THR   A O   1 
ATOM   1242 C CB  . THR   A 1 169 ? -4.67425  -27.44826 -36.91121 1.000 77.28228  ? 176 THR   A CB  1 
ATOM   1243 O OG1 . THR   A 1 169 ? -3.78621  -28.12430 -36.02124 1.000 61.93141  ? 176 THR   A OG1 1 
ATOM   1244 C CG2 . THR   A 1 169 ? -3.97465  -27.17719 -38.23736 1.000 48.25125  ? 176 THR   A CG2 1 
ATOM   1245 N N   . GLY   A 1 170 ? -6.27192  -25.92760 -34.11907 1.000 65.49602  ? 177 GLY   A N   1 
ATOM   1246 C CA  . GLY   A 1 170 ? -7.34205  -26.13280 -33.16286 1.000 62.43896  ? 177 GLY   A CA  1 
ATOM   1247 C C   . GLY   A 1 170 ? -8.57569  -25.31671 -33.48564 1.000 50.09352  ? 177 GLY   A C   1 
ATOM   1248 O O   . GLY   A 1 170 ? -8.75047  -24.87054 -34.62466 1.000 48.74523  ? 177 GLY   A O   1 
ATOM   1249 N N   . GLU   A 1 171 ? -9.44353  -25.12415 -32.50029 1.000 50.17762  ? 178 GLU   A N   1 
ATOM   1250 C CA  . GLU   A 1 171 ? -10.63842 -24.32119 -32.71778 1.000 45.03147  ? 178 GLU   A CA  1 
ATOM   1251 C C   . GLU   A 1 171 ? -10.24066 -22.91447 -33.15560 1.000 40.57583  ? 178 GLU   A C   1 
ATOM   1252 O O   . GLU   A 1 171 ? -9.36222  -22.30581 -32.53308 1.000 32.97725  ? 178 GLU   A O   1 
ATOM   1253 C CB  . GLU   A 1 171 ? -11.48383 -24.24287 -31.44595 1.000 46.69029  ? 178 GLU   A CB  1 
ATOM   1254 C CG  . GLU   A 1 171 ? -12.40498 -25.42273 -31.20093 1.000 50.61133  ? 178 GLU   A CG  1 
ATOM   1255 C CD  . GLU   A 1 171 ? -13.38410 -25.65223 -32.33414 1.000 50.18373  ? 178 GLU   A CD  1 
ATOM   1256 O OE1 . GLU   A 1 171 ? -13.30181 -26.71807 -32.97949 1.000 50.58654  ? 178 GLU   A OE1 1 
ATOM   1257 O OE2 . GLU   A 1 171 ? -14.22767 -24.76595 -32.58413 1.000 56.84279  ? 178 GLU   A OE2 1 
ATOM   1258 N N   . PRO   A 1 172 ? -10.82679 -22.38278 -34.22675 1.000 41.02381  ? 179 PRO   A N   1 
ATOM   1259 C CA  . PRO   A 1 172 ? -10.56257 -20.98426 -34.59217 1.000 45.93689  ? 179 PRO   A CA  1 
ATOM   1260 C C   . PRO   A 1 172 ? -11.10391 -20.03035 -33.53689 1.000 46.55626  ? 179 PRO   A C   1 
ATOM   1261 O O   . PRO   A 1 172 ? -12.20077 -20.21998 -33.00759 1.000 48.47412  ? 179 PRO   A O   1 
ATOM   1262 C CB  . PRO   A 1 172 ? -11.30091 -20.81268 -35.92480 1.000 43.88078  ? 179 PRO   A CB  1 
ATOM   1263 C CG  . PRO   A 1 172 ? -11.50572 -22.19021 -36.45387 1.000 48.00062  ? 179 PRO   A CG  1 
ATOM   1264 C CD  . PRO   A 1 172 ? -11.49938 -23.13963 -35.29647 1.000 48.40700  ? 179 PRO   A CD  1 
ATOM   1265 N N   . MET   A 1 173 ? -10.32853 -18.98618 -33.24110 1.000 33.08890  ? 180 MET   A N   1 
ATOM   1266 C CA  . MET   A 1 173 ? -10.68753 -18.06623 -32.16830 1.000 33.59500  ? 180 MET   A CA  1 
ATOM   1267 C C   . MET   A 1 173 ? -11.33450 -16.77349 -32.64014 1.000 38.76905  ? 180 MET   A C   1 
ATOM   1268 O O   . MET   A 1 173 ? -11.89172 -16.04638 -31.81053 1.000 44.13688  ? 180 MET   A O   1 
ATOM   1269 C CB  . MET   A 1 173 ? -9.46057  -17.67872 -31.34473 1.000 30.35186  ? 180 MET   A CB  1 
ATOM   1270 C CG  . MET   A 1 173 ? -8.51273  -18.79353 -31.00875 1.000 53.63119  ? 180 MET   A CG  1 
ATOM   1271 S SD  . MET   A 1 173 ? -7.05125  -18.05201 -30.27155 1.000 48.30037  ? 180 MET   A SD  1 
ATOM   1272 C CE  . MET   A 1 173 ? -7.76857  -16.70053 -29.35155 1.000 32.32141  ? 180 MET   A CE  1 
ATOM   1273 N N   . GLY   A 1 174 ? -11.24148 -16.44251 -33.92093 1.000 30.03457  ? 181 GLY   A N   1 
ATOM   1274 C CA  . GLY   A 1 174 ? -11.76875 -15.17411 -34.38596 1.000 31.34890  ? 181 GLY   A CA  1 
ATOM   1275 C C   . GLY   A 1 174 ? -10.77491 -14.04732 -34.20086 1.000 29.33374  ? 181 GLY   A C   1 
ATOM   1276 O O   . GLY   A 1 174 ? -10.27152 -13.48966 -35.18024 1.000 25.68186  ? 181 GLY   A O   1 
ATOM   1277 N N   . ARG   A 1 175 ? -10.48462 -13.70916 -32.94496 1.000 21.78193  ? 182 ARG   A N   1 
ATOM   1278 C CA  . ARG   A 1 175 ? -9.50035  -12.69034 -32.60518 1.000 23.45449  ? 182 ARG   A CA  1 
ATOM   1279 C C   . ARG   A 1 175 ? -9.24483  -12.74681 -31.10711 1.000 25.83761  ? 182 ARG   A C   1 
ATOM   1280 O O   . ARG   A 1 175 ? -10.19123 -12.85116 -30.32223 1.000 21.35561  ? 182 ARG   A O   1 
ATOM   1281 C CB  . ARG   A 1 175 ? -9.97740  -11.27978 -32.98956 1.000 20.59083  ? 182 ARG   A CB  1 
ATOM   1282 C CG  . ARG   A 1 175 ? -8.88916  -10.20433 -32.82480 1.000 22.09009  ? 182 ARG   A CG  1 
ATOM   1283 C CD  . ARG   A 1 175 ? -9.47957  -8.79957  -32.66381 1.000 20.66993  ? 182 ARG   A CD  1 
ATOM   1284 N NE  . ARG   A 1 175 ? -10.39706 -8.69889  -31.53130 1.000 20.71208  ? 182 ARG   A NE  1 
ATOM   1285 C CZ  . ARG   A 1 175 ? -11.71207 -8.54960  -31.63664 1.000 22.25690  ? 182 ARG   A CZ  1 
ATOM   1286 N NH1 . ARG   A 1 175 ? -12.31311 -8.49423  -32.81630 1.000 23.33824  ? 182 ARG   A NH1 1 
ATOM   1287 N NH2 . ARG   A 1 175 ? -12.44616 -8.45474  -30.53043 1.000 22.20183  ? 182 ARG   A NH2 1 
ATOM   1288 N N   . GLY   A 1 176 ? -7.97931  -12.66639 -30.71865 1.000 24.41406  ? 183 GLY   A N   1 
ATOM   1289 C CA  . GLY   A 1 176 ? -7.63584  -12.55437 -29.31927 1.000 21.70785  ? 183 GLY   A CA  1 
ATOM   1290 C C   . GLY   A 1 176 ? -6.48482  -13.46732 -28.96368 1.000 20.38710  ? 183 GLY   A C   1 
ATOM   1291 O O   . GLY   A 1 176 ? -5.71339  -13.89387 -29.82390 1.000 23.46034  ? 183 GLY   A O   1 
ATOM   1292 N N   . THR   A 1 177 ? -6.37227  -13.75172 -27.67009 1.000 18.06425  ? 184 THR   A N   1 
ATOM   1293 C CA  . THR   A 1 177 ? -5.27720  -14.55659 -27.14964 1.000 16.85191  ? 184 THR   A CA  1 
ATOM   1294 C C   . THR   A 1 177 ? -5.79796  -15.50822 -26.08732 1.000 28.52661  ? 184 THR   A C   1 
ATOM   1295 O O   . THR   A 1 177 ? -6.68699  -15.16018 -25.30108 1.000 20.95922  ? 184 THR   A O   1 
ATOM   1296 C CB  . THR   A 1 177 ? -4.15509  -13.66177 -26.59377 1.000 19.85356  ? 184 THR   A CB  1 
ATOM   1297 O OG1 . THR   A 1 177 ? -3.60314  -12.88675 -27.66955 1.000 21.92925  ? 184 THR   A OG1 1 
ATOM   1298 C CG2 . THR   A 1 177 ? -3.04284  -14.48578 -25.94538 1.000 21.06033  ? 184 THR   A CG2 1 
ATOM   1299 N N   . LYS   A 1 178 ? -5.24404  -16.71857 -26.09019 1.000 16.80942  ? 185 LYS   A N   1 
ATOM   1300 C CA  . LYS   A 1 178 ? -5.58046  -17.76205 -25.13049 1.000 17.25498  ? 185 LYS   A CA  1 
ATOM   1301 C C   . LYS   A 1 178 ? -4.28927  -18.23825 -24.48399 1.000 21.47128  ? 185 LYS   A C   1 
ATOM   1302 O O   . LYS   A 1 178 ? -3.41832  -18.76999 -25.17496 1.000 19.01572  ? 185 LYS   A O   1 
ATOM   1303 C CB  . LYS   A 1 178 ? -6.29936  -18.91225 -25.84491 1.000 22.87937  ? 185 LYS   A CB  1 
ATOM   1304 C CG  . LYS   A 1 178 ? -6.89889  -19.95985 -24.95853 1.000 40.80235  ? 185 LYS   A CG  1 
ATOM   1305 C CD  . LYS   A 1 178 ? -7.39485  -21.16217 -25.76371 1.000 40.01425  ? 185 LYS   A CD  1 
ATOM   1306 C CE  . LYS   A 1 178 ? -7.96842  -20.74275 -27.10927 1.000 48.70789  ? 185 LYS   A CE  1 
ATOM   1307 N NZ  . LYS   A 1 178 ? -8.30337  -21.92265 -27.96089 1.000 56.36227  ? 185 LYS   A NZ  1 
ATOM   1308 N N   . VAL   A 1 179 ? -4.15020  -18.03044 -23.17640 1.000 17.93007  ? 186 VAL   A N   1 
ATOM   1309 C CA  . VAL   A 1 179 ? -2.96479  -18.45972 -22.43439 1.000 15.15996  ? 186 VAL   A CA  1 
ATOM   1310 C C   . VAL   A 1 179 ? -3.34552  -19.70917 -21.64870 1.000 21.57716  ? 186 VAL   A C   1 
ATOM   1311 O O   . VAL   A 1 179 ? -4.17769  -19.65390 -20.73562 1.000 18.22379  ? 186 VAL   A O   1 
ATOM   1312 C CB  . VAL   A 1 179 ? -2.43094  -17.35750 -21.50604 1.000 18.20997  ? 186 VAL   A CB  1 
ATOM   1313 C CG1 . VAL   A 1 179 ? -1.20996  -17.85924 -20.72714 1.000 18.36906  ? 186 VAL   A CG1 1 
ATOM   1314 C CG2 . VAL   A 1 179 ? -2.06550  -16.11521 -22.29911 1.000 19.10320  ? 186 VAL   A CG2 1 
ATOM   1315 N N   . ILE   A 1 180 ? -2.74742  -20.84139 -22.00510 1.000 16.45791  ? 187 ILE   A N   1 
ATOM   1316 C CA  . ILE   A 1 180 ? -3.02868  -22.11603 -21.35699 1.000 17.22085  ? 187 ILE   A CA  1 
ATOM   1317 C C   . ILE   A 1 180 ? -1.88872  -22.42246 -20.40080 1.000 21.45879  ? 187 ILE   A C   1 
ATOM   1318 O O   . ILE   A 1 180 ? -0.74734  -22.62424 -20.83155 1.000 18.56067  ? 187 ILE   A O   1 
ATOM   1319 C CB  . ILE   A 1 180 ? -3.19832  -23.24830 -22.37801 1.000 18.03805  ? 187 ILE   A CB  1 
ATOM   1320 C CG1 . ILE   A 1 180 ? -4.27466  -22.88883 -23.40917 1.000 16.63125  ? 187 ILE   A CG1 1 
ATOM   1321 C CG2 . ILE   A 1 180 ? -3.52119  -24.55625 -21.66049 1.000 21.70311  ? 187 ILE   A CG2 1 
ATOM   1322 C CD1 . ILE   A 1 180 ? -4.22820  -23.76093 -24.64361 1.000 27.04583  ? 187 ILE   A CD1 1 
ATOM   1323 N N   . LEU   A 1 181 ? -2.19892  -22.46542 -19.10893 1.000 18.59585  ? 188 LEU   A N   1 
ATOM   1324 C CA  . LEU   A 1 181 ? -1.21394  -22.74049 -18.06895 1.000 20.08622  ? 188 LEU   A CA  1 
ATOM   1325 C C   . LEU   A 1 181 ? -1.29859  -24.21291 -17.68860 1.000 17.83579  ? 188 LEU   A C   1 
ATOM   1326 O O   . LEU   A 1 181 ? -2.29086  -24.65034 -17.09734 1.000 20.75199  ? 188 LEU   A O   1 
ATOM   1327 C CB  . LEU   A 1 181 ? -1.45283  -21.85258 -16.85098 1.000 19.45204  ? 188 LEU   A CB  1 
ATOM   1328 C CG  . LEU   A 1 181 ? -1.53387  -20.34864 -17.09939 1.000 24.09227  ? 188 LEU   A CG  1 
ATOM   1329 C CD1 . LEU   A 1 181 ? -1.79857  -19.63012 -15.78954 1.000 27.33796  ? 188 LEU   A CD1 1 
ATOM   1330 C CD2 . LEU   A 1 181 ? -0.25571  -19.84817 -17.73442 1.000 20.42636  ? 188 LEU   A CD2 1 
ATOM   1331 N N   . HIS   A 1 182 ? -0.25869  -24.97809 -18.02116 1.000 18.71504  ? 189 HIS   A N   1 
ATOM   1332 C CA  . HIS   A 1 182 ? -0.16029  -26.37002 -17.58539 1.000 18.71836  ? 189 HIS   A CA  1 
ATOM   1333 C C   . HIS   A 1 182 ? 0.47335   -26.35092 -16.19812 1.000 21.47587  ? 189 HIS   A C   1 
ATOM   1334 O O   . HIS   A 1 182 ? 1.69127   -26.20824 -16.05787 1.000 21.41608  ? 189 HIS   A O   1 
ATOM   1335 C CB  . HIS   A 1 182 ? 0.63286   -27.19925 -18.59055 1.000 20.26212  ? 189 HIS   A CB  1 
ATOM   1336 C CG  . HIS   A 1 182 ? 0.13953   -27.05894 -20.00142 1.000 23.64819  ? 189 HIS   A CG  1 
ATOM   1337 N ND1 . HIS   A 1 182 ? -0.61111  -28.02977 -20.63079 1.000 32.08389  ? 189 HIS   A ND1 1 
ATOM   1338 C CD2 . HIS   A 1 182 ? 0.27190   -26.04880 -20.89561 1.000 25.05208  ? 189 HIS   A CD2 1 
ATOM   1339 C CE1 . HIS   A 1 182 ? -0.90711  -27.62989 -21.85615 1.000 31.46686  ? 189 HIS   A CE1 1 
ATOM   1340 N NE2 . HIS   A 1 182 ? -0.38438  -26.43009 -22.04163 1.000 30.03723  ? 189 HIS   A NE2 1 
ATOM   1341 N N   . LEU   A 1 183 ? -0.36026  -26.49978 -15.17011 1.000 19.56543  ? 190 LEU   A N   1 
ATOM   1342 C CA  . LEU   A 1 183 ? 0.04504   -26.16867 -13.80696 1.000 19.02897  ? 190 LEU   A CA  1 
ATOM   1343 C C   . LEU   A 1 183 ? 0.98083   -27.21226 -13.21285 1.000 23.17376  ? 190 LEU   A C   1 
ATOM   1344 O O   . LEU   A 1 183 ? 0.86408   -28.41198 -13.48957 1.000 23.17859  ? 190 LEU   A O   1 
ATOM   1345 C CB  . LEU   A 1 183 ? -1.18599  -26.03239 -12.91045 1.000 17.69680  ? 190 LEU   A CB  1 
ATOM   1346 C CG  . LEU   A 1 183 ? -2.13403  -24.87111 -13.21699 1.000 18.84535  ? 190 LEU   A CG  1 
ATOM   1347 C CD1 . LEU   A 1 183 ? -3.28129  -24.87312 -12.21942 1.000 20.89517  ? 190 LEU   A CD1 1 
ATOM   1348 C CD2 . LEU   A 1 183 ? -1.39504  -23.55086 -13.17033 1.000 21.41396  ? 190 LEU   A CD2 1 
ATOM   1349 N N   . LYS   A 1 184 ? 1.90363   -26.74283 -12.37009 1.000 20.95258  ? 191 LYS   A N   1 
ATOM   1350 C CA  . LYS   A 1 184 ? 2.74208   -27.64122 -11.58871 1.000 28.17158  ? 191 LYS   A CA  1 
ATOM   1351 C C   . LYS   A 1 184 ? 1.88543   -28.48250 -10.64978 1.000 30.57611  ? 191 LYS   A C   1 
ATOM   1352 O O   . LYS   A 1 184 ? 0.80175   -28.07253 -10.22722 1.000 27.94324  ? 191 LYS   A O   1 
ATOM   1353 C CB  . LYS   A 1 184 ? 3.77304   -26.85457 -10.77441 1.000 32.45313  ? 191 LYS   A CB  1 
ATOM   1354 C CG  . LYS   A 1 184 ? 4.79353   -26.07246 -11.59185 1.000 33.72018  ? 191 LYS   A CG  1 
ATOM   1355 C CD  . LYS   A 1 184 ? 5.46234   -25.00667 -10.72280 1.000 38.07107  ? 191 LYS   A CD  1 
ATOM   1356 C CE  . LYS   A 1 184 ? 6.50256   -24.21265 -11.48966 1.000 40.72490  ? 191 LYS   A CE  1 
ATOM   1357 N NZ  . LYS   A 1 184 ? 7.20784   -23.21998 -10.61822 1.000 48.97427  ? 191 LYS   A NZ  1 
ATOM   1358 N N   . GLU   A 1 185 ? 2.40061   -29.66733 -10.30813 1.000 27.68849  ? 192 GLU   A N   1 
ATOM   1359 C CA  . GLU   A 1 185 ? 1.62751   -30.63237 -9.53171  1.000 35.22754  ? 192 GLU   A CA  1 
ATOM   1360 C C   . GLU   A 1 185 ? 1.17398   -30.06755 -8.19015  1.000 39.12873  ? 192 GLU   A C   1 
ATOM   1361 O O   . GLU   A 1 185 ? 0.11383   -30.45355 -7.68381  1.000 40.89562  ? 192 GLU   A O   1 
ATOM   1362 C CB  . GLU   A 1 185 ? 2.45393   -31.90277 -9.32128  1.000 43.45514  ? 192 GLU   A CB  1 
ATOM   1363 C CG  . GLU   A 1 185 ? 1.64437   -33.13024 -8.94795  1.000 64.52186  ? 192 GLU   A CG  1 
ATOM   1364 C CD  . GLU   A 1 185 ? 2.51989   -34.34769 -8.71518  1.000 84.40750  ? 192 GLU   A CD  1 
ATOM   1365 O OE1 . GLU   A 1 185 ? 2.00946   -35.48255 -8.82552  1.000 91.65650  ? 192 GLU   A OE1 1 
ATOM   1366 O OE2 . GLU   A 1 185 ? 3.72338   -34.16773 -8.43131  1.000 85.19165  ? 192 GLU   A OE2 1 
ATOM   1367 N N   . ASP   A 1 186 ? 1.94645   -29.15590 -7.60234  1.000 32.02748  ? 193 ASP   A N   1 
ATOM   1368 C CA  . ASP   A 1 186 ? 1.64158   -28.61750 -6.28416  1.000 35.12783  ? 193 ASP   A CA  1 
ATOM   1369 C C   . ASP   A 1 186 ? 0.96813   -27.25081 -6.34411  1.000 30.28344  ? 193 ASP   A C   1 
ATOM   1370 O O   . ASP   A 1 186 ? 0.84462   -26.58655 -5.31080  1.000 29.46100  ? 193 ASP   A O   1 
ATOM   1371 C CB  . ASP   A 1 186 ? 2.91738   -28.54968 -5.43943  1.000 42.60982  ? 193 ASP   A CB  1 
ATOM   1372 C CG  . ASP   A 1 186 ? 3.96542   -27.63098 -6.03510  1.000 48.08958  ? 193 ASP   A CG  1 
ATOM   1373 O OD1 . ASP   A 1 186 ? 4.00512   -27.49402 -7.27546  1.000 55.37756  ? 193 ASP   A OD1 1 
ATOM   1374 O OD2 . ASP   A 1 186 ? 4.76456   -27.05918 -5.26259  1.000 64.10126  ? 193 ASP   A OD2 1 
ATOM   1375 N N   . GLN   A 1 187 ? 0.51027   -26.82699 -7.52294  1.000 23.49271  ? 194 GLN   A N   1 
ATOM   1376 C CA  . GLN   A 1 187 ? -0.13350  -25.53291 -7.71080  1.000 22.22298  ? 194 GLN   A CA  1 
ATOM   1377 C C   . GLN   A 1 187 ? -1.58971  -25.67676 -8.15015  1.000 23.18204  ? 194 GLN   A C   1 
ATOM   1378 O O   . GLN   A 1 187 ? -2.14619  -24.77770 -8.78118  1.000 22.98849  ? 194 GLN   A O   1 
ATOM   1379 C CB  . GLN   A 1 187 ? 0.65312   -24.69358 -8.72075  1.000 21.78053  ? 194 GLN   A CB  1 
ATOM   1380 C CG  . GLN   A 1 187 ? 2.10414   -24.43392 -8.29829  1.000 22.53995  ? 194 GLN   A CG  1 
ATOM   1381 C CD  . GLN   A 1 187 ? 2.20166   -23.72693 -6.95658  1.000 28.00216  ? 194 GLN   A CD  1 
ATOM   1382 O OE1 . GLN   A 1 187 ? 1.39098   -22.85801 -6.64500  1.000 28.01919  ? 194 GLN   A OE1 1 
ATOM   1383 N NE2 . GLN   A 1 187 ? 3.19776   -24.09791 -6.15630  1.000 34.24390  ? 194 GLN   A NE2 1 
ATOM   1384 N N   . THR   A 1 188 ? -2.22622  -26.79667 -7.81966  1.000 26.75177  ? 195 THR   A N   1 
ATOM   1385 C CA  . THR   A 1 188 ? -3.58273  -27.03285 -8.30147  1.000 33.12084  ? 195 THR   A CA  1 
ATOM   1386 C C   . THR   A 1 188 ? -4.63656  -26.23272 -7.54692  1.000 28.15879  ? 195 THR   A C   1 
ATOM   1387 O O   . THR   A 1 188 ? -5.81443  -26.29424 -7.91851  1.000 30.17330  ? 195 THR   A O   1 
ATOM   1388 C CB  . THR   A 1 188 ? -3.92342  -28.52418 -8.23192  1.000 32.10543  ? 195 THR   A CB  1 
ATOM   1389 O OG1 . THR   A 1 188 ? -3.77283  -28.98972 -6.88440  1.000 35.36614  ? 195 THR   A OG1 1 
ATOM   1390 C CG2 . THR   A 1 188 ? -3.01167  -29.32627 -9.16176  1.000 29.38183  ? 195 THR   A CG2 1 
ATOM   1391 N N   . GLU   A 1 189 ? -4.25459  -25.48578 -6.50649  1.000 25.26378  ? 196 GLU   A N   1 
ATOM   1392 C CA  . GLU   A 1 189 ? -5.22361  -24.61880 -5.84011  1.000 28.45270  ? 196 GLU   A CA  1 
ATOM   1393 C C   . GLU   A 1 189 ? -5.80582  -23.59083 -6.80112  1.000 28.13461  ? 196 GLU   A C   1 
ATOM   1394 O O   . GLU   A 1 189 ? -6.93378  -23.12482 -6.60615  1.000 22.40180  ? 196 GLU   A O   1 
ATOM   1395 C CB  . GLU   A 1 189 ? -4.57509  -23.91829 -4.64538  1.000 26.56331  ? 196 GLU   A CB  1 
ATOM   1396 C CG  . GLU   A 1 189 ? -3.62087  -22.79909 -5.02836  1.000 25.58726  ? 196 GLU   A CG  1 
ATOM   1397 C CD  . GLU   A 1 189 ? -2.79548  -22.30600 -3.85687  1.000 38.32477  ? 196 GLU   A CD  1 
ATOM   1398 O OE1 . GLU   A 1 189 ? -1.82922  -22.99941 -3.47443  1.000 35.51627  ? 196 GLU   A OE1 1 
ATOM   1399 O OE2 . GLU   A 1 189 ? -3.11819  -21.22482 -3.31901  1.000 31.14952  ? 196 GLU   A OE2 1 
ATOM   1400 N N   . TYR   A 1 190 ? -5.06479  -23.23635 -7.84643  1.000 23.63262  ? 197 TYR   A N   1 
ATOM   1401 C CA  . TYR   A 1 190 ? -5.51452  -22.23443 -8.80203  1.000 22.34129  ? 197 TYR   A CA  1 
ATOM   1402 C C   . TYR   A 1 190 ? -6.49789  -22.79659 -9.82126  1.000 25.24034  ? 197 TYR   A C   1 
ATOM   1403 O O   . TYR   A 1 190 ? -6.87357  -22.08871 -10.75911 1.000 26.10219  ? 197 TYR   A O   1 
ATOM   1404 C CB  . TYR   A 1 190 ? -4.29714  -21.59734 -9.48072  1.000 20.68934  ? 197 TYR   A CB  1 
ATOM   1405 C CG  . TYR   A 1 190 ? -3.38956  -20.96364 -8.45160  1.000 21.45609  ? 197 TYR   A CG  1 
ATOM   1406 C CD1 . TYR   A 1 190 ? -3.80310  -19.84508 -7.73667  1.000 21.51010  ? 197 TYR   A CD1 1 
ATOM   1407 C CD2 . TYR   A 1 190 ? -2.14742  -21.51393 -8.14830  1.000 19.31673  ? 197 TYR   A CD2 1 
ATOM   1408 C CE1 . TYR   A 1 190 ? -2.99096  -19.27064 -6.76805  1.000 22.35607  ? 197 TYR   A CE1 1 
ATOM   1409 C CE2 . TYR   A 1 190 ? -1.33046  -20.94701 -7.18144  1.000 22.02884  ? 197 TYR   A CE2 1 
ATOM   1410 C CZ  . TYR   A 1 190 ? -1.76060  -19.82201 -6.49361  1.000 19.29342  ? 197 TYR   A CZ  1 
ATOM   1411 O OH  . TYR   A 1 190 ? -0.96232  -19.25268 -5.52941  1.000 23.49505  ? 197 TYR   A OH  1 
ATOM   1412 N N   . LEU   A 1 191 ? -6.92491  -24.04742 -9.65010  1.000 20.55906  ? 198 LEU   A N   1 
ATOM   1413 C CA  . LEU   A 1 191 ? -8.06780  -24.59202 -10.36570 1.000 21.43040  ? 198 LEU   A CA  1 
ATOM   1414 C C   . LEU   A 1 191 ? -9.34185  -24.55799 -9.53948  1.000 26.75090  ? 198 LEU   A C   1 
ATOM   1415 O O   . LEU   A 1 191 ? -10.40662 -24.91061 -10.05790 1.000 28.38290  ? 198 LEU   A O   1 
ATOM   1416 C CB  . LEU   A 1 191 ? -7.79691  -26.04022 -10.79576 1.000 23.75058  ? 198 LEU   A CB  1 
ATOM   1417 C CG  . LEU   A 1 191 ? -6.57713  -26.24260 -11.69553 1.000 24.26701  ? 198 LEU   A CG  1 
ATOM   1418 C CD1 . LEU   A 1 191 ? -6.32880  -27.72232 -11.94920 1.000 28.26613  ? 198 LEU   A CD1 1 
ATOM   1419 C CD2 . LEU   A 1 191 ? -6.77198  -25.49638 -12.99815 1.000 29.00447  ? 198 LEU   A CD2 1 
ATOM   1420 N N   . GLU   A 1 192 ? -9.25678  -24.16831 -8.27033  1.000 23.09572  ? 199 GLU   A N   1 
ATOM   1421 C CA  . GLU   A 1 192 ? -10.40614 -24.18698 -7.37462  1.000 25.97947  ? 199 GLU   A CA  1 
ATOM   1422 C C   . GLU   A 1 192 ? -11.18953 -22.89165 -7.52259  1.000 27.89787  ? 199 GLU   A C   1 
ATOM   1423 O O   . GLU   A 1 192 ? -10.61102 -21.79771 -7.49789  1.000 22.97953  ? 199 GLU   A O   1 
ATOM   1424 C CB  . GLU   A 1 192 ? -9.96534  -24.37251 -5.92282  1.000 31.86577  ? 199 GLU   A CB  1 
ATOM   1425 C CG  . GLU   A 1 192 ? -9.24425  -25.67740 -5.65786  1.000 36.96619  ? 199 GLU   A CG  1 
ATOM   1426 C CD  . GLU   A 1 192 ? -9.17793  -26.00688 -4.18306  1.000 72.89508  ? 199 GLU   A CD  1 
ATOM   1427 O OE1 . GLU   A 1 192 ? -10.24834 -26.11936 -3.54614  1.000 91.09625  ? 199 GLU   A OE1 1 
ATOM   1428 O OE2 . GLU   A 1 192 ? -8.05352  -26.14486 -3.65947  1.000 79.60249  ? 199 GLU   A OE2 1 
ATOM   1429 N N   . GLU   A 1 193 ? -12.50806 -23.02741 -7.66091  1.000 25.40390  ? 200 GLU   A N   1 
ATOM   1430 C CA  . GLU   A 1 193 ? -13.36199 -21.87711 -7.92769  1.000 25.57593  ? 200 GLU   A CA  1 
ATOM   1431 C C   . GLU   A 1 193 ? -13.20191 -20.79526 -6.85567  1.000 20.91557  ? 200 GLU   A C   1 
ATOM   1432 O O   . GLU   A 1 193 ? -13.00030 -19.61950 -7.17497  1.000 24.79345  ? 200 GLU   A O   1 
ATOM   1433 C CB  . GLU   A 1 193 ? -14.81612 -22.34149 -8.03228  1.000 28.52178  ? 200 GLU   A CB  1 
ATOM   1434 C CG  . GLU   A 1 193 ? -15.81678 -21.23509 -7.84863  1.000 43.35007  ? 200 GLU   A CG  1 
ATOM   1435 C CD  . GLU   A 1 193 ? -17.21453 -21.59099 -8.31830  1.000 68.73036  ? 200 GLU   A CD  1 
ATOM   1436 O OE1 . GLU   A 1 193 ? -17.87223 -20.72509 -8.93512  1.000 69.47339  ? 200 GLU   A OE1 1 
ATOM   1437 O OE2 . GLU   A 1 193 ? -17.66697 -22.72105 -8.04432  1.000 62.52075  ? 200 GLU   A OE2 1 
ATOM   1438 N N   . ARG   A 1 194 ? -13.27178 -21.16990 -5.57388  1.000 25.53172  ? 201 ARG   A N   1 
ATOM   1439 C CA  . ARG   A 1 194 ? -13.22679 -20.13692 -4.53935  1.000 28.06855  ? 201 ARG   A CA  1 
ATOM   1440 C C   . ARG   A 1 194 ? -11.86895 -19.44700 -4.48887  1.000 26.98617  ? 201 ARG   A C   1 
ATOM   1441 O O   . ARG   A 1 194 ? -11.78842 -18.26751 -4.12415  1.000 25.28489  ? 201 ARG   A O   1 
ATOM   1442 C CB  . ARG   A 1 194 ? -13.55745 -20.71395 -3.16239  1.000 30.95364  ? 201 ARG   A CB  1 
ATOM   1443 C CG  . ARG   A 1 194 ? -12.60873 -21.78354 -2.67128  1.000 34.60074  ? 201 ARG   A CG  1 
ATOM   1444 C CD  . ARG   A 1 194 ? -13.18968 -22.48452 -1.44439  1.000 42.20071  ? 201 ARG   A CD  1 
ATOM   1445 N NE  . ARG   A 1 194 ? -12.25334 -23.44487 -0.87452  1.000 48.14658  ? 201 ARG   A NE  1 
ATOM   1446 C CZ  . ARG   A 1 194 ? -12.32549 -23.91483 0.36410   1.000 54.54816  ? 201 ARG   A CZ  1 
ATOM   1447 N NH1 . ARG   A 1 194 ? -13.30078 -23.55612 1.18594   1.000 48.31713  ? 201 ARG   A NH1 1 
ATOM   1448 N NH2 . ARG   A 1 194 ? -11.39433 -24.76296 0.79064   1.000 53.32850  ? 201 ARG   A NH2 1 
ATOM   1449 N N   . ARG   A 1 195 ? -10.79700 -20.16063 -4.84197  1.000 20.19481  ? 202 ARG   A N   1 
ATOM   1450 C CA  . ARG   A 1 195 ? -9.47005  -19.55143 -4.83645  1.000 23.32165  ? 202 ARG   A CA  1 
ATOM   1451 C C   . ARG   A 1 195 ? -9.31904  -18.55687 -5.98258  1.000 22.90336  ? 202 ARG   A C   1 
ATOM   1452 O O   . ARG   A 1 195 ? -8.75415  -17.47173 -5.80121  1.000 20.64880  ? 202 ARG   A O   1 
ATOM   1453 C CB  . ARG   A 1 195 ? -8.39720  -20.64066 -4.91170  1.000 25.37976  ? 202 ARG   A CB  1 
ATOM   1454 C CG  . ARG   A 1 195 ? -6.95699  -20.12716 -4.93541  1.000 22.61585  ? 202 ARG   A CG  1 
ATOM   1455 C CD  . ARG   A 1 195 ? -6.52782  -19.60949 -3.56341  1.000 24.03111  ? 202 ARG   A CD  1 
ATOM   1456 N NE  . ARG   A 1 195 ? -5.09335  -19.34840 -3.51315  1.000 23.17507  ? 202 ARG   A NE  1 
ATOM   1457 C CZ  . ARG   A 1 195 ? -4.54537  -18.15592 -3.31812  1.000 26.34596  ? 202 ARG   A CZ  1 
ATOM   1458 N NH1 . ARG   A 1 195 ? -5.28459  -17.07411 -3.13412  1.000 23.38410  ? 202 ARG   A NH1 1 
ATOM   1459 N NH2 . ARG   A 1 195 ? -3.21986  -18.04686 -3.30646  1.000 24.07521  ? 202 ARG   A NH2 1 
ATOM   1460 N N   . ILE   A 1 196 ? -9.83052  -18.90094 -7.16685  1.000 21.95964  ? 203 ILE   A N   1 
ATOM   1461 C CA  . ILE   A 1 196 ? -9.75820  -17.97657 -8.29699  1.000 21.54652  ? 203 ILE   A CA  1 
ATOM   1462 C C   . ILE   A 1 196 ? -10.58333 -16.72481 -8.01928  1.000 20.58190  ? 203 ILE   A C   1 
ATOM   1463 O O   . ILE   A 1 196 ? -10.13015 -15.60264 -8.28075  1.000 21.08602  ? 203 ILE   A O   1 
ATOM   1464 C CB  . ILE   A 1 196 ? -10.20308 -18.66954 -9.59827  1.000 23.83232  ? 203 ILE   A CB  1 
ATOM   1465 C CG1 . ILE   A 1 196 ? -9.24130  -19.80770 -9.95677  1.000 22.18113  ? 203 ILE   A CG1 1 
ATOM   1466 C CG2 . ILE   A 1 196 ? -10.26858 -17.65520 -10.75309 1.000 20.95641  ? 203 ILE   A CG2 1 
ATOM   1467 C CD1 . ILE   A 1 196 ? -9.85718  -20.83584 -10.89832 1.000 25.59380  ? 203 ILE   A CD1 1 
ATOM   1468 N N   . LYS   A 1 197 ? -11.79974 -16.88809 -7.47591  1.000 19.52392  ? 204 LYS   A N   1 
ATOM   1469 C CA  . LYS   A 1 197 ? -12.62238 -15.71415 -7.18182  1.000 20.01828  ? 204 LYS   A CA  1 
ATOM   1470 C C   . LYS   A 1 197 ? -11.93169 -14.79451 -6.18897  1.000 27.98343  ? 204 LYS   A C   1 
ATOM   1471 O O   . LYS   A 1 197 ? -11.99553 -13.56530 -6.32252  1.000 23.93822  ? 204 LYS   A O   1 
ATOM   1472 C CB  . LYS   A 1 197 ? -13.99685 -16.08343 -6.61071  1.000 25.60042  ? 204 LYS   A CB  1 
ATOM   1473 C CG  . LYS   A 1 197 ? -14.89267 -16.97056 -7.42789  1.000 37.79080  ? 204 LYS   A CG  1 
ATOM   1474 C CD  . LYS   A 1 197 ? -16.22469 -17.09189 -6.68047  1.000 41.81204  ? 204 LYS   A CD  1 
ATOM   1475 C CE  . LYS   A 1 197 ? -16.51963 -18.48750 -6.20217  1.000 59.82902  ? 204 LYS   A CE  1 
ATOM   1476 N NZ  . LYS   A 1 197 ? -17.97775 -18.80362 -6.20895  1.000 56.06668  ? 204 LYS   A NZ  1 
ATOM   1477 N N   . GLU   A 1 198 ? -11.30365 -15.37420 -5.16053  1.000 21.88640  ? 205 GLU   A N   1 
ATOM   1478 C CA  . GLU   A 1 198 ? -10.60069 -14.56625 -4.17109  1.000 24.71515  ? 205 GLU   A CA  1 
ATOM   1479 C C   . GLU   A 1 198 ? -9.50642  -13.73596 -4.82867  1.000 21.72331  ? 205 GLU   A C   1 
ATOM   1480 O O   . GLU   A 1 198 ? -9.35352  -12.54382 -4.53597  1.000 20.30790  ? 205 GLU   A O   1 
ATOM   1481 C CB  . GLU   A 1 198 ? -10.01570 -15.47429 -3.08751  1.000 24.79574  ? 205 GLU   A CB  1 
ATOM   1482 C CG  . GLU   A 1 198 ? -9.06481  -14.79069 -2.11952  1.000 27.73160  ? 205 GLU   A CG  1 
ATOM   1483 C CD  . GLU   A 1 198 ? -8.37180  -15.78323 -1.20420  1.000 24.35306  ? 205 GLU   A CD  1 
ATOM   1484 O OE1 . GLU   A 1 198 ? -7.84059  -16.78755 -1.72772  1.000 27.91425  ? 205 GLU   A OE1 1 
ATOM   1485 O OE2 . GLU   A 1 198 ? -8.37425  -15.57160 0.03224   1.000 26.53232  ? 205 GLU   A OE2 1 
ATOM   1486 N N   . ILE   A 1 199 ? -8.74180  -14.34857 -5.73013  1.000 19.04277  ? 206 ILE   A N   1 
ATOM   1487 C CA  . ILE   A 1 199 ? -7.64037  -13.63901 -6.37549  1.000 24.28316  ? 206 ILE   A CA  1 
ATOM   1488 C C   . ILE   A 1 199 ? -8.17024  -12.54070 -7.28724  1.000 23.90584  ? 206 ILE   A C   1 
ATOM   1489 O O   . ILE   A 1 199 ? -7.64372  -11.42369 -7.30708  1.000 22.26609  ? 206 ILE   A O   1 
ATOM   1490 C CB  . ILE   A 1 199 ? -6.75111  -14.63104 -7.14496  1.000 19.64587  ? 206 ILE   A CB  1 
ATOM   1491 C CG1 . ILE   A 1 199 ? -6.07479  -15.59657 -6.16486  1.000 24.22449  ? 206 ILE   A CG1 1 
ATOM   1492 C CG2 . ILE   A 1 199 ? -5.70107  -13.88822 -7.95950  1.000 18.62703  ? 206 ILE   A CG2 1 
ATOM   1493 C CD1 . ILE   A 1 199 ? -5.55872  -16.84612 -6.83356  1.000 23.81914  ? 206 ILE   A CD1 1 
ATOM   1494 N N   . VAL   A 1 200 ? -9.21958  -12.83629 -8.05361  1.000 20.02878  ? 207 VAL   A N   1 
ATOM   1495 C CA  . VAL   A 1 200 ? -9.78689  -11.83093 -8.94782  1.000 18.83406  ? 207 VAL   A CA  1 
ATOM   1496 C C   . VAL   A 1 200 ? -10.32270 -10.65039 -8.14667  1.000 20.95696  ? 207 VAL   A C   1 
ATOM   1497 O O   . VAL   A 1 200 ? -10.08481 -9.48522  -8.49013  1.000 22.06296  ? 207 VAL   A O   1 
ATOM   1498 C CB  . VAL   A 1 200 ? -10.87470 -12.46635 -9.83445  1.000 24.13683  ? 207 VAL   A CB  1 
ATOM   1499 C CG1 . VAL   A 1 200 ? -11.65512 -11.39705 -10.56850 1.000 22.02526  ? 207 VAL   A CG1 1 
ATOM   1500 C CG2 . VAL   A 1 200 ? -10.23844 -13.45922 -10.82139 1.000 20.47488  ? 207 VAL   A CG2 1 
ATOM   1501 N N   . LYS   A 1 201 ? -11.02781 -10.93077 -7.05040  1.000 19.86389  ? 208 LYS   A N   1 
ATOM   1502 C CA  . LYS   A 1 201 ? -11.57177 -9.85571  -6.22578  1.000 23.34535  ? 208 LYS   A CA  1 
ATOM   1503 C C   . LYS   A 1 201 ? -10.45852 -9.04266  -5.57101  1.000 22.71203  ? 208 LYS   A C   1 
ATOM   1504 O O   . LYS   A 1 201 ? -10.57768 -7.82109  -5.42570  1.000 26.40623  ? 208 LYS   A O   1 
ATOM   1505 C CB  . LYS   A 1 201 ? -12.51645 -10.44346 -5.17627  1.000 28.70786  ? 208 LYS   A CB  1 
ATOM   1506 C CG  . LYS   A 1 201 ? -13.11269 -9.43058  -4.22354  1.000 29.94983  ? 208 LYS   A CG  1 
ATOM   1507 C CD  . LYS   A 1 201 ? -13.96672 -10.11476 -3.17026  1.000 35.15723  ? 208 LYS   A CD  1 
ATOM   1508 C CE  . LYS   A 1 201 ? -14.45442 -9.13364  -2.12064  1.000 43.24831  ? 208 LYS   A CE  1 
ATOM   1509 N NZ  . LYS   A 1 201 ? -15.52800 -9.72832  -1.27332  1.000 56.53936  ? 208 LYS   A NZ  1 
ATOM   1510 N N   . LYS   A 1 202 ? -9.35830  -9.69965  -5.19296  1.000 25.70138  ? 209 LYS   A N   1 
ATOM   1511 C CA  . LYS   A 1 202 ? -8.27451  -9.00780  -4.49557  1.000 28.62641  ? 209 LYS   A CA  1 
ATOM   1512 C C   . LYS   A 1 202 ? -7.48598  -8.09541  -5.43157  1.000 24.99407  ? 209 LYS   A C   1 
ATOM   1513 O O   . LYS   A 1 202 ? -7.15177  -6.96300  -5.06555  1.000 25.72016  ? 209 LYS   A O   1 
ATOM   1514 C CB  . LYS   A 1 202 ? -7.34095  -10.03105 -3.84468  1.000 26.04787  ? 209 LYS   A CB  1 
ATOM   1515 C CG  . LYS   A 1 202 ? -6.16553  -9.41985  -3.08291  1.000 36.56553  ? 209 LYS   A CG  1 
ATOM   1516 C CD  . LYS   A 1 202 ? -5.59200  -10.41116 -2.07637  1.000 48.52476  ? 209 LYS   A CD  1 
ATOM   1517 C CE  . LYS   A 1 202 ? -4.18382  -10.02616 -1.64858  1.000 57.23269  ? 209 LYS   A CE  1 
ATOM   1518 N NZ  . LYS   A 1 202 ? -3.47482  -11.14802 -0.96597  1.000 57.21828  ? 209 LYS   A NZ  1 
ATOM   1519 N N   . HIS   A 1 203 ? -7.18734  -8.56258  -6.64640  1.000 23.07606  ? 210 HIS   A N   1 
ATOM   1520 C CA  . HIS   A 1 203 ? -6.20625  -7.90706  -7.49925  1.000 31.59541  ? 210 HIS   A CA  1 
ATOM   1521 C C   . HIS   A 1 203 ? -6.76210  -7.31355  -8.78443  1.000 27.38093  ? 210 HIS   A C   1 
ATOM   1522 O O   . HIS   A 1 203 ? -6.08038  -6.48157  -9.39225  1.000 31.64882  ? 210 HIS   A O   1 
ATOM   1523 C CB  . HIS   A 1 203 ? -5.08781  -8.89187  -7.88084  1.000 26.15575  ? 210 HIS   A CB  1 
ATOM   1524 C CG  . HIS   A 1 203 ? -4.28214  -9.37453  -6.71545  1.000 24.35657  ? 210 HIS   A CG  1 
ATOM   1525 N ND1 . HIS   A 1 203 ? -3.46753  -8.54386  -5.97608  1.000 35.26934  ? 210 HIS   A ND1 1 
ATOM   1526 C CD2 . HIS   A 1 203 ? -4.15678  -10.60774 -6.16936  1.000 32.69780  ? 210 HIS   A CD2 1 
ATOM   1527 C CE1 . HIS   A 1 203 ? -2.88013  -9.24277  -5.02051  1.000 35.88112  ? 210 HIS   A CE1 1 
ATOM   1528 N NE2 . HIS   A 1 203 ? -3.28107  -10.49788 -5.11577  1.000 32.00603  ? 210 HIS   A NE2 1 
ATOM   1529 N N   . SER   A 1 204 ? -7.96065  -7.70613  -9.21970  1.000 24.02672  ? 211 SER   A N   1 
ATOM   1530 C CA  . SER   A 1 204 ? -8.46588  -7.30485  -10.52886 1.000 21.74652  ? 211 SER   A CA  1 
ATOM   1531 C C   . SER   A 1 204 ? -9.84882  -6.66459  -10.43414 1.000 22.15240  ? 211 SER   A C   1 
ATOM   1532 O O   . SER   A 1 204 ? -10.63563 -6.73336  -11.38511 1.000 25.57494  ? 211 SER   A O   1 
ATOM   1533 C CB  . SER   A 1 204 ? -8.49422  -8.49892  -11.48561 1.000 27.76088  ? 211 SER   A CB  1 
ATOM   1534 O OG  . SER   A 1 204 ? -7.22336  -9.13106  -11.54215 1.000 26.47973  ? 211 SER   A OG  1 
ATOM   1535 N N   . GLN   A 1 205 ? -10.15381 -6.01356  -9.30806  1.000 25.83502  ? 212 GLN   A N   1 
ATOM   1536 C CA  . GLN   A 1 205 ? -11.50798 -5.51133  -9.10108  1.000 35.32078  ? 212 GLN   A CA  1 
ATOM   1537 C C   . GLN   A 1 205 ? -11.85421 -4.33282  -10.00747 1.000 40.04896  ? 212 GLN   A C   1 
ATOM   1538 O O   . GLN   A 1 205 ? -13.04089 -4.07455  -10.23519 1.000 35.01167  ? 212 GLN   A O   1 
ATOM   1539 C CB  . GLN   A 1 205 ? -11.72280 -5.12628  -7.62989  1.000 37.93373  ? 212 GLN   A CB  1 
ATOM   1540 C CG  . GLN   A 1 205 ? -10.89500 -3.95247  -7.12318  1.000 47.22827  ? 212 GLN   A CG  1 
ATOM   1541 C CD  . GLN   A 1 205 ? -9.55280  -4.36484  -6.52403  1.000 67.69416  ? 212 GLN   A CD  1 
ATOM   1542 O OE1 . GLN   A 1 205 ? -8.79692  -5.15098  -7.10392  1.000 40.69913  ? 212 GLN   A OE1 1 
ATOM   1543 N NE2 . GLN   A 1 205 ? -9.25245  -3.82160  -5.34734  1.000 51.98531  ? 212 GLN   A NE2 1 
ATOM   1544 N N   . PHE   A 1 206 ? -10.86159 -3.62447  -10.54548 1.000 31.36808  ? 213 PHE   A N   1 
ATOM   1545 C CA  . PHE   A 1 206 ? -11.11644 -2.45999  -11.38543 1.000 35.93641  ? 213 PHE   A CA  1 
ATOM   1546 C C   . PHE   A 1 206 ? -10.80194 -2.70621  -12.86012 1.000 31.98825  ? 213 PHE   A C   1 
ATOM   1547 O O   . PHE   A 1 206 ? -10.65436 -1.74938  -13.62464 1.000 40.81496  ? 213 PHE   A O   1 
ATOM   1548 C CB  . PHE   A 1 206 ? -10.33132 -1.25632  -10.86969 1.000 32.37651  ? 213 PHE   A CB  1 
ATOM   1549 C CG  . PHE   A 1 206 ? -10.69303 -0.85570  -9.46309  1.000 39.25686  ? 213 PHE   A CG  1 
ATOM   1550 C CD1 . PHE   A 1 206 ? -11.98524 -0.46451  -9.15449  1.000 42.78544  ? 213 PHE   A CD1 1 
ATOM   1551 C CD2 . PHE   A 1 206 ? -9.74470  -0.87064  -8.45338  1.000 41.25279  ? 213 PHE   A CD2 1 
ATOM   1552 C CE1 . PHE   A 1 206 ? -12.32702 -0.09396  -7.86552  1.000 42.90114  ? 213 PHE   A CE1 1 
ATOM   1553 C CE2 . PHE   A 1 206 ? -10.08009 -0.50427  -7.16150  1.000 49.15215  ? 213 PHE   A CE2 1 
ATOM   1554 C CZ  . PHE   A 1 206 ? -11.37257 -0.11304  -6.86791  1.000 46.30619  ? 213 PHE   A CZ  1 
ATOM   1555 N N   . ILE   A 1 207 ? -10.69389 -3.96599  -13.27885 1.000 23.42802  ? 214 ILE   A N   1 
ATOM   1556 C CA  . ILE   A 1 207 ? -10.51586 -4.26522  -14.69592 1.000 21.63194  ? 214 ILE   A CA  1 
ATOM   1557 C C   . ILE   A 1 207 ? -11.81978 -3.98009  -15.42937 1.000 31.51055  ? 214 ILE   A C   1 
ATOM   1558 O O   . ILE   A 1 207 ? -12.89239 -4.44305  -15.02055 1.000 29.48170  ? 214 ILE   A O   1 
ATOM   1559 C CB  . ILE   A 1 207 ? -10.06376 -5.72065  -14.88375 1.000 23.14349  ? 214 ILE   A CB  1 
ATOM   1560 C CG1 . ILE   A 1 207 ? -8.65629  -5.90831  -14.30527 1.000 20.51159  ? 214 ILE   A CG1 1 
ATOM   1561 C CG2 . ILE   A 1 207 ? -10.09196 -6.10869  -16.35202 1.000 22.72359  ? 214 ILE   A CG2 1 
ATOM   1562 C CD1 . ILE   A 1 207 ? -7.58856  -5.13759  -15.05426 1.000 31.05168  ? 214 ILE   A CD1 1 
ATOM   1563 N N   . GLY   A 1 208 ? -11.73505 -3.21410  -16.51816 1.000 23.31106  ? 215 GLY   A N   1 
ATOM   1564 C CA  . GLY   A 1 208 ? -12.92284 -2.67638  -17.16134 1.000 28.53107  ? 215 GLY   A CA  1 
ATOM   1565 C C   . GLY   A 1 208 ? -13.58570 -3.56235  -18.19811 1.000 28.46337  ? 215 GLY   A C   1 
ATOM   1566 O O   . GLY   A 1 208 ? -14.24519 -3.06384  -19.11606 1.000 30.51701  ? 215 GLY   A O   1 
ATOM   1567 N N   . TYR   A 1 209 ? -13.43178 -4.87285  -18.06400 1.000 22.11441  ? 216 TYR   A N   1 
ATOM   1568 C CA  . TYR   A 1 209 ? -14.04548 -5.82774  -18.97370 1.000 25.21746  ? 216 TYR   A CA  1 
ATOM   1569 C C   . TYR   A 1 209 ? -14.63510 -6.95845  -18.15513 1.000 23.49955  ? 216 TYR   A C   1 
ATOM   1570 O O   . TYR   A 1 209 ? -14.11228 -7.28552  -17.08172 1.000 23.01013  ? 216 TYR   A O   1 
ATOM   1571 C CB  . TYR   A 1 209 ? -13.02660 -6.38232  -19.98405 1.000 18.33827  ? 216 TYR   A CB  1 
ATOM   1572 C CG  . TYR   A 1 209 ? -12.40948 -5.30459  -20.83761 1.000 20.48282  ? 216 TYR   A CG  1 
ATOM   1573 C CD1 . TYR   A 1 209 ? -13.03421 -4.86748  -21.99589 1.000 19.50378  ? 216 TYR   A CD1 1 
ATOM   1574 C CD2 . TYR   A 1 209 ? -11.20617 -4.70976  -20.47555 1.000 21.80498  ? 216 TYR   A CD2 1 
ATOM   1575 C CE1 . TYR   A 1 209 ? -12.48135 -3.86778  -22.76923 1.000 21.81040  ? 216 TYR   A CE1 1 
ATOM   1576 C CE2 . TYR   A 1 209 ? -10.63832 -3.70950  -21.25157 1.000 20.07354  ? 216 TYR   A CE2 1 
ATOM   1577 C CZ  . TYR   A 1 209 ? -11.28672 -3.29247  -22.39559 1.000 20.87687  ? 216 TYR   A CZ  1 
ATOM   1578 O OH  . TYR   A 1 209 ? -10.74959 -2.29882  -23.17318 1.000 23.41848  ? 216 TYR   A OH  1 
ATOM   1579 N N   . PRO   A 1 210 ? -15.72532 -7.57078  -18.61817 1.000 25.19562  ? 217 PRO   A N   1 
ATOM   1580 C CA  . PRO   A 1 210 ? -16.31386 -8.68704  -17.86848 1.000 22.72149  ? 217 PRO   A CA  1 
ATOM   1581 C C   . PRO   A 1 210 ? -15.35366 -9.86705  -17.79336 1.000 23.86571  ? 217 PRO   A C   1 
ATOM   1582 O O   . PRO   A 1 210 ? -14.79364 -10.30226 -18.80319 1.000 26.93379  ? 217 PRO   A O   1 
ATOM   1583 C CB  . PRO   A 1 210 ? -17.58007 -9.03324  -18.66387 1.000 29.60178  ? 217 PRO   A CB  1 
ATOM   1584 C CG  . PRO   A 1 210 ? -17.39484 -8.42556  -20.00828 1.000 30.12105  ? 217 PRO   A CG  1 
ATOM   1585 C CD  . PRO   A 1 210 ? -16.47758 -7.24909  -19.84597 1.000 23.14575  ? 217 PRO   A CD  1 
ATOM   1586 N N   . ILE   A 1 211 ? -15.15237 -10.36826 -16.57765 1.000 23.93495  ? 218 ILE   A N   1 
ATOM   1587 C CA  . ILE   A 1 211 ? -14.32837 -11.54442 -16.32008 1.000 19.95538  ? 218 ILE   A CA  1 
ATOM   1588 C C   . ILE   A 1 211 ? -15.26153 -12.65869 -15.88461 1.000 19.71886  ? 218 ILE   A C   1 
ATOM   1589 O O   . ILE   A 1 211 ? -15.90388 -12.56017 -14.83160 1.000 22.40135  ? 218 ILE   A O   1 
ATOM   1590 C CB  . ILE   A 1 211 ? -13.26657 -11.28544 -15.24175 1.000 19.21671  ? 218 ILE   A CB  1 
ATOM   1591 C CG1 . ILE   A 1 211 ? -12.34741 -10.12838 -15.63717 1.000 21.50775  ? 218 ILE   A CG1 1 
ATOM   1592 C CG2 . ILE   A 1 211 ? -12.48110 -12.56733 -14.96042 1.000 19.78616  ? 218 ILE   A CG2 1 
ATOM   1593 C CD1 . ILE   A 1 211 ? -11.53834 -9.57805  -14.47200 1.000 21.05183  ? 218 ILE   A CD1 1 
ATOM   1594 N N   . THR   A 1 212 ? -15.34031 -13.71280 -16.68580 1.000 19.23642  ? 219 THR   A N   1 
ATOM   1595 C CA  . THR   A 1 212 ? -16.24666 -14.82182 -16.42414 1.000 20.35649  ? 219 THR   A CA  1 
ATOM   1596 C C   . THR   A 1 212 ? -15.42726 -16.02224 -15.98614 1.000 17.97037  ? 219 THR   A C   1 
ATOM   1597 O O   . THR   A 1 212 ? -14.56542 -16.49423 -16.73203 1.000 17.89795  ? 219 THR   A O   1 
ATOM   1598 C CB  . THR   A 1 212 ? -17.07908 -15.16980 -17.65823 1.000 23.92267  ? 219 THR   A CB  1 
ATOM   1599 O OG1 . THR   A 1 212 ? -17.84608 -14.02666 -18.06708 1.000 23.05962  ? 219 THR   A OG1 1 
ATOM   1600 C CG2 . THR   A 1 212 ? -18.01869 -16.33821 -17.34732 1.000 24.83323  ? 219 THR   A CG2 1 
ATOM   1601 N N   . LEU   A 1 213 ? -15.69264 -16.50686 -14.78175 1.000 18.82335  ? 220 LEU   A N   1 
ATOM   1602 C CA  . LEU   A 1 213 ? -15.05558 -17.71609 -14.27433 1.000 16.04222  ? 220 LEU   A CA  1 
ATOM   1603 C C   . LEU   A 1 213 ? -15.95294 -18.90223 -14.62003 1.000 22.22762  ? 220 LEU   A C   1 
ATOM   1604 O O   . LEU   A 1 213 ? -17.05596 -19.03554 -14.07384 1.000 20.95146  ? 220 LEU   A O   1 
ATOM   1605 C CB  . LEU   A 1 213 ? -14.82897 -17.60816 -12.76699 1.000 17.02214  ? 220 LEU   A CB  1 
ATOM   1606 C CG  . LEU   A 1 213 ? -14.28743 -18.83553 -12.04322 1.000 23.78384  ? 220 LEU   A CG  1 
ATOM   1607 C CD1 . LEU   A 1 213 ? -13.03686 -19.36488 -12.73041 1.000 20.67213  ? 220 LEU   A CD1 1 
ATOM   1608 C CD2 . LEU   A 1 213 ? -14.00060 -18.49414 -10.57473 1.000 22.59655  ? 220 LEU   A CD2 1 
ATOM   1609 N N   . PHE   A 1 214 ? -15.49453 -19.74372 -15.54390 1.000 19.78623  ? 221 PHE   A N   1 
ATOM   1610 C CA  . PHE   A 1 214 ? -16.23548 -20.94409 -15.90794 1.000 21.13941  ? 221 PHE   A CA  1 
ATOM   1611 C C   . PHE   A 1 214 ? -16.23726 -21.92935 -14.74323 1.000 21.36737  ? 221 PHE   A C   1 
ATOM   1612 O O   . PHE   A 1 214 ? -15.29789 -21.98196 -13.94767 1.000 22.90820  ? 221 PHE   A O   1 
ATOM   1613 C CB  . PHE   A 1 214 ? -15.61077 -21.62050 -17.13627 1.000 20.34944  ? 221 PHE   A CB  1 
ATOM   1614 C CG  . PHE   A 1 214 ? -15.90574 -20.93579 -18.45547 1.000 18.24679  ? 221 PHE   A CG  1 
ATOM   1615 C CD1 . PHE   A 1 214 ? -16.04555 -19.55841 -18.53732 1.000 15.55246  ? 221 PHE   A CD1 1 
ATOM   1616 C CD2 . PHE   A 1 214 ? -16.01220 -21.68397 -19.61922 1.000 20.34521  ? 221 PHE   A CD2 1 
ATOM   1617 C CE1 . PHE   A 1 214 ? -16.29586 -18.93420 -19.75174 1.000 17.11902  ? 221 PHE   A CE1 1 
ATOM   1618 C CE2 . PHE   A 1 214 ? -16.26638 -21.06875 -20.84557 1.000 22.51796  ? 221 PHE   A CE2 1 
ATOM   1619 C CZ  . PHE   A 1 214 ? -16.41752 -19.69266 -20.90877 1.000 18.18858  ? 221 PHE   A CZ  1 
ATOM   1620 N N   . VAL   A 1 215 ? -17.29164 -22.73256 -14.65555 1.000 20.57925  ? 222 VAL   A N   1 
ATOM   1621 C CA  . VAL   A 1 215 ? -17.36401 -23.80218 -13.66911 1.000 22.77223  ? 222 VAL   A CA  1 
ATOM   1622 C C   . VAL   A 1 215 ? -17.19415 -25.14228 -14.38161 1.000 28.52137  ? 222 VAL   A C   1 
ATOM   1623 O O   . VAL   A 1 215 ? -17.23723 -25.23078 -15.60752 1.000 25.13729  ? 222 VAL   A O   1 
ATOM   1624 C CB  . VAL   A 1 215 ? -18.66944 -23.75417 -12.85038 1.000 38.71883  ? 222 VAL   A CB  1 
ATOM   1625 C CG1 . VAL   A 1 215 ? -18.73296 -22.47472 -12.03379 1.000 45.19377  ? 222 VAL   A CG1 1 
ATOM   1626 C CG2 . VAL   A 1 215 ? -19.85815 -23.82781 -13.76458 1.000 29.91050  ? 222 VAL   A CG2 1 
ATOM   1627 N N   . GLU   A 1 216 ? -16.97594 -26.19282 -13.59611 1.000 27.28094  ? 223 GLU   A N   1 
ATOM   1628 C CA  . GLU   A 1 216 ? -16.75514 -27.52981 -14.12993 1.000 36.00851  ? 223 GLU   A CA  1 
ATOM   1629 C C   . GLU   A 1 216 ? -17.86674 -28.47029 -13.68077 1.000 41.03795  ? 223 GLU   A C   1 
ATOM   1630 O O   . GLU   A 1 216 ? -18.54067 -28.22661 -12.67685 1.000 42.23422  ? 223 GLU   A O   1 
ATOM   1631 C CB  . GLU   A 1 216 ? -15.39529 -28.08519 -13.69191 1.000 39.42127  ? 223 GLU   A CB  1 
ATOM   1632 C CG  . GLU   A 1 216 ? -14.22287 -27.17549 -14.01920 1.000 37.73499  ? 223 GLU   A CG  1 
ATOM   1633 C CD  . GLU   A 1 216 ? -12.89686 -27.75768 -13.56647 1.000 45.39140  ? 223 GLU   A CD  1 
ATOM   1634 O OE1 . GLU   A 1 216 ? -12.54922 -28.87103 -14.01853 1.000 40.71655  ? 223 GLU   A OE1 1 
ATOM   1635 O OE2 . GLU   A 1 216 ? -12.21021 -27.10676 -12.74763 1.000 42.37323  ? 223 GLU   A OE2 1 
ATOM   1636 N N   . LYS   A 1 217 ? -18.04517 -29.55439 -14.44069 1.000 45.54652  ? 224 LYS   A N   1 
ATOM   1637 C CA  . LYS   A 1 217 ? -19.07140 -30.56442 -14.15473 1.000 53.72040  ? 224 LYS   A CA  1 
ATOM   1638 C C   . LYS   A 1 217 ? -19.04418 -31.02051 -12.69834 1.000 65.65995  ? 224 LYS   A C   1 
ATOM   1639 O O   . LYS   A 1 217 ? -18.07314 -31.62912 -12.25000 1.000 65.75839  ? 224 LYS   A O   1 
ATOM   1640 C CB  . LYS   A 1 217 ? -18.90818 -31.79454 -15.05671 1.000 68.16946  ? 224 LYS   A CB  1 
ATOM   1641 C CG  . LYS   A 1 217 ? -18.15025 -31.56752 -16.35116 1.000 66.95287  ? 224 LYS   A CG  1 
ATOM   1642 C CD  . LYS   A 1 217 ? -18.08505 -32.85196 -17.17571 1.000 70.66615  ? 224 LYS   A CD  1 
ATOM   1643 C CE  . LYS   A 1 217 ? -19.34816 -33.07961 -17.99262 1.000 68.32560  ? 224 LYS   A CE  1 
ATOM   1644 N NZ  . LYS   A 1 217 ? -19.04459 -33.67603 -19.33056 1.000 67.87365  ? 224 LYS   A NZ  1 
HETATM 1645 S S1  . A1AY4 B 2 .   ? -14.87838 -19.05649 -25.03407 1.000 71.11040  ? 301 A1AY4 A S1  1 
HETATM 1646 C C1  . A1AY4 B 2 .   ? -11.93714 -25.29390 -23.98213 1.000 55.66516  ? 301 A1AY4 A C1  1 
HETATM 1647 C C2  . A1AY4 B 2 .   ? -12.62946 -22.92700 -24.47381 1.000 69.15264  ? 301 A1AY4 A C2  1 
HETATM 1648 C C3  . A1AY4 B 2 .   ? -13.98059 -22.89325 -24.18743 1.000 55.91867  ? 301 A1AY4 A C3  1 
HETATM 1649 C C4  . A1AY4 B 2 .   ? -14.66113 -21.70518 -24.36415 1.000 53.73814  ? 301 A1AY4 A C4  1 
HETATM 1650 C C5  . A1AY4 B 2 .   ? -13.98734 -20.56662 -24.81387 1.000 68.97302  ? 301 A1AY4 A C5  1 
HETATM 1651 C C6  . A1AY4 B 2 .   ? -12.63454 -20.60535 -25.10315 1.000 62.04615  ? 301 A1AY4 A C6  1 
HETATM 1652 C C7  . A1AY4 B 2 .   ? -11.97752 -21.80128 -24.92256 1.000 77.03961  ? 301 A1AY4 A C7  1 
HETATM 1653 C C8  . A1AY4 B 2 .   ? -10.47278 -23.42960 -24.81049 1.000 75.21454  ? 301 A1AY4 A C8  1 
HETATM 1654 N N1  . A1AY4 B 2 .   ? -11.67901 -23.92738 -24.41013 1.000 70.11898  ? 301 A1AY4 A N1  1 
HETATM 1655 N N2  . A1AY4 B 2 .   ? -14.00342 -17.87982 -24.39060 1.000 33.02058  ? 301 A1AY4 A N2  1 
HETATM 1656 O O1  . A1AY4 B 2 .   ? -10.64314 -22.10199 -25.13326 1.000 75.83689  ? 301 A1AY4 A O1  1 
HETATM 1657 O O2  . A1AY4 B 2 .   ? -9.40627  -23.98185 -24.89519 1.000 83.34416  ? 301 A1AY4 A O2  1 
HETATM 1658 O O3  . A1AY4 B 2 .   ? -14.95531 -18.79881 -26.43484 1.000 84.02475  ? 301 A1AY4 A O3  1 
HETATM 1659 O O4  . A1AY4 B 2 .   ? -16.08842 -19.14471 -24.28441 0.294 43.22666  ? 301 A1AY4 A O4  1 
HETATM 1660 O O   . HOH   C 3 .   ? -17.62388 -24.68435 -8.69021  1.000 52.79180  ? 401 HOH   A O   1 
HETATM 1661 O O   . HOH   C 3 .   ? -12.65754 -27.49758 -34.89932 1.000 47.66773  ? 402 HOH   A O   1 
HETATM 1662 O O   . HOH   C 3 .   ? -17.52100 -10.70196 -2.18534  1.000 53.13216  ? 403 HOH   A O   1 
HETATM 1663 O O   . HOH   C 3 .   ? -1.57510  -29.07968 -5.86699  1.000 33.59308  ? 404 HOH   A O   1 
HETATM 1664 O O   . HOH   C 3 .   ? -18.69009 -10.96380 -23.78539 1.000 35.60266  ? 405 HOH   A O   1 
HETATM 1665 O O   . HOH   C 3 .   ? -8.01997  -22.89449 -30.57349 1.000 44.30846  ? 406 HOH   A O   1 
HETATM 1666 O O   . HOH   C 3 .   ? 11.66565  -21.75033 -40.65539 1.000 50.81501  ? 407 HOH   A O   1 
HETATM 1667 O O   . HOH   C 3 .   ? 0.32480   -14.83359 -1.47932  1.000 42.04159  ? 408 HOH   A O   1 
HETATM 1668 O O   . HOH   C 3 .   ? -14.08637 -16.16004 -26.16829 1.000 37.28520  ? 409 HOH   A O   1 
HETATM 1669 O O   . HOH   C 3 .   ? 9.17183   -3.27194  -20.43797 1.000 39.39131  ? 410 HOH   A O   1 
HETATM 1670 O O   . HOH   C 3 .   ? 5.57554   -29.16352 -8.31213  1.000 48.55333  ? 411 HOH   A O   1 
HETATM 1671 O O   . HOH   C 3 .   ? -0.21536  -5.56318  -38.39625 1.000 45.72261  ? 412 HOH   A O   1 
HETATM 1672 O O   . HOH   C 3 .   ? 3.62782   -30.12792 -18.93949 1.000 47.88180  ? 413 HOH   A O   1 
HETATM 1673 O O   . HOH   C 3 .   ? 1.93081   -15.49849 -41.01604 1.000 42.60524  ? 414 HOH   A O   1 
HETATM 1674 O O   . HOH   C 3 .   ? 22.90277  -15.76903 -19.25673 1.000 46.19515  ? 415 HOH   A O   1 
HETATM 1675 O O   . HOH   C 3 .   ? -16.25953 -25.78531 -17.90601 1.000 25.08448  ? 416 HOH   A O   1 
HETATM 1676 O O   . HOH   C 3 .   ? -8.65315  -11.91858 -36.40229 1.000 26.27961  ? 417 HOH   A O   1 
HETATM 1677 O O   . HOH   C 3 .   ? 8.47163   -16.48567 -39.55622 1.000 38.50459  ? 418 HOH   A O   1 
HETATM 1678 O O   . HOH   C 3 .   ? -13.08147 -7.29042  -11.97287 1.000 35.51811  ? 419 HOH   A O   1 
HETATM 1679 O O   . HOH   C 3 .   ? 18.27322  -7.22851  -20.31278 1.000 37.09441  ? 420 HOH   A O   1 
HETATM 1680 O O   . HOH   C 3 .   ? -3.63874  -10.87855 -24.05845 1.000 27.79770  ? 421 HOH   A O   1 
HETATM 1681 O O   . HOH   C 3 .   ? 5.90892   -21.84663 -37.27650 1.000 37.38311  ? 422 HOH   A O   1 
HETATM 1682 O O   . HOH   C 3 .   ? 9.06407   -26.45410 -17.01223 1.000 28.89180  ? 423 HOH   A O   1 
HETATM 1683 O O   . HOH   C 3 .   ? -13.35065 -0.78234  -20.49835 1.000 34.14706  ? 424 HOH   A O   1 
HETATM 1684 O O   . HOH   C 3 .   ? -2.97675  -3.33656  -35.37239 1.000 44.14461  ? 425 HOH   A O   1 
HETATM 1685 O O   . HOH   C 3 .   ? 7.78128   -23.18091 -14.17610 1.000 28.88577  ? 426 HOH   A O   1 
HETATM 1686 O O   . HOH   C 3 .   ? 1.45497   -7.87094  -16.55477 1.000 23.79447  ? 427 HOH   A O   1 
HETATM 1687 O O   . HOH   C 3 .   ? -16.36728 -12.80328 -19.84227 1.000 20.24669  ? 428 HOH   A O   1 
HETATM 1688 O O   . HOH   C 3 .   ? 15.26845  -0.81857  -12.06055 1.000 49.89726  ? 429 HOH   A O   1 
HETATM 1689 O O   . HOH   C 3 .   ? 3.17777   -24.51208 -38.60998 1.000 36.02801  ? 430 HOH   A O   1 
HETATM 1690 O O   . HOH   C 3 .   ? 6.69709   -26.73015 -27.60428 1.000 35.08363  ? 431 HOH   A O   1 
HETATM 1691 O O   . HOH   C 3 .   ? 7.69390   -27.84791 -23.95674 1.000 32.04315  ? 432 HOH   A O   1 
HETATM 1692 O O   . HOH   C 3 .   ? 6.08590   -21.04736 -0.02444  1.000 29.36184  ? 433 HOH   A O   1 
HETATM 1693 O O   . HOH   C 3 .   ? 7.65726   -18.74486 -6.59201  1.000 24.28266  ? 434 HOH   A O   1 
HETATM 1694 O O   . HOH   C 3 .   ? 0.414     -1.454    -19.842   1.000 38.96595  ? 435 HOH   A O   1 
HETATM 1695 O O   . HOH   C 3 .   ? -5.78013  -18.82110 -39.08222 1.000 38.32464  ? 436 HOH   A O   1 
HETATM 1696 O O   . HOH   C 3 .   ? 0.56624   -26.98204 -37.29383 1.000 48.74158  ? 437 HOH   A O   1 
HETATM 1697 O O   . HOH   C 3 .   ? -15.19452 -23.44654 -30.49884 1.000 37.56593  ? 438 HOH   A O   1 
HETATM 1698 O O   . HOH   C 3 .   ? -2.99624  -5.98432  -6.48144  1.000 35.97916  ? 439 HOH   A O   1 
HETATM 1699 O O   . HOH   C 3 .   ? -6.33671  -4.96780  -39.07077 1.000 43.98770  ? 440 HOH   A O   1 
HETATM 1700 O O   . HOH   C 3 .   ? -11.87350 -0.25935  -15.45176 1.000 40.57486  ? 441 HOH   A O   1 
HETATM 1701 O O   . HOH   C 3 .   ? -14.53718 -6.99695  -14.46876 1.000 35.03429  ? 442 HOH   A O   1 
HETATM 1702 O O   . HOH   C 3 .   ? -6.36397  -7.74914  -34.29951 1.000 21.61821  ? 443 HOH   A O   1 
HETATM 1703 O O   . HOH   C 3 .   ? 7.61353   1.28645   -14.91154 1.000 34.95524  ? 444 HOH   A O   1 
HETATM 1704 O O   . HOH   C 3 .   ? -5.34779  -10.44720 -27.37391 1.000 20.22188  ? 445 HOH   A O   1 
HETATM 1705 O O   . HOH   C 3 .   ? -4.35938  0.51052   -22.21292 1.000 36.75130  ? 446 HOH   A O   1 
HETATM 1706 O O   . HOH   C 3 .   ? -8.09269  1.80381   -36.49348 1.000 40.07723  ? 447 HOH   A O   1 
HETATM 1707 O O   . HOH   C 3 .   ? -5.77720  -2.10278  -19.33926 1.000 23.71580  ? 448 HOH   A O   1 
HETATM 1708 O O   . HOH   C 3 .   ? 18.04433  -19.26977 -24.60260 1.000 27.86597  ? 449 HOH   A O   1 
HETATM 1709 O O   . HOH   C 3 .   ? 0.85046   -20.99650 -4.60152  1.000 30.55111  ? 450 HOH   A O   1 
HETATM 1710 O O   . HOH   C 3 .   ? -2.18758  -13.67334 -35.66129 1.000 22.36688  ? 451 HOH   A O   1 
HETATM 1711 O O   . HOH   C 3 .   ? -13.76948 -17.08150 -2.74313  1.000 24.29831  ? 452 HOH   A O   1 
HETATM 1712 O O   . HOH   C 3 .   ? -8.42040  4.71862   -33.52308 1.000 30.06409  ? 453 HOH   A O   1 
HETATM 1713 O O   . HOH   C 3 .   ? -17.15333 -5.57148  -22.83320 1.000 31.77900  ? 454 HOH   A O   1 
HETATM 1714 O O   . HOH   C 3 .   ? 9.92206   -14.83943 -25.29846 1.000 24.25717  ? 455 HOH   A O   1 
HETATM 1715 O O   . HOH   C 3 .   ? -1.02508  -11.35391 -2.99569  1.000 35.71692  ? 456 HOH   A O   1 
HETATM 1716 O O   . HOH   C 3 .   ? -7.59952  -24.57858 -22.88694 1.000 33.99756  ? 457 HOH   A O   1 
HETATM 1717 O O   . HOH   C 3 .   ? -3.99995  -14.00502 -0.95794  1.000 40.20920  ? 458 HOH   A O   1 
HETATM 1718 O O   . HOH   C 3 .   ? 11.56973  -27.62802 -34.65981 1.000 30.49581  ? 459 HOH   A O   1 
HETATM 1719 O O   . HOH   C 3 .   ? 11.42252  -28.53793 -30.51239 1.000 31.24158  ? 460 HOH   A O   1 
HETATM 1720 O O   . HOH   C 3 .   ? 0.56894   -5.30653  -14.06432 1.000 43.74181  ? 461 HOH   A O   1 
HETATM 1721 O O   . HOH   C 3 .   ? 9.68546   -17.32837 -7.68404  1.000 26.72699  ? 462 HOH   A O   1 
HETATM 1722 O O   . HOH   C 3 .   ? -7.50347  -5.37575  -2.89003  1.000 51.82644  ? 463 HOH   A O   1 
HETATM 1723 O O   . HOH   C 3 .   ? -9.37947  -2.30772  -17.58984 1.000 21.30200  ? 464 HOH   A O   1 
HETATM 1724 O O   . HOH   C 3 .   ? 12.95430  -13.98947 -29.66166 1.000 28.02867  ? 465 HOH   A O   1 
HETATM 1725 O O   . HOH   C 3 .   ? -1.61943  -32.52682 -7.98633  1.000 49.16292  ? 466 HOH   A O   1 
HETATM 1726 O O   . HOH   C 3 .   ? -11.02322 -14.12832 -37.71506 1.000 36.55489  ? 467 HOH   A O   1 
HETATM 1727 O O   . HOH   C 3 .   ? -0.28318  -5.39972  -18.41148 1.000 32.39230  ? 468 HOH   A O   1 
HETATM 1728 O O   . HOH   C 3 .   ? -14.68505 -22.78976 -11.41286 1.000 32.56652  ? 469 HOH   A O   1 
HETATM 1729 O O   . HOH   C 3 .   ? -10.66531 -14.45063 1.00876   1.000 32.31188  ? 470 HOH   A O   1 
HETATM 1730 O O   . HOH   C 3 .   ? 8.03183   -23.06253 -7.08579  1.000 38.61163  ? 471 HOH   A O   1 
HETATM 1731 O O   . HOH   C 3 .   ? -15.89982 0.16526   -30.54708 1.000 47.93441  ? 472 HOH   A O   1 
HETATM 1732 O O   . HOH   C 3 .   ? 8.88344   -20.19290 -4.33862  1.000 30.10549  ? 473 HOH   A O   1 
HETATM 1733 O O   . HOH   C 3 .   ? 11.31831  -8.02921  -27.39953 1.000 23.12681  ? 474 HOH   A O   1 
HETATM 1734 O O   . HOH   C 3 .   ? -4.18933  -4.78701  -8.38267  1.000 43.87666  ? 475 HOH   A O   1 
HETATM 1735 O O   . HOH   C 3 .   ? 3.34918   -6.18102  -11.10049 1.000 29.00393  ? 476 HOH   A O   1 
HETATM 1736 O O   . HOH   C 3 .   ? 3.05508   -20.40898 -2.66672  1.000 40.39213  ? 477 HOH   A O   1 
HETATM 1737 O O   . HOH   C 3 .   ? -19.38816 -10.26342 -32.86120 1.000 49.51496  ? 478 HOH   A O   1 
HETATM 1738 O O   . HOH   C 3 .   ? 20.24941  -10.76982 -26.35502 1.000 45.42147  ? 479 HOH   A O   1 
HETATM 1739 O O   . HOH   C 3 .   ? -8.12662  -24.93567 -19.08006 1.000 18.99202  ? 480 HOH   A O   1 
HETATM 1740 O O   . HOH   C 3 .   ? -13.03537 -24.91860 -10.84431 1.000 32.55286  ? 481 HOH   A O   1 
HETATM 1741 O O   . HOH   C 3 .   ? 14.56968  -16.04314 -30.70045 1.000 35.59305  ? 482 HOH   A O   1 
HETATM 1742 O O   . HOH   C 3 .   ? -10.37694 -11.57468 -2.17885  1.000 25.76784  ? 483 HOH   A O   1 
HETATM 1743 O O   . HOH   C 3 .   ? 10.42938  -21.06329 -6.87930  1.000 40.38379  ? 484 HOH   A O   1 
HETATM 1744 O O   . HOH   C 3 .   ? -20.59090 -14.25684 -18.11279 1.000 46.21955  ? 485 HOH   A O   1 
HETATM 1745 O O   . HOH   C 3 .   ? -1.16504  -7.41583  -23.63106 1.000 25.73564  ? 486 HOH   A O   1 
HETATM 1746 O O   . HOH   C 3 .   ? -7.68388  -28.32003 -7.90771  1.000 33.75933  ? 487 HOH   A O   1 
HETATM 1747 O O   . HOH   C 3 .   ? 5.97754   -25.56623 -7.26075  1.000 40.21594  ? 488 HOH   A O   1 
HETATM 1748 O O   . HOH   C 3 .   ? -3.65105  -21.09363 -38.53652 1.000 47.81651  ? 489 HOH   A O   1 
HETATM 1749 O O   . HOH   C 3 .   ? 3.66797   -7.69338  -36.54046 1.000 36.25092  ? 490 HOH   A O   1 
HETATM 1750 O O   . HOH   C 3 .   ? 10.61153  -25.37635 -23.67261 1.000 24.01330  ? 491 HOH   A O   1 
HETATM 1751 O O   . HOH   C 3 .   ? 6.60236   -29.70684 -19.91307 1.000 37.60243  ? 492 HOH   A O   1 
HETATM 1752 O O   . HOH   C 3 .   ? 13.64153  -14.35149 -26.77622 1.000 24.03623  ? 493 HOH   A O   1 
HETATM 1753 O O   . HOH   C 3 .   ? -5.76586  -31.24333 -11.51207 1.000 31.97117  ? 494 HOH   A O   1 
HETATM 1754 O O   . HOH   C 3 .   ? -10.28168 -0.63171  -20.02568 1.000 39.69021  ? 495 HOH   A O   1 
HETATM 1755 O O   . HOH   C 3 .   ? -4.67571  0.44975   -30.39625 1.000 34.81146  ? 496 HOH   A O   1 
HETATM 1756 O O   . HOH   C 3 .   ? -6.27834  -11.31868 -10.11066 1.000 27.39435  ? 497 HOH   A O   1 
HETATM 1757 O O   . HOH   C 3 .   ? 19.94262  0.40961   -11.42867 1.000 58.24899  ? 498 HOH   A O   1 
HETATM 1758 O O   . HOH   C 3 .   ? -14.16335 -12.71783 -7.84881  1.000 24.97184  ? 499 HOH   A O   1 
HETATM 1759 O O   . HOH   C 3 .   ? 1.93190   -3.97017  -16.98905 1.000 47.88636  ? 500 HOH   A O   1 
HETATM 1760 O O   . HOH   C 3 .   ? 12.36418  -8.91567  -29.90944 1.000 38.38364  ? 501 HOH   A O   1 
HETATM 1761 O O   . HOH   C 3 .   ? -3.270    -20.916   -0.554    1.000 42.92549  ? 502 HOH   A O   1 
HETATM 1762 O O   . HOH   C 3 .   ? 8.94122   -15.52661 -27.79020 1.000 21.07691  ? 503 HOH   A O   1 
HETATM 1763 O O   . HOH   C 3 .   ? -8.08221  -3.81801  -10.69035 1.000 30.22352  ? 504 HOH   A O   1 
HETATM 1764 O O   . HOH   C 3 .   ? -5.41114  -7.68015  -13.09317 1.000 21.05699  ? 505 HOH   A O   1 
HETATM 1765 O O   . HOH   C 3 .   ? 4.74520   -30.58111 -11.52158 1.000 41.75316  ? 506 HOH   A O   1 
HETATM 1766 O O   . HOH   C 3 .   ? -16.08100 -2.97715  -21.22495 1.000 31.35794  ? 507 HOH   A O   1 
HETATM 1767 O O   . HOH   C 3 .   ? 14.06574  -15.50506 -2.10927  1.000 37.05144  ? 508 HOH   A O   1 
HETATM 1768 O O   . HOH   C 3 .   ? -5.18071  -14.18431 -22.59698 1.000 20.51056  ? 509 HOH   A O   1 
HETATM 1769 O O   . HOH   C 3 .   ? -0.14431  -7.18404  -30.78978 1.000 33.05551  ? 510 HOH   A O   1 
HETATM 1770 O O   . HOH   C 3 .   ? 18.49321  -15.96513 -13.54755 1.000 38.15383  ? 511 HOH   A O   1 
HETATM 1771 O O   . HOH   C 3 .   ? -11.99497 -7.61923  -38.33787 1.000 40.35958  ? 512 HOH   A O   1 
HETATM 1772 O O   . HOH   C 3 .   ? 4.93950   -9.71816  -2.47942  1.000 45.55724  ? 513 HOH   A O   1 
HETATM 1773 O O   . HOH   C 3 .   ? 15.27167  -0.59644  -19.37977 1.000 39.79921  ? 514 HOH   A O   1 
HETATM 1774 O O   . HOH   C 3 .   ? -19.802   -19.672   -14.275   1.000 23.61796  ? 515 HOH   A O   1 
HETATM 1775 O O   . HOH   C 3 .   ? -3.16263  -1.11420  -24.07300 1.000 27.53696  ? 516 HOH   A O   1 
HETATM 1776 O O   . HOH   C 3 .   ? 19.86358  -16.82660 -27.60850 1.000 37.03678  ? 517 HOH   A O   1 
HETATM 1777 O O   . HOH   C 3 .   ? 4.12721   -24.29290 -30.62538 1.000 23.66014  ? 518 HOH   A O   1 
HETATM 1778 O O   . HOH   C 3 .   ? 20.01562  -5.24888  -14.81939 1.000 54.81992  ? 519 HOH   A O   1 
HETATM 1779 O O   . HOH   C 3 .   ? 3.51816   -6.84365  -17.88353 1.000 27.82781  ? 520 HOH   A O   1 
HETATM 1780 O O   . HOH   C 3 .   ? 10.67058  -25.62873 -26.68288 1.000 30.67928  ? 521 HOH   A O   1 
HETATM 1781 O O   . HOH   C 3 .   ? 3.08538   -4.01036  -8.97457  1.000 48.82922  ? 522 HOH   A O   1 
HETATM 1782 O O   . HOH   C 3 .   ? 3.76748   -11.89399 -38.54060 1.000 27.22339  ? 523 HOH   A O   1 
HETATM 1783 O O   . HOH   C 3 .   ? -17.85649 -18.89874 -11.34563 1.000 33.87439  ? 524 HOH   A O   1 
HETATM 1784 O O   . HOH   C 3 .   ? 8.47788   -20.54226 -9.26198  1.000 30.85793  ? 525 HOH   A O   1 
HETATM 1785 O O   . HOH   C 3 .   ? -15.26108 -11.14822 -29.84563 1.000 27.27574  ? 526 HOH   A O   1 
HETATM 1786 O O   . HOH   C 3 .   ? 15.43551  -20.30929 -18.65109 1.000 24.80936  ? 527 HOH   A O   1 
HETATM 1787 O O   . HOH   C 3 .   ? 0.42302   -5.49193  -21.85501 1.000 38.84585  ? 528 HOH   A O   1 
HETATM 1788 O O   . HOH   C 3 .   ? -8.88227  -10.44082 -40.46485 1.000 45.20349  ? 529 HOH   A O   1 
HETATM 1789 O O   . HOH   C 3 .   ? -2.24311  -0.38724  -18.84150 1.000 41.66729  ? 530 HOH   A O   1 
HETATM 1790 O O   . HOH   C 3 .   ? -10.15175 -14.99858 -28.32544 1.000 30.89802  ? 531 HOH   A O   1 
HETATM 1791 O O   . HOH   C 3 .   ? 0.91789   -6.13979  -34.16962 1.000 43.41424  ? 532 HOH   A O   1 
HETATM 1792 O O   . HOH   C 3 .   ? -1.47234  -6.40693  -26.10987 1.000 27.98445  ? 533 HOH   A O   1 
HETATM 1793 O O   . HOH   C 3 .   ? -2.48349  -10.57128 -26.41691 1.000 35.58375  ? 534 HOH   A O   1 
HETATM 1794 O O   . HOH   C 3 .   ? 12.47024  -27.39222 -19.62557 1.000 44.29741  ? 535 HOH   A O   1 
HETATM 1795 O O   . HOH   C 3 .   ? -8.71918  -18.18628 -36.71506 1.000 44.66742  ? 536 HOH   A O   1 
HETATM 1796 O O   . HOH   C 3 .   ? -1.77877  -25.59204 -4.71300  1.000 26.10810  ? 537 HOH   A O   1 
HETATM 1797 O O   . HOH   C 3 .   ? 8.60726   -19.90429 -41.25912 1.000 49.65013  ? 538 HOH   A O   1 
HETATM 1798 O O   . HOH   C 3 .   ? -6.20975  -5.07751  -35.60581 1.000 24.09080  ? 539 HOH   A O   1 
HETATM 1799 O O   . HOH   C 3 .   ? 2.02237   -5.97966  -26.04765 1.000 45.19854  ? 540 HOH   A O   1 
HETATM 1800 O O   . HOH   C 3 .   ? -5.99789  -14.07589 0.76702   1.000 32.00466  ? 541 HOH   A O   1 
HETATM 1801 O O   . HOH   C 3 .   ? 20.85988  -14.10617 -26.70751 1.000 37.68785  ? 542 HOH   A O   1 
HETATM 1802 O O   . HOH   C 3 .   ? 13.70627  -20.47781 -20.74692 1.000 22.11016  ? 543 HOH   A O   1 
HETATM 1803 O O   . HOH   C 3 .   ? 4.41891   -19.39925 -40.62192 1.000 41.09021  ? 544 HOH   A O   1 
HETATM 1804 O O   . HOH   C 3 .   ? -13.42142 -26.60000 -18.11757 1.000 27.57700  ? 545 HOH   A O   1 
HETATM 1805 O O   . HOH   C 3 .   ? -17.79257 -15.26791 -13.18487 1.000 25.88529  ? 546 HOH   A O   1 
HETATM 1806 O O   . HOH   C 3 .   ? 20.79413  -16.83452 -20.02632 1.000 39.00662  ? 547 HOH   A O   1 
HETATM 1807 O O   . HOH   C 3 .   ? -7.56203  -13.56697 -40.99191 1.000 49.52783  ? 548 HOH   A O   1 
HETATM 1808 O O   . HOH   C 3 .   ? -3.47595  -13.12664 -20.69254 1.000 25.15642  ? 549 HOH   A O   1 
HETATM 1809 O O   . HOH   C 3 .   ? -1.25928  -4.42470  -33.83586 1.000 48.44669  ? 550 HOH   A O   1 
HETATM 1810 O O   . HOH   C 3 .   ? 3.99179   -9.19462  -20.36111 1.000 23.94198  ? 551 HOH   A O   1 
HETATM 1811 O O   . HOH   C 3 .   ? -7.64084  7.52396   -33.43614 1.000 37.01021  ? 552 HOH   A O   1 
HETATM 1812 O O   . HOH   C 3 .   ? -14.18665 -11.68753 0.44893   1.000 38.07811  ? 553 HOH   A O   1 
HETATM 1813 O O   . HOH   C 3 .   ? -16.35438 -9.11604  -14.21186 1.000 38.63094  ? 554 HOH   A O   1 
HETATM 1814 O O   . HOH   C 3 .   ? 10.89974  -11.40748 -4.74912  1.000 33.20833  ? 555 HOH   A O   1 
HETATM 1815 O O   . HOH   C 3 .   ? -7.14732  -22.49925 -36.72812 1.000 50.55597  ? 556 HOH   A O   1 
HETATM 1816 O O   . HOH   C 3 .   ? -0.07942  -16.57740 -3.49810  1.000 27.83532  ? 557 HOH   A O   1 
HETATM 1817 O O   . HOH   C 3 .   ? 1.49523   -3.15563  -24.35812 1.000 44.47433  ? 558 HOH   A O   1 
HETATM 1818 O O   . HOH   C 3 .   ? 7.64850   -4.63086  -22.21583 1.000 39.10510  ? 559 HOH   A O   1 
HETATM 1819 O O   . HOH   C 3 .   ? 4.84884   -1.05767  -6.17588  1.000 50.06520  ? 560 HOH   A O   1 
HETATM 1820 O O   . HOH   C 3 .   ? -4.10721  -3.42524  -15.41794 1.000 43.70510  ? 561 HOH   A O   1 
HETATM 1821 O O   . HOH   C 3 .   ? -19.94311 -12.71910 -16.42269 1.000 47.39671  ? 562 HOH   A O   1 
HETATM 1822 O O   . HOH   C 3 .   ? -3.47707  -32.89260 -10.83038 1.000 55.38725  ? 563 HOH   A O   1 
HETATM 1823 O O   . HOH   C 3 .   ? -17.285   -28.788   -17.214   1.000 38.51939  ? 564 HOH   A O   1 
HETATM 1824 O O   . HOH   C 3 .   ? -15.15278 -12.27295 -11.95879 1.000 30.81306  ? 565 HOH   A O   1 
HETATM 1825 O O   . HOH   C 3 .   ? 20.35055  -5.93410  -21.09141 1.000 43.74784  ? 566 HOH   A O   1 
HETATM 1826 O O   . HOH   C 3 .   ? -13.99665 -23.97366 -4.83923  1.000 35.00110  ? 567 HOH   A O   1 
HETATM 1827 O O   . HOH   C 3 .   ? -1.16848  -26.18131 -32.05842 1.000 45.92787  ? 568 HOH   A O   1 
HETATM 1828 O O   . HOH   C 3 .   ? 17.50217  -15.56573 -29.69113 1.000 47.78856  ? 569 HOH   A O   1 
HETATM 1829 O O   . HOH   C 3 .   ? -18.34644 -3.73432  -29.21978 1.000 47.86653  ? 570 HOH   A O   1 
HETATM 1830 O O   . HOH   C 3 .   ? 15.74785  -17.90770 -3.50053  1.000 39.89808  ? 571 HOH   A O   1 
HETATM 1831 O O   . HOH   C 3 .   ? -13.05224 -12.24459 -31.07214 1.000 28.07588  ? 572 HOH   A O   1 
HETATM 1832 O O   . HOH   C 3 .   ? 1.23269   -8.79104  -26.95395 1.000 39.14975  ? 573 HOH   A O   1 
HETATM 1833 O O   . HOH   C 3 .   ? -6.65717  -3.43395  -8.41610  1.000 53.10202  ? 574 HOH   A O   1 
HETATM 1834 O O   . HOH   C 3 .   ? 10.51739  -17.81414 -38.76234 1.000 44.66203  ? 575 HOH   A O   1 
HETATM 1835 O O   . HOH   C 3 .   ? 13.36730  -6.77623  -26.28485 1.000 24.11669  ? 576 HOH   A O   1 
HETATM 1836 O O   . HOH   C 3 .   ? -12.27469 -26.96368 -20.22889 1.000 29.27720  ? 577 HOH   A O   1 
HETATM 1837 O O   . HOH   C 3 .   ? -13.63890 -25.87509 -7.73373  1.000 30.47696  ? 578 HOH   A O   1 
HETATM 1838 O O   . HOH   C 3 .   ? 3.92536   -23.00401 -3.38657  1.000 39.12750  ? 579 HOH   A O   1 
HETATM 1839 O O   . HOH   C 3 .   ? 13.81890  -3.98906  -25.41392 1.000 22.57892  ? 580 HOH   A O   1 
HETATM 1840 O O   . HOH   C 3 .   ? -18.09466 -5.75049  -25.56541 1.000 34.23366  ? 581 HOH   A O   1 
HETATM 1841 O O   . HOH   C 3 .   ? 9.67029   -5.78610  -1.46685  1.000 48.96526  ? 582 HOH   A O   1 
HETATM 1842 O O   . HOH   C 3 .   ? -18.03009 -3.35850  -40.33631 1.000 52.60261  ? 583 HOH   A O   1 
HETATM 1843 O O   . HOH   C 3 .   ? 15.60073  -7.24056  -27.77681 1.000 36.61771  ? 584 HOH   A O   1 
HETATM 1844 O O   . HOH   C 3 .   ? -4.89401  -5.29518  -11.99358 1.000 43.82867  ? 585 HOH   A O   1 
HETATM 1845 O O   . HOH   C 3 .   ? -14.84957 -3.61381  -12.76841 1.000 47.16455  ? 586 HOH   A O   1 
HETATM 1846 O O   . HOH   C 3 .   ? -3.53448  -13.29334 -42.78790 1.000 47.57466  ? 587 HOH   A O   1 
HETATM 1847 O O   . HOH   C 3 .   ? -1.59497  -8.62113  -27.64538 1.000 29.57190  ? 588 HOH   A O   1 
HETATM 1848 O O   . HOH   C 3 .   ? 6.91908   -29.97087 -29.75921 1.000 54.89371  ? 589 HOH   A O   1 
HETATM 1849 O O   . HOH   C 3 .   ? -16.16968 -25.32747 -10.70365 1.000 37.93680  ? 590 HOH   A O   1 
HETATM 1850 O O   . HOH   C 3 .   ? -2.40691  -15.64372 -0.07859  1.000 40.24430  ? 591 HOH   A O   1 
HETATM 1851 O O   . HOH   C 3 .   ? 11.08941  -10.38036 -36.36182 1.000 52.23640  ? 592 HOH   A O   1 
HETATM 1852 O O   . HOH   C 3 .   ? -5.28013  -31.77730 -7.04377  1.000 49.94786  ? 593 HOH   A O   1 
HETATM 1853 O O   . HOH   C 3 .   ? 8.14069   -25.90745 -25.81860 1.000 47.06978  ? 594 HOH   A O   1 
HETATM 1854 O O   . HOH   C 3 .   ? 1.766     -18.337   0.116     1.000 37.38143  ? 595 HOH   A O   1 
HETATM 1855 O O   . HOH   C 3 .   ? -12.31317 -18.80522 -28.26127 1.000 53.00900  ? 596 HOH   A O   1 
HETATM 1856 O O   . HOH   C 3 .   ? 2.82678   -10.08298 -23.17343 1.000 30.33920  ? 597 HOH   A O   1 
HETATM 1857 O O   . HOH   C 3 .   ? -5.57743  -12.30150 -41.94226 1.000 42.03255  ? 598 HOH   A O   1 
HETATM 1858 O O   . HOH   C 3 .   ? 14.38225  -22.59408 -17.11202 1.000 39.79040  ? 599 HOH   A O   1 
HETATM 1859 O O   . HOH   C 3 .   ? -16.12284 -4.22508  -15.19847 1.000 54.03680  ? 600 HOH   A O   1 
HETATM 1860 O O   . HOH   C 3 .   ? 11.32914  -1.74698  -20.20945 1.000 44.32782  ? 601 HOH   A O   1 
HETATM 1861 O O   . HOH   C 3 .   ? 1.85210   -25.25170 -2.49798  1.000 55.56607  ? 602 HOH   A O   1 
HETATM 1862 O O   . HOH   C 3 .   ? -12.33543 -20.77202 -29.77534 1.000 47.95929  ? 603 HOH   A O   1 
HETATM 1863 O O   . HOH   C 3 .   ? -1.84372  -26.99028 -25.23113 1.000 47.76131  ? 604 HOH   A O   1 
HETATM 1864 O O   . HOH   C 3 .   ? 4.24483   -21.95704 -39.29556 1.000 52.61229  ? 605 HOH   A O   1 
HETATM 1865 O O   . HOH   C 3 .   ? 1.07700   -8.71123  -40.27986 1.000 51.69053  ? 606 HOH   A O   1 
HETATM 1866 O O   . HOH   C 3 .   ? 2.15120   -26.04910 -29.20623 1.000 41.58494  ? 607 HOH   A O   1 
HETATM 1867 O O   . HOH   C 3 .   ? 3.10434   -5.95585  -20.44608 1.000 45.85038  ? 608 HOH   A O   1 
HETATM 1868 O O   . HOH   C 3 .   ? -17.13141 -4.71605  -17.47753 1.000 41.94082  ? 609 HOH   A O   1 
HETATM 1869 O O   . HOH   C 3 .   ? 9.41637   -23.75831 -41.43317 1.000 58.17704  ? 610 HOH   A O   1 
HETATM 1870 O O   . HOH   C 3 .   ? 6.00892   -29.88044 -24.76656 1.000 49.51815  ? 611 HOH   A O   1 
HETATM 1871 O O   . HOH   C 3 .   ? 6.97649   1.94771   -12.48696 1.000 46.45556  ? 612 HOH   A O   1 
HETATM 1872 O O   . HOH   C 3 .   ? -0.45091  -1.24927  -22.88859 1.000 41.92262  ? 613 HOH   A O   1 
HETATM 1873 O O   . HOH   C 3 .   ? -13.98847 -0.62456  -13.55598 1.000 43.00528  ? 614 HOH   A O   1 
HETATM 1874 O O   . HOH   C 3 .   ? 12.10163  -27.63498 -23.01812 1.000 51.22718  ? 615 HOH   A O   1 
HETATM 1875 O O   . HOH   C 3 .   ? -18.199   -37.042   -19.948   1.000 40.99251  ? 616 HOH   A O   1 
HETATM 1876 O O   . HOH   C 3 .   ? 1.54017   -7.30662  -22.66809 1.000 50.11971  ? 617 HOH   A O   1 
HETATM 1877 O O   . HOH   C 3 .   ? 15.33334  -12.59417 -7.10709  1.000 46.55243  ? 618 HOH   A O   1 
HETATM 1878 O O   . HOH   C 3 .   ? -12.41138 -16.18888 -28.25336 1.000 39.32116  ? 619 HOH   A O   1 
HETATM 1879 O O   . HOH   C 3 .   ? -8.96581  -5.55481  -39.70022 1.000 45.47980  ? 620 HOH   A O   1 
HETATM 1880 O O   . HOH   C 3 .   ? -14.04746 -14.35144 -3.03743  1.000 36.66615  ? 621 HOH   A O   1 
HETATM 1881 O O   . HOH   C 3 .   ? 12.26663  -25.58790 -38.37365 1.000 37.91204  ? 622 HOH   A O   1 
HETATM 1882 O O   . HOH   C 3 .   ? 0.09129   -19.25060 -2.03549  1.000 42.32803  ? 623 HOH   A O   1 
HETATM 1883 O O   . HOH   C 3 .   ? -16.37659 -18.07386 -3.00225  1.000 55.38906  ? 624 HOH   A O   1 
HETATM 1884 O O   . HOH   C 3 .   ? -14.41482 -10.01627 -8.25541  1.000 42.79327  ? 625 HOH   A O   1 
HETATM 1885 O O   . HOH   C 3 .   ? -5.546    2.409     -26.088   1.000 42.90961  ? 626 HOH   A O   1 
HETATM 1886 O O   . HOH   C 3 .   ? -6.834    -23.109   -1.797    1.000 43.03529  ? 627 HOH   A O   1 
HETATM 1887 O O   . HOH   C 3 .   ? -9.75986  -26.11515 -20.85678 1.000 31.07560  ? 628 HOH   A O   1 
HETATM 1888 O O   . HOH   C 3 .   ? 19.11828  -8.39453  -17.64965 1.000 40.51835  ? 629 HOH   A O   1 
HETATM 1889 O O   . HOH   C 3 .   ? 5.483     1.797     -16.612   1.000 39.70192  ? 630 HOH   A O   1 
HETATM 1890 O O   . HOH   C 3 .   ? -18.65259 -11.74703 -21.07144 1.000 30.25537  ? 631 HOH   A O   1 
HETATM 1891 O O   . HOH   C 3 .   ? 7.82075   -13.97745 -38.25698 1.000 38.44344  ? 632 HOH   A O   1 
HETATM 1892 O O   . HOH   C 3 .   ? -2.38548  -0.81487  -30.93916 1.000 47.16646  ? 633 HOH   A O   1 
HETATM 1893 O O   . HOH   C 3 .   ? 3.73688   -9.21231  -39.04010 1.000 41.20447  ? 634 HOH   A O   1 
HETATM 1894 O O   . HOH   C 3 .   ? -4.08237  2.21084   -32.69206 1.000 55.00110  ? 635 HOH   A O   1 
HETATM 1895 O O   . HOH   C 3 .   ? -6.06219  3.85082   -34.50372 1.000 45.46583  ? 636 HOH   A O   1 
HETATM 1896 O O   . HOH   C 3 .   ? 11.07536  -1.24724  -17.44379 1.000 37.61818  ? 637 HOH   A O   1 
HETATM 1897 O O   . HOH   C 3 .   ? -17.016   -0.544    -17.750   1.000 40.84011  ? 638 HOH   A O   1 
HETATM 1898 O O   . HOH   C 3 .   ? -13.706   -24.890   -27.718   1.000 40.12975  ? 639 HOH   A O   1 
HETATM 1899 O O   . HOH   C 3 .   ? 2.392     -0.940    -25.954   1.000 43.38772  ? 640 HOH   A O   1 
HETATM 1900 O O   . HOH   C 3 .   ? 16.06419  0.45396   -9.69727  1.000 53.11613  ? 641 HOH   A O   1 
HETATM 1901 O O   . HOH   C 3 .   ? 5.86980   -13.11500 -39.73202 1.000 35.84211  ? 642 HOH   A O   1 
HETATM 1902 O O   . HOH   C 3 .   ? -3.41535  -26.94330 -2.87110  1.000 48.48864  ? 643 HOH   A O   1 
HETATM 1903 O O   . HOH   C 3 .   ? 6.21888   -7.01034  -35.85064 1.000 51.12910  ? 644 HOH   A O   1 
HETATM 1904 O O   . HOH   C 3 .   ? 10.01586  -29.33776 -23.80779 1.000 50.26399  ? 645 HOH   A O   1 
HETATM 1905 O O   . HOH   C 3 .   ? 6.73921   -21.48409 -2.65486  1.000 35.94554  ? 646 HOH   A O   1 
HETATM 1906 O O   . HOH   C 3 .   ? 7.86834   -28.98766 -28.05616 1.000 48.50050  ? 647 HOH   A O   1 
HETATM 1907 O O   . HOH   C 3 .   ? -10.484   -28.790   -23.540   1.000 52.06076  ? 648 HOH   A O   1 
HETATM 1908 O O   . HOH   C 3 .   ? -12.335   -9.627    1.359     1.000 49.94269  ? 649 HOH   A O   1 
HETATM 1909 O O   . HOH   C 3 .   ? 0.95104   -28.79751 -36.01419 1.000 58.99343  ? 650 HOH   A O   1 
HETATM 1910 O O   . HOH   C 3 .   ? -0.00000  -0.00000  -18.44494 0.50  36.36013  ? 651 HOH   A O   1 
HETATM 1911 O O   . HOH   C 3 .   ? 10.60775  -22.45376 -4.53872  1.000 43.64391  ? 652 HOH   A O   1 
HETATM 1912 O O   . HOH   C 3 .   ? 10.52306  -21.35910 -43.14677 1.000 50.28620  ? 653 HOH   A O   1 
HETATM 1913 O O   . HOH   C 3 .   ? -16.230   3.029     -26.352   1.000 41.57694  ? 654 HOH   A O   1 
HETATM 1914 O O   . HOH   C 3 .   ? 11.06618  -28.14554 -27.84130 1.000 43.29281  ? 655 HOH   A O   1 
HETATM 1915 O O   . HOH   C 3 .   ? -10.52768 -8.52930  -1.26004  1.000 46.22630  ? 656 HOH   A O   1 
HETATM 1916 O O   . HOH   C 3 .   ? 5.52406   -3.12343  -23.60502 1.000 42.93460  ? 657 HOH   A O   1 
HETATM 1917 O O   . HOH   C 3 .   ? 12.71577  -25.20639 -15.88160 1.000 43.38557  ? 658 HOH   A O   1 
HETATM 1918 O O   . HOH   C 3 .   ? -6.98359  -30.69630 -9.13876  1.000 37.75998  ? 659 HOH   A O   1 
HETATM 1919 O O   . HOH   C 3 .   ? -4.08519  -27.92970 -23.58127 1.000 46.75016  ? 660 HOH   A O   1 
HETATM 1920 O O   . HOH   C 3 .   ? 11.333    -30.303   -34.118   1.000 42.56674  ? 661 HOH   A O   1 
HETATM 1921 O O   . HOH   C 3 .   ? 0.68638   -12.04382 -23.79358 1.000 39.80154  ? 662 HOH   A O   1 
HETATM 1922 O O   . HOH   C 3 .   ? 3.04168   -2.28741  -20.43520 1.000 47.64364  ? 663 HOH   A O   1 
HETATM 1923 O O   . HOH   C 3 .   ? -1.11552  -2.58246  -31.59604 1.000 50.20020  ? 664 HOH   A O   1 
HETATM 1924 O O   . HOH   C 3 .   ? 17.52111  -17.48943 -5.19271  1.000 55.14168  ? 665 HOH   A O   1 
HETATM 1925 O O   . HOH   C 3 .   ? -1.868    -23.265   0.915     1.000 55.52572  ? 666 HOH   A O   1 
HETATM 1926 O O   . HOH   C 3 .   ? 9.69872   -12.74304 -37.16128 1.000 51.45420  ? 667 HOH   A O   1 
HETATM 1927 O O   . HOH   C 3 .   ? 1.75755   -5.91066  -36.57011 1.000 46.51335  ? 668 HOH   A O   1 
HETATM 1928 O O   . HOH   C 3 .   ? 14.19113  -27.11439 -17.15589 1.000 55.04376  ? 669 HOH   A O   1 
HETATM 1929 O O   . HOH   C 3 .   ? -14.94767 -9.71223  -11.47019 1.000 46.68113  ? 670 HOH   A O   1 
HETATM 1930 O O   . HOH   C 3 .   ? 9.67372   -25.25851 -14.67622 1.000 41.04388  ? 671 HOH   A O   1 
HETATM 1931 O O   . HOH   C 3 .   ? 6.475     -6.523    0.534     1.000 57.12210  ? 672 HOH   A O   1 
HETATM 1932 O O   . HOH   C 3 .   ? -16.13135 -13.51665 -3.73519  1.000 48.19370  ? 673 HOH   A O   1 
HETATM 1933 O O   . HOH   C 3 .   ? 4.156     -1.988    -28.136   1.000 40.41123  ? 674 HOH   A O   1 
HETATM 1934 O O   . HOH   C 3 .   ? -12.37816 -13.05324 -0.90711  1.000 31.25949  ? 675 HOH   A O   1 
HETATM 1935 O O   . HOH   C 3 .   ? -8.373    8.485     -38.541   1.000 48.80477  ? 676 HOH   A O   1 
HETATM 1936 O O   . HOH   C 3 .   ? 0.45824   -1.35953  -16.62251 1.000 38.83967  ? 677 HOH   A O   1 
HETATM 1937 O O   . HOH   C 3 .   ? -16.47365 -12.47458 -6.31280  1.000 51.65072  ? 678 HOH   A O   1 
HETATM 1938 O O   . HOH   C 3 .   ? -18.97553 -8.30235  -14.94562 1.000 53.13723  ? 679 HOH   A O   1 
HETATM 1939 O O   . HOH   C 3 .   ? -14.53451 -14.06093 -10.20736 1.000 31.93949  ? 680 HOH   A O   1 
HETATM 1940 O O   . HOH   C 3 .   ? -17.01064 -15.68918 -10.36425 1.000 39.28713  ? 681 HOH   A O   1 
HETATM 1941 O O   . HOH   C 3 .   ? 14.73368  -13.04378 -2.85355  1.000 42.23375  ? 682 HOH   A O   1 
HETATM 1942 O O   . HOH   C 3 .   ? -10.578   -11.839   1.978     1.000 41.15265  ? 683 HOH   A O   1 
HETATM 1943 O O   . HOH   C 3 .   ? -19.61733 -5.97787  -21.41872 1.000 43.04463  ? 684 HOH   A O   1 
HETATM 1944 O O   . HOH   C 3 .   ? 13.66903  -11.69622 -5.07477  1.000 40.05326  ? 685 HOH   A O   1 
HETATM 1945 O O   . HOH   C 3 .   ? -2.38486  -26.82896 -28.11140 1.000 54.11214  ? 686 HOH   A O   1 
HETATM 1946 O O   . HOH   C 3 .   ? -8.84324  -10.58452 -0.00791  1.000 52.04591  ? 687 HOH   A O   1 
HETATM 1947 O O   . HOH   C 3 .   ? -18.42966 -1.75192  -30.42828 1.000 50.30849  ? 688 HOH   A O   1 
HETATM 1948 O O   . HOH   C 3 .   ? 6.06571   -8.16143  -39.92621 1.000 51.43988  ? 689 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   ? 0.62284 0.90660 0.51298 -0.10747 -0.03984 -0.29799 16  GLU A N   
2    C CA  . GLU A 9   ? 0.74897 0.99550 0.62724 -0.06676 -0.04207 -0.27689 16  GLU A CA  
3    C C   . GLU A 9   ? 0.60384 0.83560 0.50150 -0.04861 -0.04462 -0.25117 16  GLU A C   
4    O O   . GLU A 9   ? 0.62213 0.91955 0.54215 -0.03183 -0.05378 -0.23512 16  GLU A O   
5    C CB  . GLU A 9   ? 0.90946 1.22802 0.78626 -0.03289 -0.05179 -0.26912 16  GLU A CB  
6    C CG  . GLU A 9   ? 0.99323 1.28811 0.86324 0.01192  -0.05182 -0.24224 16  GLU A CG  
7    C CD  . GLU A 9   ? 1.12354 1.33084 0.96650 0.01413  -0.03962 -0.24781 16  GLU A CD  
8    O OE1 . GLU A 9   ? 1.23301 1.43741 1.05276 0.01899  -0.03630 -0.25873 16  GLU A OE1 
9    O OE2 . GLU A 9   ? 1.03997 1.18345 0.88522 0.01369  -0.03196 -0.24059 16  GLU A OE2 
10   N N   . VAL A 10  ? 0.47075 0.61567 0.35786 -0.04854 -0.03451 -0.24678 17  VAL A N   
11   C CA  . VAL A 10  ? 0.42639 0.55037 0.33147 -0.03762 -0.03529 -0.22746 17  VAL A CA  
12   C C   . VAL A 10  ? 0.48130 0.57662 0.38160 0.00219  -0.03347 -0.20921 17  VAL A C   
13   O O   . VAL A 10  ? 0.50477 0.54341 0.38627 0.01001  -0.02221 -0.21218 17  VAL A O   
14   C CB  . VAL A 10  ? 0.51453 0.56577 0.41606 -0.06694 -0.02196 -0.23318 17  VAL A CB  
15   C CG1 . VAL A 10  ? 0.47145 0.51129 0.39399 -0.05598 -0.02411 -0.21405 17  VAL A CG1 
16   C CG2 . VAL A 10  ? 0.70078 0.77769 0.60613 -0.10732 -0.01923 -0.25070 17  VAL A CG2 
17   N N   . GLU A 11  ? 0.35495 0.48243 0.27509 0.02802  -0.03984 -0.18004 18  GLU A N   
18   C CA  . GLU A 11  ? 0.33215 0.43162 0.25643 0.05972  -0.03355 -0.15185 18  GLU A CA  
19   C C   . GLU A 11  ? 0.32289 0.38347 0.26767 0.05716  -0.02973 -0.13267 18  GLU A C   
20   O O   . GLU A 11  ? 0.28706 0.36725 0.24733 0.04836  -0.03496 -0.12648 18  GLU A O   
21   C CB  . GLU A 11  ? 0.31400 0.46464 0.23772 0.08861  -0.03671 -0.13361 18  GLU A CB  
22   C CG  . GLU A 11  ? 0.34567 0.53890 0.24482 0.10132  -0.03955 -0.14715 18  GLU A CG  
23   C CD  . GLU A 11  ? 0.54334 0.78016 0.43443 0.13702  -0.03803 -0.12344 18  GLU A CD  
24   O OE1 . GLU A 11  ? 0.49493 0.78293 0.39031 0.14309  -0.04498 -0.11831 18  GLU A OE1 
25   O OE2 . GLU A 11  ? 0.53140 0.75019 0.40891 0.16110  -0.02703 -0.10869 18  GLU A OE2 
26   N N   . THR A 12  ? 0.31348 0.32695 0.25743 0.06719  -0.02065 -0.12351 19  THR A N   
27   C CA  . THR A 12  ? 0.29416 0.28133 0.25536 0.06822  -0.01777 -0.10610 19  THR A CA  
28   C C   . THR A 12  ? 0.29208 0.29250 0.26646 0.08822  -0.01440 -0.08516 19  THR A C   
29   O O   . THR A 12  ? 0.27948 0.28066 0.24671 0.10361  -0.00801 -0.08319 19  THR A O   
30   C CB  . THR A 12  ? 0.32909 0.26155 0.27755 0.06731  -0.00807 -0.11057 19  THR A CB  
31   O OG1 . THR A 12  ? 0.37149 0.27926 0.29994 0.04312  -0.00455 -0.13408 19  THR A OG1 
32   C CG2 . THR A 12  ? 0.31284 0.22970 0.27649 0.07027  -0.00684 -0.09275 19  THR A CG2 
33   N N   . PHE A 13  ? 0.24213 0.25137 0.23378 0.08497  -0.01616 -0.07159 20  PHE A N   
34   C CA  . PHE A 13  ? 0.23303 0.25094 0.23511 0.09415  -0.00917 -0.05597 20  PHE A CA  
35   C C   . PHE A 13  ? 0.31439 0.32415 0.33335 0.08789  -0.00883 -0.04883 20  PHE A C   
36   O O   . PHE A 13  ? 0.24953 0.24889 0.27184 0.07858  -0.01474 -0.05042 20  PHE A O   
37   C CB  . PHE A 13  ? 0.22528 0.25984 0.22484 0.09673  -0.00727 -0.04760 20  PHE A CB  
38   C CG  . PHE A 13  ? 0.25045 0.30768 0.23124 0.10974  -0.00806 -0.05109 20  PHE A CG  
39   C CD1 . PHE A 13  ? 0.27240 0.35506 0.24861 0.10318  -0.01961 -0.06410 20  PHE A CD1 
40   C CD2 . PHE A 13  ? 0.32011 0.37968 0.28659 0.12796  0.00407  -0.04170 20  PHE A CD2 
41   C CE1 . PHE A 13  ? 0.27651 0.39732 0.23527 0.11682  -0.02237 -0.06899 20  PHE A CE1 
42   C CE2 . PHE A 13  ? 0.35240 0.43952 0.29736 0.14566  0.00323  -0.04276 20  PHE A CE2 
43   C CZ  . PHE A 13  ? 0.30486 0.42799 0.24655 0.14121  -0.01166 -0.05699 20  PHE A CZ  
44   N N   . ALA A 14  ? 0.21949 0.23990 0.24834 0.09160  -0.00079 -0.04169 21  ALA A N   
45   C CA  . ALA A 14  ? 0.19709 0.22774 0.24280 0.08377  -0.00107 -0.03698 21  ALA A CA  
46   C C   . ALA A 14  ? 0.21544 0.24672 0.26419 0.07052  0.00375  -0.03319 21  ALA A C   
47   O O   . ALA A 14  ? 0.21441 0.24011 0.25373 0.07170  0.01525  -0.03000 21  ALA A O   
48   C CB  . ALA A 14  ? 0.21741 0.27334 0.27438 0.09007  0.00591  -0.03547 21  ALA A CB  
49   N N   . PHE A 15  ? 0.17987 0.21185 0.23602 0.06063  -0.00216 -0.03252 22  PHE A N   
50   C CA  . PHE A 15  ? 0.22114 0.24987 0.27745 0.04733  0.00575  -0.03099 22  PHE A CA  
51   C C   . PHE A 15  ? 0.25219 0.29530 0.31563 0.03573  0.01955  -0.03418 22  PHE A C   
52   O O   . PHE A 15  ? 0.18320 0.25719 0.26088 0.03643  0.01680  -0.03735 22  PHE A O   
53   C CB  . PHE A 15  ? 0.18975 0.22189 0.25231 0.03869  -0.00302 -0.03138 22  PHE A CB  
54   C CG  . PHE A 15  ? 0.19216 0.21085 0.24794 0.04228  -0.01134 -0.02919 22  PHE A CG  
55   C CD1 . PHE A 15  ? 0.22856 0.23871 0.27373 0.04475  -0.00644 -0.02641 22  PHE A CD1 
56   C CD2 . PHE A 15  ? 0.18302 0.19913 0.24064 0.04405  -0.02094 -0.02934 22  PHE A CD2 
57   C CE1 . PHE A 15  ? 0.22157 0.23579 0.26475 0.04584  -0.01409 -0.02628 22  PHE A CE1 
58   C CE2 . PHE A 15  ? 0.19996 0.20719 0.25272 0.04012  -0.02540 -0.03011 22  PHE A CE2 
59   C CZ  . PHE A 15  ? 0.21389 0.22776 0.26283 0.03937  -0.02355 -0.02985 22  PHE A CZ  
60   N N   . GLN A 16  ? 0.22707 0.24817 0.27818 0.02500  0.03748  -0.03364 23  GLN A N   
61   C CA  . GLN A 16  ? 0.29671 0.32863 0.35388 0.00121  0.05415  -0.04196 23  GLN A CA  
62   C C   . GLN A 16  ? 0.23246 0.30317 0.30886 -0.01418 0.04207  -0.05156 23  GLN A C   
63   O O   . GLN A 16  ? 0.22922 0.29643 0.30483 -0.00956 0.02853  -0.04944 23  GLN A O   
64   C CB  . GLN A 16  ? 0.38498 0.36864 0.41652 -0.01045 0.08055  -0.04082 23  GLN A CB  
65   C CG  . GLN A 16  ? 0.40461 0.35297 0.41102 0.00871  0.09801  -0.02849 23  GLN A CG  
66   C CD  . GLN A 16  ? 0.61241 0.50093 0.58363 0.00599  0.12822  -0.02275 23  GLN A CD  
67   O OE1 . GLN A 16  ? 0.48968 0.35509 0.44147 0.02788  0.12691  -0.01216 23  GLN A OE1 
68   N NE2 . GLN A 16  ? 0.54296 0.40562 0.50322 -0.02088 0.15873  -0.03010 23  GLN A NE2 
69   N N   . ALA A 17  ? 0.22505 0.34108 0.31863 -0.03180 0.04750  -0.06224 24  ALA A N   
70   C CA  . ALA A 17  ? 0.21742 0.39005 0.32946 -0.04187 0.03442  -0.07161 24  ALA A CA  
71   C C   . ALA A 17  ? 0.21431 0.36681 0.31532 -0.06018 0.03575  -0.07865 24  ALA A C   
72   O O   . ALA A 17  ? 0.22749 0.40230 0.33291 -0.05186 0.01833  -0.07697 24  ALA A O   
73   C CB  . ALA A 17  ? 0.21266 0.44958 0.34504 -0.06422 0.04384  -0.08606 24  ALA A CB  
74   N N   . GLU A 18  ? 0.25678 0.36045 0.33797 -0.08222 0.05944  -0.08513 25  GLU A N   
75   C CA  . GLU A 18  ? 0.30139 0.37922 0.36665 -0.09946 0.06522  -0.09357 25  GLU A CA  
76   C C   . GLU A 18  ? 0.31543 0.36505 0.37106 -0.07201 0.04976  -0.07818 25  GLU A C   
77   O O   . GLU A 18  ? 0.27017 0.32739 0.32315 -0.07768 0.04207  -0.08288 25  GLU A O   
78   C CB  . GLU A 18  ? 0.38298 0.39673 0.41921 -0.12351 0.10093  -0.10129 25  GLU A CB  
79   C CG  . GLU A 18  ? 0.45474 0.49325 0.49817 -0.16363 0.12274  -0.12206 25  GLU A CG  
80   C CD  . GLU A 18  ? 0.57696 0.62147 0.62851 -0.15363 0.13085  -0.11278 25  GLU A CD  
81   O OE1 . GLU A 18  ? 0.43239 0.46502 0.48378 -0.11468 0.11717  -0.09168 25  GLU A OE1 
82   O OE2 . GLU A 18  ? 0.64545 0.70916 0.70271 -0.18779 0.15252  -0.12876 25  GLU A OE2 
83   N N   . ILE A 19  ? 0.27849 0.30229 0.32891 -0.04443 0.04551  -0.06168 26  ILE A N   
84   C CA  . ILE A 19  ? 0.25311 0.26077 0.29744 -0.02380 0.03233  -0.05011 26  ILE A CA  
85   C C   . ILE A 19  ? 0.21700 0.26236 0.27916 -0.01444 0.00878  -0.04737 26  ILE A C   
86   O O   . ILE A 19  ? 0.22802 0.27132 0.28738 -0.01096 0.00008  -0.04394 26  ILE A O   
87   C CB  . ILE A 19  ? 0.27119 0.25184 0.30355 -0.00088 0.03589  -0.03742 26  ILE A CB  
88   C CG1 . ILE A 19  ? 0.34183 0.27488 0.34476 0.00199  0.06151  -0.03300 26  ILE A CG1 
89   C CG2 . ILE A 19  ? 0.25214 0.24041 0.28837 0.01546  0.01773  -0.02986 26  ILE A CG2 
90   C CD1 . ILE A 19  ? 0.46870 0.37636 0.45893 -0.01889 0.08888  -0.04108 26  ILE A CD1 
91   N N   . ALA A 20  ? 0.17376 0.25047 0.25045 -0.00758 0.00150  -0.04725 27  ALA A N   
92   C CA  . ALA A 20  ? 0.23062 0.33559 0.31581 0.00645  -0.01470 -0.04220 27  ALA A CA  
93   C C   . ALA A 20  ? 0.24347 0.38269 0.33168 -0.00457 -0.01949 -0.04851 27  ALA A C   
94   O O   . ALA A 20  ? 0.23679 0.37808 0.32036 0.00707  -0.02929 -0.04078 27  ALA A O   
95   C CB  . ALA A 20  ? 0.19700 0.33081 0.29263 0.02051  -0.01710 -0.04044 27  ALA A CB  
96   N N   . GLN A 21  ? 0.25114 0.41730 0.34426 -0.02933 -0.01054 -0.06403 28  GLN A N   
97   C CA  . GLN A 21  ? 0.25246 0.45904 0.34636 -0.04425 -0.01508 -0.07527 28  GLN A CA  
98   C C   . GLN A 21  ? 0.24706 0.41135 0.32283 -0.04829 -0.01321 -0.07360 28  GLN A C   
99   O O   . GLN A 21  ? 0.26292 0.45157 0.33532 -0.04418 -0.02333 -0.07278 28  GLN A O   
100  C CB  . GLN A 21  ? 0.29247 0.53502 0.39326 -0.07983 -0.00195 -0.09879 28  GLN A CB  
101  C CG  . GLN A 21  ? 0.61453 0.91648 0.73713 -0.07944 -0.00245 -0.10295 28  GLN A CG  
102  C CD  . GLN A 21  ? 0.70789 1.01032 0.83113 -0.11917 0.02071  -0.12373 28  GLN A CD  
103  O OE1 . GLN A 21  ? 0.54473 0.81827 0.64771 -0.14769 0.03555  -0.13863 28  GLN A OE1 
104  N NE2 . GLN A 21  ? 0.50220 0.82398 0.63884 -0.11664 0.02722  -0.12202 28  GLN A NE2 
105  N N   . LEU A 22  ? 0.24003 0.34490 0.30160 -0.05250 0.00101  -0.07166 29  LEU A N   
106  C CA  . LEU A 22  ? 0.25225 0.32071 0.29611 -0.05113 0.00464  -0.06831 29  LEU A CA  
107  C C   . LEU A 22  ? 0.31081 0.38190 0.35796 -0.02839 -0.01143 -0.05202 29  LEU A C   
108  O O   . LEU A 22  ? 0.24898 0.32516 0.28896 -0.02818 -0.01579 -0.05086 29  LEU A O   
109  C CB  . LEU A 22  ? 0.30798 0.31888 0.33359 -0.04917 0.02423  -0.06470 29  LEU A CB  
110  C CG  . LEU A 22  ? 0.34001 0.31831 0.34742 -0.03845 0.02896  -0.05723 29  LEU A CG  
111  C CD1 . LEU A 22  ? 0.32916 0.29874 0.31925 -0.05843 0.03959  -0.07215 29  LEU A CD1 
112  C CD2 . LEU A 22  ? 0.36402 0.29927 0.35393 -0.02212 0.04556  -0.04704 29  LEU A CD2 
113  N N   . MET A 23  ? 0.23798 0.30255 0.29288 -0.01154 -0.01767 -0.04076 30  MET A N   
114  C CA  . MET A 23  ? 0.25777 0.31553 0.31165 0.00289  -0.02702 -0.02839 30  MET A CA  
115  C C   . MET A 23  ? 0.22993 0.31690 0.28439 0.01169  -0.03621 -0.02372 30  MET A C   
116  O O   . MET A 23  ? 0.25465 0.33353 0.30051 0.01812  -0.03875 -0.01486 30  MET A O   
117  C CB  . MET A 23  ? 0.26010 0.29931 0.31698 0.01325  -0.02814 -0.02247 30  MET A CB  
118  C CG  . MET A 23  ? 0.30846 0.33216 0.36289 0.01191  -0.01953 -0.02546 30  MET A CG  
119  S SD  . MET A 23  ? 0.26528 0.28158 0.32171 0.02273  -0.02247 -0.02347 30  MET A SD  
120  C CE  . MET A 23  ? 0.24611 0.25564 0.30099 0.02138  -0.02908 -0.02015 30  MET A CE  
121  N N   . SER A 24  ? 0.21191 0.33766 0.27460 0.01450  -0.03960 -0.02826 31  SER A N   
122  C CA  . SER A 24  ? 0.17174 0.33828 0.23132 0.03000  -0.04780 -0.02204 31  SER A CA  
123  C C   . SER A 24  ? 0.25431 0.44287 0.30585 0.01862  -0.04999 -0.02863 31  SER A C   
124  O O   . SER A 24  ? 0.28880 0.48572 0.32795 0.03500  -0.05455 -0.01684 31  SER A O   
125  C CB  . SER A 24  ? 0.26319 0.48639 0.33589 0.03629  -0.05114 -0.02743 31  SER A CB  
126  O OG  . SER A 24  ? 0.46978 0.67211 0.54443 0.05468  -0.04887 -0.01828 31  SER A OG  
127  N N   . LEU A 25  ? 0.23447 0.42736 0.28773 -0.00891 -0.04369 -0.04754 32  LEU A N   
128  C CA  . LEU A 25  ? 0.21585 0.42535 0.25704 -0.02266 -0.04352 -0.05812 32  LEU A CA  
129  C C   . LEU A 25  ? 0.29060 0.45539 0.31719 -0.01412 -0.04120 -0.04523 32  LEU A C   
130  O O   . LEU A 25  ? 0.25873 0.44145 0.27324 -0.00822 -0.04564 -0.04175 32  LEU A O   
131  C CB  . LEU A 25  ? 0.32081 0.52516 0.35951 -0.05706 -0.03011 -0.08324 32  LEU A CB  
132  C CG  . LEU A 25  ? 0.47990 0.69188 0.50068 -0.07949 -0.02444 -0.10220 32  LEU A CG  
133  C CD1 . LEU A 25  ? 0.46105 0.68950 0.48154 -0.11822 -0.01068 -0.13240 32  LEU A CD1 
134  C CD2 . LEU A 25  ? 0.41059 0.55501 0.41117 -0.07656 -0.01275 -0.09563 32  LEU A CD2 
135  N N   . ILE A 26  ? 0.23763 0.35233 0.26505 -0.01272 -0.03390 -0.03830 33  ILE A N   
136  C CA  . ILE A 26  ? 0.29639 0.38122 0.31444 -0.00653 -0.03084 -0.02739 33  ILE A CA  
137  C C   . ILE A 26  ? 0.29775 0.38567 0.31277 0.01093  -0.03723 -0.00997 33  ILE A C   
138  O O   . ILE A 26  ? 0.31039 0.39471 0.31365 0.01440  -0.03563 -0.00249 33  ILE A O   
139  C CB  . ILE A 26  ? 0.24759 0.29723 0.26940 -0.00634 -0.02295 -0.02460 33  ILE A CB  
140  C CG1 . ILE A 26  ? 0.29539 0.32590 0.30676 -0.01740 -0.00906 -0.03683 33  ILE A CG1 
141  C CG2 . ILE A 26  ? 0.27091 0.30779 0.29039 0.00041  -0.02192 -0.01275 33  ILE A CG2 
142  C CD1 . ILE A 26  ? 0.33107 0.33624 0.34335 -0.01039 -0.00055 -0.03287 33  ILE A CD1 
143  N N   . ILE A 27  ? 0.24392 0.33276 0.26479 0.02336  -0.04089 -0.00261 34  ILE A N   
144  C CA  . ILE A 27  ? 0.30184 0.37265 0.31116 0.04104  -0.03928 0.01518  34  ILE A CA  
145  C C   . ILE A 27  ? 0.36242 0.46699 0.35665 0.05912  -0.04337 0.02383  34  ILE A C   
146  O O   . ILE A 27  ? 0.38251 0.46826 0.35769 0.07169  -0.03759 0.03972  34  ILE A O   
147  C CB  . ILE A 27  ? 0.35319 0.40316 0.36645 0.05049  -0.03742 0.01913  34  ILE A CB  
148  C CG1 . ILE A 27  ? 0.28841 0.30723 0.31071 0.03476  -0.03299 0.01277  34  ILE A CG1 
149  C CG2 . ILE A 27  ? 0.35078 0.37633 0.34247 0.07372  -0.03060 0.03750  34  ILE A CG2 
150  C CD1 . ILE A 27  ? 0.32090 0.32773 0.34868 0.03919  -0.03255 0.00936  34  ILE A CD1 
151  N N   . ASN A 28  ? 0.27469 0.43465 0.27557 0.06020  -0.05194 0.01312  35  ASN A N   
152  C CA  . ASN A 28  ? 0.27574 0.48695 0.26298 0.08441  -0.05810 0.02186  35  ASN A CA  
153  C C   . ASN A 28  ? 0.39915 0.65374 0.37823 0.07346  -0.06338 0.01047  35  ASN A C   
154  O O   . ASN A 28  ? 0.40738 0.70159 0.36838 0.09741  -0.06766 0.02166  35  ASN A O   
155  C CB  . ASN A 28  ? 0.34637 0.61331 0.34674 0.09611  -0.06517 0.01674  35  ASN A CB  
156  C CG  . ASN A 28  ? 0.47193 0.69757 0.47204 0.11582  -0.05861 0.03065  35  ASN A CG  
157  O OD1 . ASN A 28  ? 0.48017 0.64732 0.45983 0.13283  -0.04847 0.04959  35  ASN A OD1 
158  N ND2 . ASN A 28  ? 0.50017 0.75192 0.52029 0.11074  -0.06139 0.01960  35  ASN A ND2 
159  N N   . THR A 29  ? 0.28626 0.53268 0.27286 0.04115  -0.06106 -0.01089 36  THR A N   
160  C CA  . THR A 29  ? 0.27179 0.55321 0.24574 0.02774  -0.06335 -0.02601 36  THR A CA  
161  C C   . THR A 29  ? 0.32057 0.57310 0.27275 0.04142  -0.05869 -0.00839 36  THR A C   
162  O O   . THR A 29  ? 0.34438 0.53824 0.29712 0.03963  -0.04934 0.00248  36  THR A O   
163  C CB  . THR A 29  ? 0.33813 0.59937 0.31712 -0.00881 -0.05496 -0.05288 36  THR A CB  
164  O OG1 . THR A 29  ? 0.30049 0.58667 0.29757 -0.02512 -0.05534 -0.06949 36  THR A OG1 
165  C CG2 . THR A 29  ? 0.34200 0.63060 0.30173 -0.02567 -0.05389 -0.07250 36  THR A CG2 
166  N N   . PHE A 30  ? 0.27514 0.57620 0.20793 0.05493  -0.06461 -0.00597 37  PHE A N   
167  C CA  . PHE A 30  ? 0.30839 0.58409 0.21793 0.06481  -0.05778 0.00873  37  PHE A CA  
168  C C   . PHE A 30  ? 0.31733 0.56777 0.22514 0.03580  -0.05045 -0.01127 37  PHE A C   
169  O O   . PHE A 30  ? 0.31812 0.60202 0.22154 0.01500  -0.05313 -0.03833 37  PHE A O   
170  C CB  . PHE A 30  ? 0.32474 0.65987 0.21047 0.08988  -0.06428 0.01698  37  PHE A CB  
171  C CG  . PHE A 30  ? 0.38095 0.69108 0.23798 0.10218  -0.05573 0.03444  37  PHE A CG  
172  C CD1 . PHE A 30  ? 0.43806 0.68869 0.28379 0.12185  -0.04184 0.06559  37  PHE A CD1 
173  C CD2 . PHE A 30  ? 0.36159 0.69631 0.20643 0.08838  -0.05590 0.01689  37  PHE A CD2 
174  C CE1 . PHE A 30  ? 0.39904 0.62455 0.22024 0.12923  -0.02971 0.08155  37  PHE A CE1 
175  C CE2 . PHE A 30  ? 0.45251 0.76463 0.27146 0.10016  -0.04624 0.03346  37  PHE A CE2 
176  C CZ  . PHE A 30  ? 0.41151 0.67219 0.21843 0.12111  -0.03328 0.06715  37  PHE A CZ  
177  N N   . TYR A 31  ? 0.28920 0.48240 0.19776 0.03435  -0.03887 0.00090  38  TYR A N   
178  C CA  . TYR A 31  ? 0.28575 0.45117 0.19141 0.01511  -0.02883 -0.01390 38  TYR A CA  
179  C C   . TYR A 31  ? 0.28773 0.41719 0.19093 0.02339  -0.01800 0.00639  38  TYR A C   
180  O O   . TYR A 31  ? 0.30294 0.40539 0.22318 0.02400  -0.01447 0.01757  38  TYR A O   
181  C CB  . TYR A 31  ? 0.29024 0.43288 0.21344 -0.00284 -0.02513 -0.03000 38  TYR A CB  
182  C CG  . TYR A 31  ? 0.35386 0.45780 0.26817 -0.01292 -0.00994 -0.03936 38  TYR A CG  
183  C CD1 . TYR A 31  ? 0.40900 0.51283 0.29947 -0.02650 -0.00182 -0.06088 38  TYR A CD1 
184  C CD2 . TYR A 31  ? 0.40804 0.47835 0.33410 -0.00683 -0.00204 -0.02744 38  TYR A CD2 
185  C CE1 . TYR A 31  ? 0.49764 0.55737 0.37232 -0.02904 0.01669  -0.06710 38  TYR A CE1 
186  C CE2 . TYR A 31  ? 0.37225 0.41336 0.28648 -0.00672 0.01349  -0.03237 38  TYR A CE2 
187  C CZ  . TYR A 31  ? 0.52782 0.55805 0.41451 -0.01545 0.02422  -0.05056 38  TYR A CZ  
188  O OH  . TYR A 31  ? 0.66901 0.66138 0.53674 -0.00906 0.04414  -0.05323 38  TYR A OH  
189  N N   . SER A 32  ? 0.31291 0.44783 0.19489 0.02745  -0.01205 0.00906  39  SER A N   
190  C CA  . SER A 32  ? 0.31596 0.42912 0.19497 0.03488  -0.00060 0.03001  39  SER A CA  
191  C C   . SER A 32  ? 0.37976 0.47004 0.27257 0.02558  0.01034  0.02645  39  SER A C   
192  O O   . SER A 32  ? 0.39253 0.47324 0.29444 0.02581  0.01898  0.04141  39  SER A O   
193  C CB  . SER A 32  ? 0.34640 0.47829 0.19577 0.04562  0.00322  0.03628  39  SER A CB  
194  O OG  . SER A 32  ? 0.36448 0.52537 0.19779 0.06278  -0.00586 0.04553  39  SER A OG  
195  N N   . ASN A 33  ? 0.33562 0.41855 0.22761 0.01811  0.01280  0.00723  40  ASN A N   
196  C CA  . ASN A 33  ? 0.33452 0.40103 0.23032 0.01992  0.02600  0.00661  40  ASN A CA  
197  C C   . ASN A 33  ? 0.27224 0.33115 0.19512 0.01845  0.02431  0.01059  40  ASN A C   
198  O O   . ASN A 33  ? 0.28178 0.32548 0.20540 0.02012  0.02966  0.00188  40  ASN A O   
199  C CB  . ASN A 33  ? 0.40168 0.45070 0.27251 0.01744  0.03590  -0.01377 40  ASN A CB  
200  C CG  . ASN A 33  ? 0.48342 0.51315 0.34869 0.02986  0.05366  -0.01107 40  ASN A CG  
201  O OD1 . ASN A 33  ? 0.44954 0.49695 0.32341 0.04053  0.05877  0.00432  40  ASN A OD1 
202  N ND2 . ASN A 33  ? 0.45464 0.44894 0.30196 0.02969  0.06624  -0.02587 40  ASN A ND2 
203  N N   . LYS A 34  ? 0.32415 0.28365 0.24916 0.00409  -0.08683 -0.00401 41  LYS A N   
204  C CA  . LYS A 34  ? 0.26993 0.27398 0.24483 0.00619  -0.06493 -0.00085 41  LYS A CA  
205  C C   . LYS A 34  ? 0.32005 0.30613 0.28369 0.01319  -0.04683 -0.01628 41  LYS A C   
206  O O   . LYS A 34  ? 0.25290 0.26531 0.24839 0.01072  -0.03661 -0.01454 41  LYS A O   
207  C CB  . LYS A 34  ? 0.26547 0.30127 0.26611 0.02108  -0.04311 0.00411  41  LYS A CB  
208  C CG  . LYS A 34  ? 0.26400 0.33310 0.29076 0.01795  -0.05587 0.02443  41  LYS A CG  
209  C CD  . LYS A 34  ? 0.29620 0.38358 0.33687 0.03730  -0.03253 0.02673  41  LYS A CD  
210  C CE  . LYS A 34  ? 0.23327 0.35983 0.30468 0.03964  -0.04096 0.05003  41  LYS A CE  
211  N NZ  . LYS A 34  ? 0.20055 0.37521 0.31824 0.03685  -0.03926 0.06893  41  LYS A NZ  
212  N N   . GLU A 35  ? 0.29199 0.23506 0.21024 0.02422  -0.04176 -0.02899 42  GLU A N   
213  C CA  . GLU A 35  ? 0.30459 0.23984 0.21996 0.03456  -0.02115 -0.03886 42  GLU A CA  
214  C C   . GLU A 35  ? 0.32576 0.25663 0.24712 0.02330  -0.03067 -0.04088 42  GLU A C   
215  O O   . GLU A 35  ? 0.32962 0.26783 0.26353 0.02922  -0.01450 -0.04557 42  GLU A O   
216  C CB  . GLU A 35  ? 0.34264 0.23567 0.20745 0.05312  -0.01180 -0.04651 42  GLU A CB  
217  C CG  . GLU A 35  ? 0.44063 0.27703 0.24652 0.05243  -0.03421 -0.05277 42  GLU A CG  
218  C CD  . GLU A 35  ? 0.65328 0.44390 0.39836 0.07843  -0.02135 -0.05845 42  GLU A CD  
219  O OE1 . GLU A 35  ? 0.58501 0.38619 0.32893 0.08976  -0.00739 -0.05372 42  GLU A OE1 
220  O OE2 . GLU A 35  ? 0.71779 0.45992 0.41324 0.08999  -0.02381 -0.06618 42  GLU A OE2 
221  N N   . ILE A 36  ? 0.32224 0.24153 0.23666 0.00548  -0.05872 -0.03498 43  ILE A N   
222  C CA  . ILE A 36  ? 0.30784 0.21894 0.22602 -0.00692 -0.06965 -0.03458 43  ILE A CA  
223  C C   . ILE A 36  ? 0.25642 0.21804 0.22773 -0.01096 -0.05500 -0.02747 43  ILE A C   
224  O O   . ILE A 36  ? 0.26152 0.21875 0.23696 -0.01765 -0.05801 -0.02765 43  ILE A O   
225  C CB  . ILE A 36  ? 0.38439 0.27210 0.28745 -0.03041 -0.10808 -0.02479 43  ILE A CB  
226  C CG1 . ILE A 36  ? 0.34680 0.28678 0.29849 -0.04547 -0.11925 -0.00341 43  ILE A CG1 
227  C CG2 . ILE A 36  ? 0.49771 0.31513 0.32829 -0.02455 -0.12662 -0.03558 43  ILE A CG2 
228  C CD1 . ILE A 36  ? 0.38426 0.37288 0.39071 -0.06108 -0.12074 0.01526  43  ILE A CD1 
229  N N   . PHE A 37  ? 0.21689 0.22011 0.22206 -0.00496 -0.03948 -0.02127 44  PHE A N   
230  C CA  . PHE A 37  ? 0.21090 0.25001 0.25145 -0.00323 -0.02413 -0.01672 44  PHE A CA  
231  C C   . PHE A 37  ? 0.25444 0.27822 0.28574 0.00411  -0.01096 -0.02956 44  PHE A C   
232  O O   . PHE A 37  ? 0.21287 0.24838 0.25851 0.00013  -0.00858 -0.02716 44  PHE A O   
233  C CB  . PHE A 37  ? 0.16150 0.22984 0.22260 0.00867  -0.00786 -0.01223 44  PHE A CB  
234  C CG  . PHE A 37  ? 0.20102 0.25463 0.24979 0.02235  0.00939  -0.02520 44  PHE A CG  
235  C CD1 . PHE A 37  ? 0.20846 0.24367 0.23725 0.02850  0.01024  -0.02917 44  PHE A CD1 
236  C CD2 . PHE A 37  ? 0.24246 0.29959 0.29907 0.02759  0.02254  -0.03075 44  PHE A CD2 
237  C CE1 . PHE A 37  ? 0.26381 0.29067 0.28818 0.03859  0.02571  -0.03519 44  PHE A CE1 
238  C CE2 . PHE A 37  ? 0.19135 0.23656 0.24240 0.03494  0.03321  -0.03781 44  PHE A CE2 
239  C CZ  . PHE A 37  ? 0.22084 0.25411 0.25957 0.03990  0.03565  -0.03837 44  PHE A CZ  
240  N N   . LEU A 38  ? 0.24096 0.24170 0.25025 0.01578  -0.00185 -0.04002 45  LEU A N   
241  C CA  . LEU A 38  ? 0.20108 0.19728 0.21141 0.02336  0.01098  -0.04665 45  LEU A CA  
242  C C   . LEU A 38  ? 0.27167 0.24368 0.26421 0.01996  0.00169  -0.04952 45  LEU A C   
243  O O   . LEU A 38  ? 0.23629 0.21582 0.24128 0.01943  0.00608  -0.05010 45  LEU A O   
244  C CB  . LEU A 38  ? 0.20692 0.19424 0.20690 0.03746  0.02501  -0.04962 45  LEU A CB  
245  C CG  . LEU A 38  ? 0.22343 0.21609 0.23529 0.04435  0.03743  -0.04987 45  LEU A CG  
246  C CD1 . LEU A 38  ? 0.20379 0.21960 0.24457 0.03671  0.03856  -0.04862 45  LEU A CD1 
247  C CD2 . LEU A 38  ? 0.28359 0.27545 0.29239 0.05769  0.05213  -0.04527 45  LEU A CD2 
248  N N   . ARG A 39  ? 0.28377 0.22034 0.24166 0.01790  -0.01350 -0.05134 46  ARG A N   
249  C CA  . ARG A 39  ? 0.29747 0.19983 0.23048 0.01349  -0.02694 -0.05378 46  ARG A CA  
250  C C   . ARG A 39  ? 0.35118 0.27708 0.31436 -0.00514 -0.03709 -0.04466 46  ARG A C   
251  O O   . ARG A 39  ? 0.29304 0.21098 0.25561 -0.00554 -0.03657 -0.04566 46  ARG A O   
252  C CB  . ARG A 39  ? 0.32886 0.17949 0.21166 0.01082  -0.04882 -0.05671 46  ARG A CB  
253  C CG  . ARG A 39  ? 0.43812 0.24091 0.28721 0.00285  -0.06964 -0.05863 46  ARG A CG  
254  C CD  . ARG A 39  ? 0.58715 0.32880 0.37922 -0.00402 -0.09927 -0.06125 46  ARG A CD  
255  N NE  . ARG A 39  ? 0.57802 0.34305 0.39818 -0.03296 -0.12557 -0.04684 46  ARG A NE  
256  C CZ  . ARG A 39  ? 0.68872 0.41901 0.47533 -0.04384 -0.15390 -0.04422 46  ARG A CZ  
257  N NH1 . ARG A 39  ? 0.64474 0.32087 0.37116 -0.02410 -0.15241 -0.05207 46  ARG A NH1 
258  N NH2 . ARG A 39  ? 0.60801 0.37440 0.43513 -0.07070 -0.17630 -0.02488 46  ARG A NH2 
259  N N   . GLU A 40  ? 0.24162 0.19941 0.23251 -0.01849 -0.04463 -0.03274 47  GLU A N   
260  C CA  . GLU A 40  ? 0.25148 0.23678 0.27263 -0.03399 -0.05166 -0.01810 47  GLU A CA  
261  C C   . GLU A 40  ? 0.20142 0.21422 0.24447 -0.02466 -0.03056 -0.01964 47  GLU A C   
262  O O   . GLU A 40  ? 0.21121 0.22736 0.26160 -0.03129 -0.03311 -0.01375 47  GLU A O   
263  C CB  . GLU A 40  ? 0.20825 0.22970 0.25883 -0.04544 -0.06050 0.00047  47  GLU A CB  
264  C CG  . GLU A 40  ? 0.30437 0.29842 0.33557 -0.06172 -0.09072 0.00674  47  GLU A CG  
265  C CD  . GLU A 40  ? 0.43593 0.37892 0.43465 -0.07686 -0.11612 0.00503  47  GLU A CD  
266  O OE1 . GLU A 40  ? 0.35040 0.30418 0.36745 -0.08688 -0.11793 0.01451  47  GLU A OE1 
267  O OE2 . GLU A 40  ? 0.51921 0.40531 0.46785 -0.07720 -0.13473 -0.00563 47  GLU A OE2 
268  N N   . LEU A 41  ? 0.17845 0.20619 0.22831 -0.01034 -0.01224 -0.02671 48  LEU A N   
269  C CA  . LEU A 41  ? 0.18205 0.22589 0.24398 -0.00310 0.00194  -0.02871 48  LEU A CA  
270  C C   . LEU A 41  ? 0.19198 0.21467 0.24164 0.00097  0.00330  -0.03769 48  LEU A C   
271  O O   . LEU A 41  ? 0.21923 0.24806 0.27456 0.00036  0.00546  -0.03595 48  LEU A O   
272  C CB  . LEU A 41  ? 0.14263 0.19876 0.21011 0.00823  0.01535  -0.03268 48  LEU A CB  
273  C CG  . LEU A 41  ? 0.21675 0.29739 0.29741 0.01023  0.01826  -0.02158 48  LEU A CG  
274  C CD1 . LEU A 41  ? 0.17211 0.25151 0.24881 0.02298  0.02983  -0.02760 48  LEU A CD1 
275  C CD2 . LEU A 41  ? 0.15996 0.26590 0.25530 0.00934  0.02156  -0.00687 48  LEU A CD2 
276  N N   . ILE A 42  ? 0.19576 0.19437 0.22730 0.00792  0.00339  -0.04516 49  ILE A N   
277  C CA  . ILE A 42  ? 0.23792 0.22061 0.26056 0.01588  0.00665  -0.04921 49  ILE A CA  
278  C C   . ILE A 42  ? 0.22165 0.18342 0.23086 0.00822  -0.00603 -0.04664 49  ILE A C   
279  O O   . ILE A 42  ? 0.25727 0.21792 0.26948 0.01075  -0.00443 -0.04594 49  ILE A O   
280  C CB  . ILE A 42  ? 0.26430 0.22819 0.26856 0.03104  0.01436  -0.05336 49  ILE A CB  
281  C CG1 . ILE A 42  ? 0.20287 0.19148 0.22831 0.03655  0.02727  -0.05173 49  ILE A CG1 
282  C CG2 . ILE A 42  ? 0.26696 0.21137 0.25744 0.04382  0.01813  -0.05363 49  ILE A CG2 
283  C CD1 . ILE A 42  ? 0.28133 0.25904 0.29252 0.05222  0.03823  -0.05056 49  ILE A CD1 
284  N N   . SER A 43  ? 0.24452 0.18813 0.23922 -0.00329 -0.02177 -0.04321 50  SER A N   
285  C CA  . SER A 43  ? 0.25995 0.17931 0.24198 -0.01522 -0.03832 -0.03789 50  SER A CA  
286  C C   . SER A 43  ? 0.27468 0.22853 0.28754 -0.02566 -0.03631 -0.02625 50  SER A C   
287  O O   . SER A 43  ? 0.23029 0.17163 0.23827 -0.02865 -0.04073 -0.02311 50  SER A O   
288  C CB  . SER A 43  ? 0.33309 0.22415 0.29451 -0.03036 -0.06180 -0.03340 50  SER A CB  
289  O OG  . SER A 43  ? 0.47584 0.35207 0.43624 -0.04971 -0.08185 -0.02204 50  SER A OG  
290  N N   . ASN A 44  ? 0.22915 0.22376 0.26940 -0.02801 -0.02809 -0.01877 51  ASN A N   
291  C CA  . ASN A 44  ? 0.25457 0.28025 0.31593 -0.03007 -0.02037 -0.00750 51  ASN A CA  
292  C C   . ASN A 44  ? 0.20907 0.23064 0.26434 -0.01829 -0.01020 -0.01678 51  ASN A C   
293  O O   . ASN A 44  ? 0.18627 0.21060 0.24277 -0.02090 -0.01068 -0.00993 51  ASN A O   
294  C CB  . ASN A 44  ? 0.17140 0.23420 0.25288 -0.02550 -0.00896 0.00041  51  ASN A CB  
295  C CG  . ASN A 44  ? 0.31950 0.40246 0.42032 -0.03945 -0.01970 0.02000  51  ASN A CG  
296  O OD1 . ASN A 44  ? 0.25702 0.32299 0.35540 -0.05706 -0.03983 0.02814  51  ASN A OD1 
297  N ND2 . ASN A 44  ? 0.29499 0.41220 0.41444 -0.03184 -0.00842 0.02973  51  ASN A ND2 
298  N N   . SER A 45  ? 0.16031 0.17727 0.21115 -0.00654 -0.00246 -0.02937 52  SER A N   
299  C CA  . SER A 45  ? 0.20305 0.21871 0.25332 0.00144  0.00218  -0.03451 52  SER A CA  
300  C C   . SER A 45  ? 0.22092 0.21486 0.26097 0.00240  -0.00424 -0.03420 52  SER A C   
301  O O   . SER A 45  ? 0.20889 0.20484 0.24998 0.00328  -0.00525 -0.03132 52  SER A O   
302  C CB  . SER A 45  ? 0.18951 0.20784 0.24433 0.00998  0.00863  -0.04199 52  SER A CB  
303  O OG  . SER A 45  ? 0.21494 0.24648 0.27422 0.01057  0.01366  -0.04280 52  SER A OG  
304  N N   . SER A 46  ? 0.21837 0.18577 0.24212 0.00455  -0.00916 -0.03721 53  SER A N   
305  C CA  . SER A 46  ? 0.25930 0.19596 0.26413 0.00967  -0.01493 -0.03708 53  SER A CA  
306  C C   . SER A 46  ? 0.33331 0.26415 0.33671 -0.00442 -0.02588 -0.02786 53  SER A C   
307  O O   . SER A 46  ? 0.27162 0.19277 0.27039 -0.00039 -0.02735 -0.02525 53  SER A O   
308  C CB  . SER A 46  ? 0.27545 0.17194 0.24839 0.01704  -0.01946 -0.04283 53  SER A CB  
309  O OG  . SER A 46  ? 0.33837 0.19472 0.28307 0.02651  -0.02455 -0.04333 53  SER A OG  
310  N N   . ASP A 47  ? 0.24840 0.18855 0.25914 -0.02098 -0.03359 -0.01926 54  ASP A N   
311  C CA  . ASP A 47  ? 0.23958 0.18295 0.25670 -0.03620 -0.04258 -0.00392 54  ASP A CA  
312  C C   . ASP A 47  ? 0.23785 0.20933 0.26820 -0.03050 -0.03077 0.00084  54  ASP A C   
313  O O   . ASP A 47  ? 0.25863 0.22115 0.28428 -0.03398 -0.03517 0.00889  54  ASP A O   
314  C CB  . ASP A 47  ? 0.24005 0.20334 0.27458 -0.05395 -0.05054 0.01083  54  ASP A CB  
315  C CG  . ASP A 47  ? 0.47208 0.39450 0.48566 -0.06731 -0.07343 0.01094  54  ASP A CG  
316  O OD1 . ASP A 47  ? 0.39761 0.27020 0.37479 -0.05814 -0.07982 -0.00299 54  ASP A OD1 
317  O OD2 . ASP A 47  ? 0.39349 0.33211 0.42430 -0.08503 -0.08541 0.02596  54  ASP A OD2 
318  N N   . ALA A 48  ? 0.22010 0.21888 0.26071 -0.02124 -0.01757 -0.00419 55  ALA A N   
319  C CA  . ALA A 48  ? 0.22793 0.24239 0.26844 -0.01440 -0.00946 -0.00145 55  ALA A CA  
320  C C   . ALA A 48  ? 0.19782 0.19648 0.22939 -0.00628 -0.01270 -0.00924 55  ALA A C   
321  O O   . ALA A 48  ? 0.20126 0.20092 0.22613 -0.00431 -0.01328 -0.00410 55  ALA A O   
322  C CB  . ALA A 48  ? 0.17197 0.20589 0.21483 -0.00586 0.00164  -0.00605 55  ALA A CB  
323  N N   . LEU A 49  ? 0.22470 0.21136 0.25667 0.00024  -0.01403 -0.01877 56  LEU A N   
324  C CA  . LEU A 49  ? 0.22924 0.20819 0.26061 0.00959  -0.01647 -0.02021 56  LEU A CA  
325  C C   . LEU A 49  ? 0.24155 0.19546 0.25961 0.00934  -0.02339 -0.01424 56  LEU A C   
326  O O   . LEU A 49  ? 0.25560 0.20795 0.27255 0.01421  -0.02654 -0.00981 56  LEU A O   
327  C CB  . LEU A 49  ? 0.24296 0.22299 0.28257 0.02017  -0.01160 -0.02602 56  LEU A CB  
328  C CG  . LEU A 49  ? 0.19096 0.19321 0.24558 0.01940  -0.00790 -0.02949 56  LEU A CG  
329  C CD1 . LEU A 49  ? 0.19982 0.20372 0.26160 0.02684  -0.00038 -0.03227 56  LEU A CD1 
330  C CD2 . LEU A 49  ? 0.21035 0.22403 0.27557 0.02018  -0.01462 -0.02544 56  LEU A CD2 
331  N N   . ASP A 50  ? 0.25251 0.18191 0.25736 0.00282  -0.02886 -0.01329 57  ASP A N   
332  C CA  . ASP A 50  ? 0.32317 0.21915 0.30949 -0.00074 -0.03933 -0.00660 57  ASP A CA  
333  C C   . ASP A 50  ? 0.29857 0.20936 0.29153 -0.01071 -0.04149 0.00624  57  ASP A C   
334  O O   . ASP A 50  ? 0.29833 0.19170 0.28114 -0.00730 -0.04641 0.01169  57  ASP A O   
335  C CB  . ASP A 50  ? 0.30880 0.17145 0.27686 -0.01298 -0.05166 -0.00566 57  ASP A CB  
336  C CG  . ASP A 50  ? 0.42835 0.25696 0.37114 0.00215  -0.05105 -0.01829 57  ASP A CG  
337  O OD1 . ASP A 50  ? 0.41155 0.24791 0.35675 0.02370  -0.03793 -0.02437 57  ASP A OD1 
338  O OD2 . ASP A 50  ? 0.43708 0.23095 0.35663 -0.00753 -0.06461 -0.01961 57  ASP A OD2 
339  N N   . LYS A 51  ? 0.26728 0.20971 0.27464 -0.01975 -0.03589 0.01283  58  LYS A N   
340  C CA  . LYS A 51  ? 0.29355 0.25078 0.30308 -0.02603 -0.03407 0.02874  58  LYS A CA  
341  C C   . LYS A 51  ? 0.30098 0.26235 0.30213 -0.01349 -0.03070 0.02568  58  LYS A C   
342  O O   . LYS A 51  ? 0.28779 0.24087 0.27994 -0.01459 -0.03429 0.03632  58  LYS A O   
343  C CB  . LYS A 51  ? 0.27613 0.26807 0.30036 -0.03116 -0.02406 0.03876  58  LYS A CB  
344  C CG  . LYS A 51  ? 0.31604 0.31160 0.35538 -0.04941 -0.03192 0.05305  58  LYS A CG  
345  C CD  . LYS A 51  ? 0.31453 0.35299 0.37403 -0.04863 -0.01847 0.06496  58  LYS A CD  
346  C CE  . LYS A 51  ? 0.44034 0.48604 0.52008 -0.06615 -0.02955 0.07576  58  LYS A CE  
347  N NZ  . LYS A 51  ? 0.38948 0.48464 0.49539 -0.06358 -0.01500 0.09485  58  LYS A NZ  
348  N N   . ILE A 52  ? 0.24891 0.22139 0.25215 -0.00337 -0.02660 0.01312  59  ILE A N   
349  C CA  . ILE A 52  ? 0.26678 0.23969 0.26087 0.00489  -0.03017 0.01190  59  ILE A CA  
350  C C   . ILE A 52  ? 0.28198 0.23905 0.27819 0.01076  -0.03872 0.01255  59  ILE A C   
351  O O   . ILE A 52  ? 0.28553 0.23818 0.27302 0.01424  -0.04495 0.01893  59  ILE A O   
352  C CB  . ILE A 52  ? 0.24673 0.23059 0.24127 0.00993  -0.02935 0.00121  59  ILE A CB  
353  C CG1 . ILE A 52  ? 0.27179 0.24990 0.24877 0.01443  -0.03901 0.00219  59  ILE A CG1 
354  C CG2 . ILE A 52  ? 0.22157 0.20877 0.23628 0.01236  -0.03070 -0.00721 59  ILE A CG2 
355  C CD1 . ILE A 52  ? 0.30977 0.28236 0.25797 0.01696  -0.03447 0.01117  59  ILE A CD1 
356  N N   . ARG A 53  ? 0.27699 0.22305 0.28057 0.01510  -0.03822 0.00749  60  ARG A N   
357  C CA  . ARG A 53  ? 0.28004 0.20877 0.28142 0.02718  -0.04243 0.01071  60  ARG A CA  
358  C C   . ARG A 53  ? 0.34948 0.25118 0.33219 0.02299  -0.04886 0.02036  60  ARG A C   
359  O O   . ARG A 53  ? 0.32928 0.22480 0.30810 0.03111  -0.05384 0.02732  60  ARG A O   
360  C CB  . ARG A 53  ? 0.33238 0.24730 0.33403 0.03849  -0.03696 0.00436  60  ARG A CB  
361  C CG  . ARG A 53  ? 0.48391 0.38094 0.48002 0.05867  -0.03696 0.01015  60  ARG A CG  
362  C CD  . ARG A 53  ? 0.66717 0.54154 0.65077 0.07709  -0.02811 0.00545  60  ARG A CD  
363  N NE  . ARG A 53  ? 0.71441 0.62501 0.72730 0.09149  -0.01736 0.00875  60  ARG A NE  
364  C CZ  . ARG A 53  ? 0.66852 0.57914 0.68017 0.10116  -0.00616 0.00400  60  ARG A CZ  
365  N NH1 . ARG A 53  ? 0.61334 0.48587 0.59158 0.09825  -0.00640 -0.00687 60  ARG A NH1 
366  N NH2 . ARG A 53  ? 0.56592 0.51551 0.61084 0.11308  0.00377  0.01294  60  ARG A NH2 
367  N N   . TYR A 54  ? 0.32209 0.20859 0.29553 0.00861  -0.05086 0.02384  61  TYR A N   
368  C CA  . TYR A 54  ? 0.35561 0.21534 0.31375 0.00012  -0.05952 0.03683  61  TYR A CA  
369  C C   . TYR A 54  ? 0.36184 0.24081 0.32040 -0.00136 -0.05831 0.04832  61  TYR A C   
370  O O   . TYR A 54  ? 0.38969 0.24911 0.33621 0.00232  -0.06465 0.05704  61  TYR A O   
371  C CB  . TYR A 54  ? 0.36759 0.21562 0.32413 -0.02074 -0.06563 0.04433  61  TYR A CB  
372  C CG  . TYR A 54  ? 0.46813 0.28424 0.41051 -0.03310 -0.07826 0.06104  61  TYR A CG  
373  C CD1 . TYR A 54  ? 0.45439 0.21487 0.36852 -0.02610 -0.09004 0.05788  61  TYR A CD1 
374  C CD2 . TYR A 54  ? 0.40802 0.24789 0.36264 -0.04892 -0.07699 0.08216  61  TYR A CD2 
375  C CE1 . TYR A 54  ? 0.49874 0.22309 0.39667 -0.03852 -0.10410 0.07376  61  TYR A CE1 
376  C CE2 . TYR A 54  ? 0.44748 0.25978 0.39243 -0.06233 -0.08916 0.10124  61  TYR A CE2 
377  C CZ  . TYR A 54  ? 0.50699 0.25937 0.42345 -0.05895 -0.10453 0.09621  61  TYR A CZ  
378  O OH  . TYR A 54  ? 0.55439 0.27238 0.45811 -0.07386 -0.11926 0.11583  61  TYR A OH  
379  N N   . GLU A 55  ? 0.33551 0.24745 0.30134 -0.00405 -0.05003 0.04863  62  GLU A N   
380  C CA  . GLU A 55  ? 0.39395 0.31671 0.34788 -0.00150 -0.04806 0.05881  62  GLU A CA  
381  C C   . GLU A 55  ? 0.37079 0.28825 0.31811 0.01142  -0.05631 0.05410  62  GLU A C   
382  O O   . GLU A 55  ? 0.44365 0.35308 0.37590 0.01408  -0.06113 0.06469  62  GLU A O   
383  C CB  . GLU A 55  ? 0.41196 0.36126 0.36347 -0.00052 -0.03637 0.05807  62  GLU A CB  
384  C CG  . GLU A 55  ? 0.46107 0.42645 0.42323 -0.01169 -0.02657 0.07338  62  GLU A CG  
385  C CD  . GLU A 55  ? 0.60689 0.59676 0.55815 -0.00254 -0.01041 0.07921  62  GLU A CD  
386  O OE1 . GLU A 55  ? 0.51299 0.49756 0.44196 0.01083  -0.01004 0.06574  62  GLU A OE1 
387  O OE2 . GLU A 55  ? 0.59228 0.60468 0.55547 -0.00780 0.00103  0.09936  62  GLU A OE2 
388  N N   . SER A 56  ? 0.37522 0.29984 0.33667 0.01902  -0.05887 0.04173  63  SER A N   
389  C CA  . SER A 56  ? 0.36549 0.29383 0.33149 0.02934  -0.06917 0.04271  63  SER A CA  
390  C C   . SER A 56  ? 0.43083 0.33937 0.39622 0.03860  -0.07394 0.05151  63  SER A C   
391  O O   . SER A 56  ? 0.37931 0.29338 0.34910 0.04754  -0.08334 0.05826  63  SER A O   
392  C CB  . SER A 56  ? 0.32583 0.27356 0.31590 0.03350  -0.06990 0.03375  63  SER A CB  
393  O OG  . SER A 56  ? 0.37153 0.31350 0.37585 0.04169  -0.06294 0.03163  63  SER A OG  
394  N N   . LEU A 57  ? 0.41153 0.29333 0.36888 0.03691  -0.07011 0.05262  64  LEU A N   
395  C CA  . LEU A 57  ? 0.50268 0.35366 0.44971 0.04923  -0.07475 0.05977  64  LEU A CA  
396  C C   . LEU A 57  ? 0.51296 0.35526 0.44542 0.04757  -0.08264 0.07373  64  LEU A C   
397  O O   . LEU A 57  ? 0.52837 0.35852 0.45802 0.06256  -0.08816 0.08123  64  LEU A O   
398  C CB  . LEU A 57  ? 0.49310 0.30283 0.42214 0.04482  -0.07425 0.05691  64  LEU A CB  
399  C CG  . LEU A 57  ? 0.51939 0.32484 0.45216 0.05308  -0.06725 0.04368  64  LEU A CG  
400  C CD1 . LEU A 57  ? 0.56988 0.31932 0.47122 0.04882  -0.07333 0.04102  64  LEU A CD1 
401  C CD2 . LEU A 57  ? 0.50382 0.32290 0.45039 0.07985  -0.06084 0.04357  64  LEU A CD2 
402  N N   . THR A 58  ? 0.49218 0.34156 0.41460 0.03230  -0.08148 0.07982  65  THR A N   
403  C CA  . THR A 58  ? 0.60410 0.44607 0.50862 0.03126  -0.08672 0.09498  65  THR A CA  
404  C C   . THR A 58  ? 0.61992 0.48656 0.51648 0.03375  -0.08880 0.09490  65  THR A C   
405  O O   . THR A 58  ? 0.60088 0.46024 0.47807 0.03719  -0.09509 0.10655  65  THR A O   
406  C CB  . THR A 58  ? 0.73385 0.56184 0.62781 0.01422  -0.08306 0.10905  65  THR A CB  
407  O OG1 . THR A 58  ? 0.64443 0.50031 0.54662 0.00387  -0.07207 0.10728  65  THR A OG1 
408  C CG2 . THR A 58  ? 0.59765 0.38590 0.48883 0.00863  -0.08918 0.10986  65  THR A CG2 
409  N N   . ASP A 59  ? 0.56262 0.45123 0.46726 0.03258  -0.08567 0.08205  66  ASP A N   
410  C CA  . ASP A 59  ? 0.56538 0.46358 0.45043 0.03493  -0.09149 0.07946  66  ASP A CA  
411  C C   . ASP A 59  ? 0.50647 0.42066 0.41181 0.03613  -0.09913 0.06595  66  ASP A C   
412  O O   . ASP A 59  ? 0.42953 0.35275 0.33961 0.03175  -0.09088 0.05517  66  ASP A O   
413  C CB  . ASP A 59  ? 0.51955 0.42031 0.37999 0.03120  -0.07708 0.08243  66  ASP A CB  
414  C CG  . ASP A 59  ? 0.70690 0.60180 0.52879 0.03860  -0.08308 0.07852  66  ASP A CG  
415  O OD1 . ASP A 59  ? 0.59173 0.47992 0.40799 0.04139  -0.10364 0.07429  66  ASP A OD1 
416  O OD2 . ASP A 59  ? 0.68299 0.57786 0.47766 0.04272  -0.06815 0.08154  66  ASP A OD2 
417  N N   . PRO A 60  ? 0.56040 0.48121 0.48168 0.04162  -0.11554 0.06966  67  PRO A N   
418  C CA  . PRO A 60  ? 0.53154 0.47335 0.48156 0.04005  -0.12408 0.06322  67  PRO A CA  
419  C C   . PRO A 60  ? 0.54880 0.48632 0.47502 0.03193  -0.13391 0.05380  67  PRO A C   
420  O O   . PRO A 60  ? 0.46741 0.41766 0.41394 0.02675  -0.13658 0.04649  67  PRO A O   
421  C CB  . PRO A 60  ? 0.56637 0.52124 0.54073 0.04750  -0.14143 0.07761  67  PRO A CB  
422  C CG  . PRO A 60  ? 0.67603 0.61200 0.63086 0.05501  -0.14094 0.08836  67  PRO A CG  
423  C CD  . PRO A 60  ? 0.60070 0.51382 0.52157 0.04975  -0.12567 0.08393  67  PRO A CD  
424  N N   . SER A 61  ? 0.49886 0.41356 0.37688 0.03259  -0.13915 0.05443  68  SER A N   
425  C CA  . SER A 61  ? 0.52991 0.42603 0.36921 0.02967  -0.14890 0.04401  68  SER A CA  
426  C C   . SER A 61  ? 0.55326 0.45188 0.39094 0.02934  -0.12769 0.03193  68  SER A C   
427  O O   . SER A 61  ? 0.48136 0.36357 0.29331 0.02797  -0.13537 0.02139  68  SER A O   
428  C CB  . SER A 61  ? 0.56124 0.42591 0.33755 0.03711  -0.15375 0.04799  68  SER A CB  
429  O OG  . SER A 61  ? 0.57559 0.43944 0.33434 0.04468  -0.12498 0.05247  68  SER A OG  
430  N N   . LYS A 62  ? 0.42306 0.33782 0.28529 0.03011  -0.10403 0.03406  69  LYS A N   
431  C CA  . LYS A 62  ? 0.46761 0.39007 0.33546 0.02906  -0.08594 0.02529  69  LYS A CA  
432  C C   . LYS A 62  ? 0.44446 0.37692 0.34017 0.02318  -0.09392 0.01474  69  LYS A C   
433  O O   . LYS A 62  ? 0.39381 0.32709 0.28615 0.02301  -0.08355 0.00593  69  LYS A O   
434  C CB  . LYS A 62  ? 0.49346 0.42963 0.38585 0.02665  -0.06692 0.03234  69  LYS A CB  
435  C CG  . LYS A 62  ? 0.59302 0.52303 0.46333 0.02919  -0.05799 0.04772  69  LYS A CG  
436  C CD  . LYS A 62  ? 0.52999 0.47298 0.39954 0.02865  -0.03659 0.05447  69  LYS A CD  
437  C CE  . LYS A 62  ? 0.56041 0.50303 0.40666 0.03309  -0.02552 0.07521  69  LYS A CE  
438  N NZ  . LYS A 62  ? 0.66688 0.63126 0.51536 0.03619  -0.00281 0.08716  69  LYS A NZ  
439  N N   . LEU A 63  ? 0.40724 0.35061 0.33318 0.01936  -0.11105 0.01886  70  LEU A N   
440  C CA  . LEU A 63  ? 0.36058 0.31865 0.31815 0.01290  -0.11940 0.01513  70  LEU A CA  
441  C C   . LEU A 63  ? 0.39009 0.33306 0.33027 0.00435  -0.14882 0.01504  70  LEU A C   
442  O O   . LEU A 63  ? 0.40016 0.35830 0.37335 -0.00482 -0.16194 0.01833  70  LEU A O   
443  C CB  . LEU A 63  ? 0.39170 0.37778 0.40030 0.01630  -0.11656 0.02541  70  LEU A CB  
444  C CG  . LEU A 63  ? 0.39601 0.38473 0.41489 0.02396  -0.09278 0.02352  70  LEU A CG  
445  C CD1 . LEU A 63  ? 0.37304 0.37977 0.42924 0.03428  -0.08954 0.03362  70  LEU A CD1 
446  C CD2 . LEU A 63  ? 0.34224 0.33067 0.35837 0.02020  -0.07813 0.01144  70  LEU A CD2 
447  N N   . ASP A 64  ? 0.42205 0.33238 0.30824 0.00665  -0.16109 0.01314  71  ASP A N   
448  C CA  . ASP A 64  ? 0.47080 0.35135 0.32512 -0.00266 -0.19456 0.01086  71  ASP A CA  
449  C C   . ASP A 64  ? 0.52176 0.38431 0.36228 -0.00807 -0.19608 -0.00207 71  ASP A C   
450  O O   . ASP A 64  ? 0.55023 0.39533 0.38667 -0.02248 -0.22759 -0.00139 71  ASP A O   
451  C CB  . ASP A 64  ? 0.63561 0.47295 0.41710 0.00613  -0.20336 0.00847  71  ASP A CB  
452  C CG  . ASP A 64  ? 0.80716 0.65452 0.59828 0.00676  -0.21643 0.02352  71  ASP A CG  
453  O OD1 . ASP A 64  ? 0.65606 0.54240 0.51015 0.00085  -0.22202 0.03642  71  ASP A OD1 
454  O OD2 . ASP A 64  ? 0.73454 0.55021 0.46792 0.01599  -0.21965 0.02404  71  ASP A OD2 
455  N N   . SER A 65  ? 0.45540 0.32082 0.28941 0.00200  -0.16492 -0.01166 72  SER A N   
456  C CA  . SER A 65  ? 0.48748 0.33756 0.30956 0.00058  -0.16111 -0.02338 72  SER A CA  
457  C C   . SER A 65  ? 0.60479 0.49205 0.49326 -0.01131 -0.15987 -0.01922 72  SER A C   
458  O O   . SER A 65  ? 0.55027 0.42979 0.43609 -0.01266 -0.15388 -0.02750 72  SER A O   
459  C CB  . SER A 65  ? 0.51163 0.35788 0.30618 0.01816  -0.12689 -0.03037 72  SER A CB  
460  O OG  . SER A 65  ? 0.42584 0.30949 0.25722 0.02175  -0.10393 -0.02150 72  SER A OG  
461  N N   . GLY A 66  ? 0.44087 0.36728 0.38566 -0.01653 -0.16299 -0.00505 73  GLY A N   
462  C CA  . GLY A 66  ? 0.44520 0.40882 0.45040 -0.02263 -0.15781 0.00275  73  GLY A CA  
463  C C   . GLY A 66  ? 0.33752 0.33826 0.38570 -0.01235 -0.13766 0.01275  73  GLY A C   
464  O O   . GLY A 66  ? 0.32333 0.32145 0.35921 -0.00177 -0.11439 0.00576  73  GLY A O   
465  N N   . LYS A 67  ? 0.30345 0.33683 0.40065 -0.01455 -0.14743 0.03149  74  LYS A N   
466  C CA  . LYS A 67  ? 0.32907 0.38889 0.45738 0.00119  -0.12814 0.04164  74  LYS A CA  
467  C C   . LYS A 67  ? 0.29317 0.37137 0.44743 0.01015  -0.10302 0.04057  74  LYS A C   
468  O O   . LYS A 67  ? 0.31107 0.38955 0.46536 0.02616  -0.08301 0.04004  74  LYS A O   
469  C CB  . LYS A 67  ? 0.27672 0.36655 0.44548 0.00155  -0.14601 0.06634  74  LYS A CB  
470  C CG  . LYS A 67  ? 0.50235 0.57163 0.64248 -0.00690 -0.17419 0.06882  74  LYS A CG  
471  C CD  . LYS A 67  ? 0.56660 0.66115 0.73645 0.00383  -0.17971 0.09052  74  LYS A CD  
472  C CE  . LYS A 67  ? 0.72129 0.80298 0.87407 -0.00978 -0.21723 0.09902  74  LYS A CE  
473  N NZ  . LYS A 67  ? 0.91148 1.00935 1.07972 0.00298  -0.21844 0.11632  74  LYS A NZ  
474  N N   . GLU A 68  ? 0.24010 0.32700 0.41012 0.00059  -0.10518 0.04026  75  GLU A N   
475  C CA  . GLU A 68  ? 0.24746 0.35259 0.44106 0.01025  -0.08203 0.04187  75  GLU A CA  
476  C C   . GLU A 68  ? 0.28701 0.36559 0.44379 0.01555  -0.06284 0.02042  75  GLU A C   
477  O O   . GLU A 68  ? 0.30400 0.35955 0.42922 0.00649  -0.06750 0.00623  75  GLU A O   
478  C CB  . GLU A 68  ? 0.31725 0.44076 0.54121 -0.00351 -0.09178 0.05164  75  GLU A CB  
479  C CG  . GLU A 68  ? 0.38035 0.54686 0.66138 -0.00776 -0.10607 0.08289  75  GLU A CG  
480  C CD  . GLU A 68  ? 0.76924 0.92774 1.04629 -0.02494 -0.14164 0.09024  75  GLU A CD  
481  O OE1 . GLU A 68  ? 0.77372 0.89372 1.01160 -0.04249 -0.16321 0.07518  75  GLU A OE1 
482  O OE2 . GLU A 68  ? 0.66755 0.84657 0.96456 -0.01850 -0.14294 0.10793  75  GLU A OE2 
483  N N   . LEU A 69  ? 0.20901 0.28906 0.36777 0.03157  -0.04223 0.02010  76  LEU A N   
484  C CA  . LEU A 69  ? 0.20578 0.26218 0.33452 0.03427  -0.02841 0.00401  76  LEU A CA  
485  C C   . LEU A 69  ? 0.20932 0.27516 0.35070 0.04085  -0.01407 0.00426  76  LEU A C   
486  O O   . LEU A 69  ? 0.17886 0.25109 0.32987 0.05842  -0.00141 0.01300  76  LEU A O   
487  C CB  . LEU A 69  ? 0.26818 0.30398 0.37652 0.04523  -0.02267 0.00287  76  LEU A CB  
488  C CG  . LEU A 69  ? 0.30413 0.32964 0.39802 0.03994  -0.03488 0.00473  76  LEU A CG  
489  C CD1 . LEU A 69  ? 0.37458 0.37277 0.44489 0.04726  -0.03006 0.00348  76  LEU A CD1 
490  C CD2 . LEU A 69  ? 0.27261 0.29167 0.34756 0.02525  -0.04225 -0.00368 76  LEU A CD2 
491  N N   . HIS A 70  ? 0.18504 0.24926 0.32226 0.03017  -0.01462 -0.00413 77  HIS A N   
492  C CA  . HIS A 70  ? 0.14628 0.22104 0.29668 0.03557  -0.00225 -0.00161 77  HIS A CA  
493  C C   . HIS A 70  ? 0.13530 0.19652 0.26667 0.02689  -0.00060 -0.01546 77  HIS A C   
494  O O   . HIS A 70  ? 0.14342 0.19126 0.25485 0.01823  -0.00776 -0.02463 77  HIS A O   
495  C CB  . HIS A 70  ? 0.19307 0.29920 0.38465 0.03176  -0.00753 0.01703  77  HIS A CB  
496  C CG  . HIS A 70  ? 0.22774 0.33070 0.42193 0.01070  -0.02997 0.01615  77  HIS A CG  
497  N ND1 . HIS A 70  ? 0.29859 0.41405 0.51358 0.00113  -0.05040 0.03009  77  HIS A ND1 
498  C CD2 . HIS A 70  ? 0.27781 0.35975 0.44971 -0.00093 -0.03698 0.00319  77  HIS A CD2 
499  C CE1 . HIS A 70  ? 0.28713 0.38235 0.48620 -0.01683 -0.07144 0.02385  77  HIS A CE1 
500  N NE2 . HIS A 70  ? 0.31680 0.39042 0.48812 -0.01630 -0.06185 0.00722  77  HIS A NE2 
501  N N   . ILE A 71  ? 0.13162 0.19835 0.26935 0.03228  0.01074  -0.01416 78  ILE A N   
502  C CA  . ILE A 71  ? 0.12765 0.18520 0.25167 0.02712  0.01394  -0.02412 78  ILE A CA  
503  C C   . ILE A 71  ? 0.16137 0.23485 0.30891 0.02457  0.01612  -0.01482 78  ILE A C   
504  O O   . ILE A 71  ? 0.13293 0.22327 0.29985 0.03513  0.02678  -0.00168 78  ILE A O   
505  C CB  . ILE A 71  ? 0.20187 0.24324 0.30291 0.03609  0.02395  -0.03126 78  ILE A CB  
506  C CG1 . ILE A 71  ? 0.20594 0.22970 0.28673 0.03470  0.01837  -0.03630 78  ILE A CG1 
507  C CG2 . ILE A 71  ? 0.19568 0.23341 0.28812 0.03108  0.02610  -0.03803 78  ILE A CG2 
508  C CD1 . ILE A 71  ? 0.23285 0.23170 0.28743 0.04025  0.02072  -0.04110 78  ILE A CD1 
509  N N   . ASN A 72  ? 0.12388 0.18999 0.26735 0.01265  0.00716  -0.01948 79  ASN A N   
510  C CA  . ASN A 72  ? 0.13645 0.21122 0.29937 0.00672  0.00616  -0.01010 79  ASN A CA  
511  C C   . ASN A 72  ? 0.18244 0.24265 0.32492 0.00853  0.01343  -0.02062 79  ASN A C   
512  O O   . ASN A 72  ? 0.16359 0.20627 0.27992 0.00821  0.01111  -0.03354 79  ASN A O   
513  C CB  . ASN A 72  ? 0.13601 0.20486 0.30809 -0.01062 -0.01652 -0.00409 79  ASN A CB  
514  C CG  . ASN A 72  ? 0.22112 0.30990 0.42070 -0.01486 -0.02769 0.01115  79  ASN A CG  
515  O OD1 . ASN A 72  ? 0.19672 0.31427 0.42359 -0.00358 -0.01480 0.02538  79  ASN A OD1 
516  N ND2 . ASN A 72  ? 0.19005 0.26106 0.37911 -0.02898 -0.05221 0.00966  79  ASN A ND2 
517  N N   . LEU A 73  ? 0.13691 0.20748 0.29307 0.01210  0.02333  -0.01182 80  LEU A N   
518  C CA  . LEU A 73  ? 0.11957 0.17819 0.25962 0.01398  0.02923  -0.01863 80  LEU A CA  
519  C C   . LEU A 73  ? 0.12992 0.18584 0.28450 0.00228  0.02061  -0.00903 80  LEU A C   
520  O O   . LEU A 73  ? 0.12952 0.20650 0.31575 -0.00103 0.02249  0.01011  80  LEU A O   
521  C CB  . LEU A 73  ? 0.15415 0.21852 0.28860 0.02845  0.04638  -0.01639 80  LEU A CB  
522  C CG  . LEU A 73  ? 0.18733 0.24417 0.30208 0.03898  0.05092  -0.02385 80  LEU A CG  
523  C CD1 . LEU A 73  ? 0.17953 0.22804 0.27521 0.05410  0.06396  -0.02268 80  LEU A CD1 
524  C CD2 . LEU A 73  ? 0.16936 0.21279 0.26480 0.03247  0.04184  -0.03728 80  LEU A CD2 
525  N N   . ILE A 74  ? 0.14469 0.17375 0.27566 -0.00286 0.01133  -0.01955 81  ILE A N   
526  C CA  . ILE A 74  ? 0.16815 0.17954 0.30274 -0.01646 -0.00353 -0.01228 81  ILE A CA  
527  C C   . ILE A 74  ? 0.24192 0.23443 0.35661 -0.01088 0.00293  -0.01770 81  ILE A C   
528  O O   . ILE A 74  ? 0.21729 0.18220 0.29756 -0.00429 0.00076  -0.03165 81  ILE A O   
529  C CB  . ILE A 74  ? 0.19758 0.17770 0.31021 -0.02685 -0.02665 -0.01921 81  ILE A CB  
530  C CG1 . ILE A 74  ? 0.19798 0.19770 0.32755 -0.03024 -0.03276 -0.01467 81  ILE A CG1 
531  C CG2 . ILE A 74  ? 0.23349 0.18706 0.34777 -0.04530 -0.04917 -0.00929 81  ILE A CG2 
532  C CD1 . ILE A 74  ? 0.27982 0.24568 0.38179 -0.03974 -0.05741 -0.02121 81  ILE A CD1 
533  N N   . PRO A 75  ? 0.21795 0.22515 0.35235 -0.01069 0.01235  -0.00474 82  PRO A N   
534  C CA  . PRO A 75  ? 0.23139 0.21854 0.34765 -0.00652 0.01608  -0.00755 82  PRO A CA  
535  C C   . PRO A 75  ? 0.28011 0.23270 0.38973 -0.02213 -0.00432 -0.00209 82  PRO A C   
536  O O   . PRO A 75  ? 0.25434 0.21176 0.39042 -0.04050 -0.01966 0.01384  82  PRO A O   
537  C CB  . PRO A 75  ? 0.21336 0.22882 0.35096 0.00023  0.03397  0.00650  82  PRO A CB  
538  C CG  . PRO A 75  ? 0.21748 0.26325 0.39280 -0.00641 0.03438  0.02532  82  PRO A CG  
539  C CD  . PRO A 75  ? 0.17255 0.21567 0.34653 -0.01218 0.02110  0.01665  82  PRO A CD  
540  N N   . ASN A 76  ? 0.25058 0.16586 0.32354 -0.01458 -0.00629 -0.01340 83  ASN A N   
541  C CA  . ASN A 76  ? 0.31951 0.18563 0.37155 -0.02658 -0.02715 -0.01072 83  ASN A CA  
542  C C   . ASN A 76  ? 0.32956 0.17860 0.36360 -0.01459 -0.01663 -0.01162 83  ASN A C   
543  O O   . ASN A 76  ? 0.38360 0.21691 0.38410 0.00590  -0.00706 -0.02588 83  ASN A O   
544  C CB  . ASN A 76  ? 0.38043 0.19715 0.38541 -0.02456 -0.04478 -0.02702 83  ASN A CB  
545  C CG  . ASN A 76  ? 0.46916 0.22113 0.44354 -0.04027 -0.07412 -0.02445 83  ASN A CG  
546  O OD1 . ASN A 76  ? 0.52476 0.25007 0.48716 -0.03968 -0.07503 -0.02034 83  ASN A OD1 
547  N ND2 . ASN A 76  ? 0.54617 0.26705 0.50376 -0.05528 -0.10125 -0.02642 83  ASN A ND2 
548  N N   . LYS A 77  ? 0.40153 0.25637 0.44617 -0.05254 0.00029  0.11036  84  LYS A N   
549  C CA  . LYS A 77  ? 0.41762 0.25324 0.45512 -0.03843 0.00864  0.12503  84  LYS A CA  
550  C C   . LYS A 77  ? 0.54190 0.31393 0.56828 -0.04598 0.00891  0.12229  84  LYS A C   
551  O O   . LYS A 77  ? 0.49962 0.24879 0.51555 -0.02719 0.01546  0.12777  84  LYS A O   
552  C CB  . LYS A 77  ? 0.43587 0.30102 0.48693 -0.04222 0.01560  0.15388  84  LYS A CB  
553  C CG  . LYS A 77  ? 0.47528 0.39834 0.52934 -0.02436 0.01948  0.15790  84  LYS A CG  
554  C CD  . LYS A 77  ? 0.53640 0.48800 0.60015 -0.02424 0.02873  0.18845  84  LYS A CD  
555  C CE  . LYS A 77  ? 0.52989 0.53796 0.59260 -0.00582 0.03347  0.19024  84  LYS A CE  
556  N NZ  . LYS A 77  ? 0.54566 0.58114 0.61997 -0.01445 0.02926  0.17981  84  LYS A NZ  
557  N N   . GLN A 78  ? 0.50532 0.24801 0.53240 -0.07244 0.00194  0.11414  85  GLN A N   
558  C CA  . GLN A 78  ? 0.63983 0.31633 0.65004 -0.07868 0.00319  0.10635  85  GLN A CA  
559  C C   . GLN A 78  ? 0.56911 0.22168 0.56028 -0.05783 0.00351  0.08346  85  GLN A C   
560  O O   . GLN A 78  ? 0.64453 0.26897 0.62996 -0.04059 0.00899  0.08353  85  GLN A O   
561  C CB  . GLN A 78  ? 0.61860 0.28439 0.63120 -0.10937 -0.00186 0.09547  85  GLN A CB  
562  C CG  . GLN A 78  ? 0.80259 0.47761 0.82997 -0.12980 0.00105  0.11752  85  GLN A CG  
563  C CD  . GLN A 78  ? 1.02875 0.76878 1.08091 -0.13347 -0.00173 0.13898  85  GLN A CD  
564  O OE1 . GLN A 78  ? 0.97567 0.73584 1.03698 -0.12518 0.00646  0.16383  85  GLN A OE1 
565  N NE2 . GLN A 78  ? 0.94475 0.72172 1.00764 -0.14312 -0.01148 0.13001  85  GLN A NE2 
566  N N   . ASP A 79  ? 0.48229 0.16110 0.47284 -0.05706 -0.00389 0.06485  86  ASP A N   
567  C CA  . ASP A 79  ? 0.57327 0.24066 0.54816 -0.03768 -0.00316 0.04462  86  ASP A CA  
568  C C   . ASP A 79  ? 0.49523 0.19746 0.47360 -0.00900 0.00247  0.04999  86  ASP A C   
569  O O   . ASP A 79  ? 0.50191 0.19665 0.47003 0.00912  0.00476  0.03836  86  ASP A O   
570  C CB  . ASP A 79  ? 0.51502 0.20026 0.48868 -0.04950 -0.01268 0.02475  86  ASP A CB  
571  C CG  . ASP A 79  ? 0.72045 0.39074 0.69340 -0.07358 -0.01682 0.01402  86  ASP A CG  
572  O OD1 . ASP A 79  ? 0.71190 0.35248 0.68532 -0.07991 -0.01218 0.01836  86  ASP A OD1 
573  O OD2 . ASP A 79  ? 0.77147 0.46226 0.74465 -0.08535 -0.02521 0.00191  86  ASP A OD2 
574  N N   . ARG A 80  ? 0.48895 0.23064 0.48071 -0.00520 0.00458  0.06742  87  ARG A N   
575  C CA  . ARG A 80  ? 0.38096 0.16176 0.37466 0.01786  0.00718  0.07072  87  ARG A CA  
576  C C   . ARG A 80  ? 0.39018 0.19415 0.38283 0.02284  0.00151  0.05030  87  ARG A C   
577  O O   . ARG A 80  ? 0.35613 0.16695 0.34387 0.04030  0.00249  0.04390  87  ARG A O   
578  C CB  . ARG A 80  ? 0.42592 0.18846 0.41149 0.03972  0.01461  0.08080  87  ARG A CB  
579  C CG  . ARG A 80  ? 0.42343 0.22995 0.41291 0.05698  0.01697  0.09485  87  ARG A CG  
580  C CD  . ARG A 80  ? 0.55248 0.36024 0.53535 0.08191  0.02033  0.09738  87  ARG A CD  
581  N NE  . ARG A 80  ? 0.67764 0.44427 0.65512 0.09044  0.02875  0.11343  87  ARG A NE  
582  C CZ  . ARG A 80  ? 0.77304 0.53468 0.74585 0.10645  0.03057  0.10983  87  ARG A CZ  
583  N NH1 . ARG A 80  ? 0.59036 0.37672 0.56351 0.11880  0.02773  0.09740  87  ARG A NH1 
584  N NH2 . ARG A 80  ? 0.71542 0.44901 0.68481 0.10965  0.03558  0.12020  87  ARG A NH2 
585  N N   . THR A 81  ? 0.32769 0.14635 0.32678 0.00686  -0.00447 0.04225  88  THR A N   
586  C CA  . THR A 81  ? 0.29750 0.13623 0.29676 0.00974  -0.00941 0.02565  88  THR A CA  
587  C C   . THR A 81  ? 0.30414 0.18260 0.31450 0.00623  -0.01163 0.02884  88  THR A C   
588  O O   . THR A 81  ? 0.29562 0.18451 0.31494 -0.00551 -0.01126 0.04042  88  THR A O   
589  C CB  . THR A 81  ? 0.37701 0.19160 0.36972 -0.00319 -0.01422 0.01062  88  THR A CB  
590  O OG1 . THR A 81  ? 0.34962 0.15941 0.34794 -0.02551 -0.01827 0.01562  88  THR A OG1 
591  C CG2 . THR A 81  ? 0.38346 0.15626 0.36082 0.00470  -0.01025 0.00417  88  THR A CG2 
592  N N   . LEU A 82  ? 0.24473 0.14479 0.25462 0.01683  -0.01336 0.01917  89  LEU A N   
593  C CA  . LEU A 82  ? 0.22717 0.15680 0.24410 0.01596  -0.01503 0.01737  89  LEU A CA  
594  C C   . LEU A 82  ? 0.26296 0.18972 0.27979 0.01207  -0.02000 0.00283  89  LEU A C   
595  O O   . LEU A 82  ? 0.25715 0.17698 0.26838 0.01930  -0.02105 -0.00697 89  LEU A O   
596  C CB  . LEU A 82  ? 0.26111 0.21389 0.27435 0.03151  -0.01261 0.01816  89  LEU A CB  
597  C CG  . LEU A 82  ? 0.25502 0.23124 0.27119 0.03453  -0.01273 0.01374  89  LEU A CG  
598  C CD1 . LEU A 82  ? 0.22226 0.21413 0.24876 0.02713  -0.00948 0.02687  89  LEU A CD1 
599  C CD2 . LEU A 82  ? 0.24938 0.24151 0.25556 0.04921  -0.01118 0.01049  89  LEU A CD2 
600  N N   . THR A 83  ? 0.24117 0.17715 0.26543 0.00080  -0.02289 0.00375  90  THR A N   
601  C CA  . THR A 83  ? 0.22990 0.16516 0.25388 -0.00344 -0.02753 -0.00673 90  THR A CA  
602  C C   . THR A 83  ? 0.25655 0.21741 0.28820 0.00242  -0.02713 -0.00594 90  THR A C   
603  O O   . THR A 83  ? 0.22536 0.20675 0.26580 0.00168  -0.02496 0.00442  90  THR A O   
604  C CB  . THR A 83  ? 0.26782 0.19244 0.29179 -0.02135 -0.03256 -0.00660 90  THR A CB  
605  O OG1 . THR A 83  ? 0.29037 0.18173 0.30293 -0.02512 -0.03194 -0.01007 90  THR A OG1 
606  C CG2 . THR A 83  ? 0.30219 0.23152 0.32429 -0.02426 -0.03729 -0.01549 90  THR A CG2 
607  N N   . ILE A 84  ? 0.19780 0.15696 0.22647 0.00901  -0.02823 -0.01558 91  ILE A N   
608  C CA  . ILE A 84  ? 0.22683 0.20087 0.26045 0.01573  -0.02723 -0.01604 91  ILE A CA  
609  C C   . ILE A 84  ? 0.25435 0.22895 0.29100 0.00882  -0.03128 -0.01773 91  ILE A C   
610  O O   . ILE A 84  ? 0.23684 0.19890 0.26786 0.00750  -0.03329 -0.02537 91  ILE A O   
611  C CB  . ILE A 84  ? 0.22916 0.19835 0.25655 0.02691  -0.02575 -0.02470 91  ILE A CB  
612  C CG1 . ILE A 84  ? 0.33339 0.30724 0.35499 0.03437  -0.02264 -0.02257 91  ILE A CG1 
613  C CG2 . ILE A 84  ? 0.18592 0.16012 0.21586 0.03363  -0.02417 -0.02654 91  ILE A CG2 
614  C CD1 . ILE A 84  ? 0.39692 0.36107 0.41262 0.03475  -0.02421 -0.02516 91  ILE A CD1 
615  N N   . VAL A 85  ? 0.19348 0.18715 0.23942 0.00516  -0.03222 -0.00879 92  VAL A N   
616  C CA  . VAL A 85  ? 0.21332 0.21441 0.26213 -0.00139 -0.03696 -0.00740 92  VAL A CA  
617  C C   . VAL A 85  ? 0.27676 0.29055 0.33247 0.01083  -0.03359 -0.00274 92  VAL A C   
618  O O   . VAL A 85  ? 0.22113 0.24911 0.28355 0.02033  -0.02850 0.00435  92  VAL A O   
619  C CB  . VAL A 85  ? 0.22608 0.24315 0.28116 -0.01686 -0.04256 0.00099  92  VAL A CB  
620  C CG1 . VAL A 85  ? 0.23412 0.25869 0.28707 -0.02497 -0.04945 0.00025  92  VAL A CG1 
621  C CG2 . VAL A 85  ? 0.26393 0.26178 0.31197 -0.02830 -0.04424 -0.00229 92  VAL A CG2 
622  N N   . ASP A 86  ? 0.20865 0.21674 0.26198 0.01188  -0.03527 -0.00551 93  ASP A N   
623  C CA  . ASP A 86  ? 0.21005 0.22644 0.27005 0.02310  -0.03195 0.00141  93  ASP A CA  
624  C C   . ASP A 86  ? 0.23248 0.26066 0.29420 0.01711  -0.03694 0.00757  93  ASP A C   
625  O O   . ASP A 86  ? 0.24062 0.26261 0.29371 0.00623  -0.04194 0.00159  93  ASP A O   
626  C CB  . ASP A 86  ? 0.21860 0.21120 0.27312 0.03334  -0.02723 -0.00701 93  ASP A CB  
627  C CG  . ASP A 86  ? 0.33183 0.30865 0.38056 0.02668  -0.03004 -0.01421 93  ASP A CG  
628  O OD1 . ASP A 86  ? 0.27553 0.23820 0.31865 0.02535  -0.03000 -0.02386 93  ASP A OD1 
629  O OD2 . ASP A 86  ? 0.29840 0.28056 0.34883 0.02402  -0.03179 -0.00856 93  ASP A OD2 
630  N N   . THR A 87  ? 0.17672 0.22325 0.24813 0.02617  -0.03492 0.02027  94  THR A N   
631  C CA  . THR A 87  ? 0.19689 0.25914 0.26999 0.02339  -0.03933 0.02928  94  THR A CA  
632  C C   . THR A 87  ? 0.29884 0.34336 0.37066 0.03452  -0.03405 0.03134  94  THR A C   
633  O O   . THR A 87  ? 0.20900 0.26782 0.28717 0.04223  -0.03304 0.04541  94  THR A O   
634  C CB  . THR A 87  ? 0.19336 0.29472 0.28041 0.02534  -0.04167 0.04629  94  THR A CB  
635  O OG1 . THR A 87  ? 0.20243 0.30753 0.29946 0.04447  -0.03217 0.05436  94  THR A OG1 
636  C CG2 . THR A 87  ? 0.22446 0.34379 0.31347 0.00758  -0.04927 0.04521  94  THR A CG2 
637  N N   . GLY A 88  ? 0.18812 0.20240 0.25281 0.03481  -0.03088 0.01904  95  GLY A N   
638  C CA  . GLY A 88  ? 0.23690 0.23112 0.30135 0.04083  -0.02663 0.02071  95  GLY A CA  
639  C C   . GLY A 88  ? 0.26424 0.26451 0.32518 0.03345  -0.02966 0.02550  95  GLY A C   
640  O O   . GLY A 88  ? 0.23998 0.26286 0.29721 0.02631  -0.03535 0.02890  95  GLY A O   
641  N N   . ILE A 89  ? 0.25574 0.23633 0.31673 0.03408  -0.02607 0.02572  96  ILE A N   
642  C CA  . ILE A 89  ? 0.23168 0.22085 0.29028 0.02972  -0.02664 0.03429  96  ILE A CA  
643  C C   . ILE A 89  ? 0.28012 0.27713 0.32775 0.01901  -0.03042 0.02409  96  ILE A C   
644  O O   . ILE A 89  ? 0.26266 0.27448 0.30339 0.01611  -0.03152 0.03003  96  ILE A O   
645  C CB  . ILE A 89  ? 0.27455 0.23998 0.33893 0.03175  -0.02100 0.03957  96  ILE A CB  
646  C CG1 . ILE A 89  ? 0.29106 0.26937 0.35560 0.03057  -0.01951 0.05561  96  ILE A CG1 
647  C CG2 . ILE A 89  ? 0.20938 0.15647 0.27269 0.02342  -0.02115 0.02471  96  ILE A CG2 
648  C CD1 . ILE A 89  ? 0.32060 0.27526 0.39399 0.03367  -0.01331 0.06739  96  ILE A CD1 
649  N N   . GLY A 90  ? 0.22986 0.21713 0.27380 0.01498  -0.03163 0.00944  97  GLY A N   
650  C CA  . GLY A 90  ? 0.25568 0.24520 0.28826 0.00846  -0.03325 -0.00011 97  GLY A CA  
651  C C   . GLY A 90  ? 0.23453 0.21929 0.26819 0.00755  -0.02888 0.00005  97  GLY A C   
652  O O   . GLY A 90  ? 0.26218 0.23946 0.30640 0.00846  -0.02581 0.00681  97  GLY A O   
653  N N   . MET A 91  ? 0.22425 0.21296 0.24674 0.00562  -0.02821 -0.00713 98  MET A N   
654  C CA  . MET A 91  ? 0.21280 0.20542 0.23740 0.00591  -0.02301 -0.00498 98  MET A CA  
655  C C   . MET A 91  ? 0.23715 0.24299 0.24461 0.00755  -0.02074 -0.00506 98  MET A C   
656  O O   . MET A 91  ? 0.26036 0.26361 0.25093 0.00711  -0.02389 -0.01459 98  MET A O   
657  C CB  . MET A 91  ? 0.23511 0.22066 0.26413 0.00641  -0.02174 -0.01425 98  MET A CB  
658  C CG  . MET A 91  ? 0.27712 0.25065 0.31889 0.00451  -0.02429 -0.01666 98  MET A CG  
659  S SD  . MET A 91  ? 0.30633 0.27851 0.34877 0.00631  -0.02480 -0.02712 98  MET A SD  
660  C CE  . MET A 91  ? 0.26465 0.22653 0.29456 0.00946  -0.02751 -0.03504 98  MET A CE  
661  N N   . THR A 92  ? 0.27171 0.29066 0.28236 0.00876  -0.01508 0.00544  99  THR A N   
662  C CA  . THR A 92  ? 0.28340 0.31702 0.27581 0.01301  -0.01046 0.00526  99  THR A CA  
663  C C   . THR A 92  ? 0.24107 0.27143 0.22759 0.01860  -0.00535 -0.00576 99  THR A C   
664  O O   . THR A 92  ? 0.26690 0.28895 0.26703 0.01816  -0.00575 -0.00976 99  THR A O   
665  C CB  . THR A 92  ? 0.24004 0.29274 0.24014 0.01342  -0.00440 0.02384  99  THR A CB  
666  O OG1 . THR A 92  ? 0.27583 0.32930 0.29773 0.01062  -0.00002 0.02972  99  THR A OG1 
667  C CG2 . THR A 92  ? 0.25057 0.30437 0.25802 0.01075  -0.00817 0.03775  99  THR A CG2 
668  N N   . LYS A 93  ? 0.26020 0.29819 0.22439 0.02565  -0.00006 -0.01032 100 LYS A N   
669  C CA  . LYS A 93  ? 0.32644 0.36379 0.28489 0.03565  0.00785  -0.01766 100 LYS A CA  
670  C C   . LYS A 93  ? 0.30736 0.36415 0.29280 0.03634  0.01373  -0.00451 100 LYS A C   
671  O O   . LYS A 93  ? 0.27150 0.32685 0.26690 0.04039  0.01549  -0.00827 100 LYS A O   
672  C CB  . LYS A 93  ? 0.31943 0.36277 0.24718 0.04568  0.01486  -0.02346 100 LYS A CB  
673  C CG  . LYS A 93  ? 0.32819 0.36313 0.24395 0.06023  0.02398  -0.03404 100 LYS A CG  
674  C CD  . LYS A 93  ? 0.40680 0.44611 0.28816 0.07279  0.03289  -0.04072 100 LYS A CD  
675  C CE  . LYS A 93  ? 0.47477 0.49955 0.34126 0.09090  0.04342  -0.05213 100 LYS A CE  
676  N NZ  . LYS A 93  ? 0.49090 0.53294 0.33295 0.10836  0.05749  -0.05188 100 LYS A NZ  
677  N N   . ALA A 94  ? 0.27923 0.35605 0.27748 0.03147  0.01638  0.01253  101 ALA A N   
678  C CA  . ALA A 94  ? 0.33160 0.42775 0.35779 0.02730  0.02051  0.02641  101 ALA A CA  
679  C C   . ALA A 94  ? 0.27536 0.35588 0.32251 0.01728  0.01197  0.02265  101 ALA A C   
680  O O   . ALA A 94  ? 0.31625 0.40830 0.38007 0.01606  0.01277  0.02415  101 ALA A O   
681  C CB  . ALA A 94  ? 0.30011 0.41485 0.33632 0.02117  0.02430  0.04703  101 ALA A CB  
682  N N   . ASP A 95  ? 0.22297 0.28032 0.26856 0.01101  0.00383  0.01805  102 ASP A N   
683  C CA  . ASP A 95  ? 0.25548 0.29597 0.31520 0.00369  -0.00355 0.01227  102 ASP A CA  
684  C C   . ASP A 95  ? 0.24314 0.27994 0.29853 0.00981  -0.00494 -0.00076 102 ASP A C   
685  O O   . ASP A 95  ? 0.26666 0.30802 0.33681 0.00587  -0.00772 -0.00147 102 ASP A O   
686  C CB  . ASP A 95  ? 0.25881 0.27742 0.31386 0.00100  -0.00962 0.00943  102 ASP A CB  
687  C CG  . ASP A 95  ? 0.31782 0.33528 0.38153 -0.00414 -0.00859 0.02449  102 ASP A CG  
688  O OD1 . ASP A 95  ? 0.32251 0.34516 0.40260 -0.01166 -0.00626 0.03502  102 ASP A OD1 
689  O OD2 . ASP A 95  ? 0.42411 0.43539 0.47957 -0.00117 -0.01049 0.02706  102 ASP A OD2 
690  N N   . LEU A 96  ? 0.26631 0.29373 0.30070 0.01860  -0.00374 -0.01076 103 LEU A N   
691  C CA  . LEU A 96  ? 0.29051 0.31013 0.31909 0.02612  -0.00362 -0.02100 103 LEU A CA  
692  C C   . LEU A 96  ? 0.27341 0.31599 0.31321 0.03293  0.00250  -0.01549 103 LEU A C   
693  O O   . LEU A 96  ? 0.27045 0.31700 0.32150 0.03353  -0.00038 -0.01668 103 LEU A O   
694  C CB  . LEU A 96  ? 0.26073 0.26399 0.26306 0.03334  -0.00170 -0.03131 103 LEU A CB  
695  C CG  . LEU A 96  ? 0.27852 0.26075 0.27074 0.02682  -0.00922 -0.03862 103 LEU A CG  
696  C CD1 . LEU A 96  ? 0.29340 0.25911 0.25888 0.03115  -0.00770 -0.04963 103 LEU A CD1 
697  C CD2 . LEU A 96  ? 0.25116 0.22304 0.25444 0.02411  -0.01431 -0.04138 103 LEU A CD2 
698  N N   . ILE A 97  ? 0.24469 0.30729 0.28171 0.03900  0.01123  -0.00791 104 ILE A N   
699  C CA  . ILE A 97  ? 0.26127 0.35289 0.31034 0.04801  0.01891  -0.00001 104 ILE A CA  
700  C C   . ILE A 97  ? 0.27128 0.38521 0.35151 0.03410  0.01341  0.01105  104 ILE A C   
701  O O   . ILE A 97  ? 0.25581 0.38973 0.35064 0.03718  0.01302  0.01419  104 ILE A O   
702  C CB  . ILE A 97  ? 0.30994 0.42073 0.34758 0.05858  0.03094  0.00678  104 ILE A CB  
703  C CG1 . ILE A 97  ? 0.28284 0.36754 0.28496 0.07251  0.03551  -0.00840 104 ILE A CG1 
704  C CG2 . ILE A 97  ? 0.21310 0.36346 0.26912 0.06787  0.04015  0.01967  104 ILE A CG2 
705  C CD1 . ILE A 97  ? 0.27554 0.37232 0.25682 0.08120  0.04537  -0.00577 104 ILE A CD1 
706  N N   . ASN A 98  ? 0.20914 0.31915 0.29942 0.01822  0.00855  0.01733  105 ASN A N   
707  C CA  . ASN A 98  ? 0.29489 0.41674 0.41171 0.00109  0.00179  0.02533  105 ASN A CA  
708  C C   . ASN A 98  ? 0.24393 0.34104 0.36051 -0.00603 -0.00958 0.01258  105 ASN A C   
709  O O   . ASN A 98  ? 0.25415 0.33059 0.37428 -0.01873 -0.01617 0.01073  105 ASN A O   
710  C CB  . ASN A 98  ? 0.27052 0.39267 0.39679 -0.01199 0.00280  0.03839  105 ASN A CB  
711  C CG  . ASN A 98  ? 0.59958 0.75397 0.72828 -0.00558 0.01472  0.05420  105 ASN A CG  
712  O OD1 . ASN A 98  ? 0.71223 0.86304 0.81978 0.00590  0.02154  0.05357  105 ASN A OD1 
713  N ND2 . ASN A 98  ? 0.58276 0.77225 0.73702 -0.01357 0.01705  0.06898  105 ASN A ND2 
714  N N   . ASN A 99  ? 0.23206 0.33083 0.34245 0.00469  -0.01052 0.00440  106 ASN A N   
715  C CA  . ASN A 99  ? 0.22036 0.30537 0.33041 0.00051  -0.02016 -0.00570 106 ASN A CA  
716  C C   . ASN A 99  ? 0.24711 0.29610 0.34348 -0.00314 -0.02449 -0.01524 106 ASN A C   
717  O O   . ASN A 99  ? 0.23386 0.26987 0.33338 -0.01287 -0.03217 -0.02056 106 ASN A O   
718  C CB  . ASN A 99  ? 0.16610 0.27182 0.29793 -0.01515 -0.02837 -0.00125 106 ASN A CB  
719  C CG  . ASN A 99  ? 0.15449 0.30482 0.30331 -0.01026 -0.02448 0.01054  106 ASN A CG  
720  O OD1 . ASN A 99  ? 0.19338 0.35421 0.33578 0.00755  -0.01956 0.01003  106 ASN A OD1 
721  N ND2 . ASN A 99  ? 0.16530 0.34237 0.33675 -0.02538 -0.02587 0.02289  106 ASN A ND2 
722  N N   . LEU A 100 ? 0.22425 0.25858 0.30419 0.00538  -0.01946 -0.01768 107 LEU A N   
723  C CA  . LEU A 100 ? 0.28803 0.29595 0.35655 0.00416  -0.02271 -0.02418 107 LEU A CA  
724  C C   . LEU A 100 ? 0.30416 0.30137 0.38130 -0.00681 -0.02631 -0.02078 107 LEU A C   
725  O O   . LEU A 100 ? 0.25374 0.23266 0.32789 -0.00861 -0.03073 -0.02709 107 LEU A O   
726  C CB  . LEU A 100 ? 0.25018 0.24695 0.31140 0.00879  -0.02661 -0.03347 107 LEU A CB  
727  C CG  . LEU A 100 ? 0.31820 0.31877 0.37018 0.02060  -0.02193 -0.03530 107 LEU A CG  
728  C CD1 . LEU A 100 ? 0.32792 0.34579 0.38894 0.02459  -0.02337 -0.03385 107 LEU A CD1 
729  C CD2 . LEU A 100 ? 0.33862 0.31786 0.37544 0.02432  -0.02239 -0.04159 107 LEU A CD2 
730  N N   . GLY A 101 ? 0.24888 0.25649 0.33614 -0.01302 -0.02322 -0.00974 108 GLY A N   
731  C CA  . GLY A 101 ? 0.30517 0.29701 0.39965 -0.02246 -0.02497 -0.00414 108 GLY A CA  
732  C C   . GLY A 101 ? 0.35338 0.33434 0.45818 -0.03472 -0.03181 -0.00884 108 GLY A C   
733  O O   . GLY A 101 ? 0.35682 0.31223 0.46209 -0.04024 -0.03349 -0.00880 108 GLY A O   
734  N N   . THR A 102 ? 0.24963 0.24868 0.36136 -0.03870 -0.03600 -0.01302 109 THR A N   
735  C CA  . THR A 102 ? 0.27675 0.26917 0.39600 -0.05294 -0.04491 -0.01943 109 THR A CA  
736  C C   . THR A 102 ? 0.29358 0.31179 0.43472 -0.06850 -0.04640 -0.00765 109 THR A C   
737  O O   . THR A 102 ? 0.28558 0.33330 0.43568 -0.06408 -0.03937 0.00509  109 THR A O   
738  C CB  . THR A 102 ? 0.31154 0.31127 0.42292 -0.04752 -0.05080 -0.03171 109 THR A CB  
739  O OG1 . THR A 102 ? 0.26807 0.30468 0.38838 -0.04256 -0.04895 -0.02513 109 THR A OG1 
740  C CG2 . THR A 102 ? 0.29687 0.27838 0.38944 -0.03212 -0.04775 -0.03952 109 THR A CG2 
741  N N   . ILE A 103 ? 0.22481 0.23187 0.37381 -0.08741 -0.05552 -0.01206 110 ILE A N   
742  C CA  . ILE A 103 ? 0.23264 0.26999 0.40543 -0.10653 -0.06003 -0.00152 110 ILE A CA  
743  C C   . ILE A 103 ? 0.22583 0.29294 0.40145 -0.10782 -0.06910 -0.00931 110 ILE A C   
744  O O   . ILE A 103 ? 0.24540 0.31301 0.42682 -0.12726 -0.08144 -0.01618 110 ILE A O   
745  C CB  . ILE A 103 ? 0.34907 0.35626 0.53014 -0.13052 -0.06565 -0.00009 110 ILE A CB  
746  C CG1 . ILE A 103 ? 0.35619 0.31863 0.51482 -0.13320 -0.07301 -0.02184 110 ILE A CG1 
747  C CG2 . ILE A 103 ? 0.37014 0.35854 0.55288 -0.12709 -0.05487 0.01471  110 ILE A CG2 
748  C CD1 . ILE A 103 ? 0.44007 0.37400 0.59415 -0.15182 -0.07355 -0.02463 110 ILE A CD1 
749  N N   . ALA A 104 ? 0.31571 0.15877 0.35081 0.03076  0.02160  0.04570  111 ALA A N   
750  C CA  . ALA A 104 ? 0.28961 0.17272 0.35802 0.04745  0.02446  0.04930  111 ALA A CA  
751  C C   . ALA A 104 ? 0.26230 0.21691 0.36095 0.03024  0.04119  0.03235  111 ALA A C   
752  O O   . ALA A 104 ? 0.25030 0.27268 0.36583 0.02212  0.03456  0.01279  111 ALA A O   
753  C CB  . ALA A 104 ? 0.35116 0.25818 0.37527 0.06049  -0.01070 0.04635  111 ALA A CB  
754  N N   . LYS A 105 ? 0.31584 0.27229 0.41154 0.01704  0.05845  0.03323  112 LYS A N   
755  C CA  . LYS A 105 ? 0.27844 0.32887 0.39975 -0.00668 0.07065  0.00993  112 LYS A CA  
756  C C   . LYS A 105 ? 0.33644 0.40689 0.47794 -0.05191 0.08470  -0.02031 112 LYS A C   
757  O O   . LYS A 105 ? 0.28614 0.44038 0.45050 -0.06205 0.07727  -0.04076 112 LYS A O   
758  C CB  . LYS A 105 ? 0.30544 0.35152 0.41807 -0.01720 0.09168  0.01602  112 LYS A CB  
759  C CG  . LYS A 105 ? 0.48431 0.64660 0.62948 -0.02926 0.10129  -0.00374 112 LYS A CG  
760  C CD  . LYS A 105 ? 0.40615 0.56087 0.54541 -0.06380 0.13386  -0.00692 112 LYS A CD  
761  C CE  . LYS A 105 ? 0.57781 0.85125 0.76075 -0.09928 0.15037  -0.03574 112 LYS A CE  
762  N NZ  . LYS A 105 ? 0.62925 1.01417 0.85226 -0.07414 0.12616  -0.04905 112 LYS A NZ  
763  N N   . SER A 106 ? 0.30726 0.29553 0.43601 -0.07934 0.10277  -0.02354 113 SER A N   
764  C CA  . SER A 106 ? 0.33466 0.32780 0.47419 -0.12281 0.11664  -0.05367 113 SER A CA  
765  C C   . SER A 106 ? 0.31698 0.30833 0.46127 -0.11134 0.10329  -0.06441 113 SER A C   
766  O O   . SER A 106 ? 0.33194 0.36245 0.48645 -0.14137 0.10815  -0.09272 113 SER A O   
767  C CB  . SER A 106 ? 0.48001 0.37393 0.59733 -0.15367 0.13817  -0.05414 113 SER A CB  
768  O OG  . SER A 106 ? 0.53133 0.33951 0.62320 -0.11558 0.12210  -0.03080 113 SER A OG  
769  N N   . GLY A 107 ? 0.30861 0.25634 0.44317 -0.07170 0.08732  -0.04301 114 GLY A N   
770  C CA  . GLY A 107 ? 0.31919 0.27444 0.45751 -0.06227 0.07705  -0.05314 114 GLY A CA  
771  C C   . GLY A 107 ? 0.32485 0.37693 0.46983 -0.05882 0.05929  -0.06206 114 GLY A C   
772  O O   . GLY A 107 ? 0.27049 0.35183 0.41773 -0.07761 0.05945  -0.08564 114 GLY A O   
773  N N   . THR A 108 ? 0.21847 0.31701 0.36263 -0.03370 0.04252  -0.04377 115 THR A N   
774  C CA  . THR A 108 ? 0.20925 0.39786 0.35872 -0.02659 0.02078  -0.05065 115 THR A CA  
775  C C   . THR A 108 ? 0.22338 0.48376 0.39507 -0.06803 0.03047  -0.08185 115 THR A C   
776  O O   . THR A 108 ? 0.24075 0.55407 0.41293 -0.07955 0.01683  -0.09840 115 THR A O   
777  C CB  . THR A 108 ? 0.18165 0.39862 0.32664 0.01193  0.00254  -0.02691 115 THR A CB  
778  O OG1 . THR A 108 ? 0.25855 0.40615 0.37627 0.04662  -0.01014 0.00218  115 THR A OG1 
779  C CG2 . THR A 108 ? 0.20765 0.51476 0.35866 0.02369  -0.02397 -0.03368 115 THR A CG2 
780  N N   . LYS A 109 ? 0.23311 0.49527 0.41928 -0.09439 0.05296  -0.08954 116 LYS A N   
781  C CA  . LYS A 109 ? 0.25513 0.58289 0.46242 -0.14152 0.06388  -0.11929 116 LYS A CA  
782  C C   . LYS A 109 ? 0.28301 0.58548 0.47883 -0.17460 0.06980  -0.14484 116 LYS A C   
783  O O   . LYS A 109 ? 0.31836 0.67870 0.51280 -0.19068 0.05795  -0.16236 116 LYS A O   
784  C CB  . LYS A 109 ? 0.28520 0.59322 0.49929 -0.17115 0.09182  -0.12133 116 LYS A CB  
785  C CG  . LYS A 109 ? 0.44396 0.81059 0.66626 -0.20973 0.09758  -0.14269 116 LYS A CG  
786  C CD  . LYS A 109 ? 0.49418 0.81140 0.70418 -0.24029 0.12434  -0.14199 116 LYS A CD  
787  C CE  . LYS A 109 ? 0.59981 0.99022 0.82082 -0.26689 0.12680  -0.15564 116 LYS A CE  
788  N NZ  . LYS A 109 ? 0.54779 0.96584 0.76266 -0.29060 0.11738  -0.17837 116 LYS A NZ  
789  N N   . ALA A 110 ? 0.30785 0.51009 0.48476 -0.17713 0.08621  -0.14409 117 ALA A N   
790  C CA  . ALA A 110 ? 0.38448 0.55398 0.54848 -0.20504 0.09619  -0.17139 117 ALA A CA  
791  C C   . ALA A 110 ? 0.34123 0.54341 0.49545 -0.18671 0.07608  -0.17420 117 ALA A C   
792  O O   . ALA A 110 ? 0.34603 0.57430 0.48736 -0.21181 0.07536  -0.19819 117 ALA A O   
793  C CB  . ALA A 110 ? 0.38539 0.43960 0.53533 -0.20157 0.11613  -0.16860 117 ALA A CB  
794  N N   . PHE A 111 ? 0.30952 0.50202 0.45849 -0.14157 0.05877  -0.14616 118 PHE A N   
795  C CA  . PHE A 111 ? 0.26715 0.48219 0.39870 -0.12670 0.03970  -0.14526 118 PHE A CA  
796  C C   . PHE A 111 ? 0.31630 0.62494 0.44626 -0.14053 0.01684  -0.15637 118 PHE A C   
797  O O   . PHE A 111 ? 0.29403 0.62258 0.40479 -0.16050 0.01141  -0.17560 118 PHE A O   
798  C CB  . PHE A 111 ? 0.23249 0.41981 0.35552 -0.07964 0.02293  -0.10980 118 PHE A CB  
799  C CG  . PHE A 111 ? 0.25142 0.45344 0.34965 -0.06659 0.00323  -0.10448 118 PHE A CG  
800  C CD1 . PHE A 111 ? 0.31683 0.51095 0.40177 -0.08996 0.01487  -0.12896 118 PHE A CD1 
801  C CD2 . PHE A 111 ? 0.27293 0.48949 0.35496 -0.03209 -0.02578 -0.07498 118 PHE A CD2 
802  C CE1 . PHE A 111 ? 0.32597 0.53248 0.38215 -0.08297 -0.00094 -0.12348 118 PHE A CE1 
803  C CE2 . PHE A 111 ? 0.26211 0.48442 0.31270 -0.02500 -0.04469 -0.06802 118 PHE A CE2 
804  C CZ  . PHE A 111 ? 0.28926 0.50891 0.32705 -0.05230 -0.03153 -0.09190 118 PHE A CZ  
805  N N   . MET A 112 ? 0.27795 0.64637 0.42792 -0.13021 0.00305  -0.14565 119 MET A N   
806  C CA  . MET A 112 ? 0.43676 0.87411 0.57830 -0.12647 -0.02130 -0.14577 119 MET A CA  
807  C C   . MET A 112 ? 0.40019 0.85897 0.53935 -0.16771 -0.00869 -0.17120 119 MET A C   
808  O O   . MET A 112 ? 0.37015 0.86420 0.49336 -0.17103 -0.02484 -0.17412 119 MET A O   
809  C CB  . MET A 112 ? 0.48545 0.96179 0.64412 -0.09276 -0.03571 -0.12436 119 MET A CB  
810  C CG  . MET A 112 ? 0.21590 0.67060 0.34912 -0.04426 -0.06166 -0.09457 119 MET A CG  
811  S SD  . MET A 112 ? 0.75584 1.22807 0.90181 -0.00494 -0.06899 -0.07352 119 MET A SD  
812  C CE  . MET A 112 ? 0.39749 0.78043 0.50359 0.03744  -0.08080 -0.03943 119 MET A CE  
813  N N   . GLU A 113 ? 0.32283 0.75225 0.47308 -0.19873 0.01932  -0.18676 120 GLU A N   
814  C CA  . GLU A 113 ? 0.48123 0.91478 0.61846 -0.23867 0.03182  -0.21051 120 GLU A CA  
815  C C   . GLU A 113 ? 0.52405 0.91793 0.62894 -0.25154 0.03783  -0.22591 120 GLU A C   
816  O O   . GLU A 113 ? 0.48650 0.90628 0.57316 -0.27241 0.03338  -0.23881 120 GLU A O   
817  C CB  . GLU A 113 ? 0.49262 0.88523 0.63708 -0.26600 0.05977  -0.21954 120 GLU A CB  
818  C CG  . GLU A 113 ? 0.68783 1.12890 0.86002 -0.26423 0.05876  -0.20915 120 GLU A CG  
819  C CD  . GLU A 113 ? 0.90062 1.28503 1.07024 -0.29015 0.08666  -0.21278 120 GLU A CD  
820  O OE1 . GLU A 113 ? 0.91469 1.22544 1.05880 -0.31113 0.10428  -0.22567 120 GLU A OE1 
821  O OE2 . GLU A 113 ? 0.96660 1.37655 1.15567 -0.28770 0.09107  -0.20195 120 GLU A OE2 
822  N N   . ALA A 114 ? 0.39131 0.72281 0.49005 -0.23913 0.04904  -0.22469 121 ALA A N   
823  C CA  . ALA A 114 ? 0.41989 0.71496 0.48998 -0.24766 0.05886  -0.24011 121 ALA A CA  
824  C C   . ALA A 114 ? 0.47747 0.81891 0.52590 -0.23689 0.03303  -0.23162 121 ALA A C   
825  O O   . ALA A 114 ? 0.51425 0.85469 0.53546 -0.25624 0.03757  -0.24582 121 ALA A O   
826  C CB  . ALA A 114 ? 0.40603 0.62845 0.48138 -0.23065 0.07578  -0.23879 121 ALA A CB  
827  N N   . LEU A 115 ? 0.37642 0.75122 0.43237 -0.20466 0.00566  -0.20572 122 LEU A N   
828  C CA  . LEU A 115 ? 0.39825 0.79748 0.42678 -0.18959 -0.02051 -0.19062 122 LEU A CA  
829  C C   . LEU A 115 ? 0.60253 1.04755 0.62381 -0.20853 -0.03229 -0.19728 122 LEU A C   
830  O O   . LEU A 115 ? 0.48289 0.92738 0.47347 -0.21781 -0.04071 -0.19912 122 LEU A O   
831  C CB  . LEU A 115 ? 0.35316 0.76209 0.38690 -0.14635 -0.04710 -0.15791 122 LEU A CB  
832  C CG  . LEU A 115 ? 0.30723 0.67163 0.33655 -0.12433 -0.04487 -0.14498 122 LEU A CG  
833  C CD1 . LEU A 115 ? 0.30256 0.66762 0.33378 -0.08055 -0.06945 -0.11010 122 LEU A CD1 
834  C CD2 . LEU A 115 ? 0.33924 0.67345 0.33216 -0.13144 -0.04149 -0.14790 122 LEU A CD2 
835  N N   . GLN A 116 ? 0.48450 0.96980 0.53390 -0.21604 -0.03330 -0.20089 123 GLN A N   
836  C CA  . GLN A 116 ? 0.58877 1.12117 0.63617 -0.23752 -0.04443 -0.20977 123 GLN A CA  
837  C C   . GLN A 116 ? 0.59971 1.11143 0.62851 -0.28259 -0.02067 -0.23819 123 GLN A C   
838  O O   . GLN A 116 ? 0.70339 1.25184 0.72845 -0.30648 -0.02876 -0.24772 123 GLN A O   
839  C CB  . GLN A 116 ? 0.62413 1.21254 0.71049 -0.23089 -0.05214 -0.20485 123 GLN A CB  
840  C CG  . GLN A 116 ? 0.64368 1.25755 0.74345 -0.18428 -0.08000 -0.17776 123 GLN A CG  
841  C CD  . GLN A 116 ? 0.99043 1.67221 1.11294 -0.18090 -0.10129 -0.17624 123 GLN A CD  
842  O OE1 . GLN A 116 ? 1.05073 1.76803 1.17941 -0.21562 -0.09795 -0.19431 123 GLN A OE1 
843  N NE2 . GLN A 116 ? 0.84116 1.53704 0.97544 -0.13881 -0.12347 -0.15505 123 GLN A NE2 
844  N N   . ALA A 117 ? 0.74002 1.19010 0.75648 -0.29309 0.00770  -0.25188 124 ALA A N   
845  C CA  . ALA A 117 ? 0.69483 1.11001 0.69157 -0.33101 0.03393  -0.27893 124 ALA A CA  
846  C C   . ALA A 117 ? 0.85772 1.22168 0.82394 -0.33264 0.05008  -0.28926 124 ALA A C   
847  O O   . ALA A 117 ? 0.78295 1.09497 0.73902 -0.35076 0.07913  -0.31013 124 ALA A O   
848  C CB  . ALA A 117 ? 0.61697 0.99651 0.63239 -0.34362 0.05881  -0.28881 124 ALA A CB  
849  N N   . GLY A 118 ? 0.68611 1.06117 0.63679 -0.31256 0.03208  -0.27399 125 GLY A N   
850  C CA  . GLY A 118 ? 0.75293 1.09178 0.67365 -0.31678 0.04643  -0.28293 125 GLY A CA  
851  C C   . GLY A 118 ? 0.61470 0.92707 0.54101 -0.28661 0.04876  -0.26932 125 GLY A C   
852  O O   . GLY A 118 ? 0.58531 0.88835 0.48546 -0.28497 0.04896  -0.26685 125 GLY A O   
853  N N   . ALA A 119 ? 0.52480 0.82464 0.48268 -0.26497 0.05013  -0.25998 126 ALA A N   
854  C CA  . ALA A 119 ? 0.48973 0.75792 0.45444 -0.23937 0.05482  -0.25033 126 ALA A CA  
855  C C   . ALA A 119 ? 0.43801 0.73241 0.38445 -0.21575 0.02268  -0.22058 126 ALA A C   
856  O O   . ALA A 119 ? 0.47608 0.80756 0.41308 -0.21101 -0.00505 -0.20414 126 ALA A O   
857  C CB  . ALA A 119 ? 0.43619 0.67804 0.43802 -0.22408 0.06223  -0.24662 126 ALA A CB  
858  N N   . ASP A 120 ? 0.47988 0.74767 0.42137 -0.19875 0.02661  -0.21246 127 ASP A N   
859  C CA  . ASP A 120 ? 0.40990 0.68570 0.33110 -0.17347 -0.00276 -0.17932 127 ASP A CA  
860  C C   . ASP A 120 ? 0.34682 0.60161 0.28779 -0.14649 -0.00592 -0.16525 127 ASP A C   
861  O O   . ASP A 120 ? 0.38272 0.61130 0.35549 -0.14745 0.01646  -0.18259 127 ASP A O   
862  C CB  . ASP A 120 ? 0.52113 0.78709 0.40488 -0.18433 0.00148  -0.17860 127 ASP A CB  
863  C CG  . ASP A 120 ? 0.58011 0.81833 0.47123 -0.19306 0.03663  -0.20157 127 ASP A CG  
864  O OD1 . ASP A 120 ? 0.80097 1.02522 0.70816 -0.21114 0.06702  -0.23286 127 ASP A OD1 
865  O OD2 . ASP A 120 ? 0.65630 0.88300 0.53871 -0.17958 0.03424  -0.18729 127 ASP A OD2 
866  N N   . ILE A 121 ? 0.33347 0.58524 0.25522 -0.11957 -0.03348 -0.12974 128 ILE A N   
867  C CA  . ILE A 121 ? 0.34802 0.58210 0.28302 -0.08981 -0.04453 -0.10742 128 ILE A CA  
868  C C   . ILE A 121 ? 0.32754 0.51819 0.28160 -0.08595 -0.01485 -0.11208 128 ILE A C   
869  O O   . ILE A 121 ? 0.30067 0.45631 0.28689 -0.05992 -0.00964 -0.09383 128 ILE A O   
870  C CB  . ILE A 121 ? 0.35687 0.56734 0.26466 -0.05961 -0.07464 -0.06418 128 ILE A CB  
871  C CG1 . ILE A 121 ? 0.44030 0.66141 0.35584 -0.04586 -0.09339 -0.05387 128 ILE A CG1 
872  C CG2 . ILE A 121 ? 0.34222 0.51412 0.25175 -0.03151 -0.08191 -0.03611 128 ILE A CG2 
873  C CD1 . ILE A 121 ? 0.52217 0.69460 0.40951 -0.02411 -0.11889 -0.02783 128 ILE A CD1 
874  N N   . SER A 122 ? 0.37447 0.56483 0.31247 -0.11004 0.00695  -0.13632 129 SER A N   
875  C CA  . SER A 122 ? 0.45262 0.60887 0.41837 -0.10127 0.03645  -0.14099 129 SER A CA  
876  C C   . SER A 122 ? 0.42691 0.54614 0.44489 -0.09142 0.06313  -0.15581 129 SER A C   
877  O O   . SER A 122 ? 0.40128 0.48765 0.45226 -0.07197 0.07895  -0.15073 129 SER A O   
878  C CB  . SER A 122 ? 0.35261 0.52259 0.29295 -0.13029 0.06016  -0.17066 129 SER A CB  
879  O OG  . SER A 122 ? 0.45720 0.62729 0.40164 -0.15570 0.08636  -0.21265 129 SER A OG  
880  N N   . MET A 123 ? 0.32691 0.44949 0.35181 -0.10585 0.06679  -0.17339 130 MET A N   
881  C CA  . MET A 123 ? 0.33985 0.41723 0.40305 -0.10162 0.09020  -0.18660 130 MET A CA  
882  C C   . MET A 123 ? 0.30158 0.35818 0.38626 -0.07663 0.07448  -0.15471 130 MET A C   
883  O O   . MET A 123 ? 0.30507 0.32290 0.41200 -0.07840 0.08952  -0.16267 130 MET A O   
884  C CB  . MET A 123 ? 0.43498 0.51888 0.48833 -0.13868 0.10687  -0.22592 130 MET A CB  
885  C CG  . MET A 123 ? 0.53358 0.64797 0.54997 -0.16766 0.11489  -0.25339 130 MET A CG  
886  S SD  . MET A 123 ? 0.57958 0.72206 0.57511 -0.20516 0.11644  -0.27073 130 MET A SD  
887  C CE  . MET A 123 ? 0.54879 0.63069 0.57616 -0.20641 0.14513  -0.28613 130 MET A CE  
888  N N   . ILE A 124 ? 0.27281 0.34680 0.34521 -0.05429 0.04534  -0.11911 131 ILE A N   
889  C CA  . ILE A 124 ? 0.25563 0.31048 0.34068 -0.02996 0.03071  -0.08912 131 ILE A CA  
890  C C   . ILE A 124 ? 0.25406 0.24297 0.36972 -0.01358 0.04762  -0.08222 131 ILE A C   
891  O O   . ILE A 124 ? 0.24773 0.20906 0.37419 -0.00836 0.04876  -0.07256 131 ILE A O   
892  C CB  . ILE A 124 ? 0.26161 0.33229 0.32104 -0.00560 -0.00219 -0.05358 131 ILE A CB  
893  C CG1 . ILE A 124 ? 0.27937 0.33189 0.34514 0.01937  -0.01617 -0.02574 131 ILE A CG1 
894  C CG2 . ILE A 124 ? 0.23707 0.28486 0.29158 0.00569  -0.00247 -0.04019 131 ILE A CG2 
895  C CD1 . ILE A 124 ? 0.25635 0.32327 0.28972 0.04338  -0.05041 0.00496  131 ILE A CD1 
896  N N   . GLY A 125 ? 0.28702 0.25114 0.41671 -0.00547 0.06018  -0.08686 132 GLY A N   
897  C CA  . GLY A 125 ? 0.34459 0.24721 0.50539 0.01478  0.07021  -0.07818 132 GLY A CA  
898  C C   . GLY A 125 ? 0.40785 0.28651 0.56956 -0.00007 0.08441  -0.09104 132 GLY A C   
899  O O   . GLY A 125 ? 0.40925 0.26320 0.56063 0.01145  0.07304  -0.06653 132 GLY A O   
900  N N   . GLN A 126 ? 0.32037 0.20948 0.48076 -0.02873 0.10535  -0.13095 133 GLN A N   
901  C CA  . GLN A 126 ? 0.35612 0.21834 0.51290 -0.04348 0.11750  -0.14085 133 GLN A CA  
902  C C   . GLN A 126 ? 0.36755 0.21910 0.51662 -0.05100 0.11028  -0.12780 133 GLN A C   
903  O O   . GLN A 126 ? 0.41022 0.23358 0.55067 -0.06242 0.11774  -0.13134 133 GLN A O   
904  C CB  . GLN A 126 ? 0.42009 0.30190 0.56633 -0.07633 0.13774  -0.18260 133 GLN A CB  
905  C CG  . GLN A 126 ? 0.43939 0.33099 0.59018 -0.07265 0.15058  -0.19956 133 GLN A CG  
906  C CD  . GLN A 126 ? 0.55837 0.47589 0.68652 -0.10746 0.16663  -0.23669 133 GLN A CD  
907  O OE1 . GLN A 126 ? 0.60817 0.51440 0.72360 -0.12973 0.17334  -0.24941 133 GLN A OE1 
908  N NE2 . GLN A 126 ? 0.63627 0.58948 0.75331 -0.11432 0.17145  -0.25157 133 GLN A NE2 
909  N N   . PHE A 127 ? 0.33166 0.20302 0.48275 -0.04537 0.09640  -0.11446 134 PHE A N   
910  C CA  . PHE A 127 ? 0.38271 0.25307 0.53119 -0.05398 0.09240  -0.10345 134 PHE A CA  
911  C C   . PHE A 127 ? 0.38766 0.23595 0.52700 -0.01988 0.07291  -0.05929 134 PHE A C   
912  O O   . PHE A 127 ? 0.39354 0.24130 0.53134 -0.02185 0.07066  -0.04777 134 PHE A O   
913  C CB  . PHE A 127 ? 0.28708 0.24571 0.42603 -0.06923 0.07920  -0.10890 134 PHE A CB  
914  C CG  . PHE A 127 ? 0.31413 0.30933 0.44711 -0.10443 0.08974  -0.14637 134 PHE A CG  
915  C CD1 . PHE A 127 ? 0.43361 0.41951 0.56693 -0.14230 0.10777  -0.17248 134 PHE A CD1 
916  C CD2 . PHE A 127 ? 0.33538 0.36640 0.45588 -0.10351 0.08226  -0.15573 134 PHE A CD2 
917  C CE1 . PHE A 127 ? 0.46798 0.48174 0.58917 -0.17635 0.11619  -0.20672 134 PHE A CE1 
918  C CE2 . PHE A 127 ? 0.36900 0.42776 0.47629 -0.13814 0.09195  -0.19080 134 PHE A CE2 
919  C CZ  . PHE A 127 ? 0.38971 0.43930 0.49803 -0.17452 0.10849  -0.21727 134 PHE A CZ  
920  N N   . GLY A 128 ? 0.35438 0.19643 0.47819 0.00444  0.05664  -0.03753 135 GLY A N   
921  C CA  . GLY A 128 ? 0.39210 0.22623 0.47653 0.02206  0.03160  -0.00815 135 GLY A CA  
922  C C   . GLY A 128 ? 0.35489 0.21307 0.42173 0.03428  0.01556  0.00919  135 GLY A C   
923  O O   . GLY A 128 ? 0.39497 0.25202 0.44986 0.03904  0.00823  0.02324  135 GLY A O   
924  N N   . VAL A 129 ? 0.27562 0.15856 0.36144 0.03870  0.01530  0.00719  136 VAL A N   
925  C CA  . VAL A 129 ? 0.26363 0.16929 0.31357 0.05313  -0.00484 0.02268  136 VAL A CA  
926  C C   . VAL A 129 ? 0.27273 0.19499 0.30763 0.05999  -0.01304 0.02516  136 VAL A C   
927  O O   . VAL A 129 ? 0.24289 0.19697 0.26054 0.06536  -0.02065 0.03217  136 VAL A O   
928  C CB  . VAL A 129 ? 0.25721 0.19530 0.34777 0.06010  -0.00628 0.02641  136 VAL A CB  
929  C CG1 . VAL A 129 ? 0.32182 0.23791 0.41793 0.05294  0.00750  0.02826  136 VAL A CG1 
930  C CG2 . VAL A 129 ? 0.26847 0.26063 0.37242 0.03166  0.00363  -0.00722 136 VAL A CG2 
931  N N   . GLY A 130 ? 0.29099 0.22602 0.29622 -0.01532 -0.02420 -0.06198 137 GLY A N   
932  C CA  . GLY A 130 ? 0.26421 0.20850 0.25362 -0.00012 -0.01852 -0.06221 137 GLY A CA  
933  C C   . GLY A 130 ? 0.25982 0.21980 0.25456 0.00047  -0.00772 -0.04893 137 GLY A C   
934  O O   . GLY A 130 ? 0.27424 0.24578 0.26082 0.00938  -0.00332 -0.04542 137 GLY A O   
935  N N   . PHE A 131 ? 0.21924 0.17916 0.22697 -0.00851 -0.00408 -0.04123 138 PHE A N   
936  C CA  . PHE A 131 ? 0.22926 0.20038 0.24245 -0.00816 0.00295  -0.03198 138 PHE A CA  
937  C C   . PHE A 131 ? 0.24098 0.22425 0.25409 -0.00624 0.00229  -0.03067 138 PHE A C   
938  O O   . PHE A 131 ? 0.21610 0.20444 0.22837 -0.00140 0.00687  -0.02403 138 PHE A O   
939  C CB  . PHE A 131 ? 0.24951 0.22021 0.27282 -0.01629 0.00451  -0.02723 138 PHE A CB  
940  C CG  . PHE A 131 ? 0.28589 0.26629 0.31435 -0.01602 0.00777  -0.02253 138 PHE A CG  
941  C CD1 . PHE A 131 ? 0.25657 0.23699 0.28685 -0.01285 0.01086  -0.01833 138 PHE A CD1 
942  C CD2 . PHE A 131 ? 0.21413 0.20384 0.24738 -0.01835 0.00666  -0.02314 138 PHE A CD2 
943  C CE1 . PHE A 131 ? 0.25860 0.24247 0.29459 -0.01317 0.01099  -0.01618 138 PHE A CE1 
944  C CE2 . PHE A 131 ? 0.22810 0.22212 0.26428 -0.01547 0.00807  -0.02140 138 PHE A CE2 
945  C CZ  . PHE A 131 ? 0.26964 0.25787 0.30674 -0.01344 0.00933  -0.01863 138 PHE A CZ  
946  N N   . TYR A 132 ? 0.21598 0.20440 0.23231 -0.01026 -0.00400 -0.03577 139 TYR A N   
947  C CA  . TYR A 132 ? 0.22660 0.22818 0.24433 -0.00682 -0.00553 -0.03412 139 TYR A CA  
948  C C   . TYR A 132 ? 0.26568 0.27046 0.26879 0.00427  -0.00650 -0.03386 139 TYR A C   
949  O O   . TYR A 132 ? 0.23307 0.24649 0.23529 0.00960  -0.00699 -0.02930 139 TYR A O   
950  C CB  . TYR A 132 ? 0.19648 0.20879 0.22533 -0.01384 -0.01232 -0.03909 139 TYR A CB  
951  C CG  . TYR A 132 ? 0.20716 0.22181 0.24949 -0.02321 -0.00841 -0.03523 139 TYR A CG  
952  C CD1 . TYR A 132 ? 0.22167 0.24646 0.26951 -0.02072 -0.00342 -0.03058 139 TYR A CD1 
953  C CD2 . TYR A 132 ? 0.21279 0.21813 0.26020 -0.03273 -0.00971 -0.03576 139 TYR A CD2 
954  C CE1 . TYR A 132 ? 0.21005 0.24062 0.26581 -0.02627 0.00113  -0.02692 139 TYR A CE1 
955  C CE2 . TYR A 132 ? 0.29829 0.30814 0.35552 -0.04007 -0.00465 -0.02884 139 TYR A CE2 
956  C CZ  . TYR A 132 ? 0.29609 0.32082 0.35614 -0.03614 0.00125  -0.02462 139 TYR A CZ  
957  O OH  . TYR A 132 ? 0.26122 0.29388 0.32676 -0.04057 0.00705  -0.01779 139 TYR A OH  
958  N N   . SER A 133 ? 0.24542 0.24402 0.23554 0.00999  -0.00635 -0.03783 140 SER A N   
959  C CA  . SER A 133 ? 0.28445 0.28984 0.25738 0.02310  -0.00410 -0.03467 140 SER A CA  
960  C C   . SER A 133 ? 0.26615 0.27518 0.24262 0.02578  0.00640  -0.01865 140 SER A C   
961  O O   . SER A 133 ? 0.21806 0.23523 0.18288 0.03563  0.01004  -0.01036 140 SER A O   
962  C CB  . SER A 133 ? 0.26290 0.26280 0.21991 0.03152  -0.00480 -0.04338 140 SER A CB  
963  O OG  . SER A 133 ? 0.27618 0.27159 0.23771 0.03174  0.00435  -0.03746 140 SER A OG  
964  N N   . ALA A 134 ? 0.24288 0.24612 0.23532 0.01709  0.01050  -0.01359 141 ALA A N   
965  C CA  . ALA A 134 ? 0.24569 0.24938 0.24663 0.01655  0.01700  0.00015  141 ALA A CA  
966  C C   . ALA A 134 ? 0.21537 0.22104 0.21452 0.02086  0.01489  0.00684  141 ALA A C   
967  O O   . ALA A 134 ? 0.22801 0.23380 0.22810 0.02397  0.02010  0.02098  141 ALA A O   
968  C CB  . ALA A 134 ? 0.21963 0.21585 0.23695 0.00686  0.01702  -0.00041 141 ALA A CB  
969  N N   . TYR A 135 ? 0.21343 0.22183 0.21168 0.02139  0.00727  -0.00155 142 TYR A N   
970  C CA  . TYR A 135 ? 0.23217 0.24311 0.22949 0.02794  0.00414  0.00423  142 TYR A CA  
971  C C   . TYR A 135 ? 0.26668 0.28704 0.24546 0.03985  0.00304  0.00939  142 TYR A C   
972  O O   . TYR A 135 ? 0.24579 0.26934 0.22136 0.04764  -0.00063 0.01515  142 TYR A O   
973  C CB  . TYR A 135 ? 0.19329 0.21010 0.19963 0.02563  -0.00295 -0.00587 142 TYR A CB  
974  C CG  . TYR A 135 ? 0.24252 0.25146 0.26282 0.01845  -0.00058 -0.00783 142 TYR A CG  
975  C CD1 . TYR A 135 ? 0.23117 0.23111 0.25773 0.02221  -0.00061 -0.00320 142 TYR A CD1 
976  C CD2 . TYR A 135 ? 0.23940 0.24779 0.26446 0.00947  0.00083  -0.01438 142 TYR A CD2 
977  C CE1 . TYR A 135 ? 0.27343 0.26604 0.30891 0.01806  -0.00009 -0.00789 142 TYR A CE1 
978  C CE2 . TYR A 135 ? 0.20364 0.20717 0.23713 0.00525  0.00261  -0.01610 142 TYR A CE2 
979  C CZ  . TYR A 135 ? 0.25071 0.24737 0.28842 0.00999  0.00179  -0.01420 142 TYR A CZ  
980  O OH  . TYR A 135 ? 0.23177 0.22396 0.27423 0.00810  0.00182  -0.01897 142 TYR A OH  
981  N N   . LEU A 136 ? 0.27651 0.30191 0.24104 0.04390  0.00587  0.00732  143 LEU A N   
982  C CA  . LEU A 136 ? 0.25908 0.29506 0.20179 0.05803  0.00741  0.01505  143 LEU A CA  
983  C C   . LEU A 136 ? 0.30451 0.33856 0.24959 0.06070  0.01819  0.03854  143 LEU A C   
984  O O   . LEU A 136 ? 0.27544 0.31627 0.20624 0.07208  0.01916  0.05123  143 LEU A O   
985  C CB  . LEU A 136 ? 0.27639 0.31833 0.20156 0.06437  0.00853  0.00530  143 LEU A CB  
986  C CG  . LEU A 136 ? 0.25946 0.30032 0.17902 0.06322  -0.00462 -0.01781 143 LEU A CG  
987  C CD1 . LEU A 136 ? 0.30333 0.34296 0.20643 0.07079  -0.00292 -0.02785 143 LEU A CD1 
988  C CD2 . LEU A 136 ? 0.28031 0.33256 0.18799 0.07156  -0.01704 -0.02381 143 LEU A CD2 
989  N N   . VAL A 137 ? 0.25838 0.28353 0.22254 0.04986  0.02545  0.04559  144 VAL A N   
990  C CA  . VAL A 137 ? 0.25295 0.27616 0.22579 0.04843  0.03524  0.06883  144 VAL A CA  
991  C C   . VAL A 137 ? 0.26166 0.26540 0.25958 0.03645  0.03263  0.07324  144 VAL A C   
992  O O   . VAL A 137 ? 0.30005 0.29642 0.30872 0.03360  0.03738  0.09305  144 VAL A O   
993  C CB  . VAL A 137 ? 0.25426 0.29062 0.22822 0.04797  0.04684  0.07571  144 VAL A CB  
994  C CG1 . VAL A 137 ? 0.28323 0.33835 0.22779 0.06443  0.04986  0.07166  144 VAL A CG1 
995  C CG2 . VAL A 137 ? 0.23109 0.26192 0.22143 0.03691  0.04501  0.06168  144 VAL A CG2 
996  N N   . ALA A 138 ? 0.29762 0.29207 0.30545 0.02955  0.02500  0.05618  145 ALA A N   
997  C CA  . ALA A 138 ? 0.25474 0.23104 0.28286 0.02053  0.02139  0.05618  145 ALA A CA  
998  C C   . ALA A 138 ? 0.23841 0.20549 0.26526 0.02639  0.01268  0.04870  145 ALA A C   
999  O O   . ALA A 138 ? 0.31300 0.29084 0.33141 0.03103  0.00824  0.03566  145 ALA A O   
1000 C CB  . ALA A 138 ? 0.20326 0.17905 0.24219 0.01067  0.02034  0.04314  145 ALA A CB  
1001 N N   . GLU A 139 ? 0.24196 0.18930 0.27953 0.02621  0.00972  0.05700  146 GLU A N   
1002 C CA  . GLU A 139 ? 0.32773 0.26475 0.36619 0.03391  0.00130  0.04788  146 GLU A CA  
1003 C C   . GLU A 139 ? 0.33211 0.26413 0.37969 0.02868  -0.00311 0.02978  146 GLU A C   
1004 O O   . GLU A 139 ? 0.29575 0.23077 0.34133 0.03663  -0.00798 0.01797  146 GLU A O   
1005 C CB  . GLU A 139 ? 0.34557 0.25839 0.38991 0.03855  -0.00150 0.06338  146 GLU A CB  
1006 C CG  . GLU A 139 ? 0.50710 0.39769 0.57086 0.02552  -0.00135 0.07189  146 GLU A CG  
1007 C CD  . GLU A 139 ? 0.88448 0.74451 0.95673 0.02890  -0.00625 0.08703  146 GLU A CD  
1008 O OE1 . GLU A 139 ? 0.80632 0.64056 0.89763 0.01913  -0.01214 0.08640  146 GLU A OE1 
1009 O OE2 . GLU A 139 ? 0.73858 0.59899 0.79865 0.04151  -0.00556 0.09962  146 GLU A OE2 
1010 N N   . LYS A 140 ? 0.26964 0.19795 0.32667 0.01700  -0.00125 0.02795  147 LYS A N   
1011 C CA  . LYS A 140 ? 0.29329 0.21919 0.35516 0.01326  -0.00550 0.01169  147 LYS A CA  
1012 C C   . LYS A 140 ? 0.26480 0.20126 0.32998 0.00279  -0.00103 0.01133  147 LYS A C   
1013 O O   . LYS A 140 ? 0.23121 0.16907 0.30280 -0.00304 0.00365  0.02400  147 LYS A O   
1014 C CB  . LYS A 140 ? 0.28480 0.18416 0.35764 0.01317  -0.01386 0.00821  147 LYS A CB  
1015 C CG  . LYS A 140 ? 0.32557 0.22243 0.39990 0.01159  -0.01963 -0.00968 147 LYS A CG  
1016 C CD  . LYS A 140 ? 0.36701 0.23496 0.44725 0.01702  -0.03070 -0.01751 147 LYS A CD  
1017 C CE  . LYS A 140 ? 0.52385 0.37201 0.62185 0.00375  -0.03786 -0.01536 147 LYS A CE  
1018 N NZ  . LYS A 140 ? 0.74891 0.58491 0.84608 0.00654  -0.04971 -0.03670 147 LYS A NZ  
1019 N N   . VAL A 141 ? 0.19751 0.14366 0.25847 0.00171  -0.00164 -0.00136 148 VAL A N   
1020 C CA  . VAL A 141 ? 0.18519 0.13966 0.24829 -0.00583 0.00127  -0.00244 148 VAL A CA  
1021 C C   . VAL A 141 ? 0.25673 0.20708 0.32247 -0.00760 -0.00448 -0.01398 148 VAL A C   
1022 O O   . VAL A 141 ? 0.19683 0.15016 0.25497 -0.00165 -0.00643 -0.02355 148 VAL A O   
1023 C CB  . VAL A 141 ? 0.21173 0.18149 0.26398 -0.00467 0.00602  -0.00446 148 VAL A CB  
1024 C CG1 . VAL A 141 ? 0.21499 0.18939 0.26907 -0.00999 0.00810  -0.00563 148 VAL A CG1 
1025 C CG2 . VAL A 141 ? 0.18821 0.16339 0.23342 -0.00026 0.00981  0.00399  148 VAL A CG2 
1026 N N   . THR A 142 ? 0.23375 0.18101 0.31023 -0.01469 -0.00721 -0.01279 149 THR A N   
1027 C CA  . THR A 142 ? 0.22700 0.17346 0.30349 -0.01556 -0.01400 -0.02404 149 THR A CA  
1028 C C   . THR A 142 ? 0.23094 0.19147 0.30633 -0.01903 -0.01031 -0.02179 149 THR A C   
1029 O O   . THR A 142 ? 0.23266 0.19912 0.31733 -0.02343 -0.00617 -0.01231 149 THR A O   
1030 C CB  . THR A 142 ? 0.25542 0.18613 0.34764 -0.02068 -0.02438 -0.02678 149 THR A CB  
1031 O OG1 . THR A 142 ? 0.31689 0.22891 0.41133 -0.01690 -0.02802 -0.02656 149 THR A OG1 
1032 C CG2 . THR A 142 ? 0.27943 0.20939 0.36641 -0.01809 -0.03423 -0.04248 149 THR A CG2 
1033 N N   . VAL A 143 ? 0.23809 0.20498 0.30175 -0.01546 -0.01112 -0.02917 150 VAL A N   
1034 C CA  . VAL A 143 ? 0.20063 0.17709 0.26178 -0.01686 -0.00903 -0.02665 150 VAL A CA  
1035 C C   . VAL A 143 ? 0.27377 0.25168 0.33307 -0.01527 -0.01781 -0.03472 150 VAL A C   
1036 O O   . VAL A 143 ? 0.25692 0.23537 0.30314 -0.00920 -0.02023 -0.04269 150 VAL A O   
1037 C CB  . VAL A 143 ? 0.19141 0.17347 0.23979 -0.01453 -0.00216 -0.02457 150 VAL A CB  
1038 C CG1 . VAL A 143 ? 0.21057 0.19673 0.25596 -0.01467 -0.00131 -0.02117 150 VAL A CG1 
1039 C CG2 . VAL A 143 ? 0.25444 0.23571 0.30334 -0.01516 0.00335  -0.01971 150 VAL A CG2 
1040 N N   . ILE A 144 ? 0.23127 0.21322 0.30350 -0.01935 -0.02278 -0.03283 151 ILE A N   
1041 C CA  . ILE A 144 ? 0.17709 0.16384 0.24749 -0.01720 -0.03316 -0.04062 151 ILE A CA  
1042 C C   . ILE A 144 ? 0.21701 0.21488 0.28058 -0.01390 -0.02909 -0.03409 151 ILE A C   
1043 O O   . ILE A 144 ? 0.21164 0.21395 0.28441 -0.01590 -0.02298 -0.02519 151 ILE A O   
1044 C CB  . ILE A 144 ? 0.24156 0.22743 0.33588 -0.02483 -0.04436 -0.04323 151 ILE A CB  
1045 C CG1 . ILE A 144 ? 0.38245 0.35235 0.48914 -0.03046 -0.04596 -0.04328 151 ILE A CG1 
1046 C CG2 . ILE A 144 ? 0.27650 0.26529 0.36611 -0.02122 -0.05949 -0.05657 151 ILE A CG2 
1047 C CD1 . ILE A 144 ? 0.33503 0.28933 0.42843 -0.02398 -0.05402 -0.05791 151 ILE A CD1 
1048 N N   . THR A 145 ? 0.20493 0.20713 0.25098 -0.00700 -0.03230 -0.03787 152 THR A N   
1049 C CA  . THR A 145 ? 0.26129 0.26941 0.29961 -0.00308 -0.02813 -0.02908 152 THR A CA  
1050 C C   . THR A 145 ? 0.28810 0.30470 0.31290 0.00466  -0.03695 -0.03280 152 THR A C   
1051 O O   . THR A 145 ? 0.25165 0.26963 0.26420 0.00917  -0.04295 -0.04269 152 THR A O   
1052 C CB  . THR A 145 ? 0.28730 0.28959 0.31384 -0.00292 -0.01647 -0.02162 152 THR A CB  
1053 O OG1 . THR A 145 ? 0.24829 0.24914 0.27206 -0.00050 -0.01329 -0.01236 152 THR A OG1 
1054 C CG2 . THR A 145 ? 0.27321 0.27880 0.28207 0.00130  -0.01455 -0.02400 152 THR A CG2 
1055 N N   . LYS A 146 ? 0.22373 0.24650 0.24908 0.00853  -0.03823 -0.02532 153 LYS A N   
1056 C CA  . LYS A 146 ? 0.26465 0.29725 0.27527 0.01794  -0.04685 -0.02591 153 LYS A CA  
1057 C C   . LYS A 146 ? 0.26415 0.29428 0.26597 0.02353  -0.04025 -0.01106 153 LYS A C   
1058 O O   . LYS A 146 ? 0.24796 0.27743 0.26422 0.02350  -0.03902 -0.00576 153 LYS A O   
1059 C CB  . LYS A 146 ? 0.24644 0.29147 0.27389 0.01778  -0.06249 -0.03465 153 LYS A CB  
1060 C CG  . LYS A 146 ? 0.27675 0.33512 0.28913 0.02943  -0.07378 -0.03530 153 LYS A CG  
1061 C CD  . LYS A 146 ? 0.25926 0.31957 0.24464 0.03736  -0.08036 -0.04605 153 LYS A CD  
1062 C CE  . LYS A 146 ? 0.28370 0.36010 0.25201 0.05069  -0.09372 -0.04750 153 LYS A CE  
1063 N NZ  . LYS A 146 ? 0.29020 0.36782 0.24216 0.05942  -0.08432 -0.02741 153 LYS A NZ  
1064 N N   . HIS A 147 ? 0.26336 0.29211 0.24195 0.02915  -0.03569 -0.00363 154 HIS A N   
1065 C CA  . HIS A 147 ? 0.28583 0.30817 0.25404 0.03455  -0.03079 0.01266  154 HIS A CA  
1066 C C   . HIS A 147 ? 0.27849 0.31408 0.23018 0.04738  -0.04072 0.01537  154 HIS A C   
1067 O O   . HIS A 147 ? 0.27780 0.32686 0.21728 0.05230  -0.04838 0.00512  154 HIS A O   
1068 C CB  . HIS A 147 ? 0.31419 0.32763 0.27100 0.02993  -0.01811 0.02323  154 HIS A CB  
1069 C CG  . HIS A 147 ? 0.26857 0.26791 0.21966 0.03145  -0.01272 0.04173  154 HIS A CG  
1070 N ND1 . HIS A 147 ? 0.29228 0.29556 0.22483 0.04149  -0.01451 0.05517  154 HIS A ND1 
1071 C CD2 . HIS A 147 ? 0.30221 0.28087 0.26294 0.02455  -0.00669 0.04901  154 HIS A CD2 
1072 C CE1 . HIS A 147 ? 0.39109 0.37427 0.32417 0.03978  -0.00938 0.07173  154 HIS A CE1 
1073 N NE2 . HIS A 147 ? 0.38535 0.35232 0.33583 0.02931  -0.00542 0.06675  154 HIS A NE2 
1074 N N   . ASN A 148 ? 0.28595 0.31704 0.23589 0.05481  -0.04196 0.02809  155 ASN A N   
1075 C CA  . ASN A 148 ? 0.31987 0.36482 0.25285 0.06912  -0.05242 0.03247  155 ASN A CA  
1076 C C   . ASN A 148 ? 0.36237 0.41530 0.26455 0.07537  -0.04934 0.03796  155 ASN A C   
1077 O O   . ASN A 148 ? 0.34805 0.41892 0.23272 0.08743  -0.06072 0.03282  155 ASN A O   
1078 C CB  . ASN A 148 ? 0.32821 0.36247 0.26086 0.07804  -0.05211 0.04915  155 ASN A CB  
1079 C CG  . ASN A 148 ? 0.39297 0.43339 0.35159 0.08077  -0.05972 0.04215  155 ASN A CG  
1080 O OD1 . ASN A 148 ? 0.36747 0.42708 0.34313 0.07748  -0.06884 0.02714  155 ASN A OD1 
1081 N ND2 . ASN A 148 ? 0.37400 0.39872 0.33698 0.08745  -0.05628 0.05358  155 ASN A ND2 
1082 N N   . ASP A 149 ? 0.34056 0.38383 0.23585 0.06832  -0.03443 0.04836  156 ASP A N   
1083 C CA  . ASP A 149 ? 0.42527 0.48066 0.29228 0.07527  -0.02763 0.05872  156 ASP A CA  
1084 C C   . ASP A 149 ? 0.50241 0.57220 0.36289 0.07451  -0.02623 0.04164  156 ASP A C   
1085 O O   . ASP A 149 ? 0.43239 0.51586 0.27097 0.08055  -0.01718 0.04981  156 ASP A O   
1086 C CB  . ASP A 149 ? 0.41946 0.46025 0.28553 0.06792  -0.01166 0.08385  156 ASP A CB  
1087 C CG  . ASP A 149 ? 0.54856 0.56986 0.41682 0.07151  -0.01367 0.10199  156 ASP A CG  
1088 O OD1 . ASP A 149 ? 0.43336 0.46067 0.29529 0.08460  -0.02600 0.09950  156 ASP A OD1 
1089 O OD2 . ASP A 149 ? 0.50727 0.50664 0.38473 0.06168  -0.00421 0.11809  156 ASP A OD2 
1090 N N   . ASP A 150 ? 0.34223 0.40973 0.22126 0.06834  -0.03431 0.01951  157 ASP A N   
1091 C CA  . ASP A 150 ? 0.33604 0.41128 0.21022 0.06871  -0.03384 0.00267  157 ASP A CA  
1092 C C   . ASP A 150 ? 0.45085 0.52465 0.33914 0.06757  -0.05120 -0.02181 157 ASP A C   
1093 O O   . ASP A 150 ? 0.39434 0.46644 0.29823 0.06545  -0.06225 -0.02422 157 ASP A O   
1094 C CB  . ASP A 150 ? 0.36219 0.42869 0.25112 0.05603  -0.01878 0.00770  157 ASP A CB  
1095 C CG  . ASP A 150 ? 0.40915 0.49038 0.28354 0.06214  -0.01207 0.00083  157 ASP A CG  
1096 O OD1 . ASP A 150 ? 0.39343 0.48751 0.24684 0.07635  -0.02079 -0.01319 157 ASP A OD1 
1097 O OD2 . ASP A 150 ? 0.40306 0.48442 0.28715 0.05402  0.00106  0.00830  157 ASP A OD2 
1098 N N   . GLU A 151 ? 0.34283 0.41780 0.22766 0.06912  -0.05376 -0.03935 158 GLU A N   
1099 C CA  . GLU A 151 ? 0.38443 0.45321 0.28439 0.06616  -0.07073 -0.06241 158 GLU A CA  
1100 C C   . GLU A 151 ? 0.30474 0.35690 0.23690 0.04960  -0.06565 -0.06255 158 GLU A C   
1101 O O   . GLU A 151 ? 0.30737 0.35393 0.24645 0.04244  -0.05024 -0.04847 158 GLU A O   
1102 C CB  . GLU A 151 ? 0.38197 0.45564 0.25938 0.07899  -0.07779 -0.08262 158 GLU A CB  
1103 C CG  . GLU A 151 ? 0.60083 0.69386 0.44202 0.09857  -0.08516 -0.08579 158 GLU A CG  
1104 C CD  . GLU A 151 ? 0.92571 1.02344 0.77139 0.10053  -0.10615 -0.09309 158 GLU A CD  
1105 O OE1 . GLU A 151 ? 1.09388 1.20684 0.91837 0.11162  -0.10657 -0.08072 158 GLU A OE1 
1106 O OE2 . GLU A 151 ? 1.06408 1.15168 0.93614 0.09082  -0.12248 -0.10971 158 GLU A OE2 
1107 N N   . GLN A 152 ? 0.28331 0.32771 0.23539 0.04342  -0.07971 -0.07835 159 GLN A N   
1108 C CA  . GLN A 152 ? 0.27463 0.30486 0.25578 0.02895  -0.07528 -0.07684 159 GLN A CA  
1109 C C   . GLN A 152 ? 0.28360 0.30346 0.25871 0.03041  -0.06923 -0.08416 159 GLN A C   
1110 O O   . GLN A 152 ? 0.32540 0.34233 0.28773 0.03930  -0.07910 -0.10153 159 GLN A O   
1111 C CB  . GLN A 152 ? 0.33554 0.36298 0.34441 0.02004  -0.09191 -0.08657 159 GLN A CB  
1112 C CG  . GLN A 152 ? 0.31435 0.33246 0.35482 0.00506  -0.08538 -0.07854 159 GLN A CG  
1113 C CD  . GLN A 152 ? 0.35535 0.38021 0.42819 -0.00511 -0.09834 -0.08008 159 GLN A CD  
1114 O OE1 . GLN A 152 ? 0.35067 0.39272 0.42892 -0.00286 -0.10263 -0.07520 159 GLN A OE1 
1115 N NE2 . GLN A 152 ? 0.30402 0.31657 0.40076 -0.01640 -0.10448 -0.08512 159 GLN A NE2 
1116 N N   . TYR A 153 ? 0.23982 0.25453 0.22343 0.02351  -0.05422 -0.07224 160 TYR A N   
1117 C CA  . TYR A 153 ? 0.25749 0.26644 0.23694 0.02602  -0.04726 -0.07641 160 TYR A CA  
1118 C C   . TYR A 153 ? 0.29534 0.29016 0.29896 0.01451  -0.04449 -0.07269 160 TYR A C   
1119 O O   . TYR A 153 ? 0.24595 0.23972 0.26608 0.00500  -0.04188 -0.06247 160 TYR A O   
1120 C CB  . TYR A 153 ? 0.30109 0.32321 0.26514 0.03045  -0.03138 -0.06415 160 TYR A CB  
1121 C CG  . TYR A 153 ? 0.34827 0.38700 0.28461 0.04507  -0.03126 -0.06727 160 TYR A CG  
1122 C CD1 . TYR A 153 ? 0.33987 0.38440 0.26084 0.05827  -0.03204 -0.08076 160 TYR A CD1 
1123 C CD2 . TYR A 153 ? 0.37351 0.42290 0.29712 0.04814  -0.03025 -0.05634 160 TYR A CD2 
1124 C CE1 . TYR A 153 ? 0.37363 0.43757 0.26574 0.07457  -0.03064 -0.08350 160 TYR A CE1 
1125 C CE2 . TYR A 153 ? 0.38405 0.45135 0.27890 0.06328  -0.02926 -0.05687 160 TYR A CE2 
1126 C CZ  . TYR A 153 ? 0.42853 0.50466 0.30705 0.07660  -0.02888 -0.07060 160 TYR A CZ  
1127 O OH  . TYR A 153 ? 0.57875 0.67672 0.42554 0.09433  -0.02642 -0.07090 160 TYR A OH  
1128 N N   . ALA A 154 ? 0.23475 0.22000 0.23854 0.01781  -0.04473 -0.08062 161 ALA A N   
1129 C CA  . ALA A 154 ? 0.22835 0.20067 0.25052 0.00976  -0.04135 -0.07541 161 ALA A CA  
1130 C C   . ALA A 154 ? 0.26122 0.23915 0.27546 0.01514  -0.02988 -0.07165 161 ALA A C   
1131 O O   . ALA A 154 ? 0.28860 0.27043 0.28949 0.02703  -0.03038 -0.08132 161 ALA A O   
1132 C CB  . ALA A 154 ? 0.29251 0.24442 0.32698 0.00831  -0.05505 -0.08711 161 ALA A CB  
1133 N N   . TRP A 155 ? 0.22554 0.20618 0.24825 0.00767  -0.02038 -0.05872 162 TRP A N   
1134 C CA  . TRP A 155 ? 0.21665 0.20398 0.23793 0.01013  -0.01170 -0.05456 162 TRP A CA  
1135 C C   . TRP A 155 ? 0.23157 0.20470 0.26507 0.00773  -0.01373 -0.05290 162 TRP A C   
1136 O O   . TRP A 155 ? 0.25085 0.21402 0.29575 -0.00003 -0.01636 -0.04771 162 TRP A O   
1137 C CB  . TRP A 155 ? 0.22809 0.22669 0.24933 0.00350  -0.00256 -0.04266 162 TRP A CB  
1138 C CG  . TRP A 155 ? 0.24246 0.25022 0.26706 0.00227  0.00441  -0.03760 162 TRP A CG  
1139 C CD1 . TRP A 155 ? 0.17419 0.20007 0.19573 0.00341  0.01095  -0.03406 162 TRP A CD1 
1140 C CD2 . TRP A 155 ? 0.25632 0.25880 0.28937 -0.00101 0.00490  -0.03434 162 TRP A CD2 
1141 N NE1 . TRP A 155 ? 0.21860 0.25077 0.24919 -0.00005 0.01364  -0.03063 162 TRP A NE1 
1142 C CE2 . TRP A 155 ? 0.28585 0.30328 0.32098 -0.00156 0.00950  -0.03159 162 TRP A CE2 
1143 C CE3 . TRP A 155 ? 0.20050 0.18974 0.23978 -0.00324 0.00206  -0.03219 162 TRP A CE3 
1144 C CZ2 . TRP A 155 ? 0.26741 0.28587 0.30834 -0.00295 0.00906  -0.02956 162 TRP A CZ2 
1145 C CZ3 . TRP A 155 ? 0.20949 0.19989 0.25146 -0.00333 0.00382  -0.02811 162 TRP A CZ3 
1146 C CH2 . TRP A 155 ? 0.22157 0.22594 0.26322 -0.00262 0.00620  -0.02817 162 TRP A CH2 
1147 N N   . GLU A 156 ? 0.22028 0.19468 0.25200 0.01547  -0.01217 -0.05574 163 GLU A N   
1148 C CA  . GLU A 156 ? 0.19120 0.15091 0.23235 0.01505  -0.01450 -0.05197 163 GLU A CA  
1149 C C   . GLU A 156 ? 0.21617 0.18726 0.25545 0.02253  -0.00974 -0.05018 163 GLU A C   
1150 O O   . GLU A 156 ? 0.20592 0.19207 0.23891 0.03169  -0.00747 -0.05658 163 GLU A O   
1151 C CB  . GLU A 156 ? 0.30122 0.23759 0.34640 0.01897  -0.02556 -0.06100 163 GLU A CB  
1152 C CG  . GLU A 156 ? 0.33442 0.25125 0.39140 0.01660  -0.02821 -0.05278 163 GLU A CG  
1153 C CD  . GLU A 156 ? 0.67539 0.56407 0.74159 0.01567  -0.04105 -0.06005 163 GLU A CD  
1154 O OE1 . GLU A 156 ? 0.51390 0.39435 0.59537 0.00255  -0.04440 -0.05289 163 GLU A OE1 
1155 O OE2 . GLU A 156 ? 0.57654 0.45187 0.63622 0.02833  -0.04838 -0.07342 163 GLU A OE2 
1156 N N   . SER A 157 ? 0.25052 0.21818 0.29540 0.01969  -0.00815 -0.04088 164 SER A N   
1157 C CA  . SER A 157 ? 0.22946 0.20887 0.27405 0.02765  -0.00633 -0.03951 164 SER A CA  
1158 C C   . SER A 157 ? 0.23389 0.20097 0.28162 0.02843  -0.00814 -0.02999 164 SER A C   
1159 O O   . SER A 157 ? 0.23276 0.19553 0.28174 0.02005  -0.00591 -0.02106 164 SER A O   
1160 C CB  . SER A 157 ? 0.19528 0.19987 0.23985 0.02277  -0.00045 -0.03694 164 SER A CB  
1161 O OG  . SER A 157 ? 0.23583 0.25585 0.28384 0.03010  -0.00070 -0.03649 164 SER A OG  
1162 N N   . SER A 158 ? 0.25871 0.22220 0.30659 0.04064  -0.01158 -0.03104 165 SER A N   
1163 C CA  . SER A 158 ? 0.26129 0.21910 0.30914 0.04489  -0.01282 -0.02003 165 SER A CA  
1164 C C   . SER A 158 ? 0.27828 0.26309 0.32417 0.05074  -0.01174 -0.01992 165 SER A C   
1165 O O   . SER A 158 ? 0.27024 0.25515 0.31472 0.06131  -0.01509 -0.01468 165 SER A O   
1166 C CB  . SER A 158 ? 0.28126 0.21294 0.33151 0.05557  -0.01943 -0.01949 165 SER A CB  
1167 O OG  . SER A 158 ? 0.36220 0.26763 0.41848 0.04711  -0.02285 -0.01901 165 SER A OG  
1168 N N   . ALA A 159 ? 0.23378 0.24127 0.28114 0.04371  -0.00826 -0.02495 166 ALA A N   
1169 C CA  . ALA A 159 ? 0.25629 0.29259 0.30780 0.04569  -0.00892 -0.02660 166 ALA A CA  
1170 C C   . ALA A 159 ? 0.28852 0.33819 0.34573 0.06078  -0.01070 -0.03194 166 ALA A C   
1171 O O   . ALA A 159 ? 0.31931 0.36141 0.37561 0.06714  -0.00944 -0.03833 166 ALA A O   
1172 C CB  . ALA A 159 ? 0.27896 0.31710 0.32503 0.04567  -0.01222 -0.01978 166 ALA A CB  
1173 N N   . GLY A 160 ? 0.29849 0.36992 0.36108 0.06857  -0.01447 -0.03073 167 GLY A N   
1174 C CA  . GLY A 160 ? 0.27077 0.36040 0.34082 0.08525  -0.01563 -0.03569 167 GLY A CA  
1175 C C   . GLY A 160 ? 0.34737 0.46772 0.42795 0.08337  -0.00910 -0.04180 167 GLY A C   
1176 O O   . GLY A 160 ? 0.32052 0.45653 0.40545 0.09969  -0.00767 -0.04715 167 GLY A O   
1177 N N   . GLY A 161 ? 0.20136 0.33093 0.28566 0.06527  -0.00449 -0.04010 168 GLY A N   
1178 C CA  . GLY A 161 ? 0.21426 0.37778 0.31118 0.06099  0.00273  -0.04069 168 GLY A CA  
1179 C C   . GLY A 161 ? 0.22209 0.37883 0.30969 0.06144  0.01044  -0.04352 168 GLY A C   
1180 O O   . GLY A 161 ? 0.16710 0.35399 0.26321 0.05842  0.01846  -0.04095 168 GLY A O   
1181 N N   . SER A 162 ? 0.18763 0.30814 0.25900 0.06468  0.00792  -0.04775 169 SER A N   
1182 C CA  . SER A 162 ? 0.18403 0.29924 0.24443 0.06761  0.01244  -0.05296 169 SER A CA  
1183 C C   . SER A 162 ? 0.20542 0.28514 0.25524 0.05696  0.00873  -0.05281 169 SER A C   
1184 O O   . SER A 162 ? 0.20707 0.26327 0.25687 0.05197  0.00325  -0.04963 169 SER A O   
1185 C CB  . SER A 162 ? 0.24675 0.36124 0.29967 0.09110  0.01096  -0.06440 169 SER A CB  
1186 O OG  . SER A 162 ? 0.27939 0.35388 0.32515 0.09734  0.00123  -0.06955 169 SER A OG  
1187 N N   . PHE A 163 ? 0.24151 0.32158 0.28265 0.05443  0.01226  -0.05500 170 PHE A N   
1188 C CA  . PHE A 163 ? 0.18626 0.23784 0.21896 0.04705  0.00776  -0.05658 170 PHE A CA  
1189 C C   . PHE A 163 ? 0.21555 0.26664 0.23436 0.05771  0.00689  -0.06692 170 PHE A C   
1190 O O   . PHE A 163 ? 0.22137 0.29826 0.23501 0.06901  0.01303  -0.06995 170 PHE A O   
1191 C CB  . PHE A 163 ? 0.20357 0.25566 0.23940 0.02941  0.01104  -0.04652 170 PHE A CB  
1192 C CG  . PHE A 163 ? 0.19773 0.27412 0.23298 0.02512  0.01916  -0.04076 170 PHE A CG  
1193 C CD1 . PHE A 163 ? 0.22779 0.32983 0.27592 0.01988  0.02462  -0.03339 170 PHE A CD1 
1194 C CD2 . PHE A 163 ? 0.23049 0.30476 0.25375 0.02559  0.02061  -0.04116 170 PHE A CD2 
1195 C CE1 . PHE A 163 ? 0.23099 0.35486 0.28216 0.01357  0.03281  -0.02421 170 PHE A CE1 
1196 C CE2 . PHE A 163 ? 0.20550 0.30159 0.22723 0.02198  0.02910  -0.03192 170 PHE A CE2 
1197 C CZ  . PHE A 163 ? 0.23164 0.35171 0.26842 0.01497  0.03592  -0.02217 170 PHE A CZ  
1198 N N   . THR A 164 ? 0.21135 0.23560 0.22442 0.05494  -0.00122 -0.07261 171 THR A N   
1199 C CA  . THR A 164 ? 0.23168 0.25270 0.22962 0.06515  -0.00580 -0.08523 171 THR A CA  
1200 C C   . THR A 164 ? 0.22500 0.24315 0.21880 0.05350  -0.00683 -0.08074 171 THR A C   
1201 O O   . THR A 164 ? 0.21109 0.21953 0.21539 0.03877  -0.00706 -0.07109 171 THR A O   
1202 C CB  . THR A 164 ? 0.28584 0.27583 0.28199 0.07475  -0.01922 -0.10028 171 THR A CB  
1203 O OG1 . THR A 164 ? 0.28148 0.24466 0.29031 0.05965  -0.02648 -0.09484 171 THR A OG1 
1204 C CG2 . THR A 164 ? 0.29292 0.28244 0.29242 0.08928  -0.01917 -0.10433 171 THR A CG2 
1205 N N   . VAL A 165 ? 0.24611 0.27520 0.22285 0.06270  -0.00727 -0.08776 172 VAL A N   
1206 C CA  . VAL A 165 ? 0.25845 0.28547 0.22831 0.05594  -0.01062 -0.08527 172 VAL A CA  
1207 C C   . VAL A 165 ? 0.29711 0.31641 0.24984 0.06989  -0.02277 -0.10438 172 VAL A C   
1208 O O   . VAL A 165 ? 0.31132 0.34314 0.24774 0.08800  -0.02117 -0.11507 172 VAL A O   
1209 C CB  . VAL A 165 ? 0.29380 0.34697 0.25722 0.05249  0.00206  -0.06991 172 VAL A CB  
1210 C CG1 . VAL A 165 ? 0.27278 0.32359 0.22525 0.05026  -0.00283 -0.06800 172 VAL A CG1 
1211 C CG2 . VAL A 165 ? 0.24140 0.29742 0.22301 0.03738  0.01039  -0.05402 172 VAL A CG2 
1212 N N   . ARG A 166 ? 0.27487 0.27553 0.23195 0.06252  -0.03568 -0.10981 173 ARG A N   
1213 C CA  . ARG A 166 ? 0.31633 0.30945 0.25787 0.07406  -0.05085 -0.12978 173 ARG A CA  
1214 C C   . ARG A 166 ? 0.30302 0.29637 0.24678 0.06446  -0.05882 -0.12649 173 ARG A C   
1215 O O   . ARG A 166 ? 0.27913 0.27128 0.24083 0.04870  -0.05453 -0.11104 173 ARG A O   
1216 C CB  . ARG A 166 ? 0.37508 0.33677 0.32624 0.07678  -0.06651 -0.14758 173 ARG A CB  
1217 C CG  . ARG A 166 ? 0.45062 0.38920 0.43160 0.05624  -0.07328 -0.13953 173 ARG A CG  
1218 C CD  . ARG A 166 ? 0.56744 0.47566 0.56152 0.05720  -0.08243 -0.14737 173 ARG A CD  
1219 N NE  . ARG A 166 ? 0.53549 0.44504 0.53458 0.05934  -0.06975 -0.13662 173 ARG A NE  
1220 C CZ  . ARG A 166 ? 0.63783 0.52605 0.64333 0.06490  -0.07386 -0.13970 173 ARG A CZ  
1221 N NH1 . ARG A 166 ? 0.58283 0.44914 0.59197 0.06559  -0.08739 -0.14743 173 ARG A NH1 
1222 N NH2 . ARG A 166 ? 0.68582 0.57992 0.69486 0.06844  -0.06285 -0.12973 173 ARG A NH2 
1223 N N   . THR A 167 ? 0.33158 0.32836 0.25551 0.07649  -0.07117 -0.14230 174 THR A N   
1224 C CA  . THR A 167 ? 0.36916 0.36504 0.29764 0.06921  -0.08414 -0.14367 174 THR A CA  
1225 C C   . THR A 167 ? 0.43454 0.40514 0.39525 0.05298  -0.09778 -0.14827 174 THR A C   
1226 O O   . THR A 167 ? 0.44449 0.39330 0.41355 0.05400  -0.10599 -0.15999 174 THR A O   
1227 C CB  . THR A 167 ? 0.45100 0.45553 0.35028 0.08749  -0.09755 -0.16270 174 THR A CB  
1228 O OG1 . THR A 167 ? 0.53794 0.57090 0.40731 0.10193  -0.08226 -0.15309 174 THR A OG1 
1229 C CG2 . THR A 167 ? 0.55415 0.55877 0.46287 0.07977  -0.11371 -0.16481 174 THR A CG2 
1230 N N   . ASP A 168 ? 0.36857 0.34353 0.34971 0.03800  -0.09802 -0.13494 175 ASP A N   
1231 C CA  . ASP A 168 ? 0.44374 0.40200 0.45930 0.02107  -0.10768 -0.13401 175 ASP A CA  
1232 C C   . ASP A 168 ? 0.57243 0.52920 0.59573 0.01922  -0.12943 -0.14813 175 ASP A C   
1233 O O   . ASP A 168 ? 0.51970 0.49537 0.53291 0.02359  -0.13532 -0.14960 175 ASP A O   
1234 C CB  . ASP A 168 ? 0.38499 0.35322 0.42086 0.00741  -0.09407 -0.11072 175 ASP A CB  
1235 C CG  . ASP A 168 ? 0.58516 0.54215 0.65723 -0.00940 -0.09979 -0.10536 175 ASP A CG  
1236 O OD1 . ASP A 168 ? 0.67977 0.61566 0.76196 -0.01300 -0.10213 -0.10852 175 ASP A OD1 
1237 O OD2 . ASP A 168 ? 0.50928 0.47993 0.60044 -0.01823 -0.10138 -0.09641 175 ASP A OD2 
1238 N N   . THR A 169 ? 0.68556 0.62209 0.72668 0.01326  -0.13803 -0.15285 176 THR A N   
1239 C CA  . THR A 169 ? 0.88230 0.81700 0.93554 0.00928  -0.15550 -0.16163 176 THR A CA  
1240 C C   . THR A 169 ? 0.82994 0.76309 0.92428 -0.01236 -0.15808 -0.14834 176 THR A C   
1241 O O   . THR A 169 ? 0.80363 0.73399 0.91474 -0.01910 -0.17259 -0.15423 176 THR A O   
1242 C CB  . THR A 169 ? 0.99322 0.90693 1.03622 0.01929  -0.16576 -0.17827 176 THR A CB  
1243 O OG1 . THR A 169 ? 0.80373 0.69740 0.85198 0.01810  -0.15723 -0.17325 176 THR A OG1 
1244 C CG2 . THR A 169 ? 0.63489 0.56019 0.63825 0.04264  -0.16747 -0.19329 176 THR A CG2 
1245 N N   . GLY A 170 ? 0.81352 0.75040 0.92463 -0.02287 -0.14383 -0.13011 177 GLY A N   
1246 C CA  . GLY A 170 ? 0.76072 0.70213 0.90954 -0.04149 -0.14208 -0.11388 177 GLY A CA  
1247 C C   . GLY A 170 ? 0.59014 0.55958 0.75361 -0.04650 -0.14744 -0.11009 177 GLY A C   
1248 O O   . GLY A 170 ? 0.57546 0.55619 0.72044 -0.03608 -0.15768 -0.12274 177 GLY A O   
1249 N N   . GLU A 171 ? 0.57580 0.55940 0.77132 -0.06045 -0.14012 -0.09187 178 GLU A N   
1250 C CA  . GLU A 171 ? 0.49447 0.50924 0.70728 -0.06367 -0.14403 -0.08668 178 GLU A CA  
1251 C C   . GLU A 171 ? 0.44031 0.47155 0.62983 -0.04986 -0.14085 -0.08889 178 GLU A C   
1252 O O   . GLU A 171 ? 0.35014 0.37689 0.52596 -0.04527 -0.12556 -0.08125 178 GLU A O   
1253 C CB  . GLU A 171 ? 0.49787 0.52962 0.74652 -0.07752 -0.13181 -0.06441 178 GLU A CB  
1254 C CG  . GLU A 171 ? 0.53834 0.56723 0.81743 -0.09277 -0.13833 -0.05970 178 GLU A CG  
1255 C CD  . GLU A 171 ? 0.52595 0.56666 0.81415 -0.09472 -0.15826 -0.07301 178 GLU A CD  
1256 O OE1 . GLU A 171 ? 0.53956 0.55770 0.82480 -0.09695 -0.17285 -0.08718 178 GLU A OE1 
1257 O OE2 . GLU A 171 ? 0.59622 0.66917 0.89438 -0.09273 -0.16003 -0.06975 178 GLU A OE2 
1258 N N   . PRO A 172 ? 0.44309 0.49227 0.62336 -0.04144 -0.15334 -0.09744 179 PRO A N   
1259 C CA  . PRO A 172 ? 0.50816 0.57340 0.66384 -0.02660 -0.14720 -0.09334 179 PRO A CA  
1260 C C   . PRO A 172 ? 0.50410 0.58700 0.67783 -0.02924 -0.12951 -0.07141 179 PRO A C   
1261 O O   . PRO A 172 ? 0.50922 0.61114 0.72143 -0.03988 -0.13272 -0.06416 179 PRO A O   
1262 C CB  . PRO A 172 ? 0.47944 0.56168 0.62616 -0.01760 -0.16737 -0.10584 179 PRO A CB  
1263 C CG  . PRO A 172 ? 0.53609 0.60125 0.68646 -0.02394 -0.17971 -0.11997 179 PRO A CG  
1264 C CD  . PRO A 172 ? 0.53694 0.58533 0.71697 -0.04129 -0.17192 -0.11188 179 PRO A CD  
1265 N N   . MET A 173 ? 0.34432 0.42205 0.49086 -0.01889 -0.11112 -0.06119 180 MET A N   
1266 C CA  . MET A 173 ? 0.34333 0.43185 0.50127 -0.01847 -0.09430 -0.04356 180 MET A CA  
1267 C C   . MET A 173 ? 0.40562 0.51192 0.55550 -0.00529 -0.09442 -0.03725 180 MET A C   
1268 O O   . MET A 173 ? 0.46515 0.58337 0.62848 -0.00276 -0.08381 -0.02518 180 MET A O   
1269 C CB  . MET A 173 ? 0.31575 0.38453 0.45296 -0.01638 -0.07527 -0.03649 180 MET A CB  
1270 C CG  . MET A 173 ? 0.61829 0.66633 0.75312 -0.02397 -0.07409 -0.04249 180 MET A CG  
1271 S SD  . MET A 173 ? 0.56506 0.59720 0.67293 -0.01834 -0.05449 -0.03509 180 MET A SD  
1272 C CE  . MET A 173 ? 0.35593 0.40123 0.47091 -0.01413 -0.04238 -0.02060 180 MET A CE  
1273 N N   . GLY A 174 ? 0.30257 0.41033 0.42828 0.00547  -0.10542 -0.04444 181 GLY A N   
1274 C CA  . GLY A 174 ? 0.31857 0.43921 0.43334 0.01983  -0.10528 -0.03595 181 GLY A CA  
1275 C C   . GLY A 174 ? 0.30956 0.41083 0.39415 0.02846  -0.08850 -0.02511 181 GLY A C   
1276 O O   . GLY A 174 ? 0.27520 0.37092 0.32968 0.03879  -0.09017 -0.02358 181 GLY A O   
1277 N N   . ARG A 175 ? 0.21438 0.30602 0.30721 0.02408  -0.07280 -0.01704 182 ARG A N   
1278 C CA  . ARG A 175 ? 0.25030 0.32088 0.31998 0.02890  -0.05857 -0.00842 182 ARG A CA  
1279 C C   . ARG A 175 ? 0.27868 0.34163 0.36141 0.02195  -0.04551 -0.00532 182 ARG A C   
1280 O O   . ARG A 175 ? 0.20876 0.28710 0.31556 0.02123  -0.04394 -0.00285 182 ARG A O   
1281 C CB  . ARG A 175 ? 0.21759 0.28830 0.27647 0.04330  -0.05829 0.00186  182 ARG A CB  
1282 C CG  . ARG A 175 ? 0.25312 0.29741 0.28879 0.04613  -0.04651 0.01106  182 ARG A CG  
1283 C CD  . ARG A 175 ? 0.23838 0.27532 0.27167 0.05917  -0.04461 0.02142  182 ARG A CD  
1284 N NE  . ARG A 175 ? 0.22792 0.27482 0.28423 0.06236  -0.04159 0.01956  182 ARG A NE  
1285 C CZ  . ARG A 175 ? 0.23406 0.30432 0.30728 0.07256  -0.04832 0.02052  182 ARG A CZ  
1286 N NH1 . ARG A 175 ? 0.24394 0.32894 0.31386 0.08034  -0.06079 0.02218  182 ARG A NH1 
1287 N NH2 . ARG A 175 ? 0.22234 0.30509 0.31614 0.07646  -0.04245 0.02000  182 ARG A NH2 
1288 N N   . GLY A 176 ? 0.36812 0.37653 0.18297 0.07034  -0.04558 0.04443  183 GLY A N   
1289 C CA  . GLY A 176 ? 0.31646 0.32475 0.18359 0.05442  -0.03740 0.04092  183 GLY A CA  
1290 C C   . GLY A 176 ? 0.30106 0.29537 0.17819 0.03933  -0.02428 0.02960  183 GLY A C   
1291 O O   . GLY A 176 ? 0.35582 0.33408 0.20149 0.04487  -0.01224 0.02970  183 GLY A O   
1292 N N   . THR A 177 ? 0.25520 0.25683 0.17433 0.02379  -0.02555 0.02111  184 THR A N   
1293 C CA  . THR A 177 ? 0.23774 0.23052 0.17204 0.01302  -0.01424 0.01307  184 THR A CA  
1294 C C   . THR A 177 ? 0.37401 0.37823 0.33164 -0.00176 -0.02860 -0.00222 184 THR A C   
1295 O O   . THR A 177 ? 0.26491 0.28636 0.24508 -0.00657 -0.03929 -0.00263 184 THR A O   
1296 C CB  . THR A 177 ? 0.26843 0.25460 0.23131 0.01013  0.00580  0.02520  184 THR A CB  
1297 O OG1 . THR A 177 ? 0.30711 0.27921 0.24689 0.02126  0.02356  0.04194  184 THR A OG1 
1298 C CG2 . THR A 177 ? 0.27495 0.26445 0.26080 0.00157  0.01415  0.01821  184 THR A CG2 
1299 N N   . LYS A 178 ? 0.23260 0.22444 0.18164 -0.00655 -0.02614 -0.01320 185 LYS A N   
1300 C CA  . LYS A 178 ? 0.23275 0.22512 0.19773 -0.02033 -0.03549 -0.02506 185 LYS A CA  
1301 C C   . LYS A 178 ? 0.28467 0.26673 0.26442 -0.01857 -0.02086 -0.02402 185 LYS A C   
1302 O O   . LYS A 178 ? 0.26586 0.23154 0.22510 -0.00856 -0.00892 -0.02531 185 LYS A O   
1303 C CB  . LYS A 178 ? 0.31908 0.29844 0.25180 -0.02715 -0.04940 -0.04035 185 LYS A CB  
1304 C CG  . LYS A 178 ? 0.54244 0.51847 0.48939 -0.04565 -0.05933 -0.05059 185 LYS A CG  
1305 C CD  . LYS A 178 ? 0.55316 0.50375 0.46345 -0.05634 -0.07135 -0.06836 185 LYS A CD  
1306 C CE  . LYS A 178 ? 0.67091 0.63128 0.54849 -0.05066 -0.08430 -0.07259 185 LYS A CE  
1307 N NZ  . LYS A 178 ? 0.78658 0.72376 0.63117 -0.05790 -0.09159 -0.09135 185 LYS A NZ  
1308 N N   . VAL A 179 ? 0.22451 0.21895 0.23780 -0.02522 -0.02156 -0.02121 186 VAL A N   
1309 C CA  . VAL A 179 ? 0.18372 0.17770 0.21459 -0.02224 -0.01220 -0.01915 186 VAL A CA  
1310 C C   . VAL A 179 ? 0.27029 0.25165 0.29790 -0.02817 -0.01928 -0.02641 186 VAL A C   
1311 O O   . VAL A 179 ? 0.22059 0.21094 0.26089 -0.03858 -0.02833 -0.02709 186 VAL A O   
1312 C CB  . VAL A 179 ? 0.20431 0.21865 0.26894 -0.02570 -0.00992 -0.01175 186 VAL A CB  
1313 C CG1 . VAL A 179 ? 0.19617 0.22046 0.28131 -0.02229 -0.00504 -0.00985 186 VAL A CG1 
1314 C CG2 . VAL A 179 ? 0.21404 0.23124 0.28055 -0.02320 -0.00032 -0.00275 186 VAL A CG2 
1315 N N   . ILE A 180 ? 0.22017 0.17712 0.22803 -0.01995 -0.01255 -0.03055 187 ILE A N   
1316 C CA  . ILE A 180 ? 0.24159 0.17324 0.23948 -0.02441 -0.01602 -0.03553 187 ILE A CA  
1317 C C   . ILE A 180 ? 0.28725 0.22499 0.30310 -0.01138 -0.00835 -0.02695 187 ILE A C   
1318 O O   . ILE A 180 ? 0.25090 0.18871 0.26561 0.00669  0.00359  -0.02359 187 ILE A O   
1319 C CB  . ILE A 180 ? 0.28042 0.16876 0.23619 -0.02251 -0.01440 -0.04766 187 ILE A CB  
1320 C CG1 . ILE A 180 ? 0.26818 0.15892 0.20481 -0.03463 -0.02638 -0.05698 187 ILE A CG1 
1321 C CG2 . ILE A 180 ? 0.34295 0.19458 0.28709 -0.03022 -0.01626 -0.05144 187 ILE A CG2 
1322 C CD1 . ILE A 180 ? 0.43054 0.27961 0.31747 -0.02984 -0.02524 -0.07175 187 ILE A CD1 
1323 N N   . LEU A 181 ? 0.24258 0.18966 0.27432 -0.01837 -0.01491 -0.02243 188 LEU A N   
1324 C CA  . LEU A 181 ? 0.25299 0.21090 0.29929 -0.00534 -0.01244 -0.01360 188 LEU A CA  
1325 C C   . LEU A 181 ? 0.24661 0.16304 0.26803 0.00094  -0.00896 -0.01190 188 LEU A C   
1326 O O   . LEU A 181 ? 0.29246 0.19132 0.30469 -0.01380 -0.01339 -0.01187 188 LEU A O   
1327 C CB  . LEU A 181 ? 0.22696 0.21594 0.29619 -0.01392 -0.02166 -0.00979 188 LEU A CB  
1328 C CG  . LEU A 181 ? 0.26992 0.28669 0.35879 -0.02226 -0.02483 -0.01221 188 LEU A CG  
1329 C CD1 . LEU A 181 ? 0.30082 0.33609 0.40180 -0.02848 -0.03342 -0.01185 188 LEU A CD1 
1330 C CD2 . LEU A 181 ? 0.21142 0.24702 0.31767 -0.01378 -0.01767 -0.00897 188 LEU A CD2 
1331 N N   . HIS A 182 ? 0.26697 0.16647 0.27765 0.02383  0.00128  -0.00886 189 HIS A N   
1332 C CA  . HIS A 182 ? 0.29171 0.14387 0.27564 0.03585  0.00699  -0.00448 189 HIS A CA  
1333 C C   . HIS A 182 ? 0.31118 0.19096 0.31385 0.04928  0.00290  0.01058  189 HIS A C   
1334 O O   . HIS A 182 ? 0.29309 0.20549 0.31513 0.07239  0.00515  0.01821  189 HIS A O   
1335 C CB  . HIS A 182 ? 0.33161 0.14847 0.28979 0.06011  0.02143  -0.00836 189 HIS A CB  
1336 C CG  . HIS A 182 ? 0.38894 0.18554 0.32405 0.04963  0.02368  -0.02445 189 HIS A CG  
1337 N ND1 . HIS A 182 ? 0.53191 0.26426 0.42288 0.03949  0.02419  -0.03840 189 HIS A ND1 
1338 C CD2 . HIS A 182 ? 0.39160 0.22221 0.33806 0.04697  0.02447  -0.02854 189 HIS A CD2 
1339 C CE1 . HIS A 182 ? 0.52976 0.26173 0.40410 0.03294  0.02285  -0.05176 189 HIS A CE1 
1340 N NE2 . HIS A 182 ? 0.48155 0.27185 0.38788 0.03904  0.02442  -0.04422 189 HIS A NE2 
1341 N N   . LEU A 183 ? 0.29175 0.16293 0.28872 0.03512  -0.00326 0.01552  190 LEU A N   
1342 C CA  . LEU A 183 ? 0.26878 0.17434 0.27989 0.04363  -0.01113 0.02744  190 LEU A CA  
1343 C C   . LEU A 183 ? 0.33193 0.22024 0.32833 0.07479  -0.00646 0.04249  190 LEU A C   
1344 O O   . LEU A 183 ? 0.36235 0.19119 0.32714 0.08417  0.00501  0.04619  190 LEU A O   
1345 C CB  . LEU A 183 ? 0.25627 0.15647 0.25966 0.02205  -0.01507 0.02959  190 LEU A CB  
1346 C CG  . LEU A 183 ? 0.25568 0.18330 0.27706 -0.00264 -0.02083 0.01806  190 LEU A CG  
1347 C CD1 . LEU A 183 ? 0.28432 0.21082 0.29879 -0.01758 -0.02050 0.02339  190 LEU A CD1 
1348 C CD2 . LEU A 183 ? 0.26266 0.23942 0.31156 0.00147  -0.02947 0.01330  190 LEU A CD2 
1349 N N   . LYS A 184 ? 0.27974 0.21888 0.29748 0.09116  -0.01662 0.05099  191 LYS A N   
1350 C CA  . LYS A 184 ? 0.37724 0.31112 0.38202 0.12421  -0.01622 0.06872  191 LYS A CA  
1351 C C   . LYS A 184 ? 0.43784 0.32078 0.40314 0.12150  -0.01219 0.08089  191 LYS A C   
1352 O O   . LYS A 184 ? 0.40756 0.28674 0.36741 0.09434  -0.01442 0.07688  191 LYS A O   
1353 C CB  . LYS A 184 ? 0.39559 0.40447 0.43302 0.13664  -0.03397 0.07357  191 LYS A CB  
1354 C CG  . LYS A 184 ? 0.37729 0.44320 0.46072 0.13907  -0.03611 0.06622  191 LYS A CG  
1355 C CD  . LYS A 184 ? 0.39711 0.53460 0.51482 0.13116  -0.05809 0.06365  191 LYS A CD  
1356 C CE  . LYS A 184 ? 0.39938 0.58497 0.56301 0.12175  -0.05745 0.05479  191 LYS A CE  
1357 N NZ  . LYS A 184 ? 0.47936 0.71215 0.66928 0.10444  -0.07790 0.04707  191 LYS A NZ  
1358 N N   . GLU A 185 ? 0.42344 0.26748 0.36112 0.15240  -0.00394 0.09822  192 GLU A N   
1359 C CA  . GLU A 185 ? 0.55110 0.33804 0.44935 0.14658  0.00489  0.11089  192 GLU A CA  
1360 C C   . GLU A 185 ? 0.59360 0.40824 0.48487 0.14127  -0.00528 0.12217  192 GLU A C   
1361 O O   . GLU A 185 ? 0.63767 0.41280 0.50338 0.12266  0.00438  0.12973  192 GLU A O   
1362 C CB  . GLU A 185 ? 0.66986 0.43168 0.54956 0.17342  0.01304  0.12099  192 GLU A CB  
1363 C CG  . GLU A 185 ? 0.97395 0.66312 0.81446 0.16341  0.02756  0.12998  192 GLU A CG  
1364 C CD  . GLU A 185 ? 1.24173 0.90421 1.06117 0.19475  0.03589  0.14140  192 GLU A CD  
1365 O OE1 . GLU A 185 ? 1.36652 0.96054 1.15548 0.18794  0.05031  0.14429  192 GLU A OE1 
1366 O OE2 . GLU A 185 ? 1.22989 0.94190 1.06510 0.22507  0.02765  0.14720  192 GLU A OE2 
1367 N N   . ASP A 186 ? 0.47176 0.35822 0.38692 0.15270  -0.02444 0.12060  193 ASP A N   
1368 C CA  . ASP A 186 ? 0.50554 0.42125 0.40791 0.14919  -0.03614 0.12642  193 ASP A CA  
1369 C C   . ASP A 186 ? 0.42339 0.37762 0.34963 0.11623  -0.04469 0.10497  193 ASP A C   
1370 O O   . ASP A 186 ? 0.40608 0.39057 0.32274 0.11472  -0.05639 0.10410  193 ASP A O   
1371 C CB  . ASP A 186 ? 0.57987 0.54760 0.49151 0.17189  -0.05338 0.12962  193 ASP A CB  
1372 C CG  . ASP A 186 ? 0.61096 0.64363 0.57260 0.17080  -0.06885 0.11359  193 ASP A CG  
1373 O OD1 . ASP A 186 ? 0.69669 0.72513 0.68228 0.16552  -0.06072 0.10521  193 ASP A OD1 
1374 O OD2 . ASP A 186 ? 0.79138 0.87653 0.76765 0.17282  -0.08786 0.10921  193 ASP A OD2 
1375 N N   . GLN A 187 ? 0.33069 0.28007 0.28186 0.09255  -0.03864 0.08789  194 GLN A N   
1376 C CA  . GLN A 187 ? 0.29720 0.27710 0.27008 0.06556  -0.04470 0.06927  194 GLN A CA  
1377 C C   . GLN A 187 ? 0.32274 0.26905 0.28903 0.03914  -0.03023 0.06553  194 GLN A C   
1378 O O   . GLN A 187 ? 0.30740 0.27103 0.29503 0.01963  -0.03186 0.05042  194 GLN A O   
1379 C CB  . GLN A 187 ? 0.26657 0.28231 0.27868 0.06202  -0.05249 0.05409  194 GLN A CB  
1380 C CG  . GLN A 187 ? 0.25343 0.31807 0.28492 0.08284  -0.06851 0.05701  194 GLN A CG  
1381 C CD  . GLN A 187 ? 0.31467 0.41247 0.33682 0.08253  -0.08693 0.05482  194 GLN A CD  
1382 O OE1 . GLN A 187 ? 0.31693 0.41467 0.33300 0.06263  -0.08889 0.04297  194 GLN A OE1 
1383 N NE2 . GLN A 187 ? 0.38560 0.51205 0.40346 0.10731  -0.10105 0.06580  194 GLN A NE2 
1384 N N   . THR A 188 ? 0.39276 0.29257 0.33111 0.03778  -0.01610 0.08048  195 THR A N   
1385 C CA  . THR A 188 ? 0.48140 0.35584 0.42120 0.00870  -0.00366 0.07715  195 THR A CA  
1386 C C   . THR A 188 ? 0.40737 0.31134 0.35120 -0.00658 -0.00165 0.07632  195 THR A C   
1387 O O   . THR A 188 ? 0.43097 0.33005 0.38543 -0.03105 0.00744  0.07397  195 THR A O   
1388 C CB  . THR A 188 ? 0.49965 0.30962 0.41060 0.00663  0.01237  0.09332  195 THR A CB  
1389 O OG1 . THR A 188 ? 0.55467 0.35398 0.43510 0.02405  0.01782  0.11573  195 THR A OG1 
1390 C CG2 . THR A 188 ? 0.48060 0.25197 0.38381 0.02297  0.01361  0.09066  195 THR A CG2 
1391 N N   . GLU A 189 ? 0.36277 0.29916 0.29798 0.00790  -0.01018 0.07726  196 GLU A N   
1392 C CA  . GLU A 189 ? 0.39453 0.35701 0.32953 -0.00192 -0.00636 0.07350  196 GLU A CA  
1393 C C   . GLU A 189 ? 0.37124 0.35783 0.33992 -0.01894 -0.00979 0.05445  196 GLU A C   
1394 O O   . GLU A 189 ? 0.29122 0.29334 0.26661 -0.03000 -0.00093 0.05327  196 GLU A O   
1395 C CB  . GLU A 189 ? 0.36956 0.35723 0.28249 0.01786  -0.01838 0.07203  196 GLU A CB  
1396 C CG  . GLU A 189 ? 0.33967 0.35831 0.27422 0.02142  -0.03930 0.05153  196 GLU A CG  
1397 C CD  . GLU A 189 ? 0.50156 0.54229 0.41232 0.03871  -0.05636 0.04862  196 GLU A CD  
1398 O OE1 . GLU A 189 ? 0.46963 0.51160 0.36824 0.05719  -0.06554 0.05999  196 GLU A OE1 
1399 O OE2 . GLU A 189 ? 0.40850 0.46464 0.31040 0.03529  -0.06145 0.03428  196 GLU A OE2 
1400 N N   . TYR A 190 ? 0.30561 0.29719 0.29513 -0.01864 -0.02068 0.04181  197 TYR A N   
1401 C CA  . TYR A 190 ? 0.27410 0.28466 0.29011 -0.03086 -0.02410 0.02649  197 TYR A CA  
1402 C C   . TYR A 190 ? 0.31098 0.30865 0.33940 -0.04962 -0.01640 0.02640  197 TYR A C   
1403 O O   . TYR A 190 ? 0.31054 0.32309 0.35813 -0.05735 -0.02037 0.01572  197 TYR A O   
1404 C CB  . TYR A 190 ? 0.24437 0.26622 0.27551 -0.02363 -0.03645 0.01575  197 TYR A CB  
1405 C CG  . TYR A 190 ? 0.24988 0.29159 0.27376 -0.01113 -0.04819 0.01298  197 TYR A CG  
1406 C CD1 . TYR A 190 ? 0.24779 0.30402 0.26547 -0.01295 -0.05185 0.00365  197 TYR A CD1 
1407 C CD2 . TYR A 190 ? 0.22239 0.26853 0.24303 0.00390  -0.05643 0.01915  197 TYR A CD2 
1408 C CE1 . TYR A 190 ? 0.25770 0.32861 0.26312 -0.00460 -0.06584 -0.00276 197 TYR A CE1 
1409 C CE2 . TYR A 190 ? 0.25008 0.32161 0.26531 0.01300  -0.07181 0.01525  197 TYR A CE2 
1410 C CZ  . TYR A 190 ? 0.21514 0.29696 0.22096 0.00645  -0.07759 0.00275  197 TYR A CZ  
1411 O OH  . TYR A 190 ? 0.26469 0.36809 0.25993 0.01244  -0.09595 -0.00508 197 TYR A OH  
1412 N N   . LEU A 191 ? 0.26557 0.23420 0.28138 -0.05789 -0.00641 0.03826  198 LEU A N   
1413 C CA  . LEU A 191 ? 0.27525 0.23579 0.30323 -0.08245 -0.00047 0.03757  198 LEU A CA  
1414 C C   . LEU A 191 ? 0.33275 0.31520 0.36846 -0.09540 0.01160  0.04793  198 LEU A C   
1415 O O   . LEU A 191 ? 0.34449 0.33439 0.39954 -0.11936 0.01530  0.04782  198 LEU A O   
1416 C CB  . LEU A 191 ? 0.32867 0.23539 0.33835 -0.08924 0.00440  0.04245  198 LEU A CB  
1417 C CG  . LEU A 191 ? 0.34610 0.22942 0.34651 -0.07336 -0.00286 0.03340  198 LEU A CG  
1418 C CD1 . LEU A 191 ? 0.42694 0.24662 0.40043 -0.07458 0.00531  0.03885  198 LEU A CD1 
1419 C CD2 . LEU A 191 ? 0.39297 0.29727 0.41179 -0.08133 -0.01226 0.01608  198 LEU A CD2 
1420 N N   . GLU A 192 ? 0.28702 0.28277 0.30774 -0.08035 0.01786  0.05681  199 GLU A N   
1421 C CA  . GLU A 192 ? 0.31563 0.33248 0.33899 -0.08815 0.03463  0.06969  199 GLU A CA  
1422 C C   . GLU A 192 ? 0.31524 0.38109 0.36366 -0.08588 0.03343  0.05937  199 GLU A C   
1423 O O   . GLU A 192 ? 0.25133 0.32731 0.29449 -0.06797 0.02308  0.04660  199 GLU A O   
1424 C CB  . GLU A 192 ? 0.40657 0.41203 0.39216 -0.06865 0.04346  0.08429  199 GLU A CB  
1425 C CG  . GLU A 192 ? 0.49749 0.45282 0.45423 -0.06489 0.04696  0.09957  199 GLU A CG  
1426 C CD  . GLU A 192 ? 0.96874 0.91504 0.88590 -0.04844 0.06002  0.12034  199 GLU A CD  
1427 O OE1 . GLU A 192 ? 1.19500 1.15423 1.11201 -0.05888 0.08054  0.13424  199 GLU A OE1 
1428 O OE2 . GLU A 192 ? 1.06912 0.99991 0.95550 -0.02381 0.04994  0.12389  199 GLU A OE2 
1429 N N   . GLU A 193 ? 0.26420 0.36010 0.34094 -0.10411 0.04461  0.06583  200 GLU A N   
1430 C CA  . GLU A 193 ? 0.24049 0.38612 0.34516 -0.09875 0.04438  0.05836  200 GLU A CA  
1431 C C   . GLU A 193 ? 0.18545 0.34238 0.26687 -0.07035 0.05105  0.05604  200 GLU A C   
1432 O O   . GLU A 193 ? 0.23110 0.39686 0.31408 -0.05476 0.04173  0.04167  200 GLU A O   
1433 C CB  . GLU A 193 ? 0.25987 0.42975 0.39408 -0.11266 0.05510  0.06334  200 GLU A CB  
1434 C CG  . GLU A 193 ? 0.42382 0.64379 0.57949 -0.09808 0.06153  0.06172  200 GLU A CG  
1435 C CD  . GLU A 193 ? 0.72439 0.97101 0.91604 -0.11070 0.06414  0.06156  200 GLU A CD  
1436 O OE1 . GLU A 193 ? 0.71592 0.99459 0.92916 -0.10016 0.05665  0.05436  200 GLU A OE1 
1437 O OE2 . GLU A 193 ? 0.64685 0.88326 0.84540 -0.13100 0.07452  0.06990  200 GLU A OE2 
1438 N N   . ARG A 194 ? 0.25521 0.40589 0.30899 -0.06288 0.06761  0.06973  201 ARG A N   
1439 C CA  . ARG A 194 ? 0.29405 0.45368 0.31874 -0.03568 0.07411  0.06458  201 ARG A CA  
1440 C C   . ARG A 194 ? 0.29997 0.43013 0.29525 -0.01984 0.05279  0.04636  201 ARG A C   
1441 O O   . ARG A 194 ? 0.28256 0.41602 0.26214 -0.00180 0.05013  0.03216  201 ARG A O   
1442 C CB  . ARG A 194 ? 0.34179 0.49974 0.33456 -0.02901 0.09692  0.08391  201 ARG A CB  
1443 C CG  . ARG A 194 ? 0.41399 0.52925 0.37144 -0.03056 0.09313  0.09534  201 ARG A CG  
1444 C CD  . ARG A 194 ? 0.51977 0.63456 0.44910 -0.02751 0.12089  0.12097  201 ARG A CD  
1445 N NE  . ARG A 194 ? 0.62391 0.69445 0.51100 -0.02176 0.11748  0.13462  201 ARG A NE  
1446 C CZ  . ARG A 194 ? 0.72432 0.78277 0.56549 -0.00850 0.13607  0.15585  201 ARG A CZ  
1447 N NH1 . ARG A 194 ? 0.63916 0.72284 0.47382 -0.00247 0.15769  0.16042  201 ARG A NH1 
1448 N NH2 . ARG A 194 ? 0.73562 0.75297 0.53765 0.00103  0.12959  0.16892  201 ARG A NH2 
1449 N N   . ARG A 195 ? 0.22589 0.32713 0.21429 -0.02646 0.03827  0.04638  202 ARG A N   
1450 C CA  . ARG A 195 ? 0.27689 0.36141 0.24782 -0.01488 0.01754  0.03074  202 ARG A CA  
1451 C C   . ARG A 195 ? 0.26033 0.35097 0.25892 -0.01838 0.00549  0.01361  202 ARG A C   
1452 O O   . ARG A 195 ? 0.23705 0.32304 0.22447 -0.00872 -0.00460 -0.00189 202 ARG A O   
1453 C CB  . ARG A 195 ? 0.31453 0.37443 0.27536 -0.01673 0.00825  0.03885  202 ARG A CB  
1454 C CG  . ARG A 195 ? 0.28369 0.33886 0.23675 -0.00666 -0.01377 0.02532  202 ARG A CG  
1455 C CD  . ARG A 195 ? 0.31377 0.37224 0.22707 0.01024  -0.02019 0.02077  202 ARG A CD  
1456 N NE  . ARG A 195 ? 0.30285 0.36409 0.21361 0.01603  -0.04378 0.01051  202 ARG A NE  
1457 C CZ  . ARG A 195 ? 0.34136 0.41053 0.24913 0.01655  -0.05963 -0.01034 202 ARG A CZ  
1458 N NH1 . ARG A 195 ? 0.30773 0.37368 0.20708 0.01608  -0.05362 -0.02417 202 ARG A NH1 
1459 N NH2 . ARG A 195 ? 0.30667 0.38696 0.22111 0.01752  -0.08152 -0.01734 202 ARG A NH2 
1460 N N   . ILE A 196 ? 0.23498 0.33305 0.26634 -0.03305 0.00624  0.01618  203 ILE A N   
1461 C CA  . ILE A 196 ? 0.22102 0.32408 0.27357 -0.03380 -0.00331 0.00367  203 ILE A CA  
1462 C C   . ILE A 196 ? 0.20287 0.32286 0.25629 -0.02050 0.00375  -0.00244 203 ILE A C   
1463 O O   . ILE A 196 ? 0.21477 0.32285 0.26355 -0.01206 -0.00362 -0.01510 203 ILE A O   
1464 C CB  . ILE A 196 ? 0.23917 0.34758 0.31877 -0.05054 -0.00549 0.00745  203 ILE A CB  
1465 C CG1 . ILE A 196 ? 0.23036 0.31044 0.30198 -0.05852 -0.01147 0.01024  203 ILE A CG1 
1466 C CG2 . ILE A 196 ? 0.19484 0.31080 0.29060 -0.04740 -0.01362 -0.00217 203 ILE A CG2 
1467 C CD1 . ILE A 196 ? 0.27035 0.34583 0.35627 -0.07786 -0.01051 0.01408  203 ILE A CD1 
1468 N N   . LYS A 197 ? 0.17872 0.32504 0.23805 -0.01757 0.02027  0.00748  204 LYS A N   
1469 C CA  . LYS A 197 ? 0.17946 0.34287 0.23828 0.00163  0.03025  0.00280  204 LYS A CA  
1470 C C   . LYS A 197 ? 0.30419 0.43818 0.32087 0.01955  0.02861  -0.01131 204 LYS A C   
1471 O O   . LYS A 197 ? 0.25963 0.38124 0.26867 0.03410  0.02785  -0.02366 204 LYS A O   
1472 C CB  . LYS A 197 ? 0.23146 0.43599 0.30525 0.00432  0.05200  0.01785  204 LYS A CB  
1473 C CG  . LYS A 197 ? 0.35835 0.60022 0.47731 -0.01755 0.05398  0.03102  204 LYS A CG  
1474 C CD  . LYS A 197 ? 0.38702 0.67754 0.52410 -0.01263 0.07858  0.04617  204 LYS A CD  
1475 C CE  . LYS A 197 ? 0.61433 0.90353 0.75537 -0.03664 0.08879  0.06198  204 LYS A CE  
1476 N NZ  . LYS A 197 ? 0.54528 0.86588 0.71912 -0.04426 0.09900  0.06966  204 LYS A NZ  
1477 N N   . GLU A 198 ? 0.24218 0.36200 0.22740 0.01938  0.02773  -0.00972 205 GLU A N   
1478 C CA  . GLU A 198 ? 0.30165 0.39509 0.24233 0.03363  0.02139  -0.02597 205 GLU A CA  
1479 C C   . GLU A 198 ? 0.27120 0.33888 0.21530 0.02732  0.00038  -0.04397 205 GLU A C   
1480 O O   . GLU A 198 ? 0.26846 0.31268 0.19047 0.03704  -0.00257 -0.06166 205 GLU A O   
1481 C CB  . GLU A 198 ? 0.31581 0.40333 0.22299 0.03413  0.01933  -0.01858 205 GLU A CB  
1482 C CG  . GLU A 198 ? 0.37674 0.44027 0.23666 0.04454  0.00414  -0.03747 205 GLU A CG  
1483 C CD  . GLU A 198 ? 0.34459 0.40714 0.17358 0.04680  -0.00268 -0.02714 205 GLU A CD  
1484 O OE1 . GLU A 198 ? 0.38062 0.44726 0.23273 0.03540  -0.00949 -0.01368 205 GLU A OE1 
1485 O OE2 . GLU A 198 ? 0.39186 0.44715 0.16910 0.06288  -0.00045 -0.03186 205 GLU A OE2 
1486 N N   . ILE A 199 ? 0.22803 0.29688 0.19864 0.01071  -0.01226 -0.03948 206 ILE A N   
1487 C CA  . ILE A 199 ? 0.29761 0.34830 0.27673 0.00238  -0.02903 -0.05284 206 ILE A CA  
1488 C C   . ILE A 199 ? 0.29111 0.33208 0.28513 0.00564  -0.02404 -0.05821 206 ILE A C   
1489 O O   . ILE A 199 ? 0.28300 0.29668 0.26633 0.00564  -0.03041 -0.07297 206 ILE A O   
1490 C CB  . ILE A 199 ? 0.22829 0.28652 0.23164 -0.01139 -0.03876 -0.04410 206 ILE A CB  
1491 C CG1 . ILE A 199 ? 0.29151 0.35394 0.27497 -0.00893 -0.04518 -0.03819 206 ILE A CG1 
1492 C CG2 . ILE A 199 ? 0.21325 0.26101 0.23348 -0.02085 -0.05093 -0.05410 206 ILE A CG2 
1493 C CD1 . ILE A 199 ? 0.27851 0.34547 0.28103 -0.01542 -0.04714 -0.02469 206 ILE A CD1 
1494 N N   . VAL A 200 ? 0.22697 0.28906 0.24497 0.00798  -0.01338 -0.04579 207 VAL A N   
1495 C CA  . VAL A 200 ? 0.20965 0.26623 0.23972 0.01640  -0.00922 -0.04719 207 VAL A CA  
1496 C C   . VAL A 200 ? 0.25236 0.28915 0.25475 0.03769  0.00065  -0.05767 207 VAL A C   
1497 O O   . VAL A 200 ? 0.28102 0.28366 0.27362 0.04382  -0.00064 -0.06724 207 VAL A O   
1498 C CB  . VAL A 200 ? 0.25410 0.34765 0.31534 0.01545  -0.00335 -0.03196 207 VAL A CB  
1499 C CG1 . VAL A 200 ? 0.22395 0.31945 0.29347 0.03239  0.00157  -0.03053 207 VAL A CG1 
1500 C CG2 . VAL A 200 ? 0.20032 0.29778 0.27986 -0.00444 -0.01400 -0.02654 207 VAL A CG2 
1501 N N   . LYS A 201 ? 0.23912 0.29143 0.22418 0.05016  0.01282  -0.05571 208 LYS A N   
1502 C CA  . LYS A 201 ? 0.30151 0.33244 0.25307 0.07518  0.02535  -0.06694 208 LYS A CA  
1503 C C   . LYS A 201 ? 0.32470 0.30295 0.23531 0.07143  0.01275  -0.09041 208 LYS A C   
1504 O O   . LYS A 201 ? 0.39388 0.33093 0.27851 0.08604  0.01728  -0.10500 208 LYS A O   
1505 C CB  . LYS A 201 ? 0.36234 0.42573 0.30270 0.08920  0.04406  -0.05767 208 LYS A CB  
1506 C CG  . LYS A 201 ? 0.39885 0.44132 0.29779 0.12006  0.06104  -0.06939 208 LYS A CG  
1507 C CD  . LYS A 201 ? 0.45639 0.53561 0.34382 0.13298  0.08280  -0.05706 208 LYS A CD  
1508 C CE  . LYS A 201 ? 0.58477 0.63840 0.42006 0.16728  0.10157  -0.07105 208 LYS A CE  
1509 N NZ  . LYS A 201 ? 0.73707 0.83347 0.57770 0.17610  0.12478  -0.05108 208 LYS A NZ  
1510 N N   . LYS A 202 ? 0.36449 0.34267 0.26938 0.05169  -0.00413 -0.09457 209 LYS A N   
1511 C CA  . LYS A 202 ? 0.42606 0.36540 0.29621 0.04394  -0.02063 -0.11794 209 LYS A CA  
1512 C C   . LYS A 202 ? 0.38522 0.29214 0.27230 0.02766  -0.03163 -0.12756 209 LYS A C   
1513 O O   . LYS A 202 ? 0.42025 0.27945 0.27755 0.02707  -0.03605 -0.14873 209 LYS A O   
1514 C CB  . LYS A 202 ? 0.38827 0.34865 0.25277 0.03060  -0.03701 -0.11612 209 LYS A CB  
1515 C CG  . LYS A 202 ? 0.54069 0.47468 0.37395 0.01969  -0.05985 -0.14060 209 LYS A CG  
1516 C CD  . LYS A 202 ? 0.69034 0.64992 0.50347 0.01965  -0.07205 -0.13593 209 LYS A CD  
1517 C CE  . LYS A 202 ? 0.80084 0.75698 0.61677 -0.00239 -0.09266 -0.14314 209 LYS A CE  
1518 N NZ  . LYS A 202 ? 0.79138 0.77998 0.60268 -0.00177 -0.10570 -0.13136 209 LYS A NZ  
1519 N N   . HIS A 203 ? 0.33930 0.26699 0.27050 0.01376  -0.03458 -0.11235 210 HIS A N   
1520 C CA  . HIS A 203 ? 0.44890 0.35314 0.39845 -0.00585 -0.04437 -0.11747 210 HIS A CA  
1521 C C   . HIS A 203 ? 0.39380 0.28454 0.36201 0.00074  -0.03219 -0.10598 210 HIS A C   
1522 O O   . HIS A 203 ? 0.45712 0.31489 0.43050 -0.01229 -0.03496 -0.11027 210 HIS A O   
1523 C CB  . HIS A 203 ? 0.35831 0.29609 0.33940 -0.02682 -0.05835 -0.10954 210 HIS A CB  
1524 C CG  . HIS A 203 ? 0.33615 0.28889 0.30040 -0.03328 -0.07089 -0.11365 210 HIS A CG  
1525 N ND1 . HIS A 203 ? 0.48776 0.42092 0.43139 -0.04543 -0.07845 -0.12518 210 HIS A ND1 
1526 C CD2 . HIS A 203 ? 0.43114 0.41646 0.39477 -0.02909 -0.07676 -0.10617 210 HIS A CD2 
1527 C CE1 . HIS A 203 ? 0.49126 0.44834 0.42373 -0.04694 -0.09030 -0.12499 210 HIS A CE1 
1528 N NE2 . HIS A 203 ? 0.42913 0.41519 0.37176 -0.03522 -0.08878 -0.11226 210 HIS A NE2 
1529 N N   . SER A 204 ? 0.38480 0.30196 0.22614 -0.05136 -0.08170 -0.09855 211 SER A N   
1530 C CA  . SER A 204 ? 0.35643 0.24990 0.21994 -0.04059 -0.06992 -0.09219 211 SER A CA  
1531 C C   . SER A 204 ? 0.37808 0.24106 0.22255 -0.02086 -0.05371 -0.10517 211 SER A C   
1532 O O   . SER A 204 ? 0.41611 0.27794 0.27769 -0.00452 -0.04164 -0.09465 211 SER A O   
1533 C CB  . SER A 204 ? 0.41100 0.33711 0.30667 -0.03089 -0.06629 -0.06891 211 SER A CB  
1534 O OG  . SER A 204 ? 0.37839 0.33518 0.29254 -0.04312 -0.07951 -0.05686 211 SER A OG  
1535 N N   . GLN A 205 ? 0.44247 0.28653 0.25260 -0.02083 -0.05266 -0.12842 212 GLN A N   
1536 C CA  . GLN A 205 ? 0.57177 0.40119 0.36906 0.00250  -0.03411 -0.13833 212 GLN A CA  
1537 C C   . GLN A 205 ? 0.64293 0.42651 0.45223 0.01255  -0.02467 -0.14052 212 GLN A C   
1538 O O   . GLN A 205 ? 0.58003 0.36028 0.38997 0.03714  -0.00884 -0.13929 212 GLN A O   
1539 C CB  . GLN A 205 ? 0.61146 0.44883 0.38101 -0.00014 -0.03072 -0.15942 212 GLN A CB  
1540 C CG  . GLN A 205 ? 0.74040 0.54985 0.50421 -0.01830 -0.03758 -0.18261 212 GLN A CG  
1541 C CD  . GLN A 205 ? 0.98867 0.83012 0.75327 -0.04333 -0.05816 -0.18325 212 GLN A CD  
1542 O OE1 . GLN A 205 ? 0.63366 0.49587 0.41685 -0.05258 -0.06960 -0.16161 212 GLN A OE1 
1543 N NE2 . GLN A 205 ? 0.79289 0.64283 0.53948 -0.05048 -0.06449 -0.20863 212 GLN A NE2 
1544 N N   . PHE A 206 ? 0.53856 0.29252 0.36076 -0.00594 -0.03373 -0.13955 213 PHE A N   
1545 C CA  . PHE A 206 ? 0.60778 0.31519 0.44245 0.00197  -0.02522 -0.13672 213 PHE A CA  
1546 C C   . PHE A 206 ? 0.54832 0.25733 0.40976 0.00081  -0.02770 -0.11040 213 PHE A C   
1547 O O   . PHE A 206 ? 0.66895 0.33931 0.54253 -0.00047 -0.02480 -0.10191 213 PHE A O   
1548 C CB  . PHE A 206 ? 0.57577 0.24606 0.40833 -0.01900 -0.03075 -0.15440 213 PHE A CB  
1549 C CG  . PHE A 206 ? 0.67141 0.34054 0.47963 -0.01594 -0.02700 -0.18419 213 PHE A CG  
1550 C CD1 . PHE A 206 ? 0.72307 0.38176 0.52082 0.01261  -0.00980 -0.19404 213 PHE A CD1 
1551 C CD2 . PHE A 206 ? 0.69457 0.38074 0.49211 -0.04065 -0.04088 -0.20201 213 PHE A CD2 
1552 C CE1 . PHE A 206 ? 0.73156 0.39255 0.50594 0.01514  -0.00498 -0.22296 213 PHE A CE1 
1553 C CE2 . PHE A 206 ? 0.80131 0.49133 0.57491 -0.03753 -0.03784 -0.23184 213 PHE A CE2 
1554 C CZ  . PHE A 206 ? 0.77444 0.44996 0.53503 -0.01064 -0.01869 -0.24325 213 PHE A CZ  
1555 N N   . ILE A 207 ? 0.41412 0.18111 0.29493 0.00072  -0.03027 -0.09285 214 ILE A N   
1556 C CA  . ILE A 207 ? 0.37171 0.16412 0.28609 0.00242  -0.02822 -0.06710 214 ILE A CA  
1557 C C   . ILE A 207 ? 0.49548 0.28640 0.41539 0.03080  -0.01219 -0.05772 214 ILE A C   
1558 O O   . ILE A 207 ? 0.46725 0.27616 0.37676 0.04944  -0.00348 -0.06339 214 ILE A O   
1559 C CB  . ILE A 207 ? 0.36655 0.21552 0.29728 -0.00338 -0.03461 -0.05666 214 ILE A CB  
1560 C CG1 . ILE A 207 ? 0.33007 0.18797 0.26130 -0.02892 -0.05097 -0.05996 214 ILE A CG1 
1561 C CG2 . ILE A 207 ? 0.34096 0.22100 0.30144 0.00299  -0.02988 -0.03592 214 ILE A CG2 
1562 C CD1 . ILE A 207 ? 0.46012 0.30925 0.41046 -0.04829 -0.05757 -0.04977 214 ILE A CD1 
1563 N N   . GLY A 208 ? 0.39070 0.16665 0.32836 0.03378  -0.00831 -0.04022 215 GLY A N   
1564 C CA  . GLY A 208 ? 0.45722 0.22780 0.39904 0.06247  0.00618  -0.02905 215 GLY A CA  
1565 C C   . GLY A 208 ? 0.42838 0.26239 0.39071 0.07556  0.01164  -0.01074 215 GLY A C   
1566 O O   . GLY A 208 ? 0.44766 0.28998 0.42187 0.09403  0.02041  0.00760  215 GLY A O   
1567 N N   . TYR A 209 ? 0.33172 0.21042 0.29810 0.06621  0.00632  -0.01539 216 TYR A N   
1568 C CA  . TYR A 209 ? 0.34621 0.28233 0.32961 0.07390  0.01019  -0.00474 216 TYR A CA  
1569 C C   . TYR A 209 ? 0.31967 0.27916 0.29404 0.07373  0.01057  -0.01775 216 TYR A C   
1570 O O   . TYR A 209 ? 0.32374 0.26651 0.28404 0.06212  0.00411  -0.03012 216 TYR A O   
1571 C CB  . TYR A 209 ? 0.24196 0.20866 0.24615 0.05865  0.00296  0.00601  216 TYR A CB  
1572 C CG  . TYR A 209 ? 0.27031 0.22240 0.28554 0.05557  0.00300  0.02432  216 TYR A CG  
1573 C CD1 . TYR A 209 ? 0.24583 0.22227 0.27296 0.07073  0.01084  0.04465  216 TYR A CD1 
1574 C CD2 . TYR A 209 ? 0.29867 0.21667 0.31315 0.03563  -0.00526 0.02397  216 TYR A CD2 
1575 C CE1 . TYR A 209 ? 0.27591 0.23911 0.31368 0.06740  0.01155  0.06709  216 TYR A CE1 
1576 C CE2 . TYR A 209 ? 0.27749 0.18111 0.30411 0.02871  -0.00494 0.04435  216 TYR A CE2 
1577 C CZ  . TYR A 209 ? 0.27696 0.20123 0.31503 0.04538  0.00406  0.06732  216 TYR A CZ  
1578 O OH  . TYR A 209 ? 0.30939 0.22028 0.36012 0.03845  0.00514  0.09315  216 TYR A OH  
1579 N N   . PRO A 210 ? 0.32440 0.32605 0.30686 0.08449  0.01755  -0.01336 217 PRO A N   
1580 C CA  . PRO A 210 ? 0.28749 0.31163 0.26419 0.08009  0.01824  -0.02203 217 PRO A CA  
1581 C C   . PRO A 210 ? 0.29787 0.32747 0.28145 0.06018  0.00806  -0.02535 217 PRO A C   
1582 O O   . PRO A 210 ? 0.32520 0.37216 0.32601 0.05406  0.00421  -0.02106 217 PRO A O   
1583 C CB  . PRO A 210 ? 0.35371 0.42740 0.34362 0.09078  0.02628  -0.01441 217 PRO A CB  
1584 C CG  . PRO A 210 ? 0.35099 0.43760 0.35587 0.09757  0.02676  -0.00132 217 PRO A CG  
1585 C CD  . PRO A 210 ? 0.28218 0.31725 0.28000 0.09920  0.02451  0.00188  217 PRO A CD  
1586 N N   . ILE A 211 ? 0.30775 0.32457 0.27710 0.05255  0.00438  -0.03227 218 ILE A N   
1587 C CA  . ILE A 211 ? 0.25418 0.27429 0.22975 0.03814  -0.00440 -0.03214 218 ILE A CA  
1588 C C   . ILE A 211 ? 0.24443 0.28470 0.22009 0.03511  -0.00016 -0.03072 218 ILE A C   
1589 O O   . ILE A 211 ? 0.28410 0.32460 0.24245 0.03764  0.00413  -0.03150 218 ILE A O   
1590 C CB  . ILE A 211 ? 0.25821 0.25322 0.21872 0.03001  -0.01371 -0.03575 218 ILE A CB  
1591 C CG1 . ILE A 211 ? 0.29378 0.26778 0.25564 0.02712  -0.01854 -0.03690 218 ILE A CG1 
1592 C CG2 . ILE A 211 ? 0.25962 0.26303 0.22913 0.02035  -0.02201 -0.03071 218 ILE A CG2 
1593 C CD1 . ILE A 211 ? 0.30255 0.25274 0.24458 0.01700  -0.02750 -0.04503 218 ILE A CD1 
1594 N N   . THR A 212 ? 0.22623 0.28393 0.22073 0.02847  -0.00090 -0.02938 219 THR A N   
1595 C CA  . THR A 212 ? 0.23361 0.30746 0.23239 0.02021  0.00275  -0.02726 219 THR A CA  
1596 C C   . THR A 212 ? 0.20789 0.26298 0.21192 0.00973  -0.00441 -0.02398 219 THR A C   
1597 O O   . THR A 212 ? 0.20465 0.25258 0.22282 0.00883  -0.00933 -0.02775 219 THR A O   
1598 C CB  . THR A 212 ? 0.26253 0.36808 0.27834 0.01791  0.00711  -0.03085 219 THR A CB  
1599 O OG1 . THR A 212 ? 0.24520 0.37295 0.25800 0.03185  0.01386  -0.02885 219 THR A OG1 
1600 C CG2 . THR A 212 ? 0.26706 0.38754 0.28895 0.00296  0.00991  -0.02905 219 THR A CG2 
1601 N N   . LEU A 213 ? 0.22412 0.27417 0.21692 0.00424  -0.00412 -0.01525 220 LEU A N   
1602 C CA  . LEU A 213 ? 0.19295 0.22492 0.19166 -0.00371 -0.00995 -0.00588 220 LEU A CA  
1603 C C   . LEU A 213 ? 0.26512 0.30070 0.27874 -0.01698 -0.00534 -0.00344 220 LEU A C   
1604 O O   . LEU A 213 ? 0.24467 0.29856 0.25284 -0.02501 0.00105  0.00395  220 LEU A O   
1605 C CB  . LEU A 213 ? 0.21341 0.24241 0.19094 -0.00377 -0.01275 0.00630  220 LEU A CB  
1606 C CG  . LEU A 213 ? 0.30227 0.31716 0.28424 -0.00971 -0.01819 0.02411  220 LEU A CG  
1607 C CD1 . LEU A 213 ? 0.26295 0.25834 0.26416 -0.00427 -0.02591 0.02239  220 LEU A CD1 
1608 C CD2 . LEU A 213 ? 0.29261 0.31693 0.24903 -0.00833 -0.02209 0.03588  220 LEU A CD2 
1609 N N   . PHE A 214 ? 0.23303 0.25323 0.26552 -0.02020 -0.00813 -0.01121 221 PHE A N   
1610 C CA  . PHE A 214 ? 0.24749 0.26125 0.29446 -0.03672 -0.00521 -0.01314 221 PHE A CA  
1611 C C   . PHE A 214 ? 0.25892 0.24818 0.30476 -0.04618 -0.00607 0.00804  221 PHE A C   
1612 O O   . PHE A 214 ? 0.28629 0.25869 0.32543 -0.03651 -0.01120 0.02148  221 PHE A O   
1613 C CB  . PHE A 214 ? 0.23749 0.23411 0.30159 -0.03539 -0.00778 -0.03132 221 PHE A CB  
1614 C CG  . PHE A 214 ? 0.19861 0.22859 0.26610 -0.03202 -0.00575 -0.05047 221 PHE A CG  
1615 C CD1 . PHE A 214 ? 0.15812 0.21755 0.21524 -0.02089 -0.00412 -0.04775 221 PHE A CD1 
1616 C CD2 . PHE A 214 ? 0.22078 0.25127 0.30097 -0.03933 -0.00549 -0.07110 221 PHE A CD2 
1617 C CE1 . PHE A 214 ? 0.16570 0.25794 0.22681 -0.01619 -0.00224 -0.05913 221 PHE A CE1 
1618 C CE2 . PHE A 214 ? 0.23452 0.30499 0.31607 -0.03592 -0.00415 -0.08631 221 PHE A CE2 
1619 C CZ  . PHE A 214 ? 0.17167 0.27484 0.24457 -0.02391 -0.00250 -0.07720 221 PHE A CZ  
1620 N N   . VAL A 215 ? 0.24566 0.23690 0.29936 -0.06677 -0.00151 0.01351  222 VAL A N   
1621 C CA  . VAL A 215 ? 0.28125 0.24635 0.33764 -0.07929 -0.00150 0.03782  222 VAL A CA  
1622 C C   . VAL A 215 ? 0.36225 0.28099 0.44044 -0.09144 -0.00303 0.02988  222 VAL A C   
1623 O O   . VAL A 215 ? 0.31656 0.23354 0.40500 -0.09348 -0.00328 0.00260  222 VAL A O   
1624 C CB  . VAL A 215 ? 0.47364 0.47451 0.52299 -0.09656 0.00569  0.05536  222 VAL A CB  
1625 C CG1 . VAL A 215 ? 0.55125 0.59015 0.57575 -0.07993 0.00822  0.06018  222 VAL A CG1 
1626 C CG2 . VAL A 215 ? 0.34804 0.37790 0.41053 -0.11501 0.01039  0.03991  222 VAL A CG2 
1627 N N   . GLU A 216 ? 0.35761 0.23724 0.44171 -0.09844 -0.00385 0.05398  223 GLU A N   
1628 C CA  . GLU A 216 ? 0.48095 0.30181 0.58539 -0.10787 -0.00458 0.04797  223 GLU A CA  
1629 C C   . GLU A 216 ? 0.54621 0.35286 0.66019 -0.14179 -0.00037 0.06617  223 GLU A C   
1630 O O   . GLU A 216 ? 0.55321 0.39376 0.65774 -0.15261 0.00296  0.09362  223 GLU A O   
1631 C CB  . GLU A 216 ? 0.53784 0.31332 0.64666 -0.08384 -0.00911 0.06365  223 GLU A CB  
1632 C CG  . GLU A 216 ? 0.51180 0.30831 0.61365 -0.05336 -0.01387 0.05068  223 GLU A CG  
1633 C CD  . GLU A 216 ? 0.61728 0.38058 0.72680 -0.02892 -0.01863 0.06886  223 GLU A CD  
1634 O OE1 . GLU A 216 ? 0.56988 0.27951 0.69765 -0.02414 -0.01712 0.06391  223 GLU A OE1 
1635 O OE2 . GLU A 216 ? 0.57355 0.36548 0.67096 -0.01404 -0.02397 0.08751  223 GLU A OE2 
1636 N N   . LYS A 217 ? 0.61369 0.37062 0.74625 -0.15969 -0.00017 0.04952  224 LYS A N   
1637 C CA  . LYS A 217 ? 0.72150 0.46211 0.85752 -0.19301 0.00568  0.06050  224 LYS A CA  
1638 C C   . LYS A 217 ? 0.87815 0.60901 1.00763 -0.19223 0.00928  0.10618  224 LYS A C   
1639 O O   . LYS A 217 ? 0.89623 0.58022 1.02207 -0.17160 0.00763  0.12169  224 LYS A O   
1640 C CB  . LYS A 217 ? 0.92638 0.60267 1.06109 -0.20102 0.00570  0.03365  224 LYS A CB  
1641 C CG  . LYS A 217 ? 0.91419 0.58211 1.04761 -0.17955 -0.00111 -0.00605 224 LYS A CG  
1642 C CD  . LYS A 217 ? 0.98345 0.59067 1.11088 -0.18760 -0.00440 -0.02939 224 LYS A CD  
1643 C CE  . LYS A 217 ? 0.94487 0.57659 1.07460 -0.22404 -0.01240 -0.05038 224 LYS A CE  
1644 N NZ  . LYS A 217 ? 0.94969 0.55388 1.07532 -0.21761 -0.01779 -0.09097 224 LYS A NZ  
# 
