data_7HA2
# 
_entry.id   7HA2 
# 
_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   7HA2         pdb_00007ha2 10.2210/pdb7ha2/pdb 
WWPDB D_1001407213 ?            ?                   
# 
_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                        7HA2 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.recvd_initial_deposition_date   2024-07-10 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.pdb_format_compatible           N 
_pdbx_database_status.methods_development_category    ? 
# 
_pdbx_contact_author.id                 1 
_pdbx_contact_author.name_last          Yu 
_pdbx_contact_author.name_first         Feng 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.email              yufeng@sari.ac.cn 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-9502-3277 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Huang, L.' 1  ? 
'Wang, W.'  2  ? 
'Zhu, Z.'   3  ? 
'Li, Q.'    4  ? 
'Li, M.'    5  ? 
'Zhou, H.'  6  ? 
'Xu, Q.'    7  ? 
'Wen, W.'   8  ? 
'Wang, Q.'  9  ? 
'Yu, F.'    10 ? 
# 
_citation.id                        primary 
_citation.title                     
;Novel starting points for fragment-based drug design against human heat-shock protein 90 identified using crystallographic fragment screening.
;
_citation.journal_abbrev            Iucrj 
_citation.journal_volume            12 
_citation.page_first                177 
_citation.page_last                 187 
_citation.year                      2025 
_citation.journal_id_ASTM           ? 
_citation.country                   UK 
_citation.journal_id_ISSN           2052-2525 
_citation.journal_id_CSD            ? 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   39819741 
_citation.pdbx_database_id_DOI      10.1107/S2052252524012247 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.identifier_ORCID 
_citation_author.ordinal 
primary 'Huang, L.' 0009-0001-8431-0182 1  
primary 'Wang, W.'  ?                   2  
primary 'Zhu, Z.'   ?                   3  
primary 'Li, Q.'    ?                   4  
primary 'Li, M.'    ?                   5  
primary 'Zhou, H.'  ?                   6  
primary 'Xu, Q.'    0000-0002-7137-0768 7  
primary 'Wen, W.'   ?                   8  
primary 'Wang, Q.'  ?                   9  
primary 'Yu, F.'    0000-0002-9502-3277 10 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Heat shock protein HSP 90-alpha' 26859.117 1   3.6.4.10 ? ? ? 
2 non-polymer syn 3-amino-4-methylbenzamide         150.178   1   ?        ? ? ? 
3 water       nat water                             18.015    317 ?        ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        
;Heat shock 86 kDa,HSP 86,HSP86,Heat shock protein family C member 1,Lipopolysaccharide-associated protein 2,LAP-2,LPS-associated protein 2,Renal carcinoma antigen NY-REN-38
;
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;MDQPMEEEEVETFAFQAEIAQLMSLIINTFYSNKEIFLRELISNSSDALDKIRYESLTDPSKLDSGKELHINLIPNKQDR
TLTIVDTGIGMTKADLINNLGTIAKSGTKAFMEALQAGADISMIGQFGVGFYSAYLVAEKVTVITKHNDDEQYAWESSAG
GSFTVRTDTGEPMGRGTKVILHLKEDQTEYLEERRIKEIVKKHSQFIGYPITLFVEKERDKEVSDDEAELEHHHHHH
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MDQPMEEEEVETFAFQAEIAQLMSLIINTFYSNKEIFLRELISNSSDALDKIRYESLTDPSKLDSGKELHINLIPNKQDR
TLTIVDTGIGMTKADLINNLGTIAKSGTKAFMEALQAGADISMIGQFGVGFYSAYLVAEKVTVITKHNDDEQYAWESSAG
GSFTVRTDTGEPMGRGTKVILHLKEDQTEYLEERRIKEIVKKHSQFIGYPITLFVEKERDKEVSDDEAELEHHHHHH
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 3-amino-4-methylbenzamide A1AX8 
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 
A1AX8 non-polymer         . 3-amino-4-methylbenzamide ? 'C8 H10 N2 O'    150.178 
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        A1AX8 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1AX8 
_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 A1AX8 1   301 301 A1AX8 DE4 A . 
C 3 HOH   1   401 220 HOH   HOH A . 
C 3 HOH   2   402 222 HOH   HOH A . 
C 3 HOH   3   403 268 HOH   HOH A . 
C 3 HOH   4   404 247 HOH   HOH A . 
C 3 HOH   5   405 153 HOH   HOH A . 
C 3 HOH   6   406 74  HOH   HOH A . 
C 3 HOH   7   407 263 HOH   HOH A . 
C 3 HOH   8   408 118 HOH   HOH A . 
C 3 HOH   9   409 227 HOH   HOH A . 
C 3 HOH   10  410 123 HOH   HOH A . 
C 3 HOH   11  411 196 HOH   HOH A . 
C 3 HOH   12  412 135 HOH   HOH A . 
C 3 HOH   13  413 143 HOH   HOH A . 
C 3 HOH   14  414 16  HOH   HOH A . 
C 3 HOH   15  415 102 HOH   HOH A . 
C 3 HOH   16  416 96  HOH   HOH A . 
C 3 HOH   17  417 137 HOH   HOH A . 
C 3 HOH   18  418 186 HOH   HOH A . 
C 3 HOH   19  419 13  HOH   HOH A . 
C 3 HOH   20  420 94  HOH   HOH A . 
C 3 HOH   21  421 281 HOH   HOH A . 
C 3 HOH   22  422 44  HOH   HOH A . 
C 3 HOH   23  423 50  HOH   HOH A . 
C 3 HOH   24  424 80  HOH   HOH A . 
C 3 HOH   25  425 38  HOH   HOH A . 
C 3 HOH   26  426 126 HOH   HOH A . 
C 3 HOH   27  427 195 HOH   HOH A . 
C 3 HOH   28  428 59  HOH   HOH A . 
C 3 HOH   29  429 163 HOH   HOH A . 
C 3 HOH   30  430 115 HOH   HOH A . 
C 3 HOH   31  431 60  HOH   HOH A . 
C 3 HOH   32  432 23  HOH   HOH A . 
C 3 HOH   33  433 4   HOH   HOH A . 
C 3 HOH   34  434 61  HOH   HOH A . 
C 3 HOH   35  435 12  HOH   HOH A . 
C 3 HOH   36  436 138 HOH   HOH A . 
C 3 HOH   37  437 28  HOH   HOH A . 
C 3 HOH   38  438 90  HOH   HOH A . 
C 3 HOH   39  439 315 HOH   HOH A . 
C 3 HOH   40  440 82  HOH   HOH A . 
C 3 HOH   41  441 73  HOH   HOH A . 
C 3 HOH   42  442 311 HOH   HOH A . 
C 3 HOH   43  443 31  HOH   HOH A . 
C 3 HOH   44  444 43  HOH   HOH A . 
C 3 HOH   45  445 167 HOH   HOH A . 
C 3 HOH   46  446 20  HOH   HOH A . 
C 3 HOH   47  447 234 HOH   HOH A . 
C 3 HOH   48  448 97  HOH   HOH A . 
C 3 HOH   49  449 100 HOH   HOH A . 
C 3 HOH   50  450 180 HOH   HOH A . 
C 3 HOH   51  451 78  HOH   HOH A . 
C 3 HOH   52  452 62  HOH   HOH A . 
C 3 HOH   53  453 307 HOH   HOH A . 
C 3 HOH   54  454 254 HOH   HOH A . 
C 3 HOH   55  455 165 HOH   HOH A . 
C 3 HOH   56  456 101 HOH   HOH A . 
C 3 HOH   57  457 1   HOH   HOH A . 
C 3 HOH   58  458 172 HOH   HOH A . 
C 3 HOH   59  459 117 HOH   HOH A . 
C 3 HOH   60  460 27  HOH   HOH A . 
C 3 HOH   61  461 164 HOH   HOH A . 
C 3 HOH   62  462 10  HOH   HOH A . 
C 3 HOH   63  463 14  HOH   HOH A . 
C 3 HOH   64  464 68  HOH   HOH A . 
C 3 HOH   65  465 288 HOH   HOH A . 
C 3 HOH   66  466 152 HOH   HOH A . 
C 3 HOH   67  467 21  HOH   HOH A . 
C 3 HOH   68  468 132 HOH   HOH A . 
C 3 HOH   69  469 93  HOH   HOH A . 
C 3 HOH   70  470 232 HOH   HOH A . 
C 3 HOH   71  471 8   HOH   HOH A . 
C 3 HOH   72  472 6   HOH   HOH A . 
C 3 HOH   73  473 56  HOH   HOH A . 
C 3 HOH   74  474 158 HOH   HOH A . 
C 3 HOH   75  475 65  HOH   HOH A . 
C 3 HOH   76  476 77  HOH   HOH A . 
C 3 HOH   77  477 85  HOH   HOH A . 
C 3 HOH   78  478 159 HOH   HOH A . 
C 3 HOH   79  479 7   HOH   HOH A . 
C 3 HOH   80  480 25  HOH   HOH A . 
C 3 HOH   81  481 141 HOH   HOH A . 
C 3 HOH   82  482 103 HOH   HOH A . 
C 3 HOH   83  483 149 HOH   HOH A . 
C 3 HOH   84  484 29  HOH   HOH A . 
C 3 HOH   85  485 257 HOH   HOH A . 
C 3 HOH   86  486 26  HOH   HOH A . 
C 3 HOH   87  487 55  HOH   HOH A . 
C 3 HOH   88  488 45  HOH   HOH A . 
C 3 HOH   89  489 313 HOH   HOH A . 
C 3 HOH   90  490 160 HOH   HOH A . 
C 3 HOH   91  491 105 HOH   HOH A . 
C 3 HOH   92  492 282 HOH   HOH A . 
C 3 HOH   93  493 24  HOH   HOH A . 
C 3 HOH   94  494 53  HOH   HOH A . 
C 3 HOH   95  495 15  HOH   HOH A . 
C 3 HOH   96  496 17  HOH   HOH A . 
C 3 HOH   97  497 203 HOH   HOH A . 
C 3 HOH   98  498 169 HOH   HOH A . 
C 3 HOH   99  499 310 HOH   HOH A . 
C 3 HOH   100 500 48  HOH   HOH A . 
C 3 HOH   101 501 95  HOH   HOH A . 
C 3 HOH   102 502 204 HOH   HOH A . 
C 3 HOH   103 503 34  HOH   HOH A . 
C 3 HOH   104 504 175 HOH   HOH A . 
C 3 HOH   105 505 237 HOH   HOH A . 
C 3 HOH   106 506 63  HOH   HOH A . 
C 3 HOH   107 507 37  HOH   HOH A . 
C 3 HOH   108 508 67  HOH   HOH A . 
C 3 HOH   109 509 86  HOH   HOH A . 
C 3 HOH   110 510 52  HOH   HOH A . 
C 3 HOH   111 511 179 HOH   HOH A . 
C 3 HOH   112 512 130 HOH   HOH A . 
C 3 HOH   113 513 304 HOH   HOH A . 
C 3 HOH   114 514 157 HOH   HOH A . 
C 3 HOH   115 515 19  HOH   HOH A . 
C 3 HOH   116 516 128 HOH   HOH A . 
C 3 HOH   117 517 91  HOH   HOH A . 
C 3 HOH   118 518 121 HOH   HOH A . 
C 3 HOH   119 519 198 HOH   HOH A . 
C 3 HOH   120 520 224 HOH   HOH A . 
C 3 HOH   121 521 231 HOH   HOH A . 
C 3 HOH   122 522 260 HOH   HOH A . 
C 3 HOH   123 523 127 HOH   HOH A . 
C 3 HOH   124 524 3   HOH   HOH A . 
C 3 HOH   125 525 122 HOH   HOH A . 
C 3 HOH   126 526 87  HOH   HOH A . 
C 3 HOH   127 527 18  HOH   HOH A . 
C 3 HOH   128 528 41  HOH   HOH A . 
C 3 HOH   129 529 108 HOH   HOH A . 
C 3 HOH   130 530 218 HOH   HOH A . 
C 3 HOH   131 531 70  HOH   HOH A . 
C 3 HOH   132 532 72  HOH   HOH A . 
C 3 HOH   133 533 244 HOH   HOH A . 
C 3 HOH   134 534 200 HOH   HOH A . 
C 3 HOH   135 535 239 HOH   HOH A . 
C 3 HOH   136 536 9   HOH   HOH A . 
C 3 HOH   137 537 191 HOH   HOH A . 
C 3 HOH   138 538 261 HOH   HOH A . 
C 3 HOH   139 539 219 HOH   HOH A . 
C 3 HOH   140 540 297 HOH   HOH A . 
C 3 HOH   141 541 32  HOH   HOH A . 
C 3 HOH   142 542 134 HOH   HOH A . 
C 3 HOH   143 543 33  HOH   HOH A . 
C 3 HOH   144 544 154 HOH   HOH A . 
C 3 HOH   145 545 58  HOH   HOH A . 
C 3 HOH   146 546 89  HOH   HOH A . 
C 3 HOH   147 547 275 HOH   HOH A . 
C 3 HOH   148 548 81  HOH   HOH A . 
C 3 HOH   149 549 22  HOH   HOH A . 
C 3 HOH   150 550 206 HOH   HOH A . 
C 3 HOH   151 551 166 HOH   HOH A . 
C 3 HOH   152 552 35  HOH   HOH A . 
C 3 HOH   153 553 88  HOH   HOH A . 
C 3 HOH   154 554 66  HOH   HOH A . 
C 3 HOH   155 555 11  HOH   HOH A . 
C 3 HOH   156 556 295 HOH   HOH A . 
C 3 HOH   157 557 151 HOH   HOH A . 
C 3 HOH   158 558 99  HOH   HOH A . 
C 3 HOH   159 559 250 HOH   HOH A . 
C 3 HOH   160 560 84  HOH   HOH A . 
C 3 HOH   161 561 111 HOH   HOH A . 
C 3 HOH   162 562 76  HOH   HOH A . 
C 3 HOH   163 563 124 HOH   HOH A . 
C 3 HOH   164 564 212 HOH   HOH A . 
C 3 HOH   165 565 168 HOH   HOH A . 
C 3 HOH   166 566 243 HOH   HOH A . 
C 3 HOH   167 567 109 HOH   HOH A . 
C 3 HOH   168 568 30  HOH   HOH A . 
C 3 HOH   169 569 64  HOH   HOH A . 
C 3 HOH   170 570 147 HOH   HOH A . 
C 3 HOH   171 571 146 HOH   HOH A . 
C 3 HOH   172 572 184 HOH   HOH A . 
C 3 HOH   173 573 47  HOH   HOH A . 
C 3 HOH   174 574 49  HOH   HOH A . 
C 3 HOH   175 575 150 HOH   HOH A . 
C 3 HOH   176 576 273 HOH   HOH A . 
C 3 HOH   177 577 291 HOH   HOH A . 
C 3 HOH   178 578 39  HOH   HOH A . 
C 3 HOH   179 579 125 HOH   HOH A . 
C 3 HOH   180 580 133 HOH   HOH A . 
C 3 HOH   181 581 79  HOH   HOH A . 
C 3 HOH   182 582 264 HOH   HOH A . 
C 3 HOH   183 583 249 HOH   HOH A . 
C 3 HOH   184 584 40  HOH   HOH A . 
C 3 HOH   185 585 314 HOH   HOH A . 
C 3 HOH   186 586 2   HOH   HOH A . 
C 3 HOH   187 587 42  HOH   HOH A . 
C 3 HOH   188 588 189 HOH   HOH A . 
C 3 HOH   189 589 156 HOH   HOH A . 
C 3 HOH   190 590 290 HOH   HOH A . 
C 3 HOH   191 591 36  HOH   HOH A . 
C 3 HOH   192 592 296 HOH   HOH A . 
C 3 HOH   193 593 57  HOH   HOH A . 
C 3 HOH   194 594 221 HOH   HOH A . 
C 3 HOH   195 595 5   HOH   HOH A . 
C 3 HOH   196 596 259 HOH   HOH A . 
C 3 HOH   197 597 277 HOH   HOH A . 
C 3 HOH   198 598 285 HOH   HOH A . 
C 3 HOH   199 599 298 HOH   HOH A . 
C 3 HOH   200 600 106 HOH   HOH A . 
C 3 HOH   201 601 211 HOH   HOH A . 
C 3 HOH   202 602 305 HOH   HOH A . 
C 3 HOH   203 603 197 HOH   HOH A . 
C 3 HOH   204 604 113 HOH   HOH A . 
C 3 HOH   205 605 116 HOH   HOH A . 
C 3 HOH   206 606 155 HOH   HOH A . 
C 3 HOH   207 607 267 HOH   HOH A . 
C 3 HOH   208 608 283 HOH   HOH A . 
C 3 HOH   209 609 286 HOH   HOH A . 
C 3 HOH   210 610 252 HOH   HOH A . 
C 3 HOH   211 611 194 HOH   HOH A . 
C 3 HOH   212 612 217 HOH   HOH A . 
C 3 HOH   213 613 46  HOH   HOH A . 
C 3 HOH   214 614 255 HOH   HOH A . 
C 3 HOH   215 615 248 HOH   HOH A . 
C 3 HOH   216 616 142 HOH   HOH A . 
C 3 HOH   217 617 112 HOH   HOH A . 
C 3 HOH   218 618 316 HOH   HOH A . 
C 3 HOH   219 619 265 HOH   HOH A . 
C 3 HOH   220 620 182 HOH   HOH A . 
C 3 HOH   221 621 215 HOH   HOH A . 
C 3 HOH   222 622 145 HOH   HOH A . 
C 3 HOH   223 623 276 HOH   HOH A . 
C 3 HOH   224 624 256 HOH   HOH A . 
C 3 HOH   225 625 136 HOH   HOH A . 
C 3 HOH   226 626 233 HOH   HOH A . 
C 3 HOH   227 627 287 HOH   HOH A . 
C 3 HOH   228 628 114 HOH   HOH A . 
C 3 HOH   229 629 216 HOH   HOH A . 
C 3 HOH   230 630 205 HOH   HOH A . 
C 3 HOH   231 631 274 HOH   HOH A . 
C 3 HOH   232 632 271 HOH   HOH A . 
C 3 HOH   233 633 139 HOH   HOH A . 
C 3 HOH   234 634 225 HOH   HOH A . 
C 3 HOH   235 635 183 HOH   HOH A . 
C 3 HOH   236 636 131 HOH   HOH A . 
C 3 HOH   237 637 75  HOH   HOH A . 
C 3 HOH   238 638 181 HOH   HOH A . 
C 3 HOH   239 639 69  HOH   HOH A . 
C 3 HOH   240 640 300 HOH   HOH A . 
C 3 HOH   241 641 213 HOH   HOH A . 
C 3 HOH   242 642 119 HOH   HOH A . 
C 3 HOH   243 643 262 HOH   HOH A . 
C 3 HOH   244 644 148 HOH   HOH A . 
C 3 HOH   245 645 185 HOH   HOH A . 
C 3 HOH   246 646 294 HOH   HOH A . 
C 3 HOH   247 647 306 HOH   HOH A . 
C 3 HOH   248 648 140 HOH   HOH A . 
C 3 HOH   249 649 107 HOH   HOH A . 
C 3 HOH   250 650 241 HOH   HOH A . 
C 3 HOH   251 651 174 HOH   HOH A . 
C 3 HOH   252 652 280 HOH   HOH A . 
C 3 HOH   253 653 214 HOH   HOH A . 
C 3 HOH   254 654 187 HOH   HOH A . 
C 3 HOH   255 655 71  HOH   HOH A . 
C 3 HOH   256 656 176 HOH   HOH A . 
C 3 HOH   257 657 317 HOH   HOH A . 
C 3 HOH   258 658 83  HOH   HOH A . 
C 3 HOH   259 659 228 HOH   HOH A . 
C 3 HOH   260 660 54  HOH   HOH A . 
C 3 HOH   261 661 170 HOH   HOH A . 
C 3 HOH   262 662 207 HOH   HOH A . 
C 3 HOH   263 663 309 HOH   HOH A . 
C 3 HOH   264 664 293 HOH   HOH A . 
C 3 HOH   265 665 190 HOH   HOH A . 
C 3 HOH   266 666 279 HOH   HOH A . 
C 3 HOH   267 667 120 HOH   HOH A . 
C 3 HOH   268 668 236 HOH   HOH A . 
C 3 HOH   269 669 51  HOH   HOH A . 
C 3 HOH   270 670 292 HOH   HOH A . 
C 3 HOH   271 671 199 HOH   HOH A . 
C 3 HOH   272 672 270 HOH   HOH A . 
C 3 HOH   273 673 299 HOH   HOH A . 
C 3 HOH   274 674 238 HOH   HOH A . 
C 3 HOH   275 675 235 HOH   HOH A . 
C 3 HOH   276 676 302 HOH   HOH A . 
C 3 HOH   277 677 210 HOH   HOH A . 
C 3 HOH   278 678 129 HOH   HOH A . 
C 3 HOH   279 679 188 HOH   HOH A . 
C 3 HOH   280 680 246 HOH   HOH A . 
C 3 HOH   281 681 144 HOH   HOH A . 
C 3 HOH   282 682 278 HOH   HOH A . 
C 3 HOH   283 683 104 HOH   HOH A . 
C 3 HOH   284 684 240 HOH   HOH A . 
C 3 HOH   285 685 193 HOH   HOH A . 
C 3 HOH   286 686 177 HOH   HOH A . 
C 3 HOH   287 687 226 HOH   HOH A . 
C 3 HOH   288 688 245 HOH   HOH A . 
C 3 HOH   289 689 301 HOH   HOH A . 
C 3 HOH   290 690 253 HOH   HOH A . 
C 3 HOH   291 691 312 HOH   HOH A . 
C 3 HOH   292 692 272 HOH   HOH A . 
C 3 HOH   293 693 289 HOH   HOH A . 
C 3 HOH   294 694 173 HOH   HOH A . 
C 3 HOH   295 695 178 HOH   HOH A . 
C 3 HOH   296 696 202 HOH   HOH A . 
C 3 HOH   297 697 208 HOH   HOH A . 
C 3 HOH   298 698 98  HOH   HOH A . 
C 3 HOH   299 699 209 HOH   HOH A . 
C 3 HOH   300 700 201 HOH   HOH A . 
C 3 HOH   301 701 230 HOH   HOH A . 
C 3 HOH   302 702 171 HOH   HOH A . 
C 3 HOH   303 703 303 HOH   HOH A . 
C 3 HOH   304 704 110 HOH   HOH A . 
C 3 HOH   305 705 229 HOH   HOH A . 
C 3 HOH   306 706 192 HOH   HOH A . 
C 3 HOH   307 707 161 HOH   HOH A . 
C 3 HOH   308 708 162 HOH   HOH A . 
C 3 HOH   309 709 242 HOH   HOH A . 
C 3 HOH   310 710 251 HOH   HOH A . 
C 3 HOH   311 711 92  HOH   HOH A . 
C 3 HOH   312 712 266 HOH   HOH A . 
C 3 HOH   313 713 223 HOH   HOH A . 
C 3 HOH   314 714 284 HOH   HOH A . 
C 3 HOH   315 715 269 HOH   HOH A . 
C 3 HOH   316 716 308 HOH   HOH A . 
C 3 HOH   317 717 258 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             587921.651 
_cell.length_a           65.897 
_cell.length_b           89.204 
_cell.length_c           100.016 
_cell.angle_beta         90.000 
_cell.angle_gamma        90.000 
_cell.angle_alpha        90.000 
_cell.entry_id           7HA2 
_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                         7HA2 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
# 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
_exptl.entry_id          7HA2 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_Matthews      2.88 
_exptl_crystal.density_percent_sol   57.23 
_exptl_crystal.density_meas          ? 
_exptl_crystal.description           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.pH              8.5 
_exptl_crystal_grow.temp            277 
_exptl_crystal_grow.pdbx_details    '100mM Tris-HCl pH 8.5, 22% PEG4000, 200mM MgCl2' 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_diffrn.id                     1 
_diffrn.crystal_id             1 
_diffrn.ambient_temp           100 
_diffrn.ambient_temp_details   ? 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               PIXEL 
_diffrn_detector.type                   'DECTRIS EIGER2 S 9M' 
_diffrn_detector.pdbx_collection_date   2023-07-05 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.pdbx_scattering_type             x-ray 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.monochromator                    Si111 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.97918 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.pdbx_synchrotron_beamline   BL02U1 
_diffrn_source.type                        'SSRF BEAMLINE BL02U1' 
_diffrn_source.pdbx_wavelength_list        0.97918 
_diffrn_source.pdbx_synchrotron_site       SSRF 
_diffrn_source.pdbx_wavelength             ? 
# 
_reflns.entry_id                     7HA2 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             34.650 
_reflns.d_resolution_high            1.730 
_reflns.number_obs                   29755 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         95.200 
_reflns.pdbx_Rmerge_I_obs            0.066 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        16.700 
_reflns.B_iso_Wilson_estimate        ? 
_reflns.pdbx_redundancy              5.700 
_reflns.pdbx_Rrim_I_all              0.073 
_reflns.pdbx_Rpim_I_all              0.030 
_reflns.pdbx_CC_half                 0.999 
_reflns.pdbx_netI_over_av_sigmaI     ? 
_reflns.pdbx_number_measured_all     170134 
_reflns.pdbx_scaling_rejects         4 
_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 1.730 1.820  ? 24767 4388 ? 0.591 ? ? ? 5.600 ? 2.800  ? ? ? ? ? ? 97.000 0.650 0.267 0.831 
1 2 5.460 34.650 ? 5693  1018 ? 0.028 ? ? ? 5.600 ? 44.300 ? ? ? ? ? ? 96.300 0.030 0.012 0.999 
# 
_refine.entry_id                                 7HA2 
_refine.pdbx_method_to_determine_struct          'FOURIER SYNTHESIS' 
_refine.ls_percent_reflns_R_free                 5.05 
_refine.pdbx_overall_phase_error                 19.7265 
_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                          0.1771 
_refine.B_iso_mean                               27.76 
_refine.ls_number_reflns_R_free                  1496 
_refine.ls_percent_reflns_obs                    94.42 
_refine.ls_R_factor_R_work                       0.1757 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_refine.ls_d_res_high                            1.73 
_refine.ls_number_reflns_obs                     29625 
_refine.pdbx_ls_sigma_F                          1.33 
_refine.ls_number_reflns_R_work                  28129 
_refine.ls_d_res_low                             31.23 
_refine.pdbx_stereochemistry_target_values       'GeoStd + Monomer Library + CDL v1.2' 
_refine.ls_R_factor_R_free                       0.2029 
_refine.overall_SU_ML                            0.1625 
_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         11 
_refine_hist.number_atoms_solvent             317 
_refine_hist.number_atoms_total               1972 
_refine_hist.d_res_high                       1.73 
_refine_hist.d_res_low                        31.23 
# 
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           1681 0.0043 ? ? ? 
'X-RAY DIFFRACTION' f_angle_d          2266 0.7592 ? ? ? 
'X-RAY DIFFRACTION' f_chiral_restr     259  0.0491 ? ? ? 
'X-RAY DIFFRACTION' f_plane_restr      289  0.0058 ? ? ? 
'X-RAY DIFFRACTION' f_dihedral_angle_d 223  6.8877 ? ? ? 
# 
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' 1.73 1.78  2588 0.2247 96.07 0.2804 124 . . . . . 
'X-RAY DIFFRACTION' 1.78 1.84  2588 0.2243 97.78 0.2327 138 . . . . . 
'X-RAY DIFFRACTION' 1.84 1.92  2574 0.2966 95.45 0.2955 130 . . . . . 
'X-RAY DIFFRACTION' 1.92 2.01  2587 0.2120 96.44 0.2585 122 . . . . . 
'X-RAY DIFFRACTION' 2.01 2.11  2637 0.1744 98.26 0.1724 129 . . . . . 
'X-RAY DIFFRACTION' 2.11 2.22  2133 0.1691 97.43 0.1965 139 . . . . . 
'X-RAY DIFFRACTION' 2.27 2.42  2225 0.1775 98.99 0.2150 134 . . . . . 
'X-RAY DIFFRACTION' 2.42 2.66  2665 0.1791 98.11 0.1981 140 . . . . . 
'X-RAY DIFFRACTION' 2.66 3.05  2653 0.1783 99.16 0.2024 171 . . . . . 
'X-RAY DIFFRACTION' 3.05 3.84  2695 0.1586 97.96 0.1999 145 . . . . . 
'X-RAY DIFFRACTION' 3.84 31.23 2784 0.1480 96.45 0.1684 124 . . . . . 
# 
_struct.entry_id                  7HA2 
_struct.title                     'PanDDA analysis group deposition -- Crystal structure of HSP90N in complex with Fr14256' 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_details        ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HA2 
_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              7HA2 
_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 7HA2 MET A 1   ? UNP P07900 ? ? 'initiating methionine' 8   1 
1 7HA2 LEU A 230 ? UNP P07900 ? ? 'expression tag'        237 2 
1 7HA2 GLU A 231 ? UNP P07900 ? ? 'expression tag'        238 3 
1 7HA2 HIS A 232 ? UNP P07900 ? ? 'expression tag'        239 4 
1 7HA2 HIS A 233 ? UNP P07900 ? ? 'expression tag'        240 5 
1 7HA2 HIS A 234 ? UNP P07900 ? ? 'expression tag'        241 6 
1 7HA2 HIS A 235 ? UNP P07900 ? ? 'expression tag'        242 7 
1 7HA2 HIS A 236 ? UNP P07900 ? ? 'expression tag'        243 8 
1 7HA2 HIS A 237 ? UNP P07900 ? ? 'expression tag'        244 9 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 GLN A 16  ? THR A 29  ? GLN A 23  THR A 36  1 ? 14 
HELX_P HELX_P2  AA2 GLU A 35  ? ASP A 59  ? GLU A 42  ASP A 66  1 ? 25 
HELX_P HELX_P3  AA3 PRO A 60  ? ASP A 64  ? PRO A 67  ASP A 71  5 ? 5  
HELX_P HELX_P4  AA4 THR A 92  ? ASN A 98  ? THR A 99  ASN A 105 1 ? 7  
HELX_P HELX_P5  AA5 ASN A 99  ? THR A 102 ? ASN A 106 THR A 109 5 ? 4  
HELX_P HELX_P6  AA6 ILE A 103 ? GLN A 116 ? ILE A 110 GLN A 123 1 ? 14 
HELX_P HELX_P7  AA7 ASP A 120 ? GLY A 128 ? ASP A 127 GLY A 135 5 ? 9  
HELX_P HELX_P8  AA8 VAL A 129 ? LEU A 136 ? VAL A 136 LEU A 143 5 ? 8  
HELX_P HELX_P9  AA9 GLU A 185 ? LEU A 191 ? GLU A 192 LEU A 198 5 ? 7  
HELX_P HELX_P10 AB1 GLU A 192 ? SER A 204 ? GLU A 199 SER A 211 1 ? 13 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
_struct_sheet.id               AA1 
_struct_sheet.type             ? 
_struct_sheet.number_strands   8 
_struct_sheet.details          ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA1 5 6 ? anti-parallel 
AA1 6 7 ? anti-parallel 
AA1 7 8 ? parallel      
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 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 VAL A 85  ? O VAL A 92  N ASN A 72  ? N ASN A 79  
AA1 7 8 N LEU A 73  ? N LEU A 80  O THR A 212 ? O THR A 219 
# 
_pdbx_entry_details.entry_id                   7HA2 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1  1 O A HOH 577 ? ? O A HOH 670 ? ? 1.81 
2  1 O A HOH 623 ? ? O A HOH 632 ? ? 1.86 
3  1 O A HOH 559 ? ? O A HOH 624 ? ? 1.89 
4  1 O A HOH 618 ? ? O A HOH 673 ? ? 1.92 
5  1 O A HOH 618 ? ? O A HOH 624 ? ? 1.99 
6  1 O A HOH 547 ? ? O A HOH 666 ? ? 2.08 
7  1 O A HOH 624 ? ? O A HOH 634 ? ? 2.09 
8  1 O A HOH 664 ? ? O A HOH 697 ? ? 2.12 
9  1 O A HOH 530 ? ? O A HOH 705 ? ? 2.14 
10 1 O A HOH 559 ? ? O A HOH 650 ? ? 2.16 
11 1 O A HOH 579 ? ? O A HOH 630 ? ? 2.18 
# 
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 535 ? ? 1_555 O A HOH 635 ? ? 2_555 2.04 
2 1 O A HOH 643 ? ? 1_555 O A HOH 686 ? ? 3_555 2.17 
# 
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  ? ? -163.49 109.00  
2 1 ALA A 166 ? ? 62.71   -143.29 
3 1 ARG A 182 ? ? -170.18 135.01  
# 
_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     676 
_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 12.3557020248  -17.8554477199 -18.7079066678 0.107527852414 0.158019514559 0.163571452845 
0.0017907791648    -0.0271726648146  -0.024869983813  3.04830031787 1.31592279259  6.83559870747  -1.0946832163    -3.31297082548  
0.616007141134  0.0928216657257  -0.290879631368 -0.0472012655339 0.056039484184   -0.0835176140495 -0.0538247042144 
0.109240857155   0.283063458727  -0.0860517554917 
2  ? 'X-RAY DIFFRACTION' refined -5.20771297047 -6.28155963979 -20.9394488613 0.142082442684 0.125794963428 0.187545278922 
-0.00944271462794  -0.00808988769868 -0.0422583389505 1.99270321548 4.49332372052  5.55002189585  -1.79664735917   1.94822617858   
-3.79958795421  -0.0576150142708 0.0697076896126 0.179662224252   0.115160431131   -0.111029813894  0.0546431234385  
-0.325136528199  0.155740495081  0.165519731246   
3  ? 'X-RAY DIFFRACTION' refined -10.1203563361 -14.963410096  -25.1825018588 0.126728870856 0.124088274135 0.177427110499 
-0.00722325722319  -0.0511516557448  -0.0430955940357 1.80682911085 3.27991225007  3.60556364978  -0.50528110561   0.0411463932017 
-1.71774463116  0.0669088998847  0.0708907922763 -0.154966806371  -0.202817824299  0.0263106180489  0.307548735389   
0.109006880655   -0.203666757534 -0.133070991981  
4  ? 'X-RAY DIFFRACTION' refined 6.90021539272  -10.9904479274 -29.8469530512 0.180035806982 0.155163895669 0.20745028096  
0.0158225114324    0.0117812005461   0.00115775625636 3.29177258651 2.23343285706  6.7256307987   0.00944351341294 1.39724331207   
2.3299145323    0.116695338635   0.122230877141  0.26925540876    -0.230645276744  -0.144395852335  -0.116647959419  
-0.160837382601  0.103656109285  -0.0445692432039 
5  ? 'X-RAY DIFFRACTION' refined 12.3979833426  -5.97220783937 -12.67847449   0.23110389915  0.509158788904 0.323835376498 
-0.101574376783    0.0286972179675   -0.112716201418  1.32788145732 2.51842507646  4.90552629263  1.00328195259    0.38232854452   
-0.174151555357 0.555882829857   -1.14771391362  0.728742411248   0.296852953458   -0.239860040997  -0.154930561533  
-0.637814550765  1.57818019118   -0.111585803678  
6  ? 'X-RAY DIFFRACTION' refined 2.58924722745  -19.0135462471 -20.4585531373 0.140213946179 0.122368514231 0.164863638471 
0.00864783993594   -0.00528653385261 -0.0143273571615 2.75648411269 1.09662400055  3.70730293749  -0.487596940951  0.534096132386  
-0.218671761419 0.0497066069805  -0.135763292179 -0.145939891676  0.00701496495612 0.0289059516445  0.0448480072748  
0.185584076681   0.176736070391  0.00189233880975 
7  ? 'X-RAY DIFFRACTION' refined 1.65252771974  -17.751306365  -31.7758567238 0.191912727557 0.158881966879 0.167603154518 
-0.000139950516905 0.00160302024004  -0.0353429654494 4.50073008957 2.44111747439  3.42428143883  -1.92228171614   1.42625159607   
-1.08625223297  0.242794371472   0.298338872481  -0.232673286227  -0.326639527539  -0.122365399587  0.0936833262418  
0.173957132556   0.116133013126  -0.05374567473   
8  ? 'X-RAY DIFFRACTION' refined -1.88911872848 -21.2552898595 -32.5686360783 0.232727713981 0.214342337165 0.359179110227 
0.0211403323748    -0.0592060357234  -0.0913978348059 2.5865695371  0.512723765612 0.882899094562 -0.79028779562   -0.598854727795 
0.189775856078  0.107052227438   0.485895336642  -0.851036022733  -0.106377053063  -0.161073899641  0.514942037352   
0.167187037808   -0.148329511817 0.0200975944041  
9  ? 'X-RAY DIFFRACTION' refined -5.58524032965 -20.1281931128 -10.3570027892 0.164526688213 0.206401710236 0.169807058705 
-0.0158673255248   -0.0193696136174  0.0199832205756  2.82871437354 1.97043523039  3.47467093388  -0.706159837551  -0.786239370807 
-0.322516101319 -0.0725301874531 -0.3782787116   -0.2438157557    0.169351372878   0.0451809910245  0.0598984142808  
0.234734024605   0.0428272887245 0.0431778608383  
10 ? 'X-RAY DIFFRACTION' refined -13.8960848568 -13.3346526032 -14.5293007516 0.161006273565 0.190134843829 0.142492080172 
-0.00433760335044  -0.00125656793196 -0.0320943421645 3.63057464223 2.93603040578  3.53597142337  -0.612851664193  -0.574858776222 
-0.478941137732 0.0581827807911  -0.244551303226 0.0164921397066  0.430874758811   -0.0700256405262 0.125686192713   
-0.0921180043812 -0.177323125804 0.00422687729192 
# 
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 110 A 95  . 
;chain 'A' and (resid 100 through 110 )
;
5  5  'X-RAY DIFFRACTION' A 111 A 96  A 136 A 121 . 
;chain 'A' and (resid 111 through 136 )
;
6  6  'X-RAY DIFFRACTION' A 137 A 122 A 153 A 138 . 
;chain 'A' and (resid 137 through 153 )
;
7  7  'X-RAY DIFFRACTION' A 154 A 139 A 168 A 153 . 
;chain 'A' and (resid 154 through 168 )
;
8  8  'X-RAY DIFFRACTION' A 169 A 154 A 182 A 167 . 
;chain 'A' and (resid 169 through 182 )
;
9  9  'X-RAY DIFFRACTION' A 183 A 168 A 210 A 195 . 
;chain 'A' and (resid 183 through 210 )
;
10 10 'X-RAY DIFFRACTION' A 211 A 196 A 224 A 209 . 
;chain 'A' and (resid 211 through 224 )
;
# 
_pdbx_distant_solvent_atoms.id                                1 
_pdbx_distant_solvent_atoms.PDB_model_num                     1 
_pdbx_distant_solvent_atoms.auth_atom_id                      O 
_pdbx_distant_solvent_atoms.label_alt_id                      ? 
_pdbx_distant_solvent_atoms.auth_asym_id                      A 
_pdbx_distant_solvent_atoms.auth_comp_id                      HOH 
_pdbx_distant_solvent_atoms.auth_seq_id                       717 
_pdbx_distant_solvent_atoms.PDB_ins_code                      ? 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance   5.96 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance          . 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A MET 8   ? A MET 1   
2  1 Y 1 A ASP 9   ? A ASP 2   
3  1 Y 1 A GLN 10  ? A GLN 3   
4  1 Y 1 A PRO 11  ? A PRO 4   
5  1 Y 1 A MET 12  ? A MET 5   
6  1 Y 1 A GLU 13  ? A GLU 6   
7  1 Y 1 A GLU 14  ? A GLU 7   
8  1 Y 1 A GLU 15  ? A GLU 8   
9  1 Y 1 A GLU 225 ? A GLU 218 
10 1 Y 1 A ARG 226 ? A ARG 219 
11 1 Y 1 A ASP 227 ? A ASP 220 
12 1 Y 1 A LYS 228 ? A LYS 221 
13 1 Y 1 A GLU 229 ? A GLU 222 
14 1 Y 1 A VAL 230 ? A VAL 223 
15 1 Y 1 A SER 231 ? A SER 224 
16 1 Y 1 A ASP 232 ? A ASP 225 
17 1 Y 1 A ASP 233 ? A ASP 226 
18 1 Y 1 A GLU 234 ? A GLU 227 
19 1 Y 1 A ALA 235 ? A ALA 228 
20 1 Y 1 A GLU 236 ? A GLU 229 
21 1 Y 1 A LEU 237 ? A LEU 230 
22 1 Y 1 A GLU 238 ? A GLU 231 
23 1 Y 1 A HIS 239 ? A HIS 232 
24 1 Y 1 A HIS 240 ? A HIS 233 
25 1 Y 1 A HIS 241 ? A HIS 234 
26 1 Y 1 A HIS 242 ? A HIS 235 
27 1 Y 1 A HIS 243 ? A HIS 236 
28 1 Y 1 A HIS 244 ? A HIS 237 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
A1AX8 C1   C N N 1   
A1AX8 C2   C Y N 2   
A1AX8 C3   C Y N 3   
A1AX8 C4   C Y N 4   
A1AX8 C5   C Y N 5   
A1AX8 C6   C Y N 6   
A1AX8 C7   C Y N 7   
A1AX8 C8   C N N 8   
A1AX8 N1   N N N 9   
A1AX8 N2   N N N 10  
A1AX8 O1   O N N 11  
A1AX8 H3   H N N 12  
A1AX8 H4   H N N 13  
A1AX8 H7   H N N 14  
A1AX8 H82  H N N 15  
A1AX8 H83  H N N 16  
A1AX8 H81  H N N 17  
A1AX8 H12  H N N 18  
A1AX8 H11  H N N 19  
A1AX8 H21  H N N 20  
A1AX8 H22  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 
A1AX8 O1  C1   doub N N 1   
A1AX8 C1  N1   sing N N 2   
A1AX8 C1  C2   sing N N 3   
A1AX8 C2  C3   doub Y N 4   
A1AX8 C2  C7   sing Y N 5   
A1AX8 C3  C4   sing Y N 6   
A1AX8 C4  C5   doub Y N 7   
A1AX8 C5  C6   sing Y N 8   
A1AX8 C5  C8   sing N N 9   
A1AX8 C6  N2   sing N N 10  
A1AX8 C6  C7   doub Y N 11  
A1AX8 C3  H3   sing N N 12  
A1AX8 C4  H4   sing N N 13  
A1AX8 C7  H7   sing N N 14  
A1AX8 C8  H82  sing N N 15  
A1AX8 C8  H83  sing N N 16  
A1AX8 C8  H81  sing N N 17  
A1AX8 N1  H12  sing N N 18  
A1AX8 N1  H11  sing N N 19  
A1AX8 N2  H21  sing N N 20  
A1AX8 N2  H22  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                    7HA2 
_atom_sites.fract_transf_matrix[1][1]   0.015175 
_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]   0.011210 
_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]   0.009998 
_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   ? 4.39266   -28.46070 -38.99377 1.000 39.38563  ? 16  GLU   A N   1 
ATOM   2    C CA  . GLU   A 1 9   ? 5.66326   -27.76755 -39.18049 1.000 48.68897  ? 16  GLU   A CA  1 
ATOM   3    C C   . GLU   A 1 9   ? 5.92302   -26.83395 -38.00123 1.000 48.10292  ? 16  GLU   A C   1 
ATOM   4    O O   . GLU   A 1 9   ? 5.30454   -25.77698 -37.88679 1.000 43.58914  ? 16  GLU   A O   1 
ATOM   5    C CB  . GLU   A 1 9   ? 5.66158   -26.99267 -40.50033 1.000 62.58881  ? 16  GLU   A CB  1 
ATOM   6    C CG  . GLU   A 1 9   ? 7.03439   -26.83223 -41.14190 1.000 74.33834  ? 16  GLU   A CG  1 
ATOM   7    C CD  . GLU   A 1 9   ? 7.80308   -25.63652 -40.61015 1.000 83.84356  ? 16  GLU   A CD  1 
ATOM   8    O OE1 . GLU   A 1 9   ? 7.23602   -24.86858 -39.80471 1.000 72.93127  ? 16  GLU   A OE1 1 
ATOM   9    O OE2 . GLU   A 1 9   ? 8.97916   -25.46419 -40.99728 1.000 89.91185  ? 16  GLU   A OE2 1 
ATOM   10   N N   . VAL   A 1 10  ? 6.84912   -27.22914 -37.13095 1.000 37.76162  ? 17  VAL   A N   1 
ATOM   11   C CA  . VAL   A 1 10  ? 7.09534   -26.55342 -35.86344 1.000 28.74034  ? 17  VAL   A CA  1 
ATOM   12   C C   . VAL   A 1 10  ? 8.46023   -25.88378 -35.92849 1.000 27.35052  ? 17  VAL   A C   1 
ATOM   13   O O   . VAL   A 1 10  ? 9.45675   -26.52711 -36.27821 1.000 31.80153  ? 17  VAL   A O   1 
ATOM   14   C CB  . VAL   A 1 10  ? 7.03416   -27.54162 -34.68709 1.000 30.22876  ? 17  VAL   A CB  1 
ATOM   15   C CG1 . VAL   A 1 10  ? 7.38967   -26.84148 -33.38036 1.000 34.72208  ? 17  VAL   A CG1 1 
ATOM   16   C CG2 . VAL   A 1 10  ? 5.67586   -28.21503 -34.62359 1.000 45.20985  ? 17  VAL   A CG2 1 
ATOM   17   N N   . GLU   A 1 11  ? 8.51004   -24.60081 -35.59051 1.000 23.48893  ? 18  GLU   A N   1 
ATOM   18   C CA  . GLU   A 1 11  ? 9.76256   -23.85649 -35.54696 1.000 21.08675  ? 18  GLU   A CA  1 
ATOM   19   C C   . GLU   A 1 11  ? 10.18742  -23.68461 -34.09537 1.000 19.45526  ? 18  GLU   A C   1 
ATOM   20   O O   . GLU   A 1 11  ? 9.36751   -23.32582 -33.24601 1.000 18.78504  ? 18  GLU   A O   1 
ATOM   21   C CB  . GLU   A 1 11  ? 9.61203   -22.49321 -36.22247 1.000 25.08477  ? 18  GLU   A CB  1 
ATOM   22   C CG  . GLU   A 1 11  ? 9.42942   -22.55957 -37.72632 1.000 24.58729  ? 18  GLU   A CG  1 
ATOM   23   C CD  . GLU   A 1 11  ? 9.18708   -21.19042 -38.34000 1.000 35.18572  ? 18  GLU   A CD  1 
ATOM   24   O OE1 . GLU   A 1 11  ? 8.10836   -20.61111 -38.09138 1.000 33.45851  ? 18  GLU   A OE1 1 
ATOM   25   O OE2 . GLU   A 1 11  ? 10.06516  -20.69606 -39.07658 1.000 36.59184  ? 18  GLU   A OE2 1 
ATOM   26   N N   . THR   A 1 12  ? 11.45903  -23.95392 -33.81025 1.000 18.06926  ? 19  THR   A N   1 
ATOM   27   C CA  . THR   A 1 12  ? 11.99012  -23.85547 -32.45873 1.000 16.73261  ? 19  THR   A CA  1 
ATOM   28   C C   . THR   A 1 12  ? 12.98795  -22.71130 -32.39702 1.000 18.82216  ? 19  THR   A C   1 
ATOM   29   O O   . THR   A 1 12  ? 13.88134  -22.61986 -33.24482 1.000 17.54618  ? 19  THR   A O   1 
ATOM   30   C CB  . THR   A 1 12  ? 12.65390  -25.16436 -32.02671 1.000 17.53076  ? 19  THR   A CB  1 
ATOM   31   O OG1 . THR   A 1 12  ? 11.72344  -26.24024 -32.18289 1.000 20.99531  ? 19  THR   A OG1 1 
ATOM   32   C CG2 . THR   A 1 12  ? 13.09620  -25.08447 -30.56908 1.000 18.08213  ? 19  THR   A CG2 1 
ATOM   33   N N   . PHE   A 1 13  ? 12.83066  -21.85218 -31.39207 1.000 15.33489  ? 20  PHE   A N   1 
ATOM   34   C CA  . PHE   A 1 13  ? 13.62524  -20.64306 -31.23174 1.000 14.78516  ? 20  PHE   A CA  1 
ATOM   35   C C   . PHE   A 1 13  ? 14.28861  -20.63766 -29.86473 1.000 20.95753  ? 20  PHE   A C   1 
ATOM   36   O O   . PHE   A 1 13  ? 13.73887  -21.15006 -28.88840 1.000 18.54749  ? 20  PHE   A O   1 
ATOM   37   C CB  . PHE   A 1 13  ? 12.76969  -19.36740 -31.32839 1.000 17.44969  ? 20  PHE   A CB  1 
ATOM   38   C CG  . PHE   A 1 13  ? 12.03148  -19.20732 -32.61944 1.000 18.98364  ? 20  PHE   A CG  1 
ATOM   39   C CD1 . PHE   A 1 13  ? 10.81445  -19.84332 -32.82576 1.000 19.87036  ? 20  PHE   A CD1 1 
ATOM   40   C CD2 . PHE   A 1 13  ? 12.52500  -18.37377 -33.61328 1.000 18.96847  ? 20  PHE   A CD2 1 
ATOM   41   C CE1 . PHE   A 1 13  ? 10.12889  -19.68346 -34.01633 1.000 21.77548  ? 20  PHE   A CE1 1 
ATOM   42   C CE2 . PHE   A 1 13  ? 11.84034  -18.20394 -34.80363 1.000 20.32664  ? 20  PHE   A CE2 1 
ATOM   43   C CZ  . PHE   A 1 13  ? 10.63776  -18.85885 -35.00487 1.000 23.70839  ? 20  PHE   A CZ  1 
ATOM   44   N N   . ALA   A 1 14  ? 15.45790  -20.01384 -29.79338 1.000 17.74338  ? 21  ALA   A N   1 
ATOM   45   C CA  . ALA   A 1 14  ? 16.11930  -19.76318 -28.52139 1.000 17.30149  ? 21  ALA   A CA  1 
ATOM   46   C C   . ALA   A 1 14  ? 15.63669  -18.44051 -27.93982 1.000 18.46933  ? 21  ALA   A C   1 
ATOM   47   O O   . ALA   A 1 14  ? 15.54949  -17.43506 -28.65342 1.000 16.48954  ? 21  ALA   A O   1 
ATOM   48   C CB  . ALA   A 1 14  ? 17.63667  -19.73649 -28.70515 1.000 20.88425  ? 21  ALA   A CB  1 
ATOM   49   N N   . PHE   A 1 15  ? 15.30465  -18.44293 -26.64979 1.000 17.00368  ? 22  PHE   A N   1 
ATOM   50   C CA  . PHE   A 1 15  ? 15.07542  -17.17873 -25.96768 1.000 15.81639  ? 22  PHE   A CA  1 
ATOM   51   C C   . PHE   A 1 15  ? 16.34543  -16.34535 -26.00921 1.000 17.53346  ? 22  PHE   A C   1 
ATOM   52   O O   . PHE   A 1 15  ? 17.45823  -16.87360 -25.93843 1.000 18.89482  ? 22  PHE   A O   1 
ATOM   53   C CB  . PHE   A 1 15  ? 14.69217  -17.39725 -24.50162 1.000 15.78245  ? 22  PHE   A CB  1 
ATOM   54   C CG  . PHE   A 1 15  ? 13.28972  -17.90060 -24.29391 1.000 17.18350  ? 22  PHE   A CG  1 
ATOM   55   C CD1 . PHE   A 1 15  ? 12.19822  -17.09795 -24.57616 1.000 17.63738  ? 22  PHE   A CD1 1 
ATOM   56   C CD2 . PHE   A 1 15  ? 13.07309  -19.17315 -23.78918 1.000 15.94545  ? 22  PHE   A CD2 1 
ATOM   57   C CE1 . PHE   A 1 15  ? 10.90352  -17.56016 -24.37030 1.000 16.23465  ? 22  PHE   A CE1 1 
ATOM   58   C CE2 . PHE   A 1 15  ? 11.78860  -19.64729 -23.58531 1.000 14.68234  ? 22  PHE   A CE2 1 
ATOM   59   C CZ  . PHE   A 1 15  ? 10.69958  -18.83628 -23.87149 1.000 17.23185  ? 22  PHE   A CZ  1 
ATOM   60   N N   . GLN   A 1 16  ? 16.17856  -15.03022 -26.11690 1.000 18.24023  ? 23  GLN   A N   1 
ATOM   61   C CA  . GLN   A 1 16  ? 17.29202  -14.14349 -25.81165 1.000 22.48909  ? 23  GLN   A CA  1 
ATOM   62   C C   . GLN   A 1 16  ? 17.81076  -14.45352 -24.41574 1.000 18.27959  ? 23  GLN   A C   1 
ATOM   63   O O   . GLN   A 1 16  ? 17.03941  -14.79340 -23.51492 1.000 20.09669  ? 23  GLN   A O   1 
ATOM   64   C CB  . GLN   A 1 16  ? 16.86282  -12.67964 -25.90462 1.000 22.06203  ? 23  GLN   A CB  1 
ATOM   65   C CG  . GLN   A 1 16  ? 16.48915  -12.23876 -27.29684 1.000 31.92465  ? 23  GLN   A CG  1 
ATOM   66   C CD  . GLN   A 1 16  ? 15.90903  -10.84326 -27.30807 1.000 36.43394  ? 23  GLN   A CD  1 
ATOM   67   O OE1 . GLN   A 1 16  ? 14.69511  -10.66723 -27.24421 1.000 38.50759  ? 23  GLN   A OE1 1 
ATOM   68   N NE2 . GLN   A 1 16  ? 16.77742  -9.83850  -27.38923 1.000 35.42572  ? 23  GLN   A NE2 1 
ATOM   69   N N   . ALA   A 1 17  ? 19.13437  -14.36242 -24.25259 1.000 19.14600  ? 24  ALA   A N   1 
ATOM   70   C CA  . ALA   A 1 17  ? 19.76014  -14.73299 -22.98843 1.000 22.33855  ? 24  ALA   A CA  1 
ATOM   71   C C   . ALA   A 1 17  ? 19.09712  -14.03946 -21.80528 1.000 19.68569  ? 24  ALA   A C   1 
ATOM   72   O O   . ALA   A 1 17  ? 18.84469  -14.66545 -20.76790 1.000 24.04411  ? 24  ALA   A O   1 
ATOM   73   C CB  . ALA   A 1 17  ? 21.25216  -14.40189 -23.03623 1.000 23.53545  ? 24  ALA   A CB  1 
ATOM   74   N N   . GLU   A 1 18  ? 18.78522  -12.75076 -21.95041 1.000 22.73448  ? 25  GLU   A N   1 
ATOM   75   C CA  . GLU   A 1 18  ? 18.21353  -12.00351 -20.83615 1.000 23.92480  ? 25  GLU   A CA  1 
ATOM   76   C C   . GLU   A 1 18  ? 16.84589  -12.55264 -20.44412 1.000 23.62052  ? 25  GLU   A C   1 
ATOM   77   O O   . GLU   A 1 18  ? 16.49228  -12.56276 -19.25892 1.000 23.16828  ? 25  GLU   A O   1 
ATOM   78   C CB  . GLU   A 1 18  ? 18.11996  -10.51817 -21.18852 1.000 32.51905  ? 25  GLU   A CB  1 
ATOM   79   C CG  . GLU   A 1 18  ? 19.46956  -9.83188  -21.40007 1.000 29.40443  ? 25  GLU   A CG  1 
ATOM   80   C CD  . GLU   A 1 18  ? 20.04602  -10.03740 -22.79262 1.000 40.69269  ? 25  GLU   A CD  1 
ATOM   81   O OE1 . GLU   A 1 18  ? 19.42367  -10.74999 -23.60481 1.000 31.32941  ? 25  GLU   A OE1 1 
ATOM   82   O OE2 . GLU   A 1 18  ? 21.13188  -9.48547  -23.07636 1.000 43.34516  ? 25  GLU   A OE2 1 
ATOM   83   N N   . ILE   A 1 19  ? 16.06557  -13.01981 -21.42381 1.000 20.94632  ? 26  ILE   A N   1 
ATOM   84   C CA  . ILE   A 1 19  ? 14.74531  -13.57144 -21.12263 1.000 17.76767  ? 26  ILE   A CA  1 
ATOM   85   C C   . ILE   A 1 19  ? 14.87611  -14.96295 -20.50884 1.000 17.94267  ? 26  ILE   A C   1 
ATOM   86   O O   . ILE   A 1 19  ? 14.13845  -15.31634 -19.58586 1.000 20.41196  ? 26  ILE   A O   1 
ATOM   87   C CB  . ILE   A 1 19  ? 13.84437  -13.57802 -22.37916 1.000 19.11687  ? 26  ILE   A CB  1 
ATOM   88   C CG1 . ILE   A 1 19  ? 13.25490  -12.18713 -22.67277 1.000 19.40532  ? 26  ILE   A CG1 1 
ATOM   89   C CG2 . ILE   A 1 19  ? 12.68261  -14.56513 -22.22178 1.000 17.70826  ? 26  ILE   A CG2 1 
ATOM   90   C CD1 . ILE   A 1 19  ? 14.25986  -11.08396 -22.97737 1.000 29.57463  ? 26  ILE   A CD1 1 
ATOM   91   N N   . ALA   A 1 20  ? 15.83135  -15.76381 -20.98322 1.000 16.86008  ? 27  ALA   A N   1 
ATOM   92   C CA  . ALA   A 1 20  ? 16.09785  -17.04150 -20.33122 1.000 19.04466  ? 27  ALA   A CA  1 
ATOM   93   C C   . ALA   A 1 20  ? 16.49632  -16.82817 -18.87592 1.000 21.86301  ? 27  ALA   A C   1 
ATOM   94   O O   . ALA   A 1 20  ? 16.10633  -17.59942 -17.99022 1.000 21.29219  ? 27  ALA   A O   1 
ATOM   95   C CB  . ALA   A 1 20  ? 17.19594  -17.79256 -21.08466 1.000 18.51070  ? 27  ALA   A CB  1 
ATOM   96   N N   . GLN   A 1 21  ? 17.26073  -15.76999 -18.61128 1.000 20.97105  ? 28  GLN   A N   1 
ATOM   97   C CA  . GLN   A 1 21  ? 17.67641  -15.47688 -17.24606 1.000 19.96630  ? 28  GLN   A CA  1 
ATOM   98   C C   . GLN   A 1 21  ? 16.48452  -15.07134 -16.38260 1.000 22.38059  ? 28  GLN   A C   1 
ATOM   99   O O   . GLN   A 1 21  ? 16.36908  -15.51822 -15.23495 1.000 22.99394  ? 28  GLN   A O   1 
ATOM   100  C CB  . GLN   A 1 21  ? 18.74560  -14.38546 -17.26449 1.000 25.09080  ? 28  GLN   A CB  1 
ATOM   101  C CG  . GLN   A 1 21  ? 19.27397  -13.98186 -15.90282 1.000 43.51920  ? 28  GLN   A CG  1 
ATOM   102  C CD  . GLN   A 1 21  ? 20.43892  -13.00708 -15.99601 1.000 63.01900  ? 28  GLN   A CD  1 
ATOM   103  O OE1 . GLN   A 1 21  ? 21.18854  -12.82750 -15.03399 1.000 61.68634  ? 28  GLN   A OE1 1 
ATOM   104  N NE2 . GLN   A 1 21  ? 20.61030  -12.39105 -17.16581 1.000 50.61709  ? 28  GLN   A NE2 1 
ATOM   105  N N   . LEU   A 1 22  ? 15.58973  -14.22410 -16.91656 1.000 21.25026  ? 29  LEU   A N   1 
ATOM   106  C CA  . LEU   A 1 22  ? 14.37357  -13.85076 -16.18801 1.000 22.61128  ? 29  LEU   A CA  1 
ATOM   107  C C   . LEU   A 1 22  ? 13.54706  -15.07652 -15.85613 1.000 30.27726  ? 29  LEU   A C   1 
ATOM   108  O O   . LEU   A 1 22  ? 12.99225  -15.20785 -14.75775 1.000 23.54301  ? 29  LEU   A O   1 
ATOM   109  C CB  . LEU   A 1 22  ? 13.53755  -12.87834 -17.02371 1.000 23.00011  ? 29  LEU   A CB  1 
ATOM   110  C CG  . LEU   A 1 22  ? 12.13950  -12.54604 -16.48705 1.000 28.59630  ? 29  LEU   A CG  1 
ATOM   111  C CD1 . LEU   A 1 22  ? 12.23947  -11.66044 -15.26286 1.000 28.16082  ? 29  LEU   A CD1 1 
ATOM   112  C CD2 . LEU   A 1 22  ? 11.29162  -11.88177 -17.55370 1.000 26.66769  ? 29  LEU   A CD2 1 
ATOM   113  N N   . MET   A 1 23  ? 13.47953  -15.99264 -16.80507 1.000 17.68784  ? 30  MET   A N   1 
ATOM   114  C CA  . MET   A 1 23  ? 12.61364  -17.15105 -16.71826 1.000 18.37525  ? 30  MET   A CA  1 
ATOM   115  C C   . MET   A 1 23  ? 13.13912  -18.11459 -15.65031 1.000 19.83517  ? 30  MET   A C   1 
ATOM   116  O O   . MET   A 1 23  ? 12.37400  -18.61376 -14.81668 1.000 20.03323  ? 30  MET   A O   1 
ATOM   117  C CB  . MET   A 1 23  ? 12.61547  -17.71465 -18.13186 1.000 19.86216  ? 30  MET   A CB  1 
ATOM   118  C CG  . MET   A 1 23  ? 11.45556  -17.20953 -18.94066 1.000 16.83233  ? 30  MET   A CG  1 
ATOM   119  S SD  . MET   A 1 23  ? 11.24337  -18.02377 -20.51465 1.000 18.02800  ? 30  MET   A SD  1 
ATOM   120  C CE  . MET   A 1 23  ? 10.09413  -19.35344 -20.18045 1.000 18.09812  ? 30  MET   A CE  1 
ATOM   121  N N   . SER   A 1 24  ? 14.46023  -18.32012 -15.60374 1.000 21.50206  ? 31  SER   A N   1 
ATOM   122  C CA  . SER   A 1 24  ? 15.03205  -19.16359 -14.55628 1.000 17.42882  ? 31  SER   A CA  1 
ATOM   123  C C   . SER   A 1 24  ? 14.91801  -18.50507 -13.18809 1.000 25.06680  ? 31  SER   A C   1 
ATOM   124  O O   . SER   A 1 24  ? 14.70900  -19.19404 -12.18403 1.000 25.76900  ? 31  SER   A O   1 
ATOM   125  C CB  . SER   A 1 24  ? 16.48822  -19.49844 -14.86899 1.000 29.99001  ? 31  SER   A CB  1 
ATOM   126  O OG  . SER   A 1 24  ? 17.17386  -18.39715 -15.42789 1.000 48.10697  ? 31  SER   A OG  1 
ATOM   127  N N   . LEU   A 1 25  ? 15.05687  -17.17553 -13.12298 1.000 21.04863  ? 32  LEU   A N   1 
ATOM   128  C CA  . LEU   A 1 25  ? 14.87774  -16.48469 -11.84763 1.000 22.31385  ? 32  LEU   A CA  1 
ATOM   129  C C   . LEU   A 1 25  ? 13.46262  -16.67976 -11.31810 1.000 29.36999  ? 32  LEU   A C   1 
ATOM   130  O O   . LEU   A 1 25  ? 13.26156  -16.91376 -10.12019 1.000 25.36457  ? 32  LEU   A O   1 
ATOM   131  C CB  . LEU   A 1 25  ? 15.19445  -14.99469 -12.00493 1.000 27.07196  ? 32  LEU   A CB  1 
ATOM   132  C CG  . LEU   A 1 25  ? 15.12916  -14.11989 -10.74421 1.000 29.05268  ? 32  LEU   A CG  1 
ATOM   133  C CD1 . LEU   A 1 25  ? 16.15806  -13.00304 -10.81909 1.000 30.65653  ? 32  LEU   A CD1 1 
ATOM   134  C CD2 . LEU   A 1 25  ? 13.73865  -13.53644 -10.52469 1.000 26.95502  ? 32  LEU   A CD2 1 
ATOM   135  N N   . ILE   A 1 26  ? 12.46649  -16.58220 -12.19720 1.000 21.70666  ? 33  ILE   A N   1 
ATOM   136  C CA  . ILE   A 1 26  ? 11.08479  -16.78131 -11.77003 1.000 24.01312  ? 33  ILE   A CA  1 
ATOM   137  C C   . ILE   A 1 26  ? 10.87876  -18.21298 -11.29192 1.000 26.97813  ? 33  ILE   A C   1 
ATOM   138  O O   . ILE   A 1 26  ? 10.16356  -18.46358 -10.31216 1.000 25.60346  ? 33  ILE   A O   1 
ATOM   139  C CB  . ILE   A 1 26  ? 10.12965  -16.40956 -12.91769 1.000 18.28165  ? 33  ILE   A CB  1 
ATOM   140  C CG1 . ILE   A 1 26  ? 10.11932  -14.89075 -13.08900 1.000 21.69374  ? 33  ILE   A CG1 1 
ATOM   141  C CG2 . ILE   A 1 26  ? 8.72515   -16.95653 -12.65774 1.000 17.74882  ? 33  ILE   A CG2 1 
ATOM   142  C CD1 . ILE   A 1 26  ? 9.44388   -14.40968 -14.35209 1.000 24.44853  ? 33  ILE   A CD1 1 
ATOM   143  N N   . ILE   A 1 27  ? 11.53292  -19.16992 -11.94920 1.000 21.74634  ? 34  ILE   A N   1 
ATOM   144  C CA  . ILE   A 1 27  ? 11.30753  -20.57753 -11.64151 1.000 22.79404  ? 34  ILE   A CA  1 
ATOM   145  C C   . ILE   A 1 27  ? 12.03184  -20.98684 -10.36267 1.000 25.87346  ? 34  ILE   A C   1 
ATOM   146  O O   . ILE   A 1 27  ? 11.51013  -21.77623 -9.56637  1.000 35.74056  ? 34  ILE   A O   1 
ATOM   147  C CB  . ILE   A 1 27  ? 11.73629  -21.44425 -12.84188 1.000 27.75698  ? 34  ILE   A CB  1 
ATOM   148  C CG1 . ILE   A 1 27  ? 10.71964  -21.32347 -13.97623 1.000 24.63901  ? 34  ILE   A CG1 1 
ATOM   149  C CG2 . ILE   A 1 27  ? 11.90278  -22.89898 -12.43849 1.000 25.60370  ? 34  ILE   A CG2 1 
ATOM   150  C CD1 . ILE   A 1 27  ? 11.27424  -21.72771 -15.32482 1.000 18.29029  ? 34  ILE   A CD1 1 
ATOM   151  N N   . ASN   A 1 28  ? 13.23364  -20.45564 -10.13491 1.000 24.14451  ? 35  ASN   A N   1 
ATOM   152  C CA  . ASN   A 1 28  ? 14.09391  -20.96130 -9.07047  1.000 23.39640  ? 35  ASN   A CA  1 
ATOM   153  C C   . ASN   A 1 28  ? 14.07253  -20.13790 -7.78835  1.000 38.69701  ? 35  ASN   A C   1 
ATOM   154  O O   . ASN   A 1 28  ? 14.45484  -20.66381 -6.73770  1.000 39.41128  ? 35  ASN   A O   1 
ATOM   155  C CB  . ASN   A 1 28  ? 15.53574  -21.06292 -9.57050  1.000 30.79198  ? 35  ASN   A CB  1 
ATOM   156  C CG  . ASN   A 1 28  ? 15.66598  -21.98180 -10.75738 1.000 40.81229  ? 35  ASN   A CG  1 
ATOM   157  O OD1 . ASN   A 1 28  ? 15.02344  -23.03077 -10.81435 1.000 37.94940  ? 35  ASN   A OD1 1 
ATOM   158  N ND2 . ASN   A 1 28  ? 16.49083  -21.59225 -11.71989 1.000 47.15362  ? 35  ASN   A ND2 1 
ATOM   159  N N   . THR   A 1 29  ? 13.64694  -18.87832 -7.83104  1.000 24.22246  ? 36  THR   A N   1 
ATOM   160  C CA  . THR   A 1 29  ? 13.67175  -18.05805 -6.62394  1.000 27.74166  ? 36  THR   A CA  1 
ATOM   161  C C   . THR   A 1 29  ? 12.58320  -18.50632 -5.65577  1.000 28.96853  ? 36  THR   A C   1 
ATOM   162  O O   . THR   A 1 29  ? 11.43749  -18.72719 -6.06016  1.000 29.36526  ? 36  THR   A O   1 
ATOM   163  C CB  . THR   A 1 29  ? 13.48271  -16.58189 -6.97577  1.000 30.20411  ? 36  THR   A CB  1 
ATOM   164  O OG1 . THR   A 1 29  ? 14.53489  -16.15859 -7.85029  1.000 30.02983  ? 36  THR   A OG1 1 
ATOM   165  C CG2 . THR   A 1 29  ? 13.50306  -15.72040 -5.71884  1.000 34.78117  ? 36  THR   A CG2 1 
ATOM   166  N N   . PHE   A 1 30  ? 12.93599  -18.64477 -4.37577  1.000 27.04439  ? 37  PHE   A N   1 
ATOM   167  C CA  . PHE   A 1 30  ? 11.91445  -18.91235 -3.37035  1.000 29.67801  ? 37  PHE   A CA  1 
ATOM   168  C C   . PHE   A 1 30  ? 11.06470  -17.66428 -3.16469  1.000 34.12466  ? 37  PHE   A C   1 
ATOM   169  O O   . PHE   A 1 30  ? 11.57869  -16.60803 -2.77478  1.000 28.16275  ? 37  PHE   A O   1 
ATOM   170  C CB  . PHE   A 1 30  ? 12.52644  -19.35716 -2.04609  1.000 27.26500  ? 37  PHE   A CB  1 
ATOM   171  C CG  . PHE   A 1 30  ? 11.49677  -19.62535 -0.98674  1.000 29.49338  ? 37  PHE   A CG  1 
ATOM   172  C CD1 . PHE   A 1 30  ? 10.69620  -20.75425 -1.05207  1.000 36.35779  ? 37  PHE   A CD1 1 
ATOM   173  C CD2 . PHE   A 1 30  ? 11.29572  -18.72858 0.05010   1.000 30.34088  ? 37  PHE   A CD2 1 
ATOM   174  C CE1 . PHE   A 1 30  ? 9.73023   -20.99529 -0.08980  1.000 33.09300  ? 37  PHE   A CE1 1 
ATOM   175  C CE2 . PHE   A 1 30  ? 10.32808  -18.96458 1.01375   1.000 41.01768  ? 37  PHE   A CE2 1 
ATOM   176  C CZ  . PHE   A 1 30  ? 9.54703   -20.10012 0.94423   1.000 31.30184  ? 37  PHE   A CZ  1 
ATOM   177  N N   . TYR   A 1 31  ? 9.76107   -17.79164 -3.40501  1.000 25.27800  ? 38  TYR   A N   1 
ATOM   178  C CA  . TYR   A 1 31  ? 8.87493   -16.63423 -3.37089  1.000 21.30219  ? 38  TYR   A CA  1 
ATOM   179  C C   . TYR   A 1 31  ? 7.44248   -17.14569 -3.27067  1.000 22.46400  ? 38  TYR   A C   1 
ATOM   180  O O   . TYR   A 1 31  ? 6.91112   -17.68873 -4.24403  1.000 23.75003  ? 38  TYR   A O   1 
ATOM   181  C CB  . TYR   A 1 31  ? 9.08430   -15.77470 -4.61076  1.000 22.04135  ? 38  TYR   A CB  1 
ATOM   182  C CG  . TYR   A 1 31  ? 8.08617   -14.66433 -4.74393  1.000 19.56553  ? 38  TYR   A CG  1 
ATOM   183  C CD1 . TYR   A 1 31  ? 8.21406   -13.49968 -3.99464  1.000 26.91668  ? 38  TYR   A CD1 1 
ATOM   184  C CD2 . TYR   A 1 31  ? 7.01182   -14.77650 -5.61684  1.000 28.59800  ? 38  TYR   A CD2 1 
ATOM   185  C CE1 . TYR   A 1 31  ? 7.29443   -12.48306 -4.10682  1.000 34.27762  ? 38  TYR   A CE1 1 
ATOM   186  C CE2 . TYR   A 1 31  ? 6.09192   -13.76377 -5.73705  1.000 30.67079  ? 38  TYR   A CE2 1 
ATOM   187  C CZ  . TYR   A 1 31  ? 6.23856   -12.62304 -4.98420  1.000 31.37032  ? 38  TYR   A CZ  1 
ATOM   188  O OH  . TYR   A 1 31  ? 5.31813   -11.61454 -5.10198  1.000 50.12810  ? 38  TYR   A OH  1 
ATOM   189  N N   . SER   A 1 32  ? 6.82163   -16.95919 -2.10468  1.000 21.44356  ? 39  SER   A N   1 
ATOM   190  C CA  . SER   A 1 32  ? 5.56922   -17.63831 -1.79538  1.000 21.51912  ? 39  SER   A CA  1 
ATOM   191  C C   . SER   A 1 32  ? 4.35418   -16.99103 -2.44433  1.000 25.53099  ? 39  SER   A C   1 
ATOM   192  O O   . SER   A 1 32  ? 3.34668   -17.67681 -2.65221  1.000 27.55404  ? 39  SER   A O   1 
ATOM   193  C CB  . SER   A 1 32  ? 5.36991   -17.69043 -0.28101  1.000 23.26873  ? 39  SER   A CB  1 
ATOM   194  O OG  . SER   A 1 32  ? 6.36580   -18.49635 0.31996   1.000 25.74799  ? 39  SER   A OG  1 
ATOM   195  N N   . ASN   A 1 33  ? 4.43039   -15.70281 -2.77996  1.000 24.00851  ? 40  ASN   A N   1 
ATOM   196  C CA  . ASN   A 1 33  ? 3.27572   -14.92981 -3.24395  1.000 23.84464  ? 40  ASN   A CA  1 
ATOM   197  C C   . ASN   A 1 33  ? 3.01440   -15.15487 -4.74100  1.000 21.38916  ? 40  ASN   A C   1 
ATOM   198  O O   . ASN   A 1 33  ? 2.98340   -14.23489 -5.55904  1.000 19.70732  ? 40  ASN   A O   1 
ATOM   199  C CB  . ASN   A 1 33  ? 3.50832   -13.46100 -2.90946  1.000 31.54092  ? 40  ASN   A CB  1 
ATOM   200  C CG  . ASN   A 1 33  ? 2.35406   -12.57413 -3.30436  1.000 31.15437  ? 40  ASN   A CG  1 
ATOM   201  O OD1 . ASN   A 1 33  ? 1.19243   -12.95659 -3.18847  1.000 27.68825  ? 40  ASN   A OD1 1 
ATOM   202  N ND2 . ASN   A 1 33  ? 2.66955   -11.36199 -3.74067  1.000 27.57509  ? 40  ASN   A ND2 1 
ATOM   203  N N   . LYS   A 1 34  ? 2.78552   -16.42409 -5.09135  1.000 22.00003  ? 41  LYS   A N   1 
ATOM   204  C CA  . LYS   A 1 34  ? 2.68096   -16.80573 -6.49686  1.000 19.25061  ? 41  LYS   A CA  1 
ATOM   205  C C   . LYS   A 1 34  ? 1.38621   -16.34019 -7.15360  1.000 17.65504  ? 41  LYS   A C   1 
ATOM   206  O O   . LYS   A 1 34  ? 1.32868   -16.26300 -8.38788  1.000 17.00798  ? 41  LYS   A O   1 
ATOM   207  C CB  . LYS   A 1 34  ? 2.78278   -18.32236 -6.63937  1.000 17.31989  ? 41  LYS   A CB  1 
ATOM   208  C CG  . LYS   A 1 34  ? 4.13604   -18.93115 -6.30160  1.000 19.45401  ? 41  LYS   A CG  1 
ATOM   209  C CD  . LYS   A 1 34  ? 4.06515   -20.44614 -6.48823  1.000 21.61589  ? 41  LYS   A CD  1 
ATOM   210  C CE  . LYS   A 1 34  ? 5.40770   -21.14157 -6.29308  1.000 18.86945  ? 41  LYS   A CE  1 
ATOM   211  N NZ  . LYS   A 1 34  ? 6.37127   -20.93018 -7.40154  1.000 22.35477  ? 41  LYS   A NZ  1 
ATOM   212  N N   . GLU   A 1 35  ? 0.35394   -16.03110 -6.36619  1.000 19.40360  ? 42  GLU   A N   1 
ATOM   213  C CA  . GLU   A 1 35  ? -0.96931  -15.76222 -6.92466  1.000 17.07760  ? 42  GLU   A CA  1 
ATOM   214  C C   . GLU   A 1 35  ? -0.99464  -14.55727 -7.85468  1.000 20.29057  ? 42  GLU   A C   1 
ATOM   215  O O   . GLU   A 1 35  ? -1.95054  -14.40846 -8.62612  1.000 18.99563  ? 42  GLU   A O   1 
ATOM   216  C CB  . GLU   A 1 35  ? -1.98017  -15.54792 -5.79498  1.000 17.61282  ? 42  GLU   A CB  1 
ATOM   217  C CG  . GLU   A 1 35  ? -1.85514  -14.19721 -5.10174  1.000 17.18634  ? 42  GLU   A CG  1 
ATOM   218  C CD  . GLU   A 1 35  ? -2.72824  -14.08924 -3.85817  1.000 29.24178  ? 42  GLU   A CD  1 
ATOM   219  O OE1 . GLU   A 1 35  ? -2.82036  -15.07731 -3.10459  1.000 31.23543  ? 42  GLU   A OE1 1 
ATOM   220  O OE2 . GLU   A 1 35  ? -3.29467  -13.00446 -3.62206  1.000 33.66489  ? 42  GLU   A OE2 1 
ATOM   221  N N   . ILE   A 1 36  ? 0.01783   -13.68901 -7.79453  1.000 15.63753  ? 43  ILE   A N   1 
ATOM   222  C CA  . ILE   A 1 36  ? 0.03641   -12.49099 -8.62493  1.000 18.99113  ? 43  ILE   A CA  1 
ATOM   223  C C   . ILE   A 1 36  ? 0.13685   -12.80286 -10.10867 1.000 18.41294  ? 43  ILE   A C   1 
ATOM   224  O O   . ILE   A 1 36  ? -0.07285  -11.90157 -10.93100 1.000 19.73572  ? 43  ILE   A O   1 
ATOM   225  C CB  . ILE   A 1 36  ? 1.19548   -11.55847 -8.21301  1.000 19.81098  ? 43  ILE   A CB  1 
ATOM   226  C CG1 . ILE   A 1 36  ? 2.55315   -12.26325 -8.33781  1.000 25.53193  ? 43  ILE   A CG1 1 
ATOM   227  C CG2 . ILE   A 1 36  ? 0.97899   -11.04148 -6.79689  1.000 29.05424  ? 43  ILE   A CG2 1 
ATOM   228  C CD1 . ILE   A 1 36  ? 3.27484   -11.99313 -9.65239  1.000 22.08216  ? 43  ILE   A CD1 1 
ATOM   229  N N   . PHE   A 1 37  ? 0.46422   -14.04700 -10.47838 1.000 15.93857  ? 44  PHE   A N   1 
ATOM   230  C CA  . PHE   A 1 37  ? 0.49335   -14.39496 -11.89617 1.000 16.40281  ? 44  PHE   A CA  1 
ATOM   231  C C   . PHE   A 1 37  ? -0.83845  -14.06932 -12.56122 1.000 18.71768  ? 44  PHE   A C   1 
ATOM   232  O O   . PHE   A 1 37  ? -0.87717  -13.60657 -13.70789 1.000 15.15103  ? 44  PHE   A O   1 
ATOM   233  C CB  . PHE   A 1 37  ? 0.82475   -15.88151 -12.08152 1.000 15.68035  ? 44  PHE   A CB  1 
ATOM   234  C CG  . PHE   A 1 37  ? -0.35941  -16.78398 -11.88674 1.000 16.35705  ? 44  PHE   A CG  1 
ATOM   235  C CD1 . PHE   A 1 37  ? -0.69923  -17.23203 -10.62376 1.000 17.77988  ? 44  PHE   A CD1 1 
ATOM   236  C CD2 . PHE   A 1 37  ? -1.16880  -17.14326 -12.96130 1.000 18.02794  ? 44  PHE   A CD2 1 
ATOM   237  C CE1 . PHE   A 1 37  ? -1.80141  -18.04484 -10.43390 1.000 17.86717  ? 44  PHE   A CE1 1 
ATOM   238  C CE2 . PHE   A 1 37  ? -2.28030  -17.94509 -12.77217 1.000 19.42716  ? 44  PHE   A CE2 1 
ATOM   239  C CZ  . PHE   A 1 37  ? -2.59712  -18.39848 -11.50868 1.000 18.14066  ? 44  PHE   A CZ  1 
ATOM   240  N N   . LEU   A 1 38  ? -1.94817  -14.30458 -11.85616 1.000 17.50756  ? 45  LEU   A N   1 
ATOM   241  C CA  . LEU   A 1 38  ? -3.25006  -14.12403 -12.48585 1.000 16.00459  ? 45  LEU   A CA  1 
ATOM   242  C C   . LEU   A 1 38  ? -3.53002  -12.65021 -12.73507 1.000 15.76159  ? 45  LEU   A C   1 
ATOM   243  O O   . LEU   A 1 38  ? -4.03392  -12.27987 -13.80455 1.000 17.00221  ? 45  LEU   A O   1 
ATOM   244  C CB  . LEU   A 1 38  ? -4.34486  -14.74793 -11.62347 1.000 13.18041  ? 45  LEU   A CB  1 
ATOM   245  C CG  . LEU   A 1 38  ? -5.73496  -14.78557 -12.26436 1.000 16.53568  ? 45  LEU   A CG  1 
ATOM   246  C CD1 . LEU   A 1 38  ? -5.70912  -15.55983 -13.57547 1.000 15.88896  ? 45  LEU   A CD1 1 
ATOM   247  C CD2 . LEU   A 1 38  ? -6.73527  -15.39104 -11.30525 1.000 22.46382  ? 45  LEU   A CD2 1 
ATOM   248  N N   . ARG   A 1 39  ? -3.18070  -11.79178 -11.77188 1.000 16.36353  ? 46  ARG   A N   1 
ATOM   249  C CA  . ARG   A 1 39  ? -3.33903  -10.35597 -11.97373 1.000 17.45965  ? 46  ARG   A CA  1 
ATOM   250  C C   . ARG   A 1 39  ? -2.55218  -9.89393  -13.18989 1.000 17.88886  ? 46  ARG   A C   1 
ATOM   251  O O   . ARG   A 1 39  ? -3.03628  -9.08042  -13.98305 1.000 18.90521  ? 46  ARG   A O   1 
ATOM   252  C CB  . ARG   A 1 39  ? -2.89151  -9.59223  -10.72258 1.000 21.74746  ? 46  ARG   A CB  1 
ATOM   253  C CG  . ARG   A 1 39  ? -2.70183  -8.09875  -10.92374 1.000 26.91778  ? 46  ARG   A CG  1 
ATOM   254  C CD  . ARG   A 1 39  ? -2.01466  -7.44841  -9.72446  1.000 30.02126  ? 46  ARG   A CD  1 
ATOM   255  N NE  . ARG   A 1 39  ? -0.58367  -7.73506  -9.67804  1.000 35.22729  ? 46  ARG   A NE  1 
ATOM   256  C CZ  . ARG   A 1 39  ? 0.17501   -7.61086  -8.59627  1.000 35.42673  ? 46  ARG   A CZ  1 
ATOM   257  N NH1 . ARG   A 1 39  ? -0.33134  -7.22929  -7.43477  1.000 33.37367  ? 46  ARG   A NH1 1 
ATOM   258  N NH2 . ARG   A 1 39  ? 1.47582   -7.87671  -8.68173  1.000 34.77101  ? 46  ARG   A NH2 1 
ATOM   259  N N   . GLU   A 1 40  ? -1.33887  -10.42116 -13.36354 1.000 12.84450  ? 47  GLU   A N   1 
ATOM   260  C CA  . GLU   A 1 40  ? -0.49623  -9.99029  -14.47214 1.000 14.86149  ? 47  GLU   A CA  1 
ATOM   261  C C   . GLU   A 1 40  ? -1.08438  -10.40029 -15.81807 1.000 17.12641  ? 47  GLU   A C   1 
ATOM   262  O O   . GLU   A 1 40  ? -1.04429  -9.62235  -16.77998 1.000 16.23474  ? 47  GLU   A O   1 
ATOM   263  C CB  . GLU   A 1 40  ? 0.91153   -10.56380 -14.29838 1.000 14.45974  ? 47  GLU   A CB  1 
ATOM   264  C CG  . GLU   A 1 40  ? 1.61061   -10.08058 -13.04871 1.000 18.82244  ? 47  GLU   A CG  1 
ATOM   265  C CD  . GLU   A 1 40  ? 1.61557   -8.56533  -12.92191 1.000 26.92007  ? 47  GLU   A CD  1 
ATOM   266  O OE1 . GLU   A 1 40  ? 1.75362   -7.87838  -13.95566 1.000 23.34320  ? 47  GLU   A OE1 1 
ATOM   267  O OE2 . GLU   A 1 40  ? 1.47056   -8.06175  -11.78761 1.000 30.11671  ? 47  GLU   A OE2 1 
ATOM   268  N N   . LEU   A 1 41  ? -1.63333  -11.61498 -15.90964 1.000 15.96865  ? 48  LEU   A N   1 
ATOM   269  C CA  . LEU   A 1 41  ? -2.19485  -12.07223 -17.18025 1.000 16.68756  ? 48  LEU   A CA  1 
ATOM   270  C C   . LEU   A 1 41  ? -3.51326  -11.37555 -17.48813 1.000 16.06419  ? 48  LEU   A C   1 
ATOM   271  O O   . LEU   A 1 41  ? -3.80379  -11.06831 -18.65091 1.000 14.60984  ? 48  LEU   A O   1 
ATOM   272  C CB  . LEU   A 1 41  ? -2.38899  -13.58713 -17.16479 1.000 17.16910  ? 48  LEU   A CB  1 
ATOM   273  C CG  . LEU   A 1 41  ? -1.10777  -14.40751 -17.02336 1.000 14.17536  ? 48  LEU   A CG  1 
ATOM   274  C CD1 . LEU   A 1 41  ? -1.43710  -15.88487 -16.90543 1.000 14.80406  ? 48  LEU   A CD1 1 
ATOM   275  C CD2 . LEU   A 1 41  ? -0.14850  -14.13568 -18.18558 1.000 15.18296  ? 48  LEU   A CD2 1 
ATOM   276  N N   . ILE   A 1 42  ? -4.32971  -11.12842 -16.46446 1.000 14.70201  ? 49  ILE   A N   1 
ATOM   277  C CA  . ILE   A 1 42  ? -5.56436  -10.38122 -16.67627 1.000 17.52350  ? 49  ILE   A CA  1 
ATOM   278  C C   . ILE   A 1 42  ? -5.24555  -8.95881  -17.11748 1.000 17.96429  ? 49  ILE   A C   1 
ATOM   279  O O   . ILE   A 1 42  ? -5.90813  -8.40538  -18.00299 1.000 15.28584  ? 49  ILE   A O   1 
ATOM   280  C CB  . ILE   A 1 42  ? -6.44000  -10.42196 -15.40871 1.000 16.06384  ? 49  ILE   A CB  1 
ATOM   281  C CG1 . ILE   A 1 42  ? -7.05712  -11.81465 -15.25576 1.000 13.92148  ? 49  ILE   A CG1 1 
ATOM   282  C CG2 . ILE   A 1 42  ? -7.54402  -9.35740  -15.46057 1.000 17.53442  ? 49  ILE   A CG2 1 
ATOM   283  C CD1 . ILE   A 1 42  ? -7.72858  -12.06181 -13.90300 1.000 17.19165  ? 49  ILE   A CD1 1 
ATOM   284  N N   . SER   A 1 43  ? -4.19825  -8.35486  -16.54164 1.000 13.74791  ? 50  SER   A N   1 
ATOM   285  C CA  . SER   A 1 43  ? -3.83995  -7.00345  -16.95409 1.000 14.53124  ? 50  SER   A CA  1 
ATOM   286  C C   . SER   A 1 43  ? -3.33781  -6.99302  -18.39515 1.000 18.04037  ? 50  SER   A C   1 
ATOM   287  O O   . SER   A 1 43  ? -3.66642  -6.08455  -19.16617 1.000 15.21828  ? 50  SER   A O   1 
ATOM   288  C CB  . SER   A 1 43  ? -2.80497  -6.41928  -15.98652 1.000 21.89846  ? 50  SER   A CB  1 
ATOM   289  O OG  . SER   A 1 43  ? -2.14228  -5.30017  -16.54348 1.000 29.59440  ? 50  SER   A OG  1 
ATOM   290  N N   . ASN   A 1 44  ? -2.56177  -8.00854  -18.78621 1.000 15.36605  ? 51  ASN   A N   1 
ATOM   291  C CA  . ASN   A 1 44  ? -2.16631  -8.13974  -20.18662 1.000 16.44789  ? 51  ASN   A CA  1 
ATOM   292  C C   . ASN   A 1 44  ? -3.38385  -8.23709  -21.09534 1.000 14.64368  ? 51  ASN   A C   1 
ATOM   293  O O   . ASN   A 1 44  ? -3.42680  -7.60558  -22.15833 1.000 13.67558  ? 51  ASN   A O   1 
ATOM   294  C CB  . ASN   A 1 44  ? -1.28814  -9.37224  -20.37396 1.000 16.53502  ? 51  ASN   A CB  1 
ATOM   295  C CG  . ASN   A 1 44  ? 0.11184   -9.17025  -19.87634 1.000 21.22687  ? 51  ASN   A CG  1 
ATOM   296  O OD1 . ASN   A 1 44  ? 0.50543   -8.06518  -19.49560 1.000 21.30634  ? 51  ASN   A OD1 1 
ATOM   297  N ND2 . ASN   A 1 44  ? 0.88318   -10.24788 -19.87253 1.000 20.48333  ? 51  ASN   A ND2 1 
ATOM   298  N N   . SER   A 1 45  ? -4.37609  -9.04013  -20.69965 1.000 14.62156  ? 52  SER   A N   1 
ATOM   299  C CA  . SER   A 1 45  ? -5.59168  -9.16526  -21.49678 1.000 15.96282  ? 52  SER   A CA  1 
ATOM   300  C C   . SER   A 1 45  ? -6.31871  -7.83131  -21.58615 1.000 12.77448  ? 52  SER   A C   1 
ATOM   301  O O   . SER   A 1 45  ? -6.78982  -7.44110  -22.66321 1.000 14.93738  ? 52  SER   A O   1 
ATOM   302  C CB  . SER   A 1 45  ? -6.51376  -10.23459 -20.89904 1.000 12.13459  ? 52  SER   A CB  1 
ATOM   303  O OG  . SER   A 1 45  ? -5.98502  -11.54769 -21.05701 1.000 14.64119  ? 52  SER   A OG  1 
ATOM   304  N N   . SER   A 1 46  ? -6.41062  -7.11112  -20.46453 1.000 14.62641  ? 53  SER   A N   1 
ATOM   305  C CA  . SER   A 1 46  ? -7.06689  -5.80793  -20.48737 1.000 15.22029  ? 53  SER   A CA  1 
ATOM   306  C C   . SER   A 1 46  ? -6.34542  -4.84565  -21.42560 1.000 16.64360  ? 53  SER   A C   1 
ATOM   307  O O   . SER   A 1 46  ? -6.99047  -4.10262  -22.17612 1.000 16.33539  ? 53  SER   A O   1 
ATOM   308  C CB  . SER   A 1 46  ? -7.13994  -5.23234  -19.07128 1.000 17.34433  ? 53  SER   A CB  1 
ATOM   309  O OG  . SER   A 1 46  ? -7.64020  -3.90641  -19.08877 1.000 19.16058  ? 53  SER   A OG  1 
ATOM   310  N N   . ASP   A 1 47  ? -5.00685  -4.84047  -21.39339 1.000 15.69419  ? 54  ASP   A N   1 
ATOM   311  C CA  . ASP   A 1 47  ? -4.24207  -4.01404  -22.32459 1.000 17.71527  ? 54  ASP   A CA  1 
ATOM   312  C C   . ASP   A 1 47  ? -4.54900  -4.37294  -23.77525 1.000 17.46501  ? 54  ASP   A C   1 
ATOM   313  O O   . ASP   A 1 47  ? -4.66824  -3.48426  -24.62756 1.000 17.65994  ? 54  ASP   A O   1 
ATOM   314  C CB  . ASP   A 1 47  ? -2.74267  -4.15061  -22.05560 1.000 15.14331  ? 54  ASP   A CB  1 
ATOM   315  C CG  . ASP   A 1 47  ? -2.30102  -3.46927  -20.76258 1.000 22.02505  ? 54  ASP   A CG  1 
ATOM   316  O OD1 . ASP   A 1 47  ? -3.08119  -2.67067  -20.19250 1.000 23.00711  ? 54  ASP   A OD1 1 
ATOM   317  O OD2 . ASP   A 1 47  ? -1.15259  -3.71776  -20.32763 1.000 23.46326  ? 54  ASP   A OD2 1 
ATOM   318  N N   . ALA   A 1 48  ? -4.67435  -5.67202  -24.07742 1.000 13.68369  ? 55  ALA   A N   1 
ATOM   319  C CA  . ALA   A 1 48  ? -4.94488  -6.09644  -25.44994 1.000 13.06540  ? 55  ALA   A CA  1 
ATOM   320  C C   . ALA   A 1 48  ? -6.35591  -5.71463  -25.87913 1.000 15.89149  ? 55  ALA   A C   1 
ATOM   321  O O   . ALA   A 1 48  ? -6.58976  -5.37909  -27.04510 1.000 16.43390  ? 55  ALA   A O   1 
ATOM   322  C CB  . ALA   A 1 48  ? -4.73460  -7.60805  -25.58565 1.000 12.99815  ? 55  ALA   A CB  1 
ATOM   323  N N   . LEU   A 1 49  ? -7.31357  -5.77885  -24.95471 1.000 13.54820  ? 56  LEU   A N   1 
ATOM   324  C CA  . LEU   A 1 49  ? -8.66738  -5.33370  -25.26595 1.000 14.99526  ? 56  LEU   A CA  1 
ATOM   325  C C   . LEU   A 1 49  ? -8.71955  -3.82762  -25.48626 1.000 16.91445  ? 56  LEU   A C   1 
ATOM   326  O O   . LEU   A 1 49  ? -9.44832  -3.35363  -26.36823 1.000 15.99374  ? 56  LEU   A O   1 
ATOM   327  C CB  . LEU   A 1 49  ? -9.61438  -5.75666  -24.14514 1.000 15.85020  ? 56  LEU   A CB  1 
ATOM   328  C CG  . LEU   A 1 49  ? -9.84398  -7.26724  -24.09485 1.000 15.54666  ? 56  LEU   A CG  1 
ATOM   329  C CD1 . LEU   A 1 49  ? -10.19289 -7.71923  -22.68734 1.000 18.87151  ? 56  LEU   A CD1 1 
ATOM   330  C CD2 . LEU   A 1 49  ? -10.94358 -7.67701  -25.08636 1.000 14.49680  ? 56  LEU   A CD2 1 
ATOM   331  N N   . ASP   A 1 50  ? -7.96122  -3.06119  -24.69243 1.000 16.38528  ? 57  ASP   A N   1 
ATOM   332  C CA  . ASP   A 1 50  ? -7.87880  -1.61702  -24.90612 1.000 16.87800  ? 57  ASP   A CA  1 
ATOM   333  C C   . ASP   A 1 50  ? -7.41979  -1.30162  -26.32516 1.000 15.04797  ? 57  ASP   A C   1 
ATOM   334  O O   . ASP   A 1 50  ? -7.92947  -0.37258  -26.96158 1.000 17.84855  ? 57  ASP   A O   1 
ATOM   335  C CB  . ASP   A 1 50  ? -6.90271  -0.97292  -23.91652 1.000 15.28724  ? 57  ASP   A CB  1 
ATOM   336  C CG  . ASP   A 1 50  ? -7.43274  -0.88310  -22.49745 1.000 19.08996  ? 57  ASP   A CG  1 
ATOM   337  O OD1 . ASP   A 1 50  ? -8.60975  -1.20933  -22.22509 1.000 20.87023  ? 57  ASP   A OD1 1 
ATOM   338  O OD2 . ASP   A 1 50  ? -6.64262  -0.44736  -21.63609 1.000 20.68329  ? 57  ASP   A OD2 1 
ATOM   339  N N   . LYS   A 1 51  ? -6.43693  -2.05763  -26.82510 1.000 14.80103  ? 58  LYS   A N   1 
ATOM   340  C CA  . LYS   A 1 51  ? -5.85578  -1.76765  -28.13325 1.000 15.57188  ? 58  LYS   A CA  1 
ATOM   341  C C   . LYS   A 1 51  ? -6.86643  -1.97632  -29.24955 1.000 20.28072  ? 58  LYS   A C   1 
ATOM   342  O O   . LYS   A 1 51  ? -6.99032  -1.14147  -30.15176 1.000 18.07891  ? 58  LYS   A O   1 
ATOM   343  C CB  . LYS   A 1 51  ? -4.61842  -2.64333  -28.36127 1.000 17.64589  ? 58  LYS   A CB  1 
ATOM   344  C CG  . LYS   A 1 51  ? -3.43730  -2.27773  -27.47552 1.000 18.95993  ? 58  LYS   A CG  1 
ATOM   345  C CD  . LYS   A 1 51  ? -2.26317  -3.23175  -27.69650 1.000 20.17891  ? 58  LYS   A CD  1 
ATOM   346  C CE  . LYS   A 1 51  ? -1.16860  -3.02505  -26.65318 1.000 24.33133  ? 58  LYS   A CE  1 
ATOM   347  N NZ  . LYS   A 1 51  ? -0.00275  -3.93604  -26.89606 1.000 33.47230  ? 58  LYS   A NZ  1 
ATOM   348  N N   . ILE   A 1 52  ? -7.59308  -3.09148  -29.21974 1.000 16.11566  ? 59  ILE   A N   1 
ATOM   349  C CA  . ILE   A 1 52  ? -8.54580  -3.32302  -30.29920 1.000 15.79593  ? 59  ILE   A CA  1 
ATOM   350  C C   . ILE   A 1 52  ? -9.73055  -2.37883  -30.16671 1.000 19.27167  ? 59  ILE   A C   1 
ATOM   351  O O   . ILE   A 1 52  ? -10.29044 -1.93786  -31.17765 1.000 18.11872  ? 59  ILE   A O   1 
ATOM   352  C CB  . ILE   A 1 52  ? -8.97555  -4.80278  -30.35522 1.000 19.16891  ? 59  ILE   A CB  1 
ATOM   353  C CG1 . ILE   A 1 52  ? -9.77505  -5.08470  -31.63454 1.000 22.67444  ? 59  ILE   A CG1 1 
ATOM   354  C CG2 . ILE   A 1 52  ? -9.75955  -5.20605  -29.12005 1.000 17.35409  ? 59  ILE   A CG2 1 
ATOM   355  C CD1 . ILE   A 1 52  ? -9.02068  -4.77080  -32.92091 1.000 21.78285  ? 59  ILE   A CD1 1 
ATOM   356  N N   . ARG   A 1 53  ? -10.11443 -2.01408  -28.93885 1.000 16.57362  ? 60  ARG   A N   1 
ATOM   357  C CA  . ARG   A 1 53  ? -11.17268 -1.01772  -28.80236 1.000 18.15241  ? 60  ARG   A CA  1 
ATOM   358  C C   . ARG   A 1 53  ? -10.74961 0.31370   -29.40615 1.000 22.27909  ? 60  ARG   A C   1 
ATOM   359  O O   . ARG   A 1 53  ? -11.52611 0.94711   -30.13211 1.000 20.09726  ? 60  ARG   A O   1 
ATOM   360  C CB  . ARG   A 1 53  ? -11.57598 -0.82868  -27.34171 1.000 16.55439  ? 60  ARG   A CB  1 
ATOM   361  C CG  . ARG   A 1 53  ? -12.77549 0.10895   -27.22397 1.000 25.51259  ? 60  ARG   A CG  1 
ATOM   362  C CD  . ARG   A 1 53  ? -13.13445 0.42465   -25.79601 1.000 42.61212  ? 60  ARG   A CD  1 
ATOM   363  N NE  . ARG   A 1 53  ? -14.22428 -0.41197  -25.31166 1.000 40.85157  ? 60  ARG   A NE  1 
ATOM   364  C CZ  . ARG   A 1 53  ? -14.28439 -0.91408  -24.08722 1.000 46.92761  ? 60  ARG   A CZ  1 
ATOM   365  N NH1 . ARG   A 1 53  ? -13.32735 -0.68766  -23.20157 1.000 30.50669  ? 60  ARG   A NH1 1 
ATOM   366  N NH2 . ARG   A 1 53  ? -15.33424 -1.65251  -23.73938 1.000 32.66808  ? 60  ARG   A NH2 1 
ATOM   367  N N   . TYR   A 1 54  ? -9.51282  0.74530   -29.14135 1.000 17.09732  ? 61  TYR   A N   1 
ATOM   368  C CA  . TYR   A 1 54  ? -9.05398  2.01396   -29.69744 1.000 20.34667  ? 61  TYR   A CA  1 
ATOM   369  C C   . TYR   A 1 54  ? -9.04526  1.97345   -31.22054 1.000 21.93068  ? 61  TYR   A C   1 
ATOM   370  O O   . TYR   A 1 54  ? -9.47968  2.92764   -31.87666 1.000 21.66835  ? 61  TYR   A O   1 
ATOM   371  C CB  . TYR   A 1 54  ? -7.66420  2.37211   -29.16750 1.000 20.40437  ? 61  TYR   A CB  1 
ATOM   372  C CG  . TYR   A 1 54  ? -7.19558  3.71012   -29.69701 1.000 24.24476  ? 61  TYR   A CG  1 
ATOM   373  C CD1 . TYR   A 1 54  ? -7.71442  4.89679   -29.19044 1.000 21.22686  ? 61  TYR   A CD1 1 
ATOM   374  C CD2 . TYR   A 1 54  ? -6.27226  3.78678   -30.73307 1.000 22.48812  ? 61  TYR   A CD2 1 
ATOM   375  C CE1 . TYR   A 1 54  ? -7.30702  6.12402   -29.68243 1.000 23.71233  ? 61  TYR   A CE1 1 
ATOM   376  C CE2 . TYR   A 1 54  ? -5.85953  5.01275   -31.23594 1.000 22.95605  ? 61  TYR   A CE2 1 
ATOM   377  C CZ  . TYR   A 1 54  ? -6.38150  6.17621   -30.70433 1.000 24.55924  ? 61  TYR   A CZ  1 
ATOM   378  O OH  . TYR   A 1 54  ? -5.98582  7.39990   -31.19426 1.000 28.97703  ? 61  TYR   A OH  1 
ATOM   379  N N   . GLU   A 1 55  ? -8.55554  0.87813   -31.80557 1.000 18.22143  ? 62  GLU   A N   1 
ATOM   380  C CA  . GLU   A 1 55  ? -8.55629  0.77863   -33.26303 1.000 19.91674  ? 62  GLU   A CA  1 
ATOM   381  C C   . GLU   A 1 55  ? -9.97364  0.82595   -33.81776 1.000 22.65983  ? 62  GLU   A C   1 
ATOM   382  O O   . GLU   A 1 55  ? -10.21541 1.42019   -34.87449 1.000 26.52895  ? 62  GLU   A O   1 
ATOM   383  C CB  . GLU   A 1 55  ? -7.84834  -0.50070  -33.70147 1.000 20.66537  ? 62  GLU   A CB  1 
ATOM   384  C CG  . GLU   A 1 55  ? -6.35159  -0.43496  -33.50213 1.000 26.00124  ? 62  GLU   A CG  1 
ATOM   385  C CD  . GLU   A 1 55  ? -5.62959  -1.53198  -34.24316 1.000 38.94452  ? 62  GLU   A CD  1 
ATOM   386  O OE1 . GLU   A 1 55  ? -6.31635  -2.43168  -34.76643 1.000 29.16639  ? 62  GLU   A OE1 1 
ATOM   387  O OE2 . GLU   A 1 55  ? -4.38288  -1.49963  -34.30082 1.000 33.94304  ? 62  GLU   A OE2 1 
ATOM   388  N N   . SER   A 1 56  ? -10.93208 0.22860   -33.10673 1.000 22.66472  ? 63  SER   A N   1 
ATOM   389  C CA  . SER   A 1 56  ? -12.30924 0.22346   -33.59212 1.000 24.86076  ? 63  SER   A CA  1 
ATOM   390  C C   . SER   A 1 56  ? -12.95922 1.60021   -33.53908 1.000 24.43602  ? 63  SER   A C   1 
ATOM   391  O O   . SER   A 1 56  ? -13.99069 1.80527   -34.18277 1.000 23.84176  ? 63  SER   A O   1 
ATOM   392  C CB  . SER   A 1 56  ? -13.15386 -0.76985  -32.78937 1.000 26.81617  ? 63  SER   A CB  1 
ATOM   393  O OG  . SER   A 1 56  ? -13.50055 -0.24196  -31.51724 1.000 25.81790  ? 63  SER   A OG  1 
ATOM   394  N N   . LEU   A 1 57  ? -12.39382 2.54824   -32.78857 1.000 24.20052  ? 64  LEU   A N   1 
ATOM   395  C CA  . LEU   A 1 57  ? -13.02345 3.86240   -32.69460 1.000 23.30050  ? 64  LEU   A CA  1 
ATOM   396  C C   . LEU   A 1 57  ? -13.02668 4.58436   -34.03101 1.000 27.98160  ? 64  LEU   A C   1 
ATOM   397  O O   . LEU   A 1 57  ? -13.93190 5.37976   -34.30312 1.000 33.21305  ? 64  LEU   A O   1 
ATOM   398  C CB  . LEU   A 1 57  ? -12.31721 4.72078   -31.64569 1.000 22.88995  ? 64  LEU   A CB  1 
ATOM   399  C CG  . LEU   A 1 57  ? -12.42506 4.22369   -30.20698 1.000 26.80472  ? 64  LEU   A CG  1 
ATOM   400  C CD1 . LEU   A 1 57  ? -11.79489 5.24785   -29.27638 1.000 27.47504  ? 64  LEU   A CD1 1 
ATOM   401  C CD2 . LEU   A 1 57  ? -13.87022 3.94618   -29.82591 1.000 25.18255  ? 64  LEU   A CD2 1 
ATOM   402  N N   . THR   A 1 58  ? -12.02557 4.33768   -34.86982 1.000 24.78122  ? 65  THR   A N   1 
ATOM   403  C CA  . THR   A 1 58  ? -11.96170 4.95606   -36.18545 1.000 29.01496  ? 65  THR   A CA  1 
ATOM   404  C C   . THR   A 1 58  ? -12.20720 3.97738   -37.32270 1.000 37.31962  ? 65  THR   A C   1 
ATOM   405  O O   . THR   A 1 58  ? -12.37873 4.41541   -38.46528 1.000 36.45027  ? 65  THR   A O   1 
ATOM   406  C CB  . THR   A 1 58  ? -10.60078 5.63461   -36.39797 1.000 42.39683  ? 65  THR   A CB  1 
ATOM   407  O OG1 . THR   A 1 58  ? -9.56613  4.64372   -36.38827 1.000 36.00342  ? 65  THR   A OG1 1 
ATOM   408  C CG2 . THR   A 1 58  ? -10.33407 6.66565   -35.31559 1.000 39.97117  ? 65  THR   A CG2 1 
ATOM   409  N N   . ASP   A 1 59  ? -12.23184 2.67570   -37.04331 1.000 34.14607  ? 66  ASP   A N   1 
ATOM   410  C CA  . ASP   A 1 59  ? -12.45602 1.65264   -38.06276 1.000 33.35701  ? 66  ASP   A CA  1 
ATOM   411  C C   . ASP   A 1 59  ? -13.29260 0.54914   -37.43623 1.000 23.64519  ? 66  ASP   A C   1 
ATOM   412  O O   . ASP   A 1 59  ? -12.75720 -0.41417  -36.87187 1.000 26.62049  ? 66  ASP   A O   1 
ATOM   413  C CB  . ASP   A 1 59  ? -11.13359 1.10705   -38.60162 1.000 30.24627  ? 66  ASP   A CB  1 
ATOM   414  C CG  . ASP   A 1 59  ? -11.32700 0.09125   -39.71148 1.000 38.55573  ? 66  ASP   A CG  1 
ATOM   415  O OD1 . ASP   A 1 59  ? -12.48003 -0.12459  -40.13627 1.000 38.69688  ? 66  ASP   A OD1 1 
ATOM   416  O OD2 . ASP   A 1 59  ? -10.32072 -0.49363  -40.16385 1.000 33.09804  ? 66  ASP   A OD2 1 
ATOM   417  N N   . PRO   A 1 60  ? -14.62202 0.66185   -37.50193 1.000 31.26606  ? 67  PRO   A N   1 
ATOM   418  C CA  . PRO   A 1 60  ? -15.47627 -0.37453  -36.89752 1.000 31.31976  ? 67  PRO   A CA  1 
ATOM   419  C C   . PRO   A 1 60  ? -15.27142 -1.75852  -37.49056 1.000 33.05010  ? 67  PRO   A C   1 
ATOM   420  O O   . PRO   A 1 60  ? -15.56903 -2.75009  -36.81400 1.000 33.35811  ? 67  PRO   A O   1 
ATOM   421  C CB  . PRO   A 1 60  ? -16.90497 0.13041   -37.15248 1.000 34.41941  ? 67  PRO   A CB  1 
ATOM   422  C CG  . PRO   A 1 60  ? -16.78773 1.39270   -37.91902 1.000 49.02730  ? 67  PRO   A CG  1 
ATOM   423  C CD  . PRO   A 1 60  ? -15.37541 1.85014   -37.93108 1.000 34.12558  ? 67  PRO   A CD  1 
ATOM   424  N N   . SER   A 1 61  ? -14.77394 -1.86719  -38.72717 1.000 32.27359  ? 68  SER   A N   1 
ATOM   425  C CA  . SER   A 1 61  ? -14.55482 -3.18725  -39.30766 1.000 27.56370  ? 68  SER   A CA  1 
ATOM   426  C C   . SER   A 1 61  ? -13.51153 -3.98509  -38.53725 1.000 31.53571  ? 68  SER   A C   1 
ATOM   427  O O   . SER   A 1 61  ? -13.42795 -5.20404  -38.71186 1.000 25.20546  ? 68  SER   A O   1 
ATOM   428  C CB  . SER   A 1 61  ? -14.13516 -3.07048  -40.77268 1.000 26.64966  ? 68  SER   A CB  1 
ATOM   429  O OG  . SER   A 1 61  ? -12.81754 -2.56812  -40.89024 1.000 33.73748  ? 68  SER   A OG  1 
ATOM   430  N N   . LYS   A 1 62  ? -12.71545 -3.33240  -37.68542 1.000 22.82282  ? 69  LYS   A N   1 
ATOM   431  C CA  . LYS   A 1 62  ? -11.75895 -4.07007  -36.87169 1.000 24.02764  ? 69  LYS   A CA  1 
ATOM   432  C C   . LYS   A 1 62  ? -12.44691 -5.06337  -35.94314 1.000 24.53528  ? 69  LYS   A C   1 
ATOM   433  O O   . LYS   A 1 62  ? -11.80180 -6.00086  -35.46137 1.000 22.57433  ? 69  LYS   A O   1 
ATOM   434  C CB  . LYS   A 1 62  ? -10.90544 -3.09589  -36.05807 1.000 25.36340  ? 69  LYS   A CB  1 
ATOM   435  C CG  . LYS   A 1 62  ? -10.05170 -2.17431  -36.91127 1.000 36.42838  ? 69  LYS   A CG  1 
ATOM   436  C CD  . LYS   A 1 62  ? -8.61395  -2.65847  -36.96849 1.000 28.69420  ? 69  LYS   A CD  1 
ATOM   437  C CE  . LYS   A 1 62  ? -7.78444  -1.82514  -37.93408 1.000 31.06344  ? 69  LYS   A CE  1 
ATOM   438  N NZ  . LYS   A 1 62  ? -6.34749  -2.22323  -37.88967 1.000 39.51810  ? 69  LYS   A NZ  1 
ATOM   439  N N   . LEU   A 1 63  ? -13.73667 -4.87950  -35.67630 1.000 23.78312  ? 70  LEU   A N   1 
ATOM   440  C CA  . LEU   A 1 63  ? -14.49061 -5.78271  -34.82007 1.000 25.36989  ? 70  LEU   A CA  1 
ATOM   441  C C   . LEU   A 1 63  ? -15.29156 -6.80805  -35.61243 1.000 26.53117  ? 70  LEU   A C   1 
ATOM   442  O O   . LEU   A 1 63  ? -16.10449 -7.52641  -35.02538 1.000 24.17621  ? 70  LEU   A O   1 
ATOM   443  C CB  . LEU   A 1 63  ? -15.41630 -4.98402  -33.89597 1.000 29.55571  ? 70  LEU   A CB  1 
ATOM   444  C CG  . LEU   A 1 63  ? -14.72110 -4.07375  -32.87913 1.000 25.65473  ? 70  LEU   A CG  1 
ATOM   445  C CD1 . LEU   A 1 63  ? -15.72923 -3.37261  -31.98136 1.000 26.06397  ? 70  LEU   A CD1 1 
ATOM   446  C CD2 . LEU   A 1 63  ? -13.72845 -4.87541  -32.04234 1.000 20.07235  ? 70  LEU   A CD2 1 
ATOM   447  N N   . ASP   A 1 64  ? -15.07557 -6.89964  -36.92888 1.000 22.29613  ? 71  ASP   A N   1 
ATOM   448  C CA  . ASP   A 1 64  ? -15.76228 -7.92014  -37.72040 1.000 28.52651  ? 71  ASP   A CA  1 
ATOM   449  C C   . ASP   A 1 64  ? -15.41075 -9.32172  -37.24527 1.000 27.45728  ? 71  ASP   A C   1 
ATOM   450  O O   . ASP   A 1 64  ? -16.20067 -10.25695 -37.41780 1.000 29.56494  ? 71  ASP   A O   1 
ATOM   451  C CB  . ASP   A 1 64  ? -15.41103 -7.78017  -39.20241 1.000 26.51555  ? 71  ASP   A CB  1 
ATOM   452  C CG  . ASP   A 1 64  ? -16.10562 -6.60599  -39.87005 1.000 38.80834  ? 71  ASP   A CG  1 
ATOM   453  O OD1 . ASP   A 1 64  ? -16.91808 -5.92126  -39.21421 1.000 38.87909  ? 71  ASP   A OD1 1 
ATOM   454  O OD2 . ASP   A 1 64  ? -15.83845 -6.37345  -41.06525 1.000 36.10113  ? 71  ASP   A OD2 1 
ATOM   455  N N   . SER   A 1 65  ? -14.23075 -9.48286  -36.66522 1.000 26.06058  ? 72  SER   A N   1 
ATOM   456  C CA  . SER   A 1 65  ? -13.75522 -10.73188 -36.09084 1.000 24.41839  ? 72  SER   A CA  1 
ATOM   457  C C   . SER   A 1 65  ? -14.29496 -10.98581 -34.69036 1.000 28.38868  ? 72  SER   A C   1 
ATOM   458  O O   . SER   A 1 65  ? -13.83242 -11.91645 -34.02309 1.000 30.95580  ? 72  SER   A O   1 
ATOM   459  C CB  . SER   A 1 65  ? -12.22619 -10.72196 -36.06176 1.000 25.67464  ? 72  SER   A CB  1 
ATOM   460  O OG  . SER   A 1 65  ? -11.75535 -9.51341  -35.47604 1.000 22.68449  ? 72  SER   A OG  1 
ATOM   461  N N   . GLY   A 1 66  ? -15.24477 -10.17844 -34.22617 1.000 27.89486  ? 73  GLY   A N   1 
ATOM   462  C CA  . GLY   A 1 66  ? -15.82450 -10.36654 -32.91239 1.000 28.70263  ? 73  GLY   A CA  1 
ATOM   463  C C   . GLY   A 1 66  ? -16.06354 -9.05458  -32.19683 1.000 28.37809  ? 73  GLY   A C   1 
ATOM   464  O O   . GLY   A 1 66  ? -15.12078 -8.30838  -31.92958 1.000 22.22547  ? 73  GLY   A O   1 
ATOM   465  N N   . LYS   A 1 67  ? -17.31814 -8.74740  -31.88328 1.000 24.69544  ? 74  LYS   A N   1 
ATOM   466  C CA  . LYS   A 1 67  ? -17.61508 -7.48448  -31.22457 1.000 21.63118  ? 74  LYS   A CA  1 
ATOM   467  C C   . LYS   A 1 67  ? -17.47447 -7.53978  -29.71073 1.000 28.21127  ? 74  LYS   A C   1 
ATOM   468  O O   . LYS   A 1 67  ? -17.30559 -6.48798  -29.08322 1.000 25.92318  ? 74  LYS   A O   1 
ATOM   469  C CB  . LYS   A 1 67  ? -19.03141 -7.02691  -31.57565 1.000 24.71706  ? 74  LYS   A CB  1 
ATOM   470  C CG  . LYS   A 1 67  ? -19.17985 -6.59906  -33.01334 1.000 39.70837  ? 74  LYS   A CG  1 
ATOM   471  C CD  . LYS   A 1 67  ? -20.63572 -6.58243  -33.41352 1.000 46.20547  ? 74  LYS   A CD  1 
ATOM   472  C CE  . LYS   A 1 67  ? -20.99473 -5.28801  -34.10717 1.000 69.87872  ? 74  LYS   A CE  1 
ATOM   473  N NZ  . LYS   A 1 67  ? -22.34269 -5.37173  -34.73884 1.000 70.56772  ? 74  LYS   A NZ  1 
ATOM   474  N N   . GLU   A 1 68  ? -17.54418 -8.72351  -29.10913 1.000 22.41296  ? 75  GLU   A N   1 
ATOM   475  C CA  . GLU   A 1 68  ? -17.52126 -8.82953  -27.65777 1.000 24.23450  ? 75  GLU   A CA  1 
ATOM   476  C C   . GLU   A 1 68  ? -16.09819 -8.65600  -27.14423 1.000 25.29763  ? 75  GLU   A C   1 
ATOM   477  O O   . GLU   A 1 68  ? -15.15882 -9.25856  -27.67257 1.000 25.08744  ? 75  GLU   A O   1 
ATOM   478  C CB  . GLU   A 1 68  ? -18.08780 -10.17410 -27.19730 1.000 25.23703  ? 75  GLU   A CB  1 
ATOM   479  C CG  . GLU   A 1 68  ? -19.59836 -10.34243 -27.37912 1.000 30.51065  ? 75  GLU   A CG  1 
ATOM   480  C CD  . GLU   A 1 68  ? -20.02215 -10.40911 -28.83629 1.000 68.82031  ? 75  GLU   A CD  1 
ATOM   481  O OE1 . GLU   A 1 68  ? -19.37807 -11.15738 -29.60508 1.000 67.50266  ? 75  GLU   A OE1 1 
ATOM   482  O OE2 . GLU   A 1 68  ? -20.99831 -9.71958  -29.21095 1.000 55.58383  ? 75  GLU   A OE2 1 
ATOM   483  N N   . LEU   A 1 69  ? -15.94529 -7.83550  -26.11004 1.000 18.30869  ? 76  LEU   A N   1 
ATOM   484  C CA  . LEU   A 1 69  ? -14.64489 -7.53159  -25.51060 1.000 16.70067  ? 76  LEU   A CA  1 
ATOM   485  C C   . LEU   A 1 69  ? -14.67833 -8.05456  -24.07742 1.000 15.03765  ? 76  LEU   A C   1 
ATOM   486  O O   . LEU   A 1 69  ? -15.31197 -7.44608  -23.20833 1.000 18.98143  ? 76  LEU   A O   1 
ATOM   487  C CB  . LEU   A 1 69  ? -14.38019 -6.02930  -25.55881 1.000 25.18716  ? 76  LEU   A CB  1 
ATOM   488  C CG  . LEU   A 1 69  ? -14.27172 -5.38737  -26.94552 1.000 25.45279  ? 76  LEU   A CG  1 
ATOM   489  C CD1 . LEU   A 1 69  ? -13.82959 -3.93947  -26.81716 1.000 31.64336  ? 76  LEU   A CD1 1 
ATOM   490  C CD2 . LEU   A 1 69  ? -13.29896 -6.16058  -27.82623 1.000 20.92395  ? 76  LEU   A CD2 1 
ATOM   491  N N   . HIS   A 1 70  ? -14.01980 -9.18457  -23.81997 1.000 15.36601  ? 77  HIS   A N   1 
ATOM   492  C CA  . HIS   A 1 70  ? -14.19177 -9.83473  -22.52669 1.000 19.57720  ? 77  HIS   A CA  1 
ATOM   493  C C   . HIS   A 1 70  ? -13.00050 -10.72747 -22.21456 1.000 13.08679  ? 77  HIS   A C   1 
ATOM   494  O O   . HIS   A 1 70  ? -12.15420 -11.00694 -23.06851 1.000 14.33394  ? 77  HIS   A O   1 
ATOM   495  C CB  . HIS   A 1 70  ? -15.48127 -10.65978 -22.48778 1.000 18.64673  ? 77  HIS   A CB  1 
ATOM   496  C CG  . HIS   A 1 70  ? -15.50445 -11.79467 -23.46735 1.000 21.97688  ? 77  HIS   A CG  1 
ATOM   497  N ND1 . HIS   A 1 70  ? -16.49159 -11.93661 -24.41677 1.000 25.21767  ? 77  HIS   A ND1 1 
ATOM   498  C CD2 . HIS   A 1 70  ? -14.67497 -12.85369 -23.62880 1.000 22.85125  ? 77  HIS   A CD2 1 
ATOM   499  C CE1 . HIS   A 1 70  ? -16.26274 -13.02451 -25.13028 1.000 24.66234  ? 77  HIS   A CE1 1 
ATOM   500  N NE2 . HIS   A 1 70  ? -15.16618 -13.59972 -24.67254 1.000 21.92200  ? 77  HIS   A NE2 1 
ATOM   501  N N   . ILE   A 1 71  ? -12.97416 -11.19111 -20.96531 1.000 15.96503  ? 78  ILE   A N   1 
ATOM   502  C CA  . ILE   A 1 71  ? -11.94392 -12.07009 -20.42965 1.000 15.46534  ? 78  ILE   A CA  1 
ATOM   503  C C   . ILE   A 1 71  ? -12.63595 -13.25943 -19.78310 1.000 17.07248  ? 78  ILE   A C   1 
ATOM   504  O O   . ILE   A 1 71  ? -13.51796 -13.07230 -18.93818 1.000 15.74074  ? 78  ILE   A O   1 
ATOM   505  C CB  . ILE   A 1 71  ? -11.07050 -11.35113 -19.38299 1.000 13.16635  ? 78  ILE   A CB  1 
ATOM   506  C CG1 . ILE   A 1 71  ? -10.48211 -10.05815 -19.95110 1.000 15.58726  ? 78  ILE   A CG1 1 
ATOM   507  C CG2 . ILE   A 1 71  ? -9.98102  -12.30569 -18.86551 1.000 13.67722  ? 78  ILE   A CG2 1 
ATOM   508  C CD1 . ILE   A 1 71  ? -9.70538  -9.24798  -18.92467 1.000 17.03962  ? 78  ILE   A CD1 1 
ATOM   509  N N   . ASN   A 1 72  ? -12.23654 -14.47303 -20.16974 1.000 16.04922  ? 79  ASN   A N   1 
ATOM   510  C CA  . ASN   A 1 72  ? -12.74730 -15.69728 -19.57076 1.000 17.47373  ? 79  ASN   A CA  1 
ATOM   511  C C   . ASN   A 1 72  ? -11.62991 -16.44321 -18.85495 1.000 18.02448  ? 79  ASN   A C   1 
ATOM   512  O O   . ASN   A 1 72  ? -10.51025 -16.55425 -19.36682 1.000 16.09454  ? 79  ASN   A O   1 
ATOM   513  C CB  . ASN   A 1 72  ? -13.38072 -16.61923 -20.61598 1.000 15.77098  ? 79  ASN   A CB  1 
ATOM   514  C CG  . ASN   A 1 72  ? -14.59401 -16.00789 -21.26550 1.000 17.37742  ? 79  ASN   A CG  1 
ATOM   515  O OD1 . ASN   A 1 72  ? -15.31523 -15.23098 -20.64114 1.000 17.83290  ? 79  ASN   A OD1 1 
ATOM   516  N ND2 . ASN   A 1 72  ? -14.84613 -16.37467 -22.51775 1.000 20.89094  ? 79  ASN   A ND2 1 
ATOM   517  N N   . LEU   A 1 73  ? -11.94843 -16.97224 -17.67866 1.000 15.60022  ? 80  LEU   A N   1 
ATOM   518  C CA  . LEU   A 1 73  ? -11.04022 -17.81800 -16.91325 1.000 13.53396  ? 80  LEU   A CA  1 
ATOM   519  C C   . LEU   A 1 73  ? -11.62310 -19.22347 -16.89541 1.000 17.58798  ? 80  LEU   A C   1 
ATOM   520  O O   . LEU   A 1 73  ? -12.73170 -19.42598 -16.39251 1.000 14.97332  ? 80  LEU   A O   1 
ATOM   521  C CB  . LEU   A 1 73  ? -10.88068 -17.28595 -15.48908 1.000 15.01684  ? 80  LEU   A CB  1 
ATOM   522  C CG  . LEU   A 1 73  ? -10.53329 -15.80367 -15.35927 1.000 18.23841  ? 80  LEU   A CG  1 
ATOM   523  C CD1 . LEU   A 1 73  ? -10.48519 -15.41877 -13.90012 1.000 14.41308  ? 80  LEU   A CD1 1 
ATOM   524  C CD2 . LEU   A 1 73  ? -9.20069  -15.49635 -16.03580 1.000 15.10325  ? 80  LEU   A CD2 1 
ATOM   525  N N   . ILE   A 1 74  ? -10.89881 -20.18657 -17.45411 1.000 13.64213  ? 81  ILE   A N   1 
ATOM   526  C CA  . ILE   A 1 74  ? -11.40734 -21.53690 -17.64149 1.000 16.23956  ? 81  ILE   A CA  1 
ATOM   527  C C   . ILE   A 1 74  ? -10.47296 -22.51804 -16.95158 1.000 16.83842  ? 81  ILE   A C   1 
ATOM   528  O O   . ILE   A 1 74  ? -9.42547  -22.88301 -17.48481 1.000 16.86929  ? 81  ILE   A O   1 
ATOM   529  C CB  . ILE   A 1 74  ? -11.55644 -21.88423 -19.13824 1.000 15.65967  ? 81  ILE   A CB  1 
ATOM   530  C CG1 . ILE   A 1 74  ? -12.25007 -20.74099 -19.88630 1.000 21.47165  ? 81  ILE   A CG1 1 
ATOM   531  C CG2 . ILE   A 1 74  ? -12.27730 -23.20590 -19.29150 1.000 16.57489  ? 81  ILE   A CG2 1 
ATOM   532  C CD1 . ILE   A 1 74  ? -12.26468 -20.90247 -21.38715 1.000 21.40878  ? 81  ILE   A CD1 1 
ATOM   533  N N   . PRO   A 1 75  ? -10.84414 -23.00834 -15.76790 1.000 19.52976  ? 82  PRO   A N   1 
ATOM   534  C CA  . PRO   A 1 75  ? -10.09619 -24.10029 -15.14642 1.000 22.16065  ? 82  PRO   A CA  1 
ATOM   535  C C   . PRO   A 1 75  ? -10.56466 -25.45608 -15.65456 1.000 20.71195  ? 82  PRO   A C   1 
ATOM   536  O O   . PRO   A 1 75  ? -11.74213 -25.67390 -15.94929 1.000 21.93947  ? 82  PRO   A O   1 
ATOM   537  C CB  . PRO   A 1 75  ? -10.42975 -23.92778 -13.65909 1.000 17.92693  ? 82  PRO   A CB  1 
ATOM   538  C CG  . PRO   A 1 75  ? -11.84643 -23.42515 -13.67581 1.000 20.59890  ? 82  PRO   A CG  1 
ATOM   539  C CD  . PRO   A 1 75  ? -11.99326 -22.58774 -14.94272 1.000 20.12419  ? 82  PRO   A CD  1 
ATOM   540  N N   . ASN   A 1 76  ? -9.60549  -26.37080 -15.78293 1.000 18.73089  ? 83  ASN   A N   1 
ATOM   541  C CA  . ASN   A 1 76  ? -9.89530  -27.74803 -16.18564 1.000 19.31090  ? 83  ASN   A CA  1 
ATOM   542  C C   . ASN   A 1 76  ? -9.05538  -28.66810 -15.30669 1.000 23.68571  ? 83  ASN   A C   1 
ATOM   543  O O   . ASN   A 1 76  ? -7.84780  -28.81132 -15.52175 1.000 24.02689  ? 83  ASN   A O   1 
ATOM   544  C CB  . ASN   A 1 76  ? -9.61452  -27.97552 -17.66803 1.000 19.31848  ? 83  ASN   A CB  1 
ATOM   545  C CG  . ASN   A 1 76  ? -10.09417 -29.34140 -18.14601 1.000 26.79718  ? 83  ASN   A CG  1 
ATOM   546  O OD1 . ASN   A 1 76  ? -9.70979  -30.37054 -17.59677 1.000 28.42142  ? 83  ASN   A OD1 1 
ATOM   547  N ND2 . ASN   A 1 76  ? -10.95034 -29.35071 -19.16024 1.000 33.59306  ? 83  ASN   A ND2 1 
ATOM   548  N N   . LYS   A 1 77  ? -9.70235  -29.29559 -14.32173 1.000 23.91551  ? 84  LYS   A N   1 
ATOM   549  C CA  . LYS   A 1 77  ? -8.97729  -30.14941 -13.38617 1.000 23.17924  ? 84  LYS   A CA  1 
ATOM   550  C C   . LYS   A 1 77  ? -8.49027  -31.43057 -14.05041 1.000 29.67310  ? 84  LYS   A C   1 
ATOM   551  O O   . LYS   A 1 77  ? -7.46162  -31.98084 -13.64276 1.000 28.25865  ? 84  LYS   A O   1 
ATOM   552  C CB  . LYS   A 1 77  ? -9.86214  -30.47605 -12.18157 1.000 25.53411  ? 84  LYS   A CB  1 
ATOM   553  C CG  . LYS   A 1 77  ? -10.13993 -29.28529 -11.26098 1.000 29.44280  ? 84  LYS   A CG  1 
ATOM   554  C CD  . LYS   A 1 77  ? -10.96840 -29.71649 -10.05319 1.000 30.91196  ? 84  LYS   A CD  1 
ATOM   555  C CE  . LYS   A 1 77  ? -11.30341 -28.54931 -9.13567  1.000 31.89073  ? 84  LYS   A CE  1 
ATOM   556  N NZ  . LYS   A 1 77  ? -12.06461 -27.48667 -9.84504  1.000 41.90993  ? 84  LYS   A NZ  1 
ATOM   557  N N   . GLN   A 1 78  ? -9.19981  -31.90891 -15.07772 1.000 32.91891  ? 85  GLN   A N   1 
ATOM   558  C CA  . GLN   A 1 78  ? -8.79728  -33.14097 -15.74999 1.000 36.39724  ? 85  GLN   A CA  1 
ATOM   559  C C   . GLN   A 1 78  ? -7.50595  -32.94830 -16.53254 1.000 31.89843  ? 85  GLN   A C   1 
ATOM   560  O O   . GLN   A 1 78  ? -6.63892  -33.82864 -16.53493 1.000 37.99662  ? 85  GLN   A O   1 
ATOM   561  C CB  . GLN   A 1 78  ? -9.90741  -33.65462 -16.67572 1.000 45.02551  ? 85  GLN   A CB  1 
ATOM   562  C CG  . GLN   A 1 78  ? -11.18354 -34.20321 -16.00264 1.000 58.81666  ? 85  GLN   A CG  1 
ATOM   563  C CD  . GLN   A 1 78  ? -11.69088 -33.39039 -14.82089 1.000 70.89192  ? 85  GLN   A CD  1 
ATOM   564  O OE1 . GLN   A 1 78  ? -11.88622 -33.92409 -13.72860 1.000 64.63785  ? 85  GLN   A OE1 1 
ATOM   565  N NE2 . GLN   A 1 78  ? -11.97440 -32.10936 -15.05485 1.000 55.24813  ? 85  GLN   A NE2 1 
ATOM   566  N N   . ASP   A 1 79  ? -7.36355  -31.81156 -17.20900 1.000 26.56370  ? 86  ASP   A N   1 
ATOM   567  C CA  . ASP   A 1 79  ? -6.14288  -31.48914 -17.93354 1.000 29.13315  ? 86  ASP   A CA  1 
ATOM   568  C C   . ASP   A 1 79  ? -5.11278  -30.79421 -17.05911 1.000 28.98216  ? 86  ASP   A C   1 
ATOM   569  O O   . ASP   A 1 79  ? -3.96577  -30.63783 -17.49176 1.000 28.33999  ? 86  ASP   A O   1 
ATOM   570  C CB  . ASP   A 1 79  ? -6.45487  -30.59032 -19.13523 1.000 29.99981  ? 86  ASP   A CB  1 
ATOM   571  C CG  . ASP   A 1 79  ? -7.34769  -31.26762 -20.15540 1.000 40.95326  ? 86  ASP   A CG  1 
ATOM   572  O OD1 . ASP   A 1 79  ? -7.58746  -32.48817 -20.02816 1.000 41.24706  ? 86  ASP   A OD1 1 
ATOM   573  O OD2 . ASP   A 1 79  ? -7.81828  -30.57402 -21.08052 1.000 38.77918  ? 86  ASP   A OD2 1 
ATOM   574  N N   . ARG   A 1 80  ? -5.50112  -30.39260 -15.84790 1.000 22.66314  ? 87  ARG   A N   1 
ATOM   575  C CA  . ARG   A 1 80  ? -4.68330  -29.56354 -14.95853 1.000 20.14455  ? 87  ARG   A CA  1 
ATOM   576  C C   . ARG   A 1 80  ? -4.20131  -28.30520 -15.67771 1.000 22.16563  ? 87  ARG   A C   1 
ATOM   577  O O   . ARG   A 1 80  ? -3.00691  -27.98834 -15.71310 1.000 21.82762  ? 87  ARG   A O   1 
ATOM   578  C CB  . ARG   A 1 80  ? -3.50713  -30.35457 -14.37960 1.000 23.23552  ? 87  ARG   A CB  1 
ATOM   579  C CG  . ARG   A 1 80  ? -2.93292  -29.73088 -13.11800 1.000 20.97322  ? 87  ARG   A CG  1 
ATOM   580  C CD  . ARG   A 1 80  ? -2.11227  -30.72372 -12.31795 1.000 35.97149  ? 87  ARG   A CD  1 
ATOM   581  N NE  . ARG   A 1 80  ? -0.70858  -30.67337 -12.69719 1.000 43.10986  ? 87  ARG   A NE  1 
ATOM   582  C CZ  . ARG   A 1 80  ? 0.07347   -31.73299 -12.83328 1.000 42.49248  ? 87  ARG   A CZ  1 
ATOM   583  N NH1 . ARG   A 1 80  ? -0.37454  -32.95692 -12.60526 1.000 48.36507  ? 87  ARG   A NH1 1 
ATOM   584  N NH2 . ARG   A 1 80  ? 1.34026   -31.55852 -13.19679 1.000 38.12255  ? 87  ARG   A NH2 1 
ATOM   585  N N   . THR   A 1 81  ? -5.15171  -27.57649 -16.26389 1.000 17.82831  ? 88  THR   A N   1 
ATOM   586  C CA  . THR   A 1 81  ? -4.84785  -26.33186 -16.95271 1.000 19.95617  ? 88  THR   A CA  1 
ATOM   587  C C   . THR   A 1 81  ? -5.76357  -25.22274 -16.46740 1.000 19.54669  ? 88  THR   A C   1 
ATOM   588  O O   . THR   A 1 81  ? -6.93715  -25.45299 -16.17102 1.000 19.50537  ? 88  THR   A O   1 
ATOM   589  C CB  . THR   A 1 81  ? -4.98383  -26.45002 -18.48409 1.000 21.51729  ? 88  THR   A CB  1 
ATOM   590  O OG1 . THR   A 1 81  ? -6.32280  -26.83324 -18.82638 1.000 21.46663  ? 88  THR   A OG1 1 
ATOM   591  C CG2 . THR   A 1 81  ? -3.98605  -27.45270 -19.04439 1.000 21.76871  ? 88  THR   A CG2 1 
ATOM   592  N N   . LEU   A 1 82  ? -5.21219  -24.01904 -16.39549 1.000 15.18672  ? 89  LEU   A N   1 
ATOM   593  C CA  . LEU   A 1 82  ? -5.98497  -22.79904 -16.22475 1.000 17.22597  ? 89  LEU   A CA  1 
ATOM   594  C C   . LEU   A 1 82  ? -5.76385  -21.95721 -17.47233 1.000 17.88398  ? 89  LEU   A C   1 
ATOM   595  O O   . LEU   A 1 82  ? -4.62083  -21.65679 -17.82954 1.000 17.53109  ? 89  LEU   A O   1 
ATOM   596  C CB  . LEU   A 1 82  ? -5.56641  -22.04161 -14.95908 1.000 20.81371  ? 89  LEU   A CB  1 
ATOM   597  C CG  . LEU   A 1 82  ? -6.27447  -20.70187 -14.72431 1.000 18.40774  ? 89  LEU   A CG  1 
ATOM   598  C CD1 . LEU   A 1 82  ? -7.77178  -20.91541 -14.58305 1.000 17.05314  ? 89  LEU   A CD1 1 
ATOM   599  C CD2 . LEU   A 1 82  ? -5.70711  -20.01130 -13.48301 1.000 17.59710  ? 89  LEU   A CD2 1 
ATOM   600  N N   . THR   A 1 83  ? -6.84645  -21.61137 -18.15471 1.000 15.15102  ? 90  THR   A N   1 
ATOM   601  C CA  . THR   A 1 83  ? -6.77036  -20.89249 -19.41519 1.000 17.04006  ? 90  THR   A CA  1 
ATOM   602  C C   . THR   A 1 83  ? -7.36201  -19.50169 -19.23777 1.000 16.41560  ? 90  THR   A C   1 
ATOM   603  O O   . THR   A 1 83  ? -8.47312  -19.35727 -18.70960 1.000 17.86305  ? 90  THR   A O   1 
ATOM   604  C CB  . THR   A 1 83  ? -7.51220  -21.64613 -20.52386 1.000 18.45104  ? 90  THR   A CB  1 
ATOM   605  O OG1 . THR   A 1 83  ? -6.93969  -22.94858 -20.70494 1.000 18.97225  ? 90  THR   A OG1 1 
ATOM   606  C CG2 . THR   A 1 83  ? -7.39961  -20.88737 -21.81258 1.000 18.70512  ? 90  THR   A CG2 1 
ATOM   607  N N   . ILE   A 1 84  ? -6.62029  -18.48418 -19.66998 1.000 14.83394  ? 91  ILE   A N   1 
ATOM   608  C CA  . ILE   A 1 84  ? -7.07715  -17.09548 -19.64470 1.000 14.84777  ? 91  ILE   A CA  1 
ATOM   609  C C   . ILE   A 1 84  ? -7.33872  -16.69027 -21.08904 1.000 16.60197  ? 91  ILE   A C   1 
ATOM   610  O O   . ILE   A 1 84  ? -6.39909  -16.58574 -21.88625 1.000 18.39440  ? 91  ILE   A O   1 
ATOM   611  C CB  . ILE   A 1 84  ? -6.05728  -16.14927 -18.98789 1.000 16.13281  ? 91  ILE   A CB  1 
ATOM   612  C CG1 . ILE   A 1 84  ? -5.82696  -16.49523 -17.50816 1.000 24.37207  ? 91  ILE   A CG1 1 
ATOM   613  C CG2 . ILE   A 1 84  ? -6.52179  -14.70148 -19.10594 1.000 17.31994  ? 91  ILE   A CG2 1 
ATOM   614  C CD1 . ILE   A 1 84  ? -4.77083  -17.54890 -17.26052 1.000 23.15573  ? 91  ILE   A CD1 1 
ATOM   615  N N   . VAL   A 1 85  ? -8.60625  -16.45996 -21.43135 1.000 13.50799  ? 92  VAL   A N   1 
ATOM   616  C CA  . VAL   A 1 85  ? -9.02327  -16.14293 -22.79516 1.000 13.69282  ? 92  VAL   A CA  1 
ATOM   617  C C   . VAL   A 1 85  ? -9.42703  -14.68105 -22.84760 1.000 20.06143  ? 92  VAL   A C   1 
ATOM   618  O O   . VAL   A 1 85  ? -10.18047 -14.21124 -21.98555 1.000 17.52451  ? 92  VAL   A O   1 
ATOM   619  C CB  . VAL   A 1 85  ? -10.20017 -17.02399 -23.25503 1.000 15.10853  ? 92  VAL   A CB  1 
ATOM   620  C CG1 . VAL   A 1 85  ? -10.49723 -16.78012 -24.72820 1.000 19.77865  ? 92  VAL   A CG1 1 
ATOM   621  C CG2 . VAL   A 1 85  ? -9.91510  -18.49277 -22.99457 1.000 21.47496  ? 92  VAL   A CG2 1 
ATOM   622  N N   . ASP   A 1 86  ? -8.95277  -13.96389 -23.86512 1.000 15.74166  ? 93  ASP   A N   1 
ATOM   623  C CA  . ASP   A 1 86  ? -9.45795  -12.62313 -24.11621 1.000 14.55125  ? 93  ASP   A CA  1 
ATOM   624  C C   . ASP   A 1 86  ? -9.72482  -12.45163 -25.60569 1.000 17.20067  ? 93  ASP   A C   1 
ATOM   625  O O   . ASP   A 1 86  ? -9.21351  -13.19877 -26.44604 1.000 20.52248  ? 93  ASP   A O   1 
ATOM   626  C CB  . ASP   A 1 86  ? -8.49994  -11.52937 -23.59234 1.000 15.15271  ? 93  ASP   A CB  1 
ATOM   627  C CG  . ASP   A 1 86  ? -7.19454  -11.44109 -24.37673 1.000 20.56627  ? 93  ASP   A CG  1 
ATOM   628  O OD1 . ASP   A 1 86  ? -7.22577  -11.06470 -25.56607 1.000 19.11277  ? 93  ASP   A OD1 1 
ATOM   629  O OD2 . ASP   A 1 86  ? -6.12710  -11.71767 -23.78695 1.000 19.67942  ? 93  ASP   A OD2 1 
ATOM   630  N N   . THR   A 1 87  ? -10.56766 -11.47377 -25.92120 1.000 15.79900  ? 94  THR   A N   1 
ATOM   631  C CA  . THR   A 1 87  ? -10.90853 -11.13824 -27.29830 1.000 14.20468  ? 94  THR   A CA  1 
ATOM   632  C C   . THR   A 1 87  ? -10.24422 -9.82335  -27.70020 1.000 20.09682  ? 94  THR   A C   1 
ATOM   633  O O   . THR   A 1 87  ? -10.80489 -9.00976  -28.43946 1.000 16.67686  ? 94  THR   A O   1 
ATOM   634  C CB  . THR   A 1 87  ? -12.42446 -11.08281 -27.48337 1.000 15.92481  ? 94  THR   A CB  1 
ATOM   635  O OG1 . THR   A 1 87  ? -13.01015 -10.24708 -26.47644 1.000 16.87889  ? 94  THR   A OG1 1 
ATOM   636  C CG2 . THR   A 1 87  ? -13.01481 -12.48326 -27.36548 1.000 18.27716  ? 94  THR   A CG2 1 
ATOM   637  N N   . GLY   A 1 88  ? -9.02891  -9.61200  -27.19885 1.000 17.11967  ? 95  GLY   A N   1 
ATOM   638  C CA  . GLY   A 1 88  ? -8.26927  -8.41753  -27.50517 1.000 18.42373  ? 95  GLY   A CA  1 
ATOM   639  C C   . GLY   A 1 88  ? -7.66523  -8.43346  -28.89502 1.000 15.44758  ? 95  GLY   A C   1 
ATOM   640  O O   . GLY   A 1 88  ? -8.09558  -9.19454  -29.77074 1.000 14.46969  ? 95  GLY   A O   1 
ATOM   641  N N   . ILE   A 1 89  ? -6.65052  -7.59175  -29.10453 1.000 16.36055  ? 96  ILE   A N   1 
ATOM   642  C CA  . ILE   A 1 89  ? -6.11905  -7.38407  -30.44392 1.000 13.92643  ? 96  ILE   A CA  1 
ATOM   643  C C   . ILE   A 1 89  ? -5.35167  -8.60229  -30.94906 1.000 16.18269  ? 96  ILE   A C   1 
ATOM   644  O O   . ILE   A 1 89  ? -5.17110  -8.75300  -32.16223 1.000 17.64158  ? 96  ILE   A O   1 
ATOM   645  C CB  . ILE   A 1 89  ? -5.25450  -6.10336  -30.45405 1.000 13.29997  ? 96  ILE   A CB  1 
ATOM   646  C CG1 . ILE   A 1 89  ? -4.95037  -5.64829  -31.88782 1.000 19.65024  ? 96  ILE   A CG1 1 
ATOM   647  C CG2 . ILE   A 1 89  ? -3.97288  -6.29735  -29.63763 1.000 15.94063  ? 96  ILE   A CG2 1 
ATOM   648  C CD1 . ILE   A 1 89  ? -4.59813  -4.18553  -31.97749 1.000 21.35123  ? 96  ILE   A CD1 1 
ATOM   649  N N   . GLY   A 1 90  ? -4.92743  -9.49873  -30.05674 1.000 15.52309  ? 97  GLY   A N   1 
ATOM   650  C CA  . GLY   A 1 90  ? -4.14924  -10.65015 -30.47667 1.000 17.47170  ? 97  GLY   A CA  1 
ATOM   651  C C   . GLY   A 1 90  ? -2.72332  -10.24142 -30.81884 1.000 18.23880  ? 97  GLY   A C   1 
ATOM   652  O O   . GLY   A 1 90  ? -2.30324  -9.10064  -30.63019 1.000 17.67000  ? 97  GLY   A O   1 
ATOM   653  N N   . MET   A 1 91  ? -1.96142  -11.21063 -31.31336 1.000 16.95952  ? 98  MET   A N   1 
ATOM   654  C CA  . MET   A 1 91  ? -0.62674  -10.90153 -31.79668 1.000 17.26111  ? 98  MET   A CA  1 
ATOM   655  C C   . MET   A 1 91  ? -0.33237  -11.66397 -33.07539 1.000 20.41519  ? 98  MET   A C   1 
ATOM   656  O O   . MET   A 1 91  ? -0.84414  -12.76246 -33.30182 1.000 16.78136  ? 98  MET   A O   1 
ATOM   657  C CB  . MET   A 1 91  ? 0.49856   -11.15351 -30.76390 1.000 26.23083  ? 98  MET   A CB  1 
ATOM   658  C CG  . MET   A 1 91  ? 0.21865   -10.90794 -29.28196 1.000 21.31266  ? 98  MET   A CG  1 
ATOM   659  S SD  . MET   A 1 91  ? 1.32760   -11.82141 -28.15962 1.000 21.18176  ? 98  MET   A SD  1 
ATOM   660  C CE  . MET   A 1 91  ? 0.24347   -13.11456 -27.56060 1.000 18.55467  ? 98  MET   A CE  1 
ATOM   661  N N   . THR   A 1 92  ? 0.48545   -11.04178 -33.91894 1.000 17.48862  ? 99  THR   A N   1 
ATOM   662  C CA  . THR   A 1 92  ? 0.98220   -11.64676 -35.14307 1.000 18.65038  ? 99  THR   A CA  1 
ATOM   663  C C   . THR   A 1 92  ? 2.07216   -12.66698 -34.82287 1.000 19.43579  ? 99  THR   A C   1 
ATOM   664  O O   . THR   A 1 92  ? 2.56074   -12.76286 -33.69379 1.000 21.67486  ? 99  THR   A O   1 
ATOM   665  C CB  . THR   A 1 92  ? 1.54834   -10.57926 -36.07755 1.000 21.16033  ? 99  THR   A CB  1 
ATOM   666  O OG1 . THR   A 1 92  ? 2.70877   -9.98914  -35.47359 1.000 22.98579  ? 99  THR   A OG1 1 
ATOM   667  C CG2 . THR   A 1 92  ? 0.51658   -9.49688  -36.35711 1.000 22.91366  ? 99  THR   A CG2 1 
ATOM   668  N N   . LYS   A 1 93  ? 2.45350   -13.44410 -35.83895 1.000 17.26085  ? 100 LYS   A N   1 
ATOM   669  C CA  . LYS   A 1 93  ? 3.59036   -14.34231 -35.67056 1.000 20.61391  ? 100 LYS   A CA  1 
ATOM   670  C C   . LYS   A 1 93  ? 4.83740   -13.56475 -35.28046 1.000 19.65858  ? 100 LYS   A C   1 
ATOM   671  O O   . LYS   A 1 93  ? 5.58417   -13.98148 -34.38606 1.000 16.90676  ? 100 LYS   A O   1 
ATOM   672  C CB  . LYS   A 1 93  ? 3.83837   -15.13786 -36.95041 1.000 23.47780  ? 100 LYS   A CB  1 
ATOM   673  C CG  . LYS   A 1 93  ? 4.88420   -16.23329 -36.78948 1.000 18.39480  ? 100 LYS   A CG  1 
ATOM   674  C CD  . LYS   A 1 93  ? 5.14529   -16.92892 -38.11699 1.000 18.59057  ? 100 LYS   A CD  1 
ATOM   675  C CE  . LYS   A 1 93  ? 6.12209   -18.08476 -37.95870 1.000 25.89740  ? 100 LYS   A CE  1 
ATOM   676  N NZ  . LYS   A 1 93  ? 6.88855   -18.32497 -39.21257 1.000 27.70291  ? 100 LYS   A NZ  1 
ATOM   677  N N   . ALA   A 1 94  ? 5.07068   -12.42243 -35.93506 1.000 21.21917  ? 101 ALA   A N   1 
ATOM   678  C CA  . ALA   A 1 94  ? 6.22070   -11.59227 -35.59098 1.000 22.63350  ? 101 ALA   A CA  1 
ATOM   679  C C   . ALA   A 1 94  ? 6.15455   -11.14347 -34.13829 1.000 24.60136  ? 101 ALA   A C   1 
ATOM   680  O O   . ALA   A 1 94  ? 7.16887   -11.15402 -33.43047 1.000 23.35093  ? 101 ALA   A O   1 
ATOM   681  C CB  . ALA   A 1 94  ? 6.29298   -10.38427 -36.52542 1.000 25.46109  ? 101 ALA   A CB  1 
ATOM   682  N N   . ASP   A 1 95  ? 4.96269   -10.75537 -33.67534 1.000 17.97440  ? 102 ASP   A N   1 
ATOM   683  C CA  . ASP   A 1 95  ? 4.78867   -10.37231 -32.27635 1.000 21.39445  ? 102 ASP   A CA  1 
ATOM   684  C C   . ASP   A 1 95  ? 5.14908   -11.52046 -31.34163 1.000 19.01578  ? 102 ASP   A C   1 
ATOM   685  O O   . ASP   A 1 95  ? 5.85898   -11.32681 -30.34871 1.000 19.58808  ? 102 ASP   A O   1 
ATOM   686  C CB  . ASP   A 1 95  ? 3.34492   -9.94239  -32.02124 1.000 26.93251  ? 102 ASP   A CB  1 
ATOM   687  C CG  . ASP   A 1 95  ? 3.00421   -8.60297  -32.62538 1.000 36.68210  ? 102 ASP   A CG  1 
ATOM   688  O OD1 . ASP   A 1 95  ? 3.91139   -7.76315  -32.79518 1.000 27.21902  ? 102 ASP   A OD1 1 
ATOM   689  O OD2 . ASP   A 1 95  ? 1.80505   -8.38710  -32.90890 1.000 25.48673  ? 102 ASP   A OD2 1 
ATOM   690  N N   . LEU   A 1 96  ? 4.65877   -12.72860 -31.64123 1.000 16.65968  ? 103 LEU   A N   1 
ATOM   691  C CA  . LEU   A 1 96  ? 4.93541   -13.88019 -30.78396 1.000 19.73323  ? 103 LEU   A CA  1 
ATOM   692  C C   . LEU   A 1 96  ? 6.43073   -14.11780 -30.64125 1.000 19.18147  ? 103 LEU   A C   1 
ATOM   693  O O   . LEU   A 1 96  ? 6.93812   -14.31743 -29.53172 1.000 19.89553  ? 103 LEU   A O   1 
ATOM   694  C CB  . LEU   A 1 96  ? 4.27371   -15.13487 -31.34652 1.000 21.52354  ? 103 LEU   A CB  1 
ATOM   695  C CG  . LEU   A 1 96  ? 2.78975   -15.35127 -31.09385 1.000 18.09793  ? 103 LEU   A CG  1 
ATOM   696  C CD1 . LEU   A 1 96  ? 2.35827   -16.63472 -31.79059 1.000 18.25442  ? 103 LEU   A CD1 1 
ATOM   697  C CD2 . LEU   A 1 96  ? 2.46713   -15.38667 -29.60747 1.000 15.29486  ? 103 LEU   A CD2 1 
ATOM   698  N N   . ILE   A 1 97  ? 7.15021   -14.12961 -31.76337 1.000 17.55167  ? 104 ILE   A N   1 
ATOM   699  C CA  . ILE   A 1 97  ? 8.58871   -14.37624 -31.71662 1.000 20.08781  ? 104 ILE   A CA  1 
ATOM   700  C C   . ILE   A 1 97  ? 9.29868   -13.25358 -30.97342 1.000 22.84004  ? 104 ILE   A C   1 
ATOM   701  O O   . ILE   A 1 97  ? 10.26803  -13.48637 -30.24046 1.000 21.95808  ? 104 ILE   A O   1 
ATOM   702  C CB  . ILE   A 1 97  ? 9.14301   -14.55480 -33.14199 1.000 18.76803  ? 104 ILE   A CB  1 
ATOM   703  C CG1 . ILE   A 1 97  ? 8.52417   -15.78697 -33.80407 1.000 22.92008  ? 104 ILE   A CG1 1 
ATOM   704  C CG2 . ILE   A 1 97  ? 10.66082  -14.62466 -33.12518 1.000 17.71534  ? 104 ILE   A CG2 1 
ATOM   705  C CD1 . ILE   A 1 97  ? 8.64353   -15.78372 -35.31972 1.000 20.90076  ? 104 ILE   A CD1 1 
ATOM   706  N N   . ASN   A 1 98  ? 8.81876   -12.02237 -31.13745 1.000 17.20977  ? 105 ASN   A N   1 
ATOM   707  C CA  . ASN   A 1 98  ? 9.39910   -10.85498 -30.47968 1.000 20.65978  ? 105 ASN   A CA  1 
ATOM   708  C C   . ASN   A 1 98  ? 8.87903   -10.72579 -29.04462 1.000 19.60857  ? 105 ASN   A C   1 
ATOM   709  O O   . ASN   A 1 98  ? 8.30622   -9.71192  -28.64444 1.000 22.65223  ? 105 ASN   A O   1 
ATOM   710  C CB  . ASN   A 1 98  ? 9.08910   -9.60308  -31.28907 1.000 22.99672  ? 105 ASN   A CB  1 
ATOM   711  C CG  . ASN   A 1 98  ? 10.31472  -8.79403  -31.58610 1.000 53.41773  ? 105 ASN   A CG  1 
ATOM   712  O OD1 . ASN   A 1 98  ? 10.96342  -8.26940  -30.68052 1.000 55.42208  ? 105 ASN   A OD1 1 
ATOM   713  N ND2 . ASN   A 1 98  ? 10.66009  -8.70351  -32.86103 1.000 51.87724  ? 105 ASN   A ND2 1 
ATOM   714  N N   . ASN   A 1 99  ? 9.07404   -11.79941 -28.27842 1.000 18.69008  ? 106 ASN   A N   1 
ATOM   715  C CA  . ASN   A 1 99  ? 8.74077   -11.84315 -26.85415 1.000 17.32721  ? 106 ASN   A CA  1 
ATOM   716  C C   . ASN   A 1 99  ? 7.29378   -11.44477 -26.58454 1.000 19.30316  ? 106 ASN   A C   1 
ATOM   717  O O   . ASN   A 1 99  ? 6.99741   -10.66983 -25.67344 1.000 16.23018  ? 106 ASN   A O   1 
ATOM   718  C CB  . ASN   A 1 99  ? 9.71393   -10.98768 -26.04460 1.000 19.51505  ? 106 ASN   A CB  1 
ATOM   719  C CG  . ASN   A 1 99  ? 11.14137  -11.42986 -26.22746 1.000 21.24100  ? 106 ASN   A CG  1 
ATOM   720  O OD1 . ASN   A 1 99  ? 11.45908  -12.59604 -26.00091 1.000 20.65195  ? 106 ASN   A OD1 1 
ATOM   721  N ND2 . ASN   A 1 99  ? 12.01566  -10.50840 -26.62614 1.000 19.50726  ? 106 ASN   A ND2 1 
ATOM   722  N N   . LEU   A 1 100 ? 6.38760   -12.02464 -27.37533 1.000 16.15435  ? 107 LEU   A N   1 
ATOM   723  C CA  . LEU   A 1 100 ? 4.94520   -11.84961 -27.20578 1.000 19.09675  ? 107 LEU   A CA  1 
ATOM   724  C C   . LEU   A 1 100 ? 4.56819   -10.37091 -27.15651 1.000 21.89792  ? 107 LEU   A C   1 
ATOM   725  O O   . LEU   A 1 100 ? 3.76856   -9.93157  -26.32755 1.000 17.73088  ? 107 LEU   A O   1 
ATOM   726  C CB  . LEU   A 1 100 ? 4.45240   -12.60301 -25.96961 1.000 16.86121  ? 107 LEU   A CB  1 
ATOM   727  C CG  . LEU   A 1 100 ? 4.73950   -14.10601 -26.10067 1.000 21.52537  ? 107 LEU   A CG  1 
ATOM   728  C CD1 . LEU   A 1 100 ? 5.83600   -14.55100 -25.13480 1.000 20.65658  ? 107 LEU   A CD1 1 
ATOM   729  C CD2 . LEU   A 1 100 ? 3.48192   -14.92478 -25.90619 1.000 29.57071  ? 107 LEU   A CD2 1 
ATOM   730  N N   . GLY   A 1 101 ? 5.15884   -9.59531  -28.06172 1.000 16.66392  ? 108 GLY   A N   1 
ATOM   731  C CA  . GLY   A 1 101 ? 4.78233   -8.20343  -28.20859 1.000 24.81778  ? 108 GLY   A CA  1 
ATOM   732  C C   . GLY   A 1 101 ? 5.31126   -7.27228  -27.14368 1.000 23.90724  ? 108 GLY   A C   1 
ATOM   733  O O   . GLY   A 1 101 ? 4.79178   -6.15883  -27.00151 1.000 26.87580  ? 108 GLY   A O   1 
ATOM   734  N N   . THR   A 1 102 ? 6.33667   -7.67795  -26.39532 1.000 20.63997  ? 109 THR   A N   1 
ATOM   735  C CA  . THR   A 1 102 ? 6.86429   -6.86212  -25.31267 1.000 17.92567  ? 109 THR   A CA  1 
ATOM   736  C C   . THR   A 1 102 ? 8.27311   -6.40168  -25.65053 1.000 16.87380  ? 109 THR   A C   1 
ATOM   737  O O   . THR   A 1 102 ? 8.91115   -6.89712  -26.58662 1.000 21.21782  ? 109 THR   A O   1 
ATOM   738  C CB  . THR   A 1 102 ? 6.89056   -7.62890  -23.98559 1.000 20.04509  ? 109 THR   A CB  1 
ATOM   739  O OG1 . THR   A 1 102 ? 7.79766   -8.73382  -24.08836 1.000 21.79018  ? 109 THR   A OG1 1 
ATOM   740  C CG2 . THR   A 1 102 ? 5.50662   -8.16272  -23.67373 1.000 25.04884  ? 109 THR   A CG2 1 
ATOM   741  N N   . ILE   A 1 103 ? 8.75453   -5.44182  -24.86643 1.000 18.52363  ? 110 ILE   A N   1 
ATOM   742  C CA  . ILE   A 1 103 ? 10.15373  -5.03941  -24.93353 1.000 19.02362  ? 110 ILE   A CA  1 
ATOM   743  C C   . ILE   A 1 103 ? 10.87920  -5.74024  -23.79351 1.000 22.19803  ? 110 ILE   A C   1 
ATOM   744  O O   . ILE   A 1 103 ? 11.45454  -5.10109  -22.90187 1.000 19.55465  ? 110 ILE   A O   1 
ATOM   745  C CB  . ILE   A 1 103 ? 10.31184  -3.51042  -24.87888 1.000 24.56613  ? 110 ILE   A CB  1 
ATOM   746  C CG1 . ILE   A 1 103 ? 9.49289   -2.90915  -23.73395 1.000 24.13167  ? 110 ILE   A CG1 1 
ATOM   747  C CG2 . ILE   A 1 103 ? 9.87991   -2.89548  -26.20124 1.000 31.08254  ? 110 ILE   A CG2 1 
ATOM   748  C CD1 . ILE   A 1 103 ? 9.96484   -1.52698  -23.34435 1.000 29.52219  ? 110 ILE   A CD1 1 
ATOM   749  N N   . ALA   A 1 104 ? 10.87571  -7.07224  -23.84215 1.000 21.73298  ? 111 ALA   A N   1 
ATOM   750  C CA  . ALA   A 1 104 ? 11.27183  -7.86100  -22.68620 1.000 18.04509  ? 111 ALA   A CA  1 
ATOM   751  C C   . ALA   A 1 104 ? 12.75562  -7.72506  -22.36626 1.000 18.76028  ? 111 ALA   A C   1 
ATOM   752  O O   . ALA   A 1 104 ? 13.14253  -7.89292  -21.20644 1.000 21.24837  ? 111 ALA   A O   1 
ATOM   753  C CB  . ALA   A 1 104 ? 10.90219  -9.32939  -22.90465 1.000 19.43702  ? 111 ALA   A CB  1 
ATOM   754  N N   . LYS   A 1 105 ? 13.60410  -7.43458  -23.35637 1.000 20.98801  ? 112 LYS   A N   1 
ATOM   755  C CA  . LYS   A 1 105 ? 15.02791  -7.31555  -23.05176 1.000 21.89081  ? 112 LYS   A CA  1 
ATOM   756  C C   . LYS   A 1 105 ? 15.28313  -6.13055  -22.12743 1.000 29.60536  ? 112 LYS   A C   1 
ATOM   757  O O   . LYS   A 1 105 ? 15.90859  -6.27885  -21.07213 1.000 27.92334  ? 112 LYS   A O   1 
ATOM   758  C CB  . LYS   A 1 105 ? 15.85430  -7.19467  -24.33685 1.000 22.11317  ? 112 LYS   A CB  1 
ATOM   759  C CG  . LYS   A 1 105 ? 17.35171  -7.03059  -24.09202 1.000 31.92116  ? 112 LYS   A CG  1 
ATOM   760  C CD  . LYS   A 1 105 ? 18.14456  -7.08184  -25.39166 1.000 29.29848  ? 112 LYS   A CD  1 
ATOM   761  C CE  . LYS   A 1 105 ? 19.48297  -6.37010  -25.25805 1.000 56.79205  ? 112 LYS   A CE  1 
ATOM   762  N NZ  . LYS   A 1 105 ? 20.35235  -6.98128  -24.21473 1.000 57.40594  ? 112 LYS   A NZ  1 
ATOM   763  N N   . SER   A 1 106 ? 14.78208  -4.94754  -22.49276 1.000 23.60468  ? 113 SER   A N   1 
ATOM   764  C CA  . SER   A 1 106 ? 14.98587  -3.78190  -21.63898 1.000 26.19906  ? 113 SER   A CA  1 
ATOM   765  C C   . SER   A 1 106 ? 14.14115  -3.86705  -20.37196 1.000 25.85503  ? 113 SER   A C   1 
ATOM   766  O O   . SER   A 1 106 ? 14.54915  -3.35401  -19.32482 1.000 28.81501  ? 113 SER   A O   1 
ATOM   767  C CB  . SER   A 1 106 ? 14.67398  -2.49578  -22.40606 1.000 33.10302  ? 113 SER   A CB  1 
ATOM   768  O OG  . SER   A 1 106 ? 13.33102  -2.48536  -22.85813 1.000 27.98926  ? 113 SER   A OG  1 
ATOM   769  N N   . GLY   A 1 107 ? 12.97313  -4.51155  -20.44189 1.000 22.75387  ? 114 GLY   A N   1 
ATOM   770  C CA  . GLY   A 1 107 ? 12.16296  -4.68341  -19.24535 1.000 22.02665  ? 114 GLY   A CA  1 
ATOM   771  C C   . GLY   A 1 107 ? 12.81406  -5.60334  -18.23102 1.000 26.58447  ? 114 GLY   A C   1 
ATOM   772  O O   . GLY   A 1 107 ? 12.77538  -5.34106  -17.02537 1.000 24.34407  ? 114 GLY   A O   1 
ATOM   773  N N   . THR   A 1 108 ? 13.42391  -6.69271  -18.70303 1.000 22.11334  ? 115 THR   A N   1 
ATOM   774  C CA  . THR   A 1 108 ? 14.15890  -7.57789  -17.80230 1.000 24.65345  ? 115 THR   A CA  1 
ATOM   775  C C   . THR   A 1 108 ? 15.32896  -6.85285  -17.14930 1.000 27.03712  ? 115 THR   A C   1 
ATOM   776  O O   . THR   A 1 108 ? 15.54870  -6.97972  -15.93858 1.000 30.87099  ? 115 THR   A O   1 
ATOM   777  C CB  . THR   A 1 108 ? 14.65417  -8.80609  -18.56453 1.000 25.30983  ? 115 THR   A CB  1 
ATOM   778  O OG1 . THR   A 1 108 ? 13.52824  -9.54952  -19.05025 1.000 23.39344  ? 115 THR   A OG1 1 
ATOM   779  C CG2 . THR   A 1 108 ? 15.48418  -9.69379  -17.66381 1.000 27.18687  ? 115 THR   A CG2 1 
ATOM   780  N N   . LYS   A 1 109 ? 16.09277  -6.09394  -17.94045 1.000 28.65210  ? 116 LYS   A N   1 
ATOM   781  C CA  . LYS   A 1 109 ? 17.20462  -5.31445  -17.40485 1.000 32.48187  ? 116 LYS   A CA  1 
ATOM   782  C C   . LYS   A 1 109 ? 16.74884  -4.42752  -16.25358 1.000 39.34903  ? 116 LYS   A C   1 
ATOM   783  O O   . LYS   A 1 109 ? 17.37158  -4.40121  -15.18604 1.000 38.42933  ? 116 LYS   A O   1 
ATOM   784  C CB  . LYS   A 1 109 ? 17.82764  -4.47283  -18.52272 1.000 33.84098  ? 116 LYS   A CB  1 
ATOM   785  C CG  . LYS   A 1 109 ? 18.59027  -3.23206  -18.05990 1.000 51.88395  ? 116 LYS   A CG  1 
ATOM   786  C CD  . LYS   A 1 109 ? 19.67542  -2.85858  -19.06290 1.000 46.20965  ? 116 LYS   A CD  1 
ATOM   787  C CE  . LYS   A 1 109 ? 20.82501  -2.10156  -18.41093 1.000 44.47770  ? 116 LYS   A CE  1 
ATOM   788  N NZ  . LYS   A 1 109 ? 21.38418  -2.82855  -17.23968 1.000 74.08855  ? 116 LYS   A NZ  1 
ATOM   789  N N   . ALA   A 1 110 ? 15.65273  -3.69532  -16.45281 1.000 32.40281  ? 117 ALA   A N   1 
ATOM   790  C CA  . ALA   A 1 110 ? 15.16426  -2.80837  -15.40424 1.000 33.93536  ? 117 ALA   A CA  1 
ATOM   791  C C   . ALA   A 1 110 ? 14.64169  -3.59707  -14.20973 1.000 33.21128  ? 117 ALA   A C   1 
ATOM   792  O O   . ALA   A 1 110 ? 14.84741  -3.19803  -13.05803 1.000 37.63540  ? 117 ALA   A O   1 
ATOM   793  C CB  . ALA   A 1 110 ? 14.07975  -1.89026  -15.96390 1.000 32.77222  ? 117 ALA   A CB  1 
ATOM   794  N N   . PHE   A 1 111 ? 13.96428  -4.71842  -14.46517 1.000 30.70659  ? 118 PHE   A N   1 
ATOM   795  C CA  . PHE   A 1 111 ? 13.37981  -5.50619  -13.38298 1.000 29.40293  ? 118 PHE   A CA  1 
ATOM   796  C C   . PHE   A 1 111 ? 14.46103  -6.05165  -12.45708 1.000 33.34480  ? 118 PHE   A C   1 
ATOM   797  O O   . PHE   A 1 111 ? 14.36857  -5.92995  -11.22981 1.000 33.50054  ? 118 PHE   A O   1 
ATOM   798  C CB  . PHE   A 1 111 ? 12.54426  -6.63997  -13.97873 1.000 25.85986  ? 118 PHE   A CB  1 
ATOM   799  C CG  . PHE   A 1 111 ? 11.85465  -7.51422  -12.95986 1.000 26.15885  ? 118 PHE   A CG  1 
ATOM   800  C CD1 . PHE   A 1 111 ? 11.28277  -6.97264  -11.81618 1.000 26.35527  ? 118 PHE   A CD1 1 
ATOM   801  C CD2 . PHE   A 1 111 ? 11.73880  -8.88175  -13.17611 1.000 31.09698  ? 118 PHE   A CD2 1 
ATOM   802  C CE1 . PHE   A 1 111 ? 10.62587  -7.78419  -10.89306 1.000 25.79108  ? 118 PHE   A CE1 1 
ATOM   803  C CE2 . PHE   A 1 111 ? 11.08481  -9.69806  -12.26017 1.000 30.94946  ? 118 PHE   A CE2 1 
ATOM   804  C CZ  . PHE   A 1 111 ? 10.53055  -9.14620  -11.11423 1.000 24.74491  ? 118 PHE   A CZ  1 
ATOM   805  N N   . MET   A 1 112 ? 15.50728  -6.64519  -13.02800 1.000 32.80233  ? 119 MET   A N   1 
ATOM   806  C CA  . MET   A 1 112 ? 16.52280  -7.26543  -12.18399 1.000 47.45778  ? 119 MET   A CA  1 
ATOM   807  C C   . MET   A 1 112 ? 17.34801  -6.23682  -11.42413 1.000 53.52861  ? 119 MET   A C   1 
ATOM   808  O O   . MET   A 1 112 ? 17.82761  -6.52734  -10.32160 1.000 45.44717  ? 119 MET   A O   1 
ATOM   809  C CB  . MET   A 1 112 ? 17.42313  -8.16895  -13.01589 1.000 52.43141  ? 119 MET   A CB  1 
ATOM   810  C CG  . MET   A 1 112 ? 16.89551  -9.58340  -13.11451 1.000 32.29791  ? 119 MET   A CG  1 
ATOM   811  S SD  . MET   A 1 112 ? 17.73349  -10.47758 -14.41829 1.000 67.77815  ? 119 MET   A SD  1 
ATOM   812  C CE  . MET   A 1 112 ? 16.75008  -11.96243 -14.46646 1.000 38.07371  ? 119 MET   A CE  1 
ATOM   813  N N   . GLU   A 1 113 ? 17.53135  -5.03960  -11.98042 1.000 41.35889  ? 120 GLU   A N   1 
ATOM   814  C CA  . GLU   A 1 113 ? 18.19390  -3.99760  -11.20599 1.000 55.23479  ? 120 GLU   A CA  1 
ATOM   815  C C   . GLU   A 1 113 ? 17.31993  -3.55163  -10.04428 1.000 54.29429  ? 120 GLU   A C   1 
ATOM   816  O O   . GLU   A 1 113 ? 17.82672  -3.24252  -8.95933  1.000 57.08372  ? 120 GLU   A O   1 
ATOM   817  C CB  . GLU   A 1 113 ? 18.55064  -2.81114  -12.09580 1.000 53.23369  ? 120 GLU   A CB  1 
ATOM   818  C CG  . GLU   A 1 113 ? 19.53620  -3.13532  -13.20050 1.000 69.93853  ? 120 GLU   A CG  1 
ATOM   819  C CD  . GLU   A 1 113 ? 19.73329  -1.96708  -14.13974 1.000 81.06701  ? 120 GLU   A CD  1 
ATOM   820  O OE1 . GLU   A 1 113 ? 18.81554  -1.12485  -14.22925 1.000 70.38981  ? 120 GLU   A OE1 1 
ATOM   821  O OE2 . GLU   A 1 113 ? 20.79835  -1.89071  -14.78807 1.000 79.11186  ? 120 GLU   A OE2 1 
ATOM   822  N N   . ALA   A 1 114 ? 16.00334  -3.51704  -10.25088 1.000 43.40804  ? 121 ALA   A N   1 
ATOM   823  C CA  . ALA   A 1 114 ? 15.09928  -3.19497  -9.15358  1.000 41.62701  ? 121 ALA   A CA  1 
ATOM   824  C C   . ALA   A 1 114 ? 15.12417  -4.28045  -8.08622  1.000 44.97949  ? 121 ALA   A C   1 
ATOM   825  O O   . ALA   A 1 114 ? 15.08891  -3.97797  -6.88787  1.000 55.05105  ? 121 ALA   A O   1 
ATOM   826  C CB  . ALA   A 1 114 ? 13.68314  -2.98863  -9.68181  1.000 39.70539  ? 121 ALA   A CB  1 
ATOM   827  N N   . LEU   A 1 115 ? 15.20312  -5.54820  -8.50310  1.000 43.60393  ? 122 LEU   A N   1 
ATOM   828  C CA  . LEU   A 1 115 ? 15.19541  -6.65407  -7.54894  1.000 40.24078  ? 122 LEU   A CA  1 
ATOM   829  C C   . LEU   A 1 115 ? 16.38184  -6.56868  -6.59520  1.000 54.90181  ? 122 LEU   A C   1 
ATOM   830  O O   . LEU   A 1 115 ? 16.22234  -6.67368  -5.37359  1.000 53.89873  ? 122 LEU   A O   1 
ATOM   831  C CB  . LEU   A 1 115 ? 15.19964  -7.98721  -8.29499  1.000 41.70908  ? 122 LEU   A CB  1 
ATOM   832  C CG  . LEU   A 1 115 ? 13.89090  -8.39904  -8.96758  1.000 33.21595  ? 122 LEU   A CG  1 
ATOM   833  C CD1 . LEU   A 1 115 ? 14.05746  -9.73413  -9.67211  1.000 34.85164  ? 122 LEU   A CD1 1 
ATOM   834  C CD2 . LEU   A 1 115 ? 12.75561  -8.45526  -7.94987  1.000 32.96148  ? 122 LEU   A CD2 1 
ATOM   835  N N   . GLN   A 1 116 ? 17.58584  -6.37731  -7.13389  1.000 57.38217  ? 123 GLN   A N   1 
ATOM   836  C CA  . GLN   A 1 116 ? 18.74223  -6.20932  -6.26397  1.000 60.81565  ? 123 GLN   A CA  1 
ATOM   837  C C   . GLN   A 1 116 ? 18.72834  -4.87582  -5.52825  1.000 68.04159  ? 123 GLN   A C   1 
ATOM   838  O O   . GLN   A 1 116 ? 19.58734  -4.65336  -4.66769  1.000 71.92035  ? 123 GLN   A O   1 
ATOM   839  C CB  . GLN   A 1 116 ? 20.03297  -6.35751  -7.06917  1.000 63.36079  ? 123 GLN   A CB  1 
ATOM   840  C CG  . GLN   A 1 116 ? 20.39150  -7.80318  -7.37764  1.000 75.21884  ? 123 GLN   A CG  1 
ATOM   841  C CD  . GLN   A 1 116 ? 21.81291  -7.96035  -7.88121  1.000 92.23568  ? 123 GLN   A CD  1 
ATOM   842  O OE1 . GLN   A 1 116 ? 22.52071  -6.97598  -8.09336  1.000 105.87410 ? 123 GLN   A OE1 1 
ATOM   843  N NE2 . GLN   A 1 116 ? 22.24105  -9.20438  -8.06825  1.000 89.09727  ? 123 GLN   A NE2 1 
ATOM   844  N N   . ALA   A 1 117 ? 17.77360  -3.99571  -5.83786  1.000 71.36625  ? 124 ALA   A N   1 
ATOM   845  C CA  . ALA   A 1 117 ? 17.60584  -2.72221  -5.15042  1.000 65.09311  ? 124 ALA   A CA  1 
ATOM   846  C C   . ALA   A 1 117 ? 16.39071  -2.71883  -4.22664  1.000 78.04129  ? 124 ALA   A C   1 
ATOM   847  O O   . ALA   A 1 117 ? 15.87935  -1.64774  -3.88340  1.000 72.68190  ? 124 ALA   A O   1 
ATOM   848  C CB  . ALA   A 1 117 ? 17.50556  -1.58213  -6.16392  1.000 56.23019  ? 124 ALA   A CB  1 
ATOM   849  N N   . GLY   A 1 118 ? 15.90701  -3.89609  -3.82928  1.000 59.56796  ? 125 GLY   A N   1 
ATOM   850  C CA  . GLY   A 1 118 ? 14.87443  -4.01966  -2.82312  1.000 54.20417  ? 125 GLY   A CA  1 
ATOM   851  C C   . GLY   A 1 118 ? 13.53482  -4.50659  -3.33354  1.000 54.17417  ? 125 GLY   A C   1 
ATOM   852  O O   . GLY   A 1 118 ? 12.70007  -4.93122  -2.52312  1.000 48.73163  ? 125 GLY   A O   1 
ATOM   853  N N   . ALA   A 1 119 ? 13.29849  -4.45507  -4.64259  1.000 44.23554  ? 126 ALA   A N   1 
ATOM   854  C CA  . ALA   A 1 119 ? 12.01481  -4.86747  -5.18748  1.000 40.67610  ? 126 ALA   A CA  1 
ATOM   855  C C   . ALA   A 1 119 ? 11.81400  -6.37129  -5.01732  1.000 38.69986  ? 126 ALA   A C   1 
ATOM   856  O O   . ALA   A 1 119 ? 12.74414  -7.12878  -4.72767  1.000 39.84153  ? 126 ALA   A O   1 
ATOM   857  C CB  . ALA   A 1 119 ? 11.91173  -4.49115  -6.66526  1.000 41.04151  ? 126 ALA   A CB  1 
ATOM   858  N N   . ASP   A 1 120 ? 10.57172  -6.80321  -5.21465  1.000 37.56778  ? 127 ASP   A N   1 
ATOM   859  C CA  . ASP   A 1 120 ? 10.22179  -8.21252  -5.16872  1.000 37.80061  ? 127 ASP   A CA  1 
ATOM   860  C C   . ASP   A 1 120 ? 9.49970   -8.59131  -6.45235  1.000 35.41400  ? 127 ASP   A C   1 
ATOM   861  O O   . ASP   A 1 120 ? 9.11789   -7.73560  -7.25578  1.000 30.80315  ? 127 ASP   A O   1 
ATOM   862  C CB  . ASP   A 1 120 ? 9.34600   -8.53832  -3.95836  1.000 37.00140  ? 127 ASP   A CB  1 
ATOM   863  C CG  . ASP   A 1 120 ? 8.03102   -7.80564  -3.99275  1.000 48.08023  ? 127 ASP   A CG  1 
ATOM   864  O OD1 . ASP   A 1 120 ? 8.02066   -6.58854  -3.71684  1.000 47.23951  ? 127 ASP   A OD1 1 
ATOM   865  O OD2 . ASP   A 1 120 ? 7.01545   -8.44231  -4.33326  1.000 41.85184  ? 127 ASP   A OD2 1 
ATOM   866  N N   . ILE   A 1 121 ? 9.29505   -9.90054  -6.62104  1.000 30.56196  ? 128 ILE   A N   1 
ATOM   867  C CA  . ILE   A 1 121 ? 8.80019   -10.43545 -7.88666  1.000 28.64078  ? 128 ILE   A CA  1 
ATOM   868  C C   . ILE   A 1 121 ? 7.40053   -9.92204  -8.20401  1.000 30.42975  ? 128 ILE   A C   1 
ATOM   869  O O   . ILE   A 1 121 ? 7.03077   -9.79828  -9.37843  1.000 27.01626  ? 128 ILE   A O   1 
ATOM   870  C CB  . ILE   A 1 121 ? 8.87936   -11.97824 -7.85358  1.000 29.23899  ? 128 ILE   A CB  1 
ATOM   871  C CG1 . ILE   A 1 121 ? 10.34426  -12.41480 -7.99259  1.000 37.46977  ? 128 ILE   A CG1 1 
ATOM   872  C CG2 . ILE   A 1 121 ? 8.01979   -12.61579 -8.94319  1.000 29.28864  ? 128 ILE   A CG2 1 
ATOM   873  C CD1 . ILE   A 1 121 ? 10.60760  -13.86447 -7.64438  1.000 37.90332  ? 128 ILE   A CD1 1 
ATOM   874  N N   . SER   A 1 122 ? 6.61578   -9.56428  -7.18337  1.000 31.72550  ? 129 SER   A N   1 
ATOM   875  C CA  . SER   A 1 122 ? 5.25721   -9.08679  -7.44580  1.000 34.47711  ? 129 SER   A CA  1 
ATOM   876  C C   . SER   A 1 122 ? 5.22712   -7.79602  -8.26221  1.000 28.57430  ? 129 SER   A C   1 
ATOM   877  O O   . SER   A 1 122 ? 4.17747   -7.45095  -8.81664  1.000 31.00974  ? 129 SER   A O   1 
ATOM   878  C CB  . SER   A 1 122 ? 4.50342   -8.88078  -6.13069  1.000 27.65758  ? 129 SER   A CB  1 
ATOM   879  O OG  . SER   A 1 122 ? 4.92089   -7.68798  -5.49690  1.000 32.52051  ? 129 SER   A OG  1 
ATOM   880  N N   . MET   A 1 123 ? 6.34232   -7.07652  -8.34622  1.000 25.69341  ? 130 MET   A N   1 
ATOM   881  C CA  . MET   A 1 123 ? 6.42163   -5.81953  -9.08095  1.000 26.23460  ? 130 MET   A CA  1 
ATOM   882  C C   . MET   A 1 123 ? 6.72209   -6.01711  -10.56520 1.000 26.99821  ? 130 MET   A C   1 
ATOM   883  O O   . MET   A 1 123 ? 6.91383   -5.02492  -11.28087 1.000 26.14160  ? 130 MET   A O   1 
ATOM   884  C CB  . MET   A 1 123 ? 7.48297   -4.93054  -8.42846  1.000 29.50421  ? 130 MET   A CB  1 
ATOM   885  C CG  . MET   A 1 123 ? 7.43662   -5.02424  -6.90516  1.000 39.79168  ? 130 MET   A CG  1 
ATOM   886  S SD  . MET   A 1 123 ? 8.25459   -3.69708  -6.00910  1.000 45.36048  ? 130 MET   A SD  1 
ATOM   887  C CE  . MET   A 1 123 ? 7.91408   -2.28436  -7.06072  1.000 43.53903  ? 130 MET   A CE  1 
ATOM   888  N N   . ILE   A 1 124 ? 6.73369   -7.27266  -11.02840 1.000 21.65940  ? 131 ILE   A N   1 
ATOM   889  C CA  . ILE   A 1 124 ? 7.19222   -7.61107  -12.37761 1.000 22.99179  ? 131 ILE   A CA  1 
ATOM   890  C C   . ILE   A 1 124 ? 6.40921   -6.84910  -13.44405 1.000 21.86879  ? 131 ILE   A C   1 
ATOM   891  O O   . ILE   A 1 124 ? 6.97153   -6.43453  -14.46715 1.000 19.92903  ? 131 ILE   A O   1 
ATOM   892  C CB  . ILE   A 1 124 ? 7.10277   -9.13594  -12.59366 1.000 23.27460  ? 131 ILE   A CB  1 
ATOM   893  C CG1 . ILE   A 1 124 ? 7.68863   -9.52789  -13.95459 1.000 25.35224  ? 131 ILE   A CG1 1 
ATOM   894  C CG2 . ILE   A 1 124 ? 5.65598   -9.62699  -12.44483 1.000 21.94698  ? 131 ILE   A CG2 1 
ATOM   895  C CD1 . ILE   A 1 124 ? 7.82724   -11.02577 -14.15161 1.000 25.38843  ? 131 ILE   A CD1 1 
ATOM   896  N N   . GLY   A 1 125 ? 5.10718   -6.65173  -13.22906 1.000 22.70051  ? 132 GLY   A N   1 
ATOM   897  C CA  . GLY   A 1 125 ? 4.28065   -5.97585  -14.21685 1.000 21.41797  ? 132 GLY   A CA  1 
ATOM   898  C C   . GLY   A 1 125 ? 4.65458   -4.52808  -14.45390 1.000 27.11939  ? 132 GLY   A C   1 
ATOM   899  O O   . GLY   A 1 125 ? 4.37676   -3.99479  -15.53424 1.000 25.64458  ? 132 GLY   A O   1 
ATOM   900  N N   . GLN   A 1 126 ? 5.26202   -3.87287  -13.46340 1.000 21.81416  ? 133 GLN   A N   1 
ATOM   901  C CA  . GLN   A 1 126 ? 5.74165   -2.51119  -13.66086 1.000 24.79220  ? 133 GLN   A CA  1 
ATOM   902  C C   . GLN   A 1 126 ? 6.87029   -2.42531  -14.67510 1.000 27.93074  ? 133 GLN   A C   1 
ATOM   903  O O   . GLN   A 1 126 ? 7.23349   -1.31479  -15.07868 1.000 28.05704  ? 133 GLN   A O   1 
ATOM   904  C CB  . GLN   A 1 126 ? 6.20209   -1.92059  -12.33319 1.000 30.40505  ? 133 GLN   A CB  1 
ATOM   905  C CG  . GLN   A 1 126 ? 5.06628   -1.65068  -11.37300 1.000 33.76402  ? 133 GLN   A CG  1 
ATOM   906  C CD  . GLN   A 1 126 ? 5.55801   -1.21298  -10.01442 1.000 43.10363  ? 133 GLN   A CD  1 
ATOM   907  O OE1 . GLN   A 1 126 ? 5.32154   -1.88699  -9.01145  1.000 58.06166  ? 133 GLN   A OE1 1 
ATOM   908  N NE2 . GLN   A 1 126 ? 6.27395   -0.09448  -9.97615  1.000 43.63683  ? 133 GLN   A NE2 1 
ATOM   909  N N   . PHE   A 1 127 ? 7.42921   -3.55848  -15.09130 1.000 25.75401  ? 134 PHE   A N   1 
ATOM   910  C CA  . PHE   A 1 127 ? 8.54714   -3.58985  -16.02314 1.000 23.40667  ? 134 PHE   A CA  1 
ATOM   911  C C   . PHE   A 1 127 ? 8.16706   -4.21263  -17.35968 1.000 31.00109  ? 134 PHE   A C   1 
ATOM   912  O O   . PHE   A 1 127 ? 9.04792   -4.49005  -18.18024 1.000 24.68738  ? 134 PHE   A O   1 
ATOM   913  C CB  . PHE   A 1 127 ? 9.72152   -4.33043  -15.38390 1.000 23.11995  ? 134 PHE   A CB  1 
ATOM   914  C CG  . PHE   A 1 127 ? 10.13363  -3.75215  -14.06563 1.000 26.11480  ? 134 PHE   A CG  1 
ATOM   915  C CD1 . PHE   A 1 127 ? 10.97526  -2.65845  -14.01140 1.000 36.53852  ? 134 PHE   A CD1 1 
ATOM   916  C CD2 . PHE   A 1 127 ? 9.62779   -4.26216  -12.88367 1.000 28.80395  ? 134 PHE   A CD2 1 
ATOM   917  C CE1 . PHE   A 1 127 ? 11.33865  -2.10843  -12.79822 1.000 33.91448  ? 134 PHE   A CE1 1 
ATOM   918  C CE2 . PHE   A 1 127 ? 9.98560   -3.71959  -11.66832 1.000 29.17785  ? 134 PHE   A CE2 1 
ATOM   919  C CZ  . PHE   A 1 127 ? 10.84275  -2.63950  -11.62593 1.000 32.05115  ? 134 PHE   A CZ  1 
ATOM   920  N N   . GLY   A 1 128 ? 6.87779   -4.44545  -17.59120 1.000 23.09940  ? 135 GLY   A N   1 
ATOM   921  C CA  . GLY   A 1 128 ? 6.39465   -4.87109  -18.88843 1.000 22.46423  ? 135 GLY   A CA  1 
ATOM   922  C C   . GLY   A 1 128 ? 6.64098   -6.32025  -19.23758 1.000 19.96510  ? 135 GLY   A C   1 
ATOM   923  O O   . GLY   A 1 128 ? 6.49949   -6.68518  -20.40938 1.000 24.80849  ? 135 GLY   A O   1 
ATOM   924  N N   . VAL   A 1 129 ? 6.99713   -7.15890  -18.26672 1.000 18.23996  ? 136 VAL   A N   1 
ATOM   925  C CA  . VAL   A 1 129 ? 7.29067   -8.56487  -18.52823 1.000 15.09444  ? 136 VAL   A CA  1 
ATOM   926  C C   . VAL   A 1 129 ? 6.47211   -9.44987  -17.59586 1.000 16.38470  ? 136 VAL   A C   1 
ATOM   927  O O   . VAL   A 1 129 ? 6.88092   -10.57064 -17.26445 1.000 15.91914  ? 136 VAL   A O   1 
ATOM   928  C CB  . VAL   A 1 129 ? 8.79747   -8.84242  -18.38502 1.000 22.17202  ? 136 VAL   A CB  1 
ATOM   929  C CG1 . VAL   A 1 129 ? 9.56063   -8.21416  -19.55475 1.000 20.71235  ? 136 VAL   A CG1 1 
ATOM   930  C CG2 . VAL   A 1 129 ? 9.31180   -8.28921  -17.06531 1.000 22.16561  ? 136 VAL   A CG2 1 
ATOM   931  N N   . GLY   A 1 130 ? 5.30489   -8.95475  -17.17890 1.000 18.75865  ? 137 GLY   A N   1 
ATOM   932  C CA  . GLY   A 1 130 ? 4.43052   -9.71001  -16.29378 1.000 14.81883  ? 137 GLY   A CA  1 
ATOM   933  C C   . GLY   A 1 130 ? 3.99628   -11.05962 -16.83390 1.000 18.16731  ? 137 GLY   A C   1 
ATOM   934  O O   . GLY   A 1 130 ? 3.66146   -11.94798 -16.04290 1.000 18.03985  ? 137 GLY   A O   1 
ATOM   935  N N   . PHE   A 1 131 ? 3.99389   -11.23804 -18.16077 1.000 16.95941  ? 138 PHE   A N   1 
ATOM   936  C CA  . PHE   A 1 131 ? 3.59183   -12.52138 -18.73597 1.000 15.37580  ? 138 PHE   A CA  1 
ATOM   937  C C   . PHE   A 1 131 ? 4.40178   -13.67370 -18.15513 1.000 15.04005  ? 138 PHE   A C   1 
ATOM   938  O O   . PHE   A 1 131 ? 3.86093   -14.75029 -17.87706 1.000 16.72070  ? 138 PHE   A O   1 
ATOM   939  C CB  . PHE   A 1 131 ? 3.75253   -12.50122 -20.25794 1.000 18.99955  ? 138 PHE   A CB  1 
ATOM   940  C CG  . PHE   A 1 131 ? 3.71663   -13.87235 -20.88702 1.000 19.10253  ? 138 PHE   A CG  1 
ATOM   941  C CD1 . PHE   A 1 131 ? 2.51389   -14.55253 -21.03714 1.000 17.34186  ? 138 PHE   A CD1 1 
ATOM   942  C CD2 . PHE   A 1 131 ? 4.88857   -14.49622 -21.29749 1.000 18.01160  ? 138 PHE   A CD2 1 
ATOM   943  C CE1 . PHE   A 1 131 ? 2.47377   -15.82149 -21.61025 1.000 14.17407  ? 138 PHE   A CE1 1 
ATOM   944  C CE2 . PHE   A 1 131 ? 4.85800   -15.76890 -21.86203 1.000 14.55160  ? 138 PHE   A CE2 1 
ATOM   945  C CZ  . PHE   A 1 131 ? 3.65350   -16.43014 -22.01731 1.000 17.25081  ? 138 PHE   A CZ  1 
ATOM   946  N N   . TYR   A 1 132 ? 5.70412   -13.46794 -17.97597 1.000 16.30036  ? 139 TYR   A N   1 
ATOM   947  C CA  . TYR   A 1 132 ? 6.58921   -14.54655 -17.55377 1.000 16.24564  ? 139 TYR   A CA  1 
ATOM   948  C C   . TYR   A 1 132 ? 6.34315   -14.97539 -16.11395 1.000 19.39239  ? 139 TYR   A C   1 
ATOM   949  O O   . TYR   A 1 132 ? 6.84487   -16.02950 -15.71080 1.000 19.31323  ? 139 TYR   A O   1 
ATOM   950  C CB  . TYR   A 1 132 ? 8.04751   -14.11849 -17.77024 1.000 14.68896  ? 139 TYR   A CB  1 
ATOM   951  C CG  . TYR   A 1 132 ? 8.31233   -13.83074 -19.23535 1.000 16.66294  ? 139 TYR   A CG  1 
ATOM   952  C CD1 . TYR   A 1 132 ? 8.57905   -14.86155 -20.13026 1.000 16.03264  ? 139 TYR   A CD1 1 
ATOM   953  C CD2 . TYR   A 1 132 ? 8.23767   -12.53292 -19.73365 1.000 18.33727  ? 139 TYR   A CD2 1 
ATOM   954  C CE1 . TYR   A 1 132 ? 8.79914   -14.60292 -21.48330 1.000 18.88309  ? 139 TYR   A CE1 1 
ATOM   955  C CE2 . TYR   A 1 132 ? 8.44557   -12.26726 -21.07625 1.000 21.28721  ? 139 TYR   A CE2 1 
ATOM   956  C CZ  . TYR   A 1 132 ? 8.72208   -13.30240 -21.94660 1.000 20.51778  ? 139 TYR   A CZ  1 
ATOM   957  O OH  . TYR   A 1 132 ? 8.92232   -13.03708 -23.27984 1.000 18.65808  ? 139 TYR   A OH  1 
ATOM   958  N N   . SER   A 1 133 ? 5.56659   -14.20953 -15.34223 1.000 14.13398  ? 140 SER   A N   1 
ATOM   959  C CA  . SER   A 1 133 ? 5.12964   -14.67712 -14.03224 1.000 18.05268  ? 140 SER   A CA  1 
ATOM   960  C C   . SER   A 1 133 ? 4.24647   -15.90795 -14.13197 1.000 14.57148  ? 140 SER   A C   1 
ATOM   961  O O   . SER   A 1 133 ? 4.01448   -16.56190 -13.10835 1.000 16.41707  ? 140 SER   A O   1 
ATOM   962  C CB  . SER   A 1 133 ? 4.37480   -13.57866 -13.27304 1.000 17.77322  ? 140 SER   A CB  1 
ATOM   963  O OG  . SER   A 1 133 ? 3.08444   -13.36747 -13.82379 1.000 16.97272  ? 140 SER   A OG  1 
ATOM   964  N N   . ALA   A 1 134 ? 3.75568   -16.23810 -15.33288 1.000 16.14172  ? 141 ALA   A N   1 
ATOM   965  C CA  . ALA   A 1 134 ? 3.06148   -17.50854 -15.53329 1.000 14.79921  ? 141 ALA   A CA  1 
ATOM   966  C C   . ALA   A 1 134 ? 3.87880   -18.68054 -15.01648 1.000 18.58943  ? 141 ALA   A C   1 
ATOM   967  O O   . ALA   A 1 134 ? 3.31833   -19.65395 -14.49707 1.000 17.50189  ? 141 ALA   A O   1 
ATOM   968  C CB  . ALA   A 1 134 ? 2.75498   -17.71365 -17.01682 1.000 12.96505  ? 141 ALA   A CB  1 
ATOM   969  N N   . TYR   A 1 135 ? 5.20486   -18.60402 -15.13613 1.000 17.15590  ? 142 TYR   A N   1 
ATOM   970  C CA  . TYR   A 1 135 ? 6.05436   -19.72153 -14.75159 1.000 14.35865  ? 142 TYR   A CA  1 
ATOM   971  C C   . TYR   A 1 135 ? 6.23782   -19.82539 -13.24175 1.000 16.65493  ? 142 TYR   A C   1 
ATOM   972  O O   . TYR   A 1 135 ? 6.95651   -20.71378 -12.77493 1.000 18.39805  ? 142 TYR   A O   1 
ATOM   973  C CB  . TYR   A 1 135 ? 7.39148   -19.61024 -15.49742 1.000 16.65061  ? 142 TYR   A CB  1 
ATOM   974  C CG  . TYR   A 1 135 ? 7.19373   -19.89614 -16.96970 1.000 19.29017  ? 142 TYR   A CG  1 
ATOM   975  C CD1 . TYR   A 1 135 ? 7.17208   -21.20232 -17.44464 1.000 17.38134  ? 142 TYR   A CD1 1 
ATOM   976  C CD2 . TYR   A 1 135 ? 6.94617   -18.86465 -17.87425 1.000 14.53354  ? 142 TYR   A CD2 1 
ATOM   977  C CE1 . TYR   A 1 135 ? 6.96039   -21.47733 -18.79028 1.000 17.07056  ? 142 TYR   A CE1 1 
ATOM   978  C CE2 . TYR   A 1 135 ? 6.71963   -19.12887 -19.22191 1.000 14.34564  ? 142 TYR   A CE2 1 
ATOM   979  C CZ  . TYR   A 1 135 ? 6.73517   -20.43662 -19.67239 1.000 19.36070  ? 142 TYR   A CZ  1 
ATOM   980  O OH  . TYR   A 1 135 ? 6.51925   -20.70266 -21.00357 1.000 16.89319  ? 142 TYR   A OH  1 
ATOM   981  N N   . LEU   A 1 136 ? 5.58395   -18.95360 -12.47190 1.000 18.72928  ? 143 LEU   A N   1 
ATOM   982  C CA  . LEU   A 1 136 ? 5.45761   -19.17255 -11.03594 1.000 20.05476  ? 143 LEU   A CA  1 
ATOM   983  C C   . LEU   A 1 136 ? 4.60090   -20.39456 -10.73281 1.000 18.30164  ? 143 LEU   A C   1 
ATOM   984  O O   . LEU   A 1 136 ? 4.81347   -21.06022 -9.71239  1.000 21.10594  ? 143 LEU   A O   1 
ATOM   985  C CB  . LEU   A 1 136 ? 4.84227   -17.94279 -10.36585 1.000 17.50409  ? 143 LEU   A CB  1 
ATOM   986  C CG  . LEU   A 1 136 ? 5.70869   -16.68405 -10.30285 1.000 17.74684  ? 143 LEU   A CG  1 
ATOM   987  C CD1 . LEU   A 1 136 ? 4.87220   -15.50021 -9.83321  1.000 20.08286  ? 143 LEU   A CD1 1 
ATOM   988  C CD2 . LEU   A 1 136 ? 6.91890   -16.91928 -9.40234  1.000 19.52471  ? 143 LEU   A CD2 1 
ATOM   989  N N   . VAL   A 1 137 ? 3.63646   -20.70876 -11.60294 1.000 16.68146  ? 144 VAL   A N   1 
ATOM   990  C CA  . VAL   A 1 137 ? 2.66808   -21.76379 -11.31093 1.000 17.41260  ? 144 VAL   A CA  1 
ATOM   991  C C   . VAL   A 1 137 ? 2.58450   -22.79814 -12.43020 1.000 21.10261  ? 144 VAL   A C   1 
ATOM   992  O O   . VAL   A 1 137 ? 2.03256   -23.88437 -12.22866 1.000 21.42246  ? 144 VAL   A O   1 
ATOM   993  C CB  . VAL   A 1 137 ? 1.27211   -21.17375 -11.01782 1.000 18.85850  ? 144 VAL   A CB  1 
ATOM   994  C CG1 . VAL   A 1 137 ? 1.31532   -20.24347 -9.80035  1.000 18.74391  ? 144 VAL   A CG1 1 
ATOM   995  C CG2 . VAL   A 1 137 ? 0.69985   -20.45358 -12.24445 1.000 16.33260  ? 144 VAL   A CG2 1 
ATOM   996  N N   . ALA   A 1 138 ? 3.13907   -22.49392 -13.60336 1.000 19.13794  ? 145 ALA   A N   1 
ATOM   997  C CA  . ALA   A 1 138 ? 3.00286   -23.35215 -14.77744 1.000 16.74211  ? 145 ALA   A CA  1 
ATOM   998  C C   . ALA   A 1 138 ? 4.33737   -23.98728 -15.13802 1.000 19.63338  ? 145 ALA   A C   1 
ATOM   999  O O   . ALA   A 1 138 ? 5.36381   -23.30004 -15.19036 1.000 20.30391  ? 145 ALA   A O   1 
ATOM   1000 C CB  . ALA   A 1 138 ? 2.47007   -22.56215 -15.97679 1.000 15.63789  ? 145 ALA   A CB  1 
ATOM   1001 N N   . GLU   A 1 139 ? 4.32175   -25.29604 -15.39937 1.000 17.94189  ? 146 GLU   A N   1 
ATOM   1002 C CA  . GLU   A 1 139 ? 5.51365   -25.93615 -15.94686 1.000 19.26713  ? 146 GLU   A CA  1 
ATOM   1003 C C   . GLU   A 1 139 ? 5.61380   -25.75049 -17.45223 1.000 21.72148  ? 146 GLU   A C   1 
ATOM   1004 O O   . GLU   A 1 139 ? 6.70536   -25.87399 -18.01492 1.000 22.27362  ? 146 GLU   A O   1 
ATOM   1005 C CB  . GLU   A 1 139 ? 5.53307   -27.43065 -15.61971 1.000 26.26602  ? 146 GLU   A CB  1 
ATOM   1006 C CG  . GLU   A 1 139 ? 4.41050   -28.21669 -16.26074 1.000 28.28314  ? 146 GLU   A CG  1 
ATOM   1007 C CD  . GLU   A 1 139 ? 4.16222   -29.55603 -15.58899 1.000 58.36345  ? 146 GLU   A CD  1 
ATOM   1008 O OE1 . GLU   A 1 139 ? 4.84992   -29.86480 -14.59233 1.000 42.21034  ? 146 GLU   A OE1 1 
ATOM   1009 O OE2 . GLU   A 1 139 ? 3.28415   -30.30591 -16.07051 1.000 55.55505  ? 146 GLU   A OE2 1 
ATOM   1010 N N   . LYS   A 1 140 ? 4.49732   -25.46044 -18.11046 1.000 18.43567  ? 147 LYS   A N   1 
ATOM   1011 C CA  . LYS   A 1 140 ? 4.45721   -25.24157 -19.54488 1.000 18.58812  ? 147 LYS   A CA  1 
ATOM   1012 C C   . LYS   A 1 140 ? 3.37052   -24.21581 -19.80491 1.000 18.19490  ? 147 LYS   A C   1 
ATOM   1013 O O   . LYS   A 1 140 ? 2.33874   -24.21679 -19.12583 1.000 17.51498  ? 147 LYS   A O   1 
ATOM   1014 C CB  . LYS   A 1 140 ? 4.17267   -26.54814 -20.29457 1.000 19.94805  ? 147 LYS   A CB  1 
ATOM   1015 C CG  . LYS   A 1 140 ? 4.04925   -26.42716 -21.79859 1.000 17.28843  ? 147 LYS   A CG  1 
ATOM   1016 C CD  . LYS   A 1 140 ? 4.04307   -27.81444 -22.41343 1.000 23.80507  ? 147 LYS   A CD  1 
ATOM   1017 C CE  . LYS   A 1 140 ? 2.75473   -28.07158 -23.15788 1.000 40.18516  ? 147 LYS   A CE  1 
ATOM   1018 N NZ  . LYS   A 1 140 ? 2.45199   -29.52770 -23.22515 1.000 35.48035  ? 147 LYS   A NZ  1 
ATOM   1019 N N   . VAL   A 1 141 ? 3.60853   -23.32226 -20.75811 1.000 15.36683  ? 148 VAL   A N   1 
ATOM   1020 C CA  . VAL   A 1 141 ? 2.60639   -22.33143 -21.13837 1.000 14.71781  ? 148 VAL   A CA  1 
ATOM   1021 C C   . VAL   A 1 141 ? 2.40888   -22.41418 -22.64332 1.000 18.46011  ? 148 VAL   A C   1 
ATOM   1022 O O   . VAL   A 1 141 ? 3.38639   -22.44473 -23.40054 1.000 14.47507  ? 148 VAL   A O   1 
ATOM   1023 C CB  . VAL   A 1 141 ? 3.00937   -20.90450 -20.72198 1.000 14.93274  ? 148 VAL   A CB  1 
ATOM   1024 C CG1 . VAL   A 1 141 ? 1.95699   -19.89461 -21.20534 1.000 16.79072  ? 148 VAL   A CG1 1 
ATOM   1025 C CG2 . VAL   A 1 141 ? 3.21168   -20.81897 -19.20788 1.000 16.25615  ? 148 VAL   A CG2 1 
ATOM   1026 N N   . THR   A 1 142 ? 1.14774   -22.47684 -23.07154 1.000 14.42324  ? 149 THR   A N   1 
ATOM   1027 C CA  . THR   A 1 142 ? 0.77830   -22.47497 -24.48011 1.000 13.47499  ? 149 THR   A CA  1 
ATOM   1028 C C   . THR   A 1 142 ? -0.02602  -21.21137 -24.75664 1.000 16.51709  ? 149 THR   A C   1 
ATOM   1029 O O   . THR   A 1 142 ? -0.98358  -20.91206 -24.03638 1.000 20.67388  ? 149 THR   A O   1 
ATOM   1030 C CB  . THR   A 1 142 ? -0.04960  -23.71376 -24.84612 1.000 13.96819  ? 149 THR   A CB  1 
ATOM   1031 O OG1 . THR   A 1 142 ? 0.64506   -24.89824 -24.44434 1.000 20.05405  ? 149 THR   A OG1 1 
ATOM   1032 C CG2 . THR   A 1 142 ? -0.29105  -23.76399 -26.34822 1.000 19.36303  ? 149 THR   A CG2 1 
ATOM   1033 N N   . VAL   A 1 143 ? 0.35894   -20.46405 -25.78680 1.000 13.21698  ? 150 VAL   A N   1 
ATOM   1034 C CA  . VAL   A 1 143 ? -0.34076  -19.23229 -26.14625 1.000 14.66906  ? 150 VAL   A CA  1 
ATOM   1035 C C   . VAL   A 1 143 ? -0.90701  -19.40703 -27.54689 1.000 19.19924  ? 150 VAL   A C   1 
ATOM   1036 O O   . VAL   A 1 143 ? -0.14883  -19.56166 -28.51265 1.000 18.30600  ? 150 VAL   A O   1 
ATOM   1037 C CB  . VAL   A 1 143 ? 0.57585   -17.99876 -26.07776 1.000 15.79622  ? 150 VAL   A CB  1 
ATOM   1038 C CG1 . VAL   A 1 143 ? -0.18197  -16.74357 -26.55419 1.000 16.97774  ? 150 VAL   A CG1 1 
ATOM   1039 C CG2 . VAL   A 1 143 ? 1.10402   -17.79521 -24.67071 1.000 17.86402  ? 150 VAL   A CG2 1 
ATOM   1040 N N   . ILE   A 1 144 ? -2.23367  -19.39804 -27.65584 1.000 14.58744  ? 151 ILE   A N   1 
ATOM   1041 C CA  . ILE   A 1 144 ? -2.92620  -19.42108 -28.94026 1.000 15.25325  ? 151 ILE   A CA  1 
ATOM   1042 C C   . ILE   A 1 144 ? -3.39510  -18.00800 -29.22747 1.000 18.59214  ? 151 ILE   A C   1 
ATOM   1043 O O   . ILE   A 1 144 ? -3.96731  -17.35688 -28.34894 1.000 16.04435  ? 151 ILE   A O   1 
ATOM   1044 C CB  . ILE   A 1 144 ? -4.12828  -20.37960 -28.92154 1.000 18.82900  ? 151 ILE   A CB  1 
ATOM   1045 C CG1 . ILE   A 1 144 ? -3.79683  -21.67599 -28.17982 1.000 27.59772  ? 151 ILE   A CG1 1 
ATOM   1046 C CG2 . ILE   A 1 144 ? -4.59239  -20.64311 -30.34210 1.000 23.21577  ? 151 ILE   A CG2 1 
ATOM   1047 C CD1 . ILE   A 1 144 ? -2.84199  -22.56003 -28.91000 1.000 22.87404  ? 151 ILE   A CD1 1 
ATOM   1048 N N   . THR   A 1 145 ? -3.17508  -17.52536 -30.44700 1.000 14.80665  ? 152 THR   A N   1 
ATOM   1049 C CA  . THR   A 1 145 ? -3.49257  -16.12350 -30.68904 1.000 15.05750  ? 152 THR   A CA  1 
ATOM   1050 C C   . THR   A 1 145 ? -3.89172  -15.90538 -32.14046 1.000 19.84429  ? 152 THR   A C   1 
ATOM   1051 O O   . THR   A 1 145 ? -3.41872  -16.59563 -33.04627 1.000 19.07941  ? 152 THR   A O   1 
ATOM   1052 C CB  . THR   A 1 145 ? -2.31521  -15.21324 -30.29409 1.000 19.28731  ? 152 THR   A CB  1 
ATOM   1053 O OG1 . THR   A 1 145 ? -2.75853  -13.85353 -30.22988 1.000 18.54907  ? 152 THR   A OG1 1 
ATOM   1054 C CG2 . THR   A 1 145 ? -1.16241  -15.33731 -31.28133 1.000 19.70544  ? 152 THR   A CG2 1 
ATOM   1055 N N   . LYS   A 1 146 ? -4.78161  -14.93344 -32.34256 1.000 16.89047  ? 153 LYS   A N   1 
ATOM   1056 C CA  . LYS   A 1 146 ? -5.26457  -14.56836 -33.66982 1.000 16.01916  ? 153 LYS   A CA  1 
ATOM   1057 C C   . LYS   A 1 146 ? -5.39059  -13.05572 -33.73779 1.000 19.72598  ? 153 LYS   A C   1 
ATOM   1058 O O   . LYS   A 1 146 ? -6.17666  -12.45917 -32.99355 1.000 17.70503  ? 153 LYS   A O   1 
ATOM   1059 C CB  . LYS   A 1 146 ? -6.61174  -15.23118 -33.97544 1.000 17.78194  ? 153 LYS   A CB  1 
ATOM   1060 C CG  . LYS   A 1 146 ? -7.24647  -14.78838 -35.29398 1.000 20.36770  ? 153 LYS   A CG  1 
ATOM   1061 C CD  . LYS   A 1 146 ? -6.45307  -15.31860 -36.48830 1.000 24.71770  ? 153 LYS   A CD  1 
ATOM   1062 C CE  . LYS   A 1 146 ? -7.13451  -14.97907 -37.80711 1.000 23.34227  ? 153 LYS   A CE  1 
ATOM   1063 N NZ  . LYS   A 1 146 ? -7.08857  -13.51960 -38.12222 1.000 19.29811  ? 153 LYS   A NZ  1 
ATOM   1064 N N   . HIS   A 1 147 ? -4.61695  -12.44978 -34.62737 1.000 20.62625  ? 154 HIS   A N   1 
ATOM   1065 C CA  . HIS   A 1 147 ? -4.62012  -11.01791 -34.88243 1.000 18.21985  ? 154 HIS   A CA  1 
ATOM   1066 C C   . HIS   A 1 147 ? -5.31393  -10.78712 -36.21925 1.000 22.06801  ? 154 HIS   A C   1 
ATOM   1067 O O   . HIS   A 1 147 ? -5.21735  -11.62730 -37.11793 1.000 21.61397  ? 154 HIS   A O   1 
ATOM   1068 C CB  . HIS   A 1 147 ? -3.17097  -10.50107 -34.89135 1.000 17.47243  ? 154 HIS   A CB  1 
ATOM   1069 C CG  . HIS   A 1 147 ? -3.03227  -9.01435  -35.01185 1.000 19.14036  ? 154 HIS   A CG  1 
ATOM   1070 N ND1 . HIS   A 1 147 ? -3.27401  -8.33426  -36.18468 1.000 19.54399  ? 154 HIS   A ND1 1 
ATOM   1071 C CD2 . HIS   A 1 147 ? -2.63593  -8.08342  -34.11295 1.000 16.59635  ? 154 HIS   A CD2 1 
ATOM   1072 C CE1 . HIS   A 1 147 ? -3.05501  -7.04473  -35.99791 1.000 27.20039  ? 154 HIS   A CE1 1 
ATOM   1073 N NE2 . HIS   A 1 147 ? -2.66248  -6.86642  -34.74942 1.000 22.30160  ? 154 HIS   A NE2 1 
ATOM   1074 N N   . ASN   A 1 148 ? -6.04239  -9.67054  -36.34900 1.000 20.27209  ? 155 ASN   A N   1 
ATOM   1075 C CA  . ASN   A 1 148 ? -6.75031  -9.41364  -37.60531 1.000 19.86480  ? 155 ASN   A CA  1 
ATOM   1076 C C   . ASN   A 1 148 ? -5.83512  -9.52016  -38.82065 1.000 21.96311  ? 155 ASN   A C   1 
ATOM   1077 O O   . ASN   A 1 148 ? -6.28717  -9.90779  -39.90571 1.000 24.64114  ? 155 ASN   A O   1 
ATOM   1078 C CB  . ASN   A 1 148 ? -7.41080  -8.03087  -37.59290 1.000 21.89864  ? 155 ASN   A CB  1 
ATOM   1079 C CG  . ASN   A 1 148 ? -8.67055  -7.99117  -36.75866 1.000 21.44555  ? 155 ASN   A CG  1 
ATOM   1080 O OD1 . ASN   A 1 148 ? -9.35281  -9.00277  -36.59403 1.000 28.88277  ? 155 ASN   A OD1 1 
ATOM   1081 N ND2 . ASN   A 1 148 ? -8.99404  -6.81466  -36.23009 1.000 23.97405  ? 155 ASN   A ND2 1 
ATOM   1082 N N   . ASP   A 1 149 ? -4.55226  -9.19796  -38.66479 1.000 22.52051  ? 156 ASP   A N   1 
ATOM   1083 C CA  . ASP   A 1 149 ? -3.63301  -9.09933  -39.79155 1.000 28.51538  ? 156 ASP   A CA  1 
ATOM   1084 C C   . ASP   A 1 149 ? -2.81388  -10.36619 -40.03172 1.000 29.12954  ? 156 ASP   A C   1 
ATOM   1085 O O   . ASP   A 1 149 ? -1.89837  -10.33996 -40.86140 1.000 30.13499  ? 156 ASP   A O   1 
ATOM   1086 C CB  . ASP   A 1 149 ? -2.68161  -7.91491  -39.59498 1.000 29.71887  ? 156 ASP   A CB  1 
ATOM   1087 C CG  . ASP   A 1 149 ? -3.39565  -6.57672  -39.60195 1.000 36.48344  ? 156 ASP   A CG  1 
ATOM   1088 O OD1 . ASP   A 1 149 ? -4.53888  -6.50241  -40.09896 1.000 29.26659  ? 156 ASP   A OD1 1 
ATOM   1089 O OD2 . ASP   A 1 149 ? -2.80459  -5.59493  -39.10653 1.000 38.86866  ? 156 ASP   A OD2 1 
ATOM   1090 N N   . ASP   A 1 150 ? -3.10932  -11.46910 -39.34364 1.000 28.85139  ? 157 ASP   A N   1 
ATOM   1091 C CA  . ASP   A 1 150 ? -2.29626  -12.67443 -39.47600 1.000 22.87591  ? 157 ASP   A CA  1 
ATOM   1092 C C   . ASP   A 1 150 ? -3.16892  -13.90731 -39.24930 1.000 32.86522  ? 157 ASP   A C   1 
ATOM   1093 O O   . ASP   A 1 150 ? -4.36790  -13.80638 -38.97130 1.000 24.43557  ? 157 ASP   A O   1 
ATOM   1094 C CB  . ASP   A 1 150 ? -1.10487  -12.63251 -38.50703 1.000 23.12496  ? 157 ASP   A CB  1 
ATOM   1095 C CG  . ASP   A 1 150 ? 0.09450   -13.41593 -39.01312 1.000 27.34070  ? 157 ASP   A CG  1 
ATOM   1096 O OD1 . ASP   A 1 150 ? -0.06560  -14.20992 -39.96452 1.000 28.81765  ? 157 ASP   A OD1 1 
ATOM   1097 O OD2 . ASP   A 1 150 ? 1.20147   -13.23347 -38.45827 1.000 28.80814  ? 157 ASP   A OD2 1 
ATOM   1098 N N   . GLU   A 1 151 ? -2.55358  -15.08172 -39.38561 1.000 28.65963  ? 158 GLU   A N   1 
ATOM   1099 C CA  . GLU   A 1 151 ? -3.21598  -16.35508 -39.14657 1.000 21.51132  ? 158 GLU   A CA  1 
ATOM   1100 C C   . GLU   A 1 151 ? -3.16130  -16.71517 -37.66154 1.000 18.81877  ? 158 GLU   A C   1 
ATOM   1101 O O   . GLU   A 1 151 ? -2.49941  -16.05527 -36.85514 1.000 21.13955  ? 158 GLU   A O   1 
ATOM   1102 C CB  . GLU   A 1 151 ? -2.56409  -17.46819 -39.96774 1.000 26.31147  ? 158 GLU   A CB  1 
ATOM   1103 C CG  . GLU   A 1 151 ? -2.44107  -17.17389 -41.45089 1.000 44.60531  ? 158 GLU   A CG  1 
ATOM   1104 C CD  . GLU   A 1 151 ? -1.50887  -18.14673 -42.15775 1.000 83.71132  ? 158 GLU   A CD  1 
ATOM   1105 O OE1 . GLU   A 1 151 ? -1.34908  -19.28585 -41.66742 1.000 64.74082  ? 158 GLU   A OE1 1 
ATOM   1106 O OE2 . GLU   A 1 151 ? -0.92727  -17.76860 -43.19823 1.000 80.12154  ? 158 GLU   A OE2 1 
ATOM   1107 N N   . GLN   A 1 152 ? -3.86755  -17.78492 -37.30125 1.000 19.26254  ? 159 GLN   A N   1 
ATOM   1108 C CA  . GLN   A 1 152 ? -3.86133  -18.26419 -35.92407 1.000 19.96655  ? 159 GLN   A CA  1 
ATOM   1109 C C   . GLN   A 1 152 ? -2.59888  -19.07189 -35.65490 1.000 19.96026  ? 159 GLN   A C   1 
ATOM   1110 O O   . GLN   A 1 152 ? -2.26823  -19.99411 -36.40797 1.000 19.43769  ? 159 GLN   A O   1 
ATOM   1111 C CB  . GLN   A 1 152 ? -5.09563  -19.11882 -35.63919 1.000 23.52423  ? 159 GLN   A CB  1 
ATOM   1112 C CG  . GLN   A 1 152 ? -5.35434  -19.34289 -34.14932 1.000 22.06420  ? 159 GLN   A CG  1 
ATOM   1113 C CD  . GLN   A 1 152 ? -6.77450  -19.79165 -33.86172 1.000 23.95744  ? 159 GLN   A CD  1 
ATOM   1114 O OE1 . GLN   A 1 152 ? -7.73161  -19.10190 -34.20318 1.000 26.65207  ? 159 GLN   A OE1 1 
ATOM   1115 N NE2 . GLN   A 1 152 ? -6.91653  -20.94968 -33.22692 1.000 28.42423  ? 159 GLN   A NE2 1 
ATOM   1116 N N   . TYR   A 1 153 ? -1.90471  -18.73332 -34.57065 1.000 18.87132  ? 160 TYR   A N   1 
ATOM   1117 C CA  . TYR   A 1 153 ? -0.63706  -19.35728 -34.22931 1.000 18.49856  ? 160 TYR   A CA  1 
ATOM   1118 C C   . TYR   A 1 153 ? -0.66190  -19.86189 -32.79387 1.000 20.02867  ? 160 TYR   A C   1 
ATOM   1119 O O   . TYR   A 1 153 ? -1.40510  -19.35562 -31.94901 1.000 18.70010  ? 160 TYR   A O   1 
ATOM   1120 C CB  . TYR   A 1 153 ? 0.52991   -18.37922 -34.40419 1.000 15.92012  ? 160 TYR   A CB  1 
ATOM   1121 C CG  . TYR   A 1 153 ? 0.93129   -18.19107 -35.84568 1.000 20.36250  ? 160 TYR   A CG  1 
ATOM   1122 C CD1 . TYR   A 1 153 ? 1.79810   -19.08794 -36.45667 1.000 23.98107  ? 160 TYR   A CD1 1 
ATOM   1123 C CD2 . TYR   A 1 153 ? 0.44795   -17.12282 -36.59650 1.000 26.66784  ? 160 TYR   A CD2 1 
ATOM   1124 C CE1 . TYR   A 1 153 ? 2.17394   -18.93151 -37.77250 1.000 25.58393  ? 160 TYR   A CE1 1 
ATOM   1125 C CE2 . TYR   A 1 153 ? 0.82150   -16.95833 -37.92250 1.000 25.15389  ? 160 TYR   A CE2 1 
ATOM   1126 C CZ  . TYR   A 1 153 ? 1.68388   -17.86867 -38.50109 1.000 32.42674  ? 160 TYR   A CZ  1 
ATOM   1127 O OH  . TYR   A 1 153 ? 2.07421   -17.72933 -39.81516 1.000 38.88369  ? 160 TYR   A OH  1 
ATOM   1128 N N   . ALA   A 1 154 ? 0.19161   -20.85278 -32.52587 1.000 19.43700  ? 161 ALA   A N   1 
ATOM   1129 C CA  . ALA   A 1 154 ? 0.40660   -21.38911 -31.18576 1.000 17.28406  ? 161 ALA   A CA  1 
ATOM   1130 C C   . ALA   A 1 154 ? 1.87635   -21.23417 -30.80787 1.000 20.28644  ? 161 ALA   A C   1 
ATOM   1131 O O   . ALA   A 1 154 ? 2.76039   -21.74741 -31.50635 1.000 17.79850  ? 161 ALA   A O   1 
ATOM   1132 C CB  . ALA   A 1 154 ? -0.01188  -22.85850 -31.10388 1.000 20.08782  ? 161 ALA   A CB  1 
ATOM   1133 N N   . TRP   A 1 155 ? 2.12368   -20.52265 -29.71332 1.000 15.76727  ? 162 TRP   A N   1 
ATOM   1134 C CA  . TRP   A 1 155 ? 3.43020   -20.40559 -29.07346 1.000 14.81022  ? 162 TRP   A CA  1 
ATOM   1135 C C   . TRP   A 1 155 ? 3.46314   -21.33700 -27.86765 1.000 15.82928  ? 162 TRP   A C   1 
ATOM   1136 O O   . TRP   A 1 155 ? 2.44359   -21.53019 -27.20263 1.000 16.06360  ? 162 TRP   A O   1 
ATOM   1137 C CB  . TRP   A 1 155 ? 3.64810   -18.94691 -28.65285 1.000 15.38585  ? 162 TRP   A CB  1 
ATOM   1138 C CG  . TRP   A 1 155 ? 4.90000   -18.56786 -27.88533 1.000 14.38754  ? 162 TRP   A CG  1 
ATOM   1139 C CD1 . TRP   A 1 155 ? 5.97114   -17.87952 -28.37556 1.000 14.58464  ? 162 TRP   A CD1 1 
ATOM   1140 C CD2 . TRP   A 1 155 ? 5.15834   -18.75671 -26.47901 1.000 15.96322  ? 162 TRP   A CD2 1 
ATOM   1141 N NE1 . TRP   A 1 155 ? 6.89069   -17.65592 -27.37939 1.000 14.68685  ? 162 TRP   A NE1 1 
ATOM   1142 C CE2 . TRP   A 1 155 ? 6.41972   -18.19090 -26.20854 1.000 14.93599  ? 162 TRP   A CE2 1 
ATOM   1143 C CE3 . TRP   A 1 155 ? 4.45417   -19.36487 -25.43085 1.000 15.00652  ? 162 TRP   A CE3 1 
ATOM   1144 C CZ2 . TRP   A 1 155 ? 6.99723   -18.21862 -24.93534 1.000 17.23124  ? 162 TRP   A CZ2 1 
ATOM   1145 C CZ3 . TRP   A 1 155 ? 5.02604   -19.38943 -24.17046 1.000 13.10130  ? 162 TRP   A CZ3 1 
ATOM   1146 C CH2 . TRP   A 1 155 ? 6.28897   -18.81874 -23.93448 1.000 14.16368  ? 162 TRP   A CH2 1 
ATOM   1147 N N   . GLU   A 1 156 ? 4.62303   -21.93139 -27.58397 1.000 14.49417  ? 163 GLU   A N   1 
ATOM   1148 C CA  . GLU   A 1 156 ? 4.69488   -22.85339 -26.45585 1.000 17.15586  ? 163 GLU   A CA  1 
ATOM   1149 C C   . GLU   A 1 156 ? 6.10089   -22.86755 -25.87375 1.000 15.06652  ? 163 GLU   A C   1 
ATOM   1150 O O   . GLU   A 1 156 ? 7.08361   -22.81012 -26.61560 1.000 17.11289  ? 163 GLU   A O   1 
ATOM   1151 C CB  . GLU   A 1 156 ? 4.29503   -24.27330 -26.87493 1.000 20.94577  ? 163 GLU   A CB  1 
ATOM   1152 C CG  . GLU   A 1 156 ? 4.10129   -25.25194 -25.72417 1.000 25.30743  ? 163 GLU   A CG  1 
ATOM   1153 C CD  . GLU   A 1 156 ? 3.28351   -26.46286 -26.13052 1.000 44.19121  ? 163 GLU   A CD  1 
ATOM   1154 O OE1 . GLU   A 1 156 ? 2.05942   -26.48149 -25.87282 1.000 33.03748  ? 163 GLU   A OE1 1 
ATOM   1155 O OE2 . GLU   A 1 156 ? 3.87210   -27.39572 -26.72218 1.000 37.81407  ? 163 GLU   A OE2 1 
ATOM   1156 N N   . SER   A 1 157 ? 6.19394   -22.94698 -24.54572 1.000 15.72583  ? 164 SER   A N   1 
ATOM   1157 C CA  . SER   A 1 157 ? 7.50116   -23.09558 -23.91793 1.000 15.46694  ? 164 SER   A CA  1 
ATOM   1158 C C   . SER   A 1 157 ? 7.36143   -23.76599 -22.56025 1.000 16.69244  ? 164 SER   A C   1 
ATOM   1159 O O   . SER   A 1 157 ? 6.45423   -23.44418 -21.78414 1.000 16.00567  ? 164 SER   A O   1 
ATOM   1160 C CB  . SER   A 1 157 ? 8.22042   -21.75751 -23.74300 1.000 14.82899  ? 164 SER   A CB  1 
ATOM   1161 O OG  . SER   A 1 157 ? 9.50206   -21.98032 -23.16086 1.000 16.53562  ? 164 SER   A OG  1 
ATOM   1162 N N   . SER   A 1 158 ? 8.27399   -24.69657 -22.28846 1.000 17.41180  ? 165 SER   A N   1 
ATOM   1163 C CA  . SER   A 1 158 ? 8.46607   -25.25800 -20.95941 1.000 18.08069  ? 165 SER   A CA  1 
ATOM   1164 C C   . SER   A 1 158 ? 9.70144   -24.67284 -20.28808 1.000 18.12191  ? 165 SER   A C   1 
ATOM   1165 O O   . SER   A 1 158 ? 10.32498  -25.33080 -19.44662 1.000 22.33991  ? 165 SER   A O   1 
ATOM   1166 C CB  . SER   A 1 158 ? 8.56662   -26.77950 -21.03936 1.000 23.60551  ? 165 SER   A CB  1 
ATOM   1167 O OG  . SER   A 1 158 ? 7.31995   -27.34770 -21.40377 1.000 22.54791  ? 165 SER   A OG  1 
ATOM   1168 N N   . ALA   A 1 159 ? 10.06587  -23.45147 -20.66603 1.000 18.55789  ? 166 ALA   A N   1 
ATOM   1169 C CA  . ALA   A 1 159 ? 11.31346  -22.77817 -20.25149 1.000 17.54192  ? 166 ALA   A CA  1 
ATOM   1170 C C   . ALA   A 1 159 ? 12.47350  -23.61825 -20.79629 1.000 21.22362  ? 166 ALA   A C   1 
ATOM   1171 O O   . ALA   A 1 159 ? 12.37484  -24.14318 -21.91414 1.000 25.17957  ? 166 ALA   A O   1 
ATOM   1172 C CB  . ALA   A 1 159 ? 11.31815  -22.54175 -18.75702 1.000 20.60089  ? 166 ALA   A CB  1 
ATOM   1173 N N   . GLY   A 1 160 ? 13.58152  -23.75119 -20.07131 1.000 20.26434  ? 167 GLY   A N   1 
ATOM   1174 C CA  . GLY   A 1 160 ? 14.71341  -24.47880 -20.61974 1.000 23.96463  ? 167 GLY   A CA  1 
ATOM   1175 C C   . GLY   A 1 160 ? 15.39495  -23.82082 -21.80039 1.000 22.93092  ? 167 GLY   A C   1 
ATOM   1176 O O   . GLY   A 1 160 ? 16.22675  -24.45827 -22.45667 1.000 26.40209  ? 167 GLY   A O   1 
ATOM   1177 N N   . GLY   A 1 161 ? 15.06071  -22.56974 -22.10338 1.000 19.63767  ? 168 GLY   A N   1 
ATOM   1178 C CA  . GLY   A 1 161 ? 15.80490  -21.78773 -23.06698 1.000 20.03025  ? 168 GLY   A CA  1 
ATOM   1179 C C   . GLY   A 1 161 ? 15.23268  -21.74279 -24.46722 1.000 19.53125  ? 168 GLY   A C   1 
ATOM   1180 O O   . GLY   A 1 161 ? 15.83237  -21.09901 -25.33582 1.000 20.14147  ? 168 GLY   A O   1 
ATOM   1181 N N   . SER   A 1 162 ? 14.09801  -22.39148 -24.72211 1.000 15.79343  ? 169 SER   A N   1 
ATOM   1182 C CA  . SER   A 1 162 ? 13.55986  -22.42450 -26.07251 1.000 13.98392  ? 169 SER   A CA  1 
ATOM   1183 C C   . SER   A 1 162 ? 12.04195  -22.31857 -26.03536 1.000 14.24551  ? 169 SER   A C   1 
ATOM   1184 O O   . SER   A 1 162 ? 11.39662  -22.61448 -25.02535 1.000 17.63583  ? 169 SER   A O   1 
ATOM   1185 C CB  . SER   A 1 162 ? 13.98160  -23.69314 -26.82431 1.000 17.56080  ? 169 SER   A CB  1 
ATOM   1186 O OG  . SER   A 1 162 ? 13.37598  -24.84376 -26.26252 1.000 19.18348  ? 169 SER   A OG  1 
ATOM   1187 N N   . PHE   A 1 163 ? 11.48995  -21.87169 -27.16016 1.000 14.85095  ? 170 PHE   A N   1 
ATOM   1188 C CA  . PHE   A 1 163 ? 10.05317  -21.84042 -27.37504 1.000 18.06469  ? 170 PHE   A CA  1 
ATOM   1189 C C   . PHE   A 1 163 ? 9.77760   -22.28326 -28.80318 1.000 18.04264  ? 170 PHE   A C   1 
ATOM   1190 O O   . PHE   A 1 163 ? 10.65475  -22.23216 -29.66823 1.000 18.36775  ? 170 PHE   A O   1 
ATOM   1191 C CB  . PHE   A 1 163 ? 9.44877   -20.44894 -27.09434 1.000 15.25931  ? 170 PHE   A CB  1 
ATOM   1192 C CG  . PHE   A 1 163 ? 9.93610   -19.34909 -28.01003 1.000 15.48507  ? 170 PHE   A CG  1 
ATOM   1193 C CD1 . PHE   A 1 163 ? 11.06711  -18.60812 -27.68843 1.000 17.55887  ? 170 PHE   A CD1 1 
ATOM   1194 C CD2 . PHE   A 1 163 ? 9.24573   -19.03158 -29.17041 1.000 14.25314  ? 170 PHE   A CD2 1 
ATOM   1195 C CE1 . PHE   A 1 163 ? 11.50828  -17.58141 -28.52074 1.000 17.54883  ? 170 PHE   A CE1 1 
ATOM   1196 C CE2 . PHE   A 1 163 ? 9.67885   -18.01185 -29.99980 1.000 13.71063  ? 170 PHE   A CE2 1 
ATOM   1197 C CZ  . PHE   A 1 163 ? 10.80848  -17.27894 -29.66968 1.000 19.99969  ? 170 PHE   A CZ  1 
ATOM   1198 N N   . THR   A 1 164 ? 8.55721   -22.75652 -29.03981 1.000 17.72374  ? 171 THR   A N   1 
ATOM   1199 C CA  . THR   A 1 164 ? 8.14826   -23.15361 -30.37728 1.000 17.12013  ? 171 THR   A CA  1 
ATOM   1200 C C   . THR   A 1 164 ? 7.00391   -22.27741 -30.86028 1.000 17.37910  ? 171 THR   A C   1 
ATOM   1201 O O   . THR   A 1 164 ? 6.23304   -21.73313 -30.06498 1.000 16.80875  ? 171 THR   A O   1 
ATOM   1202 C CB  . THR   A 1 164 ? 7.72770   -24.63243 -30.44267 1.000 18.73704  ? 171 THR   A CB  1 
ATOM   1203 O OG1 . THR   A 1 164 ? 6.56169   -24.84246 -29.63685 1.000 19.19094  ? 171 THR   A OG1 1 
ATOM   1204 C CG2 . THR   A 1 164 ? 8.85398   -25.54911 -29.96659 1.000 19.06856  ? 171 THR   A CG2 1 
ATOM   1205 N N   . VAL   A 1 165 ? 6.91251   -22.14408 -32.18168 1.000 18.07581  ? 172 VAL   A N   1 
ATOM   1206 C CA  . VAL   A 1 165 ? 5.81106   -21.45780 -32.84078 1.000 19.94381  ? 172 VAL   A CA  1 
ATOM   1207 C C   . VAL   A 1 165 ? 5.35216   -22.33050 -33.99452 1.000 22.84332  ? 172 VAL   A C   1 
ATOM   1208 O O   . VAL   A 1 165 ? 6.17881   -22.82885 -34.76769 1.000 21.06272  ? 172 VAL   A O   1 
ATOM   1209 C CB  . VAL   A 1 165 ? 6.20612   -20.05561 -33.34942 1.000 18.60318  ? 172 VAL   A CB  1 
ATOM   1210 C CG1 . VAL   A 1 165 ? 5.06111   -19.44083 -34.14790 1.000 19.45918  ? 172 VAL   A CG1 1 
ATOM   1211 C CG2 . VAL   A 1 165 ? 6.59828   -19.15058 -32.18646 1.000 16.14156  ? 172 VAL   A CG2 1 
ATOM   1212 N N   . ARG   A 1 166 ? 4.03957   -22.51603 -34.11020 1.000 20.03742  ? 173 ARG   A N   1 
ATOM   1213 C CA  . ARG   A 1 166 ? 3.47234   -23.27771 -35.21140 1.000 21.70581  ? 173 ARG   A CA  1 
ATOM   1214 C C   . ARG   A 1 166 ? 2.12694   -22.67508 -35.58306 1.000 23.29550  ? 173 ARG   A C   1 
ATOM   1215 O O   . ARG   A 1 166 ? 1.47103   -22.03366 -34.75810 1.000 21.34903  ? 173 ARG   A O   1 
ATOM   1216 C CB  . ARG   A 1 166 ? 3.31291   -24.76251 -34.85316 1.000 26.57116  ? 173 ARG   A CB  1 
ATOM   1217 C CG  . ARG   A 1 166 ? 2.24166   -25.04364 -33.80265 1.000 27.54836  ? 173 ARG   A CG  1 
ATOM   1218 C CD  . ARG   A 1 166 ? 2.38538   -26.44234 -33.20559 1.000 33.88170  ? 173 ARG   A CD  1 
ATOM   1219 N NE  . ARG   A 1 166 ? 3.45606   -26.50928 -32.21507 1.000 36.17288  ? 173 ARG   A NE  1 
ATOM   1220 C CZ  . ARG   A 1 166 ? 3.96853   -27.63684 -31.73652 1.000 43.49567  ? 173 ARG   A CZ  1 
ATOM   1221 N NH1 . ARG   A 1 166 ? 3.52506   -28.82019 -32.12907 1.000 36.49865  ? 173 ARG   A NH1 1 
ATOM   1222 N NH2 . ARG   A 1 166 ? 4.95456   -27.57550 -30.84527 1.000 45.64162  ? 173 ARG   A NH2 1 
ATOM   1223 N N   . THR   A 1 167 ? 1.72771   -22.87137 -36.83861 1.000 25.00441  ? 174 THR   A N   1 
ATOM   1224 C CA  . THR   A 1 167 ? 0.36580   -22.53600 -37.22166 1.000 25.69968  ? 174 THR   A CA  1 
ATOM   1225 C C   . THR   A 1 167 ? -0.58834  -23.42994 -36.44462 1.000 27.60318  ? 174 THR   A C   1 
ATOM   1226 O O   . THR   A 1 167 ? -0.36488  -24.63691 -36.32634 1.000 32.07815  ? 174 THR   A O   1 
ATOM   1227 C CB  . THR   A 1 167 ? 0.16292   -22.71302 -38.72938 1.000 29.71479  ? 174 THR   A CB  1 
ATOM   1228 O OG1 . THR   A 1 167 ? 1.08709   -21.87858 -39.43793 1.000 38.93021  ? 174 THR   A OG1 1 
ATOM   1229 C CG2 . THR   A 1 167 ? -1.25032  -22.31986 -39.11822 1.000 47.37975  ? 174 THR   A CG2 1 
ATOM   1230 N N   . ASP   A 1 168 ? -1.63483  -22.83564 -35.88238 1.000 25.55444  ? 175 ASP   A N   1 
ATOM   1231 C CA  . ASP   A 1 168 ? -2.55823  -23.57884 -35.03963 1.000 26.20857  ? 175 ASP   A CA  1 
ATOM   1232 C C   . ASP   A 1 168 ? -3.70883  -24.10158 -35.88701 1.000 36.17385  ? 175 ASP   A C   1 
ATOM   1233 O O   . ASP   A 1 168 ? -4.45923  -23.31902 -36.48022 1.000 36.33121  ? 175 ASP   A O   1 
ATOM   1234 C CB  . ASP   A 1 168 ? -3.08294  -22.70950 -33.90065 1.000 29.48743  ? 175 ASP   A CB  1 
ATOM   1235 C CG  . ASP   A 1 168 ? -3.94565  -23.48886 -32.93430 1.000 34.39330  ? 175 ASP   A CG  1 
ATOM   1236 O OD1 . ASP   A 1 168 ? -3.56495  -24.62375 -32.57973 1.000 48.44425  ? 175 ASP   A OD1 1 
ATOM   1237 O OD2 . ASP   A 1 168 ? -5.01291  -22.97933 -32.54630 1.000 30.58935  ? 175 ASP   A OD2 1 
ATOM   1238 N N   . THR   A 1 169 ? -3.83930  -25.42159 -35.94299 1.000 47.71302  ? 176 THR   A N   1 
ATOM   1239 C CA  . THR   A 1 169 ? -4.96331  -26.07338 -36.59582 1.000 66.59814  ? 176 THR   A CA  1 
ATOM   1240 C C   . THR   A 1 169 ? -6.11819  -26.34029 -35.63960 1.000 62.12776  ? 176 THR   A C   1 
ATOM   1241 O O   . THR   A 1 169 ? -7.11236  -26.95147 -36.04590 1.000 50.29930  ? 176 THR   A O   1 
ATOM   1242 C CB  . THR   A 1 169 ? -4.50491  -27.38744 -37.23704 1.000 71.42190  ? 176 THR   A CB  1 
ATOM   1243 O OG1 . THR   A 1 169 ? -3.62317  -28.07489 -36.33799 1.000 49.69296  ? 176 THR   A OG1 1 
ATOM   1244 C CG2 . THR   A 1 169 ? -3.77228  -27.10880 -38.54486 1.000 49.98796  ? 176 THR   A CG2 1 
ATOM   1245 N N   . GLY   A 1 170 ? -6.01102  -25.89371 -34.38811 1.000 55.12250  ? 177 GLY   A N   1 
ATOM   1246 C CA  . GLY   A 1 170 ? -7.04929  -26.10278 -33.39826 1.000 52.33227  ? 177 GLY   A CA  1 
ATOM   1247 C C   . GLY   A 1 170 ? -8.29826  -25.27675 -33.64292 1.000 51.80220  ? 177 GLY   A C   1 
ATOM   1248 O O   . GLY   A 1 170 ? -8.52313  -24.77893 -34.74869 1.000 43.56083  ? 177 GLY   A O   1 
ATOM   1249 N N   . GLU   A 1 171 ? -9.10648  -25.11032 -32.61105 1.000 47.09646  ? 178 GLU   A N   1 
ATOM   1250 C CA  . GLU   A 1 171 ? -10.38757 -24.43341 -32.73081 1.000 36.83133  ? 178 GLU   A CA  1 
ATOM   1251 C C   . GLU   A 1 171 ? -10.18449 -22.97646 -33.13513 1.000 35.20576  ? 178 GLU   A C   1 
ATOM   1252 O O   . GLU   A 1 171 ? -9.46837  -22.24003 -32.43213 1.000 31.88535  ? 178 GLU   A O   1 
ATOM   1253 C CB  . GLU   A 1 171 ? -11.12372 -24.53066 -31.39234 1.000 41.92650  ? 178 GLU   A CB  1 
ATOM   1254 C CG  . GLU   A 1 171 ? -12.59040 -24.22963 -31.47567 1.000 40.35782  ? 178 GLU   A CG  1 
ATOM   1255 C CD  . GLU   A 1 171 ? -13.34111 -25.28232 -32.26373 1.000 41.65654  ? 178 GLU   A CD  1 
ATOM   1256 O OE1 . GLU   A 1 171 ? -13.00877 -26.48273 -32.15003 1.000 44.92839  ? 178 GLU   A OE1 1 
ATOM   1257 O OE2 . GLU   A 1 171 ? -14.24699 -24.90112 -33.02069 1.000 45.22789  ? 178 GLU   A OE2 1 
ATOM   1258 N N   . PRO   A 1 172 ? -10.77375 -22.51529 -34.24030 1.000 36.96280  ? 179 PRO   A N   1 
ATOM   1259 C CA  . PRO   A 1 172 ? -10.63765 -21.11276 -34.63561 1.000 31.25349  ? 179 PRO   A CA  1 
ATOM   1260 C C   . PRO   A 1 172 ? -11.07829 -20.17235 -33.52049 1.000 42.86410  ? 179 PRO   A C   1 
ATOM   1261 O O   . PRO   A 1 172 ? -12.06395 -20.42415 -32.82402 1.000 44.71813  ? 179 PRO   A O   1 
ATOM   1262 C CB  . PRO   A 1 172 ? -11.56406 -20.99364 -35.85215 1.000 36.39868  ? 179 PRO   A CB  1 
ATOM   1263 C CG  . PRO   A 1 172 ? -11.84404 -22.38722 -36.30572 1.000 46.34130  ? 179 PRO   A CG  1 
ATOM   1264 C CD  . PRO   A 1 172 ? -11.17700 -23.34801 -35.37862 1.000 46.25258  ? 179 PRO   A CD  1 
ATOM   1265 N N   . MET   A 1 173 ? -10.34858 -19.06596 -33.37500 1.000 26.77204  ? 180 MET   A N   1 
ATOM   1266 C CA  . MET   A 1 173 ? -10.55957 -18.12802 -32.28509 1.000 29.07607  ? 180 MET   A CA  1 
ATOM   1267 C C   . MET   A 1 173 ? -11.26692 -16.84809 -32.69079 1.000 39.52450  ? 180 MET   A C   1 
ATOM   1268 O O   . MET   A 1 173 ? -11.80552 -16.16545 -31.81617 1.000 40.73059  ? 180 MET   A O   1 
ATOM   1269 C CB  . MET   A 1 173 ? -9.21736  -17.75832 -31.66564 1.000 33.58426  ? 180 MET   A CB  1 
ATOM   1270 C CG  . MET   A 1 173 ? -8.59993  -18.85244 -30.85064 1.000 54.85022  ? 180 MET   A CG  1 
ATOM   1271 S SD  . MET   A 1 173 ? -7.33838  -18.18051 -29.77907 1.000 46.50358  ? 180 MET   A SD  1 
ATOM   1272 C CE  . MET   A 1 173 ? -7.86593  -16.48202 -29.65255 1.000 34.56935  ? 180 MET   A CE  1 
ATOM   1273 N N   . GLY   A 1 174 ? -11.25480 -16.48756 -33.96822 1.000 35.83942  ? 181 GLY   A N   1 
ATOM   1274 C CA  . GLY   A 1 174 ? -11.84015 -15.22316 -34.37534 1.000 28.06660  ? 181 GLY   A CA  1 
ATOM   1275 C C   . GLY   A 1 174 ? -10.87296 -14.06742 -34.20946 1.000 28.75474  ? 181 GLY   A C   1 
ATOM   1276 O O   . GLY   A 1 174 ? -10.39601 -13.49160 -35.19341 1.000 24.63144  ? 181 GLY   A O   1 
ATOM   1277 N N   . ARG   A 1 175 ? -10.57539 -13.73222 -32.95524 1.000 21.42489  ? 182 ARG   A N   1 
ATOM   1278 C CA  . ARG   A 1 175 ? -9.59243  -12.70915 -32.60420 1.000 19.90754  ? 182 ARG   A CA  1 
ATOM   1279 C C   . ARG   A 1 175 ? -9.31628  -12.74064 -31.11114 1.000 19.78728  ? 182 ARG   A C   1 
ATOM   1280 O O   . ARG   A 1 175 ? -10.25333 -12.80663 -30.30895 1.000 20.28244  ? 182 ARG   A O   1 
ATOM   1281 C CB  . ARG   A 1 175 ? -10.06787 -11.30170 -32.99151 1.000 19.74965  ? 182 ARG   A CB  1 
ATOM   1282 C CG  . ARG   A 1 175 ? -8.96007  -10.23542 -32.87505 1.000 18.47396  ? 182 ARG   A CG  1 
ATOM   1283 C CD  . ARG   A 1 175 ? -9.52830  -8.82541  -32.69152 1.000 18.17937  ? 182 ARG   A CD  1 
ATOM   1284 N NE  . ARG   A 1 175 ? -10.42468 -8.72492  -31.54420 1.000 17.97624  ? 182 ARG   A NE  1 
ATOM   1285 C CZ  . ARG   A 1 175 ? -11.73092 -8.51872  -31.63680 1.000 18.80443  ? 182 ARG   A CZ  1 
ATOM   1286 N NH1 . ARG   A 1 175 ? -12.33162 -8.40541  -32.81160 1.000 19.94668  ? 182 ARG   A NH1 1 
ATOM   1287 N NH2 . ARG   A 1 175 ? -12.45722 -8.43597  -30.52325 1.000 18.57928  ? 182 ARG   A NH2 1 
ATOM   1288 N N   . GLY   A 1 176 ? -8.05251  -12.67369 -30.72414 1.000 19.52478  ? 183 GLY   A N   1 
ATOM   1289 C CA  . GLY   A 1 176 ? -7.72459  -12.55762 -29.32496 1.000 18.02263  ? 183 GLY   A CA  1 
ATOM   1290 C C   . GLY   A 1 176 ? -6.57927  -13.47037 -28.96555 1.000 18.06997  ? 183 GLY   A C   1 
ATOM   1291 O O   . GLY   A 1 176 ? -5.82790  -13.92417 -29.82805 1.000 17.76837  ? 183 GLY   A O   1 
ATOM   1292 N N   . THR   A 1 177 ? -6.46457  -13.75082 -27.67255 1.000 16.16227  ? 184 THR   A N   1 
ATOM   1293 C CA  . THR   A 1 177 ? -5.36228  -14.55384 -27.17603 1.000 15.35811  ? 184 THR   A CA  1 
ATOM   1294 C C   . THR   A 1 177 ? -5.86378  -15.49036 -26.09257 1.000 20.52507  ? 184 THR   A C   1 
ATOM   1295 O O   . THR   A 1 177 ? -6.73256  -15.13115 -25.29012 1.000 16.92994  ? 184 THR   A O   1 
ATOM   1296 C CB  . THR   A 1 177 ? -4.22901  -13.66900 -26.63758 1.000 16.21007  ? 184 THR   A CB  1 
ATOM   1297 O OG1 . THR   A 1 177 ? -3.73484  -12.85392 -27.70172 1.000 19.09692  ? 184 THR   A OG1 1 
ATOM   1298 C CG2 . THR   A 1 177 ? -3.07712  -14.51633 -26.09829 1.000 20.36522  ? 184 THR   A CG2 1 
ATOM   1299 N N   . LYS   A 1 178 ? -5.31027  -16.69752 -26.09273 1.000 16.24989  ? 185 LYS   A N   1 
ATOM   1300 C CA  . LYS   A 1 178 ? -5.61273  -17.72931 -25.11424 1.000 17.02193  ? 185 LYS   A CA  1 
ATOM   1301 C C   . LYS   A 1 178 ? -4.29711  -18.12242 -24.45641 1.000 16.12087  ? 185 LYS   A C   1 
ATOM   1302 O O   . LYS   A 1 178 ? -3.37560  -18.56312 -25.14806 1.000 20.70448  ? 185 LYS   A O   1 
ATOM   1303 C CB  . LYS   A 1 178 ? -6.26236  -18.92072 -25.82214 1.000 22.57443  ? 185 LYS   A CB  1 
ATOM   1304 C CG  . LYS   A 1 178 ? -6.56480  -20.11556 -24.97521 1.000 31.95461  ? 185 LYS   A CG  1 
ATOM   1305 C CD  . LYS   A 1 178 ? -7.31900  -21.21073 -25.75109 1.000 36.58370  ? 185 LYS   A CD  1 
ATOM   1306 C CE  . LYS   A 1 178 ? -8.18330  -20.70974 -26.91698 1.000 48.90165  ? 185 LYS   A CE  1 
ATOM   1307 N NZ  . LYS   A 1 178 ? -9.12413  -19.59171 -26.60361 1.000 55.74102  ? 185 LYS   A NZ  1 
ATOM   1308 N N   . VAL   A 1 179 ? -4.18254  -17.92416 -23.14345 1.000 13.51565  ? 186 VAL   A N   1 
ATOM   1309 C CA  . VAL   A 1 179 ? -2.98488  -18.33596 -22.40703 1.000 13.87089  ? 186 VAL   A CA  1 
ATOM   1310 C C   . VAL   A 1 179 ? -3.34740  -19.57547 -21.60103 1.000 15.36572  ? 186 VAL   A C   1 
ATOM   1311 O O   . VAL   A 1 179 ? -4.17172  -19.51336 -20.68004 1.000 16.13185  ? 186 VAL   A O   1 
ATOM   1312 C CB  . VAL   A 1 179 ? -2.44332  -17.22140 -21.50131 1.000 14.01314  ? 186 VAL   A CB  1 
ATOM   1313 C CG1 . VAL   A 1 179 ? -1.24074  -17.73414 -20.68807 1.000 15.75984  ? 186 VAL   A CG1 1 
ATOM   1314 C CG2 . VAL   A 1 179 ? -2.03982  -16.01652 -22.32388 1.000 16.37132  ? 186 VAL   A CG2 1 
ATOM   1315 N N   . ILE   A 1 180 ? -2.74181  -20.70494 -21.95013 1.000 14.89820  ? 187 ILE   A N   1 
ATOM   1316 C CA  . ILE   A 1 180 ? -3.03779  -21.99150 -21.33006 1.000 15.44529  ? 187 ILE   A CA  1 
ATOM   1317 C C   . ILE   A 1 180 ? -1.90802  -22.31239 -20.36413 1.000 16.09774  ? 187 ILE   A C   1 
ATOM   1318 O O   . ILE   A 1 180 ? -0.77032  -22.53567 -20.78539 1.000 16.76779  ? 187 ILE   A O   1 
ATOM   1319 C CB  . ILE   A 1 180 ? -3.19986  -23.09799 -22.38029 1.000 15.93863  ? 187 ILE   A CB  1 
ATOM   1320 C CG1 . ILE   A 1 180 ? -4.26017  -22.69054 -23.40841 1.000 15.75401  ? 187 ILE   A CG1 1 
ATOM   1321 C CG2 . ILE   A 1 180 ? -3.55308  -24.42361 -21.71677 1.000 18.40606  ? 187 ILE   A CG2 1 
ATOM   1322 C CD1 . ILE   A 1 180 ? -4.27683  -23.56039 -24.63913 1.000 22.18641  ? 187 ILE   A CD1 1 
ATOM   1323 N N   . LEU   A 1 181 ? -2.21893  -22.34168 -19.07008 1.000 14.18131  ? 188 LEU   A N   1 
ATOM   1324 C CA  . LEU   A 1 181 ? -1.23437  -22.64455 -18.03514 1.000 14.48030  ? 188 LEU   A CA  1 
ATOM   1325 C C   . LEU   A 1 181 ? -1.31281  -24.12536 -17.69387 1.000 19.14243  ? 188 LEU   A C   1 
ATOM   1326 O O   . LEU   A 1 181 ? -2.30536  -24.57983 -17.12042 1.000 19.53318  ? 188 LEU   A O   1 
ATOM   1327 C CB  . LEU   A 1 181 ? -1.48347  -21.79891 -16.78989 1.000 14.38859  ? 188 LEU   A CB  1 
ATOM   1328 C CG  . LEU   A 1 181 ? -1.56507  -20.29655 -17.02715 1.000 17.61388  ? 188 LEU   A CG  1 
ATOM   1329 C CD1 . LEU   A 1 181 ? -1.91166  -19.59840 -15.72884 1.000 18.68158  ? 188 LEU   A CD1 1 
ATOM   1330 C CD2 . LEU   A 1 181 ? -0.24986  -19.78648 -17.57497 1.000 16.38225  ? 188 LEU   A CD2 1 
ATOM   1331 N N   . HIS   A 1 182 ? -0.26594  -24.87966 -18.02865 1.000 17.17910  ? 189 HIS   A N   1 
ATOM   1332 C CA  . HIS   A 1 182 ? -0.17466  -26.27689 -17.60813 1.000 21.44810  ? 189 HIS   A CA  1 
ATOM   1333 C C   . HIS   A 1 182 ? 0.44339   -26.25968 -16.21600 1.000 18.11834  ? 189 HIS   A C   1 
ATOM   1334 O O   . HIS   A 1 182 ? 1.65033   -26.07694 -16.06487 1.000 18.89248  ? 189 HIS   A O   1 
ATOM   1335 C CB  . HIS   A 1 182 ? 0.63088   -27.09707 -18.61271 1.000 19.07206  ? 189 HIS   A CB  1 
ATOM   1336 C CG  . HIS   A 1 182 ? 0.11115   -26.99997 -20.01732 1.000 21.49437  ? 189 HIS   A CG  1 
ATOM   1337 N ND1 . HIS   A 1 182 ? -0.67043  -27.98057 -20.59325 1.000 27.92386  ? 189 HIS   A ND1 1 
ATOM   1338 C CD2 . HIS   A 1 182 ? 0.23989   -26.02666 -20.95180 1.000 24.82723  ? 189 HIS   A CD2 1 
ATOM   1339 C CE1 . HIS   A 1 182 ? -0.99141  -27.61968 -21.82355 1.000 24.87488  ? 189 HIS   A CE1 1 
ATOM   1340 N NE2 . HIS   A 1 182 ? -0.45206  -26.43745 -22.06604 1.000 25.63202  ? 189 HIS   A NE2 1 
ATOM   1341 N N   . LEU   A 1 183 ? -0.39521  -26.40318 -15.19096 1.000 18.11772  ? 190 LEU   A N   1 
ATOM   1342 C CA  . LEU   A 1 183 ? 0.02637   -26.08819 -13.83101 1.000 19.85542  ? 190 LEU   A CA  1 
ATOM   1343 C C   . LEU   A 1 183 ? 0.97875   -27.13797 -13.27348 1.000 21.00173  ? 190 LEU   A C   1 
ATOM   1344 O O   . LEU   A 1 183 ? 0.85571   -28.33327 -13.55387 1.000 23.98750  ? 190 LEU   A O   1 
ATOM   1345 C CB  . LEU   A 1 183 ? -1.19003  -25.96886 -12.91167 1.000 18.01262  ? 190 LEU   A CB  1 
ATOM   1346 C CG  . LEU   A 1 183 ? -2.11509  -24.77774 -13.17202 1.000 16.59409  ? 190 LEU   A CG  1 
ATOM   1347 C CD1 . LEU   A 1 183 ? -3.24697  -24.75072 -12.14875 1.000 19.41489  ? 190 LEU   A CD1 1 
ATOM   1348 C CD2 . LEU   A 1 183 ? -1.34599  -23.46416 -13.14594 1.000 20.21607  ? 190 LEU   A CD2 1 
ATOM   1349 N N   . LYS   A 1 184 ? 1.92834   -26.67061 -12.45537 1.000 20.79131  ? 191 LYS   A N   1 
ATOM   1350 C CA  . LYS   A 1 184 ? 2.75220   -27.56372 -11.65384 1.000 23.35380  ? 191 LYS   A CA  1 
ATOM   1351 C C   . LYS   A 1 184 ? 1.87015   -28.38965 -10.72398 1.000 25.06343  ? 191 LYS   A C   1 
ATOM   1352 O O   . LYS   A 1 184 ? 0.77956   -27.96620 -10.32647 1.000 25.86689  ? 191 LYS   A O   1 
ATOM   1353 C CB  . LYS   A 1 184 ? 3.77371   -26.76733 -10.83381 1.000 24.53824  ? 191 LYS   A CB  1 
ATOM   1354 C CG  . LYS   A 1 184 ? 4.80215   -25.98189 -11.65374 1.000 28.12876  ? 191 LYS   A CG  1 
ATOM   1355 C CD  . LYS   A 1 184 ? 5.57475   -24.99847 -10.76009 1.000 33.36096  ? 191 LYS   A CD  1 
ATOM   1356 C CE  . LYS   A 1 184 ? 6.25297   -23.89058 -11.56456 1.000 40.40479  ? 191 LYS   A CE  1 
ATOM   1357 N NZ  . LYS   A 1 184 ? 7.27748   -23.10470 -10.78497 1.000 30.14236  ? 191 LYS   A NZ  1 
ATOM   1358 N N   . GLU   A 1 185 ? 2.36171   -29.58064 -10.37465 1.000 29.41338  ? 192 GLU   A N   1 
ATOM   1359 C CA  . GLU   A 1 185 ? 1.56462   -30.53457 -9.60935  1.000 29.12353  ? 192 GLU   A CA  1 
ATOM   1360 C C   . GLU   A 1 185 ? 1.13077   -29.97407 -8.26062  1.000 32.71625  ? 192 GLU   A C   1 
ATOM   1361 O O   . GLU   A 1 185 ? 0.03152   -30.28585 -7.78805  1.000 35.77969  ? 192 GLU   A O   1 
ATOM   1362 C CB  . GLU   A 1 185 ? 2.35722   -31.83400 -9.43302  1.000 31.73514  ? 192 GLU   A CB  1 
ATOM   1363 C CG  . GLU   A 1 185 ? 2.20154   -32.52031 -8.08904  1.000 51.08821  ? 192 GLU   A CG  1 
ATOM   1364 C CD  . GLU   A 1 185 ? 2.86937   -33.88420 -8.05939  1.000 71.86691  ? 192 GLU   A CD  1 
ATOM   1365 O OE1 . GLU   A 1 185 ? 3.70500   -34.15514 -8.94863  1.000 61.10521  ? 192 GLU   A OE1 1 
ATOM   1366 O OE2 . GLU   A 1 185 ? 2.55921   -34.68493 -7.15009  1.000 75.97386  ? 192 GLU   A OE2 1 
ATOM   1367 N N   . ASP   A 1 186 ? 1.95503   -29.13901 -7.63250  1.000 26.94043  ? 193 ASP   A N   1 
ATOM   1368 C CA  . ASP   A 1 186 ? 1.61963   -28.59814 -6.32245  1.000 30.30230  ? 193 ASP   A CA  1 
ATOM   1369 C C   . ASP   A 1 186 ? 0.94424   -27.23431 -6.39653  1.000 32.16640  ? 193 ASP   A C   1 
ATOM   1370 O O   . ASP   A 1 186 ? 0.81360   -26.56785 -5.36703  1.000 27.52466  ? 193 ASP   A O   1 
ATOM   1371 C CB  . ASP   A 1 186 ? 2.86720   -28.51399 -5.43780  1.000 29.95202  ? 193 ASP   A CB  1 
ATOM   1372 C CG  . ASP   A 1 186 ? 3.91652   -27.56677 -5.98149  1.000 38.98685  ? 193 ASP   A CG  1 
ATOM   1373 O OD1 . ASP   A 1 186 ? 3.79334   -27.12831 -7.14548  1.000 43.00808  ? 193 ASP   A OD1 1 
ATOM   1374 O OD2 . ASP   A 1 186 ? 4.87518   -27.26057 -5.23717  1.000 47.86492  ? 193 ASP   A OD2 1 
ATOM   1375 N N   . GLN   A 1 187 ? 0.50012   -26.81028 -7.57864  1.000 25.71245  ? 194 GLN   A N   1 
ATOM   1376 C CA  . GLN   A 1 187 ? -0.13236  -25.50821 -7.74676  1.000 20.72628  ? 194 GLN   A CA  1 
ATOM   1377 C C   . GLN   A 1 187 ? -1.58523  -25.63705 -8.19523  1.000 19.99904  ? 194 GLN   A C   1 
ATOM   1378 O O   . GLN   A 1 187 ? -2.12892  -24.72368 -8.81463  1.000 21.67370  ? 194 GLN   A O   1 
ATOM   1379 C CB  . GLN   A 1 187 ? 0.65586   -24.64713 -8.73443  1.000 24.85551  ? 194 GLN   A CB  1 
ATOM   1380 C CG  . GLN   A 1 187 ? 2.09732   -24.38405 -8.31427  1.000 22.76922  ? 194 GLN   A CG  1 
ATOM   1381 C CD  . GLN   A 1 187 ? 2.20158   -23.70287 -6.95941  1.000 23.70847  ? 194 GLN   A CD  1 
ATOM   1382 O OE1 . GLN   A 1 187 ? 1.40317   -22.82536 -6.62266  1.000 28.31602  ? 194 GLN   A OE1 1 
ATOM   1383 N NE2 . GLN   A 1 187 ? 3.19989   -24.09309 -6.18137  1.000 23.31316  ? 194 GLN   A NE2 1 
ATOM   1384 N N   . THR   A 1 188 ? -2.23379  -26.75685 -7.87985  1.000 24.17307  ? 195 THR   A N   1 
ATOM   1385 C CA  . THR   A 1 188 ? -3.59765  -26.97968 -8.35495  1.000 25.41279  ? 195 THR   A CA  1 
ATOM   1386 C C   . THR   A 1 188 ? -4.64384  -26.16574 -7.60146  1.000 24.74778  ? 195 THR   A C   1 
ATOM   1387 O O   . THR   A 1 188 ? -5.82093  -26.20517 -7.97861  1.000 22.20107  ? 195 THR   A O   1 
ATOM   1388 C CB  . THR   A 1 188 ? -3.95454  -28.46987 -8.28585  1.000 29.30801  ? 195 THR   A CB  1 
ATOM   1389 O OG1 . THR   A 1 188 ? -3.82164  -28.94532 -6.93983  1.000 30.95424  ? 195 THR   A OG1 1 
ATOM   1390 C CG2 . THR   A 1 188 ? -3.03565  -29.26953 -9.19949  1.000 28.44280  ? 195 THR   A CG2 1 
ATOM   1391 N N   . GLU   A 1 189 ? -4.25406  -25.42566 -6.56186  1.000 24.09321  ? 196 GLU   A N   1 
ATOM   1392 C CA  . GLU   A 1 189 ? -5.20711  -24.54610 -5.89181  1.000 25.60504  ? 196 GLU   A CA  1 
ATOM   1393 C C   . GLU   A 1 189 ? -5.77351  -23.50126 -6.84310  1.000 22.92287  ? 196 GLU   A C   1 
ATOM   1394 O O   . GLU   A 1 189 ? -6.87746  -22.99603 -6.62346  1.000 21.78119  ? 196 GLU   A O   1 
ATOM   1395 C CB  . GLU   A 1 189 ? -4.54559  -23.86872 -4.69124  1.000 25.33650  ? 196 GLU   A CB  1 
ATOM   1396 C CG  . GLU   A 1 189 ? -3.54547  -22.77958 -5.05287  1.000 19.75975  ? 196 GLU   A CG  1 
ATOM   1397 C CD  . GLU   A 1 189 ? -2.76765  -22.30749 -3.84318  1.000 28.94320  ? 196 GLU   A CD  1 
ATOM   1398 O OE1 . GLU   A 1 189 ? -1.89124  -23.06590 -3.37556  1.000 30.19710  ? 196 GLU   A OE1 1 
ATOM   1399 O OE2 . GLU   A 1 189 ? -3.04172  -21.19011 -3.35192  1.000 28.34888  ? 196 GLU   A OE2 1 
ATOM   1400 N N   . TYR   A 1 190 ? -5.04735  -23.16975 -7.90253  1.000 21.73730  ? 197 TYR   A N   1 
ATOM   1401 C CA  . TYR   A 1 190 ? -5.51480  -22.17156 -8.85209  1.000 16.27226  ? 197 TYR   A CA  1 
ATOM   1402 C C   . TYR   A 1 190 ? -6.50356  -22.73561 -9.85764  1.000 20.10435  ? 197 TYR   A C   1 
ATOM   1403 O O   . TYR   A 1 190 ? -6.84757  -22.04224 -10.81650 1.000 22.19970  ? 197 TYR   A O   1 
ATOM   1404 C CB  . TYR   A 1 190 ? -4.31475  -21.52880 -9.55440  1.000 19.00140  ? 197 TYR   A CB  1 
ATOM   1405 C CG  . TYR   A 1 190 ? -3.39148  -20.90069 -8.54024  1.000 19.52149  ? 197 TYR   A CG  1 
ATOM   1406 C CD1 . TYR   A 1 190 ? -3.80556  -19.80641 -7.79604  1.000 22.97524  ? 197 TYR   A CD1 1 
ATOM   1407 C CD2 . TYR   A 1 190 ? -2.13500  -21.43217 -8.28117  1.000 19.33454  ? 197 TYR   A CD2 1 
ATOM   1408 C CE1 . TYR   A 1 190 ? -2.98326  -19.23709 -6.84372  1.000 21.48957  ? 197 TYR   A CE1 1 
ATOM   1409 C CE2 . TYR   A 1 190 ? -1.30508  -20.86765 -7.32308  1.000 25.78221  ? 197 TYR   A CE2 1 
ATOM   1410 C CZ  . TYR   A 1 190 ? -1.73958  -19.76635 -6.61079  1.000 22.09082  ? 197 TYR   A CZ  1 
ATOM   1411 O OH  . TYR   A 1 190 ? -0.93366  -19.19197 -5.65242  1.000 23.09819  ? 197 TYR   A OH  1 
ATOM   1412 N N   . LEU   A 1 191 ? -6.95557  -23.97482 -9.65674  1.000 19.34309  ? 198 LEU   A N   1 
ATOM   1413 C CA  . LEU   A 1 191 ? -8.08771  -24.53079 -10.38163 1.000 19.02858  ? 198 LEU   A CA  1 
ATOM   1414 C C   . LEU   A 1 191 ? -9.36956  -24.53126 -9.56440  1.000 21.16766  ? 198 LEU   A C   1 
ATOM   1415 O O   . LEU   A 1 191 ? -10.42114 -24.90485 -10.09692 1.000 22.14817  ? 198 LEU   A O   1 
ATOM   1416 C CB  . LEU   A 1 191 ? -7.78706  -25.96656 -10.82376 1.000 22.74471  ? 198 LEU   A CB  1 
ATOM   1417 C CG  . LEU   A 1 191 ? -6.56172  -26.11995 -11.71778 1.000 18.35297  ? 198 LEU   A CG  1 
ATOM   1418 C CD1 . LEU   A 1 191 ? -6.25596  -27.59376 -11.96695 1.000 25.35425  ? 198 LEU   A CD1 1 
ATOM   1419 C CD2 . LEU   A 1 191 ? -6.76797  -25.36952 -13.02419 1.000 24.69369  ? 198 LEU   A CD2 1 
ATOM   1420 N N   . GLU   A 1 192 ? -9.30874  -24.15536 -8.28659  1.000 21.61047  ? 199 GLU   A N   1 
ATOM   1421 C CA  . GLU   A 1 192 ? -10.49017 -24.16071 -7.43357  1.000 19.83940  ? 199 GLU   A CA  1 
ATOM   1422 C C   . GLU   A 1 192 ? -11.23117 -22.83602 -7.55040  1.000 26.97058  ? 199 GLU   A C   1 
ATOM   1423 O O   . GLU   A 1 192 ? -10.62066 -21.76277 -7.53459  1.000 21.59905  ? 199 GLU   A O   1 
ATOM   1424 C CB  . GLU   A 1 192 ? -10.12543 -24.43672 -5.97274  1.000 30.50695  ? 199 GLU   A CB  1 
ATOM   1425 C CG  . GLU   A 1 192 ? -9.17609  -25.61228 -5.76853  1.000 29.93129  ? 199 GLU   A CG  1 
ATOM   1426 C CD  . GLU   A 1 192 ? -8.64779  -25.69966 -4.34704  1.000 66.53683  ? 199 GLU   A CD  1 
ATOM   1427 O OE1 . GLU   A 1 192 ? -7.83308  -26.60661 -4.06795  1.000 65.97382  ? 199 GLU   A OE1 1 
ATOM   1428 O OE2 . GLU   A 1 192 ? -9.05087  -24.86523 -3.50763  1.000 76.20566  ? 199 GLU   A OE2 1 
ATOM   1429 N N   . GLU   A 1 193 ? -12.55867 -22.92777 -7.66599  1.000 24.39762  ? 200 GLU   A N   1 
ATOM   1430 C CA  . GLU   A 1 193 ? -13.37575 -21.74498 -7.91967  1.000 20.82341  ? 200 GLU   A CA  1 
ATOM   1431 C C   . GLU   A 1 193 ? -13.15756 -20.67872 -6.85165  1.000 21.99456  ? 200 GLU   A C   1 
ATOM   1432 O O   . GLU   A 1 193 ? -12.95027 -19.50079 -7.16679  1.000 22.90620  ? 200 GLU   A O   1 
ATOM   1433 C CB  . GLU   A 1 193 ? -14.85444 -22.13234 -7.98895  1.000 22.94983  ? 200 GLU   A CB  1 
ATOM   1434 C CG  . GLU   A 1 193 ? -15.74702 -20.97406 -8.40435  1.000 27.33224  ? 200 GLU   A CG  1 
ATOM   1435 C CD  . GLU   A 1 193 ? -17.22266 -21.31959 -8.39864  1.000 57.59911  ? 200 GLU   A CD  1 
ATOM   1436 O OE1 . GLU   A 1 193 ? -17.57886 -22.42596 -7.94049  1.000 38.80707  ? 200 GLU   A OE1 1 
ATOM   1437 O OE2 . GLU   A 1 193 ? -18.02412 -20.48087 -8.86417  1.000 45.46925  ? 200 GLU   A OE2 1 
ATOM   1438 N N   . ARG   A 1 194 ? -13.19540 -21.07338 -5.57743  1.000 25.66380  ? 201 ARG   A N   1 
ATOM   1439 C CA  . ARG   A 1 194 ? -13.13771 -20.07220 -4.51859  1.000 22.00239  ? 201 ARG   A CA  1 
ATOM   1440 C C   . ARG   A 1 194 ? -11.77268 -19.40120 -4.45452  1.000 22.65549  ? 201 ARG   A C   1 
ATOM   1441 O O   . ARG   A 1 194 ? -11.68336 -18.22793 -4.07904  1.000 26.07916  ? 201 ARG   A O   1 
ATOM   1442 C CB  . ARG   A 1 194 ? -13.50786 -20.69487 -3.17212  1.000 25.75530  ? 201 ARG   A CB  1 
ATOM   1443 C CG  . ARG   A 1 194 ? -12.66872 -21.87752 -2.75523  1.000 30.08929  ? 201 ARG   A CG  1 
ATOM   1444 C CD  . ARG   A 1 194 ? -12.96757 -22.24378 -1.31110  1.000 41.16742  ? 201 ARG   A CD  1 
ATOM   1445 N NE  . ARG   A 1 194 ? -12.00606 -23.20074 -0.78053  1.000 48.01916  ? 201 ARG   A NE  1 
ATOM   1446 C CZ  . ARG   A 1 194 ? -12.13683 -23.82308 0.38255   1.000 38.35675  ? 201 ARG   A CZ  1 
ATOM   1447 N NH1 . ARG   A 1 194 ? -13.19436 -23.62846 1.15528   1.000 42.55175  ? 201 ARG   A NH1 1 
ATOM   1448 N NH2 . ARG   A 1 194 ? -11.18166 -24.65854 0.78102   1.000 38.67366  ? 201 ARG   A NH2 1 
ATOM   1449 N N   . ARG   A 1 195 ? -10.70701 -20.11364 -4.83490  1.000 19.59013  ? 202 ARG   A N   1 
ATOM   1450 C CA  . ARG   A 1 195 ? -9.38168  -19.49985 -4.86020  1.000 19.83625  ? 202 ARG   A CA  1 
ATOM   1451 C C   . ARG   A 1 195 ? -9.25617  -18.50934 -6.00913  1.000 19.92752  ? 202 ARG   A C   1 
ATOM   1452 O O   . ARG   A 1 195 ? -8.70402  -17.41684 -5.83411  1.000 19.80086  ? 202 ARG   A O   1 
ATOM   1453 C CB  . ARG   A 1 195 ? -8.30275  -20.57756 -4.96497  1.000 22.36831  ? 202 ARG   A CB  1 
ATOM   1454 C CG  . ARG   A 1 195 ? -6.86768  -20.05013 -4.94622  1.000 23.17761  ? 202 ARG   A CG  1 
ATOM   1455 C CD  . ARG   A 1 195 ? -6.47054  -19.54138 -3.56543  1.000 21.44272  ? 202 ARG   A CD  1 
ATOM   1456 N NE  . ARG   A 1 195 ? -5.03738  -19.27569 -3.49552  1.000 20.72131  ? 202 ARG   A NE  1 
ATOM   1457 C CZ  . ARG   A 1 195 ? -4.48432  -18.08330 -3.31641  1.000 24.62142  ? 202 ARG   A CZ  1 
ATOM   1458 N NH1 . ARG   A 1 195 ? -5.21780  -16.99958 -3.11976  1.000 21.93794  ? 202 ARG   A NH1 1 
ATOM   1459 N NH2 . ARG   A 1 195 ? -3.15624  -17.97737 -3.33256  1.000 23.81281  ? 202 ARG   A NH2 1 
ATOM   1460 N N   . ILE   A 1 196 ? -9.74744  -18.87350 -7.19697  1.000 18.61526  ? 203 ILE   A N   1 
ATOM   1461 C CA  . ILE   A 1 196 ? -9.68435  -17.94443 -8.32331  1.000 15.65373  ? 203 ILE   A CA  1 
ATOM   1462 C C   . ILE   A 1 196 ? -10.52063 -16.70724 -8.03218  1.000 19.06763  ? 203 ILE   A C   1 
ATOM   1463 O O   . ILE   A 1 196 ? -10.07484 -15.57753 -8.26170  1.000 19.40596  ? 203 ILE   A O   1 
ATOM   1464 C CB  . ILE   A 1 196 ? -10.12693 -18.62608 -9.63112  1.000 21.72655  ? 203 ILE   A CB  1 
ATOM   1465 C CG1 . ILE   A 1 196 ? -9.20383  -19.80055 -9.97505  1.000 22.90968  ? 203 ILE   A CG1 1 
ATOM   1466 C CG2 . ILE   A 1 196 ? -10.10618 -17.60709 -10.77641 1.000 19.56813  ? 203 ILE   A CG2 1 
ATOM   1467 C CD1 . ILE   A 1 196 ? -9.86106  -20.84794 -10.87108 1.000 23.63512  ? 203 ILE   A CD1 1 
ATOM   1468 N N   . LYS   A 1 197 ? -11.73739 -16.90157 -7.50593  1.000 18.29370  ? 204 LYS   A N   1 
ATOM   1469 C CA  . LYS   A 1 197 ? -12.60072 -15.77346 -7.16080  1.000 17.08256  ? 204 LYS   A CA  1 
ATOM   1470 C C   . LYS   A 1 197 ? -11.90599 -14.82396 -6.19687  1.000 21.34151  ? 204 LYS   A C   1 
ATOM   1471 O O   . LYS   A 1 197 ? -11.97315 -13.59890 -6.36096  1.000 20.40258  ? 204 LYS   A O   1 
ATOM   1472 C CB  . LYS   A 1 197 ? -13.90674 -16.27066 -6.53392  1.000 21.26795  ? 204 LYS   A CB  1 
ATOM   1473 C CG  . LYS   A 1 197 ? -14.99702 -16.62263 -7.51401  1.000 32.56672  ? 204 LYS   A CG  1 
ATOM   1474 C CD  . LYS   A 1 197 ? -16.32734 -16.80068 -6.78987  1.000 38.74077  ? 204 LYS   A CD  1 
ATOM   1475 C CE  . LYS   A 1 197 ? -16.51904 -18.22721 -6.30254  1.000 48.65299  ? 204 LYS   A CE  1 
ATOM   1476 N NZ  . LYS   A 1 197 ? -17.90853 -18.71965 -6.54763  1.000 50.93443  ? 204 LYS   A NZ  1 
ATOM   1477 N N   . GLU   A 1 198 ? -11.24761 -15.37699 -5.17458  1.000 17.96959  ? 205 GLU   A N   1 
ATOM   1478 C CA  . GLU   A 1 198 ? -10.55382 -14.55433 -4.19094  1.000 19.10450  ? 205 GLU   A CA  1 
ATOM   1479 C C   . GLU   A 1 198 ? -9.46718  -13.71470 -4.84521  1.000 21.17012  ? 205 GLU   A C   1 
ATOM   1480 O O   . GLU   A 1 198 ? -9.31778  -12.52629 -4.53565  1.000 21.79091  ? 205 GLU   A O   1 
ATOM   1481 C CB  . GLU   A 1 198 ? -9.96227  -15.44851 -3.09751  1.000 19.51319  ? 205 GLU   A CB  1 
ATOM   1482 C CG  . GLU   A 1 198 ? -9.05570  -14.74004 -2.10791  1.000 21.58334  ? 205 GLU   A CG  1 
ATOM   1483 C CD  . GLU   A 1 198 ? -8.34921  -15.70936 -1.18048  1.000 24.36760  ? 205 GLU   A CD  1 
ATOM   1484 O OE1 . GLU   A 1 198 ? -7.76710  -16.69508 -1.68667  1.000 24.66108  ? 205 GLU   A OE1 1 
ATOM   1485 O OE2 . GLU   A 1 198 ? -8.37968  -15.49198 0.04841   1.000 24.91508  ? 205 GLU   A OE2 1 
ATOM   1486 N N   . ILE   A 1 199 ? -8.69476  -14.31994 -5.74650  1.000 16.84857  ? 206 ILE   A N   1 
ATOM   1487 C CA  . ILE   A 1 199 ? -7.59805  -13.60721 -6.39248  1.000 16.30996  ? 206 ILE   A CA  1 
ATOM   1488 C C   . ILE   A 1 199 ? -8.12830  -12.51522 -7.30662  1.000 23.25829  ? 206 ILE   A C   1 
ATOM   1489 O O   . ILE   A 1 199 ? -7.58541  -11.40684 -7.34632  1.000 21.12853  ? 206 ILE   A O   1 
ATOM   1490 C CB  . ILE   A 1 199 ? -6.70428  -14.60178 -7.15133  1.000 21.18536  ? 206 ILE   A CB  1 
ATOM   1491 C CG1 . ILE   A 1 199 ? -6.05799  -15.57192 -6.16407  1.000 20.37551  ? 206 ILE   A CG1 1 
ATOM   1492 C CG2 . ILE   A 1 199 ? -5.66816  -13.87698 -7.98188  1.000 18.92257  ? 206 ILE   A CG2 1 
ATOM   1493 C CD1 . ILE   A 1 199 ? -5.49347  -16.80660 -6.82208  1.000 22.12760  ? 206 ILE   A CD1 1 
ATOM   1494 N N   . VAL   A 1 200 ? -9.19326  -12.80469 -8.05542  1.000 20.63730  ? 207 VAL   A N   1 
ATOM   1495 C CA  . VAL   A 1 200 ? -9.75161  -11.79593 -8.95108  1.000 15.38115  ? 207 VAL   A CA  1 
ATOM   1496 C C   . VAL   A 1 200 ? -10.27985 -10.61038 -8.15193  1.000 18.92932  ? 207 VAL   A C   1 
ATOM   1497 O O   . VAL   A 1 200 ? -10.06695 -9.44924  -8.52248  1.000 21.87261  ? 207 VAL   A O   1 
ATOM   1498 C CB  . VAL   A 1 200 ? -10.83683 -12.42425 -9.84338  1.000 17.52526  ? 207 VAL   A CB  1 
ATOM   1499 C CG1 . VAL   A 1 200 ? -11.63300 -11.34010 -10.57262 1.000 21.72428  ? 207 VAL   A CG1 1 
ATOM   1500 C CG2 . VAL   A 1 200 ? -10.19184 -13.38656 -10.84071 1.000 20.02076  ? 207 VAL   A CG2 1 
ATOM   1501 N N   . LYS   A 1 201 ? -10.94556 -10.87849 -7.02557  1.000 17.40710  ? 208 LYS   A N   1 
ATOM   1502 C CA  . LYS   A 1 201 ? -11.47939 -9.78815  -6.21299  1.000 18.77110  ? 208 LYS   A CA  1 
ATOM   1503 C C   . LYS   A 1 201 ? -10.36408 -8.98203  -5.55734  1.000 21.52442  ? 208 LYS   A C   1 
ATOM   1504 O O   . LYS   A 1 201 ? -10.48299 -7.76013  -5.41568  1.000 29.18301  ? 208 LYS   A O   1 
ATOM   1505 C CB  . LYS   A 1 201 ? -12.43957 -10.35086 -5.16142  1.000 23.10600  ? 208 LYS   A CB  1 
ATOM   1506 C CG  . LYS   A 1 201 ? -13.00760 -9.32741  -4.18880  1.000 32.22018  ? 208 LYS   A CG  1 
ATOM   1507 C CD  . LYS   A 1 201 ? -13.87861 -10.01026 -3.14335  1.000 32.83492  ? 208 LYS   A CD  1 
ATOM   1508 C CE  . LYS   A 1 201 ? -14.50023 -9.00763  -2.18280  1.000 34.93069  ? 208 LYS   A CE  1 
ATOM   1509 N NZ  . LYS   A 1 201 ? -15.58041 -9.63084  -1.36648  1.000 50.64371  ? 208 LYS   A NZ  1 
ATOM   1510 N N   . LYS   A 1 202 ? -9.26981  -9.64511  -5.17284  1.000 21.98428  ? 209 LYS   A N   1 
ATOM   1511 C CA  . LYS   A 1 202 ? -8.17843  -8.97077  -4.47479  1.000 25.87400  ? 209 LYS   A CA  1 
ATOM   1512 C C   . LYS   A 1 202 ? -7.37905  -8.06629  -5.40639  1.000 23.97070  ? 209 LYS   A C   1 
ATOM   1513 O O   . LYS   A 1 202 ? -7.01069  -6.94595  -5.02737  1.000 22.71056  ? 209 LYS   A O   1 
ATOM   1514 C CB  . LYS   A 1 202 ? -7.25941  -10.01426 -3.83916  1.000 20.82699  ? 209 LYS   A CB  1 
ATOM   1515 C CG  . LYS   A 1 202 ? -6.05743  -9.44704  -3.11036  1.000 28.07050  ? 209 LYS   A CG  1 
ATOM   1516 C CD  . LYS   A 1 202 ? -5.28124  -10.56068 -2.42726  1.000 34.09205  ? 209 LYS   A CD  1 
ATOM   1517 C CE  . LYS   A 1 202 ? -4.14169  -10.01424 -1.58084  1.000 42.72283  ? 209 LYS   A CE  1 
ATOM   1518 N NZ  . LYS   A 1 202 ? -3.40596  -11.10596 -0.88250  1.000 57.85109  ? 209 LYS   A NZ  1 
ATOM   1519 N N   . HIS   A 1 203 ? -7.09171  -8.53663  -6.62273  1.000 25.24227  ? 210 HIS   A N   1 
ATOM   1520 C CA  . HIS   A 1 203 ? -6.09309  -7.91145  -7.47771  1.000 25.34944  ? 210 HIS   A CA  1 
ATOM   1521 C C   . HIS   A 1 203 ? -6.63570  -7.34769  -8.78120  1.000 27.85184  ? 210 HIS   A C   1 
ATOM   1522 O O   . HIS   A 1 203 ? -5.91283  -6.60237  -9.45135  1.000 25.66898  ? 210 HIS   A O   1 
ATOM   1523 C CB  . HIS   A 1 203 ? -4.98439  -8.91739  -7.82903  1.000 20.64232  ? 210 HIS   A CB  1 
ATOM   1524 C CG  . HIS   A 1 203 ? -4.17416  -9.36797  -6.65449  1.000 27.76594  ? 210 HIS   A CG  1 
ATOM   1525 N ND1 . HIS   A 1 203 ? -3.41935  -8.50312  -5.89131  1.000 27.94590  ? 210 HIS   A ND1 1 
ATOM   1526 C CD2 . HIS   A 1 203 ? -4.00898  -10.59612 -6.10660  1.000 26.94285  ? 210 HIS   A CD2 1 
ATOM   1527 C CE1 . HIS   A 1 203 ? -2.81804  -9.17922  -4.92896  1.000 31.29314  ? 210 HIS   A CE1 1 
ATOM   1528 N NE2 . HIS   A 1 203 ? -3.16079  -10.45056 -5.03554  1.000 34.06525  ? 210 HIS   A NE2 1 
ATOM   1529 N N   . SER   A 1 204 ? -7.86359  -7.68398  -9.17370  1.000 22.11872  ? 211 SER   A N   1 
ATOM   1530 C CA  . SER   A 1 204 ? -8.36476  -7.32621  -10.49730 1.000 22.79386  ? 211 SER   A CA  1 
ATOM   1531 C C   . SER   A 1 204 ? -9.75352  -6.70388  -10.42267 1.000 20.77171  ? 211 SER   A C   1 
ATOM   1532 O O   . SER   A 1 204 ? -10.52958 -6.79204  -11.37542 1.000 22.20467  ? 211 SER   A O   1 
ATOM   1533 C CB  . SER   A 1 204 ? -8.37660  -8.54482  -11.42614 1.000 25.61920  ? 211 SER   A CB  1 
ATOM   1534 O OG  . SER   A 1 204 ? -7.08700  -9.13714  -11.51267 1.000 27.16817  ? 211 SER   A OG  1 
ATOM   1535 N N   . GLN   A 1 205 ? -10.07209 -6.04025  -9.31451  1.000 27.39572  ? 212 GLN   A N   1 
ATOM   1536 C CA  . GLN   A 1 205 ? -11.43678 -5.57506  -9.11746  1.000 39.24231  ? 212 GLN   A CA  1 
ATOM   1537 C C   . GLN   A 1 205 ? -11.79361 -4.35515  -9.96390  1.000 33.99243  ? 212 GLN   A C   1 
ATOM   1538 O O   . GLN   A 1 205 ? -12.98428 -4.05141  -10.09630 1.000 37.23604  ? 212 GLN   A O   1 
ATOM   1539 C CB  . GLN   A 1 205 ? -11.67849 -5.28479  -7.63253  1.000 32.44770  ? 212 GLN   A CB  1 
ATOM   1540 C CG  . GLN   A 1 205 ? -10.89622 -4.11952  -7.07418  1.000 38.65909  ? 212 GLN   A CG  1 
ATOM   1541 C CD  . GLN   A 1 205 ? -9.53252  -4.51214  -6.51319  1.000 61.10239  ? 212 GLN   A CD  1 
ATOM   1542 O OE1 . GLN   A 1 205 ? -8.82214  -5.34723  -7.07919  1.000 42.09813  ? 212 GLN   A OE1 1 
ATOM   1543 N NE2 . GLN   A 1 205 ? -9.16656  -3.90848  -5.38703  1.000 54.43478  ? 212 GLN   A NE2 1 
ATOM   1544 N N   . PHE   A 1 206 ? -10.81608 -3.66921  -10.56621 1.000 27.46589  ? 213 PHE   A N   1 
ATOM   1545 C CA  . PHE   A 1 206 ? -11.09045 -2.49877  -11.39615 1.000 28.95351  ? 213 PHE   A CA  1 
ATOM   1546 C C   . PHE   A 1 206 ? -10.71887 -2.71590  -12.86388 1.000 28.54571  ? 213 PHE   A C   1 
ATOM   1547 O O   . PHE   A 1 206 ? -10.41643 -1.75892  -13.57881 1.000 44.17844  ? 213 PHE   A O   1 
ATOM   1548 C CB  . PHE   A 1 206 ? -10.37189 -1.26176  -10.85818 1.000 32.11847  ? 213 PHE   A CB  1 
ATOM   1549 C CG  . PHE   A 1 206 ? -10.75670 -0.90027  -9.45401  1.000 30.03724  ? 213 PHE   A CG  1 
ATOM   1550 C CD1 . PHE   A 1 206 ? -9.88417  -1.12286  -8.40169  1.000 37.54221  ? 213 PHE   A CD1 1 
ATOM   1551 C CD2 . PHE   A 1 206 ? -12.01133 -0.38447  -9.18100  1.000 35.39479  ? 213 PHE   A CD2 1 
ATOM   1552 C CE1 . PHE   A 1 206 ? -10.24155 -0.79211  -7.10456  1.000 41.18023  ? 213 PHE   A CE1 1 
ATOM   1553 C CE2 . PHE   A 1 206 ? -12.37724 -0.06053  -7.88849  1.000 41.36810  ? 213 PHE   A CE2 1 
ATOM   1554 C CZ  . PHE   A 1 206 ? -11.49251 -0.26843  -6.84911  1.000 39.81775  ? 213 PHE   A CZ  1 
ATOM   1555 N N   . ILE   A 1 207 ? -10.72807 -3.95896  -13.32878 1.000 19.95516  ? 214 ILE   A N   1 
ATOM   1556 C CA  . ILE   A 1 207 ? -10.52804 -4.24220  -14.74713 1.000 18.55060  ? 214 ILE   A CA  1 
ATOM   1557 C C   . ILE   A 1 207 ? -11.81956 -3.92192  -15.48888 1.000 23.54970  ? 214 ILE   A C   1 
ATOM   1558 O O   . ILE   A 1 207 ? -12.90360 -4.34799  -15.07568 1.000 22.96941  ? 214 ILE   A O   1 
ATOM   1559 C CB  . ILE   A 1 207 ? -10.10454 -5.70623  -14.95339 1.000 17.49690  ? 214 ILE   A CB  1 
ATOM   1560 C CG1 . ILE   A 1 207 ? -8.71077  -5.93405  -14.36402 1.000 21.56354  ? 214 ILE   A CG1 1 
ATOM   1561 C CG2 . ILE   A 1 207 ? -10.12128 -6.08015  -16.43042 1.000 17.95642  ? 214 ILE   A CG2 1 
ATOM   1562 C CD1 . ILE   A 1 207 ? -7.61721  -5.17353  -15.08339 1.000 27.27663  ? 214 ILE   A CD1 1 
ATOM   1563 N N   . GLY   A 1 208 ? -11.70909 -3.16320  -16.58076 1.000 19.54676  ? 215 GLY   A N   1 
ATOM   1564 C CA  . GLY   A 1 208 ? -12.86998 -2.60492  -17.25143 1.000 23.80753  ? 215 GLY   A CA  1 
ATOM   1565 C C   . GLY   A 1 208 ? -13.51867 -3.48869  -18.29778 1.000 21.06808  ? 215 GLY   A C   1 
ATOM   1566 O O   . GLY   A 1 208 ? -14.14412 -2.99101  -19.24254 1.000 22.23107  ? 215 GLY   A O   1 
ATOM   1567 N N   . TYR   A 1 209 ? -13.38903 -4.79824  -18.13203 1.000 19.18112  ? 216 TYR   A N   1 
ATOM   1568 C CA  . TYR   A 1 209 ? -13.99289 -5.77660  -19.02199 1.000 21.19627  ? 216 TYR   A CA  1 
ATOM   1569 C C   . TYR   A 1 209 ? -14.59118 -6.88209  -18.17190 1.000 21.67816  ? 216 TYR   A C   1 
ATOM   1570 O O   . TYR   A 1 209 ? -14.09447 -7.15704  -17.07297 1.000 19.14383  ? 216 TYR   A O   1 
ATOM   1571 C CB  . TYR   A 1 209 ? -12.96143 -6.35666  -20.00687 1.000 16.45678  ? 216 TYR   A CB  1 
ATOM   1572 C CG  . TYR   A 1 209 ? -12.35235 -5.28015  -20.87247 1.000 15.86840  ? 216 TYR   A CG  1 
ATOM   1573 C CD1 . TYR   A 1 209 ? -12.99571 -4.84330  -22.02249 1.000 19.92558  ? 216 TYR   A CD1 1 
ATOM   1574 C CD2 . TYR   A 1 209 ? -11.15844 -4.66259  -20.51357 1.000 20.43573  ? 216 TYR   A CD2 1 
ATOM   1575 C CE1 . TYR   A 1 209 ? -12.45509 -3.83701  -22.80311 1.000 16.82412  ? 216 TYR   A CE1 1 
ATOM   1576 C CE2 . TYR   A 1 209 ? -10.61186 -3.65187  -21.28860 1.000 17.19426  ? 216 TYR   A CE2 1 
ATOM   1577 C CZ  . TYR   A 1 209 ? -11.26691 -3.24748  -22.43326 1.000 17.41666  ? 216 TYR   A CZ  1 
ATOM   1578 O OH  . TYR   A 1 209 ? -10.74271 -2.24962  -23.21398 1.000 21.36499  ? 216 TYR   A OH  1 
ATOM   1579 N N   . PRO   A 1 210 ? -15.66542 -7.51654  -18.63558 1.000 17.10145  ? 217 PRO   A N   1 
ATOM   1580 C CA  . PRO   A 1 210 ? -16.25300 -8.61273  -17.85773 1.000 19.06631  ? 217 PRO   A CA  1 
ATOM   1581 C C   . PRO   A 1 210 ? -15.28290 -9.78082  -17.76148 1.000 19.69249  ? 217 PRO   A C   1 
ATOM   1582 O O   . PRO   A 1 210 ? -14.70061 -10.21266 -18.76005 1.000 19.96051  ? 217 PRO   A O   1 
ATOM   1583 C CB  . PRO   A 1 210 ? -17.52238 -8.97816  -18.64294 1.000 19.87496  ? 217 PRO   A CB  1 
ATOM   1584 C CG  . PRO   A 1 210 ? -17.34830 -8.38969  -20.00240 1.000 22.50583  ? 217 PRO   A CG  1 
ATOM   1585 C CD  . PRO   A 1 210 ? -16.43632 -7.20213  -19.85334 1.000 17.55397  ? 217 PRO   A CD  1 
ATOM   1586 N N   . ILE   A 1 211 ? -15.08737 -10.26730 -16.53980 1.000 20.28843  ? 218 ILE   A N   1 
ATOM   1587 C CA  . ILE   A 1 211 ? -14.25422 -11.43269 -16.26910 1.000 14.02570  ? 218 ILE   A CA  1 
ATOM   1588 C C   . ILE   A 1 211 ? -15.18808 -12.54687 -15.83493 1.000 16.26122  ? 218 ILE   A C   1 
ATOM   1589 O O   . ILE   A 1 211 ? -15.80806 -12.45974 -14.76739 1.000 18.23517  ? 218 ILE   A O   1 
ATOM   1590 C CB  . ILE   A 1 211 ? -13.20452 -11.16076 -15.18885 1.000 16.51654  ? 218 ILE   A CB  1 
ATOM   1591 C CG1 . ILE   A 1 211 ? -12.28807 -10.01065 -15.60782 1.000 18.81469  ? 218 ILE   A CG1 1 
ATOM   1592 C CG2 . ILE   A 1 211 ? -12.39876 -12.42638 -14.91461 1.000 17.48240  ? 218 ILE   A CG2 1 
ATOM   1593 C CD1 . ILE   A 1 211 ? -11.44395 -9.48283  -14.47062 1.000 17.18869  ? 218 ILE   A CD1 1 
ATOM   1594 N N   . THR   A 1 212 ? -15.29232 -13.59170 -16.64918 1.000 17.11896  ? 219 THR   A N   1 
ATOM   1595 C CA  . THR   A 1 212 ? -16.19757 -14.69974 -16.37218 1.000 17.35641  ? 219 THR   A CA  1 
ATOM   1596 C C   . THR   A 1 212 ? -15.38440 -15.90681 -15.93463 1.000 15.37415  ? 219 THR   A C   1 
ATOM   1597 O O   . THR   A 1 212 ? -14.56276 -16.41642 -16.70378 1.000 18.61998  ? 219 THR   A O   1 
ATOM   1598 C CB  . THR   A 1 212 ? -17.04289 -15.03823 -17.59697 1.000 17.75323  ? 219 THR   A CB  1 
ATOM   1599 O OG1 . THR   A 1 212 ? -17.82487 -13.89330 -17.96052 1.000 17.63955  ? 219 THR   A OG1 1 
ATOM   1600 C CG2 . THR   A 1 212 ? -17.96074 -16.22867 -17.30257 1.000 24.03502  ? 219 THR   A CG2 1 
ATOM   1601 N N   . LEU   A 1 213 ? -15.61034 -16.35194 -14.70162 1.000 17.70477  ? 220 LEU   A N   1 
ATOM   1602 C CA  . LEU   A 1 213 ? -14.98963 -17.56449 -14.18117 1.000 17.27067  ? 220 LEU   A CA  1 
ATOM   1603 C C   . LEU   A 1 213 ? -15.90111 -18.73709 -14.52446 1.000 16.63225  ? 220 LEU   A C   1 
ATOM   1604 O O   . LEU   A 1 213 ? -17.00679 -18.84936 -13.98095 1.000 17.39233  ? 220 LEU   A O   1 
ATOM   1605 C CB  . LEU   A 1 213 ? -14.77184 -17.45938 -12.67181 1.000 16.75398  ? 220 LEU   A CB  1 
ATOM   1606 C CG  . LEU   A 1 213 ? -14.26726 -18.71470 -11.95433 1.000 21.58231  ? 220 LEU   A CG  1 
ATOM   1607 C CD1 . LEU   A 1 213 ? -13.05472 -19.30642 -12.66809 1.000 18.57692  ? 220 LEU   A CD1 1 
ATOM   1608 C CD2 . LEU   A 1 213 ? -13.93196 -18.39950 -10.49774 1.000 21.26034  ? 220 LEU   A CD2 1 
ATOM   1609 N N   . PHE   A 1 214 ? -15.45412 -19.58620 -15.44621 1.000 16.95516  ? 221 PHE   A N   1 
ATOM   1610 C CA  . PHE   A 1 214 ? -16.21382 -20.77723 -15.80356 1.000 19.07974  ? 221 PHE   A CA  1 
ATOM   1611 C C   . PHE   A 1 214 ? -16.18413 -21.78375 -14.65531 1.000 20.56164  ? 221 PHE   A C   1 
ATOM   1612 O O   . PHE   A 1 214 ? -15.21673 -21.85746 -13.89208 1.000 20.91891  ? 221 PHE   A O   1 
ATOM   1613 C CB  . PHE   A 1 214 ? -15.63184 -21.44633 -17.05463 1.000 16.43133  ? 221 PHE   A CB  1 
ATOM   1614 C CG  . PHE   A 1 214 ? -15.90724 -20.73135 -18.36204 1.000 15.10120  ? 221 PHE   A CG  1 
ATOM   1615 C CD1 . PHE   A 1 214 ? -15.98347 -19.34587 -18.43954 1.000 16.69030  ? 221 PHE   A CD1 1 
ATOM   1616 C CD2 . PHE   A 1 214 ? -16.04017 -21.47185 -19.53179 1.000 15.72010  ? 221 PHE   A CD2 1 
ATOM   1617 C CE1 . PHE   A 1 214 ? -16.20645 -18.70843 -19.65544 1.000 15.65042  ? 221 PHE   A CE1 1 
ATOM   1618 C CE2 . PHE   A 1 214 ? -16.26451 -20.84902 -20.74918 1.000 19.53298  ? 221 PHE   A CE2 1 
ATOM   1619 C CZ  . PHE   A 1 214 ? -16.35460 -19.46493 -20.81511 1.000 17.42611  ? 221 PHE   A CZ  1 
ATOM   1620 N N   . VAL   A 1 215 ? -17.24499 -22.57889 -14.54520 1.000 18.89372  ? 222 VAL   A N   1 
ATOM   1621 C CA  . VAL   A 1 215 ? -17.30011 -23.66627 -13.57658 1.000 20.77057  ? 222 VAL   A CA  1 
ATOM   1622 C C   . VAL   A 1 215 ? -17.14188 -24.99128 -14.31746 1.000 23.30064  ? 222 VAL   A C   1 
ATOM   1623 O O   . VAL   A 1 215 ? -17.20553 -25.05454 -15.54477 1.000 22.12534  ? 222 VAL   A O   1 
ATOM   1624 C CB  . VAL   A 1 215 ? -18.59607 -23.64618 -12.74601 1.000 31.51535  ? 222 VAL   A CB  1 
ATOM   1625 C CG1 . VAL   A 1 215 ? -18.46809 -22.64720 -11.59468 1.000 40.59778  ? 222 VAL   A CG1 1 
ATOM   1626 C CG2 . VAL   A 1 215 ? -19.77537 -23.32394 -13.62173 1.000 23.50501  ? 222 VAL   A CG2 1 
ATOM   1627 N N   . GLU   A 1 216 ? -16.93317 -26.06014 -13.55534 1.000 23.82829  ? 223 GLU   A N   1 
ATOM   1628 C CA  . GLU   A 1 216 ? -16.66635 -27.37934 -14.12044 1.000 24.78764  ? 223 GLU   A CA  1 
ATOM   1629 C C   . GLU   A 1 216 ? -17.72359 -28.39345 -13.70059 1.000 33.82183  ? 223 GLU   A C   1 
ATOM   1630 O O   . GLU   A 1 216 ? -18.69581 -28.07062 -13.01690 1.000 37.53047  ? 223 GLU   A O   1 
ATOM   1631 C CB  . GLU   A 1 216 ? -15.28641 -27.90051 -13.71368 1.000 32.67937  ? 223 GLU   A CB  1 
ATOM   1632 C CG  . GLU   A 1 216 ? -14.12595 -27.01364 -14.06935 1.000 28.91402  ? 223 GLU   A CG  1 
ATOM   1633 C CD  . GLU   A 1 216 ? -12.82330 -27.57407 -13.54077 1.000 40.78269  ? 223 GLU   A CD  1 
ATOM   1634 O OE1 . GLU   A 1 216 ? -12.36961 -28.60545 -14.08228 1.000 30.86293  ? 223 GLU   A OE1 1 
ATOM   1635 O OE2 . GLU   A 1 216 ? -12.24962 -26.97791 -12.60101 1.000 36.88922  ? 223 GLU   A OE2 1 
ATOM   1636 N N   . LYS   A 1 217 ? -17.47992 -29.63601 -14.12683 1.000 55.82068  ? 224 LYS   A N   1 
ATOM   1637 C CA  . LYS   A 1 217 ? -18.29518 -30.82332 -13.85846 1.000 50.66310  ? 224 LYS   A CA  1 
ATOM   1638 C C   . LYS   A 1 217 ? -19.55846 -30.82278 -14.70754 1.000 68.34764  ? 224 LYS   A C   1 
ATOM   1639 O O   . LYS   A 1 217 ? -19.58987 -31.43773 -15.77540 1.000 75.34367  ? 224 LYS   A O   1 
ATOM   1640 C CB  . LYS   A 1 217 ? -18.64673 -30.93916 -12.37160 1.000 47.61669  ? 224 LYS   A CB  1 
ATOM   1641 C CG  . LYS   A 1 217 ? -18.64578 -32.36158 -11.84829 1.000 60.81502  ? 224 LYS   A CG  1 
ATOM   1642 C CD  . LYS   A 1 217 ? -18.03261 -32.43788 -10.46236 1.000 57.48483  ? 224 LYS   A CD  1 
ATOM   1643 C CE  . LYS   A 1 217 ? -17.67874 -33.87011 -10.09661 1.000 60.80492  ? 224 LYS   A CE  1 
ATOM   1644 N NZ  . LYS   A 1 217 ? -16.26522 -34.19144 -10.44168 1.000 59.95150  ? 224 LYS   A NZ  1 
HETATM 1645 C C1  . A1AX8 B 2 .   ? -2.54357  -10.67557 -24.97330 0.307 23.62845  ? 301 A1AX8 A C1  1 
HETATM 1646 C C2  . A1AX8 B 2 .   ? -1.12761  -10.66393 -24.51094 1.000 30.44986  ? 301 A1AX8 A C2  1 
HETATM 1647 C C3  . A1AX8 B 2 .   ? -0.41027  -9.47503  -24.49112 0.537 28.07375  ? 301 A1AX8 A C3  1 
HETATM 1648 C C4  . A1AX8 B 2 .   ? 0.90829   -9.46157  -24.07265 1.000 38.49590  ? 301 A1AX8 A C4  1 
HETATM 1649 C C5  . A1AX8 B 2 .   ? 1.55121   -10.63017 -23.67796 0.684 24.64519  ? 301 A1AX8 A C5  1 
HETATM 1650 C C6  . A1AX8 B 2 .   ? 0.81727   -11.83447 -23.70885 1.000 23.21987  ? 301 A1AX8 A C6  1 
HETATM 1651 C C7  . A1AX8 B 2 .   ? -0.50629  -11.84745 -24.12893 1.000 34.24150  ? 301 A1AX8 A C7  1 
HETATM 1652 C C8  . A1AX8 B 2 .   ? 2.97565   -10.60749 -23.22786 1.000 22.54633  ? 301 A1AX8 A C8  1 
HETATM 1653 N N1  . A1AX8 B 2 .   ? -3.48342  -11.03076 -24.10503 1.000 24.10270  ? 301 A1AX8 A N1  1 
HETATM 1654 N N2  . A1AX8 B 2 .   ? 1.41449   -13.02366 -23.33286 0.131 22.89364  ? 301 A1AX8 A N2  1 
HETATM 1655 O O1  . A1AX8 B 2 .   ? -2.80230  -10.35191 -26.14193 0.945 30.54860  ? 301 A1AX8 A O1  1 
HETATM 1656 O O   . HOH   C 3 .   ? -18.04103 -5.17438  -37.40000 1.000 46.02720  ? 401 HOH   A O   1 
HETATM 1657 O O   . HOH   C 3 .   ? 11.74076  -21.23536 -40.51758 1.000 48.44528  ? 402 HOH   A O   1 
HETATM 1658 O O   . HOH   C 3 .   ? 6.85197   -23.01769 -41.20577 1.000 51.12112  ? 403 HOH   A O   1 
HETATM 1659 O O   . HOH   C 3 .   ? -17.40128 -24.57243 -8.91751  1.000 50.37952  ? 404 HOH   A O   1 
HETATM 1660 O O   . HOH   C 3 .   ? 2.17522   -15.71880 -41.13183 1.000 38.59858  ? 405 HOH   A O   1 
HETATM 1661 O O   . HOH   C 3 .   ? -1.61115  -29.00058 -5.97009  1.000 30.02214  ? 406 HOH   A O   1 
HETATM 1662 O O   . HOH   C 3 .   ? 1.08992   -26.88646 -2.98245  1.000 41.76524  ? 407 HOH   A O   1 
HETATM 1663 O O   . HOH   C 3 .   ? 3.69363   -29.63595 -25.78133 1.000 39.35327  ? 408 HOH   A O   1 
HETATM 1664 O O   . HOH   C 3 .   ? -20.42457 -20.67099 -9.26827  1.000 41.39279  ? 409 HOH   A O   1 
HETATM 1665 O O   . HOH   C 3 .   ? -8.40266  1.83176   -36.48083 1.000 32.67599  ? 410 HOH   A O   1 
HETATM 1666 O O   . HOH   C 3 .   ? -0.38430  -5.64020  -38.63183 1.000 47.17015  ? 411 HOH   A O   1 
HETATM 1667 O O   . HOH   C 3 .   ? 5.05960   -28.93234 -8.26414  1.000 42.64248  ? 412 HOH   A O   1 
HETATM 1668 O O   . HOH   C 3 .   ? 13.72274  -11.30015 -29.48551 1.000 36.62455  ? 413 HOH   A O   1 
HETATM 1669 O O   . HOH   C 3 .   ? -1.67908  -8.70002  -27.74082 1.000 23.18325  ? 414 HOH   A O   1 
HETATM 1670 O O   . HOH   C 3 .   ? -14.39132 -6.69120  -14.57104 1.000 34.00824  ? 415 HOH   A O   1 
HETATM 1671 O O   . HOH   C 3 .   ? 3.31037   -24.36968 -38.69116 1.000 32.12435  ? 416 HOH   A O   1 
HETATM 1672 O O   . HOH   C 3 .   ? -13.01907 -7.26521  -11.80359 1.000 34.31579  ? 417 HOH   A O   1 
HETATM 1673 O O   . HOH   C 3 .   ? -8.02879  -22.64294 -30.33774 1.000 36.42017  ? 418 HOH   A O   1 
HETATM 1674 O O   . HOH   C 3 .   ? 9.65996   -14.62307 -25.16807 1.000 20.58348  ? 419 HOH   A O   1 
HETATM 1675 O O   . HOH   C 3 .   ? 5.95147   -21.76564 -37.28625 1.000 27.74908  ? 420 HOH   A O   1 
HETATM 1676 O O   . HOH   C 3 .   ? 20.24458  -3.44877  -8.09583  1.000 51.02447  ? 421 HOH   A O   1 
HETATM 1677 O O   . HOH   C 3 .   ? -8.73995  -11.88897 -36.34862 1.000 25.00841  ? 422 HOH   A O   1 
HETATM 1678 O O   . HOH   C 3 .   ? 6.58496   -29.42678 -20.06067 1.000 31.65795  ? 423 HOH   A O   1 
HETATM 1679 O O   . HOH   C 3 .   ? -3.21714  -12.09898 -9.20353  1.000 34.52710  ? 424 HOH   A O   1 
HETATM 1680 O O   . HOH   C 3 .   ? -0.19545  -5.26398  -18.48210 1.000 25.03301  ? 425 HOH   A O   1 
HETATM 1681 O O   . HOH   C 3 .   ? 7.81771   1.17662   -14.64196 1.000 34.97319  ? 426 HOH   A O   1 
HETATM 1682 O O   . HOH   C 3 .   ? 5.83508   -25.52634 -7.21654  1.000 40.48456  ? 427 HOH   A O   1 
HETATM 1683 O O   . HOH   C 3 .   ? -16.08685 -25.49854 -17.85832 1.000 30.18738  ? 428 HOH   A O   1 
HETATM 1684 O O   . HOH   C 3 .   ? -12.26972 -27.72903 -29.96469 1.000 35.31886  ? 429 HOH   A O   1 
HETATM 1685 O O   . HOH   C 3 .   ? -4.26218  0.46867   -22.26522 1.000 30.78109  ? 430 HOH   A O   1 
HETATM 1686 O O   . HOH   C 3 .   ? 7.69675   -18.85885 -6.46485  1.000 22.03815  ? 431 HOH   A O   1 
HETATM 1687 O O   . HOH   C 3 .   ? 1.41007   -7.75174  -16.56281 1.000 19.97024  ? 432 HOH   A O   1 
HETATM 1688 O O   . HOH   C 3 .   ? -2.31548  -13.70251 -35.68536 1.000 18.19758  ? 433 HOH   A O   1 
HETATM 1689 O O   . HOH   C 3 .   ? -10.69707 -14.64546 0.97125   1.000 28.30839  ? 434 HOH   A O   1 
HETATM 1690 O O   . HOH   C 3 .   ? -5.79394  -2.08389  -19.54928 1.000 19.57970  ? 435 HOH   A O   1 
HETATM 1691 O O   . HOH   C 3 .   ? -15.85786 0.29950   -30.46100 1.000 36.60551  ? 436 HOH   A O   1 
HETATM 1692 O O   . HOH   C 3 .   ? 0.88546   -20.83732 -4.67678  1.000 24.08290  ? 437 HOH   A O   1 
HETATM 1693 O O   . HOH   C 3 .   ? -2.72444  -3.26782  -35.34782 1.000 45.31159  ? 438 HOH   A O   1 
HETATM 1694 O O   . HOH   C 3 .   ? 7.31239   -16.86486 -41.37328 1.000 54.39443  ? 439 HOH   A O   1 
HETATM 1695 O O   . HOH   C 3 .   ? 7.67735   -27.73547 -23.99502 1.000 28.20128  ? 440 HOH   A O   1 
HETATM 1696 O O   . HOH   C 3 .   ? 7.80039   -23.36184 -14.16101 1.000 28.82620  ? 441 HOH   A O   1 
HETATM 1697 O O   . HOH   C 3 .   ? 12.93850  -8.78086  -34.20417 1.000 49.62796  ? 442 HOH   A O   1 
HETATM 1698 O O   . HOH   C 3 .   ? 3.11722   -6.08928  -11.11649 1.000 25.93189  ? 443 HOH   A O   1 
HETATM 1699 O O   . HOH   C 3 .   ? -17.06780 -5.47945  -22.88155 1.000 23.67146  ? 444 HOH   A O   1 
HETATM 1700 O O   . HOH   C 3 .   ? 0.30763   -22.22366 -2.14269  1.000 42.28188  ? 445 HOH   A O   1 
HETATM 1701 O O   . HOH   C 3 .   ? 9.76189   -17.52373 -7.74098  1.000 23.96373  ? 446 HOH   A O   1 
HETATM 1702 O O   . HOH   C 3 .   ? 8.45364   -16.18003 -39.45912 1.000 31.81360  ? 447 HOH   A O   1 
HETATM 1703 O O   . HOH   C 3 .   ? -18.85747 -10.83884 -23.84695 1.000 28.73402  ? 448 HOH   A O   1 
HETATM 1704 O O   . HOH   C 3 .   ? -13.33736 -0.78626  -20.51409 1.000 29.92795  ? 449 HOH   A O   1 
HETATM 1705 O O   . HOH   C 3 .   ? 19.58099  -16.54387 -27.52539 1.000 41.22911  ? 450 HOH   A O   1 
HETATM 1706 O O   . HOH   C 3 .   ? -13.02143 -24.90057 -10.71458 1.000 32.09264  ? 451 HOH   A O   1 
HETATM 1707 O O   . HOH   C 3 .   ? 9.12491   -26.39890 -17.00712 1.000 28.63921  ? 452 HOH   A O   1 
HETATM 1708 O O   . HOH   C 3 .   ? -6.73088  -5.18456  -39.29779 1.000 46.43394  ? 453 HOH   A O   1 
HETATM 1709 O O   . HOH   C 3 .   ? 4.78545   -33.68681 -11.36034 1.000 45.92868  ? 454 HOH   A O   1 
HETATM 1710 O O   . HOH   C 3 .   ? 0.43076   -14.91809 -1.51573  1.000 36.95666  ? 455 HOH   A O   1 
HETATM 1711 O O   . HOH   C 3 .   ? 0.74167   -5.38913  -14.02849 1.000 38.45248  ? 456 HOH   A O   1 
HETATM 1712 O O   . HOH   C 3 .   ? -5.27092  -10.49205 -27.32661 1.000 17.51551  ? 457 HOH   A O   1 
HETATM 1713 O O   . HOH   C 3 .   ? 0.80607   -26.87492 -37.27405 1.000 40.01834  ? 458 HOH   A O   1 
HETATM 1714 O O   . HOH   C 3 .   ? -7.00534  -27.82560 -21.24367 1.000 40.40903  ? 459 HOH   A O   1 
HETATM 1715 O O   . HOH   C 3 .   ? 11.57743  -27.30207 -34.66338 1.000 24.28435  ? 460 HOH   A O   1 
HETATM 1716 O O   . HOH   C 3 .   ? 3.60623   -7.74934  -36.69511 1.000 33.25234  ? 461 HOH   A O   1 
HETATM 1717 O O   . HOH   C 3 .   ? -6.46658  -7.75718  -34.31737 1.000 18.96320  ? 462 HOH   A O   1 
HETATM 1718 O O   . HOH   C 3 .   ? 11.15947  -8.11101  -27.53992 1.000 21.59043  ? 463 HOH   A O   1 
HETATM 1719 O O   . HOH   C 3 .   ? 6.63932   -26.66632 -27.63525 1.000 33.08804  ? 464 HOH   A O   1 
HETATM 1720 O O   . HOH   C 3 .   ? -2.74787  -2.83413  -17.49149 1.000 39.63463  ? 465 HOH   A O   1 
HETATM 1721 O O   . HOH   C 3 .   ? -3.05888  -5.87445  -6.45472  1.000 41.72767  ? 466 HOH   A O   1 
HETATM 1722 O O   . HOH   C 3 .   ? 13.56086  -14.12935 -26.77857 1.000 22.78696  ? 467 HOH   A O   1 
HETATM 1723 O O   . HOH   C 3 .   ? -10.96488 -14.33075 -37.71490 1.000 34.55690  ? 468 HOH   A O   1 
HETATM 1724 O O   . HOH   C 3 .   ? -9.93873  -0.47852  -19.96886 1.000 32.63400  ? 469 HOH   A O   1 
HETATM 1725 O O   . HOH   C 3 .   ? 9.42913   -11.06288 -34.93916 1.000 39.79948  ? 470 HOH   A O   1 
HETATM 1726 O O   . HOH   C 3 .   ? 8.79109   -15.35665 -27.83136 1.000 17.56025  ? 471 HOH   A O   1 
HETATM 1727 O O   . HOH   C 3 .   ? -8.22636  -24.74568 -19.06690 1.000 17.41642  ? 472 HOH   A O   1 
HETATM 1728 O O   . HOH   C 3 .   ? -1.26925  -26.03504 -32.17975 1.000 33.41401  ? 473 HOH   A O   1 
HETATM 1729 O O   . HOH   C 3 .   ? -0.98596  -11.34287 -2.91206  1.000 34.92948  ? 474 HOH   A O   1 
HETATM 1730 O O   . HOH   C 3 .   ? 11.27505  -28.32090 -30.47616 1.000 28.27889  ? 475 HOH   A O   1 
HETATM 1731 O O   . HOH   C 3 .   ? -8.51352  4.76550   -33.65158 1.000 32.84565  ? 476 HOH   A O   1 
HETATM 1732 O O   . HOH   C 3 .   ? -7.72102  -24.28246 -22.95852 1.000 28.80504  ? 477 HOH   A O   1 
HETATM 1733 O O   . HOH   C 3 .   ? 1.39481   -3.26227  -24.64633 1.000 39.14226  ? 478 HOH   A O   1 
HETATM 1734 O O   . HOH   C 3 .   ? 4.12073   -24.09779 -30.62413 1.000 19.86608  ? 479 HOH   A O   1 
HETATM 1735 O O   . HOH   C 3 .   ? -6.30181  -5.05465  -35.55062 1.000 19.81348  ? 480 HOH   A O   1 
HETATM 1736 O O   . HOH   C 3 .   ? -18.36247 -3.96245  -29.21828 1.000 48.16763  ? 481 HOH   A O   1 
HETATM 1737 O O   . HOH   C 3 .   ? -8.90171  -10.51164 -40.46982 1.000 39.81150  ? 482 HOH   A O   1 
HETATM 1738 O O   . HOH   C 3 .   ? 0.63796   -29.57869 -15.99951 1.000 32.98984  ? 483 HOH   A O   1 
HETATM 1739 O O   . HOH   C 3 .   ? -13.68377 -16.99881 -2.65619  1.000 23.41474  ? 484 HOH   A O   1 
HETATM 1740 O O   . HOH   C 3 .   ? -6.20141  -7.13435  -42.19045 1.000 49.14880  ? 485 HOH   A O   1 
HETATM 1741 O O   . HOH   C 3 .   ? -9.26994  -2.29297  -17.57785 1.000 20.84703  ? 486 HOH   A O   1 
HETATM 1742 O O   . HOH   C 3 .   ? -0.37686  -12.42716 -20.97273 1.000 28.63591  ? 487 HOH   A O   1 
HETATM 1743 O O   . HOH   C 3 .   ? -5.90998  -31.22629 -11.50093 1.000 33.77242  ? 488 HOH   A O   1 
HETATM 1744 O O   . HOH   C 3 .   ? -3.27267  -3.15339  -40.28580 1.000 51.30221  ? 489 HOH   A O   1 
HETATM 1745 O O   . HOH   C 3 .   ? 18.31284  -7.32279  -20.23071 1.000 36.76778  ? 490 HOH   A O   1 
HETATM 1746 O O   . HOH   C 3 .   ? 9.28486   -3.12546  -20.56081 1.000 31.83689  ? 491 HOH   A O   1 
HETATM 1747 O O   . HOH   C 3 .   ? -1.42594  -27.17115 -34.94477 1.000 51.50102  ? 492 HOH   A O   1 
HETATM 1748 O O   . HOH   C 3 .   ? 10.56402  -25.39650 -23.65512 1.000 21.58821  ? 493 HOH   A O   1 
HETATM 1749 O O   . HOH   C 3 .   ? 10.73274  -25.54578 -26.63458 1.000 28.33674  ? 494 HOH   A O   1 
HETATM 1750 O O   . HOH   C 3 .   ? -16.22368 -12.63203 -19.82388 1.000 20.07700  ? 495 HOH   A O   1 
HETATM 1751 O O   . HOH   C 3 .   ? 15.51653  -20.19423 -18.72910 1.000 23.88047  ? 496 HOH   A O   1 
HETATM 1752 O O   . HOH   C 3 .   ? -19.43085 -10.01841 -33.13001 1.000 45.08553  ? 497 HOH   A O   1 
HETATM 1753 O O   . HOH   C 3 .   ? -20.56889 -13.98552 -18.27844 1.000 41.42534  ? 498 HOH   A O   1 
HETATM 1754 O O   . HOH   C 3 .   ? -5.63380  -28.41112 -4.92177  1.000 49.73905  ? 499 HOH   A O   1 
HETATM 1755 O O   . HOH   C 3 .   ? 12.95733  -13.82419 -29.68229 1.000 25.41996  ? 500 HOH   A O   1 
HETATM 1756 O O   . HOH   C 3 .   ? -6.18754  -11.33209 -10.08723 1.000 23.46605  ? 501 HOH   A O   1 
HETATM 1757 O O   . HOH   C 3 .   ? 0.11003   -28.43607 -25.65192 1.000 45.96141  ? 502 HOH   A O   1 
HETATM 1758 O O   . HOH   C 3 .   ? -14.14726 -12.62235 -7.77838  1.000 21.85523  ? 503 HOH   A O   1 
HETATM 1759 O O   . HOH   C 3 .   ? -11.75959 -0.20539  -15.44730 1.000 43.91259  ? 504 HOH   A O   1 
HETATM 1760 O O   . HOH   C 3 .   ? -4.13822  -4.74373  -8.39709  1.000 41.35050  ? 505 HOH   A O   1 
HETATM 1761 O O   . HOH   C 3 .   ? -14.47944 -22.60517 -11.31369 1.000 27.43453  ? 506 HOH   A O   1 
HETATM 1762 O O   . HOH   C 3 .   ? -1.75450  -25.67765 -4.74131  1.000 24.62524  ? 507 HOH   A O   1 
HETATM 1763 O O   . HOH   C 3 .   ? 14.36450  -15.90124 -30.65915 1.000 33.92825  ? 508 HOH   A O   1 
HETATM 1764 O O   . HOH   C 3 .   ? 17.98671  -19.25596 -24.57966 1.000 27.58026  ? 509 HOH   A O   1 
HETATM 1765 O O   . HOH   C 3 .   ? -16.08493 -3.03215  -21.25249 1.000 27.56554  ? 510 HOH   A O   1 
HETATM 1766 O O   . HOH   C 3 .   ? -17.82191 -18.67613 -10.98875 1.000 40.18546  ? 511 HOH   A O   1 
HETATM 1767 O O   . HOH   C 3 .   ? -8.81161  -18.06155 -36.56256 1.000 35.00608  ? 512 HOH   A O   1 
HETATM 1768 O O   . HOH   C 3 .   ? 7.51458   -30.70646 -14.72318 1.000 44.79329  ? 513 HOH   A O   1 
HETATM 1769 O O   . HOH   C 3 .   ? 1.03589   -6.07300  -34.28076 1.000 43.12338  ? 514 HOH   A O   1 
HETATM 1770 O O   . HOH   C 3 .   ? -10.27822 -11.47840 -2.12536  1.000 21.12065  ? 515 HOH   A O   1 
HETATM 1771 O O   . HOH   C 3 .   ? 8.41607   -20.38762 -9.27155  1.000 34.47573  ? 516 HOH   A O   1 
HETATM 1772 O O   . HOH   C 3 .   ? -3.30011  -21.24485 -0.55907  1.000 30.99385  ? 517 HOH   A O   1 
HETATM 1773 O O   . HOH   C 3 .   ? 14.07989  -15.65104 -1.93259  1.000 35.09445  ? 518 HOH   A O   1 
HETATM 1774 O O   . HOH   C 3 .   ? 20.50529  -10.74856 -26.19804 1.000 42.41717  ? 519 HOH   A O   1 
HETATM 1775 O O   . HOH   C 3 .   ? -10.69709 -6.34797  -2.99426  1.000 42.69553  ? 520 HOH   A O   1 
HETATM 1776 O O   . HOH   C 3 .   ? -19.734   -12.780   -16.222   1.000 53.62242  ? 521 HOH   A O   1 
HETATM 1777 O O   . HOH   C 3 .   ? 11.86868  -2.21781  -3.71618  1.000 50.03495  ? 522 HOH   A O   1 
HETATM 1778 O O   . HOH   C 3 .   ? -1.36653  -4.55176  -33.79846 1.000 35.55677  ? 523 HOH   A O   1 
HETATM 1779 O O   . HOH   C 3 .   ? -5.05639  -14.23586 -22.67251 1.000 15.44238  ? 524 HOH   A O   1 
HETATM 1780 O O   . HOH   C 3 .   ? 15.63426  -0.76014  -19.51963 1.000 34.21095  ? 525 HOH   A O   1 
HETATM 1781 O O   . HOH   C 3 .   ? -6.13732  -13.97866 0.84487   1.000 26.89291  ? 526 HOH   A O   1 
HETATM 1782 O O   . HOH   C 3 .   ? -1.49927  -6.23831  -26.24460 1.000 18.31064  ? 527 HOH   A O   1 
HETATM 1783 O O   . HOH   C 3 .   ? -19.778   -19.341   -14.219   1.000 22.10400  ? 528 HOH   A O   1 
HETATM 1784 O O   . HOH   C 3 .   ? 3.13416   -20.48921 -2.80702  1.000 36.50613  ? 529 HOH   A O   1 
HETATM 1785 O O   . HOH   C 3 .   ? 12.14213  -27.47369 -19.76797 1.000 46.14284  ? 530 HOH   A O   1 
HETATM 1786 O O   . HOH   C 3 .   ? 5.96451   -21.27250 -0.04662  1.000 26.05670  ? 531 HOH   A O   1 
HETATM 1787 O O   . HOH   C 3 .   ? 8.71414   -20.27381 -4.27594  1.000 27.70539  ? 532 HOH   A O   1 
HETATM 1788 O O   . HOH   C 3 .   ? -15.616   6.487     -32.312   1.000 40.28781  ? 533 HOH   A O   1 
HETATM 1789 O O   . HOH   C 3 .   ? -14.41636 -21.94625 -33.25059 1.000 39.07087  ? 534 HOH   A O   1 
HETATM 1790 O O   . HOH   C 3 .   ? 14.734    -0.515    -12.132   1.000 48.86818  ? 535 HOH   A O   1 
HETATM 1791 O O   . HOH   C 3 .   ? -5.37390  -7.61518  -13.19343 1.000 20.30605  ? 536 HOH   A O   1 
HETATM 1792 O O   . HOH   C 3 .   ? -4.61302  -4.37906  -37.24081 1.000 41.17689  ? 537 HOH   A O   1 
HETATM 1793 O O   . HOH   C 3 .   ? -8.22488  4.17787   -38.85096 1.000 48.01066  ? 538 HOH   A O   1 
HETATM 1794 O O   . HOH   C 3 .   ? -14.23746 -15.00430 -30.90199 1.000 54.22051  ? 539 HOH   A O   1 
HETATM 1795 O O   . HOH   C 3 .   ? -1.78115  -32.47995 -7.75886  1.000 47.95664  ? 540 HOH   A O   1 
HETATM 1796 O O   . HOH   C 3 .   ? 3.64611   -6.73143  -17.83293 1.000 23.28149  ? 541 HOH   A O   1 
HETATM 1797 O O   . HOH   C 3 .   ? 10.12438  -5.89472  -1.76456  1.000 49.00665  ? 542 HOH   A O   1 
HETATM 1798 O O   . HOH   C 3 .   ? -15.20578 -11.12395 -29.83751 1.000 23.04196  ? 543 HOH   A O   1 
HETATM 1799 O O   . HOH   C 3 .   ? 0.37218   -5.36381  -22.09859 1.000 29.03809  ? 544 HOH   A O   1 
HETATM 1800 O O   . HOH   C 3 .   ? 3.72524   -11.89060 -38.62647 1.000 26.16582  ? 545 HOH   A O   1 
HETATM 1801 O O   . HOH   C 3 .   ? 7.83366   -23.38718 -7.18030  1.000 33.28763  ? 546 HOH   A O   1 
HETATM 1802 O O   . HOH   C 3 .   ? -7.33412  -22.78650 -36.44630 1.000 41.21511  ? 547 HOH   A O   1 
HETATM 1803 O O   . HOH   C 3 .   ? -7.96582  -3.97899  -10.79860 1.000 30.52329  ? 548 HOH   A O   1 
HETATM 1804 O O   . HOH   C 3 .   ? -13.56555 -26.39394 -18.05523 1.000 25.75744  ? 549 HOH   A O   1 
HETATM 1805 O O   . HOH   C 3 .   ? -3.09028  -31.51569 -20.09863 1.000 46.45068  ? 550 HOH   A O   1 
HETATM 1806 O O   . HOH   C 3 .   ? 10.47488  -21.46332 -6.88269  1.000 38.96295  ? 551 HOH   A O   1 
HETATM 1807 O O   . HOH   C 3 .   ? 3.93268   -9.13148  -20.14817 1.000 20.75028  ? 552 HOH   A O   1 
HETATM 1808 O O   . HOH   C 3 .   ? -4.57673  0.43334   -30.48512 1.000 23.74635  ? 553 HOH   A O   1 
HETATM 1809 O O   . HOH   C 3 .   ? -3.07456  -1.09387  -24.20061 1.000 25.15360  ? 554 HOH   A O   1 
HETATM 1810 O O   . HOH   C 3 .   ? 13.70942  -20.42500 -20.68357 1.000 18.88362  ? 555 HOH   A O   1 
HETATM 1811 O O   . HOH   C 3 .   ? 8.75153   -19.97871 -41.56743 1.000 47.36974  ? 556 HOH   A O   1 
HETATM 1812 O O   . HOH   C 3 .   ? -16.08127 -25.48146 -10.82944 1.000 36.63417  ? 557 HOH   A O   1 
HETATM 1813 O O   . HOH   C 3 .   ? 4.31924   -19.36789 -40.71548 1.000 31.27779  ? 558 HOH   A O   1 
HETATM 1814 O O   . HOH   C 3 .   ? -11.85095 -7.62277  -38.26191 1.000 38.69728  ? 559 HOH   A O   1 
HETATM 1815 O O   . HOH   C 3 .   ? -7.80615  -28.35277 -8.01741  1.000 29.22322  ? 560 HOH   A O   1 
HETATM 1816 O O   . HOH   C 3 .   ? 15.70965  -18.20942 -3.54179  1.000 31.20010  ? 561 HOH   A O   1 
HETATM 1817 O O   . HOH   C 3 .   ? -10.29654 -15.16029 -28.33710 1.000 31.01348  ? 562 HOH   A O   1 
HETATM 1818 O O   . HOH   C 3 .   ? -14.37720 -11.67110 0.36620   1.000 37.90238  ? 563 HOH   A O   1 
HETATM 1819 O O   . HOH   C 3 .   ? 18.62229  -16.11905 -13.44933 1.000 38.06406  ? 564 HOH   A O   1 
HETATM 1820 O O   . HOH   C 3 .   ? -0.28242  -7.00197  -31.05564 1.000 32.17725  ? 565 HOH   A O   1 
HETATM 1821 O O   . HOH   C 3 .   ? 4.43923   -5.08813  -21.78682 1.000 42.49129  ? 566 HOH   A O   1 
HETATM 1822 O O   . HOH   C 3 .   ? 5.00626   -30.32525 -11.47066 1.000 36.26847  ? 567 HOH   A O   1 
HETATM 1823 O O   . HOH   C 3 .   ? -3.38037  -12.98267 -20.86655 1.000 24.27260  ? 568 HOH   A O   1 
HETATM 1824 O O   . HOH   C 3 .   ? -15.10135 -12.03135 -11.92284 1.000 34.31787  ? 569 HOH   A O   1 
HETATM 1825 O O   . HOH   C 3 .   ? -2.39669  -15.50625 -0.20277  1.000 36.99902  ? 570 HOH   A O   1 
HETATM 1826 O O   . HOH   C 3 .   ? -5.81175  -18.98460 -39.19372 1.000 38.24469  ? 571 HOH   A O   1 
HETATM 1827 O O   . HOH   C 3 .   ? -16.52910 -9.07941  -14.23098 1.000 32.61186  ? 572 HOH   A O   1 
HETATM 1828 O O   . HOH   C 3 .   ? -17.74859 -15.08277 -13.07427 1.000 23.20374  ? 573 HOH   A O   1 
HETATM 1829 O O   . HOH   C 3 .   ? 20.77862  -13.94547 -26.69801 1.000 31.76624  ? 574 HOH   A O   1 
HETATM 1830 O O   . HOH   C 3 .   ? 17.16713  -24.60396 -25.27931 1.000 39.38654  ? 575 HOH   A O   1 
HETATM 1831 O O   . HOH   C 3 .   ? 15.44350  -7.20252  -27.78427 1.000 27.54099  ? 576 HOH   A O   1 
HETATM 1832 O O   . HOH   C 3 .   ? 6.81530   -29.52182 -29.56395 1.000 44.17787  ? 577 HOH   A O   1 
HETATM 1833 O O   . HOH   C 3 .   ? -12.21237 -26.89918 -20.29684 1.000 25.53138  ? 578 HOH   A O   1 
HETATM 1834 O O   . HOH   C 3 .   ? 3.11526   -30.07185 -19.04118 1.000 36.24175  ? 579 HOH   A O   1 
HETATM 1835 O O   . HOH   C 3 .   ? 1.98089   -6.02334  -25.99558 1.000 31.20687  ? 580 HOH   A O   1 
HETATM 1836 O O   . HOH   C 3 .   ? -14.21689 -16.07699 -26.06408 1.000 25.12095  ? 581 HOH   A O   1 
HETATM 1837 O O   . HOH   C 3 .   ? -18.29453 -3.26549  -35.62440 1.000 51.82806  ? 582 HOH   A O   1 
HETATM 1838 O O   . HOH   C 3 .   ? -7.57453  7.46281   -33.76063 1.000 38.17568  ? 583 HOH   A O   1 
HETATM 1839 O O   . HOH   C 3 .   ? 0.09086   -16.68634 -3.43072  1.000 24.25851  ? 584 HOH   A O   1 
HETATM 1840 O O   . HOH   C 3 .   ? 8.18030   -29.94068 -37.26005 1.000 50.94258  ? 585 HOH   A O   1 
HETATM 1841 O O   . HOH   C 3 .   ? 13.78199  -3.98584  -25.45359 1.000 17.78789  ? 586 HOH   A O   1 
HETATM 1842 O O   . HOH   C 3 .   ? -13.53082 -25.80482 -7.79075  1.000 27.73812  ? 587 HOH   A O   1 
HETATM 1843 O O   . HOH   C 3 .   ? -7.198    1.322     -19.232   1.000 34.94094  ? 588 HOH   A O   1 
HETATM 1844 O O   . HOH   C 3 .   ? 11.02991  -11.52670 -4.72761  1.000 35.70625  ? 589 HOH   A O   1 
HETATM 1845 O O   . HOH   C 3 .   ? 10.50137  -17.68034 -39.07215 1.000 46.68989  ? 590 HOH   A O   1 
HETATM 1846 O O   . HOH   C 3 .   ? 13.27536  -6.83125  -26.34442 1.000 23.75270  ? 591 HOH   A O   1 
HETATM 1847 O O   . HOH   C 3 .   ? -8.17504  -13.64789 -41.00720 1.000 49.46132  ? 592 HOH   A O   1 
HETATM 1848 O O   . HOH   C 3 .   ? -13.19986 -12.14594 -30.95280 1.000 23.71299  ? 593 HOH   A O   1 
HETATM 1849 O O   . HOH   C 3 .   ? 17.80573  -15.46698 -29.44549 1.000 42.38234  ? 594 HOH   A O   1 
HETATM 1850 O O   . HOH   C 3 .   ? -13.71907 -18.57990 -24.40748 1.000 21.28202  ? 595 HOH   A O   1 
HETATM 1851 O O   . HOH   C 3 .   ? -4.96099  -5.21481  -12.08120 1.000 35.44236  ? 596 HOH   A O   1 
HETATM 1852 O O   . HOH   C 3 .   ? -15.999   -3.971    -15.313   1.000 49.71745  ? 597 HOH   A O   1 
HETATM 1853 O O   . HOH   C 3 .   ? 0.98351   -8.71060  -3.91822  1.000 40.10054  ? 598 HOH   A O   1 
HETATM 1854 O O   . HOH   C 3 .   ? 18.70226  -19.35815 -11.94343 1.000 50.36684  ? 599 HOH   A O   1 
HETATM 1855 O O   . HOH   C 3 .   ? 1.13719   -8.47144  -27.28870 1.000 31.79308  ? 600 HOH   A O   1 
HETATM 1856 O O   . HOH   C 3 .   ? -2.09967  -27.05054 -24.69106 1.000 40.21239  ? 601 HOH   A O   1 
HETATM 1857 O O   . HOH   C 3 .   ? 5.30975   -10.08005 -2.23566  1.000 45.90062  ? 602 HOH   A O   1 
HETATM 1858 O O   . HOH   C 3 .   ? 3.20381   -4.24673  -8.93401  1.000 46.87869  ? 603 HOH   A O   1 
HETATM 1859 O O   . HOH   C 3 .   ? -18.20365 -5.67946  -25.45497 1.000 35.47968  ? 604 HOH   A O   1 
HETATM 1860 O O   . HOH   C 3 .   ? 4.15789   -22.79003 -3.42370  1.000 37.76469  ? 605 HOH   A O   1 
HETATM 1861 O O   . HOH   C 3 .   ? -4.46417  -3.28946  -15.64535 1.000 41.08999  ? 606 HOH   A O   1 
HETATM 1862 O O   . HOH   C 3 .   ? 4.28356   -21.58769 -39.21457 1.000 47.62353  ? 607 HOH   A O   1 
HETATM 1863 O O   . HOH   C 3 .   ? -5.36734  -31.76785 -6.95596  1.000 42.49902  ? 608 HOH   A O   1 
HETATM 1864 O O   . HOH   C 3 .   ? -17.251   -28.719   -17.205   1.000 39.40027  ? 609 HOH   A O   1 
HETATM 1865 O O   . HOH   C 3 .   ? -18.618   -10.897   -15.058   1.000 52.85796  ? 610 HOH   A O   1 
HETATM 1866 O O   . HOH   C 3 .   ? 1.991     -18.689   0.104     1.000 34.23540  ? 611 HOH   A O   1 
HETATM 1867 O O   . HOH   C 3 .   ? 1.12771   -9.26596  -40.44367 1.000 42.61623  ? 612 HOH   A O   1 
HETATM 1868 O O   . HOH   C 3 .   ? 14.47427  -22.45733 -17.22245 1.000 31.68633  ? 613 HOH   A O   1 
HETATM 1869 O O   . HOH   C 3 .   ? 16.194    -27.675   -22.954   1.000 45.84063  ? 614 HOH   A O   1 
HETATM 1870 O O   . HOH   C 3 .   ? -6.971    -23.305   -1.531    1.000 41.80053  ? 615 HOH   A O   1 
HETATM 1871 O O   . HOH   C 3 .   ? 2.04140   -25.60939 -29.41089 1.000 39.80333  ? 616 HOH   A O   1 
HETATM 1872 O O   . HOH   C 3 .   ? 20.35979  -5.92801  -21.11557 1.000 37.15057  ? 617 HOH   A O   1 
HETATM 1873 O O   . HOH   C 3 .   ? -11.25534 -5.66622  -41.14373 1.000 65.00657  ? 618 HOH   A O   1 
HETATM 1874 O O   . HOH   C 3 .   ? 5.410     -3.097    -25.943   1.000 41.06279  ? 619 HOH   A O   1 
HETATM 1875 O O   . HOH   C 3 .   ? 8.26280   -25.77633 -25.78048 1.000 38.37334  ? 620 HOH   A O   1 
HETATM 1876 O O   . HOH   C 3 .   ? -13.82394 -29.22938 -16.98176 1.000 43.97655  ? 621 HOH   A O   1 
HETATM 1877 O O   . HOH   C 3 .   ? 7.01562   2.04984   -12.42814 1.000 34.35956  ? 622 HOH   A O   1 
HETATM 1878 O O   . HOH   C 3 .   ? -18.49387 -15.95552 -21.40741 1.000 42.52089  ? 623 HOH   A O   1 
HETATM 1879 O O   . HOH   C 3 .   ? -10.94354 -7.14046  -39.85122 1.000 59.66856  ? 624 HOH   A O   1 
HETATM 1880 O O   . HOH   C 3 .   ? 11.44707  -1.38976  -20.21279 1.000 37.73709  ? 625 HOH   A O   1 
HETATM 1881 O O   . HOH   C 3 .   ? -15.197   -23.044   -30.276   1.000 29.58402  ? 626 HOH   A O   1 
HETATM 1882 O O   . HOH   C 3 .   ? -17.167   -4.727    -17.265   1.000 33.62016  ? 627 HOH   A O   1 
HETATM 1883 O O   . HOH   C 3 .   ? 4.73619   -1.78006  -18.18557 1.000 39.13571  ? 628 HOH   A O   1 
HETATM 1884 O O   . HOH   C 3 .   ? -2.62949  -0.71791  -31.37295 1.000 41.95185  ? 629 HOH   A O   1 
HETATM 1885 O O   . HOH   C 3 .   ? 4.33228   -30.99617 -20.59185 1.000 44.61879  ? 630 HOH   A O   1 
HETATM 1886 O O   . HOH   C 3 .   ? -0.19678  -19.24148 -1.80032  1.000 42.44973  ? 631 HOH   A O   1 
HETATM 1887 O O   . HOH   C 3 .   ? -18.17406 -14.67580 -22.71434 1.000 28.56892  ? 632 HOH   A O   1 
HETATM 1888 O O   . HOH   C 3 .   ? -1.28382  -5.60523  -12.48023 1.000 45.18348  ? 633 HOH   A O   1 
HETATM 1889 O O   . HOH   C 3 .   ? -9.44674  -5.70231  -39.62292 1.000 42.97836  ? 634 HOH   A O   1 
HETATM 1890 O O   . HOH   C 3 .   ? -13.85809 -0.65786  -13.55827 1.000 34.45694  ? 635 HOH   A O   1 
HETATM 1891 O O   . HOH   C 3 .   ? -13.90859 -14.21708 -3.00347  1.000 34.31164  ? 636 HOH   A O   1 
HETATM 1892 O O   . HOH   C 3 .   ? 12.21291  -25.24537 -38.28465 1.000 32.90968  ? 637 HOH   A O   1 
HETATM 1893 O O   . HOH   C 3 .   ? 5.609     1.503     -16.752   1.000 44.92116  ? 638 HOH   A O   1 
HETATM 1894 O O   . HOH   C 3 .   ? -12.45347 -16.35010 -28.17158 1.000 31.59960  ? 639 HOH   A O   1 
HETATM 1895 O O   . HOH   C 3 .   ? 3.53816   -7.95893  -2.05909  1.000 46.31275  ? 640 HOH   A O   1 
HETATM 1896 O O   . HOH   C 3 .   ? 18.17017  -3.47687  -22.95293 1.000 42.84113  ? 641 HOH   A O   1 
HETATM 1897 O O   . HOH   C 3 .   ? -0.37342  -1.21863  -22.99077 1.000 40.66928  ? 642 HOH   A O   1 
HETATM 1898 O O   . HOH   C 3 .   ? 1.87621   -24.79914 -2.24288  1.000 49.55440  ? 643 HOH   A O   1 
HETATM 1899 O O   . HOH   C 3 .   ? 19.09131  -8.33174  -17.78148 1.000 39.17362  ? 644 HOH   A O   1 
HETATM 1900 O O   . HOH   C 3 .   ? 6.15803   -29.80467 -24.98302 1.000 47.09840  ? 645 HOH   A O   1 
HETATM 1901 O O   . HOH   C 3 .   ? -19.398   -13.088   -13.889   1.000 45.12161  ? 646 HOH   A O   1 
HETATM 1902 O O   . HOH   C 3 .   ? 10.87628  -10.07206 -36.36994 1.000 49.36811  ? 647 HOH   A O   1 
HETATM 1903 O O   . HOH   C 3 .   ? 7.68043   -13.81249 -38.28923 1.000 30.24736  ? 648 HOH   A O   1 
HETATM 1904 O O   . HOH   C 3 .   ? -14.39312 -9.89926  -8.36518  1.000 35.47718  ? 649 HOH   A O   1 
HETATM 1905 O O   . HOH   C 3 .   ? -11.74935 -9.32426  -39.59621 1.000 48.02692  ? 650 HOH   A O   1 
HETATM 1906 O O   . HOH   C 3 .   ? -6.24920  3.77027   -34.65261 1.000 40.05407  ? 651 HOH   A O   1 
HETATM 1907 O O   . HOH   C 3 .   ? 1.66476   -2.56940  -13.08095 1.000 50.99624  ? 652 HOH   A O   1 
HETATM 1908 O O   . HOH   C 3 .   ? -3.96074  -33.22377 -11.20634 1.000 42.43963  ? 653 HOH   A O   1 
HETATM 1909 O O   . HOH   C 3 .   ? 3.37810   -9.17892  -39.19803 1.000 39.17285  ? 654 HOH   A O   1 
HETATM 1910 O O   . HOH   C 3 .   ? -18.70529 -11.72519 -21.04318 1.000 26.08910  ? 655 HOH   A O   1 
HETATM 1911 O O   . HOH   C 3 .   ? -3.26811  -27.15064 -3.23415  1.000 38.30213  ? 656 HOH   A O   1 
HETATM 1912 O O   . HOH   C 3 .   ? -11.90423 -33.28612 -9.88955  1.000 54.32313  ? 657 HOH   A O   1 
HETATM 1913 O O   . HOH   C 3 .   ? 3.79437   -0.26641  -16.61547 1.000 45.56657  ? 658 HOH   A O   1 
HETATM 1914 O O   . HOH   C 3 .   ? 2.19436   -0.81905  -26.02964 1.000 41.14583  ? 659 HOH   A O   1 
HETATM 1915 O O   . HOH   C 3 .   ? -9.85224  -25.94721 -20.75512 1.000 28.06577  ? 660 HOH   A O   1 
HETATM 1916 O O   . HOH   C 3 .   ? 11.80876  -27.73641 -23.49395 1.000 41.56042  ? 661 HOH   A O   1 
HETATM 1917 O O   . HOH   C 3 .   ? 14.89121  -7.82627  -30.24890 1.000 44.41848  ? 662 HOH   A O   1 
HETATM 1918 O O   . HOH   C 3 .   ? 5.633     -3.401    -23.449   1.000 47.63004  ? 663 HOH   A O   1 
HETATM 1919 O O   . HOH   C 3 .   ? -4.07875  -29.69983 -22.17440 1.000 49.45851  ? 664 HOH   A O   1 
HETATM 1920 O O   . HOH   C 3 .   ? 11.116    -1.144    -17.412   1.000 36.77696  ? 665 HOH   A O   1 
HETATM 1921 O O   . HOH   C 3 .   ? -8.03133  -21.21531 -37.61257 1.000 45.95637  ? 666 HOH   A O   1 
HETATM 1922 O O   . HOH   C 3 .   ? 6.64192   -21.37191 -2.60983  1.000 33.46792  ? 667 HOH   A O   1 
HETATM 1923 O O   . HOH   C 3 .   ? 10.52061  -22.32724 -4.46178  1.000 45.01051  ? 668 HOH   A O   1 
HETATM 1924 O O   . HOH   C 3 .   ? 5.69239   -12.99028 -39.90918 1.000 31.56215  ? 669 HOH   A O   1 
HETATM 1925 O O   . HOH   C 3 .   ? 7.78243   -28.87203 -28.18181 1.000 43.88081  ? 670 HOH   A O   1 
HETATM 1926 O O   . HOH   C 3 .   ? -16.990   -0.553    -17.583   1.000 42.35570  ? 671 HOH   A O   1 
HETATM 1927 O O   . HOH   C 3 .   ? -5.010    -25.207   -1.442    1.000 52.72534  ? 672 HOH   A O   1 
HETATM 1928 O O   . HOH   C 3 .   ? -11.93567 -7.26852  -41.96206 1.000 51.73230  ? 673 HOH   A O   1 
HETATM 1929 O O   . HOH   C 3 .   ? -1.38901  -2.57061  -31.69969 1.000 40.59287  ? 674 HOH   A O   1 
HETATM 1930 O O   . HOH   C 3 .   ? -15.943   -1.574    -15.500   1.000 50.40946  ? 675 HOH   A O   1 
HETATM 1931 O O   . HOH   C 3 .   ? -0.00000  -0.00000  -18.88862 0.50  47.99684  ? 676 HOH   A O   1 
HETATM 1932 O O   . HOH   C 3 .   ? -16.227   3.064     -26.411   1.000 45.79555  ? 677 HOH   A O   1 
HETATM 1933 O O   . HOH   C 3 .   ? -6.99423  -30.66182 -9.09281  1.000 35.89493  ? 678 HOH   A O   1 
HETATM 1934 O O   . HOH   C 3 .   ? 4.27158   -14.59975 -41.63990 1.000 45.39729  ? 679 HOH   A O   1 
HETATM 1935 O O   . HOH   C 3 .   ? 11.20365  -29.46813 -19.15072 1.000 53.33097  ? 680 HOH   A O   1 
HETATM 1936 O O   . HOH   C 3 .   ? 11.49995  -29.92130 -34.40402 1.000 38.71608  ? 681 HOH   A O   1 
HETATM 1937 O O   . HOH   C 3 .   ? 15.965    0.758     -9.711    1.000 48.86089  ? 682 HOH   A O   1 
HETATM 1938 O O   . HOH   C 3 .   ? 10.91236  -28.05513 -27.74431 1.000 33.92292  ? 683 HOH   A O   1 
HETATM 1939 O O   . HOH   C 3 .   ? -16.17996 -12.59904 -6.20882  1.000 42.60705  ? 684 HOH   A O   1 
HETATM 1940 O O   . HOH   C 3 .   ? -11.72391 -26.16439 -28.02935 1.000 42.19291  ? 685 HOH   A O   1 
HETATM 1941 O O   . HOH   C 3 .   ? -1.982    -23.051   0.956     1.000 49.68052  ? 686 HOH   A O   1 
HETATM 1942 O O   . HOH   C 3 .   ? -13.71533 -13.69870 -38.32654 1.000 47.72937  ? 687 HOH   A O   1 
HETATM 1943 O O   . HOH   C 3 .   ? -9.90703  -29.08885 -30.57666 1.000 42.78242  ? 688 HOH   A O   1 
HETATM 1944 O O   . HOH   C 3 .   ? 0.337     -1.548    -16.843   1.000 45.79722  ? 689 HOH   A O   1 
HETATM 1945 O O   . HOH   C 3 .   ? -6.43041  -16.97387 -41.22376 1.000 46.41825  ? 690 HOH   A O   1 
HETATM 1946 O O   . HOH   C 3 .   ? 16.92793  -27.76655 -19.62874 1.000 56.74458  ? 691 HOH   A O   1 
HETATM 1947 O O   . HOH   C 3 .   ? 21.785    -17.813   -25.027   1.000 40.99599  ? 692 HOH   A O   1 
HETATM 1948 O O   . HOH   C 3 .   ? 3.018     -2.255    -20.732   1.000 48.22608  ? 693 HOH   A O   1 
HETATM 1949 O O   . HOH   C 3 .   ? 1.94993   -5.78548  -36.76732 1.000 44.27595  ? 694 HOH   A O   1 
HETATM 1950 O O   . HOH   C 3 .   ? -0.47818  -26.84322 -30.12209 1.000 44.40056  ? 695 HOH   A O   1 
HETATM 1951 O O   . HOH   C 3 .   ? 4.002     -1.919    -28.234   1.000 42.91286  ? 696 HOH   A O   1 
HETATM 1952 O O   . HOH   C 3 .   ? -4.46596  -27.98262 -23.35468 1.000 43.67705  ? 697 HOH   A O   1 
HETATM 1953 O O   . HOH   C 3 .   ? 13.69653  -11.52546 -5.15955  1.000 33.39543  ? 698 HOH   A O   1 
HETATM 1954 O O   . HOH   C 3 .   ? 14.74787  -13.38372 -2.85393  1.000 44.72247  ? 699 HOH   A O   1 
HETATM 1955 O O   . HOH   C 3 .   ? -16.09104 -13.38703 -3.83898  1.000 44.50268  ? 700 HOH   A O   1 
HETATM 1956 O O   . HOH   C 3 .   ? -18.020   1.419     -21.778   1.000 50.25052  ? 701 HOH   A O   1 
HETATM 1957 O O   . HOH   C 3 .   ? 9.53834   -25.21737 -14.53312 1.000 41.90905  ? 702 HOH   A O   1 
HETATM 1958 O O   . HOH   C 3 .   ? -6.79439  -26.73758 -23.35653 1.000 46.51602  ? 703 HOH   A O   1 
HETATM 1959 O O   . HOH   C 3 .   ? -10.348   -11.861   2.046     1.000 34.43450  ? 704 HOH   A O   1 
HETATM 1960 O O   . HOH   C 3 .   ? 14.08737  -28.25176 -19.31836 1.000 54.22691  ? 705 HOH   A O   1 
HETATM 1961 O O   . HOH   C 3 .   ? -23.056   -31.871   -12.750   1.000 45.03335  ? 706 HOH   A O   1 
HETATM 1962 O O   . HOH   C 3 .   ? -14.53346 -14.12541 -10.19534 1.000 31.34759  ? 707 HOH   A O   1 
HETATM 1963 O O   . HOH   C 3 .   ? 19.312    -20.608   -22.220   1.000 33.48028  ? 708 HOH   A O   1 
HETATM 1964 O O   . HOH   C 3 .   ? -2.62108  -26.54005 -27.37345 1.000 51.97611  ? 709 HOH   A O   1 
HETATM 1965 O O   . HOH   C 3 .   ? -14.69658 -9.41315  -11.33759 1.000 34.91942  ? 710 HOH   A O   1 
HETATM 1966 O O   . HOH   C 3 .   ? -12.39902 -13.10826 -0.95902  1.000 28.58032  ? 711 HOH   A O   1 
HETATM 1967 O O   . HOH   C 3 .   ? -16.88711 -15.52819 -10.17255 1.000 36.84150  ? 712 HOH   A O   1 
HETATM 1968 O O   . HOH   C 3 .   ? -19.19956 -8.29992  -14.97110 1.000 52.98192  ? 713 HOH   A O   1 
HETATM 1969 O O   . HOH   C 3 .   ? 17.06620  -14.25049 -3.98807  1.000 54.31001  ? 714 HOH   A O   1 
HETATM 1970 O O   . HOH   C 3 .   ? -9.423    0.788     -3.633    1.000 49.56785  ? 715 HOH   A O   1 
HETATM 1971 O O   . HOH   C 3 .   ? -9.35853  -32.77893 -8.81407  1.000 44.29208  ? 716 HOH   A O   1 
HETATM 1972 O O   . HOH   C 3 .   ? 5.99904   -8.50269  -40.32911 1.000 52.00676  ? 717 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   ? 0.43234 0.67177 0.39237 -0.09521 -0.01341 -0.26740 16  GLU A N   
2    C CA  . GLU A 9   ? 0.56600 0.77074 0.51322 -0.06062 -0.02064 -0.24660 16  GLU A CA  
3    C C   . GLU A 9   ? 0.55700 0.75301 0.51768 -0.04422 -0.02546 -0.22430 16  GLU A C   
4    O O   . GLU A 9   ? 0.47375 0.72864 0.45380 -0.02691 -0.03483 -0.21574 16  GLU A O   
5    C CB  . GLU A 9   ? 0.72187 0.98591 0.67031 -0.03134 -0.03233 -0.24524 16  GLU A CB  
6    C CG  . GLU A 9   ? 0.89358 1.11196 0.81898 -0.00489 -0.03267 -0.23302 16  GLU A CG  
7    C CD  . GLU A 9   ? 1.01534 1.22377 0.94656 0.02910  -0.03814 -0.20569 16  GLU A CD  
8    O OE1 . GLU A 9   ? 0.86111 1.09828 0.81167 0.03383  -0.04301 -0.19634 16  GLU A OE1 
9    O OE2 . GLU A 9   ? 1.10984 1.28082 1.02558 0.05143  -0.03569 -0.19335 16  GLU A OE2 
10   N N   . VAL A 10  ? 0.45480 0.57660 0.40337 -0.04706 -0.01709 -0.21467 17  VAL A N   
11   C CA  . VAL A 10  ? 0.34107 0.44897 0.30196 -0.03837 -0.01937 -0.19733 17  VAL A CA  
12   C C   . VAL A 10  ? 0.33585 0.41419 0.28916 -0.00582 -0.02250 -0.18023 17  VAL A C   
13   O O   . VAL A 10  ? 0.41558 0.44289 0.34984 -0.00045 -0.01355 -0.17962 17  VAL A O   
14   C CB  . VAL A 10  ? 0.38021 0.43206 0.33629 -0.06508 -0.00470 -0.19858 17  VAL A CB  
15   C CG1 . VAL A 10  ? 0.43791 0.47542 0.40595 -0.05460 -0.00730 -0.18077 17  VAL A CG1 
16   C CG2 . VAL A 10  ? 0.55665 0.63955 0.52157 -0.09713 0.00172  -0.21596 17  VAL A CG2 
17   N N   . GLU A 11  ? 0.27246 0.38080 0.23921 0.01799  -0.03265 -0.16519 18  GLU A N   
18   C CA  . GLU A 11  ? 0.25188 0.33054 0.21878 0.04668  -0.03145 -0.13700 18  GLU A CA  
19   C C   . GLU A 11  ? 0.23807 0.28376 0.21738 0.04219  -0.02761 -0.11881 18  GLU A C   
20   O O   . GLU A 11  ? 0.21846 0.28473 0.21056 0.03220  -0.03101 -0.11945 18  GLU A O   
21   C CB  . GLU A 11  ? 0.28714 0.40951 0.25646 0.07622  -0.03856 -0.12501 18  GLU A CB  
22   C CG  . GLU A 11  ? 0.27490 0.43117 0.22813 0.09009  -0.04206 -0.13758 18  GLU A CG  
23   C CD  . GLU A 11  ? 0.39668 0.59305 0.34716 0.12436  -0.04510 -0.12160 18  GLU A CD  
24   O OE1 . GLU A 11  ? 0.35591 0.59814 0.31721 0.12758  -0.04959 -0.12102 18  GLU A OE1 
25   O OE2 . GLU A 11  ? 0.42424 0.60186 0.36423 0.14733  -0.04006 -0.10485 18  GLU A OE2 
26   N N   . THR A 12  ? 0.23686 0.23793 0.21176 0.05095  -0.02056 -0.10322 19  THR A N   
27   C CA  . THR A 12  ? 0.22462 0.20211 0.20903 0.04922  -0.01738 -0.08674 19  THR A CA  
28   C C   . THR A 12  ? 0.24561 0.22971 0.23984 0.06929  -0.01906 -0.06649 19  THR A C   
29   O O   . THR A 12  ? 0.23330 0.21186 0.22151 0.08452  -0.01616 -0.06070 19  THR A O   
30   C CB  . THR A 12  ? 0.25647 0.18394 0.22568 0.04416  -0.00535 -0.08523 19  THR A CB  
31   O OG1 . THR A 12  ? 0.31027 0.22193 0.26553 0.02057  0.00201  -0.10740 19  THR A OG1 
32   C CG2 . THR A 12  ? 0.26529 0.17932 0.24242 0.04530  -0.00298 -0.06837 19  THR A CG2 
33   N N   . PHE A 13  ? 0.19323 0.18817 0.20125 0.06679  -0.02157 -0.05761 20  PHE A N   
34   C CA  . PHE A 13  ? 0.18154 0.18224 0.19798 0.07798  -0.01971 -0.04324 20  PHE A CA  
35   C C   . PHE A 13  ? 0.25903 0.25202 0.28524 0.07089  -0.01845 -0.03434 20  PHE A C   
36   O O   . PHE A 13  ? 0.22956 0.21794 0.25723 0.05960  -0.02028 -0.03695 20  PHE A O   
37   C CB  . PHE A 13  ? 0.20761 0.22923 0.22617 0.08307  -0.02050 -0.04243 20  PHE A CB  
38   C CG  . PHE A 13  ? 0.22369 0.26649 0.23112 0.09616  -0.02235 -0.04932 20  PHE A CG  
39   C CD1 . PHE A 13  ? 0.22705 0.29535 0.23258 0.08797  -0.02946 -0.06526 20  PHE A CD1 
40   C CD2 . PHE A 13  ? 0.22848 0.26802 0.22422 0.10768  -0.01515 -0.03776 20  PHE A CD2 
41   C CE1 . PHE A 13  ? 0.24325 0.34562 0.23850 0.10152  -0.03273 -0.07348 20  PHE A CE1 
42   C CE2 . PHE A 13  ? 0.24337 0.30507 0.22387 0.12062  -0.01712 -0.04120 20  PHE A CE2 
43   C CZ  . PHE A 13  ? 0.27264 0.37343 0.25474 0.12433  -0.02736 -0.06102 20  PHE A CZ  
44   N N   . ALA A 14  ? 0.21492 0.21171 0.24754 0.07681  -0.01439 -0.02483 21  ALA A N   
45   C CA  . ALA A 14  ? 0.20297 0.20814 0.24626 0.06983  -0.01415 -0.01887 21  ALA A CA  
46   C C   . ALA A 14  ? 0.21323 0.22580 0.26273 0.06063  -0.01243 -0.02025 21  ALA A C   
47   O O   . ALA A 14  ? 0.19035 0.19986 0.23632 0.06486  -0.00565 -0.01986 21  ALA A O   
48   C CB  . ALA A 14  ? 0.24237 0.25986 0.29128 0.07705  -0.00970 -0.01178 21  ALA A CB  
49   N N   . PHE A 15  ? 0.19146 0.20890 0.24571 0.05029  -0.01579 -0.02102 22  PHE A N   
50   C CA  . PHE A 15  ? 0.17415 0.19514 0.23166 0.04097  -0.01145 -0.02286 22  PHE A CA  
51   C C   . PHE A 15  ? 0.19114 0.22056 0.25449 0.03530  -0.00274 -0.02250 22  PHE A C   
52   O O   . PHE A 15  ? 0.19964 0.24769 0.27059 0.03617  -0.00455 -0.02025 22  PHE A O   
53   C CB  . PHE A 15  ? 0.17018 0.19834 0.23115 0.03092  -0.01647 -0.02407 22  PHE A CB  
54   C CG  . PHE A 15  ? 0.19159 0.21319 0.24812 0.03025  -0.02092 -0.02665 22  PHE A CG  
55   C CD1 . PHE A 15  ? 0.19884 0.21979 0.25151 0.03220  -0.01849 -0.02982 22  PHE A CD1 
56   C CD2 . PHE A 15  ? 0.17817 0.19531 0.23238 0.02844  -0.02465 -0.02558 22  PHE A CD2 
57   C CE1 . PHE A 15  ? 0.17896 0.20691 0.23097 0.02981  -0.02264 -0.03407 22  PHE A CE1 
58   C CE2 . PHE A 15  ? 0.16430 0.17777 0.21579 0.02209  -0.02582 -0.03065 22  PHE A CE2 
59   C CZ  . PHE A 15  ? 0.19218 0.21718 0.24537 0.02137  -0.02629 -0.03600 22  PHE A CZ  
60   N N   . GLN A 16  ? 0.20639 0.22244 0.26422 0.02955  0.00950  -0.02513 23  GLN A N   
61   C CA  . GLN A 16  ? 0.25602 0.27922 0.31924 0.01343  0.02148  -0.03006 23  GLN A CA  
62   C C   . GLN A 16  ? 0.18787 0.24337 0.26330 -0.00107 0.01304  -0.03568 23  GLN A C   
63   O O   . GLN A 16  ? 0.21118 0.26760 0.28481 -0.00114 0.00431  -0.03572 23  GLN A O   
64   C CB  . GLN A 16  ? 0.26675 0.25691 0.31460 0.00716  0.04124  -0.03319 23  GLN A CB  
65   C CG  . GLN A 16  ? 0.40685 0.36825 0.43789 0.02664  0.05338  -0.02511 23  GLN A CG  
66   C CD  . GLN A 16  ? 0.48549 0.40595 0.49289 0.02830  0.07659  -0.02428 23  GLN A CD  
67   O OE1 . GLN A 16  ? 0.51963 0.42959 0.51389 0.04447  0.07514  -0.01973 23  GLN A OE1 
68   N NE2 . GLN A 16  ? 0.48323 0.37987 0.48292 0.01169  0.10106  -0.02901 23  GLN A NE2 
69   N N   . ALA A 17  ? 0.18367 0.27238 0.27141 -0.01204 0.01591  -0.04039 24  ALA A N   
70   C CA  . ALA A 17  ? 0.20496 0.33997 0.30384 -0.02083 0.00651  -0.04530 24  ALA A CA  
71   C C   . ALA A 17  ? 0.17520 0.30425 0.26852 -0.03703 0.00778  -0.05461 24  ALA A C   
72   O O   . ALA A 17  ? 0.22348 0.37265 0.31743 -0.03282 -0.00419 -0.05259 24  ALA A O   
73   C CB  . ALA A 17  ? 0.19920 0.38180 0.31324 -0.03486 0.01257  -0.05358 24  ALA A CB  
74   N N   . GLU A 18  ? 0.22811 0.32409 0.31160 -0.05323 0.02502  -0.06369 25  GLU A N   
75   C CA  . GLU A 18  ? 0.24953 0.33547 0.32404 -0.06904 0.02967  -0.07406 25  GLU A CA  
76   C C   . GLU A 18  ? 0.25486 0.32154 0.32108 -0.05125 0.01856  -0.06407 25  GLU A C   
77   O O   . GLU A 18  ? 0.24574 0.32453 0.31002 -0.05775 0.01300  -0.06867 25  GLU A O   
78   C CB  . GLU A 18  ? 0.37937 0.41910 0.43710 -0.08616 0.05667  -0.08395 25  GLU A CB  
79   C CG  . GLU A 18  ? 0.33147 0.38917 0.39659 -0.11423 0.07326  -0.09926 25  GLU A CG  
80   C CD  . GLU A 18  ? 0.47467 0.52677 0.54470 -0.10289 0.07928  -0.08961 25  GLU A CD  
81   O OE1 . GLU A 18  ? 0.36252 0.39844 0.42942 -0.07272 0.06903  -0.07203 25  GLU A OE1 
82   O OE2 . GLU A 18  ? 0.50109 0.56787 0.57796 -0.12627 0.09531  -0.10144 25  GLU A OE2 
83   N N   . ILE A 19  ? 0.23084 0.27276 0.29226 -0.03020 0.01575  -0.05198 26  ILE A N   
84   C CA  . ILE A 19  ? 0.19566 0.22752 0.25191 -0.01740 0.00660  -0.04539 26  ILE A CA  
85   C C   . ILE A 19  ? 0.18620 0.24427 0.25127 -0.01184 -0.00942 -0.03997 26  ILE A C   
86   O O   . ILE A 19  ? 0.21768 0.27788 0.28000 -0.01186 -0.01484 -0.03875 26  ILE A O   
87   C CB  . ILE A 19  ? 0.22341 0.23153 0.27142 0.00085  0.00953  -0.03812 26  ILE A CB  
88   C CG1 . ILE A 19  ? 0.24390 0.21983 0.27358 0.00434  0.02808  -0.03899 26  ILE A CG1 
89   C CG2 . ILE A 19  ? 0.20273 0.21773 0.25237 0.01030  -0.00288 -0.03403 26  ILE A CG2 
90   C CD1 . ILE A 19  ? 0.38250 0.33706 0.40414 -0.00801 0.04864  -0.04443 26  ILE A CD1 
91   N N   . ALA A 20  ? 0.16436 0.23955 0.23670 -0.00501 -0.01417 -0.03541 27  ALA A N   
92   C CA  . ALA A 20  ? 0.18553 0.27921 0.25887 0.00463  -0.02374 -0.02794 27  ALA A CA  
93   C C   . ALA A 20  ? 0.20997 0.33596 0.28476 -0.00368 -0.02703 -0.03198 27  ALA A C   
94   O O   . ALA A 20  ? 0.20379 0.33313 0.27209 0.00396  -0.03195 -0.02540 27  ALA A O   
95   C CB  . ALA A 20  ? 0.17286 0.28041 0.25005 0.01727  -0.02484 -0.02161 27  ALA A CB  
96   N N   . GLN A 21  ? 0.18864 0.33842 0.26975 -0.02087 -0.02229 -0.04421 28  GLN A N   
97   C CA  . GLN A 21  ? 0.16239 0.35181 0.24443 -0.03200 -0.02570 -0.05276 28  GLN A CA  
98   C C   . GLN A 21  ? 0.20476 0.36974 0.27586 -0.03811 -0.02446 -0.05575 28  GLN A C   
99   O O   . GLN A 21  ? 0.20665 0.39389 0.27312 -0.03388 -0.03122 -0.05335 28  GLN A O   
100  C CB  . GLN A 21  ? 0.21402 0.43425 0.30507 -0.05641 -0.01765 -0.07079 28  GLN A CB  
101  C CG  . GLN A 21  ? 0.43982 0.69139 0.52232 -0.06703 -0.01742 -0.08003 28  GLN A CG  
102  C CD  . GLN A 21  ? 0.67955 0.95187 0.76301 -0.08898 -0.00559 -0.09637 28  GLN A CD  
103  O OE1 . GLN A 21  ? 0.65028 0.96405 0.72947 -0.09591 -0.00575 -0.10537 28  GLN A OE1 
104  N NE2 . GLN A 21  ? 0.52961 0.77577 0.61784 -0.10020 0.00645  -0.10115 28  GLN A NE2 
105  N N   . LEU A 22  ? 0.20728 0.32841 0.27173 -0.04436 -0.01453 -0.05943 29  LEU A N   
106  C CA  . LEU A 22  ? 0.23565 0.33449 0.28899 -0.04584 -0.01208 -0.06050 29  LEU A CA  
107  C C   . LEU A 22  ? 0.33362 0.43086 0.38592 -0.02999 -0.02165 -0.04718 29  LEU A C   
108  O O   . LEU A 22  ? 0.24856 0.35130 0.29467 -0.03062 -0.02389 -0.04656 29  LEU A O   
109  C CB  . LEU A 22  ? 0.25843 0.31337 0.30209 -0.04512 0.00147  -0.06187 29  LEU A CB  
110  C CG  . LEU A 22  ? 0.34010 0.37436 0.37207 -0.03964 0.00491  -0.05991 29  LEU A CG  
111  C CD1 . LEU A 22  ? 0.33806 0.37285 0.35907 -0.05580 0.01239  -0.07259 29  LEU A CD1 
112  C CD2 . LEU A 22  ? 0.33012 0.33120 0.35194 -0.02681 0.01644  -0.05541 29  LEU A CD2 
113  N N   . MET A 23  ? 0.17618 0.26344 0.23243 -0.01745 -0.02488 -0.03766 30  MET A N   
114  C CA  . MET A 23  ? 0.19024 0.26503 0.24291 -0.00770 -0.02818 -0.02814 30  MET A CA  
115  C C   . MET A 23  ? 0.20459 0.29751 0.25155 -0.00006 -0.03194 -0.01999 30  MET A C   
116  O O   . MET A 23  ? 0.21223 0.29774 0.25120 0.00167  -0.03066 -0.01506 30  MET A O   
117  C CB  . MET A 23  ? 0.21337 0.27229 0.26901 -0.00020 -0.02778 -0.02495 30  MET A CB  
118  C CG  . MET A 23  ? 0.18020 0.22357 0.23578 -0.00098 -0.02464 -0.02900 30  MET A CG  
119  S SD  . MET A 23  ? 0.19867 0.23113 0.25519 0.00683  -0.02553 -0.02832 30  MET A SD  
120  C CE  . MET A 23  ? 0.20317 0.22820 0.25628 0.00148  -0.02542 -0.02894 30  MET A CE  
121  N N   . SER A 24  ? 0.21538 0.33684 0.26477 0.00648  -0.03508 -0.01791 31  SER A N   
122  C CA  . SER A 24  ? 0.15856 0.30537 0.19829 0.02118  -0.03760 -0.00782 31  SER A CA  
123  C C   . SER A 24  ? 0.24721 0.42187 0.28334 0.01280  -0.04038 -0.01464 31  SER A C   
124  O O   . SER A 24  ? 0.25883 0.43892 0.28135 0.02526  -0.04001 -0.00452 31  SER A O   
125  C CB  . SER A 24  ? 0.30397 0.48787 0.34764 0.03437  -0.04056 -0.00380 31  SER A CB  
126  O OG  . SER A 24  ? 0.52018 0.72773 0.57993 0.01734  -0.04187 -0.01852 31  SER A OG  
127  N N   . LEU A 25  ? 0.18914 0.37726 0.23335 -0.00803 -0.04035 -0.03200 32  LEU A N   
128  C CA  . LEU A 25  ? 0.20022 0.40971 0.23790 -0.01903 -0.04117 -0.04209 32  LEU A CA  
129  C C   . LEU A 25  ? 0.30461 0.47936 0.33196 -0.01638 -0.03764 -0.03566 32  LEU A C   
130  O O   . LEU A 25  ? 0.25215 0.44310 0.26849 -0.01145 -0.03921 -0.03252 32  LEU A O   
131  C CB  . LEU A 25  ? 0.25744 0.47089 0.30029 -0.04527 -0.03539 -0.06405 32  LEU A CB  
132  C CG  . LEU A 25  ? 0.28194 0.50809 0.31384 -0.05983 -0.03126 -0.07789 32  LEU A CG  
133  C CD1 . LEU A 25  ? 0.29819 0.53507 0.33155 -0.08023 -0.02057 -0.09495 32  LEU A CD1 
134  C CD2 . LEU A 25  ? 0.27275 0.45704 0.29438 -0.06575 -0.02489 -0.08124 32  LEU A CD2 
135  N N   . ILE A 26  ? 0.22024 0.35364 0.25087 -0.01872 -0.03252 -0.03391 33  ILE A N   
136  C CA  . ILE A 26  ? 0.25927 0.36953 0.28359 -0.01757 -0.02857 -0.02916 33  ILE A CA  
137  C C   . ILE A 26  ? 0.30117 0.40669 0.31719 -0.00422 -0.02783 -0.01369 33  ILE A C   
138  O O   . ILE A 26  ? 0.28790 0.39061 0.29430 -0.00280 -0.02430 -0.00907 33  ILE A O   
139  C CB  . ILE A 26  ? 0.19385 0.27611 0.22465 -0.02040 -0.02398 -0.03148 33  ILE A CB  
140  C CG1 . ILE A 26  ? 0.24018 0.31560 0.26849 -0.02925 -0.01787 -0.04371 33  ILE A CG1 
141  C CG2 . ILE A 26  ? 0.19169 0.26212 0.22057 -0.01880 -0.02051 -0.02606 33  ILE A CG2 
142  C CD1 . ILE A 26  ? 0.28161 0.33516 0.31216 -0.02450 -0.01210 -0.04372 33  ILE A CD1 
143  N N   . ILE A 27  ? 0.23679 0.33690 0.25257 0.00682  -0.02792 -0.00481 34  ILE A N   
144  C CA  . ILE A 27  ? 0.26214 0.34087 0.26306 0.02022  -0.02024 0.01066  34  ILE A CA  
145  C C   . ILE A 27  ? 0.29800 0.40305 0.28202 0.03794  -0.02039 0.02161  34  ILE A C   
146  O O   . ILE A 27  ? 0.43514 0.52179 0.40104 0.04710  -0.01074 0.03385  34  ILE A O   
147  C CB  . ILE A 27  ? 0.33275 0.38843 0.33346 0.02770  -0.01658 0.01582  34  ILE A CB  
148  C CG1 . ILE A 27  ? 0.29789 0.32834 0.30994 0.01200  -0.01442 0.00611  34  ILE A CG1 
149  C CG2 . ILE A 27  ? 0.32247 0.35125 0.29911 0.04628  -0.00383 0.03328  34  ILE A CG2 
150  C CD1 . ILE A 27  ? 0.22059 0.23831 0.23605 0.01608  -0.01444 0.00511  34  ILE A CD1 
151  N N   . ASN A 28  ? 0.25875 0.41142 0.24721 0.04310  -0.02991 0.01688  35  ASN A N   
152  C CA  . ASN A 28  ? 0.24153 0.43415 0.21328 0.06635  -0.03147 0.02818  35  ASN A CA  
153  C C   . ASN A 28  ? 0.42232 0.65729 0.39070 0.05932  -0.03786 0.01823  35  ASN A C   
154  O O   . ASN A 28  ? 0.42772 0.69284 0.37689 0.08152  -0.03749 0.02993  35  ASN A O   
155  C CB  . ASN A 28  ? 0.31864 0.55457 0.29675 0.07969  -0.03799 0.02898  35  ASN A CB  
156  C CG  . ASN A 28  ? 0.46025 0.65442 0.43601 0.09159  -0.03022 0.04033  35  ASN A CG  
157  O OD1 . ASN A 28  ? 0.44805 0.58897 0.40489 0.10286  -0.01680 0.05487  35  ASN A OD1 
158  N ND2 . ASN A 28  ? 0.52777 0.74297 0.52088 0.08686  -0.03613 0.03221  35  ASN A ND2 
159  N N   . THR A 29  ? 0.23399 0.47040 0.21595 0.03189  -0.04159 -0.00238 36  THR A N   
160  C CA  . THR A 29  ? 0.26835 0.54189 0.24381 0.02281  -0.04574 -0.01527 36  THR A CA  
161  C C   . THR A 29  ? 0.29800 0.54718 0.25549 0.03152  -0.03877 -0.00348 36  THR A C   
162  O O   . THR A 29  ? 0.31918 0.51796 0.27860 0.02604  -0.03046 0.00193  36  THR A O   
163  C CB  . THR A 29  ? 0.29759 0.56444 0.28559 -0.00815 -0.04540 -0.04018 36  THR A CB  
164  O OG1 . THR A 29  ? 0.28387 0.56996 0.28716 -0.01819 -0.04777 -0.05093 36  THR A OG1 
165  C CG2 . THR A 29  ? 0.34909 0.64573 0.32671 -0.02031 -0.04593 -0.05639 36  THR A CG2 
166  N N   . PHE A 30  ? 0.26553 0.55658 0.20545 0.04511  -0.04163 -0.00017 37  PHE A N   
167  C CA  . PHE A 30  ? 0.31189 0.58220 0.23354 0.05153  -0.03370 0.00936  37  PHE A CA  
168  C C   . PHE A 30  ? 0.37028 0.62766 0.29864 0.02486  -0.03313 -0.01084 37  PHE A C   
169  O O   . PHE A 30  ? 0.28260 0.57524 0.21222 0.00940  -0.03943 -0.03255 37  PHE A O   
170  C CB  . PHE A 30  ? 0.27254 0.59376 0.16965 0.07714  -0.03623 0.01924  37  PHE A CB  
171  C CG  . PHE A 30  ? 0.31529 0.61406 0.19126 0.08471  -0.02613 0.03013  37  PHE A CG  
172  C CD1 . PHE A 30  ? 0.42557 0.66773 0.28813 0.09869  -0.00911 0.05417  37  PHE A CD1 
173  C CD2 . PHE A 30  ? 0.31799 0.64473 0.19009 0.07367  -0.02999 0.01401  37  PHE A CD2 
174  C CE1 . PHE A 30  ? 0.39738 0.61873 0.24127 0.10324  0.00289  0.06398  37  PHE A CE1 
175  C CE2 . PHE A 30  ? 0.46642 0.77519 0.31687 0.08190  -0.02045 0.02479  37  PHE A CE2 
176  C CZ  . PHE A 30  ? 0.36487 0.62193 0.20252 0.09686  -0.00378 0.05060  37  PHE A CZ  
177  N N   . TYR A 31  ? 0.27388 0.48224 0.20433 0.01943  -0.02333 -0.00471 38  TYR A N   
178  C CA  . TYR A 31  ? 0.22740 0.41941 0.16258 0.00029  -0.02014 -0.02052 38  TYR A CA  
179  C C   . TYR A 31  ? 0.25428 0.41147 0.18778 0.00284  -0.00900 -0.00801 38  TYR A C   
180  O O   . TYR A 31  ? 0.27543 0.40536 0.22160 0.00051  -0.00452 -0.00148 38  TYR A O   
181  C CB  . TYR A 31  ? 0.23560 0.41333 0.18853 -0.01593 -0.02171 -0.03506 38  TYR A CB  
182  C CG  . TYR A 31  ? 0.21326 0.36424 0.16591 -0.02786 -0.01367 -0.04626 38  TYR A CG  
183  C CD1 . TYR A 31  ? 0.30842 0.46672 0.24757 -0.03927 -0.01036 -0.06443 38  TYR A CD1 
184  C CD2 . TYR A 31  ? 0.33424 0.45508 0.29727 -0.02630 -0.00767 -0.03949 38  TYR A CD2 
185  C CE1 . TYR A 31  ? 0.41443 0.54111 0.34685 -0.04466 0.00113  -0.07223 38  TYR A CE1 
186  C CE2 . TYR A 31  ? 0.36790 0.46999 0.32746 -0.02962 0.00102  -0.04676 38  TYR A CE2 
187  C CZ  . TYR A 31  ? 0.38302 0.48333 0.32558 -0.03673 0.00657  -0.06146 38  TYR A CZ  
188  O OH  . TYR A 31  ? 0.63234 0.70695 0.56535 -0.03481 0.01919  -0.06635 38  TYR A OH  
189  N N   . SER A 32  ? 0.24450 0.40753 0.16273 0.00570  -0.00401 -0.00683 39  SER A N   
190  C CA  . SER A 32  ? 0.25448 0.39384 0.16930 0.00893  0.00852  0.00688  39  SER A CA  
191  C C   . SER A 32  ? 0.30585 0.42785 0.23636 -0.00379 0.01385  -0.00092 39  SER A C   
192  O O   . SER A 32  ? 0.33393 0.44180 0.27120 -0.00641 0.02363  0.00775  39  SER A O   
193  C CB  . SER A 32  ? 0.27929 0.43451 0.17031 0.01935  0.01304  0.01253  39  SER A CB  
194  O OG  . SER A 32  ? 0.31008 0.48521 0.18302 0.03863  0.01056  0.02502  39  SER A OG  
195  N N   . ASN A 33  ? 0.28462 0.40868 0.21891 -0.01114 0.01010  -0.01726 40  ASN A N   
196  C CA  . ASN A 33  ? 0.28401 0.39632 0.22566 -0.01452 0.01725  -0.02259 40  ASN A CA  
197  C C   . ASN A 33  ? 0.24890 0.35216 0.21162 -0.01732 0.01600  -0.02161 40  ASN A C   
198  O O   . ASN A 33  ? 0.22892 0.32438 0.19549 -0.01729 0.01648  -0.02991 40  ASN A O   
199  C CB  . ASN A 33  ? 0.38781 0.49558 0.31502 -0.01752 0.01954  -0.03893 40  ASN A CB  
200  C CG  . ASN A 33  ? 0.38799 0.48107 0.31466 -0.01268 0.03042  -0.04158 40  ASN A CG  
201  O OD1 . ASN A 33  ? 0.33912 0.44068 0.27222 -0.00651 0.03595  -0.03243 40  ASN A OD1 
202  N ND2 . ASN A 33  ? 0.35318 0.42505 0.26950 -0.01444 0.03627  -0.05409 40  ASN A ND2 
203  N N   . LYS A 34  ? 0.29927 0.30379 0.23283 -0.00950 -0.02162 -0.01120 41  LYS A N   
204  C CA  . LYS A 34  ? 0.24549 0.27402 0.21192 -0.00662 -0.01101 -0.00918 41  LYS A CA  
205  C C   . LYS A 34  ? 0.22953 0.24507 0.19621 -0.00373 -0.00028 -0.02015 41  LYS A C   
206  O O   . LYS A 34  ? 0.21052 0.23848 0.19723 -0.00389 0.00282  -0.01998 41  LYS A O   
207  C CB  . LYS A 34  ? 0.21300 0.25455 0.19053 0.00475  0.00019  -0.00396 41  LYS A CB  
208  C CG  . LYS A 34  ? 0.23010 0.29386 0.21521 0.00717  -0.00699 0.01051  41  LYS A CG  
209  C CD  . LYS A 34  ? 0.25723 0.32073 0.24334 0.02274  0.00455  0.01294  41  LYS A CD  
210  C CE  . LYS A 34  ? 0.21135 0.29997 0.20563 0.03203  0.00106  0.02938  41  LYS A CE  
211  N NZ  . LYS A 34  ? 0.23656 0.35939 0.25343 0.03999  0.00234  0.04309  41  LYS A NZ  
212  N N   . GLU A 35  ? 0.26674 0.25981 0.21071 0.00169  0.00630  -0.02716 42  GLU A N   
213  C CA  . GLU A 35  ? 0.23599 0.22577 0.18711 0.00704  0.01878  -0.03196 42  GLU A CA  
214  C C   . GLU A 35  ? 0.27691 0.26205 0.23200 0.00153  0.01212  -0.03738 42  GLU A C   
215  O O   . GLU A 35  ? 0.25454 0.24356 0.22365 0.00461  0.02051  -0.03949 42  GLU A O   
216  C CB  . GLU A 35  ? 0.25702 0.23029 0.18190 0.01954  0.03002  -0.03253 42  GLU A CB  
217  C CG  . GLU A 35  ? 0.27778 0.21653 0.15869 0.02457  0.02100  -0.04089 42  GLU A CG  
218  C CD  . GLU A 35  ? 0.44990 0.36901 0.29214 0.04603  0.03530  -0.03981 42  GLU A CD  
219  O OE1 . GLU A 35  ? 0.47121 0.40177 0.31383 0.05150  0.04482  -0.03118 42  GLU A OE1 
220  O OE2 . GLU A 35  ? 0.52720 0.41738 0.33452 0.06027  0.03756  -0.04626 42  GLU A OE2 
221  N N   . ILE A 36  ? 0.22414 0.20116 0.16885 -0.00850 -0.00530 -0.03684 43  ILE A N   
222  C CA  . ILE A 36  ? 0.26835 0.23773 0.21550 -0.01588 -0.01410 -0.03925 43  ILE A CA  
223  C C   . ILE A 36  ? 0.23941 0.23813 0.22206 -0.01793 -0.00822 -0.03450 43  ILE A C   
224  O O   . ILE A 36  ? 0.25587 0.25078 0.24322 -0.02189 -0.01157 -0.03601 43  ILE A O   
225  C CB  . ILE A 36  ? 0.28907 0.24296 0.22069 -0.03171 -0.04019 -0.03376 43  ILE A CB  
226  C CG1 . ILE A 36  ? 0.33949 0.33075 0.29986 -0.04151 -0.04816 -0.01677 43  ILE A CG1 
227  C CG2 . ILE A 36  ? 0.43972 0.34585 0.31837 -0.02677 -0.05052 -0.04240 43  ILE A CG2 
228  C CD1 . ILE A 36  ? 0.27143 0.29829 0.26931 -0.05002 -0.05087 -0.00193 43  ILE A CD1 
229  N N   . PHE A 37  ? 0.19432 0.21619 0.19508 -0.01280 -0.00041 -0.02889 44  PHE A N   
230  C CA  . PHE A 37  ? 0.18831 0.22675 0.20817 -0.00843 0.00517  -0.02617 44  PHE A CA  
231  C C   . PHE A 37  ? 0.22147 0.24712 0.24259 -0.00603 0.01087  -0.03520 44  PHE A C   
232  O O   . PHE A 37  ? 0.17205 0.20239 0.20123 -0.00628 0.01003  -0.03481 44  PHE A O   
233  C CB  . PHE A 37  ? 0.17500 0.22267 0.19811 0.00270  0.01188  -0.02214 44  PHE A CB  
234  C CG  . PHE A 37  ? 0.19128 0.22095 0.20926 0.00687  0.01771  -0.02908 44  PHE A CG  
235  C CD1 . PHE A 37  ? 0.21403 0.23682 0.22471 0.00596  0.02007  -0.02858 44  PHE A CD1 
236  C CD2 . PHE A 37  ? 0.21492 0.23436 0.23570 0.01000  0.01838  -0.03296 44  PHE A CD2 
237  C CE1 . PHE A 37  ? 0.21739 0.23054 0.23094 0.00679  0.02445  -0.02781 44  PHE A CE1 
238  C CE2 . PHE A 37  ? 0.23687 0.24198 0.25929 0.00806  0.01807  -0.03338 44  PHE A CE2 
239  C CZ  . PHE A 37  ? 0.22045 0.22587 0.24294 0.00573  0.02183  -0.02882 44  PHE A CZ  
240  N N   . LEU A 38  ? 0.21203 0.22575 0.22743 -0.00275 0.01713  -0.03978 45  LEU A N   
241  C CA  . LEU A 38  ? 0.19080 0.20149 0.21581 -0.00055 0.02191  -0.04224 45  LEU A CA  
242  C C   . LEU A 38  ? 0.19284 0.19454 0.21149 -0.00134 0.01956  -0.04644 45  LEU A C   
243  O O   . LEU A 38  ? 0.20415 0.20813 0.23373 -0.00178 0.01880  -0.04739 45  LEU A O   
244  C CB  . LEU A 38  ? 0.15364 0.16502 0.18214 0.00373  0.03057  -0.03756 45  LEU A CB  
245  C CG  . LEU A 38  ? 0.18678 0.20525 0.23625 0.00370  0.03335  -0.03211 45  LEU A CG  
246  C CD1 . LEU A 38  ? 0.17627 0.19116 0.23629 -0.00270 0.02255  -0.03254 45  LEU A CD1 
247  C CD2 . LEU A 38  ? 0.25427 0.28447 0.31479 0.00723  0.04296  -0.01872 45  LEU A CD2 
248  N N   . ARG A 39  ? 0.21401 0.19860 0.20913 -0.00112 0.01546  -0.04919 46  ARG A N   
249  C CA  . ARG A 39  ? 0.24010 0.20364 0.21964 -0.00154 0.00882  -0.05368 46  ARG A CA  
250  C C   . ARG A 39  ? 0.23695 0.21058 0.23216 -0.01326 -0.00126 -0.04979 46  ARG A C   
251  O O   . ARG A 39  ? 0.25107 0.21846 0.24878 -0.01292 -0.00240 -0.05148 46  ARG A O   
252  C CB  . ARG A 39  ? 0.31928 0.24846 0.25856 -0.00048 -0.00144 -0.05778 46  ARG A CB  
253  C CG  . ARG A 39  ? 0.40465 0.29894 0.31916 -0.00531 -0.01748 -0.06177 46  ARG A CG  
254  C CD  . ARG A 39  ? 0.47502 0.32388 0.34177 -0.00892 -0.03755 -0.06532 46  ARG A CD  
255  N NE  . ARG A 39  ? 0.53035 0.39509 0.41304 -0.03145 -0.05670 -0.05457 46  ARG A NE  
256  C CZ  . ARG A 39  ? 0.55230 0.38977 0.40398 -0.03904 -0.07661 -0.05342 46  ARG A CZ  
257  N NH1 . ARG A 39  ? 0.56326 0.34832 0.35647 -0.02332 -0.07959 -0.06545 46  ARG A NH1 
258  N NH2 . ARG A 39  ? 0.52648 0.39032 0.40434 -0.06063 -0.09414 -0.03760 46  ARG A NH2 
259  N N   . GLU A 40  ? 0.16257 0.15583 0.16964 -0.02126 -0.00688 -0.04135 47  GLU A N   
260  C CA  . GLU A 40  ? 0.17643 0.18788 0.20036 -0.02920 -0.01326 -0.03085 47  GLU A CA  
261  C C   . GLU A 40  ? 0.19663 0.22031 0.23379 -0.02031 -0.00300 -0.03235 47  GLU A C   
262  O O   . GLU A 40  ? 0.18263 0.20892 0.22529 -0.02317 -0.00592 -0.02828 47  GLU A O   
263  C CB  . GLU A 40  ? 0.15779 0.19682 0.19479 -0.03419 -0.01776 -0.01561 47  GLU A CB  
264  C CG  . GLU A 40  ? 0.22202 0.24729 0.24586 -0.04736 -0.03509 -0.01115 47  GLU A CG  
265  C CD  . GLU A 40  ? 0.34075 0.33412 0.34798 -0.06209 -0.05506 -0.01106 47  GLU A CD  
266  O OE1 . GLU A 40  ? 0.28702 0.29021 0.30970 -0.06852 -0.05820 -0.00247 47  GLU A OE1 
267  O OE2 . GLU A 40  ? 0.40636 0.35894 0.37900 -0.06550 -0.06861 -0.01952 47  GLU A OE2 
268  N N   . LEU A 41  ? 0.18058 0.20680 0.21936 -0.01057 0.00584  -0.03715 48  LEU A N   
269  C CA  . LEU A 41  ? 0.18854 0.21493 0.23059 -0.00310 0.00901  -0.03922 48  LEU A CA  
270  C C   . LEU A 41  ? 0.18375 0.19788 0.22873 -0.00452 0.00812  -0.04534 48  LEU A C   
271  O O   . LEU A 41  ? 0.16515 0.17821 0.21175 -0.00252 0.00595  -0.04522 48  LEU A O   
272  C CB  . LEU A 41  ? 0.19812 0.21926 0.23496 0.00483  0.01138  -0.04133 48  LEU A CB  
273  C CG  . LEU A 41  ? 0.15837 0.19103 0.18919 0.01298  0.01431  -0.03420 48  LEU A CG  
274  C CD1 . LEU A 41  ? 0.17662 0.19114 0.19473 0.02103  0.01366  -0.03803 48  LEU A CD1 
275  C CD2 . LEU A 41  ? 0.16618 0.21551 0.19519 0.02300  0.01753  -0.02421 48  LEU A CD2 
276  N N   . ILE A 42  ? 0.16932 0.17582 0.21347 -0.00469 0.01103  -0.04852 49  ILE A N   
277  C CA  . ILE A 42  ? 0.20528 0.20629 0.25425 -0.00139 0.01286  -0.04990 49  ILE A CA  
278  C C   . ILE A 42  ? 0.21764 0.20748 0.25744 -0.00360 0.00763  -0.05133 49  ILE A C   
279  O O   . ILE A 42  ? 0.18213 0.17070 0.22796 -0.00155 0.00634  -0.05111 49  ILE A O   
280  C CB  . ILE A 42  ? 0.18794 0.18764 0.23477 0.00606  0.02179  -0.04824 49  ILE A CB  
281  C CG1 . ILE A 42  ? 0.14965 0.16412 0.21518 0.00468  0.02448  -0.04097 49  ILE A CG1 
282  C CG2 . ILE A 42  ? 0.20819 0.20333 0.25471 0.01616  0.02679  -0.04677 49  ILE A CG2 
283  C CD1 . ILE A 42  ? 0.18836 0.21031 0.25453 0.01287  0.03636  -0.03326 49  ILE A CD1 
284  N N   . SER A 43  ? 0.17233 0.15224 0.19779 -0.01006 0.00105  -0.05060 50  SER A N   
285  C CA  . SER A 43  ? 0.19060 0.15459 0.20693 -0.01661 -0.00924 -0.04861 50  SER A CA  
286  C C   . SER A 43  ? 0.22262 0.20682 0.25601 -0.02128 -0.01089 -0.04022 50  SER A C   
287  O O   . SER A 43  ? 0.18983 0.16574 0.22265 -0.02213 -0.01458 -0.03883 50  SER A O   
288  C CB  . SER A 43  ? 0.29666 0.24153 0.29385 -0.02751 -0.02320 -0.04584 50  SER A CB  
289  O OG  . SER A 43  ? 0.39813 0.33256 0.39376 -0.04115 -0.03879 -0.03722 50  SER A OG  
290  N N   . ASN A 44  ? 0.17693 0.18584 0.22107 -0.02031 -0.00678 -0.03367 51  ASN A N   
291  C CA  . ASN A 44  ? 0.18244 0.20880 0.23370 -0.01597 -0.00402 -0.02509 51  ASN A CA  
292  C C   . ASN A 44  ? 0.16416 0.17976 0.21247 -0.00778 -0.00210 -0.03354 51  ASN A C   
293  O O   . ASN A 44  ? 0.15181 0.16821 0.19959 -0.00654 -0.00383 -0.02887 51  ASN A O   
294  C CB  . ASN A 44  ? 0.17613 0.22357 0.22856 -0.00676 0.00305  -0.01822 51  ASN A CB  
295  C CG  . ASN A 44  ? 0.22352 0.29534 0.28766 -0.01454 0.00041  -0.00074 51  ASN A CG  
296  O OD1 . ASN A 44  ? 0.22282 0.29290 0.29382 -0.03107 -0.01113 0.00771  51  ASN A OD1 
297  N ND2 . ASN A 44  ? 0.20692 0.29921 0.27214 -0.00279 0.00839  0.00692  51  ASN A ND2 
298  N N   . SER A 45  ? 0.16648 0.17403 0.21504 -0.00360 -0.00041 -0.04258 52  SER A N   
299  C CA  . SER A 45  ? 0.18508 0.18501 0.23642 0.00010  -0.00385 -0.04616 52  SER A CA  
300  C C   . SER A 45  ? 0.14509 0.13906 0.20122 -0.00124 -0.00530 -0.04609 52  SER A C   
301  O O   . SER A 45  ? 0.17325 0.16447 0.22983 0.00085  -0.00972 -0.04471 52  SER A O   
302  C CB  . SER A 45  ? 0.13455 0.13267 0.19384 -0.00009 -0.00491 -0.04841 52  SER A CB  
303  O OG  . SER A 45  ? 0.17191 0.16451 0.21988 0.00274  -0.00750 -0.04939 52  SER A OG  
304  N N   . SER A 46  ? 0.17217 0.15840 0.22516 -0.00194 -0.00251 -0.04781 53  SER A N   
305  C CA  . SER A 46  ? 0.18655 0.15767 0.23408 0.00210  -0.00387 -0.04837 53  SER A CA  
306  C C   . SER A 46  ? 0.20906 0.17291 0.25040 -0.00460 -0.01165 -0.04389 53  SER A C   
307  O O   . SER A 46  ? 0.20724 0.16432 0.24911 -0.00084 -0.01416 -0.04263 53  SER A O   
308  C CB  . SER A 46  ? 0.22651 0.17729 0.25520 0.00761  -0.00101 -0.05237 53  SER A CB  
309  O OG  . SER A 46  ? 0.26400 0.18861 0.27540 0.01564  -0.00372 -0.05383 53  SER A OG  
310  N N   . ASP A 47  ? 0.19599 0.16539 0.23493 -0.01474 -0.01570 -0.03744 54  ASP A N   
311  C CA  . ASP A 47  ? 0.22008 0.19252 0.26050 -0.02276 -0.02234 -0.02543 54  ASP A CA  
312  C C   . ASP A 47  ? 0.21034 0.19746 0.25579 -0.01450 -0.01775 -0.02227 54  ASP A C   
313  O O   . ASP A 47  ? 0.21509 0.19693 0.25898 -0.01560 -0.02176 -0.01607 54  ASP A O   
314  C CB  . ASP A 47  ? 0.17915 0.16970 0.22652 -0.03461 -0.02623 -0.01103 54  ASP A CB  
315  C CG  . ASP A 47  ? 0.27853 0.24411 0.31421 -0.04785 -0.04000 -0.01116 54  ASP A CG  
316  O OD1 . ASP A 47  ? 0.31137 0.23789 0.32490 -0.04494 -0.04619 -0.02254 54  ASP A OD1 
317  O OD2 . ASP A 47  ? 0.28803 0.27057 0.33290 -0.05931 -0.04597 0.00163  54  ASP A OD2 
318  N N   . ALA A 48  ? 0.15865 0.15736 0.20391 -0.00556 -0.01182 -0.02647 55  ALA A N   
319  C CA  . ALA A 48  ? 0.15334 0.15339 0.18969 0.00470  -0.01165 -0.02534 55  ALA A CA  
320  C C   . ALA A 48  ? 0.19319 0.17896 0.23165 0.00637  -0.01840 -0.03195 55  ALA A C   
321  O O   . ALA A 48  ? 0.20423 0.18579 0.23439 0.01111  -0.02227 -0.02856 55  ALA A O   
322  C CB  . ALA A 48  ? 0.15646 0.15708 0.18033 0.01489  -0.00892 -0.02965 55  ALA A CB  
323  N N   . LEU A 49  ? 0.16085 0.14275 0.21116 0.00451  -0.01907 -0.03823 56  LEU A N   
324  C CA  . LEU A 49  ? 0.17706 0.15531 0.23739 0.00768  -0.02399 -0.03822 56  LEU A CA  
325  C C   . LEU A 49  ? 0.20611 0.17402 0.26254 0.00884  -0.02441 -0.03496 56  LEU A C   
326  O O   . LEU A 49  ? 0.19453 0.15992 0.25323 0.01277  -0.02983 -0.03188 56  LEU A O   
327  C CB  . LEU A 49  ? 0.17947 0.16562 0.25714 0.00931  -0.02026 -0.03868 56  LEU A CB  
328  C CG  . LEU A 49  ? 0.17119 0.16379 0.25572 0.00512  -0.02548 -0.03850 56  LEU A CG  
329  C CD1 . LEU A 49  ? 0.20462 0.20886 0.30354 0.00535  -0.01688 -0.03614 56  LEU A CD1 
330  C CD2 . LEU A 49  ? 0.15439 0.14712 0.24930 0.00255  -0.04115 -0.03265 56  LEU A CD2 
331  N N   . ASP A 50  ? 0.20610 0.16278 0.25368 0.00449  -0.02227 -0.03482 57  ASP A N   
332  C CA  . ASP A 50  ? 0.22308 0.15847 0.25974 0.00317  -0.02779 -0.03089 57  ASP A CA  
333  C C   . ASP A 50  ? 0.19781 0.13993 0.23401 -0.00061 -0.03204 -0.02122 57  ASP A C   
334  O O   . ASP A 50  ? 0.23879 0.16829 0.27108 0.00250  -0.03676 -0.01781 57  ASP A O   
335  C CB  . ASP A 50  ? 0.21488 0.12939 0.23658 -0.00664 -0.03305 -0.02992 57  ASP A CB  
336  C CG  . ASP A 50  ? 0.27519 0.16820 0.28194 0.00259  -0.02996 -0.03986 57  ASP A CG  
337  O OD1 . ASP A 50  ? 0.29301 0.19368 0.30628 0.01842  -0.02022 -0.04394 57  ASP A OD1 
338  O OD2 . ASP A 50  ? 0.31033 0.17831 0.29722 -0.00566 -0.03856 -0.04065 57  ASP A OD2 
339  N N   . LYS A 51  ? 0.18771 0.14975 0.22491 -0.00385 -0.02879 -0.01487 58  LYS A N   
340  C CA  . LYS A 51  ? 0.19583 0.16768 0.22815 -0.00273 -0.02879 -0.00146 58  LYS A CA  
341  C C   . LYS A 51  ? 0.25987 0.22650 0.28420 0.00870  -0.03170 -0.00594 58  LYS A C   
342  O O   . LYS A 51  ? 0.23556 0.19687 0.25449 0.01012  -0.03523 0.00218  58  LYS A O   
343  C CB  . LYS A 51  ? 0.21390 0.21137 0.24519 -0.00020 -0.02029 0.00878  58  LYS A CB  
344  C CG  . LYS A 51  ? 0.22185 0.23189 0.26666 -0.01502 -0.02125 0.02180  58  LYS A CG  
345  C CD  . LYS A 51  ? 0.22472 0.26891 0.27307 -0.00754 -0.00990 0.03578  58  LYS A CD  
346  C CE  . LYS A 51  ? 0.26528 0.32611 0.33309 -0.02459 -0.01426 0.04995  58  LYS A CE  
347  N NZ  . LYS A 51  ? 0.36451 0.46695 0.44034 -0.01343 -0.00081 0.06873  58  LYS A NZ  
348  N N   . ILE A 52  ? 0.20788 0.17374 0.23071 0.01499  -0.03360 -0.01676 59  ILE A N   
349  C CA  . ILE A 52  ? 0.20996 0.16667 0.22354 0.02223  -0.04336 -0.01886 59  ILE A CA  
350  C C   . ILE A 52  ? 0.24990 0.20208 0.28026 0.02098  -0.04923 -0.01843 59  ILE A C   
351  O O   . ILE A 52  ? 0.23933 0.18529 0.26381 0.02521  -0.05732 -0.01437 59  ILE A O   
352  C CB  . ILE A 52  ? 0.25780 0.20790 0.26263 0.02531  -0.05112 -0.02717 59  ILE A CB  
353  C CG1 . ILE A 52  ? 0.31489 0.24657 0.30006 0.03090  -0.06821 -0.02762 59  ILE A CG1 
354  C CG2 . ILE A 52  ? 0.22316 0.18098 0.25524 0.01767  -0.05216 -0.03148 59  ILE A CG2 
355  C CD1 . ILE A 52  ? 0.31856 0.24076 0.26832 0.04394  -0.06513 -0.02207 59  ILE A CD1 
356  N N   . ARG A 53  ? 0.20962 0.16345 0.25666 0.01899  -0.04432 -0.02125 60  ARG A N   
357  C CA  . ARG A 53  ? 0.22795 0.17659 0.28516 0.02550  -0.04603 -0.01831 60  ARG A CA  
358  C C   . ARG A 53  ? 0.29106 0.22177 0.33367 0.02555  -0.04824 -0.01266 60  ARG A C   
359  O O   . ARG A 53  ? 0.26445 0.19076 0.30839 0.03214  -0.05398 -0.00783 60  ARG A O   
360  C CB  . ARG A 53  ? 0.20511 0.15312 0.27076 0.03107  -0.03708 -0.02143 60  ARG A CB  
361  C CG  . ARG A 53  ? 0.31724 0.26206 0.39006 0.04649  -0.03549 -0.01578 60  ARG A CG  
362  C CD  . ARG A 53  ? 0.53768 0.47546 0.60592 0.06073  -0.02330 -0.01769 60  ARG A CD  
363  N NE  . ARG A 53  ? 0.49298 0.46653 0.59267 0.06892  -0.01642 -0.00873 60  ARG A NE  
364  C CZ  . ARG A 53  ? 0.56637 0.54836 0.66831 0.07510  -0.00461 -0.00910 60  ARG A CZ  
365  N NH1 . ARG A 53  ? 0.37858 0.33141 0.44912 0.07436  -0.00023 -0.02101 60  ARG A NH1 
366  N NH2 . ARG A 53  ? 0.36063 0.38234 0.49826 0.08108  0.00114  0.00594  60  ARG A NH2 
367  N N   . TYR A 54  ? 0.23232 0.15392 0.26337 0.01642  -0.04609 -0.00985 61  TYR A N   
368  C CA  . TYR A 54  ? 0.28322 0.18682 0.30304 0.01182  -0.05173 0.00037  61  TYR A CA  
369  C C   . TYR A 54  ? 0.30111 0.21542 0.31673 0.01485  -0.05411 0.00946  61  TYR A C   
370  O O   . TYR A 54  ? 0.30415 0.20475 0.31440 0.01809  -0.05993 0.01573  61  TYR A O   
371  C CB  . TYR A 54  ? 0.28730 0.18540 0.30258 -0.00401 -0.05371 0.00861  61  TYR A CB  
372  C CG  . TYR A 54  ? 0.34567 0.22306 0.35246 -0.01368 -0.06410 0.02403  61  TYR A CG  
373  C CD1 . TYR A 54  ? 0.32803 0.16096 0.31753 -0.01195 -0.07462 0.02029  61  TYR A CD1 
374  C CD2 . TYR A 54  ? 0.31385 0.21406 0.32653 -0.02161 -0.06311 0.04460  61  TYR A CD2 
375  C CE1 . TYR A 54  ? 0.37196 0.17821 0.35078 -0.02285 -0.08815 0.03544  61  TYR A CE1 
376  C CE2 . TYR A 54  ? 0.32638 0.21034 0.33550 -0.03316 -0.07392 0.06363  61  TYR A CE2 
377  C CZ  . TYR A 54  ? 0.36880 0.20306 0.36128 -0.03609 -0.08853 0.05827  61  TYR A CZ  
378  O OH  . TYR A 54  ? 0.43499 0.24514 0.42086 -0.04960 -0.10323 0.07793  61  TYR A OH  
379  N N   . GLU A 55  ? 0.24916 0.18280 0.26037 0.01709  -0.04989 0.01025  62  GLU A N   
380  C CA  . GLU A 55  ? 0.27530 0.21163 0.26982 0.02555  -0.05208 0.01781  62  GLU A CA  
381  C C   . GLU A 55  ? 0.31355 0.23949 0.30793 0.03297  -0.06355 0.01166  62  GLU A C   
382  O O   . GLU A 55  ? 0.36892 0.28773 0.35132 0.03805  -0.06907 0.01946  62  GLU A O   
383  C CB  . GLU A 55  ? 0.28672 0.23483 0.26364 0.03388  -0.04570 0.01725  62  GLU A CB  
384  C CG  . GLU A 55  ? 0.34622 0.31560 0.32611 0.03033  -0.03288 0.03293  62  GLU A CG  
385  C CD  . GLU A 55  ? 0.51538 0.49570 0.46863 0.04870  -0.02285 0.03748  62  GLU A CD  
386  O OE1 . GLU A 55  ? 0.40748 0.36712 0.33358 0.06179  -0.02996 0.02318  62  GLU A OE1 
387  O OE2 . GLU A 55  ? 0.44157 0.44920 0.39890 0.05121  -0.00946 0.05743  62  GLU A OE2 
388  N N   . SER A 56  ? 0.30706 0.23595 0.31815 0.03309  -0.06790 0.00165  63  SER A N   
389  C CA  . SER A 56  ? 0.33172 0.26030 0.35257 0.03784  -0.08116 0.00241  63  SER A CA  
390  C C   . SER A 56  ? 0.32464 0.24766 0.35616 0.04306  -0.08114 0.00912  63  SER A C   
391  O O   . SER A 56  ? 0.31364 0.23939 0.35285 0.04865  -0.09220 0.01472  63  SER A O   
392  C CB  . SER A 56  ? 0.34393 0.28621 0.38875 0.03486  -0.08566 -0.00198 63  SER A CB  
393  O OG  . SER A 56  ? 0.32061 0.27209 0.38826 0.03753  -0.07414 -0.00158 63  SER A OG  
394  N N   . LEU A 57  ? 0.32674 0.23731 0.35546 0.04185  -0.07193 0.00958  64  LEU A N   
395  C CA  . LEU A 57  ? 0.32133 0.21432 0.34966 0.05085  -0.07345 0.01454  64  LEU A CA  
396  C C   . LEU A 57  ? 0.38818 0.27154 0.40345 0.05214  -0.08176 0.02451  64  LEU A C   
397  O O   . LEU A 57  ? 0.45610 0.33137 0.47447 0.06314  -0.08659 0.02975  64  LEU A O   
398  C CB  . LEU A 57  ? 0.33008 0.19518 0.34445 0.04795  -0.06848 0.01192  64  LEU A CB  
399  C CG  . LEU A 57  ? 0.37723 0.24433 0.39690 0.05159  -0.05991 0.00214  64  LEU A CG  
400  C CD1 . LEU A 57  ? 0.40916 0.23302 0.40175 0.05020  -0.06188 -0.00080 64  LEU A CD1 
401  C CD2 . LEU A 57  ? 0.34320 0.22997 0.38365 0.07017  -0.05470 0.00308  64  LEU A CD2 
402  N N   . THR A 58  ? 0.35206 0.23791 0.35160 0.04426  -0.08177 0.02971  65  THR A N   
403  C CA  . THR A 58  ? 0.41337 0.29216 0.39691 0.04722  -0.08771 0.04165  65  THR A CA  
404  C C   . THR A 58  ? 0.52032 0.40867 0.48899 0.05349  -0.09448 0.04078  65  THR A C   
405  O O   . THR A 58  ? 0.51765 0.39839 0.46891 0.05958  -0.10118 0.04972  65  THR A O   
406  C CB  . THR A 58  ? 0.58838 0.46183 0.56068 0.03680  -0.08223 0.05610  65  THR A CB  
407  O OG1 . THR A 58  ? 0.50133 0.39635 0.47029 0.03302  -0.07272 0.05753  65  THR A OG1 
408  C CG2 . THR A 58  ? 0.56437 0.41303 0.54131 0.02742  -0.08429 0.05723  65  THR A CG2 
409  N N   . ASP A 59  ? 0.53072 0.37395 0.39272 0.10670  -0.05023 0.06422  66  ASP A N   
410  C CA  . ASP A 59  ? 0.51321 0.38262 0.37158 0.10626  -0.06239 0.06303  66  ASP A CA  
411  C C   . ASP A 59  ? 0.37117 0.27100 0.25624 0.10500  -0.07165 0.05286  66  ASP A C   
412  O O   . ASP A 59  ? 0.40309 0.31176 0.29661 0.09267  -0.06977 0.04081  66  ASP A O   
413  C CB  . ASP A 59  ? 0.48074 0.34667 0.32181 0.09327  -0.05696 0.05954  66  ASP A CB  
414  C CG  . ASP A 59  ? 0.58530 0.46803 0.41162 0.09482  -0.06852 0.05697  66  ASP A CG  
415  O OD1 . ASP A 59  ? 0.58134 0.47834 0.41063 0.10326  -0.08384 0.05892  66  ASP A OD1 
416  O OD2 . ASP A 59  ? 0.52198 0.40299 0.33260 0.08789  -0.06258 0.05354  66  ASP A OD2 
417  N N   . PRO A 60  ? 0.45615 0.37430 0.35752 0.11767  -0.08158 0.05944  67  PRO A N   
418  C CA  . PRO A 60  ? 0.43599 0.38644 0.36757 0.11472  -0.09039 0.05288  67  PRO A CA  
419  C C   . PRO A 60  ? 0.45454 0.42023 0.38098 0.10145  -0.10347 0.04343  67  PRO A C   
420  O O   . PRO A 60  ? 0.44504 0.42919 0.39323 0.09304  -0.10724 0.03506  67  PRO A O   
421  C CB  . PRO A 60  ? 0.46222 0.43320 0.41235 0.13177  -0.09984 0.06710  67  PRO A CB  
422  C CG  . PRO A 60  ? 0.66344 0.60987 0.58950 0.14495  -0.09648 0.08008  67  PRO A CG  
423  C CD  . PRO A 60  ? 0.49659 0.40613 0.39390 0.13590  -0.08245 0.07520  67  PRO A CD  
424  N N   . SER A 61  ? 0.45874 0.41378 0.35373 0.10004  -0.10966 0.04468  68  SER A N   
425  C CA  . SER A 61  ? 0.40155 0.36246 0.28328 0.08941  -0.12115 0.03407  68  SER A CA  
426  C C   . SER A 61  ? 0.45326 0.40752 0.33743 0.07762  -0.10887 0.02072  68  SER A C   
427  O O   . SER A 61  ? 0.37360 0.33163 0.25247 0.06932  -0.11690 0.01039  68  SER A O   
428  C CB  . SER A 61  ? 0.40933 0.35445 0.24878 0.09324  -0.12660 0.03808  68  SER A CB  
429  O OG  . SER A 61  ? 0.51356 0.43615 0.33216 0.09292  -0.10717 0.03941  68  SER A OG  
430  N N   . LYS A 62  ? 0.34465 0.28718 0.23534 0.07645  -0.09088 0.02108  69  LYS A N   
431  C CA  . LYS A 62  ? 0.35842 0.29913 0.25539 0.06568  -0.08094 0.01050  69  LYS A CA  
432  C C   . LYS A 62  ? 0.34966 0.30888 0.27369 0.05985  -0.08727 0.00223  69  LYS A C   
433  O O   . LYS A 62  ? 0.32386 0.28339 0.25048 0.05134  -0.08344 -0.00696 69  LYS A O   
434  C CB  . LYS A 62  ? 0.37911 0.30490 0.27968 0.06353  -0.06470 0.01374  69  LYS A CB  
435  C CG  . LYS A 62  ? 0.53345 0.44061 0.41005 0.06543  -0.05674 0.02356  69  LYS A CG  
436  C CD  . LYS A 62  ? 0.43855 0.34382 0.30788 0.05623  -0.04623 0.02108  69  LYS A CD  
437  C CE  . LYS A 62  ? 0.48043 0.37196 0.32788 0.05776  -0.03729 0.03383  69  LYS A CE  
438  N NZ  . LYS A 62  ? 0.58584 0.48186 0.43381 0.04936  -0.02477 0.03496  69  LYS A NZ  
439  N N   . LEU A 63  ? 0.32720 0.30337 0.27309 0.06500  -0.09592 0.00733  70  LEU A N   
440  C CA  . LEU A 63  ? 0.33057 0.32781 0.30556 0.05914  -0.10122 0.00302  70  LEU A CA  
441  C C   . LEU A 63  ? 0.33962 0.35191 0.31653 0.05309  -0.12221 0.00155  70  LEU A C   
442  O O   . LEU A 63  ? 0.29352 0.32663 0.29843 0.04686  -0.12937 0.00137  70  LEU A O   
443  C CB  . LEU A 63  ? 0.37025 0.38030 0.37243 0.06884  -0.09510 0.01150  70  LEU A CB  
444  C CG  . LEU A 63  ? 0.32935 0.31866 0.32676 0.07275  -0.07607 0.01029  70  LEU A CG  
445  C CD1 . LEU A 63  ? 0.32475 0.32254 0.34302 0.08570  -0.06874 0.01771  70  LEU A CD1 
446  C CD2 . LEU A 63  ? 0.26117 0.24419 0.25730 0.06003  -0.06886 -0.00101 70  LEU A CD2 
447  N N   . ASP A 64  ? 0.30033 0.30081 0.24600 0.05382  -0.13269 0.00097  71  ASP A N   
448  C CA  . ASP A 64  ? 0.37927 0.38638 0.31822 0.04568  -0.15565 -0.00265 71  ASP A CA  
449  C C   . ASP A 64  ? 0.36735 0.36834 0.30756 0.03225  -0.15693 -0.01580 71  ASP A C   
450  O O   . ASP A 64  ? 0.38729 0.39773 0.33831 0.02018  -0.16729 -0.01737 71  ASP A O   
451  C CB  . ASP A 64  ? 0.37496 0.36254 0.26997 0.04945  -0.16246 -0.00279 71  ASP A CB  
452  C CG  . ASP A 64  ? 0.52743 0.52453 0.42258 0.06057  -0.16759 0.01219  71  ASP A CG  
453  O OD1 . ASP A 64  ? 0.50961 0.52852 0.43909 0.06720  -0.16749 0.02285  71  ASP A OD1 
454  O OD2 . ASP A 64  ? 0.50979 0.49198 0.36992 0.06409  -0.17011 0.01409  71  ASP A OD2 
455  N N   . SER A 65  ? 0.35740 0.34303 0.28975 0.03213  -0.13808 -0.02287 72  SER A N   
456  C CA  . SER A 65  ? 0.33873 0.31656 0.27250 0.02251  -0.13543 -0.03376 72  SER A CA  
457  C C   . SER A 65  ? 0.36859 0.36676 0.34330 0.01662  -0.13119 -0.03156 72  SER A C   
458  O O   . SER A 65  ? 0.40198 0.39385 0.38035 0.00975  -0.12607 -0.03865 72  SER A O   
459  C CB  . SER A 65  ? 0.36870 0.32678 0.28004 0.02702  -0.11649 -0.03880 72  SER A CB  
460  O OG  . SER A 65  ? 0.32513 0.28851 0.24827 0.03292  -0.10085 -0.03121 72  SER A OG  
461  N N   . GLY A 66  ? 0.34490 0.36636 0.34862 0.02117  -0.13156 -0.02083 73  GLY A N   
462  C CA  . GLY A 66  ? 0.33626 0.37786 0.37644 0.01822  -0.12512 -0.01695 73  GLY A CA  
463  C C   . GLY A 66  ? 0.32427 0.37476 0.37920 0.03125  -0.11066 -0.00792 73  GLY A C   
464  O O   . GLY A 66  ? 0.25829 0.28998 0.29620 0.03704  -0.09641 -0.01049 73  GLY A O   
465  N N   . LYS A 67  ? 0.25806 0.33608 0.34417 0.03622  -0.11408 0.00354  74  LYS A N   
466  C CA  . LYS A 67  ? 0.21505 0.29636 0.31047 0.05231  -0.09887 0.01204  74  LYS A CA  
467  C C   . LYS A 67  ? 0.29448 0.37553 0.40189 0.05365  -0.08096 0.01018  74  LYS A C   
468  O O   . LYS A 67  ? 0.27262 0.34023 0.37212 0.06615  -0.06579 0.01196  74  LYS A O   
469  C CB  . LYS A 67  ? 0.23421 0.34704 0.35789 0.06209  -0.10772 0.02784  74  LYS A CB  
470  C CG  . LYS A 67  ? 0.43065 0.54073 0.53736 0.06554  -0.12390 0.03210  74  LYS A CG  
471  C CD  . LYS A 67  ? 0.48834 0.63818 0.62907 0.06935  -0.13929 0.04822  74  LYS A CD  
472  C CE  . LYS A 67  ? 0.79097 0.94027 0.92383 0.08846  -0.13922 0.06021  74  LYS A CE  
473  N NZ  . LYS A 67  ? 0.78154 0.96555 0.93416 0.08919  -0.15114 0.07040  74  LYS A NZ  
474  N N   . GLU A 68  ? 0.21258 0.30414 0.33487 0.04131  -0.08267 0.00675  75  GLU A N   
475  C CA  . GLU A 68  ? 0.23156 0.32499 0.36425 0.04328  -0.06618 0.00687  75  GLU A CA  
476  C C   . GLU A 68  ? 0.26587 0.32718 0.36814 0.04093  -0.05580 -0.00490 75  GLU A C   
477  O O   . GLU A 68  ? 0.27351 0.32083 0.35887 0.03102  -0.06213 -0.01345 75  GLU A O   
478  C CB  . GLU A 68  ? 0.22803 0.34339 0.38747 0.03008  -0.07166 0.00958  75  GLU A CB  
479  C CG  . GLU A 68  ? 0.26802 0.42337 0.46787 0.03055  -0.08017 0.02529  75  GLU A CG  
480  C CD  . GLU A 68  ? 0.75019 0.91387 0.95080 0.02516  -0.10334 0.02764  75  GLU A CD  
481  O OE1 . GLU A 68  ? 0.74796 0.89129 0.92555 0.01190  -0.11709 0.01633  75  GLU A OE1 
482  O OE2 . GLU A 68  ? 0.56797 0.75626 0.78770 0.03539  -0.10661 0.04069  75  GLU A OE2 
483  N N   . LEU A 69  ? 0.18387 0.23335 0.27843 0.05051  -0.04012 -0.00459 76  LEU A N   
484  C CA  . LEU A 69  ? 0.18222 0.20280 0.24953 0.04696  -0.03236 -0.01394 76  LEU A CA  
485  C C   . LEU A 69  ? 0.15872 0.18185 0.23079 0.04539  -0.02231 -0.01500 76  LEU A C   
486  O O   . LEU A 69  ? 0.20862 0.23110 0.28149 0.05724  -0.01025 -0.01060 76  LEU A O   
487  C CB  . LEU A 69  ? 0.30531 0.30089 0.35080 0.05764  -0.02545 -0.01355 76  LEU A CB  
488  C CG  . LEU A 69  ? 0.31363 0.30312 0.35035 0.06027  -0.03361 -0.01067 76  LEU A CG  
489  C CD1 . LEU A 69  ? 0.41100 0.36829 0.42302 0.06799  -0.02566 -0.01047 76  LEU A CD1 
490  C CD2 . LEU A 69  ? 0.25945 0.24773 0.28783 0.04701  -0.04314 -0.01627 76  LEU A CD2 
491  N N   . HIS A 70  ? 0.16220 0.18663 0.23500 0.03285  -0.02602 -0.01997 77  HIS A N   
492  C CA  . HIS A 70  ? 0.21141 0.24163 0.29081 0.03123  -0.01767 -0.01849 77  HIS A CA  
493  C C   . HIS A 70  ? 0.13618 0.15631 0.20475 0.01964  -0.02081 -0.02523 77  HIS A C   
494  O O   . HIS A 70  ? 0.15677 0.17008 0.21778 0.01335  -0.02892 -0.03012 77  HIS A O   
495  C CB  . HIS A 70  ? 0.17852 0.23896 0.29101 0.03013  -0.01915 -0.00871 77  HIS A CB  
496  C CG  . HIS A 70  ? 0.21342 0.28304 0.33856 0.01667  -0.03496 -0.00992 77  HIS A CG  
497  N ND1 . HIS A 70  ? 0.24075 0.33040 0.38700 0.01472  -0.04664 -0.00351 77  HIS A ND1 
498  C CD2 . HIS A 70  ? 0.23102 0.28950 0.34772 0.00518  -0.04150 -0.01676 77  HIS A CD2 
499  C CE1 . HIS A 70  ? 0.23515 0.32100 0.38091 0.00120  -0.06071 -0.00816 77  HIS A CE1 
500  N NE2 . HIS A 70  ? 0.21314 0.27905 0.34074 -0.00338 -0.05642 -0.01625 77  HIS A NE2 
501  N N   . ILE A 71  ? 0.17281 0.19322 0.24056 0.01883  -0.01304 -0.02385 78  ILE A N   
502  C CA  . ILE A 71  ? 0.17160 0.18497 0.23104 0.01020  -0.01481 -0.02742 78  ILE A CA  
503  C C   . ILE A 71  ? 0.18095 0.20893 0.25880 0.00664  -0.01195 -0.02085 78  ILE A C   
504  O O   . ILE A 71  ? 0.15885 0.19575 0.24348 0.01292  -0.00168 -0.01405 78  ILE A O   
505  C CB  . ILE A 71  ? 0.15753 0.15188 0.19086 0.01179  -0.00938 -0.03121 78  ILE A CB  
506  C CG1 . ILE A 71  ? 0.19966 0.17698 0.21561 0.01329  -0.01207 -0.03591 78  ILE A CG1 
507  C CG2 . ILE A 71  ? 0.16628 0.15862 0.19477 0.00350  -0.01307 -0.03237 78  ILE A CG2 
508  C CD1 . ILE A 71  ? 0.23513 0.18935 0.22295 0.01196  -0.00987 -0.03993 78  ILE A CD1 
509  N N   . ASN A 72  ? 0.16564 0.19406 0.25010 -0.00247 -0.01960 -0.02191 79  ASN A N   
510  C CA  . ASN A 72  ? 0.17582 0.21244 0.27566 -0.00841 -0.01803 -0.01517 79  ASN A CA  
511  C C   . ASN A 72  ? 0.19181 0.21558 0.27745 -0.01125 -0.01688 -0.01682 79  ASN A C   
512  O O   . ASN A 72  ? 0.17508 0.18789 0.24854 -0.01215 -0.02243 -0.02299 79  ASN A O   
513  C CB  . ASN A 72  ? 0.14594 0.18880 0.26448 -0.01757 -0.02963 -0.01391 79  ASN A CB  
514  C CG  . ASN A 72  ? 0.15350 0.21535 0.29142 -0.01588 -0.03320 -0.00898 79  ASN A CG  
515  O OD1 . ASN A 72  ? 0.15138 0.22774 0.29845 -0.00730 -0.02288 -0.00187 79  ASN A OD1 
516  N ND2 . ASN A 72  ? 0.19661 0.25787 0.33928 -0.02281 -0.04787 -0.01200 79  ASN A ND2 
517  N N   . LEU A 73  ? 0.15898 0.18634 0.24742 -0.01154 -0.00890 -0.00927 80  LEU A N   
518  C CA  . LEU A 73  ? 0.13988 0.15719 0.21715 -0.01365 -0.00824 -0.00770 80  LEU A CA  
519  C C   . LEU A 73  ? 0.18478 0.20376 0.27972 -0.02148 -0.00960 -0.00021 80  LEU A C   
520  O O   . LEU A 73  ? 0.14182 0.17381 0.25328 -0.02367 -0.00306 0.00944  80  LEU A O   
521  C CB  . LEU A 73  ? 0.16555 0.18041 0.22461 -0.00770 0.00153  -0.00432 80  LEU A CB  
522  C CG  . LEU A 73  ? 0.21588 0.22307 0.25402 -0.00147 0.00290  -0.01144 80  LEU A CG  
523  C CD1 . LEU A 73  ? 0.17856 0.17702 0.19205 0.00397  0.01166  -0.00885 80  LEU A CD1 
524  C CD2 . LEU A 73  ? 0.18216 0.18104 0.21065 -0.00490 -0.00769 -0.01911 80  LEU A CD2 
525  N N   . ILE A 74  ? 0.14060 0.14551 0.23223 -0.02538 -0.01727 -0.00352 81  ILE A N   
526  C CA  . ILE A 74  ? 0.17192 0.16910 0.27601 -0.03446 -0.02124 0.00160  81  ILE A CA  
527  C C   . ILE A 74  ? 0.18888 0.17010 0.28081 -0.03234 -0.01897 0.00532  81  ILE A C   
528  O O   . ILE A 74  ? 0.19835 0.16480 0.27781 -0.02791 -0.02337 -0.00061 81  ILE A O   
529  C CB  . ILE A 74  ? 0.16750 0.15383 0.27366 -0.04011 -0.03382 -0.00675 81  ILE A CB  
530  C CG1 . ILE A 74  ? 0.23284 0.23579 0.34720 -0.03924 -0.03729 -0.01037 81  ILE A CG1 
531  C CG2 . ILE A 74  ? 0.17915 0.15366 0.29697 -0.05295 -0.04019 -0.00152 81  ILE A CG2 
532  C CD1 . ILE A 74  ? 0.23794 0.22906 0.34644 -0.04290 -0.05047 -0.01948 81  ILE A CD1 
533  N N   . PRO A 75  ? 0.22068 0.20509 0.31627 -0.03400 -0.01105 0.01701  82  PRO A N   
534  C CA  . PRO A 75  ? 0.26288 0.23058 0.34854 -0.03230 -0.00979 0.02312  82  PRO A CA  
535  C C   . PRO A 75  ? 0.24807 0.19583 0.34306 -0.04230 -0.01511 0.02646  82  PRO A C   
536  O O   . PRO A 75  ? 0.25545 0.20861 0.36954 -0.05428 -0.01761 0.03034  82  PRO A O   
537  C CB  . PRO A 75  ? 0.20661 0.18558 0.28895 -0.02988 0.00156  0.03511  82  PRO A CB  
538  C CG  . PRO A 75  ? 0.22750 0.22554 0.32962 -0.03523 0.00715  0.03955  82  PRO A CG  
539  C CD  . PRO A 75  ? 0.21738 0.22134 0.32590 -0.03563 -0.00115 0.02701  82  PRO A CD  
540  N N   . ASN A 76  ? 0.23573 0.15912 0.31684 -0.03728 -0.01765 0.02547  83  ASN A N   
541  C CA  . ASN A 76  ? 0.25302 0.14610 0.33461 -0.04550 -0.02265 0.02794  83  ASN A CA  
542  C C   . ASN A 76  ? 0.31839 0.19408 0.38748 -0.03707 -0.01707 0.03772  83  ASN A C   
543  O O   . ASN A 76  ? 0.33107 0.19670 0.38514 -0.02320 -0.01723 0.03372  83  ASN A O   
544  C CB  . ASN A 76  ? 0.26441 0.13448 0.33512 -0.04513 -0.03282 0.01336  83  ASN A CB  
545  C CG  . ASN A 76  ? 0.37346 0.20493 0.43978 -0.05660 -0.04048 0.01374  83  ASN A CG  
546  O OD1 . ASN A 76  ? 0.40519 0.21182 0.46288 -0.05387 -0.03683 0.02136  83  ASN A OD1 
547  N ND2 . ASN A 76  ? 0.46050 0.28468 0.53121 -0.07021 -0.05249 0.00609  83  ASN A ND2 
548  N N   . LYS A 77  ? 0.31915 0.19346 0.39607 -0.04466 -0.01145 0.05267  84  LYS A N   
549  C CA  . LYS A 77  ? 0.31925 0.17786 0.38360 -0.03621 -0.00593 0.06462  84  LYS A CA  
550  C C   . LYS A 77  ? 0.41998 0.23522 0.47224 -0.03378 -0.01092 0.06239  84  LYS A C   
551  O O   . LYS A 77  ? 0.41136 0.21290 0.44944 -0.01916 -0.00774 0.06801  84  LYS A O   
552  C CB  . LYS A 77  ? 0.34296 0.21023 0.41698 -0.04496 0.00296  0.08281  84  LYS A CB  
553  C CG  . LYS A 77  ? 0.38000 0.28353 0.45516 -0.04087 0.01172  0.08666  84  LYS A CG  
554  C CD  . LYS A 77  ? 0.39462 0.30448 0.47541 -0.04659 0.02372  0.10670  84  LYS A CD  
555  C CE  . LYS A 77  ? 0.39898 0.33885 0.47387 -0.03996 0.03463  0.10981  84  LYS A CE  
556  N NZ  . LYS A 77  ? 0.51285 0.47511 0.60442 -0.04364 0.03395  0.09954  84  LYS A NZ  
557  N N   . GLN A 78  ? 0.46793 0.25949 0.52335 -0.04703 -0.01939 0.05441  85  GLN A N   
558  C CA  . GLN A 78  ? 0.53541 0.27584 0.57168 -0.04457 -0.02427 0.05023  85  GLN A CA  
559  C C   . GLN A 78  ? 0.48834 0.21942 0.50423 -0.02293 -0.02383 0.03772  85  GLN A C   
560  O O   . GLN A 78  ? 0.58217 0.28166 0.57988 -0.00794 -0.02020 0.04036  85  GLN A O   
561  C CB  . GLN A 78  ? 0.65154 0.36840 0.69082 -0.06600 -0.03561 0.04295  85  GLN A CB  
562  C CG  . GLN A 78  ? 0.81669 0.54265 0.87543 -0.08717 -0.03411 0.05663  85  GLN A CG  
563  C CD  . GLN A 78  ? 0.94559 0.71577 1.03222 -0.09118 -0.02559 0.07360  85  GLN A CD  
564  O OE1 . GLN A 78  ? 0.86462 0.63563 0.95570 -0.09336 -0.01640 0.09098  85  GLN A OE1 
565  N NE2 . GLN A 78  ? 0.72966 0.53866 0.83086 -0.09035 -0.02610 0.06761  85  GLN A NE2 
566  N N   . ASP A 79  ? 0.41048 0.16893 0.42989 -0.01990 -0.02622 0.02582  86  ASP A N   
567  C CA  . ASP A 79  ? 0.44808 0.20615 0.45270 0.00016  -0.02374 0.01672  86  ASP A CA  
568  C C   . ASP A 79  ? 0.43140 0.22657 0.44323 0.01460  -0.01657 0.02549  86  ASP A C   
569  O O   . ASP A 79  ? 0.42414 0.22370 0.42895 0.03210  -0.01323 0.02315  86  ASP A O   
570  C CB  . ASP A 79  ? 0.45604 0.22420 0.45961 -0.00433 -0.03008 0.00119  86  ASP A CB  
571  C CG  . ASP A 79  ? 0.61180 0.34112 0.60311 -0.01825 -0.04091 -0.00903 86  ASP A CG  
572  O OD1 . ASP A 79  ? 0.63140 0.32333 0.61247 -0.02323 -0.04219 -0.00561 86  ASP A OD1 
573  O OD2 . ASP A 79  ? 0.58152 0.31940 0.57250 -0.02492 -0.04844 -0.02001 86  ASP A OD2 
574  N N   . ARG A 80  ? 0.33841 0.15972 0.36296 0.00743  -0.01442 0.03633  87  ARG A N   
575  C CA  . ARG A 80  ? 0.29356 0.15006 0.32178 0.01630  -0.01153 0.04322  87  ARG A CA  
576  C C   . ARG A 80  ? 0.30957 0.19159 0.34103 0.01949  -0.01407 0.03223  87  ARG A C   
577  O O   . ARG A 80  ? 0.30043 0.19766 0.33126 0.03207  -0.01351 0.03439  87  ARG A O   
578  C CB  . ARG A 80  ? 0.33759 0.18682 0.35843 0.03328  -0.00827 0.05541  87  ARG A CB  
579  C CG  . ARG A 80  ? 0.29732 0.17913 0.32044 0.03678  -0.00863 0.06668  87  ARG A CG  
580  C CD  . ARG A 80  ? 0.49235 0.36501 0.50939 0.05052  -0.00659 0.08320  87  ARG A CD  
581  N NE  . ARG A 80  ? 0.57689 0.46366 0.59743 0.06844  -0.00766 0.08597  87  ARG A NE  
582  C CZ  . ARG A 80  ? 0.57637 0.44472 0.59343 0.08657  -0.00362 0.09513  87  ARG A CZ  
583  N NH1 . ARG A 80  ? 0.66745 0.49647 0.67373 0.08842  0.00064  0.10152  87  ARG A NH1 
584  N NH2 . ARG A 80  ? 0.51099 0.40096 0.53654 0.10373  -0.00319 0.09956  87  ARG A NH2 
585  N N   . THR A 81  ? 0.25060 0.13901 0.28779 0.00755  -0.01710 0.02228  88  THR A N   
586  C CA  . THR A 81  ? 0.26979 0.17932 0.30914 0.00895  -0.01929 0.01271  88  THR A CA  
587  C C   . THR A 81  ? 0.25471 0.18597 0.30201 -0.00178 -0.01973 0.01143  88  THR A C   
588  O O   . THR A 81  ? 0.25275 0.18111 0.30725 -0.01186 -0.01885 0.01415  88  THR A O   
589  C CB  . THR A 81  ? 0.29766 0.18923 0.33066 0.00971  -0.02243 0.00021  88  THR A CB  
590  O OG1 . THR A 81  ? 0.30132 0.17710 0.33721 -0.00454 -0.02745 -0.00372 88  THR A OG1 
591  C CG2 . THR A 81  ? 0.31359 0.18047 0.33305 0.02498  -0.01908 0.00038  88  THR A CG2 
592  N N   . LEU A 82  ? 0.19276 0.14517 0.23909 0.00084  -0.02053 0.00843  89  LEU A N   
593  C CA  . LEU A 82  ? 0.21273 0.18000 0.26178 -0.00588 -0.02035 0.00428  89  LEU A CA  
594  C C   . LEU A 82  ? 0.21955 0.19086 0.26910 -0.00490 -0.02382 -0.00593 89  LEU A C   
595  O O   . LEU A 82  ? 0.21431 0.19121 0.26059 0.00121  -0.02505 -0.00673 89  LEU A O   
596  C CB  . LEU A 82  ? 0.25670 0.23724 0.29689 -0.00474 -0.01908 0.00941  89  LEU A CB  
597  C CG  . LEU A 82  ? 0.22471 0.21385 0.26084 -0.00844 -0.01725 0.00437  89  LEU A CG  
598  C CD1 . LEU A 82  ? 0.20445 0.19341 0.25009 -0.01259 -0.01087 0.00691  89  LEU A CD1 
599  C CD2 . LEU A 82  ? 0.21918 0.21232 0.23711 -0.00728 -0.01800 0.00757  89  LEU A CD2 
600  N N   . THR A 83  ? 0.18327 0.15381 0.23859 -0.01072 -0.02538 -0.01163 90  THR A N   
601  C CA  . THR A 83  ? 0.20745 0.17908 0.26091 -0.00962 -0.02899 -0.02035 90  THR A CA  
602  C C   . THR A 83  ? 0.19411 0.17966 0.24995 -0.01205 -0.02810 -0.02224 90  THR A C   
603  O O   . THR A 83  ? 0.20794 0.19915 0.27163 -0.01583 -0.02559 -0.01912 90  THR A O   
604  C CB  . THR A 83  ? 0.23033 0.18613 0.28459 -0.01358 -0.03438 -0.02560 90  THR A CB  
605  O OG1 . THR A 83  ? 0.24698 0.18110 0.29278 -0.00965 -0.03441 -0.02504 90  THR A OG1 
606  C CG2 . THR A 83  ? 0.23565 0.19180 0.28326 -0.01109 -0.03808 -0.03374 90  THR A CG2 
607  N N   . ILE A 84  ? 0.17457 0.16507 0.22398 -0.00911 -0.02901 -0.02588 91  ILE A N   
608  C CA  . ILE A 84  ? 0.17352 0.16998 0.22065 -0.01006 -0.02829 -0.02844 91  ILE A CA  
609  C C   . ILE A 84  ? 0.19609 0.19077 0.24395 -0.00916 -0.03197 -0.03384 91  ILE A C   
610  O O   . ILE A 84  ? 0.22143 0.21407 0.26340 -0.00643 -0.03313 -0.03573 91  ILE A O   
611  C CB  . ILE A 84  ? 0.19254 0.19146 0.22897 -0.01016 -0.02834 -0.02754 91  ILE A CB  
612  C CG1 . ILE A 84  ? 0.29900 0.29807 0.32896 -0.01104 -0.02674 -0.02223 91  ILE A CG1 
613  C CG2 . ILE A 84  ? 0.21089 0.20701 0.24019 -0.01053 -0.02765 -0.03130 91  ILE A CG2 
614  C CD1 . ILE A 84  ? 0.28154 0.28382 0.31445 -0.00943 -0.02895 -0.01648 91  ILE A CD1 
615  N N   . VAL A 85  ? 0.15334 0.15099 0.20892 -0.01071 -0.03349 -0.03457 92  VAL A N   
616  C CA  . VAL A 85  ? 0.15636 0.15254 0.21137 -0.01013 -0.03927 -0.03863 92  VAL A CA  
617  C C   . VAL A 85  ? 0.23568 0.23720 0.28937 -0.00677 -0.03720 -0.03824 92  VAL A C   
618  O O   . VAL A 85  ? 0.19949 0.20715 0.25921 -0.00518 -0.03226 -0.03469 92  VAL A O   
619  C CB  . VAL A 85  ? 0.17019 0.16699 0.23687 -0.01564 -0.04622 -0.03805 92  VAL A CB  
620  C CG1 . VAL A 85  ? 0.23297 0.22549 0.29304 -0.01536 -0.05523 -0.04276 92  VAL A CG1 
621  C CG2 . VAL A 85  ? 0.25506 0.23989 0.32100 -0.01973 -0.04758 -0.03778 92  VAL A CG2 
622  N N   . ASP A 86  ? 0.18568 0.18281 0.22963 -0.00419 -0.03952 -0.04097 93  ASP A N   
623  C CA  . ASP A 86  ? 0.17118 0.16897 0.21273 -0.00027 -0.03851 -0.03993 93  ASP A CA  
624  C C   . ASP A 86  ? 0.20658 0.20302 0.24395 0.00177  -0.04527 -0.04125 93  ASP A C   
625  O O   . ASP A 86  ? 0.25310 0.24403 0.28263 0.00073  -0.04918 -0.04437 93  ASP A O   
626  C CB  . ASP A 86  ? 0.18593 0.17518 0.21462 -0.00006 -0.03376 -0.03988 93  ASP A CB  
627  C CG  . ASP A 86  ? 0.25822 0.24434 0.27887 -0.00212 -0.03497 -0.03998 93  ASP A CG  
628  O OD1 . ASP A 86  ? 0.24224 0.22613 0.25783 0.00060  -0.03682 -0.03983 93  ASP A OD1 
629  O OD2 . ASP A 86  ? 0.24661 0.23455 0.26657 -0.00587 -0.03363 -0.03848 93  ASP A OD2 
630  N N   . THR A 87  ? 0.18690 0.18661 0.22678 0.00645  -0.04622 -0.03839 94  THR A N   
631  C CA  . THR A 87  ? 0.16906 0.16787 0.20278 0.00940  -0.05363 -0.03796 94  THR A CA  
632  C C   . THR A 87  ? 0.25239 0.24029 0.27090 0.01395  -0.04906 -0.03621 94  THR A C   
633  O O   . THR A 87  ? 0.21059 0.19753 0.22552 0.01964  -0.05197 -0.03259 94  THR A O   
634  C CB  . THR A 87  ? 0.17992 0.19396 0.23119 0.01157  -0.06025 -0.03295 94  THR A CB  
635  O OG1 . THR A 87  ? 0.18649 0.20667 0.24816 0.01815  -0.05109 -0.02775 94  THR A OG1 
636  C CG2 . THR A 87  ? 0.20176 0.22490 0.26779 0.00288  -0.06798 -0.03359 94  THR A CG2 
637  N N   . GLY A 88  ? 0.21992 0.19998 0.23057 0.01053  -0.04271 -0.03723 95  GLY A N   
638  C CA  . GLY A 88  ? 0.24441 0.21312 0.24249 0.01079  -0.03901 -0.03417 95  GLY A CA  
639  C C   . GLY A 88  ? 0.21110 0.17796 0.19788 0.01227  -0.04022 -0.03208 95  GLY A C   
640  O O   . GLY A 88  ? 0.19874 0.16896 0.18208 0.01533  -0.04566 -0.03430 95  GLY A O   
641  N N   . ILE A 89  ? 0.22761 0.18753 0.20648 0.00939  -0.03534 -0.02719 96  ILE A N   
642  C CA  . ILE A 89  ? 0.20167 0.15953 0.16794 0.01253  -0.03346 -0.02235 96  ILE A CA  
643  C C   . ILE A 89  ? 0.22852 0.19431 0.19204 0.01428  -0.03071 -0.02407 96  ILE A C   
644  O O   . ILE A 89  ? 0.25335 0.21592 0.20103 0.02049  -0.02912 -0.02224 96  ILE A O   
645  C CB  . ILE A 89  ? 0.19811 0.14716 0.16007 0.00703  -0.02819 -0.01396 96  ILE A CB  
646  C CG1 . ILE A 89  ? 0.28471 0.22999 0.23192 0.01186  -0.02485 -0.00619 96  ILE A CG1 
647  C CG2 . ILE A 89  ? 0.22517 0.18249 0.19801 -0.00318 -0.02460 -0.01134 96  ILE A CG2 
648  C CD1 . ILE A 89  ? 0.31300 0.24359 0.25466 0.00686  -0.02179 0.00313  96  ILE A CD1 
649  N N   . GLY A 90  ? 0.21374 0.18720 0.18887 0.01093  -0.02949 -0.02733 97  GLY A N   
650  C CA  . GLY A 90  ? 0.23821 0.21599 0.20965 0.01550  -0.02499 -0.02812 97  GLY A CA  
651  C C   . GLY A 90  ? 0.24428 0.23131 0.21740 0.01564  -0.01483 -0.01780 97  GLY A C   
652  O O   . GLY A 90  ? 0.23431 0.22385 0.21322 0.00846  -0.01328 -0.01020 97  GLY A O   
653  N N   . MET A 91  ? 0.22815 0.21966 0.19657 0.02403  -0.00737 -0.01648 98  MET A N   
654  C CA  . MET A 91  ? 0.22578 0.23157 0.19850 0.02686  0.00479  -0.00367 98  MET A CA  
655  C C   . MET A 91  ? 0.27602 0.27450 0.22517 0.04294  0.01451  -0.00402 98  MET A C   
656  O O   . MET A 91  ? 0.24083 0.22342 0.17337 0.05091  0.01151  -0.01498 98  MET A O   
657  C CB  . MET A 91  ? 0.32299 0.35131 0.32235 0.02158  0.00826  0.00471  98  MET A CB  
658  C CG  . MET A 91  ? 0.25455 0.28521 0.27002 0.00827  -0.00246 0.00140  98  MET A CG  
659  S SD  . MET A 91  ? 0.23720 0.29119 0.27642 0.00741  -0.00128 0.00828  98  MET A SD  
660  C CE  . MET A 91  ? 0.21280 0.24946 0.24273 0.01342  -0.00683 -0.00621 98  MET A CE  
661  N N   . THR A 92  ? 0.23740 0.24463 0.18246 0.04721  0.02635  0.00850  99  THR A N   
662  C CA  . THR A 92  ? 0.26258 0.26389 0.18216 0.06503  0.04012  0.01107  99  THR A CA  
663  C C   . THR A 92  ? 0.26304 0.27995 0.19548 0.07575  0.05281  0.01665  99  THR A C   
664  O O   . THR A 92  ? 0.27382 0.31130 0.23842 0.06750  0.05026  0.02157  99  THR A O   
665  C CB  . THR A 92  ? 0.29361 0.30287 0.20752 0.06629  0.05129  0.02626  99  THR A CB  
666  O OG1 . THR A 92  ? 0.29410 0.33474 0.24452 0.05681  0.05901  0.04388  99  THR A OG1 
667  C CG2 . THR A 92  ? 0.32495 0.31835 0.22731 0.05715  0.03916  0.02310  99  THR A CG2 
668  N N   . LYS A 93  ? 0.23748 0.22556 0.19280 0.06276  -0.01064 -0.01333 100 LYS A N   
669  C CA  . LYS A 93  ? 0.28233 0.26393 0.23697 0.05688  -0.00486 -0.01114 100 LYS A CA  
670  C C   . LYS A 93  ? 0.26973 0.24625 0.23096 0.05397  0.00390  0.00025  100 LYS A C   
671  O O   . LYS A 93  ? 0.23170 0.20773 0.20295 0.04751  0.00604  -0.00100 100 LYS A O   
672  C CB  . LYS A 93  ? 0.32340 0.30739 0.26126 0.06610  -0.00555 -0.01423 100 LYS A CB  
673  C CG  . LYS A 93  ? 0.26144 0.23974 0.19774 0.06624  -0.00396 -0.01830 100 LYS A CG  
674  C CD  . LYS A 93  ? 0.26751 0.25180 0.18705 0.07883  -0.00502 -0.02487 100 LYS A CD  
675  C CE  . LYS A 93  ? 0.36338 0.34048 0.28012 0.08528  -0.00749 -0.03396 100 LYS A CE  
676  N NZ  . LYS A 93  ? 0.38351 0.37981 0.28927 0.10069  -0.00330 -0.03935 100 LYS A NZ  
677  N N   . ALA A 94  ? 0.29414 0.26515 0.24695 0.05743  0.00802  0.01125  101 ALA A N   
678  C CA  . ALA A 94  ? 0.31157 0.27831 0.27009 0.04830  0.01730  0.02122  101 ALA A CA  
679  C C   . ALA A 94  ? 0.33148 0.29377 0.30949 0.04001  0.01517  0.01776  101 ALA A C   
680  O O   . ALA A 94  ? 0.30891 0.27825 0.30007 0.03131  0.02052  0.01780  101 ALA A O   
681  C CB  . ALA A 94  ? 0.36024 0.30968 0.29749 0.04864  0.02069  0.03566  101 ALA A CB  
682  N N   . ASP A 95  ? 0.24836 0.20538 0.22920 0.04405  0.00675  0.01190  102 ASP A N   
683  C CA  . ASP A 95  ? 0.28541 0.24399 0.28350 0.03736  0.00460  0.00535  102 ASP A CA  
684  C C   . ASP A 95  ? 0.24781 0.21925 0.25545 0.02880  0.00571  -0.00078 102 ASP A C   
685  O O   . ASP A 95  ? 0.25083 0.22405 0.26938 0.02136  0.00793  -0.00112 102 ASP A O   
686  C CB  . ASP A 95  ? 0.35313 0.31664 0.35355 0.04595  -0.00485 -0.00532 102 ASP A CB  
687  C CG  . ASP A 95  ? 0.48847 0.42886 0.47643 0.05899  -0.01095 -0.00044 102 ASP A CG  
688  O OD1 . ASP A 95  ? 0.38029 0.29408 0.35983 0.05375  -0.00654 0.01204  102 ASP A OD1 
689  O OD2 . ASP A 95  ? 0.34511 0.29333 0.32994 0.07420  -0.02139 -0.01024 102 ASP A OD2 
690  N N   . LEU A 96  ? 0.21904 0.19517 0.21878 0.02963  0.00246  -0.00587 103 LEU A N   
691  C CA  . LEU A 96  ? 0.25923 0.23328 0.25726 0.02166  0.00052  -0.00954 103 LEU A CA  
692  C C   . LEU A 96  ? 0.25224 0.22405 0.25252 0.02473  0.00328  -0.00521 103 LEU A C   
693  O O   . LEU A 96  ? 0.26019 0.23118 0.26457 0.02012  0.00131  -0.00631 103 LEU A O   
694  C CB  . LEU A 96  ? 0.28884 0.25720 0.27176 0.02066  -0.00442 -0.01501 103 LEU A CB  
695  C CG  . LEU A 96  ? 0.24194 0.22147 0.22423 0.01016  -0.00784 -0.02443 103 LEU A CG  
696  C CD1 . LEU A 96  ? 0.25294 0.22223 0.21841 0.00604  -0.01265 -0.03010 103 LEU A CD1 
697  C CD2 . LEU A 96  ? 0.20340 0.18817 0.18956 -0.00600 -0.00706 -0.02726 103 LEU A CD2 
698  N N   . ILE A 97  ? 0.23117 0.20764 0.22807 0.03335  0.00741  -0.00219 104 ILE A N   
699  C CA  . ILE A 97  ? 0.25730 0.24563 0.26031 0.03788  0.01036  -0.00302 104 ILE A CA  
700  C C   . ILE A 97  ? 0.28235 0.28222 0.30324 0.02860  0.01603  -0.00013 104 ILE A C   
701  O O   . ILE A 97  ? 0.26346 0.27634 0.29451 0.02938  0.01455  -0.00482 104 ILE A O   
702  C CB  . ILE A 97  ? 0.23853 0.24005 0.23452 0.04709  0.01596  -0.00300 104 ILE A CB  
703  C CG1 . ILE A 97  ? 0.30136 0.29005 0.27944 0.05740  0.00803  -0.00984 104 ILE A CG1 
704  C CG2 . ILE A 97  ? 0.21184 0.24136 0.21990 0.05107  0.02105  -0.00773 104 ILE A CG2 
705  C CD1 . ILE A 97  ? 0.27503 0.27683 0.24228 0.06597  0.01335  -0.01016 104 ILE A CD1 
706  N N   . ASN A 98  ? 0.21264 0.20552 0.23573 0.02105  0.02036  0.00599  105 ASN A N   
707  C CA  . ASN A 98  ? 0.25100 0.24613 0.28785 0.00959  0.02465  0.00772  105 ASN A CA  
708  C C   . ASN A 98  ? 0.23626 0.22713 0.28164 0.00628  0.01779  0.00113  105 ASN A C   
709  O O   . ASN A 98  ? 0.27757 0.25707 0.32605 0.00225  0.01641  0.00028  105 ASN A O   
710  C CB  . ASN A 98  ? 0.29021 0.26640 0.31715 0.00442  0.02916  0.01736  105 ASN A CB  
711  C CG  . ASN A 98  ? 0.67182 0.65500 0.70281 -0.01103 0.03978  0.02300  105 ASN A CG  
712  O OD1 . ASN A 98  ? 0.68952 0.67946 0.73680 -0.02273 0.04105  0.01834  105 ASN A OD1 
713  N ND2 . ASN A 98  ? 0.65678 0.64230 0.67202 -0.01375 0.04817  0.03200  105 ASN A ND2 
714  N N   . ASN A 99  ? 0.22245 0.22035 0.26734 0.00951  0.01223  -0.00423 106 ASN A N   
715  C CA  . ASN A 99  ? 0.20427 0.20220 0.25189 0.00457  0.00659  -0.00969 106 ASN A CA  
716  C C   . ASN A 99  ? 0.23258 0.22416 0.27669 0.00129  0.00493  -0.01266 106 ASN A C   
717  O O   . ASN A 99  ? 0.18922 0.18567 0.24179 -0.00331 0.00388  -0.01881 106 ASN A O   
718  C CB  . ASN A 99  ? 0.22165 0.23312 0.28671 -0.00187 0.00810  -0.01385 106 ASN A CB  
719  C CG  . ASN A 99  ? 0.23401 0.26600 0.30705 0.00222  0.00895  -0.01597 106 ASN A CG  
720  O OD1 . ASN A 99  ? 0.22920 0.26276 0.29272 0.01317  0.00157  -0.01827 106 ASN A OD1 
721  N ND2 . ASN A 99  ? 0.20157 0.24935 0.29026 -0.00681 0.01701  -0.01662 106 ASN A ND2 
722  N N   . LEU A 100 ? 0.19834 0.18454 0.23092 0.00478  0.00386  -0.01160 107 LEU A N   
723  C CA  . LEU A 100 ? 0.23389 0.22650 0.26520 0.00274  0.00158  -0.01870 107 LEU A CA  
724  C C   . LEU A 100 ? 0.26519 0.25898 0.30786 0.00818  0.00096  -0.02333 107 LEU A C   
725  O O   . LEU A 100 ? 0.20556 0.21319 0.25494 0.00718  -0.00167 -0.03467 107 LEU A O   
726  C CB  . LEU A 100 ? 0.20495 0.20595 0.22975 -0.00958 -0.00034 -0.02419 107 LEU A CB  
727  C CG  . LEU A 100 ? 0.27684 0.26034 0.28069 -0.01409 -0.00326 -0.01835 107 LEU A CG  
728  C CD1 . LEU A 100 ? 0.27190 0.24495 0.26801 -0.01475 -0.00697 -0.01416 107 LEU A CD1 
729  C CD2 . LEU A 100 ? 0.38255 0.36901 0.37199 -0.02918 -0.00404 -0.02308 107 LEU A CD2 
730  N N   . GLY A 101 ? 0.20486 0.18205 0.24625 0.01387  0.00287  -0.01518 108 GLY A N   
731  C CA  . GLY A 101 ? 0.31307 0.27467 0.35522 0.02083  -0.00087 -0.01724 108 GLY A CA  
732  C C   . GLY A 101 ? 0.29971 0.25558 0.35308 0.01455  -0.00147 -0.02278 108 GLY A C   
733  O O   . GLY A 101 ? 0.34294 0.28259 0.39563 0.02247  -0.00804 -0.02953 108 GLY A O   
734  N N   . THR A 102 ? 0.25149 0.21894 0.31380 0.00296  0.00299  -0.02218 109 THR A N   
735  C CA  . THR A 102 ? 0.21318 0.18058 0.28733 -0.00411 0.00162  -0.03029 109 THR A CA  
736  C C   . THR A 102 ? 0.20112 0.16016 0.27985 -0.01613 0.00754  -0.02260 109 THR A C   
737  O O   . THR A 102 ? 0.25648 0.21899 0.33071 -0.01865 0.01389  -0.01212 109 THR A O   
738  C CB  . THR A 102 ? 0.22907 0.22342 0.30913 -0.00863 0.00029  -0.03902 109 THR A CB  
739  O OG1 . THR A 102 ? 0.24914 0.25259 0.32620 -0.01207 0.00297  -0.03112 109 THR A OG1 
740  C CG2 . THR A 102 ? 0.28940 0.29896 0.36338 -0.00422 -0.00230 -0.04659 109 THR A CG2 
741  N N   . ILE A 103 ? 0.22082 0.17369 0.30931 -0.02495 0.00572  -0.03059 110 ILE A N   
742  C CA  . ILE A 103 ? 0.22268 0.17958 0.32055 -0.04241 0.01200  -0.02801 110 ILE A CA  
743  C C   . ILE A 103 ? 0.24462 0.23996 0.35884 -0.04471 0.01043  -0.03828 110 ILE A C   
744  O O   . ILE A 103 ? 0.20432 0.20726 0.33140 -0.05450 0.00800  -0.04946 110 ILE A O   
745  C CB  . ILE A 103 ? 0.30627 0.22604 0.40109 -0.05443 0.00989  -0.03060 110 ILE A CB  
746  C CG1 . ILE A 103 ? 0.30245 0.21338 0.40106 -0.04469 -0.00124 -0.04789 110 ILE A CG1 
747  C CG2 . ILE A 103 ? 0.41204 0.28717 0.48178 -0.05298 0.01085  -0.01535 110 ILE A CG2 
748  C CD1 . ILE A 103 ? 0.38168 0.25916 0.48087 -0.05874 -0.00534 -0.05598 110 ILE A CD1 
749  N N   . ALA A 104 ? 0.29158 0.18704 0.34714 0.03833  0.02150  0.03211  111 ALA A N   
750  C CA  . ALA A 104 ? 0.22453 0.15681 0.30429 0.05620  0.02266  0.03951  111 ALA A CA  
751  C C   . ALA A 104 ? 0.19679 0.20641 0.30961 0.05169  0.03389  0.03715  111 ALA A C   
752  O O   . ALA A 104 ? 0.20378 0.28101 0.32256 0.04364  0.02819  0.02453  111 ALA A O   
753  C CB  . ALA A 104 ? 0.25010 0.19537 0.29305 0.06359  0.00076  0.04051  111 ALA A CB  
754  N N   . LYS A 105 ? 0.22085 0.23974 0.33685 0.04387  0.04356  0.04040  112 LYS A N   
755  C CA  . LYS A 105 ? 0.19395 0.31219 0.32560 0.02568  0.04784  0.02862  112 LYS A CA  
756  C C   . LYS A 105 ? 0.27835 0.42444 0.42208 -0.02308 0.05828  -0.00175 112 LYS A C   
757  O O   . LYS A 105 ? 0.22642 0.45471 0.37983 -0.03369 0.05198  -0.01400 112 LYS A O   
758  C CB  . LYS A 105 ? 0.19463 0.31825 0.32732 0.02411  0.05903  0.03752  112 LYS A CB  
759  C CG  . LYS A 105 ? 0.27456 0.50972 0.42858 0.00338  0.06500  0.02559  112 LYS A CG  
760  C CD  . LYS A 105 ? 0.23754 0.48370 0.39197 0.00724  0.07697  0.03655  112 LYS A CD  
761  C CE  . LYS A 105 ? 0.54612 0.88733 0.72439 -0.03361 0.08998  0.01891  112 LYS A CE  
762  N NZ  . LYS A 105 ? 0.50636 0.96735 0.70745 -0.02456 0.07759  0.01332  112 LYS A NZ  
763  N N   . SER A 106 ? 0.22793 0.30153 0.36740 -0.05305 0.07310  -0.01408 113 SER A N   
764  C CA  . SER A 106 ? 0.25502 0.34194 0.39848 -0.10033 0.08378  -0.04420 113 SER A CA  
765  C C   . SER A 106 ? 0.25408 0.33409 0.39421 -0.09686 0.07713  -0.05631 113 SER A C   
766  O O   . SER A 106 ? 0.27533 0.40203 0.41747 -0.12852 0.07992  -0.07992 113 SER A O   
767  C CB  . SER A 106 ? 0.37423 0.37546 0.50807 -0.13107 0.10093  -0.05355 113 SER A CB  
768  O OG  . SER A 106 ? 0.34614 0.24715 0.47017 -0.10679 0.09930  -0.04245 113 SER A OG  
769  N N   . GLY A 107 ? 0.23564 0.25997 0.36894 -0.06115 0.06860  -0.04066 114 GLY A N   
770  C CA  . GLY A 107 ? 0.22774 0.25161 0.35757 -0.05705 0.06334  -0.05083 114 GLY A CA  
771  C C   . GLY A 107 ? 0.25416 0.37163 0.38430 -0.04902 0.04829  -0.04989 114 GLY A C   
772  O O   . GLY A 107 ? 0.21623 0.36536 0.34337 -0.06915 0.04846  -0.06993 114 GLY A O   
773  N N   . THR A 108 ? 0.18303 0.34333 0.31384 -0.01863 0.03476  -0.02670 115 THR A N   
774  C CA  . THR A 108 ? 0.18502 0.43614 0.31556 -0.00815 0.01828  -0.02397 115 THR A CA  
775  C C   . THR A 108 ? 0.18340 0.51680 0.32709 -0.04895 0.02350  -0.04755 115 THR A C   
776  O O   . THR A 108 ? 0.21464 0.60337 0.35494 -0.06120 0.01479  -0.05957 115 THR A O   
777  C CB  . THR A 108 ? 0.18634 0.46133 0.31399 0.03473  0.00449  0.00464  115 THR A CB  
778  O OG1 . THR A 108 ? 0.19378 0.39182 0.30324 0.06954  -0.00315 0.02666  115 THR A OG1 
779  C CG2 . THR A 108 ? 0.17884 0.54784 0.30630 0.04836  -0.01398 0.00810  115 THR A CG2 
780  N N   . LYS A 109 ? 0.19652 0.53934 0.35279 -0.07296 0.03706  -0.05379 116 LYS A N   
781  C CA  . LYS A 109 ? 0.21555 0.63477 0.38385 -0.11827 0.04284  -0.07626 116 LYS A CA  
782  C C   . LYS A 109 ? 0.31227 0.71373 0.46908 -0.15667 0.04894  -0.10470 116 LYS A C   
783  O O   . LYS A 109 ? 0.28622 0.74218 0.43174 -0.17094 0.03997  -0.11535 116 LYS A O   
784  C CB  . LYS A 109 ? 0.23388 0.64072 0.41121 -0.14409 0.06016  -0.07928 116 LYS A CB  
785  C CG  . LYS A 109 ? 0.46333 0.87969 0.62834 -0.19323 0.06790  -0.10307 116 LYS A CG  
786  C CD  . LYS A 109 ? 0.38218 0.82120 0.55237 -0.20586 0.07528  -0.09765 116 LYS A CD  
787  C CE  . LYS A 109 ? 0.34686 0.83710 0.50598 -0.24211 0.07435  -0.11464 116 LYS A CE  
788  N NZ  . LYS A 109 ? 0.69488 1.26572 0.85443 -0.23066 0.05676  -0.11517 116 LYS A NZ  
789  N N   . ALA A 110 ? 0.26177 0.56302 0.40637 -0.16388 0.06249  -0.11350 117 ALA A N   
790  C CA  . ALA A 110 ? 0.29436 0.56986 0.42517 -0.19761 0.07140  -0.14249 117 ALA A CA  
791  C C   . ALA A 110 ? 0.27928 0.58201 0.40059 -0.17963 0.05794  -0.14249 117 ALA A C   
792  O O   . ALA A 110 ? 0.33029 0.66246 0.43722 -0.20660 0.05814  -0.16353 117 ALA A O   
793  C CB  . ALA A 110 ? 0.32102 0.48138 0.44280 -0.20193 0.08882  -0.15025 117 ALA A CB  
794  N N   . PHE A 111 ? 0.25395 0.53836 0.37440 -0.13275 0.04567  -0.11678 118 PHE A N   
795  C CA  . PHE A 111 ? 0.23617 0.53814 0.34287 -0.11639 0.03299  -0.11437 118 PHE A CA  
796  C C   . PHE A 111 ? 0.25200 0.65828 0.35667 -0.12522 0.01585  -0.11633 118 PHE A C   
797  O O   . PHE A 111 ? 0.24999 0.68306 0.33982 -0.14570 0.01304  -0.13354 118 PHE A O   
798  C CB  . PHE A 111 ? 0.20614 0.46720 0.30922 -0.06701 0.02166  -0.08342 118 PHE A CB  
799  C CG  . PHE A 111 ? 0.21274 0.48361 0.29757 -0.05038 0.00850  -0.07754 118 PHE A CG  
800  C CD1 . PHE A 111 ? 0.22106 0.48597 0.29435 -0.07552 0.01722  -0.10191 118 PHE A CD1 
801  C CD2 . PHE A 111 ? 0.27582 0.55523 0.35050 -0.00997 -0.01171 -0.04747 118 PHE A CD2 
802  C CE1 . PHE A 111 ? 0.21759 0.49110 0.27125 -0.06272 0.00636  -0.09589 118 PHE A CE1 
803  C CE2 . PHE A 111 ? 0.28003 0.56318 0.33273 0.00234  -0.02426 -0.04053 118 PHE A CE2 
804  C CZ  . PHE A 111 ? 0.20478 0.48756 0.24785 -0.02511 -0.01492 -0.06456 118 PHE A CZ  
805  N N   . MET A 112 ? 0.21978 0.68767 0.33889 -0.10962 0.00426  -0.09908 119 MET A N   
806  C CA  . MET A 112 ? 0.38713 0.92486 0.49119 -0.10401 -0.01169 -0.09301 119 MET A CA  
807  C C   . MET A 112 ? 0.45659 1.02547 0.55178 -0.14881 -0.00258 -0.11719 119 MET A C   
808  O O   . MET A 112 ? 0.34556 0.95732 0.42390 -0.15340 -0.01073 -0.11881 119 MET A O   
809  C CB  . MET A 112 ? 0.43874 1.00489 0.54852 -0.06806 -0.02153 -0.06667 119 MET A CB  
810  C CG  . MET A 112 ? 0.19961 0.73538 0.29218 -0.01865 -0.03561 -0.03910 119 MET A CG  
811  S SD  . MET A 112 ? 0.65064 1.18039 0.74423 0.02010  -0.03741 -0.01336 119 MET A SD  
812  C CE  . MET A 112 ? 0.31328 0.75842 0.37493 0.06165  -0.04498 0.01060  119 MET A CE  
813  N N   . GLU A 113 ? 0.30919 0.85064 0.41162 -0.18145 0.01510  -0.13400 120 GLU A N   
814  C CA  . GLU A 113 ? 0.48521 1.04283 0.57063 -0.22388 0.02420  -0.15664 120 GLU A CA  
815  C C   . GLU A 113 ? 0.49251 1.01552 0.55491 -0.24233 0.03154  -0.17684 120 GLU A C   
816  O O   . GLU A 113 ? 0.52289 1.07966 0.56636 -0.26507 0.03154  -0.18829 120 GLU A O   
817  C CB  . GLU A 113 ? 0.47031 0.99246 0.55987 -0.25227 0.04149  -0.16755 120 GLU A CB  
818  C CG  . GLU A 113 ? 0.66177 1.22361 0.77197 -0.23998 0.03725  -0.15000 120 GLU A CG  
819  C CD  . GLU A 113 ? 0.81842 1.33322 0.92854 -0.26816 0.05513  -0.15909 120 GLU A CD  
820  O OE1 . GLU A 113 ? 0.71486 1.14700 0.81263 -0.28262 0.06972  -0.17236 120 GLU A OE1 
821  O OE2 . GLU A 113 ? 0.77645 1.33326 0.89619 -0.27395 0.05488  -0.15223 120 GLU A OE2 
822  N N   . ALA A 114 ? 0.37641 0.83223 0.44068 -0.23246 0.03914  -0.18098 121 ALA A N   
823  C CA  . ALA A 114 ? 0.37209 0.79484 0.41471 -0.24453 0.04750  -0.19929 121 ALA A CA  
824  C C   . ALA A 114 ? 0.40040 0.87750 0.43111 -0.22880 0.02953  -0.18860 121 ALA A C   
825  O O   . ALA A 114 ? 0.53213 1.01863 0.54093 -0.24872 0.03422  -0.20226 121 ALA A O   
826  C CB  . ALA A 114 ? 0.37343 0.71192 0.42328 -0.23257 0.06002  -0.20420 121 ALA A CB  
827  N N   . LEU A 115 ? 0.36900 0.87667 0.41109 -0.19121 0.00963  -0.16149 122 LEU A N   
828  C CA  . LEU A 115 ? 0.32009 0.86290 0.34598 -0.17039 -0.00723 -0.14563 122 LEU A CA  
829  C C   . LEU A 115 ? 0.48885 1.09258 0.50459 -0.18873 -0.01111 -0.14786 122 LEU A C   
830  O O   . LEU A 115 ? 0.47893 1.09325 0.47573 -0.19987 -0.01237 -0.15316 122 LEU A O   
831  C CB  . LEU A 115 ? 0.33406 0.88236 0.36834 -0.12224 -0.02541 -0.11248 122 LEU A CB  
832  C CG  . LEU A 115 ? 0.24406 0.73637 0.28162 -0.09779 -0.02763 -0.10356 122 LEU A CG  
833  C CD1 . LEU A 115 ? 0.26763 0.75285 0.30372 -0.04849 -0.04328 -0.06715 122 LEU A CD1 
834  C CD2 . LEU A 115 ? 0.25816 0.72148 0.27275 -0.10576 -0.02489 -0.11438 122 LEU A CD2 
835  N N   . GLN A 116 ? 0.50190 1.14740 0.53095 -0.19309 -0.01298 -0.14356 123 GLN A N   
836  C CA  . GLN A 116 ? 0.52741 1.23401 0.54930 -0.21374 -0.01656 -0.14717 123 GLN A CA  
837  C C   . GLN A 116 ? 0.62899 1.32240 0.63387 -0.26235 0.00014  -0.17637 123 GLN A C   
838  O O   . GLN A 116 ? 0.66536 1.40662 0.66066 -0.28454 -0.00263 -0.18114 123 GLN A O   
839  C CB  . GLN A 116 ? 0.53647 1.29361 0.57734 -0.20540 -0.02210 -0.13530 123 GLN A CB  
840  C CG  . GLN A 116 ? 0.67533 1.45713 0.72551 -0.15699 -0.03888 -0.10574 123 GLN A CG  
841  C CD  . GLN A 116 ? 0.86496 1.70824 0.93134 -0.15115 -0.04314 -0.09680 123 GLN A CD  
842  O OE1 . GLN A 116 ? 1.02685 1.89680 1.09909 -0.18434 -0.03461 -0.11129 123 GLN A OE1 
843  N NE2 . GLN A 116 ? 0.81749 1.67864 0.88916 -0.10943 -0.05527 -0.07349 123 GLN A NE2 
844  N N   . ALA A 117 ? 0.69560 1.32061 0.69539 -0.27786 0.01791  -0.19526 124 ALA A N   
845  C CA  . ALA A 117 ? 0.63363 1.22723 0.61238 -0.31880 0.03702  -0.22258 124 ALA A CA  
846  C C   . ALA A 117 ? 0.81755 1.36914 0.77852 -0.31983 0.04508  -0.23371 124 ALA A C   
847  O O   . ALA A 117 ? 0.77156 1.27290 0.71713 -0.34467 0.06528  -0.25637 124 ALA A O   
848  C CB  . ALA A 117 ? 0.53865 1.07575 0.52210 -0.33531 0.05492  -0.23603 124 ALA A CB  
849  N N   . GLY A 118 ? 0.57812 1.14560 0.53959 -0.29162 0.03035  -0.21699 125 GLY A N   
850  C CA  . GLY A 118 ? 0.52544 1.06548 0.46859 -0.29364 0.03586  -0.22496 125 GLY A CA  
851  C C   . GLY A 118 ? 0.54013 1.02854 0.48970 -0.26620 0.03778  -0.22002 125 GLY A C   
852  O O   . GLY A 118 ? 0.48011 0.95593 0.41554 -0.26090 0.03777  -0.21990 125 GLY A O   
853  N N   . ALA A 119 ? 0.41774 0.87550 0.38750 -0.25003 0.03939  -0.21562 126 ALA A N   
854  C CA  . ALA A 119 ? 0.38755 0.79409 0.36386 -0.22555 0.04122  -0.21174 126 ALA A CA  
855  C C   . ALA A 119 ? 0.35458 0.79013 0.32572 -0.19208 0.01721  -0.18333 126 ALA A C   
856  O O   . ALA A 119 ? 0.35212 0.84036 0.32131 -0.18120 -0.00063 -0.16333 126 ALA A O   
857  C CB  . ALA A 119 ? 0.39720 0.76382 0.39837 -0.21690 0.04674  -0.21098 126 ALA A CB  
858  N N   . ASP A 120 ? 0.35588 0.74843 0.32310 -0.17317 0.01830  -0.17997 127 ASP A N   
859  C CA  . ASP A 120 ? 0.35930 0.76101 0.31594 -0.13890 -0.00293 -0.14929 127 ASP A CA  
860  C C   . ASP A 120 ? 0.33974 0.69554 0.31029 -0.10777 -0.00532 -0.13318 127 ASP A C   
861  O O   . ASP A 120 ? 0.29126 0.59486 0.28425 -0.10960 0.01425  -0.14233 127 ASP A O   
862  C CB  . ASP A 120 ? 0.36112 0.75109 0.29367 -0.14369 0.00105  -0.15151 127 ASP A CB  
863  C CG  . ASP A 120 ? 0.51998 0.85506 0.45180 -0.15278 0.02522  -0.17566 127 ASP A CG  
864  O OD1 . ASP A 120 ? 0.51346 0.83019 0.45124 -0.17939 0.04781  -0.20395 127 ASP A OD1 
865  O OD2 . ASP A 120 ? 0.45286 0.75827 0.37905 -0.13037 0.02326  -0.16395 127 ASP A OD2 
866  N N   . ILE A 121 ? 0.28120 0.64061 0.23941 -0.07416 -0.02668 -0.10113 128 ILE A N   
867  C CA  . ILE A 121 ? 0.26888 0.57795 0.24139 -0.03773 -0.03002 -0.07354 128 ILE A CA  
868  C C   . ILE A 121 ? 0.31179 0.54920 0.29520 -0.03578 -0.00873 -0.07992 128 ILE A C   
869  O O   . ILE A 121 ? 0.27810 0.46636 0.28204 -0.01682 -0.00371 -0.06730 128 ILE A O   
870  C CB  . ILE A 121 ? 0.28295 0.59325 0.23474 -0.00467 -0.05367 -0.03749 128 ILE A CB  
871  C CG1 . ILE A 121 ? 0.37493 0.71283 0.33593 0.00419  -0.06043 -0.02542 128 ILE A CG1 
872  C CG2 . ILE A 121 ? 0.30356 0.55249 0.25679 0.02743  -0.05754 -0.01149 128 ILE A CG2 
873  C CD1 . ILE A 121 ? 0.39571 0.70330 0.34114 0.02463  -0.07098 -0.00154 128 ILE A CD1 
874  N N   . SER A 122 ? 0.33419 0.56611 0.30513 -0.05546 0.00487  -0.10050 129 SER A N   
875  C CA  . SER A 122 ? 0.38422 0.55586 0.36990 -0.05049 0.02552  -0.10692 129 SER A CA  
876  C C   . SER A 122 ? 0.31392 0.44174 0.33004 -0.05761 0.04691  -0.12499 129 SER A C   
877  O O   . SER A 122 ? 0.35678 0.42991 0.39154 -0.04467 0.06005  -0.12368 129 SER A O   
878  C CB  . SER A 122 ? 0.30094 0.48233 0.26759 -0.07141 0.03926  -0.12935 129 SER A CB  
879  O OG  . SER A 122 ? 0.35924 0.55114 0.32525 -0.10434 0.05831  -0.16672 129 SER A OG  
880  N N   . MET A 123 ? 0.26844 0.41894 0.28885 -0.07881 0.04972  -0.14101 130 MET A N   
881  C CA  . MET A 123 ? 0.28312 0.38899 0.32468 -0.09060 0.06896  -0.15859 130 MET A CA  
882  C C   . MET A 123 ? 0.29540 0.37387 0.35654 -0.06762 0.06087  -0.13304 130 MET A C   
883  O O   . MET A 123 ? 0.29238 0.33328 0.36761 -0.07830 0.07420  -0.14407 130 MET A O   
884  C CB  . MET A 123 ? 0.31560 0.45825 0.34717 -0.13082 0.07604  -0.18859 130 MET A CB  
885  C CG  . MET A 123 ? 0.44121 0.62576 0.44493 -0.15364 0.07701  -0.20875 130 MET A CG  
886  S SD  . MET A 123 ? 0.51027 0.71249 0.50073 -0.20023 0.09286  -0.24208 130 MET A SD  
887  C CE  . MET A 123 ? 0.50750 0.62754 0.51925 -0.19973 0.11680  -0.24985 130 MET A CE  
888  N N   . ILE A 124 ? 0.22496 0.31577 0.28224 -0.03721 0.03972  -0.09955 131 ILE A N   
889  C CA  . ILE A 124 ? 0.24371 0.31727 0.31260 -0.01541 0.03020  -0.07464 131 ILE A CA  
890  C C   . ILE A 124 ? 0.24882 0.24484 0.33726 -0.00831 0.04477  -0.07381 131 ILE A C   
891  O O   . ILE A 124 ? 0.22734 0.20380 0.32607 -0.00874 0.04726  -0.06901 131 ILE A O   
892  C CB  . ILE A 124 ? 0.24813 0.33451 0.30169 0.01829  0.00597  -0.03997 131 ILE A CB  
893  C CG1 . ILE A 124 ? 0.27705 0.34871 0.33752 0.04120  -0.00315 -0.01587 131 ILE A CG1 
894  C CG2 . ILE A 124 ? 0.24766 0.29102 0.29521 0.03405  0.00546  -0.02837 131 ILE A CG2 
895  C CD1 . ILE A 124 ? 0.28029 0.36521 0.31915 0.07429  -0.02763 0.01617  131 ILE A CD1 
896  N N   . GLY A 125 ? 0.27195 0.22479 0.36577 -0.00171 0.05434  -0.07794 132 GLY A N   
897  C CA  . GLY A 125 ? 0.27168 0.16918 0.37293 0.00691  0.05774  -0.06517 132 GLY A CA  
898  C C   . GLY A 125 ? 0.34720 0.23204 0.45117 -0.01411 0.07071  -0.08123 132 GLY A C   
899  O O   . GLY A 125 ? 0.33811 0.20482 0.43145 -0.00614 0.06119  -0.06196 132 GLY A O   
900  N N   . GLN A 126 ? 0.27414 0.17505 0.37965 -0.04357 0.08822  -0.11802 133 GLN A N   
901  C CA  . GLN A 126 ? 0.31750 0.20584 0.41865 -0.06390 0.09892  -0.12997 133 GLN A CA  
902  C C   . GLN A 126 ? 0.35647 0.24504 0.45972 -0.07121 0.09527  -0.12392 133 GLN A C   
903  O O   . GLN A 126 ? 0.36623 0.23770 0.46210 -0.08411 0.10134  -0.12780 133 GLN A O   
904  C CB  . GLN A 126 ? 0.38316 0.29896 0.47313 -0.09756 0.11347  -0.16608 133 GLN A CB  
905  C CG  . GLN A 126 ? 0.42940 0.33713 0.51635 -0.09310 0.12242  -0.17423 133 GLN A CG  
906  C CD  . GLN A 126 ? 0.54284 0.48328 0.61162 -0.12608 0.13420  -0.20659 133 GLN A CD  
907  O OE1 . GLN A 126 ? 0.72430 0.69813 0.78365 -0.13117 0.13325  -0.21736 133 GLN A OE1 
908  N NE2 . GLN A 126 ? 0.55547 0.48898 0.61355 -0.14941 0.14311  -0.21982 133 GLN A NE2 
909  N N   . PHE A 127 ? 0.31980 0.22576 0.43297 -0.06312 0.08561  -0.11551 134 PHE A N   
910  C CA  . PHE A 127 ? 0.28372 0.20472 0.40091 -0.06920 0.08146  -0.10590 134 PHE A CA  
911  C C   . PHE A 127 ? 0.39166 0.27512 0.51112 -0.03414 0.07035  -0.07055 134 PHE A C   
912  O O   . PHE A 127 ? 0.30620 0.20238 0.42942 -0.03246 0.06686  -0.05903 134 PHE A O   
913  C CB  . PHE A 127 ? 0.25011 0.26663 0.36171 -0.07600 0.06787  -0.10376 134 PHE A CB  
914  C CG  . PHE A 127 ? 0.27599 0.33787 0.37838 -0.11185 0.07431  -0.13464 134 PHE A CG  
915  C CD1 . PHE A 127 ? 0.40502 0.47733 0.50596 -0.15261 0.08627  -0.15833 134 PHE A CD1 
916  C CD2 . PHE A 127 ? 0.30508 0.39335 0.39599 -0.10799 0.06899  -0.14051 134 PHE A CD2 
917  C CE1 . PHE A 127 ? 0.36382 0.47332 0.45146 -0.18849 0.09155  -0.18737 134 PHE A CE1 
918  C CE2 . PHE A 127 ? 0.30165 0.42773 0.37925 -0.14259 0.07501  -0.16947 134 PHE A CE2 
919  C CZ  . PHE A 127 ? 0.33535 0.47141 0.41104 -0.18278 0.08593  -0.19319 134 PHE A CZ  
920  N N   . GLY A 128 ? 0.30285 0.17318 0.40164 -0.00870 0.05498  -0.04604 135 GLY A N   
921  C CA  . GLY A 128 ? 0.30430 0.17029 0.37895 0.00956  0.03622  -0.01879 135 GLY A CA  
922  C C   . GLY A 128 ? 0.27033 0.15414 0.33411 0.02621  0.02267  -0.00143 135 GLY A C   
923  O O   . GLY A 128 ? 0.33257 0.21886 0.39118 0.03046  0.01837  0.01076  135 GLY A O   
924  N N   . VAL A 129 ? 0.24078 0.14097 0.31128 0.03590  0.02034  -0.00192 136 VAL A N   
925  C CA  . VAL A 129 ? 0.20323 0.12453 0.24576 0.05387  0.00078  0.01274  136 VAL A CA  
926  C C   . VAL A 129 ? 0.21979 0.15064 0.25211 0.05988  -0.00850 0.01450  136 VAL A C   
927  O O   . VAL A 129 ? 0.20250 0.16081 0.24154 0.06103  -0.02185 0.02137  136 VAL A O   
928  C CB  . VAL A 129 ? 0.26492 0.22965 0.34787 0.06807  0.00532  0.02119  136 VAL A CB  
929  C CG1 . VAL A 129 ? 0.24719 0.19804 0.34174 0.06120  0.01545  0.02281  136 VAL A CG1 
930  C CG2 . VAL A 129 ? 0.24082 0.26516 0.33621 0.04143  0.01301  -0.00504 136 VAL A CG2 
931  N N   . GLY A 130 ? 0.24497 0.21599 0.25177 -0.03925 -0.00668 -0.05899 137 GLY A N   
932  C CA  . GLY A 130 ? 0.19318 0.17287 0.19700 -0.02657 -0.00496 -0.05988 137 GLY A CA  
933  C C   . GLY A 130 ? 0.22990 0.22048 0.23990 -0.01898 -0.00183 -0.04960 137 GLY A C   
934  O O   . GLY A 130 ? 0.22426 0.22773 0.23344 -0.01218 -0.00098 -0.04743 137 GLY A O   
935  N N   . PHE A 131 ? 0.21493 0.19963 0.22982 -0.02048 -0.00054 -0.04311 138 PHE A N   
936  C CA  . PHE A 131 ? 0.19129 0.18241 0.21051 -0.01396 0.00095  -0.03573 138 PHE A CA  
937  C C   . PHE A 131 ? 0.18035 0.18982 0.20129 -0.01121 -0.00025 -0.03367 138 PHE A C   
938  O O   . PHE A 131 ? 0.20094 0.21230 0.22207 -0.00488 0.00008  -0.02898 138 PHE A O   
939  C CB  . PHE A 131 ? 0.23802 0.22384 0.26004 -0.01610 0.00164  -0.03124 138 PHE A CB  
940  C CG  . PHE A 131 ? 0.23612 0.22874 0.26095 -0.01025 0.00156  -0.02677 138 PHE A CG  
941  C CD1 . PHE A 131 ? 0.21581 0.20183 0.24127 -0.00514 0.00141  -0.02412 138 PHE A CD1 
942  C CD2 . PHE A 131 ? 0.21713 0.22338 0.24385 -0.00965 0.00109  -0.02597 138 PHE A CD2 
943  C CE1 . PHE A 131 ? 0.17515 0.16172 0.20167 -0.00115 -0.00016 -0.02160 138 PHE A CE1 
944  C CE2 . PHE A 131 ? 0.17291 0.18034 0.19965 -0.00205 0.00014  -0.02401 138 PHE A CE2 
945  C CZ  . PHE A 131 ? 0.21168 0.20617 0.23760 0.00140  -0.00097 -0.02227 138 PHE A CZ  
946  N N   . TYR A 132 ? 0.19116 0.21461 0.21357 -0.01614 -0.00209 -0.03624 139 TYR A N   
947  C CA  . TYR A 132 ? 0.18332 0.22644 0.20750 -0.01082 -0.00374 -0.03367 139 TYR A CA  
948  C C   . TYR A 132 ? 0.22243 0.27282 0.24157 -0.00577 -0.00502 -0.03362 139 TYR A C   
949  O O   . TYR A 132 ? 0.21754 0.27995 0.23632 0.00147  -0.00656 -0.02892 139 TYR A O   
950  C CB  . TYR A 132 ? 0.15526 0.21859 0.18426 -0.01768 -0.00542 -0.03622 139 TYR A CB  
951  C CG  . TYR A 132 ? 0.17970 0.24052 0.21289 -0.02196 -0.00305 -0.03359 139 TYR A CG  
952  C CD1 . TYR A 132 ? 0.16877 0.23653 0.20387 -0.01286 -0.00178 -0.02957 139 TYR A CD1 
953  C CD2 . TYR A 132 ? 0.20481 0.25396 0.23797 -0.03408 -0.00223 -0.03491 139 TYR A CD2 
954  C CE1 . TYR A 132 ? 0.20378 0.27300 0.24070 -0.01556 0.00084  -0.02728 139 TYR A CE1 
955  C CE2 . TYR A 132 ? 0.24165 0.29012 0.27705 -0.03797 0.00041  -0.03013 139 TYR A CE2 
956  C CZ  . TYR A 132 ? 0.22706 0.28822 0.26429 -0.02856 0.00226  -0.02646 139 TYR A CZ  
957  O OH  . TYR A 132 ? 0.20235 0.26665 0.23993 -0.03136 0.00526  -0.02192 139 TYR A OH  
958  N N   . SER A 133 ? 0.15985 0.20344 0.17374 -0.00766 -0.00433 -0.03825 140 SER A N   
959  C CA  . SER A 133 ? 0.20855 0.26125 0.21612 -0.00169 -0.00424 -0.03660 140 SER A CA  
960  C C   . SER A 133 ? 0.16594 0.21329 0.17441 0.00477  -0.00191 -0.02572 140 SER A C   
961  O O   . SER A 133 ? 0.18779 0.24466 0.19133 0.00935  -0.00160 -0.02007 140 SER A O   
962  C CB  . SER A 133 ? 0.20903 0.25668 0.20959 -0.00273 -0.00325 -0.04516 140 SER A CB  
963  O OG  . SER A 133 ? 0.20359 0.23566 0.20563 -0.00032 0.00046  -0.04321 140 SER A OG  
964  N N   . ALA A 134 ? 0.18891 0.22156 0.20284 0.00417  -0.00078 -0.02225 141 ALA A N   
965  C CA  . ALA A 134 ? 0.17394 0.19910 0.18926 0.00760  -0.00041 -0.01267 141 ALA A CA  
966  C C   . ALA A 134 ? 0.22104 0.25196 0.23331 0.01356  -0.00310 -0.00606 141 ALA A C   
967  O O   . ALA A 134 ? 0.20959 0.23609 0.21931 0.01572  -0.00306 0.00353  141 ALA A O   
968  C CB  . ALA A 134 ? 0.15395 0.16434 0.17432 0.00613  -0.00085 -0.01276 141 ALA A CB  
969  N N   . TYR A 135 ? 0.19911 0.24101 0.21173 0.01635  -0.00560 -0.00992 142 TYR A N   
970  C CA  . TYR A 135 ? 0.16259 0.21075 0.17223 0.02562  -0.00875 -0.00376 142 TYR A CA  
971  C C   . TYR A 135 ? 0.18844 0.25312 0.19125 0.02872  -0.00974 0.00055  142 TYR A C   
972  O O   . TYR A 135 ? 0.20952 0.28108 0.20844 0.03804  -0.01286 0.00712  142 TYR A O   
973  C CB  . TYR A 135 ? 0.18590 0.24684 0.19991 0.02907  -0.01071 -0.00927 142 TYR A CB  
974  C CG  . TYR A 135 ? 0.22355 0.26848 0.24091 0.02984  -0.00986 -0.01104 142 TYR A CG  
975  C CD1 . TYR A 135 ? 0.20571 0.23479 0.21991 0.03983  -0.01214 -0.00681 142 TYR A CD1 
976  C CD2 . TYR A 135 ? 0.16262 0.20531 0.18427 0.02093  -0.00733 -0.01690 142 TYR A CD2 
977  C CE1 . TYR A 135 ? 0.20620 0.22117 0.22123 0.04122  -0.01213 -0.01055 142 TYR A CE1 
978  C CE2 . TYR A 135 ? 0.16382 0.19465 0.18660 0.02233  -0.00674 -0.01824 142 TYR A CE2 
979  C CZ  . TYR A 135 ? 0.23257 0.25114 0.25191 0.03254  -0.00922 -0.01609 142 TYR A CZ  
980  O OH  . TYR A 135 ? 0.20516 0.21311 0.22359 0.03462  -0.00942 -0.01959 142 TYR A OH  
981  N N   . LEU A 136 ? 0.21347 0.28491 0.21324 0.02302  -0.00734 -0.00307 143 LEU A N   
982  C CA  . LEU A 136 ? 0.22816 0.31489 0.21894 0.02667  -0.00740 0.00238  143 LEU A CA  
983  C C   . LEU A 136 ? 0.21100 0.28600 0.19838 0.02959  -0.00568 0.01813  143 LEU A C   
984  O O   . LEU A 136 ? 0.24582 0.33114 0.22497 0.03539  -0.00683 0.02823  143 LEU A O   
985  C CB  . LEU A 136 ? 0.19429 0.28974 0.18104 0.02163  -0.00481 -0.00711 143 LEU A CB  
986  C CG  . LEU A 136 ? 0.19396 0.29964 0.18070 0.01673  -0.00797 -0.02257 143 LEU A CG  
987  C CD1 . LEU A 136 ? 0.22632 0.32923 0.20751 0.01352  -0.00557 -0.03317 143 LEU A CD1 
988  C CD2 . LEU A 136 ? 0.20951 0.34100 0.19134 0.02069  -0.01322 -0.02308 143 LEU A CD2 
989  N N   . VAL A 137 ? 0.19548 0.24954 0.18879 0.02465  -0.00350 0.02129  144 VAL A N   
990  C CA  . VAL A 137 ? 0.20905 0.25188 0.20067 0.02260  -0.00202 0.03632  144 VAL A CA  
991  C C   . VAL A 137 ? 0.26394 0.27810 0.25976 0.02200  -0.00528 0.04062  144 VAL A C   
992  O O   . VAL A 137 ? 0.27388 0.27267 0.26740 0.01966  -0.00624 0.05402  144 VAL A O   
993  C CB  . VAL A 137 ? 0.22371 0.27469 0.21814 0.01515  0.00366  0.03686  144 VAL A CB  
994  C CG1 . VAL A 137 ? 0.21584 0.29380 0.20254 0.01832  0.00659  0.03151  144 VAL A CG1 
995  C CG2 . VAL A 137 ? 0.19200 0.23252 0.19604 0.01005  0.00457  0.02647  144 VAL A CG2 
996  N N   . ALA A 138 ? 0.24006 0.24624 0.24086 0.02368  -0.00734 0.02953  145 ALA A N   
997  C CA  . ALA A 138 ? 0.21768 0.19758 0.22086 0.02396  -0.01067 0.02971  145 ALA A CA  
998  C C   . ALA A 138 ? 0.25732 0.23227 0.25639 0.03682  -0.01510 0.02736  145 ALA A C   
999  O O   . ALA A 138 ? 0.25850 0.25391 0.25904 0.04185  -0.01483 0.01941  145 ALA A O   
1000 C CB  . ALA A 138 ? 0.20221 0.17903 0.21293 0.01753  -0.00925 0.01922  145 ALA A CB  
1001 N N   . GLU A 139 ? 0.24655 0.19458 0.24058 0.04214  -0.01951 0.03401  146 GLU A N   
1002 C CA  . GLU A 139 ? 0.26701 0.20833 0.25672 0.05776  -0.02383 0.02962  146 GLU A CA  
1003 C C   . GLU A 139 ? 0.29929 0.23335 0.29268 0.05859  -0.02445 0.01657  146 GLU A C   
1004 O O   . GLU A 139 ? 0.30409 0.24613 0.29608 0.07163  -0.02589 0.00955  146 GLU A O   
1005 C CB  . GLU A 139 ? 0.36941 0.27935 0.34923 0.06627  -0.02930 0.04105  146 GLU A CB  
1006 C CG  . GLU A 139 ? 0.40781 0.28011 0.38670 0.05616  -0.03231 0.04355  146 GLU A CG  
1007 C CD  . GLU A 139 ? 0.80315 0.64221 0.77218 0.05788  -0.03719 0.05954  146 GLU A CD  
1008 O OE1 . GLU A 139 ? 0.59844 0.44497 0.56040 0.06889  -0.03777 0.06991  146 GLU A OE1 
1009 O OE2 . GLU A 139 ? 0.77934 0.58423 0.74727 0.04760  -0.04111 0.06221  146 GLU A OE2 
1010 N N   . LYS A 140 ? 0.25979 0.18303 0.25766 0.04581  -0.02331 0.01364  147 LYS A N   
1011 C CA  . LYS A 140 ? 0.26274 0.18094 0.26258 0.04580  -0.02401 0.00212  147 LYS A CA  
1012 C C   . LYS A 140 ? 0.25232 0.17916 0.25985 0.03105  -0.02032 0.00036  147 LYS A C   
1013 O O   . LYS A 140 ? 0.24359 0.16790 0.25400 0.02109  -0.01922 0.00796  147 LYS A O   
1014 C CB  . LYS A 140 ? 0.29419 0.17685 0.28690 0.05022  -0.03057 0.00020  147 LYS A CB  
1015 C CG  . LYS A 140 ? 0.26237 0.14005 0.25446 0.05097  -0.03216 -0.01258 147 LYS A CG  
1016 C CD  . LYS A 140 ? 0.36070 0.20151 0.34228 0.05922  -0.04006 -0.01715 147 LYS A CD  
1017 C CE  . LYS A 140 ? 0.57464 0.39495 0.55726 0.04489  -0.04444 -0.02076 147 LYS A CE  
1018 N NZ  . LYS A 140 ? 0.53310 0.30891 0.50608 0.04585  -0.05351 -0.02045 147 LYS A NZ  
1019 N N   . VAL A 141 ? 0.21129 0.15066 0.22192 0.03055  -0.01811 -0.00848 148 VAL A N   
1020 C CA  . VAL A 141 ? 0.19915 0.14437 0.21569 0.01969  -0.01537 -0.01013 148 VAL A CA  
1021 C C   . VAL A 141 ? 0.24964 0.18710 0.26466 0.02055  -0.01775 -0.01769 148 VAL A C   
1022 O O   . VAL A 141 ? 0.19867 0.14151 0.20980 0.02905  -0.01782 -0.02372 148 VAL A O   
1023 C CB  . VAL A 141 ? 0.19325 0.16073 0.21339 0.01693  -0.01034 -0.01183 148 VAL A CB  
1024 C CG1 . VAL A 141 ? 0.21492 0.18373 0.23932 0.00912  -0.00819 -0.01346 148 VAL A CG1 
1025 C CG2 . VAL A 141 ? 0.20688 0.18440 0.22638 0.01686  -0.00881 -0.00641 148 VAL A CG2 
1026 N N   . THR A 142 ? 0.20038 0.12929 0.21835 0.01221  -0.01980 -0.01728 149 THR A N   
1027 C CA  . THR A 142 ? 0.19049 0.11510 0.20640 0.01202  -0.02283 -0.02450 149 THR A CA  
1028 C C   . THR A 142 ? 0.22217 0.16133 0.24408 0.00556  -0.01958 -0.02337 149 THR A C   
1029 O O   . THR A 142 ? 0.27116 0.21465 0.29971 -0.00127 -0.01822 -0.01789 149 THR A O   
1030 C CB  . THR A 142 ? 0.20503 0.10688 0.21882 0.00763  -0.03028 -0.02597 149 THR A CB  
1031 O OG1 . THR A 142 ? 0.29119 0.17286 0.29791 0.01469  -0.03382 -0.02562 149 THR A OG1 
1032 C CG2 . THR A 142 ? 0.27579 0.17511 0.28480 0.00923  -0.03459 -0.03590 149 THR A CG2 
1033 N N   . VAL A 143 ? 0.17850 0.12625 0.19744 0.00886  -0.01811 -0.02767 150 VAL A N   
1034 C CA  . VAL A 143 ? 0.19248 0.14999 0.21488 0.00507  -0.01567 -0.02564 150 VAL A CA  
1035 C C   . VAL A 143 ? 0.25137 0.20815 0.26997 0.00582  -0.02010 -0.02987 150 VAL A C   
1036 O O   . VAL A 143 ? 0.24204 0.20071 0.25279 0.01158  -0.02065 -0.03464 150 VAL A O   
1037 C CB  . VAL A 143 ? 0.20381 0.17132 0.22505 0.00635  -0.01013 -0.02422 150 VAL A CB  
1038 C CG1 . VAL A 143 ? 0.21749 0.18784 0.23974 0.00413  -0.00864 -0.02143 150 VAL A CG1 
1039 C CG2 . VAL A 143 ? 0.22805 0.19844 0.25227 0.00504  -0.00712 -0.02192 150 VAL A CG2 
1040 N N   . ILE A 144 ? 0.19068 0.14887 0.21471 0.00056  -0.02334 -0.02833 151 ILE A N   
1041 C CA  . ILE A 144 ? 0.19875 0.16097 0.21983 0.00071  -0.02848 -0.03207 151 ILE A CA  
1042 C C   . ILE A 144 ? 0.23629 0.21091 0.25922 0.00263  -0.02515 -0.02680 151 ILE A C   
1043 O O   . ILE A 144 ? 0.20013 0.17894 0.23055 0.00111  -0.02201 -0.02166 151 ILE A O   
1044 C CB  . ILE A 144 ? 0.24314 0.20200 0.27028 -0.00746 -0.03577 -0.03369 151 ILE A CB  
1045 C CG1 . ILE A 144 ? 0.36052 0.30074 0.38734 -0.01131 -0.03832 -0.03480 151 ILE A CG1 
1046 C CG2 . ILE A 144 ? 0.29954 0.26181 0.32075 -0.00681 -0.04311 -0.04089 151 ILE A CG2 
1047 C CD1 . ILE A 144 ? 0.31024 0.23423 0.32464 -0.00426 -0.04229 -0.04415 151 ILE A CD1 
1048 N N   . THR A 145 ? 0.18926 0.16932 0.20400 0.00727  -0.02588 -0.02773 152 THR A N   
1049 C CA  . THR A 145 ? 0.19047 0.17680 0.20484 0.01019  -0.02266 -0.02063 152 THR A CA  
1050 C C   . THR A 145 ? 0.25067 0.24620 0.25712 0.01438  -0.02680 -0.02052 152 THR A C   
1051 O O   . THR A 145 ? 0.24312 0.24103 0.24078 0.01625  -0.02971 -0.02648 152 THR A O   
1052 C CB  . THR A 145 ? 0.24683 0.22819 0.25780 0.01073  -0.01554 -0.01639 152 THR A CB  
1053 O OG1 . THR A 145 ? 0.23829 0.21718 0.24931 0.01262  -0.01318 -0.00942 152 THR A OG1 
1054 C CG2 . THR A 145 ? 0.25382 0.23995 0.25494 0.01288  -0.01400 -0.01749 152 THR A CG2 
1055 N N   . LYS A 146 ? 0.21057 0.21220 0.21899 0.01772  -0.02731 -0.01400 153 LYS A N   
1056 C CA  . LYS A 146 ? 0.19850 0.21128 0.19887 0.02318  -0.03154 -0.01144 153 LYS A CA  
1057 C C   . LYS A 146 ? 0.24782 0.25671 0.24496 0.02920  -0.02762 -0.00010 153 LYS A C   
1058 O O   . LYS A 146 ? 0.22016 0.22726 0.22529 0.03212  -0.02701 0.00310  153 LYS A O   
1059 C CB  . LYS A 146 ? 0.21371 0.24103 0.22089 0.02192  -0.04023 -0.01602 153 LYS A CB  
1060 C CG  . LYS A 146 ? 0.24377 0.28719 0.24293 0.02885  -0.04580 -0.01303 153 LYS A CG  
1061 C CD  . LYS A 146 ? 0.30333 0.34916 0.28666 0.03039  -0.04807 -0.01873 153 LYS A CD  
1062 C CE  . LYS A 146 ? 0.28262 0.34796 0.25632 0.03739  -0.05463 -0.01620 153 LYS A CE  
1063 N NZ  . LYS A 146 ? 0.23355 0.29895 0.20073 0.04598  -0.04968 -0.00049 153 LYS A NZ  
1064 N N   . HIS A 147 ? 0.28174 0.26393 0.23803 0.01520  -0.01085 -0.01071 154 HIS A N   
1065 C CA  . HIS A 147 ? 0.25596 0.23204 0.20427 0.02114  -0.00451 -0.00117 154 HIS A CA  
1066 C C   . HIS A 147 ? 0.30712 0.28975 0.24162 0.03139  -0.01114 0.00192  154 HIS A C   
1067 O O   . HIS A 147 ? 0.30306 0.29187 0.22631 0.03487  -0.01798 -0.00468 154 HIS A O   
1068 C CB  . HIS A 147 ? 0.25190 0.21768 0.19429 0.01775  0.00576  0.00427  154 HIS A CB  
1069 C CG  . HIS A 147 ? 0.27783 0.23104 0.21838 0.02008  0.01065  0.01622  154 HIS A CG  
1070 N ND1 . HIS A 147 ? 0.28703 0.24047 0.21508 0.02846  0.01099  0.02770  154 HIS A ND1 
1071 C CD2 . HIS A 147 ? 0.24778 0.18512 0.19769 0.01545  0.01351  0.01854  154 HIS A CD2 
1072 C CE1 . HIS A 147 ? 0.38823 0.32433 0.32093 0.02757  0.01430  0.03887  154 HIS A CE1 
1073 N NE2 . HIS A 147 ? 0.32565 0.24994 0.27177 0.01951  0.01462  0.03173  154 HIS A NE2 
1074 N N   . ASN A 148 ? 0.28520 0.26618 0.21887 0.03867  -0.01084 0.01054  155 ASN A N   
1075 C CA  . ASN A 148 ? 0.28173 0.27156 0.20149 0.05025  -0.01796 0.01499  155 ASN A CA  
1076 C C   . ASN A 148 ? 0.31573 0.30686 0.21191 0.05604  -0.01473 0.01904  155 ASN A C   
1077 O O   . ASN A 148 ? 0.35089 0.35443 0.23094 0.06627  -0.02401 0.01565  155 ASN A O   
1078 C CB  . ASN A 148 ? 0.30945 0.29292 0.22968 0.05941  -0.01595 0.02690  155 ASN A CB  
1079 C CG  . ASN A 148 ? 0.29389 0.28821 0.23273 0.06198  -0.02134 0.02294  155 ASN A CG  
1080 O OD1 . ASN A 148 ? 0.37732 0.39093 0.32917 0.05759  -0.02970 0.01526  155 ASN A OD1 
1081 N ND2 . ASN A 148 ? 0.32873 0.31150 0.27067 0.06997  -0.01722 0.02909  155 ASN A ND2 
1082 N N   . ASP A 149 ? 0.32639 0.30882 0.22047 0.05099  -0.00232 0.02645  156 ASP A N   
1083 C CA  . ASP A 149 ? 0.40637 0.39698 0.28010 0.05854  0.00493  0.03663  156 ASP A CA  
1084 C C   . ASP A 149 ? 0.41382 0.41436 0.27860 0.05957  0.00496  0.02370  156 ASP A C   
1085 O O   . ASP A 149 ? 0.42798 0.44076 0.27625 0.06782  0.01377  0.03240  156 ASP A O   
1086 C CB  . ASP A 149 ? 0.42251 0.40240 0.30427 0.05224  0.01837  0.05727  156 ASP A CB  
1087 C CG  . ASP A 149 ? 0.51168 0.47661 0.39791 0.05540  0.01711  0.07158  156 ASP A CG  
1088 O OD1 . ASP A 149 ? 0.42151 0.39211 0.29838 0.06679  0.00858  0.06983  156 ASP A OD1 
1089 O OD2 . ASP A 149 ? 0.54331 0.48966 0.44386 0.04686  0.02288  0.08411  156 ASP A OD2 
1090 N N   . ASP A 150 ? 0.40786 0.40476 0.28360 0.05306  -0.00430 0.00506  157 ASP A N   
1091 C CA  . ASP A 150 ? 0.33341 0.33362 0.20216 0.05524  -0.00560 -0.00807 157 ASP A CA  
1092 C C   . ASP A 150 ? 0.45916 0.45413 0.33544 0.05269  -0.02399 -0.02791 157 ASP A C   
1093 O O   . ASP A 150 ? 0.34802 0.34263 0.23779 0.04787  -0.03397 -0.02900 157 ASP A O   
1094 C CB  . ASP A 150 ? 0.33281 0.32873 0.21710 0.04416  0.00699  -0.00336 157 ASP A CB  
1095 C CG  . ASP A 150 ? 0.38699 0.39358 0.25825 0.05282  0.01243  -0.00793 157 ASP A CG  
1096 O OD1 . ASP A 150 ? 0.41110 0.42355 0.26029 0.06801  0.00395  -0.02036 157 ASP A OD1 
1097 O OD2 . ASP A 150 ? 0.40045 0.41072 0.28340 0.04608  0.02399  -0.00016 157 ASP A OD2 
1098 N N   . GLU A 151 ? 0.40914 0.40073 0.27907 0.05638  -0.02918 -0.04240 158 GLU A N   
1099 C CA  . GLU A 151 ? 0.31836 0.29919 0.19978 0.05178  -0.04861 -0.06018 158 GLU A CA  
1100 C C   . GLU A 151 ? 0.27689 0.24903 0.18911 0.03412  -0.04521 -0.05674 158 GLU A C   
1101 O O   . GLU A 151 ? 0.30311 0.27707 0.22302 0.02792  -0.02918 -0.04517 158 GLU A O   
1102 C CB  . GLU A 151 ? 0.38838 0.36397 0.24736 0.06680  -0.05800 -0.07896 158 GLU A CB  
1103 C CG  . GLU A 151 ? 0.62795 0.61742 0.44943 0.08967  -0.05944 -0.08278 158 GLU A CG  
1104 C CD  . GLU A 151 ? 1.13265 1.12080 0.92720 0.10996  -0.06319 -0.10067 158 GLU A CD  
1105 O OE1 . GLU A 151 ? 0.89524 0.86344 0.70118 0.10616  -0.07492 -0.11682 158 GLU A OE1 
1106 O OE2 . GLU A 151 ? 1.09143 1.09962 0.85321 0.13155  -0.05393 -0.09721 158 GLU A OE2 
1107 N N   . GLN A 152 ? 0.27926 0.24250 0.21012 0.02606  -0.06197 -0.06609 159 GLN A N   
1108 C CA  . GLN A 152 ? 0.28033 0.23869 0.23961 0.01108  -0.05917 -0.06007 159 GLN A CA  
1109 C C   . GLN A 152 ? 0.28589 0.23253 0.23997 0.01407  -0.05523 -0.06638 159 GLN A C   
1110 O O   . GLN A 152 ? 0.28774 0.22222 0.22858 0.02392  -0.06722 -0.08194 159 GLN A O   
1111 C CB  . GLN A 152 ? 0.31679 0.27304 0.30399 -0.00045 -0.07820 -0.06181 159 GLN A CB  
1112 C CG  . GLN A 152 ? 0.28604 0.24775 0.30455 -0.01526 -0.07168 -0.04733 159 GLN A CG  
1113 C CD  . GLN A 152 ? 0.29521 0.26794 0.34712 -0.02765 -0.08585 -0.03988 159 GLN A CD  
1114 O OE1 . GLN A 152 ? 0.32227 0.31228 0.37811 -0.02631 -0.08827 -0.03574 159 GLN A OE1 
1115 N NE2 . GLN A 152 ? 0.34537 0.31011 0.42451 -0.03988 -0.09537 -0.03562 159 GLN A NE2 
1116 N N   . TYR A 153 ? 0.26763 0.21810 0.23130 0.00769  -0.04005 -0.05581 160 TYR A N   
1117 C CA  . TYR A 153 ? 0.26594 0.21052 0.22640 0.01134  -0.03446 -0.05911 160 TYR A CA  
1118 C C   . TYR A 153 ? 0.27805 0.21994 0.26300 -0.00074 -0.03320 -0.05098 160 TYR A C   
1119 O O   . TYR A 153 ? 0.25303 0.20413 0.25336 -0.01022 -0.02958 -0.03997 160 TYR A O   
1120 C CB  . TYR A 153 ? 0.23365 0.19124 0.18000 0.01753  -0.01664 -0.05259 160 TYR A CB  
1121 C CG  . TYR A 153 ? 0.29649 0.26084 0.21635 0.03367  -0.01537 -0.05805 160 TYR A CG  
1122 C CD1 . TYR A 153 ? 0.34782 0.31100 0.25235 0.04882  -0.01756 -0.06956 160 TYR A CD1 
1123 C CD2 . TYR A 153 ? 0.37702 0.35080 0.28544 0.03681  -0.01163 -0.05078 160 TYR A CD2 
1124 C CE1 . TYR A 153 ? 0.37337 0.34879 0.24992 0.06786  -0.01493 -0.07387 160 TYR A CE1 
1125 C CE2 . TYR A 153 ? 0.36302 0.34792 0.24480 0.05391  -0.00916 -0.05257 160 TYR A CE2 
1126 C CZ  . TYR A 153 ? 0.45977 0.44753 0.32476 0.06996  -0.01027 -0.06422 160 TYR A CZ  
1127 O OH  . TYR A 153 ? 0.54598 0.55064 0.38078 0.09121  -0.00638 -0.06557 160 TYR A OH  
1128 N N   . ALA A 154 ? 0.27354 0.20507 0.25991 0.00274  -0.03547 -0.05574 161 ALA A N   
1129 C CA  . ALA A 154 ? 0.24010 0.17060 0.24601 -0.00552 -0.03304 -0.04607 161 ALA A CA  
1130 C C   . ALA A 154 ? 0.27844 0.21615 0.27621 0.00126  -0.02082 -0.04537 161 ALA A C   
1131 O O   . ALA A 154 ? 0.25291 0.18549 0.23786 0.01370  -0.02204 -0.05523 161 ALA A O   
1132 C CB  . ALA A 154 ? 0.27747 0.18655 0.29923 -0.00885 -0.05047 -0.04929 161 ALA A CB  
1133 N N   . TRP A 155 ? 0.21402 0.16593 0.21914 -0.00519 -0.01019 -0.03461 162 TRP A N   
1134 C CA  . TRP A 155 ? 0.19877 0.16060 0.20335 -0.00209 -0.00154 -0.03211 162 TRP A CA  
1135 C C   . TRP A 155 ? 0.20789 0.16701 0.22654 -0.00500 -0.00491 -0.02475 162 TRP A C   
1136 O O   . TRP A 155 ? 0.20697 0.16589 0.23749 -0.01257 -0.00815 -0.01594 162 TRP A O   
1137 C CB  . TRP A 155 ? 0.20160 0.17832 0.20468 -0.00705 0.00823  -0.02707 162 TRP A CB  
1138 C CG  . TRP A 155 ? 0.18327 0.17321 0.19018 -0.00735 0.01435  -0.02439 162 TRP A CG  
1139 C CD1 . TRP A 155 ? 0.18245 0.18373 0.18797 -0.00614 0.02048  -0.02413 162 TRP A CD1 
1140 C CD2 . TRP A 155 ? 0.19826 0.19533 0.21294 -0.00957 0.01391  -0.01999 162 TRP A CD2 
1141 N NE1 . TRP A 155 ? 0.17654 0.19012 0.19138 -0.00909 0.02172  -0.02158 162 TRP A NE1 
1142 C CE2 . TRP A 155 ? 0.17977 0.19040 0.19733 -0.00977 0.01740  -0.02044 162 TRP A CE2 
1143 C CE3 . TRP A 155 ? 0.18430 0.18116 0.20472 -0.01084 0.01086  -0.01362 162 TRP A CE3 
1144 C CZ2 . TRP A 155 ? 0.20334 0.22516 0.22621 -0.01004 0.01571  -0.01848 162 TRP A CZ2 
1145 C CZ3 . TRP A 155 ? 0.15514 0.16467 0.17798 -0.00932 0.01177  -0.00945 162 TRP A CZ3 
1146 C CH2 . TRP A 155 ? 0.16495 0.18574 0.18746 -0.00837 0.01310  -0.01375 162 TRP A CH2 
1147 N N   . GLU A 156 ? 0.19052 0.15106 0.20913 0.00214  -0.00359 -0.02573 163 GLU A N   
1148 C CA  . GLU A 156 ? 0.22103 0.17877 0.25205 0.00115  -0.00701 -0.01615 163 GLU A CA  
1149 C C   . GLU A 156 ? 0.19023 0.16236 0.21988 0.00845  -0.00150 -0.01518 163 GLU A C   
1150 O O   . GLU A 156 ? 0.21679 0.19386 0.23955 0.01735  0.00135  -0.02334 163 GLU A O   
1151 C CB  . GLU A 156 ? 0.27550 0.20630 0.31404 0.00374  -0.02036 -0.01825 163 GLU A CB  
1152 C CG  . GLU A 156 ? 0.32676 0.25180 0.38302 -0.00009 -0.02490 -0.00218 163 GLU A CG  
1153 C CD  . GLU A 156 ? 0.57100 0.46541 0.64265 -0.00444 -0.04141 -0.00098 163 GLU A CD  
1154 O OE1 . GLU A 156 ? 0.42353 0.31952 0.51223 -0.01791 -0.04532 0.01094  163 GLU A OE1 
1155 O OE2 . GLU A 156 ? 0.49985 0.36889 0.56802 0.00634  -0.05175 -0.01238 163 GLU A OE2 
1156 N N   . SER A 157 ? 0.19253 0.17598 0.22900 0.00614  0.00004  -0.00403 164 SER A N   
1157 C CA  . SER A 157 ? 0.18400 0.18248 0.22119 0.01368  0.00226  -0.00266 164 SER A CA  
1158 C C   . SER A 157 ? 0.19573 0.19894 0.23957 0.01471  0.00007  0.01201  164 SER A C   
1159 O O   . SER A 157 ? 0.18428 0.19485 0.22902 0.00868  0.00182  0.02140  164 SER A O   
1160 C CB  . SER A 157 ? 0.16940 0.19079 0.20325 0.01052  0.00813  -0.00729 164 SER A CB  
1161 O OG  . SER A 157 ? 0.18349 0.22265 0.22214 0.01724  0.00789  -0.00580 164 SER A OG  
1162 N N   . SER A 158 ? 0.20399 0.20591 0.25167 0.02484  -0.00303 0.01533  165 SER A N   
1163 C CA  . SER A 158 ? 0.20753 0.21997 0.25949 0.02902  -0.00427 0.03103  165 SER A CA  
1164 C C   . SER A 158 ? 0.19976 0.24136 0.24743 0.03536  -0.00218 0.02764  165 SER A C   
1165 O O   . SER A 158 ? 0.24922 0.30034 0.29926 0.04457  -0.00484 0.03739  165 SER A O   
1166 C CB  . SER A 158 ? 0.28257 0.27016 0.34417 0.03666  -0.01186 0.03960  165 SER A CB  
1167 O OG  . SER A 158 ? 0.27457 0.23622 0.34592 0.02744  -0.01741 0.04604  165 SER A OG  
1168 N N   . ALA A 159 ? 0.20194 0.25745 0.24573 0.03001  0.00093  0.01505  166 ALA A N   
1169 C CA  . ALA A 159 ? 0.17914 0.26205 0.22533 0.03235  -0.00012 0.00962  166 ALA A CA  
1170 C C   . ALA A 159 ? 0.22152 0.30884 0.27604 0.04414  -0.00052 0.00897  166 ALA A C   
1171 O O   . ALA A 159 ? 0.27767 0.34719 0.33186 0.04858  0.00154  0.00455  166 ALA A O   
1172 C CB  . ALA A 159 ? 0.21356 0.31527 0.25391 0.03476  -0.00408 0.01552  166 ALA A CB  
1173 N N   . GLY A 160 ? 0.19889 0.31134 0.25973 0.05181  -0.00395 0.01186  167 GLY A N   
1174 C CA  . GLY A 160 ? 0.23957 0.36153 0.30945 0.06576  -0.00334 0.01122  167 GLY A CA  
1175 C C   . GLY A 160 ? 0.21860 0.35623 0.29644 0.06392  0.00289  0.00302  167 GLY A C   
1176 O O   . GLY A 160 ? 0.25771 0.40471 0.34074 0.07903  0.00581  0.00205  167 GLY A O   
1177 N N   . GLY A 161 ? 0.17515 0.31693 0.25406 0.04770  0.00545  -0.00133 168 GLY A N   
1178 C CA  . GLY A 161 ? 0.16857 0.33269 0.25980 0.04345  0.01169  -0.00304 168 GLY A CA  
1179 C C   . GLY A 161 ? 0.17117 0.31850 0.25243 0.04491  0.01996  -0.00664 168 GLY A C   
1180 O O   . GLY A 161 ? 0.16839 0.33786 0.25903 0.04287  0.02731  -0.00415 168 GLY A O   
1181 N N   . SER A 162 ? 0.24775 0.18803 0.16429 0.05671  0.02168  0.04090  169 SER A N   
1182 C CA  . SER A 162 ? 0.22458 0.15955 0.14720 0.05500  0.01214  0.02450  169 SER A CA  
1183 C C   . SER A 162 ? 0.22377 0.15175 0.16575 0.04925  0.01120  0.02397  169 SER A C   
1184 O O   . SER A 162 ? 0.26299 0.18625 0.22084 0.04731  0.01811  0.03604  169 SER A O   
1185 C CB  . SER A 162 ? 0.26725 0.19500 0.20498 0.06043  0.00761  0.01442  169 SER A CB  
1186 O OG  . SER A 162 ? 0.28165 0.19657 0.25066 0.06088  0.01209  0.02032  169 SER A OG  
1187 N N   . PHE A 163 ? 0.23155 0.16118 0.17154 0.04733  0.00277  0.01030  170 PHE A N   
1188 C CA  . PHE A 163 ? 0.26722 0.19237 0.22679 0.04268  -0.00020 0.00611  170 PHE A CA  
1189 C C   . PHE A 163 ? 0.26357 0.18976 0.23221 0.04479  -0.01108 -0.01359 170 PHE A C   
1190 O O   . PHE A 163 ? 0.27081 0.20367 0.22341 0.04958  -0.01629 -0.02290 170 PHE A O   
1191 C CB  . PHE A 163 ? 0.23461 0.16619 0.17899 0.03823  0.00168  0.01180  170 PHE A CB  
1192 C CG  . PHE A 163 ? 0.24305 0.18460 0.16071 0.03972  -0.00306 0.00485  170 PHE A CG  
1193 C CD1 . PHE A 163 ? 0.27544 0.22364 0.16808 0.04077  0.00144  0.01082  170 PHE A CD1 
1194 C CD2 . PHE A 163 ? 0.22563 0.17154 0.14439 0.04042  -0.01133 -0.00701 170 PHE A CD2 
1195 C CE1 . PHE A 163 ? 0.27978 0.23635 0.15065 0.04193  -0.00129 0.00605  170 PHE A CE1 
1196 C CE2 . PHE A 163 ? 0.22340 0.17915 0.11839 0.04297  -0.01420 -0.01061 170 PHE A CE2 
1197 C CZ  . PHE A 163 ? 0.30942 0.26928 0.18120 0.04339  -0.00862 -0.00342 170 PHE A CZ  
1198 N N   . THR A 164 ? 0.25208 0.17354 0.24780 0.04154  -0.01446 -0.02065 171 THR A N   
1199 C CA  . THR A 164 ? 0.23919 0.16543 0.24587 0.04357  -0.02551 -0.04163 171 THR A CA  
1200 C C   . THR A 164 ? 0.23999 0.17514 0.24520 0.04079  -0.03057 -0.04650 171 THR A C   
1201 O O   . THR A 164 ? 0.23251 0.16504 0.24111 0.03583  -0.02514 -0.03483 171 THR A O   
1202 C CB  . THR A 164 ? 0.25046 0.16570 0.29575 0.04282  -0.02663 -0.05104 171 THR A CB  
1203 O OG1 . THR A 164 ? 0.25011 0.15720 0.32186 0.03637  -0.02123 -0.04282 171 THR A OG1 
1204 C CG2 . THR A 164 ? 0.25675 0.16248 0.30529 0.04689  -0.02083 -0.04501 171 THR A CG2 
1205 N N   . VAL A 165 ? 0.24652 0.19417 0.24610 0.04511  -0.04097 -0.06375 172 VAL A N   
1206 C CA  . VAL A 165 ? 0.26600 0.22539 0.26639 0.04466  -0.04731 -0.07093 172 VAL A CA  
1207 C C   . VAL A 165 ? 0.29272 0.26094 0.31428 0.04787  -0.05857 -0.09484 172 VAL A C   
1208 O O   . VAL A 165 ? 0.27029 0.24390 0.28610 0.05382  -0.06379 -0.10702 172 VAL A O   
1209 C CB  . VAL A 165 ? 0.25657 0.22883 0.22143 0.04886  -0.04805 -0.06573 172 VAL A CB  
1210 C CG1 . VAL A 165 ? 0.26198 0.24846 0.22892 0.05061  -0.05508 -0.07357 172 VAL A CG1 
1211 C CG2 . VAL A 165 ? 0.23386 0.19830 0.18115 0.04484  -0.03692 -0.04485 172 VAL A CG2 
1212 N N   . ARG A 166 ? 0.24770 0.21910 0.29453 0.04409  -0.06240 -0.10273 173 ARG A N   
1213 C CA  . ARG A 166 ? 0.25724 0.24079 0.32670 0.04672  -0.07383 -0.12816 173 ARG A CA  
1214 C C   . ARG A 166 ? 0.27006 0.26814 0.34692 0.04553  -0.07926 -0.13349 173 ARG A C   
1215 O O   . ARG A 166 ? 0.24743 0.23953 0.32420 0.04030  -0.07267 -0.11765 173 ARG A O   
1216 C CB  . ARG A 166 ? 0.31038 0.27871 0.42050 0.04195  -0.07221 -0.13723 173 ARG A CB  
1217 C CG  . ARG A 166 ? 0.31698 0.27182 0.45791 0.03259  -0.06475 -0.12693 173 ARG A CG  
1218 C CD  . ARG A 166 ? 0.39162 0.32659 0.56915 0.02847  -0.05854 -0.12776 173 ARG A CD  
1219 N NE  . ARG A 166 ? 0.43095 0.35036 0.59309 0.02951  -0.04740 -0.10616 173 ARG A NE  
1220 C CZ  . ARG A 166 ? 0.52179 0.42469 0.70615 0.02929  -0.04097 -0.10332 173 ARG A CZ  
1221 N NH1 . ARG A 166 ? 0.42153 0.31824 0.64702 0.02710  -0.04370 -0.12087 173 ARG A NH1 
1222 N NH2 . ARG A 166 ? 0.55824 0.45148 0.72445 0.03170  -0.03129 -0.08278 173 ARG A NH2 
1223 N N   . THR A 167 ? 0.28261 0.30213 0.36531 0.05130  -0.09147 -0.15636 174 THR A N   
1224 C CA  . THR A 167 ? 0.28137 0.31695 0.37815 0.05047  -0.09769 -0.16484 174 THR A CA  
1225 C C   . THR A 167 ? 0.29563 0.31697 0.43620 0.03999  -0.09418 -0.16754 174 THR A C   
1226 O O   . THR A 167 ? 0.34677 0.35639 0.51567 0.03655  -0.09365 -0.17800 174 THR A O   
1227 C CB  . THR A 167 ? 0.32234 0.38741 0.41927 0.05975  -0.11172 -0.19066 174 THR A CB  
1228 O OG1 . THR A 167 ? 0.44797 0.52601 0.50519 0.06989  -0.11046 -0.18074 174 THR A OG1 
1229 C CG2 . THR A 167 ? 0.53506 0.61974 0.64541 0.05996  -0.11697 -0.19698 174 THR A CG2 
1230 N N   . ASP A 168 ? 0.26736 0.28892 0.41467 0.03505  -0.09068 -0.15692 175 ASP A N   
1231 C CA  . ASP A 168 ? 0.26655 0.27460 0.45465 0.02484  -0.08537 -0.15555 175 ASP A CA  
1232 C C   . ASP A 168 ? 0.37524 0.40259 0.59661 0.02387  -0.09648 -0.18169 175 ASP A C   
1233 O O   . ASP A 168 ? 0.37303 0.42263 0.58476 0.02797  -0.10347 -0.18678 175 ASP A O   
1234 C CB  . ASP A 168 ? 0.31397 0.31267 0.49375 0.01982  -0.07497 -0.13031 175 ASP A CB  
1235 C CG  . ASP A 168 ? 0.36719 0.35151 0.58810 0.00976  -0.06752 -0.12540 175 ASP A CG  
1236 O OD1 . ASP A 168 ? 0.54206 0.51055 0.78805 0.00606  -0.06315 -0.12765 175 ASP A OD1 
1237 O OD2 . ASP A 168 ? 0.31451 0.30374 0.54401 0.00601  -0.06553 -0.11891 175 ASP A OD2 
1238 N N   . THR A 169 ? 0.51047 0.53015 0.77226 0.01883  -0.09779 -0.19853 176 THR A N   
1239 C CA  . THR A 169 ? 0.73172 0.76995 1.02875 0.01741  -0.10359 -0.21807 176 THR A CA  
1240 C C   . THR A 169 ? 0.66663 0.69390 1.00004 0.00647  -0.09606 -0.20997 176 THR A C   
1241 O O   . THR A 169 ? 0.50168 0.54248 0.86698 0.00482  -0.09837 -0.22384 176 THR A O   
1242 C CB  . THR A 169 ? 0.78484 0.82573 1.10314 0.02001  -0.10448 -0.23339 176 THR A CB  
1243 O OG1 . THR A 169 ? 0.51678 0.52910 0.84223 0.01524  -0.09423 -0.21987 176 THR A OG1 
1244 C CG2 . THR A 169 ? 0.51585 0.58000 0.80347 0.03262  -0.11396 -0.24613 176 THR A CG2 
1245 N N   . GLY A 170 ? 0.58728 0.59186 0.91527 0.00017  -0.08568 -0.18616 177 GLY A N   
1246 C CA  . GLY A 170 ? 0.54449 0.53882 0.90508 -0.00963 -0.07663 -0.17450 177 GLY A CA  
1247 C C   . GLY A 170 ? 0.53035 0.54635 0.89155 -0.00999 -0.08216 -0.17766 177 GLY A C   
1248 O O   . GLY A 170 ? 0.42225 0.46419 0.76868 -0.00285 -0.09487 -0.19491 177 GLY A O   
1249 N N   . GLU A 171 ? 0.46832 0.47551 0.84563 -0.01720 -0.07232 -0.16010 178 GLU A N   
1250 C CA  . GLU A 171 ? 0.32962 0.35613 0.71368 -0.01840 -0.07632 -0.16250 178 GLU A CA  
1251 C C   . GLU A 171 ? 0.32071 0.36248 0.65447 -0.00854 -0.08089 -0.15403 178 GLU A C   
1252 O O   . GLU A 171 ? 0.29455 0.32266 0.59430 -0.00620 -0.07216 -0.13050 178 GLU A O   
1253 C CB  . GLU A 171 ? 0.39133 0.40257 0.79911 -0.02752 -0.06248 -0.14117 178 GLU A CB  
1254 C CG  . GLU A 171 ? 0.35753 0.38725 0.78863 -0.03126 -0.06594 -0.14761 178 GLU A CG  
1255 C CD  . GLU A 171 ? 0.35848 0.40063 0.82365 -0.03121 -0.07113 -0.17168 178 GLU A CD  
1256 O OE1 . GLU A 171 ? 0.39708 0.42580 0.88419 -0.03270 -0.06511 -0.17449 178 GLU A OE1 
1257 O OE2 . GLU A 171 ? 0.39464 0.46153 0.86228 -0.02816 -0.08061 -0.18696 178 GLU A OE2 
1258 N N   . PRO A 172 ? 0.33514 0.40578 0.66351 -0.00209 -0.09378 -0.17211 179 PRO A N   
1259 C CA  . PRO A 172 ? 0.27308 0.35804 0.55637 0.00812  -0.09672 -0.16205 179 PRO A CA  
1260 C C   . PRO A 172 ? 0.42783 0.50199 0.69882 0.00517  -0.08530 -0.13521 179 PRO A C   
1261 O O   . PRO A 172 ? 0.44232 0.51347 0.74329 -0.00272 -0.08034 -0.13124 179 PRO A O   
1262 C CB  . PRO A 172 ? 0.32307 0.44327 0.61665 0.01422  -0.11133 -0.18619 179 PRO A CB  
1263 C CG  . PRO A 172 ? 0.43287 0.55761 0.77028 0.00862  -0.11774 -0.21330 179 PRO A CG  
1264 C CD  . PRO A 172 ? 0.43600 0.52793 0.79347 -0.00112 -0.10721 -0.20520 179 PRO A CD  
1265 N N   . MET A 173 ? 0.24000 0.30952 0.46769 0.01175  -0.08097 -0.11758 180 MET A N   
1266 C CA  . MET A 173 ? 0.27812 0.33596 0.49067 0.00962  -0.06947 -0.09272 180 MET A CA  
1267 C C   . MET A 173 ? 0.41075 0.48705 0.60396 0.01704  -0.07253 -0.08844 180 MET A C   
1268 O O   . MET A 173 ? 0.42883 0.49908 0.61967 0.01444  -0.06409 -0.07198 180 MET A O   
1269 C CB  . MET A 173 ? 0.35258 0.39020 0.53327 0.01071  -0.06044 -0.07517 180 MET A CB  
1270 C CG  . MET A 173 ? 0.62312 0.63944 0.82150 0.00337  -0.05307 -0.07083 180 MET A CG  
1271 S SD  . MET A 173 ? 0.53590 0.53252 0.69851 0.00408  -0.04034 -0.04610 180 MET A SD  
1272 C CE  . MET A 173 ? 0.39096 0.39684 0.52568 0.00858  -0.03780 -0.03367 180 MET A CE  
1273 N N   . GLY A 174 ? 0.36127 0.46047 0.53999 0.02716  -0.08364 -0.10174 181 GLY A N   
1274 C CA  . GLY A 174 ? 0.26387 0.38036 0.42217 0.03613  -0.08535 -0.09495 181 GLY A CA  
1275 C C   . GLY A 174 ? 0.29013 0.39548 0.40694 0.04223  -0.07775 -0.07568 181 GLY A C   
1276 O O   . GLY A 174 ? 0.24170 0.36084 0.33334 0.05313  -0.08281 -0.07794 181 GLY A O   
1277 N N   . ARG A 175 ? 0.20716 0.28883 0.31806 0.03541  -0.06512 -0.05691 182 ARG A N   
1278 C CA  . ARG A 175 ? 0.20398 0.27221 0.28020 0.03873  -0.05637 -0.03962 182 ARG A CA  
1279 C C   . ARG A 175 ? 0.20940 0.25402 0.28841 0.02932  -0.04374 -0.02425 182 ARG A C   
1280 O O   . ARG A 175 ? 0.20977 0.25222 0.30864 0.02369  -0.03931 -0.01923 182 ARG A O   
1281 C CB  . ARG A 175 ? 0.20469 0.28457 0.26113 0.04793  -0.05514 -0.03050 182 ARG A CB  
1282 C CG  . ARG A 175 ? 0.20394 0.27178 0.22621 0.05219  -0.04677 -0.01558 182 ARG A CG  
1283 C CD  . ARG A 175 ? 0.20369 0.27335 0.21369 0.05748  -0.04007 -0.00156 182 ARG A CD  
1284 N NE  . ARG A 175 ? 0.19802 0.25971 0.22528 0.05005  -0.03351 0.00533  182 ARG A NE  
1285 C CZ  . ARG A 175 ? 0.19865 0.27420 0.24163 0.05226  -0.03639 0.00363  182 ARG A CZ  
1286 N NH1 . ARG A 175 ? 0.20474 0.30415 0.24900 0.06189  -0.04616 -0.00521 182 ARG A NH1 
1287 N NH2 . ARG A 175 ? 0.19346 0.26113 0.25134 0.04533  -0.02937 0.01082  182 ARG A NH2 
1288 N N   . GLY A 176 ? 0.26234 0.32305 0.15647 0.06673  -0.02875 0.00988  183 GLY A N   
1289 C CA  . GLY A 176 ? 0.24009 0.28836 0.15633 0.05568  -0.02422 0.00929  183 GLY A CA  
1290 C C   . GLY A 176 ? 0.24290 0.28000 0.16368 0.04620  -0.02068 0.00161  183 GLY A C   
1291 O O   . GLY A 176 ? 0.24447 0.27926 0.15139 0.05011  -0.01731 -0.00032 183 GLY A O   
1292 N N   . THR A 177 ? 0.21439 0.24607 0.15363 0.03557  -0.02108 -0.00224 184 THR A N   
1293 C CA  . THR A 177 ? 0.20501 0.22798 0.15056 0.02868  -0.01759 -0.00716 184 THR A CA  
1294 C C   . THR A 177 ? 0.26609 0.28928 0.22448 0.01887  -0.02474 -0.01525 184 THR A C   
1295 O O   . THR A 177 ? 0.21544 0.24378 0.18404 0.01524  -0.02799 -0.01408 184 THR A O   
1296 C CB  . THR A 177 ? 0.21526 0.23052 0.17013 0.02651  -0.00665 0.00108  184 THR A CB  
1297 O OG1 . THR A 177 ? 0.25629 0.26973 0.19958 0.03448  0.00210  0.01031  184 THR A OG1 
1298 C CG2 . THR A 177 ? 0.26562 0.27898 0.22919 0.02131  -0.00416 -0.00298 184 THR A CG2 
1299 N N   . LYS A 178 ? 0.21471 0.23124 0.17147 0.01599  -0.02568 -0.02248 185 LYS A N   
1300 C CA  . LYS A 178 ? 0.22267 0.23453 0.18956 0.00726  -0.03014 -0.02821 185 LYS A CA  
1301 C C   . LYS A 178 ? 0.21198 0.21572 0.18483 0.00753  -0.02372 -0.02584 185 LYS A C   
1302 O O   . LYS A 178 ? 0.27437 0.27317 0.23914 0.01378  -0.01925 -0.02735 185 LYS A O   
1303 C CB  . LYS A 178 ? 0.29737 0.30550 0.25486 0.00444  -0.03748 -0.03951 185 LYS A CB  
1304 C CG  . LYS A 178 ? 0.41679 0.41447 0.38287 -0.00530 -0.04033 -0.04483 185 LYS A CG  
1305 C CD  . LYS A 178 ? 0.48045 0.47200 0.43756 -0.01141 -0.04796 -0.05809 185 LYS A CD  
1306 C CE  . LYS A 178 ? 0.63382 0.64347 0.58075 -0.00924 -0.05595 -0.06309 185 LYS A CE  
1307 N NZ  . LYS A 178 ? 0.70857 0.74228 0.66705 -0.00892 -0.05921 -0.05477 185 LYS A NZ  
1308 N N   . VAL A 179 ? 0.17398 0.17939 0.16017 0.00237  -0.02304 -0.02182 186 VAL A N   
1309 C CA  . VAL A 179 ? 0.17683 0.18035 0.16986 0.00324  -0.01901 -0.01904 186 VAL A CA  
1310 C C   . VAL A 179 ? 0.19772 0.19267 0.19343 -0.00037 -0.02231 -0.02125 186 VAL A C   
1311 O O   . VAL A 179 ? 0.20448 0.20205 0.20641 -0.00679 -0.02528 -0.01985 186 VAL A O   
1312 C CB  . VAL A 179 ? 0.17202 0.18471 0.17570 0.00018  -0.01626 -0.01338 186 VAL A CB  
1313 C CG1 . VAL A 179 ? 0.18967 0.20749 0.20165 0.00120  -0.01457 -0.01081 186 VAL A CG1 
1314 C CG2 . VAL A 179 ? 0.20158 0.21737 0.20309 0.00233  -0.01086 -0.00992 186 VAL A CG2 
1315 N N   . ILE A 180 ? 0.19761 0.18070 0.18776 0.00468  -0.02030 -0.02391 187 ILE A N   
1316 C CA  . ILE A 180 ? 0.20963 0.17729 0.19993 0.00219  -0.02144 -0.02503 187 ILE A CA  
1317 C C   . ILE A 180 ? 0.21495 0.18497 0.21171 0.00869  -0.01758 -0.01699 187 ILE A C   
1318 O O   . ILE A 180 ? 0.22358 0.19473 0.21879 0.01882  -0.01304 -0.01578 187 ILE A O   
1319 C CB  . ILE A 180 ? 0.22710 0.17425 0.20425 0.00428  -0.02147 -0.03466 187 ILE A CB  
1320 C CG1 . ILE A 180 ? 0.22545 0.17772 0.19541 -0.00141 -0.02737 -0.04316 187 ILE A CG1 
1321 C CG2 . ILE A 180 ? 0.26565 0.19045 0.24324 -0.00009 -0.02113 -0.03521 187 ILE A CG2 
1322 C CD1 . ILE A 180 ? 0.31819 0.25383 0.27096 0.00144  -0.02825 -0.05551 187 ILE A CD1 
1323 N N   . LEU A 181 ? 0.18702 0.16106 0.19074 0.00416  -0.01921 -0.01094 188 LEU A N   
1324 C CA  . LEU A 181 ? 0.18696 0.16767 0.19555 0.01099  -0.01738 -0.00241 188 LEU A CA  
1325 C C   . LEU A 181 ? 0.25541 0.21312 0.25879 0.01526  -0.01469 0.00118  188 LEU A C   
1326 O O   . LEU A 181 ? 0.26422 0.21102 0.26693 0.00726  -0.01536 0.00295  188 LEU A O   
1327 C CB  . LEU A 181 ? 0.17782 0.17615 0.19273 0.00514  -0.02044 0.00207  188 LEU A CB  
1328 C CG  . LEU A 181 ? 0.21230 0.22581 0.23114 -0.00032 -0.02200 -0.00199 188 LEU A CG  
1329 C CD1 . LEU A 181 ? 0.22111 0.24628 0.24242 -0.00548 -0.02443 0.00004  188 LEU A CD1 
1330 C CD2 . LEU A 181 ? 0.19101 0.21669 0.21476 0.00456  -0.01979 -0.00188 188 LEU A CD2 
1331 N N   . HIS A 182 ? 0.23429 0.18396 0.23448 0.02841  -0.01029 0.00325  189 HIS A N   
1332 C CA  . HIS A 182 ? 0.29893 0.22279 0.29321 0.03570  -0.00594 0.00890  189 HIS A CA  
1333 C C   . HIS A 182 ? 0.24891 0.19050 0.24901 0.04275  -0.00652 0.02272  189 HIS A C   
1334 O O   . HIS A 182 ? 0.25000 0.21234 0.25549 0.05499  -0.00616 0.02780  189 HIS A O   
1335 C CB  . HIS A 182 ? 0.27776 0.18305 0.26384 0.04962  0.00009  0.00456  189 HIS A CB  
1336 C CG  . HIS A 182 ? 0.31558 0.20858 0.29253 0.04377  -0.00042 -0.01033 189 HIS A CG  
1337 N ND1 . HIS A 182 ? 0.41262 0.27066 0.37770 0.03819  0.00056  -0.02008 189 HIS A ND1 
1338 C CD2 . HIS A 182 ? 0.35168 0.26327 0.32837 0.04225  -0.00207 -0.01698 189 HIS A CD2 
1339 C CE1 . HIS A 182 ? 0.37645 0.23538 0.33330 0.03431  -0.00191 -0.03315 189 HIS A CE1 
1340 N NE2 . HIS A 182 ? 0.37338 0.26413 0.33639 0.03781  -0.00288 -0.03017 189 HIS A NE2 
1341 N N   . LEU A 183 ? 0.25035 0.18828 0.24977 0.03485  -0.00766 0.02893  190 LEU A N   
1342 C CA  . LEU A 183 ? 0.26355 0.22513 0.26574 0.03939  -0.01016 0.04026  190 LEU A CA  
1343 C C   . LEU A 183 ? 0.28135 0.23697 0.27965 0.05779  -0.00622 0.05356  190 LEU A C   
1344 O O   . LEU A 183 ? 0.33307 0.25434 0.32401 0.06396  0.00059  0.05711  190 LEU A O   
1345 C CB  . LEU A 183 ? 0.24156 0.20125 0.24159 0.02736  -0.01063 0.04391  190 LEU A CB  
1346 C CG  . LEU A 183 ? 0.21751 0.19063 0.22236 0.01265  -0.01465 0.03349  190 LEU A CG  
1347 C CD1 . LEU A 183 ? 0.25318 0.22799 0.25651 0.00405  -0.01318 0.03904  190 LEU A CD1 
1348 C CD2 . LEU A 183 ? 0.25194 0.25426 0.26192 0.01384  -0.01985 0.02850  190 LEU A CD2 
1349 N N   . LYS A 184 ? 0.26580 0.25535 0.26882 0.06673  -0.01078 0.06079  191 LYS A N   
1350 C CA  . LYS A 184 ? 0.29861 0.29099 0.29775 0.08591  -0.00866 0.07665  191 LYS A CA  
1351 C C   . LYS A 184 ? 0.33256 0.29993 0.31980 0.08486  -0.00400 0.08883  191 LYS A C   
1352 O O   . LYS A 184 ? 0.34412 0.30950 0.32921 0.06897  -0.00494 0.08597  191 LYS A O   
1353 C CB  . LYS A 184 ? 0.29465 0.33599 0.30170 0.09195  -0.01730 0.08059  191 LYS A CB  
1354 C CG  . LYS A 184 ? 0.32530 0.39572 0.34775 0.09263  -0.02059 0.07140  191 LYS A CG  
1355 C CD  . LYS A 184 ? 0.37185 0.49178 0.40394 0.09020  -0.03099 0.07148  191 LYS A CD  
1356 C CE  . LYS A 184 ? 0.44667 0.59260 0.49593 0.08074  -0.03369 0.05960  191 LYS A CE  
1357 N NZ  . LYS A 184 ? 0.29539 0.49189 0.35799 0.07897  -0.04373 0.05932  191 LYS A NZ  
1358 N N   . GLU A 185 ? 0.39649 0.34484 0.37624 0.10320  0.00243  0.10392  192 GLU A N   
1359 C CA  . GLU A 185 ? 0.40744 0.32391 0.37521 0.10295  0.01013  0.11804  192 GLU A CA  
1360 C C   . GLU A 185 ? 0.44551 0.38912 0.40844 0.09781  0.00584  0.12684  192 GLU A C   
1361 O O   . GLU A 185 ? 0.49297 0.41670 0.44980 0.08665  0.01169  0.13237  192 GLU A O   
1362 C CB  . GLU A 185 ? 0.45139 0.34357 0.41083 0.12778  0.01840  0.13493  192 GLU A CB  
1363 C CG  . GLU A 185 ? 0.70301 0.58849 0.64963 0.13819  0.02329  0.15851  192 GLU A CG  
1364 C CD  . GLU A 185 ? 0.97946 0.83331 0.91784 0.16023  0.03311  0.17223  192 GLU A CD  
1365 O OE1 . GLU A 185 ? 0.84289 0.69243 0.78640 0.17192  0.03423  0.16440  192 GLU A OE1 
1366 O OE2 . GLU A 185 ? 1.04047 0.87772 0.96847 0.16224  0.03962  0.18644  192 GLU A OE2 
1367 N N   . ASP A 186 ? 0.35601 0.34604 0.32156 0.10473  -0.00403 0.12732  193 ASP A N   
1368 C CA  . ASP A 186 ? 0.39266 0.40924 0.34945 0.10169  -0.00860 0.13374  193 ASP A CA  
1369 C C   . ASP A 186 ? 0.40797 0.44396 0.37025 0.08102  -0.01496 0.11571  193 ASP A C   
1370 O O   . ASP A 186 ? 0.34289 0.40552 0.29739 0.07894  -0.02011 0.11645  193 ASP A O   
1371 C CB  . ASP A 186 ? 0.37584 0.43305 0.32916 0.12116  -0.01687 0.14425  193 ASP A CB  
1372 C CG  . ASP A 186 ? 0.47209 0.56744 0.44179 0.12025  -0.02767 0.12966  193 ASP A CG  
1373 O OD1 . ASP A 186 ? 0.52245 0.60718 0.50449 0.10852  -0.02659 0.11420  193 ASP A OD1 
1374 O OD2 . ASP A 186 ? 0.57006 0.70812 0.54047 0.13093  -0.03728 0.13417  193 ASP A OD2 
1375 N N   . GLN A 187 ? 0.32719 0.34937 0.30040 0.06725  -0.01427 0.09977  194 GLN A N   
1376 C CA  . GLN A 187 ? 0.25732 0.29450 0.23568 0.05034  -0.01909 0.08390  194 GLN A CA  
1377 C C   . GLN A 187 ? 0.25643 0.26743 0.23600 0.03541  -0.01252 0.07956  194 GLN A C   
1378 O O   . GLN A 187 ? 0.27382 0.28932 0.26036 0.02339  -0.01502 0.06575  194 GLN A O   
1379 C CB  . GLN A 187 ? 0.30021 0.35282 0.29137 0.04759  -0.02508 0.06950  194 GLN A CB  
1380 C CG  . GLN A 187 ? 0.26088 0.34788 0.25637 0.05903  -0.03252 0.07213  194 GLN A CG  
1381 C CD  . GLN A 187 ? 0.26522 0.38296 0.25263 0.05794  -0.04007 0.07302  194 GLN A CD  
1382 O OE1 . GLN A 187 ? 0.32449 0.44407 0.30732 0.04525  -0.04132 0.06388  194 GLN A OE1 
1383 N NE2 . GLN A 187 ? 0.25262 0.39603 0.23714 0.07265  -0.04533 0.08349  194 GLN A NE2 
1384 N N   . THR A 188 ? 0.31994 0.30477 0.29376 0.03586  -0.00388 0.09203  195 THR A N   
1385 C CA  . THR A 188 ? 0.34103 0.30448 0.32006 0.01968  0.00194  0.08773  195 THR A CA  
1386 C C   . THR A 188 ? 0.32633 0.30909 0.30489 0.00954  0.00256  0.08650  195 THR A C   
1387 O O   . THR A 188 ? 0.29433 0.26842 0.28079 -0.00419 0.00656  0.08254  195 THR A O   
1388 C CB  . THR A 188 ? 0.40402 0.33039 0.37916 0.02043  0.01221  0.10104  195 THR A CB  
1389 O OG1 . THR A 188 ? 0.42770 0.35775 0.39067 0.03056  0.01737  0.12088  195 THR A OG1 
1390 C CG2 . THR A 188 ? 0.40149 0.30300 0.37621 0.03099  0.01305  0.09917  195 THR A CG2 
1391 N N   . GLU A 189 ? 0.31181 0.32226 0.28137 0.01622  -0.00140 0.08879  196 GLU A N   
1392 C CA  . GLU A 189 ? 0.32592 0.35411 0.29285 0.00877  -0.00005 0.08508  196 GLU A CA  
1393 C C   . GLU A 189 ? 0.28640 0.31922 0.26535 -0.00201 -0.00365 0.06747  196 GLU A C   
1394 O O   . GLU A 189 ? 0.26863 0.30880 0.25016 -0.00923 0.00016  0.06475  196 GLU A O   
1395 C CB  . GLU A 189 ? 0.31831 0.37413 0.27023 0.01835  -0.00524 0.08650  196 GLU A CB  
1396 C CG  . GLU A 189 ? 0.24049 0.31464 0.19565 0.01945  -0.01649 0.07092  196 GLU A CG  
1397 C CD  . GLU A 189 ? 0.35261 0.45440 0.29270 0.02791  -0.02331 0.07175  196 GLU A CD  
1398 O OE1 . GLU A 189 ? 0.36829 0.47696 0.30210 0.04015  -0.02580 0.08400  196 GLU A OE1 
1399 O OE2 . GLU A 189 ? 0.34240 0.45894 0.27579 0.02318  -0.02627 0.05987  196 GLU A OE2 
1400 N N   . TYR A 190 ? 0.26999 0.29983 0.25610 -0.00166 -0.00990 0.05691  197 TYR A N   
1401 C CA  . TYR A 190 ? 0.19666 0.22970 0.19191 -0.00959 -0.01283 0.04252  197 TYR A CA  
1402 C C   . TYR A 190 ? 0.24731 0.26388 0.25269 -0.01878 -0.00964 0.04034  197 TYR A C   
1403 O O   . TYR A 190 ? 0.27078 0.28970 0.28300 -0.02333 -0.01268 0.02975  197 TYR A O   
1404 C CB  . TYR A 190 ? 0.22844 0.26710 0.22642 -0.00578 -0.01957 0.03358  197 TYR A CB  
1405 C CG  . TYR A 190 ? 0.23054 0.29012 0.22107 -0.00012 -0.02439 0.03336  197 TYR A CG  
1406 C CD1 . TYR A 190 ? 0.27193 0.34475 0.25627 -0.00340 -0.02546 0.02669  197 TYR A CD1 
1407 C CD2 . TYR A 190 ? 0.22607 0.29345 0.21510 0.00914  -0.02799 0.03939  197 TYR A CD2 
1408 C CE1 . TYR A 190 ? 0.24961 0.34162 0.22528 -0.00010 -0.03114 0.02369  197 TYR A CE1 
1409 C CE2 . TYR A 190 ? 0.30144 0.39366 0.28451 0.01305  -0.03443 0.03814  197 TYR A CE2 
1410 C CZ  . TYR A 190 ? 0.25329 0.35702 0.22903 0.00712  -0.03649 0.02919  197 TYR A CZ  
1411 O OH  . TYR A 190 ? 0.26048 0.38867 0.22847 0.00910  -0.04413 0.02495  197 TYR A OH  
1412 N N   . LEU A 191 ? 0.24302 0.24296 0.24897 -0.02190 -0.00370 0.05024  198 LEU A N   
1413 C CA  . LEU A 191 ? 0.23943 0.22743 0.25614 -0.03457 -0.00082 0.04759  198 LEU A CA  
1414 C C   . LEU A 191 ? 0.26071 0.26069 0.28288 -0.04282 0.00588  0.05467  198 LEU A C   
1415 O O   . LEU A 191 ? 0.26960 0.26727 0.30466 -0.05559 0.00774  0.05224  198 LEU A O   
1416 C CB  . LEU A 191 ? 0.29741 0.25382 0.31297 -0.03580 0.00253  0.05206  198 LEU A CB  
1417 C CG  . LEU A 191 ? 0.24761 0.19153 0.25819 -0.02606 -0.00199 0.04544  198 LEU A CG  
1418 C CD1 . LEU A 191 ? 0.34965 0.25793 0.35576 -0.02407 0.00357  0.05089  198 LEU A CD1 
1419 C CD2 . LEU A 191 ? 0.32375 0.27448 0.34001 -0.03096 -0.00846 0.02953  198 LEU A CD2 
1420 N N   . GLU A 192 ? 0.26445 0.27944 0.27720 -0.03605 0.00965  0.06315  199 GLU A N   
1421 C CA  . GLU A 192 ? 0.23619 0.26495 0.25266 -0.04181 0.01831  0.07144  199 GLU A CA  
1422 C C   . GLU A 192 ? 0.31624 0.36990 0.33862 -0.04232 0.01637  0.06099  199 GLU A C   
1423 O O   . GLU A 192 ? 0.24831 0.31004 0.26231 -0.03397 0.01067  0.05190  199 GLU A O   
1424 C CB  . GLU A 192 ? 0.37549 0.40862 0.37502 -0.03233 0.02468  0.08640  199 GLU A CB  
1425 C CG  . GLU A 192 ? 0.37928 0.38869 0.36928 -0.02572 0.02617  0.09861  199 GLU A CG  
1426 C CD  . GLU A 192 ? 0.84622 0.86597 0.81590 -0.01237 0.02969  0.11294  199 GLU A CD  
1427 O OE1 . GLU A 192 ? 0.84758 0.85138 0.80774 -0.00307 0.03101  0.12537  199 GLU A OE1 
1428 O OE2 . GLU A 192 ? 0.96326 1.00733 0.92488 -0.00963 0.03128  0.11180  199 GLU A OE2 
1429 N N   . GLU A 193 ? 0.27443 0.34012 0.31245 -0.05227 0.02178  0.06272  200 GLU A N   
1430 C CA  . GLU A 193 ? 0.21851 0.30797 0.26472 -0.05081 0.02066  0.05388  200 GLU A CA  
1431 C C   . GLU A 193 ? 0.23437 0.33723 0.26409 -0.03798 0.02365  0.05290  200 GLU A C   
1432 O O   . GLU A 193 ? 0.24581 0.35309 0.27143 -0.03105 0.01886  0.04147  200 GLU A O   
1433 C CB  . GLU A 193 ? 0.23230 0.33974 0.29994 -0.06264 0.02733  0.05898  200 GLU A CB  
1434 C CG  . GLU A 193 ? 0.27511 0.40946 0.35393 -0.05879 0.02577  0.05082  200 GLU A CG  
1435 C CD  . GLU A 193 ? 0.64119 0.80258 0.74474 -0.06968 0.03231  0.05670  200 GLU A CD  
1436 O OE1 . GLU A 193 ? 0.40160 0.55974 0.51315 -0.08206 0.03976  0.06772  200 GLU A OE1 
1437 O OE2 . GLU A 193 ? 0.47495 0.66165 0.59102 -0.06571 0.03043  0.05113  200 GLU A OE2 
1438 N N   . ARG A 194 ? 0.28320 0.39061 0.30130 -0.03456 0.03208  0.06461  201 ARG A N   
1439 C CA  . ARG A 194 ? 0.23807 0.35979 0.23814 -0.02282 0.03540  0.06172  201 ARG A CA  
1440 C C   . ARG A 194 ? 0.25539 0.36775 0.23767 -0.01482 0.02539  0.05122  201 ARG A C   
1441 O O   . ARG A 194 ? 0.30022 0.41950 0.27117 -0.00773 0.02432  0.04043  201 ARG A O   
1442 C CB  . ARG A 194 ? 0.28625 0.41717 0.27516 -0.02022 0.04723  0.07761  201 ARG A CB  
1443 C CG  . ARG A 194 ? 0.35020 0.46438 0.32868 -0.02017 0.04726  0.09109  201 ARG A CG  
1444 C CD  . ARG A 194 ? 0.49249 0.61808 0.45360 -0.01373 0.05933  0.10721  201 ARG A CD  
1445 N NE  . ARG A 194 ? 0.58948 0.70037 0.53466 -0.00827 0.05854  0.12092  201 ARG A NE  
1446 C CZ  . ARG A 194 ? 0.47110 0.58646 0.39982 -0.00228 0.06932  0.13986  201 ARG A CZ  
1447 N NH1 . ARG A 194 ? 0.51855 0.65325 0.44497 -0.00220 0.08282  0.14732  201 ARG A NH1 
1448 N NH2 . ARG A 194 ? 0.48473 0.58627 0.39843 0.00553  0.06741  0.15292  201 ARG A NH2 
1449 N N   . ARG A 195 ? 0.22227 0.31906 0.20301 -0.01612 0.01848  0.05359  202 ARG A N   
1450 C CA  . ARG A 195 ? 0.23031 0.32381 0.19957 -0.01035 0.00861  0.04391  202 ARG A CA  
1451 C C   . ARG A 195 ? 0.22979 0.31855 0.20881 -0.01295 0.00248  0.02906  202 ARG A C   
1452 O O   . ARG A 195 ? 0.23032 0.32143 0.20059 -0.00958 -0.00173 0.01775  202 ARG A O   
1453 C CB  . ARG A 195 ? 0.26687 0.34898 0.23404 -0.00861 0.00433  0.05241  202 ARG A CB  
1454 C CG  . ARG A 195 ? 0.27846 0.36449 0.23769 -0.00308 -0.00597 0.04421  202 ARG A CG  
1455 C CD  . ARG A 195 ? 0.25749 0.36124 0.19600 0.00413  -0.00779 0.04335  202 ARG A CD  
1456 N NE  . ARG A 195 ? 0.24698 0.35921 0.18112 0.00770  -0.01869 0.03745  202 ARG A NE  
1457 C CZ  . ARG A 195 ? 0.29473 0.41705 0.22373 0.00565  -0.02580 0.02161  202 ARG A CZ  
1458 N NH1 . ARG A 195 ? 0.26297 0.38411 0.18647 0.00253  -0.02258 0.00967  202 ARG A NH1 
1459 N NH2 . ARG A 195 ? 0.28023 0.41404 0.21051 0.00670  -0.03585 0.01756  202 ARG A NH2 
1460 N N   . ILE A 196 ? 0.21005 0.29123 0.20602 -0.01935 0.00198  0.02881  203 ILE A N   
1461 C CA  . ILE A 196 ? 0.17142 0.24885 0.17450 -0.02000 -0.00286 0.01726  203 ILE A CA  
1462 C C   . ILE A 196 ? 0.21208 0.29931 0.21310 -0.01561 0.00132  0.01088  203 ILE A C   
1463 O O   . ILE A 196 ? 0.21995 0.30187 0.21552 -0.01215 -0.00128 0.00093  203 ILE A O   
1464 C CB  . ILE A 196 ? 0.24552 0.31599 0.26400 -0.02671 -0.00485 0.01800  203 ILE A CB  
1465 C CG1 . ILE A 196 ? 0.26591 0.32094 0.28361 -0.02876 -0.00790 0.02233  203 ILE A CG1 
1466 C CG2 . ILE A 196 ? 0.21736 0.28615 0.23999 -0.02497 -0.00911 0.00820  203 ILE A CG2 
1467 C CD1 . ILE A 196 ? 0.27430 0.31998 0.30375 -0.03741 -0.00759 0.02415  203 ILE A CD1 
1468 N N   . LYS A 197 ? 0.19617 0.29703 0.20188 -0.01535 0.00916  0.01705  204 LYS A N   
1469 C CA  . LYS A 197 ? 0.17800 0.28959 0.18147 -0.00789 0.01512  0.01200  204 LYS A CA  
1470 C C   . LYS A 197 ? 0.24101 0.34734 0.22253 -0.00067 0.01548  0.00323  204 LYS A C   
1471 O O   . LYS A 197 ? 0.23299 0.33284 0.20938 0.00513  0.01632  -0.00712 204 LYS A O   
1472 C CB  . LYS A 197 ? 0.22131 0.35346 0.23332 -0.00827 0.02514  0.02200  204 LYS A CB  
1473 C CG  . LYS A 197 ? 0.35175 0.49710 0.38854 -0.01430 0.02541  0.02564  204 LYS A CG  
1474 C CD  . LYS A 197 ? 0.41750 0.58965 0.46483 -0.01354 0.03692  0.03445  204 LYS A CD  
1475 C CE  . LYS A 197 ? 0.53979 0.71472 0.59408 -0.02571 0.04173  0.04771  204 LYS A CE  
1476 N NZ  . LYS A 197 ? 0.55067 0.75233 0.63228 -0.03476 0.04779  0.05528  204 LYS A NZ  
1477 N N   . GLU A 198 ? 0.20240 0.31071 0.16965 -0.00073 0.01487  0.00712  205 GLU A N   
1478 C CA  . GLU A 198 ? 0.22479 0.33164 0.16946 0.00455  0.01320  -0.00300 205 GLU A CA  
1479 C C   . GLU A 198 ? 0.25618 0.34816 0.20002 0.00128  0.00422  -0.01611 205 GLU A C   
1480 O O   . GLU A 198 ? 0.27052 0.35490 0.20253 0.00398  0.00465  -0.02957 205 GLU A O   
1481 C CB  . GLU A 198 ? 0.23190 0.34750 0.16201 0.00562  0.01202  0.00569  205 GLU A CB  
1482 C CG  . GLU A 198 ? 0.26525 0.38361 0.17121 0.00943  0.00653  -0.00589 205 GLU A CG  
1483 C CD  . GLU A 198 ? 0.30109 0.43128 0.19348 0.01218  0.00307  0.00491  205 GLU A CD  
1484 O OE1 . GLU A 198 ? 0.30196 0.42924 0.20580 0.00927  -0.00133 0.01557  205 GLU A OE1 
1485 O OE2 . GLU A 198 ? 0.31204 0.45402 0.18060 0.01890  0.00518  0.00308  205 GLU A OE2 
1486 N N   . ILE A 199 ? 0.19924 0.28563 0.15530 -0.00479 -0.00278 -0.01249 206 ILE A N   
1487 C CA  . ILE A 199 ? 0.19537 0.27107 0.15326 -0.00898 -0.00994 -0.02259 206 ILE A CA  
1488 C C   . ILE A 199 ? 0.28573 0.34809 0.24989 -0.00802 -0.00649 -0.02958 206 ILE A C   
1489 O O   . ILE A 199 ? 0.26473 0.31509 0.22296 -0.00968 -0.00762 -0.04092 206 ILE A O   
1490 C CB  . ILE A 199 ? 0.25342 0.32877 0.22277 -0.01313 -0.01608 -0.01540 206 ILE A CB  
1491 C CG1 . ILE A 199 ? 0.24203 0.32927 0.20288 -0.01091 -0.01927 -0.00761 206 ILE A CG1 
1492 C CG2 . ILE A 199 ? 0.22545 0.29285 0.20067 -0.01777 -0.02120 -0.02378 206 ILE A CG2 
1493 C CD1 . ILE A 199 ? 0.26167 0.34612 0.23296 -0.01119 -0.02184 0.00281  206 ILE A CD1 
1494 N N   . VAL A 200 ? 0.24782 0.31219 0.22411 -0.00551 -0.00227 -0.02258 207 VAL A N   
1495 C CA  . VAL A 200 ? 0.18286 0.23733 0.16423 -0.00134 0.00092  -0.02656 207 VAL A CA  
1496 C C   . VAL A 200 ? 0.23416 0.28272 0.20234 0.00665  0.00800  -0.03500 207 VAL A C   
1497 O O   . VAL A 200 ? 0.27926 0.30896 0.24284 0.00906  0.00991  -0.04300 207 VAL A O   
1498 C CB  . VAL A 200 ? 0.20110 0.26636 0.19842 0.00011  0.00222  -0.01749 207 VAL A CB  
1499 C CG1 . VAL A 200 ? 0.25451 0.31576 0.25516 0.00893  0.00630  -0.01940 207 VAL A CG1 
1500 C CG2 . VAL A 200 ? 0.23044 0.29326 0.23700 -0.00729 -0.00471 -0.01330 207 VAL A CG2 
1501 N N   . LYS A 201 ? 0.21302 0.27512 0.17325 0.01134  0.01328  -0.03325 208 LYS A N   
1502 C CA  . LYS A 201 ? 0.23751 0.29350 0.18221 0.02111  0.02140  -0.04247 208 LYS A CA  
1503 C C   . LYS A 201 ? 0.28473 0.32299 0.21010 0.01686  0.01759  -0.05786 208 LYS A C   
1504 O O   . LYS A 201 ? 0.39222 0.41042 0.30618 0.02208  0.02268  -0.06971 208 LYS A O   
1505 C CB  . LYS A 201 ? 0.28652 0.36471 0.22669 0.02749  0.02921  -0.03577 208 LYS A CB  
1506 C CG  . LYS A 201 ? 0.40986 0.48389 0.33047 0.03990  0.03915  -0.04571 208 LYS A CG  
1507 C CD  . LYS A 201 ? 0.41043 0.51047 0.32667 0.04582  0.04802  -0.03671 208 LYS A CD  
1508 C CE  . LYS A 201 ? 0.44506 0.54227 0.33988 0.06079  0.05969  -0.04698 208 LYS A CE  
1509 N NZ  . LYS A 201 ? 0.63376 0.76092 0.52955 0.06847  0.07161  -0.03500 208 LYS A NZ  
1510 N N   . LYS A 202 ? 0.28929 0.33461 0.21140 0.00738  0.00856  -0.05816 209 LYS A N   
1511 C CA  . LYS A 202 ? 0.34692 0.38343 0.25274 0.00110  0.00269  -0.07352 209 LYS A CA  
1512 C C   . LYS A 202 ? 0.32777 0.34174 0.24127 -0.00732 -0.00046 -0.08207 209 LYS A C   
1513 O O   . LYS A 202 ? 0.32247 0.31730 0.22313 -0.01069 0.00035  -0.09813 209 LYS A O   
1514 C CB  . LYS A 202 ? 0.27702 0.33442 0.17988 -0.00455 -0.00671 -0.06866 209 LYS A CB  
1515 C CG  . LYS A 202 ? 0.37327 0.43117 0.26210 -0.01247 -0.01579 -0.08428 209 LYS A CG  
1516 C CD  . LYS A 202 ? 0.44184 0.52629 0.32722 -0.01344 -0.02479 -0.07611 209 LYS A CD  
1517 C CE  . LYS A 202 ? 0.55292 0.64653 0.42383 -0.02087 -0.03573 -0.09240 209 LYS A CE  
1518 N NZ  . LYS A 202 ? 0.73601 0.85959 0.60248 -0.01822 -0.04485 -0.08228 209 LYS A NZ  
1519 N N   . HIS A 203 ? 0.33714 0.35160 0.27035 -0.01136 -0.00326 -0.07187 210 HIS A N   
1520 C CA  . HIS A 203 ? 0.34080 0.33988 0.28248 -0.02110 -0.00649 -0.07675 210 HIS A CA  
1521 C C   . HIS A 203 ? 0.37538 0.35608 0.32679 -0.01640 0.00020  -0.07104 210 HIS A C   
1522 O O   . HIS A 203 ? 0.35225 0.31521 0.30784 -0.02350 0.00076  -0.07478 210 HIS A O   
1523 C CB  . HIS A 203 ? 0.27085 0.28810 0.22536 -0.02928 -0.01561 -0.06979 210 HIS A CB  
1524 C CG  . HIS A 203 ? 0.35736 0.39433 0.30328 -0.03370 -0.02389 -0.07464 210 HIS A CG  
1525 N ND1 . HIS A 203 ? 0.36392 0.39842 0.29947 -0.04225 -0.02845 -0.09082 210 HIS A ND1 
1526 C CD2 . HIS A 203 ? 0.33961 0.39937 0.28472 -0.03018 -0.02865 -0.06506 210 HIS A CD2 
1527 C CE1 . HIS A 203 ? 0.40021 0.45996 0.32883 -0.04300 -0.03703 -0.09101 210 HIS A CE1 
1528 N NE2 . HIS A 203 ? 0.42880 0.50296 0.36256 -0.03458 -0.03654 -0.07421 210 HIS A NE2 
1529 N N   . SER A 204 ? 0.33900 0.29115 0.21026 -0.04991 -0.06423 -0.08929 211 SER A N   
1530 C CA  . SER A 204 ? 0.33952 0.28711 0.23943 -0.04392 -0.05214 -0.08331 211 SER A CA  
1531 C C   . SER A 204 ? 0.32439 0.25256 0.21228 -0.03335 -0.03464 -0.09126 211 SER A C   
1532 O O   . SER A 204 ? 0.33478 0.26743 0.24147 -0.02359 -0.02343 -0.08312 211 SER A O   
1533 C CB  . SER A 204 ? 0.35982 0.33100 0.28260 -0.03711 -0.05002 -0.06537 211 SER A CB  
1534 O OG  . SER A 204 ? 0.36868 0.35893 0.30465 -0.04335 -0.06427 -0.05723 211 SER A OG  
1535 N N   . GLN A 205 ? 0.42537 0.33354 0.28200 -0.03412 -0.03236 -0.10781 212 GLN A N   
1536 C CA  . GLN A 205 ? 0.58412 0.47814 0.42876 -0.02077 -0.01359 -0.11464 212 GLN A CA  
1537 C C   . GLN A 205 ? 0.51922 0.39049 0.38184 -0.01517 -0.00466 -0.11852 212 GLN A C   
1538 O O   . GLN A 205 ? 0.56175 0.42819 0.42486 -0.00024 0.01168  -0.11932 212 GLN A O   
1539 C CB  . GLN A 205 ? 0.51751 0.39689 0.31847 -0.02072 -0.01159 -0.13193 212 GLN A CB  
1540 C CG  . GLN A 205 ? 0.61191 0.46212 0.39484 -0.03202 -0.02200 -0.15297 212 GLN A CG  
1541 C CD  . GLN A 205 ? 0.89166 0.75904 0.67092 -0.04739 -0.04545 -0.15281 212 GLN A CD  
1542 O OE1 . GLN A 205 ? 0.63675 0.52696 0.43583 -0.05367 -0.05627 -0.13729 212 GLN A OE1 
1543 N NE2 . GLN A 205 ? 0.81544 0.67776 0.57507 -0.05057 -0.05306 -0.16902 212 GLN A NE2 
1544 N N   . PHE A 206 ? 0.43481 0.29404 0.31473 -0.02587 -0.01396 -0.11856 213 PHE A N   
1545 C CA  . PHE A 206 ? 0.45659 0.29039 0.35313 -0.02046 -0.00479 -0.11860 213 PHE A CA  
1546 C C   . PHE A 206 ? 0.43391 0.28509 0.36561 -0.02000 -0.00612 -0.09834 213 PHE A C   
1547 O O   . PHE A 206 ? 0.63349 0.46452 0.58057 -0.02186 -0.00340 -0.09488 213 PHE A O   
1548 C CB  . PHE A 206 ? 0.51325 0.30870 0.39840 -0.03382 -0.01047 -0.13672 213 PHE A CB  
1549 C CG  . PHE A 206 ? 0.50764 0.28104 0.35259 -0.03287 -0.00833 -0.16031 213 PHE A CG  
1550 C CD1 . PHE A 206 ? 0.60579 0.38823 0.43241 -0.04738 -0.02539 -0.17143 213 PHE A CD1 
1551 C CD2 . PHE A 206 ? 0.58672 0.34096 0.41717 -0.01370 0.01052  -0.16820 213 PHE A CD2 
1552 C CE1 . PHE A 206 ? 0.66338 0.44014 0.46114 -0.04183 -0.02416 -0.18847 213 PHE A CE1 
1553 C CE2 . PHE A 206 ? 0.67275 0.42259 0.47645 -0.00864 0.01227  -0.18476 213 PHE A CE2 
1554 C CZ  . PHE A 206 ? 0.65610 0.41561 0.44118 -0.02304 -0.00476 -0.19561 213 PHE A CZ  
1555 N N   . ILE A 207 ? 0.30979 0.19583 0.25259 -0.01735 -0.00931 -0.08483 214 ILE A N   
1556 C CA  . ILE A 207 ? 0.27680 0.18076 0.24728 -0.01365 -0.00867 -0.06741 214 ILE A CA  
1557 C C   . ILE A 207 ? 0.33790 0.24150 0.31538 0.00459  0.00477  -0.06146 214 ILE A C   
1558 O O   . ILE A 207 ? 0.33013 0.24315 0.29946 0.01449  0.01159  -0.06476 214 ILE A O   
1559 C CB  . ILE A 207 ? 0.25016 0.18727 0.22737 -0.01619 -0.01652 -0.05820 214 ILE A CB  
1560 C CG1 . ILE A 207 ? 0.30032 0.24240 0.27660 -0.03181 -0.03091 -0.06063 214 ILE A CG1 
1561 C CG2 . ILE A 207 ? 0.24229 0.19803 0.24194 -0.00906 -0.01373 -0.04324 214 ILE A CG2 
1562 C CD1 . ILE A 207 ? 0.36660 0.30511 0.36468 -0.04177 -0.03495 -0.05537 214 ILE A CD1 
1563 N N   . GLY A 208 ? 0.28452 0.17987 0.27830 0.00935  0.00880  -0.05108 215 GLY A N   
1564 C CA  . GLY A 208 ? 0.33750 0.22972 0.33736 0.02836  0.02024  -0.04459 215 GLY A CA  
1565 C C   . GLY A 208 ? 0.28628 0.21499 0.29923 0.03931  0.02023  -0.03182 215 GLY A C   
1566 O O   . GLY A 208 ? 0.29659 0.22881 0.31928 0.05390  0.02580  -0.02108 215 GLY A O   
1567 N N   . TYR A 209 ? 0.25391 0.20875 0.26613 0.03274  0.01344  -0.03314 216 TYR A N   
1568 C CA  . TYR A 209 ? 0.26505 0.25250 0.28781 0.03970  0.01179  -0.02560 216 TYR A CA  
1569 C C   . TYR A 209 ? 0.26795 0.27055 0.28518 0.03596  0.01127  -0.03320 216 TYR A C   
1570 O O   . TYR A 209 ? 0.24383 0.23593 0.24761 0.02600  0.00900  -0.04051 216 TYR A O   
1571 C CB  . TYR A 209 ? 0.19809 0.19882 0.22837 0.03403  0.00463  -0.01675 216 TYR A CB  
1572 C CG  . TYR A 209 ? 0.19297 0.18058 0.22939 0.03680  0.00758  -0.00594 216 TYR A CG  
1573 C CD1 . TYR A 209 ? 0.23966 0.23594 0.28149 0.05163  0.01183  0.00551  216 TYR A CD1 
1574 C CD2 . TYR A 209 ? 0.25725 0.22452 0.29469 0.02408  0.00609  -0.00609 216 TYR A CD2 
1575 C CE1 . TYR A 209 ? 0.20388 0.18567 0.24968 0.05479  0.01657  0.01885  216 TYR A CE1 
1576 C CE2 . TYR A 209 ? 0.21814 0.17139 0.26378 0.02445  0.01090  0.00575  216 TYR A CE2 
1577 C CZ  . TYR A 209 ? 0.21809 0.17697 0.26670 0.04043  0.01721  0.01930  216 TYR A CZ  
1578 O OH  . TYR A 209 ? 0.27113 0.21439 0.32626 0.04162  0.02383  0.03451  216 TYR A OH  
1579 N N   . PRO A 210 ? 0.19808 0.22615 0.22555 0.04306  0.01314  -0.03095 217 PRO A N   
1580 C CA  . PRO A 210 ? 0.21902 0.26084 0.24457 0.03718  0.01443  -0.03598 217 PRO A CA  
1581 C C   . PRO A 210 ? 0.22809 0.27099 0.24914 0.02474  0.00602  -0.03530 217 PRO A C   
1582 O O   . PRO A 210 ? 0.22654 0.27716 0.25471 0.02395  -0.00047 -0.03085 217 PRO A O   
1583 C CB  . PRO A 210 ? 0.21294 0.28501 0.25721 0.04532  0.01615  -0.03297 217 PRO A CB  
1584 C CG  . PRO A 210 ? 0.24186 0.31940 0.29385 0.05473  0.01162  -0.02543 217 PRO A CG  
1585 C CD  . PRO A 210 ? 0.19293 0.23939 0.23466 0.05645  0.01399  -0.02311 217 PRO A CD  
1586 N N   . ILE A 211 ? 0.24302 0.27762 0.25023 0.01699  0.00696  -0.03909 218 ILE A N   
1587 C CA  . ILE A 211 ? 0.16529 0.19990 0.16772 0.00780  -0.00005 -0.03654 218 ILE A CA  
1588 C C   . ILE A 211 ? 0.18926 0.23472 0.19387 0.00445  0.00517  -0.03568 218 ILE A C   
1589 O O   . ILE A 211 ? 0.21866 0.26171 0.21248 0.00376  0.01332  -0.03752 218 ILE A O   
1590 C CB  . ILE A 211 ? 0.20861 0.22654 0.19240 0.00153  -0.00486 -0.03872 218 ILE A CB  
1591 C CG1 . ILE A 211 ? 0.24043 0.24750 0.22694 0.00112  -0.00965 -0.03994 218 ILE A CG1 
1592 C CG2 . ILE A 211 ? 0.22084 0.24175 0.20166 -0.00436 -0.01210 -0.03314 218 ILE A CG2 
1593 C CD1 . ILE A 211 ? 0.23083 0.22249 0.19977 -0.00672 -0.01540 -0.04610 218 ILE A CD1 
1594 N N   . THR A 212 ? 0.19211 0.24835 0.20998 0.00178  0.00160  -0.03332 219 THR A N   
1595 C CA  . THR A 212 ? 0.18982 0.25473 0.21491 -0.00455 0.00651  -0.03238 219 THR A CA  
1596 C C   . THR A 212 ? 0.17211 0.22321 0.18883 -0.01145 0.00283  -0.02757 219 THR A C   
1597 O O   . THR A 212 ? 0.21329 0.26040 0.23379 -0.01065 -0.00469 -0.02724 219 THR A O   
1598 C CB  . THR A 212 ? 0.18073 0.26615 0.22766 -0.00403 0.00442  -0.03551 219 THR A CB  
1599 O OG1 . THR A 212 ? 0.17146 0.27196 0.22681 0.00546  0.00763  -0.03710 219 THR A OG1 
1600 C CG2 . THR A 212 ? 0.25357 0.34721 0.31243 -0.01484 0.00906  -0.03538 219 THR A CG2 
1601 N N   . LEU A 213 ? 0.20820 0.25208 0.21241 -0.01623 0.00929  -0.02272 220 LEU A N   
1602 C CA  . LEU A 213 ? 0.21026 0.23984 0.20611 -0.02110 0.00738  -0.01464 220 LEU A CA  
1603 C C   . LEU A 213 ? 0.19574 0.22751 0.20870 -0.02951 0.01301  -0.01318 220 LEU A C   
1604 O O   . LEU A 213 ? 0.20076 0.24132 0.21875 -0.03527 0.02379  -0.01109 220 LEU A O   
1605 C CB  . LEU A 213 ? 0.21533 0.23596 0.18529 -0.02152 0.01141  -0.00802 220 LEU A CB  
1606 C CG  . LEU A 213 ? 0.28519 0.29125 0.24359 -0.02450 0.01105  0.00477  220 LEU A CG  
1607 C CD1 . LEU A 213 ? 0.24748 0.24538 0.21298 -0.02056 -0.00068 0.00704  220 LEU A CD1 
1608 C CD2 . LEU A 213 ? 0.29335 0.29448 0.21996 -0.02254 0.01217  0.01089  220 LEU A CD2 
1609 N N   . PHE A 214 ? 0.19891 0.22327 0.22204 -0.03068 0.00647  -0.01533 221 PHE A N   
1610 C CA  . PHE A 214 ? 0.22181 0.24224 0.26090 -0.04116 0.01013  -0.01655 221 PHE A CA  
1611 C C   . PHE A 214 ? 0.25069 0.25051 0.28005 -0.04757 0.01806  -0.00312 221 PHE A C   
1612 O O   . PHE A 214 ? 0.26666 0.25224 0.27593 -0.04099 0.01602  0.00666  221 PHE A O   
1613 C CB  . PHE A 214 ? 0.18866 0.20032 0.23533 -0.03920 0.00142  -0.02472 221 PHE A CB  
1614 C CG  . PHE A 214 ? 0.16124 0.19449 0.21805 -0.03479 -0.00530 -0.03710 221 PHE A CG  
1615 C CD1 . PHE A 214 ? 0.17598 0.22779 0.23039 -0.02680 -0.00619 -0.03737 221 PHE A CD1 
1616 C CD2 . PHE A 214 ? 0.16650 0.19841 0.23239 -0.03769 -0.01083 -0.04839 221 PHE A CD2 
1617 C CE1 . PHE A 214 ? 0.15422 0.22459 0.21583 -0.02080 -0.01196 -0.04505 221 PHE A CE1 
1618 C CE2 . PHE A 214 ? 0.20617 0.25951 0.27649 -0.03215 -0.01778 -0.05835 221 PHE A CE2 
1619 C CZ  . PHE A 214 ? 0.17336 0.24686 0.24189 -0.02315 -0.01815 -0.05489 221 PHE A CZ  
1620 N N   . VAL A 215 ? 0.22445 0.22415 0.26928 -0.06091 0.02679  -0.00138 222 VAL A N   
1621 C CA  . VAL A 215 ? 0.25818 0.23484 0.29617 -0.06849 0.03638  0.01389  222 VAL A CA  
1622 C C   . VAL A 215 ? 0.29435 0.24516 0.34581 -0.07588 0.03354  0.01073  222 VAL A C   
1623 O O   . VAL A 215 ? 0.27298 0.22865 0.33903 -0.07718 0.02509  -0.00549 222 VAL A O   
1624 C CB  . VAL A 215 ? 0.38645 0.37860 0.43239 -0.07985 0.05214  0.02133  222 VAL A CB  
1625 C CG1 . VAL A 215 ? 0.50690 0.50938 0.52625 -0.06988 0.05811  0.02860  222 VAL A CG1 
1626 C CG2 . VAL A 215 ? 0.26434 0.28678 0.34197 -0.08857 0.05224  0.00766  222 VAL A CG2 
1627 N N   . GLU A 216 ? 0.31357 0.23437 0.35743 -0.07987 0.04111  0.02644  223 GLU A N   
1628 C CA  . GLU A 216 ? 0.33425 0.22015 0.38742 -0.08497 0.04006  0.02464  223 GLU A CA  
1629 C C   . GLU A 216 ? 0.44842 0.31848 0.51818 -0.10595 0.05363  0.03291  223 GLU A C   
1630 O O   . GLU A 216 ? 0.48594 0.37769 0.56236 -0.11641 0.06460  0.04049  223 GLU A O   
1631 C CB  . GLU A 216 ? 0.45120 0.30723 0.48324 -0.06845 0.03664  0.03794  223 GLU A CB  
1632 C CG  . GLU A 216 ? 0.40225 0.27415 0.42220 -0.04956 0.02399  0.03226  223 GLU A CG  
1633 C CD  . GLU A 216 ? 0.56543 0.41480 0.56933 -0.03340 0.02074  0.04814  223 GLU A CD  
1634 O OE1 . GLU A 216 ? 0.44763 0.26711 0.45792 -0.02881 0.02079  0.04698  223 GLU A OE1 
1635 O OE2 . GLU A 216 ? 0.51811 0.38038 0.50314 -0.02449 0.01750  0.06077  223 GLU A OE2 
1636 N N   . LYS A 217 ? 0.73795 0.56811 0.81487 -0.11146 0.05392  0.03142  224 LYS A N   
1637 C CA  . LYS A 217 ? 0.67604 0.47816 0.77077 -0.13319 0.06632  0.03895  224 LYS A CA  
1638 C C   . LYS A 217 ? 0.88069 0.70682 1.00939 -0.15631 0.06441  0.01821  224 LYS A C   
1639 O O   . LYS A 217 ? 0.97064 0.77948 1.11259 -0.16414 0.05598  -0.00220 224 LYS A O   
1640 C CB  . LYS A 217 ? 0.64184 0.44192 0.72545 -0.13708 0.08329  0.06821  224 LYS A CB  
1641 C CG  . LYS A 217 ? 0.82569 0.57427 0.91073 -0.14680 0.09608  0.08782  224 LYS A CG  
1642 C CD  . LYS A 217 ? 0.79891 0.53425 0.85100 -0.13188 0.10525  0.12008  224 LYS A CD  
1643 C CE  . LYS A 217 ? 0.85959 0.54665 0.90406 -0.13022 0.10783  0.13687  224 LYS A CE  
1644 N NZ  . LYS A 217 ? 0.86439 0.52037 0.89313 -0.10619 0.09719  0.13722  224 LYS A NZ  
# 
