data_7HB3
# 
_entry.id   7HB3 
# 
_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   7HB3         pdb_00007hb3 10.2210/pdb7hb3/pdb 
WWPDB D_1001407250 ?            ?                   
# 
_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                        7HB3 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.recvd_initial_deposition_date   2024-07-10 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.pdb_format_compatible           N 
_pdbx_database_status.methods_development_category    ? 
# 
_pdbx_contact_author.id                 1 
_pdbx_contact_author.name_last          Yu 
_pdbx_contact_author.name_first         Feng 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.email              yufeng@sari.ac.cn 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-9502-3277 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Huang, L.' 1  ? 
'Wang, W.'  2  ? 
'Zhu, Z.'   3  ? 
'Li, Q.'    4  ? 
'Li, M.'    5  ? 
'Zhou, H.'  6  ? 
'Xu, Q.'    7  ? 
'Wen, W.'   8  ? 
'Wang, Q.'  9  ? 
'Yu, F.'    10 ? 
# 
_citation.id                        primary 
_citation.title                     
;Novel starting points for fragment-based drug design against human heat-shock protein 90 identified using crystallographic fragment screening.
;
_citation.journal_abbrev            Iucrj 
_citation.journal_volume            12 
_citation.page_first                177 
_citation.page_last                 187 
_citation.year                      2025 
_citation.journal_id_ASTM           ? 
_citation.country                   UK 
_citation.journal_id_ISSN           2052-2525 
_citation.journal_id_CSD            ? 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   39819741 
_citation.pdbx_database_id_DOI      10.1107/S2052252524012247 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.identifier_ORCID 
_citation_author.ordinal 
primary 'Huang, L.' 0009-0001-8431-0182 1  
primary 'Wang, W.'  ?                   2  
primary 'Zhu, Z.'   ?                   3  
primary 'Li, Q.'    ?                   4  
primary 'Li, M.'    ?                   5  
primary 'Zhou, H.'  ?                   6  
primary 'Xu, Q.'    0000-0002-7137-0768 7  
primary 'Wen, W.'   ?                   8  
primary 'Wang, Q.'  ?                   9  
primary 'Yu, F.'    0000-0002-9502-3277 10 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Heat shock protein HSP 90-alpha'     26859.117 1   3.6.4.10 ? ? ? 
2 non-polymer syn 'N-(3-chloro-4-fluorophenyl)thiourea' 204.652   1   ?        ? ? ? 
3 water       nat water                                 18.015    133 ?        ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        
;Heat shock 86 kDa,HSP 86,HSP86,Heat shock protein family C member 1,Lipopolysaccharide-associated protein 2,LAP-2,LPS-associated protein 2,Renal carcinoma antigen NY-REN-38
;
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;MDQPMEEEEVETFAFQAEIAQLMSLIINTFYSNKEIFLRELISNSSDALDKIRYESLTDPSKLDSGKELHINLIPNKQDR
TLTIVDTGIGMTKADLINNLGTIAKSGTKAFMEALQAGADISMIGQFGVGFYSAYLVAEKVTVITKHNDDEQYAWESSAG
GSFTVRTDTGEPMGRGTKVILHLKEDQTEYLEERRIKEIVKKHSQFIGYPITLFVEKERDKEVSDDEAELEHHHHHH
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MDQPMEEEEVETFAFQAEIAQLMSLIINTFYSNKEIFLRELISNSSDALDKIRYESLTDPSKLDSGKELHINLIPNKQDR
TLTIVDTGIGMTKADLINNLGTIAKSGTKAFMEALQAGADISMIGQFGVGFYSAYLVAEKVTVITKHNDDEQYAWESSAG
GSFTVRTDTGEPMGRGTKVILHLKEDQTEYLEERRIKEIVKKHSQFIGYPITLFVEKERDKEVSDDEAELEHHHHHH
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'N-(3-chloro-4-fluorophenyl)thiourea' A1AYM 
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 
A1AYM non-polymer         . 'N-(3-chloro-4-fluorophenyl)thiourea' ? 'C7 H6 Cl F N2 S' 204.652 
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        A1AYM 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1AYM 
_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 A1AYM 1   301 301 A1AYM AJO A . 
C 3 HOH   1   401 9   HOH   HOH A . 
C 3 HOH   2   402 94  HOH   HOH A . 
C 3 HOH   3   403 71  HOH   HOH A . 
C 3 HOH   4   404 51  HOH   HOH A . 
C 3 HOH   5   405 100 HOH   HOH A . 
C 3 HOH   6   406 13  HOH   HOH A . 
C 3 HOH   7   407 132 HOH   HOH A . 
C 3 HOH   8   408 104 HOH   HOH A . 
C 3 HOH   9   409 27  HOH   HOH A . 
C 3 HOH   10  410 1   HOH   HOH A . 
C 3 HOH   11  411 92  HOH   HOH A . 
C 3 HOH   12  412 2   HOH   HOH A . 
C 3 HOH   13  413 3   HOH   HOH A . 
C 3 HOH   14  414 45  HOH   HOH A . 
C 3 HOH   15  415 32  HOH   HOH A . 
C 3 HOH   16  416 31  HOH   HOH A . 
C 3 HOH   17  417 19  HOH   HOH A . 
C 3 HOH   18  418 64  HOH   HOH A . 
C 3 HOH   19  419 40  HOH   HOH A . 
C 3 HOH   20  420 18  HOH   HOH A . 
C 3 HOH   21  421 85  HOH   HOH A . 
C 3 HOH   22  422 5   HOH   HOH A . 
C 3 HOH   23  423 49  HOH   HOH A . 
C 3 HOH   24  424 42  HOH   HOH A . 
C 3 HOH   25  425 8   HOH   HOH A . 
C 3 HOH   26  426 113 HOH   HOH A . 
C 3 HOH   27  427 37  HOH   HOH A . 
C 3 HOH   28  428 46  HOH   HOH A . 
C 3 HOH   29  429 7   HOH   HOH A . 
C 3 HOH   30  430 98  HOH   HOH A . 
C 3 HOH   31  431 47  HOH   HOH A . 
C 3 HOH   32  432 6   HOH   HOH A . 
C 3 HOH   33  433 70  HOH   HOH A . 
C 3 HOH   34  434 24  HOH   HOH A . 
C 3 HOH   35  435 77  HOH   HOH A . 
C 3 HOH   36  436 122 HOH   HOH A . 
C 3 HOH   37  437 109 HOH   HOH A . 
C 3 HOH   38  438 108 HOH   HOH A . 
C 3 HOH   39  439 12  HOH   HOH A . 
C 3 HOH   40  440 4   HOH   HOH A . 
C 3 HOH   41  441 11  HOH   HOH A . 
C 3 HOH   42  442 99  HOH   HOH A . 
C 3 HOH   43  443 20  HOH   HOH A . 
C 3 HOH   44  444 16  HOH   HOH A . 
C 3 HOH   45  445 48  HOH   HOH A . 
C 3 HOH   46  446 29  HOH   HOH A . 
C 3 HOH   47  447 34  HOH   HOH A . 
C 3 HOH   48  448 44  HOH   HOH A . 
C 3 HOH   49  449 120 HOH   HOH A . 
C 3 HOH   50  450 14  HOH   HOH A . 
C 3 HOH   51  451 30  HOH   HOH A . 
C 3 HOH   52  452 17  HOH   HOH A . 
C 3 HOH   53  453 10  HOH   HOH A . 
C 3 HOH   54  454 26  HOH   HOH A . 
C 3 HOH   55  455 33  HOH   HOH A . 
C 3 HOH   56  456 66  HOH   HOH A . 
C 3 HOH   57  457 114 HOH   HOH A . 
C 3 HOH   58  458 23  HOH   HOH A . 
C 3 HOH   59  459 21  HOH   HOH A . 
C 3 HOH   60  460 35  HOH   HOH A . 
C 3 HOH   61  461 61  HOH   HOH A . 
C 3 HOH   62  462 54  HOH   HOH A . 
C 3 HOH   63  463 80  HOH   HOH A . 
C 3 HOH   64  464 22  HOH   HOH A . 
C 3 HOH   65  465 83  HOH   HOH A . 
C 3 HOH   66  466 84  HOH   HOH A . 
C 3 HOH   67  467 101 HOH   HOH A . 
C 3 HOH   68  468 39  HOH   HOH A . 
C 3 HOH   69  469 43  HOH   HOH A . 
C 3 HOH   70  470 112 HOH   HOH A . 
C 3 HOH   71  471 93  HOH   HOH A . 
C 3 HOH   72  472 102 HOH   HOH A . 
C 3 HOH   73  473 67  HOH   HOH A . 
C 3 HOH   74  474 76  HOH   HOH A . 
C 3 HOH   75  475 50  HOH   HOH A . 
C 3 HOH   76  476 41  HOH   HOH A . 
C 3 HOH   77  477 121 HOH   HOH A . 
C 3 HOH   78  478 79  HOH   HOH A . 
C 3 HOH   79  479 105 HOH   HOH A . 
C 3 HOH   80  480 52  HOH   HOH A . 
C 3 HOH   81  481 25  HOH   HOH A . 
C 3 HOH   82  482 15  HOH   HOH A . 
C 3 HOH   83  483 95  HOH   HOH A . 
C 3 HOH   84  484 106 HOH   HOH A . 
C 3 HOH   85  485 60  HOH   HOH A . 
C 3 HOH   86  486 78  HOH   HOH A . 
C 3 HOH   87  487 53  HOH   HOH A . 
C 3 HOH   88  488 36  HOH   HOH A . 
C 3 HOH   89  489 56  HOH   HOH A . 
C 3 HOH   90  490 103 HOH   HOH A . 
C 3 HOH   91  491 57  HOH   HOH A . 
C 3 HOH   92  492 127 HOH   HOH A . 
C 3 HOH   93  493 118 HOH   HOH A . 
C 3 HOH   94  494 75  HOH   HOH A . 
C 3 HOH   95  495 74  HOH   HOH A . 
C 3 HOH   96  496 73  HOH   HOH A . 
C 3 HOH   97  497 130 HOH   HOH A . 
C 3 HOH   98  498 82  HOH   HOH A . 
C 3 HOH   99  499 117 HOH   HOH A . 
C 3 HOH   100 500 28  HOH   HOH A . 
C 3 HOH   101 501 97  HOH   HOH A . 
C 3 HOH   102 502 119 HOH   HOH A . 
C 3 HOH   103 503 55  HOH   HOH A . 
C 3 HOH   104 504 86  HOH   HOH A . 
C 3 HOH   105 505 81  HOH   HOH A . 
C 3 HOH   106 506 88  HOH   HOH A . 
C 3 HOH   107 507 38  HOH   HOH A . 
C 3 HOH   108 508 126 HOH   HOH A . 
C 3 HOH   109 509 125 HOH   HOH A . 
C 3 HOH   110 510 128 HOH   HOH A . 
C 3 HOH   111 511 63  HOH   HOH A . 
C 3 HOH   112 512 96  HOH   HOH A . 
C 3 HOH   113 513 65  HOH   HOH A . 
C 3 HOH   114 514 111 HOH   HOH A . 
C 3 HOH   115 515 91  HOH   HOH A . 
C 3 HOH   116 516 131 HOH   HOH A . 
C 3 HOH   117 517 59  HOH   HOH A . 
C 3 HOH   118 518 68  HOH   HOH A . 
C 3 HOH   119 519 58  HOH   HOH A . 
C 3 HOH   120 520 69  HOH   HOH A . 
C 3 HOH   121 521 115 HOH   HOH A . 
C 3 HOH   122 522 72  HOH   HOH A . 
C 3 HOH   123 523 107 HOH   HOH A . 
C 3 HOH   124 524 110 HOH   HOH A . 
C 3 HOH   125 525 124 HOH   HOH A . 
C 3 HOH   126 526 62  HOH   HOH A . 
C 3 HOH   127 527 123 HOH   HOH A . 
C 3 HOH   128 528 87  HOH   HOH A . 
C 3 HOH   129 529 129 HOH   HOH A . 
C 3 HOH   130 530 116 HOH   HOH A . 
C 3 HOH   131 531 133 HOH   HOH A . 
C 3 HOH   132 532 89  HOH   HOH A . 
C 3 HOH   133 533 90  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             618410.913 
_cell.length_a           69.542 
_cell.length_b           90.082 
_cell.length_c           98.717 
_cell.angle_beta         90.000 
_cell.angle_gamma        90.000 
_cell.angle_alpha        90.000 
_cell.entry_id           7HB3 
_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                         7HB3 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
# 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
_exptl.entry_id          7HB3 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_Matthews      2.88 
_exptl_crystal.density_percent_sol   57.23 
_exptl_crystal.density_meas          ? 
_exptl_crystal.description           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.pH              8.5 
_exptl_crystal_grow.temp            277 
_exptl_crystal_grow.pdbx_details    '100mM Tris-HCl pH 8.5, 22% PEG4000, 200mM MgCl2' 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_diffrn.id                     1 
_diffrn.crystal_id             1 
_diffrn.ambient_temp           100 
_diffrn.ambient_temp_details   ? 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               PIXEL 
_diffrn_detector.type                   'DECTRIS EIGER2 S 9M' 
_diffrn_detector.pdbx_collection_date   2023-07-22 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.pdbx_scattering_type             x-ray 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.monochromator                    Si111 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.97918 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.pdbx_synchrotron_beamline   BL02U1 
_diffrn_source.type                        'SSRF BEAMLINE BL02U1' 
_diffrn_source.pdbx_wavelength_list        0.97918 
_diffrn_source.pdbx_synchrotron_site       SSRF 
_diffrn_source.pdbx_wavelength             ? 
# 
_reflns.entry_id                     7HB3 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             56.850 
_reflns.d_resolution_high            2.340 
_reflns.number_obs                   13369 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         99.900 
_reflns.pdbx_Rmerge_I_obs            0.143 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        13.400 
_reflns.B_iso_Wilson_estimate        ? 
_reflns.pdbx_redundancy              10.700 
_reflns.pdbx_Rrim_I_all              0.150 
_reflns.pdbx_Rpim_I_all              0.046 
_reflns.pdbx_CC_half                 0.998 
_reflns.pdbx_netI_over_av_sigmaI     ? 
_reflns.pdbx_number_measured_all     142603 
_reflns.pdbx_scaling_rejects         92 
_reflns.pdbx_chi_squared             ? 
_reflns.Rmerge_F_all                 ? 
_reflns.Rmerge_F_obs                 ? 
_reflns.observed_criterion_F_max     ? 
_reflns.observed_criterion_F_min     ? 
_reflns.observed_criterion_I_max     ? 
_reflns.observed_criterion_I_min     ? 
_reflns.pdbx_d_res_high_opt          ? 
_reflns.pdbx_d_res_low_opt           ? 
_reflns.details                      ? 
# 
loop_
_reflns_shell.pdbx_diffrn_id 
_reflns_shell.pdbx_ordinal 
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_reflns_shell.number_measured_obs 
_reflns_shell.number_measured_all 
_reflns_shell.number_unique_obs 
_reflns_shell.pdbx_rejects 
_reflns_shell.Rmerge_I_obs 
_reflns_shell.meanI_over_sigI_obs 
_reflns_shell.pdbx_Rsym_value 
_reflns_shell.pdbx_chi_squared 
_reflns_shell.pdbx_redundancy 
_reflns_shell.percent_possible_obs 
_reflns_shell.pdbx_netI_over_sigmaI_obs 
_reflns_shell.number_possible 
_reflns_shell.number_unique_all 
_reflns_shell.Rmerge_F_all 
_reflns_shell.Rmerge_F_obs 
_reflns_shell.Rmerge_I_all 
_reflns_shell.meanI_over_sigI_all 
_reflns_shell.percent_possible_all 
_reflns_shell.pdbx_Rrim_I_all 
_reflns_shell.pdbx_Rpim_I_all 
_reflns_shell.pdbx_CC_half 
1 1 2.340 2.470  ? 21808 1910 ? 0.957 ? ? ? 11.400 ? 3.000  ? ? ? ? ? ? 99.800 1.002 0.295 0.821 
1 2 7.410 56.850 ? 4463  474  ? 0.043 ? ? ? 9.400  ? 31.700 ? ? ? ? ? ? 99.100 0.045 0.014 0.999 
# 
_refine.entry_id                                 7HB3 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.ls_percent_reflns_R_free                 4.63 
_refine.pdbx_overall_phase_error                 22.1189 
_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                          0.1841 
_refine.B_iso_mean                               43.07 
_refine.ls_number_reflns_R_free                  618 
_refine.ls_percent_reflns_obs                    99.78 
_refine.ls_R_factor_R_work                       0.1817 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_refine.ls_d_res_high                            2.34 
_refine.ls_number_reflns_obs                     13337 
_refine.pdbx_ls_sigma_F                          1.33 
_refine.ls_number_reflns_R_work                  12719 
_refine.ls_d_res_low                             28.43 
_refine.pdbx_stereochemistry_target_values       'GeoStd + Monomer Library + CDL v1.2' 
_refine.ls_R_factor_R_free                       0.2373 
_refine.overall_SU_ML                            0.2557 
_refine.pdbx_solvent_vdw_probe_radii             1.1000 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.solvent_model_param_ksol                 ? 
_refine.solvent_model_param_bsol                 ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.details                                  ? 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.overall_SU_B                             ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        1644 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         12 
_refine_hist.number_atoms_solvent             133 
_refine_hist.number_atoms_total               1789 
_refine_hist.d_res_high                       2.34 
_refine_hist.d_res_low                        28.43 
# 
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           1682 0.0036 ? ? ? 
'X-RAY DIFFRACTION' f_angle_d          2267 0.6236 ? ? ? 
'X-RAY DIFFRACTION' f_chiral_restr     259  0.0430 ? ? ? 
'X-RAY DIFFRACTION' f_plane_restr      289  0.0030 ? ? ? 
'X-RAY DIFFRACTION' f_dihedral_angle_d 224  5.1183 ? ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.R_factor_R_free 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.R_factor_all 
'X-RAY DIFFRACTION' 2.34 2.58  3128 0.2349 99.88  0.2858 154 . . . . . 
'X-RAY DIFFRACTION' 2.58 2.95  3124 0.2134 100.00 0.2599 165 . . . . . 
'X-RAY DIFFRACTION' 2.95 3.72  3180 0.1913 99.70  0.2823 139 . . . . . 
'X-RAY DIFFRACTION' 3.72 28.43 3287 0.1541 99.54  0.1932 160 . . . . . 
# 
_struct.entry_id                  7HB3 
_struct.title                     'PanDDA analysis group deposition -- Crystal structure of HSP90N in complex with Fr13043' 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_details        ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HB3 
_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              7HB3 
_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 7HB3 MET A 1   ? UNP P07900 ? ? 'initiating methionine' 8   1 
1 7HB3 LEU A 230 ? UNP P07900 ? ? 'expression tag'        237 2 
1 7HB3 GLU A 231 ? UNP P07900 ? ? 'expression tag'        238 3 
1 7HB3 HIS A 232 ? UNP P07900 ? ? 'expression tag'        239 4 
1 7HB3 HIS A 233 ? UNP P07900 ? ? 'expression tag'        240 5 
1 7HB3 HIS A 234 ? UNP P07900 ? ? 'expression tag'        241 6 
1 7HB3 HIS A 235 ? UNP P07900 ? ? 'expression tag'        242 7 
1 7HB3 HIS A 236 ? UNP P07900 ? ? 'expression tag'        243 8 
1 7HB3 HIS A 237 ? UNP P07900 ? ? 'expression tag'        244 9 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 AA1 GLN A 16  ? THR A 29  ? GLN A 23  THR A 36  1 ? 14 
HELX_P HELX_P2 AA2 GLU A 35  ? ASP A 59  ? GLU A 42  ASP A 66  1 ? 25 
HELX_P HELX_P3 AA3 PRO A 60  ? ASP A 64  ? PRO A 67  ASP A 71  5 ? 5  
HELX_P HELX_P4 AA4 THR A 92  ? ASN A 98  ? THR A 99  ASN A 105 1 ? 7  
HELX_P HELX_P5 AA5 ASN A 98  ? ALA A 117 ? ASN A 105 ALA A 124 1 ? 20 
HELX_P HELX_P6 AA6 ASP A 120 ? GLY A 128 ? ASP A 127 GLY A 135 5 ? 9  
HELX_P HELX_P7 AA7 VAL A 129 ? LEU A 136 ? VAL A 136 LEU A 143 5 ? 8  
HELX_P HELX_P8 AA8 GLU A 185 ? LEU A 191 ? GLU A 192 LEU A 198 5 ? 7  
HELX_P HELX_P9 AA9 GLU A 192 ? SER A 204 ? GLU A 199 SER A 211 1 ? 13 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
_struct_sheet.id               AA1 
_struct_sheet.type             ? 
_struct_sheet.number_strands   8 
_struct_sheet.details          ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA1 5 6 ? anti-parallel 
AA1 6 7 ? anti-parallel 
AA1 7 8 ? parallel      
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 GLU A 11  ? ALA A 14  ? GLU A 18  ALA A 21  
AA1 2 SER A 162 ? THR A 167 ? SER A 169 THR A 174 
AA1 3 TYR A 153 ? SER A 157 ? TYR A 160 SER A 164 
AA1 4 ALA A 138 ? LYS A 146 ? ALA A 145 LYS A 153 
AA1 5 GLY A 176 ? LEU A 183 ? GLY A 183 LEU A 190 
AA1 6 THR A 81  ? ASP A 86  ? THR A 88  ASP A 93  
AA1 7 ILE A 71  ? ASN A 76  ? ILE A 78  ASN A 83  
AA1 8 ILE A 211 ? LEU A 213 ? ILE A 218 LEU A 220 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N PHE A 13  ? N PHE A 20  O PHE A 163 ? O PHE A 170 
AA1 2 3 O ARG A 166 ? O ARG A 173 N ALA A 154 ? N ALA A 161 
AA1 3 4 O TRP A 155 ? O TRP A 162 N VAL A 143 ? N VAL A 150 
AA1 4 5 N ILE A 144 ? N ILE A 151 O LYS A 178 ? O LYS A 185 
AA1 5 6 O LEU A 181 ? O LEU A 188 N LEU A 82  ? N LEU A 89  
AA1 6 7 O VAL A 85  ? O VAL A 92  N ASN A 72  ? N ASN A 79  
AA1 7 8 N LEU A 73  ? N LEU A 80  O THR A 212 ? O THR A 219 
# 
_pdbx_entry_details.entry_id                   7HB3 
_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 
# 
_pdbx_validate_close_contact.id               1 
_pdbx_validate_close_contact.PDB_model_num    1 
_pdbx_validate_close_contact.auth_atom_id_1   O 
_pdbx_validate_close_contact.auth_asym_id_1   A 
_pdbx_validate_close_contact.auth_comp_id_1   HOH 
_pdbx_validate_close_contact.auth_seq_id_1    508 
_pdbx_validate_close_contact.PDB_ins_code_1   ? 
_pdbx_validate_close_contact.label_alt_id_1   ? 
_pdbx_validate_close_contact.auth_atom_id_2   O 
_pdbx_validate_close_contact.auth_asym_id_2   A 
_pdbx_validate_close_contact.auth_comp_id_2   HOH 
_pdbx_validate_close_contact.auth_seq_id_2    509 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             1.93 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 THR A 94  ? ? -102.16 41.37   
2 1 ALA A 166 ? ? 61.71   -147.03 
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z               
2 x,-y,-z             
3 -x,y,-z             
4 -x,-y,z             
5 x+1/2,y+1/2,z+1/2   
6 x+1/2,-y+1/2,-z+1/2 
7 -x+1/2,y+1/2,-z+1/2 
8 -x+1/2,-y+1/2,z+1/2 
# 
loop_
_pdbx_refine_tls.id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][3] 
1 ? 'X-RAY DIFFRACTION' refined 13.8434596619  27.5445884196 31.5583633117 0.291103664511 0.324209144038 0.407334281793 
0.0442001655099  -0.0482925575984  -0.0582581179335 3.93402217799 2.23940198602 7.65351036911 -1.35149142243  -3.10476664419  
0.659641211214  0.0987485027344  -0.240568318576 -0.115793685073 0.00118232064784 -0.0763599834998 -0.146546313404 
0.00504653728721 0.566380681387    -0.125718684171  
2 ? 'X-RAY DIFFRACTION' refined -6.53772573599 38.1787289272 23.5785348203 0.267748747289 0.280023088941 0.296253636154 
0.021497017837   -0.0102278099889  -0.0125602991109 3.76690778614 5.16924159906 6.76320797638 -1.8132859168   1.17899471498   
-3.21305647507  0.0196467898358  0.414990141729  0.232487907329  -0.0781981239009 -0.10552077264   0.119940442331  -0.463540157767 
-0.0284524808985  0.031096480048   
3 ? 'X-RAY DIFFRACTION' refined 4.72890818096  31.2254891041 29.7742703505 0.240886153764 0.230547285374 0.285171590379 
0.0744683957012  -0.0092474842194  -0.0367635160633 4.49133669309 2.31585709589 3.05395606497 0.556487166188  -0.210364859562 
-0.974125058349 -0.0162949689065 -0.294350400146 0.0442230081259 0.032841903519   -0.112495729604  -0.196353343491 0.0519379107949 
0.256335958931    0.125198838169   
4 ? 'X-RAY DIFFRACTION' refined 2.11503460218  27.8343659324 15.3968334193 0.414802641007 0.317533167567 0.330267778518 
0.0308118179282  -0.0126430691717  -0.0938842521246 6.08268765958 3.37654001887 6.33969379294 -2.21432033827  2.54381981681   
-1.81498665081  0.39315492408    0.719134136211  -0.3514610639   -0.566686530472  -0.18960004186   0.117877660332  0.695385197471 
0.336575529357    -0.0874599259418 
5 ? 'X-RAY DIFFRACTION' refined 1.6271905909   23.1065942561 21.4963657989 0.399823376131 0.263787378238 0.344197736899 
0.0161444959146  -0.030049949666   -0.0774405818527 2.60320802549 2.83481919635 3.10153616221 -0.886744977962 -0.898669689989 
-1.55219085889  0.0802762788034  0.386926108573  -0.597024333489 -0.376963211424  -0.0507528873947 0.265005869188  0.474926034904 
-0.0916177621817  -0.0628186680556 
6 ? 'X-RAY DIFFRACTION' refined -5.70275463001 25.2658643635 42.2393643094 0.342318318764 0.426668446904 0.29512155683  
-0.0501748004571 -0.00745517519666 0.0617569646515  6.94146087037 7.76731920837 6.05890449573 -2.01920188768  -1.43777627426  
0.0581502356949 -0.186914401364  -0.855940921799 -0.477221557215 0.819756100642   0.0322326305388  0.132950148522  0.516153849439 
-0.00110292974638 0.0465728544014  
7 ? 'X-RAY DIFFRACTION' refined -13.1471860987 31.1361749865 33.3891670803 0.266760966275 0.370376395181 0.284138076055 
0.0275314976824  -0.0137281409234  0.0427331809883  5.37230632416 6.42309068711 3.146081562   2.5364018923    -0.203788537788 
-0.743738308294 0.0806528915048  -0.430148505374 -0.463071031144 0.536988197872   -0.163570720293  -0.519227217757 
-0.0840393550114 -0.176983064014   0.0204668566604  
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
1 1 'X-RAY DIFFRACTION' A 16  A 1   A 40  A 25  . 
;chain 'A' and (resid 16 through 40 )
;
2 2 'X-RAY DIFFRACTION' A 41  A 26  A 76  A 61  . 
;chain 'A' and (resid 41 through 76 )
;
3 3 'X-RAY DIFFRACTION' A 77  A 62  A 153 A 138 . 
;chain 'A' and (resid 77 through 153 )
;
4 4 'X-RAY DIFFRACTION' A 154 A 139 A 164 A 149 . 
;chain 'A' and (resid 154 through 164 )
;
5 5 'X-RAY DIFFRACTION' A 165 A 150 A 190 A 175 . 
;chain 'A' and (resid 165 through 190 )
;
6 6 'X-RAY DIFFRACTION' A 191 A 176 A 210 A 195 . 
;chain 'A' and (resid 191 through 210 )
;
7 7 'X-RAY DIFFRACTION' A 211 A 196 A 224 A 209 . 
;chain 'A' and (resid 211 through 224 )
;
# 
loop_
_pdbx_distant_solvent_atoms.id 
_pdbx_distant_solvent_atoms.PDB_model_num 
_pdbx_distant_solvent_atoms.auth_atom_id 
_pdbx_distant_solvent_atoms.label_alt_id 
_pdbx_distant_solvent_atoms.auth_asym_id 
_pdbx_distant_solvent_atoms.auth_comp_id 
_pdbx_distant_solvent_atoms.auth_seq_id 
_pdbx_distant_solvent_atoms.PDB_ins_code 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance 
1 1 O ? A HOH 531 ? 6.13 . 
2 1 O ? A HOH 532 ? 6.46 . 
3 1 O ? A HOH 533 ? 7.48 . 
# 
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 
A1AYM C1   C  N N 1   
A1AYM C2   C  Y N 2   
A1AYM C3   C  Y N 3   
A1AYM C4   C  Y N 4   
A1AYM C5   C  Y N 5   
A1AYM C6   C  Y N 6   
A1AYM C7   C  Y N 7   
A1AYM F1   F  N N 8   
A1AYM N1   N  N N 9   
A1AYM N2   N  N N 10  
A1AYM S1   S  N N 11  
A1AYM CL1  CL N N 12  
A1AYM H4   H  N N 13  
A1AYM H5   H  N N 14  
A1AYM H6   H  N N 15  
A1AYM H2   H  N N 16  
A1AYM H1   H  N N 17  
A1AYM H3   H  N N 18  
ALA   N    N  N N 19  
ALA   CA   C  N S 20  
ALA   C    C  N N 21  
ALA   O    O  N N 22  
ALA   CB   C  N N 23  
ALA   OXT  O  N N 24  
ALA   H    H  N N 25  
ALA   H2   H  N N 26  
ALA   HA   H  N N 27  
ALA   HB1  H  N N 28  
ALA   HB2  H  N N 29  
ALA   HB3  H  N N 30  
ALA   HXT  H  N N 31  
ARG   N    N  N N 32  
ARG   CA   C  N S 33  
ARG   C    C  N N 34  
ARG   O    O  N N 35  
ARG   CB   C  N N 36  
ARG   CG   C  N N 37  
ARG   CD   C  N N 38  
ARG   NE   N  N N 39  
ARG   CZ   C  N N 40  
ARG   NH1  N  N N 41  
ARG   NH2  N  N N 42  
ARG   OXT  O  N N 43  
ARG   H    H  N N 44  
ARG   H2   H  N N 45  
ARG   HA   H  N N 46  
ARG   HB2  H  N N 47  
ARG   HB3  H  N N 48  
ARG   HG2  H  N N 49  
ARG   HG3  H  N N 50  
ARG   HD2  H  N N 51  
ARG   HD3  H  N N 52  
ARG   HE   H  N N 53  
ARG   HH11 H  N N 54  
ARG   HH12 H  N N 55  
ARG   HH21 H  N N 56  
ARG   HH22 H  N N 57  
ARG   HXT  H  N N 58  
ASN   N    N  N N 59  
ASN   CA   C  N S 60  
ASN   C    C  N N 61  
ASN   O    O  N N 62  
ASN   CB   C  N N 63  
ASN   CG   C  N N 64  
ASN   OD1  O  N N 65  
ASN   ND2  N  N N 66  
ASN   OXT  O  N N 67  
ASN   H    H  N N 68  
ASN   H2   H  N N 69  
ASN   HA   H  N N 70  
ASN   HB2  H  N N 71  
ASN   HB3  H  N N 72  
ASN   HD21 H  N N 73  
ASN   HD22 H  N N 74  
ASN   HXT  H  N N 75  
ASP   N    N  N N 76  
ASP   CA   C  N S 77  
ASP   C    C  N N 78  
ASP   O    O  N N 79  
ASP   CB   C  N N 80  
ASP   CG   C  N N 81  
ASP   OD1  O  N N 82  
ASP   OD2  O  N N 83  
ASP   OXT  O  N N 84  
ASP   H    H  N N 85  
ASP   H2   H  N N 86  
ASP   HA   H  N N 87  
ASP   HB2  H  N N 88  
ASP   HB3  H  N N 89  
ASP   HD2  H  N N 90  
ASP   HXT  H  N N 91  
GLN   N    N  N N 92  
GLN   CA   C  N S 93  
GLN   C    C  N N 94  
GLN   O    O  N N 95  
GLN   CB   C  N N 96  
GLN   CG   C  N N 97  
GLN   CD   C  N N 98  
GLN   OE1  O  N N 99  
GLN   NE2  N  N N 100 
GLN   OXT  O  N N 101 
GLN   H    H  N N 102 
GLN   H2   H  N N 103 
GLN   HA   H  N N 104 
GLN   HB2  H  N N 105 
GLN   HB3  H  N N 106 
GLN   HG2  H  N N 107 
GLN   HG3  H  N N 108 
GLN   HE21 H  N N 109 
GLN   HE22 H  N N 110 
GLN   HXT  H  N N 111 
GLU   N    N  N N 112 
GLU   CA   C  N S 113 
GLU   C    C  N N 114 
GLU   O    O  N N 115 
GLU   CB   C  N N 116 
GLU   CG   C  N N 117 
GLU   CD   C  N N 118 
GLU   OE1  O  N N 119 
GLU   OE2  O  N N 120 
GLU   OXT  O  N N 121 
GLU   H    H  N N 122 
GLU   H2   H  N N 123 
GLU   HA   H  N N 124 
GLU   HB2  H  N N 125 
GLU   HB3  H  N N 126 
GLU   HG2  H  N N 127 
GLU   HG3  H  N N 128 
GLU   HE2  H  N N 129 
GLU   HXT  H  N N 130 
GLY   N    N  N N 131 
GLY   CA   C  N N 132 
GLY   C    C  N N 133 
GLY   O    O  N N 134 
GLY   OXT  O  N N 135 
GLY   H    H  N N 136 
GLY   H2   H  N N 137 
GLY   HA2  H  N N 138 
GLY   HA3  H  N N 139 
GLY   HXT  H  N N 140 
HIS   N    N  N N 141 
HIS   CA   C  N S 142 
HIS   C    C  N N 143 
HIS   O    O  N N 144 
HIS   CB   C  N N 145 
HIS   CG   C  Y N 146 
HIS   ND1  N  Y N 147 
HIS   CD2  C  Y N 148 
HIS   CE1  C  Y N 149 
HIS   NE2  N  Y N 150 
HIS   OXT  O  N N 151 
HIS   H    H  N N 152 
HIS   H2   H  N N 153 
HIS   HA   H  N N 154 
HIS   HB2  H  N N 155 
HIS   HB3  H  N N 156 
HIS   HD1  H  N N 157 
HIS   HD2  H  N N 158 
HIS   HE1  H  N N 159 
HIS   HE2  H  N N 160 
HIS   HXT  H  N N 161 
HOH   O    O  N N 162 
HOH   H1   H  N N 163 
HOH   H2   H  N N 164 
ILE   N    N  N N 165 
ILE   CA   C  N S 166 
ILE   C    C  N N 167 
ILE   O    O  N N 168 
ILE   CB   C  N S 169 
ILE   CG1  C  N N 170 
ILE   CG2  C  N N 171 
ILE   CD1  C  N N 172 
ILE   OXT  O  N N 173 
ILE   H    H  N N 174 
ILE   H2   H  N N 175 
ILE   HA   H  N N 176 
ILE   HB   H  N N 177 
ILE   HG12 H  N N 178 
ILE   HG13 H  N N 179 
ILE   HG21 H  N N 180 
ILE   HG22 H  N N 181 
ILE   HG23 H  N N 182 
ILE   HD11 H  N N 183 
ILE   HD12 H  N N 184 
ILE   HD13 H  N N 185 
ILE   HXT  H  N N 186 
LEU   N    N  N N 187 
LEU   CA   C  N S 188 
LEU   C    C  N N 189 
LEU   O    O  N N 190 
LEU   CB   C  N N 191 
LEU   CG   C  N N 192 
LEU   CD1  C  N N 193 
LEU   CD2  C  N N 194 
LEU   OXT  O  N N 195 
LEU   H    H  N N 196 
LEU   H2   H  N N 197 
LEU   HA   H  N N 198 
LEU   HB2  H  N N 199 
LEU   HB3  H  N N 200 
LEU   HG   H  N N 201 
LEU   HD11 H  N N 202 
LEU   HD12 H  N N 203 
LEU   HD13 H  N N 204 
LEU   HD21 H  N N 205 
LEU   HD22 H  N N 206 
LEU   HD23 H  N N 207 
LEU   HXT  H  N N 208 
LYS   N    N  N N 209 
LYS   CA   C  N S 210 
LYS   C    C  N N 211 
LYS   O    O  N N 212 
LYS   CB   C  N N 213 
LYS   CG   C  N N 214 
LYS   CD   C  N N 215 
LYS   CE   C  N N 216 
LYS   NZ   N  N N 217 
LYS   OXT  O  N N 218 
LYS   H    H  N N 219 
LYS   H2   H  N N 220 
LYS   HA   H  N N 221 
LYS   HB2  H  N N 222 
LYS   HB3  H  N N 223 
LYS   HG2  H  N N 224 
LYS   HG3  H  N N 225 
LYS   HD2  H  N N 226 
LYS   HD3  H  N N 227 
LYS   HE2  H  N N 228 
LYS   HE3  H  N N 229 
LYS   HZ1  H  N N 230 
LYS   HZ2  H  N N 231 
LYS   HZ3  H  N N 232 
LYS   HXT  H  N N 233 
MET   N    N  N N 234 
MET   CA   C  N S 235 
MET   C    C  N N 236 
MET   O    O  N N 237 
MET   CB   C  N N 238 
MET   CG   C  N N 239 
MET   SD   S  N N 240 
MET   CE   C  N N 241 
MET   OXT  O  N N 242 
MET   H    H  N N 243 
MET   H2   H  N N 244 
MET   HA   H  N N 245 
MET   HB2  H  N N 246 
MET   HB3  H  N N 247 
MET   HG2  H  N N 248 
MET   HG3  H  N N 249 
MET   HE1  H  N N 250 
MET   HE2  H  N N 251 
MET   HE3  H  N N 252 
MET   HXT  H  N N 253 
PHE   N    N  N N 254 
PHE   CA   C  N S 255 
PHE   C    C  N N 256 
PHE   O    O  N N 257 
PHE   CB   C  N N 258 
PHE   CG   C  Y N 259 
PHE   CD1  C  Y N 260 
PHE   CD2  C  Y N 261 
PHE   CE1  C  Y N 262 
PHE   CE2  C  Y N 263 
PHE   CZ   C  Y N 264 
PHE   OXT  O  N N 265 
PHE   H    H  N N 266 
PHE   H2   H  N N 267 
PHE   HA   H  N N 268 
PHE   HB2  H  N N 269 
PHE   HB3  H  N N 270 
PHE   HD1  H  N N 271 
PHE   HD2  H  N N 272 
PHE   HE1  H  N N 273 
PHE   HE2  H  N N 274 
PHE   HZ   H  N N 275 
PHE   HXT  H  N N 276 
PRO   N    N  N N 277 
PRO   CA   C  N S 278 
PRO   C    C  N N 279 
PRO   O    O  N N 280 
PRO   CB   C  N N 281 
PRO   CG   C  N N 282 
PRO   CD   C  N N 283 
PRO   OXT  O  N N 284 
PRO   H    H  N N 285 
PRO   HA   H  N N 286 
PRO   HB2  H  N N 287 
PRO   HB3  H  N N 288 
PRO   HG2  H  N N 289 
PRO   HG3  H  N N 290 
PRO   HD2  H  N N 291 
PRO   HD3  H  N N 292 
PRO   HXT  H  N N 293 
SER   N    N  N N 294 
SER   CA   C  N S 295 
SER   C    C  N N 296 
SER   O    O  N N 297 
SER   CB   C  N N 298 
SER   OG   O  N N 299 
SER   OXT  O  N N 300 
SER   H    H  N N 301 
SER   H2   H  N N 302 
SER   HA   H  N N 303 
SER   HB2  H  N N 304 
SER   HB3  H  N N 305 
SER   HG   H  N N 306 
SER   HXT  H  N N 307 
THR   N    N  N N 308 
THR   CA   C  N S 309 
THR   C    C  N N 310 
THR   O    O  N N 311 
THR   CB   C  N R 312 
THR   OG1  O  N N 313 
THR   CG2  C  N N 314 
THR   OXT  O  N N 315 
THR   H    H  N N 316 
THR   H2   H  N N 317 
THR   HA   H  N N 318 
THR   HB   H  N N 319 
THR   HG1  H  N N 320 
THR   HG21 H  N N 321 
THR   HG22 H  N N 322 
THR   HG23 H  N N 323 
THR   HXT  H  N N 324 
TRP   N    N  N N 325 
TRP   CA   C  N S 326 
TRP   C    C  N N 327 
TRP   O    O  N N 328 
TRP   CB   C  N N 329 
TRP   CG   C  Y N 330 
TRP   CD1  C  Y N 331 
TRP   CD2  C  Y N 332 
TRP   NE1  N  Y N 333 
TRP   CE2  C  Y N 334 
TRP   CE3  C  Y N 335 
TRP   CZ2  C  Y N 336 
TRP   CZ3  C  Y N 337 
TRP   CH2  C  Y N 338 
TRP   OXT  O  N N 339 
TRP   H    H  N N 340 
TRP   H2   H  N N 341 
TRP   HA   H  N N 342 
TRP   HB2  H  N N 343 
TRP   HB3  H  N N 344 
TRP   HD1  H  N N 345 
TRP   HE1  H  N N 346 
TRP   HE3  H  N N 347 
TRP   HZ2  H  N N 348 
TRP   HZ3  H  N N 349 
TRP   HH2  H  N N 350 
TRP   HXT  H  N N 351 
TYR   N    N  N N 352 
TYR   CA   C  N S 353 
TYR   C    C  N N 354 
TYR   O    O  N N 355 
TYR   CB   C  N N 356 
TYR   CG   C  Y N 357 
TYR   CD1  C  Y N 358 
TYR   CD2  C  Y N 359 
TYR   CE1  C  Y N 360 
TYR   CE2  C  Y N 361 
TYR   CZ   C  Y N 362 
TYR   OH   O  N N 363 
TYR   OXT  O  N N 364 
TYR   H    H  N N 365 
TYR   H2   H  N N 366 
TYR   HA   H  N N 367 
TYR   HB2  H  N N 368 
TYR   HB3  H  N N 369 
TYR   HD1  H  N N 370 
TYR   HD2  H  N N 371 
TYR   HE1  H  N N 372 
TYR   HE2  H  N N 373 
TYR   HH   H  N N 374 
TYR   HXT  H  N N 375 
VAL   N    N  N N 376 
VAL   CA   C  N S 377 
VAL   C    C  N N 378 
VAL   O    O  N N 379 
VAL   CB   C  N N 380 
VAL   CG1  C  N N 381 
VAL   CG2  C  N N 382 
VAL   OXT  O  N N 383 
VAL   H    H  N N 384 
VAL   H2   H  N N 385 
VAL   HA   H  N N 386 
VAL   HB   H  N N 387 
VAL   HG11 H  N N 388 
VAL   HG12 H  N N 389 
VAL   HG13 H  N N 390 
VAL   HG21 H  N N 391 
VAL   HG22 H  N N 392 
VAL   HG23 H  N N 393 
VAL   HXT  H  N N 394 
# 
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 
A1AYM N1  C1   sing N N 1   
A1AYM C1  S1   doub N N 2   
A1AYM C1  N2   sing N N 3   
A1AYM N2  C2   sing N N 4   
A1AYM C2  C3   doub Y N 5   
A1AYM C3  C4   sing Y N 6   
A1AYM C4  C5   doub Y N 7   
A1AYM C5  F1   sing N N 8   
A1AYM C5  C6   sing Y N 9   
A1AYM C6  CL1  sing N N 10  
A1AYM C6  C7   doub Y N 11  
A1AYM C2  C7   sing Y N 12  
A1AYM C3  H4   sing N N 13  
A1AYM C4  H5   sing N N 14  
A1AYM C7  H6   sing N N 15  
A1AYM N1  H2   sing N N 16  
A1AYM N1  H1   sing N N 17  
A1AYM N2  H3   sing N N 18  
ALA   N   CA   sing N N 19  
ALA   N   H    sing N N 20  
ALA   N   H2   sing N N 21  
ALA   CA  C    sing N N 22  
ALA   CA  CB   sing N N 23  
ALA   CA  HA   sing N N 24  
ALA   C   O    doub N N 25  
ALA   C   OXT  sing N N 26  
ALA   CB  HB1  sing N N 27  
ALA   CB  HB2  sing N N 28  
ALA   CB  HB3  sing N N 29  
ALA   OXT HXT  sing N N 30  
ARG   N   CA   sing N N 31  
ARG   N   H    sing N N 32  
ARG   N   H2   sing N N 33  
ARG   CA  C    sing N N 34  
ARG   CA  CB   sing N N 35  
ARG   CA  HA   sing N N 36  
ARG   C   O    doub N N 37  
ARG   C   OXT  sing N N 38  
ARG   CB  CG   sing N N 39  
ARG   CB  HB2  sing N N 40  
ARG   CB  HB3  sing N N 41  
ARG   CG  CD   sing N N 42  
ARG   CG  HG2  sing N N 43  
ARG   CG  HG3  sing N N 44  
ARG   CD  NE   sing N N 45  
ARG   CD  HD2  sing N N 46  
ARG   CD  HD3  sing N N 47  
ARG   NE  CZ   sing N N 48  
ARG   NE  HE   sing N N 49  
ARG   CZ  NH1  sing N N 50  
ARG   CZ  NH2  doub N N 51  
ARG   NH1 HH11 sing N N 52  
ARG   NH1 HH12 sing N N 53  
ARG   NH2 HH21 sing N N 54  
ARG   NH2 HH22 sing N N 55  
ARG   OXT HXT  sing N N 56  
ASN   N   CA   sing N N 57  
ASN   N   H    sing N N 58  
ASN   N   H2   sing N N 59  
ASN   CA  C    sing N N 60  
ASN   CA  CB   sing N N 61  
ASN   CA  HA   sing N N 62  
ASN   C   O    doub N N 63  
ASN   C   OXT  sing N N 64  
ASN   CB  CG   sing N N 65  
ASN   CB  HB2  sing N N 66  
ASN   CB  HB3  sing N N 67  
ASN   CG  OD1  doub N N 68  
ASN   CG  ND2  sing N N 69  
ASN   ND2 HD21 sing N N 70  
ASN   ND2 HD22 sing N N 71  
ASN   OXT HXT  sing N N 72  
ASP   N   CA   sing N N 73  
ASP   N   H    sing N N 74  
ASP   N   H2   sing N N 75  
ASP   CA  C    sing N N 76  
ASP   CA  CB   sing N N 77  
ASP   CA  HA   sing N N 78  
ASP   C   O    doub N N 79  
ASP   C   OXT  sing N N 80  
ASP   CB  CG   sing N N 81  
ASP   CB  HB2  sing N N 82  
ASP   CB  HB3  sing N N 83  
ASP   CG  OD1  doub N N 84  
ASP   CG  OD2  sing N N 85  
ASP   OD2 HD2  sing N N 86  
ASP   OXT HXT  sing N N 87  
GLN   N   CA   sing N N 88  
GLN   N   H    sing N N 89  
GLN   N   H2   sing N N 90  
GLN   CA  C    sing N N 91  
GLN   CA  CB   sing N N 92  
GLN   CA  HA   sing N N 93  
GLN   C   O    doub N N 94  
GLN   C   OXT  sing N N 95  
GLN   CB  CG   sing N N 96  
GLN   CB  HB2  sing N N 97  
GLN   CB  HB3  sing N N 98  
GLN   CG  CD   sing N N 99  
GLN   CG  HG2  sing N N 100 
GLN   CG  HG3  sing N N 101 
GLN   CD  OE1  doub N N 102 
GLN   CD  NE2  sing N N 103 
GLN   NE2 HE21 sing N N 104 
GLN   NE2 HE22 sing N N 105 
GLN   OXT HXT  sing N N 106 
GLU   N   CA   sing N N 107 
GLU   N   H    sing N N 108 
GLU   N   H2   sing N N 109 
GLU   CA  C    sing N N 110 
GLU   CA  CB   sing N N 111 
GLU   CA  HA   sing N N 112 
GLU   C   O    doub N N 113 
GLU   C   OXT  sing N N 114 
GLU   CB  CG   sing N N 115 
GLU   CB  HB2  sing N N 116 
GLU   CB  HB3  sing N N 117 
GLU   CG  CD   sing N N 118 
GLU   CG  HG2  sing N N 119 
GLU   CG  HG3  sing N N 120 
GLU   CD  OE1  doub N N 121 
GLU   CD  OE2  sing N N 122 
GLU   OE2 HE2  sing N N 123 
GLU   OXT HXT  sing N N 124 
GLY   N   CA   sing N N 125 
GLY   N   H    sing N N 126 
GLY   N   H2   sing N N 127 
GLY   CA  C    sing N N 128 
GLY   CA  HA2  sing N N 129 
GLY   CA  HA3  sing N N 130 
GLY   C   O    doub N N 131 
GLY   C   OXT  sing N N 132 
GLY   OXT HXT  sing N N 133 
HIS   N   CA   sing N N 134 
HIS   N   H    sing N N 135 
HIS   N   H2   sing N N 136 
HIS   CA  C    sing N N 137 
HIS   CA  CB   sing N N 138 
HIS   CA  HA   sing N N 139 
HIS   C   O    doub N N 140 
HIS   C   OXT  sing N N 141 
HIS   CB  CG   sing N N 142 
HIS   CB  HB2  sing N N 143 
HIS   CB  HB3  sing N N 144 
HIS   CG  ND1  sing Y N 145 
HIS   CG  CD2  doub Y N 146 
HIS   ND1 CE1  doub Y N 147 
HIS   ND1 HD1  sing N N 148 
HIS   CD2 NE2  sing Y N 149 
HIS   CD2 HD2  sing N N 150 
HIS   CE1 NE2  sing Y N 151 
HIS   CE1 HE1  sing N N 152 
HIS   NE2 HE2  sing N N 153 
HIS   OXT HXT  sing N N 154 
HOH   O   H1   sing N N 155 
HOH   O   H2   sing N N 156 
ILE   N   CA   sing N N 157 
ILE   N   H    sing N N 158 
ILE   N   H2   sing N N 159 
ILE   CA  C    sing N N 160 
ILE   CA  CB   sing N N 161 
ILE   CA  HA   sing N N 162 
ILE   C   O    doub N N 163 
ILE   C   OXT  sing N N 164 
ILE   CB  CG1  sing N N 165 
ILE   CB  CG2  sing N N 166 
ILE   CB  HB   sing N N 167 
ILE   CG1 CD1  sing N N 168 
ILE   CG1 HG12 sing N N 169 
ILE   CG1 HG13 sing N N 170 
ILE   CG2 HG21 sing N N 171 
ILE   CG2 HG22 sing N N 172 
ILE   CG2 HG23 sing N N 173 
ILE   CD1 HD11 sing N N 174 
ILE   CD1 HD12 sing N N 175 
ILE   CD1 HD13 sing N N 176 
ILE   OXT HXT  sing N N 177 
LEU   N   CA   sing N N 178 
LEU   N   H    sing N N 179 
LEU   N   H2   sing N N 180 
LEU   CA  C    sing N N 181 
LEU   CA  CB   sing N N 182 
LEU   CA  HA   sing N N 183 
LEU   C   O    doub N N 184 
LEU   C   OXT  sing N N 185 
LEU   CB  CG   sing N N 186 
LEU   CB  HB2  sing N N 187 
LEU   CB  HB3  sing N N 188 
LEU   CG  CD1  sing N N 189 
LEU   CG  CD2  sing N N 190 
LEU   CG  HG   sing N N 191 
LEU   CD1 HD11 sing N N 192 
LEU   CD1 HD12 sing N N 193 
LEU   CD1 HD13 sing N N 194 
LEU   CD2 HD21 sing N N 195 
LEU   CD2 HD22 sing N N 196 
LEU   CD2 HD23 sing N N 197 
LEU   OXT HXT  sing N N 198 
LYS   N   CA   sing N N 199 
LYS   N   H    sing N N 200 
LYS   N   H2   sing N N 201 
LYS   CA  C    sing N N 202 
LYS   CA  CB   sing N N 203 
LYS   CA  HA   sing N N 204 
LYS   C   O    doub N N 205 
LYS   C   OXT  sing N N 206 
LYS   CB  CG   sing N N 207 
LYS   CB  HB2  sing N N 208 
LYS   CB  HB3  sing N N 209 
LYS   CG  CD   sing N N 210 
LYS   CG  HG2  sing N N 211 
LYS   CG  HG3  sing N N 212 
LYS   CD  CE   sing N N 213 
LYS   CD  HD2  sing N N 214 
LYS   CD  HD3  sing N N 215 
LYS   CE  NZ   sing N N 216 
LYS   CE  HE2  sing N N 217 
LYS   CE  HE3  sing N N 218 
LYS   NZ  HZ1  sing N N 219 
LYS   NZ  HZ2  sing N N 220 
LYS   NZ  HZ3  sing N N 221 
LYS   OXT HXT  sing N N 222 
MET   N   CA   sing N N 223 
MET   N   H    sing N N 224 
MET   N   H2   sing N N 225 
MET   CA  C    sing N N 226 
MET   CA  CB   sing N N 227 
MET   CA  HA   sing N N 228 
MET   C   O    doub N N 229 
MET   C   OXT  sing N N 230 
MET   CB  CG   sing N N 231 
MET   CB  HB2  sing N N 232 
MET   CB  HB3  sing N N 233 
MET   CG  SD   sing N N 234 
MET   CG  HG2  sing N N 235 
MET   CG  HG3  sing N N 236 
MET   SD  CE   sing N N 237 
MET   CE  HE1  sing N N 238 
MET   CE  HE2  sing N N 239 
MET   CE  HE3  sing N N 240 
MET   OXT HXT  sing N N 241 
PHE   N   CA   sing N N 242 
PHE   N   H    sing N N 243 
PHE   N   H2   sing N N 244 
PHE   CA  C    sing N N 245 
PHE   CA  CB   sing N N 246 
PHE   CA  HA   sing N N 247 
PHE   C   O    doub N N 248 
PHE   C   OXT  sing N N 249 
PHE   CB  CG   sing N N 250 
PHE   CB  HB2  sing N N 251 
PHE   CB  HB3  sing N N 252 
PHE   CG  CD1  doub Y N 253 
PHE   CG  CD2  sing Y N 254 
PHE   CD1 CE1  sing Y N 255 
PHE   CD1 HD1  sing N N 256 
PHE   CD2 CE2  doub Y N 257 
PHE   CD2 HD2  sing N N 258 
PHE   CE1 CZ   doub Y N 259 
PHE   CE1 HE1  sing N N 260 
PHE   CE2 CZ   sing Y N 261 
PHE   CE2 HE2  sing N N 262 
PHE   CZ  HZ   sing N N 263 
PHE   OXT HXT  sing N N 264 
PRO   N   CA   sing N N 265 
PRO   N   CD   sing N N 266 
PRO   N   H    sing N N 267 
PRO   CA  C    sing N N 268 
PRO   CA  CB   sing N N 269 
PRO   CA  HA   sing N N 270 
PRO   C   O    doub N N 271 
PRO   C   OXT  sing N N 272 
PRO   CB  CG   sing N N 273 
PRO   CB  HB2  sing N N 274 
PRO   CB  HB3  sing N N 275 
PRO   CG  CD   sing N N 276 
PRO   CG  HG2  sing N N 277 
PRO   CG  HG3  sing N N 278 
PRO   CD  HD2  sing N N 279 
PRO   CD  HD3  sing N N 280 
PRO   OXT HXT  sing N N 281 
SER   N   CA   sing N N 282 
SER   N   H    sing N N 283 
SER   N   H2   sing N N 284 
SER   CA  C    sing N N 285 
SER   CA  CB   sing N N 286 
SER   CA  HA   sing N N 287 
SER   C   O    doub N N 288 
SER   C   OXT  sing N N 289 
SER   CB  OG   sing N N 290 
SER   CB  HB2  sing N N 291 
SER   CB  HB3  sing N N 292 
SER   OG  HG   sing N N 293 
SER   OXT HXT  sing N N 294 
THR   N   CA   sing N N 295 
THR   N   H    sing N N 296 
THR   N   H2   sing N N 297 
THR   CA  C    sing N N 298 
THR   CA  CB   sing N N 299 
THR   CA  HA   sing N N 300 
THR   C   O    doub N N 301 
THR   C   OXT  sing N N 302 
THR   CB  OG1  sing N N 303 
THR   CB  CG2  sing N N 304 
THR   CB  HB   sing N N 305 
THR   OG1 HG1  sing N N 306 
THR   CG2 HG21 sing N N 307 
THR   CG2 HG22 sing N N 308 
THR   CG2 HG23 sing N N 309 
THR   OXT HXT  sing N N 310 
TRP   N   CA   sing N N 311 
TRP   N   H    sing N N 312 
TRP   N   H2   sing N N 313 
TRP   CA  C    sing N N 314 
TRP   CA  CB   sing N N 315 
TRP   CA  HA   sing N N 316 
TRP   C   O    doub N N 317 
TRP   C   OXT  sing N N 318 
TRP   CB  CG   sing N N 319 
TRP   CB  HB2  sing N N 320 
TRP   CB  HB3  sing N N 321 
TRP   CG  CD1  doub Y N 322 
TRP   CG  CD2  sing Y N 323 
TRP   CD1 NE1  sing Y N 324 
TRP   CD1 HD1  sing N N 325 
TRP   CD2 CE2  doub Y N 326 
TRP   CD2 CE3  sing Y N 327 
TRP   NE1 CE2  sing Y N 328 
TRP   NE1 HE1  sing N N 329 
TRP   CE2 CZ2  sing Y N 330 
TRP   CE3 CZ3  doub Y N 331 
TRP   CE3 HE3  sing N N 332 
TRP   CZ2 CH2  doub Y N 333 
TRP   CZ2 HZ2  sing N N 334 
TRP   CZ3 CH2  sing Y N 335 
TRP   CZ3 HZ3  sing N N 336 
TRP   CH2 HH2  sing N N 337 
TRP   OXT HXT  sing N N 338 
TYR   N   CA   sing N N 339 
TYR   N   H    sing N N 340 
TYR   N   H2   sing N N 341 
TYR   CA  C    sing N N 342 
TYR   CA  CB   sing N N 343 
TYR   CA  HA   sing N N 344 
TYR   C   O    doub N N 345 
TYR   C   OXT  sing N N 346 
TYR   CB  CG   sing N N 347 
TYR   CB  HB2  sing N N 348 
TYR   CB  HB3  sing N N 349 
TYR   CG  CD1  doub Y N 350 
TYR   CG  CD2  sing Y N 351 
TYR   CD1 CE1  sing Y N 352 
TYR   CD1 HD1  sing N N 353 
TYR   CD2 CE2  doub Y N 354 
TYR   CD2 HD2  sing N N 355 
TYR   CE1 CZ   doub Y N 356 
TYR   CE1 HE1  sing N N 357 
TYR   CE2 CZ   sing Y N 358 
TYR   CE2 HE2  sing N N 359 
TYR   CZ  OH   sing N N 360 
TYR   OH  HH   sing N N 361 
TYR   OXT HXT  sing N N 362 
VAL   N   CA   sing N N 363 
VAL   N   H    sing N N 364 
VAL   N   H2   sing N N 365 
VAL   CA  C    sing N N 366 
VAL   CA  CB   sing N N 367 
VAL   CA  HA   sing N N 368 
VAL   C   O    doub N N 369 
VAL   C   OXT  sing N N 370 
VAL   CB  CG1  sing N N 371 
VAL   CB  CG2  sing N N 372 
VAL   CB  HB   sing N N 373 
VAL   CG1 HG11 sing N N 374 
VAL   CG1 HG12 sing N N 375 
VAL   CG1 HG13 sing N N 376 
VAL   CG2 HG21 sing N N 377 
VAL   CG2 HG22 sing N N 378 
VAL   CG2 HG23 sing N N 379 
VAL   OXT HXT  sing N N 380 
# 
_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                    7HB3 
_atom_sites.fract_transf_matrix[1][1]   0.014380 
_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]   0.011101 
_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]   0.010130 
_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.
;
? 
CL ? ? 9.50761 7.44341 ? ? 1.04373  23.83732 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
F  ? ? 8.95735 ?       ? ? 7.27484  ?        ? ? 0.0 
;1-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   ? 7.88990   16.22552 11.13935 1.000 73.51793  ? 16  GLU   A N   1 
ATOM   2    C  CA  . GLU   A 1 9   ? 9.21359   16.83707 11.10774 1.000 64.99872  ? 16  GLU   A CA  1 
ATOM   3    C  C   . GLU   A 1 9   ? 9.39499   17.85090 12.22849 1.000 62.93507  ? 16  GLU   A C   1 
ATOM   4    O  O   . GLU   A 1 9   ? 8.82664   18.94197 12.18847 1.000 65.85772  ? 16  GLU   A O   1 
ATOM   5    C  CB  . GLU   A 1 9   ? 9.45939   17.50926 9.75513  1.000 76.71929  ? 16  GLU   A CB  1 
ATOM   6    C  CG  . GLU   A 1 9   ? 10.91953  17.88206 9.44337  1.000 84.31351  ? 16  GLU   A CG  1 
ATOM   7    C  CD  . GLU   A 1 9   ? 11.90738  16.70990 9.39539  1.000 95.35268  ? 16  GLU   A CD  1 
ATOM   8    O  OE1 . GLU   A 1 9   ? 11.62193  15.60690 9.90736  1.000 90.67737  ? 16  GLU   A OE1 1 
ATOM   9    O  OE2 . GLU   A 1 9   ? 12.99956  16.90659 8.82270  1.000 108.36538 ? 16  GLU   A OE2 1 
ATOM   10   N  N   . VAL   A 1 10  ? 10.20718  17.48963 13.21884 1.000 54.14257  ? 17  VAL   A N   1 
ATOM   11   C  CA  . VAL   A 1 10  ? 10.38588  18.26898 14.43900 1.000 47.43101  ? 17  VAL   A CA  1 
ATOM   12   C  C   . VAL   A 1 10  ? 11.74874  18.94655 14.40221 1.000 46.42730  ? 17  VAL   A C   1 
ATOM   13   O  O   . VAL   A 1 10  ? 12.77271  18.28745 14.17892 1.000 45.96689  ? 17  VAL   A O   1 
ATOM   14   C  CB  . VAL   A 1 10  ? 10.25273  17.37973 15.68670 1.000 47.32231  ? 17  VAL   A CB  1 
ATOM   15   C  CG1 . VAL   A 1 10  ? 9.93415   18.21430 16.90486 1.000 45.01202  ? 17  VAL   A CG1 1 
ATOM   16   C  CG2 . VAL   A 1 10  ? 9.17805   16.33164 15.46684 1.000 50.85985  ? 17  VAL   A CG2 1 
ATOM   17   N  N   . GLU   A 1 11  ? 11.76387  20.25708 14.63496 1.000 42.97573  ? 18  GLU   A N   1 
ATOM   18   C  CA  . GLU   A 1 11  ? 13.00277  21.01135 14.76907 1.000 48.06754  ? 18  GLU   A CA  1 
ATOM   19   C  C   . GLU   A 1 11  ? 13.28029  21.28904 16.23868 1.000 38.75131  ? 18  GLU   A C   1 
ATOM   20   O  O   . GLU   A 1 11  ? 12.37359  21.65214 16.99215 1.000 37.75992  ? 18  GLU   A O   1 
ATOM   21   C  CB  . GLU   A 1 11  ? 12.93409  22.32681 13.99359 1.000 40.93548  ? 18  GLU   A CB  1 
ATOM   22   C  CG  . GLU   A 1 11  ? 12.74906  22.13545 12.49269 1.000 47.04848  ? 18  GLU   A CG  1 
ATOM   23   C  CD  . GLU   A 1 11  ? 12.78017  23.44449 11.73319 1.000 53.21543  ? 18  GLU   A CD  1 
ATOM   24   O  OE1 . GLU   A 1 11  ? 11.92399  24.31437 12.01506 1.000 56.45995  ? 18  GLU   A OE1 1 
ATOM   25   O  OE2 . GLU   A 1 11  ? 13.65895  23.59745 10.85701 1.000 61.99411  ? 18  GLU   A OE2 1 
ATOM   26   N  N   . THR   A 1 12  ? 14.53472  21.11527 16.64147 1.000 38.18014  ? 19  THR   A N   1 
ATOM   27   C  CA  . THR   A 1 12  ? 14.94793  21.31764 18.02236 1.000 36.45052  ? 19  THR   A CA  1 
ATOM   28   C  C   . THR   A 1 12  ? 15.84761  22.54146 18.11001 1.000 35.26546  ? 19  THR   A C   1 
ATOM   29   O  O   . THR   A 1 12  ? 16.82438  22.65878 17.36215 1.000 37.36666  ? 19  THR   A O   1 
ATOM   30   C  CB  . THR   A 1 12  ? 15.67270  20.08604 18.57267 1.000 37.47846  ? 19  THR   A CB  1 
ATOM   31   O  OG1 . THR   A 1 12  ? 14.82150  18.93455 18.47523 1.000 39.17391  ? 19  THR   A OG1 1 
ATOM   32   C  CG2 . THR   A 1 12  ? 16.05997  20.29863 20.03572 1.000 36.09264  ? 19  THR   A CG2 1 
ATOM   33   N  N   . PHE   A 1 13  ? 15.51532  23.44232 19.02465 1.000 34.81204  ? 20  PHE   A N   1 
ATOM   34   C  CA  . PHE   A 1 13  ? 16.23432  24.68866 19.21467 1.000 34.37892  ? 20  PHE   A CA  1 
ATOM   35   C  C   . PHE   A 1 13  ? 16.72174  24.77852 20.65074 1.000 33.58457  ? 20  PHE   A C   1 
ATOM   36   O  O   . PHE   A 1 13  ? 16.08752  24.25690 21.57028 1.000 34.41689  ? 20  PHE   A O   1 
ATOM   37   C  CB  . PHE   A 1 13  ? 15.34587  25.90644 18.91061 1.000 32.54365  ? 20  PHE   A CB  1 
ATOM   38   C  CG  . PHE   A 1 13  ? 14.72162  25.88917 17.53989 1.000 37.10676  ? 20  PHE   A CG  1 
ATOM   39   C  CD1 . PHE   A 1 13  ? 13.48024  25.30319 17.33185 1.000 34.34289  ? 20  PHE   A CD1 1 
ATOM   40   C  CD2 . PHE   A 1 13  ? 15.37840  26.45965 16.46144 1.000 35.04615  ? 20  PHE   A CD2 1 
ATOM   41   C  CE1 . PHE   A 1 13  ? 12.90755  25.28974 16.07778 1.000 36.05946  ? 20  PHE   A CE1 1 
ATOM   42   C  CE2 . PHE   A 1 13  ? 14.81088  26.44771 15.20346 1.000 41.17922  ? 20  PHE   A CE2 1 
ATOM   43   C  CZ  . PHE   A 1 13  ? 13.57374  25.86163 15.01000 1.000 39.70742  ? 20  PHE   A CZ  1 
ATOM   44   N  N   . ALA   A 1 14  ? 17.85063  25.45014 20.83809 1.000 40.24752  ? 21  ALA   A N   1 
ATOM   45   C  CA  . ALA   A 1 14  ? 18.33289  25.76708 22.17354 1.000 37.03917  ? 21  ALA   A CA  1 
ATOM   46   C  C   . ALA   A 1 14  ? 17.74667  27.09789 22.62766 1.000 37.15990  ? 21  ALA   A C   1 
ATOM   47   O  O   . ALA   A 1 14  ? 17.68692  28.06115 21.85778 1.000 31.45892  ? 21  ALA   A O   1 
ATOM   48   C  CB  . ALA   A 1 14  ? 19.86240  25.82254 22.20833 1.000 33.39556  ? 21  ALA   A CB  1 
ATOM   49   N  N   . PHE   A 1 15  ? 17.27813  27.12998 23.87146 1.000 33.58551  ? 22  PHE   A N   1 
ATOM   50   C  CA  . PHE   A 1 15  ? 16.89918  28.38826 24.48781 1.000 33.27266  ? 22  PHE   A CA  1 
ATOM   51   C  C   . PHE   A 1 15  ? 18.08447  29.34217 24.48842 1.000 41.40342  ? 22  PHE   A C   1 
ATOM   52   O  O   . PHE   A 1 15  ? 19.24696  28.92610 24.50946 1.000 40.90863  ? 22  PHE   A O   1 
ATOM   53   C  CB  . PHE   A 1 15  ? 16.42881  28.16207 25.92533 1.000 37.47514  ? 22  PHE   A CB  1 
ATOM   54   C  CG  . PHE   A 1 15  ? 14.99417  27.75964 26.03612 1.000 33.96547  ? 22  PHE   A CG  1 
ATOM   55   C  CD1 . PHE   A 1 15  ? 13.98650  28.62112 25.63551 1.000 30.95799  ? 22  PHE   A CD1 1 
ATOM   56   C  CD2 . PHE   A 1 15  ? 14.65182  26.52018 26.53862 1.000 29.83526  ? 22  PHE   A CD2 1 
ATOM   57   C  CE1 . PHE   A 1 15  ? 12.66127  28.25205 25.73789 1.000 31.97408  ? 22  PHE   A CE1 1 
ATOM   58   C  CE2 . PHE   A 1 15  ? 13.33038  26.14374 26.63920 1.000 31.81893  ? 22  PHE   A CE2 1 
ATOM   59   C  CZ  . PHE   A 1 15  ? 12.33431  27.00849 26.24065 1.000 28.54610  ? 22  PHE   A CZ  1 
ATOM   60   N  N   . GLN   A 1 16  ? 17.78443  30.63518 24.46816 1.000 44.76893  ? 23  GLN   A N   1 
ATOM   61   C  CA  . GLN   A 1 16  ? 18.82141  31.61418 24.73861 1.000 44.36604  ? 23  GLN   A CA  1 
ATOM   62   C  C   . GLN   A 1 16  ? 19.32739  31.45002 26.16730 1.000 46.36426  ? 23  GLN   A C   1 
ATOM   63   O  O   . GLN   A 1 16  ? 18.58470  31.05434 27.07110 1.000 43.05581  ? 23  GLN   A O   1 
ATOM   64   C  CB  . GLN   A 1 16  ? 18.29355  33.02349 24.50688 1.000 44.16389  ? 23  GLN   A CB  1 
ATOM   65   C  CG  . GLN   A 1 16  ? 18.87070  33.65380 23.25926 1.000 54.28649  ? 23  GLN   A CG  1 
ATOM   66   C  CD  . GLN   A 1 16  ? 17.98574  34.72888 22.70372 1.000 56.97011  ? 23  GLN   A CD  1 
ATOM   67   O  OE1 . GLN   A 1 16  ? 16.81821  34.82793 23.07211 1.000 63.56778  ? 23  GLN   A OE1 1 
ATOM   68   N  NE2 . GLN   A 1 16  ? 18.52903  35.54376 21.80592 1.000 66.84293  ? 23  GLN   A NE2 1 
ATOM   69   N  N   . ALA   A 1 17  ? 20.61666  31.74352 26.35657 1.000 43.61835  ? 24  ALA   A N   1 
ATOM   70   C  CA  . ALA   A 1 17  ? 21.27402  31.46653 27.62951 1.000 44.96021  ? 24  ALA   A CA  1 
ATOM   71   C  C   . ALA   A 1 17  ? 20.51009  32.05865 28.80771 1.000 46.57857  ? 24  ALA   A C   1 
ATOM   72   O  O   . ALA   A 1 17  ? 20.32843  31.39326 29.83401 1.000 46.63155  ? 24  ALA   A O   1 
ATOM   73   C  CB  . ALA   A 1 17  ? 22.71071  31.99553 27.60128 1.000 39.64088  ? 24  ALA   A CB  1 
ATOM   74   N  N   . GLU   A 1 18  ? 20.04565  33.30378 28.67687 1.000 38.22103  ? 25  GLU   A N   1 
ATOM   75   C  CA  . GLU   A 1 18  ? 19.37015  33.95386 29.79634 1.000 44.12334  ? 25  GLU   A CA  1 
ATOM   76   C  C   . GLU   A 1 18  ? 18.04062  33.28121 30.09985 1.000 44.09267  ? 25  GLU   A C   1 
ATOM   77   O  O   . GLU   A 1 18  ? 17.67122  33.12030 31.26843 1.000 38.99450  ? 25  GLU   A O   1 
ATOM   78   C  CB  . GLU   A 1 18  ? 19.16007  35.43922 29.49878 1.000 48.21474  ? 25  GLU   A CB  1 
ATOM   79   C  CG  . GLU   A 1 18  ? 20.45044  36.20591 29.27380 1.000 59.51604  ? 25  GLU   A CG  1 
ATOM   80   C  CD  . GLU   A 1 18  ? 20.91328  36.14539 27.82662 1.000 65.97703  ? 25  GLU   A CD  1 
ATOM   81   O  OE1 . GLU   A 1 18  ? 20.72539  35.09069 27.17906 1.000 60.26650  ? 25  GLU   A OE1 1 
ATOM   82   O  OE2 . GLU   A 1 18  ? 21.47542  37.14789 27.33935 1.000 69.61045  ? 25  GLU   A OE2 1 
ATOM   83   N  N   . ILE   A 1 19  ? 17.31352  32.87445 29.05932 1.000 36.85198  ? 26  ILE   A N   1 
ATOM   84   C  CA  . ILE   A 1 19  ? 16.01889  32.23527 29.26133 1.000 40.50961  ? 26  ILE   A CA  1 
ATOM   85   C  C   . ILE   A 1 19  ? 16.18685  30.86846 29.91383 1.000 41.16782  ? 26  ILE   A C   1 
ATOM   86   O  O   . ILE   A 1 19  ? 15.43592  30.50781 30.82989 1.000 39.53249  ? 26  ILE   A O   1 
ATOM   87   C  CB  . ILE   A 1 19  ? 15.26178  32.14161 27.92601 1.000 35.47764  ? 26  ILE   A CB  1 
ATOM   88   C  CG1 . ILE   A 1 19  ? 15.09059  33.54281 27.32540 1.000 33.93576  ? 26  ILE   A CG1 1 
ATOM   89   C  CG2 . ILE   A 1 19  ? 13.93457  31.42200 28.12076 1.000 30.18565  ? 26  ILE   A CG2 1 
ATOM   90   C  CD1 . ILE   A 1 19  ? 13.96568  33.65332 26.31863 1.000 42.42585  ? 26  ILE   A CD1 1 
ATOM   91   N  N   . ALA   A 1 20  ? 17.16806  30.08573 29.45582 1.000 34.42105  ? 27  ALA   A N   1 
ATOM   92   C  CA  . ALA   A 1 20  ? 17.42703  28.78944 30.07558 1.000 42.05398  ? 27  ALA   A CA  1 
ATOM   93   C  C   . ALA   A 1 20  ? 17.82783  28.95565 31.53461 1.000 42.55167  ? 27  ALA   A C   1 
ATOM   94   O  O   . ALA   A 1 20  ? 17.45369  28.14315 32.39047 1.000 34.75152  ? 27  ALA   A O   1 
ATOM   95   C  CB  . ALA   A 1 20  ? 18.51411  28.04481 29.30056 1.000 33.39167  ? 27  ALA   A CB  1 
ATOM   96   N  N   . GLN   A 1 21  ? 18.58518  30.01421 31.82928 1.000 38.34793  ? 28  GLN   A N   1 
ATOM   97   C  CA  . GLN   A 1 21  ? 18.97235  30.32294 33.20008 1.000 46.27764  ? 28  GLN   A CA  1 
ATOM   98   C  C   . GLN   A 1 21  ? 17.75794  30.62450 34.06852 1.000 44.47907  ? 28  GLN   A C   1 
ATOM   99   O  O   . GLN   A 1 21  ? 17.71874  30.24772 35.24632 1.000 43.40239  ? 28  GLN   A O   1 
ATOM   100  C  CB  . GLN   A 1 21  ? 19.92976  31.51044 33.19269 1.000 50.24993  ? 28  GLN   A CB  1 
ATOM   101  C  CG  . GLN   A 1 21  ? 21.02459  31.45045 34.21824 1.000 64.51319  ? 28  GLN   A CG  1 
ATOM   102  C  CD  . GLN   A 1 21  ? 21.97304  32.61656 34.07566 1.000 72.25016  ? 28  GLN   A CD  1 
ATOM   103  O  OE1 . GLN   A 1 21  ? 22.03607  33.49568 34.93725 1.000 68.90523  ? 28  GLN   A OE1 1 
ATOM   104  N  NE2 . GLN   A 1 21  ? 22.70120  32.64588 32.96442 1.000 55.79476  ? 28  GLN   A NE2 1 
ATOM   105  N  N   . LEU   A 1 22  ? 16.76585  31.32606 33.51179 1.000 41.92659  ? 29  LEU   A N   1 
ATOM   106  C  CA  . LEU   A 1 22  ? 15.57056  31.65762 34.28167 1.000 41.29424  ? 29  LEU   A CA  1 
ATOM   107  C  C   . LEU   A 1 22  ? 14.73496  30.41889 34.54851 1.000 36.30778  ? 29  LEU   A C   1 
ATOM   108  O  O   . LEU   A 1 22  ? 14.18246  30.25595 35.64175 1.000 34.71000  ? 29  LEU   A O   1 
ATOM   109  C  CB  . LEU   A 1 22  ? 14.74217  32.70865 33.54648 1.000 36.66516  ? 29  LEU   A CB  1 
ATOM   110  C  CG  . LEU   A 1 22  ? 13.40155  33.06214 34.18760 1.000 44.44101  ? 29  LEU   A CG  1 
ATOM   111  C  CD1 . LEU   A 1 22  ? 13.61369  33.59838 35.59707 1.000 34.14792  ? 29  LEU   A CD1 1 
ATOM   112  C  CD2 . LEU   A 1 22  ? 12.65379  34.06695 33.33128 1.000 41.67168  ? 29  LEU   A CD2 1 
ATOM   113  N  N   . MET   A 1 23  ? 14.64270  29.53059 33.56262 1.000 30.99657  ? 30  MET   A N   1 
ATOM   114  C  CA  . MET   A 1 23  ? 13.81893  28.34306 33.72772 1.000 38.66795  ? 30  MET   A CA  1 
ATOM   115  C  C   . MET   A 1 23  ? 14.39997  27.43616 34.80310 1.000 36.15497  ? 30  MET   A C   1 
ATOM   116  O  O   . MET   A 1 23  ? 13.66063  26.87428 35.61706 1.000 39.87372  ? 30  MET   A O   1 
ATOM   117  C  CB  . MET   A 1 23  ? 13.69821  27.61628 32.38763 1.000 36.70288  ? 30  MET   A CB  1 
ATOM   118  C  CG  . MET   A 1 23  ? 12.81666  28.36290 31.39398 1.000 36.38203  ? 30  MET   A CG  1 
ATOM   119  S  SD  . MET   A 1 23  ? 12.84471  27.71191 29.71565 1.000 39.53628  ? 30  MET   A SD  1 
ATOM   120  C  CE  . MET   A 1 23  ? 12.07288  26.12952 29.96813 1.000 37.05398  ? 30  MET   A CE  1 
ATOM   121  N  N   . SER   A 1 24  ? 15.72749  27.30998 34.83687 1.000 34.78638  ? 31  SER   A N   1 
ATOM   122  C  CA  . SER   A 1 24  ? 16.37444  26.51268 35.87068 1.000 37.24182  ? 31  SER   A CA  1 
ATOM   123  C  C   . SER   A 1 24  ? 16.15060  27.11863 37.25235 1.000 40.91757  ? 31  SER   A C   1 
ATOM   124  O  O   . SER   A 1 24  ? 15.93021  26.39368 38.22938 1.000 42.05472  ? 31  SER   A O   1 
ATOM   125  C  CB  . SER   A 1 24  ? 17.86697  26.38495 35.56546 1.000 33.66791  ? 31  SER   A CB  1 
ATOM   126  O  OG  . SER   A 1 24  ? 18.57806  25.98490 36.71944 1.000 53.38144  ? 31  SER   A OG  1 
ATOM   127  N  N   . LEU   A 1 25  ? 16.19851  28.44854 37.35466 1.000 39.63346  ? 32  LEU   A N   1 
ATOM   128  C  CA  . LEU   A 1 25  ? 15.90265  29.09712 38.62843 1.000 35.94441  ? 32  LEU   A CA  1 
ATOM   129  C  C   . LEU   A 1 25  ? 14.45137  28.86811 39.03819 1.000 39.40339  ? 32  LEU   A C   1 
ATOM   130  O  O   . LEU   A 1 25  ? 14.16184  28.64535 40.21689 1.000 42.95674  ? 32  LEU   A O   1 
ATOM   131  C  CB  . LEU   A 1 25  ? 16.21207  30.59184 38.53442 1.000 39.01191  ? 32  LEU   A CB  1 
ATOM   132  C  CG  . LEU   A 1 25  ? 16.05401  31.47205 39.77578 1.000 50.13966  ? 32  LEU   A CG  1 
ATOM   133  C  CD1 . LEU   A 1 25  ? 17.11943  32.55592 39.77377 1.000 47.33095  ? 32  LEU   A CD1 1 
ATOM   134  C  CD2 . LEU   A 1 25  ? 14.66056  32.09014 39.86368 1.000 48.75835  ? 32  LEU   A CD2 1 
ATOM   135  N  N   . ILE   A 1 26  ? 13.52521  28.91731 38.07857 1.000 40.93973  ? 33  ILE   A N   1 
ATOM   136  C  CA  . ILE   A 1 26  ? 12.11347  28.71241 38.38685 1.000 30.30587  ? 33  ILE   A CA  1 
ATOM   137  C  C   . ILE   A 1 26  ? 11.84763  27.27108 38.80681 1.000 39.32309  ? 33  ILE   A C   1 
ATOM   138  O  O   . ILE   A 1 26  ? 10.98707  27.01442 39.65930 1.000 43.94581  ? 33  ILE   A O   1 
ATOM   139  C  CB  . ILE   A 1 26  ? 11.25498  29.12391 37.17475 1.000 36.01674  ? 33  ILE   A CB  1 
ATOM   140  C  CG1 . ILE   A 1 26  ? 11.16126  30.65107 37.08296 1.000 38.92341  ? 33  ILE   A CG1 1 
ATOM   141  C  CG2 . ILE   A 1 26  ? 9.86563   28.47803 37.22374 1.000 27.77624  ? 33  ILE   A CG2 1 
ATOM   142  C  CD1 . ILE   A 1 26  ? 10.62804  31.14939 35.74742 1.000 36.44111  ? 33  ILE   A CD1 1 
ATOM   143  N  N   . ILE   A 1 27  ? 12.58027  26.31059 38.23896 1.000 41.53109  ? 34  ILE   A N   1 
ATOM   144  C  CA  . ILE   A 1 27  ? 12.35661  24.90525 38.57466 1.000 38.37530  ? 34  ILE   A CA  1 
ATOM   145  C  C   . ILE   A 1 27  ? 13.01585  24.53402 39.90141 1.000 39.68580  ? 34  ILE   A C   1 
ATOM   146  O  O   . ILE   A 1 27  ? 12.44653  23.77771 40.69552 1.000 47.71845  ? 34  ILE   A O   1 
ATOM   147  C  CB  . ILE   A 1 27  ? 12.84299  23.99919 37.42580 1.000 45.13336  ? 34  ILE   A CB  1 
ATOM   148  C  CG1 . ILE   A 1 27  ? 11.91144  24.10994 36.21742 1.000 42.32818  ? 34  ILE   A CG1 1 
ATOM   149  C  CG2 . ILE   A 1 27  ? 12.98780  22.55199 37.87711 1.000 43.78098  ? 34  ILE   A CG2 1 
ATOM   150  C  CD1 . ILE   A 1 27  ? 12.63978  24.07530 34.91001 1.000 39.89347  ? 34  ILE   A CD1 1 
ATOM   151  N  N   . ASN   A 1 28  ? 14.20993  25.05844 40.17909 1.000 49.14988  ? 35  ASN   A N   1 
ATOM   152  C  CA  . ASN   A 1 28  ? 15.00910  24.55712 41.29209 1.000 52.09599  ? 35  ASN   A CA  1 
ATOM   153  C  C   . ASN   A 1 28  ? 14.89630  25.38119 42.56933 1.000 51.56777  ? 35  ASN   A C   1 
ATOM   154  O  O   . ASN   A 1 28  ? 15.36985  24.92667 43.61602 1.000 64.14425  ? 35  ASN   A O   1 
ATOM   155  C  CB  . ASN   A 1 28  ? 16.48420  24.46992 40.88514 1.000 53.08189  ? 35  ASN   A CB  1 
ATOM   156  C  CG  . ASN   A 1 28  ? 16.70067  23.57877 39.68209 1.000 60.26413  ? 35  ASN   A CG  1 
ATOM   157  O  OD1 . ASN   A 1 28  ? 16.02249  22.56343 39.51365 1.000 57.67582  ? 35  ASN   A OD1 1 
ATOM   158  N  ND2 . ASN   A 1 28  ? 17.64201  23.96162 38.82909 1.000 58.71606  ? 35  ASN   A ND2 1 
ATOM   159  N  N   . THR   A 1 29  ? 14.29680  26.56622 42.52471 1.000 52.70867  ? 36  THR   A N   1 
ATOM   160  C  CA  . THR   A 1 29  ? 14.20440  27.41001 43.70800 1.000 54.12438  ? 36  THR   A CA  1 
ATOM   161  C  C   . THR   A 1 29  ? 12.98085  27.01912 44.52575 1.000 46.08744  ? 36  THR   A C   1 
ATOM   162  O  O   . THR   A 1 29  ? 11.88492  26.85681 43.98022 1.000 39.67800  ? 36  THR   A O   1 
ATOM   163  C  CB  . THR   A 1 29  ? 14.14306  28.88801 43.32026 1.000 57.04982  ? 36  THR   A CB  1 
ATOM   164  O  OG1 . THR   A 1 29  ? 15.37892  29.26103 42.69822 1.000 58.25937  ? 36  THR   A OG1 1 
ATOM   165  C  CG2 . THR   A 1 29  ? 13.92028  29.76675 44.54982 1.000 42.86693  ? 36  THR   A CG2 1 
ATOM   166  N  N   . PHE   A 1 30  ? 13.18153  26.84392 45.82871 1.000 39.67822  ? 37  PHE   A N   1 
ATOM   167  C  CA  . PHE   A 1 30  ? 12.08004  26.54614 46.72987 1.000 40.02354  ? 37  PHE   A CA  1 
ATOM   168  C  C   . PHE   A 1 30  ? 11.19406  27.77713 46.85376 1.000 43.83599  ? 37  PHE   A C   1 
ATOM   169  O  O   . PHE   A 1 30  ? 11.64760  28.84010 47.29068 1.000 49.32967  ? 37  PHE   A O   1 
ATOM   170  C  CB  . PHE   A 1 30  ? 12.61497  26.11616 48.09418 1.000 43.20517  ? 37  PHE   A CB  1 
ATOM   171  C  CG  . PHE   A 1 30  ? 11.54347  25.71377 49.06914 1.000 51.29908  ? 37  PHE   A CG  1 
ATOM   172  C  CD1 . PHE   A 1 30  ? 10.89896  24.49142 48.94719 1.000 48.57905  ? 37  PHE   A CD1 1 
ATOM   173  C  CD2 . PHE   A 1 30  ? 11.18210  26.55618 50.10963 1.000 45.02525  ? 37  PHE   A CD2 1 
ATOM   174  C  CE1 . PHE   A 1 30  ? 9.91226   24.11674 49.84492 1.000 45.50801  ? 37  PHE   A CE1 1 
ATOM   175  C  CE2 . PHE   A 1 30  ? 10.20009  26.18650 51.01177 1.000 52.09943  ? 37  PHE   A CE2 1 
ATOM   176  C  CZ  . PHE   A 1 30  ? 9.56409   24.96369 50.87840 1.000 55.05866  ? 37  PHE   A CZ  1 
ATOM   177  N  N   . TYR   A 1 31  ? 9.93895   27.64011 46.44749 1.000 39.00112  ? 38  TYR   A N   1 
ATOM   178  C  CA  . TYR   A 1 31  ? 9.00338   28.75888 46.46182 1.000 41.73227  ? 38  TYR   A CA  1 
ATOM   179  C  C   . TYR   A 1 31  ? 7.60146   28.18003 46.50822 1.000 42.81645  ? 38  TYR   A C   1 
ATOM   180  O  O   . TYR   A 1 31  ? 7.19259   27.48008 45.57756 1.000 44.08552  ? 38  TYR   A O   1 
ATOM   181  C  CB  . TYR   A 1 31  ? 9.19361   29.64697 45.23369 1.000 42.14086  ? 38  TYR   A CB  1 
ATOM   182  C  CG  . TYR   A 1 31  ? 8.29685   30.85971 45.21966 1.000 47.92674  ? 38  TYR   A CG  1 
ATOM   183  C  CD1 . TYR   A 1 31  ? 8.54060   31.93693 46.06070 1.000 46.91672  ? 38  TYR   A CD1 1 
ATOM   184  C  CD2 . TYR   A 1 31  ? 7.20131   30.92506 44.36774 1.000 47.57385  ? 38  TYR   A CD2 1 
ATOM   185  C  CE1 . TYR   A 1 31  ? 7.72035   33.04653 46.05313 1.000 47.64089  ? 38  TYR   A CE1 1 
ATOM   186  C  CE2 . TYR   A 1 31  ? 6.37467   32.02910 44.35231 1.000 37.98759  ? 38  TYR   A CE2 1 
ATOM   187  C  CZ  . TYR   A 1 31  ? 6.63930   33.08798 45.19583 1.000 50.42358  ? 38  TYR   A CZ  1 
ATOM   188  O  OH  . TYR   A 1 31  ? 5.81527   34.19093 45.18031 1.000 57.33883  ? 38  TYR   A OH  1 
ATOM   189  N  N   . SER   A 1 32  ? 6.87020   28.46567 47.58346 1.000 41.98726  ? 39  SER   A N   1 
ATOM   190  C  CA  . SER   A 1 32  ? 5.62373   27.75288 47.83864 1.000 49.75129  ? 39  SER   A CA  1 
ATOM   191  C  C   . SER   A 1 32  ? 4.42615   28.38145 47.13671 1.000 44.56116  ? 39  SER   A C   1 
ATOM   192  O  O   . SER   A 1 32  ? 3.44812   27.68146 46.85224 1.000 46.34739  ? 39  SER   A O   1 
ATOM   193  C  CB  . SER   A 1 32  ? 5.37339   27.67991 49.34455 1.000 45.39320  ? 39  SER   A CB  1 
ATOM   194  O  OG  . SER   A 1 32  ? 6.35889   26.87751 49.96784 1.000 46.74658  ? 39  SER   A OG  1 
ATOM   195  N  N   . ASN   A 1 33  ? 4.48919   29.67933 46.83474 1.000 44.79679  ? 40  ASN   A N   1 
ATOM   196  C  CA  . ASN   A 1 33  ? 3.35914   30.42013 46.27169 1.000 44.24749  ? 40  ASN   A CA  1 
ATOM   197  C  C   . ASN   A 1 33  ? 3.25794   30.21658 44.75386 1.000 46.31013  ? 40  ASN   A C   1 
ATOM   198  O  O   . ASN   A 1 33  ? 3.32699   31.15104 43.95563 1.000 43.22409  ? 40  ASN   A O   1 
ATOM   199  C  CB  . ASN   A 1 33  ? 3.50147   31.89289 46.63433 1.000 47.16438  ? 40  ASN   A CB  1 
ATOM   200  C  CG  . ASN   A 1 33  ? 2.31165   32.72057 46.20899 1.000 42.63011  ? 40  ASN   A CG  1 
ATOM   201  O  OD1 . ASN   A 1 33  ? 1.16632   32.28263 46.31106 1.000 48.63634  ? 40  ASN   A OD1 1 
ATOM   202  N  ND2 . ASN   A 1 33  ? 2.57857   33.93151 45.72702 1.000 42.34897  ? 40  ASN   A ND2 1 
ATOM   203  N  N   . LYS   A 1 34  ? 3.05807   28.95579 44.35971 1.000 43.51671  ? 41  LYS   A N   1 
ATOM   204  C  CA  . LYS   A 1 34  ? 3.09494   28.59758 42.94271 1.000 36.00420  ? 41  LYS   A CA  1 
ATOM   205  C  C   . LYS   A 1 34  ? 1.84424   29.02881 42.17943 1.000 32.28154  ? 41  LYS   A C   1 
ATOM   206  O  O   . LYS   A 1 34  ? 1.89520   29.13397 40.94878 1.000 35.69647  ? 41  LYS   A O   1 
ATOM   207  C  CB  . LYS   A 1 34  ? 3.30622   27.08886 42.80255 1.000 38.83543  ? 41  LYS   A CB  1 
ATOM   208  C  CG  . LYS   A 1 34  ? 4.63318   26.60385 43.38695 1.000 43.08127  ? 41  LYS   A CG  1 
ATOM   209  C  CD  . LYS   A 1 34  ? 4.73207   25.08780 43.37983 1.000 43.13499  ? 41  LYS   A CD  1 
ATOM   210  C  CE  . LYS   A 1 34  ? 6.08102   24.61084 43.89840 1.000 42.26234  ? 41  LYS   A CE  1 
ATOM   211  N  NZ  . LYS   A 1 34  ? 7.16038   24.77946 42.88316 1.000 44.33516  ? 41  LYS   A NZ  1 
ATOM   212  N  N   . GLU   A 1 35  ? 0.74100   29.31186 42.87724 1.000 34.58308  ? 42  GLU   A N   1 
ATOM   213  C  CA  . GLU   A 1 35  ? -0.53109  29.60728 42.22126 1.000 36.69091  ? 42  GLU   A CA  1 
ATOM   214  C  C   . GLU   A 1 35  ? -0.45778  30.79821 41.26639 1.000 35.88906  ? 42  GLU   A C   1 
ATOM   215  O  O   . GLU   A 1 35  ? -1.31825  30.92237 40.38785 1.000 35.31124  ? 42  GLU   A O   1 
ATOM   216  C  CB  . GLU   A 1 35  ? -1.61262  29.86306 43.27607 1.000 36.51419  ? 42  GLU   A CB  1 
ATOM   217  C  CG  . GLU   A 1 35  ? -1.45495  31.17728 44.02516 1.000 36.62360  ? 42  GLU   A CG  1 
ATOM   218  C  CD  . GLU   A 1 35  ? -2.47112  31.35315 45.14551 1.000 49.37274  ? 42  GLU   A CD  1 
ATOM   219  O  OE1 . GLU   A 1 35  ? -2.67106  30.40929 45.94147 1.000 50.10737  ? 42  GLU   A OE1 1 
ATOM   220  O  OE2 . GLU   A 1 35  ? -3.07335  32.44382 45.23227 1.000 62.70402  ? 42  GLU   A OE2 1 
ATOM   221  N  N   . ILE   A 1 36  ? 0.54582   31.67003 41.40407 1.000 33.68813  ? 43  ILE   A N   1 
ATOM   222  C  CA  . ILE   A 1 36  ? 0.63136   32.85154 40.54931 1.000 30.27859  ? 43  ILE   A CA  1 
ATOM   223  C  C   . ILE   A 1 36  ? 0.82622   32.48655 39.08237 1.000 32.97856  ? 43  ILE   A C   1 
ATOM   224  O  O   . ILE   A 1 36  ? 0.63631   33.33953 38.21029 1.000 32.66269  ? 43  ILE   A O   1 
ATOM   225  C  CB  . ILE   A 1 36  ? 1.75742   33.79349 41.03242 1.000 36.20323  ? 43  ILE   A CB  1 
ATOM   226  C  CG1 . ILE   A 1 36  ? 3.11905   33.09092 41.00301 1.000 35.38942  ? 43  ILE   A CG1 1 
ATOM   227  C  CG2 . ILE   A 1 36  ? 1.45551   34.31203 42.43149 1.000 36.99689  ? 43  ILE   A CG2 1 
ATOM   228  C  CD1 . ILE   A 1 36  ? 4.01760   33.54420 39.87159 1.000 38.30150  ? 43  ILE   A CD1 1 
ATOM   229  N  N   . PHE   A 1 37  ? 1.20098   31.23639 38.78469 1.000 29.64246  ? 44  PHE   A N   1 
ATOM   230  C  CA  . PHE   A 1 37  ? 1.36588   30.82278 37.39357 1.000 29.19996  ? 44  PHE   A CA  1 
ATOM   231  C  C   . PHE   A 1 37  ? 0.08175   31.03773 36.60407 1.000 32.39398  ? 44  PHE   A C   1 
ATOM   232  O  O   . PHE   A 1 37  ? 0.12218   31.40780 35.42551 1.000 31.89451  ? 44  PHE   A O   1 
ATOM   233  C  CB  . PHE   A 1 37  ? 1.79111   29.35168 37.32181 1.000 31.71545  ? 44  PHE   A CB  1 
ATOM   234  C  CG  . PHE   A 1 37  ? 0.63409   28.38219 37.38829 1.000 27.94744  ? 44  PHE   A CG  1 
ATOM   235  C  CD1 . PHE   A 1 37  ? 0.14877   27.94821 38.61058 1.000 28.99847  ? 44  PHE   A CD1 1 
ATOM   236  C  CD2 . PHE   A 1 37  ? 0.01810   27.92854 36.22944 1.000 34.54115  ? 44  PHE   A CD2 1 
ATOM   237  C  CE1 . PHE   A 1 37  ? -0.91661  27.08294 38.68343 1.000 31.32436  ? 44  PHE   A CE1 1 
ATOM   238  C  CE2 . PHE   A 1 37  ? -1.05341  27.05951 36.29300 1.000 23.40843  ? 44  PHE   A CE2 1 
ATOM   239  C  CZ  . PHE   A 1 37  ? -1.51922  26.63412 37.52034 1.000 37.39798  ? 44  PHE   A CZ  1 
ATOM   240  N  N   . LEU   A 1 38  ? -1.06857  30.79598 37.23754 1.000 33.03060  ? 45  LEU   A N   1 
ATOM   241  C  CA  . LEU   A 1 38  ? -2.34350  30.92515 36.54326 1.000 33.16755  ? 45  LEU   A CA  1 
ATOM   242  C  C   . LEU   A 1 38  ? -2.64766  32.38116 36.21905 1.000 30.80894  ? 45  LEU   A C   1 
ATOM   243  O  O   . LEU   A 1 38  ? -3.05980  32.69962 35.09664 1.000 31.96425  ? 45  LEU   A O   1 
ATOM   244  C  CB  . LEU   A 1 38  ? -3.46539  30.31378 37.38276 1.000 25.15920  ? 45  LEU   A CB  1 
ATOM   245  C  CG  . LEU   A 1 38  ? -4.75198  30.12883 36.58135 1.000 36.50845  ? 45  LEU   A CG  1 
ATOM   246  C  CD1 . LEU   A 1 38  ? -4.50464  29.20574 35.38238 1.000 28.21727  ? 45  LEU   A CD1 1 
ATOM   247  C  CD2 . LEU   A 1 38  ? -5.87713  29.61520 37.46317 1.000 35.81508  ? 45  LEU   A CD2 1 
ATOM   248  N  N   . ARG   A 1 39  ? -2.44463  33.27558 37.18919 1.000 26.15706  ? 46  ARG   A N   1 
ATOM   249  C  CA  . ARG   A 1 39  ? -2.58515  34.70415 36.93401 1.000 29.21587  ? 46  ARG   A CA  1 
ATOM   250  C  C   . ARG   A 1 39  ? -1.76864  35.13202 35.71981 1.000 34.06962  ? 46  ARG   A C   1 
ATOM   251  O  O   . ARG   A 1 39  ? -2.25775  35.87851 34.86431 1.000 34.56709  ? 46  ARG   A O   1 
ATOM   252  C  CB  . ARG   A 1 39  ? -2.15967  35.49820 38.17172 1.000 31.45623  ? 46  ARG   A CB  1 
ATOM   253  C  CG  . ARG   A 1 39  ? -2.20746  37.00072 37.98802 1.000 37.42268  ? 46  ARG   A CG  1 
ATOM   254  C  CD  . ARG   A 1 39  ? -1.49128  37.73682 39.11334 1.000 41.22973  ? 46  ARG   A CD  1 
ATOM   255  N  NE  . ARG   A 1 39  ? -0.06188  37.44687 39.14808 1.000 46.77126  ? 46  ARG   A NE  1 
ATOM   256  C  CZ  . ARG   A 1 39  ? 0.70003   37.54372 40.23105 1.000 59.26779  ? 46  ARG   A CZ  1 
ATOM   257  N  NH1 . ARG   A 1 39  ? 0.20679   37.94831 41.39112 1.000 48.92528  ? 46  ARG   A NH1 1 
ATOM   258  N  NH2 . ARG   A 1 39  ? 1.99144   37.23342 40.14685 1.000 55.05261  ? 46  ARG   A NH2 1 
ATOM   259  N  N   . GLU   A 1 40  ? -0.52710  34.65026 35.61597 1.000 27.94498  ? 47  GLU   A N   1 
ATOM   260  C  CA  . GLU   A 1 40  ? 0.34710   35.09497 34.53487 1.000 30.18776  ? 47  GLU   A CA  1 
ATOM   261  C  C   . GLU   A 1 40  ? -0.11551  34.55530 33.18703 1.000 32.28189  ? 47  GLU   A C   1 
ATOM   262  O  O   . GLU   A 1 40  ? -0.10444  35.28170 32.18574 1.000 33.62977  ? 47  GLU   A O   1 
ATOM   263  C  CB  . GLU   A 1 40  ? 1.79264   34.67881 34.81701 1.000 33.22076  ? 47  GLU   A CB  1 
ATOM   264  C  CG  . GLU   A 1 40  ? 2.37285   35.22440 36.12814 1.000 35.38953  ? 47  GLU   A CG  1 
ATOM   265  C  CD  . GLU   A 1 40  ? 2.31833   36.74904 36.24354 1.000 51.87970  ? 47  GLU   A CD  1 
ATOM   266  O  OE1 . GLU   A 1 40  ? 2.36780   37.45222 35.20675 1.000 45.30030  ? 47  GLU   A OE1 1 
ATOM   267  O  OE2 . GLU   A 1 40  ? 2.22790   37.24709 37.38747 1.000 59.28371  ? 47  GLU   A OE2 1 
ATOM   268  N  N   . LEU   A 1 41  ? -0.53352  33.28906 33.13965 1.000 29.38153  ? 48  LEU   A N   1 
ATOM   269  C  CA  . LEU   A 1 41  ? -0.98827  32.71817 31.87722 1.000 29.01409  ? 48  LEU   A CA  1 
ATOM   270  C  C   . LEU   A 1 41  ? -2.30680  33.34186 31.43336 1.000 33.38791  ? 48  LEU   A C   1 
ATOM   271  O  O   . LEU   A 1 41  ? -2.49572  33.62644 30.24383 1.000 29.98909  ? 48  LEU   A O   1 
ATOM   272  C  CB  . LEU   A 1 41  ? -1.12724  31.20561 32.01182 1.000 31.45582  ? 48  LEU   A CB  1 
ATOM   273  C  CG  . LEU   A 1 41  ? 0.18718   30.46440 32.24219 1.000 31.60161  ? 48  LEU   A CG  1 
ATOM   274  C  CD1 . LEU   A 1 41  ? -0.05207  28.96117 32.30199 1.000 33.40627  ? 48  LEU   A CD1 1 
ATOM   275  C  CD2 . LEU   A 1 41  ? 1.20410   30.81632 31.17213 1.000 31.83188  ? 48  LEU   A CD2 1 
ATOM   276  N  N   . ILE   A 1 42  ? -3.22846  33.55904 32.37729 1.000 29.84862  ? 49  ILE   A N   1 
ATOM   277  C  CA  . ILE   A 1 42  ? -4.49978  34.20629 32.06122 1.000 27.82421  ? 49  ILE   A CA  1 
ATOM   278  C  C   . ILE   A 1 42  ? -4.26159  35.63222 31.59040 1.000 29.92525  ? 49  ILE   A C   1 
ATOM   279  O  O   . ILE   A 1 42  ? -4.90866  36.11178 30.65226 1.000 31.52789  ? 49  ILE   A O   1 
ATOM   280  C  CB  . ILE   A 1 42  ? -5.43784  34.17062 33.28388 1.000 28.69134  ? 49  ILE   A CB  1 
ATOM   281  C  CG1 . ILE   A 1 42  ? -6.02408  32.77167 33.48447 1.000 31.02731  ? 49  ILE   A CG1 1 
ATOM   282  C  CG2 . ILE   A 1 42  ? -6.55332  35.20615 33.14430 1.000 28.76267  ? 49  ILE   A CG2 1 
ATOM   283  C  CD1 . ILE   A 1 42  ? -6.98521  32.68855 34.66909 1.000 27.57432  ? 49  ILE   A CD1 1 
ATOM   284  N  N   . SER   A 1 43  ? -3.33669  36.33486 32.24586 1.000 31.75251  ? 50  SER   A N   1 
ATOM   285  C  CA  . SER   A 1 43  ? -2.98876  37.68627 31.82793 1.000 33.71780  ? 50  SER   A CA  1 
ATOM   286  C  C   . SER   A 1 43  ? -2.39873  37.69116 30.41960 1.000 30.80769  ? 50  SER   A C   1 
ATOM   287  O  O   . SER   A 1 43  ? -2.68292  38.59507 29.62362 1.000 29.06341  ? 50  SER   A O   1 
ATOM   288  C  CB  . SER   A 1 43  ? -2.02165  38.29842 32.84490 1.000 27.87738  ? 50  SER   A CB  1 
ATOM   289  O  OG  . SER   A 1 43  ? -1.32677  39.40607 32.30782 1.000 41.23494  ? 50  SER   A OG  1 
ATOM   290  N  N   . ASN   A 1 44  ? -1.59349  36.67418 30.08594 1.000 30.78099  ? 51  ASN   A N   1 
ATOM   291  C  CA  . ASN   A 1 44  ? -1.05780  36.55900 28.72936 1.000 30.21125  ? 51  ASN   A CA  1 
ATOM   292  C  C   . ASN   A 1 44  ? -2.16566  36.30819 27.71337 1.000 30.54759  ? 51  ASN   A C   1 
ATOM   293  O  O   . ASN   A 1 44  ? -2.11445  36.82002 26.58980 1.000 32.77074  ? 51  ASN   A O   1 
ATOM   294  C  CB  . ASN   A 1 44  ? -0.02396  35.43709 28.65904 1.000 26.38997  ? 51  ASN   A CB  1 
ATOM   295  C  CG  . ASN   A 1 44  ? 1.34613   35.87889 29.11875 1.000 36.47849  ? 51  ASN   A CG  1 
ATOM   296  O  OD1 . ASN   A 1 44  ? 1.54619   37.03227 29.50470 1.000 34.07296  ? 51  ASN   A OD1 1 
ATOM   297  N  ND2 . ASN   A 1 44  ? 2.30343   34.96215 29.07563 1.000 33.81299  ? 51  ASN   A ND2 1 
ATOM   298  N  N   . SER   A 1 45  ? -3.16209  35.49896 28.08337 1.000 31.75332  ? 52  SER   A N   1 
ATOM   299  C  CA  . SER   A 1 45  ? -4.30062  35.26478 27.20374 1.000 30.66932  ? 52  SER   A CA  1 
ATOM   300  C  C   . SER   A 1 45  ? -5.09873  36.54338 26.99605 1.000 29.79233  ? 52  SER   A C   1 
ATOM   301  O  O   . SER   A 1 45  ? -5.57731  36.81213 25.88956 1.000 33.31001  ? 52  SER   A O   1 
ATOM   302  C  CB  . SER   A 1 45  ? -5.19054  34.16703 27.78467 1.000 28.20545  ? 52  SER   A CB  1 
ATOM   303  O  OG  . SER   A 1 45  ? -4.55977  32.90369 27.70027 1.000 33.93393  ? 52  SER   A OG  1 
ATOM   304  N  N   . SER   A 1 46  ? -5.24197  37.34613 28.05198 1.000 33.07652  ? 53  SER   A N   1 
ATOM   305  C  CA  . SER   A 1 46  ? -5.96506  38.60790 27.94831 1.000 28.56969  ? 53  SER   A CA  1 
ATOM   306  C  C   . SER   A 1 46  ? -5.25715  39.57907 27.00553 1.000 31.30180  ? 53  SER   A C   1 
ATOM   307  O  O   . SER   A 1 46  ? -5.91435  40.27391 26.22308 1.000 34.43272  ? 53  SER   A O   1 
ATOM   308  C  CB  . SER   A 1 46  ? -6.13833  39.21551 29.34459 1.000 30.02710  ? 53  SER   A CB  1 
ATOM   309  O  OG  . SER   A 1 46  ? -6.86571  40.43260 29.31079 1.000 33.83520  ? 53  SER   A OG  1 
ATOM   310  N  N   . ASP   A 1 47  ? -3.92023  39.63965 27.05648 1.000 27.60598  ? 54  ASP   A N   1 
ATOM   311  C  CA  . ASP   A 1 47  ? -3.19185  40.49696 26.12270 1.000 29.22630  ? 54  ASP   A CA  1 
ATOM   312  C  C   . ASP   A 1 47  ? -3.42107  40.05738 24.67701 1.000 29.23495  ? 54  ASP   A C   1 
ATOM   313  O  O   . ASP   A 1 47  ? -3.66037  40.89009 23.79517 1.000 34.30365  ? 54  ASP   A O   1 
ATOM   314  C  CB  . ASP   A 1 47  ? -1.69347  40.51011 26.44665 1.000 31.69334  ? 54  ASP   A CB  1 
ATOM   315  C  CG  . ASP   A 1 47  ? -1.37626  41.15307 27.80126 1.000 44.50452  ? 54  ASP   A CG  1 
ATOM   316  O  OD1 . ASP   A 1 47  ? -0.42072  40.69096 28.46231 1.000 43.44602  ? 54  ASP   A OD1 1 
ATOM   317  O  OD2 . ASP   A 1 47  ? -2.07778  42.10821 28.21176 1.000 47.56644  ? 54  ASP   A OD2 1 
ATOM   318  N  N   . ALA   A 1 48  ? -3.35447  38.74782 24.41640 1.000 30.55947  ? 55  ALA   A N   1 
ATOM   319  C  CA  . ALA   A 1 48  ? -3.54888  38.24149 23.05843 1.000 32.10833  ? 55  ALA   A CA  1 
ATOM   320  C  C   . ALA   A 1 48  ? -4.95394  38.52345 22.53973 1.000 26.66045  ? 55  ALA   A C   1 
ATOM   321  O  O   . ALA   A 1 48  ? -5.14407  38.71733 21.33288 1.000 29.26100  ? 55  ALA   A O   1 
ATOM   322  C  CB  . ALA   A 1 48  ? -3.27411  36.73883 23.00979 1.000 25.94501  ? 55  ALA   A CB  1 
ATOM   323  N  N   . LEU   A 1 49  ? -5.94888  38.52834 23.42635 1.000 26.92612  ? 56  LEU   A N   1 
ATOM   324  C  CA  . LEU   A 1 49  ? -7.30447  38.86314 23.00972 1.000 28.27093  ? 56  LEU   A CA  1 
ATOM   325  C  C   . LEU   A 1 49  ? -7.43562  40.35277 22.73005 1.000 28.43930  ? 56  LEU   A C   1 
ATOM   326  O  O   . LEU   A 1 49  ? -8.08356  40.74822 21.75569 1.000 31.75481  ? 56  LEU   A O   1 
ATOM   327  C  CB  . LEU   A 1 49  ? -8.30192  38.42392 24.07679 1.000 29.60749  ? 56  LEU   A CB  1 
ATOM   328  C  CG  . LEU   A 1 49  ? -8.50555  36.91557 24.22450 1.000 31.09785  ? 56  LEU   A CG  1 
ATOM   329  C  CD1 . LEU   A 1 49  ? -9.12177  36.60876 25.58513 1.000 31.42706  ? 56  LEU   A CD1 1 
ATOM   330  C  CD2 . LEU   A 1 49  ? -9.37886  36.37132 23.10652 1.000 26.43484  ? 56  LEU   A CD2 1 
ATOM   331  N  N   . ASP   A 1 50  ? -6.82234  41.19501 23.57015 1.000 33.41818  ? 57  ASP   A N   1 
ATOM   332  C  CA  . ASP   A 1 50  ? -6.80972  42.63222 23.30221 1.000 30.50176  ? 57  ASP   A CA  1 
ATOM   333  C  C   . ASP   A 1 50  ? -6.25387  42.92554 21.91434 1.000 31.59251  ? 57  ASP   A C   1 
ATOM   334  O  O   . ASP   A 1 50  ? -6.74398  43.81845 21.21118 1.000 31.07060  ? 57  ASP   A O   1 
ATOM   335  C  CB  . ASP   A 1 50  ? -5.97557  43.37115 24.35541 1.000 30.74355  ? 57  ASP   A CB  1 
ATOM   336  C  CG  . ASP   A 1 50  ? -6.62566  43.38468 25.73313 1.000 42.46156  ? 57  ASP   A CG  1 
ATOM   337  O  OD1 . ASP   A 1 50  ? -7.86527  43.26279 25.81581 1.000 41.93095  ? 57  ASP   A OD1 1 
ATOM   338  O  OD2 . ASP   A 1 50  ? -5.89164  43.54245 26.73415 1.000 39.66583  ? 57  ASP   A OD2 1 
ATOM   339  N  N   . LYS   A 1 51  ? -5.22808  42.17625 21.50516 1.000 30.04572  ? 58  LYS   A N   1 
ATOM   340  C  CA  . LYS   A 1 51  ? -4.55061  42.45917 20.24567 1.000 29.47101  ? 58  LYS   A CA  1 
ATOM   341  C  C   . LYS   A 1 51  ? -5.45185  42.16242 19.05416 1.000 29.01696  ? 58  LYS   A C   1 
ATOM   342  O  O   . LYS   A 1 51  ? -5.60841  43.00253 18.16232 1.000 33.10986  ? 58  LYS   A O   1 
ATOM   343  C  CB  . LYS   A 1 51  ? -3.25013  41.65984 20.16683 1.000 29.92802  ? 58  LYS   A CB  1 
ATOM   344  C  CG  . LYS   A 1 51  ? -2.07788  42.36192 20.80765 1.000 34.52470  ? 58  LYS   A CG  1 
ATOM   345  C  CD  . LYS   A 1 51  ? -0.86343  41.45398 20.94305 1.000 44.17076  ? 58  LYS   A CD  1 
ATOM   346  C  CE  . LYS   A 1 51  ? 0.01236   41.88686 22.12131 1.000 45.35651  ? 58  LYS   A CE  1 
ATOM   347  N  NZ  . LYS   A 1 51  ? 0.65712   40.74089 22.82093 1.000 51.28413  ? 58  LYS   A NZ  1 
ATOM   348  N  N   . ILE   A 1 52  ? -6.06040  40.97228 19.01970 1.000 33.05183  ? 59  ILE   A N   1 
ATOM   349  C  CA  . ILE   A 1 52  ? -6.93788  40.64333 17.89915 1.000 31.76057  ? 59  ILE   A CA  1 
ATOM   350  C  C   . ILE   A 1 52  ? -8.18191  41.52158 17.93427 1.000 30.42767  ? 59  ILE   A C   1 
ATOM   351  O  O   . ILE   A 1 52  ? -8.71160  41.90426 16.88536 1.000 35.35264  ? 59  ILE   A O   1 
ATOM   352  C  CB  . ILE   A 1 52  ? -7.28246  39.13419 17.89310 1.000 30.90742  ? 59  ILE   A CB  1 
ATOM   353  C  CG1 . ILE   A 1 52  ? -7.95265  38.72363 16.57680 1.000 29.39486  ? 59  ILE   A CG1 1 
ATOM   354  C  CG2 . ILE   A 1 52  ? -8.17842  38.75692 19.06096 1.000 26.44438  ? 59  ILE   A CG2 1 
ATOM   355  C  CD1 . ILE   A 1 52  ? -7.10722  38.97100 15.34276 1.000 31.99971  ? 59  ILE   A CD1 1 
ATOM   356  N  N   . ARG   A 1 53  ? -8.64454  41.89147 19.12950 1.000 36.42503  ? 60  ARG   A N   1 
ATOM   357  C  CA  . ARG   A 1 53  ? -9.79381  42.78470 19.23336 1.000 37.10072  ? 60  ARG   A CA  1 
ATOM   358  C  C   . ARG   A 1 53  ? -9.48609  44.14745 18.62667 1.000 36.89037  ? 60  ARG   A C   1 
ATOM   359  O  O   . ARG   A 1 53  ? -10.28897 44.69861 17.86610 1.000 33.86497  ? 60  ARG   A O   1 
ATOM   360  C  CB  . ARG   A 1 53  ? -10.21322 42.93460 20.69346 1.000 32.37863  ? 60  ARG   A CB  1 
ATOM   361  C  CG  . ARG   A 1 53  ? -11.31184 43.94931 20.90188 1.000 37.17397  ? 60  ARG   A CG  1 
ATOM   362  C  CD  . ARG   A 1 53  ? -12.10599 43.63051 22.14783 1.000 42.82094  ? 60  ARG   A CD  1 
ATOM   363  N  NE  . ARG   A 1 53  ? -12.60932 44.83441 22.79475 1.000 52.08300  ? 60  ARG   A NE  1 
ATOM   364  C  CZ  . ARG   A 1 53  ? -12.19294 45.27832 23.97080 1.000 54.72481  ? 60  ARG   A CZ  1 
ATOM   365  N  NH1 . ARG   A 1 53  ? -11.25267 44.64464 24.65529 1.000 48.98424  ? 60  ARG   A NH1 1 
ATOM   366  N  NH2 . ARG   A 1 53  ? -12.73786 46.37998 24.47436 1.000 46.56450  ? 60  ARG   A NH2 1 
ATOM   367  N  N   . TYR   A 1 54  ? -8.31913  44.70617 18.95033 1.000 37.11238  ? 61  TYR   A N   1 
ATOM   368  C  CA  . TYR   A 1 54  ? -7.98032  46.03421 18.44913 1.000 39.12517  ? 61  TYR   A CA  1 
ATOM   369  C  C   . TYR   A 1 54  ? -7.74817  46.01793 16.93971 1.000 35.92099  ? 61  TYR   A C   1 
ATOM   370  O  O   . TYR   A 1 54  ? -8.11747  46.96603 16.23811 1.000 38.19060  ? 61  TYR   A O   1 
ATOM   371  C  CB  . TYR   A 1 54  ? -6.75585  46.56818 19.19102 1.000 35.09869  ? 61  TYR   A CB  1 
ATOM   372  C  CG  . TYR   A 1 54  ? -6.23271  47.85260 18.62483 1.000 38.06028  ? 61  TYR   A CG  1 
ATOM   373  C  CD1 . TYR   A 1 54  ? -6.81956  49.07149 18.95118 1.000 40.30665  ? 61  TYR   A CD1 1 
ATOM   374  C  CD2 . TYR   A 1 54  ? -5.15286  47.85100 17.75146 1.000 42.22122  ? 61  TYR   A CD2 1 
ATOM   375  C  CE1 . TYR   A 1 54  ? -6.34146  50.25782 18.41877 1.000 45.68199  ? 61  TYR   A CE1 1 
ATOM   376  C  CE2 . TYR   A 1 54  ? -4.66918  49.02676 17.21442 1.000 54.37303  ? 61  TYR   A CE2 1 
ATOM   377  C  CZ  . TYR   A 1 54  ? -5.26302  50.22610 17.55114 1.000 48.20060  ? 61  TYR   A CZ  1 
ATOM   378  O  OH  . TYR   A 1 54  ? -4.76643  51.38839 17.00764 1.000 59.39799  ? 61  TYR   A OH  1 
ATOM   379  N  N   . GLU   A 1 55  ? -7.14480  44.94754 16.42133 1.000 38.01924  ? 62  GLU   A N   1 
ATOM   380  C  CA  . GLU   A 1 55  ? -6.93153  44.84206 14.97937 1.000 42.06015  ? 62  GLU   A CA  1 
ATOM   381  C  C   . GLU   A 1 55  ? -8.25367  44.74099 14.22838 1.000 42.44539  ? 62  GLU   A C   1 
ATOM   382  O  O   . GLU   A 1 55  ? -8.39250  45.27545 13.12078 1.000 48.36664  ? 62  GLU   A O   1 
ATOM   383  C  CB  . GLU   A 1 55  ? -6.05401  43.63132 14.67169 1.000 36.94808  ? 62  GLU   A CB  1 
ATOM   384  C  CG  . GLU   A 1 55  ? -4.56797  43.90653 14.79908 1.000 49.74550  ? 62  GLU   A CG  1 
ATOM   385  C  CD  . GLU   A 1 55  ? -3.71568  42.75490 14.29721 1.000 68.52595  ? 62  GLU   A CD  1 
ATOM   386  O  OE1 . GLU   A 1 55  ? -4.28886  41.77793 13.76682 1.000 68.93598  ? 62  GLU   A OE1 1 
ATOM   387  O  OE2 . GLU   A 1 55  ? -2.47474  42.82289 14.44510 1.000 71.40286  ? 62  GLU   A OE2 1 
ATOM   388  N  N   . SER   A 1 56  ? -9.23761  44.06223 14.81476 1.000 40.25786  ? 63  SER   A N   1 
ATOM   389  C  CA  . SER   A 1 56  ? -10.52050 43.87959 14.15229 1.000 40.02104  ? 63  SER   A CA  1 
ATOM   390  C  C   . SER   A 1 56  ? -11.32254 45.17078 14.04143 1.000 49.06799  ? 63  SER   A C   1 
ATOM   391  O  O   . SER   A 1 56  ? -12.29697 45.20809 13.28116 1.000 51.19928  ? 63  SER   A O   1 
ATOM   392  C  CB  . SER   A 1 56  ? -11.33437 42.81477 14.89195 1.000 46.69768  ? 63  SER   A CB  1 
ATOM   393  O  OG  . SER   A 1 56  ? -11.86736 43.32028 16.10502 1.000 39.99484  ? 63  SER   A OG  1 
ATOM   394  N  N   . LEU   A 1 57  ? -10.94352 46.22391 14.77150 1.000 43.38601  ? 64  LEU   A N   1 
ATOM   395  C  CA  . LEU   A 1 57  ? -11.66608 47.48947 14.66872 1.000 44.70349  ? 64  LEU   A CA  1 
ATOM   396  C  C   . LEU   A 1 57  ? -11.46257 48.13673 13.30410 1.000 44.65386  ? 64  LEU   A C   1 
ATOM   397  O  O   . LEU   A 1 57  ? -12.40132 48.70656 12.73761 1.000 55.78625  ? 64  LEU   A O   1 
ATOM   398  C  CB  . LEU   A 1 57  ? -11.23399 48.43821 15.78815 1.000 42.22259  ? 64  LEU   A CB  1 
ATOM   399  C  CG  . LEU   A 1 57  ? -11.63824 47.96025 17.18409 1.000 47.08751  ? 64  LEU   A CG  1 
ATOM   400  C  CD1 . LEU   A 1 57  ? -11.09303 48.86328 18.27705 1.000 41.06015  ? 64  LEU   A CD1 1 
ATOM   401  C  CD2 . LEU   A 1 57  ? -13.14838 47.87454 17.26919 1.000 46.98400  ? 64  LEU   A CD2 1 
ATOM   402  N  N   . THR   A 1 58  ? -10.24957 48.06334 12.75916 1.000 46.55641  ? 65  THR   A N   1 
ATOM   403  C  CA  . THR   A 1 58  ? -9.96465  48.61447 11.43944 1.000 55.65130  ? 65  THR   A CA  1 
ATOM   404  C  C   . THR   A 1 58  ? -10.02357 47.57295 10.32701 1.000 50.83533  ? 65  THR   A C   1 
ATOM   405  O  O   . THR   A 1 58  ? -10.01035 47.94533 9.14918  1.000 51.78081  ? 65  THR   A O   1 
ATOM   406  C  CB  . THR   A 1 58  ? -8.58813  49.29420 11.43657 1.000 60.99339  ? 65  THR   A CB  1 
ATOM   407  O  OG1 . THR   A 1 58  ? -7.58084  48.33950 11.79552 1.000 58.62419  ? 65  THR   A OG1 1 
ATOM   408  C  CG2 . THR   A 1 58  ? -8.56354  50.45807 12.42494 1.000 54.28423  ? 65  THR   A CG2 1 
ATOM   409  N  N   . ASP   A 1 59  ? -10.09742 46.28641 10.67196 1.000 57.03676  ? 66  ASP   A N   1 
ATOM   410  C  CA  . ASP   A 1 59  ? -10.15086 45.20994 9.68397  1.000 46.17562  ? 66  ASP   A CA  1 
ATOM   411  C  C   . ASP   A 1 59  ? -11.02978 44.09694 10.23383 1.000 52.38257  ? 66  ASP   A C   1 
ATOM   412  O  O   . ASP   A 1 59  ? -10.54374 43.16618 10.89231 1.000 50.12221  ? 66  ASP   A O   1 
ATOM   413  C  CB  . ASP   A 1 59  ? -8.75729  44.68164 9.35086  1.000 52.69859  ? 66  ASP   A CB  1 
ATOM   414  C  CG  . ASP   A 1 59  ? -8.76070  43.72296 8.17045  1.000 63.70727  ? 66  ASP   A CG  1 
ATOM   415  O  OD1 . ASP   A 1 59  ? -9.82658  43.55373 7.53566  1.000 58.97996  ? 66  ASP   A OD1 1 
ATOM   416  O  OD2 . ASP   A 1 59  ? -7.69326  43.14004 7.87802  1.000 66.90342  ? 66  ASP   A OD2 1 
ATOM   417  N  N   . PRO   A 1 60  ? -12.33868 44.15498 9.97700  1.000 54.74000  ? 67  PRO   A N   1 
ATOM   418  C  CA  . PRO   A 1 60  ? -13.24438 43.15190 10.56406 1.000 52.86053  ? 67  PRO   A CA  1 
ATOM   419  C  C   . PRO   A 1 60  ? -13.00275 41.73575 10.06628 1.000 55.04299  ? 67  PRO   A C   1 
ATOM   420  O  O   . PRO   A 1 60  ? -13.38379 40.78547 10.76084 1.000 55.75236  ? 67  PRO   A O   1 
ATOM   421  C  CB  . PRO   A 1 60  ? -14.63930 43.65461 10.16119 1.000 51.30012  ? 67  PRO   A CB  1 
ATOM   422  C  CG  . PRO   A 1 60  ? -14.44158 45.10772 9.81351  1.000 53.43100  ? 67  PRO   A CG  1 
ATOM   423  C  CD  . PRO   A 1 60  ? -13.06918 45.18511 9.22122  1.000 50.58031  ? 67  PRO   A CD  1 
ATOM   424  N  N   . SER   A 1 61  ? -12.38318 41.55757 8.89759  1.000 50.37258  ? 68  SER   A N   1 
ATOM   425  C  CA  . SER   A 1 61  ? -12.10141 40.21501 8.40164  1.000 53.69699  ? 68  SER   A CA  1 
ATOM   426  C  C   . SER   A 1 61  ? -11.10863 39.45234 9.27541  1.000 50.07919  ? 68  SER   A C   1 
ATOM   427  O  O   . SER   A 1 61  ? -11.01099 38.22895 9.14513  1.000 48.67990  ? 68  SER   A O   1 
ATOM   428  C  CB  . SER   A 1 61  ? -11.58184 40.28121 6.96249  1.000 50.81391  ? 68  SER   A CB  1 
ATOM   429  O  OG  . SER   A 1 61  ? -10.30149 40.88650 6.90232  1.000 60.05570  ? 68  SER   A OG  1 
ATOM   430  N  N   . LYS   A 1 62  ? -10.37990 40.12596 10.16581 1.000 42.28835  ? 69  LYS   A N   1 
ATOM   431  C  CA  . LYS   A 1 62  ? -9.48288  39.40391 11.06101 1.000 44.38612  ? 69  LYS   A CA  1 
ATOM   432  C  C   . LYS   A 1 62  ? -10.22162 38.49768 12.03798 1.000 43.68677  ? 69  LYS   A C   1 
ATOM   433  O  O   . LYS   A 1 62  ? -9.57503  37.70246 12.72590 1.000 42.27823  ? 69  LYS   A O   1 
ATOM   434  C  CB  . LYS   A 1 62  ? -8.61002  40.38686 11.83931 1.000 46.96931  ? 69  LYS   A CB  1 
ATOM   435  C  CG  . LYS   A 1 62  ? -7.83308  41.33990 10.95952 1.000 51.67508  ? 69  LYS   A CG  1 
ATOM   436  C  CD  . LYS   A 1 62  ? -6.39934  41.45695 11.41690 1.000 43.52971  ? 69  LYS   A CD  1 
ATOM   437  C  CE  . LYS   A 1 62  ? -5.60951  42.34973 10.48304 1.000 52.66835  ? 69  LYS   A CE  1 
ATOM   438  N  NZ  . LYS   A 1 62  ? -4.19122  41.91988 10.37950 1.000 59.38134  ? 69  LYS   A NZ  1 
ATOM   439  N  N   . LEU   A 1 63  ? -11.54437 38.60023 12.12596 1.000 41.24010  ? 70  LEU   A N   1 
ATOM   440  C  CA  . LEU   A 1 63  ? -12.33907 37.72667 12.97525 1.000 42.25470  ? 70  LEU   A CA  1 
ATOM   441  C  C   . LEU   A 1 63  ? -13.05090 36.63280 12.19410 1.000 45.37173  ? 70  LEU   A C   1 
ATOM   442  O  O   . LEU   A 1 63  ? -13.84583 35.89325 12.78056 1.000 47.38595  ? 70  LEU   A O   1 
ATOM   443  C  CB  . LEU   A 1 63  ? -13.36167 38.54735 13.76588 1.000 38.41867  ? 70  LEU   A CB  1 
ATOM   444  C  CG  . LEU   A 1 63  ? -12.72666 39.46365 14.81315 1.000 40.64248  ? 70  LEU   A CG  1 
ATOM   445  C  CD1 . LEU   A 1 63  ? -13.78729 40.16274 15.64687 1.000 46.35695  ? 70  LEU   A CD1 1 
ATOM   446  C  CD2 . LEU   A 1 63  ? -11.77282 38.67969 15.69412 1.000 36.84501  ? 70  LEU   A CD2 1 
ATOM   447  N  N   . ASP   A 1 64  ? -12.78758 36.51331 10.88794 1.000 44.07656  ? 71  ASP   A N   1 
ATOM   448  C  CA  . ASP   A 1 64  ? -13.35992 35.41575 10.11445 1.000 46.43496  ? 71  ASP   A CA  1 
ATOM   449  C  C   . ASP   A 1 64  ? -12.91629 34.06382 10.65388 1.000 48.60877  ? 71  ASP   A C   1 
ATOM   450  O  O   . ASP   A 1 64  ? -13.61722 33.06233 10.47369 1.000 54.86403  ? 71  ASP   A O   1 
ATOM   451  C  CB  . ASP   A 1 64  ? -12.96984 35.53868 8.64274  1.000 49.55186  ? 71  ASP   A CB  1 
ATOM   452  C  CG  . ASP   A 1 64  ? -13.63908 36.71121 7.95721  1.000 55.78263  ? 71  ASP   A CG  1 
ATOM   453  O  OD1 . ASP   A 1 64  ? -14.66431 37.20393 8.47861  1.000 68.86170  ? 71  ASP   A OD1 1 
ATOM   454  O  OD2 . ASP   A 1 64  ? -13.14138 37.12845 6.88819  1.000 55.22658  ? 71  ASP   A OD2 1 
ATOM   455  N  N   . SER   A 1 65  ? -11.76277 34.01407 11.31307 1.000 42.87211  ? 72  SER   A N   1 
ATOM   456  C  CA  . SER   A 1 65  ? -11.26960 32.79723 11.93964 1.000 44.39385  ? 72  SER   A CA  1 
ATOM   457  C  C   . SER   A 1 65  ? -11.86961 32.56420 13.32022 1.000 45.52574  ? 72  SER   A C   1 
ATOM   458  O  O   . SER   A 1 65  ? -11.35047 31.72894 14.07012 1.000 45.73945  ? 72  SER   A O   1 
ATOM   459  C  CB  . SER   A 1 65  ? -9.74351  32.84607 12.04165 1.000 44.01942  ? 72  SER   A CB  1 
ATOM   460  O  OG  . SER   A 1 65  ? -9.31143  34.13915 12.44726 1.000 46.73770  ? 72  SER   A OG  1 
ATOM   461  N  N   . GLY   A 1 66  ? -12.93692 33.28027 13.67319 1.000 39.77199  ? 73  GLY   A N   1 
ATOM   462  C  CA  . GLY   A 1 66  ? -13.56546 33.11158 14.96908 1.000 41.04397  ? 73  GLY   A CA  1 
ATOM   463  C  C   . GLY   A 1 66  ? -13.95554 34.41992 15.62226 1.000 43.35233  ? 73  GLY   A C   1 
ATOM   464  O  O   . GLY   A 1 66  ? -13.09640 35.26630 15.89004 1.000 41.49872  ? 73  GLY   A O   1 
ATOM   465  N  N   . LYS   A 1 67  ? -15.25137 34.59182 15.89261 1.000 45.07660  ? 74  LYS   A N   1 
ATOM   466  C  CA  . LYS   A 1 67  ? -15.76584 35.83698 16.45361 1.000 53.93325  ? 74  LYS   A CA  1 
ATOM   467  C  C   . LYS   A 1 67  ? -15.67622 35.90102 17.97449 1.000 48.99394  ? 74  LYS   A C   1 
ATOM   468  O  O   . LYS   A 1 67  ? -15.60380 37.00113 18.53441 1.000 50.00212  ? 74  LYS   A O   1 
ATOM   469  C  CB  . LYS   A 1 67  ? -17.22309 36.04378 16.02893 1.000 50.35779  ? 74  LYS   A CB  1 
ATOM   470  C  CG  . LYS   A 1 67  ? -17.39251 36.86604 14.76040 1.000 62.54771  ? 74  LYS   A CG  1 
ATOM   471  C  CD  . LYS   A 1 67  ? -17.47191 35.97257 13.53060 1.000 73.50846  ? 74  LYS   A CD  1 
ATOM   472  C  CE  . LYS   A 1 67  ? -16.97129 36.68884 12.28407 1.000 70.96925  ? 74  LYS   A CE  1 
ATOM   473  N  NZ  . LYS   A 1 67  ? -16.80695 35.75276 11.13559 1.000 63.80187  ? 74  LYS   A NZ  1 
ATOM   474  N  N   . GLU   A 1 68  ? -15.67506 34.76020 18.65670 1.000 37.84110  ? 75  GLU   A N   1 
ATOM   475  C  CA  . GLU   A 1 68  ? -15.73596 34.74912 20.11181 1.000 41.15775  ? 75  GLU   A CA  1 
ATOM   476  C  C   . GLU   A 1 68  ? -14.35945 35.01190 20.70714 1.000 40.47948  ? 75  GLU   A C   1 
ATOM   477  O  O   . GLU   A 1 68  ? -13.36229 34.43492 20.26430 1.000 36.40427  ? 75  GLU   A O   1 
ATOM   478  C  CB  . GLU   A 1 68  ? -16.29139 33.41316 20.60502 1.000 47.22690  ? 75  GLU   A CB  1 
ATOM   479  C  CG  . GLU   A 1 68  ? -17.66403 33.07744 20.02130 1.000 57.59393  ? 75  GLU   A CG  1 
ATOM   480  C  CD  . GLU   A 1 68  ? -17.59918 32.03905 18.90504 1.000 80.84628  ? 75  GLU   A CD  1 
ATOM   481  O  OE1 . GLU   A 1 68  ? -18.45416 31.12268 18.88059 1.000 84.93513  ? 75  GLU   A OE1 1 
ATOM   482  O  OE2 . GLU   A 1 68  ? -16.69145 32.14150 18.05002 1.000 68.93242  ? 75  GLU   A OE2 1 
ATOM   483  N  N   . LEU   A 1 69  ? -14.30910 35.89696 21.70449 1.000 40.27710  ? 76  LEU   A N   1 
ATOM   484  C  CA  . LEU   A 1 69  ? -13.08385 36.23094 22.43331 1.000 40.15050  ? 76  LEU   A CA  1 
ATOM   485  C  C   . LEU   A 1 69  ? -13.27896 35.78982 23.88233 1.000 36.83238  ? 76  LEU   A C   1 
ATOM   486  O  O   . LEU   A 1 69  ? -13.99631 36.44608 24.64508 1.000 37.44114  ? 76  LEU   A O   1 
ATOM   487  C  CB  . LEU   A 1 69  ? -12.77305 37.72418 22.33697 1.000 30.70690  ? 76  LEU   A CB  1 
ATOM   488  C  CG  . LEU   A 1 69  ? -12.73208 38.32032 20.92639 1.000 38.27148  ? 76  LEU   A CG  1 
ATOM   489  C  CD1 . LEU   A 1 69  ? -12.47355 39.80885 20.99321 1.000 38.43848  ? 76  LEU   A CD1 1 
ATOM   490  C  CD2 . LEU   A 1 69  ? -11.67728 37.63817 20.07053 1.000 31.12926  ? 76  LEU   A CD2 1 
ATOM   491  N  N   . HIS   A 1 70  ? -12.64817 34.67756 24.25933 1.000 34.66699  ? 77  HIS   A N   1 
ATOM   492  C  CA  . HIS   A 1 70  ? -12.88743 34.06433 25.55897 1.000 33.26455  ? 77  HIS   A CA  1 
ATOM   493  C  C   . HIS   A 1 70  ? -11.65627 33.27508 25.98451 1.000 27.62993  ? 77  HIS   A C   1 
ATOM   494  O  O   . HIS   A 1 70  ? -10.73107 33.04999 25.20016 1.000 27.25241  ? 77  HIS   A O   1 
ATOM   495  C  CB  . HIS   A 1 70  ? -14.12491 33.15335 25.53165 1.000 32.89900  ? 77  HIS   A CB  1 
ATOM   496  C  CG  . HIS   A 1 70  ? -14.03824 32.04143 24.52853 1.000 36.89788  ? 77  HIS   A CG  1 
ATOM   497  N  ND1 . HIS   A 1 70  ? -14.88904 31.94521 23.44781 1.000 42.85409  ? 77  HIS   A ND1 1 
ATOM   498  C  CD2 . HIS   A 1 70  ? -13.20287 30.97817 24.44275 1.000 36.30568  ? 77  HIS   A CD2 1 
ATOM   499  C  CE1 . HIS   A 1 70  ? -14.58196 30.87186 22.74040 1.000 36.89124  ? 77  HIS   A CE1 1 
ATOM   500  N  NE2 . HIS   A 1 70  ? -13.55944 30.26938 23.32085 1.000 39.11344  ? 77  HIS   A NE2 1 
ATOM   501  N  N   . ILE   A 1 71  ? -11.67341 32.84029 27.24564 1.000 31.75005  ? 78  ILE   A N   1 
ATOM   502  C  CA  . ILE   A 1 71  ? -10.60305 32.05900 27.85945 1.000 32.05427  ? 78  ILE   A CA  1 
ATOM   503  C  C   . ILE   A 1 71  ? -11.23385 30.84345 28.53001 1.000 30.48064  ? 78  ILE   A C   1 
ATOM   504  O  O   . ILE   A 1 71  ? -12.13422 30.99107 29.36289 1.000 32.11455  ? 78  ILE   A O   1 
ATOM   505  C  CB  . ILE   A 1 71  ? -9.80813  32.88070 28.88941 1.000 31.23780  ? 78  ILE   A CB  1 
ATOM   506  C  CG1 . ILE   A 1 71  ? -9.21313  34.12766 28.23805 1.000 30.89494  ? 78  ILE   A CG1 1 
ATOM   507  C  CG2 . ILE   A 1 71  ? -8.71734  32.02434 29.53348 1.000 28.26680  ? 78  ILE   A CG2 1 
ATOM   508  C  CD1 . ILE   A 1 71  ? -8.69203  35.15476 29.23347 1.000 30.04754  ? 78  ILE   A CD1 1 
ATOM   509  N  N   . ASN   A 1 72  ? -10.76405 29.64858 28.17816 1.000 30.97325  ? 79  ASN   A N   1 
ATOM   510  C  CA  . ASN   A 1 72  ? -11.26313 28.40870 28.76304 1.000 30.96563  ? 79  ASN   A CA  1 
ATOM   511  C  C   . ASN   A 1 72  ? -10.16464 27.74578 29.58320 1.000 32.77068  ? 79  ASN   A C   1 
ATOM   512  O  O   . ASN   A 1 72  ? -9.02445  27.62820 29.12271 1.000 31.11721  ? 79  ASN   A O   1 
ATOM   513  C  CB  . ASN   A 1 72  ? -11.76402 27.44246 27.68382 1.000 30.79312  ? 79  ASN   A CB  1 
ATOM   514  C  CG  . ASN   A 1 72  ? -13.01111 27.94820 26.97501 1.000 33.60532  ? 79  ASN   A CG  1 
ATOM   515  O  OD1 . ASN   A 1 72  ? -13.75705 28.76614 27.51203 1.000 29.98482  ? 79  ASN   A OD1 1 
ATOM   516  N  ND2 . ASN   A 1 72  ? -13.24156 27.45903 25.76238 1.000 31.62889  ? 79  ASN   A ND2 1 
ATOM   517  N  N   . LEU   A 1 73  ? -10.50889 27.32548 30.79688 1.000 29.87274  ? 80  LEU   A N   1 
ATOM   518  C  CA  . LEU   A 1 73  ? -9.62467  26.53663 31.64250 1.000 31.52919  ? 80  LEU   A CA  1 
ATOM   519  C  C   . LEU   A 1 73  ? -10.15775 25.11227 31.69480 1.000 30.02176  ? 80  LEU   A C   1 
ATOM   520  O  O   . LEU   A 1 73  ? -11.33103 24.89721 32.01465 1.000 32.91836  ? 80  LEU   A O   1 
ATOM   521  C  CB  . LEU   A 1 73  ? -9.52845  27.13781 33.04475 1.000 27.89830  ? 80  LEU   A CB  1 
ATOM   522  C  CG  . LEU   A 1 73  ? -9.26438  28.64191 33.05665 1.000 29.26564  ? 80  LEU   A CG  1 
ATOM   523  C  CD1 . LEU   A 1 73  ? -9.34724  29.18345 34.47151 1.000 25.21503  ? 80  LEU   A CD1 1 
ATOM   524  C  CD2 . LEU   A 1 73  ? -7.91157  28.95996 32.43486 1.000 22.72892  ? 80  LEU   A CD2 1 
ATOM   525  N  N   . ILE   A 1 74  ? -9.30609  24.14970 31.35594 1.000 31.63115  ? 81  ILE   A N   1 
ATOM   526  C  CA  . ILE   A 1 74  ? -9.73241  22.76223 31.19637 1.000 32.30404  ? 81  ILE   A CA  1 
ATOM   527  C  C   . ILE   A 1 74  ? -8.81152  21.85095 32.00027 1.000 32.81095  ? 81  ILE   A C   1 
ATOM   528  O  O   . ILE   A 1 74  ? -7.76794  21.41636 31.49220 1.000 32.02828  ? 81  ILE   A O   1 
ATOM   529  C  CB  . ILE   A 1 74  ? -9.76217  22.35822 29.71213 1.000 32.39988  ? 81  ILE   A CB  1 
ATOM   530  C  CG1 . ILE   A 1 74  ? -10.58089 23.37186 28.90561 1.000 34.65494  ? 81  ILE   A CG1 1 
ATOM   531  C  CG2 . ILE   A 1 74  ? -10.34130 20.96455 29.54578 1.000 28.61190  ? 81  ILE   A CG2 1 
ATOM   532  C  CD1 . ILE   A 1 74  ? -10.53387 23.16566 27.40777 1.000 37.87513  ? 81  ILE   A CD1 1 
ATOM   533  N  N   . PRO   A 1 75  ? -9.14897  21.54330 33.25053 1.000 33.43969  ? 82  PRO   A N   1 
ATOM   534  C  CA  . PRO   A 1 75  ? -8.38503  20.53751 33.99614 1.000 34.31431  ? 82  PRO   A CA  1 
ATOM   535  C  C   . PRO   A 1 75  ? -8.72387  19.12521 33.54261 1.000 42.75047  ? 82  PRO   A C   1 
ATOM   536  O  O   . PRO   A 1 75  ? -9.87378  18.81042 33.22795 1.000 41.55291  ? 82  PRO   A O   1 
ATOM   537  C  CB  . PRO   A 1 75  ? -8.82837  20.76873 35.44590 1.000 41.88472  ? 82  PRO   A CB  1 
ATOM   538  C  CG  . PRO   A 1 75  ? -10.21098 21.30871 35.32241 1.000 37.20248  ? 82  PRO   A CG  1 
ATOM   539  C  CD  . PRO   A 1 75  ? -10.20293 22.16291 34.07462 1.000 33.88704  ? 82  PRO   A CD  1 
ATOM   540  N  N   . ASN   A 1 76  ? -7.70448  18.26597 33.52937 1.000 44.67009  ? 83  ASN   A N   1 
ATOM   541  C  CA  . ASN   A 1 76  ? -7.86946  16.85296 33.18580 1.000 43.23342  ? 83  ASN   A CA  1 
ATOM   542  C  C   . ASN   A 1 76  ? -7.10553  16.02255 34.20806 1.000 39.96589  ? 83  ASN   A C   1 
ATOM   543  O  O   . ASN   A 1 76  ? -5.87359  15.96469 34.16296 1.000 41.30041  ? 83  ASN   A O   1 
ATOM   544  C  CB  . ASN   A 1 76  ? -7.37210  16.56236 31.76954 1.000 40.91941  ? 83  ASN   A CB  1 
ATOM   545  C  CG  . ASN   A 1 76  ? -7.77303  15.18534 31.28115 1.000 44.91616  ? 83  ASN   A CG  1 
ATOM   546  O  OD1 . ASN   A 1 76  ? -7.65235  14.18959 31.99977 1.000 48.39552  ? 83  ASN   A OD1 1 
ATOM   547  N  ND2 . ASN   A 1 76  ? -8.25718  15.12168 30.05085 1.000 46.59248  ? 83  ASN   A ND2 1 
ATOM   548  N  N   . LYS   A 1 77  ? -7.83535  15.37058 35.11595 1.000 41.99187  ? 84  LYS   A N   1 
ATOM   549  C  CA  . LYS   A 1 77  ? -7.20061  14.61760 36.19163 1.000 48.72825  ? 84  LYS   A CA  1 
ATOM   550  C  C   . LYS   A 1 77  ? -6.58522  13.30829 35.71077 1.000 53.98955  ? 84  LYS   A C   1 
ATOM   551  O  O   . LYS   A 1 77  ? -5.62319  12.82907 36.31954 1.000 56.71509  ? 84  LYS   A O   1 
ATOM   552  C  CB  . LYS   A 1 77  ? -8.21357  14.32851 37.30047 1.000 53.61646  ? 84  LYS   A CB  1 
ATOM   553  C  CG  . LYS   A 1 77  ? -8.07368  15.21865 38.51869 1.000 55.92530  ? 84  LYS   A CG  1 
ATOM   554  C  CD  . LYS   A 1 77  ? -9.37506  15.29179 39.29795 1.000 57.38502  ? 84  LYS   A CD  1 
ATOM   555  C  CE  . LYS   A 1 77  ? -9.29519  16.33390 40.39675 1.000 56.73930  ? 84  LYS   A CE  1 
ATOM   556  N  NZ  . LYS   A 1 77  ? -10.15688 15.97757 41.55521 1.000 61.47014  ? 84  LYS   A NZ  1 
ATOM   557  N  N   . GLN   A 1 78  ? -7.12256  12.70687 34.64402 1.000 55.61721  ? 85  GLN   A N   1 
ATOM   558  C  CA  . GLN   A 1 78  ? -6.58007  11.43478 34.17204 1.000 57.03219  ? 85  GLN   A CA  1 
ATOM   559  C  C   . GLN   A 1 78  ? -5.24771  11.62857 33.45568 1.000 52.91890  ? 85  GLN   A C   1 
ATOM   560  O  O   . GLN   A 1 78  ? -4.32005  10.83149 33.63689 1.000 58.26236  ? 85  GLN   A O   1 
ATOM   561  C  CB  . GLN   A 1 78  ? -7.58972  10.72931 33.26319 1.000 59.32583  ? 85  GLN   A CB  1 
ATOM   562  C  CG  . GLN   A 1 78  ? -7.53890  9.19644  33.33848 1.000 76.46443  ? 85  GLN   A CG  1 
ATOM   563  C  CD  . GLN   A 1 78  ? -8.12234  8.61274  34.62708 1.000 88.43133  ? 85  GLN   A CD  1 
ATOM   564  O  OE1 . GLN   A 1 78  ? -8.19333  9.28213  35.65961 1.000 88.80020  ? 85  GLN   A OE1 1 
ATOM   565  N  NE2 . GLN   A 1 78  ? -8.52604  7.34516  34.56854 1.000 72.61040  ? 85  GLN   A NE2 1 
ATOM   566  N  N   . ASP   A 1 79  ? -5.12960  12.67937 32.64274 1.000 49.45839  ? 86  ASP   A N   1 
ATOM   567  C  CA  . ASP   A 1 79  ? -3.86247  13.01041 31.99880 1.000 50.80656  ? 86  ASP   A CA  1 
ATOM   568  C  C   . ASP   A 1 79  ? -2.95833  13.86668 32.87514 1.000 52.45859  ? 86  ASP   A C   1 
ATOM   569  O  O   . ASP   A 1 79  ? -1.80133  14.09618 32.50098 1.000 40.61649  ? 86  ASP   A O   1 
ATOM   570  C  CB  . ASP   A 1 79  ? -4.10907  13.75033 30.68032 1.000 48.92147  ? 86  ASP   A CB  1 
ATOM   571  C  CG  . ASP   A 1 79  ? -4.95374  12.95125 29.70815 1.000 66.52977  ? 86  ASP   A CG  1 
ATOM   572  O  OD1 . ASP   A 1 79  ? -5.25711  11.77376 30.00401 1.000 61.49496  ? 86  ASP   A OD1 1 
ATOM   573  O  OD2 . ASP   A 1 79  ? -5.31713  13.50804 28.64740 1.000 65.59388  ? 86  ASP   A OD2 1 
ATOM   574  N  N   . ARG   A 1 80  ? -3.46070  14.34293 34.01535 1.000 50.10844  ? 87  ARG   A N   1 
ATOM   575  C  CA  . ARG   A 1 80  ? -2.75014  15.29273 34.86953 1.000 42.10668  ? 87  ARG   A CA  1 
ATOM   576  C  C   . ARG   A 1 80  ? -2.27424  16.50260 34.06714 1.000 38.25063  ? 87  ARG   A C   1 
ATOM   577  O  O   . ARG   A 1 80  ? -1.10877  16.90066 34.12266 1.000 37.12344  ? 87  ARG   A O   1 
ATOM   578  C  CB  . ARG   A 1 80  ? -1.58469  14.61723 35.59305 1.000 39.66032  ? 87  ARG   A CB  1 
ATOM   579  C  CG  . ARG   A 1 80  ? -1.28812  15.20808 36.96042 1.000 49.17726  ? 87  ARG   A CG  1 
ATOM   580  C  CD  . ARG   A 1 80  ? 0.17633   15.03546 37.32583 1.000 45.00250  ? 87  ARG   A CD  1 
ATOM   581  N  NE  . ARG   A 1 80  ? 0.47458   13.64839 37.64985 1.000 57.41734  ? 87  ARG   A NE  1 
ATOM   582  C  CZ  . ARG   A 1 80  ? 1.64480   13.06400 37.43790 1.000 63.73498  ? 87  ARG   A CZ  1 
ATOM   583  N  NH1 . ARG   A 1 80  ? 2.66381   13.72594 36.90902 1.000 57.25450  ? 87  ARG   A NH1 1 
ATOM   584  N  NH2 . ARG   A 1 80  ? 1.79562   11.78427 37.76357 1.000 53.65149  ? 87  ARG   A NH2 1 
ATOM   585  N  N   . THR   A 1 81  ? -3.19482  17.08959 33.30314 1.000 35.24361  ? 88  THR   A N   1 
ATOM   586  C  CA  . THR   A 1 81  ? -2.90870  18.29286 32.53613 1.000 35.36109  ? 88  THR   A CA  1 
ATOM   587  C  C   . THR   A 1 81  ? -3.92443  19.37905 32.85192 1.000 38.19543  ? 88  THR   A C   1 
ATOM   588  O  O   . THR   A 1 81  ? -5.09600  19.10478 33.13198 1.000 34.91825  ? 88  THR   A O   1 
ATOM   589  C  CB  . THR   A 1 81  ? -2.92260  18.05262 31.01519 1.000 38.39690  ? 88  THR   A CB  1 
ATOM   590  O  OG1 . THR   A 1 81  ? -4.24625  17.69929 30.59675 1.000 40.74227  ? 88  THR   A OG1 1 
ATOM   591  C  CG2 . THR   A 1 81  ? -1.94613  16.95311 30.62612 1.000 40.21159  ? 88  THR   A CG2 1 
ATOM   592  N  N   . LEU   A 1 82  ? -3.45175  20.61962 32.79690 1.000 34.56746  ? 89  LEU   A N   1 
ATOM   593  C  CA  . LEU   A 1 82  ? -4.29415  21.80302 32.84333 1.000 33.17236  ? 89  LEU   A CA  1 
ATOM   594  C  C   . LEU   A 1 82  ? -4.09308  22.57447 31.54847 1.000 31.24342  ? 89  LEU   A C   1 
ATOM   595  O  O   . LEU   A 1 82  ? -2.95645  22.88651 31.17767 1.000 31.35184  ? 89  LEU   A O   1 
ATOM   596  C  CB  . LEU   A 1 82  ? -3.95353  22.68185 34.04507 1.000 27.38052  ? 89  LEU   A CB  1 
ATOM   597  C  CG  . LEU   A 1 82  ? -4.76022  23.97503 34.12916 1.000 31.15330  ? 89  LEU   A CG  1 
ATOM   598  C  CD1 . LEU   A 1 82  ? -6.23183  23.67270 34.35044 1.000 29.70880  ? 89  LEU   A CD1 1 
ATOM   599  C  CD2 . LEU   A 1 82  ? -4.21868  24.87443 35.22396 1.000 30.41391  ? 89  LEU   A CD2 1 
ATOM   600  N  N   . THR   A 1 83  ? -5.18802  22.87556 30.86051 1.000 33.79595  ? 90  THR   A N   1 
ATOM   601  C  CA  . THR   A 1 83  ? -5.13530  23.55482 29.57453 1.000 26.79391  ? 90  THR   A CA  1 
ATOM   602  C  C   . THR   A 1 83  ? -5.80104  24.91841 29.68551 1.000 29.29741  ? 90  THR   A C   1 
ATOM   603  O  O   . THR   A 1 83  ? -6.91833  25.02877 30.19872 1.000 28.80161  ? 90  THR   A O   1 
ATOM   604  C  CB  . THR   A 1 83  ? -5.80621  22.71593 28.48584 1.000 26.65519  ? 90  THR   A CB  1 
ATOM   605  O  OG1 . THR   A 1 83  ? -5.13779  21.45423 28.38593 1.000 29.65495  ? 90  THR   A OG1 1 
ATOM   606  C  CG2 . THR   A 1 83  ? -5.73011  23.41741 27.14706 1.000 30.46133  ? 90  THR   A CG2 1 
ATOM   607  N  N   . ILE   A 1 84  ? -5.10369  25.95019 29.21680 1.000 35.31575  ? 91  ILE   A N   1 
ATOM   608  C  CA  . ILE   A 1 84  ? -5.63335  27.30541 29.11014 1.000 31.74632  ? 91  ILE   A CA  1 
ATOM   609  C  C   . ILE   A 1 84  ? -5.78372  27.61061 27.62161 1.000 34.14948  ? 91  ILE   A C   1 
ATOM   610  O  O   . ILE   A 1 84  ? -4.78640  27.65928 26.88997 1.000 28.57248  ? 91  ILE   A O   1 
ATOM   611  C  CB  . ILE   A 1 84  ? -4.71994  28.32804 29.80176 1.000 27.74143  ? 91  ILE   A CB  1 
ATOM   612  C  CG1 . ILE   A 1 84  ? -4.58599  28.00566 31.29082 1.000 38.77949  ? 91  ILE   A CG1 1 
ATOM   613  C  CG2 . ILE   A 1 84  ? -5.26362  29.74096 29.63487 1.000 26.74907  ? 91  ILE   A CG2 1 
ATOM   614  C  CD1 . ILE   A 1 84  ? -3.32867  27.26021 31.65573 1.000 37.07240  ? 91  ILE   A CD1 1 
ATOM   615  N  N   . VAL   A 1 85  ? -7.02393  27.79683 27.16464 1.000 26.00858  ? 92  VAL   A N   1 
ATOM   616  C  CA  . VAL   A 1 85  ? -7.32765  28.09965 25.76660 1.000 27.61419  ? 92  VAL   A CA  1 
ATOM   617  C  C   . VAL   A 1 85  ? -7.81694  29.53598 25.66506 1.000 36.20669  ? 92  VAL   A C   1 
ATOM   618  O  O   . VAL   A 1 85  ? -8.73630  29.93536 26.39067 1.000 32.49425  ? 92  VAL   A O   1 
ATOM   619  C  CB  . VAL   A 1 85  ? -8.39099  27.15194 25.18776 1.000 32.89496  ? 92  VAL   A CB  1 
ATOM   620  C  CG1 . VAL   A 1 85  ? -8.46212  27.30737 23.66741 1.000 24.43446  ? 92  VAL   A CG1 1 
ATOM   621  C  CG2 . VAL   A 1 85  ? -8.11435  25.71445 25.58784 1.000 37.75471  ? 92  VAL   A CG2 1 
ATOM   622  N  N   . ASP   A 1 86  ? -7.22100  30.30413 24.75139 1.000 31.96414  ? 93  ASP   A N   1 
ATOM   623  C  CA  . ASP   A 1 86  ? -7.73824  31.61305 24.38093 1.000 28.64088  ? 93  ASP   A CA  1 
ATOM   624  C  C   . ASP   A 1 86  ? -7.88072  31.69219 22.86634 1.000 31.07046  ? 93  ASP   A C   1 
ATOM   625  O  O   . ASP   A 1 86  ? -7.18664  30.99453 22.12167 1.000 33.48982  ? 93  ASP   A O   1 
ATOM   626  C  CB  . ASP   A 1 86  ? -6.84426  32.75533 24.90439 1.000 27.16725  ? 93  ASP   A CB  1 
ATOM   627  C  CG  . ASP   A 1 86  ? -5.52988  32.88811 24.13875 1.000 38.43576  ? 93  ASP   A CG  1 
ATOM   628  O  OD1 . ASP   A 1 86  ? -5.54273  33.33393 22.96593 1.000 39.72412  ? 93  ASP   A OD1 1 
ATOM   629  O  OD2 . ASP   A 1 86  ? -4.47068  32.57913 24.72489 1.000 39.37881  ? 93  ASP   A OD2 1 
ATOM   630  N  N   . THR   A 1 87  ? -8.79878  32.54352 22.41576 1.000 28.48216  ? 94  THR   A N   1 
ATOM   631  C  CA  . THR   A 1 87  ? -8.99312  32.81093 20.99309 1.000 27.93798  ? 94  THR   A CA  1 
ATOM   632  C  C   . THR   A 1 87  ? -8.36098  34.13825 20.58816 1.000 33.85698  ? 94  THR   A C   1 
ATOM   633  O  O   . THR   A 1 87  ? -8.92800  34.91868 19.80912 1.000 30.26788  ? 94  THR   A O   1 
ATOM   634  C  CB  . THR   A 1 87  ? -10.47847 32.78028 20.64609 1.000 31.58344  ? 94  THR   A CB  1 
ATOM   635  O  OG1 . THR   A 1 87  ? -11.19525 33.64530 21.53302 1.000 29.01372  ? 94  THR   A OG1 1 
ATOM   636  C  CG2 . THR   A 1 87  ? -11.02495 31.35825 20.79333 1.000 30.92770  ? 94  THR   A CG2 1 
ATOM   637  N  N   . GLY   A 1 88  ? -7.16803  34.40590 21.11338 1.000 30.51808  ? 95  GLY   A N   1 
ATOM   638  C  CA  . GLY   A 1 88  ? -6.45911  35.63704 20.84677 1.000 29.24949  ? 95  GLY   A CA  1 
ATOM   639  C  C   . GLY   A 1 88  ? -5.82377  35.64500 19.47492 1.000 31.17763  ? 95  GLY   A C   1 
ATOM   640  O  O   . GLY   A 1 88  ? -6.14693  34.83909 18.59978 1.000 30.05607  ? 95  GLY   A O   1 
ATOM   641  N  N   . ILE   A 1 89  ? -4.89270  36.58252 19.29206 1.000 28.13721  ? 96  ILE   A N   1 
ATOM   642  C  CA  . ILE   A 1 89  ? -4.26475  36.75768 17.99040 1.000 30.79109  ? 96  ILE   A CA  1 
ATOM   643  C  C   . ILE   A 1 89  ? -3.42514  35.54573 17.58774 1.000 25.64915  ? 96  ILE   A C   1 
ATOM   644  O  O   . ILE   A 1 89  ? -3.20788  35.32040 16.39277 1.000 28.81294  ? 96  ILE   A O   1 
ATOM   645  C  CB  . ILE   A 1 89  ? -3.43274  38.05693 17.99583 1.000 31.05131  ? 96  ILE   A CB  1 
ATOM   646  C  CG1 . ILE   A 1 89  ? -3.14580  38.52691 16.56609 1.000 35.97227  ? 96  ILE   A CG1 1 
ATOM   647  C  CG2 . ILE   A 1 89  ? -2.13959  37.87316 18.78860 1.000 26.46821  ? 96  ILE   A CG2 1 
ATOM   648  C  CD1 . ILE   A 1 89  ? -2.85104  40.01790 16.45974 1.000 32.82471  ? 96  ILE   A CD1 1 
ATOM   649  N  N   . GLY   A 1 90  ? -2.97017  34.73970 18.54466 1.000 26.17733  ? 97  GLY   A N   1 
ATOM   650  C  CA  . GLY   A 1 90  ? -2.13991  33.59569 18.22860 1.000 28.71963  ? 97  GLY   A CA  1 
ATOM   651  C  C   . GLY   A 1 90  ? -0.70091  34.00282 17.97660 1.000 31.39323  ? 97  GLY   A C   1 
ATOM   652  O  O   . GLY   A 1 90  ? -0.31736  35.16592 18.09155 1.000 32.51339  ? 97  GLY   A O   1 
ATOM   653  N  N   . MET   A 1 91  ? 0.11290   33.01562 17.61136 1.000 29.28428  ? 98  MET   A N   1 
ATOM   654  C  CA  . MET   A 1 91  ? 1.53920   33.22260 17.40333 1.000 28.67105  ? 98  MET   A CA  1 
ATOM   655  C  C   . MET   A 1 91  ? 1.97866   32.59618 16.08860 1.000 30.80674  ? 98  MET   A C   1 
ATOM   656  O  O   . MET   A 1 91  ? 1.57764   31.47423 15.75758 1.000 37.23152  ? 98  MET   A O   1 
ATOM   657  C  CB  . MET   A 1 91  ? 2.37547   32.61981 18.55014 1.000 33.06387  ? 98  MET   A CB  1 
ATOM   658  C  CG  . MET   A 1 91  ? 2.31313   33.37810 19.87745 1.000 31.06492  ? 98  MET   A CG  1 
ATOM   659  S  SD  . MET   A 1 91  ? 3.01602   32.43995 21.25852 1.000 41.86254  ? 98  MET   A SD  1 
ATOM   660  C  CE  . MET   A 1 91  ? 1.86542   31.08243 21.42222 1.000 32.91749  ? 98  MET   A CE  1 
ATOM   661  N  N   . THR   A 1 92  ? 2.83109   33.31220 15.35926 1.000 33.14517  ? 99  THR   A N   1 
ATOM   662  C  CA  . THR   A 1 92  ? 3.43477   32.79070 14.14270 1.000 32.81943  ? 99  THR   A CA  1 
ATOM   663  C  C   . THR   A 1 92  ? 4.62892   31.89457 14.47236 1.000 38.31598  ? 99  THR   A C   1 
ATOM   664  O  O   . THR   A 1 92  ? 5.07912   31.79935 15.61795 1.000 34.10604  ? 99  THR   A O   1 
ATOM   665  C  CB  . THR   A 1 92  ? 3.89355   33.92996 13.23371 1.000 38.12190  ? 99  THR   A CB  1 
ATOM   666  O  OG1 . THR   A 1 92  ? 4.90932   34.68889 13.90420 1.000 34.62391  ? 99  THR   A OG1 1 
ATOM   667  C  CG2 . THR   A 1 92  ? 2.72799   34.84140 12.87728 1.000 33.42718  ? 99  THR   A CG2 1 
ATOM   668  N  N   . LYS   A 1 93  ? 5.15425   31.23674 13.43637 1.000 33.32650  ? 100 LYS   A N   1 
ATOM   669  C  CA  . LYS   A 1 93  ? 6.35975   30.43616 13.61604 1.000 40.95486  ? 100 LYS   A CA  1 
ATOM   670  C  C   . LYS   A 1 93  ? 7.54672   31.30786 14.00802 1.000 37.16809  ? 100 LYS   A C   1 
ATOM   671  O  O   . LYS   A 1 93  ? 8.34779   30.92330 14.86745 1.000 38.83515  ? 100 LYS   A O   1 
ATOM   672  C  CB  . LYS   A 1 93  ? 6.67161   29.64848 12.34224 1.000 42.40152  ? 100 LYS   A CB  1 
ATOM   673  C  CG  . LYS   A 1 93  ? 7.76324   28.59476 12.52134 1.000 42.05609  ? 100 LYS   A CG  1 
ATOM   674  C  CD  . LYS   A 1 93  ? 8.15275   27.96172 11.18857 1.000 45.82769  ? 100 LYS   A CD  1 
ATOM   675  C  CE  . LYS   A 1 93  ? 9.10688   26.78757 11.37068 1.000 50.95039  ? 100 LYS   A CE  1 
ATOM   676  N  NZ  . LYS   A 1 93  ? 9.94871   26.57336 10.15065 1.000 61.85939  ? 100 LYS   A NZ  1 
ATOM   677  N  N   . ALA   A 1 94  ? 7.67397   32.48835 13.39671 1.000 32.89689  ? 101 ALA   A N   1 
ATOM   678  C  CA  . ALA   A 1 94  ? 8.76077   33.39093 13.76458 1.000 33.93235  ? 101 ALA   A CA  1 
ATOM   679  C  C   . ALA   A 1 94  ? 8.66879   33.81995 15.22832 1.000 41.12630  ? 101 ALA   A C   1 
ATOM   680  O  O   . ALA   A 1 94  ? 9.69978   33.96418 15.89609 1.000 41.95368  ? 101 ALA   A O   1 
ATOM   681  C  CB  . ALA   A 1 94  ? 8.76536   34.60891 12.84127 1.000 32.41714  ? 101 ALA   A CB  1 
ATOM   682  N  N   . ASP   A 1 95  ? 7.45315   34.01515 15.74917 1.000 33.55720  ? 102 ASP   A N   1 
ATOM   683  C  CA  . ASP   A 1 95  ? 7.29510   34.32535 17.16965 1.000 30.08262  ? 102 ASP   A CA  1 
ATOM   684  C  C   . ASP   A 1 95  ? 7.81990   33.19079 18.04361 1.000 38.85158  ? 102 ASP   A C   1 
ATOM   685  O  O   . ASP   A 1 95  ? 8.57796   33.41983 18.99412 1.000 39.84843  ? 102 ASP   A O   1 
ATOM   686  C  CB  . ASP   A 1 95  ? 5.82509   34.59564 17.49365 1.000 33.55255  ? 102 ASP   A CB  1 
ATOM   687  C  CG  . ASP   A 1 95  ? 5.27725   35.82707 16.78733 1.000 39.48455  ? 102 ASP   A CG  1 
ATOM   688  O  OD1 . ASP   A 1 95  ? 6.02673   36.81174 16.61496 1.000 45.23679  ? 102 ASP   A OD1 1 
ATOM   689  O  OD2 . ASP   A 1 95  ? 4.08382   35.81867 16.41684 1.000 40.94255  ? 102 ASP   A OD2 1 
ATOM   690  N  N   . LEU   A 1 96  ? 7.42560   31.95188 17.72682 1.000 38.91001  ? 103 LEU   A N   1 
ATOM   691  C  CA  . LEU   A 1 96  ? 7.78755   30.80136 18.54962 1.000 36.08834  ? 103 LEU   A CA  1 
ATOM   692  C  C   . LEU   A 1 96  ? 9.28776   30.55186 18.56905 1.000 32.16344  ? 103 LEU   A C   1 
ATOM   693  O  O   . LEU   A 1 96  ? 9.81245   30.04197 19.56366 1.000 40.23183  ? 103 LEU   A O   1 
ATOM   694  C  CB  . LEU   A 1 96  ? 7.07473   29.55016 18.04524 1.000 36.00233  ? 103 LEU   A CB  1 
ATOM   695  C  CG  . LEU   A 1 96  ? 5.56000   29.52182 18.21445 1.000 33.88718  ? 103 LEU   A CG  1 
ATOM   696  C  CD1 . LEU   A 1 96  ? 5.00640   28.26679 17.56267 1.000 31.46772  ? 103 LEU   A CD1 1 
ATOM   697  C  CD2 . LEU   A 1 96  ? 5.19835   29.57267 19.68262 1.000 27.98610  ? 103 LEU   A CD2 1 
ATOM   698  N  N   . ILE   A 1 97  ? 9.98860   30.89076 17.49277 1.000 29.85962  ? 104 ILE   A N   1 
ATOM   699  C  CA  . ILE   A 1 97  ? 11.40500  30.58475 17.35980 1.000 41.95156  ? 104 ILE   A CA  1 
ATOM   700  C  C   . ILE   A 1 97  ? 12.28145  31.78714 17.69112 1.000 43.04353  ? 104 ILE   A C   1 
ATOM   701  O  O   . ILE   A 1 97  ? 13.29392  31.64491 18.37679 1.000 50.29965  ? 104 ILE   A O   1 
ATOM   702  C  CB  . ILE   A 1 97  ? 11.70505  30.06353 15.93749 1.000 45.09804  ? 104 ILE   A CB  1 
ATOM   703  C  CG1 . ILE   A 1 97  ? 10.99521  28.73475 15.68227 1.000 40.79360  ? 104 ILE   A CG1 1 
ATOM   704  C  CG2 . ILE   A 1 97  ? 13.20347  29.91153 15.72562 1.000 41.03456  ? 104 ILE   A CG2 1 
ATOM   705  C  CD1 . ILE   A 1 97  ? 11.07347  28.29815 14.23513 1.000 41.95044  ? 104 ILE   A CD1 1 
ATOM   706  N  N   . ASN   A 1 98  ? 11.91713  32.97752 17.21234 1.000 40.77268  ? 105 ASN   A N   1 
ATOM   707  C  CA  . ASN   A 1 98  ? 12.81707  34.12842 17.24761 1.000 50.02325  ? 105 ASN   A CA  1 
ATOM   708  C  C   . ASN   A 1 98  ? 12.27933  35.28596 18.07808 1.000 42.34909  ? 105 ASN   A C   1 
ATOM   709  O  O   . ASN   A 1 98  ? 12.91120  35.66900 19.06652 1.000 47.10646  ? 105 ASN   A O   1 
ATOM   710  C  CB  . ASN   A 1 98  ? 13.11083  34.60339 15.81769 1.000 40.28528  ? 105 ASN   A CB  1 
ATOM   711  C  CG  . ASN   A 1 98  ? 14.44502  34.10994 15.30442 1.000 60.05844  ? 105 ASN   A CG  1 
ATOM   712  O  OD1 . ASN   A 1 98  ? 14.50461  33.31429 14.36767 1.000 57.83846  ? 105 ASN   A OD1 1 
ATOM   713  N  ND2 . ASN   A 1 98  ? 15.52845  34.57804 15.92078 1.000 61.21818  ? 105 ASN   A ND2 1 
ATOM   714  N  N   . ASN   A 1 99  ? 11.13386  35.85807 17.70398 1.000 38.72208  ? 106 ASN   A N   1 
ATOM   715  C  CA  . ASN   A 1 99  ? 10.74879  37.17012 18.21508 1.000 38.76167  ? 106 ASN   A CA  1 
ATOM   716  C  C   . ASN   A 1 99  ? 10.49613  37.13951 19.71905 1.000 40.70108  ? 106 ASN   A C   1 
ATOM   717  O  O   . ASN   A 1 99  ? 10.95630  38.02207 20.45337 1.000 42.79599  ? 106 ASN   A O   1 
ATOM   718  C  CB  . ASN   A 1 99  ? 9.51308   37.66872 17.46657 1.000 39.22784  ? 106 ASN   A CB  1 
ATOM   719  C  CG  . ASN   A 1 99  ? 9.69954   37.65501 15.95607 1.000 47.77274  ? 106 ASN   A CG  1 
ATOM   720  O  OD1 . ASN   A 1 99  ? 10.81558  37.80569 15.45138 1.000 40.75091  ? 106 ASN   A OD1 1 
ATOM   721  N  ND2 . ASN   A 1 99  ? 8.60272   37.46774 15.22785 1.000 41.62161  ? 106 ASN   A ND2 1 
ATOM   722  N  N   . LEU   A 1 100 ? 9.75321   36.13769 20.19576 1.000 38.77764  ? 107 LEU   A N   1 
ATOM   723  C  CA  . LEU   A 1 100 ? 9.41934   36.08390 21.61532 1.000 43.57881  ? 107 LEU   A CA  1 
ATOM   724  C  C   . LEU   A 1 100 ? 10.65663  35.83716 22.47205 1.000 40.25133  ? 107 LEU   A C   1 
ATOM   725  O  O   . LEU   A 1 100 ? 10.77905  36.39804 23.56566 1.000 43.06539  ? 107 LEU   A O   1 
ATOM   726  C  CB  . LEU   A 1 100 ? 8.36335   35.00912 21.86484 1.000 41.50280  ? 107 LEU   A CB  1 
ATOM   727  C  CG  . LEU   A 1 100 ? 6.93113   35.32135 21.42020 1.000 39.95633  ? 107 LEU   A CG  1 
ATOM   728  C  CD1 . LEU   A 1 100 ? 6.01519   34.16902 21.77904 1.000 43.05504  ? 107 LEU   A CD1 1 
ATOM   729  C  CD2 . LEU   A 1 100 ? 6.42864   36.61076 22.04993 1.000 39.86451  ? 107 LEU   A CD2 1 
ATOM   730  N  N   . GLY   A 1 101 ? 11.58216  35.00173 21.99793 1.000 41.08013  ? 108 GLY   A N   1 
ATOM   731  C  CA  . GLY   A 1 101 ? 12.81914  34.79480 22.72730 1.000 42.91481  ? 108 GLY   A CA  1 
ATOM   732  C  C   . GLY   A 1 101 ? 13.71887  36.01408 22.72494 1.000 45.29683  ? 108 GLY   A C   1 
ATOM   733  O  O   . GLY   A 1 101 ? 14.45777  36.24346 23.68459 1.000 50.38438  ? 108 GLY   A O   1 
ATOM   734  N  N   . THR   A 1 102 ? 13.67079  36.80749 21.65432 1.000 42.24174  ? 109 THR   A N   1 
ATOM   735  C  CA  . THR   A 1 102 ? 14.43825  38.04789 21.61775 1.000 40.77071  ? 109 THR   A CA  1 
ATOM   736  C  C   . THR   A 1 102 ? 13.89012  39.06961 22.60634 1.000 41.81567  ? 109 THR   A C   1 
ATOM   737  O  O   . THR   A 1 102 ? 14.65885  39.71281 23.33126 1.000 36.46195  ? 109 THR   A O   1 
ATOM   738  C  CB  . THR   A 1 102 ? 14.43864  38.61682 20.20235 1.000 36.19698  ? 109 THR   A CB  1 
ATOM   739  O  OG1 . THR   A 1 102 ? 15.09187  37.69284 19.32058 1.000 51.54703  ? 109 THR   A OG1 1 
ATOM   740  C  CG2 . THR   A 1 102 ? 15.15656  39.96492 20.16511 1.000 38.99856  ? 109 THR   A CG2 1 
ATOM   741  N  N   . ILE   A 1 103 ? 12.56508  39.23045 22.65213 1.000 44.09975  ? 110 ILE   A N   1 
ATOM   742  C  CA  . ILE   A 1 103 ? 11.95971  40.16343 23.59966 1.000 45.04301  ? 110 ILE   A CA  1 
ATOM   743  C  C   . ILE   A 1 103 ? 12.22521  39.71570 25.03384 1.000 46.01622  ? 110 ILE   A C   1 
ATOM   744  O  O   . ILE   A 1 103 ? 12.51864  40.53376 25.91388 1.000 47.18324  ? 110 ILE   A O   1 
ATOM   745  C  CB  . ILE   A 1 103 ? 10.45050  40.30310 23.31940 1.000 41.27617  ? 110 ILE   A CB  1 
ATOM   746  C  CG1 . ILE   A 1 103 ? 10.21487  40.99651 21.98079 1.000 45.22561  ? 110 ILE   A CG1 1 
ATOM   747  C  CG2 . ILE   A 1 103 ? 9.77450   41.11192 24.42148 1.000 41.89039  ? 110 ILE   A CG2 1 
ATOM   748  C  CD1 . ILE   A 1 103 ? 11.01949  42.26158 21.80926 1.000 47.30694  ? 110 ILE   A CD1 1 
ATOM   749  N  N   . ALA   A 1 104 ? 12.13234  38.41057 25.29466 1.000 40.85653  ? 111 ALA   A N   1 
ATOM   750  C  CA  . ALA   A 1 104 ? 12.29738  37.90608 26.65238 1.000 39.76052  ? 111 ALA   A CA  1 
ATOM   751  C  C   . ALA   A 1 104 ? 13.74789  37.91495 27.11226 1.000 48.97594  ? 111 ALA   A C   1 
ATOM   752  O  O   . ALA   A 1 104 ? 14.00217  37.76962 28.31342 1.000 48.13820  ? 111 ALA   A O   1 
ATOM   753  C  CB  . ALA   A 1 104 ? 11.73815  36.49214 26.75577 1.000 37.83069  ? 111 ALA   A CB  1 
ATOM   754  N  N   . LYS   A 1 105 ? 14.69548  38.08384 26.18720 1.000 49.41179  ? 112 LYS   A N   1 
ATOM   755  C  CA  . LYS   A 1 105 ? 16.10939  38.12916 26.54917 1.000 41.47962  ? 112 LYS   A CA  1 
ATOM   756  C  C   . LYS   A 1 105 ? 16.38779  39.24019 27.55525 1.000 39.97907  ? 112 LYS   A C   1 
ATOM   757  O  O   . LYS   A 1 105 ? 17.10871  39.03843 28.53915 1.000 51.32097  ? 112 LYS   A O   1 
ATOM   758  C  CB  . LYS   A 1 105 ? 16.95173  38.32538 25.28923 1.000 50.34759  ? 112 LYS   A CB  1 
ATOM   759  C  CG  . LYS   A 1 105 ? 18.30337  37.65282 25.30518 1.000 59.48756  ? 112 LYS   A CG  1 
ATOM   760  C  CD  . LYS   A 1 105 ? 19.21354  38.25929 24.24334 1.000 51.83037  ? 112 LYS   A CD  1 
ATOM   761  C  CE  . LYS   A 1 105 ? 20.58992  37.61631 24.26638 1.000 60.06822  ? 112 LYS   A CE  1 
ATOM   762  N  NZ  . LYS   A 1 105 ? 21.55930  38.39772 25.08234 1.000 53.80644  ? 112 LYS   A NZ  1 
ATOM   763  N  N   . SER   A 1 106 ? 15.81907  40.42530 27.32427 1.000 42.47020  ? 113 SER   A N   1 
ATOM   764  C  CA  . SER   A 1 106 ? 16.08470  41.56330 28.19848 1.000 46.11768  ? 113 SER   A CA  1 
ATOM   765  C  C   . SER   A 1 106 ? 15.23523  41.51666 29.45965 1.000 38.35188  ? 113 SER   A C   1 
ATOM   766  O  O   . SER   A 1 106 ? 15.70877  41.88402 30.54076 1.000 43.31813  ? 113 SER   A O   1 
ATOM   767  C  CB  . SER   A 1 106 ? 15.84562  42.87331 27.44641 1.000 50.07673  ? 113 SER   A CB  1 
ATOM   768  O  OG  . SER   A 1 106 ? 14.79547  42.72906 26.50902 1.000 56.38273  ? 113 SER   A OG  1 
ATOM   769  N  N   . GLY   A 1 107 ? 13.97725  41.08859 29.33961 1.000 41.28423  ? 114 GLY   A N   1 
ATOM   770  C  CA  . GLY   A 1 107 ? 13.13764  40.95069 30.51502 1.000 41.84308  ? 114 GLY   A CA  1 
ATOM   771  C  C   . GLY   A 1 107 ? 13.65868  39.91847 31.49330 1.000 42.29426  ? 114 GLY   A C   1 
ATOM   772  O  O   . GLY   A 1 107 ? 13.58437  40.11978 32.70832 1.000 38.26426  ? 114 GLY   A O   1 
ATOM   773  N  N   . THR   A 1 108 ? 14.20080  38.81145 30.98258 1.000 39.73430  ? 115 THR   A N   1 
ATOM   774  C  CA  . THR   A 1 108 ? 14.81923  37.81672 31.85100 1.000 42.80764  ? 115 THR   A CA  1 
ATOM   775  C  C   . THR   A 1 108 ? 16.02165  38.39792 32.58437 1.000 41.96964  ? 115 THR   A C   1 
ATOM   776  O  O   . THR   A 1 108 ? 16.17979  38.19272 33.79281 1.000 47.43179  ? 115 THR   A O   1 
ATOM   777  C  CB  . THR   A 1 108 ? 15.23306  36.59172 31.03686 1.000 37.90009  ? 115 THR   A CB  1 
ATOM   778  O  OG1 . THR   A 1 108 ? 14.06384  35.89703 30.58684 1.000 40.39127  ? 115 THR   A OG1 1 
ATOM   779  C  CG2 . THR   A 1 108 ? 16.06716  35.66244 31.89536 1.000 45.68107  ? 115 THR   A CG2 1 
ATOM   780  N  N   . LYS   A 1 109 ? 16.88372  39.12210 31.86333 1.000 37.62815  ? 116 LYS   A N   1 
ATOM   781  C  CA  . LYS   A 1 109 ? 18.05721  39.73122 32.48441 1.000 44.54809  ? 116 LYS   A CA  1 
ATOM   782  C  C   . LYS   A 1 109 ? 17.65603  40.70047 33.58843 1.000 46.66933  ? 116 LYS   A C   1 
ATOM   783  O  O   . LYS   A 1 109 ? 18.24137  40.69821 34.67881 1.000 46.51374  ? 116 LYS   A O   1 
ATOM   784  C  CB  . LYS   A 1 109 ? 18.89438  40.44917 31.42653 1.000 41.80430  ? 116 LYS   A CB  1 
ATOM   785  C  CG  . LYS   A 1 109 ? 20.25915  39.84446 31.20458 1.000 64.37067  ? 116 LYS   A CG  1 
ATOM   786  C  CD  . LYS   A 1 109 ? 21.06301  40.64437 30.19110 1.000 70.07765  ? 116 LYS   A CD  1 
ATOM   787  C  CE  . LYS   A 1 109 ? 21.35565  39.80928 28.95166 1.000 75.80192  ? 116 LYS   A CE  1 
ATOM   788  N  NZ  . LYS   A 1 109 ? 22.00819  40.58889 27.85978 1.000 74.88268  ? 116 LYS   A NZ  1 
ATOM   789  N  N   . ALA   A 1 110 ? 16.66226  41.54893 33.31805 1.000 46.60891  ? 117 ALA   A N   1 
ATOM   790  C  CA  . ALA   A 1 110 ? 16.21916  42.50812 34.32412 1.000 48.28287  ? 117 ALA   A CA  1 
ATOM   791  C  C   . ALA   A 1 110 ? 15.60115  41.79829 35.52110 1.000 44.73439  ? 117 ALA   A C   1 
ATOM   792  O  O   . ALA   A 1 110 ? 15.88925  42.14009 36.67533 1.000 45.36041  ? 117 ALA   A O   1 
ATOM   793  C  CB  . ALA   A 1 110 ? 15.22485  43.49419 33.70739 1.000 44.09761  ? 117 ALA   A CB  1 
ATOM   794  N  N   . PHE   A 1 111 ? 14.76109  40.79371 35.26090 1.000 38.58196  ? 118 PHE   A N   1 
ATOM   795  C  CA  . PHE   A 1 111 ? 14.11838  40.05060 36.33757 1.000 40.21847  ? 118 PHE   A CA  1 
ATOM   796  C  C   . PHE   A 1 111 ? 15.14042  39.36442 37.23234 1.000 44.64657  ? 118 PHE   A C   1 
ATOM   797  O  O   . PHE   A 1 111 ? 14.93137  39.25045 38.44551 1.000 45.27903  ? 118 PHE   A O   1 
ATOM   798  C  CB  . PHE   A 1 111 ? 13.15452  39.02625 35.74372 1.000 36.68673  ? 118 PHE   A CB  1 
ATOM   799  C  CG  . PHE   A 1 111 ? 12.41629  38.22446 36.76883 1.000 45.30540  ? 118 PHE   A CG  1 
ATOM   800  C  CD1 . PHE   A 1 111 ? 11.80302  38.84566 37.84103 1.000 44.77825  ? 118 PHE   A CD1 1 
ATOM   801  C  CD2 . PHE   A 1 111 ? 12.33138  36.84857 36.65913 1.000 41.90864  ? 118 PHE   A CD2 1 
ATOM   802  C  CE1 . PHE   A 1 111 ? 11.11933  38.10677 38.78762 1.000 47.59929  ? 118 PHE   A CE1 1 
ATOM   803  C  CE2 . PHE   A 1 111 ? 11.65043  36.10699 37.59711 1.000 39.95877  ? 118 PHE   A CE2 1 
ATOM   804  C  CZ  . PHE   A 1 111 ? 11.04312  36.73550 38.66543 1.000 38.80581  ? 118 PHE   A CZ  1 
ATOM   805  N  N   . MET   A 1 112 ? 16.25419  38.91415 36.65678 1.000 45.29253  ? 119 MET   A N   1 
ATOM   806  C  CA  . MET   A 1 112 ? 17.28883  38.26203 37.45229 1.000 50.03378  ? 119 MET   A CA  1 
ATOM   807  C  C   . MET   A 1 112 ? 18.04088  39.24952 38.32639 1.000 50.76399  ? 119 MET   A C   1 
ATOM   808  O  O   . MET   A 1 112 ? 18.38277  38.93319 39.47293 1.000 60.23995  ? 119 MET   A O   1 
ATOM   809  C  CB  . MET   A 1 112 ? 18.24966  37.52159 36.53898 1.000 47.81855  ? 119 MET   A CB  1 
ATOM   810  C  CG  . MET   A 1 112 ? 17.99449  36.05169 36.53688 1.000 61.72376  ? 119 MET   A CG  1 
ATOM   811  S  SD  . MET   A 1 112 ? 18.51303  35.27414 35.01344 1.000 72.31380  ? 119 MET   A SD  1 
ATOM   812  C  CE  . MET   A 1 112 ? 18.14230  33.59851 35.45667 1.000 52.79147  ? 119 MET   A CE  1 
ATOM   813  N  N   . GLU   A 1 113 ? 18.33101  40.43933 37.79933 1.000 57.24046  ? 120 GLU   A N   1 
ATOM   814  C  CA  . GLU   A 1 113 ? 18.93966  41.46978 38.63208 1.000 60.17277  ? 120 GLU   A CA  1 
ATOM   815  C  C   . GLU   A 1 113 ? 18.03714  41.81944 39.80958 1.000 53.39370  ? 120 GLU   A C   1 
ATOM   816  O  O   . GLU   A 1 113 ? 18.50501  41.93831 40.94818 1.000 64.01495  ? 120 GLU   A O   1 
ATOM   817  C  CB  . GLU   A 1 113 ? 19.23682  42.70824 37.79080 1.000 58.92892  ? 120 GLU   A CB  1 
ATOM   818  C  CG  . GLU   A 1 113 ? 20.64756  42.75098 37.23074 1.000 71.15493  ? 120 GLU   A CG  1 
ATOM   819  C  CD  . GLU   A 1 113 ? 20.69853  43.31819 35.82275 1.000 85.81844  ? 120 GLU   A CD  1 
ATOM   820  O  OE1 . GLU   A 1 113 ? 19.96622  44.29419 35.54873 1.000 88.24585  ? 120 GLU   A OE1 1 
ATOM   821  O  OE2 . GLU   A 1 113 ? 21.47532  42.79184 34.99475 1.000 80.02404  ? 120 GLU   A OE2 1 
ATOM   822  N  N   . ALA   A 1 114 ? 16.73308  41.96255 39.55515 1.000 51.89706  ? 121 ALA   A N   1 
ATOM   823  C  CA  . ALA   A 1 114 ? 15.79812  42.31401 40.61884 1.000 57.91843  ? 121 ALA   A CA  1 
ATOM   824  C  C   . ALA   A 1 114 ? 15.72853  41.22531 41.68167 1.000 57.07193  ? 121 ALA   A C   1 
ATOM   825  O  O   . ALA   A 1 114 ? 15.60885  41.52371 42.87555 1.000 64.74852  ? 121 ALA   A O   1 
ATOM   826  C  CB  . ALA   A 1 114 ? 14.40863  42.58216 40.03422 1.000 52.20511  ? 121 ALA   A CB  1 
ATOM   827  N  N   . LEU   A 1 115 ? 15.80995  39.95628 41.27190 1.000 54.06154  ? 122 LEU   A N   1 
ATOM   828  C  CA  . LEU   A 1 115 ? 15.70269  38.86224 42.23054 1.000 55.73860  ? 122 LEU   A CA  1 
ATOM   829  C  C   . LEU   A 1 115 ? 16.84037  38.87454 43.24527 1.000 65.09850  ? 122 LEU   A C   1 
ATOM   830  O  O   . LEU   A 1 115 ? 16.72676  38.23442 44.29613 1.000 71.00354  ? 122 LEU   A O   1 
ATOM   831  C  CB  . LEU   A 1 115 ? 15.66051  37.52209 41.49476 1.000 47.26665  ? 122 LEU   A CB  1 
ATOM   832  C  CG  . LEU   A 1 115 ? 14.30273  37.14613 40.88154 1.000 57.56825  ? 122 LEU   A CG  1 
ATOM   833  C  CD1 . LEU   A 1 115 ? 14.47091  36.10380 39.77370 1.000 53.58034  ? 122 LEU   A CD1 1 
ATOM   834  C  CD2 . LEU   A 1 115 ? 13.27931  36.68436 41.92156 1.000 42.36669  ? 122 LEU   A CD2 1 
ATOM   835  N  N   . GLN   A 1 116 ? 17.92699  39.59392 42.96364 1.000 64.44493  ? 123 GLN   A N   1 
ATOM   836  C  CA  . GLN   A 1 116 ? 19.01507  39.75429 43.91546 1.000 61.44956  ? 123 GLN   A CA  1 
ATOM   837  C  C   . GLN   A 1 116 ? 18.97004  41.08111 44.65873 1.000 67.87754  ? 123 GLN   A C   1 
ATOM   838  O  O   . GLN   A 1 116 ? 19.74451  41.26841 45.60342 1.000 69.84355  ? 123 GLN   A O   1 
ATOM   839  C  CB  . GLN   A 1 116 ? 20.36498  39.62492 43.20767 1.000 80.12216  ? 123 GLN   A CB  1 
ATOM   840  C  CG  . GLN   A 1 116 ? 20.60780  38.27481 42.57441 1.000 70.19285  ? 123 GLN   A CG  1 
ATOM   841  C  CD  . GLN   A 1 116 ? 21.88856  38.25636 41.77053 1.000 101.67097 ? 123 GLN   A CD  1 
ATOM   842  O  OE1 . GLN   A 1 116 ? 22.05557  39.03041 40.82576 1.000 98.04335  ? 123 GLN   A OE1 1 
ATOM   843  N  NE2 . GLN   A 1 116 ? 22.81551  37.38730 42.15794 1.000 101.26409 ? 123 GLN   A NE2 1 
ATOM   844  N  N   . ALA   A 1 117 ? 18.10481  42.00424 44.24773 1.000 67.80347  ? 124 ALA   A N   1 
ATOM   845  C  CA  . ALA   A 1 117 ? 17.89827  43.26127 44.95082 1.000 68.56733  ? 124 ALA   A CA  1 
ATOM   846  C  C   . ALA   A 1 117 ? 16.74182  43.19226 45.94241 1.000 76.82309  ? 124 ALA   A C   1 
ATOM   847  O  O   . ALA   A 1 117 ? 16.32827  44.23055 46.46912 1.000 92.17929  ? 124 ALA   A O   1 
ATOM   848  C  CB  . ALA   A 1 117 ? 17.65976  44.39279 43.94735 1.000 75.52831  ? 124 ALA   A CB  1 
ATOM   849  N  N   . GLY   A 1 118 ? 16.21042  41.99820 46.20375 1.000 62.95033  ? 125 GLY   A N   1 
ATOM   850  C  CA  . GLY   A 1 118 ? 15.13758  41.80144 47.15305 1.000 67.44640  ? 125 GLY   A CA  1 
ATOM   851  C  C   . GLY   A 1 118 ? 13.84084  41.31041 46.54390 1.000 66.99386  ? 125 GLY   A C   1 
ATOM   852  O  O   . GLY   A 1 118 ? 12.98983  40.78616 47.27578 1.000 68.87200  ? 125 GLY   A O   1 
ATOM   853  N  N   . ALA   A 1 119 ? 13.66078  41.46489 45.23387 1.000 61.74577  ? 126 ALA   A N   1 
ATOM   854  C  CA  . ALA   A 1 119 ? 12.41071  41.06984 44.60033 1.000 67.27628  ? 126 ALA   A CA  1 
ATOM   855  C  C   . ALA   A 1 119 ? 12.19153  39.56387 44.73256 1.000 60.52343  ? 126 ALA   A C   1 
ATOM   856  O  O   . ALA   A 1 119 ? 13.12985  38.78693 44.92140 1.000 59.80158  ? 126 ALA   A O   1 
ATOM   857  C  CB  . ALA   A 1 119 ? 12.40433  41.48137 43.12711 1.000 54.95079  ? 126 ALA   A CB  1 
ATOM   858  N  N   . ASP   A 1 120 ? 10.92796  39.15369 44.65057 1.000 55.22614  ? 127 ASP   A N   1 
ATOM   859  C  CA  . ASP   A 1 120 ? 10.57769  37.74215 44.68909 1.000 55.60737  ? 127 ASP   A CA  1 
ATOM   860  C  C   . ASP   A 1 120 ? 9.91523   37.33288 43.37583 1.000 54.82428  ? 127 ASP   A C   1 
ATOM   861  O  O   . ASP   A 1 120 ? 9.58860   38.16492 42.52399 1.000 46.96550  ? 127 ASP   A O   1 
ATOM   862  C  CB  . ASP   A 1 120 ? 9.67193   37.41900 45.88651 1.000 54.46010  ? 127 ASP   A CB  1 
ATOM   863  C  CG  . ASP   A 1 120 ? 8.21740   37.75735 45.63200 1.000 67.29604  ? 127 ASP   A CG  1 
ATOM   864  O  OD1 . ASP   A 1 120 ? 7.91318   38.93368 45.33666 1.000 70.88170  ? 127 ASP   A OD1 1 
ATOM   865  O  OD2 . ASP   A 1 120 ? 7.37459   36.83777 45.72450 1.000 68.34632  ? 127 ASP   A OD2 1 
ATOM   866  N  N   . ILE   A 1 121 ? 9.72218   36.01807 43.23383 1.000 50.15521  ? 128 ILE   A N   1 
ATOM   867  C  CA  . ILE   A 1 121 ? 9.34399   35.41807 41.95697 1.000 46.76269  ? 128 ILE   A CA  1 
ATOM   868  C  C   . ILE   A 1 121 ? 7.98038   35.91745 41.49309 1.000 49.29540  ? 128 ILE   A C   1 
ATOM   869  O  O   . ILE   A 1 121 ? 7.71833   36.01210 40.28586 1.000 43.41615  ? 128 ILE   A O   1 
ATOM   870  C  CB  . ILE   A 1 121 ? 9.39469   33.87967 42.09289 1.000 49.02118  ? 128 ILE   A CB  1 
ATOM   871  C  CG1 . ILE   A 1 121 ? 10.80974  33.37034 41.80632 1.000 62.62562  ? 128 ILE   A CG1 1 
ATOM   872  C  CG2 . ILE   A 1 121 ? 8.41019   33.19777 41.16124 1.000 44.32900  ? 128 ILE   A CG2 1 
ATOM   873  C  CD1 . ILE   A 1 121 ? 11.06743  31.96252 42.30572 1.000 63.01740  ? 128 ILE   A CD1 1 
ATOM   874  N  N   . SER   A 1 122 ? 7.10939   36.28786 42.43403 1.000 48.79534  ? 129 SER   A N   1 
ATOM   875  C  CA  . SER   A 1 122 ? 5.75076   36.69621 42.09346 1.000 46.34075  ? 129 SER   A CA  1 
ATOM   876  C  C   . SER   A 1 122 ? 5.69757   37.95864 41.23789 1.000 41.92460  ? 129 SER   A C   1 
ATOM   877  O  O   . SER   A 1 122 ? 4.65573   38.23118 40.63481 1.000 43.92805  ? 129 SER   A O   1 
ATOM   878  C  CB  . SER   A 1 122 ? 4.93991   36.91046 43.36990 1.000 43.48202  ? 129 SER   A CB  1 
ATOM   879  O  OG  . SER   A 1 122 ? 5.27370   38.15085 43.96826 1.000 50.94626  ? 129 SER   A OG  1 
ATOM   880  N  N   . MET   A 1 123 ? 6.77820   38.73668 41.17260 1.000 48.88237  ? 130 MET   A N   1 
ATOM   881  C  CA  . MET   A 1 123 ? 6.81493   39.95357 40.36824 1.000 45.76320  ? 130 MET   A CA  1 
ATOM   882  C  C   . MET   A 1 123 ? 7.18558   39.70253 38.91215 1.000 40.97162  ? 130 MET   A C   1 
ATOM   883  O  O   . MET   A 1 123 ? 7.45746   40.66573 38.18483 1.000 42.59855  ? 130 MET   A O   1 
ATOM   884  C  CB  . MET   A 1 123 ? 7.80199   40.96613 40.95866 1.000 39.65445  ? 130 MET   A CB  1 
ATOM   885  C  CG  . MET   A 1 123 ? 7.14513   42.08020 41.75498 1.000 49.36958  ? 130 MET   A CG  1 
ATOM   886  S  SD  . MET   A 1 123 ? 8.25962   42.92022 42.89798 1.000 75.16388  ? 130 MET   A SD  1 
ATOM   887  C  CE  . MET   A 1 123 ? 8.89598   41.54945 43.85118 1.000 61.49813  ? 130 MET   A CE  1 
ATOM   888  N  N   . ILE   A 1 124 ? 7.19247   38.44128 38.47348 1.000 34.72609  ? 131 ILE   A N   1 
ATOM   889  C  CA  . ILE   A 1 124 ? 7.76450   38.08872 37.17643 1.000 40.86691  ? 131 ILE   A CA  1 
ATOM   890  C  C   . ILE   A 1 124 ? 7.02047   38.76963 36.03261 1.000 44.27383  ? 131 ILE   A C   1 
ATOM   891  O  O   . ILE   A 1 124 ? 7.62839   39.12629 35.01652 1.000 37.30719  ? 131 ILE   A O   1 
ATOM   892  C  CB  . ILE   A 1 124 ? 7.78538   36.55164 37.02118 1.000 40.97831  ? 131 ILE   A CB  1 
ATOM   893  C  CG1 . ILE   A 1 124 ? 8.59632   36.12998 35.79566 1.000 42.76301  ? 131 ILE   A CG1 1 
ATOM   894  C  CG2 . ILE   A 1 124 ? 6.36699   35.98431 36.95557 1.000 38.91952  ? 131 ILE   A CG2 1 
ATOM   895  C  CD1 . ILE   A 1 124 ? 8.64073   34.61984 35.59055 1.000 36.75884  ? 131 ILE   A CD1 1 
ATOM   896  N  N   . GLY   A 1 125 ? 5.70770   38.97467 36.17565 1.000 43.31729  ? 132 GLY   A N   1 
ATOM   897  C  CA  . GLY   A 1 125 ? 4.92997   39.61627 35.12793 1.000 40.83446  ? 132 GLY   A CA  1 
ATOM   898  C  C   . GLY   A 1 125 ? 5.32694   41.05252 34.83785 1.000 48.30861  ? 132 GLY   A C   1 
ATOM   899  O  O   . GLY   A 1 125 ? 5.09969   41.53120 33.72240 1.000 36.94318  ? 132 GLY   A O   1 
ATOM   900  N  N   . GLN   A 1 126 ? 5.91390   41.75220 35.81168 1.000 35.07904  ? 133 GLN   A N   1 
ATOM   901  C  CA  . GLN   A 1 126 ? 6.36368   43.11673 35.57017 1.000 44.00614  ? 133 GLN   A CA  1 
ATOM   902  C  C   . GLN   A 1 126 ? 7.52264   43.19234 34.58992 1.000 47.74921  ? 133 GLN   A C   1 
ATOM   903  O  O   . GLN   A 1 126 ? 7.90935   44.30039 34.20156 1.000 44.91251  ? 133 GLN   A O   1 
ATOM   904  C  CB  . GLN   A 1 126 ? 6.77680   43.76934 36.88231 1.000 48.86963  ? 133 GLN   A CB  1 
ATOM   905  C  CG  . GLN   A 1 126 ? 5.73590   43.66410 37.95902 1.000 46.62266  ? 133 GLN   A CG  1 
ATOM   906  C  CD  . GLN   A 1 126 ? 5.97444   44.64974 39.06412 1.000 54.09351  ? 133 GLN   A CD  1 
ATOM   907  O  OE1 . GLN   A 1 126 ? 6.63825   45.67243 38.87035 1.000 57.47461  ? 133 GLN   A OE1 1 
ATOM   908  N  NE2 . GLN   A 1 126 ? 5.44682   44.34782 40.24261 1.000 56.50053  ? 133 GLN   A NE2 1 
ATOM   909  N  N   . PHE   A 1 127 ? 8.08717   42.05258 34.19173 1.000 42.19816  ? 134 PHE   A N   1 
ATOM   910  C  CA  . PHE   A 1 127 ? 9.19591   42.00964 33.24838 1.000 41.10812  ? 134 PHE   A CA  1 
ATOM   911  C  C   . PHE   A 1 127 ? 8.81067   41.32320 31.94718 1.000 36.59480  ? 134 PHE   A C   1 
ATOM   912  O  O   . PHE   A 1 127 ? 9.69052   41.02639 31.12796 1.000 40.19684  ? 134 PHE   A O   1 
ATOM   913  C  CB  . PHE   A 1 127 ? 10.40624  41.31710 33.88587 1.000 37.72549  ? 134 PHE   A CB  1 
ATOM   914  C  CG  . PHE   A 1 127 ? 10.83700  41.93681 35.18605 1.000 36.00211  ? 134 PHE   A CG  1 
ATOM   915  C  CD1 . PHE   A 1 127 ? 10.24165  41.56595 36.38388 1.000 35.10634  ? 134 PHE   A CD1 1 
ATOM   916  C  CD2 . PHE   A 1 127 ? 11.82873  42.90299 35.20786 1.000 36.97265  ? 134 PHE   A CD2 1 
ATOM   917  C  CE1 . PHE   A 1 127 ? 10.63275  42.14990 37.57950 1.000 37.73821  ? 134 PHE   A CE1 1 
ATOM   918  C  CE2 . PHE   A 1 127 ? 12.22449  43.48820 36.39883 1.000 44.31416  ? 134 PHE   A CE2 1 
ATOM   919  C  CZ  . PHE   A 1 127 ? 11.62520  43.11198 37.58563 1.000 40.01443  ? 134 PHE   A CZ  1 
ATOM   920  N  N   . GLY   A 1 128 ? 7.52187   41.06205 31.73818 1.000 37.10491  ? 135 GLY   A N   1 
ATOM   921  C  CA  . GLY   A 1 128 ? 7.05001   40.48049 30.49629 1.000 37.02869  ? 135 GLY   A CA  1 
ATOM   922  C  C   . GLY   A 1 128 ? 7.42496   39.03545 30.26437 1.000 44.01699  ? 135 GLY   A C   1 
ATOM   923  O  O   . GLY   A 1 128 ? 7.29074   38.55389 29.13571 1.000 42.14076  ? 135 GLY   A O   1 
ATOM   924  N  N   . VAL   A 1 129 ? 7.88336   38.31918 31.29053 1.000 39.90237  ? 136 VAL   A N   1 
ATOM   925  C  CA  . VAL   A 1 129 ? 8.31636   36.94011 31.09911 1.000 38.70969  ? 136 VAL   A CA  1 
ATOM   926  C  C   . VAL   A 1 129 ? 7.50378   36.00808 31.99035 1.000 35.66566  ? 136 VAL   A C   1 
ATOM   927  O  O   . VAL   A 1 129 ? 7.97764   34.93719 32.38681 1.000 36.78172  ? 136 VAL   A O   1 
ATOM   928  C  CB  . VAL   A 1 129 ? 9.82646   36.79479 31.36195 1.000 41.08130  ? 136 VAL   A CB  1 
ATOM   929  C  CG1 . VAL   A 1 129 ? 10.61488  37.50116 30.26781 1.000 38.80570  ? 136 VAL   A CG1 1 
ATOM   930  C  CG2 . VAL   A 1 129 ? 10.18649  37.34792 32.72963 1.000 34.05689  ? 136 VAL   A CG2 1 
ATOM   931  N  N   . GLY   A 1 130 ? 6.26390   36.39906 32.28906 1.000 34.28531  ? 137 GLY   A N   1 
ATOM   932  C  CA  . GLY   A 1 130 ? 5.40854   35.59653 33.14321 1.000 36.34347  ? 137 GLY   A CA  1 
ATOM   933  C  C   . GLY   A 1 130 ? 5.12892   34.19871 32.62647 1.000 37.19045  ? 137 GLY   A C   1 
ATOM   934  O  O   . GLY   A 1 130 ? 4.83211   33.30480 33.42847 1.000 31.13931  ? 137 GLY   A O   1 
ATOM   935  N  N   . PHE   A 1 131 ? 5.22783   33.98450 31.30846 1.000 30.78786  ? 138 PHE   A N   1 
ATOM   936  C  CA  . PHE   A 1 131 ? 4.89857   32.67997 30.73329 1.000 31.81059  ? 138 PHE   A CA  1 
ATOM   937  C  C   . PHE   A 1 131 ? 5.71328   31.55774 31.36957 1.000 33.43531  ? 138 PHE   A C   1 
ATOM   938  O  O   . PHE   A 1 131 ? 5.20252   30.44917 31.56892 1.000 29.02994  ? 138 PHE   A O   1 
ATOM   939  C  CB  . PHE   A 1 131 ? 5.12058   32.69533 29.21859 1.000 26.73057  ? 138 PHE   A CB  1 
ATOM   940  C  CG  . PHE   A 1 131 ? 5.24979   31.31866 28.60506 1.000 31.71549  ? 138 PHE   A CG  1 
ATOM   941  C  CD1 . PHE   A 1 131 ? 4.13148   30.51777 28.41604 1.000 33.24754  ? 138 PHE   A CD1 1 
ATOM   942  C  CD2 . PHE   A 1 131 ? 6.49380   30.82461 28.22370 1.000 36.40996  ? 138 PHE   A CD2 1 
ATOM   943  C  CE1 . PHE   A 1 131 ? 4.24892   29.25456 27.85319 1.000 35.17503  ? 138 PHE   A CE1 1 
ATOM   944  C  CE2 . PHE   A 1 131 ? 6.62167   29.56509 27.66300 1.000 30.69094  ? 138 PHE   A CE2 1 
ATOM   945  C  CZ  . PHE   A 1 131 ? 5.49744   28.77693 27.47481 1.000 33.68554  ? 138 PHE   A CZ  1 
ATOM   946  N  N   . TYR   A 1 132 ? 6.98411   31.82055 31.68876 1.000 31.48268  ? 139 TYR   A N   1 
ATOM   947  C  CA  . TYR   A 1 132 ? 7.85737   30.77229 32.20593 1.000 26.72007  ? 139 TYR   A CA  1 
ATOM   948  C  C   . TYR   A 1 132 ? 7.53177   30.37721 33.64331 1.000 28.92251  ? 139 TYR   A C   1 
ATOM   949  O  O   . TYR   A 1 132 ? 8.04546   29.35722 34.11379 1.000 33.91813  ? 139 TYR   A O   1 
ATOM   950  C  CB  . TYR   A 1 132 ? 9.32058   31.20789 32.08592 1.000 32.83150  ? 139 TYR   A CB  1 
ATOM   951  C  CG  . TYR   A 1 132 ? 9.70900   31.56534 30.66883 1.000 31.11834  ? 139 TYR   A CG  1 
ATOM   952  C  CD1 . TYR   A 1 132 ? 10.07573  30.58282 29.75784 1.000 33.80017  ? 139 TYR   A CD1 1 
ATOM   953  C  CD2 . TYR   A 1 132 ? 9.67615   32.88396 30.23246 1.000 34.91966  ? 139 TYR   A CD2 1 
ATOM   954  C  CE1 . TYR   A 1 132 ? 10.41875  30.90778 28.45207 1.000 32.74386  ? 139 TYR   A CE1 1 
ATOM   955  C  CE2 . TYR   A 1 132 ? 10.01388  33.21825 28.93415 1.000 38.21726  ? 139 TYR   A CE2 1 
ATOM   956  C  CZ  . TYR   A 1 132 ? 10.38485  32.22909 28.04685 1.000 36.91222  ? 139 TYR   A CZ  1 
ATOM   957  O  OH  . TYR   A 1 132 ? 10.72373  32.57196 26.75551 1.000 48.14983  ? 139 TYR   A OH  1 
ATOM   958  N  N   . SER   A 1 133 ? 6.68332   31.13379 34.34621 1.000 30.51682  ? 140 SER   A N   1 
ATOM   959  C  CA  . SER   A 1 133 ? 6.20107   30.67911 35.64627 1.000 26.44163  ? 140 SER   A CA  1 
ATOM   960  C  C   . SER   A 1 133 ? 5.39174   29.39280 35.54255 1.000 33.28264  ? 140 SER   A C   1 
ATOM   961  O  O   . SER   A 1 133 ? 5.10790   28.77341 36.57522 1.000 31.01758  ? 140 SER   A O   1 
ATOM   962  C  CB  . SER   A 1 133 ? 5.35965   31.77009 36.31514 1.000 32.44052  ? 140 SER   A CB  1 
ATOM   963  O  OG  . SER   A 1 133 ? 4.13386   31.98346 35.62828 1.000 31.18959  ? 140 SER   A OG  1 
ATOM   964  N  N   . ALA   A 1 134 ? 5.01394   28.98642 34.32542 1.000 28.68298  ? 141 ALA   A N   1 
ATOM   965  C  CA  . ALA   A 1 134 ? 4.36478   27.69668 34.12114 1.000 30.25278  ? 141 ALA   A CA  1 
ATOM   966  C  C   . ALA   A 1 134 ? 5.21571   26.54930 34.64984 1.000 29.73122  ? 141 ALA   A C   1 
ATOM   967  O  O   . ALA   A 1 134 ? 4.67693   25.53867 35.11284 1.000 33.12420  ? 141 ALA   A O   1 
ATOM   968  C  CB  . ALA   A 1 134 ? 4.07076   27.49624 32.63384 1.000 27.02450  ? 141 ALA   A CB  1 
ATOM   969  N  N   . TYR   A 1 135 ? 6.53919   26.68832 34.60285 1.000 26.43778  ? 142 TYR   A N   1 
ATOM   970  C  CA  . TYR   A 1 135 ? 7.43986   25.65952 35.09989 1.000 29.36892  ? 142 TYR   A CA  1 
ATOM   971  C  C   . TYR   A 1 135 ? 7.52416   25.63352 36.61760 1.000 31.77247  ? 142 TYR   A C   1 
ATOM   972  O  O   . TYR   A 1 135 ? 8.32378   24.86969 37.16646 1.000 34.15982  ? 142 TYR   A O   1 
ATOM   973  C  CB  . TYR   A 1 135 ? 8.82235   25.83914 34.47188 1.000 26.75748  ? 142 TYR   A CB  1 
ATOM   974  C  CG  . TYR   A 1 135 ? 8.78353   25.50970 32.99782 1.000 37.75533  ? 142 TYR   A CG  1 
ATOM   975  C  CD1 . TYR   A 1 135 ? 8.97161   24.20371 32.55649 1.000 31.12309  ? 142 TYR   A CD1 1 
ATOM   976  C  CD2 . TYR   A 1 135 ? 8.49215   26.48949 32.05296 1.000 32.05593  ? 142 TYR   A CD2 1 
ATOM   977  C  CE1 . TYR   A 1 135 ? 8.91166   23.88750 31.22155 1.000 33.01131  ? 142 TYR   A CE1 1 
ATOM   978  C  CE2 . TYR   A 1 135 ? 8.42861   26.18310 30.70496 1.000 36.53264  ? 142 TYR   A CE2 1 
ATOM   979  C  CZ  . TYR   A 1 135 ? 8.63819   24.87782 30.29652 1.000 40.38024  ? 142 TYR   A CZ  1 
ATOM   980  O  OH  . TYR   A 1 135 ? 8.57220   24.55585 28.95917 1.000 40.98860  ? 142 TYR   A OH  1 
ATOM   981  N  N   . LEU   A 1 136 ? 6.71512   26.44521 37.30385 1.000 29.42431  ? 143 LEU   A N   1 
ATOM   982  C  CA  . LEU   A 1 136 ? 6.54861   26.26705 38.74042 1.000 37.71356  ? 143 LEU   A CA  1 
ATOM   983  C  C   . LEU   A 1 136 ? 5.74655   25.01185 39.04679 1.000 33.49347  ? 143 LEU   A C   1 
ATOM   984  O  O   . LEU   A 1 136 ? 6.00250   24.34200 40.05343 1.000 33.65403  ? 143 LEU   A O   1 
ATOM   985  C  CB  . LEU   A 1 136 ? 5.85543   27.48398 39.35734 1.000 41.49067  ? 143 LEU   A CB  1 
ATOM   986  C  CG  . LEU   A 1 136 ? 6.62931   28.79652 39.48652 1.000 37.26206  ? 143 LEU   A CG  1 
ATOM   987  C  CD1 . LEU   A 1 136 ? 5.66945   29.92031 39.83114 1.000 36.26021  ? 143 LEU   A CD1 1 
ATOM   988  C  CD2 . LEU   A 1 136 ? 7.72670   28.67848 40.53489 1.000 31.40447  ? 143 LEU   A CD2 1 
ATOM   989  N  N   . VAL   A 1 137 ? 4.78221   24.68024 38.19287 1.000 30.70286  ? 144 VAL   A N   1 
ATOM   990  C  CA  . VAL   A 1 137 ? 3.89296   23.54755 38.42498 1.000 36.27898  ? 144 VAL   A CA  1 
ATOM   991  C  C   . VAL   A 1 137 ? 3.97634   22.48652 37.33643 1.000 37.22734  ? 144 VAL   A C   1 
ATOM   992  O  O   . VAL   A 1 137 ? 3.43899   21.38576 37.52944 1.000 42.12761  ? 144 VAL   A O   1 
ATOM   993  C  CB  . VAL   A 1 137 ? 2.43062   24.01369 38.59083 1.000 29.97614  ? 144 VAL   A CB  1 
ATOM   994  C  CG1 . VAL   A 1 137 ? 2.28114   24.86127 39.85158 1.000 31.82242  ? 144 VAL   A CG1 1 
ATOM   995  C  CG2 . VAL   A 1 137 ? 1.98712   24.78887 37.36501 1.000 26.22832  ? 144 VAL   A CG2 1 
ATOM   996  N  N   . ALA   A 1 138 ? 4.62883   22.75814 36.21060 1.000 34.62097  ? 145 ALA   A N   1 
ATOM   997  C  CA  . ALA   A 1 138 ? 4.63447   21.85215 35.07250 1.000 31.70331  ? 145 ALA   A CA  1 
ATOM   998  C  C   . ALA   A 1 138 ? 6.03115   21.29759 34.82826 1.000 34.90270  ? 145 ALA   A C   1 
ATOM   999  O  O   . ALA   A 1 138 ? 7.02353   22.02985 34.88561 1.000 43.61440  ? 145 ALA   A O   1 
ATOM   1000 C  CB  . ALA   A 1 138 ? 4.13020   22.56055 33.80643 1.000 30.22782  ? 145 ALA   A CB  1 
ATOM   1001 N  N   . GLU   A 1 139 ? 6.10387   19.99726 34.55571 1.000 40.16261  ? 146 GLU   A N   1 
ATOM   1002 C  CA  . GLU   A 1 139 ? 7.33911   19.40005 34.07245 1.000 40.67554  ? 146 GLU   A CA  1 
ATOM   1003 C  C   . GLU   A 1 139 ? 7.47957   19.49706 32.55970 1.000 43.22452  ? 146 GLU   A C   1 
ATOM   1004 O  O   . GLU   A 1 139 ? 8.59668   19.37341 32.04344 1.000 44.38636  ? 146 GLU   A O   1 
ATOM   1005 C  CB  . GLU   A 1 139 ? 7.42951   17.93152 34.50119 1.000 47.68896  ? 146 GLU   A CB  1 
ATOM   1006 C  CG  . GLU   A 1 139 ? 6.26116   17.07452 34.04956 1.000 52.73802  ? 146 GLU   A CG  1 
ATOM   1007 C  CD  . GLU   A 1 139 ? 6.19040   15.74552 34.78375 1.000 71.34844  ? 146 GLU   A CD  1 
ATOM   1008 O  OE1 . GLU   A 1 139 ? 6.56072   15.69028 35.97859 1.000 75.34101  ? 146 GLU   A OE1 1 
ATOM   1009 O  OE2 . GLU   A 1 139 ? 5.76358   14.75023 34.15910 1.000 87.55890  ? 146 GLU   A OE2 1 
ATOM   1010 N  N   . LYS   A 1 140 ? 6.37790   19.71908 31.84525 1.000 38.22751  ? 147 LYS   A N   1 
ATOM   1011 C  CA  . LYS   A 1 140 ? 6.39845   19.87065 30.40001 1.000 32.96221  ? 147 LYS   A CA  1 
ATOM   1012 C  C   . LYS   A 1 140 ? 5.26835   20.79952 29.99648 1.000 34.51071  ? 147 LYS   A C   1 
ATOM   1013 O  O   . LYS   A 1 140 ? 4.16068   20.70716 30.53356 1.000 34.39385  ? 147 LYS   A O   1 
ATOM   1014 C  CB  . LYS   A 1 140 ? 6.25145   18.52543 29.68053 1.000 38.22506  ? 147 LYS   A CB  1 
ATOM   1015 C  CG  . LYS   A 1 140 ? 6.26983   18.65139 28.16323 1.000 42.93359  ? 147 LYS   A CG  1 
ATOM   1016 C  CD  . LYS   A 1 140 ? 6.45149   17.30433 27.48711 1.000 43.68927  ? 147 LYS   A CD  1 
ATOM   1017 C  CE  . LYS   A 1 140 ? 5.11642   16.62099 27.25419 1.000 48.02867  ? 147 LYS   A CE  1 
ATOM   1018 N  NZ  . LYS   A 1 140 ? 5.28783   15.22916 26.73764 1.000 54.81071  ? 147 LYS   A NZ  1 
ATOM   1019 N  N   . VAL   A 1 141 ? 5.55451   21.69100 29.05196 1.000 27.19194  ? 148 VAL   A N   1 
ATOM   1020 C  CA  . VAL   A 1 141 ? 4.58577   22.65739 28.55362 1.000 24.36805  ? 148 VAL   A CA  1 
ATOM   1021 C  C   . VAL   A 1 141 ? 4.46055   22.47647 27.04829 1.000 32.97149  ? 148 VAL   A C   1 
ATOM   1022 O  O   . VAL   A 1 141 ? 5.47068   22.44723 26.33736 1.000 37.05313  ? 148 VAL   A O   1 
ATOM   1023 C  CB  . VAL   A 1 141 ? 4.99644   24.10041 28.89859 1.000 32.56357  ? 148 VAL   A CB  1 
ATOM   1024 C  CG1 . VAL   A 1 141 ? 3.99161   25.09522 28.32138 1.000 26.95763  ? 148 VAL   A CG1 1 
ATOM   1025 C  CG2 . VAL   A 1 141 ? 5.13698   24.26458 30.40683 1.000 26.49011  ? 148 VAL   A CG2 1 
ATOM   1026 N  N   . THR   A 1 142 ? 3.22622   22.34407 26.56900 1.000 32.74912  ? 149 THR   A N   1 
ATOM   1027 C  CA  . THR   A 1 142 ? 2.92363   22.26039 25.14620 1.000 32.84325  ? 149 THR   A CA  1 
ATOM   1028 C  C   . THR   A 1 142 ? 2.06922   23.45821 24.76723 1.000 29.84469  ? 149 THR   A C   1 
ATOM   1029 O  O   . THR   A 1 142 ? 1.10725   23.78117 25.47107 1.000 37.27663  ? 149 THR   A O   1 
ATOM   1030 C  CB  . THR   A 1 142 ? 2.18883   20.95988 24.80685 1.000 35.07071  ? 149 THR   A CB  1 
ATOM   1031 O  OG1 . THR   A 1 142 ? 2.89351   19.85341 25.37517 1.000 43.21228  ? 149 THR   A OG1 1 
ATOM   1032 C  CG2 . THR   A 1 142 ? 2.08837   20.76797 23.29686 1.000 38.25289  ? 149 THR   A CG2 1 
ATOM   1033 N  N   . VAL   A 1 143 ? 2.42981   24.12852 23.67721 1.000 33.97952  ? 150 VAL   A N   1 
ATOM   1034 C  CA  . VAL   A 1 143 ? 1.68957   25.28758 23.18859 1.000 27.81294  ? 150 VAL   A CA  1 
ATOM   1035 C  C   . VAL   A 1 143 ? 1.23520   24.99730 21.76370 1.000 38.60940  ? 150 VAL   A C   1 
ATOM   1036 O  O   . VAL   A 1 143 ? 2.06469   24.81064 20.86357 1.000 38.44818  ? 150 VAL   A O   1 
ATOM   1037 C  CB  . VAL   A 1 143 ? 2.52642   26.57418 23.24730 1.000 29.20898  ? 150 VAL   A CB  1 
ATOM   1038 C  CG1 . VAL   A 1 143 ? 1.69162   27.76841 22.79452 1.000 24.75315  ? 150 VAL   A CG1 1 
ATOM   1039 C  CG2 . VAL   A 1 143 ? 3.05533   26.79026 24.65116 1.000 28.59640  ? 150 VAL   A CG2 1 
ATOM   1040 N  N   . ILE   A 1 144 ? -0.07666  24.93210 21.56560 1.000 39.70258  ? 151 ILE   A N   1 
ATOM   1041 C  CA  . ILE   A 1 144 ? -0.68045  24.84009 20.24056 1.000 35.93967  ? 151 ILE   A CA  1 
ATOM   1042 C  C   . ILE   A 1 144 ? -1.21507  26.22143 19.89667 1.000 32.46734  ? 151 ILE   A C   1 
ATOM   1043 O  O   . ILE   A 1 144 ? -1.98582  26.80010 20.67018 1.000 34.17636  ? 151 ILE   A O   1 
ATOM   1044 C  CB  . ILE   A 1 144 ? -1.80095  23.78440 20.20122 1.000 43.07110  ? 151 ILE   A CB  1 
ATOM   1045 C  CG1 . ILE   A 1 144 ? -1.37774  22.51428 20.94092 1.000 37.40099  ? 151 ILE   A CG1 1 
ATOM   1046 C  CG2 . ILE   A 1 144 ? -2.19694  23.46549 18.76654 1.000 34.41995  ? 151 ILE   A CG2 1 
ATOM   1047 C  CD1 . ILE   A 1 144 ? -0.14591  21.87032 20.38279 1.000 39.22757  ? 151 ILE   A CD1 1 
ATOM   1048 N  N   . THR   A 1 145 ? -0.79686  26.76319 18.75504 1.000 29.26027  ? 152 THR   A N   1 
ATOM   1049 C  CA  . THR   A 1 145 ? -1.11453  28.14442 18.43656 1.000 28.98100  ? 152 THR   A CA  1 
ATOM   1050 C  C   . THR   A 1 145 ? -1.41313  28.29684 16.95168 1.000 31.66122  ? 152 THR   A C   1 
ATOM   1051 O  O   . THR   A 1 145 ? -0.84644  27.59922 16.10457 1.000 30.52600  ? 152 THR   A O   1 
ATOM   1052 C  CB  . THR   A 1 145 ? 0.02687   29.08971 18.86588 1.000 31.92755  ? 152 THR   A CB  1 
ATOM   1053 O  OG1 . THR   A 1 145 ? -0.41766  30.45055 18.79924 1.000 31.00641  ? 152 THR   A OG1 1 
ATOM   1054 C  CG2 . THR   A 1 145 ? 1.25454   28.91214 17.98442 1.000 30.69365  ? 152 THR   A CG2 1 
ATOM   1055 N  N   . LYS   A 1 146 ? -2.32427  29.22342 16.65089 1.000 31.20765  ? 153 LYS   A N   1 
ATOM   1056 C  CA  . LYS   A 1 146 ? -2.73515  29.51055 15.28153 1.000 31.49809  ? 153 LYS   A CA  1 
ATOM   1057 C  C   . LYS   A 1 146 ? -2.89143  31.01515 15.11550 1.000 33.97520  ? 153 LYS   A C   1 
ATOM   1058 O  O   . LYS   A 1 146 ? -3.70586  31.64019 15.80203 1.000 30.81253  ? 153 LYS   A O   1 
ATOM   1059 C  CB  . LYS   A 1 146 ? -4.04446  28.79359 14.92900 1.000 32.28339  ? 153 LYS   A CB  1 
ATOM   1060 C  CG  . LYS   A 1 146 ? -4.57756  29.12344 13.54505 1.000 30.56175  ? 153 LYS   A CG  1 
ATOM   1061 C  CD  . LYS   A 1 146 ? -3.64736  28.60001 12.46510 1.000 32.18083  ? 153 LYS   A CD  1 
ATOM   1062 C  CE  . LYS   A 1 146 ? -4.33000  28.57841 11.11080 1.000 34.79337  ? 153 LYS   A CE  1 
ATOM   1063 N  NZ  . LYS   A 1 146 ? -4.44975  29.94884 10.53972 1.000 41.52037  ? 153 LYS   A NZ  1 
ATOM   1064 N  N   . HIS   A 1 147 ? -2.10792  31.58490 14.20920 1.000 27.68678  ? 154 HIS   A N   1 
ATOM   1065 C  CA  . HIS   A 1 147 ? -2.17300  32.98738 13.84159 1.000 29.48450  ? 154 HIS   A CA  1 
ATOM   1066 C  C   . HIS   A 1 147 ? -2.80005  33.10745 12.45701 1.000 32.80222  ? 154 HIS   A C   1 
ATOM   1067 O  O   . HIS   A 1 147 ? -2.63087  32.22601 11.61104 1.000 32.91564  ? 154 HIS   A O   1 
ATOM   1068 C  CB  . HIS   A 1 147 ? -0.76919  33.60109 13.85775 1.000 32.57071  ? 154 HIS   A CB  1 
ATOM   1069 C  CG  . HIS   A 1 147 ? -0.74574  35.08392 13.67295 1.000 33.34539  ? 154 HIS   A CG  1 
ATOM   1070 N  ND1 . HIS   A 1 147 ? -0.92626  35.68338 12.44520 1.000 37.08343  ? 154 HIS   A ND1 1 
ATOM   1071 C  CD2 . HIS   A 1 147 ? -0.53225  36.08836 14.55591 1.000 34.13704  ? 154 HIS   A CD2 1 
ATOM   1072 C  CE1 . HIS   A 1 147 ? -0.84023  36.99485 12.58172 1.000 33.08321  ? 154 HIS   A CE1 1 
ATOM   1073 N  NE2 . HIS   A 1 147 ? -0.60017  37.26667 13.85221 1.000 37.75924  ? 154 HIS   A NE2 1 
ATOM   1074 N  N   . ASN   A 1 148 ? -3.52847  34.20708 12.22793 1.000 29.28487  ? 155 ASN   A N   1 
ATOM   1075 C  CA  . ASN   A 1 148 ? -4.24105  34.38512 10.96366 1.000 34.24052  ? 155 ASN   A CA  1 
ATOM   1076 C  C   . ASN   A 1 148 ? -3.31506  34.32869 9.75075  1.000 35.17204  ? 155 ASN   A C   1 
ATOM   1077 O  O   . ASN   A 1 148 ? -3.77549  34.03419 8.64442  1.000 41.23052  ? 155 ASN   A O   1 
ATOM   1078 C  CB  . ASN   A 1 148 ? -4.99129  35.72183 10.96166 1.000 35.99825  ? 155 ASN   A CB  1 
ATOM   1079 C  CG  . ASN   A 1 148 ? -6.38196  35.62043 11.56502 1.000 34.69521  ? 155 ASN   A CG  1 
ATOM   1080 O  OD1 . ASN   A 1 148 ? -6.93132  34.53218 11.71281 1.000 41.37051  ? 155 ASN   A OD1 1 
ATOM   1081 N  ND2 . ASN   A 1 148 ? -6.95612  36.76124 11.91387 1.000 32.56878  ? 155 ASN   A ND2 1 
ATOM   1082 N  N   . ASP   A 1 149 ? -2.02461  34.59308 9.93379  1.000 37.15934  ? 156 ASP   A N   1 
ATOM   1083 C  CA  . ASP   A 1 149 ? -1.08223  34.72432 8.83411  1.000 42.93311  ? 156 ASP   A CA  1 
ATOM   1084 C  C   . ASP   A 1 149 ? -0.15039  33.52405 8.69213  1.000 40.50308  ? 156 ASP   A C   1 
ATOM   1085 O  O   . ASP   A 1 149 ? 0.83745   33.61048 7.95685  1.000 44.21541  ? 156 ASP   A O   1 
ATOM   1086 C  CB  . ASP   A 1 149 ? -0.25877  36.00617 9.00872  1.000 40.77845  ? 156 ASP   A CB  1 
ATOM   1087 C  CG  . ASP   A 1 149 ? -1.11619  37.26855 8.98274  1.000 50.18963  ? 156 ASP   A CG  1 
ATOM   1088 O  OD1 . ASP   A 1 149 ? -2.25007  37.22110 8.45579  1.000 52.05639  ? 156 ASP   A OD1 1 
ATOM   1089 O  OD2 . ASP   A 1 149 ? -0.64680  38.31702 9.47567  1.000 52.15402  ? 156 ASP   A OD2 1 
ATOM   1090 N  N   . ASP   A 1 150 ? -0.43523  32.40807 9.36103  1.000 36.29413  ? 157 ASP   A N   1 
ATOM   1091 C  CA  . ASP   A 1 150 ? 0.49180   31.28440 9.38348  1.000 36.07000  ? 157 ASP   A CA  1 
ATOM   1092 C  C   . ASP   A 1 150 ? -0.28211  29.99448 9.62757  1.000 35.89273  ? 157 ASP   A C   1 
ATOM   1093 O  O   . ASP   A 1 150 ? -1.49146  30.00298 9.87312  1.000 37.89212  ? 157 ASP   A O   1 
ATOM   1094 C  CB  . ASP   A 1 150 ? 1.57297   31.48865 10.45241 1.000 37.17413  ? 157 ASP   A CB  1 
ATOM   1095 C  CG  . ASP   A 1 150 ? 2.91631   30.90528 10.04861 1.000 45.96666  ? 157 ASP   A CG  1 
ATOM   1096 O  OD1 . ASP   A 1 150 ? 2.96622   30.14793 9.05179  1.000 49.85159  ? 157 ASP   A OD1 1 
ATOM   1097 O  OD2 . ASP   A 1 150 ? 3.92144   31.19834 10.73557 1.000 44.99182  ? 157 ASP   A OD2 1 
ATOM   1098 N  N   . GLU   A 1 151 ? 0.43256   28.87629 9.55307  1.000 39.25266  ? 158 GLU   A N   1 
ATOM   1099 C  CA  . GLU   A 1 151 ? -0.15249  27.57718 9.82364  1.000 36.79615  ? 158 GLU   A CA  1 
ATOM   1100 C  C   . GLU   A 1 151 ? -0.22562  27.33707 11.32726 1.000 35.17554  ? 158 GLU   A C   1 
ATOM   1101 O  O   . GLU   A 1 151 ? 0.31843   28.09554 12.13284 1.000 37.78044  ? 158 GLU   A O   1 
ATOM   1102 C  CB  . GLU   A 1 151 ? 0.66187   26.47382 9.15277  1.000 40.89219  ? 158 GLU   A CB  1 
ATOM   1103 C  CG  . GLU   A 1 151 ? 0.62345   26.49904 7.62287  1.000 54.48387  ? 158 GLU   A CG  1 
ATOM   1104 C  CD  . GLU   A 1 151 ? 1.40671   25.34684 7.00377  1.000 82.88736  ? 158 GLU   A CD  1 
ATOM   1105 O  OE1 . GLU   A 1 151 ? 0.78114   24.46805 6.37233  1.000 91.74091  ? 158 GLU   A OE1 1 
ATOM   1106 O  OE2 . GLU   A 1 151 ? 2.64740   25.31032 7.15805  1.000 82.90885  ? 158 GLU   A OE2 1 
ATOM   1107 N  N   . GLN   A 1 152 ? -0.90472  26.25589 11.70159 1.000 35.45017  ? 159 GLN   A N   1 
ATOM   1108 C  CA  . GLN   A 1 152 ? -0.99803  25.85250 13.09817 1.000 36.94634  ? 159 GLN   A CA  1 
ATOM   1109 C  C   . GLN   A 1 152 ? 0.29437   25.16792 13.53100 1.000 37.86178  ? 159 GLN   A C   1 
ATOM   1110 O  O   . GLN   A 1 152 ? 0.78249   24.26567 12.84320 1.000 38.23682  ? 159 GLN   A O   1 
ATOM   1111 C  CB  . GLN   A 1 152 ? -2.18835  24.91465 13.29064 1.000 35.42604  ? 159 GLN   A CB  1 
ATOM   1112 C  CG  . GLN   A 1 152 ? -2.55478  24.66422 14.73682 1.000 37.52833  ? 159 GLN   A CG  1 
ATOM   1113 C  CD  . GLN   A 1 152 ? -3.95787  24.12425 14.88721 1.000 41.34878  ? 159 GLN   A CD  1 
ATOM   1114 O  OE1 . GLN   A 1 152 ? -4.91012  24.68176 14.34466 1.000 58.30883  ? 159 GLN   A OE1 1 
ATOM   1115 N  NE2 . GLN   A 1 152 ? -4.09311  23.02220 15.61478 1.000 46.21311  ? 159 GLN   A NE2 1 
ATOM   1116 N  N   . TYR   A 1 153 ? 0.84195   25.58457 14.67638 1.000 34.09668  ? 160 TYR   A N   1 
ATOM   1117 C  CA  . TYR   A 1 153 ? 2.14131   25.10529 15.13269 1.000 31.81904  ? 160 TYR   A CA  1 
ATOM   1118 C  C   . TYR   A 1 153 ? 2.05890   24.57619 16.55734 1.000 35.63609  ? 160 TYR   A C   1 
ATOM   1119 O  O   . TYR   A 1 153 ? 1.19317   24.96313 17.34763 1.000 34.49228  ? 160 TYR   A O   1 
ATOM   1120 C  CB  . TYR   A 1 153 ? 3.20920   26.20522 15.05579 1.000 30.78904  ? 160 TYR   A CB  1 
ATOM   1121 C  CG  . TYR   A 1 153 ? 3.69640   26.45849 13.64828 1.000 38.86299  ? 160 TYR   A CG  1 
ATOM   1122 C  CD1 . TYR   A 1 153 ? 4.60711   25.60470 13.04682 1.000 35.12415  ? 160 TYR   A CD1 1 
ATOM   1123 C  CD2 . TYR   A 1 153 ? 3.23705   27.54754 12.91725 1.000 42.39588  ? 160 TYR   A CD2 1 
ATOM   1124 C  CE1 . TYR   A 1 153 ? 5.04952   25.82549 11.75866 1.000 43.26143  ? 160 TYR   A CE1 1 
ATOM   1125 C  CE2 . TYR   A 1 153 ? 3.67684   27.77718 11.62458 1.000 39.92772  ? 160 TYR   A CE2 1 
ATOM   1126 C  CZ  . TYR   A 1 153 ? 4.58221   26.91283 11.05359 1.000 40.88298  ? 160 TYR   A CZ  1 
ATOM   1127 O  OH  . TYR   A 1 153 ? 5.02338   27.13002 9.76759  1.000 64.72511  ? 160 TYR   A OH  1 
ATOM   1128 N  N   . ALA   A 1 154 ? 2.98741   23.67849 16.87479 1.000 40.43774  ? 161 ALA   A N   1 
ATOM   1129 C  CA  . ALA   A 1 154 ? 3.09608   23.07998 18.19810 1.000 35.80568  ? 161 ALA   A CA  1 
ATOM   1130 C  C   . ALA   A 1 154 ? 4.48977   23.35348 18.74055 1.000 33.64507  ? 161 ALA   A C   1 
ATOM   1131 O  O   . ALA   A 1 154 ? 5.48598   22.89175 18.17188 1.000 43.15279  ? 161 ALA   A O   1 
ATOM   1132 C  CB  . ALA   A 1 154 ? 2.81483   21.57465 18.15653 1.000 35.16036  ? 161 ALA   A CB  1 
ATOM   1133 N  N   . TRP   A 1 155 ? 4.54819   24.10885 19.82789 1.000 29.93139  ? 162 TRP   A N   1 
ATOM   1134 C  CA  . TRP   A 1 155 ? 5.76059   24.38347 20.58077 1.000 30.59249  ? 162 TRP   A CA  1 
ATOM   1135 C  C   . TRP   A 1 155 ? 5.73732   23.54952 21.85582 1.000 41.59804  ? 162 TRP   A C   1 
ATOM   1136 O  O   . TRP   A 1 155 ? 4.67813   23.37535 22.47018 1.000 37.59929  ? 162 TRP   A O   1 
ATOM   1137 C  CB  . TRP   A 1 155 ? 5.83766   25.87840 20.90708 1.000 28.12554  ? 162 TRP   A CB  1 
ATOM   1138 C  CG  . TRP   A 1 155 ? 7.02876   26.35413 21.68278 1.000 28.93346  ? 162 TRP   A CG  1 
ATOM   1139 C  CD1 . TRP   A 1 155 ? 8.11659   27.00083 21.18388 1.000 34.79669  ? 162 TRP   A CD1 1 
ATOM   1140 C  CD2 . TRP   A 1 155 ? 7.22751   26.27230 23.10312 1.000 30.36737  ? 162 TRP   A CD2 1 
ATOM   1141 N  NE1 . TRP   A 1 155 ? 8.98690   27.31675 22.19664 1.000 34.07243  ? 162 TRP   A NE1 1 
ATOM   1142 C  CE2 . TRP   A 1 155 ? 8.46624   26.87705 23.38507 1.000 32.75111  ? 162 TRP   A CE2 1 
ATOM   1143 C  CE3 . TRP   A 1 155 ? 6.48127   25.74034 24.16070 1.000 36.23014  ? 162 TRP   A CE3 1 
ATOM   1144 C  CZ2 . TRP   A 1 155 ? 8.98169   26.96064 24.67987 1.000 32.59200  ? 162 TRP   A CZ2 1 
ATOM   1145 C  CZ3 . TRP   A 1 155 ? 6.99489   25.82344 25.44713 1.000 33.17057  ? 162 TRP   A CZ3 1 
ATOM   1146 C  CH2 . TRP   A 1 155 ? 8.23197   26.43191 25.69389 1.000 33.25505  ? 162 TRP   A CH2 1 
ATOM   1147 N  N   . GLU   A 1 156 ? 6.90257   23.03617 22.25345 1.000 32.27181  ? 163 GLU   A N   1 
ATOM   1148 C  CA  . GLU   A 1 156 ? 6.99318   22.15444 23.40759 1.000 31.55561  ? 163 GLU   A CA  1 
ATOM   1149 C  C   . GLU   A 1 156 ? 8.37725   22.24547 24.03887 1.000 39.75642  ? 163 GLU   A C   1 
ATOM   1150 O  O   . GLU   A 1 156 ? 9.38430   22.37552 23.33591 1.000 32.28324  ? 163 GLU   A O   1 
ATOM   1151 C  CB  . GLU   A 1 156 ? 6.70314   20.70317 23.01439 1.000 36.35012  ? 163 GLU   A CB  1 
ATOM   1152 C  CG  . GLU   A 1 156 ? 6.40550   19.79482 24.19581 1.000 42.75948  ? 163 GLU   A CG  1 
ATOM   1153 C  CD  . GLU   A 1 156 ? 5.86557   18.43944 23.76700 1.000 58.11156  ? 163 GLU   A CD  1 
ATOM   1154 O  OE1 . GLU   A 1 156 ? 4.85796   18.40174 23.02702 1.000 63.43699  ? 163 GLU   A OE1 1 
ATOM   1155 O  OE2 . GLU   A 1 156 ? 6.44789   17.40965 24.17236 1.000 63.77668  ? 163 GLU   A OE2 1 
ATOM   1156 N  N   . SER   A 1 157 ? 8.42066   22.14618 25.36744 1.000 36.99345  ? 164 SER   A N   1 
ATOM   1157 C  CA  . SER   A 1 157 ? 9.68685   22.15171 26.08556 1.000 34.36883  ? 164 SER   A CA  1 
ATOM   1158 C  C   . SER   A 1 157 ? 9.49547   21.54710 27.46825 1.000 35.35410  ? 164 SER   A C   1 
ATOM   1159 O  O   . SER   A 1 157 ? 8.52046   21.86273 28.15739 1.000 35.04860  ? 164 SER   A O   1 
ATOM   1160 C  CB  . SER   A 1 157 ? 10.24703  23.57041 26.21374 1.000 31.15390  ? 164 SER   A CB  1 
ATOM   1161 O  OG  . SER   A 1 157 ? 11.39465  23.57594 27.04004 1.000 36.34980  ? 164 SER   A OG  1 
ATOM   1162 N  N   . SER   A 1 158 ? 10.43934  20.68855 27.86779 1.000 34.91732  ? 165 SER   A N   1 
ATOM   1163 C  CA  . SER   A 1 158 ? 10.55088  20.20030 29.24044 1.000 36.95306  ? 165 SER   A CA  1 
ATOM   1164 C  C   . SER   A 1 158 ? 11.73044  20.84235 29.96987 1.000 34.00355  ? 165 SER   A C   1 
ATOM   1165 O  O   . SER   A 1 158 ? 12.31999  20.23141 30.86334 1.000 42.68888  ? 165 SER   A O   1 
ATOM   1166 C  CB  . SER   A 1 158 ? 10.68699  18.67699 29.27330 1.000 33.80246  ? 165 SER   A CB  1 
ATOM   1167 O  OG  . SER   A 1 158 ? 9.64900   18.04303 28.54914 1.000 46.96266  ? 165 SER   A OG  1 
ATOM   1168 N  N   . ALA   A 1 159 ? 12.07243  22.07255 29.60219 1.000 35.29253  ? 166 ALA   A N   1 
ATOM   1169 C  CA  . ALA   A 1 159 ? 13.26757  22.77658 30.08994 1.000 46.61971  ? 166 ALA   A CA  1 
ATOM   1170 C  C   . ALA   A 1 159 ? 14.49762  21.97148 29.65606 1.000 45.93412  ? 166 ALA   A C   1 
ATOM   1171 O  O   . ALA   A 1 159 ? 14.49786  21.34865 28.58586 1.000 45.38218  ? 166 ALA   A O   1 
ATOM   1172 C  CB  . ALA   A 1 159 ? 13.16358  23.04001 31.58215 1.000 33.12999  ? 166 ALA   A CB  1 
ATOM   1173 N  N   . GLY   A 1 160 ? 15.55975  21.97296 30.45802 1.000 42.39198  ? 167 GLY   A N   1 
ATOM   1174 C  CA  . GLY   A 1 160 ? 16.78015  21.32645 30.01509 1.000 33.46963  ? 167 GLY   A CA  1 
ATOM   1175 C  C   . GLY   A 1 160 ? 17.53807  22.06310 28.93322 1.000 38.63711  ? 167 GLY   A C   1 
ATOM   1176 O  O   . GLY   A 1 160 ? 18.52590  21.53261 28.41456 1.000 45.70385  ? 167 GLY   A O   1 
ATOM   1177 N  N   . GLY   A 1 161 ? 17.10222  23.26544 28.56554 1.000 40.35807  ? 168 GLY   A N   1 
ATOM   1178 C  CA  . GLY   A 1 161 ? 17.82519  24.09795 27.62893 1.000 42.33325  ? 168 GLY   A CA  1 
ATOM   1179 C  C   . GLY   A 1 161 ? 17.38191  24.01757 26.18340 1.000 40.72627  ? 168 GLY   A C   1 
ATOM   1180 O  O   . GLY   A 1 161 ? 17.96836  24.70822 25.34290 1.000 39.54199  ? 168 GLY   A O   1 
ATOM   1181 N  N   . SER   A 1 162 ? 16.37523  23.20850 25.85767 1.000 35.19163  ? 169 SER   A N   1 
ATOM   1182 C  CA  . SER   A 1 162 ? 15.94415  23.08266 24.47282 1.000 43.70908  ? 169 SER   A CA  1 
ATOM   1183 C  C   . SER   A 1 162 ? 14.42303  23.09221 24.39630 1.000 37.13771  ? 169 SER   A C   1 
ATOM   1184 O  O   . SER   A 1 162 ? 13.72862  22.85607 25.38707 1.000 39.86774  ? 169 SER   A O   1 
ATOM   1185 C  CB  . SER   A 1 162 ? 16.51401  21.81290 23.81499 1.000 37.51853  ? 169 SER   A CB  1 
ATOM   1186 O  OG  . SER   A 1 162 ? 15.97445  20.64139 24.39613 1.000 43.51836  ? 169 SER   A OG  1 
ATOM   1187 N  N   . PHE   A 1 163 ? 13.91606  23.40195 23.20123 1.000 33.51218  ? 170 PHE   A N   1 
ATOM   1188 C  CA  . PHE   A 1 163 ? 12.49491  23.32022 22.88879 1.000 33.62082  ? 170 PHE   A CA  1 
ATOM   1189 C  C   . PHE   A 1 163 ? 12.34028  22.87314 21.43982 1.000 33.07061  ? 170 PHE   A C   1 
ATOM   1190 O  O   . PHE   A 1 163 ? 13.27859  22.95850 20.64267 1.000 35.56452  ? 170 PHE   A O   1 
ATOM   1191 C  CB  . PHE   A 1 163 ? 11.76794  24.65745 23.12841 1.000 28.97465  ? 170 PHE   A CB  1 
ATOM   1192 C  CG  . PHE   A 1 163 ? 12.24863  25.78719 22.25209 1.000 34.06080  ? 170 PHE   A CG  1 
ATOM   1193 C  CD1 . PHE   A 1 163 ? 13.32232  26.57450 22.64071 1.000 28.57260  ? 170 PHE   A CD1 1 
ATOM   1194 C  CD2 . PHE   A 1 163 ? 11.62479  26.06364 21.04098 1.000 30.70338  ? 170 PHE   A CD2 1 
ATOM   1195 C  CE1 . PHE   A 1 163 ? 13.77079  27.61568 21.83433 1.000 31.79837  ? 170 PHE   A CE1 1 
ATOM   1196 C  CE2 . PHE   A 1 163 ? 12.06276  27.10145 20.23264 1.000 30.63290  ? 170 PHE   A CE2 1 
ATOM   1197 C  CZ  . PHE   A 1 163 ? 13.13878  27.88173 20.62891 1.000 28.65054  ? 170 PHE   A CZ  1 
ATOM   1198 N  N   . THR   A 1 164 ? 11.14390  22.38517 21.10399 1.000 34.98322  ? 171 THR   A N   1 
ATOM   1199 C  CA  . THR   A 1 164 ? 10.84239  21.89030 19.76624 1.000 32.93546  ? 171 THR   A CA  1 
ATOM   1200 C  C   . THR   A 1 164 ? 9.67377   22.64698 19.14830 1.000 37.40626  ? 171 THR   A C   1 
ATOM   1201 O  O   . THR   A 1 164 ? 8.75634   23.09235 19.84500 1.000 37.51601  ? 171 THR   A O   1 
ATOM   1202 C  CB  . THR   A 1 164 ? 10.49333  20.40119 19.76898 1.000 35.99497  ? 171 THR   A CB  1 
ATOM   1203 O  OG1 . THR   A 1 164 ? 9.38668   20.17456 20.65118 1.000 44.13490  ? 171 THR   A OG1 1 
ATOM   1204 C  CG2 . THR   A 1 164 ? 11.68665  19.56046 20.19698 1.000 33.94715  ? 171 THR   A CG2 1 
ATOM   1205 N  N   . VAL   A 1 165 ? 9.70731   22.76962 17.82318 1.000 34.31842  ? 172 VAL   A N   1 
ATOM   1206 C  CA  . VAL   A 1 165 ? 8.62499   23.37170 17.05536 1.000 32.72326  ? 172 VAL   A CA  1 
ATOM   1207 C  C   . VAL   A 1 165 ? 8.31371   22.45336 15.88378 1.000 32.06967  ? 172 VAL   A C   1 
ATOM   1208 O  O   . VAL   A 1 165 ? 9.22682   21.97790 15.19889 1.000 37.76906  ? 172 VAL   A O   1 
ATOM   1209 C  CB  . VAL   A 1 165 ? 8.97803   24.78909 16.55875 1.000 36.06698  ? 172 VAL   A CB  1 
ATOM   1210 C  CG1 . VAL   A 1 165 ? 7.88291   25.32624 15.64400 1.000 29.46838  ? 172 VAL   A CG1 1 
ATOM   1211 C  CG2 . VAL   A 1 165 ? 9.19342   25.72874 17.73198 1.000 28.44959  ? 172 VAL   A CG2 1 
ATOM   1212 N  N   . ARG   A 1 166 ? 7.02929   22.18929 15.66936 1.000 39.61170  ? 173 ARG   A N   1 
ATOM   1213 C  CA  . ARG   A 1 166 ? 6.58123   21.38974 14.54115 1.000 38.19485  ? 173 ARG   A CA  1 
ATOM   1214 C  C   . ARG   A 1 166 ? 5.21022   21.88731 14.11392 1.000 36.50583  ? 173 ARG   A C   1 
ATOM   1215 O  O   . ARG   A 1 166 ? 4.47358   22.47512 14.91077 1.000 35.05440  ? 173 ARG   A O   1 
ATOM   1216 C  CB  . ARG   A 1 166 ? 6.51957   19.89925 14.89583 1.000 43.65880  ? 173 ARG   A CB  1 
ATOM   1217 C  CG  . ARG   A 1 166 ? 5.33227   19.51126 15.77263 1.000 46.61809  ? 173 ARG   A CG  1 
ATOM   1218 C  CD  . ARG   A 1 166 ? 5.51872   18.12669 16.36751 1.000 56.75456  ? 173 ARG   A CD  1 
ATOM   1219 N  NE  . ARG   A 1 166 ? 6.33580   18.17515 17.57602 1.000 67.60368  ? 173 ARG   A NE  1 
ATOM   1220 C  CZ  . ARG   A 1 166 ? 6.71543   17.11218 18.27383 1.000 70.77126  ? 173 ARG   A CZ  1 
ATOM   1221 N  NH1 . ARG   A 1 166 ? 6.38730   15.88455 17.89978 1.000 64.22631  ? 173 ARG   A NH1 1 
ATOM   1222 N  NH2 . ARG   A 1 166 ? 7.45651   17.28436 19.36555 1.000 57.04093  ? 173 ARG   A NH2 1 
ATOM   1223 N  N   . THR   A 1 167 ? 4.87972   21.66411 12.84598 1.000 44.32793  ? 174 THR   A N   1 
ATOM   1224 C  CA  . THR   A 1 167 ? 3.51096   21.87739 12.39811 1.000 43.84717  ? 174 THR   A CA  1 
ATOM   1225 C  C   . THR   A 1 167 ? 2.59083   20.89692 13.11400 1.000 42.51420  ? 174 THR   A C   1 
ATOM   1226 O  O   . THR   A 1 167 ? 2.89875   19.70557 13.22395 1.000 47.68581  ? 174 THR   A O   1 
ATOM   1227 C  CB  . THR   A 1 167 ? 3.40444   21.69682 10.88028 1.000 45.47110  ? 174 THR   A CB  1 
ATOM   1228 O  OG1 . THR   A 1 167 ? 3.96300   20.43174 10.51083 1.000 55.31381  ? 174 THR   A OG1 1 
ATOM   1229 C  CG2 . THR   A 1 167 ? 4.14279   22.80311 10.14354 1.000 39.69900  ? 174 THR   A CG2 1 
ATOM   1230 N  N   . ASP   A 1 168 ? 1.46862   21.40035 13.61965 1.000 41.97505  ? 175 ASP   A N   1 
ATOM   1231 C  CA  . ASP   A 1 168 ? 0.53617   20.56767 14.36453 1.000 49.11879  ? 175 ASP   A CA  1 
ATOM   1232 C  C   . ASP   A 1 168 ? -0.47721  19.93799 13.41863 1.000 65.22184  ? 175 ASP   A C   1 
ATOM   1233 O  O   . ASP   A 1 168 ? -1.15750  20.64012 12.66181 1.000 55.10954  ? 175 ASP   A O   1 
ATOM   1234 C  CB  . ASP   A 1 168 ? -0.18622  21.36776 15.44627 1.000 42.69177  ? 175 ASP   A CB  1 
ATOM   1235 C  CG  . ASP   A 1 168 ? -1.04377  20.48513 16.33899 1.000 62.71330  ? 175 ASP   A CG  1 
ATOM   1236 O  OD1 . ASP   A 1 168 ? -0.54410  19.43068 16.79150 1.000 64.97162  ? 175 ASP   A OD1 1 
ATOM   1237 O  OD2 . ASP   A 1 168 ? -2.22061  20.83338 16.57490 1.000 64.04410  ? 175 ASP   A OD2 1 
ATOM   1238 N  N   . THR   A 1 169 ? -0.58369  18.61362 13.48195 1.000 68.85019  ? 176 THR   A N   1 
ATOM   1239 C  CA  . THR   A 1 169 ? -1.49221  17.84885 12.64168 1.000 79.21892  ? 176 THR   A CA  1 
ATOM   1240 C  C   . THR   A 1 169 ? -2.81807  17.52737 13.32491 1.000 80.98381  ? 176 THR   A C   1 
ATOM   1241 O  O   . THR   A 1 169 ? -3.68606  16.90580 12.70077 1.000 76.29699  ? 176 THR   A O   1 
ATOM   1242 C  CB  . THR   A 1 169 ? -0.80691  16.55313 12.19154 1.000 86.07464  ? 176 THR   A CB  1 
ATOM   1243 O  OG1 . THR   A 1 169 ? -0.23091  15.89787 13.33044 1.000 73.83296  ? 176 THR   A OG1 1 
ATOM   1244 C  CG2 . THR   A 1 169 ? 0.28213   16.85469 11.17160 1.000 72.54177  ? 176 THR   A CG2 1 
ATOM   1245 N  N   . GLY   A 1 170 ? -3.00235  17.94610 14.57775 1.000 75.49129  ? 177 GLY   A N   1 
ATOM   1246 C  CA  . GLY   A 1 170 ? -4.19420  17.61860 15.33766 1.000 67.36238  ? 177 GLY   A CA  1 
ATOM   1247 C  C   . GLY   A 1 170 ? -5.41691  18.41904 14.94043 1.000 75.05422  ? 177 GLY   A C   1 
ATOM   1248 O  O   . GLY   A 1 170 ? -5.59779  18.80359 13.77778 1.000 74.83017  ? 177 GLY   A O   1 
ATOM   1249 N  N   . GLU   A 1 171 ? -6.27185  18.67033 15.92331 1.000 74.63786  ? 178 GLU   A N   1 
ATOM   1250 C  CA  . GLU   A 1 171 ? -7.52850  19.36575 15.67110 1.000 70.63606  ? 178 GLU   A CA  1 
ATOM   1251 C  C   . GLU   A 1 171 ? -7.26974  20.84393 15.38211 1.000 69.16366  ? 178 GLU   A C   1 
ATOM   1252 O  O   . GLU   A 1 171 ? -6.57820  21.51011 16.16011 1.000 52.89421  ? 178 GLU   A O   1 
ATOM   1253 C  CB  . GLU   A 1 171 ? -8.45762  19.21129 16.87568 1.000 80.31538  ? 178 GLU   A CB  1 
ATOM   1254 C  CG  . GLU   A 1 171 ? -9.81882  19.86879 16.70963 1.000 82.11584  ? 178 GLU   A CG  1 
ATOM   1255 C  CD  . GLU   A 1 171 ? -10.63910 19.24652 15.59745 1.000 92.83393  ? 178 GLU   A CD  1 
ATOM   1256 O  OE1 . GLU   A 1 171 ? -10.49372 18.02729 15.35672 1.000 97.06507  ? 178 GLU   A OE1 1 
ATOM   1257 O  OE2 . GLU   A 1 171 ? -11.42668 19.98084 14.96047 1.000 93.23175  ? 178 GLU   A OE2 1 
ATOM   1258 N  N   . PRO   A 1 172 ? -7.80588  21.38698 14.28821 1.000 67.99243  ? 179 PRO   A N   1 
ATOM   1259 C  CA  . PRO   A 1 172 ? -7.60281  22.81541 14.00487 1.000 55.13886  ? 179 PRO   A CA  1 
ATOM   1260 C  C   . PRO   A 1 172 ? -8.35765  23.68655 14.99860 1.000 55.21471  ? 179 PRO   A C   1 
ATOM   1261 O  O   . PRO   A 1 172 ? -9.50174  23.39938 15.35992 1.000 58.98261  ? 179 PRO   A O   1 
ATOM   1262 C  CB  . PRO   A 1 172 ? -8.16089  22.97823 12.58310 1.000 56.76029  ? 179 PRO   A CB  1 
ATOM   1263 C  CG  . PRO   A 1 172 ? -8.32207  21.57719 12.04893 1.000 56.58720  ? 179 PRO   A CG  1 
ATOM   1264 C  CD  . PRO   A 1 172 ? -8.58941  20.72154 13.23777 1.000 52.75541  ? 179 PRO   A CD  1 
ATOM   1265 N  N   . MET   A 1 173 ? -7.70669  24.76440 15.44281 1.000 51.84125  ? 180 MET   A N   1 
ATOM   1266 C  CA  . MET   A 1 173 ? -8.31849  25.66748 16.41056 1.000 52.02386  ? 180 MET   A CA  1 
ATOM   1267 C  C   . MET   A 1 173 ? -8.90540  26.92716 15.78801 1.000 51.63458  ? 180 MET   A C   1 
ATOM   1268 O  O   . MET   A 1 173 ? -9.55088  27.70243 16.50159 1.000 61.10776  ? 180 MET   A O   1 
ATOM   1269 C  CB  . MET   A 1 173 ? -7.31113  26.09618 17.47783 1.000 54.00943  ? 180 MET   A CB  1 
ATOM   1270 C  CG  . MET   A 1 173 ? -6.29092  25.06686 17.85588 1.000 55.99724  ? 180 MET   A CG  1 
ATOM   1271 S  SD  . MET   A 1 173 ? -4.78918  25.95876 18.26730 1.000 64.32333  ? 180 MET   A SD  1 
ATOM   1272 C  CE  . MET   A 1 173 ? -5.37050  26.90109 19.67488 1.000 37.49238  ? 180 MET   A CE  1 
ATOM   1273 N  N   . GLY   A 1 174 ? -8.69064  27.16402 14.49811 1.000 41.08917  ? 181 GLY   A N   1 
ATOM   1274 C  CA  . GLY   A 1 174 ? -9.20007  28.37533 13.88332 1.000 49.02268  ? 181 GLY   A CA  1 
ATOM   1275 C  C   . GLY   A 1 174 ? -8.31857  29.58509 14.11880 1.000 47.13590  ? 181 GLY   A C   1 
ATOM   1276 O  O   . GLY   A 1 174 ? -7.77390  30.15535 13.16821 1.000 44.37806  ? 181 GLY   A O   1 
ATOM   1277 N  N   . ARG   A 1 175 ? -8.17488  29.98234 15.38434 1.000 36.79341  ? 182 ARG   A N   1 
ATOM   1278 C  CA  . ARG   A 1 175 ? -7.29921  31.08255 15.77566 1.000 45.72575  ? 182 ARG   A CA  1 
ATOM   1279 C  C   . ARG   A 1 175 ? -7.13638  31.08923 17.28931 1.000 36.10834  ? 182 ARG   A C   1 
ATOM   1280 O  O   . ARG   A 1 175 ? -8.12212  30.97624 18.02198 1.000 39.93129  ? 182 ARG   A O   1 
ATOM   1281 C  CB  . ARG   A 1 175 ? -7.84500  32.43873 15.29480 1.000 34.92304  ? 182 ARG   A CB  1 
ATOM   1282 C  CG  . ARG   A 1 175 ? -6.85991  33.60033 15.46417 1.000 31.29571  ? 182 ARG   A CG  1 
ATOM   1283 C  CD  . ARG   A 1 175 ? -7.55344  34.96529 15.48771 1.000 32.65336  ? 182 ARG   A CD  1 
ATOM   1284 N  NE  . ARG   A 1 175 ? -8.44104  35.12345 16.63579 1.000 32.45876  ? 182 ARG   A NE  1 
ATOM   1285 C  CZ  . ARG   A 1 175 ? -9.76289  35.20609 16.56140 1.000 33.24473  ? 182 ARG   A CZ  1 
ATOM   1286 N  NH1 . ARG   A 1 175 ? -10.39689 35.12956 15.40312 1.000 35.33225  ? 182 ARG   A NH1 1 
ATOM   1287 N  NH2 . ARG   A 1 175 ? -10.46569 35.36643 17.67793 1.000 33.09945  ? 182 ARG   A NH2 1 
ATOM   1288 N  N   . GLY   A 1 176 ? -5.91104  31.20675 17.76993 1.000 32.19302  ? 183 GLY   A N   1 
ATOM   1289 C  CA  . GLY   A 1 176 ? -5.69018  31.38061 19.18613 1.000 32.42563  ? 183 GLY   A CA  1 
ATOM   1290 C  C   . GLY   A 1 176 ? -4.50609  30.57240 19.65998 1.000 35.22351  ? 183 GLY   A C   1 
ATOM   1291 O  O   . GLY   A 1 176 ? -3.64596  30.17091 18.87627 1.000 34.33213  ? 183 GLY   A O   1 
ATOM   1292 N  N   . THR   A 1 177 ? -4.47664  30.33918 20.96817 1.000 33.84643  ? 184 THR   A N   1 
ATOM   1293 C  CA  . THR   A 1 177 ? -3.34698  29.68713 21.61002 1.000 31.96794  ? 184 THR   A CA  1 
ATOM   1294 C  C   . THR   A 1 177 ? -3.87010  28.73825 22.67303 1.000 32.90239  ? 184 THR   A C   1 
ATOM   1295 O  O   . THR   A 1 177 ? -4.75891  29.09933 23.44853 1.000 36.89964  ? 184 THR   A O   1 
ATOM   1296 C  CB  . THR   A 1 177 ? -2.39079  30.71838 22.22509 1.000 31.65836  ? 184 THR   A CB  1 
ATOM   1297 O  OG1 . THR   A 1 177 ? -1.63662  31.34105 21.18091 1.000 36.04352  ? 184 THR   A OG1 1 
ATOM   1298 C  CG2 . THR   A 1 177 ? -1.43025  30.05923 23.21097 1.000 34.63042  ? 184 THR   A CG2 1 
ATOM   1299 N  N   . LYS   A 1 178 ? -3.32808  27.52602 22.68466 1.000 34.19939  ? 185 LYS   A N   1 
ATOM   1300 C  CA  . LYS   A 1 178 ? -3.64778  26.50355 23.66971 1.000 26.25316  ? 185 LYS   A CA  1 
ATOM   1301 C  C   . LYS   A 1 178 ? -2.37783  26.19644 24.44844 1.000 37.28124  ? 185 LYS   A C   1 
ATOM   1302 O  O   . LYS   A 1 178 ? -1.39145  25.73068 23.86561 1.000 30.77418  ? 185 LYS   A O   1 
ATOM   1303 C  CB  . LYS   A 1 178 ? -4.18027  25.24463 22.98219 1.000 34.32532  ? 185 LYS   A CB  1 
ATOM   1304 C  CG  . LYS   A 1 178 ? -5.25941  24.50740 23.74367 1.000 48.56142  ? 185 LYS   A CG  1 
ATOM   1305 C  CD  . LYS   A 1 178 ? -5.28984  23.01754 23.39696 1.000 48.64671  ? 185 LYS   A CD  1 
ATOM   1306 C  CE  . LYS   A 1 178 ? -5.19536  22.77536 21.89824 1.000 52.30589  ? 185 LYS   A CE  1 
ATOM   1307 N  NZ  . LYS   A 1 178 ? -6.46750  23.12638 21.19371 1.000 70.53934  ? 185 LYS   A NZ  1 
ATOM   1308 N  N   . VAL   A 1 179 ? -2.39139  26.46420 25.75265 1.000 27.35009  ? 186 VAL   A N   1 
ATOM   1309 C  CA  . VAL   A 1 179 ? -1.25995  26.15289 26.62043 1.000 29.19295  ? 186 VAL   A CA  1 
ATOM   1310 C  C   . VAL   A 1 179 ? -1.62351  24.93603 27.46353 1.000 31.17238  ? 186 VAL   A C   1 
ATOM   1311 O  O   . VAL   A 1 179 ? -2.56180  24.98168 28.27034 1.000 27.19142  ? 186 VAL   A O   1 
ATOM   1312 C  CB  . VAL   A 1 179 ? -0.87077  27.34735 27.50342 1.000 30.12637  ? 186 VAL   A CB  1 
ATOM   1313 C  CG1 . VAL   A 1 179 ? 0.19211   26.92970 28.51055 1.000 31.11213  ? 186 VAL   A CG1 1 
ATOM   1314 C  CG2 . VAL   A 1 179 ? -0.36779  28.50186 26.64695 1.000 26.88039  ? 186 VAL   A CG2 1 
ATOM   1315 N  N   . ILE   A 1 180 ? -0.88030  23.84802 27.27379 1.000 27.41657  ? 187 ILE   A N   1 
ATOM   1316 C  CA  . ILE   A 1 180 ? -1.12711  22.57816 27.94780 1.000 30.65823  ? 187 ILE   A CA  1 
ATOM   1317 C  C   . ILE   A 1 180 ? -0.01995  22.36298 28.97104 1.000 34.14743  ? 187 ILE   A C   1 
ATOM   1318 O  O   . ILE   A 1 180 ? 1.15164   22.21418 28.60453 1.000 32.33840  ? 187 ILE   A O   1 
ATOM   1319 C  CB  . ILE   A 1 180 ? -1.19176  21.41488 26.94710 1.000 30.61375  ? 187 ILE   A CB  1 
ATOM   1320 C  CG1 . ILE   A 1 180 ? -2.16597  21.74651 25.81293 1.000 29.74242  ? 187 ILE   A CG1 1 
ATOM   1321 C  CG2 . ILE   A 1 180 ? -1.58900  20.12161 27.64831 1.000 28.28929  ? 187 ILE   A CG2 1 
ATOM   1322 C  CD1 . ILE   A 1 180 ? -2.27231  20.66263 24.76833 1.000 34.24442  ? 187 ILE   A CD1 1 
ATOM   1323 N  N   . LEU   A 1 181 ? -0.38878  22.35045 30.25156 1.000 35.15656  ? 188 LEU   A N   1 
ATOM   1324 C  CA  . LEU   A 1 181 ? 0.55976   22.18173 31.34942 1.000 30.49864  ? 188 LEU   A CA  1 
ATOM   1325 C  C   . LEU   A 1 181 ? 0.49877   20.74057 31.84678 1.000 29.35818  ? 188 LEU   A C   1 
ATOM   1326 O  O   . LEU   A 1 181 ? -0.49725  20.32837 32.44698 1.000 33.64468  ? 188 LEU   A O   1 
ATOM   1327 C  CB  . LEU   A 1 181 ? 0.24670   23.15324 32.48305 1.000 26.07905  ? 188 LEU   A CB  1 
ATOM   1328 C  CG  . LEU   A 1 181 ? 0.07329   24.62827 32.11574 1.000 31.88890  ? 188 LEU   A CG  1 
ATOM   1329 C  CD1 . LEU   A 1 181 ? -0.55754  25.35452 33.27908 1.000 31.54986  ? 188 LEU   A CD1 1 
ATOM   1330 C  CD2 . LEU   A 1 181 ? 1.40277   25.26519 31.74867 1.000 26.12133  ? 188 LEU   A CD2 1 
ATOM   1331 N  N   . HIS   A 1 182 ? 1.56323   19.97941 31.60472 1.000 29.18812  ? 189 HIS   A N   1 
ATOM   1332 C  CA  . HIS   A 1 182 ? 1.70079   18.63268 32.15796 1.000 28.99643  ? 189 HIS   A CA  1 
ATOM   1333 C  C   . HIS   A 1 182 ? 2.27444   18.76539 33.56576 1.000 33.41132  ? 189 HIS   A C   1 
ATOM   1334 O  O   . HIS   A 1 182 ? 3.47688   18.96975 33.74384 1.000 39.96617  ? 189 HIS   A O   1 
ATOM   1335 C  CB  . HIS   A 1 182 ? 2.59067   17.77242 31.26768 1.000 29.02270  ? 189 HIS   A CB  1 
ATOM   1336 C  CG  . HIS   A 1 182 ? 2.14788   17.71765 29.83815 1.000 43.86119  ? 189 HIS   A CG  1 
ATOM   1337 N  ND1 . HIS   A 1 182 ? 1.29840   16.74243 29.35821 1.000 43.82625  ? 189 HIS   A ND1 1 
ATOM   1338 C  CD2 . HIS   A 1 182 ? 2.43139   18.52104 28.78416 1.000 40.73558  ? 189 HIS   A CD2 1 
ATOM   1339 C  CE1 . HIS   A 1 182 ? 1.08096   16.94598 28.07131 1.000 47.15389  ? 189 HIS   A CE1 1 
ATOM   1340 N  NE2 . HIS   A 1 182 ? 1.75600   18.01979 27.69807 1.000 42.62621  ? 189 HIS   A NE2 1 
ATOM   1341 N  N   . LEU   A 1 183 ? 1.41652   18.63491 34.57275 1.000 32.62608  ? 190 LEU   A N   1 
ATOM   1342 C  CA  . LEU   A 1 183 ? 1.76731   19.02199 35.93138 1.000 32.64811  ? 190 LEU   A CA  1 
ATOM   1343 C  C   . LEU   A 1 183 ? 2.70415   18.01826 36.59103 1.000 32.72068  ? 190 LEU   A C   1 
ATOM   1344 O  O   . LEU   A 1 183 ? 2.69371   16.82093 36.28597 1.000 45.05832  ? 190 LEU   A O   1 
ATOM   1345 C  CB  . LEU   A 1 183 ? 0.50792   19.16739 36.77980 1.000 31.86281  ? 190 LEU   A CB  1 
ATOM   1346 C  CG  . LEU   A 1 183 ? -0.46804  20.25531 36.33755 1.000 38.91413  ? 190 LEU   A CG  1 
ATOM   1347 C  CD1 . LEU   A 1 183 ? -1.68217  20.23495 37.24185 1.000 39.00947  ? 190 LEU   A CD1 1 
ATOM   1348 C  CD2 . LEU   A 1 183 ? 0.19498   21.64046 36.33012 1.000 34.19449  ? 190 LEU   A CD2 1 
ATOM   1349 N  N   . LYS   A 1 184 ? 3.51090   18.52347 37.52128 1.000 39.63605  ? 191 LYS   A N   1 
ATOM   1350 C  CA  . LYS   A 1 184 ? 4.29638   17.65646 38.38627 1.000 43.61109  ? 191 LYS   A CA  1 
ATOM   1351 C  C   . LYS   A 1 184 ? 3.37760   16.85323 39.30385 1.000 47.57350  ? 191 LYS   A C   1 
ATOM   1352 O  O   . LYS   A 1 184 ? 2.23896   17.24180 39.58932 1.000 44.43878  ? 191 LYS   A O   1 
ATOM   1353 C  CB  . LYS   A 1 184 ? 5.27969   18.47582 39.22082 1.000 44.39992  ? 191 LYS   A CB  1 
ATOM   1354 C  CG  . LYS   A 1 184 ? 6.26008   19.29340 38.39767 1.000 44.14138  ? 191 LYS   A CG  1 
ATOM   1355 C  CD  . LYS   A 1 184 ? 7.05363   20.25778 39.27120 1.000 45.31652  ? 191 LYS   A CD  1 
ATOM   1356 C  CE  . LYS   A 1 184 ? 7.60994   21.41116 38.45086 1.000 52.01249  ? 191 LYS   A CE  1 
ATOM   1357 N  NZ  . LYS   A 1 184 ? 8.37906   22.38080 39.28212 1.000 56.09718  ? 191 LYS   A NZ  1 
ATOM   1358 N  N   . GLU   A 1 185 ? 3.89774   15.71705 39.77523 1.000 48.79025  ? 192 GLU   A N   1 
ATOM   1359 C  CA  . GLU   A 1 185 ? 3.10475   14.81296 40.60264 1.000 51.32208  ? 192 GLU   A CA  1 
ATOM   1360 C  C   . GLU   A 1 185 ? 2.53519   15.51576 41.83308 1.000 52.93399  ? 192 GLU   A C   1 
ATOM   1361 O  O   . GLU   A 1 185 ? 1.41107   15.22401 42.25741 1.000 55.09465  ? 192 GLU   A O   1 
ATOM   1362 C  CB  . GLU   A 1 185 ? 3.95684   13.61371 41.01844 1.000 61.90443  ? 192 GLU   A CB  1 
ATOM   1363 C  CG  . GLU   A 1 185 ? 4.20272   12.60636 39.90222 1.000 88.80862  ? 192 GLU   A CG  1 
ATOM   1364 C  CD  . GLU   A 1 185 ? 5.53158   12.81542 39.18912 1.000 96.67631  ? 192 GLU   A CD  1 
ATOM   1365 O  OE1 . GLU   A 1 185 ? 6.23555   11.80865 38.94258 1.000 80.86566  ? 192 GLU   A OE1 1 
ATOM   1366 O  OE2 . GLU   A 1 185 ? 5.85954   13.98240 38.86391 1.000 82.42582  ? 192 GLU   A OE2 1 
ATOM   1367 N  N   . ASP   A 1 186 ? 3.28672   16.44382 42.41869 1.000 49.91524  ? 193 ASP   A N   1 
ATOM   1368 C  CA  . ASP   A 1 186 ? 2.88907   17.06361 43.67559 1.000 54.58763  ? 193 ASP   A CA  1 
ATOM   1369 C  C   . ASP   A 1 186 ? 2.09345   18.35060 43.48523 1.000 53.03290  ? 193 ASP   A C   1 
ATOM   1370 O  O   . ASP   A 1 186 ? 1.80033   19.03384 44.47286 1.000 48.28769  ? 193 ASP   A O   1 
ATOM   1371 C  CB  . ASP   A 1 186 ? 4.12519   17.32269 44.54834 1.000 60.36751  ? 193 ASP   A CB  1 
ATOM   1372 C  CG  . ASP   A 1 186 ? 5.06149   18.36453 43.95664 1.000 64.78294  ? 193 ASP   A CG  1 
ATOM   1373 O  OD1 . ASP   A 1 186 ? 5.01605   18.59868 42.73025 1.000 67.91565  ? 193 ASP   A OD1 1 
ATOM   1374 O  OD2 . ASP   A 1 186 ? 5.85717   18.94269 44.72581 1.000 81.23821  ? 193 ASP   A OD2 1 
ATOM   1375 N  N   . GLN   A 1 187 ? 1.72007   18.68721 42.25002 1.000 42.29609  ? 194 GLN   A N   1 
ATOM   1376 C  CA  . GLN   A 1 187 ? 0.99021   19.91837 41.96954 1.000 44.67070  ? 194 GLN   A CA  1 
ATOM   1377 C  C   . GLN   A 1 187 ? -0.40675  19.64080 41.41799 1.000 40.97770  ? 194 GLN   A C   1 
ATOM   1378 O  O   . GLN   A 1 187 ? -0.94535  20.44063 40.65255 1.000 45.70627  ? 194 GLN   A O   1 
ATOM   1379 C  CB  . GLN   A 1 187 ? 1.78118   20.80379 41.00609 1.000 39.78568  ? 194 GLN   A CB  1 
ATOM   1380 C  CG  . GLN   A 1 187 ? 3.19282   21.13236 41.47904 1.000 43.21929  ? 194 GLN   A CG  1 
ATOM   1381 C  CD  . GLN   A 1 187 ? 3.21212   21.93658 42.76403 1.000 44.97046  ? 194 GLN   A CD  1 
ATOM   1382 O  OE1 . GLN   A 1 187 ? 2.29990   22.71972 43.03463 1.000 49.83243  ? 194 GLN   A OE1 1 
ATOM   1383 N  NE2 . GLN   A 1 187 ? 4.25442   21.74813 43.56416 1.000 43.83557  ? 194 GLN   A NE2 1 
ATOM   1384 N  N   . THR   A 1 188 ? -1.01323  18.51694 41.80113 1.000 44.06510  ? 195 THR   A N   1 
ATOM   1385 C  CA  . THR   A 1 188 ? -2.33137  18.16537 41.28429 1.000 38.67206  ? 195 THR   A CA  1 
ATOM   1386 C  C   . THR   A 1 188 ? -3.45720  18.96035 41.93359 1.000 43.11878  ? 195 THR   A C   1 
ATOM   1387 O  O   . THR   A 1 188 ? -4.61189  18.81791 41.51778 1.000 46.36807  ? 195 THR   A O   1 
ATOM   1388 C  CB  . THR   A 1 188 ? -2.59308  16.66767 41.45756 1.000 42.79608  ? 195 THR   A CB  1 
ATOM   1389 O  OG1 . THR   A 1 188 ? -2.56136  16.32615 42.84855 1.000 47.13634  ? 195 THR   A OG1 1 
ATOM   1390 C  CG2 . THR   A 1 188 ? -1.53032  15.85971 40.71896 1.000 44.04362  ? 195 THR   A CG2 1 
ATOM   1391 N  N   . GLU   A 1 189 ? -3.15519  19.79603 42.92938 1.000 37.76745  ? 196 GLU   A N   1 
ATOM   1392 C  CA  . GLU   A 1 189 ? -4.18523  20.63367 43.52916 1.000 37.88189  ? 196 GLU   A CA  1 
ATOM   1393 C  C   . GLU   A 1 189 ? -4.75690  21.63495 42.53752 1.000 39.34962  ? 196 GLU   A C   1 
ATOM   1394 O  O   . GLU   A 1 189 ? -5.88248  22.10571 42.72811 1.000 40.60809  ? 196 GLU   A O   1 
ATOM   1395 C  CB  . GLU   A 1 189 ? -3.62010  21.37135 44.74001 1.000 47.22263  ? 196 GLU   A CB  1 
ATOM   1396 C  CG  . GLU   A 1 189 ? -2.83858  22.63268 44.38564 1.000 45.02091  ? 196 GLU   A CG  1 
ATOM   1397 C  CD  . GLU   A 1 189 ? -2.12711  23.22430 45.58404 1.000 56.45653  ? 196 GLU   A CD  1 
ATOM   1398 O  OE1 . GLU   A 1 189 ? -1.03668  22.71796 45.93092 1.000 60.14516  ? 196 GLU   A OE1 1 
ATOM   1399 O  OE2 . GLU   A 1 189 ? -2.66025  24.18505 46.18361 1.000 52.55869  ? 196 GLU   A OE2 1 
ATOM   1400 N  N   . TYR   A 1 190 ? -4.01147  21.97010 41.48743 1.000 38.63533  ? 197 TYR   A N   1 
ATOM   1401 C  CA  . TYR   A 1 190 ? -4.48014  22.88242 40.45501 1.000 37.30080  ? 197 TYR   A CA  1 
ATOM   1402 C  C   . TYR   A 1 190 ? -5.33635  22.19089 39.41112 1.000 41.44507  ? 197 TYR   A C   1 
ATOM   1403 O  O   . TYR   A 1 190 ? -5.66374  22.79815 38.38735 1.000 37.33387  ? 197 TYR   A O   1 
ATOM   1404 C  CB  . TYR   A 1 190 ? -3.28657  23.58389 39.80532 1.000 37.81425  ? 197 TYR   A CB  1 
ATOM   1405 C  CG  . TYR   A 1 190 ? -2.43327  24.26970 40.84108 1.000 39.47294  ? 197 TYR   A CG  1 
ATOM   1406 C  CD1 . TYR   A 1 190 ? -2.90134  25.38763 41.51317 1.000 38.87188  ? 197 TYR   A CD1 1 
ATOM   1407 C  CD2 . TYR   A 1 190 ? -1.18301  23.77351 41.18250 1.000 36.98620  ? 197 TYR   A CD2 1 
ATOM   1408 C  CE1 . TYR   A 1 190 ? -2.13694  26.01351 42.48278 1.000 41.99033  ? 197 TYR   A CE1 1 
ATOM   1409 C  CE2 . TYR   A 1 190 ? -0.40954  24.38921 42.14736 1.000 41.15774  ? 197 TYR   A CE2 1 
ATOM   1410 C  CZ  . TYR   A 1 190 ? -0.88966  25.51150 42.79472 1.000 44.47253  ? 197 TYR   A CZ  1 
ATOM   1411 O  OH  . TYR   A 1 190 ? -0.12595  26.13276 43.75920 1.000 41.15799  ? 197 TYR   A OH  1 
ATOM   1412 N  N   . LEU   A 1 191 ? -5.70327  20.93757 39.64824 1.000 40.99212  ? 198 LEU   A N   1 
ATOM   1413 C  CA  . LEU   A 1 191 ? -6.71709  20.26790 38.85724 1.000 42.13810  ? 198 LEU   A CA  1 
ATOM   1414 C  C   . LEU   A 1 191 ? -8.06447  20.24422 39.55646 1.000 42.58988  ? 198 LEU   A C   1 
ATOM   1415 O  O   . LEU   A 1 191 ? -9.04097  19.79557 38.95876 1.000 42.83341  ? 198 LEU   A O   1 
ATOM   1416 C  CB  . LEU   A 1 191 ? -6.28103  18.83634 38.52639 1.000 47.06163  ? 198 LEU   A CB  1 
ATOM   1417 C  CG  . LEU   A 1 191 ? -4.96119  18.66711 37.76924 1.000 49.18223  ? 198 LEU   A CG  1 
ATOM   1418 C  CD1 . LEU   A 1 191 ? -4.57507  17.19783 37.70151 1.000 37.29613  ? 198 LEU   A CD1 1 
ATOM   1419 C  CD2 . LEU   A 1 191 ? -5.04188  19.27034 36.37090 1.000 40.58098  ? 198 LEU   A CD2 1 
ATOM   1420 N  N   . GLU   A 1 192 ? -8.14464  20.71778 40.80021 1.000 47.32422  ? 199 GLU   A N   1 
ATOM   1421 C  CA  . GLU   A 1 192 ? -9.39293  20.68577 41.55338 1.000 43.71647  ? 199 GLU   A CA  1 
ATOM   1422 C  C   . GLU   A 1 192 ? -10.22005 21.93350 41.27724 1.000 41.49299  ? 199 GLU   A C   1 
ATOM   1423 O  O   . GLU   A 1 192 ? -9.69581  23.05164 41.22941 1.000 38.67424  ? 199 GLU   A O   1 
ATOM   1424 C  CB  . GLU   A 1 192 ? -9.12922  20.55763 43.05441 1.000 47.91841  ? 199 GLU   A CB  1 
ATOM   1425 C  CG  . GLU   A 1 192 ? -7.96974  19.63882 43.40087 1.000 64.08177  ? 199 GLU   A CG  1 
ATOM   1426 C  CD  . GLU   A 1 192 ? -8.42892  18.27855 43.89353 1.000 75.09982  ? 199 GLU   A CD  1 
ATOM   1427 O  OE1 . GLU   A 1 192 ? -9.64480  17.99714 43.80769 1.000 77.42361  ? 199 GLU   A OE1 1 
ATOM   1428 O  OE2 . GLU   A 1 192 ? -7.57466  17.49560 44.36838 1.000 77.41323  ? 199 GLU   A OE2 1 
ATOM   1429 N  N   . GLU   A 1 193 ? -11.52650 21.72614 41.11768 1.000 44.10871  ? 200 GLU   A N   1 
ATOM   1430 C  CA  . GLU   A 1 193 ? -12.42063 22.80133 40.70089 1.000 50.57123  ? 200 GLU   A CA  1 
ATOM   1431 C  C   . GLU   A 1 193 ? -12.40898 23.96518 41.68899 1.000 47.89862  ? 200 GLU   A C   1 
ATOM   1432 O  O   . GLU   A 1 193 ? -12.29942 25.13069 41.28914 1.000 38.02754  ? 200 GLU   A O   1 
ATOM   1433 C  CB  . GLU   A 1 193 ? -13.83180 22.24511 40.52887 1.000 44.36984  ? 200 GLU   A CB  1 
ATOM   1434 C  CG  . GLU   A 1 193 ? -14.85491 23.25294 40.06710 1.000 55.20371  ? 200 GLU   A CG  1 
ATOM   1435 C  CD  . GLU   A 1 193 ? -16.25319 22.66724 40.05273 1.000 69.70236  ? 200 GLU   A CD  1 
ATOM   1436 O  OE1 . GLU   A 1 193 ? -16.37435 21.42261 40.02304 1.000 71.48073  ? 200 GLU   A OE1 1 
ATOM   1437 O  OE2 . GLU   A 1 193 ? -17.22852 23.44669 40.07669 1.000 87.91705  ? 200 GLU   A OE2 1 
ATOM   1438 N  N   . ARG   A 1 194 ? -12.52453 23.67425 42.98761 1.000 46.12361  ? 201 ARG   A N   1 
ATOM   1439 C  CA  . ARG   A 1 194 ? -12.60734 24.76175 43.95537 1.000 43.12418  ? 201 ARG   A CA  1 
ATOM   1440 C  C   . ARG   A 1 194 ? -11.27762 25.48116 44.13018 1.000 40.50537  ? 201 ARG   A C   1 
ATOM   1441 O  O   . ARG   A 1 194 ? -11.26964 26.65309 44.52247 1.000 44.86882  ? 201 ARG   A O   1 
ATOM   1442 C  CB  . ARG   A 1 194 ? -13.12387 24.24980 45.30519 1.000 46.17141  ? 201 ARG   A CB  1 
ATOM   1443 C  CG  . ARG   A 1 194 ? -12.28273 23.17831 45.96322 1.000 61.41240  ? 201 ARG   A CG  1 
ATOM   1444 C  CD  . ARG   A 1 194 ? -12.96546 22.67616 47.23512 1.000 60.76348  ? 201 ARG   A CD  1 
ATOM   1445 N  NE  . ARG   A 1 194 ? -12.12990 21.73890 47.97784 1.000 65.21638  ? 201 ARG   A NE  1 
ATOM   1446 C  CZ  . ARG   A 1 194 ? -12.37310 21.33147 49.21763 1.000 74.69196  ? 201 ARG   A CZ  1 
ATOM   1447 N  NH1 . ARG   A 1 194 ? -13.42708 21.76145 49.89503 1.000 60.58039  ? 201 ARG   A NH1 1 
ATOM   1448 N  NH2 . ARG   A 1 194 ? -11.53599 20.47271 49.79419 1.000 75.57460  ? 201 ARG   A NH2 1 
ATOM   1449 N  N   . ARG   A 1 195 ? -10.15799 24.82465 43.82577 1.000 43.49735  ? 202 ARG   A N   1 
ATOM   1450 C  CA  . ARG   A 1 195 ? -8.87169  25.50486 43.92205 1.000 39.89378  ? 202 ARG   A CA  1 
ATOM   1451 C  C   . ARG   A 1 195 ? -8.66832  26.47637 42.76570 1.000 37.38251  ? 202 ARG   A C   1 
ATOM   1452 O  O   . ARG   A 1 195 ? -8.18752  27.59548 42.97136 1.000 37.47807  ? 202 ARG   A O   1 
ATOM   1453 C  CB  . ARG   A 1 195 ? -7.73598  24.48525 43.96718 1.000 40.45573  ? 202 ARG   A CB  1 
ATOM   1454 C  CG  . ARG   A 1 195 ? -6.36182  25.11584 44.05780 1.000 35.51465  ? 202 ARG   A CG  1 
ATOM   1455 C  CD  . ARG   A 1 195 ? -6.11753  25.67311 45.45232 1.000 42.96347  ? 202 ARG   A CD  1 
ATOM   1456 N  NE  . ARG   A 1 195 ? -4.71933  26.04116 45.64091 1.000 42.63582  ? 202 ARG   A NE  1 
ATOM   1457 C  CZ  . ARG   A 1 195 ? -4.28558  27.28444 45.79260 1.000 44.06066  ? 202 ARG   A CZ  1 
ATOM   1458 N  NH1 . ARG   A 1 195 ? -5.12003  28.31118 45.79654 1.000 43.30835  ? 202 ARG   A NH1 1 
ATOM   1459 N  NH2 . ARG   A 1 195 ? -2.98228  27.50285 45.94795 1.000 40.05599  ? 202 ARG   A NH2 1 
ATOM   1460 N  N   . ILE   A 1 196 ? -9.03267  26.06820 41.54761 1.000 34.76195  ? 203 ILE   A N   1 
ATOM   1461 C  CA  . ILE   A 1 196 ? -8.91746  26.96178 40.39835 1.000 37.81374  ? 203 ILE   A CA  1 
ATOM   1462 C  C   . ILE   A 1 196 ? -9.83513  28.16855 40.56648 1.000 38.98635  ? 203 ILE   A C   1 
ATOM   1463 O  O   . ILE   A 1 196 ? -9.45975  29.30203 40.24157 1.000 40.28464  ? 203 ILE   A O   1 
ATOM   1464 C  CB  . ILE   A 1 196 ? -9.22137  26.19968 39.09629 1.000 36.93234  ? 203 ILE   A CB  1 
ATOM   1465 C  CG1 . ILE   A 1 196 ? -8.17027  25.12228 38.84463 1.000 34.89997  ? 203 ILE   A CG1 1 
ATOM   1466 C  CG2 . ILE   A 1 196 ? -9.27448  27.15539 37.92031 1.000 35.06840  ? 203 ILE   A CG2 1 
ATOM   1467 C  CD1 . ILE   A 1 196 ? -8.63596  24.05751 37.87274 1.000 36.89584  ? 203 ILE   A CD1 1 
ATOM   1468 N  N   . LYS   A 1 197 ? -11.04881 27.94942 41.08056 1.000 34.90747  ? 204 LYS   A N   1 
ATOM   1469 C  CA  . LYS   A 1 197 ? -11.97618 29.06081 41.26308 1.000 38.03891  ? 204 LYS   A CA  1 
ATOM   1470 C  C   . LYS   A 1 197 ? -11.41965 30.08146 42.24478 1.000 42.03999  ? 204 LYS   A C   1 
ATOM   1471 O  O   . LYS   A 1 197 ? -11.51834 31.29406 42.01821 1.000 37.47239  ? 204 LYS   A O   1 
ATOM   1472 C  CB  . LYS   A 1 197 ? -13.33200 28.54760 41.74435 1.000 40.12084  ? 204 LYS   A CB  1 
ATOM   1473 C  CG  . LYS   A 1 197 ? -14.20418 27.96301 40.64905 1.000 53.75482  ? 204 LYS   A CG  1 
ATOM   1474 C  CD  . LYS   A 1 197 ? -15.61867 27.70175 41.15598 1.000 52.82944  ? 204 LYS   A CD  1 
ATOM   1475 C  CE  . LYS   A 1 197 ? -16.40885 26.84659 40.18199 1.000 55.40388  ? 204 LYS   A CE  1 
ATOM   1476 N  NZ  . LYS   A 1 197 ? -17.42275 26.00854 40.87708 1.000 74.30080  ? 204 LYS   A NZ  1 
ATOM   1477 N  N   . GLU   A 1 198 ? -10.82657 29.60310 43.34018 1.000 37.64240  ? 205 GLU   A N   1 
ATOM   1478 C  CA  . GLU   A 1 198 ? -10.25122 30.49835 44.33625 1.000 37.95033  ? 205 GLU   A CA  1 
ATOM   1479 C  C   . GLU   A 1 198 ? -9.11131  31.32205 43.74691 1.000 38.88367  ? 205 GLU   A C   1 
ATOM   1480 O  O   . GLU   A 1 198 ? -8.96557  32.50831 44.06318 1.000 43.93043  ? 205 GLU   A O   1 
ATOM   1481 C  CB  . GLU   A 1 198 ? -9.77561  29.67985 45.53652 1.000 38.70258  ? 205 GLU   A CB  1 
ATOM   1482 C  CG  . GLU   A 1 198 ? -8.93238  30.43435 46.54709 1.000 46.14627  ? 205 GLU   A CG  1 
ATOM   1483 C  CD  . GLU   A 1 198 ? -8.26710  29.49851 47.54644 1.000 57.22790  ? 205 GLU   A CD  1 
ATOM   1484 O  OE1 . GLU   A 1 198 ? -7.70150  28.47111 47.10798 1.000 51.73554  ? 205 GLU   A OE1 1 
ATOM   1485 O  OE2 . GLU   A 1 198 ? -8.31780  29.78158 48.76691 1.000 50.70165  ? 205 GLU   A OE2 1 
ATOM   1486 N  N   . ILE   A 1 199 ? -8.30460  30.71550 42.87310 1.000 37.01848  ? 206 ILE   A N   1 
ATOM   1487 C  CA  . ILE   A 1 199 ? -7.17335  31.42532 42.28189 1.000 30.40411  ? 206 ILE   A CA  1 
ATOM   1488 C  C   . ILE   A 1 199 ? -7.65403  32.46709 41.28000 1.000 34.14425  ? 206 ILE   A C   1 
ATOM   1489 O  O   . ILE   A 1 199 ? -7.14432  33.59485 41.24371 1.000 36.80765  ? 206 ILE   A O   1 
ATOM   1490 C  CB  . ILE   A 1 199 ? -6.19940  30.42350 41.63654 1.000 39.10000  ? 206 ILE   A CB  1 
ATOM   1491 C  CG1 . ILE   A 1 199 ? -5.57799  29.52637 42.70804 1.000 43.22202  ? 206 ILE   A CG1 1 
ATOM   1492 C  CG2 . ILE   A 1 199 ? -5.11723  31.14968 40.85081 1.000 30.54061  ? 206 ILE   A CG2 1 
ATOM   1493 C  CD1 . ILE   A 1 199 ? -4.98285  28.25290 42.15971 1.000 40.43674  ? 206 ILE   A CD1 1 
ATOM   1494 N  N   . VAL   A 1 200 ? -8.64240  32.11246 40.45589 1.000 30.18519  ? 207 VAL   A N   1 
ATOM   1495 C  CA  . VAL   A 1 200 ? -9.14623  33.03905 39.44627 1.000 31.29684  ? 207 VAL   A CA  1 
ATOM   1496 C  C   . VAL   A 1 200 ? -9.80863  34.24353 40.10759 1.000 32.97293  ? 207 VAL   A C   1 
ATOM   1497 O  O   . VAL   A 1 200 ? -9.55354  35.39557 39.73969 1.000 39.49228  ? 207 VAL   A O   1 
ATOM   1498 C  CB  . VAL   A 1 200 ? -10.10935 32.30954 38.49115 1.000 39.34519  ? 207 VAL   A CB  1 
ATOM   1499 C  CG1 . VAL   A 1 200 ? -10.87671 33.30705 37.64087 1.000 31.33048  ? 207 VAL   A CG1 1 
ATOM   1500 C  CG2 . VAL   A 1 200 ? -9.33951  31.32648 37.60785 1.000 27.00822  ? 207 VAL   A CG2 1 
ATOM   1501 N  N   . LYS   A 1 201 ? -10.65827 33.99552 41.10255 1.000 32.69473  ? 208 LYS   A N   1 
ATOM   1502 C  CA  . LYS   A 1 201 ? -11.30105 35.08941 41.82088 1.000 36.86700  ? 208 LYS   A CA  1 
ATOM   1503 C  C   . LYS   A 1 201 ? -10.27189 35.98669 42.50476 1.000 40.53084  ? 208 LYS   A C   1 
ATOM   1504 O  O   . LYS   A 1 201 ? -10.44222 37.21013 42.56286 1.000 48.46243  ? 208 LYS   A O   1 
ATOM   1505 C  CB  . LYS   A 1 201 ? -12.29816 34.51710 42.83332 1.000 36.61530  ? 208 LYS   A CB  1 
ATOM   1506 C  CG  . LYS   A 1 201 ? -12.61672 35.41150 44.01703 1.000 39.16445  ? 208 LYS   A CG  1 
ATOM   1507 C  CD  . LYS   A 1 201 ? -13.95777 36.08835 43.83979 1.000 48.25333  ? 208 LYS   A CD  1 
ATOM   1508 C  CE  . LYS   A 1 201 ? -14.47577 36.63421 45.15876 1.000 63.60719  ? 208 LYS   A CE  1 
ATOM   1509 N  NZ  . LYS   A 1 201 ? -15.55163 37.64439 44.95026 1.000 75.00477  ? 208 LYS   A NZ  1 
ATOM   1510 N  N   . LYS   A 1 202 ? -9.18397  35.40337 43.00536 1.000 38.63238  ? 209 LYS   A N   1 
ATOM   1511 C  CA  . LYS   A 1 202 ? -8.20321  36.18778 43.74779 1.000 38.42115  ? 209 LYS   A CA  1 
ATOM   1512 C  C   . LYS   A 1 202 ? -7.34045  37.05213 42.82947 1.000 42.18460  ? 209 LYS   A C   1 
ATOM   1513 O  O   . LYS   A 1 202 ? -7.08260  38.22083 43.13748 1.000 47.21363  ? 209 LYS   A O   1 
ATOM   1514 C  CB  . LYS   A 1 202 ? -7.32770  35.25525 44.58528 1.000 41.10545  ? 209 LYS   A CB  1 
ATOM   1515 C  CG  . LYS   A 1 202 ? -6.34017  35.95998 45.49907 1.000 45.58641  ? 209 LYS   A CG  1 
ATOM   1516 C  CD  . LYS   A 1 202 ? -5.59333  34.94477 46.35659 1.000 50.18267  ? 209 LYS   A CD  1 
ATOM   1517 C  CE  . LYS   A 1 202 ? -4.46305  35.58735 47.14716 1.000 54.99400  ? 209 LYS   A CE  1 
ATOM   1518 N  NZ  . LYS   A 1 202 ? -3.65444  34.55337 47.85775 1.000 61.07729  ? 209 LYS   A NZ  1 
ATOM   1519 N  N   . HIS   A 1 203 ? -6.89483  36.50830 41.69447 1.000 44.75757  ? 210 HIS   A N   1 
ATOM   1520 C  CA  . HIS   A 1 203 ? -5.89540  37.17537 40.87102 1.000 38.42101  ? 210 HIS   A CA  1 
ATOM   1521 C  C   . HIS   A 1 203 ? -6.40741  37.67643 39.52849 1.000 39.51391  ? 210 HIS   A C   1 
ATOM   1522 O  O   . HIS   A 1 203 ? -5.77102  38.55661 38.93905 1.000 44.58713  ? 210 HIS   A O   1 
ATOM   1523 C  CB  . HIS   A 1 203 ? -4.70843  36.23466 40.61220 1.000 38.12346  ? 210 HIS   A CB  1 
ATOM   1524 C  CG  . HIS   A 1 203 ? -3.96295  35.84762 41.85061 1.000 46.30312  ? 210 HIS   A CG  1 
ATOM   1525 N  ND1 . HIS   A 1 203 ? -3.30674  36.76725 42.64156 1.000 51.77963  ? 210 HIS   A ND1 1 
ATOM   1526 C  CD2 . HIS   A 1 203 ? -3.76642  34.64065 42.43321 1.000 43.09736  ? 210 HIS   A CD2 1 
ATOM   1527 C  CE1 . HIS   A 1 203 ? -2.74017  36.14362 43.65971 1.000 50.04517  ? 210 HIS   A CE1 1 
ATOM   1528 N  NE2 . HIS   A 1 203 ? -3.00284  34.85276 43.55597 1.000 54.10184  ? 210 HIS   A NE2 1 
ATOM   1529 N  N   . SER   A 1 204 ? -7.52129  37.14502 39.02495 1.000 36.10585  ? 211 SER   A N   1 
ATOM   1530 C  CA  . SER   A 1 204 ? -7.96904  37.46205 37.67390 1.000 40.35074  ? 211 SER   A CA  1 
ATOM   1531 C  C   . SER   A 1 204 ? -9.42010  37.91741 37.65856 1.000 32.29486  ? 211 SER   A C   1 
ATOM   1532 O  O   . SER   A 1 204 ? -10.10461 37.78582 36.64301 1.000 41.44070  ? 211 SER   A O   1 
ATOM   1533 C  CB  . SER   A 1 204 ? -7.78021  36.26216 36.74638 1.000 39.63871  ? 211 SER   A CB  1 
ATOM   1534 O  OG  . SER   A 1 204 ? -6.47354  35.73279 36.87393 1.000 42.48966  ? 211 SER   A OG  1 
ATOM   1535 N  N   . GLN   A 1 205 ? -9.90151  38.45615 38.77746 1.000 36.57398  ? 212 GLN   A N   1 
ATOM   1536 C  CA  . GLN   A 1 205 ? -11.30515 38.83879 38.86647 1.000 41.88566  ? 212 GLN   A CA  1 
ATOM   1537 C  C   . GLN   A 1 205 ? -11.67983 39.87659 37.81422 1.000 42.91262  ? 212 GLN   A C   1 
ATOM   1538 O  O   . GLN   A 1 205 ? -12.80110 39.85472 37.29587 1.000 46.87196  ? 212 GLN   A O   1 
ATOM   1539 C  CB  . GLN   A 1 205 ? -11.60637 39.36771 40.26920 1.000 42.81784  ? 212 GLN   A CB  1 
ATOM   1540 C  CG  . GLN   A 1 205 ? -12.98302 39.97174 40.41924 1.000 53.07659  ? 212 GLN   A CG  1 
ATOM   1541 C  CD  . GLN   A 1 205 ? -13.38346 40.14707 41.86476 1.000 58.68050  ? 212 GLN   A CD  1 
ATOM   1542 O  OE1 . GLN   A 1 205 ? -14.53558 39.91204 42.23473 1.000 71.95597  ? 212 GLN   A OE1 1 
ATOM   1543 N  NE2 . GLN   A 1 205 ? -12.43714 40.57748 42.69256 1.000 58.27337  ? 212 GLN   A NE2 1 
ATOM   1544 N  N   . PHE   A 1 206 ? -10.75251 40.76627 37.45817 1.000 48.23102  ? 213 PHE   A N   1 
ATOM   1545 C  CA  . PHE   A 1 206 ? -11.05695 41.91984 36.62105 1.000 40.02574  ? 213 PHE   A CA  1 
ATOM   1546 C  C   . PHE   A 1 206 ? -10.61385 41.75831 35.17100 1.000 39.12266  ? 213 PHE   A C   1 
ATOM   1547 O  O   . PHE   A 1 206 ? -10.62453 42.74050 34.42106 1.000 44.90174  ? 213 PHE   A O   1 
ATOM   1548 C  CB  . PHE   A 1 206 ? -10.43011 43.17113 37.22753 1.000 37.59167  ? 213 PHE   A CB  1 
ATOM   1549 C  CG  . PHE   A 1 206 ? -10.93771 43.48280 38.60126 1.000 41.88206  ? 213 PHE   A CG  1 
ATOM   1550 C  CD1 . PHE   A 1 206 ? -12.29238 43.41552 38.87855 1.000 38.85734  ? 213 PHE   A CD1 1 
ATOM   1551 C  CD2 . PHE   A 1 206 ? -10.06356 43.82654 39.61785 1.000 45.18394  ? 213 PHE   A CD2 1 
ATOM   1552 C  CE1 . PHE   A 1 206 ? -12.76853 43.69796 40.13750 1.000 44.57250  ? 213 PHE   A CE1 1 
ATOM   1553 C  CE2 . PHE   A 1 206 ? -10.53210 44.10941 40.88240 1.000 48.90917  ? 213 PHE   A CE2 1 
ATOM   1554 C  CZ  . PHE   A 1 206 ? -11.88788 44.04344 41.14455 1.000 48.69045  ? 213 PHE   A CZ  1 
ATOM   1555 N  N   . ILE   A 1 207 ? -10.23110 40.54820 34.75639 1.000 36.38991  ? 214 ILE   A N   1 
ATOM   1556 C  CA  . ILE   A 1 207 ? -9.95277  40.29760 33.34663 1.000 38.49412  ? 214 ILE   A CA  1 
ATOM   1557 C  C   . ILE   A 1 207 ? -11.20572 40.58714 32.52928 1.000 35.53083  ? 214 ILE   A C   1 
ATOM   1558 O  O   . ILE   A 1 207 ? -12.31014 40.15764 32.88323 1.000 40.48207  ? 214 ILE   A O   1 
ATOM   1559 C  CB  . ILE   A 1 207 ? -9.46437  38.85333 33.15484 1.000 33.33396  ? 214 ILE   A CB  1 
ATOM   1560 C  CG1 . ILE   A 1 207 ? -8.12141  38.65491 33.85950 1.000 32.85101  ? 214 ILE   A CG1 1 
ATOM   1561 C  CG2 . ILE   A 1 207 ? -9.34547  38.51133 31.67967 1.000 28.56973  ? 214 ILE   A CG2 1 
ATOM   1562 C  CD1 . ILE   A 1 207 ? -6.97621  39.44001 33.23780 1.000 33.61877  ? 214 ILE   A CD1 1 
ATOM   1563 N  N   . GLY   A 1 208 ? -11.04130 41.32434 31.43091 1.000 37.19578  ? 215 GLY   A N   1 
ATOM   1564 C  CA  . GLY   A 1 208 ? -12.17560 41.79301 30.65410 1.000 33.65560  ? 215 GLY   A CA  1 
ATOM   1565 C  C   . GLY   A 1 208 ? -12.67447 40.85376 29.57090 1.000 39.48097  ? 215 GLY   A C   1 
ATOM   1566 O  O   . GLY   A 1 208 ? -13.21024 41.30420 28.55235 1.000 41.85967  ? 215 GLY   A O   1 
ATOM   1567 N  N   . TYR   A 1 209 ? -12.50912 39.55059 29.77371 1.000 36.58022  ? 216 TYR   A N   1 
ATOM   1568 C  CA  . TYR   A 1 209 ? -13.03596 38.53274 28.87704 1.000 36.79504  ? 216 TYR   A CA  1 
ATOM   1569 C  C   . TYR   A 1 209 ? -13.63549 37.41385 29.71312 1.000 32.62605  ? 216 TYR   A C   1 
ATOM   1570 O  O   . TYR   A 1 209 ? -13.20748 37.19119 30.85156 1.000 33.99575  ? 216 TYR   A O   1 
ATOM   1571 C  CB  . TYR   A 1 209 ? -11.94716 37.97976 27.93895 1.000 33.23665  ? 216 TYR   A CB  1 
ATOM   1572 C  CG  . TYR   A 1 209 ? -11.34137 39.06428 27.08442 1.000 36.83792  ? 216 TYR   A CG  1 
ATOM   1573 C  CD1 . TYR   A 1 209 ? -11.99009 39.50876 25.94149 1.000 30.93334  ? 216 TYR   A CD1 1 
ATOM   1574 C  CD2 . TYR   A 1 209 ? -10.13943 39.67368 27.44146 1.000 31.52255  ? 216 TYR   A CD2 1 
ATOM   1575 C  CE1 . TYR   A 1 209 ? -11.45841 40.51697 25.16774 1.000 34.58339  ? 216 TYR   A CE1 1 
ATOM   1576 C  CE2 . TYR   A 1 209 ? -9.59545  40.68471 26.67174 1.000 31.69567  ? 216 TYR   A CE2 1 
ATOM   1577 C  CZ  . TYR   A 1 209 ? -10.26276 41.10510 25.53527 1.000 31.03741  ? 216 TYR   A CZ  1 
ATOM   1578 O  OH  . TYR   A 1 209 ? -9.74025  42.11336 24.75606 1.000 34.04525  ? 216 TYR   A OH  1 
ATOM   1579 N  N   . PRO   A 1 210 ? -14.64665 36.71669 29.19490 1.000 35.86200  ? 217 PRO   A N   1 
ATOM   1580 C  CA  . PRO   A 1 210 ? -15.25846 35.62893 29.97189 1.000 29.30131  ? 217 PRO   A CA  1 
ATOM   1581 C  C   . PRO   A 1 210 ? -14.28745 34.47020 30.14174 1.000 31.67542  ? 217 PRO   A C   1 
ATOM   1582 O  O   . PRO   A 1 210 ? -13.65833 34.02253 29.18043 1.000 35.50425  ? 217 PRO   A O   1 
ATOM   1583 C  CB  . PRO   A 1 210 ? -16.48212 35.22781 29.13605 1.000 29.47767  ? 217 PRO   A CB  1 
ATOM   1584 C  CG  . PRO   A 1 210 ? -16.23217 35.77936 27.77030 1.000 33.52322  ? 217 PRO   A CG  1 
ATOM   1585 C  CD  . PRO   A 1 210 ? -15.37233 36.99147 27.94034 1.000 28.76920  ? 217 PRO   A CD  1 
ATOM   1586 N  N   . ILE   A 1 211 ? -14.16247 33.99801 31.37941 1.000 29.96443  ? 218 ILE   A N   1 
ATOM   1587 C  CA  . ILE   A 1 211 ? -13.33119 32.84987 31.72528 1.000 30.12767  ? 218 ILE   A CA  1 
ATOM   1588 C  C   . ILE   A 1 211 ? -14.25633 31.71376 32.14559 1.000 37.80584  ? 218 ILE   A C   1 
ATOM   1589 O  O   . ILE   A 1 211 ? -15.01065 31.84542 33.11739 1.000 35.60730  ? 218 ILE   A O   1 
ATOM   1590 C  CB  . ILE   A 1 211 ? -12.33120 33.18826 32.84136 1.000 33.79266  ? 218 ILE   A CB  1 
ATOM   1591 C  CG1 . ILE   A 1 211 ? -11.51671 34.43430 32.47417 1.000 35.48313  ? 218 ILE   A CG1 1 
ATOM   1592 C  CG2 . ILE   A 1 211 ? -11.41687 31.99576 33.12084 1.000 27.54686  ? 218 ILE   A CG2 1 
ATOM   1593 C  CD1 . ILE   A 1 211 ? -10.56835 34.91126 33.57695 1.000 27.51803  ? 218 ILE   A CD1 1 
ATOM   1594 N  N   . THR   A 1 212 ? -14.20651 30.60214 31.41700 1.000 31.89161  ? 219 THR   A N   1 
ATOM   1595 C  CA  . THR   A 1 212 ? -15.05393 29.44817 31.68963 1.000 35.73789  ? 219 THR   A CA  1 
ATOM   1596 C  C   . THR   A 1 212 ? -14.20141 28.30142 32.20904 1.000 28.45533  ? 219 THR   A C   1 
ATOM   1597 O  O   . THR   A 1 212 ? -13.22335 27.91197 31.56623 1.000 32.69717  ? 219 THR   A O   1 
ATOM   1598 C  CB  . THR   A 1 212 ? -15.81667 29.01059 30.43536 1.000 35.44374  ? 219 THR   A CB  1 
ATOM   1599 O  OG1 . THR   A 1 212 ? -16.53047 30.12947 29.89903 1.000 37.48763  ? 219 THR   A OG1 1 
ATOM   1600 C  CG2 . THR   A 1 212 ? -16.80821 27.90485 30.76869 1.000 32.95407  ? 219 THR   A CG2 1 
ATOM   1601 N  N   . LEU   A 1 213 ? -14.57428 27.76687 33.37014 1.000 37.08294  ? 220 LEU   A N   1 
ATOM   1602 C  CA  . LEU   A 1 213 ? -13.89434 26.62596 33.97476 1.000 38.43342  ? 220 LEU   A CA  1 
ATOM   1603 C  C   . LEU   A 1 213 ? -14.67304 25.35549 33.64524 1.000 40.91193  ? 220 LEU   A C   1 
ATOM   1604 O  O   . LEU   A 1 213 ? -15.75100 25.11830 34.20077 1.000 42.93079  ? 220 LEU   A O   1 
ATOM   1605 C  CB  . LEU   A 1 213 ? -13.76184 26.81313 35.48358 1.000 35.33528  ? 220 LEU   A CB  1 
ATOM   1606 C  CG  . LEU   A 1 213 ? -13.11770 25.65365 36.24956 1.000 48.07967  ? 220 LEU   A CG  1 
ATOM   1607 C  CD1 . LEU   A 1 213 ? -11.76107 25.26357 35.67317 1.000 39.19477  ? 220 LEU   A CD1 1 
ATOM   1608 C  CD2 . LEU   A 1 213 ? -13.01075 25.98127 37.74125 1.000 51.08609  ? 220 LEU   A CD2 1 
ATOM   1609 N  N   . PHE   A 1 214 ? -14.12288 24.53909 32.74830 1.000 35.52871  ? 221 PHE   A N   1 
ATOM   1610 C  CA  . PHE   A 1 214 ? -14.75790 23.27860 32.37470 1.000 42.56728  ? 221 PHE   A CA  1 
ATOM   1611 C  C   . PHE   A 1 214 ? -14.67181 22.29828 33.53882 1.000 40.66318  ? 221 PHE   A C   1 
ATOM   1612 O  O   . PHE   A 1 214 ? -13.57596 21.99610 34.01947 1.000 47.25808  ? 221 PHE   A O   1 
ATOM   1613 C  CB  . PHE   A 1 214 ? -14.08054 22.68061 31.14209 1.000 36.80494  ? 221 PHE   A CB  1 
ATOM   1614 C  CG  . PHE   A 1 214 ? -14.43610 23.35882 29.84676 1.000 35.80720  ? 221 PHE   A CG  1 
ATOM   1615 C  CD1 . PHE   A 1 214 ? -14.54625 24.73772 29.76653 1.000 42.62743  ? 221 PHE   A CD1 1 
ATOM   1616 C  CD2 . PHE   A 1 214 ? -14.64148 22.61116 28.69986 1.000 41.08042  ? 221 PHE   A CD2 1 
ATOM   1617 C  CE1 . PHE   A 1 214 ? -14.86825 25.35912 28.56875 1.000 42.57082  ? 221 PHE   A CE1 1 
ATOM   1618 C  CE2 . PHE   A 1 214 ? -14.96276 23.22455 27.49906 1.000 50.97239  ? 221 PHE   A CE2 1 
ATOM   1619 C  CZ  . PHE   A 1 214 ? -15.07500 24.60276 27.43453 1.000 38.55474  ? 221 PHE   A CZ  1 
ATOM   1620 N  N   . VAL   A 1 215 ? -15.81173 21.79595 33.98925 1.000 36.40336  ? 222 VAL   A N   1 
ATOM   1621 C  CA  . VAL   A 1 215 ? -15.84321 20.78585 35.04119 1.000 37.16458  ? 222 VAL   A CA  1 
ATOM   1622 C  C   . VAL   A 1 215 ? -15.78343 19.40930 34.38678 1.000 40.97873  ? 222 VAL   A C   1 
ATOM   1623 O  O   . VAL   A 1 215 ? -16.33221 19.20581 33.29824 1.000 46.57648  ? 222 VAL   A O   1 
ATOM   1624 C  CB  . VAL   A 1 215 ? -17.09681 20.96765 35.92284 1.000 42.12656  ? 222 VAL   A CB  1 
ATOM   1625 C  CG1 . VAL   A 1 215 ? -18.23517 21.55830 35.11213 1.000 37.07450  ? 222 VAL   A CG1 1 
ATOM   1626 C  CG2 . VAL   A 1 215 ? -17.51502 19.66384 36.59263 1.000 38.76010  ? 222 VAL   A CG2 1 
ATOM   1627 N  N   . GLU   A 1 216 ? -15.08840 18.46724 35.02069 1.000 39.88752  ? 223 GLU   A N   1 
ATOM   1628 C  CA  . GLU   A 1 216 ? -14.95077 17.14038 34.43922 1.000 49.70143  ? 223 GLU   A CA  1 
ATOM   1629 C  C   . GLU   A 1 216 ? -16.17031 16.26641 34.72382 1.000 48.01309  ? 223 GLU   A C   1 
ATOM   1630 O  O   . GLU   A 1 216 ? -17.01307 16.56662 35.57411 1.000 48.78784  ? 223 GLU   A O   1 
ATOM   1631 C  CB  . GLU   A 1 216 ? -13.69932 16.44715 34.95960 1.000 50.09848  ? 223 GLU   A CB  1 
ATOM   1632 C  CG  . GLU   A 1 216 ? -12.42389 17.02131 34.40016 1.000 57.22727  ? 223 GLU   A CG  1 
ATOM   1633 C  CD  . GLU   A 1 216 ? -11.20766 16.64789 35.23035 1.000 61.60992  ? 223 GLU   A CD  1 
ATOM   1634 O  OE1 . GLU   A 1 216 ? -10.92819 17.34492 36.23659 1.000 67.76490  ? 223 GLU   A OE1 1 
ATOM   1635 O  OE2 . GLU   A 1 216 ? -10.54996 15.62645 34.91882 1.000 59.95729  ? 223 GLU   A OE2 1 
ATOM   1636 N  N   . LYS   A 1 217 ? -16.23834 15.15305 34.00009 1.000 57.84839  ? 224 LYS   A N   1 
ATOM   1637 C  CA  . LYS   A 1 217 ? -17.34245 14.20922 34.11097 1.000 57.53081  ? 224 LYS   A CA  1 
ATOM   1638 C  C   . LYS   A 1 217 ? -16.84505 12.87441 34.67571 1.000 54.47063  ? 224 LYS   A C   1 
ATOM   1639 O  O   . LYS   A 1 217 ? -16.43076 12.78895 35.83119 1.000 62.38766  ? 224 LYS   A O   1 
ATOM   1640 C  CB  . LYS   A 1 217 ? -18.00574 14.00188 32.74543 1.000 47.66910  ? 224 LYS   A CB  1 
ATOM   1641 C  CG  . LYS   A 1 217 ? -17.89104 15.19804 31.80289 1.000 46.80115  ? 224 LYS   A CG  1 
ATOM   1642 C  CD  . LYS   A 1 217 ? -18.37705 14.86983 30.38562 1.000 43.93854  ? 224 LYS   A CD  1 
ATOM   1643 C  CE  . LYS   A 1 217 ? -17.30882 14.15609 29.56150 1.000 45.95304  ? 224 LYS   A CE  1 
ATOM   1644 N  NZ  . LYS   A 1 217 ? -16.33495 15.10368 28.94244 1.000 51.39483  ? 224 LYS   A NZ  1 
HETATM 1645 C  C1  . A1AYM B 2 .   ? 6.87461   34.84685 26.71905 0.765 55.93096  ? 301 A1AYM A C1  1 
HETATM 1646 C  C2  . A1AYM B 2 .   ? 6.72250   32.80201 25.15857 0.765 44.93900  ? 301 A1AYM A C2  1 
HETATM 1647 C  C3  . A1AYM B 2 .   ? 8.00186   32.75041 24.60557 0.765 46.01682  ? 301 A1AYM A C3  1 
HETATM 1648 C  C4  . A1AYM B 2 .   ? 8.34575   31.74282 23.71383 0.765 46.87233  ? 301 A1AYM A C4  1 
HETATM 1649 C  C5  . A1AYM B 2 .   ? 7.41583   30.80124 23.39295 0.765 46.75663  ? 301 A1AYM A C5  1 
HETATM 1650 C  C6  . A1AYM B 2 .   ? 6.14800   30.82420 23.92421 0.765 48.88949  ? 301 A1AYM A C6  1 
HETATM 1651 C  C7  . A1AYM B 2 .   ? 5.79225   31.82543 24.81262 0.765 40.59528  ? 301 A1AYM A C7  1 
HETATM 1652 F  F1  . A1AYM B 2 .   ? 7.74198   29.81420 22.52426 0.765 55.78361  ? 301 A1AYM A F1  1 
HETATM 1653 N  N1  . A1AYM B 2 .   ? 6.12020   35.53952 27.55965 0.765 63.26431  ? 301 A1AYM A N1  1 
HETATM 1654 N  N2  . A1AYM B 2 .   ? 6.30011   33.80982 26.07962 0.765 45.48195  ? 301 A1AYM A N2  1 
HETATM 1655 S  S1  . A1AYM B 2 .   ? 8.49847   35.27225 26.47284 0.765 67.93210  ? 301 A1AYM A S1  1 
HETATM 1656 CL CL1 . A1AYM B 2 .   ? 5.00822   29.60422 23.48039 0.765 51.02668  ? 301 A1AYM A CL1 1 
HETATM 1657 O  O   . HOH   C 3 .   ? 5.08419   36.20933 29.37973 1.000 37.07386  ? 401 HOH   A O   1 
HETATM 1658 O  O   . HOH   C 3 .   ? 7.81890   44.80760 31.98038 1.000 57.61889  ? 402 HOH   A O   1 
HETATM 1659 O  O   . HOH   C 3 .   ? 7.05671   20.07584 11.08478 1.000 48.83025  ? 403 HOH   A O   1 
HETATM 1660 O  O   . HOH   C 3 .   ? -5.17393  39.54816 36.85541 1.000 39.38593  ? 404 HOH   A O   1 
HETATM 1661 O  O   . HOH   C 3 .   ? -1.37774  12.43975 38.54746 1.000 57.24658  ? 405 HOH   A O   1 
HETATM 1662 O  O   . HOH   C 3 .   ? -0.00515  38.46544 22.46765 1.000 36.36916  ? 406 HOH   A O   1 
HETATM 1663 O  O   . HOH   C 3 .   ? 3.00149   16.91661 23.56222 1.000 60.83041  ? 407 HOH   A O   1 
HETATM 1664 O  O   . HOH   C 3 .   ? 6.10399   24.46071 49.52529 1.000 50.58483  ? 408 HOH   A O   1 
HETATM 1665 O  O   . HOH   C 3 .   ? -6.18236  31.81328 12.24529 1.000 33.55749  ? 409 HOH   A O   1 
HETATM 1666 O  O   . HOH   C 3 .   ? -6.25579  19.84420 30.24062 1.000 39.82793  ? 410 HOH   A O   1 
HETATM 1667 O  O   . HOH   C 3 .   ? -0.31412  16.35534 44.05846 1.000 52.95595  ? 411 HOH   A O   1 
HETATM 1668 O  O   . HOH   C 3 .   ? -3.59595  33.78594 21.37153 1.000 32.46885  ? 412 HOH   A O   1 
HETATM 1669 O  O   . HOH   C 3 .   ? -5.22433  42.50239 28.97650 1.000 33.86323  ? 413 HOH   A O   1 
HETATM 1670 O  O   . HOH   C 3 .   ? -5.32331  19.94688 26.31782 1.000 43.14542  ? 414 HOH   A O   1 
HETATM 1671 O  O   . HOH   C 3 .   ? -14.70759 15.44192 31.89961 1.000 42.38644  ? 415 HOH   A O   1 
HETATM 1672 O  O   . HOH   C 3 .   ? 19.90036  26.36248 25.96553 1.000 47.90838  ? 416 HOH   A O   1 
HETATM 1673 O  O   . HOH   C 3 .   ? -0.66113  19.79957 44.94579 1.000 40.51473  ? 417 HOH   A O   1 
HETATM 1674 O  O   . HOH   C 3 .   ? 4.72650   18.60869 20.40396 1.000 54.92290  ? 418 HOH   A O   1 
HETATM 1675 O  O   . HOH   C 3 .   ? 10.87560  30.70167 48.99097 1.000 43.48817  ? 419 HOH   A O   1 
HETATM 1676 O  O   . HOH   C 3 .   ? -4.81435  37.23819 35.48147 1.000 38.01014  ? 420 HOH   A O   1 
HETATM 1677 O  O   . HOH   C 3 .   ? -12.18961 19.55529 32.19305 1.000 46.65764  ? 421 HOH   A O   1 
HETATM 1678 O  O   . HOH   C 3 .   ? 0.69596   39.43534 30.58835 1.000 39.30075  ? 422 HOH   A O   1 
HETATM 1679 O  O   . HOH   C 3 .   ? -3.52908  44.72142 26.41645 1.000 41.98325  ? 423 HOH   A O   1 
HETATM 1680 O  O   . HOH   C 3 .   ? 10.24450  17.47991 26.01311 1.000 46.39849  ? 424 HOH   A O   1 
HETATM 1681 O  O   . HOH   C 3 .   ? 0.31345   30.42915 13.44020 1.000 31.84671  ? 425 HOH   A O   1 
HETATM 1682 O  O   . HOH   C 3 .   ? -4.03284  13.50056 38.36866 1.000 54.05605  ? 426 HOH   A O   1 
HETATM 1683 O  O   . HOH   C 3 .   ? -4.68436  16.39546 28.29322 1.000 46.16741  ? 427 HOH   A O   1 
HETATM 1684 O  O   . HOH   C 3 .   ? -4.17915  38.85975 9.36540  1.000 45.77533  ? 428 HOH   A O   1 
HETATM 1685 O  O   . HOH   C 3 .   ? 14.77101  17.42964 16.24253 1.000 35.73158  ? 429 HOH   A O   1 
HETATM 1686 O  O   . HOH   C 3 .   ? 5.43454   14.94178 15.56236 1.000 56.97939  ? 430 HOH   A O   1 
HETATM 1687 O  O   . HOH   C 3 .   ? -12.30898 43.70720 27.70206 1.000 43.13185  ? 431 HOH   A O   1 
HETATM 1688 O  O   . HOH   C 3 .   ? -4.18095  36.36413 14.09504 1.000 27.33709  ? 432 HOH   A O   1 
HETATM 1689 O  O   . HOH   C 3 .   ? 19.49030  27.44702 38.81488 1.000 52.29747  ? 433 HOH   A O   1 
HETATM 1690 O  O   . HOH   C 3 .   ? 13.60744  19.68291 23.47067 1.000 45.05398  ? 434 HOH   A O   1 
HETATM 1691 O  O   . HOH   C 3 .   ? -17.32986 32.85202 24.23354 1.000 44.49354  ? 435 HOH   A O   1 
HETATM 1692 O  O   . HOH   C 3 .   ? 10.91948  32.92327 20.28639 1.000 50.42229  ? 436 HOH   A O   1 
HETATM 1693 O  O   . HOH   C 3 .   ? 12.48918  43.26699 27.86025 1.000 48.74413  ? 437 HOH   A O   1 
HETATM 1694 O  O   . HOH   C 3 .   ? 1.53963   24.39833 45.04936 1.000 45.72175  ? 438 HOH   A O   1 
HETATM 1695 O  O   . HOH   C 3 .   ? 16.264    19.847   14.935   1.000 40.07996  ? 439 HOH   A O   1 
HETATM 1696 O  O   . HOH   C 3 .   ? 12.72848  20.04692 26.49919 1.000 36.84722  ? 440 HOH   A O   1 
HETATM 1697 O  O   . HOH   C 3 .   ? 15.53091  25.22710 29.67654 1.000 38.95668  ? 441 HOH   A O   1 
HETATM 1698 O  O   . HOH   C 3 .   ? -6.43170  48.73598 14.26737 1.000 57.48758  ? 442 HOH   A O   1 
HETATM 1699 O  O   . HOH   C 3 .   ? -8.52343  42.24055 30.57291 1.000 36.34796  ? 443 HOH   A O   1 
HETATM 1700 O  O   . HOH   C 3 .   ? -15.55914 18.50838 30.73905 1.000 34.28455  ? 444 HOH   A O   1 
HETATM 1701 O  O   . HOH   C 3 .   ? -8.04206  45.99592 22.31377 1.000 40.76527  ? 445 HOH   A O   1 
HETATM 1702 O  O   . HOH   C 3 .   ? 17.05548  25.47428 31.76823 1.000 45.48242  ? 446 HOH   A O   1 
HETATM 1703 O  O   . HOH   C 3 .   ? 8.65640   37.47264 25.00857 1.000 40.31175  ? 447 HOH   A O   1 
HETATM 1704 O  O   . HOH   C 3 .   ? 9.05324   24.90182 40.84689 1.000 40.15262  ? 448 HOH   A O   1 
HETATM 1705 O  O   . HOH   C 3 .   ? 10.75602  29.65598 22.15388 1.000 46.37747  ? 449 HOH   A O   1 
HETATM 1706 O  O   . HOH   C 3 .   ? 6.76394   20.47289 19.09354 1.000 34.12282  ? 450 HOH   A O   1 
HETATM 1707 O  O   . HOH   C 3 .   ? -13.04848 43.73898 33.46244 1.000 46.14371  ? 451 HOH   A O   1 
HETATM 1708 O  O   . HOH   C 3 .   ? -12.02376 25.40454 24.25387 1.000 36.75680  ? 452 HOH   A O   1 
HETATM 1709 O  O   . HOH   C 3 .   ? -14.78019 31.58473 28.20420 1.000 36.15054  ? 453 HOH   A O   1 
HETATM 1710 O  O   . HOH   C 3 .   ? -1.97662  31.57871 28.34041 1.000 30.92971  ? 454 HOH   A O   1 
HETATM 1711 O  O   . HOH   C 3 .   ? -15.78850 38.66344 24.69420 1.000 41.74028  ? 455 HOH   A O   1 
HETATM 1712 O  O   . HOH   C 3 .   ? 10.89641  24.30196 43.18528 1.000 54.74938  ? 456 HOH   A O   1 
HETATM 1713 O  O   . HOH   C 3 .   ? 18.68758  20.22085 25.87548 1.000 51.16343  ? 457 HOH   A O   1 
HETATM 1714 O  O   . HOH   C 3 .   ? -3.47841  30.14798 26.31792 1.000 33.69727  ? 458 HOH   A O   1 
HETATM 1715 O  O   . HOH   C 3 .   ? 6.16990   33.03659 10.98247 1.000 42.60314  ? 459 HOH   A O   1 
HETATM 1716 O  O   . HOH   C 3 .   ? -12.69414 19.07381 41.13687 1.000 40.02725  ? 460 HOH   A O   1 
HETATM 1717 O  O   . HOH   C 3 .   ? -2.85751  39.41443 41.54015 1.000 48.78292  ? 461 HOH   A O   1 
HETATM 1718 O  O   . HOH   C 3 .   ? -13.36504 28.28130 45.72694 1.000 48.17049  ? 462 HOH   A O   1 
HETATM 1719 O  O   . HOH   C 3 .   ? -15.18882 40.34224 32.43206 1.000 49.16175  ? 463 HOH   A O   1 
HETATM 1720 O  O   . HOH   C 3 .   ? 2.53023   37.10806 32.30968 1.000 32.25089  ? 464 HOH   A O   1 
HETATM 1721 O  O   . HOH   C 3 .   ? 19.69372  29.43600 37.24372 1.000 44.33285  ? 465 HOH   A O   1 
HETATM 1722 O  O   . HOH   C 3 .   ? -1.63777  33.33754 24.88889 1.000 41.24009  ? 466 HOH   A O   1 
HETATM 1723 O  O   . HOH   C 3 .   ? 6.14317   40.90872 46.62326 1.000 57.56207  ? 467 HOH   A O   1 
HETATM 1724 O  O   . HOH   C 3 .   ? 0.30749   37.47090 25.03819 1.000 33.73635  ? 468 HOH   A O   1 
HETATM 1725 O  O   . HOH   C 3 .   ? 10.60524  41.18577 28.06238 1.000 37.12623  ? 469 HOH   A O   1 
HETATM 1726 O  O   . HOH   C 3 .   ? -0.91430  34.35284 45.91898 1.000 54.38897  ? 470 HOH   A O   1 
HETATM 1727 O  O   . HOH   C 3 .   ? -8.34220  29.62606 10.29549 1.000 50.98291  ? 471 HOH   A O   1 
HETATM 1728 O  O   . HOH   C 3 .   ? 3.51505   41.08300 31.23056 1.000 46.72102  ? 472 HOH   A O   1 
HETATM 1729 O  O   . HOH   C 3 .   ? -3.30988  41.64943 32.42591 1.000 48.32780  ? 473 HOH   A O   1 
HETATM 1730 O  O   . HOH   C 3 .   ? -5.87400  45.51048 11.50052 1.000 50.04875  ? 474 HOH   A O   1 
HETATM 1731 O  O   . HOH   C 3 .   ? 14.28094  16.99694 20.71478 1.000 45.22357  ? 475 HOH   A O   1 
HETATM 1732 O  O   . HOH   C 3 .   ? -17.04241 28.86863 34.70097 1.000 38.21139  ? 476 HOH   A O   1 
HETATM 1733 O  O   . HOH   C 3 .   ? -5.84035  31.30457 49.55768 1.000 45.52336  ? 477 HOH   A O   1 
HETATM 1734 O  O   . HOH   C 3 .   ? -8.13571  28.78284 20.29941 1.000 49.05729  ? 478 HOH   A O   1 
HETATM 1735 O  O   . HOH   C 3 .   ? -12.02096 26.04679 17.11862 1.000 52.42993  ? 479 HOH   A O   1 
HETATM 1736 O  O   . HOH   C 3 .   ? -7.87832  41.17053 38.36171 1.000 42.97563  ? 480 HOH   A O   1 
HETATM 1737 O  O   . HOH   C 3 .   ? 4.30418   38.51976 31.32906 1.000 38.57236  ? 481 HOH   A O   1 
HETATM 1738 O  O   . HOH   C 3 .   ? -13.11930 32.38134 18.01844 1.000 37.30893  ? 482 HOH   A O   1 
HETATM 1739 O  O   . HOH   C 3 .   ? 15.06587  31.44868 23.33782 1.000 29.15035  ? 483 HOH   A O   1 
HETATM 1740 O  O   . HOH   C 3 .   ? 11.49415  31.24177 24.11389 1.000 35.23583  ? 484 HOH   A O   1 
HETATM 1741 O  O   . HOH   C 3 .   ? -11.01115 31.63728 17.11042 1.000 38.13429  ? 485 HOH   A O   1 
HETATM 1742 O  O   . HOH   C 3 .   ? 17.80562  44.11748 30.82435 1.000 50.25404  ? 486 HOH   A O   1 
HETATM 1743 O  O   . HOH   C 3 .   ? -9.27387  43.86405 28.48537 1.000 42.82352  ? 487 HOH   A O   1 
HETATM 1744 O  O   . HOH   C 3 .   ? -4.23710  38.78808 12.89345 1.000 41.89497  ? 488 HOH   A O   1 
HETATM 1745 O  O   . HOH   C 3 .   ? -16.80522 37.68179 22.24788 1.000 46.12968  ? 489 HOH   A O   1 
HETATM 1746 O  O   . HOH   C 3 .   ? 11.51127  34.62840 45.39468 1.000 54.03562  ? 490 HOH   A O   1 
HETATM 1747 O  O   . HOH   C 3 .   ? 11.21835  19.20457 33.79567 1.000 44.98878  ? 491 HOH   A O   1 
HETATM 1748 O  O   . HOH   C 3 .   ? 16.01808  34.59027 19.05347 1.000 52.76563  ? 492 HOH   A O   1 
HETATM 1749 O  O   . HOH   C 3 .   ? 11.81765  24.72776 8.36291  1.000 53.69183  ? 493 HOH   A O   1 
HETATM 1750 O  O   . HOH   C 3 .   ? -10.31422 34.27350 46.34856 1.000 48.52694  ? 494 HOH   A O   1 
HETATM 1751 O  O   . HOH   C 3 .   ? 9.34582   24.63855 45.50039 1.000 45.40187  ? 495 HOH   A O   1 
HETATM 1752 O  O   . HOH   C 3 .   ? 1.75509   39.45582 26.43800 1.000 41.51222  ? 496 HOH   A O   1 
HETATM 1753 O  O   . HOH   C 3 .   ? 0.58250   17.42497 24.71689 1.000 46.51179  ? 497 HOH   A O   1 
HETATM 1754 O  O   . HOH   C 3 .   ? -12.07649 27.60354 22.14740 1.000 48.28548  ? 498 HOH   A O   1 
HETATM 1755 O  O   . HOH   C 3 .   ? -2.74538  10.57852 36.50389 1.000 53.97426  ? 499 HOH   A O   1 
HETATM 1756 O  O   . HOH   C 3 .   ? 16.11418  23.27823 33.48701 1.000 45.75489  ? 500 HOH   A O   1 
HETATM 1757 O  O   . HOH   C 3 .   ? -16.25041 31.65662 36.24288 1.000 60.34797  ? 501 HOH   A O   1 
HETATM 1758 O  O   . HOH   C 3 .   ? -15.02980 35.50390 34.27753 1.000 32.86937  ? 502 HOH   A O   1 
HETATM 1759 O  O   . HOH   C 3 .   ? -15.06657 41.18728 25.71033 1.000 50.51500  ? 503 HOH   A O   1 
HETATM 1760 O  O   . HOH   C 3 .   ? -14.23695 36.74409 37.06402 1.000 48.14771  ? 504 HOH   A O   1 
HETATM 1761 O  O   . HOH   C 3 .   ? -16.27696 39.59437 30.12823 1.000 47.85747  ? 505 HOH   A O   1 
HETATM 1762 O  O   . HOH   C 3 .   ? -2.10898  43.95427 23.93306 1.000 45.66246  ? 506 HOH   A O   1 
HETATM 1763 O  O   . HOH   C 3 .   ? 2.46507   17.91418 17.50330 1.000 53.96518  ? 507 HOH   A O   1 
HETATM 1764 O  O   . HOH   C 3 .   ? 20.56480  21.49828 25.52623 1.000 53.73824  ? 508 HOH   A O   1 
HETATM 1765 O  O   . HOH   C 3 .   ? 21.20202  23.27318 25.11973 1.000 54.87900  ? 509 HOH   A O   1 
HETATM 1766 O  O   . HOH   C 3 .   ? 7.24895   44.13937 29.93022 1.000 50.32746  ? 510 HOH   A O   1 
HETATM 1767 O  O   . HOH   C 3 .   ? 19.33894  24.50748 31.11480 1.000 40.13090  ? 511 HOH   A O   1 
HETATM 1768 O  O   . HOH   C 3 .   ? -13.54317 30.90955 36.70112 1.000 44.59729  ? 512 HOH   A O   1 
HETATM 1769 O  O   . HOH   C 3 .   ? -2.43314  17.98156 46.50458 1.000 48.30923  ? 513 HOH   A O   1 
HETATM 1770 O  O   . HOH   C 3 .   ? -11.90944 45.37627 31.61103 1.000 48.86960  ? 514 HOH   A O   1 
HETATM 1771 O  O   . HOH   C 3 .   ? 8.55417   31.97751 9.45931  1.000 44.82201  ? 515 HOH   A O   1 
HETATM 1772 O  O   . HOH   C 3 .   ? -8.91893  33.81618 48.79729 1.000 53.41021  ? 516 HOH   A O   1 
HETATM 1773 O  O   . HOH   C 3 .   ? 1.92398   17.96544 19.76580 1.000 54.92619  ? 517 HOH   A O   1 
HETATM 1774 O  O   . HOH   C 3 .   ? -8.216    47.262   26.903   1.000 47.61445  ? 518 HOH   A O   1 
HETATM 1775 O  O   . HOH   C 3 .   ? -12.93150 18.25870 30.44148 1.000 43.60300  ? 519 HOH   A O   1 
HETATM 1776 O  O   . HOH   C 3 .   ? -14.82207 43.26666 35.83411 1.000 42.95874  ? 520 HOH   A O   1 
HETATM 1777 O  O   . HOH   C 3 .   ? -15.86407 42.74704 32.37524 1.000 53.25249  ? 521 HOH   A O   1 
HETATM 1778 O  O   . HOH   C 3 .   ? -11.00204 36.24571 47.06490 1.000 51.32146  ? 522 HOH   A O   1 
HETATM 1779 O  O   . HOH   C 3 .   ? -18.50695 36.96728 31.55927 1.000 39.76078  ? 523 HOH   A O   1 
HETATM 1780 O  O   . HOH   C 3 .   ? -18.98901 31.54947 35.36375 1.000 51.55374  ? 524 HOH   A O   1 
HETATM 1781 O  O   . HOH   C 3 .   ? -11.32953 17.83493 27.95148 1.000 49.01473  ? 525 HOH   A O   1 
HETATM 1782 O  O   . HOH   C 3 .   ? 12.16592  15.41788 19.89500 1.000 51.28636  ? 526 HOH   A O   1 
HETATM 1783 O  O   . HOH   C 3 .   ? 13.899    11.492   10.588   1.000 56.35209  ? 527 HOH   A O   1 
HETATM 1784 O  O   . HOH   C 3 .   ? -15.09027 35.67076 39.86498 1.000 52.05561  ? 528 HOH   A O   1 
HETATM 1785 O  O   . HOH   C 3 .   ? -17.12941 39.66952 34.99504 1.000 60.42295  ? 529 HOH   A O   1 
HETATM 1786 O  O   . HOH   C 3 .   ? -17.40678 37.29860 33.88078 1.000 59.53081  ? 530 HOH   A O   1 
HETATM 1787 O  O   . HOH   C 3 .   ? -20.54076 37.91551 30.38357 1.000 56.40714  ? 531 HOH   A O   1 
HETATM 1788 O  O   . HOH   C 3 .   ? -18.73118 33.56203 38.11031 1.000 61.32451  ? 532 HOH   A O   1 
HETATM 1789 O  O   . HOH   C 3 .   ? -19.87009 35.87988 38.88738 1.000 59.28542  ? 533 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   ? 0.95137 1.01312 0.82886 0.03682  -0.06083 -0.43840 16  GLU A N   
2    C CA  . GLU A 9   ? 0.85727 0.89151 0.72088 0.08027  -0.05460 -0.40963 16  GLU A CA  
3    C C   . GLU A 9   ? 0.81891 0.85873 0.71361 0.09206  -0.05752 -0.36552 16  GLU A C   
4    O O   . GLU A 9   ? 0.83222 0.93336 0.73672 0.10377  -0.07306 -0.35158 16  GLU A O   
5    C CB  . GLU A 9   ? 0.99821 1.08398 0.83280 0.11372  -0.06411 -0.40638 16  GLU A CB  
6    C CG  . GLU A 9   ? 1.11224 1.16395 0.92734 0.15342  -0.05020 -0.37627 16  GLU A CG  
7    C CD  . GLU A 9   ? 1.28366 1.25763 1.08168 0.15308  -0.02720 -0.38395 16  GLU A CD  
8    O OE1 . GLU A 9   ? 1.24044 1.16262 1.04227 0.12220  -0.01646 -0.40278 16  GLU A OE1 
9    O OE2 . GLU A 9   ? 1.45863 1.42136 1.23740 0.18521  -0.01635 -0.36570 16  GLU A OE2 
10   N N   . VAL A 10  ? 0.72516 0.70035 0.63166 0.09155  -0.04101 -0.34220 17  VAL A N   
11   C CA  . VAL A 10  ? 0.63056 0.60497 0.56664 0.09550  -0.04198 -0.30456 17  VAL A CA  
12   C C   . VAL A 10  ? 0.62270 0.58660 0.55473 0.12834  -0.03425 -0.26828 17  VAL A C   
13   O O   . VAL A 10  ? 0.63502 0.55876 0.55274 0.14155  -0.01928 -0.26559 17  VAL A O   
14   C CB  . VAL A 10  ? 0.64197 0.56151 0.59455 0.07036  -0.02936 -0.30495 17  VAL A CB  
15   C CG1 . VAL A 10  ? 0.59617 0.53471 0.57937 0.06644  -0.03616 -0.27737 17  VAL A CG1 
16   C CG2 . VAL A 10  ? 0.69150 0.60173 0.63922 0.03289  -0.02682 -0.34908 17  VAL A CG2 
17   N N   . GLU A 11  ? 0.56314 0.56268 0.50706 0.14078  -0.04188 -0.24131 18  GLU A N   
18   C CA  . GLU A 11  ? 0.62886 0.62232 0.57517 0.16236  -0.03246 -0.20814 18  GLU A CA  
19   C C   . GLU A 11  ? 0.50622 0.48457 0.48158 0.15231  -0.02994 -0.18528 18  GLU A C   
20   O O   . GLU A 11  ? 0.48456 0.47446 0.47568 0.13712  -0.03883 -0.18464 18  GLU A O   
21   C CB  . GLU A 11  ? 0.53023 0.56243 0.46270 0.18186  -0.03630 -0.19376 18  GLU A CB  
22   C CG  . GLU A 11  ? 0.61165 0.66598 0.51000 0.19835  -0.03877 -0.21313 18  GLU A CG  
23   C CD  . GLU A 11  ? 0.68668 0.77125 0.56401 0.22423  -0.03730 -0.19255 18  GLU A CD  
24   O OE1 . GLU A 11  ? 0.71862 0.82765 0.59895 0.22631  -0.04556 -0.18370 18  GLU A OE1 
25   O OE2 . GLU A 11  ? 0.80660 0.88742 0.66147 0.24469  -0.02505 -0.18388 18  GLU A OE2 
26   N N   . THR A 12  ? 0.50307 0.46271 0.48489 0.16260  -0.01799 -0.16734 19  THR A N   
27   C CA  . THR A 12  ? 0.47499 0.42834 0.48162 0.15597  -0.01607 -0.14702 19  THR A CA  
28   C C   . THR A 12  ? 0.44795 0.42785 0.46412 0.16372  -0.01217 -0.12340 19  THR A C   
29   O O   . THR A 12  ? 0.47397 0.46345 0.48234 0.17897  -0.00241 -0.11733 19  THR A O   
30   C CB  . THR A 12  ? 0.49952 0.41811 0.50639 0.16263  -0.00468 -0.14552 19  THR A CB  
31   O OG1 . THR A 12  ? 0.53824 0.41866 0.53153 0.15038  -0.00228 -0.16958 19  THR A OG1 
32   C CG2 . THR A 12  ? 0.47316 0.39536 0.50284 0.15925  -0.00471 -0.12437 19  THR A CG2 
33   N N   . PHE A 13  ? 0.43358 0.42369 0.46543 0.15103  -0.01728 -0.11185 20  PHE A N   
34   C CA  . PHE A 13  ? 0.41964 0.42768 0.45892 0.14974  -0.01085 -0.09375 20  PHE A CA  
35   C C   . PHE A 13  ? 0.39952 0.41353 0.46301 0.13783  -0.01167 -0.08334 20  PHE A C   
36   O O   . PHE A 13  ? 0.41144 0.41371 0.48253 0.13013  -0.01923 -0.08668 20  PHE A O   
37   C CB  . PHE A 13  ? 0.39975 0.41055 0.42620 0.14736  -0.01296 -0.09066 20  PHE A CB  
38   C CG  . PHE A 13  ? 0.46492 0.48085 0.46412 0.16336  -0.01481 -0.10033 20  PHE A CG  
39   C CD1 . PHE A 13  ? 0.42971 0.45202 0.42315 0.16211  -0.02837 -0.11908 20  PHE A CD1 
40   C CD2 . PHE A 13  ? 0.44414 0.46440 0.42305 0.17877  -0.00216 -0.09175 20  PHE A CD2 
41   C CE1 . PHE A 13  ? 0.45400 0.49418 0.42192 0.17736  -0.03247 -0.13093 20  PHE A CE1 
42   C CE2 . PHE A 13  ? 0.52842 0.55853 0.47766 0.19756  -0.00447 -0.09996 20  PHE A CE2 
43   C CZ  . PHE A 13  ? 0.50710 0.55086 0.45074 0.19763  -0.02126 -0.12055 20  PHE A CZ  
44   N N   . ALA A 14  ? 0.47252 0.50921 0.54749 0.13503  -0.00286 -0.07187 21  ALA A N   
45   C CA  . ALA A 14  ? 0.41847 0.47370 0.51515 0.12147  -0.00488 -0.06468 21  ALA A CA  
46   C C   . ALA A 14  ? 0.42341 0.47087 0.51763 0.10238  -0.00450 -0.06260 21  ALA A C   
47   O O   . ALA A 14  ? 0.35927 0.39725 0.43877 0.10044  0.00568  -0.05990 21  ALA A O   
48   C CB  . ALA A 14  ? 0.35293 0.44930 0.46665 0.12395  0.00434  -0.05786 21  ALA A CB  
49   N N   . PHE A 15  ? 0.37569 0.42134 0.47906 0.09142  -0.01300 -0.06279 22  PHE A N   
50   C CA  . PHE A 15  ? 0.37563 0.41287 0.47571 0.07361  -0.01010 -0.06148 22  PHE A CA  
51   C C   . PHE A 15  ? 0.46987 0.52644 0.57682 0.05721  0.00378  -0.05935 22  PHE A C   
52   O O   . PHE A 15  ? 0.44495 0.53953 0.56986 0.05717  0.00584  -0.05879 22  PHE A O   
53   C CB  . PHE A 15  ? 0.42493 0.46432 0.53463 0.06524  -0.02058 -0.06249 22  PHE A CB  
54   C CG  . PHE A 15  ? 0.39109 0.40706 0.49238 0.07088  -0.02882 -0.06570 22  PHE A CG  
55   C CD1 . PHE A 15  ? 0.36432 0.36224 0.44970 0.07162  -0.02654 -0.06677 22  PHE A CD1 
56   C CD2 . PHE A 15  ? 0.33739 0.35083 0.44538 0.07636  -0.03616 -0.06718 22  PHE A CD2 
57   C CE1 . PHE A 15  ? 0.38003 0.37219 0.46265 0.07607  -0.03458 -0.07149 22  PHE A CE1 
58   C CE2 . PHE A 15  ? 0.36909 0.36677 0.47312 0.07531  -0.04122 -0.07283 22  PHE A CE2 
59   C CZ  . PHE A 15  ? 0.33192 0.32622 0.42647 0.07429  -0.04201 -0.07612 22  PHE A CZ  
60   N N   . GLN A 16  ? 0.52634 0.55689 0.61778 0.04307  0.01586  -0.05873 23  GLN A N   
61   C CA  . GLN A 16  ? 0.51482 0.55788 0.61301 0.01660  0.03197  -0.06134 23  GLN A CA  
62   C C   . GLN A 16  ? 0.51910 0.60144 0.64109 -0.00144 0.02120  -0.06928 23  GLN A C   
63   O O   . GLN A 16  ? 0.47878 0.55625 0.60089 0.00375  0.00650  -0.07022 23  GLN A O   
64   C CB  . GLN A 16  ? 0.53990 0.53000 0.60813 0.00584  0.05184  -0.05914 23  GLN A CB  
65   C CG  . GLN A 16  ? 0.67956 0.65196 0.73112 0.00594  0.07655  -0.05214 23  GLN A CG  
66   C CD  . GLN A 16  ? 0.74948 0.65695 0.75817 0.01630  0.09546  -0.04268 23  GLN A CD  
67   O OE1 . GLN A 16  ? 0.84600 0.72983 0.83945 0.03092  0.08594  -0.04099 23  GLN A OE1 
68   N NE2 . GLN A 16  ? 0.89132 0.77030 0.87811 0.01172  0.12480  -0.03470 23  GLN A NE2 
69   N N   . ALA A 17  ? 0.46208 0.59077 0.60445 -0.02240 0.02917  -0.07546 24  ALA A N   
70   C CA  . ALA A 17  ? 0.45141 0.63870 0.61817 -0.03479 0.01656  -0.08384 24  ALA A CA  
71   C C   . ALA A 17  ? 0.48395 0.64701 0.63881 -0.05042 0.01109  -0.09145 24  ALA A C   
72   O O   . ALA A 17  ? 0.47354 0.66235 0.63590 -0.04094 -0.00649 -0.09129 24  ALA A O   
73   C CB  . ALA A 17  ? 0.35593 0.60383 0.54641 -0.06288 0.02891  -0.09417 24  ALA A CB  
74   N N   . GLU A 18  ? 0.40395 0.51278 0.53550 -0.07113 0.02870  -0.09669 25  GLU A N   
75   C CA  . GLU A 18  ? 0.49234 0.57520 0.60894 -0.08587 0.02691  -0.10562 25  GLU A CA  
76   C C   . GLU A 18  ? 0.50486 0.56027 0.61019 -0.05626 0.01106  -0.09510 25  GLU A C   
77   O O   . GLU A 18  ? 0.43646 0.50278 0.54237 -0.05811 -0.00073 -0.09938 25  GLU A O   
78   C CB  . GLU A 18  ? 0.57574 0.59367 0.66253 -0.11001 0.05510  -0.11194 25  GLU A CB  
79   C CG  . GLU A 18  ? 0.70836 0.74759 0.80539 -0.14944 0.07662  -0.12598 25  GLU A CG  
80   C CD  . GLU A 18  ? 0.79264 0.82430 0.88989 -0.13977 0.09268  -0.11348 25  GLU A CD  
81   O OE1 . GLU A 18  ? 0.71068 0.76185 0.81731 -0.10438 0.07718  -0.09893 25  GLU A OE1 
82   O OE2 . GLU A 18  ? 0.85206 0.85528 0.93754 -0.16886 0.12324  -0.11913 25  GLU A OE2 
83   N N   . ILE A 19  ? 0.42667 0.45175 0.52179 -0.03024 0.01128  -0.08280 26  ILE A N   
84   C CA  . ILE A 19  ? 0.48155 0.48798 0.56965 -0.00739 -0.00184 -0.07618 26  ILE A CA  
85   C C   . ILE A 19  ? 0.46997 0.51521 0.57901 0.00392  -0.02021 -0.07366 26  ILE A C   
86   O O   . ILE A 19  ? 0.45100 0.49267 0.55838 0.00830  -0.02926 -0.07258 26  ILE A O   
87   C CB  . ILE A 19  ? 0.43255 0.40993 0.50550 0.01497  0.00237  -0.06800 26  ILE A CB  
88   C CG1 . ILE A 19  ? 0.43784 0.37009 0.48147 0.01084  0.02477  -0.06561 26  ILE A CG1 
89   C CG2 . ILE A 19  ? 0.36775 0.33973 0.43944 0.03297  -0.01131 -0.06563 26  ILE A CG2 
90   C CD1 . ILE A 19  ? 0.56194 0.46789 0.58215 0.03954  0.02708  -0.05647 26  ILE A CD1 
91   N N   . ALA A 20  ? 0.36766 0.44700 0.49318 0.01157  -0.02284 -0.07098 27  ALA A N   
92   C CA  . ALA A 20  ? 0.45039 0.55884 0.58863 0.02792  -0.03520 -0.06551 27  ALA A CA  
93   C C   . ALA A 20  ? 0.44277 0.58688 0.58712 0.01758  -0.04224 -0.06891 27  ALA A C   
94   O O   . ALA A 20  ? 0.34358 0.49091 0.48592 0.03144  -0.05071 -0.06219 27  ALA A O   
95   C CB  . ALA A 20  ? 0.32623 0.46540 0.47710 0.04217  -0.03319 -0.06142 27  ALA A CB  
96   N N   . GLN A 21  ? 0.37911 0.54960 0.52833 -0.00827 -0.03689 -0.08054 28  GLN A N   
97   C CA  . GLN A 21  ? 0.46485 0.67605 0.61744 -0.02256 -0.04418 -0.08947 28  GLN A CA  
98   C C   . GLN A 21  ? 0.46225 0.63282 0.59493 -0.02442 -0.04677 -0.09022 28  GLN A C   
99   O O   . GLN A 21  ? 0.44042 0.63748 0.57119 -0.01883 -0.05693 -0.08926 28  GLN A O   
100  C CB  . GLN A 21  ? 0.50297 0.74325 0.66304 -0.05877 -0.03394 -0.10801 28  GLN A CB  
101  C CG  . GLN A 21  ? 0.64883 0.97545 0.82693 -0.07037 -0.04423 -0.11972 28  GLN A CG  
102  C CD  . GLN A 21  ? 0.73313 1.09011 0.92193 -0.11440 -0.03078 -0.14281 28  GLN A CD  
103  O OE1 . GLN A 21  ? 0.69080 1.05540 0.87189 -0.14665 -0.02839 -0.16379 28  GLN A OE1 
104  N NE2 . GLN A 21  ? 0.51494 0.88553 0.71948 -0.11856 -0.01904 -0.14072 28  GLN A NE2 
105  N N   . LEU A 22  ? 0.45576 0.56594 0.57133 -0.02893 -0.03655 -0.09080 29  LEU A N   
106  C CA  . LEU A 22  ? 0.46544 0.54091 0.56265 -0.02779 -0.03699 -0.09107 29  LEU A CA  
107  C C   . LEU A 22  ? 0.40247 0.47439 0.50267 -0.00316 -0.04691 -0.07742 29  LEU A C   
108  O O   . LEU A 22  ? 0.38424 0.45745 0.47713 -0.00052 -0.05138 -0.07580 29  LEU A O   
109  C CB  . LEU A 22  ? 0.43303 0.45068 0.50940 -0.03139 -0.02177 -0.09267 29  LEU A CB  
110  C CG  . LEU A 22  ? 0.54910 0.53309 0.60637 -0.02384 -0.02022 -0.09117 29  LEU A CG  
111  C CD1 . LEU A 22  ? 0.41845 0.41300 0.46601 -0.04136 -0.02087 -0.10334 29  LEU A CD1 
112  C CD2 . LEU A 22  ? 0.53922 0.47116 0.57295 -0.01777 -0.00366 -0.08912 29  LEU A CD2 
113  N N   . MET A 23  ? 0.33468 0.39968 0.44337 0.01302  -0.04792 -0.06885 30  MET A N   
114  C CA  . MET A 23  ? 0.43570 0.48813 0.54538 0.03001  -0.05223 -0.05929 30  MET A CA  
115  C C   . MET A 23  ? 0.39364 0.47425 0.50583 0.04058  -0.05792 -0.05105 30  MET A C   
116  O O   . MET A 23  ? 0.44723 0.51556 0.55223 0.04733  -0.05801 -0.04397 30  MET A O   
117  C CB  . MET A 23  ? 0.41415 0.45151 0.52888 0.04117  -0.05020 -0.05704 30  MET A CB  
118  C CG  . MET A 23  ? 0.42086 0.43361 0.52788 0.03865  -0.04572 -0.06232 30  MET A CG  
119  S SD  . MET A 23  ? 0.46274 0.46810 0.57136 0.05054  -0.04434 -0.06406 30  MET A SD  
120  C CE  . MET A 23  ? 0.43311 0.42785 0.54693 0.05653  -0.04763 -0.06405 30  MET A CE  
121  N N   . SER A 24  ? 0.35932 0.48210 0.48031 0.04409  -0.06115 -0.05079 31  SER A N   
122  C CA  . SER A 24  ? 0.37853 0.53843 0.49806 0.06159  -0.06669 -0.04080 31  SER A CA  
123  C C   . SER A 24  ? 0.42230 0.60112 0.53127 0.05178  -0.07179 -0.04543 31  SER A C   
124  O O   . SER A 24  ? 0.43919 0.62238 0.53632 0.06935  -0.07340 -0.03311 31  SER A O   
125  C CB  . SER A 24  ? 0.30926 0.52672 0.44325 0.06889  -0.06983 -0.04141 31  SER A CB  
126  O OG  . SER A 24  ? 0.54135 0.81424 0.67267 0.08497  -0.07743 -0.03475 31  SER A OG  
127  N N   . LEU A 25  ? 0.40433 0.58889 0.51267 0.02441  -0.07152 -0.06315 32  LEU A N   
128  C CA  . LEU A 25  ? 0.35899 0.55417 0.45256 0.01310  -0.07466 -0.07157 32  LEU A CA  
129  C C   . LEU A 25  ? 0.42413 0.57023 0.50279 0.02102  -0.07000 -0.06270 32  LEU A C   
130  O O   . LEU A 25  ? 0.47005 0.62715 0.53497 0.02847  -0.07271 -0.05799 32  LEU A O   
131  C CB  . LEU A 25  ? 0.39876 0.59388 0.48964 -0.02061 -0.06953 -0.09495 32  LEU A CB  
132  C CG  . LEU A 25  ? 0.54312 0.74691 0.61505 -0.03886 -0.07040 -0.11141 32  LEU A CG  
133  C CD1 . LEU A 25  ? 0.49534 0.73151 0.57151 -0.07418 -0.06704 -0.13771 32  LEU A CD1 
134  C CD2 . LEU A 25  ? 0.55514 0.69160 0.60586 -0.04065 -0.05983 -0.11147 32  LEU A CD2 
135  N N   . ILE A 26  ? 0.45844 0.55744 0.53964 0.02031  -0.06264 -0.06062 33  ILE A N   
136  C CA  . ILE A 26  ? 0.33792 0.40282 0.41074 0.02563  -0.05759 -0.05437 33  ILE A CA  
137  C C   . ILE A 26  ? 0.45288 0.51512 0.52610 0.04390  -0.05650 -0.03733 33  ILE A C   
138  O O   . ILE A 26  ? 0.51847 0.56946 0.58181 0.04733  -0.05195 -0.03075 33  ILE A O   
139  C CB  . ILE A 26  ? 0.42003 0.45133 0.49711 0.02240  -0.05146 -0.05810 33  ILE A CB  
140  C CG1 . ILE A 26  ? 0.46659 0.48227 0.53005 0.00915  -0.04530 -0.07069 33  ILE A CG1 
141  C CG2 . ILE A 26  ? 0.32115 0.33405 0.40017 0.02965  -0.04745 -0.05120 33  ILE A CG2 
142  C CD1 . ILE A 26  ? 0.44447 0.43310 0.50703 0.01274  -0.03839 -0.07162 33  ILE A CD1 
143  N N   . ILE A 27  ? 0.47639 0.54406 0.55754 0.05671  -0.05706 -0.02921 34  ILE A N   
144  C CA  . ILE A 27  ? 0.44490 0.49392 0.51926 0.07525  -0.04967 -0.01207 34  ILE A CA  
145  C C   . ILE A 27  ? 0.45691 0.53609 0.51488 0.09360  -0.05186 0.00091  34  ILE A C   
146  O O   . ILE A 27  ? 0.57108 0.62885 0.61315 0.10548  -0.04224 0.01584  34  ILE A O   
147  C CB  . ILE A 27  ? 0.53323 0.56630 0.61533 0.08563  -0.04561 -0.00867 34  ILE A CB  
148  C CG1 . ILE A 27  ? 0.50442 0.50660 0.59726 0.07053  -0.04221 -0.02038 34  ILE A CG1 
149  C CG2 . ILE A 27  ? 0.52910 0.53851 0.59586 0.10939  -0.03388 0.01051  34  ILE A CG2 
150  C CD1 . ILE A 27  ? 0.46948 0.47500 0.57128 0.07322  -0.04441 -0.02670 34  ILE A CD1 
151  N N   . ASN A 28  ? 0.55783 0.69141 0.61822 0.09609  -0.06327 -0.00483 35  ASN A N   
152  C CA  . ASN A 28  ? 0.58548 0.76348 0.63045 0.12099  -0.06756 0.00825  35  ASN A CA  
153  C C   . ASN A 28  ? 0.57212 0.78428 0.60294 0.11211  -0.07518 -0.00022 35  ASN A C   
154  O O   . ASN A 28  ? 0.72488 0.97509 0.73722 0.13608  -0.07858 0.01210  35  ASN A O   
155  C CB  . ASN A 28  ? 0.57408 0.81097 0.63182 0.13313  -0.07639 0.00649  35  ASN A CB  
156  C CG  . ASN A 28  ? 0.67310 0.87727 0.73939 0.14755  -0.06749 0.01563  35  ASN A CG  
157  O OD1 . ASN A 28  ? 0.66449 0.80903 0.71789 0.16164  -0.05344 0.03045  35  ASN A OD1 
158  N ND2 . ASN A 28  ? 0.63436 0.87546 0.72113 0.14141  -0.07325 0.00488  35  ASN A ND2 
159  N N   . THR A 29  ? 0.58984 0.78879 0.62406 0.08209  -0.07658 -0.02037 36  THR A N   
160  C CA  . THR A 29  ? 0.60462 0.83046 0.62139 0.07174  -0.08197 -0.03262 36  THR A CA  
161  C C   . THR A 29  ? 0.52212 0.71043 0.51856 0.08205  -0.07176 -0.01846 36  THR A C   
162  O O   . THR A 29  ? 0.45621 0.59231 0.45906 0.07644  -0.06065 -0.01390 36  THR A O   
163  C CB  . THR A 29  ? 0.64241 0.86039 0.66482 0.03678  -0.08266 -0.06063 36  THR A CB  
164  O OG1 . THR A 29  ? 0.63785 0.89743 0.67831 0.02362  -0.08941 -0.07443 36  THR A OG1 
165  C CG2 . THR A 29  ? 0.46585 0.69854 0.46436 0.02452  -0.08469 -0.07643 36  THR A CG2 
166  N N   . PHE A 30  ? 0.43773 0.65998 0.40988 0.09777  -0.07514 -0.01176 37  PHE A N   
167  C CA  . PHE A 30  ? 0.45968 0.65157 0.40946 0.10715  -0.06339 0.00181  37  PHE A CA  
168  C C   . PHE A 30  ? 0.51600 0.68636 0.46321 0.08117  -0.06076 -0.01923 37  PHE A C   
169  O O   . PHE A 30  ? 0.57908 0.77840 0.51682 0.06543  -0.06956 -0.04245 37  PHE A O   
170  C CB  . PHE A 30  ? 0.49464 0.73338 0.41358 0.13441  -0.06772 0.01471  37  PHE A CB  
171  C CG  . PHE A 30  ? 0.61657 0.82394 0.50862 0.14722  -0.05222 0.03261  37  PHE A CG  
172  C CD1 . PHE A 30  ? 0.60078 0.75682 0.48819 0.16442  -0.03176 0.06139  37  PHE A CD1 
173  C CD2 . PHE A 30  ? 0.53829 0.76475 0.40772 0.14001  -0.05510 0.01927  37  PHE A CD2 
174  C CE1 . PHE A 30  ? 0.57926 0.70693 0.44290 0.17294  -0.01356 0.07825  37  PHE A CE1 
175  C CE2 . PHE A 30  ? 0.64484 0.84555 0.48915 0.15286  -0.03888 0.03682  37  PHE A CE2 
176  C CZ  . PHE A 30  ? 0.69873 0.85163 0.54162 0.16875  -0.01763 0.06726  37  PHE A CZ  
177  N N   . TYR A 31  ? 0.46875 0.58966 0.42345 0.07652  -0.04709 -0.01273 38  TYR A N   
178  C CA  . TYR A 31  ? 0.51181 0.61064 0.46319 0.05976  -0.04177 -0.02894 38  TYR A CA  
179  C C   . TYR A 31  ? 0.53469 0.60200 0.49013 0.06520  -0.02573 -0.01364 38  TYR A C   
180  O O   . TYR A 31  ? 0.55016 0.59676 0.52813 0.06344  -0.02008 -0.00574 38  TYR A O   
181  C CB  . TYR A 31  ? 0.51600 0.59974 0.48542 0.04103  -0.04497 -0.04720 38  TYR A CB  
182  C CG  . TYR A 31  ? 0.60224 0.65775 0.56101 0.03083  -0.03637 -0.06166 38  TYR A CG  
183  C CD1 . TYR A 31  ? 0.59711 0.65661 0.52891 0.02118  -0.03619 -0.08068 38  TYR A CD1 
184  C CD2 . TYR A 31  ? 0.60267 0.62947 0.57546 0.03290  -0.02726 -0.05731 38  TYR A CD2 
185  C CE1 . TYR A 31  ? 0.62374 0.64734 0.53905 0.01675  -0.02404 -0.09254 38  TYR A CE1 
186  C CE2 . TYR A 31  ? 0.49366 0.49678 0.45291 0.03212  -0.01753 -0.06722 38  TYR A CE2 
187  C CZ  . TYR A 31  ? 0.66392 0.65943 0.59252 0.02552  -0.01437 -0.08356 38  TYR A CZ  
188  O OH  . TYR A 31  ? 0.76932 0.73129 0.67801 0.02935  -0.00053 -0.09216 38  TYR A OH  
189  N N   . SER A 32  ? 0.53116 0.59899 0.46517 0.06979  -0.01752 -0.01169 39  SER A N   
190  C CA  . SER A 32  ? 0.63443 0.68358 0.57232 0.07467  0.00026  0.00510  39  SER A CA  
191  C C   . SER A 32  ? 0.56688 0.60227 0.52397 0.06396  0.00761  -0.00475 39  SER A C   
192  O O   . SER A 32  ? 0.58571 0.61387 0.56141 0.06088  0.02042  0.00486  39  SER A O   
193  C CB  . SER A 32  ? 0.58637 0.64720 0.49116 0.08812  0.00824  0.01495  39  SER A CB  
194  O OG  . SER A 32  ? 0.60430 0.68210 0.48976 0.10568  0.00384  0.03016  39  SER A OG  
195  N N   . ASN A 33  ? 0.57258 0.60542 0.52407 0.05866  0.00169  -0.02411 40  ASN A N   
196  C CA  . ASN A 33  ? 0.56566 0.58889 0.52665 0.05828  0.00994  -0.03124 40  ASN A CA  
197  C C   . ASN A 33  ? 0.58297 0.60197 0.57463 0.05274  0.00566  -0.03329 40  ASN A C   
198  O O   . ASN A 33  ? 0.54803 0.55567 0.53862 0.05295  0.00305  -0.04451 40  ASN A O   
199  C CB  . ASN A 33  ? 0.61697 0.62638 0.54868 0.05931  0.01077  -0.04912 40  ASN A CB  
200  C CG  . ASN A 33  ? 0.56337 0.56110 0.49527 0.06910  0.02279  -0.05283 40  ASN A CG  
201  O OD1 . ASN A 33  ? 0.62851 0.64412 0.57533 0.07711  0.03222  -0.04253 40  ASN A OD1 
202  N ND2 . ASN A 33  ? 0.57549 0.54424 0.48934 0.06950  0.02495  -0.06724 40  ASN A ND2 
203  N N   . LYS A 34  ? 0.63322 0.60281 0.41741 0.05075  -0.09503 0.03649  41  LYS A N   
204  C CA  . LYS A 34  ? 0.50515 0.50629 0.35655 0.04457  -0.07934 0.03918  41  LYS A CA  
205  C C   . LYS A 34  ? 0.46393 0.44288 0.31974 0.04390  -0.05577 0.02409  41  LYS A C   
206  O O   . LYS A 34  ? 0.48660 0.48405 0.38565 0.03484  -0.05050 0.02119  41  LYS A O   
207  C CB  . LYS A 34  ? 0.52183 0.54756 0.40617 0.06161  -0.06128 0.05773  41  LYS A CB  
208  C CG  . LYS A 34  ? 0.56215 0.62108 0.45365 0.06630  -0.08349 0.07711  41  LYS A CG  
209  C CD  . LYS A 34  ? 0.55301 0.62136 0.46457 0.08957  -0.06362 0.09543  41  LYS A CD  
210  C CE  . LYS A 34  ? 0.52460 0.63291 0.44826 0.09909  -0.08480 0.11795  41  LYS A CE  
211  N NZ  . LYS A 34  ? 0.51395 0.67637 0.49422 0.09412  -0.09398 0.12630  41  LYS A NZ  
212  N N   . GLU A 35  ? 0.51971 0.46349 0.33080 0.05579  -0.04138 0.01666  42  GLU A N   
213  C CA  . GLU A 35  ? 0.54653 0.47924 0.36832 0.05897  -0.01715 0.00810  42  GLU A CA  
214  C C   . GLU A 35  ? 0.53488 0.46118 0.36756 0.04312  -0.02925 -0.00702 42  GLU A C   
215  O O   . GLU A 35  ? 0.51806 0.44764 0.37596 0.04337  -0.01215 -0.01133 42  GLU A O   
216  C CB  . GLU A 35  ? 0.57201 0.47510 0.34026 0.07940  0.00031  0.00714  42  GLU A CB  
217  C CG  . GLU A 35  ? 0.61137 0.47073 0.30943 0.08334  -0.01974 -0.00989 42  GLU A CG  
218  C CD  . GLU A 35  ? 0.80409 0.63377 0.43808 0.11349  0.00200  -0.00924 42  GLU A CD  
219  O OE1 . GLU A 35  ? 0.81263 0.65468 0.43654 0.12860  0.01838  0.00879  42  GLU A OE1 
220  O OE2 . GLU A 35  ? 0.99949 0.79243 0.59055 0.12522  0.00456  -0.02472 42  GLU A OE2 
221  N N   . ILE A 36  ? 0.51535 0.43312 0.33153 0.02726  -0.06055 -0.01243 43  ILE A N   
222  C CA  . ILE A 36  ? 0.47352 0.37933 0.29760 0.00999  -0.07321 -0.02294 43  ILE A CA  
223  C C   . ILE A 36  ? 0.47185 0.41967 0.36151 0.00091  -0.06278 -0.01588 43  ILE A C   
224  O O   . ILE A 36  ? 0.46660 0.40758 0.36685 -0.00930 -0.06482 -0.02184 43  ILE A O   
225  C CB  . ILE A 36  ? 0.56346 0.45110 0.36099 -0.01190 -0.11431 -0.02530 43  ILE A CB  
226  C CG1 . ILE A 36  ? 0.52055 0.46248 0.36161 -0.02483 -0.13189 -0.00545 43  ILE A CG1 
227  C CG2 . ILE A 36  ? 0.62116 0.44987 0.33468 0.00005  -0.12753 -0.03852 43  ILE A CG2 
228  C CD1 . ILE A 36  ? 0.52537 0.50678 0.42313 -0.04982 -0.14529 0.00615  43  ILE A CD1 
229  N N   . PHE A 37  ? 0.40453 0.39011 0.33164 0.00754  -0.05152 -0.00324 44  PHE A N   
230  C CA  . PHE A 37  ? 0.37221 0.38944 0.34781 0.00555  -0.04035 0.00106  44  PHE A CA  
231  C C   . PHE A 37  ? 0.41691 0.41791 0.39600 0.00925  -0.02211 -0.01001 44  PHE A C   
232  O O   . PHE A 37  ? 0.39894 0.41220 0.40071 0.00277  -0.02077 -0.01175 44  PHE A O   
233  C CB  . PHE A 37  ? 0.38784 0.43006 0.38714 0.01990  -0.02915 0.01303  44  PHE A CB  
234  C CG  . PHE A 37  ? 0.34820 0.36998 0.34369 0.03300  -0.00714 0.01005  44  PHE A CG  
235  C CD1 . PHE A 37  ? 0.37666 0.37991 0.34524 0.04162  -0.00177 0.01482  44  PHE A CD1 
236  C CD2 . PHE A 37  ? 0.42463 0.44551 0.44226 0.03483  0.00612  0.00468  44  PHE A CD2 
237  C CE1 . PHE A 37  ? 0.40916 0.39889 0.38214 0.04874  0.01760  0.01850  44  PHE A CE1 
238  C CE2 . PHE A 37  ? 0.28934 0.29146 0.30861 0.03973  0.02030  0.00488  44  PHE A CE2 
239  C CZ  . PHE A 37  ? 0.47667 0.46594 0.47834 0.04515  0.02672  0.01390  44  PHE A CZ  
240  N N   . LEU A 38  ? 0.43904 0.41813 0.39784 0.02065  -0.00762 -0.01396 45  LEU A N   
241  C CA  . LEU A 38  ? 0.43859 0.41272 0.40891 0.02416  0.00822  -0.01953 45  LEU A CA  
242  C C   . LEU A 38  ? 0.42054 0.37596 0.37411 0.01981  0.00130  -0.02921 45  LEU A C   
243  O O   . LEU A 38  ? 0.42549 0.38872 0.40029 0.01614  0.00461  -0.03208 45  LEU A O   
244  C CB  . LEU A 38  ? 0.34271 0.30958 0.30364 0.03711  0.02658  -0.01356 45  LEU A CB  
245  C CG  . LEU A 38  ? 0.47337 0.45032 0.46347 0.03733  0.04078  -0.01242 45  LEU A CG  
246  C CD1 . LEU A 38  ? 0.35228 0.34217 0.37767 0.02782  0.03728  -0.01288 45  LEU A CD1 
247  C CD2 . LEU A 38  ? 0.46361 0.44419 0.45301 0.04803  0.06007  0.00105  45  LEU A CD2 
248  N N   . ARG A 39  ? 0.38686 0.31087 0.29612 0.02139  -0.01033 -0.03463 46  ARG A N   
249  C CA  . ARG A 39  ? 0.44455 0.33615 0.32937 0.01710  -0.02124 -0.04427 46  ARG A CA  
250  C C   . ARG A 39  ? 0.48899 0.39867 0.40682 -0.00372 -0.03464 -0.04046 46  ARG A C   
251  O O   . ARG A 39  ? 0.49631 0.39743 0.41965 -0.00489 -0.03209 -0.04322 46  ARG A O   
252  C CB  . ARG A 39  ? 0.50918 0.35331 0.33270 0.01809  -0.04070 -0.05242 46  ARG A CB  
253  C CG  . ARG A 39  ? 0.61355 0.40667 0.40167 0.01243  -0.05717 -0.06356 46  ARG A CG  
254  C CD  . ARG A 39  ? 0.70148 0.43936 0.42571 0.00521  -0.08785 -0.07324 46  ARG A CD  
255  N NE  . ARG A 39  ? 0.75337 0.51965 0.50407 -0.02439 -0.11598 -0.06268 46  ARG A NE  
256  C CZ  . ARG A 39  ? 0.93323 0.67558 0.64309 -0.03288 -0.14435 -0.06537 46  ARG A CZ  
257  N NH1 . ARG A 39  ? 0.85007 0.52977 0.47910 -0.01270 -0.14887 -0.08166 46  ARG A NH1 
258  N NH2 . ARG A 39  ? 0.85288 0.63712 0.60175 -0.05987 -0.16911 -0.04992 46  ARG A NH2 
259  N N   . GLU A 40  ? 0.39337 0.33331 0.33510 -0.01752 -0.04693 -0.03037 47  GLU A N   
260  C CA  . GLU A 40  ? 0.40255 0.36782 0.37663 -0.03559 -0.05708 -0.02048 47  GLU A CA  
261  C C   . GLU A 40  ? 0.40853 0.40241 0.41563 -0.02721 -0.03704 -0.01846 47  GLU A C   
262  O O   . GLU A 40  ? 0.42111 0.41805 0.43862 -0.03463 -0.03827 -0.01514 47  GLU A O   
263  C CB  . GLU A 40  ? 0.42122 0.42326 0.41775 -0.04811 -0.07284 -0.00481 47  GLU A CB  
264  C CG  . GLU A 40  ? 0.46951 0.44378 0.43135 -0.06101 -0.10135 -0.00608 47  GLU A CG  
265  C CD  . GLU A 40  ? 0.70723 0.62868 0.63528 -0.08013 -0.12493 -0.01368 47  GLU A CD  
266  O OE1 . GLU A 40  ? 0.61544 0.54062 0.56514 -0.09269 -0.12514 -0.00746 47  GLU A OE1 
267  O OE2 . GLU A 40  ? 0.83660 0.70620 0.70971 -0.08099 -0.14409 -0.02589 47  GLU A OE2 
268  N N   . LEU A 41  ? 0.36270 0.37197 0.38169 -0.01239 -0.02079 -0.02004 48  LEU A N   
269  C CA  . LEU A 41  ? 0.34553 0.37131 0.38556 -0.00512 -0.00751 -0.02143 48  LEU A CA  
270  C C   . LEU A 41  ? 0.40969 0.41651 0.44238 -0.00223 -0.00214 -0.02992 48  LEU A C   
271  O O   . LEU A 41  ? 0.36048 0.37607 0.40290 -0.00284 -0.00059 -0.02976 48  LEU A O   
272  C CB  . LEU A 41  ? 0.37141 0.40409 0.41968 0.00707  0.00297  -0.02184 48  LEU A CB  
273  C CG  . LEU A 41  ? 0.36208 0.41813 0.42051 0.01164  0.00058  -0.01098 48  LEU A CG  
274  C CD1 . LEU A 41  ? 0.38709 0.43539 0.44681 0.02633  0.01086  -0.01234 48  LEU A CD1 
275  C CD2 . LEU A 41  ? 0.34795 0.43678 0.42473 0.01028  -0.00062 -0.00097 48  LEU A CD2 
276  N N   . ILE A 42  ? 0.37839 0.36286 0.39286 0.00437  0.00195  -0.03488 49  ILE A N   
277  C CA  . ILE A 42  ? 0.35751 0.33116 0.36852 0.01191  0.00855  -0.03867 49  ILE A CA  
278  C C   . ILE A 42  ? 0.39573 0.34949 0.39181 0.00654  -0.00151 -0.03958 49  ILE A C   
279  O O   . ILE A 42  ? 0.41243 0.36900 0.41648 0.00988  0.00088  -0.03899 49  ILE A O   
280  C CB  . ILE A 42  ? 0.37922 0.33879 0.37213 0.02610  0.01945  -0.03896 49  ILE A CB  
281  C CG1 . ILE A 42  ? 0.39284 0.37522 0.41084 0.02872  0.03125  -0.03229 49  ILE A CG1 
282  C CG2 . ILE A 42  ? 0.38808 0.33448 0.37029 0.03963  0.02593  -0.04023 49  ILE A CG2 
283  C CD1 . ILE A 42  ? 0.35401 0.33371 0.35997 0.04403  0.04694  -0.02513 49  ILE A CD1 
284  N N   . SER A 43  ? 0.43430 0.36471 0.40744 -0.00349 -0.01589 -0.03947 50  SER A N   
285  C CA  . SER A 43  ? 0.47316 0.37620 0.43177 -0.01440 -0.02978 -0.03756 50  SER A CA  
286  C C   . SER A 43  ? 0.41426 0.35089 0.40541 -0.02608 -0.03055 -0.02579 50  SER A C   
287  O O   . SER A 43  ? 0.39753 0.32116 0.38559 -0.02771 -0.03251 -0.02184 50  SER A O   
288  C CB  . SER A 43  ? 0.41999 0.28998 0.34924 -0.02947 -0.05185 -0.03844 50  SER A CB  
289  O OG  . SER A 43  ? 0.59579 0.44705 0.52390 -0.05088 -0.07061 -0.03023 50  SER A OG  
290  N N   . ASN A 44  ? 0.39076 0.36963 0.40915 -0.02976 -0.02691 -0.01863 51  ASN A N   
291  C CA  . ASN A 44  ? 0.36396 0.37764 0.40629 -0.03258 -0.02219 -0.00670 51  ASN A CA  
292  C C   . ASN A 44  ? 0.36713 0.38374 0.40979 -0.01802 -0.01089 -0.01362 51  ASN A C   
293  O O   . ASN A 44  ? 0.39141 0.41695 0.43679 -0.01866 -0.00981 -0.00552 51  ASN A O   
294  C CB  . ASN A 44  ? 0.29460 0.34944 0.35866 -0.03001 -0.01717 0.00154  51  ASN A CB  
295  C CG  . ASN A 44  ? 0.41103 0.48517 0.48982 -0.04855 -0.03110 0.01945  51  ASN A CG  
296  O OD1 . ASN A 44  ? 0.39204 0.44098 0.46159 -0.06826 -0.04855 0.02406  51  ASN A OD1 
297  N ND2 . ASN A 44  ? 0.35521 0.47264 0.45690 -0.04228 -0.02558 0.03111  51  ASN A ND2 
298  N N   . SER A 45  ? 0.38436 0.39640 0.42571 -0.00636 -0.00410 -0.02562 52  SER A N   
299  C CA  . SER A 45  ? 0.36774 0.38437 0.41318 0.00299  0.00018  -0.03070 52  SER A CA  
300  C C   . SER A 45  ? 0.36597 0.36427 0.40173 0.00606  -0.00253 -0.02859 52  SER A C   
301  O O   . SER A 45  ? 0.40704 0.41366 0.44492 0.01035  -0.00364 -0.02580 52  SER A O   
302  C CB  . SER A 45  ? 0.33307 0.35146 0.38715 0.00872  0.00496  -0.03812 52  SER A CB  
303  O OG  . SER A 45  ? 0.40096 0.42835 0.46003 0.00896  0.00659  -0.04036 52  SER A OG  
304  N N   . SER A 46  ? 0.42322 0.39170 0.44183 0.00709  -0.00440 -0.03009 53  SER A N   
305  C CA  . SER A 46  ? 0.38133 0.32139 0.38279 0.01580  -0.00608 -0.02839 53  SER A CA  
306  C C   . SER A 46  ? 0.42113 0.35097 0.41723 0.00457  -0.01495 -0.01773 53  SER A C   
307  O O   . SER A 46  ? 0.46416 0.38756 0.45656 0.01327  -0.01477 -0.01245 53  SER A O   
308  C CB  . SER A 46  ? 0.42438 0.32225 0.39426 0.02359  -0.00653 -0.03494 53  SER A CB  
309  O OG  . SER A 46  ? 0.49334 0.35386 0.43838 0.03890  -0.00656 -0.03454 53  SER A OG  
310  N N   . ASP A 47  ? 0.37212 0.30533 0.37145 -0.01483 -0.02271 -0.01013 54  ASP A N   
311  C CA  . ASP A 47  ? 0.39169 0.32479 0.39399 -0.02860 -0.02920 0.00736  54  ASP A CA  
312  C C   . ASP A 47  ? 0.37443 0.34603 0.39034 -0.01919 -0.01938 0.01435  54  ASP A C   
313  O O   . ASP A 47  ? 0.44373 0.40702 0.45263 -0.01735 -0.02056 0.02570  54  ASP A O   
314  C CB  . ASP A 47  ? 0.41398 0.36057 0.42965 -0.05272 -0.03888 0.02055  54  ASP A CB  
315  C CG  . ASP A 47  ? 0.60006 0.49824 0.59267 -0.06661 -0.05724 0.01423  54  ASP A CG  
316  O OD1 . ASP A 47  ? 0.57656 0.49311 0.58108 -0.08073 -0.06569 0.01781  54  ASP A OD1 
317  O OD2 . ASP A 47  ? 0.67002 0.50933 0.62796 -0.06069 -0.06428 0.00546  54  ASP A OD2 
318  N N   . ALA A 48  ? 0.37517 0.38228 0.40367 -0.01159 -0.01114 0.00734  55  ALA A N   
319  C CA  . ALA A 48  ? 0.38604 0.41991 0.41402 -0.00024 -0.00503 0.00970  55  ALA A CA  
320  C C   . ALA A 48  ? 0.32320 0.34688 0.34290 0.01208  -0.00843 0.00341  55  ALA A C   
321  O O   . ALA A 48  ? 0.35570 0.39014 0.36595 0.01926  -0.00889 0.01040  55  ALA A O   
322  C CB  . ALA A 48  ? 0.29901 0.35529 0.33149 0.00759  0.00103  -0.00096 55  ALA A CB  
323  N N   . LEU A 49  ? 0.33036 0.33881 0.35390 0.01690  -0.01022 -0.00692 56  LEU A N   
324  C CA  . LEU A 49  ? 0.34672 0.35592 0.37153 0.02998  -0.01338 -0.00726 56  LEU A CA  
325  C C   . LEU A 49  ? 0.36274 0.34539 0.37243 0.03471  -0.01571 0.00541  56  LEU A C   
326  O O   . LEU A 49  ? 0.40309 0.39380 0.40965 0.04484  -0.01946 0.01301  56  LEU A O   
327  C CB  . LEU A 49  ? 0.35839 0.36916 0.39740 0.03674  -0.01016 -0.01546 56  LEU A CB  
328  C CG  . LEU A 49  ? 0.36349 0.39758 0.42051 0.03144  -0.01065 -0.02458 56  LEU A CG  
329  C CD1 . LEU A 49  ? 0.36352 0.39702 0.43355 0.03505  -0.00269 -0.02623 56  LEU A CD1 
330  C CD2 . LEU A 49  ? 0.29342 0.35049 0.36049 0.03315  -0.02179 -0.02520 56  LEU A CD2 
331  N N   . ASP A 50  ? 0.44272 0.38804 0.43899 0.02707  -0.01654 0.00817  57  ASP A N   
332  C CA  . ASP A 50  ? 0.42588 0.33123 0.40182 0.02853  -0.02170 0.02092  57  ASP A CA  
333  C C   . ASP A 50  ? 0.43354 0.35665 0.41018 0.02157  -0.02311 0.03941  57  ASP A C   
334  O O   . ASP A 50  ? 0.43635 0.34336 0.40083 0.03136  -0.02566 0.05188  57  ASP A O   
335  C CB  . ASP A 50  ? 0.45208 0.30729 0.40874 0.01317  -0.02929 0.02026  57  ASP A CB  
336  C CG  . ASP A 50  ? 0.61730 0.44047 0.55557 0.02781  -0.02704 0.00319  57  ASP A CG  
337  O OD1 . ASP A 50  ? 0.60643 0.43957 0.54718 0.05354  -0.01752 -0.00136 57  ASP A OD1 
338  O OD2 . ASP A 50  ? 0.59869 0.38917 0.51926 0.01448  -0.03522 -0.00325 57  ASP A OD2 
339  N N   . LYS A 51  ? 0.39850 0.35612 0.38698 0.00869  -0.01941 0.04375  58  LYS A N   
340  C CA  . LYS A 51  ? 0.38511 0.36366 0.37100 0.00480  -0.01604 0.06555  58  LYS A CA  
341  C C   . LYS A 51  ? 0.37604 0.37576 0.35071 0.02530  -0.01506 0.06438  58  LYS A C   
342  O O   . LYS A 51  ? 0.43468 0.42772 0.39563 0.03072  -0.01626 0.08267  58  LYS A O   
343  C CB  . LYS A 51  ? 0.37328 0.38970 0.37415 -0.00635 -0.00824 0.07199  58  LYS A CB  
344  C CG  . LYS A 51  ? 0.43025 0.43619 0.44534 -0.03272 -0.01346 0.09017  58  LYS A CG  
345  C CD  . LYS A 51  ? 0.52874 0.58227 0.56728 -0.03994 -0.00551 0.09716  58  LYS A CD  
346  C CE  . LYS A 51  ? 0.54253 0.58202 0.59880 -0.06793 -0.01932 0.10428  58  LYS A CE  
347  N NZ  . LYS A 51  ? 0.60032 0.67349 0.67475 -0.06681 -0.01570 0.09563  58  LYS A NZ  
348  N N   . ILE A 52  ? 0.41839 0.44059 0.39684 0.03527  -0.01600 0.04428  59  ILE A N   
349  C CA  . ILE A 52  ? 0.40079 0.44015 0.36582 0.05096  -0.02257 0.04161  59  ILE A CA  
350  C C   . ILE A 52  ? 0.38765 0.41303 0.35543 0.06185  -0.03098 0.04626  59  ILE A C   
351  O O   . ILE A 52  ? 0.45222 0.48542 0.40560 0.07379  -0.03771 0.05661  59  ILE A O   
352  C CB  . ILE A 52  ? 0.38317 0.44061 0.35056 0.05364  -0.02755 0.01912  59  ILE A CB  
353  C CG1 . ILE A 52  ? 0.36785 0.43795 0.31107 0.06611  -0.04029 0.01566  59  ILE A CG1 
354  C CG2 . ILE A 52  ? 0.31898 0.37257 0.31322 0.04996  -0.03201 0.00567  59  ILE A CG2 
355  C CD1 . ILE A 52  ? 0.41059 0.48724 0.31802 0.07595  -0.03273 0.02975  59  ILE A CD1 
356  N N   . ARG A 53  ? 0.46578 0.47026 0.44795 0.06205  -0.02964 0.04066  60  ARG A N   
357  C CA  . ARG A 53  ? 0.47839 0.46954 0.46173 0.07991  -0.03326 0.04770  60  ARG A CA  
358  C C   . ARG A 53  ? 0.49442 0.45266 0.45458 0.08403  -0.03375 0.06895  60  ARG A C   
359  O O   . ARG A 53  ? 0.45672 0.41937 0.41062 0.10163  -0.03934 0.08120  60  ARG A O   
360  C CB  . ARG A 53  ? 0.42257 0.39238 0.41530 0.08520  -0.02691 0.03815  60  ARG A CB  
361  C CG  . ARG A 53  ? 0.49077 0.44223 0.47943 0.11149  -0.02560 0.04723  60  ARG A CG  
362  C CD  . ARG A 53  ? 0.55504 0.51277 0.55919 0.12545  -0.01632 0.03813  60  ARG A CD  
363  N NE  . ARG A 53  ? 0.69585 0.60689 0.67617 0.15270  -0.00882 0.04347  60  ARG A NE  
364  C CZ  . ARG A 53  ? 0.75749 0.61402 0.70779 0.15589  -0.00218 0.03329  60  ARG A CZ  
365  N NH1 . ARG A 53  ? 0.68852 0.53739 0.63527 0.13142  -0.00291 0.01978  60  ARG A NH1 
366  N NH2 . ARG A 53  ? 0.68202 0.48711 0.60011 0.18705  0.00401  0.03650  60  ARG A NH2 
367  N N   . TYR A 54  ? 0.51170 0.43735 0.46105 0.06613  -0.03011 0.07659  61  TYR A N   
368  C CA  . TYR A 54  ? 0.55704 0.44342 0.48611 0.06444  -0.03248 0.10045  61  TYR A CA  
369  C C   . TYR A 54  ? 0.50868 0.42705 0.42911 0.06702  -0.03153 0.12042  61  TYR A C   
370  O O   . TYR A 54  ? 0.54946 0.44840 0.45321 0.07852  -0.03468 0.14066  61  TYR A O   
371  C CB  . TYR A 54  ? 0.52056 0.36713 0.44590 0.03726  -0.03407 0.10638  61  TYR A CB  
372  C CG  . TYR A 54  ? 0.57727 0.38275 0.48611 0.02640  -0.03901 0.13560  61  TYR A CG  
373  C CD1 . TYR A 54  ? 0.63796 0.37296 0.52055 0.03807  -0.04671 0.14026  61  TYR A CD1 
374  C CD2 . TYR A 54  ? 0.61680 0.45253 0.53488 0.00664  -0.03459 0.16158  61  TYR A CD2 
375  C CE1 . TYR A 54  ? 0.72727 0.41540 0.59303 0.02561  -0.05342 0.16948  61  TYR A CE1 
376  C CE2 . TYR A 54  ? 0.78581 0.58665 0.69347 -0.00687 -0.03878 0.19456  61  TYR A CE2 
377  C CZ  . TYR A 54  ? 0.74215 0.46556 0.62369 0.00020  -0.04998 0.19809  61  TYR A CZ  
378  O OH  . TYR A 54  ? 0.90199 0.58281 0.77205 -0.01606 -0.05613 0.23320  61  TYR A OH  
379  N N   . GLU A 55  ? 0.51852 0.48221 0.44383 0.06051  -0.02638 0.11555  62  GLU A N   
380  C CA  . GLU A 55  ? 0.56656 0.55949 0.47204 0.06914  -0.02353 0.13237  62  GLU A CA  
381  C C   . GLU A 55  ? 0.57128 0.57759 0.46386 0.09281  -0.03555 0.12756  62  GLU A C   
382  O O   . GLU A 55  ? 0.65302 0.66321 0.52148 0.10476  -0.03761 0.14817  62  GLU A O   
383  C CB  . GLU A 55  ? 0.48920 0.52098 0.39368 0.06491  -0.01416 0.12397  62  GLU A CB  
384  C CG  . GLU A 55  ? 0.64504 0.68423 0.56083 0.04578  -0.00036 0.14623  62  GLU A CG  
385  C CD  . GLU A 55  ? 0.87036 0.95332 0.78000 0.05257  0.01345  0.14331  62  GLU A CD  
386  O OE1 . GLU A 55  ? 0.87954 0.97428 0.76544 0.07194  0.00982  0.12140  62  GLU A OE1 
387  O OE2 . GLU A 55  ? 0.89365 0.99775 0.82159 0.03918  0.02648  0.16381  62  GLU A OE2 
388  N N   . SER A 56  ? 0.53374 0.55136 0.44451 0.09888  -0.04472 0.10412  63  SER A N   
389  C CA  . SER A 56  ? 0.52361 0.56441 0.43259 0.11695  -0.06087 0.10197  63  SER A CA  
390  C C   . SER A 56  ? 0.64504 0.66640 0.55293 0.13507  -0.06464 0.12250  63  SER A C   
391  O O   . SER A 56  ? 0.66492 0.71056 0.56986 0.15201  -0.07929 0.12912  63  SER A O   
392  C CB  . SER A 56  ? 0.59027 0.65421 0.52982 0.11383  -0.06964 0.07797  63  SER A CB  
393  O OG  . SER A 56  ? 0.50134 0.55039 0.46789 0.11802  -0.06326 0.07725  63  SER A OG  
394  N N   . LEU A 57  ? 0.58907 0.56342 0.49599 0.13282  -0.05449 0.13287  64  LEU A N   
395  C CA  . LEU A 57  ? 0.61945 0.56215 0.51693 0.15478  -0.05717 0.15244  64  LEU A CA  
396  C C   . LEU A 57  ? 0.62899 0.57033 0.49732 0.16181  -0.06074 0.18038  64  LEU A C   
397  O O   . LEU A 57  ? 0.77090 0.71614 0.63259 0.18673  -0.06953 0.19543  64  LEU A O   
398  C CB  . LEU A 57  ? 0.61281 0.48817 0.50329 0.14988  -0.04891 0.15346  64  LEU A CB  
399  C CG  . LEU A 57  ? 0.66892 0.54119 0.57901 0.15257  -0.04422 0.12850  64  LEU A CG  
400  C CD1 . LEU A 57  ? 0.62550 0.42083 0.51377 0.14705  -0.03999 0.12561  64  LEU A CD1 
401  C CD2 . LEU A 57  ? 0.64996 0.55523 0.57999 0.18482  -0.04658 0.12809  64  LEU A CD2 
402  N N   . THR A 58  ? 0.65878 0.59958 0.51057 0.14260  -0.05271 0.19138  65  THR A N   
403  C CA  . THR A 58  ? 0.78297 0.72748 0.60405 0.14978  -0.05202 0.22187  65  THR A CA  
404  C C   . THR A 58  ? 0.71085 0.70908 0.51159 0.15785  -0.05720 0.21507  65  THR A C   
405  O O   . THR A 58  ? 0.73116 0.73775 0.49852 0.17119  -0.05858 0.23878  65  THR A O   
406  C CB  . THR A 58  ? 0.86260 0.77725 0.67762 0.12568  -0.03801 0.24741  65  THR A CB  
407  O OG1 . THR A 58  ? 0.81799 0.76119 0.64827 0.10422  -0.02799 0.23321  65  THR A OG1 
408  C CG2 . THR A 58  ? 0.79941 0.64267 0.62048 0.11701  -0.04027 0.25463  65  THR A CG2 
409  N N   . ASP A 59  ? 0.77534 0.80306 0.58874 0.15144  -0.06138 0.18338  66  ASP A N   
410  C CA  . ASP A 59  ? 0.63589 0.69908 0.41949 0.15933  -0.07035 0.17070  66  ASP A CA  
411  C C   . ASP A 59  ? 0.69993 0.78267 0.50770 0.15603  -0.08846 0.13716  66  ASP A C   
412  O O   . ASP A 59  ? 0.66598 0.75110 0.48733 0.14169  -0.08247 0.11472  66  ASP A O   
413  C CB  . ASP A 59  ? 0.72290 0.79441 0.48499 0.15118  -0.05024 0.17322  66  ASP A CB  
414  C CG  . ASP A 59  ? 0.87203 0.96600 0.58256 0.16822  -0.05765 0.16221  66  ASP A CG  
415  O OD1 . ASP A 59  ? 0.81676 0.91765 0.50655 0.18179  -0.08304 0.15452  66  ASP A OD1 
416  O OD2 . ASP A 59  ? 0.91667 1.02058 0.60477 0.16985  -0.03918 0.16183  66  ASP A OD2 
417  N N   . PRO A 60  ? 0.72070 0.82110 0.53806 0.16830  -0.11176 0.13671  67  PRO A N   
418  C CA  . PRO A 60  ? 0.67710 0.80192 0.52944 0.16025  -0.13030 0.11197  67  PRO A CA  
419  C C   . PRO A 60  ? 0.71085 0.84423 0.53630 0.15055  -0.14449 0.08598  67  PRO A C   
420  O O   . PRO A 60  ? 0.70675 0.84909 0.56250 0.13581  -0.15411 0.06479  67  PRO A O   
421  C CB  . PRO A 60  ? 0.64282 0.79457 0.51178 0.17713  -0.15363 0.12705  67  PRO A CB  
422  C CG  . PRO A 60  ? 0.68412 0.81136 0.53465 0.19570  -0.14011 0.15790  67  PRO A CG  
423  C CD  . PRO A 60  ? 0.67170 0.77413 0.47599 0.18941  -0.12223 0.16357  67  PRO A CD  
424  N N   . SER A 61  ? 0.67424 0.80051 0.43918 0.16047  -0.14534 0.08782  68  SER A N   
425  C CA  . SER A 61  ? 0.73203 0.85199 0.45622 0.15750  -0.15824 0.06024  68  SER A CA  
426  C C   . SER A 61  ? 0.68686 0.79223 0.42369 0.14482  -0.13565 0.04258  68  SER A C   
427  O O   . SER A 61  ? 0.68156 0.77442 0.39363 0.14132  -0.14765 0.01610  68  SER A O   
428  C CB  . SER A 61  ? 0.72442 0.83659 0.36969 0.17942  -0.15821 0.06813  68  SER A CB  
429  O OG  . SER A 61  ? 0.84775 0.95459 0.47950 0.18668  -0.11995 0.08950  68  SER A OG  
430  N N   . LYS A 62  ? 0.57767 0.67979 0.34931 0.13781  -0.10656 0.05640  69  LYS A N   
431  C CA  . LYS A 62  ? 0.60139 0.69531 0.38977 0.12567  -0.08845 0.04170  69  LYS A CA  
432  C C   . LYS A 62  ? 0.57954 0.67351 0.40686 0.10972  -0.10358 0.01787  69  LYS A C   
433  O O   . LYS A 62  ? 0.56186 0.64688 0.39764 0.10121  -0.09280 0.00329  69  LYS A O   
434  C CB  . LYS A 62  ? 0.62549 0.71531 0.44382 0.11743  -0.06144 0.06301  69  LYS A CB  
435  C CG  . LYS A 62  ? 0.69371 0.78567 0.48404 0.12718  -0.04535 0.09413  69  LYS A CG  
436  C CD  . LYS A 62  ? 0.58458 0.68062 0.38874 0.11666  -0.01892 0.10785  69  LYS A CD  
437  C CE  . LYS A 62  ? 0.70438 0.81053 0.48625 0.12370  -0.00192 0.14551  69  LYS A CE  
438  N NZ  . LYS A 62  ? 0.78141 0.91299 0.56182 0.12393  0.02345  0.15824  69  LYS A NZ  
439  N N   . LEU A 63  ? 0.53455 0.64313 0.38925 0.10617  -0.12714 0.01788  70  LEU A N   
440  C CA  . LEU A 63  ? 0.53046 0.64779 0.42724 0.08958  -0.14197 0.00222  70  LEU A CA  
441  C C   . LEU A 63  ? 0.57752 0.69451 0.45189 0.08289  -0.17835 -0.01534 70  LEU A C   
442  O O   . LEU A 63  ? 0.58619 0.71412 0.50013 0.06470  -0.19628 -0.02335 70  LEU A O   
443  C CB  . LEU A 63  ? 0.45486 0.59681 0.40806 0.08985  -0.14154 0.01897  70  LEU A CB  
444  C CG  . LEU A 63  ? 0.48219 0.60864 0.45340 0.09304  -0.11052 0.02923  70  LEU A CG  
445  C CD1 . LEU A 63  ? 0.53391 0.67732 0.55013 0.10091  -0.10821 0.04235  70  LEU A CD1 
446  C CD2 . LEU A 63  ? 0.43856 0.54809 0.41329 0.07925  -0.09479 0.01319  70  LEU A CD2 
447  N N   . ASP A 64  ? 0.58783 0.69008 0.39680 0.09643  -0.19115 -0.02010 71  ASP A N   
448  C CA  . ASP A 64  ? 0.63563 0.72159 0.40710 0.08949  -0.23091 -0.04183 71  ASP A CA  
449  C C   . ASP A 64  ? 0.67731 0.72871 0.44089 0.07590  -0.23219 -0.06854 71  ASP A C   
450  O O   . ASP A 64  ? 0.76445 0.79868 0.52145 0.05837  -0.26939 -0.08621 71  ASP A O   
451  C CB  . ASP A 64  ? 0.71045 0.77681 0.39549 0.11322  -0.23940 -0.04428 71  ASP A CB  
452  C CG  . ASP A 64  ? 0.77828 0.87566 0.46554 0.12532  -0.24924 -0.01800 71  ASP A CG  
453  O OD1 . ASP A 64  ? 0.90995 1.04333 0.66315 0.11455  -0.26125 -0.00268 71  ASP A OD1 
454  O OD2 . ASP A 64  ? 0.79660 0.88373 0.41803 0.14886  -0.24339 -0.01032 71  ASP A OD2 
455  N N   . SER A 65  ? 0.60829 0.64756 0.37309 0.08238  -0.19488 -0.06989 72  SER A N   
456  C CA  . SER A 65  ? 0.63949 0.64680 0.40048 0.07349  -0.19147 -0.09135 72  SER A CA  
457  C C   . SER A 65  ? 0.62180 0.64745 0.46052 0.04786  -0.19105 -0.08714 72  SER A C   
458  O O   . SER A 65  ? 0.62970 0.63338 0.47481 0.04123  -0.18050 -0.09860 72  SER A O   
459  C CB  . SER A 65  ? 0.64796 0.64407 0.38050 0.09418  -0.15176 -0.08991 72  SER A CB  
460  O OG  . SER A 65  ? 0.65889 0.68925 0.42768 0.09754  -0.12293 -0.06301 72  SER A OG  
461  N N   . GLY A 66  ? 0.51627 0.58312 0.41177 0.03748  -0.19994 -0.06857 73  GLY A N   
462  C CA  . GLY A 66  ? 0.50061 0.59140 0.46747 0.01867  -0.19543 -0.06015 73  GLY A CA  
463  C C   . GLY A 66  ? 0.50081 0.63108 0.51530 0.02752  -0.17448 -0.03533 73  GLY A C   
464  O O   . GLY A 66  ? 0.48399 0.60613 0.48664 0.04189  -0.14542 -0.02895 73  GLY A O   
465  N N   . LYS A 67  ? 0.49082 0.66276 0.55912 0.01959  -0.18996 -0.01955 74  LYS A N   
466  C CA  . LYS A 67  ? 0.57887 0.78453 0.68581 0.03572  -0.17090 0.00421  74  LYS A CA  
467  C C   . LYS A 67  ? 0.50204 0.71230 0.64720 0.03547  -0.14173 0.00943  74  LYS A C   
468  O O   . LYS A 67  ? 0.51288 0.72364 0.66333 0.05471  -0.11804 0.02130  74  LYS A O   
469  C CB  . LYS A 67  ? 0.50193 0.76011 0.65132 0.03469  -0.19804 0.02381  74  LYS A CB  
470  C CG  . LYS A 67  ? 0.66631 0.92884 0.78138 0.05200  -0.21367 0.03174  74  LYS A CG  
471  C CD  . LYS A 67  ? 0.82415 1.07195 0.89689 0.03731  -0.25424 0.01526  74  LYS A CD  
472  C CE  . LYS A 67  ? 0.82108 1.04822 0.82720 0.05898  -0.25725 0.01535  74  LYS A CE  
473  N NZ  . LYS A 67  ? 0.76187 0.95801 0.70430 0.05053  -0.29186 -0.00700 74  LYS A NZ  
474  N N   . GLU A 68  ? 0.35526 0.56213 0.52039 0.01553  -0.14393 0.00092  75  GLU A N   
475  C CA  . GLU A 68  ? 0.38234 0.59876 0.58270 0.01649  -0.11795 0.00882  75  GLU A CA  
476  C C   . GLU A 68  ? 0.40078 0.57375 0.56350 0.02428  -0.09149 -0.00404 75  GLU A C   
477  O O   . GLU A 68  ? 0.37245 0.51289 0.49786 0.01784  -0.09466 -0.02100 75  GLU A O   
478  C CB  . GLU A 68  ? 0.44170 0.67259 0.68012 -0.00964 -0.13140 0.00993  75  GLU A CB  
479  C CG  . GLU A 68  ? 0.54120 0.82096 0.82615 -0.02541 -0.16421 0.02662  75  GLU A CG  
480  C CD  . GLU A 68  ? 0.85605 1.10538 1.11035 -0.04999 -0.20527 0.00765  75  GLU A CD  
481  O OE1 . GLU A 68  ? 0.88810 1.15706 1.18199 -0.07926 -0.23481 0.01581  75  GLU A OE1 
482  O OE2 . GLU A 68  ? 0.74251 0.94615 0.93046 -0.03964 -0.20860 -0.01416 75  GLU A OE2 
483  N N   . LEU A 69  ? 0.39589 0.56820 0.56626 0.04002  -0.06664 0.00509  76  LEU A N   
484  C CA  . LEU A 69  ? 0.41715 0.55107 0.55732 0.04391  -0.04619 -0.00407 76  LEU A CA  
485  C C   . LEU A 69  ? 0.36615 0.50492 0.52839 0.04280  -0.03022 -0.00139 76  LEU A C   
486  O O   . LEU A 69  ? 0.36419 0.51664 0.54177 0.05978  -0.01635 0.01125  76  LEU A O   
487  C CB  . LEU A 69  ? 0.31281 0.42558 0.42833 0.06207  -0.03616 0.00250  76  LEU A CB  
488  C CG  . LEU A 69  ? 0.41558 0.52783 0.51073 0.06695  -0.04921 0.00713  76  LEU A CG  
489  C CD1 . LEU A 69  ? 0.43452 0.51820 0.50777 0.08307  -0.03895 0.01728  76  LEU A CD1 
490  C CD2 . LEU A 69  ? 0.33913 0.43840 0.40524 0.05458  -0.05622 -0.00469 76  LEU A CD2 
491  N N   . HIS A 70  ? 0.34734 0.45099 0.51885 0.07596  -0.04140 0.01232  77  HIS A N   
492  C CA  . HIS A 70  ? 0.32791 0.43621 0.49979 0.07512  -0.03095 0.00197  77  HIS A CA  
493  C C   . HIS A 70  ? 0.27647 0.35657 0.41677 0.06769  -0.02695 -0.01040 77  HIS A C   
494  O O   . HIS A 70  ? 0.28531 0.34533 0.40483 0.06222  -0.03205 -0.01158 77  HIS A O   
495  C CB  . HIS A 70  ? 0.30892 0.44891 0.49218 0.06343  -0.03557 0.00977  77  HIS A CB  
496  C CG  . HIS A 70  ? 0.36824 0.50399 0.52972 0.04326  -0.04817 0.01210  77  HIS A CG  
497  N ND1 . HIS A 70  ? 0.43247 0.59284 0.60295 0.03390  -0.06225 0.02418  77  HIS A ND1 
498  C CD2 . HIS A 70  ? 0.37960 0.48907 0.51078 0.03087  -0.04860 0.00264  77  HIS A CD2 
499  C CE1 . HIS A 70  ? 0.37031 0.51785 0.51354 0.01515  -0.07060 0.01900  77  HIS A CE1 
500  N NE2 . HIS A 70  ? 0.41696 0.53170 0.53747 0.01426  -0.06157 0.00580  77  HIS A NE2 
501  N N   . ILE A 71  ? 0.32859 0.41116 0.46660 0.06813  -0.01719 -0.01803 78  ILE A N   
502  C CA  . ILE A 71  ? 0.34774 0.40942 0.46076 0.06271  -0.01315 -0.02640 78  ILE A CA  
503  C C   . ILE A 71  ? 0.32392 0.39889 0.43531 0.05194  -0.01060 -0.02313 78  ILE A C   
504  O O   . ILE A 71  ? 0.33089 0.43092 0.45839 0.05515  -0.00363 -0.02108 78  ILE A O   
505  C CB  . ILE A 71  ? 0.34178 0.39337 0.45175 0.07390  -0.00408 -0.03737 78  ILE A CB  
506  C CG1 . ILE A 71  ? 0.34068 0.37677 0.45642 0.08260  -0.00666 -0.03920 78  ILE A CG1 
507  C CG2 . ILE A 71  ? 0.31687 0.35364 0.40350 0.06814  -0.00183 -0.04216 78  ILE A CG2 
508  C CD1 . ILE A 71  ? 0.33182 0.35917 0.45069 0.09262  0.00151  -0.05209 78  ILE A CD1 
509  N N   . ASN A 72  ? 0.34180 0.39976 0.43528 0.03950  -0.01501 -0.02227 79  ASN A N   
510  C CA  . ASN A 72  ? 0.34005 0.40387 0.43263 0.02721  -0.01327 -0.01701 79  ASN A CA  
511  C C   . ASN A 72  ? 0.37572 0.41915 0.45026 0.02775  -0.00774 -0.01939 79  ASN A C   
512  O O   . ASN A 72  ? 0.36829 0.38639 0.42763 0.03028  -0.00980 -0.02443 79  ASN A O   
513  C CB  . ASN A 72  ? 0.34044 0.39895 0.43061 0.01043  -0.02363 -0.01343 79  ASN A CB  
514  C CG  . ASN A 72  ? 0.35920 0.44752 0.47013 0.00701  -0.03123 -0.00695 79  ASN A CG  
515  O OD1 . ASN A 72  ? 0.29637 0.41324 0.42968 0.01658  -0.02633 -0.00226 79  ASN A OD1 
516  N ND2 . ASN A 72  ? 0.33811 0.42169 0.44194 -0.00629 -0.04313 -0.00696 79  ASN A ND2 
517  N N   . LEU A 73  ? 0.33300 0.39150 0.41052 0.02580  -0.00049 -0.01378 80  LEU A N   
518  C CA  . LEU A 73  ? 0.36333 0.40840 0.42624 0.02461  0.00332  -0.01030 80  LEU A CA  
519  C C   . LEU A 73  ? 0.34497 0.38502 0.41071 0.00905  0.00175  0.00161  80  LEU A C   
520  O O   . LEU A 73  ? 0.36856 0.43332 0.44887 0.00065  0.00369  0.00971  80  LEU A O   
521  C CB  . LEU A 73  ? 0.31081 0.37795 0.37125 0.03300  0.01247  -0.01136 80  LEU A CB  
522  C CG  . LEU A 73  ? 0.32594 0.39791 0.38811 0.04655  0.01473  -0.02535 80  LEU A CG  
523  C CD1 . LEU A 73  ? 0.26844 0.36362 0.32600 0.05271  0.02465  -0.03031 80  LEU A CD1 
524  C CD2 . LEU A 73  ? 0.25607 0.30063 0.30690 0.05120  0.00915  -0.03229 80  LEU A CD2 
525  N N   . ILE A 74  ? 0.37980 0.38762 0.43442 0.00524  -0.00120 0.00290  81  ILE A N   
526  C CA  . ILE A 74  ? 0.39250 0.38417 0.45074 -0.01049 -0.00366 0.01191  81  ILE A CA  
527  C C   . ILE A 74  ? 0.40770 0.38014 0.45883 -0.00825 0.00031  0.02237  81  ILE A C   
528  O O   . ILE A 74  ? 0.41127 0.35199 0.45367 -0.00295 -0.00105 0.01758  81  ILE A O   
529  C CB  . ILE A 74  ? 0.40392 0.36927 0.45786 -0.01873 -0.01191 0.00129  81  ILE A CB  
530  C CG1 . ILE A 74  ? 0.42213 0.41146 0.48313 -0.01918 -0.01756 -0.00545 81  ILE A CG1 
531  C CG2 . ILE A 74  ? 0.36043 0.30698 0.41971 -0.03794 -0.01501 0.00752  81  ILE A CG2 
532  C CD1 . ILE A 74  ? 0.47259 0.44277 0.52372 -0.02666 -0.02657 -0.01654 81  ILE A CD1 
533  N N   . PRO A 75  ? 0.40721 0.40064 0.46270 -0.01121 0.00577  0.03826  82  PRO A N   
534  C CA  . PRO A 75  ? 0.42513 0.40182 0.47684 -0.01078 0.00800  0.05406  82  PRO A CA  
535  C C   . PRO A 75  ? 0.53989 0.48377 0.60067 -0.02579 0.00530  0.06290  82  PRO A C   
536  O O   . PRO A 75  ? 0.51896 0.46885 0.59101 -0.04199 0.00312  0.06463  82  PRO A O   
537  C CB  . PRO A 75  ? 0.50753 0.52462 0.55927 -0.01128 0.01470  0.06905  82  PRO A CB  
538  C CG  . PRO A 75  ? 0.43428 0.48151 0.49774 -0.01895 0.01690  0.06495  82  PRO A CG  
539  C CD  . PRO A 75  ? 0.39549 0.43253 0.45953 -0.01321 0.01132  0.04352  82  PRO A CD  
540  N N   . ASN A 76  ? 0.57670 0.48570 0.63486 -0.02044 0.00546  0.06877  83  ASN A N   
541  C CA  . ASN A 76  ? 0.56872 0.43753 0.63642 -0.03290 0.00419  0.07668  83  ASN A CA  
542  C C   . ASN A 76  ? 0.52935 0.38761 0.60155 -0.02651 0.00785  0.10144  83  ASN A C   
543  O O   . ASN A 76  ? 0.55321 0.39487 0.62115 -0.00992 0.00882  0.10033  83  ASN A O   
544  C CB  . ASN A 76  ? 0.55565 0.38178 0.61733 -0.03095 0.00118  0.05408  83  ASN A CB  
545  C CG  . ASN A 76  ? 0.61798 0.39994 0.68868 -0.04743 -0.00045 0.05523  83  ASN A CG  
546  O OD1 . ASN A 76  ? 0.66441 0.42759 0.74681 -0.05073 0.00238  0.07607  83  ASN A OD1 
547  N ND2 . ASN A 76  ? 0.64685 0.41150 0.71196 -0.05893 -0.00563 0.03319  83  ASN A ND2 
548  N N   . LYS A 77  ? 0.54727 0.41810 0.63013 -0.03977 0.00978  0.12623  84  LYS A N   
549  C CA  . LYS A 77  ? 0.63197 0.49989 0.71958 -0.03457 0.01248  0.15574  84  LYS A CA  
550  C C   . LYS A 77  ? 0.71424 0.52268 0.81443 -0.03341 0.01203  0.16219  84  LYS A C   
551  O O   . LYS A 77  ? 0.75031 0.54976 0.85484 -0.02021 0.01340  0.18195  84  LYS A O   
552  C CB  . LYS A 77  ? 0.67991 0.58258 0.77469 -0.05030 0.01573  0.18290  84  LYS A CB  
553  C CG  . LYS A 77  ? 0.69508 0.65450 0.77532 -0.04162 0.01951  0.19283  84  LYS A CG  
554  C CD  . LYS A 77  ? 0.69748 0.70081 0.78207 -0.05788 0.02516  0.20782  84  LYS A CD  
555  C CE  . LYS A 77  ? 0.67672 0.73709 0.74203 -0.04852 0.03061  0.20863  84  LYS A CE  
556  N NZ  . LYS A 77  ? 0.72194 0.82426 0.78938 -0.06172 0.03833  0.23704  84  LYS A NZ  
557  N N   . GLN A 78  ? 0.74610 0.51407 0.85304 -0.04689 0.01003  0.14592  85  GLN A N   
558  C CA  . GLN A 78  ? 0.78079 0.48623 0.89994 -0.04578 0.01129  0.14814  85  GLN A CA  
559  C C   . GLN A 78  ? 0.73952 0.42040 0.85076 -0.02174 0.01375  0.12854  85  GLN A C   
560  O O   . GLN A 78  ? 0.81413 0.46252 0.93705 -0.00777 0.01754  0.14124  85  GLN A O   
561  C CB  . GLN A 78  ? 0.81944 0.48893 0.94574 -0.07047 0.00795  0.13336  85  GLN A CB  
562  C CG  . GLN A 78  ? 1.04934 0.65979 1.19617 -0.07964 0.00979  0.14934  85  GLN A CG  
563  C CD  . GLN A 78  ? 1.18873 0.81740 1.35386 -0.09296 0.01068  0.19149  85  GLN A CD  
564  O OE1 . GLN A 78  ? 1.17625 0.86148 1.33627 -0.08777 0.01203  0.21218  85  GLN A OE1 
565  N NE2 . GLN A 78  ? 0.99785 0.57734 1.18368 -0.11093 0.01043  0.20411  85  GLN A NE2 
566  N N   . ASP A 79  ? 0.69574 0.39359 0.78986 -0.01600 0.01225  0.09990  86  ASP A N   
567  C CA  . ASP A 79  ? 0.71964 0.40459 0.80619 0.00628  0.01562  0.08299  86  ASP A CA  
568  C C   . ASP A 79  ? 0.72741 0.45504 0.81073 0.02471  0.01589  0.09624  86  ASP A C   
569  O O   . ASP A 79  ? 0.57970 0.30184 0.66171 0.04356  0.01878  0.08800  86  ASP A O   
570  C CB  . ASP A 79  ? 0.70162 0.38627 0.77090 0.00269  0.01367  0.04868  86  ASP A CB  
571  C CG  . ASP A 79  ? 0.93811 0.58331 1.00641 -0.01732 0.01145  0.03133  86  ASP A CG  
572  O OD1 . ASP A 79  ? 0.88105 0.49136 0.96411 -0.02769 0.01241  0.04380  86  ASP A OD1 
573  O OD2 . ASP A 79  ? 0.92993 0.57960 0.98273 -0.02392 0.00794  0.00597  86  ASP A OD2 
574  N N   . ARG A 80  ? 0.68351 0.45520 0.76518 0.01868  0.01327  0.11532  87  ARG A N   
575  C CA  . ARG A 80  ? 0.56978 0.38653 0.64356 0.03167  0.01195  0.12323  87  ARG A CA  
576  C C   . ARG A 80  ? 0.52100 0.35034 0.58201 0.04071  0.01113  0.09539  87  ARG A C   
577  O O   . ARG A 80  ? 0.50398 0.34218 0.56435 0.05649  0.01115  0.09456  87  ARG A O   
578  C CB  . ARG A 80  ? 0.53659 0.34832 0.62200 0.04709  0.01258  0.14858  87  ARG A CB  
579  C CG  . ARG A 80  ? 0.64200 0.50638 0.72013 0.05040  0.00897  0.16935  87  ARG A CG  
580  C CD  . ARG A 80  ? 0.58440 0.45428 0.67121 0.06990  0.00693  0.18428  87  ARG A CD  
581  N NE  . ARG A 80  ? 0.74447 0.58447 0.85266 0.07476  0.00849  0.21383  87  ARG A NE  
582  C CZ  . ARG A 80  ? 0.82511 0.64470 0.95182 0.09393  0.00984  0.22328  87  ARG A CZ  
583  N NH1 . ARG A 80  ? 0.73985 0.56946 0.86609 0.10903  0.00993  0.20621  87  ARG A NH1 
584  N NH2 . ARG A 80  ? 0.70014 0.48910 0.84928 0.09841  0.01178  0.25202  87  ARG A NH2 
585  N N   . THR A 81  ? 0.48462 0.31675 0.53773 0.02979  0.00983  0.07473  88  THR A N   
586  C CA  . THR A 81  ? 0.48539 0.33070 0.52747 0.03613  0.00865  0.05165  88  THR A CA  
587  C C   . THR A 81  ? 0.51088 0.39334 0.54704 0.02773  0.00634  0.04630  88  THR A C   
588  O O   . THR A 81  ? 0.46504 0.35599 0.50570 0.01385  0.00602  0.05264  88  THR A O   
589  C CB  . THR A 81  ? 0.53660 0.34778 0.57452 0.03422  0.00938  0.02940  88  THR A CB  
590  O OG1 . THR A 81  ? 0.56884 0.37202 0.60716 0.01532  0.00635  0.02439  88  THR A OG1 
591  C CG2 . THR A 81  ? 0.57081 0.34156 0.61549 0.04456  0.01453  0.03058  88  THR A CG2 
592  N N   . LEU A 82  ? 0.46009 0.36444 0.48887 0.03656  0.00541  0.03491  89  LEU A N   
593  C CA  . LEU A 82  ? 0.43408 0.36694 0.45938 0.03267  0.00436  0.02486  89  LEU A CA  
594  C C   . LEU A 82  ? 0.41416 0.33736 0.43559 0.03629  0.00222  0.00571  89  LEU A C   
595  O O   . LEU A 82  ? 0.41919 0.33490 0.43714 0.04645  0.00253  0.00023  89  LEU A O   
596  C CB  . LEU A 82  ? 0.35122 0.31791 0.37120 0.03889  0.00537  0.02852  89  LEU A CB  
597  C CG  . LEU A 82  ? 0.39099 0.38322 0.40948 0.03806  0.00638  0.01567  89  LEU A CG  
598  C CD1 . LEU A 82  ? 0.36550 0.37183 0.39147 0.02718  0.00909  0.02148  89  LEU A CD1 
599  C CD2 . LEU A 82  ? 0.37566 0.39442 0.38551 0.04441  0.00754  0.01318  89  LEU A CD2 
600  N N   . THR A 83  ? 0.44452 0.37163 0.46794 0.02756  -0.00018 -0.00201 90  THR A N   
601  C CA  . THR A 83  ? 0.35942 0.28024 0.37839 0.02910  -0.00330 -0.01648 90  THR A CA  
602  C C   . THR A 83  ? 0.38007 0.32920 0.40390 0.03119  -0.00466 -0.02060 90  THR A C   
603  O O   . THR A 83  ? 0.36402 0.33363 0.39667 0.02538  -0.00425 -0.01592 90  THR A O   
604  C CB  . THR A 83  ? 0.36514 0.26557 0.38206 0.01674  -0.00692 -0.02193 90  THR A CB  
605  O OG1 . THR A 83  ? 0.41507 0.28278 0.42890 0.01662  -0.00394 -0.02057 90  THR A OG1 
606  C CG2 . THR A 83  ? 0.41665 0.31556 0.42518 0.01772  -0.01071 -0.03485 90  THR A CG2 
607  N N   . ILE A 84  ? 0.45698 0.40722 0.47764 0.03997  -0.00532 -0.02837 91  ILE A N   
608  C CA  . ILE A 84  ? 0.40317 0.37216 0.43088 0.04366  -0.00659 -0.03289 91  ILE A CA  
609  C C   . ILE A 84  ? 0.43688 0.39828 0.46236 0.04137  -0.01178 -0.03725 91  ILE A C   
610  O O   . ILE A 84  ? 0.37407 0.32112 0.39044 0.04486  -0.01175 -0.04102 91  ILE A O   
611  C CB  . ILE A 84  ? 0.35049 0.32587 0.37768 0.05343  -0.00400 -0.03689 91  ILE A CB  
612  C CG1 . ILE A 84  ? 0.48690 0.47490 0.51165 0.05410  -0.00005 -0.03251 91  ILE A CG1 
613  C CG2 . ILE A 84  ? 0.33065 0.31784 0.36786 0.05806  -0.00449 -0.04248 91  ILE A CG2 
614  C CD1 . ILE A 84  ? 0.47102 0.44917 0.48839 0.05640  -0.00008 -0.02692 91  ILE A CD1 
615  N N   . VAL A 85  ? 0.32634 0.30150 0.36037 0.03522  -0.01621 -0.03527 92  VAL A N   
616  C CA  . VAL A 85  ? 0.34770 0.32277 0.37874 0.03133  -0.02321 -0.03661 92  VAL A CA  
617  C C   . VAL A 85  ? 0.44500 0.43928 0.49141 0.03923  -0.02499 -0.03316 92  VAL A C   
618  O O   . VAL A 85  ? 0.38570 0.39961 0.44932 0.04181  -0.02312 -0.02979 92  VAL A O   
619  C CB  . VAL A 85  ? 0.41366 0.39194 0.44426 0.01616  -0.02977 -0.03526 92  VAL A CB  
620  C CG1 . VAL A 85  ? 0.31067 0.28789 0.32984 0.01045  -0.03796 -0.03823 92  VAL A CG1 
621  C CG2 . VAL A 85  ? 0.48527 0.44181 0.50743 0.00826  -0.02666 -0.03735 92  VAL A CG2 
622  N N   . ASP A 86  ? 0.39456 0.38349 0.43644 0.04356  -0.02762 -0.03297 93  ASP A N   
623  C CA  . ASP A 86  ? 0.34222 0.34539 0.40061 0.05023  -0.03094 -0.02640 93  ASP A CA  
624  C C   . ASP A 86  ? 0.37455 0.38159 0.42440 0.04429  -0.03976 -0.02020 93  ASP A C   
625  O O   . ASP A 86  ? 0.41690 0.41115 0.44441 0.03789  -0.04045 -0.02486 93  ASP A O   
626  C CB  . ASP A 86  ? 0.32438 0.31859 0.38926 0.06151  -0.02542 -0.02898 93  ASP A CB  
627  C CG  . ASP A 86  ? 0.47706 0.45585 0.52747 0.06112  -0.02540 -0.02922 93  ASP A CG  
628  O OD1 . ASP A 86  ? 0.49313 0.47477 0.54143 0.05961  -0.03042 -0.02141 93  ASP A OD1 
629  O OD2 . ASP A 86  ? 0.49540 0.46304 0.53777 0.06247  -0.02021 -0.03542 93  ASP A OD2 
630  N N   . THR A 87  ? 0.32915 0.35601 0.39704 0.04716  -0.04608 -0.00924 94  THR A N   
631  C CA  . THR A 87  ? 0.32116 0.35839 0.38196 0.04198  -0.05605 0.00082  94  THR A CA  
632  C C   . THR A 87  ? 0.39500 0.42768 0.46374 0.05219  -0.05514 0.01052  94  THR A C   
633  O O   . THR A 87  ? 0.34000 0.38910 0.42094 0.05436  -0.06303 0.02644  94  THR A O   
634  C CB  . THR A 87  ? 0.35167 0.41908 0.42927 0.03664  -0.06635 0.01134  94  THR A CB  
635  O OG1 . THR A 87  ? 0.30360 0.38405 0.41475 0.04971  -0.06216 0.01735  94  THR A OG1 
636  C CG2 . THR A 87  ? 0.34611 0.41623 0.41277 0.02104  -0.06917 0.00254  94  THR A CG2 
637  N N   . GLY A 88  ? 0.36141 0.37285 0.42529 0.05767  -0.04628 0.00306  95  GLY A N   
638  C CA  . GLY A 88  ? 0.34487 0.34826 0.41822 0.06487  -0.04466 0.01147  95  GLY A CA  
639  C C   . GLY A 88  ? 0.37500 0.38090 0.42871 0.05849  -0.04839 0.02077  95  GLY A C   
640  O O   . GLY A 88  ? 0.36396 0.38103 0.39700 0.04912  -0.05395 0.02096  95  GLY A O   
641  N N   . ILE A 89  ? 0.33783 0.33392 0.39733 0.06237  -0.04491 0.02798  96  ILE A N   
642  C CA  . ILE A 89  ? 0.37481 0.37752 0.41759 0.05683  -0.04681 0.04038  96  ILE A CA  
643  C C   . ILE A 89  ? 0.32134 0.32151 0.33170 0.04969  -0.04113 0.02697  96  ILE A C   
644  O O   . ILE A 89  ? 0.36503 0.37674 0.35300 0.04330  -0.04270 0.03285  96  ILE A O   
645  C CB  . ILE A 89  ? 0.37558 0.36765 0.43658 0.06127  -0.04342 0.05258  96  ILE A CB  
646  C CG1 . ILE A 89  ? 0.43665 0.44278 0.48735 0.05607  -0.04720 0.07442  96  ILE A CG1 
647  C CG2 . ILE A 89  ? 0.32383 0.29957 0.38226 0.06125  -0.03372 0.03827  96  ILE A CG2 
648  C CD1 . ILE A 89  ? 0.39034 0.38800 0.46884 0.06012  -0.04785 0.09501  96  ILE A CD1 
649  N N   . GLY A 90  ? 0.33374 0.32010 0.34078 0.05129  -0.03411 0.00940  97  GLY A N   
650  C CA  . GLY A 90  ? 0.37628 0.35679 0.35814 0.04779  -0.02714 -0.00303 97  GLY A CA  
651  C C   . GLY A 90  ? 0.41126 0.38982 0.39172 0.05046  -0.01851 0.00061  97  GLY A C   
652  O O   . GLY A 90  ? 0.41898 0.39855 0.41783 0.05270  -0.01879 0.01257  97  GLY A O   
653  N N   . MET A 91  ? 0.39223 0.36780 0.35263 0.05004  -0.01009 -0.00985 98  MET A N   
654  C CA  . MET A 91  ? 0.38319 0.36190 0.34428 0.05327  0.00004  -0.00699 98  MET A CA  
655  C C   . MET A 91  ? 0.41679 0.40477 0.34896 0.05061  0.00727  -0.01029 98  MET A C   
656  O O   . MET A 91  ? 0.50773 0.48881 0.41809 0.04857  0.00845  -0.02524 98  MET A O   
657  C CB  . MET A 91  ? 0.43870 0.40688 0.41069 0.05980  0.00685  -0.01743 98  MET A CB  
658  C CG  . MET A 91  ? 0.40641 0.36975 0.40416 0.06177  0.00197  -0.01509 98  MET A CG  
659  S SD  . MET A 91  ? 0.54319 0.49942 0.54798 0.06776  0.00651  -0.02602 98  MET A SD  
660  C CE  . MET A 91  ? 0.43916 0.38290 0.42865 0.06716  0.00459  -0.03681 98  MET A CE  
661  N N   . THR A 92  ? 0.44142 0.44466 0.37328 0.04989  0.01301  0.00276  99  THR A N   
662  C CA  . THR A 92  ? 0.44226 0.45880 0.34593 0.04857  0.02344  -0.00066 99  THR A CA  
663  C C   . THR A 92  ? 0.51333 0.52466 0.41784 0.05765  0.03879  -0.01454 99  THR A C   
664  O O   . THR A 92  ? 0.45534 0.45675 0.38379 0.06382  0.03969  -0.01701 99  THR A O   
665  C CB  . THR A 92  ? 0.50143 0.54100 0.40603 0.04387  0.02488  0.02249  99  THR A CB  
666  O OG1 . THR A 92  ? 0.44650 0.48721 0.38184 0.04688  0.02955  0.03314  99  THR A OG1 
667  C CG2 . THR A 92  ? 0.43891 0.48434 0.34684 0.03706  0.00943  0.04025  99  THR A CG2 
668  N N   . LYS A 93  ? 0.45591 0.47654 0.33381 0.05906  0.05134  -0.02329 100 LYS A N   
669  C CA  . LYS A 93  ? 0.55155 0.57084 0.43371 0.07055  0.06836  -0.03441 100 LYS A CA  
670  C C   . LYS A 93  ? 0.48701 0.52530 0.39990 0.07404  0.07401  -0.01656 100 LYS A C   
671  O O   . LYS A 93  ? 0.50166 0.53685 0.43704 0.08320  0.07968  -0.01982 100 LYS A O   
672  C CB  . LYS A 93  ? 0.57923 0.60621 0.42563 0.07218  0.08299  -0.04906 100 LYS A CB  
673  C CG  . LYS A 93  ? 0.57544 0.59573 0.42678 0.08755  0.10224  -0.06488 100 LYS A CG  
674  C CD  . LYS A 93  ? 0.63187 0.66235 0.44702 0.09022  0.11992  -0.08082 100 LYS A CD  
675  C CE  . LYS A 93  ? 0.69870 0.71665 0.52053 0.10853  0.14026  -0.09979 100 LYS A CE  
676  N NZ  . LYS A 93  ? 0.83681 0.87871 0.63485 0.11482  0.16312  -0.10836 100 LYS A NZ  
677  N N   . ALA A 94  ? 0.42487 0.48410 0.34097 0.06570  0.07151  0.00425  101 ALA A N   
678  C CA  . ALA A 94  ? 0.42166 0.49810 0.36952 0.06512  0.07519  0.02220  101 ALA A CA  
679  C C   . ALA A 94  ? 0.50736 0.56765 0.48760 0.06490  0.06320  0.02359  101 ALA A C   
680  O O   . ALA A 94  ? 0.50601 0.57579 0.51225 0.06762  0.06719  0.02758  101 ALA A O   
681  C CB  . ALA A 94  ? 0.39609 0.49319 0.34242 0.05406  0.07309  0.04668  101 ALA A CB  
682  N N   . ASP A 95  ? 0.41890 0.45831 0.39782 0.06144  0.04876  0.01997  102 ASP A N   
683  C CA  . ASP A 95  ? 0.37144 0.39614 0.37543 0.06186  0.03908  0.01726  102 ASP A CA  
684  C C   . ASP A 95  ? 0.48279 0.50211 0.49128 0.07143  0.04432  0.00305  102 ASP A C   
685  O O   . ASP A 95  ? 0.48573 0.51045 0.51788 0.07251  0.04300  0.00568  102 ASP A O   
686  C CB  . ASP A 95  ? 0.42270 0.42951 0.42263 0.05865  0.02579  0.01448  102 ASP A CB  
687  C CG  . ASP A 95  ? 0.49516 0.50642 0.49865 0.05119  0.01879  0.03241  102 ASP A CG  
688  O OD1 . ASP A 95  ? 0.55930 0.57931 0.58018 0.04643  0.02040  0.04787  102 ASP A OD1 
689  O OD2 . ASP A 95  ? 0.51905 0.52585 0.51073 0.04965  0.01102  0.03295  102 ASP A OD2 
690  N N   . LEU A 96  ? 0.49442 0.50304 0.48094 0.07767  0.04954  -0.01134 103 LEU A N   
691  C CA  . LEU A 96  ? 0.46016 0.45876 0.45227 0.08772  0.05396  -0.02251 103 LEU A CA  
692  C C   . LEU A 96  ? 0.39835 0.41639 0.40732 0.09668  0.06650  -0.01808 103 LEU A C   
693  O O   . LEU A 96  ? 0.49460 0.51240 0.52163 0.10407  0.06637  -0.01867 103 LEU A O   
694  C CB  . LEU A 96  ? 0.47432 0.45336 0.44024 0.09102  0.05793  -0.03889 103 LEU A CB  
695  C CG  . LEU A 96  ? 0.45723 0.41930 0.41103 0.08251  0.04493  -0.04387 103 LEU A CG  
696  C CD1 . LEU A 96  ? 0.44122 0.38540 0.36900 0.08264  0.04925  -0.06090 103 LEU A CD1 
697  C CD2 . LEU A 96  ? 0.37885 0.33224 0.35225 0.08303  0.03583  -0.04201 103 LEU A CD2 
698  N N   . ILE A 97  ? 0.36368 0.40256 0.36829 0.09633  0.07747  -0.01167 104 ILE A N   
699  C CA  . ILE A 97  ? 0.50314 0.56593 0.52490 0.10617  0.09220  -0.00721 104 ILE A CA  
700  C C   . ILE A 97  ? 0.49796 0.58778 0.54972 0.09791  0.08840  0.01195  104 ILE A C   
701  O O   . ILE A 97  ? 0.57479 0.68230 0.65406 0.10340  0.09084  0.01748  104 ILE A O   
702  C CB  . ILE A 97  ? 0.54791 0.62056 0.54504 0.11192  0.11043  -0.01414 104 ILE A CB  
703  C CG1 . ILE A 97  ? 0.51246 0.55524 0.48227 0.11976  0.11503  -0.03704 104 ILE A CG1 
704  C CG2 . ILE A 97  ? 0.47847 0.58312 0.49754 0.12266  0.12790  -0.00689 104 ILE A CG2 
705  C CD1 . ILE A 97  ? 0.53597 0.58511 0.47284 0.12209  0.13110  -0.04882 104 ILE A CD1 
706  N N   . ASN A 98  ? 0.46877 0.56253 0.51787 0.08398  0.08168  0.02353  105 ASN A N   
707  C CA  . ASN A 98  ? 0.56851 0.68705 0.64509 0.07380  0.08058  0.04254  105 ASN A CA  
708  C C   . ASN A 98  ? 0.47141 0.57445 0.56321 0.06032  0.06243  0.04816  105 ASN A C   
709  O O   . ASN A 98  ? 0.52043 0.63052 0.63889 0.05577  0.05572  0.05091  105 ASN A O   
710  C CB  . ASN A 98  ? 0.44195 0.58215 0.50655 0.06876  0.09209  0.05566  105 ASN A CB  
711  C CG  . ASN A 98  ? 0.67722 0.85255 0.75218 0.07749  0.11179  0.05999  105 ASN A CG  
712  O OD1 . ASN A 98  ? 0.65512 0.83734 0.70514 0.08737  0.12767  0.05111  105 ASN A OD1 
713  N ND2 . ASN A 98  ? 0.67132 0.87084 0.78385 0.07368  0.11120  0.07265  105 ASN A ND2 
714  N N   . ASN A 99  ? 0.43726 0.52048 0.51352 0.05404  0.05435  0.04939  106 ASN A N   
715  C CA  . ASN A 99  ? 0.43619 0.50622 0.53036 0.04185  0.04095  0.05765  106 ASN A CA  
716  C C   . ASN A 99  ? 0.46221 0.51567 0.56858 0.04227  0.02988  0.04411  106 ASN A C   
717  O O   . ASN A 99  ? 0.48086 0.53432 0.61087 0.03254  0.02253  0.04737  106 ASN A O   
718  C CB  . ASN A 99  ? 0.45307 0.50745 0.52996 0.03884  0.03548  0.06311  106 ASN A CB  
719  C CG  . ASN A 99  ? 0.56067 0.63531 0.61917 0.03739  0.04554  0.07700  106 ASN A CG  
720  O OD1 . ASN A 99  ? 0.46030 0.56050 0.52754 0.03447  0.05610  0.08871  106 ASN A OD1 
721  N ND2 . ASN A 99  ? 0.49381 0.56127 0.52635 0.03865  0.04226  0.07629  106 ASN A ND2 
722  N N   . LEU A 100 ? 0.44810 0.48778 0.53750 0.05191  0.02846  0.02868  107 LEU A N   
723  C CA  . LEU A 100 ? 0.51060 0.53780 0.60739 0.05210  0.01875  0.01714  107 LEU A CA  
724  C C   . LEU A 100 ? 0.45544 0.50252 0.57141 0.05200  0.01878  0.01755  107 LEU A C   
725  O O   . LEU A 100 ? 0.48727 0.53272 0.61630 0.04479  0.00895  0.01336  107 LEU A O   
726  C CB  . LEU A 100 ? 0.49669 0.50803 0.57220 0.06117  0.01824  0.00432  107 LEU A CB  
727  C CG  . LEU A 100 ? 0.48768 0.48131 0.54917 0.05960  0.01332  0.00247  107 LEU A CG  
728  C CD1 . LEU A 100 ? 0.53640 0.51841 0.58109 0.06609  0.01266  -0.00959 107 LEU A CD1 
729  C CD2 . LEU A 100 ? 0.48507 0.46744 0.56216 0.05282  0.00397  0.00365  107 LEU A CD2 
730  N N   . GLY A 101 ? 0.45823 0.52617 0.57645 0.06021  0.02976  0.02212  108 GLY A N   
731  C CA  . GLY A 101 ? 0.46505 0.55881 0.60670 0.06091  0.02943  0.02673  108 GLY A CA  
732  C C   . GLY A 101 ? 0.48015 0.59328 0.64764 0.04553  0.02531  0.03860  108 GLY A C   
733  O O   . GLY A 101 ? 0.53213 0.66210 0.72014 0.03890  0.01708  0.03985  108 GLY A O   
734  N N   . THR A 102 ? 0.44184 0.55419 0.60897 0.03807  0.03004  0.04871  109 THR A N   
735  C CA  . THR A 102 ? 0.40989 0.53571 0.60350 0.02061  0.02563  0.06181  109 THR A CA  
736  C C   . THR A 102 ? 0.42934 0.52960 0.62987 0.00724  0.00962  0.05314  109 THR A C   
737  O O   . THR A 102 ? 0.34997 0.46153 0.57388 -0.00664 0.00112  0.05425  109 THR A O   
738  C CB  . THR A 102 ? 0.35167 0.48191 0.54174 0.01609  0.03505  0.07796  109 THR A CB  
739  O OG1 . THR A 102 ? 0.53894 0.69728 0.72233 0.02808  0.05202  0.08343  109 THR A OG1 
740  C CG2 . THR A 102 ? 0.37411 0.51349 0.59417 -0.00436 0.02988  0.09400  109 THR A CG2 
741  N N   . ILE A 103 ? 0.47577 0.54286 0.65696 0.01098  0.00560  0.04335  110 ILE A N   
742  C CA  . ILE A 103 ? 0.49463 0.53544 0.68136 0.00160  -0.00678 0.03185  110 ILE A CA  
743  C C   . ILE A 103 ? 0.50428 0.55258 0.69154 0.00134  -0.01482 0.01648  110 ILE A C   
744  O O   . ILE A 103 ? 0.51608 0.56027 0.71640 -0.01239 -0.02489 0.00862  110 ILE A O   
745  C CB  . ILE A 103 ? 0.46338 0.47322 0.63170 0.00921  -0.00740 0.02597  110 ILE A CB  
746  C CG1 . ILE A 103 ? 0.51436 0.51882 0.68518 0.00622  -0.00296 0.04459  110 ILE A CG1 
747  C CG2 . ILE A 103 ? 0.47829 0.46184 0.65151 0.00394  -0.01729 0.01001  110 ILE A CG2 
748  C CD1 . ILE A 103 ? 0.53140 0.53595 0.73010 -0.01067 -0.00585 0.05824  110 ILE A CD1 
749  N N   . ALA A 104 ? 0.44025 0.49940 0.61271 0.01557  -0.01087 0.01223  111 ALA A N   
750  C CA  . ALA A 104 ? 0.42389 0.49246 0.59436 0.01634  -0.01881 0.00148  111 ALA A CA  
751  C C   . ALA A 104 ? 0.52092 0.62533 0.71461 0.00812  -0.02335 0.00947  111 ALA A C   
752  O O   . ALA A 104 ? 0.50595 0.62263 0.70045 0.00387  -0.03345 0.00221  111 ALA A O   
753  C CB  . ALA A 104 ? 0.40653 0.47357 0.55729 0.03374  -0.01320 -0.00160 111 ALA A CB  
754  N N   . LYS A 105 ? 0.51298 0.63871 0.72573 0.00526  -0.01625 0.02544  112 LYS A N   
755  C CA  . LYS A 105 ? 0.38976 0.55588 0.63039 -0.00322 -0.02034 0.03582  112 LYS A CA  
756  C C   . LYS A 105 ? 0.36684 0.53229 0.61990 -0.02604 -0.03700 0.02717  112 LYS A C   
757  O O   . LYS A 105 ? 0.49753 0.69142 0.76101 -0.03227 -0.04753 0.02608  112 LYS A O   
758  C CB  . LYS A 105 ? 0.48831 0.67657 0.74810 -0.00452 -0.00811 0.05474  112 LYS A CB  
759  C CG  . LYS A 105 ? 0.57910 0.81658 0.86458 0.00081  -0.00330 0.06893  112 LYS A CG  
760  C CD  . LYS A 105 ? 0.46513 0.72891 0.77528 -0.00828 0.00645  0.08774  112 LYS A CD  
761  C CE  . LYS A 105 ? 0.54078 0.85951 0.88202 -0.00176 0.01255  0.10295  112 LYS A CE  
762  N NZ  . LYS A 105 ? 0.43964 0.79017 0.81460 -0.02492 -0.00350 0.10986  112 LYS A NZ  
763  N N   . SER A 106 ? 0.40952 0.54228 0.66188 -0.03895 -0.04001 0.02076  113 SER A N   
764  C CA  . SER A 106 ? 0.45419 0.57938 0.71869 -0.06212 -0.05466 0.00916  113 SER A CA  
765  C C   . SER A 106 ? 0.37046 0.47564 0.61110 -0.06093 -0.06377 -0.01545 113 SER A C   
766  O O   . SER A 106 ? 0.42810 0.54541 0.67239 -0.07654 -0.07716 -0.02735 113 SER A O   
767  C CB  . SER A 106 ? 0.51046 0.60457 0.78766 -0.07562 -0.05321 0.01309  113 SER A CB  
768  O OG  . SER A 106 ? 0.60487 0.67197 0.86545 -0.05977 -0.04202 0.01752  113 SER A OG  
769  N N   . GLY A 107 ? 0.42512 0.50267 0.64082 -0.04397 -0.05676 -0.02343 114 GLY A N   
770  C CA  . GLY A 107 ? 0.44442 0.50839 0.63704 -0.04114 -0.06261 -0.04495 114 GLY A CA  
771  C C   . GLY A 107 ? 0.44076 0.54071 0.62552 -0.03744 -0.06876 -0.04430 114 GLY A C   
772  O O   . GLY A 107 ? 0.39200 0.49671 0.56516 -0.04634 -0.07911 -0.06051 114 GLY A O   
773  N N   . THR A 108 ? 0.39755 0.52367 0.58850 -0.02399 -0.06218 -0.02536 115 THR A N   
774  C CA  . THR A 108 ? 0.42453 0.58711 0.61485 -0.01906 -0.06825 -0.01896 115 THR A CA  
775  C C   . THR A 108 ? 0.39571 0.59319 0.60575 -0.03950 -0.08322 -0.01777 115 THR A C   
776  O O   . THR A 108 ? 0.46123 0.67948 0.66148 -0.04547 -0.09550 -0.02414 115 THR A O   
777  C CB  . THR A 108 ? 0.35383 0.53333 0.55287 0.00078  -0.05627 0.00104  115 THR A CB  
778  O OG1 . THR A 108 ? 0.40305 0.55204 0.57959 0.01749  -0.04546 -0.00292 115 THR A OG1 
779  C CG2 . THR A 108 ? 0.43581 0.65609 0.64377 0.00603  -0.06329 0.01268  115 THR A CG2 
780  N N   . LYS A 109 ? 0.32809 0.53569 0.56592 -0.05197 -0.08297 -0.00833 116 LYS A N   
781  C CA  . LYS A 109 ? 0.39633 0.63918 0.65711 -0.07496 -0.09829 -0.00639 116 LYS A CA  
782  C C   . LYS A 109 ? 0.43505 0.65884 0.67933 -0.09597 -0.11297 -0.03329 116 LYS A C   
783  O O   . LYS A 109 ? 0.42277 0.67853 0.66601 -0.10969 -0.12890 -0.03866 116 LYS A O   
784  C CB  . LYS A 109 ? 0.34763 0.59913 0.64161 -0.08666 -0.09363 0.00852  116 LYS A CB  
785  C CG  . LYS A 109 ? 0.60326 0.91272 0.92981 -0.08467 -0.09342 0.03315  116 LYS A CG  
786  C CD  . LYS A 109 ? 0.66059 0.98162 1.02042 -0.09899 -0.08799 0.04841  116 LYS A CD  
787  C CE  . LYS A 109 ? 0.72384 1.06184 1.09445 -0.07586 -0.06687 0.07002  116 LYS A CE  
788  N NZ  . LYS A 109 ? 0.69928 1.04808 1.09784 -0.08871 -0.05839 0.08653  116 LYS A NZ  
789  N N   . ALA A 110 ? 0.45554 0.62840 0.68699 -0.09848 -0.10773 -0.05080 117 ALA A N   
790  C CA  . ALA A 110 ? 0.49006 0.63887 0.70561 -0.11615 -0.11849 -0.08035 117 ALA A CA  
791  C C   . ALA A 110 ? 0.45320 0.61158 0.63491 -0.10760 -0.12267 -0.09456 117 ALA A C   
792  O O   . ALA A 110 ? 0.45982 0.63391 0.62976 -0.12491 -0.13701 -0.11201 117 ALA A O   
793  C CB  . ALA A 110 ? 0.45704 0.54812 0.67035 -0.11527 -0.10932 -0.09321 117 ALA A CB  
794  N N   . PHE A 111 ? 0.38325 0.53442 0.54827 -0.08256 -0.11058 -0.08669 118 PHE A N   
795  C CA  . PHE A 111 ? 0.41091 0.57213 0.54508 -0.07391 -0.11272 -0.09557 118 PHE A CA  
796  C C   . PHE A 111 ? 0.44827 0.66393 0.58417 -0.08022 -0.12677 -0.08364 118 PHE A C   
797  O O   . PHE A 111 ? 0.45940 0.69085 0.57014 -0.08637 -0.13592 -0.09629 118 PHE A O   
798  C CB  . PHE A 111 ? 0.37511 0.52066 0.49816 -0.04791 -0.09748 -0.08429 118 PHE A CB  
799  C CG  . PHE A 111 ? 0.49099 0.64564 0.58477 -0.03906 -0.09781 -0.08952 118 PHE A CG  
800  C CD1 . PHE A 111 ? 0.49510 0.64200 0.56427 -0.04881 -0.10235 -0.11538 118 PHE A CD1 
801  C CD2 . PHE A 111 ? 0.44368 0.61390 0.53476 -0.02117 -0.09246 -0.06863 118 PHE A CD2 
802  C CE1 . PHE A 111 ? 0.53575 0.69569 0.57711 -0.04141 -0.10136 -0.11795 118 PHE A CE1 
803  C CE2 . PHE A 111 ? 0.42436 0.60345 0.49044 -0.01455 -0.09261 -0.06975 118 PHE A CE2 
804  C CZ  . PHE A 111 ? 0.41904 0.59571 0.45969 -0.02495 -0.09697 -0.09325 118 PHE A CZ  
805  N N   . MET A 112 ? 0.43557 0.68385 0.60149 -0.07843 -0.12840 -0.05825 119 MET A N   
806  C CA  . MET A 112 ? 0.47386 0.77880 0.64840 -0.08281 -0.14250 -0.04237 119 MET A CA  
807  C C   . MET A 112 ? 0.47427 0.80295 0.65159 -0.11367 -0.16275 -0.05737 119 MET A C   
808  O O   . MET A 112 ? 0.58588 0.95333 0.74963 -0.12186 -0.17800 -0.05760 119 MET A O   
809  C CB  . MET A 112 ? 0.42429 0.75806 0.63453 -0.06962 -0.13615 -0.01137 119 MET A CB  
810  C CG  . MET A 112 ? 0.59908 0.94240 0.80374 -0.04248 -0.12751 0.00776  119 MET A CG  
811  S SD  . MET A 112 ? 0.72213 1.06666 0.95881 -0.01930 -0.10821 0.03247  119 MET A SD  
812  C CE  . MET A 112 ? 0.47640 0.82755 0.70189 0.00790  -0.10299 0.04897  119 MET A CE  
813  N N   . GLU A 113 ? 0.55750 0.86475 0.75263 -0.13253 -0.16410 -0.06880 120 GLU A N   
814  C CA  . GLU A 113 ? 0.58992 0.91068 0.78569 -0.16525 -0.18358 -0.08860 120 GLU A CA  
815  C C   . GLU A 113 ? 0.52545 0.82612 0.67715 -0.17239 -0.18893 -0.12218 120 GLU A C   
816  O O   . GLU A 113 ? 0.65329 0.98886 0.79013 -0.19154 -0.20730 -0.13323 120 GLU A O   
817  C CB  . GLU A 113 ? 0.57557 0.86505 0.79841 -0.18349 -0.18154 -0.09529 120 GLU A CB  
818  C CG  . GLU A 113 ? 0.70042 1.03469 0.96845 -0.19602 -0.18821 -0.06871 120 GLU A CG  
819  C CD  . GLU A 113 ? 0.88665 1.19077 1.18330 -0.19452 -0.17343 -0.05670 120 GLU A CD  
820  O OE1 . GLU A 113 ? 0.93871 1.18681 1.22743 -0.20173 -0.16829 -0.07639 120 GLU A OE1 
821  O OE2 . GLU A 113 ? 0.79165 1.12965 1.11924 -0.18549 -0.16637 -0.02668 120 GLU A OE2 
822  N N   . ALA A 114 ? 0.53103 0.77978 0.66104 -0.15680 -0.17272 -0.13820 121 ALA A N   
823  C CA  . ALA A 114 ? 0.62733 0.85669 0.71661 -0.16076 -0.17368 -0.17116 121 ALA A CA  
824  C C   . ALA A 114 ? 0.61107 0.88559 0.67182 -0.15315 -0.18013 -0.16286 121 ALA A C   
825  O O   . ALA A 114 ? 0.71409 1.00277 0.74329 -0.16801 -0.19060 -0.18644 121 ALA A O   
826  C CB  . ALA A 114 ? 0.57788 0.74892 0.65676 -0.14184 -0.15338 -0.18408 121 ALA A CB  
827  N N   . LEU A 115 ? 0.56203 0.85930 0.63276 -0.13050 -0.17380 -0.12933 122 LEU A N   
828  C CA  . LEU A 115 ? 0.57791 0.91497 0.62493 -0.12159 -0.17900 -0.11601 122 LEU A CA  
829  C C   . LEU A 115 ? 0.67683 1.07374 0.72288 -0.14335 -0.20309 -0.11118 122 LEU A C   
830  O O   . LEU A 115 ? 0.74896 1.18113 0.76773 -0.14260 -0.21110 -0.10585 122 LEU A O   
831  C CB  . LEU A 115 ? 0.46252 0.80634 0.52705 -0.09354 -0.16738 -0.08032 122 LEU A CB  
832  C CG  . LEU A 115 ? 0.61303 0.90950 0.66481 -0.07140 -0.14624 -0.08382 122 LEU A CG  
833  C CD1 . LEU A 115 ? 0.55506 0.84796 0.63280 -0.04851 -0.13448 -0.05363 122 LEU A CD1 
834  C CD2 . LEU A 115 ? 0.43271 0.73169 0.44535 -0.06610 -0.14357 -0.09259 122 LEU A CD2 
835  N N   . GLN A 116 ? 0.65357 1.06588 0.72916 -0.16412 -0.21558 -0.11124 123 GLN A N   
836  C CA  . GLN A 116 ? 0.60014 1.05893 0.67573 -0.18465 -0.23693 -0.10711 123 GLN A CA  
837  C C   . GLN A 116 ? 0.69937 1.12863 0.75103 -0.21003 -0.24435 -0.14529 123 GLN A C   
838  O O   . GLN A 116 ? 0.71781 1.17498 0.76094 -0.22484 -0.25976 -0.14552 123 GLN A O   
839  C CB  . GLN A 116 ? 0.80818 1.30118 0.93492 -0.18776 -0.24368 -0.07747 123 GLN A CB  
840  C CG  . GLN A 116 ? 0.66339 1.18689 0.81672 -0.15985 -0.23576 -0.03717 123 GLN A CG  
841  C CD  . GLN A 116 ? 1.03533 1.58707 1.24063 -0.16052 -0.23710 -0.01121 123 GLN A CD  
842  O OE1 . GLN A 116 ? 0.98698 1.52032 1.21790 -0.17101 -0.23241 -0.01768 123 GLN A OE1 
843  N NE2 . GLN A 116 ? 1.00985 1.60627 1.23145 -0.14945 -0.24222 0.01905  123 GLN A NE2 
844  N N   . ALA A 117 ? 0.72038 1.09275 0.76309 -0.21413 -0.23333 -0.17686 124 ALA A N   
845  C CA  . ALA A 117 ? 0.75111 1.08466 0.76948 -0.23325 -0.23685 -0.21425 124 ALA A CA  
846  C C   . ALA A 117 ? 0.87903 1.19415 0.84574 -0.22382 -0.22738 -0.23765 124 ALA A C   
847  O O   . ALA A 117 ? 1.09444 1.36955 1.03840 -0.23416 -0.22503 -0.27109 124 ALA A O   
848  C CB  . ALA A 117 ? 0.85026 1.12663 0.89284 -0.24139 -0.22853 -0.23244 124 ALA A CB  
849  N N   . GLY A 118 ? 0.69973 1.04290 0.64919 -0.20381 -0.22089 -0.21931 125 GLY A N   
850  C CA  . GLY A 118 ? 0.77480 1.10977 0.67809 -0.19436 -0.21062 -0.23567 125 GLY A CA  
851  C C   . GLY A 118 ? 0.77920 1.08872 0.67754 -0.17055 -0.18986 -0.23667 125 GLY A C   
852  O O   . GLY A 118 ? 0.81151 1.12860 0.67671 -0.15923 -0.18080 -0.23869 125 GLY A O   
853  N N   . ALA A 119 ? 0.71099 0.99267 0.64240 -0.16310 -0.18201 -0.23473 126 ALA A N   
854  C CA  . ALA A 119 ? 0.79217 1.04213 0.72189 -0.13826 -0.16122 -0.23414 126 ALA A CA  
855  C C   . ALA A 119 ? 0.69760 0.98138 0.62064 -0.11812 -0.15752 -0.19890 126 ALA A C   
856  O O   . ALA A 119 ? 0.66973 0.99939 0.60307 -0.12026 -0.17066 -0.17018 126 ALA A O   
857  C CB  . ALA A 119 ? 0.63740 0.84320 0.60728 -0.12952 -0.15108 -0.22498 126 ALA A CB  
858  N N   . ASP A 120 ? 0.64303 0.90409 0.55122 -0.09852 -0.13948 -0.20035 127 ASP A N   
859  C CA  . ASP A 120 ? 0.64177 0.92495 0.54611 -0.07971 -0.13387 -0.16760 127 ASP A CA  
860  C C   . ASP A 120 ? 0.63654 0.88050 0.56604 -0.05807 -0.11699 -0.15254 127 ASP A C   
861  O O   . ASP A 120 ? 0.54555 0.74798 0.49095 -0.05656 -0.10893 -0.16749 127 ASP A O   
862  C CB  . ASP A 120 ? 0.63507 0.93733 0.49684 -0.07833 -0.12888 -0.17794 127 ASP A CB  
863  C CG  . ASP A 120 ? 0.81432 1.07569 0.66693 -0.06510 -0.10763 -0.19805 127 ASP A CG  
864  O OD1 . ASP A 120 ? 0.87074 1.09475 0.72769 -0.06954 -0.10202 -0.22925 127 ASP A OD1 
865  O OD2 . ASP A 120 ? 0.82853 1.09572 0.67260 -0.05022 -0.09662 -0.18096 127 ASP A OD2 
866  N N   . ILE A 121 ? 0.57165 0.82975 0.50427 -0.04209 -0.11248 -0.12174 128 ILE A N   
867  C CA  . ILE A 121 ? 0.53037 0.75885 0.48755 -0.02368 -0.09988 -0.10354 128 ILE A CA  
868  C C   . ILE A 121 ? 0.57828 0.76513 0.52958 -0.01555 -0.08383 -0.12283 128 ILE A C   
869  O O   . ILE A 121 ? 0.50724 0.66267 0.47971 -0.00648 -0.07552 -0.11865 128 ILE A O   
870  C CB  . ILE A 121 ? 0.55095 0.80184 0.50979 -0.01025 -0.09909 -0.06958 128 ILE A CB  
871  C CG1 . ILE A 121 ? 0.70532 0.98324 0.69093 -0.00986 -0.11021 -0.04423 128 ILE A CG1 
872  C CG2 . ILE A 121 ? 0.50004 0.71712 0.46713 0.00725  -0.08304 -0.06025 128 ILE A CG2 
873  C CD1 . ILE A 121 ? 0.70002 1.00776 0.68659 0.00075  -0.11351 -0.01108 128 ILE A CD1 
874  N N   . SER A 122 ? 0.58057 0.76974 0.50369 -0.01871 -0.07915 -0.14418 129 SER A N   
875  C CA  . SER A 122 ? 0.56128 0.71777 0.48169 -0.00875 -0.06310 -0.16019 129 SER A CA  
876  C C   . SER A 122 ? 0.51206 0.62864 0.45223 -0.01061 -0.05992 -0.17998 129 SER A C   
877  O O   . SER A 122 ? 0.54427 0.63237 0.49242 0.00067  -0.04741 -0.18564 129 SER A O   
878  C CB  . SER A 122 ? 0.53082 0.70375 0.41756 -0.01186 -0.05756 -0.18090 129 SER A CB  
879  O OG  . SER A 122 ? 0.63093 0.79941 0.50539 -0.02611 -0.06258 -0.21433 129 SER A OG  
880  N N   . MET A 123 ? 0.59716 0.71253 0.54762 -0.02518 -0.07142 -0.18843 130 MET A N   
881  C CA  . MET A 123 ? 0.56350 0.63986 0.53543 -0.02892 -0.06929 -0.20363 130 MET A CA  
882  C C   . MET A 123 ? 0.49747 0.55890 0.50036 -0.02173 -0.06772 -0.17874 130 MET A C   
883  O O   . MET A 123 ? 0.52011 0.55479 0.54366 -0.02727 -0.06820 -0.18444 130 MET A O   
884  C CB  . MET A 123 ? 0.48541 0.56549 0.45579 -0.05134 -0.08258 -0.22483 130 MET A CB  
885  C CG  . MET A 123 ? 0.62203 0.67983 0.57396 -0.05767 -0.07779 -0.26456 130 MET A CG  
886  S SD  . MET A 123 ? 0.94850 1.02410 0.88328 -0.08788 -0.09602 -0.29318 130 MET A SD  
887  C CE  . MET A 123 ? 0.76108 0.90483 0.67074 -0.09191 -0.10870 -0.26961 130 MET A CE  
888  N N   . ILE A 124 ? 0.41218 0.48923 0.41802 -0.00993 -0.06516 -0.15176 131 ILE A N   
889  C CA  . ILE A 124 ? 0.48374 0.55437 0.51464 -0.00451 -0.06414 -0.12925 131 ILE A CA  
890  C C   . ILE A 124 ? 0.53476 0.56744 0.58001 0.00228  -0.05471 -0.13241 131 ILE A C   
891  O O   . ILE A 124 ? 0.44273 0.46584 0.50893 -0.00019 -0.05538 -0.12225 131 ILE A O   
892  C CB  . ILE A 124 ? 0.47960 0.56945 0.50794 0.00815  -0.06142 -0.10417 131 ILE A CB  
893  C CG1 . ILE A 124 ? 0.49458 0.58373 0.54649 0.01333  -0.06003 -0.08355 131 ILE A CG1 
894  C CG2 . ILE A 124 ? 0.46256 0.53789 0.47832 0.02093  -0.05021 -0.10432 131 ILE A CG2 
895  C CD1 . ILE A 124 ? 0.41468 0.51573 0.46626 0.02696  -0.05592 -0.06168 131 ILE A CD1 
896  N N   . GLY A 125 ? 0.53190 0.54635 0.56761 0.01090  -0.04578 -0.14440 132 GLY A N   
897  C CA  . GLY A 125 ? 0.50596 0.48851 0.55705 0.01850  -0.03809 -0.14453 132 GLY A CA  
898  C C   . GLY A 125 ? 0.60321 0.56060 0.67170 0.00864  -0.04108 -0.15647 132 GLY A C   
899  O O   . GLY A 125 ? 0.46041 0.39580 0.54746 0.01283  -0.03755 -0.14682 132 GLY A O   
900  N N   . GLN A 126 ? 0.43671 0.39675 0.49938 -0.00567 -0.04815 -0.17663 133 GLN A N   
901  C CA  . GLN A 126 ? 0.55280 0.48507 0.63417 -0.01799 -0.05187 -0.18858 133 GLN A CA  
902  C C   . GLN A 126 ? 0.59087 0.52811 0.69527 -0.02734 -0.05812 -0.16658 133 GLN A C   
903  O O   . GLN A 126 ? 0.55627 0.46932 0.68088 -0.03847 -0.06086 -0.17043 133 GLN A O   
904  C CB  . GLN A 126 ? 0.61813 0.55370 0.68500 -0.03423 -0.05924 -0.21799 133 GLN A CB  
905  C CG  . GLN A 126 ? 0.59779 0.53577 0.63789 -0.02599 -0.05173 -0.24113 133 GLN A CG  
906  C CD  . GLN A 126 ? 0.70008 0.62848 0.72675 -0.04167 -0.05623 -0.27692 133 GLN A CD  
907  O OE1 . GLN A 126 ? 0.74527 0.64954 0.78896 -0.05697 -0.06288 -0.28749 133 GLN A OE1 
908  N NE2 . GLN A 126 ? 0.73466 0.68245 0.72965 -0.03954 -0.05254 -0.29635 133 GLN A NE2 
909  N N   . PHE A 127 ? 0.51080 0.47835 0.61419 -0.02294 -0.05936 -0.14356 134 PHE A N   
910  C CA  . PHE A 127 ? 0.48596 0.46498 0.61099 -0.02943 -0.06246 -0.12183 134 PHE A CA  
911  C C   . PHE A 127 ? 0.42816 0.40438 0.55790 -0.01384 -0.05284 -0.09934 134 PHE A C   
912  O O   . PHE A 127 ? 0.46399 0.45591 0.60740 -0.01555 -0.05231 -0.08009 134 PHE A O   
913  C CB  . PHE A 127 ? 0.42953 0.45063 0.55324 -0.03819 -0.07206 -0.11479 134 PHE A CB  
914  C CG  . PHE A 127 ? 0.40745 0.43780 0.52266 -0.05636 -0.08397 -0.13707 134 PHE A CG  
915  C CD1 . PHE A 127 ? 0.40240 0.44233 0.48915 -0.05352 -0.08542 -0.15374 134 PHE A CD1 
916  C CD2 . PHE A 127 ? 0.41312 0.44397 0.54771 -0.07811 -0.09383 -0.14168 134 PHE A CD2 
917  C CE1 . PHE A 127 ? 0.43646 0.48708 0.51033 -0.07162 -0.09659 -0.17668 134 PHE A CE1 
918  C CE2 . PHE A 127 ? 0.50677 0.54582 0.63115 -0.09761 -0.10620 -0.16525 134 PHE A CE2 
919  C CZ  . PHE A 127 ? 0.45971 0.50897 0.55168 -0.09411 -0.10760 -0.18386 134 PHE A CZ  
920  N N   . GLY A 128 ? 0.44393 0.40339 0.56250 0.00062  -0.04503 -0.10200 135 GLY A N   
921  C CA  . GLY A 128 ? 0.44369 0.39942 0.56381 0.01296  -0.03742 -0.08373 135 GLY A CA  
922  C C   . GLY A 128 ? 0.52709 0.50759 0.63777 0.02088  -0.03487 -0.07012 135 GLY A C   
923  O O   . GLY A 128 ? 0.50356 0.48259 0.61501 0.02833  -0.02885 -0.05626 135 GLY A O   
924  N N   . VAL A 129 ? 0.47063 0.47341 0.57207 0.01973  -0.03918 -0.07348 136 VAL A N   
925  C CA  . VAL A 129 ? 0.45016 0.47324 0.54739 0.02866  -0.03637 -0.05908 136 VAL A CA  
926  C C   . VAL A 129 ? 0.41670 0.44373 0.49471 0.03618  -0.03556 -0.06338 136 VAL A C   
927  O O   . VAL A 129 ? 0.42551 0.47168 0.50035 0.04091  -0.03650 -0.05364 136 VAL A O   
928  C CB  . VAL A 129 ? 0.46563 0.51828 0.57699 0.02170  -0.04236 -0.04997 136 VAL A CB  
929  C CG1 . VAL A 129 ? 0.42989 0.48239 0.56217 0.01543  -0.04017 -0.04043 136 VAL A CG1 
930  C CG2 . VAL A 129 ? 0.37314 0.43967 0.48119 0.00855  -0.05383 -0.06284 136 VAL A CG2 
931  N N   . GLY A 130 ? 0.40830 0.41829 0.47610 0.03805  -0.03301 -0.07577 137 GLY A N   
932  C CA  . GLY A 130 ? 0.43801 0.45417 0.48871 0.04356  -0.03103 -0.07877 137 GLY A CA  
933  C C   . GLY A 130 ? 0.44981 0.46690 0.49635 0.05337  -0.02593 -0.06399 137 GLY A C   
934  O O   . GLY A 130 ? 0.37313 0.40121 0.40881 0.05606  -0.02586 -0.06017 137 GLY A O   
935  N N   . PHE A 131 ? 0.37010 0.37553 0.42417 0.05782  -0.02152 -0.05570 138 PHE A N   
936  C CA  . PHE A 131 ? 0.38654 0.38697 0.43515 0.06598  -0.01613 -0.04615 138 PHE A CA  
937  C C   . PHE A 131 ? 0.40185 0.41786 0.45068 0.06996  -0.01723 -0.03575 138 PHE A C   
938  O O   . PHE A 131 ? 0.34981 0.36141 0.39178 0.07499  -0.01439 -0.03003 138 PHE A O   
939  C CB  . PHE A 131 ? 0.32414 0.31369 0.37781 0.06871  -0.01131 -0.04115 138 PHE A CB  
940  C CG  . PHE A 131 ? 0.39043 0.37539 0.43922 0.07640  -0.00538 -0.03402 138 PHE A CG  
941  C CD1 . PHE A 131 ? 0.41806 0.38931 0.45589 0.07837  -0.00296 -0.03569 138 PHE A CD1 
942  C CD2 . PHE A 131 ? 0.44399 0.43818 0.50124 0.08149  -0.00167 -0.02642 138 PHE A CD2 
943  C CE1 . PHE A 131 ? 0.44735 0.40852 0.48062 0.08405  0.00256  -0.03219 138 PHE A CE1 
944  C CE2 . PHE A 131 ? 0.37566 0.36111 0.42934 0.09029  0.00563  -0.02284 138 PHE A CE2 
945  C CZ  . PHE A 131 ? 0.42443 0.39045 0.46501 0.09100  0.00754  -0.02688 138 PHE A CZ  
946  N N   . TYR A 132 ? 0.36717 0.40228 0.42675 0.06741  -0.02184 -0.03120 139 TYR A N   
947  C CA  . TYR A 132 ? 0.29879 0.35228 0.36417 0.07338  -0.02335 -0.01735 139 TYR A CA  
948  C C   . TYR A 132 ? 0.32541 0.39383 0.37968 0.07097  -0.02942 -0.01478 139 TYR A C   
949  O O   . TYR A 132 ? 0.38279 0.46447 0.44147 0.07737  -0.03075 0.00064  139 TYR A O   
950  C CB  . TYR A 132 ? 0.36230 0.43865 0.44650 0.07085  -0.02723 -0.01100 139 TYR A CB  
951  C CG  . TYR A 132 ? 0.34023 0.40712 0.43500 0.07291  -0.01961 -0.01064 139 TYR A CG  
952  C CD1 . TYR A 132 ? 0.37386 0.43624 0.47416 0.08544  -0.00952 -0.00226 139 TYR A CD1 
953  C CD2 . TYR A 132 ? 0.38905 0.45036 0.48738 0.06237  -0.02158 -0.01872 139 TYR A CD2 
954  C CE1 . TYR A 132 ? 0.36016 0.41805 0.46590 0.08686  -0.00125 -0.00228 139 TYR A CE1 
955  C CE2 . TYR A 132 ? 0.42983 0.48590 0.53635 0.06326  -0.01447 -0.01495 139 TYR A CE2 
956  C CZ  . TYR A 132 ? 0.41240 0.46929 0.52081 0.07523  -0.00413 -0.00692 139 TYR A CZ  
957  O OH  . TYR A 132 ? 0.55355 0.60962 0.66630 0.07552  0.00405  -0.00347 139 TYR A OH  
958  N N   . SER A 133 ? 0.35053 0.41804 0.39093 0.06297  -0.03212 -0.02836 140 SER A N   
959  C CA  . SER A 133 ? 0.29876 0.38181 0.32409 0.06093  -0.03522 -0.02574 140 SER A CA  
960  C C   . SER A 133 ? 0.39084 0.46186 0.41189 0.06862  -0.02867 -0.01369 140 SER A C   
961  O O   . SER A 133 ? 0.36042 0.44652 0.37159 0.06769  -0.03055 -0.00446 140 SER A O   
962  C CB  . SER A 133 ? 0.37960 0.46246 0.39054 0.05260  -0.03579 -0.04603 140 SER A CB  
963  O OG  . SER A 133 ? 0.37220 0.43077 0.38209 0.05607  -0.02751 -0.05421 140 SER A OG  
964  N N   . ALA A 134 ? 0.33912 0.38417 0.36653 0.07445  -0.02147 -0.01335 141 ALA A N   
965  C CA  . ALA A 134 ? 0.36466 0.39431 0.39050 0.07968  -0.01607 -0.00285 141 ALA A CA  
966  C C   . ALA A 134 ? 0.35218 0.39169 0.38579 0.08649  -0.01786 0.01736  141 ALA A C   
967  O O   . ALA A 134 ? 0.39782 0.43223 0.42852 0.08782  -0.01608 0.02958  141 ALA A O   
968  C CB  . ALA A 134 ? 0.33154 0.33363 0.36164 0.08333  -0.00954 -0.00834 141 ALA A CB  
969  N N   . TYR A 135 ? 0.30091 0.35609 0.34751 0.09080  -0.02147 0.02340  142 TYR A N   
970  C CA  . TYR A 135 ? 0.32922 0.39792 0.38875 0.09973  -0.02371 0.04529  142 TYR A CA  
971  C C   . TYR A 135 ? 0.35161 0.45299 0.40261 0.09391  -0.03348 0.05737  142 TYR A C   
972  O O   . TYR A 135 ? 0.37173 0.49146 0.43473 0.10087  -0.03789 0.07941  142 TYR A O   
973  C CB  . TYR A 135 ? 0.28541 0.36552 0.36573 0.10708  -0.02351 0.04878  142 TYR A CB  
974  C CG  . TYR A 135 ? 0.43286 0.48226 0.51942 0.11540  -0.01152 0.04097  142 TYR A CG  
975  C CD1 . TYR A 135 ? 0.35200 0.38141 0.44913 0.12921  -0.00307 0.05101  142 TYR A CD1 
976  C CD2 . TYR A 135 ? 0.36634 0.40514 0.44650 0.10909  -0.00837 0.02322  142 TYR A CD2 
977  C CE1 . TYR A 135 ? 0.38494 0.38659 0.48275 0.13574  0.00846  0.04015  142 TYR A CE1 
978  C CE2 . TYR A 135 ? 0.43071 0.44571 0.51165 0.11531  0.00215  0.01626  142 TYR A CE2 
979  C CZ  . TYR A 135 ? 0.48315 0.48019 0.57093 0.12818  0.01074  0.02291  142 TYR A CZ  
980  O OH  . TYR A 135 ? 0.49987 0.47356 0.58394 0.13348  0.02182  0.01237  142 TYR A OH  
981  N N   . LEU A 136 ? 0.32554 0.43631 0.35614 0.08210  -0.03646 0.04391  143 LEU A N   
982  C CA  . LEU A 136 ? 0.42551 0.56626 0.44117 0.07602  -0.04326 0.05460  143 LEU A CA  
983  C C   . LEU A 136 ? 0.37665 0.50622 0.38974 0.07982  -0.03795 0.07343  143 LEU A C   
984  O O   . LEU A 136 ? 0.37158 0.52511 0.38202 0.08005  -0.04337 0.09610  143 LEU A O   
985  C CB  . LEU A 136 ? 0.47698 0.62909 0.47039 0.06359  -0.04481 0.03134  143 LEU A CB  
986  C CG  . LEU A 136 ? 0.41865 0.58631 0.41083 0.05509  -0.05274 0.01299  143 LEU A CG  
987  C CD1 . LEU A 136 ? 0.41397 0.57674 0.38701 0.04631  -0.04937 -0.01396 143 LEU A CD1 
988  C CD2 . LEU A 136 ? 0.33113 0.54068 0.32142 0.05017  -0.06611 0.02676  143 LEU A CD2 
989  N N   . VAL A 137 ? 0.35232 0.44732 0.36693 0.08137  -0.02836 0.06607  144 VAL A N   
990  C CA  . VAL A 137 ? 0.42790 0.50902 0.44152 0.08128  -0.02326 0.08193  144 VAL A CA  
991  C C   . VAL A 137 ? 0.44696 0.48894 0.47857 0.09030  -0.01685 0.08832  144 VAL A C   
992  O O   . VAL A 137 ? 0.51287 0.53928 0.54851 0.09016  -0.01361 0.10475  144 VAL A O   
993  C CB  . VAL A 137 ? 0.35376 0.43344 0.35176 0.07134  -0.01795 0.06786  144 VAL A CB  
994  C CG1 . VAL A 137 ? 0.37104 0.48934 0.34873 0.06352  -0.02176 0.06219  144 VAL A CG1 
995  C CG2 . VAL A 137 ? 0.31328 0.36900 0.31428 0.07116  -0.01357 0.04332  144 VAL A CG2 
996  N N   . ALA A 138 ? 0.41607 0.44126 0.45810 0.09733  -0.01425 0.07575  145 ALA A N   
997  C CA  . ALA A 138 ? 0.38805 0.37453 0.44200 0.10517  -0.00631 0.07471  145 ALA A CA  
998  C C   . ALA A 138 ? 0.42156 0.40844 0.49614 0.12054  -0.00517 0.08692  145 ALA A C   
999  O O   . ALA A 138 ? 0.52113 0.53425 0.60177 0.12384  -0.00936 0.08540  145 ALA A O   
1000 C CB  . ALA A 138 ? 0.37811 0.34520 0.42522 0.10129  -0.00173 0.04928  145 ALA A CB  
1001 N N   . GLU A 139 ? 0.49346 0.45104 0.58150 0.12990  0.00093  0.09914  146 GLU A N   
1002 C CA  . GLU A 139 ? 0.49446 0.44537 0.60565 0.14803  0.00606  0.10710  146 GLU A CA  
1003 C C   . GLU A 139 ? 0.53611 0.45913 0.64710 0.15327  0.01677  0.08323  146 GLU A C   
1004 O O   . GLU A 139 ? 0.54364 0.47087 0.67198 0.16808  0.02262  0.08432  146 GLU A O   
1005 C CB  . GLU A 139 ? 0.58467 0.51365 0.71365 0.15831  0.00899  0.13186  146 GLU A CB  
1006 C CG  . GLU A 139 ? 0.66674 0.54824 0.78883 0.15100  0.01545  0.12506  146 GLU A CG  
1007 C CD  . GLU A 139 ? 0.90295 0.76600 1.04196 0.15623  0.01570  0.15447  146 GLU A CD  
1008 O OE1 . GLU A 139 ? 0.94000 0.83730 1.08532 0.15797  0.00733  0.18259  146 GLU A OE1 
1009 O OE2 . GLU A 139 ? 1.12245 0.93620 1.26819 0.15763  0.02386  0.14986  146 GLU A OE2 
1010 N N   . LYS A 140 ? 0.48707 0.38631 0.57909 0.14140  0.01951  0.06290  147 LYS A N   
1011 C CA  . LYS A 140 ? 0.42991 0.30690 0.51560 0.14345  0.02835  0.04006  147 LYS A CA  
1012 C C   . LYS A 140 ? 0.45643 0.33461 0.52021 0.12657  0.02424  0.02254  147 LYS A C   
1013 O O   . LYS A 140 ? 0.45891 0.33379 0.51410 0.11472  0.01938  0.02486  147 LYS A O   
1014 C CB  . LYS A 140 ? 0.51043 0.34122 0.60073 0.15078  0.03874  0.03524  147 LYS A CB  
1015 C CG  . LYS A 140 ? 0.58091 0.39136 0.65901 0.15185  0.04830  0.00938  147 LYS A CG  
1016 C CD  . LYS A 140 ? 0.60263 0.37140 0.68597 0.16055  0.05879  0.00144  147 LYS A CD  
1017 C CE  . LYS A 140 ? 0.67554 0.40419 0.74514 0.14598  0.05791  -0.00837 147 LYS A CE  
1018 N NZ  . LYS A 140 ? 0.77244 0.46431 0.84581 0.14926  0.06278  -0.01681 147 LYS A NZ  
1019 N N   . VAL A 141 ? 0.36350 0.24891 0.42076 0.12606  0.02665  0.00744  148 VAL A N   
1020 C CA  . VAL A 141 ? 0.33241 0.22064 0.37283 0.11261  0.02270  -0.00676 148 VAL A CA  
1021 C C   . VAL A 141 ? 0.45232 0.31855 0.48190 0.11276  0.03014  -0.02348 148 VAL A C   
1022 O O   . VAL A 141 ? 0.50216 0.36959 0.53610 0.12306  0.03812  -0.02702 148 VAL A O   
1023 C CB  . VAL A 141 ? 0.42487 0.34563 0.46676 0.10937  0.01668  -0.00679 148 VAL A CB  
1024 C CG1 . VAL A 141 ? 0.35831 0.27879 0.38716 0.09821  0.01350  -0.01939 148 VAL A CG1 
1025 C CG2 . VAL A 141 ? 0.33814 0.28260 0.38576 0.10770  0.00900  0.00653  148 VAL A CG2 
1026 N N   . THR A 142 ? 0.45963 0.30974 0.47495 0.10081  0.02761  -0.03331 149 THR A N   
1027 C CA  . THR A 142 ? 0.47153 0.30544 0.47092 0.09689  0.03184  -0.05016 149 THR A CA  
1028 C C   . THR A 142 ? 0.43094 0.28271 0.42030 0.08530  0.02404  -0.05437 149 THR A C   
1029 O O   . THR A 142 ? 0.52142 0.38180 0.51313 0.07682  0.01641  -0.04947 149 THR A O   
1030 C CB  . THR A 142 ? 0.51386 0.31251 0.50616 0.09098  0.03399  -0.05827 149 THR A CB  
1031 O OG1 . THR A 142 ? 0.61842 0.39788 0.62558 0.10277  0.04056  -0.05009 149 THR A OG1 
1032 C CG2 . THR A 142 ? 0.56626 0.34876 0.53842 0.08752  0.03918  -0.07864 149 THR A CG2 
1033 N N   . VAL A 143 ? 0.48388 0.34326 0.46392 0.08596  0.02677  -0.06158 150 VAL A N   
1034 C CA  . VAL A 143 ? 0.40273 0.27820 0.37583 0.07675  0.01951  -0.06250 150 VAL A CA  
1035 C C   . VAL A 143 ? 0.54976 0.41551 0.50171 0.06999  0.02072  -0.07458 150 VAL A C   
1036 O O   . VAL A 143 ? 0.55198 0.41489 0.49398 0.07565  0.02957  -0.08132 150 VAL A O   
1037 C CB  . VAL A 143 ? 0.40967 0.30805 0.39208 0.08128  0.01951  -0.05542 150 VAL A CB  
1038 C CG1 . VAL A 143 ? 0.35017 0.26081 0.32953 0.07304  0.01195  -0.05376 150 VAL A CG1 
1039 C CG2 . VAL A 143 ? 0.39249 0.30168 0.39236 0.08604  0.01736  -0.04635 150 VAL A CG2 
1040 N N   . ILE A 144 ? 0.56656 0.43057 0.51138 0.05748  0.01207  -0.07741 151 ILE A N   
1041 C CA  . ILE A 144 ? 0.52655 0.38921 0.44979 0.04740  0.00900  -0.08746 151 ILE A CA  
1042 C C   . ILE A 144 ? 0.47275 0.36240 0.39846 0.04325  0.00042  -0.07756 151 ILE A C   
1043 O O   . ILE A 144 ? 0.48525 0.38628 0.42702 0.04105  -0.00685 -0.06856 151 ILE A O   
1044 C CB  . ILE A 144 ? 0.62502 0.47000 0.54148 0.03406  0.00325  -0.09597 151 ILE A CB  
1045 C CG1 . ILE A 144 ? 0.56044 0.37608 0.48454 0.03908  0.01065  -0.09939 151 ILE A CG1 
1046 C CG2 . ILE A 144 ? 0.52583 0.36695 0.41503 0.02276  0.00070  -0.11072 151 ILE A CG2 
1047 C CD1 . ILE A 144 ? 0.59292 0.38913 0.50842 0.05108  0.02409  -0.11030 151 ILE A CD1 
1048 N N   . THR A 145 ? 0.43337 0.33388 0.34450 0.04318  0.00232  -0.07807 152 THR A N   
1049 C CA  . THR A 145 ? 0.41979 0.34396 0.33740 0.04156  -0.00479 -0.06438 152 THR A CA  
1050 C C   . THR A 145 ? 0.45790 0.39413 0.35095 0.03315  -0.00835 -0.06567 152 THR A C   
1051 O O   . THR A 145 ? 0.45380 0.38308 0.32296 0.03231  -0.00054 -0.07803 152 THR A O   
1052 C CB  . THR A 145 ? 0.44907 0.38114 0.38289 0.05185  0.00132  -0.05444 152 THR A CB  
1053 O OG1 . THR A 145 ? 0.42781 0.37592 0.37437 0.05026  -0.00627 -0.04044 152 THR A OG1 
1054 C CG2 . THR A 145 ? 0.43731 0.37149 0.35742 0.05652  0.01269  -0.05771 152 THR A CG2 
1055 N N   . LYS A 146 ? 0.44348 0.39955 0.34272 0.02759  -0.01994 -0.05245 153 LYS A N   
1056 C CA  . LYS A 146 ? 0.44820 0.42307 0.32551 0.01850  -0.02667 -0.04816 153 LYS A CA  
1057 C C   . LYS A 146 ? 0.46653 0.46267 0.36170 0.02185  -0.03286 -0.02461 153 LYS A C   
1058 O O   . LYS A 146 ? 0.41612 0.41745 0.33717 0.02399  -0.04065 -0.01439 153 LYS A O   
1059 C CB  . LYS A 146 ? 0.46073 0.43939 0.32650 0.00415  -0.03890 -0.05560 153 LYS A CB  
1060 C CG  . LYS A 146 ? 0.43809 0.44264 0.28048 -0.00717 -0.04926 -0.04925 153 LYS A CG  
1061 C CD  . LYS A 146 ? 0.47238 0.47334 0.27701 -0.00950 -0.03914 -0.06338 153 LYS A CD  
1062 C CE  . LYS A 146 ? 0.50769 0.53413 0.28018 -0.02525 -0.05095 -0.06303 153 LYS A CE  
1063 N NZ  . LYS A 146 ? 0.57937 0.63910 0.35912 -0.02342 -0.05859 -0.03343 153 LYS A NZ  
1064 N N   . HIS A 147 ? 0.38073 0.33679 0.33445 -0.00508 -0.02209 -0.05061 154 HIS A N   
1065 C CA  . HIS A 147 ? 0.39740 0.36786 0.35501 -0.00128 -0.01440 -0.03431 154 HIS A CA  
1066 C C   . HIS A 147 ? 0.44203 0.42548 0.37883 0.00596  -0.02401 -0.03229 154 HIS A C   
1067 O O   . HIS A 147 ? 0.45277 0.43509 0.36278 0.01302  -0.03232 -0.04584 154 HIS A O   
1068 C CB  . HIS A 147 ? 0.43559 0.40934 0.39261 0.00197  0.00057  -0.02508 154 HIS A CB  
1069 C CG  . HIS A 147 ? 0.44084 0.41804 0.40809 0.00068  0.00511  -0.00449 154 HIS A CG  
1070 N ND1 . HIS A 147 ? 0.48834 0.47935 0.44131 0.00687  0.00480  0.01075  154 HIS A ND1 
1071 C CD2 . HIS A 147 ? 0.44855 0.41178 0.43671 -0.00519 0.00709  0.00350  154 HIS A CD2 
1072 C CE1 . HIS A 147 ? 0.43551 0.41782 0.40368 0.00281  0.00652  0.03056  154 HIS A CE1 
1073 N NE2 . HIS A 147 ? 0.49454 0.45655 0.48359 -0.00438 0.00629  0.02409  154 HIS A NE2 
1074 N N   . ASN A 148 ? 0.39106 0.38501 0.33663 0.00780  -0.02497 -0.01687 155 ASN A N   
1075 C CA  . ASN A 148 ? 0.45468 0.46513 0.38117 0.01586  -0.03603 -0.01244 155 ASN A CA  
1076 C C   . ASN A 148 ? 0.47455 0.49597 0.36585 0.02843  -0.03032 -0.00945 155 ASN A C   
1077 O O   . ASN A 148 ? 0.55608 0.59104 0.41945 0.03843  -0.04249 -0.01443 155 ASN A O   
1078 C CB  . ASN A 148 ? 0.46949 0.48722 0.41106 0.02032  -0.03595 0.00768  155 ASN A CB  
1079 C CG  . ASN A 148 ? 0.44091 0.47019 0.40716 0.01747  -0.04724 0.00438  155 ASN A CG  
1080 O OD1 . ASN A 148 ? 0.52085 0.55771 0.49332 0.00776  -0.05884 -0.00868 155 ASN A OD1 
1081 N ND2 . ASN A 148 ? 0.40785 0.43965 0.38997 0.02671  -0.04506 0.01805  155 ASN A ND2 
1082 N N   . ASP A 149 ? 0.49913 0.52161 0.39114 0.02948  -0.01272 -0.00060 156 ASP A N   
1083 C CA  . ASP A 149 ? 0.57286 0.62124 0.43716 0.04324  -0.00170 0.01133  156 ASP A CA  
1084 C C   . ASP A 149 ? 0.54806 0.60105 0.38982 0.05534  0.00256  -0.00976 156 ASP A C   
1085 O O   . ASP A 149 ? 0.59091 0.67557 0.41350 0.07008  0.01701  0.00169  156 ASP A O   
1086 C CB  . ASP A 149 ? 0.53510 0.59208 0.42222 0.03512  0.01444  0.04466  156 ASP A CB  
1087 C CG  . ASP A 149 ? 0.65324 0.69812 0.55562 0.02968  0.00784  0.06626  156 ASP A CG  
1088 O OD1 . ASP A 149 ? 0.68050 0.72817 0.56923 0.03768  -0.00518 0.06149  156 ASP A OD1 
1089 O OD2 . ASP A 149 ? 0.67412 0.70507 0.60242 0.01836  0.01293  0.08780  156 ASP A OD2 
1090 N N   . ASP A 150 ? 0.50347 0.52824 0.34731 0.05158  -0.00962 -0.03756 157 ASP A N   
1091 C CA  . ASP A 150 ? 0.50893 0.52806 0.33351 0.06574  -0.00731 -0.05810 157 ASP A CA  
1092 C C   . ASP A 150 ? 0.52298 0.50255 0.33823 0.06286  -0.03230 -0.08865 157 ASP A C   
1093 O O   . ASP A 150 ? 0.54746 0.51341 0.37886 0.04587  -0.04882 -0.08978 157 ASP A O   
1094 C CB  . ASP A 150 ? 0.51171 0.53384 0.36689 0.05789  0.01006  -0.04792 157 ASP A CB  
1095 C CG  . ASP A 150 ? 0.62158 0.66814 0.45681 0.08108  0.02308  -0.05276 157 ASP A CG  
1096 O OD1 . ASP A 150 ? 0.68353 0.73504 0.47556 0.10705  0.01704  -0.07121 157 ASP A OD1 
1097 O OD2 . ASP A 150 ? 0.59482 0.65798 0.45669 0.07581  0.03778  -0.03945 157 ASP A OD2 
1098 N N   . GLU A 151 ? 0.57923 0.54160 0.37060 0.07997  -0.03633 -0.11139 158 GLU A N   
1099 C CA  . GLU A 151 ? 0.56678 0.48052 0.35078 0.07544  -0.06355 -0.13863 158 GLU A CA  
1100 C C   . GLU A 151 ? 0.53947 0.43104 0.36601 0.05194  -0.06134 -0.13076 158 GLU A C   
1101 O O   . GLU A 151 ? 0.55644 0.46851 0.41053 0.04486  -0.03966 -0.11115 158 GLU A O   
1102 C CB  . GLU A 151 ? 0.64062 0.53567 0.37742 0.10872  -0.07162 -0.16807 158 GLU A CB  
1103 C CG  . GLU A 151 ? 0.82392 0.73931 0.50691 0.13817  -0.07871 -0.18225 158 GLU A CG  
1104 C CD  . GLU A 151 ? 1.20883 1.10231 0.83819 0.17920  -0.08879 -0.21747 158 GLU A CD  
1105 O OE1 . GLU A 151 ? 1.34495 1.19729 0.94350 0.18670  -0.12185 -0.24690 158 GLU A OE1 
1106 O OE2 . GLU A 151 ? 1.20181 1.12137 0.82698 0.20282  -0.06432 -0.21269 158 GLU A OE2 
1107 N N   . GLN A 152 ? 0.55569 0.40460 0.38665 0.03937  -0.08653 -0.14523 159 GLN A N   
1108 C CA  . GLN A 152 ? 0.56921 0.39885 0.43573 0.01927  -0.08569 -0.13523 159 GLN A CA  
1109 C C   . GLN A 152 ? 0.59097 0.40229 0.44532 0.03831  -0.07730 -0.14427 159 GLN A C   
1110 O O   . GLN A 152 ? 0.61729 0.40019 0.43534 0.06197  -0.09039 -0.16853 159 GLN A O   
1111 C CB  . GLN A 152 ? 0.55699 0.35161 0.43742 -0.00436 -0.11697 -0.13993 159 GLN A CB  
1112 C CG  . GLN A 152 ? 0.57103 0.36143 0.49345 -0.02891 -0.11376 -0.11901 159 GLN A CG  
1113 C CD  . GLN A 152 ? 0.61278 0.39478 0.56350 -0.05950 -0.13998 -0.10984 159 GLN A CD  
1114 O OE1 . GLN A 152 ? 0.81451 0.62568 0.77528 -0.06877 -0.14691 -0.10488 159 GLN A OE1 
1115 N NE2 . GLN A 152 ? 0.68142 0.42625 0.64821 -0.07621 -0.15608 -0.10412 159 GLN A NE2 
1116 N N   . TYR A 153 ? 0.52857 0.35613 0.41082 0.03147  -0.05769 -0.12674 160 TYR A N   
1117 C CA  . TYR A 153 ? 0.50336 0.32645 0.37918 0.05060  -0.04756 -0.13115 160 TYR A CA  
1118 C C   . TYR A 153 ? 0.55018 0.35189 0.45194 0.03513  -0.05045 -0.12045 160 TYR A C   
1119 O O   . TYR A 153 ? 0.52381 0.33347 0.45327 0.01076  -0.04987 -0.10362 160 TYR A O   
1120 C CB  . TYR A 153 ? 0.47073 0.34583 0.35328 0.06129  -0.02055 -0.11819 160 TYR A CB  
1121 C CG  . TYR A 153 ? 0.57418 0.47672 0.42572 0.08553  -0.01397 -0.12516 160 TYR A CG  
1122 C CD1 . TYR A 153 ? 0.53832 0.43894 0.35730 0.11981  -0.01434 -0.14352 160 TYR A CD1 
1123 C CD2 . TYR A 153 ? 0.60858 0.54159 0.46068 0.07819  -0.00714 -0.11196 160 TYR A CD2 
1124 C CE1 . TYR A 153 ? 0.64051 0.57652 0.42671 0.14711  -0.00584 -0.14828 160 TYR A CE1 
1125 C CE2 . TYR A 153 ? 0.57691 0.54200 0.39816 0.10167  0.00041  -0.11327 160 TYR A CE2 
1126 C CZ  . TYR A 153 ? 0.59848 0.56878 0.38611 0.13648  0.00215  -0.13128 160 TYR A CZ  
1127 O OH  . TYR A 153 ? 0.89813 0.91038 0.65074 0.16496  0.01212  -0.13118 160 TYR A OH  
1128 N N   . ALA A 154 ? 0.62240 0.40135 0.51270 0.05378  -0.05282 -0.12907 161 ALA A N   
1129 C CA  . ALA A 154 ? 0.56401 0.32309 0.47335 0.04462  -0.05547 -0.11687 161 ALA A CA  
1130 C C   . ALA A 154 ? 0.52524 0.31490 0.43822 0.06404  -0.03668 -0.11291 161 ALA A C   
1131 O O   . ALA A 154 ? 0.65285 0.44222 0.54454 0.09410  -0.03516 -0.12724 161 ALA A O   
1132 C CB  . ALA A 154 ? 0.58304 0.27503 0.47786 0.04715  -0.08351 -0.12811 161 ALA A CB  
1133 N N   . TRP A 155 ? 0.45946 0.27913 0.39867 0.04916  -0.02396 -0.09449 162 TRP A N   
1134 C CA  . TRP A 155 ? 0.45446 0.30398 0.40394 0.06071  -0.01150 -0.08829 162 TRP A CA  
1135 C C   . TRP A 155 ? 0.59977 0.42530 0.55547 0.05798  -0.01920 -0.07820 162 TRP A C   
1136 O O   . TRP A 155 ? 0.55161 0.36089 0.51611 0.03753  -0.02564 -0.06610 162 TRP A O   
1137 C CB  . TRP A 155 ? 0.40132 0.29552 0.37180 0.04629  0.00237  -0.07739 162 TRP A CB  
1138 C CG  . TRP A 155 ? 0.39485 0.32332 0.38117 0.05162  0.01030  -0.07098 162 TRP A CG  
1139 C CD1 . TRP A 155 ? 0.45207 0.42161 0.44844 0.05900  0.01970  -0.06876 162 TRP A CD1 
1140 C CD2 . TRP A 155 ? 0.40891 0.33975 0.40517 0.04803  0.00763  -0.06347 162 TRP A CD2 
1141 N NE1 . TRP A 155 ? 0.42801 0.42300 0.44358 0.05759  0.01999  -0.06199 162 TRP A NE1 
1142 C CE2 . TRP A 155 ? 0.42078 0.39094 0.43267 0.05308  0.01226  -0.06091 162 TRP A CE2 
1143 C CE3 . TRP A 155 ? 0.49114 0.40035 0.48508 0.04105  0.00144  -0.05582 162 TRP A CE3 
1144 C CZ2 . TRP A 155 ? 0.41124 0.39484 0.43227 0.05305  0.00790  -0.05613 162 TRP A CZ2 
1145 C CZ3 . TRP A 155 ? 0.44511 0.37066 0.44456 0.04394  0.00084  -0.04873 162 TRP A CZ3 
1146 C CH2 . TRP A 155 ? 0.43092 0.39089 0.44173 0.05063  0.00261  -0.05150 162 TRP A CH2 
1147 N N   . GLU A 156 ? 0.48117 0.31125 0.43377 0.07980  -0.01787 -0.07953 163 GLU A N   
1148 C CA  . GLU A 156 ? 0.47953 0.28537 0.43407 0.08184  -0.02625 -0.06759 163 GLU A CA  
1149 C C   . GLU A 156 ? 0.56953 0.41069 0.53034 0.10237  -0.01907 -0.06499 163 GLU A C   
1150 O O   . GLU A 156 ? 0.46655 0.33487 0.42519 0.12401  -0.01254 -0.07563 163 GLU A O   
1151 C CB  . GLU A 156 ? 0.56880 0.30798 0.50437 0.09182  -0.04648 -0.07442 163 GLU A CB  
1152 C CG  . GLU A 156 ? 0.65932 0.36475 0.60060 0.08376  -0.05796 -0.05280 163 GLU A CG  
1153 C CD  . GLU A 156 ? 0.88442 0.51139 0.81216 0.08340  -0.08433 -0.05637 163 GLU A CD  
1154 O OE1 . GLU A 156 ? 0.95988 0.56311 0.88732 0.06380  -0.09567 -0.06279 163 GLU A OE1 
1155 O OE2 . GLU A 156 ? 0.97311 0.55910 0.89100 0.10264  -0.09694 -0.05271 163 GLU A OE2 
1156 N N   . SER A 157 ? 0.52982 0.37704 0.49872 0.09696  -0.02066 -0.04878 164 SER A N   
1157 C CA  . SER A 157 ? 0.48305 0.36419 0.45862 0.11572  -0.01845 -0.04518 164 SER A CA  
1158 C C   . SER A 157 ? 0.50103 0.36845 0.47381 0.11438  -0.02571 -0.02586 164 SER A C   
1159 O O   . SER A 157 ? 0.49665 0.36396 0.47107 0.09331  -0.02439 -0.01302 164 SER A O   
1160 C CB  . SER A 157 ? 0.41584 0.35677 0.41109 0.10605  -0.00865 -0.04721 164 SER A CB  
1161 O OG  . SER A 157 ? 0.46620 0.44303 0.47190 0.11963  -0.01115 -0.04219 164 SER A OG  
1162 N N   . SER A 158 ? 0.47725 0.38102 0.46843 0.07952  0.02012  0.01549  165 SER A N   
1163 C CA  . SER A 158 ? 0.49942 0.40612 0.49851 0.08194  0.01989  0.03087  165 SER A CA  
1164 C C   . SER A 158 ? 0.44868 0.39140 0.45190 0.08267  0.01475  0.04592  165 SER A C   
1165 O O   . SER A 158 ? 0.55242 0.50560 0.56396 0.09152  0.01570  0.06149  165 SER A O   
1166 C CB  . SER A 158 ? 0.46375 0.34849 0.47210 0.09674  0.02985  0.03512  165 SER A CB  
1167 O OG  . SER A 158 ? 0.64318 0.49290 0.64828 0.09325  0.03266  0.01941  165 SER A OG  
1168 N N   . ALA A 159 ? 0.46014 0.42245 0.45836 0.07275  0.00873  0.04223  166 ALA A N   
1169 C CA  . ALA A 159 ? 0.58930 0.58773 0.59431 0.06951  0.00188  0.05454  166 ALA A CA  
1170 C C   . ALA A 159 ? 0.56785 0.58584 0.59159 0.08702  0.00927  0.06599  166 ALA A C   
1171 O O   . ALA A 159 ? 0.56550 0.56848 0.59033 0.09903  0.02017  0.05908  166 ALA A O   
1172 C CB  . ALA A 159 ? 0.41849 0.42385 0.41645 0.06197  -0.00756 0.06372  166 ALA A CB  
1173 N N   . GLY A 160 ? 0.50711 0.55909 0.54451 0.08969  0.00364  0.08388  167 GLY A N   
1174 C CA  . GLY A 160 ? 0.37868 0.45555 0.43747 0.10762  0.01188  0.09803  167 GLY A CA  
1175 C C   . GLY A 160 ? 0.43331 0.53287 0.50186 0.10616  0.01509  0.09734  167 GLY A C   
1176 O O   . GLY A 160 ? 0.51004 0.62985 0.59665 0.12364  0.02535  0.10964  167 GLY A O   
1177 N N   . GLY A 161 ? 0.45992 0.55611 0.51739 0.08765  0.00884  0.08514  168 GLY A N   
1178 C CA  . GLY A 161 ? 0.47373 0.59314 0.54161 0.08433  0.01204  0.08717  168 GLY A CA  
1179 C C   . GLY A 161 ? 0.46547 0.56108 0.52086 0.09376  0.02555  0.07349  168 GLY A C   
1180 O O   . GLY A 161 ? 0.44178 0.55611 0.50452 0.09322  0.03071  0.07674  168 GLY A O   
1181 N N   . SER A 162 ? 0.41484 0.47075 0.45153 0.10176  0.03098  0.05886  169 SER A N   
1182 C CA  . SER A 162 ? 0.53571 0.56889 0.55615 0.11056  0.04125  0.04427  169 SER A CA  
1183 C C   . SER A 162 ? 0.47217 0.46842 0.47047 0.10047  0.03558  0.02490  169 SER A C   
1184 O O   . SER A 162 ? 0.51125 0.49494 0.50861 0.09211  0.02814  0.02402  169 SER A O   
1185 C CB  . SER A 162 ? 0.46023 0.48348 0.48182 0.13632  0.05671  0.04661  169 SER A CB  
1186 O OG  . SER A 162 ? 0.54736 0.54124 0.56490 0.14247  0.05742  0.04288  169 SER A OG  
1187 N N   . PHE A 163 ? 0.43657 0.41892 0.41781 0.10189  0.03933  0.01122  170 PHE A N   
1188 C CA  . PHE A 163 ? 0.45441 0.40608 0.41695 0.09448  0.03407  -0.00658 170 PHE A CA  
1189 C C   . PHE A 163 ? 0.45980 0.39368 0.40305 0.10735  0.04144  -0.02053 170 PHE A C   
1190 O O   . PHE A 163 ? 0.48753 0.43469 0.42907 0.12093  0.05175  -0.01577 170 PHE A O   
1191 C CB  . PHE A 163 ? 0.39506 0.35310 0.35274 0.07629  0.02544  -0.00836 170 PHE A CB  
1192 C CG  . PHE A 163 ? 0.45460 0.43101 0.40854 0.07565  0.02949  -0.00576 170 PHE A CG  
1193 C CD1 . PHE A 163 ? 0.37028 0.37528 0.34006 0.07064  0.03032  0.00904  170 PHE A CD1 
1194 C CD2 . PHE A 163 ? 0.42171 0.38782 0.35706 0.07943  0.03200  -0.01705 170 PHE A CD2 
1195 C CE1 . PHE A 163 ? 0.40598 0.42666 0.37555 0.06918  0.03577  0.01345  170 PHE A CE1 
1196 C CE2 . PHE A 163 ? 0.41656 0.39907 0.34828 0.08059  0.03783  -0.01212 170 PHE A CE2 
1197 C CZ  . PHE A 163 ? 0.37662 0.38529 0.32668 0.07531  0.04082  0.00362  170 PHE A CZ  
1198 N N   . THR A 164 ? 0.49882 0.40328 0.42710 0.10299  0.03590  -0.03739 171 THR A N   
1199 C CA  . THR A 164 ? 0.48818 0.37101 0.39220 0.11290  0.03915  -0.05441 171 THR A CA  
1200 C C   . THR A 164 ? 0.55051 0.43115 0.43961 0.10110  0.02898  -0.06616 171 THR A C   
1201 O O   . THR A 164 ? 0.54812 0.43098 0.44634 0.08538  0.01940  -0.06488 171 THR A O   
1202 C CB  . THR A 164 ? 0.54132 0.38702 0.43930 0.11869  0.04042  -0.06626 171 THR A CB  
1203 O OG1 . THR A 164 ? 0.64463 0.47825 0.55404 0.10182  0.02958  -0.06867 171 THR A OG1 
1204 C CG2 . THR A 164 ? 0.51152 0.35707 0.42125 0.13591  0.05368  -0.05371 171 THR A CG2 
1205 N N   . VAL A 165 ? 0.52071 0.39773 0.38551 0.11089  0.03209  -0.07635 172 VAL A N   
1206 C CA  . VAL A 165 ? 0.50649 0.38292 0.35393 0.10332  0.02225  -0.08736 172 VAL A CA  
1207 C C   . VAL A 165 ? 0.51741 0.36671 0.33438 0.11274  0.02033  -0.10829 172 VAL A C   
1208 O O   . VAL A 165 ? 0.59806 0.43884 0.39816 0.13123  0.03247  -0.11092 172 VAL A O   
1209 C CB  . VAL A 165 ? 0.54058 0.44528 0.38452 0.10539  0.02721  -0.07625 172 VAL A CB  
1210 C CG1 . VAL A 165 ? 0.46381 0.36875 0.28711 0.10193  0.01820  -0.08622 172 VAL A CG1 
1211 C CG2 . VAL A 165 ? 0.42873 0.35361 0.29861 0.09292  0.02711  -0.05900 172 VAL A CG2 
1212 N N   . ARG A 166 ? 0.61994 0.45553 0.42959 0.10006  0.00509  -0.12293 173 ARG A N   
1213 C CA  . ARG A 166 ? 0.62163 0.43054 0.39906 0.10449  -0.00156 -0.14590 173 ARG A CA  
1214 C C   . ARG A 166 ? 0.59870 0.41744 0.37091 0.08967  -0.02008 -0.15400 173 ARG A C   
1215 O O   . ARG A 166 ? 0.56551 0.40222 0.36417 0.07493  -0.02697 -0.14318 173 ARG A O   
1216 C CB  . ARG A 166 ? 0.70345 0.47301 0.48237 0.10273  -0.00213 -0.15852 173 ARG A CB  
1217 C CG  . ARG A 166 ? 0.73478 0.49666 0.53984 0.08002  -0.01645 -0.16044 173 ARG A CG  
1218 C CD  . ARG A 166 ? 0.87255 0.59723 0.68663 0.08003  -0.01142 -0.16547 173 ARG A CD  
1219 N NE  . ARG A 166 ? 0.99667 0.73368 0.83828 0.08578  0.00170  -0.14335 173 ARG A NE  
1220 C CZ  . ARG A 166 ? 1.04112 0.75310 0.89477 0.09019  0.01023  -0.13991 173 ARG A CZ  
1221 N NH1 . ARG A 166 ? 0.97721 0.64475 0.81835 0.08924  0.00909  -0.15777 173 ARG A NH1 
1222 N NH2 . ARG A 166 ? 0.85303 0.58380 0.73047 0.09580  0.01999  -0.11793 173 ARG A NH2 
1223 N N   . THR A 167 ? 0.71319 0.52140 0.44967 0.09511  -0.02771 -0.17212 174 THR A N   
1224 C CA  . THR A 167 ? 0.70572 0.52257 0.43771 0.08019  -0.04881 -0.18177 174 THR A CA  
1225 C C   . THR A 167 ? 0.68784 0.48437 0.44314 0.05951  -0.06240 -0.19083 174 THR A C   
1226 O O   . THR A 167 ? 0.76740 0.52719 0.51725 0.06001  -0.05977 -0.20366 174 THR A O   
1227 C CB  . THR A 167 ? 0.74552 0.55280 0.42937 0.09053  -0.05618 -0.20151 174 THR A CB  
1228 O OG1 . THR A 167 ? 0.89326 0.65728 0.55113 0.09894  -0.05148 -0.22119 174 THR A OG1 
1229 C CG2 . THR A 167 ? 0.67072 0.50346 0.33421 0.11057  -0.04247 -0.18867 174 THR A CG2 
1230 N N   . ASP A 168 ? 0.66405 0.48385 0.44696 0.04235  -0.07483 -0.18215 175 ASP A N   
1231 C CA  . ASP A 168 ? 0.74931 0.55573 0.56125 0.02184  -0.08624 -0.18596 175 ASP A CA  
1232 C C   . ASP A 168 ? 0.96185 0.75802 0.75826 0.00839  -0.10933 -0.20841 175 ASP A C   
1233 O O   . ASP A 168 ? 0.82802 0.65200 0.61389 0.00632  -0.12267 -0.20932 175 ASP A O   
1234 C CB  . ASP A 168 ? 0.64462 0.48138 0.49609 0.01101  -0.08628 -0.16351 175 ASP A CB  
1235 C CG  . ASP A 168 ? 0.89110 0.71507 0.77664 -0.00804 -0.09348 -0.16286 175 ASP A CG  
1236 O OD1 . ASP A 168 ? 0.92953 0.72049 0.81861 -0.00810 -0.08671 -0.16852 175 ASP A OD1 
1237 O OD2 . ASP A 168 ? 0.89192 0.73941 0.80205 -0.02187 -0.10458 -0.15488 175 ASP A OD2 
1238 N N   . THR A 169 ? 1.02149 0.77749 0.81701 -0.00131 -0.11447 -0.22586 176 THR A N   
1239 C CA  . THR A 169 ? 1.16367 0.90216 0.94413 -0.01799 -0.13822 -0.25064 176 THR A CA  
1240 C C   . THR A 169 ? 1.16682 0.91667 0.99353 -0.04599 -0.15467 -0.24532 176 THR A C   
1241 O O   . THR A 169 ? 1.11222 0.85233 0.93439 -0.06495 -0.17771 -0.26448 176 THR A O   
1242 C CB  . THR A 169 ? 1.28033 0.96166 1.02846 -0.01252 -0.13270 -0.27460 176 THR A CB  
1243 O OG1 . THR A 169 ? 1.12535 0.78069 0.89927 -0.01004 -0.11497 -0.26471 176 THR A OG1 
1244 C CG2 . THR A 169 ? 1.12523 0.80466 0.82637 0.01359  -0.11752 -0.27868 176 THR A CG2 
1245 N N   . GLY A 170 ? 1.07560 0.84671 0.94602 -0.04922 -0.14371 -0.21947 177 GLY A N   
1246 C CA  . GLY A 170 ? 0.95312 0.73541 0.87093 -0.07294 -0.15430 -0.21004 177 GLY A CA  
1247 C C   . GLY A 170 ? 1.02898 0.85935 0.96340 -0.08458 -0.17348 -0.20244 177 GLY A C   
1248 O O   . GLY A 170 ? 1.03128 0.87645 0.93547 -0.08171 -0.18829 -0.21483 177 GLY A O   
1249 N N   . GLU A 171 ? 0.99892 0.85542 0.98156 -0.09598 -0.17217 -0.17998 178 GLU A N   
1250 C CA  . GLU A 171 ? 0.92373 0.82916 0.93095 -0.10678 -0.18871 -0.16822 178 GLU A CA  
1251 C C   . GLU A 171 ? 0.89930 0.84035 0.88825 -0.08567 -0.18003 -0.15348 178 GLU A C   
1252 O O   . GLU A 171 ? 0.69333 0.63403 0.68238 -0.06994 -0.15738 -0.13720 178 GLU A O   
1253 C CB  . GLU A 171 ? 1.02163 0.94361 1.08638 -0.12142 -0.18476 -0.14516 178 GLU A CB  
1254 C CG  . GLU A 171 ? 1.01523 0.99138 1.11342 -0.13194 -0.19985 -0.12871 178 GLU A CG  
1255 C CD  . GLU A 171 ? 1.14799 1.13295 1.24633 -0.15399 -0.23238 -0.14894 178 GLU A CD  
1256 O OE1 . GLU A 171 ? 1.21761 1.16129 1.30913 -0.17012 -0.24266 -0.17243 178 GLU A OE1 
1257 O OE2 . GLU A 171 ? 1.13537 1.16768 1.23932 -0.15506 -0.24797 -0.14134 178 GLU A OE2 
1258 N N   . PRO A 172 ? 0.87983 0.85107 0.85251 -0.08515 -0.19767 -0.15822 179 PRO A N   
1259 C CA  . PRO A 172 ? 0.71154 0.71504 0.66844 -0.06437 -0.18753 -0.14175 179 PRO A CA  
1260 C C   . PRO A 172 ? 0.68712 0.72488 0.68591 -0.06360 -0.17686 -0.11074 179 PRO A C   
1261 O O   . PRO A 172 ? 0.71382 0.77373 0.75351 -0.08015 -0.18801 -0.10110 179 PRO A O   
1262 C CB  . PRO A 172 ? 0.73230 0.76012 0.66421 -0.06610 -0.21216 -0.15433 179 PRO A CB  
1263 C CG  . PRO A 172 ? 0.74410 0.74063 0.66532 -0.08583 -0.23376 -0.18411 179 PRO A CG  
1264 C CD  . PRO A 172 ? 0.68774 0.66370 0.65303 -0.10335 -0.22818 -0.17912 179 PRO A CD  
1265 N N   . MET A 173 ? 0.64683 0.68778 0.63512 -0.04418 -0.15429 -0.09466 180 MET A N   
1266 C CA  . MET A 173 ? 0.63068 0.69612 0.64987 -0.03987 -0.14042 -0.06642 180 MET A CA  
1267 C C   . MET A 173 ? 0.61397 0.71920 0.62871 -0.02763 -0.14143 -0.05050 180 MET A C   
1268 O O   . MET A 173 ? 0.71867 0.84492 0.75823 -0.02258 -0.12983 -0.02633 180 MET A O   
1269 C CB  . MET A 173 ? 0.66654 0.70698 0.67859 -0.02806 -0.11441 -0.05752 180 MET A CB  
1270 C CG  . MET A 173 ? 0.70852 0.70877 0.71036 -0.03146 -0.10980 -0.07330 180 MET A CG  
1271 S SD  . MET A 173 ? 0.82912 0.81254 0.80234 -0.01226 -0.08626 -0.06802 180 MET A SD  
1272 C CE  . MET A 173 ? 0.47677 0.47260 0.47517 -0.00978 -0.06989 -0.04093 180 MET A CE  
1273 N N   . GLY A 174 ? 0.48826 0.60287 0.47007 -0.02047 -0.15291 -0.06198 181 GLY A N   
1274 C CA  . GLY A 174 ? 0.57819 0.73028 0.55417 -0.00621 -0.15217 -0.04461 181 GLY A CA  
1275 C C   . GLY A 174 ? 0.56525 0.70632 0.51938 0.01490  -0.12569 -0.03176 181 GLY A C   
1276 O O   . GLY A 174 ? 0.54068 0.68450 0.46099 0.02893  -0.12373 -0.03477 181 GLY A O   
1277 N N   . ARG A 175 ? 0.43279 0.56023 0.40497 0.01681  -0.10521 -0.01731 182 ARG A N   
1278 C CA  . ARG A 175 ? 0.55781 0.66851 0.51106 0.03244  -0.08065 -0.00694 182 ARG A CA  
1279 C C   . ARG A 175 ? 0.43724 0.52608 0.40863 0.02852  -0.06411 0.00152  182 ARG A C   
1280 O O   . ARG A 175 ? 0.47120 0.57285 0.47316 0.02308  -0.06382 0.01437  182 ARG A O   
1281 C CB  . ARG A 175 ? 0.41350 0.55128 0.36214 0.04871  -0.07263 0.01410  182 ARG A CB  
1282 C CG  . ARG A 175 ? 0.38266 0.49917 0.30726 0.06346  -0.04853 0.02223  182 ARG A CG  
1283 C CD  . ARG A 175 ? 0.39278 0.52659 0.32130 0.07878  -0.03393 0.04789  182 ARG A CD  
1284 N NE  . ARG A 175 ? 0.37970 0.51647 0.33712 0.07656  -0.02549 0.06348  182 ARG A NE  
1285 C CZ  . ARG A 175 ? 0.36889 0.54136 0.35291 0.07892  -0.03180 0.07986  182 ARG A CZ  
1286 N NH1 . ARG A 175 ? 0.38187 0.59252 0.36807 0.08166  -0.04986 0.08204  182 ARG A NH1 
1287 N NH2 . ARG A 175 ? 0.35898 0.53087 0.36777 0.07923  -0.01976 0.09546  182 ARG A NH2 
1288 N N   . GLY A 176 ? 0.40389 0.46218 0.35711 0.03156  -0.05063 -0.00443 183 GLY A N   
1289 C CA  . GLY A 176 ? 0.41027 0.44847 0.37328 0.02989  -0.03509 0.00413  183 GLY A CA  
1290 C C   . GLY A 176 ? 0.45804 0.46780 0.41250 0.02404  -0.03370 -0.01028 183 GLY A C   
1291 O O   . GLY A 176 ? 0.45515 0.45771 0.39161 0.02531  -0.03898 -0.02470 183 GLY A O   
1292 N N   . THR A 177 ? 0.44150 0.43620 0.40831 0.01963  -0.02535 -0.00450 184 THR A N   
1293 C CA  . THR A 177 ? 0.42801 0.39838 0.38824 0.01617  -0.02202 -0.01344 184 THR A CA  
1294 C C   . THR A 177 ? 0.43439 0.39757 0.41819 0.00776  -0.02287 -0.00993 184 THR A C   
1295 O O   . THR A 177 ? 0.47806 0.44756 0.47639 0.00821  -0.01602 0.00485  184 THR A O   
1296 C CB  . THR A 177 ? 0.43496 0.39134 0.37657 0.02225  -0.00718 -0.00753 184 THR A CB  
1297 O OG1 . THR A 177 ? 0.49579 0.45583 0.41787 0.02862  -0.00612 -0.01215 184 THR A OG1 
1298 C CG2 . THR A 177 ? 0.47919 0.41640 0.42021 0.01809  -0.00432 -0.01155 184 THR A CG2 
1299 N N   . LYS A 178 ? 0.45436 0.40347 0.44159 0.00184  -0.02932 -0.02202 185 LYS A N   
1300 C CA  . LYS A 178 ? 0.35016 0.28835 0.35899 -0.00551 -0.02866 -0.01850 185 LYS A CA  
1301 C C   . LYS A 178 ? 0.50082 0.41821 0.49749 -0.00172 -0.02061 -0.02037 185 LYS A C   
1302 O O   . LYS A 178 ? 0.42565 0.33386 0.40976 0.00058  -0.02380 -0.03267 185 LYS A O   
1303 C CB  . LYS A 178 ? 0.44724 0.38437 0.47259 -0.01644 -0.04357 -0.03051 185 LYS A CB  
1304 C CG  . LYS A 178 ? 0.61525 0.55483 0.67504 -0.02690 -0.04467 -0.02037 185 LYS A CG  
1305 C CD  . LYS A 178 ? 0.61802 0.53987 0.69046 -0.03902 -0.05583 -0.03466 185 LYS A CD  
1306 C CE  . LYS A 178 ? 0.66973 0.59236 0.72530 -0.04262 -0.07235 -0.05578 185 LYS A CE  
1307 N NZ  . LYS A 178 ? 0.88501 0.83854 0.95662 -0.05121 -0.08671 -0.05309 185 LYS A NZ  
1308 N N   . VAL A 179 ? 0.37623 0.28768 0.37526 0.00029  -0.00999 -0.00729 186 VAL A N   
1309 C CA  . VAL A 179 ? 0.40792 0.30423 0.39705 0.00349  -0.00425 -0.00658 186 VAL A CA  
1310 C C   . VAL A 179 ? 0.42964 0.31562 0.43914 -0.00010 -0.00280 -0.00091 186 VAL A C   
1311 O O   . VAL A 179 ? 0.37386 0.26242 0.39687 -0.00132 0.00306  0.01229  186 VAL A O   
1312 C CB  . VAL A 179 ? 0.42677 0.32099 0.39691 0.00836  0.00543  0.00257  186 VAL A CB  
1313 C CG1 . VAL A 179 ? 0.44548 0.32876 0.40788 0.01021  0.00832  0.00486  186 VAL A CG1 
1314 C CG2 . VAL A 179 ? 0.38974 0.29022 0.34137 0.01104  0.00541  -0.00251 186 VAL A CG2 
1315 N N   . ILE A 180 ? 0.38549 0.25883 0.39738 -0.00022 -0.00602 -0.00916 187 ILE A N   
1316 C CA  . ILE A 180 ? 0.42469 0.28392 0.45626 -0.00308 -0.00369 -0.00411 187 ILE A CA  
1317 C C   . ILE A 180 ? 0.47515 0.32607 0.49622 0.00549  0.00397  0.00349  187 ILE A C   
1318 O O   . ILE A 180 ? 0.45722 0.30549 0.46600 0.01110  0.00264  -0.00364 187 ILE A O   
1319 C CB  . ILE A 180 ? 0.42523 0.27128 0.46668 -0.00908 -0.01234 -0.01920 187 ILE A CB  
1320 C CG1 . ILE A 180 ? 0.40815 0.26732 0.45461 -0.01784 -0.02386 -0.02858 187 ILE A CG1 
1321 C CG2 . ILE A 180 ? 0.39392 0.22177 0.45917 -0.01382 -0.00853 -0.01252 187 ILE A CG2 
1322 C CD1 . ILE A 180 ? 0.46940 0.31273 0.51901 -0.02546 -0.03495 -0.04693 187 ILE A CD1 
1323 N N   . LEU A 181 ? 0.48690 0.33622 0.51267 0.00763  0.01220  0.01946  188 LEU A N   
1324 C CA  . LEU A 181 ? 0.43330 0.27820 0.44731 0.01604  0.01804  0.02892  188 LEU A CA  
1325 C C   . LEU A 181 ? 0.41739 0.24726 0.45082 0.01798  0.02284  0.03646  188 LEU A C   
1326 O O   . LEU A 181 ? 0.46727 0.29271 0.51836 0.01519  0.02893  0.04804  188 LEU A O   
1327 C CB  . LEU A 181 ? 0.38089 0.23071 0.37929 0.01935  0.02476  0.04145  188 LEU A CB  
1328 C CG  . LEU A 181 ? 0.45785 0.31614 0.43764 0.01749  0.02340  0.03635  188 LEU A CG  
1329 C CD1 . LEU A 181 ? 0.45934 0.31426 0.42515 0.02175  0.03316  0.04926  188 LEU A CD1 
1330 C CD2 . LEU A 181 ? 0.39000 0.25295 0.34954 0.01817  0.01754  0.02711  188 LEU A CD2 
1331 N N   . HIS A 182 ? 0.41851 0.24041 0.45010 0.02387  0.02197  0.03194  189 HIS A N   
1332 C CA  . HIS A 182 ? 0.41683 0.22129 0.46362 0.02892  0.02901  0.04117  189 HIS A CA  
1333 C C   . HIS A 182 ? 0.47406 0.28592 0.50950 0.03962  0.03561  0.05965  189 HIS A C   
1334 O O   . HIS A 182 ? 0.55862 0.38063 0.57928 0.04776  0.03327  0.06070  189 HIS A O   
1335 C CB  . HIS A 182 ? 0.42155 0.21231 0.46887 0.03372  0.02743  0.02935  189 HIS A CB  
1336 C CG  . HIS A 182 ? 0.61155 0.39441 0.66057 0.02447  0.01930  0.00865  189 HIS A CG  
1337 N ND1 . HIS A 182 ? 0.61268 0.37283 0.67969 0.01490  0.01780  0.00123  189 HIS A ND1 
1338 C CD2 . HIS A 182 ? 0.57321 0.36786 0.60670 0.02302  0.01163  -0.00594 189 HIS A CD2 
1339 C CE1 . HIS A 182 ? 0.65771 0.41672 0.71720 0.00801  0.00780  -0.01842 189 HIS A CE1 
1340 N NE2 . HIS A 182 ? 0.60020 0.38039 0.63902 0.01416  0.00496  -0.02214 189 HIS A NE2 
1341 N N   . LEU A 183 ? 0.46274 0.27157 0.50533 0.03995  0.04368  0.07542  190 LEU A N   
1342 C CA  . LEU A 183 ? 0.46662 0.28382 0.49004 0.04977  0.04883  0.09182  190 LEU A CA  
1343 C C   . LEU A 183 ? 0.46851 0.28151 0.49322 0.06248  0.05349  0.10445  190 LEU A C   
1344 O O   . LEU A 183 ? 0.62322 0.41928 0.66951 0.06452  0.05880  0.10644  190 LEU A O   
1345 C CB  . LEU A 183 ? 0.45572 0.27025 0.48467 0.04912  0.05892  0.10654  190 LEU A CB  
1346 C CG  . LEU A 183 ? 0.54320 0.36536 0.57000 0.04042  0.05703  0.09957  190 LEU A CG  
1347 C CD1 . LEU A 183 ? 0.54167 0.36243 0.57809 0.04312  0.07047  0.11852  190 LEU A CD1 
1348 C CD2 . LEU A 183 ? 0.49155 0.32394 0.48374 0.04146  0.05014  0.09008  190 LEU A CD2 
1349 N N   . LYS A 184 ? 0.46607 0.45285 0.58707 0.12830  -0.00793 0.12805  191 LYS A N   
1350 C CA  . LYS A 184 ? 0.51435 0.49757 0.64511 0.16106  -0.01695 0.15797  191 LYS A CA  
1351 C C   . LYS A 184 ? 0.59936 0.52500 0.68322 0.15524  -0.01651 0.17856  191 LYS A C   
1352 O O   . LYS A 184 ? 0.57369 0.48794 0.62684 0.12333  -0.01560 0.17130  191 LYS A O   
1353 C CB  . LYS A 184 ? 0.48604 0.55073 0.65023 0.17076  -0.04641 0.16910  191 LYS A CB  
1354 C CG  . LYS A 184 ? 0.44177 0.56834 0.66706 0.17287  -0.04294 0.15306  191 LYS A CG  
1355 C CD  . LYS A 184 ? 0.41606 0.62512 0.68064 0.16944  -0.07670 0.15607  191 LYS A CD  
1356 C CE  . LYS A 184 ? 0.46443 0.72643 0.78538 0.15144  -0.06779 0.13572  191 LYS A CE  
1357 N NZ  . LYS A 184 ? 0.47396 0.81430 0.84317 0.14120  -0.10238 0.13218  191 LYS A NZ  
1358 N N   . GLU A 185 ? 0.62750 0.51674 0.70957 0.18891  -0.01379 0.20772  192 GLU A N   
1359 C CA  . GLU A 185 ? 0.69636 0.51879 0.73485 0.18652  -0.00514 0.23474  192 GLU A CA  
1360 C C   . GLU A 185 ? 0.71881 0.57362 0.71882 0.16885  -0.02244 0.24929  192 GLU A C   
1361 O O   . GLU A 185 ? 0.77273 0.58330 0.73732 0.14571  -0.00662 0.25782  192 GLU A O   
1362 C CB  . GLU A 185 ? 0.84177 0.62569 0.88463 0.23416  -0.00240 0.27112  192 GLU A CB  
1363 C CG  . GLU A 185 ? 1.19703 0.91466 1.26264 0.25131  0.02542  0.25744  192 GLU A CG  
1364 C CD  . GLU A 185 ? 1.26103 1.03260 1.37962 0.28576  0.02210  0.24616  192 GLU A CD  
1365 O OE1 . GLU A 185 ? 1.06796 0.80030 1.20427 0.32474  0.03574  0.25661  192 GLU A OE1 
1366 O OE2 . GLU A 185 ? 1.04486 0.89726 1.18969 0.27128  0.00892  0.22516  192 GLU A OE2 
1367 N N   . ASP A 186 ? 0.65201 0.58414 0.66041 0.17844  -0.05322 0.24991  193 ASP A N   
1368 C CA  . ASP A 186 ? 0.71755 0.67755 0.67899 0.16927  -0.07188 0.26149  193 ASP A CA  
1369 C C   . ASP A 186 ? 0.68810 0.68086 0.64604 0.12909  -0.07257 0.22688  193 ASP A C   
1370 O O   . ASP A 186 ? 0.63184 0.65160 0.55127 0.12160  -0.08737 0.22810  193 ASP A O   
1371 C CB  . ASP A 186 ? 0.76789 0.79137 0.73442 0.20283  -0.11151 0.27796  193 ASP A CB  
1372 C CG  . ASP A 186 ? 0.77540 0.87814 0.80791 0.19767  -0.13324 0.24634  193 ASP A CG  
1373 O OD1 . ASP A 186 ? 0.80215 0.90103 0.87730 0.18171  -0.11216 0.22130  193 ASP A OD1 
1374 O OD2 . ASP A 186 ? 0.95880 1.12783 1.00004 0.20946  -0.17150 0.24685  193 ASP A OD2 
1375 N N   . GLN A 187 ? 0.54286 0.53029 0.53390 0.10677  -0.05646 0.19650  194 GLN A N   
1376 C CA  . GLN A 187 ? 0.56327 0.57902 0.55499 0.07442  -0.05668 0.16664  194 GLN A CA  
1377 C C   . GLN A 187 ? 0.53493 0.50624 0.51580 0.04758  -0.03082 0.15572  194 GLN A C   
1378 O O   . GLN A 187 ? 0.58471 0.57176 0.58017 0.02695  -0.02749 0.12890  194 GLN A O   
1379 C CB  . GLN A 187 ? 0.47017 0.53064 0.51086 0.07244  -0.06421 0.14181  194 GLN A CB  
1380 C CG  . GLN A 187 ? 0.48400 0.60113 0.55700 0.09370  -0.09095 0.14840  194 GLN A CG  
1381 C CD  . GLN A 187 ? 0.50270 0.65758 0.54839 0.08787  -0.11960 0.14732  194 GLN A CD  
1382 O OE1 . GLN A 187 ? 0.57552 0.72627 0.59161 0.06391  -0.11626 0.13168  194 GLN A OE1 
1383 N NE2 . GLN A 187 ? 0.47260 0.66595 0.52700 0.11253  -0.14942 0.16195  194 GLN A NE2 
1384 N N   . THR A 188 ? 0.59936 0.51616 0.55876 0.04746  -0.01290 0.17743  195 THR A N   
1385 C CA  . THR A 188 ? 0.54175 0.42195 0.50567 0.01812  0.00953  0.16501  195 THR A CA  
1386 C C   . THR A 188 ? 0.59502 0.50066 0.54263 -0.00590 0.01490  0.16066  195 THR A C   
1387 O O   . THR A 188 ? 0.63528 0.52731 0.59918 -0.03198 0.03079  0.14811  195 THR A O   
1388 C CB  . THR A 188 ? 0.62022 0.42790 0.57793 0.02142  0.03102  0.18916  195 THR A CB  
1389 O OG1 . THR A 188 ? 0.69236 0.48839 0.61022 0.03476  0.03564  0.22956  195 THR A OG1 
1390 C CG2 . THR A 188 ? 0.64052 0.41652 0.61642 0.04890  0.02967  0.18907  195 THR A CG2 
1391 N N   . GLU A 189 ? 0.52386 0.46848 0.44266 0.00300  0.00133  0.16755  196 GLU A N   
1392 C CA  . GLU A 189 ? 0.52339 0.49158 0.42437 -0.01501 0.00976  0.15941  196 GLU A CA  
1393 C C   . GLU A 189 ? 0.52073 0.51751 0.45687 -0.03371 0.00706  0.12411  196 GLU A C   
1394 O O   . GLU A 189 ? 0.53175 0.54122 0.46995 -0.05021 0.02063  0.11572  196 GLU A O   
1395 C CB  . GLU A 189 ? 0.64627 0.64619 0.50178 0.00125  -0.00806 0.16608  196 GLU A CB  
1396 C CG  . GLU A 189 ? 0.59643 0.64231 0.47185 0.00312  -0.03592 0.13642  196 GLU A CG  
1397 C CD  . GLU A 189 ? 0.74557 0.82055 0.57898 0.01835  -0.06108 0.13781  196 GLU A CD  
1398 O OE1 . GLU A 189 ? 0.79156 0.87401 0.61967 0.04068  -0.08280 0.15465  196 GLU A OE1 
1399 O OE2 . GLU A 189 ? 0.70010 0.79122 0.50567 0.01002  -0.06071 0.12017  196 GLU A OE2 
1400 N N   . TYR A 190 ? 0.49879 0.50681 0.46236 -0.02835 -0.00761 0.10628  197 TYR A N   
1401 C CA  . TYR A 190 ? 0.46647 0.49528 0.45551 -0.04060 -0.00990 0.07871  197 TYR A CA  
1402 C C   . TYR A 190 ? 0.51949 0.52504 0.53020 -0.05458 0.00030  0.06766  197 TYR A C   
1403 O O   . TYR A 190 ? 0.45734 0.47760 0.48358 -0.05947 -0.00507 0.04666  197 TYR A O   
1404 C CB  . TYR A 190 ? 0.46073 0.51066 0.46538 -0.02850 -0.02508 0.06841  197 TYR A CB  
1405 C CG  . TYR A 190 ? 0.47619 0.55415 0.46945 -0.01957 -0.04120 0.07308  197 TYR A CG  
1406 C CD1 . TYR A 190 ? 0.46680 0.56486 0.44529 -0.02802 -0.04507 0.06103  197 TYR A CD1 
1407 C CD2 . TYR A 190 ? 0.44069 0.52583 0.43878 -0.00117 -0.05449 0.08710  197 TYR A CD2 
1408 C CE1 . TYR A 190 ? 0.50353 0.62470 0.46721 -0.02205 -0.06424 0.05792  197 TYR A CE1 
1409 C CE2 . TYR A 190 ? 0.48508 0.60319 0.47554 0.00567  -0.07682 0.08706  197 TYR A CE2 
1410 C CZ  . TYR A 190 ? 0.52836 0.66257 0.49883 -0.00669 -0.08285 0.07014  197 TYR A CZ  
1411 O OH  . TYR A 190 ? 0.48010 0.64468 0.43903 -0.00203 -0.10934 0.06272  197 TYR A OH  
1412 N N   . LEU A 191 ? 0.52656 0.49378 0.53718 -0.06096 0.01365  0.08112  198 LEU A N   
1413 C CA  . LEU A 191 ? 0.53935 0.48594 0.57577 -0.08201 0.02152  0.06599  198 LEU A CA  
1414 C C   . LEU A 191 ? 0.53598 0.49453 0.58771 -0.10506 0.03802  0.07170  198 LEU A C   
1415 O O   . LEU A 191 ? 0.52869 0.48332 0.61547 -0.12765 0.04179  0.05614  198 LEU A O   
1416 C CB  . LEU A 191 ? 0.62100 0.50842 0.65870 -0.07851 0.02894  0.07221  198 LEU A CB  
1417 C CG  . LEU A 191 ? 0.65536 0.52891 0.68442 -0.05237 0.01959  0.06649  198 LEU A CG  
1418 C CD1 . LEU A 191 ? 0.52723 0.33428 0.55557 -0.04420 0.03192  0.07659  198 LEU A CD1 
1419 C CD2 . LEU A 191 ? 0.53809 0.43062 0.57318 -0.05377 0.00843  0.03357  198 LEU A CD2 
1420 N N   . GLU A 192 ? 0.59800 0.57430 0.62580 -0.09979 0.04817  0.09152  199 GLU A N   
1421 C CA  . GLU A 192 ? 0.54344 0.53317 0.58442 -0.11837 0.07262  0.10073  199 GLU A CA  
1422 C C   . GLU A 192 ? 0.48931 0.53344 0.55379 -0.12315 0.06769  0.07746  199 GLU A C   
1423 O O   . GLU A 192 ? 0.45252 0.51959 0.49733 -0.10665 0.05192  0.06653  199 GLU A O   
1424 C CB  . GLU A 192 ? 0.61704 0.59573 0.60790 -0.10575 0.09049  0.13412  199 GLU A CB  
1425 C CG  . GLU A 192 ? 0.84891 0.78160 0.80430 -0.08616 0.08557  0.16041  199 GLU A CG  
1426 C CD  . GLU A 192 ? 1.00612 0.88533 0.96200 -0.09703 0.11655  0.19283  199 GLU A CD  
1427 O OE1 . GLU A 192 ? 1.02172 0.90197 1.01806 -0.12632 0.14121  0.19006  199 GLU A OE1 
1428 O OE2 . GLU A 192 ? 1.06110 0.89803 0.98222 -0.07593 0.11690  0.22257  199 GLU A OE2 
1429 N N   . GLU A 193 ? 0.49942 0.56382 0.61268 -0.14589 0.08232  0.07081  200 GLU A N   
1430 C CA  . GLU A 193 ? 0.55152 0.67046 0.69949 -0.14720 0.07595  0.04898  200 GLU A CA  
1431 C C   . GLU A 193 ? 0.52052 0.66407 0.63534 -0.12888 0.08669  0.05387  200 GLU A C   
1432 O O   . GLU A 193 ? 0.38867 0.55518 0.50102 -0.11427 0.07064  0.03648  200 GLU A O   
1433 C CB  . GLU A 193 ? 0.44113 0.58595 0.65877 -0.17554 0.09125  0.04386  200 GLU A CB  
1434 C CG  . GLU A 193 ? 0.54089 0.75008 0.80652 -0.17363 0.08282  0.02315  200 GLU A CG  
1435 C CD  . GLU A 193 ? 0.68414 0.93150 1.03274 -0.20337 0.09928  0.01963  200 GLU A CD  
1436 O OE1 . GLU A 193 ? 0.70914 0.92457 1.08223 -0.23085 0.10899  0.02537  200 GLU A OE1 
1437 O OE2 . GLU A 193 ? 0.87850 1.18766 1.27428 -0.19942 0.10370  0.01110  200 GLU A OE2 
1438 N N   . ARG A 194 ? 0.51179 0.64523 0.59546 -0.12806 0.11548  0.07727  201 ARG A N   
1439 C CA  . ARG A 194 ? 0.47975 0.63382 0.52496 -0.11027 0.12706  0.07557  201 ARG A CA  
1440 C C   . ARG A 194 ? 0.47085 0.60884 0.45934 -0.08911 0.10010  0.06797  201 ARG A C   
1441 O O   . ARG A 194 ? 0.52791 0.68167 0.49523 -0.07572 0.09805  0.05211  201 ARG A O   
1442 C CB  . ARG A 194 ? 0.53037 0.67791 0.54602 -0.11250 0.16823  0.10291  201 ARG A CB  
1443 C CG  . ARG A 194 ? 0.75790 0.85623 0.71927 -0.10910 0.17268  0.13462  201 ARG A CG  
1444 C CD  . ARG A 194 ? 0.76258 0.85331 0.69285 -0.11088 0.22056  0.16703  201 ARG A CD  
1445 N NE  . ARG A 194 ? 0.85789 0.89817 0.72186 -0.09957 0.22441  0.20333  201 ARG A NE  
1446 C CZ  . ARG A 194 ? 1.00387 1.02596 0.80813 -0.09093 0.26190  0.23880  201 ARG A CZ  
1447 N NH1 . ARG A 194 ? 0.81574 0.86688 0.61915 -0.09390 0.30260  0.24042  201 ARG A NH1 
1448 N NH2 . ARG A 194 ? 1.05188 1.02579 0.79381 -0.07534 0.25921  0.27465  201 ARG A NH2 
1449 N N   . ARG A 195 ? 0.52459 0.63259 0.49553 -0.08615 0.07987  0.07665  202 ARG A N   
1450 C CA  . ARG A 195 ? 0.49199 0.59596 0.42784 -0.06941 0.05274  0.06801  202 ARG A CA  
1451 C C   . ARG A 195 ? 0.44400 0.56306 0.41331 -0.06836 0.03286  0.04275  202 ARG A C   
1452 O O   . ARG A 195 ? 0.44755 0.57460 0.40184 -0.05948 0.02143  0.02768  202 ARG A O   
1453 C CB  . ARG A 195 ? 0.51514 0.59032 0.43167 -0.06246 0.03973  0.08771  202 ARG A CB  
1454 C CG  . ARG A 195 ? 0.45654 0.53938 0.35348 -0.04721 0.01010  0.07900  202 ARG A CG  
1455 C CD  . ARG A 195 ? 0.56705 0.65911 0.40626 -0.03555 0.00592  0.07967  202 ARG A CD  
1456 N NE  . ARG A 195 ? 0.56285 0.66621 0.39091 -0.02368 -0.02751 0.07262  202 ARG A NE  
1457 C CZ  . ARG A 195 ? 0.57474 0.69757 0.40179 -0.02434 -0.04601 0.04467  202 ARG A CZ  
1458 N NH1 . ARG A 195 ? 0.56364 0.68986 0.39202 -0.03146 -0.03317 0.02217  202 ARG A NH1 
1459 N NH2 . ARG A 195 ? 0.51714 0.65647 0.34833 -0.01767 -0.07778 0.03850  202 ARG A NH2 
1460 N N   . ILE A 196 ? 0.39682 0.51604 0.40793 -0.07729 0.02892  0.03762  203 ILE A N   
1461 C CA  . ILE A 196 ? 0.42432 0.55501 0.45742 -0.07252 0.01324  0.01938  203 ILE A CA  
1462 C C   . ILE A 196 ? 0.42685 0.58269 0.47176 -0.06764 0.02059  0.00660  203 ILE A C   
1463 O O   . ILE A 196 ? 0.44413 0.60009 0.48641 -0.05748 0.01167  -0.00438 203 ILE A O   
1464 C CB  . ILE A 196 ? 0.40508 0.53076 0.46743 -0.08025 0.00599  0.01473  203 ILE A CB  
1465 C CG1 . ILE A 196 ? 0.39467 0.48790 0.44347 -0.07902 0.00072  0.02391  203 ILE A CG1 
1466 C CG2 . ILE A 196 ? 0.37331 0.51187 0.44726 -0.07106 -0.00768 0.00042  203 ILE A CG2 
1467 C CD1 . ILE A 196 ? 0.41833 0.49530 0.48824 -0.09022 -0.00126 0.01643  203 ILE A CD1 
1468 N N   . LYS A 197 ? 0.36247 0.53835 0.42551 -0.07394 0.04050  0.00913  204 LYS A N   
1469 C CA  . LYS A 197 ? 0.38740 0.59018 0.46773 -0.06409 0.05108  -0.00268 204 LYS A CA  
1470 C C   . LYS A 197 ? 0.45769 0.64653 0.49311 -0.05076 0.05537  -0.01091 204 LYS A C   
1471 O O   . LYS A 197 ? 0.39788 0.58720 0.43870 -0.03795 0.05237  -0.02579 204 LYS A O   
1472 C CB  . LYS A 197 ? 0.39150 0.62539 0.50751 -0.07359 0.07732  0.00335  204 LYS A CB  
1473 C CG  . LYS A 197 ? 0.53337 0.79565 0.71342 -0.08680 0.06784  -0.00043 204 LYS A CG  
1474 C CD  . LYS A 197 ? 0.48857 0.79536 0.72335 -0.09695 0.09576  0.00296  204 LYS A CD  
1475 C CE  . LYS A 197 ? 0.48832 0.82402 0.79275 -0.11881 0.08220  -0.00316 204 LYS A CE  
1476 N NZ  . LYS A 197 ? 0.70115 1.06359 1.05835 -0.14302 0.11557  0.00797  204 LYS A NZ  
1477 N N   . GLU A 198 ? 0.42313 0.59587 0.41124 -0.05247 0.06080  -0.00218 205 GLU A N   
1478 C CA  . GLU A 198 ? 0.44796 0.60799 0.38600 -0.04137 0.05868  -0.01594 205 GLU A CA  
1479 C C   . GLU A 198 ? 0.46410 0.60860 0.40471 -0.03959 0.03094  -0.03075 205 GLU A C   
1480 O O   . GLU A 198 ? 0.53540 0.66993 0.46382 -0.03268 0.02879  -0.05233 205 GLU A O   
1481 C CB  . GLU A 198 ? 0.48038 0.62925 0.36090 -0.04091 0.06319  -0.00036 205 GLU A CB  
1482 C CG  . GLU A 198 ? 0.59889 0.73581 0.41865 -0.03047 0.04856  -0.01787 205 GLU A CG  
1483 C CD  . GLU A 198 ? 0.76212 0.89039 0.52189 -0.02562 0.04235  0.00276  205 GLU A CD  
1484 O OE1 . GLU A 198 ? 0.68900 0.81180 0.46492 -0.03010 0.03114  0.02588  205 GLU A OE1 
1485 O OE2 . GLU A 198 ? 0.70345 0.82787 0.39511 -0.01389 0.04916  -0.00370 205 GLU A OE2 
1486 N N   . ILE A 199 ? 0.43565 0.57535 0.39553 -0.04621 0.01328  -0.02014 206 ILE A N   
1487 C CA  . ILE A 199 ? 0.35163 0.48099 0.32259 -0.04654 -0.00660 -0.02963 206 ILE A CA  
1488 C C   . ILE A 199 ? 0.38985 0.51529 0.39219 -0.04172 -0.00241 -0.03844 206 ILE A C   
1489 O O   . ILE A 199 ? 0.42778 0.53751 0.43324 -0.04038 -0.00692 -0.05217 206 ILE A O   
1490 C CB  . ILE A 199 ? 0.45823 0.58618 0.44121 -0.05054 -0.01969 -0.01387 206 ILE A CB  
1491 C CG1 . ILE A 199 ? 0.52141 0.64970 0.47113 -0.04890 -0.02696 -0.00221 206 ILE A CG1 
1492 C CG2 . ILE A 199 ? 0.34308 0.46692 0.35040 -0.05171 -0.03196 -0.02019 206 ILE A CG2 
1493 C CD1 . ILE A 199 ? 0.48397 0.60643 0.44601 -0.04780 -0.03152 0.01760  206 ILE A CD1 
1494 N N   . VAL A 200 ? 0.32714 0.46550 0.35426 -0.03880 0.00493  -0.03040 207 VAL A N   
1495 C CA  . VAL A 200 ? 0.33355 0.47062 0.38497 -0.02785 0.00557  -0.03348 207 VAL A CA  
1496 C C   . VAL A 200 ? 0.35707 0.48884 0.40691 -0.01578 0.01853  -0.04796 207 VAL A C   
1497 O O   . VAL A 200 ? 0.44592 0.55372 0.50089 -0.00713 0.01850  -0.05418 207 VAL A O   
1498 C CB  . VAL A 200 ? 0.41899 0.57995 0.49600 -0.02629 0.00324  -0.02519 207 VAL A CB  
1499 C CG1 . VAL A 200 ? 0.30833 0.47623 0.40586 -0.00781 0.00199  -0.02643 207 VAL A CG1 
1500 C CG2 . VAL A 200 ? 0.26687 0.41969 0.33963 -0.03407 -0.00919 -0.01672 207 VAL A CG2 
1501 N N   . LYS A 201 ? 0.35026 0.49958 0.39242 -0.01391 0.03415  -0.05268 208 LYS A N   
1502 C CA  . LYS A 201 ? 0.40739 0.55001 0.44338 0.00143  0.05138  -0.06966 208 LYS A CA  
1503 C C   . LYS A 201 ? 0.47853 0.58197 0.47948 -0.00093 0.04521  -0.09014 208 LYS A C   
1504 O O   . LYS A 201 ? 0.58692 0.66398 0.59045 0.01142  0.05263  -0.10694 208 LYS A O   
1505 C CB  . LYS A 201 ? 0.39699 0.56802 0.42621 0.00321  0.07542  -0.06885 208 LYS A CB  
1506 C CG  . LYS A 201 ? 0.44521 0.60219 0.44067 0.01783  0.09693  -0.09048 208 LYS A CG  
1507 C CD  . LYS A 201 ? 0.53878 0.71845 0.57618 0.04043  0.12016  -0.09481 208 LYS A CD  
1508 C CE  . LYS A 201 ? 0.74762 0.92094 0.74822 0.05651  0.15208  -0.11461 208 LYS A CE  
1509 N NZ  . LYS A 201 ? 0.87473 1.05809 0.91702 0.08607  0.17343  -0.12449 208 LYS A NZ  
1510 N N   . LYS A 202 ? 0.46556 0.56414 0.43815 -0.01636 0.02961  -0.09028 209 LYS A N   
1511 C CA  . LYS A 202 ? 0.48135 0.55257 0.42591 -0.02220 0.01726  -0.11485 209 LYS A CA  
1512 C C   . LYS A 202 ? 0.52618 0.57156 0.50508 -0.02967 0.00558  -0.11861 209 LYS A C   
1513 O O   . LYS A 202 ? 0.60161 0.61344 0.57886 -0.03055 0.00610  -0.14329 209 LYS A O   
1514 C CB  . LYS A 202 ? 0.52332 0.60748 0.43102 -0.03264 -0.00030 -0.11155 209 LYS A CB  
1515 C CG  . LYS A 202 ? 0.59602 0.66360 0.47245 -0.03943 -0.02109 -0.14167 209 LYS A CG  
1516 C CD  . LYS A 202 ? 0.66089 0.74948 0.49634 -0.04223 -0.04170 -0.13331 209 LYS A CD  
1517 C CE  . LYS A 202 ? 0.73077 0.81452 0.54423 -0.05092 -0.07401 -0.16539 209 LYS A CE  
1518 N NZ  . LYS A 202 ? 0.81020 0.92143 0.58903 -0.04840 -0.10031 -0.15164 209 LYS A NZ  
1519 N N   . HIS A 203 ? 0.54518 0.60107 0.55433 -0.03517 -0.00134 -0.09488 210 HIS A N   
1520 C CA  . HIS A 203 ? 0.46191 0.49658 0.50133 -0.04439 -0.00740 -0.09267 210 HIS A CA  
1521 C C   . HIS A 203 ? 0.47259 0.49242 0.53634 -0.03122 0.00582  -0.07394 210 HIS A C   
1522 O O   . HIS A 203 ? 0.53996 0.52950 0.62464 -0.03557 0.01042  -0.07142 210 HIS A O   
1523 C CB  . HIS A 203 ? 0.44691 0.50384 0.49777 -0.05794 -0.02316 -0.07959 210 HIS A CB  
1524 C CG  . HIS A 203 ? 0.55236 0.62495 0.58200 -0.06788 -0.04284 -0.09485 210 HIS A CG  
1525 N ND1 . HIS A 203 ? 0.62645 0.68586 0.65508 -0.07960 -0.05608 -0.12414 210 HIS A ND1 
1526 C CD2 . HIS A 203 ? 0.51105 0.60958 0.51687 -0.06608 -0.05379 -0.08463 210 HIS A CD2 
1527 C CE1 . HIS A 203 ? 0.60558 0.68914 0.60677 -0.08277 -0.07846 -0.13211 210 HIS A CE1 
1528 N NE2 . HIS A 203 ? 0.65476 0.76034 0.64053 -0.07280 -0.07565 -0.10507 210 HIS A NE2 
1529 N N   . SER A 204 ? 0.50395 0.50832 0.35959 -0.05241 -0.15905 0.04152  211 SER A N   
1530 C CA  . SER A 204 ? 0.54441 0.55344 0.43529 -0.03107 -0.12874 0.02897  211 SER A CA  
1531 C C   . SER A 204 ? 0.46137 0.45841 0.30729 -0.01889 -0.09925 0.00886  211 SER A C   
1532 O O   . SER A 204 ? 0.56533 0.57304 0.43618 -0.00142 -0.07649 0.00528  211 SER A O   
1533 C CB  . SER A 204 ? 0.50476 0.54092 0.46041 -0.01904 -0.12121 0.04505  211 SER A CB  
1534 O OG  . SER A 204 ? 0.51868 0.56877 0.52696 -0.02796 -0.14680 0.06504  211 SER A OG  
1535 N N   . GLN A 205 ? 0.54431 0.52006 0.32528 -0.02920 -0.09907 -0.00483 212 GLN A N   
1536 C CA  . GLN A 205 ? 0.62507 0.59321 0.37319 -0.01641 -0.06761 -0.02426 212 GLN A CA  
1537 C C   . GLN A 205 ? 0.63258 0.59085 0.40705 0.00222  -0.04891 -0.03940 212 GLN A C   
1538 O O   . GLN A 205 ? 0.67558 0.64403 0.46132 0.02020  -0.02501 -0.04451 212 GLN A O   
1539 C CB  . GLN A 205 ? 0.67096 0.61310 0.34282 -0.03327 -0.06649 -0.04157 212 GLN A CB  
1540 C CG  . GLN A 205 ? 0.81302 0.74488 0.45877 -0.01907 -0.02907 -0.06692 212 GLN A CG  
1541 C CD  . GLN A 205 ? 0.91758 0.82900 0.48302 -0.03816 -0.02023 -0.08382 212 GLN A CD  
1542 O OE1 . GLN A 205 ? 1.08962 1.00938 0.63500 -0.03184 0.01032  -0.09297 212 GLN A OE1 
1543 N NE2 . GLN A 205 ? 0.93714 0.82235 0.45462 -0.06425 -0.04611 -0.08884 212 GLN A NE2 
1544 N N   . PHE A 206 ? 0.70116 0.64133 0.49008 -0.00311 -0.06168 -0.04311 213 PHE A N   
1545 C CA  . PHE A 206 ? 0.59808 0.51954 0.40317 0.01063  -0.04721 -0.05534 213 PHE A CA  
1546 C C   . PHE A 206 ? 0.56253 0.50168 0.42227 0.01859  -0.04734 -0.03942 213 PHE A C   
1547 O O   . PHE A 206 ? 0.63705 0.55879 0.51022 0.02507  -0.04130 -0.04315 213 PHE A O   
1548 C CB  . PHE A 206 ? 0.58999 0.47112 0.36720 -0.00359 -0.05758 -0.07281 213 PHE A CB  
1549 C CG  . PHE A 206 ? 0.67415 0.53063 0.38655 -0.01352 -0.05169 -0.09533 213 PHE A CG  
1550 C CD1 . PHE A 206 ? 0.64151 0.49995 0.33494 0.00222  -0.02209 -0.10858 213 PHE A CD1 
1551 C CD2 . PHE A 206 ? 0.73799 0.57102 0.40777 -0.04108 -0.07495 -0.10372 213 PHE A CD2 
1552 C CE1 . PHE A 206 ? 0.74259 0.57809 0.37287 -0.00857 -0.00971 -0.13242 213 PHE A CE1 
1553 C CE2 . PHE A 206 ? 0.81782 0.62495 0.41556 -0.05454 -0.06713 -0.12736 213 PHE A CE2 
1554 C CZ  . PHE A 206 ? 0.82208 0.62959 0.39834 -0.03798 -0.03143 -0.14299 213 PHE A CZ  
1555 N N   . ILE A 207 ? 0.50759 0.47780 0.39726 0.01705  -0.05240 -0.02209 214 ILE A N   
1556 C CA  . ILE A 207 ? 0.51433 0.50100 0.44727 0.02333  -0.04510 -0.01162 214 ILE A CA  
1557 C C   . ILE A 207 ? 0.47721 0.46557 0.40723 0.04027  -0.02613 -0.01509 214 ILE A C   
1558 O O   . ILE A 207 ? 0.54115 0.53963 0.45736 0.04927  -0.01670 -0.01865 214 ILE A O   
1559 C CB  . ILE A 207 ? 0.42865 0.44437 0.39351 0.01999  -0.04888 0.00235  214 ILE A CB  
1560 C CG1 . ILE A 207 ? 0.41580 0.43320 0.39919 0.00424  -0.07233 0.01112  214 ILE A CG1 
1561 C CG2 . ILE A 207 ? 0.35188 0.38245 0.35119 0.02515  -0.03416 0.00705  214 ILE A CG2 
1562 C CD1 . ILE A 207 ? 0.41624 0.42880 0.43233 -0.00406 -0.07699 0.01250  214 ILE A CD1 
1563 N N   . GLY A 208 ? 0.49601 0.47611 0.44115 0.04291  -0.02188 -0.01139 215 GLY A N   
1564 C CA  . GLY A 208 ? 0.45183 0.43093 0.39600 0.05739  -0.01109 -0.00998 215 GLY A CA  
1565 C C   . GLY A 208 ? 0.51148 0.51954 0.46907 0.06018  -0.00426 0.00004  215 GLY A C   
1566 O O   . GLY A 208 ? 0.54072 0.54869 0.50106 0.06517  -0.00174 0.00779  215 GLY A O   
1567 N N   . TYR A 209 ? 0.46494 0.49526 0.42968 0.05516  -0.00309 0.00085  216 TYR A N   
1568 C CA  . TYR A 209 ? 0.45667 0.51085 0.43052 0.05512  0.00423  0.00540  216 TYR A CA  
1569 C C   . TYR A 209 ? 0.39847 0.46921 0.37196 0.05683  0.00571  0.00319  216 TYR A C   
1570 O O   . TYR A 209 ? 0.41940 0.48488 0.38741 0.05343  -0.00022 0.00179  216 TYR A O   
1571 C CB  . TYR A 209 ? 0.40402 0.46355 0.39528 0.04312  0.00917  0.00827  216 TYR A CB  
1572 C CG  . TYR A 209 ? 0.45564 0.49976 0.44427 0.03750  0.01048  0.01288  216 TYR A CG  
1573 C CD1 . TYR A 209 ? 0.38638 0.42960 0.35935 0.03713  0.01343  0.01975  216 TYR A CD1 
1574 C CD2 . TYR A 209 ? 0.38856 0.41901 0.39014 0.03011  0.00612  0.01324  216 TYR A CD2 
1575 C CE1 . TYR A 209 ? 0.44043 0.46674 0.40684 0.02960  0.01403  0.02827  216 TYR A CE1 
1576 C CE2 . TYR A 209 ? 0.39634 0.41142 0.39653 0.02247  0.00858  0.01932  216 TYR A CE2 
1577 C CZ  . TYR A 209 ? 0.39576 0.40725 0.37627 0.02235  0.01350  0.02755  216 TYR A CZ  
1578 O OH  . TYR A 209 ? 0.44162 0.43526 0.41668 0.01236  0.01548  0.03787  216 TYR A OH  
1579 N N   . PRO A 210 ? 0.43183 0.52205 0.40871 0.05930  0.01155  0.00468  217 PRO A N   
1580 C CA  . PRO A 210 ? 0.34317 0.44844 0.32171 0.05846  0.01427  0.00460  217 PRO A CA  
1581 C C   . PRO A 210 ? 0.36794 0.47351 0.36207 0.04867  0.01220  0.00766  217 PRO A C   
1582 O O   . PRO A 210 ? 0.41049 0.51686 0.42165 0.04313  0.01635  0.00654  217 PRO A O   
1583 C CB  . PRO A 210 ? 0.33609 0.46264 0.32129 0.06016  0.01884  0.00610  217 PRO A CB  
1584 C CG  . PRO A 210 ? 0.38929 0.51162 0.37282 0.05738  0.01643  0.00832  217 PRO A CG  
1585 C CD  . PRO A 210 ? 0.33915 0.43800 0.31595 0.06089  0.01298  0.00867  217 PRO A CD  
1586 N N   . ILE A 211 ? 0.34869 0.45238 0.33744 0.04599  0.00662  0.01204  218 ILE A N   
1587 C CA  . ILE A 211 ? 0.34340 0.44699 0.35432 0.03846  0.00046  0.02056  218 ILE A CA  
1588 C C   . ILE A 211 ? 0.43723 0.55151 0.44771 0.03539  0.00483  0.02613  218 ILE A C   
1589 O O   . ILE A 211 ? 0.41720 0.53424 0.40148 0.03472  0.00536  0.02877  218 ILE A O   
1590 C CB  . ILE A 211 ? 0.39589 0.48745 0.40063 0.03334  -0.01660 0.02795  218 ILE A CB  
1591 C CG1 . ILE A 211 ? 0.42093 0.50125 0.42602 0.03395  -0.02080 0.02165  218 ILE A CG1 
1592 C CG2 . ILE A 211 ? 0.30390 0.39749 0.34527 0.02743  -0.02711 0.04216  218 ILE A CG2 
1593 C CD1 . ILE A 211 ? 0.32715 0.39551 0.32290 0.02510  -0.04147 0.02712  218 ILE A CD1 
1594 N N   . THR A 212 ? 0.35151 0.46994 0.39029 0.03176  0.01071  0.02636  219 THR A N   
1595 C CA  . THR A 212 ? 0.39608 0.52169 0.44011 0.02613  0.01493  0.03190  219 THR A CA  
1596 C C   . THR A 212 ? 0.29783 0.41223 0.37112 0.02092  0.00693  0.04549  219 THR A C   
1597 O O   . THR A 212 ? 0.34214 0.44881 0.45139 0.02225  0.00849  0.04235  219 THR A O   
1598 C CB  . THR A 212 ? 0.38607 0.52127 0.43935 0.02312  0.02656  0.02041  219 THR A CB  
1599 O OG1 . THR A 212 ? 0.41493 0.56139 0.44803 0.02869  0.02855  0.01328  219 THR A OG1 
1600 C CG2 . THR A 212 ? 0.34967 0.49315 0.40928 0.01475  0.03020  0.02592  219 THR A CG2 
1601 N N   . LEU A 213 ? 0.41170 0.52514 0.47214 0.01468  -0.00044 0.06181  220 LEU A N   
1602 C CA  . LEU A 213 ? 0.42325 0.52460 0.51245 0.00897  -0.01254 0.08201  220 LEU A CA  
1603 C C   . LEU A 213 ? 0.44839 0.54824 0.55784 0.00250  -0.00182 0.08374  220 LEU A C   
1604 O O   . LEU A 213 ? 0.47963 0.58749 0.56406 -0.00544 0.00262  0.09019  220 LEU A O   
1605 C CB  . LEU A 213 ? 0.39698 0.49425 0.45135 0.00107  -0.03070 0.10321  220 LEU A CB  
1606 C CG  . LEU A 213 ? 0.55385 0.63839 0.63458 -0.00685 -0.05009 0.13288  220 LEU A CG  
1607 C CD1 . LEU A 213 ? 0.42148 0.49883 0.56891 0.00151  -0.05976 0.13658  220 LEU A CD1 
1608 C CD2 . LEU A 213 ? 0.61056 0.69095 0.63953 -0.01984 -0.07093 0.15442  220 LEU A CD2 
1609 N N   . PHE A 214 ? 0.36830 0.45692 0.52471 0.00443  0.00477  0.07626  221 PHE A N   
1610 C CA  . PHE A 214 ? 0.45279 0.53276 0.63181 -0.00384 0.01480  0.07462  221 PHE A CA  
1611 C C   . PHE A 214 ? 0.42857 0.49491 0.62154 -0.01097 0.00077  0.10541  221 PHE A C   
1612 O O   . PHE A 214 ? 0.50572 0.55901 0.73086 -0.00640 -0.01468 0.12362  221 PHE A O   
1613 C CB  . PHE A 214 ? 0.36998 0.43490 0.59355 -0.00076 0.02894  0.05427  221 PHE A CB  
1614 C CG  . PHE A 214 ? 0.36151 0.43680 0.56220 -0.00155 0.04460  0.02514  221 PHE A CG  
1615 C CD1 . PHE A 214 ? 0.45428 0.54739 0.61798 0.00395  0.04097  0.02134  221 PHE A CD1 
1616 C CD2 . PHE A 214 ? 0.42783 0.49138 0.64166 -0.00989 0.06191  0.00211  221 PHE A CD2 
1617 C CE1 . PHE A 214 ? 0.45822 0.55922 0.60007 0.00167  0.05142  0.00063  221 PHE A CE1 
1618 C CE2 . PHE A 214 ? 0.56025 0.63254 0.74393 -0.01502 0.07269  -0.02143 221 PHE A CE2 
1619 C CZ  . PHE A 214 ? 0.40811 0.50011 0.55669 -0.00892 0.06595  -0.01937 221 PHE A CZ  
1620 N N   . VAL A 215 ? 0.37995 0.45061 0.55260 -0.02339 0.00475  0.11424  222 VAL A N   
1621 C CA  . VAL A 215 ? 0.39187 0.44697 0.57325 -0.03431 -0.00719 0.14665  222 VAL A CA  
1622 C C   . VAL A 215 ? 0.42987 0.45998 0.66716 -0.03815 0.00004  0.14426  222 VAL A C   
1623 O O   . VAL A 215 ? 0.49729 0.52877 0.74363 -0.04082 0.01792  0.11625  222 VAL A O   
1624 C CB  . VAL A 215 ? 0.46593 0.53856 0.59612 -0.04847 -0.00228 0.15803  222 VAL A CB  
1625 C CG1 . VAL A 215 ? 0.39820 0.49725 0.51321 -0.04792 0.01778  0.12975  222 VAL A CG1 
1626 C CG2 . VAL A 215 ? 0.42455 0.48063 0.56753 -0.06565 -0.00557 0.18651  222 VAL A CG2 
1627 N N   . GLU A 216 ? 0.41167 0.41627 0.68760 -0.03933 -0.01520 0.17339  223 GLU A N   
1628 C CA  . GLU A 216 ? 0.52602 0.49939 0.86302 -0.04123 -0.00700 0.17029  223 GLU A CA  
1629 C C   . GLU A 216 ? 0.51105 0.47676 0.83647 -0.06197 -0.00080 0.18079  223 GLU A C   
1630 O O   . GLU A 216 ? 0.53102 0.51584 0.80686 -0.07489 -0.00437 0.19860  223 GLU A O   
1631 C CB  . GLU A 216 ? 0.51924 0.46656 0.91771 -0.03178 -0.02677 0.19997  223 GLU A CB  
1632 C CG  . GLU A 216 ? 0.59477 0.54736 1.03224 -0.01172 -0.02689 0.18465  223 GLU A CG  
1633 C CD  . GLU A 216 ? 0.63548 0.57663 1.12878 -0.00276 -0.05622 0.22374  223 GLU A CD  
1634 O OE1 . GLU A 216 ? 0.72038 0.67855 1.17582 -0.00639 -0.08375 0.25099  223 GLU A OE1 
1635 O OE2 . GLU A 216 ? 0.59586 0.50965 1.17259 0.00666  -0.05336 0.22863  223 GLU A OE2 
1636 N N   . LYS A 217 ? 0.62927 0.56500 1.00370 -0.06651 0.01115  0.16798  224 LYS A N   
1637 C CA  . LYS A 217 ? 0.62918 0.55295 1.00378 -0.08869 0.01790  0.17483  224 LYS A CA  
1638 C C   . LYS A 217 ? 0.58680 0.46506 1.01777 -0.09240 0.00655  0.20800  224 LYS A C   
1639 O O   . LYS A 217 ? 0.68977 0.56351 1.11716 -0.09248 -0.01604 0.25192  224 LYS A O   
1640 C CB  . LYS A 217 ? 0.50298 0.42580 0.88242 -0.09702 0.04009  0.12981  224 LYS A CB  
1641 C CG  . LYS A 217 ? 0.49241 0.44480 0.84101 -0.08566 0.04919  0.09400  224 LYS A CG  
1642 C CD  . LYS A 217 ? 0.45794 0.40235 0.80918 -0.09733 0.06732  0.05118  224 LYS A CD  
1643 C CE  . LYS A 217 ? 0.48146 0.38300 0.88154 -0.08918 0.08157  0.02685  224 LYS A CE  
1644 N NZ  . LYS A 217 ? 0.54865 0.46211 0.94201 -0.07026 0.08880  0.00686  224 LYS A NZ  
# 
