data_7H9R
# 
_entry.id   7H9R 
# 
_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   7H9R         pdb_00007h9r 10.2210/pdb7h9r/pdb 
WWPDB D_1001407202 ?            ?                   
# 
_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                        7H9R 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.recvd_initial_deposition_date   2024-07-10 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.pdb_format_compatible           N 
_pdbx_database_status.methods_development_category    ? 
# 
_pdbx_contact_author.id                 1 
_pdbx_contact_author.name_last          Yu 
_pdbx_contact_author.name_first         Feng 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.email              yufeng@sari.ac.cn 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-9502-3277 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Huang, L.' 1  ? 
'Wang, W.'  2  ? 
'Zhu, Z.'   3  ? 
'Li, Q.'    4  ? 
'Li, M.'    5  ? 
'Zhou, H.'  6  ? 
'Xu, Q.'    7  ? 
'Wen, W.'   8  ? 
'Wang, Q.'  9  ? 
'Yu, F.'    10 ? 
# 
_citation.id                        primary 
_citation.title                     
;Novel starting points for fragment-based drug design against human heat-shock protein 90 identified using crystallographic fragment screening.
;
_citation.journal_abbrev            Iucrj 
_citation.journal_volume            12 
_citation.page_first                177 
_citation.page_last                 187 
_citation.year                      2025 
_citation.journal_id_ASTM           ? 
_citation.country                   UK 
_citation.journal_id_ISSN           2052-2525 
_citation.journal_id_CSD            ? 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   39819741 
_citation.pdbx_database_id_DOI      10.1107/S2052252524012247 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.identifier_ORCID 
_citation_author.ordinal 
primary 'Huang, L.' 0009-0001-8431-0182 1  
primary 'Wang, W.'  ?                   2  
primary 'Zhu, Z.'   ?                   3  
primary 'Li, Q.'    ?                   4  
primary 'Li, M.'    ?                   5  
primary 'Zhou, H.'  ?                   6  
primary 'Xu, Q.'    0000-0002-7137-0768 7  
primary 'Wen, W.'   ?                   8  
primary 'Wang, Q.'  ?                   9  
primary 'Yu, F.'    0000-0002-9502-3277 10 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Heat shock protein HSP 90-alpha' 26859.117 1   3.6.4.10 ? ? ? 
2 non-polymer syn 'N-(3-ethynylphenyl)acetamide'    159.185   1   ?        ? ? ? 
3 water       nat water                             18.015    269 ?        ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        
;Heat shock 86 kDa,HSP 86,HSP86,Heat shock protein family C member 1,Lipopolysaccharide-associated protein 2,LAP-2,LPS-associated protein 2,Renal carcinoma antigen NY-REN-38
;
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;MDQPMEEEEVETFAFQAEIAQLMSLIINTFYSNKEIFLRELISNSSDALDKIRYESLTDPSKLDSGKELHINLIPNKQDR
TLTIVDTGIGMTKADLINNLGTIAKSGTKAFMEALQAGADISMIGQFGVGFYSAYLVAEKVTVITKHNDDEQYAWESSAG
GSFTVRTDTGEPMGRGTKVILHLKEDQTEYLEERRIKEIVKKHSQFIGYPITLFVEKERDKEVSDDEAELEHHHHHH
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MDQPMEEEEVETFAFQAEIAQLMSLIINTFYSNKEIFLRELISNSSDALDKIRYESLTDPSKLDSGKELHINLIPNKQDR
TLTIVDTGIGMTKADLINNLGTIAKSGTKAFMEALQAGADISMIGQFGVGFYSAYLVAEKVTVITKHNDDEQYAWESSAG
GSFTVRTDTGEPMGRGTKVILHLKEDQTEYLEERRIKEIVKKHSQFIGYPITLFVEKERDKEVSDDEAELEHHHHHH
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'N-(3-ethynylphenyl)acetamide' A1AX2 
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 
A1AX2 non-polymer         . 'N-(3-ethynylphenyl)acetamide' ? 'C10 H9 N O'     159.185 
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        A1AX2 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1AX2 
_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 A1AX2 1   301 301 A1AX2 CUJ A . 
C 3 HOH   1   401 98  HOH   HOH A . 
C 3 HOH   2   402 244 HOH   HOH A . 
C 3 HOH   3   403 242 HOH   HOH A . 
C 3 HOH   4   404 243 HOH   HOH A . 
C 3 HOH   5   405 258 HOH   HOH A . 
C 3 HOH   6   406 86  HOH   HOH A . 
C 3 HOH   7   407 259 HOH   HOH A . 
C 3 HOH   8   408 116 HOH   HOH A . 
C 3 HOH   9   409 52  HOH   HOH A . 
C 3 HOH   10  410 125 HOH   HOH A . 
C 3 HOH   11  411 173 HOH   HOH A . 
C 3 HOH   12  412 32  HOH   HOH A . 
C 3 HOH   13  413 19  HOH   HOH A . 
C 3 HOH   14  414 97  HOH   HOH A . 
C 3 HOH   15  415 88  HOH   HOH A . 
C 3 HOH   16  416 220 HOH   HOH A . 
C 3 HOH   17  417 96  HOH   HOH A . 
C 3 HOH   18  418 237 HOH   HOH A . 
C 3 HOH   19  419 215 HOH   HOH A . 
C 3 HOH   20  420 79  HOH   HOH A . 
C 3 HOH   21  421 94  HOH   HOH A . 
C 3 HOH   22  422 25  HOH   HOH A . 
C 3 HOH   23  423 21  HOH   HOH A . 
C 3 HOH   24  424 213 HOH   HOH A . 
C 3 HOH   25  425 93  HOH   HOH A . 
C 3 HOH   26  426 10  HOH   HOH A . 
C 3 HOH   27  427 23  HOH   HOH A . 
C 3 HOH   28  428 18  HOH   HOH A . 
C 3 HOH   29  429 64  HOH   HOH A . 
C 3 HOH   30  430 118 HOH   HOH A . 
C 3 HOH   31  431 50  HOH   HOH A . 
C 3 HOH   32  432 69  HOH   HOH A . 
C 3 HOH   33  433 2   HOH   HOH A . 
C 3 HOH   34  434 150 HOH   HOH A . 
C 3 HOH   35  435 130 HOH   HOH A . 
C 3 HOH   36  436 121 HOH   HOH A . 
C 3 HOH   37  437 187 HOH   HOH A . 
C 3 HOH   38  438 37  HOH   HOH A . 
C 3 HOH   39  439 174 HOH   HOH A . 
C 3 HOH   40  440 31  HOH   HOH A . 
C 3 HOH   41  441 20  HOH   HOH A . 
C 3 HOH   42  442 71  HOH   HOH A . 
C 3 HOH   43  443 110 HOH   HOH A . 
C 3 HOH   44  444 85  HOH   HOH A . 
C 3 HOH   45  445 127 HOH   HOH A . 
C 3 HOH   46  446 151 HOH   HOH A . 
C 3 HOH   47  447 28  HOH   HOH A . 
C 3 HOH   48  448 200 HOH   HOH A . 
C 3 HOH   49  449 34  HOH   HOH A . 
C 3 HOH   50  450 156 HOH   HOH A . 
C 3 HOH   51  451 178 HOH   HOH A . 
C 3 HOH   52  452 115 HOH   HOH A . 
C 3 HOH   53  453 99  HOH   HOH A . 
C 3 HOH   54  454 223 HOH   HOH A . 
C 3 HOH   55  455 209 HOH   HOH A . 
C 3 HOH   56  456 89  HOH   HOH A . 
C 3 HOH   57  457 265 HOH   HOH A . 
C 3 HOH   58  458 207 HOH   HOH A . 
C 3 HOH   59  459 263 HOH   HOH A . 
C 3 HOH   60  460 35  HOH   HOH A . 
C 3 HOH   61  461 106 HOH   HOH A . 
C 3 HOH   62  462 74  HOH   HOH A . 
C 3 HOH   63  463 40  HOH   HOH A . 
C 3 HOH   64  464 76  HOH   HOH A . 
C 3 HOH   65  465 109 HOH   HOH A . 
C 3 HOH   66  466 26  HOH   HOH A . 
C 3 HOH   67  467 55  HOH   HOH A . 
C 3 HOH   68  468 254 HOH   HOH A . 
C 3 HOH   69  469 36  HOH   HOH A . 
C 3 HOH   70  470 183 HOH   HOH A . 
C 3 HOH   71  471 123 HOH   HOH A . 
C 3 HOH   72  472 51  HOH   HOH A . 
C 3 HOH   73  473 227 HOH   HOH A . 
C 3 HOH   74  474 140 HOH   HOH A . 
C 3 HOH   75  475 201 HOH   HOH A . 
C 3 HOH   76  476 6   HOH   HOH A . 
C 3 HOH   77  477 80  HOH   HOH A . 
C 3 HOH   78  478 45  HOH   HOH A . 
C 3 HOH   79  479 29  HOH   HOH A . 
C 3 HOH   80  480 13  HOH   HOH A . 
C 3 HOH   81  481 22  HOH   HOH A . 
C 3 HOH   82  482 134 HOH   HOH A . 
C 3 HOH   83  483 54  HOH   HOH A . 
C 3 HOH   84  484 103 HOH   HOH A . 
C 3 HOH   85  485 132 HOH   HOH A . 
C 3 HOH   86  486 114 HOH   HOH A . 
C 3 HOH   87  487 15  HOH   HOH A . 
C 3 HOH   88  488 111 HOH   HOH A . 
C 3 HOH   89  489 100 HOH   HOH A . 
C 3 HOH   90  490 154 HOH   HOH A . 
C 3 HOH   91  491 5   HOH   HOH A . 
C 3 HOH   92  492 208 HOH   HOH A . 
C 3 HOH   93  493 4   HOH   HOH A . 
C 3 HOH   94  494 253 HOH   HOH A . 
C 3 HOH   95  495 90  HOH   HOH A . 
C 3 HOH   96  496 108 HOH   HOH A . 
C 3 HOH   97  497 233 HOH   HOH A . 
C 3 HOH   98  498 75  HOH   HOH A . 
C 3 HOH   99  499 12  HOH   HOH A . 
C 3 HOH   100 500 142 HOH   HOH A . 
C 3 HOH   101 501 39  HOH   HOH A . 
C 3 HOH   102 502 49  HOH   HOH A . 
C 3 HOH   103 503 87  HOH   HOH A . 
C 3 HOH   104 504 166 HOH   HOH A . 
C 3 HOH   105 505 255 HOH   HOH A . 
C 3 HOH   106 506 112 HOH   HOH A . 
C 3 HOH   107 507 72  HOH   HOH A . 
C 3 HOH   108 508 167 HOH   HOH A . 
C 3 HOH   109 509 128 HOH   HOH A . 
C 3 HOH   110 510 117 HOH   HOH A . 
C 3 HOH   111 511 92  HOH   HOH A . 
C 3 HOH   112 512 144 HOH   HOH A . 
C 3 HOH   113 513 7   HOH   HOH A . 
C 3 HOH   114 514 14  HOH   HOH A . 
C 3 HOH   115 515 53  HOH   HOH A . 
C 3 HOH   116 516 229 HOH   HOH A . 
C 3 HOH   117 517 84  HOH   HOH A . 
C 3 HOH   118 518 16  HOH   HOH A . 
C 3 HOH   119 519 250 HOH   HOH A . 
C 3 HOH   120 520 41  HOH   HOH A . 
C 3 HOH   121 521 168 HOH   HOH A . 
C 3 HOH   122 522 206 HOH   HOH A . 
C 3 HOH   123 523 179 HOH   HOH A . 
C 3 HOH   124 524 107 HOH   HOH A . 
C 3 HOH   125 525 216 HOH   HOH A . 
C 3 HOH   126 526 218 HOH   HOH A . 
C 3 HOH   127 527 139 HOH   HOH A . 
C 3 HOH   128 528 203 HOH   HOH A . 
C 3 HOH   129 529 131 HOH   HOH A . 
C 3 HOH   130 530 170 HOH   HOH A . 
C 3 HOH   131 531 17  HOH   HOH A . 
C 3 HOH   132 532 66  HOH   HOH A . 
C 3 HOH   133 533 11  HOH   HOH A . 
C 3 HOH   134 534 65  HOH   HOH A . 
C 3 HOH   135 535 147 HOH   HOH A . 
C 3 HOH   136 536 83  HOH   HOH A . 
C 3 HOH   137 537 30  HOH   HOH A . 
C 3 HOH   138 538 48  HOH   HOH A . 
C 3 HOH   139 539 138 HOH   HOH A . 
C 3 HOH   140 540 164 HOH   HOH A . 
C 3 HOH   141 541 70  HOH   HOH A . 
C 3 HOH   142 542 126 HOH   HOH A . 
C 3 HOH   143 543 165 HOH   HOH A . 
C 3 HOH   144 544 73  HOH   HOH A . 
C 3 HOH   145 545 91  HOH   HOH A . 
C 3 HOH   146 546 57  HOH   HOH A . 
C 3 HOH   147 547 24  HOH   HOH A . 
C 3 HOH   148 548 212 HOH   HOH A . 
C 3 HOH   149 549 60  HOH   HOH A . 
C 3 HOH   150 550 38  HOH   HOH A . 
C 3 HOH   151 551 61  HOH   HOH A . 
C 3 HOH   152 552 3   HOH   HOH A . 
C 3 HOH   153 553 145 HOH   HOH A . 
C 3 HOH   154 554 47  HOH   HOH A . 
C 3 HOH   155 555 262 HOH   HOH A . 
C 3 HOH   156 556 251 HOH   HOH A . 
C 3 HOH   157 557 122 HOH   HOH A . 
C 3 HOH   158 558 42  HOH   HOH A . 
C 3 HOH   159 559 62  HOH   HOH A . 
C 3 HOH   160 560 137 HOH   HOH A . 
C 3 HOH   161 561 230 HOH   HOH A . 
C 3 HOH   162 562 185 HOH   HOH A . 
C 3 HOH   163 563 214 HOH   HOH A . 
C 3 HOH   164 564 141 HOH   HOH A . 
C 3 HOH   165 565 129 HOH   HOH A . 
C 3 HOH   166 566 44  HOH   HOH A . 
C 3 HOH   167 567 248 HOH   HOH A . 
C 3 HOH   168 568 43  HOH   HOH A . 
C 3 HOH   169 569 8   HOH   HOH A . 
C 3 HOH   170 570 124 HOH   HOH A . 
C 3 HOH   171 571 27  HOH   HOH A . 
C 3 HOH   172 572 105 HOH   HOH A . 
C 3 HOH   173 573 204 HOH   HOH A . 
C 3 HOH   174 574 113 HOH   HOH A . 
C 3 HOH   175 575 59  HOH   HOH A . 
C 3 HOH   176 576 153 HOH   HOH A . 
C 3 HOH   177 577 162 HOH   HOH A . 
C 3 HOH   178 578 1   HOH   HOH A . 
C 3 HOH   179 579 77  HOH   HOH A . 
C 3 HOH   180 580 158 HOH   HOH A . 
C 3 HOH   181 581 58  HOH   HOH A . 
C 3 HOH   182 582 33  HOH   HOH A . 
C 3 HOH   183 583 9   HOH   HOH A . 
C 3 HOH   184 584 46  HOH   HOH A . 
C 3 HOH   185 585 135 HOH   HOH A . 
C 3 HOH   186 586 234 HOH   HOH A . 
C 3 HOH   187 587 219 HOH   HOH A . 
C 3 HOH   188 588 104 HOH   HOH A . 
C 3 HOH   189 589 175 HOH   HOH A . 
C 3 HOH   190 590 266 HOH   HOH A . 
C 3 HOH   191 591 240 HOH   HOH A . 
C 3 HOH   192 592 184 HOH   HOH A . 
C 3 HOH   193 593 149 HOH   HOH A . 
C 3 HOH   194 594 120 HOH   HOH A . 
C 3 HOH   195 595 269 HOH   HOH A . 
C 3 HOH   196 596 189 HOH   HOH A . 
C 3 HOH   197 597 256 HOH   HOH A . 
C 3 HOH   198 598 252 HOH   HOH A . 
C 3 HOH   199 599 136 HOH   HOH A . 
C 3 HOH   200 600 63  HOH   HOH A . 
C 3 HOH   201 601 232 HOH   HOH A . 
C 3 HOH   202 602 197 HOH   HOH A . 
C 3 HOH   203 603 181 HOH   HOH A . 
C 3 HOH   204 604 67  HOH   HOH A . 
C 3 HOH   205 605 146 HOH   HOH A . 
C 3 HOH   206 606 231 HOH   HOH A . 
C 3 HOH   207 607 238 HOH   HOH A . 
C 3 HOH   208 608 176 HOH   HOH A . 
C 3 HOH   209 609 160 HOH   HOH A . 
C 3 HOH   210 610 194 HOH   HOH A . 
C 3 HOH   211 611 222 HOH   HOH A . 
C 3 HOH   212 612 78  HOH   HOH A . 
C 3 HOH   213 613 157 HOH   HOH A . 
C 3 HOH   214 614 193 HOH   HOH A . 
C 3 HOH   215 615 182 HOH   HOH A . 
C 3 HOH   216 616 260 HOH   HOH A . 
C 3 HOH   217 617 241 HOH   HOH A . 
C 3 HOH   218 618 68  HOH   HOH A . 
C 3 HOH   219 619 264 HOH   HOH A . 
C 3 HOH   220 620 199 HOH   HOH A . 
C 3 HOH   221 621 257 HOH   HOH A . 
C 3 HOH   222 622 163 HOH   HOH A . 
C 3 HOH   223 623 159 HOH   HOH A . 
C 3 HOH   224 624 82  HOH   HOH A . 
C 3 HOH   225 625 188 HOH   HOH A . 
C 3 HOH   226 626 235 HOH   HOH A . 
C 3 HOH   227 627 192 HOH   HOH A . 
C 3 HOH   228 628 101 HOH   HOH A . 
C 3 HOH   229 629 228 HOH   HOH A . 
C 3 HOH   230 630 169 HOH   HOH A . 
C 3 HOH   231 631 268 HOH   HOH A . 
C 3 HOH   232 632 102 HOH   HOH A . 
C 3 HOH   233 633 224 HOH   HOH A . 
C 3 HOH   234 634 119 HOH   HOH A . 
C 3 HOH   235 635 245 HOH   HOH A . 
C 3 HOH   236 636 226 HOH   HOH A . 
C 3 HOH   237 637 191 HOH   HOH A . 
C 3 HOH   238 638 247 HOH   HOH A . 
C 3 HOH   239 639 95  HOH   HOH A . 
C 3 HOH   240 640 171 HOH   HOH A . 
C 3 HOH   241 641 152 HOH   HOH A . 
C 3 HOH   242 642 56  HOH   HOH A . 
C 3 HOH   243 643 196 HOH   HOH A . 
C 3 HOH   244 644 180 HOH   HOH A . 
C 3 HOH   245 645 161 HOH   HOH A . 
C 3 HOH   246 646 225 HOH   HOH A . 
C 3 HOH   247 647 172 HOH   HOH A . 
C 3 HOH   248 648 210 HOH   HOH A . 
C 3 HOH   249 649 246 HOH   HOH A . 
C 3 HOH   250 650 236 HOH   HOH A . 
C 3 HOH   251 651 190 HOH   HOH A . 
C 3 HOH   252 652 186 HOH   HOH A . 
C 3 HOH   253 653 211 HOH   HOH A . 
C 3 HOH   254 654 81  HOH   HOH A . 
C 3 HOH   255 655 143 HOH   HOH A . 
C 3 HOH   256 656 155 HOH   HOH A . 
C 3 HOH   257 657 133 HOH   HOH A . 
C 3 HOH   258 658 267 HOH   HOH A . 
C 3 HOH   259 659 249 HOH   HOH A . 
C 3 HOH   260 660 177 HOH   HOH A . 
C 3 HOH   261 661 221 HOH   HOH A . 
C 3 HOH   262 662 202 HOH   HOH A . 
C 3 HOH   263 663 239 HOH   HOH A . 
C 3 HOH   264 664 148 HOH   HOH A . 
C 3 HOH   265 665 205 HOH   HOH A . 
C 3 HOH   266 666 195 HOH   HOH A . 
C 3 HOH   267 667 217 HOH   HOH A . 
C 3 HOH   268 668 198 HOH   HOH A . 
C 3 HOH   269 669 261 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             593232.400 
_cell.length_a           66.320 
_cell.length_b           89.450 
_cell.length_c           100.000 
_cell.angle_beta         90.000 
_cell.angle_gamma        90.000 
_cell.angle_alpha        90.000 
_cell.entry_id           7H9R 
_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                         7H9R 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
# 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
_exptl.entry_id          7H9R 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_Matthews      2.88 
_exptl_crystal.density_percent_sol   57.23 
_exptl_crystal.density_meas          ? 
_exptl_crystal.description           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.pH              8.5 
_exptl_crystal_grow.temp            277 
_exptl_crystal_grow.pdbx_details    '100mM Tris-HCl pH 8.5, 22% PEG4000, 200mM MgCl2' 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_diffrn.id                     1 
_diffrn.crystal_id             1 
_diffrn.ambient_temp           100 
_diffrn.ambient_temp_details   ? 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               PIXEL 
_diffrn_detector.type                   'DECTRIS EIGER X 16M' 
_diffrn_detector.pdbx_collection_date   2024-01-13 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.pdbx_scattering_type             x-ray 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.monochromator                    Si111 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.97919 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.pdbx_synchrotron_beamline   BL10U2 
_diffrn_source.type                        'SSRF BEAMLINE BL10U2' 
_diffrn_source.pdbx_wavelength_list        0.97919 
_diffrn_source.pdbx_synchrotron_site       SSRF 
_diffrn_source.pdbx_wavelength             ? 
# 
_reflns.entry_id                     7H9R 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             29.780 
_reflns.d_resolution_high            1.690 
_reflns.number_obs                   33644 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         100.000 
_reflns.pdbx_Rmerge_I_obs            0.082 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        16.000 
_reflns.B_iso_Wilson_estimate        ? 
_reflns.pdbx_redundancy              12.500 
_reflns.pdbx_Rrim_I_all              0.085 
_reflns.pdbx_Rpim_I_all              0.024 
_reflns.pdbx_CC_half                 0.999 
_reflns.pdbx_netI_over_av_sigmaI     ? 
_reflns.pdbx_number_measured_all     419248 
_reflns.pdbx_scaling_rejects         9 
_reflns.pdbx_chi_squared             ? 
_reflns.Rmerge_F_all                 ? 
_reflns.Rmerge_F_obs                 ? 
_reflns.observed_criterion_F_max     ? 
_reflns.observed_criterion_F_min     ? 
_reflns.observed_criterion_I_max     ? 
_reflns.observed_criterion_I_min     ? 
_reflns.pdbx_d_res_high_opt          ? 
_reflns.pdbx_d_res_low_opt           ? 
_reflns.details                      ? 
# 
loop_
_reflns_shell.pdbx_diffrn_id 
_reflns_shell.pdbx_ordinal 
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_reflns_shell.number_measured_obs 
_reflns_shell.number_measured_all 
_reflns_shell.number_unique_obs 
_reflns_shell.pdbx_rejects 
_reflns_shell.Rmerge_I_obs 
_reflns_shell.meanI_over_sigI_obs 
_reflns_shell.pdbx_Rsym_value 
_reflns_shell.pdbx_chi_squared 
_reflns_shell.pdbx_redundancy 
_reflns_shell.percent_possible_obs 
_reflns_shell.pdbx_netI_over_sigmaI_obs 
_reflns_shell.number_possible 
_reflns_shell.number_unique_all 
_reflns_shell.Rmerge_F_all 
_reflns_shell.Rmerge_F_obs 
_reflns_shell.Rmerge_I_all 
_reflns_shell.meanI_over_sigI_all 
_reflns_shell.percent_possible_all 
_reflns_shell.pdbx_Rrim_I_all 
_reflns_shell.pdbx_Rpim_I_all 
_reflns_shell.pdbx_CC_half 
1 1 1.690 1.730  ? 27138 2442 ? 1.416 ? ? ? 11.100 ? 1.600  ? ? ? ? ? ? 100.000 1.484 0.441 0.693 
1 2 7.560 29.780 ? 4052  414  ? 0.037 ? ? ? 9.800  ? 35.700 ? ? ? ? ? ? 97.600  0.039 0.012 0.999 
# 
_refine.entry_id                                 7H9R 
_refine.pdbx_method_to_determine_struct          'FOURIER SYNTHESIS' 
_refine.ls_percent_reflns_R_free                 4.92 
_refine.pdbx_overall_phase_error                 18.6215 
_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                          0.1730 
_refine.B_iso_mean                               32.41 
_refine.ls_number_reflns_R_free                  1655 
_refine.ls_percent_reflns_obs                    99.94 
_refine.ls_R_factor_R_work                       0.1725 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_refine.ls_d_res_high                            1.69 
_refine.ls_number_reflns_obs                     33629 
_refine.pdbx_ls_sigma_F                          1.34 
_refine.ls_number_reflns_R_work                  31974 
_refine.ls_d_res_low                             26.64 
_refine.pdbx_stereochemistry_target_values       'GeoStd + Monomer Library + CDL v1.2' 
_refine.ls_R_factor_R_free                       0.1816 
_refine.overall_SU_ML                            0.1919 
_refine.pdbx_solvent_vdw_probe_radii             1.1000 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.solvent_model_param_ksol                 ? 
_refine.solvent_model_param_bsol                 ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.details                                  ? 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.overall_SU_B                             ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        1644 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         12 
_refine_hist.number_atoms_solvent             269 
_refine_hist.number_atoms_total               1925 
_refine_hist.d_res_high                       1.69 
_refine_hist.d_res_low                        26.64 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.type 
_refine_ls_restr.number 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
_refine_ls_restr.dev_ideal_target 
'X-RAY DIFFRACTION' f_bond_d           1682 0.0103 ? ? ? 
'X-RAY DIFFRACTION' f_angle_d          2266 1.0902 ? ? ? 
'X-RAY DIFFRACTION' f_chiral_restr     259  0.0688 ? ? ? 
'X-RAY DIFFRACTION' f_plane_restr      289  0.0099 ? ? ? 
'X-RAY DIFFRACTION' f_dihedral_angle_d 225  6.9209 ? ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.R_factor_R_free 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.R_factor_all 
'X-RAY DIFFRACTION' 1.69 1.74  2657 0.2980 99.93  0.3072 130 . . . . . 
'X-RAY DIFFRACTION' 1.74 1.80  2601 0.2543 99.96  0.2979 155 . . . . . 
'X-RAY DIFFRACTION' 1.80 1.86  2587 0.2193 99.96  0.2485 152 . . . . . 
'X-RAY DIFFRACTION' 1.86 1.93  2653 0.1981 99.96  0.2355 127 . . . . . 
'X-RAY DIFFRACTION' 1.93 2.02  2655 0.1824 99.96  0.2154 138 . . . . . 
'X-RAY DIFFRACTION' 2.02 2.13  2635 0.1794 100.00 0.2020 144 . . . . . 
'X-RAY DIFFRACTION' 2.13 2.26  2666 0.1636 100.00 0.1874 120 . . . . . 
'X-RAY DIFFRACTION' 2.26 2.44  2645 0.1794 100.00 0.2236 139 . . . . . 
'X-RAY DIFFRACTION' 2.44 2.68  2664 0.1845 99.96  0.1769 139 . . . . . 
'X-RAY DIFFRACTION' 2.68 3.07  2689 0.1825 100.00 0.2211 137 . . . . . 
'X-RAY DIFFRACTION' 3.07 3.87  2714 0.1560 99.96  0.1731 133 . . . . . 
'X-RAY DIFFRACTION' 3.87 26.64 2808 0.1546 99.59  0.1288 141 . . . . . 
# 
_struct.entry_id                  7H9R 
_struct.title                     'PanDDA analysis group deposition -- Crystal structure of HSP90N in complex with Fr14452' 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_details        ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7H9R 
_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              7H9R 
_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 7H9R MET A 1   ? UNP P07900 ? ? 'initiating methionine' 8   1 
1 7H9R LEU A 230 ? UNP P07900 ? ? 'expression tag'        237 2 
1 7H9R GLU A 231 ? UNP P07900 ? ? 'expression tag'        238 3 
1 7H9R HIS A 232 ? UNP P07900 ? ? 'expression tag'        239 4 
1 7H9R HIS A 233 ? UNP P07900 ? ? 'expression tag'        240 5 
1 7H9R HIS A 234 ? UNP P07900 ? ? 'expression tag'        241 6 
1 7H9R HIS A 235 ? UNP P07900 ? ? 'expression tag'        242 7 
1 7H9R HIS A 236 ? UNP P07900 ? ? 'expression tag'        243 8 
1 7H9R 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 ILE A 103 ? ALA A 117 ? ILE A 110 ALA A 124 1 ? 15 
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 GLU A 11  ? ALA A 14  ? GLU A 18  ALA A 21  
AA1 2 SER A 162 ? THR A 167 ? SER A 169 THR A 174 
AA1 3 TYR A 153 ? SER A 157 ? TYR A 160 SER A 164 
AA1 4 ALA A 138 ? LYS A 146 ? ALA A 145 LYS A 153 
AA1 5 GLY A 176 ? LEU A 183 ? GLY A 183 LEU A 190 
AA1 6 THR A 81  ? ASP A 86  ? THR A 88  ASP A 93  
AA1 7 ILE A 71  ? ASN A 76  ? ILE A 78  ASN A 83  
AA1 8 ILE A 211 ? LEU A 213 ? ILE A 218 LEU A 220 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N PHE A 13  ? N PHE A 20  O PHE A 163 ? O PHE A 170 
AA1 2 3 O ARG A 166 ? O ARG A 173 N ALA A 154 ? N ALA A 161 
AA1 3 4 O TRP A 155 ? O TRP A 162 N VAL A 143 ? N VAL A 150 
AA1 4 5 N THR A 142 ? N THR A 149 O ILE A 180 ? O ILE A 187 
AA1 5 6 O LEU A 181 ? O LEU A 188 N LEU A 82  ? N LEU A 89  
AA1 6 7 O 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                   7H9R 
_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 OD1 A ASN 105 ? ? O A HOH 401 ? ? 1.87 
2 1 OD1 A ASP 71  ? ? O A HOH 402 ? ? 1.92 
3 1 O   A HOH 448 ? ? O A HOH 548 ? ? 2.08 
4 1 OE1 A GLU 158 ? ? O A HOH 403 ? ? 2.13 
# 
loop_
_pdbx_validate_symm_contact.id 
_pdbx_validate_symm_contact.PDB_model_num 
_pdbx_validate_symm_contact.auth_atom_id_1 
_pdbx_validate_symm_contact.auth_asym_id_1 
_pdbx_validate_symm_contact.auth_comp_id_1 
_pdbx_validate_symm_contact.auth_seq_id_1 
_pdbx_validate_symm_contact.PDB_ins_code_1 
_pdbx_validate_symm_contact.label_alt_id_1 
_pdbx_validate_symm_contact.site_symmetry_1 
_pdbx_validate_symm_contact.auth_atom_id_2 
_pdbx_validate_symm_contact.auth_asym_id_2 
_pdbx_validate_symm_contact.auth_comp_id_2 
_pdbx_validate_symm_contact.auth_seq_id_2 
_pdbx_validate_symm_contact.PDB_ins_code_2 
_pdbx_validate_symm_contact.label_alt_id_2 
_pdbx_validate_symm_contact.site_symmetry_2 
_pdbx_validate_symm_contact.dist 
1 1 O A HOH 590 ? ? 1_555 O A HOH 598 ? ? 2_555 1.83 
2 1 O A HOH 609 ? ? 1_555 O A HOH 609 ? ? 2_555 2.03 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 TYR A 38  ? ? -163.15 109.01  
2 1 THR A 94  ? ? -103.90 41.48   
3 1 ILE A 110 ? ? -96.55  59.83   
4 1 ALA A 166 ? ? 63.52   -143.62 
# 
_pdbx_struct_special_symmetry.id              1 
_pdbx_struct_special_symmetry.PDB_model_num   1 
_pdbx_struct_special_symmetry.auth_asym_id    A 
_pdbx_struct_special_symmetry.auth_comp_id    HOH 
_pdbx_struct_special_symmetry.auth_seq_id     642 
_pdbx_struct_special_symmetry.PDB_ins_code    ? 
_pdbx_struct_special_symmetry.label_asym_id   C 
_pdbx_struct_special_symmetry.label_comp_id   HOH 
_pdbx_struct_special_symmetry.label_seq_id    . 
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z               
2 x,-y,-z             
3 -x,y,-z             
4 -x,-y,z             
5 x+1/2,y+1/2,z+1/2   
6 x+1/2,-y+1/2,-z+1/2 
7 -x+1/2,y+1/2,-z+1/2 
8 -x+1/2,-y+1/2,z+1/2 
# 
loop_
_pdbx_refine_tls.id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][3] 
1 ? 'X-RAY DIFFRACTION' refined 12.4273216438  -17.9257470137 -18.7765703259 0.192400064631 0.249809086082 0.254830012552 
0.00880668909612   -0.0217356905516  -0.0252741583955  1.73068274927 1.49697811495 2.88149028169 -0.388569633641   -1.30312156606  
0.0890157038929   0.0806270187745 -0.127187968283 -0.0685687092576 -0.012980285148 -0.0659944033646 -0.116564765833   
0.046803737736   0.154989638683    -0.03527755312    
2 ? 'X-RAY DIFFRACTION' refined -5.20208964905 -6.27471520433 -20.9607522949 0.245460673698 0.221472973622 0.260637037067 
-0.00313933266812  -0.00381710389625 -0.0252376828943  1.4723300676  2.74211175431 4.22663160324 -0.839696509589   1.57630214917   
-2.08335359431    -0.187128283173 0.0554003536654 0.197567422855   0.192796047596  -0.0516473662344 -0.0586123154647  
-0.493984478293  0.213872915384    0.154903301675    
3 ? 'X-RAY DIFFRACTION' refined -10.1840374748 -15.0129574877 -25.1912310033 0.218093921553 0.229894927043 0.251084259789 
-0.00336790301073  -0.0475987899662  -0.0226537574261  1.37952164719 2.61359960923 1.90511044108 -0.146902636475   -0.500168205226 
-0.334065762774   0.0620139035172 0.169267749496  -0.101322730542  -0.237905358826 0.0155289685856  0.292397942761    
0.102264340938   -0.20985111786    -0.102155688762   
4 ? 'X-RAY DIFFRACTION' refined 10.6128040679  -7.00303541021 -18.1297526608 0.243755157699 0.261605080981 0.296627703887 
-0.0258978191216   0.0179978620844   -0.012835258349   3.89013677945 2.93740161688 4.25677897718 0.495644395812    0.156906590116  
1.74483217907     0.0945530602527 -0.454733443655 0.318574229466   0.16924909527   -0.0526679269982 -0.130531321344   
-0.297972670973  0.490918080331    -0.0567489405641  
5 ? 'X-RAY DIFFRACTION' refined 0.851958636297 -19.3435589732 -27.9181565913 0.234708065516 0.219877934151 0.255049489876 
0.00368974671589   -0.0111198862438  -0.031058297716   1.68061582398 1.43277557258 1.45382626891 -0.541096164974   -0.124445116614 
-0.00116001335314 0.134093831251  0.198667953754  -0.263713419715  -0.16221875031  -0.0557921942216 0.162863385614    
0.257141639696   -0.00979316555907 -0.0804560044169  
6 ? 'X-RAY DIFFRACTION' refined -2.61350379154 -23.7208099292 -13.6938073356 0.297923209071 0.256751525101 0.296292036093 
0.0052340783109    -0.00601509013295 0.0119156377168   1.64813574558 1.83215882253 2.89558760153 -0.00833111333143 -0.059146442751 
-0.732076054538   0.0401945062431 -0.181141654675 -0.226942560866  0.15436638274   0.0247074475129  0.000372762562233 
0.268679264648   -0.0428559977372  -0.11560411219    
7 ? 'X-RAY DIFFRACTION' refined -12.227942507  -14.2430562004 -10.363972758  0.205425378452 0.25762144335  0.211460099113 
-0.000694995531015 0.00689521339897  -0.00534751190474 2.32948344486 1.53264742922 2.66429190462 -0.813642604747   0.398490344281  
-0.585169790839   0.0109882637819 -0.234626022956 -0.163549869726  0.215093340064  0.035089219509   0.125320991968    
-0.0274479361575 -0.296599556799   -0.00819765915869 
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
1 1 'X-RAY DIFFRACTION' A 16  A 1   A 40  A 25  . 
;chain 'A' and (resid 16 through 40 )
;
2 2 'X-RAY DIFFRACTION' A 41  A 26  A 65  A 50  . 
;chain 'A' and (resid 41 through 65 )
;
3 3 'X-RAY DIFFRACTION' A 66  A 51  A 99  A 84  . 
;chain 'A' and (resid 66 through 99 )
;
4 4 'X-RAY DIFFRACTION' A 100 A 85  A 136 A 121 . 
;chain 'A' and (resid 100 through 136 )
;
5 5 'X-RAY DIFFRACTION' A 137 A 122 A 182 A 167 . 
;chain 'A' and (resid 137 through 182 )
;
6 6 'X-RAY DIFFRACTION' A 183 A 168 A 199 A 184 . 
;chain 'A' and (resid 183 through 199 )
;
7 7 'X-RAY DIFFRACTION' A 200 A 185 A 224 A 209 . 
;chain 'A' and (resid 200 through 224 )
;
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A MET 8   ? A MET 1   
2  1 Y 1 A ASP 9   ? A ASP 2   
3  1 Y 1 A GLN 10  ? A GLN 3   
4  1 Y 1 A PRO 11  ? A PRO 4   
5  1 Y 1 A MET 12  ? A MET 5   
6  1 Y 1 A GLU 13  ? A GLU 6   
7  1 Y 1 A GLU 14  ? A GLU 7   
8  1 Y 1 A GLU 15  ? A GLU 8   
9  1 Y 1 A GLU 225 ? A GLU 218 
10 1 Y 1 A ARG 226 ? A ARG 219 
11 1 Y 1 A ASP 227 ? A ASP 220 
12 1 Y 1 A LYS 228 ? A LYS 221 
13 1 Y 1 A GLU 229 ? A GLU 222 
14 1 Y 1 A VAL 230 ? A VAL 223 
15 1 Y 1 A SER 231 ? A SER 224 
16 1 Y 1 A ASP 232 ? A ASP 225 
17 1 Y 1 A ASP 233 ? A ASP 226 
18 1 Y 1 A GLU 234 ? A GLU 227 
19 1 Y 1 A ALA 235 ? A ALA 228 
20 1 Y 1 A GLU 236 ? A GLU 229 
21 1 Y 1 A LEU 237 ? A LEU 230 
22 1 Y 1 A GLU 238 ? A GLU 231 
23 1 Y 1 A HIS 239 ? A HIS 232 
24 1 Y 1 A HIS 240 ? A HIS 233 
25 1 Y 1 A HIS 241 ? A HIS 234 
26 1 Y 1 A HIS 242 ? A HIS 235 
27 1 Y 1 A HIS 243 ? A HIS 236 
28 1 Y 1 A HIS 244 ? A HIS 237 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
A1AX2 C1   C N N 1   
A1AX2 C10  C Y N 2   
A1AX2 C2   C N N 3   
A1AX2 C3   C Y N 4   
A1AX2 C4   C Y N 5   
A1AX2 C5   C Y N 6   
A1AX2 C6   C Y N 7   
A1AX2 C7   C Y N 8   
A1AX2 C8   C N N 9   
A1AX2 C9   C N N 10  
A1AX2 N1   N N N 11  
A1AX2 O1   O N N 12  
A1AX2 H1   H N N 13  
A1AX2 H10  H N N 14  
A1AX2 H4   H N N 15  
A1AX2 H5   H N N 16  
A1AX2 H6   H N N 17  
A1AX2 H92  H N N 18  
A1AX2 H91  H N N 19  
A1AX2 H93  H N N 20  
A1AX2 HN1  H N N 21  
ALA   N    N N N 22  
ALA   CA   C N S 23  
ALA   C    C N N 24  
ALA   O    O N N 25  
ALA   CB   C N N 26  
ALA   OXT  O N N 27  
ALA   H    H N N 28  
ALA   H2   H N N 29  
ALA   HA   H N N 30  
ALA   HB1  H N N 31  
ALA   HB2  H N N 32  
ALA   HB3  H N N 33  
ALA   HXT  H N N 34  
ARG   N    N N N 35  
ARG   CA   C N S 36  
ARG   C    C N N 37  
ARG   O    O N N 38  
ARG   CB   C N N 39  
ARG   CG   C N N 40  
ARG   CD   C N N 41  
ARG   NE   N N N 42  
ARG   CZ   C N N 43  
ARG   NH1  N N N 44  
ARG   NH2  N N N 45  
ARG   OXT  O N N 46  
ARG   H    H N N 47  
ARG   H2   H N N 48  
ARG   HA   H N N 49  
ARG   HB2  H N N 50  
ARG   HB3  H N N 51  
ARG   HG2  H N N 52  
ARG   HG3  H N N 53  
ARG   HD2  H N N 54  
ARG   HD3  H N N 55  
ARG   HE   H N N 56  
ARG   HH11 H N N 57  
ARG   HH12 H N N 58  
ARG   HH21 H N N 59  
ARG   HH22 H N N 60  
ARG   HXT  H N N 61  
ASN   N    N N N 62  
ASN   CA   C N S 63  
ASN   C    C N N 64  
ASN   O    O N N 65  
ASN   CB   C N N 66  
ASN   CG   C N N 67  
ASN   OD1  O N N 68  
ASN   ND2  N N N 69  
ASN   OXT  O N N 70  
ASN   H    H N N 71  
ASN   H2   H N N 72  
ASN   HA   H N N 73  
ASN   HB2  H N N 74  
ASN   HB3  H N N 75  
ASN   HD21 H N N 76  
ASN   HD22 H N N 77  
ASN   HXT  H N N 78  
ASP   N    N N N 79  
ASP   CA   C N S 80  
ASP   C    C N N 81  
ASP   O    O N N 82  
ASP   CB   C N N 83  
ASP   CG   C N N 84  
ASP   OD1  O N N 85  
ASP   OD2  O N N 86  
ASP   OXT  O N N 87  
ASP   H    H N N 88  
ASP   H2   H N N 89  
ASP   HA   H N N 90  
ASP   HB2  H N N 91  
ASP   HB3  H N N 92  
ASP   HD2  H N N 93  
ASP   HXT  H N N 94  
GLN   N    N N N 95  
GLN   CA   C N S 96  
GLN   C    C N N 97  
GLN   O    O N N 98  
GLN   CB   C N N 99  
GLN   CG   C N N 100 
GLN   CD   C N N 101 
GLN   OE1  O N N 102 
GLN   NE2  N N N 103 
GLN   OXT  O N N 104 
GLN   H    H N N 105 
GLN   H2   H N N 106 
GLN   HA   H N N 107 
GLN   HB2  H N N 108 
GLN   HB3  H N N 109 
GLN   HG2  H N N 110 
GLN   HG3  H N N 111 
GLN   HE21 H N N 112 
GLN   HE22 H N N 113 
GLN   HXT  H N N 114 
GLU   N    N N N 115 
GLU   CA   C N S 116 
GLU   C    C N N 117 
GLU   O    O N N 118 
GLU   CB   C N N 119 
GLU   CG   C N N 120 
GLU   CD   C N N 121 
GLU   OE1  O N N 122 
GLU   OE2  O N N 123 
GLU   OXT  O N N 124 
GLU   H    H N N 125 
GLU   H2   H N N 126 
GLU   HA   H N N 127 
GLU   HB2  H N N 128 
GLU   HB3  H N N 129 
GLU   HG2  H N N 130 
GLU   HG3  H N N 131 
GLU   HE2  H N N 132 
GLU   HXT  H N N 133 
GLY   N    N N N 134 
GLY   CA   C N N 135 
GLY   C    C N N 136 
GLY   O    O N N 137 
GLY   OXT  O N N 138 
GLY   H    H N N 139 
GLY   H2   H N N 140 
GLY   HA2  H N N 141 
GLY   HA3  H N N 142 
GLY   HXT  H N N 143 
HIS   N    N N N 144 
HIS   CA   C N S 145 
HIS   C    C N N 146 
HIS   O    O N N 147 
HIS   CB   C N N 148 
HIS   CG   C Y N 149 
HIS   ND1  N Y N 150 
HIS   CD2  C Y N 151 
HIS   CE1  C Y N 152 
HIS   NE2  N Y N 153 
HIS   OXT  O N N 154 
HIS   H    H N N 155 
HIS   H2   H N N 156 
HIS   HA   H N N 157 
HIS   HB2  H N N 158 
HIS   HB3  H N N 159 
HIS   HD1  H N N 160 
HIS   HD2  H N N 161 
HIS   HE1  H N N 162 
HIS   HE2  H N N 163 
HIS   HXT  H N N 164 
HOH   O    O N N 165 
HOH   H1   H N N 166 
HOH   H2   H N N 167 
ILE   N    N N N 168 
ILE   CA   C N S 169 
ILE   C    C N N 170 
ILE   O    O N N 171 
ILE   CB   C N S 172 
ILE   CG1  C N N 173 
ILE   CG2  C N N 174 
ILE   CD1  C N N 175 
ILE   OXT  O N N 176 
ILE   H    H N N 177 
ILE   H2   H N N 178 
ILE   HA   H N N 179 
ILE   HB   H N N 180 
ILE   HG12 H N N 181 
ILE   HG13 H N N 182 
ILE   HG21 H N N 183 
ILE   HG22 H N N 184 
ILE   HG23 H N N 185 
ILE   HD11 H N N 186 
ILE   HD12 H N N 187 
ILE   HD13 H N N 188 
ILE   HXT  H N N 189 
LEU   N    N N N 190 
LEU   CA   C N S 191 
LEU   C    C N N 192 
LEU   O    O N N 193 
LEU   CB   C N N 194 
LEU   CG   C N N 195 
LEU   CD1  C N N 196 
LEU   CD2  C N N 197 
LEU   OXT  O N N 198 
LEU   H    H N N 199 
LEU   H2   H N N 200 
LEU   HA   H N N 201 
LEU   HB2  H N N 202 
LEU   HB3  H N N 203 
LEU   HG   H N N 204 
LEU   HD11 H N N 205 
LEU   HD12 H N N 206 
LEU   HD13 H N N 207 
LEU   HD21 H N N 208 
LEU   HD22 H N N 209 
LEU   HD23 H N N 210 
LEU   HXT  H N N 211 
LYS   N    N N N 212 
LYS   CA   C N S 213 
LYS   C    C N N 214 
LYS   O    O N N 215 
LYS   CB   C N N 216 
LYS   CG   C N N 217 
LYS   CD   C N N 218 
LYS   CE   C N N 219 
LYS   NZ   N N N 220 
LYS   OXT  O N N 221 
LYS   H    H N N 222 
LYS   H2   H N N 223 
LYS   HA   H N N 224 
LYS   HB2  H N N 225 
LYS   HB3  H N N 226 
LYS   HG2  H N N 227 
LYS   HG3  H N N 228 
LYS   HD2  H N N 229 
LYS   HD3  H N N 230 
LYS   HE2  H N N 231 
LYS   HE3  H N N 232 
LYS   HZ1  H N N 233 
LYS   HZ2  H N N 234 
LYS   HZ3  H N N 235 
LYS   HXT  H N N 236 
MET   N    N N N 237 
MET   CA   C N S 238 
MET   C    C N N 239 
MET   O    O N N 240 
MET   CB   C N N 241 
MET   CG   C N N 242 
MET   SD   S N N 243 
MET   CE   C N N 244 
MET   OXT  O N N 245 
MET   H    H N N 246 
MET   H2   H N N 247 
MET   HA   H N N 248 
MET   HB2  H N N 249 
MET   HB3  H N N 250 
MET   HG2  H N N 251 
MET   HG3  H N N 252 
MET   HE1  H N N 253 
MET   HE2  H N N 254 
MET   HE3  H N N 255 
MET   HXT  H N N 256 
PHE   N    N N N 257 
PHE   CA   C N S 258 
PHE   C    C N N 259 
PHE   O    O N N 260 
PHE   CB   C N N 261 
PHE   CG   C Y N 262 
PHE   CD1  C Y N 263 
PHE   CD2  C Y N 264 
PHE   CE1  C Y N 265 
PHE   CE2  C Y N 266 
PHE   CZ   C Y N 267 
PHE   OXT  O N N 268 
PHE   H    H N N 269 
PHE   H2   H N N 270 
PHE   HA   H N N 271 
PHE   HB2  H N N 272 
PHE   HB3  H N N 273 
PHE   HD1  H N N 274 
PHE   HD2  H N N 275 
PHE   HE1  H N N 276 
PHE   HE2  H N N 277 
PHE   HZ   H N N 278 
PHE   HXT  H N N 279 
PRO   N    N N N 280 
PRO   CA   C N S 281 
PRO   C    C N N 282 
PRO   O    O N N 283 
PRO   CB   C N N 284 
PRO   CG   C N N 285 
PRO   CD   C N N 286 
PRO   OXT  O N N 287 
PRO   H    H N N 288 
PRO   HA   H N N 289 
PRO   HB2  H N N 290 
PRO   HB3  H N N 291 
PRO   HG2  H N N 292 
PRO   HG3  H N N 293 
PRO   HD2  H N N 294 
PRO   HD3  H N N 295 
PRO   HXT  H N N 296 
SER   N    N N N 297 
SER   CA   C N S 298 
SER   C    C N N 299 
SER   O    O N N 300 
SER   CB   C N N 301 
SER   OG   O N N 302 
SER   OXT  O N N 303 
SER   H    H N N 304 
SER   H2   H N N 305 
SER   HA   H N N 306 
SER   HB2  H N N 307 
SER   HB3  H N N 308 
SER   HG   H N N 309 
SER   HXT  H N N 310 
THR   N    N N N 311 
THR   CA   C N S 312 
THR   C    C N N 313 
THR   O    O N N 314 
THR   CB   C N R 315 
THR   OG1  O N N 316 
THR   CG2  C N N 317 
THR   OXT  O N N 318 
THR   H    H N N 319 
THR   H2   H N N 320 
THR   HA   H N N 321 
THR   HB   H N N 322 
THR   HG1  H N N 323 
THR   HG21 H N N 324 
THR   HG22 H N N 325 
THR   HG23 H N N 326 
THR   HXT  H N N 327 
TRP   N    N N N 328 
TRP   CA   C N S 329 
TRP   C    C N N 330 
TRP   O    O N N 331 
TRP   CB   C N N 332 
TRP   CG   C Y N 333 
TRP   CD1  C Y N 334 
TRP   CD2  C Y N 335 
TRP   NE1  N Y N 336 
TRP   CE2  C Y N 337 
TRP   CE3  C Y N 338 
TRP   CZ2  C Y N 339 
TRP   CZ3  C Y N 340 
TRP   CH2  C Y N 341 
TRP   OXT  O N N 342 
TRP   H    H N N 343 
TRP   H2   H N N 344 
TRP   HA   H N N 345 
TRP   HB2  H N N 346 
TRP   HB3  H N N 347 
TRP   HD1  H N N 348 
TRP   HE1  H N N 349 
TRP   HE3  H N N 350 
TRP   HZ2  H N N 351 
TRP   HZ3  H N N 352 
TRP   HH2  H N N 353 
TRP   HXT  H N N 354 
TYR   N    N N N 355 
TYR   CA   C N S 356 
TYR   C    C N N 357 
TYR   O    O N N 358 
TYR   CB   C N N 359 
TYR   CG   C Y N 360 
TYR   CD1  C Y N 361 
TYR   CD2  C Y N 362 
TYR   CE1  C Y N 363 
TYR   CE2  C Y N 364 
TYR   CZ   C Y N 365 
TYR   OH   O N N 366 
TYR   OXT  O N N 367 
TYR   H    H N N 368 
TYR   H2   H N N 369 
TYR   HA   H N N 370 
TYR   HB2  H N N 371 
TYR   HB3  H N N 372 
TYR   HD1  H N N 373 
TYR   HD2  H N N 374 
TYR   HE1  H N N 375 
TYR   HE2  H N N 376 
TYR   HH   H N N 377 
TYR   HXT  H N N 378 
VAL   N    N N N 379 
VAL   CA   C N S 380 
VAL   C    C N N 381 
VAL   O    O N N 382 
VAL   CB   C N N 383 
VAL   CG1  C N N 384 
VAL   CG2  C N N 385 
VAL   OXT  O N N 386 
VAL   H    H N N 387 
VAL   H2   H N N 388 
VAL   HA   H N N 389 
VAL   HB   H N N 390 
VAL   HG11 H N N 391 
VAL   HG12 H N N 392 
VAL   HG13 H N N 393 
VAL   HG21 H N N 394 
VAL   HG22 H N N 395 
VAL   HG23 H N N 396 
VAL   HXT  H N N 397 
# 
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 
A1AX2 C1  C2   trip N N 1   
A1AX2 C2  C3   sing N N 2   
A1AX2 C3  C4   doub Y N 3   
A1AX2 C3  C10  sing Y N 4   
A1AX2 C4  C5   sing Y N 5   
A1AX2 C5  C6   doub Y N 6   
A1AX2 C6  C7   sing Y N 7   
A1AX2 C7  N1   sing N N 8   
A1AX2 C7  C10  doub Y N 9   
A1AX2 N1  C8   sing N N 10  
A1AX2 C8  C9   sing N N 11  
A1AX2 C8  O1   doub N N 12  
A1AX2 C1  H1   sing N N 13  
A1AX2 C10 H10  sing N N 14  
A1AX2 C4  H4   sing N N 15  
A1AX2 C5  H5   sing N N 16  
A1AX2 C6  H6   sing N N 17  
A1AX2 C9  H92  sing N N 18  
A1AX2 C9  H91  sing N N 19  
A1AX2 C9  H93  sing N N 20  
A1AX2 N1  HN1  sing N N 21  
ALA   N   CA   sing N N 22  
ALA   N   H    sing N N 23  
ALA   N   H2   sing N N 24  
ALA   CA  C    sing N N 25  
ALA   CA  CB   sing N N 26  
ALA   CA  HA   sing N N 27  
ALA   C   O    doub N N 28  
ALA   C   OXT  sing N N 29  
ALA   CB  HB1  sing N N 30  
ALA   CB  HB2  sing N N 31  
ALA   CB  HB3  sing N N 32  
ALA   OXT HXT  sing N N 33  
ARG   N   CA   sing N N 34  
ARG   N   H    sing N N 35  
ARG   N   H2   sing N N 36  
ARG   CA  C    sing N N 37  
ARG   CA  CB   sing N N 38  
ARG   CA  HA   sing N N 39  
ARG   C   O    doub N N 40  
ARG   C   OXT  sing N N 41  
ARG   CB  CG   sing N N 42  
ARG   CB  HB2  sing N N 43  
ARG   CB  HB3  sing N N 44  
ARG   CG  CD   sing N N 45  
ARG   CG  HG2  sing N N 46  
ARG   CG  HG3  sing N N 47  
ARG   CD  NE   sing N N 48  
ARG   CD  HD2  sing N N 49  
ARG   CD  HD3  sing N N 50  
ARG   NE  CZ   sing N N 51  
ARG   NE  HE   sing N N 52  
ARG   CZ  NH1  sing N N 53  
ARG   CZ  NH2  doub N N 54  
ARG   NH1 HH11 sing N N 55  
ARG   NH1 HH12 sing N N 56  
ARG   NH2 HH21 sing N N 57  
ARG   NH2 HH22 sing N N 58  
ARG   OXT HXT  sing N N 59  
ASN   N   CA   sing N N 60  
ASN   N   H    sing N N 61  
ASN   N   H2   sing N N 62  
ASN   CA  C    sing N N 63  
ASN   CA  CB   sing N N 64  
ASN   CA  HA   sing N N 65  
ASN   C   O    doub N N 66  
ASN   C   OXT  sing N N 67  
ASN   CB  CG   sing N N 68  
ASN   CB  HB2  sing N N 69  
ASN   CB  HB3  sing N N 70  
ASN   CG  OD1  doub N N 71  
ASN   CG  ND2  sing N N 72  
ASN   ND2 HD21 sing N N 73  
ASN   ND2 HD22 sing N N 74  
ASN   OXT HXT  sing N N 75  
ASP   N   CA   sing N N 76  
ASP   N   H    sing N N 77  
ASP   N   H2   sing N N 78  
ASP   CA  C    sing N N 79  
ASP   CA  CB   sing N N 80  
ASP   CA  HA   sing N N 81  
ASP   C   O    doub N N 82  
ASP   C   OXT  sing N N 83  
ASP   CB  CG   sing N N 84  
ASP   CB  HB2  sing N N 85  
ASP   CB  HB3  sing N N 86  
ASP   CG  OD1  doub N N 87  
ASP   CG  OD2  sing N N 88  
ASP   OD2 HD2  sing N N 89  
ASP   OXT HXT  sing N N 90  
GLN   N   CA   sing N N 91  
GLN   N   H    sing N N 92  
GLN   N   H2   sing N N 93  
GLN   CA  C    sing N N 94  
GLN   CA  CB   sing N N 95  
GLN   CA  HA   sing N N 96  
GLN   C   O    doub N N 97  
GLN   C   OXT  sing N N 98  
GLN   CB  CG   sing N N 99  
GLN   CB  HB2  sing N N 100 
GLN   CB  HB3  sing N N 101 
GLN   CG  CD   sing N N 102 
GLN   CG  HG2  sing N N 103 
GLN   CG  HG3  sing N N 104 
GLN   CD  OE1  doub N N 105 
GLN   CD  NE2  sing N N 106 
GLN   NE2 HE21 sing N N 107 
GLN   NE2 HE22 sing N N 108 
GLN   OXT HXT  sing N N 109 
GLU   N   CA   sing N N 110 
GLU   N   H    sing N N 111 
GLU   N   H2   sing N N 112 
GLU   CA  C    sing N N 113 
GLU   CA  CB   sing N N 114 
GLU   CA  HA   sing N N 115 
GLU   C   O    doub N N 116 
GLU   C   OXT  sing N N 117 
GLU   CB  CG   sing N N 118 
GLU   CB  HB2  sing N N 119 
GLU   CB  HB3  sing N N 120 
GLU   CG  CD   sing N N 121 
GLU   CG  HG2  sing N N 122 
GLU   CG  HG3  sing N N 123 
GLU   CD  OE1  doub N N 124 
GLU   CD  OE2  sing N N 125 
GLU   OE2 HE2  sing N N 126 
GLU   OXT HXT  sing N N 127 
GLY   N   CA   sing N N 128 
GLY   N   H    sing N N 129 
GLY   N   H2   sing N N 130 
GLY   CA  C    sing N N 131 
GLY   CA  HA2  sing N N 132 
GLY   CA  HA3  sing N N 133 
GLY   C   O    doub N N 134 
GLY   C   OXT  sing N N 135 
GLY   OXT HXT  sing N N 136 
HIS   N   CA   sing N N 137 
HIS   N   H    sing N N 138 
HIS   N   H2   sing N N 139 
HIS   CA  C    sing N N 140 
HIS   CA  CB   sing N N 141 
HIS   CA  HA   sing N N 142 
HIS   C   O    doub N N 143 
HIS   C   OXT  sing N N 144 
HIS   CB  CG   sing N N 145 
HIS   CB  HB2  sing N N 146 
HIS   CB  HB3  sing N N 147 
HIS   CG  ND1  sing Y N 148 
HIS   CG  CD2  doub Y N 149 
HIS   ND1 CE1  doub Y N 150 
HIS   ND1 HD1  sing N N 151 
HIS   CD2 NE2  sing Y N 152 
HIS   CD2 HD2  sing N N 153 
HIS   CE1 NE2  sing Y N 154 
HIS   CE1 HE1  sing N N 155 
HIS   NE2 HE2  sing N N 156 
HIS   OXT HXT  sing N N 157 
HOH   O   H1   sing N N 158 
HOH   O   H2   sing N N 159 
ILE   N   CA   sing N N 160 
ILE   N   H    sing N N 161 
ILE   N   H2   sing N N 162 
ILE   CA  C    sing N N 163 
ILE   CA  CB   sing N N 164 
ILE   CA  HA   sing N N 165 
ILE   C   O    doub N N 166 
ILE   C   OXT  sing N N 167 
ILE   CB  CG1  sing N N 168 
ILE   CB  CG2  sing N N 169 
ILE   CB  HB   sing N N 170 
ILE   CG1 CD1  sing N N 171 
ILE   CG1 HG12 sing N N 172 
ILE   CG1 HG13 sing N N 173 
ILE   CG2 HG21 sing N N 174 
ILE   CG2 HG22 sing N N 175 
ILE   CG2 HG23 sing N N 176 
ILE   CD1 HD11 sing N N 177 
ILE   CD1 HD12 sing N N 178 
ILE   CD1 HD13 sing N N 179 
ILE   OXT HXT  sing N N 180 
LEU   N   CA   sing N N 181 
LEU   N   H    sing N N 182 
LEU   N   H2   sing N N 183 
LEU   CA  C    sing N N 184 
LEU   CA  CB   sing N N 185 
LEU   CA  HA   sing N N 186 
LEU   C   O    doub N N 187 
LEU   C   OXT  sing N N 188 
LEU   CB  CG   sing N N 189 
LEU   CB  HB2  sing N N 190 
LEU   CB  HB3  sing N N 191 
LEU   CG  CD1  sing N N 192 
LEU   CG  CD2  sing N N 193 
LEU   CG  HG   sing N N 194 
LEU   CD1 HD11 sing N N 195 
LEU   CD1 HD12 sing N N 196 
LEU   CD1 HD13 sing N N 197 
LEU   CD2 HD21 sing N N 198 
LEU   CD2 HD22 sing N N 199 
LEU   CD2 HD23 sing N N 200 
LEU   OXT HXT  sing N N 201 
LYS   N   CA   sing N N 202 
LYS   N   H    sing N N 203 
LYS   N   H2   sing N N 204 
LYS   CA  C    sing N N 205 
LYS   CA  CB   sing N N 206 
LYS   CA  HA   sing N N 207 
LYS   C   O    doub N N 208 
LYS   C   OXT  sing N N 209 
LYS   CB  CG   sing N N 210 
LYS   CB  HB2  sing N N 211 
LYS   CB  HB3  sing N N 212 
LYS   CG  CD   sing N N 213 
LYS   CG  HG2  sing N N 214 
LYS   CG  HG3  sing N N 215 
LYS   CD  CE   sing N N 216 
LYS   CD  HD2  sing N N 217 
LYS   CD  HD3  sing N N 218 
LYS   CE  NZ   sing N N 219 
LYS   CE  HE2  sing N N 220 
LYS   CE  HE3  sing N N 221 
LYS   NZ  HZ1  sing N N 222 
LYS   NZ  HZ2  sing N N 223 
LYS   NZ  HZ3  sing N N 224 
LYS   OXT HXT  sing N N 225 
MET   N   CA   sing N N 226 
MET   N   H    sing N N 227 
MET   N   H2   sing N N 228 
MET   CA  C    sing N N 229 
MET   CA  CB   sing N N 230 
MET   CA  HA   sing N N 231 
MET   C   O    doub N N 232 
MET   C   OXT  sing N N 233 
MET   CB  CG   sing N N 234 
MET   CB  HB2  sing N N 235 
MET   CB  HB3  sing N N 236 
MET   CG  SD   sing N N 237 
MET   CG  HG2  sing N N 238 
MET   CG  HG3  sing N N 239 
MET   SD  CE   sing N N 240 
MET   CE  HE1  sing N N 241 
MET   CE  HE2  sing N N 242 
MET   CE  HE3  sing N N 243 
MET   OXT HXT  sing N N 244 
PHE   N   CA   sing N N 245 
PHE   N   H    sing N N 246 
PHE   N   H2   sing N N 247 
PHE   CA  C    sing N N 248 
PHE   CA  CB   sing N N 249 
PHE   CA  HA   sing N N 250 
PHE   C   O    doub N N 251 
PHE   C   OXT  sing N N 252 
PHE   CB  CG   sing N N 253 
PHE   CB  HB2  sing N N 254 
PHE   CB  HB3  sing N N 255 
PHE   CG  CD1  doub Y N 256 
PHE   CG  CD2  sing Y N 257 
PHE   CD1 CE1  sing Y N 258 
PHE   CD1 HD1  sing N N 259 
PHE   CD2 CE2  doub Y N 260 
PHE   CD2 HD2  sing N N 261 
PHE   CE1 CZ   doub Y N 262 
PHE   CE1 HE1  sing N N 263 
PHE   CE2 CZ   sing Y N 264 
PHE   CE2 HE2  sing N N 265 
PHE   CZ  HZ   sing N N 266 
PHE   OXT HXT  sing N N 267 
PRO   N   CA   sing N N 268 
PRO   N   CD   sing N N 269 
PRO   N   H    sing N N 270 
PRO   CA  C    sing N N 271 
PRO   CA  CB   sing N N 272 
PRO   CA  HA   sing N N 273 
PRO   C   O    doub N N 274 
PRO   C   OXT  sing N N 275 
PRO   CB  CG   sing N N 276 
PRO   CB  HB2  sing N N 277 
PRO   CB  HB3  sing N N 278 
PRO   CG  CD   sing N N 279 
PRO   CG  HG2  sing N N 280 
PRO   CG  HG3  sing N N 281 
PRO   CD  HD2  sing N N 282 
PRO   CD  HD3  sing N N 283 
PRO   OXT HXT  sing N N 284 
SER   N   CA   sing N N 285 
SER   N   H    sing N N 286 
SER   N   H2   sing N N 287 
SER   CA  C    sing N N 288 
SER   CA  CB   sing N N 289 
SER   CA  HA   sing N N 290 
SER   C   O    doub N N 291 
SER   C   OXT  sing N N 292 
SER   CB  OG   sing N N 293 
SER   CB  HB2  sing N N 294 
SER   CB  HB3  sing N N 295 
SER   OG  HG   sing N N 296 
SER   OXT HXT  sing N N 297 
THR   N   CA   sing N N 298 
THR   N   H    sing N N 299 
THR   N   H2   sing N N 300 
THR   CA  C    sing N N 301 
THR   CA  CB   sing N N 302 
THR   CA  HA   sing N N 303 
THR   C   O    doub N N 304 
THR   C   OXT  sing N N 305 
THR   CB  OG1  sing N N 306 
THR   CB  CG2  sing N N 307 
THR   CB  HB   sing N N 308 
THR   OG1 HG1  sing N N 309 
THR   CG2 HG21 sing N N 310 
THR   CG2 HG22 sing N N 311 
THR   CG2 HG23 sing N N 312 
THR   OXT HXT  sing N N 313 
TRP   N   CA   sing N N 314 
TRP   N   H    sing N N 315 
TRP   N   H2   sing N N 316 
TRP   CA  C    sing N N 317 
TRP   CA  CB   sing N N 318 
TRP   CA  HA   sing N N 319 
TRP   C   O    doub N N 320 
TRP   C   OXT  sing N N 321 
TRP   CB  CG   sing N N 322 
TRP   CB  HB2  sing N N 323 
TRP   CB  HB3  sing N N 324 
TRP   CG  CD1  doub Y N 325 
TRP   CG  CD2  sing Y N 326 
TRP   CD1 NE1  sing Y N 327 
TRP   CD1 HD1  sing N N 328 
TRP   CD2 CE2  doub Y N 329 
TRP   CD2 CE3  sing Y N 330 
TRP   NE1 CE2  sing Y N 331 
TRP   NE1 HE1  sing N N 332 
TRP   CE2 CZ2  sing Y N 333 
TRP   CE3 CZ3  doub Y N 334 
TRP   CE3 HE3  sing N N 335 
TRP   CZ2 CH2  doub Y N 336 
TRP   CZ2 HZ2  sing N N 337 
TRP   CZ3 CH2  sing Y N 338 
TRP   CZ3 HZ3  sing N N 339 
TRP   CH2 HH2  sing N N 340 
TRP   OXT HXT  sing N N 341 
TYR   N   CA   sing N N 342 
TYR   N   H    sing N N 343 
TYR   N   H2   sing N N 344 
TYR   CA  C    sing N N 345 
TYR   CA  CB   sing N N 346 
TYR   CA  HA   sing N N 347 
TYR   C   O    doub N N 348 
TYR   C   OXT  sing N N 349 
TYR   CB  CG   sing N N 350 
TYR   CB  HB2  sing N N 351 
TYR   CB  HB3  sing N N 352 
TYR   CG  CD1  doub Y N 353 
TYR   CG  CD2  sing Y N 354 
TYR   CD1 CE1  sing Y N 355 
TYR   CD1 HD1  sing N N 356 
TYR   CD2 CE2  doub Y N 357 
TYR   CD2 HD2  sing N N 358 
TYR   CE1 CZ   doub Y N 359 
TYR   CE1 HE1  sing N N 360 
TYR   CE2 CZ   sing Y N 361 
TYR   CE2 HE2  sing N N 362 
TYR   CZ  OH   sing N N 363 
TYR   OH  HH   sing N N 364 
TYR   OXT HXT  sing N N 365 
VAL   N   CA   sing N N 366 
VAL   N   H    sing N N 367 
VAL   N   H2   sing N N 368 
VAL   CA  C    sing N N 369 
VAL   CA  CB   sing N N 370 
VAL   CA  HA   sing N N 371 
VAL   C   O    doub N N 372 
VAL   C   OXT  sing N N 373 
VAL   CB  CG1  sing N N 374 
VAL   CB  CG2  sing N N 375 
VAL   CB  HB   sing N N 376 
VAL   CG1 HG11 sing N N 377 
VAL   CG1 HG12 sing N N 378 
VAL   CG1 HG13 sing N N 379 
VAL   CG2 HG21 sing N N 380 
VAL   CG2 HG22 sing N N 381 
VAL   CG2 HG23 sing N N 382 
VAL   OXT HXT  sing N N 383 
# 
_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                    7H9R 
_atom_sites.fract_transf_matrix[1][1]   0.015078 
_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]   0.011179 
_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]   0.010000 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
_atom_type.scat_dispersion_real 
_atom_type.scat_dispersion_imag 
_atom_type.scat_Cromer_Mann_a1 
_atom_type.scat_Cromer_Mann_a2 
_atom_type.scat_Cromer_Mann_a3 
_atom_type.scat_Cromer_Mann_a4 
_atom_type.scat_Cromer_Mann_b1 
_atom_type.scat_Cromer_Mann_b2 
_atom_type.scat_Cromer_Mann_b3 
_atom_type.scat_Cromer_Mann_b4 
_atom_type.scat_Cromer_Mann_c 
_atom_type.scat_source 
_atom_type.scat_dispersion_source 
C ? ? 3.54356 2.42580 ? ? 25.62398 1.50364  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
N ? ? 4.01032 2.96436 ? ? 19.97189 1.75589  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O ? ? 4.49882 3.47563 ? ? 15.80542 1.70748  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
S ? ? 9.55732 6.39887 ? ? 1.23737  29.19336 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N   . GLU   A 1 9   ? 4.51040   -28.78889 -39.03702 1.000 51.12725 ? 16  GLU   A N   1 
ATOM   2    C CA  . GLU   A 1 9   ? 5.64845   -27.89708 -39.25401 1.000 56.26070 ? 16  GLU   A CA  1 
ATOM   3    C C   . GLU   A 1 9   ? 5.87224   -26.98828 -38.04085 1.000 49.29448 ? 16  GLU   A C   1 
ATOM   4    O O   . GLU   A 1 9   ? 5.20180   -25.96450 -37.88227 1.000 45.92383 ? 16  GLU   A O   1 
ATOM   5    C CB  . GLU   A 1 9   ? 5.43143   -27.06061 -40.51840 1.000 59.26172 ? 16  GLU   A CB  1 
ATOM   6    C CG  . GLU   A 1 9   ? 6.70702   -26.68685 -41.28175 1.000 67.32906 ? 16  GLU   A CG  1 
ATOM   7    C CD  . GLU   A 1 9   ? 7.33779   -25.36240 -40.84926 1.000 70.93628 ? 16  GLU   A CD  1 
ATOM   8    O OE1 . GLU   A 1 9   ? 6.99064   -24.83213 -39.76305 1.000 67.55640 ? 16  GLU   A OE1 1 
ATOM   9    O OE2 . GLU   A 1 9   ? 8.19479   -24.84973 -41.61255 1.000 76.36062 ? 16  GLU   A OE2 1 
ATOM   10   N N   . VAL   A 1 10  ? 6.83144   -27.36094 -37.19580 1.000 44.35115 ? 17  VAL   A N   1 
ATOM   11   C CA  . VAL   A 1 10  ? 7.08978   -26.69068 -35.92479 1.000 33.96127 ? 17  VAL   A CA  1 
ATOM   12   C C   . VAL   A 1 10  ? 8.44854   -26.01246 -35.99269 1.000 36.33969 ? 17  VAL   A C   1 
ATOM   13   O O   . VAL   A 1 10  ? 9.44798   -26.66171 -36.31853 1.000 35.42220 ? 17  VAL   A O   1 
ATOM   14   C CB  . VAL   A 1 10  ? 7.06950   -27.68371 -34.75262 1.000 39.91451 ? 17  VAL   A CB  1 
ATOM   15   C CG1 . VAL   A 1 10  ? 7.15071   -26.93178 -33.43867 1.000 36.83597 ? 17  VAL   A CG1 1 
ATOM   16   C CG2 . VAL   A 1 10  ? 5.83864   -28.58546 -34.83450 1.000 43.91622 ? 17  VAL   A CG2 1 
ATOM   17   N N   . GLU   A 1 11  ? 8.49423   -24.72328 -35.66261 1.000 30.20520 ? 18  GLU   A N   1 
ATOM   18   C CA  . GLU   A 1 11  ? 9.74646   -23.97898 -35.62179 1.000 29.42834 ? 18  GLU   A CA  1 
ATOM   19   C C   . GLU   A 1 11  ? 10.17901  -23.80699 -34.16787 1.000 27.41474 ? 18  GLU   A C   1 
ATOM   20   O O   . GLU   A 1 11  ? 9.36542   -23.44420 -33.31678 1.000 24.75979 ? 18  GLU   A O   1 
ATOM   21   C CB  . GLU   A 1 11  ? 9.57609   -22.62168 -36.30039 1.000 29.39663 ? 18  GLU   A CB  1 
ATOM   22   C CG  . GLU   A 1 11  ? 9.49119   -22.70680 -37.81191 1.000 31.60756 ? 18  GLU   A CG  1 
ATOM   23   C CD  . GLU   A 1 11  ? 9.22146   -21.36151 -38.43757 1.000 40.66874 ? 18  GLU   A CD  1 
ATOM   24   O OE1 . GLU   A 1 11  ? 8.21704   -20.70983 -38.07245 1.000 43.33556 ? 18  GLU   A OE1 1 
ATOM   25   O OE2 . GLU   A 1 11  ? 10.05366  -20.91929 -39.24597 1.000 42.96034 ? 18  GLU   A OE2 1 
ATOM   26   N N   . THR   A 1 12  ? 11.45952  -24.07613 -33.87930 1.000 26.37337 ? 19  THR   A N   1 
ATOM   27   C CA  . THR   A 1 12  ? 12.00434  -23.96569 -32.53034 1.000 23.70615 ? 19  THR   A CA  1 
ATOM   28   C C   . THR   A 1 12  ? 13.01454  -22.82384 -32.47975 1.000 23.82082 ? 19  THR   A C   1 
ATOM   29   O O   . THR   A 1 12  ? 13.92176  -22.75765 -33.31155 1.000 23.51482 ? 19  THR   A O   1 
ATOM   30   C CB  . THR   A 1 12  ? 12.68796  -25.27273 -32.09931 1.000 25.78922 ? 19  THR   A CB  1 
ATOM   31   O OG1 . THR   A 1 12  ? 11.76581  -26.36507 -32.20910 1.000 26.71568 ? 19  THR   A OG1 1 
ATOM   32   C CG2 . THR   A 1 12  ? 13.18452  -25.20599 -30.66086 1.000 24.99234 ? 19  THR   A CG2 1 
ATOM   33   N N   . PHE   A 1 13  ? 12.87482  -21.96472 -31.47977 1.000 23.44924 ? 20  PHE   A N   1 
ATOM   34   C CA  . PHE   A 1 13  ? 13.65090  -20.74099 -31.31843 1.000 24.63566 ? 20  PHE   A CA  1 
ATOM   35   C C   . PHE   A 1 13  ? 14.33669  -20.73513 -29.95614 1.000 22.55771 ? 20  PHE   A C   1 
ATOM   36   O O   . PHE   A 1 13  ? 13.79759  -21.24001 -28.97441 1.000 23.45172 ? 20  PHE   A O   1 
ATOM   37   C CB  . PHE   A 1 13  ? 12.72728  -19.49442 -31.37170 1.000 26.04526 ? 20  PHE   A CB  1 
ATOM   38   C CG  . PHE   A 1 13  ? 12.00450  -19.31657 -32.67333 1.000 25.73639 ? 20  PHE   A CG  1 
ATOM   39   C CD1 . PHE   A 1 13  ? 10.77185  -19.95071 -32.90596 1.000 26.32047 ? 20  PHE   A CD1 1 
ATOM   40   C CD2 . PHE   A 1 13  ? 12.50915  -18.46480 -33.65062 1.000 27.67770 ? 20  PHE   A CD2 1 
ATOM   41   C CE1 . PHE   A 1 13  ? 10.10471  -19.78207 -34.11161 1.000 28.62454 ? 20  PHE   A CE1 1 
ATOM   42   C CE2 . PHE   A 1 13  ? 11.82005  -18.27882 -34.85281 1.000 31.23671 ? 20  PHE   A CE2 1 
ATOM   43   C CZ  . PHE   A 1 13  ? 10.62305  -18.94432 -35.07804 1.000 30.40090 ? 20  PHE   A CZ  1 
ATOM   44   N N   . ALA   A 1 14  ? 15.50555  -20.09964 -29.87630 1.000 21.25374 ? 21  ALA   A N   1 
ATOM   45   C CA  . ALA   A 1 14  ? 16.14349  -19.84060 -28.58972 1.000 22.18610 ? 21  ALA   A CA  1 
ATOM   46   C C   . ALA   A 1 14  ? 15.63569  -18.52395 -28.00591 1.000 24.85685 ? 21  ALA   A C   1 
ATOM   47   O O   . ALA   A 1 14  ? 15.54584  -17.51741 -28.71630 1.000 25.15052 ? 21  ALA   A O   1 
ATOM   48   C CB  . ALA   A 1 14  ? 17.66608  -19.75866 -28.75593 1.000 25.99645 ? 21  ALA   A CB  1 
ATOM   49   N N   . PHE   A 1 15  ? 15.32764  -18.51657 -26.70070 1.000 21.94407 ? 22  PHE   A N   1 
ATOM   50   C CA  . PHE   A 1 15  ? 15.10505  -17.23126 -26.04097 1.000 23.72851 ? 22  PHE   A CA  1 
ATOM   51   C C   . PHE   A 1 15  ? 16.39493  -16.41821 -26.07266 1.000 23.27440 ? 22  PHE   A C   1 
ATOM   52   O O   . PHE   A 1 15  ? 17.49989  -16.96887 -25.94197 1.000 25.31917 ? 22  PHE   A O   1 
ATOM   53   C CB  . PHE   A 1 15  ? 14.68384  -17.40416 -24.57446 1.000 23.23690 ? 22  PHE   A CB  1 
ATOM   54   C CG  . PHE   A 1 15  ? 13.29293  -17.94555 -24.37366 1.000 21.36323 ? 22  PHE   A CG  1 
ATOM   55   C CD1 . PHE   A 1 15  ? 12.16701  -17.16081 -24.67714 1.000 21.20564 ? 22  PHE   A CD1 1 
ATOM   56   C CD2 . PHE   A 1 15  ? 13.10234  -19.20287 -23.82172 1.000 24.04180 ? 22  PHE   A CD2 1 
ATOM   57   C CE1 . PHE   A 1 15  ? 10.87672  -17.63933 -24.45423 1.000 23.01933 ? 22  PHE   A CE1 1 
ATOM   58   C CE2 . PHE   A 1 15  ? 11.82323  -19.70611 -23.61826 1.000 22.91347 ? 22  PHE   A CE2 1 
ATOM   59   C CZ  . PHE   A 1 15  ? 10.69440  -18.91043 -23.92234 1.000 22.75260 ? 22  PHE   A CZ  1 
ATOM   60   N N   . GLN   A 1 16  ? 16.25660  -15.09759 -26.21802 1.000 23.77389 ? 23  GLN   A N   1 
ATOM   61   C CA  . GLN   A 1 16  ? 17.38074  -14.21386 -25.90627 1.000 28.35883 ? 23  GLN   A CA  1 
ATOM   62   C C   . GLN   A 1 16  ? 17.89208  -14.49645 -24.49324 1.000 25.61161 ? 23  GLN   A C   1 
ATOM   63   O O   . GLN   A 1 16  ? 17.13169  -14.86704 -23.59472 1.000 25.57408 ? 23  GLN   A O   1 
ATOM   64   C CB  . GLN   A 1 16  ? 16.95974  -12.75008 -26.02797 1.000 27.42866 ? 23  GLN   A CB  1 
ATOM   65   C CG  . GLN   A 1 16  ? 16.68123  -12.27717 -27.44054 1.000 35.14246 ? 23  GLN   A CG  1 
ATOM   66   C CD  . GLN   A 1 16  ? 16.05089  -10.88893 -27.42751 1.000 43.01657 ? 23  GLN   A CD  1 
ATOM   67   O OE1 . GLN   A 1 16  ? 14.87691  -10.75101 -27.11009 1.000 38.64173 ? 23  GLN   A OE1 1 
ATOM   68   N NE2 . GLN   A 1 16  ? 16.83818  -9.85740  -27.73730 1.000 40.30325 ? 23  GLN   A NE2 1 
ATOM   69   N N   . ALA   A 1 17  ? 19.20569  -14.32833 -24.30093 1.000 26.78085 ? 24  ALA   A N   1 
ATOM   70   C CA  . ALA   A 1 17  ? 19.82720  -14.73039 -23.04226 1.000 26.67633 ? 24  ALA   A CA  1 
ATOM   71   C C   . ALA   A 1 17  ? 19.20284  -14.02359 -21.84529 1.000 27.17934 ? 24  ALA   A C   1 
ATOM   72   O O   . ALA   A 1 17  ? 19.00618  -14.63837 -20.78741 1.000 28.60604 ? 24  ALA   A O   1 
ATOM   73   C CB  . ALA   A 1 17  ? 21.33197  -14.45869 -23.09515 1.000 30.25833 ? 24  ALA   A CB  1 
ATOM   74   N N   . GLU   A 1 18  ? 18.83942  -12.74835 -22.00612 1.000 28.07584 ? 25  GLU   A N   1 
ATOM   75   C CA  . GLU   A 1 18  ? 18.26486  -11.99732 -20.89138 1.000 28.10391 ? 25  GLU   A CA  1 
ATOM   76   C C   . GLU   A 1 18  ? 16.89179  -12.53393 -20.49718 1.000 27.01949 ? 25  GLU   A C   1 
ATOM   77   O O   . GLU   A 1 18  ? 16.55577  -12.55281 -19.30385 1.000 26.15095 ? 25  GLU   A O   1 
ATOM   78   C CB  . GLU   A 1 18  ? 18.17754  -10.52013 -21.26270 1.000 30.84518 ? 25  GLU   A CB  1 
ATOM   79   C CG  . GLU   A 1 18  ? 19.53813  -9.87701  -21.47178 1.000 35.06448 ? 25  GLU   A CG  1 
ATOM   80   C CD  . GLU   A 1 18  ? 20.05813  -9.99508  -22.90798 1.000 44.22949 ? 25  GLU   A CD  1 
ATOM   81   O OE1 . GLU   A 1 18  ? 19.49336  -10.79055 -23.70078 1.000 38.45340 ? 25  GLU   A OE1 1 
ATOM   82   O OE2 . GLU   A 1 18  ? 21.04431  -9.29040  -23.24011 1.000 46.20104 ? 25  GLU   A OE2 1 
ATOM   83   N N   . ILE   A 1 19  ? 16.09394  -12.98804 -21.48071 1.000 27.26285 ? 26  ILE   A N   1 
ATOM   84   C CA  . ILE   A 1 19  ? 14.77441  -13.55534 -21.18132 1.000 25.45211 ? 26  ILE   A CA  1 
ATOM   85   C C   . ILE   A 1 19  ? 14.93066  -14.93951 -20.55952 1.000 26.91027 ? 26  ILE   A C   1 
ATOM   86   O O   . ILE   A 1 19  ? 14.21119  -15.29820 -19.61984 1.000 25.62072 ? 26  ILE   A O   1 
ATOM   87   C CB  . ILE   A 1 19  ? 13.87921  -13.59424 -22.44517 1.000 26.84613 ? 26  ILE   A CB  1 
ATOM   88   C CG1 . ILE   A 1 19  ? 13.35003  -12.20290 -22.82642 1.000 28.44577 ? 26  ILE   A CG1 1 
ATOM   89   C CG2 . ILE   A 1 19  ? 12.62762  -14.49348 -22.24131 1.000 24.84990 ? 26  ILE   A CG2 1 
ATOM   90   C CD1 . ILE   A 1 19  ? 14.39740  -11.21413 -23.28378 1.000 34.16770 ? 26  ILE   A CD1 1 
ATOM   91   N N   . ALA   A 1 20  ? 15.87878  -15.74479 -21.06043 1.000 23.25176 ? 27  ALA   A N   1 
ATOM   92   C CA  . ALA   A 1 20  ? 16.12422  -17.02951 -20.41315 1.000 27.40834 ? 27  ALA   A CA  1 
ATOM   93   C C   . ALA   A 1 20  ? 16.51231  -16.83039 -18.95022 1.000 27.36005 ? 27  ALA   A C   1 
ATOM   94   O O   . ALA   A 1 20  ? 16.10790  -17.60716 -18.07517 1.000 26.04760 ? 27  ALA   A O   1 
ATOM   95   C CB  . ALA   A 1 20  ? 17.21239  -17.80240 -21.17236 1.000 23.74283 ? 27  ALA   A CB  1 
ATOM   96   N N   . GLN   A 1 21  ? 17.28896  -15.78411 -18.66536 1.000 25.05321 ? 28  GLN   A N   1 
ATOM   97   C CA  . GLN   A 1 21  ? 17.72281  -15.53819 -17.29689 1.000 24.06680 ? 28  GLN   A CA  1 
ATOM   98   C C   . GLN   A 1 21  ? 16.55758  -15.13040 -16.41039 1.000 28.94603 ? 28  GLN   A C   1 
ATOM   99   O O   . GLN   A 1 21  ? 16.44632  -15.60272 -15.27436 1.000 30.30228 ? 28  GLN   A O   1 
ATOM   100  C CB  . GLN   A 1 21  ? 18.81354  -14.47213 -17.29246 1.000 31.49319 ? 28  GLN   A CB  1 
ATOM   101  C CG  . GLN   A 1 21  ? 19.08786  -13.86105 -15.92069 1.000 39.13077 ? 28  GLN   A CG  1 
ATOM   102  C CD  . GLN   A 1 21  ? 20.33426  -12.96803 -15.90805 1.000 44.24669 ? 28  GLN   A CD  1 
ATOM   103  O OE1 . GLN   A 1 21  ? 20.46895  -12.04615 -16.72390 1.000 47.78728 ? 28  GLN   A OE1 1 
ATOM   104  N NE2 . GLN   A 1 21  ? 21.21219  -13.19411 -14.93399 1.000 53.00144 ? 28  GLN   A NE2 1 
ATOM   105  N N   . LEU   A 1 22  ? 15.66525  -14.27697 -16.92815 1.000 25.37342 ? 29  LEU   A N   1 
ATOM   106  C CA  . LEU   A 1 22  ? 14.45808  -13.89803 -16.18142 1.000 25.50773 ? 29  LEU   A CA  1 
ATOM   107  C C   . LEU   A 1 22  ? 13.61271  -15.11866 -15.85987 1.000 25.24020 ? 29  LEU   A C   1 
ATOM   108  O O   . LEU   A 1 22  ? 13.10964  -15.29072 -14.74064 1.000 24.85258 ? 29  LEU   A O   1 
ATOM   109  C CB  . LEU   A 1 22  ? 13.62618  -12.90660 -17.00740 1.000 24.95104 ? 29  LEU   A CB  1 
ATOM   110  C CG  . LEU   A 1 22  ? 12.23276  -12.58370 -16.47059 1.000 27.05885 ? 29  LEU   A CG  1 
ATOM   111  C CD1 . LEU   A 1 22  ? 12.39897  -11.79955 -15.14989 1.000 29.45839 ? 29  LEU   A CD1 1 
ATOM   112  C CD2 . LEU   A 1 22  ? 11.42981  -11.82102 -17.51327 1.000 27.64154 ? 29  LEU   A CD2 1 
ATOM   113  N N   . MET   A 1 23  ? 13.45776  -15.99381 -16.84080 1.000 22.87815 ? 30  MET   A N   1 
ATOM   114  C CA  . MET   A 1 23  ? 12.58945  -17.15295 -16.69334 1.000 23.75324 ? 30  MET   A CA  1 
ATOM   115  C C   . MET   A 1 23  ? 13.18892  -18.11612 -15.65861 1.000 24.07902 ? 30  MET   A C   1 
ATOM   116  O O   . MET   A 1 23  ? 12.48096  -18.67644 -14.80068 1.000 24.85483 ? 30  MET   A O   1 
ATOM   117  C CB  . MET   A 1 23  ? 12.52391  -17.77280 -18.09172 1.000 22.04367 ? 30  MET   A CB  1 
ATOM   118  C CG  . MET   A 1 23  ? 11.34659  -17.28044 -18.89405 1.000 23.62592 ? 30  MET   A CG  1 
ATOM   119  S SD  . MET   A 1 23  ? 11.32926  -17.99194 -20.55116 1.000 26.12811 ? 30  MET   A SD  1 
ATOM   120  C CE  . MET   A 1 23  ? 10.09513  -19.30149 -20.27595 1.000 28.62796 ? 30  MET   A CE  1 
ATOM   121  N N   . SER   A 1 24  ? 14.51724  -18.25996 -15.67288 1.000 25.84623 ? 31  SER   A N   1 
ATOM   122  C CA  . SER   A 1 24  ? 15.13899  -19.14012 -14.69415 1.000 26.17786 ? 31  SER   A CA  1 
ATOM   123  C C   . SER   A 1 24  ? 15.06347  -18.54054 -13.28489 1.000 28.92701 ? 31  SER   A C   1 
ATOM   124  O O   . SER   A 1 24  ? 14.85603  -19.27796 -12.30588 1.000 30.79017 ? 31  SER   A O   1 
ATOM   125  C CB  . SER   A 1 24  ? 16.57752  -19.44701 -15.14040 1.000 30.67157 ? 31  SER   A CB  1 
ATOM   126  O OG  . SER   A 1 24  ? 17.44051  -19.66424 -14.05801 1.000 43.68582 ? 31  SER   A OG  1 
ATOM   127  N N   . LEU   A 1 25  ? 15.15461  -17.21007 -13.16302 1.000 26.18502 ? 32  LEU   A N   1 
ATOM   128  C CA  . LEU   A 1 25  ? 14.97673  -16.57863 -11.85878 1.000 24.67208 ? 32  LEU   A CA  1 
ATOM   129  C C   . LEU   A 1 25  ? 13.55417  -16.73780 -11.34078 1.000 29.70964 ? 32  LEU   A C   1 
ATOM   130  O O   . LEU   A 1 25  ? 13.34936  -16.98212 -10.14516 1.000 26.72705 ? 32  LEU   A O   1 
ATOM   131  C CB  . LEU   A 1 25  ? 15.36243  -15.10849 -11.91820 1.000 30.80879 ? 32  LEU   A CB  1 
ATOM   132  C CG  . LEU   A 1 25  ? 16.82135  -14.78782 -12.25995 1.000 36.78390 ? 32  LEU   A CG  1 
ATOM   133  C CD1 . LEU   A 1 25  ? 16.99728  -13.27986 -12.32495 1.000 42.20449 ? 32  LEU   A CD1 1 
ATOM   134  C CD2 . LEU   A 1 25  ? 17.73159  -15.33373 -11.17933 1.000 37.14337 ? 32  LEU   A CD2 1 
ATOM   135  N N   . ILE   A 1 26  ? 12.56260  -16.61564 -12.22257 1.000 24.55696 ? 33  ILE   A N   1 
ATOM   136  C CA  . ILE   A 1 26  ? 11.17902  -16.83756 -11.79955 1.000 27.04357 ? 33  ILE   A CA  1 
ATOM   137  C C   . ILE   A 1 26  ? 10.98604  -18.28210 -11.34785 1.000 30.31276 ? 33  ILE   A C   1 
ATOM   138  O O   . ILE   A 1 26  ? 10.29702  -18.55736 -10.35225 1.000 27.53874 ? 33  ILE   A O   1 
ATOM   139  C CB  . ILE   A 1 26  ? 10.21587  -16.44753 -12.93442 1.000 23.57325 ? 33  ILE   A CB  1 
ATOM   140  C CG1 . ILE   A 1 26  ? 10.18619  -14.92722 -13.08976 1.000 26.09171 ? 33  ILE   A CG1 1 
ATOM   141  C CG2 . ILE   A 1 26  ? 8.80174   -17.04014 -12.71094 1.000 24.53030 ? 33  ILE   A CG2 1 
ATOM   142  C CD1 . ILE   A 1 26  ? 9.45199   -14.42560 -14.34087 1.000 26.39321 ? 33  ILE   A CD1 1 
ATOM   143  N N   . ILE   A 1 27  ? 11.61532  -19.22611 -12.04243 1.000 25.47054 ? 34  ILE   A N   1 
ATOM   144  C CA  . ILE   A 1 27  ? 11.34920  -20.63039 -11.72447 1.000 27.96785 ? 34  ILE   A CA  1 
ATOM   145  C C   . ILE   A 1 27  ? 12.07512  -21.07294 -10.45559 1.000 30.82421 ? 34  ILE   A C   1 
ATOM   146  O O   . ILE   A 1 27  ? 11.53830  -21.86097 -9.66916  1.000 34.46462 ? 34  ILE   A O   1 
ATOM   147  C CB  . ILE   A 1 27  ? 11.73077  -21.49332 -12.93337 1.000 28.51370 ? 34  ILE   A CB  1 
ATOM   148  C CG1 . ILE   A 1 27  ? 10.70616  -21.25601 -14.05293 1.000 24.21529 ? 34  ILE   A CG1 1 
ATOM   149  C CG2 . ILE   A 1 27  ? 11.84849  -22.96416 -12.55005 1.000 33.92274 ? 34  ILE   A CG2 1 
ATOM   150  C CD1 . ILE   A 1 27  ? 11.17979  -21.74768 -15.43524 1.000 27.53830 ? 34  ILE   A CD1 1 
ATOM   151  N N   . ASN   A 1 28  ? 13.27556  -20.54939 -10.20638 1.000 30.94041 ? 35  ASN   A N   1 
ATOM   152  C CA  . ASN   A 1 28  ? 14.14352  -21.07205 -9.15166  1.000 32.34981 ? 35  ASN   A CA  1 
ATOM   153  C C   . ASN   A 1 28  ? 14.13477  -20.26378 -7.86114  1.000 32.78160 ? 35  ASN   A C   1 
ATOM   154  O O   . ASN   A 1 28  ? 14.56490  -20.78842 -6.82372  1.000 36.34822 ? 35  ASN   A O   1 
ATOM   155  C CB  . ASN   A 1 28  ? 15.57940  -21.13734 -9.67097  1.000 35.16009 ? 35  ASN   A CB  1 
ATOM   156  C CG  . ASN   A 1 28  ? 15.74647  -22.17629 -10.73901 1.000 44.30632 ? 35  ASN   A CG  1 
ATOM   157  O OD1 . ASN   A 1 28  ? 15.05719  -23.20104 -10.73479 1.000 42.65844 ? 35  ASN   A OD1 1 
ATOM   158  N ND2 . ASN   A 1 28  ? 16.63482  -21.90516 -11.69775 1.000 48.43397 ? 35  ASN   A ND2 1 
ATOM   159  N N   . THR   A 1 29  ? 13.70640  -19.00213 -7.89009  1.000 27.81029 ? 36  THR   A N   1 
ATOM   160  C CA  . THR   A 1 29  ? 13.74215  -18.18571 -6.68053  1.000 27.64187 ? 36  THR   A CA  1 
ATOM   161  C C   . THR   A 1 29  ? 12.64355  -18.60984 -5.71823  1.000 30.88837 ? 36  THR   A C   1 
ATOM   162  O O   . THR   A 1 29  ? 11.48542  -18.75888 -6.12173  1.000 30.45757 ? 36  THR   A O   1 
ATOM   163  C CB  . THR   A 1 29  ? 13.59281  -16.70523 -7.03529  1.000 29.22617 ? 36  THR   A CB  1 
ATOM   164  O OG1 . THR   A 1 29  ? 14.68045  -16.31794 -7.88438  1.000 32.54413 ? 36  THR   A OG1 1 
ATOM   165  C CG2 . THR   A 1 29  ? 13.59426  -15.83792 -5.76918  1.000 32.68511 ? 36  THR   A CG2 1 
ATOM   166  N N   . PHE   A 1 30  ? 12.98904  -18.76776 -4.43778  1.000 29.06994 ? 37  PHE   A N   1 
ATOM   167  C CA  . PHE   A 1 30  ? 11.95157  -19.00775 -3.44118  1.000 30.36557 ? 37  PHE   A CA  1 
ATOM   168  C C   . PHE   A 1 30  ? 11.09890  -17.74304 -3.27146  1.000 30.40711 ? 37  PHE   A C   1 
ATOM   169  O O   . PHE   A 1 30  ? 11.61183  -16.67345 -2.90836  1.000 31.57491 ? 37  PHE   A O   1 
ATOM   170  C CB  . PHE   A 1 30  ? 12.56204  -19.42741 -2.10208  1.000 30.72266 ? 37  PHE   A CB  1 
ATOM   171  C CG  . PHE   A 1 30  ? 11.53228  -19.73819 -1.06861  1.000 32.52784 ? 37  PHE   A CG  1 
ATOM   172  C CD1 . PHE   A 1 30  ? 10.77380  -20.89455 -1.15228  1.000 35.98402 ? 37  PHE   A CD1 1 
ATOM   173  C CD2 . PHE   A 1 30  ? 11.27827  -18.84953 -0.03381  1.000 32.66633 ? 37  PHE   A CD2 1 
ATOM   174  C CE1 . PHE   A 1 30  ? 9.78770   -21.17594 -0.19470  1.000 33.40414 ? 37  PHE   A CE1 1 
ATOM   175  C CE2 . PHE   A 1 30  ? 10.30079  -19.12337 0.91218   1.000 34.31054 ? 37  PHE   A CE2 1 
ATOM   176  C CZ  . PHE   A 1 30  ? 9.55966   -20.29118 0.83279   1.000 35.03849 ? 37  PHE   A CZ  1 
ATOM   177  N N   . TYR   A 1 31  ? 9.79039   -17.87100 -3.48874  1.000 27.94750 ? 38  TYR   A N   1 
ATOM   178  C CA  . TYR   A 1 31  ? 8.90850   -16.70166 -3.49791  1.000 28.57593 ? 38  TYR   A CA  1 
ATOM   179  C C   . TYR   A 1 31  ? 7.48372   -17.22023 -3.34573  1.000 27.42771 ? 38  TYR   A C   1 
ATOM   180  O O   . TYR   A 1 31  ? 6.95235   -17.81710 -4.28385  1.000 28.63457 ? 38  TYR   A O   1 
ATOM   181  C CB  . TYR   A 1 31  ? 9.06796   -15.90949 -4.80846  1.000 30.23186 ? 38  TYR   A CB  1 
ATOM   182  C CG  . TYR   A 1 31  ? 8.20765   -14.66431 -4.84015  1.000 29.99979 ? 38  TYR   A CG  1 
ATOM   183  C CD1 . TYR   A 1 31  ? 8.51263   -13.58202 -4.01664  1.000 32.77345 ? 38  TYR   A CD1 1 
ATOM   184  C CD2 . TYR   A 1 31  ? 7.07434   -14.57943 -5.66102  1.000 29.55466 ? 38  TYR   A CD2 1 
ATOM   185  C CE1 . TYR   A 1 31  ? 7.72514   -12.43917 -4.00093  1.000 38.07008 ? 38  TYR   A CE1 1 
ATOM   186  C CE2 . TYR   A 1 31  ? 6.28166   -13.42163 -5.66341  1.000 31.57050 ? 38  TYR   A CE2 1 
ATOM   187  C CZ  . TYR   A 1 31  ? 6.62073   -12.36256 -4.82343  1.000 35.35007 ? 38  TYR   A CZ  1 
ATOM   188  O OH  . TYR   A 1 31  ? 5.85879   -11.21648 -4.79803  1.000 38.42492 ? 38  TYR   A OH  1 
ATOM   189  N N   . SER   A 1 32  ? 6.87045   -16.98959 -2.18724  1.000 26.66092 ? 39  SER   A N   1 
ATOM   190  C CA  . SER   A 1 32  ? 5.62900   -17.68883 -1.86151  1.000 25.57815 ? 39  SER   A CA  1 
ATOM   191  C C   . SER   A 1 32  ? 4.39994   -17.04498 -2.49532  1.000 28.55883 ? 39  SER   A C   1 
ATOM   192  O O   . SER   A 1 32  ? 3.37902   -17.72561 -2.65254  1.000 31.32398 ? 39  SER   A O   1 
ATOM   193  C CB  . SER   A 1 32  ? 5.44799   -17.75894 -0.34424  1.000 29.94935 ? 39  SER   A CB  1 
ATOM   194  O OG  . SER   A 1 32  ? 6.51083   -18.49886 0.24665   1.000 29.99213 ? 39  SER   A OG  1 
ATOM   195  N N   . ASN   A 1 33  ? 4.50071   -15.78612 -2.91933  1.000 28.34115 ? 40  ASN   A N   1 
ATOM   196  C CA  . ASN   A 1 33  ? 3.35178   -14.99129 -3.37030  1.000 29.57075 ? 40  ASN   A CA  1 
ATOM   197  C C   . ASN   A 1 33  ? 3.04048   -15.26804 -4.84978  1.000 28.20336 ? 40  ASN   A C   1 
ATOM   198  O O   . ASN   A 1 33  ? 3.02520   -14.37450 -5.69674  1.000 25.83871 ? 40  ASN   A O   1 
ATOM   199  C CB  . ASN   A 1 33  ? 3.66242   -13.51973 -3.10860  1.000 32.15109 ? 40  ASN   A CB  1 
ATOM   200  C CG  . ASN   A 1 33  ? 2.51712   -12.56859 -3.47284  1.000 31.99754 ? 40  ASN   A CG  1 
ATOM   201  O OD1 . ASN   A 1 33  ? 1.34371   -12.85906 -3.25594  1.000 31.41838 ? 40  ASN   A OD1 1 
ATOM   202  N ND2 . ASN   A 1 33  ? 2.87467   -11.41023 -4.00381  1.000 32.02396 ? 40  ASN   A ND2 1 
ATOM   203  N N   . LYS   A 1 34  ? 2.79124   -16.55032 -5.16684  1.000 25.09351 ? 41  LYS   A N   1 
ATOM   204  C CA  . LYS   A 1 34  ? 2.66180   -16.95236 -6.56487  1.000 22.93135 ? 41  LYS   A CA  1 
ATOM   205  C C   . LYS   A 1 34  ? 1.37055   -16.45793 -7.20079  1.000 21.74247 ? 41  LYS   A C   1 
ATOM   206  O O   . LYS   A 1 34  ? 1.31041   -16.36615 -8.43133  1.000 22.63849 ? 41  LYS   A O   1 
ATOM   207  C CB  . LYS   A 1 34  ? 2.71679   -18.48151 -6.66681  1.000 26.01033 ? 41  LYS   A CB  1 
ATOM   208  C CG  . LYS   A 1 34  ? 4.07215   -19.08835 -6.31090  1.000 23.43282 ? 41  LYS   A CG  1 
ATOM   209  C CD  . LYS   A 1 34  ? 4.05069   -20.60730 -6.53451  1.000 28.90610 ? 41  LYS   A CD  1 
ATOM   210  C CE  . LYS   A 1 34  ? 5.41123   -21.23708 -6.25963  1.000 29.00287 ? 41  LYS   A CE  1 
ATOM   211  N NZ  . LYS   A 1 34  ? 6.36067   -21.01196 -7.38742  1.000 25.56868 ? 41  LYS   A NZ  1 
ATOM   212  N N   . GLU   A 1 35  ? 0.36196   -16.10132 -6.39316  1.000 22.76624 ? 42  GLU   A N   1 
ATOM   213  C CA  . GLU   A 1 35  ? -0.94695  -15.75992 -6.97030  1.000 25.23325 ? 42  GLU   A CA  1 
ATOM   214  C C   . GLU   A 1 35  ? -0.93035  -14.54061 -7.88579  1.000 25.22216 ? 42  GLU   A C   1 
ATOM   215  O O   . GLU   A 1 35  ? -1.91001  -14.34133 -8.62547  1.000 26.24171 ? 42  GLU   A O   1 
ATOM   216  C CB  . GLU   A 1 35  ? -2.00645  -15.48545 -5.88521  1.000 25.63566 ? 42  GLU   A CB  1 
ATOM   217  C CG  . GLU   A 1 35  ? -1.72139  -14.31175 -4.98224  1.000 26.11372 ? 42  GLU   A CG  1 
ATOM   218  C CD  . GLU   A 1 35  ? -2.66738  -14.25404 -3.76341  1.000 33.24470 ? 42  GLU   A CD  1 
ATOM   219  O OE1 . GLU   A 1 35  ? -2.67162  -15.20187 -2.95446  1.000 39.47743 ? 42  GLU   A OE1 1 
ATOM   220  O OE2 . GLU   A 1 35  ? -3.28738  -13.19763 -3.54013  1.000 40.83151 ? 42  GLU   A OE2 1 
ATOM   221  N N   . ILE   A 1 36  ? 0.11463   -13.70554 -7.85063  1.000 23.51311 ? 43  ILE   A N   1 
ATOM   222  C CA  . ILE   A 1 36  ? 0.16950   -12.53251 -8.71879  1.000 25.32975 ? 43  ILE   A CA  1 
ATOM   223  C C   . ILE   A 1 36  ? 0.18448   -12.88908 -10.20204 1.000 24.28680 ? 43  ILE   A C   1 
ATOM   224  O O   . ILE   A 1 36  ? -0.09173  -12.01633 -11.02958 1.000 21.79051 ? 43  ILE   A O   1 
ATOM   225  C CB  . ILE   A 1 36  ? 1.38110   -11.64161 -8.36330  1.000 25.39362 ? 43  ILE   A CB  1 
ATOM   226  C CG1 . ILE   A 1 36  ? 2.68852   -12.41952 -8.42906  1.000 30.58659 ? 43  ILE   A CG1 1 
ATOM   227  C CG2 . ILE   A 1 36  ? 1.21780   -11.05658 -6.94526  1.000 30.53410 ? 43  ILE   A CG2 1 
ATOM   228  C CD1 . ILE   A 1 36  ? 3.51332   -12.09040 -9.60992  1.000 41.54560 ? 43  ILE   A CD1 1 
ATOM   229  N N   . PHE   A 1 37  ? 0.46405   -14.14922 -10.56892 1.000 21.33804 ? 44  PHE   A N   1 
ATOM   230  C CA  . PHE   A 1 37  ? 0.46837   -14.48679 -11.99259 1.000 24.61158 ? 44  PHE   A CA  1 
ATOM   231  C C   . PHE   A 1 37  ? -0.87267  -14.13369 -12.62194 1.000 22.09996 ? 44  PHE   A C   1 
ATOM   232  O O   . PHE   A 1 37  ? -0.92824  -13.68967 -13.77221 1.000 22.68380 ? 44  PHE   A O   1 
ATOM   233  C CB  . PHE   A 1 37  ? 0.77055   -15.97543 -12.22685 1.000 23.91771 ? 44  PHE   A CB  1 
ATOM   234  C CG  . PHE   A 1 37  ? -0.42894  -16.87884 -12.00023 1.000 24.79890 ? 44  PHE   A CG  1 
ATOM   235  C CD1 . PHE   A 1 37  ? -0.71407  -17.34725 -10.73360 1.000 22.84265 ? 44  PHE   A CD1 1 
ATOM   236  C CD2 . PHE   A 1 37  ? -1.30095  -17.20072 -13.04120 1.000 24.31766 ? 44  PHE   A CD2 1 
ATOM   237  C CE1 . PHE   A 1 37  ? -1.85417  -18.16551 -10.50091 1.000 25.06099 ? 44  PHE   A CE1 1 
ATOM   238  C CE2 . PHE   A 1 37  ? -2.42164  -17.99864 -12.81811 1.000 23.93136 ? 44  PHE   A CE2 1 
ATOM   239  C CZ  . PHE   A 1 37  ? -2.70397  -18.47109 -11.55867 1.000 23.97921 ? 44  PHE   A CZ  1 
ATOM   240  N N   . LEU   A 1 38  ? -1.96852  -14.32469 -11.87557 1.000 22.88002 ? 45  LEU   A N   1 
ATOM   241  C CA  . LEU   A 1 38  ? -3.27419  -14.15494 -12.49809 1.000 21.63063 ? 45  LEU   A CA  1 
ATOM   242  C C   . LEU   A 1 38  ? -3.57615  -12.67719 -12.70690 1.000 23.30635 ? 45  LEU   A C   1 
ATOM   243  O O   . LEU   A 1 38  ? -4.14471  -12.28945 -13.74360 1.000 25.18502 ? 45  LEU   A O   1 
ATOM   244  C CB  . LEU   A 1 38  ? -4.34550  -14.81286 -11.63087 1.000 22.39903 ? 45  LEU   A CB  1 
ATOM   245  C CG  . LEU   A 1 38  ? -5.73242  -14.79894 -12.30819 1.000 22.44685 ? 45  LEU   A CG  1 
ATOM   246  C CD1 . LEU   A 1 38  ? -5.71331  -15.61625 -13.58240 1.000 23.14910 ? 45  LEU   A CD1 1 
ATOM   247  C CD2 . LEU   A 1 38  ? -6.78689  -15.29767 -11.33476 1.000 27.32839 ? 45  LEU   A CD2 1 
ATOM   248  N N   . ARG   A 1 39  ? -3.19392  -11.83571 -11.72726 1.000 22.54617 ? 46  ARG   A N   1 
ATOM   249  C CA  . ARG   A 1 39  ? -3.28217  -10.38504 -11.90399 1.000 23.44664 ? 46  ARG   A CA  1 
ATOM   250  C C   . ARG   A 1 39  ? -2.52685  -9.93410  -13.14400 1.000 24.94718 ? 46  ARG   A C   1 
ATOM   251  O O   . ARG   A 1 39  ? -3.02434  -9.11668  -13.92859 1.000 23.10202 ? 46  ARG   A O   1 
ATOM   252  C CB  . ARG   A 1 39  ? -2.72093  -9.67592  -10.66199 1.000 25.67262 ? 46  ARG   A CB  1 
ATOM   253  C CG  . ARG   A 1 39  ? -2.73341  -8.16655  -10.74943 1.000 29.10491 ? 46  ARG   A CG  1 
ATOM   254  C CD  . ARG   A 1 39  ? -2.02549  -7.50633  -9.53159  1.000 31.51801 ? 46  ARG   A CD  1 
ATOM   255  N NE  . ARG   A 1 39  ? -0.57709  -7.69865  -9.62022  1.000 36.07376 ? 46  ARG   A NE  1 
ATOM   256  C CZ  . ARG   A 1 39  ? 0.26358   -7.67356  -8.59569  1.000 37.67693 ? 46  ARG   A CZ  1 
ATOM   257  N NH1 . ARG   A 1 39  ? -0.15201  -7.41950  -7.36335  1.000 35.56043 ? 46  ARG   A NH1 1 
ATOM   258  N NH2 . ARG   A 1 39  ? 1.55760   -7.91577  -8.81311  1.000 35.72414 ? 46  ARG   A NH2 1 
ATOM   259  N N   . GLU   A 1 40  ? -1.31449  -10.45210 -13.34064 1.000 22.59427 ? 47  GLU   A N   1 
ATOM   260  C CA  . GLU   A 1 40  ? -0.52416  -9.99085  -14.47724 1.000 23.49281 ? 47  GLU   A CA  1 
ATOM   261  C C   . GLU   A 1 40  ? -1.13863  -10.41481 -15.80052 1.000 23.09741 ? 47  GLU   A C   1 
ATOM   262  O O   . GLU   A 1 40  ? -1.08841  -9.65574  -16.78412 1.000 23.05885 ? 47  GLU   A O   1 
ATOM   263  C CB  . GLU   A 1 40  ? 0.91651   -10.50412 -14.36443 1.000 21.52908 ? 47  GLU   A CB  1 
ATOM   264  C CG  . GLU   A 1 40  ? 1.58726   -10.04800 -13.07057 1.000 26.37238 ? 47  GLU   A CG  1 
ATOM   265  C CD  . GLU   A 1 40  ? 1.61467   -8.52780  -12.93182 1.000 32.23470 ? 47  GLU   A CD  1 
ATOM   266  O OE1 . GLU   A 1 40  ? 1.65329   -7.82326  -13.96388 1.000 32.38041 ? 47  GLU   A OE1 1 
ATOM   267  O OE2 . GLU   A 1 40  ? 1.49818   -8.03247  -11.78023 1.000 33.57950 ? 47  GLU   A OE2 1 
ATOM   268  N N   . LEU   A 1 41  ? -1.68346  -11.63600 -15.87267 1.000 21.14538 ? 48  LEU   A N   1 
ATOM   269  C CA  . LEU   A 1 41  ? -2.23979  -12.09142 -17.14630 1.000 24.15700 ? 48  LEU   A CA  1 
ATOM   270  C C   . LEU   A 1 41  ? -3.56025  -11.38516 -17.44812 1.000 22.34096 ? 48  LEU   A C   1 
ATOM   271  O O   . LEU   A 1 41  ? -3.85728  -11.09233 -18.61720 1.000 24.33520 ? 48  LEU   A O   1 
ATOM   272  C CB  . LEU   A 1 41  ? -2.43895  -13.60723 -17.13766 1.000 22.40500 ? 48  LEU   A CB  1 
ATOM   273  C CG  . LEU   A 1 41  ? -1.12637  -14.39942 -17.07430 1.000 22.29356 ? 48  LEU   A CG  1 
ATOM   274  C CD1 . LEU   A 1 41  ? -1.41222  -15.89821 -16.87288 1.000 23.05911 ? 48  LEU   A CD1 1 
ATOM   275  C CD2 . LEU   A 1 41  ? -0.27646  -14.16770 -18.34101 1.000 22.90459 ? 48  LEU   A CD2 1 
ATOM   276  N N   . ILE   A 1 42  ? -4.36796  -11.12109 -16.41151 1.000 21.07039 ? 49  ILE   A N   1 
ATOM   277  C CA  . ILE   A 1 42  ? -5.59242  -10.34819 -16.62012 1.000 21.48799 ? 49  ILE   A CA  1 
ATOM   278  C C   . ILE   A 1 42  ? -5.26785  -8.91871  -17.03778 1.000 23.82943 ? 49  ILE   A C   1 
ATOM   279  O O   . ILE   A 1 42  ? -5.93408  -8.34634  -17.90834 1.000 22.95317 ? 49  ILE   A O   1 
ATOM   280  C CB  . ILE   A 1 42  ? -6.48954  -10.41572 -15.36756 1.000 23.94750 ? 49  ILE   A CB  1 
ATOM   281  C CG1 . ILE   A 1 42  ? -7.08078  -11.83477 -15.26020 1.000 22.26525 ? 49  ILE   A CG1 1 
ATOM   282  C CG2 . ILE   A 1 42  ? -7.60989  -9.33055  -15.40883 1.000 24.95452 ? 49  ILE   A CG2 1 
ATOM   283  C CD1 . ILE   A 1 42  ? -7.84159  -12.13180 -13.91421 1.000 25.83425 ? 49  ILE   A CD1 1 
ATOM   284  N N   . SER   A 1 43  ? -4.23983  -8.31084  -16.42809 1.000 21.89321 ? 50  SER   A N   1 
ATOM   285  C CA  . SER   A 1 43  ? -3.79752  -6.98965  -16.87350 1.000 24.45910 ? 50  SER   A CA  1 
ATOM   286  C C   . SER   A 1 43  ? -3.35879  -6.99257  -18.34530 1.000 24.49021 ? 50  SER   A C   1 
ATOM   287  O O   . SER   A 1 43  ? -3.67945  -6.06024  -19.11036 1.000 22.07521 ? 50  SER   A O   1 
ATOM   288  C CB  . SER   A 1 43  ? -2.64779  -6.52931  -15.96476 1.000 27.77695 ? 50  SER   A CB  1 
ATOM   289  O OG  . SER   A 1 43  ? -2.24872  -5.22429  -16.31546 1.000 32.10193 ? 50  SER   A OG  1 
ATOM   290  N N   . ASN   A 1 44  ? -2.58532  -8.00621  -18.75527 1.000 20.44560 ? 51  ASN   A N   1 
ATOM   291  C CA  . ASN   A 1 44  ? -2.18752  -8.10170  -20.15930 1.000 22.68884 ? 51  ASN   A CA  1 
ATOM   292  C C   . ASN   A 1 44  ? -3.40889  -8.22197  -21.06942 1.000 20.50541 ? 51  ASN   A C   1 
ATOM   293  O O   . ASN   A 1 44  ? -3.46331  -7.58996  -22.13438 1.000 23.40963 ? 51  ASN   A O   1 
ATOM   294  C CB  . ASN   A 1 44  ? -1.26214  -9.30472  -20.36434 1.000 23.33801 ? 51  ASN   A CB  1 
ATOM   295  C CG  . ASN   A 1 44  ? 0.11906   -9.04683  -19.85761 1.000 32.62191 ? 51  ASN   A CG  1 
ATOM   296  O OD1 . ASN   A 1 44  ? 0.41223   -7.97287  -19.35258 1.000 28.43722 ? 51  ASN   A OD1 1 
ATOM   297  N ND2 . ASN   A 1 44  ? 0.97278   -10.04169 -19.95813 1.000 29.66015 ? 51  ASN   A ND2 1 
ATOM   298  N N   . SER   A 1 45  ? -4.40716  -9.00894  -20.65350 1.000 20.47320 ? 52  SER   A N   1 
ATOM   299  C CA  . SER   A 1 45  ? -5.63038  -9.12456  -21.44006 1.000 22.52625 ? 52  SER   A CA  1 
ATOM   300  C C   . SER   A 1 45  ? -6.35086  -7.78599  -21.53194 1.000 21.32491 ? 52  SER   A C   1 
ATOM   301  O O   . SER   A 1 45  ? -6.83061  -7.40458  -22.61461 1.000 21.51486 ? 52  SER   A O   1 
ATOM   302  C CB  . SER   A 1 45  ? -6.56224  -10.20233 -20.84676 1.000 20.92075 ? 52  SER   A CB  1 
ATOM   303  O OG  . SER   A 1 45  ? -6.01447  -11.52180 -21.01385 1.000 24.27266 ? 52  SER   A OG  1 
ATOM   304  N N   . SER   A 1 46  ? -6.44143  -7.04643  -20.40779 1.000 20.90712 ? 53  SER   A N   1 
ATOM   305  C CA  . SER   A 1 46  ? -7.10546  -5.74685  -20.46341 1.000 21.78991 ? 53  SER   A CA  1 
ATOM   306  C C   . SER   A 1 46  ? -6.36815  -4.79104  -21.40264 1.000 24.36906 ? 53  SER   A C   1 
ATOM   307  O O   . SER   A 1 46  ? -6.99785  -4.02276  -22.13912 1.000 22.61846 ? 53  SER   A O   1 
ATOM   308  C CB  . SER   A 1 46  ? -7.21000  -5.15044  -19.04779 1.000 20.72115 ? 53  SER   A CB  1 
ATOM   309  O OG  . SER   A 1 46  ? -7.79125  -3.85444  -19.05677 1.000 24.34551 ? 53  SER   A OG  1 
ATOM   310  N N   . ASP   A 1 47  ? -5.02620  -4.81000  -21.39301 1.000 21.80408 ? 54  ASP   A N   1 
ATOM   311  C CA  . ASP   A 1 47  ? -4.28426  -3.98729  -22.35660 1.000 22.73274 ? 54  ASP   A CA  1 
ATOM   312  C C   . ASP   A 1 47  ? -4.58136  -4.37082  -23.80191 1.000 24.73722 ? 54  ASP   A C   1 
ATOM   313  O O   . ASP   A 1 47  ? -4.67260  -3.49212  -24.66771 1.000 23.78868 ? 54  ASP   A O   1 
ATOM   314  C CB  . ASP   A 1 47  ? -2.77008  -4.07315  -22.10454 1.000 24.20074 ? 54  ASP   A CB  1 
ATOM   315  C CG  . ASP   A 1 47  ? -2.32610  -3.42187  -20.80253 1.000 31.06667 ? 54  ASP   A CG  1 
ATOM   316  O OD1 . ASP   A 1 47  ? -3.13278  -2.71232  -20.12978 1.000 33.27966 ? 54  ASP   A OD1 1 
ATOM   317  O OD2 . ASP   A 1 47  ? -1.14091  -3.64336  -20.42078 1.000 33.04952 ? 54  ASP   A OD2 1 
ATOM   318  N N   . ALA   A 1 48  ? -4.70310  -5.67726  -24.08762 1.000 21.99144 ? 55  ALA   A N   1 
ATOM   319  C CA  . ALA   A 1 48  ? -4.95618  -6.12319  -25.45272 1.000 23.69459 ? 55  ALA   A CA  1 
ATOM   320  C C   . ALA   A 1 48  ? -6.35736  -5.72831  -25.90004 1.000 21.34432 ? 55  ALA   A C   1 
ATOM   321  O O   . ALA   A 1 48  ? -6.56829  -5.37964  -27.06544 1.000 22.40986 ? 55  ALA   A O   1 
ATOM   322  C CB  . ALA   A 1 48  ? -4.76899  -7.63476  -25.55594 1.000 24.04846 ? 55  ALA   A CB  1 
ATOM   323  N N   . LEU   A 1 49  ? -7.31927  -5.76870  -24.97231 1.000 23.43686 ? 56  LEU   A N   1 
ATOM   324  C CA  . LEU   A 1 49  ? -8.67131  -5.30100  -25.25787 1.000 21.15353 ? 56  LEU   A CA  1 
ATOM   325  C C   . LEU   A 1 49  ? -8.71253  -3.78905  -25.48039 1.000 22.59262 ? 56  LEU   A C   1 
ATOM   326  O O   . LEU   A 1 49  ? -9.42234  -3.31442  -26.37701 1.000 22.94831 ? 56  LEU   A O   1 
ATOM   327  C CB  . LEU   A 1 49  ? -9.58563  -5.72052  -24.10738 1.000 20.58736 ? 56  LEU   A CB  1 
ATOM   328  C CG  . LEU   A 1 49  ? -9.81251  -7.23609  -24.02807 1.000 22.90290 ? 56  LEU   A CG  1 
ATOM   329  C CD1 . LEU   A 1 49  ? -10.19939 -7.60640  -22.60715 1.000 24.13207 ? 56  LEU   A CD1 1 
ATOM   330  C CD2 . LEU   A 1 49  ? -10.89263 -7.68270  -25.00236 1.000 23.62825 ? 56  LEU   A CD2 1 
ATOM   331  N N   . ASP   A 1 50  ? -7.98934  -3.00557  -24.66911 1.000 22.02807 ? 57  ASP   A N   1 
ATOM   332  C CA  . ASP   A 1 50  ? -7.92698  -1.56360  -24.92527 1.000 23.91904 ? 57  ASP   A CA  1 
ATOM   333  C C   . ASP   A 1 50  ? -7.43610  -1.26692  -26.34479 1.000 25.91647 ? 57  ASP   A C   1 
ATOM   334  O O   . ASP   A 1 50  ? -7.90900  -0.32023  -26.98714 1.000 25.23918 ? 57  ASP   A O   1 
ATOM   335  C CB  . ASP   A 1 50  ? -6.99045  -0.84522  -23.94382 1.000 24.44513 ? 57  ASP   A CB  1 
ATOM   336  C CG  . ASP   A 1 50  ? -7.46745  -0.84306  -22.49847 1.000 28.78791 ? 57  ASP   A CG  1 
ATOM   337  O OD1 . ASP   A 1 50  ? -8.65343  -1.15396  -22.20093 1.000 30.76697 ? 57  ASP   A OD1 1 
ATOM   338  O OD2 . ASP   A 1 50  ? -6.64479  -0.43955  -21.64161 1.000 28.81867 ? 57  ASP   A OD2 1 
ATOM   339  N N   . LYS   A 1 51  ? -6.43938  -2.03188  -26.82985 1.000 23.49284 ? 58  LYS   A N   1 
ATOM   340  C CA  . LYS   A 1 51  ? -5.86608  -1.74629  -28.14775 1.000 23.66232 ? 58  LYS   A CA  1 
ATOM   341  C C   . LYS   A 1 51  ? -6.86582  -1.98916  -29.27209 1.000 22.42467 ? 58  LYS   A C   1 
ATOM   342  O O   . LYS   A 1 51  ? -6.95569  -1.17830  -30.20514 1.000 27.55647 ? 58  LYS   A O   1 
ATOM   343  C CB  . LYS   A 1 51  ? -4.60225  -2.59289  -28.38570 1.000 25.49108 ? 58  LYS   A CB  1 
ATOM   344  C CG  . LYS   A 1 51  ? -3.42144  -2.22570  -27.49469 1.000 30.32079 ? 58  LYS   A CG  1 
ATOM   345  C CD  . LYS   A 1 51  ? -2.26878  -3.24196  -27.68915 1.000 27.40037 ? 58  LYS   A CD  1 
ATOM   346  C CE  . LYS   A 1 51  ? -1.19191  -3.09905  -26.60711 1.000 36.13454 ? 58  LYS   A CE  1 
ATOM   347  N NZ  . LYS   A 1 51  ? -0.09810  -4.09908  -26.82459 1.000 40.65012 ? 58  LYS   A NZ  1 
ATOM   348  N N   . ILE   A 1 52  ? -7.61132  -3.09960  -29.23254 1.000 22.59861 ? 59  ILE   A N   1 
ATOM   349  C CA  . ILE   A 1 52  ? -8.56976  -3.31001  -30.32023 1.000 23.53849 ? 59  ILE   A CA  1 
ATOM   350  C C   . ILE   A 1 52  ? -9.72909  -2.33312  -30.18421 1.000 27.34211 ? 59  ILE   A C   1 
ATOM   351  O O   . ILE   A 1 52  ? -10.28126 -1.87577  -31.19702 1.000 24.40783 ? 59  ILE   A O   1 
ATOM   352  C CB  . ILE   A 1 52  ? -9.04411  -4.77169  -30.39295 1.000 22.85553 ? 59  ILE   A CB  1 
ATOM   353  C CG1 . ILE   A 1 52  ? -9.81585  -5.04275  -31.69725 1.000 26.20224 ? 59  ILE   A CG1 1 
ATOM   354  C CG2 . ILE   A 1 52  ? -9.84921  -5.17935  -29.15907 1.000 23.43187 ? 59  ILE   A CG2 1 
ATOM   355  C CD1 . ILE   A 1 52  ? -9.00679  -4.76377  -32.99559 1.000 26.32259 ? 59  ILE   A CD1 1 
ATOM   356  N N   . ARG   A 1 53  ? -10.10628 -1.97226  -28.95573 1.000 24.76909 ? 60  ARG   A N   1 
ATOM   357  C CA  . ARG   A 1 53  ? -11.13124 -0.93194  -28.82356 1.000 25.94446 ? 60  ARG   A CA  1 
ATOM   358  C C   . ARG   A 1 53  ? -10.68381 0.36786   -29.47164 1.000 26.97096 ? 60  ARG   A C   1 
ATOM   359  O O   . ARG   A 1 53  ? -11.45231 0.99616   -30.21218 1.000 27.31161 ? 60  ARG   A O   1 
ATOM   360  C CB  . ARG   A 1 53  ? -11.52241 -0.67337  -27.36903 1.000 29.46572 ? 60  ARG   A CB  1 
ATOM   361  C CG  . ARG   A 1 53  ? -12.71273 0.32735   -27.34145 1.000 33.60579 ? 60  ARG   A CG  1 
ATOM   362  C CD  . ARG   A 1 53  ? -13.30175 0.63851   -25.98954 1.000 50.28046 ? 60  ARG   A CD  1 
ATOM   363  N NE  . ARG   A 1 53  ? -14.25358 -0.33721  -25.47620 1.000 54.42062 ? 60  ARG   A NE  1 
ATOM   364  C CZ  . ARG   A 1 53  ? -14.23017 -0.80641  -24.23656 1.000 46.57866 ? 60  ARG   A CZ  1 
ATOM   365  N NH1 . ARG   A 1 53  ? -13.20854 -0.56196  -23.42448 1.000 42.30876 ? 60  ARG   A NH1 1 
ATOM   366  N NH2 . ARG   A 1 53  ? -15.26418 -1.51975  -23.79361 1.000 39.35756 ? 60  ARG   A NH2 1 
ATOM   367  N N   . TYR   A 1 54  ? -9.44314  0.78834   -29.21440 1.000 25.63213 ? 61  TYR   A N   1 
ATOM   368  C CA  . TYR   A 1 54  ? -8.98276  2.05510   -29.77620 1.000 26.11947 ? 61  TYR   A CA  1 
ATOM   369  C C   . TYR   A 1 54  ? -8.99001  2.01655   -31.30094 1.000 30.32537 ? 61  TYR   A C   1 
ATOM   370  O O   . TYR   A 1 54  ? -9.42381  2.97669   -31.95571 1.000 29.36207 ? 61  TYR   A O   1 
ATOM   371  C CB  . TYR   A 1 54  ? -7.58501  2.39036   -29.24605 1.000 27.84111 ? 61  TYR   A CB  1 
ATOM   372  C CG  . TYR   A 1 54  ? -7.12293  3.73552   -29.74710 1.000 31.07829 ? 61  TYR   A CG  1 
ATOM   373  C CD1 . TYR   A 1 54  ? -7.65086  4.91319   -29.22591 1.000 29.37020 ? 61  TYR   A CD1 1 
ATOM   374  C CD2 . TYR   A 1 54  ? -6.20546  3.82961   -30.78689 1.000 33.85382 ? 61  TYR   A CD2 1 
ATOM   375  C CE1 . TYR   A 1 54  ? -7.25683  6.14769   -29.69972 1.000 33.18481 ? 61  TYR   A CE1 1 
ATOM   376  C CE2 . TYR   A 1 54  ? -5.81377  5.06497   -31.27949 1.000 34.98355 ? 61  TYR   A CE2 1 
ATOM   377  C CZ  . TYR   A 1 54  ? -6.34164  6.21745   -30.72818 1.000 38.12298 ? 61  TYR   A CZ  1 
ATOM   378  O OH  . TYR   A 1 54  ? -5.95659  7.45341   -31.19937 1.000 40.03812 ? 61  TYR   A OH  1 
ATOM   379  N N   . GLU   A 1 55  ? -8.49513  0.92176   -31.88840 1.000 27.82553 ? 62  GLU   A N   1 
ATOM   380  C CA  . GLU   A 1 55  ? -8.49984  0.79493   -33.34721 1.000 29.87385 ? 62  GLU   A CA  1 
ATOM   381  C C   . GLU   A 1 55  ? -9.92316  0.86864   -33.89574 1.000 30.88951 ? 62  GLU   A C   1 
ATOM   382  O O   . GLU   A 1 55  ? -10.17001 1.51239   -34.92526 1.000 35.75570 ? 62  GLU   A O   1 
ATOM   383  C CB  . GLU   A 1 55  ? -7.83187  -0.52298  -33.72634 1.000 29.72405 ? 62  GLU   A CB  1 
ATOM   384  C CG  . GLU   A 1 55  ? -6.32165  -0.40603  -33.65195 1.000 34.39162 ? 62  GLU   A CG  1 
ATOM   385  C CD  . GLU   A 1 55  ? -5.58342  -1.52033  -34.37900 1.000 43.68610 ? 62  GLU   A CD  1 
ATOM   386  O OE1 . GLU   A 1 55  ? -6.23101  -2.50583  -34.79491 1.000 38.05713 ? 62  GLU   A OE1 1 
ATOM   387  O OE2 . GLU   A 1 55  ? -4.33668  -1.43627  -34.46783 1.000 42.94433 ? 62  GLU   A OE2 1 
ATOM   388  N N   . SER   A 1 56  ? -10.88683 0.26629   -33.18714 1.000 29.34254 ? 63  SER   A N   1 
ATOM   389  C CA  . SER   A 1 56  ? -12.27306 0.25303   -33.66819 1.000 30.21282 ? 63  SER   A CA  1 
ATOM   390  C C   . SER   A 1 56  ? -12.92115 1.63648   -33.62435 1.000 34.83556 ? 63  SER   A C   1 
ATOM   391  O O   . SER   A 1 56  ? -13.95864 1.84134   -34.26625 1.000 31.23735 ? 63  SER   A O   1 
ATOM   392  C CB  . SER   A 1 56  ? -13.12326 -0.72431  -32.84527 1.000 29.97566 ? 63  SER   A CB  1 
ATOM   393  O OG  . SER   A 1 56  ? -13.43036 -0.19949  -31.55459 1.000 31.79974 ? 63  SER   A OG  1 
ATOM   394  N N   . LEU   A 1 57  ? -12.34043 2.59607   -32.89931 1.000 29.99048 ? 64  LEU   A N   1 
ATOM   395  C CA  . LEU   A 1 57  ? -12.96554 3.91565   -32.82660 1.000 31.74411 ? 64  LEU   A CA  1 
ATOM   396  C C   . LEU   A 1 57  ? -12.96031 4.61738   -34.16881 1.000 39.04639 ? 64  LEU   A C   1 
ATOM   397  O O   . LEU   A 1 57  ? -13.85217 5.42536   -34.45366 1.000 42.05451 ? 64  LEU   A O   1 
ATOM   398  C CB  . LEU   A 1 57  ? -12.25142 4.79400   -31.80212 1.000 33.28987 ? 64  LEU   A CB  1 
ATOM   399  C CG  . LEU   A 1 57  ? -12.39299 4.33315   -30.35877 1.000 33.20227 ? 64  LEU   A CG  1 
ATOM   400  C CD1 . LEU   A 1 57  ? -11.71086 5.33297   -29.44473 1.000 33.85127 ? 64  LEU   A CD1 1 
ATOM   401  C CD2 . LEU   A 1 57  ? -13.84849 4.11493   -29.99387 1.000 36.23678 ? 64  LEU   A CD2 1 
ATOM   402  N N   . THR   A 1 58  ? -11.95470 4.36350   -34.99258 1.000 35.57795 ? 65  THR   A N   1 
ATOM   403  C CA  . THR   A 1 58  ? -11.90175 4.98791   -36.30203 1.000 35.90447 ? 65  THR   A CA  1 
ATOM   404  C C   . THR   A 1 58  ? -12.17846 4.01340   -37.43732 1.000 43.07777 ? 65  THR   A C   1 
ATOM   405  O O   . THR   A 1 58  ? -12.42827 4.46175   -38.55958 1.000 44.10067 ? 65  THR   A O   1 
ATOM   406  C CB  . THR   A 1 58  ? -10.53620 5.65894   -36.51489 1.000 45.47971 ? 65  THR   A CB  1 
ATOM   407  O OG1 . THR   A 1 58  ? -9.49439  4.68415   -36.35124 1.000 43.39181 ? 65  THR   A OG1 1 
ATOM   408  C CG2 . THR   A 1 58  ? -10.33605 6.78245   -35.49399 1.000 42.71730 ? 65  THR   A CG2 1 
ATOM   409  N N   . ASP   A 1 59  ? -12.16661 2.70548   -37.17259 1.000 43.19105 ? 66  ASP   A N   1 
ATOM   410  C CA  . ASP   A 1 59  ? -12.41763 1.68533   -38.19091 1.000 39.11224 ? 66  ASP   A CA  1 
ATOM   411  C C   . ASP   A 1 59  ? -13.26584 0.58031   -37.57289 1.000 37.91983 ? 66  ASP   A C   1 
ATOM   412  O O   . ASP   A 1 59  ? -12.73417 -0.37635  -36.99890 1.000 35.98528 ? 66  ASP   A O   1 
ATOM   413  C CB  . ASP   A 1 59  ? -11.10521 1.12361   -38.73606 1.000 39.14422 ? 66  ASP   A CB  1 
ATOM   414  C CG  . ASP   A 1 59  ? -11.32235 0.13697   -39.87958 1.000 47.32646 ? 66  ASP   A CG  1 
ATOM   415  O OD1 . ASP   A 1 59  ? -12.49530 -0.12724  -40.22859 1.000 47.86459 ? 66  ASP   A OD1 1 
ATOM   416  O OD2 . ASP   A 1 59  ? -10.31987 -0.36720  -40.43555 1.000 49.29674 ? 66  ASP   A OD2 1 
ATOM   417  N N   . PRO   A 1 60  ? -14.59963 0.68121   -37.66454 1.000 43.98333 ? 67  PRO   A N   1 
ATOM   418  C CA  . PRO   A 1 60  ? -15.45207 -0.30192  -36.96453 1.000 37.16753 ? 67  PRO   A CA  1 
ATOM   419  C C   . PRO   A 1 60  ? -15.26646 -1.72248  -37.47404 1.000 38.52841 ? 67  PRO   A C   1 
ATOM   420  O O   . PRO   A 1 60  ? -15.52506 -2.67828  -36.72854 1.000 38.83164 ? 67  PRO   A O   1 
ATOM   421  C CB  . PRO   A 1 60  ? -16.87530 0.18681   -37.25668 1.000 40.03006 ? 67  PRO   A CB  1 
ATOM   422  C CG  . PRO   A 1 60  ? -16.75343 1.60363   -37.57895 1.000 48.81289 ? 67  PRO   A CG  1 
ATOM   423  C CD  . PRO   A 1 60  ? -15.33317 1.90930   -37.99885 1.000 43.06677 ? 67  PRO   A CD  1 
ATOM   424  N N   . SER   A 1 61  ? -14.84462 -1.89117  -38.73626 1.000 41.67919 ? 68  SER   A N   1 
ATOM   425  C CA  . SER   A 1 61  ? -14.66790 -3.23062  -39.28182 1.000 39.64184 ? 68  SER   A CA  1 
ATOM   426  C C   . SER   A 1 61  ? -13.59027 -4.01015  -38.55130 1.000 37.95907 ? 68  SER   A C   1 
ATOM   427  O O   . SER   A 1 61  ? -13.50203 -5.22865  -38.72533 1.000 37.93381 ? 68  SER   A O   1 
ATOM   428  C CB  . SER   A 1 61  ? -14.33758 -3.16268  -40.77905 1.000 39.97900 ? 68  SER   A CB  1 
ATOM   429  O OG  . SER   A 1 61  ? -13.03193 -2.64361  -40.99348 1.000 44.12672 ? 68  SER   A OG  1 
ATOM   430  N N   . LYS   A 1 62  ? -12.78272 -3.34951  -37.71896 1.000 33.52034 ? 69  LYS   A N   1 
ATOM   431  C CA  . LYS   A 1 62  ? -11.81746 -4.09561  -36.93639 1.000 31.40209 ? 69  LYS   A CA  1 
ATOM   432  C C   . LYS   A 1 62  ? -12.49707 -5.06217  -35.97567 1.000 30.76697 ? 69  LYS   A C   1 
ATOM   433  O O   . LYS   A 1 62  ? -11.83801 -5.95965  -35.45188 1.000 30.68000 ? 69  LYS   A O   1 
ATOM   434  C CB  . LYS   A 1 62  ? -10.91080 -3.13628  -36.17046 1.000 34.89071 ? 69  LYS   A CB  1 
ATOM   435  C CG  . LYS   A 1 62  ? -10.07502 -2.26583  -37.08698 1.000 41.41933 ? 69  LYS   A CG  1 
ATOM   436  C CD  . LYS   A 1 62  ? -8.60565  -2.60728  -36.97539 1.000 39.12414 ? 69  LYS   A CD  1 
ATOM   437  C CE  . LYS   A 1 62  ? -7.75283  -1.79031  -37.93353 1.000 43.90217 ? 69  LYS   A CE  1 
ATOM   438  N NZ  . LYS   A 1 62  ? -6.33059  -2.20069  -37.75326 1.000 48.97091 ? 69  LYS   A NZ  1 
ATOM   439  N N   . LEU   A 1 63  ? -13.79466 -4.89771  -35.72605 1.000 32.31198 ? 70  LEU   A N   1 
ATOM   440  C CA  . LEU   A 1 63  ? -14.52390 -5.80125  -34.85482 1.000 35.62442 ? 70  LEU   A CA  1 
ATOM   441  C C   . LEU   A 1 63  ? -15.33814 -6.82686  -35.63439 1.000 35.11952 ? 70  LEU   A C   1 
ATOM   442  O O   . LEU   A 1 63  ? -16.11924 -7.56228  -35.02517 1.000 35.93152 ? 70  LEU   A O   1 
ATOM   443  C CB  . LEU   A 1 63  ? -15.43127 -5.01021  -33.89920 1.000 34.45445 ? 70  LEU   A CB  1 
ATOM   444  C CG  . LEU   A 1 63  ? -14.73588 -4.07712  -32.89907 1.000 33.92564 ? 70  LEU   A CG  1 
ATOM   445  C CD1 . LEU   A 1 63  ? -15.75064 -3.33896  -32.00794 1.000 34.80911 ? 70  LEU   A CD1 1 
ATOM   446  C CD2 . LEU   A 1 63  ? -13.74524 -4.86034  -32.04010 1.000 32.19938 ? 70  LEU   A CD2 1 
ATOM   447  N N   . ASP   A 1 64  ? -15.15235 -6.91594  -36.95518 1.000 32.08166 ? 71  ASP   A N   1 
ATOM   448  C CA  . ASP   A 1 64  ? -15.88339 -7.92751  -37.71950 1.000 36.23614 ? 71  ASP   A CA  1 
ATOM   449  C C   . ASP   A 1 64  ? -15.52402 -9.33032  -37.24588 1.000 36.61726 ? 71  ASP   A C   1 
ATOM   450  O O   . ASP   A 1 64  ? -16.33585 -10.25638 -37.36096 1.000 40.56776 ? 71  ASP   A O   1 
ATOM   451  C CB  . ASP   A 1 64  ? -15.60296 -7.78545  -39.22266 1.000 38.71396 ? 71  ASP   A CB  1 
ATOM   452  C CG  . ASP   A 1 64  ? -16.21710 -6.53254  -39.83008 1.000 46.24305 ? 71  ASP   A CG  1 
ATOM   453  O OD1 . ASP   A 1 64  ? -15.86646 -6.21609  -40.99102 1.000 48.50228 ? 71  ASP   A OD1 1 
ATOM   454  O OD2 . ASP   A 1 64  ? -17.05928 -5.87865  -39.17050 1.000 53.22340 ? 71  ASP   A OD2 1 
ATOM   455  N N   . SER   A 1 65  ? -14.32182 -9.49849  -36.70694 1.000 33.61228 ? 72  SER   A N   1 
ATOM   456  C CA  . SER   A 1 65  ? -13.84901 -10.74481 -36.12453 1.000 30.39308 ? 72  SER   A CA  1 
ATOM   457  C C   . SER   A 1 65  ? -14.37332 -10.98554 -34.71570 1.000 36.18159 ? 72  SER   A C   1 
ATOM   458  O O   . SER   A 1 65  ? -13.88806 -11.89680 -34.03795 1.000 37.64886 ? 72  SER   A O   1 
ATOM   459  C CB  . SER   A 1 65  ? -12.31828 -10.74508 -36.14846 1.000 35.00205 ? 72  SER   A CB  1 
ATOM   460  O OG  . SER   A 1 65  ? -11.82556 -9.55261  -35.54218 1.000 31.46438 ? 72  SER   A OG  1 
ATOM   461  N N   . GLY   A 1 66  ? -15.34267 -10.19119 -34.25034 1.000 33.26299 ? 73  GLY   A N   1 
ATOM   462  C CA  . GLY   A 1 66  ? -15.88125 -10.38432 -32.91324 1.000 35.16351 ? 73  GLY   A CA  1 
ATOM   463  C C   . GLY   A 1 66  ? -16.13187 -9.06629  -32.20639 1.000 36.53968 ? 73  GLY   A C   1 
ATOM   464  O O   . GLY   A 1 66  ? -15.18998 -8.31369  -31.96077 1.000 31.34869 ? 73  GLY   A O   1 
ATOM   465  N N   . LYS   A 1 67  ? -17.39395 -8.75712  -31.89476 1.000 32.71760 ? 74  LYS   A N   1 
ATOM   466  C CA  . LYS   A 1 67  ? -17.72130 -7.47687  -31.28135 1.000 32.11051 ? 74  LYS   A CA  1 
ATOM   467  C C   . LYS   A 1 67  ? -17.56300 -7.47091  -29.76605 1.000 33.70583 ? 74  LYS   A C   1 
ATOM   468  O O   . LYS   A 1 67  ? -17.38234 -6.39813  -29.17843 1.000 34.15171 ? 74  LYS   A O   1 
ATOM   469  C CB  . LYS   A 1 67  ? -19.16349 -7.08825  -31.62677 1.000 33.75533 ? 74  LYS   A CB  1 
ATOM   470  C CG  . LYS   A 1 67  ? -19.26980 -6.22299  -32.87580 1.000 43.90932 ? 74  LYS   A CG  1 
ATOM   471  C CD  . LYS   A 1 67  ? -20.66721 -6.31862  -33.46246 1.000 51.40032 ? 74  LYS   A CD  1 
ATOM   472  C CE  . LYS   A 1 67  ? -20.70373 -5.87674  -34.92439 1.000 54.48442 ? 74  LYS   A CE  1 
ATOM   473  N NZ  . LYS   A 1 67  ? -21.36663 -4.54498  -35.12978 1.000 61.48817 ? 74  LYS   A NZ  1 
ATOM   474  N N   . GLU   A 1 68  ? -17.64213 -8.62801  -29.11397 1.000 29.90963 ? 75  GLU   A N   1 
ATOM   475  C CA  . GLU   A 1 68  ? -17.63479 -8.67378  -27.65696 1.000 31.41076 ? 75  GLU   A CA  1 
ATOM   476  C C   . GLU   A 1 68  ? -16.21430 -8.57558  -27.12574 1.000 29.51009 ? 75  GLU   A C   1 
ATOM   477  O O   . GLU   A 1 68  ? -15.32167 -9.27904  -27.60245 1.000 32.67104 ? 75  GLU   A O   1 
ATOM   478  C CB  . GLU   A 1 68  ? -18.27627 -9.96834  -27.15184 1.000 33.20113 ? 75  GLU   A CB  1 
ATOM   479  C CG  . GLU   A 1 68  ? -19.79056 -10.05900 -27.34460 1.000 38.56885 ? 75  GLU   A CG  1 
ATOM   480  C CD  . GLU   A 1 68  ? -20.20974 -10.37846 -28.77232 1.000 56.56534 ? 75  GLU   A CD  1 
ATOM   481  O OE1 . GLU   A 1 68  ? -19.50543 -11.19101 -29.42235 1.000 54.26440 ? 75  GLU   A OE1 1 
ATOM   482  O OE2 . GLU   A 1 68  ? -21.25047 -9.83366  -29.23899 1.000 53.59584 ? 75  GLU   A OE2 1 
ATOM   483  N N   . LEU   A 1 69  ? -16.01203 -7.72399  -26.12714 1.000 24.66501 ? 76  LEU   A N   1 
ATOM   484  C CA  . LEU   A 1 69  ? -14.69679 -7.49683  -25.51835 1.000 25.05939 ? 76  LEU   A CA  1 
ATOM   485  C C   . LEU   A 1 69  ? -14.74623 -8.01969  -24.08286 1.000 22.19002 ? 76  LEU   A C   1 
ATOM   486  O O   . LEU   A 1 69  ? -15.39367 -7.40360  -23.22751 1.000 24.71725 ? 76  LEU   A O   1 
ATOM   487  C CB  . LEU   A 1 69  ? -14.36733 -6.00515  -25.55031 1.000 24.79603 ? 76  LEU   A CB  1 
ATOM   488  C CG  . LEU   A 1 69  ? -14.29512 -5.36544  -26.95295 1.000 29.37536 ? 76  LEU   A CG  1 
ATOM   489  C CD1 . LEU   A 1 69  ? -13.79264 -3.92795  -26.85105 1.000 34.22538 ? 76  LEU   A CD1 1 
ATOM   490  C CD2 . LEU   A 1 69  ? -13.38481 -6.15437  -27.87736 1.000 28.89190 ? 76  LEU   A CD2 1 
ATOM   491  N N   . HIS   A 1 70  ? -14.08947 -9.16168  -23.80979 1.000 23.47652 ? 77  HIS   A N   1 
ATOM   492  C CA  . HIS   A 1 70  ? -14.25571 -9.81090  -22.50612 1.000 22.32432 ? 77  HIS   A CA  1 
ATOM   493  C C   . HIS   A 1 70  ? -13.06944 -10.70499 -22.19250 1.000 24.21551 ? 77  HIS   A C   1 
ATOM   494  O O   . HIS   A 1 70  ? -12.19873 -10.93841 -23.03484 1.000 21.71725 ? 77  HIS   A O   1 
ATOM   495  C CB  . HIS   A 1 70  ? -15.54262 -10.64667 -22.47024 1.000 25.14768 ? 77  HIS   A CB  1 
ATOM   496  C CG  . HIS   A 1 70  ? -15.55258 -11.76596 -23.47053 1.000 27.03547 ? 77  HIS   A CG  1 
ATOM   497  N ND1 . HIS   A 1 70  ? -16.50754 -11.87507 -24.45765 1.000 31.93895 ? 77  HIS   A ND1 1 
ATOM   498  C CD2 . HIS   A 1 70  ? -14.74385 -12.84633 -23.60890 1.000 28.21522 ? 77  HIS   A CD2 1 
ATOM   499  C CE1 . HIS   A 1 70  ? -16.27214 -12.95753 -25.17813 1.000 29.79367 ? 77  HIS   A CE1 1 
ATOM   500  N NE2 . HIS   A 1 70  ? -15.20622 -13.56504 -24.68634 1.000 28.64142 ? 77  HIS   A NE2 1 
ATOM   501  N N   . ILE   A 1 71  ? -13.07511 -11.22066 -20.95539 1.000 20.62951 ? 78  ILE   A N   1 
ATOM   502  C CA  . ILE   A 1 71  ? -12.04427 -12.10400 -20.41424 1.000 20.81728 ? 78  ILE   A CA  1 
ATOM   503  C C   . ILE   A 1 71  ? -12.74490 -13.29109 -19.76816 1.000 22.66727 ? 78  ILE   A C   1 
ATOM   504  O O   . ILE   A 1 71  ? -13.65257 -13.10317 -18.94755 1.000 21.94531 ? 78  ILE   A O   1 
ATOM   505  C CB  . ILE   A 1 71  ? -11.17237 -11.39136 -19.35702 1.000 20.65739 ? 78  ILE   A CB  1 
ATOM   506  C CG1 . ILE   A 1 71  ? -10.53728 -10.13484 -19.94892 1.000 20.20944 ? 78  ILE   A CG1 1 
ATOM   507  C CG2 . ILE   A 1 71  ? -10.14352 -12.39064 -18.77499 1.000 20.83912 ? 78  ILE   A CG2 1 
ATOM   508  C CD1 . ILE   A 1 71  ? -9.80989  -9.23895  -18.90762 1.000 22.43592 ? 78  ILE   A CD1 1 
ATOM   509  N N   . ASN   A 1 72  ? -12.33671 -14.51128 -20.13761 1.000 21.28634 ? 79  ASN   A N   1 
ATOM   510  C CA  . ASN   A 1 72  ? -12.88847 -15.72306 -19.53494 1.000 18.82658 ? 79  ASN   A CA  1 
ATOM   511  C C   . ASN   A 1 72  ? -11.77734 -16.47294 -18.81375 1.000 21.74193 ? 79  ASN   A C   1 
ATOM   512  O O   . ASN   A 1 72  ? -10.66109 -16.57560 -19.32560 1.000 22.85804 ? 79  ASN   A O   1 
ATOM   513  C CB  . ASN   A 1 72  ? -13.53406 -16.64340 -20.58963 1.000 22.70218 ? 79  ASN   A CB  1 
ATOM   514  C CG  . ASN   A 1 72  ? -14.73513 -16.02442 -21.25902 1.000 25.99330 ? 79  ASN   A CG  1 
ATOM   515  O OD1 . ASN   A 1 72  ? -15.42804 -15.19056 -20.67293 1.000 25.39582 ? 79  ASN   A OD1 1 
ATOM   516  N ND2 . ASN   A 1 72  ? -15.01768 -16.45839 -22.48799 1.000 27.24437 ? 79  ASN   A ND2 1 
ATOM   517  N N   . LEU   A 1 73  ? -12.09539 -17.03437 -17.64286 1.000 21.38845 ? 80  LEU   A N   1 
ATOM   518  C CA  . LEU   A 1 73  ? -11.15782 -17.85733 -16.87178 1.000 18.77841 ? 80  LEU   A CA  1 
ATOM   519  C C   . LEU   A 1 73  ? -11.73052 -19.26345 -16.85451 1.000 22.92075 ? 80  LEU   A C   1 
ATOM   520  O O   . LEU   A 1 73  ? -12.84128 -19.45866 -16.35768 1.000 22.13745 ? 80  LEU   A O   1 
ATOM   521  C CB  . LEU   A 1 73  ? -10.99705 -17.34024 -15.43305 1.000 20.29500 ? 80  LEU   A CB  1 
ATOM   522  C CG  . LEU   A 1 73  ? -10.62582 -15.86068 -15.34149 1.000 19.13371 ? 80  LEU   A CG  1 
ATOM   523  C CD1 . LEU   A 1 73  ? -10.52469 -15.44373 -13.87251 1.000 21.74361 ? 80  LEU   A CD1 1 
ATOM   524  C CD2 . LEU   A 1 73  ? -9.30239  -15.55147 -16.07257 1.000 21.72848 ? 80  LEU   A CD2 1 
ATOM   525  N N   . ILE   A 1 74  ? -10.99484 -20.22869 -17.40111 1.000 21.30976 ? 81  ILE   A N   1 
ATOM   526  C CA  . ILE   A 1 74  ? -11.49894 -21.58089 -17.61644 1.000 22.08525 ? 81  ILE   A CA  1 
ATOM   527  C C   . ILE   A 1 74  ? -10.58430 -22.58343 -16.92026 1.000 23.40800 ? 81  ILE   A C   1 
ATOM   528  O O   . ILE   A 1 74  ? -9.56665  -23.00480 -17.48090 1.000 24.19215 ? 81  ILE   A O   1 
ATOM   529  C CB  . ILE   A 1 74  ? -11.63766 -21.91013 -19.11402 1.000 21.20402 ? 81  ILE   A CB  1 
ATOM   530  C CG1 . ILE   A 1 74  ? -12.36193 -20.76730 -19.82512 1.000 24.20729 ? 81  ILE   A CG1 1 
ATOM   531  C CG2 . ILE   A 1 74  ? -12.32743 -23.25046 -19.29120 1.000 23.24274 ? 81  ILE   A CG2 1 
ATOM   532  C CD1 . ILE   A 1 74  ? -12.46979 -20.91232 -21.35868 1.000 24.81808 ? 81  ILE   A CD1 1 
ATOM   533  N N   . PRO   A 1 75  ? -10.95544 -23.04435 -15.73024 1.000 25.33632 ? 82  PRO   A N   1 
ATOM   534  C CA  . PRO   A 1 75  ? -10.20612 -24.12603 -15.07612 1.000 22.81272 ? 82  PRO   A CA  1 
ATOM   535  C C   . PRO   A 1 75  ? -10.65313 -25.47694 -15.59759 1.000 27.77646 ? 82  PRO   A C   1 
ATOM   536  O O   . PRO   A 1 75  ? -11.83547 -25.68819 -15.87906 1.000 27.47494 ? 82  PRO   A O   1 
ATOM   537  C CB  . PRO   A 1 75  ? -10.56847 -23.95437 -13.59433 1.000 26.96856 ? 82  PRO   A CB  1 
ATOM   538  C CG  . PRO   A 1 75  ? -11.97622 -23.38771 -13.62802 1.000 28.56776 ? 82  PRO   A CG  1 
ATOM   539  C CD  . PRO   A 1 75  ? -12.11892 -22.60818 -14.93061 1.000 25.00381 ? 82  PRO   A CD  1 
ATOM   540  N N   . ASN   A 1 76  ? -9.69212  -26.39779 -15.74810 1.000 26.10469 ? 83  ASN   A N   1 
ATOM   541  C CA  . ASN   A 1 76  ? -10.00543 -27.77252 -16.14530 1.000 27.37815 ? 83  ASN   A CA  1 
ATOM   542  C C   . ASN   A 1 76  ? -9.19736  -28.71488 -15.25832 1.000 28.75768 ? 83  ASN   A C   1 
ATOM   543  O O   . ASN   A 1 76  ? -7.99047  -28.87186 -15.46002 1.000 29.73543 ? 83  ASN   A O   1 
ATOM   544  C CB  . ASN   A 1 76  ? -9.69616  -28.02297 -17.61656 1.000 26.71015 ? 83  ASN   A CB  1 
ATOM   545  C CG  . ASN   A 1 76  ? -10.21370 -29.36800 -18.09068 1.000 33.89989 ? 83  ASN   A CG  1 
ATOM   546  O OD1 . ASN   A 1 76  ? -9.91904  -30.39764 -17.49253 1.000 36.17553 ? 83  ASN   A OD1 1 
ATOM   547  N ND2 . ASN   A 1 76  ? -10.99339 -29.36376 -19.16743 1.000 41.76883 ? 83  ASN   A ND2 1 
ATOM   548  N N   . LYS   A 1 77  ? -9.86400  -29.36253 -14.30347 1.000 31.42154 ? 84  LYS   A N   1 
ATOM   549  C CA  . LYS   A 1 77  ? -9.13956  -30.21663 -13.35824 1.000 31.47657 ? 84  LYS   A CA  1 
ATOM   550  C C   . LYS   A 1 77  ? -8.66638  -31.50823 -13.99996 1.000 36.13821 ? 84  LYS   A C   1 
ATOM   551  O O   . LYS   A 1 77  ? -7.67654  -32.08336 -13.54223 1.000 35.89603 ? 84  LYS   A O   1 
ATOM   552  C CB  . LYS   A 1 77  ? -9.99668  -30.55751 -12.13884 1.000 34.60063 ? 84  LYS   A CB  1 
ATOM   553  C CG  . LYS   A 1 77  ? -10.27737 -29.38477 -11.21263 1.000 33.91409 ? 84  LYS   A CG  1 
ATOM   554  C CD  . LYS   A 1 77  ? -10.98600 -29.85391 -9.92728  1.000 39.87884 ? 84  LYS   A CD  1 
ATOM   555  C CE  . LYS   A 1 77  ? -11.21122 -28.71947 -8.94050  1.000 40.32819 ? 84  LYS   A CE  1 
ATOM   556  N NZ  . LYS   A 1 77  ? -11.98072 -27.63904 -9.59670  1.000 44.79250 ? 84  LYS   A NZ  1 
ATOM   557  N N   . GLN   A 1 78  ? -9.36569  -32.00191 -15.02748 1.000 35.68977 ? 85  GLN   A N   1 
ATOM   558  C CA  . GLN   A 1 78  ? -8.92839  -33.24064 -15.67088 1.000 42.12688 ? 85  GLN   A CA  1 
ATOM   559  C C   . GLN   A 1 78  ? -7.61619  -33.04384 -16.42315 1.000 39.22412 ? 85  GLN   A C   1 
ATOM   560  O O   . GLN   A 1 78  ? -6.73320  -33.91084 -16.37855 1.000 40.95023 ? 85  GLN   A O   1 
ATOM   561  C CB  . GLN   A 1 78  ? -10.01906 -33.76994 -16.60444 1.000 41.71973 ? 85  GLN   A CB  1 
ATOM   562  C CG  . GLN   A 1 78  ? -11.35291 -34.18018 -15.93533 1.000 51.00990 ? 85  GLN   A CG  1 
ATOM   563  C CD  . GLN   A 1 78  ? -11.23814 -35.27633 -14.85269 1.000 66.96882 ? 85  GLN   A CD  1 
ATOM   564  O OE1 . GLN   A 1 78  ? -10.20274 -35.44444 -14.19622 1.000 70.87959 ? 85  GLN   A OE1 1 
ATOM   565  N NE2 . GLN   A 1 78  ? -12.31834 -36.04959 -14.68998 1.000 71.33152 ? 85  GLN   A NE2 1 
ATOM   566  N N   . ASP   A 1 79  ? -7.47203  -31.91028 -17.10606 1.000 32.14554 ? 86  ASP   A N   1 
ATOM   567  C CA  . ASP   A 1 79  ? -6.28808  -31.55963 -17.87696 1.000 33.35121 ? 86  ASP   A CA  1 
ATOM   568  C C   . ASP   A 1 79  ? -5.23286  -30.87047 -17.02176 1.000 31.13361 ? 86  ASP   A C   1 
ATOM   569  O O   . ASP   A 1 79  ? -4.10569  -30.66990 -17.49447 1.000 33.03594 ? 86  ASP   A O   1 
ATOM   570  C CB  . ASP   A 1 79  ? -6.68497  -30.61714 -19.02877 1.000 34.15311 ? 86  ASP   A CB  1 
ATOM   571  C CG  . ASP   A 1 79  ? -7.54250  -31.30512 -20.08668 1.000 45.57641 ? 86  ASP   A CG  1 
ATOM   572  O OD1 . ASP   A 1 79  ? -7.82895  -32.52056 -19.95301 1.000 48.91961 ? 86  ASP   A OD1 1 
ATOM   573  O OD2 . ASP   A 1 79  ? -7.99188  -30.60438 -21.01799 1.000 46.09246 ? 86  ASP   A OD2 1 
ATOM   574  N N   . ARG   A 1 80  ? -5.58611  -30.49754 -15.78906 1.000 29.50949 ? 87  ARG   A N   1 
ATOM   575  C CA  . ARG   A 1 80  ? -4.74284  -29.67010 -14.91044 1.000 25.77349 ? 87  ARG   A CA  1 
ATOM   576  C C   . ARG   A 1 80  ? -4.27470  -28.40082 -15.61837 1.000 25.91357 ? 87  ARG   A C   1 
ATOM   577  O O   . ARG   A 1 80  ? -3.08606  -28.04690 -15.61167 1.000 27.17273 ? 87  ARG   A O   1 
ATOM   578  C CB  . ARG   A 1 80  ? -3.56030  -30.47275 -14.34997 1.000 30.96149 ? 87  ARG   A CB  1 
ATOM   579  C CG  . ARG   A 1 80  ? -3.22837  -30.01291 -12.94689 1.000 31.86246 ? 87  ARG   A CG  1 
ATOM   580  C CD  . ARG   A 1 80  ? -2.29569  -30.90441 -12.17811 1.000 38.19888 ? 87  ARG   A CD  1 
ATOM   581  N NE  . ARG   A 1 80  ? -0.92323  -30.77053 -12.61452 1.000 42.23857 ? 87  ARG   A NE  1 
ATOM   582  C CZ  . ARG   A 1 80  ? -0.06354  -31.77301 -12.70598 1.000 45.47358 ? 87  ARG   A CZ  1 
ATOM   583  N NH1 . ARG   A 1 80  ? -0.39452  -33.00214 -12.34218 1.000 47.88759 ? 87  ARG   A NH1 1 
ATOM   584  N NH2 . ARG   A 1 80  ? 1.17359   -31.52541 -13.12761 1.000 42.88394 ? 87  ARG   A NH2 1 
ATOM   585  N N   . THR   A 1 81  ? -5.23073  -27.68111 -16.21166 1.000 25.25329 ? 88  THR   A N   1 
ATOM   586  C CA  . THR   A 1 81  ? -4.93743  -26.43335 -16.90599 1.000 23.81505 ? 88  THR   A CA  1 
ATOM   587  C C   . THR   A 1 81  ? -5.84854  -25.30718 -16.43764 1.000 25.16952 ? 88  THR   A C   1 
ATOM   588  O O   . THR   A 1 81  ? -7.01490  -25.52653 -16.10374 1.000 25.21392 ? 88  THR   A O   1 
ATOM   589  C CB  . THR   A 1 81  ? -5.07515  -26.55114 -18.44493 1.000 27.37150 ? 88  THR   A CB  1 
ATOM   590  O OG1 . THR   A 1 81  ? -6.41927  -26.94668 -18.77639 1.000 28.79838 ? 88  THR   A OG1 1 
ATOM   591  C CG2 . THR   A 1 81  ? -4.07667  -27.54844 -19.02757 1.000 27.37092 ? 88  THR   A CG2 1 
ATOM   592  N N   . LEU   A 1 82  ? -5.29458  -24.10286 -16.40748 1.000 20.52169 ? 89  LEU   A N   1 
ATOM   593  C CA  . LEU   A 1 82  ? -6.07401  -22.88110 -16.23251 1.000 21.84727 ? 89  LEU   A CA  1 
ATOM   594  C C   . LEU   A 1 82  ? -5.87933  -22.05418 -17.49647 1.000 24.26322 ? 89  LEU   A C   1 
ATOM   595  O O   . LEU   A 1 82  ? -4.74924  -21.73763 -17.86089 1.000 24.10002 ? 89  LEU   A O   1 
ATOM   596  C CB  . LEU   A 1 82  ? -5.62089  -22.09460 -14.99620 1.000 23.84192 ? 89  LEU   A CB  1 
ATOM   597  C CG  . LEU   A 1 82  ? -6.37331  -20.76933 -14.77564 1.000 22.24094 ? 89  LEU   A CG  1 
ATOM   598  C CD1 . LEU   A 1 82  ? -7.88051  -21.01287 -14.59044 1.000 24.05213 ? 89  LEU   A CD1 1 
ATOM   599  C CD2 . LEU   A 1 82  ? -5.80708  -20.08235 -13.53698 1.000 23.15884 ? 89  LEU   A CD2 1 
ATOM   600  N N   . THR   A 1 83  ? -6.96523  -21.69875 -18.15941 1.000 21.98957 ? 90  THR   A N   1 
ATOM   601  C CA  . THR   A 1 83  ? -6.87439  -20.96216 -19.41651 1.000 20.49100 ? 90  THR   A CA  1 
ATOM   602  C C   . THR   A 1 83  ? -7.47248  -19.57751 -19.23080 1.000 24.12024 ? 90  THR   A C   1 
ATOM   603  O O   . THR   A 1 83  ? -8.55654  -19.44441 -18.64521 1.000 24.13231 ? 90  THR   A O   1 
ATOM   604  C CB  . THR   A 1 83  ? -7.60524  -21.70502 -20.53938 1.000 21.71181 ? 90  THR   A CB  1 
ATOM   605  O OG1 . THR   A 1 83  ? -7.02551  -23.00025 -20.73435 1.000 25.83883 ? 90  THR   A OG1 1 
ATOM   606  C CG2 . THR   A 1 83  ? -7.54809  -20.90445 -21.82025 1.000 26.66893 ? 90  THR   A CG2 1 
ATOM   607  N N   . ILE   A 1 84  ? -6.74683  -18.54550 -19.68290 1.000 22.71623 ? 91  ILE   A N   1 
ATOM   608  C CA  . ILE   A 1 84  ? -7.21039  -17.15798 -19.64864 1.000 20.40636 ? 91  ILE   A CA  1 
ATOM   609  C C   . ILE   A 1 84  ? -7.43717  -16.75645 -21.10441 1.000 25.18362 ? 91  ILE   A C   1 
ATOM   610  O O   . ILE   A 1 84  ? -6.48435  -16.72088 -21.89182 1.000 22.10812 ? 91  ILE   A O   1 
ATOM   611  C CB  . ILE   A 1 84  ? -6.20388  -16.20979 -18.95651 1.000 22.66028 ? 91  ILE   A CB  1 
ATOM   612  C CG1 . ILE   A 1 84  ? -5.93989  -16.57318 -17.46739 1.000 26.62182 ? 91  ILE   A CG1 1 
ATOM   613  C CG2 . ILE   A 1 84  ? -6.67066  -14.75981 -19.07043 1.000 23.57457 ? 91  ILE   A CG2 1 
ATOM   614  C CD1 . ILE   A 1 84  ? -4.86074  -17.61703 -17.22150 1.000 32.92000 ? 91  ILE   A CD1 1 
ATOM   615  N N   . VAL   A 1 85  ? -8.69372  -16.49644 -21.48029 1.000 20.14061 ? 92  VAL   A N   1 
ATOM   616  C CA  . VAL   A 1 85  ? -9.07371  -16.12359 -22.84179 1.000 21.29240 ? 92  VAL   A CA  1 
ATOM   617  C C   . VAL   A 1 85  ? -9.48605  -14.66491 -22.86753 1.000 23.72605 ? 92  VAL   A C   1 
ATOM   618  O O   . VAL   A 1 85  ? -10.30041 -14.23095 -22.03844 1.000 25.20920 ? 92  VAL   A O   1 
ATOM   619  C CB  . VAL   A 1 85  ? -10.24096 -16.97864 -23.38053 1.000 23.14438 ? 92  VAL   A CB  1 
ATOM   620  C CG1 . VAL   A 1 85  ? -10.50397 -16.65847 -24.85223 1.000 27.77794 ? 92  VAL   A CG1 1 
ATOM   621  C CG2 . VAL   A 1 85  ? -9.96438  -18.47005 -23.18112 1.000 27.61671 ? 92  VAL   A CG2 1 
ATOM   622  N N   . ASP   A 1 86  ? -8.99178  -13.91932 -23.86595 1.000 23.38389 ? 93  ASP   A N   1 
ATOM   623  C CA  . ASP   A 1 86  ? -9.49986  -12.56934 -24.10838 1.000 21.94668 ? 93  ASP   A CA  1 
ATOM   624  C C   . ASP   A 1 86  ? -9.75419  -12.37589 -25.60157 1.000 25.11457 ? 93  ASP   A C   1 
ATOM   625  O O   . ASP   A 1 86  ? -9.20129  -13.08828 -26.44905 1.000 23.01852 ? 93  ASP   A O   1 
ATOM   626  C CB  . ASP   A 1 86  ? -8.52309  -11.50408 -23.55864 1.000 22.84923 ? 93  ASP   A CB  1 
ATOM   627  C CG  . ASP   A 1 86  ? -7.21687  -11.39231 -24.36624 1.000 25.87037 ? 93  ASP   A CG  1 
ATOM   628  O OD1 . ASP   A 1 86  ? -7.23129  -11.12362 -25.60193 1.000 26.90710 ? 93  ASP   A OD1 1 
ATOM   629  O OD2 . ASP   A 1 86  ? -6.14769  -11.63590 -23.75405 1.000 26.35018 ? 93  ASP   A OD2 1 
ATOM   630  N N   . THR   A 1 87  ? -10.64367 -11.43511 -25.91874 1.000 23.48077 ? 94  THR   A N   1 
ATOM   631  C CA  . THR   A 1 87  ? -10.93238 -11.08614 -27.30468 1.000 21.11890 ? 94  THR   A CA  1 
ATOM   632  C C   . THR   A 1 87  ? -10.26796 -9.76683  -27.68396 1.000 23.97142 ? 94  THR   A C   1 
ATOM   633  O O   . THR   A 1 87  ? -10.83289 -8.92550  -28.39882 1.000 23.12410 ? 94  THR   A O   1 
ATOM   634  C CB  . THR   A 1 87  ? -12.43890 -11.04090 -27.53418 1.000 23.44373 ? 94  THR   A CB  1 
ATOM   635  O OG1 . THR   A 1 87  ? -13.03151 -10.23371 -26.50953 1.000 25.02623 ? 94  THR   A OG1 1 
ATOM   636  C CG2 . THR   A 1 87  ? -13.01427 -12.45817 -27.40724 1.000 24.58529 ? 94  THR   A CG2 1 
ATOM   637  N N   . GLY   A 1 88  ? -9.02809  -9.58337  -27.23873 1.000 22.09166 ? 95  GLY   A N   1 
ATOM   638  C CA  . GLY   A 1 88  ? -8.28112  -8.38200  -27.55468 1.000 25.09801 ? 95  GLY   A CA  1 
ATOM   639  C C   . GLY   A 1 88  ? -7.68223  -8.40424  -28.95123 1.000 22.25535 ? 95  GLY   A C   1 
ATOM   640  O O   . GLY   A 1 88  ? -8.10484  -9.15386  -29.83691 1.000 23.47520 ? 95  GLY   A O   1 
ATOM   641  N N   . ILE   A 1 89  ? -6.65207  -7.56884  -29.14253 1.000 21.02356 ? 96  ILE   A N   1 
ATOM   642  C CA  . ILE   A 1 89  ? -6.13227  -7.35394  -30.49578 1.000 23.18629 ? 96  ILE   A CA  1 
ATOM   643  C C   . ILE   A 1 89  ? -5.37130  -8.57055  -31.01892 1.000 23.99178 ? 96  ILE   A C   1 
ATOM   644  O O   . ILE   A 1 89  ? -5.18674  -8.70936  -32.23571 1.000 25.47059 ? 96  ILE   A O   1 
ATOM   645  C CB  . ILE   A 1 89  ? -5.26418  -6.07773  -30.52234 1.000 23.55508 ? 96  ILE   A CB  1 
ATOM   646  C CG1 . ILE   A 1 89  ? -5.01764  -5.62761  -31.98614 1.000 27.42947 ? 96  ILE   A CG1 1 
ATOM   647  C CG2 . ILE   A 1 89  ? -3.96581  -6.32655  -29.72322 1.000 22.86211 ? 96  ILE   A CG2 1 
ATOM   648  C CD1 . ILE   A 1 89  ? -4.56475  -4.18184  -32.13844 1.000 30.70078 ? 96  ILE   A CD1 1 
ATOM   649  N N   . GLY   A 1 90  ? -4.95110  -9.47656  -30.13556 1.000 22.51663 ? 97  GLY   A N   1 
ATOM   650  C CA  . GLY   A 1 90  ? -4.20983  -10.64650 -30.58231 1.000 24.32144 ? 97  GLY   A CA  1 
ATOM   651  C C   . GLY   A 1 90  ? -2.77311  -10.29428 -30.96682 1.000 25.90973 ? 97  GLY   A C   1 
ATOM   652  O O   . GLY   A 1 90  ? -2.29130  -9.17786  -30.77080 1.000 26.18682 ? 97  GLY   A O   1 
ATOM   653  N N   . MET   A 1 91  ? -2.06461  -11.31127 -31.45037 1.000 24.15666 ? 98  MET   A N   1 
ATOM   654  C CA  . MET   A 1 91  ? -0.66674  -11.14821 -31.85250 1.000 23.85568 ? 98  MET   A CA  1 
ATOM   655  C C   . MET   A 1 91  ? -0.40747  -11.78398 -33.20621 1.000 24.51877 ? 98  MET   A C   1 
ATOM   656  O O   . MET   A 1 91  ? -0.91017  -12.87292 -33.48439 1.000 25.71165 ? 98  MET   A O   1 
ATOM   657  C CB  . MET   A 1 91  ? 0.31416   -11.78155 -30.83734 1.000 24.14390 ? 98  MET   A CB  1 
ATOM   658  C CG  . MET   A 1 91  ? 0.43508   -11.01555 -29.51699 1.000 26.10892 ? 98  MET   A CG  1 
ATOM   659  S SD  . MET   A 1 91  ? 1.31576   -11.93593 -28.21985 1.000 27.23783 ? 98  MET   A SD  1 
ATOM   660  C CE  . MET   A 1 91  ? 0.17685   -13.26917 -27.78980 1.000 26.91792 ? 98  MET   A CE  1 
ATOM   661  N N   . THR   A 1 92  ? 0.42574   -11.13225 -34.03347 1.000 24.94810 ? 99  THR   A N   1 
ATOM   662  C CA  . THR   A 1 92  ? 0.92930   -11.74263 -35.25597 1.000 27.15641 ? 99  THR   A CA  1 
ATOM   663  C C   . THR   A 1 92  ? 2.05255   -12.72662 -34.94170 1.000 27.79291 ? 99  THR   A C   1 
ATOM   664  O O   . THR   A 1 92  ? 2.57536   -12.77779 -33.82714 1.000 27.63238 ? 99  THR   A O   1 
ATOM   665  C CB  . THR   A 1 92  ? 1.47901   -10.69170 -36.21014 1.000 29.82233 ? 99  THR   A CB  1 
ATOM   666  O OG1 . THR   A 1 92  ? 2.62143   -10.10399 -35.57520 1.000 31.75010 ? 99  THR   A OG1 1 
ATOM   667  C CG2 . THR   A 1 92  ? 0.43165   -9.58204  -36.46892 1.000 30.67252 ? 99  THR   A CG2 1 
ATOM   668  N N   . LYS   A 1 93  ? 2.41960   -13.52077 -35.95181 1.000 23.93917 ? 100 LYS   A N   1 
ATOM   669  C CA  . LYS   A 1 93  ? 3.53039   -14.45465 -35.76781 1.000 25.63738 ? 100 LYS   A CA  1 
ATOM   670  C C   . LYS   A 1 93  ? 4.79625   -13.70685 -35.38991 1.000 25.94540 ? 100 LYS   A C   1 
ATOM   671  O O   . LYS   A 1 93  ? 5.53952   -14.14145 -34.50231 1.000 25.66016 ? 100 LYS   A O   1 
ATOM   672  C CB  . LYS   A 1 93  ? 3.75637   -15.27793 -37.03773 1.000 28.79470 ? 100 LYS   A CB  1 
ATOM   673  C CG  . LYS   A 1 93  ? 4.91005   -16.28002 -36.91870 1.000 28.55452 ? 100 LYS   A CG  1 
ATOM   674  C CD  . LYS   A 1 93  ? 5.16393   -17.03490 -38.25231 1.000 30.73699 ? 100 LYS   A CD  1 
ATOM   675  C CE  . LYS   A 1 93  ? 6.10566   -18.21475 -38.01841 1.000 32.79012 ? 100 LYS   A CE  1 
ATOM   676  N NZ  . LYS   A 1 93  ? 6.80842   -18.59858 -39.26959 1.000 38.19253 ? 100 LYS   A NZ  1 
ATOM   677  N N   . ALA   A 1 94  ? 5.04310   -12.56785 -36.04833 1.000 25.96506 ? 101 ALA   A N   1 
ATOM   678  C CA  . ALA   A 1 94  ? 6.22286   -11.76464 -35.73870 1.000 29.21198 ? 101 ALA   A CA  1 
ATOM   679  C C   . ALA   A 1 94  ? 6.18154   -11.27161 -34.29814 1.000 27.49613 ? 101 ALA   A C   1 
ATOM   680  O O   . ALA   A 1 94  ? 7.20748   -11.27452 -33.60658 1.000 29.32916 ? 101 ALA   A O   1 
ATOM   681  C CB  . ALA   A 1 94  ? 6.32824   -10.58996 -36.70475 1.000 30.71641 ? 101 ALA   A CB  1 
ATOM   682  N N   . ASP   A 1 95  ? 4.99339   -10.86870 -33.82397 1.000 27.84616 ? 102 ASP   A N   1 
ATOM   683  C CA  . ASP   A 1 95  ? 4.81640   -10.49454 -32.41495 1.000 28.02608 ? 102 ASP   A CA  1 
ATOM   684  C C   . ASP   A 1 95  ? 5.16422   -11.65323 -31.48538 1.000 27.41937 ? 102 ASP   A C   1 
ATOM   685  O O   . ASP   A 1 95  ? 5.85271   -11.47465 -30.47621 1.000 26.22983 ? 102 ASP   A O   1 
ATOM   686  C CB  . ASP   A 1 95  ? 3.35808   -10.06761 -32.15559 1.000 28.46754 ? 102 ASP   A CB  1 
ATOM   687  C CG  . ASP   A 1 95  ? 3.02099   -8.70119  -32.69766 1.000 35.98364 ? 102 ASP   A CG  1 
ATOM   688  O OD1 . ASP   A 1 95  ? 3.94291   -7.87767  -32.92371 1.000 37.67793 ? 102 ASP   A OD1 1 
ATOM   689  O OD2 . ASP   A 1 95  ? 1.80392   -8.45078  -32.92441 1.000 34.45426 ? 102 ASP   A OD2 1 
ATOM   690  N N   . LEU   A 1 96  ? 4.64871   -12.85065 -31.77774 1.000 24.95485 ? 103 LEU   A N   1 
ATOM   691  C CA  . LEU   A 1 96  ? 4.92964   -13.99664 -30.92013 1.000 25.01549 ? 103 LEU   A CA  1 
ATOM   692  C C   . LEU   A 1 96  ? 6.42226   -14.21861 -30.78030 1.000 28.36893 ? 103 LEU   A C   1 
ATOM   693  O O   . LEU   A 1 96  ? 6.92386   -14.45485 -29.67577 1.000 25.86001 ? 103 LEU   A O   1 
ATOM   694  C CB  . LEU   A 1 96  ? 4.30009   -15.26473 -31.49552 1.000 26.64633 ? 103 LEU   A CB  1 
ATOM   695  C CG  . LEU   A 1 96  ? 2.82225   -15.44428 -31.25121 1.000 27.34937 ? 103 LEU   A CG  1 
ATOM   696  C CD1 . LEU   A 1 96  ? 2.37171   -16.73329 -31.94973 1.000 25.47515 ? 103 LEU   A CD1 1 
ATOM   697  C CD2 . LEU   A 1 96  ? 2.48570   -15.49549 -29.72812 1.000 25.02424 ? 103 LEU   A CD2 1 
ATOM   698  N N   . ILE   A 1 97  ? 7.14829   -14.16397 -31.90121 1.000 26.69824 ? 104 ILE   A N   1 
ATOM   699  C CA  . ILE   A 1 97  ? 8.57990   -14.46359 -31.87035 1.000 27.15936 ? 104 ILE   A CA  1 
ATOM   700  C C   . ILE   A 1 97  ? 9.33102   -13.37673 -31.10200 1.000 27.64951 ? 104 ILE   A C   1 
ATOM   701  O O   . ILE   A 1 97  ? 10.26193  -13.66329 -30.33371 1.000 29.13691 ? 104 ILE   A O   1 
ATOM   702  C CB  . ILE   A 1 97  ? 9.11209   -14.62703 -33.30325 1.000 29.91788 ? 104 ILE   A CB  1 
ATOM   703  C CG1 . ILE   A 1 97  ? 8.51046   -15.89124 -33.94339 1.000 26.13500 ? 104 ILE   A CG1 1 
ATOM   704  C CG2 . ILE   A 1 97  ? 10.65189  -14.69768 -33.28039 1.000 29.14055 ? 104 ILE   A CG2 1 
ATOM   705  C CD1 . ILE   A 1 97  ? 8.69918   -15.97850 -35.49648 1.000 31.59779 ? 104 ILE   A CD1 1 
ATOM   706  N N   . ASN   A 1 98  ? 8.89720   -12.13285 -31.25520 1.000 25.11695 ? 105 ASN   A N   1 
ATOM   707  C CA  . ASN   A 1 98  ? 9.47318   -10.96344 -30.60910 1.000 29.81695 ? 105 ASN   A CA  1 
ATOM   708  C C   . ASN   A 1 98  ? 8.93620   -10.85310 -29.18058 1.000 27.06910 ? 105 ASN   A C   1 
ATOM   709  O O   . ASN   A 1 98  ? 8.35717   -9.83059  -28.79652 1.000 27.14834 ? 105 ASN   A O   1 
ATOM   710  C CB  . ASN   A 1 98  ? 9.15461   -9.72352  -31.46467 1.000 30.94454 ? 105 ASN   A CB  1 
ATOM   711  C CG  . ASN   A 1 98  ? 10.03560  -8.54349  -31.14667 1.000 42.40709 ? 105 ASN   A CG  1 
ATOM   712  O OD1 . ASN   A 1 98  ? 10.99055  -8.65231  -30.35949 1.000 43.22750 ? 105 ASN   A OD1 1 
ATOM   713  N ND2 . ASN   A 1 98  ? 9.75662   -7.40485  -31.79515 1.000 44.99574 ? 105 ASN   A ND2 1 
ATOM   714  N N   . ASN   A 1 99  ? 9.09646   -11.93230 -28.41103 1.000 26.71545 ? 106 ASN   A N   1 
ATOM   715  C CA  . ASN   A 1 99  ? 8.77186   -11.97758 -26.98555 1.000 24.75265 ? 106 ASN   A CA  1 
ATOM   716  C C   . ASN   A 1 99  ? 7.31683   -11.59508 -26.71145 1.000 28.47511 ? 106 ASN   A C   1 
ATOM   717  O O   . ASN   A 1 99  ? 7.01825   -10.81346 -25.81052 1.000 25.07140 ? 106 ASN   A O   1 
ATOM   718  C CB  . ASN   A 1 99  ? 9.74646   -11.10437 -26.18420 1.000 28.38176 ? 106 ASN   A CB  1 
ATOM   719  C CG  . ASN   A 1 99  ? 11.19762  -11.58151 -26.32549 1.000 24.54810 ? 106 ASN   A CG  1 
ATOM   720  O OD1 . ASN   A 1 99  ? 11.50647  -12.75449 -26.07599 1.000 25.83959 ? 106 ASN   A OD1 1 
ATOM   721  N ND2 . ASN   A 1 99  ? 12.08102  -10.68030 -26.75834 1.000 27.42148 ? 106 ASN   A ND2 1 
ATOM   722  N N   . LEU   A 1 100 ? 6.40740   -12.21753 -27.45935 1.000 25.48320 ? 107 LEU   A N   1 
ATOM   723  C CA  . LEU   A 1 100 ? 4.96088   -12.02127 -27.29182 1.000 27.05911 ? 107 LEU   A CA  1 
ATOM   724  C C   . LEU   A 1 100 ? 4.58434   -10.54217 -27.22465 1.000 29.40831 ? 107 LEU   A C   1 
ATOM   725  O O   . LEU   A 1 100 ? 3.80717   -10.09796 -26.36554 1.000 27.74440 ? 107 LEU   A O   1 
ATOM   726  C CB  . LEU   A 1 100 ? 4.44341   -12.78631 -26.06977 1.000 23.45262 ? 107 LEU   A CB  1 
ATOM   727  C CG  . LEU   A 1 100 ? 4.88180   -14.26100 -26.09286 1.000 26.64907 ? 107 LEU   A CG  1 
ATOM   728  C CD1 . LEU   A 1 100 ? 5.99526   -14.55765 -25.11535 1.000 32.24493 ? 107 LEU   A CD1 1 
ATOM   729  C CD2 . LEU   A 1 100 ? 3.73023   -15.19753 -25.82976 1.000 30.59807 ? 107 LEU   A CD2 1 
ATOM   730  N N   . GLY   A 1 101 ? 5.12717   -9.77093  -28.17279 1.000 23.13015 ? 108 GLY   A N   1 
ATOM   731  C CA  . GLY   A 1 101 ? 4.75217   -8.37463  -28.30057 1.000 28.30919 ? 108 GLY   A CA  1 
ATOM   732  C C   . GLY   A 1 101 ? 5.25381   -7.44603  -27.21378 1.000 28.69569 ? 108 GLY   A C   1 
ATOM   733  O O   . GLY   A 1 101 ? 4.71503   -6.33772  -27.08090 1.000 35.87058 ? 108 GLY   A O   1 
ATOM   734  N N   . THR   A 1 102 ? 6.26084   -7.86132  -26.43586 1.000 28.50603 ? 109 THR   A N   1 
ATOM   735  C CA  . THR   A 1 102 ? 6.82597   -7.08310  -25.33862 1.000 28.83135 ? 109 THR   A CA  1 
ATOM   736  C C   . THR   A 1 102 ? 8.21399   -6.57176  -25.70294 1.000 31.46715 ? 109 THR   A C   1 
ATOM   737  O O   . THR   A 1 102 ? 8.86611   -7.07384  -26.62744 1.000 29.63958 ? 109 THR   A O   1 
ATOM   738  C CB  . THR   A 1 102 ? 6.93027   -7.91368  -24.05018 1.000 28.11206 ? 109 THR   A CB  1 
ATOM   739  O OG1 . THR   A 1 102 ? 7.97588   -8.89673  -24.18997 1.000 29.24963 ? 109 THR   A OG1 1 
ATOM   740  C CG2 . THR   A 1 102 ? 5.62047   -8.62225  -23.73976 1.000 32.19187 ? 109 THR   A CG2 1 
ATOM   741  N N   . ILE   A 1 103 ? 8.67660   -5.59142  -24.92941 1.000 26.41216 ? 110 ILE   A N   1 
ATOM   742  C CA  . ILE   A 1 103 ? 10.06670  -5.13910  -25.00425 1.000 26.69468 ? 110 ILE   A CA  1 
ATOM   743  C C   . ILE   A 1 103 ? 10.84532  -5.85513  -23.89980 1.000 28.32402 ? 110 ILE   A C   1 
ATOM   744  O O   . ILE   A 1 103 ? 11.45086  -5.22935  -23.01053 1.000 29.62902 ? 110 ILE   A O   1 
ATOM   745  C CB  . ILE   A 1 103 ? 10.18002  -3.61085  -24.88151 1.000 32.61272 ? 110 ILE   A CB  1 
ATOM   746  C CG1 . ILE   A 1 103 ? 9.39819   -3.11121  -23.66984 1.000 29.91058 ? 110 ILE   A CG1 1 
ATOM   747  C CG2 . ILE   A 1 103 ? 9.64281   -2.95277  -26.16460 1.000 30.91067 ? 110 ILE   A CG2 1 
ATOM   748  C CD1 . ILE   A 1 103 ? 9.57815   -1.63420  -23.43170 1.000 42.50645 ? 110 ILE   A CD1 1 
ATOM   749  N N   . ALA   A 1 104 ? 10.85018  -7.18517  -23.97116 1.000 26.13977 ? 111 ALA   A N   1 
ATOM   750  C CA  . ALA   A 1 104 ? 11.29161  -7.98554  -22.83961 1.000 26.75808 ? 111 ALA   A CA  1 
ATOM   751  C C   . ALA   A 1 104 ? 12.77262  -7.79787  -22.51974 1.000 25.17173 ? 111 ALA   A C   1 
ATOM   752  O O   . ALA   A 1 104 ? 13.14218  -7.88723  -21.34637 1.000 27.63177 ? 111 ALA   A O   1 
ATOM   753  C CB  . ALA   A 1 104 ? 10.97387  -9.46279  -23.08721 1.000 27.94892 ? 111 ALA   A CB  1 
ATOM   754  N N   . LYS   A 1 105 ? 13.63429  -7.52482  -23.51095 1.000 25.42922 ? 112 LYS   A N   1 
ATOM   755  C CA  . LYS   A 1 105 ? 15.04735  -7.35748  -23.18524 1.000 28.57963 ? 112 LYS   A CA  1 
ATOM   756  C C   . LYS   A 1 105 ? 15.26029  -6.11781  -22.31443 1.000 34.06399 ? 112 LYS   A C   1 
ATOM   757  O O   . LYS   A 1 105 ? 15.85730  -6.19956  -21.23349 1.000 30.11168 ? 112 LYS   A O   1 
ATOM   758  C CB  . LYS   A 1 105 ? 15.90446  -7.28896  -24.45836 1.000 27.76918 ? 112 LYS   A CB  1 
ATOM   759  C CG  . LYS   A 1 105 ? 17.36618  -7.00417  -24.18920 1.000 38.90017 ? 112 LYS   A CG  1 
ATOM   760  C CD  . LYS   A 1 105 ? 18.24389  -7.44174  -25.37388 1.000 38.73449 ? 112 LYS   A CD  1 
ATOM   761  C CE  . LYS   A 1 105 ? 19.68997  -7.02877  -25.15974 1.000 51.72827 ? 112 LYS   A CE  1 
ATOM   762  N NZ  . LYS   A 1 105 ? 20.50863  -7.10071  -26.42118 1.000 55.49877 ? 112 LYS   A NZ  1 
ATOM   763  N N   . SER   A 1 106 ? 14.75877  -4.95703  -22.75270 1.000 29.05108 ? 113 SER   A N   1 
ATOM   764  C CA  . SER   A 1 106 ? 14.95595  -3.76210  -21.93832 1.000 31.63422 ? 113 SER   A CA  1 
ATOM   765  C C   . SER   A 1 106 ? 14.08980  -3.80529  -20.67964 1.000 30.01295 ? 113 SER   A C   1 
ATOM   766  O O   . SER   A 1 106 ? 14.50497  -3.31009  -19.62866 1.000 33.16070 ? 113 SER   A O   1 
ATOM   767  C CB  . SER   A 1 106 ? 14.69582  -2.49870  -22.77258 1.000 38.94827 ? 113 SER   A CB  1 
ATOM   768  O OG  . SER   A 1 106 ? 13.34634  -2.44081  -23.20291 1.000 36.73151 ? 113 SER   A OG  1 
ATOM   769  N N   . GLY   A 1 107 ? 12.90481  -4.41702  -20.75930 1.000 27.57952 ? 114 GLY   A N   1 
ATOM   770  C CA  . GLY   A 1 107 ? 12.07277  -4.57235  -19.57379 1.000 28.07224 ? 114 GLY   A CA  1 
ATOM   771  C C   . GLY   A 1 107 ? 12.73516  -5.41976  -18.50486 1.000 29.80263 ? 114 GLY   A C   1 
ATOM   772  O O   . GLY   A 1 107 ? 12.67252  -5.09503  -17.31605 1.000 28.78980 ? 114 GLY   A O   1 
ATOM   773  N N   . THR   A 1 108 ? 13.37424  -6.52557  -18.91245 1.000 28.90830 ? 115 THR   A N   1 
ATOM   774  C CA  . THR   A 1 108 ? 14.08508  -7.36149  -17.94888 1.000 26.54654 ? 115 THR   A CA  1 
ATOM   775  C C   . THR   A 1 108 ? 15.21875  -6.58611  -17.29317 1.000 31.40727 ? 115 THR   A C   1 
ATOM   776  O O   . THR   A 1 108 ? 15.42673  -6.68865  -16.08208 1.000 27.94617 ? 115 THR   A O   1 
ATOM   777  C CB  . THR   A 1 108 ? 14.62716  -8.62567  -18.63047 1.000 27.31765 ? 115 THR   A CB  1 
ATOM   778  O OG1 . THR   A 1 108 ? 13.52803  -9.41726  -19.10833 1.000 25.51676 ? 115 THR   A OG1 1 
ATOM   779  C CG2 . THR   A 1 108 ? 15.39719  -9.46320  -17.67401 1.000 28.94284 ? 115 THR   A CG2 1 
ATOM   780  N N   . LYS   A 1 109 ? 15.95530  -5.79302  -18.07724 1.000 29.72185 ? 116 LYS   A N   1 
ATOM   781  C CA  . LYS   A 1 109 ? 17.04050  -4.99733  -17.51267 1.000 30.94389 ? 116 LYS   A CA  1 
ATOM   782  C C   . LYS   A 1 109 ? 16.50422  -3.97847  -16.50961 1.000 33.87443 ? 116 LYS   A C   1 
ATOM   783  O O   . LYS   A 1 109 ? 17.07048  -3.80420  -15.41912 1.000 36.29989 ? 116 LYS   A O   1 
ATOM   784  C CB  . LYS   A 1 109 ? 17.80574  -4.32273  -18.66072 1.000 32.18561 ? 116 LYS   A CB  1 
ATOM   785  C CG  . LYS   A 1 109 ? 19.05620  -3.49637  -18.34622 1.000 47.29919 ? 116 LYS   A CG  1 
ATOM   786  C CD  . LYS   A 1 109 ? 19.25953  -2.43746  -19.44307 1.000 48.52892 ? 116 LYS   A CD  1 
ATOM   787  C CE  . LYS   A 1 109 ? 20.37641  -1.45443  -19.12780 1.000 56.05099 ? 116 LYS   A CE  1 
ATOM   788  N NZ  . LYS   A 1 109 ? 21.19810  -1.95082  -17.99369 1.000 58.20624 ? 116 LYS   A NZ  1 
ATOM   789  N N   . ALA   A 1 110 ? 15.42196  -3.27819  -16.86814 1.000 30.61220 ? 117 ALA   A N   1 
ATOM   790  C CA  . ALA   A 1 110 ? 14.84921  -2.29308  -15.94892 1.000 30.43209 ? 117 ALA   A CA  1 
ATOM   791  C C   . ALA   A 1 110 ? 14.30298  -2.95974  -14.68956 1.000 31.82981 ? 117 ALA   A C   1 
ATOM   792  O O   . ALA   A 1 110 ? 14.43040  -2.40432  -13.59213 1.000 33.66132 ? 117 ALA   A O   1 
ATOM   793  C CB  . ALA   A 1 110 ? 13.74882  -1.48078  -16.64254 1.000 34.25085 ? 117 ALA   A CB  1 
ATOM   794  N N   . PHE   A 1 111 ? 13.67164  -4.13405  -14.83186 1.000 30.82523 ? 118 PHE   A N   1 
ATOM   795  C CA  . PHE   A 1 111 ? 13.16023  -4.87414  -13.67217 1.000 30.84761 ? 118 PHE   A CA  1 
ATOM   796  C C   . PHE   A 1 111 ? 14.30104  -5.27744  -12.74529 1.000 34.67567 ? 118 PHE   A C   1 
ATOM   797  O O   . PHE   A 1 111 ? 14.25441  -5.04349  -11.53353 1.000 31.97197 ? 118 PHE   A O   1 
ATOM   798  C CB  . PHE   A 1 111 ? 12.37616  -6.10359  -14.16323 1.000 27.55244 ? 118 PHE   A CB  1 
ATOM   799  C CG  . PHE   A 1 111 ? 11.76880  -6.96544  -13.07459 1.000 28.68033 ? 118 PHE   A CG  1 
ATOM   800  C CD1 . PHE   A 1 111 ? 11.18494  -6.40650  -11.93065 1.000 29.37444 ? 118 PHE   A CD1 1 
ATOM   801  C CD2 . PHE   A 1 111 ? 11.68107  -8.34581  -13.25185 1.000 30.29082 ? 118 PHE   A CD2 1 
ATOM   802  C CE1 . PHE   A 1 111 ? 10.60265  -7.22438  -10.95253 1.000 31.27212 ? 118 PHE   A CE1 1 
ATOM   803  C CE2 . PHE   A 1 111 ? 11.09096  -9.16327  -12.28847 1.000 31.36018 ? 118 PHE   A CE2 1 
ATOM   804  C CZ  . PHE   A 1 111 ? 10.54643  -8.59874  -11.13491 1.000 27.33301 ? 118 PHE   A CZ  1 
ATOM   805  N N   . MET   A 1 112 ? 15.36905  -5.83434  -13.30807 1.000 36.29062 ? 119 MET   A N   1 
ATOM   806  C CA  . MET   A 1 112 ? 16.45917  -6.26821  -12.45040 1.000 38.47125 ? 119 MET   A CA  1 
ATOM   807  C C   . MET   A 1 112 ? 17.18540  -5.08056  -11.81084 1.000 40.85257 ? 119 MET   A C   1 
ATOM   808  O O   . MET   A 1 112 ? 17.57503  -5.15501  -10.63645 1.000 38.73941 ? 119 MET   A O   1 
ATOM   809  C CB  . MET   A 1 112 ? 17.37413  -7.19122  -13.25923 1.000 39.69040 ? 119 MET   A CB  1 
ATOM   810  C CG  . MET   A 1 112 ? 16.75310  -8.61581  -13.32129 1.000 39.37827 ? 119 MET   A CG  1 
ATOM   811  S SD  . MET   A 1 112 ? 17.76234  -9.77610  -14.21460 1.000 60.45673 ? 119 MET   A SD  1 
ATOM   812  C CE  . MET   A 1 112 ? 18.89476  -10.27531 -12.90370 1.000 49.29736 ? 119 MET   A CE  1 
ATOM   813  N N   . GLU   A 1 113 ? 17.32225  -3.95684  -12.52713 1.000 38.17018 ? 120 GLU   A N   1 
ATOM   814  C CA  . GLU   A 1 113 ? 17.87170  -2.75390  -11.89395 1.000 44.05622 ? 120 GLU   A CA  1 
ATOM   815  C C   . GLU   A 1 113 ? 16.94791  -2.21021  -10.80340 1.000 42.72680 ? 120 GLU   A C   1 
ATOM   816  O O   . GLU   A 1 113 ? 17.42616  -1.67893  -9.78985  1.000 42.19701 ? 120 GLU   A O   1 
ATOM   817  C CB  . GLU   A 1 113 ? 18.13911  -1.67146  -12.94562 1.000 48.30562 ? 120 GLU   A CB  1 
ATOM   818  C CG  . GLU   A 1 113 ? 19.21369  -2.01202  -13.96646 1.000 51.44756 ? 120 GLU   A CG  1 
ATOM   819  C CD  . GLU   A 1 113 ? 19.25133  -1.01937  -15.13338 1.000 60.60786 ? 120 GLU   A CD  1 
ATOM   820  O OE1 . GLU   A 1 113 ? 20.32247  -0.86737  -15.76825 1.000 63.32905 ? 120 GLU   A OE1 1 
ATOM   821  O OE2 . GLU   A 1 113 ? 18.19328  -0.41317  -15.43696 1.000 57.46462 ? 120 GLU   A OE2 1 
ATOM   822  N N   . ALA   A 1 114 ? 15.62983  -2.32483  -10.99392 1.000 37.28197 ? 121 ALA   A N   1 
ATOM   823  C CA  . ALA   A 1 114 ? 14.69286  -1.87927  -9.96813  1.000 39.47028 ? 121 ALA   A CA  1 
ATOM   824  C C   . ALA   A 1 114 ? 14.81640  -2.71884  -8.70365  1.000 41.89984 ? 121 ALA   A C   1 
ATOM   825  O O   . ALA   A 1 114 ? 14.77441  -2.17607  -7.59237  1.000 43.19135 ? 121 ALA   A O   1 
ATOM   826  C CB  . ALA   A 1 114 ? 13.26156  -1.92950  -10.49735 1.000 35.99159 ? 121 ALA   A CB  1 
ATOM   827  N N   . LEU   A 1 115 ? 14.96521  -4.04134  -8.85497  1.000 35.98851 ? 122 LEU   A N   1 
ATOM   828  C CA  . LEU   A 1 115 ? 15.14060  -4.91982  -7.69495  1.000 37.47842 ? 122 LEU   A CA  1 
ATOM   829  C C   . LEU   A 1 115 ? 16.40674  -4.57386  -6.92529  1.000 42.63457 ? 122 LEU   A C   1 
ATOM   830  O O   . LEU   A 1 115 ? 16.42045  -4.61041  -5.68849  1.000 45.22015 ? 122 LEU   A O   1 
ATOM   831  C CB  . LEU   A 1 115 ? 15.17533  -6.38118  -8.14809  1.000 36.15555 ? 122 LEU   A CB  1 
ATOM   832  C CG  . LEU   A 1 115 ? 13.86593  -6.89361  -8.76262  1.000 35.70218 ? 122 LEU   A CG  1 
ATOM   833  C CD1 . LEU   A 1 115 ? 13.99688  -8.33326  -9.23283  1.000 35.53536 ? 122 LEU   A CD1 1 
ATOM   834  C CD2 . LEU   A 1 115 ? 12.75679  -6.79030  -7.72962  1.000 35.83790 ? 122 LEU   A CD2 1 
ATOM   835  N N   . GLN   A 1 116 ? 17.48661  -4.23425  -7.63090  1.000 45.95856 ? 123 GLN   A N   1 
ATOM   836  C CA  . GLN   A 1 116 ? 18.67398  -3.81185  -6.89625  1.000 48.55578 ? 123 GLN   A CA  1 
ATOM   837  C C   . GLN   A 1 116 ? 18.45995  -2.50521  -6.14601  1.000 48.55685 ? 123 GLN   A C   1 
ATOM   838  O O   . GLN   A 1 116 ? 19.18387  -2.22928  -5.18141  1.000 53.15328 ? 123 GLN   A O   1 
ATOM   839  C CB  . GLN   A 1 116 ? 19.88534  -3.68884  -7.82184  1.000 54.92800 ? 123 GLN   A CB  1 
ATOM   840  C CG  . GLN   A 1 116 ? 20.23070  -4.98783  -8.49270  1.000 60.21780 ? 123 GLN   A CG  1 
ATOM   841  C CD  . GLN   A 1 116 ? 20.75937  -5.99811  -7.48287  1.000 69.58128 ? 123 GLN   A CD  1 
ATOM   842  O OE1 . GLN   A 1 116 ? 21.90283  -5.90179  -7.01582  1.000 68.07474 ? 123 GLN   A OE1 1 
ATOM   843  N NE2 . GLN   A 1 116 ? 19.91849  -6.98412  -7.14279  1.000 64.15172 ? 123 GLN   A NE2 1 
ATOM   844  N N   . ALA   A 1 117 ? 17.47808  -1.70670  -6.54901  1.000 50.56367 ? 124 ALA   A N   1 
ATOM   845  C CA  . ALA   A 1 117 ? 17.19993  -0.42904  -5.91148  1.000 52.71312 ? 124 ALA   A CA  1 
ATOM   846  C C   . ALA   A 1 117 ? 16.02408  -0.48612  -4.93915  1.000 47.55837 ? 124 ALA   A C   1 
ATOM   847  O O   . ALA   A 1 117 ? 15.57784  0.56373   -4.46963  1.000 54.50778 ? 124 ALA   A O   1 
ATOM   848  C CB  . ALA   A 1 117 ? 16.94861  0.63893   -6.97972  1.000 52.52993 ? 124 ALA   A CB  1 
ATOM   849  N N   . GLY   A 1 118 ? 15.50480  -1.67205  -4.62888  1.000 48.66055 ? 125 GLY   A N   1 
ATOM   850  C CA  . GLY   A 1 118 ? 14.50535  -1.77878  -3.57808  1.000 48.08194 ? 125 GLY   A CA  1 
ATOM   851  C C   . GLY   A 1 118 ? 13.08469  -2.11775  -4.00505  1.000 46.95788 ? 125 GLY   A C   1 
ATOM   852  O O   . GLY   A 1 118 ? 12.14447  -1.81442  -3.27517  1.000 46.30169 ? 125 GLY   A O   1 
ATOM   853  N N   . ALA   A 1 119 ? 12.89117  -2.71174  -5.17348  1.000 46.39702 ? 126 ALA   A N   1 
ATOM   854  C CA  . ALA   A 1 119 ? 11.58004  -3.22636  -5.55692  1.000 45.14818 ? 126 ALA   A CA  1 
ATOM   855  C C   . ALA   A 1 119 ? 11.48709  -4.70696  -5.18591  1.000 47.48836 ? 126 ALA   A C   1 
ATOM   856  O O   . ALA   A 1 119 ? 12.49660  -5.33749  -4.87339  1.000 51.28797 ? 126 ALA   A O   1 
ATOM   857  C CB  . ALA   A 1 119 ? 11.34964  -3.00473  -7.05614  1.000 48.54470 ? 126 ALA   A CB  1 
ATOM   858  N N   . ASP   A 1 120 ? 10.26865  -5.27171  -5.17713  1.000 52.05717 ? 127 ASP   A N   1 
ATOM   859  C CA  . ASP   A 1 120 ? 10.22214  -6.73832  -5.11064  1.000 54.33940 ? 127 ASP   A CA  1 
ATOM   860  C C   . ASP   A 1 120 ? 9.55143   -7.26803  -6.35649  1.000 39.17266 ? 127 ASP   A C   1 
ATOM   861  O O   . ASP   A 1 120 ? 9.08137   -6.51384  -7.22239  1.000 41.64259 ? 127 ASP   A O   1 
ATOM   862  C CB  . ASP   A 1 120 ? 9.47231   -7.33861  -3.90517  1.000 62.70817 ? 127 ASP   A CB  1 
ATOM   863  C CG  . ASP   A 1 120 ? 7.94732   -7.25946  -4.05235  1.000 65.09698 ? 127 ASP   A CG  1 
ATOM   864  O OD1 . ASP   A 1 120 ? 7.46322   -6.11296  -4.22826  1.000 64.63602 ? 127 ASP   A OD1 1 
ATOM   865  O OD2 . ASP   A 1 120 ? 7.25751   -8.34399  -4.04936  1.000 48.21991 ? 127 ASP   A OD2 1 
ATOM   866  N N   . ILE   A 1 121 ? 9.51439   -8.59825  -6.39775  1.000 43.21477 ? 128 ILE   A N   1 
ATOM   867  C CA  . ILE   A 1 121 ? 9.07639   -9.34768  -7.55173  1.000 43.39950 ? 128 ILE   A CA  1 
ATOM   868  C C   . ILE   A 1 121 ? 7.68156   -8.93398  -7.98353  1.000 37.97067 ? 128 ILE   A C   1 
ATOM   869  O O   . ILE   A 1 121 ? 7.36871   -8.95852  -9.17643  1.000 34.56408 ? 128 ILE   A O   1 
ATOM   870  C CB  . ILE   A 1 121 ? 9.15581   -10.85687 -7.23697  1.000 41.29654 ? 128 ILE   A CB  1 
ATOM   871  C CG1 . ILE   A 1 121 ? 10.60779  -11.35408 -7.21130  1.000 53.85535 ? 128 ILE   A CG1 1 
ATOM   872  C CG2 . ILE   A 1 121 ? 8.40487   -11.65027 -8.22310  1.000 34.86686 ? 128 ILE   A CG2 1 
ATOM   873  C CD1 . ILE   A 1 121 ? 11.23201  -11.43174 -5.85046  1.000 47.49987 ? 128 ILE   A CD1 1 
ATOM   874  N N   . SER   A 1 122 ? 6.81871   -8.54611  -7.04261  1.000 39.42072 ? 129 SER   A N   1 
ATOM   875  C CA  . SER   A 1 122 ? 5.43017   -8.35232  -7.45163  1.000 35.96824 ? 129 SER   A CA  1 
ATOM   876  C C   . SER   A 1 122 ? 5.23232   -7.12274  -8.33339  1.000 35.99928 ? 129 SER   A C   1 
ATOM   877  O O   . SER   A 1 122 ? 4.14651   -6.96958  -8.90661  1.000 36.87271 ? 129 SER   A O   1 
ATOM   878  C CB  . SER   A 1 122 ? 4.51600   -8.28804  -6.23136  1.000 34.88785 ? 129 SER   A CB  1 
ATOM   879  O OG  . SER   A 1 122 ? 4.69337   -7.07432  -5.54878  1.000 42.01781 ? 129 SER   A OG  1 
ATOM   880  N N   . MET   A 1 123 ? 6.24484   -6.26813  -8.48094  1.000 30.72620 ? 130 MET   A N   1 
ATOM   881  C CA  . MET   A 1 123 ? 6.20293   -5.14244  -9.41050  1.000 32.95451 ? 130 MET   A CA  1 
ATOM   882  C C   . MET   A 1 123 ? 6.54399   -5.52032  -10.84901 1.000 30.35089 ? 130 MET   A C   1 
ATOM   883  O O   . MET   A 1 123 ? 6.57945   -4.63180  -11.71017 1.000 30.39659 ? 130 MET   A O   1 
ATOM   884  C CB  . MET   A 1 123 ? 7.13567   -4.03399  -8.90732  1.000 33.34235 ? 130 MET   A CB  1 
ATOM   885  C CG  . MET   A 1 123 ? 6.67381   -3.53760  -7.52091  1.000 38.80374 ? 130 MET   A CG  1 
ATOM   886  S SD  . MET   A 1 123 ? 7.78292   -2.34236  -6.71879  1.000 47.38303 ? 130 MET   A SD  1 
ATOM   887  C CE  . MET   A 1 123 ? 7.86463   -1.06406  -7.95343  1.000 46.11892 ? 130 MET   A CE  1 
ATOM   888  N N   . ILE   A 1 124 ? 6.74347   -6.81218  -11.13975 1.000 26.59060 ? 131 ILE   A N   1 
ATOM   889  C CA  . ILE   A 1 124 ? 7.16551   -7.27058  -12.47027 1.000 27.22446 ? 131 ILE   A CA  1 
ATOM   890  C C   . ILE   A 1 124 ? 6.33488   -6.63190  -13.58957 1.000 24.67526 ? 131 ILE   A C   1 
ATOM   891  O O   . ILE   A 1 124 ? 6.86871   -6.26573  -14.63735 1.000 25.18175 ? 131 ILE   A O   1 
ATOM   892  C CB  . ILE   A 1 124 ? 7.10343   -8.81166  -12.54144 1.000 25.82978 ? 131 ILE   A CB  1 
ATOM   893  C CG1 . ILE   A 1 124 ? 7.71977   -9.32115  -13.85626 1.000 25.72895 ? 131 ILE   A CG1 1 
ATOM   894  C CG2 . ILE   A 1 124 ? 5.64869   -9.31543  -12.30420 1.000 26.34437 ? 131 ILE   A CG2 1 
ATOM   895  C CD1 . ILE   A 1 124 ? 7.78616   -10.85029 -13.93894 1.000 28.75562 ? 131 ILE   A CD1 1 
ATOM   896  N N   . GLY   A 1 125 ? 5.02951   -6.44427  -13.36798 1.000 26.65745 ? 132 GLY   A N   1 
ATOM   897  C CA  . GLY   A 1 125 ? 4.17685   -5.90946  -14.42309 1.000 27.57433 ? 132 GLY   A CA  1 
ATOM   898  C C   . GLY   A 1 125 ? 4.50727   -4.48174  -14.83480 1.000 29.42989 ? 132 GLY   A C   1 
ATOM   899  O O   . GLY   A 1 125 ? 4.18755   -4.06852  -15.95550 1.000 31.96077 ? 132 GLY   A O   1 
ATOM   900  N N   . GLN   A 1 126 ? 5.11650   -3.70458  -13.93776 1.000 29.29219 ? 133 GLN   A N   1 
ATOM   901  C CA  . GLN   A 1 126 ? 5.50100   -2.33559  -14.25545 1.000 31.28657 ? 133 GLN   A CA  1 
ATOM   902  C C   . GLN   A 1 126 ? 6.60460   -2.25820  -15.28867 1.000 35.30274 ? 133 GLN   A C   1 
ATOM   903  O O   . GLN   A 1 126 ? 6.88137   -1.15779  -15.78412 1.000 36.08223 ? 133 GLN   A O   1 
ATOM   904  C CB  . GLN   A 1 126 ? 5.94560   -1.60117  -12.99775 1.000 34.45731 ? 133 GLN   A CB  1 
ATOM   905  C CG  . GLN   A 1 126 ? 4.87149   -1.62657  -11.91363 1.000 39.27601 ? 133 GLN   A CG  1 
ATOM   906  C CD  . GLN   A 1 126 ? 5.32482   -0.99330  -10.61841 1.000 44.52877 ? 133 GLN   A CD  1 
ATOM   907  O OE1 . GLN   A 1 126 ? 6.26243   -0.17750  -10.59000 1.000 44.96900 ? 133 GLN   A OE1 1 
ATOM   908  N NE2 . GLN   A 1 126 ? 4.65117   -1.35341  -9.53039  1.000 46.00949 ? 133 GLN   A NE2 1 
ATOM   909  N N   . PHE   A 1 127 ? 7.24008   -3.38248  -15.60687 1.000 30.51506 ? 134 PHE   A N   1 
ATOM   910  C CA  . PHE   A 1 127 ? 8.36455   -3.41685  -16.53480 1.000 26.70411 ? 134 PHE   A CA  1 
ATOM   911  C C   . PHE   A 1 127 ? 8.02899   -4.15003  -17.81777 1.000 29.63003 ? 134 PHE   A C   1 
ATOM   912  O O   . PHE   A 1 127 ? 8.92861   -4.42727  -18.62111 1.000 29.94914 ? 134 PHE   A O   1 
ATOM   913  C CB  . PHE   A 1 127 ? 9.57491   -4.02235  -15.81959 1.000 26.45094 ? 134 PHE   A CB  1 
ATOM   914  C CG  . PHE   A 1 127 ? 9.88639   -3.29035  -14.54963 1.000 28.46007 ? 134 PHE   A CG  1 
ATOM   915  C CD1 . PHE   A 1 127 ? 10.38926  -1.98682  -14.59870 1.000 34.96600 ? 134 PHE   A CD1 1 
ATOM   916  C CD2 . PHE   A 1 127 ? 9.55124   -3.82676  -13.31827 1.000 27.26946 ? 134 PHE   A CD2 1 
ATOM   917  C CE1 . PHE   A 1 127 ? 10.61266  -1.26864  -13.42370 1.000 32.13597 ? 134 PHE   A CE1 1 
ATOM   918  C CE2 . PHE   A 1 127 ? 9.75997   -3.12485  -12.15969 1.000 34.81150 ? 134 PHE   A CE2 1 
ATOM   919  C CZ  . PHE   A 1 127 ? 10.30203  -1.84466  -12.20942 1.000 37.46874 ? 134 PHE   A CZ  1 
ATOM   920  N N   . GLY   A 1 128 ? 6.75352   -4.44860  -18.03366 1.000 26.68983 ? 135 GLY   A N   1 
ATOM   921  C CA  . GLY   A 1 128 ? 6.30964   -4.99055  -19.28802 1.000 27.90455 ? 135 GLY   A CA  1 
ATOM   922  C C   . GLY   A 1 128 ? 6.55595   -6.46711  -19.47652 1.000 27.86557 ? 135 GLY   A C   1 
ATOM   923  O O   . GLY   A 1 128 ? 6.33467   -6.96230  -20.58812 1.000 29.73893 ? 135 GLY   A O   1 
ATOM   924  N N   . VAL   A 1 129 ? 7.00831   -7.18893  -18.44088 1.000 23.82907 ? 136 VAL   A N   1 
ATOM   925  C CA  . VAL   A 1 129 ? 7.34492   -8.60267  -18.60199 1.000 21.91805 ? 136 VAL   A CA  1 
ATOM   926  C C   . VAL   A 1 129 ? 6.49298   -9.45651  -17.65871 1.000 22.90072 ? 136 VAL   A C   1 
ATOM   927  O O   . VAL   A 1 129 ? 6.86738   -10.58404 -17.28956 1.000 22.95435 ? 136 VAL   A O   1 
ATOM   928  C CB  . VAL   A 1 129 ? 8.86329   -8.84177  -18.40902 1.000 23.87865 ? 136 VAL   A CB  1 
ATOM   929  C CG1 . VAL   A 1 129 ? 9.64834   -8.24617  -19.61510 1.000 25.13051 ? 136 VAL   A CG1 1 
ATOM   930  C CG2 . VAL   A 1 129 ? 9.35921   -8.20233  -17.12582 1.000 23.35282 ? 136 VAL   A CG2 1 
ATOM   931  N N   . GLY   A 1 130 ? 5.30631   -8.94987  -17.30710 1.000 20.96927 ? 137 GLY   A N   1 
ATOM   932  C CA  . GLY   A 1 130 ? 4.43624   -9.69991  -16.41553 1.000 22.37673 ? 137 GLY   A CA  1 
ATOM   933  C C   . GLY   A 1 130 ? 4.01179   -11.05464 -16.95287 1.000 22.72684 ? 137 GLY   A C   1 
ATOM   934  O O   . GLY   A 1 130 ? 3.69249   -11.95117 -16.15574 1.000 22.82076 ? 137 GLY   A O   1 
ATOM   935  N N   . PHE   A 1 131 ? 4.02712   -11.23955 -18.27494 1.000 22.26270 ? 138 PHE   A N   1 
ATOM   936  C CA  . PHE   A 1 131 ? 3.62588   -12.53535 -18.82447 1.000 20.78396 ? 138 PHE   A CA  1 
ATOM   937  C C   . PHE   A 1 131 ? 4.42887   -13.67702 -18.22520 1.000 21.06588 ? 138 PHE   A C   1 
ATOM   938  O O   . PHE   A 1 131 ? 3.88357   -14.74518 -17.93822 1.000 21.39607 ? 138 PHE   A O   1 
ATOM   939  C CB  . PHE   A 1 131 ? 3.78492   -12.56049 -20.34310 1.000 24.91286 ? 138 PHE   A CB  1 
ATOM   940  C CG  . PHE   A 1 131 ? 3.73700   -13.94887 -20.92294 1.000 22.71273 ? 138 PHE   A CG  1 
ATOM   941  C CD1 . PHE   A 1 131 ? 2.52314   -14.58019 -21.11717 1.000 22.76286 ? 138 PHE   A CD1 1 
ATOM   942  C CD2 . PHE   A 1 131 ? 4.91742   -14.63288 -21.23213 1.000 21.90593 ? 138 PHE   A CD2 1 
ATOM   943  C CE1 . PHE   A 1 131 ? 2.45793   -15.87662 -21.65308 1.000 22.41366 ? 138 PHE   A CE1 1 
ATOM   944  C CE2 . PHE   A 1 131 ? 4.87087   -15.92081 -21.77028 1.000 23.39380 ? 138 PHE   A CE2 1 
ATOM   945  C CZ  . PHE   A 1 131 ? 3.63454   -16.54917 -21.97214 1.000 22.55806 ? 138 PHE   A CZ  1 
ATOM   946  N N   . TYR   A 1 132 ? 5.73586   -13.48146 -18.05974 1.000 20.96788 ? 139 TYR   A N   1 
ATOM   947  C CA  . TYR   A 1 132 ? 6.57960   -14.58439 -17.61961 1.000 21.28283 ? 139 TYR   A CA  1 
ATOM   948  C C   . TYR   A 1 132 ? 6.32489   -15.01594 -16.17688 1.000 23.45683 ? 139 TYR   A C   1 
ATOM   949  O O   . TYR   A 1 132 ? 6.82389   -16.08390 -15.78391 1.000 21.98563 ? 139 TYR   A O   1 
ATOM   950  C CB  . TYR   A 1 132 ? 8.05832   -14.19906 -17.82522 1.000 21.10145 ? 139 TYR   A CB  1 
ATOM   951  C CG  . TYR   A 1 132 ? 8.32942   -13.90653 -19.28737 1.000 23.88846 ? 139 TYR   A CG  1 
ATOM   952  C CD1 . TYR   A 1 132 ? 8.57968   -14.93517 -20.21323 1.000 23.90257 ? 139 TYR   A CD1 1 
ATOM   953  C CD2 . TYR   A 1 132 ? 8.28539   -12.58693 -19.76270 1.000 24.11344 ? 139 TYR   A CD2 1 
ATOM   954  C CE1 . TYR   A 1 132 ? 8.80262   -14.64407 -21.58845 1.000 22.54452 ? 139 TYR   A CE1 1 
ATOM   955  C CE2 . TYR   A 1 132 ? 8.49926   -12.28996 -21.10028 1.000 27.08721 ? 139 TYR   A CE2 1 
ATOM   956  C CZ  . TYR   A 1 132 ? 8.76197   -13.31516 -22.00482 1.000 27.45774 ? 139 TYR   A CZ  1 
ATOM   957  O OH  . TYR   A 1 132 ? 8.94958   -12.98660 -23.31534 1.000 27.09783 ? 139 TYR   A OH  1 
ATOM   958  N N   . SER   A 1 133 ? 5.56306   -14.24165 -15.38063 1.000 22.42396 ? 140 SER   A N   1 
ATOM   959  C CA  . SER   A 1 133 ? 5.13760   -14.71544 -14.07011 1.000 23.34312 ? 140 SER   A CA  1 
ATOM   960  C C   . SER   A 1 133 ? 4.25043   -15.94553 -14.16005 1.000 20.14745 ? 140 SER   A C   1 
ATOM   961  O O   . SER   A 1 133 ? 4.03205   -16.59314 -13.13506 1.000 21.06058 ? 140 SER   A O   1 
ATOM   962  C CB  . SER   A 1 133 ? 4.39917   -13.62368 -13.27095 1.000 23.90542 ? 140 SER   A CB  1 
ATOM   963  O OG  . SER   A 1 133 ? 3.10901   -13.31645 -13.80142 1.000 23.37238 ? 140 SER   A OG  1 
ATOM   964  N N   . ALA   A 1 134 ? 3.73843   -16.27211 -15.35155 1.000 23.86707 ? 141 ALA   A N   1 
ATOM   965  C CA  . ALA   A 1 134 ? 3.04845   -17.54357 -15.54809 1.000 20.05592 ? 141 ALA   A CA  1 
ATOM   966  C C   . ALA   A 1 134 ? 3.87983   -18.71945 -15.04902 1.000 21.53758 ? 141 ALA   A C   1 
ATOM   967  O O   . ALA   A 1 134 ? 3.32199   -19.71615 -14.58432 1.000 21.76119 ? 141 ALA   A O   1 
ATOM   968  C CB  . ALA   A 1 134 ? 2.74821   -17.75941 -17.04035 1.000 20.66997 ? 141 ALA   A CB  1 
ATOM   969  N N   . TYR   A 1 135 ? 5.22313   -18.63232 -15.15923 1.000 21.01766 ? 142 TYR   A N   1 
ATOM   970  C CA  . TYR   A 1 135 ? 6.08680   -19.73900 -14.75861 1.000 20.79635 ? 142 TYR   A CA  1 
ATOM   971  C C   . TYR   A 1 135 ? 6.24712   -19.84330 -13.23268 1.000 24.04721 ? 142 TYR   A C   1 
ATOM   972  O O   . TYR   A 1 135 ? 6.92503   -20.75517 -12.75170 1.000 24.94570 ? 142 TYR   A O   1 
ATOM   973  C CB  . TYR   A 1 135 ? 7.44214   -19.61322 -15.51725 1.000 20.77283 ? 142 TYR   A CB  1 
ATOM   974  C CG  . TYR   A 1 135 ? 7.25130   -19.93683 -16.99779 1.000 24.78067 ? 142 TYR   A CG  1 
ATOM   975  C CD1 . TYR   A 1 135 ? 7.24808   -21.25497 -17.45467 1.000 23.47098 ? 142 TYR   A CD1 1 
ATOM   976  C CD2 . TYR   A 1 135 ? 6.96344   -18.91942 -17.91665 1.000 20.81823 ? 142 TYR   A CD2 1 
ATOM   977  C CE1 . TYR   A 1 135 ? 7.01291   -21.55927 -18.80917 1.000 21.15780 ? 142 TYR   A CE1 1 
ATOM   978  C CE2 . TYR   A 1 135 ? 6.72475   -19.21166 -19.27943 1.000 23.10324 ? 142 TYR   A CE2 1 
ATOM   979  C CZ  . TYR   A 1 135 ? 6.74095   -20.53236 -19.69797 1.000 23.03569 ? 142 TYR   A CZ  1 
ATOM   980  O OH  . TYR   A 1 135 ? 6.51201   -20.80827 -21.02862 1.000 21.69668 ? 142 TYR   A OH  1 
ATOM   981  N N   . LEU   A 1 136 ? 5.58802   -18.97356 -12.45785 1.000 23.68037 ? 143 LEU   A N   1 
ATOM   982  C CA  . LEU   A 1 136 ? 5.45423   -19.19616 -11.02035 1.000 23.82391 ? 143 LEU   A CA  1 
ATOM   983  C C   . LEU   A 1 136 ? 4.60473   -20.42803 -10.74022 1.000 24.39401 ? 143 LEU   A C   1 
ATOM   984  O O   . LEU   A 1 136 ? 4.82158   -21.10999 -9.73443  1.000 25.96608 ? 143 LEU   A O   1 
ATOM   985  C CB  . LEU   A 1 136 ? 4.79529   -17.99075 -10.34093 1.000 24.04488 ? 143 LEU   A CB  1 
ATOM   986  C CG  . LEU   A 1 136 ? 5.62698   -16.70042 -10.34917 1.000 23.19912 ? 143 LEU   A CG  1 
ATOM   987  C CD1 . LEU   A 1 136 ? 4.80829   -15.50837 -9.88387  1.000 25.87862 ? 143 LEU   A CD1 1 
ATOM   988  C CD2 . LEU   A 1 136 ? 6.88602   -16.87765 -9.48861  1.000 25.38075 ? 143 LEU   A CD2 1 
ATOM   989  N N   . VAL   A 1 137 ? 3.64076   -20.74090 -11.62975 1.000 23.82416 ? 144 VAL   A N   1 
ATOM   990  C CA  . VAL   A 1 137 ? 2.68624   -21.80840 -11.35591 1.000 23.12972 ? 144 VAL   A CA  1 
ATOM   991  C C   . VAL   A 1 137 ? 2.60645   -22.85162 -12.47087 1.000 23.60358 ? 144 VAL   A C   1 
ATOM   992  O O   . VAL   A 1 137 ? 2.05741   -23.93092 -12.25260 1.000 24.97563 ? 144 VAL   A O   1 
ATOM   993  C CB  . VAL   A 1 137 ? 1.27381   -21.24927 -11.06046 1.000 24.45407 ? 144 VAL   A CB  1 
ATOM   994  C CG1 . VAL   A 1 137 ? 1.28564   -20.36679 -9.79313  1.000 24.50570 ? 144 VAL   A CG1 1 
ATOM   995  C CG2 . VAL   A 1 137 ? 0.70321   -20.47697 -12.26274 1.000 21.37490 ? 144 VAL   A CG2 1 
ATOM   996  N N   . ALA   A 1 138 ? 3.15650   -22.56794 -13.64368 1.000 25.44776 ? 145 ALA   A N   1 
ATOM   997  C CA  . ALA   A 1 138 ? 2.99825   -23.45459 -14.79178 1.000 25.09782 ? 145 ALA   A CA  1 
ATOM   998  C C   . ALA   A 1 138 ? 4.31560   -24.12157 -15.13078 1.000 24.14930 ? 145 ALA   A C   1 
ATOM   999  O O   . ALA   A 1 138 ? 5.35881   -23.45955 -15.16831 1.000 28.52198 ? 145 ALA   A O   1 
ATOM   1000 C CB  . ALA   A 1 138 ? 2.49744   -22.68184 -16.01678 1.000 21.07742 ? 145 ALA   A CB  1 
ATOM   1001 N N   . GLU   A 1 139 ? 4.26149   -25.41868 -15.42578 1.000 23.31171 ? 146 GLU   A N   1 
ATOM   1002 C CA  . GLU   A 1 139 ? 5.43456   -26.09134 -15.97906 1.000 23.71096 ? 146 GLU   A CA  1 
ATOM   1003 C C   . GLU   A 1 139 ? 5.53556   -25.90497 -17.49733 1.000 27.33085 ? 146 GLU   A C   1 
ATOM   1004 O O   . GLU   A 1 139 ? 6.63130   -25.97586 -18.06416 1.000 28.04752 ? 146 GLU   A O   1 
ATOM   1005 C CB  . GLU   A 1 139 ? 5.38378   -27.56388 -15.58001 1.000 30.07112 ? 146 GLU   A CB  1 
ATOM   1006 C CG  . GLU   A 1 139 ? 4.26978   -28.34551 -16.23067 1.000 38.67293 ? 146 GLU   A CG  1 
ATOM   1007 C CD  . GLU   A 1 139 ? 4.20084   -29.80948 -15.76989 1.000 51.36628 ? 146 GLU   A CD  1 
ATOM   1008 O OE1 . GLU   A 1 139 ? 3.39170   -30.58004 -16.35509 1.000 53.88622 ? 146 GLU   A OE1 1 
ATOM   1009 O OE2 . GLU   A 1 139 ? 4.90662   -30.17351 -14.79382 1.000 50.47761 ? 146 GLU   A OE2 1 
ATOM   1010 N N   . LYS   A 1 140 ? 4.42768   -25.61252 -18.16190 1.000 23.51219 ? 147 LYS   A N   1 
ATOM   1011 C CA  . LYS   A 1 140 ? 4.40557   -25.39538 -19.60040 1.000 22.90010 ? 147 LYS   A CA  1 
ATOM   1012 C C   . LYS   A 1 140 ? 3.33296   -24.35250 -19.84545 1.000 22.26471 ? 147 LYS   A C   1 
ATOM   1013 O O   . LYS   A 1 140 ? 2.32016   -24.35031 -19.14208 1.000 22.67547 ? 147 LYS   A O   1 
ATOM   1014 C CB  . LYS   A 1 140 ? 4.10388   -26.69421 -20.34723 1.000 24.92317 ? 147 LYS   A CB  1 
ATOM   1015 C CG  . LYS   A 1 140 ? 4.09758   -26.57363 -21.84509 1.000 26.80712 ? 147 LYS   A CG  1 
ATOM   1016 C CD  . LYS   A 1 140 ? 3.96501   -27.95507 -22.45021 1.000 32.45857 ? 147 LYS   A CD  1 
ATOM   1017 C CE  . LYS   A 1 140 ? 2.57979   -28.24239 -22.96368 1.000 40.14075 ? 147 LYS   A CE  1 
ATOM   1018 N NZ  . LYS   A 1 140 ? 2.47743   -29.70317 -23.28078 1.000 42.41164 ? 147 LYS   A NZ  1 
ATOM   1019 N N   . VAL   A 1 141 ? 3.58210   -23.43575 -20.77697 1.000 20.59088 ? 148 VAL   A N   1 
ATOM   1020 C CA  . VAL   A 1 141 ? 2.57847   -22.44929 -21.18048 1.000 20.14339 ? 148 VAL   A CA  1 
ATOM   1021 C C   . VAL   A 1 141 ? 2.40348   -22.53350 -22.69489 1.000 26.67635 ? 148 VAL   A C   1 
ATOM   1022 O O   . VAL   A 1 141 ? 3.39662   -22.57649 -23.44139 1.000 21.36706 ? 148 VAL   A O   1 
ATOM   1023 C CB  . VAL   A 1 141 ? 2.97186   -21.02295 -20.76000 1.000 20.11491 ? 148 VAL   A CB  1 
ATOM   1024 C CG1 . VAL   A 1 141 ? 1.91413   -20.01801 -21.24856 1.000 20.82822 ? 148 VAL   A CG1 1 
ATOM   1025 C CG2 . VAL   A 1 141 ? 3.22240   -20.92362 -19.21432 1.000 19.95401 ? 148 VAL   A CG2 1 
ATOM   1026 N N   . THR   A 1 142 ? 1.13960   -22.58376 -23.14206 1.000 23.09313 ? 149 THR   A N   1 
ATOM   1027 C CA  . THR   A 1 142 ? 0.75655   -22.53419 -24.54972 1.000 22.65225 ? 149 THR   A CA  1 
ATOM   1028 C C   . THR   A 1 142 ? -0.03057  -21.24820 -24.77296 1.000 24.39616 ? 149 THR   A C   1 
ATOM   1029 O O   . THR   A 1 142 ? -0.94238  -20.93573 -23.99998 1.000 25.38118 ? 149 THR   A O   1 
ATOM   1030 C CB  . THR   A 1 142 ? -0.10700  -23.75276 -24.93059 1.000 23.33200 ? 149 THR   A CB  1 
ATOM   1031 O OG1 . THR   A 1 142 ? 0.52075   -24.97328 -24.50241 1.000 27.82043 ? 149 THR   A OG1 1 
ATOM   1032 C CG2 . THR   A 1 142 ? -0.34017  -23.81933 -26.43815 1.000 27.14344 ? 149 THR   A CG2 1 
ATOM   1033 N N   . VAL   A 1 143 ? 0.30580   -20.50360 -25.81923 1.000 20.62523 ? 150 VAL   A N   1 
ATOM   1034 C CA  . VAL   A 1 143 ? -0.40172  -19.26561 -26.16050 1.000 21.66959 ? 150 VAL   A CA  1 
ATOM   1035 C C   . VAL   A 1 143 ? -0.97385  -19.44230 -27.55807 1.000 25.98149 ? 150 VAL   A C   1 
ATOM   1036 O O   . VAL   A 1 143 ? -0.21020  -19.63464 -28.51092 1.000 23.43173 ? 150 VAL   A O   1 
ATOM   1037 C CB  . VAL   A 1 143 ? 0.53373   -18.04636 -26.10614 1.000 22.40547 ? 150 VAL   A CB  1 
ATOM   1038 C CG1 . VAL   A 1 143 ? -0.20843  -16.77131 -26.58538 1.000 23.52092 ? 150 VAL   A CG1 1 
ATOM   1039 C CG2 . VAL   A 1 143 ? 1.08703   -17.85351 -24.68732 1.000 24.48068 ? 150 VAL   A CG2 1 
ATOM   1040 N N   . ILE   A 1 144 ? -2.31292  -19.40987 -27.68893 1.000 21.08403 ? 151 ILE   A N   1 
ATOM   1041 C CA  . ILE   A 1 144 ? -2.97797  -19.45663 -28.99472 1.000 21.92047 ? 151 ILE   A CA  1 
ATOM   1042 C C   . ILE   A 1 144 ? -3.42889  -18.03699 -29.29666 1.000 23.94917 ? 151 ILE   A C   1 
ATOM   1043 O O   . ILE   A 1 144 ? -4.02426  -17.39150 -28.42412 1.000 23.72524 ? 151 ILE   A O   1 
ATOM   1044 C CB  . ILE   A 1 144 ? -4.19665  -20.40351 -28.98343 1.000 23.75754 ? 151 ILE   A CB  1 
ATOM   1045 C CG1 . ILE   A 1 144 ? -3.92515  -21.73730 -28.27798 1.000 32.50289 ? 151 ILE   A CG1 1 
ATOM   1046 C CG2 . ILE   A 1 144 ? -4.70410  -20.65079 -30.41616 1.000 31.76793 ? 151 ILE   A CG2 1 
ATOM   1047 C CD1 . ILE   A 1 144 ? -2.87831  -22.54353 -28.89908 1.000 33.69977 ? 151 ILE   A CD1 1 
ATOM   1048 N N   . THR   A 1 145 ? -3.15520  -17.53943 -30.50826 1.000 21.34929 ? 152 THR   A N   1 
ATOM   1049 C CA  . THR   A 1 145 ? -3.49238  -16.15008 -30.79357 1.000 23.03105 ? 152 THR   A CA  1 
ATOM   1050 C C   . THR   A 1 145 ? -3.92047  -15.96020 -32.24348 1.000 24.75334 ? 152 THR   A C   1 
ATOM   1051 O O   . THR   A 1 145 ? -3.47512  -16.67202 -33.15079 1.000 23.72115 ? 152 THR   A O   1 
ATOM   1052 C CB  . THR   A 1 145 ? -2.30949  -15.22805 -30.40697 1.000 23.63813 ? 152 THR   A CB  1 
ATOM   1053 O OG1 . THR   A 1 145 ? -2.74863  -13.86780 -30.35408 1.000 24.77041 ? 152 THR   A OG1 1 
ATOM   1054 C CG2 . THR   A 1 145 ? -1.10858  -15.38573 -31.37225 1.000 24.05034 ? 152 THR   A CG2 1 
ATOM   1055 N N   . LYS   A 1 146 ? -4.83905  -15.00761 -32.43781 1.000 23.19541 ? 153 LYS   A N   1 
ATOM   1056 C CA  . LYS   A 1 146 ? -5.31782  -14.62129 -33.76116 1.000 24.50773 ? 153 LYS   A CA  1 
ATOM   1057 C C   . LYS   A 1 146 ? -5.40263  -13.10457 -33.79769 1.000 24.27854 ? 153 LYS   A C   1 
ATOM   1058 O O   . LYS   A 1 146 ? -6.15027  -12.51568 -33.01842 1.000 24.03139 ? 153 LYS   A O   1 
ATOM   1059 C CB  . LYS   A 1 146 ? -6.68792  -15.24337 -34.05957 1.000 23.31260 ? 153 LYS   A CB  1 
ATOM   1060 C CG  . LYS   A 1 146 ? -7.33243  -14.82278 -35.40482 1.000 26.67028 ? 153 LYS   A CG  1 
ATOM   1061 C CD  . LYS   A 1 146 ? -6.55121  -15.37921 -36.61188 1.000 29.01533 ? 153 LYS   A CD  1 
ATOM   1062 C CE  . LYS   A 1 146 ? -7.25832  -15.02271 -37.93767 1.000 30.84676 ? 153 LYS   A CE  1 
ATOM   1063 N NZ  . LYS   A 1 146 ? -7.20000  -13.55980 -38.25679 1.000 27.50264 ? 153 LYS   A NZ  1 
ATOM   1064 N N   . HIS   A 1 147 ? -4.64465  -12.48843 -34.70037 1.000 24.46363 ? 154 HIS   A N   1 
ATOM   1065 C CA  . HIS   A 1 147 ? -4.66157  -11.05383 -34.96560 1.000 25.59450 ? 154 HIS   A CA  1 
ATOM   1066 C C   . HIS   A 1 147 ? -5.37260  -10.82388 -36.29856 1.000 28.16133 ? 154 HIS   A C   1 
ATOM   1067 O O   . HIS   A 1 147 ? -5.28369  -11.65902 -37.19322 1.000 26.00851 ? 154 HIS   A O   1 
ATOM   1068 C CB  . HIS   A 1 147 ? -3.21369  -10.54183 -35.00643 1.000 24.21405 ? 154 HIS   A CB  1 
ATOM   1069 C CG  . HIS   A 1 147 ? -3.07586  -9.05958  -35.13613 1.000 28.12569 ? 154 HIS   A CG  1 
ATOM   1070 N ND1 . HIS   A 1 147 ? -3.30183  -8.39119  -36.31968 1.000 26.57285 ? 154 HIS   A ND1 1 
ATOM   1071 C CD2 . HIS   A 1 147 ? -2.69163  -8.12058  -34.23667 1.000 25.33536 ? 154 HIS   A CD2 1 
ATOM   1072 C CE1 . HIS   A 1 147 ? -3.07577  -7.10060  -36.14649 1.000 32.16627 ? 154 HIS   A CE1 1 
ATOM   1073 N NE2 . HIS   A 1 147 ? -2.70095  -6.90947  -34.89275 1.000 28.57208 ? 154 HIS   A NE2 1 
ATOM   1074 N N   . ASN   A 1 148 ? -6.11272  -9.71144  -36.43869 1.000 27.62185 ? 155 ASN   A N   1 
ATOM   1075 C CA  . ASN   A 1 148 ? -6.82363  -9.46959  -37.70192 1.000 28.38796 ? 155 ASN   A CA  1 
ATOM   1076 C C   . ASN   A 1 148 ? -5.91368  -9.57693  -38.92865 1.000 29.30598 ? 155 ASN   A C   1 
ATOM   1077 O O   . ASN   A 1 148 ? -6.37790  -9.94108  -40.01791 1.000 32.51771 ? 155 ASN   A O   1 
ATOM   1078 C CB  . ASN   A 1 148 ? -7.49629  -8.08229  -37.69026 1.000 27.70233 ? 155 ASN   A CB  1 
ATOM   1079 C CG  . ASN   A 1 148 ? -8.79167  -8.04691  -36.91980 1.000 32.35057 ? 155 ASN   A CG  1 
ATOM   1080 O OD1 . ASN   A 1 148 ? -9.47960  -9.05887  -36.78042 1.000 34.88938 ? 155 ASN   A OD1 1 
ATOM   1081 N ND2 . ASN   A 1 148 ? -9.15331  -6.85815  -36.41999 1.000 31.17712 ? 155 ASN   A ND2 1 
ATOM   1082 N N   . ASP   A 1 149 ? -4.62605  -9.25569  -38.79234 1.000 30.86622 ? 156 ASP   A N   1 
ATOM   1083 C CA  . ASP   A 1 149 ? -3.72770  -9.17368  -39.94528 1.000 32.88352 ? 156 ASP   A CA  1 
ATOM   1084 C C   . ASP   A 1 149 ? -2.93239  -10.45737 -40.20409 1.000 36.46345 ? 156 ASP   A C   1 
ATOM   1085 O O   . ASP   A 1 149 ? -2.02844  -10.43924 -41.05085 1.000 34.96743 ? 156 ASP   A O   1 
ATOM   1086 C CB  . ASP   A 1 149 ? -2.73603  -8.01259  -39.76733 1.000 36.44649 ? 156 ASP   A CB  1 
ATOM   1087 C CG  . ASP   A 1 149 ? -3.39862  -6.64775  -39.76404 1.000 36.83490 ? 156 ASP   A CG  1 
ATOM   1088 O OD1 . ASP   A 1 149 ? -4.55543  -6.53841  -40.19164 1.000 34.38366 ? 156 ASP   A OD1 1 
ATOM   1089 O OD2 . ASP   A 1 149 ? -2.75502  -5.67934  -39.30781 1.000 42.73810 ? 156 ASP   A OD2 1 
ATOM   1090 N N   . ASP   A 1 150 ? -3.21137  -11.55629 -39.49398 1.000 31.99890 ? 157 ASP   A N   1 
ATOM   1091 C CA  . ASP   A 1 150 ? -2.39545  -12.77002 -39.62058 1.000 27.61788 ? 157 ASP   A CA  1 
ATOM   1092 C C   . ASP   A 1 150 ? -3.26696  -14.00342 -39.35481 1.000 37.23615 ? 157 ASP   A C   1 
ATOM   1093 O O   . ASP   A 1 150 ? -4.46016  -13.89840 -39.04586 1.000 30.26069 ? 157 ASP   A O   1 
ATOM   1094 C CB  . ASP   A 1 150 ? -1.18023  -12.71532 -38.67480 1.000 30.06396 ? 157 ASP   A CB  1 
ATOM   1095 C CG  . ASP   A 1 150 ? -0.00144  -13.55147 -39.17101 1.000 32.20098 ? 157 ASP   A CG  1 
ATOM   1096 O OD1 . ASP   A 1 150 ? -0.16146  -14.31670 -40.15343 1.000 34.39329 ? 157 ASP   A OD1 1 
ATOM   1097 O OD2 . ASP   A 1 150 ? 1.10832   -13.41572 -38.59365 1.000 32.37515 ? 157 ASP   A OD2 1 
ATOM   1098 N N   . GLU   A 1 151 ? -2.65578  -15.18475 -39.48364 1.000 30.99948 ? 158 GLU   A N   1 
ATOM   1099 C CA  . GLU   A 1 151 ? -3.29670  -16.47075 -39.25122 1.000 31.30798 ? 158 GLU   A CA  1 
ATOM   1100 C C   . GLU   A 1 151 ? -3.22696  -16.84390 -37.76426 1.000 25.45457 ? 158 GLU   A C   1 
ATOM   1101 O O   . GLU   A 1 151 ? -2.52444  -16.21471 -36.97328 1.000 29.27470 ? 158 GLU   A O   1 
ATOM   1102 C CB  . GLU   A 1 151 ? -2.61177  -17.55600 -40.08408 1.000 34.84006 ? 158 GLU   A CB  1 
ATOM   1103 C CG  . GLU   A 1 151 ? -2.71815  -17.38378 -41.59565 1.000 43.97338 ? 158 GLU   A CG  1 
ATOM   1104 C CD  . GLU   A 1 151 ? -4.09022  -16.91231 -42.08018 1.000 54.42801 ? 158 GLU   A CD  1 
ATOM   1105 O OE1 . GLU   A 1 151 ? -5.12774  -17.38178 -41.55253 1.000 59.37018 ? 158 GLU   A OE1 1 
ATOM   1106 O OE2 . GLU   A 1 151 ? -4.13333  -16.08312 -43.02167 1.000 66.04361 ? 158 GLU   A OE2 1 
ATOM   1107 N N   . GLN   A 1 152 ? -3.93765  -17.90825 -37.39401 1.000 26.93150 ? 159 GLN   A N   1 
ATOM   1108 C CA  . GLN   A 1 152 ? -3.93708  -18.38702 -36.00843 1.000 26.07822 ? 159 GLN   A CA  1 
ATOM   1109 C C   . GLN   A 1 152 ? -2.67389  -19.19624 -35.73929 1.000 25.50686 ? 159 GLN   A C   1 
ATOM   1110 O O   . GLN   A 1 152 ? -2.35780  -20.12444 -36.49706 1.000 28.22450 ? 159 GLN   A O   1 
ATOM   1111 C CB  . GLN   A 1 152 ? -5.16209  -19.25569 -35.73195 1.000 30.89129 ? 159 GLN   A CB  1 
ATOM   1112 C CG  . GLN   A 1 152 ? -5.40780  -19.53931 -34.24791 1.000 32.02037 ? 159 GLN   A CG  1 
ATOM   1113 C CD  . GLN   A 1 152 ? -6.83966  -19.98345 -33.96258 1.000 32.70553 ? 159 GLN   A CD  1 
ATOM   1114 O OE1 . GLN   A 1 152 ? -7.78267  -19.27188 -34.29902 1.000 34.92709 ? 159 GLN   A OE1 1 
ATOM   1115 N NE2 . GLN   A 1 152 ? -7.00670  -21.14610 -33.32771 1.000 31.82875 ? 159 GLN   A NE2 1 
ATOM   1116 N N   . TYR   A 1 153 ? -1.95376  -18.82880 -34.67413 1.000 23.86698 ? 160 TYR   A N   1 
ATOM   1117 C CA  . TYR   A 1 153 ? -0.68235  -19.45120 -34.30017 1.000 23.91063 ? 160 TYR   A CA  1 
ATOM   1118 C C   . TYR   A 1 153 ? -0.70505  -19.95102 -32.85505 1.000 25.54434 ? 160 TYR   A C   1 
ATOM   1119 O O   . TYR   A 1 153 ? -1.41249  -19.40608 -31.99484 1.000 24.40380 ? 160 TYR   A O   1 
ATOM   1120 C CB  . TYR   A 1 153 ? 0.47121   -18.46284 -34.46003 1.000 24.29794 ? 160 TYR   A CB  1 
ATOM   1121 C CG  . TYR   A 1 153 ? 0.88504   -18.28692 -35.90234 1.000 28.79971 ? 160 TYR   A CG  1 
ATOM   1122 C CD1 . TYR   A 1 153 ? 0.44117   -17.19946 -36.67298 1.000 30.73726 ? 160 TYR   A CD1 1 
ATOM   1123 C CD2 . TYR   A 1 153 ? 1.70613   -19.21926 -36.50240 1.000 30.05626 ? 160 TYR   A CD2 1 
ATOM   1124 C CE1 . TYR   A 1 153 ? 0.82240   -17.07693 -38.01254 1.000 36.13797 ? 160 TYR   A CE1 1 
ATOM   1125 C CE2 . TYR   A 1 153 ? 2.10263   -19.08818 -37.81297 1.000 34.77005 ? 160 TYR   A CE2 1 
ATOM   1126 C CZ  . TYR   A 1 153 ? 1.65354   -18.02997 -38.56272 1.000 37.32220 ? 160 TYR   A CZ  1 
ATOM   1127 O OH  . TYR   A 1 153 ? 2.06891   -17.95148 -39.86677 1.000 44.13005 ? 160 TYR   A OH  1 
ATOM   1128 N N   . ALA   A 1 154 ? 0.11401   -20.97530 -32.58458 1.000 23.43225 ? 161 ALA   A N   1 
ATOM   1129 C CA  . ALA   A 1 154 ? 0.34106   -21.49315 -31.23427 1.000 22.43412 ? 161 ALA   A CA  1 
ATOM   1130 C C   . ALA   A 1 154 ? 1.81890   -21.35379 -30.86142 1.000 24.86119 ? 161 ALA   A C   1 
ATOM   1131 O O   . ALA   A 1 154 ? 2.69263   -21.88259 -31.56914 1.000 25.12746 ? 161 ALA   A O   1 
ATOM   1132 C CB  . ALA   A 1 154 ? -0.09021  -22.96317 -31.14624 1.000 26.30390 ? 161 ALA   A CB  1 
ATOM   1133 N N   . TRP   A 1 155 ? 2.08666   -20.64536 -29.76483 1.000 21.56536 ? 162 TRP   A N   1 
ATOM   1134 C CA  . TRP   A 1 155 ? 3.40730   -20.52670 -29.13540 1.000 24.31410 ? 162 TRP   A CA  1 
ATOM   1135 C C   . TRP   A 1 155 ? 3.46109   -21.47342 -27.94772 1.000 24.08208 ? 162 TRP   A C   1 
ATOM   1136 O O   . TRP   A 1 155 ? 2.45879   -21.67672 -27.26347 1.000 24.38403 ? 162 TRP   A O   1 
ATOM   1137 C CB  . TRP   A 1 155 ? 3.63057   -19.07780 -28.67943 1.000 22.08860 ? 162 TRP   A CB  1 
ATOM   1138 C CG  . TRP   A 1 155 ? 4.89926   -18.67874 -27.90102 1.000 23.56000 ? 162 TRP   A CG  1 
ATOM   1139 C CD1 . TRP   A 1 155 ? 5.96662   -17.96787 -28.39450 1.000 22.33318 ? 162 TRP   A CD1 1 
ATOM   1140 C CD2 . TRP   A 1 155 ? 5.15772   -18.86539 -26.49894 1.000 21.25530 ? 162 TRP   A CD2 1 
ATOM   1141 N NE1 . TRP   A 1 155 ? 6.88307   -17.72911 -27.38522 1.000 21.26829 ? 162 TRP   A NE1 1 
ATOM   1142 C CE2 . TRP   A 1 155 ? 6.40020   -18.24802 -26.21242 1.000 23.69500 ? 162 TRP   A CE2 1 
ATOM   1143 C CE3 . TRP   A 1 155 ? 4.45412   -19.48034 -25.44871 1.000 22.30723 ? 162 TRP   A CE3 1 
ATOM   1144 C CZ2 . TRP   A 1 155 ? 6.97588   -18.27011 -24.94067 1.000 22.25501 ? 162 TRP   A CZ2 1 
ATOM   1145 C CZ3 . TRP   A 1 155 ? 5.01009   -19.46707 -24.18337 1.000 22.42570 ? 162 TRP   A CZ3 1 
ATOM   1146 C CH2 . TRP   A 1 155 ? 6.27916   -18.87456 -23.94159 1.000 22.54116 ? 162 TRP   A CH2 1 
ATOM   1147 N N   . GLU   A 1 156 ? 4.62725   -22.06633 -27.68860 1.000 19.75754 ? 163 GLU   A N   1 
ATOM   1148 C CA  . GLU   A 1 156 ? 4.67132   -22.94253 -26.52144 1.000 21.22666 ? 163 GLU   A CA  1 
ATOM   1149 C C   . GLU   A 1 156 ? 6.07201   -22.95859 -25.91158 1.000 23.39098 ? 163 GLU   A C   1 
ATOM   1150 O O   . GLU   A 1 156 ? 7.07415   -22.96139 -26.64849 1.000 22.81788 ? 163 GLU   A O   1 
ATOM   1151 C CB  . GLU   A 1 156 ? 4.29517   -24.36984 -26.91584 1.000 29.31943 ? 163 GLU   A CB  1 
ATOM   1152 C CG  . GLU   A 1 156 ? 4.10855   -25.36002 -25.76883 1.000 30.66349 ? 163 GLU   A CG  1 
ATOM   1153 C CD  . GLU   A 1 156 ? 3.25886   -26.54297 -26.22253 1.000 43.02065 ? 163 GLU   A CD  1 
ATOM   1154 O OE1 . GLU   A 1 156 ? 3.82888   -27.36992 -26.97826 1.000 39.35993 ? 163 GLU   A OE1 1 
ATOM   1155 O OE2 . GLU   A 1 156 ? 2.04107   -26.62431 -25.89574 1.000 37.45156 ? 163 GLU   A OE2 1 
ATOM   1156 N N   . SER   A 1 157 ? 6.14302   -23.02653 -24.57292 1.000 21.58054 ? 164 SER   A N   1 
ATOM   1157 C CA  . SER   A 1 157 ? 7.44976   -23.18340 -23.92038 1.000 21.32080 ? 164 SER   A CA  1 
ATOM   1158 C C   . SER   A 1 157 ? 7.31782   -23.84977 -22.55952 1.000 23.13429 ? 164 SER   A C   1 
ATOM   1159 O O   . SER   A 1 157 ? 6.44259   -23.49486 -21.75493 1.000 21.54965 ? 164 SER   A O   1 
ATOM   1160 C CB  . SER   A 1 157 ? 8.19308   -21.84899 -23.73750 1.000 20.87409 ? 164 SER   A CB  1 
ATOM   1161 O OG  . SER   A 1 157 ? 9.51736   -22.11984 -23.17730 1.000 22.92006 ? 164 SER   A OG  1 
ATOM   1162 N N   . SER   A 1 158 ? 8.24227   -24.77546 -22.29340 1.000 24.22921 ? 165 SER   A N   1 
ATOM   1163 C CA  . SER   A 1 158 ? 8.46964   -25.31661 -20.95299 1.000 23.94209 ? 165 SER   A CA  1 
ATOM   1164 C C   . SER   A 1 158 ? 9.73798   -24.73844 -20.32262 1.000 24.18578 ? 165 SER   A C   1 
ATOM   1165 O O   . SER   A 1 158 ? 10.36198  -25.38732 -19.45832 1.000 29.30734 ? 165 SER   A O   1 
ATOM   1166 C CB  . SER   A 1 158 ? 8.55972   -26.83885 -21.01381 1.000 28.63887 ? 165 SER   A CB  1 
ATOM   1167 O OG  . SER   A 1 158 ? 7.33021   -27.41706 -21.45416 1.000 28.51492 ? 165 SER   A OG  1 
ATOM   1168 N N   . ALA   A 1 159 ? 10.12718  -23.54048 -20.74965 1.000 23.08990 ? 166 ALA   A N   1 
ATOM   1169 C CA  . ALA   A 1 159 ? 11.35400  -22.82919 -20.32603 1.000 28.86568 ? 166 ALA   A CA  1 
ATOM   1170 C C   . ALA   A 1 159 ? 12.52902  -23.69778 -20.79518 1.000 27.11008 ? 166 ALA   A C   1 
ATOM   1171 O O   . ALA   A 1 159 ? 12.46030  -24.27517 -21.88952 1.000 30.56472 ? 166 ALA   A O   1 
ATOM   1172 C CB  . ALA   A 1 159 ? 11.30857  -22.50159 -18.84296 1.000 28.52483 ? 166 ALA   A CB  1 
ATOM   1173 N N   . GLY   A 1 160 ? 13.63473  -23.80534 -20.05253 1.000 30.46959 ? 167 GLY   A N   1 
ATOM   1174 C CA  . GLY   A 1 160 ? 14.72243  -24.58240 -20.63105 1.000 30.87424 ? 167 GLY   A CA  1 
ATOM   1175 C C   . GLY   A 1 160 ? 15.40114  -23.95353 -21.83610 1.000 30.10862 ? 167 GLY   A C   1 
ATOM   1176 O O   . GLY   A 1 160 ? 16.17600  -24.62676 -22.53738 1.000 31.55595 ? 167 GLY   A O   1 
ATOM   1177 N N   . GLY   A 1 161 ? 15.13111  -22.68388 -22.10658 1.000 24.26773 ? 168 GLY   A N   1 
ATOM   1178 C CA  . GLY   A 1 161 ? 15.86551  -21.93096 -23.10168 1.000 24.66997 ? 168 GLY   A CA  1 
ATOM   1179 C C   . GLY   A 1 161 ? 15.25374  -21.83292 -24.48432 1.000 26.97737 ? 168 GLY   A C   1 
ATOM   1180 O O   . GLY   A 1 161 ? 15.84215  -21.15810 -25.34086 1.000 25.47451 ? 168 GLY   A O   1 
ATOM   1181 N N   . SER   A 1 162 ? 14.10433  -22.46414 -24.74751 1.000 22.99300 ? 169 SER   A N   1 
ATOM   1182 C CA  . SER   A 1 162 ? 13.58806  -22.47088 -26.11210 1.000 22.65750 ? 169 SER   A CA  1 
ATOM   1183 C C   . SER   A 1 162 ? 12.07183  -22.39785 -26.07382 1.000 22.98713 ? 169 SER   A C   1 
ATOM   1184 O O   . SER   A 1 162 ? 11.44436  -22.69060 -25.05085 1.000 23.70488 ? 169 SER   A O   1 
ATOM   1185 C CB  . SER   A 1 162 ? 13.99679  -23.70963 -26.91449 1.000 25.68967 ? 169 SER   A CB  1 
ATOM   1186 O OG  . SER   A 1 162 ? 13.44840  -24.88918 -26.33929 1.000 25.80858 ? 169 SER   A OG  1 
ATOM   1187 N N   . PHE   A 1 163 ? 11.50867  -21.99414 -27.21147 1.000 23.66402 ? 170 PHE   A N   1 
ATOM   1188 C CA  . PHE   A 1 163 ? 10.06021  -21.96741 -27.44735 1.000 22.88257 ? 170 PHE   A CA  1 
ATOM   1189 C C   . PHE   A 1 163 ? 9.78422   -22.41257 -28.87773 1.000 25.61431 ? 170 PHE   A C   1 
ATOM   1190 O O   . PHE   A 1 163 ? 10.67874  -22.39706 -29.73399 1.000 23.71622 ? 170 PHE   A O   1 
ATOM   1191 C CB  . PHE   A 1 163 ? 9.44600   -20.57107 -27.18199 1.000 24.85704 ? 170 PHE   A CB  1 
ATOM   1192 C CG  . PHE   A 1 163 ? 9.95841   -19.47042 -28.09482 1.000 22.89115 ? 170 PHE   A CG  1 
ATOM   1193 C CD1 . PHE   A 1 163 ? 11.08629  -18.73365 -27.75552 1.000 26.51975 ? 170 PHE   A CD1 1 
ATOM   1194 C CD2 . PHE   A 1 163 ? 9.28207   -19.13550 -29.25097 1.000 22.51192 ? 170 PHE   A CD2 1 
ATOM   1195 C CE1 . PHE   A 1 163 ? 11.54254  -17.68958 -28.61280 1.000 26.31375 ? 170 PHE   A CE1 1 
ATOM   1196 C CE2 . PHE   A 1 163 ? 9.71475   -18.10983 -30.07084 1.000 23.79320 ? 170 PHE   A CE2 1 
ATOM   1197 C CZ  . PHE   A 1 163 ? 10.84245  -17.37758 -29.74750 1.000 26.94119 ? 170 PHE   A CZ  1 
ATOM   1198 N N   . THR   A 1 164 ? 8.53854   -22.86022 -29.12857 1.000 21.00343 ? 171 THR   A N   1 
ATOM   1199 C CA  . THR   A 1 164 ? 8.12552   -23.28051 -30.45963 1.000 21.73962 ? 171 THR   A CA  1 
ATOM   1200 C C   . THR   A 1 164 ? 6.99441   -22.40601 -30.94959 1.000 21.31113 ? 171 THR   A C   1 
ATOM   1201 O O   . THR   A 1 164 ? 6.22172   -21.85170 -30.15567 1.000 20.95247 ? 171 THR   A O   1 
ATOM   1202 C CB  . THR   A 1 164 ? 7.69220   -24.76349 -30.51953 1.000 25.03115 ? 171 THR   A CB  1 
ATOM   1203 O OG1 . THR   A 1 164 ? 6.57381   -24.94388 -29.63925 1.000 27.74864 ? 171 THR   A OG1 1 
ATOM   1204 C CG2 . THR   A 1 164 ? 8.83551   -25.70723 -30.12407 1.000 25.35527 ? 171 THR   A CG2 1 
ATOM   1205 N N   . VAL   A 1 165 ? 6.92059   -22.27001 -32.26786 1.000 23.14371 ? 172 VAL   A N   1 
ATOM   1206 C CA  . VAL   A 1 165 ? 5.79011   -21.59978 -32.89902 1.000 23.09019 ? 172 VAL   A CA  1 
ATOM   1207 C C   . VAL   A 1 165 ? 5.30460   -22.48788 -34.03603 1.000 27.76967 ? 172 VAL   A C   1 
ATOM   1208 O O   . VAL   A 1 165 ? 6.10602   -22.99371 -34.82955 1.000 27.37351 ? 172 VAL   A O   1 
ATOM   1209 C CB  . VAL   A 1 165 ? 6.15223   -20.19458 -33.43085 1.000 23.16830 ? 172 VAL   A CB  1 
ATOM   1210 C CG1 . VAL   A 1 165 ? 4.95365   -19.58437 -34.19356 1.000 26.08733 ? 172 VAL   A CG1 1 
ATOM   1211 C CG2 . VAL   A 1 165 ? 6.58482   -19.28069 -32.30747 1.000 22.88493 ? 172 VAL   A CG2 1 
ATOM   1212 N N   . ARG   A 1 166 ? 3.98806   -22.64981 -34.14368 1.000 23.31273 ? 173 ARG   A N   1 
ATOM   1213 C CA  . ARG   A 1 166 ? 3.42297   -23.41955 -35.24557 1.000 25.64671 ? 173 ARG   A CA  1 
ATOM   1214 C C   . ARG   A 1 166 ? 2.07266   -22.83351 -35.61107 1.000 27.84010 ? 173 ARG   A C   1 
ATOM   1215 O O   . ARG   A 1 166 ? 1.43382   -22.18171 -34.78492 1.000 26.71881 ? 173 ARG   A O   1 
ATOM   1216 C CB  . ARG   A 1 166 ? 3.27575   -24.90326 -34.88726 1.000 33.52290 ? 173 ARG   A CB  1 
ATOM   1217 C CG  . ARG   A 1 166 ? 2.14397   -25.19602 -33.90814 1.000 35.74088 ? 173 ARG   A CG  1 
ATOM   1218 C CD  . ARG   A 1 166 ? 2.32737   -26.55740 -33.19861 1.000 39.22855 ? 173 ARG   A CD  1 
ATOM   1219 N NE  . ARG   A 1 166 ? 3.38864   -26.53289 -32.19455 1.000 40.99292 ? 173 ARG   A NE  1 
ATOM   1220 C CZ  . ARG   A 1 166 ? 4.01029   -27.60987 -31.72338 1.000 48.86439 ? 173 ARG   A CZ  1 
ATOM   1221 N NH1 . ARG   A 1 166 ? 3.63997   -28.83239 -32.07220 1.000 43.98970 ? 173 ARG   A NH1 1 
ATOM   1222 N NH2 . ARG   A 1 166 ? 5.03054   -27.45664 -30.87921 1.000 45.25345 ? 173 ARG   A NH2 1 
ATOM   1223 N N   . THR   A 1 167 ? 1.65384   -23.07321 -36.85858 1.000 29.69263 ? 174 THR   A N   1 
ATOM   1224 C CA  . THR   A 1 167 ? 0.27684   -22.78166 -37.25276 1.000 28.24416 ? 174 THR   A CA  1 
ATOM   1225 C C   . THR   A 1 167 ? -0.66665  -23.63444 -36.41898 1.000 33.72549 ? 174 THR   A C   1 
ATOM   1226 O O   . THR   A 1 167 ? -0.38756  -24.80295 -36.14149 1.000 36.65720 ? 174 THR   A O   1 
ATOM   1227 C CB  . THR   A 1 167 ? 0.08519   -23.05124 -38.74776 1.000 38.68753 ? 174 THR   A CB  1 
ATOM   1228 O OG1 . THR   A 1 167 ? 0.82181   -22.07182 -39.48782 1.000 38.53504 ? 174 THR   A OG1 1 
ATOM   1229 C CG2 . THR   A 1 167 ? -1.36957  -22.97103 -39.12735 1.000 43.67866 ? 174 THR   A CG2 1 
ATOM   1230 N N   . ASP   A 1 168 ? -1.76265  -23.03335 -35.95795 1.000 32.71207 ? 175 ASP   A N   1 
ATOM   1231 C CA  . ASP   A 1 168 ? -2.68606  -23.73146 -35.07945 1.000 37.31630 ? 175 ASP   A CA  1 
ATOM   1232 C C   . ASP   A 1 168 ? -3.86967  -24.20226 -35.90091 1.000 42.34682 ? 175 ASP   A C   1 
ATOM   1233 O O   . ASP   A 1 168 ? -4.58549  -23.38623 -36.48497 1.000 44.34600 ? 175 ASP   A O   1 
ATOM   1234 C CB  . ASP   A 1 168 ? -3.15915  -22.84461 -33.93009 1.000 33.52239 ? 175 ASP   A CB  1 
ATOM   1235 C CG  . ASP   A 1 168 ? -4.09559  -23.58116 -32.98447 1.000 46.38247 ? 175 ASP   A CG  1 
ATOM   1236 O OD1 . ASP   A 1 168 ? -3.80793  -24.75164 -32.63998 1.000 51.14046 ? 175 ASP   A OD1 1 
ATOM   1237 O OD2 . ASP   A 1 168 ? -5.14548  -23.00946 -32.62201 1.000 41.64728 ? 175 ASP   A OD2 1 
ATOM   1238 N N   . THR   A 1 169 ? -4.05991  -25.51505 -35.94523 1.000 49.09330 ? 176 THR   A N   1 
ATOM   1239 C CA  . THR   A 1 169 ? -5.16804  -26.14232 -36.64640 1.000 56.60402 ? 176 THR   A CA  1 
ATOM   1240 C C   . THR   A 1 169 ? -6.34506  -26.44031 -35.72354 1.000 55.49164 ? 176 THR   A C   1 
ATOM   1241 O O   . THR   A 1 169 ? -7.32478  -27.05255 -36.16300 1.000 56.33669 ? 176 THR   A O   1 
ATOM   1242 C CB  . THR   A 1 169 ? -4.68482  -27.42975 -37.31523 1.000 55.09340 ? 176 THR   A CB  1 
ATOM   1243 O OG1 . THR   A 1 169 ? -3.97883  -28.22180 -36.34476 1.000 59.65067 ? 176 THR   A OG1 1 
ATOM   1244 C CG2 . THR   A 1 169 ? -3.75577  -27.10376 -38.48663 1.000 54.65469 ? 176 THR   A CG2 1 
ATOM   1245 N N   . GLY   A 1 170 ? -6.26289  -26.03175 -34.45656 1.000 53.38313 ? 177 GLY   A N   1 
ATOM   1246 C CA  . GLY   A 1 170 ? -7.33214  -26.23604 -33.50153 1.000 55.91160 ? 177 GLY   A CA  1 
ATOM   1247 C C   . GLY   A 1 170 ? -8.52799  -25.32915 -33.73562 1.000 49.87163 ? 177 GLY   A C   1 
ATOM   1248 O O   . GLY   A 1 170 ? -8.70101  -24.72619 -34.79952 1.000 50.71286 ? 177 GLY   A O   1 
ATOM   1249 N N   . GLU   A 1 171 ? -9.37228  -25.25146 -32.70905 1.000 50.51803 ? 178 GLU   A N   1 
ATOM   1250 C CA  . GLU   A 1 171 ? -10.59833 -24.46595 -32.71392 1.000 44.43273 ? 178 GLU   A CA  1 
ATOM   1251 C C   . GLU   A 1 171 ? -10.32651 -23.02486 -33.14589 1.000 42.05733 ? 178 GLU   A C   1 
ATOM   1252 O O   . GLU   A 1 171 ? -9.52751  -22.33506 -32.49714 1.000 37.83417 ? 178 GLU   A O   1 
ATOM   1253 C CB  . GLU   A 1 171 ? -11.20654 -24.49578 -31.30810 1.000 47.84126 ? 178 GLU   A CB  1 
ATOM   1254 C CG  . GLU   A 1 171 ? -12.72648 -24.61899 -31.21294 1.000 47.00763 ? 178 GLU   A CG  1 
ATOM   1255 C CD  . GLU   A 1 171 ? -13.32224 -25.64030 -32.17386 1.000 47.84702 ? 178 GLU   A CD  1 
ATOM   1256 O OE1 . GLU   A 1 171 ? -13.85234 -25.22435 -33.23130 1.000 50.72055 ? 178 GLU   A OE1 1 
ATOM   1257 O OE2 . GLU   A 1 171 ? -13.21539 -26.85710 -31.89732 1.000 51.03977 ? 178 GLU   A OE2 1 
ATOM   1258 N N   . PRO   A 1 172 ? -10.94744 -22.54428 -34.22621 1.000 39.97212 ? 179 PRO   A N   1 
ATOM   1259 C CA  . PRO   A 1 172 ? -10.75727 -21.14669 -34.63830 1.000 40.15027 ? 179 PRO   A CA  1 
ATOM   1260 C C   . PRO   A 1 172 ? -11.18854 -20.18519 -33.54140 1.000 42.58380 ? 179 PRO   A C   1 
ATOM   1261 O O   . PRO   A 1 172 ? -12.20766 -20.39148 -32.87744 1.000 45.77747 ? 179 PRO   A O   1 
ATOM   1262 C CB  . PRO   A 1 172 ? -11.65908 -21.01652 -35.86987 1.000 43.77426 ? 179 PRO   A CB  1 
ATOM   1263 C CG  . PRO   A 1 172 ? -11.71668 -22.39658 -36.44163 1.000 45.09988 ? 179 PRO   A CG  1 
ATOM   1264 C CD  . PRO   A 1 172 ? -11.63806 -23.34383 -35.25899 1.000 46.54054 ? 179 PRO   A CD  1 
ATOM   1265 N N   . MET   A 1 173 ? -10.41234 -19.11405 -33.36607 1.000 36.92534 ? 180 MET   A N   1 
ATOM   1266 C CA  . MET   A 1 173 ? -10.64637 -18.17036 -32.28322 1.000 35.06874 ? 180 MET   A CA  1 
ATOM   1267 C C   . MET   A 1 173 ? -11.35032 -16.88531 -32.69531 1.000 41.61105 ? 180 MET   A C   1 
ATOM   1268 O O   . MET   A 1 173 ? -11.90323 -16.19926 -31.82624 1.000 47.56543 ? 180 MET   A O   1 
ATOM   1269 C CB  . MET   A 1 173 ? -9.32070  -17.77409 -31.64151 1.000 37.25997 ? 180 MET   A CB  1 
ATOM   1270 C CG  . MET   A 1 173 ? -8.79384  -18.74570 -30.64923 1.000 47.39978 ? 180 MET   A CG  1 
ATOM   1271 S SD  . MET   A 1 173 ? -7.23626  -18.02223 -30.16709 1.000 47.81389 ? 180 MET   A SD  1 
ATOM   1272 C CE  . MET   A 1 173 ? -7.82689  -16.44048 -29.61418 1.000 38.85550 ? 180 MET   A CE  1 
ATOM   1273 N N   . GLY   A 1 174 ? -11.28879 -16.49518 -33.95575 1.000 38.80802 ? 181 GLY   A N   1 
ATOM   1274 C CA  . GLY   A 1 174 ? -11.92385 -15.24077 -34.31829 1.000 33.51802 ? 181 GLY   A CA  1 
ATOM   1275 C C   . GLY   A 1 174 ? -10.96179 -14.08034 -34.17790 1.000 32.34995 ? 181 GLY   A C   1 
ATOM   1276 O O   . GLY   A 1 174 ? -10.49247 -13.54835 -35.18389 1.000 30.30192 ? 181 GLY   A O   1 
ATOM   1277 N N   . ARG   A 1 175 ? -10.64478 -13.69957 -32.93504 1.000 25.15511 ? 182 ARG   A N   1 
ATOM   1278 C CA  . ARG   A 1 175 ? -9.63557  -12.68621 -32.62487 1.000 24.72811 ? 182 ARG   A CA  1 
ATOM   1279 C C   . ARG   A 1 175 ? -9.33353  -12.74614 -31.13495 1.000 24.92127 ? 182 ARG   A C   1 
ATOM   1280 O O   . ARG   A 1 175 ? -10.25713 -12.86315 -30.33439 1.000 27.54005 ? 182 ARG   A O   1 
ATOM   1281 C CB  . ARG   A 1 175 ? -10.11493 -11.26932 -32.99910 1.000 25.54331 ? 182 ARG   A CB  1 
ATOM   1282 C CG  . ARG   A 1 175 ? -9.01953  -10.19089 -32.82752 1.000 26.34692 ? 182 ARG   A CG  1 
ATOM   1283 C CD  . ARG   A 1 175 ? -9.60061  -8.76752  -32.73190 1.000 23.09021 ? 182 ARG   A CD  1 
ATOM   1284 N NE  . ARG   A 1 175 ? -10.53058 -8.63004  -31.60598 1.000 24.39457 ? 182 ARG   A NE  1 
ATOM   1285 C CZ  . ARG   A 1 175 ? -11.84878 -8.52663  -31.70352 1.000 26.92034 ? 182 ARG   A CZ  1 
ATOM   1286 N NH1 . ARG   A 1 175 ? -12.46710 -8.50976  -32.88391 1.000 25.62807 ? 182 ARG   A NH1 1 
ATOM   1287 N NH2 . ARG   A 1 175 ? -12.57275 -8.41668  -30.59082 1.000 24.71724 ? 182 ARG   A NH2 1 
ATOM   1288 N N   . GLY   A 1 176 ? -8.05177  -12.68248 -30.76361 1.000 23.88294 ? 183 GLY   A N   1 
ATOM   1289 C CA  . GLY   A 1 176 ? -7.73152  -12.58174 -29.34944 1.000 23.07527 ? 183 GLY   A CA  1 
ATOM   1290 C C   . GLY   A 1 176 ? -6.57766  -13.47842 -28.98987 1.000 25.74788 ? 183 GLY   A C   1 
ATOM   1291 O O   . GLY   A 1 176 ? -5.80932  -13.89477 -29.85374 1.000 23.50489 ? 183 GLY   A O   1 
ATOM   1292 N N   . THR   A 1 177 ? -6.48251  -13.78293 -27.69657 1.000 21.75797 ? 184 THR   A N   1 
ATOM   1293 C CA  . THR   A 1 177 ? -5.38662  -14.58913 -27.17233 1.000 21.17973 ? 184 THR   A CA  1 
ATOM   1294 C C   . THR   A 1 177 ? -5.89696  -15.52902 -26.09955 1.000 24.53448 ? 184 THR   A C   1 
ATOM   1295 O O   . THR   A 1 177 ? -6.73524  -15.14073 -25.26982 1.000 23.20284 ? 184 THR   A O   1 
ATOM   1296 C CB  . THR   A 1 177 ? -4.27836  -13.68325 -26.60192 1.000 24.43941 ? 184 THR   A CB  1 
ATOM   1297 O OG1 . THR   A 1 177 ? -3.73066  -12.90234 -27.66439 1.000 26.29191 ? 184 THR   A OG1 1 
ATOM   1298 C CG2 . THR   A 1 177 ? -3.16472  -14.49007 -25.89084 1.000 26.54707 ? 184 THR   A CG2 1 
ATOM   1299 N N   . LYS   A 1 178 ? -5.38541  -16.76271 -26.11576 1.000 20.88547 ? 185 LYS   A N   1 
ATOM   1300 C CA  . LYS   A 1 178 ? -5.68687  -17.76327 -25.09329 1.000 21.89957 ? 185 LYS   A CA  1 
ATOM   1301 C C   . LYS   A 1 178 ? -4.36516  -18.17146 -24.46084 1.000 21.17774 ? 185 LYS   A C   1 
ATOM   1302 O O   . LYS   A 1 178 ? -3.47429  -18.63730 -25.17507 1.000 24.53405 ? 185 LYS   A O   1 
ATOM   1303 C CB  . LYS   A 1 178 ? -6.35469  -18.97235 -25.74950 1.000 26.95179 ? 185 LYS   A CB  1 
ATOM   1304 C CG  . LYS   A 1 178 ? -6.66110  -20.13838 -24.88158 1.000 35.29342 ? 185 LYS   A CG  1 
ATOM   1305 C CD  . LYS   A 1 178 ? -7.44522  -21.20299 -25.69336 1.000 40.25321 ? 185 LYS   A CD  1 
ATOM   1306 C CE  . LYS   A 1 178 ? -8.37389  -20.57289 -26.70532 1.000 43.44718 ? 185 LYS   A CE  1 
ATOM   1307 N NZ  . LYS   A 1 178 ? -9.32692  -21.59276 -27.24757 1.000 54.40197 ? 185 LYS   A NZ  1 
ATOM   1308 N N   . VAL   A 1 179 ? -4.22383  -17.98869 -23.14691 1.000 21.32520 ? 186 VAL   A N   1 
ATOM   1309 C CA  . VAL   A 1 179 ? -3.02252  -18.43672 -22.42336 1.000 21.04741 ? 186 VAL   A CA  1 
ATOM   1310 C C   . VAL   A 1 179 ? -3.40653  -19.67877 -21.62724 1.000 21.89869 ? 186 VAL   A C   1 
ATOM   1311 O O   . VAL   A 1 179 ? -4.25959  -19.59766 -20.73251 1.000 22.52128 ? 186 VAL   A O   1 
ATOM   1312 C CB  . VAL   A 1 179 ? -2.48827  -17.34220 -21.48662 1.000 21.11188 ? 186 VAL   A CB  1 
ATOM   1313 C CG1 . VAL   A 1 179 ? -1.28483  -17.88899 -20.64386 1.000 22.80251 ? 186 VAL   A CG1 1 
ATOM   1314 C CG2 . VAL   A 1 179 ? -2.04627  -16.11970 -22.26968 1.000 22.97799 ? 186 VAL   A CG2 1 
ATOM   1315 N N   . ILE   A 1 180 ? -2.80476  -20.82631 -21.96684 1.000 21.19112 ? 187 ILE   A N   1 
ATOM   1316 C CA  . ILE   A 1 180 ? -3.11815  -22.11601 -21.34693 1.000 20.92411 ? 187 ILE   A CA  1 
ATOM   1317 C C   . ILE   A 1 180 ? -1.98807  -22.42257 -20.37772 1.000 22.40784 ? 187 ILE   A C   1 
ATOM   1318 O O   . ILE   A 1 180 ? -0.85170  -22.63098 -20.81046 1.000 21.90784 ? 187 ILE   A O   1 
ATOM   1319 C CB  . ILE   A 1 180 ? -3.26120  -23.24230 -22.38419 1.000 23.09835 ? 187 ILE   A CB  1 
ATOM   1320 C CG1 . ILE   A 1 180 ? -4.30037  -22.84175 -23.44366 1.000 23.05632 ? 187 ILE   A CG1 1 
ATOM   1321 C CG2 . ILE   A 1 180 ? -3.63937  -24.55432 -21.66240 1.000 23.31443 ? 187 ILE   A CG2 1 
ATOM   1322 C CD1 . ILE   A 1 180 ? -4.36476  -23.80631 -24.63853 1.000 29.47335 ? 187 ILE   A CD1 1 
ATOM   1323 N N   . LEU   A 1 181 ? -2.27998  -22.42253 -19.07353 1.000 20.92354 ? 188 LEU   A N   1 
ATOM   1324 C CA  . LEU   A 1 181 ? -1.28372  -22.72877 -18.04830 1.000 21.12584 ? 188 LEU   A CA  1 
ATOM   1325 C C   . LEU   A 1 181 ? -1.39335  -24.20690 -17.71046 1.000 23.55094 ? 188 LEU   A C   1 
ATOM   1326 O O   . LEU   A 1 181 ? -2.40645  -24.64280 -17.15026 1.000 24.57915 ? 188 LEU   A O   1 
ATOM   1327 C CB  . LEU   A 1 181 ? -1.50392  -21.87473 -16.80028 1.000 20.92423 ? 188 LEU   A CB  1 
ATOM   1328 C CG  . LEU   A 1 181 ? -1.62422  -20.38684 -17.08262 1.000 21.57012 ? 188 LEU   A CG  1 
ATOM   1329 C CD1 . LEU   A 1 181 ? -1.98467  -19.72289 -15.74860 1.000 24.03248 ? 188 LEU   A CD1 1 
ATOM   1330 C CD2 . LEU   A 1 181 ? -0.30523  -19.86089 -17.61616 1.000 23.97946 ? 188 LEU   A CD2 1 
ATOM   1331 N N   . HIS   A 1 182 ? -0.34780  -24.98088 -18.02700 1.000 23.31598 ? 189 HIS   A N   1 
ATOM   1332 C CA  . HIS   A 1 182 ? -0.27804  -26.38549 -17.61055 1.000 26.28730 ? 189 HIS   A CA  1 
ATOM   1333 C C   . HIS   A 1 182 ? 0.34524   -26.40215 -16.21549 1.000 25.62191 ? 189 HIS   A C   1 
ATOM   1334 O O   . HIS   A 1 182 ? 1.54639   -26.21210 -16.06333 1.000 26.04210 ? 189 HIS   A O   1 
ATOM   1335 C CB  . HIS   A 1 182 ? 0.52377   -27.20572 -18.61870 1.000 24.90271 ? 189 HIS   A CB  1 
ATOM   1336 C CG  . HIS   A 1 182 ? 0.01993   -27.09299 -20.03078 1.000 28.54272 ? 189 HIS   A CG  1 
ATOM   1337 N ND1 . HIS   A 1 182 ? -0.81048  -28.03793 -20.59947 1.000 33.54651 ? 189 HIS   A ND1 1 
ATOM   1338 C CD2 . HIS   A 1 182 ? 0.22345   -26.14805 -20.98203 1.000 26.96110 ? 189 HIS   A CD2 1 
ATOM   1339 C CE1 . HIS   A 1 182 ? -1.09555  -27.68302 -21.84393 1.000 30.15280 ? 189 HIS   A CE1 1 
ATOM   1340 N NE2 . HIS   A 1 182 ? -0.47683  -26.54240 -22.10385 1.000 32.17377 ? 189 HIS   A NE2 1 
ATOM   1341 N N   . LEU   A 1 183 ? -0.48133  -26.54666 -15.18212 1.000 24.23809 ? 190 LEU   A N   1 
ATOM   1342 C CA  . LEU   A 1 183 ? -0.05072  -26.20562 -13.82762 1.000 24.44626 ? 190 LEU   A CA  1 
ATOM   1343 C C   . LEU   A 1 183 ? 0.90652   -27.24888 -13.26531 1.000 27.37401 ? 190 LEU   A C   1 
ATOM   1344 O O   . LEU   A 1 183 ? 0.80335   -28.44274 -13.56084 1.000 27.83840 ? 190 LEU   A O   1 
ATOM   1345 C CB  . LEU   A 1 183 ? -1.26783  -26.09891 -12.90187 1.000 24.84063 ? 190 LEU   A CB  1 
ATOM   1346 C CG  . LEU   A 1 183 ? -2.20121  -24.92247 -13.22057 1.000 25.78469 ? 190 LEU   A CG  1 
ATOM   1347 C CD1 . LEU   A 1 183 ? -3.33012  -24.85761 -12.19000 1.000 26.63849 ? 190 LEU   A CD1 1 
ATOM   1348 C CD2 . LEU   A 1 183 ? -1.43712  -23.64262 -13.20900 1.000 26.27186 ? 190 LEU   A CD2 1 
ATOM   1349 N N   . LYS   A 1 184 ? 1.85772   -26.78211 -12.45189 1.000 26.09924 ? 191 LYS   A N   1 
ATOM   1350 C CA  . LYS   A 1 184 ? 2.68636   -27.69442 -11.67776 1.000 28.18319 ? 191 LYS   A CA  1 
ATOM   1351 C C   . LYS   A 1 184 ? 1.81969   -28.52079 -10.73542 1.000 32.23281 ? 191 LYS   A C   1 
ATOM   1352 O O   . LYS   A 1 184 ? 0.74128   -28.10496 -10.30477 1.000 30.95504 ? 191 LYS   A O   1 
ATOM   1353 C CB  . LYS   A 1 184 ? 3.74426   -26.93851 -10.85881 1.000 30.83200 ? 191 LYS   A CB  1 
ATOM   1354 C CG  . LYS   A 1 184 ? 4.74890   -26.11669 -11.66707 1.000 34.43899 ? 191 LYS   A CG  1 
ATOM   1355 C CD  . LYS   A 1 184 ? 5.42768   -25.05732 -10.78424 1.000 35.90254 ? 191 LYS   A CD  1 
ATOM   1356 C CE  . LYS   A 1 184 ? 6.31342   -24.10154 -11.58319 1.000 39.08334 ? 191 LYS   A CE  1 
ATOM   1357 N NZ  . LYS   A 1 184 ? 7.14423   -23.16179 -10.71387 1.000 42.17374 ? 191 LYS   A NZ  1 
ATOM   1358 N N   . GLU   A 1 185 ? 2.33162   -29.69943 -10.39017 1.000 31.56702 ? 192 GLU   A N   1 
ATOM   1359 C CA  . GLU   A 1 185 ? 1.55837   -30.64721 -9.59906  1.000 34.62767 ? 192 GLU   A CA  1 
ATOM   1360 C C   . GLU   A 1 185 ? 1.14335   -30.07755 -8.24562  1.000 36.78923 ? 192 GLU   A C   1 
ATOM   1361 O O   . GLU   A 1 185 ? 0.09584   -30.46189 -7.71369  1.000 35.50873 ? 192 GLU   A O   1 
ATOM   1362 C CB  . GLU   A 1 185 ? 2.38067   -31.92087 -9.40646  1.000 42.93569 ? 192 GLU   A CB  1 
ATOM   1363 C CG  . GLU   A 1 185 ? 1.59400   -33.12093 -8.97520  1.000 49.72264 ? 192 GLU   A CG  1 
ATOM   1364 C CD  . GLU   A 1 185 ? 2.49611   -34.33435 -8.79893  1.000 65.90582 ? 192 GLU   A CD  1 
ATOM   1365 O OE1 . GLU   A 1 185 ? 3.66678   -34.14244 -8.38779  1.000 69.86762 ? 192 GLU   A OE1 1 
ATOM   1366 O OE2 . GLU   A 1 185 ? 2.03748   -35.47008 -9.07019  1.000 69.64554 ? 192 GLU   A OE2 1 
ATOM   1367 N N   . ASP   A 1 186 ? 1.93743   -29.17857 -7.65995  1.000 32.51154 ? 193 ASP   A N   1 
ATOM   1368 C CA  . ASP   A 1 186 ? 1.61656   -28.68253 -6.32885  1.000 33.86278 ? 193 ASP   A CA  1 
ATOM   1369 C C   . ASP   A 1 186 ? 0.93321   -27.32145 -6.37216  1.000 31.64834 ? 193 ASP   A C   1 
ATOM   1370 O O   . ASP   A 1 186 ? 0.82099   -26.66220 -5.33238  1.000 29.87617 ? 193 ASP   A O   1 
ATOM   1371 C CB  . ASP   A 1 186 ? 2.87178   -28.60218 -5.46491  1.000 32.70437 ? 193 ASP   A CB  1 
ATOM   1372 C CG  . ASP   A 1 186 ? 3.97858   -27.79310 -6.10444  1.000 42.29428 ? 193 ASP   A CG  1 
ATOM   1373 O OD1 . ASP   A 1 186 ? 4.01210   -27.66532 -7.35073  1.000 48.14578 ? 193 ASP   A OD1 1 
ATOM   1374 O OD2 . ASP   A 1 186 ? 4.86502   -27.32511 -5.35270  1.000 45.22877 ? 193 ASP   A OD2 1 
ATOM   1375 N N   . GLN   A 1 187 ? 0.44015   -26.90577 -7.54208  1.000 27.58099 ? 194 GLN   A N   1 
ATOM   1376 C CA  . GLN   A 1 187 ? -0.17553  -25.60121 -7.71492  1.000 26.23165 ? 194 GLN   A CA  1 
ATOM   1377 C C   . GLN   A 1 187 ? -1.62917  -25.73034 -8.16192  1.000 25.88974 ? 194 GLN   A C   1 
ATOM   1378 O O   . GLN   A 1 187 ? -2.16654  -24.82801 -8.80661  1.000 25.04657 ? 194 GLN   A O   1 
ATOM   1379 C CB  . GLN   A 1 187 ? 0.62553   -24.75394 -8.71174  1.000 29.22931 ? 194 GLN   A CB  1 
ATOM   1380 C CG  . GLN   A 1 187 ? 2.08203   -24.48341 -8.27011  1.000 26.81826 ? 194 GLN   A CG  1 
ATOM   1381 C CD  . GLN   A 1 187 ? 2.17055   -23.77576 -6.93312  1.000 31.85614 ? 194 GLN   A CD  1 
ATOM   1382 O OE1 . GLN   A 1 187 ? 1.36860   -22.89370 -6.63321  1.000 31.52647 ? 194 GLN   A OE1 1 
ATOM   1383 N NE2 . GLN   A 1 187 ? 3.16297   -24.14510 -6.12981  1.000 32.53209 ? 194 GLN   A NE2 1 
ATOM   1384 N N   . THR   A 1 188 ? -2.29069  -26.82704 -7.81567  1.000 27.77295 ? 195 THR   A N   1 
ATOM   1385 C CA  . THR   A 1 188 ? -3.65765  -27.02173 -8.30286  1.000 31.78099 ? 195 THR   A CA  1 
ATOM   1386 C C   . THR   A 1 188 ? -4.70792  -26.23474 -7.52200  1.000 30.19402 ? 195 THR   A C   1 
ATOM   1387 O O   . THR   A 1 188 ? -5.88944  -26.28268 -7.90239  1.000 30.46621 ? 195 THR   A O   1 
ATOM   1388 C CB  . THR   A 1 188 ? -4.04237  -28.50622 -8.28236  1.000 34.49491 ? 195 THR   A CB  1 
ATOM   1389 O OG1 . THR   A 1 188 ? -3.93859  -29.01449 -6.94651  1.000 37.83881 ? 195 THR   A OG1 1 
ATOM   1390 C CG2 . THR   A 1 188 ? -3.14486  -29.29653 -9.20268  1.000 33.55699 ? 195 THR   A CG2 1 
ATOM   1391 N N   . GLU   A 1 189 ? -4.33032  -25.51097 -6.45668  1.000 30.20436 ? 196 GLU   A N   1 
ATOM   1392 C CA  . GLU   A 1 189 ? -5.29321  -24.61063 -5.81728  1.000 28.72075 ? 196 GLU   A CA  1 
ATOM   1393 C C   . GLU   A 1 189 ? -5.85103  -23.58802 -6.79098  1.000 28.01540 ? 196 GLU   A C   1 
ATOM   1394 O O   . GLU   A 1 189 ? -6.96919  -23.10099 -6.59686  1.000 26.93795 ? 196 GLU   A O   1 
ATOM   1395 C CB  . GLU   A 1 189 ? -4.66764  -23.88635 -4.61972  1.000 31.14470 ? 196 GLU   A CB  1 
ATOM   1396 C CG  . GLU   A 1 189 ? -3.58367  -22.90113 -5.02607  1.000 28.49276 ? 196 GLU   A CG  1 
ATOM   1397 C CD  . GLU   A 1 189 ? -2.82173  -22.38914 -3.83053  1.000 36.12024 ? 196 GLU   A CD  1 
ATOM   1398 O OE1 . GLU   A 1 189 ? -1.90034  -23.11362 -3.40088  1.000 35.61863 ? 196 GLU   A OE1 1 
ATOM   1399 O OE2 . GLU   A 1 189 ? -3.10706  -21.26666 -3.34454  1.000 33.46066 ? 196 GLU   A OE2 1 
ATOM   1400 N N   . TYR   A 1 190 ? -5.09521  -23.23667 -7.82775  1.000 26.14046 ? 197 TYR   A N   1 
ATOM   1401 C CA  . TYR   A 1 190 ? -5.52270  -22.24594 -8.81785  1.000 24.47734 ? 197 TYR   A CA  1 
ATOM   1402 C C   . TYR   A 1 190 ? -6.54486  -22.79716 -9.80981  1.000 26.50226 ? 197 TYR   A C   1 
ATOM   1403 O O   . TYR   A 1 190 ? -6.91626  -22.09328 -10.76500 1.000 26.73420 ? 197 TYR   A O   1 
ATOM   1404 C CB  . TYR   A 1 190 ? -4.28414  -21.67204 -9.53499  1.000 23.79451 ? 197 TYR   A CB  1 
ATOM   1405 C CG  . TYR   A 1 190 ? -3.38394  -21.00942 -8.51750  1.000 23.98676 ? 197 TYR   A CG  1 
ATOM   1406 C CD1 . TYR   A 1 190 ? -3.82026  -19.89733 -7.81045  1.000 26.86887 ? 197 TYR   A CD1 1 
ATOM   1407 C CD2 . TYR   A 1 190 ? -2.13674  -21.53705 -8.20382  1.000 25.69083 ? 197 TYR   A CD2 1 
ATOM   1408 C CE1 . TYR   A 1 190 ? -3.03268  -19.32078 -6.83558  1.000 29.72130 ? 197 TYR   A CE1 1 
ATOM   1409 C CE2 . TYR   A 1 190 ? -1.34931  -20.96683 -7.23449  1.000 28.43079 ? 197 TYR   A CE2 1 
ATOM   1410 C CZ  . TYR   A 1 190 ? -1.80895  -19.85026 -6.55586  1.000 27.93597 ? 197 TYR   A CZ  1 
ATOM   1411 O OH  . TYR   A 1 190 ? -1.04481  -19.26861 -5.57311  1.000 28.52178 ? 197 TYR   A OH  1 
ATOM   1412 N N   . LEU   A 1 191 ? -7.01139  -24.02595 -9.60192  1.000 26.09413 ? 198 LEU   A N   1 
ATOM   1413 C CA  . LEU   A 1 191 ? -8.15975  -24.55554 -10.32147 1.000 27.04839 ? 198 LEU   A CA  1 
ATOM   1414 C C   . LEU   A 1 191 ? -9.43746  -24.51883 -9.50024  1.000 30.16780 ? 198 LEU   A C   1 
ATOM   1415 O O   . LEU   A 1 191 ? -10.49865 -24.85935 -10.03703 1.000 32.52814 ? 198 LEU   A O   1 
ATOM   1416 C CB  . LEU   A 1 191 ? -7.91074  -26.00754 -10.74663 1.000 26.16526 ? 198 LEU   A CB  1 
ATOM   1417 C CG  . LEU   A 1 191 ? -6.68653  -26.19556 -11.63300 1.000 26.65281 ? 198 LEU   A CG  1 
ATOM   1418 C CD1 . LEU   A 1 191 ? -6.41878  -27.68348 -11.86937 1.000 30.98850 ? 198 LEU   A CD1 1 
ATOM   1419 C CD2 . LEU   A 1 191 ? -6.85979  -25.43319 -12.93263 1.000 28.30819 ? 198 LEU   A CD2 1 
ATOM   1420 N N   . GLU   A 1 192 ? -9.36280  -24.19719 -8.20974  1.000 27.76797 ? 199 GLU   A N   1 
ATOM   1421 C CA  . GLU   A 1 192 ? -10.55678 -24.21268 -7.37202  1.000 30.03421 ? 199 GLU   A CA  1 
ATOM   1422 C C   . GLU   A 1 192 ? -11.29367 -22.88207 -7.47822  1.000 30.59639 ? 199 GLU   A C   1 
ATOM   1423 O O   . GLU   A 1 192 ? -10.68793 -21.80704 -7.44627  1.000 27.55569 ? 199 GLU   A O   1 
ATOM   1424 C CB  . GLU   A 1 192 ? -10.23560 -24.54186 -5.90714  1.000 35.01846 ? 199 GLU   A CB  1 
ATOM   1425 C CG  . GLU   A 1 192 ? -9.24347  -25.69859 -5.69124  1.000 36.67238 ? 199 GLU   A CG  1 
ATOM   1426 C CD  . GLU   A 1 192 ? -8.75622  -25.81799 -4.24506  1.000 52.56151 ? 199 GLU   A CD  1 
ATOM   1427 O OE1 . GLU   A 1 192 ? -9.17819  -24.99956 -3.38614  1.000 64.54441 ? 199 GLU   A OE1 1 
ATOM   1428 O OE2 . GLU   A 1 192 ? -7.94994  -26.73944 -3.95994  1.000 57.34481 ? 199 GLU   A OE2 1 
ATOM   1429 N N   . GLU   A 1 193 ? -12.61704 -22.96929 -7.63699  1.000 27.59330 ? 200 GLU   A N   1 
ATOM   1430 C CA  . GLU   A 1 193 ? -13.41158 -21.77328 -7.88575  1.000 27.36537 ? 200 GLU   A CA  1 
ATOM   1431 C C   . GLU   A 1 193 ? -13.21961 -20.72881 -6.78178  1.000 27.94160 ? 200 GLU   A C   1 
ATOM   1432 O O   . GLU   A 1 193 ? -13.05329 -19.53187 -7.06291  1.000 26.59857 ? 200 GLU   A O   1 
ATOM   1433 C CB  . GLU   A 1 193 ? -14.88654 -22.17334 -7.99121  1.000 33.76409 ? 200 GLU   A CB  1 
ATOM   1434 C CG  . GLU   A 1 193 ? -15.83420 -20.99417 -7.94616  1.000 37.20676 ? 200 GLU   A CG  1 
ATOM   1435 C CD  . GLU   A 1 193 ? -17.27300 -21.33151 -8.35111  1.000 49.36068 ? 200 GLU   A CD  1 
ATOM   1436 O OE1 . GLU   A 1 193 ? -17.74441 -22.41277 -7.94525  1.000 45.75973 ? 200 GLU   A OE1 1 
ATOM   1437 O OE2 . GLU   A 1 193 ? -17.94802 -20.49471 -9.00396  1.000 52.46129 ? 200 GLU   A OE2 1 
ATOM   1438 N N   . ARG   A 1 194 ? -13.23687 -21.15868 -5.52128  1.000 31.30462 ? 201 ARG   A N   1 
ATOM   1439 C CA  . ARG   A 1 194 ? -13.18959 -20.17152 -4.44322  1.000 26.54365 ? 201 ARG   A CA  1 
ATOM   1440 C C   . ARG   A 1 194 ? -11.84437 -19.45598 -4.40142  1.000 26.58602 ? 201 ARG   A C   1 
ATOM   1441 O O   . ARG   A 1 194 ? -11.78659 -18.28378 -4.01394  1.000 26.89143 ? 201 ARG   A O   1 
ATOM   1442 C CB  . ARG   A 1 194 ? -13.52293 -20.83683 -3.11034  1.000 35.79904 ? 201 ARG   A CB  1 
ATOM   1443 C CG  . ARG   A 1 194 ? -12.64580 -21.97818 -2.74155  1.000 33.48031 ? 201 ARG   A CG  1 
ATOM   1444 C CD  . ARG   A 1 194 ? -12.98940 -22.35147 -1.30571  1.000 38.81109 ? 201 ARG   A CD  1 
ATOM   1445 N NE  . ARG   A 1 194 ? -12.04007 -23.29128 -0.74189  1.000 47.74240 ? 201 ARG   A NE  1 
ATOM   1446 C CZ  . ARG   A 1 194 ? -12.24979 -23.90855 0.41158   1.000 42.11494 ? 201 ARG   A CZ  1 
ATOM   1447 N NH1 . ARG   A 1 194 ? -13.36919 -23.71633 1.09844   1.000 45.32792 ? 201 ARG   A NH1 1 
ATOM   1448 N NH2 . ARG   A 1 194 ? -11.31802 -24.72999 0.88685   1.000 51.07981 ? 201 ARG   A NH2 1 
ATOM   1449 N N   . ARG   A 1 195 ? -10.75948 -20.14995 -4.78082  1.000 25.98195 ? 202 ARG   A N   1 
ATOM   1450 C CA  . ARG   A 1 195 ? -9.42844  -19.53596 -4.82079  1.000 26.35303 ? 202 ARG   A CA  1 
ATOM   1451 C C   . ARG   A 1 195 ? -9.31705  -18.53708 -5.96940  1.000 26.54242 ? 202 ARG   A C   1 
ATOM   1452 O O   . ARG   A 1 195 ? -8.77693  -17.43812 -5.79993  1.000 24.16047 ? 202 ARG   A O   1 
ATOM   1453 C CB  . ARG   A 1 195 ? -8.36754  -20.63318 -4.96334  1.000 24.44824 ? 202 ARG   A CB  1 
ATOM   1454 C CG  . ARG   A 1 195 ? -6.89891  -20.14230 -4.95088  1.000 26.35141 ? 202 ARG   A CG  1 
ATOM   1455 C CD  . ARG   A 1 195 ? -6.51305  -19.53636 -3.58585  1.000 30.69170 ? 202 ARG   A CD  1 
ATOM   1456 N NE  . ARG   A 1 195 ? -5.07526  -19.27533 -3.50681  1.000 26.45529 ? 202 ARG   A NE  1 
ATOM   1457 C CZ  . ARG   A 1 195 ? -4.52889  -18.09522 -3.24548  1.000 28.68813 ? 202 ARG   A CZ  1 
ATOM   1458 N NH1 . ARG   A 1 195 ? -5.26965  -17.02631 -2.99057  1.000 28.88769 ? 202 ARG   A NH1 1 
ATOM   1459 N NH2 . ARG   A 1 195 ? -3.20166  -17.97783 -3.27498  1.000 30.13553 ? 202 ARG   A NH2 1 
ATOM   1460 N N   . ILE   A 1 196 ? -9.80651  -18.90304 -7.15337  1.000 23.67631 ? 203 ILE   A N   1 
ATOM   1461 C CA  . ILE   A 1 196 ? -9.75945  -17.96121 -8.27655  1.000 21.53078 ? 203 ILE   A CA  1 
ATOM   1462 C C   . ILE   A 1 196 ? -10.57791 -16.71191 -7.96124  1.000 23.73112 ? 203 ILE   A C   1 
ATOM   1463 O O   . ILE   A 1 196 ? -10.10266 -15.58663 -8.14039  1.000 24.35285 ? 203 ILE   A O   1 
ATOM   1464 C CB  . ILE   A 1 196 ? -10.22906 -18.63352 -9.57863  1.000 24.16554 ? 203 ILE   A CB  1 
ATOM   1465 C CG1 . ILE   A 1 196 ? -9.29635  -19.80852 -9.93562  1.000 22.60616 ? 203 ILE   A CG1 1 
ATOM   1466 C CG2 . ILE   A 1 196 ? -10.28103 -17.58415 -10.73528 1.000 22.78883 ? 203 ILE   A CG2 1 
ATOM   1467 C CD1 . ILE   A 1 196 ? -9.95773  -20.83228 -10.88114 1.000 27.01697 ? 203 ILE   A CD1 1 
ATOM   1468 N N   . LYS   A 1 197 ? -11.81469 -16.88981 -7.47209  1.000 25.18821 ? 204 LYS   A N   1 
ATOM   1469 C CA  . LYS   A 1 197 ? -12.64607 -15.73739 -7.10317  1.000 23.75873 ? 204 LYS   A CA  1 
ATOM   1470 C C   . LYS   A 1 197 ? -11.93039 -14.80639 -6.13493  1.000 25.21637 ? 204 LYS   A C   1 
ATOM   1471 O O   . LYS   A 1 197 ? -12.00966 -13.58229 -6.26620  1.000 27.01810 ? 204 LYS   A O   1 
ATOM   1472 C CB  . LYS   A 1 197 ? -13.95562 -16.18097 -6.44287  1.000 29.15462 ? 204 LYS   A CB  1 
ATOM   1473 C CG  . LYS   A 1 197 ? -14.99005 -16.76820 -7.34833  1.000 36.97180 ? 204 LYS   A CG  1 
ATOM   1474 C CD  . LYS   A 1 197 ? -16.31500 -16.87165 -6.56101  1.000 40.28696 ? 204 LYS   A CD  1 
ATOM   1475 C CE  . LYS   A 1 197 ? -16.96872 -18.21178 -6.75807  1.000 48.37738 ? 204 LYS   A CE  1 
ATOM   1476 N NZ  . LYS   A 1 197 ? -18.44054 -18.25745 -6.51087  1.000 52.58811 ? 204 LYS   A NZ  1 
ATOM   1477 N N   . GLU   A 1 198 ? -11.30456 -15.38134 -5.10196  1.000 21.27995 ? 205 GLU   A N   1 
ATOM   1478 C CA  . GLU   A 1 198 ? -10.58895 -14.59573 -4.09685  1.000 23.03860 ? 205 GLU   A CA  1 
ATOM   1479 C C   . GLU   A 1 198 ? -9.50670  -13.74242 -4.74607  1.000 25.07366 ? 205 GLU   A C   1 
ATOM   1480 O O   . GLU   A 1 198 ? -9.32055  -12.56617 -4.38501  1.000 24.14324 ? 205 GLU   A O   1 
ATOM   1481 C CB  . GLU   A 1 198 ? -9.97778  -15.53201 -3.04858  1.000 23.46260 ? 205 GLU   A CB  1 
ATOM   1482 C CG  . GLU   A 1 198 ? -9.03662  -14.84560 -2.07915  1.000 26.28301 ? 205 GLU   A CG  1 
ATOM   1483 C CD  . GLU   A 1 198 ? -8.36563  -15.81774 -1.12497  1.000 30.44070 ? 205 GLU   A CD  1 
ATOM   1484 O OE1 . GLU   A 1 198 ? -7.78849  -16.81452 -1.63769  1.000 32.09297 ? 205 GLU   A OE1 1 
ATOM   1485 O OE2 . GLU   A 1 198 ? -8.37656  -15.56953 0.11059   1.000 29.92458 ? 205 GLU   A OE2 1 
ATOM   1486 N N   . ILE   A 1 199 ? -8.75224  -14.33829 -5.67451  1.000 21.85278 ? 206 ILE   A N   1 
ATOM   1487 C CA  . ILE   A 1 199 ? -7.64233  -13.61885 -6.30690  1.000 21.98739 ? 206 ILE   A CA  1 
ATOM   1488 C C   . ILE   A 1 199 ? -8.16313  -12.51497 -7.21405  1.000 26.49496 ? 206 ILE   A C   1 
ATOM   1489 O O   . ILE   A 1 199 ? -7.59326  -11.41927 -7.26362  1.000 25.02440 ? 206 ILE   A O   1 
ATOM   1490 C CB  . ILE   A 1 199 ? -6.72781  -14.59053 -7.08160  1.000 22.44591 ? 206 ILE   A CB  1 
ATOM   1491 C CG1 . ILE   A 1 199 ? -6.13110  -15.60040 -6.09457  1.000 26.92022 ? 206 ILE   A CG1 1 
ATOM   1492 C CG2 . ILE   A 1 199 ? -5.62022  -13.83121 -7.81096  1.000 25.57734 ? 206 ILE   A CG2 1 
ATOM   1493 C CD1 . ILE   A 1 199 ? -5.58531  -16.85958 -6.78634  1.000 29.24568 ? 206 ILE   A CD1 1 
ATOM   1494 N N   . VAL   A 1 200 ? -9.23576  -12.78951 -7.96350  1.000 23.03312 ? 207 VAL   A N   1 
ATOM   1495 C CA  . VAL   A 1 200 ? -9.77427  -11.77555 -8.86485  1.000 21.26246 ? 207 VAL   A CA  1 
ATOM   1496 C C   . VAL   A 1 200 ? -10.29545 -10.59588 -8.05368  1.000 24.91636 ? 207 VAL   A C   1 
ATOM   1497 O O   . VAL   A 1 200 ? -10.06212 -9.42610  -8.39434  1.000 25.64068 ? 207 VAL   A O   1 
ATOM   1498 C CB  . VAL   A 1 200 ? -10.86733 -12.39462 -9.75222  1.000 23.87201 ? 207 VAL   A CB  1 
ATOM   1499 C CG1 . VAL   A 1 200 ? -11.63100 -11.30704 -10.51101 1.000 24.12491 ? 207 VAL   A CG1 1 
ATOM   1500 C CG2 . VAL   A 1 200 ? -10.26012 -13.42453 -10.72843 1.000 21.79224 ? 207 VAL   A CG2 1 
ATOM   1501 N N   . LYS   A 1 201 ? -10.97183 -10.88196 -6.94079  1.000 22.82012 ? 208 LYS   A N   1 
ATOM   1502 C CA  . LYS   A 1 201 ? -11.50879 -9.80172  -6.11708  1.000 25.04790 ? 208 LYS   A CA  1 
ATOM   1503 C C   . LYS   A 1 201 ? -10.39526 -9.00486  -5.45598  1.000 27.35729 ? 208 LYS   A C   1 
ATOM   1504 O O   . LYS   A 1 201 ? -10.50994 -7.78548  -5.31367  1.000 32.07872 ? 208 LYS   A O   1 
ATOM   1505 C CB  . LYS   A 1 201 ? -12.48336 -10.37355 -5.08264  1.000 30.39216 ? 208 LYS   A CB  1 
ATOM   1506 C CG  . LYS   A 1 201 ? -13.25769 -9.31256  -4.27718  1.000 33.90935 ? 208 LYS   A CG  1 
ATOM   1507 C CD  . LYS   A 1 201 ? -14.09228 -9.94280  -3.18853  1.000 43.94811 ? 208 LYS   A CD  1 
ATOM   1508 C CE  . LYS   A 1 201 ? -14.52872 -8.90591  -2.16304  1.000 44.19420 ? 208 LYS   A CE  1 
ATOM   1509 N NZ  . LYS   A 1 201 ? -14.92942 -9.53373  -0.85970  1.000 55.79243 ? 208 LYS   A NZ  1 
ATOM   1510 N N   . LYS   A 1 202 ? -9.30679  -9.67733  -5.06262  1.000 28.10894 ? 209 LYS   A N   1 
ATOM   1511 C CA  . LYS   A 1 202 ? -8.19775  -8.99897  -4.39108  1.000 26.53380 ? 209 LYS   A CA  1 
ATOM   1512 C C   . LYS   A 1 202 ? -7.42672  -8.07032  -5.32720  1.000 27.37841 ? 209 LYS   A C   1 
ATOM   1513 O O   . LYS   A 1 202 ? -7.03886  -6.96179  -4.92521  1.000 28.07100 ? 209 LYS   A O   1 
ATOM   1514 C CB  . LYS   A 1 202 ? -7.24237  -10.03998 -3.81294  1.000 27.38532 ? 209 LYS   A CB  1 
ATOM   1515 C CG  . LYS   A 1 202 ? -6.07759  -9.41398  -3.04166  1.000 32.90686 ? 209 LYS   A CG  1 
ATOM   1516 C CD  . LYS   A 1 202 ? -5.20872  -10.50392 -2.41218  1.000 40.26093 ? 209 LYS   A CD  1 
ATOM   1517 C CE  . LYS   A 1 202 ? -4.11395  -9.92275  -1.52146  1.000 46.85083 ? 209 LYS   A CE  1 
ATOM   1518 N NZ  . LYS   A 1 202 ? -3.42137  -10.99419 -0.71941  1.000 50.38290 ? 209 LYS   A NZ  1 
ATOM   1519 N N   . HIS   A 1 203 ? -7.14785  -8.52504  -6.55884  1.000 27.06887 ? 210 HIS   A N   1 
ATOM   1520 C CA  . HIS   A 1 203 ? -6.15692  -7.90412  -7.43411  1.000 29.82825 ? 210 HIS   A CA  1 
ATOM   1521 C C   . HIS   A 1 203 ? -6.71538  -7.32473  -8.72314  1.000 32.17626 ? 210 HIS   A C   1 
ATOM   1522 O O   . HIS   A 1 203 ? -6.01660  -6.52636  -9.36579  1.000 28.76445 ? 210 HIS   A O   1 
ATOM   1523 C CB  . HIS   A 1 203 ? -5.08053  -8.92981  -7.84699  1.000 28.33386 ? 210 HIS   A CB  1 
ATOM   1524 C CG  . HIS   A 1 203 ? -4.22565  -9.38299  -6.71288  1.000 32.66874 ? 210 HIS   A CG  1 
ATOM   1525 N ND1 . HIS   A 1 203 ? -3.43431  -8.51848  -5.98579  1.000 34.87115 ? 210 HIS   A ND1 1 
ATOM   1526 C CD2 . HIS   A 1 203 ? -4.05612  -10.60877 -6.15933  1.000 33.16040 ? 210 HIS   A CD2 1 
ATOM   1527 C CE1 . HIS   A 1 203 ? -2.80548  -9.19372  -5.03797  1.000 37.44656 ? 210 HIS   A CE1 1 
ATOM   1528 N NE2 . HIS   A 1 203 ? -3.16558  -10.46427 -5.12146  1.000 33.92758 ? 210 HIS   A NE2 1 
ATOM   1529 N N   . SER   A 1 204 ? -7.91857  -7.73404  -9.14732  1.000 27.38643 ? 211 SER   A N   1 
ATOM   1530 C CA  . SER   A 1 204 ? -8.44327  -7.37621  -10.45960 1.000 25.60398 ? 211 SER   A CA  1 
ATOM   1531 C C   . SER   A 1 204 ? -9.87201  -6.84714  -10.37520 1.000 26.29100 ? 211 SER   A C   1 
ATOM   1532 O O   . SER   A 1 204 ? -10.59978 -6.89246  -11.37270 1.000 29.37162 ? 211 SER   A O   1 
ATOM   1533 C CB  . SER   A 1 204 ? -8.37920  -8.58183  -11.40701 1.000 27.28668 ? 211 SER   A CB  1 
ATOM   1534 O OG  . SER   A 1 204 ? -7.03654  -9.06572  -11.47936 1.000 28.18811 ? 211 SER   A OG  1 
ATOM   1535 N N   . GLN   A 1 205 ? -10.28427 -6.31384  -9.22102  1.000 27.80241 ? 212 GLN   A N   1 
ATOM   1536 C CA  . GLN   A 1 205 ? -11.71134 -6.03899  -9.05164  1.000 30.87989 ? 212 GLN   A CA  1 
ATOM   1537 C C   . GLN   A 1 205 ? -12.18673 -4.84751  -9.88113  1.000 33.64843 ? 212 GLN   A C   1 
ATOM   1538 O O   . GLN   A 1 205 ? -13.39947 -4.68793  -10.05667 1.000 32.61685 ? 212 GLN   A O   1 
ATOM   1539 C CB  . GLN   A 1 205 ? -12.06193 -5.76024  -7.58556  1.000 36.38102 ? 212 GLN   A CB  1 
ATOM   1540 C CG  . GLN   A 1 205 ? -11.29694 -4.61245  -7.00151  1.000 35.51182 ? 212 GLN   A CG  1 
ATOM   1541 C CD  . GLN   A 1 205 ? -11.48601 -4.48101  -5.50467  1.000 48.50391 ? 212 GLN   A CD  1 
ATOM   1542 O OE1 . GLN   A 1 205 ? -12.61724 -4.35275  -5.01799  1.000 45.17276 ? 212 GLN   A OE1 1 
ATOM   1543 N NE2 . GLN   A 1 205 ? -10.37160 -4.48168  -4.76630  1.000 45.13702 ? 212 GLN   A NE2 1 
ATOM   1544 N N   . PHE   A 1 206 ? -11.28178 -3.99949  -10.37893 1.000 27.73272 ? 213 PHE   A N   1 
ATOM   1545 C CA  . PHE   A 1 206 ? -11.68011 -2.81517  -11.13235 1.000 31.17699 ? 213 PHE   A CA  1 
ATOM   1546 C C   . PHE   A 1 206 ? -11.38755 -2.89083  -12.63360 1.000 32.54761 ? 213 PHE   A C   1 
ATOM   1547 O O   . PHE   A 1 206 ? -11.60204 -1.89014  -13.33274 1.000 32.82131 ? 213 PHE   A O   1 
ATOM   1548 C CB  . PHE   A 1 206 ? -11.01350 -1.57474  -10.53946 1.000 30.47378 ? 213 PHE   A CB  1 
ATOM   1549 C CG  . PHE   A 1 206 ? -11.30466 -1.37345  -9.07172  1.000 33.42846 ? 213 PHE   A CG  1 
ATOM   1550 C CD1 . PHE   A 1 206 ? -12.61736 -1.26932  -8.61317  1.000 36.09949 ? 213 PHE   A CD1 1 
ATOM   1551 C CD2 . PHE   A 1 206 ? -10.27323 -1.33231  -8.14589  1.000 35.52445 ? 213 PHE   A CD2 1 
ATOM   1552 C CE1 . PHE   A 1 206 ? -12.88789 -1.08188  -7.25420  1.000 39.92452 ? 213 PHE   A CE1 1 
ATOM   1553 C CE2 . PHE   A 1 206 ? -10.54029 -1.14534  -6.78847  1.000 41.52035 ? 213 PHE   A CE2 1 
ATOM   1554 C CZ  . PHE   A 1 206 ? -11.85172 -1.03156  -6.34851  1.000 37.96204 ? 213 PHE   A CZ  1 
ATOM   1555 N N   . ILE   A 1 207 ? -10.93929 -4.04648  -13.15002 1.000 26.45739 ? 214 ILE   A N   1 
ATOM   1556 C CA  . ILE   A 1 207 ? -10.73271 -4.22691  -14.58950 1.000 25.94472 ? 214 ILE   A CA  1 
ATOM   1557 C C   . ILE   A 1 207 ? -12.00662 -3.86108  -15.35565 1.000 28.15140 ? 214 ILE   A C   1 
ATOM   1558 O O   . ILE   A 1 207 ? -13.11919 -4.26707  -14.98976 1.000 28.00897 ? 214 ILE   A O   1 
ATOM   1559 C CB  . ILE   A 1 207 ? -10.28317 -5.67563  -14.86631 1.000 25.89798 ? 214 ILE   A CB  1 
ATOM   1560 C CG1 . ILE   A 1 207 ? -8.88901  -5.94205  -14.27218 1.000 23.45123 ? 214 ILE   A CG1 1 
ATOM   1561 C CG2 . ILE   A 1 207 ? -10.24412 -5.98583  -16.36948 1.000 26.70963 ? 214 ILE   A CG2 1 
ATOM   1562 C CD1 . ILE   A 1 207 ? -7.77798  -5.19473  -15.02064 1.000 28.04043 ? 214 ILE   A CD1 1 
ATOM   1563 N N   . GLY   A 1 208 ? -11.85519 -3.05741  -16.40243 1.000 25.33989 ? 215 GLY   A N   1 
ATOM   1564 C CA  . GLY   A 1 208 ? -12.99857 -2.52480  -17.12284 1.000 25.89170 ? 215 GLY   A CA  1 
ATOM   1565 C C   . GLY   A 1 208 ? -13.61199 -3.40566  -18.19920 1.000 26.08156 ? 215 GLY   A C   1 
ATOM   1566 O O   . GLY   A 1 208 ? -14.21508 -2.89887  -19.15858 1.000 29.23127 ? 215 GLY   A O   1 
ATOM   1567 N N   . TYR   A 1 209 ? -13.46382 -4.71696  -18.06900 1.000 25.01091 ? 216 TYR   A N   1 
ATOM   1568 C CA  . TYR   A 1 209 ? -14.06584 -5.66697  -19.00083 1.000 23.81316 ? 216 TYR   A CA  1 
ATOM   1569 C C   . TYR   A 1 209 ? -14.65900 -6.77875  -18.15844 1.000 25.98209 ? 216 TYR   A C   1 
ATOM   1570 O O   . TYR   A 1 209 ? -14.11489 -7.09405  -17.09515 1.000 25.57938 ? 216 TYR   A O   1 
ATOM   1571 C CB  . TYR   A 1 209 ? -13.01950 -6.25574  -19.96877 1.000 23.76527 ? 216 TYR   A CB  1 
ATOM   1572 C CG  . TYR   A 1 209 ? -12.40251 -5.18114  -20.83617 1.000 23.41328 ? 216 TYR   A CG  1 
ATOM   1573 C CD1 . TYR   A 1 209 ? -13.04284 -4.73301  -21.98004 1.000 26.71795 ? 216 TYR   A CD1 1 
ATOM   1574 C CD2 . TYR   A 1 209 ? -11.18103 -4.59414  -20.48767 1.000 27.31813 ? 216 TYR   A CD2 1 
ATOM   1575 C CE1 . TYR   A 1 209 ? -12.49570 -3.73564  -22.76922 1.000 30.07990 ? 216 TYR   A CE1 1 
ATOM   1576 C CE2 . TYR   A 1 209 ? -10.62473 -3.58217  -21.27013 1.000 23.09330 ? 216 TYR   A CE2 1 
ATOM   1577 C CZ  . TYR   A 1 209 ? -11.30395 -3.15649  -22.40377 1.000 25.30383 ? 216 TYR   A CZ  1 
ATOM   1578 O OH  . TYR   A 1 209 ? -10.80321 -2.16881  -23.20443 1.000 31.18570 ? 216 TYR   A OH  1 
ATOM   1579 N N   . PRO   A 1 210 ? -15.73731 -7.42485  -18.60762 1.000 27.06144 ? 217 PRO   A N   1 
ATOM   1580 C CA  . PRO   A 1 210 ? -16.31149 -8.52429  -17.81081 1.000 23.94532 ? 217 PRO   A CA  1 
ATOM   1581 C C   . PRO   A 1 210 ? -15.36982 -9.72076  -17.74208 1.000 27.99655 ? 217 PRO   A C   1 
ATOM   1582 O O   . PRO   A 1 210 ? -14.83617 -10.16920 -18.76311 1.000 27.33191 ? 217 PRO   A O   1 
ATOM   1583 C CB  . PRO   A 1 210 ? -17.61845 -8.86931  -18.54888 1.000 28.83259 ? 217 PRO   A CB  1 
ATOM   1584 C CG  . PRO   A 1 210 ? -17.45807 -8.36138  -19.90484 1.000 29.66153 ? 217 PRO   A CG  1 
ATOM   1585 C CD  . PRO   A 1 210 ? -16.52699 -7.13990  -19.81794 1.000 30.15944 ? 217 PRO   A CD  1 
ATOM   1586 N N   . ILE   A 1 211 ? -15.16826 -10.22413 -16.52331 1.000 24.94194 ? 218 ILE   A N   1 
ATOM   1587 C CA  . ILE   A 1 211 ? -14.36184 -11.41669 -16.25234 1.000 21.61386 ? 218 ILE   A CA  1 
ATOM   1588 C C   . ILE   A 1 211 ? -15.31557 -12.51318 -15.80508 1.000 24.14125 ? 218 ILE   A C   1 
ATOM   1589 O O   . ILE   A 1 211 ? -15.99042 -12.37650 -14.77267 1.000 27.71571 ? 218 ILE   A O   1 
ATOM   1590 C CB  . ILE   A 1 211 ? -13.28307 -11.14748 -15.19147 1.000 26.37308 ? 218 ILE   A CB  1 
ATOM   1591 C CG1 . ILE   A 1 211 ? -12.34882 -9.99453  -15.64527 1.000 23.36845 ? 218 ILE   A CG1 1 
ATOM   1592 C CG2 . ILE   A 1 211 ? -12.53496 -12.43573 -14.82186 1.000 25.41277 ? 218 ILE   A CG2 1 
ATOM   1593 C CD1 . ILE   A 1 211 ? -11.42363 -9.47441  -14.49228 1.000 22.90610 ? 218 ILE   A CD1 1 
ATOM   1594 N N   . THR   A 1 212 ? -15.40114 -13.58414 -16.58378 1.000 22.76123 ? 219 THR   A N   1 
ATOM   1595 C CA  . THR   A 1 212 ? -16.34039 -14.66897 -16.29029 1.000 20.77466 ? 219 THR   A CA  1 
ATOM   1596 C C   . THR   A 1 212 ? -15.52590 -15.87394 -15.86354 1.000 23.24634 ? 219 THR   A C   1 
ATOM   1597 O O   . THR   A 1 212 ? -14.69279 -16.36280 -16.63912 1.000 21.70051 ? 219 THR   A O   1 
ATOM   1598 C CB  . THR   A 1 212 ? -17.20052 -15.01651 -17.50963 1.000 23.59172 ? 219 THR   A CB  1 
ATOM   1599 O OG1 . THR   A 1 212 ? -17.93004 -13.85264 -17.95506 1.000 26.55368 ? 219 THR   A OG1 1 
ATOM   1600 C CG2 . THR   A 1 212 ? -18.21777 -16.14695 -17.15014 1.000 23.95524 ? 219 THR   A CG2 1 
ATOM   1601 N N   . LEU   A 1 213 ? -15.77411 -16.35913 -14.65582 1.000 24.49568 ? 220 LEU   A N   1 
ATOM   1602 C CA  . LEU   A 1 213 ? -15.12327 -17.57033 -14.17327 1.000 23.60777 ? 220 LEU   A CA  1 
ATOM   1603 C C   . LEU   A 1 213 ? -16.04065 -18.73132 -14.50784 1.000 22.13741 ? 220 LEU   A C   1 
ATOM   1604 O O   . LEU   A 1 213 ? -17.15295 -18.81544 -13.96402 1.000 23.87441 ? 220 LEU   A O   1 
ATOM   1605 C CB  . LEU   A 1 213 ? -14.86211 -17.48319 -12.66859 1.000 24.55100 ? 220 LEU   A CB  1 
ATOM   1606 C CG  . LEU   A 1 213 ? -14.36012 -18.74356 -11.96692 1.000 25.28324 ? 220 LEU   A CG  1 
ATOM   1607 C CD1 . LEU   A 1 213 ? -13.10772 -19.31275 -12.62268 1.000 23.99433 ? 220 LEU   A CD1 1 
ATOM   1608 C CD2 . LEU   A 1 213 ? -14.06596 -18.36144 -10.50294 1.000 31.09351 ? 220 LEU   A CD2 1 
ATOM   1609 N N   . PHE   A 1 214 ? -15.58944 -19.61300 -15.40941 1.000 20.34652 ? 221 PHE   A N   1 
ATOM   1610 C CA  . PHE   A 1 214 ? -16.36239 -20.78893 -15.77050 1.000 24.05824 ? 221 PHE   A CA  1 
ATOM   1611 C C   . PHE   A 1 214 ? -16.34798 -21.80446 -14.62720 1.000 26.34177 ? 221 PHE   A C   1 
ATOM   1612 O O   . PHE   A 1 214 ? -15.37451 -21.91382 -13.88651 1.000 26.68772 ? 221 PHE   A O   1 
ATOM   1613 C CB  . PHE   A 1 214 ? -15.77620 -21.46247 -17.02989 1.000 22.98565 ? 221 PHE   A CB  1 
ATOM   1614 C CG  . PHE   A 1 214 ? -16.02884 -20.73693 -18.33705 1.000 21.92522 ? 221 PHE   A CG  1 
ATOM   1615 C CD1 . PHE   A 1 214 ? -16.11936 -19.35470 -18.40866 1.000 22.19901 ? 221 PHE   A CD1 1 
ATOM   1616 C CD2 . PHE   A 1 214 ? -16.18599 -21.48232 -19.52096 1.000 22.39433 ? 221 PHE   A CD2 1 
ATOM   1617 C CE1 . PHE   A 1 214 ? -16.34086 -18.69807 -19.62823 1.000 22.48837 ? 221 PHE   A CE1 1 
ATOM   1618 C CE2 . PHE   A 1 214 ? -16.42698 -20.84026 -20.75812 1.000 24.00846 ? 221 PHE   A CE2 1 
ATOM   1619 C CZ  . PHE   A 1 214 ? -16.50951 -19.44649 -20.81655 1.000 24.44248 ? 221 PHE   A CZ  1 
ATOM   1620 N N   . VAL   A 1 215 ? -17.41940 -22.57994 -14.49863 1.000 26.11361 ? 222 VAL   A N   1 
ATOM   1621 C CA  . VAL   A 1 215 ? -17.44342 -23.67907 -13.53798 1.000 30.14885 ? 222 VAL   A CA  1 
ATOM   1622 C C   . VAL   A 1 215 ? -17.30528 -25.01898 -14.26469 1.000 33.15393 ? 222 VAL   A C   1 
ATOM   1623 O O   . VAL   A 1 215 ? -17.44103 -25.11149 -15.48445 1.000 30.27711 ? 222 VAL   A O   1 
ATOM   1624 C CB  . VAL   A 1 215 ? -18.69952 -23.64104 -12.65305 1.000 38.62164 ? 222 VAL   A CB  1 
ATOM   1625 C CG1 . VAL   A 1 215 ? -18.62859 -22.42017 -11.71721 1.000 39.77591 ? 222 VAL   A CG1 1 
ATOM   1626 C CG2 . VAL   A 1 215 ? -19.90807 -23.55476 -13.49861 1.000 33.41734 ? 222 VAL   A CG2 1 
ATOM   1627 N N   . GLU   A 1 216 ? -17.03658 -26.07200 -13.49597 1.000 33.65490 ? 223 GLU   A N   1 
ATOM   1628 C CA  . GLU   A 1 216 ? -16.89320 -27.40112 -14.07708 1.000 37.61351 ? 223 GLU   A CA  1 
ATOM   1629 C C   . GLU   A 1 216 ? -17.99673 -28.33709 -13.60912 1.000 40.67480 ? 223 GLU   A C   1 
ATOM   1630 O O   . GLU   A 1 216 ? -18.61479 -28.13034 -12.56339 1.000 46.34011 ? 223 GLU   A O   1 
ATOM   1631 C CB  . GLU   A 1 216 ? -15.52215 -28.02552 -13.77012 1.000 38.11893 ? 223 GLU   A CB  1 
ATOM   1632 C CG  . GLU   A 1 216 ? -14.36837 -27.08262 -14.01414 1.000 37.19197 ? 223 GLU   A CG  1 
ATOM   1633 C CD  . GLU   A 1 216 ? -13.04585 -27.61339 -13.48429 1.000 39.98098 ? 223 GLU   A CD  1 
ATOM   1634 O OE1 . GLU   A 1 216 ? -12.42610 -26.92806 -12.62860 1.000 42.54724 ? 223 GLU   A OE1 1 
ATOM   1635 O OE2 . GLU   A 1 216 ? -12.62775 -28.70737 -13.94613 1.000 38.82207 ? 223 GLU   A OE2 1 
ATOM   1636 N N   . LYS   A 1 217 ? -18.23164 -29.37546 -14.41847 1.000 44.24265 ? 224 LYS   A N   1 
ATOM   1637 C CA  . LYS   A 1 217 ? -19.18866 -30.44308 -14.11842 1.000 50.89021 ? 224 LYS   A CA  1 
ATOM   1638 C C   . LYS   A 1 217 ? -19.02791 -31.04668 -12.70942 1.000 59.13627 ? 224 LYS   A C   1 
ATOM   1639 O O   . LYS   A 1 217 ? -17.91604 -31.27387 -12.22077 1.000 55.95772 ? 224 LYS   A O   1 
ATOM   1640 C CB  . LYS   A 1 217 ? -19.07482 -31.55673 -15.17456 1.000 57.03974 ? 224 LYS   A CB  1 
ATOM   1641 C CG  . LYS   A 1 217 ? -19.21323 -32.98103 -14.62008 1.000 57.31792 ? 224 LYS   A CG  1 
ATOM   1642 C CD  . LYS   A 1 217 ? -20.66058 -33.44058 -14.54596 1.000 63.70141 ? 224 LYS   A CD  1 
ATOM   1643 C CE  . LYS   A 1 217 ? -20.81882 -34.96860 -14.57869 1.000 63.48490 ? 224 LYS   A CE  1 
ATOM   1644 N NZ  . LYS   A 1 217 ? -19.84440 -35.71281 -13.71209 1.000 62.49853 ? 224 LYS   A NZ  1 
HETATM 1645 C C1  . A1AX2 B 2 .   ? 10.57679  -14.78519 -8.68541  0.718 32.88757 ? 301 A1AX2 A C1  1 
HETATM 1646 C C10 . A1AX2 B 2 .   ? 13.64737  -13.08679 -8.87573  0.753 38.42341 ? 301 A1AX2 A C10 1 
HETATM 1647 C C2  . A1AX2 B 2 .   ? 11.40977  -14.05764 -9.07904  0.814 33.68234 ? 301 A1AX2 A C2  1 
HETATM 1648 C C3  . A1AX2 B 2 .   ? 12.44486  -13.18416 -9.57190  0.745 35.84365 ? 301 A1AX2 A C3  1 
HETATM 1649 C C4  . A1AX2 B 2 .   ? 12.25907  -12.41681 -10.72870 0.717 34.04419 ? 301 A1AX2 A C4  1 
HETATM 1650 C C5  . A1AX2 B 2 .   ? 13.26372  -11.56361 -11.15576 0.600 35.04998 ? 301 A1AX2 A C5  1 
HETATM 1651 C C6  . A1AX2 B 2 .   ? 14.45918  -11.46933 -10.45889 1.000 40.96731 ? 301 A1AX2 A C6  1 
HETATM 1652 C C7  . A1AX2 B 2 .   ? 14.64515  -12.21735 -9.29743  0.754 41.51345 ? 301 A1AX2 A C7  1 
HETATM 1653 C C8  . A1AX2 B 2 .   ? 16.06699  -11.85566 -7.25869  1.000 52.52239 ? 301 A1AX2 A C8  1 
HETATM 1654 C C9  . A1AX2 B 2 .   ? 14.88973  -11.28761 -6.51988  0.756 52.69055 ? 301 A1AX2 A C9  1 
HETATM 1655 N N1  . A1AX2 B 2 .   ? 15.85986  -12.16673 -8.56456  1.000 49.01899 ? 301 A1AX2 A N1  1 
HETATM 1656 O O1  . A1AX2 B 2 .   ? 17.12580  -12.08194 -6.68595  0.315 57.18987 ? 301 A1AX2 A O1  1 
HETATM 1657 O O   . HOH   C 3 .   ? 12.83005  -8.95899  -30.25567 1.000 44.62297 ? 401 HOH   A O   1 
HETATM 1658 O O   . HOH   C 3 .   ? -14.62650 -7.23389  -42.05139 1.000 56.88342 ? 402 HOH   A O   1 
HETATM 1659 O O   . HOH   C 3 .   ? -7.22812  -17.26876 -41.22721 1.000 50.27066 ? 403 HOH   A O   1 
HETATM 1660 O O   . HOH   C 3 .   ? 5.30541   -29.20932 -8.38142  1.000 46.30132 ? 404 HOH   A O   1 
HETATM 1661 O O   . HOH   C 3 .   ? 9.26126   -23.72651 -9.79877  1.000 51.34497 ? 405 HOH   A O   1 
HETATM 1662 O O   . HOH   C 3 .   ? -12.396   -28.051   -29.983   1.000 36.71612 ? 406 HOH   A O   1 
HETATM 1663 O O   . HOH   C 3 .   ? -15.72343 -1.36289  -27.11357 1.000 60.43182 ? 407 HOH   A O   1 
HETATM 1664 O O   . HOH   C 3 .   ? -2.81761  -6.17798  -6.38404  1.000 42.43615 ? 408 HOH   A O   1 
HETATM 1665 O O   . HOH   C 3 .   ? -1.67302  -29.09793 -5.95261  1.000 36.29475 ? 409 HOH   A O   1 
HETATM 1666 O O   . HOH   C 3 .   ? 1.99437   -15.80243 -41.22491 1.000 45.12944 ? 410 HOH   A O   1 
HETATM 1667 O O   . HOH   C 3 .   ? 5.80929   -25.57001 -6.96332  1.000 48.29389 ? 411 HOH   A O   1 
HETATM 1668 O O   . HOH   C 3 .   ? -16.25456 -25.44827 -17.74225 1.000 30.45489 ? 412 HOH   A O   1 
HETATM 1669 O O   . HOH   C 3 .   ? -16.38495 -12.67835 -19.65647 1.000 27.63457 ? 413 HOH   A O   1 
HETATM 1670 O O   . HOH   C 3 .   ? -2.92470  -3.33198  -35.52886 1.000 45.77855 ? 414 HOH   A O   1 
HETATM 1671 O O   . HOH   C 3 .   ? 3.16109   -24.57678 -38.67236 1.000 41.94982 ? 415 HOH   A O   1 
HETATM 1672 O O   . HOH   C 3 .   ? 17.32302  -10.41735 -9.79841  1.000 50.14730 ? 416 HOH   A O   1 
HETATM 1673 O O   . HOH   C 3 .   ? 7.65304   -27.89947 -23.99592 1.000 38.40348 ? 417 HOH   A O   1 
HETATM 1674 O O   . HOH   C 3 .   ? -7.41279  -28.07654 -21.30649 1.000 47.44386 ? 418 HOH   A O   1 
HETATM 1675 O O   . HOH   C 3 .   ? -0.22058  -5.50896  -38.69848 1.000 51.59810 ? 419 HOH   A O   1 
HETATM 1676 O O   . HOH   C 3 .   ? -14.68216 -7.11370  -14.54270 1.000 37.86292 ? 420 HOH   A O   1 
HETATM 1677 O O   . HOH   C 3 .   ? 5.93095   -22.02703 -37.25348 1.000 37.71405 ? 421 HOH   A O   1 
HETATM 1678 O O   . HOH   C 3 .   ? -9.23391  -2.32060  -17.49578 1.000 27.59866 ? 422 HOH   A O   1 
HETATM 1679 O O   . HOH   C 3 .   ? 3.18025   -6.09886  -11.20054 1.000 29.10180 ? 423 HOH   A O   1 
HETATM 1680 O O   . HOH   C 3 .   ? -10.64623 -6.15192  -2.74889  1.000 46.39726 ? 424 HOH   A O   1 
HETATM 1681 O O   . HOH   C 3 .   ? -10.67512 -14.64161 1.01352   1.000 34.33054 ? 425 HOH   A O   1 
HETATM 1682 O O   . HOH   C 3 .   ? -3.62793  -10.92406 -24.08545 1.000 33.20451 ? 426 HOH   A O   1 
HETATM 1683 O O   . HOH   C 3 .   ? 7.80054   -18.90872 -6.53445  1.000 29.45597 ? 427 HOH   A O   1 
HETATM 1684 O O   . HOH   C 3 .   ? 1.42189   -7.82399  -16.60059 1.000 26.41772 ? 428 HOH   A O   1 
HETATM 1685 O O   . HOH   C 3 .   ? 7.79578   -23.28306 -14.14634 1.000 33.12154 ? 429 HOH   A O   1 
HETATM 1686 O O   . HOH   C 3 .   ? -0.67097  -11.14585 -3.09148  1.000 41.88072 ? 430 HOH   A O   1 
HETATM 1687 O O   . HOH   C 3 .   ? -8.75886  -11.94082 -36.38131 1.000 33.66629 ? 431 HOH   A O   1 
HETATM 1688 O O   . HOH   C 3 .   ? -8.46033  4.69126   -33.73369 1.000 36.39640 ? 432 HOH   A O   1 
HETATM 1689 O O   . HOH   C 3 .   ? -5.40224  -10.39522 -27.38225 1.000 24.68243 ? 433 HOH   A O   1 
HETATM 1690 O O   . HOH   C 3 .   ? 18.25762  -7.14150  -20.57465 1.000 40.27988 ? 434 HOH   A O   1 
HETATM 1691 O O   . HOH   C 3 .   ? 16.26330  1.40426   -15.17623 1.000 43.74105 ? 435 HOH   A O   1 
HETATM 1692 O O   . HOH   C 3 .   ? 0.43919   -1.58291  -19.81868 1.000 43.59271 ? 436 HOH   A O   1 
HETATM 1693 O O   . HOH   C 3 .   ? -4.25458  -4.78660  -8.36859  1.000 47.79080 ? 437 HOH   A O   1 
HETATM 1694 O O   . HOH   C 3 .   ? 13.57921  -14.23271 -26.88819 1.000 29.78858 ? 438 HOH   A O   1 
HETATM 1695 O O   . HOH   C 3 .   ? 9.74257   -17.57299 -7.77786  1.000 27.37040 ? 439 HOH   A O   1 
HETATM 1696 O O   . HOH   C 3 .   ? 11.56865  -27.44841 -34.65397 1.000 33.83831 ? 440 HOH   A O   1 
HETATM 1697 O O   . HOH   C 3 .   ? 9.79092   -14.71030 -25.19416 1.000 27.92796 ? 441 HOH   A O   1 
HETATM 1698 O O   . HOH   C 3 .   ? -13.15999 -7.34864  -12.04801 1.000 32.80400 ? 442 HOH   A O   1 
HETATM 1699 O O   . HOH   C 3 .   ? 6.60283   -29.72024 -20.26505 1.000 41.06622 ? 443 HOH   A O   1 
HETATM 1700 O O   . HOH   C 3 .   ? 10.90178  -25.65350 -26.76674 1.000 35.39495 ? 444 HOH   A O   1 
HETATM 1701 O O   . HOH   C 3 .   ? 9.53309   -11.13690 -34.95902 1.000 43.34550 ? 445 HOH   A O   1 
HETATM 1702 O O   . HOH   C 3 .   ? 18.56474  -7.47555  -9.68785  1.000 45.93918 ? 446 HOH   A O   1 
HETATM 1703 O O   . HOH   C 3 .   ? 11.12244  -8.15174  -27.63869 1.000 29.93670 ? 447 HOH   A O   1 
HETATM 1704 O O   . HOH   C 3 .   ? -8.12130  -22.70496 -30.22403 1.000 50.35558 ? 448 HOH   A O   1 
HETATM 1705 O O   . HOH   C 3 .   ? -6.33774  -5.05151  -35.69407 1.000 29.19508 ? 449 HOH   A O   1 
HETATM 1706 O O   . HOH   C 3 .   ? -4.10166  0.26932   -22.23422 1.000 41.90880 ? 450 HOH   A O   1 
HETATM 1707 O O   . HOH   C 3 .   ? 20.57813  -10.87604 -26.18235 1.000 42.82452 ? 451 HOH   A O   1 
HETATM 1708 O O   . HOH   C 3 .   ? 4.08763   -19.51886 -40.77494 1.000 41.74163 ? 452 HOH   A O   1 
HETATM 1709 O O   . HOH   C 3 .   ? 0.96145   -6.23764  -34.25203 1.000 46.45361 ? 453 HOH   A O   1 
HETATM 1710 O O   . HOH   C 3 .   ? -5.56078  -28.54363 -4.81797  1.000 47.07503 ? 454 HOH   A O   1 
HETATM 1711 O O   . HOH   C 3 .   ? -9.86512  -34.04022 -20.91839 1.000 57.05994 ? 455 HOH   A O   1 
HETATM 1712 O O   . HOH   C 3 .   ? -13.09212 -24.86516 -10.85256 1.000 38.62258 ? 456 HOH   A O   1 
HETATM 1713 O O   . HOH   C 3 .   ? 0.69551   -27.13673 -37.02442 1.000 52.39422 ? 457 HOH   A O   1 
HETATM 1714 O O   . HOH   C 3 .   ? -12.74937 -27.24192 -34.69902 1.000 48.79564 ? 458 HOH   A O   1 
HETATM 1715 O O   . HOH   C 3 .   ? 8.92409   -4.77968  -2.34772  1.000 51.79333 ? 459 HOH   A O   1 
HETATM 1716 O O   . HOH   C 3 .   ? -5.96085  -31.28689 -11.57458 1.000 35.17669 ? 460 HOH   A O   1 
HETATM 1717 O O   . HOH   C 3 .   ? -6.23122  -14.05382 0.85979   1.000 39.60451 ? 461 HOH   A O   1 
HETATM 1718 O O   . HOH   C 3 .   ? 11.41149  -28.43467 -30.46180 1.000 38.12783 ? 462 HOH   A O   1 
HETATM 1719 O O   . HOH   C 3 .   ? -13.77553 -17.00412 -2.64309  1.000 32.54152 ? 463 HOH   A O   1 
HETATM 1720 O O   . HOH   C 3 .   ? -2.41579  -10.77540 -26.55439 1.000 36.48391 ? 464 HOH   A O   1 
HETATM 1721 O O   . HOH   C 3 .   ? 6.63498   -26.93282 -27.75759 1.000 38.67786 ? 465 HOH   A O   1 
HETATM 1722 O O   . HOH   C 3 .   ? -1.55250  -6.33501  -26.19612 1.000 28.97368 ? 466 HOH   A O   1 
HETATM 1723 O O   . HOH   C 3 .   ? -1.16988  -7.42720  -23.62574 1.000 32.00661 ? 467 HOH   A O   1 
HETATM 1724 O O   . HOH   C 3 .   ? -2.33426  -15.62716 -0.26823  1.000 50.34262 ? 468 HOH   A O   1 
HETATM 1725 O O   . HOH   C 3 .   ? -0.38443  -5.31357  -18.38289 1.000 33.22166 ? 469 HOH   A O   1 
HETATM 1726 O O   . HOH   C 3 .   ? -6.56018  -5.12354  -38.96739 1.000 45.46302 ? 470 HOH   A O   1 
HETATM 1727 O O   . HOH   C 3 .   ? -17.90053 -18.73056 -11.10567 1.000 39.53420 ? 471 HOH   A O   1 
HETATM 1728 O O   . HOH   C 3 .   ? 6.05478   -21.17911 -0.12783  1.000 32.62852 ? 472 HOH   A O   1 
HETATM 1729 O O   . HOH   C 3 .   ? 1.53125   -26.09878 -2.74148  1.000 46.34921 ? 473 HOH   A O   1 
HETATM 1730 O O   . HOH   C 3 .   ? 0.48212   -5.34495  -14.11314 1.000 42.52665 ? 474 HOH   A O   1 
HETATM 1731 O O   . HOH   C 3 .   ? -3.80184  -13.35756 -42.95053 1.000 49.50101 ? 475 HOH   A O   1 
HETATM 1732 O O   . HOH   C 3 .   ? -8.27167  -24.83185 -19.07321 1.000 25.13313 ? 476 HOH   A O   1 
HETATM 1733 O O   . HOH   C 3 .   ? -7.74905  -28.30498 -7.76926  1.000 37.42685 ? 477 HOH   A O   1 
HETATM 1734 O O   . HOH   C 3 .   ? -17.10345 -5.28381  -22.83584 1.000 32.56810 ? 478 HOH   A O   1 
HETATM 1735 O O   . HOH   C 3 .   ? 0.85715   -21.06902 -4.63767  1.000 33.13440 ? 479 HOH   A O   1 
HETATM 1736 O O   . HOH   C 3 .   ? -10.37395 -11.58216 -2.03341  1.000 28.46748 ? 480 HOH   A O   1 
HETATM 1737 O O   . HOH   C 3 .   ? -5.72183  -2.05785  -19.43473 1.000 28.94845 ? 481 HOH   A O   1 
HETATM 1738 O O   . HOH   C 3 .   ? 15.79153  -0.88257  -19.91167 1.000 40.68543 ? 482 HOH   A O   1 
HETATM 1739 O O   . HOH   C 3 .   ? 14.34117  -16.05995 -30.72945 1.000 35.93694 ? 483 HOH   A O   1 
HETATM 1740 O O   . HOH   C 3 .   ? -13.54110 -0.63217  -20.68208 1.000 36.67945 ? 484 HOH   A O   1 
HETATM 1741 O O   . HOH   C 3 .   ? -20.68265 -14.03684 -18.12305 1.000 47.25922 ? 485 HOH   A O   1 
HETATM 1742 O O   . HOH   C 3 .   ? -2.13611  -0.49750  -18.80849 1.000 44.34928 ? 486 HOH   A O   1 
HETATM 1743 O O   . HOH   C 3 .   ? -5.42559  -7.55374  -13.14463 1.000 24.07664 ? 487 HOH   A O   1 
HETATM 1744 O O   . HOH   C 3 .   ? -15.92462 0.41006   -30.51776 1.000 44.00590 ? 488 HOH   A O   1 
HETATM 1745 O O   . HOH   C 3 .   ? 8.39370   -16.37982 -39.75170 1.000 43.61652 ? 489 HOH   A O   1 
HETATM 1746 O O   . HOH   C 3 .   ? 19.85891  -16.61716 -27.35560 1.000 42.20876 ? 490 HOH   A O   1 
HETATM 1747 O O   . HOH   C 3 .   ? -2.30717  -13.71316 -35.79276 1.000 27.19811 ? 491 HOH   A O   1 
HETATM 1748 O O   . HOH   C 3 .   ? -19.50820 -10.26562 -32.87109 1.000 50.14650 ? 492 HOH   A O   1 
HETATM 1749 O O   . HOH   C 3 .   ? -6.52273  -7.77438  -34.48078 1.000 25.87893 ? 493 HOH   A O   1 
HETATM 1750 O O   . HOH   C 3 .   ? 1.57372   -3.92279  -16.88103 1.000 44.35329 ? 494 HOH   A O   1 
HETATM 1751 O O   . HOH   C 3 .   ? -11.16767 -14.15690 -37.80805 1.000 39.15366 ? 495 HOH   A O   1 
HETATM 1752 O O   . HOH   C 3 .   ? -18.96150 -10.85071 -23.65311 1.000 40.17650 ? 496 HOH   A O   1 
HETATM 1753 O O   . HOH   C 3 .   ? -3.61228  -21.02825 -38.80810 1.000 38.75639 ? 497 HOH   A O   1 
HETATM 1754 O O   . HOH   C 3 .   ? 7.61302   1.40847   -15.00264 1.000 37.41708 ? 498 HOH   A O   1 
HETATM 1755 O O   . HOH   C 3 .   ? 15.53196  -20.23644 -18.79271 1.000 29.87874 ? 499 HOH   A O   1 
HETATM 1756 O O   . HOH   C 3 .   ? 3.50363   -7.78556  -36.84471 1.000 42.53180 ? 500 HOH   A O   1 
HETATM 1757 O O   . HOH   C 3 .   ? -14.16567 -12.54007 -7.69564  1.000 29.50057 ? 501 HOH   A O   1 
HETATM 1758 O O   . HOH   C 3 .   ? -14.70460 -22.56596 -11.25887 1.000 36.20117 ? 502 HOH   A O   1 
HETATM 1759 O O   . HOH   C 3 .   ? -7.83412  -24.45462 -22.97507 1.000 35.94443 ? 503 HOH   A O   1 
HETATM 1760 O O   . HOH   C 3 .   ? 0.33949   -22.26106 -1.96815  1.000 50.03525 ? 504 HOH   A O   1 
HETATM 1761 O O   . HOH   C 3 .   ? -18.13566 -3.71504  -28.99923 1.000 48.09808 ? 505 HOH   A O   1 
HETATM 1762 O O   . HOH   C 3 .   ? -9.07783  -10.55612 -40.38015 1.000 45.13128 ? 506 HOH   A O   1 
HETATM 1763 O O   . HOH   C 3 .   ? 12.99145  -13.97984 -29.83266 1.000 34.12870 ? 507 HOH   A O   1 
HETATM 1764 O O   . HOH   C 3 .   ? -8.05714  1.88646   -36.71543 1.000 48.80649 ? 508 HOH   A O   1 
HETATM 1765 O O   . HOH   C 3 .   ? 3.61940   -29.91061 -25.83244 1.000 50.70780 ? 509 HOH   A O   1 
HETATM 1766 O O   . HOH   C 3 .   ? -6.22493  -11.32502 -10.04146 1.000 31.07203 ? 510 HOH   A O   1 
HETATM 1767 O O   . HOH   C 3 .   ? 7.96129   -23.29415 -7.12856  1.000 42.53617 ? 511 HOH   A O   1 
HETATM 1768 O O   . HOH   C 3 .   ? 0.72559   -29.75378 -16.13020 1.000 42.30002 ? 512 HOH   A O   1 
HETATM 1769 O O   . HOH   C 3 .   ? 4.05797   -24.24283 -30.72008 1.000 27.93096 ? 513 HOH   A O   1 
HETATM 1770 O O   . HOH   C 3 .   ? 10.59022  -25.40036 -23.69732 1.000 28.07814 ? 514 HOH   A O   1 
HETATM 1771 O O   . HOH   C 3 .   ? 9.21172   -26.37381 -17.03087 1.000 36.15742 ? 515 HOH   A O   1 
HETATM 1772 O O   . HOH   C 3 .   ? 19.57875  0.13174   -9.81538  1.000 49.15601 ? 516 HOH   A O   1 
HETATM 1773 O O   . HOH   C 3 .   ? 3.02998   -20.51648 -2.72933  1.000 39.75557 ? 517 HOH   A O   1 
HETATM 1774 O O   . HOH   C 3 .   ? -19.925   -19.316   -14.171   1.000 27.97305 ? 518 HOH   A O   1 
HETATM 1775 O O   . HOH   C 3 .   ? -8.87741  -18.11938 -36.63540 1.000 42.83287 ? 519 HOH   A O   1 
HETATM 1776 O O   . HOH   C 3 .   ? -13.65926 -26.45717 -17.90247 1.000 32.47236 ? 520 HOH   A O   1 
HETATM 1777 O O   . HOH   C 3 .   ? 17.10649  0.55456   -17.86961 1.000 45.18481 ? 521 HOH   A O   1 
HETATM 1778 O O   . HOH   C 3 .   ? -7.23802  1.03681   -19.28356 1.000 46.20337 ? 522 HOH   A O   1 
HETATM 1779 O O   . HOH   C 3 .   ? -14.72986 -4.37198  -12.64492 1.000 39.79995 ? 523 HOH   A O   1 
HETATM 1780 O O   . HOH   C 3 .   ? 13.93487  -11.35925 -29.72752 1.000 44.23314 ? 524 HOH   A O   1 
HETATM 1781 O O   . HOH   C 3 .   ? 3.32473   -30.28015 -19.18786 1.000 50.40590 ? 525 HOH   A O   1 
HETATM 1782 O O   . HOH   C 3 .   ? -19.36745 -12.10873 -16.21711 1.000 52.11194 ? 526 HOH   A O   1 
HETATM 1783 O O   . HOH   C 3 .   ? -12.03290 -7.66104  -38.47284 1.000 43.15060 ? 527 HOH   A O   1 
HETATM 1784 O O   . HOH   C 3 .   ? 0.43874   -14.90038 -1.47408  1.000 46.71972 ? 528 HOH   A O   1 
HETATM 1785 O O   . HOH   C 3 .   ? 18.11730  -19.47282 -24.70256 1.000 35.26537 ? 529 HOH   A O   1 
HETATM 1786 O O   . HOH   C 3 .   ? 12.37489  -27.42131 -19.39184 1.000 46.56294 ? 530 HOH   A O   1 
HETATM 1787 O O   . HOH   C 3 .   ? 4.05357   -9.21828  -20.30360 1.000 25.53450 ? 531 HOH   A O   1 
HETATM 1788 O O   . HOH   C 3 .   ? 8.33982   -20.59285 -9.41603  1.000 36.69687 ? 532 HOH   A O   1 
HETATM 1789 O O   . HOH   C 3 .   ? 8.80540   -15.51780 -27.79468 1.000 24.74152 ? 533 HOH   A O   1 
HETATM 1790 O O   . HOH   C 3 .   ? -10.23887 -15.04681 -28.26739 1.000 35.28724 ? 534 HOH   A O   1 
HETATM 1791 O O   . HOH   C 3 .   ? 10.46784  -21.65289 -7.01592  1.000 46.91276 ? 535 HOH   A O   1 
HETATM 1792 O O   . HOH   C 3 .   ? -4.61311  0.42995   -30.63451 1.000 33.90677 ? 536 HOH   A O   1 
HETATM 1793 O O   . HOH   C 3 .   ? -3.56265  -13.09921 -20.65446 1.000 31.01392 ? 537 HOH   A O   1 
HETATM 1794 O O   . HOH   C 3 .   ? -1.82020  -25.71269 -4.69577  1.000 29.38043 ? 538 HOH   A O   1 
HETATM 1795 O O   . HOH   C 3 .   ? 0.52249   -5.39115  -21.99014 1.000 42.59861 ? 539 HOH   A O   1 
HETATM 1796 O O   . HOH   C 3 .   ? -1.29724  -30.04843 -17.36016 1.000 43.42053 ? 540 HOH   A O   1 
HETATM 1797 O O   . HOH   C 3 .   ? -15.27207 -12.04198 -12.00143 1.000 37.19027 ? 541 HOH   A O   1 
HETATM 1798 O O   . HOH   C 3 .   ? -0.35322  -7.06123  -31.04462 1.000 38.31233 ? 542 HOH   A O   1 
HETATM 1799 O O   . HOH   C 3 .   ? 16.98976  -25.00724 -25.28369 1.000 39.66052 ? 543 HOH   A O   1 
HETATM 1800 O O   . HOH   C 3 .   ? -3.08652  -1.11645  -24.20801 1.000 33.57640 ? 544 HOH   A O   1 
HETATM 1801 O O   . HOH   C 3 .   ? 15.72824  -18.36757 -3.59223  1.000 36.58764 ? 545 HOH   A O   1 
HETATM 1802 O O   . HOH   C 3 .   ? -15.39750 -11.08818 -29.86507 1.000 34.08461 ? 546 HOH   A O   1 
HETATM 1803 O O   . HOH   C 3 .   ? 3.56596   -6.73156  -17.98094 1.000 27.56316 ? 547 HOH   A O   1 
HETATM 1804 O O   . HOH   C 3 .   ? -6.65512  -24.16412 -30.43172 1.000 51.22130 ? 548 HOH   A O   1 
HETATM 1805 O O   . HOH   C 3 .   ? -14.226   -0.652    -13.514   1.000 31.89696 ? 549 HOH   A O   1 
HETATM 1806 O O   . HOH   C 3 .   ? -17.79889 -15.10633 -12.98671 1.000 28.89984 ? 550 HOH   A O   1 
HETATM 1807 O O   . HOH   C 3 .   ? -16.20297 -3.04387  -21.28132 1.000 35.46578 ? 551 HOH   A O   1 
HETATM 1808 O O   . HOH   C 3 .   ? -5.17321  -14.23360 -22.66020 1.000 24.48884 ? 552 HOH   A O   1 
HETATM 1809 O O   . HOH   C 3 .   ? 14.22402  -15.64247 -2.11107  1.000 45.84727 ? 553 HOH   A O   1 
HETATM 1810 O O   . HOH   C 3 .   ? 3.65195   -11.98647 -38.72115 1.000 30.12310 ? 554 HOH   A O   1 
HETATM 1811 O O   . HOH   C 3 .   ? -17.37824 -28.71259 -17.13368 1.000 48.56732 ? 555 HOH   A O   1 
HETATM 1812 O O   . HOH   C 3 .   ? -1.47104  -4.48993  -33.79547 1.000 47.27502 ? 556 HOH   A O   1 
HETATM 1813 O O   . HOH   C 3 .   ? 4.94694   -30.52021 -11.41978 1.000 43.73497 ? 557 HOH   A O   1 
HETATM 1814 O O   . HOH   C 3 .   ? -8.37188  -3.88936  -10.70139 1.000 29.56108 ? 558 HOH   A O   1 
HETATM 1815 O O   . HOH   C 3 .   ? 20.92477  -14.27925 -26.67394 1.000 37.63816 ? 559 HOH   A O   1 
HETATM 1816 O O   . HOH   C 3 .   ? 1.93781   -6.05034  -26.01825 1.000 41.09371 ? 560 HOH   A O   1 
HETATM 1817 O O   . HOH   C 3 .   ? -9.857    -24.637   3.432     1.000 56.06711 ? 561 HOH   A O   1 
HETATM 1818 O O   . HOH   C 3 .   ? -6.03999  -18.88770 -39.19591 1.000 42.50719 ? 562 HOH   A O   1 
HETATM 1819 O O   . HOH   C 3 .   ? 9.41629   -0.72137  -3.32743  1.000 56.25211 ? 563 HOH   A O   1 
HETATM 1820 O O   . HOH   C 3 .   ? -18.05272 -5.69894  -25.49270 1.000 38.83041 ? 564 HOH   A O   1 
HETATM 1821 O O   . HOH   C 3 .   ? -16.31111 -25.32845 -10.73008 1.000 40.89773 ? 565 HOH   A O   1 
HETATM 1822 O O   . HOH   C 3 .   ? 8.84280   -20.51526 -4.41753  1.000 32.10228 ? 566 HOH   A O   1 
HETATM 1823 O O   . HOH   C 3 .   ? -1.28261  -26.26826 -32.36517 1.000 43.50701 ? 567 HOH   A O   1 
HETATM 1824 O O   . HOH   C 3 .   ? -13.66504 -25.73696 -7.73019  1.000 35.54077 ? 568 HOH   A O   1 
HETATM 1825 O O   . HOH   C 3 .   ? 13.76289  -20.45308 -20.71530 1.000 26.78420 ? 569 HOH   A O   1 
HETATM 1826 O O   . HOH   C 3 .   ? -16.52937 -9.05866  -14.15247 1.000 40.10962 ? 570 HOH   A O   1 
HETATM 1827 O O   . HOH   C 3 .   ? -12.33230 -26.95688 -20.28848 1.000 33.67205 ? 571 HOH   A O   1 
HETATM 1828 O O   . HOH   C 3 .   ? -3.32983  -21.11247 -0.36970  1.000 38.46654 ? 572 HOH   A O   1 
HETATM 1829 O O   . HOH   C 3 .   ? -19.48084 -13.20418 -27.21441 1.000 48.24414 ? 573 HOH   A O   1 
HETATM 1830 O O   . HOH   C 3 .   ? -14.35240 -16.09877 -26.04409 1.000 33.37833 ? 574 HOH   A O   1 
HETATM 1831 O O   . HOH   C 3 .   ? -1.62039  -8.69449  -27.88452 1.000 32.94097 ? 575 HOH   A O   1 
HETATM 1832 O O   . HOH   C 3 .   ? 1.22924   -8.69256  -27.08792 1.000 40.76288 ? 576 HOH   A O   1 
HETATM 1833 O O   . HOH   C 3 .   ? -5.66312  -11.09450 1.30747   1.000 49.17955 ? 577 HOH   A O   1 
HETATM 1834 O O   . HOH   C 3 .   ? 13.63580  -4.14032  -25.69755 1.000 24.53571 ? 578 HOH   A O   1 
HETATM 1835 O O   . HOH   C 3 .   ? -14.21076 -23.92894 -4.75597  1.000 33.75370 ? 579 HOH   A O   1 
HETATM 1836 O O   . HOH   C 3 .   ? -16.10103 -4.05447  -15.51208 1.000 41.67064 ? 580 HOH   A O   1 
HETATM 1837 O O   . HOH   C 3 .   ? -13.14448 -12.23800 -31.05497 1.000 32.75163 ? 581 HOH   A O   1 
HETATM 1838 O O   . HOH   C 3 .   ? 0.02860   -16.65225 -3.40429  1.000 32.80828 ? 582 HOH   A O   1 
HETATM 1839 O O   . HOH   C 3 .   ? -13.84823 -18.52803 -24.41336 1.000 27.59448 ? 583 HOH   A O   1 
HETATM 1840 O O   . HOH   C 3 .   ? 13.20422  -6.94162  -26.49620 1.000 28.75286 ? 584 HOH   A O   1 
HETATM 1841 O O   . HOH   C 3 .   ? 7.44386   1.96707   -12.46888 1.000 36.81601 ? 585 HOH   A O   1 
HETATM 1842 O O   . HOH   C 3 .   ? -7.468    7.622     -33.891   1.000 45.45658 ? 586 HOH   A O   1 
HETATM 1843 O O   . HOH   C 3 .   ? -18.37801 -3.08599  -35.60174 1.000 51.38378 ? 587 HOH   A O   1 
HETATM 1844 O O   . HOH   C 3 .   ? 3.95449   -22.97460 -3.37313  1.000 39.32607 ? 588 HOH   A O   1 
HETATM 1845 O O   . HOH   C 3 .   ? 8.25511   -25.76668 -26.05059 1.000 43.82065 ? 589 HOH   A O   1 
HETATM 1846 O O   . HOH   C 3 .   ? -4.60728  -3.23393  -15.91353 1.000 53.83860 ? 590 HOH   A O   1 
HETATM 1847 O O   . HOH   C 3 .   ? 1.886     -18.217   0.040     1.000 40.54904 ? 591 HOH   A O   1 
HETATM 1848 O O   . HOH   C 3 .   ? -5.18443  -5.09086  -12.02188 1.000 44.74454 ? 592 HOH   A O   1 
HETATM 1849 O O   . HOH   C 3 .   ? 1.13918   -3.17682  -24.09668 1.000 47.75308 ? 593 HOH   A O   1 
HETATM 1850 O O   . HOH   C 3 .   ? -5.45405  -12.13059 -42.14955 1.000 46.12722 ? 594 HOH   A O   1 
HETATM 1851 O O   . HOH   C 3 .   ? -5.37951  -31.86274 -7.11517  1.000 51.23495 ? 595 HOH   A O   1 
HETATM 1852 O O   . HOH   C 3 .   ? 2.05647   -26.02757 -29.33223 1.000 43.20807 ? 596 HOH   A O   1 
HETATM 1853 O O   . HOH   C 3 .   ? 10.50668  -17.75730 -38.90547 1.000 48.14784 ? 597 HOH   A O   1 
HETATM 1854 O O   . HOH   C 3 .   ? 5.47315   1.74738   -16.54449 1.000 48.12667 ? 598 HOH   A O   1 
HETATM 1855 O O   . HOH   C 3 .   ? -1.09379  -5.79122  -12.34536 1.000 46.77798 ? 599 HOH   A O   1 
HETATM 1856 O O   . HOH   C 3 .   ? 14.51015  -22.18371 -17.16392 1.000 40.07766 ? 600 HOH   A O   1 
HETATM 1857 O O   . HOH   C 3 .   ? 3.56806   0.00350   -16.53630 1.000 48.63237 ? 601 HOH   A O   1 
HETATM 1858 O O   . HOH   C 3 .   ? -14.45162 -28.97704 -17.04466 1.000 44.76314 ? 602 HOH   A O   1 
HETATM 1859 O O   . HOH   C 3 .   ? -6.759    -23.057   -1.546    1.000 41.66276 ? 603 HOH   A O   1 
HETATM 1860 O O   . HOH   C 3 .   ? -14.09119 -9.50961  -8.24241  1.000 37.25277 ? 604 HOH   A O   1 
HETATM 1861 O O   . HOH   C 3 .   ? 2.82304   -5.48903  -20.55982 1.000 45.70252 ? 605 HOH   A O   1 
HETATM 1862 O O   . HOH   C 3 .   ? 17.79595  -21.52240 -19.86489 1.000 41.97810 ? 606 HOH   A O   1 
HETATM 1863 O O   . HOH   C 3 .   ? 14.90469  -8.05493  -30.33481 1.000 45.61619 ? 607 HOH   A O   1 
HETATM 1864 O O   . HOH   C 3 .   ? 12.23186  -25.42090 -38.43220 1.000 35.61157 ? 608 HOH   A O   1 
HETATM 1865 O O   . HOH   C 3 .   ? -0.23924  -0.98811  -22.85894 1.000 55.12731 ? 609 HOH   A O   1 
HETATM 1866 O O   . HOH   C 3 .   ? -15.585   -1.906    -11.197   1.000 43.59509 ? 610 HOH   A O   1 
HETATM 1867 O O   . HOH   C 3 .   ? -9.05925  -5.65265  -39.95454 1.000 48.38325 ? 611 HOH   A O   1 
HETATM 1868 O O   . HOH   C 3 .   ? -12.55560 -16.32069 -28.14658 1.000 39.74077 ? 612 HOH   A O   1 
HETATM 1869 O O   . HOH   C 3 .   ? -14.16139 -14.17518 -2.98248  1.000 41.05435 ? 613 HOH   A O   1 
HETATM 1870 O O   . HOH   C 3 .   ? 7.67745   -14.04536 -38.32905 1.000 39.35004 ? 614 HOH   A O   1 
HETATM 1871 O O   . HOH   C 3 .   ? -3.93604  -33.16170 -10.95497 1.000 47.66720 ? 615 HOH   A O   1 
HETATM 1872 O O   . HOH   C 3 .   ? -7.50486  1.99416   -39.27822 1.000 51.21281 ? 616 HOH   A O   1 
HETATM 1873 O O   . HOH   C 3 .   ? 1.39001   -3.03301  -13.10748 1.000 54.46719 ? 617 HOH   A O   1 
HETATM 1874 O O   . HOH   C 3 .   ? -10.04566 -25.98211 -20.83772 1.000 36.88607 ? 618 HOH   A O   1 
HETATM 1875 O O   . HOH   C 3 .   ? -6.12293  3.70741   -34.60200 1.000 45.57596 ? 619 HOH   A O   1 
HETATM 1876 O O   . HOH   C 3 .   ? 6.11881   -29.83564 -24.73645 1.000 51.67814 ? 620 HOH   A O   1 
HETATM 1877 O O   . HOH   C 3 .   ? -11.89275 -9.76239  -39.79344 1.000 50.74093 ? 621 HOH   A O   1 
HETATM 1878 O O   . HOH   C 3 .   ? -3.56002  -27.25345 -3.01957  1.000 46.89509 ? 622 HOH   A O   1 
HETATM 1879 O O   . HOH   C 3 .   ? 3.56402   -9.25640  -39.32496 1.000 45.46527 ? 623 HOH   A O   1 
HETATM 1880 O O   . HOH   C 3 .   ? 5.75289   -13.12895 -39.91010 1.000 40.16779 ? 624 HOH   A O   1 
HETATM 1881 O O   . HOH   C 3 .   ? 18.36601  -3.45221  -23.49395 1.000 48.10798 ? 625 HOH   A O   1 
HETATM 1882 O O   . HOH   C 3 .   ? 6.05663   -7.07305  -36.20809 1.000 46.91064 ? 626 HOH   A O   1 
HETATM 1883 O O   . HOH   C 3 .   ? -10.48410 -8.78000  -1.35862  1.000 42.42526 ? 627 HOH   A O   1 
HETATM 1884 O O   . HOH   C 3 .   ? -18.79837 -11.61513 -21.15714 1.000 37.88650 ? 628 HOH   A O   1 
HETATM 1885 O O   . HOH   C 3 .   ? -10.171   -29.248   -30.770   1.000 52.14469 ? 629 HOH   A O   1 
HETATM 1886 O O   . HOH   C 3 .   ? 20.23278  -5.74447  -21.49473 1.000 50.31230 ? 630 HOH   A O   1 
HETATM 1887 O O   . HOH   C 3 .   ? -19.54420 -8.37626  -24.23165 1.000 63.33669 ? 631 HOH   A O   1 
HETATM 1888 O O   . HOH   C 3 .   ? 6.83931   -21.59569 -2.77734  1.000 39.43076 ? 632 HOH   A O   1 
HETATM 1889 O O   . HOH   C 3 .   ? -17.867   1.066     -21.991   1.000 49.80989 ? 633 HOH   A O   1 
HETATM 1890 O O   . HOH   C 3 .   ? 19.20729  -8.30319  -17.93580 1.000 44.97498 ? 634 HOH   A O   1 
HETATM 1891 O O   . HOH   C 3 .   ? 2.246     -0.780    -26.089   1.000 44.84235 ? 635 HOH   A O   1 
HETATM 1892 O O   . HOH   C 3 .   ? 7.86992   -29.00752 -28.26407 1.000 46.69942 ? 636 HOH   A O   1 
HETATM 1893 O O   . HOH   C 3 .   ? -16.298   3.174     -26.414   1.000 45.04450 ? 637 HOH   A O   1 
HETATM 1894 O O   . HOH   C 3 .   ? -12.51462 -12.92619 -1.08488  1.000 41.64495 ? 638 HOH   A O   1 
HETATM 1895 O O   . HOH   C 3 .   ? -7.10188  -30.79242 -9.10237  1.000 38.89849 ? 639 HOH   A O   1 
HETATM 1896 O O   . HOH   C 3 .   ? 10.18799  -29.29660 -23.99264 1.000 48.76825 ? 640 HOH   A O   1 
HETATM 1897 O O   . HOH   C 3 .   ? -10.546   -22.653   4.543     1.000 47.88561 ? 641 HOH   A O   1 
HETATM 1898 O O   . HOH   C 3 .   ? -0.00000  -0.00000  -18.47262 0.50  30.42079 ? 642 HOH   A O   1 
HETATM 1899 O O   . HOH   C 3 .   ? -12.095   -26.397   -27.766   1.000 47.00724 ? 643 HOH   A O   1 
HETATM 1900 O O   . HOH   C 3 .   ? 10.95883  -28.03928 -27.91188 1.000 45.21996 ? 644 HOH   A O   1 
HETATM 1901 O O   . HOH   C 3 .   ? 4.77334   -15.12646 -41.74152 1.000 48.49488 ? 645 HOH   A O   1 
HETATM 1902 O O   . HOH   C 3 .   ? 14.25360  -13.21261 -2.91356  1.000 55.13347 ? 646 HOH   A O   1 
HETATM 1903 O O   . HOH   C 3 .   ? 11.496    -30.139   -34.434   1.000 47.17663 ? 647 HOH   A O   1 
HETATM 1904 O O   . HOH   C 3 .   ? -20.90498 -10.97197 -19.47888 1.000 51.06637 ? 648 HOH   A O   1 
HETATM 1905 O O   . HOH   C 3 .   ? -16.37200 -12.70900 -6.31201  1.000 45.74795 ? 649 HOH   A O   1 
HETATM 1906 O O   . HOH   C 3 .   ? 21.91922  -17.78833 -25.17625 1.000 49.42027 ? 650 HOH   A O   1 
HETATM 1907 O O   . HOH   C 3 .   ? 2.03011   -0.46778  -14.30414 1.000 52.15035 ? 651 HOH   A O   1 
HETATM 1908 O O   . HOH   C 3 .   ? -3.172    2.131     -20.347   1.000 46.92111 ? 652 HOH   A O   1 
HETATM 1909 O O   . HOH   C 3 .   ? 20.39543  -6.76557  -16.25165 1.000 52.76156 ? 653 HOH   A O   1 
HETATM 1910 O O   . HOH   C 3 .   ? 0.49993   -1.28361  -16.87195 1.000 42.22014 ? 654 HOH   A O   1 
HETATM 1911 O O   . HOH   C 3 .   ? -4.02072  1.84425   -28.38642 1.000 40.84290 ? 655 HOH   A O   1 
HETATM 1912 O O   . HOH   C 3 .   ? -8.76822  -10.99104 0.20551   1.000 46.80268 ? 656 HOH   A O   1 
HETATM 1913 O O   . HOH   C 3 .   ? 9.56072   -25.24552 -14.57732 1.000 43.18526 ? 657 HOH   A O   1 
HETATM 1914 O O   . HOH   C 3 .   ? -21.08521 -12.49429 -24.79907 1.000 51.41439 ? 658 HOH   A O   1 
HETATM 1915 O O   . HOH   C 3 .   ? 19.27048  -20.36400 -22.31785 1.000 39.40285 ? 659 HOH   A O   1 
HETATM 1916 O O   . HOH   C 3 .   ? -14.55185 -14.14091 -10.18389 1.000 38.33441 ? 660 HOH   A O   1 
HETATM 1917 O O   . HOH   C 3 .   ? 9.76895   -12.82714 -37.23906 1.000 51.51813 ? 661 HOH   A O   1 
HETATM 1918 O O   . HOH   C 3 .   ? -17.07350 -15.57188 -10.14828 1.000 41.89810 ? 662 HOH   A O   1 
HETATM 1919 O O   . HOH   C 3 .   ? -6.66912  -26.84441 -23.55609 1.000 46.83336 ? 663 HOH   A O   1 
HETATM 1920 O O   . HOH   C 3 .   ? -14.86615 -9.40234  -11.19983 1.000 40.64030 ? 664 HOH   A O   1 
HETATM 1921 O O   . HOH   C 3 .   ? -8.911    8.708     -38.896   1.000 51.71651 ? 665 HOH   A O   1 
HETATM 1922 O O   . HOH   C 3 .   ? -19.68656 -5.86608  -21.62038 1.000 48.98626 ? 666 HOH   A O   1 
HETATM 1923 O O   . HOH   C 3 .   ? 10.695    -11.142   -2.056    1.000 48.14936 ? 667 HOH   A O   1 
HETATM 1924 O O   . HOH   C 3 .   ? -6.609    8.108     -39.385   1.000 53.04793 ? 668 HOH   A O   1 
HETATM 1925 O O   . HOH   C 3 .   ? 10.71502  -29.97611 -26.14544 1.000 51.47934 ? 669 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   ? 0.68778 0.70542 0.54940 -0.02635 -0.05039 -0.20336 16  GLU A N   
2    C CA  . GLU A 9   ? 0.75803 0.76648 0.61314 -0.00434 -0.04436 -0.18588 16  GLU A CA  
3    C C   . GLU A 9   ? 0.65977 0.67442 0.53878 0.00317  -0.04313 -0.16582 16  GLU A C   
4    O O   . GLU A 9   ? 0.60431 0.64903 0.49156 0.00854  -0.05177 -0.15855 16  GLU A O   
5    C CB  . GLU A 9   ? 0.79469 0.82784 0.62915 0.00858  -0.05229 -0.18669 16  GLU A CB  
6    C CG  . GLU A 9   ? 0.91021 0.92255 0.72544 0.02661  -0.04203 -0.17785 16  GLU A CG  
7    C CD  . GLU A 9   ? 0.95102 0.96772 0.77651 0.04358  -0.03802 -0.15531 16  GLU A CD  
8    O OE1 . GLU A 9   ? 0.89674 0.92464 0.74545 0.04149  -0.04099 -0.14556 16  GLU A OE1 
9    O OE2 . GLU A 9   ? 1.02820 1.03575 0.83740 0.05838  -0.03071 -0.14794 16  GLU A OE2 
10   N N   . VAL A 10  ? 0.60334 0.58969 0.49211 0.00452  -0.03202 -0.15702 17  VAL A N   
11   C CA  . VAL A 10  ? 0.46331 0.45295 0.37411 0.00860  -0.03039 -0.14054 17  VAL A CA  
12   C C   . VAL A 10  ? 0.49796 0.47593 0.40685 0.02492  -0.02194 -0.12620 17  VAL A C   
13   O O   . VAL A 10  ? 0.49725 0.45095 0.39769 0.02906  -0.01222 -0.12709 17  VAL A O   
14   C CB  . VAL A 10  ? 0.54037 0.51088 0.46532 -0.00353 -0.02494 -0.14139 17  VAL A CB  
15   C CG1 . VAL A 10  ? 0.49142 0.47096 0.43722 -0.00021 -0.02550 -0.12595 17  VAL A CG1 
16   C CG2 . VAL A 10  ? 0.58937 0.56515 0.51410 -0.02285 -0.02978 -0.15856 17  VAL A CG2 
17   N N   . GLU A 11  ? 0.41189 0.40656 0.32921 0.03371  -0.02438 -0.11333 18  GLU A N   
18   C CA  . GLU A 11  ? 0.40431 0.39063 0.32320 0.04619  -0.01581 -0.10014 18  GLU A CA  
19   C C   . GLU A 11  ? 0.37234 0.35599 0.31331 0.04371  -0.01312 -0.08986 18  GLU A C   
20   O O   . GLU A 11  ? 0.33024 0.32717 0.28336 0.03799  -0.01928 -0.08770 18  GLU A O   
21   C CB  . GLU A 11  ? 0.40152 0.40386 0.31155 0.05731  -0.01795 -0.09321 18  GLU A CB  
22   C CG  . GLU A 11  ? 0.43777 0.44096 0.32221 0.06401  -0.01843 -0.10047 18  GLU A CG  
23   C CD  . GLU A 11  ? 0.55115 0.56929 0.42479 0.07678  -0.01993 -0.09177 18  GLU A CD  
24   O OE1 . GLU A 11  ? 0.57609 0.61443 0.45603 0.07694  -0.02807 -0.08903 18  GLU A OE1 
25   O OE2 . GLU A 11  ? 0.58828 0.59661 0.44742 0.08770  -0.01127 -0.08628 18  GLU A OE2 
26   N N   . THR A 12  ? 0.36247 0.33120 0.30840 0.04860  -0.00394 -0.08365 19  THR A N   
27   C CA  . THR A 12  ? 0.32228 0.29096 0.28749 0.04733  -0.00183 -0.07421 19  THR A CA  
28   C C   . THR A 12  ? 0.31942 0.29482 0.29083 0.05549  0.00330  -0.06357 19  THR A C   
29   O O   . THR A 12  ? 0.31990 0.28946 0.28409 0.06317  0.01080  -0.06225 19  THR A O   
30   C CB  . THR A 12  ? 0.35410 0.30360 0.32217 0.04673  0.00459  -0.07511 19  THR A CB  
31   O OG1 . THR A 12  ? 0.37212 0.31035 0.33260 0.03717  0.00236  -0.08625 19  THR A OG1 
32   C CG2 . THR A 12  ? 0.33674 0.28979 0.32306 0.04650  0.00526  -0.06503 19  THR A CG2 
33   N N   . PHE A 13  ? 0.30652 0.29321 0.29123 0.05277  0.00044  -0.05677 20  PHE A N   
34   C CA  . PHE A 13  ? 0.31718 0.31054 0.30832 0.05673  0.00525  -0.04841 20  PHE A CA  
35   C C   . PHE A 13  ? 0.28304 0.28141 0.29264 0.05303  0.00577  -0.04271 20  PHE A C   
36   O O   . PHE A 13  ? 0.29172 0.29138 0.30796 0.04749  0.00042  -0.04331 20  PHE A O   
37   C CB  . PHE A 13  ? 0.33351 0.33564 0.32045 0.05677  0.00170  -0.04638 20  PHE A CB  
38   C CG  . PHE A 13  ? 0.33570 0.33847 0.30369 0.06262  -0.00006 -0.05032 20  PHE A CG  
39   C CD1 . PHE A 13  ? 0.34298 0.35214 0.30494 0.05905  -0.00907 -0.05843 20  PHE A CD1 
40   C CD2 . PHE A 13  ? 0.36553 0.36469 0.32140 0.07140  0.00737  -0.04587 20  PHE A CD2 
41   C CE1 . PHE A 13  ? 0.37618 0.39123 0.32020 0.06489  -0.01228 -0.06267 20  PHE A CE1 
42   C CE2 . PHE A 13  ? 0.41657 0.41813 0.35215 0.07882  0.00518  -0.04852 20  PHE A CE2 
43   C CZ  . PHE A 13  ? 0.40467 0.41601 0.33442 0.07585  -0.00559 -0.05719 20  PHE A CZ  
44   N N   . ALA A 14  ? 0.26215 0.26547 0.27993 0.05556  0.01235  -0.03725 21  ALA A N   
45   C CA  . ALA A 14  ? 0.26459 0.27879 0.29959 0.05133  0.01155  -0.03258 21  ALA A CA  
46   C C   . ALA A 14  ? 0.29564 0.31585 0.33296 0.04544  0.00971  -0.03104 21  ALA A C   
47   O O   . ALA A 14  ? 0.30300 0.31990 0.33271 0.04703  0.01459  -0.03024 21  ALA A O   
48   C CB  . ALA A 14  ? 0.30695 0.32859 0.35221 0.05512  0.01945  -0.02884 21  ALA A CB  
49   N N   . PHE A 15  ? 0.25361 0.28053 0.29963 0.03951  0.00408  -0.03014 22  PHE A N   
50   C CA  . PHE A 15  ? 0.27382 0.30522 0.32253 0.03379  0.00451  -0.02908 22  PHE A CA  
51   C C   . PHE A 15  ? 0.26320 0.30087 0.32025 0.03127  0.01208  -0.02737 22  PHE A C   
52   O O   . PHE A 15  ? 0.28219 0.32976 0.35006 0.03225  0.01346  -0.02613 22  PHE A O   
53   C CB  . PHE A 15  ? 0.26304 0.30121 0.31864 0.02787  -0.00210 -0.02881 22  PHE A CB  
54   C CG  . PHE A 15  ? 0.24283 0.27655 0.29232 0.02744  -0.00799 -0.03065 22  PHE A CG  
55   C CD1 . PHE A 15  ? 0.24419 0.27557 0.28596 0.02775  -0.00846 -0.03199 22  PHE A CD1 
56   C CD2 . PHE A 15  ? 0.27624 0.30896 0.32828 0.02684  -0.01203 -0.03054 22  PHE A CD2 
57   C CE1 . PHE A 15  ? 0.26739 0.30034 0.30690 0.02638  -0.01386 -0.03417 22  PHE A CE1 
58   C CE2 . PHE A 15  ? 0.26428 0.29382 0.31250 0.02401  -0.01605 -0.03299 22  PHE A CE2 
59   C CZ  . PHE A 15  ? 0.26293 0.29520 0.30636 0.02309  -0.01753 -0.03529 22  PHE A CZ  
60   N N   . GLN A 16  ? 0.27280 0.30516 0.32534 0.02796  0.01793  -0.02725 23  GLN A N   
61   C CA  . GLN A 16  ? 0.32530 0.36428 0.38793 0.02048  0.02527  -0.02744 23  GLN A CA  
62   C C   . GLN A 16  ? 0.27958 0.33654 0.35701 0.01298  0.01858  -0.02905 23  GLN A C   
63   O O   . GLN A 16  ? 0.27915 0.33750 0.35505 0.01206  0.01040  -0.02947 23  GLN A O   
64   C CB  . GLN A 16  ? 0.32132 0.34636 0.37449 0.01671  0.03335  -0.02757 23  GLN A CB  
65   C CG  . GLN A 16  ? 0.42976 0.43833 0.46716 0.02539  0.04216  -0.02423 23  GLN A CG  
66   C CD  . GLN A 16  ? 0.53930 0.53069 0.56445 0.02466  0.05023  -0.02267 23  GLN A CD  
67   O OE1 . GLN A 16  ? 0.48797 0.47516 0.50508 0.02870  0.04500  -0.02218 23  GLN A OE1 
68   N NE2 . GLN A 16  ? 0.50875 0.48971 0.53288 0.01941  0.06429  -0.02182 23  GLN A NE2 
69   N N   . ALA A 17  ? 0.28411 0.35737 0.37607 0.00783  0.02225  -0.02981 24  ALA A N   
70   C CA  . ALA A 17  ? 0.27035 0.36674 0.37648 0.00308  0.01463  -0.03079 24  ALA A CA  
71   C C   . ALA A 17  ? 0.27809 0.37396 0.38064 -0.00626 0.01019  -0.03450 24  ALA A C   
72   O O   . ALA A 17  ? 0.29193 0.39839 0.39658 -0.00581 0.00100  -0.03379 24  ALA A O   
73   C CB  . ALA A 17  ? 0.30217 0.42133 0.42618 -0.00224 0.01975  -0.03212 24  ALA A CB  
74   N N   . GLU A 18  ? 0.29712 0.37784 0.39179 -0.01353 0.01786  -0.03791 25  GLU A N   
75   C CA  . GLU A 18  ? 0.30039 0.37762 0.38981 -0.02226 0.01575  -0.04232 25  GLU A CA  
76   C C   . GLU A 18  ? 0.29354 0.36108 0.37200 -0.01503 0.00853  -0.03960 25  GLU A C   
77   O O   . GLU A 18  ? 0.28079 0.35450 0.35833 -0.01938 0.00259  -0.04165 25  GLU A O   
78   C CB  . GLU A 18  ? 0.34445 0.40188 0.42564 -0.02989 0.02856  -0.04594 25  GLU A CB  
79   C CG  . GLU A 18  ? 0.39046 0.45794 0.48389 -0.04155 0.03731  -0.05038 25  GLU A CG  
80   C CD  . GLU A 18  ? 0.50797 0.56972 0.60282 -0.03479 0.04645  -0.04558 25  GLU A CD  
81   O OE1 . GLU A 18  ? 0.43970 0.49423 0.52712 -0.02050 0.04335  -0.03940 25  GLU A OE1 
82   O OE2 . GLU A 18  ? 0.52918 0.59400 0.63225 -0.04479 0.05737  -0.04874 25  GLU A OE2 
83   N N   . ILE A 19  ? 0.30376 0.35817 0.37394 -0.00463 0.00908  -0.03552 26  ILE A N   
84   C CA  . ILE A 19  ? 0.28518 0.33409 0.34779 0.00076  0.00263  -0.03376 26  ILE A CA  
85   C C   . ILE A 19  ? 0.29733 0.35851 0.36663 0.00314  -0.00617 -0.03159 26  ILE A C   
86   O O   . ILE A 19  ? 0.28126 0.34395 0.34826 0.00212  -0.01143 -0.03112 26  ILE A O   
87   C CB  . ILE A 19  ? 0.31071 0.34635 0.36297 0.00990  0.00519  -0.03152 26  ILE A CB  
88   C CG1 . ILE A 19  ? 0.33950 0.36038 0.38093 0.01085  0.01382  -0.03146 26  ILE A CG1 
89   C CG2 . ILE A 19  ? 0.28623 0.32273 0.33523 0.01407  -0.00252 -0.03078 26  ILE A CG2 
90   C CD1 . ILE A 19  ? 0.41437 0.42797 0.45588 0.00636  0.02491  -0.03216 26  ILE A CD1 
91   N N   . ALA A 20  ? 0.24606 0.31466 0.32274 0.00734  -0.00640 -0.02951 27  ALA A N   
92   C CA  . ALA A 20  ? 0.29415 0.37161 0.37563 0.01142  -0.01274 -0.02610 27  ALA A CA  
93   C C   . ALA A 20  ? 0.28657 0.38005 0.37294 0.00576  -0.01769 -0.02630 27  ALA A C   
94   O O   . ALA A 20  ? 0.27028 0.36545 0.35397 0.00817  -0.02293 -0.02310 27  ALA A O   
95   C CB  . ALA A 20  ? 0.24343 0.32659 0.33210 0.01848  -0.01029 -0.02347 27  ALA A CB  
96   N N   . GLN A 21  ? 0.25157 0.35649 0.34385 -0.00252 -0.01547 -0.03050 28  GLN A N   
97   C CA  . GLN A 21  ? 0.23175 0.35513 0.32756 -0.00914 -0.02096 -0.03263 28  GLN A CA  
98   C C   . GLN A 21  ? 0.30118 0.41370 0.38494 -0.01327 -0.02279 -0.03463 28  GLN A C   
99   O O   . GLN A 21  ? 0.31607 0.43808 0.39720 -0.01275 -0.02907 -0.03274 28  GLN A O   
100  C CB  . GLN A 21  ? 0.31769 0.45584 0.42307 -0.01999 -0.01716 -0.03912 28  GLN A CB  
101  C CG  . GLN A 21  ? 0.40883 0.56364 0.51432 -0.03095 -0.02203 -0.04523 28  GLN A CG  
102  C CD  . GLN A 21  ? 0.46262 0.63761 0.58095 -0.04395 -0.01874 -0.05320 28  GLN A CD  
103  O OE1 . GLN A 21  ? 0.51192 0.67296 0.63083 -0.05113 -0.00827 -0.05750 28  GLN A OE1 
104  N NE2 . GLN A 21  ? 0.55922 0.76761 0.68698 -0.04769 -0.02723 -0.05548 28  GLN A NE2 
105  N N   . LEU A 22  ? 0.26529 0.35810 0.34068 -0.01563 -0.01662 -0.03750 29  LEU A N   
106  C CA  . LEU A 22  ? 0.27415 0.35644 0.33859 -0.01746 -0.01684 -0.03878 29  LEU A CA  
107  C C   . LEU A 22  ? 0.27218 0.35297 0.33386 -0.01035 -0.02206 -0.03304 29  LEU A C   
108  O O   . LEU A 22  ? 0.26817 0.35156 0.32456 -0.01189 -0.02512 -0.03234 29  LEU A O   
109  C CB  . LEU A 22  ? 0.27638 0.33867 0.33298 -0.01670 -0.00857 -0.04058 29  LEU A CB  
110  C CG  . LEU A 22  ? 0.30981 0.36185 0.35645 -0.01506 -0.00754 -0.04058 29  LEU A CG  
111  C CD1 . LEU A 22  ? 0.34128 0.39541 0.38259 -0.02418 -0.00662 -0.04619 29  LEU A CD1 
112  C CD2 . LEU A 22  ? 0.32482 0.36068 0.36476 -0.00932 -0.00009 -0.03973 29  LEU A CD2 
113  N N   . MET A 23  ? 0.24326 0.31858 0.30743 -0.00327 -0.02205 -0.02935 30  MET A N   
114  C CA  . MET A 23  ? 0.25707 0.32698 0.31846 0.00129  -0.02476 -0.02529 30  MET A CA  
115  C C   . MET A 23  ? 0.25752 0.33702 0.32036 0.00354  -0.02923 -0.02036 30  MET A C   
116  O O   . MET A 23  ? 0.27012 0.34669 0.32756 0.00380  -0.03058 -0.01724 30  MET A O   
117  C CB  . MET A 23  ? 0.23771 0.29932 0.30052 0.00672  -0.02289 -0.02478 30  MET A CB  
118  C CG  . MET A 23  ? 0.26239 0.31519 0.32009 0.00713  -0.02057 -0.02755 30  MET A CG  
119  S SD  . MET A 23  ? 0.29697 0.34247 0.35331 0.01295  -0.01938 -0.02859 30  MET A SD  
120  C CE  . MET A 23  ? 0.33046 0.37183 0.38543 0.01119  -0.02250 -0.02903 30  MET A CE  
121  N N   . SER A 24  ? 0.27308 0.36595 0.34301 0.00582  -0.03094 -0.01901 31  SER A N   
122  C CA  . SER A 24  ? 0.27309 0.37803 0.34352 0.01099  -0.03541 -0.01285 31  SER A CA  
123  C C   . SER A 24  ? 0.30583 0.42260 0.37066 0.00529  -0.03943 -0.01445 31  SER A C   
124  O O   . SER A 24  ? 0.33112 0.44967 0.38909 0.00963  -0.04209 -0.00846 31  SER A O   
125  C CB  . SER A 24  ? 0.32105 0.44193 0.40239 0.01672  -0.03620 -0.01066 31  SER A CB  
126  O OG  . SER A 24  ? 0.47724 0.62135 0.56127 0.01971  -0.04194 -0.00697 31  SER A OG  
127  N N   . LEU A 25  ? 0.26946 0.39095 0.33451 -0.00443 -0.03855 -0.02261 32  LEU A N   
128  C CA  . LEU A 25  ? 0.25047 0.37975 0.30721 -0.01103 -0.04132 -0.02624 32  LEU A CA  
129  C C   . LEU A 25  ? 0.32364 0.43641 0.36879 -0.01042 -0.03890 -0.02422 32  LEU A C   
130  O O   . LEU A 25  ? 0.28706 0.40526 0.32319 -0.01004 -0.04173 -0.02182 32  LEU A O   
131  C CB  . LEU A 25  ? 0.32671 0.45913 0.38475 -0.02278 -0.03843 -0.03677 32  LEU A CB  
132  C CG  . LEU A 25  ? 0.39101 0.54437 0.46224 -0.02719 -0.03998 -0.04067 32  LEU A CG  
133  C CD1 . LEU A 25  ? 0.46162 0.61029 0.53167 -0.04135 -0.03395 -0.05206 32  LEU A CD1 
134  C CD2 . LEU A 25  ? 0.38461 0.56809 0.45857 -0.02527 -0.04935 -0.03855 32  LEU A CD2 
135  N N   . ILE A 26  ? 0.26423 0.35931 0.30951 -0.00985 -0.03360 -0.02492 33  ILE A N   
136  C CA  . ILE A 26  ? 0.30193 0.38579 0.33981 -0.00931 -0.03090 -0.02293 33  ILE A CA  
137  C C   . ILE A 26  ? 0.34449 0.42686 0.38040 -0.00358 -0.03251 -0.01448 33  ILE A C   
138  O O   . ILE A 26  ? 0.31282 0.39304 0.34048 -0.00394 -0.03140 -0.01143 33  ILE A O   
139  C CB  . ILE A 26  ? 0.26122 0.33268 0.30177 -0.00882 -0.02602 -0.02540 33  ILE A CB  
140  C CG1 . ILE A 26  ? 0.29547 0.36310 0.33280 -0.01308 -0.02165 -0.03208 33  ILE A CG1 
141  C CG2 . ILE A 26  ? 0.27620 0.34142 0.31442 -0.00763 -0.02381 -0.02254 33  ILE A CG2 
142  C CD1 . ILE A 26  ? 0.30216 0.35968 0.34098 -0.00949 -0.01685 -0.03313 33  ILE A CD1 
143  N N   . ILE A 27  ? 0.28148 0.36283 0.32345 0.00220  -0.03355 -0.01023 34  ILE A N   
144  C CA  . ILE A 27  ? 0.31723 0.38996 0.35546 0.00789  -0.03212 -0.00203 34  ILE A CA  
145  C C   . ILE A 27  ? 0.35217 0.43584 0.38318 0.01328  -0.03558 0.00506  34  ILE A C   
146  O O   . ILE A 27  ? 0.40407 0.47944 0.42599 0.01617  -0.03283 0.01201  34  ILE A O   
147  C CB  . ILE A 27  ? 0.32502 0.38875 0.36962 0.01296  -0.03027 -0.00051 34  ILE A CB  
148  C CG1 . ILE A 27  ? 0.27309 0.32600 0.32098 0.00796  -0.02715 -0.00687 34  ILE A CG1 
149  C CG2 . ILE A 27  ? 0.39897 0.45169 0.43825 0.02041  -0.02740 0.00864  34  ILE A CG2 
150  C CD1 . ILE A 27  ? 0.31584 0.36194 0.36855 0.01167  -0.02583 -0.00862 34  ILE A CD1 
151  N N   . ASN A 28  ? 0.34572 0.44973 0.38015 0.01444  -0.04132 0.00342  35  ASN A N   
152  C CA  . ASN A 28  ? 0.35989 0.48050 0.38876 0.02226  -0.04632 0.01084  35  ASN A CA  
153  C C   . ASN A 28  ? 0.36360 0.49949 0.38246 0.01684  -0.05086 0.00726  35  ASN A C   
154  O O   . ASN A 28  ? 0.40780 0.55600 0.41727 0.02427  -0.05484 0.01462  35  ASN A O   
155  C CB  . ASN A 28  ? 0.38481 0.52535 0.42576 0.02785  -0.05069 0.01135  35  ASN A CB  
156  C CG  . ASN A 28  ? 0.50370 0.62919 0.55055 0.03676  -0.04573 0.01691  35  ASN A CG  
157  O OD1 . ASN A 28  ? 0.49287 0.59598 0.53198 0.04189  -0.04022 0.02360  35  ASN A OD1 
158  N ND2 . ASN A 28  ? 0.54823 0.68386 0.60819 0.03751  -0.04622 0.01329  35  ASN A ND2 
159  N N   . THR A 29  ? 0.30094 0.43606 0.31966 0.00517  -0.04992 -0.00368 36  THR A N   
160  C CA  . THR A 29  ? 0.29847 0.44608 0.30572 -0.00107 -0.05334 -0.00918 36  THR A CA  
161  C C   . THR A 29  ? 0.34914 0.48402 0.34046 0.00135  -0.04944 -0.00350 36  THR A C   
162  O O   . THR A 29  ? 0.35038 0.46478 0.34209 0.00004  -0.04210 -0.00249 36  THR A O   
163  C CB  . THR A 29  ? 0.31868 0.46318 0.32860 -0.01384 -0.05064 -0.02266 36  THR A CB  
164  O OG1 . THR A 29  ? 0.35184 0.50842 0.37627 -0.01700 -0.05285 -0.02750 36  THR A OG1 
165  C CG2 . THR A 29  ? 0.36423 0.51795 0.35971 -0.02165 -0.05280 -0.03041 36  THR A CG2 
166  N N   . PHE A 30  ? 0.32601 0.47527 0.30324 0.00461  -0.05415 -0.00015 37  PHE A N   
167  C CA  . PHE A 30  ? 0.35216 0.48949 0.31210 0.00587  -0.04907 0.00445  37  PHE A CA  
168  C C   . PHE A 30  ? 0.35711 0.48593 0.31229 -0.00546 -0.04421 -0.00732 37  PHE A C   
169  O O   . PHE A 30  ? 0.36932 0.50994 0.32044 -0.01339 -0.04798 -0.01835 37  PHE A O   
170  C CB  . PHE A 30  ? 0.35637 0.51189 0.29906 0.01340  -0.05530 0.01115  37  PHE A CB  
171  C CG  . PHE A 30  ? 0.39026 0.53233 0.31332 0.01567  -0.04860 0.01727  37  PHE A CG  
172  C CD1 . PHE A 30  ? 0.44193 0.56258 0.36272 0.02282  -0.03979 0.02994  37  PHE A CD1 
173  C CD2 . PHE A 30  ? 0.39534 0.54411 0.30172 0.00934  -0.04943 0.00940  37  PHE A CD2 
174  C CE1 . PHE A 30  ? 0.41930 0.52725 0.32266 0.02387  -0.03160 0.03586  37  PHE A CE1 
175  C CE2 . PHE A 30  ? 0.42662 0.56269 0.31434 0.01180  -0.04174 0.01529  37  PHE A CE2 
176  C CZ  . PHE A 30  ? 0.44261 0.55911 0.32959 0.01913  -0.03267 0.02907  37  PHE A CZ  
177  N N   . TYR A 31  ? 0.33263 0.44144 0.28782 -0.00625 -0.03506 -0.00526 38  TYR A N   
178  C CA  . TYR A 31  ? 0.34445 0.44408 0.29722 -0.01395 -0.02880 -0.01498 38  TYR A CA  
179  C C   . TYR A 31  ? 0.33530 0.42061 0.28622 -0.01177 -0.01948 -0.00879 38  TYR A C   
180  O O   . TYR A 31  ? 0.34877 0.42599 0.31323 -0.01044 -0.01629 -0.00509 38  TYR A O   
181  C CB  . TYR A 31  ? 0.36169 0.45706 0.32992 -0.01855 -0.02807 -0.02296 38  TYR A CB  
182  C CG  . TYR A 31  ? 0.36391 0.44790 0.32804 -0.02369 -0.02034 -0.03164 38  TYR A CG  
183  C CD1 . TYR A 31  ? 0.40311 0.48866 0.35348 -0.03022 -0.01964 -0.04139 38  TYR A CD1 
184  C CD2 . TYR A 31  ? 0.35925 0.43155 0.33214 -0.02142 -0.01329 -0.03030 38  TYR A CD2 
185  C CE1 . TYR A 31  ? 0.47714 0.54813 0.42122 -0.03326 -0.01040 -0.04886 38  TYR A CE1 
186  C CE2 . TYR A 31  ? 0.38958 0.45207 0.35788 -0.02293 -0.00526 -0.03672 38  TYR A CE2 
187  C CZ  . TYR A 31  ? 0.44347 0.50300 0.39668 -0.02830 -0.00302 -0.04555 38  TYR A CZ  
188  O OH  . TYR A 31  ? 0.48930 0.53499 0.43568 -0.02839 0.00693  -0.05158 38  TYR A OH  
189  N N   . SER A 32  ? 0.33162 0.41524 0.26613 -0.01224 -0.01478 -0.00853 39  SER A N   
190  C CA  . SER A 32  ? 0.32186 0.39545 0.25454 -0.01010 -0.00535 -0.00077 39  SER A CA  
191  C C   . SER A 32  ? 0.35815 0.42500 0.30196 -0.01345 0.00280  -0.00597 39  SER A C   
192  O O   . SER A 32  ? 0.39218 0.45454 0.34346 -0.01326 0.00986  -0.00047 39  SER A O   
193  C CB  . SER A 32  ? 0.38449 0.45955 0.29391 -0.00799 -0.00226 0.00291  39  SER A CB  
194  O OG  . SER A 32  ? 0.38577 0.46957 0.28422 -0.00202 -0.00989 0.01023  39  SER A OG  
195  N N   . ASN A 33  ? 0.35473 0.42142 0.30068 -0.01626 0.00242  -0.01613 40  ASN A N   
196  C CA  . ASN A 33  ? 0.36976 0.43133 0.32247 -0.01624 0.01085  -0.02043 40  ASN A CA  
197  C C   . ASN A 33  ? 0.34514 0.40742 0.31903 -0.01507 0.00958  -0.01945 40  ASN A C   
198  O O   . ASN A 33  ? 0.31398 0.37391 0.29387 -0.01417 0.01011  -0.02501 40  ASN A O   
199  C CB  . ASN A 33  ? 0.40792 0.46435 0.34932 -0.01854 0.01284  -0.03105 40  ASN A CB  
200  C CG  . ASN A 33  ? 0.40728 0.45643 0.35205 -0.01528 0.02320  -0.03459 40  ASN A CG  
201  O OD1 . ASN A 33  ? 0.39777 0.44957 0.34642 -0.01175 0.03041  -0.03002 40  ASN A OD1 
202  N ND2 . ASN A 33  ? 0.41118 0.45139 0.35419 -0.01600 0.02500  -0.04243 40  ASN A ND2 
203  N N   . LYS A 34  ? 0.33029 0.34091 0.28224 0.01516  -0.03300 -0.00751 41  LYS A N   
204  C CA  . LYS A 34  ? 0.28607 0.31924 0.26597 0.01842  -0.02233 -0.00643 41  LYS A CA  
205  C C   . LYS A 34  ? 0.27629 0.29762 0.25221 0.02067  -0.01133 -0.01423 41  LYS A C   
206  O O   . LYS A 34  ? 0.27696 0.31194 0.27127 0.02028  -0.00654 -0.01399 41  LYS A O   
207  C CB  . LYS A 34  ? 0.31789 0.36229 0.30809 0.02905  -0.01447 -0.00351 41  LYS A CB  
208  C CG  . LYS A 34  ? 0.27551 0.33890 0.27593 0.03091  -0.02366 0.00583  41  LYS A CG  
209  C CD  . LYS A 34  ? 0.34211 0.40885 0.34734 0.04468  -0.01626 0.00731  41  LYS A CD  
210  C CE  . LYS A 34  ? 0.33237 0.42079 0.34882 0.05107  -0.02413 0.01738  41  LYS A CE  
211  N NZ  . LYS A 34  ? 0.26865 0.39193 0.31091 0.05515  -0.02314 0.02491  41  LYS A NZ  
212  N N   . GLU A 35  ? 0.30514 0.30323 0.25664 0.02452  -0.00715 -0.01990 42  GLU A N   
213  C CA  . GLU A 35  ? 0.33793 0.33109 0.28973 0.02919  0.00469  -0.02468 42  GLU A CA  
214  C C   . GLU A 35  ? 0.33752 0.32761 0.29320 0.02365  0.00047  -0.02785 42  GLU A C   
215  O O   . GLU A 35  ? 0.34773 0.33917 0.31017 0.02732  0.00959  -0.03052 42  GLU A O   
216  C CB  . GLU A 35  ? 0.35857 0.33264 0.28283 0.03812  0.01169  -0.02763 42  GLU A CB  
217  C CG  . GLU A 35  ? 0.38584 0.33125 0.27511 0.03900  0.00100  -0.03284 42  GLU A CG  
218  C CD  . GLU A 35  ? 0.49316 0.42090 0.34908 0.05359  0.01033  -0.03464 42  GLU A CD  
219  O OE1 . GLU A 35  ? 0.57165 0.50499 0.42332 0.05686  0.01473  -0.02948 42  GLU A OE1 
220  O OE2 . GLU A 35  ? 0.60562 0.51104 0.43475 0.06300  0.01177  -0.04078 42  GLU A OE2 
221  N N   . ILE A 36  ? 0.31858 0.30437 0.27045 0.01358  -0.01463 -0.02585 43  ILE A N   
222  C CA  . ILE A 36  ? 0.34233 0.32313 0.29696 0.00595  -0.02070 -0.02656 43  ILE A CA  
223  C C   . ILE A 36  ? 0.30987 0.31787 0.29504 0.00508  -0.01238 -0.02303 43  ILE A C   
224  O O   . ILE A 36  ? 0.27894 0.28273 0.26628 0.00113  -0.01351 -0.02405 43  ILE A O   
225  C CB  . ILE A 36  ? 0.34872 0.32079 0.29533 -0.00909 -0.04235 -0.02085 43  ILE A CB  
226  C CG1 . ILE A 36  ? 0.39454 0.40043 0.36719 -0.01573 -0.04777 -0.00892 43  ILE A CG1 
227  C CG2 . ILE A 36  ? 0.44163 0.37290 0.34562 -0.00701 -0.05372 -0.02719 43  ILE A CG2 
228  C CD1 . ILE A 36  ? 0.51341 0.54963 0.51551 -0.02600 -0.05135 0.00235  43  ILE A CD1 
229  N N   . PHE A 37  ? 0.25857 0.28968 0.26250 0.01038  -0.00469 -0.01937 44  PHE A N   
230  C CA  . PHE A 37  ? 0.28688 0.33723 0.31102 0.01272  0.00250  -0.01729 44  PHE A CA  
231  C C   . PHE A 37  ? 0.26037 0.29820 0.28113 0.01580  0.01005  -0.02393 44  PHE A C   
232  O O   . PHE A 37  ? 0.26261 0.30700 0.29228 0.01362  0.01125  -0.02311 44  PHE A O   
233  C CB  . PHE A 37  ? 0.26995 0.33486 0.30396 0.02255  0.00894  -0.01499 44  PHE A CB  
234  C CG  . PHE A 37  ? 0.28855 0.33845 0.31524 0.02942  0.01649  -0.02036 44  PHE A CG  
235  C CD1 . PHE A 37  ? 0.27127 0.31038 0.28627 0.03091  0.01622  -0.02049 44  PHE A CD1 
236  C CD2 . PHE A 37  ? 0.28205 0.32877 0.31315 0.03250  0.02223  -0.02324 44  PHE A CD2 
237  C CE1 . PHE A 37  ? 0.30366 0.33338 0.31517 0.03441  0.02254  -0.02101 44  PHE A CE1 
238  C CE2 . PHE A 37  ? 0.28217 0.31732 0.30979 0.03463  0.02584  -0.02428 44  PHE A CE2 
239  C CZ  . PHE A 37  ? 0.28751 0.31634 0.30725 0.03495  0.02644  -0.02204 44  PHE A CZ  
240  N N   . LEU A 38  ? 0.27917 0.30213 0.28804 0.02138  0.01542  -0.02853 45  LEU A N   
241  C CA  . LEU A 38  ? 0.26368 0.28275 0.27544 0.02517  0.02287  -0.03147 45  LEU A CA  
242  C C   . LEU A 38  ? 0.29272 0.29823 0.29458 0.02320  0.01909  -0.03470 45  LEU A C   
243  O O   . LEU A 38  ? 0.31314 0.32072 0.32306 0.02309  0.02135  -0.03541 45  LEU A O   
244  C CB  . LEU A 38  ? 0.27627 0.29192 0.28286 0.03177  0.03056  -0.03069 45  LEU A CB  
245  C CG  . LEU A 38  ? 0.27207 0.29202 0.28879 0.03454  0.03742  -0.02940 45  LEU A CG  
246  C CD1 . LEU A 38  ? 0.27320 0.30058 0.30578 0.03066  0.03564  -0.02797 45  LEU A CD1 
247  C CD2 . LEU A 38  ? 0.33335 0.35719 0.34781 0.04023  0.04553  -0.02387 45  LEU A CD2 
248  N N   . ARG A 39  ? 0.29655 0.28321 0.27690 0.02190  0.01120  -0.03679 46  ARG A N   
249  C CA  . ARG A 39  ? 0.32067 0.28524 0.28495 0.01930  0.00290  -0.03991 46  ARG A CA  
250  C C   . ARG A 39  ? 0.33035 0.30627 0.31126 0.00717  -0.00398 -0.03485 46  ARG A C   
251  O O   . ARG A 39  ? 0.31013 0.27772 0.28992 0.00662  -0.00484 -0.03611 46  ARG A O   
252  C CB  . ARG A 39  ? 0.36881 0.30470 0.30193 0.01748  -0.01000 -0.04243 46  ARG A CB  
253  C CG  . ARG A 39  ? 0.43195 0.33376 0.34015 0.01419  -0.02338 -0.04592 46  ARG A CG  
254  C CD  . ARG A 39  ? 0.48689 0.35235 0.35830 0.00975  -0.04201 -0.04819 46  ARG A CD  
255  N NE  . ARG A 39  ? 0.53319 0.41534 0.42211 -0.01055 -0.05687 -0.03804 46  ARG A NE  
256  C CZ  . ARG A 39  ? 0.56421 0.43187 0.43547 -0.01805 -0.07257 -0.03576 46  ARG A CZ  
257  N NH1 . ARG A 39  ? 0.56454 0.39364 0.39295 -0.00657 -0.07655 -0.04481 46  ARG A NH1 
258  N NH2 . ARG A 39  ? 0.52219 0.41646 0.41870 -0.03623 -0.08453 -0.02284 46  ARG A NH2 
259  N N   . GLU A 40  ? 0.28810 0.28563 0.28475 -0.00137 -0.00832 -0.02735 47  GLU A N   
260  C CA  . GLU A 40  ? 0.28845 0.30288 0.30128 -0.01195 -0.01334 -0.01889 47  GLU A CA  
261  C C   . GLU A 40  ? 0.27381 0.30271 0.30108 -0.00561 -0.00160 -0.01982 47  GLU A C   
262  O O   . GLU A 40  ? 0.27143 0.30202 0.30268 -0.01142 -0.00420 -0.01606 47  GLU A O   
263  C CB  . GLU A 40  ? 0.24880 0.29126 0.27795 -0.01907 -0.01846 -0.00754 47  GLU A CB  
264  C CG  . GLU A 40  ? 0.32037 0.34705 0.33461 -0.02832 -0.03440 -0.00508 47  GLU A CG  
265  C CD  . GLU A 40  ? 0.41187 0.40682 0.40608 -0.04167 -0.05200 -0.00432 47  GLU A CD  
266  O OE1 . GLU A 40  ? 0.40935 0.40880 0.41216 -0.04937 -0.05424 0.00121  47  GLU A OE1 
267  O OE2 . GLU A 40  ? 0.45073 0.41016 0.41498 -0.04270 -0.06395 -0.01029 47  GLU A OE2 
268  N N   . LEU A 41  ? 0.24442 0.28141 0.27760 0.00502  0.00918  -0.02368 48  LEU A N   
269  C CA  . LEU A 41  ? 0.27706 0.32186 0.31894 0.01013  0.01648  -0.02464 48  LEU A CA  
270  C C   . LEU A 41  ? 0.26143 0.28970 0.29773 0.01177  0.01761  -0.02971 48  LEU A C   
271  O O   . LEU A 41  ? 0.28457 0.31502 0.32504 0.01112  0.01829  -0.02887 48  LEU A O   
272  C CB  . LEU A 41  ? 0.25190 0.30224 0.29714 0.01911  0.02287  -0.02652 48  LEU A CB  
273  C CG  . LEU A 41  ? 0.24278 0.31106 0.29321 0.02252  0.02305  -0.02108 48  LEU A CG  
274  C CD1 . LEU A 41  ? 0.25562 0.31830 0.30222 0.03228  0.02658  -0.02414 48  LEU A CD1 
275  C CD2 . LEU A 41  ? 0.24131 0.32973 0.29923 0.02374  0.02487  -0.01423 48  LEU A CD2 
276  N N   . ILE A 42  ? 0.25376 0.26714 0.27968 0.01602  0.01850  -0.03396 49  ILE A N   
277  C CA  . ILE A 42  ? 0.26469 0.26603 0.28572 0.02105  0.02030  -0.03690 49  ILE A CA  
278  C C   . ILE A 42  ? 0.30309 0.28868 0.31363 0.01547  0.01145  -0.03685 49  ILE A C   
279  O O   . ILE A 42  ? 0.29271 0.27426 0.30514 0.01693  0.01138  -0.03700 49  ILE A O   
280  C CB  . ILE A 42  ? 0.30185 0.29546 0.31259 0.03123  0.02590  -0.03921 49  ILE A CB  
281  C CG1 . ILE A 42  ? 0.26963 0.28079 0.29556 0.03373  0.03358  -0.03558 49  ILE A CG1 
282  C CG2 . ILE A 42  ? 0.32219 0.30271 0.32326 0.04090  0.02767  -0.04130 49  ILE A CG2 
283  C CD1 . ILE A 42  ? 0.31689 0.32899 0.33570 0.04293  0.04120  -0.03347 49  ILE A CD1 
284  N N   . SER A 43  ? 0.28627 0.26074 0.28483 0.00746  0.00141  -0.03529 50  SER A N   
285  C CA  . SER A 43  ? 0.32797 0.28500 0.31637 -0.00240 -0.01107 -0.03229 50  SER A CA  
286  C C   . SER A 43  ? 0.31501 0.29332 0.32218 -0.01068 -0.01031 -0.02448 50  SER A C   
287  O O   . SER A 43  ? 0.29013 0.25617 0.29245 -0.01383 -0.01511 -0.02296 50  SER A O   
288  C CB  . SER A 43  ? 0.37865 0.32286 0.35389 -0.01389 -0.02558 -0.02863 50  SER A CB  
289  O OG  . SER A 43  ? 0.44504 0.36683 0.40785 -0.02638 -0.04152 -0.02394 50  SER A OG  
290  N N   . ASN A 44  ? 0.24763 0.25631 0.27290 -0.01244 -0.00442 -0.01885 51  ASN A N   
291  C CA  . ASN A 44  ? 0.26472 0.29449 0.30287 -0.01540 -0.00095 -0.01133 51  ASN A CA  
292  C C   . ASN A 44  ? 0.23962 0.26271 0.27678 -0.00686 0.00524  -0.01734 51  ASN A C   
293  O O   . ASN A 44  ? 0.27648 0.29946 0.31352 -0.01066 0.00324  -0.01300 51  ASN A O   
294  C CB  . ASN A 44  ? 0.25815 0.31872 0.30987 -0.01129 0.00651  -0.00592 51  ASN A CB  
295  C CG  . ASN A 44  ? 0.36711 0.44542 0.42695 -0.02195 -0.00069 0.00601  51  ASN A CG  
296  O OD1 . ASN A 44  ? 0.32093 0.38487 0.37468 -0.03551 -0.01391 0.01037  51  ASN A OD1 
297  N ND2 . ASN A 44  ? 0.31575 0.42341 0.38779 -0.01548 0.00612  0.01210  51  ASN A ND2 
298  N N   . SER A 45  ? 0.24077 0.25919 0.27793 0.00320  0.01132  -0.02524 52  SER A N   
299  C CA  . SER A 45  ? 0.26766 0.28153 0.30671 0.00907  0.01410  -0.02847 52  SER A CA  
300  C C   . SER A 45  ? 0.26130 0.25665 0.29231 0.00890  0.00890  -0.02944 52  SER A C   
301  O O   . SER A 45  ? 0.26398 0.25740 0.29608 0.00873  0.00724  -0.02784 52  SER A O   
302  C CB  . SER A 45  ? 0.24497 0.26080 0.28913 0.01653  0.01929  -0.03234 52  SER A CB  
303  O OG  . SER A 45  ? 0.28297 0.30886 0.33041 0.01794  0.02194  -0.03192 52  SER A OG  
304  N N   . SER A 46  ? 0.26611 0.24368 0.28458 0.01081  0.00531  -0.03237 53  SER A N   
305  C CA  . SER A 46  ? 0.29018 0.24335 0.29439 0.01456  -0.00062 -0.03415 53  SER A CA  
306  C C   . SER A 46  ? 0.32723 0.27196 0.32672 0.00197  -0.01069 -0.02800 53  SER A C   
307  O O   . SER A 46  ? 0.31076 0.24317 0.30547 0.00410  -0.01427 -0.02735 53  SER A O   
308  C CB  . SER A 46  ? 0.29240 0.22057 0.27433 0.02181  -0.00389 -0.03943 53  SER A CB  
309  O OG  . SER A 46  ? 0.35579 0.25282 0.31641 0.02899  -0.01094 -0.04215 53  SER A OG  
310  N N   . ASP A 47  ? 0.29075 0.24465 0.29305 -0.01169 -0.01582 -0.02099 54  ASP A N   
311  C CA  . ASP A 47  ? 0.30225 0.25664 0.30484 -0.02582 -0.02444 -0.01026 54  ASP A CA  
312  C C   . ASP A 47  ? 0.31744 0.29114 0.33132 -0.02325 -0.01679 -0.00676 54  ASP A C   
313  O O   . ASP A 47  ? 0.31040 0.27455 0.31892 -0.02895 -0.02287 -0.00107 54  ASP A O   
314  C CB  . ASP A 47  ? 0.31196 0.28481 0.32275 -0.04103 -0.02995 0.00133  54  ASP A CB  
315  C CG  . ASP A 47  ? 0.41339 0.35946 0.40755 -0.04884 -0.04447 0.00042  54  ASP A CG  
316  O OD1 . ASP A 47  ? 0.46294 0.36927 0.43226 -0.04130 -0.05108 -0.00968 54  ASP A OD1 
317  O OD2 . ASP A 47  ? 0.42905 0.39363 0.43306 -0.06109 -0.04990 0.01043  54  ASP A OD2 
318  N N   . ALA A 48  ? 0.27126 0.26773 0.29658 -0.01486 -0.00532 -0.00981 55  ALA A N   
319  C CA  . ALA A 48  ? 0.28785 0.29618 0.31626 -0.01096 -0.00011 -0.00771 55  ALA A CA  
320  C C   . ALA A 48  ? 0.26547 0.25607 0.28945 -0.00476 -0.00276 -0.01324 55  ALA A C   
321  O O   . ALA A 48  ? 0.28068 0.26983 0.30095 -0.00595 -0.00481 -0.00933 55  ALA A O   
322  C CB  . ALA A 48  ? 0.28459 0.31077 0.31838 -0.00224 0.00909  -0.01097 55  ALA A CB  
323  N N   . LEU A 49  ? 0.29530 0.27517 0.32002 0.00287  -0.00237 -0.02058 56  LEU A N   
324  C CA  . LEU A 49  ? 0.27024 0.23892 0.29458 0.01058  -0.00468 -0.02298 56  LEU A CA  
325  C C   . LEU A 49  ? 0.30092 0.24605 0.31145 0.00816  -0.01367 -0.02043 56  LEU A C   
326  O O   . LEU A 49  ? 0.30783 0.24692 0.31718 0.01077  -0.01735 -0.01844 56  LEU A O   
327  C CB  . LEU A 49  ? 0.26054 0.23101 0.29068 0.02121  0.00035  -0.02779 56  LEU A CB  
328  C CG  . LEU A 49  ? 0.27876 0.26871 0.32273 0.02209  0.00616  -0.02828 56  LEU A CG  
329  C CD1 . LEU A 49  ? 0.29177 0.28583 0.33931 0.02898  0.01207  -0.03022 56  LEU A CD1 
330  C CD2 . LEU A 49  ? 0.28250 0.27884 0.33642 0.02362  0.00323  -0.02554 56  LEU A CD2 
331  N N   . ASP A 50  ? 0.30408 0.23143 0.30145 0.00279  -0.01983 -0.02007 57  ASP A N   
332  C CA  . ASP A 50  ? 0.34422 0.24124 0.32335 -0.00188 -0.03237 -0.01666 57  ASP A CA  
333  C C   . ASP A 50  ? 0.36568 0.27091 0.34812 -0.01406 -0.03611 -0.00634 57  ASP A C   
334  O O   . ASP A 50  ? 0.36737 0.25232 0.33929 -0.01382 -0.04405 -0.00359 57  ASP A O   
335  C CB  . ASP A 50  ? 0.36475 0.23779 0.32626 -0.01143 -0.04341 -0.01550 57  ASP A CB  
336  C CG  . ASP A 50  ? 0.43118 0.28490 0.37773 0.00271  -0.04213 -0.02596 57  ASP A CG  
337  O OD1 . ASP A 50  ? 0.45407 0.31170 0.40323 0.02195  -0.03233 -0.03268 57  ASP A OD1 
338  O OD2 . ASP A 50  ? 0.44391 0.27720 0.37387 -0.00567 -0.05245 -0.02575 57  ASP A OD2 
339  N N   . LYS A 51  ? 0.32116 0.25573 0.31573 -0.02318 -0.03020 0.00059  58  LYS A N   
340  C CA  . LYS A 51  ? 0.31926 0.26541 0.31438 -0.03289 -0.03149 0.01277  58  LYS A CA  
341  C C   . LYS A 51  ? 0.30369 0.25052 0.29782 -0.02347 -0.02831 0.00990  58  LYS A C   
342  O O   . LYS A 51  ? 0.37483 0.31166 0.36052 -0.02845 -0.03463 0.01732  58  LYS A O   
343  C CB  . LYS A 51  ? 0.32652 0.30852 0.33351 -0.03865 -0.02281 0.02165  58  LYS A CB  
344  C CG  . LYS A 51  ? 0.38445 0.37176 0.39585 -0.05274 -0.02919 0.03055  58  LYS A CG  
345  C CD  . LYS A 51  ? 0.32781 0.35829 0.35499 -0.05281 -0.01770 0.03970  58  LYS A CD  
346  C CE  . LYS A 51  ? 0.43227 0.47227 0.46841 -0.06540 -0.02457 0.04778  58  LYS A CE  
347  N NZ  . LYS A 51  ? 0.46817 0.55466 0.52169 -0.06176 -0.01222 0.05820  58  LYS A NZ  
348  N N   . ILE A 52  ? 0.29992 0.25708 0.30164 -0.01169 -0.02076 0.00084  59  ILE A N   
349  C CA  . ILE A 52  ? 0.31318 0.26837 0.31281 -0.00537 -0.02206 -0.00038 59  ILE A CA  
350  C C   . ILE A 52  ? 0.36932 0.30300 0.36656 0.00015  -0.03016 -0.00251 59  ILE A C   
351  O O   . ILE A 52  ? 0.33660 0.26252 0.32827 0.00098  -0.03598 0.00111  59  ILE A O   
352  C CB  . ILE A 52  ? 0.29800 0.26601 0.30440 0.00246  -0.01648 -0.00705 59  ILE A CB  
353  C CG1 . ILE A 52  ? 0.34426 0.30769 0.34361 0.00567  -0.02158 -0.00637 59  ILE A CG1 
354  C CG2 . ILE A 52  ? 0.30086 0.26939 0.32005 0.00871  -0.01481 -0.01392 59  ILE A CG2 
355  C CD1 . ILE A 52  ? 0.35115 0.31575 0.33323 0.00222  -0.02098 0.00131  59  ILE A CD1 
356  N N   . ARG A 53  ? 0.33992 0.26281 0.33838 0.00629  -0.03057 -0.00784 60  ARG A N   
357  C CA  . ARG A 53  ? 0.36444 0.26533 0.35601 0.01629  -0.03734 -0.00900 60  ARG A CA  
358  C C   . ARG A 53  ? 0.39216 0.26725 0.36537 0.00786  -0.04863 -0.00225 60  ARG A C   
359  O O   . ARG A 53  ? 0.40209 0.26520 0.37043 0.01314  -0.05501 0.00036  60  ARG A O   
360  C CB  . ARG A 53  ? 0.41413 0.30370 0.40173 0.02844  -0.03488 -0.01567 60  ARG A CB  
361  C CG  . ARG A 53  ? 0.47607 0.34565 0.45515 0.04550  -0.03981 -0.01630 60  ARG A CG  
362  C CD  . ARG A 53  ? 0.69413 0.55219 0.66410 0.06502  -0.03535 -0.02235 60  ARG A CD  
363  N NE  . ARG A 53  ? 0.72720 0.61936 0.72117 0.07766  -0.02298 -0.02205 60  ARG A NE  
364  C CZ  . ARG A 53  ? 0.62559 0.52492 0.61927 0.08548  -0.01388 -0.02593 60  ARG A CZ  
365  N NH1 . ARG A 53  ? 0.58652 0.46268 0.55834 0.07990  -0.01634 -0.03182 60  ARG A NH1 
366  N NH2 . ARG A 53  ? 0.51604 0.44735 0.53202 0.09826  -0.00326 -0.02185 60  ARG A NH2 
367  N N   . TYR A 54  ? 0.38099 0.24802 0.34489 -0.00667 -0.05288 0.00278  61  TYR A N   
368  C CA  . TYR A 54  ? 0.40173 0.24247 0.34822 -0.01847 -0.06638 0.01241  61  TYR A CA  
369  C C   . TYR A 54  ? 0.44970 0.30386 0.39867 -0.02412 -0.06599 0.02169  61  TYR A C   
370  O O   . TYR A 54  ? 0.44961 0.28036 0.38565 -0.02437 -0.07620 0.02653  61  TYR A O   
371  C CB  . TYR A 54  ? 0.42654 0.26338 0.36791 -0.03739 -0.07281 0.02047  61  TYR A CB  
372  C CG  . TYR A 54  ? 0.48374 0.29023 0.40687 -0.05316 -0.09029 0.03324  61  TYR A CG  
373  C CD1 . TYR A 54  ? 0.48838 0.24287 0.38469 -0.04783 -0.10626 0.02861  61  TYR A CD1 
374  C CD2 . TYR A 54  ? 0.50925 0.33772 0.43932 -0.07162 -0.09093 0.05111  61  TYR A CD2 
375  C CE1 . TYR A 54  ? 0.55490 0.27483 0.43114 -0.06358 -0.12543 0.04101  61  TYR A CE1 
376  C CE2 . TYR A 54  ? 0.53774 0.33924 0.45223 -0.08862 -0.10818 0.06598  61  TYR A CE2 
377  C CZ  . TYR A 54  ? 0.60546 0.35021 0.49283 -0.08596 -0.12684 0.06061  61  TYR A CZ  
378  O OH  . TYR A 54  ? 0.64733 0.35822 0.51572 -0.10433 -0.14727 0.07597  61  TYR A OH  
379  N N   . GLU A 55  ? 0.40260 0.29096 0.36367 -0.02699 -0.05482 0.02428  62  GLU A N   
380  C CA  . GLU A 55  ? 0.42640 0.32542 0.38325 -0.02910 -0.05353 0.03213  62  GLU A CA  
381  C C   . GLU A 55  ? 0.44412 0.33069 0.39885 -0.01659 -0.05827 0.02611  62  GLU A C   
382  O O   . GLU A 55  ? 0.51325 0.38856 0.45675 -0.01895 -0.06540 0.03338  62  GLU A O   
383  C CB  . GLU A 55  ? 0.41127 0.34330 0.37482 -0.02753 -0.04021 0.03248  62  GLU A CB  
384  C CG  . GLU A 55  ? 0.46270 0.41497 0.42906 -0.04053 -0.03588 0.04593  62  GLU A CG  
385  C CD  . GLU A 55  ? 0.56954 0.55448 0.53585 -0.03482 -0.02181 0.05022  62  GLU A CD  
386  O OE1 . GLU A 55  ? 0.50026 0.48501 0.46073 -0.02117 -0.01713 0.03945  62  GLU A OE1 
387  O OE2 . GLU A 55  ? 0.54991 0.56040 0.52138 -0.04329 -0.01630 0.06519  62  GLU A OE2 
388  N N   . SER A 56  ? 0.41928 0.30945 0.38615 -0.00385 -0.05535 0.01517  63  SER A N   
389  C CA  . SER A 56  ? 0.42989 0.31669 0.40137 0.00729  -0.06055 0.01284  63  SER A CA  
390  C C   . SER A 56  ? 0.50085 0.35992 0.46282 0.01344  -0.07102 0.01537  63  SER A C   
391  O O   . SER A 56  ? 0.45529 0.31186 0.41973 0.02159  -0.07730 0.01727  63  SER A O   
392  C CB  . SER A 56  ? 0.41455 0.31849 0.40589 0.01765  -0.05492 0.00517  63  SER A CB  
393  O OG  . SER A 56  ? 0.43923 0.33505 0.43396 0.02692  -0.05280 0.00099  63  SER A OG  
394  N N   . LEU A 57  ? 0.45198 0.28691 0.40062 0.01011  -0.07522 0.01595  64  LEU A N   
395  C CA  . LEU A 57  ? 0.49141 0.29100 0.42373 0.01905  -0.08698 0.01711  64  LEU A CA  
396  C C   . LEU A 57  ? 0.59251 0.37868 0.51239 0.01117  -0.09730 0.02745  64  LEU A C   
397  O O   . LEU A 57  ? 0.64065 0.40519 0.55205 0.02286  -0.10649 0.02859  64  LEU A O   
398  C CB  . LEU A 57  ? 0.52887 0.29501 0.44099 0.01509  -0.09374 0.01546  64  LEU A CB  
399  C CG  . LEU A 57  ? 0.52502 0.29502 0.44149 0.02708  -0.08543 0.00459  64  LEU A CG  
400  C CD1 . LEU A 57  ? 0.55761 0.28357 0.44502 0.02294  -0.09721 0.00290  64  LEU A CD1 
401  C CD2 . LEU A 57  ? 0.55626 0.33665 0.48392 0.05317  -0.07877 -0.00145 64  LEU A CD2 
402  N N   . THR A 58  ? 0.54522 0.34426 0.46233 -0.00677 -0.09554 0.03636  65  THR A N   
403  C CA  . THR A 58  ? 0.55737 0.34611 0.46073 -0.01454 -0.10398 0.04805  65  THR A CA  
404  C C   . THR A 58  ? 0.63749 0.45291 0.54635 -0.01285 -0.09789 0.04921  65  THR A C   
405  O O   . THR A 58  ? 0.65781 0.46393 0.55388 -0.01485 -0.10532 0.05730  65  THR A O   
406  C CB  . THR A 58  ? 0.68551 0.46630 0.57621 -0.03642 -0.10847 0.06242  65  THR A CB  
407  O OG1 . THR A 58  ? 0.64296 0.45941 0.54632 -0.04519 -0.09494 0.06452  65  THR A OG1 
408  C CG2 . THR A 58  ? 0.66873 0.40911 0.54522 -0.04012 -0.12184 0.06204  65  THR A CG2 
409  N N   . ASP A 59  ? 0.64356 0.52100 0.47651 0.12445  -0.03182 0.10562  66  ASP A N   
410  C CA  . ASP A 59  ? 0.59496 0.48216 0.40897 0.12368  -0.04967 0.10343  66  ASP A CA  
411  C C   . ASP A 59  ? 0.55967 0.47774 0.40337 0.11857  -0.06540 0.09424  66  ASP A C   
412  O O   . ASP A 59  ? 0.52943 0.45526 0.38259 0.10644  -0.06260 0.08148  66  ASP A O   
413  C CB  . ASP A 59  ? 0.60946 0.48186 0.39598 0.11395  -0.04021 0.09620  66  ASP A CB  
414  C CG  . ASP A 59  ? 0.72098 0.59684 0.48037 0.11387  -0.05701 0.09350  66  ASP A CG  
415  O OD1 . ASP A 59  ? 0.72124 0.61273 0.48466 0.11988  -0.07807 0.09678  66  ASP A OD1 
416  O OD2 . ASP A 59  ? 0.75869 0.62149 0.49287 0.10776  -0.04906 0.08791  66  ASP A OD2 
417  N N   . PRO A 60  ? 0.62451 0.56130 0.48536 0.12775  -0.08187 0.10117  67  PRO A N   
418  C CA  . PRO A 60  ? 0.51669 0.48394 0.41157 0.12192  -0.09449 0.09318  67  PRO A CA  
419  C C   . PRO A 60  ? 0.53540 0.51046 0.41805 0.11067  -0.10762 0.08187  67  PRO A C   
420  O O   . PRO A 60  ? 0.52487 0.51815 0.43241 0.10124  -0.11142 0.07204  67  PRO A O   
421  C CB  . PRO A 60  ? 0.54104 0.52631 0.45361 0.13541  -0.11045 0.10529  67  PRO A CB  
422  C CG  . PRO A 60  ? 0.66449 0.62787 0.56231 0.14911  -0.10002 0.11908  67  PRO A CG  
423  C CD  . PRO A 60  ? 0.61488 0.54586 0.47560 0.14403  -0.08343 0.11715  67  PRO A CD  
424  N N   . SER A 61  ? 0.59377 0.55322 0.43663 0.11172  -0.11396 0.08312  68  SER A N   
425  C CA  . SER A 61  ? 0.57229 0.53474 0.39918 0.10162  -0.12577 0.07155  68  SER A CA  
426  C C   . SER A 61  ? 0.55120 0.50839 0.38268 0.08919  -0.11052 0.05839  68  SER A C   
427  O O   . SER A 61  ? 0.55122 0.51244 0.37766 0.08017  -0.11855 0.04741  68  SER A O   
428  C CB  . SER A 61  ? 0.60001 0.54169 0.37733 0.10626  -0.13241 0.07552  68  SER A CB  
429  O OG  . SER A 61  ? 0.67037 0.58486 0.42138 0.10649  -0.11013 0.07689  68  SER A OG  
430  N N   . LYS A 62  ? 0.49467 0.44276 0.33620 0.08844  -0.08948 0.05912  69  LYS A N   
431  C CA  . LYS A 62  ? 0.46529 0.41235 0.31549 0.07734  -0.07729 0.04750  69  LYS A CA  
432  C C   . LYS A 62  ? 0.43875 0.40854 0.32171 0.07007  -0.08563 0.03946  69  LYS A C   
433  O O   . LYS A 62  ? 0.43592 0.40609 0.32368 0.06099  -0.08012 0.02947  69  LYS A O   
434  C CB  . LYS A 62  ? 0.51104 0.44636 0.36829 0.07720  -0.05587 0.05001  69  LYS A CB  
435  C CG  . LYS A 62  ? 0.61231 0.52330 0.43814 0.08193  -0.04437 0.05736  69  LYS A CG  
436  C CD  . LYS A 62  ? 0.58951 0.48981 0.40722 0.07346  -0.02816 0.05013  69  LYS A CD  
437  C CE  . LYS A 62  ? 0.66808 0.54452 0.45548 0.07717  -0.01475 0.05782  69  LYS A CE  
438  N NZ  . LYS A 62  ? 0.73419 0.60544 0.52103 0.06849  0.00123  0.05051  69  LYS A NZ  
439  N N   . LEU A 63  ? 0.44403 0.43290 0.35078 0.07431  -0.09792 0.04443  70  LEU A N   
440  C CA  . LEU A 63  ? 0.46794 0.47874 0.40688 0.06714  -0.10491 0.03806  70  LEU A CA  
441  C C   . LEU A 63  ? 0.45831 0.48140 0.39467 0.06280  -0.12688 0.03408  70  LEU A C   
442  O O   . LEU A 63  ? 0.45236 0.49524 0.41763 0.05652  -0.13451 0.03011  70  LEU A O   
443  C CB  . LEU A 63  ? 0.43662 0.46276 0.40974 0.07344  -0.10136 0.04538  70  LEU A CB  
444  C CG  . LEU A 63  ? 0.43221 0.44606 0.41076 0.07563  -0.08007 0.04696  70  LEU A CG  
445  C CD1 . LEU A 63  ? 0.42856 0.45566 0.43837 0.08304  -0.07634 0.05362  70  LEU A CD1 
446  C CD2 . LEU A 63  ? 0.41142 0.42063 0.39138 0.06421  -0.06953 0.03594  70  LEU A CD2 
447  N N   . ASP A 64  ? 0.43585 0.44622 0.33689 0.06507  -0.13673 0.03459  71  ASP A N   
448  C CA  . ASP A 64  ? 0.48759 0.50696 0.38226 0.05929  -0.15906 0.02895  71  ASP A CA  
449  C C   . ASP A 64  ? 0.49053 0.50959 0.39117 0.04569  -0.15762 0.01492  71  ASP A C   
450  O O   . ASP A 64  ? 0.53211 0.56454 0.44474 0.03776  -0.17425 0.00916  71  ASP A O   
451  C CB  . ASP A 64  ? 0.54111 0.54131 0.38853 0.06407  -0.16815 0.03086  71  ASP A CB  
452  C CG  . ASP A 64  ? 0.63800 0.64020 0.47882 0.07801  -0.17529 0.04603  71  ASP A CG  
453  O OD1 . ASP A 64  ? 0.68727 0.66987 0.48572 0.08375  -0.17878 0.04992  71  ASP A OD1 
454  O OD2 . ASP A 64  ? 0.70790 0.73001 0.58434 0.08402  -0.17694 0.05452  71  ASP A OD2 
455  N N   . SER A 65  ? 0.45973 0.46382 0.35357 0.04279  -0.13826 0.00977  72  SER A N   
456  C CA  . SER A 65  ? 0.41756 0.41924 0.31800 0.03205  -0.13366 -0.00186 72  SER A CA  
457  C C   . SER A 65  ? 0.47061 0.49129 0.41284 0.02727  -0.12965 -0.00210 72  SER A C   
458  O O   . SER A 65  ? 0.48802 0.50538 0.43709 0.01968  -0.12274 -0.00980 72  SER A O   
459  C CB  . SER A 65  ? 0.49072 0.47072 0.36847 0.03275  -0.11481 -0.00550 72  SER A CB  
460  O OG  . SER A 65  ? 0.44319 0.42238 0.32993 0.03898  -0.09948 0.00247  72  SER A OG  
461  N N   . GLY A 66  ? 0.41838 0.45771 0.38775 0.03244  -0.13268 0.00671  73  GLY A N   
462  C CA  . GLY A 66  ? 0.42427 0.48049 0.43129 0.02862  -0.12687 0.00699  73  GLY A CA  
463  C C   . GLY A 66  ? 0.43385 0.49635 0.45814 0.03833  -0.11598 0.01682  73  GLY A C   
464  O O   . GLY A 66  ? 0.37784 0.42483 0.38844 0.04270  -0.10131 0.01850  73  GLY A O   
465  N N   . LYS A 67  ? 0.36782 0.45253 0.42277 0.04177  -0.12256 0.02331  74  LYS A N   
466  C CA  . LYS A 67  ? 0.35363 0.44234 0.42408 0.05267  -0.11168 0.03275  74  LYS A CA  
467  C C   . LYS A 67  ? 0.36688 0.45672 0.45706 0.04985  -0.09422 0.03053  74  LYS A C   
468  O O   . LYS A 67  ? 0.37444 0.45693 0.46623 0.05758  -0.08055 0.03531  74  LYS A O   
469  C CB  . LYS A 67  ? 0.35757 0.47078 0.45420 0.05989  -0.12534 0.04186  74  LYS A CB  
470  C CG  . LYS A 67  ? 0.49533 0.60255 0.57047 0.07102  -0.13580 0.05031  74  LYS A CG  
471  C CD  . LYS A 67  ? 0.57298 0.70804 0.67197 0.07456  -0.15718 0.05684  74  LYS A CD  
472  C CE  . LYS A 67  ? 0.62463 0.75225 0.69328 0.08236  -0.17374 0.06290  74  LYS A CE  
473  N NZ  . LYS A 67  ? 0.70770 0.84186 0.78671 0.09997  -0.17447 0.07817  74  LYS A NZ  
474  N N   . GLU A 68  ? 0.31222 0.40890 0.41531 0.03905  -0.09415 0.02352  75  GLU A N   
475  C CA  . GLU A 68  ? 0.32478 0.42327 0.44542 0.03675  -0.07868 0.02241  75  GLU A CA  
476  C C   . GLU A 68  ? 0.31604 0.39209 0.41312 0.03442  -0.06530 0.01706  75  GLU A C   
477  O O   . GLU A 68  ? 0.36656 0.43133 0.44346 0.02862  -0.06851 0.01080  75  GLU A O   
478  C CB  . GLU A 68  ? 0.33521 0.44824 0.47804 0.02601  -0.08308 0.01826  75  GLU A CB  
479  C CG  . GLU A 68  ? 0.38254 0.52328 0.55962 0.02672  -0.09382 0.02398  75  GLU A CG  
480  C CD  . GLU A 68  ? 0.60978 0.75835 0.78110 0.02503  -0.11606 0.02367  75  GLU A CD  
481  O OE1 . GLU A 68  ? 0.59396 0.72807 0.73977 0.01735  -0.12341 0.01560  75  GLU A OE1 
482  O OE2 . GLU A 68  ? 0.55856 0.72748 0.75036 0.03177  -0.12640 0.03147  75  GLU A OE2 
483  N N   . LEU A 69  ? 0.25564 0.32551 0.35601 0.03886  -0.05044 0.01924  76  LEU A N   
484  C CA  . LEU A 69  ? 0.27339 0.32424 0.35452 0.03628  -0.03871 0.01451  76  LEU A CA  
485  C C   . LEU A 69  ? 0.23261 0.28557 0.32493 0.03111  -0.02948 0.01133  76  LEU A C   
486  O O   . LEU A 69  ? 0.25912 0.31549 0.36452 0.03555  -0.02034 0.01474  76  LEU A O   
487  C CB  . LEU A 69  ? 0.27771 0.31559 0.34884 0.04466  -0.02971 0.01893  76  LEU A CB  
488  C CG  . LEU A 69  ? 0.34236 0.37478 0.39899 0.05107  -0.03695 0.02399  76  LEU A CG  
489  C CD1 . LEU A 69  ? 0.41358 0.42819 0.45864 0.05767  -0.02521 0.02790  76  LEU A CD1 
490  C CD2 . LEU A 69  ? 0.34546 0.37105 0.38126 0.04507  -0.04396 0.01894  76  LEU A CD2 
491  N N   . HIS A 70  ? 0.25215 0.30173 0.33812 0.02264  -0.03104 0.00530  77  HIS A N   
492  C CA  . HIS A 70  ? 0.23372 0.28538 0.32912 0.01784  -0.02377 0.00361  77  HIS A CA  
493  C C   . HIS A 70  ? 0.26631 0.30722 0.34655 0.01136  -0.02338 -0.00224 77  HIS A C   
494  O O   . HIS A 70  ? 0.24169 0.27583 0.30764 0.01029  -0.02860 -0.00536 77  HIS A O   
495  C CB  . HIS A 70  ? 0.25552 0.32463 0.37534 0.01444  -0.02897 0.00591  77  HIS A CB  
496  C CG  . HIS A 70  ? 0.27882 0.35120 0.39720 0.00788  -0.04272 0.00236  77  HIS A CG  
497  N ND1 . HIS A 70  ? 0.33191 0.41840 0.46322 0.00790  -0.05536 0.00452  77  HIS A ND1 
498  C CD2 . HIS A 70  ? 0.30162 0.36385 0.40659 0.00120  -0.04587 -0.00354 77  HIS A CD2 
499  C CE1 . HIS A 70  ? 0.30874 0.39153 0.43175 0.00055  -0.06583 -0.00100 77  HIS A CE1 
500  N NE2 . HIS A 70  ? 0.30455 0.37192 0.41178 -0.00306 -0.05930 -0.00584 77  HIS A NE2 
501  N N   . ILE A 71  ? 0.22026 0.25969 0.30388 0.00789  -0.01641 -0.00294 78  ILE A N   
502  C CA  . ILE A 71  ? 0.22969 0.25993 0.30135 0.00304  -0.01557 -0.00686 78  ILE A CA  
503  C C   . ILE A 71  ? 0.24780 0.28240 0.33106 -0.00217 -0.01482 -0.00578 78  ILE A C   
504  O O   . ILE A 71  ? 0.23280 0.27297 0.32805 -0.00165 -0.00755 -0.00214 78  ILE A O   
505  C CB  . ILE A 71  ? 0.23541 0.25546 0.29402 0.00437  -0.00710 -0.00801 78  ILE A CB  
506  C CG1 . ILE A 71  ? 0.23467 0.24919 0.28401 0.00814  -0.00630 -0.00879 78  ILE A CG1 
507  C CG2 . ILE A 71  ? 0.24324 0.25666 0.29189 0.00029  -0.00822 -0.01072 78  ILE A CG2 
508  C CD1 . ILE A 71  ? 0.27027 0.27422 0.30797 0.00810  0.00145  -0.01076 78  ILE A CD1 
509  N N   . ASN A 72  ? 0.23285 0.26343 0.31250 -0.00698 -0.02083 -0.00868 79  ASN A N   
510  C CA  . ASN A 72  ? 0.19860 0.22931 0.28741 -0.01290 -0.01945 -0.00753 79  ASN A CA  
511  C C   . ASN A 72  ? 0.24508 0.26237 0.31865 -0.01381 -0.01663 -0.00883 79  ASN A C   
512  O O   . ASN A 72  ? 0.26570 0.27626 0.32655 -0.01191 -0.02052 -0.01224 79  ASN A O   
513  C CB  . ASN A 72  ? 0.24273 0.27811 0.34174 -0.01856 -0.02954 -0.00974 79  ASN A CB  
514  C CG  . ASN A 72  ? 0.27280 0.32472 0.39010 -0.01794 -0.03478 -0.00742 79  ASN A CG  
515  O OD1 . ASN A 72  ? 0.25780 0.31941 0.38771 -0.01414 -0.02794 -0.00262 79  ASN A OD1 
516  N ND2 . ASN A 72  ? 0.28721 0.34215 0.40581 -0.02129 -0.04721 -0.01075 79  ASN A ND2 
517  N N   . LEU A 73  ? 0.24116 0.25487 0.31662 -0.01621 -0.00954 -0.00533 80  LEU A N   
518  C CA  . LEU A 73  ? 0.21708 0.21798 0.27843 -0.01635 -0.00765 -0.00478 80  LEU A CA  
519  C C   . LEU A 73  ? 0.26852 0.26451 0.33786 -0.02245 -0.00789 -0.00325 80  LEU A C   
520  O O   . LEU A 73  ? 0.25257 0.25327 0.33528 -0.02655 -0.00213 0.00062  80  LEU A O   
521  C CB  . LEU A 73  ? 0.24125 0.23773 0.29214 -0.01383 0.00112  -0.00127 80  LEU A CB  
522  C CG  . LEU A 73  ? 0.22799 0.22720 0.27180 -0.00941 0.00268  -0.00336 80  LEU A CG  
523  C CD1 . LEU A 73  ? 0.26838 0.25988 0.29790 -0.00795 0.01100  -0.00115 80  LEU A CD1 
524  C CD2 . LEU A 73  ? 0.26427 0.26201 0.29930 -0.00724 -0.00480 -0.00770 80  LEU A CD2 
525  N N   . ILE A 74  ? 0.25382 0.23974 0.31611 -0.02314 -0.01335 -0.00619 81  ILE A N   
526  C CA  . ILE A 74  ? 0.26424 0.24187 0.33303 -0.02977 -0.01455 -0.00631 81  ILE A CA  
527  C C   . ILE A 74  ? 0.29133 0.25171 0.34635 -0.02734 -0.01163 -0.00373 81  ILE A C   
528  O O   . ILE A 74  ? 0.30729 0.25931 0.35259 -0.02336 -0.01595 -0.00716 81  ILE A O   
529  C CB  . ILE A 74  ? 0.25184 0.22981 0.32400 -0.03303 -0.02428 -0.01322 81  ILE A CB  
530  C CG1 . ILE A 74  ? 0.28057 0.27608 0.36312 -0.03277 -0.02882 -0.01455 81  ILE A CG1 
531  C CG2 . ILE A 74  ? 0.27817 0.24664 0.35831 -0.04215 -0.02567 -0.01431 81  ILE A CG2 
532  C CD1 . ILE A 74  ? 0.28880 0.28472 0.36946 -0.03500 -0.03998 -0.02122 81  ILE A CD1 
533  N N   . PRO A 75  ? 0.31821 0.27217 0.37228 -0.02911 -0.00367 0.00298  82  PRO A N   
534  C CA  . PRO A 75  ? 0.29671 0.23241 0.33765 -0.02646 -0.00133 0.00706  82  PRO A CA  
535  C C   . PRO A 75  ? 0.36204 0.28395 0.40938 -0.03329 -0.00182 0.00582  82  PRO A C   
536  O O   . PRO A 75  ? 0.35130 0.27780 0.41482 -0.04261 -0.00067 0.00501  82  PRO A O   
537  C CB  . PRO A 75  ? 0.35225 0.28561 0.38683 -0.02594 0.00823  0.01533  82  PRO A CB  
538  C CG  . PRO A 75  ? 0.36182 0.30885 0.41478 -0.03249 0.01356  0.01563  82  PRO A CG  
539  C CD  . PRO A 75  ? 0.30762 0.26999 0.37242 -0.03289 0.00482  0.00798  82  PRO A CD  
540  N N   . ASN A 76  ? 0.35038 0.25526 0.38622 -0.02870 -0.00366 0.00546  83  ASN A N   
541  C CA  . ASN A 76  ? 0.37230 0.25768 0.41027 -0.03472 -0.00286 0.00414  83  ASN A CA  
542  C C   . ASN A 76  ? 0.40146 0.26613 0.42507 -0.02785 0.00208  0.01174  83  ASN A C   
543  O O   . ASN A 76  ? 0.41906 0.27832 0.43243 -0.01785 -0.00119 0.01089  83  ASN A O   
544  C CB  . ASN A 76  ? 0.36534 0.24680 0.40273 -0.03540 -0.01070 -0.00625 83  ASN A CB  
545  C CG  . ASN A 76  ? 0.46289 0.32282 0.50233 -0.04420 -0.01037 -0.00968 83  ASN A CG  
546  O OD1 . ASN A 76  ? 0.50119 0.33970 0.53361 -0.04263 -0.00453 -0.00461 83  ASN A OD1 
547  N ND2 . ASN A 76  ? 0.55822 0.42249 0.60632 -0.05371 -0.01723 -0.01824 83  ASN A ND2 
548  N N   . LYS A 77  ? 0.43897 0.29215 0.46276 -0.03277 0.01040  0.01990  84  LYS A N   
549  C CA  . LYS A 77  ? 0.45194 0.28441 0.45962 -0.02515 0.01514  0.02924  84  LYS A CA  
550  C C   . LYS A 77  ? 0.52053 0.32824 0.52431 -0.02362 0.01438  0.02680  84  LYS A C   
551  O O   . LYS A 77  ? 0.52668 0.31999 0.51721 -0.01263 0.01508  0.03286  84  LYS A O   
552  C CB  . LYS A 77  ? 0.49499 0.31899 0.50069 -0.03058 0.02617  0.03980  84  LYS A CB  
553  C CG  . LYS A 77  ? 0.48160 0.32345 0.48353 -0.02881 0.02971  0.04404  84  LYS A CG  
554  C CD  . LYS A 77  ? 0.56408 0.39269 0.55845 -0.03226 0.04305  0.05579  84  LYS A CD  
555  C CE  . LYS A 77  ? 0.56844 0.41033 0.55352 -0.02930 0.04813  0.05957  84  LYS A CE  
556  N NZ  . LYS A 77  ? 0.60974 0.47647 0.61570 -0.03490 0.04687  0.05141  84  LYS A NZ  
557  N N   . GLN A 78  ? 0.51345 0.31469 0.52791 -0.03422 0.01278  0.01818  85  GLN A N   
558  C CA  . GLN A 78  ? 0.60650 0.37983 0.61430 -0.03305 0.01300  0.01433  85  GLN A CA  
559  C C   . GLN A 78  ? 0.57213 0.34705 0.57116 -0.01983 0.00729  0.00857  85  GLN A C   
560  O O   . GLN A 78  ? 0.60442 0.35822 0.59328 -0.00997 0.00996  0.01127  85  GLN A O   
561  C CB  . GLN A 78  ? 0.60004 0.36559 0.61953 -0.04925 0.01122  0.00494  85  GLN A CB  
562  C CG  . GLN A 78  ? 0.71417 0.47648 0.74750 -0.06420 0.01834  0.01075  85  GLN A CG  
563  C CD  . GLN A 78  ? 0.92917 0.66263 0.95271 -0.06244 0.02987  0.02286  85  GLN A CD  
564  O OE1 . GLN A 78  ? 0.98777 0.71107 0.99426 -0.04772 0.03245  0.03081  85  GLN A OE1 
565  N NE2 . GLN A 78  ? 0.98501 0.70501 1.02026 -0.07793 0.03648  0.02469  85  GLN A NE2 
566  N N   . ASP A 79  ? 0.47274 0.27221 0.47644 -0.01887 0.00059  0.00148  86  ASP A N   
567  C CA  . ASP A 79  ? 0.48814 0.29298 0.48608 -0.00761 -0.00339 -0.00398 86  ASP A CA  
568  C C   . ASP A 79  ? 0.45577 0.27616 0.45100 0.00493  -0.00408 0.00399  86  ASP A C   
569  O O   . ASP A 79  ? 0.47878 0.30429 0.47214 0.01537  -0.00604 0.00164  86  ASP A O   
570  C CB  . ASP A 79  ? 0.49054 0.31344 0.49369 -0.01343 -0.00984 -0.01453 86  ASP A CB  
571  C CG  . ASP A 79  ? 0.64022 0.44799 0.64349 -0.02503 -0.01246 -0.02444 86  ASP A CG  
572  O OD1 . ASP A 79  ? 0.69211 0.47416 0.69246 -0.02966 -0.00855 -0.02411 86  ASP A OD1 
573  O OD2 . ASP A 79  ? 0.64135 0.46263 0.64733 -0.03035 -0.01903 -0.03227 86  ASP A OD2 
574  N N   . ARG A 80  ? 0.43274 0.26080 0.42769 0.00355  -0.00237 0.01300  87  ARG A N   
575  C CA  . ARG A 80  ? 0.38121 0.22595 0.37212 0.01260  -0.00519 0.01937  87  ARG A CA  
576  C C   . ARG A 80  ? 0.37298 0.24176 0.36986 0.01416  -0.01076 0.01206  87  ARG A C   
577  O O   . ARG A 80  ? 0.38576 0.26427 0.38241 0.02369  -0.01424 0.01290  87  ARG A O   
578  C CB  . ARG A 80  ? 0.45360 0.28624 0.43655 0.02595  -0.00526 0.02737  87  ARG A CB  
579  C CG  . ARG A 80  ? 0.46505 0.30617 0.43941 0.03075  -0.00746 0.03758  87  ARG A CG  
580  C CD  . ARG A 80  ? 0.55282 0.38056 0.51800 0.04334  -0.00838 0.04834  87  ARG A CD  
581  N NE  . ARG A 80  ? 0.59757 0.43746 0.56984 0.05535  -0.01452 0.04702  87  ARG A NE  
582  C CZ  . ARG A 80  ? 0.64281 0.46948 0.61551 0.06762  -0.01386 0.05202  87  ARG A CZ  
583  N NH1 . ARG A 80  ? 0.68607 0.48385 0.64958 0.06980  -0.00777 0.05911  87  ARG A NH1 
584  N NH2 . ARG A 80  ? 0.60099 0.44377 0.58464 0.07839  -0.01864 0.05073  87  ARG A NH2 
585  N N   . THR A 81  ? 0.35881 0.23812 0.36258 0.00462  -0.01155 0.00562  88  THR A N   
586  C CA  . THR A 81  ? 0.33243 0.23186 0.34057 0.00528  -0.01575 -0.00052 88  THR A CA  
587  C C   . THR A 81  ? 0.34304 0.25782 0.35547 -0.00124 -0.01549 0.00025  88  THR A C   
588  O O   . THR A 81  ? 0.34318 0.25487 0.35996 -0.00893 -0.01209 0.00217  88  THR A O   
589  C CB  . THR A 81  ? 0.37774 0.27422 0.38803 0.00262  -0.01774 -0.01030 88  THR A CB  
590  O OG1 . THR A 81  ? 0.39648 0.28652 0.41121 -0.00844 -0.01783 -0.01330 88  THR A OG1 
591  C CG2 . THR A 81  ? 0.38497 0.26543 0.38957 0.01069  -0.01610 -0.01246 88  THR A CG2 
592  N N   . LEU A 82  ? 0.27884 0.20967 0.29122 0.00198  -0.01812 -0.00108 89  LEU A N   
593  C CA  . LEU A 82  ? 0.28983 0.23417 0.30610 -0.00277 -0.01742 -0.00211 89  LEU A CA  
594  C C   . LEU A 82  ? 0.31559 0.27000 0.33630 -0.00259 -0.02091 -0.00905 89  LEU A C   
595  O O   . LEU A 82  ? 0.31295 0.27137 0.33138 0.00283  -0.02291 -0.01088 89  LEU A O   
596  C CB  . LEU A 82  ? 0.31571 0.26601 0.32416 0.00024  -0.01675 0.00234  89  LEU A CB  
597  C CG  . LEU A 82  ? 0.29117 0.25218 0.30170 -0.00342 -0.01428 0.00081  89  LEU A CG  
598  C CD1 . LEU A 82  ? 0.31221 0.27144 0.33022 -0.00958 -0.00825 0.00291  89  LEU A CD1 
599  C CD2 . LEU A 82  ? 0.30656 0.26884 0.30453 -0.00081 -0.01409 0.00374  89  LEU A CD2 
600  N N   . THR A 83  ? 0.28289 0.24204 0.31057 -0.00825 -0.02155 -0.01212 90  THR A N   
601  C CA  . THR A 83  ? 0.26120 0.22746 0.28991 -0.00773 -0.02516 -0.01770 90  THR A CA  
602  C C   . THR A 83  ? 0.30131 0.28052 0.33463 -0.00881 -0.02426 -0.01666 90  THR A C   
603  O O   . THR A 83  ? 0.29776 0.28069 0.33847 -0.01257 -0.02169 -0.01373 90  THR A O   
604  C CB  . THR A 83  ? 0.27810 0.23799 0.30886 -0.01254 -0.02903 -0.02254 90  THR A CB  
605  O OG1 . THR A 83  ? 0.33790 0.28156 0.36230 -0.01108 -0.02852 -0.02431 90  THR A OG1 
606  C CG2 . THR A 83  ? 0.33998 0.30588 0.36744 -0.01133 -0.03312 -0.02736 90  THR A CG2 
607  N N   . ILE A 84  ? 0.28277 0.26792 0.31243 -0.00520 -0.02489 -0.01855 91  ILE A N   
608  C CA  . ILE A 84  ? 0.24969 0.24368 0.28198 -0.00520 -0.02343 -0.01789 91  ILE A CA  
609  C C   . ILE A 84  ? 0.30944 0.30590 0.34152 -0.00470 -0.02725 -0.02105 91  ILE A C   
610  O O   . ILE A 84  ? 0.27385 0.26739 0.29877 -0.00193 -0.02794 -0.02370 91  ILE A O   
611  C CB  . ILE A 84  ? 0.27941 0.27555 0.30604 -0.00259 -0.02089 -0.01727 91  ILE A CB  
612  C CG1 . ILE A 84  ? 0.33224 0.32495 0.35432 -0.00276 -0.01887 -0.01406 91  ILE A CG1 
613  C CG2 . ILE A 84  ? 0.28903 0.28994 0.31675 -0.00240 -0.01843 -0.01728 91  ILE A CG2 
614  C CD1 . ILE A 84  ? 0.41459 0.40298 0.43324 -0.00014 -0.02157 -0.01308 91  ILE A CD1 
615  N N   . VAL A 85  ? 0.24107 0.24319 0.28099 -0.00698 -0.02968 -0.02027 92  VAL A N   
616  C CA  . VAL A 85  ? 0.25550 0.26008 0.29344 -0.00627 -0.03535 -0.02229 92  VAL A CA  
617  C C   . VAL A 85  ? 0.28279 0.29480 0.32389 -0.00292 -0.03333 -0.01905 92  VAL A C   
618  O O   . VAL A 85  ? 0.29589 0.31419 0.34776 -0.00311 -0.02980 -0.01558 92  VAL A O   
619  C CB  . VAL A 85  ? 0.27552 0.28228 0.32158 -0.01150 -0.04256 -0.02368 92  VAL A CB  
620  C CG1 . VAL A 85  ? 0.33636 0.34397 0.37510 -0.01045 -0.05073 -0.02623 92  VAL A CG1 
621  C CG2 . VAL A 85  ? 0.33665 0.33244 0.38023 -0.01563 -0.04299 -0.02665 92  VAL A CG2 
622  N N   . ASP A 86  ? 0.28248 0.29229 0.31371 0.00063  -0.03449 -0.01975 93  ASP A N   
623  C CA  . ASP A 86  ? 0.26218 0.27634 0.29535 0.00453  -0.03325 -0.01598 93  ASP A CA  
624  C C   . ASP A 86  ? 0.30549 0.31875 0.33000 0.00692  -0.04035 -0.01598 93  ASP A C   
625  O O   . ASP A 86  ? 0.28535 0.29174 0.29751 0.00592  -0.04378 -0.01991 93  ASP A O   
626  C CB  . ASP A 86  ? 0.27727 0.28646 0.30444 0.00671  -0.02496 -0.01523 93  ASP A CB  
627  C CG  . ASP A 86  ? 0.32207 0.32442 0.33647 0.00761  -0.02343 -0.01742 93  ASP A CG  
628  O OD1 . ASP A 86  ? 0.33926 0.33851 0.34457 0.01019  -0.02579 -0.01682 93  ASP A OD1 
629  O OD2 . ASP A 86  ? 0.32901 0.32959 0.34259 0.00589  -0.01976 -0.01941 93  ASP A OD2 
630  N N   . THR A 87  ? 0.28100 0.30032 0.31084 0.01085  -0.04254 -0.01127 94  THR A N   
631  C CA  . THR A 87  ? 0.25509 0.27319 0.27414 0.01440  -0.05017 -0.00965 94  THR A CA  
632  C C   . THR A 87  ? 0.29821 0.30780 0.30480 0.02022  -0.04323 -0.00587 94  THR A C   
633  O O   . THR A 87  ? 0.28851 0.29859 0.29152 0.02589  -0.04657 -0.00053 94  THR A O   
634  C CB  . THR A 87  ? 0.27457 0.30669 0.30949 0.01538  -0.05972 -0.00584 94  THR A CB  
635  O OG1 . THR A 87  ? 0.28612 0.32590 0.33886 0.01868  -0.05235 -0.00086 94  THR A OG1 
636  C CG2 . THR A 87  ? 0.28341 0.32183 0.32889 0.00738  -0.06745 -0.01041 94  THR A CG2 
637  N N   . GLY A 88  ? 0.27925 0.28069 0.27945 0.01872  -0.03379 -0.00815 95  GLY A N   
638  C CA  . GLY A 88  ? 0.32385 0.31603 0.31373 0.02201  -0.02591 -0.00510 95  GLY A CA  
639  C C   . GLY A 88  ? 0.29755 0.28077 0.26727 0.02413  -0.02673 -0.00486 95  GLY A C   
640  O O   . GLY A 88  ? 0.31592 0.29934 0.27669 0.02460  -0.03550 -0.00648 95  GLY A O   
641  N N   . ILE A 89  ? 0.28783 0.26181 0.24917 0.02475  -0.01677 -0.00314 96  ILE A N   
642  C CA  . ILE A 89  ? 0.32581 0.28919 0.26597 0.02785  -0.01448 -0.00101 96  ILE A CA  
643  C C   . ILE A 89  ? 0.33982 0.30108 0.27068 0.02565  -0.01449 -0.00708 96  ILE A C   
644  O O   . ILE A 89  ? 0.36877 0.32067 0.27833 0.02864  -0.01458 -0.00663 96  ILE A O   
645  C CB  . ILE A 89  ? 0.33503 0.28864 0.27131 0.02815  -0.00191 0.00328  96  ILE A CB  
646  C CG1 . ILE A 89  ? 0.39662 0.33710 0.30847 0.03296  0.00133  0.00836  96  ILE A CG1 
647  C CG2 . ILE A 89  ? 0.32151 0.27827 0.26888 0.02166  0.00645  -0.00160 96  ILE A CG2 
648  C CD1 . ILE A 89  ? 0.44377 0.37195 0.35077 0.03424  0.01279  0.01524  96  ILE A CD1 
649  N N   . GLY A 90  ? 0.31442 0.28240 0.25871 0.02135  -0.01407 -0.01251 97  GLY A N   
650  C CA  . GLY A 90  ? 0.34099 0.30539 0.27772 0.02069  -0.01272 -0.01800 97  GLY A CA  
651  C C   . GLY A 90  ? 0.36440 0.32383 0.29622 0.02153  0.00032  -0.01734 97  GLY A C   
652  O O   . GLY A 90  ? 0.36641 0.32576 0.30281 0.02073  0.00793  -0.01313 97  GLY A O   
653  N N   . MET A 91  ? 0.34591 0.30126 0.27068 0.02277  0.00372  -0.02184 98  MET A N   
654  C CA  . MET A 91  ? 0.34325 0.29631 0.26684 0.02419  0.01750  -0.02121 98  MET A CA  
655  C C   . MET A 91  ? 0.36477 0.30394 0.26290 0.02888  0.02188  -0.02387 98  MET A C   
656  O O   . MET A 91  ? 0.38527 0.31848 0.27318 0.02984  0.01450  -0.02943 98  MET A O   
657  C CB  . MET A 91  ? 0.33546 0.29994 0.28196 0.02234  0.02120  -0.02378 98  MET A CB  
658  C CG  . MET A 91  ? 0.34900 0.32557 0.31745 0.01725  0.01962  -0.02141 98  MET A CG  
659  S SD  . MET A 91  ? 0.35081 0.34119 0.34291 0.01572  0.01818  -0.02406 98  MET A SD  
660  C CE  . MET A 91  ? 0.34943 0.33604 0.33729 0.01687  0.00667  -0.02765 98  MET A CE  
661  N N   . THR A 92  ? 0.37618 0.30852 0.26321 0.03134  0.03511  -0.02026 99  THR A N   
662  C CA  . THR A 92  ? 0.41729 0.33524 0.27929 0.03645  0.04360  -0.02298 99  THR A CA  
663  C C   . THR A 92  ? 0.41860 0.34187 0.29553 0.03831  0.05296  -0.02734 99  THR A C   
664  O O   . THR A 92  ? 0.40112 0.34064 0.30815 0.03554  0.05320  -0.02678 99  THR A O   
665  C CB  . THR A 92  ? 0.45977 0.36815 0.30520 0.03873  0.05728  -0.01640 99  THR A CB  
666  O OG1 . THR A 92  ? 0.47072 0.39186 0.34378 0.03553  0.06996  -0.01284 99  THR A OG1 
667  C CG2 . THR A 92  ? 0.47668 0.37954 0.30920 0.03837  0.04884  -0.01002 99  THR A CG2 
668  N N   . LYS A 93  ? 0.30455 0.30586 0.29917 0.08431  -0.01948 -0.01228 100 LYS A N   
669  C CA  . LYS A 93  ? 0.32041 0.32974 0.32395 0.07738  -0.00518 -0.01798 100 LYS A CA  
670  C C   . LYS A 93  ? 0.33034 0.33170 0.32377 0.06949  0.00475  -0.00283 100 LYS A C   
671  O O   . LYS A 93  ? 0.31981 0.32321 0.33195 0.06602  0.01342  -0.00401 100 LYS A O   
672  C CB  . LYS A 93  ? 0.35837 0.38623 0.34947 0.07808  -0.00387 -0.03143 100 LYS A CB  
673  C CG  . LYS A 93  ? 0.34778 0.38524 0.35192 0.07491  0.01000  -0.04094 100 LYS A CG  
674  C CD  . LYS A 93  ? 0.37305 0.43096 0.36385 0.07601  0.01266  -0.05818 100 LYS A CD  
675  C CE  . LYS A 93  ? 0.38883 0.45447 0.40258 0.07776  0.02423  -0.07320 100 LYS A CE  
676  N NZ  . LYS A 93  ? 0.45471 0.54431 0.45212 0.07735  0.03185  -0.08790 100 LYS A NZ  
677  N N   . ALA A 94  ? 0.34404 0.33547 0.30704 0.06593  0.00277  0.01181  101 ALA A N   
678  C CA  . ALA A 94  ? 0.39079 0.37478 0.34435 0.05415  0.01326  0.02511  101 ALA A CA  
679  C C   . ALA A 94  ? 0.36697 0.33638 0.34138 0.05265  0.01325  0.02961  101 ALA A C   
680  O O   . ALA A 94  ? 0.38431 0.36014 0.36992 0.04432  0.02283  0.03063  101 ALA A O   
681  C CB  . ALA A 94  ? 0.42901 0.39611 0.34196 0.04831  0.01083  0.04215  101 ALA A CB  
682  N N   . ASP A 95  ? 0.37407 0.32855 0.35541 0.06119  0.00222  0.02973  102 ASP A N   
683  C CA  . ASP A 95  ? 0.37298 0.31755 0.37434 0.06021  0.00296  0.02972  102 ASP A CA  
684  C C   . ASP A 95  ? 0.35142 0.31246 0.37794 0.05846  0.01014  0.02013  102 ASP A C   
685  O O   . ASP A 95  ? 0.33376 0.29428 0.36858 0.05216  0.01564  0.02283  102 ASP A O   
686  C CB  . ASP A 95  ? 0.37913 0.31389 0.38861 0.07173  -0.00911 0.02562  102 ASP A CB  
687  C CG  . ASP A 95  ? 0.49059 0.39915 0.47748 0.07677  -0.01894 0.03758  102 ASP A CG  
688  O OD1 . ASP A 95  ? 0.52557 0.41532 0.49070 0.06675  -0.01395 0.05131  102 ASP A OD1 
689  O OD2 . ASP A 95  ? 0.47049 0.37675 0.46186 0.09104  -0.03242 0.03292  102 ASP A OD2 
690  N N   . LEU A 96  ? 0.31235 0.28571 0.35012 0.06402  0.00890  0.00882  103 LEU A N   
691  C CA  . LEU A 96  ? 0.30433 0.28415 0.36199 0.06312  0.01452  0.00243  103 LEU A CA  
692  C C   . LEU A 96  ? 0.34376 0.33245 0.40169 0.05939  0.02194  0.00593  103 LEU A C   
693  O O   . LEU A 96  ? 0.30833 0.29713 0.37710 0.05778  0.02429  0.00837  103 LEU A O   
694  C CB  . LEU A 96  ? 0.31958 0.30632 0.38653 0.06759  0.01305  -0.01094 103 LEU A CB  
695  C CG  . LEU A 96  ? 0.32484 0.31047 0.40384 0.06902  0.00761  -0.01928 103 LEU A CG  
696  C CD1 . LEU A 96  ? 0.29568 0.28858 0.38368 0.06999  0.00715  -0.03474 103 LEU A CD1 
697  C CD2 . LEU A 96  ? 0.29327 0.27147 0.38607 0.06394  0.01197  -0.01677 103 LEU A CD2 
698  N N   . ILE A 97  ? 0.32278 0.32289 0.36874 0.05813  0.02549  0.00507  104 ILE A N   
699  C CA  . ILE A 97  ? 0.32054 0.33850 0.37289 0.05548  0.03343  0.00366  104 ILE A CA  
700  C C   . ILE A 97  ? 0.32739 0.34489 0.37827 0.04550  0.03617  0.01369  104 ILE A C   
701  O O   . ILE A 97  ? 0.33651 0.36787 0.40269 0.04499  0.03854  0.01219  104 ILE A O   
702  C CB  . ILE A 97  ? 0.35404 0.38943 0.39327 0.05425  0.03924  -0.00254 104 ILE A CB  
703  C CG1 . ILE A 97  ? 0.30292 0.34170 0.34839 0.06423  0.03670  -0.01776 104 ILE A CG1 
704  C CG2 . ILE A 97  ? 0.33226 0.39366 0.38130 0.04975  0.04922  -0.00577 104 ILE A CG2 
705  C CD1 . ILE A 97  ? 0.37322 0.42891 0.39844 0.06289  0.04092  -0.02622 104 ILE A CD1 
706  N N   . ASN A 98  ? 0.30695 0.30707 0.34032 0.03847  0.03419  0.02300  105 ASN A N   
707  C CA  . ASN A 98  ? 0.37008 0.36295 0.39987 0.02658  0.03675  0.03088  105 ASN A CA  
708  C C   . ASN A 98  ? 0.33451 0.31687 0.37713 0.02928  0.03153  0.03004  105 ASN A C   
709  O O   . ASN A 98  ? 0.34487 0.30620 0.38044 0.02625  0.02826  0.03398  105 ASN A O   
710  C CB  . ASN A 98  ? 0.40121 0.37095 0.40359 0.01934  0.03604  0.04163  105 ASN A CB  
711  C CG  . ASN A 98  ? 0.55146 0.51285 0.54697 0.00197  0.04235  0.04890  105 ASN A CG  
712  O OD1 . ASN A 98  ? 0.54920 0.53076 0.56249 -0.00557 0.04753  0.04362  105 ASN A OD1 
713  N ND2 . ASN A 98  ? 0.60337 0.53420 0.57206 -0.00505 0.04124  0.06106  105 ASN A ND2 
714  N N   . ASN A 99  ? 0.32010 0.31532 0.37964 0.03570  0.03068  0.02460  106 ASN A N   
715  C CA  . ASN A 99  ? 0.29432 0.28446 0.36171 0.03611  0.02751  0.02443  106 ASN A CA  
716  C C   . ASN A 99  ? 0.34899 0.31991 0.41303 0.03881  0.02403  0.02323  106 ASN A C   
717  O O   . ASN A 99  ? 0.30882 0.27169 0.37208 0.03459  0.02334  0.02271  106 ASN A O   
718  C CB  . ASN A 99  ? 0.33740 0.33523 0.40575 0.02533  0.02897  0.02602  106 ASN A CB  
719  C CG  . ASN A 99  ? 0.27552 0.30245 0.35475 0.02393  0.03157  0.02368  106 ASN A CG  
720  O OD1 . ASN A 99  ? 0.28395 0.32348 0.37436 0.03469  0.02871  0.02126  106 ASN A OD1 
721  N ND2 . ASN A 99  ? 0.30925 0.34633 0.38631 0.01069  0.03717  0.02369  106 ASN A ND2 
722  N N   . LEU A 100 ? 0.31174 0.27969 0.37682 0.04623  0.02185  0.01956  107 LEU A N   
723  C CA  . LEU A 100 ? 0.33352 0.29247 0.40213 0.05030  0.01809  0.01458  107 LEU A CA  
724  C C   . LEU A 100 ? 0.37044 0.31503 0.43191 0.04967  0.01464  0.01653  107 LEU A C   
725  O O   . LEU A 100 ? 0.34835 0.28875 0.41706 0.05063  0.01393  0.01089  107 LEU A O   
726  C CB  . LEU A 100 ? 0.28335 0.24492 0.36282 0.04859  0.02101  0.01051  107 LEU A CB  
727  C CG  . LEU A 100 ? 0.32092 0.28646 0.40515 0.05006  0.02327  0.01090  107 LEU A CG  
728  C CD1 . LEU A 100 ? 0.39146 0.35997 0.47374 0.04786  0.02448  0.01776  107 LEU A CD1 
729  C CD2 . LEU A 100 ? 0.36921 0.33118 0.46220 0.04899  0.02523  0.00447  107 LEU A CD2 
730  N N   . GLY A 101 ? 0.29921 0.23441 0.34522 0.04785  0.01310  0.02405  108 GLY A N   
731  C CA  . GLY A 101 ? 0.37613 0.28772 0.41177 0.04877  0.00817  0.02810  108 GLY A CA  
732  C C   . GLY A 101 ? 0.38415 0.28481 0.42135 0.03964  0.01177  0.02761  108 GLY A C   
733  O O   . GLY A 101 ? 0.48408 0.36115 0.51768 0.04284  0.00715  0.02690  108 GLY A O   
734  N N   . THR A 102 ? 0.37428 0.29146 0.41736 0.02973  0.01841  0.02646  109 THR A N   
735  C CA  . THR A 102 ? 0.37894 0.29257 0.42395 0.01930  0.02124  0.02300  109 THR A CA  
736  C C   . THR A 102 ? 0.41417 0.32962 0.45182 0.00452  0.02606  0.02890  109 THR A C   
737  O O   . THR A 102 ? 0.38809 0.31619 0.42188 0.00248  0.02922  0.03456  109 THR A O   
738  C CB  . THR A 102 ? 0.35892 0.29447 0.41474 0.01847  0.02324  0.01647  109 THR A CB  
739  O OG1 . THR A 102 ? 0.36491 0.32258 0.42386 0.01664  0.02500  0.02075  109 THR A OG1 
740  C CG2 . THR A 102 ? 0.40724 0.34550 0.47040 0.02844  0.02215  0.01087  109 THR A CG2 
741  N N   . ILE A 103 ? 0.35315 0.25961 0.39077 -0.00735 0.02779  0.02464  110 ILE A N   
742  C CA  . ILE A 103 ? 0.35381 0.27003 0.39043 -0.02580 0.03371  0.02604  110 ILE A CA  
743  C C   . ILE A 103 ? 0.35695 0.31045 0.40878 -0.02852 0.03347  0.01781  110 ILE A C   
744  O O   . ILE A 103 ? 0.36987 0.32992 0.42598 -0.04102 0.03386  0.00972  110 ILE A O   
745  C CB  . ILE A 103 ? 0.44331 0.32510 0.47073 -0.03988 0.03533  0.02511  110 ILE A CB  
746  C CG1 . ILE A 103 ? 0.41132 0.28029 0.44486 -0.03465 0.03096  0.01241  110 ILE A CG1 
747  C CG2 . ILE A 103 ? 0.44181 0.28418 0.44848 -0.03698 0.03405  0.03856  110 ILE A CG2 
748  C CD1 . ILE A 103 ? 0.58496 0.41779 0.61231 -0.04838 0.03238  0.00756  110 ILE A CD1 
749  N N   . ALA A 104 ? 0.31913 0.29593 0.37813 -0.01634 0.03155  0.01963  111 ALA A N   
750  C CA  . ALA A 104 ? 0.31475 0.31852 0.38341 -0.01287 0.02754  0.01503  111 ALA A CA  
751  C C   . ALA A 104 ? 0.28081 0.31563 0.35997 -0.02460 0.02779  0.01016  111 ALA A C   
752  O O   . ALA A 104 ? 0.30487 0.35729 0.38772 -0.02606 0.02223  0.00444  111 ALA A O   
753  C CB  . ALA A 104 ? 0.32547 0.33828 0.39819 0.00311  0.02505  0.01949  111 ALA A CB  
754  N N   . LYS A 105 ? 0.27886 0.32472 0.36261 -0.03415 0.03421  0.01109  112 LYS A N   
755  C CA  . LYS A 105 ? 0.30072 0.38467 0.40050 -0.04658 0.03506  0.00289  112 LYS A CA  
756  C C   . LYS A 105 ? 0.37330 0.44988 0.47110 -0.06539 0.03490  -0.00555 112 LYS A C   
757  O O   . LYS A 105 ? 0.31049 0.41545 0.41817 -0.06777 0.02789  -0.01489 112 LYS A O   
758  C CB  . LYS A 105 ? 0.28265 0.38404 0.38841 -0.05650 0.04553  0.00346  112 LYS A CB  
759  C CG  . LYS A 105 ? 0.40123 0.54815 0.52864 -0.07272 0.04846  -0.00829 112 LYS A CG  
760  C CD  . LYS A 105 ? 0.38398 0.56413 0.52363 -0.07602 0.05907  -0.01086 112 LYS A CD  
761  C CE  . LYS A 105 ? 0.52295 0.75403 0.68846 -0.09589 0.06414  -0.02549 112 LYS A CE  
762  N NZ  . LYS A 105 ? 0.55771 0.81915 0.73184 -0.10792 0.08045  -0.02954 112 LYS A NZ  
763  N N   . SER A 106 ? 0.32790 0.36429 0.41162 -0.07798 0.04119  -0.00300 113 SER A N   
764  C CA  . SER A 106 ? 0.36500 0.38912 0.44784 -0.09629 0.04148  -0.01379 113 SER A CA  
765  C C   . SER A 106 ? 0.34907 0.36431 0.42698 -0.08533 0.03327  -0.02095 113 SER A C   
766  O O   . SER A 106 ? 0.38319 0.41167 0.46510 -0.09627 0.03008  -0.03476 113 SER A O   
767  C CB  . SER A 106 ? 0.47876 0.45461 0.54649 -0.11197 0.04985  -0.00806 113 SER A CB  
768  O OG  . SER A 106 ? 0.47017 0.40375 0.52171 -0.09470 0.04689  0.00164  113 SER A OG  
769  N N   . GLY A 107 ? 0.32697 0.32449 0.39643 -0.06548 0.03057  -0.01367 114 GLY A N   
770  C CA  . GLY A 107 ? 0.33562 0.33099 0.40000 -0.05681 0.02572  -0.02095 114 GLY A CA  
771  C C   . GLY A 107 ? 0.34280 0.37889 0.41068 -0.05437 0.01864  -0.02457 114 GLY A C   
772  O O   . GLY A 107 ? 0.32931 0.37318 0.39139 -0.05928 0.01525  -0.03577 114 GLY A O   
773  N N   . THR A 108 ? 0.32017 0.38216 0.39605 -0.04531 0.01533  -0.01563 115 THR A N   
774  C CA  . THR A 108 ? 0.27733 0.37556 0.35575 -0.03941 0.00524  -0.01664 115 THR A CA  
775  C C   . THR A 108 ? 0.32591 0.45417 0.41325 -0.05610 0.00110  -0.03094 115 THR A C   
776  O O   . THR A 108 ? 0.27778 0.42614 0.35791 -0.05621 -0.00806 -0.03733 115 THR A O   
777  C CB  . THR A 108 ? 0.27704 0.39418 0.36673 -0.02421 0.00175  -0.00656 115 THR A CB  
778  O OG1 . THR A 108 ? 0.26630 0.35599 0.34723 -0.01028 0.00476  0.00423  115 THR A OG1 
779  C CG2 . THR A 108 ? 0.28568 0.43614 0.37787 -0.01454 -0.01170 -0.00601 115 THR A CG2 
780  N N   . LYS A 109 ? 0.29851 0.43100 0.39978 -0.07242 0.00810  -0.03662 116 LYS A N   
781  C CA  . LYS A 109 ? 0.29983 0.46252 0.41338 -0.09270 0.00568  -0.05319 116 LYS A CA  
782  C C   . LYS A 109 ? 0.34851 0.49021 0.44835 -0.10481 0.00534  -0.06670 116 LYS A C   
783  O O   . LYS A 109 ? 0.36845 0.54118 0.46961 -0.11203 -0.00350 -0.08089 116 LYS A O   
784  C CB  . LYS A 109 ? 0.30988 0.47453 0.43850 -0.11205 0.01745  -0.05527 116 LYS A CB  
785  C CG  . LYS A 109 ? 0.48320 0.68298 0.63097 -0.13871 0.01857  -0.07373 116 LYS A CG  
786  C CD  . LYS A 109 ? 0.50842 0.67900 0.65646 -0.16438 0.03556  -0.07260 116 LYS A CD  
787  C CE  . LYS A 109 ? 0.58906 0.78559 0.75503 -0.19749 0.03985  -0.09247 116 LYS A CE  
788  N NZ  . LYS A 109 ? 0.58827 0.84912 0.77418 -0.19314 0.02447  -0.10929 116 LYS A NZ  
789  N N   . ALA A 110 ? 0.32828 0.41925 0.41560 -0.10608 0.01393  -0.06460 117 ALA A N   
790  C CA  . ALA A 110 ? 0.33676 0.40587 0.41365 -0.11508 0.01456  -0.08091 117 ALA A CA  
791  C C   . ALA A 110 ? 0.35343 0.44021 0.41575 -0.10229 0.00678  -0.08445 117 ALA A C   
792  O O   . ALA A 110 ? 0.37481 0.47345 0.43072 -0.11248 0.00330  -0.10286 117 ALA A O   
793  C CB  . ALA A 110 ? 0.40700 0.41811 0.47626 -0.11326 0.02331  -0.07777 117 ALA A CB  
794  N N   . PHE A 111 ? 0.34323 0.43023 0.39775 -0.08207 0.00495  -0.06761 118 PHE A N   
795  C CA  . PHE A 111 ? 0.34511 0.44620 0.38076 -0.07238 -0.00067 -0.06676 118 PHE A CA  
796  C C   . PHE A 111 ? 0.37921 0.52614 0.41217 -0.07533 -0.01418 -0.07071 118 PHE A C   
797  O O   . PHE A 111 ? 0.34563 0.50753 0.36163 -0.08101 -0.01905 -0.08278 118 PHE A O   
798  C CB  . PHE A 111 ? 0.30930 0.39821 0.33935 -0.05351 0.00098  -0.04645 118 PHE A CB  
799  C CG  . PHE A 111 ? 0.32882 0.42526 0.33564 -0.04602 -0.00202 -0.04107 118 PHE A CG  
800  C CD1 . PHE A 111 ? 0.34306 0.44099 0.33204 -0.05410 0.00115  -0.05593 118 PHE A CD1 
801  C CD2 . PHE A 111 ? 0.35088 0.44820 0.35184 -0.03176 -0.00597 -0.02123 118 PHE A CD2 
802  C CE1 . PHE A 111 ? 0.37367 0.47838 0.33615 -0.05029 0.00097  -0.04912 118 PHE A CE1 
803  C CE2 . PHE A 111 ? 0.37311 0.47030 0.34814 -0.02782 -0.00704 -0.01288 118 PHE A CE2 
804  C CZ  . PHE A 111 ? 0.32743 0.42953 0.28157 -0.03816 -0.00288 -0.02592 118 PHE A CZ  
805  N N   . MET A 112 ? 0.38501 0.55836 0.43551 -0.07130 -0.02103 -0.06300 119 MET A N   
806  C CA  . MET A 112 ? 0.39640 0.61764 0.44769 -0.06978 -0.03728 -0.06704 119 MET A CA  
807  C C   . MET A 112 ? 0.41617 0.66138 0.47466 -0.09255 -0.04002 -0.09247 119 MET A C   
808  O O   . MET A 112 ? 0.38321 0.66027 0.42845 -0.09396 -0.05315 -0.10154 119 MET A O   
809  C CB  . MET A 112 ? 0.39600 0.64220 0.46985 -0.05644 -0.04380 -0.05545 119 MET A CB  
810  C CG  . MET A 112 ? 0.40283 0.63175 0.46161 -0.03170 -0.04791 -0.03248 119 MET A CG  
811  S SD  . MET A 112 ? 0.65213 0.90689 0.73806 -0.01163 -0.05624 -0.02227 119 MET A SD  
812  C CE  . MET A 112 ? 0.49447 0.80102 0.57759 -0.00116 -0.08239 -0.02532 119 MET A CE  
813  N N   . GLU A 113 ? 0.38255 0.60952 0.45822 -0.11173 -0.02797 -0.10440 120 GLU A N   
814  C CA  . GLU A 113 ? 0.45079 0.69101 0.53214 -0.13662 -0.02850 -0.13096 120 GLU A CA  
815  C C   . GLU A 113 ? 0.44925 0.66954 0.50463 -0.13986 -0.02718 -0.14490 120 GLU A C   
816  O O   . GLU A 113 ? 0.43490 0.68263 0.48576 -0.15359 -0.03466 -0.16716 120 GLU A O   
817  C CB  . GLU A 113 ? 0.50707 0.72015 0.60817 -0.15807 -0.01412 -0.13761 120 GLU A CB  
818  C CG  . GLU A 113 ? 0.52819 0.77032 0.65627 -0.16234 -0.01229 -0.13046 120 GLU A CG  
819  C CD  . GLU A 113 ? 0.65426 0.85729 0.79128 -0.18356 0.00521  -0.12989 120 GLU A CD  
820  O OE1 . GLU A 113 ? 0.67128 0.90350 0.83143 -0.20025 0.01008  -0.13380 120 GLU A OE1 
821  O OE2 . GLU A 113 ? 0.64001 0.78327 0.76011 -0.18288 0.01405  -0.12478 120 GLU A OE2 
822  N N   . ALA A 114 ? 0.39977 0.57715 0.43962 -0.12791 -0.01750 -0.13511 121 ALA A N   
823  C CA  . ALA A 114 ? 0.43944 0.60339 0.45687 -0.12946 -0.01407 -0.15049 121 ALA A CA  
824  C C   . ALA A 114 ? 0.46585 0.66914 0.45701 -0.12246 -0.02635 -0.14886 121 ALA A C   
825  O O   . ALA A 114 ? 0.48272 0.70103 0.45732 -0.13305 -0.02880 -0.17085 121 ALA A O   
826  C CB  . ALA A 114 ? 0.41242 0.53080 0.42430 -0.11638 -0.00146 -0.14096 121 ALA A CB  
827  N N   . LEU A 115 ? 0.38850 0.60605 0.37285 -0.10467 -0.03448 -0.12300 122 LEU A N   
828  C CA  . LEU A 115 ? 0.40702 0.65593 0.36106 -0.09663 -0.04838 -0.11561 122 LEU A CA  
829  C C   . LEU A 115 ? 0.45493 0.75350 0.41149 -0.10703 -0.06564 -0.13294 122 LEU A C   
830  O O   . LEU A 115 ? 0.48989 0.81233 0.41594 -0.11013 -0.07485 -0.14154 122 LEU A O   
831  C CB  . LEU A 115 ? 0.39225 0.63894 0.34256 -0.07482 -0.05506 -0.08382 122 LEU A CB  
832  C CG  . LEU A 115 ? 0.40300 0.60615 0.34737 -0.06529 -0.03961 -0.06740 122 LEU A CG  
833  C CD1 . LEU A 115 ? 0.40300 0.60141 0.34577 -0.04564 -0.04664 -0.03884 122 LEU A CD1 
834  C CD2 . LEU A 115 ? 0.41909 0.61262 0.32998 -0.07056 -0.03090 -0.07362 122 LEU A CD2 
835  N N   . GLN A 116 ? 0.47844 0.79723 0.47055 -0.11392 -0.07007 -0.13965 123 GLN A N   
836  C CA  . GLN A 116 ? 0.49102 0.86289 0.49098 -0.12659 -0.08624 -0.16122 123 GLN A CA  
837  C C   . GLN A 116 ? 0.49478 0.86334 0.48682 -0.15093 -0.07999 -0.19440 123 GLN A C   
838  O O   . GLN A 116 ? 0.54021 0.95378 0.52559 -0.16107 -0.09477 -0.21469 123 GLN A O   
839  C CB  . GLN A 116 ? 0.54749 0.94775 0.59177 -0.13246 -0.08954 -0.16499 123 GLN A CB  
840  C CG  . GLN A 116 ? 0.60721 1.01837 0.66243 -0.10691 -0.09747 -0.13786 123 GLN A CG  
841  C CD  . GLN A 116 ? 0.71816 1.17166 0.75396 -0.08704 -0.12351 -0.12870 123 GLN A CD  
842  O OE1 . GLN A 116 ? 0.67441 1.18561 0.72651 -0.09010 -0.14193 -0.14396 123 GLN A OE1 
843  N NE2 . GLN A 116 ? 0.67103 1.09540 0.67104 -0.06679 -0.12583 -0.10315 123 GLN A NE2 
844  N N   . ALA A 117 ? 0.53710 0.85418 0.52991 -0.15895 -0.05995 -0.20196 124 ALA A N   
845  C CA  . ALA A 117 ? 0.56978 0.87513 0.55794 -0.17995 -0.05258 -0.23573 124 ALA A CA  
846  C C   . ALA A 117 ? 0.52134 0.81353 0.47213 -0.17372 -0.04669 -0.24185 124 ALA A C   
847  O O   . ALA A 117 ? 0.61599 0.89161 0.56345 -0.18755 -0.03762 -0.27146 124 ALA A O   
848  C CB  . ALA A 117 ? 0.57538 0.82966 0.59086 -0.19291 -0.03533 -0.24362 124 ALA A CB  
849  N N   . GLY A 118 ? 0.54261 0.84065 0.46562 -0.15450 -0.05024 -0.21608 125 GLY A N   
850  C CA  . GLY A 118 ? 0.54882 0.84515 0.43292 -0.15289 -0.04391 -0.22309 125 GLY A CA  
851  C C   . GLY A 118 ? 0.55032 0.80536 0.42851 -0.14083 -0.02539 -0.20885 125 GLY A C   
852  O O   . GLY A 118 ? 0.55072 0.80081 0.40773 -0.14433 -0.01380 -0.22509 125 GLY A O   
853  N N   . ALA A 119 ? 0.54511 0.77433 0.44344 -0.12748 -0.02173 -0.18222 126 ALA A N   
854  C CA  . ALA A 119 ? 0.54140 0.73974 0.43429 -0.11546 -0.00696 -0.16729 126 ALA A CA  
855  C C   . ALA A 119 ? 0.57664 0.78787 0.43984 -0.10384 -0.01343 -0.13668 126 ALA A C   
856  O O   . ALA A 119 ? 0.61941 0.85741 0.47189 -0.10030 -0.03128 -0.12354 126 ALA A O   
857  C CB  . ALA A 119 ? 0.58485 0.74594 0.51369 -0.10832 0.00030  -0.15738 126 ALA A CB  
858  N N   . ASP A 120 ? 0.64533 0.83757 0.49503 -0.09808 0.00054  -0.12600 127 ASP A N   
859  C CA  . ASP A 120 ? 0.68218 0.87377 0.50871 -0.08758 -0.00486 -0.09234 127 ASP A CA  
860  C C   . ASP A 120 ? 0.49243 0.65165 0.34430 -0.07644 0.00454  -0.07517 127 ASP A C   
861  O O   . ASP A 120 ? 0.51972 0.65946 0.40305 -0.07577 0.01418  -0.08778 127 ASP A O   
862  C CB  . ASP A 120 ? 0.80134 1.00163 0.57965 -0.09354 0.00215  -0.08694 127 ASP A CB  
863  C CG  . ASP A 120 ? 0.83650 1.01802 0.61886 -0.09693 0.02658  -0.09471 127 ASP A CG  
864  O OD1 . ASP A 120 ? 0.82352 1.00193 0.63042 -0.10109 0.03727  -0.12447 127 ASP A OD1 
865  O OD2 . ASP A 120 ? 0.63293 0.80180 0.39741 -0.09492 0.03437  -0.07164 127 ASP A OD2 
866  N N   . ILE A 121 ? 0.55175 0.70383 0.38638 -0.06746 0.00023  -0.04594 128 ILE A N   
867  C CA  . ILE A 121 ? 0.55615 0.68107 0.41177 -0.05639 0.00530  -0.02748 128 ILE A CA  
868  C C   . ILE A 121 ? 0.48830 0.59531 0.35910 -0.05981 0.02543  -0.04005 128 ILE A C   
869  O O   . ILE A 121 ? 0.44160 0.52954 0.34213 -0.05188 0.02906  -0.03664 128 ILE A O   
870  C CB  . ILE A 121 ? 0.54196 0.65830 0.36882 -0.04893 -0.00155 0.00340  128 ILE A CB  
871  C CG1 . ILE A 121 ? 0.69632 0.82770 0.52224 -0.03697 -0.02524 0.01728  128 ILE A CG1 
872  C CG2 . ILE A 121 ? 0.46491 0.55193 0.30795 -0.04200 0.00793  0.01770  128 ILE A CG2 
873  C CD1 . ILE A 121 ? 0.62046 0.77764 0.40668 -0.04049 -0.03976 0.01941  128 ILE A CD1 
874  N N   . SER A 122 ? 0.50990 0.62636 0.36155 -0.07076 0.03833  -0.05640 129 SER A N   
875  C CA  . SER A 122 ? 0.46401 0.56903 0.33359 -0.07121 0.05674  -0.06770 129 SER A CA  
876  C C   . SER A 122 ? 0.45505 0.54873 0.36403 -0.06546 0.05862  -0.08929 129 SER A C   
877  O O   . SER A 122 ? 0.46227 0.54581 0.39291 -0.06050 0.06946  -0.09720 129 SER A O   
878  C CB  . SER A 122 ? 0.45360 0.57673 0.29525 -0.08457 0.07253  -0.08216 129 SER A CB  
879  O OG  . SER A 122 ? 0.53875 0.67881 0.37892 -0.09090 0.07338  -0.11212 129 SER A OG  
880  N N   . MET A 123 ? 0.38487 0.47900 0.30358 -0.06623 0.04772  -0.09820 130 MET A N   
881  C CA  . MET A 123 ? 0.40909 0.48262 0.36041 -0.06181 0.04792  -0.11267 130 MET A CA  
882  C C   . MET A 123 ? 0.37560 0.42917 0.34842 -0.05156 0.04179  -0.09220 130 MET A C   
883  O O   . MET A 123 ? 0.37602 0.40849 0.37042 -0.04859 0.04105  -0.09916 130 MET A O   
884  C CB  . MET A 123 ? 0.41194 0.49234 0.36258 -0.07214 0.04125  -0.13254 130 MET A CB  
885  C CG  . MET A 123 ? 0.48142 0.58174 0.41120 -0.08211 0.04883  -0.15884 130 MET A CG  
886  S SD  . MET A 123 ? 0.58715 0.70137 0.51181 -0.09761 0.04033  -0.18659 130 MET A SD  
887  C CE  . MET A 123 ? 0.57235 0.64378 0.53618 -0.09509 0.04086  -0.19770 130 MET A CE  
888  N N   . ILE A 124 ? 0.32939 0.38615 0.29478 -0.04610 0.03797  -0.06760 131 ILE A N   
889  C CA  . ILE A 124 ? 0.33599 0.37881 0.31960 -0.03669 0.03237  -0.05025 131 ILE A CA  
890  C C   . ILE A 124 ? 0.30381 0.32292 0.31082 -0.02979 0.03796  -0.05656 131 ILE A C   
891  O O   . ILE A 124 ? 0.31004 0.31586 0.33089 -0.02681 0.03345  -0.05142 131 ILE A O   
892  C CB  . ILE A 124 ? 0.32155 0.36569 0.29417 -0.03036 0.03057  -0.02744 131 ILE A CB  
893  C CG1 . ILE A 124 ? 0.31734 0.35214 0.30810 -0.02047 0.02416  -0.01300 131 ILE A CG1 
894  C CG2 . ILE A 124 ? 0.33176 0.36997 0.29924 -0.03126 0.04357  -0.02876 131 ILE A CG2 
895  C CD1 . ILE A 124 ? 0.35977 0.39122 0.34160 -0.01282 0.02088  0.00746  131 ILE A CD1 
896  N N   . GLY A 125 ? 0.32868 0.34446 0.33972 -0.02727 0.04749  -0.06868 132 GLY A N   
897  C CA  . GLY A 125 ? 0.33944 0.33531 0.37295 -0.01675 0.04933  -0.07409 132 GLY A CA  
898  C C   . GLY A 125 ? 0.36685 0.34069 0.41066 -0.01619 0.04530  -0.08575 132 GLY A C   
899  O O   . GLY A 125 ? 0.40218 0.35292 0.45926 -0.00660 0.04204  -0.08194 132 GLY A O   
900  N N   . GLN A 126 ? 0.36636 0.34455 0.40206 -0.02708 0.04509  -0.10014 133 GLN A N   
901  C CA  . GLN A 126 ? 0.39778 0.34920 0.44177 -0.03025 0.04211  -0.11183 133 GLN A CA  
902  C C   . GLN A 126 ? 0.45262 0.39015 0.49857 -0.03497 0.03570  -0.09419 133 GLN A C   
903  O O   . GLN A 126 ? 0.47087 0.37812 0.52197 -0.03915 0.03427  -0.09898 133 GLN A O   
904  C CB  . GLN A 126 ? 0.43722 0.39986 0.47214 -0.04379 0.04378  -0.13437 133 GLN A CB  
905  C CG  . GLN A 126 ? 0.49367 0.47457 0.52407 -0.04126 0.05279  -0.15514 133 GLN A CG  
906  C CD  . GLN A 126 ? 0.55931 0.55647 0.57612 -0.05545 0.05456  -0.17916 133 GLN A CD  
907  O OE1 . GLN A 126 ? 0.56825 0.55416 0.58620 -0.06618 0.04904  -0.18716 133 GLN A OE1 
908  N NE2 . GLN A 126 ? 0.57332 0.59865 0.57618 -0.05781 0.06325  -0.19242 133 GLN A NE2 
909  N N   . PHE A 127 ? 0.38672 0.34438 0.42834 -0.03507 0.03271  -0.07497 134 PHE A N   
910  C CA  . PHE A 127 ? 0.33819 0.29315 0.38330 -0.04059 0.02872  -0.06098 134 PHE A CA  
911  C C   . PHE A 127 ? 0.37673 0.32289 0.42619 -0.02855 0.02826  -0.04278 134 PHE A C   
912  O O   . PHE A 127 ? 0.37847 0.32949 0.42997 -0.03198 0.02667  -0.03095 134 PHE A O   
913  C CB  . PHE A 127 ? 0.32462 0.31568 0.36471 -0.04971 0.02401  -0.05877 134 PHE A CB  
914  C CG  . PHE A 127 ? 0.34816 0.35154 0.38165 -0.06231 0.02307  -0.07890 134 PHE A CG  
915  C CD1 . PHE A 127 ? 0.43390 0.42090 0.47375 -0.07679 0.02414  -0.09351 134 PHE A CD1 
916  C CD2 . PHE A 127 ? 0.33046 0.35686 0.34879 -0.06106 0.02234  -0.08464 134 PHE A CD2 
917  C CE1 . PHE A 127 ? 0.39635 0.39393 0.43074 -0.08918 0.02344  -0.11649 134 PHE A CE1 
918  C CE2 . PHE A 127 ? 0.42474 0.46401 0.43393 -0.07272 0.02173  -0.10572 134 PHE A CE2 
919  C CZ  . PHE A 127 ? 0.45948 0.48579 0.47837 -0.08642 0.02185  -0.12335 134 PHE A CZ  
920  N N   . GLY A 128 ? 0.34148 0.27874 0.39387 -0.01536 0.03008  -0.04310 135 GLY A N   
921  C CA  . GLY A 128 ? 0.35860 0.28643 0.41521 -0.00422 0.02853  -0.02992 135 GLY A CA  
922  C C   . GLY A 128 ? 0.35118 0.30072 0.40687 -0.00052 0.02816  -0.01754 135 GLY A C   
923  O O   . GLY A 128 ? 0.37570 0.31969 0.43455 0.00722  0.02681  -0.00832 135 GLY A O   
924  N N   . VAL A 129 ? 0.29472 0.26642 0.34426 -0.00504 0.02827  -0.01708 136 VAL A N   
925  C CA  . VAL A 129 ? 0.26661 0.25164 0.31453 0.00006  0.02631  -0.00422 136 VAL A CA  
926  C C   . VAL A 129 ? 0.27995 0.27064 0.31954 0.00111  0.02990  -0.00422 136 VAL A C   
927  O O   . VAL A 129 ? 0.28083 0.27899 0.31234 0.00279  0.02750  0.00648  136 VAL A O   
928  C CB  . VAL A 129 ? 0.28529 0.28961 0.33238 -0.00423 0.02061  0.00097  136 VAL A CB  
929  C CG1 . VAL A 129 ? 0.29903 0.30015 0.35567 -0.00745 0.02083  0.00270  136 VAL A CG1 
930  C CG2 . VAL A 129 ? 0.27672 0.29488 0.31570 -0.01451 0.01823  -0.00866 136 VAL A CG2 
931  N N   . GLY A 130 ? 0.24182 0.27821 0.27670 -0.01585 0.03545  -0.01393 137 GLY A N   
932  C CA  . GLY A 130 ? 0.26277 0.29618 0.29126 -0.01442 0.03471  -0.01098 137 GLY A CA  
933  C C   . GLY A 130 ? 0.26853 0.29870 0.29629 -0.01229 0.03221  -0.00632 137 GLY A C   
934  O O   . GLY A 130 ? 0.27211 0.29999 0.29499 -0.01108 0.03091  -0.00322 137 GLY A O   
935  N N   . PHE A 131 ? 0.26161 0.29084 0.29343 -0.01168 0.03156  -0.00585 138 PHE A N   
936  C CA  . PHE A 131 ? 0.24460 0.26935 0.27575 -0.00992 0.02836  -0.00325 138 PHE A CA  
937  C C   . PHE A 131 ? 0.24992 0.27353 0.27696 -0.00700 0.02459  -0.00280 138 PHE A C   
938  O O   . PHE A 131 ? 0.25688 0.27407 0.28200 -0.00650 0.02291  0.00062  138 PHE A O   
939  C CB  . PHE A 131 ? 0.29611 0.32094 0.32953 -0.00840 0.02743  -0.00454 138 PHE A CB  
940  C CG  . PHE A 131 ? 0.27053 0.29023 0.30223 -0.00589 0.02300  -0.00452 138 PHE A CG  
941  C CD1 . PHE A 131 ? 0.27240 0.28662 0.30586 -0.00767 0.02116  -0.00265 138 PHE A CD1 
942  C CD2 . PHE A 131 ? 0.26078 0.28124 0.29031 -0.00173 0.02064  -0.00687 138 PHE A CD2 
943  C CE1 . PHE A 131 ? 0.27059 0.27789 0.30313 -0.00610 0.01657  -0.00382 138 PHE A CE1 
944  C CE2 . PHE A 131 ? 0.28269 0.29607 0.31010 0.00127  0.01661  -0.00783 138 PHE A CE2 
945  C CZ  . PHE A 131 ? 0.27430 0.27992 0.30289 -0.00130 0.01435  -0.00662 138 PHE A CZ  
946  N N   . TYR A 132 ? 0.24667 0.27653 0.27348 -0.00493 0.02321  -0.00587 139 TYR A N   
947  C CA  . TYR A 132 ? 0.25178 0.28155 0.27533 -0.00039 0.01904  -0.00524 139 TYR A CA  
948  C C   . TYR A 132 ? 0.28238 0.30980 0.29907 0.00036  0.01807  -0.00165 139 TYR A C   
949  O O   . TYR A 132 ? 0.26599 0.29060 0.27876 0.00496  0.01461  0.00083  139 TYR A O   
950  C CB  . TYR A 132 ? 0.24457 0.28506 0.27213 0.00184  0.01773  -0.00955 139 TYR A CB  
951  C CG  . TYR A 132 ? 0.27743 0.32002 0.31019 0.00205  0.01994  -0.01160 139 TYR A CG  
952  C CD1 . TYR A 132 ? 0.27912 0.31822 0.31085 0.00698  0.01814  -0.01182 139 TYR A CD1 
953  C CD2 . TYR A 132 ? 0.27733 0.32406 0.31480 -0.00221 0.02433  -0.01310 139 TYR A CD2 
954  C CE1 . TYR A 132 ? 0.26038 0.30200 0.29421 0.00811  0.02076  -0.01367 139 TYR A CE1 
955  C CE2 . TYR A 132 ? 0.31348 0.36196 0.35375 -0.00145 0.02724  -0.01346 139 TYR A CE2 
956  C CZ  . TYR A 132 ? 0.31957 0.36640 0.35730 0.00390  0.02550  -0.01379 139 TYR A CZ  
957  O OH  . TYR A 132 ? 0.31414 0.36329 0.35216 0.00544  0.02888  -0.01406 139 TYR A OH  
958  N N   . SER A 133 ? 0.26995 0.29796 0.28410 -0.00303 0.02143  -0.00090 140 SER A N   
959  C CA  . SER A 133 ? 0.28537 0.31057 0.29099 -0.00181 0.02187  0.00371  140 SER A CA  
960  C C   . SER A 133 ? 0.24852 0.26333 0.25367 -0.00178 0.02253  0.01064  140 SER A C   
961  O O   . SER A 133 ? 0.26378 0.27490 0.26153 0.00003  0.02316  0.01638  140 SER A O   
962  C CB  . SER A 133 ? 0.29264 0.32046 0.29519 -0.00477 0.02651  0.00258  140 SER A CB  
963  O OG  . SER A 133 ? 0.28523 0.30934 0.29348 -0.00835 0.03118  0.00460  140 SER A OG  
964  N N   . ALA A 134 ? 0.29476 0.30468 0.30740 -0.00385 0.02232  0.01023  141 ALA A N   
965  C CA  . ALA A 134 ? 0.24953 0.24866 0.26385 -0.00452 0.02153  0.01523  141 ALA A CA  
966  C C   . ALA A 134 ? 0.27247 0.26517 0.28069 0.00088  0.01803  0.01855  141 ALA A C   
967  O O   . ALA A 134 ? 0.27919 0.26177 0.28586 0.00041  0.01884  0.02520  141 ALA A O   
968  C CB  . ALA A 134 ? 0.25588 0.25174 0.27775 -0.00607 0.01929  0.01142  141 ALA A CB  
969  N N   . TYR A 135 ? 0.26469 0.26327 0.27061 0.00624  0.01434  0.01447  142 TYR A N   
970  C CA  . TYR A 135 ? 0.26527 0.25873 0.26617 0.01314  0.01044  0.01748  142 TYR A CA  
971  C C   . TYR A 135 ? 0.30927 0.30450 0.29992 0.01614  0.01069  0.02349  142 TYR A C   
972  O O   . TYR A 135 ? 0.32394 0.31489 0.30899 0.02293  0.00736  0.02758  142 TYR A O   
973  C CB  . TYR A 135 ? 0.26104 0.26277 0.26546 0.01835  0.00667  0.01082  142 TYR A CB  
974  C CG  . TYR A 135 ? 0.31166 0.30770 0.32219 0.01768  0.00642  0.00659  142 TYR A CG  
975  C CD1 . TYR A 135 ? 0.29982 0.28218 0.30979 0.02159  0.00388  0.00765  142 TYR A CD1 
976  C CD2 . TYR A 135 ? 0.25752 0.26032 0.27316 0.01320  0.00881  0.00171  142 TYR A CD2 
977  C CE1 . TYR A 135 ? 0.27118 0.24793 0.28479 0.02124  0.00303  0.00238  142 TYR A CE1 
978  C CE2 . TYR A 135 ? 0.28705 0.28515 0.30562 0.01334  0.00822  -0.00211 142 TYR A CE2 
979  C CZ  . TYR A 135 ? 0.29086 0.27640 0.30799 0.01726  0.00505  -0.00236 142 TYR A CZ  
980  O OH  . TYR A 135 ? 0.27502 0.25613 0.29322 0.01787  0.00379  -0.00759 142 TYR A OH  
981  N N   . LEU A 136 ? 0.30405 0.30472 0.29098 0.01215  0.01471  0.02447  143 LEU A N   
982  C CA  . LEU A 136 ? 0.31009 0.31034 0.28477 0.01501  0.01614  0.03131  143 LEU A CA  
983  C C   . LEU A 136 ? 0.32301 0.30820 0.29565 0.01454  0.01929  0.04184  143 LEU A C   
984  O O   . LEU A 136 ? 0.34803 0.32890 0.30966 0.01974  0.01917  0.04977  143 LEU A O   
985  C CB  . LEU A 136 ? 0.31147 0.31971 0.28242 0.01100  0.02092  0.02919  143 LEU A CB  
986  C CG  . LEU A 136 ? 0.29600 0.31754 0.26792 0.01084  0.01813  0.01902  143 LEU A CG  
987  C CD1 . LEU A 136 ? 0.32923 0.35486 0.29917 0.00657  0.02357  0.01595  143 LEU A CD1 
988  C CD2 . LEU A 136 ? 0.32410 0.35337 0.28688 0.01775  0.01169  0.01780  143 LEU A CD2 
989  N N   . VAL A 137 ? 0.31489 0.29191 0.29840 0.00829  0.02190  0.04229  144 VAL A N   
990  C CA  . VAL A 137 ? 0.31022 0.27341 0.29519 0.00536  0.02572  0.05197  144 VAL A CA  
991  C C   . VAL A 137 ? 0.31756 0.26701 0.31226 0.00387  0.02232  0.05070  144 VAL A C   
992  O O   . VAL A 137 ? 0.33917 0.27416 0.33563 0.00201  0.02422  0.05855  144 VAL A O   
993  C CB  . VAL A 137 ? 0.32410 0.29106 0.31399 -0.00220 0.03326  0.05506  144 VAL A CB  
994  C CG1 . VAL A 137 ? 0.32530 0.30311 0.30269 0.00044  0.03750  0.05686  144 VAL A CG1 
995  C CG2 . VAL A 137 ? 0.27865 0.25156 0.28194 -0.00806 0.03275  0.04659  144 VAL A CG2 
996  N N   . ALA A 138 ? 0.33782 0.29076 0.33832 0.00478  0.01765  0.04098  145 ALA A N   
997  C CA  . ALA A 138 ? 0.33484 0.27541 0.34336 0.00346  0.01427  0.03758  145 ALA A CA  
998  C C   . ALA A 138 ? 0.32587 0.26164 0.33005 0.01262  0.00893  0.03448  145 ALA A C   
999  O O   . ALA A 138 ? 0.37807 0.32669 0.37894 0.01794  0.00684  0.02969  145 ALA A O   
1000 C CB  . ALA A 138 ? 0.27846 0.22643 0.29595 -0.00166 0.01342  0.02882  145 ALA A CB  
1001 N N   . GLU A 139 ? 0.32082 0.23827 0.32665 0.01431  0.00685  0.03666  146 GLU A N   
1002 C CA  . GLU A 139 ? 0.32852 0.24047 0.33192 0.02376  0.00191  0.03210  146 GLU A CA  
1003 C C   . GLU A 139 ? 0.37171 0.28572 0.38101 0.02314  -0.00095 0.02045  146 GLU A C   
1004 O O   . GLU A 139 ? 0.38003 0.29816 0.38748 0.03127  -0.00374 0.01456  146 GLU A O   
1005 C CB  . GLU A 139 ? 0.41738 0.30649 0.41869 0.02715  0.00120  0.03957  146 GLU A CB  
1006 C CG  . GLU A 139 ? 0.52940 0.40043 0.53957 0.01887  0.00140  0.03863  146 GLU A CG  
1007 C CD  . GLU A 139 ? 0.69907 0.54447 0.70815 0.02132  0.00146  0.04697  146 GLU A CD  
1008 O OE1 . GLU A 139 ? 0.73384 0.56193 0.75166 0.01444  0.00068  0.04496  146 GLU A OE1 
1009 O OE2 . GLU A 139 ? 0.69192 0.53427 0.69173 0.02975  0.00218  0.05587  146 GLU A OE2 
1010 N N   . LYS A 140 ? 0.32129 0.23468 0.33739 0.01425  -0.00015 0.01712  147 LYS A N   
1011 C CA  . LYS A 140 ? 0.31159 0.22751 0.33100 0.01386  -0.00306 0.00656  147 LYS A CA  
1012 C C   . LYS A 140 ? 0.29793 0.22510 0.32293 0.00499  -0.00084 0.00563  147 LYS A C   
1013 O O   . LYS A 140 ? 0.30227 0.22751 0.33178 -0.00205 0.00199  0.01205  147 LYS A O   
1014 C CB  . LYS A 140 ? 0.34321 0.23864 0.36511 0.01407  -0.00716 0.00237  147 LYS A CB  
1015 C CG  . LYS A 140 ? 0.36631 0.26358 0.38866 0.01502  -0.01085 -0.00933 147 LYS A CG  
1016 C CD  . LYS A 140 ? 0.44510 0.31999 0.46819 0.01665  -0.01553 -0.01465 147 LYS A CD  
1017 C CE  . LYS A 140 ? 0.54211 0.40930 0.57375 0.00603  -0.01859 -0.01805 147 LYS A CE  
1018 N NZ  . LYS A 140 ? 0.57882 0.42041 0.61222 0.00667  -0.02304 -0.02228 147 LYS A NZ  
1019 N N   . VAL A 141 ? 0.27267 0.21233 0.29736 0.00603  -0.00131 -0.00128 148 VAL A N   
1020 C CA  . VAL A 141 ? 0.26202 0.21152 0.29181 -0.00078 0.00015  -0.00249 148 VAL A CA  
1021 C C   . VAL A 141 ? 0.34497 0.29358 0.37503 0.00011  -0.00411 -0.01131 148 VAL A C   
1022 O O   . VAL A 141 ? 0.27919 0.22940 0.30326 0.00721  -0.00536 -0.01682 148 VAL A O   
1023 C CB  . VAL A 141 ? 0.25680 0.22283 0.28464 -0.00033 0.00447  -0.00098 148 VAL A CB  
1024 C CG1 . VAL A 141 ? 0.26127 0.23573 0.29437 -0.00595 0.00601  -0.00195 148 VAL A CG1 
1025 C CG2 . VAL A 141 ? 0.25518 0.22296 0.28003 -0.00013 0.00783  0.00638  148 VAL A CG2 
1026 N N   . THR A 142 ? 0.29777 0.24490 0.33477 -0.00664 -0.00639 -0.01269 149 THR A N   
1027 C CA  . THR A 142 ? 0.29184 0.24045 0.32839 -0.00630 -0.01135 -0.02104 149 THR A CA  
1028 C C   . THR A 142 ? 0.30762 0.27127 0.34805 -0.00991 -0.00940 -0.01938 149 THR A C   
1029 O O   . THR A 142 ? 0.31600 0.28344 0.36492 -0.01612 -0.00677 -0.01359 149 THR A O   
1030 C CB  . THR A 142 ? 0.30305 0.23743 0.34602 -0.01117 -0.01753 -0.02516 149 THR A CB  
1031 O OG1 . THR A 142 ? 0.36640 0.28362 0.40703 -0.00825 -0.01835 -0.02477 149 THR A OG1 
1032 C CG2 . THR A 142 ? 0.35223 0.28754 0.39156 -0.00908 -0.02426 -0.03582 149 THR A CG2 
1033 N N   . VAL A 143 ? 0.25917 0.23122 0.29327 -0.00538 -0.01005 -0.02379 150 VAL A N   
1034 C CA  . VAL A 143 ? 0.26727 0.25209 0.30398 -0.00720 -0.00844 -0.02191 150 VAL A CA  
1035 C C   . VAL A 143 ? 0.32235 0.30823 0.35659 -0.00577 -0.01534 -0.02891 150 VAL A C   
1036 O O   . VAL A 143 ? 0.29418 0.27839 0.31772 0.00075  -0.01719 -0.03458 150 VAL A O   
1037 C CB  . VAL A 143 ? 0.27549 0.26961 0.30620 -0.00289 -0.00213 -0.01919 150 VAL A CB  
1038 C CG1 . VAL A 143 ? 0.28552 0.29004 0.31812 -0.00368 -0.00049 -0.01701 150 VAL A CG1 
1039 C CG2 . VAL A 143 ? 0.30108 0.29531 0.33377 -0.00433 0.00321  -0.01372 150 VAL A CG2 
1040 N N   . ILE A 144 ? 0.25576 0.24551 0.29983 -0.01137 -0.01936 -0.02887 151 ILE A N   
1041 C CA  . ILE A 144 ? 0.26569 0.25941 0.30777 -0.00996 -0.02726 -0.03565 151 ILE A CA  
1042 C C   . ILE A 144 ? 0.28663 0.29469 0.32864 -0.00787 -0.02453 -0.03102 151 ILE A C   
1043 O O   . ILE A 144 ? 0.27842 0.29247 0.33056 -0.01189 -0.01989 -0.02423 151 ILE A O   
1044 C CB  . ILE A 144 ? 0.28564 0.27566 0.34137 -0.01785 -0.03486 -0.03931 151 ILE A CB  
1045 C CG1 . ILE A 144 ? 0.40047 0.37395 0.46055 -0.02204 -0.03522 -0.04029 151 ILE A CG1 
1046 C CG2 . ILE A 144 ? 0.38758 0.38053 0.43892 -0.01551 -0.04533 -0.04913 151 ILE A CG2 
1047 C CD1 . ILE A 144 ? 0.42416 0.38510 0.47118 -0.01560 -0.03806 -0.04786 151 ILE A CD1 
1048 N N   . THR A 145 ? 0.25607 0.26907 0.28604 -0.00092 -0.02677 -0.03419 152 THR A N   
1049 C CA  . THR A 145 ? 0.27396 0.29836 0.30275 0.00212  -0.02330 -0.02834 152 THR A CA  
1050 C C   . THR A 145 ? 0.29679 0.32747 0.31625 0.00797  -0.03054 -0.03265 152 THR A C   
1051 O O   . THR A 145 ? 0.28916 0.31537 0.29677 0.01222  -0.03564 -0.04031 152 THR A O   
1052 C CB  . THR A 145 ? 0.28399 0.30834 0.30581 0.00562  -0.01299 -0.02256 152 THR A CB  
1053 O OG1 . THR A 145 ? 0.29484 0.32707 0.31925 0.00675  -0.00843 -0.01573 152 THR A OG1 
1054 C CG2 . THR A 145 ? 0.29528 0.31723 0.30130 0.01293  -0.01192 -0.02628 152 THR A CG2 
1055 N N   . LYS A 146 ? 0.27184 0.31314 0.29634 0.00890  -0.03128 -0.02785 153 LYS A N   
1056 C CA  . LYS A 146 ? 0.28895 0.33836 0.30387 0.01574  -0.03802 -0.02985 153 LYS A CA  
1057 C C   . LYS A 146 ? 0.28439 0.34069 0.29740 0.02053  -0.03093 -0.01982 153 LYS A C   
1058 O O   . LYS A 146 ? 0.27492 0.33602 0.30215 0.01710  -0.02819 -0.01434 153 LYS A O   
1059 C CB  . LYS A 146 ? 0.26749 0.32396 0.29432 0.01175  -0.05014 -0.03570 153 LYS A CB  
1060 C CG  . LYS A 146 ? 0.30944 0.37702 0.32689 0.01943  -0.05919 -0.03797 153 LYS A CG  
1061 C CD  . LYS A 146 ? 0.34851 0.41078 0.34317 0.02669  -0.06390 -0.04625 153 LYS A CD  
1062 C CE  . LYS A 146 ? 0.37152 0.44562 0.35490 0.03491  -0.07416 -0.04889 153 LYS A CE  
1063 N NZ  . LYS A 146 ? 0.32959 0.41090 0.30448 0.04328  -0.06706 -0.03675 153 LYS A NZ  
1064 N N   . HIS A 147 ? 0.29261 0.34871 0.28819 0.02869  -0.02736 -0.01725 154 HIS A N   
1065 C CA  . HIS A 147 ? 0.30703 0.36722 0.29822 0.03435  -0.02074 -0.00734 154 HIS A CA  
1066 C C   . HIS A 147 ? 0.34036 0.40912 0.32052 0.04273  -0.02921 -0.00767 154 HIS A C   
1067 O O   . HIS A 147 ? 0.31679 0.38621 0.28520 0.04595  -0.03720 -0.01578 154 HIS A O   
1068 C CB  . HIS A 147 ? 0.29541 0.34902 0.27559 0.03692  -0.00950 -0.00301 154 HIS A CB  
1069 C CG  . HIS A 147 ? 0.34568 0.39981 0.32316 0.04102  -0.00075 0.00779  154 HIS A CG  
1070 N ND1 . HIS A 147 ? 0.32918 0.38733 0.29313 0.05002  -0.00166 0.01297  154 HIS A ND1 
1071 C CD2 . HIS A 147 ? 0.30903 0.35873 0.29486 0.03752  0.00920  0.01429  154 HIS A CD2 
1072 C CE1 . HIS A 147 ? 0.40073 0.45569 0.36576 0.05169  0.00795  0.02314  154 HIS A CE1 
1073 N NE2 . HIS A 147 ? 0.35245 0.40205 0.33110 0.04385  0.01444  0.02334  154 HIS A NE2 
1074 N N   . ASN A 148 ? 0.33030 0.40558 0.31362 0.04708  -0.02818 0.00065  155 ASN A N   
1075 C CA  . ASN A 148 ? 0.34059 0.42536 0.31266 0.05633  -0.03719 0.00113  155 ASN A CA  
1076 C C   . ASN A 148 ? 0.36176 0.44382 0.30792 0.06478  -0.03652 0.00008  155 ASN A C   
1077 O O   . ASN A 148 ? 0.40429 0.49348 0.33775 0.07147  -0.04718 -0.00489 155 ASN A O   
1078 C CB  . ASN A 148 ? 0.32879 0.41851 0.30526 0.06205  -0.03341 0.01277  155 ASN A CB  
1079 C CG  . ASN A 148 ? 0.37687 0.47563 0.37667 0.05760  -0.03838 0.01238  155 ASN A CG  
1080 O OD1 . ASN A 148 ? 0.40293 0.50859 0.41412 0.05188  -0.04833 0.00351  155 ASN A OD1 
1081 N ND2 . ASN A 148 ? 0.35927 0.45802 0.36729 0.06033  -0.03101 0.02213  155 ASN A ND2 
1082 N N   . ASP A 149 ? 0.38721 0.46038 0.32518 0.06497  -0.02418 0.00447  156 ASP A N   
1083 C CA  . ASP A 149 ? 0.42120 0.49319 0.33504 0.07382  -0.02052 0.00596  156 ASP A CA  
1084 C C   . ASP A 149 ? 0.47072 0.53894 0.37578 0.07284  -0.02311 -0.00580 156 ASP A C   
1085 O O   . ASP A 149 ? 0.45851 0.52583 0.34427 0.08001  -0.01782 -0.00489 156 ASP A O   
1086 C CB  . ASP A 149 ? 0.46931 0.53524 0.38025 0.07502  -0.00450 0.01838  156 ASP A CB  
1087 C CG  . ASP A 149 ? 0.47272 0.53951 0.38733 0.07875  -0.00082 0.03086  156 ASP A CG  
1088 O OD1 . ASP A 149 ? 0.43924 0.51366 0.35352 0.08371  -0.01067 0.03113  156 ASP A OD1 
1089 O OD2 . ASP A 149 ? 0.54839 0.60803 0.46743 0.07668  0.01176  0.04009  156 ASP A OD2 
1090 N N   . ASP A 150 ? 0.41059 0.47598 0.32924 0.06465  -0.03002 -0.01614 157 ASP A N   
1091 C CA  . ASP A 150 ? 0.35950 0.41848 0.27137 0.06395  -0.03147 -0.02692 157 ASP A CA  
1092 C C   . ASP A 150 ? 0.47817 0.53561 0.40102 0.05762  -0.04490 -0.03922 157 ASP A C   
1093 O O   . ASP A 150 ? 0.38313 0.44639 0.32024 0.05315  -0.05228 -0.03892 157 ASP A O   
1094 C CB  . ASP A 150 ? 0.39034 0.44220 0.30975 0.05908  -0.01900 -0.02338 157 ASP A CB  
1095 C CG  . ASP A 150 ? 0.42333 0.47090 0.32926 0.06367  -0.01623 -0.03046 157 ASP A CG  
1096 O OD1 . ASP A 150 ? 0.45605 0.50380 0.34694 0.06981  -0.02445 -0.03991 157 ASP A OD1 
1097 O OD2 . ASP A 150 ? 0.42500 0.46978 0.33533 0.06175  -0.00581 -0.02695 157 ASP A OD2 
1098 N N   . GLU A 151 ? 0.40373 0.45314 0.32098 0.05730  -0.04763 -0.05000 158 GLU A N   
1099 C CA  . GLU A 151 ? 0.40610 0.45015 0.33331 0.05079  -0.05927 -0.06225 158 GLU A CA  
1100 C C   . GLU A 151 ? 0.32714 0.36365 0.27638 0.03986  -0.05462 -0.05973 158 GLU A C   
1101 O O   . GLU A 151 ? 0.37440 0.40957 0.32834 0.03834  -0.04312 -0.05069 158 GLU A O   
1102 C CB  . GLU A 151 ? 0.45935 0.49551 0.36891 0.05672  -0.06357 -0.07507 158 GLU A CB  
1103 C CG  . GLU A 151 ? 0.58099 0.62417 0.46563 0.06826  -0.06959 -0.07987 158 GLU A CG  
1104 C CD  . GLU A 151 ? 0.70845 0.76383 0.59574 0.06852  -0.08100 -0.07932 158 GLU A CD  
1105 O OE1 . GLU A 151 ? 0.76390 0.82043 0.67147 0.05920  -0.09056 -0.08395 158 GLU A OE1 
1106 O OE2 . GLU A 151 ? 0.85854 0.92316 0.72765 0.07857  -0.08042 -0.07389 158 GLU A OE2 
1107 N N   . GLN A 152 ? 0.34325 0.37448 0.30555 0.03219  -0.06378 -0.06806 159 GLN A N   
1108 C CA  . GLN A 152 ? 0.32866 0.35199 0.31020 0.02227  -0.05973 -0.06534 159 GLN A CA  
1109 C C   . GLN A 152 ? 0.32822 0.33808 0.30285 0.02416  -0.05463 -0.06909 159 GLN A C   
1110 O O   . GLN A 152 ? 0.36896 0.37106 0.33239 0.02834  -0.06059 -0.08005 159 GLN A O   
1111 C CB  . GLN A 152 ? 0.38412 0.40626 0.38335 0.01292  -0.07043 -0.07172 159 GLN A CB  
1112 C CG  . GLN A 152 ? 0.39317 0.41014 0.41332 0.00254  -0.06506 -0.06561 159 GLN A CG  
1113 C CD  . GLN A 152 ? 0.39303 0.41508 0.43455 -0.00723 -0.07336 -0.06788 159 GLN A CD  
1114 O OE1 . GLN A 152 ? 0.41402 0.45117 0.46187 -0.00692 -0.07741 -0.06558 159 GLN A OE1 
1115 N NE2 . GLN A 152 ? 0.38186 0.39176 0.43573 -0.01579 -0.07547 -0.07163 159 GLN A NE2 
1116 N N   . TYR A 153 ? 0.30609 0.31369 0.28706 0.02186  -0.04405 -0.06055 160 TYR A N   
1117 C CA  . TYR A 153 ? 0.31151 0.30921 0.28777 0.02455  -0.03839 -0.06217 160 TYR A CA  
1118 C C   . TYR A 153 ? 0.32952 0.31939 0.32166 0.01644  -0.03565 -0.05811 160 TYR A C   
1119 O O   . TYR A 153 ? 0.30909 0.30388 0.31426 0.00969  -0.03342 -0.05080 160 TYR A O   
1120 C CB  . TYR A 153 ? 0.31732 0.32199 0.28391 0.03123  -0.02764 -0.05541 160 TYR A CB  
1121 C CG  . TYR A 153 ? 0.37939 0.38850 0.32637 0.04129  -0.02826 -0.05979 160 TYR A CG  
1122 C CD1 . TYR A 153 ? 0.40293 0.42274 0.34220 0.04496  -0.02752 -0.05471 160 TYR A CD1 
1123 C CD2 . TYR A 153 ? 0.40157 0.40381 0.33662 0.04814  -0.02926 -0.06872 160 TYR A CD2 
1124 C CE1 . TYR A 153 ? 0.47685 0.50067 0.39556 0.05509  -0.02766 -0.05798 160 TYR A CE1 
1125 C CE2 . TYR A 153 ? 0.46638 0.47313 0.38159 0.05824  -0.02894 -0.07288 160 TYR A CE2 
1126 C CZ  . TYR A 153 ? 0.49796 0.51563 0.40448 0.06153  -0.02814 -0.06729 160 TYR A CZ  
1127 O OH  . TYR A 153 ? 0.59011 0.61204 0.47459 0.07241  -0.02732 -0.07086 160 TYR A OH  
1128 N N   . ALA A 154 ? 0.30762 0.28529 0.29741 0.01833  -0.03518 -0.06242 161 ALA A N   
1129 C CA  . ALA A 154 ? 0.29405 0.26334 0.29500 0.01307  -0.03170 -0.05754 161 ALA A CA  
1130 C C   . ALA A 154 ? 0.32670 0.29630 0.32160 0.01951  -0.02378 -0.05444 161 ALA A C   
1131 O O   . ALA A 154 ? 0.33495 0.30048 0.31930 0.02753  -0.02405 -0.06085 161 ALA A O   
1132 C CB  . ALA A 154 ? 0.34687 0.29958 0.35298 0.00930  -0.03914 -0.06471 161 ALA A CB  
1133 N N   . TRP A 155 ? 0.28068 0.25610 0.28261 0.01631  -0.01704 -0.04535 162 TRP A N   
1134 C CA  . TRP A 155 ? 0.31532 0.29269 0.31581 0.02052  -0.01056 -0.04187 162 TRP A CA  
1135 C C   . TRP A 155 ? 0.31384 0.28004 0.32112 0.01759  -0.01151 -0.03941 162 TRP A C   
1136 O O   . TRP A 155 ? 0.31642 0.27811 0.33195 0.01012  -0.01336 -0.03601 162 TRP A O   
1137 C CB  . TRP A 155 ? 0.28163 0.27247 0.28517 0.01851  -0.00347 -0.03431 162 TRP A CB  
1138 C CG  . TRP A 155 ? 0.29768 0.29447 0.30302 0.02072  0.00284  -0.03038 162 TRP A CG  
1139 C CD1 . TRP A 155 ? 0.27986 0.28682 0.28188 0.02541  0.00835  -0.03001 162 TRP A CD1 
1140 C CD2 . TRP A 155 ? 0.26700 0.26191 0.27870 0.01778  0.00411  -0.02599 162 TRP A CD2 
1141 N NE1 . TRP A 155 ? 0.26270 0.27485 0.27055 0.02497  0.01201  -0.02670 162 TRP A NE1 
1142 C CE2 . TRP A 155 ? 0.29429 0.29926 0.30675 0.02084  0.00910  -0.02432 162 TRP A CE2 
1143 C CE3 . TRP A 155 ? 0.28147 0.26791 0.29819 0.01288  0.00177  -0.02285 162 TRP A CE3 
1144 C CZ2 . TRP A 155 ? 0.27388 0.28095 0.29076 0.01991  0.01022  -0.02092 162 TRP A CZ2 
1145 C CZ3 . TRP A 155 ? 0.28171 0.26948 0.30088 0.01249  0.00411  -0.01823 162 TRP A CZ3 
1146 C CH2 . TRP A 155 ? 0.27984 0.27808 0.29854 0.01635  0.00757  -0.01786 162 TRP A CH2 
1147 N N   . GLU A 156 ? 0.26144 0.22369 0.26557 0.02399  -0.00986 -0.04035 163 GLU A N   
1148 C CA  . GLU A 156 ? 0.28207 0.23313 0.29131 0.02218  -0.01068 -0.03639 163 GLU A CA  
1149 C C   . GLU A 156 ? 0.30843 0.26420 0.31611 0.02914  -0.00691 -0.03370 163 GLU A C   
1150 O O   . GLU A 156 ? 0.30109 0.26212 0.30376 0.03719  -0.00549 -0.03829 163 GLU A O   
1151 C CB  . GLU A 156 ? 0.39121 0.32321 0.39958 0.02298  -0.01687 -0.04256 163 GLU A CB  
1152 C CG  . GLU A 156 ? 0.41139 0.32826 0.42543 0.02008  -0.01764 -0.03709 163 GLU A CG  
1153 C CD  . GLU A 156 ? 0.57327 0.47099 0.59033 0.01625  -0.02397 -0.04293 163 GLU A CD  
1154 O OE1 . GLU A 156 ? 0.53275 0.41935 0.54340 0.02358  -0.02730 -0.05142 163 GLU A OE1 
1155 O OE2 . GLU A 156 ? 0.50071 0.39521 0.52707 0.00615  -0.02560 -0.03999 163 GLU A OE2 
1156 N N   . SER A 157 ? 0.28447 0.23911 0.29638 0.02666  -0.00546 -0.02637 164 SER A N   
1157 C CA  . SER A 157 ? 0.27990 0.23923 0.29096 0.03382  -0.00372 -0.02408 164 SER A CA  
1158 C C   . SER A 157 ? 0.30549 0.25552 0.31798 0.03272  -0.00465 -0.01679 164 SER A C   
1159 O O   . SER A 157 ? 0.28463 0.23449 0.29966 0.02514  -0.00332 -0.01097 164 SER A O   
1160 C CB  . SER A 157 ? 0.26680 0.24639 0.27993 0.03377  0.00084  -0.02237 164 SER A CB  
1161 O OG  . SER A 157 ? 0.29027 0.27619 0.30440 0.04124  0.00114  -0.02136 164 SER A OG  
1162 N N   . SER A 158 ? 0.32230 0.26572 0.33258 0.04142  -0.00632 -0.01658 165 SER A N   
1163 C CA  . SER A 158 ? 0.32083 0.25853 0.33032 0.04348  -0.00683 -0.00841 165 SER A CA  
1164 C C   . SER A 158 ? 0.31791 0.27354 0.32750 0.04974  -0.00595 -0.00660 165 SER A C   
1165 O O   . SER A 158 ? 0.38460 0.33692 0.39202 0.05646  -0.00783 -0.00169 165 SER A O   
1166 C CB  . SER A 158 ? 0.38841 0.30399 0.39575 0.04950  -0.01000 -0.00836 165 SER A CB  
1167 O OG  . SER A 158 ? 0.39191 0.29026 0.40126 0.04197  -0.01152 -0.01003 165 SER A OG  
1168 N N   . ALA A 159 ? 0.29672 0.27117 0.30942 0.04767  -0.00342 -0.01031 166 ALA A N   
1169 C CA  . ALA A 159 ? 0.36202 0.35653 0.37822 0.05175  -0.00269 -0.01049 166 ALA A CA  
1170 C C   . ALA A 159 ? 0.33922 0.33440 0.35645 0.06377  -0.00441 -0.01381 166 ALA A C   
1171 O O   . ALA A 159 ? 0.38656 0.37280 0.40196 0.06741  -0.00410 -0.01907 166 ALA A O   
1172 C CB  . ALA A 159 ? 0.35669 0.35583 0.37130 0.04925  -0.00373 -0.00403 166 ALA A CB  
1173 N N   . GLY A 160 ? 0.37698 0.38359 0.39713 0.07098  -0.00643 -0.01173 167 GLY A N   
1174 C CA  . GLY A 160 ? 0.38050 0.38938 0.40321 0.08324  -0.00731 -0.01543 167 GLY A CA  
1175 C C   . GLY A 160 ? 0.36344 0.38837 0.39218 0.08487  -0.00290 -0.02238 167 GLY A C   
1176 O O   . GLY A 160 ? 0.38107 0.40682 0.41109 0.09540  -0.00224 -0.02652 167 GLY A O   
1177 N N   . GLY A 161 ? 0.28426 0.32139 0.31641 0.07534  0.00087  -0.02336 168 GLY A N   
1178 C CA  . GLY A 161 ? 0.28126 0.33605 0.32004 0.07614  0.00625  -0.02775 168 GLY A CA  
1179 C C   . GLY A 161 ? 0.31508 0.36237 0.34756 0.07465  0.01026  -0.03189 168 GLY A C   
1180 O O   . GLY A 161 ? 0.28979 0.35176 0.32636 0.07542  0.01596  -0.03424 168 GLY A O   
1181 N N   . SER A 162 ? 0.27488 0.30089 0.29786 0.07246  0.00752  -0.03272 169 SER A N   
1182 C CA  . SER A 162 ? 0.27504 0.29499 0.29085 0.07271  0.00976  -0.03793 169 SER A CA  
1183 C C   . SER A 162 ? 0.28596 0.29098 0.29647 0.06335  0.00683  -0.03675 169 SER A C   
1184 O O   . SER A 162 ? 0.29785 0.29337 0.30946 0.05856  0.00338  -0.03234 169 SER A O   
1185 C CB  . SER A 162 ? 0.31902 0.32838 0.32869 0.08435  0.00847  -0.04444 169 SER A CB  
1186 O OG  . SER A 162 ? 0.32899 0.31642 0.33520 0.08571  0.00243  -0.04406 169 SER A OG  
1187 N N   . PHE A 163 ? 0.29654 0.30116 0.30143 0.06138  0.00853  -0.04035 170 PHE A N   
1188 C CA  . PHE A 163 ? 0.29201 0.28473 0.29269 0.05379  0.00514  -0.04074 170 PHE A CA  
1189 C C   . PHE A 163 ? 0.33200 0.31837 0.32286 0.05862  0.00369  -0.04865 170 PHE A C   
1190 O O   . PHE A 163 ? 0.30684 0.30108 0.29319 0.06692  0.00746  -0.05259 170 PHE A O   
1191 C CB  . PHE A 163 ? 0.31235 0.31519 0.31691 0.04440  0.00820  -0.03546 170 PHE A CB  
1192 C CG  . PHE A 163 ? 0.28287 0.30061 0.28627 0.04564  0.01439  -0.03556 170 PHE A CG  
1193 C CD1 . PHE A 163 ? 0.32121 0.35449 0.33193 0.04642  0.01985  -0.03274 170 PHE A CD1 
1194 C CD2 . PHE A 163 ? 0.28104 0.29763 0.27668 0.04551  0.01468  -0.03783 170 PHE A CD2 
1195 C CE1 . PHE A 163 ? 0.31425 0.36037 0.32519 0.04655  0.02683  -0.03154 170 PHE A CE1 
1196 C CE2 . PHE A 163 ? 0.29387 0.32284 0.28732 0.04684  0.02125  -0.03605 170 PHE A CE2 
1197 C CZ  . PHE A 163 ? 0.32632 0.36941 0.32791 0.04692  0.02796  -0.03244 170 PHE A CZ  
1198 N N   . THR A 164 ? 0.27925 0.25186 0.26693 0.05365  -0.00200 -0.05144 171 THR A N   
1199 C CA  . THR A 164 ? 0.29413 0.26035 0.27153 0.05746  -0.00533 -0.06024 171 THR A CA  
1200 C C   . THR A 164 ? 0.28753 0.25880 0.26339 0.05028  -0.00674 -0.05900 171 THR A C   
1201 O O   . THR A 164 ? 0.27962 0.25274 0.26373 0.04136  -0.00701 -0.05254 171 THR A O   
1202 C CB  . THR A 164 ? 0.34383 0.28818 0.31906 0.05909  -0.01267 -0.06738 171 THR A CB  
1203 O OG1 . THR A 164 ? 0.37839 0.31360 0.36233 0.04843  -0.01666 -0.06273 171 THR A OG1 
1204 C CG2 . THR A 164 ? 0.35009 0.28754 0.32575 0.06852  -0.01145 -0.06875 171 THR A CG2 
1205 N N   . VAL A 165 ? 0.31354 0.28784 0.27797 0.05535  -0.00740 -0.06509 172 VAL A N   
1206 C CA  . VAL A 165 ? 0.31271 0.29083 0.27378 0.05058  -0.01058 -0.06501 172 VAL A CA  
1207 C C   . VAL A 165 ? 0.37910 0.34745 0.32857 0.05506  -0.01846 -0.07669 172 VAL A C   
1208 O O   . VAL A 165 ? 0.37852 0.34508 0.31647 0.06497  -0.01722 -0.08378 172 VAL A O   
1209 C CB  . VAL A 165 ? 0.30954 0.30447 0.26628 0.05244  -0.00293 -0.05887 172 VAL A CB  
1210 C CG1 . VAL A 165 ? 0.34726 0.34530 0.29864 0.04973  -0.00725 -0.05888 172 VAL A CG1 
1211 C CG2 . VAL A 165 ? 0.29904 0.30250 0.26798 0.04701  0.00390  -0.04901 172 VAL A CG2 
1212 N N   . ARG A 166 ? 0.32326 0.28654 0.27598 0.04804  -0.02665 -0.07933 173 ARG A N   
1213 C CA  . ARG A 166 ? 0.35899 0.31419 0.30128 0.05118  -0.03585 -0.09171 173 ARG A CA  
1214 C C   . ARG A 166 ? 0.38357 0.34578 0.32845 0.04469  -0.04233 -0.09108 173 ARG A C   
1215 O O   . ARG A 166 ? 0.36292 0.33098 0.32129 0.03634  -0.04067 -0.08199 173 ARG A O   
1216 C CB  . ARG A 166 ? 0.46391 0.39849 0.41132 0.04922  -0.04251 -0.09990 173 ARG A CB  
1217 C CG  . ARG A 166 ? 0.48839 0.41587 0.45373 0.03628  -0.04728 -0.09581 173 ARG A CG  
1218 C CD  . ARG A 166 ? 0.53731 0.44334 0.50985 0.03445  -0.04960 -0.09877 173 ARG A CD  
1219 N NE  . ARG A 166 ? 0.55871 0.46441 0.53442 0.03795  -0.04111 -0.08992 173 ARG A NE  
1220 C CZ  . ARG A 166 ? 0.66357 0.55262 0.64043 0.04182  -0.04098 -0.09161 173 ARG A CZ  
1221 N NH1 . ARG A 166 ? 0.60888 0.47717 0.58536 0.04142  -0.04823 -0.10144 173 ARG A NH1 
1222 N NH2 . ARG A 166 ? 0.61587 0.50885 0.59470 0.04642  -0.03383 -0.08343 173 ARG A NH2 
1223 N N   . THR A 167 ? 0.41148 0.37387 0.34284 0.04952  -0.04993 -0.10123 174 THR A N   
1224 C CA  . THR A 167 ? 0.38993 0.35819 0.32503 0.04373  -0.05921 -0.10311 174 THR A CA  
1225 C C   . THR A 167 ? 0.45649 0.41375 0.41117 0.03195  -0.06644 -0.10551 174 THR A C   
1226 O O   . THR A 167 ? 0.49831 0.43869 0.45580 0.03089  -0.06896 -0.11227 174 THR A O   
1227 C CB  . THR A 167 ? 0.52841 0.49797 0.44357 0.05205  -0.06754 -0.11549 174 THR A CB  
1228 O OG1 . THR A 167 ? 0.52807 0.51029 0.42579 0.06226  -0.05928 -0.10998 174 THR A OG1 
1229 C CG2 . THR A 167 ? 0.58769 0.56302 0.50887 0.04584  -0.07979 -0.11958 174 THR A CG2 
1230 N N   . ASP A 168 ? 0.43563 0.40225 0.40503 0.02322  -0.06861 -0.09884 175 ASP A N   
1231 C CA  . ASP A 168 ? 0.48951 0.44841 0.47993 0.01117  -0.07327 -0.09869 175 ASP A CA  
1232 C C   . ASP A 168 ? 0.55147 0.51186 0.54565 0.00698  -0.08715 -0.10972 175 ASP A C   
1233 O O   . ASP A 168 ? 0.57184 0.54838 0.56473 0.00802  -0.09128 -0.10860 175 ASP A O   
1234 C CB  . ASP A 168 ? 0.43269 0.40170 0.43931 0.00395  -0.06608 -0.08457 175 ASP A CB  
1235 C CG  . ASP A 168 ? 0.59066 0.55264 0.61903 -0.00833 -0.06904 -0.08304 175 ASP A CG  
1236 O OD1 . ASP A 168 ? 0.65583 0.60005 0.68722 -0.01096 -0.07050 -0.08736 175 ASP A OD1 
1237 O OD2 . ASP A 168 ? 0.52183 0.49590 0.56468 -0.01502 -0.06971 -0.07736 175 ASP A OD2 
1238 N N   . THR A 169 ? 0.64093 0.58423 0.64016 0.00250  -0.09466 -0.12047 176 THR A N   
1239 C CA  . THR A 169 ? 0.73407 0.67665 0.73998 -0.00340 -0.10915 -0.13302 176 THR A CA  
1240 C C   . THR A 169 ? 0.71004 0.65336 0.74503 -0.01865 -0.11175 -0.12830 176 THR A C   
1241 O O   . THR A 169 ? 0.71718 0.65992 0.76344 -0.02614 -0.12395 -0.13854 176 THR A O   
1242 C CB  . THR A 169 ? 0.72572 0.64733 0.72024 0.00043  -0.11625 -0.14934 176 THR A CB  
1243 O OG1 . THR A 169 ? 0.78798 0.68965 0.78883 -0.00172 -0.10879 -0.14536 176 THR A OG1 
1244 C CG2 . THR A 169 ? 0.72880 0.65414 0.69368 0.01616  -0.11547 -0.15616 176 THR A CG2 
1245 N N   . GLY A 170 ? 0.67854 0.62376 0.72602 -0.02342 -0.10047 -0.11339 177 GLY A N   
1246 C CA  . GLY A 170 ? 0.70082 0.64844 0.77513 -0.03703 -0.10022 -0.10679 177 GLY A CA  
1247 C C   . GLY A 170 ? 0.61213 0.58395 0.69882 -0.04078 -0.10462 -0.10382 177 GLY A C   
1248 O O   . GLY A 170 ? 0.62229 0.60728 0.69729 -0.03369 -0.11140 -0.10936 177 GLY A O   
1249 N N   . GLU A 171 ? 0.61029 0.58828 0.72089 -0.05139 -0.10033 -0.09439 178 GLU A N   
1250 C CA  . GLU A 171 ? 0.51965 0.52118 0.64742 -0.05582 -0.10320 -0.09020 178 GLU A CA  
1251 C C   . GLU A 171 ? 0.48911 0.50753 0.60134 -0.04425 -0.09945 -0.08449 178 GLU A C   
1252 O O   . GLU A 171 ? 0.43936 0.45598 0.54218 -0.03906 -0.08728 -0.07441 178 GLU A O   
1253 C CB  . GLU A 171 ? 0.55406 0.55801 0.70569 -0.06637 -0.09373 -0.07777 178 GLU A CB  
1254 C CG  . GLU A 171 ? 0.52818 0.54836 0.70953 -0.07784 -0.09985 -0.07810 178 GLU A CG  
1255 C CD  . GLU A 171 ? 0.53718 0.55342 0.72737 -0.08447 -0.11596 -0.09388 178 GLU A CD  
1256 O OE1 . GLU A 171 ? 0.56880 0.60144 0.75692 -0.08055 -0.12762 -0.10220 178 GLU A OE1 
1257 O OE2 . GLU A 171 ? 0.58198 0.57763 0.77967 -0.09289 -0.11737 -0.09837 178 GLU A OE2 
1258 N N   . PRO A 172 ? 0.45851 0.49276 0.56749 -0.03987 -0.10976 -0.09054 179 PRO A N   
1259 C CA  . PRO A 172 ? 0.46051 0.50958 0.55544 -0.02876 -0.10571 -0.08349 179 PRO A CA  
1260 C C   . PRO A 172 ? 0.48257 0.54286 0.59257 -0.03133 -0.09462 -0.06904 179 PRO A C   
1261 O O   . PRO A 172 ? 0.51199 0.58033 0.64702 -0.04089 -0.09516 -0.06618 179 PRO A O   
1262 C CB  . PRO A 172 ? 0.50122 0.56615 0.59585 -0.02578 -0.12086 -0.09249 179 PRO A CB  
1263 C CG  . PRO A 172 ? 0.52217 0.57450 0.61692 -0.03104 -0.13296 -0.10832 179 PRO A CG  
1264 C CD  . PRO A 172 ? 0.53988 0.57575 0.65270 -0.04311 -0.12645 -0.10579 179 PRO A CD  
1265 N N   . MET A 173 ? 0.41562 0.47670 0.51068 -0.02271 -0.08422 -0.06024 180 MET A N   
1266 C CA  . MET A 173 ? 0.38611 0.45448 0.49187 -0.02396 -0.07274 -0.04766 180 MET A CA  
1267 C C   . MET A 173 ? 0.46216 0.54906 0.56982 -0.01735 -0.07340 -0.04213 180 MET A C   
1268 O O   . MET A 173 ? 0.53004 0.62538 0.65185 -0.01934 -0.06603 -0.03348 180 MET A O   
1269 C CB  . MET A 173 ? 0.42294 0.47907 0.51370 -0.01979 -0.06016 -0.04137 180 MET A CB  
1270 C CG  . MET A 173 ? 0.55500 0.59592 0.65006 -0.02661 -0.05519 -0.04102 180 MET A CG  
1271 S SD  . MET A 173 ? 0.56929 0.60191 0.64552 -0.01926 -0.04289 -0.03470 180 MET A SD  
1272 C CE  . MET A 173 ? 0.44857 0.49588 0.53188 -0.01733 -0.03504 -0.02431 180 MET A CE  
1273 N N   . GLY A 174 ? 0.42995 0.52252 0.52206 -0.00835 -0.08093 -0.04612 181 GLY A N   
1274 C CA  . GLY A 174 ? 0.35728 0.46592 0.45033 -0.00080 -0.08098 -0.03926 181 GLY A CA  
1275 C C   . GLY A 174 ? 0.35017 0.45271 0.42627 0.00753  -0.06862 -0.02989 181 GLY A C   
1276 O O   . GLY A 174 ? 0.33082 0.43352 0.38699 0.01723  -0.07015 -0.02944 181 GLY A O   
1277 N N   . ARG A 175 ? 0.25846 0.35533 0.34199 0.00362  -0.05628 -0.02257 182 ARG A N   
1278 C CA  . ARG A 175 ? 0.26012 0.34913 0.33030 0.00910  -0.04419 -0.01493 182 ARG A CA  
1279 C C   . ARG A 175 ? 0.26161 0.34352 0.34176 0.00202  -0.03377 -0.01094 182 ARG A C   
1280 O O   . ARG A 175 ? 0.28627 0.37503 0.38510 -0.00362 -0.03293 -0.00898 182 ARG A O   
1281 C CB  . ARG A 175 ? 0.26781 0.36627 0.33645 0.01770  -0.04174 -0.00692 182 ARG A CB  
1282 C CG  . ARG A 175 ? 0.28598 0.37450 0.34058 0.02289  -0.02963 0.00043  182 ARG A CG  
1283 C CD  . ARG A 175 ? 0.24137 0.33562 0.30034 0.02923  -0.02448 0.00956  182 ARG A CD  
1284 N NE  . ARG A 175 ? 0.24870 0.34940 0.32878 0.02439  -0.02153 0.01156  182 ARG A NE  
1285 C CZ  . ARG A 175 ? 0.27048 0.38628 0.36609 0.02582  -0.02749 0.01232  182 ARG A CZ  
1286 N NH1 . ARG A 175 ? 0.25142 0.37821 0.34412 0.03221  -0.03828 0.01106  182 ARG A NH1 
1287 N NH2 . ARG A 175 ? 0.23440 0.35586 0.34888 0.02140  -0.02249 0.01446  182 ARG A NH2 
1288 N N   . GLY A 176 ? 0.28848 0.33267 0.28629 0.02898  -0.00698 0.01995  183 GLY A N   
1289 C CA  . GLY A 176 ? 0.27755 0.31446 0.28474 0.02998  -0.00122 0.01691  183 GLY A CA  
1290 C C   . GLY A 176 ? 0.31592 0.34271 0.31967 0.02415  0.00085  0.00789  183 GLY A C   
1291 O O   . GLY A 176 ? 0.29227 0.31482 0.28600 0.02167  0.00084  0.00427  183 GLY A O   
1292 N N   . THR A 177 ? 0.26375 0.28760 0.27536 0.02315  0.00302  0.00484  184 THR A N   
1293 C CA  . THR A 177 ? 0.25970 0.27501 0.27002 0.01938  0.00472  -0.00213 184 THR A CA  
1294 C C   . THR A 177 ? 0.29924 0.31670 0.31625 0.01618  0.00251  -0.00418 184 THR A C   
1295 O O   . THR A 177 ? 0.27809 0.30129 0.30222 0.01814  0.00359  -0.00045 184 THR A O   
1296 C CB  . THR A 177 ? 0.30395 0.31014 0.31449 0.02113  0.01067  -0.00243 184 THR A CB  
1297 O OG1 . THR A 177 ? 0.33037 0.33417 0.33443 0.02226  0.01322  0.00046  184 THR A OG1 
1298 C CG2 . THR A 177 ? 0.33137 0.33343 0.34387 0.01825  0.01153  -0.00805 184 THR A CG2 
1299 N N   . LYS A 178 ? 0.25601 0.26784 0.26971 0.01208  0.00031  -0.00958 185 LYS A N   
1300 C CA  . LYS A 178 ? 0.26806 0.27800 0.28603 0.00825  -0.00154 -0.01082 185 LYS A CA  
1301 C C   . LYS A 178 ? 0.26282 0.26262 0.27922 0.00982  0.00116  -0.01473 185 LYS A C   
1302 O O   . LYS A 178 ? 0.30919 0.30311 0.31988 0.01115  0.00163  -0.01876 185 LYS A O   
1303 C CB  . LYS A 178 ? 0.33367 0.34283 0.34754 0.00151  -0.00796 -0.01293 185 LYS A CB  
1304 C CG  . LYS A 178 ? 0.44040 0.44405 0.45654 -0.00431 -0.01032 -0.01347 185 LYS A CG  
1305 C CD  . LYS A 178 ? 0.50602 0.50697 0.51645 -0.01359 -0.01791 -0.01557 185 LYS A CD  
1306 C CE  . LYS A 178 ? 0.54080 0.55761 0.55238 -0.01546 -0.02231 -0.01246 185 LYS A CE  
1307 N NZ  . LYS A 178 ? 0.68032 0.69809 0.68861 -0.02770 -0.03156 -0.01344 185 LYS A NZ  
1308 N N   . VAL A 179 ? 0.26340 0.26257 0.28429 0.01048  0.00307  -0.01322 186 VAL A N   
1309 C CA  . VAL A 179 ? 0.26210 0.25489 0.28272 0.01176  0.00383  -0.01550 186 VAL A CA  
1310 C C   . VAL A 179 ? 0.27469 0.26235 0.29501 0.00884  0.00106  -0.01477 186 VAL A C   
1311 O O   . VAL A 179 ? 0.28057 0.27193 0.30321 0.00655  0.00136  -0.01116 186 VAL A O   
1312 C CB  . VAL A 179 ? 0.26188 0.25592 0.28436 0.01326  0.00652  -0.01437 186 VAL A CB  
1313 C CG1 . VAL A 179 ? 0.28375 0.27538 0.30726 0.01378  0.00520  -0.01550 186 VAL A CG1 
1314 C CG2 . VAL A 179 ? 0.28526 0.28061 0.30718 0.01454  0.00930  -0.01424 186 VAL A CG2 
1315 N N   . ILE A 180 ? 0.27020 0.24828 0.28669 0.00948  -0.00079 -0.01767 187 ILE A N   
1316 C CA  . ILE A 180 ? 0.27112 0.23889 0.28502 0.00636  -0.00366 -0.01645 187 ILE A CA  
1317 C C   . ILE A 180 ? 0.29090 0.25480 0.30569 0.01143  -0.00316 -0.01520 187 ILE A C   
1318 O O   . ILE A 180 ? 0.28534 0.24696 0.30010 0.01761  -0.00220 -0.01789 187 ILE A O   
1319 C CB  . ILE A 180 ? 0.30591 0.26006 0.31166 0.00419  -0.00651 -0.02083 187 ILE A CB  
1320 C CG1 . ILE A 180 ? 0.30346 0.26486 0.30772 -0.00135 -0.00873 -0.02192 187 ILE A CG1 
1321 C CG2 . ILE A 180 ? 0.31487 0.25406 0.31691 -0.00058 -0.00959 -0.01854 187 ILE A CG2 
1322 C CD1 . ILE A 180 ? 0.39383 0.34051 0.38551 -0.00420 -0.01226 -0.02826 187 ILE A CD1 
1323 N N   . LEU A 181 ? 0.27128 0.23680 0.28691 0.00944  -0.00361 -0.01049 188 LEU A N   
1324 C CA  . LEU A 181 ? 0.27468 0.23810 0.28990 0.01364  -0.00484 -0.00799 188 LEU A CA  
1325 C C   . LEU A 181 ? 0.31228 0.26012 0.32243 0.01330  -0.00735 -0.00499 188 LEU A C   
1326 O O   . LEU A 181 ? 0.32761 0.27142 0.33487 0.00675  -0.00784 -0.00077 188 LEU A O   
1327 C CB  . LEU A 181 ? 0.26971 0.24126 0.28406 0.01175  -0.00410 -0.00483 188 LEU A CB  
1328 C CG  . LEU A 181 ? 0.27411 0.25490 0.29056 0.01135  -0.00122 -0.00776 188 LEU A CG  
1329 C CD1 . LEU A 181 ? 0.30644 0.28953 0.31716 0.00996  0.00008  -0.00568 188 LEU A CD1 
1330 C CD2 . LEU A 181 ? 0.30182 0.28685 0.32244 0.01448  -0.00181 -0.01078 188 LEU A CD2 
1331 N N   . HIS A 182 ? 0.31262 0.25148 0.32180 0.02074  -0.00833 -0.00633 189 HIS A N   
1332 C CA  . HIS A 182 ? 0.35892 0.27830 0.36158 0.02263  -0.01063 -0.00271 189 HIS A CA  
1333 C C   . HIS A 182 ? 0.34844 0.27308 0.35200 0.02634  -0.01288 0.00450  189 HIS A C   
1334 O O   . HIS A 182 ? 0.34901 0.28252 0.35795 0.03477  -0.01390 0.00501  189 HIS A O   
1335 C CB  . HIS A 182 ? 0.34717 0.25242 0.34659 0.03151  -0.00966 -0.00767 189 HIS A CB  
1336 C CG  . HIS A 182 ? 0.39611 0.29715 0.39124 0.02804  -0.00789 -0.01562 189 HIS A CG  
1337 N ND1 . HIS A 182 ? 0.47046 0.34965 0.45450 0.02155  -0.00989 -0.01868 189 HIS A ND1 
1338 C CD2 . HIS A 182 ? 0.37012 0.28542 0.36887 0.02919  -0.00502 -0.02063 189 HIS A CD2 
1339 C CE1 . HIS A 182 ? 0.42799 0.30938 0.40830 0.01924  -0.00898 -0.02577 189 HIS A CE1 
1340 N NE2 . HIS A 182 ? 0.44345 0.34657 0.43243 0.02449  -0.00555 -0.02656 189 HIS A NE2 
1341 N N   . LEU A 183 ? 0.33325 0.25584 0.33185 0.01947  -0.01370 0.01064  190 LEU A N   
1342 C CA  . LEU A 183 ? 0.33351 0.26526 0.33008 0.02112  -0.01576 0.01665  190 LEU A CA  
1343 C C   . LEU A 183 ? 0.37499 0.29653 0.36856 0.02963  -0.01981 0.02300  190 LEU A C   
1344 O O   . LEU A 183 ? 0.38943 0.28991 0.37839 0.03183  -0.02013 0.02524  190 LEU A O   
1345 C CB  . LEU A 183 ? 0.34039 0.27309 0.33035 0.01217  -0.01377 0.02187  190 LEU A CB  
1346 C CG  . LEU A 183 ? 0.34649 0.29299 0.34022 0.00655  -0.00930 0.01728  190 LEU A CG  
1347 C CD1 . LEU A 183 ? 0.35789 0.30844 0.34581 0.00018  -0.00571 0.02355  190 LEU A CD1 
1348 C CD2 . LEU A 183 ? 0.34742 0.30688 0.34390 0.01047  -0.00938 0.01204  190 LEU A CD2 
1349 N N   . LYS A 184 ? 0.35346 0.28922 0.34898 0.03448  -0.02354 0.02612  191 LYS A N   
1350 C CA  . LYS A 184 ? 0.38274 0.31283 0.37526 0.04292  -0.02853 0.03481  191 LYS A CA  
1351 C C   . LYS A 184 ? 0.44417 0.35744 0.42310 0.03776  -0.02887 0.04374  191 LYS A C   
1352 O O   . LYS A 184 ? 0.42938 0.34460 0.40217 0.02750  -0.02575 0.04416  191 LYS A O   
1353 C CB  . LYS A 184 ? 0.40749 0.36007 0.40392 0.04608  -0.03432 0.03729  191 LYS A CB  
1354 C CG  . LYS A 184 ? 0.44145 0.41391 0.45317 0.04975  -0.03451 0.03081  191 LYS A CG  
1355 C CD  . LYS A 184 ? 0.45219 0.44674 0.46520 0.04551  -0.04073 0.03160  191 LYS A CD  
1356 C CE  . LYS A 184 ? 0.48052 0.49535 0.50912 0.04506  -0.04050 0.02571  191 LYS A CE  
1357 N NZ  . LYS A 184 ? 0.51210 0.54787 0.54244 0.03930  -0.04870 0.02692  191 LYS A NZ  
1358 N N   . GLU A 185 ? 0.44257 0.33984 0.41699 0.04588  -0.03211 0.05203  192 GLU A N   
1359 C CA  . GLU A 185 ? 0.49270 0.36951 0.45348 0.04074  -0.03209 0.06211  192 GLU A CA  
1360 C C   . GLU A 185 ? 0.51894 0.40895 0.46993 0.03382  -0.03304 0.06863  192 GLU A C   
1361 O O   . GLU A 185 ? 0.50934 0.38944 0.45039 0.02459  -0.02969 0.07484  192 GLU A O   
1362 C CB  . GLU A 185 ? 0.60598 0.46255 0.56282 0.05339  -0.03600 0.07091  192 GLU A CB  
1363 C CG  . GLU A 185 ? 0.70696 0.53267 0.64961 0.04797  -0.03512 0.08062  192 GLU A CG  
1364 C CD  . GLU A 185 ? 0.92125 0.72387 0.85900 0.06319  -0.03892 0.08969  192 GLU A CD  
1365 O OE1 . GLU A 185 ? 0.96362 0.78354 0.90749 0.07682  -0.04392 0.09371  192 GLU A OE1 
1366 O OE2 . GLU A 185 ? 0.98373 0.75085 0.91164 0.06144  -0.03726 0.09313  192 GLU A OE2 
1367 N N   . ASP A 186 ? 0.45695 0.36906 0.40928 0.03733  -0.03741 0.06748  193 ASP A N   
1368 C CA  . ASP A 186 ? 0.47579 0.39709 0.41374 0.03173  -0.03864 0.07279  193 ASP A CA  
1369 C C   . ASP A 186 ? 0.44302 0.37896 0.38051 0.02328  -0.03347 0.06296  193 ASP A C   
1370 O O   . ASP A 186 ? 0.42207 0.36684 0.34625 0.02001  -0.03417 0.06405  193 ASP A O   
1371 C CB  . ASP A 186 ? 0.45808 0.39188 0.39265 0.03953  -0.04838 0.07861  193 ASP A CB  
1372 C CG  . ASP A 186 ? 0.56738 0.52131 0.51829 0.04427  -0.05275 0.07010  193 ASP A CG  
1373 O OD1 . ASP A 186 ? 0.63685 0.59011 0.60236 0.04587  -0.04834 0.06186  193 ASP A OD1 
1374 O OD2 . ASP A 186 ? 0.59948 0.57074 0.54827 0.04594  -0.06121 0.07255  193 ASP A OD2 
1375 N N   . GLN A 187 ? 0.38726 0.32397 0.33672 0.02035  -0.02813 0.05362  194 GLN A N   
1376 C CA  . GLN A 187 ? 0.36583 0.31462 0.31623 0.01473  -0.02301 0.04474  194 GLN A CA  
1377 C C   . GLN A 187 ? 0.36226 0.30667 0.31476 0.00766  -0.01481 0.04446  194 GLN A C   
1378 O O   . GLN A 187 ? 0.34664 0.29923 0.30578 0.00529  -0.01029 0.03684  194 GLN A O   
1379 C CB  . GLN A 187 ? 0.39599 0.35474 0.35985 0.01781  -0.02483 0.03479  194 GLN A CB  
1380 C CG  . GLN A 187 ? 0.36125 0.33101 0.32671 0.02284  -0.03342 0.03546  194 GLN A CG  
1381 C CD  . GLN A 187 ? 0.42824 0.40467 0.37747 0.01894  -0.03695 0.03660  194 GLN A CD  
1382 O OE1 . GLN A 187 ? 0.42733 0.40355 0.36698 0.01346  -0.03161 0.03151  194 GLN A OE1 
1383 N NE2 . GLN A 187 ? 0.43625 0.41860 0.38121 0.02258  -0.04613 0.04317  194 GLN A NE2 
1384 N N   . THR A 188 ? 0.39176 0.32432 0.33917 0.00371  -0.01316 0.05372  195 THR A N   
1385 C CA  . THR A 188 ? 0.44096 0.37289 0.39369 -0.00498 -0.00661 0.05447  195 THR A CA  
1386 C C   . THR A 188 ? 0.41775 0.36452 0.36496 -0.00952 0.00125  0.05629  195 THR A C   
1387 O O   . THR A 188 ? 0.41661 0.36945 0.37152 -0.01643 0.00702  0.05782  195 THR A O   
1388 C CB  . THR A 188 ? 0.48278 0.39515 0.43272 -0.01027 -0.00764 0.06407  195 THR A CB  
1389 O OG1 . THR A 188 ? 0.53171 0.43907 0.46692 -0.01020 -0.00809 0.07567  195 THR A OG1 
1390 C CG2 . THR A 188 ? 0.47546 0.36977 0.42978 -0.00422 -0.01349 0.06075  195 THR A CG2 
1391 N N   . GLU A 189 ? 0.42010 0.37364 0.35388 -0.00569 0.00171  0.05606  196 GLU A N   
1392 C CA  . GLU A 189 ? 0.39933 0.36571 0.32622 -0.00724 0.01090  0.05525  196 GLU A CA  
1393 C C   . GLU A 189 ? 0.38250 0.35921 0.32275 -0.00625 0.01556  0.04584  196 GLU A C   
1394 O O   . GLU A 189 ? 0.36460 0.35288 0.30604 -0.00732 0.02475  0.04703  196 GLU A O   
1395 C CB  . GLU A 189 ? 0.43638 0.40428 0.34270 -0.00288 0.00961  0.05333  196 GLU A CB  
1396 C CG  . GLU A 189 ? 0.40198 0.37060 0.31002 0.00159  0.00302  0.04185  196 GLU A CG  
1397 C CD  . GLU A 189 ? 0.50604 0.47397 0.39240 0.00330  -0.00174 0.04052  196 GLU A CD  
1398 O OE1 . GLU A 189 ? 0.50220 0.46694 0.38421 0.00439  -0.01096 0.04660  196 GLU A OE1 
1399 O OE2 . GLU A 189 ? 0.47626 0.44591 0.34918 0.00398  0.00305  0.03326  196 GLU A OE2 
1400 N N   . TYR A 190 ? 0.35626 0.33033 0.30663 -0.00328 0.00999  0.03751  197 TYR A N   
1401 C CA  . TYR A 190 ? 0.32876 0.31083 0.29044 -0.00174 0.01345  0.02951  197 TYR A CA  
1402 C C   . TYR A 190 ? 0.34766 0.33455 0.32476 -0.00698 0.01563  0.03228  197 TYR A C   
1403 O O   . TYR A 190 ? 0.34473 0.33893 0.33212 -0.00559 0.01721  0.02699  197 TYR A O   
1404 C CB  . TYR A 190 ? 0.32015 0.29832 0.28561 0.00227  0.00697  0.02095  197 TYR A CB  
1405 C CG  . TYR A 190 ? 0.32809 0.30447 0.27884 0.00480  0.00386  0.01819  197 TYR A CG  
1406 C CD1 . TYR A 190 ? 0.36820 0.34635 0.30634 0.00618  0.00949  0.01415  197 TYR A CD1 
1407 C CD2 . TYR A 190 ? 0.35175 0.32453 0.29986 0.00598  -0.00490 0.02002  197 TYR A CD2 
1408 C CE1 . TYR A 190 ? 0.41147 0.38548 0.33232 0.00655  0.00552  0.01075  197 TYR A CE1 
1409 C CE2 . TYR A 190 ? 0.39078 0.36432 0.32514 0.00637  -0.00957 0.01816  197 TYR A CE2 
1410 C CZ  . TYR A 190 ? 0.38967 0.36265 0.30913 0.00558  -0.00474 0.01290  197 TYR A CZ  
1411 O OH  . TYR A 190 ? 0.40351 0.37466 0.30553 0.00424  -0.01042 0.00979  197 TYR A OH  
1412 N N   . LEU A 191 ? 0.34374 0.32606 0.32165 -0.01383 0.01505  0.04093  198 LEU A N   
1413 C CA  . LEU A 191 ? 0.34931 0.33822 0.34019 -0.02214 0.01684  0.04482  198 LEU A CA  
1414 C C   . LEU A 191 ? 0.38288 0.38834 0.37503 -0.02681 0.02571  0.05376  198 LEU A C   
1415 O O   . LEU A 191 ? 0.40434 0.42148 0.41010 -0.03496 0.02729  0.05820  198 LEU A O   
1416 C CB  . LEU A 191 ? 0.34430 0.31445 0.33541 -0.02917 0.01020  0.04857  198 LEU A CB  
1417 C CG  . LEU A 191 ? 0.35583 0.31043 0.34643 -0.02319 0.00299  0.04037  198 LEU A CG  
1418 C CD1 . LEU A 191 ? 0.42009 0.35086 0.40647 -0.02768 -0.00221 0.04423  198 LEU A CD1 
1419 C CD2 . LEU A 191 ? 0.37031 0.33389 0.37138 -0.02183 0.00253  0.03154  198 LEU A CD2 
1420 N N   . GLU A 192 ? 0.35647 0.36418 0.33441 -0.02271 0.03128  0.05721  199 GLU A N   
1421 C CA  . GLU A 192 ? 0.37949 0.40427 0.35740 -0.02618 0.04169  0.06662  199 GLU A CA  
1422 C C   . GLU A 192 ? 0.37785 0.42275 0.36192 -0.01807 0.05068  0.06191  199 GLU A C   
1423 O O   . GLU A 192 ? 0.34399 0.38362 0.31938 -0.00812 0.05093  0.05218  199 GLU A O   
1424 C CB  . GLU A 192 ? 0.45208 0.46985 0.40861 -0.02524 0.04482  0.07348  199 GLU A CB  
1425 C CG  . GLU A 192 ? 0.48398 0.47854 0.43086 -0.02878 0.03507  0.07788  199 GLU A CG  
1426 C CD  . GLU A 192 ? 0.69528 0.68360 0.61822 -0.02553 0.03640  0.08386  199 GLU A CD  
1427 O OE1 . GLU A 192 ? 0.84698 0.84733 0.75809 -0.02110 0.04535  0.08330  199 GLU A OE1 
1428 O OE2 . GLU A 192 ? 0.76464 0.73524 0.67897 -0.02653 0.02853  0.08930  199 GLU A OE2 
1429 N N   . GLU A 193 ? 0.32956 0.34487 0.37400 -0.04815 0.00217  0.05631  200 GLU A N   
1430 C CA  . GLU A 193 ? 0.31885 0.35618 0.36473 -0.04552 0.00678  0.04954  200 GLU A CA  
1431 C C   . GLU A 193 ? 0.32775 0.37779 0.35612 -0.03651 0.01316  0.05116  200 GLU A C   
1432 O O   . GLU A 193 ? 0.31143 0.36687 0.33232 -0.02876 0.01337  0.04062  200 GLU A O   
1433 C CB  . GLU A 193 ? 0.38850 0.44174 0.45264 -0.05635 0.01038  0.05640  200 GLU A CB  
1434 C CG  . GLU A 193 ? 0.42262 0.50319 0.48787 -0.05164 0.01724  0.05333  200 GLU A CG  
1435 C CD  . GLU A 193 ? 0.56218 0.66319 0.65011 -0.06207 0.01898  0.05809  200 GLU A CD  
1436 O OE1 . GLU A 193 ? 0.51237 0.61339 0.61290 -0.07447 0.01975  0.07105  200 GLU A OE1 
1437 O OE2 . GLU A 193 ? 0.59368 0.71222 0.68739 -0.05795 0.01974  0.05037  200 GLU A OE2 
1438 N N   . ARG A 194 ? 0.37193 0.42533 0.39217 -0.03702 0.01792  0.06423  201 ARG A N   
1439 C CA  . ARG A 194 ? 0.31363 0.38013 0.31477 -0.02762 0.02363  0.06437  201 ARG A CA  
1440 C C   . ARG A 194 ? 0.32350 0.37801 0.30864 -0.01910 0.01700  0.05375  201 ARG A C   
1441 O O   . ARG A 194 ? 0.32984 0.39083 0.30107 -0.01133 0.01849  0.04603  201 ARG A O   
1442 C CB  . ARG A 194 ? 0.43030 0.50534 0.42456 -0.02918 0.03050  0.08180  201 ARG A CB  
1443 C CG  . ARG A 194 ? 0.40794 0.46455 0.39962 -0.03214 0.02569  0.09173  201 ARG A CG  
1444 C CD  . ARG A 194 ? 0.47527 0.54418 0.45519 -0.03085 0.03383  0.10947  201 ARG A CD  
1445 N NE  . ARG A 194 ? 0.59664 0.64878 0.56857 -0.03014 0.02932  0.12004  201 ARG A NE  
1446 C CZ  . ARG A 194 ? 0.52614 0.58473 0.48931 -0.03018 0.03547  0.13901  201 ARG A CZ  
1447 N NH1 . ARG A 194 ? 0.55901 0.64192 0.52132 -0.03143 0.04702  0.14962  201 ARG A NH1 
1448 N NH2 . ARG A 194 ? 0.64789 0.69011 0.60280 -0.02771 0.03046  0.14860  201 ARG A NH2 
1449 N N   . ARG A 195 ? 0.32085 0.35807 0.30827 -0.02033 0.00937  0.05340  202 ARG A N   
1450 C CA  . ARG A 195 ? 0.33148 0.36131 0.30850 -0.01379 0.00251  0.04476  202 ARG A CA  
1451 C C   . ARG A 195 ? 0.33219 0.36158 0.31472 -0.01211 -0.00000 0.03087  202 ARG A C   
1452 O O   . ARG A 195 ? 0.30501 0.33546 0.27751 -0.00743 -0.00227 0.02310  202 ARG A O   
1453 C CB  . ARG A 195 ? 0.31105 0.32636 0.29151 -0.01401 -0.00389 0.04975  202 ARG A CB  
1454 C CG  . ARG A 195 ? 0.33844 0.35111 0.31168 -0.00775 -0.01132 0.04347  202 ARG A CG  
1455 C CD  . ARG A 195 ? 0.39698 0.41801 0.35115 -0.00331 -0.01221 0.04559  202 ARG A CD  
1456 N NE  . ARG A 195 ? 0.34471 0.36513 0.29534 0.00065  -0.02097 0.04178  202 ARG A NE  
1457 C CZ  . ARG A 195 ? 0.37400 0.39986 0.31616 0.00220  -0.02558 0.03268  202 ARG A CZ  
1458 N NH1 . ARG A 195 ? 0.37858 0.40750 0.31152 0.00222  -0.02223 0.02537  202 ARG A NH1 
1459 N NH2 . ARG A 195 ? 0.39095 0.41901 0.33505 0.00382  -0.03420 0.03075  202 ARG A NH2 
1460 N N   . ILE A 196 ? 0.29162 0.31849 0.28948 -0.01612 -0.00036 0.02783  203 ILE A N   
1461 C CA  . ILE A 196 ? 0.26273 0.29065 0.26470 -0.01358 -0.00203 0.01654  203 ILE A CA  
1462 C C   . ILE A 196 ? 0.28915 0.32808 0.28444 -0.00994 0.00310  0.01250  203 ILE A C   
1463 O O   . ILE A 196 ? 0.30024 0.33655 0.28851 -0.00540 0.00127  0.00490  203 ILE A O   
1464 C CB  . ILE A 196 ? 0.29206 0.31690 0.30922 -0.01747 -0.00392 0.01375  203 ILE A CB  
1465 C CG1 . ILE A 196 ? 0.27614 0.28603 0.29677 -0.01796 -0.00956 0.01544  203 ILE A CG1 
1466 C CG2 . ILE A 196 ? 0.27254 0.30131 0.29202 -0.01349 -0.00472 0.00370  203 ILE A CG2 
1467 C CD1 . ILE A 196 ? 0.33022 0.33295 0.36336 -0.02328 -0.01222 0.01392  203 ILE A CD1 
1468 N N   . LYS A 197 ? 0.30263 0.35397 0.30044 -0.01156 0.00972  0.01819  204 LYS A N   
1469 C CA  . LYS A 197 ? 0.28309 0.34625 0.27338 -0.00508 0.01557  0.01457  204 LYS A CA  
1470 C C   . LYS A 197 ? 0.31057 0.36781 0.27973 0.00208  0.01446  0.00998  204 LYS A C   
1471 O O   . LYS A 197 ? 0.33691 0.39159 0.29806 0.00856  0.01453  0.00122  204 LYS A O   
1472 C CB  . LYS A 197 ? 0.34347 0.42554 0.33874 -0.00687 0.02402  0.02424  204 LYS A CB  
1473 C CG  . LYS A 197 ? 0.43146 0.52469 0.44861 -0.01402 0.02510  0.02719  204 LYS A CG  
1474 C CD  . LYS A 197 ? 0.46340 0.58181 0.48551 -0.01432 0.03492  0.03729  204 LYS A CD  
1475 C CE  . LYS A 197 ? 0.55644 0.68184 0.59984 -0.02819 0.03489  0.04860  204 LYS A CE  
1476 N NZ  . LYS A 197 ? 0.59453 0.75069 0.65289 -0.03105 0.04326  0.05771  204 LYS A NZ  
1477 N N   . GLU A 198 ? 0.26496 0.31959 0.22399 0.00131  0.01305  0.01610  205 GLU A N   
1478 C CA  . GLU A 198 ? 0.29602 0.34576 0.23358 0.00743  0.00994  0.01110  205 GLU A CA  
1479 C C   . GLU A 198 ? 0.32653 0.36265 0.26351 0.00729  0.00136  0.00048  205 GLU A C   
1480 O O   . GLU A 198 ? 0.32142 0.35144 0.24447 0.01213  -0.00108 -0.00859 205 GLU A O   
1481 C CB  . GLU A 198 ? 0.30408 0.35432 0.23307 0.00617  0.00813  0.02079  205 GLU A CB  
1482 C CG  . GLU A 198 ? 0.34862 0.39400 0.25601 0.01140  0.00163  0.01482  205 GLU A CG  
1483 C CD  . GLU A 198 ? 0.40332 0.45067 0.30262 0.01115  -0.00124 0.02540  205 GLU A CD  
1484 O OE1 . GLU A 198 ? 0.42116 0.46351 0.33472 0.00605  -0.00454 0.03225  205 GLU A OE1 
1485 O OE2 . GLU A 198 ? 0.40218 0.45531 0.27951 0.01746  -0.00067 0.02641  205 GLU A OE2 
1486 N N   . ILE A 199 ? 0.28262 0.31345 0.23424 0.00188  -0.00343 0.00190  206 ILE A N   
1487 C CA  . ILE A 199 ? 0.28642 0.30863 0.24038 0.00079  -0.01069 -0.00513 206 ILE A CA  
1488 C C   . ILE A 199 ? 0.34345 0.36240 0.30085 0.00277  -0.00870 -0.01243 206 ILE A C   
1489 O O   . ILE A 199 ? 0.32959 0.33989 0.28134 0.00327  -0.01309 -0.01898 206 ILE A O   
1490 C CB  . ILE A 199 ? 0.28791 0.30883 0.25610 -0.00288 -0.01474 -0.00085 206 ILE A CB  
1491 C CG1 . ILE A 199 ? 0.34591 0.36804 0.30889 -0.00296 -0.01747 0.00704  206 ILE A CG1 
1492 C CG2 . ILE A 199 ? 0.32692 0.34446 0.30044 -0.00413 -0.02056 -0.00592 206 ILE A CG2 
1493 C CD1 . ILE A 199 ? 0.37190 0.39120 0.34811 -0.00401 -0.01933 0.01268  206 ILE A CD1 
1494 N N   . VAL A 200 ? 0.29410 0.31953 0.26152 0.00345  -0.00289 -0.01082 207 VAL A N   
1495 C CA  . VAL A 200 ? 0.27124 0.29497 0.24166 0.00697  -0.00103 -0.01638 207 VAL A CA  
1496 C C   . VAL A 200 ? 0.32423 0.34394 0.27853 0.01406  0.00128  -0.02199 207 VAL A C   
1497 O O   . VAL A 200 ? 0.33892 0.34692 0.28838 0.01692  -0.00115 -0.02821 207 VAL A O   
1498 C CB  . VAL A 200 ? 0.29590 0.33087 0.28025 0.00652  0.00343  -0.01347 207 VAL A CB  
1499 C CG1 . VAL A 200 ? 0.29827 0.33485 0.28352 0.01270  0.00605  -0.01803 207 VAL A CG1 
1500 C CG2 . VAL A 200 ? 0.26567 0.29937 0.26296 0.00126  -0.00043 -0.01125 207 VAL A CG2 
1501 N N   . LYS A 201 ? 0.29814 0.32625 0.24267 0.01765  0.00603  -0.01956 208 LYS A N   
1502 C CA  . LYS A 201 ? 0.33364 0.35836 0.25970 0.02736  0.00884  -0.02609 208 LYS A CA  
1503 C C   . LYS A 201 ? 0.37453 0.38103 0.28389 0.02730  0.00035  -0.03409 208 LYS A C   
1504 O O   . LYS A 201 ? 0.44318 0.43585 0.33982 0.03376  -0.00125 -0.04323 208 LYS A O   
1505 C CB  . LYS A 201 ? 0.39764 0.44008 0.31704 0.03212  0.01718  -0.02003 208 LYS A CB  
1506 C CG  . LYS A 201 ? 0.44857 0.49180 0.34804 0.04595  0.02243  -0.02687 208 LYS A CG  
1507 C CD  . LYS A 201 ? 0.57088 0.63570 0.46325 0.05088  0.03165  -0.01877 208 LYS A CD  
1508 C CE  . LYS A 201 ? 0.58360 0.64657 0.44901 0.06680  0.03548  -0.02746 208 LYS A CE  
1509 N NZ  . LYS A 201 ? 0.72860 0.81086 0.58040 0.07170  0.04298  -0.01932 208 LYS A NZ  
1510 N N   . LYS A 202 ? 0.38422 0.38985 0.29395 0.02009  -0.00607 -0.03092 209 LYS A N   
1511 C CA  . LYS A 202 ? 0.37337 0.36540 0.26940 0.01823  -0.01605 -0.03821 209 LYS A CA  
1512 C C   . LYS A 202 ? 0.38619 0.36318 0.29089 0.01278  -0.02287 -0.04340 209 LYS A C   
1513 O O   . LYS A 202 ? 0.40480 0.36504 0.29672 0.01324  -0.02960 -0.05270 209 LYS A O   
1514 C CB  . LYS A 202 ? 0.38121 0.38074 0.27857 0.01258  -0.02126 -0.03158 209 LYS A CB  
1515 C CG  . LYS A 202 ? 0.45862 0.44875 0.34294 0.00989  -0.03328 -0.03884 209 LYS A CG  
1516 C CD  . LYS A 202 ? 0.54779 0.54899 0.43295 0.00667  -0.03814 -0.03087 209 LYS A CD  
1517 C CE  . LYS A 202 ? 0.63746 0.63377 0.50889 0.00428  -0.05140 -0.03819 209 LYS A CE  
1518 N NZ  . LYS A 202 ? 0.67884 0.68849 0.54699 0.00446  -0.05564 -0.02959 209 LYS A NZ  
1519 N N   . HIS A 203 ? 0.37353 0.35572 0.29925 0.00728  -0.02172 -0.03720 210 HIS A N   
1520 C CA  . HIS A 203 ? 0.40762 0.38133 0.34439 0.00042  -0.02782 -0.03789 210 HIS A CA  
1521 C C   . HIS A 203 ? 0.43544 0.40528 0.38182 0.00265  -0.02296 -0.03705 210 HIS A C   
1522 O O   . HIS A 203 ? 0.39345 0.35360 0.34586 -0.00213 -0.02713 -0.03720 210 HIS A O   
1523 C CB  . HIS A 203 ? 0.37942 0.36520 0.33194 -0.00639 -0.03105 -0.03028 210 HIS A CB  
1524 C CG  . HIS A 203 ? 0.43535 0.42514 0.38078 -0.00915 -0.03816 -0.02986 210 HIS A CG  
1525 N ND1 . HIS A 203 ? 0.46913 0.45032 0.40549 -0.01336 -0.04798 -0.03618 210 HIS A ND1 
1526 C CD2 . HIS A 203 ? 0.43788 0.43884 0.38322 -0.00802 -0.03769 -0.02366 210 HIS A CD2 
1527 C CE1 . HIS A 203 ? 0.50071 0.49062 0.43147 -0.01409 -0.05347 -0.03409 210 HIS A CE1 
1528 N NE2 . HIS A 203 ? 0.45061 0.45207 0.38641 -0.01031 -0.04682 -0.02573 210 HIS A NE2 
1529 N N   . SER A 204 ? 0.37068 0.34980 0.32007 0.00908  -0.01469 -0.03484 211 SER A N   
1530 C CA  . SER A 204 ? 0.34446 0.32451 0.30387 0.01189  -0.01071 -0.03284 211 SER A CA  
1531 C C   . SER A 204 ? 0.35530 0.33616 0.30748 0.02231  -0.00432 -0.03583 211 SER A C   
1532 O O   . SER A 204 ? 0.38849 0.37769 0.34980 0.02608  -0.00019 -0.03304 211 SER A O   
1533 C CB  . SER A 204 ? 0.35529 0.35086 0.33062 0.00891  -0.00863 -0.02649 211 SER A CB  
1534 O OG  . SER A 204 ? 0.36419 0.36080 0.34602 0.00198  -0.01379 -0.02349 211 SER A OG  
1535 N N   . GLN A 205 ? 0.38243 0.35627 0.31767 0.02842  -0.00367 -0.04175 212 GLN A N   
1536 C CA  . GLN A 205 ? 0.42049 0.40238 0.35043 0.04025  0.00409  -0.04317 212 GLN A CA  
1537 C C   . GLN A 205 ? 0.45985 0.42974 0.38890 0.04842  0.00524  -0.04568 212 GLN A C   
1538 O O   . GLN A 205 ? 0.44267 0.42412 0.37250 0.05899  0.01184  -0.04505 212 GLN A O   
1539 C CB  . GLN A 205 ? 0.49794 0.47717 0.40720 0.04786  0.00576  -0.04905 212 GLN A CB  
1540 C CG  . GLN A 205 ? 0.50224 0.45373 0.39332 0.04903  -0.00200 -0.05902 212 GLN A CG  
1541 C CD  . GLN A 205 ? 0.67533 0.62485 0.54274 0.05662  -0.00184 -0.06608 212 GLN A CD  
1542 O OE1 . GLN A 205 ? 0.63299 0.59272 0.49065 0.06994  0.00658  -0.06748 212 GLN A OE1 
1543 N NE2 . GLN A 205 ? 0.63964 0.57815 0.49721 0.04914  -0.01130 -0.07051 212 GLN A NE2 
1544 N N   . PHE A 206 ? 0.39241 0.34061 0.32070 0.04399  -0.00091 -0.04723 213 PHE A N   
1545 C CA  . PHE A 206 ? 0.44197 0.37465 0.36796 0.05195  -0.00006 -0.04797 213 PHE A CA  
1546 C C   . PHE A 206 ? 0.45210 0.39005 0.39451 0.04746  0.00001  -0.03946 213 PHE A C   
1547 O O   . PHE A 206 ? 0.46081 0.38480 0.40145 0.05349  0.00041  -0.03780 213 PHE A O   
1548 C CB  . PHE A 206 ? 0.44947 0.34863 0.35977 0.05152  -0.00700 -0.05568 213 PHE A CB  
1549 C CG  . PHE A 206 ? 0.49644 0.38808 0.38561 0.05860  -0.00783 -0.06617 213 PHE A CG  
1550 C CD1 . PHE A 206 ? 0.53044 0.43176 0.40941 0.07513  0.00027  -0.06946 213 PHE A CD1 
1551 C CD2 . PHE A 206 ? 0.53046 0.40931 0.41000 0.04958  -0.01659 -0.07231 213 PHE A CD2 
1552 C CE1 . PHE A 206 ? 0.58781 0.48438 0.44476 0.08384  0.00062  -0.07894 213 PHE A CE1 
1553 C CE2 . PHE A 206 ? 0.61611 0.48875 0.47272 0.05764  -0.01776 -0.08270 213 PHE A CE2 
1554 C CZ  . PHE A 206 ? 0.57216 0.45363 0.41660 0.07534  -0.00850 -0.08591 213 PHE A CZ  
1555 N N   . ILE A 207 ? 0.36390 0.32094 0.32042 0.03875  -0.00013 -0.03394 214 ILE A N   
1556 C CA  . ILE A 207 ? 0.35025 0.31584 0.31968 0.03692  0.00061  -0.02673 214 ILE A CA  
1557 C C   . ILE A 207 ? 0.37513 0.34903 0.34546 0.04906  0.00535  -0.02509 214 ILE A C   
1558 O O   . ILE A 207 ? 0.36818 0.35742 0.33861 0.05561  0.00908  -0.02735 214 ILE A O   
1559 C CB  . ILE A 207 ? 0.33930 0.32437 0.32033 0.02921  0.00005  -0.02380 214 ILE A CB  
1560 C CG1 . ILE A 207 ? 0.31023 0.28880 0.29201 0.01871  -0.00509 -0.02362 214 ILE A CG1 
1561 C CG2 . ILE A 207 ? 0.34226 0.33909 0.33350 0.03032  0.00119  -0.01828 214 ILE A CG2 
1562 C CD1 . ILE A 207 ? 0.36974 0.33896 0.35670 0.01333  -0.00798 -0.01854 214 ILE A CD1 
1563 N N   . GLY A 208 ? 0.34189 0.30743 0.31348 0.05235  0.00529  -0.01990 215 GLY A N   
1564 C CA  . GLY A 208 ? 0.34720 0.31864 0.31793 0.06560  0.00882  -0.01761 215 GLY A CA  
1565 C C   . GLY A 208 ? 0.33655 0.33613 0.31831 0.06792  0.01015  -0.01404 215 GLY A C   
1566 O O   . GLY A 208 ? 0.37459 0.37935 0.35672 0.07752  0.01138  -0.00966 215 GLY A O   
1567 N N   . TYR A 209 ? 0.31466 0.33113 0.30451 0.05963  0.00900  -0.01603 216 TYR A N   
1568 C CA  . TYR A 209 ? 0.28813 0.32895 0.28771 0.06041  0.00827  -0.01520 216 TYR A CA  
1569 C C   . TYR A 209 ? 0.30865 0.36402 0.31454 0.05518  0.00845  -0.01928 216 TYR A C   
1570 O O   . TYR A 209 ? 0.30740 0.35417 0.31033 0.04846  0.00857  -0.02117 216 TYR A O   
1571 C CB  . TYR A 209 ? 0.28562 0.32844 0.28891 0.05432  0.00566  -0.01245 216 TYR A CB  
1572 C CG  . TYR A 209 ? 0.28651 0.31808 0.28501 0.05851  0.00665  -0.00540 216 TYR A CG  
1573 C CD1 . TYR A 209 ? 0.32585 0.36642 0.32289 0.06868  0.00738  -0.00107 216 TYR A CD1 
1574 C CD2 . TYR A 209 ? 0.34301 0.35582 0.33914 0.05173  0.00649  -0.00188 216 TYR A CD2 
1575 C CE1 . TYR A 209 ? 0.37356 0.40348 0.36586 0.07262  0.00909  0.00794  216 TYR A CE1 
1576 C CE2 . TYR A 209 ? 0.29375 0.29611 0.28758 0.05375  0.00778  0.00696  216 TYR A CE2 
1577 C CZ  . TYR A 209 ? 0.31996 0.33017 0.31129 0.06458  0.00967  0.01245  216 TYR A CZ  
1578 O OH  . TYR A 209 ? 0.39871 0.39889 0.38732 0.06707  0.01169  0.02354  216 TYR A OH  
1579 N N   . PRO A 210 ? 0.31159 0.38974 0.32687 0.05710  0.00788  -0.01982 217 PRO A N   
1580 C CA  . PRO A 210 ? 0.26460 0.35677 0.28845 0.04984  0.00818  -0.02142 217 PRO A CA  
1581 C C   . PRO A 210 ? 0.31683 0.40309 0.34382 0.03796  0.00455  -0.02251 217 PRO A C   
1582 O O   . PRO A 210 ? 0.30801 0.39364 0.33684 0.03616  0.00051  -0.02354 217 PRO A O   
1583 C CB  . PRO A 210 ? 0.31365 0.43230 0.34956 0.05317  0.00654  -0.02114 217 PRO A CB  
1584 C CG  . PRO A 210 ? 0.32528 0.44360 0.35812 0.06007  0.00341  -0.02066 217 PRO A CG  
1585 C CD  . PRO A 210 ? 0.34454 0.43781 0.36357 0.06570  0.00642  -0.01816 217 PRO A CD  
1586 N N   . ILE A 211 ? 0.27985 0.36198 0.30584 0.03169  0.00629  -0.02204 218 ILE A N   
1587 C CA  . ILE A 211 ? 0.23878 0.31486 0.26759 0.02171  0.00321  -0.02193 218 ILE A CA  
1588 C C   . ILE A 211 ? 0.26227 0.35283 0.30216 0.01499  0.00339  -0.02002 218 ILE A C   
1589 O O   . ILE A 211 ? 0.30488 0.40352 0.34466 0.01548  0.00836  -0.01685 218 ILE A O   
1590 C CB  . ILE A 211 ? 0.30790 0.36763 0.32653 0.01951  0.00413  -0.02117 218 ILE A CB  
1591 C CG1 . ILE A 211 ? 0.27712 0.32287 0.28790 0.02363  0.00319  -0.02195 218 ILE A CG1 
1592 C CG2 . ILE A 211 ? 0.29612 0.35151 0.31794 0.01109  0.00116  -0.01971 218 ILE A CG2 
1593 C CD1 . ILE A 211 ? 0.27972 0.31023 0.28038 0.02118  0.00258  -0.02243 218 ILE A CD1 
1594 N N   . THR A 212 ? 0.24051 0.33456 0.28975 0.00889  -0.00202 -0.02175 219 THR A N   
1595 C CA  . THR A 212 ? 0.20670 0.31313 0.26951 -0.00018 -0.00339 -0.01930 219 THR A CA  
1596 C C   . THR A 212 ? 0.24330 0.33387 0.30608 -0.00888 -0.00635 -0.01796 219 THR A C   
1597 O O   . THR A 212 ? 0.22893 0.30675 0.28884 -0.00875 -0.01168 -0.02264 219 THR A O   
1598 C CB  . THR A 212 ? 0.23376 0.35469 0.30793 -0.00145 -0.00955 -0.02339 219 THR A CB  
1599 O OG1 . THR A 212 ? 0.26628 0.40277 0.33987 0.00888  -0.00701 -0.02364 219 THR A OG1 
1600 C CG2 . THR A 212 ? 0.22803 0.36232 0.31984 -0.01405 -0.01201 -0.01990 219 THR A CG2 
1601 N N   . LEU A 213 ? 0.25781 0.34993 0.32298 -0.01489 -0.00252 -0.01097 220 LEU A N   
1602 C CA  . LEU A 213 ? 0.25144 0.32835 0.31719 -0.02278 -0.00523 -0.00756 220 LEU A CA  
1603 C C   . LEU A 213 ? 0.22550 0.30780 0.30782 -0.03404 -0.00981 -0.00584 220 LEU A C   
1604 O O   . LEU A 213 ? 0.23760 0.33840 0.33112 -0.03975 -0.00595 0.00106  220 LEU A O   
1605 C CB  . LEU A 213 ? 0.26661 0.34188 0.32433 -0.02296 0.00104  0.00054  220 LEU A CB  
1606 C CG  . LEU A 213 ? 0.28008 0.34204 0.33852 -0.03053 -0.00064 0.00754  220 LEU A CG  
1607 C CD1 . LEU A 213 ? 0.27216 0.31323 0.32629 -0.02879 -0.00747 0.00227  220 LEU A CD1 
1608 C CD2 . LEU A 213 ? 0.35722 0.42101 0.40318 -0.02731 0.00572  0.01478  220 LEU A CD2 
1609 N N   . PHE A 214 ? 0.20735 0.27422 0.29151 -0.03708 -0.01822 -0.01222 221 PHE A N   
1610 C CA  . PHE A 214 ? 0.24975 0.31549 0.34887 -0.04928 -0.02516 -0.01244 221 PHE A CA  
1611 C C   . PHE A 214 ? 0.28054 0.33576 0.38457 -0.05965 -0.02318 -0.00114 221 PHE A C   
1612 O O   . PHE A 214 ? 0.29359 0.33428 0.38614 -0.05559 -0.01995 0.00324  221 PHE A O   
1613 C CB  . PHE A 214 ? 0.24371 0.29082 0.33881 -0.04732 -0.03542 -0.02444 221 PHE A CB  
1614 C CG  . PHE A 214 ? 0.22708 0.28653 0.31944 -0.03924 -0.03924 -0.03481 221 PHE A CG  
1615 C CD1 . PHE A 214 ? 0.22670 0.30313 0.31363 -0.02937 -0.03271 -0.03369 221 PHE A CD1 
1616 C CD2 . PHE A 214 ? 0.23505 0.28702 0.32881 -0.04101 -0.05031 -0.04599 221 PHE A CD2 
1617 C CE1 . PHE A 214 ? 0.22793 0.31515 0.31138 -0.02106 -0.03606 -0.04121 221 PHE A CE1 
1618 C CE2 . PHE A 214 ? 0.25269 0.31776 0.34176 -0.03237 -0.05424 -0.05502 221 PHE A CE2 
1619 C CZ  . PHE A 214 ? 0.25359 0.33714 0.33797 -0.02235 -0.04671 -0.05153 221 PHE A CZ  
1620 N N   . VAL A 215 ? 0.26897 0.33220 0.39102 -0.07364 -0.02568 0.00462  222 VAL A N   
1621 C CA  . VAL A 215 ? 0.32222 0.37285 0.45045 -0.08514 -0.02460 0.01709  222 VAL A CA  
1622 C C   . VAL A 215 ? 0.36736 0.39037 0.50196 -0.09475 -0.03682 0.01134  222 VAL A C   
1623 O O   . VAL A 215 ? 0.33156 0.35088 0.46795 -0.09410 -0.04625 -0.00246 222 VAL A O   
1624 C CB  . VAL A 215 ? 0.41457 0.49353 0.55934 -0.09530 -0.01699 0.03168  222 VAL A CB  
1625 C CG1 . VAL A 215 ? 0.42679 0.52555 0.55896 -0.08275 -0.00441 0.03700  222 VAL A CG1 
1626 C CG2 . VAL A 215 ? 0.33439 0.43652 0.49879 -0.10289 -0.02215 0.02723  222 VAL A CG2 
1627 N N   . GLU A 216 ? 0.38015 0.38205 0.51653 -0.10286 -0.03702 0.02197  223 GLU A N   
1628 C CA  . GLU A 216 ? 0.43952 0.40897 0.58065 -0.11170 -0.04897 0.01691  223 GLU A CA  
1629 C C   . GLU A 216 ? 0.47026 0.44097 0.63422 -0.13342 -0.05127 0.02998  223 GLU A C   
1630 O O   . GLU A 216 ? 0.53129 0.52487 0.70455 -0.14003 -0.04112 0.04717  223 GLU A O   
1631 C CB  . GLU A 216 ? 0.46307 0.39825 0.58702 -0.10217 -0.04994 0.01739  223 GLU A CB  
1632 C CG  . GLU A 216 ? 0.45666 0.39538 0.56109 -0.08238 -0.04601 0.00880  223 GLU A CG  
1633 C CD  . GLU A 216 ? 0.50505 0.41873 0.59532 -0.07268 -0.04536 0.01287  223 GLU A CD  
1634 O OE1 . GLU A 216 ? 0.53691 0.46210 0.61760 -0.06458 -0.03726 0.02023  223 GLU A OE1 
1635 O OE2 . GLU A 216 ? 0.50148 0.38385 0.58973 -0.07237 -0.05378 0.00783  223 GLU A OE2 
1636 N N   . LYS A 217 ? 0.52091 0.46661 0.69350 -0.14441 -0.06507 0.02143  224 LYS A N   
1637 C CA  . LYS A 217 ? 0.59949 0.53844 0.79566 -0.16810 -0.07055 0.03282  224 LYS A CA  
1638 C C   . LYS A 217 ? 0.70660 0.63548 0.90483 -0.17484 -0.06130 0.05659  224 LYS A C   
1639 O O   . LYS A 217 ? 0.68103 0.58502 0.86009 -0.16272 -0.05802 0.05962  224 LYS A O   
1640 C CB  . LYS A 217 ? 0.69035 0.58943 0.88747 -0.17530 -0.08871 0.01700  224 LYS A CB  
1641 C CG  . LYS A 217 ? 0.70214 0.56510 0.91058 -0.19350 -0.09445 0.02976  224 LYS A CG  
1642 C CD  . LYS A 217 ? 0.76620 0.64716 1.00700 -0.22093 -0.09937 0.03974  224 LYS A CD  
1643 C CE  . LYS A 217 ? 0.77668 0.61699 1.01846 -0.23250 -0.10687 0.04047  224 LYS A CE  
1644 N NZ  . LYS A 217 ? 0.78206 0.58323 1.00937 -0.22643 -0.10200 0.05327  224 LYS A NZ  
# 
