data_7HBM
# 
_entry.id   7HBM 
# 
_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   7HBM         pdb_00007hbm 10.2210/pdb7hbm/pdb 
WWPDB D_1001407268 ?            ?                   
# 
_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                        7HBM 
_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-cycloheptyl-N'-(2-hydroxyethyl)thiourea" 216.344   1  ?        ? ? ? 
3 water       nat water                                       18.015    95 ?        ? ? ? 
# 
_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-cycloheptyl-N'-(2-hydroxyethyl)thiourea" A1AYJ 
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 
A1AYJ non-polymer         . "N-cycloheptyl-N'-(2-hydroxyethyl)thiourea" ? 'C10 H20 N2 O S' 216.344 
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        A1AYJ 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1AYJ 
_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 A1AYJ 1  301 301 A1AYJ C0U A . 
C 3 HOH   1  401 86  HOH   HOH A . 
C 3 HOH   2  402 82  HOH   HOH A . 
C 3 HOH   3  403 66  HOH   HOH A . 
C 3 HOH   4  404 22  HOH   HOH A . 
C 3 HOH   5  405 83  HOH   HOH A . 
C 3 HOH   6  406 29  HOH   HOH A . 
C 3 HOH   7  407 31  HOH   HOH A . 
C 3 HOH   8  408 15  HOH   HOH A . 
C 3 HOH   9  409 28  HOH   HOH A . 
C 3 HOH   10 410 6   HOH   HOH A . 
C 3 HOH   11 411 9   HOH   HOH A . 
C 3 HOH   12 412 16  HOH   HOH A . 
C 3 HOH   13 413 74  HOH   HOH A . 
C 3 HOH   14 414 2   HOH   HOH A . 
C 3 HOH   15 415 33  HOH   HOH A . 
C 3 HOH   16 416 3   HOH   HOH A . 
C 3 HOH   17 417 35  HOH   HOH A . 
C 3 HOH   18 418 5   HOH   HOH A . 
C 3 HOH   19 419 13  HOH   HOH A . 
C 3 HOH   20 420 78  HOH   HOH A . 
C 3 HOH   21 421 65  HOH   HOH A . 
C 3 HOH   22 422 75  HOH   HOH A . 
C 3 HOH   23 423 25  HOH   HOH A . 
C 3 HOH   24 424 30  HOH   HOH A . 
C 3 HOH   25 425 32  HOH   HOH A . 
C 3 HOH   26 426 11  HOH   HOH A . 
C 3 HOH   27 427 24  HOH   HOH A . 
C 3 HOH   28 428 80  HOH   HOH A . 
C 3 HOH   29 429 26  HOH   HOH A . 
C 3 HOH   30 430 7   HOH   HOH A . 
C 3 HOH   31 431 44  HOH   HOH A . 
C 3 HOH   32 432 79  HOH   HOH A . 
C 3 HOH   33 433 73  HOH   HOH A . 
C 3 HOH   34 434 58  HOH   HOH A . 
C 3 HOH   35 435 50  HOH   HOH A . 
C 3 HOH   36 436 77  HOH   HOH A . 
C 3 HOH   37 437 4   HOH   HOH A . 
C 3 HOH   38 438 36  HOH   HOH A . 
C 3 HOH   39 439 1   HOH   HOH A . 
C 3 HOH   40 440 37  HOH   HOH A . 
C 3 HOH   41 441 84  HOH   HOH A . 
C 3 HOH   42 442 20  HOH   HOH A . 
C 3 HOH   43 443 19  HOH   HOH A . 
C 3 HOH   44 444 8   HOH   HOH A . 
C 3 HOH   45 445 14  HOH   HOH A . 
C 3 HOH   46 446 61  HOH   HOH A . 
C 3 HOH   47 447 27  HOH   HOH A . 
C 3 HOH   48 448 18  HOH   HOH A . 
C 3 HOH   49 449 38  HOH   HOH A . 
C 3 HOH   50 450 81  HOH   HOH A . 
C 3 HOH   51 451 89  HOH   HOH A . 
C 3 HOH   52 452 17  HOH   HOH A . 
C 3 HOH   53 453 54  HOH   HOH A . 
C 3 HOH   54 454 23  HOH   HOH A . 
C 3 HOH   55 455 59  HOH   HOH A . 
C 3 HOH   56 456 41  HOH   HOH A . 
C 3 HOH   57 457 70  HOH   HOH A . 
C 3 HOH   58 458 43  HOH   HOH A . 
C 3 HOH   59 459 88  HOH   HOH A . 
C 3 HOH   60 460 34  HOH   HOH A . 
C 3 HOH   61 461 64  HOH   HOH A . 
C 3 HOH   62 462 10  HOH   HOH A . 
C 3 HOH   63 463 21  HOH   HOH A . 
C 3 HOH   64 464 45  HOH   HOH A . 
C 3 HOH   65 465 39  HOH   HOH A . 
C 3 HOH   66 466 42  HOH   HOH A . 
C 3 HOH   67 467 55  HOH   HOH A . 
C 3 HOH   68 468 94  HOH   HOH A . 
C 3 HOH   69 469 63  HOH   HOH A . 
C 3 HOH   70 470 57  HOH   HOH A . 
C 3 HOH   71 471 69  HOH   HOH A . 
C 3 HOH   72 472 87  HOH   HOH A . 
C 3 HOH   73 473 90  HOH   HOH A . 
C 3 HOH   74 474 93  HOH   HOH A . 
C 3 HOH   75 475 47  HOH   HOH A . 
C 3 HOH   76 476 85  HOH   HOH A . 
C 3 HOH   77 477 71  HOH   HOH A . 
C 3 HOH   78 478 46  HOH   HOH A . 
C 3 HOH   79 479 12  HOH   HOH A . 
C 3 HOH   80 480 48  HOH   HOH A . 
C 3 HOH   81 481 40  HOH   HOH A . 
C 3 HOH   82 482 95  HOH   HOH A . 
C 3 HOH   83 483 67  HOH   HOH A . 
C 3 HOH   84 484 52  HOH   HOH A . 
C 3 HOH   85 485 49  HOH   HOH A . 
C 3 HOH   86 486 51  HOH   HOH A . 
C 3 HOH   87 487 68  HOH   HOH A . 
C 3 HOH   88 488 60  HOH   HOH A . 
C 3 HOH   89 489 91  HOH   HOH A . 
C 3 HOH   90 490 76  HOH   HOH A . 
C 3 HOH   91 491 56  HOH   HOH A . 
C 3 HOH   92 492 62  HOH   HOH A . 
C 3 HOH   93 493 72  HOH   HOH A . 
C 3 HOH   94 494 92  HOH   HOH A . 
C 3 HOH   95 495 53  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             602306.171 
_cell.length_a           69.826 
_cell.length_b           88.732 
_cell.length_c           97.212 
_cell.angle_beta         90.000 
_cell.angle_gamma        90.000 
_cell.angle_alpha        90.000 
_cell.entry_id           7HBM 
_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                         7HBM 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
# 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
_exptl.entry_id          7HBM 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_Matthews      2.88 
_exptl_crystal.density_percent_sol   57.23 
_exptl_crystal.density_meas          ? 
_exptl_crystal.description           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.pH              8.5 
_exptl_crystal_grow.temp            277 
_exptl_crystal_grow.pdbx_details    '100mM Tris-HCl pH 8.5, 22% PEG4000, 200mM MgCl2' 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_diffrn.id                     1 
_diffrn.crystal_id             1 
_diffrn.ambient_temp           100 
_diffrn.ambient_temp_details   ? 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               PIXEL 
_diffrn_detector.type                   'DECTRIS EIGER X 16M' 
_diffrn_detector.pdbx_collection_date   2024-01-20 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.pdbx_scattering_type             x-ray 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.monochromator                    Si111 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.97918 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.pdbx_synchrotron_beamline   BL10U2 
_diffrn_source.type                        'SSRF BEAMLINE BL10U2' 
_diffrn_source.pdbx_wavelength_list        0.97918 
_diffrn_source.pdbx_synchrotron_site       SSRF 
_diffrn_source.pdbx_wavelength             ? 
# 
_reflns.entry_id                     7HBM 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             65.540 
_reflns.d_resolution_high            2.210 
_reflns.number_obs                   15370 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         99.500 
_reflns.pdbx_Rmerge_I_obs            0.168 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        10.300 
_reflns.B_iso_Wilson_estimate        ? 
_reflns.pdbx_redundancy              12.800 
_reflns.pdbx_Rrim_I_all              0.175 
_reflns.pdbx_Rpim_I_all              0.049 
_reflns.pdbx_CC_half                 0.995 
_reflns.pdbx_netI_over_av_sigmaI     ? 
_reflns.pdbx_number_measured_all     196982 
_reflns.pdbx_scaling_rejects         3502 
_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 2.210 2.270  ? 14565 1114 ? 2.151 ? ? ? 13.100 ? 1.500  ? ? ? ? ? ? 99.000 2.239 0.616 0.615 
1 2 9.880 65.540 ? 1855  210  ? 0.046 ? ? ? 8.800  ? 21.600 ? ? ? ? ? ? 99.800 0.050 0.017 0.990 
# 
_refine.entry_id                                 7HBM 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.ls_percent_reflns_R_free                 4.64 
_refine.pdbx_overall_phase_error                 28.0289 
_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                          0.2038 
_refine.B_iso_mean                               47.54 
_refine.ls_number_reflns_R_free                  712 
_refine.ls_percent_reflns_obs                    99.08 
_refine.ls_R_factor_R_work                       0.2020 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_refine.ls_d_res_high                            2.21 
_refine.ls_number_reflns_obs                     15340 
_refine.pdbx_ls_sigma_F                          1.35 
_refine.ls_number_reflns_R_work                  14628 
_refine.ls_d_res_low                             65.54 
_refine.pdbx_stereochemistry_target_values       'GeoStd + Monomer Library + CDL v1.2' 
_refine.ls_R_factor_R_free                       0.2385 
_refine.overall_SU_ML                            0.2645 
_refine.pdbx_solvent_vdw_probe_radii             1.1000 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.solvent_model_param_ksol                 ? 
_refine.solvent_model_param_bsol                 ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.details                                  ? 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.overall_SU_B                             ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        1644 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         14 
_refine_hist.number_atoms_solvent             95 
_refine_hist.number_atoms_total               1753 
_refine_hist.d_res_high                       2.21 
_refine_hist.d_res_low                        65.54 
# 
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           1684 0.0031 ? ? ? 
'X-RAY DIFFRACTION' f_angle_d          2267 0.6161 ? ? ? 
'X-RAY DIFFRACTION' f_chiral_restr     260  0.0440 ? ? ? 
'X-RAY DIFFRACTION' f_plane_restr      288  0.0039 ? ? ? 
'X-RAY DIFFRACTION' f_dihedral_angle_d 234  6.4767 ? ? ? 
# 
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' 2.21 2.38  2860 0.2770 98.55 0.3296 123 . . . . . 
'X-RAY DIFFRACTION' 2.38 2.62  2882 0.2572 98.89 0.3062 139 . . . . . 
'X-RAY DIFFRACTION' 2.62 3.00  2922 0.2541 99.06 0.3053 134 . . . . . 
'X-RAY DIFFRACTION' 3.00 3.78  2901 0.1984 99.45 0.2466 170 . . . . . 
'X-RAY DIFFRACTION' 3.78 65.54 3063 0.1632 99.41 0.1841 146 . . . . . 
# 
_struct.entry_id                  7HBM 
_struct.title                     'PanDDA analysis group deposition -- Crystal structure of HSP90N in complex with Fr13278' 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_details        ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HBM 
_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              7HBM 
_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 7HBM MET A 1   ? UNP P07900 ? ? 'initiating methionine' 8   1 
1 7HBM LEU A 230 ? UNP P07900 ? ? 'expression tag'        237 2 
1 7HBM GLU A 231 ? UNP P07900 ? ? 'expression tag'        238 3 
1 7HBM HIS A 232 ? UNP P07900 ? ? 'expression tag'        239 4 
1 7HBM HIS A 233 ? UNP P07900 ? ? 'expression tag'        240 5 
1 7HBM HIS A 234 ? UNP P07900 ? ? 'expression tag'        241 6 
1 7HBM HIS A 235 ? UNP P07900 ? ? 'expression tag'        242 7 
1 7HBM HIS A 236 ? UNP P07900 ? ? 'expression tag'        243 8 
1 7HBM 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  ? LEU A 115 ? ASN A 105 LEU A 122 1 ? 18 
HELX_P HELX_P6 AA6 ASP A 120 ? GLY A 128 ? ASP A 127 GLY A 135 5 ? 9  
HELX_P HELX_P7 AA7 VAL A 129 ? LEU A 136 ? VAL A 136 LEU A 143 5 ? 8  
HELX_P HELX_P8 AA8 GLN A 187 ? LEU A 191 ? GLN A 194 LEU A 198 5 ? 5  
HELX_P HELX_P9 AA9 GLU A 192 ? SER A 204 ? GLU A 199 SER A 211 1 ? 13 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
_struct_sheet.id               AA1 
_struct_sheet.type             ? 
_struct_sheet.number_strands   8 
_struct_sheet.details          ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA1 5 6 ? anti-parallel 
AA1 6 7 ? anti-parallel 
AA1 7 8 ? parallel      
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 VAL A 10  ? ALA A 14  ? VAL A 17  ALA A 21  
AA1 2 SER A 162 ? THR A 167 ? SER A 169 THR A 174 
AA1 3 TYR A 153 ? SER A 157 ? TYR A 160 SER A 164 
AA1 4 ALA A 138 ? LYS A 146 ? ALA A 145 LYS A 153 
AA1 5 GLY A 176 ? LEU A 183 ? GLY A 183 LEU A 190 
AA1 6 THR A 81  ? ASP A 86  ? THR A 88  ASP A 93  
AA1 7 ILE A 71  ? ASN A 76  ? ILE A 78  ASN A 83  
AA1 8 ILE A 211 ? LEU A 213 ? ILE A 218 LEU A 220 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N PHE A 13  ? N PHE A 20  O PHE A 163 ? O PHE A 170 
AA1 2 3 O ARG A 166 ? O ARG A 173 N ALA A 154 ? N ALA A 161 
AA1 3 4 O TRP A 155 ? O TRP A 162 N VAL A 143 ? N VAL A 150 
AA1 4 5 N THR A 142 ? N THR A 149 O ILE A 180 ? O ILE A 187 
AA1 5 6 O LEU A 181 ? O LEU A 188 N LEU A 82  ? N LEU A 89  
AA1 6 7 O THR A 83  ? O THR A 90  N ILE A 74  ? N ILE A 81  
AA1 7 8 N LEU A 73  ? N LEU A 80  O THR A 212 ? O THR A 219 
# 
_pdbx_entry_details.entry_id                   7HBM 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 O   A HOH 486 ? ? O A HOH 492 ? ? 1.93 
2 1 O   A PHE 37  ? ? O A HOH 401 ? ? 2.06 
3 1 NE2 A GLN 133 ? ? O A HOH 402 ? ? 2.06 
4 1 O   A LYS 224 ? ? O A HOH 403 ? ? 2.13 
5 1 O   A THR 36  ? ? O A HOH 404 ? ? 2.17 
6 1 OG1 A THR 36  ? ? O A HOH 404 ? ? 2.18 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ASP A 66  ? ? -153.86 82.91   
2 1 ASN A 105 ? ? -125.85 -59.27  
3 1 ALA A 166 ? ? 59.84   -149.41 
4 1 ARG A 182 ? ? -172.58 139.22  
# 
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 13.8332507439  27.1874278308 31.096832565  0.384822608648 0.356821799433 0.422366391276 
0.0610134838191   -0.0782455524075 0.0424734116236  4.15240460163 2.37400423478 4.2701034743  -0.642331309923 -1.22703320563  
0.828570116381  -0.069231367818   -0.416419072501  -0.0710282396132 0.337341860811   -0.133000241859  -0.264273143525  
-0.00225649236708 0.437491803234   0.0832895699927   
2  ? 'X-RAY DIFFRACTION' refined -3.97594653514 37.2193714678 27.4637697569 0.339151180197 0.300626968516 0.356221877598 
-0.0272231881003  -0.0323341689277 -0.0358784429195 2.21946987568 4.31801386124 4.14946576563 -1.14737507679  0.480097079748  
-3.0100147045   0.0510427095517   -0.0965844051069 0.0751722973925  0.44843721772    0.129553336039   0.237335368353   
-0.590259633804   0.22531076836    -0.0269026738435  
3  ? 'X-RAY DIFFRACTION' refined -12.1690434248 37.811043294  12.5035253087 0.44247674212  0.552147242006 0.421553328082 
-0.00412371910096 -0.117678191159  0.0733447851943  2.18547201052 2.06961086163 2.98216193914 -1.49181939308  0.376443223578  
1.49931710694   0.162469388829    0.769123854235   -0.163876511051  -0.916821132163  0.328765193665   0.496615370121   
0.361862381075    -1.25126134976   -0.1403297768     
4  ? 'X-RAY DIFFRACTION' refined -2.74531844719 25.8181552214 24.9783340278 0.331312312653 0.282353745838 0.331502800224 
0.0151100444695   -0.0456671441407 -0.0023881688154 2.70845176215 1.7988487138  2.48099767411 -0.309809792891 -1.02492622566  
-0.535071269197 -0.00559816804517 -0.228441056772  -0.0635590244354 -0.0772467002643 0.0253558081056  0.139287383925   
0.385941390932    0.059936901732   -0.00984303391756 
5  ? 'X-RAY DIFFRACTION' refined 12.492363789   38.9892187319 34.062192671  0.430250597671 0.450577506468 0.489018726428 
-0.0809206015731  -0.0766800887979 -0.0571860891815 8.61577067677 7.33772245718 5.14214094173 0.826973049833  0.0740595852077 
-1.97954860028  0.307655552233    -1.08710994105   0.727594922873   0.893110925397   -0.28073559231   -0.548164706743  
-0.678059761505   1.0944775365     0.0780829384313   
6  ? 'X-RAY DIFFRACTION' refined 4.47707148955  25.4569421454 28.6376614354 0.320304249476 0.32743399886  0.337153665694 
0.0132615212119   -0.0423918479643 0.00138397199013 2.40955340478 1.80234943013 4.43592353151 -0.305711010355 0.850415521087  
0.661558034444  0.0207433289678   -0.16551944358   -0.150689355457  0.138018578602   -0.0556180588917 -0.23544410103   
0.621063977762    0.464659219959   0.0128305133182   
7  ? 'X-RAY DIFFRACTION' refined 2.44688512402  27.3427662623 14.8758103236 0.485865960703 0.377212398191 0.38681381035  
0.0238354953491   -0.0587689750241 -0.0235391528696 4.85124447742 3.00085068103 4.24383815978 -1.43608007854  2.1730584133    
-0.739272721269 0.159445642135    0.602360643381   0.017165759711   -0.586340491059  -0.275152488323  -0.103999426295  
0.482001916918    0.316716538827   -0.055337155667   
8  ? 'X-RAY DIFFRACTION' refined 1.87687854256  22.5919534959 20.9304584626 0.428761161556 0.313104379539 0.399767012633 
0.0169829386347   -0.0271590736389 -0.0801369559384 2.65371705511 2.35131155398 1.69826379217 -0.54041912626  -0.341881745509 
-1.50622669     -0.0172029483436  0.241945282822   -0.527731233969  -0.170387234061  0.0778952572019  0.0600341614347  
0.465774465039    0.0919102228878  -0.0350610991944  
9  ? 'X-RAY DIFFRACTION' refined -5.67668103882 24.4592015381 41.5375679783 0.506534632121 0.515131655179 0.341660008379 
-0.0191572924821  -0.0160759487658 0.119791845086   6.07835757774 3.86211575513 4.25627298254 -1.8557511316   -0.226505297324 
-0.060817981137 -0.215274110617   -0.4718087298    -0.369700280927  0.866950696583   0.064560407453   -0.0837675116452 
-0.04494426882    -0.0261146756595 -0.0495618761422  
10 ? 'X-RAY DIFFRACTION' refined -12.9669867431 30.3880623374 32.635437276  0.493975613337 0.464179607651 0.45955201164  
0.026643152836    0.0137159395221  0.00752702622547 3.44316446792 3.00263578812 3.88332865575 -0.318570598044 0.106599783328  
-1.11354219334  -0.0289459189333  -0.442203650659  -0.225577386294  0.752287580608   0.0934142943482  -0.47671753376   
-0.305938042897   -0.558238637235  -0.0996254492275  
# 
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 64  A 49  . 
;chain 'A' and (resid 41 through 64 )
;
3  3  'X-RAY DIFFRACTION' A 65  A 50  A 76  A 61  . 
;chain 'A' and (resid 65 through 76 )
;
4  4  'X-RAY DIFFRACTION' A 77  A 62  A 105 A 90  . 
;chain 'A' and (resid 77 through 105 )
;
5  5  'X-RAY DIFFRACTION' A 106 A 91  A 136 A 121 . 
;chain 'A' and (resid 106 through 136 )
;
6  6  'X-RAY DIFFRACTION' A 137 A 122 A 153 A 138 . 
;chain 'A' and (resid 137 through 153 )
;
7  7  'X-RAY DIFFRACTION' A 154 A 139 A 164 A 149 . 
;chain 'A' and (resid 154 through 164 )
;
8  8  'X-RAY DIFFRACTION' A 165 A 150 A 190 A 175 . 
;chain 'A' and (resid 165 through 190 )
;
9  9  'X-RAY DIFFRACTION' A 191 A 176 A 210 A 195 . 
;chain 'A' and (resid 191 through 210 )
;
10 10 'X-RAY DIFFRACTION' A 211 A 196 A 224 A 209 . 
;chain 'A' and (resid 211 through 224 )
;
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A MET 8   ? A MET 1   
2  1 Y 1 A ASP 9   ? A ASP 2   
3  1 Y 1 A GLN 10  ? A GLN 3   
4  1 Y 1 A PRO 11  ? A PRO 4   
5  1 Y 1 A MET 12  ? A MET 5   
6  1 Y 1 A GLU 13  ? A GLU 6   
7  1 Y 1 A GLU 14  ? A GLU 7   
8  1 Y 1 A GLU 15  ? A GLU 8   
9  1 Y 1 A GLU 225 ? A GLU 218 
10 1 Y 1 A ARG 226 ? A ARG 219 
11 1 Y 1 A ASP 227 ? A ASP 220 
12 1 Y 1 A LYS 228 ? A LYS 221 
13 1 Y 1 A GLU 229 ? A GLU 222 
14 1 Y 1 A VAL 230 ? A VAL 223 
15 1 Y 1 A SER 231 ? A SER 224 
16 1 Y 1 A ASP 232 ? A ASP 225 
17 1 Y 1 A ASP 233 ? A ASP 226 
18 1 Y 1 A GLU 234 ? A GLU 227 
19 1 Y 1 A ALA 235 ? A ALA 228 
20 1 Y 1 A GLU 236 ? A GLU 229 
21 1 Y 1 A LEU 237 ? A LEU 230 
22 1 Y 1 A GLU 238 ? A GLU 231 
23 1 Y 1 A HIS 239 ? A HIS 232 
24 1 Y 1 A HIS 240 ? A HIS 233 
25 1 Y 1 A HIS 241 ? A HIS 234 
26 1 Y 1 A HIS 242 ? A HIS 235 
27 1 Y 1 A HIS 243 ? A HIS 236 
28 1 Y 1 A HIS 244 ? A HIS 237 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
A1AYJ C1   C N N 1   
A1AYJ C10  C N N 2   
A1AYJ C2   C N N 3   
A1AYJ C3   C N N 4   
A1AYJ C4   C N N 5   
A1AYJ C5   C N N 6   
A1AYJ C6   C N N 7   
A1AYJ C7   C N N 8   
A1AYJ C8   C N N 9   
A1AYJ C9   C N N 10  
A1AYJ N1   N N N 11  
A1AYJ N2   N N N 12  
A1AYJ O1   O N N 13  
A1AYJ S1   S N N 14  
A1AYJ H2   H N N 15  
A1AYJ H3   H N N 16  
A1AYJ H20  H N N 17  
A1AYJ H19  H N N 18  
A1AYJ H4   H N N 19  
A1AYJ H5   H N N 20  
A1AYJ H8   H N N 21  
A1AYJ H9   H N N 22  
A1AYJ H10  H N N 23  
A1AYJ H11  H N N 24  
A1AYJ H12  H N N 25  
A1AYJ H13  H N N 26  
A1AYJ H14  H N N 27  
A1AYJ H16  H N N 28  
A1AYJ H15  H N N 29  
A1AYJ H18  H N N 30  
A1AYJ H17  H N N 31  
A1AYJ H6   H N N 32  
A1AYJ H7   H N N 33  
A1AYJ H1   H N N 34  
ALA   N    N N N 35  
ALA   CA   C N S 36  
ALA   C    C N N 37  
ALA   O    O N N 38  
ALA   CB   C N N 39  
ALA   OXT  O N N 40  
ALA   H    H N N 41  
ALA   H2   H N N 42  
ALA   HA   H N N 43  
ALA   HB1  H N N 44  
ALA   HB2  H N N 45  
ALA   HB3  H N N 46  
ALA   HXT  H N N 47  
ARG   N    N N N 48  
ARG   CA   C N S 49  
ARG   C    C N N 50  
ARG   O    O N N 51  
ARG   CB   C N N 52  
ARG   CG   C N N 53  
ARG   CD   C N N 54  
ARG   NE   N N N 55  
ARG   CZ   C N N 56  
ARG   NH1  N N N 57  
ARG   NH2  N N N 58  
ARG   OXT  O N N 59  
ARG   H    H N N 60  
ARG   H2   H N N 61  
ARG   HA   H N N 62  
ARG   HB2  H N N 63  
ARG   HB3  H N N 64  
ARG   HG2  H N N 65  
ARG   HG3  H N N 66  
ARG   HD2  H N N 67  
ARG   HD3  H N N 68  
ARG   HE   H N N 69  
ARG   HH11 H N N 70  
ARG   HH12 H N N 71  
ARG   HH21 H N N 72  
ARG   HH22 H N N 73  
ARG   HXT  H N N 74  
ASN   N    N N N 75  
ASN   CA   C N S 76  
ASN   C    C N N 77  
ASN   O    O N N 78  
ASN   CB   C N N 79  
ASN   CG   C N N 80  
ASN   OD1  O N N 81  
ASN   ND2  N N N 82  
ASN   OXT  O N N 83  
ASN   H    H N N 84  
ASN   H2   H N N 85  
ASN   HA   H N N 86  
ASN   HB2  H N N 87  
ASN   HB3  H N N 88  
ASN   HD21 H N N 89  
ASN   HD22 H N N 90  
ASN   HXT  H N N 91  
ASP   N    N N N 92  
ASP   CA   C N S 93  
ASP   C    C N N 94  
ASP   O    O N N 95  
ASP   CB   C N N 96  
ASP   CG   C N N 97  
ASP   OD1  O N N 98  
ASP   OD2  O N N 99  
ASP   OXT  O N N 100 
ASP   H    H N N 101 
ASP   H2   H N N 102 
ASP   HA   H N N 103 
ASP   HB2  H N N 104 
ASP   HB3  H N N 105 
ASP   HD2  H N N 106 
ASP   HXT  H N N 107 
GLN   N    N N N 108 
GLN   CA   C N S 109 
GLN   C    C N N 110 
GLN   O    O N N 111 
GLN   CB   C N N 112 
GLN   CG   C N N 113 
GLN   CD   C N N 114 
GLN   OE1  O N N 115 
GLN   NE2  N N N 116 
GLN   OXT  O N N 117 
GLN   H    H N N 118 
GLN   H2   H N N 119 
GLN   HA   H N N 120 
GLN   HB2  H N N 121 
GLN   HB3  H N N 122 
GLN   HG2  H N N 123 
GLN   HG3  H N N 124 
GLN   HE21 H N N 125 
GLN   HE22 H N N 126 
GLN   HXT  H N N 127 
GLU   N    N N N 128 
GLU   CA   C N S 129 
GLU   C    C N N 130 
GLU   O    O N N 131 
GLU   CB   C N N 132 
GLU   CG   C N N 133 
GLU   CD   C N N 134 
GLU   OE1  O N N 135 
GLU   OE2  O N N 136 
GLU   OXT  O N N 137 
GLU   H    H N N 138 
GLU   H2   H N N 139 
GLU   HA   H N N 140 
GLU   HB2  H N N 141 
GLU   HB3  H N N 142 
GLU   HG2  H N N 143 
GLU   HG3  H N N 144 
GLU   HE2  H N N 145 
GLU   HXT  H N N 146 
GLY   N    N N N 147 
GLY   CA   C N N 148 
GLY   C    C N N 149 
GLY   O    O N N 150 
GLY   OXT  O N N 151 
GLY   H    H N N 152 
GLY   H2   H N N 153 
GLY   HA2  H N N 154 
GLY   HA3  H N N 155 
GLY   HXT  H N N 156 
HIS   N    N N N 157 
HIS   CA   C N S 158 
HIS   C    C N N 159 
HIS   O    O N N 160 
HIS   CB   C N N 161 
HIS   CG   C Y N 162 
HIS   ND1  N Y N 163 
HIS   CD2  C Y N 164 
HIS   CE1  C Y N 165 
HIS   NE2  N Y N 166 
HIS   OXT  O N N 167 
HIS   H    H N N 168 
HIS   H2   H N N 169 
HIS   HA   H N N 170 
HIS   HB2  H N N 171 
HIS   HB3  H N N 172 
HIS   HD1  H N N 173 
HIS   HD2  H N N 174 
HIS   HE1  H N N 175 
HIS   HE2  H N N 176 
HIS   HXT  H N N 177 
HOH   O    O N N 178 
HOH   H1   H N N 179 
HOH   H2   H N N 180 
ILE   N    N N N 181 
ILE   CA   C N S 182 
ILE   C    C N N 183 
ILE   O    O N N 184 
ILE   CB   C N S 185 
ILE   CG1  C N N 186 
ILE   CG2  C N N 187 
ILE   CD1  C N N 188 
ILE   OXT  O N N 189 
ILE   H    H N N 190 
ILE   H2   H N N 191 
ILE   HA   H N N 192 
ILE   HB   H N N 193 
ILE   HG12 H N N 194 
ILE   HG13 H N N 195 
ILE   HG21 H N N 196 
ILE   HG22 H N N 197 
ILE   HG23 H N N 198 
ILE   HD11 H N N 199 
ILE   HD12 H N N 200 
ILE   HD13 H N N 201 
ILE   HXT  H N N 202 
LEU   N    N N N 203 
LEU   CA   C N S 204 
LEU   C    C N N 205 
LEU   O    O N N 206 
LEU   CB   C N N 207 
LEU   CG   C N N 208 
LEU   CD1  C N N 209 
LEU   CD2  C N N 210 
LEU   OXT  O N N 211 
LEU   H    H N N 212 
LEU   H2   H N N 213 
LEU   HA   H N N 214 
LEU   HB2  H N N 215 
LEU   HB3  H N N 216 
LEU   HG   H N N 217 
LEU   HD11 H N N 218 
LEU   HD12 H N N 219 
LEU   HD13 H N N 220 
LEU   HD21 H N N 221 
LEU   HD22 H N N 222 
LEU   HD23 H N N 223 
LEU   HXT  H N N 224 
LYS   N    N N N 225 
LYS   CA   C N S 226 
LYS   C    C N N 227 
LYS   O    O N N 228 
LYS   CB   C N N 229 
LYS   CG   C N N 230 
LYS   CD   C N N 231 
LYS   CE   C N N 232 
LYS   NZ   N N N 233 
LYS   OXT  O N N 234 
LYS   H    H N N 235 
LYS   H2   H N N 236 
LYS   HA   H N N 237 
LYS   HB2  H N N 238 
LYS   HB3  H N N 239 
LYS   HG2  H N N 240 
LYS   HG3  H N N 241 
LYS   HD2  H N N 242 
LYS   HD3  H N N 243 
LYS   HE2  H N N 244 
LYS   HE3  H N N 245 
LYS   HZ1  H N N 246 
LYS   HZ2  H N N 247 
LYS   HZ3  H N N 248 
LYS   HXT  H N N 249 
MET   N    N N N 250 
MET   CA   C N S 251 
MET   C    C N N 252 
MET   O    O N N 253 
MET   CB   C N N 254 
MET   CG   C N N 255 
MET   SD   S N N 256 
MET   CE   C N N 257 
MET   OXT  O N N 258 
MET   H    H N N 259 
MET   H2   H N N 260 
MET   HA   H N N 261 
MET   HB2  H N N 262 
MET   HB3  H N N 263 
MET   HG2  H N N 264 
MET   HG3  H N N 265 
MET   HE1  H N N 266 
MET   HE2  H N N 267 
MET   HE3  H N N 268 
MET   HXT  H N N 269 
PHE   N    N N N 270 
PHE   CA   C N S 271 
PHE   C    C N N 272 
PHE   O    O N N 273 
PHE   CB   C N N 274 
PHE   CG   C Y N 275 
PHE   CD1  C Y N 276 
PHE   CD2  C Y N 277 
PHE   CE1  C Y N 278 
PHE   CE2  C Y N 279 
PHE   CZ   C Y N 280 
PHE   OXT  O N N 281 
PHE   H    H N N 282 
PHE   H2   H N N 283 
PHE   HA   H N N 284 
PHE   HB2  H N N 285 
PHE   HB3  H N N 286 
PHE   HD1  H N N 287 
PHE   HD2  H N N 288 
PHE   HE1  H N N 289 
PHE   HE2  H N N 290 
PHE   HZ   H N N 291 
PHE   HXT  H N N 292 
PRO   N    N N N 293 
PRO   CA   C N S 294 
PRO   C    C N N 295 
PRO   O    O N N 296 
PRO   CB   C N N 297 
PRO   CG   C N N 298 
PRO   CD   C N N 299 
PRO   OXT  O N N 300 
PRO   H    H N N 301 
PRO   HA   H N N 302 
PRO   HB2  H N N 303 
PRO   HB3  H N N 304 
PRO   HG2  H N N 305 
PRO   HG3  H N N 306 
PRO   HD2  H N N 307 
PRO   HD3  H N N 308 
PRO   HXT  H N N 309 
SER   N    N N N 310 
SER   CA   C N S 311 
SER   C    C N N 312 
SER   O    O N N 313 
SER   CB   C N N 314 
SER   OG   O N N 315 
SER   OXT  O N N 316 
SER   H    H N N 317 
SER   H2   H N N 318 
SER   HA   H N N 319 
SER   HB2  H N N 320 
SER   HB3  H N N 321 
SER   HG   H N N 322 
SER   HXT  H N N 323 
THR   N    N N N 324 
THR   CA   C N S 325 
THR   C    C N N 326 
THR   O    O N N 327 
THR   CB   C N R 328 
THR   OG1  O N N 329 
THR   CG2  C N N 330 
THR   OXT  O N N 331 
THR   H    H N N 332 
THR   H2   H N N 333 
THR   HA   H N N 334 
THR   HB   H N N 335 
THR   HG1  H N N 336 
THR   HG21 H N N 337 
THR   HG22 H N N 338 
THR   HG23 H N N 339 
THR   HXT  H N N 340 
TRP   N    N N N 341 
TRP   CA   C N S 342 
TRP   C    C N N 343 
TRP   O    O N N 344 
TRP   CB   C N N 345 
TRP   CG   C Y N 346 
TRP   CD1  C Y N 347 
TRP   CD2  C Y N 348 
TRP   NE1  N Y N 349 
TRP   CE2  C Y N 350 
TRP   CE3  C Y N 351 
TRP   CZ2  C Y N 352 
TRP   CZ3  C Y N 353 
TRP   CH2  C Y N 354 
TRP   OXT  O N N 355 
TRP   H    H N N 356 
TRP   H2   H N N 357 
TRP   HA   H N N 358 
TRP   HB2  H N N 359 
TRP   HB3  H N N 360 
TRP   HD1  H N N 361 
TRP   HE1  H N N 362 
TRP   HE3  H N N 363 
TRP   HZ2  H N N 364 
TRP   HZ3  H N N 365 
TRP   HH2  H N N 366 
TRP   HXT  H N N 367 
TYR   N    N N N 368 
TYR   CA   C N S 369 
TYR   C    C N N 370 
TYR   O    O N N 371 
TYR   CB   C N N 372 
TYR   CG   C Y N 373 
TYR   CD1  C Y N 374 
TYR   CD2  C Y N 375 
TYR   CE1  C Y N 376 
TYR   CE2  C Y N 377 
TYR   CZ   C Y N 378 
TYR   OH   O N N 379 
TYR   OXT  O N N 380 
TYR   H    H N N 381 
TYR   H2   H N N 382 
TYR   HA   H N N 383 
TYR   HB2  H N N 384 
TYR   HB3  H N N 385 
TYR   HD1  H N N 386 
TYR   HD2  H N N 387 
TYR   HE1  H N N 388 
TYR   HE2  H N N 389 
TYR   HH   H N N 390 
TYR   HXT  H N N 391 
VAL   N    N N N 392 
VAL   CA   C N S 393 
VAL   C    C N N 394 
VAL   O    O N N 395 
VAL   CB   C N N 396 
VAL   CG1  C N N 397 
VAL   CG2  C N N 398 
VAL   OXT  O N N 399 
VAL   H    H N N 400 
VAL   H2   H N N 401 
VAL   HA   H N N 402 
VAL   HB   H N N 403 
VAL   HG11 H N N 404 
VAL   HG12 H N N 405 
VAL   HG13 H N N 406 
VAL   HG21 H N N 407 
VAL   HG22 H N N 408 
VAL   HG23 H N N 409 
VAL   HXT  H N N 410 
# 
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 
A1AYJ O1  C1   sing N N 1   
A1AYJ C1  C2   sing N N 2   
A1AYJ C2  N1   sing N N 3   
A1AYJ N1  C3   sing N N 4   
A1AYJ C3  S1   doub N N 5   
A1AYJ C3  N2   sing N N 6   
A1AYJ N2  C4   sing N N 7   
A1AYJ C4  C5   sing N N 8   
A1AYJ C5  C6   sing N N 9   
A1AYJ C6  C7   sing N N 10  
A1AYJ C7  C8   sing N N 11  
A1AYJ C8  C9   sing N N 12  
A1AYJ C9  C10  sing N N 13  
A1AYJ C4  C10  sing N N 14  
A1AYJ C1  H2   sing N N 15  
A1AYJ C1  H3   sing N N 16  
A1AYJ C10 H20  sing N N 17  
A1AYJ C10 H19  sing N N 18  
A1AYJ C2  H4   sing N N 19  
A1AYJ C2  H5   sing N N 20  
A1AYJ C4  H8   sing N N 21  
A1AYJ C5  H9   sing N N 22  
A1AYJ C5  H10  sing N N 23  
A1AYJ C6  H11  sing N N 24  
A1AYJ C6  H12  sing N N 25  
A1AYJ C7  H13  sing N N 26  
A1AYJ C7  H14  sing N N 27  
A1AYJ C8  H16  sing N N 28  
A1AYJ C8  H15  sing N N 29  
A1AYJ C9  H18  sing N N 30  
A1AYJ C9  H17  sing N N 31  
A1AYJ N1  H6   sing N N 32  
A1AYJ N2  H7   sing N N 33  
A1AYJ O1  H1   sing N N 34  
ALA   N   CA   sing N N 35  
ALA   N   H    sing N N 36  
ALA   N   H2   sing N N 37  
ALA   CA  C    sing N N 38  
ALA   CA  CB   sing N N 39  
ALA   CA  HA   sing N N 40  
ALA   C   O    doub N N 41  
ALA   C   OXT  sing N N 42  
ALA   CB  HB1  sing N N 43  
ALA   CB  HB2  sing N N 44  
ALA   CB  HB3  sing N N 45  
ALA   OXT HXT  sing N N 46  
ARG   N   CA   sing N N 47  
ARG   N   H    sing N N 48  
ARG   N   H2   sing N N 49  
ARG   CA  C    sing N N 50  
ARG   CA  CB   sing N N 51  
ARG   CA  HA   sing N N 52  
ARG   C   O    doub N N 53  
ARG   C   OXT  sing N N 54  
ARG   CB  CG   sing N N 55  
ARG   CB  HB2  sing N N 56  
ARG   CB  HB3  sing N N 57  
ARG   CG  CD   sing N N 58  
ARG   CG  HG2  sing N N 59  
ARG   CG  HG3  sing N N 60  
ARG   CD  NE   sing N N 61  
ARG   CD  HD2  sing N N 62  
ARG   CD  HD3  sing N N 63  
ARG   NE  CZ   sing N N 64  
ARG   NE  HE   sing N N 65  
ARG   CZ  NH1  sing N N 66  
ARG   CZ  NH2  doub N N 67  
ARG   NH1 HH11 sing N N 68  
ARG   NH1 HH12 sing N N 69  
ARG   NH2 HH21 sing N N 70  
ARG   NH2 HH22 sing N N 71  
ARG   OXT HXT  sing N N 72  
ASN   N   CA   sing N N 73  
ASN   N   H    sing N N 74  
ASN   N   H2   sing N N 75  
ASN   CA  C    sing N N 76  
ASN   CA  CB   sing N N 77  
ASN   CA  HA   sing N N 78  
ASN   C   O    doub N N 79  
ASN   C   OXT  sing N N 80  
ASN   CB  CG   sing N N 81  
ASN   CB  HB2  sing N N 82  
ASN   CB  HB3  sing N N 83  
ASN   CG  OD1  doub N N 84  
ASN   CG  ND2  sing N N 85  
ASN   ND2 HD21 sing N N 86  
ASN   ND2 HD22 sing N N 87  
ASN   OXT HXT  sing N N 88  
ASP   N   CA   sing N N 89  
ASP   N   H    sing N N 90  
ASP   N   H2   sing N N 91  
ASP   CA  C    sing N N 92  
ASP   CA  CB   sing N N 93  
ASP   CA  HA   sing N N 94  
ASP   C   O    doub N N 95  
ASP   C   OXT  sing N N 96  
ASP   CB  CG   sing N N 97  
ASP   CB  HB2  sing N N 98  
ASP   CB  HB3  sing N N 99  
ASP   CG  OD1  doub N N 100 
ASP   CG  OD2  sing N N 101 
ASP   OD2 HD2  sing N N 102 
ASP   OXT HXT  sing N N 103 
GLN   N   CA   sing N N 104 
GLN   N   H    sing N N 105 
GLN   N   H2   sing N N 106 
GLN   CA  C    sing N N 107 
GLN   CA  CB   sing N N 108 
GLN   CA  HA   sing N N 109 
GLN   C   O    doub N N 110 
GLN   C   OXT  sing N N 111 
GLN   CB  CG   sing N N 112 
GLN   CB  HB2  sing N N 113 
GLN   CB  HB3  sing N N 114 
GLN   CG  CD   sing N N 115 
GLN   CG  HG2  sing N N 116 
GLN   CG  HG3  sing N N 117 
GLN   CD  OE1  doub N N 118 
GLN   CD  NE2  sing N N 119 
GLN   NE2 HE21 sing N N 120 
GLN   NE2 HE22 sing N N 121 
GLN   OXT HXT  sing N N 122 
GLU   N   CA   sing N N 123 
GLU   N   H    sing N N 124 
GLU   N   H2   sing N N 125 
GLU   CA  C    sing N N 126 
GLU   CA  CB   sing N N 127 
GLU   CA  HA   sing N N 128 
GLU   C   O    doub N N 129 
GLU   C   OXT  sing N N 130 
GLU   CB  CG   sing N N 131 
GLU   CB  HB2  sing N N 132 
GLU   CB  HB3  sing N N 133 
GLU   CG  CD   sing N N 134 
GLU   CG  HG2  sing N N 135 
GLU   CG  HG3  sing N N 136 
GLU   CD  OE1  doub N N 137 
GLU   CD  OE2  sing N N 138 
GLU   OE2 HE2  sing N N 139 
GLU   OXT HXT  sing N N 140 
GLY   N   CA   sing N N 141 
GLY   N   H    sing N N 142 
GLY   N   H2   sing N N 143 
GLY   CA  C    sing N N 144 
GLY   CA  HA2  sing N N 145 
GLY   CA  HA3  sing N N 146 
GLY   C   O    doub N N 147 
GLY   C   OXT  sing N N 148 
GLY   OXT HXT  sing N N 149 
HIS   N   CA   sing N N 150 
HIS   N   H    sing N N 151 
HIS   N   H2   sing N N 152 
HIS   CA  C    sing N N 153 
HIS   CA  CB   sing N N 154 
HIS   CA  HA   sing N N 155 
HIS   C   O    doub N N 156 
HIS   C   OXT  sing N N 157 
HIS   CB  CG   sing N N 158 
HIS   CB  HB2  sing N N 159 
HIS   CB  HB3  sing N N 160 
HIS   CG  ND1  sing Y N 161 
HIS   CG  CD2  doub Y N 162 
HIS   ND1 CE1  doub Y N 163 
HIS   ND1 HD1  sing N N 164 
HIS   CD2 NE2  sing Y N 165 
HIS   CD2 HD2  sing N N 166 
HIS   CE1 NE2  sing Y N 167 
HIS   CE1 HE1  sing N N 168 
HIS   NE2 HE2  sing N N 169 
HIS   OXT HXT  sing N N 170 
HOH   O   H1   sing N N 171 
HOH   O   H2   sing N N 172 
ILE   N   CA   sing N N 173 
ILE   N   H    sing N N 174 
ILE   N   H2   sing N N 175 
ILE   CA  C    sing N N 176 
ILE   CA  CB   sing N N 177 
ILE   CA  HA   sing N N 178 
ILE   C   O    doub N N 179 
ILE   C   OXT  sing N N 180 
ILE   CB  CG1  sing N N 181 
ILE   CB  CG2  sing N N 182 
ILE   CB  HB   sing N N 183 
ILE   CG1 CD1  sing N N 184 
ILE   CG1 HG12 sing N N 185 
ILE   CG1 HG13 sing N N 186 
ILE   CG2 HG21 sing N N 187 
ILE   CG2 HG22 sing N N 188 
ILE   CG2 HG23 sing N N 189 
ILE   CD1 HD11 sing N N 190 
ILE   CD1 HD12 sing N N 191 
ILE   CD1 HD13 sing N N 192 
ILE   OXT HXT  sing N N 193 
LEU   N   CA   sing N N 194 
LEU   N   H    sing N N 195 
LEU   N   H2   sing N N 196 
LEU   CA  C    sing N N 197 
LEU   CA  CB   sing N N 198 
LEU   CA  HA   sing N N 199 
LEU   C   O    doub N N 200 
LEU   C   OXT  sing N N 201 
LEU   CB  CG   sing N N 202 
LEU   CB  HB2  sing N N 203 
LEU   CB  HB3  sing N N 204 
LEU   CG  CD1  sing N N 205 
LEU   CG  CD2  sing N N 206 
LEU   CG  HG   sing N N 207 
LEU   CD1 HD11 sing N N 208 
LEU   CD1 HD12 sing N N 209 
LEU   CD1 HD13 sing N N 210 
LEU   CD2 HD21 sing N N 211 
LEU   CD2 HD22 sing N N 212 
LEU   CD2 HD23 sing N N 213 
LEU   OXT HXT  sing N N 214 
LYS   N   CA   sing N N 215 
LYS   N   H    sing N N 216 
LYS   N   H2   sing N N 217 
LYS   CA  C    sing N N 218 
LYS   CA  CB   sing N N 219 
LYS   CA  HA   sing N N 220 
LYS   C   O    doub N N 221 
LYS   C   OXT  sing N N 222 
LYS   CB  CG   sing N N 223 
LYS   CB  HB2  sing N N 224 
LYS   CB  HB3  sing N N 225 
LYS   CG  CD   sing N N 226 
LYS   CG  HG2  sing N N 227 
LYS   CG  HG3  sing N N 228 
LYS   CD  CE   sing N N 229 
LYS   CD  HD2  sing N N 230 
LYS   CD  HD3  sing N N 231 
LYS   CE  NZ   sing N N 232 
LYS   CE  HE2  sing N N 233 
LYS   CE  HE3  sing N N 234 
LYS   NZ  HZ1  sing N N 235 
LYS   NZ  HZ2  sing N N 236 
LYS   NZ  HZ3  sing N N 237 
LYS   OXT HXT  sing N N 238 
MET   N   CA   sing N N 239 
MET   N   H    sing N N 240 
MET   N   H2   sing N N 241 
MET   CA  C    sing N N 242 
MET   CA  CB   sing N N 243 
MET   CA  HA   sing N N 244 
MET   C   O    doub N N 245 
MET   C   OXT  sing N N 246 
MET   CB  CG   sing N N 247 
MET   CB  HB2  sing N N 248 
MET   CB  HB3  sing N N 249 
MET   CG  SD   sing N N 250 
MET   CG  HG2  sing N N 251 
MET   CG  HG3  sing N N 252 
MET   SD  CE   sing N N 253 
MET   CE  HE1  sing N N 254 
MET   CE  HE2  sing N N 255 
MET   CE  HE3  sing N N 256 
MET   OXT HXT  sing N N 257 
PHE   N   CA   sing N N 258 
PHE   N   H    sing N N 259 
PHE   N   H2   sing N N 260 
PHE   CA  C    sing N N 261 
PHE   CA  CB   sing N N 262 
PHE   CA  HA   sing N N 263 
PHE   C   O    doub N N 264 
PHE   C   OXT  sing N N 265 
PHE   CB  CG   sing N N 266 
PHE   CB  HB2  sing N N 267 
PHE   CB  HB3  sing N N 268 
PHE   CG  CD1  doub Y N 269 
PHE   CG  CD2  sing Y N 270 
PHE   CD1 CE1  sing Y N 271 
PHE   CD1 HD1  sing N N 272 
PHE   CD2 CE2  doub Y N 273 
PHE   CD2 HD2  sing N N 274 
PHE   CE1 CZ   doub Y N 275 
PHE   CE1 HE1  sing N N 276 
PHE   CE2 CZ   sing Y N 277 
PHE   CE2 HE2  sing N N 278 
PHE   CZ  HZ   sing N N 279 
PHE   OXT HXT  sing N N 280 
PRO   N   CA   sing N N 281 
PRO   N   CD   sing N N 282 
PRO   N   H    sing N N 283 
PRO   CA  C    sing N N 284 
PRO   CA  CB   sing N N 285 
PRO   CA  HA   sing N N 286 
PRO   C   O    doub N N 287 
PRO   C   OXT  sing N N 288 
PRO   CB  CG   sing N N 289 
PRO   CB  HB2  sing N N 290 
PRO   CB  HB3  sing N N 291 
PRO   CG  CD   sing N N 292 
PRO   CG  HG2  sing N N 293 
PRO   CG  HG3  sing N N 294 
PRO   CD  HD2  sing N N 295 
PRO   CD  HD3  sing N N 296 
PRO   OXT HXT  sing N N 297 
SER   N   CA   sing N N 298 
SER   N   H    sing N N 299 
SER   N   H2   sing N N 300 
SER   CA  C    sing N N 301 
SER   CA  CB   sing N N 302 
SER   CA  HA   sing N N 303 
SER   C   O    doub N N 304 
SER   C   OXT  sing N N 305 
SER   CB  OG   sing N N 306 
SER   CB  HB2  sing N N 307 
SER   CB  HB3  sing N N 308 
SER   OG  HG   sing N N 309 
SER   OXT HXT  sing N N 310 
THR   N   CA   sing N N 311 
THR   N   H    sing N N 312 
THR   N   H2   sing N N 313 
THR   CA  C    sing N N 314 
THR   CA  CB   sing N N 315 
THR   CA  HA   sing N N 316 
THR   C   O    doub N N 317 
THR   C   OXT  sing N N 318 
THR   CB  OG1  sing N N 319 
THR   CB  CG2  sing N N 320 
THR   CB  HB   sing N N 321 
THR   OG1 HG1  sing N N 322 
THR   CG2 HG21 sing N N 323 
THR   CG2 HG22 sing N N 324 
THR   CG2 HG23 sing N N 325 
THR   OXT HXT  sing N N 326 
TRP   N   CA   sing N N 327 
TRP   N   H    sing N N 328 
TRP   N   H2   sing N N 329 
TRP   CA  C    sing N N 330 
TRP   CA  CB   sing N N 331 
TRP   CA  HA   sing N N 332 
TRP   C   O    doub N N 333 
TRP   C   OXT  sing N N 334 
TRP   CB  CG   sing N N 335 
TRP   CB  HB2  sing N N 336 
TRP   CB  HB3  sing N N 337 
TRP   CG  CD1  doub Y N 338 
TRP   CG  CD2  sing Y N 339 
TRP   CD1 NE1  sing Y N 340 
TRP   CD1 HD1  sing N N 341 
TRP   CD2 CE2  doub Y N 342 
TRP   CD2 CE3  sing Y N 343 
TRP   NE1 CE2  sing Y N 344 
TRP   NE1 HE1  sing N N 345 
TRP   CE2 CZ2  sing Y N 346 
TRP   CE3 CZ3  doub Y N 347 
TRP   CE3 HE3  sing N N 348 
TRP   CZ2 CH2  doub Y N 349 
TRP   CZ2 HZ2  sing N N 350 
TRP   CZ3 CH2  sing Y N 351 
TRP   CZ3 HZ3  sing N N 352 
TRP   CH2 HH2  sing N N 353 
TRP   OXT HXT  sing N N 354 
TYR   N   CA   sing N N 355 
TYR   N   H    sing N N 356 
TYR   N   H2   sing N N 357 
TYR   CA  C    sing N N 358 
TYR   CA  CB   sing N N 359 
TYR   CA  HA   sing N N 360 
TYR   C   O    doub N N 361 
TYR   C   OXT  sing N N 362 
TYR   CB  CG   sing N N 363 
TYR   CB  HB2  sing N N 364 
TYR   CB  HB3  sing N N 365 
TYR   CG  CD1  doub Y N 366 
TYR   CG  CD2  sing Y N 367 
TYR   CD1 CE1  sing Y N 368 
TYR   CD1 HD1  sing N N 369 
TYR   CD2 CE2  doub Y N 370 
TYR   CD2 HD2  sing N N 371 
TYR   CE1 CZ   doub Y N 372 
TYR   CE1 HE1  sing N N 373 
TYR   CE2 CZ   sing Y N 374 
TYR   CE2 HE2  sing N N 375 
TYR   CZ  OH   sing N N 376 
TYR   OH  HH   sing N N 377 
TYR   OXT HXT  sing N N 378 
VAL   N   CA   sing N N 379 
VAL   N   H    sing N N 380 
VAL   N   H2   sing N N 381 
VAL   CA  C    sing N N 382 
VAL   CA  CB   sing N N 383 
VAL   CA  HA   sing N N 384 
VAL   C   O    doub N N 385 
VAL   C   OXT  sing N N 386 
VAL   CB  CG1  sing N N 387 
VAL   CB  CG2  sing N N 388 
VAL   CB  HB   sing N N 389 
VAL   CG1 HG11 sing N N 390 
VAL   CG1 HG12 sing N N 391 
VAL   CG1 HG13 sing N N 392 
VAL   CG2 HG21 sing N N 393 
VAL   CG2 HG22 sing N N 394 
VAL   CG2 HG23 sing N N 395 
VAL   OXT HXT  sing N N 396 
# 
_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                    7HBM 
_atom_sites.fract_transf_matrix[1][1]   0.014321 
_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]   0.011270 
_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]   0.010287 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
_atom_type.scat_dispersion_real 
_atom_type.scat_dispersion_imag 
_atom_type.scat_Cromer_Mann_a1 
_atom_type.scat_Cromer_Mann_a2 
_atom_type.scat_Cromer_Mann_a3 
_atom_type.scat_Cromer_Mann_a4 
_atom_type.scat_Cromer_Mann_b1 
_atom_type.scat_Cromer_Mann_b2 
_atom_type.scat_Cromer_Mann_b3 
_atom_type.scat_Cromer_Mann_b4 
_atom_type.scat_Cromer_Mann_c 
_atom_type.scat_source 
_atom_type.scat_dispersion_source 
C ? ? 3.54356 2.42580 ? ? 25.62398 1.50364  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
N ? ? 4.01032 2.96436 ? ? 19.97189 1.75589  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O ? ? 4.49882 3.47563 ? ? 15.80542 1.70748  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
S ? ? 9.55732 6.39887 ? ? 1.23737  29.19336 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N   . GLU   A 1 9   ? 8.34803   15.78940 10.62979 1.000 67.88639  ? 16  GLU   A N   1 
ATOM   2    C CA  . GLU   A 1 9   ? 9.62770   16.48320 10.55933 1.000 70.31991  ? 16  GLU   A CA  1 
ATOM   3    C C   . GLU   A 1 9   ? 9.74922   17.49257 11.70092 1.000 69.38492  ? 16  GLU   A C   1 
ATOM   4    O O   . GLU   A 1 9   ? 9.00094   18.46969 11.76140 1.000 64.32095  ? 16  GLU   A O   1 
ATOM   5    C CB  . GLU   A 1 9   ? 9.78554   17.18167 9.20502  1.000 82.79816  ? 16  GLU   A CB  1 
ATOM   6    C CG  . GLU   A 1 9   ? 10.92849  18.18254 9.14373  1.000 75.13916  ? 16  GLU   A CG  1 
ATOM   7    C CD  . GLU   A 1 9   ? 12.28973  17.51222 9.16560  1.000 85.24368  ? 16  GLU   A CD  1 
ATOM   8    O OE1 . GLU   A 1 9   ? 13.22573  18.09355 9.75468  1.000 91.60710  ? 16  GLU   A OE1 1 
ATOM   9    O OE2 . GLU   A 1 9   ? 12.42205  16.40540 8.59628  1.000 91.36156  ? 16  GLU   A OE2 1 
ATOM   10   N N   . VAL   A 1 10  ? 10.69942  17.25345 12.60237 1.000 59.54892  ? 17  VAL   A N   1 
ATOM   11   C CA  . VAL   A 1 10  ? 10.84367  18.02597 13.83025 1.000 50.95911  ? 17  VAL   A CA  1 
ATOM   12   C C   . VAL   A 1 10  ? 12.20290  18.71418 13.82703 1.000 48.62155  ? 17  VAL   A C   1 
ATOM   13   O O   . VAL   A 1 10  ? 13.22371  18.08605 13.52444 1.000 47.76209  ? 17  VAL   A O   1 
ATOM   14   C CB  . VAL   A 1 10  ? 10.68705  17.13268 15.07490 1.000 47.28731  ? 17  VAL   A CB  1 
ATOM   15   C CG1 . VAL   A 1 10  ? 10.82964  17.95450 16.34423 1.000 45.18899  ? 17  VAL   A CG1 1 
ATOM   16   C CG2 . VAL   A 1 10  ? 9.34962   16.40971 15.04555 1.000 57.76192  ? 17  VAL   A CG2 1 
ATOM   17   N N   . GLU   A 1 11  ? 12.21359  19.99967 14.16772 1.000 48.61124  ? 18  GLU   A N   1 
ATOM   18   C CA  . GLU   A 1 11  ? 13.43913  20.76992 14.32768 1.000 45.07901  ? 18  GLU   A CA  1 
ATOM   19   C C   . GLU   A 1 11  ? 13.66579  21.06351 15.80478 1.000 36.08913  ? 18  GLU   A C   1 
ATOM   20   O O   . GLU   A 1 11  ? 12.72409  21.38795 16.53354 1.000 40.37980  ? 18  GLU   A O   1 
ATOM   21   C CB  . GLU   A 1 11  ? 13.37740  22.08194 13.53659 1.000 45.19122  ? 18  GLU   A CB  1 
ATOM   22   C CG  . GLU   A 1 11  ? 13.27412  21.89894 12.02715 1.000 49.58182  ? 18  GLU   A CG  1 
ATOM   23   C CD  . GLU   A 1 11  ? 13.19006  23.21870 11.28103 1.000 63.27984  ? 18  GLU   A CD  1 
ATOM   24   O OE1 . GLU   A 1 11  ? 12.28279  24.02154 11.59138 1.000 56.94561  ? 18  GLU   A OE1 1 
ATOM   25   O OE2 . GLU   A 1 11  ? 14.02912  23.44931 10.38191 1.000 70.01716  ? 18  GLU   A OE2 1 
ATOM   26   N N   . THR   A 1 12  ? 14.91389  20.94662 16.24508 1.000 38.42209  ? 19  THR   A N   1 
ATOM   27   C CA  . THR   A 1 12  ? 15.27945  21.16237 17.63910 1.000 40.19118  ? 19  THR   A CA  1 
ATOM   28   C C   . THR   A 1 12  ? 16.14907  22.40784 17.74385 1.000 36.29828  ? 19  THR   A C   1 
ATOM   29   O O   . THR   A 1 12  ? 17.14501  22.53681 17.02298 1.000 40.15780  ? 19  THR   A O   1 
ATOM   30   C CB  . THR   A 1 12  ? 16.01622  19.94398 18.20731 1.000 38.69016  ? 19  THR   A CB  1 
ATOM   31   O OG1 . THR   A 1 12  ? 15.14168  18.80670 18.20568 1.000 39.24540  ? 19  THR   A OG1 1 
ATOM   32   C CG2 . THR   A 1 12  ? 16.48353  20.20880 19.63306 1.000 36.28054  ? 19  THR   A CG2 1 
ATOM   33   N N   . PHE   A 1 13  ? 15.76695  23.32258 18.63224 1.000 37.15642  ? 20  PHE   A N   1 
ATOM   34   C CA  . PHE   A 1 13  ? 16.47719  24.57717 18.82984 1.000 40.10536  ? 20  PHE   A CA  1 
ATOM   35   C C   . PHE   A 1 13  ? 16.94746  24.68345 20.27327 1.000 37.16630  ? 20  PHE   A C   1 
ATOM   36   O O   . PHE   A 1 13  ? 16.32686  24.13623 21.18879 1.000 37.58542  ? 20  PHE   A O   1 
ATOM   37   C CB  . PHE   A 1 13  ? 15.59805  25.79917 18.50555 1.000 33.70616  ? 20  PHE   A CB  1 
ATOM   38   C CG  . PHE   A 1 13  ? 14.91186  25.73324 17.16771 1.000 32.19082  ? 20  PHE   A CG  1 
ATOM   39   C CD1 . PHE   A 1 13  ? 13.78066  24.95428 16.98443 1.000 35.97896  ? 20  PHE   A CD1 1 
ATOM   40   C CD2 . PHE   A 1 13  ? 15.39441  26.46122 16.09499 1.000 40.88895  ? 20  PHE   A CD2 1 
ATOM   41   C CE1 . PHE   A 1 13  ? 13.14968  24.89929 15.75446 1.000 42.46264  ? 20  PHE   A CE1 1 
ATOM   42   C CE2 . PHE   A 1 13  ? 14.75999  26.41544 14.86906 1.000 45.50535  ? 20  PHE   A CE2 1 
ATOM   43   C CZ  . PHE   A 1 13  ? 13.64363  25.62638 14.69657 1.000 40.43945  ? 20  PHE   A CZ  1 
ATOM   44   N N   . ALA   A 1 14  ? 18.04525  25.40400 20.47209 1.000 38.17820  ? 21  ALA   A N   1 
ATOM   45   C CA  . ALA   A 1 14  ? 18.53612  25.70179 21.80964 1.000 37.86203  ? 21  ALA   A CA  1 
ATOM   46   C C   . ALA   A 1 14  ? 17.90055  26.99070 22.31195 1.000 40.74322  ? 21  ALA   A C   1 
ATOM   47   O O   . ALA   A 1 14  ? 17.78384  27.96971 21.56471 1.000 39.38847  ? 21  ALA   A O   1 
ATOM   48   C CB  . ALA   A 1 14  ? 20.05922  25.83113 21.82335 1.000 35.66765  ? 21  ALA   A CB  1 
ATOM   49   N N   . PHE   A 1 15  ? 17.47566  26.98070 23.57169 1.000 41.98572  ? 22  PHE   A N   1 
ATOM   50   C CA  . PHE   A 1 15  ? 17.01834  28.20748 24.20343 1.000 41.72095  ? 22  PHE   A CA  1 
ATOM   51   C C   . PHE   A 1 15  ? 18.15990  29.21370 24.28309 1.000 48.20810  ? 22  PHE   A C   1 
ATOM   52   O O   . PHE   A 1 15  ? 19.33043  28.85170 24.43214 1.000 47.71686  ? 22  PHE   A O   1 
ATOM   53   C CB  . PHE   A 1 15  ? 16.48407  27.92794 25.60955 1.000 41.33140  ? 22  PHE   A CB  1 
ATOM   54   C CG  . PHE   A 1 15  ? 15.05994  27.46287 25.64064 1.000 39.94421  ? 22  PHE   A CG  1 
ATOM   55   C CD1 . PHE   A 1 15  ? 14.03939  28.28487 25.18736 1.000 38.55117  ? 22  PHE   A CD1 1 
ATOM   56   C CD2 . PHE   A 1 15  ? 14.73755  26.21609 26.14606 1.000 35.03190  ? 22  PHE   A CD2 1 
ATOM   57   C CE1 . PHE   A 1 15  ? 12.72376  27.86417 25.22366 1.000 36.62872  ? 22  PHE   A CE1 1 
ATOM   58   C CE2 . PHE   A 1 15  ? 13.42500  25.78563 26.18498 1.000 34.69381  ? 22  PHE   A CE2 1 
ATOM   59   C CZ  . PHE   A 1 15  ? 12.41608  26.61027 25.72410 1.000 41.79890  ? 22  PHE   A CZ  1 
ATOM   60   N N   . GLN   A 1 16  ? 17.80679  30.48966 24.16717 1.000 43.04043  ? 23  GLN   A N   1 
ATOM   61   C CA  . GLN   A 1 16  ? 18.75804  31.55646 24.43293 1.000 51.47688  ? 23  GLN   A CA  1 
ATOM   62   C C   . GLN   A 1 16  ? 19.26735  31.43284 25.86364 1.000 48.82268  ? 23  GLN   A C   1 
ATOM   63   O O   . GLN   A 1 16  ? 18.52530  31.03928 26.76790 1.000 48.82023  ? 23  GLN   A O   1 
ATOM   64   C CB  . GLN   A 1 16  ? 18.10220  32.92055 24.18636 1.000 48.79193  ? 23  GLN   A CB  1 
ATOM   65   C CG  . GLN   A 1 16  ? 17.20373  32.97021 22.92839 1.000 70.38772  ? 23  GLN   A CG  1 
ATOM   66   C CD  . GLN   A 1 16  ? 15.86864  32.23307 23.07464 1.000 78.94247  ? 23  GLN   A CD  1 
ATOM   67   O OE1 . GLN   A 1 16  ? 15.59625  31.26344 22.35922 1.000 79.59213  ? 23  GLN   A OE1 1 
ATOM   68   N NE2 . GLN   A 1 16  ? 15.02056  32.71808 23.97031 1.000 77.87586  ? 23  GLN   A NE2 1 
ATOM   69   N N   . ALA   A 1 17  ? 20.54932  31.76149 26.05925 1.000 51.34824  ? 24  ALA   A N   1 
ATOM   70   C CA  . ALA   A 1 17  ? 21.23661  31.42564 27.30552 1.000 45.81908  ? 24  ALA   A CA  1 
ATOM   71   C C   . ALA   A 1 17  ? 20.48155  31.92587 28.52747 1.000 46.04673  ? 24  ALA   A C   1 
ATOM   72   O O   . ALA   A 1 17  ? 20.40552  31.23621 29.55125 1.000 58.97123  ? 24  ALA   A O   1 
ATOM   73   C CB  . ALA   A 1 17  ? 22.65048  32.00514 27.29126 1.000 51.07672  ? 24  ALA   A CB  1 
ATOM   74   N N   . GLU   A 1 18  ? 19.90719  33.12201 28.43172 1.000 46.78976  ? 25  GLU   A N   1 
ATOM   75   C CA  . GLU   A 1 18  ? 19.27990  33.73708 29.59214 1.000 53.96598  ? 25  GLU   A CA  1 
ATOM   76   C C   . GLU   A 1 18  ? 17.90064  33.13902 29.84813 1.000 44.77995  ? 25  GLU   A C   1 
ATOM   77   O O   . GLU   A 1 18  ? 17.46410  33.05019 31.00082 1.000 40.97284  ? 25  GLU   A O   1 
ATOM   78   C CB  . GLU   A 1 18  ? 19.19979  35.25127 29.39014 1.000 53.86461  ? 25  GLU   A CB  1 
ATOM   79   C CG  . GLU   A 1 18  ? 20.52537  35.93072 29.02022 1.000 73.92532  ? 25  GLU   A CG  1 
ATOM   80   C CD  . GLU   A 1 18  ? 20.82831  35.87310 27.52807 1.000 70.73902  ? 25  GLU   A CD  1 
ATOM   81   O OE1 . GLU   A 1 18  ? 20.03584  35.24411 26.79706 1.000 71.19659  ? 25  GLU   A OE1 1 
ATOM   82   O OE2 . GLU   A 1 18  ? 21.80568  36.50946 27.07277 1.000 78.13197  ? 25  GLU   A OE2 1 
ATOM   83   N N   . ILE   A 1 19  ? 17.21011  32.70494 28.78707 1.000 39.73752  ? 26  ILE   A N   1 
ATOM   84   C CA  . ILE   A 1 19  ? 15.93815  32.00053 28.95169 1.000 43.77772  ? 26  ILE   A CA  1 
ATOM   85   C C   . ILE   A 1 19  ? 16.16225  30.61729 29.54754 1.000 42.11609  ? 26  ILE   A C   1 
ATOM   86   O O   . ILE   A 1 19  ? 15.41149  30.17574 30.42717 1.000 38.84493  ? 26  ILE   A O   1 
ATOM   87   C CB  . ILE   A 1 19  ? 15.18466  31.90862 27.61171 1.000 42.95228  ? 26  ILE   A CB  1 
ATOM   88   C CG1 . ILE   A 1 19  ? 14.90171  33.30352 27.04989 1.000 47.20082  ? 26  ILE   A CG1 1 
ATOM   89   C CG2 . ILE   A 1 19  ? 13.90139  31.10524 27.77785 1.000 38.62682  ? 26  ILE   A CG2 1 
ATOM   90   C CD1 . ILE   A 1 19  ? 13.58379  33.89615 27.50045 1.000 49.06124  ? 26  ILE   A CD1 1 
ATOM   91   N N   . ALA   A 1 20  ? 17.18247  29.90176 29.06579 1.000 40.09550  ? 27  ALA   A N   1 
ATOM   92   C CA  . ALA   A 1 20  ? 17.51166  28.60766 29.64996 1.000 39.08551  ? 27  ALA   A CA  1 
ATOM   93   C C   . ALA   A 1 20  ? 17.87884  28.74653 31.11950 1.000 44.50432  ? 27  ALA   A C   1 
ATOM   94   O O   . ALA   A 1 20  ? 17.57383  27.85788 31.92569 1.000 36.84295  ? 27  ALA   A O   1 
ATOM   95   C CB  . ALA   A 1 20  ? 18.65518  27.95239 28.87356 1.000 34.11488  ? 27  ALA   A CB  1 
ATOM   96   N N   . GLN   A 1 21  ? 18.53059  29.85410 31.48276 1.000 36.30049  ? 28  GLN   A N   1 
ATOM   97   C CA  . GLN   A 1 21  ? 18.86666  30.10359 32.88008 1.000 45.10472  ? 28  GLN   A CA  1 
ATOM   98   C C   . GLN   A 1 21  ? 17.61904  30.38484 33.70583 1.000 42.85789  ? 28  GLN   A C   1 
ATOM   99   O O   . GLN   A 1 21  ? 17.53779  29.98672 34.87357 1.000 45.08811  ? 28  GLN   A O   1 
ATOM   100  C CB  . GLN   A 1 21  ? 19.84164  31.27564 32.98261 1.000 46.06943  ? 28  GLN   A CB  1 
ATOM   101  C CG  . GLN   A 1 21  ? 21.29852  30.89181 32.91460 1.000 52.92878  ? 28  GLN   A CG  1 
ATOM   102  C CD  . GLN   A 1 21  ? 22.12634  31.93491 32.20368 1.000 65.77957  ? 28  GLN   A CD  1 
ATOM   103  O OE1 . GLN   A 1 21  ? 21.97211  33.13242 32.44419 1.000 69.76890  ? 28  GLN   A OE1 1 
ATOM   104  N NE2 . GLN   A 1 21  ? 23.01378  31.48818 31.32188 1.000 73.85926  ? 28  GLN   A NE2 1 
ATOM   105  N N   . LEU   A 1 22  ? 16.64500  31.08977 33.12567 1.000 38.82033  ? 29  LEU   A N   1 
ATOM   106  C CA  . LEU   A 1 22  ? 15.41797  31.38215 33.85782 1.000 39.47314  ? 29  LEU   A CA  1 
ATOM   107  C C   . LEU   A 1 22  ? 14.61048  30.11688 34.10807 1.000 41.39460  ? 29  LEU   A C   1 
ATOM   108  O O   . LEU   A 1 22  ? 14.08145  29.92023 35.20893 1.000 35.31389  ? 29  LEU   A O   1 
ATOM   109  C CB  . LEU   A 1 22  ? 14.57911  32.40326 33.09660 1.000 41.13728  ? 29  LEU   A CB  1 
ATOM   110  C CG  . LEU   A 1 22  ? 13.20659  32.64479 33.71719 1.000 43.95322  ? 29  LEU   A CG  1 
ATOM   111  C CD1 . LEU   A 1 22  ? 13.37313  33.22161 35.11654 1.000 35.66947  ? 29  LEU   A CD1 1 
ATOM   112  C CD2 . LEU   A 1 22  ? 12.36817  33.56063 32.84221 1.000 37.54644  ? 29  LEU   A CD2 1 
ATOM   113  N N   . MET   A 1 23  ? 14.50165  29.24832 33.09860 1.000 38.02650  ? 30  MET   A N   1 
ATOM   114  C CA  . MET   A 1 23  ? 13.74420  28.01470 33.27602 1.000 40.86311  ? 30  MET   A CA  1 
ATOM   115  C C   . MET   A 1 23  ? 14.39778  27.11287 34.31205 1.000 33.82749  ? 30  MET   A C   1 
ATOM   116  O O   . MET   A 1 23  ? 13.70801  26.51533 35.14463 1.000 43.79792  ? 30  MET   A O   1 
ATOM   117  C CB  . MET   A 1 23  ? 13.58778  27.28542 31.94205 1.000 31.63844  ? 30  MET   A CB  1 
ATOM   118  C CG  . MET   A 1 23  ? 12.80980  28.07278 30.90272 1.000 36.54217  ? 30  MET   A CG  1 
ATOM   119  S SD  . MET   A 1 23  ? 12.96768  27.37125 29.25098 1.000 40.21985  ? 30  MET   A SD  1 
ATOM   120  C CE  . MET   A 1 23  ? 11.91451  25.93343 29.41941 1.000 41.69992  ? 30  MET   A CE  1 
ATOM   121  N N   . SER   A 1 24  ? 15.72838  27.01138 34.28921 1.000 37.62111  ? 31  SER   A N   1 
ATOM   122  C CA  . SER   A 1 24  ? 16.40888  26.21950 35.30624 1.000 43.65669  ? 31  SER   A CA  1 
ATOM   123  C C   . SER   A 1 24  ? 16.20685  26.82846 36.68756 1.000 38.93338  ? 31  SER   A C   1 
ATOM   124  O O   . SER   A 1 24  ? 16.07142  26.10508 37.68039 1.000 42.11978  ? 31  SER   A O   1 
ATOM   125  C CB  . SER   A 1 24  ? 17.89588  26.09705 34.97540 1.000 49.26075  ? 31  SER   A CB  1 
ATOM   126  O OG  . SER   A 1 24  ? 18.64362  25.74726 36.12792 1.000 58.24258  ? 31  SER   A OG  1 
ATOM   127  N N   . LEU   A 1 25  ? 16.17053  28.16042 36.76761 1.000 49.78985  ? 32  LEU   A N   1 
ATOM   128  C CA  . LEU   A 1 25  ? 15.84009  28.82251 38.02631 1.000 48.41316  ? 32  LEU   A CA  1 
ATOM   129  C C   . LEU   A 1 25  ? 14.42764  28.45639 38.47120 1.000 44.65895  ? 32  LEU   A C   1 
ATOM   130  O O   . LEU   A 1 25  ? 14.21115  28.03343 39.61186 1.000 45.91877  ? 32  LEU   A O   1 
ATOM   131  C CB  . LEU   A 1 25  ? 15.99691  30.33973 37.86188 1.000 48.99178  ? 32  LEU   A CB  1 
ATOM   132  C CG  . LEU   A 1 25  ? 15.86873  31.38012 38.98939 1.000 61.44419  ? 32  LEU   A CG  1 
ATOM   133  C CD1 . LEU   A 1 25  ? 14.49491  31.43731 39.66011 1.000 57.43238  ? 32  LEU   A CD1 1 
ATOM   134  C CD2 . LEU   A 1 25  ? 16.96059  31.16267 40.02658 1.000 62.88862  ? 32  LEU   A CD2 1 
ATOM   135  N N   . ILE   A 1 26  ? 13.45295  28.60257 37.57054 1.000 42.99753  ? 33  ILE   A N   1 
ATOM   136  C CA  . ILE   A 1 26  ? 12.05711  28.35160 37.91696 1.000 45.24343  ? 33  ILE   A CA  1 
ATOM   137  C C   . ILE   A 1 26  ? 11.85204  26.91256 38.37111 1.000 43.51950  ? 33  ILE   A C   1 
ATOM   138  O O   . ILE   A 1 26  ? 11.05924  26.64575 39.28242 1.000 55.39339  ? 33  ILE   A O   1 
ATOM   139  C CB  . ILE   A 1 26  ? 11.15814  28.70928 36.71748 1.000 39.28472  ? 33  ILE   A CB  1 
ATOM   140  C CG1 . ILE   A 1 26  ? 11.07694  30.22754 36.55670 1.000 34.43300  ? 33  ILE   A CG1 1 
ATOM   141  C CG2 . ILE   A 1 26  ? 9.77468   28.08585 36.86484 1.000 41.43597  ? 33  ILE   A CG2 1 
ATOM   142  C CD1 . ILE   A 1 26  ? 10.39887  30.67100 35.27344 1.000 38.36509  ? 33  ILE   A CD1 1 
ATOM   143  N N   . ILE   A 1 27  ? 12.57988  25.97024 37.77601 1.000 45.46882  ? 34  ILE   A N   1 
ATOM   144  C CA  . ILE   A 1 27  ? 12.36966  24.55843 38.07550 1.000 52.88646  ? 34  ILE   A CA  1 
ATOM   145  C C   . ILE   A 1 27  ? 13.02710  24.16507 39.39425 1.000 51.60981  ? 34  ILE   A C   1 
ATOM   146  O O   . ILE   A 1 27  ? 12.47210  23.37302 40.16267 1.000 61.78453  ? 34  ILE   A O   1 
ATOM   147  C CB  . ILE   A 1 27  ? 12.89123  23.70568 36.90643 1.000 51.01061  ? 34  ILE   A CB  1 
ATOM   148  C CG1 . ILE   A 1 27  ? 11.96214  23.83594 35.70433 1.000 38.63789  ? 34  ILE   A CG1 1 
ATOM   149  C CG2 . ILE   A 1 27  ? 13.04073  22.24627 37.31525 1.000 59.00321  ? 34  ILE   A CG2 1 
ATOM   150  C CD1 . ILE   A 1 27  ? 12.64115  23.53164 34.42009 1.000 40.74854  ? 34  ILE   A CD1 1 
ATOM   151  N N   . ASN   A 1 28  ? 14.20705  24.71071 39.68809 1.000 48.20930  ? 35  ASN   A N   1 
ATOM   152  C CA  . ASN   A 1 28  ? 15.02752  24.17708 40.77030 1.000 59.84647  ? 35  ASN   A CA  1 
ATOM   153  C C   . ASN   A 1 28  ? 14.84181  24.89344 42.10162 1.000 65.57423  ? 35  ASN   A C   1 
ATOM   154  O O   . ASN   A 1 28  ? 15.05568  24.27754 43.15289 1.000 69.48148  ? 35  ASN   A O   1 
ATOM   155  C CB  . ASN   A 1 28  ? 16.50636  24.21874 40.37752 1.000 54.21985  ? 35  ASN   A CB  1 
ATOM   156  C CG  . ASN   A 1 28  ? 16.79725  23.39046 39.14415 1.000 65.47536  ? 35  ASN   A CG  1 
ATOM   157  O OD1 . ASN   A 1 28  ? 16.18153  22.34590 38.92671 1.000 62.52491  ? 35  ASN   A OD1 1 
ATOM   158  N ND2 . ASN   A 1 28  ? 17.73137  23.85539 38.32391 1.000 70.20475  ? 35  ASN   A ND2 1 
ATOM   159  N N   . THR   A 1 29  ? 14.46775  26.17017 42.10185 1.000 62.85573  ? 36  THR   A N   1 
ATOM   160  C CA  . THR   A 1 29  ? 14.28375  26.85861 43.37253 1.000 69.04561  ? 36  THR   A CA  1 
ATOM   161  C C   . THR   A 1 29  ? 13.02961  26.36850 44.09024 1.000 57.27009  ? 36  THR   A C   1 
ATOM   162  O O   . THR   A 1 29  ? 12.05803  25.92137 43.47259 1.000 53.45217  ? 36  THR   A O   1 
ATOM   163  C CB  . THR   A 1 29  ? 14.21906  28.37493 43.17794 1.000 66.53426  ? 36  THR   A CB  1 
ATOM   164  O OG1 . THR   A 1 29  ? 12.95386  28.74271 42.61453 1.000 77.45421  ? 36  THR   A OG1 1 
ATOM   165  C CG2 . THR   A 1 29  ? 15.36968  28.87381 42.31289 1.000 63.09558  ? 36  THR   A CG2 1 
ATOM   166  N N   . PHE   A 1 30  ? 13.07639  26.43876 45.41762 1.000 58.22787  ? 37  PHE   A N   1 
ATOM   167  C CA  . PHE   A 1 30  ? 11.95097  26.06022 46.26179 1.000 55.63740  ? 37  PHE   A CA  1 
ATOM   168  C C   . PHE   A 1 30  ? 11.01541  27.25482 46.37713 1.000 55.04771  ? 37  PHE   A C   1 
ATOM   169  O O   . PHE   A 1 30  ? 11.35149  28.25624 47.01825 1.000 69.08555  ? 37  PHE   A O   1 
ATOM   170  C CB  . PHE   A 1 30  ? 12.44926  25.60445 47.63042 1.000 55.78705  ? 37  PHE   A CB  1 
ATOM   171  C CG  . PHE   A 1 30  ? 11.36561  25.08242 48.52831 1.000 71.32099  ? 37  PHE   A CG  1 
ATOM   172  C CD1 . PHE   A 1 30  ? 10.80154  23.83775 48.30276 1.000 64.25486  ? 37  PHE   A CD1 1 
ATOM   173  C CD2 . PHE   A 1 30  ? 10.91456  25.83402 49.60347 1.000 59.46372  ? 37  PHE   A CD2 1 
ATOM   174  C CE1 . PHE   A 1 30  ? 9.80306   23.35231 49.12879 1.000 67.56824  ? 37  PHE   A CE1 1 
ATOM   175  C CE2 . PHE   A 1 30  ? 9.91805   25.35434 50.43299 1.000 63.19093  ? 37  PHE   A CE2 1 
ATOM   176  C CZ  . PHE   A 1 30  ? 9.36192   24.11010 50.19553 1.000 61.20522  ? 37  PHE   A CZ  1 
ATOM   177  N N   . TYR   A 1 31  ? 9.84795   27.15887 45.74776 1.000 49.14884  ? 38  TYR   A N   1 
ATOM   178  C CA  . TYR   A 1 31  ? 8.87696   28.24847 45.74556 1.000 50.73921  ? 38  TYR   A CA  1 
ATOM   179  C C   . TYR   A 1 31  ? 7.49090   27.62954 45.83441 1.000 52.95898  ? 38  TYR   A C   1 
ATOM   180  O O   . TYR   A 1 31  ? 7.06221   26.92861 44.91337 1.000 53.68365  ? 38  TYR   A O   1 
ATOM   181  C CB  . TYR   A 1 31  ? 9.02540   29.11820 44.49765 1.000 49.29738  ? 38  TYR   A CB  1 
ATOM   182  C CG  . TYR   A 1 31  ? 8.13833   30.33941 44.49774 1.000 58.97036  ? 38  TYR   A CG  1 
ATOM   183  C CD1 . TYR   A 1 31  ? 8.39859   31.40870 45.34735 1.000 56.95278  ? 38  TYR   A CD1 1 
ATOM   184  C CD2 . TYR   A 1 31  ? 7.05318   30.43301 43.63731 1.000 47.56753  ? 38  TYR   A CD2 1 
ATOM   185  C CE1 . TYR   A 1 31  ? 7.59347   32.52851 45.35485 1.000 49.21869  ? 38  TYR   A CE1 1 
ATOM   186  C CE2 . TYR   A 1 31  ? 6.24416   31.55102 43.63200 1.000 53.56214  ? 38  TYR   A CE2 1 
ATOM   187  C CZ  . TYR   A 1 31  ? 6.51759   32.59422 44.49171 1.000 58.58411  ? 38  TYR   A CZ  1 
ATOM   188  O OH  . TYR   A 1 31  ? 5.71347   33.70721 44.49024 1.000 65.09757  ? 38  TYR   A OH  1 
ATOM   189  N N   . SER   A 1 32  ? 6.79439   27.88721 46.94216 1.000 53.15521  ? 39  SER   A N   1 
ATOM   190  C CA  . SER   A 1 32  ? 5.54648   27.18560 47.21903 1.000 54.25919  ? 39  SER   A CA  1 
ATOM   191  C C   . SER   A 1 32  ? 4.34380   27.82578 46.53341 1.000 57.68091  ? 39  SER   A C   1 
ATOM   192  O O   . SER   A 1 32  ? 3.36074   27.13111 46.24985 1.000 61.20918  ? 39  SER   A O   1 
ATOM   193  C CB  . SER   A 1 32  ? 5.31558   27.11918 48.72815 1.000 54.55549  ? 39  SER   A CB  1 
ATOM   194  O OG  . SER   A 1 32  ? 6.12065   26.11432 49.32398 1.000 56.56195  ? 39  SER   A OG  1 
ATOM   195  N N   . ASN   A 1 33  ? 4.39731   29.13044 46.25830 1.000 51.26860  ? 40  ASN   A N   1 
ATOM   196  C CA  . ASN   A 1 33  ? 3.27483   29.85519 45.65857 1.000 50.15014  ? 40  ASN   A CA  1 
ATOM   197  C C   . ASN   A 1 33  ? 3.22002   29.62199 44.14441 1.000 49.89330  ? 40  ASN   A C   1 
ATOM   198  O O   . ASN   A 1 33  ? 3.33721   30.53722 43.32991 1.000 51.29652  ? 40  ASN   A O   1 
ATOM   199  C CB  . ASN   A 1 33  ? 3.38405   31.33833 45.98860 1.000 48.20241  ? 40  ASN   A CB  1 
ATOM   200  C CG  . ASN   A 1 33  ? 2.15762   32.12131 45.57143 1.000 53.33347  ? 40  ASN   A CG  1 
ATOM   201  O OD1 . ASN   A 1 33  ? 1.02472   31.67909 45.76880 1.000 54.27848  ? 40  ASN   A OD1 1 
ATOM   202  N ND2 . ASN   A 1 33  ? 2.37818   33.28854 44.97860 1.000 54.74712  ? 40  ASN   A ND2 1 
ATOM   203  N N   . LYS   A 1 34  ? 3.01750   28.35855 43.77254 1.000 42.36294  ? 41  LYS   A N   1 
ATOM   204  C CA  . LYS   A 1 34  ? 3.08574   27.96832 42.37023 1.000 40.00420  ? 41  LYS   A CA  1 
ATOM   205  C C   . LYS   A 1 34  ? 1.84141   28.34483 41.57459 1.000 42.18759  ? 41  LYS   A C   1 
ATOM   206  O O   . LYS   A 1 34  ? 1.89511   28.33504 40.33961 1.000 37.38641  ? 41  LYS   A O   1 
ATOM   207  C CB  . LYS   A 1 34  ? 3.33306   26.46114 42.26855 1.000 42.65831  ? 41  LYS   A CB  1 
ATOM   208  C CG  . LYS   A 1 34  ? 4.75314   26.05660 42.65131 1.000 39.83359  ? 41  LYS   A CG  1 
ATOM   209  C CD  . LYS   A 1 34  ? 4.94356   24.55422 42.59004 1.000 43.13974  ? 41  LYS   A CD  1 
ATOM   210  C CE  . LYS   A 1 34  ? 6.28791   24.14965 43.16671 1.000 43.41759  ? 41  LYS   A CE  1 
ATOM   211  N NZ  . LYS   A 1 34  ? 7.34960   24.15910 42.12552 1.000 50.92336  ? 41  LYS   A NZ  1 
ATOM   212  N N   . GLU   A 1 35  ? 0.73692   28.69634 42.23872 1.000 37.65509  ? 42  GLU   A N   1 
ATOM   213  C CA  . GLU   A 1 35  ? -0.52493  28.93633 41.54356 1.000 37.71603  ? 42  GLU   A CA  1 
ATOM   214  C C   . GLU   A 1 35  ? -0.49195  30.15094 40.62367 1.000 47.18773  ? 42  GLU   A C   1 
ATOM   215  O O   . GLU   A 1 35  ? -1.37464  30.27844 39.76679 1.000 41.84459  ? 42  GLU   A O   1 
ATOM   216  C CB  . GLU   A 1 35  ? -1.65753  29.09432 42.55732 1.000 42.74930  ? 42  GLU   A CB  1 
ATOM   217  C CG  . GLU   A 1 35  ? -1.65221  30.41684 43.29983 1.000 42.75705  ? 42  GLU   A CG  1 
ATOM   218  C CD  . GLU   A 1 35  ? -2.79556  30.52676 44.29195 1.000 60.80903  ? 42  GLU   A CD  1 
ATOM   219  O OE1 . GLU   A 1 35  ? -2.85274  29.70124 45.22897 1.000 57.86278  ? 42  GLU   A OE1 1 
ATOM   220  O OE2 . GLU   A 1 35  ? -3.63512  31.43841 44.13741 1.000 72.57784  ? 42  GLU   A OE2 1 
ATOM   221  N N   . ILE   A 1 36  ? 0.49377   31.03777 40.76735 1.000 40.55670  ? 43  ILE   A N   1 
ATOM   222  C CA  . ILE   A 1 36  ? 0.57588   32.21456 39.91696 1.000 36.28950  ? 43  ILE   A CA  1 
ATOM   223  C C   . ILE   A 1 36  ? 0.77091   31.86524 38.44848 1.000 41.42770  ? 43  ILE   A C   1 
ATOM   224  O O   . ILE   A 1 36  ? 0.56797   32.72581 37.58850 1.000 39.94504  ? 43  ILE   A O   1 
ATOM   225  C CB  . ILE   A 1 36  ? 1.70501   33.14760 40.40783 1.000 41.97594  ? 43  ILE   A CB  1 
ATOM   226  C CG1 . ILE   A 1 36  ? 3.04809   32.41457 40.43402 1.000 49.37287  ? 43  ILE   A CG1 1 
ATOM   227  C CG2 . ILE   A 1 36  ? 1.38143   33.68344 41.78839 1.000 41.12314  ? 43  ILE   A CG2 1 
ATOM   228  C CD1 . ILE   A 1 36  ? 3.95884   32.74328 39.27159 1.000 43.60464  ? 43  ILE   A CD1 1 
ATOM   229  N N   . PHE   A 1 37  ? 1.15691   30.62218 38.13668 1.000 38.51338  ? 44  PHE   A N   1 
ATOM   230  C CA  . PHE   A 1 37  ? 1.31500   30.22829 36.73809 1.000 35.14858  ? 44  PHE   A CA  1 
ATOM   231  C C   . PHE   A 1 37  ? 0.01224   30.39272 35.96511 1.000 36.27588  ? 44  PHE   A C   1 
ATOM   232  O O   . PHE   A 1 37  ? 0.02531   30.75204 34.78258 1.000 32.87404  ? 44  PHE   A O   1 
ATOM   233  C CB  . PHE   A 1 37  ? 1.79510   28.77800 36.63484 1.000 35.32717  ? 44  PHE   A CB  1 
ATOM   234  C CG  . PHE   A 1 37  ? 0.68095   27.76860 36.70836 1.000 32.11064  ? 44  PHE   A CG  1 
ATOM   235  C CD1 . PHE   A 1 37  ? 0.22290   27.31748 37.93209 1.000 34.52336  ? 44  PHE   A CD1 1 
ATOM   236  C CD2 . PHE   A 1 37  ? 0.06167   27.30433 35.55326 1.000 31.12608  ? 44  PHE   A CD2 1 
ATOM   237  C CE1 . PHE   A 1 37  ? -0.80776  26.40523 38.00848 1.000 40.96967  ? 44  PHE   A CE1 1 
ATOM   238  C CE2 . PHE   A 1 37  ? -0.97857  26.39841 35.62528 1.000 32.67404  ? 44  PHE   A CE2 1 
ATOM   239  C CZ  . PHE   A 1 37  ? -1.41127  25.94517 36.85382 1.000 38.85552  ? 44  PHE   A CZ  1 
ATOM   240  N N   . LEU   A 1 38  ? -1.12328  30.10348 36.60558 1.000 35.78325  ? 45  LEU   A N   1 
ATOM   241  C CA  . LEU   A 1 38  ? -2.39549  30.17038 35.89577 1.000 38.50758  ? 45  LEU   A CA  1 
ATOM   242  C C   . LEU   A 1 38  ? -2.75247  31.60885 35.55809 1.000 39.78851  ? 45  LEU   A C   1 
ATOM   243  O O   . LEU   A 1 38  ? -3.21819  31.89491 34.44892 1.000 36.51200  ? 45  LEU   A O   1 
ATOM   244  C CB  . LEU   A 1 38  ? -3.50172  29.51957 36.72491 1.000 34.58026  ? 45  LEU   A CB  1 
ATOM   245  C CG  . LEU   A 1 38  ? -4.78244  29.19664 35.95431 1.000 40.51648  ? 45  LEU   A CG  1 
ATOM   246  C CD1 . LEU   A 1 38  ? -4.45294  28.47943 34.65124 1.000 32.50226  ? 45  LEU   A CD1 1 
ATOM   247  C CD2 . LEU   A 1 38  ? -5.72137  28.35882 36.80526 1.000 36.96804  ? 45  LEU   A CD2 1 
ATOM   248  N N   . ARG   A 1 39  ? -2.53460  32.52515 36.50312 1.000 35.16072  ? 46  ARG   A N   1 
ATOM   249  C CA  . ARG   A 1 39  ? -2.75873  33.94056 36.23500 1.000 39.62054  ? 46  ARG   A CA  1 
ATOM   250  C C   . ARG   A 1 39  ? -1.92194  34.41047 35.05327 1.000 42.18501  ? 46  ARG   A C   1 
ATOM   251  O O   . ARG   A 1 39  ? -2.42284  35.11879 34.17193 1.000 38.47554  ? 46  ARG   A O   1 
ATOM   252  C CB  . ARG   A 1 39  ? -2.44269  34.75965 37.48892 1.000 38.35474  ? 46  ARG   A CB  1 
ATOM   253  C CG  . ARG   A 1 39  ? -2.25393  36.25223 37.25463 1.000 58.19526  ? 46  ARG   A CG  1 
ATOM   254  C CD  . ARG   A 1 39  ? -1.65922  36.93048 38.48450 1.000 56.37126  ? 46  ARG   A CD  1 
ATOM   255  N NE  . ARG   A 1 39  ? -0.21514  36.74227 38.55370 1.000 62.95679  ? 46  ARG   A NE  1 
ATOM   256  C CZ  . ARG   A 1 39  ? 0.50726   36.84812 39.66129 1.000 62.46050  ? 46  ARG   A CZ  1 
ATOM   257  N NH1 . ARG   A 1 39  ? -0.04631  37.15977 40.82175 1.000 49.84543  ? 46  ARG   A NH1 1 
ATOM   258  N NH2 . ARG   A 1 39  ? 1.81868   36.63178 39.60342 1.000 53.31314  ? 46  ARG   A NH2 1 
ATOM   259  N N   . GLU   A 1 40  ? -0.65160  33.99686 35.00269 1.000 30.67862  ? 47  GLU   A N   1 
ATOM   260  C CA  . GLU   A 1 40  ? 0.23476   34.43031 33.92711 1.000 35.26547  ? 47  GLU   A CA  1 
ATOM   261  C C   . GLU   A 1 40  ? -0.23385  33.90845 32.57356 1.000 40.53641  ? 47  GLU   A C   1 
ATOM   262  O O   . GLU   A 1 40  ? -0.21992  34.64459 31.57871 1.000 34.43162  ? 47  GLU   A O   1 
ATOM   263  C CB  . GLU   A 1 40  ? 1.66481   33.97046 34.21217 1.000 37.83928  ? 47  GLU   A CB  1 
ATOM   264  C CG  . GLU   A 1 40  ? 2.28581   34.56284 35.47410 1.000 43.57630  ? 47  GLU   A CG  1 
ATOM   265  C CD  . GLU   A 1 40  ? 2.02111   36.05325 35.62613 1.000 58.00574  ? 47  GLU   A CD  1 
ATOM   266  O OE1 . GLU   A 1 40  ? 2.26094   36.80938 34.66021 1.000 52.03450  ? 47  GLU   A OE1 1 
ATOM   267  O OE2 . GLU   A 1 40  ? 1.58090   36.47172 36.71677 1.000 64.73200  ? 47  GLU   A OE2 1 
ATOM   268  N N   . LEU   A 1 41  ? -0.65278  32.64239 32.51557 1.000 34.08901  ? 48  LEU   A N   1 
ATOM   269  C CA  . LEU   A 1 41  ? -1.11903  32.07935 31.25335 1.000 34.38951  ? 48  LEU   A CA  1 
ATOM   270  C C   . LEU   A 1 41  ? -2.44162  32.70439 30.82861 1.000 32.19562  ? 48  LEU   A C   1 
ATOM   271  O O   . LEU   A 1 41  ? -2.64922  32.98429 29.64275 1.000 36.03043  ? 48  LEU   A O   1 
ATOM   272  C CB  . LEU   A 1 41  ? -1.25317  30.56068 31.37398 1.000 28.78613  ? 48  LEU   A CB  1 
ATOM   273  C CG  . LEU   A 1 41  ? 0.07483   29.82664 31.56959 1.000 32.21898  ? 48  LEU   A CG  1 
ATOM   274  C CD1 . LEU   A 1 41  ? -0.12844  28.31660 31.63658 1.000 30.18376  ? 48  LEU   A CD1 1 
ATOM   275  C CD2 . LEU   A 1 41  ? 1.05813   30.20100 30.47294 1.000 31.13441  ? 48  LEU   A CD2 1 
ATOM   276  N N   . ILE   A 1 42  ? -3.34787  32.93228 31.78073 1.000 30.55354  ? 49  ILE   A N   1 
ATOM   277  C CA  . ILE   A 1 42  ? -4.61792  33.57159 31.45154 1.000 33.69716  ? 49  ILE   A CA  1 
ATOM   278  C C   . ILE   A 1 42  ? -4.38671  35.00865 31.00058 1.000 35.63324  ? 49  ILE   A C   1 
ATOM   279  O O   . ILE   A 1 42  ? -5.03823  35.49489 30.06742 1.000 34.31082  ? 49  ILE   A O   1 
ATOM   280  C CB  . ILE   A 1 42  ? -5.58128  33.49399 32.65144 1.000 33.36147  ? 49  ILE   A CB  1 
ATOM   281  C CG1 . ILE   A 1 42  ? -6.05488  32.05128 32.86093 1.000 33.55065  ? 49  ILE   A CG1 1 
ATOM   282  C CG2 . ILE   A 1 42  ? -6.76879  34.42389 32.44955 1.000 34.39842  ? 49  ILE   A CG2 1 
ATOM   283  C CD1 . ILE   A 1 42  ? -7.01942  31.87784 34.02846 1.000 33.11445  ? 49  ILE   A CD1 1 
ATOM   284  N N   . SER   A 1 43  ? -3.44423  35.70515 31.64240 1.000 30.44516  ? 50  SER   A N   1 
ATOM   285  C CA  . SER   A 1 43  ? -3.11273  37.06309 31.22458 1.000 34.39986  ? 50  SER   A CA  1 
ATOM   286  C C   . SER   A 1 43  ? -2.48648  37.07774 29.83130 1.000 35.53542  ? 50  SER   A C   1 
ATOM   287  O O   . SER   A 1 43  ? -2.76666  37.97780 29.03032 1.000 33.89610  ? 50  SER   A O   1 
ATOM   288  C CB  . SER   A 1 43  ? -2.18671  37.70992 32.25612 1.000 31.08194  ? 50  SER   A CB  1 
ATOM   289  O OG  . SER   A 1 43  ? -1.27091  38.59889 31.64458 1.000 50.21548  ? 50  SER   A OG  1 
ATOM   290  N N   . ASN   A 1 44  ? -1.64595  36.08460 29.51808 1.000 37.13545  ? 51  ASN   A N   1 
ATOM   291  C CA  . ASN   A 1 44  ? -1.11210  35.96714 28.16255 1.000 32.64844  ? 51  ASN   A CA  1 
ATOM   292  C C   . ASN   A 1 44  ? -2.22823  35.75075 27.14929 1.000 31.84469  ? 51  ASN   A C   1 
ATOM   293  O O   . ASN   A 1 44  ? -2.21387  36.33870 26.06098 1.000 34.63922  ? 51  ASN   A O   1 
ATOM   294  C CB  . ASN   A 1 44  ? -0.10762  34.81831 28.08575 1.000 30.89351  ? 51  ASN   A CB  1 
ATOM   295  C CG  . ASN   A 1 44  ? 1.26384   35.20905 28.58343 1.000 40.70170  ? 51  ASN   A CG  1 
ATOM   296  O OD1 . ASN   A 1 44  ? 1.46254   36.31242 29.08804 1.000 37.32213  ? 51  ASN   A OD1 1 
ATOM   297  N ND2 . ASN   A 1 44  ? 2.22211   34.29885 28.44950 1.000 39.22286  ? 51  ASN   A ND2 1 
ATOM   298  N N   . SER   A 1 45  ? -3.19884  34.89804 27.48635 1.000 32.45235  ? 52  SER   A N   1 
ATOM   299  C CA  . SER   A 1 45  ? -4.32311  34.65702 26.58812 1.000 29.45659  ? 52  SER   A CA  1 
ATOM   300  C C   . SER   A 1 45  ? -5.13549  35.92769 26.37853 1.000 36.25923  ? 52  SER   A C   1 
ATOM   301  O O   . SER   A 1 45  ? -5.57772  36.21578 25.25942 1.000 33.99383  ? 52  SER   A O   1 
ATOM   302  C CB  . SER   A 1 45  ? -5.20610  33.53951 27.14553 1.000 30.11411  ? 52  SER   A CB  1 
ATOM   303  O OG  . SER   A 1 45  ? -4.54358  32.28690 27.10077 1.000 31.20401  ? 52  SER   A OG  1 
ATOM   304  N N   . SER   A 1 46  ? -5.33687  36.70243 27.44786 1.000 36.19281  ? 53  SER   A N   1 
ATOM   305  C CA  . SER   A 1 46  ? -6.04973  37.96983 27.33084 1.000 36.74235  ? 53  SER   A CA  1 
ATOM   306  C C   . SER   A 1 46  ? -5.34587  38.91285 26.36262 1.000 30.47792  ? 53  SER   A C   1 
ATOM   307  O O   . SER   A 1 46  ? -5.99733  39.56404 25.53913 1.000 31.88247  ? 53  SER   A O   1 
ATOM   308  C CB  . SER   A 1 46  ? -6.18646  38.61715 28.71036 1.000 42.37643  ? 53  SER   A CB  1 
ATOM   309  O OG  . SER   A 1 46  ? -7.05668  39.73475 28.67626 1.000 42.73463  ? 53  SER   A OG  1 
ATOM   310  N N   . ASP   A 1 47  ? -4.01498  39.00175 26.44962 1.000 29.73862  ? 54  ASP   A N   1 
ATOM   311  C CA  . ASP   A 1 47  ? -3.26055  39.83347 25.51418 1.000 30.86851  ? 54  ASP   A CA  1 
ATOM   312  C C   . ASP   A 1 47  ? -3.45854  39.36423 24.07646 1.000 35.65906  ? 54  ASP   A C   1 
ATOM   313  O O   . ASP   A 1 47  ? -3.65659  40.18063 23.16923 1.000 33.92041  ? 54  ASP   A O   1 
ATOM   314  C CB  . ASP   A 1 47  ? -1.77345  39.81312 25.87178 1.000 34.19013  ? 54  ASP   A CB  1 
ATOM   315  C CG  . ASP   A 1 47  ? -1.45827  40.58209 27.14577 1.000 42.56156  ? 54  ASP   A CG  1 
ATOM   316  O OD1 . ASP   A 1 47  ? -2.34214  41.30385 27.65851 1.000 44.07173  ? 54  ASP   A OD1 1 
ATOM   317  O OD2 . ASP   A 1 47  ? -0.31907  40.44792 27.64434 1.000 46.55760  ? 54  ASP   A OD2 1 
ATOM   318  N N   . ALA   A 1 48  ? -3.40673  38.04960 23.84949 1.000 30.04231  ? 55  ALA   A N   1 
ATOM   319  C CA  . ALA   A 1 48  ? -3.57883  37.52249 22.49902 1.000 31.42997  ? 55  ALA   A CA  1 
ATOM   320  C C   . ALA   A 1 48  ? -4.96975  37.82705 21.95933 1.000 31.34928  ? 55  ALA   A C   1 
ATOM   321  O O   . ALA   A 1 48  ? -5.13325  38.12283 20.76924 1.000 28.01763  ? 55  ALA   A O   1 
ATOM   322  C CB  . ALA   A 1 48  ? -3.31928  36.01630 22.48711 1.000 32.10972  ? 55  ALA   A CB  1 
ATOM   323  N N   . LEU   A 1 49  ? -5.98750  37.75519 22.81768 1.000 26.55613  ? 56  LEU   A N   1 
ATOM   324  C CA  . LEU   A 1 49  ? -7.34070  38.06555 22.37217 1.000 29.41272  ? 56  LEU   A CA  1 
ATOM   325  C C   . LEU   A 1 49  ? -7.50048  39.55603 22.09636 1.000 30.39224  ? 56  LEU   A C   1 
ATOM   326  O O   . LEU   A 1 49  ? -8.18068  39.94404 21.14032 1.000 33.77241  ? 56  LEU   A O   1 
ATOM   327  C CB  . LEU   A 1 49  ? -8.35162  37.58891 23.41268 1.000 28.03805  ? 56  LEU   A CB  1 
ATOM   328  C CG  . LEU   A 1 49  ? -8.54096  36.07523 23.51762 1.000 37.05186  ? 56  LEU   A CG  1 
ATOM   329  C CD1 . LEU   A 1 49  ? -9.13064  35.71600 24.87024 1.000 33.75969  ? 56  LEU   A CD1 1 
ATOM   330  C CD2 . LEU   A 1 49  ? -9.43303  35.57027 22.39189 1.000 34.61702  ? 56  LEU   A CD2 1 
ATOM   331  N N   . ASP   A 1 50  ? -6.87451  40.40573 22.91743 1.000 32.26823  ? 57  ASP   A N   1 
ATOM   332  C CA  . ASP   A 1 50  ? -6.88101  41.84229 22.64874 1.000 35.09407  ? 57  ASP   A CA  1 
ATOM   333  C C   . ASP   A 1 50  ? -6.31686  42.15098 21.26742 1.000 31.75905  ? 57  ASP   A C   1 
ATOM   334  O O   . ASP   A 1 50  ? -6.84039  43.01560 20.55408 1.000 31.71475  ? 57  ASP   A O   1 
ATOM   335  C CB  . ASP   A 1 50  ? -6.07409  42.58981 23.71405 1.000 29.96055  ? 57  ASP   A CB  1 
ATOM   336  C CG  . ASP   A 1 50  ? -6.81493  42.72065 25.03561 1.000 41.41252  ? 57  ASP   A CG  1 
ATOM   337  O OD1 . ASP   A 1 50  ? -8.06092  42.63572 25.04464 1.000 42.97382  ? 57  ASP   A OD1 1 
ATOM   338  O OD2 . ASP   A 1 50  ? -6.14358  42.91340 26.07153 1.000 47.20205  ? 57  ASP   A OD2 1 
ATOM   339  N N   . LYS   A 1 51  ? -5.24794  41.45491 20.87036 1.000 27.30858  ? 58  LYS   A N   1 
ATOM   340  C CA  . LYS   A 1 51  ? -4.57293  41.79987 19.62242 1.000 30.98935  ? 58  LYS   A CA  1 
ATOM   341  C C   . LYS   A 1 51  ? -5.43700  41.47256 18.40853 1.000 30.03640  ? 58  LYS   A C   1 
ATOM   342  O O   . LYS   A 1 51  ? -5.57679  42.29887 17.49907 1.000 38.66723  ? 58  LYS   A O   1 
ATOM   343  C CB  . LYS   A 1 51  ? -3.22171  41.09154 19.53157 1.000 32.23845  ? 58  LYS   A CB  1 
ATOM   344  C CG  . LYS   A 1 51  ? -2.37118  41.57887 18.36218 1.000 49.42904  ? 58  LYS   A CG  1 
ATOM   345  C CD  . LYS   A 1 51  ? -0.88135  41.52921 18.67105 1.000 56.10689  ? 58  LYS   A CD  1 
ATOM   346  C CE  . LYS   A 1 51  ? -0.07363  42.31017 17.63718 1.000 50.37279  ? 58  LYS   A CE  1 
ATOM   347  N NZ  . LYS   A 1 51  ? 0.72036   41.42030 16.74985 1.000 53.25767  ? 58  LYS   A NZ  1 
ATOM   348  N N   . ILE   A 1 52  ? -6.02162  40.27157 18.36430 1.000 33.82312  ? 59  ILE   A N   1 
ATOM   349  C CA  . ILE   A 1 52  ? -6.85338  39.92433 17.21302 1.000 32.17846  ? 59  ILE   A CA  1 
ATOM   350  C C   . ILE   A 1 52  ? -8.08908  40.81233 17.17530 1.000 32.60856  ? 59  ILE   A C   1 
ATOM   351  O O   . ILE   A 1 52  ? -8.52855  41.24641 16.10377 1.000 38.93859  ? 59  ILE   A O   1 
ATOM   352  C CB  . ILE   A 1 52  ? -7.21757  38.42275 17.21808 1.000 38.62079  ? 59  ILE   A CB  1 
ATOM   353  C CG1 . ILE   A 1 52  ? -7.91471  38.03549 15.90953 1.000 32.07135  ? 59  ILE   A CG1 1 
ATOM   354  C CG2 . ILE   A 1 52  ? -8.11144  38.05686 18.39377 1.000 27.37674  ? 59  ILE   A CG2 1 
ATOM   355  C CD1 . ILE   A 1 52  ? -7.07523  38.27259 14.66815 1.000 32.06743  ? 59  ILE   A CD1 1 
ATOM   356  N N   . ARG   A 1 53  ? -8.64339  41.13409 18.34474 1.000 37.31800  ? 60  ARG   A N   1 
ATOM   357  C CA  . ARG   A 1 53  ? -9.83917  41.96470 18.37651 1.000 40.79363  ? 60  ARG   A CA  1 
ATOM   358  C C   . ARG   A 1 53  ? -9.53488  43.37288 17.88683 1.000 40.05744  ? 60  ARG   A C   1 
ATOM   359  O O   . ARG   A 1 53  ? -10.34392 43.97620 17.17389 1.000 43.38796  ? 60  ARG   A O   1 
ATOM   360  C CB  . ARG   A 1 53  ? -10.42522 41.98686 19.78862 1.000 35.89519  ? 60  ARG   A CB  1 
ATOM   361  C CG  . ARG   A 1 53  ? -11.76127 42.69556 19.87928 1.000 47.47961  ? 60  ARG   A CG  1 
ATOM   362  C CD  . ARG   A 1 53  ? -12.26405 42.77759 21.31952 1.000 57.76785  ? 60  ARG   A CD  1 
ATOM   363  N NE  . ARG   A 1 53  ? -13.12810 43.93185 21.55407 1.000 69.46769  ? 60  ARG   A NE  1 
ATOM   364  C CZ  . ARG   A 1 53  ? -14.22531 44.23211 20.86800 1.000 76.83603  ? 60  ARG   A CZ  1 
ATOM   365  N NH1 . ARG   A 1 53  ? -14.70319 43.42956 19.93109 1.000 80.48240  ? 60  ARG   A NH1 1 
ATOM   366  N NH2 . ARG   A 1 53  ? -14.86964 45.36390 21.14116 1.000 64.71133  ? 60  ARG   A NH2 1 
ATOM   367  N N   . TYR   A 1 54  ? -8.36183  43.90250 18.24086 1.000 36.18955  ? 61  TYR   A N   1 
ATOM   368  C CA  . TYR   A 1 54  ? -7.96986  45.22069 17.75842 1.000 39.80754  ? 61  TYR   A CA  1 
ATOM   369  C C   . TYR   A 1 54  ? -7.75558  45.21718 16.24999 1.000 34.27031  ? 61  TYR   A C   1 
ATOM   370  O O   . TYR   A 1 54  ? -8.20360  46.13431 15.55136 1.000 32.24821  ? 61  TYR   A O   1 
ATOM   371  C CB  . TYR   A 1 54  ? -6.70332  45.68450 18.47608 1.000 31.03092  ? 61  TYR   A CB  1 
ATOM   372  C CG  . TYR   A 1 54  ? -6.09291  46.91535 17.85816 1.000 36.84170  ? 61  TYR   A CG  1 
ATOM   373  C CD1 . TYR   A 1 54  ? -6.62896  48.16805 18.10941 1.000 37.58729  ? 61  TYR   A CD1 1 
ATOM   374  C CD2 . TYR   A 1 54  ? -4.97866  46.83085 17.03261 1.000 34.17936  ? 61  TYR   A CD2 1 
ATOM   375  C CE1 . TYR   A 1 54  ? -6.08451  49.30225 17.55039 1.000 35.15655  ? 61  TYR   A CE1 1 
ATOM   376  C CE2 . TYR   A 1 54  ? -4.42182  47.96800 16.46759 1.000 35.79066  ? 61  TYR   A CE2 1 
ATOM   377  C CZ  . TYR   A 1 54  ? -4.98491  49.20074 16.73041 1.000 35.09993  ? 61  TYR   A CZ  1 
ATOM   378  O OH  . TYR   A 1 54  ? -4.44716  50.34510 16.18557 1.000 36.77547  ? 61  TYR   A OH  1 
ATOM   379  N N   . GLU   A 1 55  ? -7.06380  44.19782 15.73415 1.000 32.84461  ? 62  GLU   A N   1 
ATOM   380  C CA  . GLU   A 1 55  ? -6.79765  44.11942 14.30184 1.000 37.89883  ? 62  GLU   A CA  1 
ATOM   381  C C   . GLU   A 1 55  ? -8.07809  43.92784 13.50236 1.000 43.02540  ? 62  GLU   A C   1 
ATOM   382  O O   . GLU   A 1 55  ? -8.18192  44.41723 12.37212 1.000 38.70621  ? 62  GLU   A O   1 
ATOM   383  C CB  . GLU   A 1 55  ? -5.82611  42.97466 14.01150 1.000 33.01481  ? 62  GLU   A CB  1 
ATOM   384  C CG  . GLU   A 1 55  ? -4.42131  43.20790 14.53598 1.000 50.12664  ? 62  GLU   A CG  1 
ATOM   385  C CD  . GLU   A 1 55  ? -3.41206  42.23182 13.96464 1.000 57.34580  ? 62  GLU   A CD  1 
ATOM   386  O OE1 . GLU   A 1 55  ? -3.83395  41.20939 13.38352 1.000 54.34070  ? 62  GLU   A OE1 1 
ATOM   387  O OE2 . GLU   A 1 55  ? -2.19567  42.48701 14.10301 1.000 63.70350  ? 62  GLU   A OE2 1 
ATOM   388  N N   . SER   A 1 56  ? -9.05514  43.21658 14.06604 1.000 36.05107  ? 63  SER   A N   1 
ATOM   389  C CA  . SER   A 1 56  ? -10.31442 42.97392 13.37813 1.000 34.39842  ? 63  SER   A CA  1 
ATOM   390  C C   . SER   A 1 56  ? -11.15681 44.23234 13.22475 1.000 41.65590  ? 63  SER   A C   1 
ATOM   391  O O   . SER   A 1 56  ? -12.10265 44.22607 12.43035 1.000 48.15705  ? 63  SER   A O   1 
ATOM   392  C CB  . SER   A 1 56  ? -11.11336 41.90602 14.12414 1.000 35.76896  ? 63  SER   A CB  1 
ATOM   393  O OG  . SER   A 1 56  ? -11.93439 42.48578 15.12207 1.000 40.45327  ? 63  SER   A OG  1 
ATOM   394  N N   . LEU   A 1 57  ? -10.84286 45.30287 13.96009 1.000 40.94538  ? 64  LEU   A N   1 
ATOM   395  C CA  . LEU   A 1 57  ? -11.61296 46.53724 13.83966 1.000 46.43455  ? 64  LEU   A CA  1 
ATOM   396  C C   . LEU   A 1 57  ? -11.36573 47.23135 12.50696 1.000 45.95821  ? 64  LEU   A C   1 
ATOM   397  O O   . LEU   A 1 57  ? -12.26626 47.89176 11.97891 1.000 48.45753  ? 64  LEU   A O   1 
ATOM   398  C CB  . LEU   A 1 57  ? -11.28018 47.47953 14.99592 1.000 45.82529  ? 64  LEU   A CB  1 
ATOM   399  C CG  . LEU   A 1 57  ? -11.61265 46.93978 16.38608 1.000 50.05208  ? 64  LEU   A CG  1 
ATOM   400  C CD1 . LEU   A 1 57  ? -11.36890 48.00363 17.43772 1.000 42.36820  ? 64  LEU   A CD1 1 
ATOM   401  C CD2 . LEU   A 1 57  ? -13.05255 46.46276 16.42832 1.000 39.97631  ? 64  LEU   A CD2 1 
ATOM   402  N N   . THR   A 1 58  ? -10.16145 47.10564 11.95556 1.000 45.81902  ? 65  THR   A N   1 
ATOM   403  C CA  . THR   A 1 58  ? -9.84604  47.64777 10.64223 1.000 54.68720  ? 65  THR   A CA  1 
ATOM   404  C C   . THR   A 1 58  ? -9.85227  46.58565 9.55223  1.000 51.00765  ? 65  THR   A C   1 
ATOM   405  O O   . THR   A 1 58  ? -9.66193  46.91994 8.37985  1.000 57.31966  ? 65  THR   A O   1 
ATOM   406  C CB  . THR   A 1 58  ? -8.48385  48.34879 10.66874 1.000 49.34666  ? 65  THR   A CB  1 
ATOM   407  O OG1 . THR   A 1 58  ? -7.47337  47.40869 11.04908 1.000 57.58520  ? 65  THR   A OG1 1 
ATOM   408  C CG2 . THR   A 1 58  ? -8.49381  49.51273 11.64876 1.000 53.72365  ? 65  THR   A CG2 1 
ATOM   409  N N   . ASP   A 1 59  ? -10.07021 45.32178 9.90953  1.000 58.54251  ? 66  ASP   A N   1 
ATOM   410  C CA  . ASP   A 1 59  ? -10.08115 44.21599 8.96145  1.000 47.87937  ? 66  ASP   A CA  1 
ATOM   411  C C   . ASP   A 1 59  ? -10.95359 43.09474 9.51152  1.000 50.88184  ? 66  ASP   A C   1 
ATOM   412  O O   . ASP   A 1 59  ? -10.43406 42.14283 10.10979 1.000 50.46474  ? 66  ASP   A O   1 
ATOM   413  C CB  . ASP   A 1 59  ? -8.66259  43.70546 8.70839  1.000 56.58944  ? 66  ASP   A CB  1 
ATOM   414  C CG  . ASP   A 1 59  ? -8.57620  42.77920 7.50579  1.000 65.31048  ? 66  ASP   A CG  1 
ATOM   415  O OD1 . ASP   A 1 59  ? -9.62521  42.26607 7.05839  1.000 56.15877  ? 66  ASP   A OD1 1 
ATOM   416  O OD2 . ASP   A 1 59  ? -7.44737  42.54863 7.01919  1.000 64.38424  ? 66  ASP   A OD2 1 
ATOM   417  N N   . PRO   A 1 60  ? -12.27434 43.16659 9.33115  1.000 53.57563  ? 67  PRO   A N   1 
ATOM   418  C CA  . PRO   A 1 60  ? -13.15043 42.12574 9.89479  1.000 49.95165  ? 67  PRO   A CA  1 
ATOM   419  C C   . PRO   A 1 60  ? -12.87873 40.73160 9.35306  1.000 55.54155  ? 67  PRO   A C   1 
ATOM   420  O O   . PRO   A 1 60  ? -13.26994 39.74871 9.99591  1.000 49.16666  ? 67  PRO   A O   1 
ATOM   421  C CB  . PRO   A 1 60  ? -14.55727 42.60898 9.51169  1.000 56.38381  ? 67  PRO   A CB  1 
ATOM   422  C CG  . PRO   A 1 60  ? -14.40331 44.08197 9.29851  1.000 55.54684  ? 67  PRO   A CG  1 
ATOM   423  C CD  . PRO   A 1 60  ? -13.04406 44.24294 8.68783  1.000 54.89228  ? 67  PRO   A CD  1 
ATOM   424  N N   . SER   A 1 61  ? -12.21956 40.60902 8.19763  1.000 47.44493  ? 68  SER   A N   1 
ATOM   425  C CA  . SER   A 1 61  ? -11.93631 39.29113 7.64051  1.000 44.80384  ? 68  SER   A CA  1 
ATOM   426  C C   . SER   A 1 61  ? -10.91771 38.51214 8.46760  1.000 52.25935  ? 68  SER   A C   1 
ATOM   427  O O   . SER   A 1 61  ? -10.79175 37.29719 8.28424  1.000 49.67893  ? 68  SER   A O   1 
ATOM   428  C CB  . SER   A 1 61  ? -11.44478 39.42233 6.19950  1.000 46.87951  ? 68  SER   A CB  1 
ATOM   429  O OG  . SER   A 1 61  ? -10.13380 39.95391 6.15768  1.000 53.66097  ? 68  SER   A OG  1 
ATOM   430  N N   . LYS   A 1 62  ? -10.19111 39.17426 9.37162  1.000 42.19213  ? 69  LYS   A N   1 
ATOM   431  C CA  . LYS   A 1 62  ? -9.28472  38.46227 10.26442 1.000 39.71310  ? 69  LYS   A CA  1 
ATOM   432  C C   . LYS   A 1 62  ? -10.01739 37.55349 11.24073 1.000 45.69804  ? 69  LYS   A C   1 
ATOM   433  O O   . LYS   A 1 62  ? -9.37630  36.70704 11.87262 1.000 42.80541  ? 69  LYS   A O   1 
ATOM   434  C CB  . LYS   A 1 62  ? -8.41723  39.45550 11.03899 1.000 39.32303  ? 69  LYS   A CB  1 
ATOM   435  C CG  . LYS   A 1 62  ? -7.61720  40.38102 10.14590 1.000 51.17954  ? 69  LYS   A CG  1 
ATOM   436  C CD  . LYS   A 1 62  ? -6.25695  40.68962 10.73889 1.000 46.16862  ? 69  LYS   A CD  1 
ATOM   437  C CE  . LYS   A 1 62  ? -5.52843  41.72427 9.89964  1.000 53.34579  ? 69  LYS   A CE  1 
ATOM   438  N NZ  . LYS   A 1 62  ? -4.05997  41.67612 10.11008 1.000 60.36327  ? 69  LYS   A NZ  1 
ATOM   439  N N   . LEU   A 1 63  ? -11.33210 37.70818 11.38026 1.000 43.90334  ? 70  LEU   A N   1 
ATOM   440  C CA  . LEU   A 1 63  ? -12.14573 36.84013 12.21649 1.000 43.00633  ? 70  LEU   A CA  1 
ATOM   441  C C   . LEU   A 1 63  ? -12.83413 35.73869 11.41948 1.000 49.91544  ? 70  LEU   A C   1 
ATOM   442  O O   . LEU   A 1 63  ? -13.67563 35.02299 11.97164 1.000 46.14245  ? 70  LEU   A O   1 
ATOM   443  C CB  . LEU   A 1 63  ? -13.18537 37.66676 12.97146 1.000 43.99165  ? 70  LEU   A CB  1 
ATOM   444  C CG  . LEU   A 1 63  ? -12.62811 38.65208 13.99817 1.000 41.11807  ? 70  LEU   A CG  1 
ATOM   445  C CD1 . LEU   A 1 63  ? -13.76129 39.37307 14.69926 1.000 41.86878  ? 70  LEU   A CD1 1 
ATOM   446  C CD2 . LEU   A 1 63  ? -11.74161 37.93407 15.00344 1.000 34.47976  ? 70  LEU   A CD2 1 
ATOM   447  N N   . ASP   A 1 64  ? -12.50553 35.59229 10.13208 1.000 42.84438  ? 71  ASP   A N   1 
ATOM   448  C CA  . ASP   A 1 64  ? -13.05074 34.48806 9.34893  1.000 50.24300  ? 71  ASP   A CA  1 
ATOM   449  C C   . ASP   A 1 64  ? -12.62318 33.13412 9.89567  1.000 47.88455  ? 71  ASP   A C   1 
ATOM   450  O O   . ASP   A 1 64  ? -13.30265 32.13298 9.64576  1.000 48.52787  ? 71  ASP   A O   1 
ATOM   451  C CB  . ASP   A 1 64  ? -12.62271 34.61153 7.88714  1.000 47.62570  ? 71  ASP   A CB  1 
ATOM   452  C CG  . ASP   A 1 64  ? -13.28410 35.77775 7.18398  1.000 60.99466  ? 71  ASP   A CG  1 
ATOM   453  O OD1 . ASP   A 1 64  ? -14.25582 36.33488 7.74137  1.000 57.79660  ? 71  ASP   A OD1 1 
ATOM   454  O OD2 . ASP   A 1 64  ? -12.82813 36.13714 6.07591  1.000 50.38008  ? 71  ASP   A OD2 1 
ATOM   455  N N   . SER   A 1 65  ? -11.51373 33.08352 10.63137 1.000 44.88151  ? 72  SER   A N   1 
ATOM   456  C CA  . SER   A 1 65  ? -11.05009 31.87477 11.29421 1.000 41.92455  ? 72  SER   A CA  1 
ATOM   457  C C   . SER   A 1 65  ? -11.65879 31.69923 12.68290 1.000 54.16205  ? 72  SER   A C   1 
ATOM   458  O O   . SER   A 1 65  ? -11.12443 30.93224 13.49266 1.000 51.98888  ? 72  SER   A O   1 
ATOM   459  C CB  . SER   A 1 65  ? -9.52328  31.88810 11.39000 1.000 45.92888  ? 72  SER   A CB  1 
ATOM   460  O OG  . SER   A 1 65  ? -9.04545  33.18800 11.71173 1.000 39.87847  ? 72  SER   A OG  1 
ATOM   461  N N   . GLY   A 1 66  ? -12.75256 32.39857 12.97965 1.000 44.17798  ? 73  GLY   A N   1 
ATOM   462  C CA  . GLY   A 1 66  ? -13.39860 32.27224 14.27098 1.000 46.29536  ? 73  GLY   A CA  1 
ATOM   463  C C   . GLY   A 1 66  ? -13.78591 33.60133 14.88489 1.000 45.18322  ? 73  GLY   A C   1 
ATOM   464  O O   . GLY   A 1 66  ? -12.92895 34.45586 15.13143 1.000 45.48834  ? 73  GLY   A O   1 
ATOM   465  N N   . LYS   A 1 67  ? -15.07933 33.78542 15.13982 1.000 46.52374  ? 74  LYS   A N   1 
ATOM   466  C CA  . LYS   A 1 67  ? -15.57214 35.01982 15.73601 1.000 45.43321  ? 74  LYS   A CA  1 
ATOM   467  C C   . LYS   A 1 67  ? -15.50804 35.00762 17.25727 1.000 50.26067  ? 74  LYS   A C   1 
ATOM   468  O O   . LYS   A 1 67  ? -15.38076 36.07261 17.87270 1.000 46.27263  ? 74  LYS   A O   1 
ATOM   469  C CB  . LYS   A 1 67  ? -17.01393 35.27632 15.29074 1.000 43.98638  ? 74  LYS   A CB  1 
ATOM   470  C CG  . LYS   A 1 67  ? -17.13704 36.15254 14.05475 1.000 61.17156  ? 74  LYS   A CG  1 
ATOM   471  C CD  . LYS   A 1 67  ? -17.42081 35.31841 12.81324 1.000 67.32786  ? 74  LYS   A CD  1 
ATOM   472  C CE  . LYS   A 1 67  ? -16.91343 36.00906 11.55521 1.000 73.30273  ? 74  LYS   A CE  1 
ATOM   473  N NZ  . LYS   A 1 67  ? -16.31535 35.04138 10.59269 1.000 75.15606  ? 74  LYS   A NZ  1 
ATOM   474  N N   . GLU   A 1 68  ? -15.59069 33.83404 17.87700 1.000 45.98465  ? 75  GLU   A N   1 
ATOM   475  C CA  . GLU   A 1 68  ? -15.62633 33.75830 19.33102 1.000 46.99015  ? 75  GLU   A CA  1 
ATOM   476  C C   . GLU   A 1 68  ? -14.26453 34.09847 19.92604 1.000 43.11565  ? 75  GLU   A C   1 
ATOM   477  O O   . GLU   A 1 68  ? -13.22292 33.65252 19.43731 1.000 47.85899  ? 75  GLU   A O   1 
ATOM   478  C CB  . GLU   A 1 68  ? -16.06447 32.36380 19.78161 1.000 47.22209  ? 75  GLU   A CB  1 
ATOM   479  C CG  . GLU   A 1 68  ? -17.03501 31.67113 18.83348 1.000 64.84931  ? 75  GLU   A CG  1 
ATOM   480  C CD  . GLU   A 1 68  ? -16.32889 30.86060 17.75848 1.000 88.42526  ? 75  GLU   A CD  1 
ATOM   481  O OE1 . GLU   A 1 68  ? -15.35757 30.14748 18.09243 1.000 81.25668  ? 75  GLU   A OE1 1 
ATOM   482  O OE2 . GLU   A 1 68  ? -16.74497 30.93861 16.58078 1.000 84.74150  ? 75  GLU   A OE2 1 
ATOM   483  N N   . LEU   A 1 69  ? -14.28205 34.89649 20.99057 1.000 39.05672  ? 76  LEU   A N   1 
ATOM   484  C CA  . LEU   A 1 69  ? -13.08051 35.32576 21.70398 1.000 34.58830  ? 76  LEU   A CA  1 
ATOM   485  C C   . LEU   A 1 69  ? -13.24898 34.89980 23.15687 1.000 36.91694  ? 76  LEU   A C   1 
ATOM   486  O O   . LEU   A 1 69  ? -14.00250 35.52655 23.90792 1.000 36.80198  ? 76  LEU   A O   1 
ATOM   487  C CB  . LEU   A 1 69  ? -12.87942 36.83472 21.58813 1.000 31.08012  ? 76  LEU   A CB  1 
ATOM   488  C CG  . LEU   A 1 69  ? -12.77314 37.42302 20.18159 1.000 40.38213  ? 76  LEU   A CG  1 
ATOM   489  C CD1 . LEU   A 1 69  ? -12.52485 38.92145 20.25632 1.000 39.92813  ? 76  LEU   A CD1 1 
ATOM   490  C CD2 . LEU   A 1 69  ? -11.67467 36.73087 19.39289 1.000 41.45521  ? 76  LEU   A CD2 1 
ATOM   491  N N   . HIS   A 1 70  ? -12.56044 33.83533 23.55905 1.000 32.15157  ? 77  HIS   A N   1 
ATOM   492  C CA  . HIS   A 1 70  ? -12.78337 33.27553 24.88227 1.000 28.26280  ? 77  HIS   A CA  1 
ATOM   493  C C   . HIS   A 1 70  ? -11.54667 32.51196 25.32903 1.000 33.31200  ? 77  HIS   A C   1 
ATOM   494  O O   . HIS   A 1 70  ? -10.59780 32.31417 24.56544 1.000 34.03860  ? 77  HIS   A O   1 
ATOM   495  C CB  . HIS   A 1 70  ? -14.01766 32.36504 24.89768 1.000 28.77012  ? 77  HIS   A CB  1 
ATOM   496  C CG  . HIS   A 1 70  ? -14.01933 31.32489 23.82001 1.000 36.01015  ? 77  HIS   A CG  1 
ATOM   497  N ND1 . HIS   A 1 70  ? -13.10938 30.29019 23.78309 1.000 33.91731  ? 77  HIS   A ND1 1 
ATOM   498  C CD2 . HIS   A 1 70  ? -14.83360 31.14578 22.75336 1.000 38.99285  ? 77  HIS   A CD2 1 
ATOM   499  C CE1 . HIS   A 1 70  ? -13.35519 29.52632 22.73399 1.000 33.85448  ? 77  HIS   A CE1 1 
ATOM   500  N NE2 . HIS   A 1 70  ? -14.39654 30.02362 22.09231 1.000 38.00230  ? 77  HIS   A NE2 1 
ATOM   501  N N   . ILE   A 1 71  ? -11.57127 32.08687 26.59047 1.000 35.47977  ? 78  ILE   A N   1 
ATOM   502  C CA  . ILE   A 1 71  ? -10.51378 31.28168 27.18715 1.000 32.88910  ? 78  ILE   A CA  1 
ATOM   503  C C   . ILE   A 1 71  ? -11.15840 30.06402 27.82746 1.000 33.31498  ? 78  ILE   A C   1 
ATOM   504  O O   . ILE   A 1 71  ? -12.11068 30.20116 28.60353 1.000 35.27305  ? 78  ILE   A O   1 
ATOM   505  C CB  . ILE   A 1 71  ? -9.70868  32.07127 28.23514 1.000 30.95363  ? 78  ILE   A CB  1 
ATOM   506  C CG1 . ILE   A 1 71  ? -9.25164  33.40862 27.65445 1.000 26.33859  ? 78  ILE   A CG1 1 
ATOM   507  C CG2 . ILE   A 1 71  ? -8.51646  31.24645 28.71467 1.000 27.54034  ? 78  ILE   A CG2 1 
ATOM   508  C CD1 . ILE   A 1 71  ? -8.65514  34.36254 28.68079 1.000 34.73487  ? 78  ILE   A CD1 1 
ATOM   509  N N   . ASN   A 1 72  ? -10.64912 28.87698 27.49897 1.000 34.05000  ? 79  ASN   A N   1 
ATOM   510  C CA  . ASN   A 1 72  ? -11.13264 27.62680 28.07090 1.000 33.34074  ? 79  ASN   A CA  1 
ATOM   511  C C   . ASN   A 1 72  ? -10.03268 27.00067 28.91221 1.000 36.15986  ? 79  ASN   A C   1 
ATOM   512  O O   . ASN   A 1 72  ? -8.86947  26.96575 28.49615 1.000 33.32506  ? 79  ASN   A O   1 
ATOM   513  C CB  . ASN   A 1 72  ? -11.57948 26.64522 26.98576 1.000 27.99564  ? 79  ASN   A CB  1 
ATOM   514  C CG  . ASN   A 1 72  ? -12.81219 27.11556 26.25477 1.000 38.72792  ? 79  ASN   A CG  1 
ATOM   515  O OD1 . ASN   A 1 72  ? -13.62521 27.86239 26.80351 1.000 32.81189  ? 79  ASN   A OD1 1 
ATOM   516  N ND2 . ASN   A 1 72  ? -12.96781 26.67424 25.01222 1.000 32.75162  ? 79  ASN   A ND2 1 
ATOM   517  N N   . LEU   A 1 73  ? -10.40234 26.51939 30.09381 1.000 31.10211  ? 80  LEU   A N   1 
ATOM   518  C CA  . LEU   A 1 73  ? -9.49400  25.81506 30.98725 1.000 39.96011  ? 80  LEU   A CA  1 
ATOM   519  C C   . LEU   A 1 73  ? -9.96825  24.37369 31.07450 1.000 35.43052  ? 80  LEU   A C   1 
ATOM   520  O O   . LEU   A 1 73  ? -11.12092 24.11989 31.43789 1.000 35.54560  ? 80  LEU   A O   1 
ATOM   521  C CB  . LEU   A 1 73  ? -9.45912  26.46474 32.36976 1.000 34.64144  ? 80  LEU   A CB  1 
ATOM   522  C CG  . LEU   A 1 73  ? -9.17743  27.96636 32.42208 1.000 28.38721  ? 80  LEU   A CG  1 
ATOM   523  C CD1 . LEU   A 1 73  ? -9.25479  28.45917 33.85481 1.000 30.38126  ? 80  LEU   A CD1 1 
ATOM   524  C CD2 . LEU   A 1 73  ? -7.82193  28.29257 31.82125 1.000 28.38980  ? 80  LEU   A CD2 1 
ATOM   525  N N   . ILE   A 1 74  ? -9.09018  23.44048 30.72373 1.000 34.41760  ? 81  ILE   A N   1 
ATOM   526  C CA  . ILE   A 1 74  ? -9.47003  22.04147 30.55041 1.000 35.89875  ? 81  ILE   A CA  1 
ATOM   527  C C   . ILE   A 1 74  ? -8.51345  21.15366 31.33536 1.000 41.07631  ? 81  ILE   A C   1 
ATOM   528  O O   . ILE   A 1 74  ? -7.42060  20.83712 30.84361 1.000 40.00086  ? 81  ILE   A O   1 
ATOM   529  C CB  . ILE   A 1 74  ? -9.48395  21.65300 29.06305 1.000 34.40158  ? 81  ILE   A CB  1 
ATOM   530  C CG1 . ILE   A 1 74  ? -10.31110 22.66036 28.25826 1.000 39.18966  ? 81  ILE   A CG1 1 
ATOM   531  C CG2 . ILE   A 1 74  ? -10.02147 20.24159 28.88062 1.000 38.09016  ? 81  ILE   A CG2 1 
ATOM   532  C CD1 . ILE   A 1 74  ? -10.11830 22.56726 26.76327 1.000 40.26940  ? 81  ILE   A CD1 1 
ATOM   533  N N   . PRO   A 1 75  ? -8.86638  20.74527 32.55090 1.000 35.82340  ? 82  PRO   A N   1 
ATOM   534  C CA  . PRO   A 1 75  ? -8.05256  19.76088 33.26256 1.000 34.89973  ? 82  PRO   A CA  1 
ATOM   535  C C   . PRO   A 1 75  ? -8.38350  18.34904 32.81337 1.000 49.06271  ? 82  PRO   A C   1 
ATOM   536  O O   . PRO   A 1 75  ? -9.51196  18.03905 32.42328 1.000 43.57966  ? 82  PRO   A O   1 
ATOM   537  C CB  . PRO   A 1 75  ? -8.44616  19.97675 34.72772 1.000 41.84075  ? 82  PRO   A CB  1 
ATOM   538  C CG  . PRO   A 1 75  ? -9.86413  20.43100 34.65011 1.000 41.27815  ? 82  PRO   A CG  1 
ATOM   539  C CD  . PRO   A 1 75  ? -9.98091  21.24179 33.37756 1.000 34.01561  ? 82  PRO   A CD  1 
ATOM   540  N N   . ASN   A 1 76  ? -7.37274  17.48518 32.88163 1.000 43.82660  ? 83  ASN   A N   1 
ATOM   541  C CA  . ASN   A 1 76  ? -7.51934  16.08222 32.49886 1.000 44.02419  ? 83  ASN   A CA  1 
ATOM   542  C C   . ASN   A 1 76  ? -6.75394  15.24444 33.51792 1.000 47.43556  ? 83  ASN   A C   1 
ATOM   543  O O   . ASN   A 1 76  ? -5.52662  15.13236 33.43858 1.000 42.42521  ? 83  ASN   A O   1 
ATOM   544  C CB  . ASN   A 1 76  ? -7.01268  15.84153 31.08180 1.000 41.51680  ? 83  ASN   A CB  1 
ATOM   545  C CG  . ASN   A 1 76  ? -7.44086  14.49505 30.53192 1.000 48.09820  ? 83  ASN   A CG  1 
ATOM   546  O OD1 . ASN   A 1 76  ? -7.15768  13.44976 31.11933 1.000 58.23745  ? 83  ASN   A OD1 1 
ATOM   547  N ND2 . ASN   A 1 76  ? -8.13639  14.51446 29.40373 1.000 52.60666  ? 83  ASN   A ND2 1 
ATOM   548  N N   . LYS   A 1 77  ? -7.48450  14.65442 34.46921 1.000 47.71609  ? 84  LYS   A N   1 
ATOM   549  C CA  . LYS   A 1 77  ? -6.84240  13.86772 35.51786 1.000 47.68334  ? 84  LYS   A CA  1 
ATOM   550  C C   . LYS   A 1 77  ? -6.20086  12.59983 34.96717 1.000 47.09759  ? 84  LYS   A C   1 
ATOM   551  O O   . LYS   A 1 77  ? -5.17780  12.14990 35.49595 1.000 46.23843  ? 84  LYS   A O   1 
ATOM   552  C CB  . LYS   A 1 77  ? -7.85482  13.51599 36.60978 1.000 50.86861  ? 84  LYS   A CB  1 
ATOM   553  C CG  . LYS   A 1 77  ? -8.15175  14.65357 37.57863 1.000 52.62940  ? 84  LYS   A CG  1 
ATOM   554  C CD  . LYS   A 1 77  ? -8.72898  14.12995 38.88997 1.000 66.12243  ? 84  LYS   A CD  1 
ATOM   555  C CE  . LYS   A 1 77  ? -9.32496  15.24905 39.73665 1.000 63.38239  ? 84  LYS   A CE  1 
ATOM   556  N NZ  . LYS   A 1 77  ? -10.66300 15.68716 39.24718 1.000 75.93796  ? 84  LYS   A NZ  1 
ATOM   557  N N   . GLN   A 1 78  ? -6.77705  12.01191 33.91454 1.000 53.59574  ? 85  GLN   A N   1 
ATOM   558  C CA  . GLN   A 1 78  ? -6.21312  10.78794 33.34848 1.000 52.20979  ? 85  GLN   A CA  1 
ATOM   559  C C   . GLN   A 1 78  ? -4.83296  11.03950 32.75300 1.000 53.64647  ? 85  GLN   A C   1 
ATOM   560  O O   . GLN   A 1 78  ? -3.86928  10.33487 33.07400 1.000 61.17803  ? 85  GLN   A O   1 
ATOM   561  C CB  . GLN   A 1 78  ? -7.15499  10.21121 32.29040 1.000 53.00111  ? 85  GLN   A CB  1 
ATOM   562  C CG  . GLN   A 1 78  ? -7.23760  8.69146  32.28947 1.000 71.70991  ? 85  GLN   A CG  1 
ATOM   563  C CD  . GLN   A 1 78  ? -8.17207  8.15578  33.35758 1.000 90.55780  ? 85  GLN   A CD  1 
ATOM   564  O OE1 . GLN   A 1 78  ? -9.27738  8.66653  33.54374 1.000 99.74568  ? 85  GLN   A OE1 1 
ATOM   565  N NE2 . GLN   A 1 78  ? -7.73266  7.11877  34.06496 1.000 65.62447  ? 85  GLN   A NE2 1 
ATOM   566  N N   . ASP   A 1 79  ? -4.72104  12.03700 31.87632 1.000 46.75172  ? 86  ASP   A N   1 
ATOM   567  C CA  . ASP   A 1 79  ? -3.44823  12.38530 31.25774 1.000 49.01382  ? 86  ASP   A CA  1 
ATOM   568  C C   . ASP   A 1 79  ? -2.56313  13.24151 32.15274 1.000 44.62339  ? 86  ASP   A C   1 
ATOM   569  O O   . ASP   A 1 79  ? -1.40526  13.48477 31.79515 1.000 46.76281  ? 86  ASP   A O   1 
ATOM   570  C CB  . ASP   A 1 79  ? -3.69120  13.13180 29.94491 1.000 46.82080  ? 86  ASP   A CB  1 
ATOM   571  C CG  . ASP   A 1 79  ? -4.61613  12.38259 29.01108 1.000 66.27688  ? 86  ASP   A CG  1 
ATOM   572  O OD1 . ASP   A 1 79  ? -4.80483  11.16198 29.20702 1.000 67.05433  ? 86  ASP   A OD1 1 
ATOM   573  O OD2 . ASP   A 1 79  ? -5.16385  13.02113 28.08677 1.000 60.38901  ? 86  ASP   A OD2 1 
ATOM   574  N N   . ARG   A 1 80  ? -3.08187  13.71178 33.28760 1.000 47.43380  ? 87  ARG   A N   1 
ATOM   575  C CA  . ARG   A 1 80  ? -2.36233  14.62891 34.17051 1.000 49.09206  ? 87  ARG   A CA  1 
ATOM   576  C C   . ARG   A 1 80  ? -1.91889  15.88281 33.41639 1.000 43.44547  ? 87  ARG   A C   1 
ATOM   577  O O   . ARG   A 1 80  ? -0.76677  16.31293 33.50307 1.000 41.84239  ? 87  ARG   A O   1 
ATOM   578  C CB  . ARG   A 1 80  ? -1.17076  13.93405 34.83773 1.000 44.37123  ? 87  ARG   A CB  1 
ATOM   579  C CG  . ARG   A 1 80  ? -0.88819  14.42628 36.24751 1.000 56.32712  ? 87  ARG   A CG  1 
ATOM   580  C CD  . ARG   A 1 80  ? -0.05328  13.43293 37.03506 1.000 56.73850  ? 87  ARG   A CD  1 
ATOM   581  N NE  . ARG   A 1 80  ? 1.37075   13.57940 36.76331 1.000 64.37813  ? 87  ARG   A NE  1 
ATOM   582  C CZ  . ARG   A 1 80  ? 2.13989   12.62167 36.26510 1.000 73.07424  ? 87  ARG   A CZ  1 
ATOM   583  N NH1 . ARG   A 1 80  ? 1.65259   11.42783 35.97084 1.000 79.86558  ? 87  ARG   A NH1 1 
ATOM   584  N NH2 . ARG   A 1 80  ? 3.43073   12.86763 36.05888 1.000 69.75001  ? 87  ARG   A NH2 1 
ATOM   585  N N   . THR   A 1 81  ? -2.85013  16.47100 32.66167 1.000 39.03552  ? 88  THR   A N   1 
ATOM   586  C CA  . THR   A 1 81  ? -2.58999  17.70160 31.92705 1.000 38.44976  ? 88  THR   A CA  1 
ATOM   587  C C   . THR   A 1 81  ? -3.63191  18.75388 32.27166 1.000 42.91019  ? 88  THR   A C   1 
ATOM   588  O O   . THR   A 1 81  ? -4.80067  18.43604 32.50966 1.000 38.27505  ? 88  THR   A O   1 
ATOM   589  C CB  . THR   A 1 81  ? -2.59925  17.49548 30.40038 1.000 37.28982  ? 88  THR   A CB  1 
ATOM   590  O OG1 . THR   A 1 81  ? -3.87887  16.99828 29.99109 1.000 40.09441  ? 88  THR   A OG1 1 
ATOM   591  C CG2 . THR   A 1 81  ? -1.50407  16.52931 29.96350 1.000 34.51439  ? 88  THR   A CG2 1 
ATOM   592  N N   . LEU   A 1 82  ? -3.19656  20.00853 32.28924 1.000 37.99235  ? 89  LEU   A N   1 
ATOM   593  C CA  . LEU   A 1 82  ? -4.08506  21.15863 32.33664 1.000 35.14701  ? 89  LEU   A CA  1 
ATOM   594  C C   . LEU   A 1 82  ? -3.86890  21.95107 31.05956 1.000 35.70266  ? 89  LEU   A C   1 
ATOM   595  O O   . LEU   A 1 82  ? -2.73028  22.29479 30.72397 1.000 34.96025  ? 89  LEU   A O   1 
ATOM   596  C CB  . LEU   A 1 82  ? -3.81582  22.02671 33.56839 1.000 31.14877  ? 89  LEU   A CB  1 
ATOM   597  C CG  . LEU   A 1 82  ? -4.57925  23.34914 33.67447 1.000 30.06868  ? 89  LEU   A CG  1 
ATOM   598  C CD1 . LEU   A 1 82  ? -6.08143  23.12031 33.60653 1.000 30.17853  ? 89  LEU   A CD1 1 
ATOM   599  C CD2 . LEU   A 1 82  ? -4.20620  24.05175 34.96649 1.000 30.52899  ? 89  LEU   A CD2 1 
ATOM   600  N N   . THR   A 1 83  ? -4.95089  22.22060 30.34032 1.000 30.64539  ? 90  THR   A N   1 
ATOM   601  C CA  . THR   A 1 83  ? -4.87740  22.86271 29.03727 1.000 34.38173  ? 90  THR   A CA  1 
ATOM   602  C C   . THR   A 1 83  ? -5.57211  24.21365 29.10510 1.000 34.18772  ? 90  THR   A C   1 
ATOM   603  O O   . THR   A 1 83  ? -6.68556  24.31661 29.63258 1.000 33.50474  ? 90  THR   A O   1 
ATOM   604  C CB  . THR   A 1 83  ? -5.51500  21.97773 27.95861 1.000 36.06491  ? 90  THR   A CB  1 
ATOM   605  O OG1 . THR   A 1 83  ? -4.74008  20.78241 27.80612 1.000 40.58050  ? 90  THR   A OG1 1 
ATOM   606  C CG2 . THR   A 1 83  ? -5.55964  22.70076 26.62979 1.000 36.97623  ? 90  THR   A CG2 1 
ATOM   607  N N   . ILE   A 1 84  ? -4.90679  25.24342 28.58455 1.000 31.13481  ? 91  ILE   A N   1 
ATOM   608  C CA  . ILE   A 1 84  ? -5.45209  26.59532 28.49255 1.000 33.21931  ? 91  ILE   A CA  1 
ATOM   609  C C   . ILE   A 1 84  ? -5.58831  26.93318 27.01156 1.000 33.56583  ? 91  ILE   A C   1 
ATOM   610  O O   . ILE   A 1 84  ? -4.58517  26.97285 26.28895 1.000 31.81443  ? 91  ILE   A O   1 
ATOM   611  C CB  . ILE   A 1 84  ? -4.56977  27.63294 29.21532 1.000 29.62013  ? 91  ILE   A CB  1 
ATOM   612  C CG1 . ILE   A 1 84  ? -4.36303  27.28135 30.69660 1.000 35.53873  ? 91  ILE   A CG1 1 
ATOM   613  C CG2 . ILE   A 1 84  ? -5.16997  29.02770 29.10291 1.000 30.95008  ? 91  ILE   A CG2 1 
ATOM   614  C CD1 . ILE   A 1 84  ? -3.24488  26.30409 30.98545 1.000 47.97776  ? 91  ILE   A CD1 1 
ATOM   615  N N   . VAL   A 1 85  ? -6.82227  27.16591 26.55888 1.000 29.33289  ? 92  VAL   A N   1 
ATOM   616  C CA  . VAL   A 1 85  ? -7.12215  27.43255 25.15425 1.000 29.59977  ? 92  VAL   A CA  1 
ATOM   617  C C   . VAL   A 1 85  ? -7.66106  28.85059 25.02513 1.000 42.73930  ? 92  VAL   A C   1 
ATOM   618  O O   . VAL   A 1 85  ? -8.60725  29.22350 25.72720 1.000 38.84944  ? 92  VAL   A O   1 
ATOM   619  C CB  . VAL   A 1 85  ? -8.14705  26.43548 24.58174 1.000 32.60844  ? 92  VAL   A CB  1 
ATOM   620  C CG1 . VAL   A 1 85  ? -8.43690  26.76288 23.11158 1.000 33.04254  ? 92  VAL   A CG1 1 
ATOM   621  C CG2 . VAL   A 1 85  ? -7.66843  25.00742 24.73549 1.000 35.70131  ? 92  VAL   A CG2 1 
ATOM   622  N N   . ASP   A 1 86  ? -7.07592  29.63090 24.11679 1.000 30.99482  ? 93  ASP   A N   1 
ATOM   623  C CA  . ASP   A 1 86  ? -7.62277  30.92472 23.73223 1.000 29.52418  ? 93  ASP   A CA  1 
ATOM   624  C C   . ASP   A 1 86  ? -7.78264  30.98200 22.22234 1.000 35.04348  ? 93  ASP   A C   1 
ATOM   625  O O   . ASP   A 1 86  ? -7.09396  30.27622 21.48154 1.000 30.71241  ? 93  ASP   A O   1 
ATOM   626  C CB  . ASP   A 1 86  ? -6.74477  32.10185 24.20648 1.000 26.20198  ? 93  ASP   A CB  1 
ATOM   627  C CG  . ASP   A 1 86  ? -5.42501  32.20657 23.44657 1.000 37.99471  ? 93  ASP   A CG  1 
ATOM   628  O OD1 . ASP   A 1 86  ? -4.37819  31.82977 24.02182 1.000 38.09523  ? 93  ASP   A OD1 1 
ATOM   629  O OD2 . ASP   A 1 86  ? -5.42736  32.65238 22.27811 1.000 36.38851  ? 93  ASP   A OD2 1 
ATOM   630  N N   . THR   A 1 87  ? -8.69743  31.83643 21.77055 1.000 32.36899  ? 94  THR   A N   1 
ATOM   631  C CA  . THR   A 1 87  ? -8.89994  32.07817 20.34484 1.000 27.79060  ? 94  THR   A CA  1 
ATOM   632  C C   . THR   A 1 87  ? -8.28286  33.40389 19.91493 1.000 32.88062  ? 94  THR   A C   1 
ATOM   633  O O   . THR   A 1 87  ? -8.81763  34.11691 19.06060 1.000 29.30997  ? 94  THR   A O   1 
ATOM   634  C CB  . THR   A 1 87  ? -10.38496 32.02277 20.00675 1.000 37.65390  ? 94  THR   A CB  1 
ATOM   635  O OG1 . THR   A 1 87  ? -11.12192 32.80749 20.95081 1.000 34.05011  ? 94  THR   A OG1 1 
ATOM   636  C CG2 . THR   A 1 87  ? -10.87851 30.57881 20.07819 1.000 32.27410  ? 94  THR   A CG2 1 
ATOM   637  N N   . GLY   A 1 88  ? -7.13640  33.74454 20.50031 1.000 30.58649  ? 95  GLY   A N   1 
ATOM   638  C CA  . GLY   A 1 88  ? -6.43809  34.97537 20.18670 1.000 32.25424  ? 95  GLY   A CA  1 
ATOM   639  C C   . GLY   A 1 88  ? -5.75060  34.95845 18.83590 1.000 32.73926  ? 95  GLY   A C   1 
ATOM   640  O O   . GLY   A 1 88  ? -6.03408  34.10114 17.99290 1.000 34.83026  ? 95  GLY   A O   1 
ATOM   641  N N   . ILE   A 1 89  ? -4.82666  35.89924 18.62708 1.000 30.01022  ? 96  ILE   A N   1 
ATOM   642  C CA  . ILE   A 1 89  ? -4.21623  36.08053 17.31526 1.000 37.57069  ? 96  ILE   A CA  1 
ATOM   643  C C   . ILE   A 1 89  ? -3.32784  34.90408 16.92035 1.000 38.10202  ? 96  ILE   A C   1 
ATOM   644  O O   . ILE   A 1 89  ? -3.04585  34.71836 15.72902 1.000 33.13737  ? 96  ILE   A O   1 
ATOM   645  C CB  . ILE   A 1 89  ? -3.43709  37.41187 17.28715 1.000 36.54840  ? 96  ILE   A CB  1 
ATOM   646  C CG1 . ILE   A 1 89  ? -3.11397  37.81833 15.84671 1.000 36.74364  ? 96  ILE   A CG1 1 
ATOM   647  C CG2 . ILE   A 1 89  ? -2.18020  37.32179 18.14201 1.000 29.52282  ? 96  ILE   A CG2 1 
ATOM   648  C CD1 . ILE   A 1 89  ? -2.51592  39.19292 15.71650 1.000 41.92378  ? 96  ILE   A CD1 1 
ATOM   649  N N   . GLY   A 1 90  ? -2.89511  34.08807 17.87947 1.000 28.74139  ? 97  GLY   A N   1 
ATOM   650  C CA  . GLY   A 1 90  ? -2.03665  32.96239 17.57191 1.000 28.98916  ? 97  GLY   A CA  1 
ATOM   651  C C   . GLY   A 1 90  ? -0.60107  33.38910 17.34259 1.000 30.70231  ? 97  GLY   A C   1 
ATOM   652  O O   . GLY   A 1 90  ? -0.23148  34.55631 17.46982 1.000 35.91995  ? 97  GLY   A O   1 
ATOM   653  N N   . MET   A 1 91  ? 0.22586   32.41174 16.97957 1.000 30.77707  ? 98  MET   A N   1 
ATOM   654  C CA  . MET   A 1 91  ? 1.65921   32.62093 16.85264 1.000 32.44677  ? 98  MET   A CA  1 
ATOM   655  C C   . MET   A 1 91  ? 2.15105   32.01565 15.54364 1.000 37.32552  ? 98  MET   A C   1 
ATOM   656  O O   . MET   A 1 91  ? 1.71454   30.92945 15.14951 1.000 36.73069  ? 98  MET   A O   1 
ATOM   657  C CB  . MET   A 1 91  ? 2.39336   32.00119 18.04932 1.000 39.20173  ? 98  MET   A CB  1 
ATOM   658  C CG  . MET   A 1 91  ? 2.63820   32.97419 19.20477 1.000 38.91911  ? 98  MET   A CG  1 
ATOM   659  S SD  . MET   A 1 91  ? 3.18619   32.15265 20.72373 1.000 38.38144  ? 98  MET   A SD  1 
ATOM   660  C CE  . MET   A 1 91  ? 1.81057   31.05192 21.04797 1.000 37.87996  ? 98  MET   A CE  1 
ATOM   661  N N   . THR   A 1 92  ? 3.04536   32.73044 14.86430 1.000 39.17629  ? 99  THR   A N   1 
ATOM   662  C CA  . THR   A 1 92  ? 3.65809   32.25736 13.63084 1.000 32.24730  ? 99  THR   A CA  1 
ATOM   663  C C   . THR   A 1 92  ? 4.87663   31.38993 13.94443 1.000 36.86644  ? 99  THR   A C   1 
ATOM   664  O O   . THR   A 1 92  ? 5.28061   31.23783 15.09777 1.000 31.72099  ? 99  THR   A O   1 
ATOM   665  C CB  . THR   A 1 92  ? 4.06677   33.43628 12.74768 1.000 36.45882  ? 99  THR   A CB  1 
ATOM   666  O OG1 . THR   A 1 92  ? 5.00247   34.25958 13.45702 1.000 39.64449  ? 99  THR   A OG1 1 
ATOM   667  C CG2 . THR   A 1 92  ? 2.85354   34.27088 12.36801 1.000 32.29279  ? 99  THR   A CG2 1 
ATOM   668  N N   . LYS   A 1 93  ? 5.47566   30.81625 12.89722 1.000 33.38646  ? 100 LYS   A N   1 
ATOM   669  C CA  . LYS   A 1 93  ? 6.69369   30.03919 13.10995 1.000 40.10599  ? 100 LYS   A CA  1 
ATOM   670  C C   . LYS   A 1 93  ? 7.82288   30.92758 13.61430 1.000 37.62175  ? 100 LYS   A C   1 
ATOM   671  O O   . LYS   A 1 93  ? 8.58567   30.53221 14.50451 1.000 44.26739  ? 100 LYS   A O   1 
ATOM   672  C CB  . LYS   A 1 93  ? 7.10845   29.32146 11.82443 1.000 36.73978  ? 100 LYS   A CB  1 
ATOM   673  C CG  . LYS   A 1 93  ? 8.07913   28.16431 12.05108 1.000 33.31819  ? 100 LYS   A CG  1 
ATOM   674  C CD  . LYS   A 1 93  ? 8.59433   27.59985 10.73312 1.000 44.68863  ? 100 LYS   A CD  1 
ATOM   675  C CE  . LYS   A 1 93  ? 9.51829   26.40795 10.95035 1.000 59.55005  ? 100 LYS   A CE  1 
ATOM   676  N NZ  . LYS   A 1 93  ? 10.06927  25.89411 9.65915  1.000 60.61042  ? 100 LYS   A NZ  1 
ATOM   677  N N   . ALA   A 1 94  ? 7.93465   32.14021 13.06776 1.000 32.35560  ? 101 ALA   A N   1 
ATOM   678  C CA  . ALA   A 1 94  ? 8.97918   33.05682 13.50770 1.000 40.86762  ? 101 ALA   A CA  1 
ATOM   679  C C   . ALA   A 1 94  ? 8.77412   33.49651 14.95269 1.000 42.74468  ? 101 ALA   A C   1 
ATOM   680  O O   . ALA   A 1 94  ? 9.75391   33.67233 15.68553 1.000 45.27665  ? 101 ALA   A O   1 
ATOM   681  C CB  . ALA   A 1 94  ? 9.03683   34.27004 12.57887 1.000 36.77224  ? 101 ALA   A CB  1 
ATOM   682  N N   . ASP   A 1 95  ? 7.52156   33.68308 15.38017 1.000 36.64503  ? 102 ASP   A N   1 
ATOM   683  C CA  . ASP   A 1 95  ? 7.25439   33.97761 16.78734 1.000 28.05760  ? 102 ASP   A CA  1 
ATOM   684  C C   . ASP   A 1 95  ? 7.79596   32.87352 17.68677 1.000 45.17760  ? 102 ASP   A C   1 
ATOM   685  O O   . ASP   A 1 95  ? 8.51061   33.13949 18.66043 1.000 38.75343  ? 102 ASP   A O   1 
ATOM   686  C CB  . ASP   A 1 95  ? 5.75238   34.14741 17.02260 1.000 33.13921  ? 102 ASP   A CB  1 
ATOM   687  C CG  . ASP   A 1 95  ? 5.20916   35.44304 16.45973 1.000 36.96715  ? 102 ASP   A CG  1 
ATOM   688  O OD1 . ASP   A 1 95  ? 5.96340   36.43865 16.41139 1.000 41.21527  ? 102 ASP   A OD1 1 
ATOM   689  O OD2 . ASP   A 1 95  ? 4.01713   35.46703 16.07989 1.000 37.17244  ? 102 ASP   A OD2 1 
ATOM   690  N N   . LEU   A 1 96  ? 7.46301   31.62049 17.36589 1.000 37.59545  ? 103 LEU   A N   1 
ATOM   691  C CA  . LEU   A 1 96  ? 7.84991   30.49415 18.20826 1.000 40.69195  ? 103 LEU   A CA  1 
ATOM   692  C C   . LEU   A 1 96  ? 9.36357   30.34467 18.28912 1.000 37.30318  ? 103 LEU   A C   1 
ATOM   693  O O   . LEU   A 1 96  ? 9.90587   30.01788 19.35060 1.000 44.66887  ? 103 LEU   A O   1 
ATOM   694  C CB  . LEU   A 1 96  ? 7.22196   29.21030 17.66950 1.000 33.86442  ? 103 LEU   A CB  1 
ATOM   695  C CG  . LEU   A 1 96  ? 5.69680   29.14726 17.68976 1.000 36.43647  ? 103 LEU   A CG  1 
ATOM   696  C CD1 . LEU   A 1 96  ? 5.22038   27.84914 17.06172 1.000 38.08666  ? 103 LEU   A CD1 1 
ATOM   697  C CD2 . LEU   A 1 96  ? 5.19273   29.26966 19.11434 1.000 28.45205  ? 103 LEU   A CD2 1 
ATOM   698  N N   . ILE   A 1 97  ? 10.06132  30.58166 17.18266 1.000 36.23933  ? 104 ILE   A N   1 
ATOM   699  C CA  . ILE   A 1 97  ? 11.49114  30.29864 17.11732 1.000 42.73776  ? 104 ILE   A CA  1 
ATOM   700  C C   . ILE   A 1 97  ? 12.33353  31.51750 17.48139 1.000 49.49376  ? 104 ILE   A C   1 
ATOM   701  O O   . ILE   A 1 97  ? 13.33303  31.39028 18.19300 1.000 55.05692  ? 104 ILE   A O   1 
ATOM   702  C CB  . ILE   A 1 97  ? 11.84885  29.76355 15.71595 1.000 46.84651  ? 104 ILE   A CB  1 
ATOM   703  C CG1 . ILE   A 1 97  ? 11.15413  28.42414 15.46231 1.000 44.46548  ? 104 ILE   A CG1 1 
ATOM   704  C CG2 . ILE   A 1 97  ? 13.35110  29.61771 15.56422 1.000 46.24363  ? 104 ILE   A CG2 1 
ATOM   705  C CD1 . ILE   A 1 97  ? 11.18889  27.98436 14.01432 1.000 41.93183  ? 104 ILE   A CD1 1 
ATOM   706  N N   . ASN   A 1 98  ? 11.95716  32.71435 17.02437 1.000 44.94531  ? 105 ASN   A N   1 
ATOM   707  C CA  . ASN   A 1 98  ? 12.87301  33.84806 17.11477 1.000 51.94773  ? 105 ASN   A CA  1 
ATOM   708  C C   . ASN   A 1 98  ? 12.29769  35.07320 17.81703 1.000 51.25874  ? 105 ASN   A C   1 
ATOM   709  O O   . ASN   A 1 98  ? 12.85606  35.53605 18.81841 1.000 53.94884  ? 105 ASN   A O   1 
ATOM   710  C CB  . ASN   A 1 98  ? 13.33555  34.25756 15.71646 1.000 43.03126  ? 105 ASN   A CB  1 
ATOM   711  C CG  . ASN   A 1 98  ? 14.80087  33.96740 15.48360 1.000 64.42364  ? 105 ASN   A CG  1 
ATOM   712  O OD1 . ASN   A 1 98  ? 15.66426  34.40737 16.24531 1.000 68.20395  ? 105 ASN   A OD1 1 
ATOM   713  N ND2 . ASN   A 1 98  ? 15.09255  33.22377 14.42394 1.000 69.26785  ? 105 ASN   A ND2 1 
ATOM   714  N N   . ASN   A 1 99  ? 11.19853  35.62045 17.29171 1.000 40.58593  ? 106 ASN   A N   1 
ATOM   715  C CA  . ASN   A 1 99  ? 10.82420  36.99088 17.64074 1.000 56.07275  ? 106 ASN   A CA  1 
ATOM   716  C C   . ASN   A 1 99  ? 10.44768  37.11724 19.11172 1.000 48.96233  ? 106 ASN   A C   1 
ATOM   717  O O   . ASN   A 1 99  ? 10.86091  38.06573 19.78845 1.000 56.37015  ? 106 ASN   A O   1 
ATOM   718  C CB  . ASN   A 1 99  ? 9.68018   37.48315 16.75264 1.000 43.10294  ? 106 ASN   A CB  1 
ATOM   719  C CG  . ASN   A 1 99  ? 9.95798   37.28310 15.27602 1.000 52.06708  ? 106 ASN   A CG  1 
ATOM   720  O OD1 . ASN   A 1 99  ? 11.05695  37.56422 14.79575 1.000 48.17139  ? 106 ASN   A OD1 1 
ATOM   721  N ND2 . ASN   A 1 99  ? 8.93989   36.85941 14.53548 1.000 56.72803  ? 106 ASN   A ND2 1 
ATOM   722  N N   . LEU   A 1 100 ? 9.65847   36.17325 19.62602 1.000 48.72776  ? 107 LEU   A N   1 
ATOM   723  C CA  . LEU   A 1 100 ? 9.22129   36.27162 21.01494 1.000 53.66553  ? 107 LEU   A CA  1 
ATOM   724  C C   . LEU   A 1 100 ? 10.38966  36.09929 21.97832 1.000 50.48572  ? 107 LEU   A C   1 
ATOM   725  O O   . LEU   A 1 100 ? 10.50136  36.83871 22.96302 1.000 51.54847  ? 107 LEU   A O   1 
ATOM   726  C CB  . LEU   A 1 100 ? 8.12729   35.24367 21.29637 1.000 46.79896  ? 107 LEU   A CB  1 
ATOM   727  C CG  . LEU   A 1 100 ? 6.78778   35.51581 20.60872 1.000 49.56064  ? 107 LEU   A CG  1 
ATOM   728  C CD1 . LEU   A 1 100 ? 5.70353   34.61524 21.17763 1.000 46.87735  ? 107 LEU   A CD1 1 
ATOM   729  C CD2 . LEU   A 1 100 ? 6.40095   36.97764 20.74647 1.000 32.69794  ? 107 LEU   A CD2 1 
ATOM   730  N N   . GLY   A 1 101 ? 11.27351  35.13580 21.70954 1.000 48.63610  ? 108 GLY   A N   1 
ATOM   731  C CA  . GLY   A 1 101 ? 12.45121  34.97169 22.54423 1.000 50.02878  ? 108 GLY   A CA  1 
ATOM   732  C C   . GLY   A 1 101 ? 13.39358  36.15678 22.48363 1.000 58.75807  ? 108 GLY   A C   1 
ATOM   733  O O   . GLY   A 1 101 ? 14.08408  36.45479 23.46304 1.000 62.93670  ? 108 GLY   A O   1 
ATOM   734  N N   . THR   A 1 102 ? 13.43771  36.84852 21.34152 1.000 54.05063  ? 109 THR   A N   1 
ATOM   735  C CA  . THR   A 1 102 ? 14.26744  38.04513 21.23188 1.000 61.26851  ? 109 THR   A CA  1 
ATOM   736  C C   . THR   A 1 102 ? 13.73253  39.17268 22.10893 1.000 56.79938  ? 109 THR   A C   1 
ATOM   737  O O   . THR   A 1 102 ? 14.51012  39.90901 22.72789 1.000 60.56885  ? 109 THR   A O   1 
ATOM   738  C CB  . THR   A 1 102 ? 14.35370  38.49445 19.77150 1.000 52.28494  ? 109 THR   A CB  1 
ATOM   739  O OG1 . THR   A 1 102 ? 14.87979  37.42907 18.96950 1.000 54.82030  ? 109 THR   A OG1 1 
ATOM   740  C CG2 . THR   A 1 102 ? 15.25214  39.71570 19.63580 1.000 52.67686  ? 109 THR   A CG2 1 
ATOM   741  N N   . ILE   A 1 103 ? 12.40785  39.32111 22.17652 1.000 56.59988  ? 110 ILE   A N   1 
ATOM   742  C CA  . ILE   A 1 103 ? 11.80966  40.35799 23.01206 1.000 58.97525  ? 110 ILE   A CA  1 
ATOM   743  C C   . ILE   A 1 103 ? 11.92835  39.99826 24.48674 1.000 60.34414  ? 110 ILE   A C   1 
ATOM   744  O O   . ILE   A 1 103 ? 12.05349  40.88247 25.34371 1.000 69.04298  ? 110 ILE   A O   1 
ATOM   745  C CB  . ILE   A 1 103 ? 10.34239  40.57607 22.59783 1.000 51.42186  ? 110 ILE   A CB  1 
ATOM   746  C CG1 . ILE   A 1 103 ? 10.26683  41.04966 21.14507 1.000 45.98549  ? 110 ILE   A CG1 1 
ATOM   747  C CG2 . ILE   A 1 103 ? 9.64455   41.55440 23.53017 1.000 51.59995  ? 110 ILE   A CG2 1 
ATOM   748  C CD1 . ILE   A 1 103 ? 10.39121  42.55234 20.98128 1.000 52.32250  ? 110 ILE   A CD1 1 
ATOM   749  N N   . ALA   A 1 104 ? 11.89342  38.70565 24.80948 1.000 53.57854  ? 111 ALA   A N   1 
ATOM   750  C CA  . ALA   A 1 104 ? 11.98795  38.25577 26.19019 1.000 56.47308  ? 111 ALA   A CA  1 
ATOM   751  C C   . ALA   A 1 104 ? 13.40946  38.30248 26.72702 1.000 65.83824  ? 111 ALA   A C   1 
ATOM   752  O O   . ALA   A 1 104 ? 13.61437  38.03131 27.91581 1.000 66.89826  ? 111 ALA   A O   1 
ATOM   753  C CB  . ALA   A 1 104 ? 11.44088  36.83259 26.31758 1.000 38.79705  ? 111 ALA   A CB  1 
ATOM   754  N N   . LYS   A 1 105 ? 14.39071  38.63403 25.88480 1.000 64.83057  ? 112 LYS   A N   1 
ATOM   755  C CA  . LYS   A 1 105 ? 15.77556  38.66028 26.34170 1.000 53.82869  ? 112 LYS   A CA  1 
ATOM   756  C C   . LYS   A 1 105 ? 15.94909  39.67614 27.46470 1.000 61.36730  ? 112 LYS   A C   1 
ATOM   757  O O   . LYS   A 1 105 ? 16.38944  39.33610 28.56843 1.000 67.10000  ? 112 LYS   A O   1 
ATOM   758  C CB  . LYS   A 1 105 ? 16.71914  38.98282 25.17643 1.000 61.04079  ? 112 LYS   A CB  1 
ATOM   759  C CG  . LYS   A 1 105 ? 17.45991  37.76584 24.61442 1.000 68.52743  ? 112 LYS   A CG  1 
ATOM   760  C CD  . LYS   A 1 105 ? 17.92403  37.98316 23.15564 1.000 71.94899  ? 112 LYS   A CD  1 
ATOM   761  C CE  . LYS   A 1 105 ? 18.86590  39.15515 23.09680 1.000 76.17693  ? 112 LYS   A CE  1 
ATOM   762  N NZ  . LYS   A 1 105 ? 20.12923  38.70765 23.71903 1.000 72.82768  ? 112 LYS   A NZ  1 
ATOM   763  N N   . SER   A 1 106 ? 15.57304  40.92800 27.20164 1.000 60.27743  ? 113 SER   A N   1 
ATOM   764  C CA  . SER   A 1 106 ? 15.74527  41.99880 28.17703 1.000 58.42297  ? 113 SER   A CA  1 
ATOM   765  C C   . SER   A 1 106 ? 14.94099  41.74620 29.44488 1.000 56.78437  ? 113 SER   A C   1 
ATOM   766  O O   . SER   A 1 106 ? 15.40312  42.05285 30.55022 1.000 50.60284  ? 113 SER   A O   1 
ATOM   767  C CB  . SER   A 1 106 ? 15.32945  43.32162 27.54578 1.000 69.56039  ? 113 SER   A CB  1 
ATOM   768  O OG  . SER   A 1 106 ? 14.60631  43.05942 26.35052 1.000 70.52736  ? 113 SER   A OG  1 
ATOM   769  N N   . GLY   A 1 107 ? 13.72678  41.21005 29.30583 1.000 57.79659  ? 114 GLY   A N   1 
ATOM   770  C CA  . GLY   A 1 107 ? 12.91297  40.93866 30.47971 1.000 49.98192  ? 114 GLY   A CA  1 
ATOM   771  C C   . GLY   A 1 107 ? 13.50445  39.85477 31.35959 1.000 47.20048  ? 114 GLY   A C   1 
ATOM   772  O O   . GLY   A 1 107 ? 13.46263  39.94970 32.58947 1.000 50.73328  ? 114 GLY   A O   1 
ATOM   773  N N   . THR   A 1 108 ? 14.07258  38.81535 30.74256 1.000 49.22026  ? 115 THR   A N   1 
ATOM   774  C CA  . THR   A 1 108 ? 14.68025  37.73131 31.50770 1.000 46.64829  ? 115 THR   A CA  1 
ATOM   775  C C   . THR   A 1 108 ? 15.90274  38.21738 32.27618 1.000 44.16631  ? 115 THR   A C   1 
ATOM   776  O O   . THR   A 1 108 ? 16.07263  37.89483 33.45789 1.000 47.05702  ? 115 THR   A O   1 
ATOM   777  C CB  . THR   A 1 108 ? 15.05884  36.57809 30.57756 1.000 46.57348  ? 115 THR   A CB  1 
ATOM   778  O OG1 . THR   A 1 108 ? 13.90674  36.15584 29.83980 1.000 57.18462  ? 115 THR   A OG1 1 
ATOM   779  C CG2 . THR   A 1 108 ? 15.58368  35.41720 31.38002 1.000 46.34560  ? 115 THR   A CG2 1 
ATOM   780  N N   . LYS   A 1 109 ? 16.77303  38.98595 31.61453 1.000 50.76974  ? 116 LYS   A N   1 
ATOM   781  C CA  . LYS   A 1 109 ? 17.91877  39.57538 32.30011 1.000 49.38859  ? 116 LYS   A CA  1 
ATOM   782  C C   . LYS   A 1 109 ? 17.47151  40.43478 33.47513 1.000 49.07499  ? 116 LYS   A C   1 
ATOM   783  O O   . LYS   A 1 109 ? 17.99418  40.30648 34.58824 1.000 58.72679  ? 116 LYS   A O   1 
ATOM   784  C CB  . LYS   A 1 109 ? 18.74808  40.40967 31.32448 1.000 55.59821  ? 116 LYS   A CB  1 
ATOM   785  C CG  . LYS   A 1 109 ? 19.46923  39.63091 30.24411 1.000 55.02870  ? 116 LYS   A CG  1 
ATOM   786  C CD  . LYS   A 1 109 ? 20.93734  40.05571 30.19695 1.000 71.35916  ? 116 LYS   A CD  1 
ATOM   787  C CE  . LYS   A 1 109 ? 21.75029  39.20543 29.23047 1.000 80.04480  ? 116 LYS   A CE  1 
ATOM   788  N NZ  . LYS   A 1 109 ? 22.81439  38.41446 29.91604 1.000 68.40365  ? 116 LYS   A NZ  1 
ATOM   789  N N   . ALA   A 1 110 ? 16.50231  41.32400 33.24268 1.000 53.95792  ? 117 ALA   A N   1 
ATOM   790  C CA  . ALA   A 1 110 ? 16.05066  42.21621 34.30506 1.000 55.17448  ? 117 ALA   A CA  1 
ATOM   791  C C   . ALA   A 1 110 ? 15.34558  41.44426 35.41197 1.000 52.62823  ? 117 ALA   A C   1 
ATOM   792  O O   . ALA   A 1 110 ? 15.52443  41.74866 36.59713 1.000 52.34817  ? 117 ALA   A O   1 
ATOM   793  C CB  . ALA   A 1 110 ? 15.13327  43.29581 33.73352 1.000 47.56454  ? 117 ALA   A CB  1 
ATOM   794  N N   . PHE   A 1 111 ? 14.54245  40.44019 35.04867 1.000 45.72756  ? 118 PHE   A N   1 
ATOM   795  C CA  . PHE   A 1 111 ? 13.87142  39.63868 36.06688 1.000 43.39683  ? 118 PHE   A CA  1 
ATOM   796  C C   . PHE   A 1 111 ? 14.87257  38.93466 36.96812 1.000 46.67073  ? 118 PHE   A C   1 
ATOM   797  O O   . PHE   A 1 111 ? 14.61824  38.75969 38.16472 1.000 56.24875  ? 118 PHE   A O   1 
ATOM   798  C CB  . PHE   A 1 111 ? 12.94473  38.61422 35.41824 1.000 39.41454  ? 118 PHE   A CB  1 
ATOM   799  C CG  . PHE   A 1 111 ? 12.19709  37.77004 36.40882 1.000 44.52529  ? 118 PHE   A CG  1 
ATOM   800  C CD1 . PHE   A 1 111 ? 11.54506  38.35480 37.48149 1.000 41.81216  ? 118 PHE   A CD1 1 
ATOM   801  C CD2 . PHE   A 1 111 ? 12.15688  36.39183 36.27586 1.000 45.03061  ? 118 PHE   A CD2 1 
ATOM   802  C CE1 . PHE   A 1 111 ? 10.85971  37.58286 38.39800 1.000 45.58114  ? 118 PHE   A CE1 1 
ATOM   803  C CE2 . PHE   A 1 111 ? 11.47287  35.61293 37.18879 1.000 45.91109  ? 118 PHE   A CE2 1 
ATOM   804  C CZ  . PHE   A 1 111 ? 10.82343  36.20767 38.25020 1.000 53.03407  ? 118 PHE   A CZ  1 
ATOM   805  N N   . MET   A 1 112 ? 16.01740  38.53714 36.41999 1.000 51.24593  ? 119 MET   A N   1 
ATOM   806  C CA  . MET   A 1 112 ? 17.03363  37.88701 37.23418 1.000 64.17519  ? 119 MET   A CA  1 
ATOM   807  C C   . MET   A 1 112 ? 17.84202  38.87589 38.05907 1.000 56.94568  ? 119 MET   A C   1 
ATOM   808  O O   . MET   A 1 112 ? 18.33365  38.51625 39.13510 1.000 76.08672  ? 119 MET   A O   1 
ATOM   809  C CB  . MET   A 1 112 ? 17.94568  37.05390 36.34731 1.000 55.82455  ? 119 MET   A CB  1 
ATOM   810  C CG  . MET   A 1 112 ? 17.36086  35.70018 36.07881 1.000 62.68255  ? 119 MET   A CG  1 
ATOM   811  S SD  . MET   A 1 112 ? 17.98190  34.93587 34.59020 1.000 69.16543  ? 119 MET   A SD  1 
ATOM   812  C CE  . MET   A 1 112 ? 18.10896  33.27941 35.22783 1.000 59.56702  ? 119 MET   A CE  1 
ATOM   813  N N   . GLU   A 1 113 ? 17.99861  40.11071 37.57972 1.000 67.60726  ? 120 GLU   A N   1 
ATOM   814  C CA  . GLU   A 1 113 ? 18.53332  41.15849 38.44167 1.000 72.40314  ? 120 GLU   A CA  1 
ATOM   815  C C   . GLU   A 1 113 ? 17.58071  41.44173 39.59547 1.000 68.32459  ? 120 GLU   A C   1 
ATOM   816  O O   . GLU   A 1 113 ? 18.01100  41.59647 40.74431 1.000 86.66663  ? 120 GLU   A O   1 
ATOM   817  C CB  . GLU   A 1 113 ? 18.78270  42.43102 37.63343 1.000 79.49306  ? 120 GLU   A CB  1 
ATOM   818  C CG  . GLU   A 1 113 ? 19.83759  42.29828 36.55031 1.000 78.49892  ? 120 GLU   A CG  1 
ATOM   819  C CD  . GLU   A 1 113 ? 19.83471  43.47810 35.59478 1.000 97.01013  ? 120 GLU   A CD  1 
ATOM   820  O OE1 . GLU   A 1 113 ? 19.08889  44.44937 35.84896 1.000 99.59279  ? 120 GLU   A OE1 1 
ATOM   821  O OE2 . GLU   A 1 113 ? 20.57377  43.43235 34.58804 1.000 90.51495  ? 120 GLU   A OE2 1 
ATOM   822  N N   . ALA   A 1 114 ? 16.27857  41.50480 39.30474 1.000 68.59684  ? 121 ALA   A N   1 
ATOM   823  C CA  . ALA   A 1 114 ? 15.29090  41.76926 40.34393 1.000 75.77942  ? 121 ALA   A CA  1 
ATOM   824  C C   . ALA   A 1 114 ? 15.23927  40.64813 41.37088 1.000 78.86580  ? 121 ALA   A C   1 
ATOM   825  O O   . ALA   A 1 114 ? 15.00746  40.90797 42.55742 1.000 84.33041  ? 121 ALA   A O   1 
ATOM   826  C CB  . ALA   A 1 114 ? 13.91248  41.97482 39.71660 1.000 67.66558  ? 121 ALA   A CB  1 
ATOM   827  N N   . LEU   A 1 115 ? 15.45537  39.40268 40.93968 1.000 77.36593  ? 122 LEU   A N   1 
ATOM   828  C CA  . LEU   A 1 115 ? 15.44145  38.27086 41.85716 1.000 72.16804  ? 122 LEU   A CA  1 
ATOM   829  C C   . LEU   A 1 115 ? 16.56039  38.33949 42.88443 1.000 80.45209  ? 122 LEU   A C   1 
ATOM   830  O O   . LEU   A 1 115 ? 16.55480  37.55095 43.83522 1.000 78.63254  ? 122 LEU   A O   1 
ATOM   831  C CB  . LEU   A 1 115 ? 15.52922  36.95852 41.07805 1.000 61.30086  ? 122 LEU   A CB  1 
ATOM   832  C CG  . LEU   A 1 115 ? 14.20718  36.49619 40.46378 1.000 59.71621  ? 122 LEU   A CG  1 
ATOM   833  C CD1 . LEU   A 1 115 ? 14.37483  35.18338 39.71306 1.000 59.37954  ? 122 LEU   A CD1 1 
ATOM   834  C CD2 . LEU   A 1 115 ? 13.12965  36.37887 41.53028 1.000 62.22962  ? 122 LEU   A CD2 1 
ATOM   835  N N   . GLN   A 1 116 ? 17.51438  39.25160 42.71791 1.000 86.63100  ? 123 GLN   A N   1 
ATOM   836  C CA  . GLN   A 1 116 ? 18.51744  39.51707 43.73535 1.000 94.67047  ? 123 GLN   A CA  1 
ATOM   837  C C   . GLN   A 1 116 ? 18.37183  40.90007 44.35405 1.000 86.98909  ? 123 GLN   A C   1 
ATOM   838  O O   . GLN   A 1 116 ? 19.14128  41.24265 45.25720 1.000 100.45763 ? 123 GLN   A O   1 
ATOM   839  C CB  . GLN   A 1 116 ? 19.92154  39.34922 43.14838 1.000 101.62337 ? 123 GLN   A CB  1 
ATOM   840  C CG  . GLN   A 1 116 ? 20.19095  37.95708 42.60184 1.000 99.09893  ? 123 GLN   A CG  1 
ATOM   841  C CD  . GLN   A 1 116 ? 21.52789  37.85996 41.89954 1.000 116.14684 ? 123 GLN   A CD  1 
ATOM   842  O OE1 . GLN   A 1 116 ? 22.23224  38.85721 41.73938 1.000 124.69607 ? 123 GLN   A OE1 1 
ATOM   843  N NE2 . GLN   A 1 116 ? 21.88997  36.65271 41.48236 1.000 111.05327 ? 123 GLN   A NE2 1 
ATOM   844  N N   . ALA   A 1 117 ? 17.40586  41.69916 43.89574 1.000 101.23981 ? 124 ALA   A N   1 
ATOM   845  C CA  . ALA   A 1 117 ? 17.12720  43.01684 44.45017 1.000 100.65725 ? 124 ALA   A CA  1 
ATOM   846  C C   . ALA   A 1 117 ? 15.92275  43.01028 45.38533 1.000 111.25296 ? 124 ALA   A C   1 
ATOM   847  O O   . ALA   A 1 117 ? 15.38747  44.07745 45.70720 1.000 111.04990 ? 124 ALA   A O   1 
ATOM   848  C CB  . ALA   A 1 117 ? 16.91450  44.02821 43.32301 1.000 100.68707 ? 124 ALA   A CB  1 
ATOM   849  N N   . GLY   A 1 118 ? 15.48421  41.83062 45.81969 1.000 112.05420 ? 125 GLY   A N   1 
ATOM   850  C CA  . GLY   A 1 118 ? 14.33617  41.71719 46.69718 1.000 110.99785 ? 125 GLY   A CA  1 
ATOM   851  C C   . GLY   A 1 118 ? 13.19133  40.92171 46.10151 1.000 98.49841  ? 125 GLY   A C   1 
ATOM   852  O O   . GLY   A 1 118 ? 12.55636  40.12434 46.79844 1.000 91.48629  ? 125 GLY   A O   1 
ATOM   853  N N   . ALA   A 1 119 ? 12.93254  41.12187 44.80961 1.000 91.21499  ? 126 ALA   A N   1 
ATOM   854  C CA  . ALA   A 1 119 ? 11.75145  40.55763 44.16851 1.000 91.42450  ? 126 ALA   A CA  1 
ATOM   855  C C   . ALA   A 1 119 ? 11.76708  39.03386 44.21277 1.000 83.49101  ? 126 ALA   A C   1 
ATOM   856  O O   . ALA   A 1 119 ? 12.82254  38.39979 44.29409 1.000 86.20954  ? 126 ALA   A O   1 
ATOM   857  C CB  . ALA   A 1 119 ? 11.65952  41.03238 42.71744 1.000 76.97490  ? 126 ALA   A CB  1 
ATOM   858  N N   . ASP   A 1 120 ? 10.57398  38.44874 44.15673 1.000 75.84987  ? 127 ASP   A N   1 
ATOM   859  C CA  . ASP   A 1 120 ? 10.38934  37.00654 44.12450 1.000 75.43449  ? 127 ASP   A CA  1 
ATOM   860  C C   . ASP   A 1 120 ? 9.79422   36.59129 42.78243 1.000 63.26503  ? 127 ASP   A C   1 
ATOM   861  O O   . ASP   A 1 120 ? 9.56028   37.41393 41.89211 1.000 65.49715  ? 127 ASP   A O   1 
ATOM   862  C CB  . ASP   A 1 120 ? 9.50162   36.54244 45.28078 1.000 76.54811  ? 127 ASP   A CB  1 
ATOM   863  C CG  . ASP   A 1 120 ? 8.14231   37.20657 45.27250 1.000 76.54897  ? 127 ASP   A CG  1 
ATOM   864  O OD1 . ASP   A 1 120 ? 8.03592   38.33999 44.75828 1.000 85.27226  ? 127 ASP   A OD1 1 
ATOM   865  O OD2 . ASP   A 1 120 ? 7.17730   36.58872 45.76900 1.000 79.34928  ? 127 ASP   A OD2 1 
ATOM   866  N N   . ILE   A 1 121 ? 9.53310   35.28831 42.65758 1.000 67.52368  ? 128 ILE   A N   1 
ATOM   867  C CA  . ILE   A 1 121 ? 9.13021   34.71050 41.37901 1.000 55.91104  ? 128 ILE   A CA  1 
ATOM   868  C C   . ILE   A 1 121 ? 7.76810   35.23422 40.93763 1.000 54.61355  ? 128 ILE   A C   1 
ATOM   869  O O   . ILE   A 1 121 ? 7.51833   35.39411 39.73657 1.000 52.96513  ? 128 ILE   A O   1 
ATOM   870  C CB  . ILE   A 1 121 ? 9.15914   33.17201 41.48470 1.000 57.38086  ? 128 ILE   A CB  1 
ATOM   871  C CG1 . ILE   A 1 121 ? 10.60336  32.66657 41.41828 1.000 62.60148  ? 128 ILE   A CG1 1 
ATOM   872  C CG2 . ILE   A 1 121 ? 8.32086   32.52104 40.39898 1.000 49.90817  ? 128 ILE   A CG2 1 
ATOM   873  C CD1 . ILE   A 1 121 ? 10.75176  31.19103 41.71299 1.000 66.32106  ? 128 ILE   A CD1 1 
ATOM   874  N N   . SER   A 1 122 ? 6.88162   35.54592 41.88673 1.000 56.12068  ? 129 SER   A N   1 
ATOM   875  C CA  . SER   A 1 122 ? 5.52963   35.98199 41.55161 1.000 49.47882  ? 129 SER   A CA  1 
ATOM   876  C C   . SER   A 1 122 ? 5.49345   37.27600 40.74877 1.000 55.39902  ? 129 SER   A C   1 
ATOM   877  O O   . SER   A 1 122 ? 4.42969   37.63220 40.23053 1.000 51.11091  ? 129 SER   A O   1 
ATOM   878  C CB  . SER   A 1 122 ? 4.70849   36.16208 42.82552 1.000 54.58308  ? 129 SER   A CB  1 
ATOM   879  O OG  . SER   A 1 122 ? 5.10624   37.33472 43.50690 1.000 60.13761  ? 129 SER   A OG  1 
ATOM   880  N N   . MET   A 1 123 ? 6.60697   37.99058 40.63848 1.000 56.75368  ? 130 MET   A N   1 
ATOM   881  C CA  . MET   A 1 123 ? 6.64775   39.22831 39.87690 1.000 56.06899  ? 130 MET   A CA  1 
ATOM   882  C C   . MET   A 1 123 ? 7.05031   39.00179 38.42793 1.000 49.25183  ? 130 MET   A C   1 
ATOM   883  O O   . MET   A 1 123 ? 7.34860   39.96741 37.71626 1.000 50.24238  ? 130 MET   A O   1 
ATOM   884  C CB  . MET   A 1 123 ? 7.60479   40.21174 40.54229 1.000 52.03862  ? 130 MET   A CB  1 
ATOM   885  C CG  . MET   A 1 123 ? 6.92992   41.06872 41.58963 1.000 62.60418  ? 130 MET   A CG  1 
ATOM   886  S SD  . MET   A 1 123 ? 8.13626   41.81922 42.68038 1.000 81.31041  ? 130 MET   A SD  1 
ATOM   887  C CE  . MET   A 1 123 ? 8.77279   43.08914 41.59837 1.000 80.59799  ? 130 MET   A CE  1 
ATOM   888  N N   . ILE   A 1 124 ? 7.05557   37.74486 37.98293 1.000 47.83867  ? 131 ILE   A N   1 
ATOM   889  C CA  . ILE   A 1 124 ? 7.53441   37.40152 36.64942 1.000 44.96167  ? 131 ILE   A CA  1 
ATOM   890  C C   . ILE   A 1 124 ? 6.71633   38.10055 35.56987 1.000 48.03363  ? 131 ILE   A C   1 
ATOM   891  O O   . ILE   A 1 124 ? 7.25023   38.46248 34.51320 1.000 41.64958  ? 131 ILE   A O   1 
ATOM   892  C CB  . ILE   A 1 124 ? 7.52876   35.86540 36.49002 1.000 43.83522  ? 131 ILE   A CB  1 
ATOM   893  C CG1 . ILE   A 1 124 ? 8.32429   35.43458 35.25906 1.000 43.51666  ? 131 ILE   A CG1 1 
ATOM   894  C CG2 . ILE   A 1 124 ? 6.10352   35.31877 36.46613 1.000 41.53899  ? 131 ILE   A CG2 1 
ATOM   895  C CD1 . ILE   A 1 124 ? 8.58585   33.94693 35.20723 1.000 36.74648  ? 131 ILE   A CD1 1 
ATOM   896  N N   . GLY   A 1 125 ? 5.42601   38.33537 35.82273 1.000 45.88463  ? 132 GLY   A N   1 
ATOM   897  C CA  . GLY   A 1 125 ? 4.58634   38.96389 34.81835 1.000 50.89387  ? 132 GLY   A CA  1 
ATOM   898  C C   . GLY   A 1 125 ? 4.97753   40.39403 34.50965 1.000 49.32280  ? 132 GLY   A C   1 
ATOM   899  O O   . GLY   A 1 125 ? 4.77551   40.86577 33.38714 1.000 50.10763  ? 132 GLY   A O   1 
ATOM   900  N N   . GLN   A 1 126 ? 5.54455   41.10188 35.48808 1.000 47.92311  ? 133 GLN   A N   1 
ATOM   901  C CA  . GLN   A 1 126 ? 5.95289   42.48349 35.27069 1.000 55.61461  ? 133 GLN   A CA  1 
ATOM   902  C C   . GLN   A 1 126 ? 7.15977   42.61091 34.35472 1.000 46.58572  ? 133 GLN   A C   1 
ATOM   903  O O   . GLN   A 1 126 ? 7.52656   43.73640 34.00228 1.000 49.91685  ? 133 GLN   A O   1 
ATOM   904  C CB  . GLN   A 1 126 ? 6.26070   43.15681 36.60282 1.000 52.06491  ? 133 GLN   A CB  1 
ATOM   905  C CG  . GLN   A 1 126 ? 5.07944   43.26263 37.52987 1.000 55.56572  ? 133 GLN   A CG  1 
ATOM   906  C CD  . GLN   A 1 126 ? 5.45220   43.92641 38.83375 1.000 83.21530  ? 133 GLN   A CD  1 
ATOM   907  O OE1 . GLN   A 1 126 ? 5.46513   43.28824 39.88685 1.000 81.58261  ? 133 GLN   A OE1 1 
ATOM   908  N NE2 . GLN   A 1 126 ? 5.77681   45.21478 38.76987 1.000 87.26817  ? 133 GLN   A NE2 1 
ATOM   909  N N   . PHE   A 1 127 ? 7.79096   41.50191 33.97688 1.000 42.96099  ? 134 PHE   A N   1 
ATOM   910  C CA  . PHE   A 1 127 ? 8.91029   41.51937 33.04502 1.000 49.30558  ? 134 PHE   A CA  1 
ATOM   911  C C   . PHE   A 1 127 ? 8.55840   40.87653 31.70990 1.000 43.02509  ? 134 PHE   A C   1 
ATOM   912  O O   . PHE   A 1 127 ? 9.44968   40.64795 30.88510 1.000 46.91748  ? 134 PHE   A O   1 
ATOM   913  C CB  . PHE   A 1 127 ? 10.13018  40.83101 33.66492 1.000 49.08452  ? 134 PHE   A CB  1 
ATOM   914  C CG  . PHE   A 1 127 ? 10.57118  41.43923 34.96882 1.000 48.36591  ? 134 PHE   A CG  1 
ATOM   915  C CD1 . PHE   A 1 127 ? 9.94624   41.09741 36.15837 1.000 43.23528  ? 134 PHE   A CD1 1 
ATOM   916  C CD2 . PHE   A 1 127 ? 11.60143  42.36518 35.00177 1.000 44.77061  ? 134 PHE   A CD2 1 
ATOM   917  C CE1 . PHE   A 1 127 ? 10.34862  41.65928 37.35596 1.000 46.63099  ? 134 PHE   A CE1 1 
ATOM   918  C CE2 . PHE   A 1 127 ? 12.00740  42.93291 36.19674 1.000 51.33998  ? 134 PHE   A CE2 1 
ATOM   919  C CZ  . PHE   A 1 127 ? 11.37929  42.57980 37.37389 1.000 51.98399  ? 134 PHE   A CZ  1 
ATOM   920  N N   . GLY   A 1 128 ? 7.28152   40.58241 31.47822 1.000 46.05688  ? 135 GLY   A N   1 
ATOM   921  C CA  . GLY   A 1 128 ? 6.85649   40.02752 30.20973 1.000 45.20274  ? 135 GLY   A CA  1 
ATOM   922  C C   . GLY   A 1 128 ? 7.32558   38.62017 29.93208 1.000 50.00319  ? 135 GLY   A C   1 
ATOM   923  O O   . GLY   A 1 128 ? 7.36243   38.21267 28.76906 1.000 41.77438  ? 135 GLY   A O   1 
ATOM   924  N N   . VAL   A 1 129 ? 7.68681   37.85850 30.96372 1.000 38.30242  ? 136 VAL   A N   1 
ATOM   925  C CA  . VAL   A 1 129 ? 8.17017   36.49843 30.76022 1.000 40.93658  ? 136 VAL   A CA  1 
ATOM   926  C C   . VAL   A 1 129 ? 7.34093   35.52639 31.58955 1.000 38.03659  ? 136 VAL   A C   1 
ATOM   927  O O   . VAL   A 1 129 ? 7.81381   34.44453 31.95473 1.000 34.19695  ? 136 VAL   A O   1 
ATOM   928  C CB  . VAL   A 1 129 ? 9.67048   36.38334 31.08793 1.000 45.81914  ? 136 VAL   A CB  1 
ATOM   929  C CG1 . VAL   A 1 129 ? 10.49269  37.06472 30.00280 1.000 44.77074  ? 136 VAL   A CG1 1 
ATOM   930  C CG2 . VAL   A 1 129 ? 9.96962   36.99271 32.44804 1.000 41.44494  ? 136 VAL   A CG2 1 
ATOM   931  N N   . GLY   A 1 130 ? 6.08772   35.89431 31.86495 1.000 32.40001  ? 137 GLY   A N   1 
ATOM   932  C CA  . GLY   A 1 130 ? 5.22215   35.07862 32.70255 1.000 37.31026  ? 137 GLY   A CA  1 
ATOM   933  C C   . GLY   A 1 130 ? 4.97289   33.67171 32.19069 1.000 38.86464  ? 137 GLY   A C   1 
ATOM   934  O O   . GLY   A 1 130 ? 4.67100   32.77996 32.99225 1.000 35.55994  ? 137 GLY   A O   1 
ATOM   935  N N   . PHE   A 1 131 ? 5.09247   33.44744 30.87695 1.000 32.55182  ? 138 PHE   A N   1 
ATOM   936  C CA  . PHE   A 1 131 ? 4.80009   32.12766 30.32007 1.000 36.80957  ? 138 PHE   A CA  1 
ATOM   937  C C   . PHE   A 1 131 ? 5.65509   31.04790 30.96518 1.000 30.77973  ? 138 PHE   A C   1 
ATOM   938  O O   . PHE   A 1 131 ? 5.18258   29.93039 31.20314 1.000 31.10146  ? 138 PHE   A O   1 
ATOM   939  C CB  . PHE   A 1 131 ? 5.02201   32.11334 28.80558 1.000 29.22092  ? 138 PHE   A CB  1 
ATOM   940  C CG  . PHE   A 1 131 ? 5.09783   30.72139 28.22131 1.000 32.69201  ? 138 PHE   A CG  1 
ATOM   941  C CD1 . PHE   A 1 131 ? 3.94166   29.98823 27.99363 1.000 29.92825  ? 138 PHE   A CD1 1 
ATOM   942  C CD2 . PHE   A 1 131 ? 6.32489   30.13562 27.93059 1.000 32.55622  ? 138 PHE   A CD2 1 
ATOM   943  C CE1 . PHE   A 1 131 ? 4.00354   28.70662 27.46825 1.000 32.83035  ? 138 PHE   A CE1 1 
ATOM   944  C CE2 . PHE   A 1 131 ? 6.39587   28.85415 27.40935 1.000 31.62375  ? 138 PHE   A CE2 1 
ATOM   945  C CZ  . PHE   A 1 131 ? 5.23466   28.13915 27.17583 1.000 36.01501  ? 138 PHE   A CZ  1 
ATOM   946  N N   . TYR   A 1 132 ? 6.92297   31.35338 31.23610 1.000 31.56409  ? 139 TYR   A N   1 
ATOM   947  C CA  . TYR   A 1 132 ? 7.83356   30.33639 31.74174 1.000 31.41208  ? 139 TYR   A CA  1 
ATOM   948  C C   . TYR   A 1 132 ? 7.52540   29.92940 33.17433 1.000 33.26806  ? 139 TYR   A C   1 
ATOM   949  O O   . TYR   A 1 132 ? 8.12319   28.96619 33.66468 1.000 36.55240  ? 139 TYR   A O   1 
ATOM   950  C CB  . TYR   A 1 132 ? 9.27361   30.82919 31.60689 1.000 32.00845  ? 139 TYR   A CB  1 
ATOM   951  C CG  . TYR   A 1 132 ? 9.62467   31.14396 30.17147 1.000 40.18391  ? 139 TYR   A CG  1 
ATOM   952  C CD1 . TYR   A 1 132 ? 9.96436   30.13013 29.28100 1.000 38.69101  ? 139 TYR   A CD1 1 
ATOM   953  C CD2 . TYR   A 1 132 ? 9.57896   32.44765 29.69462 1.000 39.90100  ? 139 TYR   A CD2 1 
ATOM   954  C CE1 . TYR   A 1 132 ? 10.27114  30.40968 27.95850 1.000 31.51953  ? 139 TYR   A CE1 1 
ATOM   955  C CE2 . TYR   A 1 132 ? 9.87840   32.73712 28.37592 1.000 36.91384  ? 139 TYR   A CE2 1 
ATOM   956  C CZ  . TYR   A 1 132 ? 10.22434  31.71539 27.51258 1.000 46.48282  ? 139 TYR   A CZ  1 
ATOM   957  O OH  . TYR   A 1 132 ? 10.52735  32.00516 26.20032 1.000 58.85549  ? 139 TYR   A OH  1 
ATOM   958  N N   . SER   A 1 133 ? 6.59806   30.61683 33.84633 1.000 32.87680  ? 140 SER   A N   1 
ATOM   959  C CA  . SER   A 1 133 ? 6.13216   30.16278 35.14999 1.000 28.94491  ? 140 SER   A CA  1 
ATOM   960  C C   . SER   A 1 133 ? 5.32831   28.87601 35.05150 1.000 31.31616  ? 140 SER   A C   1 
ATOM   961  O O   . SER   A 1 133 ? 5.02100   28.27346 36.08668 1.000 36.21324  ? 140 SER   A O   1 
ATOM   962  C CB  . SER   A 1 133 ? 5.29361   31.25171 35.82489 1.000 33.01064  ? 140 SER   A CB  1 
ATOM   963  O OG  . SER   A 1 133 ? 4.07307   31.45508 35.13601 1.000 32.06972  ? 140 SER   A OG  1 
ATOM   964  N N   . ALA   A 1 134 ? 4.98458   28.45090 33.83303 1.000 32.60018  ? 141 ALA   A N   1 
ATOM   965  C CA  . ALA   A 1 134 ? 4.35102   27.15413 33.63354 1.000 33.71535  ? 141 ALA   A CA  1 
ATOM   966  C C   . ALA   A 1 134 ? 5.22020   26.02217 34.15679 1.000 37.09456  ? 141 ALA   A C   1 
ATOM   967  O O   . ALA   A 1 134 ? 4.69717   24.99328 34.59657 1.000 36.19101  ? 141 ALA   A O   1 
ATOM   968  C CB  . ALA   A 1 134 ? 4.05216   26.94419 32.14857 1.000 32.63340  ? 141 ALA   A CB  1 
ATOM   969  N N   . TYR   A 1 135 ? 6.54261   26.19147 34.12343 1.000 32.41654  ? 142 TYR   A N   1 
ATOM   970  C CA  . TYR   A 1 135 ? 7.45757   25.16036 34.59375 1.000 38.04917  ? 142 TYR   A CA  1 
ATOM   971  C C   . TYR   A 1 135 ? 7.55098   25.10166 36.11144 1.000 37.76334  ? 142 TYR   A C   1 
ATOM   972  O O   . TYR   A 1 135 ? 8.31702   24.28781 36.63901 1.000 43.36222  ? 142 TYR   A O   1 
ATOM   973  C CB  . TYR   A 1 135 ? 8.83994   25.36952 33.96652 1.000 31.87289  ? 142 TYR   A CB  1 
ATOM   974  C CG  . TYR   A 1 135 ? 8.81450   25.03586 32.49710 1.000 38.68946  ? 142 TYR   A CG  1 
ATOM   975  C CD1 . TYR   A 1 135 ? 8.45708   25.99318 31.55694 1.000 33.35318  ? 142 TYR   A CD1 1 
ATOM   976  C CD2 . TYR   A 1 135 ? 9.08912   23.74735 32.05270 1.000 32.47882  ? 142 TYR   A CD2 1 
ATOM   977  C CE1 . TYR   A 1 135 ? 8.39909   25.68741 30.21180 1.000 38.23651  ? 142 TYR   A CE1 1 
ATOM   978  C CE2 . TYR   A 1 135 ? 9.03552   23.43196 30.70770 1.000 33.90681  ? 142 TYR   A CE2 1 
ATOM   979  C CZ  . TYR   A 1 135 ? 8.68744   24.40738 29.79298 1.000 32.37540  ? 142 TYR   A CZ  1 
ATOM   980  O OH  . TYR   A 1 135 ? 8.63167   24.10369 28.45396 1.000 38.87831  ? 142 TYR   A OH  1 
ATOM   981  N N   . LEU   A 1 136 ? 6.79178   25.93727 36.82359 1.000 35.58960  ? 143 LEU   A N   1 
ATOM   982  C CA  . LEU   A 1 136 ? 6.62690   25.73003 38.25676 1.000 40.56540  ? 143 LEU   A CA  1 
ATOM   983  C C   . LEU   A 1 136 ? 5.83083   24.46378 38.53452 1.000 35.00803  ? 143 LEU   A C   1 
ATOM   984  O O   . LEU   A 1 136 ? 6.07256   23.78337 39.53719 1.000 37.06966  ? 143 LEU   A O   1 
ATOM   985  C CB  . LEU   A 1 136 ? 5.92728   26.93371 38.89365 1.000 43.42448  ? 143 LEU   A CB  1 
ATOM   986  C CG  . LEU   A 1 136 ? 6.66590   28.26812 39.02263 1.000 40.22439  ? 143 LEU   A CG  1 
ATOM   987  C CD1 . LEU   A 1 136 ? 5.69600   29.34686 39.47666 1.000 40.44005  ? 143 LEU   A CD1 1 
ATOM   988  C CD2 . LEU   A 1 136 ? 7.83158   28.16416 39.99024 1.000 35.22696  ? 143 LEU   A CD2 1 
ATOM   989  N N   . VAL   A 1 137 ? 4.88583   24.12892 37.65781 1.000 32.56798  ? 144 VAL   A N   1 
ATOM   990  C CA  . VAL   A 1 137 ? 4.00824   22.98455 37.86111 1.000 38.67753  ? 144 VAL   A CA  1 
ATOM   991  C C   . VAL   A 1 137 ? 4.10501   21.95287 36.74823 1.000 42.57467  ? 144 VAL   A C   1 
ATOM   992  O O   . VAL   A 1 137 ? 3.58517   20.83987 36.91403 1.000 44.72302  ? 144 VAL   A O   1 
ATOM   993  C CB  . VAL   A 1 137 ? 2.53794   23.42829 38.03238 1.000 36.29568  ? 144 VAL   A CB  1 
ATOM   994  C CG1 . VAL   A 1 137 ? 2.39638   24.36626 39.22201 1.000 37.25149  ? 144 VAL   A CG1 1 
ATOM   995  C CG2 . VAL   A 1 137 ? 2.03262   24.08904 36.75715 1.000 36.88654  ? 144 VAL   A CG2 1 
ATOM   996  N N   . ALA   A 1 138 ? 4.74367   22.27041 35.62627 1.000 36.15499  ? 145 ALA   A N   1 
ATOM   997  C CA  . ALA   A 1 138 ? 4.77490   21.39375 34.46374 1.000 36.16430  ? 145 ALA   A CA  1 
ATOM   998  C C   . ALA   A 1 138 ? 6.18380   20.86570 34.24194 1.000 44.17639  ? 145 ALA   A C   1 
ATOM   999  O O   . ALA   A 1 138 ? 7.15064   21.63535 34.25910 1.000 49.44364  ? 145 ALA   A O   1 
ATOM   1000 C CB  . ALA   A 1 138 ? 4.29353   22.12837 33.21043 1.000 33.79636  ? 145 ALA   A CB  1 
ATOM   1001 N N   . GLU   A 1 139 ? 6.29569   19.55252 34.03364 1.000 47.06925  ? 146 GLU   A N   1 
ATOM   1002 C CA  . GLU   A 1 139 ? 7.55321   18.97661 33.57860 1.000 40.82825  ? 146 GLU   A CA  1 
ATOM   1003 C C   . GLU   A 1 139 ? 7.72418   19.09786 32.07181 1.000 42.73715  ? 146 GLU   A C   1 
ATOM   1004 O O   . GLU   A 1 139 ? 8.85801   19.05975 31.58299 1.000 42.22256  ? 146 GLU   A O   1 
ATOM   1005 C CB  . GLU   A 1 139 ? 7.64664   17.50732 33.99515 1.000 46.04092  ? 146 GLU   A CB  1 
ATOM   1006 C CG  . GLU   A 1 139 ? 6.52997   16.63690 33.44772 1.000 48.02406  ? 146 GLU   A CG  1 
ATOM   1007 C CD  . GLU   A 1 139 ? 6.52547   15.24661 34.05153 1.000 79.07914  ? 146 GLU   A CD  1 
ATOM   1008 O OE1 . GLU   A 1 139 ? 6.52814   15.14023 35.29747 1.000 84.25596  ? 146 GLU   A OE1 1 
ATOM   1009 O OE2 . GLU   A 1 139 ? 6.50943   14.26146 33.28260 1.000 79.20491  ? 146 GLU   A OE2 1 
ATOM   1010 N N   . LYS   A 1 140 ? 6.62679   19.25133 31.33370 1.000 40.10594  ? 147 LYS   A N   1 
ATOM   1011 C CA  . LYS   A 1 140 ? 6.66424   19.40721 29.88785 1.000 39.07790  ? 147 LYS   A CA  1 
ATOM   1012 C C   . LYS   A 1 140 ? 5.50155   20.29636 29.47513 1.000 36.97316  ? 147 LYS   A C   1 
ATOM   1013 O O   . LYS   A 1 140 ? 4.39141   20.15883 29.99700 1.000 38.27401  ? 147 LYS   A O   1 
ATOM   1014 C CB  . LYS   A 1 140 ? 6.58932   18.04768 29.17525 1.000 41.80447  ? 147 LYS   A CB  1 
ATOM   1015 C CG  . LYS   A 1 140 ? 6.50287   18.12234 27.65131 1.000 35.21784  ? 147 LYS   A CG  1 
ATOM   1016 C CD  . LYS   A 1 140 ? 6.76296   16.76081 27.01618 1.000 37.40909  ? 147 LYS   A CD  1 
ATOM   1017 C CE  . LYS   A 1 140 ? 5.52933   16.24998 26.28314 1.000 54.23243  ? 147 LYS   A CE  1 
ATOM   1018 N NZ  . LYS   A 1 140 ? 5.53372   14.76685 26.09859 1.000 45.62020  ? 147 LYS   A NZ  1 
ATOM   1019 N N   . VAL   A 1 141 ? 5.76644   21.21548 28.55130 1.000 30.77542  ? 148 VAL   A N   1 
ATOM   1020 C CA  . VAL   A 1 141 ? 4.76281   22.13983 28.04119 1.000 28.88739  ? 148 VAL   A CA  1 
ATOM   1021 C C   . VAL   A 1 141 ? 4.69133   21.97868 26.53064 1.000 31.69678  ? 148 VAL   A C   1 
ATOM   1022 O O   . VAL   A 1 141 ? 5.72272   22.01335 25.84997 1.000 40.08370  ? 148 VAL   A O   1 
ATOM   1023 C CB  . VAL   A 1 141 ? 5.08513   23.59755 28.42042 1.000 33.24835  ? 148 VAL   A CB  1 
ATOM   1024 C CG1 . VAL   A 1 141 ? 4.02060   24.53097 27.87763 1.000 27.32079  ? 148 VAL   A CG1 1 
ATOM   1025 C CG2 . VAL   A 1 141 ? 5.20187   23.74323 29.93177 1.000 28.91362  ? 148 VAL   A CG2 1 
ATOM   1026 N N   . THR   A 1 142 ? 3.47853   21.78931 26.01397 1.000 28.04861  ? 149 THR   A N   1 
ATOM   1027 C CA  . THR   A 1 142 ? 3.21553   21.71723 24.58340 1.000 29.20644  ? 149 THR   A CA  1 
ATOM   1028 C C   . THR   A 1 142 ? 2.34768   22.90388 24.19327 1.000 34.22417  ? 149 THR   A C   1 
ATOM   1029 O O   . THR   A 1 142 ? 1.35637   23.20033 24.86888 1.000 34.61488  ? 149 THR   A O   1 
ATOM   1030 C CB  . THR   A 1 142 ? 2.51556   20.40625 24.21073 1.000 30.44170  ? 149 THR   A CB  1 
ATOM   1031 O OG1 . THR   A 1 142 ? 3.25941   19.30262 24.73422 1.000 39.93511  ? 149 THR   A OG1 1 
ATOM   1032 C CG2 . THR   A 1 142 ? 2.40462   20.26281 22.70233 1.000 36.73173  ? 149 THR   A CG2 1 
ATOM   1033 N N   . VAL   A 1 143 ? 2.72142   23.58925 23.11863 1.000 32.88126  ? 150 VAL   A N   1 
ATOM   1034 C CA  . VAL   A 1 143 ? 1.98327   24.75352 22.64693 1.000 30.57245  ? 150 VAL   A CA  1 
ATOM   1035 C C   . VAL   A 1 143 ? 1.55740   24.48281 21.21016 1.000 36.71689  ? 150 VAL   A C   1 
ATOM   1036 O O   . VAL   A 1 143 ? 2.40423   24.31295 20.32261 1.000 35.59389  ? 150 VAL   A O   1 
ATOM   1037 C CB  . VAL   A 1 143 ? 2.80600   26.04435 22.74837 1.000 30.94238  ? 150 VAL   A CB  1 
ATOM   1038 C CG1 . VAL   A 1 143 ? 1.99550   27.21980 22.22101 1.000 25.28366  ? 150 VAL   A CG1 1 
ATOM   1039 C CG2 . VAL   A 1 143 ? 3.22878   26.29001 24.18883 1.000 27.28445  ? 150 VAL   A CG2 1 
ATOM   1040 N N   . ILE   A 1 144 ? 0.24792   24.41614 20.98698 1.000 33.20815  ? 151 ILE   A N   1 
ATOM   1041 C CA  . ILE   A 1 144 ? -0.33306  24.32744 19.65346 1.000 36.62478  ? 151 ILE   A CA  1 
ATOM   1042 C C   . ILE   A 1 144 ? -0.87545  25.70208 19.30567 1.000 36.92370  ? 151 ILE   A C   1 
ATOM   1043 O O   . ILE   A 1 144 ? -1.64029  26.28897 20.08182 1.000 38.87722  ? 151 ILE   A O   1 
ATOM   1044 C CB  . ILE   A 1 144 ? -1.44616  23.26704 19.58938 1.000 34.78847  ? 151 ILE   A CB  1 
ATOM   1045 C CG1 . ILE   A 1 144 ? -1.06627  22.02261 20.39361 1.000 39.48208  ? 151 ILE   A CG1 1 
ATOM   1046 C CG2 . ILE   A 1 144 ? -1.72662  22.87989 18.14721 1.000 41.37351  ? 151 ILE   A CG2 1 
ATOM   1047 C CD1 . ILE   A 1 144 ? 0.02220   21.19968 19.76018 1.000 41.03734  ? 151 ILE   A CD1 1 
ATOM   1048 N N   . THR   A 1 145 ? -0.48299  26.22837 18.15222 1.000 28.36172  ? 152 THR   A N   1 
ATOM   1049 C CA  . THR   A 1 145 ? -0.84088  27.59921 17.83609 1.000 36.17297  ? 152 THR   A CA  1 
ATOM   1050 C C   . THR   A 1 145 ? -1.10121  27.74335 16.34614 1.000 37.13810  ? 152 THR   A C   1 
ATOM   1051 O O   . THR   A 1 145 ? -0.47299  27.08122 15.51441 1.000 31.48094  ? 152 THR   A O   1 
ATOM   1052 C CB  . THR   A 1 145 ? 0.24704   28.58003 18.29892 1.000 30.77341  ? 152 THR   A CB  1 
ATOM   1053 O OG1 . THR   A 1 145 ? -0.26252  29.91640 18.24999 1.000 32.57921  ? 152 THR   A OG1 1 
ATOM   1054 C CG2 . THR   A 1 145 ? 1.49252   28.47576 17.43015 1.000 32.25303  ? 152 THR   A CG2 1 
ATOM   1055 N N   . LYS   A 1 146 ? -2.05263  28.61532 16.02360 1.000 30.22951  ? 153 LYS   A N   1 
ATOM   1056 C CA  . LYS   A 1 146 ? -2.45499  28.86145 14.64497 1.000 34.18292  ? 153 LYS   A CA  1 
ATOM   1057 C C   . LYS   A 1 146 ? -2.64890  30.35780 14.46470 1.000 37.27833  ? 153 LYS   A C   1 
ATOM   1058 O O   . LYS   A 1 146 ? -3.49644  30.96144 15.12986 1.000 30.11781  ? 153 LYS   A O   1 
ATOM   1059 C CB  . LYS   A 1 146 ? -3.73781  28.09905 14.29882 1.000 32.67902  ? 153 LYS   A CB  1 
ATOM   1060 C CG  . LYS   A 1 146 ? -4.24580  28.33530 12.88552 1.000 37.12609  ? 153 LYS   A CG  1 
ATOM   1061 C CD  . LYS   A 1 146 ? -3.17525  28.03383 11.84662 1.000 37.85451  ? 153 LYS   A CD  1 
ATOM   1062 C CE  . LYS   A 1 146 ? -3.75478  28.04846 10.43818 1.000 39.25540  ? 153 LYS   A CE  1 
ATOM   1063 N NZ  . LYS   A 1 146 ? -3.92934  29.43603 9.91682  1.000 41.07597  ? 153 LYS   A NZ  1 
ATOM   1064 N N   . HIS   A 1 147 ? -1.84840  30.94992 13.58637 1.000 37.53109  ? 154 HIS   A N   1 
ATOM   1065 C CA  . HIS   A 1 147 ? -1.94939  32.35174 13.21900 1.000 33.13259  ? 154 HIS   A CA  1 
ATOM   1066 C C   . HIS   A 1 147 ? -2.53775  32.45379 11.81770 1.000 36.50362  ? 154 HIS   A C   1 
ATOM   1067 O O   . HIS   A 1 147 ? -2.35565  31.55751 10.98939 1.000 39.58960  ? 154 HIS   A O   1 
ATOM   1068 C CB  . HIS   A 1 147 ? -0.57083  33.02221 13.27552 1.000 43.33419  ? 154 HIS   A CB  1 
ATOM   1069 C CG  . HIS   A 1 147 ? -0.59985  34.50790 13.09032 1.000 35.47749  ? 154 HIS   A CG  1 
ATOM   1070 N ND1 . HIS   A 1 147 ? -0.65742  35.10326 11.84859 1.000 40.92254  ? 154 HIS   A ND1 1 
ATOM   1071 C CD2 . HIS   A 1 147 ? -0.54480  35.51906 13.98976 1.000 41.18504  ? 154 HIS   A CD2 1 
ATOM   1072 C CE1 . HIS   A 1 147 ? -0.65399  36.41686 11.99162 1.000 42.29097  ? 154 HIS   A CE1 1 
ATOM   1073 N NE2 . HIS   A 1 147 ? -0.58321  36.69510 13.28111 1.000 39.36935  ? 154 HIS   A NE2 1 
ATOM   1074 N N   . ASN   A 1 148 ? -3.25157  33.55428 11.56113 1.000 38.56379  ? 155 ASN   A N   1 
ATOM   1075 C CA  . ASN   A 1 148 ? -3.91635  33.73187 10.27204 1.000 39.32612  ? 155 ASN   A CA  1 
ATOM   1076 C C   . ASN   A 1 148 ? -2.93062  33.68136 9.10829  1.000 40.49359  ? 155 ASN   A C   1 
ATOM   1077 O O   . ASN   A 1 148 ? -3.30185  33.28357 7.99787  1.000 41.70483  ? 155 ASN   A O   1 
ATOM   1078 C CB  . ASN   A 1 148 ? -4.67083  35.06443 10.24329 1.000 41.13475  ? 155 ASN   A CB  1 
ATOM   1079 C CG  . ASN   A 1 148 ? -6.06278  34.97428 10.84928 1.000 41.34491  ? 155 ASN   A CG  1 
ATOM   1080 O OD1 . ASN   A 1 148 ? -6.67373  33.90683 10.88922 1.000 45.29397  ? 155 ASN   A OD1 1 
ATOM   1081 N ND2 . ASN   A 1 148 ? -6.58072  36.11200 11.30294 1.000 37.38985  ? 155 ASN   A ND2 1 
ATOM   1082 N N   . ASP   A 1 149 ? -1.68040  34.08174 9.33540  1.000 39.44056  ? 156 ASP   A N   1 
ATOM   1083 C CA  . ASP   A 1 149 ? -0.69119  34.20539 8.27289  1.000 48.06906  ? 156 ASP   A CA  1 
ATOM   1084 C C   . ASP   A 1 149 ? 0.26891   33.02249 8.19718  1.000 49.09146  ? 156 ASP   A C   1 
ATOM   1085 O O   . ASP   A 1 149 ? 1.28123   33.11257 7.49459  1.000 48.57252  ? 156 ASP   A O   1 
ATOM   1086 C CB  . ASP   A 1 149 ? 0.11499   35.49796 8.44341  1.000 43.89935  ? 156 ASP   A CB  1 
ATOM   1087 C CG  . ASP   A 1 149 ? -0.75312  36.74553 8.42467  1.000 50.50514  ? 156 ASP   A CG  1 
ATOM   1088 O OD1 . ASP   A 1 149 ? -1.94845  36.65052 8.07446  1.000 55.22084  ? 156 ASP   A OD1 1 
ATOM   1089 O OD2 . ASP   A 1 149 ? -0.23178  37.82978 8.75870  1.000 54.51210  ? 156 ASP   A OD2 1 
ATOM   1090 N N   . ASP   A 1 150 ? -0.01249  31.92275 8.89496  1.000 39.55703  ? 157 ASP   A N   1 
ATOM   1091 C CA  . ASP   A 1 150 ? 0.90926   30.79494 8.91994  1.000 43.56433  ? 157 ASP   A CA  1 
ATOM   1092 C C   . ASP   A 1 150 ? 0.11686   29.50688 9.10360  1.000 40.34413  ? 157 ASP   A C   1 
ATOM   1093 O O   . ASP   A 1 150 ? -1.10888  29.52061 9.25096  1.000 45.40213  ? 157 ASP   A O   1 
ATOM   1094 C CB  . ASP   A 1 150 ? 1.96470   30.97760 10.01984 1.000 44.20038  ? 157 ASP   A CB  1 
ATOM   1095 C CG  . ASP   A 1 150 ? 3.32413   30.41310 9.63186  1.000 52.41196  ? 157 ASP   A CG  1 
ATOM   1096 O OD1 . ASP   A 1 150 ? 3.37851   29.53706 8.74088  1.000 49.33953  ? 157 ASP   A OD1 1 
ATOM   1097 O OD2 . ASP   A 1 150 ? 4.34238   30.85936 10.20894 1.000 39.97199  ? 157 ASP   A OD2 1 
ATOM   1098 N N   . GLU   A 1 151 ? 0.83263   28.38539 9.07727  1.000 42.32589  ? 158 GLU   A N   1 
ATOM   1099 C CA  . GLU   A 1 151 ? 0.23994   27.08118 9.31922  1.000 43.56455  ? 158 GLU   A CA  1 
ATOM   1100 C C   . GLU   A 1 151 ? 0.14955   26.81309 10.81904 1.000 42.63749  ? 158 GLU   A C   1 
ATOM   1101 O O   . GLU   A 1 151 ? 0.66756   27.56820 11.64612 1.000 40.08730  ? 158 GLU   A O   1 
ATOM   1102 C CB  . GLU   A 1 151 ? 1.06149   25.98350 8.64589  1.000 42.27688  ? 158 GLU   A CB  1 
ATOM   1103 C CG  . GLU   A 1 151 ? 0.78051   25.78044 7.16967  1.000 56.80525  ? 158 GLU   A CG  1 
ATOM   1104 C CD  . GLU   A 1 151 ? 2.02528   25.36029 6.40804  1.000 88.85156  ? 158 GLU   A CD  1 
ATOM   1105 O OE1 . GLU   A 1 151 ? 2.59413   26.20763 5.68661  1.000 93.82282  ? 158 GLU   A OE1 1 
ATOM   1106 O OE2 . GLU   A 1 151 ? 2.44479   24.18909 6.54409  1.000 74.50593  ? 158 GLU   A OE2 1 
ATOM   1107 N N   . GLN   A 1 152 ? -0.50950  25.70962 11.16723 1.000 37.86957  ? 159 GLN   A N   1 
ATOM   1108 C CA  . GLN   A 1 152 ? -0.59114  25.28161 12.55724 1.000 40.01097  ? 159 GLN   A CA  1 
ATOM   1109 C C   . GLN   A 1 152 ? 0.72027   24.62683 12.97345 1.000 38.38448  ? 159 GLN   A C   1 
ATOM   1110 O O   . GLN   A 1 152 ? 1.23635   23.75366 12.27162 1.000 38.35703  ? 159 GLN   A O   1 
ATOM   1111 C CB  . GLN   A 1 152 ? -1.75138  24.30726 12.74835 1.000 44.95358  ? 159 GLN   A CB  1 
ATOM   1112 C CG  . GLN   A 1 152 ? -2.14768  24.10481 14.19640 1.000 42.17767  ? 159 GLN   A CG  1 
ATOM   1113 C CD  . GLN   A 1 152 ? -3.54492  23.54057 14.33499 1.000 43.79062  ? 159 GLN   A CD  1 
ATOM   1114 O OE1 . GLN   A 1 152 ? -4.52215  24.16812 13.92570 1.000 46.23542  ? 159 GLN   A OE1 1 
ATOM   1115 N NE2 . GLN   A 1 152 ? -3.65035  22.35880 14.92807 1.000 45.15940  ? 159 GLN   A NE2 1 
ATOM   1116 N N   . TYR   A 1 153 ? 1.25540   25.04190 14.11714 1.000 36.04830  ? 160 TYR   A N   1 
ATOM   1117 C CA  . TYR   A 1 153 ? 2.55422   24.57518 14.57392 1.000 35.01809  ? 160 TYR   A CA  1 
ATOM   1118 C C   . TYR   A 1 153 ? 2.44209   24.04619 15.99447 1.000 38.14435  ? 160 TYR   A C   1 
ATOM   1119 O O   . TYR   A 1 153 ? 1.55718   24.43727 16.76098 1.000 36.55641  ? 160 TYR   A O   1 
ATOM   1120 C CB  . TYR   A 1 153 ? 3.59934   25.69493 14.51048 1.000 34.70565  ? 160 TYR   A CB  1 
ATOM   1121 C CG  . TYR   A 1 153 ? 4.10559   25.95791 13.11204 1.000 41.56070  ? 160 TYR   A CG  1 
ATOM   1122 C CD1 . TYR   A 1 153 ? 3.77832   27.13212 12.44531 1.000 40.34146  ? 160 TYR   A CD1 1 
ATOM   1123 C CD2 . TYR   A 1 153 ? 4.92361   25.04330 12.46483 1.000 39.66371  ? 160 TYR   A CD2 1 
ATOM   1124 C CE1 . TYR   A 1 153 ? 4.23615   27.38014 11.16484 1.000 42.50866  ? 160 TYR   A CE1 1 
ATOM   1125 C CE2 . TYR   A 1 153 ? 5.39140   25.28686 11.18612 1.000 52.46639  ? 160 TYR   A CE2 1 
ATOM   1126 C CZ  . TYR   A 1 153 ? 5.04235   26.45650 10.54152 1.000 47.79001  ? 160 TYR   A CZ  1 
ATOM   1127 O OH  . TYR   A 1 153 ? 5.50185   26.70345 9.26870  1.000 63.06504  ? 160 TYR   A OH  1 
ATOM   1128 N N   . ALA   A 1 154 ? 3.35831   23.14364 16.33544 1.000 39.42830  ? 161 ALA   A N   1 
ATOM   1129 C CA  . ALA   A 1 154 ? 3.44390   22.56795 17.67009 1.000 37.11918  ? 161 ALA   A CA  1 
ATOM   1130 C C   . ALA   A 1 154 ? 4.82096   22.86846 18.24225 1.000 34.00107  ? 161 ALA   A C   1 
ATOM   1131 O O   . ALA   A 1 154 ? 5.83666   22.42897 17.69109 1.000 45.13603  ? 161 ALA   A O   1 
ATOM   1132 C CB  . ALA   A 1 154 ? 3.17934   21.06006 17.64370 1.000 35.84825  ? 161 ALA   A CB  1 
ATOM   1133 N N   . TRP   A 1 155 ? 4.84429   23.63103 19.33090 1.000 33.26602  ? 162 TRP   A N   1 
ATOM   1134 C CA  . TRP   A 1 155 ? 6.04196   23.93138 20.10381 1.000 32.20414  ? 162 TRP   A CA  1 
ATOM   1135 C C   . TRP   A 1 155 ? 6.02338   23.08116 21.36627 1.000 41.58076  ? 162 TRP   A C   1 
ATOM   1136 O O   . TRP   A 1 155 ? 4.96817   22.89902 21.98099 1.000 40.72971  ? 162 TRP   A O   1 
ATOM   1137 C CB  . TRP   A 1 155 ? 6.06736   25.42103 20.45520 1.000 31.02204  ? 162 TRP   A CB  1 
ATOM   1138 C CG  . TRP   A 1 155 ? 7.21497   25.93642 21.28980 1.000 33.06677  ? 162 TRP   A CG  1 
ATOM   1139 C CD1 . TRP   A 1 155 ? 8.28251   26.66400 20.84583 1.000 33.67129  ? 162 TRP   A CD1 1 
ATOM   1140 C CD2 . TRP   A 1 155 ? 7.36923   25.83219 22.71427 1.000 30.66903  ? 162 TRP   A CD2 1 
ATOM   1141 N NE1 . TRP   A 1 155 ? 9.10094   26.99802 21.89716 1.000 31.92166  ? 162 TRP   A NE1 1 
ATOM   1142 C CE2 . TRP   A 1 155 ? 8.56387   26.49902 23.05454 1.000 31.18114  ? 162 TRP   A CE2 1 
ATOM   1143 C CE3 . TRP   A 1 155 ? 6.62106   25.22914 23.73246 1.000 34.45096  ? 162 TRP   A CE3 1 
ATOM   1144 C CZ2 . TRP   A 1 155 ? 9.02854   26.57856 24.36824 1.000 33.45956  ? 162 TRP   A CZ2 1 
ATOM   1145 C CZ3 . TRP   A 1 155 ? 7.08556   25.30824 25.03818 1.000 30.40765  ? 162 TRP   A CZ3 1 
ATOM   1146 C CH2 . TRP   A 1 155 ? 8.27766   25.97802 25.34236 1.000 34.69213  ? 162 TRP   A CH2 1 
ATOM   1147 N N   . GLU   A 1 156 ? 7.18446   22.55232 21.74904 1.000 33.17020  ? 163 GLU   A N   1 
ATOM   1148 C CA  . GLU   A 1 156 ? 7.25332   21.69166 22.92181 1.000 34.98014  ? 163 GLU   A CA  1 
ATOM   1149 C C   . GLU   A 1 156 ? 8.61157   21.82602 23.59512 1.000 39.30142  ? 163 GLU   A C   1 
ATOM   1150 O O   . GLU   A 1 156 ? 9.63777   21.93647 22.92024 1.000 36.01471  ? 163 GLU   A O   1 
ATOM   1151 C CB  . GLU   A 1 156 ? 7.00009   20.22604 22.54483 1.000 40.70541  ? 163 GLU   A CB  1 
ATOM   1152 C CG  . GLU   A 1 156 ? 6.55139   19.35824 23.70719 1.000 41.43741  ? 163 GLU   A CG  1 
ATOM   1153 C CD  . GLU   A 1 156 ? 6.21346   17.94325 23.28172 1.000 60.58772  ? 163 GLU   A CD  1 
ATOM   1154 O OE1 . GLU   A 1 156 ? 7.14987   17.16418 22.99891 1.000 66.00369  ? 163 GLU   A OE1 1 
ATOM   1155 O OE2 . GLU   A 1 156 ? 5.00915   17.61056 23.23192 1.000 56.42491  ? 163 GLU   A OE2 1 
ATOM   1156 N N   . SER   A 1 157 ? 8.61480   21.80304 24.92684 1.000 39.16671  ? 164 SER   A N   1 
ATOM   1157 C CA  . SER   A 1 157 ? 9.87486   21.75643 25.65586 1.000 39.11929  ? 164 SER   A CA  1 
ATOM   1158 C C   . SER   A 1 157 ? 9.66829   21.12290 27.02426 1.000 35.62914  ? 164 SER   A C   1 
ATOM   1159 O O   . SER   A 1 157 ? 8.66218   21.38115 27.69212 1.000 39.84525  ? 164 SER   A O   1 
ATOM   1160 C CB  . SER   A 1 157 ? 10.48695  23.15041 25.82533 1.000 34.82404  ? 164 SER   A CB  1 
ATOM   1161 O OG  . SER   A 1 157 ? 11.67626  23.07728 26.59720 1.000 35.13887  ? 164 SER   A OG  1 
ATOM   1162 N N   . SER   A 1 158 ? 10.63713  20.29764 27.42810 1.000 37.92762  ? 165 SER   A N   1 
ATOM   1163 C CA  . SER   A 1 158 ? 10.78377  19.82018 28.79903 1.000 38.50595  ? 165 SER   A CA  1 
ATOM   1164 C C   . SER   A 1 158 ? 11.90719  20.54798 29.52955 1.000 37.88362  ? 165 SER   A C   1 
ATOM   1165 O O   . SER   A 1 158 ? 12.51546  19.98850 30.44982 1.000 40.94733  ? 165 SER   A O   1 
ATOM   1166 C CB  . SER   A 1 158 ? 11.04049  18.30988 28.82556 1.000 36.33993  ? 165 SER   A CB  1 
ATOM   1167 O OG  . SER   A 1 158 ? 9.98306   17.57668 28.23600 1.000 49.12427  ? 165 SER   A OG  1 
ATOM   1168 N N   . ALA   A 1 159 ? 12.19969  21.77742 29.11972 1.000 40.47850  ? 166 ALA   A N   1 
ATOM   1169 C CA  . ALA   A 1 159 ? 13.33533  22.56633 29.61399 1.000 39.89064  ? 166 ALA   A CA  1 
ATOM   1170 C C   . ALA   A 1 159 ? 14.62093  21.79444 29.30504 1.000 38.88495  ? 166 ALA   A C   1 
ATOM   1171 O O   . ALA   A 1 159 ? 14.69618  21.05988 28.31168 1.000 46.46924  ? 166 ALA   A O   1 
ATOM   1172 C CB  . ALA   A 1 159 ? 13.14026  22.92005 31.07246 1.000 35.22367  ? 166 ALA   A CB  1 
ATOM   1173 N N   . GLY   A 1 160 ? 15.64616  21.94715 30.13675 1.000 37.59639  ? 167 GLY   A N   1 
ATOM   1174 C CA  . GLY   A 1 160 ? 16.92642  21.35237 29.82310 1.000 39.13592  ? 167 GLY   A CA  1 
ATOM   1175 C C   . GLY   A 1 160 ? 17.68890  22.04217 28.71579 1.000 39.11834  ? 167 GLY   A C   1 
ATOM   1176 O O   . GLY   A 1 160 ? 18.70719  21.50861 28.26113 1.000 45.35416  ? 167 GLY   A O   1 
ATOM   1177 N N   . GLY   A 1 161 ? 17.22545  23.20357 28.25627 1.000 42.66245  ? 168 GLY   A N   1 
ATOM   1178 C CA  . GLY   A 1 161 ? 17.96201  24.00685 27.30271 1.000 43.82406  ? 168 GLY   A CA  1 
ATOM   1179 C C   . GLY   A 1 161 ? 17.54631  23.88060 25.85184 1.000 42.47406  ? 168 GLY   A C   1 
ATOM   1180 O O   . GLY   A 1 161 ? 18.14231  24.55132 24.99979 1.000 43.34998  ? 168 GLY   A O   1 
ATOM   1181 N N   . SER   A 1 162 ? 16.55028  23.05728 25.53497 1.000 39.99204  ? 169 SER   A N   1 
ATOM   1182 C CA  . SER   A 1 162 ? 16.14017  22.88551 24.15009 1.000 44.06159  ? 169 SER   A CA  1 
ATOM   1183 C C   . SER   A 1 162 ? 14.62080  22.86518 24.04831 1.000 40.28417  ? 169 SER   A C   1 
ATOM   1184 O O   . SER   A 1 162 ? 13.90807  22.59563 25.01902 1.000 38.87788  ? 169 SER   A O   1 
ATOM   1185 C CB  . SER   A 1 162 ? 16.73967  21.60634 23.53672 1.000 38.79884  ? 169 SER   A CB  1 
ATOM   1186 O OG  . SER   A 1 162 ? 16.18721  20.43488 24.11416 1.000 41.50056  ? 169 SER   A OG  1 
ATOM   1187 N N   . PHE   A 1 163 ? 14.13629  23.18145 22.84918 1.000 34.96512  ? 170 PHE   A N   1 
ATOM   1188 C CA  . PHE   A 1 163 ? 12.72909  23.05836 22.50421 1.000 34.95701  ? 170 PHE   A CA  1 
ATOM   1189 C C   . PHE   A 1 163 ? 12.62992  22.60018 21.05638 1.000 35.70584  ? 170 PHE   A C   1 
ATOM   1190 O O   . PHE   A 1 163 ? 13.60094  22.66514 20.29714 1.000 36.85822  ? 170 PHE   A O   1 
ATOM   1191 C CB  . PHE   A 1 163 ? 11.96494  24.37485 22.72492 1.000 32.67672  ? 170 PHE   A CB  1 
ATOM   1192 C CG  . PHE   A 1 163 ? 12.42584  25.50821 21.84979 1.000 35.31409  ? 170 PHE   A CG  1 
ATOM   1193 C CD1 . PHE   A 1 163 ? 13.48780  26.31072 22.23756 1.000 32.36029  ? 170 PHE   A CD1 1 
ATOM   1194 C CD2 . PHE   A 1 163 ? 11.78610  25.78514 20.64982 1.000 34.39166  ? 170 PHE   A CD2 1 
ATOM   1195 C CE1 . PHE   A 1 163 ? 13.91192  27.36208 21.43768 1.000 38.14704  ? 170 PHE   A CE1 1 
ATOM   1196 C CE2 . PHE   A 1 163 ? 12.20476  26.83610 19.84550 1.000 31.23222  ? 170 PHE   A CE2 1 
ATOM   1197 C CZ  . PHE   A 1 163 ? 13.26765  27.62560 20.24125 1.000 31.53252  ? 170 PHE   A CZ  1 
ATOM   1198 N N   . THR   A 1 164 ? 11.44931  22.10845 20.68651 1.000 33.79611  ? 171 THR   A N   1 
ATOM   1199 C CA  . THR   A 1 164 ? 11.18543  21.63486 19.33722 1.000 34.62167  ? 171 THR   A CA  1 
ATOM   1200 C C   . THR   A 1 164 ? 10.01179  22.39425 18.73492 1.000 36.33095  ? 171 THR   A C   1 
ATOM   1201 O O   . THR   A 1 164 ? 9.11256   22.85252 19.44625 1.000 36.52710  ? 171 THR   A O   1 
ATOM   1202 C CB  . THR   A 1 164 ? 10.87020  20.12912 19.30174 1.000 35.94350  ? 171 THR   A CB  1 
ATOM   1203 O OG1 . THR   A 1 164 ? 9.68701   19.86837 20.06698 1.000 37.62263  ? 171 THR   A OG1 1 
ATOM   1204 C CG2 . THR   A 1 164 ? 12.02803  19.31326 19.85584 1.000 37.24740  ? 171 THR   A CG2 1 
ATOM   1205 N N   . VAL   A 1 165 ? 10.02896  22.51416 17.41008 1.000 34.18883  ? 172 VAL   A N   1 
ATOM   1206 C CA  . VAL   A 1 165 ? 8.92767   23.08403 16.64795 1.000 33.59828  ? 172 VAL   A CA  1 
ATOM   1207 C C   . VAL   A 1 165 ? 8.66339   22.17394 15.45912 1.000 37.78347  ? 172 VAL   A C   1 
ATOM   1208 O O   . VAL   A 1 165 ? 9.60146   21.70145 14.80872 1.000 39.37363  ? 172 VAL   A O   1 
ATOM   1209 C CB  . VAL   A 1 165 ? 9.23579   24.52385 16.18223 1.000 36.32315  ? 172 VAL   A CB  1 
ATOM   1210 C CG1 . VAL   A 1 165 ? 8.11532   25.05391 15.30105 1.000 35.25688  ? 172 VAL   A CG1 1 
ATOM   1211 C CG2 . VAL   A 1 165 ? 9.45133   25.43424 17.38107 1.000 31.46432  ? 172 VAL   A CG2 1 
ATOM   1212 N N   . ARG   A 1 166 ? 7.38787   21.90954 15.18941 1.000 42.24117  ? 173 ARG   A N   1 
ATOM   1213 C CA  . ARG   A 1 166 ? 6.99677   21.10970 14.03911 1.000 41.91458  ? 173 ARG   A CA  1 
ATOM   1214 C C   . ARG   A 1 166 ? 5.63961   21.58944 13.55209 1.000 41.24461  ? 173 ARG   A C   1 
ATOM   1215 O O   . ARG   A 1 166 ? 4.89802   22.25692 14.27859 1.000 40.61552  ? 173 ARG   A O   1 
ATOM   1216 C CB  . ARG   A 1 166 ? 6.93345   19.61903 14.38476 1.000 43.62612  ? 173 ARG   A CB  1 
ATOM   1217 C CG  . ARG   A 1 166 ? 5.99519   19.33127 15.54099 1.000 45.23189  ? 173 ARG   A CG  1 
ATOM   1218 C CD  . ARG   A 1 166 ? 5.41682   17.93181 15.49073 1.000 55.47427  ? 173 ARG   A CD  1 
ATOM   1219 N NE  . ARG   A 1 166 ? 4.83673   17.56120 16.77647 1.000 78.46235  ? 173 ARG   A NE  1 
ATOM   1220 C CZ  . ARG   A 1 166 ? 3.53596   17.42698 17.00213 1.000 75.16717  ? 173 ARG   A CZ  1 
ATOM   1221 N NH1 . ARG   A 1 166 ? 2.64321   17.61848 16.04283 1.000 55.63468  ? 173 ARG   A NH1 1 
ATOM   1222 N NH2 . ARG   A 1 166 ? 3.11949   17.09949 18.22287 1.000 73.99029  ? 173 ARG   A NH2 1 
ATOM   1223 N N   . THR   A 1 167 ? 5.32087   21.24538 12.30833 1.000 40.50080  ? 174 THR   A N   1 
ATOM   1224 C CA  . THR   A 1 167 ? 3.96962   21.46071 11.81036 1.000 50.64350  ? 174 THR   A CA  1 
ATOM   1225 C C   . THR   A 1 167 ? 3.03087   20.47035 12.48645 1.000 43.48927  ? 174 THR   A C   1 
ATOM   1226 O O   . THR   A 1 167 ? 3.33449   19.27778 12.57658 1.000 54.71378  ? 174 THR   A O   1 
ATOM   1227 C CB  . THR   A 1 167 ? 3.91784   21.29384 10.29089 1.000 43.41781  ? 174 THR   A CB  1 
ATOM   1228 O OG1 . THR   A 1 167 ? 4.23746   19.94102 9.94760  1.000 56.64290  ? 174 THR   A OG1 1 
ATOM   1229 C CG2 . THR   A 1 167 ? 4.91261   22.21934 9.61991  1.000 40.10132  ? 174 THR   A CG2 1 
ATOM   1230 N N   . ASP   A 1 168 ? 1.89979   20.96253 12.98007 1.000 39.88527  ? 175 ASP   A N   1 
ATOM   1231 C CA  . ASP   A 1 168 ? 0.97182   20.10785 13.70563 1.000 47.40510  ? 175 ASP   A CA  1 
ATOM   1232 C C   . ASP   A 1 168 ? 0.04366   19.38986 12.73614 1.000 58.16709  ? 175 ASP   A C   1 
ATOM   1233 O O   . ASP   A 1 168 ? -0.56240  20.01568 11.86044 1.000 59.30237  ? 175 ASP   A O   1 
ATOM   1234 C CB  . ASP   A 1 168 ? 0.16120   20.91847 14.71380 1.000 43.61837  ? 175 ASP   A CB  1 
ATOM   1235 C CG  . ASP   A 1 168 ? -0.75283  20.04599 15.55346 1.000 52.61406  ? 175 ASP   A CG  1 
ATOM   1236 O OD1 . ASP   A 1 168 ? -0.34714  18.91367 15.89468 1.000 65.63523  ? 175 ASP   A OD1 1 
ATOM   1237 O OD2 . ASP   A 1 168 ? -1.87528  20.48905 15.87230 1.000 63.00840  ? 175 ASP   A OD2 1 
ATOM   1238 N N   . THR   A 1 169 ? -0.06586  18.07140 12.90251 1.000 76.42722  ? 176 THR   A N   1 
ATOM   1239 C CA  . THR   A 1 169 ? -0.88410  17.22807 12.04350 1.000 84.51374  ? 176 THR   A CA  1 
ATOM   1240 C C   . THR   A 1 169 ? -2.26401  16.93992 12.62048 1.000 81.10306  ? 176 THR   A C   1 
ATOM   1241 O O   . THR   A 1 169 ? -3.13904  16.47412 11.88219 1.000 73.91074  ? 176 THR   A O   1 
ATOM   1242 C CB  . THR   A 1 169 ? -0.16469  15.89842 11.77270 1.000 88.63372  ? 176 THR   A CB  1 
ATOM   1243 O OG1 . THR   A 1 169 ? 0.22769   15.30137 13.01750 1.000 78.87403  ? 176 THR   A OG1 1 
ATOM   1244 C CG2 . THR   A 1 169 ? 1.06797   16.12035 10.90760 1.000 73.97085  ? 176 THR   A CG2 1 
ATOM   1245 N N   . GLY   A 1 170 ? -2.48060  17.21077 13.90711 1.000 77.85631  ? 177 GLY   A N   1 
ATOM   1246 C CA  . GLY   A 1 170 ? -3.72393  16.86161 14.56835 1.000 77.01964  ? 177 GLY   A CA  1 
ATOM   1247 C C   . GLY   A 1 170 ? -4.91287  17.72674 14.20009 1.000 74.81007  ? 177 GLY   A C   1 
ATOM   1248 O O   . GLY   A 1 170 ? -4.98497  18.26406 13.09013 1.000 71.87685  ? 177 GLY   A O   1 
ATOM   1249 N N   . GLU   A 1 171 ? -5.85241  17.86264 15.12947 1.000 67.88238  ? 178 GLU   A N   1 
ATOM   1250 C CA  . GLU   A 1 171 ? -7.08293  18.60237 14.88296 1.000 72.10383  ? 178 GLU   A CA  1 
ATOM   1251 C C   . GLU   A 1 171 ? -6.77866  20.06539 14.57436 1.000 64.79944  ? 178 GLU   A C   1 
ATOM   1252 O O   . GLU   A 1 171 ? -6.09515  20.72832 15.36949 1.000 50.79804  ? 178 GLU   A O   1 
ATOM   1253 C CB  . GLU   A 1 171 ? -8.01094  18.50370 16.09351 1.000 77.78091  ? 178 GLU   A CB  1 
ATOM   1254 C CG  . GLU   A 1 171 ? -9.49214  18.55020 15.75084 1.000 89.41564  ? 178 GLU   A CG  1 
ATOM   1255 C CD  . GLU   A 1 171 ? -9.92932  17.38284 14.88254 1.000 104.75946 ? 178 GLU   A CD  1 
ATOM   1256 O OE1 . GLU   A 1 171 ? -9.75330  16.22120 15.31052 1.000 104.08402 ? 178 GLU   A OE1 1 
ATOM   1257 O OE2 . GLU   A 1 171 ? -10.45088 17.62623 13.77272 1.000 105.31471 ? 178 GLU   A OE2 1 
ATOM   1258 N N   . PRO   A 1 172 ? -7.23979  20.59771 13.44315 1.000 57.93709  ? 179 PRO   A N   1 
ATOM   1259 C CA  . PRO   A 1 172 ? -7.05111  22.02843 13.17179 1.000 59.45741  ? 179 PRO   A CA  1 
ATOM   1260 C C   . PRO   A 1 172 ? -7.76701  22.88844 14.20467 1.000 52.54654  ? 179 PRO   A C   1 
ATOM   1261 O O   . PRO   A 1 172 ? -8.88817  22.59072 14.62098 1.000 61.88245  ? 179 PRO   A O   1 
ATOM   1262 C CB  . PRO   A 1 172 ? -7.65449  22.20480 11.77342 1.000 48.28652  ? 179 PRO   A CB  1 
ATOM   1263 C CG  . PRO   A 1 172 ? -7.58540  20.83434 11.15919 1.000 51.67017  ? 179 PRO   A CG  1 
ATOM   1264 C CD  . PRO   A 1 172 ? -7.82516  19.88729 12.29423 1.000 60.51668  ? 179 PRO   A CD  1 
ATOM   1265 N N   . MET   A 1 173 ? -7.10541  23.97054 14.61434 1.000 49.51925  ? 180 MET   A N   1 
ATOM   1266 C CA  . MET   A 1 173 ? -7.64577  24.84849 15.64544 1.000 53.30742  ? 180 MET   A CA  1 
ATOM   1267 C C   . MET   A 1 173 ? -8.47997  25.99144 15.09078 1.000 53.01588  ? 180 MET   A C   1 
ATOM   1268 O O   . MET   A 1 173 ? -9.37567  26.48485 15.78514 1.000 59.02572  ? 180 MET   A O   1 
ATOM   1269 C CB  . MET   A 1 173 ? -6.51786  25.45874 16.47413 1.000 53.49844  ? 180 MET   A CB  1 
ATOM   1270 C CG  . MET   A 1 173 ? -5.91935  24.55165 17.51145 1.000 61.11667  ? 180 MET   A CG  1 
ATOM   1271 S SD  . MET   A 1 173 ? -4.39532  25.31094 18.07498 1.000 62.88641  ? 180 MET   A SD  1 
ATOM   1272 C CE  . MET   A 1 173 ? -5.05998  26.72482 18.93970 1.000 41.79011  ? 180 MET   A CE  1 
ATOM   1273 N N   . GLY   A 1 174 ? -8.19036  26.44379 13.87467 1.000 39.28788  ? 181 GLY   A N   1 
ATOM   1274 C CA  . GLY   A 1 174 ? -8.81179  27.64717 13.35689 1.000 45.59745  ? 181 GLY   A CA  1 
ATOM   1275 C C   . GLY   A 1 174 ? -7.94893  28.87516 13.56867 1.000 44.22133  ? 181 GLY   A C   1 
ATOM   1276 O O   . GLY   A 1 174 ? -7.43846  29.45840 12.60661 1.000 40.35769  ? 181 GLY   A O   1 
ATOM   1277 N N   . ARG   A 1 175 ? -7.78027  29.27082 14.82972 1.000 39.04563  ? 182 ARG   A N   1 
ATOM   1278 C CA  . ARG   A 1 175 ? -6.95385  30.40622 15.22053 1.000 39.51766  ? 182 ARG   A CA  1 
ATOM   1279 C C   . ARG   A 1 175 ? -6.86053  30.43086 16.73685 1.000 29.71206  ? 182 ARG   A C   1 
ATOM   1280 O O   . ARG   A 1 175 ? -7.85458  30.19268 17.42505 1.000 35.84735  ? 182 ARG   A O   1 
ATOM   1281 C CB  . ARG   A 1 175 ? -7.52857  31.74041 14.71483 1.000 30.51672  ? 182 ARG   A CB  1 
ATOM   1282 C CG  . ARG   A 1 175 ? -6.53456  32.89585 14.75768 1.000 31.41205  ? 182 ARG   A CG  1 
ATOM   1283 C CD  . ARG   A 1 175 ? -7.23669  34.25162 14.75494 1.000 36.03133  ? 182 ARG   A CD  1 
ATOM   1284 N NE  . ARG   A 1 175 ? -8.12819  34.40696 15.89675 1.000 28.31574  ? 182 ARG   A NE  1 
ATOM   1285 C CZ  . ARG   A 1 175 ? -9.45168  34.41564 15.81648 1.000 38.71476  ? 182 ARG   A CZ  1 
ATOM   1286 N NH1 . ARG   A 1 175 ? -10.07432 34.30223 14.65484 1.000 31.10837  ? 182 ARG   A NH1 1 
ATOM   1287 N NH2 . ARG   A 1 175 ? -10.16849 34.54038 16.92985 1.000 30.97715  ? 182 ARG   A NH2 1 
ATOM   1288 N N   . GLY   A 1 176 ? -5.67500  30.72422 17.24907 1.000 29.74358  ? 183 GLY   A N   1 
ATOM   1289 C CA  . GLY   A 1 176 ? -5.50877  30.83043 18.67824 1.000 26.62238  ? 183 GLY   A CA  1 
ATOM   1290 C C   . GLY   A 1 176 ? -4.29905  30.05415 19.13255 1.000 33.83616  ? 183 GLY   A C   1 
ATOM   1291 O O   . GLY   A 1 176 ? -3.40301  29.73796 18.34229 1.000 39.86221  ? 183 GLY   A O   1 
ATOM   1292 N N   . THR   A 1 177 ? -4.27886  29.73683 20.42216 1.000 30.62338  ? 184 THR   A N   1 
ATOM   1293 C CA  . THR   A 1 177 ? -3.15273  29.05047 21.02924 1.000 36.23111  ? 184 THR   A CA  1 
ATOM   1294 C C   . THR   A 1 177 ? -3.66409  28.11745 22.11489 1.000 44.66167  ? 184 THR   A C   1 
ATOM   1295 O O   . THR   A 1 177 ? -4.57869  28.46570 22.86787 1.000 36.48875  ? 184 THR   A O   1 
ATOM   1296 C CB  . THR   A 1 177 ? -2.14227  30.04986 21.60687 1.000 35.04652  ? 184 THR   A CB  1 
ATOM   1297 O OG1 . THR   A 1 177 ? -1.54427  30.78790 20.53509 1.000 38.92450  ? 184 THR   A OG1 1 
ATOM   1298 C CG2 . THR   A 1 177 ? -1.05182  29.33043 22.38759 1.000 29.27874  ? 184 THR   A CG2 1 
ATOM   1299 N N   . LYS   A 1 178 ? -3.07677  26.92536 22.17050 1.000 35.71367  ? 185 LYS   A N   1 
ATOM   1300 C CA  . LYS   A 1 178 ? -3.39920  25.90653 23.15879 1.000 32.93485  ? 185 LYS   A CA  1 
ATOM   1301 C C   . LYS   A 1 178 ? -2.13245  25.57826 23.93755 1.000 33.60758  ? 185 LYS   A C   1 
ATOM   1302 O O   . LYS   A 1 178 ? -1.16019  25.07996 23.36030 1.000 34.86200  ? 185 LYS   A O   1 
ATOM   1303 C CB  . LYS   A 1 178 ? -3.95751  24.65890 22.47245 1.000 34.25877  ? 185 LYS   A CB  1 
ATOM   1304 C CG  . LYS   A 1 178 ? -4.34422  23.53711 23.40710 1.000 50.22376  ? 185 LYS   A CG  1 
ATOM   1305 C CD  . LYS   A 1 178 ? -5.47873  22.70671 22.82881 1.000 55.95859  ? 185 LYS   A CD  1 
ATOM   1306 C CE  . LYS   A 1 178 ? -5.33858  22.52206 21.32440 1.000 47.85491  ? 185 LYS   A CE  1 
ATOM   1307 N NZ  . LYS   A 1 178 ? -6.01436  21.27097 20.86716 1.000 67.61559  ? 185 LYS   A NZ  1 
ATOM   1308 N N   . VAL   A 1 179 ? -2.13930  25.86388 25.23616 1.000 31.64558  ? 186 VAL   A N   1 
ATOM   1309 C CA  . VAL   A 1 179 ? -1.00680  25.58735 26.11634 1.000 31.96040  ? 186 VAL   A CA  1 
ATOM   1310 C C   . VAL   A 1 179 ? -1.34360  24.34134 26.92704 1.000 32.88908  ? 186 VAL   A C   1 
ATOM   1311 O O   . VAL   A 1 179 ? -2.24399  24.36496 27.77267 1.000 30.91090  ? 186 VAL   A O   1 
ATOM   1312 C CB  . VAL   A 1 179 ? -0.69604  26.77619 27.03720 1.000 30.84677  ? 186 VAL   A CB  1 
ATOM   1313 C CG1 . VAL   A 1 179 ? 0.41306   26.40634 28.01386 1.000 30.62649  ? 186 VAL   A CG1 1 
ATOM   1314 C CG2 . VAL   A 1 179 ? -0.32181  28.01294 26.22518 1.000 27.27381  ? 186 VAL   A CG2 1 
ATOM   1315 N N   . ILE   A 1 180 ? -0.62054  23.25172 26.68402 1.000 29.98196  ? 187 ILE   A N   1 
ATOM   1316 C CA  . ILE   A 1 180 ? -0.85964  21.98114 27.35905 1.000 32.90656  ? 187 ILE   A CA  1 
ATOM   1317 C C   . ILE   A 1 180 ? 0.23285   21.77140 28.39746 1.000 38.26402  ? 187 ILE   A C   1 
ATOM   1318 O O   . ILE   A 1 180 ? 1.41160   21.63528 28.04911 1.000 35.63882  ? 187 ILE   A O   1 
ATOM   1319 C CB  . ILE   A 1 180 ? -0.89785  20.81391 26.36288 1.000 36.98259  ? 187 ILE   A CB  1 
ATOM   1320 C CG1 . ILE   A 1 180 ? -1.94639  21.07138 25.27739 1.000 38.31630  ? 187 ILE   A CG1 1 
ATOM   1321 C CG2 . ILE   A 1 180 ? -1.18588  19.51218 27.09135 1.000 32.11275  ? 187 ILE   A CG2 1 
ATOM   1322 C CD1 . ILE   A 1 180 ? -1.90279  20.06830 24.14056 1.000 38.57083  ? 187 ILE   A CD1 1 
ATOM   1323 N N   . LEU   A 1 181 ? -0.15836  21.72550 29.67188 1.000 37.03486  ? 188 LEU   A N   1 
ATOM   1324 C CA  . LEU   A 1 181 ? 0.77629   21.57953 30.78276 1.000 35.09229  ? 188 LEU   A CA  1 
ATOM   1325 C C   . LEU   A 1 181 ? 0.75591   20.13761 31.27206 1.000 37.48098  ? 188 LEU   A C   1 
ATOM   1326 O O   . LEU   A 1 181 ? -0.22333  19.69713 31.88049 1.000 36.86817  ? 188 LEU   A O   1 
ATOM   1327 C CB  . LEU   A 1 181 ? 0.42388   22.53586 31.91893 1.000 33.11103  ? 188 LEU   A CB  1 
ATOM   1328 C CG  . LEU   A 1 181 ? 0.20541   23.98926 31.51476 1.000 36.32490  ? 188 LEU   A CG  1 
ATOM   1329 C CD1 . LEU   A 1 181 ? -0.40032  24.74821 32.67020 1.000 34.97826  ? 188 LEU   A CD1 1 
ATOM   1330 C CD2 . LEU   A 1 181 ? 1.51542   24.62139 31.08060 1.000 33.13693  ? 188 LEU   A CD2 1 
ATOM   1331 N N   . HIS   A 1 182 ? 1.84113   19.41050 31.01689 1.000 32.78806  ? 189 HIS   A N   1 
ATOM   1332 C CA  . HIS   A 1 182 ? 2.02755   18.06614 31.55785 1.000 36.62887  ? 189 HIS   A CA  1 
ATOM   1333 C C   . HIS   A 1 182 ? 2.54021   18.21131 32.98653 1.000 39.39050  ? 189 HIS   A C   1 
ATOM   1334 O O   . HIS   A 1 182 ? 3.74169   18.37165 33.22036 1.000 41.84444  ? 189 HIS   A O   1 
ATOM   1335 C CB  . HIS   A 1 182 ? 2.98402   17.26933 30.67651 1.000 34.84023  ? 189 HIS   A CB  1 
ATOM   1336 C CG  . HIS   A 1 182 ? 2.58030   17.23764 29.23320 1.000 46.23188  ? 189 HIS   A CG  1 
ATOM   1337 N ND1 . HIS   A 1 182 ? 1.78657   16.24275 28.70181 1.000 45.67330  ? 189 HIS   A ND1 1 
ATOM   1338 C CD2 . HIS   A 1 182 ? 2.82596   18.10255 28.21990 1.000 48.41199  ? 189 HIS   A CD2 1 
ATOM   1339 C CE1 . HIS   A 1 182 ? 1.58091   16.48369 27.41937 1.000 40.95782  ? 189 HIS   A CE1 1 
ATOM   1340 N NE2 . HIS   A 1 182 ? 2.19755   17.60863 27.10239 1.000 38.19494  ? 189 HIS   A NE2 1 
ATOM   1341 N N   . LEU   A 1 183 ? 1.62010   18.15870 33.94633 1.000 39.45580  ? 190 LEU   A N   1 
ATOM   1342 C CA  . LEU   A 1 183 ? 1.92596   18.51806 35.32441 1.000 37.33951  ? 190 LEU   A CA  1 
ATOM   1343 C C   . LEU   A 1 183 ? 2.87884   17.52113 35.97438 1.000 49.22330  ? 190 LEU   A C   1 
ATOM   1344 O O   . LEU   A 1 183 ? 2.87250   16.32361 35.67135 1.000 50.19653  ? 190 LEU   A O   1 
ATOM   1345 C CB  . LEU   A 1 183 ? 0.63971   18.59935 36.14401 1.000 36.45849  ? 190 LEU   A CB  1 
ATOM   1346 C CG  . LEU   A 1 183 ? -0.38233  19.62604 35.65744 1.000 43.38986  ? 190 LEU   A CG  1 
ATOM   1347 C CD1 . LEU   A 1 183 ? -1.58575  19.65988 36.58238 1.000 35.89431  ? 190 LEU   A CD1 1 
ATOM   1348 C CD2 . LEU   A 1 183 ? 0.25496   21.00200 35.54648 1.000 34.30809  ? 190 LEU   A CD2 1 
ATOM   1349 N N   . LYS   A 1 184 ? 3.70020   18.03267 36.88929 1.000 45.38098  ? 191 LYS   A N   1 
ATOM   1350 C CA  . LYS   A 1 184 ? 4.53264   17.16883 37.70923 1.000 48.02083  ? 191 LYS   A CA  1 
ATOM   1351 C C   . LYS   A 1 184 ? 3.65799   16.29007 38.59804 1.000 52.73477  ? 191 LYS   A C   1 
ATOM   1352 O O   . LYS   A 1 184 ? 2.48418   16.58237 38.84673 1.000 43.43483  ? 191 LYS   A O   1 
ATOM   1353 C CB  . LYS   A 1 184 ? 5.48739   17.99598 38.56610 1.000 44.77453  ? 191 LYS   A CB  1 
ATOM   1354 C CG  . LYS   A 1 184 ? 6.40997   18.89937 37.77185 1.000 51.50642  ? 191 LYS   A CG  1 
ATOM   1355 C CD  . LYS   A 1 184 ? 7.04745   19.95019 38.66790 1.000 53.74543  ? 191 LYS   A CD  1 
ATOM   1356 C CE  . LYS   A 1 184 ? 7.91729   20.90433 37.86766 1.000 52.81230  ? 191 LYS   A CE  1 
ATOM   1357 N NZ  . LYS   A 1 184 ? 8.49170   21.98393 38.71979 1.000 59.12627  ? 191 LYS   A NZ  1 
ATOM   1358 N N   . GLU   A 1 185 ? 4.25679   15.19935 39.08506 1.000 48.22887  ? 192 GLU   A N   1 
ATOM   1359 C CA  . GLU   A 1 185 ? 3.51601   14.21335 39.86705 1.000 54.59360  ? 192 GLU   A CA  1 
ATOM   1360 C C   . GLU   A 1 185 ? 2.86697   14.82928 41.10280 1.000 55.19941  ? 192 GLU   A C   1 
ATOM   1361 O O   . GLU   A 1 185 ? 1.76626   14.42323 41.49268 1.000 60.75862  ? 192 GLU   A O   1 
ATOM   1362 C CB  . GLU   A 1 185 ? 4.45238   13.06919 40.26622 1.000 52.34245  ? 192 GLU   A CB  1 
ATOM   1363 C CG  . GLU   A 1 185 ? 3.85961   12.05724 41.23973 1.000 69.96527  ? 192 GLU   A CG  1 
ATOM   1364 C CD  . GLU   A 1 185 ? 4.61227   10.73437 41.24110 1.000 84.70545  ? 192 GLU   A CD  1 
ATOM   1365 O OE1 . GLU   A 1 185 ? 5.46877   10.53292 40.35240 1.000 70.06247  ? 192 GLU   A OE1 1 
ATOM   1366 O OE2 . GLU   A 1 185 ? 4.34703   9.89627  42.13075 1.000 84.04584  ? 192 GLU   A OE2 1 
ATOM   1367 N N   . ASP   A 1 186 ? 3.51620   15.81231 41.72044 1.000 48.51038  ? 193 ASP   A N   1 
ATOM   1368 C CA  . ASP   A 1 186 ? 3.04805   16.39067 42.97172 1.000 48.96648  ? 193 ASP   A CA  1 
ATOM   1369 C C   . ASP   A 1 186 ? 2.20470   17.64673 42.77436 1.000 54.39711  ? 193 ASP   A C   1 
ATOM   1370 O O   . ASP   A 1 186 ? 1.83531   18.28884 43.76189 1.000 49.88827  ? 193 ASP   A O   1 
ATOM   1371 C CB  . ASP   A 1 186 ? 4.24037   16.71099 43.87791 1.000 52.90966  ? 193 ASP   A CB  1 
ATOM   1372 C CG  . ASP   A 1 186 ? 5.31829   17.51248 43.16344 1.000 74.85241  ? 193 ASP   A CG  1 
ATOM   1373 O OD1 . ASP   A 1 186 ? 5.88662   18.43786 43.78299 1.000 76.25520  ? 193 ASP   A OD1 1 
ATOM   1374 O OD2 . ASP   A 1 186 ? 5.60003   17.21435 41.98265 1.000 72.20121  ? 193 ASP   A OD2 1 
ATOM   1375 N N   . GLN   A 1 187 ? 1.88652   18.01258 41.53345 1.000 49.07213  ? 194 GLN   A N   1 
ATOM   1376 C CA  . GLN   A 1 187 ? 1.17021   19.25092 41.25184 1.000 46.37206  ? 194 GLN   A CA  1 
ATOM   1377 C C   . GLN   A 1 187 ? -0.22257  18.99736 40.68243 1.000 42.09643  ? 194 GLN   A C   1 
ATOM   1378 O O   . GLN   A 1 187 ? -0.75205  19.82458 39.93741 1.000 47.58891  ? 194 GLN   A O   1 
ATOM   1379 C CB  . GLN   A 1 187 ? 1.98342   20.12947 40.30260 1.000 42.61916  ? 194 GLN   A CB  1 
ATOM   1380 C CG  . GLN   A 1 187 ? 3.37409   20.47849 40.82014 1.000 42.25882  ? 194 GLN   A CG  1 
ATOM   1381 C CD  . GLN   A 1 187 ? 3.33033   21.22540 42.13958 1.000 48.28105  ? 194 GLN   A CD  1 
ATOM   1382 O OE1 . GLN   A 1 187 ? 2.47190   22.08227 42.35221 1.000 50.29493  ? 194 GLN   A OE1 1 
ATOM   1383 N NE2 . GLN   A 1 187 ? 4.25648   20.90313 43.03461 1.000 46.24196  ? 194 GLN   A NE2 1 
ATOM   1384 N N   . THR   A 1 188 ? -0.83143  17.86222 41.03433 1.000 45.41694  ? 195 THR   A N   1 
ATOM   1385 C CA  . THR   A 1 188 ? -2.13257  17.48597 40.49293 1.000 44.95631  ? 195 THR   A CA  1 
ATOM   1386 C C   . THR   A 1 188 ? -3.29089  18.25849 41.10991 1.000 45.48102  ? 195 THR   A C   1 
ATOM   1387 O O   . THR   A 1 188 ? -4.42590  18.10999 40.64555 1.000 42.67289  ? 195 THR   A O   1 
ATOM   1388 C CB  . THR   A 1 188 ? -2.37233  15.98909 40.68399 1.000 44.59159  ? 195 THR   A CB  1 
ATOM   1389 O OG1 . THR   A 1 188 ? -2.40003  15.68807 42.08416 1.000 52.30230  ? 195 THR   A OG1 1 
ATOM   1390 C CG2 . THR   A 1 188 ? -1.26607  15.18921 40.01480 1.000 47.83985  ? 195 THR   A CG2 1 
ATOM   1391 N N   . GLU   A 1 189 ? -3.04237  19.07507 42.13507 1.000 45.19128  ? 196 GLU   A N   1 
ATOM   1392 C CA  . GLU   A 1 189 ? -4.11373  19.88751 42.69703 1.000 46.38632  ? 196 GLU   A CA  1 
ATOM   1393 C C   . GLU   A 1 189 ? -4.66657  20.87790 41.68404 1.000 44.07940  ? 196 GLU   A C   1 
ATOM   1394 O O   . GLU   A 1 189 ? -5.80301  21.33769 41.83539 1.000 51.39209  ? 196 GLU   A O   1 
ATOM   1395 C CB  . GLU   A 1 189 ? -3.61646  20.63713 43.93074 1.000 45.50531  ? 196 GLU   A CB  1 
ATOM   1396 C CG  . GLU   A 1 189 ? -2.89586  21.93572 43.60890 1.000 42.70495  ? 196 GLU   A CG  1 
ATOM   1397 C CD  . GLU   A 1 189 ? -1.98763  22.38181 44.73096 1.000 58.30637  ? 196 GLU   A CD  1 
ATOM   1398 O OE1 . GLU   A 1 189 ? -1.00271  21.66955 45.01091 1.000 67.21329  ? 196 GLU   A OE1 1 
ATOM   1399 O OE2 . GLU   A 1 189 ? -2.26624  23.43549 45.34235 1.000 58.44903  ? 196 GLU   A OE2 1 
ATOM   1400 N N   . TYR   A 1 190 ? -3.89505  21.21376 40.65677 1.000 36.82690  ? 197 TYR   A N   1 
ATOM   1401 C CA  . TYR   A 1 190 ? -4.34359  22.13896 39.63031 1.000 42.99852  ? 197 TYR   A CA  1 
ATOM   1402 C C   . TYR   A 1 190 ? -5.20865  21.46493 38.57917 1.000 47.49953  ? 197 TYR   A C   1 
ATOM   1403 O O   . TYR   A 1 190 ? -5.56437  22.10019 37.58049 1.000 42.49383  ? 197 TYR   A O   1 
ATOM   1404 C CB  . TYR   A 1 190 ? -3.13201  22.82599 38.99774 1.000 44.78618  ? 197 TYR   A CB  1 
ATOM   1405 C CG  . TYR   A 1 190 ? -2.28896  23.51840 40.04098 1.000 46.88124  ? 197 TYR   A CG  1 
ATOM   1406 C CD1 . TYR   A 1 190 ? -2.74977  24.66561 40.67418 1.000 45.01855  ? 197 TYR   A CD1 1 
ATOM   1407 C CD2 . TYR   A 1 190 ? -1.05338  23.01048 40.42057 1.000 41.27736  ? 197 TYR   A CD2 1 
ATOM   1408 C CE1 . TYR   A 1 190 ? -1.99924  25.29895 41.64462 1.000 42.17540  ? 197 TYR   A CE1 1 
ATOM   1409 C CE2 . TYR   A 1 190 ? -0.29438  23.63817 41.39106 1.000 43.81205  ? 197 TYR   A CE2 1 
ATOM   1410 C CZ  . TYR   A 1 190 ? -0.77420  24.78330 41.99808 1.000 44.87000  ? 197 TYR   A CZ  1 
ATOM   1411 O OH  . TYR   A 1 190 ? -0.03192  25.41886 42.96286 1.000 44.90044  ? 197 TYR   A OH  1 
ATOM   1412 N N   . LEU   A 1 191 ? -5.55573  20.19848 38.79086 1.000 44.15297  ? 198 LEU   A N   1 
ATOM   1413 C CA  . LEU   A 1 191 ? -6.57105  19.51816 38.00430 1.000 45.56331  ? 198 LEU   A CA  1 
ATOM   1414 C C   . LEU   A 1 191 ? -7.93110  19.52997 38.68690 1.000 46.62374  ? 198 LEU   A C   1 
ATOM   1415 O O   . LEU   A 1 191 ? -8.91617  19.08794 38.08882 1.000 50.42529  ? 198 LEU   A O   1 
ATOM   1416 C CB  . LEU   A 1 191 ? -6.13948  18.07527 37.72574 1.000 41.81992  ? 198 LEU   A CB  1 
ATOM   1417 C CG  . LEU   A 1 191 ? -4.80852  17.94750 36.98313 1.000 45.53097  ? 198 LEU   A CG  1 
ATOM   1418 C CD1 . LEU   A 1 191 ? -4.39453  16.49440 36.85214 1.000 48.57875  ? 198 LEU   A CD1 1 
ATOM   1419 C CD2 . LEU   A 1 191 ? -4.90685  18.60723 35.61948 1.000 43.72257  ? 198 LEU   A CD2 1 
ATOM   1420 N N   . GLU   A 1 192 ? -8.00907  20.03406 39.91568 1.000 41.89463  ? 199 GLU   A N   1 
ATOM   1421 C CA  . GLU   A 1 192 ? -9.24231  20.01559 40.68778 1.000 45.84359  ? 199 GLU   A CA  1 
ATOM   1422 C C   . GLU   A 1 192 ? -10.09607 21.23483 40.36981 1.000 51.76874  ? 199 GLU   A C   1 
ATOM   1423 O O   . GLU   A 1 192 ? -9.58052  22.34268 40.19275 1.000 44.13613  ? 199 GLU   A O   1 
ATOM   1424 C CB  . GLU   A 1 192 ? -8.93827  19.96700 42.18480 1.000 48.27986  ? 199 GLU   A CB  1 
ATOM   1425 C CG  . GLU   A 1 192 ? -8.09335  18.77729 42.58655 1.000 59.44613  ? 199 GLU   A CG  1 
ATOM   1426 C CD  . GLU   A 1 192 ? -8.92081  17.52756 42.80619 1.000 69.97849  ? 199 GLU   A CD  1 
ATOM   1427 O OE1 . GLU   A 1 192 ? -10.14320 17.65110 43.03863 1.000 76.95153  ? 199 GLU   A OE1 1 
ATOM   1428 O OE2 . GLU   A 1 192 ? -8.34934  16.41971 42.73304 1.000 86.44397  ? 199 GLU   A OE2 1 
ATOM   1429 N N   . GLU   A 1 193 ? -11.41260 21.01833 40.31561 1.000 48.64969  ? 200 GLU   A N   1 
ATOM   1430 C CA  . GLU   A 1 193 ? -12.33785 22.07427 39.91533 1.000 50.32690  ? 200 GLU   A CA  1 
ATOM   1431 C C   . GLU   A 1 193 ? -12.32736 23.23346 40.90502 1.000 54.03627  ? 200 GLU   A C   1 
ATOM   1432 O O   . GLU   A 1 193 ? -12.19539 24.39667 40.50925 1.000 37.17693  ? 200 GLU   A O   1 
ATOM   1433 C CB  . GLU   A 1 193 ? -13.74672 21.50078 39.77754 1.000 53.19113  ? 200 GLU   A CB  1 
ATOM   1434 C CG  . GLU   A 1 193 ? -14.81129 22.52219 39.42326 1.000 57.25061  ? 200 GLU   A CG  1 
ATOM   1435 C CD  . GLU   A 1 193 ? -16.20902 21.92585 39.43093 1.000 77.73074  ? 200 GLU   A CD  1 
ATOM   1436 O OE1 . GLU   A 1 193 ? -16.37407 20.79835 39.94993 1.000 69.97600  ? 200 GLU   A OE1 1 
ATOM   1437 O OE2 . GLU   A 1 193 ? -17.14214 22.58480 38.92270 1.000 73.08591  ? 200 GLU   A OE2 1 
ATOM   1438 N N   . ARG   A 1 194 ? -12.47657 22.93925 42.19927 1.000 51.31231  ? 201 ARG   A N   1 
ATOM   1439 C CA  . ARG   A 1 194 ? -12.54185 24.01058 43.18500 1.000 53.93811  ? 201 ARG   A CA  1 
ATOM   1440 C C   . ARG   A 1 194 ? -11.20704 24.72066 43.35262 1.000 51.22607  ? 201 ARG   A C   1 
ATOM   1441 O O   . ARG   A 1 194 ? -11.18638 25.87902 43.78090 1.000 48.24089  ? 201 ARG   A O   1 
ATOM   1442 C CB  . ARG   A 1 194 ? -13.02779 23.46843 44.53066 1.000 46.72450  ? 201 ARG   A CB  1 
ATOM   1443 C CG  . ARG   A 1 194 ? -12.07468 22.50666 45.20220 1.000 64.47741  ? 201 ARG   A CG  1 
ATOM   1444 C CD  . ARG   A 1 194 ? -12.70415 21.91102 46.44973 1.000 69.23066  ? 201 ARG   A CD  1 
ATOM   1445 N NE  . ARG   A 1 194 ? -11.79949 20.99258 47.13070 1.000 83.78332  ? 201 ARG   A NE  1 
ATOM   1446 C CZ  . ARG   A 1 194 ? -12.09439 20.34205 48.24803 1.000 86.02869  ? 201 ARG   A CZ  1 
ATOM   1447 N NH1 . ARG   A 1 194 ? -13.26540 20.49077 48.84575 1.000 85.99128  ? 201 ARG   A NH1 1 
ATOM   1448 N NH2 . ARG   A 1 194 ? -11.19017 19.52515 48.78174 1.000 91.32275  ? 201 ARG   A NH2 1 
ATOM   1449 N N   . ARG   A 1 195 ? -10.09772 24.06129 43.01548 1.000 51.07693  ? 202 ARG   A N   1 
ATOM   1450 C CA  . ARG   A 1 195 ? -8.80144  24.72523 43.08179 1.000 44.15826  ? 202 ARG   A CA  1 
ATOM   1451 C C   . ARG   A 1 195 ? -8.63113  25.71037 41.93194 1.000 45.38777  ? 202 ARG   A C   1 
ATOM   1452 O O   . ARG   A 1 195 ? -8.18635  26.84488 42.14010 1.000 43.88013  ? 202 ARG   A O   1 
ATOM   1453 C CB  . ARG   A 1 195 ? -7.68152  23.68608 43.07576 1.000 41.85209  ? 202 ARG   A CB  1 
ATOM   1454 C CG  . ARG   A 1 195 ? -6.29235  24.27283 43.23087 1.000 40.98982  ? 202 ARG   A CG  1 
ATOM   1455 C CD  . ARG   A 1 195 ? -6.08507  24.83776 44.63224 1.000 48.56184  ? 202 ARG   A CD  1 
ATOM   1456 N NE  . ARG   A 1 195 ? -4.69667  25.22626 44.85264 1.000 50.28443  ? 202 ARG   A NE  1 
ATOM   1457 C CZ  . ARG   A 1 195 ? -4.27880  26.47699 45.00004 1.000 46.71974  ? 202 ARG   A CZ  1 
ATOM   1458 N NH1 . ARG   A 1 195 ? -5.12225  27.49664 44.97784 1.000 45.21617  ? 202 ARG   A NH1 1 
ATOM   1459 N NH2 . ARG   A 1 195 ? -2.97990  26.71182 45.16294 1.000 42.48798  ? 202 ARG   A NH2 1 
ATOM   1460 N N   . ILE   A 1 196 ? -8.98423  25.29900 40.71144 1.000 41.62654  ? 203 ILE   A N   1 
ATOM   1461 C CA  . ILE   A 1 196 ? -8.88391  26.20460 39.57076 1.000 45.28727  ? 203 ILE   A CA  1 
ATOM   1462 C C   . ILE   A 1 196 ? -9.80158  27.40552 39.76446 1.000 44.15746  ? 203 ILE   A C   1 
ATOM   1463 O O   . ILE   A 1 196 ? -9.42388  28.54683 39.47128 1.000 46.17287  ? 203 ILE   A O   1 
ATOM   1464 C CB  . ILE   A 1 196 ? -9.19427  25.45628 38.26039 1.000 41.21622  ? 203 ILE   A CB  1 
ATOM   1465 C CG1 . ILE   A 1 196 ? -8.09146  24.44576 37.94291 1.000 37.26595  ? 203 ILE   A CG1 1 
ATOM   1466 C CG2 . ILE   A 1 196 ? -9.34436  26.43278 37.10673 1.000 34.84963  ? 203 ILE   A CG2 1 
ATOM   1467 C CD1 . ILE   A 1 196 ? -8.55537  23.30485 37.06286 1.000 47.67864  ? 203 ILE   A CD1 1 
ATOM   1468 N N   . LYS   A 1 197 ? -11.01433 27.17053 40.27476 1.000 40.39790  ? 204 LYS   A N   1 
ATOM   1469 C CA  . LYS   A 1 197 ? -11.95422 28.26475 40.50633 1.000 47.04343  ? 204 LYS   A CA  1 
ATOM   1470 C C   . LYS   A 1 197 ? -11.38099 29.28460 41.48174 1.000 45.16809  ? 204 LYS   A C   1 
ATOM   1471 O O   . LYS   A 1 197 ? -11.44005 30.49628 41.24013 1.000 42.16109  ? 204 LYS   A O   1 
ATOM   1472 C CB  . LYS   A 1 197 ? -13.27905 27.71527 41.03285 1.000 42.42723  ? 204 LYS   A CB  1 
ATOM   1473 C CG  . LYS   A 1 197 ? -14.32464 27.46212 39.96298 1.000 54.68997  ? 204 LYS   A CG  1 
ATOM   1474 C CD  . LYS   A 1 197 ? -15.15940 26.23384 40.29698 1.000 59.38597  ? 204 LYS   A CD  1 
ATOM   1475 C CE  . LYS   A 1 197 ? -16.63921 26.48033 40.04030 1.000 59.22982  ? 204 LYS   A CE  1 
ATOM   1476 N NZ  . LYS   A 1 197 ? -17.50447 25.71224 40.98066 1.000 64.45209  ? 204 LYS   A NZ  1 
ATOM   1477 N N   . GLU   A 1 198 ? -10.82036 28.80718 42.59501 1.000 39.84088  ? 205 GLU   A N   1 
ATOM   1478 C CA  . GLU   A 1 198 ? -10.25431 29.71093 43.59168 1.000 40.56950  ? 205 GLU   A CA  1 
ATOM   1479 C C   . GLU   A 1 198 ? -9.10898  30.53232 43.00975 1.000 42.46416  ? 205 GLU   A C   1 
ATOM   1480 O O   . GLU   A 1 198 ? -8.95899  31.71782 43.32984 1.000 44.22868  ? 205 GLU   A O   1 
ATOM   1481 C CB  . GLU   A 1 198 ? -9.78802  28.90812 44.80777 1.000 44.46731  ? 205 GLU   A CB  1 
ATOM   1482 C CG  . GLU   A 1 198 ? -8.92245  29.68025 45.79105 1.000 54.28585  ? 205 GLU   A CG  1 
ATOM   1483 C CD  . GLU   A 1 198 ? -8.21579  28.77035 46.78209 1.000 65.65001  ? 205 GLU   A CD  1 
ATOM   1484 O OE1 . GLU   A 1 198 ? -7.62540  27.76133 46.33920 1.000 60.25469  ? 205 GLU   A OE1 1 
ATOM   1485 O OE2 . GLU   A 1 198 ? -8.25082  29.06338 47.99915 1.000 53.57621  ? 205 GLU   A OE2 1 
ATOM   1486 N N   . ILE   A 1 199 ? -8.29305  29.92352 42.14752 1.000 44.80113  ? 206 ILE   A N   1 
ATOM   1487 C CA  . ILE   A 1 199 ? -7.18630  30.65731 41.54399 1.000 42.02025  ? 206 ILE   A CA  1 
ATOM   1488 C C   . ILE   A 1 199 ? -7.71194  31.72186 40.59067 1.000 48.10644  ? 206 ILE   A C   1 
ATOM   1489 O O   . ILE   A 1 199 ? -7.24760  32.86854 40.60229 1.000 44.86468  ? 206 ILE   A O   1 
ATOM   1490 C CB  . ILE   A 1 199 ? -6.22127  29.68836 40.83533 1.000 45.54760  ? 206 ILE   A CB  1 
ATOM   1491 C CG1 . ILE   A 1 199 ? -5.61007  28.70760 41.83638 1.000 48.12349  ? 206 ILE   A CG1 1 
ATOM   1492 C CG2 . ILE   A 1 199 ? -5.11855  30.45600 40.12634 1.000 41.47325  ? 206 ILE   A CG2 1 
ATOM   1493 C CD1 . ILE   A 1 199 ? -4.84075  27.58204 41.18415 1.000 45.76392  ? 206 ILE   A CD1 1 
ATOM   1494 N N   . VAL   A 1 200 ? -8.69519  31.36386 39.76052 1.000 42.30299  ? 207 VAL   A N   1 
ATOM   1495 C CA  . VAL   A 1 200 ? -9.20583  32.28889 38.75402 1.000 43.91815  ? 207 VAL   A CA  1 
ATOM   1496 C C   . VAL   A 1 200 ? -9.89655  33.47855 39.41362 1.000 51.66178  ? 207 VAL   A C   1 
ATOM   1497 O O   . VAL   A 1 200 ? -9.71365  34.62838 38.99590 1.000 44.94034  ? 207 VAL   A O   1 
ATOM   1498 C CB  . VAL   A 1 200 ? -10.14185 31.54350 37.78475 1.000 41.44286  ? 207 VAL   A CB  1 
ATOM   1499 C CG1 . VAL   A 1 200 ? -10.92909 32.52358 36.93570 1.000 46.29599  ? 207 VAL   A CG1 1 
ATOM   1500 C CG2 . VAL   A 1 200 ? -9.33813  30.59932 36.90178 1.000 37.57434  ? 207 VAL   A CG2 1 
ATOM   1501 N N   . LYS   A 1 201 ? -10.68646 33.22619 40.46034 1.000 41.86176  ? 208 LYS   A N   1 
ATOM   1502 C CA  . LYS   A 1 201 ? -11.37073 34.31128 41.15623 1.000 43.03579  ? 208 LYS   A CA  1 
ATOM   1503 C C   . LYS   A 1 201 ? -10.37928 35.25286 41.83456 1.000 60.35708  ? 208 LYS   A C   1 
ATOM   1504 O O   . LYS   A 1 201 ? -10.58053 36.47316 41.84849 1.000 52.68352  ? 208 LYS   A O   1 
ATOM   1505 C CB  . LYS   A 1 201 ? -12.35241 33.73217 42.17721 1.000 46.20767  ? 208 LYS   A CB  1 
ATOM   1506 C CG  . LYS   A 1 201 ? -12.97158 34.75941 43.11413 1.000 57.35499  ? 208 LYS   A CG  1 
ATOM   1507 C CD  . LYS   A 1 201 ? -13.61330 34.09241 44.32121 1.000 65.38020  ? 208 LYS   A CD  1 
ATOM   1508 C CE  . LYS   A 1 201 ? -14.91769 33.40248 43.95167 1.000 76.28887  ? 208 LYS   A CE  1 
ATOM   1509 N NZ  . LYS   A 1 201 ? -16.10031 34.09105 44.54664 1.000 78.84079  ? 208 LYS   A NZ  1 
ATOM   1510 N N   . LYS   A 1 202 ? -9.30017  34.70803 42.39694 1.000 55.03432  ? 209 LYS   A N   1 
ATOM   1511 C CA  . LYS   A 1 202 ? -8.34620  35.53411 43.12852 1.000 57.02750  ? 209 LYS   A CA  1 
ATOM   1512 C C   . LYS   A 1 202 ? -7.44561  36.32725 42.18789 1.000 61.11307  ? 209 LYS   A C   1 
ATOM   1513 O O   . LYS   A 1 202 ? -7.12392  37.48760 42.46522 1.000 66.31360  ? 209 LYS   A O   1 
ATOM   1514 C CB  . LYS   A 1 202 ? -7.50621  34.65761 44.06420 1.000 61.86269  ? 209 LYS   A CB  1 
ATOM   1515 C CG  . LYS   A 1 202 ? -6.14030  35.23567 44.42322 1.000 59.68835  ? 209 LYS   A CG  1 
ATOM   1516 C CD  . LYS   A 1 202 ? -5.83833  35.09568 45.90747 1.000 64.27983  ? 209 LYS   A CD  1 
ATOM   1517 C CE  . LYS   A 1 202 ? -5.90206  33.64620 46.35992 1.000 74.13531  ? 209 LYS   A CE  1 
ATOM   1518 N NZ  . LYS   A 1 202 ? -4.72166  32.86361 45.90085 1.000 77.51334  ? 209 LYS   A NZ  1 
ATOM   1519 N N   . HIS   A 1 203 ? -7.04169  35.73118 41.06566 1.000 62.03370  ? 210 HIS   A N   1 
ATOM   1520 C CA  . HIS   A 1 203 ? -6.02947  36.33166 40.20995 1.000 60.64835  ? 210 HIS   A CA  1 
ATOM   1521 C C   . HIS   A 1 203 ? -6.56535  36.90407 38.90439 1.000 59.87987  ? 210 HIS   A C   1 
ATOM   1522 O O   . HIS   A 1 203 ? -5.91380  37.77937 38.32655 1.000 64.65556  ? 210 HIS   A O   1 
ATOM   1523 C CB  . HIS   A 1 203 ? -4.93770  35.30012 39.88105 1.000 60.14570  ? 210 HIS   A CB  1 
ATOM   1524 C CG  . HIS   A 1 203 ? -4.00348  35.01771 41.01828 1.000 61.43147  ? 210 HIS   A CG  1 
ATOM   1525 N ND1 . HIS   A 1 203 ? -3.19064  35.98271 41.57406 1.000 69.75912  ? 210 HIS   A ND1 1 
ATOM   1526 C CD2 . HIS   A 1 203 ? -3.75211  33.87545 41.70227 1.000 56.58429  ? 210 HIS   A CD2 1 
ATOM   1527 C CE1 . HIS   A 1 203 ? -2.48033  35.44778 42.55159 1.000 64.82267  ? 210 HIS   A CE1 1 
ATOM   1528 N NE2 . HIS   A 1 203 ? -2.80205  34.17018 42.65006 1.000 53.50496  ? 210 HIS   A NE2 1 
ATOM   1529 N N   . SER   A 1 204 ? -7.72125  36.44677 38.42551 1.000 56.64912  ? 211 SER   A N   1 
ATOM   1530 C CA  . SER   A 1 204 ? -8.17486  36.79307 37.08078 1.000 64.71732  ? 211 SER   A CA  1 
ATOM   1531 C C   . SER   A 1 204 ? -9.65383  37.15832 37.07682 1.000 61.46838  ? 211 SER   A C   1 
ATOM   1532 O O   . SER   A 1 204 ? -10.37089 36.90670 36.10248 1.000 56.69376  ? 211 SER   A O   1 
ATOM   1533 C CB  . SER   A 1 204 ? -7.90362  35.64958 36.10375 1.000 60.35671  ? 211 SER   A CB  1 
ATOM   1534 O OG  . SER   A 1 204 ? -6.53195  35.29568 36.10857 1.000 59.83609  ? 211 SER   A OG  1 
ATOM   1535 N N   . GLN   A 1 205 ? -10.13035 37.77440 38.15945 1.000 65.29997  ? 212 GLN   A N   1 
ATOM   1536 C CA  . GLN   A 1 205 ? -11.53156 38.17046 38.22898 1.000 68.68030  ? 212 GLN   A CA  1 
ATOM   1537 C C   . GLN   A 1 205 ? -11.86134 39.35082 37.32040 1.000 69.98951  ? 212 GLN   A C   1 
ATOM   1538 O O   . GLN   A 1 205 ? -13.03933 39.70391 37.20151 1.000 81.97843  ? 212 GLN   A O   1 
ATOM   1539 C CB  . GLN   A 1 205 ? -11.90763 38.50403 39.67659 1.000 62.04093  ? 212 GLN   A CB  1 
ATOM   1540 C CG  . GLN   A 1 205 ? -11.23140 39.75278 40.22320 1.000 72.05398  ? 212 GLN   A CG  1 
ATOM   1541 C CD  . GLN   A 1 205 ? -9.96906  39.45313 41.01527 1.000 79.85776  ? 212 GLN   A CD  1 
ATOM   1542 O OE1 . GLN   A 1 205 ? -9.00019  38.90701 40.48247 1.000 70.08619  ? 212 GLN   A OE1 1 
ATOM   1543 N NE2 . GLN   A 1 205 ? -9.96834  39.82757 42.29092 1.000 74.73784  ? 212 GLN   A NE2 1 
ATOM   1544 N N   . PHE   A 1 206 ? -10.86338 39.95936 36.67120 1.000 81.56425  ? 213 PHE   A N   1 
ATOM   1545 C CA  . PHE   A 1 206 ? -11.06751 41.15168 35.85348 1.000 68.13839  ? 213 PHE   A CA  1 
ATOM   1546 C C   . PHE   A 1 206 ? -10.52697 40.96590 34.43849 1.000 74.54102  ? 213 PHE   A C   1 
ATOM   1547 O O   . PHE   A 1 206 ? -10.01334 41.91071 33.83131 1.000 64.66654  ? 213 PHE   A O   1 
ATOM   1548 C CB  . PHE   A 1 206 ? -10.43224 42.37370 36.51292 1.000 66.88391  ? 213 PHE   A CB  1 
ATOM   1549 C CG  . PHE   A 1 206 ? -10.97198 42.66945 37.88229 1.000 67.72727  ? 213 PHE   A CG  1 
ATOM   1550 C CD1 . PHE   A 1 206 ? -12.33819 42.69498 38.11261 1.000 71.73292  ? 213 PHE   A CD1 1 
ATOM   1551 C CD2 . PHE   A 1 206 ? -10.11564 42.91802 38.94062 1.000 72.57850  ? 213 PHE   A CD2 1 
ATOM   1552 C CE1 . PHE   A 1 206 ? -12.83985 42.96727 39.37502 1.000 72.24676  ? 213 PHE   A CE1 1 
ATOM   1553 C CE2 . PHE   A 1 206 ? -10.61214 43.18913 40.20277 1.000 72.37726  ? 213 PHE   A CE2 1 
ATOM   1554 C CZ  . PHE   A 1 206 ? -11.97388 43.21574 40.42020 1.000 62.94705  ? 213 PHE   A CZ  1 
ATOM   1555 N N   . ILE   A 1 207 ? -10.63997 39.75628 33.90147 1.000 70.51027  ? 214 ILE   A N   1 
ATOM   1556 C CA  . ILE   A 1 207 ? -10.25987 39.48465 32.51979 1.000 55.80369  ? 214 ILE   A CA  1 
ATOM   1557 C C   . ILE   A 1 207 ? -11.43927 39.82317 31.61738 1.000 51.45255  ? 214 ILE   A C   1 
ATOM   1558 O O   . ILE   A 1 207 ? -12.58628 39.46980 31.91609 1.000 57.50315  ? 214 ILE   A O   1 
ATOM   1559 C CB  . ILE   A 1 207 ? -9.82376  38.01810 32.35953 1.000 50.88865  ? 214 ILE   A CB  1 
ATOM   1560 C CG1 . ILE   A 1 207 ? -8.50483  37.77998 33.09606 1.000 47.90206  ? 214 ILE   A CG1 1 
ATOM   1561 C CG2 . ILE   A 1 207 ? -9.69532  37.63759 30.89946 1.000 39.43761  ? 214 ILE   A CG2 1 
ATOM   1562 C CD1 . ILE   A 1 207 ? -7.34561  38.57485 32.53821 1.000 43.29298  ? 214 ILE   A CD1 1 
ATOM   1563 N N   . GLY   A 1 208 ? -11.16476 40.51989 30.51686 1.000 48.28952  ? 215 GLY   A N   1 
ATOM   1564 C CA  . GLY   A 1 208 ? -12.22068 41.00652 29.64846 1.000 49.05082  ? 215 GLY   A CA  1 
ATOM   1565 C C   . GLY   A 1 208 ? -12.72321 40.01513 28.61742 1.000 46.69330  ? 215 GLY   A C   1 
ATOM   1566 O O   . GLY   A 1 208 ? -13.19542 40.41517 27.54772 1.000 46.10039  ? 215 GLY   A O   1 
ATOM   1567 N N   . TYR   A 1 209 ? -12.63141 38.72205 28.92002 1.000 42.18773  ? 216 TYR   A N   1 
ATOM   1568 C CA  . TYR   A 1 209 ? -13.12589 37.67656 28.03415 1.000 40.93273  ? 216 TYR   A CA  1 
ATOM   1569 C C   . TYR   A 1 209 ? -13.66468 36.54208 28.88922 1.000 36.66025  ? 216 TYR   A C   1 
ATOM   1570 O O   . TYR   A 1 209 ? -13.21648 36.36331 30.02882 1.000 39.83616  ? 216 TYR   A O   1 
ATOM   1571 C CB  . TYR   A 1 209 ? -12.02660 37.16873 27.08444 1.000 38.06001  ? 216 TYR   A CB  1 
ATOM   1572 C CG  . TYR   A 1 209 ? -11.46986 38.26300 26.19730 1.000 44.76946  ? 216 TYR   A CG  1 
ATOM   1573 C CD1 . TYR   A 1 209 ? -12.12280 38.63839 25.03291 1.000 41.85986  ? 216 TYR   A CD1 1 
ATOM   1574 C CD2 . TYR   A 1 209 ? -10.30908 38.94347 26.54510 1.000 43.55187  ? 216 TYR   A CD2 1 
ATOM   1575 C CE1 . TYR   A 1 209 ? -11.62903 39.64963 24.23105 1.000 42.85494  ? 216 TYR   A CE1 1 
ATOM   1576 C CE2 . TYR   A 1 209 ? -9.80697  39.95686 25.74862 1.000 42.66530  ? 216 TYR   A CE2 1 
ATOM   1577 C CZ  . TYR   A 1 209 ? -10.47060 40.30504 24.59444 1.000 42.67735  ? 216 TYR   A CZ  1 
ATOM   1578 O OH  . TYR   A 1 209 ? -9.97415  41.31235 23.80075 1.000 41.94293  ? 216 TYR   A OH  1 
ATOM   1579 N N   . PRO   A 1 210 ? -14.63542 35.77629 28.38759 1.000 40.48166  ? 217 PRO   A N   1 
ATOM   1580 C CA  . PRO   A 1 210 ? -15.20162 34.68675 29.19613 1.000 38.47764  ? 217 PRO   A CA  1 
ATOM   1581 C C   . PRO   A 1 210 ? -14.17752 33.58304 29.41769 1.000 35.11365  ? 217 PRO   A C   1 
ATOM   1582 O O   . PRO   A 1 210 ? -13.55786 33.09158 28.47237 1.000 35.66338  ? 217 PRO   A O   1 
ATOM   1583 C CB  . PRO   A 1 210 ? -16.39612 34.19170 28.36976 1.000 36.56777  ? 217 PRO   A CB  1 
ATOM   1584 C CG  . PRO   A 1 210 ? -16.28673 34.82310 27.03614 1.000 37.21063  ? 217 PRO   A CG  1 
ATOM   1585 C CD  . PRO   A 1 210 ? -15.30479 35.94126 27.08488 1.000 41.55856  ? 217 PRO   A CD  1 
ATOM   1586 N N   . ILE   A 1 211 ? -13.99646 33.20821 30.68070 1.000 36.05927  ? 218 ILE   A N   1 
ATOM   1587 C CA  . ILE   A 1 211 ? -13.11796 32.11312 31.07286 1.000 35.98892  ? 218 ILE   A CA  1 
ATOM   1588 C C   . ILE   A 1 211 ? -14.01156 30.95766 31.50506 1.000 42.67617  ? 218 ILE   A C   1 
ATOM   1589 O O   . ILE   A 1 211 ? -14.69223 31.03725 32.53573 1.000 45.16280  ? 218 ILE   A O   1 
ATOM   1590 C CB  . ILE   A 1 211 ? -12.15421 32.52417 32.19408 1.000 37.23234  ? 218 ILE   A CB  1 
ATOM   1591 C CG1 . ILE   A 1 211 ? -11.45097 33.83718 31.84137 1.000 45.28164  ? 218 ILE   A CG1 1 
ATOM   1592 C CG2 . ILE   A 1 211 ? -11.13252 31.42697 32.44504 1.000 37.30086  ? 218 ILE   A CG2 1 
ATOM   1593 C CD1 . ILE   A 1 211 ? -10.54907 34.35991 32.94053 1.000 39.08321  ? 218 ILE   A CD1 1 
ATOM   1594 N N   . THR   A 1 212 ? -14.01501 29.88455 30.72014 1.000 38.43049  ? 219 THR   A N   1 
ATOM   1595 C CA  . THR   A 1 212 ? -14.88574 28.73783 30.94649 1.000 41.82428  ? 219 THR   A CA  1 
ATOM   1596 C C   . THR   A 1 212 ? -14.07644 27.56262 31.47452 1.000 38.19400  ? 219 THR   A C   1 
ATOM   1597 O O   . THR   A 1 212 ? -13.11487 27.12973 30.83245 1.000 36.00429  ? 219 THR   A O   1 
ATOM   1598 C CB  . THR   A 1 212 ? -15.59783 28.33308 29.65457 1.000 42.65402  ? 219 THR   A CB  1 
ATOM   1599 O OG1 . THR   A 1 212 ? -16.36425 29.43964 29.16387 1.000 39.86308  ? 219 THR   A OG1 1 
ATOM   1600 C CG2 . THR   A 1 212 ? -16.51546 27.14949 29.90123 1.000 40.12412  ? 219 THR   A CG2 1 
ATOM   1601 N N   . LEU   A 1 213 ? -14.47237 27.04321 32.63272 1.000 38.79795  ? 220 LEU   A N   1 
ATOM   1602 C CA  . LEU   A 1 213 ? -13.83565 25.86602 33.21012 1.000 43.93420  ? 220 LEU   A CA  1 
ATOM   1603 C C   . LEU   A 1 213 ? -14.57517 24.61463 32.74809 1.000 39.96096  ? 220 LEU   A C   1 
ATOM   1604 O O   . LEU   A 1 213 ? -15.75609 24.43325 33.06498 1.000 43.75578  ? 220 LEU   A O   1 
ATOM   1605 C CB  . LEU   A 1 213 ? -13.82222 25.94758 34.73566 1.000 40.63608  ? 220 LEU   A CB  1 
ATOM   1606 C CG  . LEU   A 1 213 ? -13.23287 24.73827 35.46863 1.000 56.17125  ? 220 LEU   A CG  1 
ATOM   1607 C CD1 . LEU   A 1 213 ? -11.87946 24.33942 34.88396 1.000 41.44707  ? 220 LEU   A CD1 1 
ATOM   1608 C CD2 . LEU   A 1 213 ? -13.12029 25.01724 36.96120 1.000 52.67940  ? 220 LEU   A CD2 1 
ATOM   1609 N N   . PHE   A 1 214 ? -13.88194 23.75678 32.00151 1.000 38.95092  ? 221 PHE   A N   1 
ATOM   1610 C CA  . PHE   A 1 214 ? -14.44468 22.48319 31.56136 1.000 43.46045  ? 221 PHE   A CA  1 
ATOM   1611 C C   . PHE   A 1 214 ? -14.28900 21.47117 32.68951 1.000 50.37267  ? 221 PHE   A C   1 
ATOM   1612 O O   . PHE   A 1 214 ? -13.16893 21.07194 33.02545 1.000 50.18673  ? 221 PHE   A O   1 
ATOM   1613 C CB  . PHE   A 1 214 ? -13.74687 21.98289 30.30038 1.000 39.03387  ? 221 PHE   A CB  1 
ATOM   1614 C CG  . PHE   A 1 214 ? -14.18847 22.66622 29.03795 1.000 41.93351  ? 221 PHE   A CG  1 
ATOM   1615 C CD1 . PHE   A 1 214 ? -14.32089 24.04283 28.98241 1.000 47.78220  ? 221 PHE   A CD1 1 
ATOM   1616 C CD2 . PHE   A 1 214 ? -14.45568 21.92869 27.89896 1.000 44.80443  ? 221 PHE   A CD2 1 
ATOM   1617 C CE1 . PHE   A 1 214 ? -14.71727 24.66753 27.81845 1.000 46.20236  ? 221 PHE   A CE1 1 
ATOM   1618 C CE2 . PHE   A 1 214 ? -14.85085 22.54877 26.73176 1.000 47.02071  ? 221 PHE   A CE2 1 
ATOM   1619 C CZ  . PHE   A 1 214 ? -14.98193 23.91861 26.69184 1.000 40.52859  ? 221 PHE   A CZ  1 
ATOM   1620 N N   . VAL   A 1 215 ? -15.39114 21.05421 33.27241 1.000 43.64406  ? 222 VAL   A N   1 
ATOM   1621 C CA  . VAL   A 1 215 ? -15.33917 20.06911 34.34335 1.000 52.24947  ? 222 VAL   A CA  1 
ATOM   1622 C C   . VAL   A 1 215 ? -15.41064 18.67644 33.72857 1.000 50.50081  ? 222 VAL   A C   1 
ATOM   1623 O O   . VAL   A 1 215 ? -16.03618 18.46034 32.68422 1.000 47.77448  ? 222 VAL   A O   1 
ATOM   1624 C CB  . VAL   A 1 215 ? -16.45505 20.32420 35.37978 1.000 56.64351  ? 222 VAL   A CB  1 
ATOM   1625 C CG1 . VAL   A 1 215 ? -16.55183 21.80759 35.68877 1.000 55.96459  ? 222 VAL   A CG1 1 
ATOM   1626 C CG2 . VAL   A 1 215 ? -17.76789 19.84975 34.87033 1.000 51.72671  ? 222 VAL   A CG2 1 
ATOM   1627 N N   . GLU   A 1 216 ? -14.72981 17.72546 34.36047 1.000 47.87552  ? 223 GLU   A N   1 
ATOM   1628 C CA  . GLU   A 1 216 ? -14.60221 16.39484 33.79015 1.000 49.21883  ? 223 GLU   A CA  1 
ATOM   1629 C C   . GLU   A 1 216 ? -15.83616 15.54589 34.08479 1.000 51.36523  ? 223 GLU   A C   1 
ATOM   1630 O O   . GLU   A 1 216 ? -16.60019 15.80635 35.01780 1.000 54.82569  ? 223 GLU   A O   1 
ATOM   1631 C CB  . GLU   A 1 216 ? -13.35103 15.70317 34.32452 1.000 51.89280  ? 223 GLU   A CB  1 
ATOM   1632 C CG  . GLU   A 1 216 ? -12.06734 16.43875 34.01105 1.000 51.60269  ? 223 GLU   A CG  1 
ATOM   1633 C CD  . GLU   A 1 216 ? -10.85036 15.54863 34.14249 1.000 61.79778  ? 223 GLU   A CD  1 
ATOM   1634 O OE1 . GLU   A 1 216 ? -10.74445 14.57018 33.37140 1.000 62.23544  ? 223 GLU   A OE1 1 
ATOM   1635 O OE2 . GLU   A 1 216 ? -9.99830  15.82874 35.01268 1.000 61.19251  ? 223 GLU   A OE2 1 
ATOM   1636 N N   . LYS   A 1 217 ? -16.01595 14.50908 33.27280 1.000 55.56212  ? 224 LYS   A N   1 
ATOM   1637 C CA  . LYS   A 1 217 ? -17.17259 13.63104 33.39124 1.000 58.93275  ? 224 LYS   A CA  1 
ATOM   1638 C C   . LYS   A 1 217 ? -16.78036 12.26518 33.94803 1.000 63.77568  ? 224 LYS   A C   1 
ATOM   1639 O O   . LYS   A 1 217 ? -16.39697 12.14132 35.11063 1.000 74.80248  ? 224 LYS   A O   1 
ATOM   1640 C CB  . LYS   A 1 217 ? -17.85520 13.46817 32.03105 1.000 54.52004  ? 224 LYS   A CB  1 
ATOM   1641 C CG  . LYS   A 1 217 ? -18.02547 14.76794 31.25605 1.000 59.74586  ? 224 LYS   A CG  1 
ATOM   1642 C CD  . LYS   A 1 217 ? -18.48435 14.50540 29.82620 1.000 54.57099  ? 224 LYS   A CD  1 
ATOM   1643 C CE  . LYS   A 1 217 ? -17.49820 13.61165 29.08502 1.000 52.25816  ? 224 LYS   A CE  1 
ATOM   1644 N NZ  . LYS   A 1 217 ? -16.25110 14.34721 28.71352 1.000 52.52927  ? 224 LYS   A NZ  1 
HETATM 1645 C C1  . A1AYJ B 2 .   ? 6.54880   35.32088 28.03903 0.860 48.20203  ? 301 A1AYJ A C1  1 
HETATM 1646 C C10 . A1AYJ B 2 .   ? 5.43071   30.64313 23.92583 0.860 39.61641  ? 301 A1AYJ A C10 1 
HETATM 1647 C C2  . A1AYJ B 2 .   ? 7.08221   35.43704 26.63289 0.860 28.17768  ? 301 A1AYJ A C2  1 
HETATM 1648 C C3  . A1AYJ B 2 .   ? 5.79238   34.24204 24.92074 0.860 58.40426  ? 301 A1AYJ A C3  1 
HETATM 1649 C C4  . A1AYJ B 2 .   ? 6.22217   31.78822 24.57123 0.860 45.20044  ? 301 A1AYJ A C4  1 
HETATM 1650 C C5  . A1AYJ B 2 .   ? 7.71771   31.79306 24.22523 0.860 39.99960  ? 301 A1AYJ A C5  1 
HETATM 1651 C C6  . A1AYJ B 2 .   ? 8.01841   31.93085 22.74294 0.860 40.46577  ? 301 A1AYJ A C6  1 
HETATM 1652 C C7  . A1AYJ B 2 .   ? 7.23581   31.01310 21.81502 0.860 44.45557  ? 301 A1AYJ A C7  1 
HETATM 1653 C C8  . A1AYJ B 2 .   ? 7.08149   29.57404 22.28834 0.860 38.84451  ? 301 A1AYJ A C8  1 
HETATM 1654 C C9  . A1AYJ B 2 .   ? 6.28350   29.43273 23.57743 0.860 39.36142  ? 301 A1AYJ A C9  1 
HETATM 1655 N N1  . A1AYJ B 2 .   ? 6.76711   34.27042 25.82380 0.860 48.13652  ? 301 A1AYJ A N1  1 
HETATM 1656 N N2  . A1AYJ B 2 .   ? 5.56887   33.07056 24.28821 0.860 62.61653  ? 301 A1AYJ A N2  1 
HETATM 1657 O O1  . A1AYJ B 2 .   ? 5.14045   35.47898 28.15381 0.860 39.46821  ? 301 A1AYJ A O1  1 
HETATM 1658 S S1  . A1AYJ B 2 .   ? 4.83432   35.59205 24.64221 0.860 77.70679  ? 301 A1AYJ A S1  1 
HETATM 1659 O O   . HOH   C 3 .   ? 10.96245  29.97701 48.08811 1.000 55.71015  ? 401 HOH   A O   1 
HETATM 1660 O O   . HOH   C 3 .   ? 6.72086   46.55084 37.51236 1.000 64.14742  ? 402 HOH   A O   1 
HETATM 1661 O O   . HOH   C 3 .   ? -16.47627 11.37237 37.09429 1.000 61.64051  ? 403 HOH   A O   1 
HETATM 1662 O O   . HOH   C 3 .   ? 11.15826  27.53377 42.33495 1.000 55.73747  ? 404 HOH   A O   1 
HETATM 1663 O O   . HOH   C 3 .   ? 0.36866   38.98674 30.13999 1.000 44.51210  ? 405 HOH   A O   1 
HETATM 1664 O O   . HOH   C 3 .   ? -9.60476  12.60440 33.02384 1.000 48.96802  ? 406 HOH   A O   1 
HETATM 1665 O O   . HOH   C 3 .   ? 7.43801   19.68546 10.48205 1.000 44.51551  ? 407 HOH   A O   1 
HETATM 1666 O O   . HOH   C 3 .   ? -0.83221  19.41088 44.04176 1.000 43.48674  ? 408 HOH   A O   1 
HETATM 1667 O O   . HOH   C 3 .   ? -10.74254 17.45331 36.71884 1.000 52.13464  ? 409 HOH   A O   1 
HETATM 1668 O O   . HOH   C 3 .   ? -5.24790  41.88514 28.13783 1.000 34.81172  ? 410 HOH   A O   1 
HETATM 1669 O O   . HOH   C 3 .   ? -18.03640 24.70232 34.00239 1.000 39.21809  ? 411 HOH   A O   1 
HETATM 1670 O O   . HOH   C 3 .   ? 1.30460   23.82194 44.31419 1.000 50.00826  ? 412 HOH   A O   1 
HETATM 1671 O O   . HOH   C 3 .   ? -15.20282 10.04873 34.42939 1.000 67.43401  ? 413 HOH   A O   1 
HETATM 1672 O O   . HOH   C 3 .   ? -5.68399  18.98338 29.34188 1.000 31.94514  ? 414 HOH   A O   1 
HETATM 1673 O O   . HOH   C 3 .   ? 17.15267  25.38819 31.45360 1.000 41.77581  ? 415 HOH   A O   1 
HETATM 1674 O O   . HOH   C 3 .   ? -4.05544  35.52280 13.49361 1.000 32.80994  ? 416 HOH   A O   1 
HETATM 1675 O O   . HOH   C 3 .   ? -8.69500  41.42632 29.73369 1.000 49.58279  ? 417 HOH   A O   1 
HETATM 1676 O O   . HOH   C 3 .   ? 0.49233   30.03462 12.91709 1.000 39.23474  ? 418 HOH   A O   1 
HETATM 1677 O O   . HOH   C 3 .   ? -15.30809 17.65848 30.30740 1.000 42.15661  ? 419 HOH   A O   1 
HETATM 1678 O O   . HOH   C 3 .   ? 2.89783   24.59732 46.68779 1.000 49.43313  ? 420 HOH   A O   1 
HETATM 1679 O O   . HOH   C 3 .   ? -7.72444  41.94657 35.10533 1.000 61.08252  ? 421 HOH   A O   1 
HETATM 1680 O O   . HOH   C 3 .   ? 13.01910  32.83014 12.86634 1.000 55.18878  ? 422 HOH   A O   1 
HETATM 1681 O O   . HOH   C 3 .   ? -5.92471  31.25944 11.44229 1.000 42.00509  ? 423 HOH   A O   1 
HETATM 1682 O O   . HOH   C 3 .   ? -11.93791 19.22910 31.61676 1.000 45.05482  ? 424 HOH   A O   1 
HETATM 1683 O O   . HOH   C 3 .   ? 6.44206   32.47381 10.30394 1.000 42.36098  ? 425 HOH   A O   1 
HETATM 1684 O O   . HOH   C 3 .   ? 15.21154  17.39483 15.95943 1.000 40.29003  ? 426 HOH   A O   1 
HETATM 1685 O O   . HOH   C 3 .   ? 13.90044  19.39953 23.22144 1.000 36.61530  ? 427 HOH   A O   1 
HETATM 1686 O O   . HOH   C 3 .   ? 1.91755   43.09544 15.05737 1.000 50.19720  ? 428 HOH   A O   1 
HETATM 1687 O O   . HOH   C 3 .   ? -3.53409  12.95590 37.45780 1.000 46.85788  ? 429 HOH   A O   1 
HETATM 1688 O O   . HOH   C 3 .   ? -14.63157 30.64064 27.47516 1.000 37.23964  ? 430 HOH   A O   1 
HETATM 1689 O O   . HOH   C 3 .   ? 8.05679   24.27758 8.86233  1.000 51.53613  ? 431 HOH   A O   1 
HETATM 1690 O O   . HOH   C 3 .   ? 3.91512   19.54574 7.29339  1.000 55.39648  ? 432 HOH   A O   1 
HETATM 1691 O O   . HOH   C 3 .   ? 6.67821   14.36425 38.22116 1.000 53.32127  ? 433 HOH   A O   1 
HETATM 1692 O O   . HOH   C 3 .   ? -14.99164 18.76518 38.81883 1.000 54.14448  ? 434 HOH   A O   1 
HETATM 1693 O O   . HOH   C 3 .   ? 9.68323   24.91532 40.85431 1.000 52.51642  ? 435 HOH   A O   1 
HETATM 1694 O O   . HOH   C 3 .   ? 5.89833   36.62956 12.41355 1.000 51.96926  ? 436 HOH   A O   1 
HETATM 1695 O O   . HOH   C 3 .   ? 15.53734  25.12441 29.26253 1.000 34.19629  ? 437 HOH   A O   1 
HETATM 1696 O O   . HOH   C 3 .   ? 1.68716   36.67066 16.92777 1.000 45.32136  ? 438 HOH   A O   1 
HETATM 1697 O O   . HOH   C 3 .   ? -3.32444  33.17040 20.55042 1.000 24.70960  ? 439 HOH   A O   1 
HETATM 1698 O O   . HOH   C 3 .   ? -6.47895  47.74518 13.61430 1.000 51.89919  ? 440 HOH   A O   1 
HETATM 1699 O O   . HOH   C 3 .   ? 9.71879   17.83680 21.95907 1.000 43.91217  ? 441 HOH   A O   1 
HETATM 1700 O O   . HOH   C 3 .   ? -12.97275 31.64185 17.52864 1.000 44.43858  ? 442 HOH   A O   1 
HETATM 1701 O O   . HOH   C 3 .   ? 13.10335  19.76165 26.25327 1.000 46.83073  ? 443 HOH   A O   1 
HETATM 1702 O O   . HOH   C 3 .   ? 7.24653   20.25736 18.73649 1.000 32.96876  ? 444 HOH   A O   1 
HETATM 1703 O O   . HOH   C 3 .   ? 4.28556   37.85960 30.96317 1.000 40.40621  ? 445 HOH   A O   1 
HETATM 1704 O O   . HOH   C 3 .   ? -14.30652 14.26406 30.76938 1.000 53.31938  ? 446 HOH   A O   1 
HETATM 1705 O O   . HOH   C 3 .   ? -5.71105  44.75830 11.02299 1.000 46.49124  ? 447 HOH   A O   1 
HETATM 1706 O O   . HOH   C 3 .   ? 2.28649   36.78475 31.76162 1.000 39.61354  ? 448 HOH   A O   1 
HETATM 1707 O O   . HOH   C 3 .   ? 18.38078  19.62131 25.74841 1.000 46.68345  ? 449 HOH   A O   1 
HETATM 1708 O O   . HOH   C 3 .   ? -13.67592 31.25798 39.63041 1.000 51.86290  ? 450 HOH   A O   1 
HETATM 1709 O O   . HOH   C 3 .   ? 1.21075   11.11056 33.14703 1.000 62.15260  ? 451 HOH   A O   1 
HETATM 1710 O O   . HOH   C 3 .   ? -2.01210  30.96850 27.48506 1.000 40.36252  ? 452 HOH   A O   1 
HETATM 1711 O O   . HOH   C 3 .   ? 9.60117   23.06266 12.06069 1.000 51.20689  ? 453 HOH   A O   1 
HETATM 1712 O O   . HOH   C 3 .   ? -3.27637  29.68427 25.63338 1.000 35.53665  ? 454 HOH   A O   1 
HETATM 1713 O O   . HOH   C 3 .   ? -13.26678 27.58701 44.87451 1.000 50.72669  ? 455 HOH   A O   1 
HETATM 1714 O O   . HOH   C 3 .   ? -16.47389 38.67840 17.16207 1.000 55.07821  ? 456 HOH   A O   1 
HETATM 1715 O O   . HOH   C 3 .   ? -16.58058 23.79988 42.97806 1.000 52.19004  ? 457 HOH   A O   1 
HETATM 1716 O O   . HOH   C 3 .   ? -16.77978 28.11040 34.07459 1.000 45.91176  ? 458 HOH   A O   1 
HETATM 1717 O O   . HOH   C 3 .   ? -12.53578 18.38010 41.04246 1.000 57.28612  ? 459 HOH   A O   1 
HETATM 1718 O O   . HOH   C 3 .   ? -15.90039 37.79934 24.10464 1.000 46.33855  ? 460 HOH   A O   1 
HETATM 1719 O O   . HOH   C 3 .   ? -11.63421 24.44532 23.50483 1.000 39.57095  ? 461 HOH   A O   1 
HETATM 1720 O O   . HOH   C 3 .   ? -1.53341  32.78990 24.30158 1.000 35.01425  ? 462 HOH   A O   1 
HETATM 1721 O O   . HOH   C 3 .   ? -8.04952  28.62726 9.76894  1.000 50.90564  ? 463 HOH   A O   1 
HETATM 1722 O O   . HOH   C 3 .   ? -10.88790 30.95928 16.52023 1.000 48.86338  ? 464 HOH   A O   1 
HETATM 1723 O O   . HOH   C 3 .   ? 9.34608   14.95856 29.63844 1.000 52.05855  ? 465 HOH   A O   1 
HETATM 1724 O O   . HOH   C 3 .   ? 7.10158   15.86490 17.88852 1.000 55.13370  ? 466 HOH   A O   1 
HETATM 1725 O O   . HOH   C 3 .   ? -10.19071 33.48169 45.52363 1.000 48.29810  ? 467 HOH   A O   1 
HETATM 1726 O O   . HOH   C 3 .   ? 22.15756  33.35292 23.95275 1.000 59.70867  ? 468 HOH   A O   1 
HETATM 1727 O O   . HOH   C 3 .   ? -4.26202  38.13229 11.76469 1.000 35.30815  ? 469 HOH   A O   1 
HETATM 1728 O O   . HOH   C 3 .   ? -6.23800  25.67468 11.56838 1.000 48.76879  ? 470 HOH   A O   1 
HETATM 1729 O O   . HOH   C 3 .   ? -2.41369  24.31353 9.04561  1.000 49.14886  ? 471 HOH   A O   1 
HETATM 1730 O O   . HOH   C 3 .   ? 14.877    46.008   25.199   1.000 59.40712  ? 472 HOH   A O   1 
HETATM 1731 O O   . HOH   C 3 .   ? -9.86459  49.75291 6.94192  1.000 59.61162  ? 473 HOH   A O   1 
HETATM 1732 O O   . HOH   C 3 .   ? 2.43696   40.54111 31.20507 1.000 48.84216  ? 474 HOH   A O   1 
HETATM 1733 O O   . HOH   C 3 .   ? 0.88307   31.85776 26.70516 1.000 38.97120  ? 475 HOH   A O   1 
HETATM 1734 O O   . HOH   C 3 .   ? -13.04785 19.79015 43.11420 1.000 49.23301  ? 476 HOH   A O   1 
HETATM 1735 O O   . HOH   C 3 .   ? -15.31178 31.36888 35.79346 1.000 60.58587  ? 477 HOH   A O   1 
HETATM 1736 O O   . HOH   C 3 .   ? -12.95966 18.81890 36.99437 1.000 48.08970  ? 478 HOH   A O   1 
HETATM 1737 O O   . HOH   C 3 .   ? 16.20976  23.05899 33.25770 1.000 40.66680  ? 479 HOH   A O   1 
HETATM 1738 O O   . HOH   C 3 .   ? 11.40013  19.15309 23.58908 1.000 43.59954  ? 480 HOH   A O   1 
HETATM 1739 O O   . HOH   C 3 .   ? -0.81008  34.07350 21.12778 1.000 45.98900  ? 481 HOH   A O   1 
HETATM 1740 O O   . HOH   C 3 .   ? -7.39125  17.41730 27.71746 1.000 51.81247  ? 482 HOH   A O   1 
HETATM 1741 O O   . HOH   C 3 .   ? 8.93547   31.48898 9.41010  1.000 43.78046  ? 483 HOH   A O   1 
HETATM 1742 O O   . HOH   C 3 .   ? 5.54332   35.26137 9.69697  1.000 51.84944  ? 484 HOH   A O   1 
HETATM 1743 O O   . HOH   C 3 .   ? -12.36664 17.53219 29.63033 1.000 48.44930  ? 485 HOH   A O   1 
HETATM 1744 O O   . HOH   C 3 .   ? -17.43138 32.31030 23.63238 1.000 43.37752  ? 486 HOH   A O   1 
HETATM 1745 O O   . HOH   C 3 .   ? -13.59068 29.90968 36.36314 1.000 55.57378  ? 487 HOH   A O   1 
HETATM 1746 O O   . HOH   C 3 .   ? -10.69572 35.74557 46.16797 1.000 43.90246  ? 488 HOH   A O   1 
HETATM 1747 O O   . HOH   C 3 .   ? -15.44363 41.02688 23.62025 1.000 60.02564  ? 489 HOH   A O   1 
HETATM 1748 O O   . HOH   C 3 .   ? 14.19778  17.14864 26.07880 1.000 48.81261  ? 490 HOH   A O   1 
HETATM 1749 O O   . HOH   C 3 .   ? -16.13704 27.61933 36.65675 1.000 49.69314  ? 491 HOH   A O   1 
HETATM 1750 O O   . HOH   C 3 .   ? -17.12534 31.58023 25.39421 1.000 42.70312  ? 492 HOH   A O   1 
HETATM 1751 O O   . HOH   C 3 .   ? 0.71912   32.66702 24.55123 1.000 57.85535  ? 493 HOH   A O   1 
HETATM 1752 O O   . HOH   C 3 .   ? 8.12179   29.74615 7.24249  1.000 56.10814  ? 494 HOH   A O   1 
HETATM 1753 O O   . HOH   C 3 .   ? -11.29582 17.10693 27.28114 1.000 43.54466  ? 495 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   ? 0.77816 0.90956 0.89166 0.11282  0.03996  -0.28016 16  GLU A N   
2    C CA  . GLU A 9   ? 0.81390 0.94383 0.91411 0.12937  0.04067  -0.24606 16  GLU A CA  
3    C C   . GLU A 9   ? 0.80732 0.92155 0.90744 0.12860  0.03224  -0.20737 16  GLU A C   
4    O O   . GLU A 9   ? 0.74036 0.87486 0.82868 0.12822  0.01918  -0.19954 16  GLU A O   
5    C CB  . GLU A 9   ? 0.96540 1.14347 1.03709 0.14352  0.03467  -0.24931 16  GLU A CB  
6    C CG  . GLU A 9   ? 0.87205 1.05385 0.92905 0.15680  0.03489  -0.21072 16  GLU A CG  
7    C CD  . GLU A 9   ? 1.00203 1.16500 1.07184 0.16328  0.05060  -0.20463 16  GLU A CD  
8    O OE1 . GLU A 9   ? 1.08475 1.23660 1.15931 0.16689  0.05181  -0.17163 16  GLU A OE1 
9    O OE2 . GLU A 9   ? 1.07789 1.23892 1.15452 0.16504  0.06179  -0.23458 16  GLU A OE2 
10   N N   . VAL A 10  ? 0.68999 0.76964 0.80295 0.12996  0.03946  -0.18444 17  VAL A N   
11   C CA  . VAL A 10  ? 0.58642 0.64823 0.70157 0.12691  0.03241  -0.15252 17  VAL A CA  
12   C C   . VAL A 10  ? 0.55676 0.62341 0.66724 0.13780  0.03248  -0.12333 17  VAL A C   
13   O O   . VAL A 10  ? 0.54402 0.60768 0.66304 0.14622  0.04284  -0.12329 17  VAL A O   
14   C CB  . VAL A 10  ? 0.54741 0.56737 0.68192 0.11733  0.03962  -0.15068 17  VAL A CB  
15   C CG1 . VAL A 10  ? 0.52578 0.53255 0.65864 0.11483  0.03140  -0.11989 17  VAL A CG1 
16   C CG2 . VAL A 10  ? 0.67860 0.69443 0.82166 0.10241  0.04297  -0.18137 17  VAL A CG2 
17   N N   . GLU A 11  ? 0.55780 0.63229 0.65691 0.13717  0.02204  -0.10004 18  GLU A N   
18   C CA  . GLU A 11  ? 0.51199 0.59043 0.61038 0.14187  0.02202  -0.07238 18  GLU A CA  
19   C C   . GLU A 11  ? 0.40247 0.45731 0.51145 0.13487  0.01639  -0.05230 18  GLU A C   
20   O O   . GLU A 11  ? 0.46213 0.50490 0.56722 0.12719  0.00892  -0.05263 18  GLU A O   
21   C CB  . GLU A 11  ? 0.51329 0.61491 0.58886 0.14538  0.01662  -0.06075 18  GLU A CB  
22   C CG  . GLU A 11  ? 0.56465 0.69580 0.62343 0.15494  0.02182  -0.07684 18  GLU A CG  
23   C CD  . GLU A 11  ? 0.74099 0.89078 0.77257 0.16073  0.01767  -0.06004 18  GLU A CD  
24   O OE1 . GLU A 11  ? 0.66620 0.81091 0.68656 0.15957  0.00688  -0.05424 18  GLU A OE1 
25   O OE2 . GLU A 11  ? 0.82366 0.99216 0.84452 0.16755  0.02668  -0.05178 18  GLU A OE2 
26   N N   . THR A 12  ? 0.42809 0.48123 0.55054 0.13839  0.01979  -0.03613 19  THR A N   
27   C CA  . THR A 12  ? 0.45272 0.49012 0.58424 0.13349  0.01344  -0.01798 19  THR A CA  
28   C C   . THR A 12  ? 0.39832 0.45216 0.52869 0.12990  0.00797  0.00231  19  THR A C   
29   O O   . THR A 12  ? 0.43781 0.51354 0.57446 0.13462  0.01430  0.00752  19  THR A O   
30   C CB  . THR A 12  ? 0.43177 0.45615 0.58213 0.14166  0.02037  -0.01597 19  THR A CB  
31   O OG1 . THR A 12  ? 0.44654 0.44642 0.59818 0.14144  0.02776  -0.03463 19  THR A OG1 
32   C CG2 . THR A 12  ? 0.40206 0.41809 0.55834 0.13916  0.01194  0.00438  19  THR A CG2 
33   N N   . PHE A 13  ? 0.41506 0.45839 0.53832 0.12035  -0.00213 0.01206  20  PHE A N   
34   C CA  . PHE A 13  ? 0.44964 0.50203 0.57215 0.11276  -0.00687 0.02837  20  PHE A CA  
35   C C   . PHE A 13  ? 0.41101 0.45730 0.54384 0.10648  -0.01535 0.03826  20  PHE A C   
36   O O   . PHE A 13  ? 0.42289 0.45181 0.55337 0.10681  -0.01926 0.03483  20  PHE A O   
37   C CB  . PHE A 13  ? 0.37856 0.42251 0.47961 0.10762  -0.01123 0.02965  20  PHE A CB  
38   C CG  . PHE A 13  ? 0.36160 0.41460 0.44690 0.11622  -0.00616 0.01970  20  PHE A CG  
39   C CD1 . PHE A 13  ? 0.41201 0.46230 0.49272 0.12100  -0.00707 0.00085  20  PHE A CD1 
40   C CD2 . PHE A 13  ? 0.47074 0.53762 0.54524 0.11872  -0.00009 0.02890  20  PHE A CD2 
41   C CE1 . PHE A 13  ? 0.49370 0.55997 0.55972 0.12914  -0.00472 -0.01108 20  PHE A CE1 
42   C CE2 . PHE A 13  ? 0.53138 0.61088 0.58674 0.12891  0.00327  0.02054  20  PHE A CE2 
43   C CZ  . PHE A 13  ? 0.46778 0.54957 0.51916 0.13465  -0.00036 -0.00073 20  PHE A CZ  
44   N N   . ALA A 14  ? 0.41449 0.47783 0.55827 0.09977  -0.01764 0.05003  21  ALA A N   
45   C CA  . ALA A 14  ? 0.40716 0.47240 0.55902 0.09229  -0.02811 0.05740  21  ALA A CA  
46   C C   . ALA A 14  ? 0.45501 0.50232 0.59073 0.07861  -0.03543 0.05774  21  ALA A C   
47   O O   . ALA A 14  ? 0.44219 0.48496 0.56943 0.07253  -0.03155 0.05979  21  ALA A O   
48   C CB  . ALA A 14  ? 0.35978 0.45917 0.53625 0.08998  -0.02785 0.06602  21  ALA A CB  
49   N N   . PHE A 15  ? 0.47694 0.51198 0.60635 0.07538  -0.04466 0.05629  22  PHE A N   
50   C CA  . PHE A 15  ? 0.48330 0.50246 0.59945 0.06293  -0.05157 0.05457  22  PHE A CA  
51   C C   . PHE A 15  ? 0.55622 0.59047 0.68500 0.04835  -0.05412 0.05985  22  PHE A C   
52   O O   . PHE A 15  ? 0.53291 0.59711 0.68300 0.04720  -0.05575 0.06443  22  PHE A O   
53   C CB  . PHE A 15  ? 0.48486 0.49395 0.59159 0.06255  -0.06004 0.05128  22  PHE A CB  
54   C CG  . PHE A 15  ? 0.47950 0.46737 0.57083 0.06919  -0.05636 0.04359  22  PHE A CG  
55   C CD1 . PHE A 15  ? 0.47167 0.44365 0.54945 0.06786  -0.05474 0.03672  22  PHE A CD1 
56   C CD2 . PHE A 15  ? 0.41835 0.40277 0.50994 0.07692  -0.05370 0.04360  22  PHE A CD2 
57   C CE1 . PHE A 15  ? 0.45400 0.41535 0.52237 0.07328  -0.05178 0.02751  22  PHE A CE1 
58   C CE2 . PHE A 15  ? 0.42289 0.39092 0.50440 0.07911  -0.04846 0.03483  22  PHE A CE2 
59   C CZ  . PHE A 15  ? 0.51862 0.47927 0.59028 0.07680  -0.04817 0.02549  22  PHE A CZ  
60   N N   . GLN A 16  ? 0.50153 0.51505 0.61876 0.03729  -0.05355 0.05857  23  GLN A N   
61   C CA  . GLN A 16  ? 0.60238 0.62239 0.73111 0.01818  -0.05521 0.06036  23  GLN A CA  
62   C C   . GLN A 16  ? 0.56012 0.59765 0.69727 0.01068  -0.06874 0.05452  23  GLN A C   
63   O O   . GLN A 16  ? 0.56841 0.59569 0.69085 0.01750  -0.07610 0.04932  23  GLN A O   
64   C CB  . GLN A 16  ? 0.58692 0.56935 0.69760 0.00963  -0.05112 0.05935  23  GLN A CB  
65   C CG  . GLN A 16  ? 0.87279 0.83626 0.96537 0.02423  -0.04124 0.06502  23  GLN A CG  
66   C CD  . GLN A 16  ? 0.98914 0.94418 1.06614 0.04158  -0.04530 0.05728  23  GLN A CD  
67   O OE1 . GLN A 16  ? 0.99260 0.96138 1.07015 0.05456  -0.04150 0.05693  23  GLN A OE1 
68   N NE2 . GLN A 16  ? 0.98714 0.92051 1.05128 0.04066  -0.05165 0.04909  23  GLN A NE2 
69   N N   . ALA A 17  ? 0.57380 0.64238 0.73482 -0.00349 -0.07168 0.05518  24  ALA A N   
70   C CA  . ALA A 17  ? 0.48921 0.59009 0.66162 -0.00650 -0.08635 0.05054  24  ALA A CA  
71   C C   . ALA A 17  ? 0.50699 0.58600 0.65657 -0.01202 -0.09691 0.03956  24  ALA A C   
72   O O   . ALA A 17  ? 0.66842 0.76161 0.81061 -0.00281 -0.10758 0.03864  24  ALA A O   
73   C CB  . ALA A 17  ? 0.53227 0.67248 0.73593 -0.02592 -0.08818 0.04859  24  ALA A CB  
74   N N   . GLU A 18  ? 0.53292 0.57579 0.66909 -0.02525 -0.09277 0.03196  25  GLU A N   
75   C CA  . GLU A 18  ? 0.63701 0.66043 0.75302 -0.03188 -0.10151 0.01812  25  GLU A CA  
76   C C   . GLU A 18  ? 0.53755 0.53649 0.62739 -0.01289 -0.10016 0.01864  25  GLU A C   
77   O O   . GLU A 18  ? 0.49488 0.49350 0.56839 -0.01135 -0.10838 0.01048  25  GLU A O   
78   C CB  . GLU A 18  ? 0.64815 0.63742 0.76104 -0.05176 -0.09563 0.00891  25  GLU A CB  
79   C CG  . GLU A 18  ? 0.88594 0.89532 1.02757 -0.07569 -0.09255 0.00802  25  GLU A CG  
80   C CD  . GLU A 18  ? 0.84263 0.84903 0.99611 -0.07286 -0.07647 0.02488  25  GLU A CD  
81   O OE1 . GLU A 18  ? 0.85792 0.85034 0.99689 -0.05113 -0.07016 0.03553  25  GLU A OE1 
82   O OE2 . GLU A 18  ? 0.92512 0.94252 1.10103 -0.09358 -0.06901 0.02628  25  GLU A OE2 
83   N N   . ILE A 19  ? 0.48043 0.46305 0.56636 0.00092  -0.08940 0.02707  26  ILE A N   
84   C CA  . ILE A 19  ? 0.54276 0.51013 0.61046 0.01701  -0.08705 0.02619  26  ILE A CA  
85   C C   . ILE A 19  ? 0.51294 0.50363 0.58365 0.02761  -0.09100 0.03232  26  ILE A C   
86   O O   . ILE A 19  ? 0.47917 0.46325 0.53351 0.03331  -0.09292 0.02951  26  ILE A O   
87   C CB  . ILE A 19  ? 0.53877 0.48955 0.60367 0.02783  -0.07593 0.03064  26  ILE A CB  
88   C CG1 . ILE A 19  ? 0.60456 0.52719 0.66167 0.02164  -0.07125 0.02868  26  ILE A CG1 
89   C CG2 . ILE A 19  ? 0.49085 0.43369 0.54311 0.04140  -0.07339 0.02667  26  ILE A CG2 
90   C CD1 . ILE A 19  ? 0.64422 0.53899 0.68089 0.02775  -0.07150 0.01875  26  ILE A CD1 
91   N N   . ALA A 20  ? 0.47190 0.48860 0.56295 0.03174  -0.09041 0.04190  27  ALA A N   
92   C CA  . ALA A 20  ? 0.45194 0.48710 0.54603 0.04467  -0.09363 0.05015  27  ALA A CA  
93   C C   . ALA A 20  ? 0.51806 0.57000 0.60290 0.04073  -0.10713 0.04829  27  ALA A C   
94   O O   . ALA A 20  ? 0.42549 0.47744 0.49694 0.05227  -0.10882 0.05474  27  ALA A O   
95   C CB  . ALA A 20  ? 0.37114 0.43387 0.49120 0.05156  -0.09077 0.05937  27  ALA A CB  
96   N N   . GLN A 21  ? 0.40758 0.47357 0.49810 0.02385  -0.11601 0.03915  28  GLN A N   
97   C CA  . GLN A 21  ? 0.51589 0.60240 0.59549 0.01841  -0.13055 0.03272  28  GLN A CA  
98   C C   . GLN A 21  ? 0.50781 0.56520 0.55540 0.01851  -0.12962 0.02399  28  GLN A C   
99   O O   . GLN A 21  ? 0.53813 0.60808 0.56693 0.02417  -0.13738 0.02504  28  GLN A O   
100  C CB  . GLN A 21  ? 0.51518 0.62332 0.61193 -0.00382 -0.13894 0.01999  28  GLN A CB  
101  C CG  . GLN A 21  ? 0.57439 0.73510 0.70156 -0.00401 -0.14716 0.02591  28  GLN A CG  
102  C CD  . GLN A 21  ? 0.72424 0.89588 0.87921 -0.02741 -0.14398 0.01735  28  GLN A CD  
103  O OE1 . GLN A 21  ? 0.78270 0.93565 0.93255 -0.04901 -0.14462 0.00147  28  GLN A OE1 
104  N NE2 . GLN A 21  ? 0.80714 1.00726 0.99191 -0.02363 -0.13852 0.02755  28  GLN A NE2 
105  N N   . LEU A 22  ? 0.47123 0.49243 0.51133 0.01386  -0.11986 0.01585  29  LEU A N   
106  C CA  . LEU A 22  ? 0.49655 0.49366 0.50959 0.01547  -0.11736 0.00606  29  LEU A CA  
107  C C   . LEU A 22  ? 0.52648 0.51917 0.52716 0.03137  -0.11023 0.01684  29  LEU A C   
108  O O   . LEU A 22  ? 0.45699 0.44988 0.43490 0.03404  -0.11160 0.01448  29  LEU A O   
109  C CB  . LEU A 22  ? 0.52993 0.49231 0.54079 0.01113  -0.10854 -0.00367 29  LEU A CB  
110  C CG  . LEU A 22  ? 0.58074 0.52146 0.56782 0.01648  -0.10384 -0.01420 29  LEU A CG  
111  C CD1 . LEU A 22  ? 0.47944 0.42756 0.44829 0.00772  -0.11317 -0.02843 29  LEU A CD1 
112  C CD2 . LEU A 22  ? 0.51010 0.41936 0.49713 0.01840  -0.09537 -0.02088 29  LEU A CD2 
113  N N   . MET A 23  ? 0.48073 0.46861 0.49549 0.04081  -0.10102 0.02778  30  MET A N   
114  C CA  . MET A 23  ? 0.52240 0.50144 0.52877 0.05258  -0.09167 0.03642  30  MET A CA  
115  C C   . MET A 23  ? 0.43028 0.42703 0.42798 0.06061  -0.09732 0.05019  30  MET A C   
116  O O   . MET A 23  ? 0.56633 0.55420 0.54358 0.06563  -0.09191 0.05515  30  MET A O   
117  C CB  . MET A 23  ? 0.40219 0.37310 0.42682 0.05942  -0.08103 0.04130  30  MET A CB  
118  C CG  . MET A 23  ? 0.46795 0.42414 0.49634 0.05581  -0.07556 0.03006  30  MET A CG  
119  S SD  . MET A 23  ? 0.50734 0.46481 0.55601 0.06310  -0.06662 0.03377  30  MET A SD  
120  C CE  . MET A 23  ? 0.53104 0.47694 0.57642 0.06998  -0.05481 0.03316  30  MET A CE  
121  N N   . SER A 24  ? 0.46419 0.48835 0.47689 0.06290  -0.10763 0.05754  31  SER A N   
122  C CA  . SER A 24  ? 0.53651 0.58260 0.53964 0.07459  -0.11556 0.07209  31  SER A CA  
123  C C   . SER A 24  ? 0.48265 0.53935 0.45729 0.06876  -0.12568 0.06474  31  SER A C   
124  O O   . SER A 24  ? 0.52964 0.58996 0.48076 0.07988  -0.12610 0.07737  31  SER A O   
125  C CB  . SER A 24  ? 0.58662 0.66917 0.61590 0.07913  -0.12613 0.07873  31  SER A CB  
126  O OG  . SER A 24  ? 0.69320 0.80821 0.71155 0.08900  -0.14001 0.08850  31  SER A OG  
127  N N   . LEU A 25  ? 0.61945 0.67871 0.59363 0.05180  -0.13251 0.04431  32  LEU A N   
128  C CA  . LEU A 25  ? 0.60952 0.67506 0.55490 0.04514  -0.14022 0.03163  32  LEU A CA  
129  C C   . LEU A 25  ? 0.58028 0.61744 0.49912 0.05036  -0.12598 0.03280  32  LEU A C   
130  O O   . LEU A 25  ? 0.60297 0.64876 0.49298 0.05695  -0.12714 0.03919  32  LEU A O   
131  C CB  . LEU A 25  ? 0.61506 0.67819 0.56821 0.02514  -0.14645 0.00704  32  LEU A CB  
132  C CG  . LEU A 25  ? 0.77835 0.84788 0.70837 0.01291  -0.15587 -0.01554 32  LEU A CG  
133  C CD1 . LEU A 25  ? 0.74643 0.79125 0.64449 0.01752  -0.14553 -0.02223 32  LEU A CD1 
134  C CD2 . LEU A 25  ? 0.78284 0.90110 0.70554 0.01381  -0.17478 -0.01453 32  LEU A CD2 
135  N N   . ILE A 26  ? 0.56612 0.57314 0.49445 0.04787  -0.11197 0.02705  33  ILE A N   
136  C CA  . ILE A 26  ? 0.60776 0.59386 0.51742 0.05037  -0.09757 0.02438  33  ILE A CA  
137  C C   . ILE A 26  ? 0.59057 0.57431 0.48866 0.06185  -0.08785 0.04605  33  ILE A C   
138  O O   . ILE A 26  ? 0.75110 0.73009 0.62350 0.06323  -0.07932 0.04787  33  ILE A O   
139  C CB  . ILE A 26  ? 0.53395 0.49698 0.46171 0.04773  -0.08659 0.01457  33  ILE A CB  
140  C CG1 . ILE A 26  ? 0.47456 0.43043 0.40331 0.03856  -0.09263 -0.00582 33  ILE A CG1 
141  C CG2 . ILE A 26  ? 0.56870 0.51808 0.48760 0.05130  -0.06991 0.01458  33  ILE A CG2 
142  C CD1 . ILE A 26  ? 0.52512 0.46155 0.47103 0.03982  -0.08475 -0.01186 33  ILE A CD1 
143  N N   . ILE A 27  ? 0.60885 0.59416 0.52460 0.07059  -0.08732 0.06322  34  ILE A N   
144  C CA  . ILE A 27  ? 0.71004 0.68244 0.61696 0.08218  -0.07483 0.08490  34  ILE A CA  
145  C C   . ILE A 27  ? 0.69691 0.68834 0.57569 0.09288  -0.08368 0.10196  34  ILE A C   
146  O O   . ILE A 27  ? 0.83857 0.81644 0.69252 0.09924  -0.07154 0.11722  34  ILE A O   
147  C CB  . ILE A 27  ? 0.67955 0.64284 0.61577 0.08969  -0.06972 0.09468  34  ILE A CB  
148  C CG1 . ILE A 27  ? 0.52281 0.46642 0.47884 0.08114  -0.05756 0.07959  34  ILE A CG1 
149  C CG2 . ILE A 27  ? 0.78877 0.73703 0.71605 0.10457  -0.05916 0.11966  34  ILE A CG2 
150  C CD1 . ILE A 27  ? 0.53958 0.48419 0.52448 0.08531  -0.05790 0.08034  34  ILE A CD1 
151  N N   . ASN A 28  ? 0.64157 0.66703 0.52313 0.09476  -0.10444 0.09991  35  ASN A N   
152  C CA  . ASN A 28  ? 0.78758 0.83945 0.64686 0.10997  -0.11581 0.11889  35  ASN A CA  
153  C C   . ASN A 28  ? 0.86516 0.93876 0.68761 0.10518  -0.12578 0.10906  35  ASN A C   
154  O O   . ASN A 28  ? 0.92065 1.00781 0.71152 0.11967  -0.12879 0.12816  35  ASN A O   
155  C CB  . ASN A 28  ? 0.69541 0.78321 0.58148 0.11698  -0.13398 0.12235  35  ASN A CB  
156  C CG  . ASN A 28  ? 0.83294 0.90288 0.75195 0.12568  -0.12355 0.13336  35  ASN A CG  
157  O OD1 . ASN A 28  ? 0.80889 0.84325 0.72351 0.13477  -0.10523 0.14832  35  ASN A OD1 
158  N ND2 . ASN A 28  ? 0.87356 0.96783 0.82607 0.12148  -0.13353 0.12442  35  ASN A ND2 
159  N N   . THR A 29  ? 0.82952 0.90602 0.65270 0.08699  -0.13056 0.08016  36  THR A N   
160  C CA  . THR A 29  ? 0.91324 1.00988 0.70030 0.08243  -0.13917 0.06674  36  THR A CA  
161  C C   . THR A 29  ? 0.78321 0.85712 0.53567 0.08636  -0.11952 0.07492  36  THR A C   
162  O O   . THR A 29  ? 0.74268 0.78248 0.50578 0.08433  -0.09876 0.07911  36  THR A O   
163  C CB  . THR A 29  ? 0.87699 0.97629 0.67472 0.06226  -0.14740 0.03181  36  THR A CB  
164  O OG1 . THR A 29  ? 1.02620 1.08763 0.82907 0.05484  -0.12918 0.01994  36  THR A OG1 
165  C CG2 . THR A 29  ? 0.81486 0.93110 0.65138 0.05412  -0.16146 0.02425  36  THR A CG2 
166  N N   . PHE A 30  ? 0.80134 0.89897 0.51208 0.09148  -0.12601 0.07657  37  PHE A N   
167  C CA  . PHE A 30  ? 0.78610 0.86887 0.45899 0.09424  -0.10677 0.08397  37  PHE A CA  
168  C C   . PHE A 30  ? 0.78217 0.85845 0.45095 0.07828  -0.10156 0.04963  37  PHE A C   
169  O O   . PHE A 30  ? 0.95700 1.05786 0.61008 0.07195  -0.11713 0.02557  37  PHE A O   
170  C CB  . PHE A 30  ? 0.79354 0.90717 0.41894 0.10940  -0.11570 0.10266  37  PHE A CB  
171  C CG  . PHE A 30  ? 1.00942 1.10811 0.59234 0.11334  -0.09289 0.11630  37  PHE A CG  
172  C CD1 . PHE A 30  ? 0.93190 0.99501 0.51448 0.12065  -0.06813 0.14740  37  PHE A CD1 
173  C CD2 . PHE A 30  ? 0.86535 0.98518 0.40882 0.10847  -0.09437 0.09680  37  PHE A CD2 
174  C CE1 . PHE A 30  ? 0.99093 1.04036 0.53599 0.12141  -0.04403 0.16094  37  PHE A CE1 
175  C CE2 . PHE A 30  ? 0.92923 1.03859 0.43315 0.11161  -0.07095 0.10995  37  PHE A CE2 
176  C CZ  . PHE A 30  ? 0.91524 0.98970 0.42057 0.11732  -0.04516 0.14322  37  PHE A CZ  
177  N N   . TYR A 31  ? 0.71278 0.75744 0.39721 0.07235  -0.07989 0.04543  38  TYR A N   
178  C CA  . TYR A 31  ? 0.73532 0.77228 0.42026 0.06150  -0.07310 0.01423  38  TYR A CA  
179  C C   . TYR A 31  ? 0.77157 0.79050 0.45014 0.06160  -0.04529 0.02136  38  TYR A C   
180  O O   . TYR A 31  ? 0.77824 0.77622 0.48527 0.06068  -0.03206 0.03247  38  TYR A O   
181  C CB  . TYR A 31  ? 0.70789 0.73070 0.43448 0.05283  -0.08032 -0.00556 38  TYR A CB  
182  C CG  . TYR A 31  ? 0.83378 0.84637 0.56045 0.04569  -0.07535 -0.03711 38  TYR A CG  
183  C CD1 . TYR A 31  ? 0.81139 0.83712 0.51544 0.04068  -0.08687 -0.06215 38  TYR A CD1 
184  C CD2 . TYR A 31  ? 0.68872 0.67981 0.43882 0.04526  -0.05964 -0.04346 38  TYR A CD2 
185  C CE1 . TYR A 31  ? 0.71830 0.72954 0.42224 0.03682  -0.08089 -0.09147 38  TYR A CE1 
186  C CE2 . TYR A 31  ? 0.76741 0.74954 0.51817 0.04341  -0.05520 -0.07084 38  TYR A CE2 
187  C CZ  . TYR A 31  ? 0.83651 0.82543 0.56399 0.03986  -0.06494 -0.09418 38  TYR A CZ  
188  O OH  . TYR A 31  ? 0.92350 0.89838 0.65154 0.04052  -0.05902 -0.12184 38  TYR A OH  
189  N N   . SER A 32  ? 0.78242 0.81266 0.42457 0.06155  -0.03578 0.01298  39  SER A N   
190  C CA  . SER A 32  ? 0.80282 0.82302 0.43576 0.06054  -0.00718 0.02283  39  SER A CA  
191  C C   . SER A 32  ? 0.83961 0.85041 0.50160 0.05318  0.00603  -0.00282 39  SER A C   
192  O O   . SER A 32  ? 0.88269 0.88458 0.55840 0.04942  0.02886  0.00462  39  SER A O   
193  C CB  . SER A 32  ? 0.81785 0.85835 0.39666 0.06486  -0.00011 0.02737  39  SER A CB  
194  O OG  . SER A 32  ? 0.85100 0.89651 0.40159 0.07529  -0.00382 0.06188  39  SER A OG  
195  N N   . ASN A 33  ? 0.75410 0.76706 0.42681 0.05138  -0.00735 -0.03295 40  ASN A N   
196  C CA  . ASN A 33  ? 0.73399 0.74003 0.43145 0.04965  0.00325  -0.05730 40  ASN A CA  
197  C C   . ASN A 33  ? 0.72087 0.71016 0.46469 0.04842  0.00215  -0.05300 40  ASN A C   
198  O O   . ASN A 33  ? 0.73442 0.71411 0.50050 0.04952  -0.00859 -0.06949 40  ASN A O   
199  C CB  . ASN A 33  ? 0.71209 0.71992 0.39946 0.05059  -0.00915 -0.08946 40  ASN A CB  
200  C CG  . ASN A 33  ? 0.77261 0.77474 0.47908 0.05427  0.00316  -0.11390 40  ASN A CG  
201  O OD1 . ASN A 33  ? 0.78037 0.79347 0.48850 0.05578  0.02424  -0.11342 40  ASN A OD1 
202  N ND2 . ASN A 33  ? 0.79077 0.77620 0.51317 0.05625  -0.00904 -0.13469 40  ASN A ND2 
203  N N   . LYS A 34  ? 0.61116 0.63410 0.36433 0.00350  -0.10951 0.01342  41  LYS A N   
204  C CA  . LYS A 34  ? 0.54625 0.60570 0.36803 0.00038  -0.10614 0.01454  41  LYS A CA  
205  C C   . LYS A 34  ? 0.57572 0.61407 0.41314 0.00835  -0.08368 0.00853  41  LYS A C   
206  O O   . LYS A 34  ? 0.49389 0.55193 0.37469 0.00271  -0.08404 0.00532  41  LYS A O   
207  C CB  . LYS A 34  ? 0.55042 0.65075 0.41966 0.01356  -0.10320 0.03061  41  LYS A CB  
208  C CG  . LYS A 34  ? 0.50078 0.63785 0.37486 0.00499  -0.12688 0.03966  41  LYS A CG  
209  C CD  . LYS A 34  ? 0.51769 0.68788 0.43354 0.02245  -0.12108 0.05614  41  LYS A CD  
210  C CE  . LYS A 34  ? 0.50820 0.71566 0.42582 0.01790  -0.14271 0.06939  41  LYS A CE  
211  N NZ  . LYS A 34  ? 0.57387 0.82513 0.53586 0.00939  -0.15385 0.07300  41  LYS A NZ  
212  N N   . GLU A 35  ? 0.54285 0.54280 0.34506 0.02279  -0.06385 0.00888  42  GLU A N   
213  C CA  . GLU A 35  ? 0.53998 0.52760 0.36546 0.03290  -0.04148 0.00954  42  GLU A CA  
214  C C   . GLU A 35  ? 0.66664 0.63818 0.48810 0.01873  -0.04619 -0.00570 42  GLU A C   
215  O O   . GLU A 35  ? 0.58825 0.56022 0.44144 0.02402  -0.03253 -0.00429 42  GLU A O   
216  C CB  . GLU A 35  ? 0.62738 0.58150 0.41540 0.05494  -0.01635 0.01832  42  GLU A CB  
217  C CG  . GLU A 35  ? 0.67186 0.57208 0.38063 0.05542  -0.01545 0.00484  42  GLU A CG  
218  C CD  . GLU A 35  ? 0.92514 0.79195 0.59337 0.08427  0.01501  0.01626  42  GLU A CD  
219  O OE1 . GLU A 35  ? 0.88894 0.76345 0.54612 0.09826  0.02198  0.03065  42  GLU A OE1 
220  O OE2 . GLU A 35  ? 1.09215 0.92592 0.73955 0.09520  0.03383  0.01315  42  GLU A OE2 
221  N N   . ILE A 36  ? 0.59923 0.55706 0.38468 -0.00050 -0.06693 -0.01801 43  ILE A N   
222  C CA  . ILE A 36  ? 0.55232 0.49287 0.33364 -0.01546 -0.07216 -0.03043 43  ILE A CA  
223  C C   . ILE A 36  ? 0.58197 0.56390 0.42819 -0.02213 -0.07455 -0.02848 43  ILE A C   
224  O O   . ILE A 36  ? 0.56531 0.53577 0.41665 -0.02969 -0.07297 -0.03556 43  ILE A O   
225  C CB  . ILE A 36  ? 0.64752 0.56646 0.38092 -0.03933 -0.09916 -0.04061 43  ILE A CB  
226  C CG1 . ILE A 36  ? 0.71442 0.68412 0.47740 -0.05411 -0.12349 -0.03222 43  ILE A CG1 
227  C CG2 . ILE A 36  ? 0.68335 0.54362 0.33552 -0.03099 -0.09692 -0.04674 43  ILE A CG2 
228  C CD1 . ILE A 36  ? 0.61478 0.62051 0.42150 -0.07520 -0.13875 -0.03126 43  ILE A CD1 
229  N N   . PHE A 37  ? 0.51577 0.54102 0.40655 -0.01745 -0.07773 -0.01888 44  PHE A N   
230  C CA  . PHE A 37  ? 0.44578 0.50217 0.38753 -0.01919 -0.07871 -0.01796 44  PHE A CA  
231  C C   . PHE A 37  ? 0.45939 0.49998 0.41894 -0.00972 -0.06210 -0.01912 44  PHE A C   
232  O O   . PHE A 37  ? 0.40701 0.45468 0.38737 -0.01533 -0.06385 -0.02358 44  PHE A O   
233  C CB  . PHE A 37  ? 0.42423 0.51713 0.40091 -0.00979 -0.08195 -0.00767 44  PHE A CB  
234  C CG  . PHE A 37  ? 0.37884 0.46563 0.37560 0.00788  -0.06750 0.00019  44  PHE A CG  
235  C CD1 . PHE A 37  ? 0.41912 0.49460 0.39801 0.01820  -0.05967 0.00915  44  PHE A CD1 
236  C CD2 . PHE A 37  ? 0.35350 0.44371 0.38544 0.01305  -0.06311 0.00027  44  PHE A CD2 
237  C CE1 . PHE A 37  ? 0.49342 0.56625 0.49698 0.03197  -0.04695 0.02098  44  PHE A CE1 
238  C CE2 . PHE A 37  ? 0.36815 0.45148 0.42183 0.02457  -0.05443 0.01008  44  PHE A CE2 
239  C CZ  . PHE A 37  ? 0.45198 0.52896 0.49539 0.03336  -0.04584 0.02188  44  PHE A CZ  
240  N N   . LEU A 38  ? 0.46081 0.48358 0.41520 0.00534  -0.04592 -0.01196 45  LEU A N   
241  C CA  . LEU A 38  ? 0.48901 0.50459 0.46950 0.01379  -0.03208 -0.00743 45  LEU A CA  
242  C C   . LEU A 38  ? 0.52234 0.51023 0.47921 0.00918  -0.02653 -0.01605 45  LEU A C   
243  O O   . LEU A 38  ? 0.47104 0.46274 0.45351 0.00734  -0.02527 -0.01694 45  LEU A O   
244  C CB  . LEU A 38  ? 0.43878 0.44888 0.42623 0.03100  -0.01499 0.00873  45  LEU A CB  
245  C CG  . LEU A 38  ? 0.49676 0.51321 0.52948 0.03760  -0.00582 0.02086  45  LEU A CG  
246  C CD1 . LEU A 38  ? 0.37576 0.41220 0.44697 0.02865  -0.02269 0.01649  45  LEU A CD1 
247  C CD2 . LEU A 38  ? 0.44446 0.46542 0.49474 0.05220  0.00891  0.04296  45  LEU A CD2 
248  N N   . ARG A 39  ? 0.49249 0.44754 0.39591 0.00773  -0.02448 -0.02258 46  ARG A N   
249  C CA  . ARG A 39  ? 0.57093 0.49052 0.44395 0.00309  -0.02069 -0.03196 46  ARG A CA  
250  C C   . ARG A 39  ? 0.59184 0.52720 0.48380 -0.01692 -0.03725 -0.04023 46  ARG A C   
251  O O   . ARG A 39  ? 0.54463 0.47071 0.44655 -0.01753 -0.03163 -0.04193 46  ARG A O   
252  C CB  . ARG A 39  ? 0.59428 0.46716 0.39587 0.00259  -0.02178 -0.04028 46  ARG A CB  
253  C CG  . ARG A 39  ? 0.87412 0.70253 0.63451 -0.00898 -0.02664 -0.05343 46  ARG A CG  
254  C CD  . ARG A 39  ? 0.89366 0.67136 0.57684 -0.01543 -0.03785 -0.06434 46  ARG A CD  
255  N NE  . ARG A 39  ? 0.96829 0.76944 0.65434 -0.04266 -0.06916 -0.06828 46  ARG A NE  
256  C CZ  . ARG A 39  ? 0.98758 0.76459 0.62105 -0.05193 -0.08724 -0.07339 46  ARG A CZ  
257  N NH1 . ARG A 39  ? 0.86980 0.59090 0.43319 -0.03475 -0.07655 -0.07826 46  ARG A NH1 
258  N NH2 . ARG A 39  ? 0.85496 0.66532 0.50538 -0.07771 -0.11674 -0.07166 46  ARG A NH2 
259  N N   . GLU A 40  ? 0.43410 0.39725 0.33429 -0.03159 -0.05632 -0.04210 47  GLU A N   
260  C CA  . GLU A 40  ? 0.47882 0.46247 0.39863 -0.04892 -0.06966 -0.04524 47  GLU A CA  
261  C C   . GLU A 40  ? 0.52188 0.53083 0.48749 -0.04097 -0.06332 -0.04147 47  GLU A C   
262  O O   . GLU A 40  ? 0.44276 0.44983 0.41565 -0.04773 -0.06382 -0.04399 47  GLU A O   
263  C CB  . GLU A 40  ? 0.49824 0.51498 0.42450 -0.06234 -0.08881 -0.04178 47  GLU A CB  
264  C CG  . GLU A 40  ? 0.59555 0.58660 0.47354 -0.07596 -0.10322 -0.04543 47  GLU A CG  
265  C CD  . GLU A 40  ? 0.81174 0.74845 0.64377 -0.08738 -0.10502 -0.05580 47  GLU A CD  
266  O OE1 . GLU A 40  ? 0.73055 0.66927 0.57725 -0.10025 -0.10868 -0.05679 47  GLU A OE1 
267  O OE2 . GLU A 40  ? 0.93142 0.81960 0.70851 -0.08183 -0.10201 -0.06243 47  GLU A OE2 
268  N N   . LEU A 41  ? 0.42451 0.45304 0.41768 -0.02717 -0.05904 -0.03511 48  LEU A N   
269  C CA  . LEU A 41  ? 0.41159 0.45519 0.43986 -0.02044 -0.05761 -0.03293 48  LEU A CA  
270  C C   . LEU A 41  ? 0.38987 0.41144 0.42198 -0.01491 -0.04677 -0.03138 48  LEU A C   
271  O O   . LEU A 41  ? 0.43245 0.45745 0.47909 -0.01649 -0.04886 -0.03276 48  LEU A O   
272  C CB  . LEU A 41  ? 0.32727 0.38752 0.37895 -0.00904 -0.05913 -0.02649 48  LEU A CB  
273  C CG  . LEU A 41  ? 0.36103 0.44794 0.41520 -0.01020 -0.06872 -0.02536 48  LEU A CG  
274  C CD1 . LEU A 41  ? 0.32600 0.42074 0.40010 0.00310  -0.06947 -0.01910 48  LEU A CD1 
275  C CD2 . LEU A 41  ? 0.33834 0.44534 0.39929 -0.01652 -0.07500 -0.02819 48  LEU A CD2 
276  N N   . ILE A 42  ? 0.38068 0.38091 0.39931 -0.00620 -0.03402 -0.02618 49  ILE A N   
277  C CA  . ILE A 42  ? 0.42370 0.40727 0.44937 0.00202  -0.02118 -0.02004 49  ILE A CA  
278  C C   . ILE A 42  ? 0.46401 0.42516 0.46473 -0.00604 -0.02031 -0.02849 49  ILE A C   
279  O O   . ILE A 42  ? 0.44272 0.40177 0.45917 -0.00400 -0.01711 -0.02533 49  ILE A O   
280  C CB  . ILE A 42  ? 0.42790 0.39618 0.44350 0.01773  -0.00315 -0.00850 49  ILE A CB  
281  C CG1 . ILE A 42  ? 0.40963 0.40246 0.46269 0.02472  -0.00385 0.00532  49  ILE A CG1 
282  C CG2 . ILE A 42  ? 0.44699 0.39659 0.46340 0.02892  0.01376  -0.00001 49  ILE A CG2 
283  C CD1 . ILE A 42  ? 0.40768 0.39289 0.45763 0.04184  0.01654  0.02255  49  ILE A CD1 
284  N N   . SER A 43  ? 0.41747 0.36026 0.37905 -0.01686 -0.02562 -0.03804 50  SER A N   
285  C CA  . SER A 43  ? 0.48418 0.40147 0.42139 -0.02830 -0.02809 -0.04530 50  SER A CA  
286  C C   . SER A 43  ? 0.47939 0.42519 0.44560 -0.03982 -0.03909 -0.04581 50  SER A C   
287  O O   . SER A 43  ? 0.46308 0.39602 0.42880 -0.04238 -0.03608 -0.04575 50  SER A O   
288  C CB  . SER A 43  ? 0.46786 0.35668 0.35643 -0.04162 -0.03744 -0.05420 50  SER A CB  
289  O OG  . SER A 43  ? 0.71375 0.59851 0.59571 -0.06292 -0.05120 -0.05893 50  SER A OG  
290  N N   . ASN A 44  ? 0.47945 0.46281 0.46872 -0.04386 -0.04989 -0.04478 51  ASN A N   
291  C CA  . ASN A 44  ? 0.40565 0.41596 0.41889 -0.04810 -0.05618 -0.04330 51  ASN A CA  
292  C C   . ASN A 44  ? 0.38878 0.39850 0.42267 -0.03603 -0.05065 -0.04015 51  ASN A C   
293  O O   . ASN A 44  ? 0.42244 0.43329 0.46040 -0.03874 -0.05137 -0.03944 51  ASN A O   
294  C CB  . ASN A 44  ? 0.36539 0.41254 0.39588 -0.04733 -0.06471 -0.04106 51  ASN A CB  
295  C CG  . ASN A 44  ? 0.48793 0.54949 0.50906 -0.06372 -0.07470 -0.03922 51  ASN A CG  
296  O OD1 . ASN A 44  ? 0.46107 0.49883 0.45817 -0.07862 -0.07854 -0.04161 51  ASN A OD1 
297  N ND2 . ASN A 44  ? 0.45056 0.54950 0.49023 -0.06104 -0.08025 -0.03341 51  ASN A ND2 
298  N N   . SER A 45  ? 0.39179 0.40098 0.44027 -0.02381 -0.04685 -0.03588 52  SER A N   
299  C CA  . SER A 45  ? 0.34608 0.35553 0.41760 -0.01558 -0.04656 -0.02991 52  SER A CA  
300  C C   . SER A 45  ? 0.44163 0.42983 0.50623 -0.01412 -0.03674 -0.02594 52  SER A C   
301  O O   . SER A 45  ? 0.40829 0.39869 0.48463 -0.01304 -0.04002 -0.02277 52  SER A O   
302  C CB  . SER A 45  ? 0.34563 0.35963 0.43895 -0.00639 -0.04596 -0.02148 52  SER A CB  
303  O OG  . SER A 45  ? 0.35184 0.38117 0.45260 -0.00590 -0.05636 -0.02459 52  SER A OG  
304  N N   . SER A 46  ? 0.45697 0.42057 0.49762 -0.01210 -0.02455 -0.02583 53  SER A N   
305  C CA  . SER A 46  ? 0.47755 0.41370 0.50479 -0.00729 -0.01260 -0.02206 53  SER A CA  
306  C C   . SER A 46  ? 0.40385 0.33413 0.42004 -0.01958 -0.01895 -0.02776 53  SER A C   
307  O O   . SER A 46  ? 0.42116 0.34505 0.44518 -0.01520 -0.01501 -0.02162 53  SER A O   
308  C CB  . SER A 46  ? 0.57373 0.47403 0.56235 -0.00101 0.00134  -0.02409 53  SER A CB  
309  O OG  . SER A 46  ? 0.59348 0.46256 0.56768 0.01046  0.01700  -0.01822 53  SER A OG  
310  N N   . ASP A 47  ? 0.39771 0.33324 0.39898 -0.03507 -0.02884 -0.03614 54  ASP A N   
311  C CA  . ASP A 47  ? 0.41312 0.34964 0.41009 -0.04805 -0.03454 -0.03692 54  ASP A CA  
312  C C   . ASP A 47  ? 0.45567 0.41965 0.47957 -0.04248 -0.03859 -0.03192 54  ASP A C   
313  O O   . ASP A 47  ? 0.43634 0.39304 0.45945 -0.04339 -0.03655 -0.02766 54  ASP A O   
314  C CB  . ASP A 47  ? 0.45393 0.40344 0.44170 -0.06602 -0.04585 -0.04078 54  ASP A CB  
315  C CG  . ASP A 47  ? 0.58508 0.49682 0.53524 -0.07691 -0.04775 -0.04671 54  ASP A CG  
316  O OD1 . ASP A 47  ? 0.62738 0.49586 0.55128 -0.06845 -0.03706 -0.04909 54  ASP A OD1 
317  O OD2 . ASP A 47  ? 0.63351 0.55745 0.57801 -0.09278 -0.06058 -0.04799 54  ASP A OD2 
318  N N   . ALA A 48  ? 0.36942 0.35995 0.41210 -0.03589 -0.04518 -0.03250 55  ALA A N   
319  C CA  . ALA A 48  ? 0.37686 0.38385 0.43348 -0.02926 -0.05179 -0.03016 55  ALA A CA  
320  C C   . ALA A 48  ? 0.37632 0.37101 0.44380 -0.02107 -0.05043 -0.02313 55  ALA A C   
321  O O   . ALA A 48  ? 0.33327 0.33009 0.40117 -0.01903 -0.05459 -0.01990 55  ALA A O   
322  C CB  . ALA A 48  ? 0.37595 0.40136 0.44272 -0.02255 -0.06023 -0.03350 55  ALA A CB  
323  N N   . LEU A 49  ? 0.31572 0.30018 0.39312 -0.01500 -0.04415 -0.01783 56  LEU A N   
324  C CA  . LEU A 49  ? 0.34733 0.32717 0.44305 -0.00654 -0.04219 -0.00552 56  LEU A CA  
325  C C   . LEU A 49  ? 0.37154 0.33093 0.45230 -0.00616 -0.03128 -0.00164 56  LEU A C   
326  O O   . LEU A 49  ? 0.41009 0.37124 0.50187 -0.00173 -0.03414 0.00748  56  LEU A O   
327  C CB  . LEU A 49  ? 0.32326 0.30357 0.43849 0.00216  -0.03470 0.00464  56  LEU A CB  
328  C CG  . LEU A 49  ? 0.42341 0.42221 0.56218 0.00188  -0.04783 0.00646  56  LEU A CG  
329  C CD1 . LEU A 49  ? 0.37771 0.37685 0.52816 0.00911  -0.03519 0.01615  56  LEU A CD1 
330  C CD2 . LEU A 49  ? 0.38004 0.38920 0.54605 0.00199  -0.06528 0.01639  56  LEU A CD2 
331  N N   . ASP A 50  ? 0.41231 0.34846 0.46527 -0.01143 -0.02088 -0.00805 57  ASP A N   
332  C CA  . ASP A 50  ? 0.46416 0.37224 0.49702 -0.01307 -0.01228 -0.00569 57  ASP A CA  
333  C C   . ASP A 50  ? 0.41685 0.33784 0.45201 -0.02075 -0.02111 -0.00446 57  ASP A C   
334  O O   . ASP A 50  ? 0.42025 0.32968 0.45508 -0.01631 -0.01683 0.00418  57  ASP A O   
335  C CB  . ASP A 50  ? 0.42242 0.29754 0.41840 -0.02287 -0.00693 -0.01540 57  ASP A CB  
336  C CG  . ASP A 50  ? 0.58297 0.42923 0.56129 -0.00941 0.00756  -0.01487 57  ASP A CG  
337  O OD1 . ASP A 50  ? 0.59566 0.44453 0.59262 0.00928  0.01909  -0.00225 57  ASP A OD1 
338  O OD2 . ASP A 50  ? 0.67565 0.49723 0.62058 -0.01684 0.00726  -0.02511 57  ASP A OD2 
339  N N   . LYS A 51  ? 0.35186 0.29738 0.38837 -0.02958 -0.03152 -0.01084 58  LYS A N   
340  C CA  . LYS A 51  ? 0.39534 0.35317 0.42895 -0.03443 -0.03579 -0.00751 58  LYS A CA  
341  C C   . LYS A 51  ? 0.37615 0.34389 0.42120 -0.02255 -0.04210 -0.00080 58  LYS A C   
342  O O   . LYS A 51  ? 0.48918 0.45110 0.52890 -0.02141 -0.04015 0.00710  58  LYS A O   
343  C CB  . LYS A 51  ? 0.40245 0.38712 0.43535 -0.04180 -0.04171 -0.01228 58  LYS A CB  
344  C CG  . LYS A 51  ? 0.61665 0.61602 0.64541 -0.04567 -0.04109 -0.00466 58  LYS A CG  
345  C CD  . LYS A 51  ? 0.69326 0.71492 0.72363 -0.05853 -0.04146 -0.00250 58  LYS A CD  
346  C CE  . LYS A 51  ? 0.61594 0.65162 0.64637 -0.06443 -0.03708 0.01140  58  LYS A CE  
347  N NZ  . LYS A 51  ? 0.63878 0.71167 0.67310 -0.05207 -0.03524 0.01680  58  LYS A NZ  
348  N N   . ILE A 52  ? 0.41518 0.39551 0.47444 -0.01492 -0.05209 -0.00282 59  ILE A N   
349  C CA  . ILE A 52  ? 0.39028 0.37556 0.45680 -0.00680 -0.06438 0.00348  59  ILE A CA  
350  C C   . ILE A 52  ? 0.39474 0.36901 0.47522 -0.00161 -0.05931 0.01738  59  ILE A C   
351  O O   . ILE A 52  ? 0.47535 0.44953 0.55461 0.00244  -0.06508 0.02606  59  ILE A O   
352  C CB  . ILE A 52  ? 0.46523 0.45950 0.54268 -0.00324 -0.08055 -0.00113 59  ILE A CB  
353  C CG1 . ILE A 52  ? 0.38340 0.37640 0.45876 0.00193  -0.09978 0.00345  59  ILE A CG1 
354  C CG2 . ILE A 52  ? 0.31412 0.30831 0.41776 -0.00271 -0.07776 0.00420  59  ILE A CG2 
355  C CD1 . ILE A 52  ? 0.39450 0.38625 0.43766 0.00605  -0.10144 -0.00051 59  ILE A CD1 
356  N N   . ARG A 53  ? 0.45424 0.41837 0.54530 0.00088  -0.04675 0.02131  60  ARG A N   
357  C CA  . ARG A 53  ? 0.49651 0.45140 0.60207 0.01094  -0.03769 0.03777  60  ARG A CA  
358  C C   . ARG A 53  ? 0.50135 0.43501 0.58565 0.01059  -0.02722 0.04097  60  ARG A C   
359  O O   . ARG A 53  ? 0.54058 0.47333 0.63464 0.01885  -0.02691 0.05570  60  ARG A O   
360  C CB  . ARG A 53  ? 0.43462 0.38022 0.54901 0.01867  -0.02183 0.04214  60  ARG A CB  
361  C CG  . ARG A 53  ? 0.57600 0.51739 0.71062 0.03483  -0.00912 0.06377  60  ARG A CG  
362  C CD  . ARG A 53  ? 0.71046 0.63907 0.84539 0.04762  0.01223  0.06922  60  ARG A CD  
363  N NE  . ARG A 53  ? 0.86663 0.77393 0.99889 0.06703  0.03442  0.08583  60  ARG A NE  
364  C CZ  . ARG A 53  ? 0.94281 0.86805 1.10856 0.07906  0.03487  0.10989  60  ARG A CZ  
365  N NH1 . ARG A 53  ? 0.96275 0.92700 1.16821 0.07165  0.01104  0.12076  60  ARG A NH1 
366  N NH2 . ARG A 53  ? 0.80047 0.70101 0.95725 0.09975  0.05872  0.12423  60  ARG A NH2 
367  N N   . TYR A 54  ? 0.46683 0.38407 0.52414 -0.00028 -0.02051 0.02958  61  TYR A N   
368  C CA  . TYR A 54  ? 0.52676 0.42126 0.56449 -0.00442 -0.01284 0.03389  61  TYR A CA  
369  C C   . TYR A 54  ? 0.44977 0.36335 0.48900 -0.00492 -0.02291 0.04031  61  TYR A C   
370  O O   . TYR A 54  ? 0.42873 0.33102 0.46554 0.00048  -0.01874 0.05268  61  TYR A O   
371  C CB  . TYR A 54  ? 0.43019 0.30572 0.44312 -0.02092 -0.00896 0.02272  61  TYR A CB  
372  C CG  . TYR A 54  ? 0.51592 0.37164 0.51226 -0.03078 -0.00548 0.02881  61  TYR A CG  
373  C CD1 . TYR A 54  ? 0.54547 0.35738 0.52529 -0.02620 0.00620  0.03507  61  TYR A CD1 
374  C CD2 . TYR A 54  ? 0.47413 0.35354 0.47099 -0.04302 -0.01223 0.03067  61  TYR A CD2 
375  C CE1 . TYR A 54  ? 0.52708 0.31657 0.49214 -0.03673 0.00833  0.04220  61  TYR A CE1 
376  C CE2 . TYR A 54  ? 0.50326 0.36705 0.48958 -0.05343 -0.00858 0.04052  61  TYR A CE2 
377  C CZ  . TYR A 54  ? 0.51516 0.33251 0.48596 -0.05184 0.00033  0.04579  61  TYR A CZ  
378  O OH  . TYR A 54  ? 0.54666 0.34362 0.50702 -0.06369 0.00293  0.05687  61  TYR A OH  
379  N N   . GLU A 55  ? 0.42322 0.36274 0.46199 -0.00878 -0.03494 0.03274  62  GLU A N   
380  C CA  . GLU A 55  ? 0.48548 0.43907 0.51544 -0.00550 -0.04309 0.03791  62  GLU A CA  
381  C C   . GLU A 55  ? 0.54558 0.50283 0.58636 0.00623  -0.05488 0.04805  62  GLU A C   
382  O O   . GLU A 55  ? 0.49443 0.45179 0.52443 0.01091  -0.05817 0.05761  62  GLU A O   
383  C CB  . GLU A 55  ? 0.41945 0.39449 0.44048 -0.00666 -0.05107 0.02731  62  GLU A CB  
384  C CG  . GLU A 55  ? 0.63598 0.61772 0.65089 -0.01872 -0.04150 0.02352  62  GLU A CG  
385  C CD  . GLU A 55  ? 0.72213 0.72902 0.72773 -0.01404 -0.04500 0.01944  62  GLU A CD  
386  O OE1 . GLU A 55  ? 0.68558 0.69567 0.68345 -0.00148 -0.05622 0.01388  62  GLU A OE1 
387  O OE2 . GLU A 55  ? 0.79771 0.81959 0.80314 -0.02253 -0.03709 0.02331  62  GLU A OE2 
388  N N   . SER A 56  ? 0.44788 0.41024 0.51166 0.01025  -0.06259 0.04882  63  SER A N   
389  C CA  . SER A 56  ? 0.41805 0.38873 0.50020 0.01788  -0.07831 0.06231  63  SER A CA  
390  C C   . SER A 56  ? 0.50908 0.47108 0.60258 0.02583  -0.06737 0.08154  63  SER A C   
391  O O   . SER A 56  ? 0.58323 0.55545 0.69107 0.03188  -0.08153 0.09677  63  SER A O   
392  C CB  . SER A 56  ? 0.42158 0.40386 0.53362 0.01763  -0.08871 0.06317  63  SER A CB  
393  O OG  . SER A 56  ? 0.47298 0.45303 0.61103 0.02379  -0.07198 0.07607  63  SER A OG  
394  N N   . LEU A 57  ? 0.51012 0.45038 0.59524 0.02614  -0.04432 0.08189  64  LEU A N   
395  C CA  . LEU A 57  ? 0.58307 0.50751 0.67372 0.03700  -0.03126 0.10016  64  LEU A CA  
396  C C   . LEU A 57  ? 0.58330 0.50567 0.65724 0.03750  -0.03584 0.10873  64  LEU A C   
397  O O   . LEU A 57  ? 0.61132 0.53302 0.69683 0.04876  -0.03507 0.12826  64  LEU A O   
398  C CB  . LEU A 57  ? 0.59272 0.48143 0.66701 0.03744  -0.00709 0.09534  64  LEU A CB  
399  C CG  . LEU A 57  ? 0.64390 0.52965 0.72819 0.04145  0.00145  0.08946  64  LEU A CG  
400  C CD1 . LEU A 57  ? 0.57197 0.41066 0.62717 0.04493  0.02399  0.08476  64  LEU A CD1 
401  C CD2 . LEU A 57  ? 0.49417 0.40540 0.61935 0.05667  -0.00130 0.10938  64  LEU A CD2 
402  N N   . THR A 58  ? 0.56630 0.62365 0.55096 0.19205  0.01737  0.17200  65  THR A N   
403  C CA  . THR A 58  ? 0.70820 0.73246 0.63720 0.19671  0.02598  0.18113  65  THR A CA  
404  C C   . THR A 58  ? 0.68056 0.69781 0.55969 0.17297  0.01046  0.16976  65  THR A C   
405  O O   . THR A 58  ? 0.78626 0.77922 0.61241 0.17662  0.01513  0.17740  65  THR A O   
406  C CB  . THR A 58  ? 0.66023 0.62806 0.58666 0.20490  0.06367  0.17101  65  THR A CB  
407  O OG1 . THR A 58  ? 0.76951 0.71307 0.70540 0.18621  0.07502  0.13831  65  THR A OG1 
408  C CG2 . THR A 58  ? 0.69751 0.67259 0.67115 0.22071  0.07665  0.17436  65  THR A CG2 
409  N N   . ASP A 59  ? 0.76515 0.80109 0.65811 0.14964  -0.00787 0.15195  66  ASP A N   
410  C CA  . ASP A 59  ? 0.64662 0.67585 0.49673 0.12623  -0.02552 0.13732  66  ASP A CA  
411  C C   . ASP A 59  ? 0.66134 0.73193 0.54002 0.10502  -0.05467 0.13056  66  ASP A C   
412  O O   . ASP A 59  ? 0.65679 0.71043 0.55021 0.08718  -0.05263 0.10809  66  ASP A O   
413  C CB  . ASP A 59  ? 0.78328 0.75742 0.60944 0.11486  -0.00320 0.10913  66  ASP A CB  
414  C CG  . ASP A 59  ? 0.91634 0.87769 0.68747 0.09665  -0.01890 0.09516  66  ASP A CG  
415  O OD1 . ASP A 59  ? 0.79229 0.78897 0.55251 0.08750  -0.05068 0.10196  66  ASP A OD1 
416  O OD2 . ASP A 59  ? 0.92916 0.84730 0.66985 0.09178  0.00017  0.07513  66  ASP A OD2 
417  N N   . PRO A 60  ? 0.67476 0.79904 0.56182 0.10625  -0.08179 0.14876  67  PRO A N   
418  C CA  . PRO A 60  ? 0.60364 0.77056 0.52373 0.08315  -0.10733 0.14325  67  PRO A CA  
419  C C   . PRO A 60  ? 0.69081 0.83627 0.58325 0.05239  -0.12217 0.11834  67  PRO A C   
420  O O   . PRO A 60  ? 0.59505 0.75719 0.51586 0.02946  -0.13586 0.10912  67  PRO A O   
421  C CB  . PRO A 60  ? 0.66220 0.89120 0.58893 0.09298  -0.13294 0.16576  67  PRO A CB  
422  C CG  . PRO A 60  ? 0.65893 0.87805 0.57354 0.12777  -0.11595 0.18657  67  PRO A CG  
423  C CD  . PRO A 60  ? 0.68848 0.83838 0.55879 0.13018  -0.08964 0.17512  67  PRO A CD  
424  N N   . SER A 61  ? 0.61947 0.72698 0.45624 0.05144  -0.11951 0.10722  68  SER A N   
425  C CA  . SER A 61  ? 0.60289 0.68860 0.41086 0.02465  -0.13533 0.08129  68  SER A CA  
426  C C   . SER A 61  ? 0.70685 0.75004 0.52873 0.01135  -0.11982 0.05687  68  SER A C   
427  O O   . SER A 61  ? 0.68434 0.71103 0.49220 -0.01257 -0.13575 0.03492  68  SER A O   
428  C CB  . SER A 61  ? 0.66056 0.71774 0.40290 0.03109  -0.13462 0.07531  68  SER A CB  
429  O OG  . SER A 61  ? 0.76967 0.77635 0.49284 0.04399  -0.09988 0.06836  68  SER A OG  
430  N N   . LYS A 62  ? 0.57689 0.60097 0.42525 0.02774  -0.09076 0.05856  69  LYS A N   
431  C CA  . LYS A 62  ? 0.55226 0.54013 0.41653 0.01927  -0.07796 0.03472  69  LYS A CA  
432  C C   . LYS A 62  ? 0.60800 0.61905 0.50927 0.00020  -0.09583 0.03432  69  LYS A C   
433  O O   . LYS A 62  ? 0.58128 0.55880 0.48633 -0.01017 -0.09181 0.01317  69  LYS A O   
434  C CB  . LYS A 62  ? 0.54560 0.51409 0.43441 0.04382  -0.04451 0.03591  69  LYS A CB  
435  C CG  . LYS A 62  ? 0.71598 0.65709 0.57151 0.06021  -0.02185 0.03674  69  LYS A CG  
436  C CD  . LYS A 62  ? 0.66150 0.56230 0.53040 0.07157  0.01018  0.01644  69  LYS A CD  
437  C CE  . LYS A 62  ? 0.76948 0.64615 0.61127 0.08613  0.03630  0.02087  69  LYS A CE  
438  N NZ  . LYS A 62  ? 0.87211 0.70644 0.71498 0.08876  0.06447  -0.00913 69  LYS A NZ  
439  N N   . LEU A 63  ? 0.55784 0.62486 0.48542 -0.00411 -0.11470 0.05679  70  LEU A N   
440  C CA  . LEU A 63  ? 0.52567 0.61998 0.48840 -0.02593 -0.13111 0.05897  70  LEU A CA  
441  C C   . LEU A 63  ? 0.61593 0.72131 0.55932 -0.05686 -0.16270 0.05008  70  LEU A C   
442  O O   . LEU A 63  ? 0.54869 0.68238 0.52213 -0.07922 -0.17836 0.05405  70  LEU A O   
443  C CB  . LEU A 63  ? 0.50153 0.65716 0.51279 -0.01259 -0.13114 0.08710  70  LEU A CB  
444  C CG  . LEU A 63  ? 0.45776 0.60675 0.49779 0.01688  -0.10287 0.09481  70  LEU A CG  
445  C CD1 . LEU A 63  ? 0.42993 0.64439 0.51651 0.02955  -0.10707 0.12124  70  LEU A CD1 
446  C CD2 . LEU A 63  ? 0.38507 0.49092 0.43409 0.01183  -0.08856 0.07526  70  LEU A CD2 
447  N N   . ASP A 64  ? 0.54961 0.63418 0.44411 -0.05874 -0.17205 0.03776  71  ASP A N   
448  C CA  . ASP A 64  ? 0.64829 0.73820 0.52251 -0.08708 -0.20349 0.02407  71  ASP A CA  
449  C C   . ASP A 64  ? 0.63207 0.68048 0.50684 -0.11360 -0.20874 0.00109  71  ASP A C   
450  O O   . ASP A 64  ? 0.63611 0.69508 0.51265 -0.14237 -0.23554 -0.00695 71  ASP A O   
451  C CB  . ASP A 64  ? 0.64118 0.71110 0.45729 -0.07924 -0.21000 0.01297  71  ASP A CB  
452  C CG  . ASP A 64  ? 0.79912 0.91128 0.60712 -0.05626 -0.21292 0.03659  71  ASP A CG  
453  O OD1 . ASP A 64  ? 0.72723 0.89176 0.57701 -0.05051 -0.21749 0.05894  71  ASP A OD1 
454  O OD2 . ASP A 64  ? 0.68809 0.78043 0.44570 -0.04256 -0.21041 0.03276  71  ASP A OD2 
455  N N   . SER A 65  ? 0.61067 0.61092 0.48370 -0.10380 -0.18458 -0.01074 72  SER A N   
456  C CA  . SER A 65  ? 0.58851 0.54413 0.46030 -0.12330 -0.18747 -0.03131 72  SER A CA  
457  C C   . SER A 65  ? 0.72018 0.69657 0.64116 -0.13109 -0.18296 -0.01528 72  SER A C   
458  O O   . SER A 65  ? 0.70686 0.64070 0.62778 -0.13822 -0.17714 -0.02838 72  SER A O   
459  C CB  . SER A 65  ? 0.66892 0.56371 0.51246 -0.10578 -0.16489 -0.05526 72  SER A CB  
460  O OG  . SER A 65  ? 0.58421 0.48835 0.44264 -0.07496 -0.13645 -0.04311 72  SER A OG  
461  N N   . GLY A 66  ? 0.55913 0.59979 0.51964 -0.12782 -0.18521 0.01245  73  GLY A N   
462  C CA  . GLY A 66  ? 0.56129 0.62898 0.56875 -0.13460 -0.17982 0.02924  73  GLY A CA  
463  C C   . GLY A 66  ? 0.51805 0.63564 0.56307 -0.10587 -0.16288 0.05480  73  GLY A C   
464  O O   . GLY A 66  ? 0.53022 0.62720 0.57093 -0.07567 -0.14020 0.05350  73  GLY A O   
465  N N   . LYS A 67  ? 0.49961 0.68442 0.58366 -0.11497 -0.17417 0.07652  74  LYS A N   
466  C CA  . LYS A 67  ? 0.45567 0.69348 0.57711 -0.08713 -0.16148 0.10063  74  LYS A CA  
467  C C   . LYS A 67  ? 0.50430 0.74416 0.66122 -0.07965 -0.14245 0.10916  74  LYS A C   
468  O O   . LYS A 67  ? 0.44023 0.69897 0.61894 -0.04771 -0.12505 0.12131  74  LYS A O   
469  C CB  . LYS A 67  ? 0.40248 0.71852 0.55028 -0.09659 -0.18337 0.11816  74  LYS A CB  
470  C CG  . LYS A 67  ? 0.62307 0.95620 0.74497 -0.07742 -0.19318 0.12151  74  LYS A CG  
471  C CD  . LYS A 67  ? 0.71336 1.04161 0.80318 -0.10351 -0.22083 0.10609  74  LYS A CD  
472  C CE  . LYS A 67  ? 0.81239 1.11969 0.85308 -0.08130 -0.22246 0.10186  74  LYS A CE  
473  N NZ  . LYS A 67  ? 0.86842 1.12615 0.86102 -0.10089 -0.23522 0.07638  74  LYS A NZ  
474  N N   . GLU A 68  ? 0.45586 0.67443 0.61692 -0.10708 -0.14553 0.10309  75  GLU A N   
475  C CA  . GLU A 68  ? 0.45729 0.67970 0.64842 -0.10015 -0.12809 0.11324  75  GLU A CA  
476  C C   . GLU A 68  ? 0.43331 0.59769 0.60719 -0.06919 -0.10493 0.09903  75  GLU A C   
477  O O   . GLU A 68  ? 0.52761 0.62886 0.66195 -0.07025 -0.10416 0.07495  75  GLU A O   
478  C CB  . GLU A 68  ? 0.46426 0.67178 0.65818 -0.13926 -0.13690 0.11157  75  GLU A CB  
479  C CG  . GLU A 68  ? 0.67690 0.91443 0.87265 -0.17803 -0.16433 0.11115  75  GLU A CG  
480  C CD  . GLU A 68  ? 1.01287 1.18799 1.15889 -0.19482 -0.17995 0.08427  75  GLU A CD  
481  O OE1 . GLU A 68  ? 0.95623 1.05913 1.07203 -0.19646 -0.17257 0.06686  75  GLU A OE1 
482  O OE2 . GLU A 68  ? 0.96167 1.16081 1.09731 -0.20402 -0.20053 0.07942  75  GLU A OE2 
483  N N   . LEU A 69  ? 0.36305 0.55235 0.56857 -0.04037 -0.08680 0.11202  76  LEU A N   
484  C CA  . LEU A 69  ? 0.32351 0.46820 0.52249 -0.00749 -0.06487 0.09826  76  LEU A CA  
485  C C   . LEU A 69  ? 0.34525 0.49191 0.56552 -0.00369 -0.05402 0.10589  76  LEU A C   
486  O O   . LEU A 69  ? 0.31193 0.51553 0.57085 0.01027  -0.04790 0.12733  76  LEU A O   
487  C CB  . LEU A 69  ? 0.26462 0.43570 0.48058 0.02935  -0.05314 0.10508  76  LEU A CB  
488  C CG  . LEU A 69  ? 0.38996 0.56131 0.58307 0.02999  -0.06085 0.10269  76  LEU A CG  
489  C CD1 . LEU A 69  ? 0.37261 0.56143 0.58304 0.06778  -0.04600 0.11094  76  LEU A CD1 
490  C CD2 . LEU A 69  ? 0.44190 0.54511 0.58809 0.01816  -0.06152 0.07471  76  LEU A CD2 
491  N N   . HIS A 70  ? 0.32725 0.38781 0.50655 0.00078  -0.03404 0.02014  77  HIS A N   
492  C CA  . HIS A 70  ? 0.27720 0.34164 0.45502 -0.00372 -0.02849 0.01597  77  HIS A CA  
493  C C   . HIS A 70  ? 0.35476 0.40333 0.50761 -0.00668 -0.02996 0.00762  77  HIS A C   
494  O O   . HIS A 70  ? 0.37324 0.40861 0.51146 -0.00593 -0.03569 0.00532  77  HIS A O   
495  C CB  . HIS A 70  ? 0.27556 0.35473 0.46285 -0.01192 -0.03448 0.02440  77  HIS A CB  
496  C CG  . HIS A 70  ? 0.37332 0.44635 0.54855 -0.02031 -0.04929 0.02738  77  HIS A CG  
497  N ND1 . HIS A 70  ? 0.36193 0.41471 0.51206 -0.02521 -0.05393 0.02184  77  HIS A ND1 
498  C CD2 . HIS A 70  ? 0.40427 0.48906 0.58822 -0.02464 -0.06032 0.03459  77  HIS A CD2 
499  C CE1 . HIS A 70  ? 0.36506 0.41357 0.50768 -0.03252 -0.06607 0.02394  77  HIS A CE1 
500  N NE2 . HIS A 70  ? 0.40425 0.47327 0.56639 -0.03320 -0.07112 0.03108  77  HIS A NE2 
501  N N   . ILE A 71  ? 0.38263 0.43457 0.53087 -0.00880 -0.02397 0.00433  78  ILE A N   
502  C CA  . ILE A 71  ? 0.36067 0.40238 0.48659 -0.01017 -0.02492 -0.00085 78  ILE A CA  
503  C C   . ILE A 71  ? 0.36670 0.41095 0.48816 -0.01657 -0.02559 0.00544  78  ILE A C   
504  O O   . ILE A 71  ? 0.38264 0.44085 0.51673 -0.01777 -0.01860 0.00874  78  ILE A O   
505  C CB  . ILE A 71  ? 0.33653 0.38123 0.45834 -0.00533 -0.01578 -0.01139 78  ILE A CB  
506  C CG1 . ILE A 71  ? 0.27593 0.31711 0.40771 -0.00072 -0.01240 -0.01736 78  ILE A CG1 
507  C CG2 . ILE A 71  ? 0.30274 0.34140 0.40227 -0.00525 -0.01882 -0.01483 78  ILE A CG2 
508  C CD1 . ILE A 71  ? 0.38118 0.42551 0.51308 0.00151  -0.00249 -0.03027 78  ILE A CD1 
509  N N   . ASN A 72  ? 0.38668 0.41623 0.49083 -0.02026 -0.03239 0.00768  79  ASN A N   
510  C CA  . ASN A 72  ? 0.38070 0.40688 0.47921 -0.02676 -0.03183 0.01447  79  ASN A CA  
511  C C   . ASN A 72  ? 0.42638 0.44403 0.50349 -0.02190 -0.02853 0.01321  79  ASN A C   
512  O O   . ASN A 72  ? 0.39846 0.40570 0.46204 -0.01671 -0.03211 0.00877  79  ASN A O   
513  C CB  . ASN A 72  ? 0.31802 0.33111 0.41457 -0.03590 -0.04153 0.01880  79  ASN A CB  
514  C CG  . ASN A 72  ? 0.44142 0.46971 0.56035 -0.04177 -0.04628 0.02222  79  ASN A CG  
515  O OD1 . ASN A 72  ? 0.35296 0.40186 0.49189 -0.04013 -0.03993 0.02509  79  ASN A OD1 
516  N ND2 . ASN A 72  ? 0.36980 0.38954 0.48507 -0.04796 -0.05731 0.02206  79  ASN A ND2 
517  N N   . LEU A 73  ? 0.36079 0.38541 0.43554 -0.02265 -0.02123 0.01849  80  LEU A N   
518  C CA  . LEU A 73  ? 0.48128 0.50139 0.53563 -0.01709 -0.01794 0.02086  80  LEU A CA  
519  C C   . LEU A 73  ? 0.43082 0.43586 0.47952 -0.02319 -0.01703 0.03249  80  LEU A C   
520  O O   . LEU A 73  ? 0.42585 0.43761 0.48711 -0.03061 -0.01241 0.03929  80  LEU A O   
521  C CB  . LEU A 73  ? 0.40761 0.44853 0.46007 -0.01176 -0.00901 0.01796  80  LEU A CB  
522  C CG  . LEU A 73  ? 0.32136 0.37534 0.38188 -0.00796 -0.00729 0.00475  80  LEU A CG  
523  C CD1 . LEU A 73  ? 0.34221 0.41479 0.39735 -0.00418 0.00222  0.00044  80  LEU A CD1 
524  C CD2 . LEU A 73  ? 0.32638 0.37376 0.37854 -0.00369 -0.01387 -0.00323 80  LEU A CD2 
525  N N   . ILE A 74  ? 0.43075 0.41478 0.46219 -0.02012 -0.02027 0.03502  81  ILE A N   
526  C CA  . ILE A 74  ? 0.45905 0.42006 0.48487 -0.02681 -0.01929 0.04449  81  ILE A CA  
527  C C   . ILE A 74  ? 0.53495 0.48559 0.54018 -0.01672 -0.01384 0.05275  81  ILE A C   
528  O O   . ILE A 74  ? 0.53065 0.46710 0.52210 -0.00877 -0.01721 0.05064  81  ILE A O   
529  C CB  . ILE A 74  ? 0.44787 0.38648 0.47275 -0.03356 -0.02832 0.03933  81  ILE A CB  
530  C CG1 . ILE A 74  ? 0.49681 0.45107 0.54115 -0.04054 -0.03488 0.03256  81  ILE A CG1 
531  C CG2 . ILE A 74  ? 0.50464 0.41706 0.52555 -0.04377 -0.02666 0.04650  81  ILE A CG2 
532  C CD1 . ILE A 74  ? 0.51736 0.45588 0.55682 -0.04405 -0.04492 0.02577  81  ILE A CD1 
533  N N   . PRO A 75  ? 0.46651 0.42554 0.46907 -0.01523 -0.00477 0.06354  82  PRO A N   
534  C CA  . PRO A 75  ? 0.46495 0.41316 0.44792 -0.00481 0.00086  0.07524  82  PRO A CA  
535  C C   . PRO A 75  ? 0.65741 0.57000 0.63676 -0.01138 0.00422  0.08501  82  PRO A C   
536  O O   . PRO A 75  ? 0.58643 0.48961 0.57978 -0.02657 0.00477  0.08578  82  PRO A O   
537  C CB  . PRO A 75  ? 0.54498 0.51840 0.52638 -0.00127 0.00996  0.08334  82  PRO A CB  
538  C CG  . PRO A 75  ? 0.52744 0.51049 0.53045 -0.01465 0.01237  0.08120  82  PRO A CG  
539  C CD  . PRO A 75  ? 0.43130 0.41305 0.44809 -0.02076 0.00194  0.06652  82  PRO A CD  
540  N N   . ASN A 76  ? 0.60361 0.49669 0.56491 0.00020  0.00690  0.09248  83  ASN A N   
541  C CA  . ASN A 76  ? 0.62168 0.47453 0.57651 -0.00388 0.01237  0.10153  83  ASN A CA  
542  C C   . ASN A 76  ? 0.67245 0.51969 0.61019 0.01240  0.02235  0.11951  83  ASN A C   
543  O O   . ASN A 76  ? 0.61399 0.45969 0.53828 0.02848  0.02074  0.12058  83  ASN A O   
544  C CB  . ASN A 76  ? 0.60090 0.42618 0.55037 -0.00530 0.00511  0.08989  83  ASN A CB  
545  C CG  . ASN A 76  ? 0.70063 0.48109 0.64580 -0.01506 0.01029  0.09395  83  ASN A CG  
546  O OD1 . ASN A 76  ? 0.83999 0.59809 0.77467 -0.00791 0.02114  0.10857  83  ASN A OD1 
547  N ND2 . ASN A 76  ? 0.75963 0.52657 0.71262 -0.03169 0.00278  0.08107  83  ASN A ND2 
548  N N   . LYS A 77  ? 0.67583 0.52203 0.61513 0.00892  0.03319  0.13519  84  LYS A N   
549  C CA  . LYS A 77  ? 0.68187 0.52544 0.60444 0.02555  0.04363  0.15562  84  LYS A CA  
550  C C   . LYS A 77  ? 0.69342 0.49185 0.60423 0.03280  0.04917  0.16399  84  LYS A C   
551  O O   . LYS A 77  ? 0.68757 0.48643 0.58285 0.05307  0.05374  0.17729  84  LYS A O   
552  C CB  . LYS A 77  ? 0.71818 0.56929 0.64531 0.01947  0.05576  0.17188  84  LYS A CB  
553  C CG  . LYS A 77  ? 0.72366 0.62263 0.65338 0.02157  0.05460  0.16877  84  LYS A CG  
554  C CD  . LYS A 77  ? 0.89329 0.80126 0.81780 0.02429  0.06941  0.19037  84  LYS A CD  
555  C CE  . LYS A 77  ? 0.84263 0.79386 0.77175 0.02235  0.07020  0.18450  84  LYS A CE  
556  N NZ  . LYS A 77  ? 0.99231 0.94536 0.94763 0.00222  0.07036  0.17517  84  LYS A NZ  
557  N N   . GLN A 78  ? 0.78625 0.54629 0.70385 0.01708  0.04903  0.15621  85  GLN A N   
558  C CA  . GLN A 78  ? 0.78909 0.50036 0.69428 0.02323  0.05610  0.16177  85  GLN A CA  
559  C C   . GLN A 78  ? 0.81094 0.52377 0.70361 0.04161  0.04966  0.15421  85  GLN A C   
560  O O   . GLN A 78  ? 0.91537 0.61497 0.79415 0.06176  0.05750  0.16826  85  GLN A O   
561  C CB  . GLN A 78  ? 0.80919 0.48127 0.72334 -0.00040 0.05557  0.15030  85  GLN A CB  
562  C CG  . GLN A 78  ? 1.06686 0.68448 0.97331 -0.00194 0.07067  0.16322  85  GLN A CG  
563  C CD  . GLN A 78  ? 1.30260 0.91955 1.21863 -0.01064 0.08368  0.18287  85  GLN A CD  
564  O OE1 . GLN A 78  ? 1.40478 1.04569 1.33941 -0.02908 0.08022  0.17910  85  GLN A OE1 
565  N NE2 . GLN A 78  ? 0.99972 0.58987 0.90384 0.00373  0.09991  0.20557  85  GLN A NE2 
566  N N   . ASP A 79  ? 0.71592 0.44585 0.61458 0.03576  0.03633  0.13362  86  ASP A N   
567  C CA  . ASP A 79  ? 0.74573 0.48101 0.63556 0.05146  0.03051  0.12583  86  ASP A CA  
568  C C   . ASP A 79  ? 0.67436 0.45789 0.56324 0.06792  0.02647  0.13061  86  ASP A C   
569  O O   . ASP A 79  ? 0.70012 0.49293 0.58373 0.08236  0.02278  0.12725  86  ASP A O   
570  C CB  . ASP A 79  ? 0.71600 0.45063 0.61235 0.03839  0.01881  0.10327  86  ASP A CB  
571  C CG  . ASP A 79  ? 0.97617 0.66900 0.87305 0.01943  0.01980  0.09526  86  ASP A CG  
572  O OD1 . ASP A 79  ? 1.00093 0.65592 0.89091 0.01850  0.03098  0.10558  86  ASP A OD1 
573  O OD2 . ASP A 79  ? 0.89725 0.59561 0.80164 0.00505  0.00942  0.07881  86  ASP A OD2 
574  N N   . ARG A 80  ? 0.69764 0.51304 0.59158 0.06530  0.02721  0.13737  87  ARG A N   
575  C CA  . ARG A 80  ? 0.70303 0.56685 0.59540 0.07711  0.02199  0.13801  87  ARG A CA  
576  C C   . ARG A 80  ? 0.62112 0.50740 0.52221 0.07359  0.00975  0.11712  87  ARG A C   
577  O O   . ARG A 80  ? 0.59398 0.50383 0.49202 0.08661  0.00505  0.11518  87  ARG A O   
578  C CB  . ARG A 80  ? 0.64619 0.51559 0.52412 0.10084  0.02718  0.15614  87  ARG A CB  
579  C CG  . ARG A 80  ? 0.78378 0.70012 0.65628 0.11027  0.02603  0.16518  87  ARG A CG  
580  C CD  . ARG A 80  ? 0.79366 0.71091 0.65123 0.13296  0.03384  0.18997  87  ARG A CD  
581  N NE  . ARG A 80  ? 0.88495 0.82087 0.74025 0.15031  0.02751  0.18915  87  ARG A NE  
582  C CZ  . ARG A 80  ? 1.00592 0.91455 0.85602 0.16618  0.03382  0.20060  87  ARG A CZ  
583  N NH1 . ARG A 80  ? 1.11088 0.96790 0.95574 0.16647  0.04684  0.21258  87  ARG A NH1 
584  N NH2 . ARG A 80  ? 0.95521 0.88854 0.80644 0.18193  0.02784  0.19980  87  ARG A NH2 
585  N N   . THR A 81  ? 0.56317 0.44330 0.47671 0.05572  0.00490  0.10251  88  THR A N   
586  C CA  . THR A 81  ? 0.54633 0.44516 0.46943 0.05134  -0.00507 0.08439  88  THR A CA  
587  C C   . THR A 81  ? 0.59026 0.51248 0.52765 0.03789  -0.00791 0.07586  88  THR A C   
588  O O   . THR A 81  ? 0.53234 0.44618 0.47576 0.02682  -0.00368 0.08030  88  THR A O   
589  C CB  . THR A 81  ? 0.54171 0.40981 0.46533 0.04538  -0.00870 0.07423  88  THR A CB  
590  O OG1 . THR A 81  ? 0.58382 0.42717 0.51241 0.02895  -0.00725 0.07333  88  THR A OG1 
591  C CG2 . THR A 81  ? 0.51957 0.36306 0.42876 0.06039  -0.00437 0.08067  88  THR A CG2 
592  N N   . LEU A 82  ? 0.51608 0.46716 0.46030 0.03896  -0.01401 0.06381  89  LEU A N   
593  C CA  . LEU A 82  ? 0.46906 0.43802 0.42835 0.02764  -0.01634 0.05297  89  LEU A CA  
594  C C   . LEU A 82  ? 0.47442 0.43921 0.44291 0.02353  -0.02343 0.03956  89  LEU A C   
595  O O   . LEU A 82  ? 0.46389 0.43523 0.42921 0.03146  -0.02680 0.03473  89  LEU A O   
596  C CB  . LEU A 82  ? 0.40678 0.41149 0.36524 0.03207  -0.01523 0.04976  89  LEU A CB  
597  C CG  . LEU A 82  ? 0.38212 0.40478 0.35557 0.02306  -0.01568 0.03690  89  LEU A CG  
598  C CD1 . LEU A 82  ? 0.38310 0.39604 0.36751 0.01230  -0.01108 0.04149  89  LEU A CD1 
599  C CD2 . LEU A 82  ? 0.37945 0.43376 0.34676 0.02786  -0.01358 0.03236  89  LEU A CD2 
600  N N   . THR A 83  ? 0.40932 0.36526 0.38980 0.01158  -0.02545 0.03499  90  THR A N   
601  C CA  . THR A 83  ? 0.45632 0.40630 0.44373 0.00798  -0.03183 0.02506  90  THR A CA  
602  C C   . THR A 83  ? 0.44083 0.41207 0.44608 0.00212  -0.03276 0.01726  90  THR A C   
603  O O   . THR A 83  ? 0.42625 0.40534 0.44144 -0.00460 -0.02959 0.02004  90  THR A O   
604  C CB  . THR A 83  ? 0.48824 0.40924 0.47282 -0.00020 -0.03463 0.02656  90  THR A CB  
605  O OG1 . THR A 83  ? 0.55952 0.45590 0.52646 0.00700  -0.03201 0.03219  90  THR A OG1 
606  C CG2 . THR A 83  ? 0.49863 0.41758 0.48873 -0.00370 -0.04158 0.01733  90  THR A CG2 
607  N N   . ILE A 84  ? 0.39757 0.37752 0.40789 0.00531  -0.03559 0.00842  91  ILE A N   
608  C CA  . ILE A 84  ? 0.41320 0.40822 0.44077 0.00142  -0.03510 0.00104  91  ILE A CA  
609  C C   . ILE A 84  ? 0.41954 0.40332 0.45249 -0.00109 -0.04042 -0.00136 91  ILE A C   
610  O O   . ILE A 84  ? 0.40209 0.37885 0.42786 0.00391  -0.04274 -0.00390 91  ILE A O   
611  C CB  . ILE A 84  ? 0.36030 0.37485 0.39029 0.00627  -0.03230 -0.00753 91  ILE A CB  
612  C CG1 . ILE A 84  ? 0.43353 0.46283 0.45396 0.00954  -0.02825 -0.00547 91  ILE A CG1 
613  C CG2 . ILE A 84  ? 0.36796 0.39199 0.41601 0.00263  -0.02940 -0.01529 91  ILE A CG2 
614  C CD1 . ILE A 84  ? 0.59715 0.62497 0.60082 0.01765  -0.03013 0.00072  91  ILE A CD1 
615  N N   . VAL A 85  ? 0.36141 0.34611 0.40699 -0.00813 -0.04220 0.00048  92  VAL A N   
616  C CA  . VAL A 85  ? 0.36595 0.34341 0.41530 -0.01059 -0.04838 -0.00002 92  VAL A CA  
617  C C   . VAL A 85  ? 0.52044 0.51367 0.58980 -0.00989 -0.04602 -0.00206 92  VAL A C   
618  O O   . VAL A 85  ? 0.46197 0.46840 0.54573 -0.01247 -0.04187 -0.00038 92  VAL A O   
619  C CB  . VAL A 85  ? 0.40807 0.37512 0.45578 -0.01987 -0.05425 0.00476  92  VAL A CB  
620  C CG1 . VAL A 85  ? 0.41421 0.37813 0.46313 -0.02201 -0.06215 0.00367  92  VAL A CG1 
621  C CG2 . VAL A 85  ? 0.46080 0.40655 0.48913 -0.02060 -0.05421 0.00688  92  VAL A CG2 
622  N N   . ASP A 86  ? 0.37202 0.36296 0.44268 -0.00555 -0.04716 -0.00457 93  ASP A N   
623  C CA  . ASP A 86  ? 0.34383 0.34474 0.43321 -0.00379 -0.04454 -0.00396 93  ASP A CA  
624  C C   . ASP A 86  ? 0.41657 0.41167 0.50325 -0.00316 -0.05158 0.00062  93  ASP A C   
625  O O   . ASP A 86  ? 0.37216 0.35408 0.44069 -0.00254 -0.05643 -0.00006 93  ASP A O   
626  C CB  . ASP A 86  ? 0.29809 0.30310 0.39437 0.00124  -0.03619 -0.01099 93  ASP A CB  
627  C CG  . ASP A 86  ? 0.45369 0.44983 0.54011 0.00509  -0.03722 -0.01325 93  ASP A CG  
628  O OD1 . ASP A 86  ? 0.45818 0.45439 0.53487 0.00635  -0.03614 -0.01804 93  ASP A OD1 
629  O OD2 . ASP A 86  ? 0.43421 0.42559 0.52280 0.00756  -0.03882 -0.00908 93  ASP A OD2 
630  N N   . THR A 87  ? 0.37332 0.37922 0.47734 -0.00205 -0.05150 0.00583  94  THR A N   
631  C CA  . THR A 87  ? 0.31623 0.32151 0.41818 0.00015  -0.05806 0.01180  94  THR A CA  
632  C C   . THR A 87  ? 0.37824 0.38268 0.48840 0.00873  -0.05049 0.01327  94  THR A C   
633  O O   . THR A 87  ? 0.32775 0.33871 0.44718 0.01319  -0.05153 0.02161  94  THR A O   
634  C CB  . THR A 87  ? 0.43116 0.45239 0.54713 -0.00393 -0.06468 0.01955  94  THR A CB  
635  O OG1 . THR A 87  ? 0.37281 0.40835 0.51259 -0.00173 -0.05606 0.02163  94  THR A OG1 
636  C CG2 . THR A 87  ? 0.36778 0.38566 0.47283 -0.01499 -0.07362 0.01795  94  THR A CG2 
637  N N   . GLY A 88  ? 0.35240 0.34975 0.46000 0.01089  -0.04265 0.00594  95  GLY A N   
638  C CA  . GLY A 88  ? 0.37147 0.36567 0.48837 0.01661  -0.03389 0.00601  95  GLY A CA  
639  C C   . GLY A 88  ? 0.38445 0.37077 0.48873 0.02083  -0.03665 0.01135  95  GLY A C   
640  O O   . GLY A 88  ? 0.41697 0.40123 0.50519 0.02003  -0.04630 0.01526  95  GLY A O   
641  N N   . ILE A 89  ? 0.34930 0.33080 0.46015 0.02461  -0.02747 0.01085  96  ILE A N   
642  C CA  . ILE A 89  ? 0.45027 0.42571 0.55153 0.02999  -0.02716 0.01824  96  ILE A CA  
643  C C   . ILE A 89  ? 0.46736 0.43626 0.54409 0.02955  -0.03282 0.01458  96  ILE A C   
644  O O   . ILE A 89  ? 0.41104 0.37514 0.47290 0.03412  -0.03495 0.02061  96  ILE A O   
645  C CB  . ILE A 89  ? 0.43313 0.40441 0.55113 0.03278  -0.01366 0.01905  96  ILE A CB  
646  C CG1 . ILE A 89  ? 0.43925 0.40594 0.55090 0.04002  -0.01122 0.03142  96  ILE A CG1 
647  C CG2 . ILE A 89  ? 0.34401 0.31466 0.46307 0.02787  -0.00889 0.00699  96  ILE A CG2 
648  C CD1 . ILE A 89  ? 0.50046 0.46101 0.63145 0.04246  0.00364  0.03528  96  ILE A CD1 
649  N N   . GLY A 90  ? 0.35089 0.31938 0.42177 0.02546  -0.03457 0.00561  97  GLY A N   
650  C CA  . GLY A 90  ? 0.36387 0.32459 0.41300 0.02713  -0.03797 0.00301  97  GLY A CA  
651  C C   . GLY A 90  ? 0.38492 0.34589 0.43574 0.03146  -0.02979 0.00219  97  GLY A C   
652  O O   . GLY A 90  ? 0.44305 0.40924 0.51250 0.03113  -0.02158 0.00255  97  GLY A O   
653  N N   . MET A 91  ? 0.39423 0.34886 0.42629 0.03548  -0.03110 0.00119  98  MET A N   
654  C CA  . MET A 91  ? 0.41308 0.37193 0.44783 0.03995  -0.02341 0.00080  98  MET A CA  
655  C C   . MET A 91  ? 0.48588 0.43395 0.49837 0.04776  -0.02259 0.00562  98  MET A C   
656  O O   . MET A 91  ? 0.49007 0.42548 0.48005 0.04921  -0.02908 0.00453  98  MET A O   
657  C CB  . MET A 91  ? 0.49512 0.46237 0.53199 0.03921  -0.02374 -0.00568 98  MET A CB  
658  C CG  . MET A 91  ? 0.47809 0.46169 0.53897 0.03276  -0.02004 -0.01185 98  MET A CG  
659  S SD  . MET A 91  ? 0.46715 0.46484 0.52633 0.03198  -0.02367 -0.01841 98  MET A SD  
660  C CE  . MET A 91  ? 0.47099 0.45493 0.51335 0.03098  -0.03137 -0.01660 98  MET A CE  
661  N N   . THR A 92  ? 0.50595 0.45810 0.52447 0.05220  -0.01366 0.01045  99  THR A N   
662  C CA  . THR A 92  ? 0.42802 0.37190 0.42533 0.06102  -0.01009 0.01526  99  THR A CA  
663  C C   . THR A 92  ? 0.48778 0.43379 0.47919 0.06696  -0.00618 0.01202  99  THR A C   
664  O O   . THR A 92  ? 0.41445 0.37134 0.41947 0.06415  -0.00694 0.00731  99  THR A O   
665  C CB  . THR A 92  ? 0.47646 0.42488 0.48393 0.06399  -0.00023 0.02440  99  THR A CB  
666  O OG1 . THR A 92  ? 0.50281 0.46510 0.53840 0.06026  0.00854  0.02310  99  THR A OG1 
667  C CG2 . THR A 92  ? 0.42258 0.36906 0.43534 0.06120  -0.00335 0.03045  99  THR A CG2 
668  N N   . LYS A 93  ? 0.45382 0.39079 0.42393 0.07649  -0.00149 0.01519  100 LYS A N   
669  C CA  . LYS A 93  ? 0.53901 0.47930 0.50553 0.08495  0.00443  0.01417  100 LYS A CA  
670  C C   . LYS A 93  ? 0.48910 0.45422 0.48613 0.08389  0.01286  0.01690  100 LYS A C   
671  O O   . LYS A 93  ? 0.56499 0.54411 0.57286 0.08559  0.01323  0.01446  100 LYS A O   
672  C CB  . LYS A 93  ? 0.51143 0.43606 0.44845 0.09647  0.01008  0.01659  100 LYS A CB  
673  C CG  . LYS A 93  ? 0.47286 0.39342 0.39966 0.10744  0.01520  0.01479  100 LYS A CG  
674  C CD  . LYS A 93  ? 0.63151 0.53669 0.52977 0.12007  0.02404  0.01661  100 LYS A CD  
675  C CE  . LYS A 93  ? 0.82548 0.72364 0.71352 0.13325  0.03089  0.01536  100 LYS A CE  
676  N NZ  . LYS A 93  ? 0.85373 0.73607 0.71312 0.14684  0.04191  0.01617  100 LYS A NZ  
677  N N   . ALA A 94  ? 0.41512 0.38701 0.42724 0.08060  0.01962  0.02242  101 ALA A N   
678  C CA  . ALA A 94  ? 0.50487 0.49939 0.54852 0.07644  0.02810  0.02390  101 ALA A CA  
679  C C   . ALA A 94  ? 0.51629 0.52446 0.58336 0.06475  0.02193  0.01523  101 ALA A C   
680  O O   . ALA A 94  ? 0.53406 0.56455 0.62169 0.06174  0.02433  0.01214  101 ALA A O   
681  C CB  . ALA A 94  ? 0.44972 0.44343 0.50403 0.07472  0.03818  0.03267  101 ALA A CB  
682  N N   . ASP A 95  ? 0.44349 0.44106 0.50780 0.05815  0.01406  0.01107  102 ASP A N   
683  C CA  . ASP A 95  ? 0.32532 0.33429 0.40645 0.04839  0.00860  0.00181  102 ASP A CA  
684  C C   . ASP A 95  ? 0.54055 0.56076 0.61524 0.05220  0.00295  -0.00232 102 ASP A C   
685  O O   . ASP A 95  ? 0.44565 0.48843 0.53837 0.04738  0.00259  -0.00765 102 ASP A O   
686  C CB  . ASP A 95  ? 0.39604 0.39125 0.47185 0.04353  0.00193  -0.00039 102 ASP A CB  
687  C CG  . ASP A 95  ? 0.44215 0.43093 0.53151 0.03965  0.00804  0.00397  102 ASP A CG  
688  O OD1 . ASP A 95  ? 0.48635 0.48276 0.59689 0.03563  0.01748  0.00450  102 ASP A OD1 
689  O OD2 . ASP A 95  ? 0.45176 0.42854 0.53208 0.04053  0.00371  0.00754  102 ASP A OD2 
690  N N   . LEU A 96  ? 0.45843 0.46301 0.50701 0.06085  -0.00137 0.00026  103 LEU A N   
691  C CA  . LEU A 96  ? 0.49833 0.50883 0.53895 0.06639  -0.00564 -0.00117 103 LEU A CA  
692  C C   . LEU A 96  ? 0.44422 0.47722 0.49590 0.07378  0.00022  0.00202  103 LEU A C   
693  O O   . LEU A 96  ? 0.52782 0.58151 0.58789 0.07471  -0.00316 0.00038  103 LEU A O   
694  C CB  . LEU A 96  ? 0.43090 0.41428 0.44152 0.07386  -0.00882 0.00110  103 LEU A CB  
695  C CG  . LEU A 96  ? 0.47269 0.43816 0.47357 0.06593  -0.01630 -0.00173 103 LEU A CG  
696  C CD1 . LEU A 96  ? 0.51216 0.45082 0.48414 0.07135  -0.01895 -0.00103 103 LEU A CD1 
697  C CD2 . LEU A 96  ? 0.36363 0.34088 0.37653 0.05825  -0.02170 -0.00610 103 LEU A CD2 
698  N N   . ILE A 97  ? 0.43081 0.46304 0.48308 0.07968  0.00918  0.00763  104 ILE A N   
699  C CA  . ILE A 97  ? 0.50250 0.55653 0.56481 0.08893  0.01604  0.01256  104 ILE A CA  
700  C C   . ILE A 97  ? 0.56599 0.65157 0.66298 0.07879  0.01996  0.01085  104 ILE A C   
701  O O   . ILE A 97  ? 0.62049 0.73670 0.73473 0.08014  0.01933  0.01086  104 ILE A O   
702  C CB  . ILE A 97  ? 0.56712 0.60350 0.60934 0.10231  0.02546  0.01976  104 ILE A CB  
703  C CG1 . ILE A 97  ? 0.55881 0.56396 0.56672 0.11134  0.02162  0.01884  104 ILE A CG1 
704  C CG2 . ILE A 97  ? 0.54606 0.60801 0.60298 0.11248  0.03504  0.02629  104 ILE A CG2 
705  C CD1 . ILE A 97  ? 0.54348 0.52471 0.52502 0.12163  0.02950  0.02208  104 ILE A CD1 
706  N N   . ASN A 98  ? 0.50637 0.58602 0.61533 0.06816  0.02410  0.00959  105 ASN A N   
707  C CA  . ASN A 98  ? 0.57574 0.68038 0.71766 0.05845  0.03120  0.00887  105 ASN A CA  
708  C C   . ASN A 98  ? 0.56013 0.66574 0.72173 0.04076  0.02883  -0.00081 105 ASN A C   
709  O O   . ASN A 98  ? 0.57800 0.70947 0.76234 0.03006  0.02588  -0.00946 105 ASN A O   
710  C CB  . ASN A 98  ? 0.46495 0.56236 0.60768 0.06381  0.04469  0.01935  105 ASN A CB  
711  C CG  . ASN A 98  ? 0.72194 0.84682 0.87904 0.07140  0.05294  0.02587  105 ASN A CG  
712  O OD1 . ASN A 98  ? 0.74889 0.90655 0.93601 0.06273  0.05248  0.02211  105 ASN A OD1 
713  N ND2 . ASN A 98  ? 0.79422 0.90755 0.93009 0.08758  0.06069  0.03521  105 ASN A ND2 
714  N N   . ASN A 99  ? 0.57067 0.53296 0.43845 0.08148  0.04711  0.07227  106 ASN A N   
715  C CA  . ASN A 99  ? 0.75792 0.71289 0.65970 0.05670  0.03970  0.10440  106 ASN A CA  
716  C C   . ASN A 99  ? 0.65395 0.59218 0.61422 0.05246  0.02363  0.09599  106 ASN A C   
717  O O   . ASN A 99  ? 0.72922 0.67762 0.73496 0.03518  0.03026  0.10728  106 ASN A O   
718  C CB  . ASN A 99  ? 0.61859 0.54175 0.47737 0.04801  0.01912  0.12745  106 ASN A CB  
719  C CG  . ASN A 99  ? 0.75293 0.69170 0.53368 0.05092  0.03158  0.13437  106 ASN A CG  
720  O OD1 . ASN A 99  ? 0.69298 0.67193 0.46538 0.04837  0.06552  0.14436  106 ASN A OD1 
721  N ND2 . ASN A 99  ? 0.84072 0.75133 0.56336 0.05354  0.00384  0.13156  106 ASN A ND2 
722  N N   . LEU A 100 ? 0.66095 0.57233 0.61815 0.06591  0.00297  0.07565  107 LEU A N   
723  C CA  . LEU A 100 ? 0.71291 0.61101 0.71513 0.06195  -0.00872 0.06992  107 LEU A CA  
724  C C   . LEU A 100 ? 0.64894 0.58293 0.68635 0.06243  0.00298  0.05934  107 LEU A C   
725  O O   . LEU A 100 ? 0.65035 0.58749 0.72077 0.04718  0.00192  0.06115  107 LEU A O   
726  C CB  . LEU A 100 ? 0.63908 0.50598 0.63309 0.07420  -0.03106 0.05706  107 LEU A CB  
727  C CG  . LEU A 100 ? 0.68974 0.52596 0.66737 0.06924  -0.05132 0.07105  107 LEU A CG  
728  C CD1 . LEU A 100 ? 0.65890 0.47108 0.65115 0.07548  -0.07278 0.06194  107 LEU A CD1 
729  C CD2 . LEU A 100 ? 0.46873 0.29863 0.47501 0.05417  -0.04811 0.09588  107 LEU A CD2 
730  N N   . GLY A 101 ? 0.61806 0.57976 0.65013 0.08017  0.01317  0.04726  108 GLY A N   
731  C CA  . GLY A 101 ? 0.60657 0.61295 0.68134 0.08167  0.02083  0.04380  108 GLY A CA  
732  C C   . GLY A 101 ? 0.69429 0.73950 0.79875 0.05868  0.03645  0.05931  108 GLY A C   
733  O O   . GLY A 101 ? 0.72323 0.79859 0.86949 0.04630  0.03188  0.05924  108 GLY A O   
734  N N   . THR A 102 ? 0.64158 0.68746 0.72464 0.04969  0.05264  0.07515  109 THR A N   
735  C CA  . THR A 102 ? 0.71097 0.78862 0.82833 0.02303  0.06784  0.09586  109 THR A CA  
736  C C   . THR A 102 ? 0.65743 0.70115 0.79954 -0.00381 0.05186  0.09957  109 THR A C   
737  O O   . THR A 102 ? 0.68232 0.74989 0.86913 -0.02769 0.05303  0.10233  109 THR A O   
738  C CB  . THR A 102 ? 0.60683 0.69043 0.68933 0.01945  0.08993  0.11873  109 THR A CB  
739  O OG1 . THR A 102 ? 0.63924 0.75252 0.69116 0.04633  0.11005  0.10713  109 THR A OG1 
740  C CG2 . THR A 102 ? 0.58581 0.70325 0.71241 -0.01111 0.10770  0.14657  109 THR A CG2 
741  N N   . ILE A 103 ? 0.68161 0.66991 0.79901 -0.00044 0.03706  0.09769  110 ILE A N   
742  C CA  . ILE A 103 ? 0.71639 0.66664 0.85776 -0.01970 0.02752  0.09600  110 ILE A CA  
743  C C   . ILE A 103 ? 0.72657 0.68263 0.88360 -0.02087 0.01543  0.06967  110 ILE A C   
744  O O   . ILE A 103 ? 0.83317 0.77689 1.01326 -0.04289 0.01234  0.06005  110 ILE A O   
745  C CB  . ILE A 103 ? 0.64495 0.54324 0.76561 -0.01110 0.01811  0.10543  110 ILE A CB  
746  C CG1 . ILE A 103 ? 0.58395 0.47988 0.68342 -0.01408 0.02533  0.13787  110 ILE A CG1 
747  C CG2 . ILE A 103 ? 0.65126 0.50757 0.80173 -0.02326 0.01386  0.09846  110 ILE A CG2 
748  C CD1 . ILE A 103 ? 0.65964 0.53539 0.79299 -0.03879 0.03308  0.16376  110 ILE A CD1 
749  N N   . ALA A 104 ? 0.64078 0.61263 0.78233 0.00149  0.00769  0.05777  111 ALA A N   
750  C CA  . ALA A 104 ? 0.67178 0.65343 0.82052 0.00145  -0.00544 0.04047  111 ALA A CA  
751  C C   . ALA A 104 ? 0.76123 0.79893 0.94139 -0.01173 -0.00813 0.03863  111 ALA A C   
752  O O   . ALA A 104 ? 0.76872 0.82141 0.95170 -0.01632 -0.02343 0.02756  111 ALA A O   
753  C CB  . ALA A 104 ? 0.45656 0.43260 0.58496 0.02906  -0.01426 0.03636  111 ALA A CB  
754  N N   . LYS A 105 ? 0.72791 0.80247 0.93288 -0.01899 0.00572  0.05243  112 LYS A N   
755  C CA  . LYS A 105 ? 0.55194 0.69120 0.80211 -0.03219 0.00203  0.05507  112 LYS A CA  
756  C C   . LYS A 105 ? 0.64428 0.77715 0.91024 -0.06823 -0.01504 0.04228  112 LYS A C   
757  O O   . LYS A 105 ? 0.70455 0.86696 0.97798 -0.07410 -0.03628 0.03206  112 LYS A O   
758  C CB  . LYS A 105 ? 0.61903 0.80117 0.89908 -0.03677 0.02639  0.07566  112 LYS A CB  
759  C CG  . LYS A 105 ? 0.69227 0.92660 0.98486 -0.00372 0.04058  0.08059  112 LYS A CG  
760  C CD  . LYS A 105 ? 0.72798 0.98615 1.01961 0.00058  0.07557  0.09841  112 LYS A CD  
761  C CE  . LYS A 105 ? 0.74880 1.05019 1.09539 -0.03675 0.08497  0.11884  112 LYS A CE  
762  N NZ  . LYS A 105 ? 0.65657 1.03822 1.07233 -0.03559 0.08018  0.12091  112 LYS A NZ  
763  N N   . SER A 106 ? 0.64411 0.73408 0.91208 -0.09273 -0.00754 0.04224  113 SER A N   
764  C CA  . SER A 106 ? 0.62209 0.69370 0.90402 -0.12938 -0.02129 0.02312  113 SER A CA  
765  C C   . SER A 106 ? 0.62616 0.66516 0.86623 -0.12456 -0.03675 -0.00568 113 SER A C   
766  O O   . SER A 106 ? 0.54387 0.59591 0.78290 -0.14898 -0.05601 -0.02685 113 SER A O   
767  C CB  . SER A 106 ? 0.77727 0.79394 1.07176 -0.14977 -0.00688 0.03050  113 SER A CB  
768  O OG  . SER A 106 ? 0.80320 0.79853 1.07799 -0.12383 0.01088  0.05404  113 SER A OG  
769  N N   . GLY A 107 ? 0.66430 0.66348 0.86822 -0.09580 -0.02875 -0.00623 114 GLY A N   
770  C CA  . GLY A 107 ? 0.58656 0.56036 0.75217 -0.09011 -0.03655 -0.02874 114 GLY A CA  
771  C C   . GLY A 107 ? 0.53799 0.56441 0.69101 -0.08329 -0.05657 -0.02872 114 GLY A C   
772  O O   . GLY A 107 ? 0.59197 0.61931 0.71635 -0.09680 -0.06985 -0.04847 114 GLY A O   
773  N N   . THR A 108 ? 0.54250 0.61253 0.71512 -0.06138 -0.05853 -0.00607 115 THR A N   
774  C CA  . THR A 108 ? 0.49290 0.61323 0.66630 -0.05044 -0.07876 0.00180  115 THR A CA  
775  C C   . THR A 108 ? 0.43555 0.60948 0.63308 -0.08117 -0.10172 -0.00295 115 THR A C   
776  O O   . THR A 108 ? 0.47230 0.66886 0.64680 -0.08881 -0.12576 -0.00753 115 THR A O   
777  C CB  . THR A 108 ? 0.47415 0.62221 0.67321 -0.01723 -0.07172 0.02371  115 THR A CB  
778  O OG1 . THR A 108 ? 0.63444 0.73061 0.80771 0.00548  -0.05628 0.02467  115 THR A OG1 
779  C CG2 . THR A 108 ? 0.45379 0.64520 0.66194 -0.00103 -0.09275 0.03662  115 THR A CG2 
780  N N   . LYS A 109 ? 0.49520 0.69407 0.73975 -0.10155 -0.09658 0.00131  116 LYS A N   
781  C CA  . LYS A 109 ? 0.44960 0.69991 0.72703 -0.13826 -0.12180 -0.00376 116 LYS A CA  
782  C C   . LYS A 109 ? 0.47544 0.68465 0.70454 -0.17105 -0.13830 -0.03850 116 LYS A C   
783  O O   . LYS A 109 ? 0.59010 0.83684 0.80441 -0.18975 -0.17049 -0.04716 116 LYS A O   
784  C CB  . LYS A 109 ? 0.49982 0.77350 0.83916 -0.15954 -0.10781 0.00803  116 LYS A CB  
785  C CG  . LYS A 109 ? 0.45661 0.78787 0.84637 -0.13121 -0.08894 0.03920  116 LYS A CG  
786  C CD  . LYS A 109 ? 0.60908 1.02281 1.07943 -0.15982 -0.09864 0.05488  116 LYS A CD  
787  C CE  . LYS A 109 ? 0.67733 1.16006 1.20395 -0.12706 -0.07499 0.08428  116 LYS A CE  
788  N NZ  . LYS A 109 ? 0.48066 1.05298 1.06539 -0.11870 -0.10144 0.09917  116 LYS A NZ  
789  N N   . ALA A 110 ? 0.57173 0.70381 0.77461 -0.17746 -0.11662 -0.05921 117 ALA A N   
790  C CA  . ALA A 110 ? 0.61832 0.70242 0.77564 -0.20567 -0.12452 -0.09968 117 ALA A CA  
791  C C   . ALA A 110 ? 0.61030 0.69052 0.69881 -0.18912 -0.13187 -0.11093 117 ALA A C   
792  O O   . ALA A 110 ? 0.62022 0.70443 0.66434 -0.21475 -0.15272 -0.13899 117 ALA A O   
793  C CB  . ALA A 110 ? 0.54952 0.55025 0.70747 -0.20842 -0.09525 -0.11507 117 ALA A CB  
794  N N   . PHE A 111 ? 0.52954 0.60238 0.60552 -0.14912 -0.11560 -0.08881 118 PHE A N   
795  C CA  . PHE A 111 ? 0.51933 0.59274 0.53681 -0.13429 -0.11996 -0.09041 118 PHE A CA  
796  C C   . PHE A 111 ? 0.54045 0.68471 0.54812 -0.14399 -0.15732 -0.07694 118 PHE A C   
797  O O   . PHE A 111 ? 0.68103 0.83008 0.62610 -0.15258 -0.16985 -0.08813 118 PHE A O   
798  C CB  . PHE A 111 ? 0.47294 0.53001 0.49463 -0.09362 -0.10029 -0.06368 118 PHE A CB  
799  C CG  . PHE A 111 ? 0.55465 0.61188 0.52523 -0.07983 -0.10107 -0.05777 118 PHE A CG  
800  C CD1 . PHE A 111 ? 0.54891 0.57930 0.46046 -0.09469 -0.09201 -0.08733 118 PHE A CD1 
801  C CD2 . PHE A 111 ? 0.54891 0.63137 0.53068 -0.05235 -0.10826 -0.02251 118 PHE A CD2 
802  C CE1 . PHE A 111 ? 0.61102 0.64769 0.47317 -0.08346 -0.08807 -0.07692 118 PHE A CE1 
803  C CE2 . PHE A 111 ? 0.57401 0.65692 0.51349 -0.04264 -0.10828 -0.00974 118 PHE A CE2 
804  C CZ  . PHE A 111 ? 0.69082 0.75502 0.56920 -0.05878 -0.09726 -0.03439 118 PHE A CZ  
805  N N   . MET A 112 ? 0.55788 0.76177 0.62747 -0.14215 -0.17471 -0.05059 119 MET A N   
806  C CA  . MET A 112 ? 0.69420 0.97347 0.77070 -0.14964 -0.21434 -0.03131 119 MET A CA  
807  C C   . MET A 112 ? 0.59772 0.90278 0.66318 -0.19909 -0.24651 -0.05827 119 MET A C   
808  O O   . MET A 112 ? 0.83413 1.18784 0.86897 -0.21319 -0.28421 -0.05248 119 MET A O   
809  C CB  . MET A 112 ? 0.54189 0.87936 0.69983 -0.12435 -0.21754 0.00711  119 MET A CB  
810  C CG  . MET A 112 ? 0.63324 0.96039 0.78801 -0.07843 -0.20527 0.03499  119 MET A CG  
811  S SD  . MET A 112 ? 0.67871 1.03230 0.91696 -0.04089 -0.18494 0.06135  119 MET A SD  
812  C CE  . MET A 112 ? 0.54418 0.92873 0.79036 -0.00450 -0.20643 0.09864  119 MET A CE  
813  N N   . GLU A 113 ? 0.73537 1.00804 0.82535 -0.22801 -0.23566 -0.08579 120 GLU A N   
814  C CA  . GLU A 113 ? 0.80325 1.07729 0.87045 -0.27992 -0.26483 -0.12317 120 GLU A CA  
815  C C   . GLU A 113 ? 0.80515 1.02471 0.76616 -0.28874 -0.26179 -0.16407 120 GLU A C   
816  O O   . GLU A 113 ? 1.04653 1.29063 0.95578 -0.31704 -0.29638 -0.18377 120 GLU A O   
817  C CB  . GLU A 113 ? 0.88799 1.12391 1.00848 -0.30818 -0.24924 -0.14223 120 GLU A CB  
818  C CG  . GLU A 113 ? 0.82016 1.11865 1.04380 -0.30708 -0.24934 -0.10295 120 GLU A CG  
819  C CD  . GLU A 113 ? 1.05502 1.30498 1.32594 -0.32815 -0.22333 -0.11126 120 GLU A CD  
820  O OE1 . GLU A 113 ? 1.12932 1.29494 1.35981 -0.34575 -0.21099 -0.14984 120 GLU A OE1 
821  O OE2 . GLU A 113 ? 0.93106 1.22700 1.28109 -0.32566 -0.21274 -0.07724 120 GLU A OE2 
822  N N   . ALA A 114 ? 0.84342 0.99080 0.77215 -0.26113 -0.21810 -0.17547 121 ALA A N   
823  C CA  . ALA A 114 ? 0.98261 1.08026 0.81640 -0.26399 -0.20393 -0.21381 121 ALA A CA  
824  C C   . ALA A 114 ? 1.02615 1.17443 0.79596 -0.25260 -0.22437 -0.19142 121 ALA A C   
825  O O   . ALA A 114 ? 1.12801 1.26815 0.80801 -0.27283 -0.23260 -0.22380 121 ALA A O   
826  C CB  . ALA A 114 ? 0.90435 0.92748 0.73915 -0.23198 -0.15193 -0.22032 121 ALA A CB  
827  N N   . LEU A 115 ? 0.97663 1.17449 0.78843 -0.22057 -0.23183 -0.13625 122 LEU A N   
828  C CA  . LEU A 115 ? 0.91138 1.15635 0.67432 -0.20812 -0.25295 -0.10380 122 LEU A CA  
829  C C   . LEU A 115 ? 1.00432 1.31587 0.73662 -0.24434 -0.30824 -0.10484 122 LEU A C   
830  O O   . LEU A 115 ? 0.98809 1.32774 0.67184 -0.23263 -0.32294 -0.07830 122 LEU A O   
831  C CB  . LEU A 115 ? 0.74132 1.01662 0.57121 -0.16603 -0.25059 -0.04612 122 LEU A CB  
832  C CG  . LEU A 115 ? 0.74017 0.95795 0.57082 -0.12994 -0.20533 -0.03725 122 LEU A CG  
833  C CD1 . LEU A 115 ? 0.70712 0.94846 0.60057 -0.09225 -0.20751 0.01270  122 LEU A CD1 
834  C CD2 . LEU A 115 ? 0.81034 1.00234 0.55177 -0.13004 -0.18801 -0.04710 122 LEU A CD2 
835  N N   . GLN A 116 ? 1.06503 1.38345 0.84310 -0.27193 -0.32619 -0.12753 123 GLN A N   
836  C CA  . GLN A 116 ? 1.16069 1.51477 0.92159 -0.29413 -0.36579 -0.13403 123 GLN A CA  
837  C C   . GLN A 116 ? 1.10172 1.39743 0.80604 -0.32916 -0.36284 -0.19918 123 GLN A C   
838  O O   . GLN A 116 ? 1.27270 1.59143 0.95280 -0.35197 -0.39837 -0.21297 123 GLN A O   
839  C CB  . GLN A 116 ? 1.18958 1.61130 1.06035 -0.29629 -0.39489 -0.10176 123 GLN A CB  
840  C CG  . GLN A 116 ? 1.11859 1.59439 1.05233 -0.25486 -0.39602 -0.03958 123 GLN A CG  
841  C CD  . GLN A 116 ? 1.27527 1.81381 1.32398 -0.25219 -0.41164 -0.01299 123 GLN A CD  
842  O OE1 . GLN A 116 ? 1.36856 1.91401 1.45531 -0.28451 -0.42177 -0.03735 123 GLN A OE1 
843  N NE2 . GLN A 116 ? 1.17678 1.75819 1.28455 -0.21215 -0.41016 0.03644  123 GLN A NE2 
844  N N   . ALA A 117 ? 1.31418 1.53169 1.00078 -0.33161 -0.32153 -0.23973 124 ALA A N   
845  C CA  . ALA A 117 ? 1.34659 1.49312 0.98481 -0.35556 -0.31065 -0.30290 124 ALA A CA  
846  C C   . ALA A 117 ? 1.53356 1.63282 1.06073 -0.34228 -0.27881 -0.33300 124 ALA A C   
847  O O   . ALA A 117 ? 1.56757 1.59420 1.05763 -0.35033 -0.25460 -0.38708 124 ALA A O   
848  C CB  . ALA A 117 ? 1.34470 1.42870 1.05225 -0.36272 -0.28229 -0.32534 124 ALA A CB  
849  N N   . GLY A 118 ? 1.54615 1.68518 1.02622 -0.31944 -0.27581 -0.29584 125 GLY A N   
850  C CA  . GLY A 118 ? 1.57732 1.68299 0.95710 -0.30508 -0.24060 -0.31569 125 GLY A CA  
851  C C   . GLY A 118 ? 1.42069 1.51704 0.80476 -0.27340 -0.19812 -0.28834 125 GLY A C   
852  O O   . GLY A 118 ? 1.34685 1.46217 0.66704 -0.25670 -0.18440 -0.26521 125 GLY A O   
853  N N   . ALA A 119 ? 1.31225 1.38037 0.77313 -0.26609 -0.17801 -0.28793 126 ALA A N   
854  C CA  . ALA A 119 ? 1.31438 1.35571 0.80362 -0.22493 -0.13129 -0.26175 126 ALA A CA  
855  C C   . ALA A 119 ? 1.19080 1.29182 0.68966 -0.19889 -0.14564 -0.19287 126 ALA A C   
856  O O   . ALA A 119 ? 1.19761 1.36129 0.71667 -0.20689 -0.19212 -0.15773 126 ALA A O   
857  C CB  . ALA A 119 ? 1.10955 1.11102 0.70413 -0.21044 -0.11308 -0.25740 126 ALA A CB  
858  N N   . ASP A 120 ? 1.10269 1.18331 0.59594 -0.16730 -0.10523 -0.17194 127 ASP A N   
859  C CA  . ASP A 120 ? 1.07827 1.19853 0.58937 -0.14122 -0.11207 -0.10687 127 ASP A CA  
860  C C   . ASP A 120 ? 0.90232 0.99366 0.50780 -0.10831 -0.08876 -0.08089 127 ASP A C   
861  O O   . ASP A 120 ? 0.92914 0.97712 0.58234 -0.10565 -0.06972 -0.10784 127 ASP A O   
862  C CB  . ASP A 120 ? 1.11943 1.24763 0.54142 -0.13755 -0.08815 -0.09733 127 ASP A CB  
863  C CG  . ASP A 120 ? 1.14282 1.21495 0.55074 -0.12536 -0.02732 -0.13324 127 ASP A CG  
864  O OD1 . ASP A 120 ? 1.26054 1.28392 0.69549 -0.13039 -0.01030 -0.18218 127 ASP A OD1 
865  O OD2 . ASP A 120 ? 1.18598 1.26462 0.56431 -0.11001 0.00433  -0.10845 127 ASP A OD2 
866  N N   . ILE A 121 ? 0.94081 1.05442 0.57036 -0.08462 -0.09247 -0.02662 128 ILE A N   
867  C CA  . ILE A 121 ? 0.77284 0.86427 0.48725 -0.05643 -0.08125 -0.00070 128 ILE A CA  
868  C C   . ILE A 121 ? 0.76901 0.80816 0.49789 -0.04458 -0.03566 -0.02075 128 ILE A C   
869  O O   . ILE A 121 ? 0.73621 0.74694 0.52928 -0.03122 -0.02755 -0.02131 128 ILE A O   
870  C CB  . ILE A 121 ? 0.77564 0.89561 0.50897 -0.03688 -0.09774 0.05839  128 ILE A CB  
871  C CG1 . ILE A 121 ? 0.81614 0.98452 0.57790 -0.03834 -0.14329 0.08198  128 ILE A CG1 
872  C CG2 . ILE A 121 ? 0.67063 0.75557 0.47009 -0.01044 -0.07851 0.07860  128 ILE A CG2 
873  C CD1 . ILE A 121 ? 0.84866 1.04371 0.62752 -0.01925 -0.16310 0.14127  128 ILE A CD1 
874  N N   . SER A 122 ? 0.81083 0.84033 0.48117 -0.04892 -0.00476 -0.03700 129 SER A N   
875  C CA  . SER A 122 ? 0.73154 0.72087 0.42756 -0.03398 0.04069  -0.05040 129 SER A CA  
876  C C   . SER A 122 ? 0.80894 0.75317 0.54280 -0.03612 0.05286  -0.09251 129 SER A C   
877  O O   . SER A 122 ? 0.75102 0.66330 0.52766 -0.01985 0.08448  -0.09660 129 SER A O   
878  C CB  . SER A 122 ? 0.81890 0.81335 0.44166 -0.03803 0.07708  -0.06444 129 SER A CB  
879  O OG  . SER A 122 ? 0.91584 0.89499 0.47412 -0.05880 0.08299  -0.12184 129 SER A OG  
880  N N   . MET A 123 ? 0.82912 0.77197 0.55530 -0.05664 0.02760  -0.11932 130 MET A N   
881  C CA  . MET A 123 ? 0.82241 0.71960 0.58835 -0.06184 0.03734  -0.15310 130 MET A CA  
882  C C   . MET A 123 ? 0.71091 0.60741 0.55303 -0.05196 0.01961  -0.12524 130 MET A C   
883  O O   . MET A 123 ? 0.72175 0.58883 0.59840 -0.06033 0.02018  -0.14321 130 MET A O   
884  C CB  . MET A 123 ? 0.78849 0.68034 0.50840 -0.09492 0.02101  -0.19882 130 MET A CB  
885  C CG  . MET A 123 ? 0.95568 0.81202 0.61097 -0.10267 0.05456  -0.25011 130 MET A CG  
886  S SD  . MET A 123 ? 1.21749 1.08114 0.79079 -0.14814 0.02260  -0.30192 130 MET A SD  
887  C CE  . MET A 123 ? 1.19892 1.01259 0.85085 -0.16543 0.01240  -0.32731 130 MET A CE  
888  N N   . ILE A 124 ? 0.67538 0.60071 0.54156 -0.03480 0.00559  -0.08204 131 ILE A N   
889  C CA  . ILE A 124 ? 0.61850 0.54720 0.54263 -0.02486 -0.01059 -0.05933 131 ILE A CA  
890  C C   . ILE A 124 ? 0.65706 0.54188 0.62612 -0.01446 0.00976  -0.06350 131 ILE A C   
891  O O   . ILE A 124 ? 0.56673 0.44539 0.57038 -0.01641 0.00120  -0.05948 131 ILE A O   
892  C CB  . ILE A 124 ? 0.59097 0.54734 0.52723 -0.00612 -0.02532 -0.01866 131 ILE A CB  
893  C CG1 . ILE A 124 ? 0.56818 0.53485 0.55041 0.00336  -0.04306 -0.00269 131 ILE A CG1 
894  C CG2 . ILE A 124 ? 0.56528 0.50110 0.51191 0.01099  -0.00386 -0.00194 131 ILE A CG2 
895  C CD1 . ILE A 124 ? 0.47051 0.46045 0.46524 0.02125  -0.06009 0.03031  131 ILE A CD1 
896  N N   . GLY A 125 ? 0.63774 0.49620 0.60947 -0.00343 0.03753  -0.06834 132 GLY A N   
897  C CA  . GLY A 125 ? 0.69636 0.51878 0.71859 0.00851  0.05241  -0.06509 132 GLY A CA  
898  C C   . GLY A 125 ? 0.68344 0.47128 0.71932 -0.00489 0.05838  -0.09149 132 GLY A C   
899  O O   . GLY A 125 ? 0.68602 0.45178 0.76606 0.00089  0.05771  -0.07818 132 GLY A O   
900  N N   . GLN A 126 ? 0.68108 0.46184 0.67794 -0.02518 0.06197  -0.12778 133 GLN A N   
901  C CA  . GLN A 126 ? 0.78659 0.52625 0.80026 -0.04240 0.06633  -0.15560 133 GLN A CA  
902  C C   . GLN A 126 ? 0.65826 0.41394 0.69784 -0.05880 0.03990  -0.13970 133 GLN A C   
903  O O   . GLN A 126 ? 0.70337 0.42487 0.76837 -0.07548 0.04199  -0.15334 133 GLN A O   
904  C CB  . GLN A 126 ? 0.76491 0.48981 0.72351 -0.06403 0.07381  -0.20508 133 GLN A CB  
905  C CG  . GLN A 126 ? 0.82559 0.53049 0.75516 -0.04801 0.11053  -0.22809 133 GLN A CG  
906  C CD  . GLN A 126 ? 1.20498 0.89322 1.06361 -0.07142 0.11767  -0.28383 133 GLN A CD  
907  O OE1 . GLN A 126 ? 1.19590 0.91870 0.98517 -0.07567 0.11783  -0.29078 133 GLN A OE1 
908  N NE2 . GLN A 126 ? 1.27020 0.90313 1.14246 -0.08908 0.12170  -0.32347 133 GLN A NE2 
909  N N   . PHE A 127 ? 0.59620 0.40183 0.63429 -0.05415 0.01812  -0.11088 134 PHE A N   
910  C CA  . PHE A 127 ? 0.65872 0.48883 0.72584 -0.06473 0.00019  -0.09294 134 PHE A CA  
911  C C   . PHE A 127 ? 0.56813 0.40332 0.66331 -0.04170 0.00076  -0.05740 134 PHE A C   
912  O O   . PHE A 127 ? 0.60230 0.46565 0.71470 -0.04456 -0.00912 -0.04006 134 PHE A O   
913  C CB  . PHE A 127 ? 0.64298 0.53111 0.69090 -0.07788 -0.02504 -0.09213 134 PHE A CB  
914  C CG  . PHE A 127 ? 0.64602 0.53520 0.65646 -0.10603 -0.03394 -0.12784 134 PHE A CG  
915  C CD1 . PHE A 127 ? 0.60016 0.48733 0.55525 -0.10197 -0.02856 -0.14424 134 PHE A CD1 
916  C CD2 . PHE A 127 ? 0.59352 0.48622 0.62134 -0.13945 -0.04784 -0.14524 134 PHE A CD2 
917  C CE1 . PHE A 127 ? 0.65958 0.54708 0.56510 -0.12969 -0.03790 -0.18139 134 PHE A CE1 
918  C CE2 . PHE A 127 ? 0.69091 0.58150 0.67828 -0.16977 -0.06128 -0.18352 134 PHE A CE2 
919  C CZ  . PHE A 127 ? 0.72269 0.60977 0.64269 -0.16436 -0.05669 -0.20378 134 PHE A CZ  
920  N N   . GLY A 128 ? 0.61281 0.42436 0.71278 -0.02004 0.01239  -0.04730 135 GLY A N   
921  C CA  . GLY A 128 ? 0.59530 0.40734 0.71486 -0.00225 0.00806  -0.01794 135 GLY A CA  
922  C C   . GLY A 128 ? 0.64795 0.49709 0.75486 0.00957  -0.00725 -0.00311 135 GLY A C   
923  O O   . GLY A 128 ? 0.54040 0.39228 0.65456 0.01940  -0.01268 0.01405  135 GLY A O   
924  N N   . VAL A 129 ? 0.49793 0.37345 0.58394 0.00954  -0.01444 -0.00907 136 VAL A N   
925  C CA  . VAL A 129 ? 0.52236 0.42738 0.60567 0.02369  -0.02872 0.00638  136 VAL A CA  
926  C C   . VAL A 129 ? 0.49063 0.39363 0.56095 0.03461  -0.03029 0.01424  136 VAL A C   
927  O O   . VAL A 129 ? 0.43570 0.36225 0.50138 0.04275  -0.04304 0.02611  136 VAL A O   
928  C CB  . VAL A 129 ? 0.56872 0.51833 0.65387 0.01416  -0.04085 0.00427  136 VAL A CB  
929  C CG1 . VAL A 129 ? 0.54454 0.50362 0.65293 0.00630  -0.03649 0.00606  136 VAL A CG1 
930  C CG2 . VAL A 129 ? 0.51674 0.47768 0.58030 -0.00728 -0.04499 -0.01346 136 VAL A CG2 
931  N N   . GLY A 130 ? 0.32275 0.45448 0.45383 -0.07020 -0.09293 -0.03911 137 GLY A N   
932  C CA  . GLY A 130 ? 0.39348 0.51810 0.50604 -0.05952 -0.09111 -0.04179 137 GLY A CA  
933  C C   . GLY A 130 ? 0.41831 0.53731 0.52106 -0.04913 -0.08056 -0.03280 137 GLY A C   
934  O O   . GLY A 130 ? 0.38236 0.49908 0.46968 -0.04155 -0.07960 -0.03114 137 GLY A O   
935  N N   . PHE A 131 ? 0.33806 0.45221 0.44655 -0.04912 -0.07302 -0.02690 138 PHE A N   
936  C CA  . PHE A 131 ? 0.39944 0.50282 0.49633 -0.03921 -0.06417 -0.02070 138 PHE A CA  
937  C C   . PHE A 131 ? 0.32109 0.43523 0.41317 -0.02688 -0.06566 -0.01517 138 PHE A C   
938  O O   . PHE A 131 ? 0.33730 0.43385 0.41056 -0.01910 -0.06235 -0.01155 138 PHE A O   
939  C CB  . PHE A 131 ? 0.30172 0.40309 0.40545 -0.03963 -0.05694 -0.01649 138 PHE A CB  
940  C CG  . PHE A 131 ? 0.35191 0.44519 0.44504 -0.02717 -0.04965 -0.01154 138 PHE A CG  
941  C CD1 . PHE A 131 ? 0.33138 0.39880 0.40696 -0.02580 -0.04530 -0.01282 138 PHE A CD1 
942  C CD2 . PHE A 131 ? 0.34135 0.45367 0.44197 -0.01647 -0.04799 -0.00697 138 PHE A CD2 
943  C CE1 . PHE A 131 ? 0.37706 0.43030 0.44004 -0.01533 -0.04024 -0.00953 138 PHE A CE1 
944  C CE2 . PHE A 131 ? 0.33791 0.43783 0.42582 -0.00208 -0.04280 -0.00440 138 PHE A CE2 
945  C CZ  . PHE A 131 ? 0.41138 0.47799 0.47904 -0.00212 -0.03935 -0.00562 138 PHE A CZ  
946  N N   . TYR A 132 ? 0.31624 0.45860 0.42446 -0.02512 -0.07143 -0.01426 139 TYR A N   
947  C CA  . TYR A 132 ? 0.31090 0.46677 0.41585 -0.00927 -0.07443 -0.00936 139 TYR A CA  
948  C C   . TYR A 132 ? 0.34338 0.49162 0.42903 -0.00448 -0.08140 -0.00931 139 TYR A C   
949  O O   . TYR A 132 ? 0.38750 0.53829 0.46303 0.01095  -0.08502 -0.00379 139 TYR A O   
950  C CB  . TYR A 132 ? 0.29593 0.49294 0.42730 -0.00927 -0.07906 -0.00975 139 TYR A CB  
951  C CG  . TYR A 132 ? 0.39069 0.59803 0.53809 -0.01459 -0.07012 -0.00777 139 TYR A CG  
952  C CD1 . TYR A 132 ? 0.37233 0.58103 0.51672 0.00086  -0.06211 -0.00372 139 TYR A CD1 
953  C CD2 . TYR A 132 ? 0.38083 0.59280 0.54243 -0.03463 -0.06987 -0.00991 139 TYR A CD2 
954  C CE1 . TYR A 132 ? 0.27357 0.49438 0.42965 -0.00359 -0.05288 -0.00205 139 TYR A CE1 
955  C CE2 . TYR A 132 ? 0.33687 0.55696 0.50872 -0.04079 -0.06097 -0.00597 139 TYR A CE2 
956  C CZ  . TYR A 132 ? 0.45645 0.68385 0.62584 -0.02531 -0.05185 -0.00215 139 TYR A CZ  
957  O OH  . TYR A 132 ? 0.60679 0.84551 0.78394 -0.03110 -0.04211 0.00159  139 TYR A OH  
958  N N   . SER A 133 ? 0.34421 0.48283 0.42213 -0.01561 -0.08344 -0.01530 140 SER A N   
959  C CA  . SER A 133 ? 0.30481 0.43545 0.35951 -0.01210 -0.08724 -0.01450 140 SER A CA  
960  C C   . SER A 133 ? 0.35360 0.45362 0.38266 -0.00711 -0.07912 -0.00628 140 SER A C   
961  O O   . SER A 133 ? 0.42675 0.51722 0.43197 -0.00426 -0.08093 -0.00174 140 SER A O   
962  C CB  . SER A 133 ? 0.35650 0.48823 0.40953 -0.02407 -0.09017 -0.02519 140 SER A CB  
963  O OG  . SER A 133 ? 0.35150 0.46484 0.40216 -0.03165 -0.08160 -0.02852 140 SER A OG  
964  N N   . ALA A 134 ? 0.37459 0.45798 0.40608 -0.00742 -0.07061 -0.00412 141 ALA A N   
965  C CA  . ALA A 134 ? 0.40745 0.45861 0.41497 -0.00384 -0.06427 0.00320  141 ALA A CA  
966  C C   . ALA A 134 ? 0.45908 0.50090 0.44945 0.01328  -0.06954 0.01277  141 ALA A C   
967  O O   . ALA A 134 ? 0.46752 0.47844 0.42913 0.01446  -0.06783 0.02061  141 ALA A O   
968  C CB  . ALA A 134 ? 0.39561 0.43388 0.41043 -0.00503 -0.05653 0.00176  141 ALA A CB  
969  N N   . TYR A 135 ? 0.38555 0.45373 0.39240 0.02646  -0.07652 0.01247  142 TYR A N   
970  C CA  . TYR A 135 ? 0.46338 0.52668 0.45563 0.04765  -0.08376 0.02024  142 TYR A CA  
971  C C   . TYR A 135 ? 0.46499 0.53141 0.43843 0.05012  -0.09304 0.02454  142 TYR A C   
972  O O   . TYR A 135 ? 0.54248 0.60445 0.50064 0.06950  -0.10149 0.03174  142 TYR A O   
973  C CB  . TYR A 135 ? 0.36366 0.46351 0.38386 0.06188  -0.08758 0.01678  142 TYR A CB  
974  C CG  . TYR A 135 ? 0.45044 0.54111 0.47848 0.06536  -0.07805 0.01497  142 TYR A CG  
975  C CD1 . TYR A 135 ? 0.37160 0.47491 0.42076 0.04882  -0.07028 0.00893  142 TYR A CD1 
976  C CD2 . TYR A 135 ? 0.38653 0.45111 0.39641 0.08597  -0.07756 0.01908  142 TYR A CD2 
977  C CE1 . TYR A 135 ? 0.43493 0.53030 0.48758 0.05216  -0.06162 0.00735  142 TYR A CE1 
978  C CE2 . TYR A 135 ? 0.40606 0.46197 0.42027 0.09002  -0.06909 0.01550  142 TYR A CE2 
979  C CZ  . TYR A 135 ? 0.37366 0.44714 0.40932 0.07263  -0.06076 0.00982  142 TYR A CZ  
980  O OH  . TYR A 135 ? 0.45794 0.52429 0.49498 0.07703  -0.05252 0.00633  142 TYR A OH  
981  N N   . LEU A 136 ? 0.43536 0.50940 0.40748 0.03312  -0.09233 0.01974  143 LEU A N   
982  C CA  . LEU A 136 ? 0.50834 0.57910 0.45386 0.03420  -0.09866 0.02466  143 LEU A CA  
983  C C   . LEU A 136 ? 0.46611 0.49153 0.37251 0.03389  -0.09304 0.03767  143 LEU A C   
984  O O   . LEU A 136 ? 0.50648 0.51894 0.38305 0.04305  -0.09972 0.04797  143 LEU A O   
985  C CB  . LEU A 136 ? 0.53583 0.62610 0.48800 0.01716  -0.09810 0.01401  143 LEU A CB  
986  C CG  . LEU A 136 ? 0.47222 0.60149 0.45463 0.01422  -0.10704 0.00112  143 LEU A CG  
987  C CD1 . LEU A 136 ? 0.47270 0.60777 0.45607 -0.00140 -0.10497 -0.01067 143 LEU A CD1 
988  C CD2 . LEU A 136 ? 0.40213 0.55505 0.38128 0.02790  -0.12163 0.00270  143 LEU A CD2 
989  N N   . VAL A 137 ? 0.44443 0.44422 0.34878 0.02239  -0.08159 0.03786  144 VAL A N   
990  C CA  . VAL A 137 ? 0.54845 0.50405 0.41708 0.01551  -0.07541 0.04944  144 VAL A CA  
991  C C   . VAL A 137 ? 0.61217 0.53096 0.47452 0.02323  -0.07257 0.05370  144 VAL A C   
992  O O   . VAL A 137 ? 0.66551 0.53938 0.49438 0.01943  -0.07020 0.06472  144 VAL A O   
993  C CB  . VAL A 137 ? 0.51810 0.47642 0.38456 -0.00953 -0.06432 0.04484  144 VAL A CB  
994  C CG1 . VAL A 137 ? 0.51900 0.51062 0.38576 -0.01462 -0.06729 0.03933  144 VAL A CG1 
995  C CG2 . VAL A 137 ? 0.51170 0.48087 0.40896 -0.01822 -0.05741 0.03249  144 VAL A CG2 
996  N N   . ALA A 138 ? 0.51610 0.45065 0.40697 0.03298  -0.07272 0.04533  145 ALA A N   
997  C CA  . ALA A 138 ? 0.52833 0.43145 0.41430 0.04069  -0.06932 0.04580  145 ALA A CA  
998  C C   . ALA A 138 ? 0.62797 0.53456 0.51597 0.07030  -0.07830 0.04746  145 ALA A C   
999  O O   . ALA A 138 ? 0.67009 0.62246 0.58608 0.07996  -0.08308 0.04171  145 ALA A O   
1000 C CB  . ALA A 138 ? 0.48338 0.40301 0.39772 0.02918  -0.06079 0.03414  145 ALA A CB  
1001 N N   . GLU A 139 ? 0.69049 0.54911 0.54881 0.08461  -0.08111 0.05453  146 GLU A N   
1002 C CA  . GLU A 139 ? 0.60969 0.47074 0.47086 0.11655  -0.08877 0.05297  146 GLU A CA  
1003 C C   . GLU A 139 ? 0.62236 0.49480 0.50665 0.12104  -0.08148 0.04143  146 GLU A C   
1004 O O   . GLU A 139 ? 0.60088 0.50117 0.50221 0.14510  -0.08505 0.03603  146 GLU A O   
1005 C CB  . GLU A 139 ? 0.71168 0.51054 0.52713 0.13406  -0.09689 0.06457  146 GLU A CB  
1006 C CG  . GLU A 139 ? 0.76712 0.50360 0.55397 0.11825  -0.09020 0.06744  146 GLU A CG  
1007 C CD  . GLU A 139 ? 1.20087 0.86726 0.93651 0.12996  -0.09922 0.08163  146 GLU A CD  
1008 O OE1 . GLU A 139 ? 1.27669 0.93512 0.98954 0.12796  -0.10509 0.09477  146 GLU A OE1 
1009 O OE2 . GLU A 139 ? 1.22600 0.84220 0.94122 0.14108  -0.10101 0.07972  146 GLU A OE2 
1010 N N   . LYS A 140 ? 0.59427 0.45013 0.47945 0.09883  -0.07141 0.03715  147 LYS A N   
1011 C CA  . LYS A 140 ? 0.57205 0.43754 0.47519 0.10098  -0.06425 0.02651  147 LYS A CA  
1012 C C   . LYS A 140 ? 0.53708 0.41313 0.45461 0.07136  -0.05506 0.02162  147 LYS A C   
1013 O O   . LYS A 140 ? 0.56701 0.41877 0.46846 0.05116  -0.05291 0.02554  147 LYS A O   
1014 C CB  . LYS A 140 ? 0.63451 0.44550 0.50836 0.11590  -0.06549 0.02540  147 LYS A CB  
1015 C CG  . LYS A 140 ? 0.54487 0.36189 0.43136 0.11766  -0.05792 0.01338  147 LYS A CG  
1016 C CD  . LYS A 140 ? 0.59896 0.36605 0.45636 0.14074  -0.06196 0.00964  147 LYS A CD  
1017 C CE  . LYS A 140 ? 0.83414 0.55447 0.67198 0.12120  -0.05755 0.00504  147 LYS A CE  
1018 N NZ  . LYS A 140 ? 0.76169 0.41238 0.55930 0.13715  -0.06480 0.00443  147 LYS A NZ  
1019 N N   . VAL A 141 ? 0.43601 0.35016 0.38316 0.06921  -0.04983 0.01344  148 VAL A N   
1020 C CA  . VAL A 141 ? 0.40361 0.32908 0.36490 0.04585  -0.04294 0.00815  148 VAL A CA  
1021 C C   . VAL A 141 ? 0.43962 0.36052 0.40420 0.04983  -0.03711 0.00069  148 VAL A C   
1022 O O   . VAL A 141 ? 0.53450 0.47768 0.51081 0.06671  -0.03601 -0.00218 148 VAL A O   
1023 C CB  . VAL A 141 ? 0.43346 0.40600 0.42382 0.03683  -0.04359 0.00649  148 VAL A CB  
1024 C CG1 . VAL A 141 ? 0.35287 0.33113 0.35406 0.01657  -0.03833 0.00086  148 VAL A CG1 
1025 C CG2 . VAL A 141 ? 0.37836 0.35701 0.36322 0.03474  -0.05035 0.01200  148 VAL A CG2 
1026 N N   . THR A 142 ? 0.40525 0.30112 0.35934 0.03439  -0.03338 -0.00306 149 THR A N   
1027 C CA  . THR A 142 ? 0.42115 0.31260 0.37596 0.03543  -0.02866 -0.01117 149 THR A CA  
1028 C C   . THR A 142 ? 0.47156 0.38518 0.44361 0.01615  -0.02522 -0.01501 149 THR A C   
1029 O O   . THR A 142 ? 0.47785 0.38806 0.44930 -0.00086 -0.02598 -0.01441 149 THR A O   
1030 C CB  . THR A 142 ? 0.46354 0.30398 0.38913 0.03484  -0.02969 -0.01420 149 THR A CB  
1031 O OG1 . THR A 142 ? 0.60051 0.41158 0.50526 0.05365  -0.03505 -0.00946 149 THR A OG1 
1032 C CG2 . THR A 142 ? 0.54486 0.38199 0.46878 0.04003  -0.02617 -0.02434 149 THR A CG2 
1033 N N   . VAL A 143 ? 0.44211 0.37919 0.42803 0.01976  -0.02155 -0.01875 150 VAL A N   
1034 C CA  . VAL A 143 ? 0.40284 0.35685 0.40193 0.00499  -0.01996 -0.02156 150 VAL A CA  
1035 C C   . VAL A 143 ? 0.48718 0.43082 0.47707 0.00695  -0.01685 -0.02826 150 VAL A C   
1036 O O   . VAL A 143 ? 0.47033 0.42279 0.45929 0.02032  -0.01316 -0.02929 150 VAL A O   
1037 C CB  . VAL A 143 ? 0.38783 0.37817 0.40967 0.00388  -0.01968 -0.01764 150 VAL A CB  
1038 C CG1 . VAL A 143 ? 0.31100 0.30887 0.34080 -0.00936 -0.01986 -0.02006 150 VAL A CG1 
1039 C CG2 . VAL A 143 ? 0.33533 0.33646 0.36490 0.00231  -0.02440 -0.01307 150 VAL A CG2 
1040 N N   . ILE A 144 ? 0.45008 0.37869 0.43299 -0.00586 -0.01841 -0.03373 151 ILE A N   
1041 C CA  . ILE A 144 ? 0.49822 0.42039 0.47297 -0.00623 -0.01751 -0.04131 151 ILE A CA  
1042 C C   . ILE A 144 ? 0.48992 0.43453 0.47848 -0.01495 -0.01870 -0.04141 151 ILE A C   
1043 O O   . ILE A 144 ? 0.50956 0.46048 0.50712 -0.02599 -0.02198 -0.04169 151 ILE A O   
1044 C CB  . ILE A 144 ? 0.49102 0.38220 0.44858 -0.01509 -0.02030 -0.04869 151 ILE A CB  
1045 C CG1 . ILE A 144 ? 0.56585 0.42659 0.50770 -0.01084 -0.02126 -0.04543 151 ILE A CG1 
1046 C CG2 . ILE A 144 ? 0.58210 0.46323 0.52667 -0.01034 -0.02045 -0.05808 151 ILE A CG2 
1047 C CD1 . ILE A 144 ? 0.59507 0.44078 0.52338 0.01080  -0.02024 -0.04721 151 ILE A CD1 
1048 N N   . THR A 145 ? 0.37788 0.33379 0.36595 -0.00899 -0.01627 -0.04111 152 THR A N   
1049 C CA  . THR A 145 ? 0.46847 0.43992 0.46602 -0.01552 -0.01859 -0.03863 152 THR A CA  
1050 C C   . THR A 145 ? 0.48520 0.45570 0.47017 -0.01152 -0.01796 -0.04169 152 THR A C   
1051 O O   . THR A 145 ? 0.41809 0.38670 0.39134 -0.00161 -0.01293 -0.04307 152 THR A O   
1052 C CB  . THR A 145 ? 0.38834 0.37974 0.40116 -0.01589 -0.01668 -0.02891 152 THR A CB  
1053 O OG1 . THR A 145 ? 0.40742 0.40365 0.42679 -0.02390 -0.02152 -0.02689 152 THR A OG1 
1054 C CG2 . THR A 145 ? 0.40307 0.40846 0.41394 -0.00679 -0.00928 -0.02394 152 THR A CG2 
1055 N N   . LYS A 146 ? 0.39679 0.36920 0.38260 -0.01736 -0.02386 -0.04359 153 LYS A N   
1056 C CA  . LYS A 146 ? 0.45212 0.42322 0.42345 -0.01351 -0.02561 -0.04607 153 LYS A CA  
1057 C C   . LYS A 146 ? 0.48797 0.46516 0.46328 -0.01658 -0.03044 -0.03901 153 LYS A C   
1058 O O   . LYS A 146 ? 0.39419 0.37130 0.37885 -0.02106 -0.03794 -0.04227 153 LYS A O   
1059 C CB  . LYS A 146 ? 0.43947 0.40036 0.40182 -0.01570 -0.03166 -0.05932 153 LYS A CB  
1060 C CG  . LYS A 146 ? 0.50128 0.46226 0.44707 -0.01066 -0.03578 -0.06349 153 LYS A CG  
1061 C CD  . LYS A 146 ? 0.51598 0.47703 0.44529 -0.00062 -0.02780 -0.05942 153 LYS A CD  
1062 C CE  . LYS A 146 ? 0.54147 0.50092 0.44913 0.00491  -0.03231 -0.06548 153 LYS A CE  
1063 N NZ  . LYS A 146 ? 0.56354 0.52998 0.46718 0.00507  -0.03650 -0.05551 153 LYS A NZ  
1064 N N   . HIS A 147 ? 0.52997 0.43797 0.45807 -0.00603 -0.10578 -0.01618 154 HIS A N   
1065 C CA  . HIS A 147 ? 0.46671 0.38285 0.40933 -0.00573 -0.11160 -0.00152 154 HIS A CA  
1066 C C   . HIS A 147 ? 0.51983 0.43425 0.43289 0.00009  -0.11898 0.00227  154 HIS A C   
1067 O O   . HIS A 147 ? 0.57240 0.48178 0.45004 0.00734  -0.11474 -0.00299 154 HIS A O   
1068 C CB  . HIS A 147 ? 0.58853 0.51219 0.54578 -0.00463 -0.10034 0.01809  154 HIS A CB  
1069 C CG  . HIS A 147 ? 0.48095 0.40616 0.46088 -0.00794 -0.10968 0.03571  154 HIS A CG  
1070 N ND1 . HIS A 147 ? 0.55455 0.48175 0.51857 -0.00473 -0.11187 0.05461  154 HIS A ND1 
1071 C CD2 . HIS A 147 ? 0.54235 0.46403 0.55846 -0.01324 -0.11953 0.03765  154 HIS A CD2 
1072 C CE1 . HIS A 147 ? 0.56418 0.48615 0.55654 -0.00986 -0.12323 0.06987  154 HIS A CE1 
1073 N NE2 . HIS A 147 ? 0.51826 0.43490 0.54270 -0.01447 -0.12915 0.05783  154 HIS A NE2 
1074 N N   . ASN A 148 ? 0.54075 0.45802 0.46648 -0.00061 -0.13215 0.00993  155 ASN A N   
1075 C CA  . ASN A 148 ? 0.55978 0.47683 0.45760 0.00567  -0.14243 0.01446  155 ASN A CA  
1076 C C   . ASN A 148 ? 0.58443 0.50579 0.44836 0.01474  -0.12977 0.03255  155 ASN A C   
1077 O O   . ASN A 148 ? 0.61278 0.53419 0.43762 0.02370  -0.13452 0.02968  155 ASN A O   
1078 C CB  . ASN A 148 ? 0.57474 0.49287 0.49533 0.00575  -0.15889 0.02394  155 ASN A CB  
1079 C CG  . ASN A 148 ? 0.56909 0.49295 0.50888 0.00359  -0.17453 0.00359  155 ASN A CG  
1080 O OD1 . ASN A 148 ? 0.62128 0.54890 0.55078 -0.00010 -0.17669 -0.01369 155 ASN A OD1 
1081 N ND2 . ASN A 148 ? 0.50842 0.43405 0.47817 0.00644  -0.18683 0.00628  155 ASN A ND2 
1082 N N   . ASP A 149 ? 0.56361 0.49296 0.44199 0.01341  -0.11417 0.05141  156 ASP A N   
1083 C CA  . ASP A 149 ? 0.67593 0.62114 0.52934 0.02184  -0.09910 0.07504  156 ASP A CA  
1084 C C   . ASP A 149 ? 0.69339 0.64736 0.52450 0.03189  -0.07987 0.06589  156 ASP A C   
1085 O O   . ASP A 149 ? 0.68386 0.66074 0.50093 0.04052  -0.06265 0.08641  156 ASP A O   
1086 C CB  . ASP A 149 ? 0.60803 0.56255 0.49740 0.01251  -0.09524 0.10781  156 ASP A CB  
1087 C CG  . ASP A 149 ? 0.68966 0.62983 0.59947 0.00617  -0.11671 0.11841  156 ASP A CG  
1088 O OD1 . ASP A 149 ? 0.75830 0.68945 0.65039 0.01148  -0.13207 0.10411  156 ASP A OD1 
1089 O OD2 . ASP A 149 ? 0.72948 0.66648 0.67525 -0.00374 -0.12046 0.14092  156 ASP A OD2 
1090 N N   . ASP A 150 ? 0.57870 0.51699 0.40730 0.03196  -0.08240 0.03758  157 ASP A N   
1091 C CA  . ASP A 150 ? 0.63484 0.57538 0.44502 0.04370  -0.06713 0.02745  157 ASP A CA  
1092 C C   . ASP A 150 ? 0.61049 0.52328 0.39913 0.04585  -0.07928 -0.00449 157 ASP A C   
1093 O O   . ASP A 150 ? 0.67768 0.57659 0.47080 0.03579  -0.09760 -0.01614 157 ASP A O   
1094 C CB  . ASP A 150 ? 0.62583 0.57708 0.47650 0.03689  -0.05488 0.03679  157 ASP A CB  
1095 C CG  . ASP A 150 ? 0.72697 0.70026 0.56419 0.05295  -0.03353 0.04406  157 ASP A CG  
1096 O OD1 . ASP A 150 ? 0.70360 0.67534 0.49573 0.07228  -0.02896 0.03167  157 ASP A OD1 
1097 O OD2 . ASP A 150 ? 0.55072 0.54484 0.42319 0.04778  -0.02264 0.06110  157 ASP A OD2 
1098 N N   . GLU A 151 ? 0.64500 0.55053 0.41267 0.05925  -0.07022 -0.01754 158 GLU A N   
1099 C CA  . GLU A 151 ? 0.67738 0.54975 0.42812 0.05982  -0.08349 -0.04571 158 GLU A CA  
1100 C C   . GLU A 151 ? 0.65601 0.51774 0.44628 0.04316  -0.08524 -0.04882 158 GLU A C   
1101 O O   . GLU A 151 ? 0.60586 0.48576 0.43152 0.03542  -0.07582 -0.03333 158 GLU A O   
1102 C CB  . GLU A 151 ? 0.67793 0.54130 0.38710 0.08516  -0.07592 -0.06002 158 GLU A CB  
1103 C CG  . GLU A 151 ? 0.88013 0.74256 0.53565 0.10460  -0.08223 -0.07008 158 GLU A CG  
1104 C CD  . GLU A 151 ? 1.29151 1.17285 0.91159 0.13607  -0.06262 -0.07050 158 GLU A CD  
1105 O OE1 . GLU A 151 ? 1.34364 1.26571 0.95549 0.14542  -0.04559 -0.04664 158 GLU A OE1 
1106 O OE2 . GLU A 151 ? 1.12384 0.98118 0.72586 0.15220  -0.06417 -0.09305 158 GLU A OE2 
1107 N N   . GLN A 152 ? 0.60800 0.43962 0.39126 0.03744  -0.09906 -0.06835 159 GLN A N   
1108 C CA  . GLN A 152 ? 0.62789 0.45026 0.44208 0.02309  -0.09998 -0.06916 159 GLN A CA  
1109 C C   . GLN A 152 ? 0.61005 0.42736 0.42103 0.03695  -0.08626 -0.06860 159 GLN A C   
1110 O O   . GLN A 152 ? 0.62662 0.42633 0.40445 0.05607  -0.08565 -0.08074 159 GLN A O   
1111 C CB  . GLN A 152 ? 0.70103 0.49477 0.51223 0.00920  -0.12015 -0.08450 159 GLN A CB  
1112 C CG  . GLN A 152 ? 0.65348 0.44881 0.50027 -0.01004 -0.12113 -0.07873 159 GLN A CG  
1113 C CD  . GLN A 152 ? 0.67454 0.45865 0.53065 -0.03014 -0.14057 -0.08552 159 GLN A CD  
1114 O OE1 . GLN A 152 ? 0.69695 0.49851 0.56127 -0.03774 -0.14981 -0.08594 159 GLN A OE1 
1115 N NE2 . GLN A 152 ? 0.70033 0.45687 0.55865 -0.03969 -0.14795 -0.08853 159 GLN A NE2 
1116 N N   . TYR A 153 ? 0.56403 0.39725 0.40840 0.02995  -0.07705 -0.05647 160 TYR A N   
1117 C CA  . TYR A 153 ? 0.54897 0.38494 0.39662 0.04331  -0.06457 -0.05323 160 TYR A CA  
1118 C C   . TYR A 153 ? 0.58562 0.40915 0.45455 0.03162  -0.06894 -0.05310 160 TYR A C   
1119 O O   . TYR A 153 ? 0.55705 0.38543 0.44650 0.01308  -0.07575 -0.05000 160 TYR A O   
1120 C CB  . TYR A 153 ? 0.52497 0.40011 0.39358 0.04842  -0.04882 -0.03456 160 TYR A CB  
1121 C CG  . TYR A 153 ? 0.61416 0.50714 0.45782 0.06543  -0.03880 -0.02949 160 TYR A CG  
1122 C CD1 . TYR A 153 ? 0.59039 0.50389 0.43851 0.05865  -0.03812 -0.01507 160 TYR A CD1 
1123 C CD2 . TYR A 153 ? 0.60052 0.49169 0.41484 0.09059  -0.02999 -0.03806 160 TYR A CD2 
1124 C CE1 . TYR A 153 ? 0.61932 0.55390 0.44192 0.07417  -0.02758 -0.00595 160 TYR A CE1 
1125 C CE2 . TYR A 153 ? 0.76329 0.67905 0.55114 0.10921  -0.01833 -0.03247 160 TYR A CE2 
1126 C CZ  . TYR A 153 ? 0.69507 0.63406 0.48667 0.09971  -0.01642 -0.01461 160 TYR A CZ  
1127 O OH  . TYR A 153 ? 0.88856 0.85638 0.65124 0.11811  -0.00356 -0.00474 160 TYR A OH  
1128 N N   . ALA A 154 ? 0.60840 0.41884 0.47085 0.04517  -0.06464 -0.05578 161 ALA A N   
1129 C CA  . ALA A 154 ? 0.57765 0.37666 0.45605 0.03753  -0.06801 -0.05220 161 ALA A CA  
1130 C C   . ALA A 154 ? 0.52365 0.34808 0.42015 0.04992  -0.05558 -0.04239 161 ALA A C   
1131 O O   . ALA A 154 ? 0.66802 0.49429 0.55265 0.07185  -0.04784 -0.04509 161 ALA A O   
1132 C CB  . ALA A 154 ? 0.58512 0.33644 0.44050 0.04106  -0.08043 -0.06354 161 ALA A CB  
1133 N N   . TRP A 155 ? 0.49715 0.34417 0.42263 0.03756  -0.05480 -0.03237 162 TRP A N   
1134 C CA  . TRP A 155 ? 0.46826 0.33925 0.41610 0.04505  -0.04839 -0.02352 162 TRP A CA  
1135 C C   . TRP A 155 ? 0.59254 0.44662 0.54072 0.04284  -0.05491 -0.02238 162 TRP A C   
1136 O O   . TRP A 155 ? 0.58653 0.42866 0.53236 0.02735  -0.06237 -0.02235 162 TRP A O   
1137 C CB  . TRP A 155 ? 0.43241 0.33613 0.41016 0.03356  -0.04797 -0.01536 162 TRP A CB  
1138 C CG  . TRP A 155 ? 0.43974 0.37015 0.44650 0.03688  -0.04650 -0.00709 162 TRP A CG  
1139 C CD1 . TRP A 155 ? 0.42985 0.39017 0.45934 0.04158  -0.03989 0.00314  162 TRP A CD1 
1140 C CD2 . TRP A 155 ? 0.40463 0.33786 0.42279 0.03410  -0.05370 -0.00704 162 TRP A CD2 
1141 N NE1 . TRP A 155 ? 0.39209 0.37138 0.44941 0.04087  -0.04489 0.00772  162 TRP A NE1 
1142 C CE2 . TRP A 155 ? 0.39163 0.35386 0.43926 0.03802  -0.05368 0.00019  162 TRP A CE2 
1143 C CE3 . TRP A 155 ? 0.46175 0.37918 0.46805 0.02846  -0.06032 -0.01036 162 TRP A CE3 
1144 C CZ2 . TRP A 155 ? 0.41225 0.38479 0.47427 0.03847  -0.06242 0.00030  162 TRP A CZ2 
1145 C CZ3 . TRP A 155 ? 0.40255 0.33284 0.41996 0.03010  -0.06596 -0.00780 162 TRP A CZ3 
1146 C CH2 . TRP A 155 ? 0.43964 0.39556 0.48295 0.03605  -0.06812 -0.00445 162 TRP A CH2 
1147 N N   . GLU A 156 ? 0.48381 0.34079 0.43572 0.05891  -0.05186 -0.01920 163 GLU A N   
1148 C CA  . GLU A 156 ? 0.51355 0.35281 0.46272 0.05910  -0.05898 -0.01507 163 GLU A CA  
1149 C C   . GLU A 156 ? 0.55329 0.41824 0.52174 0.07333  -0.05630 -0.00848 163 GLU A C   
1150 O O   . GLU A 156 ? 0.50262 0.38655 0.47922 0.08995  -0.04836 -0.00886 163 GLU A O   
1151 C CB  . GLU A 156 ? 0.61164 0.40212 0.53286 0.06693  -0.06580 -0.02100 163 GLU A CB  
1152 C CG  . GLU A 156 ? 0.63114 0.39568 0.54761 0.05716  -0.07600 -0.01168 163 GLU A CG  
1153 C CD  . GLU A 156 ? 0.90069 0.60845 0.79291 0.06097  -0.08755 -0.01651 163 GLU A CD  
1154 O OE1 . GLU A 156 ? 0.98014 0.66620 0.86149 0.08546  -0.08971 -0.02213 163 GLU A OE1 
1155 O OE2 . GLU A 156 ? 0.85758 0.54252 0.74379 0.03993  -0.09622 -0.01510 163 GLU A OE2 
1156 N N   . SER A 157 ? 0.54739 0.41755 0.52321 0.06765  -0.06305 -0.00160 164 SER A N   
1157 C CA  . SER A 157 ? 0.53443 0.42548 0.52644 0.08202  -0.06475 0.00409  164 SER A CA  
1158 C C   . SER A 157 ? 0.49781 0.37603 0.47990 0.07967  -0.07430 0.01199  164 SER A C   
1159 O O   . SER A 157 ? 0.55338 0.43150 0.52906 0.06310  -0.07755 0.01458  164 SER A O   
1160 C CB  . SER A 157 ? 0.45397 0.39009 0.47909 0.07740  -0.06400 0.00552  164 SER A CB  
1161 O OG  . SER A 157 ? 0.44432 0.40272 0.48807 0.08968  -0.06905 0.01075  164 SER A OG  
1162 N N   . SER A 158 ? 0.49539 0.42071 0.52497 0.09545  -0.02459 -0.01118 165 SER A N   
1163 C CA  . SER A 158 ? 0.50191 0.42749 0.53364 0.09998  -0.02901 0.00415  165 SER A CA  
1164 C C   . SER A 158 ? 0.48385 0.43646 0.51910 0.10111  -0.03891 0.01448  165 SER A C   
1165 O O   . SER A 158 ? 0.51783 0.47743 0.56055 0.10880  -0.04257 0.02899  165 SER A O   
1166 C CB  . SER A 158 ? 0.47453 0.38472 0.52149 0.11234  -0.02123 0.01037  165 SER A CB  
1167 O OG  . SER A 158 ? 0.64646 0.52887 0.69117 0.10951  -0.01432 0.00062  165 SER A OG  
1168 N N   . ALA A 159 ? 0.51262 0.48108 0.54430 0.09310  -0.04402 0.00813  166 ALA A N   
1169 C CA  . ALA A 159 ? 0.49401 0.48881 0.53285 0.09152  -0.05510 0.01609  166 ALA A CA  
1170 C C   . ALA A 159 ? 0.46757 0.47742 0.53246 0.10429  -0.05170 0.02621  166 ALA A C   
1171 O O   . ALA A 159 ? 0.56332 0.56435 0.63795 0.11280  -0.03912 0.02138  166 ALA A O   
1172 C CB  . ALA A 159 ? 0.43989 0.43616 0.46229 0.08712  -0.06684 0.02375  166 ALA A CB  
1173 N N   . GLY A 160 ? 0.43996 0.47253 0.51600 0.10623  -0.06276 0.04048  167 GLY A N   
1174 C CA  . GLY A 160 ? 0.44335 0.49525 0.54839 0.11849  -0.05935 0.05287  167 GLY A CA  
1175 C C   . GLY A 160 ? 0.43104 0.50206 0.55322 0.11777  -0.05584 0.04982  167 GLY A C   
1176 O O   . GLY A 160 ? 0.49642 0.58270 0.64412 0.13020  -0.04882 0.06007  167 GLY A O   
1177 N N   . GLY A 161 ? 0.47978 0.55094 0.59025 0.10486  -0.05892 0.03778  168 GLY A N   
1178 C CA  . GLY A 161 ? 0.48143 0.57409 0.60960 0.10299  -0.05671 0.03780  168 GLY A CA  
1179 C C   . GLY A 161 ? 0.46915 0.55105 0.59362 0.10796  -0.03980 0.02546  168 GLY A C   
1180 O O   . GLY A 161 ? 0.46907 0.57016 0.60788 0.10786  -0.03598 0.02700  168 GLY A O   
1181 N N   . SER A 162 ? 0.45356 0.50638 0.55957 0.11190  -0.03020 0.01397  169 SER A N   
1182 C CA  . SER A 162 ? 0.51133 0.55302 0.60979 0.11618  -0.01611 0.00084  169 SER A CA  
1183 C C   . SER A 162 ? 0.48145 0.49571 0.55346 0.10680  -0.01598 -0.01417 169 SER A C   
1184 O O   . SER A 162 ? 0.47198 0.47142 0.53378 0.10173  -0.02235 -0.01326 169 SER A O   
1185 C CB  . SER A 162 ? 0.44373 0.47805 0.55240 0.13490  -0.00148 0.00234  169 SER A CB  
1186 O OG  . SER A 162 ? 0.48927 0.49676 0.59080 0.13951  0.00024  0.00069  169 SER A OG  
1187 N N   . PHE A 163 ? 0.41879 0.42903 0.48070 0.10484  -0.00856 -0.02621 170 PHE A N   
1188 C CA  . PHE A 163 ? 0.43374 0.42048 0.47399 0.09694  -0.00754 -0.03982 170 PHE A CA  
1189 C C   . PHE A 163 ? 0.44862 0.42738 0.48066 0.10393  0.00395  -0.05213 170 PHE A C   
1190 O O   . PHE A 163 ? 0.45502 0.44939 0.49603 0.11416  0.01203  -0.04978 170 PHE A O   
1191 C CB  . PHE A 163 ? 0.40568 0.39903 0.43686 0.08170  -0.01534 -0.04123 170 PHE A CB  
1192 C CG  . PHE A 163 ? 0.42945 0.44556 0.46676 0.07908  -0.01323 -0.04078 170 PHE A CG  
1193 C CD1 . PHE A 163 ? 0.37793 0.41816 0.43345 0.07805  -0.01848 -0.02955 170 PHE A CD1 
1194 C CD2 . PHE A 163 ? 0.42202 0.43654 0.44817 0.07696  -0.00688 -0.05027 170 PHE A CD2 
1195 C CE1 . PHE A 163 ? 0.44086 0.50234 0.50621 0.07530  -0.01596 -0.02692 170 PHE A CE1 
1196 C CE2 . PHE A 163 ? 0.37215 0.40920 0.40533 0.07547  -0.00381 -0.04725 170 PHE A CE2 
1197 C CZ  . PHE A 163 ? 0.36129 0.42134 0.41546 0.07474  -0.00766 -0.03512 170 PHE A CZ  
1198 N N   . THR A 164 ? 0.43835 0.39284 0.45291 0.09863  0.00449  -0.06477 171 THR A N   
1199 C CA  . THR A 164 ? 0.45749 0.40021 0.45776 0.10322  0.01268  -0.07948 171 THR A CA  
1200 C C   . THR A 164 ? 0.48427 0.42752 0.46862 0.08956  0.00805  -0.08775 171 THR A C   
1201 O O   . THR A 164 ? 0.48787 0.42875 0.47124 0.07728  -0.00010 -0.08430 171 THR A O   
1202 C CB  . THR A 164 ? 0.48721 0.39665 0.48183 0.10954  0.01663  -0.08871 171 THR A CB  
1203 O OG1 . THR A 164 ? 0.51548 0.40698 0.50703 0.09739  0.00807  -0.08907 171 THR A OG1 
1204 C CG2 . THR A 164 ? 0.49808 0.40672 0.51043 0.12503  0.02304  -0.07874 171 THR A CG2 
1205 N N   . VAL A 165 ? 0.46010 0.40741 0.43151 0.09304  0.01414  -0.09755 172 VAL A N   
1206 C CA  . VAL A 165 ? 0.45756 0.40615 0.41287 0.08170  0.01010  -0.10544 172 VAL A CA  
1207 C C   . VAL A 165 ? 0.52408 0.45373 0.45779 0.08694  0.01451  -0.12302 172 VAL A C   
1208 O O   . VAL A 165 ? 0.54594 0.47494 0.47514 0.10190  0.02493  -0.12750 172 VAL A O   
1209 C CB  . VAL A 165 ? 0.47987 0.46039 0.43986 0.07917  0.01162  -0.09698 172 VAL A CB  
1210 C CG1 . VAL A 165 ? 0.47066 0.45443 0.41451 0.06923  0.00838  -0.10344 172 VAL A CG1 
1211 C CG2 . VAL A 165 ? 0.40761 0.40165 0.38625 0.07243  0.00568  -0.08249 172 VAL A CG2 
1212 N N   . ARG A 166 ? 0.59038 0.50397 0.51062 0.07483  0.00649  -0.13286 173 ARG A N   
1213 C CA  . ARG A 166 ? 0.60086 0.49482 0.49688 0.07641  0.00702  -0.15189 173 ARG A CA  
1214 C C   . ARG A 166 ? 0.59483 0.49263 0.47965 0.05981  -0.00396 -0.15595 173 ARG A C   
1215 O O   . ARG A 166 ? 0.57905 0.48676 0.47739 0.04784  -0.01090 -0.14433 173 ARG A O   
1216 C CB  . ARG A 166 ? 0.63529 0.49172 0.53059 0.07998  0.00708  -0.16220 173 ARG A CB  
1217 C CG  . ARG A 166 ? 0.65471 0.49792 0.56598 0.06683  -0.00276 -0.15488 173 ARG A CG  
1218 C CD  . ARG A 166 ? 0.79894 0.60316 0.70566 0.06381  -0.00642 -0.16834 173 ARG A CD  
1219 N NE  . ARG A 166 ? 1.08644 0.88015 1.01462 0.05623  -0.01169 -0.15610 173 ARG A NE  
1220 C CZ  . ARG A 166 ? 1.04629 0.83086 0.97886 0.04009  -0.02222 -0.15532 173 ARG A CZ  
1221 N NH1 . ARG A 166 ? 0.80369 0.58846 0.72172 0.02817  -0.03077 -0.16638 173 ARG A NH1 
1222 N NH2 . ARG A 166 ? 1.02702 0.80433 0.97994 0.03613  -0.02423 -0.14132 173 ARG A NH2 
1223 N N   . THR A 167 ? 0.59653 0.48677 0.45554 0.05988  -0.00530 -0.17214 174 THR A N   
1224 C CA  . THR A 167 ? 0.72815 0.61942 0.57666 0.04327  -0.01816 -0.17692 174 THR A CA  
1225 C C   . THR A 167 ? 0.64480 0.50590 0.50170 0.03136  -0.02856 -0.18167 174 THR A C   
1226 O O   . THR A 167 ? 0.79860 0.62851 0.65177 0.03697  -0.02657 -0.19350 174 THR A O   
1227 C CB  . THR A 167 ? 0.64790 0.53878 0.46300 0.04653  -0.01855 -0.19396 174 THR A CB  
1228 O OG1 . THR A 167 ? 0.83345 0.68794 0.63078 0.05415  -0.01628 -0.21426 174 THR A OG1 
1229 C CG2 . THR A 167 ? 0.59766 0.51940 0.40661 0.06045  -0.00583 -0.18664 174 THR A CG2 
1230 N N   . ASP A 168 ? 0.59145 0.46176 0.46225 0.01575  -0.03837 -0.17074 175 ASP A N   
1231 C CA  . ASP A 168 ? 0.69019 0.53622 0.57476 0.00418  -0.04733 -0.17043 175 ASP A CA  
1232 C C   . ASP A 168 ? 0.83779 0.66632 0.70597 -0.00799 -0.06033 -0.18745 175 ASP A C   
1233 O O   . ASP A 168 ? 0.84997 0.69764 0.70561 -0.01606 -0.06776 -0.18911 175 ASP A O   
1234 C CB  . ASP A 168 ? 0.62865 0.49212 0.53654 -0.00570 -0.05042 -0.14943 175 ASP A CB  
1235 C CG  . ASP A 168 ? 0.74402 0.58524 0.66984 -0.01585 -0.05732 -0.14497 175 ASP A CG  
1236 O OD1 . ASP A 168 ? 0.91731 0.73053 0.84600 -0.01068 -0.05526 -0.15207 175 ASP A OD1 
1237 O OD2 . ASP A 168 ? 0.86751 0.71980 0.80672 -0.02823 -0.06372 -0.13262 175 ASP A OD2 
1238 N N   . THR A 169 ? 1.08092 0.87285 0.95011 -0.00975 -0.06383 -0.19956 176 THR A N   
1239 C CA  . THR A 169 ? 1.19634 0.96452 1.05028 -0.02249 -0.07797 -0.21858 176 THR A CA  
1240 C C   . THR A 169 ? 1.14655 0.90924 1.02575 -0.04283 -0.09226 -0.20873 176 THR A C   
1241 O O   . THR A 169 ? 1.06217 0.81341 0.93269 -0.05798 -0.10800 -0.22105 176 THR A O   
1242 C CB  . THR A 169 ? 1.26733 0.99352 1.10683 -0.01230 -0.07299 -0.23995 176 THR A CB  
1243 O OG1 . THR A 169 ? 1.14012 0.84986 1.00687 -0.00577 -0.06471 -0.22860 176 THR A OG1 
1244 C CG2 . THR A 169 ? 1.08964 0.82129 0.89963 0.00751  -0.05950 -0.25184 176 THR A CG2 
1245 N N   . GLY A 170 ? 1.09232 0.86381 1.00206 -0.04345 -0.08745 -0.18633 177 GLY A N   
1246 C CA  . GLY A 170 ? 1.07431 0.84034 1.01175 -0.06000 -0.09766 -0.17367 177 GLY A CA  
1247 C C   . GLY A 170 ? 1.03430 0.82982 0.97832 -0.07559 -0.10891 -0.16253 177 GLY A C   
1248 O O   . GLY A 170 ? 0.99905 0.81099 0.92095 -0.07833 -0.11486 -0.17180 177 GLY A O   
1249 N N   . GLU A 171 ? 0.93350 0.73724 0.90848 -0.08469 -0.11089 -0.14080 178 GLU A N   
1250 C CA  . GLU A 171 ? 0.97332 0.80497 0.96133 -0.09934 -0.12069 -0.12633 178 GLU A CA  
1251 C C   . GLU A 171 ? 0.87299 0.74026 0.84884 -0.09145 -0.11289 -0.11836 178 GLU A C   
1252 O O   . GLU A 171 ? 0.69188 0.56789 0.67031 -0.07808 -0.09802 -0.10801 178 GLU A O   
1253 C CB  . GLU A 171 ? 1.03203 0.86616 1.05713 -0.10593 -0.11905 -0.10124 178 GLU A CB  
1254 C CG  . GLU A 171 ? 1.16718 1.01622 1.21398 -0.12611 -0.13447 -0.08951 178 GLU A CG  
1255 C CD  . GLU A 171 ? 1.37073 1.19501 1.41464 -0.14251 -0.15428 -0.10895 178 GLU A CD  
1256 O OE1 . GLU A 171 ? 1.37041 1.16055 1.42376 -0.14352 -0.15495 -0.11603 178 GLU A OE1 
1257 O OE2 . GLU A 171 ? 1.37711 1.21539 1.40898 -0.15457 -0.16966 -0.11712 178 GLU A OE2 
1258 N N   . PRO A 172 ? 0.78355 0.67154 0.74626 -0.09941 -0.12291 -0.12254 179 PRO A N   
1259 C CA  . PRO A 172 ? 0.79322 0.71617 0.74972 -0.09250 -0.11488 -0.11127 179 PRO A CA  
1260 C C   . PRO A 172 ? 0.68941 0.63201 0.67511 -0.09368 -0.10747 -0.08360 179 PRO A C   
1261 O O   . PRO A 172 ? 0.79914 0.74244 0.80967 -0.10562 -0.11444 -0.07024 179 PRO A O   
1262 C CB  . PRO A 172 ? 0.65146 0.59137 0.59183 -0.10360 -0.13017 -0.11899 179 PRO A CB  
1263 C CG  . PRO A 172 ? 0.71117 0.61800 0.63405 -0.11043 -0.14323 -0.14443 179 PRO A CG  
1264 C CD  . PRO A 172 ? 0.82386 0.70248 0.77302 -0.11406 -0.14225 -0.13986 179 PRO A CD  
1265 N N   . MET A 173 ? 0.64686 0.60482 0.62983 -0.08088 -0.09276 -0.07476 180 MET A N   
1266 C CA  . MET A 173 ? 0.68285 0.65480 0.68779 -0.07896 -0.08300 -0.05105 180 MET A CA  
1267 C C   . MET A 173 ? 0.66564 0.67008 0.67865 -0.08421 -0.08419 -0.03554 180 MET A C   
1268 O O   . MET A 173 ? 0.73071 0.74563 0.76637 -0.08674 -0.07955 -0.01455 180 MET A O   
1269 C CB  . MET A 173 ? 0.68855 0.65725 0.68689 -0.06337 -0.06741 -0.04976 180 MET A CB  
1270 C CG  . MET A 173 ? 0.79334 0.73531 0.79351 -0.05692 -0.06302 -0.05399 180 MET A CG  
1271 S SD  . MET A 173 ? 0.81947 0.76317 0.80676 -0.04035 -0.04969 -0.05663 180 MET A SD  
1272 C CE  . MET A 173 ? 0.54242 0.50352 0.54189 -0.03934 -0.04034 -0.03480 180 MET A CE  
1273 N N   . GLY A 174 ? 0.49205 0.51342 0.48728 -0.08425 -0.08863 -0.04369 181 GLY A N   
1274 C CA  . GLY A 174 ? 0.55841 0.61273 0.56136 -0.08635 -0.08727 -0.02702 181 GLY A CA  
1275 C C   . GLY A 174 ? 0.53888 0.60428 0.53705 -0.07270 -0.07108 -0.02143 181 GLY A C   
1276 O O   . GLY A 174 ? 0.48908 0.57145 0.47288 -0.06870 -0.07024 -0.02536 181 GLY A O   
1277 N N   . ARG A 175 ? 0.47277 0.52822 0.48256 -0.06566 -0.05845 -0.01202 182 ARG A N   
1278 C CA  . ARG A 175 ? 0.47794 0.53846 0.48509 -0.05424 -0.04422 -0.00764 182 ARG A CA  
1279 C C   . ARG A 175 ? 0.35752 0.39888 0.37252 -0.04864 -0.03459 -0.00182 182 ARG A C   
1280 O O   . ARG A 175 ? 0.43158 0.46883 0.46163 -0.05273 -0.03410 0.01029  182 ARG A O   
1281 C CB  . ARG A 175 ? 0.35094 0.43976 0.36880 -0.05450 -0.03901 0.00989  182 ARG A CB  
1282 C CG  . ARG A 175 ? 0.36170 0.45637 0.37545 -0.04426 -0.02672 0.01122  182 ARG A CG  
1283 C CD  . ARG A 175 ? 0.40800 0.52205 0.43898 -0.04313 -0.01743 0.03238  182 ARG A CD  
1284 N NE  . ARG A 175 ? 0.30856 0.41244 0.35487 -0.04325 -0.01073 0.04562  182 ARG A NE  
1285 C CZ  . ARG A 175 ? 0.42997 0.54701 0.49400 -0.04925 -0.01276 0.06226  182 ARG A CZ  
1286 N NH1 . ARG A 175 ? 0.32384 0.46554 0.39260 -0.05725 -0.02351 0.06759  182 ARG A NH1 
1287 N NH2 . ARG A 175 ? 0.33112 0.43765 0.40822 -0.04679 -0.00385 0.07487  182 ARG A NH2 
1288 N N   . GLY A 176 ? 0.36460 0.39593 0.36959 -0.03920 -0.02722 -0.00925 183 GLY A N   
1289 C CA  . GLY A 176 ? 0.32993 0.34422 0.33738 -0.03340 -0.01910 -0.00460 183 GLY A CA  
1290 C C   . GLY A 176 ? 0.43132 0.42751 0.42679 -0.02750 -0.02054 -0.01893 183 GLY A C   
1291 O O   . GLY A 176 ? 0.51010 0.50859 0.49590 -0.02542 -0.02426 -0.03161 183 GLY A O   
1292 N N   . THR A 177 ? 0.39607 0.37531 0.39217 -0.02363 -0.01672 -0.01537 184 THR A N   
1293 C CA  . THR A 177 ? 0.47523 0.43902 0.46237 -0.01713 -0.01761 -0.02523 184 THR A CA  
1294 C C   . THR A 177 ? 0.58638 0.53267 0.57788 -0.01656 -0.01735 -0.01943 184 THR A C   
1295 O O   . THR A 177 ? 0.48116 0.42646 0.47879 -0.01692 -0.01179 -0.00594 184 THR A O   
1296 C CB  . THR A 177 ? 0.46197 0.42741 0.44222 -0.01023 -0.01208 -0.02579 184 THR A CB  
1297 O OG1 . THR A 177 ? 0.50570 0.48789 0.48536 -0.01038 -0.01210 -0.03021 184 THR A OG1 
1298 C CG2 . THR A 177 ? 0.39559 0.34770 0.36916 -0.00372 -0.01400 -0.03242 184 THR A CG2 
1299 N N   . LYS A 178 ? 0.47830 0.41102 0.46763 -0.01456 -0.02198 -0.02827 185 LYS A N   
1300 C CA  . LYS A 178 ? 0.44683 0.36252 0.44202 -0.01304 -0.02163 -0.02230 185 LYS A CA  
1301 C C   . LYS A 178 ? 0.46145 0.36775 0.44773 -0.00313 -0.02009 -0.02678 185 LYS A C   
1302 O O   . LYS A 178 ? 0.47933 0.38334 0.46192 -0.00003 -0.02335 -0.03856 185 LYS A O   
1303 C CB  . LYS A 178 ? 0.46351 0.36971 0.46847 -0.02078 -0.02943 -0.02731 185 LYS A CB  
1304 C CG  . LYS A 178 ? 0.66790 0.55624 0.68414 -0.02012 -0.02891 -0.01927 185 LYS A CG  
1305 C CD  . LYS A 178 ? 0.73665 0.61972 0.76981 -0.03243 -0.03660 -0.01734 185 LYS A CD  
1306 C CE  . LYS A 178 ? 0.63561 0.52106 0.66160 -0.03984 -0.04645 -0.03503 185 LYS A CE  
1307 N NZ  . LYS A 178 ? 0.88718 0.75623 0.92567 -0.05078 -0.05667 -0.03987 185 LYS A NZ  
1308 N N   . VAL A 179 ? 0.43947 0.34136 0.42156 0.00255  -0.01490 -0.01672 186 VAL A N   
1309 C CA  . VAL A 179 ? 0.44837 0.34398 0.42199 0.01148  -0.01498 -0.01813 186 VAL A CA  
1310 C C   . VAL A 179 ? 0.46267 0.34359 0.44338 0.01455  -0.01412 -0.00968 186 VAL A C   
1311 O O   . VAL A 179 ? 0.43821 0.31554 0.42072 0.01516  -0.00902 0.00373  186 VAL A O   
1312 C CB  . VAL A 179 ? 0.43743 0.33738 0.39723 0.01575  -0.01143 -0.01391 186 VAL A CB  
1313 C CG1 . VAL A 179 ? 0.43910 0.33432 0.39025 0.02381  -0.01414 -0.01382 186 VAL A CG1 
1314 C CG2 . VAL A 179 ? 0.38864 0.30195 0.34569 0.01233  -0.01189 -0.02099 186 VAL A CG2 
1315 N N   . ILE A 180 ? 0.42701 0.29927 0.41290 0.01767  -0.01759 -0.01599 187 ILE A N   
1316 C CA  . ILE A 180 ? 0.46566 0.32266 0.46198 0.02081  -0.01651 -0.00755 187 ILE A CA  
1317 C C   . ILE A 180 ? 0.53621 0.39254 0.52511 0.03208  -0.01559 -0.00278 187 ILE A C   
1318 O O   . ILE A 180 ? 0.50261 0.36199 0.48952 0.03689  -0.01843 -0.01138 187 ILE A O   
1319 C CB  . ILE A 180 ? 0.51755 0.36130 0.52631 0.01652  -0.02062 -0.01759 187 ILE A CB  
1320 C CG1 . ILE A 180 ? 0.53163 0.37884 0.54538 0.00397  -0.02456 -0.02309 187 ILE A CG1 
1321 C CG2 . ILE A 180 ? 0.45687 0.28285 0.48041 0.01925  -0.01885 -0.00722 187 ILE A CG2 
1322 C CD1 . ILE A 180 ? 0.53788 0.37100 0.55664 -0.00119 -0.03064 -0.03798 187 ILE A CD1 
1323 N N   . LEU A 181 ? 0.52270 0.37663 0.50782 0.03696  -0.01145 0.01241  188 LEU A N   
1324 C CA  . LEU A 181 ? 0.50080 0.35648 0.47606 0.04743  -0.01187 0.01928  188 LEU A CA  
1325 C C   . LEU A 181 ? 0.53014 0.37341 0.52056 0.05312  -0.00967 0.03018  188 LEU A C   
1326 O O   . LEU A 181 ? 0.52225 0.35873 0.51985 0.05317  -0.00436 0.04438  188 LEU A O   
1327 C CB  . LEU A 181 ? 0.48071 0.34149 0.43586 0.05072  -0.00851 0.02844  188 LEU A CB  
1328 C CG  . LEU A 181 ? 0.52300 0.39176 0.46543 0.04495  -0.00847 0.01978  188 LEU A CG  
1329 C CD1 . LEU A 181 ? 0.51321 0.38015 0.43565 0.04936  -0.00228 0.02944  188 LEU A CD1 
1330 C CD2 . LEU A 181 ? 0.48146 0.36004 0.41756 0.04451  -0.01606 0.00689  188 LEU A CD2 
1331 N N   . HIS A 182 ? 0.46916 0.30997 0.46667 0.05873  -0.01257 0.02541  189 HIS A N   
1332 C CA  . HIS A 182 ? 0.51669 0.34567 0.52937 0.06633  -0.00979 0.03697  189 HIS A CA  
1333 C C   . HIS A 182 ? 0.55254 0.39149 0.55263 0.07667  -0.00958 0.05269  189 HIS A C   
1334 O O   . HIS A 182 ? 0.58207 0.43195 0.57588 0.08313  -0.01435 0.05130  189 HIS A O   
1335 C CB  . HIS A 182 ? 0.49242 0.31401 0.51734 0.06983  -0.01123 0.02581  189 HIS A CB  
1336 C CG  . HIS A 182 ? 0.63821 0.45081 0.66758 0.06032  -0.01258 0.00762  189 HIS A CG  
1337 N ND1 . HIS A 182 ? 0.63301 0.42427 0.67810 0.05444  -0.01154 0.00480  189 HIS A ND1 
1338 C CD2 . HIS A 182 ? 0.66589 0.48849 0.68505 0.05518  -0.01562 -0.00808 189 HIS A CD2 
1339 C CE1 . HIS A 182 ? 0.57553 0.36400 0.61669 0.04615  -0.01492 -0.01324 189 HIS A CE1 
1340 N NE2 . HIS A 182 ? 0.53914 0.34742 0.56467 0.04722  -0.01656 -0.02036 189 HIS A NE2 
1341 N N   . LEU A 183 ? 0.55540 0.39205 0.55169 0.07845  -0.00423 0.06876  190 LEU A N   
1342 C CA  . LEU A 183 ? 0.53215 0.37892 0.50766 0.08780  -0.00406 0.08243  190 LEU A CA  
1343 C C   . LEU A 183 ? 0.67925 0.52799 0.66303 0.09915  -0.00549 0.09477  190 LEU A C   
1344 O O   . LEU A 183 ? 0.68700 0.52385 0.69639 0.10149  -0.00186 0.10014  190 LEU A O   
1345 C CB  . LEU A 183 ? 0.52402 0.36717 0.49407 0.08909  0.00495  0.09851  190 LEU A CB  
1346 C CG  . LEU A 183 ? 0.61413 0.45744 0.57704 0.07987  0.00816  0.09088  190 LEU A CG  
1347 C CD1 . LEU A 183 ? 0.52114 0.36276 0.47992 0.08424  0.01933  0.11049  190 LEU A CD1 
1348 C CD2 . LEU A 183 ? 0.50470 0.35760 0.44125 0.07774  0.00201  0.07532  190 LEU A CD2 
1349 N N   . LYS A 184 ? 0.48472 0.62689 0.61266 0.03695  -0.07175 0.13193  191 LYS A N   
1350 C CA  . LYS A 184 ? 0.51843 0.65166 0.65448 0.05440  -0.08314 0.14796  191 LYS A CA  
1351 C C   . LYS A 184 ? 0.60357 0.68463 0.71547 0.05805  -0.07612 0.16005  191 LYS A C   
1352 O O   . LYS A 184 ? 0.50249 0.56010 0.58773 0.04409  -0.06599 0.15840  191 LYS A O   
1353 C CB  . LYS A 184 ? 0.47173 0.62938 0.60011 0.05246  -0.10698 0.16111  191 LYS A CB  
1354 C CG  . LYS A 184 ? 0.52881 0.73890 0.68930 0.04498  -0.11285 0.15376  191 LYS A CG  
1355 C CD  . LYS A 184 ? 0.55456 0.78181 0.70572 0.03362  -0.13750 0.16118  191 LYS A CD  
1356 C CE  . LYS A 184 ? 0.51282 0.79015 0.70366 0.02093  -0.14061 0.15663  191 LYS A CE  
1357 N NZ  . LYS A 184 ? 0.58940 0.87975 0.77737 0.00506  -0.16643 0.15909  191 LYS A NZ  
1358 N N   . GLU A 185 ? 0.54793 0.61244 0.67211 0.07839  -0.08020 0.17505  192 GLU A N   
1359 C CA  . GLU A 185 ? 0.65142 0.66334 0.75955 0.08360  -0.06990 0.19226  192 GLU A CA  
1360 C C   . GLU A 185 ? 0.68165 0.67743 0.73825 0.07419  -0.07328 0.21051  192 GLU A C   
1361 O O   . GLU A 185 ? 0.76970 0.72905 0.80981 0.06703  -0.05605 0.21887  192 GLU A O   
1362 C CB  . GLU A 185 ? 0.62083 0.61920 0.74874 0.11123  -0.07667 0.21094  192 GLU A CB  
1363 C CG  . GLU A 185 ? 0.86898 0.81047 0.97891 0.11944  -0.06666 0.23895  192 GLU A CG  
1364 C CD  . GLU A 185 ? 1.05302 0.97037 1.19504 0.14798  -0.06675 0.25226  192 GLU A CD  
1365 O OE1 . GLU A 185 ? 0.84537 0.79012 1.02656 0.16111  -0.07156 0.23350  192 GLU A OE1 
1366 O OE2 . GLU A 185 ? 1.06483 0.93564 1.19289 0.15919  -0.06036 0.28318  192 GLU A OE2 
1367 N N   . ASP A 186 ? 0.59543 0.61963 0.62812 0.07374  -0.09466 0.21503  193 ASP A N   
1368 C CA  . ASP A 186 ? 0.62367 0.63503 0.60180 0.07033  -0.10103 0.22923  193 ASP A CA  
1369 C C   . ASP A 186 ? 0.69759 0.71568 0.65358 0.04847  -0.09613 0.21067  193 ASP A C   
1370 O O   . ASP A 186 ? 0.65864 0.66935 0.56753 0.04653  -0.10199 0.21646  193 ASP A O   
1371 C CB  . ASP A 186 ? 0.67061 0.70729 0.63243 0.08450  -0.13155 0.24119  193 ASP A CB  
1372 C CG  . ASP A 186 ? 0.91986 1.00575 0.91844 0.07796  -0.15035 0.22234  193 ASP A CG  
1373 O OD1 . ASP A 186 ? 0.93519 1.04556 0.91660 0.07357  -0.17497 0.21889  193 ASP A OD1 
1374 O OD2 . ASP A 186 ? 0.86542 0.96673 0.91117 0.07703  -0.14003 0.21040  193 ASP A OD2 
1375 N N   . GLN A 187 ? 0.61549 0.64764 0.60140 0.03517  -0.08554 0.18862  194 GLN A N   
1376 C CA  . GLN A 187 ? 0.58440 0.62421 0.55332 0.01792  -0.08200 0.17281  194 GLN A CA  
1377 C C   . GLN A 187 ? 0.53436 0.55791 0.50720 0.00870  -0.05701 0.16405  194 GLN A C   
1378 O O   . GLN A 187 ? 0.59812 0.63553 0.57451 -0.00227 -0.05166 0.14778  194 GLN A O   
1379 C CB  . GLN A 187 ? 0.51503 0.59177 0.51254 0.01050  -0.09250 0.15782  194 GLN A CB  
1380 C CG  . GLN A 187 ? 0.49984 0.60133 0.50448 0.01535  -0.11876 0.16394  194 GLN A CG  
1381 C CD  . GLN A 187 ? 0.59553 0.68538 0.55355 0.01325  -0.13660 0.16790  194 GLN A CD  
1382 O OE1 . GLN A 187 ? 0.63659 0.71045 0.56394 0.00284  -0.13135 0.15927  194 GLN A OE1 
1383 N NE2 . GLN A 187 ? 0.56872 0.66848 0.51978 0.02590  -0.15881 0.17939  194 GLN A NE2 
1384 N N   . THR A 188 ? 0.58507 0.58027 0.56029 0.01298  -0.04193 0.17603  195 THR A N   
1385 C CA  . THR A 188 ? 0.57797 0.56188 0.56828 0.00201  -0.01958 0.16635  195 THR A CA  
1386 C C   . THR A 188 ? 0.59761 0.57707 0.55340 -0.00682 -0.00931 0.16847  195 THR A C   
1387 O O   . THR A 188 ? 0.55665 0.53631 0.52842 -0.01701 0.00790  0.15892  195 THR A O   
1388 C CB  . THR A 188 ? 0.57652 0.52814 0.58963 0.00647  -0.00602 0.17934  195 THR A CB  
1389 O OG1 . THR A 188 ? 0.69428 0.62091 0.67206 0.01467  -0.00398 0.21052  195 THR A OG1 
1390 C CG2 . THR A 188 ? 0.60476 0.55880 0.65414 0.01919  -0.01476 0.17377  195 THR A CG2 
1391 N N   . GLU A 189 ? 0.60936 0.58775 0.51995 -0.00198 -0.02019 0.17812  196 GLU A N   
1392 C CA  . GLU A 189 ? 0.63697 0.61274 0.51276 -0.00645 -0.00978 0.17660  196 GLU A CA  
1393 C C   . GLU A 189 ? 0.59636 0.59239 0.48607 -0.01613 -0.00762 0.15290  196 GLU A C   
1394 O O   . GLU A 189 ? 0.69299 0.68997 0.56971 -0.01942 0.00657  0.14894  196 GLU A O   
1395 C CB  . GLU A 189 ? 0.64533 0.61649 0.46718 0.00316  -0.02581 0.18458  196 GLU A CB  
1396 C CG  . GLU A 189 ? 0.60618 0.59329 0.42312 -0.00059 -0.04831 0.16517  196 GLU A CG  
1397 C CD  . GLU A 189 ? 0.81760 0.80285 0.59493 0.00854  -0.07296 0.16946  196 GLU A CD  
1398 O OE1 . GLU A 189 ? 0.92617 0.91595 0.71167 0.01696  -0.08690 0.18227  196 GLU A OE1 
1399 O OE2 . GLU A 189 ? 0.83418 0.81423 0.57239 0.00902  -0.07963 0.15823  196 GLU A OE2 
1400 N N   . TYR A 190 ? 0.48946 0.50434 0.40545 -0.01857 -0.01995 0.13956  197 TYR A N   
1401 C CA  . TYR A 190 ? 0.55723 0.59182 0.48469 -0.02477 -0.01772 0.12209  197 TYR A CA  
1402 C C   . TYR A 190 ? 0.59822 0.64594 0.56060 -0.02916 -0.00244 0.11055  197 TYR A C   
1403 O O   . TYR A 190 ? 0.52382 0.59356 0.49720 -0.03109 -0.00129 0.09684  197 TYR A O   
1404 C CB  . TYR A 190 ? 0.56994 0.62206 0.50967 -0.02543 -0.03491 0.11706  197 TYR A CB  
1405 C CG  . TYR A 190 ? 0.60917 0.65129 0.52081 -0.02416 -0.05385 0.12367  197 TYR A CG  
1406 C CD1 . TYR A 190 ? 0.60168 0.63040 0.47842 -0.02588 -0.05735 0.11880  197 TYR A CD1 
1407 C CD2 . TYR A 190 ? 0.53353 0.58066 0.45416 -0.01953 -0.06972 0.13225  197 TYR A CD2 
1408 C CE1 . TYR A 190 ? 0.57769 0.59682 0.42796 -0.02515 -0.07776 0.11875  197 TYR A CE1 
1409 C CE2 . TYR A 190 ? 0.57482 0.61841 0.47143 -0.01872 -0.09107 0.13477  197 TYR A CE2 
1410 C CZ  . TYR A 190 ? 0.60513 0.63388 0.46584 -0.02260 -0.09576 0.12625  197 TYR A CZ  
1411 O OH  . TYR A 190 ? 0.61496 0.63980 0.45125 -0.02231 -0.11998 0.12271  197 TYR A OH  
1412 N N   . LEU A 191 ? 0.55433 0.58848 0.53480 -0.03048 0.00836  0.11589  198 LEU A N   
1413 C CA  . LEU A 191 ? 0.55753 0.60103 0.57264 -0.03790 0.02220  0.10193  198 LEU A CA  
1414 C C   . LEU A 191 ? 0.57492 0.61356 0.58301 -0.04446 0.03966  0.10828  198 LEU A C   
1415 O O   . LEU A 191 ? 0.60740 0.66003 0.64851 -0.05323 0.05035  0.09528  198 LEU A O   
1416 C CB  . LEU A 191 ? 0.50367 0.53187 0.55342 -0.03765 0.02420  0.10082  198 LEU A CB  
1417 C CG  . LEU A 191 ? 0.54283 0.58203 0.60510 -0.02797 0.00996  0.09306  198 LEU A CG  
1418 C CD1 . LEU A 191 ? 0.57813 0.59517 0.67247 -0.02349 0.01279  0.09211  198 LEU A CD1 
1419 C CD2 . LEU A 191 ? 0.50372 0.58052 0.57701 -0.02800 0.00654  0.06972  198 LEU A CD2 
1420 N N   . GLU A 192 ? 0.53369 0.55742 0.50070 -0.03973 0.04251  0.12622  199 GLU A N   
1421 C CA  . GLU A 192 ? 0.58736 0.60955 0.54493 -0.04299 0.06287  0.13598  199 GLU A CA  
1422 C C   . GLU A 192 ? 0.65751 0.70464 0.60483 -0.04092 0.06535  0.12165  199 GLU A C   
1423 O O   . GLU A 192 ? 0.56820 0.61801 0.49076 -0.03361 0.05085  0.11415  199 GLU A O   
1424 C CB  . GLU A 192 ? 0.64203 0.63944 0.55294 -0.03401 0.06627  0.16182  199 GLU A CB  
1425 C CG  . GLU A 192 ? 0.78977 0.76135 0.70757 -0.03145 0.06358  0.18134  199 GLU A CG  
1426 C CD  . GLU A 192 ? 0.91709 0.87421 0.86757 -0.04114 0.08815  0.19743  199 GLU A CD  
1427 O OE1 . GLU A 192 ? 0.99931 0.96870 0.95579 -0.04875 0.10910  0.19981  199 GLU A OE1 
1428 O OE2 . GLU A 192 ? 1.12541 1.05891 1.10015 -0.04121 0.08722  0.20794  199 GLU A OE2 
1429 N N   . GLU A 193 ? 0.60415 0.66935 0.57496 -0.04736 0.08431  0.11912  200 GLU A N   
1430 C CA  . GLU A 193 ? 0.61626 0.71033 0.58560 -0.04252 0.08752  0.10540  200 GLU A CA  
1431 C C   . GLU A 193 ? 0.68582 0.76735 0.59997 -0.02806 0.08788  0.11225  200 GLU A C   
1432 O O   . GLU A 193 ? 0.47657 0.56212 0.37387 -0.01915 0.07653  0.10072  200 GLU A O   
1433 C CB  . GLU A 193 ? 0.62899 0.75081 0.64123 -0.05260 0.10801  0.10255  200 GLU A CB  
1434 C CG  . GLU A 193 ? 0.66734 0.82531 0.68261 -0.04426 0.11250  0.09019  200 GLU A CG  
1435 C CD  . GLU A 193 ? 0.89909 1.09168 0.96265 -0.05520 0.13338  0.08901  200 GLU A CD  
1436 O OE1 . GLU A 193 ? 0.79664 0.97745 0.88468 -0.07025 0.14843  0.10266  200 GLU A OE1 
1437 O OE2 . GLU A 193 ? 0.82129 1.05381 0.90183 -0.04868 0.13501  0.07604  200 GLU A OE2 
1438 N N   . ARG A 194 ? 0.66694 0.73166 0.55104 -0.02428 0.10139  0.13090  201 ARG A N   
1439 C CA  . ARG A 194 ? 0.72262 0.77660 0.55018 -0.00813 0.10194  0.13222  201 ARG A CA  
1440 C C   . ARG A 194 ? 0.70901 0.73759 0.49975 -0.00194 0.07485  0.12650  201 ARG A C   
1441 O O   . ARG A 194 ? 0.68721 0.70598 0.43974 0.00976  0.06797  0.11648  201 ARG A O   
1442 C CB  . ARG A 194 ? 0.64284 0.69032 0.44216 -0.00299 0.12460  0.15464  201 ARG A CB  
1443 C CG  . ARG A 194 ? 0.88201 0.90318 0.66465 -0.00481 0.11951  0.17629  201 ARG A CG  
1444 C CD  . ARG A 194 ? 0.95159 0.97044 0.70842 0.00111  0.14716  0.20427  201 ARG A CD  
1445 N NE  . ARG A 194 ? 1.15132 1.14393 0.88814 0.00352  0.14222  0.22971  201 ARG A NE  
1446 C CZ  . ARG A 194 ? 1.19160 1.17685 0.90026 0.01068  0.16448  0.26178  201 ARG A CZ  
1447 N NH1 . ARG A 194 ? 1.18821 1.19287 0.88620 0.01486  0.19558  0.27226  201 ARG A NH1 
1448 N NH2 . ARG A 194 ? 1.27283 1.23337 0.96364 0.01590  0.15665  0.28632  201 ARG A NH2 
1449 N N   . ARG A 195 ? 0.70545 0.72404 0.51120 -0.00954 0.05920  0.13098  202 ARG A N   
1450 C CA  . ARG A 195 ? 0.63047 0.63370 0.41364 -0.00656 0.03271  0.12507  202 ARG A CA  
1451 C C   . ARG A 195 ? 0.63608 0.64918 0.43928 -0.00948 0.02133  0.10775  202 ARG A C   
1452 O O   . ARG A 195 ? 0.62977 0.62937 0.40811 -0.00526 0.00725  0.09898  202 ARG A O   
1453 C CB  . ARG A 195 ? 0.59871 0.59479 0.39669 -0.01096 0.02126  0.13698  202 ARG A CB  
1454 C CG  . ARG A 195 ? 0.59569 0.58403 0.37770 -0.00898 -0.00664 0.13250  202 ARG A CG  
1455 C CD  . ARG A 195 ? 0.71652 0.68849 0.44011 0.00201  -0.01600 0.13459  202 ARG A CD  
1456 N NE  . ARG A 195 ? 0.74190 0.71093 0.45775 0.00162  -0.04588 0.12976  202 ARG A NE  
1457 C CZ  . ARG A 195 ? 0.70479 0.66695 0.40340 0.00013  -0.06459 0.11179  202 ARG A CZ  
1458 N NH1 . ARG A 195 ? 0.69469 0.64687 0.37644 0.00235  -0.05644 0.09727  202 ARG A NH1 
1459 N NH2 . ARG A 195 ? 0.64860 0.61397 0.35177 -0.00373 -0.09245 0.10776  202 ARG A NH2 
1460 N N   . ILE A 196 ? 0.56605 0.60187 0.41369 -0.01623 0.02709  0.10271  203 ILE A N   
1461 C CA  . ILE A 196 ? 0.60292 0.65183 0.46596 -0.01589 0.01901  0.09127  203 ILE A CA  
1462 C C   . ILE A 196 ? 0.59660 0.64292 0.43827 -0.00548 0.02528  0.08458  203 ILE A C   
1463 O O   . ILE A 196 ? 0.62938 0.66429 0.46069 -0.00173 0.01464  0.07974  203 ILE A O   
1464 C CB  . ILE A 196 ? 0.52622 0.60538 0.43443 -0.02132 0.02399  0.08515  203 ILE A CB  
1465 C CG1 . ILE A 196 ? 0.46977 0.54765 0.39851 -0.02773 0.01556  0.08819  203 ILE A CG1 
1466 C CG2 . ILE A 196 ? 0.43633 0.53450 0.35329 -0.01624 0.01952  0.07719  203 ILE A CG2 
1467 C CD1 . ILE A 196 ? 0.58112 0.68000 0.55045 -0.03286 0.02335  0.07917  203 ILE A CD1 
1468 N N   . LYS A 197 ? 0.54693 0.60310 0.38491 -0.00013 0.04400  0.08535  204 LYS A N   
1469 C CA  . LYS A 197 ? 0.63720 0.69385 0.45638 0.01419  0.05215  0.07835  204 LYS A CA  
1470 C C   . LYS A 197 ? 0.64225 0.66130 0.41263 0.02295  0.04139  0.07394  204 LYS A C   
1471 O O   . LYS A 197 ? 0.61248 0.61714 0.37231 0.03192  0.03516  0.06487  204 LYS A O   
1472 C CB  . LYS A 197 ? 0.56867 0.64800 0.39537 0.01811  0.07650  0.08194  204 LYS A CB  
1473 C CG  . LYS A 197 ? 0.69352 0.81601 0.56844 0.01645  0.08565  0.07614  204 LYS A CG  
1474 C CD  . LYS A 197 ? 0.73451 0.88133 0.64055 0.00565  0.10582  0.08317  204 LYS A CD  
1475 C CE  . LYS A 197 ? 0.70826 0.89874 0.64346 0.01295  0.12217  0.07708  204 LYS A CE  
1476 N NZ  . LYS A 197 ? 0.76523 0.97081 0.71285 0.00729  0.14873  0.08928  204 LYS A NZ  
1477 N N   . GLU A 198 ? 0.59076 0.59226 0.33076 0.02144  0.03795  0.07967  205 GLU A N   
1478 C CA  . GLU A 198 ? 0.62724 0.59600 0.31822 0.02984  0.02395  0.07031  205 GLU A CA  
1479 C C   . GLU A 198 ? 0.65438 0.60416 0.35490 0.02122  -0.00127 0.06208  205 GLU A C   
1480 O O   . GLU A 198 ? 0.69384 0.61585 0.37079 0.02740  -0.01175 0.04773  205 GLU A O   
1481 C CB  . GLU A 198 ? 0.69047 0.65180 0.34728 0.03107  0.02223  0.08031  205 GLU A CB  
1482 C CG  . GLU A 198 ? 0.84084 0.77334 0.44844 0.03746  -0.00065 0.06741  205 GLU A CG  
1483 C CD  . GLU A 198 ? 0.99451 0.92647 0.57342 0.03884  -0.00849 0.08085  205 GLU A CD  
1484 O OE1 . GLU A 198 ? 0.91137 0.85481 0.52323 0.02778  -0.01179 0.09710  205 GLU A OE1 
1485 O OE2 . GLU A 198 ? 0.86460 0.78509 0.38596 0.05374  -0.01155 0.07496  205 GLU A OE2 
1486 N N   . ILE A 199 ? 0.66678 0.63085 0.40461 0.00691  -0.00997 0.07064  206 ILE A N   
1487 C CA  . ILE A 199 ? 0.62968 0.58299 0.38391 -0.00299 -0.03002 0.06714  206 ILE A CA  
1488 C C   . ILE A 199 ? 0.70275 0.65298 0.47210 0.00123  -0.02475 0.06356  206 ILE A C   
1489 O O   . ILE A 199 ? 0.67291 0.59524 0.43651 -0.00052 -0.03681 0.05684  206 ILE A O   
1490 C CB  . ILE A 199 ? 0.65454 0.63057 0.44550 -0.01556 -0.03665 0.07817  206 ILE A CB  
1491 C CG1 . ILE A 199 ? 0.69304 0.66741 0.46802 -0.01622 -0.04416 0.08445  206 ILE A CG1 
1492 C CG2 . ILE A 199 ? 0.59586 0.56933 0.41061 -0.02637 -0.05263 0.07803  206 ILE A CG2 
1493 C CD1 . ILE A 199 ? 0.64351 0.63966 0.45565 -0.02335 -0.04656 0.09510  206 ILE A CD1 
1494 N N   . VAL A 200 ? 0.61282 0.59118 0.40332 0.00723  -0.00761 0.06822  207 VAL A N   
1495 C CA  . VAL A 200 ? 0.62729 0.60927 0.43213 0.01511  -0.00312 0.06899  207 VAL A CA  
1496 C C   . VAL A 200 ? 0.74591 0.69611 0.52090 0.03094  -0.00013 0.05883  207 VAL A C   
1497 O O   . VAL A 200 ? 0.66860 0.59377 0.44516 0.03470  -0.00580 0.05877  207 VAL A O   
1498 C CB  . VAL A 200 ? 0.57156 0.59846 0.40462 0.01974  0.01109  0.07283  207 VAL A CB  
1499 C CG1 . VAL A 200 ? 0.62831 0.66298 0.46775 0.03516  0.01643  0.07428  207 VAL A CG1 
1500 C CG2 . VAL A 200 ? 0.50404 0.55669 0.36693 0.00682  0.00602  0.07872  207 VAL A CG2 
1501 N N   . LYS A 201 ? 0.63127 0.58031 0.37897 0.04166  0.01041  0.05105  208 LYS A N   
1502 C CA  . LYS A 201 ? 0.66629 0.58661 0.38227 0.06097  0.01501  0.03784  208 LYS A CA  
1503 C C   . LYS A 201 ? 0.91161 0.78084 0.60085 0.05657  -0.00549 0.02452  208 LYS A C   
1504 O O   . LYS A 201 ? 0.82967 0.66336 0.50870 0.06789  -0.00834 0.01395  208 LYS A O   
1505 C CB  . LYS A 201 ? 0.70904 0.64611 0.40054 0.07359  0.03352  0.03405  208 LYS A CB  
1506 C CG  . LYS A 201 ? 0.87365 0.78192 0.52366 0.09688  0.03927  0.01678  208 LYS A CG  
1507 C CD  . LYS A 201 ? 0.98066 0.90552 0.59797 0.10712  0.05706  0.01577  208 LYS A CD  
1508 C CE  . LYS A 201 ? 1.09083 1.06760 0.74020 0.11333  0.08419  0.02775  208 LYS A CE  
1509 N NZ  . LYS A 201 ? 1.12818 1.11097 0.75644 0.14198  0.10450  0.01723  208 LYS A NZ  
1510 N N   . LYS A 202 ? 0.84859 0.71313 0.52934 0.04057  -0.02135 0.02375  209 LYS A N   
1511 C CA  . LYS A 202 ? 0.89537 0.71776 0.55365 0.03438  -0.04471 0.00679  209 LYS A CA  
1512 C C   . LYS A 202 ? 0.94076 0.74466 0.63660 0.01776  -0.05897 0.01147  209 LYS A C   
1513 O O   . LYS A 202 ? 1.02406 0.78334 0.71221 0.01657  -0.07195 -0.00396 209 LYS A O   
1514 C CB  . LYS A 202 ? 0.96036 0.79198 0.59817 0.02537  -0.05884 0.00562  209 LYS A CB  
1515 C CG  . LYS A 202 ? 0.94100 0.74731 0.57958 0.00928  -0.09002 -0.00750 209 LYS A CG  
1516 C CD  . LYS A 202 ? 1.02033 0.81653 0.60548 0.01699  -0.10557 -0.02539 209 LYS A CD  
1517 C CE  . LYS A 202 ? 1.13775 0.97017 0.70888 0.02155  -0.09630 -0.00635 209 LYS A CE  
1518 N NZ  . LYS A 202 ? 1.15977 1.01580 0.76959 0.00298  -0.11150 0.00938  209 LYS A NZ  
1519 N N   . HIS A 203 ? 0.92756 0.76435 0.66508 0.00518  -0.05543 0.03246  210 HIS A N   
1520 C CA  . HIS A 203 ? 0.90064 0.72849 0.67523 -0.01245 -0.06647 0.04214  210 HIS A CA  
1521 C C   . HIS A 203 ? 0.88100 0.71364 0.68053 -0.00517 -0.05161 0.05912  210 HIS A C   
1522 O O   . HIS A 203 ? 0.94083 0.75172 0.76407 -0.01572 -0.05730 0.06801  210 HIS A O   
1523 C CB  . HIS A 203 ? 0.87265 0.73709 0.67552 -0.03046 -0.07453 0.05434  210 HIS A CB  
1524 C CG  . HIS A 203 ? 0.89638 0.75341 0.68432 -0.04055 -0.09659 0.04149  210 HIS A CG  
1525 N ND1 . HIS A 203 ? 1.01303 0.83662 0.80088 -0.05285 -0.11907 0.02618  210 HIS A ND1 
1526 C CD2 . HIS A 203 ? 0.83228 0.71193 0.60573 -0.03916 -0.10105 0.04198  210 HIS A CD2 
1527 C CE1 . HIS A 203 ? 0.95307 0.78495 0.72494 -0.05749 -0.13855 0.01596  210 HIS A CE1 
1528 N NE2 . HIS A 203 ? 0.80238 0.66710 0.56346 -0.04785 -0.12711 0.02774  210 HIS A NE2 
1529 N N   . SER A 204 ? 0.89453 0.60299 0.65489 0.02652  -0.14274 -0.06027 211 SER A N   
1530 C CA  . SER A 204 ? 0.98141 0.70231 0.77524 0.03226  -0.11621 -0.06075 211 SER A CA  
1531 C C   . SER A 204 ? 0.95397 0.67930 0.70225 0.05577  -0.08802 -0.06488 211 SER A C   
1532 O O   . SER A 204 ? 0.87467 0.63055 0.64889 0.06253  -0.06272 -0.05803 211 SER A O   
1533 C CB  . SER A 204 ? 0.88904 0.65253 0.75171 0.02257  -0.10613 -0.04466 211 SER A CB  
1534 O OG  . SER A 204 ? 0.86700 0.63091 0.77559 0.00430  -0.13022 -0.03938 211 SER A OG  
1535 N N   . GLN A 205 ? 1.03509 0.73172 0.71429 0.06945  -0.09208 -0.07645 212 GLN A N   
1536 C CA  . GLN A 205 ? 1.09002 0.79353 0.72599 0.09526  -0.06417 -0.07985 212 GLN A CA  
1537 C C   . GLN A 205 ? 1.11271 0.79549 0.75108 0.10808  -0.04901 -0.09006 212 GLN A C   
1538 O O   . GLN A 205 ? 1.26962 0.96363 0.88156 0.13186  -0.02396 -0.09080 212 GLN A O   
1539 C CB  . GLN A 205 ? 1.04077 0.71826 0.59825 0.10906  -0.07117 -0.09031 212 GLN A CB  
1540 C CG  . GLN A 205 ? 1.20342 0.81615 0.71816 0.10902  -0.09370 -0.11391 212 GLN A CG  
1541 C CD  . GLN A 205 ? 1.30878 0.90274 0.82272 0.08547  -0.13199 -0.11589 212 GLN A CD  
1542 O OE1 . GLN A 205 ? 1.15843 0.76908 0.73545 0.06283  -0.14715 -0.10496 212 GLN A OE1 
1543 N NE2 . GLN A 205 ? 1.27925 0.83974 0.72071 0.09192  -0.14796 -0.13001 212 GLN A NE2 
1544 N N   . PHE A 206 ? 1.25729 0.91290 0.92888 0.09342  -0.06287 -0.09543 213 PHE A N   
1545 C CA  . PHE A 206 ? 1.09636 0.72449 0.76810 0.10412  -0.05098 -0.10315 213 PHE A CA  
1546 C C   . PHE A 206 ? 1.14601 0.79808 0.88813 0.08944  -0.04503 -0.09131 213 PHE A C   
1547 O O   . PHE A 206 ? 1.02695 0.64747 0.78261 0.08482  -0.04829 -0.09557 213 PHE A O   
1548 C CB  . PHE A 206 ? 1.11738 0.67574 0.74817 0.10186  -0.07287 -0.12323 213 PHE A CB  
1549 C CG  . PHE A 206 ? 1.16399 0.69295 0.71639 0.11908  -0.07756 -0.13856 213 PHE A CG  
1550 C CD1 . PHE A 206 ? 1.22222 0.76883 0.73448 0.14967  -0.04972 -0.13827 213 PHE A CD1 
1551 C CD2 . PHE A 206 ? 1.25075 0.73781 0.76909 0.10503  -0.10974 -0.15290 213 PHE A CD2 
1552 C CE1 . PHE A 206 ? 1.26196 0.78376 0.69933 0.16790  -0.05092 -0.15232 213 PHE A CE1 
1553 C CE2 . PHE A 206 ? 1.28379 0.74302 0.72319 0.12195  -0.11347 -0.16844 213 PHE A CE2 
1554 C CZ  . PHE A 206 ? 1.17263 0.64863 0.57044 0.15438  -0.08257 -0.16830 213 PHE A CZ  
1555 N N   . ILE A 207 ? 1.06275 0.76842 0.84789 0.08195  -0.03565 -0.07638 214 ILE A N   
1556 C CA  . ILE A 207 ? 0.84708 0.58016 0.69305 0.07151  -0.02588 -0.06618 214 ILE A CA  
1557 C C   . ILE A 207 ? 0.78627 0.54118 0.62751 0.09150  0.00255  -0.06202 214 ILE A C   
1558 O O   . ILE A 207 ? 0.86271 0.64342 0.67872 0.10740  0.01737  -0.05941 214 ILE A O   
1559 C CB  . ILE A 207 ? 0.75599 0.53076 0.64679 0.05547  -0.02956 -0.05469 214 ILE A CB  
1560 C CG1 . ILE A 207 ? 0.71962 0.47545 0.62499 0.03624  -0.05929 -0.05595 214 ILE A CG1 
1561 C CG2 . ILE A 207 ? 0.58220 0.38982 0.52643 0.04985  -0.01364 -0.04612 214 ILE A CG2 
1562 C CD1 . ILE A 207 ? 0.65760 0.39057 0.59676 0.02190  -0.07142 -0.05843 214 ILE A CD1 
1563 N N   . GLY A 208 ? 0.74024 0.48788 0.60667 0.09064  0.01001  -0.05940 215 GLY A N   
1564 C CA  . GLY A 208 ? 0.74642 0.51116 0.60613 0.11095  0.03412  -0.05431 215 GLY A CA  
1565 C C   . GLY A 208 ? 0.68433 0.50938 0.58042 0.10842  0.05076  -0.04250 215 GLY A C   
1566 O O   . GLY A 208 ? 0.66781 0.50959 0.57421 0.11786  0.06666  -0.03592 215 GLY A O   
1567 N N   . TYR A 209 ? 0.61111 0.46690 0.52493 0.09556  0.04633  -0.03962 216 TYR A N   
1568 C CA  . TYR A 209 ? 0.56755 0.47556 0.51215 0.09077  0.05986  -0.03133 216 TYR A CA  
1569 C C   . TYR A 209 ? 0.50855 0.44031 0.44406 0.08713  0.05793  -0.02884 216 TYR A C   
1570 O O   . TYR A 209 ? 0.56217 0.47091 0.48051 0.08232  0.04265  -0.03192 216 TYR A O   
1571 C CB  . TYR A 209 ? 0.51182 0.42804 0.50624 0.07183  0.05653  -0.02876 216 TYR A CB  
1572 C CG  . TYR A 209 ? 0.59953 0.49602 0.60548 0.07333  0.06023  -0.02747 216 TYR A CG  
1573 C CD1 . TYR A 209 ? 0.55425 0.47323 0.56300 0.08379  0.07839  -0.02153 216 TYR A CD1 
1574 C CD2 . TYR A 209 ? 0.59506 0.45117 0.60854 0.06330  0.04457  -0.03045 216 TYR A CD2 
1575 C CE1 . TYR A 209 ? 0.57033 0.47019 0.58778 0.08527  0.08267  -0.01699 216 TYR A CE1 
1576 C CE2 . TYR A 209 ? 0.58620 0.42317 0.61172 0.06237  0.04853  -0.02655 216 TYR A CE2 
1577 C CZ  . TYR A 209 ? 0.57906 0.43686 0.60562 0.07397  0.06850  -0.01904 216 TYR A CZ  
1578 O OH  . TYR A 209 ? 0.57280 0.41073 0.61011 0.07297  0.07328  -0.01192 216 TYR A OH  
1579 N N   . PRO A 210 ? 0.53840 0.51599 0.48372 0.08822  0.07215  -0.02221 217 PRO A N   
1580 C CA  . PRO A 210 ? 0.50778 0.50802 0.44617 0.08254  0.07140  -0.01689 217 PRO A CA  
1581 C C   . PRO A 210 ? 0.45817 0.45044 0.42555 0.06129  0.05678  -0.01569 217 PRO A C   
1582 O O   . PRO A 210 ? 0.44995 0.44943 0.45567 0.04962  0.05693  -0.01647 217 PRO A O   
1583 C CB  . PRO A 210 ? 0.46231 0.51418 0.41292 0.08461  0.08874  -0.01001 217 PRO A CB  
1584 C CG  . PRO A 210 ? 0.46275 0.52050 0.43059 0.08897  0.09640  -0.01210 217 PRO A CG  
1585 C CD  . PRO A 210 ? 0.53595 0.54667 0.49642 0.09432  0.08856  -0.01824 217 PRO A CD  
1586 N N   . ILE A 211 ? 0.48193 0.45920 0.42896 0.05839  0.04467  -0.01325 218 ILE A N   
1587 C CA  . ILE A 211 ? 0.47529 0.44558 0.44655 0.04130  0.02981  -0.00872 218 ILE A CA  
1588 C C   . ILE A 211 ? 0.55198 0.55013 0.51939 0.03576  0.03636  0.00247  218 ILE A C   
1589 O O   . ILE A 211 ? 0.59501 0.59604 0.52493 0.04323  0.03782  0.00790  218 ILE A O   
1590 C CB  . ILE A 211 ? 0.51014 0.44254 0.46199 0.04023  0.00772  -0.01163 218 ILE A CB  
1591 C CG1 . ILE A 211 ? 0.62231 0.52540 0.57278 0.04465  0.00176  -0.02246 218 ILE A CG1 
1592 C CG2 . ILE A 211 ? 0.50125 0.42954 0.48648 0.02442  -0.00848 -0.00485 218 ILE A CG2 
1593 C CD1 . ILE A 211 ? 0.56397 0.42874 0.49227 0.04152  -0.02267 -0.02764 218 ILE A CD1 
1594 N N   . THR A 212 ? 0.47930 0.49674 0.48414 0.02233  0.04098  0.00594  219 THR A N   
1595 C CA  . THR A 212 ? 0.51283 0.55574 0.52056 0.01273  0.04754  0.01701  219 THR A CA  
1596 C C   . THR A 212 ? 0.46651 0.49095 0.49374 -0.00135 0.03337  0.02477  219 THR A C   
1597 O O   . THR A 212 ? 0.43135 0.44265 0.49400 -0.00832 0.02732  0.01982  219 THR A O   
1598 C CB  . THR A 212 ? 0.50418 0.57957 0.53691 0.00631  0.06205  0.01424  219 THR A CB  
1599 O OG1 . THR A 212 ? 0.46790 0.56321 0.48351 0.02159  0.07439  0.00996  219 THR A OG1 
1600 C CG2 . THR A 212 ? 0.46208 0.56246 0.49999 -0.00767 0.06708  0.02595  219 THR A CG2 
1601 N N   . LEU A 213 ? 0.48174 0.50647 0.48594 -0.00387 0.02935  0.03840  220 LEU A N   
1602 C CA  . LEU A 213 ? 0.54715 0.55490 0.56725 -0.01608 0.01625  0.05024  220 LEU A CA  
1603 C C   . LEU A 213 ? 0.48306 0.50912 0.52616 -0.03172 0.02631  0.05884  220 LEU A C   
1604 O O   . LEU A 213 ? 0.52814 0.58073 0.55365 -0.03487 0.03763  0.06884  220 LEU A O   
1605 C CB  . LEU A 213 ? 0.52274 0.51887 0.50237 -0.01133 0.00534  0.06275  220 LEU A CB  
1606 C CG  . LEU A 213 ? 0.72124 0.70060 0.71241 -0.02220 -0.00917 0.07995  220 LEU A CG  
1607 C CD1 . LEU A 213 ? 0.52710 0.48424 0.56346 -0.02629 -0.02290 0.07428  220 LEU A CD1 
1608 C CD2 . LEU A 213 ? 0.69653 0.66448 0.64057 -0.01532 -0.02195 0.09090  220 LEU A CD2 
1609 N N   . PHE A 214 ? 0.46175 0.47360 0.54461 -0.04163 0.02247  0.05475  221 PHE A N   
1610 C CA  . PHE A 214 ? 0.50946 0.52746 0.61438 -0.05875 0.02889  0.06044  221 PHE A CA  
1611 C C   . PHE A 214 ? 0.60461 0.60356 0.70576 -0.06700 0.01863  0.08169  221 PHE A C   
1612 O O   . PHE A 214 ? 0.60723 0.57650 0.72314 -0.06452 0.00431  0.08541  221 PHE A O   
1613 C CB  . PHE A 214 ? 0.44477 0.44965 0.58869 -0.06328 0.03009  0.04501  221 PHE A CB  
1614 C CG  . PHE A 214 ? 0.47218 0.50142 0.61968 -0.06024 0.04305  0.02758  221 PHE A CG  
1615 C CD1 . PHE A 214 ? 0.54821 0.59238 0.67492 -0.04554 0.04696  0.02196  221 PHE A CD1 
1616 C CD2 . PHE A 214 ? 0.49963 0.53379 0.66894 -0.07175 0.05049  0.01672  221 PHE A CD2 
1617 C CE1 . PHE A 214 ? 0.51988 0.58620 0.64940 -0.04159 0.05838  0.00918  221 PHE A CE1 
1618 C CE2 . PHE A 214 ? 0.51956 0.57815 0.68886 -0.06864 0.06104  0.00204  221 PHE A CE2 
1619 C CZ  . PHE A 214 ? 0.43782 0.51388 0.58821 -0.05313 0.06515  -0.00008 221 PHE A CZ  
1620 N N   . VAL A 215 ? 0.51885 0.53715 0.60228 -0.07639 0.02594  0.09787  222 VAL A N   
1621 C CA  . VAL A 215 ? 0.63539 0.63684 0.71301 -0.08545 0.01791  0.12201  222 VAL A CA  
1622 C C   . VAL A 215 ? 0.60673 0.59162 0.72045 -0.10533 0.01897  0.12560  222 VAL A C   
1623 O O   . VAL A 215 ? 0.56118 0.56129 0.69274 -0.11635 0.02937  0.11324  222 VAL A O   
1624 C CB  . VAL A 215 ? 0.69430 0.72520 0.73270 -0.08537 0.02668  0.14078  222 VAL A CB  
1625 C CG1 . VAL A 215 ? 0.69262 0.73911 0.69466 -0.06391 0.02979  0.12955  222 VAL A CG1 
1626 C CG2 . VAL A 215 ? 0.61670 0.68204 0.66664 -0.10211 0.04295  0.14609  222 VAL A CG2 
1627 N N   . GLU A 216 ? 0.58162 0.53215 0.70527 -0.10943 0.00678  0.14189  223 GLU A N   
1628 C CA  . GLU A 216 ? 0.59675 0.51855 0.75479 -0.12532 0.00608  0.14336  223 GLU A CA  
1629 C C   . GLU A 216 ? 0.62145 0.55467 0.77552 -0.14901 0.01442  0.16283  223 GLU A C   
1630 O O   . GLU A 216 ? 0.66596 0.62588 0.79128 -0.15125 0.01897  0.18293  223 GLU A O   
1631 C CB  . GLU A 216 ? 0.63977 0.51833 0.81359 -0.11776 -0.01031 0.15488  223 GLU A CB  
1632 C CG  . GLU A 216 ? 0.63440 0.50513 0.82114 -0.09715 -0.01952 0.13800  223 GLU A CG  
1633 C CD  . GLU A 216 ? 0.76624 0.59744 0.98436 -0.09046 -0.03306 0.14580  223 GLU A CD  
1634 O OE1 . GLU A 216 ? 0.77027 0.57586 1.01853 -0.09706 -0.02796 0.13897  223 GLU A OE1 
1635 O OE2 . GLU A 216 ? 0.76241 0.58797 0.97465 -0.07783 -0.04939 0.15828  223 GLU A OE2 
1636 N N   . LYS A 217 ? 0.67191 0.58398 0.85521 -0.16733 0.01675  0.15652  224 LYS A N   
1637 C CA  . LYS A 217 ? 0.71057 0.63113 0.89749 -0.19519 0.02337  0.17330  224 LYS A CA  
1638 C C   . LYS A 217 ? 0.78428 0.65350 0.98541 -0.20742 0.01441  0.19569  224 LYS A C   
1639 O O   . LYS A 217 ? 0.93321 0.79040 1.11855 -0.19956 0.00695  0.22177  224 LYS A O   
1640 C CB  . LYS A 217 ? 0.64334 0.57856 0.84961 -0.21187 0.03139  0.14898  224 LYS A CB  
1641 C CG  . LYS A 217 ? 0.69854 0.67589 0.89564 -0.19643 0.03873  0.12456  224 LYS A CG  
1642 C CD  . LYS A 217 ? 0.62419 0.60932 0.83994 -0.21135 0.04326  0.09912  224 LYS A CD  
1643 C CE  . LYS A 217 ? 0.60645 0.53414 0.84498 -0.21242 0.03693  0.08091  224 LYS A CE  
1644 N NZ  . LYS A 217 ? 0.61354 0.52842 0.85391 -0.18363 0.03541  0.06307  224 LYS A NZ  
# 
