data_7HBX
# 
_entry.id   7HBX 
# 
_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   7HBX         pdb_00007hbx 10.2210/pdb7hbx/pdb 
WWPDB D_1001407279 ?            ?                   
# 
_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                        7HBX 
_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-5-phenyl-1,2-oxazol-4-yl)methanol' 189.211   1  ?        ? ? ? 
3 water       nat water                                         18.015    54 ?        ? ? ? 
# 
_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-5-phenyl-1,2-oxazol-4-yl)methanol' A1AY7 
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 
A1AY7 non-polymer         . '(3-methyl-5-phenyl-1,2-oxazol-4-yl)methanol' ? 'C11 H11 N O2'   189.211 
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        A1AY7 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1AY7 
_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 A1AY7 1  301 301 A1AY7 EYI A . 
C 3 HOH   1  401 46  HOH   HOH A . 
C 3 HOH   2  402 12  HOH   HOH A . 
C 3 HOH   3  403 48  HOH   HOH A . 
C 3 HOH   4  404 54  HOH   HOH A . 
C 3 HOH   5  405 23  HOH   HOH A . 
C 3 HOH   6  406 40  HOH   HOH A . 
C 3 HOH   7  407 4   HOH   HOH A . 
C 3 HOH   8  408 25  HOH   HOH A . 
C 3 HOH   9  409 31  HOH   HOH A . 
C 3 HOH   10 410 17  HOH   HOH A . 
C 3 HOH   11 411 10  HOH   HOH A . 
C 3 HOH   12 412 21  HOH   HOH A . 
C 3 HOH   13 413 2   HOH   HOH A . 
C 3 HOH   14 414 7   HOH   HOH A . 
C 3 HOH   15 415 18  HOH   HOH A . 
C 3 HOH   16 416 53  HOH   HOH A . 
C 3 HOH   17 417 3   HOH   HOH A . 
C 3 HOH   18 418 34  HOH   HOH A . 
C 3 HOH   19 419 24  HOH   HOH A . 
C 3 HOH   20 420 15  HOH   HOH A . 
C 3 HOH   21 421 13  HOH   HOH A . 
C 3 HOH   22 422 51  HOH   HOH A . 
C 3 HOH   23 423 5   HOH   HOH A . 
C 3 HOH   24 424 41  HOH   HOH A . 
C 3 HOH   25 425 19  HOH   HOH A . 
C 3 HOH   26 426 8   HOH   HOH A . 
C 3 HOH   27 427 6   HOH   HOH A . 
C 3 HOH   28 428 14  HOH   HOH A . 
C 3 HOH   29 429 33  HOH   HOH A . 
C 3 HOH   30 430 16  HOH   HOH A . 
C 3 HOH   31 431 1   HOH   HOH A . 
C 3 HOH   32 432 26  HOH   HOH A . 
C 3 HOH   33 433 38  HOH   HOH A . 
C 3 HOH   34 434 11  HOH   HOH A . 
C 3 HOH   35 435 28  HOH   HOH A . 
C 3 HOH   36 436 9   HOH   HOH A . 
C 3 HOH   37 437 43  HOH   HOH A . 
C 3 HOH   38 438 47  HOH   HOH A . 
C 3 HOH   39 439 20  HOH   HOH A . 
C 3 HOH   40 440 22  HOH   HOH A . 
C 3 HOH   41 441 30  HOH   HOH A . 
C 3 HOH   42 442 44  HOH   HOH A . 
C 3 HOH   43 443 42  HOH   HOH A . 
C 3 HOH   44 444 35  HOH   HOH A . 
C 3 HOH   45 445 36  HOH   HOH A . 
C 3 HOH   46 446 27  HOH   HOH A . 
C 3 HOH   47 447 50  HOH   HOH A . 
C 3 HOH   48 448 29  HOH   HOH A . 
C 3 HOH   49 449 37  HOH   HOH A . 
C 3 HOH   50 450 49  HOH   HOH A . 
C 3 HOH   51 451 39  HOH   HOH A . 
C 3 HOH   52 452 52  HOH   HOH A . 
C 3 HOH   53 453 32  HOH   HOH A . 
C 3 HOH   54 454 45  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             620546.374 
_cell.length_a           70.720 
_cell.length_b           89.620 
_cell.length_c           97.910 
_cell.angle_beta         90.000 
_cell.angle_gamma        90.000 
_cell.angle_alpha        90.000 
_cell.entry_id           7HBX 
_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                         7HBX 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
# 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
_exptl.entry_id          7HBX 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_Matthews      2.88 
_exptl_crystal.density_percent_sol   57.23 
_exptl_crystal.density_meas          ? 
_exptl_crystal.description           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.pH              8.5 
_exptl_crystal_grow.temp            277 
_exptl_crystal_grow.pdbx_details    '100mM Tris-HCl pH 8.5, 22% PEG4000, 200mM MgCl2' 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_diffrn.id                     1 
_diffrn.crystal_id             1 
_diffrn.ambient_temp           100 
_diffrn.ambient_temp_details   ? 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               PIXEL 
_diffrn_detector.type                   'DECTRIS EIGER X 16M' 
_diffrn_detector.pdbx_collection_date   2024-01-13 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.pdbx_scattering_type             x-ray 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.monochromator                    Si111 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.97919 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.pdbx_synchrotron_beamline   BL10U2 
_diffrn_source.type                        'SSRF BEAMLINE BL10U2' 
_diffrn_source.pdbx_wavelength_list        0.97919 
_diffrn_source.pdbx_synchrotron_site       SSRF 
_diffrn_source.pdbx_wavelength             ? 
# 
_reflns.entry_id                     7HBX 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             66.110 
_reflns.d_resolution_high            2.250 
_reflns.number_obs                   14788 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         97.800 
_reflns.pdbx_Rmerge_I_obs            0.111 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        15.400 
_reflns.B_iso_Wilson_estimate        ? 
_reflns.pdbx_redundancy              12.600 
_reflns.pdbx_Rrim_I_all              0.115 
_reflns.pdbx_Rpim_I_all              0.033 
_reflns.pdbx_CC_half                 0.998 
_reflns.pdbx_netI_over_av_sigmaI     ? 
_reflns.pdbx_number_measured_all     186424 
_reflns.pdbx_scaling_rejects         41 
_reflns.pdbx_chi_squared             ? 
_reflns.Rmerge_F_all                 ? 
_reflns.Rmerge_F_obs                 ? 
_reflns.observed_criterion_F_max     ? 
_reflns.observed_criterion_F_min     ? 
_reflns.observed_criterion_I_max     ? 
_reflns.observed_criterion_I_min     ? 
_reflns.pdbx_d_res_high_opt          ? 
_reflns.pdbx_d_res_low_opt           ? 
_reflns.details                      ? 
_reflns.pdbx_CC_star                 ? 
# 
loop_
_reflns_shell.pdbx_diffrn_id 
_reflns_shell.pdbx_ordinal 
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_reflns_shell.number_measured_obs 
_reflns_shell.number_measured_all 
_reflns_shell.number_unique_obs 
_reflns_shell.pdbx_rejects 
_reflns_shell.Rmerge_I_obs 
_reflns_shell.meanI_over_sigI_obs 
_reflns_shell.pdbx_Rsym_value 
_reflns_shell.pdbx_chi_squared 
_reflns_shell.pdbx_redundancy 
_reflns_shell.percent_possible_obs 
_reflns_shell.pdbx_netI_over_sigmaI_obs 
_reflns_shell.number_possible 
_reflns_shell.number_unique_all 
_reflns_shell.Rmerge_F_all 
_reflns_shell.Rmerge_F_obs 
_reflns_shell.Rmerge_I_all 
_reflns_shell.meanI_over_sigI_all 
_reflns_shell.percent_possible_all 
_reflns_shell.pdbx_Rrim_I_all 
_reflns_shell.pdbx_Rpim_I_all 
_reflns_shell.pdbx_CC_half 
_reflns_shell.pdbx_CC_star 
1 1 2.250  2.310  ? 9778 803 ? 1.839 ? ? ? 12.200 ? 1.300  ? ? ? ? ? ? 73.700 1.920 0.547 0.901 ? 
1 2 10.060 66.110 ? 1495 194 ? 0.045 ? ? ? 7.700  ? 34.000 ? ? ? ? ? ? 96.000 0.049 0.017 0.998 ? 
# 
_refine.entry_id                                 7HBX 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.ls_percent_reflns_R_free                 4.93 
_refine.pdbx_overall_phase_error                 32.4620 
_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                          0.2065 
_refine.B_iso_mean                               60.35 
_refine.ls_number_reflns_R_free                  726 
_refine.ls_percent_reflns_obs                    97.41 
_refine.ls_R_factor_R_work                       0.2039 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_refine.ls_d_res_high                            2.25 
_refine.ls_number_reflns_obs                     14726 
_refine.pdbx_ls_sigma_F                          1.35 
_refine.ls_number_reflns_R_work                  14000 
_refine.ls_d_res_low                             33.05 
_refine.pdbx_stereochemistry_target_values       'GeoStd + Monomer Library + CDL v1.2' 
_refine.ls_R_factor_R_free                       0.2556 
_refine.overall_SU_ML                            0.3250 
_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         14 
_refine_hist.number_atoms_solvent             54 
_refine_hist.number_atoms_total               1712 
_refine_hist.d_res_high                       2.25 
_refine_hist.d_res_low                        33.05 
# 
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           1685 0.0029 ? ? ? 
'X-RAY DIFFRACTION' f_angle_d          2271 0.5445 ? ? ? 
'X-RAY DIFFRACTION' f_chiral_restr     259  0.0412 ? ? ? 
'X-RAY DIFFRACTION' f_plane_restr      289  0.0029 ? ? ? 
'X-RAY DIFFRACTION' f_dihedral_angle_d 224  4.8982 ? ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.R_factor_R_free 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.number_reflns_obs 
'X-RAY DIFFRACTION' 2.25 2.42  2529 0.3545 88.77 0.4012 118 . . . . . . . 
'X-RAY DIFFRACTION' 2.42 2.67  2813 0.2760 99.70 0.2724 147 . . . . . . . 
'X-RAY DIFFRACTION' 2.67 3.05  2832 0.2442 99.83 0.2806 150 . . . . . . . 
'X-RAY DIFFRACTION' 3.05 3.85  2832 0.2144 99.24 0.2973 168 . . . . . . . 
'X-RAY DIFFRACTION' 3.85 33.05 2994 0.1595 99.40 0.2024 143 . . . . . . . 
# 
_struct.entry_id                  7HBX 
_struct.title                     'PanDDA analysis group deposition -- Crystal structure of HSP90N in complex with AS-5591' 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_details        ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HBX 
_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              7HBX 
_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 7HBX MET A 1   ? UNP P07900 ? ? 'initiating methionine' 8   1 
1 7HBX LEU A 230 ? UNP P07900 ? ? 'expression tag'        237 2 
1 7HBX GLU A 231 ? UNP P07900 ? ? 'expression tag'        238 3 
1 7HBX HIS A 232 ? UNP P07900 ? ? 'expression tag'        239 4 
1 7HBX HIS A 233 ? UNP P07900 ? ? 'expression tag'        240 5 
1 7HBX HIS A 234 ? UNP P07900 ? ? 'expression tag'        241 6 
1 7HBX HIS A 235 ? UNP P07900 ? ? 'expression tag'        242 7 
1 7HBX HIS A 236 ? UNP P07900 ? ? 'expression tag'        243 8 
1 7HBX HIS A 237 ? UNP P07900 ? ? 'expression tag'        244 9 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 AA1 GLN A 16  ? THR A 29  ? GLN A 23  THR A 36  1 ? 14 
HELX_P HELX_P2 AA2 GLU A 35  ? ASP A 59  ? GLU A 42  ASP A 66  1 ? 25 
HELX_P HELX_P3 AA3 PRO A 60  ? ASP A 64  ? PRO A 67  ASP A 71  5 ? 5  
HELX_P HELX_P4 AA4 THR A 92  ? ASN A 98  ? THR A 99  ASN A 105 1 ? 7  
HELX_P HELX_P5 AA5 ASN A 98  ? ALA A 117 ? ASN A 105 ALA A 124 1 ? 20 
HELX_P HELX_P6 AA6 ASP A 120 ? GLY A 128 ? ASP A 127 GLY A 135 5 ? 9  
HELX_P HELX_P7 AA7 VAL A 129 ? LEU A 136 ? VAL A 136 LEU A 143 5 ? 8  
HELX_P HELX_P8 AA8 GLN A 187 ? LEU A 191 ? GLN A 194 LEU A 198 5 ? 5  
HELX_P HELX_P9 AA9 GLU A 192 ? SER A 204 ? GLU A 199 SER A 211 1 ? 13 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
_struct_sheet.id               AA1 
_struct_sheet.type             ? 
_struct_sheet.number_strands   8 
_struct_sheet.details          ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA1 5 6 ? anti-parallel 
AA1 6 7 ? anti-parallel 
AA1 7 8 ? parallel      
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 VAL A 10  ? ALA A 14  ? VAL A 17  ALA A 21  
AA1 2 SER A 162 ? THR A 167 ? SER A 169 THR A 174 
AA1 3 GLN A 152 ? SER A 157 ? GLN A 159 SER A 164 
AA1 4 ALA A 138 ? LYS A 146 ? ALA A 145 LYS A 153 
AA1 5 GLY A 176 ? LEU A 183 ? GLY A 183 LEU A 190 
AA1 6 THR A 81  ? ASP A 86  ? THR A 88  ASP A 93  
AA1 7 ILE A 71  ? ASN A 76  ? ILE A 78  ASN A 83  
AA1 8 ILE A 211 ? LEU A 213 ? ILE A 218 LEU A 220 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N PHE A 13  ? N PHE A 20  O PHE A 163 ? O PHE A 170 
AA1 2 3 O ARG A 166 ? O ARG A 173 N ALA A 154 ? N ALA A 161 
AA1 3 4 O TRP A 155 ? O TRP A 162 N VAL A 143 ? N VAL A 150 
AA1 4 5 N THR A 142 ? N THR A 149 O ILE A 180 ? O ILE A 187 
AA1 5 6 O LEU A 181 ? O LEU A 188 N LEU A 82  ? N LEU A 89  
AA1 6 7 O 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                   7HBX 
_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 OE1 A GLU 199 ? ? O A HOH 401 ? ? 1.96 
2 1 O   A LYS 224 ? ? O A HOH 402 ? ? 2.19 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ASP A 66  ? ? -150.93 89.11   
2 1 ASN A 105 ? ? -123.91 -51.26  
3 1 ALA A 124 ? ? -89.41  32.73   
4 1 ALA A 166 ? ? 60.67   -143.18 
5 1 PHE A 213 ? ? -117.00 52.61   
# 
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 14.0191573937  27.6423025769 31.4555401834 0.507601272274 0.53786867676  0.603699376609 
-0.00946611005358 -0.140486347896  0.0396093243682   4.11041811327 2.52190168817 5.40678876494 -1.4120850619   -2.30055758249  
1.04695099654  -0.0684490516214 -0.388883098243  -0.105766055728  0.314898377129    -0.0818523413641 -0.198448824746  
-0.0853690211256 0.373778631275   0.132713820071  
2 ? 'X-RAY DIFFRACTION' refined -4.74907392235 32.6186015963 23.976396186  0.391700054958 0.342338378835 0.393451497201 
-0.0127255710156  -0.0675494078229 -0.0222220777744  2.33670696591 4.03864505299 2.29094286535 -0.547559843779 -0.391422371709 
-1.70467648259 0.0315119578639  -0.0514341989608 -0.0604542809817 0.109547580047    0.0782506994134  0.145891072815   
0.0393536260998  -0.0914680127514 -0.122983152255 
3 ? 'X-RAY DIFFRACTION' refined 12.3141622882  39.5793240461 34.5667511925 0.628069653373 0.692270172682 0.752905107308 
-0.0785534389617  -0.186248549767  -0.0780227958609  2.7392280928  8.00950381813 2.66710927135 0.614745560549  -2.22612168137  
-2.67520608481 0.05504202021    -0.949775124972  0.706044290664   1.20577291032     -0.201331774042  -0.736144671646  
-0.642769150922  0.801282555802   0.135203011755  
4 ? 'X-RAY DIFFRACTION' refined 0.500813043596 24.9385023707 28.1045881158 0.349669038749 0.306153018677 0.456225752799 
0.00119677510381  -0.048092742288  -0.00856494499325 3.71947426009 2.99471217859 2.91385421084 -0.555487562759 -0.530603603197 
-0.58835675695 -0.120568115663  -0.192822814438  -0.409067267705  -0.00518927030601 -0.017040733811  -0.0318960339896 
0.305057290957   0.0440863328513  0.11045391877   
5 ? 'X-RAY DIFFRACTION' refined -12.9730301192 30.4506468529 32.5446081772 0.527210329926 0.575614280431 0.556721162784 
-0.00410733674734 -0.0299969380652 0.0192299570883   4.7156148525  3.83387080538 3.61848244325 -0.279109386964 -0.489665548517 
-1.97065084076 -0.144863433165  -0.464815218906  -0.101862489959  0.965153430678    0.199584986279   -0.301914154773  
-0.269153611232  -0.26163371168   -0.087599374449 
# 
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 105 A 90  . 
;chain 'A' and (resid 41 through 105 )
;
3 3 'X-RAY DIFFRACTION' A 106 A 91  A 136 A 121 . 
;chain 'A' and (resid 106 through 136 )
;
4 4 'X-RAY DIFFRACTION' A 137 A 122 A 210 A 195 . 
;chain 'A' and (resid 137 through 210 )
;
5 5 'X-RAY DIFFRACTION' A 211 A 196 A 224 A 209 . 
;chain 'A' and (resid 211 through 224 )
;
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A MET 8   ? A MET 1   
2  1 Y 1 A ASP 9   ? A ASP 2   
3  1 Y 1 A GLN 10  ? A GLN 3   
4  1 Y 1 A PRO 11  ? A PRO 4   
5  1 Y 1 A MET 12  ? A MET 5   
6  1 Y 1 A GLU 13  ? A GLU 6   
7  1 Y 1 A GLU 14  ? A GLU 7   
8  1 Y 1 A GLU 15  ? A GLU 8   
9  1 Y 1 A GLU 225 ? A GLU 218 
10 1 Y 1 A ARG 226 ? A ARG 219 
11 1 Y 1 A ASP 227 ? A ASP 220 
12 1 Y 1 A LYS 228 ? A LYS 221 
13 1 Y 1 A GLU 229 ? A GLU 222 
14 1 Y 1 A VAL 230 ? A VAL 223 
15 1 Y 1 A SER 231 ? A SER 224 
16 1 Y 1 A ASP 232 ? A ASP 225 
17 1 Y 1 A ASP 233 ? A ASP 226 
18 1 Y 1 A GLU 234 ? A GLU 227 
19 1 Y 1 A ALA 235 ? A ALA 228 
20 1 Y 1 A GLU 236 ? A GLU 229 
21 1 Y 1 A LEU 237 ? A LEU 230 
22 1 Y 1 A GLU 238 ? A GLU 231 
23 1 Y 1 A HIS 239 ? A HIS 232 
24 1 Y 1 A HIS 240 ? A HIS 233 
25 1 Y 1 A HIS 241 ? A HIS 234 
26 1 Y 1 A HIS 242 ? A HIS 235 
27 1 Y 1 A HIS 243 ? A HIS 236 
28 1 Y 1 A HIS 244 ? A HIS 237 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
A1AY7 N1   N Y N 1   
A1AY7 C2   C Y N 2   
A1AY7 C4   C Y N 3   
A1AY7 C5   C Y N 4   
A1AY7 C6   C Y N 5   
A1AY7 C3   C Y N 6   
A1AY7 C1   C N N 7   
A1AY7 C8   C Y N 8   
A1AY7 C11  C N N 9   
A1AY7 C10  C Y N 10  
A1AY7 C9   C Y N 11  
A1AY7 C7   C Y N 12  
A1AY7 O1   O Y N 13  
A1AY7 O2   O N N 14  
A1AY7 H5   H N N 15  
A1AY7 H6   H N N 16  
A1AY7 H12  H N N 17  
A1AY7 H13  H N N 18  
A1AY7 H11  H N N 19  
A1AY7 H8   H N N 20  
A1AY7 H112 H N N 21  
A1AY7 H113 H N N 22  
A1AY7 H9   H N N 23  
A1AY7 H7   H N N 24  
A1AY7 H2   H N N 25  
ALA   N    N N N 26  
ALA   CA   C N S 27  
ALA   C    C N N 28  
ALA   O    O N N 29  
ALA   CB   C N N 30  
ALA   OXT  O N N 31  
ALA   H    H N N 32  
ALA   H2   H N N 33  
ALA   HA   H N N 34  
ALA   HB1  H N N 35  
ALA   HB2  H N N 36  
ALA   HB3  H N N 37  
ALA   HXT  H N N 38  
ARG   N    N N N 39  
ARG   CA   C N S 40  
ARG   C    C N N 41  
ARG   O    O N N 42  
ARG   CB   C N N 43  
ARG   CG   C N N 44  
ARG   CD   C N N 45  
ARG   NE   N N N 46  
ARG   CZ   C N N 47  
ARG   NH1  N N N 48  
ARG   NH2  N N N 49  
ARG   OXT  O N N 50  
ARG   H    H N N 51  
ARG   H2   H N N 52  
ARG   HA   H N N 53  
ARG   HB2  H N N 54  
ARG   HB3  H N N 55  
ARG   HG2  H N N 56  
ARG   HG3  H N N 57  
ARG   HD2  H N N 58  
ARG   HD3  H N N 59  
ARG   HE   H N N 60  
ARG   HH11 H N N 61  
ARG   HH12 H N N 62  
ARG   HH21 H N N 63  
ARG   HH22 H N N 64  
ARG   HXT  H N N 65  
ASN   N    N N N 66  
ASN   CA   C N S 67  
ASN   C    C N N 68  
ASN   O    O N N 69  
ASN   CB   C N N 70  
ASN   CG   C N N 71  
ASN   OD1  O N N 72  
ASN   ND2  N N N 73  
ASN   OXT  O N N 74  
ASN   H    H N N 75  
ASN   H2   H N N 76  
ASN   HA   H N N 77  
ASN   HB2  H N N 78  
ASN   HB3  H N N 79  
ASN   HD21 H N N 80  
ASN   HD22 H N N 81  
ASN   HXT  H N N 82  
ASP   N    N N N 83  
ASP   CA   C N S 84  
ASP   C    C N N 85  
ASP   O    O N N 86  
ASP   CB   C N N 87  
ASP   CG   C N N 88  
ASP   OD1  O N N 89  
ASP   OD2  O N N 90  
ASP   OXT  O N N 91  
ASP   H    H N N 92  
ASP   H2   H N N 93  
ASP   HA   H N N 94  
ASP   HB2  H N N 95  
ASP   HB3  H N N 96  
ASP   HD2  H N N 97  
ASP   HXT  H N N 98  
GLN   N    N N N 99  
GLN   CA   C N S 100 
GLN   C    C N N 101 
GLN   O    O N N 102 
GLN   CB   C N N 103 
GLN   CG   C N N 104 
GLN   CD   C N N 105 
GLN   OE1  O N N 106 
GLN   NE2  N N N 107 
GLN   OXT  O N N 108 
GLN   H    H N N 109 
GLN   H2   H N N 110 
GLN   HA   H N N 111 
GLN   HB2  H N N 112 
GLN   HB3  H N N 113 
GLN   HG2  H N N 114 
GLN   HG3  H N N 115 
GLN   HE21 H N N 116 
GLN   HE22 H N N 117 
GLN   HXT  H N N 118 
GLU   N    N N N 119 
GLU   CA   C N S 120 
GLU   C    C N N 121 
GLU   O    O N N 122 
GLU   CB   C N N 123 
GLU   CG   C N N 124 
GLU   CD   C N N 125 
GLU   OE1  O N N 126 
GLU   OE2  O N N 127 
GLU   OXT  O N N 128 
GLU   H    H N N 129 
GLU   H2   H N N 130 
GLU   HA   H N N 131 
GLU   HB2  H N N 132 
GLU   HB3  H N N 133 
GLU   HG2  H N N 134 
GLU   HG3  H N N 135 
GLU   HE2  H N N 136 
GLU   HXT  H N N 137 
GLY   N    N N N 138 
GLY   CA   C N N 139 
GLY   C    C N N 140 
GLY   O    O N N 141 
GLY   OXT  O N N 142 
GLY   H    H N N 143 
GLY   H2   H N N 144 
GLY   HA2  H N N 145 
GLY   HA3  H N N 146 
GLY   HXT  H N N 147 
HIS   N    N N N 148 
HIS   CA   C N S 149 
HIS   C    C N N 150 
HIS   O    O N N 151 
HIS   CB   C N N 152 
HIS   CG   C Y N 153 
HIS   ND1  N Y N 154 
HIS   CD2  C Y N 155 
HIS   CE1  C Y N 156 
HIS   NE2  N Y N 157 
HIS   OXT  O N N 158 
HIS   H    H N N 159 
HIS   H2   H N N 160 
HIS   HA   H N N 161 
HIS   HB2  H N N 162 
HIS   HB3  H N N 163 
HIS   HD1  H N N 164 
HIS   HD2  H N N 165 
HIS   HE1  H N N 166 
HIS   HE2  H N N 167 
HIS   HXT  H N N 168 
HOH   O    O N N 169 
HOH   H1   H N N 170 
HOH   H2   H N N 171 
ILE   N    N N N 172 
ILE   CA   C N S 173 
ILE   C    C N N 174 
ILE   O    O N N 175 
ILE   CB   C N S 176 
ILE   CG1  C N N 177 
ILE   CG2  C N N 178 
ILE   CD1  C N N 179 
ILE   OXT  O N N 180 
ILE   H    H N N 181 
ILE   H2   H N N 182 
ILE   HA   H N N 183 
ILE   HB   H N N 184 
ILE   HG12 H N N 185 
ILE   HG13 H N N 186 
ILE   HG21 H N N 187 
ILE   HG22 H N N 188 
ILE   HG23 H N N 189 
ILE   HD11 H N N 190 
ILE   HD12 H N N 191 
ILE   HD13 H N N 192 
ILE   HXT  H N N 193 
LEU   N    N N N 194 
LEU   CA   C N S 195 
LEU   C    C N N 196 
LEU   O    O N N 197 
LEU   CB   C N N 198 
LEU   CG   C N N 199 
LEU   CD1  C N N 200 
LEU   CD2  C N N 201 
LEU   OXT  O N N 202 
LEU   H    H N N 203 
LEU   H2   H N N 204 
LEU   HA   H N N 205 
LEU   HB2  H N N 206 
LEU   HB3  H N N 207 
LEU   HG   H N N 208 
LEU   HD11 H N N 209 
LEU   HD12 H N N 210 
LEU   HD13 H N N 211 
LEU   HD21 H N N 212 
LEU   HD22 H N N 213 
LEU   HD23 H N N 214 
LEU   HXT  H N N 215 
LYS   N    N N N 216 
LYS   CA   C N S 217 
LYS   C    C N N 218 
LYS   O    O N N 219 
LYS   CB   C N N 220 
LYS   CG   C N N 221 
LYS   CD   C N N 222 
LYS   CE   C N N 223 
LYS   NZ   N N N 224 
LYS   OXT  O N N 225 
LYS   H    H N N 226 
LYS   H2   H N N 227 
LYS   HA   H N N 228 
LYS   HB2  H N N 229 
LYS   HB3  H N N 230 
LYS   HG2  H N N 231 
LYS   HG3  H N N 232 
LYS   HD2  H N N 233 
LYS   HD3  H N N 234 
LYS   HE2  H N N 235 
LYS   HE3  H N N 236 
LYS   HZ1  H N N 237 
LYS   HZ2  H N N 238 
LYS   HZ3  H N N 239 
LYS   HXT  H N N 240 
MET   N    N N N 241 
MET   CA   C N S 242 
MET   C    C N N 243 
MET   O    O N N 244 
MET   CB   C N N 245 
MET   CG   C N N 246 
MET   SD   S N N 247 
MET   CE   C N N 248 
MET   OXT  O N N 249 
MET   H    H N N 250 
MET   H2   H N N 251 
MET   HA   H N N 252 
MET   HB2  H N N 253 
MET   HB3  H N N 254 
MET   HG2  H N N 255 
MET   HG3  H N N 256 
MET   HE1  H N N 257 
MET   HE2  H N N 258 
MET   HE3  H N N 259 
MET   HXT  H N N 260 
PHE   N    N N N 261 
PHE   CA   C N S 262 
PHE   C    C N N 263 
PHE   O    O N N 264 
PHE   CB   C N N 265 
PHE   CG   C Y N 266 
PHE   CD1  C Y N 267 
PHE   CD2  C Y N 268 
PHE   CE1  C Y N 269 
PHE   CE2  C Y N 270 
PHE   CZ   C Y N 271 
PHE   OXT  O N N 272 
PHE   H    H N N 273 
PHE   H2   H N N 274 
PHE   HA   H N N 275 
PHE   HB2  H N N 276 
PHE   HB3  H N N 277 
PHE   HD1  H N N 278 
PHE   HD2  H N N 279 
PHE   HE1  H N N 280 
PHE   HE2  H N N 281 
PHE   HZ   H N N 282 
PHE   HXT  H N N 283 
PRO   N    N N N 284 
PRO   CA   C N S 285 
PRO   C    C N N 286 
PRO   O    O N N 287 
PRO   CB   C N N 288 
PRO   CG   C N N 289 
PRO   CD   C N N 290 
PRO   OXT  O N N 291 
PRO   H    H N N 292 
PRO   HA   H N N 293 
PRO   HB2  H N N 294 
PRO   HB3  H N N 295 
PRO   HG2  H N N 296 
PRO   HG3  H N N 297 
PRO   HD2  H N N 298 
PRO   HD3  H N N 299 
PRO   HXT  H N N 300 
SER   N    N N N 301 
SER   CA   C N S 302 
SER   C    C N N 303 
SER   O    O N N 304 
SER   CB   C N N 305 
SER   OG   O N N 306 
SER   OXT  O N N 307 
SER   H    H N N 308 
SER   H2   H N N 309 
SER   HA   H N N 310 
SER   HB2  H N N 311 
SER   HB3  H N N 312 
SER   HG   H N N 313 
SER   HXT  H N N 314 
THR   N    N N N 315 
THR   CA   C N S 316 
THR   C    C N N 317 
THR   O    O N N 318 
THR   CB   C N R 319 
THR   OG1  O N N 320 
THR   CG2  C N N 321 
THR   OXT  O N N 322 
THR   H    H N N 323 
THR   H2   H N N 324 
THR   HA   H N N 325 
THR   HB   H N N 326 
THR   HG1  H N N 327 
THR   HG21 H N N 328 
THR   HG22 H N N 329 
THR   HG23 H N N 330 
THR   HXT  H N N 331 
TRP   N    N N N 332 
TRP   CA   C N S 333 
TRP   C    C N N 334 
TRP   O    O N N 335 
TRP   CB   C N N 336 
TRP   CG   C Y N 337 
TRP   CD1  C Y N 338 
TRP   CD2  C Y N 339 
TRP   NE1  N Y N 340 
TRP   CE2  C Y N 341 
TRP   CE3  C Y N 342 
TRP   CZ2  C Y N 343 
TRP   CZ3  C Y N 344 
TRP   CH2  C Y N 345 
TRP   OXT  O N N 346 
TRP   H    H N N 347 
TRP   H2   H N N 348 
TRP   HA   H N N 349 
TRP   HB2  H N N 350 
TRP   HB3  H N N 351 
TRP   HD1  H N N 352 
TRP   HE1  H N N 353 
TRP   HE3  H N N 354 
TRP   HZ2  H N N 355 
TRP   HZ3  H N N 356 
TRP   HH2  H N N 357 
TRP   HXT  H N N 358 
TYR   N    N N N 359 
TYR   CA   C N S 360 
TYR   C    C N N 361 
TYR   O    O N N 362 
TYR   CB   C N N 363 
TYR   CG   C Y N 364 
TYR   CD1  C Y N 365 
TYR   CD2  C Y N 366 
TYR   CE1  C Y N 367 
TYR   CE2  C Y N 368 
TYR   CZ   C Y N 369 
TYR   OH   O N N 370 
TYR   OXT  O N N 371 
TYR   H    H N N 372 
TYR   H2   H N N 373 
TYR   HA   H N N 374 
TYR   HB2  H N N 375 
TYR   HB3  H N N 376 
TYR   HD1  H N N 377 
TYR   HD2  H N N 378 
TYR   HE1  H N N 379 
TYR   HE2  H N N 380 
TYR   HH   H N N 381 
TYR   HXT  H N N 382 
VAL   N    N N N 383 
VAL   CA   C N S 384 
VAL   C    C N N 385 
VAL   O    O N N 386 
VAL   CB   C N N 387 
VAL   CG1  C N N 388 
VAL   CG2  C N N 389 
VAL   OXT  O N N 390 
VAL   H    H N N 391 
VAL   H2   H N N 392 
VAL   HA   H N N 393 
VAL   HB   H N N 394 
VAL   HG11 H N N 395 
VAL   HG12 H N N 396 
VAL   HG13 H N N 397 
VAL   HG21 H N N 398 
VAL   HG22 H N N 399 
VAL   HG23 H N N 400 
VAL   HXT  H N N 401 
# 
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 
A1AY7 C1  C2   sing N N 1   
A1AY7 C2  N1   doub Y N 2   
A1AY7 C2  C10  sing Y N 3   
A1AY7 N1  O1   sing Y N 4   
A1AY7 O1  C3   sing Y N 5   
A1AY7 C3  C4   sing N N 6   
A1AY7 C3  C10  doub Y N 7   
A1AY7 C4  C5   doub Y N 8   
A1AY7 C4  C9   sing Y N 9   
A1AY7 C5  C6   sing Y N 10  
A1AY7 C6  C7   doub Y N 11  
A1AY7 C7  C8   sing Y N 12  
A1AY7 C8  C9   doub Y N 13  
A1AY7 C10 C11  sing N N 14  
A1AY7 C11 O2   sing N N 15  
A1AY7 C5  H5   sing N N 16  
A1AY7 C6  H6   sing N N 17  
A1AY7 C1  H12  sing N N 18  
A1AY7 C1  H13  sing N N 19  
A1AY7 C1  H11  sing N N 20  
A1AY7 C8  H8   sing N N 21  
A1AY7 C11 H112 sing N N 22  
A1AY7 C11 H113 sing N N 23  
A1AY7 C9  H9   sing N N 24  
A1AY7 C7  H7   sing N N 25  
A1AY7 O2  H2   sing N N 26  
ALA   N   CA   sing N N 27  
ALA   N   H    sing N N 28  
ALA   N   H2   sing N N 29  
ALA   CA  C    sing N N 30  
ALA   CA  CB   sing N N 31  
ALA   CA  HA   sing N N 32  
ALA   C   O    doub N N 33  
ALA   C   OXT  sing N N 34  
ALA   CB  HB1  sing N N 35  
ALA   CB  HB2  sing N N 36  
ALA   CB  HB3  sing N N 37  
ALA   OXT HXT  sing N N 38  
ARG   N   CA   sing N N 39  
ARG   N   H    sing N N 40  
ARG   N   H2   sing N N 41  
ARG   CA  C    sing N N 42  
ARG   CA  CB   sing N N 43  
ARG   CA  HA   sing N N 44  
ARG   C   O    doub N N 45  
ARG   C   OXT  sing N N 46  
ARG   CB  CG   sing N N 47  
ARG   CB  HB2  sing N N 48  
ARG   CB  HB3  sing N N 49  
ARG   CG  CD   sing N N 50  
ARG   CG  HG2  sing N N 51  
ARG   CG  HG3  sing N N 52  
ARG   CD  NE   sing N N 53  
ARG   CD  HD2  sing N N 54  
ARG   CD  HD3  sing N N 55  
ARG   NE  CZ   sing N N 56  
ARG   NE  HE   sing N N 57  
ARG   CZ  NH1  sing N N 58  
ARG   CZ  NH2  doub N N 59  
ARG   NH1 HH11 sing N N 60  
ARG   NH1 HH12 sing N N 61  
ARG   NH2 HH21 sing N N 62  
ARG   NH2 HH22 sing N N 63  
ARG   OXT HXT  sing N N 64  
ASN   N   CA   sing N N 65  
ASN   N   H    sing N N 66  
ASN   N   H2   sing N N 67  
ASN   CA  C    sing N N 68  
ASN   CA  CB   sing N N 69  
ASN   CA  HA   sing N N 70  
ASN   C   O    doub N N 71  
ASN   C   OXT  sing N N 72  
ASN   CB  CG   sing N N 73  
ASN   CB  HB2  sing N N 74  
ASN   CB  HB3  sing N N 75  
ASN   CG  OD1  doub N N 76  
ASN   CG  ND2  sing N N 77  
ASN   ND2 HD21 sing N N 78  
ASN   ND2 HD22 sing N N 79  
ASN   OXT HXT  sing N N 80  
ASP   N   CA   sing N N 81  
ASP   N   H    sing N N 82  
ASP   N   H2   sing N N 83  
ASP   CA  C    sing N N 84  
ASP   CA  CB   sing N N 85  
ASP   CA  HA   sing N N 86  
ASP   C   O    doub N N 87  
ASP   C   OXT  sing N N 88  
ASP   CB  CG   sing N N 89  
ASP   CB  HB2  sing N N 90  
ASP   CB  HB3  sing N N 91  
ASP   CG  OD1  doub N N 92  
ASP   CG  OD2  sing N N 93  
ASP   OD2 HD2  sing N N 94  
ASP   OXT HXT  sing N N 95  
GLN   N   CA   sing N N 96  
GLN   N   H    sing N N 97  
GLN   N   H2   sing N N 98  
GLN   CA  C    sing N N 99  
GLN   CA  CB   sing N N 100 
GLN   CA  HA   sing N N 101 
GLN   C   O    doub N N 102 
GLN   C   OXT  sing N N 103 
GLN   CB  CG   sing N N 104 
GLN   CB  HB2  sing N N 105 
GLN   CB  HB3  sing N N 106 
GLN   CG  CD   sing N N 107 
GLN   CG  HG2  sing N N 108 
GLN   CG  HG3  sing N N 109 
GLN   CD  OE1  doub N N 110 
GLN   CD  NE2  sing N N 111 
GLN   NE2 HE21 sing N N 112 
GLN   NE2 HE22 sing N N 113 
GLN   OXT HXT  sing N N 114 
GLU   N   CA   sing N N 115 
GLU   N   H    sing N N 116 
GLU   N   H2   sing N N 117 
GLU   CA  C    sing N N 118 
GLU   CA  CB   sing N N 119 
GLU   CA  HA   sing N N 120 
GLU   C   O    doub N N 121 
GLU   C   OXT  sing N N 122 
GLU   CB  CG   sing N N 123 
GLU   CB  HB2  sing N N 124 
GLU   CB  HB3  sing N N 125 
GLU   CG  CD   sing N N 126 
GLU   CG  HG2  sing N N 127 
GLU   CG  HG3  sing N N 128 
GLU   CD  OE1  doub N N 129 
GLU   CD  OE2  sing N N 130 
GLU   OE2 HE2  sing N N 131 
GLU   OXT HXT  sing N N 132 
GLY   N   CA   sing N N 133 
GLY   N   H    sing N N 134 
GLY   N   H2   sing N N 135 
GLY   CA  C    sing N N 136 
GLY   CA  HA2  sing N N 137 
GLY   CA  HA3  sing N N 138 
GLY   C   O    doub N N 139 
GLY   C   OXT  sing N N 140 
GLY   OXT HXT  sing N N 141 
HIS   N   CA   sing N N 142 
HIS   N   H    sing N N 143 
HIS   N   H2   sing N N 144 
HIS   CA  C    sing N N 145 
HIS   CA  CB   sing N N 146 
HIS   CA  HA   sing N N 147 
HIS   C   O    doub N N 148 
HIS   C   OXT  sing N N 149 
HIS   CB  CG   sing N N 150 
HIS   CB  HB2  sing N N 151 
HIS   CB  HB3  sing N N 152 
HIS   CG  ND1  sing Y N 153 
HIS   CG  CD2  doub Y N 154 
HIS   ND1 CE1  doub Y N 155 
HIS   ND1 HD1  sing N N 156 
HIS   CD2 NE2  sing Y N 157 
HIS   CD2 HD2  sing N N 158 
HIS   CE1 NE2  sing Y N 159 
HIS   CE1 HE1  sing N N 160 
HIS   NE2 HE2  sing N N 161 
HIS   OXT HXT  sing N N 162 
HOH   O   H1   sing N N 163 
HOH   O   H2   sing N N 164 
ILE   N   CA   sing N N 165 
ILE   N   H    sing N N 166 
ILE   N   H2   sing N N 167 
ILE   CA  C    sing N N 168 
ILE   CA  CB   sing N N 169 
ILE   CA  HA   sing N N 170 
ILE   C   O    doub N N 171 
ILE   C   OXT  sing N N 172 
ILE   CB  CG1  sing N N 173 
ILE   CB  CG2  sing N N 174 
ILE   CB  HB   sing N N 175 
ILE   CG1 CD1  sing N N 176 
ILE   CG1 HG12 sing N N 177 
ILE   CG1 HG13 sing N N 178 
ILE   CG2 HG21 sing N N 179 
ILE   CG2 HG22 sing N N 180 
ILE   CG2 HG23 sing N N 181 
ILE   CD1 HD11 sing N N 182 
ILE   CD1 HD12 sing N N 183 
ILE   CD1 HD13 sing N N 184 
ILE   OXT HXT  sing N N 185 
LEU   N   CA   sing N N 186 
LEU   N   H    sing N N 187 
LEU   N   H2   sing N N 188 
LEU   CA  C    sing N N 189 
LEU   CA  CB   sing N N 190 
LEU   CA  HA   sing N N 191 
LEU   C   O    doub N N 192 
LEU   C   OXT  sing N N 193 
LEU   CB  CG   sing N N 194 
LEU   CB  HB2  sing N N 195 
LEU   CB  HB3  sing N N 196 
LEU   CG  CD1  sing N N 197 
LEU   CG  CD2  sing N N 198 
LEU   CG  HG   sing N N 199 
LEU   CD1 HD11 sing N N 200 
LEU   CD1 HD12 sing N N 201 
LEU   CD1 HD13 sing N N 202 
LEU   CD2 HD21 sing N N 203 
LEU   CD2 HD22 sing N N 204 
LEU   CD2 HD23 sing N N 205 
LEU   OXT HXT  sing N N 206 
LYS   N   CA   sing N N 207 
LYS   N   H    sing N N 208 
LYS   N   H2   sing N N 209 
LYS   CA  C    sing N N 210 
LYS   CA  CB   sing N N 211 
LYS   CA  HA   sing N N 212 
LYS   C   O    doub N N 213 
LYS   C   OXT  sing N N 214 
LYS   CB  CG   sing N N 215 
LYS   CB  HB2  sing N N 216 
LYS   CB  HB3  sing N N 217 
LYS   CG  CD   sing N N 218 
LYS   CG  HG2  sing N N 219 
LYS   CG  HG3  sing N N 220 
LYS   CD  CE   sing N N 221 
LYS   CD  HD2  sing N N 222 
LYS   CD  HD3  sing N N 223 
LYS   CE  NZ   sing N N 224 
LYS   CE  HE2  sing N N 225 
LYS   CE  HE3  sing N N 226 
LYS   NZ  HZ1  sing N N 227 
LYS   NZ  HZ2  sing N N 228 
LYS   NZ  HZ3  sing N N 229 
LYS   OXT HXT  sing N N 230 
MET   N   CA   sing N N 231 
MET   N   H    sing N N 232 
MET   N   H2   sing N N 233 
MET   CA  C    sing N N 234 
MET   CA  CB   sing N N 235 
MET   CA  HA   sing N N 236 
MET   C   O    doub N N 237 
MET   C   OXT  sing N N 238 
MET   CB  CG   sing N N 239 
MET   CB  HB2  sing N N 240 
MET   CB  HB3  sing N N 241 
MET   CG  SD   sing N N 242 
MET   CG  HG2  sing N N 243 
MET   CG  HG3  sing N N 244 
MET   SD  CE   sing N N 245 
MET   CE  HE1  sing N N 246 
MET   CE  HE2  sing N N 247 
MET   CE  HE3  sing N N 248 
MET   OXT HXT  sing N N 249 
PHE   N   CA   sing N N 250 
PHE   N   H    sing N N 251 
PHE   N   H2   sing N N 252 
PHE   CA  C    sing N N 253 
PHE   CA  CB   sing N N 254 
PHE   CA  HA   sing N N 255 
PHE   C   O    doub N N 256 
PHE   C   OXT  sing N N 257 
PHE   CB  CG   sing N N 258 
PHE   CB  HB2  sing N N 259 
PHE   CB  HB3  sing N N 260 
PHE   CG  CD1  doub Y N 261 
PHE   CG  CD2  sing Y N 262 
PHE   CD1 CE1  sing Y N 263 
PHE   CD1 HD1  sing N N 264 
PHE   CD2 CE2  doub Y N 265 
PHE   CD2 HD2  sing N N 266 
PHE   CE1 CZ   doub Y N 267 
PHE   CE1 HE1  sing N N 268 
PHE   CE2 CZ   sing Y N 269 
PHE   CE2 HE2  sing N N 270 
PHE   CZ  HZ   sing N N 271 
PHE   OXT HXT  sing N N 272 
PRO   N   CA   sing N N 273 
PRO   N   CD   sing N N 274 
PRO   N   H    sing N N 275 
PRO   CA  C    sing N N 276 
PRO   CA  CB   sing N N 277 
PRO   CA  HA   sing N N 278 
PRO   C   O    doub N N 279 
PRO   C   OXT  sing N N 280 
PRO   CB  CG   sing N N 281 
PRO   CB  HB2  sing N N 282 
PRO   CB  HB3  sing N N 283 
PRO   CG  CD   sing N N 284 
PRO   CG  HG2  sing N N 285 
PRO   CG  HG3  sing N N 286 
PRO   CD  HD2  sing N N 287 
PRO   CD  HD3  sing N N 288 
PRO   OXT HXT  sing N N 289 
SER   N   CA   sing N N 290 
SER   N   H    sing N N 291 
SER   N   H2   sing N N 292 
SER   CA  C    sing N N 293 
SER   CA  CB   sing N N 294 
SER   CA  HA   sing N N 295 
SER   C   O    doub N N 296 
SER   C   OXT  sing N N 297 
SER   CB  OG   sing N N 298 
SER   CB  HB2  sing N N 299 
SER   CB  HB3  sing N N 300 
SER   OG  HG   sing N N 301 
SER   OXT HXT  sing N N 302 
THR   N   CA   sing N N 303 
THR   N   H    sing N N 304 
THR   N   H2   sing N N 305 
THR   CA  C    sing N N 306 
THR   CA  CB   sing N N 307 
THR   CA  HA   sing N N 308 
THR   C   O    doub N N 309 
THR   C   OXT  sing N N 310 
THR   CB  OG1  sing N N 311 
THR   CB  CG2  sing N N 312 
THR   CB  HB   sing N N 313 
THR   OG1 HG1  sing N N 314 
THR   CG2 HG21 sing N N 315 
THR   CG2 HG22 sing N N 316 
THR   CG2 HG23 sing N N 317 
THR   OXT HXT  sing N N 318 
TRP   N   CA   sing N N 319 
TRP   N   H    sing N N 320 
TRP   N   H2   sing N N 321 
TRP   CA  C    sing N N 322 
TRP   CA  CB   sing N N 323 
TRP   CA  HA   sing N N 324 
TRP   C   O    doub N N 325 
TRP   C   OXT  sing N N 326 
TRP   CB  CG   sing N N 327 
TRP   CB  HB2  sing N N 328 
TRP   CB  HB3  sing N N 329 
TRP   CG  CD1  doub Y N 330 
TRP   CG  CD2  sing Y N 331 
TRP   CD1 NE1  sing Y N 332 
TRP   CD1 HD1  sing N N 333 
TRP   CD2 CE2  doub Y N 334 
TRP   CD2 CE3  sing Y N 335 
TRP   NE1 CE2  sing Y N 336 
TRP   NE1 HE1  sing N N 337 
TRP   CE2 CZ2  sing Y N 338 
TRP   CE3 CZ3  doub Y N 339 
TRP   CE3 HE3  sing N N 340 
TRP   CZ2 CH2  doub Y N 341 
TRP   CZ2 HZ2  sing N N 342 
TRP   CZ3 CH2  sing Y N 343 
TRP   CZ3 HZ3  sing N N 344 
TRP   CH2 HH2  sing N N 345 
TRP   OXT HXT  sing N N 346 
TYR   N   CA   sing N N 347 
TYR   N   H    sing N N 348 
TYR   N   H2   sing N N 349 
TYR   CA  C    sing N N 350 
TYR   CA  CB   sing N N 351 
TYR   CA  HA   sing N N 352 
TYR   C   O    doub N N 353 
TYR   C   OXT  sing N N 354 
TYR   CB  CG   sing N N 355 
TYR   CB  HB2  sing N N 356 
TYR   CB  HB3  sing N N 357 
TYR   CG  CD1  doub Y N 358 
TYR   CG  CD2  sing Y N 359 
TYR   CD1 CE1  sing Y N 360 
TYR   CD1 HD1  sing N N 361 
TYR   CD2 CE2  doub Y N 362 
TYR   CD2 HD2  sing N N 363 
TYR   CE1 CZ   doub Y N 364 
TYR   CE1 HE1  sing N N 365 
TYR   CE2 CZ   sing Y N 366 
TYR   CE2 HE2  sing N N 367 
TYR   CZ  OH   sing N N 368 
TYR   OH  HH   sing N N 369 
TYR   OXT HXT  sing N N 370 
VAL   N   CA   sing N N 371 
VAL   N   H    sing N N 372 
VAL   N   H2   sing N N 373 
VAL   CA  C    sing N N 374 
VAL   CA  CB   sing N N 375 
VAL   CA  HA   sing N N 376 
VAL   C   O    doub N N 377 
VAL   C   OXT  sing N N 378 
VAL   CB  CG1  sing N N 379 
VAL   CB  CG2  sing N N 380 
VAL   CB  HB   sing N N 381 
VAL   CG1 HG11 sing N N 382 
VAL   CG1 HG12 sing N N 383 
VAL   CG1 HG13 sing N N 384 
VAL   CG2 HG21 sing N N 385 
VAL   CG2 HG22 sing N N 386 
VAL   CG2 HG23 sing N N 387 
VAL   OXT HXT  sing N N 388 
# 
_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                    7HBX 
_atom_sites.fract_transf_matrix[1][1]   0.014140 
_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]   0.011158 
_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]   0.010213 
_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   ? 9.08847   16.31792 10.79024 1.000 78.42321  ? 16  GLU   A N   1 
ATOM   2    C CA  . GLU   A 1 9   ? 10.40183  16.93935 10.91706 1.000 83.22786  ? 16  GLU   A CA  1 
ATOM   3    C C   . GLU   A 1 9   ? 10.43654  17.92462 12.08128 1.000 85.52604  ? 16  GLU   A C   1 
ATOM   4    O O   . GLU   A 1 9   ? 9.64104   18.86349 12.13442 1.000 81.99972  ? 16  GLU   A O   1 
ATOM   5    C CB  . GLU   A 1 9   ? 10.78843  17.64945 9.61811  1.000 90.71999  ? 16  GLU   A CB  1 
ATOM   6    C CG  . GLU   A 1 9   ? 12.28512  17.91037 9.46606  1.000 94.11560  ? 16  GLU   A CG  1 
ATOM   7    C CD  . GLU   A 1 9   ? 13.07015  16.69113 8.99723  1.000 109.94154 ? 16  GLU   A CD  1 
ATOM   8    O OE1 . GLU   A 1 9   ? 12.76821  15.55944 9.43608  1.000 103.46893 ? 16  GLU   A OE1 1 
ATOM   9    O OE2 . GLU   A 1 9   ? 14.00085  16.86758 8.18147  1.000 113.99384 ? 16  GLU   A OE2 1 
ATOM   10   N N   . VAL   A 1 10  ? 11.37087  17.71219 13.00647 1.000 78.10566  ? 17  VAL   A N   1 
ATOM   11   C CA  . VAL   A 1 10  ? 11.45868  18.48258 14.24072 1.000 60.13734  ? 17  VAL   A CA  1 
ATOM   12   C C   . VAL   A 1 10  ? 12.79190  19.21482 14.27986 1.000 58.23883  ? 17  VAL   A C   1 
ATOM   13   O O   . VAL   A 1 10  ? 13.83778  18.63844 13.96219 1.000 65.33444  ? 17  VAL   A O   1 
ATOM   14   C CB  . VAL   A 1 10  ? 11.30812  17.57808 15.48032 1.000 56.93326  ? 17  VAL   A CB  1 
ATOM   15   C CG1 . VAL   A 1 10  ? 11.28299  18.41285 16.74988 1.000 50.88281  ? 17  VAL   A CG1 1 
ATOM   16   C CG2 . VAL   A 1 10  ? 10.06183  16.70853 15.36166 1.000 58.62475  ? 17  VAL   A CG2 1 
ATOM   17   N N   . GLU   A 1 11  ? 12.75217  20.48302 14.67958 1.000 60.37600  ? 18  GLU   A N   1 
ATOM   18   C CA  . GLU   A 1 11  ? 13.94653  21.29762 14.85254 1.000 55.05492  ? 18  GLU   A CA  1 
ATOM   19   C C   . GLU   A 1 11  ? 14.15144  21.57342 16.33548 1.000 47.72800  ? 18  GLU   A C   1 
ATOM   20   O O   . GLU   A 1 11  ? 13.20914  21.95967 17.03491 1.000 50.40559  ? 18  GLU   A O   1 
ATOM   21   C CB  . GLU   A 1 11  ? 13.83531  22.61663 14.08253 1.000 64.27788  ? 18  GLU   A CB  1 
ATOM   22   C CG  . GLU   A 1 11  ? 13.72326  22.45606 12.57341 1.000 72.37595  ? 18  GLU   A CG  1 
ATOM   23   C CD  . GLU   A 1 11  ? 13.49482  23.77740 11.85868 1.000 79.70384  ? 18  GLU   A CD  1 
ATOM   24   O OE1 . GLU   A 1 11  ? 12.41935  24.38602 12.05473 1.000 73.58443  ? 18  GLU   A OE1 1 
ATOM   25   O OE2 . GLU   A 1 11  ? 14.39026  24.20190 11.09511 1.000 77.40328  ? 18  GLU   A OE2 1 
ATOM   26   N N   . THR   A 1 12  ? 15.37932  21.37957 16.80642 1.000 46.81821  ? 19  THR   A N   1 
ATOM   27   C CA  . THR   A 1 12  ? 15.74244  21.59740 18.19891 1.000 53.27781  ? 19  THR   A CA  1 
ATOM   28   C C   . THR   A 1 12  ? 16.58642  22.86062 18.29987 1.000 48.80783  ? 19  THR   A C   1 
ATOM   29   O O   . THR   A 1 12  ? 17.59380  22.99494 17.59633 1.000 48.50933  ? 19  THR   A O   1 
ATOM   30   C CB  . THR   A 1 12  ? 16.51639  20.39940 18.75883 1.000 47.56502  ? 19  THR   A CB  1 
ATOM   31   O OG1 . THR   A 1 12  ? 15.75052  19.19958 18.57840 1.000 47.61488  ? 19  THR   A OG1 1 
ATOM   32   C CG2 . THR   A 1 12  ? 16.80508  20.59648 20.24133 1.000 45.79519  ? 19  THR   A CG2 1 
ATOM   33   N N   . PHE   A 1 13  ? 16.17394  23.78158 19.16679 1.000 53.74850  ? 20  PHE   A N   1 
ATOM   34   C CA  . PHE   A 1 13  ? 16.89016  25.02936 19.38554 1.000 50.38072  ? 20  PHE   A CA  1 
ATOM   35   C C   . PHE   A 1 13  ? 17.32043  25.13445 20.84037 1.000 51.98759  ? 20  PHE   A C   1 
ATOM   36   O O   . PHE   A 1 13  ? 16.64889  24.62471 21.74245 1.000 51.38318  ? 20  PHE   A O   1 
ATOM   37   C CB  . PHE   A 1 13  ? 16.03220  26.24718 19.03251 1.000 49.54567  ? 20  PHE   A CB  1 
ATOM   38   C CG  . PHE   A 1 13  ? 15.41308  26.18371 17.66715 1.000 53.78959  ? 20  PHE   A CG  1 
ATOM   39   C CD1 . PHE   A 1 13  ? 14.20436  25.53754 17.47183 1.000 44.63923  ? 20  PHE   A CD1 1 
ATOM   40   C CD2 . PHE   A 1 13  ? 16.03047  26.78607 16.58223 1.000 56.21533  ? 20  PHE   A CD2 1 
ATOM   41   C CE1 . PHE   A 1 13  ? 13.62649  25.48032 16.21871 1.000 47.49381  ? 20  PHE   A CE1 1 
ATOM   42   C CE2 . PHE   A 1 13  ? 15.45587  26.73536 15.32560 1.000 53.78999  ? 20  PHE   A CE2 1 
ATOM   43   C CZ  . PHE   A 1 13  ? 14.25264  26.08109 15.14357 1.000 49.35975  ? 20  PHE   A CZ  1 
ATOM   44   N N   . ALA   A 1 14  ? 18.44633  25.80439 21.06102 1.000 48.74914  ? 21  ALA   A N   1 
ATOM   45   C CA  . ALA   A 1 14  ? 18.90257  26.11367 22.40645 1.000 50.93576  ? 21  ALA   A CA  1 
ATOM   46   C C   . ALA   A 1 14  ? 18.26984  27.41569 22.87318 1.000 50.01170  ? 21  ALA   A C   1 
ATOM   47   O O   . ALA   A 1 14  ? 18.07907  28.34405 22.08433 1.000 48.19075  ? 21  ALA   A O   1 
ATOM   48   C CB  . ALA   A 1 14  ? 20.42571  26.23114 22.45336 1.000 48.25934  ? 21  ALA   A CB  1 
ATOM   49   N N   . PHE   A 1 15  ? 17.92708  27.47256 24.15504 1.000 63.13338  ? 22  PHE   A N   1 
ATOM   50   C CA  . PHE   A 1 15  ? 17.44434  28.71725 24.73215 1.000 51.82730  ? 22  PHE   A CA  1 
ATOM   51   C C   . PHE   A 1 15  ? 18.57714  29.73215 24.82482 1.000 60.03992  ? 22  PHE   A C   1 
ATOM   52   O O   . PHE   A 1 15  ? 19.74186  29.37797 25.03399 1.000 66.65874  ? 22  PHE   A O   1 
ATOM   53   C CB  . PHE   A 1 15  ? 16.85971  28.47943 26.12602 1.000 51.85626  ? 22  PHE   A CB  1 
ATOM   54   C CG  . PHE   A 1 15  ? 15.45015  27.96526 26.11936 1.000 52.45098  ? 22  PHE   A CG  1 
ATOM   55   C CD1 . PHE   A 1 15  ? 14.41147  28.75413 25.65047 1.000 56.92325  ? 22  PHE   A CD1 1 
ATOM   56   C CD2 . PHE   A 1 15  ? 15.16133  26.69790 26.59710 1.000 50.73380  ? 22  PHE   A CD2 1 
ATOM   57   C CE1 . PHE   A 1 15  ? 13.10941  28.28642 25.65303 1.000 47.36154  ? 22  PHE   A CE1 1 
ATOM   58   C CE2 . PHE   A 1 15  ? 13.86015  26.22086 26.59887 1.000 43.68637  ? 22  PHE   A CE2 1 
ATOM   59   C CZ  . PHE   A 1 15  ? 12.83357  27.01690 26.12709 1.000 46.64635  ? 22  PHE   A CZ  1 
ATOM   60   N N   . GLN   A 1 16  ? 18.22592  31.00633 24.65635 1.000 54.47153  ? 23  GLN   A N   1 
ATOM   61   C CA  . GLN   A 1 16  ? 19.15637  32.07209 24.99450 1.000 69.67421  ? 23  GLN   A CA  1 
ATOM   62   C C   . GLN   A 1 16  ? 19.56696  31.93888 26.45606 1.000 69.68791  ? 23  GLN   A C   1 
ATOM   63   O O   . GLN   A 1 16  ? 18.77829  31.51914 27.30844 1.000 67.05986  ? 23  GLN   A O   1 
ATOM   64   C CB  . GLN   A 1 16  ? 18.54350  33.45469 24.73692 1.000 54.86394  ? 23  GLN   A CB  1 
ATOM   65   C CG  . GLN   A 1 16  ? 17.02739  33.59061 24.94067 1.000 84.01897  ? 23  GLN   A CG  1 
ATOM   66   C CD  . GLN   A 1 16  ? 16.19455  32.85077 23.89750 1.000 86.32765  ? 23  GLN   A CD  1 
ATOM   67   O OE1 . GLN   A 1 16  ? 16.32968  33.08769 22.69926 1.000 101.56090 ? 23  GLN   A OE1 1 
ATOM   68   N NE2 . GLN   A 1 16  ? 15.32806  31.95477 24.35488 1.000 50.85593  ? 23  GLN   A NE2 1 
ATOM   69   N N   . ALA   A 1 17  ? 20.82201  32.29862 26.73903 1.000 69.47958  ? 24  ALA   A N   1 
ATOM   70   C CA  . ALA   A 1 17  ? 21.39314  32.03280 28.05659 1.000 66.54638  ? 24  ALA   A CA  1 
ATOM   71   C C   . ALA   A 1 17  ? 20.55427  32.65077 29.16837 1.000 72.57739  ? 24  ALA   A C   1 
ATOM   72   O O   . ALA   A 1 17  ? 20.40571  32.05768 30.24343 1.000 72.75159  ? 24  ALA   A O   1 
ATOM   73   C CB  . ALA   A 1 17  ? 22.83205  32.54438 28.11711 1.000 63.19354  ? 24  ALA   A CB  1 
ATOM   74   N N   . GLU   A 1 18  ? 19.98156  33.83166 28.92318 1.000 61.94020  ? 25  GLU   A N   1 
ATOM   75   C CA  . GLU   A 1 18  ? 19.19134  34.49591 29.95523 1.000 74.84638  ? 25  GLU   A CA  1 
ATOM   76   C C   . GLU   A 1 18  ? 17.91641  33.71892 30.25033 1.000 62.64694  ? 25  GLU   A C   1 
ATOM   77   O O   . GLU   A 1 18  ? 17.57250  33.48959 31.41570 1.000 64.25239  ? 25  GLU   A O   1 
ATOM   78   C CB  . GLU   A 1 18  ? 18.85914  35.92896 29.53259 1.000 74.30085  ? 25  GLU   A CB  1 
ATOM   79   C CG  . GLU   A 1 18  ? 20.07156  36.81501 29.25805 1.000 83.88943  ? 25  GLU   A CG  1 
ATOM   80   C CD  . GLU   A 1 18  ? 20.62879  36.63651 27.85533 1.000 85.25043  ? 25  GLU   A CD  1 
ATOM   81   O OE1 . GLU   A 1 18  ? 20.05804  35.83929 27.07881 1.000 90.26132  ? 25  GLU   A OE1 1 
ATOM   82   O OE2 . GLU   A 1 18  ? 21.63986  37.29410 27.52914 1.000 96.68598  ? 25  GLU   A OE2 1 
ATOM   83   N N   . ILE   A 1 19  ? 17.19798  33.30994 29.20318 1.000 60.44733  ? 26  ILE   A N   1 
ATOM   84   C CA  . ILE   A 1 19  ? 15.97240  32.54526 29.40257 1.000 55.67402  ? 26  ILE   A CA  1 
ATOM   85   C C   . ILE   A 1 19  ? 16.28806  31.18381 30.01003 1.000 56.65803  ? 26  ILE   A C   1 
ATOM   86   O O   . ILE   A 1 19  ? 15.55347  30.68659 30.87208 1.000 53.69565  ? 26  ILE   A O   1 
ATOM   87   C CB  . ILE   A 1 19  ? 15.20606  32.42124 28.07335 1.000 59.61764  ? 26  ILE   A CB  1 
ATOM   88   C CG1 . ILE   A 1 19  ? 14.56282  33.76305 27.71398 1.000 55.29889  ? 26  ILE   A CG1 1 
ATOM   89   C CG2 . ILE   A 1 19  ? 14.16313  31.31865 28.15351 1.000 49.56291  ? 26  ILE   A CG2 1 
ATOM   90   C CD1 . ILE   A 1 19  ? 13.45798  33.66838 26.68312 1.000 64.09243  ? 26  ILE   A CD1 1 
ATOM   91   N N   . ALA   A 1 20  ? 17.39817  30.57177 29.59369 1.000 63.09278  ? 27  ALA   A N   1 
ATOM   92   C CA  . ALA   A 1 20  ? 17.77464  29.27405 30.14455 1.000 52.04979  ? 27  ALA   A CA  1 
ATOM   93   C C   . ALA   A 1 20  ? 18.05605  29.36507 31.63992 1.000 58.83157  ? 27  ALA   A C   1 
ATOM   94   O O   . ALA   A 1 20  ? 17.75171  28.43227 32.39283 1.000 49.05332  ? 27  ALA   A O   1 
ATOM   95   C CB  . ALA   A 1 20  ? 18.98925  28.72189 29.39997 1.000 54.76656  ? 27  ALA   A CB  1 
ATOM   96   N N   . GLN   A 1 21  ? 18.63833  30.48073 32.08984 1.000 55.76484  ? 28  GLN   A N   1 
ATOM   97   C CA  . GLN   A 1 21  ? 18.87498  30.66603 33.51877 1.000 56.51324  ? 28  GLN   A CA  1 
ATOM   98   C C   . GLN   A 1 21  ? 17.57250  30.91956 34.26676 1.000 56.16082  ? 28  GLN   A C   1 
ATOM   99   O O   . GLN   A 1 21  ? 17.37799  30.40852 35.37583 1.000 67.02863  ? 28  GLN   A O   1 
ATOM   100  C CB  . GLN   A 1 21  ? 19.84416  31.82317 33.74771 1.000 56.16613  ? 28  GLN   A CB  1 
ATOM   101  C CG  . GLN   A 1 21  ? 21.24108  31.62274 33.20417 1.000 67.93104  ? 28  GLN   A CG  1 
ATOM   102  C CD  . GLN   A 1 21  ? 22.02381  32.92013 33.17443 1.000 86.83218  ? 28  GLN   A CD  1 
ATOM   103  O OE1 . GLN   A 1 21  ? 21.57580  33.93760 33.70675 1.000 75.32712  ? 28  GLN   A OE1 1 
ATOM   104  N NE2 . GLN   A 1 21  ? 23.19656  32.89396 32.54774 1.000 74.32505  ? 28  GLN   A NE2 1 
ATOM   105  N N   . LEU   A 1 22  ? 16.67500  31.71799 33.68315 1.000 59.50397  ? 29  LEU   A N   1 
ATOM   106  C CA  . LEU   A 1 22  ? 15.39702  31.98912 34.33243 1.000 56.08800  ? 29  LEU   A CA  1 
ATOM   107  C C   . LEU   A 1 22  ? 14.58696  30.71133 34.49892 1.000 55.83559  ? 29  LEU   A C   1 
ATOM   108  O O   . LEU   A 1 22  ? 13.94062  30.50440 35.53409 1.000 55.42948  ? 29  LEU   A O   1 
ATOM   109  C CB  . LEU   A 1 22  ? 14.60492  33.01997 33.52674 1.000 47.33640  ? 29  LEU   A CB  1 
ATOM   110  C CG  . LEU   A 1 22  ? 13.15749  33.23170 33.98200 1.000 49.51165  ? 29  LEU   A CG  1 
ATOM   111  C CD1 . LEU   A 1 22  ? 13.11201  33.65230 35.44559 1.000 51.51768  ? 29  LEU   A CD1 1 
ATOM   112  C CD2 . LEU   A 1 22  ? 12.43582  34.24132 33.10157 1.000 58.99376  ? 29  LEU   A CD2 1 
ATOM   113  N N   . MET   A 1 23  ? 14.61351  29.84059 33.48758 1.000 53.06723  ? 30  MET   A N   1 
ATOM   114  C CA  . MET   A 1 23  ? 13.84621  28.60286 33.55746 1.000 54.60112  ? 30  MET   A CA  1 
ATOM   115  C C   . MET   A 1 23  ? 14.41297  27.67979 34.62522 1.000 50.84844  ? 30  MET   A C   1 
ATOM   116  O O   . MET   A 1 23  ? 13.66239  27.07829 35.40241 1.000 65.05758  ? 30  MET   A O   1 
ATOM   117  C CB  . MET   A 1 23  ? 13.84686  27.90766 32.19538 1.000 53.96203  ? 30  MET   A CB  1 
ATOM   118  C CG  . MET   A 1 23  ? 13.11853  28.69028 31.11343 1.000 59.11616  ? 30  MET   A CG  1 
ATOM   119  S SD  . MET   A 1 23  ? 13.09183  27.89152 29.49384 1.000 55.51451  ? 30  MET   A SD  1 
ATOM   120  C CE  . MET   A 1 23  ? 12.20513  26.38666 29.86324 1.000 57.49082  ? 30  MET   A CE  1 
ATOM   121  N N   . SER   A 1 24  ? 15.73993  27.56891 34.68787 1.000 55.04392  ? 31  SER   A N   1 
ATOM   122  C CA  . SER   A 1 24  ? 16.35602  26.73408 35.70831 1.000 57.16625  ? 31  SER   A CA  1 
ATOM   123  C C   . SER   A 1 24  ? 16.14879  27.31421 37.10200 1.000 62.75658  ? 31  SER   A C   1 
ATOM   124  O O   . SER   A 1 24  ? 16.04634  26.55825 38.07335 1.000 57.92172  ? 31  SER   A O   1 
ATOM   125  C CB  . SER   A 1 24  ? 17.84449  26.55281 35.40757 1.000 60.29171  ? 31  SER   A CB  1 
ATOM   126  O OG  . SER   A 1 24  ? 18.57236  26.26297 36.58696 1.000 71.61461  ? 31  SER   A OG  1 
ATOM   127  N N   . LEU   A 1 25  ? 16.07259  28.64232 37.22480 1.000 65.14966  ? 32  LEU   A N   1 
ATOM   128  C CA  . LEU   A 1 25  ? 15.76468  29.23484 38.52284 1.000 60.17696  ? 32  LEU   A CA  1 
ATOM   129  C C   . LEU   A 1 25  ? 14.32947  28.93130 38.93488 1.000 60.30363  ? 32  LEU   A C   1 
ATOM   130  O O   . LEU   A 1 25  ? 14.06922  28.60240 40.09656 1.000 68.15130  ? 32  LEU   A O   1 
ATOM   131  C CB  . LEU   A 1 25  ? 16.02012  30.74502 38.48681 1.000 57.17280  ? 32  LEU   A CB  1 
ATOM   132  C CG  . LEU   A 1 25  ? 15.85167  31.58947 39.75671 1.000 77.65287  ? 32  LEU   A CG  1 
ATOM   133  C CD1 . LEU   A 1 25  ? 16.82151  32.75862 39.71205 1.000 64.18534  ? 32  LEU   A CD1 1 
ATOM   134  C CD2 . LEU   A 1 25  ? 14.42504  32.11005 39.92933 1.000 79.98980  ? 32  LEU   A CD2 1 
ATOM   135  N N   . ILE   A 1 26  ? 13.38633  29.03297 37.99624 1.000 62.09671  ? 33  ILE   A N   1 
ATOM   136  C CA  . ILE   A 1 26  ? 11.97891  28.82039 38.32210 1.000 60.41363  ? 33  ILE   A CA  1 
ATOM   137  C C   . ILE   A 1 26  ? 11.73769  27.37815 38.75304 1.000 59.02461  ? 33  ILE   A C   1 
ATOM   138  O O   . ILE   A 1 26  ? 10.94292  27.10938 39.66228 1.000 59.66982  ? 33  ILE   A O   1 
ATOM   139  C CB  . ILE   A 1 26  ? 11.09859  29.21375 37.12155 1.000 50.65746  ? 33  ILE   A CB  1 
ATOM   140  C CG1 . ILE   A 1 26  ? 10.94405  30.73457 37.04984 1.000 51.02212  ? 33  ILE   A CG1 1 
ATOM   141  C CG2 . ILE   A 1 26  ? 9.73625   28.55102 37.20591 1.000 56.90420  ? 33  ILE   A CG2 1 
ATOM   142  C CD1 . ILE   A 1 26  ? 10.39377  31.22322 35.72808 1.000 49.37763  ? 33  ILE   A CD1 1 
ATOM   143  N N   . ILE   A 1 27  ? 12.43269  26.42998 38.12595 1.000 64.57862  ? 34  ILE   A N   1 
ATOM   144  C CA  . ILE   A 1 27  ? 12.21267  25.02223 38.44022 1.000 72.51778  ? 34  ILE   A CA  1 
ATOM   145  C C   . ILE   A 1 27  ? 12.83624  24.65960 39.78389 1.000 77.16473  ? 34  ILE   A C   1 
ATOM   146  O O   . ILE   A 1 27  ? 12.23703  23.93167 40.58522 1.000 86.12471  ? 34  ILE   A O   1 
ATOM   147  C CB  . ILE   A 1 27  ? 12.75884  24.14174 37.30354 1.000 67.35364  ? 34  ILE   A CB  1 
ATOM   148  C CG1 . ILE   A 1 27  ? 11.73454  24.04785 36.18121 1.000 53.73357  ? 34  ILE   A CG1 1 
ATOM   149  C CG2 . ILE   A 1 27  ? 13.11720  22.75359 37.81101 1.000 85.01112  ? 34  ILE   A CG2 1 
ATOM   150  C CD1 . ILE   A 1 27  ? 12.35413  24.03121 34.83301 1.000 60.38064  ? 34  ILE   A CD1 1 
ATOM   151  N N   . ASN   A 1 28  ? 14.03436  25.17173 40.06190 1.000 70.54180  ? 35  ASN   A N   1 
ATOM   152  C CA  . ASN   A 1 28  ? 14.81487  24.70765 41.20100 1.000 74.22102  ? 35  ASN   A CA  1 
ATOM   153  C C   . ASN   A 1 28  ? 14.61968  25.53662 42.46365 1.000 78.99164  ? 35  ASN   A C   1 
ATOM   154  O O   . ASN   A 1 28  ? 14.94853  25.05502 43.55423 1.000 93.36613  ? 35  ASN   A O   1 
ATOM   155  C CB  . ASN   A 1 28  ? 16.30148  24.68034 40.83577 1.000 72.37820  ? 35  ASN   A CB  1 
ATOM   156  C CG  . ASN   A 1 28  ? 16.57396  23.86417 39.58925 1.000 75.75030  ? 35  ASN   A CG  1 
ATOM   157  O OD1 . ASN   A 1 28  ? 15.95561  22.82268 39.36903 1.000 78.36898  ? 35  ASN   A OD1 1 
ATOM   158  N ND2 . ASN   A 1 28  ? 17.49539  24.33846 38.76035 1.000 81.19615  ? 35  ASN   A ND2 1 
ATOM   159  N N   . THR   A 1 29  ? 14.10684  26.75946 42.35539 1.000 83.35988  ? 36  THR   A N   1 
ATOM   160  C CA  . THR   A 1 29  ? 13.83549  27.54809 43.54986 1.000 79.67591  ? 36  THR   A CA  1 
ATOM   161  C C   . THR   A 1 29  ? 12.58994  27.01352 44.24409 1.000 72.44114  ? 36  THR   A C   1 
ATOM   162  O O   . THR   A 1 29  ? 11.55271  26.79912 43.60862 1.000 75.70064  ? 36  THR   A O   1 
ATOM   163  C CB  . THR   A 1 29  ? 13.65858  29.02575 43.19902 1.000 84.57308  ? 36  THR   A CB  1 
ATOM   164  O OG1 . THR   A 1 29  ? 14.94126  29.61496 42.95134 1.000 88.79547  ? 36  THR   A OG1 1 
ATOM   165  C CG2 . THR   A 1 29  ? 12.98222  29.77297 44.34238 1.000 80.34133  ? 36  THR   A CG2 1 
ATOM   166  N N   . PHE   A 1 30  ? 12.70192  26.78000 45.54799 1.000 82.46595  ? 37  PHE   A N   1 
ATOM   167  C CA  . PHE   A 1 30  ? 11.58854  26.28082 46.34993 1.000 76.64860  ? 37  PHE   A CA  1 
ATOM   168  C C   . PHE   A 1 30  ? 10.69195  27.46284 46.68844 1.000 69.06109  ? 37  PHE   A C   1 
ATOM   169  O O   . PHE   A 1 30  ? 10.89155  28.16417 47.68114 1.000 98.75746  ? 37  PHE   A O   1 
ATOM   170  C CB  . PHE   A 1 30  ? 12.09790  25.57769 47.60296 1.000 88.26598  ? 37  PHE   A CB  1 
ATOM   171  C CG  . PHE   A 1 30  ? 13.09546  24.48466 47.32521 1.000 99.99752  ? 37  PHE   A CG  1 
ATOM   172  C CD1 . PHE   A 1 30  ? 12.87044  23.56232 46.31473 1.000 107.98618 ? 37  PHE   A CD1 1 
ATOM   173  C CD2 . PHE   A 1 30  ? 14.25430  24.37493 48.07994 1.000 111.09436 ? 37  PHE   A CD2 1 
ATOM   174  C CE1 . PHE   A 1 30  ? 13.78481  22.55616 46.05733 1.000 114.03236 ? 37  PHE   A CE1 1 
ATOM   175  C CE2 . PHE   A 1 30  ? 15.17255  23.36922 47.82863 1.000 111.19595 ? 37  PHE   A CE2 1 
ATOM   176  C CZ  . PHE   A 1 30  ? 14.93654  22.45913 46.81579 1.000 116.25047 ? 37  PHE   A CZ  1 
ATOM   177  N N   . TYR   A 1 31  ? 9.69736   27.69281 45.83846 1.000 73.66198  ? 38  TYR   A N   1 
ATOM   178  C CA  . TYR   A 1 31  ? 8.74161   28.77844 46.00025 1.000 67.86754  ? 38  TYR   A CA  1 
ATOM   179  C C   . TYR   A 1 31  ? 7.35722   28.17015 46.15812 1.000 72.29340  ? 38  TYR   A C   1 
ATOM   180  O O   . TYR   A 1 31  ? 6.94577   27.33734 45.34377 1.000 68.59498  ? 38  TYR   A O   1 
ATOM   181  C CB  . TYR   A 1 31  ? 8.80005   29.73188 44.80249 1.000 71.40878  ? 38  TYR   A CB  1 
ATOM   182  C CG  . TYR   A 1 31  ? 7.81687   30.87828 44.84655 1.000 78.82016  ? 38  TYR   A CG  1 
ATOM   183  C CD1 . TYR   A 1 31  ? 8.02766   31.97093 45.67903 1.000 81.30164  ? 38  TYR   A CD1 1 
ATOM   184  C CD2 . TYR   A 1 31  ? 6.69573   30.88561 44.03016 1.000 80.81877  ? 38  TYR   A CD2 1 
ATOM   185  C CE1 . TYR   A 1 31  ? 7.13327   33.02663 45.71464 1.000 77.02454  ? 38  TYR   A CE1 1 
ATOM   186  C CE2 . TYR   A 1 31  ? 5.80099   31.93771 44.05613 1.000 77.48380  ? 38  TYR   A CE2 1 
ATOM   187  C CZ  . TYR   A 1 31  ? 6.02080   33.00210 44.89963 1.000 75.83685  ? 38  TYR   A CZ  1 
ATOM   188  O OH  . TYR   A 1 31  ? 5.12613   34.04540 44.92452 1.000 77.85425  ? 38  TYR   A OH  1 
ATOM   189  N N   . SER   A 1 32  ? 6.65052   28.56880 47.21356 1.000 77.73930  ? 39  SER   A N   1 
ATOM   190  C CA  . SER   A 1 32  ? 5.41414   27.88684 47.57341 1.000 70.99820  ? 39  SER   A CA  1 
ATOM   191  C C   . SER   A 1 32  ? 4.20121   28.42484 46.82402 1.000 68.47991  ? 39  SER   A C   1 
ATOM   192  O O   . SER   A 1 32  ? 3.33998   27.64353 46.40533 1.000 78.67651  ? 39  SER   A O   1 
ATOM   193  C CB  . SER   A 1 32  ? 5.18542   27.98232 49.08323 1.000 78.04001  ? 39  SER   A CB  1 
ATOM   194  O OG  . SER   A 1 32  ? 5.75384   26.86319 49.74603 1.000 78.78311  ? 39  SER   A OG  1 
ATOM   195  N N   . ASN   A 1 33  ? 4.11752   29.74005 46.63116 1.000 69.99984  ? 40  ASN   A N   1 
ATOM   196  C CA  . ASN   A 1 33  ? 2.96609   30.34201 45.96814 1.000 71.28089  ? 40  ASN   A CA  1 
ATOM   197  C C   . ASN   A 1 33  ? 2.97009   30.03377 44.47322 1.000 65.97293  ? 40  ASN   A C   1 
ATOM   198  O O   . ASN   A 1 33  ? 3.05308   30.94073 43.63828 1.000 66.69940  ? 40  ASN   A O   1 
ATOM   199  C CB  . ASN   A 1 33  ? 2.95199   31.85116 46.20851 1.000 64.57923  ? 40  ASN   A CB  1 
ATOM   200  C CG  . ASN   A 1 33  ? 1.61649   32.47776 45.88301 1.000 72.99721  ? 40  ASN   A CG  1 
ATOM   201  O OD1 . ASN   A 1 33  ? 0.56248   31.91604 46.18631 1.000 77.26374  ? 40  ASN   A OD1 1 
ATOM   202  N ND2 . ASN   A 1 33  ? 1.65119   33.64899 45.25930 1.000 74.00105  ? 40  ASN   A ND2 1 
ATOM   203  N N   . LYS   A 1 34  ? 2.86321   28.75074 44.12631 1.000 66.42758  ? 41  LYS   A N   1 
ATOM   204  C CA  . LYS   A 1 34  ? 2.94128   28.33093 42.73326 1.000 67.34383  ? 41  LYS   A CA  1 
ATOM   205  C C   . LYS   A 1 34  ? 1.68905   28.66833 41.93569 1.000 61.83944  ? 41  LYS   A C   1 
ATOM   206  O O   . LYS   A 1 34  ? 1.72227   28.57161 40.70432 1.000 56.01053  ? 41  LYS   A O   1 
ATOM   207  C CB  . LYS   A 1 34  ? 3.20682   26.82572 42.65832 1.000 63.62966  ? 41  LYS   A CB  1 
ATOM   208  C CG  . LYS   A 1 34  ? 4.61654   26.43011 43.07334 1.000 54.32326  ? 41  LYS   A CG  1 
ATOM   209  C CD  . LYS   A 1 34  ? 4.82593   24.92922 43.00933 1.000 63.31330  ? 41  LYS   A CD  1 
ATOM   210  C CE  . LYS   A 1 34  ? 6.12561   24.53724 43.69223 1.000 68.56456  ? 41  LYS   A CE  1 
ATOM   211  N NZ  . LYS   A 1 34  ? 7.30791   25.02288 42.92757 1.000 71.89376  ? 41  LYS   A NZ  1 
ATOM   212  N N   . GLU   A 1 35  ? 0.60073   29.07811 42.59390 1.000 63.39637  ? 42  GLU   A N   1 
ATOM   213  C CA  . GLU   A 1 35  ? -0.67083  29.25872 41.89913 1.000 48.43504  ? 42  GLU   A CA  1 
ATOM   214  C C   . GLU   A 1 35  ? -0.65926  30.43934 40.93833 1.000 59.14512  ? 42  GLU   A C   1 
ATOM   215  O O   . GLU   A 1 35  ? -1.54363  30.52993 40.07799 1.000 55.07744  ? 42  GLU   A O   1 
ATOM   216  C CB  . GLU   A 1 35  ? -1.80467  29.43151 42.91063 1.000 63.52422  ? 42  GLU   A CB  1 
ATOM   217  C CG  . GLU   A 1 35  ? -1.67943  30.65727 43.79811 1.000 69.02412  ? 42  GLU   A CG  1 
ATOM   218  C CD  . GLU   A 1 35  ? -2.75610  30.70510 44.86886 1.000 86.32768  ? 42  GLU   A CD  1 
ATOM   219  O OE1 . GLU   A 1 35  ? -3.12356  29.62934 45.39024 1.000 88.54933  ? 42  GLU   A OE1 1 
ATOM   220  O OE2 . GLU   A 1 35  ? -3.23115  31.81423 45.19388 1.000 87.03665  ? 42  GLU   A OE2 1 
ATOM   221  N N   . ILE   A 1 36  ? 0.32017   31.33722 41.05307 1.000 59.84593  ? 43  ILE   A N   1 
ATOM   222  C CA  . ILE   A 1 36  ? 0.36163   32.51569 40.20286 1.000 55.52822  ? 43  ILE   A CA  1 
ATOM   223  C C   . ILE   A 1 36  ? 0.53912   32.17091 38.73168 1.000 58.40032  ? 43  ILE   A C   1 
ATOM   224  O O   . ILE   A 1 36  ? 0.28886   33.02307 37.87720 1.000 56.70768  ? 43  ILE   A O   1 
ATOM   225  C CB  . ILE   A 1 36  ? 1.47221   33.47891 40.68151 1.000 61.93217  ? 43  ILE   A CB  1 
ATOM   226  C CG1 . ILE   A 1 36  ? 2.81842   32.76008 40.79971 1.000 67.50037  ? 43  ILE   A CG1 1 
ATOM   227  C CG2 . ILE   A 1 36  ? 1.09933   34.08225 42.02147 1.000 59.76583  ? 43  ILE   A CG2 1 
ATOM   228  C CD1 . ILE   A 1 36  ? 3.80309   33.11492 39.70546 1.000 61.06524  ? 43  ILE   A CD1 1 
ATOM   229  N N   . PHE   A 1 37  ? 0.94534   30.93539 38.41420 1.000 48.00305  ? 44  PHE   A N   1 
ATOM   230  C CA  . PHE   A 1 37  ? 1.13882   30.55092 37.01787 1.000 50.44790  ? 44  PHE   A CA  1 
ATOM   231  C C   . PHE   A 1 37  ? -0.14406  30.71290 36.21347 1.000 52.86221  ? 44  PHE   A C   1 
ATOM   232  O O   . PHE   A 1 37  ? -0.10506  31.11744 35.04582 1.000 56.84194  ? 44  PHE   A O   1 
ATOM   233  C CB  . PHE   A 1 37  ? 1.63993   29.10583 36.92609 1.000 52.21444  ? 44  PHE   A CB  1 
ATOM   234  C CG  . PHE   A 1 37  ? 0.54097   28.07155 36.98982 1.000 48.12827  ? 44  PHE   A CG  1 
ATOM   235  C CD1 . PHE   A 1 37  ? 0.09967   27.58723 38.20861 1.000 44.63768  ? 44  PHE   A CD1 1 
ATOM   236  C CD2 . PHE   A 1 37  ? -0.05865  27.59609 35.83189 1.000 50.08692  ? 44  PHE   A CD2 1 
ATOM   237  C CE1 . PHE   A 1 37  ? -0.90878  26.64797 38.27458 1.000 52.05202  ? 44  PHE   A CE1 1 
ATOM   238  C CE2 . PHE   A 1 37  ? -1.07474  26.66174 35.89590 1.000 46.73521  ? 44  PHE   A CE2 1 
ATOM   239  C CZ  . PHE   A 1 37  ? -1.49436  26.18343 37.11543 1.000 52.33821  ? 44  PHE   A CZ  1 
ATOM   240  N N   . LEU   A 1 38  ? -1.29015  30.38482 36.81531 1.000 51.86385  ? 45  LEU   A N   1 
ATOM   241  C CA  . LEU   A 1 38  ? -2.55262  30.46275 36.08996 1.000 51.08391  ? 45  LEU   A CA  1 
ATOM   242  C C   . LEU   A 1 38  ? -2.90051  31.90480 35.74685 1.000 54.36244  ? 45  LEU   A C   1 
ATOM   243  O O   . LEU   A 1 38  ? -3.37153  32.18897 34.63836 1.000 56.18261  ? 45  LEU   A O   1 
ATOM   244  C CB  . LEU   A 1 38  ? -3.66584  29.81807 36.91236 1.000 51.54605  ? 45  LEU   A CB  1 
ATOM   245  C CG  . LEU   A 1 38  ? -5.00357  29.65077 36.19756 1.000 40.35223  ? 45  LEU   A CG  1 
ATOM   246  C CD1 . LEU   A 1 38  ? -4.79883  28.95610 34.86592 1.000 41.01632  ? 45  LEU   A CD1 1 
ATOM   247  C CD2 . LEU   A 1 38  ? -5.97344  28.87677 37.07441 1.000 46.64924  ? 45  LEU   A CD2 1 
ATOM   248  N N   . ARG   A 1 39  ? -2.67010  32.82810 36.68437 1.000 55.26339  ? 46  ARG   A N   1 
ATOM   249  C CA  . ARG   A 1 39  ? -2.89734  34.24323 36.40798 1.000 52.97827  ? 46  ARG   A CA  1 
ATOM   250  C C   . ARG   A 1 39  ? -2.01681  34.72964 35.26293 1.000 54.78274  ? 46  ARG   A C   1 
ATOM   251  O O   . ARG   A 1 39  ? -2.47105  35.49270 34.40161 1.000 57.45145  ? 46  ARG   A O   1 
ATOM   252  C CB  . ARG   A 1 39  ? -2.64152  35.06391 37.67259 1.000 59.43966  ? 46  ARG   A CB  1 
ATOM   253  C CG  . ARG   A 1 39  ? -2.31356  36.52889 37.42797 1.000 67.67809  ? 46  ARG   A CG  1 
ATOM   254  C CD  . ARG   A 1 39  ? -1.93690  37.23317 38.72334 1.000 68.90321  ? 46  ARG   A CD  1 
ATOM   255  N NE  . ARG   A 1 39  ? -0.50795  37.51808 38.78495 1.000 87.99539  ? 46  ARG   A NE  1 
ATOM   256  C CZ  . ARG   A 1 39  ? 0.23584   37.41033 39.87860 1.000 94.99793  ? 46  ARG   A CZ  1 
ATOM   257  N NH1 . ARG   A 1 39  ? -0.29018  37.06310 41.04260 1.000 80.30184  ? 46  ARG   A NH1 1 
ATOM   258  N NH2 . ARG   A 1 39  ? 1.54092   37.65885 39.80299 1.000 85.25636  ? 46  ARG   A NH2 1 
ATOM   259  N N   . GLU   A 1 40  ? -0.75561  34.28553 35.23030 1.000 47.89954  ? 47  GLU   A N   1 
ATOM   260  C CA  . GLU   A 1 40  ? 0.17117   34.73702 34.19659 1.000 48.05830  ? 47  GLU   A CA  1 
ATOM   261  C C   . GLU   A 1 40  ? -0.25307  34.25208 32.81496 1.000 56.62784  ? 47  GLU   A C   1 
ATOM   262  O O   . GLU   A 1 40  ? -0.18820  35.00825 31.83699 1.000 54.29129  ? 47  GLU   A O   1 
ATOM   263  C CB  . GLU   A 1 40  ? 1.58724   34.25866 34.51906 1.000 47.67090  ? 47  GLU   A CB  1 
ATOM   264  C CG  . GLU   A 1 40  ? 2.18737   34.84280 35.79565 1.000 48.43082  ? 47  GLU   A CG  1 
ATOM   265  C CD  . GLU   A 1 40  ? 2.02499   36.35412 35.90393 1.000 73.32648  ? 47  GLU   A CD  1 
ATOM   266  O OE1 . GLU   A 1 40  ? 2.24160   37.06328 34.89687 1.000 66.36043  ? 47  GLU   A OE1 1 
ATOM   267  O OE2 . GLU   A 1 40  ? 1.68773   36.83558 37.00618 1.000 75.82123  ? 47  GLU   A OE2 1 
ATOM   268  N N   . LEU   A 1 41  ? -0.68951  32.99553 32.71339 1.000 45.83052  ? 48  LEU   A N   1 
ATOM   269  C CA  . LEU   A 1 41  ? -1.09546  32.45996 31.41761 1.000 47.38791  ? 48  LEU   A CA  1 
ATOM   270  C C   . LEU   A 1 41  ? -2.43061  33.04461 30.96863 1.000 40.73247  ? 48  LEU   A C   1 
ATOM   271  O O   . LEU   A 1 41  ? -2.62055  33.32762 29.78048 1.000 49.86363  ? 48  LEU   A O   1 
ATOM   272  C CB  . LEU   A 1 41  ? -1.16691  30.93536 31.48420 1.000 42.19250  ? 48  LEU   A CB  1 
ATOM   273  C CG  . LEU   A 1 41  ? 0.15964   30.22046 31.74053 1.000 48.08451  ? 48  LEU   A CG  1 
ATOM   274  C CD1 . LEU   A 1 41  ? -0.04305  28.71544 31.75892 1.000 41.76002  ? 48  LEU   A CD1 1 
ATOM   275  C CD2 . LEU   A 1 41  ? 1.18805   30.61258 30.69083 1.000 47.61542  ? 48  LEU   A CD2 1 
ATOM   276  N N   . ILE   A 1 42  ? -3.36830  33.22735 31.90245 1.000 43.78301  ? 49  ILE   A N   1 
ATOM   277  C CA  . ILE   A 1 42  ? -4.64460  33.85954 31.57329 1.000 47.81819  ? 49  ILE   A CA  1 
ATOM   278  C C   . ILE   A 1 42  ? -4.42217  35.29794 31.12154 1.000 48.29003  ? 49  ILE   A C   1 
ATOM   279  O O   . ILE   A 1 42  ? -5.07528  35.78307 30.18782 1.000 41.62487  ? 49  ILE   A O   1 
ATOM   280  C CB  . ILE   A 1 42  ? -5.60068  33.78474 32.78138 1.000 45.34996  ? 49  ILE   A CB  1 
ATOM   281  C CG1 . ILE   A 1 42  ? -6.15353  32.36816 32.94392 1.000 49.12150  ? 49  ILE   A CG1 1 
ATOM   282  C CG2 . ILE   A 1 42  ? -6.73450  34.80558 32.65795 1.000 49.56169  ? 49  ILE   A CG2 1 
ATOM   283  C CD1 . ILE   A 1 42  ? -7.12268  32.22955 34.09370 1.000 41.54644  ? 49  ILE   A CD1 1 
ATOM   284  N N   . SER   A 1 43  ? -3.49234  36.00065 31.77354 1.000 48.95910  ? 50  SER   A N   1 
ATOM   285  C CA  . SER   A 1 43  ? -3.17511  37.36470 31.36553 1.000 50.46268  ? 50  SER   A CA  1 
ATOM   286  C C   . SER   A 1 43  ? -2.53790  37.39300 29.97998 1.000 55.18643  ? 50  SER   A C   1 
ATOM   287  O O   . SER   A 1 43  ? -2.83837  38.28179 29.17233 1.000 49.75396  ? 50  SER   A O   1 
ATOM   288  C CB  . SER   A 1 43  ? -2.26024  38.02106 32.39954 1.000 48.34263  ? 50  SER   A CB  1 
ATOM   289  O OG  . SER   A 1 43  ? -1.59465  39.14779 31.85205 1.000 68.04347  ? 50  SER   A OG  1 
ATOM   290  N N   . ASN   A 1 44  ? -1.65597  36.43058 29.68548 1.000 43.42031  ? 51  ASN   A N   1 
ATOM   291  C CA  . ASN   A 1 44  ? -1.10071  36.32349 28.33735 1.000 40.91207  ? 51  ASN   A CA  1 
ATOM   292  C C   . ASN   A 1 44  ? -2.19660  36.06256 27.31170 1.000 44.80140  ? 51  ASN   A C   1 
ATOM   293  O O   . ASN   A 1 44  ? -2.20495  36.66390 26.23054 1.000 50.99175  ? 51  ASN   A O   1 
ATOM   294  C CB  . ASN   A 1 44  ? -0.05295  35.21180 28.27730 1.000 53.27598  ? 51  ASN   A CB  1 
ATOM   295  C CG  . ASN   A 1 44  ? 1.29522   35.64527 28.81760 1.000 59.22728  ? 51  ASN   A CG  1 
ATOM   296  O OD1 . ASN   A 1 44  ? 1.45635   36.76800 29.29042 1.000 55.56200  ? 51  ASN   A OD1 1 
ATOM   297  N ND2 . ASN   A 1 44  ? 2.27545   34.75061 28.74596 1.000 61.07658  ? 51  ASN   A ND2 1 
ATOM   298  N N   . SER   A 1 45  ? -3.12625  35.16065 27.63205 1.000 49.20807  ? 52  SER   A N   1 
ATOM   299  C CA  . SER   A 1 45  ? -4.24241  34.89039 26.73322 1.000 48.44660  ? 52  SER   A CA  1 
ATOM   300  C C   . SER   A 1 45  ? -5.09673  36.13341 26.52607 1.000 46.57985  ? 52  SER   A C   1 
ATOM   301  O O   . SER   A 1 45  ? -5.56512  36.39549 25.41122 1.000 38.56545  ? 52  SER   A O   1 
ATOM   302  C CB  . SER   A 1 45  ? -5.09137  33.74559 27.28516 1.000 40.93799  ? 52  SER   A CB  1 
ATOM   303  O OG  . SER   A 1 45  ? -4.47516  32.49114 27.04918 1.000 49.83356  ? 52  SER   A OG  1 
ATOM   304  N N   . SER   A 1 46  ? -5.31524  36.90896 27.59163 1.000 48.59468  ? 53  SER   A N   1 
ATOM   305  C CA  . SER   A 1 46  ? -6.10889  38.12665 27.46796 1.000 41.87050  ? 53  SER   A CA  1 
ATOM   306  C C   . SER   A 1 46  ? -5.42978  39.12979 26.54448 1.000 49.48388  ? 53  SER   A C   1 
ATOM   307  O O   . SER   A 1 46  ? -6.08959  39.76280 25.70952 1.000 44.94035  ? 53  SER   A O   1 
ATOM   308  C CB  . SER   A 1 46  ? -6.35029  38.73690 28.84999 1.000 54.24773  ? 53  SER   A CB  1 
ATOM   309  O OG  . SER   A 1 46  ? -7.12796  39.91880 28.76068 1.000 60.95130  ? 53  SER   A OG  1 
ATOM   310  N N   . ASP   A 1 47  ? -4.10993  39.28830 26.67985 1.000 40.44373  ? 54  ASP   A N   1 
ATOM   311  C CA  . ASP   A 1 47  ? -3.36919  40.15318 25.76693 1.000 44.61836  ? 54  ASP   A CA  1 
ATOM   312  C C   . ASP   A 1 47  ? -3.56182  39.70395 24.32410 1.000 43.74738  ? 54  ASP   A C   1 
ATOM   313  O O   . ASP   A 1 47  ? -3.89499  40.51104 23.45079 1.000 49.43962  ? 54  ASP   A O   1 
ATOM   314  C CB  . ASP   A 1 47  ? -1.88349  40.16215 26.13659 1.000 39.15465  ? 54  ASP   A CB  1 
ATOM   315  C CG  . ASP   A 1 47  ? -1.60446  40.88296 27.44876 1.000 54.94280  ? 54  ASP   A CG  1 
ATOM   316  O OD1 . ASP   A 1 47  ? -2.53119  41.51255 28.00306 1.000 65.33970  ? 54  ASP   A OD1 1 
ATOM   317  O OD2 . ASP   A 1 47  ? -0.45181  40.81512 27.92908 1.000 57.32267  ? 54  ASP   A OD2 1 
ATOM   318  N N   . ALA   A 1 48  ? -3.38831  38.40414 24.06446 1.000 50.07309  ? 55  ALA   A N   1 
ATOM   319  C CA  . ALA   A 1 48  ? -3.51114  37.88948 22.70435 1.000 41.20765  ? 55  ALA   A CA  1 
ATOM   320  C C   . ALA   A 1 48  ? -4.90105  38.12643 22.12825 1.000 34.12835  ? 55  ALA   A C   1 
ATOM   321  O O   . ALA   A 1 48  ? -5.04065  38.34538 20.91974 1.000 34.86100  ? 55  ALA   A O   1 
ATOM   322  C CB  . ALA   A 1 48  ? -3.17035  36.39862 22.67564 1.000 32.39577  ? 55  ALA   A CB  1 
ATOM   323  N N   . LEU   A 1 49  ? -5.94062  38.07983 22.96334 1.000 38.12232  ? 56  LEU   A N   1 
ATOM   324  C CA  . LEU   A 1 49  ? -7.27757  38.38339 22.46480 1.000 38.42919  ? 56  LEU   A CA  1 
ATOM   325  C C   . LEU   A 1 49  ? -7.44315  39.87182 22.19391 1.000 48.73659  ? 56  LEU   A C   1 
ATOM   326  O O   . LEU   A 1 49  ? -8.17583  40.25661 21.27494 1.000 46.94007  ? 56  LEU   A O   1 
ATOM   327  C CB  . LEU   A 1 49  ? -8.32880  37.88852 23.45562 1.000 42.60750  ? 56  LEU   A CB  1 
ATOM   328  C CG  . LEU   A 1 49  ? -8.39449  36.36342 23.56280 1.000 42.47427  ? 56  LEU   A CG  1 
ATOM   329  C CD1 . LEU   A 1 49  ? -8.83618  35.93518 24.94669 1.000 41.00905  ? 56  LEU   A CD1 1 
ATOM   330  C CD2 . LEU   A 1 49  ? -9.33033  35.81331 22.50824 1.000 41.85369  ? 56  LEU   A CD2 1 
ATOM   331  N N   . ASP   A 1 50  ? -6.76438  40.71795 22.97147 1.000 40.94709  ? 57  ASP   A N   1 
ATOM   332  C CA  . ASP   A 1 50  ? -6.80596  42.15254 22.72017 1.000 42.72292  ? 57  ASP   A CA  1 
ATOM   333  C C   . ASP   A 1 50  ? -6.23116  42.48977 21.34903 1.000 49.35547  ? 57  ASP   A C   1 
ATOM   334  O O   . ASP   A 1 50  ? -6.79295  43.31616 20.62049 1.000 45.62584  ? 57  ASP   A O   1 
ATOM   335  C CB  . ASP   A 1 50  ? -6.04044  42.89762 23.81618 1.000 43.85442  ? 57  ASP   A CB  1 
ATOM   336  C CG  . ASP   A 1 50  ? -6.84190  43.04819 25.09719 1.000 49.63753  ? 57  ASP   A CG  1 
ATOM   337  O OD1 . ASP   A 1 50  ? -8.07376  42.84444 25.06497 1.000 60.27034  ? 57  ASP   A OD1 1 
ATOM   338  O OD2 . ASP   A 1 50  ? -6.23445  43.36771 26.14162 1.000 52.14227  ? 57  ASP   A OD2 1 
ATOM   339  N N   . LYS   A 1 51  ? -5.11544  41.85381 20.97246 1.000 44.95574  ? 58  LYS   A N   1 
ATOM   340  C CA  . LYS   A 1 51  ? -4.45192  42.22430 19.72395 1.000 43.89246  ? 58  LYS   A CA  1 
ATOM   341  C C   . LYS   A 1 51  ? -5.28743  41.83856 18.50961 1.000 48.72422  ? 58  LYS   A C   1 
ATOM   342  O O   . LYS   A 1 51  ? -5.42526  42.63253 17.57159 1.000 42.36334  ? 58  LYS   A O   1 
ATOM   343  C CB  . LYS   A 1 51  ? -3.06395  41.58834 19.64105 1.000 35.54726  ? 58  LYS   A CB  1 
ATOM   344  C CG  . LYS   A 1 51  ? -2.38008  41.40799 20.98046 1.000 60.44744  ? 58  LYS   A CG  1 
ATOM   345  C CD  . LYS   A 1 51  ? -0.95459  41.94194 20.98412 1.000 81.13454  ? 58  LYS   A CD  1 
ATOM   346  C CE  . LYS   A 1 51  ? -0.23426  41.55620 22.27495 1.000 70.05115  ? 58  LYS   A CE  1 
ATOM   347  N NZ  . LYS   A 1 51  ? 1.20337   41.21130 22.06931 1.000 68.20576  ? 58  LYS   A NZ  1 
ATOM   348  N N   . ILE   A 1 52  ? -5.85357  40.63004 18.49771 1.000 40.31999  ? 59  ILE   A N   1 
ATOM   349  C CA  . ILE   A 1 52  ? -6.65414  40.23872 17.34111 1.000 45.73152  ? 59  ILE   A CA  1 
ATOM   350  C C   . ILE   A 1 52  ? -7.93203  41.06563 17.27631 1.000 41.11640  ? 59  ILE   A C   1 
ATOM   351  O O   . ILE   A 1 52  ? -8.36121  41.48197 16.19367 1.000 42.86200  ? 59  ILE   A O   1 
ATOM   352  C CB  . ILE   A 1 52  ? -6.94168  38.72365 17.34794 1.000 42.95052  ? 59  ILE   A CB  1 
ATOM   353  C CG1 . ILE   A 1 52  ? -7.63514  38.31778 16.04639 1.000 35.59952  ? 59  ILE   A CG1 1 
ATOM   354  C CG2 . ILE   A 1 52  ? -7.77213  38.30936 18.55761 1.000 38.74295  ? 59  ILE   A CG2 1 
ATOM   355  C CD1 . ILE   A 1 52  ? -6.82755  38.63787 14.80239 1.000 40.21600  ? 59  ILE   A CD1 1 
ATOM   356  N N   . ARG   A 1 53  ? -8.54210  41.34725 18.42976 1.000 37.71260  ? 60  ARG   A N   1 
ATOM   357  C CA  . ARG   A 1 53  ? -9.74430  42.17126 18.43489 1.000 44.80156  ? 60  ARG   A CA  1 
ATOM   358  C C   . ARG   A 1 53  ? -9.45270  43.56942 17.90010 1.000 51.73710  ? 60  ARG   A C   1 
ATOM   359  O O   . ARG   A 1 53  ? -10.22960 44.11333 17.10594 1.000 47.50482  ? 60  ARG   A O   1 
ATOM   360  C CB  . ARG   A 1 53  ? -10.32788 42.24119 19.84511 1.000 42.27520  ? 60  ARG   A CB  1 
ATOM   361  C CG  . ARG   A 1 53  ? -11.32569 43.35750 20.01707 1.000 52.85746  ? 60  ARG   A CG  1 
ATOM   362  C CD  . ARG   A 1 53  ? -12.32600 43.08383 21.11579 1.000 60.14004  ? 60  ARG   A CD  1 
ATOM   363  N NE  . ARG   A 1 53  ? -13.61598 43.67833 20.78619 1.000 80.40180  ? 60  ARG   A NE  1 
ATOM   364  C CZ  . ARG   A 1 53  ? -14.24468 44.57400 21.53625 1.000 76.38954  ? 60  ARG   A CZ  1 
ATOM   365  N NH1 . ARG   A 1 53  ? -13.73312 45.00116 22.68143 1.000 71.81740  ? 60  ARG   A NH1 1 
ATOM   366  N NH2 . ARG   A 1 53  ? -15.41162 45.06110 21.12240 1.000 70.67535  ? 60  ARG   A NH2 1 
ATOM   367  N N   . TYR   A 1 54  ? -8.32182  44.15500 18.30389 1.000 49.92817  ? 61  TYR   A N   1 
ATOM   368  C CA  . TYR   A 1 54  ? -7.95762  45.48700 17.82937 1.000 52.57061  ? 61  TYR   A CA  1 
ATOM   369  C C   . TYR   A 1 54  ? -7.70533  45.48751 16.32490 1.000 46.68203  ? 61  TYR   A C   1 
ATOM   370  O O   . TYR   A 1 54  ? -8.18741  46.36882 15.60150 1.000 44.97294  ? 61  TYR   A O   1 
ATOM   371  C CB  . TYR   A 1 54  ? -6.72532  45.98559 18.58249 1.000 47.37695  ? 61  TYR   A CB  1 
ATOM   372  C CG  . TYR   A 1 54  ? -6.16313  47.27396 18.03304 1.000 43.15521  ? 61  TYR   A CG  1 
ATOM   373  C CD1 . TYR   A 1 54  ? -6.73834  48.49582 18.35511 1.000 45.53342  ? 61  TYR   A CD1 1 
ATOM   374  C CD2 . TYR   A 1 54  ? -5.05054  47.26972 17.19890 1.000 41.41154  ? 61  TYR   A CD2 1 
ATOM   375  C CE1 . TYR   A 1 54  ? -6.22356  49.68434 17.85672 1.000 40.14218  ? 61  TYR   A CE1 1 
ATOM   376  C CE2 . TYR   A 1 54  ? -4.53010  48.44711 16.69510 1.000 44.87283  ? 61  TYR   A CE2 1 
ATOM   377  C CZ  . TYR   A 1 54  ? -5.11947  49.65399 17.03006 1.000 37.13216  ? 61  TYR   A CZ  1 
ATOM   378  O OH  . TYR   A 1 54  ? -4.60502  50.83125 16.52896 1.000 47.15382  ? 61  TYR   A OH  1 
ATOM   379  N N   . GLU   A 1 55  ? -6.93908  44.50587 15.83872 1.000 49.78156  ? 62  GLU   A N   1 
ATOM   380  C CA  . GLU   A 1 55  ? -6.68217  44.39225 14.40470 1.000 45.26261  ? 62  GLU   A CA  1 
ATOM   381  C C   . GLU   A 1 55  ? -7.98003  44.26180 13.61925 1.000 54.02083  ? 62  GLU   A C   1 
ATOM   382  O O   . GLU   A 1 55  ? -8.11241  44.82088 12.52260 1.000 49.61767  ? 62  GLU   A O   1 
ATOM   383  C CB  . GLU   A 1 55  ? -5.77447  43.19273 14.12647 1.000 42.89343  ? 62  GLU   A CB  1 
ATOM   384  C CG  . GLU   A 1 55  ? -4.33305  43.38550 14.57528 1.000 49.97979  ? 62  GLU   A CG  1 
ATOM   385  C CD  . GLU   A 1 55  ? -3.37575  42.38407 13.94891 1.000 68.27463  ? 62  GLU   A CD  1 
ATOM   386  O OE1 . GLU   A 1 55  ? -3.84538  41.46480 13.24220 1.000 71.31745  ? 62  GLU   A OE1 1 
ATOM   387  O OE2 . GLU   A 1 55  ? -2.15078  42.52399 14.15647 1.000 62.92467  ? 62  GLU   A OE2 1 
ATOM   388  N N   . SER   A 1 56  ? -8.95269  43.53272 14.17195 1.000 42.60865  ? 63  SER   A N   1 
ATOM   389  C CA  . SER   A 1 56  ? -10.22215 43.31089 13.49116 1.000 47.89412  ? 63  SER   A CA  1 
ATOM   390  C C   . SER   A 1 56  ? -11.06964 44.57242 13.40609 1.000 54.69960  ? 63  SER   A C   1 
ATOM   391  O O   . SER   A 1 56  ? -12.00990 44.61632 12.60584 1.000 49.37435  ? 63  SER   A O   1 
ATOM   392  C CB  . SER   A 1 56  ? -11.00610 42.20717 14.20278 1.000 43.23775  ? 63  SER   A CB  1 
ATOM   393  O OG  . SER   A 1 56  ? -11.76024 42.73923 15.27716 1.000 46.45170  ? 63  SER   A OG  1 
ATOM   394  N N   . LEU   A 1 57  ? -10.76410 45.59550 14.20926 1.000 56.71355  ? 64  LEU   A N   1 
ATOM   395  C CA  . LEU   A 1 57  ? -11.54668 46.82581 14.15817 1.000 55.89530  ? 64  LEU   A CA  1 
ATOM   396  C C   . LEU   A 1 57  ? -11.35025 47.56750 12.84101 1.000 59.60902  ? 64  LEU   A C   1 
ATOM   397  O O   . LEU   A 1 57  ? -12.24733 48.29826 12.40573 1.000 58.00993  ? 64  LEU   A O   1 
ATOM   398  C CB  . LEU   A 1 57  ? -11.18944 47.73067 15.33715 1.000 50.40664  ? 64  LEU   A CB  1 
ATOM   399  C CG  . LEU   A 1 57  ? -11.49716 47.18965 16.73374 1.000 58.21862  ? 64  LEU   A CG  1 
ATOM   400  C CD1 . LEU   A 1 57  ? -11.27154 48.26697 17.78586 1.000 56.91225  ? 64  LEU   A CD1 1 
ATOM   401  C CD2 . LEU   A 1 57  ? -12.91857 46.65787 16.79813 1.000 46.86501  ? 64  LEU   A CD2 1 
ATOM   402  N N   . THR   A 1 58  ? -10.19456 47.40248 12.19745 1.000 58.91923  ? 65  THR   A N   1 
ATOM   403  C CA  . THR   A 1 58  ? -9.94918  47.97780 10.88122 1.000 60.84545  ? 65  THR   A CA  1 
ATOM   404  C C   . THR   A 1 58  ? -9.94438  46.93261 9.77498  1.000 65.30808  ? 65  THR   A C   1 
ATOM   405  O O   . THR   A 1 58  ? -9.84725  47.29826 8.59856  1.000 58.36049  ? 65  THR   A O   1 
ATOM   406  C CB  . THR   A 1 58  ? -8.61949  48.74297 10.86319 1.000 55.85568  ? 65  THR   A CB  1 
ATOM   407  O OG1 . THR   A 1 58  ? -7.54863  47.85123 11.19343 1.000 62.23382  ? 65  THR   A OG1 1 
ATOM   408  C CG2 . THR   A 1 58  ? -8.64633  49.89396 11.85691 1.000 47.44362  ? 65  THR   A CG2 1 
ATOM   409  N N   . ASP   A 1 59  ? -10.04496 45.65030 10.11675 1.000 65.72534  ? 66  ASP   A N   1 
ATOM   410  C CA  . ASP   A 1 59  ? -10.04791 44.57793 9.12121  1.000 66.12875  ? 66  ASP   A CA  1 
ATOM   411  C C   . ASP   A 1 59  ? -10.85742 43.41767 9.67287  1.000 63.38809  ? 66  ASP   A C   1 
ATOM   412  O O   . ASP   A 1 59  ? -10.31707 42.51355 10.32771 1.000 60.42059  ? 66  ASP   A O   1 
ATOM   413  C CB  . ASP   A 1 59  ? -8.63079  44.13416 8.76377  1.000 60.65676  ? 66  ASP   A CB  1 
ATOM   414  C CG  . ASP   A 1 59  ? -8.60427  43.13890 7.61805  1.000 69.17609  ? 66  ASP   A CG  1 
ATOM   415  O OD1 . ASP   A 1 59  ? -9.67141  42.89792 7.00777  1.000 62.34314  ? 66  ASP   A OD1 1 
ATOM   416  O OD2 . ASP   A 1 59  ? -7.51517  42.60183 7.32568  1.000 78.56042  ? 66  ASP   A OD2 1 
ATOM   417  N N   . PRO   A 1 60  ? -12.16885 43.40376 9.43045  1.000 59.67667  ? 67  PRO   A N   1 
ATOM   418  C CA  . PRO   A 1 60  ? -13.00340 42.31783 9.96522  1.000 57.81732  ? 67  PRO   A CA  1 
ATOM   419  C C   . PRO   A 1 60  ? -12.64708 40.94481 9.41799  1.000 61.16231  ? 67  PRO   A C   1 
ATOM   420  O O   . PRO   A 1 60  ? -12.98932 39.93795 10.05147 1.000 57.95032  ? 67  PRO   A O   1 
ATOM   421  C CB  . PRO   A 1 60  ? -14.42436 42.73453 9.55769  1.000 60.95995  ? 67  PRO   A CB  1 
ATOM   422  C CG  . PRO   A 1 60  ? -14.33420 44.20976 9.31618  1.000 55.14134  ? 67  PRO   A CG  1 
ATOM   423  C CD  . PRO   A 1 60  ? -12.97182 44.42818 8.74234  1.000 57.50024  ? 67  PRO   A CD  1 
ATOM   424  N N   . SER   A 1 61  ? -11.96696 40.87039 8.26907  1.000 53.92216  ? 68  SER   A N   1 
ATOM   425  C CA  . SER   A 1 61  ? -11.56419 39.58362 7.70976  1.000 65.22446  ? 68  SER   A CA  1 
ATOM   426  C C   . SER   A 1 61  ? -10.56582 38.84547 8.59433  1.000 64.51503  ? 68  SER   A C   1 
ATOM   427  O O   . SER   A 1 61  ? -10.37752 37.63718 8.41728  1.000 57.02847  ? 68  SER   A O   1 
ATOM   428  C CB  . SER   A 1 61  ? -10.96214 39.77535 6.31693  1.000 60.23574  ? 68  SER   A CB  1 
ATOM   429  O OG  . SER   A 1 61  ? -9.63114  40.25820 6.40120  1.000 66.38820  ? 68  SER   A OG  1 
ATOM   430  N N   . LYS   A 1 62  ? -9.91887  39.53808 9.53476  1.000 50.26661  ? 69  LYS   A N   1 
ATOM   431  C CA  . LYS   A 1 62  ? -8.99768  38.87666 10.44983 1.000 49.56393  ? 69  LYS   A CA  1 
ATOM   432  C C   . LYS   A 1 62  ? -9.70134  37.89757 11.37965 1.000 53.86580  ? 69  LYS   A C   1 
ATOM   433  O O   . LYS   A 1 62  ? -9.02714  37.09896 12.04245 1.000 48.91267  ? 69  LYS   A O   1 
ATOM   434  C CB  . LYS   A 1 62  ? -8.23746  39.91985 11.27116 1.000 47.49999  ? 69  LYS   A CB  1 
ATOM   435  C CG  . LYS   A 1 62  ? -7.48619  40.92635 10.42700 1.000 58.28194  ? 69  LYS   A CG  1 
ATOM   436  C CD  . LYS   A 1 62  ? -6.04727  41.06529 10.87789 1.000 53.09492  ? 69  LYS   A CD  1 
ATOM   437  C CE  . LYS   A 1 62  ? -5.21248  41.74528 9.80401  1.000 58.07414  ? 69  LYS   A CE  1 
ATOM   438  N NZ  . LYS   A 1 62  ? -3.75146  41.61506 10.05137 1.000 61.97850  ? 69  LYS   A NZ  1 
ATOM   439  N N   . LEU   A 1 63  ? -11.02964 37.93558 11.43987 1.000 42.89604  ? 70  LEU   A N   1 
ATOM   440  C CA  . LEU   A 1 63  ? -11.80455 37.05086 12.29442 1.000 45.59089  ? 70  LEU   A CA  1 
ATOM   441  C C   . LEU   A 1 63  ? -12.43073 35.89754 11.52602 1.000 53.13816  ? 70  LEU   A C   1 
ATOM   442  O O   . LEU   A 1 63  ? -13.14010 35.08435 12.12658 1.000 53.60765  ? 70  LEU   A O   1 
ATOM   443  C CB  . LEU   A 1 63  ? -12.89149 37.84853 13.01865 1.000 51.29634  ? 70  LEU   A CB  1 
ATOM   444  C CG  . LEU   A 1 63  ? -12.37233 38.74406 14.14436 1.000 53.66461  ? 70  LEU   A CG  1 
ATOM   445  C CD1 . LEU   A 1 63  ? -13.52228 39.27828 14.96474 1.000 48.07175  ? 70  LEU   A CD1 1 
ATOM   446  C CD2 . LEU   A 1 63  ? -11.39890 37.97828 15.02519 1.000 44.79272  ? 70  LEU   A CD2 1 
ATOM   447  N N   . ASP   A 1 64  ? -12.18139 35.80646 10.21565 1.000 49.84721  ? 71  ASP   A N   1 
ATOM   448  C CA  . ASP   A 1 64  ? -12.69237 34.68288 9.43566  1.000 61.39113  ? 71  ASP   A CA  1 
ATOM   449  C C   . ASP   A 1 64  ? -12.19583 33.35372 9.98238  1.000 56.32468  ? 71  ASP   A C   1 
ATOM   450  O O   . ASP   A 1 64  ? -12.87626 32.33203 9.84389  1.000 63.17637  ? 71  ASP   A O   1 
ATOM   451  C CB  . ASP   A 1 64  ? -12.28932 34.82833 7.96854  1.000 52.61567  ? 71  ASP   A CB  1 
ATOM   452  C CG  . ASP   A 1 64  ? -12.94640 36.01763 7.29850  1.000 73.77302  ? 71  ASP   A CG  1 
ATOM   453  O OD1 . ASP   A 1 64  ? -13.86621 36.61300 7.90142  1.000 72.82273  ? 71  ASP   A OD1 1 
ATOM   454  O OD2 . ASP   A 1 64  ? -12.54054 36.35566 6.16715  1.000 67.88067  ? 71  ASP   A OD2 1 
ATOM   455  N N   . SER   A 1 65  ? -11.02142 33.34781 10.60605 1.000 55.88393  ? 72  SER   A N   1 
ATOM   456  C CA  . SER   A 1 65  ? -10.49703 32.15867 11.25981 1.000 52.05592  ? 72  SER   A CA  1 
ATOM   457  C C   . SER   A 1 65  ? -11.17643 31.86667 12.59171 1.000 57.31528  ? 72  SER   A C   1 
ATOM   458  O O   . SER   A 1 65  ? -10.82902 30.87295 13.23746 1.000 54.01369  ? 72  SER   A O   1 
ATOM   459  C CB  . SER   A 1 65  ? -8.99028  32.30960 11.47376 1.000 58.53245  ? 72  SER   A CB  1 
ATOM   460  O OG  . SER   A 1 65  ? -8.67725  33.61134 11.94316 1.000 48.50425  ? 72  SER   A OG  1 
ATOM   461  N N   . GLY   A 1 66  ? -12.12473 32.69958 13.01755 1.000 51.16908  ? 73  GLY   A N   1 
ATOM   462  C CA  . GLY   A 1 66  ? -12.78800 32.51353 14.29303 1.000 53.78280  ? 73  GLY   A CA  1 
ATOM   463  C C   . GLY   A 1 66  ? -13.25470 33.81689 14.91159 1.000 66.54723  ? 73  GLY   A C   1 
ATOM   464  O O   . GLY   A 1 66  ? -12.44051 34.69310 15.22100 1.000 60.19122  ? 73  GLY   A O   1 
ATOM   465  N N   . LYS   A 1 67  ? -14.56781 33.95189 15.10169 1.000 56.43399  ? 74  LYS   A N   1 
ATOM   466  C CA  . LYS   A 1 67  ? -15.15856 35.16036 15.66414 1.000 58.88874  ? 74  LYS   A CA  1 
ATOM   467  C C   . LYS   A 1 67  ? -15.17678 35.15248 17.18751 1.000 58.87211  ? 74  LYS   A C   1 
ATOM   468  O O   . LYS   A 1 67  ? -15.16542 36.22416 17.80368 1.000 52.36267  ? 74  LYS   A O   1 
ATOM   469  C CB  . LYS   A 1 67  ? -16.59328 35.35463 15.14811 1.000 61.91706  ? 74  LYS   A CB  1 
ATOM   470  C CG  . LYS   A 1 67  ? -16.78299 35.40992 13.62246 1.000 74.23858  ? 74  LYS   A CG  1 
ATOM   471  C CD  . LYS   A 1 67  ? -16.59282 34.05924 12.92614 1.000 91.92826  ? 74  LYS   A CD  1 
ATOM   472  C CE  . LYS   A 1 67  ? -17.54910 33.00235 13.47662 1.000 87.40423  ? 74  LYS   A CE  1 
ATOM   473  N NZ  . LYS   A 1 67  ? -17.11475 31.62187 13.10420 1.000 79.53914  ? 74  LYS   A NZ  1 
ATOM   474  N N   . GLU   A 1 68  ? -15.20031 33.97477 17.80710 1.000 54.62890  ? 75  GLU   A N   1 
ATOM   475  C CA  . GLU   A 1 68  ? -15.28201 33.88571 19.25957 1.000 46.32725  ? 75  GLU   A CA  1 
ATOM   476  C C   . GLU   A 1 68  ? -13.95604 34.28167 19.90264 1.000 46.48546  ? 75  GLU   A C   1 
ATOM   477  O O   . GLU   A 1 68  ? -12.88092 33.86524 19.46219 1.000 54.96973  ? 75  GLU   A O   1 
ATOM   478  C CB  . GLU   A 1 68  ? -15.66303 32.46566 19.70399 1.000 54.32160  ? 75  GLU   A CB  1 
ATOM   479  C CG  . GLU   A 1 68  ? -16.93571 31.84607 19.09247 1.000 52.37484  ? 75  GLU   A CG  1 
ATOM   480  C CD  . GLU   A 1 68  ? -16.89038 31.68751 17.57949 1.000 81.97295  ? 75  GLU   A CD  1 
ATOM   481  O OE1 . GLU   A 1 68  ? -15.83193 31.29301 17.04280 1.000 82.32641  ? 75  GLU   A OE1 1 
ATOM   482  O OE2 . GLU   A 1 68  ? -17.91547 31.97276 16.92460 1.000 98.44274  ? 75  GLU   A OE2 1 
ATOM   483  N N   . LEU   A 1 69  ? -14.03926 35.08096 20.96234 1.000 47.27861  ? 76  LEU   A N   1 
ATOM   484  C CA  . LEU   A 1 69  ? -12.87537 35.54058 21.71779 1.000 45.81587  ? 76  LEU   A CA  1 
ATOM   485  C C   . LEU   A 1 69  ? -13.06856 35.09562 23.16342 1.000 49.85548  ? 76  LEU   A C   1 
ATOM   486  O O   . LEU   A 1 69  ? -13.78218 35.75050 23.92967 1.000 51.98813  ? 76  LEU   A O   1 
ATOM   487  C CB  . LEU   A 1 69  ? -12.71865 37.05493 21.60993 1.000 41.15765  ? 76  LEU   A CB  1 
ATOM   488  C CG  . LEU   A 1 69  ? -12.67375 37.60901 20.18473 1.000 42.64951  ? 76  LEU   A CG  1 
ATOM   489  C CD1 . LEU   A 1 69  ? -12.44837 39.11425 20.20172 1.000 45.93685  ? 76  LEU   A CD1 1 
ATOM   490  C CD2 . LEU   A 1 69  ? -11.59625 36.91105 19.36017 1.000 44.66341  ? 76  LEU   A CD2 1 
ATOM   491  N N   . HIS   A 1 70  ? -12.44373 33.98073 23.53811 1.000 42.25741  ? 77  HIS   A N   1 
ATOM   492  C CA  . HIS   A 1 70  ? -12.67192 33.40433 24.85404 1.000 46.89091  ? 77  HIS   A CA  1 
ATOM   493  C C   . HIS   A 1 70  ? -11.43506 32.64343 25.30689 1.000 47.46916  ? 77  HIS   A C   1 
ATOM   494  O O   . HIS   A 1 70  ? -10.50260 32.40235 24.53424 1.000 40.71083  ? 77  HIS   A O   1 
ATOM   495  C CB  . HIS   A 1 70  ? -13.90319 32.48732 24.85593 1.000 42.70114  ? 77  HIS   A CB  1 
ATOM   496  C CG  . HIS   A 1 70  ? -13.84413 31.38586 23.84310 1.000 37.34210  ? 77  HIS   A CG  1 
ATOM   497  N ND1 . HIS   A 1 70  ? -14.77603 31.25262 22.83550 1.000 52.36982  ? 77  HIS   A ND1 1 
ATOM   498  C CD2 . HIS   A 1 70  ? -12.97181 30.36270 23.68434 1.000 45.02145  ? 77  HIS   A CD2 1 
ATOM   499  C CE1 . HIS   A 1 70  ? -14.47989 30.19601 22.10028 1.000 43.21954  ? 77  HIS   A CE1 1 
ATOM   500  N NE2 . HIS   A 1 70  ? -13.38839 29.63936 22.59295 1.000 47.63355  ? 77  HIS   A NE2 1 
ATOM   501  N N   . ILE   A 1 71  ? -11.44533 32.26634 26.58317 1.000 44.97898  ? 78  ILE   A N   1 
ATOM   502  C CA  . ILE   A 1 71  ? -10.39665 31.46139 27.19592 1.000 44.37253  ? 78  ILE   A CA  1 
ATOM   503  C C   . ILE   A 1 71  ? -11.05109 30.23248 27.80771 1.000 43.34842  ? 78  ILE   A C   1 
ATOM   504  O O   . ILE   A 1 71  ? -12.03273 30.35416 28.54980 1.000 46.62917  ? 78  ILE   A O   1 
ATOM   505  C CB  . ILE   A 1 71  ? -9.61891  32.25846 28.25937 1.000 49.45364  ? 78  ILE   A CB  1 
ATOM   506  C CG1 . ILE   A 1 71  ? -9.08845  33.56016 27.65654 1.000 43.87870  ? 78  ILE   A CG1 1 
ATOM   507  C CG2 . ILE   A 1 71  ? -8.48130  31.42007 28.83081 1.000 40.53443  ? 78  ILE   A CG2 1 
ATOM   508  C CD1 . ILE   A 1 71  ? -8.59382  34.56023 28.67976 1.000 42.95154  ? 78  ILE   A CD1 1 
ATOM   509  N N   . ASN   A 1 72  ? -10.52519 29.05472 27.48020 1.000 46.99162  ? 79  ASN   A N   1 
ATOM   510  C CA  . ASN   A 1 72  ? -11.00087 27.79651 28.03814 1.000 45.17021  ? 79  ASN   A CA  1 
ATOM   511  C C   . ASN   A 1 72  ? -9.93217  27.18315 28.93040 1.000 43.51087  ? 79  ASN   A C   1 
ATOM   512  O O   . ASN   A 1 72  ? -8.74885  27.16117 28.57549 1.000 49.58470  ? 79  ASN   A O   1 
ATOM   513  C CB  . ASN   A 1 72  ? -11.37400 26.79808 26.93928 1.000 47.30058  ? 79  ASN   A CB  1 
ATOM   514  C CG  . ASN   A 1 72  ? -12.63409 27.18775 26.19957 1.000 50.55884  ? 79  ASN   A CG  1 
ATOM   515  O OD1 . ASN   A 1 72  ? -13.44634 27.97114 26.69794 1.000 43.13182  ? 79  ASN   A OD1 1 
ATOM   516  N ND2 . ASN   A 1 72  ? -12.81477 26.62809 25.00637 1.000 48.12953  ? 79  ASN   A ND2 1 
ATOM   517  N N   . LEU   A 1 73  ? -10.35712 26.68536 30.08715 1.000 45.75233  ? 80  LEU   A N   1 
ATOM   518  C CA  . LEU   A 1 73  ? -9.48982  25.96888 31.01208 1.000 48.21877  ? 80  LEU   A CA  1 
ATOM   519  C C   . LEU   A 1 73  ? -9.91279  24.50649 31.02171 1.000 48.48841  ? 80  LEU   A C   1 
ATOM   520  O O   . LEU   A 1 73  ? -11.05524 24.19205 31.37158 1.000 51.62428  ? 80  LEU   A O   1 
ATOM   521  C CB  . LEU   A 1 73  ? -9.57417  26.57015 32.41344 1.000 41.66045  ? 80  LEU   A CB  1 
ATOM   522  C CG  . LEU   A 1 73  ? -9.33989  28.07640 32.54239 1.000 45.22984  ? 80  LEU   A CG  1 
ATOM   523  C CD1 . LEU   A 1 73  ? -9.40010  28.49620 34.00325 1.000 47.90507  ? 80  LEU   A CD1 1 
ATOM   524  C CD2 . LEU   A 1 73  ? -8.01062  28.48939 31.91918 1.000 41.63289  ? 80  LEU   A CD2 1 
ATOM   525  N N   . ILE   A 1 74  ? -9.00007  23.61854 30.63898 1.000 46.27657  ? 81  ILE   A N   1 
ATOM   526  C CA  . ILE   A 1 74  ? -9.34573  22.21231 30.44046 1.000 44.46813  ? 81  ILE   A CA  1 
ATOM   527  C C   . ILE   A 1 74  ? -8.43335  21.31711 31.27186 1.000 49.74586  ? 81  ILE   A C   1 
ATOM   528  O O   . ILE   A 1 74  ? -7.32842  20.97445 30.82479 1.000 48.88400  ? 81  ILE   A O   1 
ATOM   529  C CB  . ILE   A 1 74  ? -9.27207  21.83156 28.95328 1.000 44.05759  ? 81  ILE   A CB  1 
ATOM   530  C CG1 . ILE   A 1 74  ? -10.07834 22.81970 28.10910 1.000 43.46674  ? 81  ILE   A CG1 1 
ATOM   531  C CG2 . ILE   A 1 74  ? -9.79784  20.42441 28.74031 1.000 42.24180  ? 81  ILE   A CG2 1 
ATOM   532  C CD1 . ILE   A 1 74  ? -9.86464  22.66960 26.62484 1.000 49.58135  ? 81  ILE   A CD1 1 
ATOM   533  N N   . PRO   A 1 75  ? -8.84367  20.91720 32.47282 1.000 46.25852  ? 82  PRO   A N   1 
ATOM   534  C CA  . PRO   A 1 75  ? -8.05935  19.94520 33.23752 1.000 44.55980  ? 82  PRO   A CA  1 
ATOM   535  C C   . PRO   A 1 75  ? -8.32668  18.52164 32.77882 1.000 55.76955  ? 82  PRO   A C   1 
ATOM   536  O O   . PRO   A 1 75  ? -9.41832  18.18238 32.31577 1.000 56.95841  ? 82  PRO   A O   1 
ATOM   537  C CB  . PRO   A 1 75  ? -8.55154  20.15497 34.67284 1.000 53.52652  ? 82  PRO   A CB  1 
ATOM   538  C CG  . PRO   A 1 75  ? -9.97164  20.57478 34.49556 1.000 45.64642  ? 82  PRO   A CG  1 
ATOM   539  C CD  . PRO   A 1 75  ? -9.99830  21.41751 33.23992 1.000 53.84448  ? 82  PRO   A CD  1 
ATOM   540  N N   . ASN   A 1 76  ? -7.30553  17.67803 32.92757 1.000 58.23194  ? 83  ASN   A N   1 
ATOM   541  C CA  . ASN   A 1 76  ? -7.38443  16.27558 32.51889 1.000 53.14788  ? 83  ASN   A CA  1 
ATOM   542  C C   . ASN   A 1 76  ? -6.59931  15.44552 33.53059 1.000 62.59521  ? 83  ASN   A C   1 
ATOM   543  O O   . ASN   A 1 76  ? -5.36760  15.39581 33.47496 1.000 62.88408  ? 83  ASN   A O   1 
ATOM   544  C CB  . ASN   A 1 76  ? -6.84800  16.08840 31.10511 1.000 47.58100  ? 83  ASN   A CB  1 
ATOM   545  C CG  . ASN   A 1 76  ? -7.16246  14.71525 30.53947 1.000 56.81543  ? 83  ASN   A CG  1 
ATOM   546  O OD1 . ASN   A 1 76  ? -7.02248  13.70236 31.22051 1.000 61.12670  ? 83  ASN   A OD1 1 
ATOM   547  N ND2 . ASN   A 1 76  ? -7.59180  14.67817 29.28618 1.000 61.37098  ? 83  ASN   A ND2 1 
ATOM   548  N N   . LYS   A 1 77  ? -7.31510  14.77981 34.44126 1.000 53.84212  ? 84  LYS   A N   1 
ATOM   549  C CA  . LYS   A 1 77  ? -6.64519  14.02202 35.49424 1.000 63.03323  ? 84  LYS   A CA  1 
ATOM   550  C C   . LYS   A 1 77  ? -5.94876  12.78380 34.94235 1.000 68.82567  ? 84  LYS   A C   1 
ATOM   551  O O   . LYS   A 1 77  ? -4.85383  12.43314 35.39766 1.000 65.59375  ? 84  LYS   A O   1 
ATOM   552  C CB  . LYS   A 1 77  ? -7.64447  13.63159 36.58313 1.000 60.99953  ? 84  LYS   A CB  1 
ATOM   553  C CG  . LYS   A 1 77  ? -7.96564  14.75840 37.55738 1.000 61.59818  ? 84  LYS   A CG  1 
ATOM   554  C CD  . LYS   A 1 77  ? -8.65305  14.24512 38.81470 1.000 74.76714  ? 84  LYS   A CD  1 
ATOM   555  C CE  . LYS   A 1 77  ? -9.33735  15.37379 39.57313 1.000 75.12922  ? 84  LYS   A CE  1 
ATOM   556  N NZ  . LYS   A 1 77  ? -10.62403 15.77540 38.93637 1.000 82.83630  ? 84  LYS   A NZ  1 
ATOM   557  N N   . GLN   A 1 78  ? -6.56724  12.10473 33.96994 1.000 63.29388  ? 85  GLN   A N   1 
ATOM   558  C CA  . GLN   A 1 78  ? -5.97060  10.88794 33.42285 1.000 65.04428  ? 85  GLN   A CA  1 
ATOM   559  C C   . GLN   A 1 78  ? -4.61987  11.17115 32.77373 1.000 68.29449  ? 85  GLN   A C   1 
ATOM   560  O O   . GLN   A 1 78  ? -3.65642  10.42147 32.97230 1.000 65.19202  ? 85  GLN   A O   1 
ATOM   561  C CB  . GLN   A 1 78  ? -6.92407  10.23934 32.41943 1.000 74.89215  ? 85  GLN   A CB  1 
ATOM   562  C CG  . GLN   A 1 78  ? -8.09962  9.51288  33.05332 1.000 79.05010  ? 85  GLN   A CG  1 
ATOM   563  C CD  . GLN   A 1 78  ? -7.67159  8.47698  34.07838 1.000 105.94544 ? 85  GLN   A CD  1 
ATOM   564  O OE1 . GLN   A 1 78  ? -7.39077  7.32795  33.73614 1.000 103.73721 ? 85  GLN   A OE1 1 
ATOM   565  N NE2 . GLN   A 1 78  ? -7.62939  8.87758  35.34600 1.000 101.62650 ? 85  GLN   A NE2 1 
ATOM   566  N N   . ASP   A 1 79  ? -4.52806  12.24690 31.99771 1.000 55.46027  ? 86  ASP   A N   1 
ATOM   567  C CA  . ASP   A 1 79  ? -3.27235  12.64394 31.37555 1.000 64.29854  ? 86  ASP   A CA  1 
ATOM   568  C C   . ASP   A 1 79  ? -2.39859  13.49844 32.28469 1.000 60.07370  ? 86  ASP   A C   1 
ATOM   569  O O   . ASP   A 1 79  ? -1.22830  13.72402 31.95526 1.000 60.00727  ? 86  ASP   A O   1 
ATOM   570  C CB  . ASP   A 1 79  ? -3.54158  13.41631 30.07677 1.000 61.21007  ? 86  ASP   A CB  1 
ATOM   571  C CG  . ASP   A 1 79  ? -4.28677  12.58938 29.04495 1.000 63.58905  ? 86  ASP   A CG  1 
ATOM   572  O OD1 . ASP   A 1 79  ? -4.66251  11.43865 29.35393 1.000 77.52588  ? 86  ASP   A OD1 1 
ATOM   573  O OD2 . ASP   A 1 79  ? -4.49160  13.09132 27.91937 1.000 85.26355  ? 86  ASP   A OD2 1 
ATOM   574  N N   . ARG   A 1 80  ? -2.93841  13.97723 33.40602 1.000 59.19852  ? 87  ARG   A N   1 
ATOM   575  C CA  . ARG   A 1 80  ? -2.24497  14.90701 34.29951 1.000 61.02577  ? 87  ARG   A CA  1 
ATOM   576  C C   . ARG   A 1 80  ? -1.79216  16.16189 33.55312 1.000 50.09810  ? 87  ARG   A C   1 
ATOM   577  O O   . ARG   A 1 80  ? -0.65181  16.61390 33.67760 1.000 60.01397  ? 87  ARG   A O   1 
ATOM   578  C CB  . ARG   A 1 80  ? -1.06264  14.22986 34.99584 1.000 51.12760  ? 87  ARG   A CB  1 
ATOM   579  C CG  . ARG   A 1 80  ? -0.75577  14.80697 36.36688 1.000 61.44174  ? 87  ARG   A CG  1 
ATOM   580  C CD  . ARG   A 1 80  ? 0.08118   13.85506 37.19786 1.000 70.72545  ? 87  ARG   A CD  1 
ATOM   581  N NE  . ARG   A 1 80  ? 1.46846   13.83183 36.75279 1.000 71.57110  ? 87  ARG   A NE  1 
ATOM   582  C CZ  . ARG   A 1 80  ? 2.29723   12.81504 36.94114 1.000 77.33313  ? 87  ARG   A CZ  1 
ATOM   583  N NH1 . ARG   A 1 80  ? 1.91111   11.71685 37.57131 1.000 62.07481  ? 87  ARG   A NH1 1 
ATOM   584  N NH2 . ARG   A 1 80  ? 3.54518   12.90410 36.48937 1.000 70.98819  ? 87  ARG   A NH2 1 
ATOM   585  N N   . THR   A 1 81  ? -2.70242  16.73202 32.76513 1.000 49.10422  ? 88  THR   A N   1 
ATOM   586  C CA  . THR   A 1 81  ? -2.42030  17.95538 32.02804 1.000 52.48243  ? 88  THR   A CA  1 
ATOM   587  C C   . THR   A 1 81  ? -3.48562  19.00094 32.31341 1.000 56.93606  ? 88  THR   A C   1 
ATOM   588  O O   . THR   A 1 81  ? -4.66436  18.67540 32.47921 1.000 58.15014  ? 88  THR   A O   1 
ATOM   589  C CB  . THR   A 1 81  ? -2.34946  17.72428 30.50988 1.000 39.31237  ? 88  THR   A CB  1 
ATOM   590  O OG1 . THR   A 1 81  ? -3.61758  17.26077 30.03751 1.000 47.47080  ? 88  THR   A OG1 1 
ATOM   591  C CG2 . THR   A 1 81  ? -1.27583  16.71234 30.16223 1.000 43.00401  ? 88  THR   A CG2 1 
ATOM   592  N N   . LEU   A 1 82  ? -3.05493  20.25803 32.36842 1.000 55.75915  ? 89  LEU   A N   1 
ATOM   593  C CA  . LEU   A 1 82  ? -3.94107  21.41174 32.42641 1.000 43.00961  ? 89  LEU   A CA  1 
ATOM   594  C C   . LEU   A 1 82  ? -3.71432  22.22395 31.16118 1.000 48.80139  ? 89  LEU   A C   1 
ATOM   595  O O   . LEU   A 1 82  ? -2.57890  22.61667 30.86767 1.000 51.63372  ? 89  LEU   A O   1 
ATOM   596  C CB  . LEU   A 1 82  ? -3.67304  22.25839 33.66990 1.000 50.63673  ? 89  LEU   A CB  1 
ATOM   597  C CG  . LEU   A 1 82  ? -4.52759  23.51930 33.80392 1.000 47.69693  ? 89  LEU   A CG  1 
ATOM   598  C CD1 . LEU   A 1 82  ? -6.00467  23.16391 33.71780 1.000 47.40528  ? 89  LEU   A CD1 1 
ATOM   599  C CD2 . LEU   A 1 82  ? -4.21794  24.22802 35.11051 1.000 49.12554  ? 89  LEU   A CD2 1 
ATOM   600  N N   . THR   A 1 83  ? -4.78345  22.46376 30.40842 1.000 38.55628  ? 90  THR   A N   1 
ATOM   601  C CA  . THR   A 1 83  ? -4.69062  23.12249 29.11387 1.000 50.58987  ? 90  THR   A CA  1 
ATOM   602  C C   . THR   A 1 83  ? -5.41481  24.46148 29.16231 1.000 45.75105  ? 90  THR   A C   1 
ATOM   603  O O   . THR   A 1 83  ? -6.58351  24.52540 29.55976 1.000 47.17954  ? 90  THR   A O   1 
ATOM   604  C CB  . THR   A 1 83  ? -5.27198  22.23488 28.00938 1.000 42.51554  ? 90  THR   A CB  1 
ATOM   605  O OG1 . THR   A 1 83  ? -4.46214  21.06192 27.86077 1.000 51.44978  ? 90  THR   A OG1 1 
ATOM   606  C CG2 . THR   A 1 83  ? -5.29788  22.98191 26.69852 1.000 38.82252  ? 90  THR   A CG2 1 
ATOM   607  N N   . ILE   A 1 84  ? -4.71584  25.52407 28.76566 1.000 48.48990  ? 91  ILE   A N   1 
ATOM   608  C CA  . ILE   A 1 84  ? -5.27794  26.86895 28.66761 1.000 47.04783  ? 91  ILE   A CA  1 
ATOM   609  C C   . ILE   A 1 84  ? -5.39036  27.19694 27.18292 1.000 47.45349  ? 91  ILE   A C   1 
ATOM   610  O O   . ILE   A 1 84  ? -4.37206  27.34206 26.49469 1.000 44.19850  ? 91  ILE   A O   1 
ATOM   611  C CB  . ILE   A 1 84  ? -4.41999  27.91783 29.39438 1.000 35.75677  ? 91  ILE   A CB  1 
ATOM   612  C CG1 . ILE   A 1 84  ? -4.49527  27.76997 30.91899 1.000 50.84111  ? 91  ILE   A CG1 1 
ATOM   613  C CG2 . ILE   A 1 84  ? -4.85924  29.32105 29.00762 1.000 46.54945  ? 91  ILE   A CG2 1 
ATOM   614  C CD1 . ILE   A 1 84  ? -3.71097  26.60354 31.49786 1.000 61.47211  ? 91  ILE   A CD1 1 
ATOM   615  N N   . VAL   A 1 85  ? -6.62015  27.30844 26.68181 1.000 39.54577  ? 92  VAL   A N   1 
ATOM   616  C CA  . VAL   A 1 85  ? -6.88511  27.60220 25.27705 1.000 35.41608  ? 92  VAL   A CA  1 
ATOM   617  C C   . VAL   A 1 85  ? -7.40718  29.02597 25.16883 1.000 49.33132  ? 92  VAL   A C   1 
ATOM   618  O O   . VAL   A 1 85  ? -8.24998  29.44861 25.96790 1.000 50.28564  ? 92  VAL   A O   1 
ATOM   619  C CB  . VAL   A 1 85  ? -7.89970  26.61658 24.66037 1.000 43.90759  ? 92  VAL   A CB  1 
ATOM   620  C CG1 . VAL   A 1 85  ? -7.87619  26.70561 23.13622 1.000 39.31591  ? 92  VAL   A CG1 1 
ATOM   621  C CG2 . VAL   A 1 85  ? -7.62633  25.19747 25.11727 1.000 45.99133  ? 92  VAL   A CG2 1 
ATOM   622  N N   . ASP   A 1 86  ? -6.91382  29.76305 24.17672 1.000 38.34350  ? 93  ASP   A N   1 
ATOM   623  C CA  . ASP   A 1 86  ? -7.46990  31.06716 23.84534 1.000 43.28557  ? 93  ASP   A CA  1 
ATOM   624  C C   . ASP   A 1 86  ? -7.56917  31.17623 22.32819 1.000 42.44533  ? 93  ASP   A C   1 
ATOM   625  O O   . ASP   A 1 86  ? -6.85463  30.49419 21.59001 1.000 36.32995  ? 93  ASP   A O   1 
ATOM   626  C CB  . ASP   A 1 86  ? -6.63311  32.20353 24.47672 1.000 40.44968  ? 93  ASP   A CB  1 
ATOM   627  C CG  . ASP   A 1 86  ? -5.32780  32.48944 23.72985 1.000 51.66774  ? 93  ASP   A CG  1 
ATOM   628  O OD1 . ASP   A 1 86  ? -5.36342  32.83801 22.52869 1.000 43.19576  ? 93  ASP   A OD1 1 
ATOM   629  O OD2 . ASP   A 1 86  ? -4.24881  32.32260 24.34558 1.000 53.10570  ? 93  ASP   A OD2 1 
ATOM   630  N N   . THR   A 1 87  ? -8.48698  32.02245 21.86472 1.000 44.28841  ? 94  THR   A N   1 
ATOM   631  C CA  . THR   A 1 87  ? -8.66838  32.28443 20.43765 1.000 41.47749  ? 94  THR   A CA  1 
ATOM   632  C C   . THR   A 1 87  ? -8.05473  33.62062 20.03800 1.000 44.69738  ? 94  THR   A C   1 
ATOM   633  O O   . THR   A 1 87  ? -8.61222  34.35903 19.21878 1.000 40.61155  ? 94  THR   A O   1 
ATOM   634  C CB  . THR   A 1 87  ? -10.14870 32.24518 20.07700 1.000 39.94540  ? 94  THR   A CB  1 
ATOM   635  O OG1 . THR   A 1 87  ? -10.88895 32.99042 21.05002 1.000 41.53895  ? 94  THR   A OG1 1 
ATOM   636  C CG2 . THR   A 1 87  ? -10.66373 30.80453 20.06396 1.000 36.00917  ? 94  THR   A CG2 1 
ATOM   637  N N   . GLY   A 1 88  ? -6.90214  33.95296 20.61450 1.000 39.86802  ? 95  GLY   A N   1 
ATOM   638  C CA  . GLY   A 1 88  ? -6.24503  35.21765 20.35912 1.000 37.56378  ? 95  GLY   A CA  1 
ATOM   639  C C   . GLY   A 1 88  ? -5.53582  35.24954 19.02138 1.000 39.45311  ? 95  GLY   A C   1 
ATOM   640  O O   . GLY   A 1 88  ? -5.79157  34.44150 18.12482 1.000 41.85222  ? 95  GLY   A O   1 
ATOM   641  N N   . ILE   A 1 89  ? -4.61302  36.20829 18.89667 1.000 40.47953  ? 96  ILE   A N   1 
ATOM   642  C CA  . ILE   A 1 89  ? -3.92676  36.43907 17.63068 1.000 46.39038  ? 96  ILE   A CA  1 
ATOM   643  C C   . ILE   A 1 89  ? -3.01115  35.27898 17.25360 1.000 41.93852  ? 96  ILE   A C   1 
ATOM   644  O O   . ILE   A 1 89  ? -2.68224  35.11074 16.07362 1.000 44.01182  ? 96  ILE   A O   1 
ATOM   645  C CB  . ILE   A 1 89  ? -3.14274  37.76505 17.69833 1.000 40.74382  ? 96  ILE   A CB  1 
ATOM   646  C CG1 . ILE   A 1 89  ? -2.75944  38.24287 16.29913 1.000 34.26008  ? 96  ILE   A CG1 1 
ATOM   647  C CG2 . ILE   A 1 89  ? -1.89638  37.60588 18.55393 1.000 29.92037  ? 96  ILE   A CG2 1 
ATOM   648  C CD1 . ILE   A 1 89  ? -2.40953  39.70415 16.23705 1.000 45.71204  ? 96  ILE   A CD1 1 
ATOM   649  N N   . GLY   A 1 90  ? -2.60476  34.45648 18.21481 1.000 43.34963  ? 97  GLY   A N   1 
ATOM   650  C CA  . GLY   A 1 90  ? -1.69463  33.36948 17.92485 1.000 35.68801  ? 97  GLY   A CA  1 
ATOM   651  C C   . GLY   A 1 90  ? -0.27205  33.85910 17.73555 1.000 46.14084  ? 97  GLY   A C   1 
ATOM   652  O O   . GLY   A 1 90  ? 0.04880   35.03762 17.89471 1.000 53.13327  ? 97  GLY   A O   1 
ATOM   653  N N   . MET   A 1 91  ? 0.59873   32.92059 17.37466 1.000 45.68602  ? 98  MET   A N   1 
ATOM   654  C CA  . MET   A 1 91  ? 2.02728   33.17406 17.26092 1.000 43.33664  ? 98  MET   A CA  1 
ATOM   655  C C   . MET   A 1 91  ? 2.56265   32.57088 15.97180 1.000 41.67618  ? 98  MET   A C   1 
ATOM   656  O O   . MET   A 1 91  ? 2.18270   31.45944 15.59040 1.000 47.64363  ? 98  MET   A O   1 
ATOM   657  C CB  . MET   A 1 91  ? 2.78599   32.58976 18.46067 1.000 42.04157  ? 98  MET   A CB  1 
ATOM   658  C CG  . MET   A 1 91  ? 2.80320   33.48431 19.69656 1.000 46.75925  ? 98  MET   A CG  1 
ATOM   659  S SD  . MET   A 1 91  ? 3.38068   32.61543 21.16923 1.000 53.95448  ? 98  MET   A SD  1 
ATOM   660  C CE  . MET   A 1 91  ? 2.19337   31.27639 21.26761 1.000 50.00540  ? 98  MET   A CE  1 
ATOM   661  N N   . THR   A 1 92  ? 3.44969   33.30546 15.30639 1.000 49.21526  ? 99  THR   A N   1 
ATOM   662  C CA  . THR   A 1 92  ? 4.09037   32.80776 14.09920 1.000 46.27440  ? 99  THR   A CA  1 
ATOM   663  C C   . THR   A 1 92  ? 5.28598   31.92562 14.45768 1.000 50.05523  ? 99  THR   A C   1 
ATOM   664  O O   . THR   A 1 92  ? 5.66254   31.78413 15.62455 1.000 49.32438  ? 99  THR   A O   1 
ATOM   665  C CB  . THR   A 1 92  ? 4.54447   33.96679 13.21459 1.000 46.29734  ? 99  THR   A CB  1 
ATOM   666  O OG1 . THR   A 1 92  ? 5.56060   34.71004 13.89602 1.000 50.27060  ? 99  THR   A OG1 1 
ATOM   667  C CG2 . THR   A 1 92  ? 3.37952   34.88850 12.90071 1.000 43.20662  ? 99  THR   A CG2 1 
ATOM   668  N N   . LYS   A 1 93  ? 5.89399   31.32506 13.43076 1.000 47.31636  ? 100 LYS   A N   1 
ATOM   669  C CA  . LYS   A 1 93  ? 7.12201   30.56887 13.65830 1.000 52.46737  ? 100 LYS   A CA  1 
ATOM   670  C C   . LYS   A 1 93  ? 8.24152   31.48068 14.14168 1.000 45.42817  ? 100 LYS   A C   1 
ATOM   671  O O   . LYS   A 1 93  ? 9.00504   31.11792 15.04611 1.000 52.64740  ? 100 LYS   A O   1 
ATOM   672  C CB  . LYS   A 1 93  ? 7.54515   29.83431 12.38454 1.000 51.65311  ? 100 LYS   A CB  1 
ATOM   673  C CG  . LYS   A 1 93  ? 8.60743   28.77035 12.63486 1.000 47.60208  ? 100 LYS   A CG  1 
ATOM   674  C CD  . LYS   A 1 93  ? 9.26964   28.27279 11.35413 1.000 49.97526  ? 100 LYS   A CD  1 
ATOM   675  C CE  . LYS   A 1 93  ? 10.10001  27.01744 11.63628 1.000 55.66763  ? 100 LYS   A CE  1 
ATOM   676  N NZ  . LYS   A 1 93  ? 10.80989  26.47622 10.43670 1.000 63.60563  ? 100 LYS   A NZ  1 
ATOM   677  N N   . ALA   A 1 94  ? 8.35019   32.67256 13.55094 1.000 54.92062  ? 101 ALA   A N   1 
ATOM   678  C CA  . ALA   A 1 94  ? 9.36498   33.62700 13.98167 1.000 50.65037  ? 101 ALA   A CA  1 
ATOM   679  C C   . ALA   A 1 94  ? 9.15791   34.03704 15.43420 1.000 52.03105  ? 101 ALA   A C   1 
ATOM   680  O O   . ALA   A 1 94  ? 10.12828  34.23330 16.17443 1.000 57.04172  ? 101 ALA   A O   1 
ATOM   681  C CB  . ALA   A 1 94  ? 9.35026   34.85210 13.06779 1.000 52.00151  ? 101 ALA   A CB  1 
ATOM   682  N N   . ASP   A 1 95  ? 7.89997   34.17141 15.86163 1.000 52.18864  ? 102 ASP   A N   1 
ATOM   683  C CA  . ASP   A 1 95  ? 7.62411   34.48497 17.26057 1.000 45.30328  ? 102 ASP   A CA  1 
ATOM   684  C C   . ASP   A 1 95  ? 8.19222   33.41130 18.18327 1.000 52.37250  ? 102 ASP   A C   1 
ATOM   685  O O   . ASP   A 1 95  ? 8.87851   33.71732 19.16607 1.000 50.27985  ? 102 ASP   A O   1 
ATOM   686  C CB  . ASP   A 1 95  ? 6.11675   34.63731 17.47836 1.000 40.04824  ? 102 ASP   A CB  1 
ATOM   687  C CG  . ASP   A 1 95  ? 5.56000   35.92246 16.87947 1.000 56.15812  ? 102 ASP   A CG  1 
ATOM   688  O OD1 . ASP   A 1 95  ? 6.29637   36.93254 16.82353 1.000 52.90513  ? 102 ASP   A OD1 1 
ATOM   689  O OD2 . ASP   A 1 95  ? 4.37775   35.92309 16.47537 1.000 52.13931  ? 102 ASP   A OD2 1 
ATOM   690  N N   . LEU   A 1 96  ? 7.93111   32.13899 17.86583 1.000 52.38917  ? 103 LEU   A N   1 
ATOM   691  C CA  . LEU   A 1 96  ? 8.32578   31.04518 18.75162 1.000 45.96799  ? 103 LEU   A CA  1 
ATOM   692  C C   . LEU   A 1 96  ? 9.83722   30.86916 18.82165 1.000 42.88541  ? 103 LEU   A C   1 
ATOM   693  O O   . LEU   A 1 96  ? 10.35323  30.36165 19.82561 1.000 57.09560  ? 103 LEU   A O   1 
ATOM   694  C CB  . LEU   A 1 96  ? 7.68859   29.73228 18.29448 1.000 38.38692  ? 103 LEU   A CB  1 
ATOM   695  C CG  . LEU   A 1 96  ? 6.16511   29.64622 18.22172 1.000 41.96654  ? 103 LEU   A CG  1 
ATOM   696  C CD1 . LEU   A 1 96  ? 5.75250   28.45538 17.36819 1.000 45.16955  ? 103 LEU   A CD1 1 
ATOM   697  C CD2 . LEU   A 1 96  ? 5.56334   29.55057 19.61226 1.000 36.97665  ? 103 LEU   A CD2 1 
ATOM   698  N N   . ILE   A 1 97  ? 10.56000  31.25778 17.77844 1.000 53.24967  ? 104 ILE   A N   1 
ATOM   699  C CA  . ILE   A 1 97  ? 11.99138  31.00935 17.70402 1.000 54.35194  ? 104 ILE   A CA  1 
ATOM   700  C C   . ILE   A 1 97  ? 12.81177  32.25014 18.04765 1.000 70.13265  ? 104 ILE   A C   1 
ATOM   701  O O   . ILE   A 1 97  ? 13.80143  32.14765 18.77251 1.000 73.94814  ? 104 ILE   A O   1 
ATOM   702  C CB  . ILE   A 1 97  ? 12.35635  30.45763 16.31016 1.000 64.92792  ? 104 ILE   A CB  1 
ATOM   703  C CG1 . ILE   A 1 97  ? 11.79459  29.04523 16.14070 1.000 51.38660  ? 104 ILE   A CG1 1 
ATOM   704  C CG2 . ILE   A 1 97  ? 13.85699  30.45695 16.09572 1.000 64.96961  ? 104 ILE   A CG2 1 
ATOM   705  C CD1 . ILE   A 1 97  ? 11.60819  28.62631 14.70247 1.000 44.23338  ? 104 ILE   A CD1 1 
ATOM   706  N N   . ASN   A 1 98  ? 12.42577  33.43558 17.56115 1.000 62.64737  ? 105 ASN   A N   1 
ATOM   707  C CA  . ASN   A 1 98  ? 13.26018  34.62543 17.71980 1.000 63.93508  ? 105 ASN   A CA  1 
ATOM   708  C C   . ASN   A 1 98  ? 12.55088  35.78564 18.40564 1.000 66.63629  ? 105 ASN   A C   1 
ATOM   709  O O   . ASN   A 1 98  ? 13.08747  36.34639 19.36801 1.000 64.55051  ? 105 ASN   A O   1 
ATOM   710  C CB  . ASN   A 1 98  ? 13.79774  35.10581 16.35573 1.000 58.36946  ? 105 ASN   A CB  1 
ATOM   711  C CG  . ASN   A 1 98  ? 14.27009  33.97212 15.47429 1.000 73.56207  ? 105 ASN   A CG  1 
ATOM   712  O OD1 . ASN   A 1 98  ? 13.58122  33.57483 14.53436 1.000 85.56615  ? 105 ASN   A OD1 1 
ATOM   713  N ND2 . ASN   A 1 98  ? 15.46451  33.46095 15.75519 1.000 81.03130  ? 105 ASN   A ND2 1 
ATOM   714  N N   . ASN   A 1 99  ? 11.36329  36.16808 17.93448 1.000 56.80645  ? 106 ASN   A N   1 
ATOM   715  C CA  . ASN   A 1 99  ? 10.83539  37.49369 18.25418 1.000 61.58780  ? 106 ASN   A CA  1 
ATOM   716  C C   . ASN   A 1 99  ? 10.41881  37.61515 19.71526 1.000 66.01673  ? 106 ASN   A C   1 
ATOM   717  O O   . ASN   A 1 99  ? 10.59799  38.67748 20.32267 1.000 61.27497  ? 106 ASN   A O   1 
ATOM   718  C CB  . ASN   A 1 99  ? 9.66152   37.82272 17.33563 1.000 50.88771  ? 106 ASN   A CB  1 
ATOM   719  C CG  . ASN   A 1 99  ? 10.06401  37.86182 15.87772 1.000 57.07547  ? 106 ASN   A CG  1 
ATOM   720  O OD1 . ASN   A 1 99  ? 11.23117  38.09224 15.55025 1.000 55.98957  ? 106 ASN   A OD1 1 
ATOM   721  N ND2 . ASN   A 1 99  ? 9.09703   37.65548 14.98991 1.000 67.90584  ? 106 ASN   A ND2 1 
ATOM   722  N N   . LEU   A 1 100 ? 9.83963   36.55962 20.29343 1.000 60.04933  ? 107 LEU   A N   1 
ATOM   723  C CA  . LEU   A 1 100 ? 9.42498   36.64555 21.69006 1.000 68.67161  ? 107 LEU   A CA  1 
ATOM   724  C C   . LEU   A 1 100 ? 10.63193  36.74055 22.61362 1.000 69.63377  ? 107 LEU   A C   1 
ATOM   725  O O   . LEU   A 1 100 ? 10.61264  37.49335 23.59427 1.000 81.32212  ? 107 LEU   A O   1 
ATOM   726  C CB  . LEU   A 1 100 ? 8.55394   35.44603 22.06732 1.000 80.75290  ? 107 LEU   A CB  1 
ATOM   727  C CG  . LEU   A 1 100 ? 7.03170   35.54618 21.89730 1.000 67.17399  ? 107 LEU   A CG  1 
ATOM   728  C CD1 . LEU   A 1 100 ? 6.61388   36.83591 21.20212 1.000 45.30075  ? 107 LEU   A CD1 1 
ATOM   729  C CD2 . LEU   A 1 100 ? 6.48254   34.32843 21.16711 1.000 72.00202  ? 107 LEU   A CD2 1 
ATOM   730  N N   . GLY   A 1 101 ? 11.69311  35.99025 22.31304 1.000 71.27432  ? 108 GLY   A N   1 
ATOM   731  C CA  . GLY   A 1 101 ? 12.89327  36.06844 23.12795 1.000 73.67735  ? 108 GLY   A CA  1 
ATOM   732  C C   . GLY   A 1 101 ? 13.58897  37.41162 23.01579 1.000 80.13014  ? 108 GLY   A C   1 
ATOM   733  O O   . GLY   A 1 101 ? 14.05397  37.96450 24.01682 1.000 82.67764  ? 108 GLY   A O   1 
ATOM   734  N N   . THR   A 1 102 ? 13.66359  37.95855 21.79942 1.000 71.58210  ? 109 THR   A N   1 
ATOM   735  C CA  . THR   A 1 102 ? 14.31382  39.25238 21.60929 1.000 56.96689  ? 109 THR   A CA  1 
ATOM   736  C C   . THR   A 1 102 ? 13.60722  40.34862 22.39682 1.000 72.61943  ? 109 THR   A C   1 
ATOM   737  O O   . THR   A 1 102 ? 14.25991  41.21095 22.99822 1.000 86.56686  ? 109 THR   A O   1 
ATOM   738  C CB  . THR   A 1 102 ? 14.36215  39.60428 20.12158 1.000 59.48897  ? 109 THR   A CB  1 
ATOM   739  O OG1 . THR   A 1 102 ? 14.99402  38.54119 19.39739 1.000 65.00814  ? 109 THR   A OG1 1 
ATOM   740  C CG2 . THR   A 1 102 ? 15.12124  40.90790 19.89136 1.000 50.06009  ? 109 THR   A CG2 1 
ATOM   741  N N   . ILE   A 1 103 ? 12.27184  40.32821 22.41203 1.000 75.64676  ? 110 ILE   A N   1 
ATOM   742  C CA  . ILE   A 1 103 ? 11.52600  41.30412 23.20088 1.000 68.31287  ? 110 ILE   A CA  1 
ATOM   743  C C   . ILE   A 1 103 ? 11.74676  41.06689 24.68973 1.000 79.85514  ? 110 ILE   A C   1 
ATOM   744  O O   . ILE   A 1 103 ? 11.72593  42.01075 25.48969 1.000 86.55573  ? 110 ILE   A O   1 
ATOM   745  C CB  . ILE   A 1 103 ? 10.02841  41.24515 22.84416 1.000 70.04933  ? 110 ILE   A CB  1 
ATOM   746  C CG1 . ILE   A 1 103 ? 9.80761   41.66577 21.39234 1.000 73.41926  ? 110 ILE   A CG1 1 
ATOM   747  C CG2 . ILE   A 1 103 ? 9.21432   42.13759 23.77312 1.000 72.12967  ? 110 ILE   A CG2 1 
ATOM   748  C CD1 . ILE   A 1 103 ? 10.23692  43.07946 21.09362 1.000 63.51688  ? 110 ILE   A CD1 1 
ATOM   749  N N   . ALA   A 1 104 ? 11.98320  39.81562 25.08657 1.000 73.63746  ? 111 ALA   A N   1 
ATOM   750  C CA  . ALA   A 1 104 ? 12.01607  39.47970 26.50436 1.000 67.18327  ? 111 ALA   A CA  1 
ATOM   751  C C   . ALA   A 1 104 ? 13.38068  39.70883 27.13614 1.000 71.14415  ? 111 ALA   A C   1 
ATOM   752  O O   . ALA   A 1 104 ? 13.44934  40.02381 28.32900 1.000 70.91244  ? 111 ALA   A O   1 
ATOM   753  C CB  . ALA   A 1 104 ? 11.60102  38.02475 26.70890 1.000 69.40519  ? 111 ALA   A CB  1 
ATOM   754  N N   . LYS   A 1 105 ? 14.45949  39.55952 26.36166 1.000 79.59134  ? 112 LYS   A N   1 
ATOM   755  C CA  . LYS   A 1 105 ? 15.83019  39.52575 26.86966 1.000 70.57569  ? 112 LYS   A CA  1 
ATOM   756  C C   . LYS   A 1 105 ? 16.10226  40.57026 27.94707 1.000 75.76499  ? 112 LYS   A C   1 
ATOM   757  O O   . LYS   A 1 105 ? 16.79406  40.28298 28.92942 1.000 84.23759  ? 112 LYS   A O   1 
ATOM   758  C CB  . LYS   A 1 105 ? 16.82406  39.70634 25.71820 1.000 73.10299  ? 112 LYS   A CB  1 
ATOM   759  C CG  . LYS   A 1 105 ? 18.25113  39.28448 26.05300 1.000 79.77695  ? 112 LYS   A CG  1 
ATOM   760  C CD  . LYS   A 1 105 ? 19.23972  39.73416 24.97842 1.000 79.58732  ? 112 LYS   A CD  1 
ATOM   761  C CE  . LYS   A 1 105 ? 20.21517  38.62750 24.59896 1.000 77.40388  ? 112 LYS   A CE  1 
ATOM   762  N NZ  . LYS   A 1 105 ? 21.60579  39.15459 24.46869 1.000 78.59007  ? 112 LYS   A NZ  1 
ATOM   763  N N   . SER   A 1 106 ? 15.55706  41.77887 27.78134 1.000 62.49551  ? 113 SER   A N   1 
ATOM   764  C CA  . SER   A 1 106 ? 15.77999  42.82523 28.77428 1.000 73.21513  ? 113 SER   A CA  1 
ATOM   765  C C   . SER   A 1 106 ? 14.96511  42.57129 30.03872 1.000 73.91219  ? 113 SER   A C   1 
ATOM   766  O O   . SER   A 1 106 ? 15.46647  42.75445 31.15542 1.000 61.26190  ? 113 SER   A O   1 
ATOM   767  C CB  . SER   A 1 106 ? 15.44739  44.19370 28.17711 1.000 72.47485  ? 113 SER   A CB  1 
ATOM   768  O OG  . SER   A 1 106 ? 15.23380  45.16065 29.19120 1.000 89.40037  ? 113 SER   A OG  1 
ATOM   769  N N   . GLY   A 1 107 ? 13.70820  42.14981 29.88631 1.000 78.09540  ? 114 GLY   A N   1 
ATOM   770  C CA  . GLY   A 1 107 ? 12.89887  41.84115 31.05426 1.000 72.26410  ? 114 GLY   A CA  1 
ATOM   771  C C   . GLY   A 1 107 ? 13.41657  40.63841 31.82047 1.000 64.51934  ? 114 GLY   A C   1 
ATOM   772  O O   . GLY   A 1 107 ? 13.33273  40.59189 33.05086 1.000 69.76214  ? 114 GLY   A O   1 
ATOM   773  N N   . THR   A 1 108 ? 13.95833  39.65028 31.10555 1.000 59.21712  ? 115 THR   A N   1 
ATOM   774  C CA  . THR   A 1 108 ? 14.53534  38.48410 31.76604 1.000 61.66276  ? 115 THR   A CA  1 
ATOM   775  C C   . THR   A 1 108 ? 15.73643  38.88088 32.61332 1.000 61.95651  ? 115 THR   A C   1 
ATOM   776  O O   . THR   A 1 108 ? 15.83078  38.51097 33.78828 1.000 69.46938  ? 115 THR   A O   1 
ATOM   777  C CB  . THR   A 1 108 ? 14.92897  37.43503 30.72485 1.000 66.97274  ? 115 THR   A CB  1 
ATOM   778  O OG1 . THR   A 1 108 ? 13.87371  37.29760 29.76558 1.000 61.98649  ? 115 THR   A OG1 1 
ATOM   779  C CG2 . THR   A 1 108 ? 15.19420  36.09032 31.38650 1.000 63.31106  ? 115 THR   A CG2 1 
ATOM   780  N N   . LYS   A 1 109 ? 16.66386  39.64310 32.02870 1.000 57.53332  ? 116 LYS   A N   1 
ATOM   781  C CA  . LYS   A 1 109 ? 17.80341  40.15600 32.78299 1.000 62.03737  ? 116 LYS   A CA  1 
ATOM   782  C C   . LYS   A 1 109 ? 17.34398  40.95827 33.99462 1.000 65.39880  ? 116 LYS   A C   1 
ATOM   783  O O   . LYS   A 1 109 ? 17.84841  40.77000 35.10817 1.000 70.21965  ? 116 LYS   A O   1 
ATOM   784  C CB  . LYS   A 1 109 ? 18.67775  41.02197 31.87661 1.000 69.18020  ? 116 LYS   A CB  1 
ATOM   785  C CG  . LYS   A 1 109 ? 19.72703  40.26972 31.08469 1.000 71.75469  ? 116 LYS   A CG  1 
ATOM   786  C CD  . LYS   A 1 109 ? 20.76594  41.23955 30.53870 1.000 82.69809  ? 116 LYS   A CD  1 
ATOM   787  C CE  . LYS   A 1 109 ? 21.84050  40.52815 29.73083 1.000 97.23747  ? 116 LYS   A CE  1 
ATOM   788  N NZ  . LYS   A 1 109 ? 22.73229  39.69582 30.58736 1.000 93.44811  ? 116 LYS   A NZ  1 
ATOM   789  N N   . ALA   A 1 110 ? 16.38027  41.86239 33.79266 1.000 64.03063  ? 117 ALA   A N   1 
ATOM   790  C CA  . ALA   A 1 110 ? 15.91165  42.70972 34.88420 1.000 65.66824  ? 117 ALA   A CA  1 
ATOM   791  C C   . ALA   A 1 110 ? 15.21545  41.90092 35.96902 1.000 69.55093  ? 117 ALA   A C   1 
ATOM   792  O O   . ALA   A 1 110 ? 15.29530  42.25310 37.15226 1.000 74.53156  ? 117 ALA   A O   1 
ATOM   793  C CB  . ALA   A 1 110 ? 14.97163  43.78651 34.34491 1.000 64.29792  ? 117 ALA   A CB  1 
ATOM   794  N N   . PHE   A 1 111 ? 14.53195  40.81769 35.58888 1.000 61.94251  ? 118 PHE   A N   1 
ATOM   795  C CA  . PHE   A 1 111 ? 13.84015  39.99092 36.57204 1.000 65.13654  ? 118 PHE   A CA  1 
ATOM   796  C C   . PHE   A 1 111 ? 14.81429  39.32075 37.53501 1.000 77.19846  ? 118 PHE   A C   1 
ATOM   797  O O   . PHE   A 1 111 ? 14.49997  39.16339 38.72088 1.000 78.58030  ? 118 PHE   A O   1 
ATOM   798  C CB  . PHE   A 1 111 ? 12.98286  38.94131 35.86345 1.000 57.48795  ? 118 PHE   A CB  1 
ATOM   799  C CG  . PHE   A 1 111 ? 12.12933  38.12853 36.79388 1.000 64.61100  ? 118 PHE   A CG  1 
ATOM   800  C CD1 . PHE   A 1 111 ? 11.44945  38.73418 37.83725 1.000 66.05427  ? 118 PHE   A CD1 1 
ATOM   801  C CD2 . PHE   A 1 111 ? 11.99393  36.76340 36.61790 1.000 55.12083  ? 118 PHE   A CD2 1 
ATOM   802  C CE1 . PHE   A 1 111 ? 10.66165  37.99129 38.69492 1.000 64.56664  ? 118 PHE   A CE1 1 
ATOM   803  C CE2 . PHE   A 1 111 ? 11.20494  36.01539 37.46997 1.000 60.61547  ? 118 PHE   A CE2 1 
ATOM   804  C CZ  . PHE   A 1 111 ? 10.53896  36.63196 38.51137 1.000 66.65539  ? 118 PHE   A CZ  1 
ATOM   805  N N   . MET   A 1 112 ? 15.99631  38.92467 37.05462 1.000 75.80184  ? 119 MET   A N   1 
ATOM   806  C CA  . MET   A 1 112 ? 16.97958  38.31879 37.94821 1.000 80.53924  ? 119 MET   A CA  1 
ATOM   807  C C   . MET   A 1 112 ? 17.55855  39.34719 38.90866 1.000 79.25753  ? 119 MET   A C   1 
ATOM   808  O O   . MET   A 1 112 ? 17.78253  39.04621 40.08710 1.000 93.80030  ? 119 MET   A O   1 
ATOM   809  C CB  . MET   A 1 112 ? 18.09906  37.65774 37.14622 1.000 83.04527  ? 119 MET   A CB  1 
ATOM   810  C CG  . MET   A 1 112 ? 17.67287  37.11529 35.80225 1.000 68.60325  ? 119 MET   A CG  1 
ATOM   811  S SD  . MET   A 1 112 ? 17.02320  35.44191 35.90110 1.000 82.27312  ? 119 MET   A SD  1 
ATOM   812  C CE  . MET   A 1 112 ? 18.37544  34.55345 35.15667 1.000 65.63697  ? 119 MET   A CE  1 
ATOM   813  N N   . GLU   A 1 113 ? 17.81934  40.56205 38.42009 1.000 83.08706  ? 120 GLU   A N   1 
ATOM   814  C CA  . GLU   A 1 113 ? 18.29566  41.62399 39.29992 1.000 92.23392  ? 120 GLU   A CA  1 
ATOM   815  C C   . GLU   A 1 113 ? 17.26696  41.94478 40.37564 1.000 95.65984  ? 120 GLU   A C   1 
ATOM   816  O O   . GLU   A 1 113 ? 17.62357  42.19148 41.53421 1.000 103.24163 ? 120 GLU   A O   1 
ATOM   817  C CB  . GLU   A 1 113 ? 18.62027  42.87377 38.48388 1.000 93.66375  ? 120 GLU   A CB  1 
ATOM   818  C CG  . GLU   A 1 113 ? 19.67431  42.66282 37.41481 1.000 87.08305  ? 120 GLU   A CG  1 
ATOM   819  C CD  . GLU   A 1 113 ? 19.68136  43.77946 36.39163 1.000 106.28908 ? 120 GLU   A CD  1 
ATOM   820  O OE1 . GLU   A 1 113 ? 19.06800  44.83427 36.66137 1.000 114.58281 ? 120 GLU   A OE1 1 
ATOM   821  O OE2 . GLU   A 1 113 ? 20.29129  43.60063 35.31629 1.000 101.37226 ? 120 GLU   A OE2 1 
ATOM   822  N N   . ALA   A 1 114 ? 15.98180  41.93882 40.01066 1.000 78.57542  ? 121 ALA   A N   1 
ATOM   823  C CA  . ALA   A 1 114 ? 14.93529  42.24223 40.97889 1.000 79.96779  ? 121 ALA   A CA  1 
ATOM   824  C C   . ALA   A 1 114 ? 14.82820  41.16397 42.04833 1.000 94.14921  ? 121 ALA   A C   1 
ATOM   825  O O   . ALA   A 1 114 ? 14.55908  41.47608 43.21430 1.000 109.50908 ? 121 ALA   A O   1 
ATOM   826  C CB  . ALA   A 1 114 ? 13.59509  42.41979 40.26587 1.000 75.38899  ? 121 ALA   A CB  1 
ATOM   827  N N   . LEU   A 1 115 ? 15.04795  39.89888 41.67759 1.000 90.82774  ? 122 LEU   A N   1 
ATOM   828  C CA  . LEU   A 1 115 ? 14.92176  38.80900 42.64019 1.000 95.99225  ? 122 LEU   A CA  1 
ATOM   829  C C   . LEU   A 1 115 ? 15.91539  38.95028 43.78733 1.000 100.53843 ? 122 LEU   A C   1 
ATOM   830  O O   . LEU   A 1 115 ? 15.66331  38.45244 44.89047 1.000 104.53709 ? 122 LEU   A O   1 
ATOM   831  C CB  . LEU   A 1 115 ? 15.09979  37.46565 41.93263 1.000 85.82603  ? 122 LEU   A CB  1 
ATOM   832  C CG  . LEU   A 1 115 ? 13.88093  36.99499 41.13493 1.000 84.27425  ? 122 LEU   A CG  1 
ATOM   833  C CD1 . LEU   A 1 115 ? 14.16586  35.69005 40.40913 1.000 80.19112  ? 122 LEU   A CD1 1 
ATOM   834  C CD2 . LEU   A 1 115 ? 12.66191  36.85576 42.03458 1.000 88.52017  ? 122 LEU   A CD2 1 
ATOM   835  N N   . GLN   A 1 116 ? 17.04080  39.62511 43.55299 1.000 105.72454 ? 123 GLN   A N   1 
ATOM   836  C CA  . GLN   A 1 116 ? 17.97427  39.94980 44.62267 1.000 115.13439 ? 123 GLN   A CA  1 
ATOM   837  C C   . GLN   A 1 116 ? 17.65923  41.27538 45.30067 1.000 110.03148 ? 123 GLN   A C   1 
ATOM   838  O O   . GLN   A 1 116 ? 18.11412  41.50289 46.42779 1.000 117.29391 ? 123 GLN   A O   1 
ATOM   839  C CB  . GLN   A 1 116 ? 19.40601  39.98600 44.08157 1.000 128.49098 ? 123 GLN   A CB  1 
ATOM   840  C CG  . GLN   A 1 116 ? 19.95301  38.62824 43.67937 1.000 131.55813 ? 123 GLN   A CG  1 
ATOM   841  C CD  . GLN   A 1 116 ? 21.13550  38.73995 42.74078 1.000 136.10356 ? 123 GLN   A CD  1 
ATOM   842  O OE1 . GLN   A 1 116 ? 21.24448  39.69711 41.97338 1.000 129.04969 ? 123 GLN   A OE1 1 
ATOM   843  N NE2 . GLN   A 1 116 ? 22.03709  37.76700 42.80568 1.000 126.17211 ? 123 GLN   A NE2 1 
ATOM   844  N N   . ALA   A 1 117 ? 16.89601  42.15098 44.64083 1.000 120.67451 ? 124 ALA   A N   1 
ATOM   845  C CA  . ALA   A 1 117 ? 16.50839  43.44486 45.18986 1.000 120.59810 ? 124 ALA   A CA  1 
ATOM   846  C C   . ALA   A 1 117 ? 15.20727  43.38063 45.98289 1.000 139.72013 ? 124 ALA   A C   1 
ATOM   847  O O   . ALA   A 1 117 ? 14.43681  44.35153 45.98477 1.000 143.44556 ? 124 ALA   A O   1 
ATOM   848  C CB  . ALA   A 1 117 ? 16.39895  44.47922 44.06796 1.000 98.65549  ? 124 ALA   A CB  1 
ATOM   849  N N   . GLY   A 1 118 ? 14.93632  42.25795 46.64857 1.000 136.67936 ? 125 GLY   A N   1 
ATOM   850  C CA  . GLY   A 1 118 ? 13.77121  42.12432 47.49625 1.000 131.86299 ? 125 GLY   A CA  1 
ATOM   851  C C   . GLY   A 1 118 ? 12.51073  41.64291 46.81123 1.000 117.86448 ? 125 GLY   A C   1 
ATOM   852  O O   . GLY   A 1 118 ? 11.47914  41.50456 47.48133 1.000 128.68087 ? 125 GLY   A O   1 
ATOM   853  N N   . ALA   A 1 119 ? 12.55170  41.38415 45.50857 1.000 108.39326 ? 126 ALA   A N   1 
ATOM   854  C CA  . ALA   A 1 119 ? 11.37478  40.93144 44.78325 1.000 106.00582 ? 126 ALA   A CA  1 
ATOM   855  C C   . ALA   A 1 119 ? 11.29449  39.41133 44.78615 1.000 102.38025 ? 126 ALA   A C   1 
ATOM   856  O O   . ALA   A 1 119 ? 12.31199  38.71328 44.78087 1.000 101.14794 ? 126 ALA   A O   1 
ATOM   857  C CB  . ALA   A 1 119 ? 11.38845  41.44461 43.34261 1.000 87.22240  ? 126 ALA   A CB  1 
ATOM   858  N N   . ASP   A 1 120 ? 10.06904  38.90288 44.79786 1.000 89.79484  ? 127 ASP   A N   1 
ATOM   859  C CA  . ASP   A 1 120 ? 9.82345   37.47265 44.72344 1.000 96.16493  ? 127 ASP   A CA  1 
ATOM   860  C C   . ASP   A 1 120 ? 9.29326   37.10789 43.34057 1.000 91.57101  ? 127 ASP   A C   1 
ATOM   861  O O   . ASP   A 1 120 ? 9.04123   37.96742 42.49145 1.000 83.34239  ? 127 ASP   A O   1 
ATOM   862  C CB  . ASP   A 1 120 ? 8.85465   37.02278 45.82615 1.000 91.34625  ? 127 ASP   A CB  1 
ATOM   863  C CG  . ASP   A 1 120 ? 7.42299   37.42403 45.54759 1.000 97.53210  ? 127 ASP   A CG  1 
ATOM   864  O OD1 . ASP   A 1 120 ? 7.17097   38.63116 45.34117 1.000 93.63558  ? 127 ASP   A OD1 1 
ATOM   865  O OD2 . ASP   A 1 120 ? 6.55079   36.52905 45.53515 1.000 93.25537  ? 127 ASP   A OD2 1 
ATOM   866  N N   . ILE   A 1 121 ? 9.13138   35.80051 43.12709 1.000 88.36818  ? 128 ILE   A N   1 
ATOM   867  C CA  . ILE   A 1 121 ? 8.79643   35.27553 41.80671 1.000 78.09332  ? 128 ILE   A CA  1 
ATOM   868  C C   . ILE   A 1 121 ? 7.43917   35.78699 41.33447 1.000 76.62011  ? 128 ILE   A C   1 
ATOM   869  O O   . ILE   A 1 121 ? 7.20332   35.92694 40.12737 1.000 77.48843  ? 128 ILE   A O   1 
ATOM   870  C CB  . ILE   A 1 121 ? 8.86285   33.73244 41.84758 1.000 76.94804  ? 128 ILE   A CB  1 
ATOM   871  C CG1 . ILE   A 1 121 ? 10.32272  33.26801 41.85907 1.000 86.04289  ? 128 ILE   A CG1 1 
ATOM   872  C CG2 . ILE   A 1 121 ? 8.11707   33.10451 40.68101 1.000 80.50051  ? 128 ILE   A CG2 1 
ATOM   873  C CD1 . ILE   A 1 121 ? 10.55785  31.98649 42.62724 1.000 74.89785  ? 128 ILE   A CD1 1 
ATOM   874  N N   . SER   A 1 122 ? 6.54445   36.11864 42.26646 1.000 80.34622  ? 129 SER   A N   1 
ATOM   875  C CA  . SER   A 1 122 ? 5.17937   36.48469 41.90507 1.000 74.38675  ? 129 SER   A CA  1 
ATOM   876  C C   . SER   A 1 122 ? 5.08803   37.75831 41.06808 1.000 77.19440  ? 129 SER   A C   1 
ATOM   877  O O   . SER   A 1 122 ? 4.01264   38.03998 40.52767 1.000 73.61670  ? 129 SER   A O   1 
ATOM   878  C CB  . SER   A 1 122 ? 4.33318   36.63743 43.17004 1.000 73.58752  ? 129 SER   A CB  1 
ATOM   879  O OG  . SER   A 1 122 ? 4.65744   37.83223 43.85489 1.000 82.06789  ? 129 SER   A OG  1 
ATOM   880  N N   . MET   A 1 123 ? 6.16707   38.53257 40.94063 1.000 68.20464  ? 130 MET   A N   1 
ATOM   881  C CA  . MET   A 1 123 ? 6.16090   39.73130 40.11016 1.000 67.90201  ? 130 MET   A CA  1 
ATOM   882  C C   . MET   A 1 123 ? 6.68244   39.46979 38.70151 1.000 69.75279  ? 130 MET   A C   1 
ATOM   883  O O   . MET   A 1 123 ? 7.05545   40.41671 37.99846 1.000 61.01797  ? 130 MET   A O   1 
ATOM   884  C CB  . MET   A 1 123 ? 6.97473   40.84510 40.76897 1.000 72.10138  ? 130 MET   A CB  1 
ATOM   885  C CG  . MET   A 1 123 ? 6.75284   40.98671 42.25997 1.000 75.28951  ? 130 MET   A CG  1 
ATOM   886  S SD  . MET   A 1 123 ? 7.88660   42.19050 42.96538 1.000 93.97819  ? 130 MET   A SD  1 
ATOM   887  C CE  . MET   A 1 123 ? 7.89223   43.43602 41.67674 1.000 79.96095  ? 130 MET   A CE  1 
ATOM   888  N N   . ILE   A 1 124 ? 6.69823   38.20588 38.27212 1.000 59.96004  ? 131 ILE   A N   1 
ATOM   889  C CA  . ILE   A 1 124 ? 7.29222   37.85121 36.98706 1.000 60.32764  ? 131 ILE   A CA  1 
ATOM   890  C C   . ILE   A 1 124 ? 6.55942   38.52520 35.83145 1.000 59.20431  ? 131 ILE   A C   1 
ATOM   891  O O   . ILE   A 1 124 ? 7.17020   38.85004 34.80471 1.000 53.25774  ? 131 ILE   A O   1 
ATOM   892  C CB  . ILE   A 1 124 ? 7.31942   36.31459 36.83971 1.000 57.20953  ? 131 ILE   A CB  1 
ATOM   893  C CG1 . ILE   A 1 124 ? 8.11003   35.89589 35.60158 1.000 50.49911  ? 131 ILE   A CG1 1 
ATOM   894  C CG2 . ILE   A 1 124 ? 5.91123   35.74884 36.80356 1.000 48.66080  ? 131 ILE   A CG2 1 
ATOM   895  C CD1 . ILE   A 1 124 ? 8.46774   34.43029 35.58793 1.000 51.25431  ? 131 ILE   A CD1 1 
ATOM   896  N N   . GLY   A 1 125 ? 5.25482   38.76960 35.98037 1.000 55.14794  ? 132 GLY   A N   1 
ATOM   897  C CA  . GLY   A 1 125 ? 4.49792   39.37907 34.90053 1.000 60.02271  ? 132 GLY   A CA  1 
ATOM   898  C C   . GLY   A 1 125 ? 4.92507   40.79942 34.59049 1.000 67.79913  ? 132 GLY   A C   1 
ATOM   899  O O   . GLY   A 1 125 ? 4.86479   41.22959 33.43400 1.000 64.03337  ? 132 GLY   A O   1 
ATOM   900  N N   . GLN   A 1 126 ? 5.37483   41.54108 35.60695 1.000 57.77752  ? 133 GLN   A N   1 
ATOM   901  C CA  . GLN   A 1 126 ? 5.80955   42.92011 35.41681 1.000 65.44600  ? 133 GLN   A CA  1 
ATOM   902  C C   . GLN   A 1 126 ? 7.01429   43.04039 34.49628 1.000 63.10415  ? 133 GLN   A C   1 
ATOM   903  O O   . GLN   A 1 126 ? 7.37020   44.16148 34.11601 1.000 74.39996  ? 133 GLN   A O   1 
ATOM   904  C CB  . GLN   A 1 126 ? 6.14220   43.55326 36.76583 1.000 64.77925  ? 133 GLN   A CB  1 
ATOM   905  C CG  . GLN   A 1 126 ? 5.09870   43.31195 37.83485 1.000 69.96355  ? 133 GLN   A CG  1 
ATOM   906  C CD  . GLN   A 1 126 ? 5.29087   44.21768 39.03012 1.000 89.03981  ? 133 GLN   A CD  1 
ATOM   907  O OE1 . GLN   A 1 126 ? 5.90443   45.28154 38.92473 1.000 95.32207  ? 133 GLN   A OE1 1 
ATOM   908  N NE2 . GLN   A 1 126 ? 4.76993   43.80054 40.17837 1.000 91.72783  ? 133 GLN   A NE2 1 
ATOM   909  N N   . PHE   A 1 127 ? 7.65189   41.92703 34.14029 1.000 52.29625  ? 134 PHE   A N   1 
ATOM   910  C CA  . PHE   A 1 127 ? 8.80633   41.92681 33.25289 1.000 60.32798  ? 134 PHE   A CA  1 
ATOM   911  C C   . PHE   A 1 127 ? 8.51475   41.23941 31.92575 1.000 57.72422  ? 134 PHE   A C   1 
ATOM   912  O O   . PHE   A 1 127 ? 9.42916   41.06829 31.11030 1.000 58.35108  ? 134 PHE   A O   1 
ATOM   913  C CB  . PHE   A 1 127 ? 10.00411  41.27190 33.94735 1.000 52.83231  ? 134 PHE   A CB  1 
ATOM   914  C CG  . PHE   A 1 127 ? 10.33200  41.87984 35.28529 1.000 56.71485  ? 134 PHE   A CG  1 
ATOM   915  C CD1 . PHE   A 1 127 ? 9.69077   41.44794 36.43553 1.000 57.94110  ? 134 PHE   A CD1 1 
ATOM   916  C CD2 . PHE   A 1 127 ? 11.27417  42.89285 35.38915 1.000 65.61554  ? 134 PHE   A CD2 1 
ATOM   917  C CE1 . PHE   A 1 127 ? 9.98611   42.00974 37.66399 1.000 62.09055  ? 134 PHE   A CE1 1 
ATOM   918  C CE2 . PHE   A 1 127 ? 11.57465  43.45893 36.61385 1.000 66.26854  ? 134 PHE   A CE2 1 
ATOM   919  C CZ  . PHE   A 1 127 ? 10.92987  43.01732 37.75294 1.000 68.78982  ? 134 PHE   A CZ  1 
ATOM   920  N N   . GLY   A 1 128 ? 7.26523   40.84072 31.69262 1.000 53.04886  ? 135 GLY   A N   1 
ATOM   921  C CA  . GLY   A 1 128 ? 6.87416   40.29242 30.40916 1.000 56.47568  ? 135 GLY   A CA  1 
ATOM   922  C C   . GLY   A 1 128 ? 7.33849   38.88255 30.12874 1.000 58.47273  ? 135 GLY   A C   1 
ATOM   923  O O   . GLY   A 1 128 ? 7.36506   38.47475 28.96680 1.000 49.70384  ? 135 GLY   A O   1 
ATOM   924  N N   . VAL   A 1 129 ? 7.71015   38.12227 31.15688 1.000 56.30737  ? 136 VAL   A N   1 
ATOM   925  C CA  . VAL   A 1 129 ? 8.16499   36.74689 30.97567 1.000 49.54325  ? 136 VAL   A CA  1 
ATOM   926  C C   . VAL   A 1 129 ? 7.34475   35.82318 31.86507 1.000 50.77528  ? 136 VAL   A C   1 
ATOM   927  O O   . VAL   A 1 129 ? 7.83234   34.78564 32.32928 1.000 55.23582  ? 136 VAL   A O   1 
ATOM   928  C CB  . VAL   A 1 129 ? 9.67168   36.61567 31.26451 1.000 55.18061  ? 136 VAL   A CB  1 
ATOM   929  C CG1 . VAL   A 1 129 ? 10.46820  37.49880 30.31632 1.000 54.28875  ? 136 VAL   A CG1 1 
ATOM   930  C CG2 . VAL   A 1 129 ? 9.97006   37.02193 32.69627 1.000 56.81623  ? 136 VAL   A CG2 1 
ATOM   931  N N   . GLY   A 1 130 ? 6.07768   36.18290 32.07868 1.000 50.08723  ? 137 GLY   A N   1 
ATOM   932  C CA  . GLY   A 1 130 ? 5.22402   35.40009 32.95936 1.000 59.20793  ? 137 GLY   A CA  1 
ATOM   933  C C   . GLY   A 1 130 ? 4.96262   33.98422 32.47346 1.000 52.83141  ? 137 GLY   A C   1 
ATOM   934  O O   . GLY   A 1 130 ? 4.69078   33.08858 33.27964 1.000 49.62586  ? 137 GLY   A O   1 
ATOM   935  N N   . PHE   A 1 131 ? 5.03479   33.76075 31.15600 1.000 47.95498  ? 138 PHE   A N   1 
ATOM   936  C CA  . PHE   A 1 131 ? 4.77082   32.43262 30.60091 1.000 56.73136  ? 138 PHE   A CA  1 
ATOM   937  C C   . PHE   A 1 131 ? 5.63681   31.36259 31.24933 1.000 53.93148  ? 138 PHE   A C   1 
ATOM   938  O O   . PHE   A 1 131 ? 5.19429   30.21909 31.41972 1.000 44.90926  ? 138 PHE   A O   1 
ATOM   939  C CB  . PHE   A 1 131 ? 5.00172   32.43334 29.08639 1.000 47.83712  ? 138 PHE   A CB  1 
ATOM   940  C CG  . PHE   A 1 131 ? 5.22100   31.06173 28.50089 1.000 56.44083  ? 138 PHE   A CG  1 
ATOM   941  C CD1 . PHE   A 1 131 ? 4.14209   30.23922 28.22337 1.000 39.81082  ? 138 PHE   A CD1 1 
ATOM   942  C CD2 . PHE   A 1 131 ? 6.50231   30.59639 28.22626 1.000 50.30740  ? 138 PHE   A CD2 1 
ATOM   943  C CE1 . PHE   A 1 131 ? 4.32981   28.97933 27.68508 1.000 42.08601  ? 138 PHE   A CE1 1 
ATOM   944  C CE2 . PHE   A 1 131 ? 6.69723   29.33340 27.69160 1.000 53.26081  ? 138 PHE   A CE2 1 
ATOM   945  C CZ  . PHE   A 1 131 ? 5.61103   28.52625 27.41895 1.000 47.82922  ? 138 PHE   A CZ  1 
ATOM   946  N N   . TYR   A 1 132 ? 6.87041   31.70918 31.61103 1.000 50.41598  ? 139 TYR   A N   1 
ATOM   947  C CA  . TYR   A 1 132 ? 7.78423   30.71812 32.15690 1.000 52.24564  ? 139 TYR   A CA  1 
ATOM   948  C C   . TYR   A 1 132 ? 7.45811   30.33577 33.59476 1.000 57.59855  ? 139 TYR   A C   1 
ATOM   949  O O   . TYR   A 1 132 ? 8.05813   29.38828 34.11203 1.000 51.73305  ? 139 TYR   A O   1 
ATOM   950  C CB  . TYR   A 1 132 ? 9.21668   31.23109 32.02572 1.000 42.36769  ? 139 TYR   A CB  1 
ATOM   951  C CG  . TYR   A 1 132 ? 9.61830   31.34674 30.57520 1.000 50.89653  ? 139 TYR   A CG  1 
ATOM   952  C CD1 . TYR   A 1 132 ? 9.79262   30.21063 29.79918 1.000 55.27138  ? 139 TYR   A CD1 1 
ATOM   953  C CD2 . TYR   A 1 132 ? 9.78225   32.58523 29.96993 1.000 59.47256  ? 139 TYR   A CD2 1 
ATOM   954  C CE1 . TYR   A 1 132 ? 10.14220  30.29866 28.46833 1.000 60.20596  ? 139 TYR   A CE1 1 
ATOM   955  C CE2 . TYR   A 1 132 ? 10.13342  32.68395 28.63358 1.000 61.55244  ? 139 TYR   A CE2 1 
ATOM   956  C CZ  . TYR   A 1 132 ? 10.31134  31.53344 27.88878 1.000 60.40191  ? 139 TYR   A CZ  1 
ATOM   957  O OH  . TYR   A 1 132 ? 10.66085  31.60898 26.55937 1.000 73.52760  ? 139 TYR   A OH  1 
ATOM   958  N N   . SER   A 1 133 ? 6.51211   31.02154 34.24322 1.000 53.68841  ? 140 SER   A N   1 
ATOM   959  C CA  . SER   A 1 133 ? 6.00788   30.54595 35.52512 1.000 41.71523  ? 140 SER   A CA  1 
ATOM   960  C C   . SER   A 1 133 ? 5.24239   29.24068 35.38580 1.000 53.68022  ? 140 SER   A C   1 
ATOM   961  O O   . SER   A 1 133 ? 4.89274   28.63387 36.40452 1.000 54.30504  ? 140 SER   A O   1 
ATOM   962  C CB  . SER   A 1 133 ? 5.10972   31.59839 36.17909 1.000 49.09888  ? 140 SER   A CB  1 
ATOM   963  O OG  . SER   A 1 133 ? 3.91479   31.78244 35.44106 1.000 43.20771  ? 140 SER   A OG  1 
ATOM   964  N N   . ALA   A 1 134 ? 4.96681   28.80890 34.15191 1.000 51.88686  ? 141 ALA   A N   1 
ATOM   965  C CA  . ALA   A 1 134 ? 4.37068   27.49863 33.92943 1.000 49.20574  ? 141 ALA   A CA  1 
ATOM   966  C C   . ALA   A 1 134 ? 5.22690   26.39291 34.52371 1.000 49.02262  ? 141 ALA   A C   1 
ATOM   967  O O   . ALA   A 1 134 ? 4.69806   25.36661 34.96384 1.000 44.48528  ? 141 ALA   A O   1 
ATOM   968  C CB  . ALA   A 1 134 ? 4.17330   27.26567 32.43213 1.000 50.60093  ? 141 ALA   A CB  1 
ATOM   969  N N   . TYR   A 1 135 ? 6.54433   26.58792 34.55481 1.000 45.20590  ? 142 TYR   A N   1 
ATOM   970  C CA  . TYR   A 1 135 ? 7.47037   25.57853 35.04681 1.000 55.17252  ? 142 TYR   A CA  1 
ATOM   971  C C   . TYR   A 1 135 ? 7.56024   25.54371 36.56468 1.000 54.04365  ? 142 TYR   A C   1 
ATOM   972  O O   . TYR   A 1 135 ? 8.38835   24.80072 37.10280 1.000 58.35159  ? 142 TYR   A O   1 
ATOM   973  C CB  . TYR   A 1 135 ? 8.84978   25.80406 34.42639 1.000 49.88593  ? 142 TYR   A CB  1 
ATOM   974  C CG  . TYR   A 1 135 ? 8.84217   25.50173 32.94972 1.000 54.30700  ? 142 TYR   A CG  1 
ATOM   975  C CD1 . TYR   A 1 135 ? 9.01306   24.20271 32.48946 1.000 48.07121  ? 142 TYR   A CD1 1 
ATOM   976  C CD2 . TYR   A 1 135 ? 8.61217   26.50575 32.01544 1.000 46.42057  ? 142 TYR   A CD2 1 
ATOM   977  C CE1 . TYR   A 1 135 ? 8.98284   23.91551 31.13862 1.000 39.75752  ? 142 TYR   A CE1 1 
ATOM   978  C CE2 . TYR   A 1 135 ? 8.57798   26.22817 30.65894 1.000 46.12633  ? 142 TYR   A CE2 1 
ATOM   979  C CZ  . TYR   A 1 135 ? 8.76474   24.92932 30.22926 1.000 56.68789  ? 142 TYR   A CZ  1 
ATOM   980  O OH  . TYR   A 1 135 ? 8.73534   24.63466 28.88671 1.000 50.24701  ? 142 TYR   A OH  1 
ATOM   981  N N   . LEU   A 1 136 ? 6.73460   26.32486 37.26531 1.000 47.95249  ? 143 LEU   A N   1 
ATOM   982  C CA  . LEU   A 1 136 ? 6.56079   26.10154 38.69575 1.000 44.71365  ? 143 LEU   A CA  1 
ATOM   983  C C   . LEU   A 1 136 ? 5.75793   24.83527 38.95542 1.000 57.36737  ? 143 LEU   A C   1 
ATOM   984  O O   . LEU   A 1 136 ? 6.00743   24.13330 39.94179 1.000 50.17752  ? 143 LEU   A O   1 
ATOM   985  C CB  . LEU   A 1 136 ? 5.86071   27.29478 39.34797 1.000 58.98649  ? 143 LEU   A CB  1 
ATOM   986  C CG  . LEU   A 1 136 ? 6.51115   28.67885 39.31046 1.000 50.20133  ? 143 LEU   A CG  1 
ATOM   987  C CD1 . LEU   A 1 136 ? 5.44161   29.73640 39.45281 1.000 46.85898  ? 143 LEU   A CD1 1 
ATOM   988  C CD2 . LEU   A 1 136 ? 7.54853   28.82007 40.41308 1.000 44.64697  ? 143 LEU   A CD2 1 
ATOM   989  N N   . VAL   A 1 137 ? 4.80052   24.52894 38.08371 1.000 49.49657  ? 144 VAL   A N   1 
ATOM   990  C CA  . VAL   A 1 137 ? 3.90516   23.39391 38.27986 1.000 57.41883  ? 144 VAL   A CA  1 
ATOM   991  C C   . VAL   A 1 137 ? 4.01717   22.34694 37.18245 1.000 51.71371  ? 144 VAL   A C   1 
ATOM   992  O O   . VAL   A 1 137 ? 3.43356   21.26308 37.32804 1.000 52.19085  ? 144 VAL   A O   1 
ATOM   993  C CB  . VAL   A 1 137 ? 2.43840   23.85697 38.41192 1.000 50.54859  ? 144 VAL   A CB  1 
ATOM   994  C CG1 . VAL   A 1 137 ? 2.29793   24.85744 39.55033 1.000 53.13132  ? 144 VAL   A CG1 1 
ATOM   995  C CG2 . VAL   A 1 137 ? 1.95115   24.45600 37.10059 1.000 42.65559  ? 144 VAL   A CG2 1 
ATOM   996  N N   . ALA   A 1 138 ? 4.73375   22.61600 36.09446 1.000 48.69345  ? 145 ALA   A N   1 
ATOM   997  C CA  . ALA   A 1 138 ? 4.79080   21.71399 34.95186 1.000 46.59624  ? 145 ALA   A CA  1 
ATOM   998  C C   . ALA   A 1 138 ? 6.22431   21.26349 34.71601 1.000 52.38493  ? 145 ALA   A C   1 
ATOM   999  O O   . ALA   A 1 138 ? 7.14892   22.08303 34.73481 1.000 54.44857  ? 145 ALA   A O   1 
ATOM   1000 C CB  . ALA   A 1 138 ? 4.23438   22.38222 33.69163 1.000 39.83173  ? 145 ALA   A CB  1 
ATOM   1001 N N   . GLU   A 1 139 ? 6.40441   19.95713 34.50577 1.000 52.19455  ? 146 GLU   A N   1 
ATOM   1002 C CA  . GLU   A 1 139 ? 7.69501   19.43337 34.08031 1.000 57.82608  ? 146 GLU   A CA  1 
ATOM   1003 C C   . GLU   A 1 139 ? 7.92073   19.61434 32.58633 1.000 53.49087  ? 146 GLU   A C   1 
ATOM   1004 O O   . GLU   A 1 139 ? 9.07428   19.62293 32.14069 1.000 52.23035  ? 146 GLU   A O   1 
ATOM   1005 C CB  . GLU   A 1 139 ? 7.81006   17.94911 34.44062 1.000 53.91483  ? 146 GLU   A CB  1 
ATOM   1006 C CG  . GLU   A 1 139 ? 6.82212   17.05931 33.70089 1.000 63.95895  ? 146 GLU   A CG  1 
ATOM   1007 C CD  . GLU   A 1 139 ? 6.66445   15.69019 34.33779 1.000 86.18786  ? 146 GLU   A CD  1 
ATOM   1008 O OE1 . GLU   A 1 139 ? 5.88949   14.86936 33.80014 1.000 86.32489  ? 146 GLU   A OE1 1 
ATOM   1009 O OE2 . GLU   A 1 139 ? 7.31843   15.43112 35.37038 1.000 93.81086  ? 146 GLU   A OE2 1 
ATOM   1010 N N   . LYS   A 1 140 ? 6.84675   19.76277 31.81265 1.000 47.26958  ? 147 LYS   A N   1 
ATOM   1011 C CA  . LYS   A 1 140 ? 6.92845   19.90641 30.36837 1.000 51.60414  ? 147 LYS   A CA  1 
ATOM   1012 C C   . LYS   A 1 140 ? 5.74594   20.73722 29.89643 1.000 47.67769  ? 147 LYS   A C   1 
ATOM   1013 O O   . LYS   A 1 140 ? 4.62116   20.55913 30.37455 1.000 46.55121  ? 147 LYS   A O   1 
ATOM   1014 C CB  . LYS   A 1 140 ? 6.93822   18.54229 29.66833 1.000 49.76987  ? 147 LYS   A CB  1 
ATOM   1015 C CG  . LYS   A 1 140 ? 6.70262   18.61162 28.16472 1.000 47.00861  ? 147 LYS   A CG  1 
ATOM   1016 C CD  . LYS   A 1 140 ? 7.19654   17.34682 27.47103 1.000 55.06000  ? 147 LYS   A CD  1 
ATOM   1017 C CE  . LYS   A 1 140 ? 6.06022   16.59006 26.80106 1.000 60.87848  ? 147 LYS   A CE  1 
ATOM   1018 N NZ  . LYS   A 1 140 ? 6.42116   15.16845 26.53869 1.000 75.19856  ? 147 LYS   A NZ  1 
ATOM   1019 N N   . VAL   A 1 141 ? 6.01152   21.65150 28.96897 1.000 40.15142  ? 148 VAL   A N   1 
ATOM   1020 C CA  . VAL   A 1 141 ? 4.99692   22.53243 28.40789 1.000 41.65530  ? 148 VAL   A CA  1 
ATOM   1021 C C   . VAL   A 1 141 ? 4.98407   22.34134 26.89922 1.000 40.43459  ? 148 VAL   A C   1 
ATOM   1022 O O   . VAL   A 1 141 ? 6.03681   22.40375 26.25304 1.000 42.85500  ? 148 VAL   A O   1 
ATOM   1023 C CB  . VAL   A 1 141 ? 5.25969   24.00796 28.76619 1.000 41.38461  ? 148 VAL   A CB  1 
ATOM   1024 C CG1 . VAL   A 1 141 ? 4.25838   24.91415 28.06241 1.000 35.87543  ? 148 VAL   A CG1 1 
ATOM   1025 C CG2 . VAL   A 1 141 ? 5.20097   24.21411 30.27236 1.000 41.85554  ? 148 VAL   A CG2 1 
ATOM   1026 N N   . THR   A 1 142 ? 3.79780   22.10190 26.34552 1.000 46.81660  ? 149 THR   A N   1 
ATOM   1027 C CA  . THR   A 1 142 ? 3.57988   22.07941 24.90509 1.000 39.18433  ? 149 THR   A CA  1 
ATOM   1028 C C   . THR   A 1 142 ? 2.66747   23.23444 24.52201 1.000 47.80313  ? 149 THR   A C   1 
ATOM   1029 O O   . THR   A 1 142 ? 1.64525   23.46970 25.17809 1.000 43.67557  ? 149 THR   A O   1 
ATOM   1030 C CB  . THR   A 1 142 ? 2.96059   20.75897 24.45198 1.000 39.06909  ? 149 THR   A CB  1 
ATOM   1031 O OG1 . THR   A 1 142 ? 3.69350   19.67305 25.02305 1.000 47.90666  ? 149 THR   A OG1 1 
ATOM   1032 C CG2 . THR   A 1 142 ? 2.99441   20.64860 22.93089 1.000 44.66250  ? 149 THR   A CG2 1 
ATOM   1033 N N   . VAL   A 1 143 ? 3.03556   23.95304 23.46646 1.000 40.96937  ? 150 VAL   A N   1 
ATOM   1034 C CA  . VAL   A 1 143 ? 2.25659   25.08423 22.97992 1.000 38.20117  ? 150 VAL   A CA  1 
ATOM   1035 C C   . VAL   A 1 143 ? 1.87338   24.81039 21.53175 1.000 47.04368  ? 150 VAL   A C   1 
ATOM   1036 O O   . VAL   A 1 143 ? 2.74674   24.63877 20.67211 1.000 49.94814  ? 150 VAL   A O   1 
ATOM   1037 C CB  . VAL   A 1 143 ? 3.02460   26.40811 23.11468 1.000 47.62078  ? 150 VAL   A CB  1 
ATOM   1038 C CG1 . VAL   A 1 143 ? 2.16545   27.57159 22.64181 1.000 40.84885  ? 150 VAL   A CG1 1 
ATOM   1039 C CG2 . VAL   A 1 143 ? 3.44956   26.61807 24.56058 1.000 44.73806  ? 150 VAL   A CG2 1 
ATOM   1040 N N   . ILE   A 1 144 ? 0.57088   24.72893 21.27551 1.000 47.52952  ? 151 ILE   A N   1 
ATOM   1041 C CA  . ILE   A 1 144 ? 0.01697   24.67584 19.92799 1.000 49.31602  ? 151 ILE   A CA  1 
ATOM   1042 C C   . ILE   A 1 144 ? -0.49713  26.06848 19.60048 1.000 51.02395  ? 151 ILE   A C   1 
ATOM   1043 O O   . ILE   A 1 144 ? -1.25027  26.65587 20.38788 1.000 47.51027  ? 151 ILE   A O   1 
ATOM   1044 C CB  . ILE   A 1 144 ? -1.10922  23.62999 19.82603 1.000 48.73669  ? 151 ILE   A CB  1 
ATOM   1045 C CG1 . ILE   A 1 144 ? -0.71084  22.33560 20.53793 1.000 42.43379  ? 151 ILE   A CG1 1 
ATOM   1046 C CG2 . ILE   A 1 144 ? -1.46129  23.35253 18.37491 1.000 46.58436  ? 151 ILE   A CG2 1 
ATOM   1047 C CD1 . ILE   A 1 144 ? 0.37372   21.56759 19.82538 1.000 46.63245  ? 151 ILE   A CD1 1 
ATOM   1048 N N   . THR   A 1 145 ? -0.08141  26.61424 18.45938 1.000 47.59296  ? 152 THR   A N   1 
ATOM   1049 C CA  . THR   A 1 145 ? -0.42623  27.99151 18.13338 1.000 51.19510  ? 152 THR   A CA  1 
ATOM   1050 C C   . THR   A 1 145 ? -0.68029  28.13388 16.64026 1.000 44.81822  ? 152 THR   A C   1 
ATOM   1051 O O   . THR   A 1 145 ? -0.13001  27.39123 15.82280 1.000 48.44332  ? 152 THR   A O   1 
ATOM   1052 C CB  . THR   A 1 145 ? 0.66793   28.97305 18.58499 1.000 40.67781  ? 152 THR   A CB  1 
ATOM   1053 O OG1 . THR   A 1 145 ? 0.16574   30.31169 18.51645 1.000 47.35807  ? 152 THR   A OG1 1 
ATOM   1054 C CG2 . THR   A 1 145 ? 1.90148   28.85820 17.71084 1.000 43.08118  ? 152 THR   A CG2 1 
ATOM   1055 N N   . LYS   A 1 146 ? -1.53502  29.09485 16.29647 1.000 40.58488  ? 153 LYS   A N   1 
ATOM   1056 C CA  . LYS   A 1 146 ? -1.91018  29.33325 14.90686 1.000 48.19696  ? 153 LYS   A CA  1 
ATOM   1057 C C   . LYS   A 1 146 ? -2.13082  30.82408 14.70745 1.000 47.67447  ? 153 LYS   A C   1 
ATOM   1058 O O   . LYS   A 1 146 ? -3.00144  31.41359 15.35357 1.000 42.51122  ? 153 LYS   A O   1 
ATOM   1059 C CB  . LYS   A 1 146 ? -3.16893  28.54552 14.53170 1.000 44.21476  ? 153 LYS   A CB  1 
ATOM   1060 C CG  . LYS   A 1 146 ? -3.68305  28.82511 13.12578 1.000 37.39302  ? 153 LYS   A CG  1 
ATOM   1061 C CD  . LYS   A 1 146 ? -2.66494  28.41051 12.07155 1.000 41.61979  ? 153 LYS   A CD  1 
ATOM   1062 C CE  . LYS   A 1 146 ? -3.22811  28.54121 10.65798 1.000 41.21115  ? 153 LYS   A CE  1 
ATOM   1063 N NZ  . LYS   A 1 146 ? -3.24985  29.94590 10.16961 1.000 48.48621  ? 153 LYS   A NZ  1 
ATOM   1064 N N   . HIS   A 1 147 ? -1.34292  31.42121 13.81808 1.000 52.30942  ? 154 HIS   A N   1 
ATOM   1065 C CA  . HIS   A 1 147 ? -1.45138  32.82220 13.44178 1.000 35.50682  ? 154 HIS   A CA  1 
ATOM   1066 C C   . HIS   A 1 147 ? -2.03409  32.92097 12.03804 1.000 47.23388  ? 154 HIS   A C   1 
ATOM   1067 O O   . HIS   A 1 147 ? -1.78121  32.06136 11.18918 1.000 54.58734  ? 154 HIS   A O   1 
ATOM   1068 C CB  . HIS   A 1 147 ? -0.07411  33.50019 13.49740 1.000 43.81679  ? 154 HIS   A CB  1 
ATOM   1069 C CG  . HIS   A 1 147 ? -0.11391  34.99320 13.37968 1.000 47.97955  ? 154 HIS   A CG  1 
ATOM   1070 N ND1 . HIS   A 1 147 ? -0.31406  35.64150 12.17944 1.000 50.81189  ? 154 HIS   A ND1 1 
ATOM   1071 C CD2 . HIS   A 1 147 ? 0.05340   35.96516 14.30814 1.000 42.09903  ? 154 HIS   A CD2 1 
ATOM   1072 C CE1 . HIS   A 1 147 ? -0.28558  36.94740 12.37634 1.000 47.25279  ? 154 HIS   A CE1 1 
ATOM   1073 N NE2 . HIS   A 1 147 ? -0.06303  37.17034 13.65925 1.000 42.27071  ? 154 HIS   A NE2 1 
ATOM   1074 N N   . ASN   A 1 148 ? -2.82120  33.97813 11.79781 1.000 49.19219  ? 155 ASN   A N   1 
ATOM   1075 C CA  . ASN   A 1 148 ? -3.44732  34.16131 10.48805 1.000 43.10038  ? 155 ASN   A CA  1 
ATOM   1076 C C   . ASN   A 1 148 ? -2.42877  34.14916 9.35506  1.000 42.22794  ? 155 ASN   A C   1 
ATOM   1077 O O   . ASN   A 1 148 ? -2.74907  33.74255 8.23118  1.000 45.86983  ? 155 ASN   A O   1 
ATOM   1078 C CB  . ASN   A 1 148 ? -4.22567  35.48099 10.44233 1.000 48.34561  ? 155 ASN   A CB  1 
ATOM   1079 C CG  . ASN   A 1 148 ? -5.57730  35.39627 11.12740 1.000 62.08407  ? 155 ASN   A CG  1 
ATOM   1080 O OD1 . ASN   A 1 148 ? -6.15917  34.31753 11.26064 1.000 50.57888  ? 155 ASN   A OD1 1 
ATOM   1081 N ND2 . ASN   A 1 148 ? -6.09058  36.54600 11.55783 1.000 50.38779  ? 155 ASN   A ND2 1 
ATOM   1082 N N   . ASP   A 1 149 ? -1.20594  34.59821 9.62197  1.000 41.55129  ? 156 ASP   A N   1 
ATOM   1083 C CA  . ASP   A 1 149 ? -0.19034  34.74922 8.59064  1.000 54.90531  ? 156 ASP   A CA  1 
ATOM   1084 C C   . ASP   A 1 149 ? 0.79738   33.58629 8.54736  1.000 63.28700  ? 156 ASP   A C   1 
ATOM   1085 O O   . ASP   A 1 149 ? 1.84225   33.70048 7.89599  1.000 52.72337  ? 156 ASP   A O   1 
ATOM   1086 C CB  . ASP   A 1 149 ? 0.56078   36.06759 8.79262  1.000 55.86246  ? 156 ASP   A CB  1 
ATOM   1087 C CG  . ASP   A 1 149 ? -0.36309  37.27491 8.77956  1.000 67.81578  ? 156 ASP   A CG  1 
ATOM   1088 O OD1 . ASP   A 1 149 ? -1.52100  37.13946 8.32896  1.000 69.64013  ? 156 ASP   A OD1 1 
ATOM   1089 O OD2 . ASP   A 1 149 ? 0.06752   38.36003 9.22510  1.000 68.70123  ? 156 ASP   A OD2 1 
ATOM   1090 N N   . ASP   A 1 150 ? 0.49498   32.47195 9.21246  1.000 47.94198  ? 157 ASP   A N   1 
ATOM   1091 C CA  . ASP   A 1 150 ? 1.42518   31.35469 9.27357  1.000 47.90743  ? 157 ASP   A CA  1 
ATOM   1092 C C   . ASP   A 1 150 ? 0.63546   30.06102 9.43053  1.000 49.87859  ? 157 ASP   A C   1 
ATOM   1093 O O   . ASP   A 1 150 ? -0.59601  30.06596 9.49830  1.000 53.02904  ? 157 ASP   A O   1 
ATOM   1094 C CB  . ASP   A 1 150 ? 2.43019   31.55138 10.41239 1.000 52.80710  ? 157 ASP   A CB  1 
ATOM   1095 C CG  . ASP   A 1 150 ? 3.80409   31.00591 10.07853 1.000 60.57884  ? 157 ASP   A CG  1 
ATOM   1096 O OD1 . ASP   A 1 150 ? 3.89834   30.12783 9.19415  1.000 60.21374  ? 157 ASP   A OD1 1 
ATOM   1097 O OD2 . ASP   A 1 150 ? 4.79027   31.45920 10.70035 1.000 61.37999  ? 157 ASP   A OD2 1 
ATOM   1098 N N   . GLU   A 1 151 ? 1.35583   28.94407 9.47997  1.000 51.12594  ? 158 GLU   A N   1 
ATOM   1099 C CA  . GLU   A 1 151 ? 0.73832   27.64031 9.66236  1.000 48.85552  ? 158 GLU   A CA  1 
ATOM   1100 C C   . GLU   A 1 151 ? 0.64158   27.30554 11.14785 1.000 45.75081  ? 158 GLU   A C   1 
ATOM   1101 O O   . GLU   A 1 151 ? 1.11234   28.04649 12.01032 1.000 46.04123  ? 158 GLU   A O   1 
ATOM   1102 C CB  . GLU   A 1 151 ? 1.53031   26.56183 8.92320  1.000 54.77858  ? 158 GLU   A CB  1 
ATOM   1103 C CG  . GLU   A 1 151 ? 1.09166   26.33968 7.48688  1.000 53.40651  ? 158 GLU   A CG  1 
ATOM   1104 C CD  . GLU   A 1 151 ? 1.96551   25.33136 6.76218  1.000 87.51065  ? 158 GLU   A CD  1 
ATOM   1105 O OE1 . GLU   A 1 151 ? 1.84669   24.12071 7.04764  1.000 88.25774  ? 158 GLU   A OE1 1 
ATOM   1106 O OE2 . GLU   A 1 151 ? 2.77238   25.74898 5.90530  1.000 96.64265  ? 158 GLU   A OE2 1 
ATOM   1107 N N   . GLN   A 1 152 ? 0.01709   26.16929 11.44336 1.000 47.00571  ? 159 GLN   A N   1 
ATOM   1108 C CA  . GLN   A 1 152 ? -0.09831  25.70132 12.81788 1.000 43.52348  ? 159 GLN   A CA  1 
ATOM   1109 C C   . GLN   A 1 152 ? 1.20922   25.04726 13.25251 1.000 49.85616  ? 159 GLN   A C   1 
ATOM   1110 O O   . GLN   A 1 152 ? 1.75194   24.19639 12.54166 1.000 57.54212  ? 159 GLN   A O   1 
ATOM   1111 C CB  . GLN   A 1 152 ? -1.25863  24.71604 12.94358 1.000 48.64629  ? 159 GLN   A CB  1 
ATOM   1112 C CG  . GLN   A 1 152 ? -1.67142  24.40293 14.37056 1.000 48.16076  ? 159 GLN   A CG  1 
ATOM   1113 C CD  . GLN   A 1 152 ? -3.10910  23.92048 14.45849 1.000 52.81822  ? 159 GLN   A CD  1 
ATOM   1114 O OE1 . GLN   A 1 152 ? -4.03306  24.60261 14.01323 1.000 58.85786  ? 159 GLN   A OE1 1 
ATOM   1115 N NE2 . GLN   A 1 152 ? -3.30464  22.74229 15.03561 1.000 52.31586  ? 159 GLN   A NE2 1 
ATOM   1116 N N   . TYR   A 1 153 ? 1.71755   25.44462 14.41834 1.000 47.14978  ? 160 TYR   A N   1 
ATOM   1117 C CA  . TYR   A 1 153 ? 2.99699   24.95161 14.90570 1.000 45.54061  ? 160 TYR   A CA  1 
ATOM   1118 C C   . TYR   A 1 153 ? 2.85067   24.42076 16.32236 1.000 48.24464  ? 160 TYR   A C   1 
ATOM   1119 O O   . TYR   A 1 153 ? 1.95762   24.83229 17.07017 1.000 48.97476  ? 160 TYR   A O   1 
ATOM   1120 C CB  . TYR   A 1 153 ? 4.08533   26.03713 14.89488 1.000 48.52136  ? 160 TYR   A CB  1 
ATOM   1121 C CG  . TYR   A 1 153 ? 4.56842   26.42272 13.51536 1.000 56.28518  ? 160 TYR   A CG  1 
ATOM   1122 C CD1 . TYR   A 1 153 ? 4.01665   27.50882 12.84321 1.000 57.61235  ? 160 TYR   A CD1 1 
ATOM   1123 C CD2 . TYR   A 1 153 ? 5.55320   25.68647 12.87289 1.000 52.13143  ? 160 TYR   A CD2 1 
ATOM   1124 C CE1 . TYR   A 1 153 ? 4.45453   27.86496 11.57707 1.000 59.50213  ? 160 TYR   A CE1 1 
ATOM   1125 C CE2 . TYR   A 1 153 ? 5.99385   26.02994 11.61106 1.000 57.47026  ? 160 TYR   A CE2 1 
ATOM   1126 C CZ  . TYR   A 1 153 ? 5.44015   27.11955 10.96655 1.000 61.67389  ? 160 TYR   A CZ  1 
ATOM   1127 O OH  . TYR   A 1 153 ? 5.87471   27.46536 9.70842  1.000 70.39242  ? 160 TYR   A OH  1 
ATOM   1128 N N   . ALA   A 1 154 ? 3.75866   23.51385 16.68516 1.000 49.32374  ? 161 ALA   A N   1 
ATOM   1129 C CA  . ALA   A 1 154 ? 3.81075   22.91172 18.01128 1.000 45.85609  ? 161 ALA   A CA  1 
ATOM   1130 C C   . ALA   A 1 154 ? 5.16296   23.21560 18.64392 1.000 50.95398  ? 161 ALA   A C   1 
ATOM   1131 O O   . ALA   A 1 154 ? 6.20534   22.79412 18.12850 1.000 51.55382  ? 161 ALA   A O   1 
ATOM   1132 C CB  . ALA   A 1 154 ? 3.57507   21.40102 17.93670 1.000 38.28286  ? 161 ALA   A CB  1 
ATOM   1133 N N   . TRP   A 1 155 ? 5.13793   23.94723 19.75350 1.000 41.33397  ? 162 TRP   A N   1 
ATOM   1134 C CA  . TRP   A 1 155 ? 6.31735   24.27638 20.54222 1.000 38.68857  ? 162 TRP   A CA  1 
ATOM   1135 C C   . TRP   A 1 155 ? 6.33276   23.40955 21.79354 1.000 48.25337  ? 162 TRP   A C   1 
ATOM   1136 O O   . TRP   A 1 155 ? 5.28340   23.14426 22.38721 1.000 45.54455  ? 162 TRP   A O   1 
ATOM   1137 C CB  . TRP   A 1 155 ? 6.29581   25.75871 20.92395 1.000 37.04639  ? 162 TRP   A CB  1 
ATOM   1138 C CG  . TRP   A 1 155 ? 7.45669   26.28303 21.73016 1.000 47.00679  ? 162 TRP   A CG  1 
ATOM   1139 C CD1 . TRP   A 1 155 ? 8.53473   26.98014 21.25873 1.000 45.64645  ? 162 TRP   A CD1 1 
ATOM   1140 C CD2 . TRP   A 1 155 ? 7.62523   26.20351 23.15356 1.000 47.38524  ? 162 TRP   A CD2 1 
ATOM   1141 N NE1 . TRP   A 1 155 ? 9.36825   27.32392 22.29635 1.000 41.24836  ? 162 TRP   A NE1 1 
ATOM   1142 C CE2 . TRP   A 1 155 ? 8.83307   26.86007 23.46913 1.000 37.80037  ? 162 TRP   A CE2 1 
ATOM   1143 C CE3 . TRP   A 1 155 ? 6.87582   25.63483 24.19002 1.000 44.79670  ? 162 TRP   A CE3 1 
ATOM   1144 C CZ2 . TRP   A 1 155 ? 9.31111   26.95879 24.77526 1.000 42.19184  ? 162 TRP   A CZ2 1 
ATOM   1145 C CZ3 . TRP   A 1 155 ? 7.34901   25.73792 25.48594 1.000 45.59592  ? 162 TRP   A CZ3 1 
ATOM   1146 C CH2 . TRP   A 1 155 ? 8.55694   26.39514 25.76725 1.000 43.62744  ? 162 TRP   A CH2 1 
ATOM   1147 N N   . GLU   A 1 156 ? 7.52203   22.97134 22.19550 1.000 38.23560  ? 163 GLU   A N   1 
ATOM   1148 C CA  . GLU   A 1 156 ? 7.63670   22.07028 23.33099 1.000 39.15792  ? 163 GLU   A CA  1 
ATOM   1149 C C   . GLU   A 1 156 ? 8.98656   22.24208 24.00305 1.000 45.67934  ? 163 GLU   A C   1 
ATOM   1150 O O   . GLU   A 1 156 ? 10.01897  22.30315 23.32897 1.000 38.76959  ? 163 GLU   A O   1 
ATOM   1151 C CB  . GLU   A 1 156 ? 7.47508   20.61388 22.89706 1.000 36.60518  ? 163 GLU   A CB  1 
ATOM   1152 C CG  . GLU   A 1 156 ? 7.27917   19.66840 24.05136 1.000 51.68201  ? 163 GLU   A CG  1 
ATOM   1153 C CD  . GLU   A 1 156 ? 6.80313   18.31272 23.59591 1.000 67.46177  ? 163 GLU   A CD  1 
ATOM   1154 O OE1 . GLU   A 1 156 ? 7.58187   17.60393 22.92022 1.000 73.65186  ? 163 GLU   A OE1 1 
ATOM   1155 O OE2 . GLU   A 1 156 ? 5.64405   17.96384 23.90227 1.000 59.90632  ? 163 GLU   A OE2 1 
ATOM   1156 N N   . SER   A 1 157 ? 8.97706   22.29028 25.33239 1.000 49.73286  ? 164 SER   A N   1 
ATOM   1157 C CA  . SER   A 1 157 ? 10.22403  22.26920 26.07912 1.000 51.04541  ? 164 SER   A CA  1 
ATOM   1158 C C   . SER   A 1 157 ? 9.98684   21.66218 27.45183 1.000 53.81412  ? 164 SER   A C   1 
ATOM   1159 O O   . SER   A 1 157 ? 8.96843   21.93681 28.09533 1.000 48.70408  ? 164 SER   A O   1 
ATOM   1160 C CB  . SER   A 1 157 ? 10.82346  23.67140 26.22590 1.000 45.53439  ? 164 SER   A CB  1 
ATOM   1161 O OG  . SER   A 1 157 ? 12.06207  23.60567 26.91311 1.000 49.35174  ? 164 SER   A OG  1 
ATOM   1162 N N   . SER   A 1 158 ? 10.93114  20.82135 27.87890 1.000 48.85219  ? 165 SER   A N   1 
ATOM   1163 C CA  . SER   A 1 158 ? 11.03272  20.35642 29.25631 1.000 43.97315  ? 165 SER   A CA  1 
ATOM   1164 C C   . SER   A 1 158 ? 12.13026  21.09372 30.01676 1.000 52.97310  ? 165 SER   A C   1 
ATOM   1165 O O   . SER   A 1 158 ? 12.70809  20.54657 30.96264 1.000 52.31997  ? 165 SER   A O   1 
ATOM   1166 C CB  . SER   A 1 158 ? 11.28427  18.84744 29.29598 1.000 45.33012  ? 165 SER   A CB  1 
ATOM   1167 O OG  . SER   A 1 158 ? 10.24152  18.13195 28.65846 1.000 56.28823  ? 165 SER   A OG  1 
ATOM   1168 N N   . ALA   A 1 159 ? 12.42086  22.32639 29.61675 1.000 51.22709  ? 166 ALA   A N   1 
ATOM   1169 C CA  . ALA   A 1 159 ? 13.56164  23.10312 30.12351 1.000 58.04789  ? 166 ALA   A CA  1 
ATOM   1170 C C   . ALA   A 1 159 ? 14.82293  22.30942 29.76985 1.000 48.59827  ? 166 ALA   A C   1 
ATOM   1171 O O   . ALA   A 1 159 ? 14.87649  21.69596 28.69292 1.000 64.49947  ? 166 ALA   A O   1 
ATOM   1172 C CB  . ALA   A 1 159 ? 13.37798  23.42253 31.58791 1.000 46.07647  ? 166 ALA   A CB  1 
ATOM   1173 N N   . GLY   A 1 160 ? 15.84247  22.29051 30.62345 1.000 44.76086  ? 167 GLY   A N   1 
ATOM   1174 C CA  . GLY   A 1 160 ? 17.06318  21.61382 30.23121 1.000 48.19538  ? 167 GLY   A CA  1 
ATOM   1175 C C   . GLY   A 1 160 ? 17.88366  22.34189 29.19111 1.000 49.35125  ? 167 GLY   A C   1 
ATOM   1176 O O   . GLY   A 1 160 ? 18.90880  21.81520 28.74779 1.000 48.87529  ? 167 GLY   A O   1 
ATOM   1177 N N   . GLY   A 1 161 ? 17.45705  23.53361 28.77267 1.000 51.91922  ? 168 GLY   A N   1 
ATOM   1178 C CA  . GLY   A 1 161 ? 18.24546  24.38147 27.90449 1.000 56.25876  ? 168 GLY   A CA  1 
ATOM   1179 C C   . GLY   A 1 161 ? 17.83198  24.39420 26.44767 1.000 59.03566  ? 168 GLY   A C   1 
ATOM   1180 O O   . GLY   A 1 161 ? 18.42292  25.15036 25.66624 1.000 58.49493  ? 168 GLY   A O   1 
ATOM   1181 N N   . SER   A 1 162 ? 16.83735  23.59944 26.05611 1.000 47.40159  ? 169 SER   A N   1 
ATOM   1182 C CA  . SER   A 1 162 ? 16.46789  23.48918 24.65312 1.000 44.14348  ? 169 SER   A CA  1 
ATOM   1183 C C   . SER   A 1 162 ? 14.95395  23.41872 24.50263 1.000 48.77955  ? 169 SER   A C   1 
ATOM   1184 O O   . SER   A 1 162 ? 14.22180  23.10921 25.44688 1.000 49.67340  ? 169 SER   A O   1 
ATOM   1185 C CB  . SER   A 1 162 ? 17.10971  22.25622 24.00288 1.000 52.41686  ? 169 SER   A CB  1 
ATOM   1186 O OG  . SER   A 1 162 ? 16.51759  21.06791 24.49519 1.000 56.32443  ? 169 SER   A OG  1 
ATOM   1187 N N   . PHE   A 1 163 ? 14.49439  23.71369 23.28747 1.000 45.99844  ? 170 PHE   A N   1 
ATOM   1188 C CA  . PHE   A 1 163 ? 13.09509  23.56085 22.91975 1.000 46.23033  ? 170 PHE   A CA  1 
ATOM   1189 C C   . PHE   A 1 163 ? 13.01547  23.08310 21.47713 1.000 51.85046  ? 170 PHE   A C   1 
ATOM   1190 O O   . PHE   A 1 163 ? 13.96406  23.22848 20.69944 1.000 44.30615  ? 170 PHE   A O   1 
ATOM   1191 C CB  . PHE   A 1 163 ? 12.30227  24.86550 23.10609 1.000 43.35268  ? 170 PHE   A CB  1 
ATOM   1192 C CG  . PHE   A 1 163 ? 12.72713  25.98958 22.18834 1.000 55.83932  ? 170 PHE   A CG  1 
ATOM   1193 C CD1 . PHE   A 1 163 ? 13.76630  26.83862 22.54288 1.000 49.85927  ? 170 PHE   A CD1 1 
ATOM   1194 C CD2 . PHE   A 1 163 ? 12.06675  26.21505 20.98575 1.000 51.91333  ? 170 PHE   A CD2 1 
ATOM   1195 C CE1 . PHE   A 1 163 ? 14.15055  27.88242 21.70966 1.000 56.84941  ? 170 PHE   A CE1 1 
ATOM   1196 C CE2 . PHE   A 1 163 ? 12.44603  27.25517 20.14687 1.000 47.08689  ? 170 PHE   A CE2 1 
ATOM   1197 C CZ  . PHE   A 1 163 ? 13.48797  28.09110 20.51047 1.000 53.70582  ? 170 PHE   A CZ  1 
ATOM   1198 N N   . THR   A 1 164 ? 11.87427  22.49240 21.13110 1.000 47.20893  ? 171 THR   A N   1 
ATOM   1199 C CA  . THR   A 1 164 ? 11.62114  22.00833 19.78291 1.000 39.79554  ? 171 THR   A CA  1 
ATOM   1200 C C   . THR   A 1 164 ? 10.47326  22.78432 19.14805 1.000 44.46857  ? 171 THR   A C   1 
ATOM   1201 O O   . THR   A 1 164 ? 9.56717   23.26608 19.83377 1.000 45.59136  ? 171 THR   A O   1 
ATOM   1202 C CB  . THR   A 1 164 ? 11.28592  20.51228 19.77159 1.000 46.31137  ? 171 THR   A CB  1 
ATOM   1203 O OG1 . THR   A 1 164 ? 10.05407  20.29010 20.46798 1.000 52.01367  ? 171 THR   A OG1 1 
ATOM   1204 C CG2 . THR   A 1 164 ? 12.39274  19.70224 20.42796 1.000 42.58740  ? 171 THR   A CG2 1 
ATOM   1205 N N   . VAL   A 1 165 ? 10.52674  22.90670 17.82515 1.000 41.41147  ? 172 VAL   A N   1 
ATOM   1206 C CA  . VAL   A 1 165 ? 9.44482   23.47902 17.03868 1.000 44.27024  ? 172 VAL   A CA  1 
ATOM   1207 C C   . VAL   A 1 165 ? 9.18786   22.55929 15.85515 1.000 44.16911  ? 172 VAL   A C   1 
ATOM   1208 O O   . VAL   A 1 165 ? 10.12759  22.08149 15.20945 1.000 47.58014  ? 172 VAL   A O   1 
ATOM   1209 C CB  . VAL   A 1 165 ? 9.76682   24.91410 16.56654 1.000 48.96177  ? 172 VAL   A CB  1 
ATOM   1210 C CG1 . VAL   A 1 165 ? 8.67565   25.43203 15.63881 1.000 38.29473  ? 172 VAL   A CG1 1 
ATOM   1211 C CG2 . VAL   A 1 165 ? 9.92269   25.83893 17.75929 1.000 37.92935  ? 172 VAL   A CG2 1 
ATOM   1212 N N   . ARG   A 1 166 ? 7.91273   22.29836 15.58335 1.000 48.90723  ? 173 ARG   A N   1 
ATOM   1213 C CA  . ARG   A 1 166 ? 7.52223   21.46104 14.46062 1.000 50.07170  ? 173 ARG   A CA  1 
ATOM   1214 C C   . ARG   A 1 166 ? 6.17933   21.94429 13.93736 1.000 54.28440  ? 173 ARG   A C   1 
ATOM   1215 O O   . ARG   A 1 166 ? 5.42945   22.63381 14.63482 1.000 50.05529  ? 173 ARG   A O   1 
ATOM   1216 C CB  . ARG   A 1 166 ? 7.42962   19.98498 14.86159 1.000 53.59632  ? 173 ARG   A CB  1 
ATOM   1217 C CG  . ARG   A 1 166 ? 6.14114   19.63363 15.59954 1.000 56.71731  ? 173 ARG   A CG  1 
ATOM   1218 C CD  . ARG   A 1 166 ? 6.23184   18.27128 16.27019 1.000 58.24676  ? 173 ARG   A CD  1 
ATOM   1219 N NE  . ARG   A 1 166 ? 7.08493   18.32170 17.45209 1.000 68.09780  ? 173 ARG   A NE  1 
ATOM   1220 C CZ  . ARG   A 1 166 ? 7.67242   17.26794 18.00432 1.000 87.44958  ? 173 ARG   A CZ  1 
ATOM   1221 N NH1 . ARG   A 1 166 ? 7.52554   16.05041 17.50362 1.000 84.40609  ? 173 ARG   A NH1 1 
ATOM   1222 N NH2 . ARG   A 1 166 ? 8.42828   17.44026 19.08572 1.000 77.44765  ? 173 ARG   A NH2 1 
ATOM   1223 N N   . THR   A 1 167 ? 5.88505   21.58118 12.69372 1.000 48.56411  ? 174 THR   A N   1 
ATOM   1224 C CA  . THR   A 1 167 ? 4.54859   21.80209 12.16223 1.000 57.63848  ? 174 THR   A CA  1 
ATOM   1225 C C   . THR   A 1 167 ? 3.58750   20.81158 12.80413 1.000 58.17765  ? 174 THR   A C   1 
ATOM   1226 O O   . THR   A 1 167 ? 3.85184   19.60559 12.83696 1.000 74.46956  ? 174 THR   A O   1 
ATOM   1227 C CB  . THR   A 1 167 ? 4.53496   21.65164 10.63975 1.000 58.07537  ? 174 THR   A CB  1 
ATOM   1228 O OG1 . THR   A 1 167 ? 5.39749   22.63474 10.05542 1.000 63.35034  ? 174 THR   A OG1 1 
ATOM   1229 C CG2 . THR   A 1 167 ? 3.12484   21.84817 10.09621 1.000 63.73523  ? 174 THR   A CG2 1 
ATOM   1230 N N   . ASP   A 1 168 ? 2.48121   21.32228 13.33379 1.000 55.04875  ? 175 ASP   A N   1 
ATOM   1231 C CA  . ASP   A 1 168 ? 1.50193   20.46829 13.98552 1.000 59.36493  ? 175 ASP   A CA  1 
ATOM   1232 C C   . ASP   A 1 168 ? 0.58605   19.84413 12.94472 1.000 71.42709  ? 175 ASP   A C   1 
ATOM   1233 O O   . ASP   A 1 168 ? 0.05901   20.53724 12.06877 1.000 72.02329  ? 175 ASP   A O   1 
ATOM   1234 C CB  . ASP   A 1 168 ? 0.68683   21.25862 15.00558 1.000 53.68202  ? 175 ASP   A CB  1 
ATOM   1235 C CG  . ASP   A 1 168 ? -0.18773  20.36736 15.86156 1.000 64.30763  ? 175 ASP   A CG  1 
ATOM   1236 O OD1 . ASP   A 1 168 ? 0.31355   19.33291 16.34999 1.000 86.08846  ? 175 ASP   A OD1 1 
ATOM   1237 O OD2 . ASP   A 1 168 ? -1.37533  20.69955 16.04863 1.000 72.23657  ? 175 ASP   A OD2 1 
ATOM   1238 N N   . THR   A 1 169 ? 0.40693   18.53097 13.04226 1.000 82.15790  ? 176 THR   A N   1 
ATOM   1239 C CA  . THR   A 1 169 ? -0.45240  17.77835 12.14338 1.000 82.15352  ? 176 THR   A CA  1 
ATOM   1240 C C   . THR   A 1 169 ? -1.80317  17.44778 12.76260 1.000 85.82131  ? 176 THR   A C   1 
ATOM   1241 O O   . THR   A 1 169 ? -2.65486  16.86268 12.08482 1.000 94.95750  ? 176 THR   A O   1 
ATOM   1242 C CB  . THR   A 1 169 ? 0.25204   16.48865 11.71681 1.000 98.27800  ? 176 THR   A CB  1 
ATOM   1243 O OG1 . THR   A 1 169 ? 0.59494   15.72436 12.88178 1.000 92.27279  ? 176 THR   A OG1 1 
ATOM   1244 C CG2 . THR   A 1 169 ? 1.52319   16.81864 10.94909 1.000 93.01585  ? 176 THR   A CG2 1 
ATOM   1245 N N   . GLY   A 1 170 ? -2.02142  17.81837 14.02395 1.000 83.60213  ? 177 GLY   A N   1 
ATOM   1246 C CA  . GLY   A 1 170 ? -3.22828  17.46486 14.74278 1.000 88.44180  ? 177 GLY   A CA  1 
ATOM   1247 C C   . GLY   A 1 170 ? -4.43738  18.28983 14.35417 1.000 86.29077  ? 177 GLY   A C   1 
ATOM   1248 O O   . GLY   A 1 170 ? -4.50392  18.88178 13.27505 1.000 82.45100  ? 177 GLY   A O   1 
ATOM   1249 N N   . GLU   A 1 171 ? -5.41069  18.31891 15.26006 1.000 80.10915  ? 178 GLU   A N   1 
ATOM   1250 C CA  . GLU   A 1 171 ? -6.67546  19.00601 15.02972 1.000 79.38868  ? 178 GLU   A CA  1 
ATOM   1251 C C   . GLU   A 1 171 ? -6.44219  20.48901 14.75673 1.000 62.49385  ? 178 GLU   A C   1 
ATOM   1252 O O   . GLU   A 1 171 ? -5.88775  21.18711 15.61972 1.000 60.09058  ? 178 GLU   A O   1 
ATOM   1253 C CB  . GLU   A 1 171 ? -7.59173  18.83238 16.24064 1.000 84.14478  ? 178 GLU   A CB  1 
ATOM   1254 C CG  . GLU   A 1 171 ? -9.07434  18.93495 15.92598 1.000 94.68812  ? 178 GLU   A CG  1 
ATOM   1255 C CD  . GLU   A 1 171 ? -9.52550  17.91986 14.89272 1.000 115.80445 ? 178 GLU   A CD  1 
ATOM   1256 O OE1 . GLU   A 1 171 ? -9.21131  16.72068 15.05413 1.000 99.57688  ? 178 GLU   A OE1 1 
ATOM   1257 O OE2 . GLU   A 1 171 ? -10.20039 18.32123 13.92089 1.000 120.28795 ? 178 GLU   A OE2 1 
ATOM   1258 N N   . PRO   A 1 172 ? -6.83416  21.00435 13.58869 1.000 69.65231  ? 179 PRO   A N   1 
ATOM   1259 C CA  . PRO   A 1 172 ? -6.64581  22.43629 13.31448 1.000 61.07459  ? 179 PRO   A CA  1 
ATOM   1260 C C   . PRO   A 1 172 ? -7.40177  23.29984 14.31493 1.000 59.43213  ? 179 PRO   A C   1 
ATOM   1261 O O   . PRO   A 1 172 ? -8.55675  23.03136 14.65239 1.000 65.29522  ? 179 PRO   A O   1 
ATOM   1262 C CB  . PRO   A 1 172 ? -7.19893  22.60230 11.89298 1.000 46.87038  ? 179 PRO   A CB  1 
ATOM   1263 C CG  . PRO   A 1 172 ? -7.11152  21.22991 11.28881 1.000 53.93781  ? 179 PRO   A CG  1 
ATOM   1264 C CD  . PRO   A 1 172 ? -7.37198  20.28126 12.42268 1.000 66.28447  ? 179 PRO   A CD  1 
ATOM   1265 N N   . MET   A 1 173 ? -6.72878  24.34454 14.79562 1.000 54.79797  ? 180 MET   A N   1 
ATOM   1266 C CA  . MET   A 1 173 ? -7.31222  25.24984 15.77777 1.000 58.84989  ? 180 MET   A CA  1 
ATOM   1267 C C   . MET   A 1 173 ? -8.09648  26.39460 15.15424 1.000 54.86776  ? 180 MET   A C   1 
ATOM   1268 O O   . MET   A 1 173 ? -9.02669  26.91110 15.78526 1.000 65.45575  ? 180 MET   A O   1 
ATOM   1269 C CB  . MET   A 1 173 ? -6.21808  25.84202 16.66478 1.000 60.61038  ? 180 MET   A CB  1 
ATOM   1270 C CG  . MET   A 1 173 ? -5.98022  25.09938 17.95797 1.000 68.01052  ? 180 MET   A CG  1 
ATOM   1271 S SD  . MET   A 1 173 ? -4.62652  25.87738 18.84855 1.000 84.70553  ? 180 MET   A SD  1 
ATOM   1272 C CE  . MET   A 1 173 ? -3.57160  26.33616 17.47830 1.000 60.12436  ? 180 MET   A CE  1 
ATOM   1273 N N   . GLY   A 1 174 ? -7.73998  26.81158 13.94278 1.000 44.03259  ? 181 GLY   A N   1 
ATOM   1274 C CA  . GLY   A 1 174 ? -8.32737  28.00106 13.35853 1.000 55.56567  ? 181 GLY   A CA  1 
ATOM   1275 C C   . GLY   A 1 174 ? -7.48326  29.22586 13.64454 1.000 45.24311  ? 181 GLY   A C   1 
ATOM   1276 O O   . GLY   A 1 174 ? -6.85434  29.78233 12.74047 1.000 45.63064  ? 181 GLY   A O   1 
ATOM   1277 N N   . ARG   A 1 175 ? -7.44728  29.64116 14.90820 1.000 43.44385  ? 182 ARG   A N   1 
ATOM   1278 C CA  . ARG   A 1 175 ? -6.60743  30.74772 15.34589 1.000 45.28919  ? 182 ARG   A CA  1 
ATOM   1279 C C   . ARG   A 1 175 ? -6.53512  30.72848 16.86304 1.000 33.66681  ? 182 ARG   A C   1 
ATOM   1280 O O   . ARG   A 1 175 ? -7.53528  30.45771 17.52956 1.000 44.83999  ? 182 ARG   A O   1 
ATOM   1281 C CB  . ARG   A 1 175 ? -7.15063  32.09965 14.86067 1.000 38.38893  ? 182 ARG   A CB  1 
ATOM   1282 C CG  . ARG   A 1 175 ? -6.16159  33.24995 15.02203 1.000 44.97596  ? 182 ARG   A CG  1 
ATOM   1283 C CD  . ARG   A 1 175 ? -6.86001  34.60760 15.05095 1.000 47.91385  ? 182 ARG   A CD  1 
ATOM   1284 N NE  . ARG   A 1 175 ? -7.86135  34.69075 16.10802 1.000 40.38113  ? 182 ARG   A NE  1 
ATOM   1285 C CZ  . ARG   A 1 175 ? -9.17043  34.70094 15.90031 1.000 41.13053  ? 182 ARG   A CZ  1 
ATOM   1286 N NH1 . ARG   A 1 175 ? -9.67607  34.64387 14.67957 1.000 44.01020  ? 182 ARG   A NH1 1 
ATOM   1287 N NH2 . ARG   A 1 175 ? -9.99198  34.77690 16.94364 1.000 44.83756  ? 182 ARG   A NH2 1 
ATOM   1288 N N   . GLY   A 1 176 ? -5.35369  31.00676 17.40117 1.000 36.06369  ? 183 GLY   A N   1 
ATOM   1289 C CA  . GLY   A 1 176 ? -5.21907  31.10092 18.83459 1.000 38.88706  ? 183 GLY   A CA  1 
ATOM   1290 C C   . GLY   A 1 176 ? -4.02843  30.31194 19.31712 1.000 42.74423  ? 183 GLY   A C   1 
ATOM   1291 O O   . GLY   A 1 176 ? -3.17203  29.89516 18.53030 1.000 52.59594  ? 183 GLY   A O   1 
ATOM   1292 N N   . THR   A 1 177 ? -3.98680  30.10208 20.62911 1.000 43.29146  ? 184 THR   A N   1 
ATOM   1293 C CA  . THR   A 1 177 ? -2.87022  29.44356 21.28472 1.000 44.62297  ? 184 THR   A CA  1 
ATOM   1294 C C   . THR   A 1 177 ? -3.40677  28.48481 22.33624 1.000 48.98317  ? 184 THR   A C   1 
ATOM   1295 O O   . THR   A 1 177 ? -4.36120  28.79782 23.05436 1.000 46.28361  ? 184 THR   A O   1 
ATOM   1296 C CB  . THR   A 1 177 ? -1.92000  30.46786 21.92551 1.000 42.52660  ? 184 THR   A CB  1 
ATOM   1297 O OG1 . THR   A 1 177 ? -1.31009  31.25916 20.89666 1.000 54.46383  ? 184 THR   A OG1 1 
ATOM   1298 C CG2 . THR   A 1 177 ? -0.83723  29.77260 22.73604 1.000 44.58709  ? 184 THR   A CG2 1 
ATOM   1299 N N   . LYS   A 1 178 ? -2.79374  27.30978 22.40478 1.000 36.00637  ? 185 LYS   A N   1 
ATOM   1300 C CA  . LYS   A 1 178 ? -3.12912  26.28132 23.37712 1.000 41.87948  ? 185 LYS   A CA  1 
ATOM   1301 C C   . LYS   A 1 178 ? -1.86904  25.95581 24.16596 1.000 43.40281  ? 185 LYS   A C   1 
ATOM   1302 O O   . LYS   A 1 178 ? -0.86595  25.52793 23.58525 1.000 40.55327  ? 185 LYS   A O   1 
ATOM   1303 C CB  . LYS   A 1 178 ? -3.67956  25.03990 22.67003 1.000 43.70130  ? 185 LYS   A CB  1 
ATOM   1304 C CG  . LYS   A 1 178 ? -3.90272  23.84567 23.56232 1.000 52.74088  ? 185 LYS   A CG  1 
ATOM   1305 C CD  . LYS   A 1 178 ? -5.05984  22.99333 23.05984 1.000 65.91926  ? 185 LYS   A CD  1 
ATOM   1306 C CE  . LYS   A 1 178 ? -4.94411  22.72092 21.56917 1.000 61.66886  ? 185 LYS   A CE  1 
ATOM   1307 N NZ  . LYS   A 1 178 ? -5.14724  21.27916 21.25802 1.000 69.63864  ? 185 LYS   A NZ  1 
ATOM   1308 N N   . VAL   A 1 179 ? -1.90839  26.18553 25.47554 1.000 40.94235  ? 186 VAL   A N   1 
ATOM   1309 C CA  . VAL   A 1 179 ? -0.79238  25.87388 26.36232 1.000 38.08795  ? 186 VAL   A CA  1 
ATOM   1310 C C   . VAL   A 1 179 ? -1.14670  24.60896 27.13115 1.000 44.93900  ? 186 VAL   A C   1 
ATOM   1311 O O   . VAL   A 1 179 ? -2.14801  24.57541 27.85885 1.000 35.93315  ? 186 VAL   A O   1 
ATOM   1312 C CB  . VAL   A 1 179 ? -0.48666  27.03345 27.32368 1.000 46.02867  ? 186 VAL   A CB  1 
ATOM   1313 C CG1 . VAL   A 1 179 ? 0.67437   26.66493 28.23606 1.000 34.50423  ? 186 VAL   A CG1 1 
ATOM   1314 C CG2 . VAL   A 1 179 ? -0.19383  28.32341 26.55182 1.000 32.25856  ? 186 VAL   A CG2 1 
ATOM   1315 N N   . ILE   A 1 180 ? -0.33219  23.56860 26.97064 1.000 40.03989  ? 187 ILE   A N   1 
ATOM   1316 C CA  . ILE   A 1 180 ? -0.56869  22.26927 27.59085 1.000 39.22992  ? 187 ILE   A CA  1 
ATOM   1317 C C   . ILE   A 1 180 ? 0.49287   22.06953 28.66254 1.000 43.37474  ? 187 ILE   A C   1 
ATOM   1318 O O   . ILE   A 1 180 ? 1.67965   21.90235 28.35247 1.000 33.88723  ? 187 ILE   A O   1 
ATOM   1319 C CB  . ILE   A 1 180 ? -0.54067  21.13401 26.56020 1.000 40.32457  ? 187 ILE   A CB  1 
ATOM   1320 C CG1 . ILE   A 1 180 ? -1.49805  21.43939 25.40823 1.000 44.39033  ? 187 ILE   A CG1 1 
ATOM   1321 C CG2 . ILE   A 1 180 ? -0.88846  19.80701 27.21236 1.000 35.45849  ? 187 ILE   A CG2 1 
ATOM   1322 C CD1 . ILE   A 1 180 ? -1.38498  20.46187 24.26805 1.000 48.50441  ? 187 ILE   A CD1 1 
ATOM   1323 N N   . LEU   A 1 181 ? 0.06862   22.08617 29.92443 1.000 41.24105  ? 188 LEU   A N   1 
ATOM   1324 C CA  . LEU   A 1 181 ? 0.97175   21.91396 31.05704 1.000 43.70198  ? 188 LEU   A CA  1 
ATOM   1325 C C   . LEU   A 1 181 ? 0.96376   20.45207 31.48471 1.000 45.97139  ? 188 LEU   A C   1 
ATOM   1326 O O   . LEU   A 1 181 ? -0.05540  19.94699 31.96425 1.000 44.97303  ? 188 LEU   A O   1 
ATOM   1327 C CB  . LEU   A 1 181 ? 0.55727   22.80976 32.21995 1.000 37.75363  ? 188 LEU   A CB  1 
ATOM   1328 C CG  . LEU   A 1 181 ? 0.40727   24.29845 31.93617 1.000 51.30215  ? 188 LEU   A CG  1 
ATOM   1329 C CD1 . LEU   A 1 181 ? -0.06075  24.97779 33.18974 1.000 36.92354  ? 188 LEU   A CD1 1 
ATOM   1330 C CD2 . LEU   A 1 181 ? 1.72063   24.88635 31.47220 1.000 35.09313  ? 188 LEU   A CD2 1 
ATOM   1331 N N   . HIS   A 1 182 ? 2.09738   19.77420 31.31853 1.000 43.33477  ? 189 HIS   A N   1 
ATOM   1332 C CA  . HIS   A 1 182 ? 2.26954   18.42440 31.85439 1.000 47.05527  ? 189 HIS   A CA  1 
ATOM   1333 C C   . HIS   A 1 182 ? 2.73066   18.57315 33.29819 1.000 45.06338  ? 189 HIS   A C   1 
ATOM   1334 O O   . HIS   A 1 182 ? 3.91042   18.81304 33.56862 1.000 50.68737  ? 189 HIS   A O   1 
ATOM   1335 C CB  . HIS   A 1 182 ? 3.26017   17.62702 31.01291 1.000 43.47556  ? 189 HIS   A CB  1 
ATOM   1336 C CG  . HIS   A 1 182 ? 2.92029   17.60160 29.55479 1.000 46.36749  ? 189 HIS   A CG  1 
ATOM   1337 N ND1 . HIS   A 1 182 ? 2.24463   16.55493 28.96480 1.000 51.39691  ? 189 HIS   A ND1 1 
ATOM   1338 C CD2 . HIS   A 1 182 ? 3.14966   18.50299 28.57051 1.000 54.81624  ? 189 HIS   A CD2 1 
ATOM   1339 C CE1 . HIS   A 1 182 ? 2.07519   16.81148 27.68024 1.000 42.81927  ? 189 HIS   A CE1 1 
ATOM   1340 N NE2 . HIS   A 1 182 ? 2.61644   17.98647 27.41478 1.000 58.45497  ? 189 HIS   A NE2 1 
ATOM   1341 N N   . LEU   A 1 183 ? 1.79006   18.44027 34.22921 1.000 48.47439  ? 190 LEU   A N   1 
ATOM   1342 C CA  . LEU   A 1 183 ? 2.02450   18.83278 35.61125 1.000 49.50997  ? 190 LEU   A CA  1 
ATOM   1343 C C   . LEU   A 1 183 ? 2.97999   17.87392 36.31291 1.000 58.27196  ? 190 LEU   A C   1 
ATOM   1344 O O   . LEU   A 1 183 ? 3.01510   16.67270 36.02981 1.000 61.75481  ? 190 LEU   A O   1 
ATOM   1345 C CB  . LEU   A 1 183 ? 0.69866   18.89426 36.37006 1.000 45.34030  ? 190 LEU   A CB  1 
ATOM   1346 C CG  . LEU   A 1 183 ? -0.26887  19.98231 35.89291 1.000 50.01481  ? 190 LEU   A CG  1 
ATOM   1347 C CD1 . LEU   A 1 183 ? -1.52059  20.00515 36.75205 1.000 47.26351  ? 190 LEU   A CD1 1 
ATOM   1348 C CD2 . LEU   A 1 183 ? 0.40558   21.34205 35.89536 1.000 43.01063  ? 190 LEU   A CD2 1 
ATOM   1349 N N   . LYS   A 1 184 ? 3.76579   18.42609 37.23760 1.000 54.46316  ? 191 LYS   A N   1 
ATOM   1350 C CA  . LYS   A 1 184 ? 4.61115   17.61141 38.09748 1.000 61.56612  ? 191 LYS   A CA  1 
ATOM   1351 C C   . LYS   A 1 184 ? 3.74561   16.71280 38.97971 1.000 62.79341  ? 191 LYS   A C   1 
ATOM   1352 O O   . LYS   A 1 184 ? 2.56302   16.98017 39.21199 1.000 66.16910  ? 191 LYS   A O   1 
ATOM   1353 C CB  . LYS   A 1 184 ? 5.51102   18.49876 38.96158 1.000 55.33908  ? 191 LYS   A CB  1 
ATOM   1354 C CG  . LYS   A 1 184 ? 6.55407   19.29908 38.18067 1.000 52.41267  ? 191 LYS   A CG  1 
ATOM   1355 C CD  . LYS   A 1 184 ? 7.09024   20.47287 39.00064 1.000 54.39699  ? 191 LYS   A CD  1 
ATOM   1356 C CE  . LYS   A 1 184 ? 8.05169   21.33182 38.18858 1.000 61.00270  ? 191 LYS   A CE  1 
ATOM   1357 N NZ  . LYS   A 1 184 ? 8.71418   22.39198 39.00513 1.000 61.13921  ? 191 LYS   A NZ  1 
ATOM   1358 N N   . GLU   A 1 185 ? 4.35492   15.63309 39.48191 1.000 67.87226  ? 192 GLU   A N   1 
ATOM   1359 C CA  . GLU   A 1 185 ? 3.59212   14.63140 40.22380 1.000 56.44177  ? 192 GLU   A CA  1 
ATOM   1360 C C   . GLU   A 1 185 ? 2.96060   15.20774 41.48780 1.000 67.13275  ? 192 GLU   A C   1 
ATOM   1361 O O   . GLU   A 1 185 ? 1.89510   14.74605 41.91117 1.000 67.68328  ? 192 GLU   A O   1 
ATOM   1362 C CB  . GLU   A 1 185 ? 4.48539   13.43506 40.57017 1.000 69.90384  ? 192 GLU   A CB  1 
ATOM   1363 C CG  . GLU   A 1 185 ? 5.29694   13.59916 41.85160 1.000 88.56309  ? 192 GLU   A CG  1 
ATOM   1364 C CD  . GLU   A 1 185 ? 6.45520   12.61955 41.96078 1.000 117.73158 ? 192 GLU   A CD  1 
ATOM   1365 O OE1 . GLU   A 1 185 ? 7.60432   13.08440 42.12495 1.000 118.18192 ? 192 GLU   A OE1 1 
ATOM   1366 O OE2 . GLU   A 1 185 ? 6.21810   11.39240 41.89937 1.000 117.12130 ? 192 GLU   A OE2 1 
ATOM   1367 N N   . ASP   A 1 186 ? 3.58249   16.21692 42.09354 1.000 65.72139  ? 193 ASP   A N   1 
ATOM   1368 C CA  . ASP   A 1 186 ? 3.10962   16.78294 43.34966 1.000 61.78351  ? 193 ASP   A CA  1 
ATOM   1369 C C   . ASP   A 1 186 ? 2.25396   18.03048 43.15735 1.000 64.78830  ? 193 ASP   A C   1 
ATOM   1370 O O   . ASP   A 1 186 ? 1.94747   18.71293 44.14003 1.000 73.53702  ? 193 ASP   A O   1 
ATOM   1371 C CB  . ASP   A 1 186 ? 4.30060   17.10641 44.25818 1.000 74.71445  ? 193 ASP   A CB  1 
ATOM   1372 C CG  . ASP   A 1 186 ? 5.34503   17.97065 43.56761 1.000 91.27894  ? 193 ASP   A CG  1 
ATOM   1373 O OD1 . ASP   A 1 186 ? 5.89034   17.53310 42.53262 1.000 90.32717  ? 193 ASP   A OD1 1 
ATOM   1374 O OD2 . ASP   A 1 186 ? 5.62231   19.08651 44.05721 1.000 92.78586  ? 193 ASP   A OD2 1 
ATOM   1375 N N   . GLN   A 1 187 ? 1.85834   18.34198 41.92338 1.000 63.37825  ? 194 GLN   A N   1 
ATOM   1376 C CA  . GLN   A 1 187 ? 1.11062   19.55784 41.62282 1.000 67.02013  ? 194 GLN   A CA  1 
ATOM   1377 C C   . GLN   A 1 187 ? -0.23969  19.24854 40.98206 1.000 61.07505  ? 194 GLN   A C   1 
ATOM   1378 O O   . GLN   A 1 187 ? -0.71520  20.00197 40.13032 1.000 61.81479  ? 194 GLN   A O   1 
ATOM   1379 C CB  . GLN   A 1 187 ? 1.92883   20.48036 40.71874 1.000 58.76272  ? 194 GLN   A CB  1 
ATOM   1380 C CG  . GLN   A 1 187 ? 3.29917   20.85382 41.27236 1.000 53.74976  ? 194 GLN   A CG  1 
ATOM   1381 C CD  . GLN   A 1 187 ? 3.21403   21.69225 42.52868 1.000 62.82754  ? 194 GLN   A CD  1 
ATOM   1382 O OE1 . GLN   A 1 187 ? 2.29210   22.49088 42.69120 1.000 68.41954  ? 194 GLN   A OE1 1 
ATOM   1383 N NE2 . GLN   A 1 187 ? 4.17826   21.51625 43.42772 1.000 61.61425  ? 194 GLN   A NE2 1 
ATOM   1384 N N   . THR   A 1 188 ? -0.87295  18.14704 41.38266 1.000 65.54104  ? 195 THR   A N   1 
ATOM   1385 C CA  . THR   A 1 188 ? -2.14421  17.75763 40.78566 1.000 57.54183  ? 195 THR   A CA  1 
ATOM   1386 C C   . THR   A 1 188 ? -3.33328  18.48997 41.39053 1.000 62.52748  ? 195 THR   A C   1 
ATOM   1387 O O   . THR   A 1 188 ? -4.46085  18.29313 40.92497 1.000 60.76390  ? 195 THR   A O   1 
ATOM   1388 C CB  . THR   A 1 188 ? -2.35405  16.24644 40.91149 1.000 56.87565  ? 195 THR   A CB  1 
ATOM   1389 O OG1 . THR   A 1 188 ? -2.59193  15.90508 42.28407 1.000 68.82863  ? 195 THR   A OG1 1 
ATOM   1390 C CG2 . THR   A 1 188 ? -1.12483  15.49742 40.40627 1.000 59.58392  ? 195 THR   A CG2 1 
ATOM   1391 N N   . GLU   A 1 189 ? -3.11538  19.32728 42.40700 1.000 62.43777  ? 196 GLU   A N   1 
ATOM   1392 C CA  . GLU   A 1 189 ? -4.20777  20.12515 42.94859 1.000 63.81982  ? 196 GLU   A CA  1 
ATOM   1393 C C   . GLU   A 1 189 ? -4.77082  21.08715 41.91371 1.000 65.35199  ? 196 GLU   A C   1 
ATOM   1394 O O   . GLU   A 1 189 ? -5.92316  21.51323 42.04098 1.000 74.42614  ? 196 GLU   A O   1 
ATOM   1395 C CB  . GLU   A 1 189 ? -3.73911  20.90187 44.18062 1.000 63.65104  ? 196 GLU   A CB  1 
ATOM   1396 C CG  . GLU   A 1 189 ? -2.87132  22.10920 43.85490 1.000 59.94236  ? 196 GLU   A CG  1 
ATOM   1397 C CD  . GLU   A 1 189 ? -2.12336  22.63881 45.06354 1.000 74.51003  ? 196 GLU   A CD  1 
ATOM   1398 O OE1 . GLU   A 1 189 ? -1.12308  22.00865 45.46826 1.000 76.86211  ? 196 GLU   A OE1 1 
ATOM   1399 O OE2 . GLU   A 1 189 ? -2.53200  23.69000 45.60488 1.000 69.21735  ? 196 GLU   A OE2 1 
ATOM   1400 N N   . TYR   A 1 190 ? -3.99068  21.42715 40.88983 1.000 45.74102  ? 197 TYR   A N   1 
ATOM   1401 C CA  . TYR   A 1 190 ? -4.42247  22.33875 39.84049 1.000 59.69893  ? 197 TYR   A CA  1 
ATOM   1402 C C   . TYR   A 1 190 ? -5.22066  21.64096 38.74730 1.000 61.10465  ? 197 TYR   A C   1 
ATOM   1403 O O   . TYR   A 1 190 ? -5.56517  22.27352 37.74312 1.000 55.64659  ? 197 TYR   A O   1 
ATOM   1404 C CB  . TYR   A 1 190 ? -3.20553  23.05895 39.25636 1.000 56.23754  ? 197 TYR   A CB  1 
ATOM   1405 C CG  . TYR   A 1 190 ? -2.41953  23.78577 40.32249 1.000 61.51426  ? 197 TYR   A CG  1 
ATOM   1406 C CD1 . TYR   A 1 190 ? -2.97481  24.86179 40.99918 1.000 62.00041  ? 197 TYR   A CD1 1 
ATOM   1407 C CD2 . TYR   A 1 190 ? -1.13955  23.37805 40.67715 1.000 57.19725  ? 197 TYR   A CD2 1 
ATOM   1408 C CE1 . TYR   A 1 190 ? -2.27634  25.52383 41.98806 1.000 61.13183  ? 197 TYR   A CE1 1 
ATOM   1409 C CE2 . TYR   A 1 190 ? -0.43085  24.03567 41.66862 1.000 57.75087  ? 197 TYR   A CE2 1 
ATOM   1410 C CZ  . TYR   A 1 190 ? -1.00691  25.10968 42.32030 1.000 53.67777  ? 197 TYR   A CZ  1 
ATOM   1411 O OH  . TYR   A 1 190 ? -0.31889  25.77789 43.30822 1.000 66.25392  ? 197 TYR   A OH  1 
ATOM   1412 N N   . LEU   A 1 191 ? -5.51886  20.35707 38.92052 1.000 58.33346  ? 198 LEU   A N   1 
ATOM   1413 C CA  . LEU   A 1 191 ? -6.51122  19.67238 38.10803 1.000 58.01208  ? 198 LEU   A CA  1 
ATOM   1414 C C   . LEU   A 1 191 ? -7.87185  19.62667 38.78684 1.000 54.88910  ? 198 LEU   A C   1 
ATOM   1415 O O   . LEU   A 1 191 ? -8.82646  19.10563 38.20214 1.000 62.39897  ? 198 LEU   A O   1 
ATOM   1416 C CB  . LEU   A 1 191 ? -6.04592  18.24910 37.78407 1.000 49.58030  ? 198 LEU   A CB  1 
ATOM   1417 C CG  . LEU   A 1 191 ? -4.69840  18.10987 37.07410 1.000 45.55207  ? 198 LEU   A CG  1 
ATOM   1418 C CD1 . LEU   A 1 191 ? -4.21814  16.67408 37.12700 1.000 55.32822  ? 198 LEU   A CD1 1 
ATOM   1419 C CD2 . LEU   A 1 191 ? -4.80104  18.58633 35.64071 1.000 51.40665  ? 198 LEU   A CD2 1 
ATOM   1420 N N   . GLU   A 1 192 ? -7.98012  20.16410 40.00009 1.000 56.25926  ? 199 GLU   A N   1 
ATOM   1421 C CA  . GLU   A 1 192 ? -9.20785  20.10657 40.77954 1.000 63.84783  ? 199 GLU   A CA  1 
ATOM   1422 C C   . GLU   A 1 192 ? -10.07284 21.32695 40.49003 1.000 65.90493  ? 199 GLU   A C   1 
ATOM   1423 O O   . GLU   A 1 192 ? -9.56790  22.44714 40.37304 1.000 61.98316  ? 199 GLU   A O   1 
ATOM   1424 C CB  . GLU   A 1 192 ? -8.88724  20.02268 42.27499 1.000 67.27443  ? 199 GLU   A CB  1 
ATOM   1425 C CG  . GLU   A 1 192 ? -8.80001  18.59543 42.82262 1.000 81.50075  ? 199 GLU   A CG  1 
ATOM   1426 C CD  . GLU   A 1 192 ? -10.15329 17.90756 42.96938 1.000 104.88064 ? 199 GLU   A CD  1 
ATOM   1427 O OE1 . GLU   A 1 192 ? -11.18580 18.48508 42.56399 1.000 100.59517 ? 199 GLU   A OE1 1 
ATOM   1428 O OE2 . GLU   A 1 192 ? -10.18210 16.77033 43.48750 1.000 107.84413 ? 199 GLU   A OE2 1 
ATOM   1429 N N   . GLU   A 1 193 ? -11.38355 21.09707 40.37817 1.000 64.31688  ? 200 GLU   A N   1 
ATOM   1430 C CA  . GLU   A 1 193 ? -12.30458 22.15216 39.96428 1.000 59.01042  ? 200 GLU   A CA  1 
ATOM   1431 C C   . GLU   A 1 193 ? -12.33668 23.29111 40.97796 1.000 63.94700  ? 200 GLU   A C   1 
ATOM   1432 O O   . GLU   A 1 193 ? -12.13534 24.45946 40.62694 1.000 62.90807  ? 200 GLU   A O   1 
ATOM   1433 C CB  . GLU   A 1 193 ? -13.70461 21.56929 39.76495 1.000 67.54744  ? 200 GLU   A CB  1 
ATOM   1434 C CG  . GLU   A 1 193 ? -14.80458 22.61581 39.65446 1.000 80.29330  ? 200 GLU   A CG  1 
ATOM   1435 C CD  . GLU   A 1 193 ? -16.15189 22.01007 39.30618 1.000 94.12519  ? 200 GLU   A CD  1 
ATOM   1436 O OE1 . GLU   A 1 193 ? -16.23470 20.76733 39.19028 1.000 88.64531  ? 200 GLU   A OE1 1 
ATOM   1437 O OE2 . GLU   A 1 193 ? -17.12787 22.77570 39.14820 1.000 102.51968 ? 200 GLU   A OE2 1 
ATOM   1438 N N   . ARG   A 1 194 ? -12.59367 22.96836 42.24955 1.000 60.38812  ? 201 ARG   A N   1 
ATOM   1439 C CA  . ARG   A 1 194 ? -12.71156 24.01549 43.26231 1.000 69.66387  ? 201 ARG   A CA  1 
ATOM   1440 C C   . ARG   A 1 194 ? -11.39047 24.74685 43.47189 1.000 62.78002  ? 201 ARG   A C   1 
ATOM   1441 O O   . ARG   A 1 194 ? -11.38106 25.90629 43.90313 1.000 71.94605  ? 201 ARG   A O   1 
ATOM   1442 C CB  . ARG   A 1 194 ? -13.22042 23.42691 44.58194 1.000 58.05332  ? 201 ARG   A CB  1 
ATOM   1443 C CG  . ARG   A 1 194 ? -12.23230 22.52118 45.30074 1.000 80.79656  ? 201 ARG   A CG  1 
ATOM   1444 C CD  . ARG   A 1 194 ? -12.19718 22.82279 46.79312 1.000 89.43059  ? 201 ARG   A CD  1 
ATOM   1445 N NE  . ARG   A 1 194 ? -11.73026 24.17863 47.05942 1.000 101.73001 ? 201 ARG   A NE  1 
ATOM   1446 C CZ  . ARG   A 1 194 ? -10.48843 24.48691 47.41037 1.000 95.27530  ? 201 ARG   A CZ  1 
ATOM   1447 N NH1 . ARG   A 1 194 ? -9.55733  23.55653 47.54779 1.000 86.41602  ? 201 ARG   A NH1 1 
ATOM   1448 N NH2 . ARG   A 1 194 ? -10.17248 25.76049 47.62874 1.000 90.66384  ? 201 ARG   A NH2 1 
ATOM   1449 N N   . ARG   A 1 195 ? -10.26811 24.09735 43.16141 1.000 68.50612  ? 202 ARG   A N   1 
ATOM   1450 C CA  . ARG   A 1 195 ? -8.98294  24.78153 43.24505 1.000 61.07509  ? 202 ARG   A CA  1 
ATOM   1451 C C   . ARG   A 1 195 ? -8.81208  25.77152 42.10008 1.000 65.54669  ? 202 ARG   A C   1 
ATOM   1452 O O   . ARG   A 1 195 ? -8.36575  26.90348 42.31541 1.000 62.98023  ? 202 ARG   A O   1 
ATOM   1453 C CB  . ARG   A 1 195 ? -7.84391  23.76449 43.24664 1.000 64.56384  ? 202 ARG   A CB  1 
ATOM   1454 C CG  . ARG   A 1 195 ? -6.46757  24.37176 43.44779 1.000 59.27248  ? 202 ARG   A CG  1 
ATOM   1455 C CD  . ARG   A 1 195 ? -6.32796  24.96184 44.83735 1.000 63.63687  ? 202 ARG   A CD  1 
ATOM   1456 N NE  . ARG   A 1 195 ? -4.97593  25.44806 45.07832 1.000 62.94117  ? 202 ARG   A NE  1 
ATOM   1457 C CZ  . ARG   A 1 195 ? -4.65561  26.72847 45.20693 1.000 66.95195  ? 202 ARG   A CZ  1 
ATOM   1458 N NH1 . ARG   A 1 195 ? -5.57218  27.68067 45.14143 1.000 73.85955  ? 202 ARG   A NH1 1 
ATOM   1459 N NH2 . ARG   A 1 195 ? -3.38282  27.06299 45.39809 1.000 62.29266  ? 202 ARG   A NH2 1 
ATOM   1460 N N   . ILE   A 1 196 ? -9.16698  25.36520 40.87674 1.000 66.34028  ? 203 ILE   A N   1 
ATOM   1461 C CA  . ILE   A 1 196 ? -9.03584  26.25781 39.72683 1.000 59.87722  ? 203 ILE   A CA  1 
ATOM   1462 C C   . ILE   A 1 196 ? -9.96611  27.45373 39.87466 1.000 64.89405  ? 203 ILE   A C   1 
ATOM   1463 O O   . ILE   A 1 196 ? -9.58244  28.59735 39.59513 1.000 59.76552  ? 203 ILE   A O   1 
ATOM   1464 C CB  . ILE   A 1 196 ? -9.30585  25.49654 38.41576 1.000 55.91346  ? 203 ILE   A CB  1 
ATOM   1465 C CG1 . ILE   A 1 196 ? -8.23697  24.43278 38.17467 1.000 53.32881  ? 203 ILE   A CG1 1 
ATOM   1466 C CG2 . ILE   A 1 196 ? -9.33865  26.45743 37.24654 1.000 49.42584  ? 203 ILE   A CG2 1 
ATOM   1467 C CD1 . ILE   A 1 196 ? -8.67073  23.35210 37.20870 1.000 51.46882  ? 203 ILE   A CD1 1 
ATOM   1468 N N   . LYS   A 1 197 ? -11.20291 27.20995 40.31807 1.000 66.14966  ? 204 LYS   A N   1 
ATOM   1469 C CA  . LYS   A 1 197 ? -12.14666 28.30413 40.52360 1.000 59.49869  ? 204 LYS   A CA  1 
ATOM   1470 C C   . LYS   A 1 197 ? -11.61220 29.31009 41.53403 1.000 59.94231  ? 204 LYS   A C   1 
ATOM   1471 O O   . LYS   A 1 197 ? -11.79176 30.52224 41.36828 1.000 70.87960  ? 204 LYS   A O   1 
ATOM   1472 C CB  . LYS   A 1 197 ? -13.49622 27.75310 40.98157 1.000 57.63497  ? 204 LYS   A CB  1 
ATOM   1473 C CG  . LYS   A 1 197 ? -14.48068 27.48858 39.85492 1.000 66.67210  ? 204 LYS   A CG  1 
ATOM   1474 C CD  . LYS   A 1 197 ? -15.30829 26.24862 40.14300 1.000 71.76111  ? 204 LYS   A CD  1 
ATOM   1475 C CE  . LYS   A 1 197 ? -16.79451 26.56041 40.13404 1.000 80.41181  ? 204 LYS   A CE  1 
ATOM   1476 N NZ  . LYS   A 1 197 ? -17.58647 25.46572 40.76493 1.000 91.51456  ? 204 LYS   A NZ  1 
ATOM   1477 N N   . GLU   A 1 198 ? -10.94359 28.82442 42.58385 1.000 66.87614  ? 205 GLU   A N   1 
ATOM   1478 C CA  . GLU   A 1 198 ? -10.38125 29.71991 43.59060 1.000 72.05475  ? 205 GLU   A CA  1 
ATOM   1479 C C   . GLU   A 1 198 ? -9.29644  30.60808 42.99537 1.000 66.58340  ? 205 GLU   A C   1 
ATOM   1480 O O   . GLU   A 1 198 ? -9.23716  31.80820 43.28589 1.000 76.57915  ? 205 GLU   A O   1 
ATOM   1481 C CB  . GLU   A 1 198 ? -9.81951  28.90864 44.75900 1.000 68.69735  ? 205 GLU   A CB  1 
ATOM   1482 C CG  . GLU   A 1 198 ? -9.00458  29.72986 45.75099 1.000 76.53907  ? 205 GLU   A CG  1 
ATOM   1483 C CD  . GLU   A 1 198 ? -8.40938  28.88614 46.86447 1.000 95.97654  ? 205 GLU   A CD  1 
ATOM   1484 O OE1 . GLU   A 1 198 ? -8.43215  27.64100 46.74535 1.000 90.96304  ? 205 GLU   A OE1 1 
ATOM   1485 O OE2 . GLU   A 1 198 ? -7.93074  29.46816 47.86429 1.000 90.47162  ? 205 GLU   A OE2 1 
ATOM   1486 N N   . ILE   A 1 199 ? -8.42850  30.03423 42.15978 1.000 66.39142  ? 206 ILE   A N   1 
ATOM   1487 C CA  . ILE   A 1 199 ? -7.33857  30.80313 41.56710 1.000 65.72269  ? 206 ILE   A CA  1 
ATOM   1488 C C   . ILE   A 1 199 ? -7.88074  31.82805 40.58076 1.000 66.60927  ? 206 ILE   A C   1 
ATOM   1489 O O   . ILE   A 1 199 ? -7.42787  32.97828 40.54967 1.000 63.15144  ? 206 ILE   A O   1 
ATOM   1490 C CB  . ILE   A 1 199 ? -6.32600  29.85590 40.90042 1.000 59.25931  ? 206 ILE   A CB  1 
ATOM   1491 C CG1 . ILE   A 1 199 ? -5.94009  28.73596 41.86939 1.000 65.68050  ? 206 ILE   A CG1 1 
ATOM   1492 C CG2 . ILE   A 1 199 ? -5.09662  30.62893 40.43899 1.000 58.20657  ? 206 ILE   A CG2 1 
ATOM   1493 C CD1 . ILE   A 1 199 ? -4.72028  27.96072 41.45824 1.000 56.37386  ? 206 ILE   A CD1 1 
ATOM   1494 N N   . VAL   A 1 200 ? -8.85334  31.42839 39.75774 1.000 61.04467  ? 207 VAL   A N   1 
ATOM   1495 C CA  . VAL   A 1 200 ? -9.46425  32.36159 38.81548 1.000 60.55544  ? 207 VAL   A CA  1 
ATOM   1496 C C   . VAL   A 1 200 ? -10.17373 33.48576 39.56234 1.000 67.71809  ? 207 VAL   A C   1 
ATOM   1497 O O   . VAL   A 1 200 ? -10.03198 34.66557 39.21936 1.000 68.89012  ? 207 VAL   A O   1 
ATOM   1498 C CB  . VAL   A 1 200 ? -10.42017 31.61016 37.86916 1.000 55.99435  ? 207 VAL   A CB  1 
ATOM   1499 C CG1 . VAL   A 1 200 ? -11.35711 32.57747 37.16655 1.000 59.45752  ? 207 VAL   A CG1 1 
ATOM   1500 C CG2 . VAL   A 1 200 ? -9.63196  30.80704 36.85208 1.000 53.53121  ? 207 VAL   A CG2 1 
ATOM   1501 N N   . LYS   A 1 201 ? -10.93109 33.14061 40.60725 1.000 72.32262  ? 208 LYS   A N   1 
ATOM   1502 C CA  . LYS   A 1 201 ? -11.67770 34.13509 41.37167 1.000 63.83777  ? 208 LYS   A CA  1 
ATOM   1503 C C   . LYS   A 1 201 ? -10.76527 35.04367 42.19216 1.000 75.15298  ? 208 LYS   A C   1 
ATOM   1504 O O   . LYS   A 1 201 ? -11.20798 36.10446 42.64566 1.000 82.65892  ? 208 LYS   A O   1 
ATOM   1505 C CB  . LYS   A 1 201 ? -12.68221 33.42531 42.28841 1.000 71.73308  ? 208 LYS   A CB  1 
ATOM   1506 C CG  . LYS   A 1 201 ? -13.55600 34.33722 43.13509 1.000 64.31640  ? 208 LYS   A CG  1 
ATOM   1507 C CD  . LYS   A 1 201 ? -13.57623 33.88673 44.58406 1.000 68.52506  ? 208 LYS   A CD  1 
ATOM   1508 C CE  . LYS   A 1 201 ? -13.61215 35.08389 45.52274 1.000 69.51331  ? 208 LYS   A CE  1 
ATOM   1509 N NZ  . LYS   A 1 201 ? -14.97002 35.31803 46.08668 1.000 75.25476  ? 208 LYS   A NZ  1 
ATOM   1510 N N   . LYS   A 1 202 ? -9.50514  34.65907 42.39314 1.000 84.80572  ? 209 LYS   A N   1 
ATOM   1511 C CA  . LYS   A 1 202 ? -8.58339  35.43913 43.21066 1.000 74.13258  ? 209 LYS   A CA  1 
ATOM   1512 C C   . LYS   A 1 202 ? -7.56220  36.21581 42.38929 1.000 74.09207  ? 209 LYS   A C   1 
ATOM   1513 O O   . LYS   A 1 202 ? -7.10734  37.27706 42.82932 1.000 70.25374  ? 209 LYS   A O   1 
ATOM   1514 C CB  . LYS   A 1 202 ? -7.86278  34.51608 44.20646 1.000 80.95731  ? 209 LYS   A CB  1 
ATOM   1515 C CG  . LYS   A 1 202 ? -6.51254  35.01194 44.70749 1.000 73.73284  ? 209 LYS   A CG  1 
ATOM   1516 C CD  . LYS   A 1 202 ? -6.03223  34.22032 45.91472 1.000 74.75802  ? 209 LYS   A CD  1 
ATOM   1517 C CE  . LYS   A 1 202 ? -4.95606  34.97863 46.68013 1.000 87.19882  ? 209 LYS   A CE  1 
ATOM   1518 N NZ  . LYS   A 1 202 ? -4.41977  34.19427 47.83016 1.000 92.12469  ? 209 LYS   A NZ  1 
ATOM   1519 N N   . HIS   A 1 203 ? -7.22366  35.74318 41.18844 1.000 81.82436  ? 210 HIS   A N   1 
ATOM   1520 C CA  . HIS   A 1 203 ? -6.17018  36.35323 40.39084 1.000 79.16189  ? 210 HIS   A CA  1 
ATOM   1521 C C   . HIS   A 1 203 ? -6.62519  36.89579 39.04238 1.000 79.09978  ? 210 HIS   A C   1 
ATOM   1522 O O   . HIS   A 1 203 ? -5.91870  37.73434 38.47010 1.000 80.67489  ? 210 HIS   A O   1 
ATOM   1523 C CB  . HIS   A 1 203 ? -5.03733  35.34428 40.14572 1.000 71.36264  ? 210 HIS   A CB  1 
ATOM   1524 C CG  . HIS   A 1 203 ? -4.20511  35.05955 41.35678 1.000 79.35391  ? 210 HIS   A CG  1 
ATOM   1525 N ND1 . HIS   A 1 203 ? -3.46046  36.02885 41.99368 1.000 78.57229  ? 210 HIS   A ND1 1 
ATOM   1526 C CD2 . HIS   A 1 203 ? -3.99146  33.91062 42.04150 1.000 79.47360  ? 210 HIS   A CD2 1 
ATOM   1527 C CE1 . HIS   A 1 203 ? -2.82812  35.49071 43.02144 1.000 84.94288  ? 210 HIS   A CE1 1 
ATOM   1528 N NE2 . HIS   A 1 203 ? -3.13305  34.20639 43.07265 1.000 79.75574  ? 210 HIS   A NE2 1 
ATOM   1529 N N   . SER   A 1 204 ? -7.76383  36.45019 38.51516 1.000 69.95640  ? 211 SER   A N   1 
ATOM   1530 C CA  . SER   A 1 204 ? -8.18921  36.85047 37.17767 1.000 82.36217  ? 211 SER   A CA  1 
ATOM   1531 C C   . SER   A 1 204 ? -9.66954  37.21310 37.16857 1.000 75.14709  ? 211 SER   A C   1 
ATOM   1532 O O   . SER   A 1 204 ? -10.41887 36.82182 36.26805 1.000 75.09919  ? 211 SER   A O   1 
ATOM   1533 C CB  . SER   A 1 204 ? -7.89027  35.75181 36.15618 1.000 81.49982  ? 211 SER   A CB  1 
ATOM   1534 O OG  . SER   A 1 204 ? -6.50916  35.42348 36.15555 1.000 88.65812  ? 211 SER   A OG  1 
ATOM   1535 N N   . GLN   A 1 205 ? -10.10815 37.98592 38.16487 1.000 93.30122  ? 212 GLN   A N   1 
ATOM   1536 C CA  . GLN   A 1 205 ? -11.50807 38.38749 38.23744 1.000 96.68397  ? 212 GLN   A CA  1 
ATOM   1537 C C   . GLN   A 1 205 ? -11.85265 39.45258 37.20498 1.000 91.14943  ? 212 GLN   A C   1 
ATOM   1538 O O   . GLN   A 1 205 ? -13.02756 39.60106 36.85491 1.000 96.27266  ? 212 GLN   A O   1 
ATOM   1539 C CB  . GLN   A 1 205 ? -11.86229 38.92555 39.63222 1.000 78.14211  ? 212 GLN   A CB  1 
ATOM   1540 C CG  . GLN   A 1 205 ? -10.78465 39.77070 40.34124 1.000 101.29070 ? 212 GLN   A CG  1 
ATOM   1541 C CD  . GLN   A 1 205 ? -9.56811  38.98429 40.79345 1.000 102.09666 ? 212 GLN   A CD  1 
ATOM   1542 O OE1 . GLN   A 1 205 ? -9.68101  38.05985 41.59222 1.000 103.41048 ? 212 GLN   A OE1 1 
ATOM   1543 N NE2 . GLN   A 1 205 ? -8.39235  39.35896 40.28679 1.000 91.56372  ? 212 GLN   A NE2 1 
ATOM   1544 N N   . PHE   A 1 206 ? -10.85965 40.19544 36.71413 1.000 95.30209  ? 213 PHE   A N   1 
ATOM   1545 C CA  . PHE   A 1 206 ? -11.11163 41.34811 35.85700 1.000 85.98114  ? 213 PHE   A CA  1 
ATOM   1546 C C   . PHE   A 1 206 ? -10.51783 41.14179 34.47052 1.000 76.88966  ? 213 PHE   A C   1 
ATOM   1547 O O   . PHE   A 1 206 ? -9.75668  41.98077 33.97976 1.000 79.39987  ? 213 PHE   A O   1 
ATOM   1548 C CB  . PHE   A 1 206 ? -10.54397 42.61323 36.49945 1.000 91.27649  ? 213 PHE   A CB  1 
ATOM   1549 C CG  . PHE   A 1 206 ? -11.04051 42.85125 37.89739 1.000 96.28415  ? 213 PHE   A CG  1 
ATOM   1550 C CD1 . PHE   A 1 206 ? -12.39005 42.74479 38.19350 1.000 92.88516  ? 213 PHE   A CD1 1 
ATOM   1551 C CD2 . PHE   A 1 206 ? -10.15996 43.18171 38.91538 1.000 101.43837 ? 213 PHE   A CD2 1 
ATOM   1552 C CE1 . PHE   A 1 206 ? -12.85233 42.96430 39.47663 1.000 101.56721 ? 213 PHE   A CE1 1 
ATOM   1553 C CE2 . PHE   A 1 206 ? -10.61693 43.40267 40.20252 1.000 101.09969 ? 213 PHE   A CE2 1 
ATOM   1554 C CZ  . PHE   A 1 206 ? -11.96565 43.29341 40.48201 1.000 95.57900  ? 213 PHE   A CZ  1 
ATOM   1555 N N   . ILE   A 1 207 ? -10.85286 40.02058 33.84170 1.000 77.11202  ? 214 ILE   A N   1 
ATOM   1556 C CA  . ILE   A 1 207 ? -10.43335 39.71311 32.48051 1.000 66.29404  ? 214 ILE   A CA  1 
ATOM   1557 C C   . ILE   A 1 207 ? -11.60039 40.00873 31.54891 1.000 59.70750  ? 214 ILE   A C   1 
ATOM   1558 O O   . ILE   A 1 207 ? -12.73862 39.60538 31.81925 1.000 63.28779  ? 214 ILE   A O   1 
ATOM   1559 C CB  . ILE   A 1 207 ? -9.97503  38.24913 32.36083 1.000 61.45376  ? 214 ILE   A CB  1 
ATOM   1560 C CG1 . ILE   A 1 207 ? -8.67537  38.04096 33.14238 1.000 65.23256  ? 214 ILE   A CG1 1 
ATOM   1561 C CG2 . ILE   A 1 207 ? -9.81284  37.84303 30.90332 1.000 57.75050  ? 214 ILE   A CG2 1 
ATOM   1562 C CD1 . ILE   A 1 207 ? -7.46306  38.66164 32.48875 1.000 58.28425  ? 214 ILE   A CD1 1 
ATOM   1563 N N   . GLY   A 1 208 ? -11.32443 40.71514 30.45653 1.000 59.57850  ? 215 GLY   A N   1 
ATOM   1564 C CA  . GLY   A 1 208 ? -12.37790 41.18016 29.57506 1.000 48.77303  ? 215 GLY   A CA  1 
ATOM   1565 C C   . GLY   A 1 208 ? -12.84015 40.17532 28.53940 1.000 56.14612  ? 215 GLY   A C   1 
ATOM   1566 O O   . GLY   A 1 208 ? -13.26429 40.55724 27.44388 1.000 55.97754  ? 215 GLY   A O   1 
ATOM   1567 N N   . TYR   A 1 209 ? -12.76548 38.88878 28.86777 1.000 46.63544  ? 216 TYR   A N   1 
ATOM   1568 C CA  . TYR   A 1 209 ? -13.19937 37.82489 27.97356 1.000 47.60043  ? 216 TYR   A CA  1 
ATOM   1569 C C   . TYR   A 1 209 ? -13.72183 36.68045 28.82778 1.000 53.31875  ? 216 TYR   A C   1 
ATOM   1570 O O   . TYR   A 1 209 ? -13.30377 36.53938 29.98320 1.000 46.66619  ? 216 TYR   A O   1 
ATOM   1571 C CB  . TYR   A 1 209 ? -12.05365 37.35072 27.06428 1.000 49.27843  ? 216 TYR   A CB  1 
ATOM   1572 C CG  . TYR   A 1 209 ? -11.47917 38.46190 26.21252 1.000 49.21959  ? 216 TYR   A CG  1 
ATOM   1573 C CD1 . TYR   A 1 209 ? -12.11286 38.86307 25.04254 1.000 47.66008  ? 216 TYR   A CD1 1 
ATOM   1574 C CD2 . TYR   A 1 209 ? -10.31623 39.12594 26.58986 1.000 49.39923  ? 216 TYR   A CD2 1 
ATOM   1575 C CE1 . TYR   A 1 209 ? -11.60220 39.88776 24.26534 1.000 42.56325  ? 216 TYR   A CE1 1 
ATOM   1576 C CE2 . TYR   A 1 209 ? -9.79780  40.15625 25.81825 1.000 51.21155  ? 216 TYR   A CE2 1 
ATOM   1577 C CZ  . TYR   A 1 209 ? -10.44820 40.53283 24.65715 1.000 48.02820  ? 216 TYR   A CZ  1 
ATOM   1578 O OH  . TYR   A 1 209 ? -9.94671  41.55316 23.87798 1.000 53.18577  ? 216 TYR   A OH  1 
ATOM   1579 N N   . PRO   A 1 210 ? -14.65052 35.87289 28.30867 1.000 42.90874  ? 217 PRO   A N   1 
ATOM   1580 C CA  . PRO   A 1 210 ? -15.20264 34.77800 29.12156 1.000 41.66326  ? 217 PRO   A CA  1 
ATOM   1581 C C   . PRO   A 1 210 ? -14.16110 33.68984 29.34513 1.000 44.40013  ? 217 PRO   A C   1 
ATOM   1582 O O   . PRO   A 1 210 ? -13.48189 33.25760 28.41068 1.000 48.16112  ? 217 PRO   A O   1 
ATOM   1583 C CB  . PRO   A 1 210 ? -16.38644 34.26916 28.28972 1.000 42.48869  ? 217 PRO   A CB  1 
ATOM   1584 C CG  . PRO   A 1 210 ? -16.13433 34.73657 26.90287 1.000 50.47330  ? 217 PRO   A CG  1 
ATOM   1585 C CD  . PRO   A 1 210 ? -15.26805 35.95504 26.97291 1.000 46.25856  ? 217 PRO   A CD  1 
ATOM   1586 N N   . ILE   A 1 211 ? -14.02476 33.26545 30.59951 1.000 42.20057  ? 218 ILE   A N   1 
ATOM   1587 C CA  . ILE   A 1 211 ? -13.13127 32.17785 30.98410 1.000 48.05748  ? 218 ILE   A CA  1 
ATOM   1588 C C   . ILE   A 1 211 ? -14.00191 30.99421 31.38283 1.000 52.89560  ? 218 ILE   A C   1 
ATOM   1589 O O   . ILE   A 1 211 ? -14.63633 31.00792 32.44500 1.000 55.49525  ? 218 ILE   A O   1 
ATOM   1590 C CB  . ILE   A 1 211 ? -12.18453 32.58506 32.12213 1.000 53.95465  ? 218 ILE   A CB  1 
ATOM   1591 C CG1 . ILE   A 1 211 ? -11.45416 33.88647 31.77302 1.000 50.46862  ? 218 ILE   A CG1 1 
ATOM   1592 C CG2 . ILE   A 1 211 ? -11.19203 31.46813 32.42181 1.000 44.81902  ? 218 ILE   A CG2 1 
ATOM   1593 C CD1 . ILE   A 1 211 ? -10.72513 34.51161 32.94367 1.000 46.77672  ? 218 ILE   A CD1 1 
ATOM   1594 N N   . THR   A 1 212 ? -14.03680 29.96888 30.53551 1.000 43.89131  ? 219 THR   A N   1 
ATOM   1595 C CA  . THR   A 1 212 ? -14.88422 28.80234 30.75010 1.000 45.58169  ? 219 THR   A CA  1 
ATOM   1596 C C   . THR   A 1 212 ? -14.05445 27.65472 31.31183 1.000 45.17517  ? 219 THR   A C   1 
ATOM   1597 O O   . THR   A 1 212 ? -13.05752 27.24590 30.70554 1.000 47.37123  ? 219 THR   A O   1 
ATOM   1598 C CB  . THR   A 1 212 ? -15.56511 28.37390 29.45177 1.000 46.91206  ? 219 THR   A CB  1 
ATOM   1599 O OG1 . THR   A 1 212 ? -16.44032 29.41590 29.01208 1.000 49.48362  ? 219 THR   A OG1 1 
ATOM   1600 C CG2 . THR   A 1 212 ? -16.37877 27.10342 29.67238 1.000 50.12442  ? 219 THR   A CG2 1 
ATOM   1601 N N   . LEU   A 1 213 ? -14.47413 27.13455 32.45972 1.000 45.71238  ? 220 LEU   A N   1 
ATOM   1602 C CA  . LEU   A 1 213 ? -13.83908 25.97501 33.06827 1.000 51.43935  ? 220 LEU   A CA  1 
ATOM   1603 C C   . LEU   A 1 213 ? -14.58013 24.72218 32.61566 1.000 46.69621  ? 220 LEU   A C   1 
ATOM   1604 O O   . LEU   A 1 213 ? -15.77544 24.57172 32.89011 1.000 52.94349  ? 220 LEU   A O   1 
ATOM   1605 C CB  . LEU   A 1 213 ? -13.85125 26.09286 34.59141 1.000 48.39480  ? 220 LEU   A CB  1 
ATOM   1606 C CG  . LEU   A 1 213 ? -13.42136 24.85762 35.38686 1.000 68.22600  ? 220 LEU   A CG  1 
ATOM   1607 C CD1 . LEU   A 1 213 ? -12.10752 24.28932 34.84733 1.000 53.09556  ? 220 LEU   A CD1 1 
ATOM   1608 C CD2 . LEU   A 1 213 ? -13.30781 25.18949 36.86883 1.000 56.44013  ? 220 LEU   A CD2 1 
ATOM   1609 N N   . PHE   A 1 214 ? -13.87419 23.82935 31.92492 1.000 53.63299  ? 221 PHE   A N   1 
ATOM   1610 C CA  . PHE   A 1 214 ? -14.46070 22.58489 31.44128 1.000 49.81730  ? 221 PHE   A CA  1 
ATOM   1611 C C   . PHE   A 1 214 ? -14.42534 21.55250 32.56117 1.000 58.26431  ? 221 PHE   A C   1 
ATOM   1612 O O   . PHE   A 1 214 ? -13.35137 21.22943 33.08124 1.000 60.70158  ? 221 PHE   A O   1 
ATOM   1613 C CB  . PHE   A 1 214 ? -13.71508 22.06893 30.21154 1.000 51.76901  ? 221 PHE   A CB  1 
ATOM   1614 C CG  . PHE   A 1 214 ? -14.13271 22.72513 28.92357 1.000 51.31818  ? 221 PHE   A CG  1 
ATOM   1615 C CD1 . PHE   A 1 214 ? -14.10609 24.10194 28.78625 1.000 55.84693  ? 221 PHE   A CD1 1 
ATOM   1616 C CD2 . PHE   A 1 214 ? -14.54901 21.96092 27.84658 1.000 58.34931  ? 221 PHE   A CD2 1 
ATOM   1617 C CE1 . PHE   A 1 214 ? -14.48880 24.70454 27.59650 1.000 53.26197  ? 221 PHE   A CE1 1 
ATOM   1618 C CE2 . PHE   A 1 214 ? -14.92861 22.55816 26.65543 1.000 54.57551  ? 221 PHE   A CE2 1 
ATOM   1619 C CZ  . PHE   A 1 214 ? -14.89791 23.92869 26.53164 1.000 49.93770  ? 221 PHE   A CZ  1 
ATOM   1620 N N   . VAL   A 1 215 ? -15.59540 21.04050 32.92999 1.000 49.09938  ? 222 VAL   A N   1 
ATOM   1621 C CA  . VAL   A 1 215 ? -15.71835 20.05452 33.99719 1.000 56.18565  ? 222 VAL   A CA  1 
ATOM   1622 C C   . VAL   A 1 215 ? -15.50565 18.66368 33.41181 1.000 60.27651  ? 222 VAL   A C   1 
ATOM   1623 O O   . VAL   A 1 215 ? -16.07328 18.32375 32.36675 1.000 59.57915  ? 222 VAL   A O   1 
ATOM   1624 C CB  . VAL   A 1 215 ? -17.09074 20.16070 34.68417 1.000 53.23755  ? 222 VAL   A CB  1 
ATOM   1625 C CG1 . VAL   A 1 215 ? -17.25361 19.06267 35.73731 1.000 59.00596  ? 222 VAL   A CG1 1 
ATOM   1626 C CG2 . VAL   A 1 215 ? -17.28051 21.54719 35.29155 1.000 60.14456  ? 222 VAL   A CG2 1 
ATOM   1627 N N   . GLU   A 1 216 ? -14.68952 17.85615 34.08089 1.000 55.74721  ? 223 GLU   A N   1 
ATOM   1628 C CA  . GLU   A 1 216 ? -14.44262 16.49766 33.62117 1.000 63.97325  ? 223 GLU   A CA  1 
ATOM   1629 C C   . GLU   A 1 216 ? -15.62440 15.59330 33.94736 1.000 67.17464  ? 223 GLU   A C   1 
ATOM   1630 O O   . GLU   A 1 216 ? -16.24609 15.71092 35.00682 1.000 66.10269  ? 223 GLU   A O   1 
ATOM   1631 C CB  . GLU   A 1 216 ? -13.16843 15.94229 34.25303 1.000 67.36543  ? 223 GLU   A CB  1 
ATOM   1632 C CG  . GLU   A 1 216 ? -11.91814 16.20331 33.43467 1.000 67.57661  ? 223 GLU   A CG  1 
ATOM   1633 C CD  . GLU   A 1 216 ? -10.67181 15.66272 34.10015 1.000 70.41863  ? 223 GLU   A CD  1 
ATOM   1634 O OE1 . GLU   A 1 216 ? -10.24597 16.23648 35.12600 1.000 67.71136  ? 223 GLU   A OE1 1 
ATOM   1635 O OE2 . GLU   A 1 216 ? -10.12116 14.65911 33.60237 1.000 84.01700  ? 223 GLU   A OE2 1 
ATOM   1636 N N   . LYS   A 1 217 ? -15.92203 14.67798 33.03261 1.000 63.05859  ? 224 LYS   A N   1 
ATOM   1637 C CA  . LYS   A 1 217 ? -17.07120 13.79533 33.17780 1.000 66.51543  ? 224 LYS   A CA  1 
ATOM   1638 C C   . LYS   A 1 217 ? -16.86654 12.73707 34.26316 1.000 66.70563  ? 224 LYS   A C   1 
ATOM   1639 O O   . LYS   A 1 217 ? -15.74608 12.31148 34.53613 1.000 75.86460  ? 224 LYS   A O   1 
ATOM   1640 C CB  . LYS   A 1 217 ? -17.37835 13.11661 31.84625 1.000 70.19961  ? 224 LYS   A CB  1 
ATOM   1641 C CG  . LYS   A 1 217 ? -18.54611 13.73389 31.10611 1.000 77.19953  ? 224 LYS   A CG  1 
ATOM   1642 C CD  . LYS   A 1 217 ? -18.09551 14.52923 29.89710 1.000 65.05066  ? 224 LYS   A CD  1 
ATOM   1643 C CE  . LYS   A 1 217 ? -17.65961 13.58967 28.78761 1.000 73.11525  ? 224 LYS   A CE  1 
ATOM   1644 N NZ  . LYS   A 1 217 ? -17.45652 14.30421 27.50311 1.000 76.10449  ? 224 LYS   A NZ  1 
HETATM 1645 N N1  . A1AY7 B 2 .   ? 9.42786   34.48403 25.74162 0.957 79.69131  ? 301 A1AY7 A N1  1 
HETATM 1646 C C2  . A1AY7 B 2 .   ? 8.37714   35.08678 26.23010 0.957 69.84701  ? 301 A1AY7 A C2  1 
HETATM 1647 C C4  . A1AY7 B 2 .   ? 6.96850   32.05397 24.73646 0.957 68.28187  ? 301 A1AY7 A C4  1 
HETATM 1648 C C5  . A1AY7 B 2 .   ? 7.72179   31.10510 24.04566 0.957 56.56119  ? 301 A1AY7 A C5  1 
HETATM 1649 C C6  . A1AY7 B 2 .   ? 7.11632   29.98470 23.50732 0.957 56.73848  ? 301 A1AY7 A C6  1 
HETATM 1650 C C3  . A1AY7 B 2 .   ? 7.60991   33.23473 25.30422 0.957 68.32516  ? 301 A1AY7 A C3  1 
HETATM 1651 C C1  . A1AY7 B 2 .   ? 8.52724   36.39702 26.93580 0.957 70.58777  ? 301 A1AY7 A C1  1 
HETATM 1652 C C8  . A1AY7 B 2 .   ? 5.00352   30.71926 24.32615 0.957 65.74949  ? 301 A1AY7 A C8  1 
HETATM 1653 C C11 . A1AY7 B 2 .   ? 5.83342   34.73882 26.39732 0.957 70.30863  ? 301 A1AY7 A C11 1 
HETATM 1654 C C10 . A1AY7 B 2 .   ? 7.22166   34.36077 25.98685 0.957 59.94392  ? 301 A1AY7 A C10 1 
HETATM 1655 C C9  . A1AY7 B 2 .   ? 5.59663   31.84426 24.86850 0.957 61.32856  ? 301 A1AY7 A C9  1 
HETATM 1656 C C7  . A1AY7 B 2 .   ? 5.76117   29.79219 23.64775 0.957 58.04058  ? 301 A1AY7 A C7  1 
HETATM 1657 O O1  . A1AY7 B 2 .   ? 8.95449   33.29696 25.14807 0.957 84.00077  ? 301 A1AY7 A O1  1 
HETATM 1658 O O2  . A1AY7 B 2 .   ? 5.75196   35.32637 27.68699 0.957 78.17280  ? 301 A1AY7 A O2  1 
HETATM 1659 O O   . HOH   C 3 .   ? -12.48017 18.29767 41.10721 1.000 59.04425  ? 401 HOH   A O   1 
HETATM 1660 O O   . HOH   C 3 .   ? -15.44738 10.14760 34.71090 1.000 66.77310  ? 402 HOH   A O   1 
HETATM 1661 O O   . HOH   C 3 .   ? 4.83757   35.96383 29.57864 1.000 59.76464  ? 403 HOH   A O   1 
HETATM 1662 O O   . HOH   C 3 .   ? -15.33642 17.78403 30.34472 1.000 54.80818  ? 404 HOH   A O   1 
HETATM 1663 O O   . HOH   C 3 .   ? -1.87659  33.47523 45.89262 1.000 69.67668  ? 405 HOH   A O   1 
HETATM 1664 O O   . HOH   C 3 .   ? -10.86815 17.68953 36.74491 1.000 59.90101  ? 406 HOH   A O   1 
HETATM 1665 O O   . HOH   C 3 .   ? -0.76985  19.85427 44.77219 1.000 56.34911  ? 407 HOH   A O   1 
HETATM 1666 O O   . HOH   C 3 .   ? -7.71086  42.02070 35.22471 1.000 72.23963  ? 408 HOH   A O   1 
HETATM 1667 O O   . HOH   C 3 .   ? -17.81610 24.86329 34.22043 1.000 54.52138  ? 409 HOH   A O   1 
HETATM 1668 O O   . HOH   C 3 .   ? 15.71207  17.86363 16.48853 1.000 47.62868  ? 410 HOH   A O   1 
HETATM 1669 O O   . HOH   C 3 .   ? -14.90000 18.69907 38.65962 1.000 68.88184  ? 411 HOH   A O   1 
HETATM 1670 O O   . HOH   C 3 .   ? -5.40749  31.53911 11.57671 1.000 52.33833  ? 412 HOH   A O   1 
HETATM 1671 O O   . HOH   C 3 .   ? -5.67709  19.26493 29.24261 1.000 43.20643  ? 413 HOH   A O   1 
HETATM 1672 O O   . HOH   C 3 .   ? 1.07390   23.96246 44.48540 1.000 58.74994  ? 414 HOH   A O   1 
HETATM 1673 O O   . HOH   C 3 .   ? 14.41133  19.80285 23.69895 1.000 47.79980  ? 415 HOH   A O   1 
HETATM 1674 O O   . HOH   C 3 .   ? 17.50539  25.89270 31.79791 1.000 56.21655  ? 416 HOH   A O   1 
HETATM 1675 O O   . HOH   C 3 .   ? -3.74940  35.94951 13.81172 1.000 44.33719  ? 417 HOH   A O   1 
HETATM 1676 O O   . HOH   C 3 .   ? 2.42371   36.97077 32.25856 1.000 57.43455  ? 418 HOH   A O   1 
HETATM 1677 O O   . HOH   C 3 .   ? 8.92469   25.07183 9.19535  1.000 56.75748  ? 419 HOH   A O   1 
HETATM 1678 O O   . HOH   C 3 .   ? -3.26985  29.69064 25.90975 1.000 46.15077  ? 420 HOH   A O   1 
HETATM 1679 O O   . HOH   C 3 .   ? -11.53219 24.82777 23.47367 1.000 49.38672  ? 421 HOH   A O   1 
HETATM 1680 O O   . HOH   C 3 .   ? 10.85176  17.42497 26.13473 1.000 60.36344  ? 422 HOH   A O   1 
HETATM 1681 O O   . HOH   C 3 .   ? 7.68942   20.74817 19.06082 1.000 46.42660  ? 423 HOH   A O   1 
HETATM 1682 O O   . HOH   C 3 .   ? -8.74524  41.73650 29.91899 1.000 53.96322  ? 424 HOH   A O   1 
HETATM 1683 O O   . HOH   C 3 .   ? 7.58675   20.15062 10.90203 1.000 49.55311  ? 425 HOH   A O   1 
HETATM 1684 O O   . HOH   C 3 .   ? 11.09712  29.77702 22.39342 1.000 50.69650  ? 426 HOH   A O   1 
HETATM 1685 O O   . HOH   C 3 .   ? 15.90668  25.55723 29.78128 1.000 52.67536  ? 427 HOH   A O   1 
HETATM 1686 O O   . HOH   C 3 .   ? 3.13318   15.21747 33.67395 1.000 57.34088  ? 428 HOH   A O   1 
HETATM 1687 O O   . HOH   C 3 .   ? -5.22787  42.04055 28.40206 1.000 53.56224  ? 429 HOH   A O   1 
HETATM 1688 O O   . HOH   C 3 .   ? 2.06177   36.97098 17.63276 1.000 56.08310  ? 430 HOH   A O   1 
HETATM 1689 O O   . HOH   C 3 .   ? -3.21160  33.53090 20.86202 1.000 43.08998  ? 431 HOH   A O   1 
HETATM 1690 O O   . HOH   C 3 .   ? -3.26087  12.89756 37.66682 1.000 60.85862  ? 432 HOH   A O   1 
HETATM 1691 O O   . HOH   C 3 .   ? -14.15801 31.19268 39.96957 1.000 65.11865  ? 433 HOH   A O   1 
HETATM 1692 O O   . HOH   C 3 .   ? -1.87732  31.50015 27.60128 1.000 47.42215  ? 434 HOH   A O   1 
HETATM 1693 O O   . HOH   C 3 .   ? -1.54283  33.25323 24.67189 1.000 48.99926  ? 435 HOH   A O   1 
HETATM 1694 O O   . HOH   C 3 .   ? -12.55104 31.75319 17.46791 1.000 56.01627  ? 436 HOH   A O   1 
HETATM 1695 O O   . HOH   C 3 .   ? -3.45434  44.40940 25.91833 1.000 57.33529  ? 437 HOH   A O   1 
HETATM 1696 O O   . HOH   C 3 .   ? -3.70872  38.63466 12.29732 1.000 42.16773  ? 438 HOH   A O   1 
HETATM 1697 O O   . HOH   C 3 .   ? 4.21727   38.39688 31.32039 1.000 52.57586  ? 439 HOH   A O   1 
HETATM 1698 O O   . HOH   C 3 .   ? 7.37246   33.11313 10.75804 1.000 53.34644  ? 440 HOH   A O   1 
HETATM 1699 O O   . HOH   C 3 .   ? -5.60680  45.39518 10.96625 1.000 51.63091  ? 441 HOH   A O   1 
HETATM 1700 O O   . HOH   C 3 .   ? -14.45751 36.57903 32.76898 1.000 60.91199  ? 442 HOH   A O   1 
HETATM 1701 O O   . HOH   C 3 .   ? -12.14166 18.99439 31.20094 1.000 64.06518  ? 443 HOH   A O   1 
HETATM 1702 O O   . HOH   C 3 .   ? 18.68486  19.42732 25.99178 1.000 63.16279  ? 444 HOH   A O   1 
HETATM 1703 O O   . HOH   C 3 .   ? -17.05359 28.02338 34.01016 1.000 54.53654  ? 445 HOH   A O   1 
HETATM 1704 O O   . HOH   C 3 .   ? -16.39441 37.49957 23.72639 1.000 59.78711  ? 446 HOH   A O   1 
HETATM 1705 O O   . HOH   C 3 .   ? -15.92336 34.48886 32.79983 1.000 59.94528  ? 447 HOH   A O   1 
HETATM 1706 O O   . HOH   C 3 .   ? -16.93602 35.88663 22.00751 1.000 62.94194  ? 448 HOH   A O   1 
HETATM 1707 O O   . HOH   C 3 .   ? -18.05413 24.75548 36.80360 1.000 63.62917  ? 449 HOH   A O   1 
HETATM 1708 O O   . HOH   C 3 .   ? -12.95056 18.81598 36.74351 1.000 54.18115  ? 450 HOH   A O   1 
HETATM 1709 O O   . HOH   C 3 .   ? -16.282   27.791   24.789   1.000 49.08708  ? 451 HOH   A O   1 
HETATM 1710 O O   . HOH   C 3 .   ? 16.47436  23.66682 33.77933 1.000 51.38686  ? 452 HOH   A O   1 
HETATM 1711 O O   . HOH   C 3 .   ? 9.55606   32.22746 9.55975  1.000 54.04005  ? 453 HOH   A O   1 
HETATM 1712 O O   . HOH   C 3 .   ? -16.73948 27.96506 36.33714 1.000 61.21799  ? 454 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   ? 0.83465 1.10851 1.03657 0.03682  -0.06984 -0.32539 16  GLU A N   
2    C CA  . GLU A 9   ? 0.91218 1.15544 1.09466 0.05788  -0.06761 -0.27882 16  GLU A CA  
3    C C   . GLU A 9   ? 0.94640 1.17346 1.12973 0.05812  -0.07362 -0.23880 16  GLU A C   
4    O O   . GLU A 9   ? 0.89290 1.15433 1.06838 0.06423  -0.08766 -0.23602 16  GLU A O   
5    C CB  . GLU A 9   ? 1.00476 1.28780 1.15439 0.08717  -0.07673 -0.27550 16  GLU A CB  
6    C CG  . GLU A 9   ? 1.06268 1.31542 1.19787 0.10414  -0.06723 -0.23909 16  GLU A CG  
7    C CD  . GLU A 9   ? 1.26962 1.49691 1.41075 0.10292  -0.05048 -0.25605 16  GLU A CD  
8    O OE1 . GLU A 9   ? 1.18978 1.38792 1.35365 0.08237  -0.03969 -0.28017 16  GLU A OE1 
9    O OE2 . GLU A 9   ? 1.32531 1.55879 1.44714 0.12337  -0.04541 -0.24461 16  GLU A OE2 
10   N N   . VAL A 10  ? 0.86653 1.04336 1.05777 0.05387  -0.06297 -0.20885 17  VAL A N   
11   C CA  . VAL A 10  ? 0.64439 0.80246 0.83809 0.05053  -0.06723 -0.17530 17  VAL A CA  
12   C C   . VAL A 10  ? 0.62912 0.77425 0.80944 0.06650  -0.06746 -0.13790 17  VAL A C   
13   O O   . VAL A 10  ? 0.72378 0.85286 0.90577 0.07321  -0.05738 -0.13204 17  VAL A O   
14   C CB  . VAL A 10  ? 0.61062 0.72628 0.82630 0.02995  -0.05458 -0.17396 17  VAL A CB  
15   C CG1 . VAL A 10  ? 0.53831 0.64205 0.75296 0.02741  -0.06082 -0.14332 17  VAL A CG1 
16   C CG2 . VAL A 10  ? 0.62275 0.74814 0.85659 0.00867  -0.04829 -0.21496 17  VAL A CG2 
17   N N   . GLU A 11  ? 0.65759 0.81014 0.82628 0.07178  -0.07726 -0.11429 18  GLU A N   
18   C CA  . GLU A 11  ? 0.59672 0.73804 0.75707 0.08029  -0.07624 -0.08101 18  GLU A CA  
19   C C   . GLU A 11  ? 0.50844 0.62519 0.67982 0.06818  -0.07805 -0.06005 18  GLU A C   
20   O O   . GLU A 11  ? 0.54250 0.65905 0.71364 0.06035  -0.08452 -0.06279 18  GLU A O   
21   C CB  . GLU A 11  ? 0.71521 0.87786 0.84920 0.09580  -0.08213 -0.07045 18  GLU A CB  
22   C CG  . GLU A 11  ? 0.81422 1.00598 0.92976 0.11322  -0.08074 -0.08737 18  GLU A CG  
23   C CD  . GLU A 11  ? 0.91222 1.12094 0.99522 0.13317  -0.08433 -0.07322 18  GLU A CD  
24   O OE1 . GLU A 11  ? 0.83360 1.05527 0.90700 0.13765  -0.09399 -0.07750 18  GLU A OE1 
25   O OE2 . GLU A 11  ? 0.88893 1.09713 0.95491 0.14611  -0.07531 -0.05673 18  GLU A OE2 
26   N N   . THR A 12  ? 0.49885 0.60058 0.67945 0.06848  -0.07270 -0.04034 19  THR A N   
27   C CA  . THR A 12  ? 0.58329 0.66866 0.77237 0.05981  -0.07560 -0.02101 19  THR A CA  
28   C C   . THR A 12  ? 0.52589 0.61966 0.70892 0.06079  -0.07978 0.00044  19  THR A C   
29   O O   . THR A 12  ? 0.51779 0.62282 0.70252 0.06781  -0.07420 0.00828  19  THR A O   
30   C CB  . THR A 12  ? 0.51164 0.57937 0.71625 0.06161  -0.06679 -0.01537 19  THR A CB  
31   O OG1 . THR A 12  ? 0.51634 0.56697 0.72584 0.05815  -0.05751 -0.03709 19  THR A OG1 
32   C CG2 . THR A 12  ? 0.49131 0.54845 0.70025 0.05606  -0.07151 0.00380  19  THR A CG2 
33   N N   . PHE A 13  ? 0.59270 0.68017 0.76933 0.05235  -0.08730 0.00819  20  PHE A N   
34   C CA  . PHE A 13  ? 0.55135 0.64006 0.72282 0.04799  -0.08904 0.02474  20  PHE A CA  
35   C C   . PHE A 13  ? 0.57012 0.65350 0.75168 0.03673  -0.09505 0.03448  20  PHE A C   
36   O O   . PHE A 13  ? 0.56553 0.63895 0.74785 0.03354  -0.09891 0.03046  20  PHE A O   
37   C CB  . PHE A 13  ? 0.55047 0.63323 0.69880 0.05043  -0.09097 0.02403  20  PHE A CB  
38   C CG  . PHE A 13  ? 0.60542 0.70019 0.73815 0.06610  -0.08786 0.01359  20  PHE A CG  
39   C CD1 . PHE A 13  ? 0.48636 0.59173 0.61799 0.07056  -0.09273 -0.00664 20  PHE A CD1 
40   C CD2 . PHE A 13  ? 0.63928 0.73862 0.75803 0.07613  -0.07929 0.02295  20  PHE A CD2 
41   C CE1 . PHE A 13  ? 0.52036 0.64689 0.63731 0.08608  -0.09252 -0.01990 20  PHE A CE1 
42   C CE2 . PHE A 13  ? 0.60997 0.72482 0.70898 0.09450  -0.07738 0.01372  20  PHE A CE2 
43   C CZ  . PHE A 13  ? 0.54861 0.68019 0.64665 0.10018  -0.08575 -0.00897 20  PHE A CZ  
44   N N   . ALA A 14  ? 0.52323 0.61658 0.71243 0.03017  -0.09489 0.04616  21  ALA A N   
45   C CA  . ALA A 14  ? 0.54724 0.64435 0.74373 0.01908  -0.10289 0.05238  21  ALA A CA  
46   C C   . ALA A 14  ? 0.54716 0.62682 0.72624 0.00796  -0.10634 0.05070  21  ALA A C   
47   O O   . ALA A 14  ? 0.53232 0.60058 0.69813 0.00766  -0.09971 0.05134  21  ALA A O   
48   C CB  . ALA A 14  ? 0.49679 0.62240 0.71445 0.01475  -0.10178 0.06068  21  ALA A CB  
49   N N   . PHE A 15  ? 0.71621 0.79082 0.89176 0.00158  -0.11484 0.04943  22  PHE A N   
50   C CA  . PHE A 15  ? 0.58449 0.64128 0.74343 -0.00891 -0.11734 0.04641  22  PHE A CA  
51   C C   . PHE A 15  ? 0.68378 0.74726 0.85021 -0.02504 -0.11527 0.04870  22  PHE A C   
52   O O   . PHE A 15  ? 0.75025 0.84375 0.93873 -0.03034 -0.11802 0.05152  22  PHE A O   
53   C CB  . PHE A 15  ? 0.58845 0.64133 0.74052 -0.01131 -0.12604 0.04346  22  PHE A CB  
54   C CG  . PHE A 15  ? 0.60402 0.64339 0.74549 -0.00220 -0.12427 0.03783  22  PHE A CG  
55   C CD1 . PHE A 15  ? 0.67111 0.69540 0.79631 0.00163  -0.12125 0.03164  22  PHE A CD1 
56   C CD2 . PHE A 15  ? 0.57891 0.62160 0.72714 0.00307  -0.12376 0.03866  22  PHE A CD2 
57   C CE1 . PHE A 15  ? 0.55168 0.57516 0.67268 0.00880  -0.12019 0.02340  22  PHE A CE1 
58   C CE2 . PHE A 15  ? 0.49427 0.52777 0.63784 0.00636  -0.11944 0.03051  22  PHE A CE2 
59   C CZ  . PHE A 15  ? 0.53685 0.56614 0.66936 0.00830  -0.11890 0.02136  22  PHE A CZ  
60   N N   . GLN A 16  ? 0.62839 0.66416 0.77712 -0.03260 -0.10865 0.04665  23  GLN A N   
61   C CA  . GLN A 16  ? 0.81947 0.85344 0.97439 -0.05456 -0.10444 0.04418  23  GLN A CA  
62   C C   . GLN A 16  ? 0.80877 0.86551 0.97354 -0.06689 -0.11898 0.03600  23  GLN A C   
63   O O   . GLN A 16  ? 0.78075 0.83381 0.93341 -0.05890 -0.12859 0.03339  23  GLN A O   
64   C CB  . GLN A 16  ? 0.65654 0.64357 0.78447 -0.05878 -0.09206 0.04310  23  GLN A CB  
65   C CG  . GLN A 16  ? 1.04416 1.00411 1.14407 -0.04154 -0.09494 0.04093  23  GLN A CG  
66   C CD  . GLN A 16  ? 1.07356 1.03977 1.16673 -0.01666 -0.09396 0.04603  23  GLN A CD  
67   O OE1 . GLN A 16  ? 1.27102 1.23088 1.35695 -0.00716 -0.08280 0.05373  23  GLN A OE1 
68   N NE2 . GLN A 16  ? 0.61903 0.59922 0.71404 -0.00700 -0.10441 0.04037  23  GLN A NE2 
69   N N   . ALA A 17  ? 0.78917 0.87443 0.97631 -0.08632 -0.11992 0.03121  24  ALA A N   
70   C CA  . ALA A 17  ? 0.73541 0.85878 0.93427 -0.09419 -0.13650 0.02285  24  ALA A CA  
71   C C   . ALA A 17  ? 0.82893 0.92693 1.00176 -0.09974 -0.14318 0.01209  24  ALA A C   
72   O O   . ALA A 17  ? 0.82595 0.94477 0.99351 -0.09203 -0.15734 0.01054  24  ALA A O   
73   C CB  . ALA A 17  ? 0.66917 0.83325 0.89865 -0.11807 -0.13582 0.01399  24  ALA A CB  
74   N N   . GLU A 18  ? 0.71667 0.76715 0.86962 -0.10999 -0.13116 0.00601  25  GLU A N   
75   C CA  . GLU A 18  ? 0.89771 0.92151 1.02461 -0.11422 -0.13528 -0.00588 25  GLU A CA  
76   C C   . GLU A 18  ? 0.75309 0.76664 0.86057 -0.08938 -0.14074 0.00168  25  GLU A C   
77   O O   . GLU A 18  ? 0.77400 0.79724 0.87006 -0.08700 -0.15141 -0.00399 25  GLU A O   
78   C CB  . GLU A 18  ? 0.91581 0.88363 1.02366 -0.12655 -0.11715 -0.01220 25  GLU A CB  
79   C CG  . GLU A 18  ? 1.03050 0.99932 1.15759 -0.15728 -0.10560 -0.02181 25  GLU A CG  
80   C CD  . GLU A 18  ? 1.04138 1.01277 1.18498 -0.15438 -0.09082 -0.00611 25  GLU A CD  
81   O OE1 . GLU A 18  ? 1.10654 1.07861 1.24436 -0.12749 -0.09120 0.01033  25  GLU A OE1 
82   O OE2 . GLU A 18  ? 1.17884 1.15321 1.34158 -0.18036 -0.07759 -0.01202 25  GLU A OE2 
83   N N   . ILE A 19  ? 0.73202 0.72908 0.83562 -0.07148 -0.13255 0.01308  26  ILE A N   
84   C CA  . ILE A 19  ? 0.67711 0.66964 0.76861 -0.05207 -0.13552 0.01686  26  ILE A CA  
85   C C   . ILE A 19  ? 0.67369 0.70025 0.77881 -0.04541 -0.14540 0.02264  26  ILE A C   
86   O O   . ILE A 19  ? 0.64016 0.66626 0.73377 -0.03806 -0.14908 0.02267  26  ILE A O   
87   C CB  . ILE A 19  ? 0.73355 0.71064 0.82101 -0.03599 -0.12569 0.02328  26  ILE A CB  
88   C CG1 . ILE A 19  ? 0.70015 0.63771 0.76324 -0.03339 -0.11515 0.02049  26  ILE A CG1 
89   C CG2 . ILE A 19  ? 0.60266 0.58996 0.69054 -0.02072 -0.12865 0.02417  26  ILE A CG2 
90   C CD1 . ILE A 19  ? 0.81793 0.74774 0.86955 -0.01045 -0.10920 0.02475  26  ILE A CD1 
91   N N   . ALA A 20  ? 0.73806 0.79293 0.86624 -0.04617 -0.14744 0.02894  27  ALA A N   
92   C CA  . ALA A 20  ? 0.58574 0.66817 0.72375 -0.03482 -0.15429 0.03733  27  ALA A CA  
93   C C   . ALA A 20  ? 0.66860 0.77009 0.79664 -0.03819 -0.16630 0.03382  27  ALA A C   
94   O O   . ALA A 20  ? 0.54596 0.65271 0.66513 -0.02428 -0.16889 0.04216  27  ALA A O   
95   C CB  . ALA A 20  ? 0.60161 0.71327 0.76600 -0.03216 -0.15347 0.04416  27  ALA A CB  
96   N N   . GLN A 21  ? 0.62675 0.73779 0.75427 -0.05676 -0.17211 0.02072  28  GLN A N   
97   C CA  . GLN A 21  ? 0.63291 0.76671 0.74763 -0.06044 -0.18515 0.01264  28  GLN A CA  
98   C C   . GLN A 21  ? 0.64990 0.75083 0.73313 -0.05585 -0.18266 0.00893  28  GLN A C   
99   O O   . GLN A 21  ? 0.78849 0.90325 0.85505 -0.04553 -0.18954 0.01233  28  GLN A O   
100  C CB  . GLN A 21  ? 0.61810 0.77230 0.74365 -0.08626 -0.19076 -0.00656 28  GLN A CB  
101  C CG  . GLN A 21  ? 0.73984 0.94041 0.90082 -0.09348 -0.19386 -0.00584 28  GLN A CG  
102  C CD  . GLN A 21  ? 0.97138 1.18095 1.14690 -0.12651 -0.19206 -0.02792 28  GLN A CD  
103  O OE1 . GLN A 21  ? 0.84202 1.02205 0.99801 -0.14300 -0.19007 -0.04496 28  GLN A OE1 
104  N NE2 . GLN A 21  ? 0.78820 1.03696 0.99885 -0.13735 -0.19023 -0.02896 28  GLN A NE2 
105  N N   . LEU A 22  ? 0.70955 0.76882 0.78251 -0.06070 -0.17172 0.00307  29  LEU A N   
106  C CA  . LEU A 22  ? 0.68435 0.71661 0.73013 -0.05435 -0.16789 -0.00117 29  LEU A CA  
107  C C   . LEU A 22  ? 0.68142 0.71569 0.72439 -0.03593 -0.16405 0.01294  29  LEU A C   
108  O O   . LEU A 22  ? 0.68346 0.71627 0.70633 -0.02973 -0.16421 0.01307  29  LEU A O   
109  C CB  . LEU A 22  ? 0.59022 0.58126 0.62709 -0.05667 -0.15586 -0.00748 29  LEU A CB  
110  C CG  . LEU A 22  ? 0.63342 0.60112 0.64668 -0.04515 -0.14989 -0.01076 29  LEU A CG  
111  C CD1 . LEU A 22  ? 0.66541 0.63602 0.65601 -0.05039 -0.15623 -0.02240 29  LEU A CD1 
112  C CD2 . LEU A 22  ? 0.76890 0.70009 0.77250 -0.04061 -0.13817 -0.01451 29  LEU A CD2 
113  N N   . MET A 23  ? 0.63935 0.67523 0.70173 -0.02829 -0.15823 0.02371  30  MET A N   
114  C CA  . MET A 23  ? 0.65992 0.69195 0.72272 -0.01532 -0.15048 0.03400  30  MET A CA  
115  C C   . MET A 23  ? 0.60846 0.65887 0.66468 -0.00643 -0.15478 0.04606  30  MET A C   
116  O O   . MET A 23  ? 0.79660 0.83792 0.83737 0.00130  -0.14772 0.05249  30  MET A O   
117  C CB  . MET A 23  ? 0.64546 0.67474 0.73012 -0.01098 -0.14307 0.03831  30  MET A CB  
118  C CG  . MET A 23  ? 0.71539 0.72968 0.80107 -0.01293 -0.13797 0.02893  30  MET A CG  
119  S SD  . MET A 23  ? 0.66159 0.67937 0.76834 -0.00629 -0.13076 0.03026  30  MET A SD  
120  C CE  . MET A 23  ? 0.68539 0.70100 0.79800 -0.00134 -0.12146 0.03145  30  MET A CE  
121  N N   . SER A 24  ? 0.64853 0.72739 0.71550 -0.00567 -0.16507 0.05010  31  SER A N   
122  C CA  . SER A 24  ? 0.67082 0.77312 0.72811 0.00913  -0.17066 0.06340  31  SER A CA  
123  C C   . SER A 24  ? 0.74811 0.86011 0.77625 0.00818  -0.17908 0.05708  31  SER A C   
124  O O   . SER A 24  ? 0.69209 0.80938 0.69930 0.02480  -0.17751 0.07084  31  SER A O   
125  C CB  . SER A 24  ? 0.69006 0.83183 0.76892 0.01244  -0.18130 0.06694  31  SER A CB  
126  O OG  . SER A 24  ? 0.82551 1.00454 0.89098 0.02563  -0.19359 0.07349  31  SER A OG  
127  N N   . LEU A 25  ? 0.78059 0.89126 0.80355 -0.00973 -0.18580 0.03669  32  LEU A N   
128  C CA  . LEU A 25  ? 0.72600 0.84203 0.71842 -0.01116 -0.19229 0.02660  32  LEU A CA  
129  C C   . LEU A 25  ? 0.74574 0.82942 0.71611 -0.00270 -0.17766 0.03254  32  LEU A C   
130  O O   . LEU A 25  ? 0.85196 0.94285 0.79463 0.00854  -0.17760 0.03864  32  LEU A O   
131  C CB  . LEU A 25  ? 0.68873 0.80232 0.68125 -0.03409 -0.19915 0.00064  32  LEU A CB  
132  C CG  . LEU A 25  ? 0.95645 1.07574 0.91827 -0.04027 -0.20693 -0.01814 32  LEU A CG  
133  C CD1 . LEU A 25  ? 0.77681 0.91190 0.75004 -0.06547 -0.21705 -0.04392 32  LEU A CD1 
134  C CD2 . LEU A 25  ? 1.00842 1.08366 0.94717 -0.03873 -0.19348 -0.02363 32  LEU A CD2 
135  N N   . ILE A 26  ? 0.77473 0.82767 0.75700 -0.00697 -0.16463 0.03056  33  ILE A N   
136  C CA  . ILE A 26  ? 0.76550 0.79628 0.73365 -0.00161 -0.15007 0.03228  33  ILE A CA  
137  C C   . ILE A 26  ? 0.74956 0.77936 0.71375 0.01190  -0.13835 0.05312  33  ILE A C   
138  O O   . ILE A 26  ? 0.76752 0.78997 0.70969 0.01796  -0.12797 0.05808  33  ILE A O   
139  C CB  . ILE A 26  ? 0.64296 0.65308 0.62871 -0.00684 -0.14091 0.02403  33  ILE A CB  
140  C CG1 . ILE A 26  ? 0.65546 0.65273 0.63043 -0.01485 -0.14532 0.00588  33  ILE A CG1 
141  C CG2 . ILE A 26  ? 0.72547 0.72566 0.71097 -0.00124 -0.12432 0.02763  33  ILE A CG2 
142  C CD1 . ILE A 26  ? 0.63522 0.61596 0.62495 -0.01485 -0.13887 0.00091  33  ILE A CD1 
143  N N   . ILE A 27  ? 0.81216 0.84583 0.79570 0.01751  -0.13699 0.06625  34  ILE A N   
144  C CA  . ILE A 27  ? 0.91849 0.93935 0.89750 0.03067  -0.12086 0.08695  34  ILE A CA  
145  C C   . ILE A 27  ? 0.98246 1.01926 0.93019 0.04810  -0.12583 0.10286  34  ILE A C   
146  O O   . ILE A 27  ? 1.10900 1.12913 1.03421 0.05877  -0.10932 0.11820  34  ILE A O   
147  C CB  . ILE A 27  ? 0.84563 0.86058 0.85292 0.03332  -0.11599 0.09426  34  ILE A CB  
148  C CG1 . ILE A 27  ? 0.67194 0.66747 0.70223 0.02082  -0.10330 0.08197  34  ILE A CG1 
149  C CG2 . ILE A 27  ? 1.07671 1.07987 1.07345 0.05234  -0.10295 0.11889  34  ILE A CG2 
150  C CD1 . ILE A 27  ? 0.74536 0.74633 0.80250 0.01754  -0.10862 0.07620  34  ILE A CD1 
151  N N   . ASN A 28  ? 0.88754 0.96001 0.83272 0.05148  -0.14764 0.09892  35  ASN A N   
152  C CA  . ASN A 28  ? 0.93404 1.03404 0.85198 0.07343  -0.15577 0.11465  35  ASN A CA  
153  C C   . ASN A 28  ? 0.99975 1.11896 0.88261 0.07336  -0.16628 0.10361  35  ASN A C   
154  O O   . ASN A 28  ? 1.18626 1.32463 1.03660 0.09564  -0.16887 0.11904  35  ASN A O   
155  C CB  . ASN A 28  ? 0.89000 1.03208 0.82796 0.07954  -0.17471 0.11493  35  ASN A CB  
156  C CG  . ASN A 28  ? 0.92776 1.05240 0.89801 0.08199  -0.16409 0.12484  35  ASN A CG  
157  O OD1 . ASN A 28  ? 0.97468 1.06038 0.94260 0.09116  -0.14220 0.14128  35  ASN A OD1 
158  N ND2 . ASN A 28  ? 0.97739 1.12967 0.97802 0.07208  -0.17742 0.11309  35  ASN A ND2 
159  N N   . THR A 29  ? 1.05623 1.16984 0.94123 0.05189  -0.17142 0.07777  36  THR A N   
160  C CA  . THR A 29  ? 1.01717 1.14353 0.86662 0.05157  -0.17880 0.06419  36  THR A CA  
161  C C   . THR A 29  ? 0.94452 1.04215 0.76576 0.06245  -0.15646 0.07834  36  THR A C   
162  O O   . THR A 29  ? 0.99176 1.05552 0.82900 0.05459  -0.13721 0.08010  36  THR A O   
163  C CB  . THR A 29  ? 1.07826 1.19825 0.93688 0.02671  -0.18701 0.03222  36  THR A CB  
164  O OG1 . THR A 29  ? 1.11429 1.26866 0.99088 0.01494  -0.20749 0.01668  36  THR A OG1 
165  C CG2 . THR A 29  ? 1.03846 1.15557 0.85858 0.02673  -0.18663 0.01731  36  THR A CG2 
166  N N   . PHE A 30  ? 1.07927 1.19528 0.85879 0.08098  -0.15839 0.08799  37  PHE A N   
167  C CA  . PHE A 30  ? 1.02432 1.11574 0.77224 0.09219  -0.13463 0.10326  37  PHE A CA  
168  C C   . PHE A 30  ? 0.93459 1.01901 0.67041 0.07768  -0.13395 0.07674  37  PHE A C   
169  O O   . PHE A 30  ? 1.31448 1.42162 1.01623 0.08181  -0.14648 0.06260  37  PHE A O   
170  C CB  . PHE A 30  ? 1.17937 1.29290 0.88143 0.12218  -0.13555 0.12678  37  PHE A CB  
171  C CG  . PHE A 30  ? 1.32213 1.44508 1.03225 0.14277  -0.13759 0.15333  37  PHE A CG  
172  C CD1 . PHE A 30  ? 1.42532 1.51013 1.16753 0.13968  -0.11771 0.16962  37  PHE A CD1 
173  C CD2 . PHE A 30  ? 1.45433 1.62741 1.13933 0.16707  -0.15929 0.16028  37  PHE A CD2 
174  C CE1 . PHE A 30  ? 1.49885 1.58742 1.24644 0.16135  -0.11727 0.19374  37  PHE A CE1 
175  C CE2 . PHE A 30  ? 1.44977 1.63378 1.14139 0.19134  -0.16041 0.18602  37  PHE A CE2 
176  C CZ  . PHE A 30  ? 1.51908 1.65671 1.24119 0.18899  -0.13821 0.20355  37  PHE A CZ  
177  N N   . TYR A 31  ? 0.99344 1.04851 0.75687 0.06229  -0.11937 0.06833  38  TYR A N   
178  C CA  . TYR A 31  ? 0.92606 0.97071 0.68189 0.05239  -0.11534 0.04501  38  TYR A CA  
179  C C   . TYR A 31  ? 0.98917 1.01382 0.74383 0.05568  -0.08583 0.05690  38  TYR A C   
180  O O   . TYR A 31  ? 0.93683 0.94678 0.72268 0.05087  -0.07051 0.06875  38  TYR A O   
181  C CB  . TYR A 31  ? 0.96291 0.99735 0.75296 0.03438  -0.12491 0.02292  38  TYR A CB  
182  C CG  . TYR A 31  ? 1.06468 1.08307 0.84706 0.02887  -0.11903 0.00050  38  TYR A CG  
183  C CD1 . TYR A 31  ? 1.10536 1.12728 0.85645 0.02731  -0.12950 -0.02150 38  TYR A CD1 
184  C CD2 . TYR A 31  ? 1.08736 1.08935 0.89403 0.02653  -0.10317 -0.00078 38  TYR A CD2 
185  C CE1 . TYR A 31  ? 1.06123 1.06252 0.80283 0.02574  -0.12169 -0.04155 38  TYR A CE1 
186  C CE2 . TYR A 31  ? 1.05180 1.04165 0.85058 0.02729  -0.09742 -0.01961 38  TYR A CE2 
187  C CZ  . TYR A 31  ? 1.04362 1.02903 0.80880 0.02790  -0.10548 -0.03869 38  TYR A CZ  
188  O OH  . TYR A 31  ? 1.07853 1.04611 0.83347 0.03204  -0.09722 -0.05680 38  TYR A OH  
189  N N   . SER A 32  ? 1.06908 1.09588 0.78879 0.06258  -0.07676 0.05169  39  SER A N   
190  C CA  . SER A 32  ? 0.98912 1.00369 0.70480 0.06621  -0.04573 0.06542  39  SER A CA  
191  C C   . SER A 32  ? 0.94894 0.95669 0.69630 0.05416  -0.03403 0.04737  39  SER A C   
192  O O   . SER A 32  ? 1.07129 1.07306 0.84500 0.04817  -0.01094 0.05622  39  SER A O   
193  C CB  . SER A 32  ? 1.09336 1.11715 0.75466 0.08210  -0.03812 0.07074  39  SER A CB  
194  O OG  . SER A 32  ? 1.11144 1.13584 0.74612 0.09872  -0.03069 0.10174  39  SER A OG  
195  N N   . ASN A 33  ? 0.96816 0.97755 0.71396 0.05109  -0.04844 0.02133  40  ASN A N   
196  C CA  . ASN A 33  ? 0.97703 0.98380 0.74752 0.04712  -0.03834 0.00518  40  ASN A CA  
197  C C   . ASN A 33  ? 0.89439 0.89890 0.71337 0.03707  -0.04129 0.00511  40  ASN A C   
198  O O   . ASN A 33  ? 0.90077 0.89994 0.73357 0.03515  -0.05357 -0.01057 40  ASN A O   
199  C CB  . ASN A 33  ? 0.90168 0.90174 0.65029 0.05087  -0.05055 -0.02050 40  ASN A CB  
200  C CG  . ASN A 33  ? 1.00391 1.00447 0.76518 0.05645  -0.03604 -0.03424 40  ASN A CG  
201  O OD1 . ASN A 33  ? 1.05062 1.06611 0.81894 0.05998  -0.01421 -0.02774 40  ASN A OD1 
202  N ND2 . ASN A 33  ? 1.02075 1.00572 0.78523 0.05831  -0.04618 -0.05290 40  ASN A ND2 
203  N N   . LYS A 34  ? 1.05829 0.87546 0.59019 0.02068  -0.19896 0.04102  41  LYS A N   
204  C CA  . LYS A 34  ? 1.03530 0.88142 0.64204 0.01739  -0.18979 0.04401  41  LYS A CA  
205  C C   . LYS A 34  ? 0.96217 0.80247 0.58498 0.02000  -0.15922 0.03492  41  LYS A C   
206  O O   . LYS A 34  ? 0.86398 0.72331 0.54086 0.01571  -0.15364 0.03283  41  LYS A O   
207  C CB  . LYS A 34  ? 0.97019 0.83722 0.61024 0.02483  -0.18634 0.06719  41  LYS A CB  
208  C CG  . LYS A 34  ? 0.84365 0.72795 0.49243 0.02190  -0.21775 0.07950  41  LYS A CG  
209  C CD  . LYS A 34  ? 0.94103 0.84229 0.62229 0.03172  -0.21086 0.10351  41  LYS A CD  
210  C CE  . LYS A 34  ? 1.00234 0.91919 0.68361 0.03175  -0.24184 0.11969  41  LYS A CE  
211  N NZ  . LYS A 34  ? 1.01972 0.96196 0.74995 0.02122  -0.26373 0.11579  41  LYS A NZ  
212  N N   . GLU A 35  ? 1.00569 0.82036 0.58272 0.02766  -0.13931 0.03047  42  GLU A N   
213  C CA  . GLU A 35  ? 0.80939 0.62320 0.40772 0.03170  -0.10941 0.02726  42  GLU A CA  
214  C C   . GLU A 35  ? 0.93772 0.75203 0.55750 0.02303  -0.11154 0.00870  42  GLU A C   
215  O O   . GLU A 35  ? 0.87301 0.69483 0.52485 0.02440  -0.09172 0.00759  42  GLU A O   
216  C CB  . GLU A 35  ? 1.02671 0.81422 0.57271 0.04425  -0.08526 0.03023  42  GLU A CB  
217  C CG  . GLU A 35  ? 1.13039 0.88341 0.60881 0.04520  -0.09257 0.01351  42  GLU A CG  
218  C CD  . GLU A 35  ? 1.37804 1.10267 0.79935 0.06124  -0.06502 0.01903  42  GLU A CD  
219  O OE1 . GLU A 35  ? 1.40534 1.13590 0.82323 0.07052  -0.05206 0.03943  42  GLU A OE1 
220  O OE2 . GLU A 35  ? 1.41079 1.10561 0.79060 0.06559  -0.05447 0.00402  42  GLU A OE2 
221  N N   . ILE A 36  ? 0.95394 0.76097 0.55896 0.01347  -0.13620 -0.00443 43  ILE A N   
222  C CA  . ILE A 36  ? 0.89394 0.69842 0.51746 0.00528  -0.13773 -0.02080 43  ILE A CA  
223  C C   . ILE A 36  ? 0.89747 0.73265 0.58883 0.00046  -0.13483 -0.01711 43  ILE A C   
224  O O   . ILE A 36  ? 0.86949 0.70468 0.58047 -0.00351 -0.12892 -0.02720 43  ILE A O   
225  C CB  . ILE A 36  ? 0.98889 0.77863 0.58562 -0.00632 -0.16773 -0.03389 43  ILE A CB  
226  C CG1 . ILE A 36  ? 1.04404 0.85769 0.66297 -0.01351 -0.19641 -0.02275 43  ILE A CG1 
227  C CG2 . ILE A 36  ? 1.00111 0.74978 0.51994 -0.00126 -0.16760 -0.04335 43  ILE A CG2 
228  C CD1 . ILE A 36  ? 0.93497 0.77365 0.61158 -0.02571 -0.21159 -0.02466 43  ILE A CD1 
229  N N   . PHE A 37  ? 0.74710 0.60538 0.47141 0.00194  -0.13760 -0.00260 44  PHE A N   
230  C CA  . PHE A 37  ? 0.75135 0.63325 0.53219 -0.00114 -0.13383 -0.00009 44  PHE A CA  
231  C C   . PHE A 37  ? 0.77721 0.65799 0.57333 0.00200  -0.11034 -0.00345 44  PHE A C   
232  O O   . PHE A 37  ? 0.81378 0.70454 0.64141 -0.00231 -0.10853 -0.00915 44  PHE A O   
233  C CB  . PHE A 37  ? 0.75958 0.65863 0.56570 0.00271  -0.13652 0.01608  44  PHE A CB  
234  C CG  . PHE A 37  ? 0.70806 0.60434 0.51626 0.01061  -0.11561 0.02627  44  PHE A CG  
235  C CD1 . PHE A 37  ? 0.67982 0.56374 0.45247 0.01770  -0.11025 0.03598  44  PHE A CD1 
236  C CD2 . PHE A 37  ? 0.71789 0.62258 0.56260 0.01026  -0.10195 0.02675  44  PHE A CD2 
237  C CE1 . PHE A 37  ? 0.77178 0.65413 0.55184 0.02381  -0.09036 0.04762  44  PHE A CE1 
238  C CE2 . PHE A 37  ? 0.67446 0.57619 0.52507 0.01471  -0.08535 0.03650  44  PHE A CE2 
239  C CZ  . PHE A 37  ? 0.75838 0.65013 0.58010 0.02124  -0.07888 0.04779  44  PHE A CZ  
240  N N   . LEU A 38  ? 0.77481 0.64508 0.55070 0.00980  -0.09222 0.00212  45  LEU A N   
241  C CA  . LEU A 38  ? 0.75683 0.63044 0.55368 0.01230  -0.07158 0.00251  45  LEU A CA  
242  C C   . LEU A 38  ? 0.80387 0.66787 0.59378 0.01074  -0.06749 -0.01095 45  LEU A C   
243  O O   . LEU A 38  ? 0.81294 0.68748 0.63427 0.00853  -0.06107 -0.01324 45  LEU A O   
244  C CB  . LEU A 38  ? 0.77025 0.63689 0.55138 0.02117  -0.05227 0.01481  45  LEU A CB  
245  C CG  . LEU A 38  ? 0.61478 0.49076 0.42766 0.02266  -0.03273 0.02045  45  LEU A CG  
246  C CD1 . LEU A 38  ? 0.60182 0.49595 0.46067 0.01496  -0.03993 0.02118  45  LEU A CD1 
247  C CD2 . LEU A 38  ? 0.69872 0.57096 0.50278 0.03073  -0.01389 0.03677  45  LEU A CD2 
248  N N   . ARG A 39  ? 0.83734 0.67864 0.58378 0.01200  -0.07182 -0.01993 46  ARG A N   
249  C CA  . ARG A 39  ? 0.81617 0.64285 0.55391 0.01060  -0.06837 -0.03343 46  ARG A CA  
250  C C   . ARG A 39  ? 0.82269 0.66328 0.59553 0.00010  -0.08321 -0.04009 46  ARG A C   
251  O O   . ARG A 39  ? 0.84955 0.69177 0.64157 -0.00041 -0.07490 -0.04465 46  ARG A O   
252  C CB  . ARG A 39  ? 0.92887 0.72214 0.60743 0.01251  -0.07374 -0.04384 46  ARG A CB  
253  C CG  . ARG A 39  ? 1.04306 0.81685 0.71155 0.00641  -0.08051 -0.06049 46  ARG A CG  
254  C CD  . ARG A 39  ? 1.09301 0.82822 0.69678 0.00617  -0.09057 -0.07283 46  ARG A CD  
255  N NE  . ARG A 39  ? 1.33457 1.07010 0.93875 -0.00910 -0.12317 -0.08017 46  ARG A NE  
256  C CZ  . ARG A 39  ? 1.44327 1.16230 1.00392 -0.01342 -0.14467 -0.08351 46  ARG A CZ  
257  N NH1 . ARG A 39  ? 1.28333 0.97968 0.78810 -0.00245 -0.13586 -0.08156 46  ARG A NH1 
258  N NH2 . ARG A 39  ? 1.31299 1.03928 0.88708 -0.02900 -0.17606 -0.08731 46  ARG A NH2 
259  N N   . GLU A 40  ? 0.72804 0.58015 0.51178 -0.00724 -0.10396 -0.03831 47  GLU A N   
260  C CA  . GLU A 40  ? 0.71379 0.58002 0.53218 -0.01617 -0.11606 -0.04196 47  GLU A CA  
261  C C   . GLU A 40  ? 0.80156 0.68838 0.66166 -0.01427 -0.10440 -0.03640 47  GLU A C   
262  O O   . GLU A 40  ? 0.76379 0.65475 0.64428 -0.01752 -0.10258 -0.04089 47  GLU A O   
263  C CB  . GLU A 40  ? 0.70245 0.58021 0.52861 -0.02262 -0.13892 -0.03720 47  GLU A CB  
264  C CG  . GLU A 40  ? 0.73260 0.59012 0.51744 -0.02794 -0.15790 -0.04375 47  GLU A CG  
265  C CD  . GLU A 40  ? 1.06397 0.89544 0.82666 -0.03358 -0.15923 -0.05960 47  GLU A CD  
266  O OE1 . GLU A 40  ? 0.96269 0.80125 0.75745 -0.03914 -0.15794 -0.06324 47  GLU A OE1 
267  O OE2 . GLU A 40  ? 1.12320 0.92407 0.83359 -0.03167 -0.16060 -0.06820 47  GLU A OE2 
268  N N   . LEU A 41  ? 0.65772 0.55506 0.52857 -0.00935 -0.09710 -0.02655 48  LEU A N   
269  C CA  . LEU A 41  ? 0.66147 0.57343 0.56562 -0.00874 -0.08892 -0.02291 48  LEU A CA  
270  C C   . LEU A 41  ? 0.57746 0.48614 0.48405 -0.00606 -0.07406 -0.02499 48  LEU A C   
271  O O   . LEU A 41  ? 0.68299 0.60005 0.61155 -0.00774 -0.07170 -0.02654 48  LEU A O   
272  C CB  . LEU A 41  ? 0.59018 0.50913 0.50381 -0.00568 -0.08694 -0.01265 48  LEU A CB  
273  C CG  . LEU A 41  ? 0.66043 0.58633 0.58023 -0.00615 -0.10006 -0.00717 48  LEU A CG  
274  C CD1 . LEU A 41  ? 0.57642 0.50459 0.50568 -0.00185 -0.09499 0.00325  48  LEU A CD1 
275  C CD2 . LEU A 41  ? 0.64222 0.57944 0.58751 -0.00964 -0.10688 -0.01016 48  LEU A CD2 
276  N N   . ILE A 42  ? 0.62739 0.52448 0.51169 -0.00071 -0.06317 -0.02331 49  ILE A N   
277  C CA  . ILE A 42  ? 0.67677 0.57278 0.56732 0.00352  -0.04778 -0.02252 49  ILE A CA  
278  C C   . ILE A 42  ? 0.68604 0.57409 0.57467 0.00201  -0.04904 -0.03223 49  ILE A C   
279  O O   . ILE A 42  ? 0.59219 0.48780 0.50157 0.00303  -0.04236 -0.03091 49  ILE A O   
280  C CB  . ILE A 42  ? 0.65766 0.54167 0.52376 0.01203  -0.03244 -0.01675 49  ILE A CB  
281  C CG1 . ILE A 42  ? 0.69670 0.59226 0.57744 0.01320  -0.02695 -0.00325 49  ILE A CG1 
282  C CG2 . ILE A 42  ? 0.71205 0.59093 0.58013 0.01877  -0.01539 -0.01658 49  ILE A CG2 
283  C CD1 . ILE A 42  ? 0.61049 0.49676 0.47133 0.02264  -0.00847 0.00621  49  ILE A CD1 
284  N N   . SER A 43  ? 0.70794 0.57995 0.57233 -0.00116 -0.05906 -0.04125 50  SER A N   
285  C CA  . SER A 43  ? 0.73064 0.59183 0.59488 -0.00437 -0.06139 -0.05036 50  SER A CA  
286  C C   . SER A 43  ? 0.77230 0.65247 0.67206 -0.01035 -0.06859 -0.04877 50  SER A C   
287  O O   . SER A 43  ? 0.69930 0.57906 0.61206 -0.00985 -0.06293 -0.05009 50  SER A O   
288  C CB  . SER A 43  ? 0.72267 0.56061 0.55352 -0.00938 -0.07442 -0.06063 50  SER A CB  
289  O OG  . SER A 43  ? 0.97116 0.80227 0.81191 -0.01677 -0.08218 -0.06816 50  SER A OG  
290  N N   . ASN A 44  ? 0.61318 0.50885 0.52775 -0.01441 -0.07927 -0.04464 51  ASN A N   
291  C CA  . ASN A 44  ? 0.56590 0.47800 0.51057 -0.01720 -0.08194 -0.04177 51  ASN A CA  
292  C C   . ASN A 44  ? 0.60741 0.52847 0.56637 -0.01282 -0.07099 -0.03743 51  ASN A C   
293  O O   . ASN A 44  ? 0.67950 0.60536 0.65260 -0.01308 -0.06867 -0.03714 51  ASN A O   
294  C CB  . ASN A 44  ? 0.71433 0.63915 0.67076 -0.01908 -0.09141 -0.03673 51  ASN A CB  
295  C CG  . ASN A 44  ? 0.78954 0.71393 0.74689 -0.02559 -0.10617 -0.03819 51  ASN A CG  
296  O OD1 . ASN A 44  ? 0.75161 0.66254 0.69695 -0.03052 -0.11122 -0.04497 51  ASN A OD1 
297  N ND2 . ASN A 44  ? 0.80296 0.74132 0.77635 -0.02587 -0.11373 -0.03114 51  ASN A ND2 
298  N N   . SER A 45  ? 0.66325 0.58694 0.61950 -0.00941 -0.06530 -0.03270 52  SER A N   
299  C CA  . SER A 45  ? 0.64529 0.57830 0.61716 -0.00751 -0.05864 -0.02771 52  SER A CA  
300  C C   . SER A 45  ? 0.62202 0.55200 0.59581 -0.00394 -0.05002 -0.02757 52  SER A C   
301  O O   . SER A 45  ? 0.51226 0.45132 0.50173 -0.00363 -0.04919 -0.02437 52  SER A O   
302  C CB  . SER A 45  ? 0.54894 0.48488 0.52164 -0.00622 -0.05457 -0.02098 52  SER A CB  
303  O OG  . SER A 45  ? 0.65892 0.59803 0.63649 -0.00903 -0.06151 -0.01958 52  SER A OG  
304  N N   . SER A 46  ? 0.65869 0.57370 0.61399 -0.00023 -0.04330 -0.03064 53  SER A N   
305  C CA  . SER A 46  ? 0.57541 0.48357 0.53191 0.00541  -0.03234 -0.03006 53  SER A CA  
306  C C   . SER A 46  ? 0.66976 0.57584 0.63456 0.00240  -0.03694 -0.03397 53  SER A C   
307  O O   . SER A 46  ? 0.60526 0.51714 0.58512 0.00609  -0.03111 -0.02876 53  SER A O   
308  C CB  . SER A 46  ? 0.74980 0.63459 0.67678 0.01121  -0.02282 -0.03474 53  SER A CB  
309  O OG  . SER A 46  ? 0.83791 0.71237 0.76559 0.01888  -0.00927 -0.03387 53  SER A OG  
310  N N   . ASP A 47  ? 0.55973 0.45914 0.51780 -0.00424 -0.04748 -0.04087 54  ASP A N   
311  C CA  . ASP A 47  ? 0.60825 0.50783 0.57922 -0.00790 -0.05097 -0.04189 54  ASP A CA  
312  C C   . ASP A 47  ? 0.58374 0.50304 0.57543 -0.00667 -0.05076 -0.03421 54  ASP A C   
313  O O   . ASP A 47  ? 0.65199 0.57291 0.65358 -0.00390 -0.04589 -0.03006 54  ASP A O   
314  C CB  . ASP A 47  ? 0.54110 0.43672 0.50988 -0.01642 -0.06370 -0.04706 54  ASP A CB  
315  C CG  . ASP A 47  ? 0.75779 0.62848 0.70131 -0.01976 -0.06791 -0.05651 54  ASP A CG  
316  O OD1 . ASP A 47  ? 0.90171 0.75408 0.82682 -0.01369 -0.05738 -0.06001 54  ASP A OD1 
317  O OD2 . ASP A 47  ? 0.78943 0.65789 0.73068 -0.02812 -0.08207 -0.06002 54  ASP A OD2 
318  N N   . ALA A 48  ? 0.65867 0.59016 0.65372 -0.00810 -0.05599 -0.03215 55  ALA A N   
319  C CA  . ALA A 48  ? 0.53864 0.48258 0.54449 -0.00716 -0.05718 -0.02731 55  ALA A CA  
320  C C   . ALA A 48  ? 0.44483 0.39498 0.45691 -0.00332 -0.05298 -0.02131 55  ALA A C   
321  O O   . ALA A 48  ? 0.45027 0.40663 0.46767 -0.00193 -0.05405 -0.01708 55  ALA A O   
322  C CB  . ALA A 48  ? 0.42592 0.37486 0.43011 -0.00890 -0.06261 -0.02774 55  ALA A CB  
323  N N   . LEU A 49  ? 0.49555 0.44523 0.50770 -0.00091 -0.04801 -0.01903 56  LEU A N   
324  C CA  . LEU A 49  ? 0.49151 0.45125 0.51737 0.00312  -0.04407 -0.01007 56  LEU A CA  
325  C C   . LEU A 49  ? 0.62269 0.57678 0.65230 0.00876  -0.03638 -0.00727 56  LEU A C   
326  O O   . LEU A 49  ? 0.59191 0.55680 0.63480 0.01205  -0.03644 0.00168  56  LEU A O   
327  C CB  . LEU A 49  ? 0.54178 0.50486 0.57225 0.00537  -0.03777 -0.00521 56  LEU A CB  
328  C CG  . LEU A 49  ? 0.53722 0.50685 0.56975 -0.00063 -0.04523 -0.00468 56  LEU A CG  
329  C CD1 . LEU A 49  ? 0.52153 0.48701 0.54962 0.00185  -0.03639 -0.00210 56  LEU A CD1 
330  C CD2 . LEU A 49  ? 0.51770 0.50321 0.56934 -0.00433 -0.05333 0.00325  56  LEU A CD2 
331  N N   . ASP A 50  ? 0.53418 0.46988 0.55174 0.00948  -0.03112 -0.01443 57  ASP A N   
332  C CA  . ASP A 50  ? 0.55941 0.48402 0.57985 0.01409  -0.02347 -0.01273 57  ASP A CA  
333  C C   . ASP A 50  ? 0.63784 0.56991 0.66753 0.01230  -0.02832 -0.00830 57  ASP A C   
334  O O   . ASP A 50  ? 0.58626 0.52106 0.62625 0.01807  -0.02326 0.00053  57  ASP A O   
335  C CB  . ASP A 50  ? 0.58858 0.48696 0.59073 0.01202  -0.02063 -0.02379 57  ASP A CB  
336  C CG  . ASP A 50  ? 0.67215 0.55532 0.65853 0.01867  -0.00974 -0.02659 57  ASP A CG  
337  O OD1 . ASP A 50  ? 0.79917 0.69397 0.79686 0.02668  -0.00049 -0.01687 57  ASP A OD1 
338  O OD2 . ASP A 50  ? 0.71990 0.57919 0.68208 0.01600  -0.01055 -0.03769 57  ASP A OD2 
339  N N   . LYS A 51  ? 0.58211 0.51766 0.60834 0.00592  -0.03653 -0.01244 58  LYS A N   
340  C CA  . LYS A 51  ? 0.56528 0.50521 0.59723 0.00590  -0.03737 -0.00732 58  LYS A CA  
341  C C   . LYS A 51  ? 0.62089 0.57544 0.65497 0.01009  -0.04021 0.00163  58  LYS A C   
342  O O   . LYS A 51  ? 0.53840 0.49466 0.57656 0.01454  -0.03703 0.01022  58  LYS A O   
343  C CB  . LYS A 51  ? 0.45982 0.40093 0.48988 0.00023  -0.04248 -0.01181 58  LYS A CB  
344  C CG  . LYS A 51  ? 0.77953 0.71176 0.80543 -0.00572 -0.04651 -0.02069 58  LYS A CG  
345  C CD  . LYS A 51  ? 1.03955 0.96796 1.07524 -0.01165 -0.04882 -0.02119 58  LYS A CD  
346  C CE  . LYS A 51  ? 0.90272 0.82561 0.93329 -0.01862 -0.05792 -0.02898 58  LYS A CE  
347  N NZ  . LYS A 51  ? 0.87065 0.80358 0.91728 -0.02371 -0.06366 -0.02562 58  LYS A NZ  
348  N N   . ILE A 52  ? 0.51255 0.47636 0.54307 0.00811  -0.04751 0.00035  59  ILE A N   
349  C CA  . ILE A 52  ? 0.57741 0.55277 0.60740 0.00966  -0.05467 0.00768  59  ILE A CA  
350  C C   . ILE A 52  ? 0.51099 0.49485 0.55639 0.01503  -0.05202 0.01876  59  ILE A C   
351  O O   . ILE A 52  ? 0.53008 0.52144 0.57705 0.01867  -0.05569 0.02847  59  ILE A O   
352  C CB  . ILE A 52  ? 0.54289 0.52242 0.56660 0.00406  -0.06492 0.00297  59  ILE A CB  
353  C CG1 . ILE A 52  ? 0.44952 0.43622 0.46688 0.00339  -0.07637 0.00840  59  ILE A CG1 
354  C CG2 . ILE A 52  ? 0.48431 0.46790 0.51985 0.00194  -0.06375 0.00289  59  ILE A CG2 
355  C CD1 . ILE A 52  ? 0.51648 0.49663 0.51492 0.00742  -0.07552 0.00938  59  ILE A CD1 
356  N N   . ARG A 53  ? 0.46490 0.44711 0.52090 0.01716  -0.04443 0.01891  60  ARG A N   
357  C CA  . ARG A 53  ? 0.54577 0.53611 0.62037 0.02493  -0.03812 0.03146  60  ARG A CA  
358  C C   . ARG A 53  ? 0.63598 0.61754 0.71225 0.03177  -0.03004 0.03720  60  ARG A C   
359  O O   . ARG A 53  ? 0.57421 0.56735 0.66340 0.03796  -0.03091 0.05124  60  ARG A O   
360  C CB  . ARG A 53  ? 0.51345 0.49853 0.59428 0.02852  -0.02648 0.03010  60  ARG A CB  
361  C CG  . ARG A 53  ? 0.64113 0.62749 0.73973 0.04012  -0.01310 0.04234  60  ARG A CG  
362  C CD  . ARG A 53  ? 0.72803 0.71869 0.83833 0.04546  -0.00198 0.04719  60  ARG A CD  
363  N NE  . ARG A 53  ? 0.96862 0.97686 1.10942 0.05589  0.00514  0.06650  60  ARG A NE  
364  C CZ  . ARG A 53  ? 0.91852 0.91676 1.06717 0.06951  0.02622  0.07289  60  ARG A CZ  
365  N NH1 . ARG A 53  ? 0.87988 0.84672 1.00213 0.07360  0.04127  0.05943  60  ARG A NH1 
366  N NH2 . ARG A 53  ? 0.82805 0.84682 1.01047 0.07986  0.03209  0.09364  60  ARG A NH2 
367  N N   . TYR A 54  ? 0.62339 0.58494 0.68872 0.03002  -0.02346 0.02790  61  TYR A N   
368  C CA  . TYR A 54  ? 0.65951 0.60943 0.72850 0.03491  -0.01522 0.03355  61  TYR A CA  
369  C C   . TYR A 54  ? 0.58180 0.54291 0.64899 0.03586  -0.02155 0.04324  61  TYR A C   
370  O O   . TYR A 54  ? 0.55633 0.52023 0.63221 0.04350  -0.01752 0.05682  61  TYR A O   
371  C CB  . TYR A 54  ? 0.60444 0.53106 0.66461 0.02921  -0.01061 0.02129  61  TYR A CB  
372  C CG  . TYR A 54  ? 0.55342 0.46642 0.61985 0.03123  -0.00328 0.02710  61  TYR A CG  
373  C CD1 . TYR A 54  ? 0.58690 0.48292 0.66024 0.03882  0.00868  0.03161  61  TYR A CD1 
374  C CD2 . TYR A 54  ? 0.53042 0.44596 0.59708 0.02645  -0.00617 0.02938  61  TYR A CD2 
375  C CE1 . TYR A 54  ? 0.52124 0.40192 0.60206 0.04009  0.01588  0.03780  61  TYR A CE1 
376  C CE2 . TYR A 54  ? 0.57516 0.47864 0.65116 0.02775  0.00178  0.03708  61  TYR A CE2 
377  C CZ  . TYR A 54  ? 0.48073 0.36611 0.56402 0.03377  0.01193  0.04100  61  TYR A CZ  
378  O OH  . TYR A 54  ? 0.60890 0.47959 0.70314 0.03452  0.02025  0.04952  61  TYR A OH  
379  N N   . GLU A 55  ? 0.62415 0.58973 0.67759 0.02960  -0.03020 0.03718  62  GLU A N   
380  C CA  . GLU A 55  ? 0.56825 0.54048 0.61104 0.03193  -0.03481 0.04524  62  GLU A CA  
381  C C   . GLU A 55  ? 0.67320 0.66145 0.71789 0.03634  -0.04439 0.05716  62  GLU A C   
382  O O   . GLU A 55  ? 0.61794 0.60962 0.65769 0.04228  -0.04521 0.06960  62  GLU A O   
383  C CB  . GLU A 55  ? 0.54449 0.51589 0.56938 0.02634  -0.04069 0.03555  62  GLU A CB  
384  C CG  . GLU A 55  ? 0.63696 0.59772 0.66433 0.02280  -0.03254 0.02909  62  GLU A CG  
385  C CD  . GLU A 55  ? 0.87368 0.83474 0.88571 0.02187  -0.03395 0.02530  62  GLU A CD  
386  O OE1 . GLU A 55  ? 0.91741 0.88161 0.91072 0.02326  -0.04185 0.02422  62  GLU A OE1 
387  O OE2 . GLU A 55  ? 0.80479 0.76184 0.82421 0.01983  -0.02715 0.02393  62  GLU A OE2 
388  N N   . SER A 56  ? 0.52203 0.52130 0.57561 0.03322  -0.05239 0.05537  63  SER A N   
389  C CA  . SER A 56  ? 0.57983 0.59815 0.64178 0.03478  -0.06530 0.06784  63  SER A CA  
390  C C   . SER A 56  ? 0.65567 0.68174 0.74093 0.04513  -0.05775 0.08518  63  SER A C   
391  O O   . SER A 56  ? 0.57939 0.62343 0.67318 0.04792  -0.06945 0.09993  63  SER A O   
392  C CB  . SER A 56  ? 0.51350 0.54266 0.58667 0.02753  -0.07432 0.06338  63  SER A CB  
393  O OG  . SER A 56  ? 0.54366 0.57780 0.64349 0.03249  -0.06263 0.06900  63  SER A OG  
394  N N   . LEU A 57  ? 0.68273 0.69413 0.77800 0.05088  -0.03945 0.08408  64  LEU A N   
395  C CA  . LEU A 57  ? 0.66421 0.67818 0.78138 0.06273  -0.02915 0.10064  64  LEU A CA  
396  C C   . LEU A 57  ? 0.71279 0.72821 0.82387 0.06875  -0.03120 0.11489  64  LEU A C   
397  O O   . LEU A 57  ? 0.68248 0.70943 0.81220 0.07868  -0.03012 0.13398  64  LEU A O   
398  C CB  . LEU A 57  ? 0.60134 0.59057 0.72331 0.06697  -0.00888 0.09302  64  LEU A CB  
399  C CG  . LEU A 57  ? 0.70105 0.68561 0.82538 0.06456  -0.00331 0.08154  64  LEU A CG  
400  C CD1 . LEU A 57  ? 0.69515 0.64983 0.81742 0.07093  0.01642  0.07508  64  LEU A CD1 
401  C CD2 . LEU A 57  ? 0.54027 0.55180 0.68860 0.06842  -0.00787 0.09469  64  LEU A CD2 
402  N N   . THR A 58  ? 0.71586 0.72047 0.80233 0.06431  -0.03268 0.10820  65  THR A N   
403  C CA  . THR A 58  ? 0.74389 0.74925 0.81871 0.07050  -0.03370 0.12261  65  THR A CA  
404  C C   . THR A 58  ? 0.80650 0.82219 0.85272 0.06643  -0.05230 0.12226  65  THR A C   
405  O O   . THR A 58  ? 0.72387 0.74044 0.75311 0.07254  -0.05500 0.13513  65  THR A O   
406  C CB  . THR A 58  ? 0.68998 0.67329 0.75899 0.07075  -0.01755 0.11943  65  THR A CB  
407  O OG1 . THR A 58  ? 0.77835 0.75437 0.83187 0.06089  -0.01892 0.10159  65  THR A OG1 
408  C CG2 . THR A 58  ? 0.58134 0.54762 0.67368 0.07421  -0.00100 0.11934  65  THR A CG2 
409  N N   . ASP A 59  ? 0.81331 0.83342 0.85054 0.05676  -0.06467 0.10795  66  ASP A N   
410  C CA  . ASP A 59  ? 0.82822 0.85099 0.83337 0.05195  -0.08300 0.10422  66  ASP A CA  
411  C C   . ASP A 59  ? 0.78693 0.82076 0.80077 0.04186  -0.09923 0.09565  66  ASP A C   
412  O O   . ASP A 59  ? 0.75456 0.77937 0.76178 0.03427  -0.09794 0.07889  66  ASP A O   
413  C CB  . ASP A 59  ? 0.77568 0.77940 0.74959 0.05060  -0.07487 0.09213  66  ASP A CB  
414  C CG  . ASP A 59  ? 0.89921 0.89796 0.83121 0.04879  -0.09051 0.08826  66  ASP A CG  
415  O OD1 . ASP A 59  ? 0.81115 0.82100 0.73660 0.04722  -0.11079 0.09564  66  ASP A OD1 
416  O OD2 . ASP A 59  ? 1.03233 1.01497 0.93764 0.04915  -0.08276 0.07823  66  ASP A OD2 
417  N N   . PRO A 60  ? 0.72669 0.78156 0.75919 0.04133  -0.11499 0.10889  67  PRO A N   
418  C CA  . PRO A 60  ? 0.69365 0.76123 0.74192 0.03042  -0.13035 0.10374  67  PRO A CA  
419  C C   . PRO A 60  ? 0.75202 0.80742 0.76444 0.01926  -0.14781 0.08820  67  PRO A C   
420  O O   . PRO A 60  ? 0.70696 0.76489 0.73000 0.00894  -0.15566 0.07941  67  PRO A O   
421  C CB  . PRO A 60  ? 0.71409 0.80965 0.79246 0.03295  -0.14509 0.12607  67  PRO A CB  
422  C CG  . PRO A 60  ? 0.63710 0.73292 0.72510 0.04791  -0.12879 0.14183  67  PRO A CG  
423  C CD  . PRO A 60  ? 0.68908 0.75935 0.73632 0.05093  -0.11854 0.13194  67  PRO A CD  
424  N N   . SER A 61  ? 0.68020 0.71965 0.64895 0.02198  -0.15221 0.08499  68  SER A N   
425  C CA  . SER A 61  ? 0.84338 0.86382 0.77103 0.01365  -0.16582 0.06866  68  SER A CA  
426  C C   . SER A 61  ? 0.84118 0.84484 0.76526 0.01037  -0.15091 0.05019  68  SER A C   
427  O O   . SER A 61  ? 0.75979 0.74786 0.65918 0.00266  -0.16107 0.03612  68  SER A O   
428  C CB  . SER A 61  ? 0.80300 0.80607 0.67962 0.02117  -0.16769 0.07011  68  SER A CB  
429  O OG  . SER A 61  ? 0.88969 0.87774 0.75502 0.03078  -0.14097 0.06648  68  SER A OG  
430  N N   . LYS A 62  ? 0.65275 0.65739 0.59977 0.01589  -0.12827 0.05011  69  LYS A N   
431  C CA  . LYS A 62  ? 0.64791 0.64018 0.59512 0.01264  -0.11654 0.03504  69  LYS A CA  
432  C C   . LYS A 62  ? 0.69371 0.69230 0.66065 0.00227  -0.12590 0.02878  69  LYS A C   
433  O O   . LYS A 62  ? 0.63619 0.62348 0.59878 -0.00125 -0.12025 0.01653  69  LYS A O   
434  C CB  . LYS A 62  ? 0.61500 0.60709 0.58269 0.01892  -0.09470 0.03726  69  LYS A CB  
435  C CG  . LYS A 62  ? 0.75784 0.74375 0.71286 0.02826  -0.08314 0.04555  69  LYS A CG  
436  C CD  . LYS A 62  ? 0.69585 0.67020 0.65132 0.02981  -0.06586 0.03873  69  LYS A CD  
437  C CE  . LYS A 62  ? 0.76684 0.73404 0.70567 0.03843  -0.05462 0.04774  69  LYS A CE  
438  N NZ  . LYS A 62  ? 0.81872 0.77726 0.75892 0.03919  -0.03976 0.04267  69  LYS A NZ  
439  N N   . LEU A 63  ? 0.54023 0.55798 0.53165 -0.00220 -0.13939 0.03916  70  LEU A N   
440  C CA  . LEU A 63  ? 0.56318 0.58984 0.57923 -0.01207 -0.14706 0.03731  70  LEU A CA  
441  C C   . LEU A 63  ? 0.66449 0.68793 0.66659 -0.02429 -0.17297 0.03366  70  LEU A C   
442  O O   . LEU A 63  ? 0.66015 0.69116 0.68553 -0.03451 -0.18158 0.03384  70  LEU A O   
443  C CB  . LEU A 63  ? 0.61215 0.66392 0.67296 -0.00866 -0.14182 0.05366  70  LEU A CB  
444  C CG  . LEU A 63  ? 0.63909 0.68711 0.71281 0.00077  -0.11635 0.05303  70  LEU A CG  
445  C CD1 . LEU A 63  ? 0.54812 0.61604 0.66234 0.00495  -0.10893 0.06755  70  LEU A CD1 
446  C CD2 . LEU A 63  ? 0.53706 0.56774 0.59712 -0.00299 -0.10771 0.03678  70  LEU A CD2 
447  N N   . ASP A 64  ? 0.64047 0.65036 0.60314 -0.02373 -0.18551 0.03046  71  ASP A N   
448  C CA  . ASP A 64  ? 0.79818 0.79667 0.73774 -0.03644 -0.21236 0.02347  71  ASP A CA  
449  C C   . ASP A 64  ? 0.74504 0.72118 0.67385 -0.04448 -0.21071 0.00618  71  ASP A C   
450  O O   . ASP A 64  ? 0.83346 0.80399 0.76297 -0.05873 -0.23188 0.00177  71  ASP A O   
451  C CB  . ASP A 64  ? 0.71144 0.69060 0.59712 -0.03153 -0.22180 0.02020  71  ASP A CB  
452  C CG  . ASP A 64  ? 0.96888 0.97029 0.86386 -0.02493 -0.22885 0.03979  71  ASP A CG  
453  O OD1 . ASP A 64  ? 0.92957 0.96196 0.87540 -0.02566 -0.22998 0.05591  71  ASP A OD1 
454  O OD2 . ASP A 64  ? 0.91371 0.90088 0.76457 -0.01754 -0.23161 0.04042  71  ASP A OD2 
455  N N   . SER A 65  ? 0.74622 0.70954 0.66758 -0.03615 -0.18691 -0.00248 72  SER A N   
456  C CA  . SER A 65  ? 0.70560 0.65018 0.62210 -0.04131 -0.18232 -0.01588 72  SER A CA  
457  C C   . SER A 65  ? 0.75068 0.71370 0.71335 -0.04840 -0.17999 -0.00989 72  SER A C   
458  O O   . SER A 65  ? 0.71336 0.66278 0.67614 -0.05276 -0.17617 -0.01834 72  SER A O   
459  C CB  . SER A 65  ? 0.79904 0.72824 0.69668 -0.02917 -0.15859 -0.02363 72  SER A CB  
460  O OG  . SER A 65  ? 0.65876 0.60641 0.57777 -0.01990 -0.14225 -0.01382 72  SER A OG  
461  N N   . GLY A 66  ? 0.65024 0.64266 0.65130 -0.04802 -0.18013 0.00581  73  GLY A N   
462  C CA  . GLY A 66  ? 0.66351 0.67330 0.70668 -0.05181 -0.17347 0.01378  73  GLY A CA  
463  C C   . GLY A 66  ? 0.80648 0.84086 0.88114 -0.04197 -0.15899 0.02870  73  GLY A C   
464  O O   . GLY A 66  ? 0.73093 0.76019 0.79587 -0.03072 -0.14104 0.02623  73  GLY A O   
465  N N   . LYS A 67  ? 0.65659 0.71669 0.77096 -0.04615 -0.16630 0.04495  74  LYS A N   
466  C CA  . LYS A 67  ? 0.66974 0.75183 0.81593 -0.03502 -0.15096 0.06091  74  LYS A CA  
467  C C   . LYS A 67  ? 0.66276 0.74620 0.82792 -0.02996 -0.12839 0.06261  74  LYS A C   
468  O O   . LYS A 67  ? 0.57657 0.66328 0.74969 -0.01733 -0.10880 0.06815  74  LYS A O   
469  C CB  . LYS A 67  ? 0.68509 0.79750 0.86998 -0.03950 -0.16753 0.08134  74  LYS A CB  
470  C CG  . LYS A 67  ? 0.84710 0.96077 1.01286 -0.04491 -0.19412 0.08283  74  LYS A CG  
471  C CD  . LYS A 67  ? 1.08755 1.18128 1.22403 -0.06136 -0.21874 0.06807  74  LYS A CD  
472  C CE  . LYS A 67  ? 1.01301 1.11966 1.18830 -0.07696 -0.23097 0.07447  74  LYS A CE  
473  N NZ  . LYS A 67  ? 0.93439 1.01074 1.07699 -0.09167 -0.24753 0.05557  74  LYS A NZ  
474  N N   . GLU A 68  ? 0.60963 0.68729 0.77873 -0.03902 -0.13028 0.05796  75  GLU A N   
475  C CA  . GLU A 68  ? 0.49948 0.57788 0.68287 -0.03385 -0.10930 0.06140  75  GLU A CA  
476  C C   . GLU A 68  ? 0.52074 0.57593 0.66957 -0.02493 -0.09295 0.04661  75  GLU A C   
477  O O   . GLU A 68  ? 0.64459 0.68115 0.76286 -0.02792 -0.09919 0.03201  75  GLU A O   
478  C CB  . GLU A 68  ? 0.59607 0.67410 0.79381 -0.04636 -0.11628 0.06263  75  GLU A CB  
479  C CG  . GLU A 68  ? 0.55161 0.65114 0.78726 -0.06026 -0.13726 0.07669  75  GLU A CG  
480  C CD  . GLU A 68  ? 0.93426 1.02875 1.15159 -0.06987 -0.16523 0.06971  75  GLU A CD  
481  O OE1 . GLU A 68  ? 0.96279 1.02941 1.13582 -0.07134 -0.17077 0.05069  75  GLU A OE1 
482  O OE2 . GLU A 68  ? 1.12517 1.24358 1.37162 -0.07495 -0.18127 0.08440  75  GLU A OE2 
483  N N   . LEU A 69  ? 0.52899 0.58446 0.68293 -0.01381 -0.07200 0.05103  76  LEU A N   
484  C CA  . LEU A 69  ? 0.52776 0.56165 0.65139 -0.00681 -0.05869 0.03820  76  LEU A CA  
485  C C   . LEU A 69  ? 0.57987 0.60950 0.70491 -0.00393 -0.04416 0.04070  76  LEU A C   
486  O O   . LEU A 69  ? 0.60141 0.63564 0.73827 0.00557  -0.02731 0.05034  76  LEU A O   
487  C CB  . LEU A 69  ? 0.47166 0.50173 0.59041 0.00402  -0.04814 0.03897  76  LEU A CB  
488  C CG  . LEU A 69  ? 0.48829 0.52459 0.60760 0.00335  -0.06005 0.04108  76  LEU A CG  
489  C CD1 . LEU A 69  ? 0.53376 0.56249 0.64914 0.01439  -0.04709 0.04258  76  LEU A CD1 
490  C CD2 . LEU A 69  ? 0.52624 0.55093 0.61984 -0.00433 -0.07375 0.02820  76  LEU A CD2 
491  N N   . HIS A 70  ? 0.49164 0.51095 0.60300 -0.01053 -0.04898 0.03320  77  HIS A N   
492  C CA  . HIS A 70  ? 0.55138 0.56722 0.66304 -0.00820 -0.03648 0.03800  77  HIS A CA  
493  C C   . HIS A 70  ? 0.57425 0.57169 0.65767 -0.01117 -0.04029 0.02579  77  HIS A C   
494  O O   . HIS A 70  ? 0.49567 0.48552 0.56563 -0.01570 -0.05233 0.01510  77  HIS A O   
495  C CB  . HIS A 70  ? 0.48017 0.51434 0.62794 -0.01502 -0.03883 0.05366  77  HIS A CB  
496  C CG  . HIS A 70  ? 0.40966 0.44469 0.56448 -0.02952 -0.06070 0.04989  77  HIS A CG  
497  N ND1 . HIS A 70  ? 0.58473 0.63711 0.76797 -0.03819 -0.07587 0.05826  77  HIS A ND1 
498  C CD2 . HIS A 70  ? 0.51923 0.53709 0.65429 -0.03647 -0.07022 0.03851  77  HIS A CD2 
499  C CE1 . HIS A 70  ? 0.47484 0.51682 0.65049 -0.05069 -0.09445 0.04998  77  HIS A CE1 
500  N NE2 . HIS A 70  ? 0.54744 0.56785 0.69457 -0.04888 -0.08960 0.03810  77  HIS A NE2 
501  N N   . ILE A 71  ? 0.54786 0.53858 0.62255 -0.00710 -0.02856 0.02939  78  ILE A N   
502  C CA  . ILE A 71  ? 0.55277 0.52880 0.60438 -0.00877 -0.03165 0.02221  78  ILE A CA  
503  C C   . ILE A 71  ? 0.53371 0.51329 0.60005 -0.01216 -0.02753 0.03401  78  ILE A C   
504  O O   . ILE A 71  ? 0.56863 0.55555 0.64752 -0.00710 -0.01281 0.04705  78  ILE A O   
505  C CB  . ILE A 71  ? 0.63307 0.59365 0.65230 -0.00030 -0.02320 0.01528  78  ILE A CB  
506  C CG1 . ILE A 71  ? 0.56671 0.52313 0.57735 0.00179  -0.02626 0.00552  78  ILE A CG1 
507  C CG2 . ILE A 71  ? 0.53069 0.47997 0.52947 -0.00233 -0.02990 0.01009  78  ILE A CG2 
508  C CD1 . ILE A 71  ? 0.57085 0.50931 0.55181 0.00877  -0.01839 -0.00130 78  ILE A CD1 
509  N N   . ASN A 72  ? 0.58195 0.55522 0.64830 -0.01984 -0.03857 0.03076  79  ASN A N   
510  C CA  . ASN A 72  ? 0.55454 0.52706 0.63466 -0.02417 -0.03552 0.04179  79  ASN A CA  
511  C C   . ASN A 72  ? 0.54749 0.50441 0.60132 -0.01994 -0.03345 0.03893  79  ASN A C   
512  O O   . ASN A 72  ? 0.63345 0.58112 0.66942 -0.01959 -0.04261 0.02729  79  ASN A O   
513  C CB  . ASN A 72  ? 0.57362 0.54707 0.67651 -0.03735 -0.05065 0.04161  79  ASN A CB  
514  C CG  . ASN A 72  ? 0.59784 0.59028 0.73289 -0.04352 -0.05534 0.04957  79  ASN A CG  
515  O OD1 . ASN A 72  ? 0.49367 0.50154 0.64360 -0.03707 -0.04263 0.06077  79  ASN A OD1 
516  N ND2 . ASN A 72  ? 0.56445 0.55475 0.70950 -0.05548 -0.07384 0.04451  79  ASN A ND2 
517  N N   . LEU A 73  ? 0.57652 0.53202 0.62983 -0.01594 -0.02077 0.05184  80  LEU A N   
518  C CA  . LEU A 73  ? 0.61986 0.56202 0.65022 -0.01170 -0.01923 0.05350  80  LEU A CA  
519  C C   . LEU A 73  ? 0.61665 0.55597 0.66972 -0.01872 -0.01936 0.06504  80  LEU A C   
520  O O   . LEU A 73  ? 0.64566 0.59330 0.72253 -0.02079 -0.00880 0.08029  80  LEU A O   
521  C CB  . LEU A 73  ? 0.54745 0.48518 0.55028 -0.00008 -0.00395 0.05967  80  LEU A CB  
522  C CG  . LEU A 73  ? 0.60151 0.53649 0.58054 0.00660  -0.00166 0.04867  80  LEU A CG  
523  C CD1 . LEU A 73  ? 0.65172 0.57412 0.59434 0.01821  0.01305  0.05347  80  LEU A CD1 
524  C CD2 . LEU A 73  ? 0.56220 0.49217 0.52749 0.00341  -0.01889 0.03215  80  LEU A CD2 
525  N N   . ILE A 74  ? 0.59435 0.52127 0.64269 -0.02202 -0.03001 0.05906  81  ILE A N   
526  C CA  . ILE A 74  ? 0.56712 0.48532 0.63715 -0.03018 -0.03211 0.06713  81  ILE A CA  
527  C C   . ILE A 74  ? 0.64420 0.54825 0.69766 -0.02374 -0.02937 0.07297  81  ILE A C   
528  O O   . ILE A 74  ? 0.64053 0.53383 0.68302 -0.02196 -0.03829 0.06350  81  ILE A O   
529  C CB  . ILE A 74  ? 0.56039 0.47117 0.64243 -0.04082 -0.04764 0.05433  81  ILE A CB  
530  C CG1 . ILE A 74  ? 0.54331 0.46988 0.63836 -0.04599 -0.05282 0.04944  81  ILE A CG1 
531  C CG2 . ILE A 74  ? 0.53440 0.43159 0.63901 -0.05154 -0.05079 0.06158  81  ILE A CG2 
532  C CD1 . ILE A 74  ? 0.62399 0.54160 0.71828 -0.05413 -0.06912 0.03483  81  ILE A CD1 
533  N N   . PRO A 75  ? 0.60061 0.50469 0.65231 -0.01876 -0.01611 0.09025  82  PRO A N   
534  C CA  . PRO A 75  ? 0.58792 0.47861 0.62654 -0.01273 -0.01423 0.09913  82  PRO A CA  
535  C C   . PRO A 75  ? 0.72571 0.60199 0.79129 -0.02163 -0.01611 0.10567  82  PRO A C   
536  O O   . PRO A 75  ? 0.72998 0.60824 0.82594 -0.03304 -0.01515 0.11033  82  PRO A O   
537  C CB  . PRO A 75  ? 0.70528 0.60036 0.72813 -0.00348 0.00241  0.11627  82  PRO A CB  
538  C CG  . PRO A 75  ? 0.59234 0.50068 0.64134 -0.00876 0.01287  0.12283  82  PRO A CG  
539  C CD  . PRO A 75  ? 0.69017 0.60674 0.74893 -0.01575 0.00001  0.10410  82  PRO A CD  
540  N N   . ASN A 76  ? 0.76533 0.62613 0.82109 -0.01649 -0.01947 0.10687  83  ASN A N   
541  C CA  . ASN A 76  ? 0.70116 0.54067 0.77755 -0.02321 -0.02059 0.11171  83  ASN A CA  
542  C C   . ASN A 76  ? 0.82834 0.65735 0.89265 -0.01182 -0.01425 0.12707  83  ASN A C   
543  O O   . ASN A 76  ? 0.83877 0.66344 0.88710 -0.00273 -0.02030 0.12164  83  ASN A O   
544  C CB  . ASN A 76  ? 0.63494 0.45996 0.71296 -0.02866 -0.03352 0.09155  83  ASN A CB  
545  C CG  . ASN A 76  ? 0.75492 0.55166 0.85214 -0.03834 -0.03550 0.09285  83  ASN A CG  
546  O OD1 . ASN A 76  ? 0.81241 0.59470 0.91542 -0.03494 -0.02795 0.10770  83  ASN A OD1 
547  N ND2 . ASN A 76  ? 0.81365 0.59969 0.91848 -0.05068 -0.04648 0.07725  83  ASN A ND2 
548  N N   . LYS A 77  ? 0.71485 0.54116 0.78974 -0.01190 -0.00164 0.14857  84  LYS A N   
549  C CA  . LYS A 77  ? 0.83875 0.65616 0.90006 0.00008  0.00507  0.16661  84  LYS A CA  
550  C C   . LYS A 77  ? 0.91651 0.70835 0.99020 -0.00005 0.00078  0.16602  84  LYS A C   
551  O O   . LYS A 77  ? 0.88206 0.66931 0.94089 0.01269  -0.00063 0.17235  84  LYS A O   
552  C CB  . LYS A 77  ? 0.80957 0.62955 0.87859 0.00090  0.02254  0.19189  84  LYS A CB  
553  C CG  . LYS A 77  ? 0.82015 0.65946 0.86084 0.00991  0.03155  0.19716  84  LYS A CG  
554  C CD  . LYS A 77  ? 0.98825 0.82624 1.02633 0.01662  0.05214  0.22582  84  LYS A CD  
555  C CE  . LYS A 77  ? 0.99554 0.84881 1.01022 0.02390  0.06569  0.22965  84  LYS A CE  
556  N NZ  . LYS A 77  ? 1.07601 0.94273 1.12866 0.01251  0.07284  0.22810  84  LYS A NZ  
557  N N   . GLN A 78  ? 0.84371 0.61713 0.94403 -0.01406 -0.00185 0.15893  85  GLN A N   
558  C CA  . GLN A 78  ? 0.87388 0.61508 0.98242 -0.01372 -0.00379 0.15691  85  GLN A CA  
559  C C   . GLN A 78  ? 0.92245 0.66047 1.01195 -0.00295 -0.01192 0.14034  85  GLN A C   
560  O O   . GLN A 78  ? 0.88921 0.61238 0.97541 0.00906  -0.00891 0.14762  85  GLN A O   
561  C CB  . GLN A 78  ? 0.99752 0.71592 1.13212 -0.03307 -0.00853 0.14812  85  GLN A CB  
562  C CG  . GLN A 78  ? 1.04153 0.75582 1.20619 -0.04399 0.00085  0.17005  85  GLN A CG  
563  C CD  . GLN A 78  ? 1.38696 1.08584 1.55265 -0.03284 0.01409  0.19424  85  GLN A CD  
564  O OE1 . GLN A 78  ? 1.36741 1.03126 1.54287 -0.03487 0.01445  0.19510  85  GLN A OE1 
565  N NE2 . GLN A 78  ? 1.32888 1.05099 1.48148 -0.02030 0.02538  0.21429  85  GLN A NE2 
566  N N   . ASP A 79  ? 0.75817 0.51104 0.83803 -0.00612 -0.02088 0.12038  86  ASP A N   
567  C CA  . ASP A 79  ? 0.87453 0.62880 0.93972 0.00410  -0.02668 0.10670  86  ASP A CA  
568  C C   . ASP A 79  ? 0.81696 0.59955 0.86601 0.01682  -0.02863 0.11404  86  ASP A C   
569  O O   . ASP A 79  ? 0.81649 0.60352 0.86000 0.02647  -0.03286 0.10860  86  ASP A O   
570  C CB  . ASP A 79  ? 0.83612 0.59197 0.89761 -0.00504 -0.03519 0.08316  86  ASP A CB  
571  C CG  . ASP A 79  ? 0.87350 0.59773 0.94486 -0.01861 -0.03822 0.07267  86  ASP A CG  
572  O OD1 . ASP A 79  ? 1.05340 0.75412 1.13811 -0.02265 -0.03338 0.08340  86  ASP A OD1 
573  O OD2 . ASP A 79  ? 1.15141 0.87249 1.21572 -0.02575 -0.04648 0.05389  86  ASP A OD2 
574  N N   . ARG A 80  ? 0.80262 0.60305 0.84361 0.01693  -0.02569 0.12652  87  ARG A N   
575  C CA  . ARG A 80  ? 0.82547 0.64911 0.84412 0.02624  -0.03059 0.13073  87  ARG A CA  
576  C C   . ARG A 80  ? 0.68434 0.52349 0.69568 0.02419  -0.04039 0.11075  87  ARG A C   
577  O O   . ARG A 80  ? 0.80869 0.65948 0.81209 0.03179  -0.04855 0.10936  87  ARG A O   
578  C CB  . ARG A 80  ? 0.70214 0.52408 0.71640 0.04007  -0.03254 0.14641  87  ARG A CB  
579  C CG  . ARG A 80  ? 0.83576 0.67518 0.82356 0.04756  -0.03685 0.15934  87  ARG A CG  
580  C CD  . ARG A 80  ? 0.95514 0.79059 0.94152 0.06025  -0.03753 0.18158  87  ARG A CD  
581  N NE  . ARG A 80  ? 0.95967 0.80300 0.95671 0.06809  -0.04818 0.17932  87  ARG A NE  
582  C CZ  . ARG A 80  ? 1.03023 0.86711 1.04097 0.07967  -0.04718 0.19605  87  ARG A CZ  
583  N NH1 . ARG A 80  ? 0.84177 0.66181 0.85497 0.08441  -0.03682 0.21582  87  ARG A NH1 
584  N NH2 . ARG A 80  ? 0.94124 0.78948 0.96650 0.08745  -0.05544 0.19496  87  ARG A NH2 
585  N N   . THR A 81  ? 0.66934 0.50983 0.68656 0.01337  -0.04012 0.09703  88  THR A N   
586  C CA  . THR A 81  ? 0.70970 0.56364 0.72074 0.01102  -0.04766 0.07959  88  THR A CA  
587  C C   . THR A 81  ? 0.76385 0.63093 0.76853 0.00487  -0.04529 0.07659  88  THR A C   
588  O O   . THR A 81  ? 0.77658 0.64069 0.79216 -0.00135 -0.03776 0.08340  88  THR A O   
589  C CB  . THR A 81  ? 0.54341 0.38455 0.56573 0.00600  -0.05027 0.06407  88  THR A CB  
590  O OG1 . THR A 81  ? 0.64661 0.47580 0.68127 -0.00573 -0.04791 0.06210  88  THR A OG1 
591  C CG2 . THR A 81  ? 0.59410 0.41858 0.62128 0.01483  -0.04882 0.06649  88  THR A CG2 
592  N N   . LEU A 82  ? 0.74916 0.63037 0.73906 0.00690  -0.05100 0.06762  89  LEU A N   
593  C CA  . LEU A 82  ? 0.58642 0.47771 0.57004 0.00281  -0.04814 0.06179  89  LEU A CA  
594  C C   . LEU A 82  ? 0.65596 0.55236 0.64591 -0.00159 -0.05508 0.04505  89  LEU A C   
595  O O   . LEU A 82  ? 0.69234 0.59234 0.67717 0.00194  -0.06252 0.03851  89  LEU A O   
596  C CB  . LEU A 82  ? 0.69065 0.58793 0.64539 0.00939  -0.04796 0.06545  89  LEU A CB  
597  C CG  . LEU A 82  ? 0.65495 0.55802 0.59929 0.00796  -0.04223 0.05914  89  LEU A CG  
598  C CD1 . LEU A 82  ? 0.64437 0.54853 0.60829 0.00414  -0.02875 0.06767  89  LEU A CD1 
599  C CD2 . LEU A 82  ? 0.68649 0.58655 0.59350 0.01518  -0.04189 0.06150  89  LEU A CD2 
600  N N   . THR A 83  ? 0.52118 0.41930 0.52448 -0.00915 -0.05286 0.04028  90  THR A N   
601  C CA  . THR A 83  ? 0.67100 0.57211 0.67907 -0.01320 -0.05919 0.02628  90  THR A CA  
602  C C   . THR A 83  ? 0.60627 0.52035 0.61172 -0.01444 -0.05677 0.02303  90  THR A C   
603  O O   . THR A 83  ? 0.61977 0.53878 0.63406 -0.01681 -0.04954 0.03080  90  THR A O   
604  C CB  . THR A 83  ? 0.56742 0.45678 0.59119 -0.02136 -0.06227 0.02273  90  THR A CB  
605  O OG1 . THR A 83  ? 0.68670 0.55859 0.70957 -0.01820 -0.06294 0.02351  90  THR A OG1 
606  C CG2 . THR A 83  ? 0.52007 0.41215 0.54286 -0.02482 -0.06879 0.00955  90  THR A CG2 
607  N N   . ILE A 84  ? 0.64228 0.56166 0.63846 -0.01216 -0.06132 0.01328  91  ILE A N   
608  C CA  . ILE A 84  ? 0.62202 0.55007 0.61552 -0.01239 -0.05886 0.00902  91  ILE A CA  
609  C C   . ILE A 84  ? 0.62268 0.55342 0.62691 -0.01678 -0.06440 0.00065  91  ILE A C   
610  O O   . ILE A 84  ? 0.58362 0.51211 0.58361 -0.01530 -0.06947 -0.00645 91  ILE A O   
611  C CB  . ILE A 84  ? 0.48569 0.41414 0.45877 -0.00750 -0.06048 0.00471  91  ILE A CB  
612  C CG1 . ILE A 84  ? 0.68516 0.60827 0.63830 -0.00263 -0.05542 0.01247  91  ILE A CG1 
613  C CG2 . ILE A 84  ? 0.62138 0.55403 0.59326 -0.00773 -0.05810 -0.00173 91  ILE A CG2 
614  C CD1 . ILE A 84  ? 0.82252 0.74135 0.77179 -0.00035 -0.05972 0.01991  91  ILE A CD1 
615  N N   . VAL A 85  ? 0.51576 0.45227 0.53453 -0.02165 -0.06335 0.00324  92  VAL A N   
616  C CA  . VAL A 85  ? 0.46043 0.39921 0.48601 -0.02611 -0.07058 -0.00314 92  VAL A CA  
617  C C   . VAL A 85  ? 0.63186 0.58251 0.65999 -0.02358 -0.06710 -0.00291 92  VAL A C   
618  O O   . VAL A 85  ? 0.63931 0.59711 0.67421 -0.02128 -0.05854 0.00491  92  VAL A O   
619  C CB  . VAL A 85  ? 0.56321 0.49957 0.60552 -0.03542 -0.07677 0.00041  92  VAL A CB  
620  C CG1 . VAL A 85  ? 0.50806 0.43979 0.54597 -0.03974 -0.08778 -0.00864 92  VAL A CG1 
621  C CG2 . VAL A 85  ? 0.59423 0.51623 0.63700 -0.03759 -0.07651 0.00341  92  VAL A CG2 
622  N N   . ASP A 86  ? 0.49434 0.44561 0.51693 -0.02262 -0.07155 -0.01017 93  ASP A N   
623  C CA  . ASP A 86  ? 0.55209 0.51290 0.57966 -0.02033 -0.06888 -0.00890 93  ASP A CA  
624  C C   . ASP A 86  ? 0.54052 0.50285 0.56936 -0.02339 -0.07789 -0.01224 93  ASP A C   
625  O O   . ASP A 86  ? 0.47009 0.42230 0.48799 -0.02490 -0.08365 -0.01860 93  ASP A O   
626  C CB  . ASP A 86  ? 0.52178 0.47907 0.53606 -0.01426 -0.06289 -0.01308 93  ASP A CB  
627  C CG  . ASP A 86  ? 0.66802 0.62102 0.67409 -0.01365 -0.06761 -0.02035 93  ASP A CG  
628  O OD1 . ASP A 86  ? 0.55910 0.51462 0.56752 -0.01396 -0.07049 -0.02164 93  ASP A OD1 
629  O OD2 . ASP A 86  ? 0.69049 0.63858 0.68871 -0.01251 -0.06842 -0.02301 93  ASP A OD2 
630  N N   . THR A 87  ? 0.55617 0.52997 0.59661 -0.02303 -0.07828 -0.00687 94  THR A N   
631  C CA  . THR A 87  ? 0.52055 0.49666 0.55875 -0.02501 -0.08782 -0.00813 94  THR A CA  
632  C C   . THR A 87  ? 0.56379 0.54044 0.59407 -0.01800 -0.08231 -0.00972 94  THR A C   
633  O O   . THR A 87  ? 0.50775 0.49231 0.54300 -0.01657 -0.08536 -0.00475 94  THR A O   
634  C CB  . THR A 87  ? 0.48861 0.47976 0.54937 -0.03019 -0.09525 0.00207  94  THR A CB  
635  O OG1 . THR A 87  ? 0.49809 0.50196 0.57824 -0.02492 -0.08307 0.01213  94  THR A OG1 
636  C CG2 . THR A 87  ? 0.43742 0.42472 0.50605 -0.04067 -0.10551 0.00266  94  THR A CG2 
637  N N   . GLY A 88  ? 0.50867 0.47735 0.52878 -0.01415 -0.07516 -0.01517 95  GLY A N   
638  C CA  . GLY A 88  ? 0.48110 0.44854 0.49761 -0.00935 -0.06976 -0.01605 95  GLY A CA  
639  C C   . GLY A 88  ? 0.50954 0.47369 0.51581 -0.00804 -0.07290 -0.01803 95  GLY A C   
640  O O   . GLY A 88  ? 0.54361 0.50517 0.54141 -0.01016 -0.08030 -0.01925 95  GLY A O   
641  N N   . ILE A 89  ? 0.52360 0.48545 0.52899 -0.00455 -0.06672 -0.01820 96  ILE A N   
642  C CA  . ILE A 89  ? 0.60214 0.56161 0.59887 -0.00111 -0.06529 -0.01694 96  ILE A CA  
643  C C   . ILE A 89  ? 0.55220 0.50410 0.53717 -0.00026 -0.06563 -0.02171 96  ILE A C   
644  O O   . ILE A 89  ? 0.58521 0.53153 0.55550 0.00388  -0.06403 -0.02123 96  ILE A O   
645  C CB  . ILE A 89  ? 0.52786 0.48721 0.53301 0.00137  -0.05726 -0.01370 96  ILE A CB  
646  C CG1 . ILE A 89  ? 0.44820 0.40712 0.44641 0.00646  -0.05308 -0.00790 96  ILE A CG1 
647  C CG2 . ILE A 89  ? 0.38956 0.34642 0.40086 -0.00100 -0.05539 -0.01742 96  ILE A CG2 
648  C CD1 . ILE A 89  ? 0.58915 0.54811 0.59959 0.00824  -0.04546 -0.00151 96  ILE A CD1 
649  N N   . GLY A 90  ? 0.56957 0.51927 0.55825 -0.00255 -0.06647 -0.02547 97  GLY A N   
650  C CA  . GLY A 90  ? 0.47788 0.41952 0.45858 0.00028  -0.06457 -0.02842 97  GLY A CA  
651  C C   . GLY A 90  ? 0.60659 0.55140 0.59515 0.00529  -0.05598 -0.02469 97  GLY A C   
652  O O   . GLY A 90  ? 0.68863 0.64073 0.68947 0.00445  -0.05322 -0.02065 97  GLY A O   
653  N N   . MET A 91  ? 0.60461 0.54293 0.58832 0.01076  -0.05090 -0.02504 98  MET A N   
654  C CA  . MET A 91  ? 0.56769 0.51255 0.56635 0.01631  -0.04155 -0.01840 98  MET A CA  
655  C C   . MET A 91  ? 0.55624 0.48944 0.53783 0.02697  -0.02991 -0.01733 98  MET A C   
656  O O   . MET A 91  ? 0.64498 0.56108 0.60419 0.02971  -0.03079 -0.02409 98  MET A O   
657  C CB  . MET A 91  ? 0.54307 0.49457 0.55975 0.01469  -0.04485 -0.01641 98  MET A CB  
658  C CG  . MET A 91  ? 0.59387 0.55620 0.62657 0.00607  -0.05368 -0.01543 98  MET A CG  
659  S SD  . MET A 91  ? 0.68013 0.64709 0.72281 0.00375  -0.06216 -0.01373 98  MET A SD  
660  C CE  . MET A 91  ? 0.64213 0.59457 0.66328 0.00475  -0.06345 -0.01997 98  MET A CE  
661  N N   . THR A 92  ? 0.64639 0.58623 0.63733 0.03316  -0.01803 -0.00856 99  THR A N   
662  C CA  . THR A 92  ? 0.61916 0.54692 0.59213 0.04626  -0.00228 -0.00555 99  THR A CA  
663  C C   . THR A 92  ? 0.66025 0.59055 0.65107 0.05408  0.00740  -0.00021 99  THR A C   
664  O O   . THR A 92  ? 0.63706 0.58128 0.65576 0.04830  -0.00037 0.00242  99  THR A O   
665  C CB  . THR A 92  ? 0.61554 0.55037 0.59317 0.05127  0.00978  0.00508  99  THR A CB  
666  O OG1 . THR A 92  ? 0.64410 0.60070 0.66526 0.04785  0.01292  0.01640  99  THR A OG1 
667  C CG2 . THR A 92  ? 0.58136 0.51519 0.54511 0.04478  0.00029  0.00240  99  THR A CG2 
668  N N   . LYS A 93  ? 0.63654 0.55210 0.60917 0.06873  0.02521  0.00236  100 LYS A N   
669  C CA  . LYS A 93  ? 0.69300 0.61289 0.68763 0.07956  0.03872  0.01123  100 LYS A CA  
670  C C   . LYS A 93  ? 0.57592 0.52810 0.62204 0.07781  0.04290  0.02853  100 LYS A C   
671  O O   . LYS A 93  ? 0.65029 0.61896 0.73110 0.07693  0.03957  0.03621  100 LYS A O   
672  C CB  . LYS A 93  ? 0.70243 0.59640 0.66375 0.09827  0.06120  0.01107  100 LYS A CB  
673  C CG  . LYS A 93  ? 0.64601 0.53775 0.62490 0.11184  0.07608  0.01840  100 LYS A CG  
674  C CD  . LYS A 93  ? 0.69352 0.56123 0.64408 0.13410  0.10522  0.02214  100 LYS A CD  
675  C CE  . LYS A 93  ? 0.76491 0.62303 0.72718 0.14882  0.11966  0.02684  100 LYS A CE  
676  N NZ  . LYS A 93  ? 0.88413 0.71508 0.81751 0.17386  0.15250  0.03099  100 LYS A NZ  
677  N N   . ALA A 94  ? 0.69074 0.65219 0.74381 0.07647  0.04873  0.03594  101 ALA A N   
678  C CA  . ALA A 94  ? 0.60971 0.60030 0.71447 0.07161  0.05046  0.05246  101 ALA A CA  
679  C C   . ALA A 94  ? 0.61385 0.61935 0.74375 0.05366  0.02577  0.04837  101 ALA A C   
680  O O   . ALA A 94  ? 0.65549 0.68316 0.82867 0.04887  0.02086  0.05967  101 ALA A O   
681  C CB  . ALA A 94  ? 0.62625 0.61925 0.73032 0.07227  0.06075  0.06047  101 ALA A CB  
682  N N   . ASP A 95  ? 0.62897 0.62226 0.73169 0.04390  0.00990  0.03315  102 ASP A N   
683  C CA  . ASP A 95  ? 0.53437 0.53591 0.65104 0.02933  -0.01096 0.02794  102 ASP A CA  
684  C C   . ASP A 95  ? 0.61715 0.62524 0.74752 0.03062  -0.01734 0.03000  102 ASP A C   
685  O O   . ASP A 95  ? 0.57498 0.60000 0.73542 0.02255  -0.02925 0.03634  102 ASP A O   
686  C CB  . ASP A 95  ? 0.48374 0.47009 0.56782 0.02262  -0.02175 0.01326  102 ASP A CB  
687  C CG  . ASP A 95  ? 0.69038 0.67438 0.76899 0.01926  -0.01965 0.01351  102 ASP A CG  
688  O OD1 . ASP A 95  ? 0.63683 0.63147 0.74185 0.01590  -0.01642 0.02293  102 ASP A OD1 
689  O OD2 . ASP A 95  ? 0.65277 0.62478 0.70351 0.01954  -0.02195 0.00567  102 ASP A OD2 
690  N N   . LEU A 96  ? 0.62993 0.62299 0.73763 0.04059  -0.01052 0.02521  103 LEU A N   
691  C CA  . LEU A 96  ? 0.54433 0.54025 0.66200 0.04288  -0.01608 0.02754  103 LEU A CA  
692  C C   . LEU A 96  ? 0.48412 0.50151 0.64381 0.05050  -0.00827 0.04569  103 LEU A C   
693  O O   . LEU A 96  ? 0.65296 0.68270 0.83371 0.04875  -0.01869 0.05215  103 LEU A O   
694  C CB  . LEU A 96  ? 0.46818 0.43819 0.55215 0.05175  -0.00907 0.01828  103 LEU A CB  
695  C CG  . LEU A 96  ? 0.53213 0.48257 0.57984 0.04407  -0.01808 0.00258  103 LEU A CG  
696  C CD1 . LEU A 96  ? 0.59290 0.51480 0.60854 0.05300  -0.00916 -0.00545 103 LEU A CD1 
697  C CD2 . LEU A 96  ? 0.46607 0.42155 0.51732 0.03293  -0.03526 -0.00094 103 LEU A CD2 
698  N N   . ILE A 97  ? 0.60865 0.63207 0.78253 0.05977  0.01041  0.05623  104 ILE A N   
699  C CA  . ILE A 97  ? 0.60033 0.64587 0.81893 0.06977  0.02230  0.07674  104 ILE A CA  
700  C C   . ILE A 97  ? 0.77395 0.84984 1.04093 0.05809  0.01397  0.09095  104 ILE A C   
701  O O   . ILE A 97  ? 0.79863 0.90033 1.11073 0.05547  0.00549  0.10593  104 ILE A O   
702  C CB  . ILE A 97  ? 0.74421 0.77480 0.94795 0.09104  0.05321  0.08192  104 ILE A CB  
703  C CG1 . ILE A 97  ? 0.59691 0.59598 0.75956 0.10201  0.05908  0.06929  104 ILE A CG1 
704  C CG2 . ILE A 97  ? 0.71789 0.77561 0.97506 0.10271  0.07047  0.10724  104 ILE A CG2 
705  C CD1 . ILE A 97  ? 0.53078 0.49891 0.65098 0.11885  0.08398  0.06357  104 ILE A CD1 
706  N N   . ASN A 98  ? 0.68218 0.75534 0.94279 0.05005  0.01451  0.08753  105 ASN A N   
707  C CA  . ASN A 98  ? 0.67425 0.77225 0.98274 0.03906  0.00946  0.10212  105 ASN A CA  
708  C C   . ASN A 98  ? 0.71344 0.80561 1.01282 0.01876  -0.01275 0.08980  105 ASN A C   
709  O O   . ASN A 98  ? 0.67121 0.77892 1.00249 0.00359  -0.03308 0.09425  105 ASN A O   
710  C CB  . ASN A 98  ? 0.59812 0.70003 0.91963 0.05092  0.03754  0.11683  105 ASN A CB  
711  C CG  . ASN A 98  ? 0.79529 0.89138 1.10835 0.07500  0.06548  0.12511  105 ASN A CG  
712  O OD1 . ASN A 98  ? 0.97336 1.04167 1.23609 0.08728  0.08116  0.11449  105 ASN A OD1 
713  N ND2 . ASN A 98  ? 0.86523 0.98633 1.22726 0.08231  0.07179  0.14480  105 ASN A ND2 
714  N N   . ASN A 99  ? 0.79757 0.53649 0.82432 -0.05156 0.03017  0.13187  106 ASN A N   
715  C CA  . ASN A 99  ? 0.83598 0.59969 0.90438 -0.05487 0.00573  0.12441  106 ASN A CA  
716  C C   . ASN A 99  ? 0.85513 0.67942 0.97378 -0.05042 -0.01605 0.10738  106 ASN A C   
717  O O   . ASN A 99  ? 0.76910 0.62104 0.93803 -0.05084 -0.02363 0.09725  106 ASN A O   
718  C CB  . ASN A 99  ? 0.73037 0.45297 0.75016 -0.06429 -0.01380 0.13322  106 ASN A CB  
719  C CG  . ASN A 99  ? 0.85327 0.50577 0.80957 -0.07025 0.00622  0.14969  106 ASN A CG  
720  O OD1 . ASN A 99  ? 0.84056 0.47820 0.80858 -0.06550 0.03847  0.15452  106 ASN A OD1 
721  N ND2 . ASN A 99  ? 1.02839 0.63487 0.91685 -0.08162 -0.01310 0.16020  106 ASN A ND2 
722  N N   . LEU A 100 ? 0.78093 0.61937 0.88130 -0.04693 -0.02399 0.10348  107 LEU A N   
723  C CA  . LEU A 100 ? 0.86170 0.74846 0.99905 -0.04137 -0.04010 0.08826  107 LEU A CA  
724  C C   . LEU A 100 ? 0.84665 0.77264 1.02648 -0.03653 -0.03388 0.08064  107 LEU A C   
725  O O   . LEU A 100 ? 0.97392 0.92893 1.18703 -0.03736 -0.04735 0.06579  107 LEU A O   
726  C CB  . LEU A 100 ? 1.02321 0.91299 1.13204 -0.03786 -0.04602 0.08838  107 LEU A CB  
727  C CG  . LEU A 100 ? 0.85797 0.73738 0.95696 -0.04276 -0.06593 0.09110  107 LEU A CG  
728  C CD1 . LEU A 100 ? 0.58184 0.44468 0.69469 -0.04954 -0.07685 0.09711  107 LEU A CD1 
729  C CD2 . LEU A 100 ? 0.94736 0.79429 0.99410 -0.04963 -0.06673 0.10163  107 LEU A CD2 
730  N N   . GLY A 101 ? 0.86825 0.79254 1.04731 -0.03252 -0.01344 0.09223  108 GLY A N   
731  C CA  . GLY A 101 ? 0.86723 0.83438 1.09780 -0.02945 -0.01218 0.09155  108 GLY A CA  
732  C C   . GLY A 101 ? 0.93087 0.90510 1.20861 -0.03857 -0.01516 0.08753  108 GLY A C   
733  O O   . GLY A 101 ? 0.93661 0.94897 1.25580 -0.04344 -0.03271 0.07603  108 GLY A O   
734  N N   . THR A 102 ? 0.83988 0.77284 1.10707 -0.04264 0.00144  0.09683  109 THR A N   
735  C CA  . THR A 102 ? 0.63844 0.57327 0.95277 -0.05110 0.00329  0.09452  109 THR A CA  
736  C C   . THR A 102 ? 0.82691 0.77578 1.15652 -0.05873 -0.02209 0.07259  109 THR A C   
737  O O   . THR A 102 ? 0.97992 0.95161 1.35762 -0.06793 -0.03056 0.06176  109 THR A O   
738  C CB  . THR A 102 ? 0.69807 0.57696 0.98528 -0.05201 0.02828  0.11014  109 THR A CB  
739  O OG1 . THR A 102 ? 0.78530 0.63804 1.04667 -0.04460 0.05904  0.12936  109 THR A OG1 
740  C CG2 . THR A 102 ? 0.56037 0.43954 0.90214 -0.05953 0.03613  0.11027  109 THR A CG2 
741  N N   . ILE A 103 ? 0.88337 0.81610 1.17477 -0.05605 -0.03294 0.06680  110 ILE A N   
742  C CA  . ILE A 103 ? 0.78338 0.72319 1.08901 -0.06007 -0.04878 0.04813  110 ILE A CA  
743  C C   . ILE A 103 ? 0.91373 0.89034 1.23007 -0.06098 -0.06401 0.02973  110 ILE A C   
744  O O   . ILE A 103 ? 0.99147 0.97219 1.32506 -0.06899 -0.07310 0.01063  110 ILE A O   
745  C CB  . ILE A 103 ? 0.82347 0.74066 1.09743 -0.05499 -0.05423 0.05310  110 ILE A CB  
746  C CG1 . ILE A 103 ? 0.88461 0.76213 1.14286 -0.05719 -0.04606 0.07232  110 ILE A CG1 
747  C CG2 . ILE A 103 ? 0.84192 0.76431 1.13437 -0.05517 -0.06231 0.03628  110 ILE A CG2 
748  C CD1 . ILE A 103 ? 0.75156 0.61647 1.04532 -0.06283 -0.03788 0.07042  110 ILE A CD1 
749  N N   . ALA A 104 ? 0.83311 0.83113 1.13365 -0.05353 -0.06583 0.03547  111 ALA A N   
750  C CA  . ALA A 104 ? 0.74275 0.77055 1.03935 -0.05244 -0.08196 0.02100  111 ALA A CA  
751  C C   . ALA A 104 ? 0.76923 0.82984 1.10408 -0.06242 -0.09438 0.01802  111 ALA A C   
752  O O   . ALA A 104 ? 0.76307 0.83813 1.09315 -0.06964 -0.11422 0.00006  111 ALA A O   
753  C CB  . ALA A 104 ? 0.77886 0.81523 1.04299 -0.03897 -0.07846 0.03077  111 ALA A CB  
754  N N   . LYS A 105 ? 0.86088 0.93037 1.23287 -0.06397 -0.08293 0.03678  112 LYS A N   
755  C CA  . LYS A 105 ? 0.71581 0.82589 1.13985 -0.07197 -0.09500 0.04384  112 LYS A CA  
756  C C   . LYS A 105 ? 0.77136 0.89562 1.21174 -0.09166 -0.12494 0.02003  112 LYS A C   
757  O O   . LYS A 105 ? 0.86132 1.02251 1.31682 -0.09867 -0.15058 0.01976  112 LYS A O   
758  C CB  . LYS A 105 ? 0.73295 0.83804 1.20659 -0.07318 -0.07097 0.06592  112 LYS A CB  
759  C CG  . LYS A 105 ? 0.77929 0.93179 1.32008 -0.07560 -0.07606 0.08615  112 LYS A CG  
760  C CD  . LYS A 105 ? 0.75956 0.90339 1.36100 -0.07848 -0.04817 0.10675  112 LYS A CD  
761  C CE  . LYS A 105 ? 0.71154 0.87536 1.35410 -0.06403 -0.02227 0.14183  112 LYS A CE  
762  N NZ  . LYS A 105 ? 0.68205 0.87795 1.42607 -0.07400 -0.01831 0.16171  112 LYS A NZ  
763  N N   . SER A 106 ? 0.61649 0.70786 1.05019 -0.10170 -0.12246 0.00087  113 SER A N   
764  C CA  . SER A 106 ? 0.75068 0.84151 1.18965 -0.12322 -0.14650 -0.02533 113 SER A CA  
765  C C   . SER A 106 ? 0.78292 0.86592 1.15949 -0.12119 -0.16227 -0.04633 113 SER A C   
766  O O   . SER A 106 ? 0.62179 0.71768 0.98820 -0.13726 -0.19093 -0.06116 113 SER A O   
767  C CB  . SER A 106 ? 0.75012 0.80155 1.20204 -0.13273 -0.13146 -0.03772 113 SER A CB  
768  O OG  . SER A 106 ? 0.97769 1.00920 1.40991 -0.15082 -0.14700 -0.06860 113 SER A OG  
769  N N   . GLY A 107 ? 0.85836 0.91751 1.19140 -0.10274 -0.14432 -0.04653 114 GLY A N   
770  C CA  . GLY A 107 ? 0.80735 0.85502 1.08334 -0.09735 -0.15111 -0.06306 114 GLY A CA  
771  C C   . GLY A 107 ? 0.70235 0.78676 0.96233 -0.09137 -0.16920 -0.05299 114 GLY A C   
772  O O   . GLY A 107 ? 0.78476 0.86501 1.00087 -0.09633 -0.18649 -0.06881 114 GLY A O   
773  N N   . THR A 108 ? 0.61472 0.72989 0.90537 -0.08004 -0.16275 -0.02531 115 THR A N   
774  C CA  . THR A 108 ? 0.63459 0.78752 0.92080 -0.07213 -0.17672 -0.00993 115 THR A CA  
775  C C   . THR A 108 ? 0.61931 0.80406 0.93070 -0.09269 -0.21321 -0.01283 115 THR A C   
776  O O   . THR A 108 ? 0.72286 0.91943 0.99724 -0.09497 -0.23788 -0.01797 115 THR A O   
777  C CB  . THR A 108 ? 0.68512 0.85597 1.00356 -0.05632 -0.15476 0.02135  115 THR A CB  
778  O OG1 . THR A 108 ? 0.64177 0.77642 0.93701 -0.04541 -0.12700 0.02228  115 THR A OG1 
779  C CG2 . THR A 108 ? 0.63249 0.83405 0.93899 -0.04163 -0.15957 0.03908  115 THR A CG2 
780  N N   . LYS A 109 ? 0.53813 0.73556 0.91231 -0.10921 -0.21860 -0.00812 116 LYS A N   
781  C CA  . LYS A 109 ? 0.57347 0.80171 0.98196 -0.13471 -0.25843 -0.01086 116 LYS A CA  
782  C C   . LYS A 109 ? 0.64969 0.84461 0.99055 -0.15452 -0.28443 -0.04728 116 LYS A C   
783  O O   . LYS A 109 ? 0.71230 0.92601 1.02971 -0.16800 -0.32317 -0.05034 116 LYS A O   
784  C CB  . LYS A 109 ? 0.63438 0.87094 1.12322 -0.15031 -0.25293 -0.00337 116 LYS A CB  
785  C CG  . LYS A 109 ? 0.62519 0.90606 1.19510 -0.13955 -0.23993 0.03690  116 LYS A CG  
786  C CD  . LYS A 109 ? 0.73090 1.02472 1.38653 -0.16072 -0.24276 0.04327  116 LYS A CD  
787  C CE  . LYS A 109 ? 0.87260 1.20564 1.61634 -0.14812 -0.22132 0.08667  116 LYS A CE  
788  N NZ  . LYS A 109 ? 0.78934 1.18516 1.57611 -0.14910 -0.25447 0.11254  116 LYS A NZ  
789  N N   . ALA A 110 ? 0.66235 0.80282 0.96769 -0.15652 -0.26219 -0.07360 117 ALA A N   
790  C CA  . ALA A 110 ? 0.72150 0.81557 0.95803 -0.17488 -0.27615 -0.10971 117 ALA A CA  
791  C C   . ALA A 110 ? 0.80295 0.88319 0.95647 -0.16121 -0.28017 -0.11585 117 ALA A C   
792  O O   . ALA A 110 ? 0.89590 0.95026 0.98570 -0.17966 -0.30562 -0.13861 117 ALA A O   
793  C CB  . ALA A 110 ? 0.72611 0.76422 0.95269 -0.17419 -0.24187 -0.13007 117 ALA A CB  
794  N N   . PHE A 111 ? 0.70473 0.79613 0.85267 -0.13046 -0.25452 -0.09618 118 PHE A N   
795  C CA  . PHE A 111 ? 0.77407 0.85190 0.84892 -0.11472 -0.25249 -0.09894 118 PHE A CA  
796  C C   . PHE A 111 ? 0.91959 1.03519 0.97841 -0.12292 -0.29427 -0.08758 118 PHE A C   
797  O O   . PHE A 111 ? 0.97301 1.06172 0.95096 -0.12457 -0.30658 -0.10140 118 PHE A O   
798  C CB  . PHE A 111 ? 0.67142 0.75691 0.75596 -0.08305 -0.21761 -0.07786 118 PHE A CB  
799  C CG  . PHE A 111 ? 0.79061 0.85736 0.80695 -0.06478 -0.20705 -0.08007 118 PHE A CG  
800  C CD1 . PHE A 111 ? 0.85114 0.86441 0.79421 -0.07009 -0.20245 -0.10767 118 PHE A CD1 
801  C CD2 . PHE A 111 ? 0.65851 0.75402 0.68181 -0.04183 -0.19621 -0.05439 118 PHE A CD2 
802  C CE1 . PHE A 111 ? 0.86077 0.85174 0.74073 -0.05160 -0.18699 -0.10796 118 PHE A CE1 
803  C CE2 . PHE A 111 ? 0.75397 0.83081 0.71833 -0.02441 -0.18322 -0.05510 118 PHE A CE2 
804  C CZ  . PHE A 111 ? 0.87120 0.89661 0.76479 -0.02864 -0.17834 -0.08113 118 PHE A CZ  
805  N N   . MET A 112 ? 0.85661 1.03207 0.99145 -0.12740 -0.31506 -0.05973 119 MET A N   
806  C CA  . MET A 112 ? 0.90233 1.12146 1.03633 -0.13572 -0.35929 -0.04225 119 MET A CA  
807  C C   . MET A 112 ? 0.90334 1.10520 1.00289 -0.17398 -0.40675 -0.06752 119 MET A C   
808  O O   . MET A 112 ? 1.10900 1.30966 1.14533 -0.18309 -0.44304 -0.06958 119 MET A O   
809  C CB  . MET A 112 ? 0.87635 1.16424 1.11476 -0.12913 -0.36384 -0.00112 119 MET A CB  
810  C CG  . MET A 112 ? 0.67898 0.96719 0.96044 -0.10263 -0.31282 0.01624  119 MET A CG  
811  S SD  . MET A 112 ? 0.86115 1.15674 1.10812 -0.06537 -0.28478 0.03976  119 MET A SD  
812  C CE  . MET A 112 ? 0.59466 0.95434 0.94490 -0.05512 -0.28071 0.08854  119 MET A CE  
813  N N   . GLU A 113 ? 0.94560 1.12990 1.08143 -0.19833 -0.40798 -0.08655 120 GLU A N   
814  C CA  . GLU A 113 ? 1.08420 1.23986 1.18041 -0.23920 -0.45059 -0.11586 120 GLU A CA  
815  C C   . GLU A 113 ? 1.19845 1.27404 1.16215 -0.24179 -0.44225 -0.15280 120 GLU A C   
816  O O   . GLU A 113 ? 1.32718 1.37895 1.21659 -0.26867 -0.48519 -0.16966 120 GLU A O   
817  C CB  . GLU A 113 ? 1.08517 1.22816 1.24547 -0.26153 -0.44196 -0.13047 120 GLU A CB  
818  C CG  . GLU A 113 ? 0.93509 1.14790 1.22577 -0.25998 -0.44419 -0.09422 120 GLU A CG  
819  C CD  . GLU A 113 ? 1.16714 1.35701 1.51435 -0.27002 -0.41604 -0.10607 120 GLU A CD  
820  O OE1 . GLU A 113 ? 1.31217 1.43748 1.60397 -0.28583 -0.40631 -0.14340 120 GLU A OE1 
821  O OE2 . GLU A 113 ? 1.05865 1.28991 1.50312 -0.26072 -0.39936 -0.07681 120 GLU A OE2 
822  N N   . ALA A 114 ? 1.00791 1.03808 0.93953 -0.21462 -0.38672 -0.16385 121 ALA A N   
823  C CA  . ALA A 114 ? 1.09161 1.04085 0.90595 -0.21254 -0.36672 -0.19551 121 ALA A CA  
824  C C   . ALA A 114 ? 1.29653 1.24805 1.03266 -0.19948 -0.38302 -0.18515 121 ALA A C   
825  O O   . ALA A 114 ? 1.54955 1.43742 1.17388 -0.21336 -0.39294 -0.21124 121 ALA A O   
826  C CB  . ALA A 114 ? 1.04386 0.95538 0.86520 -0.18411 -0.30323 -0.20084 121 ALA A CB  
827  N N   . LEU A 115 ? 1.21543 1.23285 1.00276 -0.17307 -0.38330 -0.14712 122 LEU A N   
828  C CA  . LEU A 115 ? 1.30237 1.32373 1.02117 -0.15667 -0.39412 -0.13289 122 LEU A CA  
829  C C   . LEU A 115 ? 1.37758 1.40243 1.03999 -0.18862 -0.45949 -0.13621 122 LEU A C   
830  O O   . LEU A 115 ? 1.47219 1.46593 1.03381 -0.18374 -0.47018 -0.13836 122 LEU A O   
831  C CB  . LEU A 115 ? 1.12418 1.21667 0.92014 -0.12474 -0.38129 -0.08970 122 LEU A CB  
832  C CG  . LEU A 115 ? 1.10426 1.18051 0.91726 -0.09104 -0.31995 -0.08578 122 LEU A CG  
833  C CD1 . LEU A 115 ? 1.00846 1.14691 0.89153 -0.06503 -0.30861 -0.04565 122 LEU A CD1 
834  C CD2 . LEU A 115 ? 1.21417 1.22369 0.92551 -0.07578 -0.28952 -0.10459 122 LEU A CD2 
835  N N   . GLN A 116 ? 1.41054 1.47106 1.13545 -0.22262 -0.50498 -0.13517 123 GLN A N   
836  C CA  . GLN A 116 ? 1.54770 1.60674 1.22014 -0.26178 -0.57494 -0.14151 123 GLN A CA  
837  C C   . GLN A 116 ? 1.54906 1.51283 1.11880 -0.29831 -0.58136 -0.19329 123 GLN A C   
838  O O   . GLN A 116 ? 1.67365 1.61481 1.16817 -0.31954 -0.61474 -0.20458 123 GLN A O   
839  C CB  . GLN A 116 ? 1.64300 1.79250 1.44657 -0.28126 -0.62052 -0.11054 123 GLN A CB  
840  C CG  . GLN A 116 ? 1.62203 1.86155 1.51504 -0.25050 -0.62382 -0.05573 123 GLN A CG  
841  C CD  . GLN A 116 ? 1.60234 1.92032 1.64865 -0.25528 -0.62972 -0.02560 123 GLN A CD  
842  O OE1 . GLN A 116 ? 1.49839 1.80604 1.59887 -0.27237 -0.61740 -0.04243 123 GLN A OE1 
843  N NE2 . GLN A 116 ? 1.42892 1.82017 1.54487 -0.23873 -0.64391 0.02019  123 GLN A NE2 
844  N N   . ALA A 117 ? 1.69665 1.61042 1.27801 -0.29476 -0.52908 -0.22085 124 ALA A N   
845  C CA  . ALA A 117 ? 1.75963 1.57397 1.24858 -0.32566 -0.52126 -0.27014 124 ALA A CA  
846  C C   . ALA A 117 ? 2.07868 1.79639 1.43366 -0.30494 -0.47148 -0.29482 124 ALA A C   
847  O O   . ALA A 117 ? 2.16858 1.80297 1.47873 -0.30954 -0.42696 -0.32908 124 ALA A O   
848  C CB  . ALA A 117 ? 1.45354 1.26304 1.03188 -0.33178 -0.48809 -0.28310 124 ALA A CB  
849  N N   . GLY A 118 ? 2.05768 1.78280 1.35271 -0.28030 -0.47302 -0.27563 125 GLY A N   
850  C CA  . GLY A 118 ? 2.07058 1.70290 1.23671 -0.26033 -0.42552 -0.29541 125 GLY A CA  
851  C C   . GLY A 118 ? 1.87808 1.51002 1.09022 -0.21191 -0.34957 -0.28280 125 GLY A C   
852  O O   . GLY A 118 ? 2.07114 1.62802 1.19013 -0.19190 -0.30288 -0.29525 125 GLY A O   
853  N N   . ALA A 119 ? 1.68640 1.39550 1.03655 -0.19370 -0.33549 -0.25757 126 ALA A N   
854  C CA  . ALA A 119 ? 1.63871 1.35114 1.03788 -0.15270 -0.27162 -0.24377 126 ALA A CA  
855  C C   . ALA A 119 ? 1.56714 1.33710 0.98574 -0.12053 -0.27084 -0.20714 126 ALA A C   
856  O O   . ALA A 119 ? 1.51724 1.35583 0.97009 -0.12564 -0.31715 -0.18217 126 ALA A O   
857  C CB  . ALA A 119 ? 1.34515 1.09972 0.86918 -0.15102 -0.25584 -0.23601 126 ALA A CB  
858  N N   . ASP A 120 ? 1.42273 1.16369 0.82538 -0.08711 -0.21555 -0.20196 127 ASP A N   
859  C CA  . ASP A 120 ? 1.48042 1.26785 0.90556 -0.05505 -0.20452 -0.16876 127 ASP A CA  
860  C C   . ASP A 120 ? 1.36822 1.20324 0.90782 -0.03354 -0.17280 -0.14800 127 ASP A C   
861  O O   . ASP A 120 ? 1.24726 1.07668 0.84270 -0.04100 -0.15827 -0.15786 127 ASP A O   
862  C CB  . ASP A 120 ? 1.47718 1.19634 0.79721 -0.03403 -0.16716 -0.17490 127 ASP A CB  
863  C CG  . ASP A 120 ? 1.56974 1.23518 0.90086 -0.01400 -0.09980 -0.18525 127 ASP A CG  
864  O OD1 . ASP A 120 ? 1.53442 1.15565 0.86766 -0.02942 -0.08501 -0.20988 127 ASP A OD1 
865  O OD2 . ASP A 120 ? 1.51025 1.17876 0.85427 0.01707  -0.06107 -0.16636 127 ASP A OD2 
866  N N   . ILE A 121 ? 1.30350 1.18172 0.87236 -0.00766 -0.16293 -0.11819 128 ILE A N   
867  C CA  . ILE A 121 ? 1.12479 1.04957 0.79283 0.00847  -0.14186 -0.09619 128 ILE A CA  
868  C C   . ILE A 121 ? 1.11326 0.99690 0.80106 0.01958  -0.09419 -0.10607 128 ILE A C   
869  O O   . ILE A 121 ? 1.08977 0.99858 0.85586 0.02096  -0.08495 -0.09676 128 ILE A O   
870  C CB  . ILE A 121 ? 1.09290 1.05879 0.77199 0.03238  -0.13778 -0.06492 128 ILE A CB  
871  C CG1 . ILE A 121 ? 1.17986 1.20561 0.88377 0.02230  -0.18440 -0.04495 128 ILE A CG1 
872  C CG2 . ILE A 121 ? 1.10629 1.09369 0.85867 0.05040  -0.10469 -0.04735 128 ILE A CG2 
873  C CD1 . ILE A 121 ? 1.04392 1.08924 0.71262 0.04131  -0.18945 -0.02025 128 ILE A CD1 
874  N N   . SER A 122 ? 1.20606 1.02304 0.82370 0.02707  -0.06299 -0.12304 129 SER A N   
875  C CA  . SER A 122 ? 1.13239 0.91402 0.77995 0.04197  -0.01346 -0.12478 129 SER A CA  
876  C C   . SER A 122 ? 1.15351 0.92581 0.85372 0.02660  -0.01088 -0.13708 129 SER A C   
877  O O   . SER A 122 ? 1.09669 0.85483 0.84558 0.03894  0.02453  -0.13044 129 SER A O   
878  C CB  . SER A 122 ? 1.17775 0.88187 0.73637 0.05381  0.02538  -0.13945 129 SER A CB  
879  O OG  . SER A 122 ? 1.32932 0.97221 0.81667 0.03215  0.01997  -0.17105 129 SER A OG  
880  N N   . MET A 123 ? 1.03750 0.81862 0.73535 0.00014  -0.04727 -0.15185 130 MET A N   
881  C CA  . MET A 123 ? 1.01898 0.79190 0.76909 -0.01422 -0.04406 -0.16179 130 MET A CA  
882  C C   . MET A 123 ? 0.98953 0.82919 0.83156 -0.01676 -0.06445 -0.13988 130 MET A C   
883  O O   . MET A 123 ? 0.86469 0.70618 0.74753 -0.03250 -0.07237 -0.14635 130 MET A O   
884  C CB  . MET A 123 ? 1.10375 0.83718 0.79860 -0.04416 -0.06672 -0.19277 130 MET A CB  
885  C CG  . MET A 123 ? 1.20729 0.86845 0.78492 -0.04747 -0.05616 -0.21643 130 MET A CG  
886  S SD  . MET A 123 ? 1.48175 1.09944 0.98955 -0.09137 -0.09626 -0.25311 130 MET A SD  
887  C CE  . MET A 123 ? 1.26851 0.89427 0.87537 -0.10328 -0.08486 -0.25767 130 MET A CE  
888  N N   . ILE A 124 ? 0.84028 0.72722 0.71071 -0.00135 -0.06867 -0.11417 131 ILE A N   
889  C CA  . ILE A 124 ? 0.80378 0.74365 0.74475 -0.00428 -0.08508 -0.09379 131 ILE A CA  
890  C C   . ILE A 124 ? 0.77331 0.70464 0.77154 -0.00330 -0.06639 -0.08842 131 ILE A C   
891  O O   . ILE A 124 ? 0.67502 0.62918 0.71936 -0.01366 -0.07963 -0.08114 131 ILE A O   
892  C CB  . ILE A 124 ? 0.74939 0.72683 0.69748 0.01303  -0.08489 -0.06888 131 ILE A CB  
893  C CG1 . ILE A 124 ? 0.63015 0.65209 0.63649 0.00884  -0.09872 -0.04895 131 ILE A CG1 
894  C CG2 . ILE A 124 ? 0.64644 0.60540 0.59705 0.03346  -0.05084 -0.05969 131 ILE A CG2 
895  C CD1 . ILE A 124 ? 0.62848 0.68354 0.63541 0.02252  -0.09978 -0.02631 131 ILE A CD1 
896  N N   . GLY A 125 ? 0.73314 0.63050 0.73174 0.00953  -0.03464 -0.08903 132 GLY A N   
897  C CA  . GLY A 125 ? 0.77657 0.66965 0.83437 0.01132  -0.02062 -0.07795 132 GLY A CA  
898  C C   . GLY A 125 ? 0.87667 0.74948 0.94991 -0.00538 -0.02421 -0.09282 132 GLY A C   
899  O O   . GLY A 125 ? 0.80801 0.69225 0.93272 -0.00885 -0.02663 -0.07992 132 GLY A O   
900  N N   . GLN A 126 ? 0.77786 0.61579 0.80163 -0.01744 -0.02500 -0.12004 133 GLN A N   
901  C CA  . GLN A 126 ? 0.88013 0.69187 0.91465 -0.03601 -0.02630 -0.13753 133 GLN A CA  
902  C C   . GLN A 126 ? 0.82315 0.67607 0.89846 -0.05242 -0.05721 -0.13108 133 GLN A C   
903  O O   . GLN A 126 ? 0.96417 0.80017 1.06251 -0.06720 -0.05684 -0.14100 133 GLN A O   
904  C CB  . GLN A 126 ? 0.91399 0.67445 0.87288 -0.05057 -0.02550 -0.17060 133 GLN A CB  
905  C CG  . GLN A 126 ? 1.01510 0.72650 0.91669 -0.03361 0.00888  -0.17785 133 GLN A CG  
906  C CD  . GLN A 126 ? 1.30917 0.94734 1.12660 -0.05036 0.01832  -0.21338 133 GLN A CD  
907  O OE1 . GLN A 126 ? 1.39619 1.01232 1.21330 -0.07384 0.00821  -0.23284 133 GLN A OE1 
908  N NE2 . GLN A 126 ? 1.38396 0.97747 1.12381 -0.03965 0.03946  -0.22264 133 GLN A NE2 
909  N N   . PHE A 127 ? 0.66609 0.56824 0.75270 -0.04926 -0.07877 -0.11363 134 PHE A N   
910  C CA  . PHE A 127 ? 0.74126 0.68044 0.87048 -0.06145 -0.10066 -0.10298 134 PHE A CA  
911  C C   . PHE A 127 ? 0.68671 0.65004 0.85651 -0.04871 -0.09330 -0.07447 134 PHE A C   
912  O O   . PHE A 127 ? 0.67591 0.66459 0.87658 -0.05493 -0.10379 -0.06176 134 PHE A O   
913  C CB  . PHE A 127 ? 0.64153 0.61372 0.75214 -0.07089 -0.13093 -0.10432 134 PHE A CB  
914  C CG  . PHE A 127 ? 0.71818 0.66234 0.77438 -0.08806 -0.14634 -0.13239 134 PHE A CG  
915  C CD1 . PHE A 127 ? 0.76570 0.68271 0.75309 -0.07866 -0.13905 -0.14284 134 PHE A CD1 
916  C CD2 . PHE A 127 ? 0.82850 0.76719 0.89740 -0.11538 -0.16736 -0.14861 134 PHE A CD2 
917  C CE1 . PHE A 127 ? 0.85344 0.73247 0.77325 -0.09671 -0.15330 -0.16998 134 PHE A CE1 
918  C CE2 . PHE A 127 ? 0.86847 0.77314 0.87629 -0.13628 -0.18544 -0.17657 134 PHE A CE2 
919  C CZ  . PHE A 127 ? 0.93839 0.81008 0.86523 -0.12723 -0.17882 -0.18785 134 PHE A CZ  
920  N N   . GLY A 128 ? 0.63143 0.58354 0.80065 -0.03243 -0.07489 -0.06331 135 GLY A N   
921  C CA  . GLY A 128 ? 0.66110 0.62568 0.85904 -0.02540 -0.07172 -0.03816 135 GLY A CA  
922  C C   . GLY A 128 ? 0.68004 0.67337 0.86829 -0.01973 -0.07920 -0.02259 135 GLY A C   
923  O O   . GLY A 128 ? 0.56326 0.55993 0.76533 -0.01962 -0.07848 -0.00445 135 GLY A O   
924  N N   . VAL A 129 ? 0.65707 0.66568 0.81668 -0.01506 -0.08463 -0.02826 136 VAL A N   
925  C CA  . VAL A 129 ? 0.56513 0.59931 0.71797 -0.00733 -0.08687 -0.01163 136 VAL A CA  
926  C C   . VAL A 129 ? 0.59176 0.62393 0.71354 0.00746  -0.07748 -0.01110 136 VAL A C   
927  O O   . VAL A 129 ? 0.64719 0.69931 0.75221 0.01494  -0.07993 -0.00345 136 VAL A O   
928  C CB  . VAL A 129 ? 0.62410 0.68730 0.78521 -0.01484 -0.10337 -0.01039 136 VAL A CB  
929  C CG1 . VAL A 129 ? 0.59961 0.66332 0.79979 -0.02862 -0.10716 -0.00809 136 VAL A CG1 
930  C CG2 . VAL A 129 ? 0.65390 0.71831 0.78655 -0.02046 -0.11906 -0.02956 136 VAL A CG2 
931  N N   . GLY A 130 ? 0.58598 0.60827 0.70884 -0.03476 -0.11905 -0.06192 137 GLY A N   
932  C CA  . GLY A 130 ? 0.70831 0.73408 0.80724 -0.02512 -0.11819 -0.06178 137 GLY A CA  
933  C C   . GLY A 130 ? 0.62543 0.65669 0.72523 -0.01659 -0.10936 -0.04680 137 GLY A C   
934  O O   . GLY A 130 ? 0.58625 0.62617 0.67314 -0.00990 -0.10962 -0.04157 137 GLY A O   
935  N N   . PHE A 131 ? 0.56139 0.58592 0.67476 -0.01670 -0.10090 -0.03985 138 PHE A N   
936  C CA  . PHE A 131 ? 0.67252 0.69708 0.78593 -0.00961 -0.09241 -0.02934 138 PHE A CA  
937  C C   . PHE A 131 ? 0.62969 0.67116 0.74830 -0.00449 -0.09572 -0.02010 138 PHE A C   
938  O O   . PHE A 131 ? 0.51843 0.55726 0.63066 0.00236  -0.09040 -0.01252 138 PHE A O   
939  C CB  . PHE A 131 ? 0.55859 0.57572 0.68329 -0.01059 -0.08425 -0.02554 138 PHE A CB  
940  C CG  . PHE A 131 ? 0.66620 0.68415 0.79414 -0.00402 -0.07671 -0.01735 138 PHE A CG  
941  C CD1 . PHE A 131 ? 0.46329 0.46939 0.57996 -0.00059 -0.07113 -0.01726 138 PHE A CD1 
942  C CD2 . PHE A 131 ? 0.57881 0.60917 0.72347 -0.00136 -0.07481 -0.01047 138 PHE A CD2 
943  C CE1 . PHE A 131 ? 0.49293 0.49408 0.61207 0.00457  -0.06410 -0.01250 138 PHE A CE1 
944  C CE2 . PHE A 131 ? 0.61667 0.64343 0.76357 0.00667  -0.06622 -0.00461 138 PHE A CE2 
945  C CZ  . PHE A 131 ? 0.55838 0.56780 0.69111 0.00924  -0.06101 -0.00664 138 PHE A CZ  
946  N N   . TYR A 132 ? 0.57446 0.63383 0.70729 -0.00780 -0.10469 -0.01950 139 TYR A N   
947  C CA  . TYR A 132 ? 0.58792 0.66738 0.72980 -0.00081 -0.10877 -0.00825 139 TYR A CA  
948  C C   . TYR A 132 ? 0.65960 0.74769 0.78119 0.00414  -0.11672 -0.00618 139 TYR A C   
949  O O   . TYR A 132 ? 0.57889 0.68209 0.70463 0.01267  -0.11957 0.00658  139 TYR A O   
950  C CB  . TYR A 132 ? 0.44635 0.54824 0.61519 -0.00635 -0.11662 -0.00721 139 TYR A CB  
951  C CG  . TYR A 132 ? 0.54980 0.64592 0.73813 -0.00815 -0.10458 -0.00418 139 TYR A CG  
952  C CD1 . TYR A 132 ? 0.60418 0.69730 0.79858 0.00241  -0.09211 0.00564  139 TYR A CD1 
953  C CD2 . TYR A 132 ? 0.65688 0.74779 0.85502 -0.01972 -0.10422 -0.01105 139 TYR A CD2 
954  C CE1 . TYR A 132 ? 0.66425 0.75263 0.87067 0.00227  -0.07972 0.00752  139 TYR A CE1 
955  C CE2 . TYR A 132 ? 0.67992 0.76672 0.89207 -0.02027 -0.09143 -0.00579 139 TYR A CE2 
956  C CZ  . TYR A 132 ? 0.66456 0.75154 0.87890 -0.00884 -0.07919 0.00294  139 TYR A CZ  
957  O OH  . TYR A 132 ? 0.82902 0.91277 1.05193 -0.00790 -0.06526 0.00726  139 TYR A OH  
958  N N   . SER A 133 ? 0.62065 0.69968 0.71958 0.00088  -0.11893 -0.01697 140 SER A N   
959  C CA  . SER A 133 ? 0.47507 0.56049 0.54943 0.00747  -0.12176 -0.01321 140 SER A CA  
960  C C   . SER A 133 ? 0.63154 0.70662 0.70144 0.01590  -0.10856 0.00114  140 SER A C   
961  O O   . SER A 133 ? 0.64342 0.72438 0.69555 0.02249  -0.10811 0.01003  140 SER A O   
962  C CB  . SER A 133 ? 0.57924 0.65618 0.63011 0.00363  -0.12356 -0.02927 140 SER A CB  
963  O OG  . SER A 133 ? 0.51195 0.56802 0.56172 0.00313  -0.11067 -0.03282 140 SER A OG  
964  N N   . ALA A 134 ? 0.60924 0.66843 0.69379 0.01515  -0.09777 0.00333  141 ALA A N   
965  C CA  . ALA A 134 ? 0.57926 0.62613 0.66421 0.02085  -0.08632 0.01522  141 ALA A CA  
966  C C   . ALA A 134 ? 0.57184 0.62896 0.66183 0.03076  -0.08794 0.03231  141 ALA A C   
967  O O   . ALA A 134 ? 0.51918 0.56821 0.60285 0.03634  -0.08051 0.04496  141 ALA A O   
968  C CB  . ALA A 134 ? 0.59805 0.62770 0.69686 0.01789  -0.07751 0.01135  141 ALA A CB  
969  N N   . TYR A 135 ? 0.51255 0.58846 0.61661 0.03325  -0.09728 0.03453  142 TYR A N   
970  C CA  . TYR A 135 ? 0.63108 0.72053 0.74469 0.04516  -0.09983 0.05242  142 TYR A CA  
971  C C   . TYR A 135 ? 0.61678 0.72623 0.71040 0.05039  -0.11095 0.06119  142 TYR A C   
972  O O   . TYR A 135 ? 0.66361 0.78943 0.76405 0.06170  -0.11610 0.07815  142 TYR A O   
973  C CB  . TYR A 135 ? 0.54880 0.65618 0.69046 0.04641  -0.10500 0.05239  142 TYR A CB  
974  C CG  . TYR A 135 ? 0.60615 0.69370 0.76357 0.04605  -0.09069 0.04843  142 TYR A CG  
975  C CD1 . TYR A 135 ? 0.52863 0.60199 0.69586 0.05765  -0.07874 0.05953  142 TYR A CD1 
976  C CD2 . TYR A 135 ? 0.50802 0.58836 0.66740 0.03487  -0.08845 0.03340  142 TYR A CD2 
977  C CE1 . TYR A 135 ? 0.42689 0.48090 0.60282 0.05778  -0.06563 0.05289  142 TYR A CE1 
978  C CE2 . TYR A 135 ? 0.50709 0.57076 0.67474 0.03545  -0.07557 0.02992  142 TYR A CE2 
979  C CZ  . TYR A 135 ? 0.64282 0.69390 0.81716 0.04673  -0.06449 0.03824  142 TYR A CZ  
980  O OH  . TYR A 135 ? 0.56596 0.59970 0.74349 0.04789  -0.05178 0.03200  142 TYR A OH  
981  N N   . LEU A 136 ? 0.54824 0.65762 0.61611 0.04411  -0.11436 0.05051  143 LEU A N   
982  C CA  . LEU A 136 ? 0.51152 0.63541 0.55199 0.05093  -0.12036 0.06012  143 LEU A CA  
983  C C   . LEU A 136 ? 0.67970 0.78753 0.71247 0.05923  -0.10494 0.08010  143 LEU A C   
984  O O   . LEU A 136 ? 0.58896 0.70893 0.60863 0.07003  -0.10751 0.09944  143 LEU A O   
985  C CB  . LEU A 136 ? 0.70073 0.82673 0.71376 0.04333  -0.12531 0.04114  143 LEU A CB  
986  C CG  . LEU A 136 ? 0.58472 0.72186 0.60084 0.03302  -0.14094 0.01903  143 LEU A CG  
987  C CD1 . LEU A 136 ? 0.55430 0.67619 0.54994 0.02622  -0.13647 -0.00099 143 LEU A CD1 
988  C CD2 . LEU A 136 ? 0.50736 0.67618 0.51284 0.03606  -0.16148 0.02094  143 LEU A CD2 
989  N N   . VAL A 137 ? 0.58593 0.66722 0.62750 0.05382  -0.08952 0.07663  144 VAL A N   
990  C CA  . VAL A 137 ? 0.69328 0.75674 0.73164 0.05742  -0.07410 0.09334  144 VAL A CA  
991  C C   . VAL A 137 ? 0.62042 0.65942 0.68504 0.05843  -0.06357 0.09940  144 VAL A C   
992  O O   . VAL A 137 ? 0.63173 0.65266 0.69862 0.06090  -0.05122 0.11469  144 VAL A O   
993  C CB  . VAL A 137 ? 0.61354 0.66894 0.63813 0.04903  -0.06455 0.08416  144 VAL A CB  
994  C CG1 . VAL A 137 ? 0.64928 0.72554 0.64393 0.05027  -0.07252 0.07645  144 VAL A CG1 
995  C CG2 . VAL A 137 ? 0.51288 0.55394 0.55390 0.03822  -0.06180 0.06440  144 VAL A CG2 
996  N N   . ALA A 138 ? 0.57665 0.61293 0.66055 0.05642  -0.06677 0.08782  145 ALA A N   
997  C CA  . ALA A 138 ? 0.55181 0.56275 0.65589 0.05741  -0.05589 0.08833  145 ALA A CA  
998  C C   . ALA A 138 ? 0.61616 0.63569 0.73854 0.06966  -0.05915 0.09685  145 ALA A C   
999  O O   . ALA A 138 ? 0.63194 0.67681 0.76005 0.07022  -0.07060 0.09131  145 ALA A O   
1000 C CB  . ALA A 138 ? 0.46858 0.46753 0.57732 0.04546  -0.05319 0.06670  145 ALA A CB  
1001 N N   . GLU A 139 ? 0.61681 0.61518 0.75117 0.07945  -0.04847 0.11057  146 GLU A N   
1002 C CA  . GLU A 139 ? 0.67939 0.68224 0.83549 0.09334  -0.04762 0.11772  146 GLU A CA  
1003 C C   . GLU A 139 ? 0.62459 0.61422 0.79359 0.08926  -0.04056 0.09904  146 GLU A C   
1004 O O   . GLU A 139 ? 0.59779 0.60140 0.78532 0.09870  -0.04081 0.10027  146 GLU A O   
1005 C CB  . GLU A 139 ? 0.63458 0.61545 0.79849 0.10794  -0.03717 0.14009  146 GLU A CB  
1006 C CG  . GLU A 139 ? 0.77645 0.71196 0.94173 0.10132  -0.02098 0.13415  146 GLU A CG  
1007 C CD  . GLU A 139 ? 1.06500 0.97504 1.23470 0.11200  -0.01058 0.15853  146 GLU A CD  
1008 O OE1 . GLU A 139 ? 1.07850 0.94884 1.25261 0.10535  0.00241  0.15429  146 GLU A OE1 
1009 O OE2 . GLU A 139 ? 1.15525 1.08466 1.32448 0.12669  -0.01595 0.18240  146 GLU A OE2 
1010 N N   . LYS A 140 ? 0.55672 0.52297 0.71634 0.07603  -0.03426 0.08275  147 LYS A N   
1011 C CA  . LYS A 140 ? 0.61447 0.56702 0.77923 0.07219  -0.02755 0.06496  147 LYS A CA  
1012 C C   . LYS A 140 ? 0.57147 0.51887 0.72119 0.05523  -0.03018 0.04796  147 LYS A C   
1013 O O   . LYS A 140 ? 0.56356 0.50121 0.70396 0.04742  -0.02977 0.04914  147 LYS A O   
1014 C CB  . LYS A 140 ? 0.60053 0.51747 0.77303 0.07999  -0.01306 0.06521  147 LYS A CB  
1015 C CG  . LYS A 140 ? 0.57332 0.47126 0.74153 0.07402  -0.00583 0.04350  147 LYS A CG  
1016 C CD  . LYS A 140 ? 0.68254 0.54974 0.85975 0.08671  0.00856  0.04205  147 LYS A CD  
1017 C CE  . LYS A 140 ? 0.77310 0.59994 0.94006 0.07589  0.01511  0.02717  147 LYS A CE  
1018 N NZ  . LYS A 140 ? 0.96386 0.75304 1.14030 0.08835  0.02900  0.02898  147 LYS A NZ  
1019 N N   . VAL A 141 ? 0.47340 0.42943 0.62274 0.05044  -0.03214 0.03433  148 VAL A N   
1020 C CA  . VAL A 141 ? 0.49752 0.45093 0.63426 0.03703  -0.03526 0.01980  148 VAL A CA  
1021 C C   . VAL A 141 ? 0.48842 0.42512 0.62278 0.03593  -0.02774 0.00652  148 VAL A C   
1022 O O   . VAL A 141 ? 0.51475 0.45723 0.65632 0.04339  -0.02303 0.00587  148 VAL A O   
1023 C CB  . VAL A 141 ? 0.48625 0.46539 0.62079 0.03199  -0.04567 0.01707  148 VAL A CB  
1024 C CG1 . VAL A 141 ? 0.42175 0.39594 0.54541 0.02126  -0.04746 0.00393  148 VAL A CG1 
1025 C CG2 . VAL A 141 ? 0.48836 0.48338 0.61858 0.03294  -0.05394 0.02660  148 VAL A CG2 
1026 N N   . THR A 142 ? 0.57859 0.49731 0.70291 0.02681  -0.02661 -0.00389 149 THR A N   
1027 C CA  . THR A 142 ? 0.48945 0.39507 0.60430 0.02384  -0.02281 -0.01905 149 THR A CA  
1028 C C   . THR A 142 ? 0.59844 0.51507 0.70279 0.01342  -0.03104 -0.02673 149 THR A C   
1029 O O   . THR A 142 ? 0.54472 0.46561 0.64915 0.00598  -0.03676 -0.02522 149 THR A O   
1030 C CB  . THR A 142 ? 0.49900 0.37395 0.61149 0.02143  -0.01672 -0.02697 149 THR A CB  
1031 O OG1 . THR A 142 ? 0.61135 0.47292 0.73596 0.03235  -0.00864 -0.01640 149 THR A OG1 
1032 C CG2 . THR A 142 ? 0.57899 0.44083 0.67715 0.02118  -0.01275 -0.04446 149 THR A CG2 
1033 N N   . VAL A 143 ? 0.51285 0.43484 0.60896 0.01430  -0.03028 -0.03316 150 VAL A N   
1034 C CA  . VAL A 143 ? 0.47800 0.40919 0.56427 0.00712  -0.03745 -0.03802 150 VAL A CA  
1035 C C   . VAL A 143 ? 0.59945 0.51923 0.66876 0.00567  -0.03561 -0.05042 150 VAL A C   
1036 O O   . VAL A 143 ? 0.64001 0.55578 0.70201 0.01253  -0.02742 -0.05325 150 VAL A O   
1037 C CB  . VAL A 143 ? 0.58981 0.53912 0.68044 0.00885  -0.03929 -0.03134 150 VAL A CB  
1038 C CG1 . VAL A 143 ? 0.50538 0.45981 0.58688 0.00328  -0.04570 -0.03431 150 VAL A CG1 
1039 C CG2 . VAL A 143 ? 0.54487 0.50602 0.64895 0.00977  -0.04331 -0.02229 150 VAL A CG2 
1040 N N   . ILE A 144 ? 0.60868 0.52543 0.67179 -0.00285 -0.04314 -0.05796 151 ILE A N   
1041 C CA  . ILE A 144 ? 0.63931 0.55115 0.68332 -0.00581 -0.04639 -0.07045 151 ILE A CA  
1042 C C   . ILE A 144 ? 0.65682 0.58693 0.69493 -0.00708 -0.05425 -0.06596 151 ILE A C   
1043 O O   . ILE A 144 ? 0.60472 0.54583 0.65463 -0.01093 -0.06076 -0.06040 151 ILE A O   
1044 C CB  . ILE A 144 ? 0.63582 0.53501 0.68093 -0.01574 -0.05183 -0.08202 151 ILE A CB  
1045 C CG1 . ILE A 144 ? 0.55860 0.43703 0.61666 -0.01486 -0.04343 -0.08121 151 ILE A CG1 
1046 C CG2 . ILE A 144 ? 0.61876 0.51081 0.64042 -0.01827 -0.05589 -0.09852 151 ILE A CG2 
1047 C CD1 . ILE A 144 ? 0.62190 0.48046 0.66946 -0.00533 -0.03223 -0.08854 151 ILE A CD1 
1048 N N   . THR A 145 ? 0.61864 0.55136 0.63831 -0.00241 -0.05209 -0.06706 152 THR A N   
1049 C CA  . THR A 145 ? 0.66108 0.60807 0.67604 -0.00151 -0.05765 -0.05899 152 THR A CA  
1050 C C   . THR A 145 ? 0.58915 0.53730 0.57644 0.00082  -0.06004 -0.06428 152 THR A C   
1051 O O   . THR A 145 ? 0.64434 0.58270 0.61358 0.00414  -0.05309 -0.07307 152 THR A O   
1052 C CB  . THR A 145 ? 0.52237 0.47511 0.54809 0.00301  -0.05050 -0.04598 152 THR A CB  
1053 O OG1 . THR A 145 ? 0.60403 0.56522 0.63015 0.00286  -0.05622 -0.03787 152 THR A OG1 
1054 C CG2 . THR A 145 ? 0.55701 0.50740 0.57248 0.00946  -0.03817 -0.04410 152 THR A CG2 
1055 N N   . LYS A 146 ? 0.53298 0.49346 0.51559 0.00055  -0.06975 -0.05870 153 LYS A N   
1056 C CA  . LYS A 146 ? 0.63716 0.60306 0.59104 0.00368  -0.07496 -0.06100 153 LYS A CA  
1057 C C   . LYS A 146 ? 0.62676 0.60395 0.58070 0.00899  -0.07784 -0.04401 153 LYS A C   
1058 O O   . LYS A 146 ? 0.55260 0.53811 0.52452 0.00751  -0.08642 -0.03899 153 LYS A O   
1059 C CB  . LYS A 146 ? 0.58746 0.55762 0.53487 -0.00373 -0.08980 -0.07592 153 LYS A CB  
1060 C CG  . LYS A 146 ? 0.50821 0.48890 0.42365 -0.00056 -0.09961 -0.07876 153 LYS A CG  
1061 C CD  . LYS A 146 ? 0.57698 0.54605 0.45833 0.00585  -0.08806 -0.08521 153 LYS A CD  
1062 C CE  . LYS A 146 ? 0.58113 0.56123 0.42348 0.00898  -0.09916 -0.09044 153 LYS A CE  
1063 N NZ  . LYS A 146 ? 0.67156 0.66681 0.50389 0.01853  -0.09976 -0.06766 153 LYS A NZ  
1064 N N   . HIS A 147 ? 0.69212 0.66853 0.62687 0.01597  -0.06894 -0.03434 154 HIS A N   
1065 C CA  . HIS A 147 ? 0.47824 0.46069 0.41017 0.02184  -0.06938 -0.01575 154 HIS A CA  
1066 C C   . HIS A 147 ? 0.63529 0.62710 0.53228 0.02760  -0.07687 -0.01414 154 HIS A C   
1067 O O   . HIS A 147 ? 0.73826 0.72859 0.60722 0.02840  -0.07469 -0.02592 154 HIS A O   
1068 C CB  . HIS A 147 ? 0.58339 0.55907 0.52238 0.02434  -0.05236 -0.00209 154 HIS A CB  
1069 C CG  . HIS A 147 ? 0.63422 0.60952 0.57926 0.02806  -0.05101 0.01809  154 HIS A CG  
1070 N ND1 . HIS A 147 ? 0.67730 0.65661 0.59671 0.03573  -0.05045 0.03197  154 HIS A ND1 
1071 C CD2 . HIS A 147 ? 0.55272 0.52137 0.52548 0.02547  -0.04949 0.02677  154 HIS A CD2 
1072 C CE1 . HIS A 147 ? 0.62936 0.60265 0.56338 0.03790  -0.04784 0.05015  154 HIS A CE1 
1073 N NE2 . HIS A 147 ? 0.55800 0.52354 0.52456 0.03121  -0.04733 0.04560  154 HIS A NE2 
1074 N N   . ASN A 148 ? 0.65684 0.65808 0.55415 0.03286  -0.08593 0.00030  155 ASN A N   
1075 C CA  . ASN A 148 ? 0.58660 0.60103 0.44999 0.03988  -0.09588 0.00496  155 ASN A CA  
1076 C C   . ASN A 148 ? 0.58908 0.59913 0.41626 0.04614  -0.08176 0.01094  155 ASN A C   
1077 O O   . ASN A 148 ? 0.64495 0.66418 0.43372 0.05014  -0.08865 0.00498  155 ASN A O   
1078 C CB  . ASN A 148 ? 0.64699 0.67016 0.51976 0.04816  -0.10394 0.02600  155 ASN A CB  
1079 C CG  . ASN A 148 ? 0.80764 0.84514 0.70613 0.04551  -0.12134 0.01922  155 ASN A CG  
1080 O OD1 . ASN A 148 ? 0.65817 0.70467 0.55893 0.03697  -0.13177 -0.00031 155 ASN A OD1 
1081 N ND2 . ASN A 148 ? 0.65182 0.69091 0.57178 0.05301  -0.12329 0.03576  155 ASN A ND2 
1082 N N   . ASP A 149 ? 0.58061 0.57895 0.41919 0.04692  -0.06202 0.02250  156 ASP A N   
1083 C CA  . ASP A 149 ? 0.75982 0.75687 0.56946 0.05369  -0.04464 0.03304  156 ASP A CA  
1084 C C   . ASP A 149 ? 0.87031 0.86105 0.67326 0.05160  -0.03061 0.01571  156 ASP A C   
1085 O O   . ASP A 149 ? 0.74160 0.73209 0.52956 0.05723  -0.01121 0.02492  156 ASP A O   
1086 C CB  . ASP A 149 ? 0.76723 0.75790 0.59739 0.05552  -0.03016 0.05987  156 ASP A CB  
1087 C CG  . ASP A 149 ? 0.91612 0.90795 0.75262 0.06038  -0.04138 0.07876  156 ASP A CG  
1088 O OD1 . ASP A 149 ? 0.94136 0.94521 0.75943 0.06521  -0.05941 0.07506  156 ASP A OD1 
1089 O OD2 . ASP A 149 ? 0.92255 0.90323 0.78456 0.05941  -0.03253 0.09699  156 ASP A OD2 
1090 N N   . ASP A 150 ? 0.67362 0.65921 0.48874 0.04465  -0.03836 -0.00757 157 ASP A N   
1091 C CA  . ASP A 150 ? 0.67680 0.65306 0.49040 0.04454  -0.02452 -0.02307 157 ASP A CA  
1092 C C   . ASP A 150 ? 0.70607 0.67543 0.51366 0.03854  -0.03817 -0.05007 157 ASP A C   
1093 O O   . ASP A 150 ? 0.74391 0.71966 0.55129 0.03313  -0.05815 -0.05586 157 ASP A O   
1094 C CB  . ASP A 150 ? 0.72601 0.69809 0.58234 0.04108  -0.01215 -0.01499 157 ASP A CB  
1095 C CG  . ASP A 150 ? 0.82598 0.79627 0.67947 0.04709  0.01009  -0.01605 157 ASP A CG  
1096 O OD1 . ASP A 150 ? 0.83392 0.79988 0.65405 0.05336  0.01577  -0.03059 157 ASP A OD1 
1097 O OD2 . ASP A 150 ? 0.82413 0.79836 0.70967 0.04572  0.02177  -0.00320 157 ASP A OD2 
1098 N N   . GLU A 151 ? 0.72686 0.68317 0.53252 0.03958  -0.02657 -0.06591 158 GLU A N   
1099 C CA  . GLU A 151 ? 0.70324 0.64649 0.50656 0.03288  -0.03649 -0.09158 158 GLU A CA  
1100 C C   . GLU A 151 ? 0.65095 0.58779 0.49959 0.02476  -0.03949 -0.09139 158 GLU A C   
1101 O O   . GLU A 151 ? 0.64279 0.58576 0.52081 0.02497  -0.03442 -0.07418 158 GLU A O   
1102 C CB  . GLU A 151 ? 0.79264 0.72002 0.56868 0.04012  -0.02123 -0.10966 158 GLU A CB  
1103 C CG  . GLU A 151 ? 0.79284 0.72148 0.51488 0.04406  -0.02671 -0.12417 158 GLU A CG  
1104 C CD  . GLU A 151 ? 1.24060 1.15124 0.93317 0.05365  -0.00799 -0.14323 158 GLU A CD  
1105 O OE1 . GLU A 151 ? 1.25584 1.14371 0.95384 0.04924  -0.00932 -0.16673 158 GLU A OE1 
1106 O OE2 . GLU A 151 ? 1.36312 1.28124 1.02762 0.06626  0.00964  -0.13411 158 GLU A OE2 
1107 N N   . GLN A 152 ? 0.66973 0.59352 0.52276 0.01694  -0.04794 -0.11096 159 GLN A N   
1108 C CA  . GLN A 152 ? 0.61515 0.53171 0.50683 0.00999  -0.04928 -0.11009 159 GLN A CA  
1109 C C   . GLN A 152 ? 0.69594 0.59833 0.60004 0.01745  -0.03039 -0.10937 159 GLN A C   
1110 O O   . GLN A 152 ? 0.80516 0.69204 0.68914 0.02374  -0.01991 -0.12316 159 GLN A O   
1111 C CB  . GLN A 152 ? 0.68204 0.58952 0.57678 -0.00217 -0.06378 -0.12865 159 GLN A CB  
1112 C CG  . GLN A 152 ? 0.66371 0.56881 0.59737 -0.01042 -0.06685 -0.12341 159 GLN A CG  
1113 C CD  . GLN A 152 ? 0.71870 0.62717 0.66099 -0.02472 -0.08402 -0.13464 159 GLN A CD  
1114 O OE1 . GLN A 152 ? 0.79007 0.71955 0.72671 -0.02811 -0.09848 -0.13301 159 GLN A OE1 
1115 N NE2 . GLN A 152 ? 0.71324 0.60222 0.67230 -0.03306 -0.08221 -0.14444 159 GLN A NE2 
1116 N N   . TYR A 153 ? 0.64865 0.55734 0.58548 0.01781  -0.02635 -0.09387 160 TYR A N   
1117 C CA  . TYR A 153 ? 0.62465 0.52729 0.57839 0.02601  -0.01050 -0.08922 160 TYR A CA  
1118 C C   . TYR A 153 ? 0.65032 0.54765 0.63511 0.02136  -0.01450 -0.08564 160 TYR A C   
1119 O O   . TYR A 153 ? 0.65313 0.55760 0.65009 0.01253  -0.02684 -0.08126 160 TYR A O   
1120 C CB  . TYR A 153 ? 0.65297 0.57412 0.61650 0.03243  -0.00022 -0.07078 160 TYR A CB  
1121 C CG  . TYR A 153 ? 0.75942 0.68542 0.69374 0.04014  0.01078  -0.07018 160 TYR A CG  
1122 C CD1 . TYR A 153 ? 0.77869 0.71571 0.69461 0.03771  0.00417  -0.06241 160 TYR A CD1 
1123 C CD2 . TYR A 153 ? 0.71246 0.63199 0.63631 0.05154  0.02902  -0.07630 160 TYR A CD2 
1124 C CE1 . TYR A 153 ? 0.81092 0.75321 0.69669 0.04561  0.01538  -0.05895 160 TYR A CE1 
1125 C CE2 . TYR A 153 ? 0.78808 0.71359 0.68194 0.05966  0.04148  -0.07500 160 TYR A CE2 
1126 C CZ  . TYR A 153 ? 0.84420 0.78136 0.71776 0.05620  0.03445  -0.06563 160 TYR A CZ  
1127 O OH  . TYR A 153 ? 0.96341 0.90730 0.80389 0.06507  0.04790  -0.06153 160 TYR A OH  
1128 N N   . ALA A 154 ? 0.66367 0.54962 0.66078 0.02923  -0.00268 -0.08599 161 ALA A N   
1129 C CA  . ALA A 154 ? 0.61247 0.49314 0.63671 0.02802  -0.00416 -0.07935 161 ALA A CA  
1130 C C   . ALA A 154 ? 0.66438 0.56062 0.71102 0.03780  0.00476  -0.06354 161 ALA A C   
1131 O O   . ALA A 154 ? 0.67251 0.56669 0.71961 0.04963  0.01887  -0.06397 161 ALA A O   
1132 C CB  . ALA A 154 ? 0.52747 0.37785 0.54926 0.02885  0.00019  -0.09297 161 ALA A CB  
1133 N N   . TRP A 155 ? 0.53051 0.44397 0.59602 0.03304  -0.00365 -0.05057 162 TRP A N   
1134 C CA  . TRP A 155 ? 0.48262 0.41498 0.57239 0.03918  -0.00033 -0.03617 162 TRP A CA  
1135 C C   . TRP A 155 ? 0.60002 0.52712 0.70627 0.04171  -0.00324 -0.02990 162 TRP A C   
1136 O O   . TRP A 155 ? 0.57017 0.48753 0.67278 0.03410  -0.01113 -0.03195 162 TRP A O   
1137 C CB  . TRP A 155 ? 0.45254 0.40630 0.54875 0.03136  -0.00905 -0.02799 162 TRP A CB  
1138 C CG  . TRP A 155 ? 0.56251 0.53901 0.68453 0.03359  -0.00946 -0.01545 162 TRP A CG  
1139 C CD1 . TRP A 155 ? 0.53512 0.52956 0.66968 0.03552  -0.00248 -0.00857 162 TRP A CD1 
1140 C CD2 . TRP A 155 ? 0.55840 0.54499 0.69703 0.03269  -0.01851 -0.00824 162 TRP A CD2 
1141 N NE1 . TRP A 155 ? 0.46339 0.47928 0.62458 0.03448  -0.00835 0.00096  162 TRP A NE1 
1142 C CE2 . TRP A 155 ? 0.42115 0.43268 0.58242 0.03349  -0.01895 0.00085  162 TRP A CE2 
1143 C CE3 . TRP A 155 ? 0.52912 0.50771 0.66523 0.03110  -0.02596 -0.00777 162 TRP A CE3 
1144 C CZ2 . TRP A 155 ? 0.46511 0.49431 0.64368 0.03296  -0.02918 0.00827  162 TRP A CZ2 
1145 C CZ3 . TRP A 155 ? 0.52913 0.52409 0.67922 0.03217  -0.03378 0.00146  162 TRP A CZ3 
1146 C CH2 . TRP A 155 ? 0.48920 0.50950 0.65895 0.03318  -0.03663 0.00837  162 TRP A CH2 
1147 N N   . GLU A 156 ? 0.46372 0.39967 0.58939 0.05314  0.00368  -0.02026 163 GLU A N   
1148 C CA  . GLU A 156 ? 0.47233 0.40326 0.61223 0.05869  0.00189  -0.01105 163 GLU A CA  
1149 C C   . GLU A 156 ? 0.53723 0.49567 0.70270 0.06865  0.00226  0.00409  163 GLU A C   
1150 O O   . GLU A 156 ? 0.44218 0.41231 0.61858 0.07751  0.01226  0.00562  163 GLU A O   
1151 C CB  . GLU A 156 ? 0.45263 0.35055 0.58765 0.06648  0.01267  -0.01814 163 GLU A CB  
1152 C CG  . GLU A 156 ? 0.64373 0.52973 0.79023 0.06998  0.01086  -0.00702 163 GLU A CG  
1153 C CD  . GLU A 156 ? 0.85915 0.70450 0.99959 0.07247  0.02029  -0.01662 163 GLU A CD  
1154 O OE1 . GLU A 156 ? 0.94148 0.77212 1.08483 0.08625  0.03354  -0.02127 163 GLU A OE1 
1155 O OE2 . GLU A 156 ? 0.77141 0.59920 0.90556 0.06032  0.01519  -0.02023 163 GLU A OE2 
1156 N N   . SER A 157 ? 0.58110 0.55229 0.75623 0.06760  -0.00850 0.01560  164 SER A N   
1157 C CA  . SER A 157 ? 0.58001 0.57923 0.78025 0.07775  -0.01120 0.03055  164 SER A CA  
1158 C C   . SER A 157 ? 0.61447 0.61382 0.81641 0.08147  -0.01952 0.04318  164 SER A C   
1159 O O   . SER A 157 ? 0.55718 0.55028 0.74307 0.07114  -0.02772 0.04127  164 SER A O   
1160 C CB  . SER A 157 ? 0.49533 0.52803 0.70674 0.06904  -0.02051 0.03194  164 SER A CB  
1161 O OG  . SER A 157 ? 0.52387 0.58807 0.76321 0.07775  -0.02503 0.04560  164 SER A OG  
1162 N N   . SER A 158 ? 0.54234 0.54991 0.76391 0.09789  -0.01604 0.05762  165 SER A N   
1163 C CA  . SER A 158 ? 0.47573 0.49351 0.70154 0.10462  -0.02526 0.07511  165 SER A CA  
1164 C C   . SER A 158 ? 0.56785 0.63206 0.81283 0.10704  -0.03942 0.08545  165 SER A C   
1165 O O   . SER A 158 ? 0.55025 0.63123 0.80644 0.11948  -0.04576 0.10326  165 SER A O   
1166 C CB  . SER A 158 ? 0.49779 0.49160 0.73295 0.12286  -0.01306 0.08705  165 SER A CB  
1167 O OG  . SER A 158 ? 0.65695 0.60603 0.87572 0.11784  -0.00176 0.07567  165 SER A OG  
1168 N N   . ALA A 159 ? 0.53715 0.62242 0.78682 0.09484  -0.04518 0.07512  166 ALA A N   
1169 C CA  . ALA A 159 ? 0.60044 0.73061 0.87451 0.09364  -0.05835 0.08146  166 ALA A CA  
1170 C C   . ALA A 159 ? 0.46373 0.61159 0.77119 0.11281  -0.04903 0.09460  166 ALA A C   
1171 O O   . ALA A 159 ? 0.67160 0.79734 0.98174 0.12152  -0.02985 0.09065  166 ALA A O   
1172 C CB  . ALA A 159 ? 0.44639 0.59484 0.70947 0.08941  -0.07819 0.08743  166 ALA A CB  
1173 N N   . GLY A 160 ? 0.39314 0.58142 0.72614 0.12075  -0.06188 0.10951  167 GLY A N   
1174 C CA  . GLY A 160 ? 0.41706 0.62691 0.78723 0.14025  -0.05207 0.12263  167 GLY A CA  
1175 C C   . GLY A 160 ? 0.41498 0.64767 0.81247 0.13504  -0.04300 0.11630  167 GLY A C   
1176 O O   . GLY A 160 ? 0.39113 0.64388 0.82203 0.15208  -0.03129 0.12652  167 GLY A O   
1177 N N   . GLY A 161 ? 0.45254 0.68232 0.83783 0.11311  -0.04619 0.10123  168 GLY A N   
1178 C CA  . GLY A 161 ? 0.49029 0.74480 0.90249 0.10514  -0.03882 0.09828  168 GLY A CA  
1179 C C   . GLY A 161 ? 0.54141 0.76467 0.93700 0.10474  -0.01537 0.08741  168 GLY A C   
1180 O O   . GLY A 161 ? 0.52209 0.76399 0.93646 0.09760  -0.00679 0.08662  168 GLY A O   
1181 N N   . SER A 162 ? 0.42083 0.59846 0.78175 0.11119  -0.00516 0.07933  169 SER A N   
1182 C CA  . SER A 162 ? 0.39549 0.54471 0.73706 0.11271  0.01572  0.06786  169 SER A CA  
1183 C C   . SER A 162 ? 0.48363 0.58872 0.78105 0.10295  0.01294  0.05344  169 SER A C   
1184 O O   . SER A 162 ? 0.50386 0.59577 0.78773 0.10008  0.00036  0.05411  169 SER A O   
1185 C CB  . SER A 162 ? 0.49906 0.64040 0.85214 0.13710  0.03721  0.07171  169 SER A CB  
1186 O OG  . SER A 162 ? 0.56463 0.67319 0.90225 0.14826  0.03671  0.07187  169 SER A OG  
1187 N N   . PHE A 163 ? 0.46224 0.54762 0.73787 0.09821  0.02518  0.04152  170 PHE A N   
1188 C CA  . PHE A 163 ? 0.49099 0.53772 0.72784 0.09044  0.02392  0.02724  170 PHE A CA  
1189 C C   . PHE A 163 ? 0.57602 0.60063 0.79343 0.09820  0.04339  0.01607  170 PHE A C   
1190 O O   . PHE A 163 ? 0.47062 0.51206 0.70075 0.10635  0.05836  0.01939  170 PHE A O   
1191 C CB  . PHE A 163 ? 0.45835 0.50760 0.68125 0.07056  0.00999  0.02252  170 PHE A CB  
1192 C CG  . PHE A 163 ? 0.61040 0.67427 0.83696 0.06328  0.01649  0.02266  170 PHE A CG  
1193 C CD1 . PHE A 163 ? 0.51235 0.61079 0.77128 0.05811  0.01280  0.03306  170 PHE A CD1 
1194 C CD2 . PHE A 163 ? 0.57690 0.62070 0.77487 0.06063  0.02543  0.01335  170 PHE A CD2 
1195 C CE1 . PHE A 163 ? 0.59503 0.70491 0.86007 0.04999  0.02045  0.03571  170 PHE A CE1 
1196 C CE2 . PHE A 163 ? 0.51104 0.56732 0.71073 0.05480  0.03272  0.01714  170 PHE A CE2 
1197 C CZ  . PHE A 163 ? 0.57279 0.66066 0.80712 0.04916  0.03140  0.02909  170 PHE A CZ  
1198 N N   . THR A 164 ? 0.53969 0.52792 0.72611 0.09541  0.04326  0.00235  171 THR A N   
1199 C CA  . THR A 164 ? 0.46278 0.42644 0.62283 0.10091  0.05827  -0.01264 171 THR A CA  
1200 C C   . THR A 164 ? 0.53606 0.48912 0.66442 0.08530  0.05032  -0.02379 171 THR A C   
1201 O O   . THR A 164 ? 0.55201 0.50385 0.67641 0.07205  0.03410  -0.02332 171 THR A O   
1202 C CB  . THR A 164 ? 0.56034 0.48761 0.71167 0.11124  0.06493  -0.02207 171 THR A CB  
1203 O OG1 . THR A 164 ? 0.64290 0.55020 0.78319 0.09846  0.04997  -0.02600 171 THR A OG1 
1204 C CG2 . THR A 164 ? 0.49932 0.43557 0.68324 0.12978  0.07292  -0.00834 171 THR A CG2 
1205 N N   . VAL A 165 ? 0.50699 0.45430 0.61216 0.08862  0.06249  -0.03297 172 VAL A N   
1206 C CA  . VAL A 165 ? 0.55803 0.49462 0.62942 0.07738  0.05569  -0.04362 172 VAL A CA  
1207 C C   . VAL A 165 ? 0.57653 0.48662 0.61508 0.08524  0.06699  -0.06272 172 VAL A C   
1208 O O   . VAL A 165 ? 0.62001 0.53015 0.65767 0.10019  0.08609  -0.06471 172 VAL A O   
1209 C CB  . VAL A 165 ? 0.60903 0.57070 0.68060 0.07154  0.05680  -0.03265 172 VAL A CB  
1210 C CG1 . VAL A 165 ? 0.48992 0.44075 0.52436 0.06379  0.05068  -0.04162 172 VAL A CG1 
1211 C CG2 . VAL A 165 ? 0.45229 0.43489 0.55396 0.06153  0.04357  -0.01844 172 VAL A CG2 
1212 N N   . ARG A 166 ? 0.65241 0.54098 0.66487 0.07525  0.05515  -0.07781 173 ARG A N   
1213 C CA  . ARG A 166 ? 0.68767 0.54977 0.66505 0.07928  0.06150  -0.10009 173 ARG A CA  
1214 C C   . ARG A 166 ? 0.75155 0.61073 0.70029 0.06475  0.04451  -0.11023 173 ARG A C   
1215 O O   . ARG A 166 ? 0.69006 0.56080 0.65101 0.05254  0.02844  -0.10142 173 ARG A O   
1216 C CB  . ARG A 166 ? 0.74087 0.57011 0.72543 0.08395  0.06495  -0.11239 173 ARG A CB  
1217 C CG  . ARG A 166 ? 0.78412 0.59756 0.77332 0.06765  0.04631  -0.11746 173 ARG A CG  
1218 C CD  . ARG A 166 ? 0.80777 0.59069 0.81466 0.07247  0.05161  -0.12101 173 ARG A CD  
1219 N NE  . ARG A 166 ? 0.91513 0.71439 0.95788 0.08114  0.05519  -0.09776 173 ARG A NE  
1220 C CZ  . ARG A 166 ? 1.15981 0.94060 1.22228 0.09358  0.06508  -0.09292 173 ARG A CZ  
1221 N NH1 . ARG A 166 ? 1.13844 0.87846 1.19015 0.09883  0.07444  -0.11060 173 ARG A NH1 
1222 N NH2 . ARG A 166 ? 1.01538 0.81836 1.10892 0.10129  0.06495  -0.06998 173 ARG A NH2 
1223 N N   . THR A 167 ? 0.69669 0.54198 0.60654 0.06734  0.04810  -0.12922 174 THR A N   
1224 C CA  . THR A 167 ? 0.82163 0.66389 0.70448 0.05411  0.02955  -0.14165 174 THR A CA  
1225 C C   . THR A 167 ? 0.83242 0.65108 0.72699 0.04234  0.01673  -0.15537 174 THR A C   
1226 O O   . THR A 167 ? 1.04783 0.83762 0.94406 0.04687  0.02543  -0.16927 174 THR A O   
1227 C CB  . THR A 167 ? 0.84559 0.68141 0.67959 0.06038  0.03549  -0.15936 174 THR A CB  
1228 O OG1 . THR A 167 ? 0.90763 0.76739 0.73201 0.07068  0.04925  -0.14249 174 THR A OG1 
1229 C CG2 . THR A 167 ? 0.92566 0.76281 0.73318 0.04655  0.01278  -0.17217 174 THR A CG2 
1230 N N   . ASP A 168 ? 0.78528 0.61565 0.69068 0.02772  -0.00235 -0.15022 175 ASP A N   
1231 C CA  . ASP A 168 ? 0.84054 0.65335 0.76171 0.01449  -0.01375 -0.15984 175 ASP A CA  
1232 C C   . ASP A 168 ? 1.00847 0.80566 0.89977 0.00520  -0.02431 -0.18664 175 ASP A C   
1233 O O   . ASP A 168 ? 1.01895 0.83380 0.88381 0.00236  -0.03500 -0.19088 175 ASP A O   
1234 C CB  . ASP A 168 ? 0.75258 0.58745 0.69965 0.00364  -0.02782 -0.14329 175 ASP A CB  
1235 C CG  . ASP A 168 ? 0.88455 0.70430 0.85454 -0.00906 -0.03509 -0.14771 175 ASP A CG  
1236 O OD1 . ASP A 168 ? 1.16432 0.95932 1.14733 -0.00532 -0.02457 -0.14932 175 ASP A OD1 
1237 O OD2 . ASP A 168 ? 0.97807 0.81145 0.95514 -0.02209 -0.05025 -0.14782 175 ASP A OD2 
1238 N N   . THR A 169 ? 1.15413 0.91765 1.04985 0.00041  -0.02194 -0.20448 176 THR A N   
1239 C CA  . THR A 169 ? 1.16885 0.91280 1.03981 -0.01136 -0.03318 -0.23400 176 THR A CA  
1240 C C   . THR A 169 ? 1.20655 0.95078 1.10349 -0.03343 -0.05172 -0.23714 176 THR A C   
1241 O O   . THR A 169 ? 1.33093 1.06341 1.21362 -0.04750 -0.06510 -0.26175 176 THR A O   
1242 C CB  . THR A 169 ? 1.39199 1.09249 1.24964 -0.00277 -0.01690 -0.25571 176 THR A CB  
1243 O OG1 . THR A 169 ? 1.31045 0.98881 1.20668 -0.00115 -0.00664 -0.24452 176 THR A OG1 
1244 C CG2 . THR A 169 ? 1.33314 1.03793 1.16311 0.01969  0.00271  -0.25429 176 THR A CG2 
1245 N N   . GLY A 170 ? 1.16084 0.92026 1.09541 -0.03716 -0.05279 -0.21330 177 GLY A N   
1246 C CA  . GLY A 170 ? 1.21160 0.97290 1.17588 -0.05665 -0.06563 -0.21246 177 GLY A CA  
1247 C C   . GLY A 170 ? 1.17354 0.96992 1.13520 -0.06892 -0.08708 -0.21370 177 GLY A C   
1248 O O   . GLY A 170 ? 1.13046 0.94226 1.06004 -0.06510 -0.09540 -0.22230 177 GLY A O   
1249 N N   . GLU A 171 ? 1.07882 0.88956 1.07540 -0.08256 -0.09523 -0.20319 178 GLU A N   
1250 C CA  . GLU A 171 ? 1.05525 0.90189 1.05926 -0.09429 -0.11539 -0.20273 178 GLU A CA  
1251 C C   . GLU A 171 ? 0.83569 0.71507 0.82372 -0.07995 -0.11817 -0.18696 178 GLU A C   
1252 O O   . GLU A 171 ? 0.79833 0.68589 0.79895 -0.06925 -0.10752 -0.16544 178 GLU A O   
1253 C CB  . GLU A 171 ? 1.09671 0.95489 1.14552 -0.10759 -0.11738 -0.18914 178 GLU A CB  
1254 C CG  . GLU A 171 ? 1.21485 1.10211 1.28076 -0.12581 -0.13836 -0.19659 178 GLU A CG  
1255 C CD  . GLU A 171 ? 1.49260 1.36122 1.54622 -0.14231 -0.15120 -0.22717 178 GLU A CD  
1256 O OE1 . GLU A 171 ? 1.29890 1.12664 1.35793 -0.14984 -0.14184 -0.23925 178 GLU A OE1 
1257 O OE2 . GLU A 171 ? 1.54605 1.44018 1.58416 -0.14750 -0.17131 -0.23939 178 GLU A OE2 
1258 N N   . PRO A 172 ? 0.92967 0.82713 0.88967 -0.07933 -0.13241 -0.19650 179 PRO A N   
1259 C CA  . PRO A 172 ? 0.81620 0.74179 0.76257 -0.06544 -0.13411 -0.17858 179 PRO A CA  
1260 C C   . PRO A 172 ? 0.77426 0.72798 0.75591 -0.06704 -0.13887 -0.15777 179 PRO A C   
1261 O O   . PRO A 172 ? 0.83456 0.80355 0.84282 -0.08056 -0.15083 -0.16041 179 PRO A O   
1262 C CB  . PRO A 172 ? 0.64296 0.58324 0.55467 -0.06728 -0.15186 -0.19354 179 PRO A CB  
1263 C CG  . PRO A 172 ? 0.74856 0.65829 0.64254 -0.07710 -0.15287 -0.22318 179 PRO A CG  
1264 C CD  . PRO A 172 ? 0.89757 0.78775 0.83319 -0.09034 -0.14714 -0.22456 179 PRO A CD  
1265 N N   . MET A 173 ? 0.71284 0.67334 0.69590 -0.05325 -0.12849 -0.13766 180 MET A N   
1266 C CA  . MET A 173 ? 0.74705 0.72978 0.75920 -0.05168 -0.13010 -0.11932 180 MET A CA  
1267 C C   . MET A 173 ? 0.68838 0.70113 0.69521 -0.04651 -0.14401 -0.11133 180 MET A C   
1268 O O   . MET A 173 ? 0.80595 0.84090 0.84017 -0.04805 -0.14995 -0.10190 180 MET A O   
1269 C CB  . MET A 173 ? 0.77069 0.74417 0.78806 -0.04051 -0.11355 -0.10364 180 MET A CB  
1270 C CG  . MET A 173 ? 0.86087 0.82079 0.90243 -0.04494 -0.10328 -0.10062 180 MET A CG  
1271 S SD  . MET A 173 ? 1.07353 1.02807 1.11682 -0.03188 -0.08845 -0.08434 180 MET A SD  
1272 C CE  . MET A 173 ? 0.77485 0.72373 0.78587 -0.02196 -0.08447 -0.08673 180 MET A CE  
1273 N N   . GLY A 174 ? 0.56211 0.57665 0.53427 -0.03870 -0.14804 -0.11325 181 GLY A N   
1274 C CA  . GLY A 174 ? 0.70184 0.74255 0.66685 -0.03005 -0.15924 -0.10050 181 GLY A CA  
1275 C C   . GLY A 174 ? 0.57371 0.60958 0.53574 -0.01565 -0.14581 -0.08012 181 GLY A C   
1276 O O   . GLY A 174 ? 0.58944 0.62250 0.52182 -0.00611 -0.14235 -0.07376 181 GLY A O   
1277 N N   . ARG A 175 ? 0.54149 0.57565 0.53353 -0.01471 -0.13756 -0.07013 182 ARG A N   
1278 C CA  . ARG A 175 ? 0.56705 0.59298 0.56076 -0.00425 -0.12515 -0.05403 182 ARG A CA  
1279 C C   . ARG A 175 ? 0.41176 0.43235 0.43507 -0.00714 -0.11698 -0.05148 182 ARG A C   
1280 O O   . ARG A 175 ? 0.54154 0.57470 0.58748 -0.01245 -0.12258 -0.05384 182 ARG A O   
1281 C CB  . ARG A 175 ? 0.47539 0.51674 0.46647 0.00650  -0.13197 -0.03821 182 ARG A CB  
1282 C CG  . ARG A 175 ? 0.56447 0.59180 0.55261 0.01576  -0.11889 -0.02257 182 ARG A CG  
1283 C CD  . ARG A 175 ? 0.59487 0.63179 0.59384 0.02617  -0.12349 -0.00621 182 ARG A CD  
1284 N NE  . ARG A 175 ? 0.48537 0.53370 0.51522 0.02516  -0.12784 -0.00831 182 ARG A NE  
1285 C CZ  . ARG A 175 ? 0.48256 0.55593 0.52429 0.02725  -0.14135 -0.00761 182 ARG A CZ  
1286 N NH1 . ARG A 175 ? 0.51927 0.60963 0.54329 0.03003  -0.15493 -0.00551 182 ARG A NH1 
1287 N NH2 . ARG A 175 ? 0.51568 0.60016 0.58779 0.02706  -0.14127 -0.00867 182 ARG A NH2 
1288 N N   . GLY A 176 ? 0.44748 0.45216 0.47061 -0.00380 -0.10386 -0.04633 183 GLY A N   
1289 C CA  . GLY A 176 ? 0.47697 0.47812 0.52243 -0.00519 -0.09747 -0.04361 183 GLY A CA  
1290 C C   . GLY A 176 ? 0.53140 0.51682 0.57586 -0.00776 -0.08711 -0.04724 183 GLY A C   
1291 O O   . GLY A 176 ? 0.66463 0.64085 0.69293 -0.00643 -0.08225 -0.05034 183 GLY A O   
1292 N N   . THR A 177 ? 0.53312 0.51724 0.59451 -0.00993 -0.08321 -0.04601 184 THR A N   
1293 C CA  . THR A 177 ? 0.55285 0.52577 0.61685 -0.01035 -0.07467 -0.04610 184 THR A CA  
1294 C C   . THR A 177 ? 0.60361 0.57633 0.68120 -0.01556 -0.07380 -0.04789 184 THR A C   
1295 O O   . THR A 177 ? 0.56208 0.54559 0.65089 -0.01706 -0.07644 -0.04554 184 THR A O   
1296 C CB  . THR A 177 ? 0.52497 0.49747 0.59337 -0.00593 -0.07031 -0.03843 184 THR A CB  
1297 O OG1 . THR A 177 ? 0.68019 0.65085 0.73834 -0.00236 -0.06841 -0.03434 184 THR A OG1 
1298 C CG2 . THR A 177 ? 0.55058 0.51821 0.62531 -0.00582 -0.06423 -0.03722 184 THR A CG2 
1299 N N   . LYS A 178 ? 0.44366 0.40366 0.52075 -0.01722 -0.06844 -0.05079 185 LYS A N   
1300 C CA  . LYS A 178 ? 0.51546 0.47083 0.60494 -0.02165 -0.06526 -0.04920 185 LYS A CA  
1301 C C   . LYS A 178 ? 0.53645 0.48484 0.62781 -0.01558 -0.05794 -0.04215 185 LYS A C   
1302 O O   . LYS A 178 ? 0.50556 0.44379 0.59148 -0.01121 -0.05334 -0.04407 185 LYS A O   
1303 C CB  . LYS A 178 ? 0.54257 0.48570 0.63218 -0.02957 -0.06646 -0.05901 185 LYS A CB  
1304 C CG  . LYS A 178 ? 0.65601 0.58808 0.75982 -0.03478 -0.06079 -0.05551 185 LYS A CG  
1305 C CD  . LYS A 178 ? 0.82148 0.74909 0.93406 -0.04794 -0.06560 -0.06512 185 LYS A CD  
1306 C CE  . LYS A 178 ? 0.77686 0.69387 0.87240 -0.05011 -0.07124 -0.08154 185 LYS A CE  
1307 N NZ  . LYS A 178 ? 0.88473 0.77653 0.98469 -0.05982 -0.06936 -0.09293 185 LYS A NZ  
1308 N N   . VAL A 179 ? 0.50027 0.45668 0.59867 -0.01411 -0.05690 -0.03387 186 VAL A N   
1309 C CA  . VAL A 179 ? 0.46384 0.41894 0.56439 -0.00811 -0.05288 -0.02568 186 VAL A CA  
1310 C C   . VAL A 179 ? 0.55113 0.49777 0.65858 -0.00974 -0.04781 -0.01909 186 VAL A C   
1311 O O   . VAL A 179 ? 0.43353 0.38668 0.54509 -0.01405 -0.04732 -0.01536 186 VAL A O   
1312 C CB  . VAL A 179 ? 0.56002 0.52983 0.65903 -0.00502 -0.05653 -0.02162 186 VAL A CB  
1313 C CG1 . VAL A 179 ? 0.41213 0.38548 0.51340 0.00073  -0.05556 -0.01327 186 VAL A CG1 
1314 C CG2 . VAL A 179 ? 0.38553 0.35928 0.48088 -0.00476 -0.06037 -0.02668 186 VAL A CG2 
1315 N N   . ILE A 180 ? 0.49314 0.42490 0.60329 -0.00545 -0.04239 -0.01628 187 ILE A N   
1316 C CA  . ILE A 180 ? 0.48509 0.40239 0.60308 -0.00618 -0.03597 -0.00804 187 ILE A CA  
1317 C C   . ILE A 180 ? 0.53518 0.45830 0.65456 0.00466  -0.03388 0.00686  187 ILE A C   
1318 O O   . ILE A 180 ? 0.41499 0.33610 0.53646 0.01351  -0.03245 0.00824  187 ILE A O   
1319 C CB  . ILE A 180 ? 0.50696 0.39771 0.62749 -0.00856 -0.03102 -0.01697 187 ILE A CB  
1320 C CG1 . ILE A 180 ? 0.56031 0.45046 0.67586 -0.01909 -0.03679 -0.03345 187 ILE A CG1 
1321 C CG2 . ILE A 180 ? 0.44823 0.31905 0.57998 -0.01102 -0.02353 -0.00762 187 ILE A CG2 
1322 C CD1 . ILE A 180 ? 0.62243 0.48663 0.73388 -0.02141 -0.03374 -0.04739 187 ILE A CD1 
1323 N N   . LEU A 181 ? 0.50516 0.43847 0.62334 0.00482  -0.03360 0.01871  188 LEU A N   
1324 C CA  . LEU A 181 ? 0.53387 0.47693 0.64968 0.01530  -0.03409 0.03412  188 LEU A CA  
1325 C C   . LEU A 181 ? 0.56657 0.49014 0.68999 0.01917  -0.02495 0.04921  188 LEU A C   
1326 O O   . LEU A 181 ? 0.55552 0.47233 0.68093 0.01261  -0.01905 0.05609  188 LEU A O   
1327 C CB  . LEU A 181 ? 0.45511 0.42039 0.55897 0.01492  -0.03876 0.03804  188 LEU A CB  
1328 C CG  . LEU A 181 ? 0.62417 0.60383 0.72125 0.01101  -0.04655 0.02352  188 LEU A CG  
1329 C CD1 . LEU A 181 ? 0.44114 0.43732 0.52447 0.01224  -0.04858 0.02641  188 LEU A CD1 
1330 C CD2 . LEU A 181 ? 0.41577 0.40207 0.51554 0.01508  -0.05333 0.01873  188 LEU A CD2 
1331 N N   . HIS A 182 ? 0.53387 0.44851 0.66414 0.03031  -0.02255 0.05580  189 HIS A N   
1332 C CA  . HIS A 182 ? 0.58495 0.47983 0.72311 0.03777  -0.01366 0.07388  189 HIS A CA  
1333 C C   . HIS A 182 ? 0.55472 0.47275 0.68473 0.04778  -0.01798 0.09464  189 HIS A C   
1334 O O   . HIS A 182 ? 0.61963 0.55553 0.75072 0.05960  -0.02475 0.10049  189 HIS A O   
1335 C CB  . HIS A 182 ? 0.54255 0.41692 0.69240 0.04811  -0.00798 0.07161  189 HIS A CB  
1336 C CG  . HIS A 182 ? 0.58541 0.44034 0.73600 0.03955  -0.00514 0.04839  189 HIS A CG  
1337 N ND1 . HIS A 182 ? 0.65913 0.47852 0.81520 0.03248  0.00320  0.04132  189 HIS A ND1 
1338 C CD2 . HIS A 182 ? 0.69063 0.55687 0.83526 0.03652  -0.00998 0.03077  189 HIS A CD2 
1339 C CE1 . HIS A 182 ? 0.55495 0.36655 0.70543 0.02602  0.00190  0.01872  189 HIS A CE1 
1340 N NE2 . HIS A 182 ? 0.74608 0.58601 0.88892 0.02919  -0.00522 0.01361  189 HIS A NE2 
1341 N N   . LEU A 183 ? 0.59977 0.52047 0.72156 0.04293  -0.01425 0.10592  190 LEU A N   
1342 C CA  . LEU A 183 ? 0.60967 0.55690 0.71459 0.05072  -0.01961 0.12160  190 LEU A CA  
1343 C C   . LEU A 183 ? 0.72039 0.66559 0.82809 0.06734  -0.01815 0.14670  190 LEU A C   
1344 O O   . LEU A 183 ? 0.76935 0.68522 0.89184 0.07136  -0.00736 0.15796  190 LEU A O   
1345 C CB  . LEU A 183 ? 0.55921 0.50990 0.65361 0.04224  -0.01236 0.12785  190 LEU A CB  
1346 C CG  . LEU A 183 ? 0.61617 0.57654 0.70763 0.02918  -0.01488 0.10588  190 LEU A CG  
1347 C CD1 . LEU A 183 ? 0.58103 0.54981 0.66496 0.02369  -0.00555 0.11473  190 LEU A CD1 
1348 C CD2 . LEU A 183 ? 0.52390 0.50752 0.60279 0.03216  -0.02879 0.09072  190 LEU A CD2 
1349 N N   . LYS A 184 ? 0.66641 0.64289 0.76006 0.07735  -0.03001 0.15506  191 LYS A N   
1350 C CA  . LYS A 184 ? 0.75446 0.73723 0.84755 0.09488  -0.03127 0.18244  191 LYS A CA  
1351 C C   . LYS A 184 ? 0.77819 0.74612 0.86155 0.09629  -0.01812 0.20710  191 LYS A C   
1352 O O   . LYS A 184 ? 0.82526 0.79083 0.89803 0.08400  -0.01099 0.20278  191 LYS A O   
1353 C CB  . LYS A 184 ? 0.66689 0.69169 0.74406 0.10258  -0.04997 0.18387  191 LYS A CB  
1354 C CG  . LYS A 184 ? 0.61874 0.66093 0.71177 0.10170  -0.06251 0.16484  191 LYS A CG  
1355 C CD  . LYS A 184 ? 0.63633 0.71842 0.71209 0.10061  -0.08221 0.15756  191 LYS A CD  
1356 C CE  . LYS A 184 ? 0.70771 0.80627 0.80385 0.09601  -0.09309 0.13889  191 LYS A CE  
1357 N NZ  . LYS A 184 ? 0.70063 0.83723 0.78516 0.09369  -0.11412 0.13177  191 LYS A NZ  
1358 N N   . GLU A 185 ? 0.84354 0.80253 0.93276 0.11242  -0.01381 0.23538  192 GLU A N   
1359 C CA  . GLU A 185 ? 0.70712 0.64587 0.79153 0.11409  0.00173  0.26305  192 GLU A CA  
1360 C C   . GLU A 185 ? 0.84413 0.81148 0.89513 0.11266  0.00013  0.27331  192 GLU A C   
1361 O O   . GLU A 185 ? 0.85708 0.81087 0.90370 0.10557  0.01586  0.28690  192 GLU A O   
1362 C CB  . GLU A 185 ? 0.87841 0.80309 0.97452 0.13504  0.00572  0.29422  192 GLU A CB  
1363 C CG  . GLU A 185 ? 1.10950 1.07283 1.18267 0.15393  -0.00746 0.31906  192 GLU A CG  
1364 C CD  . GLU A 185 ? 1.47493 1.43218 1.56615 0.17781  -0.00846 0.34554  192 GLU A CD  
1365 O OE1 . GLU A 185 ? 1.46825 1.46157 1.56056 0.19049  -0.02677 0.34471  192 GLU A OE1 
1366 O OE2 . GLU A 185 ? 1.47548 1.39249 1.58211 0.18400  0.00900  0.36770  192 GLU A OE2 
1367 N N   . ASP A 186 ? 0.82088 0.82771 0.84852 0.11855  -0.01787 0.26597  193 ASP A N   
1368 C CA  . ASP A 186 ? 0.77434 0.80910 0.76405 0.12009  -0.02027 0.27357  193 ASP A CA  
1369 C C   . ASP A 186 ? 0.81283 0.85869 0.79013 0.10421  -0.02178 0.24275  193 ASP A C   
1370 O O   . ASP A 186 ? 0.92668 0.99744 0.86994 0.10615  -0.02523 0.24179  193 ASP A O   
1371 C CB  . ASP A 186 ? 0.93315 1.00490 0.90076 0.13666  -0.04079 0.28374  193 ASP A CB  
1372 C CG  . ASP A 186 ? 1.13192 1.22190 1.11437 0.13470  -0.06107 0.25742  193 ASP A CG  
1373 O OD1 . ASP A 186 ? 1.11432 1.18647 1.13123 0.13564  -0.05911 0.25347  193 ASP A OD1 
1374 O OD2 . ASP A 186 ? 1.14810 1.26935 1.10799 0.13190  -0.07797 0.24034  193 ASP A OD2 
1375 N N   . GLN A 187 ? 0.79267 0.82042 0.79499 0.09010  -0.01899 0.21784  194 GLN A N   
1376 C CA  . GLN A 187 ? 0.83809 0.87537 0.83301 0.07712  -0.02126 0.18932  194 GLN A CA  
1377 C C   . GLN A 187 ? 0.76390 0.77920 0.77748 0.06277  -0.00411 0.18457  194 GLN A C   
1378 O O   . GLN A 187 ? 0.77044 0.78377 0.79446 0.05161  -0.00640 0.15966  194 GLN A O   
1379 C CB  . GLN A 187 ? 0.72761 0.77129 0.73382 0.07346  -0.03746 0.16242  194 GLN A CB  
1380 C CG  . GLN A 187 ? 0.65899 0.72891 0.65435 0.08461  -0.05653 0.16470  194 GLN A CG  
1381 C CD  . GLN A 187 ? 0.77718 0.87552 0.73446 0.08778  -0.06575 0.16184  194 GLN A CD  
1382 O OE1 . GLN A 187 ? 0.85273 0.95248 0.79442 0.07996  -0.06106 0.14596  194 GLN A OE1 
1383 N NE2 . GLN A 187 ? 0.75919 0.88127 0.70060 0.10037  -0.07925 0.17662  194 GLN A NE2 
1384 N N   . THR A 188 ? 0.82352 0.82344 0.84330 0.06250  0.01268  0.20947  195 THR A N   
1385 C CA  . THR A 188 ? 0.72053 0.70187 0.76392 0.04663  0.02790  0.20603  195 THR A CA  
1386 C C   . THR A 188 ? 0.78096 0.78406 0.81074 0.04065  0.03648  0.20197  195 THR A C   
1387 O O   . THR A 188 ? 0.75353 0.74915 0.80607 0.02677  0.04794  0.19831  195 THR A O   
1388 C CB  . THR A 188 ? 0.71553 0.66805 0.77744 0.04610  0.04364  0.23418  195 THR A CB  
1389 O OG1 . THR A 188 ? 0.87009 0.83581 0.90927 0.05509  0.05430  0.26447  195 THR A OG1 
1390 C CG2 . THR A 188 ? 0.75311 0.68339 0.82742 0.05637  0.03701  0.23962  195 THR A CG2 
1391 N N   . GLU A 189 ? 0.78243 0.81332 0.77660 0.05095  0.03112  0.20142  196 GLU A N   
1392 C CA  . GLU A 189 ? 0.79795 0.84931 0.77761 0.04790  0.04044  0.19400  196 GLU A CA  
1393 C C   . GLU A 189 ? 0.81100 0.86294 0.80914 0.03693  0.03526  0.16303  196 GLU A C   
1394 O O   . GLU A 189 ? 0.92062 0.98434 0.92289 0.03191  0.04670  0.15820  196 GLU A O   
1395 C CB  . GLU A 189 ? 0.80250 0.88036 0.73559 0.06202  0.03349  0.19387  196 GLU A CB  
1396 C CG  . GLU A 189 ? 0.75659 0.84318 0.67776 0.06411  0.01116  0.16428  196 GLU A CG  
1397 C CD  . GLU A 189 ? 0.94836 1.05804 0.82465 0.07723  -0.00044 0.16515  196 GLU A CD  
1398 O OE1 . GLU A 189 ? 0.97978 1.09299 0.84763 0.08625  -0.00984 0.18300  196 GLU A OE1 
1399 O OE2 . GLU A 189 ? 0.88534 1.00989 0.73472 0.07914  -0.00080 0.14717  196 GLU A OE2 
1400 N N   . TYR A 190 ? 0.56215 0.60328 0.57251 0.03430  0.01935  0.14406  197 TYR A N   
1401 C CA  . TYR A 190 ? 0.73391 0.77443 0.75994 0.02542  0.01331  0.11731  197 TYR A CA  
1402 C C   . TYR A 190 ? 0.74534 0.76877 0.80759 0.01151  0.02019  0.11596  197 TYR A C   
1403 O O   . TYR A 190 ? 0.67176 0.69433 0.74823 0.00437  0.01393  0.09582  197 TYR A O   
1404 C CB  . TYR A 190 ? 0.69239 0.73090 0.71348 0.02872  -0.00559 0.09945  197 TYR A CB  
1405 C CG  . TYR A 190 ? 0.76414 0.82116 0.75196 0.03955  -0.01542 0.09764  197 TYR A CG  
1406 C CD1 . TYR A 190 ? 0.77264 0.84537 0.73772 0.04214  -0.01424 0.08520  197 TYR A CD1 
1407 C CD2 . TYR A 190 ? 0.71136 0.77109 0.69078 0.04772  -0.02614 0.10781  197 TYR A CD2 
1408 C CE1 . TYR A 190 ? 0.76764 0.85577 0.69932 0.05070  -0.02457 0.08005  197 TYR A CE1 
1409 C CE2 . TYR A 190 ? 0.72168 0.80184 0.67076 0.05607  -0.03808 0.10483  197 TYR A CE2 
1410 C CZ  . TYR A 190 ? 0.67429 0.76734 0.59789 0.05660  -0.03772 0.08960  197 TYR A CZ  
1411 O OH  . TYR A 190 ? 0.83841 0.95006 0.72888 0.06355  -0.05097 0.08283  197 TYR A OH  
1412 N N   . LEU A 191 ? 0.71003 0.71930 0.78707 0.00721  0.03221  0.13702  198 LEU A N   
1413 C CA  . LEU A 191 ? 0.69889 0.69498 0.81032 -0.00877 0.04020  0.13605  198 LEU A CA  
1414 C C   . LEU A 191 ? 0.65008 0.66475 0.77070 -0.01496 0.05692  0.14778  198 LEU A C   
1415 O O   . LEU A 191 ? 0.73582 0.74583 0.88922 -0.03037 0.06336  0.14745  198 LEU A O   
1416 C CB  . LEU A 191 ? 0.59735 0.56117 0.72530 -0.01222 0.04422  0.15007  198 LEU A CB  
1417 C CG  . LEU A 191 ? 0.55396 0.49898 0.67783 -0.00467 0.03129  0.14082  198 LEU A CG  
1418 C CD1 . LEU A 191 ? 0.68429 0.59795 0.81998 -0.00243 0.03920  0.16030  198 LEU A CD1 
1419 C CD2 . LEU A 191 ? 0.62572 0.56441 0.76309 -0.01391 0.02089  0.11290  198 LEU A CD2 
1420 N N   . GLU A 192 ? 0.66913 0.70654 0.76192 -0.00353 0.06410  0.15731  199 GLU A N   
1421 C CA  . GLU A 192 ? 0.75636 0.81464 0.85493 -0.00638 0.08373  0.17151  199 GLU A CA  
1422 C C   . GLU A 192 ? 0.77238 0.85497 0.87673 -0.00718 0.08263  0.15018  199 GLU A C   
1423 O O   . GLU A 192 ? 0.72811 0.81610 0.81087 0.00196  0.06976  0.12988  199 GLU A O   
1424 C CB  . GLU A 192 ? 0.80838 0.87910 0.86864 0.00872  0.09410  0.19358  199 GLU A CB  
1425 C CG  . GLU A 192 ? 0.99190 1.04636 1.05840 0.00706  0.10806  0.22767  199 GLU A CG  
1426 C CD  . GLU A 192 ? 1.27509 1.33498 1.37492 -0.00708 0.13107  0.24592  199 GLU A CD  
1427 O OE1 . GLU A 192 ? 1.20685 1.28581 1.32950 -0.01613 0.13503  0.23145  199 GLU A OE1 
1428 O OE2 . GLU A 192 ? 1.31522 1.36085 1.42151 -0.00925 0.14550  0.27644  199 GLU A OE2 
1429 N N   . GLU A 193 ? 0.73649 0.83388 0.87338 -0.01821 0.09655  0.15595  200 GLU A N   
1430 C CA  . GLU A 193 ? 0.65631 0.77785 0.80797 -0.01872 0.09569  0.13768  200 GLU A CA  
1431 C C   . GLU A 193 ? 0.72391 0.86671 0.83907 -0.00031 0.10200  0.13235  200 GLU A C   
1432 O O   . GLU A 193 ? 0.71374 0.85937 0.81710 0.00740  0.09027  0.10955  200 GLU A O   
1433 C CB  . GLU A 193 ? 0.74312 0.88205 0.94132 -0.03421 0.11032  0.14865  200 GLU A CB  
1434 C CG  . GLU A 193 ? 0.88756 1.06065 1.10257 -0.03060 0.11486  0.13695  200 GLU A CG  
1435 C CD  . GLU A 193 ? 1.03733 1.23212 1.30688 -0.04829 0.12572  0.14687  200 GLU A CD  
1436 O OE1 . GLU A 193 ? 0.96512 1.14495 1.25805 -0.06511 0.13038  0.16215  200 GLU A OE1 
1437 O OE2 . GLU A 193 ? 1.12558 1.35248 1.41722 -0.04550 0.12947  0.13952  200 GLU A OE2 
1438 N N   . ARG A 194 ? 0.68102 0.83718 0.77628 0.00721  0.12141  0.15319  201 ARG A N   
1439 C CA  . ARG A 194 ? 0.80456 0.98084 0.86151 0.02516  0.12945  0.14615  201 ARG A CA  
1440 C C   . ARG A 194 ? 0.73707 0.89903 0.74926 0.03696  0.10993  0.12893  201 ARG A C   
1441 O O   . ARG A 194 ? 0.85929 1.03041 0.84392 0.04935  0.10854  0.11050  201 ARG A O   
1442 C CB  . ARG A 194 ? 0.65713 0.85116 0.69747 0.03116  0.15542  0.17400  201 ARG A CB  
1443 C CG  . ARG A 194 ? 0.96087 1.13900 0.97004 0.03501  0.15428  0.19621  201 ARG A CG  
1444 C CD  . ARG A 194 ? 1.08144 1.27874 1.03777 0.05316  0.16897  0.20722  201 ARG A CD  
1445 N NE  . ARG A 194 ? 1.24886 1.45126 1.16516 0.06733  0.15603  0.17717  201 ARG A NE  
1446 C CZ  . ARG A 194 ? 1.18450 1.37655 1.05898 0.07601  0.13636  0.16775  201 ARG A CZ  
1447 N NH1 . ARG A 194 ? 1.07954 1.25820 0.94567 0.07486  0.12716  0.18717  201 ARG A NH1 
1448 N NH2 . ARG A 194 ? 1.13555 1.33087 0.97840 0.08606  0.12543  0.13817  201 ARG A NH2 
1449 N N   . ARG A 195 ? 0.81877 0.95828 0.82587 0.03314  0.09489  0.13381  202 ARG A N   
1450 C CA  . ARG A 195 ? 0.73908 0.86881 0.71269 0.04177  0.07445  0.11733  202 ARG A CA  
1451 C C   . ARG A 195 ? 0.79331 0.91436 0.78281 0.03777  0.05795  0.08906  202 ARG A C   
1452 O O   . ARG A 195 ? 0.76871 0.89089 0.73336 0.04586  0.04830  0.06894  202 ARG A O   
1453 C CB  . ARG A 195 ? 0.79065 0.90318 0.75931 0.04065  0.06475  0.13339  202 ARG A CB  
1454 C CG  . ARG A 195 ? 0.73508 0.84420 0.67279 0.04915  0.04364  0.12009  202 ARG A CG  
1455 C CD  . ARG A 195 ? 0.80036 0.92836 0.68919 0.06299  0.04607  0.11967  202 ARG A CD  
1456 N NE  . ARG A 195 ? 0.80053 0.92818 0.66277 0.06881  0.02355  0.10788  202 ARG A NE  
1457 C CZ  . ARG A 195 ? 0.85689 0.98856 0.69843 0.07181  0.01129  0.08009  202 ARG A CZ  
1458 N NH1 . ARG A 195 ? 0.94368 1.07772 0.78493 0.07242  0.02020  0.06133  202 ARG A NH1 
1459 N NH2 . ARG A 195 ? 0.80330 0.93649 0.62704 0.07416  -0.01039 0.07105  202 ARG A NH2 
1460 N N   . ILE A 196 ? 0.79318 0.90456 0.82289 0.02499  0.05449  0.08723  203 ILE A N   
1461 C CA  . ILE A 196 ? 0.70917 0.81304 0.75285 0.02182  0.03968  0.06395  203 ILE A CA  
1462 C C   . ILE A 196 ? 0.76730 0.88759 0.81080 0.02890  0.04619  0.04995  203 ILE A C   
1463 O O   . ILE A 196 ? 0.70811 0.82244 0.74027 0.03452  0.03547  0.03010  203 ILE A O   
1464 C CB  . ILE A 196 ? 0.64989 0.74230 0.73227 0.00723  0.03507  0.06542  203 ILE A CB  
1465 C CG1 . ILE A 196 ? 0.62489 0.69546 0.70590 0.00309  0.02817  0.07508  203 ILE A CG1 
1466 C CG2 . ILE A 196 ? 0.56487 0.65386 0.65922 0.00544  0.02184  0.04429  203 ILE A CG2 
1467 C CD1 . ILE A 196 ? 0.59422 0.65154 0.70982 -0.01155 0.02957  0.08023  203 ILE A CD1 
1468 N N   . LYS A 197 ? 0.77128 0.91214 0.82997 0.02918  0.06512  0.06100  204 LYS A N   
1469 C CA  . LYS A 197 ? 0.68021 0.83913 0.74133 0.03898  0.07435  0.04941  204 LYS A CA  
1470 C C   . LYS A 197 ? 0.70206 0.85874 0.71674 0.05479  0.07468  0.03577  204 LYS A C   
1471 O O   . LYS A 197 ? 0.84271 0.99745 0.85294 0.06336  0.07179  0.01601  204 LYS A O   
1472 C CB  . LYS A 197 ? 0.63919 0.82533 0.72535 0.03725  0.09742  0.06703  204 LYS A CB  
1473 C CG  . LYS A 197 ? 0.73189 0.92998 0.87136 0.02468  0.09593  0.06855  204 LYS A CG  
1474 C CD  . LYS A 197 ? 0.78074 0.99519 0.95067 0.01224  0.11281  0.09278  204 LYS A CD  
1475 C CE  . LYS A 197 ? 0.86517 1.11633 1.07379 0.01312  0.12828  0.09642  204 LYS A CE  
1476 N NZ  . LYS A 197 ? 0.99093 1.26181 1.22440 0.00291  0.15037  0.12259  204 LYS A NZ  
1477 N N   . GLU A 198 ? 0.80207 0.95780 0.78112 0.05899  0.07735  0.04579  205 GLU A N   
1478 C CA  . GLU A 198 ? 0.88424 1.03867 0.81484 0.07256  0.07498  0.03079  205 GLU A CA  
1479 C C   . GLU A 198 ? 0.82503 0.95793 0.74691 0.07090  0.05113  0.00744  205 GLU A C   
1480 O O   . GLU A 198 ? 0.96025 1.08782 0.86159 0.07951  0.04845  -0.01492 205 GLU A O   
1481 C CB  . GLU A 198 ? 0.85186 1.01237 0.74596 0.07671  0.07931  0.04900  205 GLU A CB  
1482 C CG  . GLU A 198 ? 0.96973 1.12862 0.80978 0.08830  0.07021  0.03178  205 GLU A CG  
1483 C CD  . GLU A 198 ? 1.22533 1.39356 1.02778 0.09338  0.07165  0.05233  205 GLU A CD  
1484 O OE1 . GLU A 198 ? 1.15503 1.32457 0.97658 0.08716  0.07743  0.08062  205 GLU A OE1 
1485 O OE2 . GLU A 198 ? 1.17035 1.34382 0.92335 0.10388  0.06673  0.04020  205 GLU A OE2 
1486 N N   . ILE A 199 ? 0.82161 0.94086 0.76010 0.05986  0.03503  0.01227  206 ILE A N   
1487 C CA  . ILE A 199 ? 0.82045 0.92198 0.75473 0.05690  0.01399  -0.00650 206 ILE A CA  
1488 C C   . ILE A 199 ? 0.82661 0.91977 0.78447 0.05626  0.01203  -0.02307 206 ILE A C   
1489 O O   . ILE A 199 ? 0.79114 0.87191 0.73642 0.05958  0.00299  -0.04327 206 ILE A O   
1490 C CB  . ILE A 199 ? 0.73698 0.82903 0.68557 0.04717  0.00097  0.00508  206 ILE A CB  
1491 C CG1 . ILE A 199 ? 0.82178 0.92239 0.75140 0.05006  0.00530  0.02671  206 ILE A CG1 
1492 C CG2 . ILE A 199 ? 0.72966 0.80856 0.67336 0.04435  -0.01906 -0.01184 206 ILE A CG2 
1493 C CD1 . ILE A 199 ? 0.70458 0.79597 0.64140 0.04535  -0.00854 0.03602  206 ILE A CD1 
1494 N N   . VAL A 200 ? 0.74215 0.84181 0.73546 0.05163  0.01966  -0.01420 207 VAL A N   
1495 C CA  . VAL A 200 ? 0.72956 0.82534 0.74593 0.05313  0.01767  -0.02624 207 VAL A CA  
1496 C C   . VAL A 200 ? 0.82341 0.92431 0.82526 0.06778  0.02921  -0.03943 207 VAL A C   
1497 O O   . VAL A 200 ? 0.84395 0.92979 0.84377 0.07307  0.02309  -0.05662 207 VAL A O   
1498 C CB  . VAL A 200 ? 0.65435 0.76215 0.71103 0.04495  0.02193  -0.01339 207 VAL A CB  
1499 C CG1 . VAL A 200 ? 0.68861 0.80242 0.76808 0.05093  0.02335  -0.02199 207 VAL A CG1 
1500 C CG2 . VAL A 200 ? 0.62345 0.71770 0.69279 0.03186  0.00807  -0.00836 207 VAL A CG2 
1501 N N   . LYS A 201 ? 0.87883 0.99932 0.86978 0.07533  0.04767  -0.03119 208 LYS A N   
1502 C CA  . LYS A 201 ? 0.77428 0.90112 0.75014 0.09168  0.06247  -0.04388 208 LYS A CA  
1503 C C   . LYS A 201 ? 0.93924 1.04687 0.86936 0.09896  0.05511  -0.06569 208 LYS A C   
1504 O O   . LYS A 201 ? 1.04079 1.14313 0.95674 0.11263  0.06386  -0.08338 208 LYS A O   
1505 C CB  . LYS A 201 ? 0.86482 1.02058 0.84013 0.09751  0.08648  -0.02696 208 LYS A CB  
1506 C CG  . LYS A 201 ? 0.77233 0.93907 0.73233 0.11681  0.10671  -0.03837 208 LYS A CG  
1507 C CD  . LYS A 201 ? 0.83471 1.01565 0.75328 0.12464  0.12333  -0.03097 208 LYS A CD  
1508 C CE  . LYS A 201 ? 0.86428 1.03707 0.73983 0.14364  0.13186  -0.05623 208 LYS A CE  
1509 N NZ  . LYS A 201 ? 0.92567 1.12454 0.80913 0.16027  0.16212  -0.05242 208 LYS A NZ  
1510 N N   . LYS A 202 ? 1.07217 1.16960 0.98046 0.09031  0.03887  -0.06578 209 LYS A N   
1511 C CA  . LYS A 202 ? 0.95578 1.03905 0.82187 0.09428  0.02862  -0.08687 209 LYS A CA  
1512 C C   . LYS A 202 ? 0.96076 1.01856 0.83584 0.08524  0.00707  -0.10298 209 LYS A C   
1513 O O   . LYS A 202 ? 0.92572 0.96644 0.77716 0.08852  0.00031  -0.12684 209 LYS A O   
1514 C CB  . LYS A 202 ? 1.04907 1.14506 0.88188 0.09257  0.02497  -0.07487 209 LYS A CB  
1515 C CG  . LYS A 202 ? 0.97244 1.05701 0.77207 0.08929  0.00362  -0.09242 209 LYS A CG  
1516 C CD  . LYS A 202 ? 0.99259 1.09554 0.75234 0.09308  0.00254  -0.08044 209 LYS A CD  
1517 C CE  . LYS A 202 ? 1.16571 1.26261 0.88484 0.09302  -0.01715 -0.10443 209 LYS A CE  
1518 N NZ  . LYS A 202 ? 1.23454 1.35289 0.91289 0.09767  -0.02157 -0.09090 209 LYS A NZ  
1519 N N   . HIS A 203 ? 1.04866 1.10254 0.95776 0.07371  -0.00266 -0.09125 210 HIS A N   
1520 C CA  . HIS A 203 ? 1.01865 1.05175 0.93739 0.06425  -0.02123 -0.10201 210 HIS A CA  
1521 C C   . HIS A 203 ? 1.01024 1.03119 0.96399 0.06252  -0.02135 -0.10207 210 HIS A C   
1522 O O   . HIS A 203 ? 1.03520 1.03562 0.99445 0.05748  -0.03266 -0.11331 210 HIS A O   
1523 C CB  . HIS A 203 ? 0.91671 0.95536 0.83938 0.05285  -0.03472 -0.08843 210 HIS A CB  
1524 C CG  . HIS A 203 ? 1.02643 1.07432 0.91434 0.05379  -0.04221 -0.09046 210 HIS A CG  
1525 N ND1 . HIS A 203 ? 1.02791 1.06674 0.89074 0.05327  -0.05428 -0.11272 210 HIS A ND1 
1526 C CD2 . HIS A 203 ? 1.02663 1.09236 0.90065 0.05521  -0.04050 -0.07233 210 HIS A CD2 
1527 C CE1 . HIS A 203 ? 1.11319 1.16768 0.94657 0.05460  -0.06129 -0.10884 210 HIS A CE1 
1528 N NE2 . HIS A 203 ? 1.04016 1.11084 0.87936 0.05689  -0.05245 -0.08286 210 HIS A NE2 
1529 N N   . SER A 204 ? 1.02727 0.83353 0.79722 -0.02072 -0.21141 -0.08442 211 SER A N   
1530 C CA  . SER A 204 ? 1.16098 0.98151 0.98689 -0.01915 -0.18574 -0.08099 211 SER A CA  
1531 C C   . SER A 204 ? 1.08555 0.89387 0.87583 0.00241  -0.14774 -0.08507 211 SER A C   
1532 O O   . SER A 204 ? 1.06165 0.90237 0.88940 0.00937  -0.11950 -0.07057 211 SER A O   
1533 C CB  . SER A 204 ? 1.10845 0.98105 1.00712 -0.02453 -0.17804 -0.05749 211 SER A CB  
1534 O OG  . SER A 204 ? 1.18133 1.06862 1.11865 -0.04107 -0.21013 -0.05087 211 SER A OG  
1535 N N   . GLN A 205 ? 1.35519 1.11738 1.07245 0.01354  -0.14662 -0.10512 212 GLN A N   
1536 C CA  . GLN A 205 ? 1.41294 1.16385 1.09675 0.03767  -0.10832 -0.10760 212 GLN A CA  
1537 C C   . GLN A 205 ? 1.33324 1.07453 1.05550 0.04109  -0.09122 -0.11194 212 GLN A C   
1538 O O   . GLN A 205 ? 1.39364 1.14657 1.11771 0.06023  -0.05648 -0.10366 212 GLN A O   
1539 C CB  . GLN A 205 ? 1.22645 0.92721 0.81538 0.05219  -0.10863 -0.12947 212 GLN A CB  
1540 C CG  . GLN A 205 ? 1.55038 1.19877 1.09944 0.03665  -0.14800 -0.15823 212 GLN A CG  
1541 C CD  . GLN A 205 ? 1.55189 1.21961 1.10770 0.01485  -0.18961 -0.15133 212 GLN A CD  
1542 O OE1 . GLN A 205 ? 1.57503 1.26021 1.09389 0.02077  -0.19214 -0.13968 212 GLN A OE1 
1543 N NE2 . GLN A 205 ? 1.40169 1.06888 1.00843 -0.00986 -0.22191 -0.15518 212 GLN A NE2 
1544 N N   . PHE A 206 ? 1.38036 1.10385 1.13683 0.02296  -0.11484 -0.12130 213 PHE A N   
1545 C CA  . PHE A 206 ? 1.25797 0.96351 1.04541 0.02631  -0.10068 -0.12487 213 PHE A CA  
1546 C C   . PHE A 206 ? 1.09951 0.84975 0.97220 0.01023  -0.10430 -0.10525 213 PHE A C   
1547 O O   . PHE A 206 ? 1.12600 0.85856 1.03227 -0.00388 -0.11911 -0.10952 213 PHE A O   
1548 C CB  . PHE A 206 ? 1.36092 0.99656 1.11061 0.01962  -0.12187 -0.15397 213 PHE A CB  
1549 C CG  . PHE A 206 ? 1.47209 1.05856 1.12771 0.03553  -0.11944 -0.17799 213 PHE A CG  
1550 C CD1 . PHE A 206 ? 1.44091 1.02978 1.05852 0.06573  -0.08043 -0.17396 213 PHE A CD1 
1551 C CD2 . PHE A 206 ? 1.56968 1.11046 1.17405 0.02023  -0.15613 -0.20383 213 PHE A CD2 
1552 C CE1 . PHE A 206 ? 1.59549 1.14058 1.12302 0.08312  -0.07415 -0.19539 213 PHE A CE1 
1553 C CE2 . PHE A 206 ? 1.61261 1.10733 1.12139 0.03573  -0.15322 -0.22792 213 PHE A CE2 
1554 C CZ  . PHE A 206 ? 1.55549 1.05165 1.02443 0.06861  -0.11017 -0.22375 213 PHE A CZ  
1555 N N   . ILE A 207 ? 1.07213 0.87898 0.97879 0.01171  -0.09039 -0.08390 214 ILE A N   
1556 C CA  . ILE A 207 ? 0.89565 0.74817 0.87505 0.00013  -0.08810 -0.06607 214 ILE A CA  
1557 C C   . ILE A 207 ? 0.79784 0.67396 0.79681 0.01497  -0.05475 -0.05321 214 ILE A C   
1558 O O   . ILE A 207 ? 0.84744 0.73611 0.82110 0.03101  -0.03255 -0.04810 214 ILE A O   
1559 C CB  . ILE A 207 ? 0.81226 0.70766 0.81504 -0.00891 -0.09600 -0.05366 214 ILE A CB  
1560 C CG1 . ILE A 207 ? 0.86733 0.74700 0.86420 -0.02419 -0.13186 -0.06087 214 ILE A CG1 
1561 C CG2 . ILE A 207 ? 0.72776 0.67103 0.79546 -0.01566 -0.08500 -0.03731 214 ILE A CG2 
1562 C CD1 . ILE A 207 ? 0.76122 0.64274 0.81057 -0.04245 -0.15214 -0.05978 214 ILE A CD1 
1563 N N   . GLY A 208 ? 0.77713 0.66325 0.82333 0.00945  -0.05151 -0.04488 215 GLY A N   
1564 C CA  . GLY A 208 ? 0.62691 0.53453 0.69171 0.02376  -0.02314 -0.03056 215 GLY A CA  
1565 C C   . GLY A 208 ? 0.68702 0.65949 0.78679 0.02167  -0.00917 -0.01156 215 GLY A C   
1566 O O   . GLY A 208 ? 0.66408 0.66610 0.79671 0.02500  0.00554  0.00388  215 GLY A O   
1567 N N   . TYR A 209 ? 0.56213 0.55579 0.65402 0.01565  -0.01430 -0.01229 216 TYR A N   
1568 C CA  . TYR A 209 ? 0.54714 0.59467 0.66678 0.01117  -0.00293 0.00090  216 TYR A CA  
1569 C C   . TYR A 209 ? 0.62780 0.67961 0.71846 0.01361  -0.00029 -0.00054 216 TYR A C   
1570 O O   . TYR A 209 ? 0.56582 0.58477 0.62252 0.01445  -0.01343 -0.01055 216 TYR A O   
1571 C CB  . TYR A 209 ? 0.54609 0.61740 0.70886 -0.00564 -0.01507 0.00374  216 TYR A CB  
1572 C CG  . TYR A 209 ? 0.53482 0.60547 0.72982 -0.00915 -0.01665 0.00958  216 TYR A CG  
1573 C CD1 . TYR A 209 ? 0.49613 0.60044 0.71429 -0.00474 0.00092  0.02440  216 TYR A CD1 
1574 C CD2 . TYR A 209 ? 0.54499 0.58327 0.74869 -0.01796 -0.03676 0.00282  216 TYR A CD2 
1575 C CE1 . TYR A 209 ? 0.42136 0.52591 0.66994 -0.00719 0.00111  0.03426  216 TYR A CE1 
1576 C CE2 . TYR A 209 ? 0.55691 0.59405 0.79484 -0.02270 -0.03727 0.01149  216 TYR A CE2 
1577 C CZ  . TYR A 209 ? 0.49847 0.56807 0.75831 -0.01630 -0.01693 0.02816  216 TYR A CZ  
1578 O OH  . TYR A 209 ? 0.55197 0.62188 0.84697 -0.02028 -0.01575 0.04125  216 TYR A OH  
1579 N N   . PRO A 210 ? 0.47862 0.57059 0.58112 0.01378  0.01555  0.01059  217 PRO A N   
1580 C CA  . PRO A 210 ? 0.46909 0.56503 0.54890 0.01481  0.01972  0.01299  217 PRO A CA  
1581 C C   . PRO A 210 ? 0.50272 0.59374 0.59054 0.00141  0.00210  0.00852  217 PRO A C   
1582 O O   . PRO A 210 ? 0.53218 0.64181 0.65591 -0.01026 -0.00350 0.00823  217 PRO A O   
1583 C CB  . PRO A 210 ? 0.45628 0.59976 0.55834 0.01340  0.03833  0.02688  217 PRO A CB  
1584 C CG  . PRO A 210 ? 0.53681 0.70602 0.67493 0.00694  0.03834  0.02970  217 PRO A CG  
1585 C CD  . PRO A 210 ? 0.49494 0.63128 0.63139 0.01178  0.02914  0.02287  217 PRO A CD  
1586 N N   . ILE A 211 ? 0.49470 0.56093 0.54780 0.00517  -0.00542 0.00640  218 ILE A N   
1587 C CA  . ILE A 211 ? 0.56832 0.62990 0.62774 -0.00410 -0.02128 0.00705  218 ILE A CA  
1588 C C   . ILE A 211 ? 0.62777 0.70307 0.67896 -0.00367 -0.00836 0.01885  218 ILE A C   
1589 O O   . ILE A 211 ? 0.67810 0.74102 0.68945 0.00658  -0.00192 0.02378  218 ILE A O   
1590 C CB  . ILE A 211 ? 0.66566 0.69089 0.69348 -0.00211 -0.04428 -0.00089 218 ILE A CB  
1591 C CG1 . ILE A 211 ? 0.62410 0.63235 0.66113 -0.00479 -0.05670 -0.01224 218 ILE A CG1 
1592 C CG2 . ILE A 211 ? 0.54401 0.57117 0.58774 -0.01041 -0.06162 0.00468  218 ILE A CG2 
1593 C CD1 . ILE A 211 ? 0.60360 0.57211 0.60160 -0.00455 -0.08056 -0.02372 218 ILE A CD1 
1594 N N   . THR A 212 ? 0.49352 0.59280 0.58135 -0.01504 -0.00358 0.02332  219 THR A N   
1595 C CA  . THR A 212 ? 0.51009 0.62214 0.59966 -0.01914 0.00850  0.03508  219 THR A CA  
1596 C C   . THR A 212 ? 0.50887 0.60428 0.60330 -0.02372 -0.00338 0.03971  219 THR A C   
1597 O O   . THR A 212 ? 0.52713 0.62110 0.65167 -0.03038 -0.01315 0.03382  219 THR A O   
1598 C CB  . THR A 212 ? 0.50411 0.64962 0.62872 -0.03090 0.02073  0.03541  219 THR A CB  
1599 O OG1 . THR A 212 ? 0.53085 0.69703 0.65228 -0.02457 0.03204  0.03712  219 THR A OG1 
1600 C CG2 . THR A 212 ? 0.53919 0.69434 0.67098 -0.03983 0.03036  0.04702  219 THR A CG2 
1601 N N   . LEU A 213 ? 0.52858 0.61340 0.59488 -0.01831 -0.00057 0.05284  220 LEU A N   
1602 C CA  . LEU A 213 ? 0.60411 0.67482 0.67553 -0.02096 -0.00974 0.06359  220 LEU A CA  
1603 C C   . LEU A 213 ? 0.53035 0.61314 0.63075 -0.03231 0.00525  0.07373  220 LEU A C   
1604 O O   . LEU A 213 ? 0.60846 0.70440 0.69876 -0.03298 0.02121  0.08523  220 LEU A O   
1605 C CB  . LEU A 213 ? 0.58817 0.64100 0.60962 -0.00903 -0.01574 0.07498  220 LEU A CB  
1606 C CG  . LEU A 213 ? 0.84267 0.88470 0.86491 -0.00940 -0.02262 0.09434  220 LEU A CG  
1607 C CD1 . LEU A 213 ? 0.63895 0.67515 0.70329 -0.01522 -0.03927 0.09092  220 LEU A CD1 
1608 C CD2 . LEU A 213 ? 0.71800 0.74488 0.68159 0.00335  -0.03217 0.10369  220 LEU A CD2 
1609 N N   . PHE A 214 ? 0.60745 0.68503 0.74533 -0.04133 0.00082  0.06950  221 PHE A N   
1610 C CA  . PHE A 214 ? 0.54892 0.62872 0.71520 -0.05474 0.01280  0.07466  221 PHE A CA  
1611 C C   . PHE A 214 ? 0.66446 0.72466 0.82465 -0.05203 0.01247  0.09744  221 PHE A C   
1612 O O   . PHE A 214 ? 0.70107 0.74259 0.86272 -0.04417 -0.00070 0.10336  221 PHE A O   
1613 C CB  . PHE A 214 ? 0.56215 0.63850 0.76634 -0.06327 0.01104  0.05754  221 PHE A CB  
1614 C CG  . PHE A 214 ? 0.54489 0.64660 0.75837 -0.07116 0.01701  0.03954  221 PHE A CG  
1615 C CD1 . PHE A 214 ? 0.60234 0.71979 0.79980 -0.06321 0.01357  0.03414  221 PHE A CD1 
1616 C CD2 . PHE A 214 ? 0.62404 0.73220 0.86077 -0.08698 0.02534  0.02832  221 PHE A CD2 
1617 C CE1 . PHE A 214 ? 0.55771 0.70117 0.76483 -0.06923 0.01917  0.02238  221 PHE A CE1 
1618 C CE2 . PHE A 214 ? 0.56557 0.70135 0.80670 -0.09428 0.02902  0.01372  221 PHE A CE2 
1619 C CZ  . PHE A 214 ? 0.50474 0.66029 0.73238 -0.08456 0.02633  0.01303  221 PHE A CZ  
1620 N N   . VAL A 215 ? 0.54690 0.61500 0.70366 -0.05848 0.02683  0.11364  222 VAL A N   
1621 C CA  . VAL A 215 ? 0.64354 0.69600 0.79526 -0.05658 0.02988  0.14064  222 VAL A CA  
1622 C C   . VAL A 215 ? 0.68690 0.71978 0.88355 -0.07082 0.03288  0.14190  222 VAL A C   
1623 O O   . VAL A 215 ? 0.66662 0.70646 0.89065 -0.08808 0.04078  0.12807  222 VAL A O   
1624 C CB  . VAL A 215 ? 0.60656 0.67889 0.73734 -0.05663 0.04680  0.16102  222 VAL A CB  
1625 C CG1 . VAL A 215 ? 0.68486 0.74315 0.81395 -0.05604 0.05234  0.19341  222 VAL A CG1 
1626 C CG2 . VAL A 215 ? 0.70625 0.79060 0.78836 -0.03890 0.04680  0.15702  222 VAL A CG2 
1627 N N   . GLU A 216 ? 0.63590 0.64296 0.83928 -0.06348 0.02604  0.15832  223 GLU A N   
1628 C CA  . GLU A 216 ? 0.73490 0.71468 0.98111 -0.07376 0.03089  0.16081  223 GLU A CA  
1629 C C   . GLU A 216 ? 0.77254 0.74912 1.03067 -0.08898 0.04604  0.18262  223 GLU A C   
1630 O O   . GLU A 216 ? 0.76331 0.75221 0.99608 -0.08365 0.05130  0.20976  223 GLU A O   
1631 C CB  . GLU A 216 ? 0.78315 0.73827 1.03816 -0.05815 0.01931  0.17607  223 GLU A CB  
1632 C CG  . GLU A 216 ? 0.78043 0.73071 1.05647 -0.05081 0.00924  0.15276  223 GLU A CG  
1633 C CD  . GLU A 216 ? 0.81705 0.75034 1.10820 -0.03410 -0.00287 0.17274  223 GLU A CD  
1634 O OE1 . GLU A 216 ? 0.78869 0.73409 1.04995 -0.02177 -0.01887 0.18938  223 GLU A OE1 
1635 O OE2 . GLU A 216 ? 0.98410 0.89169 1.31647 -0.03284 0.00336  0.17190  223 GLU A OE2 
1636 N N   . LYS A 217 ? 0.71342 0.67267 1.00985 -0.10858 0.05344  0.17060  224 LYS A N   
1637 C CA  . LYS A 217 ? 0.75149 0.70749 1.06830 -0.12917 0.06623  0.18893  224 LYS A CA  
1638 C C   . LYS A 217 ? 0.76019 0.68676 1.08757 -0.12358 0.07021  0.22638  224 LYS A C   
1639 O O   . LYS A 217 ? 0.88340 0.78136 1.21775 -0.10834 0.06316  0.23171  224 LYS A O   
1640 C CB  . LYS A 217 ? 0.79160 0.73200 1.14367 -0.15455 0.06952  0.16077  224 LYS A CB  
1641 C CG  . LYS A 217 ? 0.86717 0.84894 1.21713 -0.17382 0.07211  0.14655  224 LYS A CG  
1642 C CD  . LYS A 217 ? 0.71148 0.70732 1.05283 -0.17239 0.06472  0.10831  224 LYS A CD  
1643 C CE  . LYS A 217 ? 0.81745 0.77652 1.18407 -0.18759 0.06429  0.07904  224 LYS A CE  
1644 N NZ  . LYS A 217 ? 0.85172 0.83145 1.20845 -0.19043 0.05961  0.04357  224 LYS A NZ  
# 
