data_7HB0
# 
_entry.id   7HB0 
# 
_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   7HB0         pdb_00007hb0 10.2210/pdb7hb0/pdb 
WWPDB D_1001407247 ?            ?                   
# 
_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                        7HB0 
_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 '2-[(oxan-4-yl)oxy]aniline'       193.242   1   ?        ? ? ? 
3 water       nat water                             18.015    345 ?        ? ? ? 
# 
_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 '2-[(oxan-4-yl)oxy]aniline' A1AYK 
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 
A1AYK non-polymer         . '2-[(oxan-4-yl)oxy]aniline' ? 'C11 H15 N O2'   193.242 
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        A1AYK 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1AYK 
_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 A1AYK 1   301 301 A1AYK ABK A . 
C 3 HOH   1   401 294 HOH   HOH A . 
C 3 HOH   2   402 136 HOH   HOH A . 
C 3 HOH   3   403 251 HOH   HOH A . 
C 3 HOH   4   404 92  HOH   HOH A . 
C 3 HOH   5   405 218 HOH   HOH A . 
C 3 HOH   6   406 163 HOH   HOH A . 
C 3 HOH   7   407 250 HOH   HOH A . 
C 3 HOH   8   408 134 HOH   HOH A . 
C 3 HOH   9   409 230 HOH   HOH A . 
C 3 HOH   10  410 157 HOH   HOH A . 
C 3 HOH   11  411 180 HOH   HOH A . 
C 3 HOH   12  412 149 HOH   HOH A . 
C 3 HOH   13  413 133 HOH   HOH A . 
C 3 HOH   14  414 53  HOH   HOH A . 
C 3 HOH   15  415 113 HOH   HOH A . 
C 3 HOH   16  416 229 HOH   HOH A . 
C 3 HOH   17  417 317 HOH   HOH A . 
C 3 HOH   18  418 210 HOH   HOH A . 
C 3 HOH   19  419 46  HOH   HOH A . 
C 3 HOH   20  420 97  HOH   HOH A . 
C 3 HOH   21  421 241 HOH   HOH A . 
C 3 HOH   22  422 67  HOH   HOH A . 
C 3 HOH   23  423 80  HOH   HOH A . 
C 3 HOH   24  424 114 HOH   HOH A . 
C 3 HOH   25  425 68  HOH   HOH A . 
C 3 HOH   26  426 59  HOH   HOH A . 
C 3 HOH   27  427 95  HOH   HOH A . 
C 3 HOH   28  428 13  HOH   HOH A . 
C 3 HOH   29  429 64  HOH   HOH A . 
C 3 HOH   30  430 33  HOH   HOH A . 
C 3 HOH   31  431 16  HOH   HOH A . 
C 3 HOH   32  432 26  HOH   HOH A . 
C 3 HOH   33  433 63  HOH   HOH A . 
C 3 HOH   34  434 167 HOH   HOH A . 
C 3 HOH   35  435 48  HOH   HOH A . 
C 3 HOH   36  436 2   HOH   HOH A . 
C 3 HOH   37  437 245 HOH   HOH A . 
C 3 HOH   38  438 172 HOH   HOH A . 
C 3 HOH   39  439 202 HOH   HOH A . 
C 3 HOH   40  440 28  HOH   HOH A . 
C 3 HOH   41  441 50  HOH   HOH A . 
C 3 HOH   42  442 11  HOH   HOH A . 
C 3 HOH   43  443 100 HOH   HOH A . 
C 3 HOH   44  444 240 HOH   HOH A . 
C 3 HOH   45  445 145 HOH   HOH A . 
C 3 HOH   46  446 239 HOH   HOH A . 
C 3 HOH   47  447 232 HOH   HOH A . 
C 3 HOH   48  448 20  HOH   HOH A . 
C 3 HOH   49  449 76  HOH   HOH A . 
C 3 HOH   50  450 54  HOH   HOH A . 
C 3 HOH   51  451 265 HOH   HOH A . 
C 3 HOH   52  452 35  HOH   HOH A . 
C 3 HOH   53  453 183 HOH   HOH A . 
C 3 HOH   54  454 49  HOH   HOH A . 
C 3 HOH   55  455 164 HOH   HOH A . 
C 3 HOH   56  456 127 HOH   HOH A . 
C 3 HOH   57  457 238 HOH   HOH A . 
C 3 HOH   58  458 120 HOH   HOH A . 
C 3 HOH   59  459 281 HOH   HOH A . 
C 3 HOH   60  460 137 HOH   HOH A . 
C 3 HOH   61  461 177 HOH   HOH A . 
C 3 HOH   62  462 6   HOH   HOH A . 
C 3 HOH   63  463 81  HOH   HOH A . 
C 3 HOH   64  464 91  HOH   HOH A . 
C 3 HOH   65  465 44  HOH   HOH A . 
C 3 HOH   66  466 79  HOH   HOH A . 
C 3 HOH   67  467 148 HOH   HOH A . 
C 3 HOH   68  468 30  HOH   HOH A . 
C 3 HOH   69  469 226 HOH   HOH A . 
C 3 HOH   70  470 326 HOH   HOH A . 
C 3 HOH   71  471 62  HOH   HOH A . 
C 3 HOH   72  472 57  HOH   HOH A . 
C 3 HOH   73  473 41  HOH   HOH A . 
C 3 HOH   74  474 90  HOH   HOH A . 
C 3 HOH   75  475 7   HOH   HOH A . 
C 3 HOH   76  476 174 HOH   HOH A . 
C 3 HOH   77  477 138 HOH   HOH A . 
C 3 HOH   78  478 152 HOH   HOH A . 
C 3 HOH   79  479 15  HOH   HOH A . 
C 3 HOH   80  480 93  HOH   HOH A . 
C 3 HOH   81  481 267 HOH   HOH A . 
C 3 HOH   82  482 176 HOH   HOH A . 
C 3 HOH   83  483 268 HOH   HOH A . 
C 3 HOH   84  484 83  HOH   HOH A . 
C 3 HOH   85  485 21  HOH   HOH A . 
C 3 HOH   86  486 160 HOH   HOH A . 
C 3 HOH   87  487 65  HOH   HOH A . 
C 3 HOH   88  488 5   HOH   HOH A . 
C 3 HOH   89  489 209 HOH   HOH A . 
C 3 HOH   90  490 17  HOH   HOH A . 
C 3 HOH   91  491 4   HOH   HOH A . 
C 3 HOH   92  492 103 HOH   HOH A . 
C 3 HOH   93  493 150 HOH   HOH A . 
C 3 HOH   94  494 84  HOH   HOH A . 
C 3 HOH   95  495 312 HOH   HOH A . 
C 3 HOH   96  496 185 HOH   HOH A . 
C 3 HOH   97  497 78  HOH   HOH A . 
C 3 HOH   98  498 146 HOH   HOH A . 
C 3 HOH   99  499 121 HOH   HOH A . 
C 3 HOH   100 500 262 HOH   HOH A . 
C 3 HOH   101 501 96  HOH   HOH A . 
C 3 HOH   102 502 261 HOH   HOH A . 
C 3 HOH   103 503 109 HOH   HOH A . 
C 3 HOH   104 504 19  HOH   HOH A . 
C 3 HOH   105 505 85  HOH   HOH A . 
C 3 HOH   106 506 105 HOH   HOH A . 
C 3 HOH   107 507 166 HOH   HOH A . 
C 3 HOH   108 508 278 HOH   HOH A . 
C 3 HOH   109 509 27  HOH   HOH A . 
C 3 HOH   110 510 170 HOH   HOH A . 
C 3 HOH   111 511 89  HOH   HOH A . 
C 3 HOH   112 512 29  HOH   HOH A . 
C 3 HOH   113 513 51  HOH   HOH A . 
C 3 HOH   114 514 25  HOH   HOH A . 
C 3 HOH   115 515 9   HOH   HOH A . 
C 3 HOH   116 516 101 HOH   HOH A . 
C 3 HOH   117 517 18  HOH   HOH A . 
C 3 HOH   118 518 153 HOH   HOH A . 
C 3 HOH   119 519 252 HOH   HOH A . 
C 3 HOH   120 520 56  HOH   HOH A . 
C 3 HOH   121 521 260 HOH   HOH A . 
C 3 HOH   122 522 22  HOH   HOH A . 
C 3 HOH   123 523 288 HOH   HOH A . 
C 3 HOH   124 524 58  HOH   HOH A . 
C 3 HOH   125 525 142 HOH   HOH A . 
C 3 HOH   126 526 8   HOH   HOH A . 
C 3 HOH   127 527 24  HOH   HOH A . 
C 3 HOH   128 528 311 HOH   HOH A . 
C 3 HOH   129 529 98  HOH   HOH A . 
C 3 HOH   130 530 130 HOH   HOH A . 
C 3 HOH   131 531 168 HOH   HOH A . 
C 3 HOH   132 532 156 HOH   HOH A . 
C 3 HOH   133 533 47  HOH   HOH A . 
C 3 HOH   134 534 112 HOH   HOH A . 
C 3 HOH   135 535 61  HOH   HOH A . 
C 3 HOH   136 536 32  HOH   HOH A . 
C 3 HOH   137 537 300 HOH   HOH A . 
C 3 HOH   138 538 42  HOH   HOH A . 
C 3 HOH   139 539 282 HOH   HOH A . 
C 3 HOH   140 540 69  HOH   HOH A . 
C 3 HOH   141 541 10  HOH   HOH A . 
C 3 HOH   142 542 283 HOH   HOH A . 
C 3 HOH   143 543 314 HOH   HOH A . 
C 3 HOH   144 544 266 HOH   HOH A . 
C 3 HOH   145 545 123 HOH   HOH A . 
C 3 HOH   146 546 74  HOH   HOH A . 
C 3 HOH   147 547 40  HOH   HOH A . 
C 3 HOH   148 548 182 HOH   HOH A . 
C 3 HOH   149 549 242 HOH   HOH A . 
C 3 HOH   150 550 71  HOH   HOH A . 
C 3 HOH   151 551 144 HOH   HOH A . 
C 3 HOH   152 552 259 HOH   HOH A . 
C 3 HOH   153 553 249 HOH   HOH A . 
C 3 HOH   154 554 271 HOH   HOH A . 
C 3 HOH   155 555 117 HOH   HOH A . 
C 3 HOH   156 556 253 HOH   HOH A . 
C 3 HOH   157 557 178 HOH   HOH A . 
C 3 HOH   158 558 208 HOH   HOH A . 
C 3 HOH   159 559 201 HOH   HOH A . 
C 3 HOH   160 560 116 HOH   HOH A . 
C 3 HOH   161 561 276 HOH   HOH A . 
C 3 HOH   162 562 257 HOH   HOH A . 
C 3 HOH   163 563 320 HOH   HOH A . 
C 3 HOH   164 564 14  HOH   HOH A . 
C 3 HOH   165 565 72  HOH   HOH A . 
C 3 HOH   166 566 23  HOH   HOH A . 
C 3 HOH   167 567 140 HOH   HOH A . 
C 3 HOH   168 568 45  HOH   HOH A . 
C 3 HOH   169 569 143 HOH   HOH A . 
C 3 HOH   170 570 129 HOH   HOH A . 
C 3 HOH   171 571 159 HOH   HOH A . 
C 3 HOH   172 572 336 HOH   HOH A . 
C 3 HOH   173 573 193 HOH   HOH A . 
C 3 HOH   174 574 291 HOH   HOH A . 
C 3 HOH   175 575 313 HOH   HOH A . 
C 3 HOH   176 576 87  HOH   HOH A . 
C 3 HOH   177 577 126 HOH   HOH A . 
C 3 HOH   178 578 12  HOH   HOH A . 
C 3 HOH   179 579 318 HOH   HOH A . 
C 3 HOH   180 580 52  HOH   HOH A . 
C 3 HOH   181 581 277 HOH   HOH A . 
C 3 HOH   182 582 88  HOH   HOH A . 
C 3 HOH   183 583 37  HOH   HOH A . 
C 3 HOH   184 584 119 HOH   HOH A . 
C 3 HOH   185 585 181 HOH   HOH A . 
C 3 HOH   186 586 227 HOH   HOH A . 
C 3 HOH   187 587 124 HOH   HOH A . 
C 3 HOH   188 588 285 HOH   HOH A . 
C 3 HOH   189 589 188 HOH   HOH A . 
C 3 HOH   190 590 31  HOH   HOH A . 
C 3 HOH   191 591 224 HOH   HOH A . 
C 3 HOH   192 592 3   HOH   HOH A . 
C 3 HOH   193 593 195 HOH   HOH A . 
C 3 HOH   194 594 315 HOH   HOH A . 
C 3 HOH   195 595 77  HOH   HOH A . 
C 3 HOH   196 596 60  HOH   HOH A . 
C 3 HOH   197 597 106 HOH   HOH A . 
C 3 HOH   198 598 99  HOH   HOH A . 
C 3 HOH   199 599 36  HOH   HOH A . 
C 3 HOH   200 600 286 HOH   HOH A . 
C 3 HOH   201 601 102 HOH   HOH A . 
C 3 HOH   202 602 1   HOH   HOH A . 
C 3 HOH   203 603 296 HOH   HOH A . 
C 3 HOH   204 604 39  HOH   HOH A . 
C 3 HOH   205 605 333 HOH   HOH A . 
C 3 HOH   206 606 38  HOH   HOH A . 
C 3 HOH   207 607 34  HOH   HOH A . 
C 3 HOH   208 608 118 HOH   HOH A . 
C 3 HOH   209 609 287 HOH   HOH A . 
C 3 HOH   210 610 310 HOH   HOH A . 
C 3 HOH   211 611 173 HOH   HOH A . 
C 3 HOH   212 612 309 HOH   HOH A . 
C 3 HOH   213 613 169 HOH   HOH A . 
C 3 HOH   214 614 207 HOH   HOH A . 
C 3 HOH   215 615 327 HOH   HOH A . 
C 3 HOH   216 616 345 HOH   HOH A . 
C 3 HOH   217 617 284 HOH   HOH A . 
C 3 HOH   218 618 248 HOH   HOH A . 
C 3 HOH   219 619 254 HOH   HOH A . 
C 3 HOH   220 620 203 HOH   HOH A . 
C 3 HOH   221 621 128 HOH   HOH A . 
C 3 HOH   222 622 308 HOH   HOH A . 
C 3 HOH   223 623 338 HOH   HOH A . 
C 3 HOH   224 624 280 HOH   HOH A . 
C 3 HOH   225 625 298 HOH   HOH A . 
C 3 HOH   226 626 337 HOH   HOH A . 
C 3 HOH   227 627 225 HOH   HOH A . 
C 3 HOH   228 628 334 HOH   HOH A . 
C 3 HOH   229 629 323 HOH   HOH A . 
C 3 HOH   230 630 115 HOH   HOH A . 
C 3 HOH   231 631 289 HOH   HOH A . 
C 3 HOH   232 632 125 HOH   HOH A . 
C 3 HOH   233 633 212 HOH   HOH A . 
C 3 HOH   234 634 215 HOH   HOH A . 
C 3 HOH   235 635 141 HOH   HOH A . 
C 3 HOH   236 636 344 HOH   HOH A . 
C 3 HOH   237 637 155 HOH   HOH A . 
C 3 HOH   238 638 217 HOH   HOH A . 
C 3 HOH   239 639 214 HOH   HOH A . 
C 3 HOH   240 640 299 HOH   HOH A . 
C 3 HOH   241 641 122 HOH   HOH A . 
C 3 HOH   242 642 198 HOH   HOH A . 
C 3 HOH   243 643 86  HOH   HOH A . 
C 3 HOH   244 644 316 HOH   HOH A . 
C 3 HOH   245 645 73  HOH   HOH A . 
C 3 HOH   246 646 228 HOH   HOH A . 
C 3 HOH   247 647 342 HOH   HOH A . 
C 3 HOH   248 648 343 HOH   HOH A . 
C 3 HOH   249 649 236 HOH   HOH A . 
C 3 HOH   250 650 293 HOH   HOH A . 
C 3 HOH   251 651 306 HOH   HOH A . 
C 3 HOH   252 652 111 HOH   HOH A . 
C 3 HOH   253 653 329 HOH   HOH A . 
C 3 HOH   254 654 162 HOH   HOH A . 
C 3 HOH   255 655 219 HOH   HOH A . 
C 3 HOH   256 656 290 HOH   HOH A . 
C 3 HOH   257 657 275 HOH   HOH A . 
C 3 HOH   258 658 131 HOH   HOH A . 
C 3 HOH   259 659 246 HOH   HOH A . 
C 3 HOH   260 660 94  HOH   HOH A . 
C 3 HOH   261 661 213 HOH   HOH A . 
C 3 HOH   262 662 243 HOH   HOH A . 
C 3 HOH   263 663 233 HOH   HOH A . 
C 3 HOH   264 664 325 HOH   HOH A . 
C 3 HOH   265 665 255 HOH   HOH A . 
C 3 HOH   266 666 196 HOH   HOH A . 
C 3 HOH   267 667 43  HOH   HOH A . 
C 3 HOH   268 668 191 HOH   HOH A . 
C 3 HOH   269 669 247 HOH   HOH A . 
C 3 HOH   270 670 66  HOH   HOH A . 
C 3 HOH   271 671 332 HOH   HOH A . 
C 3 HOH   272 672 55  HOH   HOH A . 
C 3 HOH   273 673 331 HOH   HOH A . 
C 3 HOH   274 674 305 HOH   HOH A . 
C 3 HOH   275 675 184 HOH   HOH A . 
C 3 HOH   276 676 235 HOH   HOH A . 
C 3 HOH   277 677 220 HOH   HOH A . 
C 3 HOH   278 678 295 HOH   HOH A . 
C 3 HOH   279 679 179 HOH   HOH A . 
C 3 HOH   280 680 70  HOH   HOH A . 
C 3 HOH   281 681 189 HOH   HOH A . 
C 3 HOH   282 682 319 HOH   HOH A . 
C 3 HOH   283 683 263 HOH   HOH A . 
C 3 HOH   284 684 211 HOH   HOH A . 
C 3 HOH   285 685 107 HOH   HOH A . 
C 3 HOH   286 686 231 HOH   HOH A . 
C 3 HOH   287 687 321 HOH   HOH A . 
C 3 HOH   288 688 171 HOH   HOH A . 
C 3 HOH   289 689 154 HOH   HOH A . 
C 3 HOH   290 690 234 HOH   HOH A . 
C 3 HOH   291 691 108 HOH   HOH A . 
C 3 HOH   292 692 132 HOH   HOH A . 
C 3 HOH   293 693 304 HOH   HOH A . 
C 3 HOH   294 694 328 HOH   HOH A . 
C 3 HOH   295 695 244 HOH   HOH A . 
C 3 HOH   296 696 204 HOH   HOH A . 
C 3 HOH   297 697 279 HOH   HOH A . 
C 3 HOH   298 698 330 HOH   HOH A . 
C 3 HOH   299 699 270 HOH   HOH A . 
C 3 HOH   300 700 192 HOH   HOH A . 
C 3 HOH   301 701 307 HOH   HOH A . 
C 3 HOH   302 702 216 HOH   HOH A . 
C 3 HOH   303 703 258 HOH   HOH A . 
C 3 HOH   304 704 322 HOH   HOH A . 
C 3 HOH   305 705 297 HOH   HOH A . 
C 3 HOH   306 706 237 HOH   HOH A . 
C 3 HOH   307 707 273 HOH   HOH A . 
C 3 HOH   308 708 341 HOH   HOH A . 
C 3 HOH   309 709 206 HOH   HOH A . 
C 3 HOH   310 710 197 HOH   HOH A . 
C 3 HOH   311 711 186 HOH   HOH A . 
C 3 HOH   312 712 292 HOH   HOH A . 
C 3 HOH   313 713 165 HOH   HOH A . 
C 3 HOH   314 714 205 HOH   HOH A . 
C 3 HOH   315 715 256 HOH   HOH A . 
C 3 HOH   316 716 264 HOH   HOH A . 
C 3 HOH   317 717 223 HOH   HOH A . 
C 3 HOH   318 718 303 HOH   HOH A . 
C 3 HOH   319 719 151 HOH   HOH A . 
C 3 HOH   320 720 272 HOH   HOH A . 
C 3 HOH   321 721 75  HOH   HOH A . 
C 3 HOH   322 722 199 HOH   HOH A . 
C 3 HOH   323 723 104 HOH   HOH A . 
C 3 HOH   324 724 335 HOH   HOH A . 
C 3 HOH   325 725 82  HOH   HOH A . 
C 3 HOH   326 726 269 HOH   HOH A . 
C 3 HOH   327 727 222 HOH   HOH A . 
C 3 HOH   328 728 200 HOH   HOH A . 
C 3 HOH   329 729 187 HOH   HOH A . 
C 3 HOH   330 730 135 HOH   HOH A . 
C 3 HOH   331 731 110 HOH   HOH A . 
C 3 HOH   332 732 139 HOH   HOH A . 
C 3 HOH   333 733 158 HOH   HOH A . 
C 3 HOH   334 734 221 HOH   HOH A . 
C 3 HOH   335 735 190 HOH   HOH A . 
C 3 HOH   336 736 339 HOH   HOH A . 
C 3 HOH   337 737 147 HOH   HOH A . 
C 3 HOH   338 738 340 HOH   HOH A . 
C 3 HOH   339 739 161 HOH   HOH A . 
C 3 HOH   340 740 324 HOH   HOH A . 
C 3 HOH   341 741 175 HOH   HOH A . 
C 3 HOH   342 742 301 HOH   HOH A . 
C 3 HOH   343 743 274 HOH   HOH A . 
C 3 HOH   344 744 194 HOH   HOH A . 
C 3 HOH   345 745 302 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             595168.486 
_cell.length_a           66.177 
_cell.length_b           89.549 
_cell.length_c           100.432 
_cell.angle_beta         90.000 
_cell.angle_gamma        90.000 
_cell.angle_alpha        90.000 
_cell.entry_id           7HB0 
_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                         7HB0 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
# 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
_exptl.entry_id          7HB0 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_Matthews      2.88 
_exptl_crystal.density_percent_sol   57.23 
_exptl_crystal.density_meas          ? 
_exptl_crystal.description           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.pH              8.5 
_exptl_crystal_grow.temp            277 
_exptl_crystal_grow.pdbx_details    '100mM Tris-HCl pH 8.5, 22% PEG4000, 200mM MgCl2' 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_diffrn.id                     1 
_diffrn.crystal_id             1 
_diffrn.ambient_temp           100 
_diffrn.ambient_temp_details   ? 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               PIXEL 
_diffrn_detector.type                   'DECTRIS EIGER2 S 9M' 
_diffrn_detector.pdbx_collection_date   2023-07-22 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.pdbx_scattering_type             x-ray 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.monochromator                    Si111 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.97918 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.pdbx_synchrotron_beamline   BL02U1 
_diffrn_source.type                        'SSRF BEAMLINE BL02U1' 
_diffrn_source.pdbx_wavelength_list        0.97918 
_diffrn_source.pdbx_synchrotron_site       SSRF 
_diffrn_source.pdbx_wavelength             ? 
# 
_reflns.entry_id                     7HB0 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             66.840 
_reflns.d_resolution_high            1.780 
_reflns.number_obs                   28431 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         98.000 
_reflns.pdbx_Rmerge_I_obs            0.068 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        17.100 
_reflns.B_iso_Wilson_estimate        ? 
_reflns.pdbx_redundancy              6.600 
_reflns.pdbx_Rrim_I_all              0.073 
_reflns.pdbx_Rpim_I_all              0.026 
_reflns.pdbx_CC_half                 0.998 
_reflns.pdbx_netI_over_av_sigmaI     ? 
_reflns.pdbx_number_measured_all     188153 
_reflns.pdbx_scaling_rejects         26 
_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 1.780 1.870  ? 9742 3653 ? 0.251 ? ? ? 2.700 ? 2.900  ? ? ? ? ? ? 87.900 0.306 0.170 0.918 
1 2 5.620 66.840 ? 7688 1005 ? 0.040 ? ? ? 7.600 ? 33.200 ? ? ? ? ? ? 99.400 0.043 0.015 0.998 
# 
_refine.entry_id                                 7HB0 
_refine.pdbx_method_to_determine_struct          'FOURIER SYNTHESIS' 
_refine.ls_percent_reflns_R_free                 5.22 
_refine.pdbx_overall_phase_error                 19.1240 
_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                          0.1679 
_refine.B_iso_mean                               25.53 
_refine.ls_number_reflns_R_free                  1480 
_refine.ls_percent_reflns_obs                    97.48 
_refine.ls_R_factor_R_work                       0.1661 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_refine.ls_d_res_high                            1.78 
_refine.ls_number_reflns_obs                     28334 
_refine.pdbx_ls_sigma_F                          1.34 
_refine.ls_number_reflns_R_work                  26854 
_refine.ls_d_res_low                             28.61 
_refine.pdbx_stereochemistry_target_values       'GeoStd + Monomer Library + CDL v1.2' 
_refine.ls_R_factor_R_free                       0.1993 
_refine.overall_SU_ML                            0.2050 
_refine.pdbx_solvent_vdw_probe_radii             1.1000 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.solvent_model_param_ksol                 ? 
_refine.solvent_model_param_bsol                 ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.details                                  ? 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.overall_SU_B                             ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        1644 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         14 
_refine_hist.number_atoms_solvent             345 
_refine_hist.number_atoms_total               2003 
_refine_hist.d_res_high                       1.78 
_refine_hist.d_res_low                        28.61 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.type 
_refine_ls_restr.number 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
_refine_ls_restr.dev_ideal_target 
'X-RAY DIFFRACTION' f_bond_d           1685 0.0088 ? ? ? 
'X-RAY DIFFRACTION' f_angle_d          2270 0.9927 ? ? ? 
'X-RAY DIFFRACTION' f_chiral_restr     260  0.0624 ? ? ? 
'X-RAY DIFFRACTION' f_plane_restr      288  0.0063 ? ? ? 
'X-RAY DIFFRACTION' f_dihedral_angle_d 230  7.7075 ? ? ? 
# 
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' 1.78 1.84  2061 0.2732 83.07  0.3211 107 . . . . . 
'X-RAY DIFFRACTION' 1.84 1.90  2310 0.2291 94.07  0.2674 133 . . . . . 
'X-RAY DIFFRACTION' 1.90 1.98  2452 0.2322 98.47  0.2908 130 . . . . . 
'X-RAY DIFFRACTION' 1.98 2.07  2493 0.1547 99.89  0.1792 117 . . . . . 
'X-RAY DIFFRACTION' 2.07 2.18  2465 0.1597 100.00 0.1796 137 . . . . . 
'X-RAY DIFFRACTION' 2.18 2.31  2421 0.1935 97.21  0.2267 126 . . . . . 
'X-RAY DIFFRACTION' 2.31 2.49  2493 0.1664 100.00 0.2062 151 . . . . . 
'X-RAY DIFFRACTION' 2.49 2.74  2492 0.1717 100.00 0.1904 138 . . . . . 
'X-RAY DIFFRACTION' 2.74 3.14  2529 0.1689 99.96  0.2172 134 . . . . . 
'X-RAY DIFFRACTION' 3.14 3.95  2510 0.1476 99.59  0.1753 156 . . . . . 
'X-RAY DIFFRACTION' 3.95 28.61 2628 0.1393 99.71  0.1739 151 . . . . . 
# 
_struct.entry_id                  7HB0 
_struct.title                     'PanDDA analysis group deposition -- Crystal structure of HSP90N in complex with Fr12780' 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_details        ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HB0 
_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              7HB0 
_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 7HB0 MET A 1   ? UNP P07900 ? ? 'initiating methionine' 8   1 
1 7HB0 LEU A 230 ? UNP P07900 ? ? 'expression tag'        237 2 
1 7HB0 GLU A 231 ? UNP P07900 ? ? 'expression tag'        238 3 
1 7HB0 HIS A 232 ? UNP P07900 ? ? 'expression tag'        239 4 
1 7HB0 HIS A 233 ? UNP P07900 ? ? 'expression tag'        240 5 
1 7HB0 HIS A 234 ? UNP P07900 ? ? 'expression tag'        241 6 
1 7HB0 HIS A 235 ? UNP P07900 ? ? 'expression tag'        242 7 
1 7HB0 HIS A 236 ? UNP P07900 ? ? 'expression tag'        243 8 
1 7HB0 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 ? ALA A 117 ? ILE A 110 ALA A 124 1 ? 15 
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 VAL A 10  ? ALA A 14  ? VAL A 17  ALA A 21  
AA1 2 SER A 162 ? THR A 167 ? SER A 169 THR A 174 
AA1 3 TYR A 153 ? SER A 157 ? TYR A 160 SER A 164 
AA1 4 ALA A 138 ? LYS A 146 ? ALA A 145 LYS A 153 
AA1 5 GLY A 176 ? LEU A 183 ? GLY A 183 LEU A 190 
AA1 6 THR A 81  ? ASP A 86  ? THR A 88  ASP A 93  
AA1 7 ILE A 71  ? ASN A 76  ? ILE A 78  ASN A 83  
AA1 8 ILE A 211 ? LEU A 213 ? ILE A 218 LEU A 220 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N PHE A 13  ? N PHE A 20  O PHE A 163 ? O PHE A 170 
AA1 2 3 O ARG A 166 ? O ARG A 173 N ALA A 154 ? N ALA A 161 
AA1 3 4 O TRP A 155 ? O TRP A 162 N VAL A 143 ? N VAL A 150 
AA1 4 5 N THR A 142 ? N THR A 149 O ILE A 180 ? O ILE A 187 
AA1 5 6 O LEU A 181 ? O LEU A 188 N LEU A 82  ? N LEU A 89  
AA1 6 7 O 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                   7HB0 
_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 628 ? ? O A HOH 664 ? ? 1.86 
2  1 O A HOH 403 ? ? O A HOH 600 ? ? 1.89 
3  1 O A HOH 609 ? ? O A HOH 624 ? ? 1.92 
4  1 O A HOH 407 ? ? O A HOH 644 ? ? 1.96 
5  1 O A HOH 575 ? ? O A HOH 609 ? ? 1.99 
6  1 O A HOH 688 ? ? O A HOH 713 ? ? 2.00 
7  1 O A HOH 640 ? ? O A HOH 646 ? ? 2.07 
8  1 O A HOH 523 ? ? O A HOH 660 ? ? 2.08 
9  1 O A HOH 556 ? ? O A HOH 678 ? ? 2.08 
10 1 O A HOH 586 ? ? O A HOH 684 ? ? 2.09 
11 1 O A HOH 437 ? ? O A HOH 552 ? ? 2.12 
12 1 O A HOH 598 ? ? O A HOH 663 ? ? 2.13 
13 1 O A HOH 506 ? ? O A HOH 700 ? ? 2.19 
# 
_pdbx_validate_symm_contact.id                1 
_pdbx_validate_symm_contact.PDB_model_num     1 
_pdbx_validate_symm_contact.auth_atom_id_1    O 
_pdbx_validate_symm_contact.auth_asym_id_1    A 
_pdbx_validate_symm_contact.auth_comp_id_1    HOH 
_pdbx_validate_symm_contact.auth_seq_id_1     571 
_pdbx_validate_symm_contact.PDB_ins_code_1    ? 
_pdbx_validate_symm_contact.label_alt_id_1    ? 
_pdbx_validate_symm_contact.site_symmetry_1   1_555 
_pdbx_validate_symm_contact.auth_atom_id_2    O 
_pdbx_validate_symm_contact.auth_asym_id_2    A 
_pdbx_validate_symm_contact.auth_comp_id_2    HOH 
_pdbx_validate_symm_contact.auth_seq_id_2     588 
_pdbx_validate_symm_contact.PDB_ins_code_2    ? 
_pdbx_validate_symm_contact.label_alt_id_2    ? 
_pdbx_validate_symm_contact.site_symmetry_2   3_555 
_pdbx_validate_symm_contact.dist              1.89 
# 
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  ? ? -161.62 109.05  
2 1 ALA A 166 ? ? 62.95   -144.14 
# 
_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     701 
_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 12.3818076899  -17.9032731261 -18.7579888484 0.111783216071 0.180995151092  0.147320727166 
0.00394987949526  -0.020633375746    -0.024067282227  1.77395656384 0.98245740449  2.9818868636  -0.69502886467  -1.57884161149  
0.109060474749   0.0759445959998  -0.226691978798 -0.0932953939925 0.0166001335421 -0.0651671845002  -0.0778359154781 
0.0225025214552 0.126522092063   -0.0378394147649 
2 ? 'X-RAY DIFFRACTION' refined -5.23117474895 -6.29998490178 -20.9143873076 0.140370212167 0.122864107733  0.157675170312 
-0.0111470144589  -0.0043132356489   -0.0260665393143 1.12004922712 2.35964690635  3.13024548624 -0.835723799136 0.942317426943  
-1.62159149426   -0.0800697101703 0.0504362523801 0.093833045006   0.11215128782   -0.0194529648344  0.0535246208038  
-0.315434049855 0.160525473565   0.0110113638068  
3 ? 'X-RAY DIFFRACTION' refined -10.1368796944 -15.027003866  -25.2096107422 0.11829073197  0.134588479777  0.176975947177 
0.00920803758101  -0.0364300997199   -0.0328192259487 1.12020119432 2.04974082734  2.51566451324 0.161072344968  -0.293932808632 
-0.90643744326   0.0614729539491  0.0856031870278 -0.089899590849  -0.168370081986 -0.0152018843724  0.188401265409   
0.0881032361831 -0.138675579249  -0.0613023085808 
4 ? 'X-RAY DIFFRACTION' refined 10.7446596533  -7.52608779249 -17.8714873817 0.133860016648 0.212575685281  0.224285428522 
-0.0393679671849  0.00903776430308   -0.0464023074626 1.95321545222 2.54213824547  3.24042835958 0.323758735572  -0.386980469727 
0.323765134844   0.121622702099   -0.326647139442 0.255433804572   0.0468381129394 -0.119560809622   -0.153022613391  
-0.316859959748 0.53179176387    -0.0209990579099 
5 ? 'X-RAY DIFFRACTION' refined 0.930922760774 -19.3010082414 -27.9249100062 0.135082525808 0.0984423498105 0.148557624968 
0.00659676648562  -0.0191683341098   -0.0311856639867 1.95216077374 0.979139405844 1.22360096853 -0.634501501414 -0.315220748749 
-0.0573205614718 0.0545079085941  0.139917198186  -0.227062842995  -0.100674840705 -0.0172548644823  0.124059160693   
0.144819544202  0.0436305505525  -0.0356111369087 
6 ? 'X-RAY DIFFRACTION' refined -5.60210644814 -20.2207546693 -10.3995316203 0.139348840322 0.177100350828  0.138083661765 
-0.0162773311247  -0.010672928361    0.0145757497638  1.69682210201 1.54963467152  2.23485810883 -0.39710139596  -0.12673861959  
-0.256322616762  -0.030027098383  -0.227825341881 -0.184395446165  0.154750855254  0.000869652564711 0.0360986354216  
0.16455666314   -0.0519156258391 0.00628736033654 
7 ? 'X-RAY DIFFRACTION' refined -13.9838051161 -13.4147108855 -14.7443391836 0.147904011039 0.167873244167  0.137653190352 
0.000877008988514 -0.000782636648125 -0.0199445047512 2.68156806912 2.81877464309  2.84479329605 0.0150378152028 0.201876936355  
-0.181172317596  0.0693082364296  -0.244732111282 -0.0624079855413 0.394855806111  -0.0631205260803  -0.0429390326478 
-0.137875255995 -0.249476390081  0.0142029457337  
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
1 1 'X-RAY DIFFRACTION' A 16  A 1   A 40  A 25  . 
;chain 'A' and (resid 16 through 40 )
;
2 2 'X-RAY DIFFRACTION' A 41  A 26  A 65  A 50  . 
;chain 'A' and (resid 41 through 65 )
;
3 3 'X-RAY DIFFRACTION' A 66  A 51  A 99  A 84  . 
;chain 'A' and (resid 66 through 99 )
;
4 4 'X-RAY DIFFRACTION' A 100 A 85  A 136 A 121 . 
;chain 'A' and (resid 100 through 136 )
;
5 5 'X-RAY DIFFRACTION' A 137 A 122 A 182 A 167 . 
;chain 'A' and (resid 137 through 182 )
;
6 6 'X-RAY DIFFRACTION' A 183 A 168 A 210 A 195 . 
;chain 'A' and (resid 183 through 210 )
;
7 7 '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                       745 
_pdbx_distant_solvent_atoms.PDB_ins_code                      ? 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance   6.25 
_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 
A1AYK C2   C Y N 1   
A1AYK C1   C Y N 2   
A1AYK C10  C N N 3   
A1AYK C11  C N N 4   
A1AYK C3   C Y N 5   
A1AYK C4   C Y N 6   
A1AYK C5   C Y N 7   
A1AYK C6   C Y N 8   
A1AYK C7   C N N 9   
A1AYK C8   C N N 10  
A1AYK C9   C N N 11  
A1AYK N1   N N N 12  
A1AYK O1   O N N 13  
A1AYK O2   O N N 14  
A1AYK H2   H N N 15  
A1AYK H102 H N N 16  
A1AYK H103 H N N 17  
A1AYK H113 H N N 18  
A1AYK H112 H N N 19  
A1AYK H3   H N N 20  
A1AYK H4   H N N 21  
A1AYK H5   H N N 22  
A1AYK H7   H N N 23  
A1AYK H82  H N N 24  
A1AYK H83  H N N 25  
A1AYK H93  H N N 26  
A1AYK H92  H N N 27  
A1AYK H12  H N N 28  
A1AYK H11  H N N 29  
ALA   N    N N N 30  
ALA   CA   C N S 31  
ALA   C    C N N 32  
ALA   O    O N N 33  
ALA   CB   C N N 34  
ALA   OXT  O N N 35  
ALA   H    H N N 36  
ALA   H2   H N N 37  
ALA   HA   H N N 38  
ALA   HB1  H N N 39  
ALA   HB2  H N N 40  
ALA   HB3  H N N 41  
ALA   HXT  H N N 42  
ARG   N    N N N 43  
ARG   CA   C N S 44  
ARG   C    C N N 45  
ARG   O    O N N 46  
ARG   CB   C N N 47  
ARG   CG   C N N 48  
ARG   CD   C N N 49  
ARG   NE   N N N 50  
ARG   CZ   C N N 51  
ARG   NH1  N N N 52  
ARG   NH2  N N N 53  
ARG   OXT  O N N 54  
ARG   H    H N N 55  
ARG   H2   H N N 56  
ARG   HA   H N N 57  
ARG   HB2  H N N 58  
ARG   HB3  H N N 59  
ARG   HG2  H N N 60  
ARG   HG3  H N N 61  
ARG   HD2  H N N 62  
ARG   HD3  H N N 63  
ARG   HE   H N N 64  
ARG   HH11 H N N 65  
ARG   HH12 H N N 66  
ARG   HH21 H N N 67  
ARG   HH22 H N N 68  
ARG   HXT  H N N 69  
ASN   N    N N N 70  
ASN   CA   C N S 71  
ASN   C    C N N 72  
ASN   O    O N N 73  
ASN   CB   C N N 74  
ASN   CG   C N N 75  
ASN   OD1  O N N 76  
ASN   ND2  N N N 77  
ASN   OXT  O N N 78  
ASN   H    H N N 79  
ASN   H2   H N N 80  
ASN   HA   H N N 81  
ASN   HB2  H N N 82  
ASN   HB3  H N N 83  
ASN   HD21 H N N 84  
ASN   HD22 H N N 85  
ASN   HXT  H N N 86  
ASP   N    N N N 87  
ASP   CA   C N S 88  
ASP   C    C N N 89  
ASP   O    O N N 90  
ASP   CB   C N N 91  
ASP   CG   C N N 92  
ASP   OD1  O N N 93  
ASP   OD2  O N N 94  
ASP   OXT  O N N 95  
ASP   H    H N N 96  
ASP   H2   H N N 97  
ASP   HA   H N N 98  
ASP   HB2  H N N 99  
ASP   HB3  H N N 100 
ASP   HD2  H N N 101 
ASP   HXT  H N N 102 
GLN   N    N N N 103 
GLN   CA   C N S 104 
GLN   C    C N N 105 
GLN   O    O N N 106 
GLN   CB   C N N 107 
GLN   CG   C N N 108 
GLN   CD   C N N 109 
GLN   OE1  O N N 110 
GLN   NE2  N N N 111 
GLN   OXT  O N N 112 
GLN   H    H N N 113 
GLN   H2   H N N 114 
GLN   HA   H N N 115 
GLN   HB2  H N N 116 
GLN   HB3  H N N 117 
GLN   HG2  H N N 118 
GLN   HG3  H N N 119 
GLN   HE21 H N N 120 
GLN   HE22 H N N 121 
GLN   HXT  H N N 122 
GLU   N    N N N 123 
GLU   CA   C N S 124 
GLU   C    C N N 125 
GLU   O    O N N 126 
GLU   CB   C N N 127 
GLU   CG   C N N 128 
GLU   CD   C N N 129 
GLU   OE1  O N N 130 
GLU   OE2  O N N 131 
GLU   OXT  O N N 132 
GLU   H    H N N 133 
GLU   H2   H N N 134 
GLU   HA   H N N 135 
GLU   HB2  H N N 136 
GLU   HB3  H N N 137 
GLU   HG2  H N N 138 
GLU   HG3  H N N 139 
GLU   HE2  H N N 140 
GLU   HXT  H N N 141 
GLY   N    N N N 142 
GLY   CA   C N N 143 
GLY   C    C N N 144 
GLY   O    O N N 145 
GLY   OXT  O N N 146 
GLY   H    H N N 147 
GLY   H2   H N N 148 
GLY   HA2  H N N 149 
GLY   HA3  H N N 150 
GLY   HXT  H N N 151 
HIS   N    N N N 152 
HIS   CA   C N S 153 
HIS   C    C N N 154 
HIS   O    O N N 155 
HIS   CB   C N N 156 
HIS   CG   C Y N 157 
HIS   ND1  N Y N 158 
HIS   CD2  C Y N 159 
HIS   CE1  C Y N 160 
HIS   NE2  N Y N 161 
HIS   OXT  O N N 162 
HIS   H    H N N 163 
HIS   H2   H N N 164 
HIS   HA   H N N 165 
HIS   HB2  H N N 166 
HIS   HB3  H N N 167 
HIS   HD1  H N N 168 
HIS   HD2  H N N 169 
HIS   HE1  H N N 170 
HIS   HE2  H N N 171 
HIS   HXT  H N N 172 
HOH   O    O N N 173 
HOH   H1   H N N 174 
HOH   H2   H N N 175 
ILE   N    N N N 176 
ILE   CA   C N S 177 
ILE   C    C N N 178 
ILE   O    O N N 179 
ILE   CB   C N S 180 
ILE   CG1  C N N 181 
ILE   CG2  C N N 182 
ILE   CD1  C N N 183 
ILE   OXT  O N N 184 
ILE   H    H N N 185 
ILE   H2   H N N 186 
ILE   HA   H N N 187 
ILE   HB   H N N 188 
ILE   HG12 H N N 189 
ILE   HG13 H N N 190 
ILE   HG21 H N N 191 
ILE   HG22 H N N 192 
ILE   HG23 H N N 193 
ILE   HD11 H N N 194 
ILE   HD12 H N N 195 
ILE   HD13 H N N 196 
ILE   HXT  H N N 197 
LEU   N    N N N 198 
LEU   CA   C N S 199 
LEU   C    C N N 200 
LEU   O    O N N 201 
LEU   CB   C N N 202 
LEU   CG   C N N 203 
LEU   CD1  C N N 204 
LEU   CD2  C N N 205 
LEU   OXT  O N N 206 
LEU   H    H N N 207 
LEU   H2   H N N 208 
LEU   HA   H N N 209 
LEU   HB2  H N N 210 
LEU   HB3  H N N 211 
LEU   HG   H N N 212 
LEU   HD11 H N N 213 
LEU   HD12 H N N 214 
LEU   HD13 H N N 215 
LEU   HD21 H N N 216 
LEU   HD22 H N N 217 
LEU   HD23 H N N 218 
LEU   HXT  H N N 219 
LYS   N    N N N 220 
LYS   CA   C N S 221 
LYS   C    C N N 222 
LYS   O    O N N 223 
LYS   CB   C N N 224 
LYS   CG   C N N 225 
LYS   CD   C N N 226 
LYS   CE   C N N 227 
LYS   NZ   N N N 228 
LYS   OXT  O N N 229 
LYS   H    H N N 230 
LYS   H2   H N N 231 
LYS   HA   H N N 232 
LYS   HB2  H N N 233 
LYS   HB3  H N N 234 
LYS   HG2  H N N 235 
LYS   HG3  H N N 236 
LYS   HD2  H N N 237 
LYS   HD3  H N N 238 
LYS   HE2  H N N 239 
LYS   HE3  H N N 240 
LYS   HZ1  H N N 241 
LYS   HZ2  H N N 242 
LYS   HZ3  H N N 243 
LYS   HXT  H N N 244 
MET   N    N N N 245 
MET   CA   C N S 246 
MET   C    C N N 247 
MET   O    O N N 248 
MET   CB   C N N 249 
MET   CG   C N N 250 
MET   SD   S N N 251 
MET   CE   C N N 252 
MET   OXT  O N N 253 
MET   H    H N N 254 
MET   H2   H N N 255 
MET   HA   H N N 256 
MET   HB2  H N N 257 
MET   HB3  H N N 258 
MET   HG2  H N N 259 
MET   HG3  H N N 260 
MET   HE1  H N N 261 
MET   HE2  H N N 262 
MET   HE3  H N N 263 
MET   HXT  H N N 264 
PHE   N    N N N 265 
PHE   CA   C N S 266 
PHE   C    C N N 267 
PHE   O    O N N 268 
PHE   CB   C N N 269 
PHE   CG   C Y N 270 
PHE   CD1  C Y N 271 
PHE   CD2  C Y N 272 
PHE   CE1  C Y N 273 
PHE   CE2  C Y N 274 
PHE   CZ   C Y N 275 
PHE   OXT  O N N 276 
PHE   H    H N N 277 
PHE   H2   H N N 278 
PHE   HA   H N N 279 
PHE   HB2  H N N 280 
PHE   HB3  H N N 281 
PHE   HD1  H N N 282 
PHE   HD2  H N N 283 
PHE   HE1  H N N 284 
PHE   HE2  H N N 285 
PHE   HZ   H N N 286 
PHE   HXT  H N N 287 
PRO   N    N N N 288 
PRO   CA   C N S 289 
PRO   C    C N N 290 
PRO   O    O N N 291 
PRO   CB   C N N 292 
PRO   CG   C N N 293 
PRO   CD   C N N 294 
PRO   OXT  O N N 295 
PRO   H    H N N 296 
PRO   HA   H N N 297 
PRO   HB2  H N N 298 
PRO   HB3  H N N 299 
PRO   HG2  H N N 300 
PRO   HG3  H N N 301 
PRO   HD2  H N N 302 
PRO   HD3  H N N 303 
PRO   HXT  H N N 304 
SER   N    N N N 305 
SER   CA   C N S 306 
SER   C    C N N 307 
SER   O    O N N 308 
SER   CB   C N N 309 
SER   OG   O N N 310 
SER   OXT  O N N 311 
SER   H    H N N 312 
SER   H2   H N N 313 
SER   HA   H N N 314 
SER   HB2  H N N 315 
SER   HB3  H N N 316 
SER   HG   H N N 317 
SER   HXT  H N N 318 
THR   N    N N N 319 
THR   CA   C N S 320 
THR   C    C N N 321 
THR   O    O N N 322 
THR   CB   C N R 323 
THR   OG1  O N N 324 
THR   CG2  C N N 325 
THR   OXT  O N N 326 
THR   H    H N N 327 
THR   H2   H N N 328 
THR   HA   H N N 329 
THR   HB   H N N 330 
THR   HG1  H N N 331 
THR   HG21 H N N 332 
THR   HG22 H N N 333 
THR   HG23 H N N 334 
THR   HXT  H N N 335 
TRP   N    N N N 336 
TRP   CA   C N S 337 
TRP   C    C N N 338 
TRP   O    O N N 339 
TRP   CB   C N N 340 
TRP   CG   C Y N 341 
TRP   CD1  C Y N 342 
TRP   CD2  C Y N 343 
TRP   NE1  N Y N 344 
TRP   CE2  C Y N 345 
TRP   CE3  C Y N 346 
TRP   CZ2  C Y N 347 
TRP   CZ3  C Y N 348 
TRP   CH2  C Y N 349 
TRP   OXT  O N N 350 
TRP   H    H N N 351 
TRP   H2   H N N 352 
TRP   HA   H N N 353 
TRP   HB2  H N N 354 
TRP   HB3  H N N 355 
TRP   HD1  H N N 356 
TRP   HE1  H N N 357 
TRP   HE3  H N N 358 
TRP   HZ2  H N N 359 
TRP   HZ3  H N N 360 
TRP   HH2  H N N 361 
TRP   HXT  H N N 362 
TYR   N    N N N 363 
TYR   CA   C N S 364 
TYR   C    C N N 365 
TYR   O    O N N 366 
TYR   CB   C N N 367 
TYR   CG   C Y N 368 
TYR   CD1  C Y N 369 
TYR   CD2  C Y N 370 
TYR   CE1  C Y N 371 
TYR   CE2  C Y N 372 
TYR   CZ   C Y N 373 
TYR   OH   O N N 374 
TYR   OXT  O N N 375 
TYR   H    H N N 376 
TYR   H2   H N N 377 
TYR   HA   H N N 378 
TYR   HB2  H N N 379 
TYR   HB3  H N N 380 
TYR   HD1  H N N 381 
TYR   HD2  H N N 382 
TYR   HE1  H N N 383 
TYR   HE2  H N N 384 
TYR   HH   H N N 385 
TYR   HXT  H N N 386 
VAL   N    N N N 387 
VAL   CA   C N S 388 
VAL   C    C N N 389 
VAL   O    O N N 390 
VAL   CB   C N N 391 
VAL   CG1  C N N 392 
VAL   CG2  C N N 393 
VAL   OXT  O N N 394 
VAL   H    H N N 395 
VAL   H2   H N N 396 
VAL   HA   H N N 397 
VAL   HB   H N N 398 
VAL   HG11 H N N 399 
VAL   HG12 H N N 400 
VAL   HG13 H N N 401 
VAL   HG21 H N N 402 
VAL   HG22 H N N 403 
VAL   HG23 H N N 404 
VAL   HXT  H N N 405 
# 
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 
A1AYK N1  C1   sing N N 1   
A1AYK C1  C2   doub Y N 2   
A1AYK C1  C6   sing Y N 3   
A1AYK C2  C3   sing Y N 4   
A1AYK C3  C4   doub Y N 5   
A1AYK C4  C5   sing Y N 6   
A1AYK C5  C6   doub Y N 7   
A1AYK C6  O1   sing N N 8   
A1AYK O1  C7   sing N N 9   
A1AYK C7  C8   sing N N 10  
A1AYK C7  C11  sing N N 11  
A1AYK C8  C9   sing N N 12  
A1AYK C9  O2   sing N N 13  
A1AYK O2  C10  sing N N 14  
A1AYK C10 C11  sing N N 15  
A1AYK C2  H2   sing N N 16  
A1AYK C10 H102 sing N N 17  
A1AYK C10 H103 sing N N 18  
A1AYK C11 H113 sing N N 19  
A1AYK C11 H112 sing N N 20  
A1AYK C3  H3   sing N N 21  
A1AYK C4  H4   sing N N 22  
A1AYK C5  H5   sing N N 23  
A1AYK C7  H7   sing N N 24  
A1AYK C8  H82  sing N N 25  
A1AYK C8  H83  sing N N 26  
A1AYK C9  H93  sing N N 27  
A1AYK C9  H92  sing N N 28  
A1AYK N1  H12  sing N N 29  
A1AYK N1  H11  sing N N 30  
ALA   N   CA   sing N N 31  
ALA   N   H    sing N N 32  
ALA   N   H2   sing N N 33  
ALA   CA  C    sing N N 34  
ALA   CA  CB   sing N N 35  
ALA   CA  HA   sing N N 36  
ALA   C   O    doub N N 37  
ALA   C   OXT  sing N N 38  
ALA   CB  HB1  sing N N 39  
ALA   CB  HB2  sing N N 40  
ALA   CB  HB3  sing N N 41  
ALA   OXT HXT  sing N N 42  
ARG   N   CA   sing N N 43  
ARG   N   H    sing N N 44  
ARG   N   H2   sing N N 45  
ARG   CA  C    sing N N 46  
ARG   CA  CB   sing N N 47  
ARG   CA  HA   sing N N 48  
ARG   C   O    doub N N 49  
ARG   C   OXT  sing N N 50  
ARG   CB  CG   sing N N 51  
ARG   CB  HB2  sing N N 52  
ARG   CB  HB3  sing N N 53  
ARG   CG  CD   sing N N 54  
ARG   CG  HG2  sing N N 55  
ARG   CG  HG3  sing N N 56  
ARG   CD  NE   sing N N 57  
ARG   CD  HD2  sing N N 58  
ARG   CD  HD3  sing N N 59  
ARG   NE  CZ   sing N N 60  
ARG   NE  HE   sing N N 61  
ARG   CZ  NH1  sing N N 62  
ARG   CZ  NH2  doub N N 63  
ARG   NH1 HH11 sing N N 64  
ARG   NH1 HH12 sing N N 65  
ARG   NH2 HH21 sing N N 66  
ARG   NH2 HH22 sing N N 67  
ARG   OXT HXT  sing N N 68  
ASN   N   CA   sing N N 69  
ASN   N   H    sing N N 70  
ASN   N   H2   sing N N 71  
ASN   CA  C    sing N N 72  
ASN   CA  CB   sing N N 73  
ASN   CA  HA   sing N N 74  
ASN   C   O    doub N N 75  
ASN   C   OXT  sing N N 76  
ASN   CB  CG   sing N N 77  
ASN   CB  HB2  sing N N 78  
ASN   CB  HB3  sing N N 79  
ASN   CG  OD1  doub N N 80  
ASN   CG  ND2  sing N N 81  
ASN   ND2 HD21 sing N N 82  
ASN   ND2 HD22 sing N N 83  
ASN   OXT HXT  sing N N 84  
ASP   N   CA   sing N N 85  
ASP   N   H    sing N N 86  
ASP   N   H2   sing N N 87  
ASP   CA  C    sing N N 88  
ASP   CA  CB   sing N N 89  
ASP   CA  HA   sing N N 90  
ASP   C   O    doub N N 91  
ASP   C   OXT  sing N N 92  
ASP   CB  CG   sing N N 93  
ASP   CB  HB2  sing N N 94  
ASP   CB  HB3  sing N N 95  
ASP   CG  OD1  doub N N 96  
ASP   CG  OD2  sing N N 97  
ASP   OD2 HD2  sing N N 98  
ASP   OXT HXT  sing N N 99  
GLN   N   CA   sing N N 100 
GLN   N   H    sing N N 101 
GLN   N   H2   sing N N 102 
GLN   CA  C    sing N N 103 
GLN   CA  CB   sing N N 104 
GLN   CA  HA   sing N N 105 
GLN   C   O    doub N N 106 
GLN   C   OXT  sing N N 107 
GLN   CB  CG   sing N N 108 
GLN   CB  HB2  sing N N 109 
GLN   CB  HB3  sing N N 110 
GLN   CG  CD   sing N N 111 
GLN   CG  HG2  sing N N 112 
GLN   CG  HG3  sing N N 113 
GLN   CD  OE1  doub N N 114 
GLN   CD  NE2  sing N N 115 
GLN   NE2 HE21 sing N N 116 
GLN   NE2 HE22 sing N N 117 
GLN   OXT HXT  sing N N 118 
GLU   N   CA   sing N N 119 
GLU   N   H    sing N N 120 
GLU   N   H2   sing N N 121 
GLU   CA  C    sing N N 122 
GLU   CA  CB   sing N N 123 
GLU   CA  HA   sing N N 124 
GLU   C   O    doub N N 125 
GLU   C   OXT  sing N N 126 
GLU   CB  CG   sing N N 127 
GLU   CB  HB2  sing N N 128 
GLU   CB  HB3  sing N N 129 
GLU   CG  CD   sing N N 130 
GLU   CG  HG2  sing N N 131 
GLU   CG  HG3  sing N N 132 
GLU   CD  OE1  doub N N 133 
GLU   CD  OE2  sing N N 134 
GLU   OE2 HE2  sing N N 135 
GLU   OXT HXT  sing N N 136 
GLY   N   CA   sing N N 137 
GLY   N   H    sing N N 138 
GLY   N   H2   sing N N 139 
GLY   CA  C    sing N N 140 
GLY   CA  HA2  sing N N 141 
GLY   CA  HA3  sing N N 142 
GLY   C   O    doub N N 143 
GLY   C   OXT  sing N N 144 
GLY   OXT HXT  sing N N 145 
HIS   N   CA   sing N N 146 
HIS   N   H    sing N N 147 
HIS   N   H2   sing N N 148 
HIS   CA  C    sing N N 149 
HIS   CA  CB   sing N N 150 
HIS   CA  HA   sing N N 151 
HIS   C   O    doub N N 152 
HIS   C   OXT  sing N N 153 
HIS   CB  CG   sing N N 154 
HIS   CB  HB2  sing N N 155 
HIS   CB  HB3  sing N N 156 
HIS   CG  ND1  sing Y N 157 
HIS   CG  CD2  doub Y N 158 
HIS   ND1 CE1  doub Y N 159 
HIS   ND1 HD1  sing N N 160 
HIS   CD2 NE2  sing Y N 161 
HIS   CD2 HD2  sing N N 162 
HIS   CE1 NE2  sing Y N 163 
HIS   CE1 HE1  sing N N 164 
HIS   NE2 HE2  sing N N 165 
HIS   OXT HXT  sing N N 166 
HOH   O   H1   sing N N 167 
HOH   O   H2   sing N N 168 
ILE   N   CA   sing N N 169 
ILE   N   H    sing N N 170 
ILE   N   H2   sing N N 171 
ILE   CA  C    sing N N 172 
ILE   CA  CB   sing N N 173 
ILE   CA  HA   sing N N 174 
ILE   C   O    doub N N 175 
ILE   C   OXT  sing N N 176 
ILE   CB  CG1  sing N N 177 
ILE   CB  CG2  sing N N 178 
ILE   CB  HB   sing N N 179 
ILE   CG1 CD1  sing N N 180 
ILE   CG1 HG12 sing N N 181 
ILE   CG1 HG13 sing N N 182 
ILE   CG2 HG21 sing N N 183 
ILE   CG2 HG22 sing N N 184 
ILE   CG2 HG23 sing N N 185 
ILE   CD1 HD11 sing N N 186 
ILE   CD1 HD12 sing N N 187 
ILE   CD1 HD13 sing N N 188 
ILE   OXT HXT  sing N N 189 
LEU   N   CA   sing N N 190 
LEU   N   H    sing N N 191 
LEU   N   H2   sing N N 192 
LEU   CA  C    sing N N 193 
LEU   CA  CB   sing N N 194 
LEU   CA  HA   sing N N 195 
LEU   C   O    doub N N 196 
LEU   C   OXT  sing N N 197 
LEU   CB  CG   sing N N 198 
LEU   CB  HB2  sing N N 199 
LEU   CB  HB3  sing N N 200 
LEU   CG  CD1  sing N N 201 
LEU   CG  CD2  sing N N 202 
LEU   CG  HG   sing N N 203 
LEU   CD1 HD11 sing N N 204 
LEU   CD1 HD12 sing N N 205 
LEU   CD1 HD13 sing N N 206 
LEU   CD2 HD21 sing N N 207 
LEU   CD2 HD22 sing N N 208 
LEU   CD2 HD23 sing N N 209 
LEU   OXT HXT  sing N N 210 
LYS   N   CA   sing N N 211 
LYS   N   H    sing N N 212 
LYS   N   H2   sing N N 213 
LYS   CA  C    sing N N 214 
LYS   CA  CB   sing N N 215 
LYS   CA  HA   sing N N 216 
LYS   C   O    doub N N 217 
LYS   C   OXT  sing N N 218 
LYS   CB  CG   sing N N 219 
LYS   CB  HB2  sing N N 220 
LYS   CB  HB3  sing N N 221 
LYS   CG  CD   sing N N 222 
LYS   CG  HG2  sing N N 223 
LYS   CG  HG3  sing N N 224 
LYS   CD  CE   sing N N 225 
LYS   CD  HD2  sing N N 226 
LYS   CD  HD3  sing N N 227 
LYS   CE  NZ   sing N N 228 
LYS   CE  HE2  sing N N 229 
LYS   CE  HE3  sing N N 230 
LYS   NZ  HZ1  sing N N 231 
LYS   NZ  HZ2  sing N N 232 
LYS   NZ  HZ3  sing N N 233 
LYS   OXT HXT  sing N N 234 
MET   N   CA   sing N N 235 
MET   N   H    sing N N 236 
MET   N   H2   sing N N 237 
MET   CA  C    sing N N 238 
MET   CA  CB   sing N N 239 
MET   CA  HA   sing N N 240 
MET   C   O    doub N N 241 
MET   C   OXT  sing N N 242 
MET   CB  CG   sing N N 243 
MET   CB  HB2  sing N N 244 
MET   CB  HB3  sing N N 245 
MET   CG  SD   sing N N 246 
MET   CG  HG2  sing N N 247 
MET   CG  HG3  sing N N 248 
MET   SD  CE   sing N N 249 
MET   CE  HE1  sing N N 250 
MET   CE  HE2  sing N N 251 
MET   CE  HE3  sing N N 252 
MET   OXT HXT  sing N N 253 
PHE   N   CA   sing N N 254 
PHE   N   H    sing N N 255 
PHE   N   H2   sing N N 256 
PHE   CA  C    sing N N 257 
PHE   CA  CB   sing N N 258 
PHE   CA  HA   sing N N 259 
PHE   C   O    doub N N 260 
PHE   C   OXT  sing N N 261 
PHE   CB  CG   sing N N 262 
PHE   CB  HB2  sing N N 263 
PHE   CB  HB3  sing N N 264 
PHE   CG  CD1  doub Y N 265 
PHE   CG  CD2  sing Y N 266 
PHE   CD1 CE1  sing Y N 267 
PHE   CD1 HD1  sing N N 268 
PHE   CD2 CE2  doub Y N 269 
PHE   CD2 HD2  sing N N 270 
PHE   CE1 CZ   doub Y N 271 
PHE   CE1 HE1  sing N N 272 
PHE   CE2 CZ   sing Y N 273 
PHE   CE2 HE2  sing N N 274 
PHE   CZ  HZ   sing N N 275 
PHE   OXT HXT  sing N N 276 
PRO   N   CA   sing N N 277 
PRO   N   CD   sing N N 278 
PRO   N   H    sing N N 279 
PRO   CA  C    sing N N 280 
PRO   CA  CB   sing N N 281 
PRO   CA  HA   sing N N 282 
PRO   C   O    doub N N 283 
PRO   C   OXT  sing N N 284 
PRO   CB  CG   sing N N 285 
PRO   CB  HB2  sing N N 286 
PRO   CB  HB3  sing N N 287 
PRO   CG  CD   sing N N 288 
PRO   CG  HG2  sing N N 289 
PRO   CG  HG3  sing N N 290 
PRO   CD  HD2  sing N N 291 
PRO   CD  HD3  sing N N 292 
PRO   OXT HXT  sing N N 293 
SER   N   CA   sing N N 294 
SER   N   H    sing N N 295 
SER   N   H2   sing N N 296 
SER   CA  C    sing N N 297 
SER   CA  CB   sing N N 298 
SER   CA  HA   sing N N 299 
SER   C   O    doub N N 300 
SER   C   OXT  sing N N 301 
SER   CB  OG   sing N N 302 
SER   CB  HB2  sing N N 303 
SER   CB  HB3  sing N N 304 
SER   OG  HG   sing N N 305 
SER   OXT HXT  sing N N 306 
THR   N   CA   sing N N 307 
THR   N   H    sing N N 308 
THR   N   H2   sing N N 309 
THR   CA  C    sing N N 310 
THR   CA  CB   sing N N 311 
THR   CA  HA   sing N N 312 
THR   C   O    doub N N 313 
THR   C   OXT  sing N N 314 
THR   CB  OG1  sing N N 315 
THR   CB  CG2  sing N N 316 
THR   CB  HB   sing N N 317 
THR   OG1 HG1  sing N N 318 
THR   CG2 HG21 sing N N 319 
THR   CG2 HG22 sing N N 320 
THR   CG2 HG23 sing N N 321 
THR   OXT HXT  sing N N 322 
TRP   N   CA   sing N N 323 
TRP   N   H    sing N N 324 
TRP   N   H2   sing N N 325 
TRP   CA  C    sing N N 326 
TRP   CA  CB   sing N N 327 
TRP   CA  HA   sing N N 328 
TRP   C   O    doub N N 329 
TRP   C   OXT  sing N N 330 
TRP   CB  CG   sing N N 331 
TRP   CB  HB2  sing N N 332 
TRP   CB  HB3  sing N N 333 
TRP   CG  CD1  doub Y N 334 
TRP   CG  CD2  sing Y N 335 
TRP   CD1 NE1  sing Y N 336 
TRP   CD1 HD1  sing N N 337 
TRP   CD2 CE2  doub Y N 338 
TRP   CD2 CE3  sing Y N 339 
TRP   NE1 CE2  sing Y N 340 
TRP   NE1 HE1  sing N N 341 
TRP   CE2 CZ2  sing Y N 342 
TRP   CE3 CZ3  doub Y N 343 
TRP   CE3 HE3  sing N N 344 
TRP   CZ2 CH2  doub Y N 345 
TRP   CZ2 HZ2  sing N N 346 
TRP   CZ3 CH2  sing Y N 347 
TRP   CZ3 HZ3  sing N N 348 
TRP   CH2 HH2  sing N N 349 
TRP   OXT HXT  sing N N 350 
TYR   N   CA   sing N N 351 
TYR   N   H    sing N N 352 
TYR   N   H2   sing N N 353 
TYR   CA  C    sing N N 354 
TYR   CA  CB   sing N N 355 
TYR   CA  HA   sing N N 356 
TYR   C   O    doub N N 357 
TYR   C   OXT  sing N N 358 
TYR   CB  CG   sing N N 359 
TYR   CB  HB2  sing N N 360 
TYR   CB  HB3  sing N N 361 
TYR   CG  CD1  doub Y N 362 
TYR   CG  CD2  sing Y N 363 
TYR   CD1 CE1  sing Y N 364 
TYR   CD1 HD1  sing N N 365 
TYR   CD2 CE2  doub Y N 366 
TYR   CD2 HD2  sing N N 367 
TYR   CE1 CZ   doub Y N 368 
TYR   CE1 HE1  sing N N 369 
TYR   CE2 CZ   sing Y N 370 
TYR   CE2 HE2  sing N N 371 
TYR   CZ  OH   sing N N 372 
TYR   OH  HH   sing N N 373 
TYR   OXT HXT  sing N N 374 
VAL   N   CA   sing N N 375 
VAL   N   H    sing N N 376 
VAL   N   H2   sing N N 377 
VAL   CA  C    sing N N 378 
VAL   CA  CB   sing N N 379 
VAL   CA  HA   sing N N 380 
VAL   C   O    doub N N 381 
VAL   C   OXT  sing N N 382 
VAL   CB  CG1  sing N N 383 
VAL   CB  CG2  sing N N 384 
VAL   CB  HB   sing N N 385 
VAL   CG1 HG11 sing N N 386 
VAL   CG1 HG12 sing N N 387 
VAL   CG1 HG13 sing N N 388 
VAL   CG2 HG21 sing N N 389 
VAL   CG2 HG22 sing N N 390 
VAL   CG2 HG23 sing N N 391 
VAL   OXT HXT  sing N N 392 
# 
_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                    7HB0 
_atom_sites.fract_transf_matrix[1][1]   0.015111 
_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]   0.011167 
_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]   0.009957 
_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   ? 4.44020   -28.62876 -39.09940 1.000 37.77461  ? 16  GLU   A N   1 
ATOM   2    C CA  . GLU   A 1 9   ? 5.69999   -27.91300 -39.24756 1.000 53.19997  ? 16  GLU   A CA  1 
ATOM   3    C C   . GLU   A 1 9   ? 5.92147   -26.97872 -38.04962 1.000 39.71892  ? 16  GLU   A C   1 
ATOM   4    O O   . GLU   A 1 9   ? 5.18449   -26.00773 -37.86373 1.000 40.57307  ? 16  GLU   A O   1 
ATOM   5    C CB  . GLU   A 1 9   ? 5.70542   -27.12829 -40.56077 1.000 60.79002  ? 16  GLU   A CB  1 
ATOM   6    C CG  . GLU   A 1 9   ? 7.09429   -26.86155 -41.11949 1.000 71.79296  ? 16  GLU   A CG  1 
ATOM   7    C CD  . GLU   A 1 9   ? 7.71147   -25.57652 -40.59089 1.000 80.87000  ? 16  GLU   A CD  1 
ATOM   8    O OE1 . GLU   A 1 9   ? 8.81520   -25.20936 -41.04831 1.000 69.63798  ? 16  GLU   A OE1 1 
ATOM   9    O OE2 . GLU   A 1 9   ? 7.09646   -24.92552 -39.72102 1.000 76.82544  ? 16  GLU   A OE2 1 
ATOM   10   N N   . VAL   A 1 10  ? 6.94826   -27.26398 -37.25031 1.000 26.71764  ? 17  VAL   A N   1 
ATOM   11   C CA  . VAL   A 1 10  ? 7.18447   -26.59120 -35.97480 1.000 20.57823  ? 17  VAL   A CA  1 
ATOM   12   C C   . VAL   A 1 10  ? 8.54653   -25.91639 -36.03626 1.000 25.95450  ? 17  VAL   A C   1 
ATOM   13   O O   . VAL   A 1 10  ? 9.54489   -26.56154 -36.37078 1.000 26.63274  ? 17  VAL   A O   1 
ATOM   14   C CB  . VAL   A 1 10  ? 7.13737   -27.58651 -34.80316 1.000 30.39729  ? 17  VAL   A CB  1 
ATOM   15   C CG1 . VAL   A 1 10  ? 7.49620   -26.89846 -33.49066 1.000 28.06135  ? 17  VAL   A CG1 1 
ATOM   16   C CG2 . VAL   A 1 10  ? 5.79114   -28.29158 -34.75240 1.000 38.36599  ? 17  VAL   A CG2 1 
ATOM   17   N N   . GLU   A 1 11  ? 8.59417   -24.63149 -35.70472 1.000 19.37811  ? 18  GLU   A N   1 
ATOM   18   C CA  . GLU   A 1 11  ? 9.84458   -23.88238 -35.65009 1.000 18.33765  ? 18  GLU   A CA  1 
ATOM   19   C C   . GLU   A 1 11  ? 10.27647  -23.74167 -34.19579 1.000 17.24249  ? 18  GLU   A C   1 
ATOM   20   O O   . GLU   A 1 11  ? 9.46096   -23.38656 -33.34582 1.000 16.84344  ? 18  GLU   A O   1 
ATOM   21   C CB  . GLU   A 1 11  ? 9.66367   -22.51454 -36.30546 1.000 21.49809  ? 18  GLU   A CB  1 
ATOM   22   C CG  . GLU   A 1 11  ? 9.47497   -22.60525 -37.80595 1.000 21.86556  ? 18  GLU   A CG  1 
ATOM   23   C CD  . GLU   A 1 11  ? 9.19074   -21.24617 -38.43222 1.000 37.61748  ? 18  GLU   A CD  1 
ATOM   24   O OE1 . GLU   A 1 11  ? 8.07488   -20.72179 -38.24362 1.000 33.60153  ? 18  GLU   A OE1 1 
ATOM   25   O OE2 . GLU   A 1 11  ? 10.08349  -20.67988 -39.09242 1.000 37.93584  ? 18  GLU   A OE2 1 
ATOM   26   N N   . THR   A 1 12  ? 11.54240  -24.06307 -33.90456 1.000 15.53936  ? 19  THR   A N   1 
ATOM   27   C CA  . THR   A 1 12  ? 12.08413  -23.95575 -32.55688 1.000 14.76095  ? 19  THR   A CA  1 
ATOM   28   C C   . THR   A 1 12  ? 13.06452  -22.79589 -32.49772 1.000 16.56327  ? 19  THR   A C   1 
ATOM   29   O O   . THR   A 1 12  ? 13.93451  -22.67362 -33.36480 1.000 14.24339  ? 19  THR   A O   1 
ATOM   30   C CB  . THR   A 1 12  ? 12.76915  -25.25996 -32.13595 1.000 16.76848  ? 19  THR   A CB  1 
ATOM   31   O OG1 . THR   A 1 12  ? 11.84124  -26.33876 -32.28135 1.000 16.84321  ? 19  THR   A OG1 1 
ATOM   32   C CG2 . THR   A 1 12  ? 13.26005  -25.18045 -30.68075 1.000 18.44566  ? 19  THR   A CG2 1 
ATOM   33   N N   . PHE   A 1 13  ? 12.93421  -21.96964 -31.46021 1.000 13.79975  ? 20  PHE   A N   1 
ATOM   34   C CA  . PHE   A 1 13  ? 13.69368  -20.73904 -31.29982 1.000 14.64143  ? 20  PHE   A CA  1 
ATOM   35   C C   . PHE   A 1 13  ? 14.37162  -20.73955 -29.94057 1.000 17.57888  ? 20  PHE   A C   1 
ATOM   36   O O   . PHE   A 1 13  ? 13.82838  -21.25818 -28.96491 1.000 16.41199  ? 20  PHE   A O   1 
ATOM   37   C CB  . PHE   A 1 13  ? 12.79413  -19.48421 -31.35944 1.000 14.73311  ? 20  PHE   A CB  1 
ATOM   38   C CG  . PHE   A 1 13  ? 12.06874  -19.28283 -32.66759 1.000 17.14507  ? 20  PHE   A CG  1 
ATOM   39   C CD1 . PHE   A 1 13  ? 10.84702  -19.89269 -32.90592 1.000 17.36124  ? 20  PHE   A CD1 1 
ATOM   40   C CD2 . PHE   A 1 13  ? 12.60251  -18.44878 -33.65058 1.000 17.99479  ? 20  PHE   A CD2 1 
ATOM   41   C CE1 . PHE   A 1 13  ? 10.18439  -19.68912 -34.10445 1.000 18.58265  ? 20  PHE   A CE1 1 
ATOM   42   C CE2 . PHE   A 1 13  ? 11.93005  -18.23104 -34.85693 1.000 21.72570  ? 20  PHE   A CE2 1 
ATOM   43   C CZ  . PHE   A 1 13  ? 10.72015  -18.85702 -35.07968 1.000 18.46657  ? 20  PHE   A CZ  1 
ATOM   44   N N   . ALA   A 1 14  ? 15.54590  -20.12079 -29.86436 1.000 15.73489  ? 21  ALA   A N   1 
ATOM   45   C CA  . ALA   A 1 14  ? 16.17658  -19.87444 -28.57518 1.000 14.34809  ? 21  ALA   A CA  1 
ATOM   46   C C   . ALA   A 1 14  ? 15.68395  -18.55692 -27.99039 1.000 18.76030  ? 21  ALA   A C   1 
ATOM   47   O O   . ALA   A 1 14  ? 15.58971  -17.55272 -28.69763 1.000 16.18374  ? 21  ALA   A O   1 
ATOM   48   C CB  . ALA   A 1 14  ? 17.70105  -19.82664 -28.71945 1.000 15.83396  ? 21  ALA   A CB  1 
ATOM   49   N N   . PHE   A 1 15  ? 15.36809  -18.55506 -26.69103 1.000 12.95712  ? 22  PHE   A N   1 
ATOM   50   C CA  . PHE   A 1 15  ? 15.14569  -17.27252 -26.03597 1.000 14.69509  ? 22  PHE   A CA  1 
ATOM   51   C C   . PHE   A 1 15  ? 16.41683  -16.43617 -26.10629 1.000 15.26144  ? 22  PHE   A C   1 
ATOM   52   O O   . PHE   A 1 15  ? 17.53884  -16.95906 -26.03619 1.000 16.58026  ? 22  PHE   A O   1 
ATOM   53   C CB  . PHE   A 1 15  ? 14.76653  -17.45198 -24.55656 1.000 13.73869  ? 22  PHE   A CB  1 
ATOM   54   C CG  . PHE   A 1 15  ? 13.36353  -17.97937 -24.33611 1.000 13.11124  ? 22  PHE   A CG  1 
ATOM   55   C CD1 . PHE   A 1 15  ? 12.25893  -17.19696 -24.64050 1.000 14.53280  ? 22  PHE   A CD1 1 
ATOM   56   C CD2 . PHE   A 1 15  ? 13.16418  -19.26780 -23.84794 1.000 11.67538  ? 22  PHE   A CD2 1 
ATOM   57   C CE1 . PHE   A 1 15  ? 10.96293  -17.66416 -24.43683 1.000 12.53134  ? 22  PHE   A CE1 1 
ATOM   58   C CE2 . PHE   A 1 15  ? 11.87410  -19.76149 -23.65878 1.000 11.68746  ? 22  PHE   A CE2 1 
ATOM   59   C CZ  . PHE   A 1 15  ? 10.77022  -18.95397 -23.94190 1.000 14.35800  ? 22  PHE   A CZ  1 
ATOM   60   N N   . GLN   A 1 16  ? 16.24452  -15.12389 -26.23358 1.000 14.46174  ? 23  GLN   A N   1 
ATOM   61   C CA  . GLN   A 1 16  ? 17.36739  -14.23779 -25.92686 1.000 19.56703  ? 23  GLN   A CA  1 
ATOM   62   C C   . GLN   A 1 16  ? 17.89890  -14.52089 -24.52360 1.000 15.98528  ? 23  GLN   A C   1 
ATOM   63   O O   . GLN   A 1 16  ? 17.14302  -14.86240 -23.60964 1.000 16.33971  ? 23  GLN   A O   1 
ATOM   64   C CB  . GLN   A 1 16  ? 16.95126  -12.77406 -26.03422 1.000 18.65342  ? 23  GLN   A CB  1 
ATOM   65   C CG  . GLN   A 1 16  ? 16.57228  -12.34496 -27.42303 1.000 24.89038  ? 23  GLN   A CG  1 
ATOM   66   C CD  . GLN   A 1 16  ? 16.02724  -10.93136 -27.43938 1.000 35.32353  ? 23  GLN   A CD  1 
ATOM   67   O OE1 . GLN   A 1 16  ? 14.82462  -10.73977 -27.45470 1.000 33.29334  ? 23  GLN   A OE1 1 
ATOM   68   N NE2 . GLN   A 1 16  ? 16.91769  -9.93366  -27.45883 1.000 33.91461  ? 23  GLN   A NE2 1 
ATOM   69   N N   . ALA   A 1 17  ? 19.22073  -14.37338 -24.35523 1.000 18.80838  ? 24  ALA   A N   1 
ATOM   70   C CA  . ALA   A 1 17  ? 19.84946  -14.76875 -23.09419 1.000 20.00720  ? 24  ALA   A CA  1 
ATOM   71   C C   . ALA   A 1 17  ? 19.18780  -14.09688 -21.90291 1.000 18.35387  ? 24  ALA   A C   1 
ATOM   72   O O   . ALA   A 1 17  ? 18.97094  -14.73172 -20.86437 1.000 18.48283  ? 24  ALA   A O   1 
ATOM   73   C CB  . ALA   A 1 17  ? 21.34526  -14.44055 -23.10917 1.000 20.82604  ? 24  ALA   A CB  1 
ATOM   74   N N   . GLU   A 1 18  ? 18.85250  -12.81078 -22.03489 1.000 19.34817  ? 25  GLU   A N   1 
ATOM   75   C CA  . GLU   A 1 18  ? 18.26254  -12.08281 -20.91417 1.000 23.64093  ? 25  GLU   A CA  1 
ATOM   76   C C   . GLU   A 1 18  ? 16.88340  -12.62243 -20.53788 1.000 20.32894  ? 25  GLU   A C   1 
ATOM   77   O O   . GLU   A 1 18  ? 16.52014  -12.60675 -19.35447 1.000 18.09211  ? 25  GLU   A O   1 
ATOM   78   C CB  . GLU   A 1 18  ? 18.18008  -10.58844 -21.23378 1.000 28.64210  ? 25  GLU   A CB  1 
ATOM   79   C CG  . GLU   A 1 18  ? 19.53713  -9.89866  -21.47815 1.000 30.24229  ? 25  GLU   A CG  1 
ATOM   80   C CD  . GLU   A 1 18  ? 20.13133  -10.10342 -22.87403 1.000 37.79104  ? 25  GLU   A CD  1 
ATOM   81   O OE1 . GLU   A 1 18  ? 19.55393  -10.83228 -23.71101 1.000 26.72574  ? 25  GLU   A OE1 1 
ATOM   82   O OE2 . GLU   A 1 18  ? 21.20408  -9.52136  -23.13383 1.000 46.09410  ? 25  GLU   A OE2 1 
ATOM   83   N N   . ILE   A 1 19  ? 16.10902  -13.09637 -21.51472 1.000 19.10590  ? 26  ILE   A N   1 
ATOM   84   C CA  . ILE   A 1 19  ? 14.78592  -13.64842 -21.21010 1.000 16.51369  ? 26  ILE   A CA  1 
ATOM   85   C C   . ILE   A 1 19  ? 14.91787  -15.03373 -20.58153 1.000 17.84426  ? 26  ILE   A C   1 
ATOM   86   O O   . ILE   A 1 19  ? 14.16103  -15.39089 -19.67292 1.000 14.80111  ? 26  ILE   A O   1 
ATOM   87   C CB  . ILE   A 1 19  ? 13.88007  -13.66363 -22.46976 1.000 17.89524  ? 26  ILE   A CB  1 
ATOM   88   C CG1 . ILE   A 1 19  ? 13.34637  -12.26250 -22.83001 1.000 20.64236  ? 26  ILE   A CG1 1 
ATOM   89   C CG2 . ILE   A 1 19  ? 12.66014  -14.57845 -22.27973 1.000 16.76539  ? 26  ILE   A CG2 1 
ATOM   90   C CD1 . ILE   A 1 19  ? 14.37609  -11.18771 -23.08061 1.000 24.30542  ? 26  ILE   A CD1 1 
ATOM   91   N N   . ALA   A 1 20  ? 15.89306  -15.82543 -21.03073 1.000 14.30372  ? 27  ALA   A N   1 
ATOM   92   C CA  . ALA   A 1 20  ? 16.16878  -17.09722 -20.37041 1.000 15.43002  ? 27  ALA   A CA  1 
ATOM   93   C C   . ALA   A 1 20  ? 16.52839  -16.87049 -18.90740 1.000 13.49419  ? 27  ALA   A C   1 
ATOM   94   O O   . ALA   A 1 20  ? 16.09576  -17.61827 -18.01702 1.000 19.54088  ? 27  ALA   A O   1 
ATOM   95   C CB  . ALA   A 1 20  ? 17.30799  -17.82270 -21.09452 1.000 15.96208  ? 27  ALA   A CB  1 
ATOM   96   N N   . GLN   A 1 21  ? 17.30094  -15.82156 -18.64279 1.000 19.88798  ? 28  GLN   A N   1 
ATOM   97   C CA  . GLN   A 1 21  ? 17.70286  -15.53386 -17.27439 1.000 18.52373  ? 28  GLN   A CA  1 
ATOM   98   C C   . GLN   A 1 21  ? 16.49552  -15.09810 -16.44627 1.000 19.22734  ? 28  GLN   A C   1 
ATOM   99   O O   . GLN   A 1 21  ? 16.34246  -15.52438 -15.29578 1.000 21.26228  ? 28  GLN   A O   1 
ATOM   100  C CB  . GLN   A 1 21  ? 18.80354  -14.46714 -17.29545 1.000 21.77711  ? 28  GLN   A CB  1 
ATOM   101  C CG  . GLN   A 1 21  ? 19.45498  -14.15141 -15.96308 1.000 40.89549  ? 28  GLN   A CG  1 
ATOM   102  C CD  . GLN   A 1 21  ? 20.43690  -12.98354 -16.06878 1.000 56.38722  ? 28  GLN   A CD  1 
ATOM   103  O OE1 . GLN   A 1 21  ? 20.89541  -12.44466 -15.05585 1.000 52.12328  ? 28  GLN   A OE1 1 
ATOM   104  N NE2 . GLN   A 1 21  ? 20.74008  -12.57122 -17.30852 1.000 44.58118  ? 28  GLN   A NE2 1 
ATOM   105  N N   . LEU   A 1 22  ? 15.61963  -14.26451 -17.02423 1.000 16.23299  ? 29  LEU   A N   1 
ATOM   106  C CA  . LEU   A 1 22  ? 14.37422  -13.88879 -16.34188 1.000 18.25007  ? 29  LEU   A CA  1 
ATOM   107  C C   . LEU   A 1 22  ? 13.54744  -15.11994 -15.98332 1.000 22.33445  ? 29  LEU   A C   1 
ATOM   108  O O   . LEU   A 1 22  ? 13.05235  -15.25377 -14.85747 1.000 18.34428  ? 29  LEU   A O   1 
ATOM   109  C CB  . LEU   A 1 22  ? 13.53977  -12.94850 -17.21863 1.000 19.39245  ? 29  LEU   A CB  1 
ATOM   110  C CG  . LEU   A 1 22  ? 12.13518  -12.65895 -16.66693 1.000 19.23712  ? 29  LEU   A CG  1 
ATOM   111  C CD1 . LEU   A 1 22  ? 12.22744  -11.79193 -15.41767 1.000 22.87154  ? 29  LEU   A CD1 1 
ATOM   112  C CD2 . LEU   A 1 22  ? 11.21310  -12.03773 -17.70888 1.000 25.47409  ? 29  LEU   A CD2 1 
ATOM   113  N N   . MET   A 1 23  ? 13.38157  -16.03946 -16.93198 1.000 14.12796  ? 30  MET   A N   1 
ATOM   114  C CA  . MET   A 1 23  ? 12.54998  -17.20041 -16.64113 1.000 15.74736  ? 30  MET   A CA  1 
ATOM   115  C C   . MET   A 1 23  ? 13.17280  -18.09336 -15.57742 1.000 18.56454  ? 30  MET   A C   1 
ATOM   116  O O   . MET   A 1 23  ? 12.45603  -18.63016 -14.72120 1.000 16.92497  ? 30  MET   A O   1 
ATOM   117  C CB  . MET   A 1 23  ? 12.21968  -18.02277 -17.89308 1.000 13.58191  ? 30  MET   A CB  1 
ATOM   118  C CG  . MET   A 1 23  ? 11.41866  -17.24345 -18.96263 1.000 13.71212  ? 30  MET   A CG  1 
ATOM   119  S SD  . MET   A 1 23  ? 11.36319  -17.96545 -20.61624 1.000 16.69675  ? 30  MET   A SD  1 
ATOM   120  C CE  . MET   A 1 23  ? 10.36196  -19.40155 -20.23567 1.000 17.86110  ? 30  MET   A CE  1 
ATOM   121  N N   . SER   A 1 24  ? 14.49041  -18.29707 -15.62300 1.000 18.42708  ? 31  SER   A N   1 
ATOM   122  C CA  . SER   A 1 24  ? 15.08090  -19.14664 -14.58996 1.000 16.46256  ? 31  SER   A CA  1 
ATOM   123  C C   . SER   A 1 24  ? 14.99319  -18.48365 -13.21257 1.000 20.42280  ? 31  SER   A C   1 
ATOM   124  O O   . SER   A 1 24  ? 14.77319  -19.17112 -12.21122 1.000 21.08171  ? 31  SER   A O   1 
ATOM   125  C CB  . SER   A 1 24  ? 16.51228  -19.52491 -14.97793 1.000 27.24389  ? 31  SER   A CB  1 
ATOM   126  O OG  . SER   A 1 24  ? 17.41770  -18.47421 -14.74366 1.000 44.94767  ? 31  SER   A OG  1 
ATOM   127  N N   . LEU   A 1 25  ? 15.08709  -17.15420 -13.14201 1.000 17.49427  ? 32  LEU   A N   1 
ATOM   128  C CA  . LEU   A 1 25  ? 14.87947  -16.48017 -11.85741 1.000 17.53569  ? 32  LEU   A CA  1 
ATOM   129  C C   . LEU   A 1 25  ? 13.46571  -16.72417 -11.33309 1.000 24.53002  ? 32  LEU   A C   1 
ATOM   130  O O   . LEU   A 1 25  ? 13.25825  -17.00315 -10.13745 1.000 19.17875  ? 32  LEU   A O   1 
ATOM   131  C CB  . LEU   A 1 25  ? 15.14680  -14.97827 -12.02541 1.000 24.56677  ? 32  LEU   A CB  1 
ATOM   132  C CG  . LEU   A 1 25  ? 14.99319  -14.00621 -10.83613 1.000 33.60691  ? 32  LEU   A CG  1 
ATOM   133  C CD1 . LEU   A 1 25  ? 15.75581  -12.71949 -11.13444 1.000 47.05614  ? 32  LEU   A CD1 1 
ATOM   134  C CD2 . LEU   A 1 25  ? 13.53160  -13.65814 -10.50324 1.000 29.62503  ? 32  LEU   A CD2 1 
ATOM   135  N N   . ILE   A 1 26  ? 12.47662  -16.59729 -12.21245 1.000 18.14873  ? 33  ILE   A N   1 
ATOM   136  C CA  . ILE   A 1 26  ? 11.09024  -16.79960 -11.80450 1.000 19.48803  ? 33  ILE   A CA  1 
ATOM   137  C C   . ILE   A 1 26  ? 10.88190  -18.22660 -11.31826 1.000 23.10021  ? 33  ILE   A C   1 
ATOM   138  O O   . ILE   A 1 26  ? 10.17081  -18.46946 -10.33210 1.000 20.78712  ? 33  ILE   A O   1 
ATOM   139  C CB  . ILE   A 1 26  ? 10.15192  -16.45347 -12.96940 1.000 15.08626  ? 33  ILE   A CB  1 
ATOM   140  C CG1 . ILE   A 1 26  ? 10.11444  -14.93899 -13.14168 1.000 17.82240  ? 33  ILE   A CG1 1 
ATOM   141  C CG2 . ILE   A 1 26  ? 8.72417   -17.01112 -12.69601 1.000 16.56801  ? 33  ILE   A CG2 1 
ATOM   142  C CD1 . ILE   A 1 26  ? 9.58739   -14.46153 -14.49809 1.000 18.71604  ? 33  ILE   A CD1 1 
ATOM   143  N N   . ILE   A 1 27  ? 11.51453  -19.18988 -11.98855 1.000 17.41004  ? 34  ILE   A N   1 
ATOM   144  C CA  . ILE   A 1 27  ? 11.31072  -20.59619 -11.65904 1.000 19.61912  ? 34  ILE   A CA  1 
ATOM   145  C C   . ILE   A 1 27  ? 12.04794  -20.97824 -10.38186 1.000 25.54453  ? 34  ILE   A C   1 
ATOM   146  O O   . ILE   A 1 27  ? 11.54841  -21.77759 -9.57979  1.000 27.63892  ? 34  ILE   A O   1 
ATOM   147  C CB  . ILE   A 1 27  ? 11.74495  -21.46862 -12.85294 1.000 24.48947  ? 34  ILE   A CB  1 
ATOM   148  C CG1 . ILE   A 1 27  ? 10.72291  -21.35339 -13.98468 1.000 24.23494  ? 34  ILE   A CG1 1 
ATOM   149  C CG2 . ILE   A 1 27  ? 11.97204  -22.92270 -12.43884 1.000 27.10011  ? 34  ILE   A CG2 1 
ATOM   150  C CD1 . ILE   A 1 27  ? 11.27741  -21.82995 -15.33701 1.000 21.93793  ? 34  ILE   A CD1 1 
ATOM   151  N N   . ASN   A 1 28  ? 13.23358  -20.41075 -10.16121 1.000 23.13453  ? 35  ASN   A N   1 
ATOM   152  C CA  . ASN   A 1 28  ? 14.11586  -20.89478 -9.10113  1.000 25.10434  ? 35  ASN   A CA  1 
ATOM   153  C C   . ASN   A 1 28  ? 14.07369  -20.08555 -7.81422  1.000 31.04484  ? 35  ASN   A C   1 
ATOM   154  O O   . ASN   A 1 28  ? 14.48146  -20.60594 -6.76916  1.000 32.53980  ? 35  ASN   A O   1 
ATOM   155  C CB  . ASN   A 1 28  ? 15.55811  -20.93976 -9.59873  1.000 30.19840  ? 35  ASN   A CB  1 
ATOM   156  C CG  . ASN   A 1 28  ? 15.74423  -21.95517 -10.67761 1.000 31.95023  ? 35  ASN   A CG  1 
ATOM   157  O OD1 . ASN   A 1 28  ? 15.10086  -23.00580 -10.66210 1.000 31.66038  ? 35  ASN   A OD1 1 
ATOM   158  N ND2 . ASN   A 1 28  ? 16.59958  -21.64802 -11.64082 1.000 40.50259  ? 35  ASN   A ND2 1 
ATOM   159  N N   . THR   A 1 29  ? 13.62778  -18.83850 -7.84609  1.000 23.37723  ? 36  THR   A N   1 
ATOM   160  C CA  . THR   A 1 29  ? 13.64358  -18.04029 -6.62314  1.000 24.20416  ? 36  THR   A CA  1 
ATOM   161  C C   . THR   A 1 29  ? 12.57209  -18.52667 -5.65526  1.000 25.09183  ? 36  THR   A C   1 
ATOM   162  O O   . THR   A 1 29  ? 11.41778  -18.72815 -6.04677  1.000 24.70903  ? 36  THR   A O   1 
ATOM   163  C CB  . THR   A 1 29  ? 13.42428  -16.55934 -6.94618  1.000 25.29596  ? 36  THR   A CB  1 
ATOM   164  O OG1 . THR   A 1 29  ? 14.47673  -16.08869 -7.79206  1.000 23.09643  ? 36  THR   A OG1 1 
ATOM   165  C CG2 . THR   A 1 29  ? 13.35812  -15.71389 -5.67205  1.000 31.53464  ? 36  THR   A CG2 1 
ATOM   166  N N   . PHE   A 1 30  ? 12.94285  -18.69790 -4.38306  1.000 23.64000  ? 37  PHE   A N   1 
ATOM   167  C CA  . PHE   A 1 30  ? 11.92495  -18.95049 -3.37478  1.000 24.04371  ? 37  PHE   A CA  1 
ATOM   168  C C   . PHE   A 1 30  ? 11.06853  -17.70074 -3.18772  1.000 26.09347  ? 37  PHE   A C   1 
ATOM   169  O O   . PHE   A 1 30  ? 11.57492  -16.64044 -2.79692  1.000 23.67892  ? 37  PHE   A O   1 
ATOM   170  C CB  . PHE   A 1 30  ? 12.54706  -19.38743 -2.04743  1.000 22.60333  ? 37  PHE   A CB  1 
ATOM   171  C CG  . PHE   A 1 30  ? 11.51805  -19.66189 -0.99203  1.000 22.69883  ? 37  PHE   A CG  1 
ATOM   172  C CD1 . PHE   A 1 30  ? 10.72918  -20.79921 -1.05353  1.000 31.02865  ? 37  PHE   A CD1 1 
ATOM   173  C CD2 . PHE   A 1 30  ? 11.32249  -18.77244 0.05924   1.000 24.74791  ? 37  PHE   A CD2 1 
ATOM   174  C CE1 . PHE   A 1 30  ? 9.74400   -21.03988 -0.09515  1.000 27.21422  ? 37  PHE   A CE1 1 
ATOM   175  C CE2 . PHE   A 1 30  ? 10.34490  -19.00889 1.02390   1.000 30.39240  ? 37  PHE   A CE2 1 
ATOM   176  C CZ  . PHE   A 1 30  ? 9.56659   -20.14506 0.95938   1.000 23.56618  ? 37  PHE   A CZ  1 
ATOM   177  N N   . TYR   A 1 31  ? 9.76547   -17.82807 -3.44758  1.000 19.65068  ? 38  TYR   A N   1 
ATOM   178  C CA  . TYR   A 1 31  ? 8.88087   -16.66912 -3.40738  1.000 18.52750  ? 38  TYR   A CA  1 
ATOM   179  C C   . TYR   A 1 31  ? 7.43853   -17.16608 -3.28483  1.000 19.98334  ? 38  TYR   A C   1 
ATOM   180  O O   . TYR   A 1 31  ? 6.89721   -17.73872 -4.23003  1.000 20.84796  ? 38  TYR   A O   1 
ATOM   181  C CB  . TYR   A 1 31  ? 9.10164   -15.81632 -4.65615  1.000 22.12968  ? 38  TYR   A CB  1 
ATOM   182  C CG  . TYR   A 1 31  ? 8.08774   -14.73848 -4.82615  1.000 25.11315  ? 38  TYR   A CG  1 
ATOM   183  C CD1 . TYR   A 1 31  ? 8.15300   -13.57266 -4.06800  1.000 25.01460  ? 38  TYR   A CD1 1 
ATOM   184  C CD2 . TYR   A 1 31  ? 7.05142   -14.88450 -5.73817  1.000 25.60352  ? 38  TYR   A CD2 1 
ATOM   185  C CE1 . TYR   A 1 31  ? 7.19797   -12.58299 -4.21224  1.000 31.88332  ? 38  TYR   A CE1 1 
ATOM   186  C CE2 . TYR   A 1 31  ? 6.10220   -13.90002 -5.88752  1.000 27.11087  ? 38  TYR   A CE2 1 
ATOM   187  C CZ  . TYR   A 1 31  ? 6.18304   -12.75946 -5.12969  1.000 30.55610  ? 38  TYR   A CZ  1 
ATOM   188  O OH  . TYR   A 1 31  ? 5.22758   -11.79353 -5.29731  1.000 42.43904  ? 38  TYR   A OH  1 
ATOM   189  N N   . SER   A 1 32  ? 6.82271   -16.97114 -2.11630  1.000 18.95717  ? 39  SER   A N   1 
ATOM   190  C CA  . SER   A 1 32  ? 5.57274   -17.66609 -1.82690  1.000 19.01957  ? 39  SER   A CA  1 
ATOM   191  C C   . SER   A 1 32  ? 4.34455   -17.02820 -2.48341  1.000 18.73498  ? 39  SER   A C   1 
ATOM   192  O O   . SER   A 1 32  ? 3.34888   -17.72583 -2.70692  1.000 21.71661  ? 39  SER   A O   1 
ATOM   193  C CB  . SER   A 1 32  ? 5.36750   -17.75378 -0.30799  1.000 20.25716  ? 39  SER   A CB  1 
ATOM   194  O OG  . SER   A 1 32  ? 6.38753   -18.56192 0.25958   1.000 21.60872  ? 39  SER   A OG  1 
ATOM   195  N N   . ASN   A 1 33  ? 4.38624   -15.73714 -2.79861  1.000 19.65617  ? 40  ASN   A N   1 
ATOM   196  C CA  . ASN   A 1 33  ? 3.20306   -14.99787 -3.25193  1.000 17.84915  ? 40  ASN   A CA  1 
ATOM   197  C C   . ASN   A 1 33  ? 2.94365   -15.23087 -4.74999  1.000 16.49277  ? 40  ASN   A C   1 
ATOM   198  O O   . ASN   A 1 33  ? 2.92558   -14.31541 -5.57881  1.000 19.80750  ? 40  ASN   A O   1 
ATOM   199  C CB  . ASN   A 1 33  ? 3.41152   -13.52471 -2.92247  1.000 22.85888  ? 40  ASN   A CB  1 
ATOM   200  C CG  . ASN   A 1 33  ? 2.22150   -12.65710 -3.27009  1.000 24.61961  ? 40  ASN   A CG  1 
ATOM   201  O OD1 . ASN   A 1 33  ? 1.06900   -13.07500 -3.16232  1.000 25.99446  ? 40  ASN   A OD1 1 
ATOM   202  N ND2 . ASN   A 1 33  ? 2.50164   -11.41899 -3.65649  1.000 25.97428  ? 40  ASN   A ND2 1 
ATOM   203  N N   . LYS   A 1 34  ? 2.70092   -16.50097 -5.09501  1.000 15.12831  ? 41  LYS   A N   1 
ATOM   204  C CA  . LYS   A 1 34  ? 2.63099   -16.87917 -6.50462  1.000 14.31582  ? 41  LYS   A CA  1 
ATOM   205  C C   . LYS   A 1 34  ? 1.35125   -16.40638 -7.17297  1.000 13.57914  ? 41  LYS   A C   1 
ATOM   206  O O   . LYS   A 1 34  ? 1.31019   -16.30712 -8.40882  1.000 15.19356  ? 41  LYS   A O   1 
ATOM   207  C CB  . LYS   A 1 34  ? 2.72592   -18.39581 -6.63194  1.000 14.67972  ? 41  LYS   A CB  1 
ATOM   208  C CG  . LYS   A 1 34  ? 4.12052   -18.98168 -6.31246  1.000 16.96707  ? 41  LYS   A CG  1 
ATOM   209  C CD  . LYS   A 1 34  ? 4.07538   -20.50376 -6.43950  1.000 19.19824  ? 41  LYS   A CD  1 
ATOM   210  C CE  . LYS   A 1 34  ? 5.45272   -21.15884 -6.21847  1.000 18.90709  ? 41  LYS   A CE  1 
ATOM   211  N NZ  . LYS   A 1 34  ? 6.34691   -20.93110 -7.39270  1.000 18.87165  ? 41  LYS   A NZ  1 
ATOM   212  N N   . GLU   A 1 35  ? 0.31236   -16.10911 -6.39235  1.000 16.31594  ? 42  GLU   A N   1 
ATOM   213  C CA  . GLU   A 1 35  ? -1.00482  -15.82633 -6.95883  1.000 15.38370  ? 42  GLU   A CA  1 
ATOM   214  C C   . GLU   A 1 35  ? -1.01778  -14.60979 -7.87031  1.000 18.58181  ? 42  GLU   A C   1 
ATOM   215  O O   . GLU   A 1 35  ? -1.97201  -14.44797 -8.64488  1.000 18.14080  ? 42  GLU   A O   1 
ATOM   216  C CB  . GLU   A 1 35  ? -2.03828  -15.60124 -5.84260  1.000 16.67728  ? 42  GLU   A CB  1 
ATOM   217  C CG  . GLU   A 1 35  ? -1.83430  -14.30822 -5.06623  1.000 17.45866  ? 42  GLU   A CG  1 
ATOM   218  C CD  . GLU   A 1 35  ? -2.76698  -14.20235 -3.87300  1.000 22.97649  ? 42  GLU   A CD  1 
ATOM   219  O OE1 . GLU   A 1 35  ? -2.93508  -15.20199 -3.15083  1.000 30.31870  ? 42  GLU   A OE1 1 
ATOM   220  O OE2 . GLU   A 1 35  ? -3.32740  -13.12009 -3.65700  1.000 35.45914  ? 42  GLU   A OE2 1 
ATOM   221  N N   . ILE   A 1 36  ? -0.01037  -13.73466 -7.78197  1.000 16.10469  ? 43  ILE   A N   1 
ATOM   222  C CA  . ILE   A 1 36  ? 0.01916   -12.55363 -8.62980  1.000 13.37195  ? 43  ILE   A CA  1 
ATOM   223  C C   . ILE   A 1 36  ? 0.13553   -12.88707 -10.11333 1.000 13.45135  ? 43  ILE   A C   1 
ATOM   224  O O   . ILE   A 1 36  ? -0.07910  -11.99531 -10.93907 1.000 13.77079  ? 43  ILE   A O   1 
ATOM   225  C CB  . ILE   A 1 36  ? 1.16074   -11.58985 -8.22184  1.000 18.81863  ? 43  ILE   A CB  1 
ATOM   226  C CG1 . ILE   A 1 36  ? 2.54607   -12.23628 -8.37717  1.000 19.56899  ? 43  ILE   A CG1 1 
ATOM   227  C CG2 . ILE   A 1 36  ? 0.91827   -11.08724 -6.80094  1.000 21.65010  ? 43  ILE   A CG2 1 
ATOM   228  C CD1 . ILE   A 1 36  ? 3.23705   -11.90252 -9.75779  1.000 21.46135  ? 43  ILE   A CD1 1 
ATOM   229  N N   . PHE   A 1 37  ? 0.45101   -14.13858 -10.48227 1.000 12.30167  ? 44  PHE   A N   1 
ATOM   230  C CA  . PHE   A 1 37  ? 0.48785   -14.46823 -11.91310 1.000 15.08715  ? 44  PHE   A CA  1 
ATOM   231  C C   . PHE   A 1 37  ? -0.85013  -14.14498 -12.57999 1.000 17.49438  ? 44  PHE   A C   1 
ATOM   232  O O   . PHE   A 1 37  ? -0.89487  -13.70105 -13.73535 1.000 13.88973  ? 44  PHE   A O   1 
ATOM   233  C CB  . PHE   A 1 37  ? 0.82578   -15.95024 -12.12131 1.000 12.62685  ? 44  PHE   A CB  1 
ATOM   234  C CG  . PHE   A 1 37  ? -0.37352  -16.85332 -11.94241 1.000 15.02962  ? 44  PHE   A CG  1 
ATOM   235  C CD1 . PHE   A 1 37  ? -0.71478  -17.32185 -10.68770 1.000 15.13325  ? 44  PHE   A CD1 1 
ATOM   236  C CD2 . PHE   A 1 37  ? -1.19709  -17.17064 -13.02229 1.000 16.08495  ? 44  PHE   A CD2 1 
ATOM   237  C CE1 . PHE   A 1 37  ? -1.86673  -18.12192 -10.50884 1.000 15.78501  ? 44  PHE   A CE1 1 
ATOM   238  C CE2 . PHE   A 1 37  ? -2.33403  -17.95824 -12.85309 1.000 13.93955  ? 44  PHE   A CE2 1 
ATOM   239  C CZ  . PHE   A 1 37  ? -2.66694  -18.43833 -11.59454 1.000 14.43856  ? 44  PHE   A CZ  1 
ATOM   240  N N   . LEU   A 1 38  ? -1.96046  -14.39384 -11.87933 1.000 14.69227  ? 45  LEU   A N   1 
ATOM   241  C CA  . LEU   A 1 38  ? -3.26053  -14.20965 -12.51185 1.000 12.54005  ? 45  LEU   A CA  1 
ATOM   242  C C   . LEU   A 1 38  ? -3.53818  -12.73123 -12.75060 1.000 14.58608  ? 45  LEU   A C   1 
ATOM   243  O O   . LEU   A 1 38  ? -4.03747  -12.34816 -13.81630 1.000 13.86673  ? 45  LEU   A O   1 
ATOM   244  C CB  . LEU   A 1 38  ? -4.35368  -14.84661 -11.65120 1.000 12.34652  ? 45  LEU   A CB  1 
ATOM   245  C CG  . LEU   A 1 38  ? -5.74109  -14.86724 -12.30192 1.000 13.87475  ? 45  LEU   A CG  1 
ATOM   246  C CD1 . LEU   A 1 38  ? -5.71663  -15.61157 -13.63083 1.000 11.98357  ? 45  LEU   A CD1 1 
ATOM   247  C CD2 . LEU   A 1 38  ? -6.73423  -15.53599 -11.36441 1.000 17.60466  ? 45  LEU   A CD2 1 
ATOM   248  N N   . ARG   A 1 39  ? -3.19108  -11.88068 -11.77622 1.000 15.66609  ? 46  ARG   A N   1 
ATOM   249  C CA  . ARG   A 1 39  ? -3.34899  -10.44288 -11.96418 1.000 13.33372  ? 46  ARG   A CA  1 
ATOM   250  C C   . ARG   A 1 39  ? -2.56647  -9.96658  -13.17951 1.000 14.96748  ? 46  ARG   A C   1 
ATOM   251  O O   . ARG   A 1 39  ? -3.04806  -9.13606  -13.96396 1.000 15.79019  ? 46  ARG   A O   1 
ATOM   252  C CB  . ARG   A 1 39  ? -2.86714  -9.70269  -10.71618 1.000 17.26314  ? 46  ARG   A CB  1 
ATOM   253  C CG  . ARG   A 1 39  ? -2.73590  -8.22508  -10.88321 1.000 19.51400  ? 46  ARG   A CG  1 
ATOM   254  C CD  . ARG   A 1 39  ? -2.07126  -7.57773  -9.66139  1.000 21.96579  ? 46  ARG   A CD  1 
ATOM   255  N NE  . ARG   A 1 39  ? -0.62075  -7.78118  -9.62402  1.000 28.80753  ? 46  ARG   A NE  1 
ATOM   256  C CZ  . ARG   A 1 39  ? 0.12802   -7.66089  -8.53369  1.000 28.99532  ? 46  ARG   A CZ  1 
ATOM   257  N NH1 . ARG   A 1 39  ? -0.39577  -7.32697  -7.36593  1.000 28.28874  ? 46  ARG   A NH1 1 
ATOM   258  N NH2 . ARG   A 1 39  ? 1.44264   -7.84790  -8.62074  1.000 30.21115  ? 46  ARG   A NH2 1 
ATOM   259  N N   . GLU   A 1 40  ? -1.35056  -10.48439 -13.35288 1.000 12.58930  ? 47  GLU   A N   1 
ATOM   260  C CA  . GLU   A 1 40  ? -0.51828  -10.03619 -14.46545 1.000 15.14918  ? 47  GLU   A CA  1 
ATOM   261  C C   . GLU   A 1 40  ? -1.11638  -10.45574 -15.79875 1.000 15.93600  ? 47  GLU   A C   1 
ATOM   262  O O   . GLU   A 1 40  ? -1.10564  -9.68228  -16.76397 1.000 12.09928  ? 47  GLU   A O   1 
ATOM   263  C CB  . GLU   A 1 40  ? 0.89346   -10.60827 -14.32005 1.000 12.46398  ? 47  GLU   A CB  1 
ATOM   264  C CG  . GLU   A 1 40  ? 1.64284   -10.10016 -13.07835 1.000 17.80937  ? 47  GLU   A CG  1 
ATOM   265  C CD  . GLU   A 1 40  ? 1.59906   -8.58024  -12.93432 1.000 24.42508  ? 47  GLU   A CD  1 
ATOM   266  O OE1 . GLU   A 1 40  ? 1.65510   -7.87635  -13.96821 1.000 23.25416  ? 47  GLU   A OE1 1 
ATOM   267  O OE2 . GLU   A 1 40  ? 1.50104   -8.09009  -11.78730 1.000 29.03148  ? 47  GLU   A OE2 1 
ATOM   268  N N   . LEU   A 1 41  ? -1.62007  -11.68402 -15.88409 1.000 10.81100  ? 48  LEU   A N   1 
ATOM   269  C CA  . LEU   A 1 41  ? -2.19557  -12.12998 -17.16084 1.000 12.51108  ? 48  LEU   A CA  1 
ATOM   270  C C   . LEU   A 1 41  ? -3.50662  -11.41761 -17.46442 1.000 13.79503  ? 48  LEU   A C   1 
ATOM   271  O O   . LEU   A 1 41  ? -3.80512  -11.11247 -18.63058 1.000 13.31015  ? 48  LEU   A O   1 
ATOM   272  C CB  . LEU   A 1 41  ? -2.40402  -13.64710 -17.15088 1.000 12.32727  ? 48  LEU   A CB  1 
ATOM   273  C CG  . LEU   A 1 41  ? -1.10391  -14.44831 -17.06239 1.000 14.89252  ? 48  LEU   A CG  1 
ATOM   274  C CD1 . LEU   A 1 41  ? -1.38347  -15.95784 -16.94251 1.000 13.31028  ? 48  LEU   A CD1 1 
ATOM   275  C CD2 . LEU   A 1 41  ? -0.14369  -14.13137 -18.24920 1.000 14.02646  ? 48  LEU   A CD2 1 
ATOM   276  N N   . ILE   A 1 42  ? -4.31846  -11.16801 -16.43592 1.000 11.16256  ? 49  ILE   A N   1 
ATOM   277  C CA  . ILE   A 1 42  ? -5.55167  -10.42736 -16.66071 1.000 13.31256  ? 49  ILE   A CA  1 
ATOM   278  C C   . ILE   A 1 42  ? -5.24221  -9.00385  -17.08980 1.000 15.55979  ? 49  ILE   A C   1 
ATOM   279  O O   . ILE   A 1 42  ? -5.90436  -8.45339  -17.97703 1.000 14.15542  ? 49  ILE   A O   1 
ATOM   280  C CB  . ILE   A 1 42  ? -6.46033  -10.48693 -15.41885 1.000 12.56666  ? 49  ILE   A CB  1 
ATOM   281  C CG1 . ILE   A 1 42  ? -7.03134  -11.90838 -15.30452 1.000 11.99865  ? 49  ILE   A CG1 1 
ATOM   282  C CG2 . ILE   A 1 42  ? -7.58477  -9.42080  -15.52615 1.000 15.28728  ? 49  ILE   A CG2 1 
ATOM   283  C CD1 . ILE   A 1 42  ? -7.77817  -12.14966 -13.95820 1.000 15.69998  ? 49  ILE   A CD1 1 
ATOM   284  N N   . SER   A 1 43  ? -4.19413  -8.40376  -16.51795 1.000 12.80757  ? 50  SER   A N   1 
ATOM   285  C CA  . SER   A 1 43  ? -3.85042  -7.04803  -16.91200 1.000 14.08330  ? 50  SER   A CA  1 
ATOM   286  C C   . SER   A 1 43  ? -3.34415  -7.02210  -18.35541 1.000 15.29382  ? 50  SER   A C   1 
ATOM   287  O O   . SER   A 1 43  ? -3.68339  -6.11089  -19.11451 1.000 13.70214  ? 50  SER   A O   1 
ATOM   288  C CB  . SER   A 1 43  ? -2.82515  -6.46725  -15.92195 1.000 19.92493  ? 50  SER   A CB  1 
ATOM   289  O OG  . SER   A 1 43  ? -2.13768  -5.35194  -16.46048 1.000 25.68049  ? 50  SER   A OG  1 
ATOM   290  N N   . ASN   A 1 44  ? -2.54549  -8.02565  -18.76129 1.000 13.61810  ? 51  ASN   A N   1 
ATOM   291  C CA  . ASN   A 1 44  ? -2.17178  -8.14609  -20.17401 1.000 18.96168  ? 51  ASN   A CA  1 
ATOM   292  C C   . ASN   A 1 44  ? -3.40212  -8.24524  -21.07195 1.000 17.60717  ? 51  ASN   A C   1 
ATOM   293  O O   . ASN   A 1 44  ? -3.45070  -7.63254  -22.14798 1.000 12.72991  ? 51  ASN   A O   1 
ATOM   294  C CB  . ASN   A 1 44  ? -1.28977  -9.37557  -20.39057 1.000 15.75410  ? 51  ASN   A CB  1 
ATOM   295  C CG  . ASN   A 1 44  ? 0.10492   -9.15912  -19.92155 1.000 22.81341  ? 51  ASN   A CG  1 
ATOM   296  O OD1 . ASN   A 1 44  ? 0.47864   -8.05161  -19.51756 1.000 18.19209  ? 51  ASN   A OD1 1 
ATOM   297  N ND2 . ASN   A 1 44  ? 0.88163   -10.22444 -19.92222 1.000 20.22859  ? 51  ASN   A ND2 1 
ATOM   298  N N   . SER   A 1 45  ? -4.37760  -9.05971  -20.67631 1.000 11.31550  ? 52  SER   A N   1 
ATOM   299  C CA  . SER   A 1 45  ? -5.59402  -9.18382  -21.47848 1.000 13.06030  ? 52  SER   A CA  1 
ATOM   300  C C   . SER   A 1 45  ? -6.32393  -7.84888  -21.56667 1.000 12.93238  ? 52  SER   A C   1 
ATOM   301  O O   . SER   A 1 45  ? -6.79588  -7.46049  -22.64273 1.000 13.57930  ? 52  SER   A O   1 
ATOM   302  C CB  . SER   A 1 45  ? -6.51855  -10.26068 -20.89351 1.000 13.62910  ? 52  SER   A CB  1 
ATOM   303  O OG  . SER   A 1 45  ? -5.97994  -11.57223 -21.04138 1.000 14.24586  ? 52  SER   A OG  1 
ATOM   304  N N   . SER   A 1 46  ? -6.42317  -7.12771  -20.44176 1.000 11.33812  ? 53  SER   A N   1 
ATOM   305  C CA  . SER   A 1 46  ? -7.07263  -5.81841  -20.46710 1.000 13.63292  ? 53  SER   A CA  1 
ATOM   306  C C   . SER   A 1 46  ? -6.34716  -4.86032  -21.41344 1.000 16.54599  ? 53  SER   A C   1 
ATOM   307  O O   . SER   A 1 46  ? -6.98719  -4.12049  -22.16477 1.000 15.15439  ? 53  SER   A O   1 
ATOM   308  C CB  . SER   A 1 46  ? -7.13169  -5.23176  -19.04911 1.000 12.95483  ? 53  SER   A CB  1 
ATOM   309  O OG  . SER   A 1 46  ? -7.70458  -3.92188  -19.05481 1.000 15.73670  ? 53  SER   A OG  1 
ATOM   310  N N   . ASP   A 1 47  ? -5.00773  -4.84119  -21.37202 1.000 14.98830  ? 54  ASP   A N   1 
ATOM   311  C CA  . ASP   A 1 47  ? -4.25155  -4.00147  -22.29836 1.000 13.89695  ? 54  ASP   A CA  1 
ATOM   312  C C   . ASP   A 1 47  ? -4.54078  -4.36156  -23.75609 1.000 17.53314  ? 54  ASP   A C   1 
ATOM   313  O O   . ASP   A 1 47  ? -4.65232  -3.46894  -24.60616 1.000 15.46173  ? 54  ASP   A O   1 
ATOM   314  C CB  . ASP   A 1 47  ? -2.74658  -4.11338  -22.03678 1.000 14.04091  ? 54  ASP   A CB  1 
ATOM   315  C CG  . ASP   A 1 47  ? -2.32152  -3.49478  -20.70402 1.000 25.24650  ? 54  ASP   A CG  1 
ATOM   316  O OD1 . ASP   A 1 47  ? -3.12164  -2.74742  -20.08318 1.000 23.60672  ? 54  ASP   A OD1 1 
ATOM   317  O OD2 . ASP   A 1 47  ? -1.14336  -3.70086  -20.31459 1.000 21.19431  ? 54  ASP   A OD2 1 
ATOM   318  N N   . ALA   A 1 48  ? -4.66221  -5.66656  -24.06330 1.000 11.56689  ? 55  ALA   A N   1 
ATOM   319  C CA  . ALA   A 1 48  ? -4.94812  -6.10574  -25.43204 1.000 12.79927  ? 55  ALA   A CA  1 
ATOM   320  C C   . ALA   A 1 48  ? -6.35979  -5.71292  -25.85619 1.000 13.41809  ? 55  ALA   A C   1 
ATOM   321  O O   . ALA   A 1 48  ? -6.59274  -5.34660  -27.01231 1.000 13.06647  ? 55  ALA   A O   1 
ATOM   322  C CB  . ALA   A 1 48  ? -4.76178  -7.62650  -25.54864 1.000 14.34115  ? 55  ALA   A CB  1 
ATOM   323  N N   . LEU   A 1 49  ? -7.31823  -5.79920  -24.93609 1.000 12.87441  ? 56  LEU   A N   1 
ATOM   324  C CA  . LEU   A 1 49  ? -8.67255  -5.34970  -25.24041 1.000 13.56884  ? 56  LEU   A CA  1 
ATOM   325  C C   . LEU   A 1 49  ? -8.73160  -3.84210  -25.45622 1.000 14.55149  ? 56  LEU   A C   1 
ATOM   326  O O   . LEU   A 1 49  ? -9.43609  -3.38236  -26.36611 1.000 14.44191  ? 56  LEU   A O   1 
ATOM   327  C CB  . LEU   A 1 49  ? -9.62906  -5.79374  -24.13235 1.000 12.74590  ? 56  LEU   A CB  1 
ATOM   328  C CG  . LEU   A 1 49  ? -9.83448  -7.30438  -24.13182 1.000 11.33220  ? 56  LEU   A CG  1 
ATOM   329  C CD1 . LEU   A 1 49  ? -10.15445 -7.82161  -22.71944 1.000 14.67647  ? 56  LEU   A CD1 1 
ATOM   330  C CD2 . LEU   A 1 49  ? -10.96838 -7.65901  -25.12355 1.000 11.74741  ? 56  LEU   A CD2 1 
ATOM   331  N N   . ASP   A 1 50  ? -7.99570  -3.06026  -24.64431 1.000 12.48775  ? 57  ASP   A N   1 
ATOM   332  C CA  . ASP   A 1 50  ? -7.91432  -1.61266  -24.86908 1.000 13.29092  ? 57  ASP   A CA  1 
ATOM   333  C C   . ASP   A 1 50  ? -7.42879  -1.30927  -26.28199 1.000 15.67676  ? 57  ASP   A C   1 
ATOM   334  O O   . ASP   A 1 50  ? -7.92513  -0.38453  -26.93732 1.000 14.66246  ? 57  ASP   A O   1 
ATOM   335  C CB  . ASP   A 1 50  ? -6.96210  -0.93914  -23.86995 1.000 13.58592  ? 57  ASP   A CB  1 
ATOM   336  C CG  . ASP   A 1 50  ? -7.49051  -0.88972  -22.44885 1.000 16.78344  ? 57  ASP   A CG  1 
ATOM   337  O OD1 . ASP   A 1 50  ? -8.66494  -1.23913  -22.18047 1.000 20.04254  ? 57  ASP   A OD1 1 
ATOM   338  O OD2 . ASP   A 1 50  ? -6.68990  -0.47018  -21.58547 1.000 18.01655  ? 57  ASP   A OD2 1 
ATOM   339  N N   . LYS   A 1 51  ? -6.44774  -2.07956  -26.76742 1.000 13.11129  ? 58  LYS   A N   1 
ATOM   340  C CA  . LYS   A 1 51  ? -5.86346  -1.78284  -28.07414 1.000 13.59246  ? 58  LYS   A CA  1 
ATOM   341  C C   . LYS   A 1 51  ? -6.86763  -1.97598  -29.19908 1.000 17.25441  ? 58  LYS   A C   1 
ATOM   342  O O   . LYS   A 1 51  ? -6.96667  -1.14000  -30.10840 1.000 17.04986  ? 58  LYS   A O   1 
ATOM   343  C CB  . LYS   A 1 51  ? -4.62801  -2.65860  -28.31272 1.000 15.53698  ? 58  LYS   A CB  1 
ATOM   344  C CG  . LYS   A 1 51  ? -3.42028  -2.26682  -27.44935 1.000 15.87269  ? 58  LYS   A CG  1 
ATOM   345  C CD  . LYS   A 1 51  ? -2.27911  -3.28330  -27.66116 1.000 17.21739  ? 58  LYS   A CD  1 
ATOM   346  C CE  . LYS   A 1 51  ? -1.15457  -3.10480  -26.64399 1.000 25.98330  ? 58  LYS   A CE  1 
ATOM   347  N NZ  . LYS   A 1 51  ? 0.02447   -3.96631  -26.99405 1.000 31.29702  ? 58  LYS   A NZ  1 
ATOM   348  N N   . ILE   A 1 52  ? -7.59079  -3.09442  -29.19349 1.000 15.55382  ? 59  ILE   A N   1 
ATOM   349  C CA  . ILE   A 1 52  ? -8.54553  -3.29851  -30.28501 1.000 14.96441  ? 59  ILE   A CA  1 
ATOM   350  C C   . ILE   A 1 52  ? -9.73067  -2.34562  -30.13665 1.000 15.83120  ? 59  ILE   A C   1 
ATOM   351  O O   . ILE   A 1 52  ? -10.28405 -1.87953  -31.13935 1.000 17.07811  ? 59  ILE   A O   1 
ATOM   352  C CB  . ILE   A 1 52  ? -8.99593  -4.77312  -30.38398 1.000 14.38205  ? 59  ILE   A CB  1 
ATOM   353  C CG1 . ILE   A 1 52  ? -9.81088  -5.02352  -31.67463 1.000 15.61107  ? 59  ILE   A CG1 1 
ATOM   354  C CG2 . ILE   A 1 52  ? -9.80366  -5.19616  -29.17443 1.000 15.23814  ? 59  ILE   A CG2 1 
ATOM   355  C CD1 . ILE   A 1 52  ? -9.06532  -4.71715  -32.95316 1.000 21.04747  ? 59  ILE   A CD1 1 
ATOM   356  N N   . ARG   A 1 53  ? -10.11743 -2.00079  -28.90339 1.000 15.73055  ? 60  ARG   A N   1 
ATOM   357  C CA  . ARG   A 1 53  ? -11.17707 -1.00452  -28.74195 1.000 16.00045  ? 60  ARG   A CA  1 
ATOM   358  C C   . ARG   A 1 53  ? -10.77192 0.33390   -29.33155 1.000 16.91895  ? 60  ARG   A C   1 
ATOM   359  O O   . ARG   A 1 53  ? -11.56303 0.96985   -30.04621 1.000 17.03790  ? 60  ARG   A O   1 
ATOM   360  C CB  . ARG   A 1 53  ? -11.56538 -0.82339  -27.26872 1.000 17.59815  ? 60  ARG   A CB  1 
ATOM   361  C CG  . ARG   A 1 53  ? -12.79904 0.09124   -27.17437 1.000 31.64477  ? 60  ARG   A CG  1 
ATOM   362  C CD  . ARG   A 1 53  ? -13.21264 0.43779   -25.77122 1.000 40.22800  ? 60  ARG   A CD  1 
ATOM   363  N NE  . ARG   A 1 53  ? -14.26567 -0.44210  -25.27914 1.000 41.78370  ? 60  ARG   A NE  1 
ATOM   364  C CZ  . ARG   A 1 53  ? -14.34809 -0.87506  -24.02980 1.000 43.14152  ? 60  ARG   A CZ  1 
ATOM   365  N NH1 . ARG   A 1 53  ? -13.40993 -0.59265  -23.13959 1.000 37.27348  ? 60  ARG   A NH1 1 
ATOM   366  N NH2 . ARG   A 1 53  ? -15.40232 -1.60080  -23.66170 1.000 32.85866  ? 60  ARG   A NH2 1 
ATOM   367  N N   . TYR   A 1 54  ? -9.53052  0.76596   -29.07634 1.000 14.87461  ? 61  TYR   A N   1 
ATOM   368  C CA  . TYR   A 1 54  ? -9.08150  2.04068   -29.61923 1.000 15.95622  ? 61  TYR   A CA  1 
ATOM   369  C C   . TYR   A 1 54  ? -9.06319  1.99989   -31.14280 1.000 18.92704  ? 61  TYR   A C   1 
ATOM   370  O O   . TYR   A 1 54  ? -9.50750  2.94610   -31.79622 1.000 17.73045  ? 61  TYR   A O   1 
ATOM   371  C CB  . TYR   A 1 54  ? -7.69478  2.41685   -29.07250 1.000 16.01206  ? 61  TYR   A CB  1 
ATOM   372  C CG  . TYR   A 1 54  ? -7.25763  3.79611   -29.55697 1.000 22.71787  ? 61  TYR   A CG  1 
ATOM   373  C CD1 . TYR   A 1 54  ? -7.80599  4.94834   -29.00454 1.000 18.43289  ? 61  TYR   A CD1 1 
ATOM   374  C CD2 . TYR   A 1 54  ? -6.35155  3.93859   -30.60584 1.000 21.17480  ? 61  TYR   A CD2 1 
ATOM   375  C CE1 . TYR   A 1 54  ? -7.43881  6.20587   -29.45669 1.000 23.63298  ? 61  TYR   A CE1 1 
ATOM   376  C CE2 . TYR   A 1 54  ? -5.97726  5.20639   -31.06980 1.000 23.13025  ? 61  TYR   A CE2 1 
ATOM   377  C CZ  . TYR   A 1 54  ? -6.52459  6.32625   -30.49259 1.000 22.96621  ? 61  TYR   A CZ  1 
ATOM   378  O OH  . TYR   A 1 54  ? -6.16217  7.58167   -30.93553 1.000 29.82847  ? 61  TYR   A OH  1 
ATOM   379  N N   . GLU   A 1 55  ? -8.57797  0.90140   -31.73347 1.000 15.56176  ? 62  GLU   A N   1 
ATOM   380  C CA  . GLU   A 1 55  ? -8.57564  0.81220   -33.19950 1.000 17.69354  ? 62  GLU   A CA  1 
ATOM   381  C C   . GLU   A 1 55  ? -9.98882  0.87688   -33.77001 1.000 20.41475  ? 62  GLU   A C   1 
ATOM   382  O O   . GLU   A 1 55  ? -10.21830 1.49279   -34.82051 1.000 23.17173  ? 62  GLU   A O   1 
ATOM   383  C CB  . GLU   A 1 55  ? -7.89186  -0.47801  -33.64548 1.000 19.94431  ? 62  GLU   A CB  1 
ATOM   384  C CG  . GLU   A 1 55  ? -6.40835  -0.48829  -33.34083 1.000 22.25166  ? 62  GLU   A CG  1 
ATOM   385  C CD  . GLU   A 1 55  ? -5.64665  -1.45664  -34.21064 1.000 33.03710  ? 62  GLU   A CD  1 
ATOM   386  O OE1 . GLU   A 1 55  ? -6.28156  -2.39077  -34.73935 1.000 30.17096  ? 62  GLU   A OE1 1 
ATOM   387  O OE2 . GLU   A 1 55  ? -4.40916  -1.32382  -34.31404 1.000 33.03443  ? 62  GLU   A OE2 1 
ATOM   388  N N   . SER   A 1 56  ? -10.94901 0.25213   -33.09121 1.000 19.35634  ? 63  SER   A N   1 
ATOM   389  C CA  . SER   A 1 56  ? -12.32331 0.23750   -33.57617 1.000 21.57934  ? 63  SER   A CA  1 
ATOM   390  C C   . SER   A 1 56  ? -12.98329 1.60703   -33.49868 1.000 24.93682  ? 63  SER   A C   1 
ATOM   391  O O   . SER   A 1 56  ? -13.99853 1.82564   -34.16515 1.000 21.92956  ? 63  SER   A O   1 
ATOM   392  C CB  . SER   A 1 56  ? -13.15184 -0.78754  -32.78696 1.000 20.90082  ? 63  SER   A CB  1 
ATOM   393  O OG  . SER   A 1 56  ? -13.46816 -0.31409  -31.46520 1.000 21.59713  ? 63  SER   A OG  1 
ATOM   394  N N   . LEU   A 1 57  ? -12.44581 2.53605   -32.70140 1.000 20.21850  ? 64  LEU   A N   1 
ATOM   395  C CA  . LEU   A 1 57  ? -13.07721 3.85112   -32.59800 1.000 26.46304  ? 64  LEU   A CA  1 
ATOM   396  C C   . LEU   A 1 57  ? -13.08990 4.57264   -33.92731 1.000 29.22814  ? 64  LEU   A C   1 
ATOM   397  O O   . LEU   A 1 57  ? -13.98170 5.38989   -34.18389 1.000 30.47423  ? 64  LEU   A O   1 
ATOM   398  C CB  . LEU   A 1 57  ? -12.35954 4.71815   -31.56274 1.000 21.94107  ? 64  LEU   A CB  1 
ATOM   399  C CG  . LEU   A 1 57  ? -12.52188 4.20078   -30.13964 1.000 25.80070  ? 64  LEU   A CG  1 
ATOM   400  C CD1 . LEU   A 1 57  ? -11.90537 5.17198   -29.15629 1.000 24.36855  ? 64  LEU   A CD1 1 
ATOM   401  C CD2 . LEU   A 1 57  ? -13.98648 3.95545   -29.82871 1.000 29.78139  ? 64  LEU   A CD2 1 
ATOM   402  N N   . THR   A 1 58  ? -12.10027 4.31652   -34.76911 1.000 25.31708  ? 65  THR   A N   1 
ATOM   403  C CA  . THR   A 1 58  ? -12.03476 4.95788   -36.06943 1.000 26.21683  ? 65  THR   A CA  1 
ATOM   404  C C   . THR   A 1 58  ? -12.24900 4.00184   -37.22840 1.000 31.79897  ? 65  THR   A C   1 
ATOM   405  O O   . THR   A 1 58  ? -12.41148 4.46341   -38.36386 1.000 35.62805  ? 65  THR   A O   1 
ATOM   406  C CB  . THR   A 1 58  ? -10.68968 5.67381   -36.25016 1.000 35.67594  ? 65  THR   A CB  1 
ATOM   407  O OG1 . THR   A 1 58  ? -9.63862  4.70394   -36.31479 1.000 38.48418  ? 65  THR   A OG1 1 
ATOM   408  C CG2 . THR   A 1 58  ? -10.43823 6.65822   -35.12051 1.000 34.31990  ? 65  THR   A CG2 1 
ATOM   409  N N   . ASP   A 1 59  ? -12.25254 2.69239   -36.98407 1.000 31.35146  ? 66  ASP   A N   1 
ATOM   410  C CA  . ASP   A 1 59  ? -12.49821 1.70944   -38.03872 1.000 28.63523  ? 66  ASP   A CA  1 
ATOM   411  C C   . ASP   A 1 59  ? -13.34644 0.59001   -37.44613 1.000 24.85077  ? 66  ASP   A C   1 
ATOM   412  O O   . ASP   A 1 59  ? -12.81961 -0.37638  -36.88134 1.000 25.84030  ? 66  ASP   A O   1 
ATOM   413  C CB  . ASP   A 1 59  ? -11.18154 1.18095   -38.60941 1.000 25.19218  ? 66  ASP   A CB  1 
ATOM   414  C CG  . ASP   A 1 59  ? -11.38821 0.18069   -39.73477 1.000 37.64711  ? 66  ASP   A CG  1 
ATOM   415  O OD1 . ASP   A 1 59  ? -12.54594 -0.05818  -40.12354 1.000 36.18835  ? 66  ASP   A OD1 1 
ATOM   416  O OD2 . ASP   A 1 59  ? -10.38713 -0.35164  -40.25000 1.000 36.51757  ? 66  ASP   A OD2 1 
ATOM   417  N N   . PRO   A 1 60  ? -14.67545 0.69128   -37.54842 1.000 29.91253  ? 67  PRO   A N   1 
ATOM   418  C CA  . PRO   A 1 60  ? -15.53101 -0.33862  -36.93532 1.000 31.71020  ? 67  PRO   A CA  1 
ATOM   419  C C   . PRO   A 1 60  ? -15.29755 -1.73261  -37.48656 1.000 27.04695  ? 67  PRO   A C   1 
ATOM   420  O O   . PRO   A 1 60  ? -15.54279 -2.71770  -36.77391 1.000 26.89623  ? 67  PRO   A O   1 
ATOM   421  C CB  . PRO   A 1 60  ? -16.94544 0.16313   -37.25081 1.000 37.94065  ? 67  PRO   A CB  1 
ATOM   422  C CG  . PRO   A 1 60  ? -16.78085 1.63496   -37.33675 1.000 36.86516  ? 67  PRO   A CG  1 
ATOM   423  C CD  . PRO   A 1 60  ? -15.47849 1.80177   -38.08110 1.000 36.65541  ? 67  PRO   A CD  1 
ATOM   424  N N   . SER   A 1 61  ? -14.82118 -1.85277  -38.73275 1.000 29.07230  ? 68  SER   A N   1 
ATOM   425  C CA  . SER   A 1 61  ? -14.59239 -3.17708  -39.29544 1.000 29.01806  ? 68  SER   A CA  1 
ATOM   426  C C   . SER   A 1 61  ? -13.51199 -3.94925  -38.54787 1.000 30.27260  ? 68  SER   A C   1 
ATOM   427  O O   . SER   A 1 61  ? -13.41631 -5.16782  -38.73042 1.000 22.06714  ? 68  SER   A O   1 
ATOM   428  C CB  . SER   A 1 61  ? -14.22426 -3.07957  -40.77970 1.000 29.51821  ? 68  SER   A CB  1 
ATOM   429  O OG  . SER   A 1 61  ? -12.94408 -2.50192  -40.95040 1.000 30.96246  ? 68  SER   A OG  1 
ATOM   430  N N   . LYS   A 1 62  ? -12.70003 -3.28152  -37.71179 1.000 23.48977  ? 69  LYS   A N   1 
ATOM   431  C CA  . LYS   A 1 62  ? -11.73270 -3.99388  -36.88669 1.000 24.68419  ? 69  LYS   A CA  1 
ATOM   432  C C   . LYS   A 1 62  ? -12.40497 -5.01505  -35.97880 1.000 23.63389  ? 69  LYS   A C   1 
ATOM   433  O O   . LYS   A 1 62  ? -11.74008 -5.94124  -35.49479 1.000 19.88439  ? 69  LYS   A O   1 
ATOM   434  C CB  . LYS   A 1 62  ? -10.93385 -2.99135  -36.04610 1.000 24.40521  ? 69  LYS   A CB  1 
ATOM   435  C CG  . LYS   A 1 62  ? -10.06010 -2.06028  -36.88479 1.000 29.96260  ? 69  LYS   A CG  1 
ATOM   436  C CD  . LYS   A 1 62  ? -8.65500  -2.61190  -37.01911 1.000 32.79249  ? 69  LYS   A CD  1 
ATOM   437  C CE  . LYS   A 1 62  ? -7.76756  -1.70778  -37.86520 1.000 30.21448  ? 69  LYS   A CE  1 
ATOM   438  N NZ  . LYS   A 1 62  ? -6.36199  -2.23598  -37.82857 1.000 31.59555  ? 69  LYS   A NZ  1 
ATOM   439  N N   . LEU   A 1 63  ? -13.70108 -4.85673  -35.71331 1.000 21.92103  ? 70  LEU   A N   1 
ATOM   440  C CA  . LEU   A 1 63  ? -14.42997 -5.78982  -34.86811 1.000 20.70826  ? 70  LEU   A CA  1 
ATOM   441  C C   . LEU   A 1 63  ? -15.23844 -6.79453  -35.67339 1.000 23.60577  ? 70  LEU   A C   1 
ATOM   442  O O   . LEU   A 1 63  ? -16.08053 -7.49296  -35.09628 1.000 21.84445  ? 70  LEU   A O   1 
ATOM   443  C CB  . LEU   A 1 63  ? -15.35099 -5.03343  -33.90295 1.000 23.04475  ? 70  LEU   A CB  1 
ATOM   444  C CG  . LEU   A 1 63  ? -14.65649 -4.09166  -32.91767 1.000 22.82800  ? 70  LEU   A CG  1 
ATOM   445  C CD1 . LEU   A 1 63  ? -15.67237 -3.45996  -31.95863 1.000 25.08020  ? 70  LEU   A CD1 1 
ATOM   446  C CD2 . LEU   A 1 63  ? -13.57575 -4.83929  -32.14338 1.000 22.00424  ? 70  LEU   A CD2 1 
ATOM   447  N N   . ASP   A 1 64  ? -15.00988 -6.88468  -36.98829 1.000 19.58987  ? 71  ASP   A N   1 
ATOM   448  C CA  . ASP   A 1 64  ? -15.71712 -7.90040  -37.76477 1.000 22.13055  ? 71  ASP   A CA  1 
ATOM   449  C C   . ASP   A 1 64  ? -15.34877 -9.30276  -37.30128 1.000 25.87068  ? 71  ASP   A C   1 
ATOM   450  O O   . ASP   A 1 64  ? -16.12374 -10.24525 -37.50203 1.000 25.36650  ? 71  ASP   A O   1 
ATOM   451  C CB  . ASP   A 1 64  ? -15.40897 -7.76368  -39.25535 1.000 24.34201  ? 71  ASP   A CB  1 
ATOM   452  C CG  . ASP   A 1 64  ? -16.11056 -6.56889  -39.90559 1.000 38.18992  ? 71  ASP   A CG  1 
ATOM   453  O OD1 . ASP   A 1 64  ? -16.90933 -5.88189  -39.23678 1.000 33.58988  ? 71  ASP   A OD1 1 
ATOM   454  O OD2 . ASP   A 1 64  ? -15.87230 -6.32874  -41.10743 1.000 38.43147  ? 71  ASP   A OD2 1 
ATOM   455  N N   . SER   A 1 65  ? -14.17314 -9.45564  -36.71068 1.000 21.87447  ? 72  SER   A N   1 
ATOM   456  C CA  . SER   A 1 65  ? -13.67976 -10.70736 -36.15947 1.000 21.90322  ? 72  SER   A CA  1 
ATOM   457  C C   . SER   A 1 65  ? -14.24132 -11.00757 -34.77522 1.000 27.01873  ? 72  SER   A C   1 
ATOM   458  O O   . SER   A 1 65  ? -13.85464 -12.01091 -34.17450 1.000 26.68629  ? 72  SER   A O   1 
ATOM   459  C CB  . SER   A 1 65  ? -12.14036 -10.65734 -36.10883 1.000 25.62990  ? 72  SER   A CB  1 
ATOM   460  O OG  . SER   A 1 65  ? -11.68801 -9.40546  -35.56672 1.000 20.87313  ? 72  SER   A OG  1 
ATOM   461  N N   . GLY   A 1 66  ? -15.12197 -10.15749 -34.25128 1.000 23.40610  ? 73  GLY   A N   1 
ATOM   462  C CA  . GLY   A 1 66  ? -15.81540 -10.39918 -32.99912 1.000 27.27923  ? 73  GLY   A CA  1 
ATOM   463  C C   . GLY   A 1 66  ? -16.09562 -9.10197  -32.26128 1.000 21.88328  ? 73  GLY   A C   1 
ATOM   464  O O   . GLY   A 1 66  ? -15.16265 -8.37086  -31.93802 1.000 20.77318  ? 73  GLY   A O   1 
ATOM   465  N N   . LYS   A 1 67  ? -17.36771 -8.78407  -32.00213 1.000 21.78237  ? 74  LYS   A N   1 
ATOM   466  C CA  . LYS   A 1 67  ? -17.68573 -7.53455  -31.31541 1.000 21.43331  ? 74  LYS   A CA  1 
ATOM   467  C C   . LYS   A 1 67  ? -17.52370 -7.60873  -29.80173 1.000 23.27045  ? 74  LYS   A C   1 
ATOM   468  O O   . LYS   A 1 67  ? -17.35416 -6.56550  -29.16200 1.000 23.83905  ? 74  LYS   A O   1 
ATOM   469  C CB  . LYS   A 1 67  ? -19.12656 -7.09596  -31.63828 1.000 21.46841  ? 74  LYS   A CB  1 
ATOM   470  C CG  . LYS   A 1 67  ? -19.41257 -6.94794  -33.12475 1.000 41.53244  ? 74  LYS   A CG  1 
ATOM   471  C CD  . LYS   A 1 67  ? -20.91383 -6.99556  -33.40905 1.000 52.01955  ? 74  LYS   A CD  1 
ATOM   472  C CE  . LYS   A 1 67  ? -21.74777 -6.59383  -32.18940 1.000 60.26985  ? 74  LYS   A CE  1 
ATOM   473  N NZ  . LYS   A 1 67  ? -23.18736 -6.98080  -32.35023 1.000 75.83473  ? 74  LYS   A NZ  1 
ATOM   474  N N   . GLU   A 1 68  ? -17.57710 -8.79225  -29.20230 1.000 18.93959  ? 75  GLU   A N   1 
ATOM   475  C CA  . GLU   A 1 68  ? -17.54051 -8.85372  -27.74584 1.000 19.65823  ? 75  GLU   A CA  1 
ATOM   476  C C   . GLU   A 1 68  ? -16.11576 -8.67202  -27.23147 1.000 19.01435  ? 75  GLU   A C   1 
ATOM   477  O O   . GLU   A 1 68  ? -15.17205 -9.25224  -27.76569 1.000 24.20386  ? 75  GLU   A O   1 
ATOM   478  C CB  . GLU   A 1 68  ? -18.10409 -10.18200 -27.24746 1.000 25.63952  ? 75  GLU   A CB  1 
ATOM   479  C CG  . GLU   A 1 68  ? -19.62599 -10.29609 -27.36358 1.000 29.41673  ? 75  GLU   A CG  1 
ATOM   480  C CD  . GLU   A 1 68  ? -20.08495 -10.57056 -28.78793 1.000 65.90270  ? 75  GLU   A CD  1 
ATOM   481  O OE1 . GLU   A 1 68  ? -19.45192 -11.42330 -29.45124 1.000 68.31872  ? 75  GLU   A OE1 1 
ATOM   482  O OE2 . GLU   A 1 68  ? -21.07652 -9.94504  -29.23922 1.000 58.44408  ? 75  GLU   A OE2 1 
ATOM   483  N N   . LEU   A 1 69  ? -15.97960 -7.90019  -26.16065 1.000 16.08986  ? 76  LEU   A N   1 
ATOM   484  C CA  . LEU   A 1 69  ? -14.68232 -7.59898  -25.54713 1.000 14.71896  ? 76  LEU   A CA  1 
ATOM   485  C C   . LEU   A 1 69  ? -14.71914 -8.13859  -24.12103 1.000 17.15960  ? 76  LEU   A C   1 
ATOM   486  O O   . LEU   A 1 69  ? -15.33904 -7.52243  -23.24336 1.000 16.84820  ? 76  LEU   A O   1 
ATOM   487  C CB  . LEU   A 1 69  ? -14.43669 -6.09409  -25.57989 1.000 18.28619  ? 76  LEU   A CB  1 
ATOM   488  C CG  . LEU   A 1 69  ? -14.34129 -5.46059  -26.97909 1.000 21.03333  ? 76  LEU   A CG  1 
ATOM   489  C CD1 . LEU   A 1 69  ? -13.98139 -4.00010  -26.83691 1.000 26.53509  ? 76  LEU   A CD1 1 
ATOM   490  C CD2 . LEU   A 1 69  ? -13.31266 -6.16671  -27.86063 1.000 17.26727  ? 76  LEU   A CD2 1 
ATOM   491  N N   . HIS   A 1 70  ? -14.06980 -9.27817  -23.87263 1.000 16.19960  ? 77  HIS   A N   1 
ATOM   492  C CA  . HIS   A 1 70  ? -14.21495 -9.90624  -22.56008 1.000 17.09939  ? 77  HIS   A CA  1 
ATOM   493  C C   . HIS   A 1 70  ? -13.01447 -10.79105 -22.24075 1.000 13.54545  ? 77  HIS   A C   1 
ATOM   494  O O   . HIS   A 1 70  ? -12.13888 -11.03593 -23.07926 1.000 13.03245  ? 77  HIS   A O   1 
ATOM   495  C CB  . HIS   A 1 70  ? -15.49941 -10.74428 -22.49104 1.000 15.62660  ? 77  HIS   A CB  1 
ATOM   496  C CG  . HIS   A 1 70  ? -15.52934 -11.87031 -23.47795 1.000 19.29450  ? 77  HIS   A CG  1 
ATOM   497  N ND1 . HIS   A 1 70  ? -16.53601 -12.01945 -24.40267 1.000 26.40223  ? 77  HIS   A ND1 1 
ATOM   498  C CD2 . HIS   A 1 70  ? -14.67440 -12.90285 -23.68630 1.000 21.93660  ? 77  HIS   A CD2 1 
ATOM   499  C CE1 . HIS   A 1 70  ? -16.30380 -13.09225 -25.13766 1.000 20.76526  ? 77  HIS   A CE1 1 
ATOM   500  N NE2 . HIS   A 1 70  ? -15.17539 -13.64031 -24.73259 1.000 22.82456  ? 77  HIS   A NE2 1 
ATOM   501  N N   . ILE   A 1 71  ? -13.01142 -11.28761 -21.00131 1.000 12.03213  ? 78  ILE   A N   1 
ATOM   502  C CA  . ILE   A 1 71  ? -11.97149 -12.14858 -20.45601 1.000 11.80517  ? 78  ILE   A CA  1 
ATOM   503  C C   . ILE   A 1 71  ? -12.65362 -13.35134 -19.81955 1.000 14.91591  ? 78  ILE   A C   1 
ATOM   504  O O   . ILE   A 1 71  ? -13.52900 -13.17629 -18.96874 1.000 13.36295  ? 78  ILE   A O   1 
ATOM   505  C CB  . ILE   A 1 71  ? -11.12067 -11.40669 -19.40013 1.000 12.33827  ? 78  ILE   A CB  1 
ATOM   506  C CG1 . ILE   A 1 71  ? -10.53566 -10.12272 -19.98101 1.000 12.34623  ? 78  ILE   A CG1 1 
ATOM   507  C CG2 . ILE   A 1 71  ? -10.01919 -12.34709 -18.83918 1.000 11.93446  ? 78  ILE   A CG2 1 
ATOM   508  C CD1 . ILE   A 1 71  ? -9.72963  -9.32361  -18.93817 1.000 15.47711  ? 78  ILE   A CD1 1 
ATOM   509  N N   . ASN   A 1 72  ? -12.26293 -14.56139 -20.22581 1.000 12.96756  ? 79  ASN   A N   1 
ATOM   510  C CA  . ASN   A 1 72  ? -12.78517 -15.78703 -19.62884 1.000 13.67967  ? 79  ASN   A CA  1 
ATOM   511  C C   . ASN   A 1 72  ? -11.67446 -16.54285 -18.90972 1.000 14.79548  ? 79  ASN   A C   1 
ATOM   512  O O   . ASN   A 1 72  ? -10.55298 -16.65464 -19.41852 1.000 14.50660  ? 79  ASN   A O   1 
ATOM   513  C CB  . ASN   A 1 72  ? -13.41499 -16.71518 -20.67909 1.000 12.40880  ? 79  ASN   A CB  1 
ATOM   514  C CG  . ASN   A 1 72  ? -14.62772 -16.12164 -21.34870 1.000 16.75372  ? 79  ASN   A CG  1 
ATOM   515  O OD1 . ASN   A 1 72  ? -15.35550 -15.32196 -20.75011 1.000 15.78709  ? 79  ASN   A OD1 1 
ATOM   516  N ND2 . ASN   A 1 72  ? -14.88125 -16.54497 -22.58394 1.000 16.97859  ? 79  ASN   A ND2 1 
ATOM   517  N N   . LEU   A 1 73  ? -12.00765 -17.10867 -17.75040 1.000 13.45832  ? 80  LEU   A N   1 
ATOM   518  C CA  . LEU   A 1 73  ? -11.08757 -17.93156 -16.97319 1.000 11.85240  ? 80  LEU   A CA  1 
ATOM   519  C C   . LEU   A 1 73  ? -11.64760 -19.34157 -16.94141 1.000 13.66795  ? 80  LEU   A C   1 
ATOM   520  O O   . LEU   A 1 73  ? -12.75849 -19.55277 -16.44483 1.000 12.97050  ? 80  LEU   A O   1 
ATOM   521  C CB  . LEU   A 1 73  ? -10.92319 -17.37649 -15.55144 1.000 12.37797  ? 80  LEU   A CB  1 
ATOM   522  C CG  . LEU   A 1 73  ? -10.54984 -15.89252 -15.41649 1.000 14.41031  ? 80  LEU   A CG  1 
ATOM   523  C CD1 . LEU   A 1 73  ? -10.48930 -15.49592 -13.95430 1.000 12.21017  ? 80  LEU   A CD1 1 
ATOM   524  C CD2 . LEU   A 1 73  ? -9.20349  -15.64917 -16.07031 1.000 12.50155  ? 80  LEU   A CD2 1 
ATOM   525  N N   . ILE   A 1 74  ? -10.91846 -20.30034 -17.50740 1.000 12.41356  ? 81  ILE   A N   1 
ATOM   526  C CA  . ILE   A 1 74  ? -11.42725 -21.64737 -17.70549 1.000 13.83643  ? 81  ILE   A CA  1 
ATOM   527  C C   . ILE   A 1 74  ? -10.49928 -22.63908 -17.01857 1.000 14.40195  ? 81  ILE   A C   1 
ATOM   528  O O   . ILE   A 1 74  ? -9.45877  -23.01240 -17.56579 1.000 14.08184  ? 81  ILE   A O   1 
ATOM   529  C CB  . ILE   A 1 74  ? -11.58269 -21.99003 -19.19965 1.000 13.55580  ? 81  ILE   A CB  1 
ATOM   530  C CG1 . ILE   A 1 74  ? -12.32657 -20.86043 -19.91528 1.000 16.16983  ? 81  ILE   A CG1 1 
ATOM   531  C CG2 . ILE   A 1 74  ? -12.30174 -23.30571 -19.33236 1.000 14.26901  ? 81  ILE   A CG2 1 
ATOM   532  C CD1 . ILE   A 1 74  ? -12.41989 -21.02839 -21.42538 1.000 20.59399  ? 81  ILE   A CD1 1 
ATOM   533  N N   . PRO   A 1 75  ? -10.85907 -23.10600 -15.82294 1.000 14.92034  ? 82  PRO   A N   1 
ATOM   534  C CA  . PRO   A 1 75  ? -10.08863 -24.17726 -15.18765 1.000 14.34902  ? 82  PRO   A CA  1 
ATOM   535  C C   . PRO   A 1 75  ? -10.54557 -25.53410 -15.69619 1.000 17.16549  ? 82  PRO   A C   1 
ATOM   536  O O   . PRO   A 1 75  ? -11.72597 -25.74957 -15.97956 1.000 18.79289  ? 82  PRO   A O   1 
ATOM   537  C CB  . PRO   A 1 75  ? -10.42685 -24.01893 -13.69802 1.000 16.65905  ? 82  PRO   A CB  1 
ATOM   538  C CG  . PRO   A 1 75  ? -11.86095 -23.48678 -13.70147 1.000 19.20882  ? 82  PRO   A CG  1 
ATOM   539  C CD  . PRO   A 1 75  ? -12.05140 -22.72783 -15.02974 1.000 16.69831  ? 82  PRO   A CD  1 
ATOM   540  N N   . ASN   A 1 76  ? -9.59120  -26.46177 -15.78994 1.000 15.62139  ? 83  ASN   A N   1 
ATOM   541  C CA  . ASN   A 1 76  ? -9.88220  -27.83494 -16.20056 1.000 17.80203  ? 83  ASN   A CA  1 
ATOM   542  C C   . ASN   A 1 76  ? -9.06834  -28.78033 -15.33466 1.000 18.86831  ? 83  ASN   A C   1 
ATOM   543  O O   . ASN   A 1 76  ? -7.86710  -28.94368 -15.55853 1.000 20.49227  ? 83  ASN   A O   1 
ATOM   544  C CB  . ASN   A 1 76  ? -9.57951  -28.06363 -17.68279 1.000 18.42878  ? 83  ASN   A CB  1 
ATOM   545  C CG  . ASN   A 1 76  ? -10.08014 -29.42941 -18.17022 1.000 30.18212  ? 83  ASN   A CG  1 
ATOM   546  O OD1 . ASN   A 1 76  ? -9.79546  -30.46096 -17.56731 1.000 26.62621  ? 83  ASN   A OD1 1 
ATOM   547  N ND2 . ASN   A 1 76  ? -10.85572 -29.42759 -19.24135 1.000 29.45503  ? 83  ASN   A ND2 1 
ATOM   548  N N   . LYS   A 1 77  ? -9.72763  -29.44145 -14.38272 1.000 21.89611  ? 84  LYS   A N   1 
ATOM   549  C CA  . LYS   A 1 77  ? -8.98936  -30.28158 -13.44166 1.000 21.14872  ? 84  LYS   A CA  1 
ATOM   550  C C   . LYS   A 1 77  ? -8.51117  -31.57454 -14.09011 1.000 25.05945  ? 84  LYS   A C   1 
ATOM   551  O O   . LYS   A 1 77  ? -7.47779  -32.11483 -13.68368 1.000 24.70773  ? 84  LYS   A O   1 
ATOM   552  C CB  . LYS   A 1 77  ? -9.84729  -30.60231 -12.22010 1.000 22.74444  ? 84  LYS   A CB  1 
ATOM   553  C CG  . LYS   A 1 77  ? -10.13141 -29.40323 -11.32195 1.000 29.52675  ? 84  LYS   A CG  1 
ATOM   554  C CD  . LYS   A 1 77  ? -10.92374 -29.82975 -10.09347 1.000 34.27412  ? 84  LYS   A CD  1 
ATOM   555  C CE  . LYS   A 1 77  ? -11.20615 -28.66547 -9.14685  1.000 32.18902  ? 84  LYS   A CE  1 
ATOM   556  N NZ  . LYS   A 1 77  ? -12.00681 -27.62345 -9.83260  1.000 39.48727  ? 84  LYS   A NZ  1 
ATOM   557  N N   . GLN   A 1 78  ? -9.22731  -32.07176 -15.10362 1.000 26.49487  ? 85  GLN   A N   1 
ATOM   558  C CA  . GLN   A 1 78  ? -8.80273  -33.30547 -15.76733 1.000 28.57359  ? 85  GLN   A CA  1 
ATOM   559  C C   . GLN   A 1 78  ? -7.50842  -33.10149 -16.54293 1.000 31.45976  ? 85  GLN   A C   1 
ATOM   560  O O   . GLN   A 1 78  ? -6.62525  -33.96298 -16.51261 1.000 30.03125  ? 85  GLN   A O   1 
ATOM   561  C CB  . GLN   A 1 78  ? -9.90350  -33.82956 -16.68870 1.000 35.60017  ? 85  GLN   A CB  1 
ATOM   562  C CG  . GLN   A 1 78  ? -11.10210 -34.42934 -15.95533 1.000 51.59510  ? 85  GLN   A CG  1 
ATOM   563  C CD  . GLN   A 1 78  ? -11.87118 -33.39513 -15.14401 1.000 61.24409  ? 85  GLN   A CD  1 
ATOM   564  O OE1 . GLN   A 1 78  ? -11.99977 -33.52305 -13.92275 1.000 59.84007  ? 85  GLN   A OE1 1 
ATOM   565  N NE2 . GLN   A 1 78  ? -12.35093 -32.34426 -15.81261 1.000 54.55799  ? 85  GLN   A NE2 1 
ATOM   566  N N   . ASP   A 1 79  ? -7.37194  -31.96762 -17.22705 1.000 25.37692  ? 86  ASP   A N   1 
ATOM   567  C CA  . ASP   A 1 79  ? -6.16426  -31.63930 -17.96828 1.000 25.95245  ? 86  ASP   A CA  1 
ATOM   568  C C   . ASP   A 1 79  ? -5.13133  -30.93943 -17.10459 1.000 23.19792  ? 86  ASP   A C   1 
ATOM   569  O O   . ASP   A 1 79  ? -3.97921  -30.81235 -17.53097 1.000 22.31098  ? 86  ASP   A O   1 
ATOM   570  C CB  . ASP   A 1 79  ? -6.49202  -30.72877 -19.15533 1.000 28.42381  ? 86  ASP   A CB  1 
ATOM   571  C CG  . ASP   A 1 79  ? -7.41784  -31.38840 -20.15482 1.000 47.38215  ? 86  ASP   A CG  1 
ATOM   572  O OD1 . ASP   A 1 79  ? -7.61559  -32.61967 -20.06511 1.000 48.90812  ? 86  ASP   A OD1 1 
ATOM   573  O OD2 . ASP   A 1 79  ? -7.94476  -30.67614 -21.03167 1.000 39.35966  ? 86  ASP   A OD2 1 
ATOM   574  N N   . ARG   A 1 80  ? -5.53252  -30.49539 -15.90896 1.000 19.92677  ? 87  ARG   A N   1 
ATOM   575  C CA  . ARG   A 1 80  ? -4.71291  -29.68238 -15.00759 1.000 18.06428  ? 87  ARG   A CA  1 
ATOM   576  C C   . ARG   A 1 80  ? -4.23118  -28.40994 -15.70554 1.000 18.10912  ? 87  ARG   A C   1 
ATOM   577  O O   . ARG   A 1 80  ? -3.04051  -28.07401 -15.71186 1.000 19.37567  ? 87  ARG   A O   1 
ATOM   578  C CB  . ARG   A 1 80  ? -3.54495  -30.48472 -14.41904 1.000 23.23237  ? 87  ARG   A CB  1 
ATOM   579  C CG  . ARG   A 1 80  ? -3.10491  -29.94729 -13.06687 1.000 25.16627  ? 87  ARG   A CG  1 
ATOM   580  C CD  . ARG   A 1 80  ? -1.64549  -30.17710 -12.74841 1.000 32.50658  ? 87  ARG   A CD  1 
ATOM   581  N NE  . ARG   A 1 80  ? -1.35950  -31.57860 -12.49488 1.000 45.50638  ? 87  ARG   A NE  1 
ATOM   582  C CZ  . ARG   A 1 80  ? -0.19195  -32.16203 -12.73057 1.000 50.72979  ? 87  ARG   A CZ  1 
ATOM   583  N NH1 . ARG   A 1 80  ? 0.84933   -31.47699 -13.17939 1.000 35.34504  ? 87  ARG   A NH1 1 
ATOM   584  N NH2 . ARG   A 1 80  ? -0.05737  -33.46092 -12.48497 1.000 41.09737  ? 87  ARG   A NH2 1 
ATOM   585  N N   . THR   A 1 81  ? -5.17881  -27.68836 -16.29374 1.000 16.22529  ? 88  THR   A N   1 
ATOM   586  C CA  . THR   A 1 81  ? -4.87748  -26.44973 -16.98973 1.000 16.21632  ? 88  THR   A CA  1 
ATOM   587  C C   . THR   A 1 81  ? -5.79361  -25.33402 -16.51760 1.000 16.87671  ? 88  THR   A C   1 
ATOM   588  O O   . THR   A 1 81  ? -6.95817  -25.55458 -16.17484 1.000 18.21584  ? 88  THR   A O   1 
ATOM   589  C CB  . THR   A 1 81  ? -4.99848  -26.56182 -18.52946 1.000 18.00465  ? 88  THR   A CB  1 
ATOM   590  O OG1 . THR   A 1 81  ? -6.32644  -26.96441 -18.89608 1.000 18.50787  ? 88  THR   A OG1 1 
ATOM   591  C CG2 . THR   A 1 81  ? -3.94093  -27.50834 -19.11605 1.000 19.63486  ? 88  THR   A CG2 1 
ATOM   592  N N   . LEU   A 1 82  ? -5.24192  -24.12920 -16.49812 1.000 13.77150  ? 89  LEU   A N   1 
ATOM   593  C CA  . LEU   A 1 82  ? -6.01900  -22.90821 -16.31975 1.000 13.34733  ? 89  LEU   A CA  1 
ATOM   594  C C   . LEU   A 1 82  ? -5.80039  -22.07682 -17.56967 1.000 13.82452  ? 89  LEU   A C   1 
ATOM   595  O O   . LEU   A 1 82  ? -4.65681  -21.76992 -17.91137 1.000 16.20768  ? 89  LEU   A O   1 
ATOM   596  C CB  . LEU   A 1 82  ? -5.58276  -22.12626 -15.06899 1.000 15.80210  ? 89  LEU   A CB  1 
ATOM   597  C CG  . LEU   A 1 82  ? -6.31749  -20.77952 -14.85597 1.000 12.37981  ? 89  LEU   A CG  1 
ATOM   598  C CD1 . LEU   A 1 82  ? -7.81482  -21.01475 -14.67308 1.000 13.73636  ? 89  LEU   A CD1 1 
ATOM   599  C CD2 . LEU   A 1 82  ? -5.73821  -20.07139 -13.62518 1.000 14.81031  ? 89  LEU   A CD2 1 
ATOM   600  N N   . THR   A 1 83  ? -6.88251  -21.73229 -18.26133 1.000 12.31058  ? 90  THR   A N   1 
ATOM   601  C CA  . THR   A 1 83  ? -6.79269  -20.98541 -19.51093 1.000 13.93631  ? 90  THR   A CA  1 
ATOM   602  C C   . THR   A 1 83  ? -7.37709  -19.58871 -19.31987 1.000 15.30852  ? 90  THR   A C   1 
ATOM   603  O O   . THR   A 1 83  ? -8.48549  -19.44415 -18.78619 1.000 15.59540  ? 90  THR   A O   1 
ATOM   604  C CB  . THR   A 1 83  ? -7.53725  -21.71217 -20.63256 1.000 16.44405  ? 90  THR   A CB  1 
ATOM   605  O OG1 . THR   A 1 83  ? -6.97440  -23.02166 -20.82243 1.000 16.24712  ? 90  THR   A OG1 1 
ATOM   606  C CG2 . THR   A 1 83  ? -7.43721  -20.92215 -21.91666 1.000 15.12647  ? 90  THR   A CG2 1 
ATOM   607  N N   . ILE   A 1 84  ? -6.61810  -18.56800 -19.71209 1.000 13.33907  ? 91  ILE   A N   1 
ATOM   608  C CA  . ILE   A 1 84  ? -7.07479  -17.17738 -19.68715 1.000 15.42372  ? 91  ILE   A CA  1 
ATOM   609  C C   . ILE   A 1 84  ? -7.34061  -16.78529 -21.14004 1.000 12.42716  ? 91  ILE   A C   1 
ATOM   610  O O   . ILE   A 1 84  ? -6.40547  -16.73674 -21.94751 1.000 14.73746  ? 91  ILE   A O   1 
ATOM   611  C CB  . ILE   A 1 84  ? -6.04336  -16.24471 -19.02842 1.000 15.37787  ? 91  ILE   A CB  1 
ATOM   612  C CG1 . ILE   A 1 84  ? -5.81457  -16.61845 -17.55066 1.000 21.14725  ? 91  ILE   A CG1 1 
ATOM   613  C CG2 . ILE   A 1 84  ? -6.50039  -14.79973 -19.09911 1.000 13.75915  ? 91  ILE   A CG2 1 
ATOM   614  C CD1 . ILE   A 1 84  ? -4.71428  -17.61807 -17.29043 1.000 27.32325  ? 91  ILE   A CD1 1 
ATOM   615  N N   . VAL   A 1 85  ? -8.60605  -16.52239 -21.48610 1.000 10.77311  ? 92  VAL   A N   1 
ATOM   616  C CA  . VAL   A 1 85  ? -9.01976  -16.19215 -22.85122 1.000 11.09042  ? 92  VAL   A CA  1 
ATOM   617  C C   . VAL   A 1 85  ? -9.41751  -14.72889 -22.89819 1.000 18.15463  ? 92  VAL   A C   1 
ATOM   618  O O   . VAL   A 1 85  ? -10.20026 -14.27122 -22.06017 1.000 15.87875  ? 92  VAL   A O   1 
ATOM   619  C CB  . VAL   A 1 85  ? -10.19793 -17.05599 -23.34356 1.000 15.14779  ? 92  VAL   A CB  1 
ATOM   620  C CG1 . VAL   A 1 85  ? -10.45988 -16.78633 -24.83409 1.000 18.01415  ? 92  VAL   A CG1 1 
ATOM   621  C CG2 . VAL   A 1 85  ? -9.92386  -18.53679 -23.12798 1.000 17.43015  ? 92  VAL   A CG2 1 
ATOM   622  N N   . ASP   A 1 86  ? -8.91789  -13.99855 -23.89710 1.000 14.38066  ? 93  ASP   A N   1 
ATOM   623  C CA  . ASP   A 1 86  ? -9.41220  -12.64459 -24.14388 1.000 11.84601  ? 93  ASP   A CA  1 
ATOM   624  C C   . ASP   A 1 86  ? -9.67121  -12.46644 -25.63137 1.000 15.24391  ? 93  ASP   A C   1 
ATOM   625  O O   . ASP   A 1 86  ? -9.15428  -13.20724 -26.46545 1.000 16.23842  ? 93  ASP   A O   1 
ATOM   626  C CB  . ASP   A 1 86  ? -8.44144  -11.56496 -23.60599 1.000 13.21154  ? 93  ASP   A CB  1 
ATOM   627  C CG  . ASP   A 1 86  ? -7.14620  -11.45800 -24.40475 1.000 20.63304  ? 93  ASP   A CG  1 
ATOM   628  O OD1 . ASP   A 1 86  ? -7.14934  -11.07904 -25.60033 1.000 17.18763  ? 93  ASP   A OD1 1 
ATOM   629  O OD2 . ASP   A 1 86  ? -6.09622  -11.80835 -23.83152 1.000 16.37407  ? 93  ASP   A OD2 1 
ATOM   630  N N   . THR   A 1 87  ? -10.52327 -11.50239 -25.95123 1.000 11.57702  ? 94  THR   A N   1 
ATOM   631  C CA  . THR   A 1 87  ? -10.84665 -11.17713 -27.33523 1.000 12.90164  ? 94  THR   A CA  1 
ATOM   632  C C   . THR   A 1 87  ? -10.19524 -9.85033  -27.71109 1.000 17.25849  ? 94  THR   A C   1 
ATOM   633  O O   . THR   A 1 87  ? -10.77219 -9.03030  -28.41851 1.000 16.55789  ? 94  THR   A O   1 
ATOM   634  C CB  . THR   A 1 87  ? -12.36042 -11.14198 -27.55963 1.000 16.04695  ? 94  THR   A CB  1 
ATOM   635  O OG1 . THR   A 1 87  ? -13.00104 -10.27934 -26.60486 1.000 13.71922  ? 94  THR   A OG1 1 
ATOM   636  C CG2 . THR   A 1 87  ? -12.92743 -12.56134 -27.41611 1.000 16.06243  ? 94  THR   A CG2 1 
ATOM   637  N N   . GLY   A 1 88  ? -8.97489  -9.63767  -27.22385 1.000 14.92167  ? 95  GLY   A N   1 
ATOM   638  C CA  . GLY   A 1 88  ? -8.24060  -8.42556  -27.51590 1.000 13.96926  ? 95  GLY   A CA  1 
ATOM   639  C C   . GLY   A 1 88  ? -7.64621  -8.42494  -28.90920 1.000 13.50334  ? 95  GLY   A C   1 
ATOM   640  O O   . GLY   A 1 88  ? -8.05437  -9.17967  -29.79664 1.000 13.41652  ? 95  GLY   A O   1 
ATOM   641  N N   . ILE   A 1 89  ? -6.64385  -7.56181  -29.09862 1.000 13.95630  ? 96  ILE   A N   1 
ATOM   642  C CA  . ILE   A 1 89  ? -6.10983  -7.34947  -30.44442 1.000 14.57903  ? 96  ILE   A CA  1 
ATOM   643  C C   . ILE   A 1 89  ? -5.33943  -8.56619  -30.97678 1.000 15.67081  ? 96  ILE   A C   1 
ATOM   644  O O   . ILE   A 1 89  ? -5.19589  -8.71328  -32.20096 1.000 15.12441  ? 96  ILE   A O   1 
ATOM   645  C CB  . ILE   A 1 89  ? -5.23880  -6.07351  -30.45481 1.000 15.64773  ? 96  ILE   A CB  1 
ATOM   646  C CG1 . ILE   A 1 89  ? -4.90979  -5.65047  -31.89000 1.000 19.46821  ? 96  ILE   A CG1 1 
ATOM   647  C CG2 . ILE   A 1 89  ? -3.97489  -6.29088  -29.64603 1.000 14.54623  ? 96  ILE   A CG2 1 
ATOM   648  C CD1 . ILE   A 1 89  ? -4.61662  -4.17217  -31.99085 1.000 18.67229  ? 96  ILE   A CD1 1 
ATOM   649  N N   . GLY   A 1 90  ? -4.87627  -9.46983  -30.10663 1.000 13.23568  ? 97  GLY   A N   1 
ATOM   650  C CA  . GLY   A 1 90  ? -4.10248  -10.61694 -30.56257 1.000 14.18832  ? 97  GLY   A CA  1 
ATOM   651  C C   . GLY   A 1 90  ? -2.68256  -10.23116 -30.92715 1.000 16.64998  ? 97  GLY   A C   1 
ATOM   652  O O   . GLY   A 1 90  ? -2.24978  -9.09413  -30.76171 1.000 15.89630  ? 97  GLY   A O   1 
ATOM   653  N N   . MET   A 1 91  ? -1.92917  -11.21950 -31.41095 1.000 13.79976  ? 98  MET   A N   1 
ATOM   654  C CA  . MET   A 1 91  ? -0.55101  -10.95589 -31.79931 1.000 13.55515  ? 98  MET   A CA  1 
ATOM   655  C C   . MET   A 1 91  ? -0.28154  -11.61892 -33.13767 1.000 14.37659  ? 98  MET   A C   1 
ATOM   656  O O   . MET   A 1 91  ? -0.76552  -12.72325 -33.38970 1.000 16.23861  ? 98  MET   A O   1 
ATOM   657  C CB  . MET   A 1 91  ? 0.51445   -11.48775 -30.81080 1.000 18.01641  ? 98  MET   A CB  1 
ATOM   658  C CG  . MET   A 1 91  ? 0.58891   -10.78164 -29.45513 1.000 20.87367  ? 98  MET   A CG  1 
ATOM   659  S SD  . MET   A 1 91  ? 1.43429   -11.77334 -28.20066 1.000 18.21933  ? 98  MET   A SD  1 
ATOM   660  C CE  . MET   A 1 91  ? 0.19094   -12.92505 -27.62739 1.000 20.28065  ? 98  MET   A CE  1 
ATOM   661  N N   . THR   A 1 92  ? 0.51479   -10.95478 -33.97732 1.000 16.02017  ? 99  THR   A N   1 
ATOM   662  C CA  . THR   A 1 92  ? 1.02030   -11.56603 -35.20908 1.000 19.56022  ? 99  THR   A CA  1 
ATOM   663  C C   . THR   A 1 92  ? 2.11903   -12.58446 -34.88527 1.000 16.64890  ? 99  THR   A C   1 
ATOM   664  O O   . THR   A 1 92  ? 2.60091   -12.68255 -33.74582 1.000 16.97689  ? 99  THR   A O   1 
ATOM   665  C CB  . THR   A 1 92  ? 1.60250   -10.50191 -36.13901 1.000 18.06325  ? 99  THR   A CB  1 
ATOM   666  O OG1 . THR   A 1 92  ? 2.76086   -9.92408  -35.51166 1.000 20.39379  ? 99  THR   A OG1 1 
ATOM   667  C CG2 . THR   A 1 92  ? 0.57011   -9.40497  -36.41414 1.000 23.23348  ? 99  THR   A CG2 1 
ATOM   668  N N   . LYS   A 1 93  ? 2.49727   -13.37321 -35.90092 1.000 17.07755  ? 100 LYS   A N   1 
ATOM   669  C CA  . LYS   A 1 93  ? 3.61907   -14.29370 -35.72450 1.000 17.64934  ? 100 LYS   A CA  1 
ATOM   670  C C   . LYS   A 1 93  ? 4.87171   -13.54658 -35.29296 1.000 17.42781  ? 100 LYS   A C   1 
ATOM   671  O O   . LYS   A 1 93  ? 5.58481   -13.99175 -34.38555 1.000 15.40246  ? 100 LYS   A O   1 
ATOM   672  C CB  . LYS   A 1 93  ? 3.89410   -15.07322 -37.01314 1.000 19.71401  ? 100 LYS   A CB  1 
ATOM   673  C CG  . LYS   A 1 93  ? 4.89364   -16.22697 -36.81642 1.000 19.45804  ? 100 LYS   A CG  1 
ATOM   674  C CD  . LYS   A 1 93  ? 5.18476   -16.90513 -38.15005 1.000 20.93686  ? 100 LYS   A CD  1 
ATOM   675  C CE  . LYS   A 1 93  ? 6.05547   -18.13807 -37.96198 1.000 26.98747  ? 100 LYS   A CE  1 
ATOM   676  N NZ  . LYS   A 1 93  ? 6.81321   -18.41616 -39.21552 1.000 27.56118  ? 100 LYS   A NZ  1 
ATOM   677  N N   . ALA   A 1 94  ? 5.15087   -12.40698 -35.93648 1.000 17.42207  ? 101 ALA   A N   1 
ATOM   678  C CA  . ALA   A 1 94  ? 6.32550   -11.61306 -35.58571 1.000 22.63844  ? 101 ALA   A CA  1 
ATOM   679  C C   . ALA   A 1 94  ? 6.26726   -11.15857 -34.13368 1.000 20.57180  ? 101 ALA   A C   1 
ATOM   680  O O   . ALA   A 1 94  ? 7.27572   -11.21902 -33.41777 1.000 22.36197  ? 101 ALA   A O   1 
ATOM   681  C CB  . ALA   A 1 94  ? 6.44690   -10.40742 -36.51913 1.000 23.30933  ? 101 ALA   A CB  1 
ATOM   682  N N   . ASP   A 1 95  ? 5.09239   -10.69001 -33.68639 1.000 16.87037  ? 102 ASP   A N   1 
ATOM   683  C CA  . ASP   A 1 95  ? 4.88498   -10.34456 -32.27790 1.000 20.55204  ? 102 ASP   A CA  1 
ATOM   684  C C   . ASP   A 1 95  ? 5.21171   -11.51003 -31.34828 1.000 16.84205  ? 102 ASP   A C   1 
ATOM   685  O O   . ASP   A 1 95  ? 5.89822   -11.33066 -30.33156 1.000 17.47920  ? 102 ASP   A O   1 
ATOM   686  C CB  . ASP   A 1 95  ? 3.42955   -9.90971  -32.03610 1.000 23.96766  ? 102 ASP   A CB  1 
ATOM   687  C CG  . ASP   A 1 95  ? 3.09910   -8.54467  -32.59599 1.000 30.84952  ? 102 ASP   A CG  1 
ATOM   688  O OD1 . ASP   A 1 95  ? 4.02659   -7.72269  -32.78702 1.000 31.45572  ? 102 ASP   A OD1 1 
ATOM   689  O OD2 . ASP   A 1 95  ? 1.88129   -8.29159  -32.83338 1.000 28.77167  ? 102 ASP   A OD2 1 
ATOM   690  N N   . LEU   A 1 96  ? 4.67569   -12.70390 -31.63421 1.000 17.40922  ? 103 LEU   A N   1 
ATOM   691  C CA  . LEU   A 1 96  ? 4.95300   -13.85477 -30.77680 1.000 16.83665  ? 103 LEU   A CA  1 
ATOM   692  C C   . LEU   A 1 96  ? 6.44533   -14.09493 -30.64165 1.000 18.56767  ? 103 LEU   A C   1 
ATOM   693  O O   . LEU   A 1 96  ? 6.96308   -14.28568 -29.53242 1.000 16.88100  ? 103 LEU   A O   1 
ATOM   694  C CB  . LEU   A 1 96  ? 4.31649   -15.12923 -31.32813 1.000 18.77756  ? 103 LEU   A CB  1 
ATOM   695  C CG  . LEU   A 1 96  ? 2.83922   -15.36521 -31.12430 1.000 19.61844  ? 103 LEU   A CG  1 
ATOM   696  C CD1 . LEU   A 1 96  ? 2.47924   -16.67204 -31.83622 1.000 16.89470  ? 103 LEU   A CD1 1 
ATOM   697  C CD2 . LEU   A 1 96  ? 2.50700   -15.41284 -29.62282 1.000 15.58275  ? 103 LEU   A CD2 1 
ATOM   698  N N   . ILE   A 1 97  ? 7.15061   -14.13139 -31.77446 1.000 17.42979  ? 104 ILE   A N   1 
ATOM   699  C CA  . ILE   A 1 97  ? 8.58050   -14.43265 -31.74188 1.000 17.49354  ? 104 ILE   A CA  1 
ATOM   700  C C   . ILE   A 1 97  ? 9.33073   -13.34790 -30.98142 1.000 19.16053  ? 104 ILE   A C   1 
ATOM   701  O O   . ILE   A 1 97  ? 10.27003  -13.62658 -30.22541 1.000 22.36351  ? 104 ILE   A O   1 
ATOM   702  C CB  . ILE   A 1 97  ? 9.11092   -14.59518 -33.17794 1.000 16.05017  ? 104 ILE   A CB  1 
ATOM   703  C CG1 . ILE   A 1 97  ? 8.46959   -15.81995 -33.82937 1.000 16.95657  ? 104 ILE   A CG1 1 
ATOM   704  C CG2 . ILE   A 1 97  ? 10.64886  -14.68470 -33.18874 1.000 17.64678  ? 104 ILE   A CG2 1 
ATOM   705  C CD1 . ILE   A 1 97  ? 8.63705   -15.84354 -35.35981 1.000 20.92420  ? 104 ILE   A CD1 1 
ATOM   706  N N   . ASN   A 1 98  ? 8.91566   -12.09778 -31.15554 1.000 15.61265  ? 105 ASN   A N   1 
ATOM   707  C CA  . ASN   A 1 98  ? 9.52696   -10.95396 -30.48651 1.000 18.02271  ? 105 ASN   A CA  1 
ATOM   708  C C   . ASN   A 1 98  ? 8.95972   -10.79339 -29.06699 1.000 17.10855  ? 105 ASN   A C   1 
ATOM   709  O O   . ASN   A 1 98  ? 8.36600   -9.77776  -28.69734 1.000 19.13990  ? 105 ASN   A O   1 
ATOM   710  C CB  . ASN   A 1 98  ? 9.31229   -9.71216  -31.34281 1.000 20.52101  ? 105 ASN   A CB  1 
ATOM   711  C CG  . ASN   A 1 98  ? 10.19372  -8.56311  -30.93637 1.000 35.35857  ? 105 ASN   A CG  1 
ATOM   712  O OD1 . ASN   A 1 98  ? 11.17681  -8.72905  -30.19582 1.000 40.83554  ? 105 ASN   A OD1 1 
ATOM   713  N ND2 . ASN   A 1 98  ? 9.84064   -7.37521  -31.40579 1.000 31.76016  ? 105 ASN   A ND2 1 
ATOM   714  N N   . ASN   A 1 99  ? 9.13464   -11.85826 -28.27906 1.000 15.75673  ? 106 ASN   A N   1 
ATOM   715  C CA  . ASN   A 1 99  ? 8.80683   -11.88061 -26.85361 1.000 14.69700  ? 106 ASN   A CA  1 
ATOM   716  C C   . ASN   A 1 99  ? 7.36376   -11.48134 -26.56618 1.000 15.82050  ? 106 ASN   A C   1 
ATOM   717  O O   . ASN   A 1 99  ? 7.07810   -10.72602 -25.63462 1.000 14.95354  ? 106 ASN   A O   1 
ATOM   718  C CB  . ASN   A 1 99  ? 9.79165   -11.01695 -26.06794 1.000 15.86181  ? 106 ASN   A CB  1 
ATOM   719  C CG  . ASN   A 1 99  ? 11.20828  -11.50099 -26.24205 1.000 17.39756  ? 106 ASN   A CG  1 
ATOM   720  O OD1 . ASN   A 1 99  ? 11.47826  -12.68393 -26.04584 1.000 17.01568  ? 106 ASN   A OD1 1 
ATOM   721  N ND2 . ASN   A 1 99  ? 12.12554  -10.59484 -26.58567 1.000 19.98471  ? 106 ASN   A ND2 1 
ATOM   722  N N   . LEU   A 1 100 ? 6.44285   -12.06972 -27.33165 1.000 13.54313  ? 107 LEU   A N   1 
ATOM   723  C CA  . LEU   A 1 100 ? 5.00090   -11.89784 -27.12137 1.000 16.41214  ? 107 LEU   A CA  1 
ATOM   724  C C   . LEU   A 1 100 ? 4.62700   -10.41963 -27.00857 1.000 18.58490  ? 107 LEU   A C   1 
ATOM   725  O O   . LEU   A 1 100 ? 3.88290   -9.99629  -26.12011 1.000 17.37715  ? 107 LEU   A O   1 
ATOM   726  C CB  . LEU   A 1 100 ? 4.53111   -12.70763 -25.90136 1.000 13.26828  ? 107 LEU   A CB  1 
ATOM   727  C CG  . LEU   A 1 100 ? 4.86478   -14.21125 -26.03188 1.000 15.64634  ? 107 LEU   A CG  1 
ATOM   728  C CD1 . LEU   A 1 100 ? 6.05268   -14.61296 -25.14630 1.000 19.72819  ? 107 LEU   A CD1 1 
ATOM   729  C CD2 . LEU   A 1 100 ? 3.67846   -15.07928 -25.72827 1.000 28.72953  ? 107 LEU   A CD2 1 
ATOM   730  N N   . GLY   A 1 101 ? 5.14343   -9.62233  -27.94621 1.000 18.28084  ? 108 GLY   A N   1 
ATOM   731  C CA  . GLY   A 1 101 ? 4.76038   -8.22492  -28.00555 1.000 19.89526  ? 108 GLY   A CA  1 
ATOM   732  C C   . GLY   A 1 101 ? 5.31534   -7.32843  -26.91676 1.000 21.89135  ? 108 GLY   A C   1 
ATOM   733  O O   . GLY   A 1 101 ? 4.80599   -6.21474  -26.72207 1.000 24.07934  ? 108 GLY   A O   1 
ATOM   734  N N   . THR   A 1 102 ? 6.34044   -7.76964  -26.19445 1.000 16.20994  ? 109 THR   A N   1 
ATOM   735  C CA  . THR   A 1 102 ? 6.91923   -7.01159  -25.09080 1.000 17.49631  ? 109 THR   A CA  1 
ATOM   736  C C   . THR   A 1 102 ? 8.30324   -6.49704  -25.46993 1.000 17.17627  ? 109 THR   A C   1 
ATOM   737  O O   . THR   A 1 102 ? 8.94053   -7.00009  -26.40075 1.000 20.83646  ? 109 THR   A O   1 
ATOM   738  C CB  . THR   A 1 102 ? 7.01111   -7.87551  -23.82303 1.000 16.69903  ? 109 THR   A CB  1 
ATOM   739  O OG1 . THR   A 1 102 ? 8.07195   -8.83471  -23.97495 1.000 19.83782  ? 109 THR   A OG1 1 
ATOM   740  C CG2 . THR   A 1 102 ? 5.70618   -8.61644  -23.57347 1.000 22.49074  ? 109 THR   A CG2 1 
ATOM   741  N N   . ILE   A 1 103 ? 8.76041   -5.47155  -24.75216 1.000 16.26229  ? 110 ILE   A N   1 
ATOM   742  C CA  . ILE   A 1 103 ? 10.15411  -5.05035  -24.86330 1.000 15.79701  ? 110 ILE   A CA  1 
ATOM   743  C C   . ILE   A 1 103 ? 10.94025  -5.77135  -23.76527 1.000 20.01298  ? 110 ILE   A C   1 
ATOM   744  O O   . ILE   A 1 103 ? 11.49057  -5.15078  -22.84241 1.000 16.30252  ? 110 ILE   A O   1 
ATOM   745  C CB  . ILE   A 1 103 ? 10.29551  -3.51628  -24.81096 1.000 25.45367  ? 110 ILE   A CB  1 
ATOM   746  C CG1 . ILE   A 1 103 ? 9.65124   -2.90137  -23.56474 1.000 25.88248  ? 110 ILE   A CG1 1 
ATOM   747  C CG2 . ILE   A 1 103 ? 9.68303   -2.88061  -26.07124 1.000 21.92941  ? 110 ILE   A CG2 1 
ATOM   748  C CD1 . ILE   A 1 103 ? 10.14328  -1.47129  -23.32377 1.000 27.81314  ? 110 ILE   A CD1 1 
ATOM   749  N N   . ALA   A 1 104 ? 11.00747  -7.10201  -23.87500 1.000 19.75659  ? 111 ALA   A N   1 
ATOM   750  C CA  . ALA   A 1 104 ? 11.40878  -7.91447  -22.73437 1.000 19.76889  ? 111 ALA   A CA  1 
ATOM   751  C C   . ALA   A 1 104 ? 12.88671  -7.76052  -22.40110 1.000 17.63033  ? 111 ALA   A C   1 
ATOM   752  O O   . ALA   A 1 104 ? 13.27031  -7.94685  -21.24162 1.000 18.24392  ? 111 ALA   A O   1 
ATOM   753  C CB  . ALA   A 1 104 ? 11.05705  -9.39066  -22.98870 1.000 20.73567  ? 111 ALA   A CB  1 
ATOM   754  N N   . LYS   A 1 105 ? 13.73116  -7.40591  -23.37219 1.000 18.39347  ? 112 LYS   A N   1 
ATOM   755  C CA  . LYS   A 1 105 ? 15.14503  -7.25421  -23.05284 1.000 22.60510  ? 112 LYS   A CA  1 
ATOM   756  C C   . LYS   A 1 105 ? 15.36592  -6.07594  -22.10842 1.000 28.89990  ? 112 LYS   A C   1 
ATOM   757  O O   . LYS   A 1 105 ? 15.95697  -6.23307  -21.03553 1.000 23.72544  ? 112 LYS   A O   1 
ATOM   758  C CB  . LYS   A 1 105 ? 15.97618  -7.10320  -24.32662 1.000 19.79750  ? 112 LYS   A CB  1 
ATOM   759  C CG  . LYS   A 1 105 ? 17.46925  -7.00370  -24.07681 1.000 33.09241  ? 112 LYS   A CG  1 
ATOM   760  C CD  . LYS   A 1 105 ? 18.25936  -7.19780  -25.36982 1.000 32.90416  ? 112 LYS   A CD  1 
ATOM   761  C CE  . LYS   A 1 105 ? 19.49876  -6.31154  -25.38557 1.000 54.18061  ? 112 LYS   A CE  1 
ATOM   762  N NZ  . LYS   A 1 105 ? 20.33358  -6.48154  -24.17155 1.000 50.92391  ? 112 LYS   A NZ  1 
ATOM   763  N N   . SER   A 1 106 ? 14.86401  -4.89379  -22.46551 1.000 20.89389  ? 113 SER   A N   1 
ATOM   764  C CA  . SER   A 1 106 ? 15.06019  -3.75245  -21.58080 1.000 24.12149  ? 113 SER   A CA  1 
ATOM   765  C C   . SER   A 1 106 ? 14.21609  -3.88131  -20.31350 1.000 24.23352  ? 113 SER   A C   1 
ATOM   766  O O   . SER   A 1 106 ? 14.62550  -3.40164  -19.25121 1.000 25.03681  ? 113 SER   A O   1 
ATOM   767  C CB  . SER   A 1 106 ? 14.75384  -2.44946  -22.32609 1.000 31.63556  ? 113 SER   A CB  1 
ATOM   768  O OG  . SER   A 1 106 ? 13.41351  -2.42121  -22.79383 1.000 26.86632  ? 113 SER   A OG  1 
ATOM   769  N N   . GLY   A 1 107 ? 13.05236  -4.52871  -20.39344 1.000 21.28455  ? 114 GLY   A N   1 
ATOM   770  C CA  . GLY   A 1 107 ? 12.24286  -4.71204  -19.19116 1.000 19.87235  ? 114 GLY   A CA  1 
ATOM   771  C C   . GLY   A 1 107 ? 12.89920  -5.63780  -18.18573 1.000 27.13582  ? 114 GLY   A C   1 
ATOM   772  O O   . GLY   A 1 107 ? 12.87146  -5.38158  -16.97653 1.000 21.42704  ? 114 GLY   A O   1 
ATOM   773  N N   . THR   A 1 108 ? 13.50852  -6.72372  -18.66914 1.000 18.86052  ? 115 THR   A N   1 
ATOM   774  C CA  . THR   A 1 108 ? 14.23710  -7.61708  -17.76827 1.000 21.25549  ? 115 THR   A CA  1 
ATOM   775  C C   . THR   A 1 108 ? 15.38972  -6.89316  -17.09773 1.000 26.97454  ? 115 THR   A C   1 
ATOM   776  O O   . THR   A 1 108 ? 15.59925  -7.03175  -15.88773 1.000 26.83875  ? 115 THR   A O   1 
ATOM   777  C CB  . THR   A 1 108 ? 14.74999  -8.82995  -18.54347 1.000 19.97755  ? 115 THR   A CB  1 
ATOM   778  O OG1 . THR   A 1 108 ? 13.62520  -9.55333  -19.04724 1.000 21.95543  ? 115 THR   A OG1 1 
ATOM   779  C CG2 . THR   A 1 108 ? 15.54557  -9.74596  -17.64128 1.000 24.04183  ? 115 THR   A CG2 1 
ATOM   780  N N   . LYS   A 1 109 ? 16.14697  -6.11507  -17.87202 1.000 24.55297  ? 116 LYS   A N   1 
ATOM   781  C CA  . LYS   A 1 109 ? 17.25376  -5.34532  -17.31373 1.000 27.39258  ? 116 LYS   A CA  1 
ATOM   782  C C   . LYS   A 1 109 ? 16.78638  -4.49659  -16.13825 1.000 30.64041  ? 116 LYS   A C   1 
ATOM   783  O O   . LYS   A 1 109 ? 17.35667  -4.55775  -15.04525 1.000 31.16599  ? 116 LYS   A O   1 
ATOM   784  C CB  . LYS   A 1 109 ? 17.87616  -4.47734  -18.40694 1.000 29.68271  ? 116 LYS   A CB  1 
ATOM   785  C CG  . LYS   A 1 109 ? 18.88303  -3.42825  -17.91884 1.000 43.39891  ? 116 LYS   A CG  1 
ATOM   786  C CD  . LYS   A 1 109 ? 19.53208  -2.72980  -19.11438 1.000 37.81650  ? 116 LYS   A CD  1 
ATOM   787  C CE  . LYS   A 1 109 ? 20.71119  -1.85172  -18.71542 1.000 48.09501  ? 116 LYS   A CE  1 
ATOM   788  N NZ  . LYS   A 1 109 ? 21.58206  -2.51499  -17.71682 1.000 60.67021  ? 116 LYS   A NZ  1 
ATOM   789  N N   . ALA   A 1 110 ? 15.72732  -3.71424  -16.34215 1.000 27.57127  ? 117 ALA   A N   1 
ATOM   790  C CA  . ALA   A 1 110 ? 15.22413  -2.86201  -15.27088 1.000 31.23656  ? 117 ALA   A CA  1 
ATOM   791  C C   . ALA   A 1 110 ? 14.71848  -3.68970  -14.09373 1.000 29.10789  ? 117 ALA   A C   1 
ATOM   792  O O   . ALA   A 1 110 ? 14.97130  -3.35094  -12.93136 1.000 27.70677  ? 117 ALA   A O   1 
ATOM   793  C CB  . ALA   A 1 110 ? 14.11706  -1.95515  -15.80850 1.000 26.97505  ? 117 ALA   A CB  1 
ATOM   794  N N   . PHE   A 1 111 ? 13.98843  -4.77018  -14.37403 1.000 26.47992  ? 118 PHE   A N   1 
ATOM   795  C CA  . PHE   A 1 111 ? 13.42484  -5.58388  -13.29946 1.000 22.47764  ? 118 PHE   A CA  1 
ATOM   796  C C   . PHE   A 1 111 ? 14.52579  -6.13519  -12.39810 1.000 26.24362  ? 118 PHE   A C   1 
ATOM   797  O O   . PHE   A 1 111 ? 14.42796  -6.06747  -11.17021 1.000 26.34439  ? 118 PHE   A O   1 
ATOM   798  C CB  . PHE   A 1 111 ? 12.58089  -6.70102  -13.92187 1.000 18.82097  ? 118 PHE   A CB  1 
ATOM   799  C CG  . PHE   A 1 111 ? 11.88431  -7.60412  -12.93892 1.000 20.85283  ? 118 PHE   A CG  1 
ATOM   800  C CD1 . PHE   A 1 111 ? 11.23312  -7.09572  -11.80929 1.000 21.81627  ? 118 PHE   A CD1 1 
ATOM   801  C CD2 . PHE   A 1 111 ? 11.78206  -8.96820  -13.19986 1.000 23.65064  ? 118 PHE   A CD2 1 
ATOM   802  C CE1 . PHE   A 1 111 ? 10.55204  -7.94231  -10.93048 1.000 20.59705  ? 118 PHE   A CE1 1 
ATOM   803  C CE2 . PHE   A 1 111 ? 11.08896  -9.80921  -12.32572 1.000 20.73940  ? 118 PHE   A CE2 1 
ATOM   804  C CZ  . PHE   A 1 111 ? 10.48167  -9.28796  -11.18515 1.000 23.99612  ? 118 PHE   A CZ  1 
ATOM   805  N N   . MET   A 1 112 ? 15.61044  -6.63523  -12.98479 1.000 31.10025  ? 119 MET   A N   1 
ATOM   806  C CA  . MET   A 1 112 ? 16.63110  -7.27545  -12.15958 1.000 43.75351  ? 119 MET   A CA  1 
ATOM   807  C C   . MET   A 1 112 ? 17.44821  -6.25877  -11.37247 1.000 42.98510  ? 119 MET   A C   1 
ATOM   808  O O   . MET   A 1 112 ? 17.93562  -6.56604  -10.27400 1.000 37.49014  ? 119 MET   A O   1 
ATOM   809  C CB  . MET   A 1 112 ? 17.51096  -8.14839  -13.04008 1.000 43.54636  ? 119 MET   A CB  1 
ATOM   810  C CG  . MET   A 1 112 ? 16.85214  -9.48097  -13.32156 1.000 23.68109  ? 119 MET   A CG  1 
ATOM   811  S SD  . MET   A 1 112 ? 18.02226  -10.47085 -14.23637 1.000 67.08548  ? 119 MET   A SD  1 
ATOM   812  C CE  . MET   A 1 112 ? 17.01889  -11.87372 -14.68644 1.000 29.90598  ? 119 MET   A CE  1 
ATOM   813  N N   . GLU   A 1 113 ? 17.59544  -5.04624  -11.90127 1.000 30.92993  ? 120 GLU   A N   1 
ATOM   814  C CA  . GLU   A 1 113 ? 18.18633  -3.97921  -11.10951 1.000 40.45808  ? 120 GLU   A CA  1 
ATOM   815  C C   . GLU   A 1 113 ? 17.28202  -3.62351  -9.94053  1.000 40.91601  ? 120 GLU   A C   1 
ATOM   816  O O   . GLU   A 1 113 ? 17.75841  -3.39318  -8.82052  1.000 39.35897  ? 120 GLU   A O   1 
ATOM   817  C CB  . GLU   A 1 113 ? 18.44282  -2.76046  -11.99238 1.000 40.82128  ? 120 GLU   A CB  1 
ATOM   818  C CG  . GLU   A 1 113 ? 19.41932  -3.04798  -13.12114 1.000 55.49422  ? 120 GLU   A CG  1 
ATOM   819  C CD  . GLU   A 1 113 ? 19.77002  -1.82681  -13.94547 1.000 65.51161  ? 120 GLU   A CD  1 
ATOM   820  O OE1 . GLU   A 1 113 ? 20.96790  -1.65702  -14.26374 1.000 77.94172  ? 120 GLU   A OE1 1 
ATOM   821  O OE2 . GLU   A 1 113 ? 18.85369  -1.04353  -14.27849 1.000 69.61664  ? 120 GLU   A OE2 1 
ATOM   822  N N   . ALA   A 1 114 ? 15.97042  -3.59731  -10.17979 1.000 31.76703  ? 121 ALA   A N   1 
ATOM   823  C CA  . ALA   A 1 114 ? 15.02921  -3.28688  -9.11192  1.000 27.35019  ? 121 ALA   A CA  1 
ATOM   824  C C   . ALA   A 1 114 ? 15.05771  -4.35365  -8.02841  1.000 31.21305  ? 121 ALA   A C   1 
ATOM   825  O O   . ALA   A 1 114 ? 14.95428  -4.03878  -6.83863  1.000 38.44512  ? 121 ALA   A O   1 
ATOM   826  C CB  . ALA   A 1 114 ? 13.62060  -3.13221  -9.68418  1.000 26.23870  ? 121 ALA   A CB  1 
ATOM   827  N N   . LEU   A 1 115 ? 15.21289  -5.62160  -8.42093  1.000 31.51048  ? 122 LEU   A N   1 
ATOM   828  C CA  . LEU   A 1 115 ? 15.18332  -6.70675  -7.44515  1.000 32.22457  ? 122 LEU   A CA  1 
ATOM   829  C C   . LEU   A 1 115 ? 16.38120  -6.64127  -6.50879  1.000 48.78463  ? 122 LEU   A C   1 
ATOM   830  O O   . LEU   A 1 115 ? 16.24427  -6.83544  -5.29354  1.000 40.16534  ? 122 LEU   A O   1 
ATOM   831  C CB  . LEU   A 1 115 ? 15.14908  -8.04894  -8.16174  1.000 29.93149  ? 122 LEU   A CB  1 
ATOM   832  C CG  . LEU   A 1 115 ? 13.81820  -8.35900  -8.84454  1.000 23.33084  ? 122 LEU   A CG  1 
ATOM   833  C CD1 . LEU   A 1 115 ? 13.98103  -9.62637  -9.64042  1.000 29.78761  ? 122 LEU   A CD1 1 
ATOM   834  C CD2 . LEU   A 1 115 ? 12.67964  -8.45567  -7.81583  1.000 25.71705  ? 122 LEU   A CD2 1 
ATOM   835  N N   . GLN   A 1 116 ? 17.56533  -6.37354  -7.05222  1.000 44.43104  ? 123 GLN   A N   1 
ATOM   836  C CA  . GLN   A 1 116 ? 18.72257  -6.20026  -6.18811  1.000 51.32827  ? 123 GLN   A CA  1 
ATOM   837  C C   . GLN   A 1 116 ? 18.64670  -4.92032  -5.36483  1.000 51.24823  ? 123 GLN   A C   1 
ATOM   838  O O   . GLN   A 1 116 ? 19.41293  -4.77648  -4.40684  1.000 67.33230  ? 123 GLN   A O   1 
ATOM   839  C CB  . GLN   A 1 116 ? 20.00086  -6.22510  -7.02455  1.000 58.95565  ? 123 GLN   A CB  1 
ATOM   840  C CG  . GLN   A 1 116 ? 20.35233  -7.61614  -7.54212  1.000 63.03381  ? 123 GLN   A CG  1 
ATOM   841  C CD  . GLN   A 1 116 ? 21.82701  -7.95529  -7.37168  1.000 91.47357  ? 123 GLN   A CD  1 
ATOM   842  O OE1 . GLN   A 1 116 ? 22.69656  -7.09160  -7.50276  1.000 101.25480 ? 123 GLN   A OE1 1 
ATOM   843  N NE2 . GLN   A 1 116 ? 22.11331  -9.22186  -7.07873  1.000 84.05910  ? 123 GLN   A NE2 1 
ATOM   844  N N   . ALA   A 1 117 ? 17.72924  -4.00850  -5.69581  1.000 54.30033  ? 124 ALA   A N   1 
ATOM   845  C CA  . ALA   A 1 117 ? 17.57965  -2.72834  -5.01431  1.000 50.83970  ? 124 ALA   A CA  1 
ATOM   846  C C   . ALA   A 1 117 ? 16.28474  -2.64126  -4.20253  1.000 72.77340  ? 124 ALA   A C   1 
ATOM   847  O O   . ALA   A 1 117 ? 15.73684  -1.55015  -4.01779  1.000 60.76625  ? 124 ALA   A O   1 
ATOM   848  C CB  . ALA   A 1 117 ? 17.64673  -1.58531  -6.02511  1.000 51.55507  ? 124 ALA   A CB  1 
ATOM   849  N N   . GLY   A 1 118 ? 15.76618  -3.78005  -3.73010  1.000 56.13659  ? 125 GLY   A N   1 
ATOM   850  C CA  . GLY   A 1 118 ? 14.68502  -3.81214  -2.75809  1.000 53.75055  ? 125 GLY   A CA  1 
ATOM   851  C C   . GLY   A 1 118 ? 13.40574  -4.46393  -3.25332  1.000 50.95606  ? 125 GLY   A C   1 
ATOM   852  O O   . GLY   A 1 118 ? 12.65290  -5.01453  -2.44481  1.000 42.85403  ? 125 GLY   A O   1 
ATOM   853  N N   . ALA   A 1 119 ? 13.14880  -4.40984  -4.56319  1.000 35.11473  ? 126 ALA   A N   1 
ATOM   854  C CA  . ALA   A 1 119 ? 11.88511  -4.87050  -5.13388  1.000 27.69408  ? 126 ALA   A CA  1 
ATOM   855  C C   . ALA   A 1 119 ? 11.71554  -6.37757  -4.96406  1.000 31.60726  ? 126 ALA   A C   1 
ATOM   856  O O   . ALA   A 1 119 ? 12.65521  -7.11576  -4.66360  1.000 33.93837  ? 126 ALA   A O   1 
ATOM   857  C CB  . ALA   A 1 119 ? 11.81069  -4.52385  -6.62111  1.000 27.97413  ? 126 ALA   A CB  1 
ATOM   858  N N   . ASP   A 1 120 ? 10.48542  -6.83616  -5.18579  1.000 32.70222  ? 127 ASP   A N   1 
ATOM   859  C CA  . ASP   A 1 120 ? 10.17144  -8.25498  -5.17292  1.000 31.24839  ? 127 ASP   A CA  1 
ATOM   860  C C   . ASP   A 1 120 ? 9.45459   -8.62480  -6.45923  1.000 24.55216  ? 127 ASP   A C   1 
ATOM   861  O O   . ASP   A 1 120 ? 9.07760   -7.76104  -7.25499  1.000 25.75655  ? 127 ASP   A O   1 
ATOM   862  C CB  . ASP   A 1 120 ? 9.31980   -8.63663  -3.96279  1.000 33.76821  ? 127 ASP   A CB  1 
ATOM   863  C CG  . ASP   A 1 120 ? 7.96944   -7.95899  -3.97646  1.000 47.04385  ? 127 ASP   A CG  1 
ATOM   864  O OD1 . ASP   A 1 120 ? 7.91774   -6.72896  -3.75565  1.000 45.86394  ? 127 ASP   A OD1 1 
ATOM   865  O OD2 . ASP   A 1 120 ? 6.97315   -8.64221  -4.28508  1.000 42.63079  ? 127 ASP   A OD2 1 
ATOM   866  N N   . ILE   A 1 121 ? 9.25556   -9.93514  -6.64222  1.000 22.98333  ? 128 ILE   A N   1 
ATOM   867  C CA  . ILE   A 1 121 ? 8.76197   -10.46256 -7.91592  1.000 20.52451  ? 128 ILE   A CA  1 
ATOM   868  C C   . ILE   A 1 121 ? 7.36117   -9.96830  -8.22825  1.000 23.25185  ? 128 ILE   A C   1 
ATOM   869  O O   . ILE   A 1 121 ? 6.97941   -9.86140  -9.40588  1.000 24.55589  ? 128 ILE   A O   1 
ATOM   870  C CB  . ILE   A 1 121 ? 8.87175   -12.00400 -7.90015  1.000 23.22323  ? 128 ILE   A CB  1 
ATOM   871  C CG1 . ILE   A 1 121 ? 10.34982  -12.38993 -8.10952  1.000 28.28432  ? 128 ILE   A CG1 1 
ATOM   872  C CG2 . ILE   A 1 121 ? 7.97264   -12.65919 -8.94232  1.000 22.98525  ? 128 ILE   A CG2 1 
ATOM   873  C CD1 . ILE   A 1 121 ? 10.71053  -13.82351 -7.77752  1.000 32.27630  ? 128 ILE   A CD1 1 
ATOM   874  N N   . SER   A 1 122 ? 6.57620   -9.62646  -7.19857  1.000 25.78616  ? 129 SER   A N   1 
ATOM   875  C CA  . SER   A 1 122 ? 5.22414   -9.13440  -7.44986  1.000 28.41333  ? 129 SER   A CA  1 
ATOM   876  C C   . SER   A 1 122 ? 5.20686   -7.83439  -8.25569  1.000 27.53867  ? 129 SER   A C   1 
ATOM   877  O O   . SER   A 1 122 ? 4.16775   -7.49027  -8.82852  1.000 25.88131  ? 129 SER   A O   1 
ATOM   878  C CB  . SER   A 1 122 ? 4.46580   -8.93680  -6.13109  1.000 24.65932  ? 129 SER   A CB  1 
ATOM   879  O OG  . SER   A 1 122 ? 4.83351   -7.72605  -5.51403  1.000 26.64975  ? 129 SER   A OG  1 
ATOM   880  N N   . MET   A 1 123 ? 6.31139   -7.09957  -8.32867  1.000 22.81660  ? 130 MET   A N   1 
ATOM   881  C CA  . MET   A 1 123 ? 6.30337   -5.86147  -9.10212  1.000 19.72192  ? 130 MET   A CA  1 
ATOM   882  C C   . MET   A 1 123 ? 6.68440   -6.06314  -10.56239 1.000 20.25599  ? 130 MET   A C   1 
ATOM   883  O O   . MET   A 1 123 ? 6.86593   -5.07544  -11.28492 1.000 21.60403  ? 130 MET   A O   1 
ATOM   884  C CB  . MET   A 1 123 ? 7.19085   -4.80378  -8.43263  1.000 31.59528  ? 130 MET   A CB  1 
ATOM   885  C CG  . MET   A 1 123 ? 6.97952   -4.75868  -6.91399  1.000 29.54508  ? 130 MET   A CG  1 
ATOM   886  S SD  . MET   A 1 123 ? 8.29404   -4.01212  -5.96293  1.000 37.33676  ? 130 MET   A SD  1 
ATOM   887  C CE  . MET   A 1 123 ? 8.34109   -2.40840  -6.76444  1.000 35.23042  ? 130 MET   A CE  1 
ATOM   888  N N   . ILE   A 1 124 ? 6.71771   -7.31534  -11.02274 1.000 17.30677  ? 131 ILE   A N   1 
ATOM   889  C CA  . ILE   A 1 124 ? 7.17544   -7.63544  -12.38431 1.000 18.48318  ? 131 ILE   A CA  1 
ATOM   890  C C   . ILE   A 1 124 ? 6.39933   -6.86272  -13.45412 1.000 20.45329  ? 131 ILE   A C   1 
ATOM   891  O O   . ILE   A 1 124 ? 6.95647   -6.47709  -14.49389 1.000 17.29363  ? 131 ILE   A O   1 
ATOM   892  C CB  . ILE   A 1 124 ? 7.07518   -9.15555  -12.62072 1.000 18.67110  ? 131 ILE   A CB  1 
ATOM   893  C CG1 . ILE   A 1 124 ? 7.63889   -9.52202  -14.00232 1.000 19.98440  ? 131 ILE   A CG1 1 
ATOM   894  C CG2 . ILE   A 1 124 ? 5.61314   -9.64913  -12.45318 1.000 16.91366  ? 131 ILE   A CG2 1 
ATOM   895  C CD1 . ILE   A 1 124 ? 7.82653   -11.01157 -14.20322 1.000 21.57374  ? 131 ILE   A CD1 1 
ATOM   896  N N   . GLY   A 1 125 ? 5.10195   -6.65022  -13.23521 1.000 21.22777  ? 132 GLY   A N   1 
ATOM   897  C CA  . GLY   A 1 125 ? 4.27969   -5.98305  -14.23016 1.000 19.74001  ? 132 GLY   A CA  1 
ATOM   898  C C   . GLY   A 1 125 ? 4.68394   -4.54479  -14.48534 1.000 23.57068  ? 132 GLY   A C   1 
ATOM   899  O O   . GLY   A 1 125 ? 4.44565   -4.02829  -15.58141 1.000 23.73314  ? 132 GLY   A O   1 
ATOM   900  N N   . GLN   A 1 126 ? 5.30856   -3.89255  -13.50627 1.000 19.36935  ? 133 GLN   A N   1 
ATOM   901  C CA  . GLN   A 1 126 ? 5.78247   -2.53096  -13.71772 1.000 20.58533  ? 133 GLN   A CA  1 
ATOM   902  C C   . GLN   A 1 126 ? 6.91353   -2.45290  -14.72986 1.000 25.89318  ? 133 GLN   A C   1 
ATOM   903  O O   . GLN   A 1 126 ? 7.27592   -1.34767  -15.14619 1.000 24.95832  ? 133 GLN   A O   1 
ATOM   904  C CB  . GLN   A 1 126 ? 6.23172   -1.93573  -12.39209 1.000 24.73031  ? 133 GLN   A CB  1 
ATOM   905  C CG  . GLN   A 1 126 ? 5.11813   -1.93004  -11.37987 1.000 35.60393  ? 133 GLN   A CG  1 
ATOM   906  C CD  . GLN   A 1 126 ? 5.54211   -1.34110  -10.07383 1.000 37.82328  ? 133 GLN   A CD  1 
ATOM   907  O OE1 . GLN   A 1 126 ? 6.25272   -0.33352  -10.03802 1.000 39.71919  ? 133 GLN   A OE1 1 
ATOM   908  N NE2 . GLN   A 1 126 ? 5.09646   -1.95081  -8.97967  1.000 42.92677  ? 133 GLN   A NE2 1 
ATOM   909  N N   . PHE   A 1 127 ? 7.48220   -3.58777  -15.11909 1.000 23.99949  ? 134 PHE   A N   1 
ATOM   910  C CA  . PHE   A 1 127 ? 8.60228   -3.62572  -16.05040 1.000 20.65210  ? 134 PHE   A CA  1 
ATOM   911  C C   . PHE   A 1 127 ? 8.19595   -4.25948  -17.37587 1.000 22.67356  ? 134 PHE   A C   1 
ATOM   912  O O   . PHE   A 1 127 ? 9.05956   -4.57170  -18.20402 1.000 22.52279  ? 134 PHE   A O   1 
ATOM   913  C CB  . PHE   A 1 127 ? 9.77111   -4.37683  -15.40185 1.000 19.66858  ? 134 PHE   A CB  1 
ATOM   914  C CG  . PHE   A 1 127 ? 10.19361  -3.79270  -14.08571 1.000 19.06017  ? 134 PHE   A CG  1 
ATOM   915  C CD1 . PHE   A 1 127 ? 11.04199  -2.69478  -14.02720 1.000 32.92990  ? 134 PHE   A CD1 1 
ATOM   916  C CD2 . PHE   A 1 127 ? 9.66926   -4.29215  -12.90563 1.000 24.51050  ? 134 PHE   A CD2 1 
ATOM   917  C CE1 . PHE   A 1 127 ? 11.40560  -2.14024  -12.79976 1.000 33.52186  ? 134 PHE   A CE1 1 
ATOM   918  C CE2 . PHE   A 1 127 ? 10.01342  -3.75720  -11.68248 1.000 20.61660  ? 134 PHE   A CE2 1 
ATOM   919  C CZ  . PHE   A 1 127 ? 10.88464  -2.67150  -11.62159 1.000 27.77570  ? 134 PHE   A CZ  1 
ATOM   920  N N   . GLY   A 1 128 ? 6.89600   -4.48151  -17.58272 1.000 18.55009  ? 135 GLY   A N   1 
ATOM   921  C CA  . GLY   A 1 128 ? 6.41137   -4.87116  -18.88627 1.000 18.55589  ? 135 GLY   A CA  1 
ATOM   922  C C   . GLY   A 1 128 ? 6.65960   -6.30965  -19.26859 1.000 19.58630  ? 135 GLY   A C   1 
ATOM   923  O O   . GLY   A 1 128 ? 6.50474   -6.64374  -20.44015 1.000 20.50944  ? 135 GLY   A O   1 
ATOM   924  N N   . VAL   A 1 129 ? 7.03388   -7.17344  -18.31862 1.000 16.57414  ? 136 VAL   A N   1 
ATOM   925  C CA  . VAL   A 1 129 ? 7.32953   -8.58327  -18.60041 1.000 13.84127  ? 136 VAL   A CA  1 
ATOM   926  C C   . VAL   A 1 129 ? 6.47948   -9.48508  -17.70427 1.000 17.10273  ? 136 VAL   A C   1 
ATOM   927  O O   . VAL   A 1 129 ? 6.87487   -10.61354 -17.37676 1.000 14.59111  ? 136 VAL   A O   1 
ATOM   928  C CB  . VAL   A 1 129 ? 8.84176   -8.87118  -18.44307 1.000 13.47814  ? 136 VAL   A CB  1 
ATOM   929  C CG1 . VAL   A 1 129 ? 9.64776   -8.20192  -19.55760 1.000 16.84446  ? 136 VAL   A CG1 1 
ATOM   930  C CG2 . VAL   A 1 129 ? 9.36010   -8.34721  -17.09773 1.000 18.42613  ? 136 VAL   A CG2 1 
ATOM   931  N N   . GLY   A 1 130 ? 5.29587   -8.99889  -17.31592 1.000 16.94169  ? 137 GLY   A N   1 
ATOM   932  C CA  . GLY   A 1 130 ? 4.40952   -9.74319  -16.43179 1.000 14.95529  ? 137 GLY   A CA  1 
ATOM   933  C C   . GLY   A 1 130 ? 3.95719   -11.08818 -16.97891 1.000 15.73596  ? 137 GLY   A C   1 
ATOM   934  O O   . GLY   A 1 130 ? 3.60502   -11.97702 -16.19027 1.000 14.09648  ? 137 GLY   A O   1 
ATOM   935  N N   . PHE   A 1 131 ? 3.97446   -11.26691 -18.30580 1.000 11.77158  ? 138 PHE   A N   1 
ATOM   936  C CA  . PHE   A 1 131 ? 3.59198   -12.56139 -18.88113 1.000 11.71986  ? 138 PHE   A CA  1 
ATOM   937  C C   . PHE   A 1 131 ? 4.40231   -13.69691 -18.26829 1.000 12.95882  ? 138 PHE   A C   1 
ATOM   938  O O   . PHE   A 1 131 ? 3.86781   -14.77580 -17.97916 1.000 13.77192  ? 138 PHE   A O   1 
ATOM   939  C CB  . PHE   A 1 131 ? 3.78019   -12.55847 -20.40977 1.000 14.79960  ? 138 PHE   A CB  1 
ATOM   940  C CG  . PHE   A 1 131 ? 3.76949   -13.94465 -21.01106 1.000 17.96469  ? 138 PHE   A CG  1 
ATOM   941  C CD1 . PHE   A 1 131 ? 2.55697   -14.62441 -21.18030 1.000 16.61977  ? 138 PHE   A CD1 1 
ATOM   942  C CD2 . PHE   A 1 131 ? 4.95444   -14.59418 -21.34503 1.000 16.23381  ? 138 PHE   A CD2 1 
ATOM   943  C CE1 . PHE   A 1 131 ? 2.52768   -15.92281 -21.70126 1.000 13.25650  ? 138 PHE   A CE1 1 
ATOM   944  C CE2 . PHE   A 1 131 ? 4.93608   -15.89175 -21.85364 1.000 15.12428  ? 138 PHE   A CE2 1 
ATOM   945  C CZ  . PHE   A 1 131 ? 3.72870   -16.55772 -22.03542 1.000 17.44547  ? 138 PHE   A CZ  1 
ATOM   946  N N   . TYR   A 1 132 ? 5.70585   -13.47445 -18.06906 1.000 12.12149  ? 139 TYR   A N   1 
ATOM   947  C CA  . TYR   A 1 132 ? 6.57730   -14.57583 -17.66815 1.000 12.25914  ? 139 TYR   A CA  1 
ATOM   948  C C   . TYR   A 1 132 ? 6.32285   -15.01779 -16.23169 1.000 14.44299  ? 139 TYR   A C   1 
ATOM   949  O O   . TYR   A 1 132 ? 6.79958   -16.08667 -15.84526 1.000 15.19418  ? 139 TYR   A O   1 
ATOM   950  C CB  . TYR   A 1 132 ? 8.04428   -14.18516 -17.87312 1.000 10.36298  ? 139 TYR   A CB  1 
ATOM   951  C CG  . TYR   A 1 132 ? 8.32884   -13.89060 -19.33727 1.000 15.32439  ? 139 TYR   A CG  1 
ATOM   952  C CD1 . TYR   A 1 132 ? 8.60222   -14.92236 -20.23207 1.000 12.83242  ? 139 TYR   A CD1 1 
ATOM   953  C CD2 . TYR   A 1 132 ? 8.25358   -12.58907 -19.83990 1.000 15.57470  ? 139 TYR   A CD2 1 
ATOM   954  C CE1 . TYR   A 1 132 ? 8.83904   -14.66306 -21.60460 1.000 13.49305  ? 139 TYR   A CE1 1 
ATOM   955  C CE2 . TYR   A 1 132 ? 8.48364   -12.32971 -21.19745 1.000 18.46387  ? 139 TYR   A CE2 1 
ATOM   956  C CZ  . TYR   A 1 132 ? 8.77160   -13.36393 -22.06600 1.000 15.34712  ? 139 TYR   A CZ  1 
ATOM   957  O OH  . TYR   A 1 132 ? 9.00451   -13.11128 -23.40578 1.000 15.49240  ? 139 TYR   A OH  1 
ATOM   958  N N   . SER   A 1 133 ? 5.55375   -14.24914 -15.45826 1.000 12.14227  ? 140 SER   A N   1 
ATOM   959  C CA  . SER   A 1 133 ? 5.11280   -14.71659 -14.14607 1.000 14.82616  ? 140 SER   A CA  1 
ATOM   960  C C   . SER   A 1 133 ? 4.22983   -15.95087 -14.24151 1.000 14.81842  ? 140 SER   A C   1 
ATOM   961  O O   . SER   A 1 133 ? 4.00869   -16.60881 -13.21808 1.000 12.81577  ? 140 SER   A O   1 
ATOM   962  C CB  . SER   A 1 133 ? 4.34219   -13.63046 -13.38773 1.000 16.02630  ? 140 SER   A CB  1 
ATOM   963  O OG  . SER   A 1 133 ? 3.05782   -13.41158 -13.93215 1.000 15.74374  ? 140 SER   A OG  1 
ATOM   964  N N   . ALA   A 1 134 ? 3.72787   -16.28246 -15.43878 1.000 13.24726  ? 141 ALA   A N   1 
ATOM   965  C CA  . ALA   A 1 134 ? 3.06817   -17.57943 -15.62987 1.000 14.29707  ? 141 ALA   A CA  1 
ATOM   966  C C   . ALA   A 1 134 ? 3.90051   -18.74154 -15.08677 1.000 11.93623  ? 141 ALA   A C   1 
ATOM   967  O O   . ALA   A 1 134 ? 3.34404   -19.72263 -14.56915 1.000 12.71485  ? 141 ALA   A O   1 
ATOM   968  C CB  . ALA   A 1 134 ? 2.77216   -17.79925 -17.12331 1.000 12.21219  ? 141 ALA   A CB  1 
ATOM   969  N N   . TYR   A 1 135 ? 5.24396   -18.65945 -15.20156 1.000 12.93689  ? 142 TYR   A N   1 
ATOM   970  C CA  . TYR   A 1 135 ? 6.09867   -19.77167 -14.79836 1.000 13.61250  ? 142 TYR   A CA  1 
ATOM   971  C C   . TYR   A 1 135 ? 6.26905   -19.87498 -13.28455 1.000 13.73187  ? 142 TYR   A C   1 
ATOM   972  O O   . TYR   A 1 135 ? 6.95032   -20.78875 -12.81243 1.000 14.43717  ? 142 TYR   A O   1 
ATOM   973  C CB  . TYR   A 1 135 ? 7.46017   -19.67357 -15.51781 1.000 11.80180  ? 142 TYR   A CB  1 
ATOM   974  C CG  . TYR   A 1 135 ? 7.26820   -19.97606 -16.98766 1.000 13.73908  ? 142 TYR   A CG  1 
ATOM   975  C CD1 . TYR   A 1 135 ? 7.25961   -21.28875 -17.45118 1.000 13.37645  ? 142 TYR   A CD1 1 
ATOM   976  C CD2 . TYR   A 1 135 ? 6.98538   -18.95171 -17.89206 1.000 11.35580  ? 142 TYR   A CD2 1 
ATOM   977  C CE1 . TYR   A 1 135 ? 7.03631   -21.57735 -18.81568 1.000 15.48511  ? 142 TYR   A CE1 1 
ATOM   978  C CE2 . TYR   A 1 135 ? 6.75291   -19.21996 -19.24922 1.000 12.68803  ? 142 TYR   A CE2 1 
ATOM   979  C CZ  . TYR   A 1 135 ? 6.77054   -20.52667 -19.69547 1.000 16.02884  ? 142 TYR   A CZ  1 
ATOM   980  O OH  . TYR   A 1 135 ? 6.54408   -20.76373 -21.02060 1.000 13.88286  ? 142 TYR   A OH  1 
ATOM   981  N N   . LEU   A 1 136 ? 5.61745   -18.99683 -12.51602 1.000 17.43224  ? 143 LEU   A N   1 
ATOM   982  C CA  . LEU   A 1 136 ? 5.48502   -19.21644 -11.08193 1.000 14.50258  ? 143 LEU   A CA  1 
ATOM   983  C C   . LEU   A 1 136 ? 4.61629   -20.43159 -10.77802 1.000 16.94909  ? 143 LEU   A C   1 
ATOM   984  O O   . LEU   A 1 136 ? 4.82189   -21.10160 -9.75932  1.000 16.82712  ? 143 LEU   A O   1 
ATOM   985  C CB  . LEU   A 1 136 ? 4.86947   -17.97964 -10.41983 1.000 15.11643  ? 143 LEU   A CB  1 
ATOM   986  C CG  . LEU   A 1 136 ? 5.72362   -16.70847 -10.36422 1.000 13.72021  ? 143 LEU   A CG  1 
ATOM   987  C CD1 . LEU   A 1 136 ? 4.82705   -15.53748 -9.91399  1.000 16.84029  ? 143 LEU   A CD1 1 
ATOM   988  C CD2 . LEU   A 1 136 ? 6.93998   -16.88656 -9.44424  1.000 17.19659  ? 143 LEU   A CD2 1 
ATOM   989  N N   . VAL   A 1 137 ? 3.65027   -20.73462 -11.64903 1.000 14.68440  ? 144 VAL   A N   1 
ATOM   990  C CA  . VAL   A 1 137 ? 2.70147   -21.81404 -11.39415 1.000 15.74769  ? 144 VAL   A CA  1 
ATOM   991  C C   . VAL   A 1 137 ? 2.63728   -22.85158 -12.50189 1.000 17.48085  ? 144 VAL   A C   1 
ATOM   992  O O   . VAL   A 1 137 ? 2.10936   -23.95053 -12.26623 1.000 18.88789  ? 144 VAL   A O   1 
ATOM   993  C CB  . VAL   A 1 137 ? 1.28292   -21.25815 -11.11170 1.000 16.06264  ? 144 VAL   A CB  1 
ATOM   994  C CG1 . VAL   A 1 137 ? 1.28854   -20.39535 -9.83601  1.000 20.15599  ? 144 VAL   A CG1 1 
ATOM   995  C CG2 . VAL   A 1 137 ? 0.74142   -20.45775 -12.30496 1.000 13.48708  ? 144 VAL   A CG2 1 
ATOM   996  N N   . ALA   A 1 138 ? 3.14248   -22.58713 -13.70117 1.000 16.90545  ? 145 ALA   A N   1 
ATOM   997  C CA  . ALA   A 1 138 ? 2.98694   -23.48975 -14.83205 1.000 14.68617  ? 145 ALA   A CA  1 
ATOM   998  C C   . ALA   A 1 138 ? 4.32409   -24.12763 -15.17340 1.000 15.81956  ? 145 ALA   A C   1 
ATOM   999  O O   . ALA   A 1 138 ? 5.35726   -23.44934 -15.18112 1.000 19.77992  ? 145 ALA   A O   1 
ATOM   1000 C CB  . ALA   A 1 138 ? 2.43926   -22.73431 -16.04943 1.000 14.50726  ? 145 ALA   A CB  1 
ATOM   1001 N N   . GLU   A 1 139 ? 4.30960   -25.44035 -15.43464 1.000 14.84820  ? 146 GLU   A N   1 
ATOM   1002 C CA  . GLU   A 1 139 ? 5.50290   -26.07404 -15.99428 1.000 15.38089  ? 146 GLU   A CA  1 
ATOM   1003 C C   . GLU   A 1 139 ? 5.60838   -25.86140 -17.49740 1.000 17.73908  ? 146 GLU   A C   1 
ATOM   1004 O O   . GLU   A 1 139 ? 6.70115   -25.96787 -18.05907 1.000 20.69452  ? 146 GLU   A O   1 
ATOM   1005 C CB  . GLU   A 1 139 ? 5.52915   -27.57538 -15.68911 1.000 18.80476  ? 146 GLU   A CB  1 
ATOM   1006 C CG  . GLU   A 1 139 ? 4.29203   -28.31097 -16.09883 1.000 27.16080  ? 146 GLU   A CG  1 
ATOM   1007 C CD  . GLU   A 1 139 ? 4.26825   -29.73968 -15.57086 1.000 56.61771  ? 146 GLU   A CD  1 
ATOM   1008 O OE1 . GLU   A 1 139 ? 4.95061   -30.00456 -14.55854 1.000 40.29711  ? 146 GLU   A OE1 1 
ATOM   1009 O OE2 . GLU   A 1 139 ? 3.56731   -30.59156 -16.16488 1.000 49.23128  ? 146 GLU   A OE2 1 
ATOM   1010 N N   . LYS   A 1 140 ? 4.49809   -25.57510 -18.15510 1.000 15.52390  ? 147 LYS   A N   1 
ATOM   1011 C CA  . LYS   A 1 140 ? 4.47443   -25.33927 -19.58531 1.000 15.19123  ? 147 LYS   A CA  1 
ATOM   1012 C C   . LYS   A 1 140 ? 3.39321   -24.31036 -19.85176 1.000 14.34459  ? 147 LYS   A C   1 
ATOM   1013 O O   . LYS   A 1 140 ? 2.36405   -24.29412 -19.16795 1.000 15.11078  ? 147 LYS   A O   1 
ATOM   1014 C CB  . LYS   A 1 140 ? 4.19961   -26.63500 -20.35274 1.000 14.36612  ? 147 LYS   A CB  1 
ATOM   1015 C CG  . LYS   A 1 140 ? 4.09511   -26.50344 -21.85247 1.000 15.42087  ? 147 LYS   A CG  1 
ATOM   1016 C CD  . LYS   A 1 140 ? 4.01524   -27.90807 -22.39728 1.000 26.50855  ? 147 LYS   A CD  1 
ATOM   1017 C CE  . LYS   A 1 140 ? 2.81730   -28.14051 -23.25366 1.000 34.38262  ? 147 LYS   A CE  1 
ATOM   1018 N NZ  . LYS   A 1 140 ? 2.50398   -29.60338 -23.25389 1.000 37.26529  ? 147 LYS   A NZ  1 
ATOM   1019 N N   . VAL   A 1 141 ? 3.63950   -23.43197 -20.81202 1.000 11.49345  ? 148 VAL   A N   1 
ATOM   1020 C CA  . VAL   A 1 141 ? 2.63724   -22.43237 -21.19404 1.000 12.00335  ? 148 VAL   A CA  1 
ATOM   1021 C C   . VAL   A 1 141 ? 2.45932   -22.50654 -22.70198 1.000 17.35863  ? 148 VAL   A C   1 
ATOM   1022 O O   . VAL   A 1 141 ? 3.44871   -22.52246 -23.44704 1.000 12.19912  ? 148 VAL   A O   1 
ATOM   1023 C CB  . VAL   A 1 141 ? 3.03777   -21.00702 -20.77097 1.000 13.41864  ? 148 VAL   A CB  1 
ATOM   1024 C CG1 . VAL   A 1 141 ? 1.94697   -19.99527 -21.23172 1.000 12.19129  ? 148 VAL   A CG1 1 
ATOM   1025 C CG2 . VAL   A 1 141 ? 3.27148   -20.92095 -19.24515 1.000 11.36278  ? 148 VAL   A CG2 1 
ATOM   1026 N N   . THR   A 1 142 ? 1.20073   -22.57644 -23.14327 1.000 13.36285  ? 149 THR   A N   1 
ATOM   1027 C CA  . THR   A 1 142 ? 0.82266   -22.53114 -24.54850 1.000 13.44165  ? 149 THR   A CA  1 
ATOM   1028 C C   . THR   A 1 142 ? 0.05599   -21.23413 -24.79504 1.000 15.08627  ? 149 THR   A C   1 
ATOM   1029 O O   . THR   A 1 142 ? -0.85899  -20.90493 -24.03964 1.000 17.54660  ? 149 THR   A O   1 
ATOM   1030 C CB  . THR   A 1 142 ? -0.04296  -23.73292 -24.93628 1.000 15.30374  ? 149 THR   A CB  1 
ATOM   1031 O OG1 . THR   A 1 142 ? 0.60308   -24.95139 -24.53248 1.000 19.24084  ? 149 THR   A OG1 1 
ATOM   1032 C CG2 . THR   A 1 142 ? -0.25032  -23.75798 -26.45202 1.000 17.84646  ? 149 THR   A CG2 1 
ATOM   1033 N N   . VAL   A 1 143 ? 0.43167   -20.48945 -25.83133 1.000 12.36202  ? 150 VAL   A N   1 
ATOM   1034 C CA  . VAL   A 1 143 ? -0.26792  -19.25198 -26.17400 1.000 13.19135  ? 150 VAL   A CA  1 
ATOM   1035 C C   . VAL   A 1 143 ? -0.83046  -19.41977 -27.57973 1.000 18.13543  ? 150 VAL   A C   1 
ATOM   1036 O O   . VAL   A 1 143 ? -0.06618  -19.60862 -28.53215 1.000 16.14966  ? 150 VAL   A O   1 
ATOM   1037 C CB  . VAL   A 1 143 ? 0.65571   -18.02667 -26.09591 1.000 12.13770  ? 150 VAL   A CB  1 
ATOM   1038 C CG1 . VAL   A 1 143 ? -0.11867  -16.75492 -26.51721 1.000 12.10480  ? 150 VAL   A CG1 1 
ATOM   1039 C CG2 . VAL   A 1 143 ? 1.26326   -17.88268 -24.70067 1.000 15.20615  ? 150 VAL   A CG2 1 
ATOM   1040 N N   . ILE   A 1 144 ? -2.15589  -19.35677 -27.71182 1.000 12.60906  ? 151 ILE   A N   1 
ATOM   1041 C CA  . ILE   A 1 144 ? -2.82412  -19.41058 -29.01030 1.000 13.27055  ? 151 ILE   A CA  1 
ATOM   1042 C C   . ILE   A 1 144 ? -3.32214  -18.01175 -29.30323 1.000 18.63225  ? 151 ILE   A C   1 
ATOM   1043 O O   . ILE   A 1 144 ? -3.96616  -17.39605 -28.44582 1.000 13.87426  ? 151 ILE   A O   1 
ATOM   1044 C CB  . ILE   A 1 144 ? -4.01205  -20.38552 -29.02254 1.000 14.38038  ? 151 ILE   A CB  1 
ATOM   1045 C CG1 . ILE   A 1 144 ? -3.71389  -21.67496 -28.25749 1.000 25.01703  ? 151 ILE   A CG1 1 
ATOM   1046 C CG2 . ILE   A 1 144 ? -4.52630  -20.59084 -30.48363 1.000 17.85724  ? 151 ILE   A CG2 1 
ATOM   1047 C CD1 . ILE   A 1 144 ? -2.82436  -22.59640 -28.97373 1.000 20.91858  ? 151 ILE   A CD1 1 
ATOM   1048 N N   . THR   A 1 145 ? -3.07354  -17.51850 -30.51452 1.000 10.90139  ? 152 THR   A N   1 
ATOM   1049 C CA  . THR   A 1 145 ? -3.38133  -16.11170 -30.76475 1.000 12.68267  ? 152 THR   A CA  1 
ATOM   1050 C C   . THR   A 1 145 ? -3.80204  -15.90493 -32.21151 1.000 16.09768  ? 152 THR   A C   1 
ATOM   1051 O O   . THR   A 1 145 ? -3.36786  -16.62660 -33.11298 1.000 16.15886  ? 152 THR   A O   1 
ATOM   1052 C CB  . THR   A 1 145 ? -2.18408  -15.21019 -30.38446 1.000 15.87167  ? 152 THR   A CB  1 
ATOM   1053 O OG1 . THR   A 1 145 ? -2.61802  -13.85382 -30.22768 1.000 15.57250  ? 152 THR   A OG1 1 
ATOM   1054 C CG2 . THR   A 1 145 ? -1.05334  -15.28472 -31.41743 1.000 15.48884  ? 152 THR   A CG2 1 
ATOM   1055 N N   . LYS   A 1 146 ? -4.67558  -14.91519 -32.40704 1.000 13.36206  ? 153 LYS   A N   1 
ATOM   1056 C CA  . LYS   A 1 146 ? -5.18080  -14.52624 -33.72106 1.000 15.84002  ? 153 LYS   A CA  1 
ATOM   1057 C C   . LYS   A 1 146 ? -5.31115  -13.01311 -33.76819 1.000 16.67936  ? 153 LYS   A C   1 
ATOM   1058 O O   . LYS   A 1 146 ? -6.12668  -12.43000 -33.04152 1.000 15.96890  ? 153 LYS   A O   1 
ATOM   1059 C CB  . LYS   A 1 146 ? -6.53529  -15.17243 -34.02152 1.000 14.96591  ? 153 LYS   A CB  1 
ATOM   1060 C CG  . LYS   A 1 146 ? -7.15446  -14.72819 -35.37641 1.000 17.86021  ? 153 LYS   A CG  1 
ATOM   1061 C CD  . LYS   A 1 146 ? -6.42902  -15.32772 -36.58009 1.000 19.78891  ? 153 LYS   A CD  1 
ATOM   1062 C CE  . LYS   A 1 146 ? -7.10669  -14.94889 -37.91085 1.000 16.88180  ? 153 LYS   A CE  1 
ATOM   1063 N NZ  . LYS   A 1 146 ? -7.08327  -13.49848 -38.23525 1.000 15.41278  ? 153 LYS   A NZ  1 
ATOM   1064 N N   . HIS   A 1 147 ? -4.53552  -12.38983 -34.64370 1.000 14.58014  ? 154 HIS   A N   1 
ATOM   1065 C CA  . HIS   A 1 147 ? -4.57987  -10.95566 -34.89157 1.000 14.96681  ? 154 HIS   A CA  1 
ATOM   1066 C C   . HIS   A 1 147 ? -5.25935  -10.74638 -36.24310 1.000 20.27861  ? 154 HIS   A C   1 
ATOM   1067 O O   . HIS   A 1 147 ? -5.15908  -11.60140 -37.12857 1.000 18.71999  ? 154 HIS   A O   1 
ATOM   1068 C CB  . HIS   A 1 147 ? -3.13690  -10.39966 -34.87002 1.000 14.26651  ? 154 HIS   A CB  1 
ATOM   1069 C CG  . HIS   A 1 147 ? -3.02192  -8.91014  -35.01252 1.000 15.98695  ? 154 HIS   A CG  1 
ATOM   1070 N ND1 . HIS   A 1 147 ? -3.21441  -8.26179  -36.21377 1.000 17.56302  ? 154 HIS   A ND1 1 
ATOM   1071 C CD2 . HIS   A 1 147 ? -2.63577  -7.95845  -34.12960 1.000 17.06442  ? 154 HIS   A CD2 1 
ATOM   1072 C CE1 . HIS   A 1 147 ? -3.01760  -6.96644  -36.04805 1.000 20.77784  ? 154 HIS   A CE1 1 
ATOM   1073 N NE2 . HIS   A 1 147 ? -2.65999  -6.75620  -34.79226 1.000 20.72544  ? 154 HIS   A NE2 1 
ATOM   1074 N N   . ASN   A 1 148 ? -5.98775  -9.62905  -36.40085 1.000 16.38801  ? 155 ASN   A N   1 
ATOM   1075 C CA  . ASN   A 1 148 ? -6.68520  -9.39320  -37.67023 1.000 18.89410  ? 155 ASN   A CA  1 
ATOM   1076 C C   . ASN   A 1 148 ? -5.76334  -9.47984  -38.88518 1.000 18.90626  ? 155 ASN   A C   1 
ATOM   1077 O O   . ASN   A 1 148 ? -6.22275  -9.83013  -39.98777 1.000 20.15902  ? 155 ASN   A O   1 
ATOM   1078 C CB  . ASN   A 1 148 ? -7.36971  -8.02164  -37.68232 1.000 19.23812  ? 155 ASN   A CB  1 
ATOM   1079 C CG  . ASN   A 1 148 ? -8.61783  -7.98864  -36.84820 1.000 19.79911  ? 155 ASN   A CG  1 
ATOM   1080 O OD1 . ASN   A 1 148 ? -9.27965  -9.01498  -36.67079 1.000 24.03959  ? 155 ASN   A OD1 1 
ATOM   1081 N ND2 . ASN   A 1 148 ? -8.96872  -6.80355  -36.33592 1.000 22.87908  ? 155 ASN   A ND2 1 
ATOM   1082 N N   . ASP   A 1 149 ? -4.48886  -9.12076  -38.72781 1.000 19.96855  ? 156 ASP   A N   1 
ATOM   1083 C CA  . ASP   A 1 149 ? -3.56046  -9.03614  -39.85403 1.000 21.73021  ? 156 ASP   A CA  1 
ATOM   1084 C C   . ASP   A 1 149 ? -2.73962  -10.30685 -40.08109 1.000 27.75237  ? 156 ASP   A C   1 
ATOM   1085 O O   . ASP   A 1 149 ? -1.84685  -10.29478 -40.94190 1.000 24.20581  ? 156 ASP   A O   1 
ATOM   1086 C CB  . ASP   A 1 149 ? -2.59118  -7.85643  -39.66583 1.000 21.98770  ? 156 ASP   A CB  1 
ATOM   1087 C CG  . ASP   A 1 149 ? -3.28839  -6.50799  -39.67197 1.000 30.63562  ? 156 ASP   A CG  1 
ATOM   1088 O OD1 . ASP   A 1 149 ? -4.44097  -6.42473  -40.13811 1.000 25.04869  ? 156 ASP   A OD1 1 
ATOM   1089 O OD2 . ASP   A 1 149 ? -2.67356  -5.53168  -39.19012 1.000 31.69444  ? 156 ASP   A OD2 1 
ATOM   1090 N N   . ASP   A 1 150 ? -2.99136  -11.39589 -39.34632 1.000 19.25616  ? 157 ASP   A N   1 
ATOM   1091 C CA  . ASP   A 1 150 ? -2.19896  -12.62084 -39.51423 1.000 16.66827  ? 157 ASP   A CA  1 
ATOM   1092 C C   . ASP   A 1 150 ? -3.09797  -13.84543 -39.31468 1.000 24.70280  ? 157 ASP   A C   1 
ATOM   1093 O O   . ASP   A 1 150 ? -4.30631  -13.73420 -39.07671 1.000 22.29268  ? 157 ASP   A O   1 
ATOM   1094 C CB  . ASP   A 1 150 ? -1.00189  -12.63014 -38.54257 1.000 18.97588  ? 157 ASP   A CB  1 
ATOM   1095 C CG  . ASP   A 1 150 ? 0.19599   -13.40914 -39.07269 1.000 24.03052  ? 157 ASP   A CG  1 
ATOM   1096 O OD1 . ASP   A 1 150 ? 0.03461   -14.21464 -40.01797 1.000 23.95266  ? 157 ASP   A OD1 1 
ATOM   1097 O OD2 . ASP   A 1 150 ? 1.31045   -13.21297 -38.52711 1.000 26.60011  ? 157 ASP   A OD2 1 
ATOM   1098 N N   . GLU   A 1 151 ? -2.50094  -15.02729 -39.43671 1.000 23.48851  ? 158 GLU   A N   1 
ATOM   1099 C CA  . GLU   A 1 151 ? -3.18093  -16.29331 -39.21515 1.000 19.22314  ? 158 GLU   A CA  1 
ATOM   1100 C C   . GLU   A 1 151 ? -3.09305  -16.68323 -37.73356 1.000 14.84956  ? 158 GLU   A C   1 
ATOM   1101 O O   . GLU   A 1 151 ? -2.40819  -16.04072 -36.93521 1.000 17.66346  ? 158 GLU   A O   1 
ATOM   1102 C CB  . GLU   A 1 151 ? -2.56645  -17.38685 -40.09662 1.000 22.79850  ? 158 GLU   A CB  1 
ATOM   1103 C CG  . GLU   A 1 151 ? -2.84781  -17.25719 -41.61272 1.000 37.43519  ? 158 GLU   A CG  1 
ATOM   1104 C CD  . GLU   A 1 151 ? -4.23061  -16.69308 -41.94996 1.000 61.53845  ? 158 GLU   A CD  1 
ATOM   1105 O OE1 . GLU   A 1 151 ? -5.24932  -17.21801 -41.44385 1.000 65.04607  ? 158 GLU   A OE1 1 
ATOM   1106 O OE2 . GLU   A 1 151 ? -4.30036  -15.73278 -42.75017 1.000 68.53381  ? 158 GLU   A OE2 1 
ATOM   1107 N N   . GLN   A 1 152 ? -3.78142  -17.76627 -37.37511 1.000 19.23976  ? 159 GLN   A N   1 
ATOM   1108 C CA  . GLN   A 1 152 ? -3.77347  -18.25357 -35.99560 1.000 17.27880  ? 159 GLN   A CA  1 
ATOM   1109 C C   . GLN   A 1 152 ? -2.52823  -19.08795 -35.71089 1.000 18.62455  ? 159 GLN   A C   1 
ATOM   1110 O O   . GLN   A 1 152 ? -2.22724  -20.04303 -36.43749 1.000 19.73819  ? 159 GLN   A O   1 
ATOM   1111 C CB  . GLN   A 1 152 ? -5.01874  -19.08549 -35.70895 1.000 19.90013  ? 159 GLN   A CB  1 
ATOM   1112 C CG  . GLN   A 1 152 ? -5.23240  -19.39865 -34.22181 1.000 21.04115  ? 159 GLN   A CG  1 
ATOM   1113 C CD  . GLN   A 1 152 ? -6.67263  -19.80650 -33.92283 1.000 24.78064  ? 159 GLN   A CD  1 
ATOM   1114 O OE1 . GLN   A 1 152 ? -7.60580  -19.08748 -34.25785 1.000 25.61048  ? 159 GLN   A OE1 1 
ATOM   1115 N NE2 . GLN   A 1 152 ? -6.85271  -20.96833 -33.30672 1.000 23.85528  ? 159 GLN   A NE2 1 
ATOM   1116 N N   . TYR   A 1 153 ? -1.82592  -18.74100 -34.63508 1.000 14.75729  ? 160 TYR   A N   1 
ATOM   1117 C CA  . TYR   A 1 153 ? -0.55962  -19.36653 -34.28758 1.000 15.61617  ? 160 TYR   A CA  1 
ATOM   1118 C C   . TYR   A 1 153 ? -0.58401  -19.86835 -32.84931 1.000 17.55428  ? 160 TYR   A C   1 
ATOM   1119 O O   . TYR   A 1 153 ? -1.27955  -19.30969 -31.99117 1.000 15.44302  ? 160 TYR   A O   1 
ATOM   1120 C CB  . TYR   A 1 153 ? 0.59946   -18.37366 -34.46750 1.000 12.33072  ? 160 TYR   A CB  1 
ATOM   1121 C CG  . TYR   A 1 153 ? 0.99032   -18.17108 -35.91207 1.000 15.76190  ? 160 TYR   A CG  1 
ATOM   1122 C CD1 . TYR   A 1 153 ? 1.84632   -19.06312 -36.53397 1.000 21.89827  ? 160 TYR   A CD1 1 
ATOM   1123 C CD2 . TYR   A 1 153 ? 0.50936   -17.09791 -36.64856 1.000 23.46881  ? 160 TYR   A CD2 1 
ATOM   1124 C CE1 . TYR   A 1 153 ? 2.21657   -18.90317 -37.86886 1.000 20.75880  ? 160 TYR   A CE1 1 
ATOM   1125 C CE2 . TYR   A 1 153 ? 0.87076   -16.93591 -37.98977 1.000 25.54522  ? 160 TYR   A CE2 1 
ATOM   1126 C CZ  . TYR   A 1 153 ? 1.72310   -17.84271 -38.58055 1.000 32.67647  ? 160 TYR   A CZ  1 
ATOM   1127 O OH  . TYR   A 1 153 ? 2.10496   -17.70522 -39.89046 1.000 36.18929  ? 160 TYR   A OH  1 
ATOM   1128 N N   . ALA   A 1 154 ? 0.22878   -20.89816 -32.58532 1.000 14.06856  ? 161 ALA   A N   1 
ATOM   1129 C CA  . ALA   A 1 154 ? 0.45631   -21.43077 -31.24296 1.000 14.28884  ? 161 ALA   A CA  1 
ATOM   1130 C C   . ALA   A 1 154 ? 1.92954   -21.28922 -30.86793 1.000 16.90191  ? 161 ALA   A C   1 
ATOM   1131 O O   . ALA   A 1 154 ? 2.80642   -21.82784 -31.55905 1.000 14.68916  ? 161 ALA   A O   1 
ATOM   1132 C CB  . ALA   A 1 154 ? 0.04462   -22.90618 -31.14918 1.000 17.85380  ? 161 ALA   A CB  1 
ATOM   1133 N N   . TRP   A 1 155 ? 2.18374   -20.59375 -29.76437 1.000 14.03113  ? 162 TRP   A N   1 
ATOM   1134 C CA  . TRP   A 1 155 ? 3.48914   -20.48686 -29.11790 1.000 15.07848  ? 162 TRP   A CA  1 
ATOM   1135 C C   . TRP   A 1 155 ? 3.51922   -21.44067 -27.93044 1.000 14.80276  ? 162 TRP   A C   1 
ATOM   1136 O O   . TRP   A 1 155 ? 2.49571   -21.64816 -27.26861 1.000 16.15158  ? 162 TRP   A O   1 
ATOM   1137 C CB  . TRP   A 1 155 ? 3.69391   -19.03261 -28.66413 1.000 13.05165  ? 162 TRP   A CB  1 
ATOM   1138 C CG  . TRP   A 1 155 ? 4.94364   -18.65561 -27.90587 1.000 12.93132  ? 162 TRP   A CG  1 
ATOM   1139 C CD1 . TRP   A 1 155 ? 6.00652   -17.93699 -28.40163 1.000 12.78685  ? 162 TRP   A CD1 1 
ATOM   1140 C CD2 . TRP   A 1 155 ? 5.21216   -18.84774 -26.50134 1.000 13.51084  ? 162 TRP   A CD2 1 
ATOM   1141 N NE1 . TRP   A 1 155 ? 6.93211   -17.71738 -27.41190 1.000 14.47173  ? 162 TRP   A NE1 1 
ATOM   1142 C CE2 . TRP   A 1 155 ? 6.47239   -18.26412 -26.23730 1.000 13.50067  ? 162 TRP   A CE2 1 
ATOM   1143 C CE3 . TRP   A 1 155 ? 4.52311   -19.47893 -25.44931 1.000 12.40781  ? 162 TRP   A CE3 1 
ATOM   1144 C CZ2 . TRP   A 1 155 ? 7.06393   -18.29011 -24.97097 1.000 13.84225  ? 162 TRP   A CZ2 1 
ATOM   1145 C CZ3 . TRP   A 1 155 ? 5.12360   -19.50858 -24.18602 1.000 12.41340  ? 162 TRP   A CZ3 1 
ATOM   1146 C CH2 . TRP   A 1 155 ? 6.37911   -18.91182 -23.96411 1.000 13.19440  ? 162 TRP   A CH2 1 
ATOM   1147 N N   . GLU   A 1 156 ? 4.67625   -22.05046 -27.66117 1.000 12.10288  ? 163 GLU   A N   1 
ATOM   1148 C CA  . GLU   A 1 156 ? 4.74589   -22.92607 -26.50060 1.000 12.50094  ? 163 GLU   A CA  1 
ATOM   1149 C C   . GLU   A 1 156 ? 6.15273   -22.96643 -25.92551 1.000 11.82226  ? 163 GLU   A C   1 
ATOM   1150 O O   . GLU   A 1 156 ? 7.13312   -22.99687 -26.67841 1.000 13.72879  ? 163 GLU   A O   1 
ATOM   1151 C CB  . GLU   A 1 156 ? 4.32364   -24.34275 -26.87378 1.000 16.41685  ? 163 GLU   A CB  1 
ATOM   1152 C CG  . GLU   A 1 156 ? 3.98839   -25.23451 -25.70996 1.000 20.84848  ? 163 GLU   A CG  1 
ATOM   1153 C CD  . GLU   A 1 156 ? 3.27102   -26.48779 -26.18225 1.000 35.58702  ? 163 GLU   A CD  1 
ATOM   1154 O OE1 . GLU   A 1 156 ? 3.95144   -27.35460 -26.77974 1.000 29.46595  ? 163 GLU   A OE1 1 
ATOM   1155 O OE2 . GLU   A 1 156 ? 2.04130   -26.61374 -25.95438 1.000 28.10441  ? 163 GLU   A OE2 1 
ATOM   1156 N N   . SER   A 1 157 ? 6.24460   -23.01453 -24.59512 1.000 14.53792  ? 164 SER   A N   1 
ATOM   1157 C CA  . SER   A 1 157 ? 7.54687   -23.18092 -23.95719 1.000 12.82702  ? 164 SER   A CA  1 
ATOM   1158 C C   . SER   A 1 157 ? 7.40654   -23.85427 -22.59835 1.000 12.52628  ? 164 SER   A C   1 
ATOM   1159 O O   . SER   A 1 157 ? 6.50850   -23.52676 -21.80781 1.000 13.72180  ? 164 SER   A O   1 
ATOM   1160 C CB  . SER   A 1 157 ? 8.27842   -21.84807 -23.78812 1.000 12.67654  ? 164 SER   A CB  1 
ATOM   1161 O OG  . SER   A 1 157 ? 9.56416   -22.09294 -23.20886 1.000 13.56596  ? 164 SER   A OG  1 
ATOM   1162 N N   . SER   A 1 158 ? 8.31193   -24.79467 -22.33556 1.000 14.10101  ? 165 SER   A N   1 
ATOM   1163 C CA  . SER   A 1 158 ? 8.51192   -25.33993 -21.00023 1.000 14.99650  ? 165 SER   A CA  1 
ATOM   1164 C C   . SER   A 1 158 ? 9.75248   -24.74259 -20.34778 1.000 16.21467  ? 165 SER   A C   1 
ATOM   1165 O O   . SER   A 1 158 ? 10.37404  -25.37886 -19.48593 1.000 20.66215  ? 165 SER   A O   1 
ATOM   1166 C CB  . SER   A 1 158 ? 8.63310   -26.85997 -21.07089 1.000 21.24247  ? 165 SER   A CB  1 
ATOM   1167 O OG  . SER   A 1 158 ? 7.39868   -27.42735 -21.47229 1.000 21.01447  ? 165 SER   A OG  1 
ATOM   1168 N N   . ALA   A 1 159 ? 10.11929  -23.53041 -20.74899 1.000 15.41136  ? 166 ALA   A N   1 
ATOM   1169 C CA  . ALA   A 1 159 ? 11.37151  -22.87125 -20.32037 1.000 16.49394  ? 166 ALA   A CA  1 
ATOM   1170 C C   . ALA   A 1 159 ? 12.52952  -23.73557 -20.84161 1.000 18.05449  ? 166 ALA   A C   1 
ATOM   1171 O O   . ALA   A 1 159 ? 12.45231  -24.26034 -21.96006 1.000 21.96757  ? 166 ALA   A O   1 
ATOM   1172 C CB  . ALA   A 1 159 ? 11.35536  -22.61714 -18.82290 1.000 18.01740  ? 166 ALA   A CB  1 
ATOM   1173 N N   . GLY   A 1 160 ? 13.63229  -23.87080 -20.11536 1.000 19.54614  ? 167 GLY   A N   1 
ATOM   1174 C CA  . GLY   A 1 160 ? 14.74208  -24.62422 -20.68900 1.000 20.55852  ? 167 GLY   A CA  1 
ATOM   1175 C C   . GLY   A 1 160 ? 15.44983  -23.96762 -21.85858 1.000 22.86286  ? 167 GLY   A C   1 
ATOM   1176 O O   . GLY   A 1 160 ? 16.27277  -24.61595 -22.52584 1.000 21.83629  ? 167 GLY   A O   1 
ATOM   1177 N N   . GLY   A 1 161 ? 15.14988  -22.70693 -22.14239 1.000 15.30559  ? 168 GLY   A N   1 
ATOM   1178 C CA  . GLY   A 1 161 ? 15.91039  -21.92770 -23.09629 1.000 17.67650  ? 168 GLY   A CA  1 
ATOM   1179 C C   . GLY   A 1 161 ? 15.34225  -21.84515 -24.49624 1.000 18.33134  ? 168 GLY   A C   1 
ATOM   1180 O O   . GLY   A 1 161 ? 15.95294  -21.19272 -25.34435 1.000 16.35297  ? 168 GLY   A O   1 
ATOM   1181 N N   . SER   A 1 162 ? 14.19895  -22.47822 -24.77427 1.000 16.10686  ? 169 SER   A N   1 
ATOM   1182 C CA  . SER   A 1 162 ? 13.68046  -22.50785 -26.13460 1.000 12.80461  ? 169 SER   A CA  1 
ATOM   1183 C C   . SER   A 1 162 ? 12.15993  -22.41410 -26.11280 1.000 15.46416  ? 169 SER   A C   1 
ATOM   1184 O O   . SER   A 1 162 ? 11.51503  -22.72640 -25.10940 1.000 14.56079  ? 169 SER   A O   1 
ATOM   1185 C CB  . SER   A 1 162 ? 14.13552  -23.76254 -26.89436 1.000 19.29386  ? 169 SER   A CB  1 
ATOM   1186 O OG  . SER   A 1 162 ? 13.49339  -24.93094 -26.40359 1.000 17.03300  ? 169 SER   A OG  1 
ATOM   1187 N N   . PHE   A 1 163 ? 11.59935  -21.95089 -27.23253 1.000 12.51787  ? 170 PHE   A N   1 
ATOM   1188 C CA  . PHE   A 1 163 ? 10.15218  -21.95306 -27.44188 1.000 12.13983  ? 170 PHE   A CA  1 
ATOM   1189 C C   . PHE   A 1 163 ? 9.87315   -22.42473 -28.86682 1.000 15.40309  ? 170 PHE   A C   1 
ATOM   1190 O O   . PHE   A 1 163 ? 10.75393  -22.42006 -29.72250 1.000 15.97034  ? 170 PHE   A O   1 
ATOM   1191 C CB  . PHE   A 1 163 ? 9.51043   -20.56424 -27.18120 1.000 12.18150  ? 170 PHE   A CB  1 
ATOM   1192 C CG  . PHE   A 1 163 ? 9.99694   -19.45003 -28.09471 1.000 11.20275  ? 170 PHE   A CG  1 
ATOM   1193 C CD1 . PHE   A 1 163 ? 11.12021  -18.69047 -27.76944 1.000 14.36471  ? 170 PHE   A CD1 1 
ATOM   1194 C CD2 . PHE   A 1 163 ? 9.31071   -19.14462 -29.25674 1.000 13.86650  ? 170 PHE   A CD2 1 
ATOM   1195 C CE1 . PHE   A 1 163 ? 11.55982  -17.65257 -28.59325 1.000 13.71935  ? 170 PHE   A CE1 1 
ATOM   1196 C CE2 . PHE   A 1 163 ? 9.73480   -18.12508 -30.08295 1.000 12.06761  ? 170 PHE   A CE2 1 
ATOM   1197 C CZ  . PHE   A 1 163 ? 10.85587  -17.35725 -29.74790 1.000 16.18023  ? 170 PHE   A CZ  1 
ATOM   1198 N N   . THR   A 1 164 ? 8.64224   -22.88084 -29.11339 1.000 12.14717  ? 171 THR   A N   1 
ATOM   1199 C CA  . THR   A 1 164 ? 8.23122   -23.25631 -30.45876 1.000 12.62916  ? 171 THR   A CA  1 
ATOM   1200 C C   . THR   A 1 164 ? 7.08288   -22.38190 -30.92905 1.000 14.92328  ? 171 THR   A C   1 
ATOM   1201 O O   . THR   A 1 164 ? 6.33987   -21.81808 -30.11739 1.000 13.32997  ? 171 THR   A O   1 
ATOM   1202 C CB  . THR   A 1 164 ? 7.81152   -24.73542 -30.54936 1.000 15.83664  ? 171 THR   A CB  1 
ATOM   1203 O OG1 . THR   A 1 164 ? 6.64354   -24.93745 -29.74367 1.000 16.42277  ? 171 THR   A OG1 1 
ATOM   1204 C CG2 . THR   A 1 164 ? 8.94075   -25.68185 -30.12779 1.000 17.10409  ? 171 THR   A CG2 1 
ATOM   1205 N N   . VAL   A 1 165 ? 6.97396   -22.25948 -32.25310 1.000 16.16447  ? 172 VAL   A N   1 
ATOM   1206 C CA  . VAL   A 1 165 ? 5.86700   -21.56628 -32.89669 1.000 15.49911  ? 172 VAL   A CA  1 
ATOM   1207 C C   . VAL   A 1 165 ? 5.39790   -22.42773 -34.05148 1.000 22.96468  ? 172 VAL   A C   1 
ATOM   1208 O O   . VAL   A 1 165 ? 6.21235   -22.92890 -34.84104 1.000 16.77087  ? 172 VAL   A O   1 
ATOM   1209 C CB  . VAL   A 1 165 ? 6.24077   -20.15639 -33.40090 1.000 15.35148  ? 172 VAL   A CB  1 
ATOM   1210 C CG1 . VAL   A 1 165 ? 5.03432   -19.52866 -34.14392 1.000 19.74347  ? 172 VAL   A CG1 1 
ATOM   1211 C CG2 . VAL   A 1 165 ? 6.69697   -19.27207 -32.24461 1.000 14.33050  ? 172 VAL   A CG2 1 
ATOM   1212 N N   . ARG   A 1 166 ? 4.08381   -22.59664 -34.15700 1.000 15.34433  ? 173 ARG   A N   1 
ATOM   1213 C CA  . ARG   A 1 166 ? 3.52722   -23.36850 -35.25743 1.000 15.67466  ? 173 ARG   A CA  1 
ATOM   1214 C C   . ARG   A 1 166 ? 2.18713   -22.76846 -35.63726 1.000 19.69717  ? 173 ARG   A C   1 
ATOM   1215 O O   . ARG   A 1 166 ? 1.53612   -22.09750 -34.83516 1.000 15.98732  ? 173 ARG   A O   1 
ATOM   1216 C CB  . ARG   A 1 166 ? 3.36789   -24.85159 -34.89442 1.000 19.84126  ? 173 ARG   A CB  1 
ATOM   1217 C CG  . ARG   A 1 166 ? 2.25747   -25.13720 -33.88151 1.000 24.01907  ? 173 ARG   A CG  1 
ATOM   1218 C CD  . ARG   A 1 166 ? 2.41214   -26.53265 -33.25625 1.000 28.68572  ? 173 ARG   A CD  1 
ATOM   1219 N NE  . ARG   A 1 166 ? 3.51160   -26.55673 -32.29252 1.000 30.45131  ? 173 ARG   A NE  1 
ATOM   1220 C CZ  . ARG   A 1 166 ? 4.06968   -27.65742 -31.79963 1.000 39.48387  ? 173 ARG   A CZ  1 
ATOM   1221 N NH1 . ARG   A 1 166 ? 3.66795   -28.86326 -32.16756 1.000 32.47111  ? 173 ARG   A NH1 1 
ATOM   1222 N NH2 . ARG   A 1 166 ? 5.06250   -27.54443 -30.91799 1.000 42.88273  ? 173 ARG   A NH2 1 
ATOM   1223 N N   . THR   A 1 167 ? 1.78456   -22.99859 -36.88132 1.000 20.37826  ? 174 THR   A N   1 
ATOM   1224 C CA  . THR   A 1 167 ? 0.41408   -22.67390 -37.24824 1.000 18.25215  ? 174 THR   A CA  1 
ATOM   1225 C C   . THR   A 1 167 ? -0.54284  -23.53320 -36.43333 1.000 23.44036  ? 174 THR   A C   1 
ATOM   1226 O O   . THR   A 1 167 ? -0.32055  -24.73256 -36.25623 1.000 27.54613  ? 174 THR   A O   1 
ATOM   1227 C CB  . THR   A 1 167 ? 0.20771   -22.90191 -38.74564 1.000 28.51895  ? 174 THR   A CB  1 
ATOM   1228 O OG1 . THR   A 1 167 ? 0.97817   -21.93441 -39.47039 1.000 31.56101  ? 174 THR   A OG1 1 
ATOM   1229 C CG2 . THR   A 1 167 ? -1.24201  -22.75143 -39.09758 1.000 39.28047  ? 174 THR   A CG2 1 
ATOM   1230 N N   . ASP   A 1 168 ? -1.60199  -22.91837 -35.91013 1.000 19.17049  ? 175 ASP   A N   1 
ATOM   1231 C CA  . ASP   A 1 168 ? -2.54251  -23.63296 -35.05833 1.000 24.08561  ? 175 ASP   A CA  1 
ATOM   1232 C C   . ASP   A 1 168 ? -3.67365  -24.20644 -35.90408 1.000 36.11603  ? 175 ASP   A C   1 
ATOM   1233 O O   . ASP   A 1 168 ? -4.34951  -23.47064 -36.63040 1.000 32.88449  ? 175 ASP   A O   1 
ATOM   1234 C CB  . ASP   A 1 168 ? -3.09598  -22.70691 -33.97675 1.000 22.67968  ? 175 ASP   A CB  1 
ATOM   1235 C CG  . ASP   A 1 168 ? -3.97301  -23.43689 -32.98400 1.000 33.37029  ? 175 ASP   A CG  1 
ATOM   1236 O OD1 . ASP   A 1 168 ? -3.58412  -24.53085 -32.52618 1.000 43.28328  ? 175 ASP   A OD1 1 
ATOM   1237 O OD2 . ASP   A 1 168 ? -5.06250  -22.92070 -32.67169 1.000 29.81970  ? 175 ASP   A OD2 1 
ATOM   1238 N N   . THR   A 1 169 ? -3.88425  -25.51389 -35.79981 1.000 42.49578  ? 176 THR   A N   1 
ATOM   1239 C CA  . THR   A 1 169 ? -4.98836  -26.18085 -36.47629 1.000 62.08511  ? 176 THR   A CA  1 
ATOM   1240 C C   . THR   A 1 169 ? -6.19077  -26.39023 -35.56869 1.000 53.18497  ? 176 THR   A C   1 
ATOM   1241 O O   . THR   A 1 169 ? -7.20596  -26.92974 -36.02190 1.000 56.06451  ? 176 THR   A O   1 
ATOM   1242 C CB  . THR   A 1 169 ? -4.53250  -27.53158 -37.03936 1.000 59.49907  ? 176 THR   A CB  1 
ATOM   1243 O OG1 . THR   A 1 169 ? -3.69535  -28.19259 -36.07703 1.000 50.45936  ? 176 THR   A OG1 1 
ATOM   1244 C CG2 . THR   A 1 169 ? -3.78556  -27.33821 -38.36015 1.000 40.44543  ? 176 THR   A CG2 1 
ATOM   1245 N N   . GLY   A 1 170 ? -6.10001  -25.97696 -34.30553 1.000 53.10722  ? 177 GLY   A N   1 
ATOM   1246 C CA  . GLY   A 1 170 ? -7.18806  -26.14215 -33.36410 1.000 52.56420  ? 177 GLY   A CA  1 
ATOM   1247 C C   . GLY   A 1 170 ? -8.41036  -25.29980 -33.67014 1.000 36.98510  ? 177 GLY   A C   1 
ATOM   1248 O O   . GLY   A 1 170 ? -8.55715  -24.75426 -34.76883 1.000 35.30489  ? 177 GLY   A O   1 
ATOM   1249 N N   . GLU   A 1 171 ? -9.29843  -25.20099 -32.69510 1.000 45.03089  ? 178 GLU   A N   1 
ATOM   1250 C CA  . GLU   A 1 171 ? -10.52851 -24.43253 -32.83028 1.000 35.70694  ? 178 GLU   A CA  1 
ATOM   1251 C C   . GLU   A 1 171 ? -10.20760 -22.99020 -33.22268 1.000 35.71898  ? 178 GLU   A C   1 
ATOM   1252 O O   . GLU   A 1 171 ? -9.41750  -22.33361 -32.52723 1.000 24.63240  ? 178 GLU   A O   1 
ATOM   1253 C CB  . GLU   A 1 171 ? -11.28336 -24.48337 -31.49693 1.000 37.65088  ? 178 GLU   A CB  1 
ATOM   1254 C CG  . GLU   A 1 171 ? -12.78294 -24.30326 -31.58434 1.000 41.25444  ? 178 GLU   A CG  1 
ATOM   1255 C CD  . GLU   A 1 171 ? -13.45727 -25.26278 -32.55989 1.000 38.26627  ? 178 GLU   A CD  1 
ATOM   1256 O OE1 . GLU   A 1 171 ? -13.30635 -26.49208 -32.41453 1.000 39.92987  ? 178 GLU   A OE1 1 
ATOM   1257 O OE2 . GLU   A 1 171 ? -14.12417 -24.77579 -33.48912 1.000 49.95308  ? 178 GLU   A OE2 1 
ATOM   1258 N N   . PRO   A 1 172 ? -10.75890 -22.47403 -34.32255 1.000 31.99644  ? 179 PRO   A N   1 
ATOM   1259 C CA  . PRO   A 1 172 ? -10.50371 -21.07454 -34.69142 1.000 33.42234  ? 179 PRO   A CA  1 
ATOM   1260 C C   . PRO   A 1 172 ? -11.01686 -20.10677 -33.62866 1.000 40.55874  ? 179 PRO   A C   1 
ATOM   1261 O O   . PRO   A 1 172 ? -12.06974 -20.32192 -33.02781 1.000 40.70993  ? 179 PRO   A O   1 
ATOM   1262 C CB  . PRO   A 1 172 ? -11.27271 -20.92880 -36.00637 1.000 32.91343  ? 179 PRO   A CB  1 
ATOM   1263 C CG  . PRO   A 1 172 ? -11.18331 -22.31337 -36.60475 1.000 43.86381  ? 179 PRO   A CG  1 
ATOM   1264 C CD  . PRO   A 1 172 ? -11.44865 -23.20173 -35.40832 1.000 41.01337  ? 179 PRO   A CD  1 
ATOM   1265 N N   . MET   A 1 173 ? -10.26731 -19.02273 -33.39952 1.000 22.59765  ? 180 MET   A N   1 
ATOM   1266 C CA  . MET   A 1 173 ? -10.60987 -18.09185 -32.32376 1.000 22.99087  ? 180 MET   A CA  1 
ATOM   1267 C C   . MET   A 1 173 ? -11.27908 -16.79958 -32.76723 1.000 31.88397  ? 180 MET   A C   1 
ATOM   1268 O O   . MET   A 1 173 ? -11.81455 -16.08354 -31.91331 1.000 36.51222  ? 180 MET   A O   1 
ATOM   1269 C CB  . MET   A 1 173 ? -9.36748  -17.67612 -31.54613 1.000 28.06755  ? 180 MET   A CB  1 
ATOM   1270 C CG  . MET   A 1 173 ? -8.75559  -18.75500 -30.71512 1.000 50.06146  ? 180 MET   A CG  1 
ATOM   1271 S SD  . MET   A 1 173 ? -7.13962  -18.13562 -30.29174 1.000 43.88897  ? 180 MET   A SD  1 
ATOM   1272 C CE  . MET   A 1 173 ? -7.58546  -16.50233 -29.75105 1.000 30.94740  ? 180 MET   A CE  1 
ATOM   1273 N N   . GLY   A 1 174 ? -11.18525 -16.42726 -34.03100 1.000 24.91158  ? 181 GLY   A N   1 
ATOM   1274 C CA  . GLY   A 1 174 ? -11.77613 -15.16955 -34.44588 1.000 24.88337  ? 181 GLY   A CA  1 
ATOM   1275 C C   . GLY   A 1 174 ? -10.81041 -14.01888 -34.27650 1.000 21.45171  ? 181 GLY   A C   1 
ATOM   1276 O O   . GLY   A 1 174 ? -10.32837 -13.44909 -35.26315 1.000 19.26010  ? 181 GLY   A O   1 
ATOM   1277 N N   . ARG   A 1 175 ? -10.51142 -13.68459 -33.02101 1.000 15.42501  ? 182 ARG   A N   1 
ATOM   1278 C CA  . ARG   A 1 175 ? -9.52057  -12.66771 -32.67959 1.000 14.03549  ? 182 ARG   A CA  1 
ATOM   1279 C C   . ARG   A 1 175 ? -9.23927  -12.74110 -31.18892 1.000 18.29374  ? 182 ARG   A C   1 
ATOM   1280 O O   . ARG   A 1 175 ? -10.16904 -12.88566 -30.39394 1.000 19.12148  ? 182 ARG   A O   1 
ATOM   1281 C CB  . ARG   A 1 175 ? -10.00761 -11.24466 -33.02121 1.000 13.05050  ? 182 ARG   A CB  1 
ATOM   1282 C CG  . ARG   A 1 175 ? -8.89838  -10.16456 -32.86731 1.000 13.81300  ? 182 ARG   A CG  1 
ATOM   1283 C CD  . ARG   A 1 175 ? -9.52827  -8.76066  -32.72870 1.000 13.41419  ? 182 ARG   A CD  1 
ATOM   1284 N NE  . ARG   A 1 175 ? -10.43334 -8.68553  -31.57511 1.000 15.26847  ? 182 ARG   A NE  1 
ATOM   1285 C CZ  . ARG   A 1 175 ? -11.75230 -8.53803  -31.66813 1.000 15.52500  ? 182 ARG   A CZ  1 
ATOM   1286 N NH1 . ARG   A 1 175 ? -12.36392 -8.48236  -32.84482 1.000 16.36044  ? 182 ARG   A NH1 1 
ATOM   1287 N NH2 . ARG   A 1 175 ? -12.48785 -8.47011  -30.55295 1.000 13.74175  ? 182 ARG   A NH2 1 
ATOM   1288 N N   . GLY   A 1 176 ? -7.96513  -12.61350 -30.81718 1.000 14.81685  ? 183 GLY   A N   1 
ATOM   1289 C CA  . GLY   A 1 176 ? -7.63358  -12.51593 -29.40548 1.000 13.84101  ? 183 GLY   A CA  1 
ATOM   1290 C C   . GLY   A 1 176 ? -6.52763  -13.46759 -29.02971 1.000 15.94956  ? 183 GLY   A C   1 
ATOM   1291 O O   . GLY   A 1 176 ? -5.76922  -13.94644 -29.87971 1.000 16.75929  ? 183 GLY   A O   1 
ATOM   1292 N N   . THR   A 1 177 ? -6.41767  -13.74356 -27.73057 1.000 12.64382  ? 184 THR   A N   1 
ATOM   1293 C CA  . THR   A 1 177 ? -5.33555  -14.58610 -27.24289 1.000 14.29123  ? 184 THR   A CA  1 
ATOM   1294 C C   . THR   A 1 177 ? -5.84600  -15.51337 -26.15828 1.000 18.09108  ? 184 THR   A C   1 
ATOM   1295 O O   . THR   A 1 177 ? -6.70309  -15.13345 -25.35166 1.000 14.53284  ? 184 THR   A O   1 
ATOM   1296 C CB  . THR   A 1 177 ? -4.16785  -13.73741 -26.70000 1.000 15.12651  ? 184 THR   A CB  1 
ATOM   1297 O OG1 . THR   A 1 177 ? -3.65030  -12.92849 -27.75565 1.000 16.79253  ? 184 THR   A OG1 1 
ATOM   1298 C CG2 . THR   A 1 177 ? -3.04222  -14.59517 -26.14514 1.000 16.90780  ? 184 THR   A CG2 1 
ATOM   1299 N N   . LYS   A 1 178 ? -5.30922  -16.73251 -26.15700 1.000 11.99132  ? 185 LYS   A N   1 
ATOM   1300 C CA  . LYS   A 1 178 ? -5.58783  -17.75117 -25.15042 1.000 15.82959  ? 185 LYS   A CA  1 
ATOM   1301 C C   . LYS   A 1 178 ? -4.26778  -18.15712 -24.50553 1.000 16.35361  ? 185 LYS   A C   1 
ATOM   1302 O O   . LYS   A 1 178 ? -3.37123  -18.60623 -25.21279 1.000 16.06805  ? 185 LYS   A O   1 
ATOM   1303 C CB  . LYS   A 1 178 ? -6.23901  -18.95472 -25.84480 1.000 20.16509  ? 185 LYS   A CB  1 
ATOM   1304 C CG  . LYS   A 1 178 ? -6.66256  -20.06986 -24.98583 1.000 33.77103  ? 185 LYS   A CG  1 
ATOM   1305 C CD  . LYS   A 1 178 ? -7.41651  -21.13300 -25.77986 1.000 34.16586  ? 185 LYS   A CD  1 
ATOM   1306 C CE  . LYS   A 1 178 ? -8.55791  -20.53060 -26.56683 1.000 46.80154  ? 185 LYS   A CE  1 
ATOM   1307 N NZ  . LYS   A 1 178 ? -8.29007  -20.63144 -28.02388 1.000 57.59135  ? 185 LYS   A NZ  1 
ATOM   1308 N N   . VAL   A 1 179 ? -4.13136  -17.98805 -23.17760 1.000 13.48648  ? 186 VAL   A N   1 
ATOM   1309 C CA  . VAL   A 1 179 ? -2.93512  -18.43752 -22.45290 1.000 11.41355  ? 186 VAL   A CA  1 
ATOM   1310 C C   . VAL   A 1 179 ? -3.33314  -19.69008 -21.68027 1.000 16.12306  ? 186 VAL   A C   1 
ATOM   1311 O O   . VAL   A 1 179 ? -4.20865  -19.63701 -20.80113 1.000 13.54014  ? 186 VAL   A O   1 
ATOM   1312 C CB  . VAL   A 1 179 ? -2.37314  -17.35445 -21.51137 1.000 13.26921  ? 186 VAL   A CB  1 
ATOM   1313 C CG1 . VAL   A 1 179 ? -1.15014  -17.91525 -20.70889 1.000 12.57362  ? 186 VAL   A CG1 1 
ATOM   1314 C CG2 . VAL   A 1 179 ? -1.97230  -16.12892 -22.31190 1.000 15.84833  ? 186 VAL   A CG2 1 
ATOM   1315 N N   . ILE   A 1 180 ? -2.73823  -20.82679 -22.04470 1.000 12.66625  ? 187 ILE   A N   1 
ATOM   1316 C CA  . ILE   A 1 180 ? -3.02345  -22.11099 -21.41620 1.000 12.40145  ? 187 ILE   A CA  1 
ATOM   1317 C C   . ILE   A 1 180 ? -1.89066  -22.41784 -20.45048 1.000 12.08575  ? 187 ILE   A C   1 
ATOM   1318 O O   . ILE   A 1 180 ? -0.74293  -22.58679 -20.87524 1.000 14.84198  ? 187 ILE   A O   1 
ATOM   1319 C CB  . ILE   A 1 180 ? -3.16985  -23.23287 -22.45668 1.000 14.33846  ? 187 ILE   A CB  1 
ATOM   1320 C CG1 . ILE   A 1 180 ? -4.22973  -22.84018 -23.48692 1.000 15.78148  ? 187 ILE   A CG1 1 
ATOM   1321 C CG2 . ILE   A 1 180 ? -3.51425  -24.57073 -21.75548 1.000 16.21994  ? 187 ILE   A CG2 1 
ATOM   1322 C CD1 . ILE   A 1 180 ? -4.17621  -23.67657 -24.75195 1.000 19.28474  ? 187 ILE   A CD1 1 
ATOM   1323 N N   . LEU   A 1 181 ? -2.20283  -22.46862 -19.14770 1.000 12.11821  ? 188 LEU   A N   1 
ATOM   1324 C CA  . LEU   A 1 181 ? -1.21164  -22.76140 -18.11688 1.000 12.31003  ? 188 LEU   A CA  1 
ATOM   1325 C C   . LEU   A 1 181 ? -1.30907  -24.23557 -17.76460 1.000 16.46623  ? 188 LEU   A C   1 
ATOM   1326 O O   . LEU   A 1 181 ? -2.30834  -24.66723 -17.18309 1.000 15.47265  ? 188 LEU   A O   1 
ATOM   1327 C CB  . LEU   A 1 181 ? -1.45098  -21.91095 -16.86820 1.000 11.63197  ? 188 LEU   A CB  1 
ATOM   1328 C CG  . LEU   A 1 181 ? -1.53201  -20.40096 -17.10291 1.000 15.45455  ? 188 LEU   A CG  1 
ATOM   1329 C CD1 . LEU   A 1 181 ? -1.82886  -19.68608 -15.78607 1.000 20.27766  ? 188 LEU   A CD1 1 
ATOM   1330 C CD2 . LEU   A 1 181 ? -0.21976  -19.89376 -17.69117 1.000 15.64742  ? 188 LEU   A CD2 1 
ATOM   1331 N N   . HIS   A 1 182 ? -0.27146  -25.00628 -18.09123 1.000 13.70617  ? 189 HIS   A N   1 
ATOM   1332 C CA  . HIS   A 1 182 ? -0.19687  -26.40526 -17.65989 1.000 17.06546  ? 189 HIS   A CA  1 
ATOM   1333 C C   . HIS   A 1 182 ? 0.43578   -26.39976 -16.27647 1.000 14.75884  ? 189 HIS   A C   1 
ATOM   1334 O O   . HIS   A 1 182 ? 1.64745   -26.21689 -16.13433 1.000 16.44152  ? 189 HIS   A O   1 
ATOM   1335 C CB  . HIS   A 1 182 ? 0.59563   -27.23946 -18.65987 1.000 15.24880  ? 189 HIS   A CB  1 
ATOM   1336 C CG  . HIS   A 1 182 ? 0.12471   -27.07608 -20.07355 1.000 21.09605  ? 189 HIS   A CG  1 
ATOM   1337 N ND1 . HIS   A 1 182 ? -0.68728  -28.00054 -20.69607 1.000 26.25878  ? 189 HIS   A ND1 1 
ATOM   1338 C CD2 . HIS   A 1 182 ? 0.33629   -26.08766 -20.97915 1.000 19.66319  ? 189 HIS   A CD2 1 
ATOM   1339 C CE1 . HIS   A 1 182 ? -0.96050  -27.58674 -21.92264 1.000 22.94156  ? 189 HIS   A CE1 1 
ATOM   1340 N NE2 . HIS   A 1 182 ? -0.34536  -26.43223 -22.12162 1.000 23.33503  ? 189 HIS   A NE2 1 
ATOM   1341 N N   . LEU   A 1 183 ? -0.39071  -26.54990 -15.24829 1.000 15.79917  ? 190 LEU   A N   1 
ATOM   1342 C CA  . LEU   A 1 183 ? 0.03310   -26.20132 -13.89590 1.000 15.99796  ? 190 LEU   A CA  1 
ATOM   1343 C C   . LEU   A 1 183 ? 0.97420   -27.24656 -13.32311 1.000 23.61229  ? 190 LEU   A C   1 
ATOM   1344 O O   . LEU   A 1 183 ? 0.85278   -28.44712 -13.60213 1.000 19.44718  ? 190 LEU   A O   1 
ATOM   1345 C CB  . LEU   A 1 183 ? -1.18460  -26.05754 -12.97518 1.000 15.21523  ? 190 LEU   A CB  1 
ATOM   1346 C CG  . LEU   A 1 183 ? -2.13218  -24.87450 -13.25219 1.000 14.48721  ? 190 LEU   A CG  1 
ATOM   1347 C CD1 . LEU   A 1 183 ? -3.28007  -24.85200 -12.22543 1.000 17.77157  ? 190 LEU   A CD1 1 
ATOM   1348 C CD2 . LEU   A 1 183 ? -1.38944  -23.56622 -13.20691 1.000 17.14613  ? 190 LEU   A CD2 1 
ATOM   1349 N N   . LYS   A 1 184 ? 1.90296   -26.77274 -12.49073 1.000 16.53161  ? 191 LYS   A N   1 
ATOM   1350 C CA  . LYS   A 1 184 ? 2.73112   -27.66040 -11.68328 1.000 19.37144  ? 191 LYS   A CA  1 
ATOM   1351 C C   . LYS   A 1 184 ? 1.85769   -28.48563 -10.74787 1.000 20.38815  ? 191 LYS   A C   1 
ATOM   1352 O O   . LYS   A 1 184 ? 0.77781   -28.05808 -10.33201 1.000 22.40942  ? 191 LYS   A O   1 
ATOM   1353 C CB  . LYS   A 1 184 ? 3.74675   -26.85727 -10.86270 1.000 19.11520  ? 191 LYS   A CB  1 
ATOM   1354 C CG  . LYS   A 1 184 ? 4.79347   -26.09024 -11.69506 1.000 23.48451  ? 191 LYS   A CG  1 
ATOM   1355 C CD  . LYS   A 1 184 ? 5.43461   -24.95553 -10.85604 1.000 30.50339  ? 191 LYS   A CD  1 
ATOM   1356 C CE  . LYS   A 1 184 ? 6.51018   -24.19612 -11.64241 1.000 39.74689  ? 191 LYS   A CE  1 
ATOM   1357 N NZ  . LYS   A 1 184 ? 7.29078   -23.14140 -10.87004 1.000 36.54833  ? 191 LYS   A NZ  1 
ATOM   1358 N N   . GLU   A 1 185 ? 2.35689   -29.67709 -10.40722 1.000 24.96320  ? 192 GLU   A N   1 
ATOM   1359 C CA  . GLU   A 1 185 ? 1.58922   -30.63864 -9.61918  1.000 30.09308  ? 192 GLU   A CA  1 
ATOM   1360 C C   . GLU   A 1 185 ? 1.13745   -30.06535 -8.28182  1.000 26.84267  ? 192 GLU   A C   1 
ATOM   1361 O O   . GLU   A 1 185 ? 0.06421   -30.41733 -7.78484  1.000 30.31720  ? 192 GLU   A O   1 
ATOM   1362 C CB  . GLU   A 1 185 ? 2.42982   -31.89355 -9.38639  1.000 29.52058  ? 192 GLU   A CB  1 
ATOM   1363 C CG  . GLU   A 1 185 ? 1.63883   -33.17596 -9.35054  1.000 51.57196  ? 192 GLU   A CG  1 
ATOM   1364 C CD  . GLU   A 1 185 ? 2.49631   -34.35818 -8.93686  1.000 73.41574  ? 192 GLU   A CD  1 
ATOM   1365 O OE1 . GLU   A 1 185 ? 3.68201   -34.14413 -8.59850  1.000 75.45894  ? 192 GLU   A OE1 1 
ATOM   1366 O OE2 . GLU   A 1 185 ? 1.98087   -35.49648 -8.93807  1.000 72.69696  ? 192 GLU   A OE2 1 
ATOM   1367 N N   . ASP   A 1 186 ? 1.95154   -29.21225 -7.66400  1.000 24.80235  ? 193 ASP   A N   1 
ATOM   1368 C CA  . ASP   A 1 186 ? 1.62938   -28.66933 -6.35235  1.000 27.59954  ? 193 ASP   A CA  1 
ATOM   1369 C C   . ASP   A 1 186 ? 0.94782   -27.30413 -6.41749  1.000 21.21470  ? 193 ASP   A C   1 
ATOM   1370 O O   . ASP   A 1 186 ? 0.80994   -26.64655 -5.38415  1.000 21.79380  ? 193 ASP   A O   1 
ATOM   1371 C CB  . ASP   A 1 186 ? 2.88677   -28.60435 -5.48315  1.000 32.51198  ? 193 ASP   A CB  1 
ATOM   1372 C CG  . ASP   A 1 186 ? 3.96113   -27.69454 -6.05205  1.000 34.21326  ? 193 ASP   A CG  1 
ATOM   1373 O OD1 . ASP   A 1 186 ? 3.84802   -27.25891 -7.21623  1.000 38.60640  ? 193 ASP   A OD1 1 
ATOM   1374 O OD2 . ASP   A 1 186 ? 4.94874   -27.43746 -5.33185  1.000 40.83780  ? 193 ASP   A OD2 1 
ATOM   1375 N N   . GLN   A 1 187 ? 0.48824   -26.88063 -7.59466  1.000 17.10807  ? 194 GLN   A N   1 
ATOM   1376 C CA  . GLN   A 1 187 ? -0.14389  -25.58064 -7.76898  1.000 17.61341  ? 194 GLN   A CA  1 
ATOM   1377 C C   . GLN   A 1 187 ? -1.59577  -25.73138 -8.22226  1.000 17.93750  ? 194 GLN   A C   1 
ATOM   1378 O O   . GLN   A 1 187 ? -2.15234  -24.82971 -8.84981  1.000 20.35055  ? 194 GLN   A O   1 
ATOM   1379 C CB  . GLN   A 1 187 ? 0.65023   -24.72003 -8.75721  1.000 19.30453  ? 194 GLN   A CB  1 
ATOM   1380 C CG  . GLN   A 1 187 ? 2.10253   -24.45523 -8.31775  1.000 18.45274  ? 194 GLN   A CG  1 
ATOM   1381 C CD  . GLN   A 1 187 ? 2.20271   -23.77909 -6.95856  1.000 24.07358  ? 194 GLN   A CD  1 
ATOM   1382 O OE1 . GLN   A 1 187 ? 1.40085   -22.90158 -6.63017  1.000 23.93153  ? 194 GLN   A OE1 1 
ATOM   1383 N NE2 . GLN   A 1 187 ? 3.19777   -24.17473 -6.16657  1.000 22.48700  ? 194 GLN   A NE2 1 
ATOM   1384 N N   . THR   A 1 188 ? -2.23069  -26.85870 -7.91347  1.000 22.35704  ? 195 THR   A N   1 
ATOM   1385 C CA  . THR   A 1 188 ? -3.60339  -27.06099 -8.37980  1.000 20.95441  ? 195 THR   A CA  1 
ATOM   1386 C C   . THR   A 1 188 ? -4.64231  -26.26965 -7.59254  1.000 16.72945  ? 195 THR   A C   1 
ATOM   1387 O O   . THR   A 1 188 ? -5.82933  -26.32918 -7.94020  1.000 22.56552  ? 195 THR   A O   1 
ATOM   1388 C CB  . THR   A 1 188 ? -3.97725  -28.55320 -8.36709  1.000 23.54387  ? 195 THR   A CB  1 
ATOM   1389 O OG1 . THR   A 1 188 ? -3.91408  -29.06851 -7.02834  1.000 27.14685  ? 195 THR   A OG1 1 
ATOM   1390 C CG2 . THR   A 1 188 ? -3.05037  -29.34806 -9.30042  1.000 26.84773  ? 195 THR   A CG2 1 
ATOM   1391 N N   . GLU   A 1 189 ? -4.24712  -25.52116 -6.56094  1.000 18.49673  ? 196 GLU   A N   1 
ATOM   1392 C CA  . GLU   A 1 189 ? -5.20912  -24.62779 -5.91597  1.000 21.10582  ? 196 GLU   A CA  1 
ATOM   1393 C C   . GLU   A 1 189 ? -5.77194  -23.60021 -6.88680  1.000 18.02108  ? 196 GLU   A C   1 
ATOM   1394 O O   . GLU   A 1 189 ? -6.87689  -23.09657 -6.68264  1.000 17.00838  ? 196 GLU   A O   1 
ATOM   1395 C CB  . GLU   A 1 189 ? -4.56620  -23.91965 -4.72475  1.000 18.86291  ? 196 GLU   A CB  1 
ATOM   1396 C CG  . GLU   A 1 189 ? -3.55693  -22.84326 -5.09210  1.000 18.46124  ? 196 GLU   A CG  1 
ATOM   1397 C CD  . GLU   A 1 189 ? -2.78820  -22.36786 -3.87434  1.000 32.18037  ? 196 GLU   A CD  1 
ATOM   1398 O OE1 . GLU   A 1 189 ? -1.86549  -23.10262 -3.45116  1.000 29.18134  ? 196 GLU   A OE1 1 
ATOM   1399 O OE2 . GLU   A 1 189 ? -3.11333  -21.28391 -3.33174  1.000 24.69550  ? 196 GLU   A OE2 1 
ATOM   1400 N N   . TYR   A 1 190 ? -5.02884  -23.25746 -7.92559  1.000 19.96234  ? 197 TYR   A N   1 
ATOM   1401 C CA  . TYR   A 1 190 ? -5.49528  -22.24537 -8.86270  1.000 17.65745  ? 197 TYR   A CA  1 
ATOM   1402 C C   . TYR   A 1 190 ? -6.50678  -22.78997 -9.86182  1.000 19.24379  ? 197 TYR   A C   1 
ATOM   1403 O O   . TYR   A 1 190 ? -6.87898  -22.06556 -10.78947 1.000 20.05874  ? 197 TYR   A O   1 
ATOM   1404 C CB  . TYR   A 1 190 ? -4.29114  -21.59143 -9.56190  1.000 15.54353  ? 197 TYR   A CB  1 
ATOM   1405 C CG  . TYR   A 1 190 ? -3.37742  -20.97309 -8.53700  1.000 14.68082  ? 197 TYR   A CG  1 
ATOM   1406 C CD1 . TYR   A 1 190 ? -3.80182  -19.86890 -7.79841  1.000 20.16032  ? 197 TYR   A CD1 1 
ATOM   1407 C CD2 . TYR   A 1 190 ? -2.12966  -21.52598 -8.24294  1.000 15.84139  ? 197 TYR   A CD2 1 
ATOM   1408 C CE1 . TYR   A 1 190 ? -2.99236  -19.30571 -6.81899  1.000 16.80273  ? 197 TYR   A CE1 1 
ATOM   1409 C CE2 . TYR   A 1 190 ? -1.30799  -20.96253 -7.25127  1.000 18.78092  ? 197 TYR   A CE2 1 
ATOM   1410 C CZ  . TYR   A 1 190 ? -1.75605  -19.84631 -6.55523  1.000 21.06763  ? 197 TYR   A CZ  1 
ATOM   1411 O OH  . TYR   A 1 190 ? -0.98122  -19.28063 -5.56338  1.000 20.58129  ? 197 TYR   A OH  1 
ATOM   1412 N N   . LEU   A 1 191 ? -6.95721  -24.04077 -9.68538  1.000 16.97707  ? 198 LEU   A N   1 
ATOM   1413 C CA  . LEU   A 1 191 ? -8.10132  -24.57908 -10.40552 1.000 19.32921  ? 198 LEU   A CA  1 
ATOM   1414 C C   . LEU   A 1 191 ? -9.37863  -24.56074 -9.57031  1.000 19.21395  ? 198 LEU   A C   1 
ATOM   1415 O O   . LEU   A 1 191 ? -10.44533 -24.92054 -10.08375 1.000 19.16127  ? 198 LEU   A O   1 
ATOM   1416 C CB  . LEU   A 1 191 ? -7.81034  -26.02505 -10.84049 1.000 17.51063  ? 198 LEU   A CB  1 
ATOM   1417 C CG  . LEU   A 1 191 ? -6.59533  -26.21678 -11.74292 1.000 17.35658  ? 198 LEU   A CG  1 
ATOM   1418 C CD1 . LEU   A 1 191 ? -6.37286  -27.70977 -12.04101 1.000 23.51865  ? 198 LEU   A CD1 1 
ATOM   1419 C CD2 . LEU   A 1 191 ? -6.74896  -25.41822 -13.03648 1.000 22.79781  ? 198 LEU   A CD2 1 
ATOM   1420 N N   . GLU   A 1 192 ? -9.29220  -24.21119 -8.28642  1.000 18.87019  ? 199 GLU   A N   1 
ATOM   1421 C CA  . GLU   A 1 192 ? -10.45526 -24.23990 -7.40564  1.000 17.43220  ? 199 GLU   A CA  1 
ATOM   1422 C C   . GLU   A 1 192 ? -11.20448 -22.91929 -7.50860  1.000 22.80086  ? 199 GLU   A C   1 
ATOM   1423 O O   . GLU   A 1 192 ? -10.60227 -21.83709 -7.45394  1.000 19.43053  ? 199 GLU   A O   1 
ATOM   1424 C CB  . GLU   A 1 192 ? -10.05399 -24.52326 -5.95978  1.000 25.67468  ? 199 GLU   A CB  1 
ATOM   1425 C CG  . GLU   A 1 192 ? -9.28926  -25.83184 -5.79634  1.000 30.67219  ? 199 GLU   A CG  1 
ATOM   1426 C CD  . GLU   A 1 192 ? -8.81882  -26.06463 -4.37485  1.000 61.66752  ? 199 GLU   A CD  1 
ATOM   1427 O OE1 . GLU   A 1 192 ? -9.32818  -25.38261 -3.45774  1.000 76.25633  ? 199 GLU   A OE1 1 
ATOM   1428 O OE2 . GLU   A 1 192 ? -7.92815  -26.92172 -4.17813  1.000 67.47928  ? 199 GLU   A OE2 1 
ATOM   1429 N N   . GLU   A 1 193 ? -12.52189 -23.02616 -7.66391  1.000 19.89487  ? 200 GLU   A N   1 
ATOM   1430 C CA  . GLU   A 1 193 ? -13.35212 -21.85752 -7.90984  1.000 18.53549  ? 200 GLU   A CA  1 
ATOM   1431 C C   . GLU   A 1 193 ? -13.17278 -20.80096 -6.81606  1.000 18.04990  ? 200 GLU   A C   1 
ATOM   1432 O O   . GLU   A 1 193 ? -13.02556 -19.60699 -7.11189  1.000 20.35216  ? 200 GLU   A O   1 
ATOM   1433 C CB  . GLU   A 1 193 ? -14.81350 -22.30643 -8.01286  1.000 24.80168  ? 200 GLU   A CB  1 
ATOM   1434 C CG  . GLU   A 1 193 ? -15.78691 -21.17506 -7.95211  1.000 32.94098  ? 200 GLU   A CG  1 
ATOM   1435 C CD  . GLU   A 1 193 ? -17.20667 -21.56424 -8.35285  1.000 59.14081  ? 200 GLU   A CD  1 
ATOM   1436 O OE1 . GLU   A 1 193 ? -17.63231 -22.68483 -8.00598  1.000 42.65124  ? 200 GLU   A OE1 1 
ATOM   1437 O OE2 . GLU   A 1 193 ? -17.90043 -20.74457 -8.99744  1.000 46.45972  ? 200 GLU   A OE2 1 
ATOM   1438 N N   . ARG   A 1 194 ? -13.15960 -21.21127 -5.54618  1.000 20.64495  ? 201 ARG   A N   1 
ATOM   1439 C CA  . ARG   A 1 194 ? -13.14612 -20.18926 -4.50572  1.000 22.41476  ? 201 ARG   A CA  1 
ATOM   1440 C C   . ARG   A 1 194 ? -11.80888 -19.47427 -4.45102  1.000 19.79870  ? 201 ARG   A C   1 
ATOM   1441 O O   . ARG   A 1 194 ? -11.76091 -18.29699 -4.08388  1.000 19.48040  ? 201 ARG   A O   1 
ATOM   1442 C CB  . ARG   A 1 194 ? -13.48123 -20.78919 -3.14540  1.000 23.20765  ? 201 ARG   A CB  1 
ATOM   1443 C CG  . ARG   A 1 194 ? -12.68628 -21.99572 -2.79657  1.000 25.69245  ? 201 ARG   A CG  1 
ATOM   1444 C CD  . ARG   A 1 194 ? -13.08809 -22.44171 -1.39087  1.000 35.59270  ? 201 ARG   A CD  1 
ATOM   1445 N NE  . ARG   A 1 194 ? -12.08816 -23.30457 -0.77892  1.000 42.29049  ? 201 ARG   A NE  1 
ATOM   1446 C CZ  . ARG   A 1 194 ? -12.21731 -23.83171 0.42998   1.000 40.34880  ? 201 ARG   A CZ  1 
ATOM   1447 N NH1 . ARG   A 1 194 ? -13.30563 -23.62808 1.15559   1.000 41.39126  ? 201 ARG   A NH1 1 
ATOM   1448 N NH2 . ARG   A 1 194 ? -11.23577 -24.58606 0.91747   1.000 42.01028  ? 201 ARG   A NH2 1 
ATOM   1449 N N   . ARG   A 1 195 ? -10.72334 -20.17198 -4.81081  1.000 15.96458  ? 202 ARG   A N   1 
ATOM   1450 C CA  . ARG   A 1 195 ? -9.39978  -19.55378 -4.83642  1.000 17.43672  ? 202 ARG   A CA  1 
ATOM   1451 C C   . ARG   A 1 195 ? -9.28815  -18.56587 -5.99162  1.000 15.58023  ? 202 ARG   A C   1 
ATOM   1452 O O   . ARG   A 1 195 ? -8.74834  -17.46509 -5.82558  1.000 15.88662  ? 202 ARG   A O   1 
ATOM   1453 C CB  . ARG   A 1 195 ? -8.32621  -20.64008 -4.95065  1.000 16.95385  ? 202 ARG   A CB  1 
ATOM   1454 C CG  . ARG   A 1 195 ? -6.88168  -20.13405 -4.98867  1.000 14.82822  ? 202 ARG   A CG  1 
ATOM   1455 C CD  . ARG   A 1 195 ? -6.48005  -19.63470 -3.60071  1.000 18.81257  ? 202 ARG   A CD  1 
ATOM   1456 N NE  . ARG   A 1 195 ? -5.05205  -19.37315 -3.53193  1.000 18.05103  ? 202 ARG   A NE  1 
ATOM   1457 C CZ  . ARG   A 1 195 ? -4.49450  -18.18942 -3.31086  1.000 19.15457  ? 202 ARG   A CZ  1 
ATOM   1458 N NH1 . ARG   A 1 195 ? -5.22109  -17.10841 -3.08523  1.000 18.96477  ? 202 ARG   A NH1 1 
ATOM   1459 N NH2 . ARG   A 1 195 ? -3.16915  -18.08720 -3.33361  1.000 19.01450  ? 202 ARG   A NH2 1 
ATOM   1460 N N   . ILE   A 1 196 ? -9.79382  -18.93747 -7.17282  1.000 14.27839  ? 203 ILE   A N   1 
ATOM   1461 C CA  . ILE   A 1 196 ? -9.72594  -18.01468 -8.30610  1.000 15.33226  ? 203 ILE   A CA  1 
ATOM   1462 C C   . ILE   A 1 196 ? -10.57977 -16.78034 -8.04197  1.000 15.84308  ? 203 ILE   A C   1 
ATOM   1463 O O   . ILE   A 1 196 ? -10.12575 -15.65318 -8.28496  1.000 16.40748  ? 203 ILE   A O   1 
ATOM   1464 C CB  . ILE   A 1 196 ? -10.13360 -18.69278 -9.62623  1.000 17.17064  ? 203 ILE   A CB  1 
ATOM   1465 C CG1 . ILE   A 1 196 ? -9.17976  -19.83547 -9.98694  1.000 15.63199  ? 203 ILE   A CG1 1 
ATOM   1466 C CG2 . ILE   A 1 196 ? -10.18358 -17.63203 -10.77623 1.000 15.63630  ? 203 ILE   A CG2 1 
ATOM   1467 C CD1 . ILE   A 1 196 ? -9.79627  -20.83207 -10.99707 1.000 18.08872  ? 203 ILE   A CD1 1 
ATOM   1468 N N   . LYS   A 1 197 ? -11.81240 -16.95527 -7.51305  1.000 16.47292  ? 204 LYS   A N   1 
ATOM   1469 C CA  . LYS   A 1 197 ? -12.62335 -15.77384 -7.20572  1.000 14.65137  ? 204 LYS   A CA  1 
ATOM   1470 C C   . LYS   A 1 197 ? -11.92926 -14.85185 -6.21578  1.000 20.00811  ? 204 LYS   A C   1 
ATOM   1471 O O   . LYS   A 1 197 ? -12.00873 -13.62294 -6.34519  1.000 17.76263  ? 204 LYS   A O   1 
ATOM   1472 C CB  . LYS   A 1 197 ? -14.02053 -16.09495 -6.63144  1.000 18.24804  ? 204 LYS   A CB  1 
ATOM   1473 C CG  . LYS   A 1 197 ? -15.04992 -16.78973 -7.46418  1.000 31.74500  ? 204 LYS   A CG  1 
ATOM   1474 C CD  . LYS   A 1 197 ? -16.09015 -17.40706 -6.51508  1.000 32.80044  ? 204 LYS   A CD  1 
ATOM   1475 C CE  . LYS   A 1 197 ? -17.05435 -18.31618 -7.22060  1.000 47.86793  ? 204 LYS   A CE  1 
ATOM   1476 N NZ  . LYS   A 1 197 ? -18.12061 -18.86740 -6.31400  1.000 54.60575  ? 204 LYS   A NZ  1 
ATOM   1477 N N   . GLU   A 1 198 ? -11.31399 -15.42514 -5.18098  1.000 15.10674  ? 205 GLU   A N   1 
ATOM   1478 C CA  . GLU   A 1 198 ? -10.59429 -14.61626 -4.19851  1.000 16.09867  ? 205 GLU   A CA  1 
ATOM   1479 C C   . GLU   A 1 198 ? -9.51803  -13.76417 -4.85929  1.000 18.14437  ? 205 GLU   A C   1 
ATOM   1480 O O   . GLU   A 1 198 ? -9.35031  -12.57763 -4.52693  1.000 16.26297  ? 205 GLU   A O   1 
ATOM   1481 C CB  . GLU   A 1 198 ? -9.97593  -15.52654 -3.12378  1.000 16.05550  ? 205 GLU   A CB  1 
ATOM   1482 C CG  . GLU   A 1 198 ? -9.05434  -14.82153 -2.11811  1.000 19.97118  ? 205 GLU   A CG  1 
ATOM   1483 C CD  . GLU   A 1 198 ? -8.35624  -15.80346 -1.18284  1.000 23.85700  ? 205 GLU   A CD  1 
ATOM   1484 O OE1 . GLU   A 1 198 ? -7.81096  -16.80391 -1.69037  1.000 22.19569  ? 205 GLU   A OE1 1 
ATOM   1485 O OE2 . GLU   A 1 198 ? -8.35367  -15.58152 0.05018   1.000 21.05832  ? 205 GLU   A OE2 1 
ATOM   1486 N N   . ILE   A 1 199 ? -8.75832  -14.36095 -5.77604  1.000 13.95829  ? 206 ILE   A N   1 
ATOM   1487 C CA  . ILE   A 1 199 ? -7.64589  -13.64606 -6.40190  1.000 15.37102  ? 206 ILE   A CA  1 
ATOM   1488 C C   . ILE   A 1 199 ? -8.16059  -12.55262 -7.31478  1.000 19.03689  ? 206 ILE   A C   1 
ATOM   1489 O O   . ILE   A 1 199 ? -7.62121  -11.44374 -7.32981  1.000 16.35190  ? 206 ILE   A O   1 
ATOM   1490 C CB  . ILE   A 1 199 ? -6.72759  -14.62608 -7.15537  1.000 14.69637  ? 206 ILE   A CB  1 
ATOM   1491 C CG1 . ILE   A 1 199 ? -6.08964  -15.61025 -6.16693  1.000 14.14454  ? 206 ILE   A CG1 1 
ATOM   1492 C CG2 . ILE   A 1 199 ? -5.68092  -13.88434 -7.97640  1.000 18.28327  ? 206 ILE   A CG2 1 
ATOM   1493 C CD1 . ILE   A 1 199 ? -5.53451  -16.84765 -6.84898  1.000 16.91760  ? 206 ILE   A CD1 1 
ATOM   1494 N N   . VAL   A 1 200 ? -9.20730  -12.84295 -8.08999  1.000 15.70157  ? 207 VAL   A N   1 
ATOM   1495 C CA  . VAL   A 1 200 ? -9.78124  -11.82254 -8.96269  1.000 14.40602  ? 207 VAL   A CA  1 
ATOM   1496 C C   . VAL   A 1 200 ? -10.31389 -10.65726 -8.13902  1.000 18.14414  ? 207 VAL   A C   1 
ATOM   1497 O O   . VAL   A 1 200 ? -10.09633 -9.49100  -8.48120  1.000 17.91073  ? 207 VAL   A O   1 
ATOM   1498 C CB  . VAL   A 1 200 ? -10.87102 -12.44644 -9.85488  1.000 16.35413  ? 207 VAL   A CB  1 
ATOM   1499 C CG1 . VAL   A 1 200 ? -11.69297 -11.34827 -10.57346 1.000 15.84055  ? 207 VAL   A CG1 1 
ATOM   1500 C CG2 . VAL   A 1 200 ? -10.22017 -13.42334 -10.87153 1.000 14.40687  ? 207 VAL   A CG2 1 
ATOM   1501 N N   . LYS   A 1 201 ? -10.98898 -10.95023 -7.02495  1.000 15.26331  ? 208 LYS   A N   1 
ATOM   1502 C CA  . LYS   A 1 201 ? -11.52997 -9.86982  -6.19515  1.000 16.03015  ? 208 LYS   A CA  1 
ATOM   1503 C C   . LYS   A 1 201 ? -10.41091 -9.06334  -5.55624  1.000 20.25501  ? 208 LYS   A C   1 
ATOM   1504 O O   . LYS   A 1 201 ? -10.50856 -7.83720  -5.44649  1.000 23.55098  ? 208 LYS   A O   1 
ATOM   1505 C CB  . LYS   A 1 201 ? -12.47492 -10.44304 -5.13683  1.000 19.98788  ? 208 LYS   A CB  1 
ATOM   1506 C CG  . LYS   A 1 201 ? -13.13329 -9.40728  -4.21808  1.000 28.45233  ? 208 LYS   A CG  1 
ATOM   1507 C CD  . LYS   A 1 201 ? -13.93020 -10.09591 -3.12156  1.000 32.93790  ? 208 LYS   A CD  1 
ATOM   1508 C CE  . LYS   A 1 201 ? -14.44768 -9.12780  -2.08591  1.000 39.54886  ? 208 LYS   A CE  1 
ATOM   1509 N NZ  . LYS   A 1 201 ? -15.44521 -9.81726  -1.22369  1.000 51.33531  ? 208 LYS   A NZ  1 
ATOM   1510 N N   . LYS   A 1 202 ? -9.31861  -9.72927  -5.17358  1.000 21.49627  ? 209 LYS   A N   1 
ATOM   1511 C CA  . LYS   A 1 202 ? -8.23630  -9.04503  -4.46909  1.000 23.01265  ? 209 LYS   A CA  1 
ATOM   1512 C C   . LYS   A 1 202 ? -7.43015  -8.13725  -5.39993  1.000 23.73124  ? 209 LYS   A C   1 
ATOM   1513 O O   . LYS   A 1 202 ? -7.07884  -7.00559  -5.02643  1.000 20.34885  ? 209 LYS   A O   1 
ATOM   1514 C CB  . LYS   A 1 202 ? -7.32491  -10.07951 -3.79931  1.000 20.73514  ? 209 LYS   A CB  1 
ATOM   1515 C CG  . LYS   A 1 202 ? -6.02789  -9.49232  -3.23352  1.000 26.12577  ? 209 LYS   A CG  1 
ATOM   1516 C CD  . LYS   A 1 202 ? -5.58072  -10.28649 -2.02573  1.000 37.71211  ? 209 LYS   A CD  1 
ATOM   1517 C CE  . LYS   A 1 202 ? -4.15040  -10.74716 -2.12134  1.000 52.06118  ? 209 LYS   A CE  1 
ATOM   1518 N NZ  . LYS   A 1 202 ? -3.42973  -10.71185 -0.81356  1.000 49.40035  ? 209 LYS   A NZ  1 
ATOM   1519 N N   . HIS   A 1 203 ? -7.14094  -8.60068  -6.61812  1.000 18.44107  ? 210 HIS   A N   1 
ATOM   1520 C CA  . HIS   A 1 203 ? -6.15713  -7.95363  -7.48043  1.000 21.80082  ? 210 HIS   A CA  1 
ATOM   1521 C C   . HIS   A 1 203 ? -6.70068  -7.38677  -8.78440  1.000 23.35816  ? 210 HIS   A C   1 
ATOM   1522 O O   . HIS   A 1 203 ? -5.96871  -6.65307  -9.45586  1.000 23.37721  ? 210 HIS   A O   1 
ATOM   1523 C CB  . HIS   A 1 203 ? -5.03901  -8.94735  -7.84804  1.000 22.25211  ? 210 HIS   A CB  1 
ATOM   1524 C CG  . HIS   A 1 203 ? -4.21145  -9.37825  -6.68433  1.000 21.45390  ? 210 HIS   A CG  1 
ATOM   1525 N ND1 . HIS   A 1 203 ? -3.44789  -8.49748  -5.95018  1.000 26.12389  ? 210 HIS   A ND1 1 
ATOM   1526 C CD2 . HIS   A 1 203 ? -4.04447  -10.59311 -6.10883  1.000 29.27433  ? 210 HIS   A CD2 1 
ATOM   1527 C CE1 . HIS   A 1 203 ? -2.83022  -9.15417  -4.98487  1.000 28.78042  ? 210 HIS   A CE1 1 
ATOM   1528 N NE2 . HIS   A 1 203 ? -3.18050  -10.42610 -5.05528  1.000 28.44781  ? 210 HIS   A NE2 1 
ATOM   1529 N N   . SER   A 1 204 ? -7.93161  -7.71486  -9.18751  1.000 19.72139  ? 211 SER   A N   1 
ATOM   1530 C CA  . SER   A 1 204 ? -8.40840  -7.32945  -10.51317 1.000 19.88381  ? 211 SER   A CA  1 
ATOM   1531 C C   . SER   A 1 204 ? -9.78020  -6.65540  -10.44074 1.000 21.79636  ? 211 SER   A C   1 
ATOM   1532 O O   . SER   A 1 204 ? -10.56719 -6.72766  -11.39357 1.000 21.31530  ? 211 SER   A O   1 
ATOM   1533 C CB  . SER   A 1 204 ? -8.45510  -8.54760  -11.43861 1.000 19.30786  ? 211 SER   A CB  1 
ATOM   1534 O OG  . SER   A 1 204 ? -7.16783  -9.16558  -11.51938 1.000 24.44120  ? 211 SER   A OG  1 
ATOM   1535 N N   . GLN   A 1 205 ? -10.06957 -5.96883  -9.33109  1.000 23.35650  ? 212 GLN   A N   1 
ATOM   1536 C CA  . GLN   A 1 205 ? -11.42909 -5.48279  -9.11687  1.000 27.24121  ? 212 GLN   A CA  1 
ATOM   1537 C C   . GLN   A 1 205 ? -11.79079 -4.29996  -10.01851 1.000 30.41827  ? 212 GLN   A C   1 
ATOM   1538 O O   . GLN   A 1 205 ? -12.98091 -4.03976  -10.22350 1.000 33.43497  ? 212 GLN   A O   1 
ATOM   1539 C CB  . GLN   A 1 205 ? -11.64811 -5.09163  -7.64459  1.000 29.62063  ? 212 GLN   A CB  1 
ATOM   1540 C CG  . GLN   A 1 205 ? -10.76375 -3.98401  -7.07530  1.000 45.60371  ? 212 GLN   A CG  1 
ATOM   1541 C CD  . GLN   A 1 205 ? -9.38549  -4.41044  -6.55110  1.000 57.68905  ? 212 GLN   A CD  1 
ATOM   1542 O OE1 . GLN   A 1 205 ? -8.72335  -5.30108  -7.09460  1.000 34.17767  ? 212 GLN   A OE1 1 
ATOM   1543 N NE2 . GLN   A 1 205 ? -8.95367  -3.75569  -5.46886  1.000 47.48572  ? 212 GLN   A NE2 1 
ATOM   1544 N N   . PHE   A 1 206 ? -10.80919 -3.58497  -10.57279 1.000 23.92586  ? 213 PHE   A N   1 
ATOM   1545 C CA  . PHE   A 1 206 ? -11.07653 -2.44606  -11.44168 1.000 30.58402  ? 213 PHE   A CA  1 
ATOM   1546 C C   . PHE   A 1 206 ? -10.72696 -2.71522  -12.90631 1.000 25.03568  ? 213 PHE   A C   1 
ATOM   1547 O O   . PHE   A 1 206 ? -10.48768 -1.77405  -13.66859 1.000 33.13327  ? 213 PHE   A O   1 
ATOM   1548 C CB  . PHE   A 1 206 ? -10.31590 -1.22712  -10.93332 1.000 29.32980  ? 213 PHE   A CB  1 
ATOM   1549 C CG  . PHE   A 1 206 ? -10.69513 -0.82453  -9.52882  1.000 34.64528  ? 213 PHE   A CG  1 
ATOM   1550 C CD1 . PHE   A 1 206 ? -11.97641 -0.39860  -9.23510  1.000 30.29672  ? 213 PHE   A CD1 1 
ATOM   1551 C CD2 . PHE   A 1 206 ? -9.77052  -0.90212  -8.49998  1.000 35.31633  ? 213 PHE   A CD2 1 
ATOM   1552 C CE1 . PHE   A 1 206 ? -12.32635 -0.02644  -7.94234  1.000 36.35181  ? 213 PHE   A CE1 1 
ATOM   1553 C CE2 . PHE   A 1 206 ? -10.11970 -0.54063  -7.20819  1.000 45.23395  ? 213 PHE   A CE2 1 
ATOM   1554 C CZ  . PHE   A 1 206 ? -11.39921 -0.10341  -6.93383  1.000 35.32368  ? 213 PHE   A CZ  1 
ATOM   1555 N N   . ILE   A 1 207 ? -10.65847 -3.97751  -13.31581 1.000 17.43963  ? 214 ILE   A N   1 
ATOM   1556 C CA  . ILE   A 1 207 ? -10.51118 -4.28898  -14.74143 1.000 16.77893  ? 214 ILE   A CA  1 
ATOM   1557 C C   . ILE   A 1 207 ? -11.82124 -3.98020  -15.46534 1.000 23.73854  ? 214 ILE   A C   1 
ATOM   1558 O O   . ILE   A 1 207 ? -12.89846 -4.42172  -15.04270 1.000 19.80065  ? 214 ILE   A O   1 
ATOM   1559 C CB  . ILE   A 1 207 ? -10.08572 -5.75766  -14.91294 1.000 16.72465  ? 214 ILE   A CB  1 
ATOM   1560 C CG1 . ILE   A 1 207 ? -8.66878  -5.94092  -14.35609 1.000 17.29259  ? 214 ILE   A CG1 1 
ATOM   1561 C CG2 . ILE   A 1 207 ? -10.14562 -6.19600  -16.38457 1.000 15.40883  ? 214 ILE   A CG2 1 
ATOM   1562 C CD1 . ILE   A 1 207 ? -7.60177  -5.11666  -15.08219 1.000 23.46312  ? 214 ILE   A CD1 1 
ATOM   1563 N N   . GLY   A 1 208 ? -11.73779 -3.22489  -16.57065 1.000 17.66965  ? 215 GLY   A N   1 
ATOM   1564 C CA  . GLY   A 1 208 ? -12.92101 -2.67458  -17.21149 1.000 19.04060  ? 215 GLY   A CA  1 
ATOM   1565 C C   . GLY   A 1 208 ? -13.57657 -3.55069  -18.26300 1.000 21.16308  ? 215 GLY   A C   1 
ATOM   1566 O O   . GLY   A 1 208 ? -14.18167 -3.04420  -19.21126 1.000 19.65116  ? 215 GLY   A O   1 
ATOM   1567 N N   . TYR   A 1 209 ? -13.48919 -4.86234  -18.09107 1.000 17.41617  ? 216 TYR   A N   1 
ATOM   1568 C CA  . TYR   A 1 209 ? -14.07106 -5.82503  -19.01217 1.000 18.34614  ? 216 TYR   A CA  1 
ATOM   1569 C C   . TYR   A 1 209 ? -14.66614 -6.94045  -18.17995 1.000 17.68097  ? 216 TYR   A C   1 
ATOM   1570 O O   . TYR   A 1 209 ? -14.15978 -7.24184  -17.08900 1.000 18.80429  ? 216 TYR   A O   1 
ATOM   1571 C CB  . TYR   A 1 209 ? -13.02457 -6.39397  -20.00174 1.000 13.55824  ? 216 TYR   A CB  1 
ATOM   1572 C CG  . TYR   A 1 209 ? -12.40761 -5.32287  -20.86415 1.000 18.04203  ? 216 TYR   A CG  1 
ATOM   1573 C CD1 . TYR   A 1 209 ? -13.04865 -4.88490  -22.02537 1.000 17.28657  ? 216 TYR   A CD1 1 
ATOM   1574 C CD2 . TYR   A 1 209 ? -11.20954 -4.71136  -20.50274 1.000 18.34296  ? 216 TYR   A CD2 1 
ATOM   1575 C CE1 . TYR   A 1 209 ? -12.51867 -3.87131  -22.79742 1.000 17.38849  ? 216 TYR   A CE1 1 
ATOM   1576 C CE2 . TYR   A 1 209 ? -10.65813 -3.67423  -21.28790 1.000 15.63283  ? 216 TYR   A CE2 1 
ATOM   1577 C CZ  . TYR   A 1 209 ? -11.33009 -3.26925  -22.42894 1.000 16.14469  ? 216 TYR   A CZ  1 
ATOM   1578 O OH  . TYR   A 1 209 ? -10.81950 -2.25764  -23.19799 1.000 20.27991  ? 216 TYR   A OH  1 
ATOM   1579 N N   . PRO   A 1 210 ? -15.73587 -7.57699  -18.65333 1.000 17.51206  ? 217 PRO   A N   1 
ATOM   1580 C CA  . PRO   A 1 210 ? -16.31527 -8.69472  -17.89979 1.000 17.39224  ? 217 PRO   A CA  1 
ATOM   1581 C C   . PRO   A 1 210 ? -15.33729 -9.86411  -17.81614 1.000 20.75193  ? 217 PRO   A C   1 
ATOM   1582 O O   . PRO   A 1 210 ? -14.76001 -10.28703 -18.82058 1.000 21.05132  ? 217 PRO   A O   1 
ATOM   1583 C CB  . PRO   A 1 210 ? -17.58231 -9.05253  -18.69829 1.000 19.73143  ? 217 PRO   A CB  1 
ATOM   1584 C CG  . PRO   A 1 210 ? -17.39437 -8.47260  -20.05486 1.000 22.75390  ? 217 PRO   A CG  1 
ATOM   1585 C CD  . PRO   A 1 210 ? -16.49546 -7.25844  -19.88297 1.000 17.84420  ? 217 PRO   A CD  1 
ATOM   1586 N N   . ILE   A 1 211 ? -15.12736 -10.35724 -16.59679 1.000 16.89811  ? 218 ILE   A N   1 
ATOM   1587 C CA  . ILE   A 1 211 ? -14.28720 -11.51984 -16.33054 1.000 12.52008  ? 218 ILE   A CA  1 
ATOM   1588 C C   . ILE   A 1 211 ? -15.20855 -12.63731 -15.88120 1.000 14.98917  ? 218 ILE   A C   1 
ATOM   1589 O O   . ILE   A 1 211 ? -15.86041 -12.52364 -14.83152 1.000 18.97529  ? 218 ILE   A O   1 
ATOM   1590 C CB  . ILE   A 1 211 ? -13.23681 -11.22531 -15.25199 1.000 16.65537  ? 218 ILE   A CB  1 
ATOM   1591 C CG1 . ILE   A 1 211 ? -12.36571 -10.01771 -15.64204 1.000 15.44798  ? 218 ILE   A CG1 1 
ATOM   1592 C CG2 . ILE   A 1 211 ? -12.43357 -12.46339 -14.96373 1.000 15.65968  ? 218 ILE   A CG2 1 
ATOM   1593 C CD1 . ILE   A 1 211 ? -11.46921 -9.53117  -14.47852 1.000 16.20745  ? 218 ILE   A CD1 1 
ATOM   1594 N N   . THR   A 1 212 ? -15.28098 -13.70021 -16.66579 1.000 14.18833  ? 219 THR   A N   1 
ATOM   1595 C CA  . THR   A 1 212 ? -16.22125 -14.78347 -16.39839 1.000 13.93579  ? 219 THR   A CA  1 
ATOM   1596 C C   . THR   A 1 212 ? -15.41787 -16.00028 -15.97988 1.000 12.88652  ? 219 THR   A C   1 
ATOM   1597 O O   . THR   A 1 212 ? -14.57948 -16.48306 -16.74754 1.000 13.90307  ? 219 THR   A O   1 
ATOM   1598 C CB  . THR   A 1 212 ? -17.07038 -15.10187 -17.63249 1.000 17.66984  ? 219 THR   A CB  1 
ATOM   1599 O OG1 . THR   A 1 212 ? -17.83571 -13.94617 -18.00244 1.000 15.35442  ? 219 THR   A OG1 1 
ATOM   1600 C CG2 . THR   A 1 212 ? -18.01683 -16.29719 -17.34272 1.000 17.68115  ? 219 THR   A CG2 1 
ATOM   1601 N N   . LEU   A 1 213 ? -15.66129 -16.47782 -14.76571 1.000 14.32998  ? 220 LEU   A N   1 
ATOM   1602 C CA  . LEU   A 1 213 ? -15.03485 -17.69887 -14.27462 1.000 13.06883  ? 220 LEU   A CA  1 
ATOM   1603 C C   . LEU   A 1 213 ? -15.95476 -18.86998 -14.62097 1.000 13.58276  ? 220 LEU   A C   1 
ATOM   1604 O O   . LEU   A 1 213 ? -17.05097 -18.99092 -14.06012 1.000 16.33783  ? 220 LEU   A O   1 
ATOM   1605 C CB  . LEU   A 1 213 ? -14.81767 -17.61132 -12.76430 1.000 14.20320  ? 220 LEU   A CB  1 
ATOM   1606 C CG  . LEU   A 1 213 ? -14.28551 -18.86302 -12.06489 1.000 18.64720  ? 220 LEU   A CG  1 
ATOM   1607 C CD1 . LEU   A 1 213 ? -13.05078 -19.42452 -12.76984 1.000 15.98506  ? 220 LEU   A CD1 1 
ATOM   1608 C CD2 . LEU   A 1 213 ? -13.93187 -18.46724 -10.62023 1.000 17.30562  ? 220 LEU   A CD2 1 
ATOM   1609 N N   . PHE   A 1 214 ? -15.52263 -19.70764 -15.55951 1.000 15.49464  ? 221 PHE   A N   1 
ATOM   1610 C CA  . PHE   A 1 214 ? -16.28388 -20.89236 -15.93489 1.000 16.49157  ? 221 PHE   A CA  1 
ATOM   1611 C C   . PHE   A 1 214 ? -16.25242 -21.89815 -14.79045 1.000 18.92817  ? 221 PHE   A C   1 
ATOM   1612 O O   . PHE   A 1 214 ? -15.26296 -21.99085 -14.06073 1.000 18.59810  ? 221 PHE   A O   1 
ATOM   1613 C CB  . PHE   A 1 214 ? -15.67192 -21.55588 -17.17636 1.000 13.71718  ? 221 PHE   A CB  1 
ATOM   1614 C CG  . PHE   A 1 214 ? -15.95106 -20.84876 -18.48696 1.000 14.87528  ? 221 PHE   A CG  1 
ATOM   1615 C CD1 . PHE   A 1 214 ? -16.01438 -19.45975 -18.56918 1.000 13.33161  ? 221 PHE   A CD1 1 
ATOM   1616 C CD2 . PHE   A 1 214 ? -16.06488 -21.59707 -19.65422 1.000 15.40832  ? 221 PHE   A CD2 1 
ATOM   1617 C CE1 . PHE   A 1 214 ? -16.21682 -18.82022 -19.76975 1.000 12.90734  ? 221 PHE   A CE1 1 
ATOM   1618 C CE2 . PHE   A 1 214 ? -16.27592 -20.96938 -20.88134 1.000 14.86262  ? 221 PHE   A CE2 1 
ATOM   1619 C CZ  . PHE   A 1 214 ? -16.36672 -19.57194 -20.93857 1.000 17.47385  ? 221 PHE   A CZ  1 
ATOM   1620 N N   . VAL   A 1 215 ? -17.32213 -22.67456 -14.65038 1.000 17.61123  ? 222 VAL   A N   1 
ATOM   1621 C CA  . VAL   A 1 215 ? -17.35874 -23.75375 -13.66318 1.000 18.31708  ? 222 VAL   A CA  1 
ATOM   1622 C C   . VAL   A 1 215 ? -17.20583 -25.09059 -14.38414 1.000 23.78394  ? 222 VAL   A C   1 
ATOM   1623 O O   . VAL   A 1 215 ? -17.29341 -25.17846 -15.60700 1.000 18.76637  ? 222 VAL   A O   1 
ATOM   1624 C CB  . VAL   A 1 215 ? -18.64006 -23.70880 -12.79883 1.000 33.34492  ? 222 VAL   A CB  1 
ATOM   1625 C CG1 . VAL   A 1 215 ? -18.59115 -22.51510 -11.83259 1.000 37.41824  ? 222 VAL   A CG1 1 
ATOM   1626 C CG2 . VAL   A 1 215 ? -19.81252 -23.58659 -13.65333 1.000 20.92419  ? 222 VAL   A CG2 1 
ATOM   1627 N N   . GLU   A 1 216 ? -16.94888 -26.14578 -13.62554 1.000 22.95664  ? 223 GLU   A N   1 
ATOM   1628 C CA  . GLU   A 1 216 ? -16.72820 -27.44515 -14.24142 1.000 26.97333  ? 223 GLU   A CA  1 
ATOM   1629 C C   . GLU   A 1 216 ? -17.82648 -28.42801 -13.87254 1.000 29.57278  ? 223 GLU   A C   1 
ATOM   1630 O O   . GLU   A 1 216 ? -18.38260 -28.36658 -12.77635 1.000 31.49689  ? 223 GLU   A O   1 
ATOM   1631 C CB  . GLU   A 1 216 ? -15.36372 -28.02139 -13.85068 1.000 33.97277  ? 223 GLU   A CB  1 
ATOM   1632 C CG  . GLU   A 1 216 ? -14.22132 -27.04880 -14.06011 1.000 32.86559  ? 223 GLU   A CG  1 
ATOM   1633 C CD  . GLU   A 1 216 ? -12.89867 -27.60439 -13.57194 1.000 41.56578  ? 223 GLU   A CD  1 
ATOM   1634 O OE1 . GLU   A 1 216 ? -12.29539 -26.99213 -12.65180 1.000 33.61446  ? 223 GLU   A OE1 1 
ATOM   1635 O OE2 . GLU   A 1 216 ? -12.49781 -28.68004 -14.08626 1.000 30.48944  ? 223 GLU   A OE2 1 
ATOM   1636 N N   . LYS   A 1 217 ? -18.11765 -29.33855 -14.80867 1.000 30.62059  ? 224 LYS   A N   1 
ATOM   1637 C CA  . LYS   A 1 217 ? -19.03395 -30.46557 -14.61673 1.000 44.92844  ? 224 LYS   A CA  1 
ATOM   1638 C C   . LYS   A 1 217 ? -18.88224 -31.09976 -13.22983 1.000 57.95830  ? 224 LYS   A C   1 
ATOM   1639 O O   . LYS   A 1 217 ? -17.77368 -31.42983 -12.79859 1.000 50.85014  ? 224 LYS   A O   1 
ATOM   1640 C CB  . LYS   A 1 217 ? -18.81314 -31.54805 -15.68446 1.000 43.39559  ? 224 LYS   A CB  1 
ATOM   1641 C CG  . LYS   A 1 217 ? -20.04259 -32.45496 -15.85677 1.000 64.19261  ? 224 LYS   A CG  1 
ATOM   1642 C CD  . LYS   A 1 217 ? -19.76742 -33.78023 -16.56155 1.000 57.26640  ? 224 LYS   A CD  1 
ATOM   1643 C CE  . LYS   A 1 217 ? -20.21320 -34.91596 -15.66352 1.000 66.73875  ? 224 LYS   A CE  1 
ATOM   1644 N NZ  . LYS   A 1 217 ? -19.86300 -36.25919 -16.17635 1.000 45.68304  ? 224 LYS   A NZ  1 
HETATM 1645 C C2  . A1AYK B 2 .   ? -1.62043  -12.66186 -23.64910 0.395 87.18575  ? 301 A1AYK A C2  1 
HETATM 1646 C C1  . A1AYK B 2 .   ? -1.82088  -11.31788 -23.93595 1.000 76.02575  ? 301 A1AYK A C1  1 
HETATM 1647 C C10 . A1AYK B 2 .   ? -0.69906  -6.37493  -24.90510 0.529 70.75993  ? 301 A1AYK A C10 1 
HETATM 1648 C C11 . A1AYK B 2 .   ? 0.58850   -7.16627  -24.88320 1.000 94.79835  ? 301 A1AYK A C11 1 
HETATM 1649 C C3  . A1AYK B 2 .   ? -0.33806  -13.18657 -23.57536 0.988 63.91568  ? 301 A1AYK A C3  1 
HETATM 1650 C C4  . A1AYK B 2 .   ? 0.75680   -12.38111 -23.78380 1.000 59.03575  ? 301 A1AYK A C4  1 
HETATM 1651 C C5  . A1AYK B 2 .   ? 0.59592   -11.04024 -24.06918 1.000 53.83575  ? 301 A1AYK A C5  1 
HETATM 1652 C C6  . A1AYK B 2 .   ? -0.67611  -10.48808 -24.15909 1.000 67.26575  ? 301 A1AYK A C6  1 
HETATM 1653 C C7  . A1AYK B 2 .   ? 0.28770   -8.57658  -25.33578 1.000 97.96575  ? 301 A1AYK A C7  1 
HETATM 1654 C C8  . A1AYK B 2 .   ? -0.21083  -8.58251  -26.76474 1.000 79.46575  ? 301 A1AYK A C8  1 
HETATM 1655 C C9  . A1AYK B 2 .   ? -0.68862  -7.20179  -27.15520 0.790 68.28648  ? 301 A1AYK A C9  1 
HETATM 1656 N N1  . A1AYK B 2 .   ? -3.11544  -10.76613 -24.02507 1.000 26.65792  ? 301 A1AYK A N1  1 
HETATM 1657 O O1  . A1AYK B 2 .   ? -0.73346  -9.14898  -24.44031 0.662 73.64575  ? 301 A1AYK A O1  1 
HETATM 1658 O O2  . A1AYK B 2 .   ? -1.44386  -6.59772  -26.10521 1.000 54.30575  ? 301 A1AYK A O2  1 
HETATM 1659 O O   . HOH   C 3 .   ? -17.56682 -24.64668 -9.05187  1.000 45.03215  ? 401 HOH   A O   1 
HETATM 1660 O O   . HOH   C 3 .   ? 2.19051   -15.72767 -41.11328 1.000 45.40590  ? 402 HOH   A O   1 
HETATM 1661 O O   . HOH   C 3 .   ? 11.63757  -21.50341 -40.72274 1.000 48.97160  ? 403 HOH   A O   1 
HETATM 1662 O O   . HOH   C 3 .   ? -2.87031  -2.95454  -35.44276 1.000 37.17370  ? 404 HOH   A O   1 
HETATM 1663 O O   . HOH   C 3 .   ? -3.64234  -13.31373 -42.89611 1.000 42.64536  ? 405 HOH   A O   1 
HETATM 1664 O O   . HOH   C 3 .   ? -17.45669 -28.38923 -17.03890 1.000 38.42614  ? 406 HOH   A O   1 
HETATM 1665 O O   . HOH   C 3 .   ? 1.40998   -26.63119 -2.93603  1.000 43.69056  ? 407 HOH   A O   1 
HETATM 1666 O O   . HOH   C 3 .   ? 9.21724   -3.27611  -20.38476 1.000 32.92172  ? 408 HOH   A O   1 
HETATM 1667 O O   . HOH   C 3 .   ? 20.20446  -3.20615  -8.15055  1.000 47.32370  ? 409 HOH   A O   1 
HETATM 1668 O O   . HOH   C 3 .   ? 13.86141  -11.30296 -29.74903 1.000 39.20725  ? 410 HOH   A O   1 
HETATM 1669 O O   . HOH   C 3 .   ? -4.40227  0.48921   -22.21470 1.000 34.15288  ? 411 HOH   A O   1 
HETATM 1670 O O   . HOH   C 3 .   ? -8.34334  1.93174   -36.50839 1.000 34.17954  ? 412 HOH   A O   1 
HETATM 1671 O O   . HOH   C 3 .   ? -12.99320 -7.29005  -12.02950 1.000 32.71733  ? 413 HOH   A O   1 
HETATM 1672 O O   . HOH   C 3 .   ? -1.62821  -29.10896 -5.83756  1.000 29.92689  ? 414 HOH   A O   1 
HETATM 1673 O O   . HOH   C 3 .   ? 7.63648   1.17443   -14.73586 1.000 27.92437  ? 415 HOH   A O   1 
HETATM 1674 O O   . HOH   C 3 .   ? 5.21183   -29.09700 -8.41461  1.000 40.12154  ? 416 HOH   A O   1 
HETATM 1675 O O   . HOH   C 3 .   ? -8.09011  -22.47359 -30.31167 1.000 42.55065  ? 417 HOH   A O   1 
HETATM 1676 O O   . HOH   C 3 .   ? -0.20765  -5.50324  -38.40163 1.000 41.44335  ? 418 HOH   A O   1 
HETATM 1677 O O   . HOH   C 3 .   ? 7.66831   -18.85188 -6.58944  1.000 21.93041  ? 419 HOH   A O   1 
HETATM 1678 O O   . HOH   C 3 .   ? 3.32296   -24.39068 -38.67799 1.000 33.45951  ? 420 HOH   A O   1 
HETATM 1679 O O   . HOH   C 3 .   ? 21.77954  -13.43375 -19.54029 1.000 45.33855  ? 421 HOH   A O   1 
HETATM 1680 O O   . HOH   C 3 .   ? 5.92460   -21.89933 -37.33848 1.000 27.98634  ? 422 HOH   A O   1 
HETATM 1681 O O   . HOH   C 3 .   ? -13.40392 -0.82386  -20.53619 1.000 26.79647  ? 423 HOH   A O   1 
HETATM 1682 O O   . HOH   C 3 .   ? -3.27597  -12.13951 -9.17542  1.000 32.11626  ? 424 HOH   A O   1 
HETATM 1683 O O   . HOH   C 3 .   ? 7.78908   -23.18793 -14.22730 1.000 23.79545  ? 425 HOH   A O   1 
HETATM 1684 O O   . HOH   C 3 .   ? -16.18009 -25.35278 -17.97824 1.000 24.80382  ? 426 HOH   A O   1 
HETATM 1685 O O   . HOH   C 3 .   ? -2.62398  -10.57182 -26.60211 1.000 35.89673  ? 427 HOH   A O   1 
HETATM 1686 O O   . HOH   C 3 .   ? 9.83660   -14.74013 -25.30115 1.000 18.28114  ? 428 HOH   A O   1 
HETATM 1687 O O   . HOH   C 3 .   ? -18.87835 -10.98217 -23.77441 1.000 26.72316  ? 429 HOH   A O   1 
HETATM 1688 O O   . HOH   C 3 .   ? 9.09727   -26.42983 -17.05235 1.000 22.51753  ? 430 HOH   A O   1 
HETATM 1689 O O   . HOH   C 3 .   ? -16.34948 -12.74457 -19.82484 1.000 17.65120  ? 431 HOH   A O   1 
HETATM 1690 O O   . HOH   C 3 .   ? 1.43901   -7.86636  -16.60336 1.000 17.94964  ? 432 HOH   A O   1 
HETATM 1691 O O   . HOH   C 3 .   ? -12.96479 -25.03669 -10.90204 1.000 27.85734  ? 433 HOH   A O   1 
HETATM 1692 O O   . HOH   C 3 .   ? 3.56518   -7.67640  -36.66608 1.000 33.61224  ? 434 HOH   A O   1 
HETATM 1693 O O   . HOH   C 3 .   ? 6.05499   -21.16855 -0.10478  1.000 23.15266  ? 435 HOH   A O   1 
HETATM 1694 O O   . HOH   C 3 .   ? -5.25191  -10.41965 -27.33532 1.000 18.76257  ? 436 HOH   A O   1 
HETATM 1695 O O   . HOH   C 3 .   ? -3.22581  -31.67105 -19.92853 1.000 43.66281  ? 437 HOH   A O   1 
HETATM 1696 O O   . HOH   C 3 .   ? -6.36164  -4.94775  -39.04532 1.000 37.41891  ? 438 HOH   A O   1 
HETATM 1697 O O   . HOH   C 3 .   ? -6.74288  -28.06375 -21.28067 1.000 35.65655  ? 439 HOH   A O   1 
HETATM 1698 O O   . HOH   C 3 .   ? 3.26488   -6.20194  -11.14062 1.000 20.98649  ? 440 HOH   A O   1 
HETATM 1699 O O   . HOH   C 3 .   ? -0.25978  -5.38887  -18.45323 1.000 27.46926  ? 441 HOH   A O   1 
HETATM 1700 O O   . HOH   C 3 .   ? -5.78617  -2.11349  -19.45177 1.000 19.57228  ? 442 HOH   A O   1 
HETATM 1701 O O   . HOH   C 3 .   ? 6.73779   -29.71520 -20.26181 1.000 33.16152  ? 443 HOH   A O   1 
HETATM 1702 O O   . HOH   C 3 .   ? -4.07231  -5.00846  -8.54064  1.000 39.63583  ? 444 HOH   A O   1 
HETATM 1703 O O   . HOH   C 3 .   ? 0.32882   -14.96111 -1.41644  1.000 35.04542  ? 445 HOH   A O   1 
HETATM 1704 O O   . HOH   C 3 .   ? 3.10231   -5.78543  -6.14349  1.000 38.60195  ? 446 HOH   A O   1 
HETATM 1705 O O   . HOH   C 3 .   ? 8.53733   -0.41815  -17.31615 1.000 40.73609  ? 447 HOH   A O   1 
HETATM 1706 O O   . HOH   C 3 .   ? -9.28491  -2.32864  -17.59378 1.000 16.59523  ? 448 HOH   A O   1 
HETATM 1707 O O   . HOH   C 3 .   ? -7.70707  -28.24485 -7.93928  1.000 30.49373  ? 449 HOH   A O   1 
HETATM 1708 O O   . HOH   C 3 .   ? -17.20888 -5.64552  -22.81235 1.000 24.66363  ? 450 HOH   A O   1 
HETATM 1709 O O   . HOH   C 3 .   ? -20.541   -20.805   -9.479    1.000 45.11676  ? 451 HOH   A O   1 
HETATM 1710 O O   . HOH   C 3 .   ? 11.58310  -27.40869 -34.73016 1.000 22.44966  ? 452 HOH   A O   1 
HETATM 1711 O O   . HOH   C 3 .   ? 9.82941   -23.82959 -9.37303  1.000 42.15943  ? 453 HOH   A O   1 
HETATM 1712 O O   . HOH   C 3 .   ? 11.47293  -28.26985 -30.45142 1.000 29.08307  ? 454 HOH   A O   1 
HETATM 1713 O O   . HOH   C 3 .   ? 18.35635  -7.16137  -20.25280 1.000 32.56687  ? 455 HOH   A O   1 
HETATM 1714 O O   . HOH   C 3 .   ? -14.34176 -6.85283  -14.43262 1.000 31.14958  ? 456 HOH   A O   1 
HETATM 1715 O O   . HOH   C 3 .   ? 14.36147  -9.17423  -4.35176  1.000 47.13485  ? 457 HOH   A O   1 
HETATM 1716 O O   . HOH   C 3 .   ? 3.49081   -29.82301 -25.80279 1.000 47.63931  ? 458 HOH   A O   1 
HETATM 1717 O O   . HOH   C 3 .   ? 6.73893   -26.61632 -27.63742 1.000 29.96950  ? 459 HOH   A O   1 
HETATM 1718 O O   . HOH   C 3 .   ? -15.85912 0.17736   -30.32179 1.000 43.90640  ? 460 HOH   A O   1 
HETATM 1719 O O   . HOH   C 3 .   ? 0.67239   -29.68909 -15.98763 1.000 35.26692  ? 461 HOH   A O   1 
HETATM 1720 O O   . HOH   C 3 .   ? -2.25140  -13.65373 -35.68948 1.000 16.36125  ? 462 HOH   A O   1 
HETATM 1721 O O   . HOH   C 3 .   ? -7.73123  -24.30070 -23.07401 1.000 25.66589  ? 463 HOH   A O   1 
HETATM 1722 O O   . HOH   C 3 .   ? -11.03487 -14.13060 -37.77710 1.000 32.09568  ? 464 HOH   A O   1 
HETATM 1723 O O   . HOH   C 3 .   ? -8.65568  -11.80174 -36.60050 1.000 22.12703  ? 465 HOH   A O   1 
HETATM 1724 O O   . HOH   C 3 .   ? 7.67629   -27.95693 -24.10914 1.000 27.16806  ? 466 HOH   A O   1 
HETATM 1725 O O   . HOH   C 3 .   ? 9.58931   -11.08196 -34.81353 1.000 36.38209  ? 467 HOH   A O   1 
HETATM 1726 O O   . HOH   C 3 .   ? 9.78194   -17.42288 -7.76708  1.000 21.11439  ? 468 HOH   A O   1 
HETATM 1727 O O   . HOH   C 3 .   ? -19.40590 -9.99201  -33.31920 1.000 38.67810  ? 469 HOH   A O   1 
HETATM 1728 O O   . HOH   C 3 .   ? -1.85316  -33.77742 -10.47376 1.000 51.94179  ? 470 HOH   A O   1 
HETATM 1729 O O   . HOH   C 3 .   ? -8.48303  4.72797   -33.57104 1.000 26.20896  ? 471 HOH   A O   1 
HETATM 1730 O O   . HOH   C 3 .   ? 0.89698   -21.02442 -4.66482  1.000 23.47219  ? 472 HOH   A O   1 
HETATM 1731 O O   . HOH   C 3 .   ? 10.827    -14.766   -0.976    1.000 24.27343  ? 473 HOH   A O   1 
HETATM 1732 O O   . HOH   C 3 .   ? 0.73613   -5.31292  -14.00966 1.000 33.45008  ? 474 HOH   A O   1 
HETATM 1733 O O   . HOH   C 3 .   ? -6.42568  -7.70810  -34.41480 1.000 15.32306  ? 475 HOH   A O   1 
HETATM 1734 O O   . HOH   C 3 .   ? 0.77931   -26.92860 -37.43729 1.000 40.95775  ? 476 HOH   A O   1 
HETATM 1735 O O   . HOH   C 3 .   ? 0.28900   -21.97685 -2.21798  1.000 42.95277  ? 477 HOH   A O   1 
HETATM 1736 O O   . HOH   C 3 .   ? -3.05509  -5.87155  -6.56822  1.000 35.45653  ? 478 HOH   A O   1 
HETATM 1737 O O   . HOH   C 3 .   ? 11.22998  -8.02944  -27.48367 1.000 19.95321  ? 479 HOH   A O   1 
HETATM 1738 O O   . HOH   C 3 .   ? -6.27991  -11.31315 -10.07730 1.000 23.59247  ? 480 HOH   A O   1 
HETATM 1739 O O   . HOH   C 3 .   ? -15.68279 6.59956   -32.40717 1.000 43.80494  ? 481 HOH   A O   1 
HETATM 1740 O O   . HOH   C 3 .   ? -11.82756 -0.25824  -15.52077 1.000 34.96472  ? 482 HOH   A O   1 
HETATM 1741 O O   . HOH   C 3 .   ? -12.61497 -27.16765 -34.98175 1.000 45.69169  ? 483 HOH   A O   1 
HETATM 1742 O O   . HOH   C 3 .   ? 18.10865  -19.25771 -24.63829 1.000 27.48817  ? 484 HOH   A O   1 
HETATM 1743 O O   . HOH   C 3 .   ? 13.58769  -14.24594 -26.88288 1.000 19.15749  ? 485 HOH   A O   1 
HETATM 1744 O O   . HOH   C 3 .   ? -1.03864  -11.29642 -3.06134  1.000 30.74511  ? 486 HOH   A O   1 
HETATM 1745 O O   . HOH   C 3 .   ? -10.17026 -14.95122 -28.35514 1.000 25.38444  ? 487 HOH   A O   1 
HETATM 1746 O O   . HOH   C 3 .   ? 4.16850   -24.16754 -30.70705 1.000 17.49408  ? 488 HOH   A O   1 
HETATM 1747 O O   . HOH   C 3 .   ? -3.51105  -20.90399 -38.73065 1.000 39.86730  ? 489 HOH   A O   1 
HETATM 1748 O O   . HOH   C 3 .   ? -15.16736 -11.15762 -29.77183 1.000 21.94839  ? 490 HOH   A O   1 
HETATM 1749 O O   . HOH   C 3 .   ? -8.16848  -24.90101 -19.12381 1.000 14.66866  ? 491 HOH   A O   1 
HETATM 1750 O O   . HOH   C 3 .   ? 3.02169   -20.47575 -2.70330  1.000 30.96664  ? 492 HOH   A O   1 
HETATM 1751 O O   . HOH   C 3 .   ? -2.28622  -0.49329  -18.70676 1.000 40.49440  ? 493 HOH   A O   1 
HETATM 1752 O O   . HOH   C 3 .   ? 8.52747   -16.26792 -39.59708 1.000 33.69004  ? 494 HOH   A O   1 
HETATM 1753 O O   . HOH   C 3 .   ? -4.65724  -4.39264  -37.44023 1.000 45.04881  ? 495 HOH   A O   1 
HETATM 1754 O O   . HOH   C 3 .   ? -20.58595 -14.24509 -18.24122 1.000 34.78857  ? 496 HOH   A O   1 
HETATM 1755 O O   . HOH   C 3 .   ? 12.97358  -14.01293 -29.72138 1.000 24.22244  ? 497 HOH   A O   1 
HETATM 1756 O O   . HOH   C 3 .   ? 20.67306  -16.78596 -20.09244 1.000 32.89334  ? 498 HOH   A O   1 
HETATM 1757 O O   . HOH   C 3 .   ? 4.72644   -30.64144 -11.49006 1.000 34.85462  ? 499 HOH   A O   1 
HETATM 1758 O O   . HOH   C 3 .   ? -12.05805 -25.88961 -3.55924  1.000 46.39033  ? 500 HOH   A O   1 
HETATM 1759 O O   . HOH   C 3 .   ? 8.52399   -20.41101 -9.21659  1.000 27.04797  ? 501 HOH   A O   1 
HETATM 1760 O O   . HOH   C 3 .   ? 15.06563  -0.67946  -12.15119 1.000 39.39154  ? 502 HOH   A O   1 
HETATM 1761 O O   . HOH   C 3 .   ? -14.21255 -11.71546 0.40059   1.000 37.17277  ? 503 HOH   A O   1 
HETATM 1762 O O   . HOH   C 3 .   ? 3.64990   -6.80274  -17.79429 1.000 23.44615  ? 504 HOH   A O   1 
HETATM 1763 O O   . HOH   C 3 .   ? -10.16208 -0.62380  -19.91266 1.000 27.66383  ? 505 HOH   A O   1 
HETATM 1764 O O   . HOH   C 3 .   ? -1.20328  -25.98213 -32.45346 1.000 37.39941  ? 506 HOH   A O   1 
HETATM 1765 O O   . HOH   C 3 .   ? 19.73288  -16.57720 -27.71848 1.000 37.65991  ? 507 HOH   A O   1 
HETATM 1766 O O   . HOH   C 3 .   ? -7.39094  -5.44212  -2.73022  1.000 48.34815  ? 508 HOH   A O   1 
HETATM 1767 O O   . HOH   C 3 .   ? -14.20244 -12.71751 -7.82332  1.000 19.34651  ? 509 HOH   A O   1 
HETATM 1768 O O   . HOH   C 3 .   ? -18.27238 -3.92441  -29.10932 1.000 45.70520  ? 510 HOH   A O   1 
HETATM 1769 O O   . HOH   C 3 .   ? -4.73820  0.50016   -30.52685 1.000 26.06940  ? 511 HOH   A O   1 
HETATM 1770 O O   . HOH   C 3 .   ? -13.78526 -17.03868 -2.61506  1.000 21.08838  ? 512 HOH   A O   1 
HETATM 1771 O O   . HOH   C 3 .   ? -14.61307 -22.57707 -11.40003 1.000 23.38394  ? 513 HOH   A O   1 
HETATM 1772 O O   . HOH   C 3 .   ? 10.65420  -25.38908 -23.78884 1.000 18.35438  ? 514 HOH   A O   1 
HETATM 1773 O O   . HOH   C 3 .   ? 8.83266   -15.48056 -27.81396 1.000 16.28808  ? 515 HOH   A O   1 
HETATM 1774 O O   . HOH   C 3 .   ? 14.10927  -15.68956 -2.04254  1.000 29.42101  ? 516 HOH   A O   1 
HETATM 1775 O O   . HOH   C 3 .   ? -10.41176 -11.50159 -2.15790  1.000 20.19484  ? 517 HOH   A O   1 
HETATM 1776 O O   . HOH   C 3 .   ? 10.49788  -21.24145 -6.92003  1.000 35.28155  ? 518 HOH   A O   1 
HETATM 1777 O O   . HOH   C 3 .   ? 5.99305   -25.43382 -7.25487  1.000 38.95403  ? 519 HOH   A O   1 
HETATM 1778 O O   . HOH   C 3 .   ? -6.12211  -14.04559 0.82906   1.000 25.29501  ? 520 HOH   A O   1 
HETATM 1779 O O   . HOH   C 3 .   ? 0.09918   -28.57675 -25.38184 1.000 47.12070  ? 521 HOH   A O   1 
HETATM 1780 O O   . HOH   C 3 .   ? 15.49523  -20.30520 -18.65561 1.000 21.02895  ? 522 HOH   A O   1 
HETATM 1781 O O   . HOH   C 3 .   ? 14.39227  -24.02898 -17.39745 1.000 38.92981  ? 523 HOH   A O   1 
HETATM 1782 O O   . HOH   C 3 .   ? -8.00679  -3.91624  -10.75165 1.000 25.82288  ? 524 HOH   A O   1 
HETATM 1783 O O   . HOH   C 3 .   ? 1.42937   -3.21494  -24.65586 1.000 35.39175  ? 525 HOH   A O   1 
HETATM 1784 O O   . HOH   C 3 .   ? -5.39821  -7.66152  -13.13645 1.000 17.11682  ? 526 HOH   A O   1 
HETATM 1785 O O   . HOH   C 3 .   ? -19.825   -19.506   -14.297   1.000 17.04133  ? 527 HOH   A O   1 
HETATM 1786 O O   . HOH   C 3 .   ? 0.25131   -1.28483  -19.81999 1.000 41.15059  ? 528 HOH   A O   1 
HETATM 1787 O O   . HOH   C 3 .   ? 7.91660   -23.29176 -7.24185  1.000 34.29465  ? 529 HOH   A O   1 
HETATM 1788 O O   . HOH   C 3 .   ? -3.93533  -13.99637 -0.78211  1.000 36.86859  ? 530 HOH   A O   1 
HETATM 1789 O O   . HOH   C 3 .   ? -17.80936 -18.89953 -11.32057 1.000 32.33816  ? 531 HOH   A O   1 
HETATM 1790 O O   . HOH   C 3 .   ? -8.92995  -10.43016 -40.64490 1.000 39.51472  ? 532 HOH   A O   1 
HETATM 1791 O O   . HOH   C 3 .   ? -16.15730 -2.96351  -21.27475 1.000 26.34367  ? 533 HOH   A O   1 
HETATM 1792 O O   . HOH   C 3 .   ? -0.27801  -7.05384  -31.03705 1.000 25.20081  ? 534 HOH   A O   1 
HETATM 1793 O O   . HOH   C 3 .   ? 3.78914   -11.80840 -38.67191 1.000 23.14095  ? 535 HOH   A O   1 
HETATM 1794 O O   . HOH   C 3 .   ? -6.28592  -5.10193  -35.63928 1.000 18.18165  ? 536 HOH   A O   1 
HETATM 1795 O O   . HOH   C 3 .   ? -2.556    -24.822   -1.277    1.000 48.44158  ? 537 HOH   A O   1 
HETATM 1796 O O   . HOH   C 3 .   ? -5.74427  -31.29698 -11.56454 1.000 28.13087  ? 538 HOH   A O   1 
HETATM 1797 O O   . HOH   C 3 .   ? -11.89719 -7.56294  -38.34456 1.000 35.34006  ? 539 HOH   A O   1 
HETATM 1798 O O   . HOH   C 3 .   ? 10.73561  -25.64065 -26.70935 1.000 26.92051  ? 540 HOH   A O   1 
HETATM 1799 O O   . HOH   C 3 .   ? -5.12701  -14.25648 -22.70361 1.000 17.33261  ? 541 HOH   A O   1 
HETATM 1800 O O   . HOH   C 3 .   ? -1.35899  -4.35040  -33.93012 1.000 39.92328  ? 542 HOH   A O   1 
HETATM 1801 O O   . HOH   C 3 .   ? -14.43461 -21.92082 -33.53375 1.000 36.82847  ? 543 HOH   A O   1 
HETATM 1802 O O   . HOH   C 3 .   ? -10.61788 -6.36121  -2.97693  1.000 44.98651  ? 544 HOH   A O   1 
HETATM 1803 O O   . HOH   C 3 .   ? 15.49383  -0.65434  -19.42353 1.000 36.76493  ? 545 HOH   A O   1 
HETATM 1804 O O   . HOH   C 3 .   ? -3.16028  -1.04116  -24.14524 1.000 24.09056  ? 546 HOH   A O   1 
HETATM 1805 O O   . HOH   C 3 .   ? -1.84181  -25.68911 -4.76025  1.000 21.22366  ? 547 HOH   A O   1 
HETATM 1806 O O   . HOH   C 3 .   ? 8.55601   -19.98390 -41.44256 1.000 42.18927  ? 548 HOH   A O   1 
HETATM 1807 O O   . HOH   C 3 .   ? 20.13750  -10.30328 -26.49576 1.000 37.00594  ? 549 HOH   A O   1 
HETATM 1808 O O   . HOH   C 3 .   ? 14.38167  -15.93602 -30.77600 1.000 32.98465  ? 550 HOH   A O   1 
HETATM 1809 O O   . HOH   C 3 .   ? -5.83470  -18.85288 -39.10980 1.000 31.65275  ? 551 HOH   A O   1 
HETATM 1810 O O   . HOH   C 3 .   ? -1.55382  -30.46598 -19.43466 1.000 42.15678  ? 552 HOH   A O   1 
HETATM 1811 O O   . HOH   C 3 .   ? 3.12842   -4.08227  -9.04725  1.000 43.62457  ? 553 HOH   A O   1 
HETATM 1812 O O   . HOH   C 3 .   ? -19.06442 -13.55504 -27.51640 1.000 47.16351  ? 554 HOH   A O   1 
HETATM 1813 O O   . HOH   C 3 .   ? 7.37227   -4.61982  -22.34641 1.000 35.49015  ? 555 HOH   A O   1 
HETATM 1814 O O   . HOH   C 3 .   ? -7.18340  -22.82761 -36.63106 1.000 44.24564  ? 556 HOH   A O   1 
HETATM 1815 O O   . HOH   C 3 .   ? 0.45318   -5.47938  -21.97071 1.000 39.42967  ? 557 HOH   A O   1 
HETATM 1816 O O   . HOH   C 3 .   ? -7.33617  1.28008   -19.35227 1.000 33.17994  ? 558 HOH   A O   1 
HETATM 1817 O O   . HOH   C 3 .   ? -5.17969  -31.68908 -7.03241  1.000 41.29488  ? 559 HOH   A O   1 
HETATM 1818 O O   . HOH   C 3 .   ? -3.39709  -21.10601 -0.44039  1.000 32.85201  ? 560 HOH   A O   1 
HETATM 1819 O O   . HOH   C 3 .   ? -1.66207  -32.75774 -7.91608  1.000 47.49697  ? 561 HOH   A O   1 
HETATM 1820 O O   . HOH   C 3 .   ? 12.38326  -27.48583 -19.48280 1.000 42.63058  ? 562 HOH   A O   1 
HETATM 1821 O O   . HOH   C 3 .   ? 2.99299   -4.93417  -28.60992 1.000 38.23554  ? 563 HOH   A O   1 
HETATM 1822 O O   . HOH   C 3 .   ? -3.37568  -13.06640 -20.76764 1.000 20.41651  ? 564 HOH   A O   1 
HETATM 1823 O O   . HOH   C 3 .   ? 20.90664  -14.07237 -26.72977 1.000 31.12086  ? 565 HOH   A O   1 
HETATM 1824 O O   . HOH   C 3 .   ? 4.04950   -9.18928  -20.36878 1.000 17.72876  ? 566 HOH   A O   1 
HETATM 1825 O O   . HOH   C 3 .   ? -4.04537  -3.36543  -15.46292 1.000 39.95862  ? 567 HOH   A O   1 
HETATM 1826 O O   . HOH   C 3 .   ? -17.71027 -15.20568 -13.09244 1.000 21.50269  ? 568 HOH   A O   1 
HETATM 1827 O O   . HOH   C 3 .   ? -2.45099  -15.54600 -0.27431  1.000 34.24329  ? 569 HOH   A O   1 
HETATM 1828 O O   . HOH   C 3 .   ? -8.79891  -18.04329 -36.73172 1.000 38.29071  ? 570 HOH   A O   1 
HETATM 1829 O O   . HOH   C 3 .   ? 4.98770   -9.88718  -2.50384  1.000 37.76098  ? 571 HOH   A O   1 
HETATM 1830 O O   . HOH   C 3 .   ? -13.66674 -30.86378 -12.49018 1.000 50.94615  ? 572 HOH   A O   1 
HETATM 1831 O O   . HOH   C 3 .   ? -14.58784 -3.57181  -12.77915 1.000 41.56559  ? 573 HOH   A O   1 
HETATM 1832 O O   . HOH   C 3 .   ? 11.61578  -2.00331  -3.78610  1.000 48.14908  ? 574 HOH   A O   1 
HETATM 1833 O O   . HOH   C 3 .   ? -19.52069 -14.49978 -20.37360 1.000 43.00555  ? 575 HOH   A O   1 
HETATM 1834 O O   . HOH   C 3 .   ? 4.40212   -19.36291 -40.75581 1.000 29.70157  ? 576 HOH   A O   1 
HETATM 1835 O O   . HOH   C 3 .   ? -5.08458  -5.23355  -11.90202 1.000 34.78633  ? 577 HOH   A O   1 
HETATM 1836 O O   . HOH   C 3 .   ? 13.75785  -20.48974 -20.75207 1.000 17.69359  ? 578 HOH   A O   1 
HETATM 1837 O O   . HOH   C 3 .   ? 1.83283   -4.02715  -16.98346 1.000 46.44583  ? 579 HOH   A O   1 
HETATM 1838 O O   . HOH   C 3 .   ? 8.85205   -20.49637 -4.36600  1.000 24.38022  ? 580 HOH   A O   1 
HETATM 1839 O O   . HOH   C 3 .   ? 4.99377   -1.05657  -6.14795  1.000 48.74146  ? 581 HOH   A O   1 
HETATM 1840 O O   . HOH   C 3 .   ? 15.75852  -18.19337 -3.57447  1.000 31.06070  ? 582 HOH   A O   1 
HETATM 1841 O O   . HOH   C 3 .   ? -13.53575 -26.53493 -18.21933 1.000 21.85529  ? 583 HOH   A O   1 
HETATM 1842 O O   . HOH   C 3 .   ? 10.91766  -11.59921 -4.79578  1.000 29.92629  ? 584 HOH   A O   1 
HETATM 1843 O O   . HOH   C 3 .   ? 12.23977  -3.82144  0.26627   1.000 47.95937  ? 585 HOH   A O   1 
HETATM 1844 O O   . HOH   C 3 .   ? 6.97209   -29.72958 -30.19188 1.000 46.19562  ? 586 HOH   A O   1 
HETATM 1845 O O   . HOH   C 3 .   ? -16.34638 -25.45678 -10.77528 1.000 31.79914  ? 587 HOH   A O   1 
HETATM 1846 O O   . HOH   C 3 .   ? -5.556    -11.181   1.248     1.000 49.40038  ? 588 HOH   A O   1 
HETATM 1847 O O   . HOH   C 3 .   ? -16.43180 -9.09745  -14.20552 1.000 30.08223  ? 589 HOH   A O   1 
HETATM 1848 O O   . HOH   C 3 .   ? 13.39586  -6.81032  -26.29672 1.000 19.45798  ? 590 HOH   A O   1 
HETATM 1849 O O   . HOH   C 3 .   ? 10.54511  -17.70958 -39.07006 1.000 36.59994  ? 591 HOH   A O   1 
HETATM 1850 O O   . HOH   C 3 .   ? -13.73771 -18.60983 -24.45086 1.000 17.55587  ? 592 HOH   A O   1 
HETATM 1851 O O   . HOH   C 3 .   ? 18.63928  -15.93447 -13.38627 1.000 37.96382  ? 593 HOH   A O   1 
HETATM 1852 O O   . HOH   C 3 .   ? -1.02206  -27.67092 -34.76666 1.000 47.60819  ? 594 HOH   A O   1 
HETATM 1853 O O   . HOH   C 3 .   ? -15.13250 -11.96750 -11.95085 1.000 30.17007  ? 595 HOH   A O   1 
HETATM 1854 O O   . HOH   C 3 .   ? -14.17615 -16.09379 -26.19820 1.000 25.09040  ? 596 HOH   A O   1 
HETATM 1855 O O   . HOH   C 3 .   ? 3.85018   -23.13229 -3.39810  1.000 32.65881  ? 597 HOH   A O   1 
HETATM 1856 O O   . HOH   C 3 .   ? 15.63341  -7.20853  -27.80555 1.000 32.79080  ? 598 HOH   A O   1 
HETATM 1857 O O   . HOH   C 3 .   ? -13.61222 -25.86642 -7.75084  1.000 22.84751  ? 599 HOH   A O   1 
HETATM 1858 O O   . HOH   C 3 .   ? 10.78873  -22.95357 -41.58943 1.000 52.86718  ? 600 HOH   A O   1 
HETATM 1859 O O   . HOH   C 3 .   ? -14.10019 -24.04522 -4.88376  1.000 28.31936  ? 601 HOH   A O   1 
HETATM 1860 O O   . HOH   C 3 .   ? 13.78499  -3.98716  -25.39638 1.000 14.75893  ? 602 HOH   A O   1 
HETATM 1861 O O   . HOH   C 3 .   ? 20.24976  -5.49525  -14.67591 1.000 42.51084  ? 603 HOH   A O   1 
HETATM 1862 O O   . HOH   C 3 .   ? -12.30773 -26.95082 -20.31176 1.000 24.16714  ? 604 HOH   A O   1 
HETATM 1863 O O   . HOH   C 3 .   ? -2.30673  -8.75592  -43.55633 1.000 48.57461  ? 605 HOH   A O   1 
HETATM 1864 O O   . HOH   C 3 .   ? -0.03147  -16.61586 -3.38380  1.000 22.46930  ? 606 HOH   A O   1 
HETATM 1865 O O   . HOH   C 3 .   ? -13.10123 -12.23095 -31.03777 1.000 20.32904  ? 607 HOH   A O   1 
HETATM 1866 O O   . HOH   C 3 .   ? 11.51083  -1.85910  -20.30550 1.000 36.43637  ? 608 HOH   A O   1 
HETATM 1867 O O   . HOH   C 3 .   ? -18.34279 -15.56909 -21.56626 1.000 39.83898  ? 609 HOH   A O   1 
HETATM 1868 O O   . HOH   C 3 .   ? -18.13887 -5.73065  -25.58925 1.000 30.90360  ? 610 HOH   A O   1 
HETATM 1869 O O   . HOH   C 3 .   ? 17.15337  -24.90790 -25.51095 1.000 35.29311  ? 611 HOH   A O   1 
HETATM 1870 O O   . HOH   C 3 .   ? 1.12792   -8.62920  -4.15164  1.000 35.91598  ? 612 HOH   A O   1 
HETATM 1871 O O   . HOH   C 3 .   ? 20.36390  -6.07615  -21.04369 1.000 33.18742  ? 613 HOH   A O   1 
HETATM 1872 O O   . HOH   C 3 .   ? 3.14327   -6.60521  -20.42922 1.000 35.34791  ? 614 HOH   A O   1 
HETATM 1873 O O   . HOH   C 3 .   ? -15.89493 0.01280   -41.08635 1.000 43.44733  ? 615 HOH   A O   1 
HETATM 1874 O O   . HOH   C 3 .   ? 21.76122  -3.81369  -25.22877 1.000 48.54648  ? 616 HOH   A O   1 
HETATM 1875 O O   . HOH   C 3 .   ? 8.25419   -25.90804 -25.92314 1.000 38.44573  ? 617 HOH   A O   1 
HETATM 1876 O O   . HOH   C 3 .   ? -16.04685 -3.82231  -15.33250 1.000 46.90656  ? 618 HOH   A O   1 
HETATM 1877 O O   . HOH   C 3 .   ? -1.89889  -26.86654 -25.21760 1.000 37.66706  ? 619 HOH   A O   1 
HETATM 1878 O O   . HOH   C 3 .   ? -5.56590  -12.32071 -41.95028 1.000 37.89991  ? 620 HOH   A O   1 
HETATM 1879 O O   . HOH   C 3 .   ? 1.88329   -18.42040 0.10867   1.000 29.32735  ? 621 HOH   A O   1 
HETATM 1880 O O   . HOH   C 3 .   ? -7.63092  7.60137   -33.84002 1.000 30.74781  ? 622 HOH   A O   1 
HETATM 1881 O O   . HOH   C 3 .   ? 18.50654  -9.63856  -9.34283  1.000 51.99138  ? 623 HOH   A O   1 
HETATM 1882 O O   . HOH   C 3 .   ? -17.976   -15.904   -23.426   1.000 29.23501  ? 624 HOH   A O   1 
HETATM 1883 O O   . HOH   C 3 .   ? 17.72320  -15.34624 -29.83134 1.000 40.73800  ? 625 HOH   A O   1 
HETATM 1884 O O   . HOH   C 3 .   ? -13.62864 -29.38233 -17.07980 1.000 46.94577  ? 626 HOH   A O   1 
HETATM 1885 O O   . HOH   C 3 .   ? 5.590     -3.045    -26.123   1.000 38.10263  ? 627 HOH   A O   1 
HETATM 1886 O O   . HOH   C 3 .   ? -12.38930 -20.41472 -29.72116 1.000 44.87905  ? 628 HOH   A O   1 
HETATM 1887 O O   . HOH   C 3 .   ? -1.56016  -33.01437 -16.76851 1.000 45.72521  ? 629 HOH   A O   1 
HETATM 1888 O O   . HOH   C 3 .   ? 4.76059   -1.94667  -18.22485 1.000 35.57157  ? 630 HOH   A O   1 
HETATM 1889 O O   . HOH   C 3 .   ? -1.26870  -5.66280  -12.23035 1.000 44.66101  ? 631 HOH   A O   1 
HETATM 1890 O O   . HOH   C 3 .   ? 1.92711   -25.90300 -29.33162 1.000 29.97137  ? 632 HOH   A O   1 
HETATM 1891 O O   . HOH   C 3 .   ? 4.40974   -21.87142 -39.45447 1.000 45.11474  ? 633 HOH   A O   1 
HETATM 1892 O O   . HOH   C 3 .   ? -17.03210 -4.70094  -17.29949 1.000 31.46574  ? 634 HOH   A O   1 
HETATM 1893 O O   . HOH   C 3 .   ? -7.184    -1.962    -12.602   1.000 35.07492  ? 635 HOH   A O   1 
HETATM 1894 O O   . HOH   C 3 .   ? -18.43594 -33.89456 -10.42059 1.000 60.04313  ? 636 HOH   A O   1 
HETATM 1895 O O   . HOH   C 3 .   ? -0.06402  -19.11164 -1.98122  1.000 32.32823  ? 637 HOH   A O   1 
HETATM 1896 O O   . HOH   C 3 .   ? -13.88484 -0.69599  -13.60233 1.000 33.33609  ? 638 HOH   A O   1 
HETATM 1897 O O   . HOH   C 3 .   ? 17.73979  -21.64408 -19.89926 1.000 31.67145  ? 639 HOH   A O   1 
HETATM 1898 O O   . HOH   C 3 .   ? -10.54956 -6.90556  -40.08151 1.000 59.50637  ? 640 HOH   A O   1 
HETATM 1899 O O   . HOH   C 3 .   ? -14.03790 -14.26681 -3.08625  1.000 31.19704  ? 641 HOH   A O   1 
HETATM 1900 O O   . HOH   C 3 .   ? 1.87177   -3.11723  -12.61578 1.000 36.38730  ? 642 HOH   A O   1 
HETATM 1901 O O   . HOH   C 3 .   ? 12.29260  -25.30417 -38.39572 1.000 28.22229  ? 643 HOH   A O   1 
HETATM 1902 O O   . HOH   C 3 .   ? 2.08123   -24.84595 -2.48347  1.000 55.27285  ? 644 HOH   A O   1 
HETATM 1903 O O   . HOH   C 3 .   ? -12.37338 -16.32922 -28.31144 1.000 30.26542  ? 645 HOH   A O   1 
HETATM 1904 O O   . HOH   C 3 .   ? -9.01716  -5.55181  -39.78506 1.000 43.57040  ? 646 HOH   A O   1 
HETATM 1905 O O   . HOH   C 3 .   ? -3.11193  -34.32295 -15.33317 1.000 51.38291  ? 647 HOH   A O   1 
HETATM 1906 O O   . HOH   C 3 .   ? 23.05166  -11.19860 -20.36995 1.000 51.09766  ? 648 HOH   A O   1 
HETATM 1907 O O   . HOH   C 3 .   ? 15.40229  -12.54292 -7.04230  1.000 41.69407  ? 649 HOH   A O   1 
HETATM 1908 O O   . HOH   C 3 .   ? 18.18980  -3.27175  -23.03628 1.000 45.00595  ? 650 HOH   A O   1 
HETATM 1909 O O   . HOH   C 3 .   ? -16.50257 -18.29870 -2.97943  1.000 48.40313  ? 651 HOH   A O   1 
HETATM 1910 O O   . HOH   C 3 .   ? -14.35840 -9.90600  -8.32074  1.000 35.17228  ? 652 HOH   A O   1 
HETATM 1911 O O   . HOH   C 3 .   ? 3.27661   -7.93369  -2.09090  1.000 48.07480  ? 653 HOH   A O   1 
HETATM 1912 O O   . HOH   C 3 .   ? -0.46299  -1.27085  -23.12115 1.000 38.61497  ? 654 HOH   A O   1 
HETATM 1913 O O   . HOH   C 3 .   ? 3.48977   -9.06896  -39.11796 1.000 35.38921  ? 655 HOH   A O   1 
HETATM 1914 O O   . HOH   C 3 .   ? 16.222    1.430     -15.440   1.000 47.33969  ? 656 HOH   A O   1 
HETATM 1915 O O   . HOH   C 3 .   ? 11.97982  -27.70973 -23.47124 1.000 50.52077  ? 657 HOH   A O   1 
HETATM 1916 O O   . HOH   C 3 .   ? 19.17652  -8.40958  -17.74966 1.000 38.33491  ? 658 HOH   A O   1 
HETATM 1917 O O   . HOH   C 3 .   ? -2.28082  -0.87989  -31.17255 1.000 35.81765  ? 659 HOH   A O   1 
HETATM 1918 O O   . HOH   C 3 .   ? 14.56378  -22.01667 -16.89452 1.000 34.08270  ? 660 HOH   A O   1 
HETATM 1919 O O   . HOH   C 3 .   ? -6.702    -23.183   -1.735    1.000 35.25400  ? 661 HOH   A O   1 
HETATM 1920 O O   . HOH   C 3 .   ? 14.95225  -8.05178  -30.29902 1.000 40.60164  ? 662 HOH   A O   1 
HETATM 1921 O O   . HOH   C 3 .   ? 16.92314  -6.59831  -29.39370 1.000 44.85283  ? 663 HOH   A O   1 
HETATM 1922 O O   . HOH   C 3 .   ? -11.94769 -19.39013 -28.23518 1.000 47.78697  ? 664 HOH   A O   1 
HETATM 1923 O O   . HOH   C 3 .   ? -11.58154 -9.61535  -39.72936 1.000 44.80509  ? 665 HOH   A O   1 
HETATM 1924 O O   . HOH   C 3 .   ? 7.85299   -13.93117 -38.26140 1.000 32.30083  ? 666 HOH   A O   1 
HETATM 1925 O O   . HOH   C 3 .   ? -9.84695  -26.06025 -20.91171 1.000 23.68674  ? 667 HOH   A O   1 
HETATM 1926 O O   . HOH   C 3 .   ? -5.46132  -1.71584  -16.76211 1.000 35.11890  ? 668 HOH   A O   1 
HETATM 1927 O O   . HOH   C 3 .   ? 2.24401   -0.91646  -26.00996 1.000 37.18104  ? 669 HOH   A O   1 
HETATM 1928 O O   . HOH   C 3 .   ? -18.64176 -11.69138 -21.07900 1.000 26.82582  ? 670 HOH   A O   1 
HETATM 1929 O O   . HOH   C 3 .   ? 19.87729  -3.35607  -26.55633 1.000 55.28977  ? 671 HOH   A O   1 
HETATM 1930 O O   . HOH   C 3 .   ? 3.69041   -0.20576  -16.38442 1.000 36.72065  ? 672 HOH   A O   1 
HETATM 1931 O O   . HOH   C 3 .   ? -12.05406 -27.26158 -5.87035  1.000 52.68322  ? 673 HOH   A O   1 
HETATM 1932 O O   . HOH   C 3 .   ? -18.045   0.856     -21.946   1.000 51.04645  ? 674 HOH   A O   1 
HETATM 1933 O O   . HOH   C 3 .   ? -3.22671  -27.38517 -3.17382  1.000 43.65481  ? 675 HOH   A O   1 
HETATM 1934 O O   . HOH   C 3 .   ? 6.22822   -30.10602 -24.96615 1.000 43.61207  ? 676 HOH   A O   1 
HETATM 1935 O O   . HOH   C 3 .   ? 11.184    -1.275    -17.358   1.000 33.45358  ? 677 HOH   A O   1 
HETATM 1936 O O   . HOH   C 3 .   ? -7.78058  -21.16558 -37.73801 1.000 44.69342  ? 678 HOH   A O   1 
HETATM 1937 O O   . HOH   C 3 .   ? 12.39725  -9.83388  -1.62103  1.000 42.20330  ? 679 HOH   A O   1 
HETATM 1938 O O   . HOH   C 3 .   ? 5.80988   -12.95289 -39.93626 1.000 27.00196  ? 680 HOH   A O   1 
HETATM 1939 O O   . HOH   C 3 .   ? 17.04368  0.48761   -17.61262 1.000 36.95944  ? 681 HOH   A O   1 
HETATM 1940 O O   . HOH   C 3 .   ? 5.485     -3.300    -23.596   1.000 45.49179  ? 682 HOH   A O   1 
HETATM 1941 O O   . HOH   C 3 .   ? -10.42358 -8.78227  -1.33844  1.000 40.04015  ? 683 HOH   A O   1 
HETATM 1942 O O   . HOH   C 3 .   ? 7.91078   -29.13030 -28.42503 1.000 41.02271  ? 684 HOH   A O   1 
HETATM 1943 O O   . HOH   C 3 .   ? 6.67121   -21.56583 -2.75107  1.000 30.70858  ? 685 HOH   A O   1 
HETATM 1944 O O   . HOH   C 3 .   ? 2.86665   -4.46804  -19.79334 1.000 46.04379  ? 686 HOH   A O   1 
HETATM 1945 O O   . HOH   C 3 .   ? -10.592   -22.590   4.465     1.000 38.71265  ? 687 HOH   A O   1 
HETATM 1946 O O   . HOH   C 3 .   ? -4.07817  -29.73411 -22.32695 1.000 45.77482  ? 688 HOH   A O   1 
HETATM 1947 O O   . HOH   C 3 .   ? 11.11721  -28.03200 -27.84818 1.000 35.04669  ? 689 HOH   A O   1 
HETATM 1948 O O   . HOH   C 3 .   ? 8.190     -8.371    0.066     1.000 42.18861  ? 690 HOH   A O   1 
HETATM 1949 O O   . HOH   C 3 .   ? -6.97570  -30.84128 -9.24031  1.000 30.03269  ? 691 HOH   A O   1 
HETATM 1950 O O   . HOH   C 3 .   ? -7.65131  -24.27987 -26.09144 1.000 48.58874  ? 692 HOH   A O   1 
HETATM 1951 O O   . HOH   C 3 .   ? -17.32503 4.00345   -32.04101 1.000 46.94724  ? 693 HOH   A O   1 
HETATM 1952 O O   . HOH   C 3 .   ? 10.06287  -29.58730 -23.91109 1.000 42.81541  ? 694 HOH   A O   1 
HETATM 1953 O O   . HOH   C 3 .   ? 2.35222   -0.62232  -14.20309 1.000 39.69597  ? 695 HOH   A O   1 
HETATM 1954 O O   . HOH   C 3 .   ? 4.74451   -14.82876 -41.53054 1.000 41.00607  ? 696 HOH   A O   1 
HETATM 1955 O O   . HOH   C 3 .   ? -1.912    -23.111   0.785     1.000 45.06992  ? 697 HOH   A O   1 
HETATM 1956 O O   . HOH   C 3 .   ? 17.37282  -17.46239 -5.01059  1.000 45.01121  ? 698 HOH   A O   1 
HETATM 1957 O O   . HOH   C 3 .   ? -10.39295 -16.64882 -38.20049 1.000 48.74964  ? 699 HOH   A O   1 
HETATM 1958 O O   . HOH   C 3 .   ? -0.48709  -26.61570 -30.48521 1.000 37.64441  ? 700 HOH   A O   1 
HETATM 1959 O O   . HOH   C 3 .   ? -0.00000  -0.00000  -18.48657 0.50  31.03507  ? 701 HOH   A O   1 
HETATM 1960 O O   . HOH   C 3 .   ? -16.416   3.181     -26.275   1.000 36.18451  ? 702 HOH   A O   1 
HETATM 1961 O O   . HOH   C 3 .   ? 21.05619  -18.30460 -22.25711 1.000 37.00623  ? 703 HOH   A O   1 
HETATM 1962 O O   . HOH   C 3 .   ? -5.029    -25.151   -1.201    1.000 51.51967  ? 704 HOH   A O   1 
HETATM 1963 O O   . HOH   C 3 .   ? 6.522     -6.597    0.414     1.000 51.44600  ? 705 HOH   A O   1 
HETATM 1964 O O   . HOH   C 3 .   ? -6.66957  -26.90179 -23.29774 1.000 43.13093  ? 706 HOH   A O   1 
HETATM 1965 O O   . HOH   C 3 .   ? 11.12066  -29.71952 -19.09297 1.000 50.09946  ? 707 HOH   A O   1 
HETATM 1966 O O   . HOH   C 3 .   ? -21.18566 -4.33779  -29.07876 1.000 50.34367  ? 708 HOH   A O   1 
HETATM 1967 O O   . HOH   C 3 .   ? 1.67855   -5.74491  -36.52174 1.000 42.94006  ? 709 HOH   A O   1 
HETATM 1968 O O   . HOH   C 3 .   ? 9.69024   -25.23726 -14.86383 1.000 47.10384  ? 710 HOH   A O   1 
HETATM 1969 O O   . HOH   C 3 .   ? 11.371    -30.216   -34.416   1.000 36.54010  ? 711 HOH   A O   1 
HETATM 1970 O O   . HOH   C 3 .   ? 12.88186  -25.14809 -15.80767 1.000 37.56395  ? 712 HOH   A O   1 
HETATM 1971 O O   . HOH   C 3 .   ? -4.22558  -28.12960 -23.51869 1.000 37.96553  ? 713 HOH   A O   1 
HETATM 1972 O O   . HOH   C 3 .   ? -16.32873 -12.52094 -6.12649  1.000 39.72794  ? 714 HOH   A O   1 
HETATM 1973 O O   . HOH   C 3 .   ? 20.74890  -7.32664  -15.97550 1.000 46.36964  ? 715 HOH   A O   1 
HETATM 1974 O O   . HOH   C 3 .   ? 14.37377  -28.49187 -23.74292 1.000 45.27451  ? 716 HOH   A O   1 
HETATM 1975 O O   . HOH   C 3 .   ? -16.15188 -13.52699 -3.64696  1.000 39.05582  ? 717 HOH   A O   1 
HETATM 1976 O O   . HOH   C 3 .   ? -9.124    -28.533   -24.808   1.000 42.23616  ? 718 HOH   A O   1 
HETATM 1977 O O   . HOH   C 3 .   ? 4.111     -2.008    -28.254   1.000 35.85660  ? 719 HOH   A O   1 
HETATM 1978 O O   . HOH   C 3 .   ? -19.05866 -4.51170  -18.96083 1.000 48.50329  ? 720 HOH   A O   1 
HETATM 1979 O O   . HOH   C 3 .   ? -12.37288 -13.13946 -0.95059  1.000 24.57004  ? 721 HOH   A O   1 
HETATM 1980 O O   . HOH   C 3 .   ? -3.111    2.094     -20.451   1.000 42.31670  ? 722 HOH   A O   1 
HETATM 1981 O O   . HOH   C 3 .   ? 0.56293   -1.43671  -16.74915 1.000 36.32169  ? 723 HOH   A O   1 
HETATM 1982 O O   . HOH   C 3 .   ? -19.94125 -6.19314  -17.52842 1.000 51.85149  ? 724 HOH   A O   1 
HETATM 1983 O O   . HOH   C 3 .   ? 13.64566  -11.54925 -5.15159  1.000 28.06028  ? 725 HOH   A O   1 
HETATM 1984 O O   . HOH   C 3 .   ? 14.938    -16.980   0.306     1.000 36.91049  ? 726 HOH   A O   1 
HETATM 1985 O O   . HOH   C 3 .   ? 19.34714  -20.53957 -22.31718 1.000 37.39984  ? 727 HOH   A O   1 
HETATM 1986 O O   . HOH   C 3 .   ? 14.46379  -13.04497 -2.89607  1.000 38.54877  ? 728 HOH   A O   1 
HETATM 1987 O O   . HOH   C 3 .   ? 22.04740  -17.99714 -25.09677 1.000 41.44333  ? 729 HOH   A O   1 
HETATM 1988 O O   . HOH   C 3 .   ? -14.58132 -14.13922 -10.22616 1.000 28.43534  ? 730 HOH   A O   1 
HETATM 1989 O O   . HOH   C 3 .   ? -16.91925 -15.45050 -10.37132 1.000 32.08929  ? 731 HOH   A O   1 
HETATM 1990 O O   . HOH   C 3 .   ? -10.349   -11.824   2.027     1.000 31.75563  ? 732 HOH   A O   1 
HETATM 1991 O O   . HOH   C 3 .   ? -14.79180 -9.58038  -11.29994 1.000 36.04205  ? 733 HOH   A O   1 
HETATM 1992 O O   . HOH   C 3 .   ? 9.75328   -12.69242 -37.15824 1.000 46.24345  ? 734 HOH   A O   1 
HETATM 1993 O O   . HOH   C 3 .   ? -12.24889 -20.53294 -25.37846 1.000 46.70697  ? 735 HOH   A O   1 
HETATM 1994 O O   . HOH   C 3 .   ? 20.83352  -20.34770 -26.69579 1.000 43.15720  ? 736 HOH   A O   1 
HETATM 1995 O O   . HOH   C 3 .   ? -8.73337  -10.79840 0.04838   1.000 46.28445  ? 737 HOH   A O   1 
HETATM 1996 O O   . HOH   C 3 .   ? 9.93249   -25.45994 -6.68393  1.000 51.92118  ? 738 HOH   A O   1 
HETATM 1997 O O   . HOH   C 3 .   ? -19.63242 -5.75507  -21.48001 1.000 41.86671  ? 739 HOH   A O   1 
HETATM 1998 O O   . HOH   C 3 .   ? -18.20883 -1.48074  -30.35406 1.000 51.27139  ? 740 HOH   A O   1 
HETATM 1999 O O   . HOH   C 3 .   ? -16.83081 -9.50008  -6.03621  1.000 49.73671  ? 741 HOH   A O   1 
HETATM 2000 O O   . HOH   C 3 .   ? -20.67093 -10.12050 -19.75485 1.000 44.86563  ? 742 HOH   A O   1 
HETATM 2001 O O   . HOH   C 3 .   ? 17.52401  -4.64714  -28.21646 1.000 44.67457  ? 743 HOH   A O   1 
HETATM 2002 O O   . HOH   C 3 .   ? -9.29271  -32.88023 -8.79084  1.000 47.31300  ? 744 HOH   A O   1 
HETATM 2003 O O   . HOH   C 3 .   ? 25.36189  -15.05019 -23.43487 1.000 42.48497  ? 745 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   ? 0.46128 0.55053 0.42346 -0.01277 -0.03815 -0.19268 16  GLU A N   
2    C CA  . GLU A 9   ? 0.66567 0.73762 0.61807 0.00745  -0.03651 -0.18060 16  GLU A CA  
3    C C   . GLU A 9   ? 0.49121 0.56476 0.45317 0.01394  -0.03711 -0.16740 16  GLU A C   
4    O O   . GLU A 9   ? 0.48948 0.59425 0.45786 0.01987  -0.04260 -0.16273 16  GLU A O   
5    C CB  . GLU A 9   ? 0.75739 0.85296 0.69940 0.02591  -0.04140 -0.17902 16  GLU A CB  
6    C CG  . GLU A 9   ? 0.90995 0.97986 0.83799 0.04337  -0.03653 -0.17003 16  GLU A CG  
7    C CD  . GLU A 9   ? 1.02413 1.09430 0.95426 0.06048  -0.03571 -0.15292 16  GLU A CD  
8    O OE1 . GLU A 9   ? 0.89065 0.94346 0.81181 0.07515  -0.03078 -0.14303 16  GLU A OE1 
9    O OE2 . GLU A 9   ? 0.96382 1.05074 0.90446 0.05869  -0.03887 -0.14875 16  GLU A OE2 
10   N N   . VAL A 10  ? 0.33769 0.37746 0.30000 0.01420  -0.03072 -0.16111 17  VAL A N   
11   C CA  . VAL A 10  ? 0.25724 0.29387 0.23076 0.01627  -0.02953 -0.14505 17  VAL A CA  
12   C C   . VAL A 10  ? 0.33278 0.35201 0.30136 0.03360  -0.02542 -0.12825 17  VAL A C   
13   O O   . VAL A 10  ? 0.35235 0.34527 0.31430 0.03702  -0.01936 -0.12625 17  VAL A O   
14   C CB  . VAL A 10  ? 0.38600 0.39993 0.36903 -0.00076 -0.02327 -0.14397 17  VAL A CB  
15   C CG1 . VAL A 10  ? 0.35409 0.36517 0.34694 0.00287  -0.02204 -0.12589 17  VAL A CG1 
16   C CG2 . VAL A 10  ? 0.47940 0.50960 0.46873 -0.02074 -0.02527 -0.16174 17  VAL A CG2 
17   N N   . GLU A 11  ? 0.24371 0.27711 0.21546 0.04401  -0.02743 -0.11657 18  GLU A N   
18   C CA  . GLU A 11  ? 0.23583 0.25537 0.20555 0.05724  -0.02251 -0.10149 18  GLU A CA  
19   C C   . GLU A 11  ? 0.22113 0.23102 0.20298 0.05106  -0.01990 -0.08975 18  GLU A C   
20   O O   . GLU A 11  ? 0.20913 0.23220 0.19864 0.04429  -0.02296 -0.08913 18  GLU A O   
21   C CB  . GLU A 11  ? 0.27213 0.30992 0.23477 0.07276  -0.02375 -0.09707 18  GLU A CB  
22   C CG  . GLU A 11  ? 0.27856 0.32583 0.22640 0.08327  -0.02548 -0.10621 18  GLU A CG  
23   C CD  . GLU A 11  ? 0.47496 0.54020 0.41413 0.10064  -0.02507 -0.09941 18  GLU A CD  
24   O OE1 . GLU A 11  ? 0.41517 0.50549 0.35605 0.10146  -0.02974 -0.10156 18  GLU A OE1 
25   O OE2 . GLU A 11  ? 0.48514 0.53835 0.41790 0.11123  -0.01922 -0.08775 18  GLU A OE2 
26   N N   . THR A 12  ? 0.20590 0.19540 0.18913 0.05395  -0.01428 -0.08078 19  THR A N   
27   C CA  . THR A 12  ? 0.19438 0.17854 0.18793 0.04983  -0.01220 -0.06974 19  THR A CA  
28   C C   . THR A 12  ? 0.21558 0.20284 0.21091 0.05922  -0.00959 -0.05918 19  THR A C   
29   O O   . THR A 12  ? 0.19007 0.17105 0.18007 0.06870  -0.00573 -0.05687 19  THR A O   
30   C CB  . THR A 12  ? 0.22666 0.18938 0.22109 0.04627  -0.00706 -0.06710 19  THR A CB  
31   O OG1 . THR A 12  ? 0.23106 0.18642 0.22249 0.03563  -0.00684 -0.07862 19  THR A OG1 
32   C CG2 . THR A 12  ? 0.24476 0.20726 0.24883 0.04355  -0.00568 -0.05548 19  THR A CG2 
33   N N   . PHE A 13  ? 0.17518 0.17132 0.17783 0.05556  -0.01065 -0.05349 20  PHE A N   
34   C CA  . PHE A 13  ? 0.18405 0.18357 0.18869 0.06065  -0.00713 -0.04603 20  PHE A CA  
35   C C   . PHE A 13  ? 0.21735 0.21826 0.23230 0.05414  -0.00669 -0.03901 20  PHE A C   
36   O O   . PHE A 13  ? 0.20047 0.20345 0.21967 0.04657  -0.00984 -0.03915 20  PHE A O   
37   C CB  . PHE A 13  ? 0.18313 0.19301 0.18365 0.06310  -0.00751 -0.04730 20  PHE A CB  
38   C CG  . PHE A 13  ? 0.21573 0.23094 0.20477 0.07262  -0.00817 -0.05306 20  PHE A CG  
39   C CD1 . PHE A 13  ? 0.21533 0.24200 0.20232 0.06937  -0.01443 -0.06204 20  PHE A CD1 
40   C CD2 . PHE A 13  ? 0.23081 0.24197 0.21094 0.08497  -0.00189 -0.04959 20  PHE A CD2 
41   C CE1 . PHE A 13  ? 0.23061 0.26870 0.20675 0.07906  -0.01608 -0.06807 20  PHE A CE1 
42   C CE2 . PHE A 13  ? 0.27977 0.29856 0.24715 0.09629  -0.00240 -0.05371 20  PHE A CE2 
43   C CZ  . PHE A 13  ? 0.23396 0.26842 0.19927 0.09398  -0.01034 -0.06346 20  PHE A CZ  
44   N N   . ALA A 14  ? 0.19222 0.19442 0.21121 0.05692  -0.00238 -0.03320 21  ALA A N   
45   C CA  . ALA A 14  ? 0.16864 0.17931 0.19721 0.05063  -0.00271 -0.02810 21  ALA A CA  
46   C C   . ALA A 14  ? 0.22251 0.23923 0.25107 0.04552  -0.00206 -0.02951 21  ALA A C   
47   O O   . ALA A 14  ? 0.19304 0.20596 0.21590 0.04943  0.00285  -0.03084 21  ALA A O   
48   C CB  . ALA A 14  ? 0.18401 0.19872 0.21888 0.05415  0.00169  -0.02278 21  ALA A CB  
49   N N   . PHE A 15  ? 0.14503 0.16919 0.17809 0.03792  -0.00557 -0.02871 22  PHE A N   
50   C CA  . PHE A 15  ? 0.16590 0.19413 0.19832 0.03274  -0.00335 -0.03014 22  PHE A CA  
51   C C   . PHE A 15  ? 0.17070 0.20161 0.20755 0.03065  0.00279  -0.02929 22  PHE A C   
52   O O   . PHE A 15  ? 0.18208 0.22099 0.22690 0.03067  0.00247  -0.02632 22  PHE A O   
53   C CB  . PHE A 15  ? 0.14957 0.18676 0.18568 0.02511  -0.00794 -0.02940 22  PHE A CB  
54   C CG  . PHE A 15  ? 0.14329 0.17900 0.17588 0.02451  -0.01191 -0.03098 22  PHE A CG  
55   C CD1 . PHE A 15  ? 0.16392 0.19833 0.18994 0.02626  -0.01064 -0.03442 22  PHE A CD1 
56   C CD2 . PHE A 15  ? 0.12395 0.15996 0.15969 0.02279  -0.01543 -0.02863 22  PHE A CD2 
57   C CE1 . PHE A 15  ? 0.13745 0.17615 0.16253 0.02491  -0.01425 -0.03648 22  PHE A CE1 
58   C CE2 . PHE A 15  ? 0.12480 0.16026 0.15901 0.01985  -0.01762 -0.03109 22  PHE A CE2 
59   C CZ  . PHE A 15  ? 0.15863 0.19811 0.18880 0.02021  -0.01778 -0.03549 22  PHE A CZ  
60   N N   . GLN A 16  ? 0.16448 0.18896 0.19604 0.02885  0.00972  -0.03189 23  GLN A N   
61   C CA  . GLN A 16  ? 0.22600 0.25417 0.26328 0.02120  0.01654  -0.03336 23  GLN A CA  
62   C C   . GLN A 16  ? 0.17099 0.21832 0.21806 0.01126  0.01049  -0.03431 23  GLN A C   
63   O O   . GLN A 16  ? 0.17462 0.22634 0.21988 0.00921  0.00415  -0.03433 23  GLN A O   
64   C CB  . GLN A 16  ? 0.22255 0.23598 0.25021 0.01910  0.02697  -0.03663 23  GLN A CB  
65   C CG  . GLN A 16  ? 0.31101 0.30741 0.32730 0.03136  0.03503  -0.03426 23  GLN A CG  
66   C CD  . GLN A 16  ? 0.45329 0.43204 0.45681 0.03230  0.04716  -0.03559 23  GLN A CD  
67   O OE1 . GLN A 16  ? 0.43254 0.40686 0.42559 0.03988  0.04612  -0.03470 23  GLN A OE1 
68   N NE2 . GLN A 16  ? 0.43873 0.40710 0.44277 0.02479  0.06018  -0.03770 23  GLN A NE2 
69   N N   . ALA A 17  ? 0.19844 0.26017 0.25603 0.00556  0.01277  -0.03504 24  ALA A N   
70   C CA  . ALA A 17  ? 0.20202 0.28909 0.26907 -0.00118 0.00591  -0.03535 24  ALA A CA  
71   C C   . ALA A 17  ? 0.18202 0.27113 0.24421 -0.01043 0.00420  -0.04079 24  ALA A C   
72   O O   . ALA A 17  ? 0.17871 0.28164 0.24191 -0.01057 -0.00378 -0.03874 24  ALA A O   
73   C CB  . ALA A 17  ? 0.20120 0.30894 0.28116 -0.00769 0.00958  -0.03754 24  ALA A CB  
74   N N   . GLU A 18  ? 0.20226 0.27558 0.25731 -0.01702 0.01310  -0.04714 25  GLU A N   
75   C CA  . GLU A 18  ? 0.25901 0.33169 0.30755 -0.02578 0.01328  -0.05317 25  GLU A CA  
76   C C   . GLU A 18  ? 0.22222 0.28792 0.26227 -0.01823 0.00706  -0.04892 25  GLU A C   
77   O O   . GLU A 18  ? 0.19159 0.26644 0.22939 -0.02305 0.00262  -0.05095 25  GLU A O   
78   C CB  . GLU A 18  ? 0.33250 0.38332 0.37245 -0.03282 0.02739  -0.06023 25  GLU A CB  
79   C CG  . GLU A 18  ? 0.34763 0.40470 0.39674 -0.04485 0.03626  -0.06673 25  GLU A CG  
80   C CD  . GLU A 18  ? 0.44409 0.49403 0.49777 -0.03703 0.04213  -0.06124 25  GLU A CD  
81   O OE1 . GLU A 18  ? 0.30846 0.34931 0.35769 -0.02186 0.03850  -0.05295 25  GLU A OE1 
82   O OE2 . GLU A 18  ? 0.54495 0.59955 0.60687 -0.04707 0.05101  -0.06614 25  GLU A OE2 
83   N N   . ILE A 19  ? 0.21285 0.26478 0.24832 -0.00704 0.00690  -0.04378 26  ILE A N   
84   C CA  . ILE A 19  ? 0.18283 0.23191 0.21271 -0.00166 0.00146  -0.04084 26  ILE A CA  
85   C C   . ILE A 19  ? 0.19244 0.25610 0.22946 -0.00044 -0.00785 -0.03589 26  ILE A C   
86   O O   . ILE A 19  ? 0.15320 0.22116 0.18801 -0.00148 -0.01195 -0.03448 26  ILE A O   
87   C CB  . ILE A 19  ? 0.20750 0.24208 0.23036 0.00885  0.00424  -0.03891 26  ILE A CB  
88   C CG1 . ILE A 19  ? 0.25156 0.27024 0.26252 0.01139  0.01468  -0.04150 26  ILE A CG1 
89   C CG2 . ILE A 19  ? 0.19217 0.23069 0.21415 0.01277  -0.00278 -0.03661 26  ILE A CG2 
90   C CD1 . ILE A 19  ? 0.30179 0.31031 0.31140 0.00602  0.02569  -0.04484 26  ILE A CD1 
91   N N   . ALA A 20  ? 0.14289 0.21311 0.18748 0.00281  -0.00971 -0.03233 27  ALA A N   
92   C CA  . ALA A 20  ? 0.15172 0.23357 0.20097 0.00583  -0.01580 -0.02624 27  ALA A CA  
93   C C   . ALA A 20  ? 0.12018 0.22147 0.17107 -0.00017 -0.01920 -0.02688 27  ALA A C   
94   O O   . ALA A 20  ? 0.19568 0.30221 0.24457 0.00210  -0.02308 -0.02213 27  ALA A O   
95   C CB  . ALA A 20  ? 0.15482 0.24099 0.21068 0.01196  -0.01526 -0.02197 27  ALA A CB  
96   N N   . GLN A 21  ? 0.19665 0.30867 0.25033 -0.00839 -0.01686 -0.03342 28  GLN A N   
97   C CA  . GLN A 21  ? 0.17160 0.30603 0.22620 -0.01526 -0.02059 -0.03655 28  GLN A CA  
98   C C   . GLN A 21  ? 0.18686 0.31249 0.23119 -0.01848 -0.02077 -0.03913 28  GLN A C   
99   O O   . GLN A 21  ? 0.20873 0.34843 0.25071 -0.01780 -0.02570 -0.03649 28  GLN A O   
100  C CB  . GLN A 21  ? 0.20638 0.35399 0.26706 -0.02641 -0.01674 -0.04587 28  GLN A CB  
101  C CG  . GLN A 21  ? 0.43748 0.61563 0.50073 -0.03528 -0.02129 -0.05192 28  GLN A CG  
102  C CD  . GLN A 21  ? 0.62799 0.81677 0.69770 -0.05048 -0.01550 -0.06446 28  GLN A CD  
103  O OE1 . GLN A 21  ? 0.56593 0.77791 0.63661 -0.06186 -0.01770 -0.07391 28  GLN A OE1 
104  N NE2 . GLN A 21  ? 0.48307 0.65432 0.55650 -0.05146 -0.00706 -0.06537 28  GLN A NE2 
105  N N   . LEU A 22  ? 0.15885 0.26197 0.19596 -0.02000 -0.01468 -0.04318 29  LEU A N   
106  C CA  . LEU A 22  ? 0.19057 0.28510 0.21774 -0.02062 -0.01389 -0.04436 29  LEU A CA  
107  C C   . LEU A 22  ? 0.24156 0.33813 0.26892 -0.01350 -0.01930 -0.03592 29  LEU A C   
108  O O   . LEU A 22  ? 0.19008 0.29384 0.21307 -0.01452 -0.02165 -0.03457 29  LEU A O   
109  C CB  . LEU A 22  ? 0.21549 0.28671 0.23463 -0.01865 -0.00571 -0.04737 29  LEU A CB  
110  C CG  . LEU A 22  ? 0.21917 0.28311 0.22864 -0.01607 -0.00445 -0.04684 29  LEU A CG  
111  C CD1 . LEU A 22  ? 0.26653 0.33400 0.26849 -0.02445 -0.00211 -0.05342 29  LEU A CD1 
112  C CD2 . LEU A 22  ? 0.30663 0.35246 0.30881 -0.00859 0.00254  -0.04649 29  LEU A CD2 
113  N N   . MET A 23  ? 0.13872 0.22774 0.17034 -0.00683 -0.02012 -0.03067 30  MET A N   
114  C CA  . MET A 23  ? 0.15984 0.24697 0.19151 -0.00261 -0.02267 -0.02418 30  MET A CA  
115  C C   . MET A 23  ? 0.19026 0.29149 0.22361 -0.00050 -0.02608 -0.01754 30  MET A C   
116  O O   . MET A 23  ? 0.17035 0.27247 0.20026 0.00056  -0.02646 -0.01300 30  MET A O   
117  C CB  . MET A 23  ? 0.13553 0.21032 0.17020 0.00221  -0.02187 -0.02226 30  MET A CB  
118  C CG  . MET A 23  ? 0.14172 0.20633 0.17295 0.00328  -0.01892 -0.02762 30  MET A CG  
119  S SD  . MET A 23  ? 0.18215 0.23679 0.21546 0.00894  -0.01849 -0.02834 30  MET A SD  
120  C CE  . MET A 23  ? 0.19646 0.24995 0.23224 0.00685  -0.02049 -0.02588 30  MET A CE  
121  N N   . SER A 24  ? 0.18269 0.29644 0.22101 0.00157  -0.02777 -0.01588 31  SER A N   
122  C CA  . SER A 24  ? 0.15224 0.28284 0.19042 0.00708  -0.03060 -0.00801 31  SER A CA  
123  C C   . SER A 24  ? 0.19843 0.34640 0.23114 0.00252  -0.03334 -0.01109 31  SER A C   
124  O O   . SER A 24  ? 0.20594 0.36130 0.23377 0.00791  -0.03439 -0.00368 31  SER A O   
125  C CB  . SER A 24  ? 0.28163 0.42669 0.32682 0.01242  -0.03175 -0.00491 31  SER A CB  
126  O OG  . SER A 24  ? 0.49729 0.66365 0.54687 0.00510  -0.03391 -0.01299 31  SER A OG  
127  N N   . LEU A 25  ? 0.16056 0.31213 0.19202 -0.00715 -0.03301 -0.02203 32  LEU A N   
128  C CA  . LEU A 25  ? 0.15931 0.32382 0.18315 -0.01250 -0.03472 -0.02696 32  LEU A CA  
129  C C   . LEU A 25  ? 0.25517 0.40596 0.27090 -0.00995 -0.03280 -0.02270 32  LEU A C   
130  O O   . LEU A 25  ? 0.18560 0.34827 0.19484 -0.00739 -0.03472 -0.01896 32  LEU A O   
131  C CB  . LEU A 25  ? 0.24960 0.41201 0.27182 -0.02461 -0.03151 -0.04078 32  LEU A CB  
132  C CG  . LEU A 25  ? 0.36436 0.53574 0.37681 -0.03326 -0.03134 -0.05029 32  LEU A CG  
133  C CD1 . LEU A 25  ? 0.53429 0.70570 0.54793 -0.04668 -0.02668 -0.06455 32  LEU A CD1 
134  C CD2 . LEU A 25  ? 0.32453 0.47541 0.32568 -0.03185 -0.02719 -0.04967 32  LEU A CD2 
135  N N   . ILE A 26  ? 0.18167 0.31028 0.19762 -0.01015 -0.02875 -0.02330 33  ILE A N   
136  C CA  . ILE A 26  ? 0.20346 0.32277 0.21422 -0.00858 -0.02643 -0.01995 33  ILE A CA  
137  C C   . ILE A 26  ? 0.24811 0.36941 0.26018 -0.00218 -0.02688 -0.00874 33  ILE A C   
138  O O   . ILE A 26  ? 0.21988 0.34370 0.22624 -0.00085 -0.02552 -0.00445 33  ILE A O   
139  C CB  . ILE A 26  ? 0.15300 0.25478 0.16542 -0.00882 -0.02267 -0.02291 33  ILE A CB  
140  C CG1 . ILE A 26  ? 0.19179 0.28766 0.19772 -0.01297 -0.01883 -0.03204 33  ILE A CG1 
141  C CG2 . ILE A 26  ? 0.17347 0.27100 0.18504 -0.00698 -0.02069 -0.01830 33  ILE A CG2 
142  C CD1 . ILE A 26  ? 0.20789 0.28893 0.21431 -0.01011 -0.01457 -0.03444 33  ILE A CD1 
143  N N   . ILE A 27  ? 0.17508 0.29310 0.19332 0.00246  -0.02709 -0.00339 34  ILE A N   
144  C CA  . ILE A 27  ? 0.20509 0.31754 0.22280 0.00898  -0.02414 0.00764  34  ILE A CA  
145  C C   . ILE A 27  ? 0.27605 0.40682 0.28770 0.01620  -0.02570 0.01543  34  ILE A C   
146  O O   . ILE A 27  ? 0.30559 0.43297 0.31159 0.02132  -0.02158 0.02467  34  ILE A O   
147  C CB  . ILE A 27  ? 0.26920 0.36832 0.29297 0.01235  -0.02210 0.01012  34  ILE A CB  
148  C CG1 . ILE A 27  ? 0.27014 0.35279 0.29788 0.00644  -0.02009 0.00351  34  ILE A CG1 
149  C CG2 . ILE A 27  ? 0.30561 0.39771 0.32637 0.02106  -0.01702 0.02239  34  ILE A CG2 
150  C CD1 . ILE A 27  ? 0.24314 0.31487 0.27553 0.00864  -0.01937 0.00192  34  ILE A CD1 
151  N N   . ASN A 28  ? 0.23802 0.39045 0.25054 0.01685  -0.03103 0.01176  35  ASN A N   
152  C CA  . ASN A 28  ? 0.25654 0.43315 0.26416 0.02636  -0.03355 0.01960  35  ASN A CA  
153  C C   . ASN A 28  ? 0.32722 0.52582 0.32652 0.02329  -0.03761 0.01466  35  ASN A C   
154  O O   . ASN A 28  ? 0.34199 0.56035 0.33402 0.03322  -0.03897 0.02290  35  ASN A O   
155  C CB  . ASN A 28  ? 0.31242 0.50760 0.32738 0.03021  -0.03730 0.01905  35  ASN A CB  
156  C CG  . ASN A 28  ? 0.33964 0.51483 0.35950 0.03717  -0.03247 0.02643  35  ASN A CG  
157  O OD1 . ASN A 28  ? 0.34461 0.49849 0.35985 0.04342  -0.02592 0.03597  35  ASN A OD1 
158  N ND2 . ASN A 28  ? 0.44347 0.62330 0.47214 0.03523  -0.03431 0.02139  35  ASN A ND2 
159  N N   . THR A 29  ? 0.23142 0.42714 0.22967 0.01126  -0.03876 0.00173  36  THR A N   
160  C CA  . THR A 29  ? 0.23865 0.45387 0.22714 0.00750  -0.04192 -0.00488 36  THR A CA  
161  C C   . THR A 29  ? 0.25563 0.46421 0.23353 0.01360  -0.03827 0.00386  36  THR A C   
162  O O   . THR A 29  ? 0.25857 0.44279 0.23747 0.01221  -0.03263 0.00683  36  THR A O   
163  C CB  . THR A 29  ? 0.25533 0.46271 0.24309 -0.00666 -0.04108 -0.02106 36  THR A CB  
164  O OG1 . THR A 29  ? 0.22214 0.43585 0.21957 -0.01304 -0.04277 -0.02899 36  THR A OG1 
165  C CG2 . THR A 29  ? 0.33323 0.55643 0.30851 -0.01177 -0.04289 -0.02974 36  THR A CG2 
166  N N   . PHE A 30  ? 0.23248 0.46549 0.20024 0.02044  -0.04123 0.00769  37  PHE A N   
167  C CA  . PHE A 30  ? 0.24334 0.47094 0.19928 0.02538  -0.03693 0.01465  37  PHE A CA  
168  C C   . PHE A 30  ? 0.27422 0.49250 0.22471 0.01401  -0.03564 0.00193  37  PHE A C   
169  O O   . PHE A 30  ? 0.24041 0.47362 0.18566 0.00627  -0.03985 -0.01154 37  PHE A O   
170  C CB  . PHE A 30  ? 0.21910 0.47678 0.16294 0.03750  -0.04015 0.02211  37  PHE A CB  
171  C CG  . PHE A 30  ? 0.22686 0.47830 0.15730 0.04370  -0.03443 0.03038  37  PHE A CG  
172  C CD1 . PHE A 30  ? 0.34003 0.56839 0.27052 0.05179  -0.02479 0.04616  37  PHE A CD1 
173  C CD2 . PHE A 30  ? 0.25191 0.51920 0.16920 0.04044  -0.03738 0.02158  37  PHE A CD2 
174  C CE1 . PHE A 30  ? 0.29760 0.51968 0.21674 0.05662  -0.01784 0.05407  37  PHE A CE1 
175  C CE2 . PHE A 30  ? 0.32970 0.59092 0.23415 0.04686  -0.03124 0.02971  37  PHE A CE2 
176  C CZ  . PHE A 30  ? 0.24995 0.48960 0.15586 0.05523  -0.02140 0.04658  37  PHE A CZ  
177  N N   . TYR A 31  ? 0.20037 0.39464 0.15163 0.01297  -0.02882 0.00581  38  TYR A N   
178  C CA  . TYR A 31  ? 0.19148 0.37490 0.13758 0.00496  -0.02594 -0.00447 38  TYR A CA  
179  C C   . TYR A 31  ? 0.21508 0.38312 0.16107 0.00824  -0.01849 0.00449  38  TYR A C   
180  O O   . TYR A 31  ? 0.22712 0.38048 0.18453 0.00736  -0.01521 0.00874  38  TYR A O   
181  C CB  . TYR A 31  ? 0.23845 0.40946 0.19291 -0.00405 -0.02620 -0.01565 38  TYR A CB  
182  C CG  . TYR A 31  ? 0.28352 0.43825 0.23241 -0.00879 -0.02059 -0.02322 38  TYR A CG  
183  C CD1 . TYR A 31  ? 0.28596 0.44334 0.22114 -0.01379 -0.01928 -0.03431 38  TYR A CD1 
184  C CD2 . TYR A 31  ? 0.29292 0.43070 0.24919 -0.00758 -0.01591 -0.01962 38  TYR A CD2 
185  C CE1 . TYR A 31  ? 0.38143 0.52092 0.30907 -0.01554 -0.01196 -0.03984 38  TYR A CE1 
186  C CE2 . TYR A 31  ? 0.31799 0.44388 0.26822 -0.00861 -0.01009 -0.02486 38  TYR A CE2 
187  C CZ  . TYR A 31  ? 0.36690 0.49177 0.30232 -0.01164 -0.00746 -0.03405 38  TYR A CZ  
188  O OH  . TYR A 31  ? 0.52491 0.63515 0.45243 -0.01019 0.00031  -0.03784 38  TYR A OH  
189  N N   . SER A 32  ? 0.20446 0.37799 0.13783 0.01153  -0.01557 0.00674  39  SER A N   
190  C CA  . SER A 32  ? 0.20811 0.37215 0.14240 0.01545  -0.00768 0.01757  39  SER A CA  
191  C C   . SER A 32  ? 0.20709 0.35781 0.14695 0.01005  -0.00282 0.01258  39  SER A C   
192  O O   . SER A 32  ? 0.24432 0.38842 0.19239 0.01029  0.00320  0.02001  39  SER A O   
193  C CB  . SER A 32  ? 0.22519 0.40129 0.14319 0.02282  -0.00532 0.02350  39  SER A CB  
194  O OG  . SER A 32  ? 0.23911 0.42976 0.15216 0.03143  -0.00862 0.03163  39  SER A OG  
195  N N   . ASN A 33  ? 0.22136 0.36877 0.15671 0.00551  -0.00417 0.00030  40  ASN A N   
196  C CA  . ASN A 33  ? 0.20144 0.33903 0.13772 0.00447  0.00159  -0.00321 40  ASN A CA  
197  C C   . ASN A 33  ? 0.18165 0.31106 0.13394 0.00190  0.00135  -0.00386 40  ASN A C   
198  O O   . ASN A 33  ? 0.22628 0.34787 0.17844 0.00056  0.00198  -0.01160 40  ASN A O   
199  C CB  . ASN A 33  ? 0.27138 0.40465 0.19250 0.00246  0.00283  -0.01530 40  ASN A CB  
200  C CG  . ASN A 33  ? 0.29832 0.42100 0.21612 0.00513  0.01057  -0.01763 40  ASN A CG  
201  O OD1 . ASN A 33  ? 0.31287 0.43930 0.23551 0.00947  0.01502  -0.00983 40  ASN A OD1 
202  N ND2 . ASN A 33  ? 0.32275 0.43262 0.23154 0.00298  0.01354  -0.02827 40  ASN A ND2 
203  N N   . LYS A 34  ? 0.21078 0.21392 0.15010 0.02306  -0.01210 -0.01352 41  LYS A N   
204  C CA  . LYS A 34  ? 0.18679 0.20742 0.14973 0.02290  -0.00675 -0.01282 41  LYS A CA  
205  C C   . LYS A 34  ? 0.17993 0.19049 0.14552 0.02243  0.00120  -0.01714 41  LYS A C   
206  O O   . LYS A 34  ? 0.19171 0.21300 0.17257 0.02001  0.00258  -0.01755 41  LYS A O   
207  C CB  . LYS A 34  ? 0.18608 0.21455 0.15713 0.03202  -0.00079 -0.00992 41  LYS A CB  
208  C CG  . LYS A 34  ? 0.20816 0.25390 0.18261 0.03510  -0.00782 -0.00415 41  LYS A CG  
209  C CD  . LYS A 34  ? 0.23554 0.28131 0.21259 0.04655  -0.00159 -0.00226 41  LYS A CD  
210  C CE  . LYS A 34  ? 0.22407 0.28898 0.20533 0.05333  -0.00715 0.00432  41  LYS A CE  
211  N NZ  . LYS A 34  ? 0.20870 0.30067 0.20767 0.05436  -0.00842 0.00819  41  LYS A NZ  
212  N N   . GLU A 35  ? 0.22592 0.21750 0.17652 0.02606  0.00679  -0.01929 42  GLU A N   
213  C CA  . GLU A 35  ? 0.21387 0.20018 0.17046 0.02771  0.01560  -0.02092 42  GLU A CA  
214  C C   . GLU A 35  ? 0.25333 0.23927 0.21342 0.02118  0.01124  -0.02428 42  GLU A C   
215  O O   . GLU A 35  ? 0.24414 0.23076 0.21437 0.02192  0.01708  -0.02501 42  GLU A O   
216  C CB  . GLU A 35  ? 0.24178 0.21136 0.18051 0.03542  0.02361  -0.02022 42  GLU A CB  
217  C CG  . GLU A 35  ? 0.26774 0.21699 0.17862 0.03621  0.01759  -0.02453 42  GLU A CG  
218  C CD  . GLU A 35  ? 0.35109 0.28320 0.23871 0.04856  0.02735  -0.02315 42  GLU A CD  
219  O OE1 . GLU A 35  ? 0.44323 0.37891 0.32983 0.05423  0.03398  -0.01792 42  GLU A OE1 
220  O OE2 . GLU A 35  ? 0.52142 0.43579 0.39008 0.05392  0.02887  -0.02652 42  GLU A OE2 
221  N N   . ILE A 36  ? 0.22515 0.20948 0.17727 0.01386  -0.00008 -0.02510 43  ILE A N   
222  C CA  . ILE A 36  ? 0.19060 0.17253 0.14495 0.00628  -0.00532 -0.02680 43  ILE A CA  
223  C C   . ILE A 36  ? 0.17658 0.17942 0.15509 0.00354  -0.00263 -0.02481 43  ILE A C   
224  O O   . ILE A 36  ? 0.18026 0.18115 0.16182 -0.00138 -0.00452 -0.02573 43  ILE A O   
225  C CB  . ILE A 36  ? 0.26572 0.24144 0.20786 -0.00418 -0.02094 -0.02551 43  ILE A CB  
226  C CG1 . ILE A 36  ? 0.26081 0.26336 0.21936 -0.00956 -0.02767 -0.01848 43  ILE A CG1 
227  C CG2 . ILE A 36  ? 0.32260 0.26808 0.23193 -0.00014 -0.02538 -0.02944 43  ILE A CG2 
228  C CD1 . ILE A 36  ? 0.26885 0.29613 0.25045 -0.01795 -0.03048 -0.01261 43  ILE A CD1 
229  N N   . PHE A 37  ? 0.15205 0.17135 0.14400 0.00799  0.00145  -0.02228 44  PHE A N   
230  C CA  . PHE A 37  ? 0.17732 0.21077 0.18515 0.00841  0.00414  -0.02140 44  PHE A CA  
231  C C   . PHE A 37  ? 0.21037 0.23351 0.22082 0.00918  0.00920  -0.02490 44  PHE A C   
232  O O   . PHE A 37  ? 0.16064 0.18904 0.17807 0.00640  0.00838  -0.02506 44  PHE A O   
233  C CB  . PHE A 37  ? 0.14089 0.18392 0.15495 0.01660  0.00775  -0.01965 44  PHE A CB  
234  C CG  . PHE A 37  ? 0.17618 0.20561 0.18927 0.02184  0.01377  -0.02181 44  PHE A CG  
235  C CD1 . PHE A 37  ? 0.18324 0.20332 0.18844 0.02461  0.01616  -0.02065 44  PHE A CD1 
236  C CD2 . PHE A 37  ? 0.18847 0.21427 0.20842 0.02277  0.01593  -0.02357 44  PHE A CD2 
237  C CE1 . PHE A 37  ? 0.19383 0.20436 0.20157 0.02735  0.02156  -0.01930 44  PHE A CE1 
238  C CE2 . PHE A 37  ? 0.16424 0.17889 0.18650 0.02433  0.01890  -0.02294 44  PHE A CE2 
239  C CZ  . PHE A 37  ? 0.17402 0.18266 0.19192 0.02612  0.02212  -0.01986 44  PHE A CZ  
240  N N   . LEU A 38  ? 0.18043 0.19128 0.18653 0.01352  0.01474  -0.02608 45  LEU A N   
241  C CA  . LEU A 38  ? 0.15221 0.15869 0.16557 0.01463  0.01923  -0.02679 45  LEU A CA  
242  C C   . LEU A 38  ? 0.18287 0.18139 0.18995 0.01164  0.01710  -0.02890 45  LEU A C   
243  O O   . LEU A 38  ? 0.17039 0.17088 0.18560 0.00994  0.01684  -0.02941 45  LEU A O   
244  C CB  . LEU A 38  ? 0.15129 0.15247 0.16535 0.02002  0.02646  -0.02377 45  LEU A CB  
245  C CG  . LEU A 38  ? 0.16552 0.16828 0.19338 0.02048  0.03030  -0.02110 45  LEU A CG  
246  C CD1 . LEU A 38  ? 0.13594 0.14346 0.17592 0.01679  0.02531  -0.02175 45  LEU A CD1 
247  C CD2 . LEU A 38  ? 0.21112 0.21444 0.24333 0.02486  0.03793  -0.01411 45  LEU A CD2 
248  N N   . ARG A 39  ? 0.20665 0.19258 0.19602 0.01119  0.01399  -0.03027 46  ARG A N   
249  C CA  . ARG A 39  ? 0.18571 0.15729 0.16362 0.00843  0.00961  -0.03259 46  ARG A CA  
250  C C   . ARG A 39  ? 0.19998 0.18142 0.18730 -0.00114 0.00256  -0.03130 46  ARG A C   
251  O O   . ARG A 39  ? 0.21200 0.18790 0.20005 -0.00282 0.00166  -0.03197 46  ARG A O   
252  C CB  . ARG A 39  ? 0.25116 0.20195 0.20281 0.00844  0.00341  -0.03470 46  ARG A CB  
253  C CG  . ARG A 39  ? 0.29227 0.22213 0.22704 0.00341  -0.00556 -0.03709 46  ARG A CG  
254  C CD  . ARG A 39  ? 0.34191 0.24625 0.24644 0.00134  -0.01635 -0.03943 46  ARG A CD  
255  N NE  . ARG A 39  ? 0.42200 0.33924 0.33331 -0.01198 -0.02856 -0.03529 46  ARG A NE  
256  C CZ  . ARG A 39  ? 0.43551 0.33905 0.32713 -0.01538 -0.03930 -0.03546 46  ARG A CZ  
257  N NH1 . ARG A 39  ? 0.44804 0.32015 0.30665 -0.00545 -0.03930 -0.04092 46  ARG A NH1 
258  N NH2 . ARG A 39  ? 0.44059 0.36257 0.34473 -0.02821 -0.05075 -0.02906 46  ARG A NH2 
259  N N   . GLU A 40  ? 0.16188 0.15976 0.15669 -0.00633 -0.00177 -0.02797 47  GLU A N   
260  C CA  . GLU A 40  ? 0.18637 0.19833 0.19089 -0.01435 -0.00682 -0.02373 47  GLU A CA  
261  C C   . GLU A 40  ? 0.18923 0.21022 0.20605 -0.01028 -0.00079 -0.02421 47  GLU A C   
262  O O   . GLU A 40  ? 0.13948 0.16163 0.15860 -0.01479 -0.00303 -0.02244 47  GLU A O   
263  C CB  . GLU A 40  ? 0.14262 0.17598 0.15497 -0.01769 -0.01073 -0.01757 47  GLU A CB  
264  C CG  . GLU A 40  ? 0.21714 0.24211 0.21742 -0.02467 -0.02092 -0.01568 47  GLU A CG  
265  C CD  . GLU A 40  ? 0.31324 0.31599 0.29881 -0.03500 -0.03143 -0.01605 47  GLU A CD  
266  O OE1 . GLU A 40  ? 0.29465 0.30165 0.28726 -0.04143 -0.03331 -0.01266 47  GLU A OE1 
267  O OE2 . GLU A 40  ? 0.38726 0.36496 0.35085 -0.03588 -0.03833 -0.01975 47  GLU A OE2 
268  N N   . LEU A 41  ? 0.12098 0.14601 0.14378 -0.00239 0.00531  -0.02607 48  LEU A N   
269  C CA  . LEU A 41  ? 0.13884 0.16736 0.16916 0.00100  0.00789  -0.02700 48  LEU A CA  
270  C C   . LEU A 41  ? 0.15906 0.17538 0.18971 0.00079  0.00864  -0.02920 48  LEU A C   
271  O O   . LEU A 41  ? 0.15151 0.16889 0.18533 0.00001  0.00731  -0.02913 48  LEU A O   
272  C CB  . LEU A 41  ? 0.13504 0.16492 0.16841 0.00807  0.01085  -0.02812 48  LEU A CB  
273  C CG  . LEU A 41  ? 0.16360 0.20629 0.19595 0.01202  0.01086  -0.02555 48  LEU A CG  
274  C CD1 . LEU A 41  ? 0.14637 0.18256 0.17680 0.01982  0.01250  -0.02724 48  LEU A CD1 
275  C CD2 . LEU A 41  ? 0.14675 0.20521 0.18098 0.01272  0.01041  -0.02174 48  LEU A CD2 
276  N N   . ILE A 42  ? 0.13062 0.13622 0.15729 0.00327  0.01135  -0.03026 49  ILE A N   
277  C CA  . ILE A 42  ? 0.16028 0.15743 0.18811 0.00566  0.01313  -0.03056 49  ILE A CA  
278  C C   . ILE A 42  ? 0.19482 0.18306 0.21333 0.00128  0.00831  -0.03119 49  ILE A C   
279  O O   . ILE A 42  ? 0.17665 0.16255 0.19864 0.00168  0.00748  -0.03087 49  ILE A O   
280  C CB  . ILE A 42  ? 0.15419 0.14463 0.17866 0.01268  0.01949  -0.02951 49  ILE A CB  
281  C CG1 . ILE A 42  ? 0.13891 0.13932 0.17767 0.01475  0.02328  -0.02612 49  ILE A CG1 
282  C CG2 . ILE A 42  ? 0.19219 0.17421 0.21444 0.01808  0.02208  -0.02871 49  ILE A CG2 
283  C CD1 . ILE A 42  ? 0.18697 0.18578 0.22377 0.02181  0.03142  -0.02202 49  ILE A CD1 
284  N N   . SER A 43  ? 0.16582 0.14836 0.17245 -0.00422 0.00324  -0.03107 50  SER A N   
285  C CA  . SER A 43  ? 0.18918 0.15995 0.18597 -0.01094 -0.00379 -0.03015 50  SER A CA  
286  C C   . SER A 43  ? 0.19570 0.18168 0.20372 -0.01675 -0.00583 -0.02621 50  SER A C   
287  O O   . SER A 43  ? 0.17919 0.15715 0.18428 -0.01903 -0.00850 -0.02519 50  SER A O   
288  C CB  . SER A 43  ? 0.27205 0.23155 0.25346 -0.01809 -0.01207 -0.02942 50  SER A CB  
289  O OG  . SER A 43  ? 0.34893 0.30174 0.32508 -0.02946 -0.02186 -0.02548 50  SER A OG  
290  N N   . ASN A 44  ? 0.16397 0.17093 0.18252 -0.01714 -0.00393 -0.02351 51  ASN A N   
291  C CA  . ASN A 44  ? 0.22450 0.24578 0.25019 -0.01802 -0.00329 -0.01966 51  ASN A CA  
292  C C   . ASN A 44  ? 0.20900 0.22349 0.23651 -0.01230 -0.00114 -0.02312 51  ASN A C   
293  O O   . ASN A 44  ? 0.14759 0.16212 0.17397 -0.01431 -0.00295 -0.02064 51  ASN A O   
294  C CB  . ASN A 44  ? 0.17491 0.21648 0.20719 -0.01353 0.00030  -0.01723 51  ASN A CB  
295  C CG  . ASN A 44  ? 0.25815 0.31514 0.29351 -0.02010 -0.00276 -0.00982 51  ASN A CG  
296  O OD1 . ASN A 44  ? 0.20264 0.25375 0.23483 -0.03080 -0.00974 -0.00600 51  ASN A OD1 
297  N ND2 . ASN A 44  ? 0.21754 0.29280 0.25825 -0.01374 0.00101  -0.00710 51  ASN A ND2 
298  N N   . SER A 45  ? 0.12943 0.13968 0.16082 -0.00589 0.00189  -0.02726 52  SER A N   
299  C CA  . SER A 45  ? 0.15142 0.15719 0.18762 -0.00222 0.00144  -0.02868 52  SER A CA  
300  C C   . SER A 45  ? 0.15471 0.14912 0.18754 -0.00305 -0.00022 -0.02808 52  SER A C   
301  O O   . SER A 45  ? 0.16318 0.15588 0.19688 -0.00284 -0.00297 -0.02715 52  SER A O   
302  C CB  . SER A 45  ? 0.15594 0.16143 0.20047 0.00219  0.00366  -0.02994 52  SER A CB  
303  O OG  . SER A 45  ? 0.16207 0.17244 0.20677 0.00400  0.00339  -0.03090 52  SER A OG  
304  N N   . SER A 46  ? 0.14060 0.12418 0.16602 -0.00248 0.00088  -0.02878 53  SER A N   
305  C CA  . SER A 46  ? 0.17790 0.14543 0.19466 -0.00052 -0.00089 -0.02864 53  SER A CA  
306  C C   . SER A 46  ? 0.21880 0.18153 0.22835 -0.00845 -0.00713 -0.02604 53  SER A C   
307  O O   . SER A 46  ? 0.20441 0.15942 0.21196 -0.00673 -0.00923 -0.02495 53  SER A O   
308  C CB  . SER A 46  ? 0.17998 0.13058 0.18166 0.00344  0.00052  -0.03070 53  SER A CB  
309  O OG  . SER A 46  ? 0.22709 0.15640 0.21443 0.00780  -0.00173 -0.03116 53  SER A OG  
310  N N   . ASP A 47  ? 0.19792 0.16685 0.20472 -0.01735 -0.01028 -0.02320 54  ASP A N   
311  C CA  . ASP A 47  ? 0.18498 0.15458 0.18846 -0.02635 -0.01557 -0.01719 54  ASP A CA  
312  C C   . ASP A 47  ? 0.22471 0.20625 0.23522 -0.02322 -0.01332 -0.01527 54  ASP A C   
313  O O   . ASP A 47  ? 0.20247 0.17707 0.20794 -0.02621 -0.01668 -0.01158 54  ASP A O   
314  C CB  . ASP A 47  ? 0.18132 0.16491 0.18726 -0.03633 -0.01851 -0.01099 54  ASP A CB  
315  C CG  . ASP A 47  ? 0.33292 0.29926 0.32707 -0.04271 -0.02549 -0.01173 54  ASP A CG  
316  O OD1 . ASP A 47  ? 0.32665 0.26515 0.30515 -0.03882 -0.02814 -0.01702 54  ASP A OD1 
317  O OD2 . ASP A 47  ? 0.27560 0.25539 0.27430 -0.05110 -0.02925 -0.00612 54  ASP A OD2 
318  N N   . ALA A 48  ? 0.14168 0.13744 0.16037 -0.01689 -0.00885 -0.01777 55  ALA A N   
319  C CA  . ALA A 48  ? 0.15519 0.15671 0.17441 -0.01251 -0.00859 -0.01723 55  ALA A CA  
320  C C   . ALA A 48  ? 0.16695 0.15603 0.18685 -0.00855 -0.01160 -0.01979 55  ALA A C   
321  O O   . ALA A 48  ? 0.16473 0.15154 0.18020 -0.00784 -0.01444 -0.01766 55  ALA A O   
322  C CB  . ALA A 48  ? 0.17039 0.18202 0.19248 -0.00602 -0.00560 -0.02028 55  ALA A CB  
323  N N   . LEU A 49  ? 0.16007 0.14315 0.18595 -0.00492 -0.01063 -0.02297 56  LEU A N   
324  C CA  . LEU A 49  ? 0.16972 0.14590 0.19994 -0.00009 -0.01290 -0.02277 56  LEU A CA  
325  C C   . LEU A 49  ? 0.19057 0.15220 0.21012 -0.00117 -0.01548 -0.02039 56  LEU A C   
326  O O   . LEU A 49  ? 0.19046 0.14828 0.20999 0.00144  -0.01913 -0.01850 56  LEU A O   
327  C CB  . LEU A 49  ? 0.15500 0.13331 0.19598 0.00554  -0.00903 -0.02362 56  LEU A CB  
328  C CG  . LEU A 49  ? 0.12944 0.11909 0.18204 0.00544  -0.00920 -0.02432 56  LEU A CG  
329  C CD1 . LEU A 49  ? 0.16792 0.16169 0.22803 0.00840  -0.00305 -0.02375 56  LEU A CD1 
330  C CD2 . LEU A 49  ? 0.13020 0.12282 0.19333 0.00658  -0.01595 -0.02189 56  LEU A CD2 
331  N N   . ASP A 50  ? 0.17183 0.12237 0.18028 -0.00543 -0.01547 -0.02014 57  ASP A N   
332  C CA  . ASP A 50  ? 0.19351 0.12404 0.18744 -0.00828 -0.02045 -0.01747 57  ASP A CA  
333  C C   . ASP A 50  ? 0.22269 0.15805 0.21490 -0.01443 -0.02406 -0.01207 57  ASP A C   
334  O O   . ASP A 50  ? 0.21665 0.13884 0.20161 -0.01307 -0.02797 -0.00955 57  ASP A O   
335  C CB  . ASP A 50  ? 0.20698 0.12239 0.18683 -0.01577 -0.02380 -0.01718 57  ASP A CB  
336  C CG  . ASP A 50  ? 0.25491 0.15616 0.22662 -0.00733 -0.02103 -0.02252 57  ASP A CG  
337  O OD1 . ASP A 50  ? 0.29270 0.19747 0.27135 0.00523  -0.01490 -0.02475 57  ASP A OD1 
338  O OD2 . ASP A 50  ? 0.28012 0.16681 0.23761 -0.01354 -0.02562 -0.02317 57  ASP A OD2 
339  N N   . LYS A 51  ? 0.18226 0.13649 0.17942 -0.01946 -0.02203 -0.00942 58  LYS A N   
340  C CA  . LYS A 51  ? 0.18756 0.14832 0.18057 -0.02364 -0.02339 -0.00242 58  LYS A CA  
341  C C   . LYS A 51  ? 0.23472 0.19387 0.22700 -0.01578 -0.02490 -0.00403 58  LYS A C   
342  O O   . LYS A 51  ? 0.23746 0.18886 0.22149 -0.01722 -0.02829 0.00097  58  LYS A O   
343  C CB  . LYS A 51  ? 0.20295 0.18693 0.20046 -0.02619 -0.01864 0.00165  58  LYS A CB  
344  C CG  . LYS A 51  ? 0.20456 0.19420 0.20432 -0.03714 -0.01967 0.00767  58  LYS A CG  
345  C CD  . LYS A 51  ? 0.20954 0.22763 0.21702 -0.03590 -0.01336 0.01264  58  LYS A CD  
346  C CE  . LYS A 51  ? 0.31505 0.34293 0.32927 -0.04638 -0.01558 0.01873  58  LYS A CE  
347  N NZ  . LYS A 51  ? 0.36847 0.42877 0.39191 -0.04363 -0.00864 0.02700  58  LYS A NZ  
348  N N   . ILE A 52  ? 0.20841 0.17401 0.20855 -0.00850 -0.02398 -0.00993 59  ILE A N   
349  C CA  . ILE A 52  ? 0.20230 0.16504 0.20125 -0.00280 -0.02882 -0.01070 59  ILE A CA  
350  C C   . ILE A 52  ? 0.21630 0.16687 0.21834 0.00044  -0.03276 -0.01005 59  ILE A C   
351  O O   . ILE A 52  ? 0.23568 0.18044 0.23277 0.00289  -0.03804 -0.00745 59  ILE A O   
352  C CB  . ILE A 52  ? 0.19054 0.16012 0.19580 0.00183  -0.03035 -0.01582 59  ILE A CB  
353  C CG1 . ILE A 52  ? 0.20991 0.17376 0.20947 0.00587  -0.03891 -0.01601 59  ILE A CG1 
354  C CG2 . ILE A 52  ? 0.19524 0.16717 0.21657 0.00310  -0.02922 -0.01869 59  ILE A CG2 
355  C CD1 . ILE A 52  ? 0.28621 0.24734 0.26616 0.00720  -0.03906 -0.01265 59  ILE A CD1 
356  N N   . ARG A 53  ? 0.21478 0.16046 0.22244 0.00239  -0.02993 -0.01180 60  ARG A N   
357  C CA  . ARG A 53  ? 0.22246 0.15582 0.22967 0.00920  -0.03198 -0.01021 60  ARG A CA  
358  C C   . ARG A 53  ? 0.24593 0.16105 0.23586 0.00589  -0.03591 -0.00616 60  ARG A C   
359  O O   . ARG A 53  ? 0.25084 0.15837 0.23815 0.01119  -0.04033 -0.00334 60  ARG A O   
360  C CB  . ARG A 53  ? 0.24346 0.17191 0.25328 0.01514  -0.02656 -0.01250 60  ARG A CB  
361  C CG  . ARG A 53  ? 0.42484 0.34328 0.43424 0.02720  -0.02708 -0.00991 60  ARG A CG  
362  C CD  . ARG A 53  ? 0.53787 0.44764 0.54297 0.03752  -0.02035 -0.01143 60  ARG A CD  
363  N NE  . ARG A 53  ? 0.54223 0.47490 0.57046 0.04606  -0.01461 -0.00871 60  ARG A NE  
364  C CZ  . ARG A 53  ? 0.55702 0.49430 0.58786 0.05130  -0.00651 -0.00972 60  ARG A CZ  
365  N NH1 . ARG A 53  ? 0.49544 0.41484 0.50594 0.04867  -0.00441 -0.01504 60  ARG A NH1 
366  N NH2 . ARG A 53  ? 0.41104 0.37185 0.46559 0.05876  -0.00123 -0.00388 60  ARG A NH2 
367  N N   . TYR A 54  ? 0.22586 0.13448 0.20483 -0.00387 -0.03554 -0.00425 61  TYR A N   
368  C CA  . TYR A 54  ? 0.25102 0.14119 0.21405 -0.01001 -0.04077 0.00188  61  TYR A CA  
369  C C   . TYR A 54  ? 0.28671 0.18457 0.24786 -0.01089 -0.04301 0.00714  61  TYR A C   
370  O O   . TYR A 54  ? 0.27999 0.16237 0.23132 -0.00904 -0.04793 0.01118  61  TYR A O   
371  C CB  . TYR A 54  ? 0.25557 0.14150 0.21131 -0.02356 -0.04198 0.00583  61  TYR A CB  
372  C CG  . TYR A 54  ? 0.35334 0.21703 0.29280 -0.03259 -0.04959 0.01423  61  TYR A CG  
373  C CD1 . TYR A 54  ? 0.31638 0.14542 0.23856 -0.02918 -0.05591 0.01244  61  TYR A CD1 
374  C CD2 . TYR A 54  ? 0.32965 0.20571 0.26918 -0.04291 -0.05023 0.02491  61  TYR A CD2 
375  C CE1 . TYR A 54  ? 0.39649 0.20007 0.30139 -0.03815 -0.06479 0.02048  61  TYR A CE1 
376  C CE2 . TYR A 54  ? 0.36581 0.22150 0.29153 -0.05286 -0.05787 0.03489  61  TYR A CE2 
377  C CZ  . TYR A 54  ? 0.38212 0.20001 0.29048 -0.05144 -0.06612 0.03230  61  TYR A CZ  
378  O OH  . TYR A 54  ? 0.48287 0.27541 0.37506 -0.06217 -0.07559 0.04244  61  TYR A OH  
379  N N   . GLU A 55  ? 0.23505 0.15411 0.20211 -0.01181 -0.03961 0.00702  62  GLU A N   
380  C CA  . GLU A 55  ? 0.26317 0.18651 0.22259 -0.00993 -0.04160 0.01142  62  GLU A CA  
381  C C   . GLU A 55  ? 0.29970 0.21557 0.26040 -0.00073 -0.04790 0.00871  62  GLU A C   
382  O O   . GLU A 55  ? 0.34099 0.24869 0.29074 0.00069  -0.05246 0.01366  62  GLU A O   
383  C CB  . GLU A 55  ? 0.28493 0.22768 0.24518 -0.00826 -0.03680 0.01010  62  GLU A CB  
384  C CG  . GLU A 55  ? 0.30963 0.26582 0.27001 -0.01622 -0.03028 0.01659  62  GLU A CG  
385  C CD  . GLU A 55  ? 0.44251 0.41630 0.39646 -0.01078 -0.02442 0.01918  62  GLU A CD  
386  O OE1 . GLU A 55  ? 0.40882 0.38021 0.35733 -0.00106 -0.02646 0.01194  62  GLU A OE1 
387  O OE2 . GLU A 55  ? 0.43714 0.42693 0.39109 -0.01568 -0.01827 0.02903  62  GLU A OE2 
388  N N   . SER A 56  ? 0.27986 0.20038 0.25521 0.00527  -0.04859 0.00266  63  SER A N   
389  C CA  . SER A 56  ? 0.30597 0.22550 0.28844 0.01309  -0.05559 0.00262  63  SER A CA  
390  C C   . SER A 56  ? 0.35527 0.25887 0.33334 0.01808  -0.05814 0.00661  63  SER A C   
391  O O   . SER A 56  ? 0.31633 0.21914 0.29775 0.02467  -0.06486 0.00926  63  SER A O   
392  C CB  . SER A 56  ? 0.28584 0.21892 0.28937 0.01673  -0.05527 -0.00137 63  SER A CB  
393  O OG  . SER A 56  ? 0.29250 0.22380 0.30429 0.02056  -0.04913 -0.00184 63  SER A OG  
394  N N   . LEU A 57  ? 0.30366 0.19213 0.27242 0.01560  -0.05443 0.00733  64  LEU A N   
395  C CA  . LEU A 57  ? 0.39338 0.25989 0.35221 0.02262  -0.05762 0.01039  64  LEU A CA  
396  C C   . LEU A 57  ? 0.43642 0.29231 0.38181 0.02134  -0.06438 0.01672  64  LEU A C   
397  O O   . LEU A 57  ? 0.45796 0.30082 0.39910 0.03072  -0.06889 0.01961  64  LEU A O   
398  C CB  . LEU A 57  ? 0.34870 0.19258 0.29238 0.01855  -0.05559 0.00953  64  LEU A CB  
399  C CG  . LEU A 57  ? 0.39313 0.24200 0.34518 0.02345  -0.04909 0.00336  64  LEU A CG  
400  C CD1 . LEU A 57  ? 0.39228 0.21100 0.32261 0.02072  -0.05033 0.00195  64  LEU A CD1 
401  C CD2 . LEU A 57  ? 0.43491 0.29433 0.40232 0.03994  -0.04631 0.00279  64  LEU A CD2 
402  N N   . THR A 58  ? 0.38771 0.24916 0.32507 0.01144  -0.06438 0.02004  65  THR A N   
403  C CA  . THR A 58  ? 0.40713 0.25947 0.32952 0.01033  -0.06967 0.02738  65  THR A CA  
404  C C   . THR A 58  ? 0.47246 0.34036 0.39539 0.01326  -0.07237 0.02692  65  THR A C   
405  O O   . THR A 58  ? 0.52812 0.38824 0.43735 0.01517  -0.07762 0.03254  65  THR A O   
406  C CB  . THR A 58  ? 0.53485 0.37820 0.44248 -0.00273 -0.06778 0.03555  65  THR A CB  
407  O OG1 . THR A 58  ? 0.56115 0.42715 0.47393 -0.00955 -0.06101 0.03590  65  THR A OG1 
408  C CG2 . THR A 58  ? 0.52743 0.34762 0.42895 -0.00748 -0.06919 0.03579  65  THR A CG2 
409  N N   . ASP A 59  ? 0.46567 0.35593 0.36961 0.09833  -0.03537 0.05334  66  ASP A N   
410  C CA  . ASP A 59  ? 0.42567 0.33481 0.32753 0.09632  -0.04754 0.05317  66  ASP A CA  
411  C C   . ASP A 59  ? 0.36064 0.29632 0.28726 0.09578  -0.05495 0.04752  66  ASP A C   
412  O O   . ASP A 59  ? 0.36847 0.31158 0.30176 0.08626  -0.05301 0.03760  66  ASP A O   
413  C CB  . ASP A 59  ? 0.38976 0.29338 0.27405 0.08451  -0.04428 0.04755  66  ASP A CB  
414  C CG  . ASP A 59  ? 0.54614 0.46277 0.42152 0.08252  -0.05550 0.04619  66  ASP A CG  
415  O OD1 . ASP A 59  ? 0.52078 0.45117 0.40304 0.08848  -0.06777 0.05022  66  ASP A OD1 
416  O OD2 . ASP A 59  ? 0.53809 0.45080 0.39861 0.07491  -0.05191 0.04149  66  ASP A OD2 
417  N N   . PRO A 60  ? 0.41440 0.36583 0.35631 0.10589  -0.06344 0.05477  67  PRO A N   
418  C CA  . PRO A 60  ? 0.41962 0.39779 0.38743 0.10408  -0.06997 0.05066  67  PRO A CA  
419  C C   . PRO A 60  ? 0.35777 0.34823 0.32166 0.09218  -0.07976 0.04288  67  PRO A C   
420  O O   . PRO A 60  ? 0.34528 0.35041 0.32625 0.08608  -0.08127 0.03603  67  PRO A O   
421  C CB  . PRO A 60  ? 0.48794 0.48246 0.47117 0.11750  -0.07841 0.06317  67  PRO A CB  
422  C CG  . PRO A 60  ? 0.48679 0.45690 0.45702 0.12901  -0.06930 0.07165  67  PRO A CG  
423  C CD  . PRO A 60  ? 0.50221 0.44879 0.44174 0.12012  -0.06618 0.06824  67  PRO A CD  
424  N N   . SER A 61  ? 0.39436 0.37654 0.33372 0.08877  -0.08560 0.04367  68  SER A N   
425  C CA  . SER A 61  ? 0.39449 0.38294 0.32512 0.07823  -0.09378 0.03545  68  SER A CA  
426  C C   . SER A 61  ? 0.41239 0.39453 0.34331 0.06940  -0.08342 0.02376  68  SER A C   
427  O O   . SER A 61  ? 0.30776 0.29473 0.23596 0.06162  -0.08858 0.01600  68  SER A O   
428  C CB  . SER A 61  ? 0.41520 0.39194 0.31441 0.07729  -0.09977 0.03840  68  SER A CB  
429  O OG  . SER A 61  ? 0.44712 0.40250 0.32682 0.07651  -0.08639 0.03749  68  SER A OG  
430  N N   . LYS A 62  ? 0.32956 0.30015 0.26280 0.07013  -0.06953 0.02269  69  LYS A N   
431  C CA  . LYS A 62  ? 0.34390 0.31266 0.28134 0.06228  -0.06096 0.01336  69  LYS A CA  
432  C C   . LYS A 62  ? 0.31773 0.30289 0.27737 0.05899  -0.06498 0.00792  69  LYS A C   
433  O O   . LYS A 62  ? 0.26940 0.25500 0.23111 0.05228  -0.06134 0.00020  69  LYS A O   
434  C CB  . LYS A 62  ? 0.34456 0.30022 0.28251 0.06250  -0.04795 0.01455  69  LYS A CB  
435  C CG  . LYS A 62  ? 0.42823 0.36631 0.34391 0.06269  -0.04230 0.01972  69  LYS A CG  
436  C CD  . LYS A 62  ? 0.46806 0.40316 0.37475 0.05436  -0.03511 0.01453  69  LYS A CD  
437  C CE  . LYS A 62  ? 0.44737 0.36731 0.33333 0.05336  -0.02841 0.02071  69  LYS A CE  
438  N NZ  . LYS A 62  ? 0.46510 0.38707 0.34832 0.04565  -0.01964 0.01680  69  LYS A NZ  
439  N N   . LEU A 63  ? 0.28537 0.28478 0.26275 0.06399  -0.07166 0.01287  70  LEU A N   
440  C CA  . LEU A 63  ? 0.25683 0.27343 0.25656 0.06024  -0.07511 0.00927  70  LEU A CA  
441  C C   . LEU A 63  ? 0.28857 0.31878 0.28956 0.05508  -0.09024 0.00879  70  LEU A C   
442  O O   . LEU A 63  ? 0.25371 0.30094 0.27533 0.05150  -0.09514 0.00821  70  LEU A O   
443  C CB  . LEU A 63  ? 0.27592 0.30207 0.29760 0.06850  -0.07078 0.01534  70  LEU A CB  
444  C CG  . LEU A 63  ? 0.27973 0.28925 0.29838 0.07193  -0.05603 0.01441  70  LEU A CG  
445  C CD1 . LEU A 63  ? 0.29933 0.31636 0.33724 0.08123  -0.05064 0.01954  70  LEU A CD1 
446  C CD2 . LEU A 63  ? 0.27234 0.27578 0.28794 0.06209  -0.04957 0.00506  70  LEU A CD2 
447  N N   . ASP A 64  ? 0.24807 0.27032 0.22594 0.05352  -0.09782 0.00916  71  ASP A N   
448  C CA  . ASP A 64  ? 0.27858 0.30980 0.25247 0.04608  -0.11332 0.00728  71  ASP A CA  
449  C C   . ASP A 64  ? 0.32684 0.35485 0.30127 0.03571  -0.11232 -0.00353 71  ASP A C   
450  O O   . ASP A 64  ? 0.31582 0.35308 0.29491 0.02749  -0.12433 -0.00559 71  ASP A O   
451  C CB  . ASP A 64  ? 0.32150 0.33969 0.26370 0.04583  -0.12039 0.00840  71  ASP A CB  
452  C CG  . ASP A 64  ? 0.49495 0.51945 0.43664 0.05517  -0.12696 0.02110  71  ASP A CG  
453  O OD1 . ASP A 64  ? 0.42301 0.46289 0.39037 0.06276  -0.12628 0.02915  71  ASP A OD1 
454  O OD2 . ASP A 64  ? 0.51091 0.52415 0.42516 0.05575  -0.13237 0.02355  71  ASP A OD2 
455  N N   . SER A 65  ? 0.28239 0.29708 0.25166 0.03554  -0.09877 -0.00970 72  SER A N   
456  C CA  . SER A 65  ? 0.28422 0.29376 0.25424 0.02824  -0.09537 -0.01875 72  SER A CA  
457  C C   . SER A 65  ? 0.33475 0.35852 0.33332 0.02618  -0.09279 -0.01842 72  SER A C   
458  O O   . SER A 65  ? 0.33122 0.35065 0.33209 0.02066  -0.08939 -0.02468 72  SER A O   
459  C CB  . SER A 65  ? 0.34198 0.33495 0.29689 0.03040  -0.08178 -0.02309 72  SER A CB  
460  O OG  . SER A 65  ? 0.27929 0.27274 0.24105 0.03649  -0.07212 -0.01773 72  SER A OG  
461  N N   . GLY A 66  ? 0.27694 0.31633 0.29605 0.03152  -0.09313 -0.01076 73  GLY A N   
462  C CA  . GLY A 66  ? 0.31215 0.36661 0.35774 0.03028  -0.09024 -0.00932 73  GLY A CA  
463  C C   . GLY A 66  ? 0.23762 0.29743 0.29641 0.04058  -0.08138 -0.00252 73  GLY A C   
464  O O   . GLY A 66  ? 0.23193 0.27696 0.28039 0.04468  -0.07091 -0.00380 73  GLY A O   
465  N N   . LYS A 67  ? 0.22212 0.30234 0.30316 0.04485  -0.08507 0.00513  74  LYS A N   
466  C CA  . LYS A 67  ? 0.21376 0.29561 0.30499 0.05679  -0.07498 0.01156  74  LYS A CA  
467  C C   . LYS A 67  ? 0.23417 0.31433 0.33568 0.05659  -0.06208 0.00833  74  LYS A C   
468  O O   . LYS A 67  ? 0.24552 0.31556 0.34470 0.06503  -0.05090 0.01020  74  LYS A O   
469  C CB  . LYS A 67  ? 0.19898 0.30514 0.31158 0.06440  -0.08234 0.02275  74  LYS A CB  
470  C CG  . LYS A 67  ? 0.45535 0.56516 0.55753 0.06490  -0.09696 0.02775  74  LYS A CG  
471  C CD  . LYS A 67  ? 0.56849 0.71069 0.69733 0.06757  -0.10869 0.03878  74  LYS A CD  
472  C CE  . LYS A 67  ? 0.65685 0.81715 0.81598 0.07664  -0.09773 0.04518  74  LYS A CE  
473  N NZ  . LYS A 67  ? 0.83325 1.02827 1.01986 0.07492  -0.10748 0.05349  74  LYS A NZ  
474  N N   . GLU A 68  ? 0.17411 0.26125 0.28426 0.04699  -0.06318 0.00366  75  GLU A N   
475  C CA  . GLU A 68  ? 0.18031 0.26709 0.29953 0.04708  -0.05138 0.00193  75  GLU A CA  
476  C C   . GLU A 68  ? 0.18661 0.25010 0.28575 0.04483  -0.04277 -0.00500 75  GLU A C   
477  O O   . GLU A 68  ? 0.26037 0.31390 0.34537 0.03859  -0.04652 -0.01020 75  GLU A O   
478  C CB  . GLU A 68  ? 0.24579 0.34750 0.38089 0.03719  -0.05529 0.00069  75  GLU A CB  
479  C CG  . GLU A 68  ? 0.27511 0.40550 0.43709 0.03839  -0.06136 0.00938  75  GLU A CG  
480  C CD  . GLU A 68  ? 0.73423 0.87423 0.89554 0.03443  -0.07804 0.01210  75  GLU A CD  
481  O OE1 . GLU A 68  ? 0.77489 0.90207 0.91884 0.02458  -0.08596 0.00508  75  GLU A OE1 
482  O OE2 . GLU A 68  ? 0.62795 0.78771 0.80495 0.04155  -0.08314 0.02156  75  GLU A OE2 
483  N N   . LEU A 69  ? 0.15260 0.20807 0.25066 0.04968  -0.03108 -0.00476 76  LEU A N   
484  C CA  . LEU A 69  ? 0.14790 0.18325 0.22810 0.04632  -0.02375 -0.01013 76  LEU A CA  
485  C C   . LEU A 69  ? 0.17629 0.21346 0.26223 0.04221  -0.01692 -0.01251 76  LEU A C   
486  O O   . LEU A 69  ? 0.17107 0.20781 0.26128 0.04797  -0.00821 -0.01027 76  LEU A O   
487  C CB  . LEU A 69  ? 0.20294 0.22155 0.27030 0.05400  -0.01689 -0.00797 76  LEU A CB  
488  C CG  . LEU A 69  ? 0.24206 0.25623 0.30088 0.05839  -0.02279 -0.00440 76  LEU A CG  
489  C CD1 . LEU A 69  ? 0.32400 0.31654 0.36767 0.06440  -0.01454 -0.00251 76  LEU A CD1 
490  C CD2 . LEU A 69  ? 0.19902 0.21034 0.24672 0.05031  -0.02943 -0.00829 76  LEU A CD2 
491  N N   . HIS A 70  ? 0.16443 0.20214 0.24894 0.03329  -0.01992 -0.01659 77  HIS A N   
492  C CA  . HIS A 70  ? 0.17295 0.21363 0.26312 0.02921  -0.01455 -0.01750 77  HIS A CA  
493  C C   . HIS A 70  ? 0.13338 0.16683 0.21446 0.02120  -0.01623 -0.02160 77  HIS A C   
494  O O   . HIS A 70  ? 0.13118 0.15971 0.20428 0.01926  -0.02109 -0.02372 77  HIS A O   
495  C CB  . HIS A 70  ? 0.14086 0.20099 0.25189 0.02791  -0.01754 -0.01394 77  HIS A CB  
496  C CG  . HIS A 70  ? 0.18402 0.25024 0.29885 0.02123  -0.02896 -0.01523 77  HIS A CG  
497  N ND1 . HIS A 70  ? 0.26504 0.34589 0.39223 0.02149  -0.03746 -0.01164 77  HIS A ND1 
498  C CD2 . HIS A 70  ? 0.22322 0.28106 0.32921 0.01422  -0.03322 -0.01969 77  HIS A CD2 
499  C CE1 . HIS A 70  ? 0.19592 0.27435 0.31871 0.01356  -0.04676 -0.01497 77  HIS A CE1 
500  N NE2 . HIS A 70  ? 0.23134 0.29479 0.34109 0.01013  -0.04343 -0.01998 77  HIS A NE2 
501  N N   . ILE A 71  ? 0.11365 0.14726 0.19626 0.01751  -0.01146 -0.02179 78  ILE A N   
502  C CA  . ILE A 71  ? 0.11471 0.14319 0.19065 0.01111  -0.01246 -0.02376 78  ILE A CA  
503  C C   . ILE A 71  ? 0.14787 0.18414 0.23473 0.00692  -0.01262 -0.02211 78  ILE A C   
504  O O   . ILE A 71  ? 0.12436 0.16580 0.21757 0.00783  -0.00657 -0.01966 78  ILE A O   
505  C CB  . ILE A 71  ? 0.12985 0.14733 0.19162 0.00945  -0.00665 -0.02463 78  ILE A CB  
506  C CG1 . ILE A 71  ? 0.13690 0.14473 0.18747 0.01190  -0.00593 -0.02571 78  ILE A CG1 
507  C CG2 . ILE A 71  ? 0.12667 0.14277 0.18401 0.00338  -0.00917 -0.02470 78  ILE A CG2 
508  C CD1 . ILE A 71  ? 0.18635 0.18111 0.22060 0.00763  -0.00145 -0.02692 78  ILE A CD1 
509  N N   . ASN A 72  ? 0.12308 0.15858 0.21104 0.00265  -0.01839 -0.02313 79  ASN A N   
510  C CA  . ASN A 72  ? 0.12842 0.16714 0.22420 -0.00278 -0.01877 -0.02128 79  ASN A CA  
511  C C   . ASN A 72  ? 0.14862 0.17825 0.23530 -0.00546 -0.01794 -0.02114 79  ASN A C   
512  O O   . ASN A 72  ? 0.14968 0.17309 0.22842 -0.00378 -0.02058 -0.02285 79  ASN A O   
513  C CB  . ASN A 72  ? 0.10876 0.15062 0.21210 -0.00644 -0.02672 -0.02210 79  ASN A CB  
514  C CG  . ASN A 72  ? 0.15520 0.21057 0.27080 -0.00485 -0.02962 -0.02024 79  ASN A CG  
515  O OD1 . ASN A 72  ? 0.13674 0.20200 0.26110 -0.00111 -0.02361 -0.01674 79  ASN A OD1 
516  N ND2 . ASN A 72  ? 0.15792 0.21360 0.27359 -0.00734 -0.03879 -0.02208 79  ASN A ND2 
517  N N   . LEU A 73  ? 0.13081 0.16099 0.21956 -0.00916 -0.01405 -0.01798 80  LEU A N   
518  C CA  . LEU A 73  ? 0.11555 0.13814 0.19664 -0.01145 -0.01389 -0.01594 80  LEU A CA  
519  C C   . LEU A 73  ? 0.13738 0.15720 0.22475 -0.01633 -0.01588 -0.01387 80  LEU A C   
520  O O   . LEU A 73  ? 0.12358 0.14958 0.21966 -0.02047 -0.01287 -0.01116 80  LEU A O   
521  C CB  . LEU A 73  ? 0.12520 0.14699 0.19812 -0.01248 -0.00779 -0.01337 80  LEU A CB  
522  C CG  . LEU A 73  ? 0.15456 0.17484 0.21812 -0.00973 -0.00499 -0.01581 80  LEU A CG  
523  C CD1 . LEU A 73  ? 0.13254 0.14788 0.18351 -0.01231 0.00085  -0.01404 80  LEU A CD1 
524  C CD2 . LEU A 73  ? 0.13321 0.15087 0.19093 -0.00859 -0.01022 -0.01726 80  LEU A CD2 
525  N N   . ILE A 74  ? 0.12629 0.13612 0.20926 -0.01583 -0.02020 -0.01483 81  ILE A N   
526  C CA  . ILE A 74  ? 0.14629 0.14760 0.23183 -0.02103 -0.02282 -0.01406 81  ILE A CA  
527  C C   . ILE A 74  ? 0.16030 0.14921 0.23771 -0.01974 -0.02165 -0.01022 81  ILE A C   
528  O O   . ILE A 74  ? 0.16145 0.14157 0.23203 -0.01399 -0.02335 -0.01143 81  ILE A O   
529  C CB  . ILE A 74  ? 0.14527 0.14029 0.22949 -0.02125 -0.02908 -0.01948 81  ILE A CB  
530  C CG1 . ILE A 74  ? 0.17136 0.18026 0.26276 -0.02056 -0.03118 -0.02189 81  ILE A CG1 
531  C CG2 . ILE A 74  ? 0.15755 0.14173 0.24287 -0.02958 -0.03229 -0.01912 81  ILE A CG2 
532  C CD1 . ILE A 74  ? 0.23093 0.23409 0.31745 -0.02068 -0.03826 -0.02707 81  ILE A CD1 
533  N N   . PRO A 75  ? 0.16692 0.15508 0.24490 -0.02415 -0.01813 -0.00460 82  PRO A N   
534  C CA  . PRO A 75  ? 0.16666 0.14166 0.23688 -0.02279 -0.01772 0.00056  82  PRO A CA  
535  C C   . PRO A 75  ? 0.20832 0.16618 0.27771 -0.02729 -0.01989 0.00021  82  PRO A C   
536  O O   . PRO A 75  ? 0.22603 0.18544 0.30257 -0.03587 -0.02102 -0.00127 82  PRO A O   
537  C CB  . PRO A 75  ? 0.19462 0.17507 0.26328 -0.02672 -0.01281 0.00691  82  PRO A CB  
538  C CG  . PRO A 75  ? 0.21952 0.21154 0.29879 -0.03280 -0.00957 0.00530  82  PRO A CG  
539  C CD  . PRO A 75  ? 0.18318 0.18229 0.26899 -0.02998 -0.01350 -0.00183 82  PRO A CD  
540  N N   . ASN A 76  ? 0.19735 0.13836 0.25782 -0.02158 -0.02042 0.00223  83  ASN A N   
541  C CA  . ASN A 76  ? 0.23492 0.15212 0.28936 -0.02524 -0.02165 0.00184  83  ASN A CA  
542  C C   . ASN A 76  ? 0.25598 0.15854 0.30240 -0.01993 -0.01894 0.01004  83  ASN A C   
543  O O   . ASN A 76  ? 0.27987 0.17752 0.32123 -0.00829 -0.01840 0.01146  83  ASN A O   
544  C CB  . ASN A 76  ? 0.24950 0.15365 0.29705 -0.02114 -0.02477 -0.00636 83  ASN A CB  
545  C CG  . ASN A 76  ? 0.41137 0.28651 0.44891 -0.02782 -0.02663 -0.00863 83  ASN A CG  
546  O OD1 . ASN A 76  ? 0.37516 0.23103 0.40548 -0.02684 -0.02395 -0.00319 83  ASN A OD1 
547  N ND2 . ASN A 76  ? 0.40419 0.27501 0.43996 -0.03554 -0.03183 -0.01625 83  ASN A ND2 
548  N N   . LYS A 77  ? 0.29670 0.19266 0.34259 -0.02802 -0.01692 0.01646  84  LYS A N   
549  C CA  . LYS A 77  ? 0.29438 0.17724 0.33193 -0.02273 -0.01462 0.02608  84  LYS A CA  
550  C C   . LYS A 77  ? 0.35792 0.20962 0.38461 -0.01719 -0.01458 0.02584  84  LYS A C   
551  O O   . LYS A 77  ? 0.35858 0.20105 0.37916 -0.00601 -0.01296 0.03302  84  LYS A O   
552  C CB  . LYS A 77  ? 0.31434 0.19765 0.35219 -0.03317 -0.01147 0.03378  84  LYS A CB  
553  C CG  . LYS A 77  ? 0.38976 0.29922 0.43291 -0.03571 -0.00910 0.03563  84  LYS A CG  
554  C CD  . LYS A 77  ? 0.45136 0.35891 0.49199 -0.04488 -0.00402 0.04411  84  LYS A CD  
555  C CE  . LYS A 77  ? 0.41762 0.34673 0.45869 -0.04642 0.00020  0.04551  84  LYS A CE  
556  N NZ  . LYS A 77  ? 0.49982 0.44680 0.55371 -0.04910 0.00110  0.03704  84  LYS A NZ  
557  N N   . GLN A 78  ? 0.38303 0.21756 0.40610 -0.02442 -0.01648 0.01792  85  GLN A N   
558  C CA  . GLN A 78  ? 0.42648 0.22504 0.43415 -0.01933 -0.01552 0.01615  85  GLN A CA  
559  C C   . GLN A 78  ? 0.46495 0.26224 0.46813 -0.00164 -0.01374 0.01308  85  GLN A C   
560  O O   . GLN A 78  ? 0.45726 0.23312 0.45067 0.01070  -0.00981 0.01768  85  GLN A O   
561  C CB  . GLN A 78  ? 0.52385 0.30321 0.52558 -0.03375 -0.01932 0.00751  85  GLN A CB  
562  C CG  . GLN A 78  ? 0.72725 0.50083 0.73230 -0.05163 -0.02002 0.01265  85  GLN A CG  
563  C CD  . GLN A 78  ? 0.83036 0.64169 0.85494 -0.05939 -0.01973 0.01668  85  GLN A CD  
564  O OE1 . GLN A 78  ? 0.80971 0.62670 0.83725 -0.06168 -0.01557 0.02634  85  GLN A OE1 
565  N NE2 . GLN A 78  ? 0.73362 0.56961 0.76973 -0.06208 -0.02333 0.00968  85  GLN A NE2 
566  N N   . ASP A 79  ? 0.37769 0.19809 0.38843 0.00056  -0.01570 0.00643  86  ASP A N   
567  C CA  . ASP A 79  ? 0.38432 0.20857 0.39319 0.01625  -0.01312 0.00430  86  ASP A CA  
568  C C   . ASP A 79  ? 0.33646 0.18806 0.35689 0.02570  -0.01199 0.01346  86  ASP A C   
569  O O   . ASP A 79  ? 0.32302 0.17996 0.34474 0.03959  -0.00909 0.01516  86  ASP A O   
570  C CB  . ASP A 79  ? 0.41160 0.24677 0.42160 0.01318  -0.01590 -0.00644 86  ASP A CB  
571  C CG  . ASP A 79  ? 0.66500 0.47385 0.66145 0.00347  -0.01897 -0.01589 86  ASP A CG  
572  O OD1 . ASP A 79  ? 0.69909 0.47645 0.68275 0.00083  -0.01777 -0.01515 86  ASP A OD1 
573  O OD2 . ASP A 79  ? 0.55992 0.37837 0.55720 -0.00213 -0.02321 -0.02368 86  ASP A OD2 
574  N N   . ARG A 80  ? 0.28677 0.15559 0.31476 0.01779  -0.01411 0.01959  87  ARG A N   
575  C CA  . ARG A 80  ? 0.25154 0.14694 0.28788 0.02234  -0.01521 0.02733  87  ARG A CA  
576  C C   . ARG A 80  ? 0.24203 0.16023 0.28581 0.02520  -0.01642 0.02176  87  ARG A C   
577  O O   . ARG A 80  ? 0.25163 0.18400 0.30056 0.03484  -0.01624 0.02653  87  ARG A O   
578  C CB  . ARG A 80  ? 0.31931 0.20941 0.35400 0.03516  -0.01371 0.03897  87  ARG A CB  
579  C CG  . ARG A 80  ? 0.33486 0.24721 0.37413 0.03347  -0.01720 0.04919  87  ARG A CG  
580  C CD  . ARG A 80  ? 0.42250 0.34570 0.46690 0.04757  -0.01825 0.06053  87  ARG A CD  
581  N NE  . ARG A 80  ? 0.59732 0.49649 0.63523 0.05705  -0.01532 0.06921  87  ARG A NE  
582  C CZ  . ARG A 80  ? 0.66226 0.56077 0.70447 0.07415  -0.01303 0.07739  87  ARG A CZ  
583  N NH1 . ARG A 80  ? 0.45447 0.37885 0.50963 0.08280  -0.01363 0.07904  87  ARG A NH1 
584  N NH2 . ARG A 80  ? 0.55194 0.42363 0.58594 0.08309  -0.00950 0.08516  87  ARG A NH2 
585  N N   . THR A 81  ? 0.21610 0.13895 0.26144 0.01636  -0.01781 0.01266  88  THR A N   
586  C CA  . THR A 81  ? 0.20818 0.14930 0.25867 0.01784  -0.01876 0.00734  88  THR A CA  
587  C C   . THR A 81  ? 0.20983 0.16641 0.26500 0.00750  -0.02056 0.00470  88  THR A C   
588  O O   . THR A 81  ? 0.22818 0.18018 0.28376 -0.00125 -0.02061 0.00356  88  THR A O   
589  C CB  . THR A 81  ? 0.23640 0.16599 0.28171 0.02090  -0.01799 -0.00178 88  THR A CB  
590  O OG1 . THR A 81  ? 0.24870 0.16465 0.28987 0.01073  -0.02032 -0.00783 88  THR A OG1 
591  C CG2 . THR A 81  ? 0.26451 0.17832 0.30320 0.03420  -0.01366 0.00006  88  THR A CG2 
592  N N   . LEU A 82  ? 0.16329 0.13788 0.22208 0.00879  -0.02131 0.00435  89  LEU A N   
593  C CA  . LEU A 82  ? 0.15333 0.13941 0.21439 0.00173  -0.02169 0.00041  89  LEU A CA  
594  C C   . LEU A 82  ? 0.15722 0.14840 0.21965 0.00483  -0.02226 -0.00578 89  LEU A C   
595  O O   . LEU A 82  ? 0.18511 0.18266 0.24804 0.01061  -0.02212 -0.00406 89  LEU A O   
596  C CB  . LEU A 82  ? 0.18116 0.17906 0.24019 -0.00112 -0.02198 0.00547  89  LEU A CB  
597  C CG  . LEU A 82  ? 0.13566 0.14113 0.19359 -0.00671 -0.02056 0.00102  89  LEU A CG  
598  C CD1 . LEU A 82  ? 0.15322 0.15475 0.21395 -0.01171 -0.01754 -0.00103 89  LEU A CD1 
599  C CD2 . LEU A 82  ? 0.16699 0.17867 0.21707 -0.01016 -0.02118 0.00521  89  LEU A CD2 
600  N N   . THR A 83  ? 0.13807 0.12784 0.20184 0.00097  -0.02298 -0.01181 90  THR A N   
601  C CA  . THR A 83  ? 0.15802 0.15060 0.22090 0.00376  -0.02395 -0.01720 90  THR A CA  
602  C C   . THR A 83  ? 0.17072 0.17446 0.23648 0.00039  -0.02366 -0.01869 90  THR A C   
603  O O   . THR A 83  ? 0.17212 0.17842 0.24201 -0.00436 -0.02302 -0.01863 90  THR A O   
604  C CB  . THR A 83  ? 0.19491 0.17532 0.25457 0.00264  -0.02644 -0.02259 90  THR A CB  
605  O OG1 . THR A 83  ? 0.20002 0.16419 0.25310 0.00659  -0.02542 -0.02192 90  THR A OG1 
606  C CG2 . THR A 83  ? 0.17866 0.16147 0.23461 0.00563  -0.02775 -0.02743 90  THR A CG2 
607  N N   . ILE A 84  ? 0.14448 0.15428 0.20806 0.00316  -0.02314 -0.01927 91  ILE A N   
608  C CA  . ILE A 84  ? 0.16914 0.18455 0.23233 0.00127  -0.02223 -0.02097 91  ILE A CA  
609  C C   . ILE A 84  ? 0.13205 0.14609 0.19404 0.00426  -0.02396 -0.02498 91  ILE A C   
610  O O   . ILE A 84  ? 0.16298 0.17606 0.22092 0.00795  -0.02380 -0.02536 91  ILE A O   
611  C CB  . ILE A 84  ? 0.16844 0.18861 0.22723 -0.00008 -0.02102 -0.01828 91  ILE A CB  
612  C CG1 . ILE A 84  ? 0.24191 0.26294 0.29865 -0.00390 -0.02068 -0.01397 91  ILE A CG1 
613  C CG2 . ILE A 84  ? 0.14942 0.16920 0.20416 -0.00155 -0.01925 -0.02067 91  ILE A CG2 
614  C CD1 . ILE A 84  ? 0.31859 0.34220 0.37737 -0.00165 -0.02267 -0.00872 91  ILE A CD1 
615  N N   . VAL A 85  ? 0.10943 0.12472 0.17518 0.00296  -0.02550 -0.02701 92  VAL A N   
616  C CA  . VAL A 85  ? 0.11443 0.12888 0.17808 0.00519  -0.02888 -0.02994 92  VAL A CA  
617  C C   . VAL A 85  ? 0.20219 0.22134 0.26626 0.00700  -0.02721 -0.02917 92  VAL A C   
618  O O   . VAL A 85  ? 0.17002 0.19346 0.23984 0.00612  -0.02453 -0.02753 92  VAL A O   
619  C CB  . VAL A 85  ? 0.16451 0.17819 0.23285 0.00181  -0.03407 -0.03161 92  VAL A CB  
620  C CG1 . VAL A 85  ? 0.20360 0.21515 0.26570 0.00360  -0.03929 -0.03449 92  VAL A CG1 
621  C CG2 . VAL A 85  ? 0.19745 0.20142 0.26339 -0.00085 -0.03489 -0.03232 92  VAL A CG2 
622  N N   . ASP A 86  ? 0.15760 0.17434 0.21446 0.01021  -0.02778 -0.02997 93  ASP A N   
623  C CA  . ASP A 86  ? 0.12559 0.14325 0.18126 0.01284  -0.02664 -0.02882 93  ASP A CA  
624  C C   . ASP A 86  ? 0.17072 0.18707 0.22142 0.01591  -0.03131 -0.02960 93  ASP A C   
625  O O   . ASP A 86  ? 0.18688 0.19919 0.23091 0.01590  -0.03379 -0.03178 93  ASP A O   
626  C CB  . ASP A 86  ? 0.14690 0.15998 0.19510 0.01218  -0.02164 -0.02754 93  ASP A CB  
627  C CG  . ASP A 86  ? 0.24414 0.25502 0.28480 0.01223  -0.02145 -0.02719 93  ASP A CG  
628  O OD1 . ASP A 86  ? 0.20322 0.21157 0.23826 0.01529  -0.02272 -0.02728 93  ASP A OD1 
629  O OD2 . ASP A 86  ? 0.18935 0.20255 0.23024 0.00937  -0.01989 -0.02594 93  ASP A OD2 
630  N N   . THR A 87  ? 0.12279 0.14159 0.17549 0.01931  -0.03219 -0.02744 94  THR A N   
631  C CA  . THR A 87  ? 0.14188 0.15985 0.18848 0.02247  -0.03753 -0.02677 94  THR A CA  
632  C C   . THR A 87  ? 0.20322 0.21337 0.23915 0.02604  -0.03334 -0.02452 94  THR A C   
633  O O   . THR A 87  ? 0.19553 0.20490 0.22869 0.03061  -0.03552 -0.02143 94  THR A O   
634  C CB  . THR A 87  ? 0.17416 0.20302 0.23253 0.02406  -0.04336 -0.02399 94  THR A CB  
635  O OG1 . THR A 87  ? 0.13979 0.17335 0.20813 0.02798  -0.03755 -0.02042 94  THR A OG1 
636  C CG2 . THR A 87  ? 0.16947 0.20452 0.23630 0.01766  -0.04892 -0.02616 94  THR A CG2 
637  N N   . GLY A 88  ? 0.17737 0.18200 0.20758 0.02335  -0.02770 -0.02516 95  GLY A N   
638  C CA  . GLY A 88  ? 0.17157 0.16781 0.19139 0.02390  -0.02360 -0.02275 95  GLY A CA  
639  C C   . GLY A 88  ? 0.17036 0.16353 0.17918 0.02543  -0.02494 -0.02199 95  GLY A C   
640  O O   . GLY A 88  ? 0.16941 0.16463 0.17573 0.02738  -0.03005 -0.02362 95  GLY A O   
641  N N   . ILE A 89  ? 0.18095 0.16802 0.18130 0.02348  -0.02007 -0.01939 96  ILE A N   
642  C CA  . ILE A 89  ? 0.19422 0.17743 0.18229 0.02537  -0.01944 -0.01736 96  ILE A CA  
643  C C   . ILE A 89  ? 0.20702 0.19515 0.19325 0.02553  -0.01852 -0.01988 96  ILE A C   
644  O O   . ILE A 89  ? 0.20558 0.18969 0.17938 0.02863  -0.01867 -0.01972 96  ILE A O   
645  C CB  . ILE A 89  ? 0.21288 0.18834 0.19332 0.02177  -0.01364 -0.01287 96  ILE A CB  
646  C CG1 . ILE A 89  ? 0.26795 0.23774 0.23401 0.02438  -0.01234 -0.00931 96  ILE A CG1 
647  C CG2 . ILE A 89  ? 0.19466 0.17673 0.18130 0.01457  -0.00935 -0.01252 96  ILE A CG2 
648  C CD1 . ILE A 89  ? 0.26509 0.22244 0.22193 0.02180  -0.00833 -0.00390 96  ILE A CD1 
649  N N   . GLY A 90  ? 0.17055 0.16549 0.16685 0.02327  -0.01718 -0.02201 97  GLY A N   
650  C CA  . GLY A 90  ? 0.18250 0.17982 0.17677 0.02556  -0.01460 -0.02376 97  GLY A CA  
651  C C   . GLY A 90  ? 0.21302 0.21468 0.20492 0.02515  -0.00685 -0.01926 97  GLY A C   
652  O O   . GLY A 90  ? 0.20310 0.20574 0.19514 0.02080  -0.00440 -0.01487 97  GLY A O   
653  N N   . MET A 91  ? 0.17684 0.18075 0.16673 0.02968  -0.00225 -0.01995 98  MET A N   
654  C CA  . MET A 91  ? 0.17062 0.18292 0.16149 0.03043  0.00656  -0.01434 98  MET A CA  
655  C C   . MET A 91  ? 0.18875 0.19358 0.16391 0.03839  0.01210  -0.01631 98  MET A C   
656  O O   . MET A 91  ? 0.21791 0.21326 0.18583 0.04317  0.01000  -0.02231 98  MET A O   
657  C CB  . MET A 91  ? 0.21590 0.24406 0.22457 0.02947  0.01010  -0.01031 98  MET A CB  
658  C CG  . MET A 91  ? 0.24519 0.28140 0.26652 0.02007  0.00570  -0.00735 98  MET A CG  
659  S SD  . MET A 91  ? 0.19982 0.25261 0.23982 0.02002  0.00554  -0.00370 98  MET A SD  
660  C CE  . MET A 91  ? 0.23053 0.27134 0.26870 0.02384  -0.00033 -0.01106 98  MET A CE  
661  N N   . THR A 92  ? 0.21107 0.21846 0.17917 0.03915  0.01977  -0.01122 99  THR A N   
662  C CA  . THR A 92  ? 0.26342 0.26450 0.21527 0.04753  0.02836  -0.01214 99  THR A CA  
663  C C   . THR A 92  ? 0.21875 0.23112 0.18272 0.05424  0.03751  -0.00996 99  THR A C   
664  O O   . THR A 92  ? 0.21020 0.23846 0.19639 0.05125  0.03650  -0.00600 99  THR A O   
665  C CB  . THR A 92  ? 0.24742 0.24966 0.18924 0.04612  0.03549  -0.00570 99  THR A CB  
666  O OG1 . THR A 92  ? 0.26342 0.28592 0.22552 0.04093  0.04174  0.00311  99  THR A OG1 
667  C CG2 . THR A 92  ? 0.32043 0.31120 0.25113 0.04075  0.02679  -0.00593 99  THR A CG2 
668  N N   . LYS A 93  ? 0.30551 0.15063 0.19273 0.05898  -0.04465 -0.01005 100 LYS A N   
669  C CA  . LYS A 93  ? 0.31240 0.16087 0.19732 0.05727  -0.02851 -0.01287 100 LYS A CA  
670  C C   . LYS A 93  ? 0.30526 0.16002 0.19689 0.05522  -0.01376 -0.00634 100 LYS A C   
671  O O   . LYS A 93  ? 0.26786 0.13825 0.17911 0.05468  -0.00383 -0.00818 100 LYS A O   
672  C CB  . LYS A 93  ? 0.35577 0.18762 0.20565 0.05787  -0.02602 -0.01583 100 LYS A CB  
673  C CG  . LYS A 93  ? 0.35151 0.18613 0.20168 0.05935  -0.01000 -0.02086 100 LYS A CG  
674  C CD  . LYS A 93  ? 0.38936 0.20455 0.20159 0.06046  -0.00554 -0.02517 100 LYS A CD  
675  C CE  . LYS A 93  ? 0.46555 0.28077 0.27908 0.06486  0.00988  -0.03155 100 LYS A CE  
676  N NZ  . LYS A 93  ? 0.48987 0.28969 0.26764 0.06698  0.02189  -0.03382 100 LYS A NZ  
677  N N   . ALA A 94  ? 0.31492 0.15738 0.18965 0.05335  -0.01273 0.00169  101 ALA A N   
678  C CA  . ALA A 94  ? 0.37707 0.22517 0.25791 0.04798  0.00141  0.00740  101 ALA A CA  
679  C C   . ALA A 94  ? 0.33389 0.19897 0.24878 0.04564  0.00089  0.00576  101 ALA A C   
680  O O   . ALA A 94  ? 0.34546 0.22788 0.27631 0.04160  0.01219  0.00531  101 ALA A O   
681  C CB  . ALA A 94  ? 0.40192 0.22774 0.25598 0.04469  0.00157  0.01700  101 ALA A CB  
682  N N   . ASP A 95  ? 0.28420 0.14625 0.21055 0.04843  -0.01228 0.00434  102 ASP A N   
683  C CA  . ASP A 95  ? 0.31584 0.19298 0.27207 0.04661  -0.01258 0.00071  102 ASP A CA  
684  C C   . ASP A 95  ? 0.25560 0.15419 0.23013 0.04629  -0.00745 -0.00516 102 ASP A C   
685  O O   . ASP A 95  ? 0.25310 0.16686 0.24417 0.04205  -0.00050 -0.00584 102 ASP A O   
686  C CB  . ASP A 95  ? 0.35691 0.23016 0.32359 0.05208  -0.02682 -0.00187 102 ASP A CB  
687  C CG  . ASP A 95  ? 0.45546 0.30698 0.40969 0.05462  -0.03239 0.00487  102 ASP A CG  
688  O OD1 . ASP A 95  ? 0.47118 0.31049 0.41351 0.04869  -0.02323 0.01097  102 ASP A OD1 
689  O OD2 . ASP A 95  ? 0.42966 0.27651 0.38702 0.06269  -0.04623 0.00420  102 ASP A OD2 
690  N N   . LEU A 96  ? 0.26403 0.16260 0.23484 0.05033  -0.01181 -0.00947 103 LEU A N   
691  C CA  . LEU A 96  ? 0.24760 0.16018 0.23194 0.05086  -0.00691 -0.01352 103 LEU A CA  
692  C C   . LEU A 96  ? 0.26608 0.18881 0.25060 0.05070  0.00611  -0.01049 103 LEU A C   
693  O O   . LEU A 96  ? 0.23310 0.17305 0.23525 0.04979  0.01021  -0.01061 103 LEU A O   
694  C CB  . LEU A 96  ? 0.27852 0.18239 0.25256 0.05376  -0.01144 -0.01843 103 LEU A CB  
695  C CG  . LEU A 96  ? 0.28608 0.19002 0.26931 0.05249  -0.02356 -0.02379 103 LEU A CG  
696  C CD1 . LEU A 96  ? 0.26050 0.15283 0.22859 0.05249  -0.02612 -0.02921 103 LEU A CD1 
697  C CD2 . LEU A 96  ? 0.22089 0.14106 0.23013 0.04973  -0.02195 -0.02589 103 LEU A CD2 
698  N N   . ILE A 97  ? 0.26111 0.17527 0.22587 0.05195  0.01270  -0.00792 104 ILE A N   
699  C CA  . ILE A 97  ? 0.25599 0.18445 0.22423 0.05303  0.02624  -0.00589 104 ILE A CA  
700  C C   . ILE A 97  ? 0.26557 0.21149 0.25095 0.04543  0.03062  -0.00242 104 ILE A C   
701  O O   . ILE A 97  ? 0.29259 0.26167 0.29545 0.04567  0.03682  -0.00215 104 ILE A O   
702  C CB  . ILE A 97  ? 0.25075 0.16634 0.19274 0.05492  0.03433  -0.00475 104 ILE A CB  
703  C CG1 . ILE A 97  ? 0.27379 0.17233 0.19815 0.06161  0.03052  -0.01054 104 ILE A CG1 
704  C CG2 . ILE A 97  ? 0.26155 0.19737 0.21158 0.05549  0.05036  -0.00268 104 ILE A CG2 
705  C CD1 . ILE A 97  ? 0.34178 0.22117 0.23208 0.06212  0.03520  -0.01076 104 ILE A CD1 
706  N N   . ASN A 98  ? 0.22622 0.16052 0.20647 0.03868  0.02661  0.00008  105 ASN A N   
707  C CA  . ASN A 98  ? 0.24920 0.19348 0.24211 0.02889  0.03049  0.00203  105 ASN A CA  
708  C C   . ASN A 98  ? 0.22738 0.18180 0.24087 0.02750  0.02331  -0.00232 105 ASN A C   
709  O O   . ASN A 98  ? 0.25581 0.19997 0.27145 0.02308  0.01862  -0.00333 105 ASN A O   
710  C CB  . ASN A 98  ? 0.29534 0.21517 0.26920 0.02299  0.03030  0.00699  105 ASN A CB  
711  C CG  . ASN A 98  ? 0.47896 0.40429 0.46022 0.01001  0.03809  0.00918  105 ASN A CG  
712  O OD1 . ASN A 98  ? 0.53276 0.48560 0.53320 0.00455  0.04471  0.00698  105 ASN A OD1 
713  N ND2 . ASN A 98  ? 0.44749 0.34597 0.41329 0.00472  0.03656  0.01358  105 ASN A ND2 
714  N N   . ASN A 99  ? 0.19991 0.17245 0.22633 0.03233  0.02317  -0.00486 106 ASN A N   
715  C CA  . ASN A 99  ? 0.17659 0.16210 0.21973 0.03039  0.01866  -0.00843 106 ASN A CA  
716  C C   . ASN A 99  ? 0.19565 0.16642 0.23903 0.03083  0.01028  -0.01229 106 ASN A C   
717  O O   . ASN A 99  ? 0.18043 0.15461 0.23313 0.02564  0.00863  -0.01575 106 ASN A O   
718  C CB  . ASN A 99  ? 0.18123 0.18511 0.23634 0.02029  0.02271  -0.00865 106 ASN A CB  
719  C CG  . ASN A 99  ? 0.19068 0.21791 0.25243 0.02080  0.03040  -0.00546 106 ASN A CG  
720  O OD1 . ASN A 99  ? 0.18057 0.21930 0.24664 0.03044  0.03070  -0.00433 106 ASN A OD1 
721  N ND2 . ASN A 99  ? 0.22034 0.25492 0.28406 0.01051  0.03721  -0.00401 106 ASN A ND2 
722  N N   . LEU A 100 ? 0.17458 0.13120 0.20879 0.03724  0.00510  -0.01284 107 LEU A N   
723  C CA  . LEU A 100 ? 0.21186 0.16081 0.25092 0.03916  -0.00342 -0.01705 107 LEU A CA  
724  C C   . LEU A 100 ? 0.24149 0.18150 0.28315 0.03647  -0.00575 -0.01771 107 LEU A C   
725  O O   . LEU A 100 ? 0.22064 0.16435 0.27526 0.03597  -0.00808 -0.02280 107 LEU A O   
726  C CB  . LEU A 100 ? 0.16303 0.12530 0.21580 0.03877  -0.00382 -0.02124 107 LEU A CB  
727  C CG  . LEU A 100 ? 0.19439 0.15833 0.24177 0.04248  -0.00142 -0.01974 107 LEU A CG  
728  C CD1 . LEU A 100 ? 0.23911 0.21893 0.29154 0.04223  0.00486  -0.01659 107 LEU A CD1 
729  C CD2 . LEU A 100 ? 0.35972 0.32076 0.41111 0.04260  -0.00566 -0.02385 107 LEU A CD2 
730  N N   . GLY A 101 ? 0.24729 0.17271 0.27459 0.03495  -0.00394 -0.01250 108 GLY A N   
731  C CA  . GLY A 101 ? 0.27410 0.18262 0.29921 0.03376  -0.00631 -0.01177 108 GLY A CA  
732  C C   . GLY A 101 ? 0.29455 0.20756 0.32966 0.02494  -0.00025 -0.01521 108 GLY A C   
733  O O   . GLY A 101 ? 0.32754 0.22423 0.36313 0.02507  -0.00205 -0.01707 108 GLY A O   
734  N N   . THR A 102 ? 0.21309 0.14715 0.25566 0.01777  0.00627  -0.01657 109 THR A N   
735  C CA  . THR A 102 ? 0.22382 0.16593 0.27503 0.00737  0.01064  -0.02127 109 THR A CA  
736  C C   . THR A 102 ? 0.22049 0.16560 0.26653 -0.00390 0.01829  -0.01721 109 THR A C   
737  O O   . THR A 102 ? 0.26799 0.21672 0.30698 -0.00256 0.02201  -0.01110 109 THR A O   
738  C CB  . THR A 102 ? 0.20066 0.16874 0.26509 0.00674  0.01037  -0.02611 109 THR A CB  
739  O OG1 . THR A 102 ? 0.23328 0.22135 0.29912 0.00679  0.01340  -0.02147 109 THR A OG1 
740  C CG2 . THR A 102 ? 0.27254 0.24014 0.34187 0.01609  0.00508  -0.02912 109 THR A CG2 
741  N N   . ILE A 103 ? 0.20829 0.15190 0.25771 -0.01613 0.02160  -0.02166 110 ILE A N   
742  C CA  . ILE A 103 ? 0.19826 0.15342 0.24854 -0.03058 0.02921  -0.01971 110 ILE A CA  
743  C C   . ILE A 103 ? 0.23314 0.22697 0.30030 -0.03459 0.02868  -0.02373 110 ILE A C   
744  O O   . ILE A 103 ? 0.18016 0.18525 0.25401 -0.04777 0.02938  -0.02986 110 ILE A O   
745  C CB  . ILE A 103 ? 0.33191 0.26110 0.37411 -0.04427 0.03315  -0.02219 110 ILE A CB  
746  C CG1 . ILE A 103 ? 0.33800 0.26019 0.38522 -0.04677 0.02973  -0.03287 110 ILE A CG1 
747  C CG2 . ILE A 103 ? 0.30713 0.19696 0.32913 -0.03851 0.03339  -0.01452 110 ILE A CG2 
748  C CD1 . ILE A 103 ? 0.37204 0.27246 0.41227 -0.06441 0.03533  -0.03749 110 ILE A CD1 
749  N N   . ALA A 104 ? 0.22185 0.23467 0.29414 -0.02301 0.02678  -0.02018 111 ALA A N   
750  C CA  . ALA A 104 ? 0.20749 0.25099 0.29264 -0.02158 0.02332  -0.02260 111 ALA A CA  
751  C C   . ALA A 104 ? 0.16553 0.24108 0.26326 -0.03258 0.02645  -0.02246 111 ALA A C   
752  O O   . ALA A 104 ? 0.16220 0.26189 0.26909 -0.03632 0.02171  -0.02599 111 ALA A O   
753  C CB  . ALA A 104 ? 0.21811 0.26674 0.30300 -0.00554 0.02096  -0.01809 111 ALA A CB  
754  N N   . LYS A 105 ? 0.17401 0.25247 0.27239 -0.03873 0.03424  -0.01859 112 LYS A N   
755  C CA  . LYS A 105 ? 0.20935 0.32471 0.32483 -0.05033 0.03751  -0.01929 112 LYS A CA  
756  C C   . LYS A 105 ? 0.28761 0.40464 0.40581 -0.07014 0.03517  -0.02748 112 LYS A C   
757  O O   . LYS A 105 ? 0.20712 0.35606 0.33828 -0.07566 0.02925  -0.03165 112 LYS A O   
758  C CB  . LYS A 105 ? 0.17245 0.29142 0.28835 -0.05435 0.04904  -0.01397 112 LYS A CB  
759  C CG  . LYS A 105 ? 0.31803 0.48217 0.45716 -0.06628 0.05361  -0.01499 112 LYS A CG  
760  C CD  . LYS A 105 ? 0.31193 0.48505 0.45323 -0.06566 0.06728  -0.00939 112 LYS A CD  
761  C CE  . LYS A 105 ? 0.56649 0.76763 0.72450 -0.08890 0.07583  -0.01174 112 LYS A CE  
762  N NZ  . LYS A 105 ? 0.49925 0.74990 0.68572 -0.09456 0.06753  -0.01690 112 LYS A NZ  
763  N N   . SER A 106 ? 0.20318 0.28366 0.30703 -0.08047 0.03897  -0.03010 113 SER A N   
764  C CA  . SER A 106 ? 0.24556 0.32174 0.34922 -0.10001 0.03786  -0.03954 113 SER A CA  
765  C C   . SER A 106 ? 0.24914 0.32209 0.34954 -0.09498 0.02909  -0.04740 113 SER A C   
766  O O   . SER A 106 ? 0.25349 0.34050 0.35730 -0.10915 0.02562  -0.05632 113 SER A O   
767  C CB  . SER A 106 ? 0.36120 0.39287 0.44794 -0.11105 0.04526  -0.03955 113 SER A CB  
768  O OG  . SER A 106 ? 0.31917 0.31179 0.38984 -0.09496 0.04313  -0.03674 113 SER A OG  
769  N N   . GLY A 107 ? 0.21976 0.27592 0.31303 -0.07647 0.02586  -0.04493 114 GLY A N   
770  C CA  . GLY A 107 ? 0.20313 0.25853 0.29340 -0.07231 0.01993  -0.05219 114 GLY A CA  
771  C C   . GLY A 107 ? 0.27864 0.37416 0.37824 -0.07151 0.01348  -0.05200 114 GLY A C   
772  O O   . GLY A 107 ? 0.20467 0.30850 0.30096 -0.07942 0.00925  -0.06019 114 GLY A O   
773  N N   . THR A 108 ? 0.16258 0.28208 0.27196 -0.06114 0.01258  -0.04260 115 THR A N   
774  C CA  . THR A 108 ? 0.17711 0.33479 0.29571 -0.05792 0.00540  -0.04031 115 THR A CA  
775  C C   . THR A 108 ? 0.23648 0.42372 0.36470 -0.07685 0.00214  -0.04635 115 THR A C   
776  O O   . THR A 108 ? 0.22845 0.43597 0.35533 -0.08108 -0.00626 -0.05035 115 THR A O   
777  C CB  . THR A 108 ? 0.15206 0.32660 0.28039 -0.04185 0.00660  -0.02951 115 THR A CB  
778  O OG1 . THR A 108 ? 0.19003 0.33671 0.30747 -0.02652 0.00821  -0.02558 115 THR A OG1 
779  C CG2 . THR A 108 ? 0.18749 0.40017 0.32582 -0.03560 -0.00167 -0.02553 115 THR A CG2 
780  N N   . LYS A 109 ? 0.20203 0.39226 0.33861 -0.08986 0.00866  -0.04714 116 LYS A N   
781  C CA  . LYS A 109 ? 0.22467 0.44371 0.37242 -0.11178 0.00620  -0.05419 116 LYS A CA  
782  C C   . LYS A 109 ? 0.27613 0.47941 0.40865 -0.12556 0.00130  -0.06655 116 LYS A C   
783  O O   . LYS A 109 ? 0.27560 0.50167 0.40689 -0.12938 -0.00782 -0.06933 116 LYS A O   
784  C CB  . LYS A 109 ? 0.25425 0.46579 0.40777 -0.12631 0.01722  -0.05366 116 LYS A CB  
785  C CG  . LYS A 109 ? 0.42521 0.64426 0.57949 -0.14609 0.01578  -0.05935 116 LYS A CG  
786  C CD  . LYS A 109 ? 0.35599 0.56647 0.51440 -0.15766 0.02797  -0.05576 116 LYS A CD  
787  C CE  . LYS A 109 ? 0.47868 0.70522 0.64349 -0.17685 0.02695  -0.06055 116 LYS A CE  
788  N NZ  . LYS A 109 ? 0.61668 0.89068 0.79783 -0.17257 0.01487  -0.06133 116 LYS A NZ  
789  N N   . ALA A 110 ? 0.25847 0.41515 0.37396 -0.12766 0.00737  -0.07214 117 ALA A N   
790  C CA  . ALA A 110 ? 0.31672 0.45387 0.41625 -0.13913 0.00529  -0.08543 117 ALA A CA  
791  C C   . ALA A 110 ? 0.28721 0.43905 0.37971 -0.12954 -0.00298 -0.08746 117 ALA A C   
792  O O   . ALA A 110 ? 0.27025 0.43017 0.35232 -0.13856 -0.00847 -0.09504 117 ALA A O   
793  C CB  . ALA A 110 ? 0.28544 0.36902 0.37046 -0.13804 0.01405  -0.08993 117 ALA A CB  
794  N N   . PHE A 111 ? 0.25543 0.40330 0.34739 -0.10766 -0.00306 -0.07776 118 PHE A N   
795  C CA  . PHE A 111 ? 0.20547 0.36137 0.28720 -0.09850 -0.00883 -0.07776 118 PHE A CA  
796  C C   . PHE A 111 ? 0.23689 0.43708 0.32316 -0.10323 -0.02020 -0.07550 118 PHE A C   
797  O O   . PHE A 111 ? 0.24060 0.44799 0.31238 -0.10993 -0.02609 -0.08239 118 PHE A O   
798  C CB  . PHE A 111 ? 0.16268 0.30714 0.24529 -0.07651 -0.00630 -0.06668 118 PHE A CB  
799  C CG  . PHE A 111 ? 0.19151 0.33858 0.26223 -0.06742 -0.00964 -0.06494 118 PHE A CG  
800  C CD1 . PHE A 111 ? 0.21256 0.34947 0.26689 -0.07543 -0.00862 -0.07619 118 PHE A CD1 
801  C CD2 . PHE A 111 ? 0.22355 0.37801 0.29706 -0.05079 -0.01172 -0.05232 118 PHE A CD2 
802  C CE1 . PHE A 111 ? 0.20124 0.33911 0.24225 -0.06828 -0.00946 -0.07379 118 PHE A CE1 
803  C CE2 . PHE A 111 ? 0.19203 0.34396 0.25201 -0.04400 -0.01317 -0.04960 118 PHE A CE2 
804  C CZ  . PHE A 111 ? 0.24107 0.38594 0.28474 -0.05336 -0.01180 -0.05993 118 PHE A CZ  
805  N N   . MET A 112 ? 0.28131 0.51299 0.38736 -0.09992 -0.02353 -0.06638 119 MET A N   
806  C CA  . MET A 112 ? 0.42523 0.69977 0.53743 -0.09874 -0.03578 -0.06170 119 MET A CA  
807  C C   . MET A 112 ? 0.41481 0.69685 0.52158 -0.11732 -0.03999 -0.07053 119 MET A C   
808  O O   . MET A 112 ? 0.34004 0.64454 0.43987 -0.11798 -0.05082 -0.07004 119 MET A O   
809  C CB  . MET A 112 ? 0.40669 0.70661 0.54126 -0.08416 -0.03593 -0.04853 119 MET A CB  
810  C CG  . MET A 112 ? 0.15858 0.45086 0.29034 -0.06062 -0.03545 -0.03726 119 MET A CG  
811  S SD  . MET A 112 ? 0.68904 1.01321 0.84670 -0.04344 -0.03527 -0.02437 119 MET A SD  
812  C CE  . MET A 112 ? 0.23188 0.52662 0.37780 -0.01759 -0.03129 -0.01341 119 MET A CE  
813  N N   . GLU A 113 ? 0.26839 0.53036 0.37645 -0.13249 -0.03184 -0.07826 120 GLU A N   
814  C CA  . GLU A 113 ? 0.39184 0.65397 0.49141 -0.15139 -0.03465 -0.08859 120 GLU A CA  
815  C C   . GLU A 113 ? 0.41377 0.65416 0.48670 -0.15612 -0.03605 -0.09935 120 GLU A C   
816  O O   . GLU A 113 ? 0.39282 0.64741 0.45523 -0.16502 -0.04400 -0.10486 120 GLU A O   
817  C CB  . GLU A 113 ? 0.40271 0.64171 0.50661 -0.16582 -0.02429 -0.09344 120 GLU A CB  
818  C CG  . GLU A 113 ? 0.57260 0.83471 0.70121 -0.16350 -0.02106 -0.08367 120 GLU A CG  
819  C CD  . GLU A 113 ? 0.70629 0.94645 0.83641 -0.18017 -0.01068 -0.08748 120 GLU A CD  
820  O OE1 . GLU A 113 ? 0.84907 1.11608 0.99629 -0.18850 -0.01053 -0.08502 120 GLU A OE1 
821  O OE2 . GLU A 113 ? 0.77845 0.97399 0.89268 -0.18434 -0.00247 -0.09254 120 GLU A OE2 
822  N N   . ALA A 114 ? 0.31275 0.51953 0.37472 -0.14978 -0.02803 -0.10281 121 ALA A N   
823  C CA  . ALA A 114 ? 0.27231 0.45738 0.30949 -0.15248 -0.02650 -0.11368 121 ALA A CA  
824  C C   . ALA A 114 ? 0.31567 0.52802 0.34226 -0.14582 -0.03700 -0.10928 121 ALA A C   
825  O O   . ALA A 114 ? 0.41508 0.62519 0.42047 -0.15353 -0.03983 -0.11747 121 ALA A O   
826  C CB  . ALA A 114 ? 0.27269 0.41920 0.30506 -0.14422 -0.01520 -0.11763 121 ALA A CB  
827  N N   . LEU A 115 ? 0.30715 0.54377 0.34634 -0.13090 -0.04272 -0.09556 122 LEU A N   
828  C CA  . LEU A 115 ? 0.31348 0.57150 0.33940 -0.12228 -0.05292 -0.08851 122 LEU A CA  
829  C C   . LEU A 115 ? 0.51441 0.80202 0.53717 -0.12906 -0.06540 -0.08700 122 LEU A C   
830  O O   . LEU A 115 ? 0.41194 0.70328 0.41089 -0.13151 -0.07186 -0.08901 122 LEU A O   
831  C CB  . LEU A 115 ? 0.27485 0.54700 0.31541 -0.10195 -0.05544 -0.07208 122 LEU A CB  
832  C CG  . LEU A 115 ? 0.20580 0.43803 0.24263 -0.08852 -0.04178 -0.06901 122 LEU A CG  
833  C CD1 . LEU A 115 ? 0.28069 0.51981 0.33130 -0.06773 -0.04261 -0.05181 122 LEU A CD1 
834  C CD2 . LEU A 115 ? 0.25249 0.46307 0.26157 -0.08895 -0.03747 -0.07464 122 LEU A CD2 
835  N N   . GLN A 116 ? 0.44431 0.75350 0.49036 -0.13243 -0.06867 -0.08367 123 GLN A N   
836  C CA  . GLN A 116 ? 0.52180 0.86039 0.56805 -0.14052 -0.08079 -0.08438 123 GLN A CA  
837  C C   . GLN A 116 ? 0.53304 0.85423 0.55992 -0.16162 -0.07884 -0.10102 123 GLN A C   
838  O O   . GLN A 116 ? 0.73177 1.07456 0.75198 -0.16972 -0.08999 -0.10364 123 GLN A O   
839  C CB  . GLN A 116 ? 0.59801 0.96553 0.67651 -0.13931 -0.08312 -0.07789 123 GLN A CB  
840  C CG  . GLN A 116 ? 0.63579 1.02701 0.73220 -0.11604 -0.08780 -0.06091 123 GLN A CG  
841  C CD  . GLN A 116 ? 0.97459 1.40840 1.09259 -0.11263 -0.09902 -0.05451 123 GLN A CD  
842  O OE1 . GLN A 116 ? 1.08917 1.53692 1.22113 -0.12814 -0.09886 -0.06171 123 GLN A OE1 
843  N NE2 . GLN A 116 ? 0.87308 1.32669 0.99409 -0.09193 -0.10866 -0.04085 123 GLN A NE2 
844  N N   . ALA A 117 ? 0.58814 0.86966 0.60536 -0.16933 -0.06526 -0.11219 124 ALA A N   
845  C CA  . ALA A 117 ? 0.55831 0.81633 0.55703 -0.18732 -0.06086 -0.12837 124 ALA A CA  
846  C C   . ALA A 117 ? 0.85600 1.08389 0.82517 -0.18562 -0.05415 -0.13706 124 ALA A C   
847  O O   . ALA A 117 ? 0.71933 0.91392 0.67559 -0.19501 -0.04420 -0.15054 124 ALA A O   
848  C CB  . ALA A 117 ? 0.57192 0.80437 0.58257 -0.19708 -0.04952 -0.13453 124 ALA A CB  
849  N N   . GLY A 118 ? 0.64576 0.88343 0.60375 -0.17290 -0.05835 -0.12919 125 GLY A N   
850  C CA  . GLY A 118 ? 0.63278 0.84901 0.56049 -0.17247 -0.05262 -0.13680 125 GLY A CA  
851  C C   . GLY A 118 ? 0.60438 0.80128 0.53044 -0.15873 -0.04223 -0.13357 125 GLY A C   
852  O O   . GLY A 118 ? 0.51129 0.70287 0.41409 -0.15459 -0.03998 -0.13379 125 GLY A O   
853  N N   . ALA A 119 ? 0.39958 0.58567 0.34895 -0.15226 -0.03552 -0.13063 126 ALA A N   
854  C CA  . ALA A 119 ? 0.31209 0.47734 0.26282 -0.14047 -0.02502 -0.13020 126 ALA A CA  
855  C C   . ALA A 119 ? 0.35642 0.54214 0.30237 -0.12777 -0.03173 -0.11631 126 ALA A C   
856  O O   . ALA A 119 ? 0.37501 0.59272 0.32178 -0.12541 -0.04579 -0.10484 126 ALA A O   
857  C CB  . ALA A 119 ? 0.31138 0.46297 0.28854 -0.13612 -0.01902 -0.12816 126 ALA A CB  
858  N N   . ASP A 120 ? 0.37895 0.54080 0.32278 -0.11479 -0.01969 -0.11294 127 ASP A N   
859  C CA  . ASP A 120 ? 0.35946 0.52695 0.30089 -0.09883 -0.02115 -0.09533 127 ASP A CA  
860  C C   . ASP A 120 ? 0.27297 0.42250 0.23741 -0.08429 -0.01231 -0.08798 127 ASP A C   
861  O O   . ASP A 120 ? 0.28927 0.42114 0.26822 -0.08561 -0.00496 -0.09639 127 ASP A O   
862  C CB  . ASP A 120 ? 0.40463 0.56339 0.31501 -0.10050 -0.01522 -0.09815 127 ASP A CB  
863  C CG  . ASP A 120 ? 0.58283 0.71303 0.49159 -0.10181 0.00267  -0.11270 127 ASP A CG  
864  O OD1 . ASP A 120 ? 0.57272 0.69234 0.47756 -0.11324 0.00723  -0.13083 127 ASP A OD1 
865  O OD2 . ASP A 120 ? 0.52906 0.64743 0.44328 -0.09097 0.01217  -0.10627 127 ASP A OD2 
866  N N   . ILE A 121 ? 0.25209 0.40405 0.21712 -0.07048 -0.01362 -0.07198 128 ILE A N   
867  C CA  . ILE A 121 ? 0.21840 0.35719 0.20425 -0.05708 -0.00828 -0.06374 128 ILE A CA  
868  C C   . ILE A 121 ? 0.25997 0.37347 0.25003 -0.05635 0.00524  -0.07372 128 ILE A C   
869  O O   . ILE A 121 ? 0.27405 0.37572 0.28324 -0.04907 0.00871  -0.07237 128 ILE A O   
870  C CB  . ILE A 121 ? 0.25259 0.39608 0.23371 -0.04408 -0.01248 -0.04578 128 ILE A CB  
871  C CG1 . ILE A 121 ? 0.30487 0.47484 0.29496 -0.03921 -0.02593 -0.03538 128 ILE A CG1 
872  C CG2 . ILE A 121 ? 0.25188 0.37552 0.24593 -0.03293 -0.00447 -0.04024 128 ILE A CG2 
873  C CD1 . ILE A 121 ? 0.35662 0.53290 0.33683 -0.02602 -0.03279 -0.01781 128 ILE A CD1 
874  N N   . SER A 122 ? 0.30030 0.40657 0.27288 -0.06337 0.01303  -0.08435 129 SER A N   
875  C CA  . SER A 122 ? 0.33727 0.42426 0.31804 -0.06095 0.02633  -0.09477 129 SER A CA  
876  C C   . SER A 122 ? 0.32522 0.39892 0.32220 -0.06206 0.02834  -0.10558 129 SER A C   
877  O O   . SER A 122 ? 0.30468 0.36330 0.31539 -0.05513 0.03640  -0.11071 129 SER A O   
878  C CB  . SER A 122 ? 0.29807 0.38208 0.25679 -0.06863 0.03633  -0.10592 129 SER A CB  
879  O OG  . SER A 122 ? 0.32806 0.40930 0.27521 -0.07998 0.03688  -0.12180 129 SER A OG  
880  N N   . MET A 123 ? 0.26409 0.34271 0.26012 -0.07075 0.02109  -0.10878 130 MET A N   
881  C CA  . MET A 123 ? 0.22714 0.28729 0.23491 -0.07302 0.02404  -0.11770 130 MET A CA  
882  C C   . MET A 123 ? 0.22797 0.28621 0.25546 -0.06485 0.01970  -0.10587 130 MET A C   
883  O O   . MET A 123 ? 0.24806 0.29030 0.28250 -0.06771 0.02105  -0.11018 130 MET A O   
884  C CB  . MET A 123 ? 0.38143 0.44258 0.37646 -0.09029 0.02104  -0.12999 130 MET A CB  
885  C CG  . MET A 123 ? 0.36223 0.42862 0.33173 -0.09956 0.02364  -0.14103 130 MET A CG  
886  S SD  . MET A 123 ? 0.46263 0.54281 0.41319 -0.12139 0.01421  -0.15127 130 MET A SD  
887  C CE  . MET A 123 ? 0.44243 0.49048 0.40569 -0.12428 0.02076  -0.15823 130 MET A CE  
888  N N   . ILE A 124 ? 0.18460 0.25445 0.21853 -0.05456 0.01591  -0.09147 131 ILE A N   
889  C CA  . ILE A 124 ? 0.19454 0.26423 0.24351 -0.04693 0.01221  -0.08044 131 ILE A CA  
890  C C   . ILE A 124 ? 0.22449 0.26910 0.28354 -0.04141 0.01715  -0.08395 131 ILE A C   
891  O O   . ILE A 124 ? 0.18428 0.22277 0.25003 -0.04125 0.01537  -0.07953 131 ILE A O   
892  C CB  . ILE A 124 ? 0.19304 0.27244 0.24394 -0.03557 0.00948  -0.06689 131 ILE A CB  
893  C CG1 . ILE A 124 ? 0.20549 0.28497 0.26885 -0.02782 0.00656  -0.05691 131 ILE A CG1 
894  C CG2 . ILE A 124 ? 0.17505 0.24236 0.22523 -0.02913 0.01618  -0.06876 131 ILE A CG2 
895  C CD1 . ILE A 124 ? 0.22288 0.31076 0.28607 -0.01724 0.00357  -0.04436 131 ILE A CD1 
896  N N   . GLY A 125 ? 0.23841 0.26942 0.29872 -0.03611 0.02342  -0.09119 132 GLY A N   
897  C CA  . GLY A 125 ? 0.22329 0.23258 0.29416 -0.02771 0.02601  -0.09330 132 GLY A CA  
898  C C   . GLY A 125 ? 0.27964 0.26853 0.34740 -0.03428 0.02754  -0.10045 132 GLY A C   
899  O O   . GLY A 125 ? 0.28621 0.25600 0.35954 -0.02777 0.02685  -0.09698 132 GLY A O   
900  N N   . GLN A 126 ? 0.22967 0.22017 0.28610 -0.04800 0.02922  -0.11009 133 GLN A N   
901  C CA  . GLN A 126 ? 0.25436 0.22210 0.30569 -0.05749 0.03129  -0.11746 133 GLN A CA  
902  C C   . GLN A 126 ? 0.31983 0.28962 0.37438 -0.06335 0.02674  -0.10701 133 GLN A C   
903  O O   . GLN A 126 ? 0.31713 0.26370 0.36747 -0.07150 0.02930  -0.11050 133 GLN A O   
904  C CB  . GLN A 126 ? 0.31076 0.28147 0.34742 -0.07347 0.03353  -0.13166 133 GLN A CB  
905  C CG  . GLN A 126 ? 0.45155 0.41899 0.48225 -0.06814 0.04070  -0.14266 133 GLN A CG  
906  C CD  . GLN A 126 ? 0.48504 0.45527 0.49680 -0.08171 0.04231  -0.15264 133 GLN A CD  
907  O OE1 . GLN A 126 ? 0.51572 0.47339 0.52004 -0.09218 0.04115  -0.15556 133 GLN A OE1 
908  N NE2 . GLN A 126 ? 0.54792 0.53325 0.54985 -0.08228 0.04539  -0.15791 133 GLN A NE2 
909  N N   . PHE A 127 ? 0.28517 0.28051 0.34619 -0.05969 0.02144  -0.09469 134 PHE A N   
910  C CA  . PHE A 127 ? 0.23866 0.24165 0.30437 -0.06469 0.01904  -0.08523 134 PHE A CA  
911  C C   . PHE A 127 ? 0.26464 0.26061 0.33625 -0.04980 0.01842  -0.07321 134 PHE A C   
912  O O   . PHE A 127 ? 0.25835 0.26396 0.33346 -0.05100 0.01769  -0.06427 134 PHE A O   
913  C CB  . PHE A 127 ? 0.21256 0.25351 0.28125 -0.07234 0.01353  -0.08196 134 PHE A CB  
914  C CG  . PHE A 127 ? 0.20454 0.25497 0.26469 -0.08816 0.01189  -0.09410 134 PHE A CG  
915  C CD1 . PHE A 127 ? 0.38210 0.42877 0.44032 -0.10699 0.01280  -0.10159 134 PHE A CD1 
916  C CD2 . PHE A 127 ? 0.27344 0.33323 0.32462 -0.08576 0.01024  -0.09897 134 PHE A CD2 
917  C CE1 . PHE A 127 ? 0.39051 0.44482 0.43835 -0.12330 0.01045  -0.11475 134 PHE A CE1 
918  C CE2 . PHE A 127 ? 0.22587 0.29295 0.26452 -0.10061 0.00845  -0.11103 134 PHE A CE2 
919  C CZ  . PHE A 127 ? 0.31794 0.38254 0.35486 -0.11952 0.00787  -0.11970 134 PHE A CZ  
920  N N   . GLY A 128 ? 0.21664 0.19842 0.28976 -0.03621 0.01887  -0.07365 135 GLY A N   
921  C CA  . GLY A 128 ? 0.21939 0.19029 0.29536 -0.02377 0.01705  -0.06436 135 GLY A CA  
922  C C   . GLY A 128 ? 0.22433 0.21578 0.30408 -0.01671 0.01383  -0.05497 135 GLY A C   
923  O O   . GLY A 128 ? 0.23910 0.22218 0.31799 -0.00891 0.01233  -0.04759 135 GLY A O   
924  N N   . VAL A 129 ? 0.17771 0.19306 0.25897 -0.01878 0.01261  -0.05498 136 VAL A N   
925  C CA  . VAL A 129 ? 0.13723 0.16818 0.22050 -0.01106 0.01013  -0.04592 136 VAL A CA  
926  C C   . VAL A 129 ? 0.17688 0.21365 0.25930 -0.00658 0.00965  -0.04738 136 VAL A C   
927  O O   . VAL A 129 ? 0.14113 0.19156 0.22170 -0.00322 0.00785  -0.04111 136 VAL A O   
928  C CB  . VAL A 129 ? 0.12391 0.17873 0.20947 -0.01650 0.00892  -0.04110 136 VAL A CB  
929  C CG1 . VAL A 129 ? 0.16745 0.21770 0.25486 -0.02090 0.01179  -0.03798 136 VAL A CG1 
930  C CG2 . VAL A 129 ? 0.18193 0.25232 0.26586 -0.02856 0.00729  -0.04806 136 VAL A CG2 
931  N N   . GLY A 130 ? 0.20622 0.21975 0.21773 -0.00981 0.00244  -0.04344 137 GLY A N   
932  C CA  . GLY A 130 ? 0.18290 0.19758 0.18776 -0.00439 0.00217  -0.03954 137 GLY A CA  
933  C C   . GLY A 130 ? 0.19423 0.20573 0.19793 -0.00103 0.00179  -0.03090 137 GLY A C   
934  O O   . GLY A 130 ? 0.17369 0.18858 0.17333 0.00360  0.00151  -0.02666 137 GLY A O   
935  N N   . PHE A 131 ? 0.14494 0.15011 0.15222 -0.00304 0.00198  -0.02831 138 PHE A N   
936  C CA  . PHE A 131 ? 0.14559 0.14713 0.15258 -0.00029 0.00097  -0.02231 138 PHE A CA  
937  C C   . PHE A 131 ? 0.15966 0.16838 0.16433 0.00400  -0.00097 -0.02076 138 PHE A C   
938  O O   . PHE A 131 ? 0.17112 0.17714 0.17501 0.00745  -0.00090 -0.01528 138 PHE A O   
939  C CB  . PHE A 131 ? 0.18538 0.18204 0.19490 -0.00223 0.00076  -0.02191 138 PHE A CB  
940  C CG  . PHE A 131 ? 0.22638 0.22062 0.23558 0.00071  -0.00115 -0.01883 138 PHE A CG  
941  C CD1 . PHE A 131 ? 0.21110 0.19866 0.22172 0.00144  -0.00162 -0.01516 138 PHE A CD1 
942  C CD2 . PHE A 131 ? 0.20307 0.20195 0.21180 0.00281  -0.00240 -0.02009 138 PHE A CD2 
943  C CE1 . PHE A 131 ? 0.16939 0.15308 0.18121 0.00355  -0.00350 -0.01373 138 PHE A CE1 
944  C CE2 . PHE A 131 ? 0.19038 0.18528 0.19899 0.00614  -0.00390 -0.01824 138 PHE A CE2 
945  C CZ  . PHE A 131 ? 0.22206 0.20848 0.23231 0.00621  -0.00456 -0.01552 138 PHE A CZ  
946  N N   . TYR A 132 ? 0.14583 0.16408 0.15065 0.00395  -0.00247 -0.02508 139 TYR A N   
947  C CA  . TYR A 132 ? 0.14554 0.17151 0.14875 0.00915  -0.00443 -0.02299 139 TYR A CA  
948  C C   . TYR A 132 ? 0.17287 0.20496 0.17093 0.01423  -0.00464 -0.01995 139 TYR A C   
949  O O   . TYR A 132 ? 0.18152 0.21801 0.17778 0.02006  -0.00554 -0.01551 139 TYR A O   
950  C CB  . TYR A 132 ? 0.11671 0.15398 0.12305 0.00787  -0.00610 -0.02835 139 TYR A CB  
951  C CG  . TYR A 132 ? 0.17979 0.21193 0.19055 0.00418  -0.00473 -0.02932 139 TYR A CG  
952  C CD1 . TYR A 132 ? 0.14925 0.17838 0.15994 0.00767  -0.00488 -0.02632 139 TYR A CD1 
953  C CD2 . TYR A 132 ? 0.18262 0.21203 0.19712 -0.00206 -0.00273 -0.03281 139 TYR A CD2 
954  C CE1 . TYR A 132 ? 0.15799 0.18389 0.17079 0.00550  -0.00331 -0.02709 139 TYR A CE1 
955  C CE2 . TYR A 132 ? 0.21952 0.24509 0.23693 -0.00432 -0.00064 -0.03191 139 TYR A CE2 
956  C CZ  . TYR A 132 ? 0.18084 0.20568 0.19660 -0.00030 -0.00105 -0.02917 139 TYR A CZ  
957  O OH  . TYR A 132 ? 0.18299 0.20584 0.19981 -0.00137 0.00123  -0.02833 139 TYR A OH  
958  N N   . SER A 133 ? 0.14461 0.17686 0.13988 0.01310  -0.00328 -0.02152 140 SER A N   
959  C CA  . SER A 133 ? 0.17880 0.21665 0.16788 0.01890  -0.00236 -0.01708 140 SER A CA  
960  C C   . SER A 133 ? 0.18127 0.21028 0.17149 0.02213  0.00018  -0.00678 140 SER A C   
961  O O   . SER A 133 ? 0.15578 0.18954 0.14162 0.02803  0.00179  -0.00033 140 SER A O   
962  C CB  . SER A 133 ? 0.19477 0.23371 0.18045 0.01755  -0.00059 -0.02118 140 SER A CB  
963  O OG  . SER A 133 ? 0.19407 0.22090 0.18321 0.01470  0.00261  -0.01797 140 SER A OG  
964  N N   . ALA A 134 ? 0.16335 0.18025 0.15973 0.01849  0.00064  -0.00514 141 ALA A N   
965  C CA  . ALA A 134 ? 0.17831 0.18650 0.17841 0.02064  0.00226  0.00306  141 ALA A CA  
966  C C   . ALA A 134 ? 0.14775 0.15997 0.14581 0.02748  0.00199  0.00838  141 ALA A C   
967  O O   . ALA A 134 ? 0.15853 0.16650 0.15808 0.03112  0.00483  0.01719  141 ALA A O   
968  C CB  . ALA A 134 ? 0.15348 0.15069 0.15984 0.01619  0.00096  0.00095  141 ALA A CB  
969  N N   . TYR A 135 ? 0.15833 0.17908 0.15413 0.02959  -0.00097 0.00390  142 TYR A N   
970  C CA  . TYR A 135 ? 0.16589 0.19095 0.16037 0.03719  -0.00139 0.00914  142 TYR A CA  
971  C C   . TYR A 135 ? 0.16556 0.20342 0.15277 0.04420  -0.00061 0.01425  142 TYR A C   
972  O O   . TYR A 135 ? 0.17344 0.21637 0.15873 0.05207  -0.00067 0.02025  142 TYR A O   
973  C CB  . TYR A 135 ? 0.14029 0.17190 0.13622 0.03753  -0.00464 0.00286  142 TYR A CB  
974  C CG  . TYR A 135 ? 0.16739 0.18583 0.16880 0.03364  -0.00456 0.00040  142 TYR A CG  
975  C CD1 . TYR A 135 ? 0.16522 0.17325 0.16977 0.03772  -0.00370 0.00473  142 TYR A CD1 
976  C CD2 . TYR A 135 ? 0.13758 0.15317 0.14072 0.02634  -0.00507 -0.00607 142 TYR A CD2 
977  C CE1 . TYR A 135 ? 0.19443 0.19106 0.20288 0.03459  -0.00420 0.00079  142 TYR A CE1 
978  C CE2 . TYR A 135 ? 0.15679 0.16216 0.16313 0.02381  -0.00523 -0.00827 142 TYR A CE2 
979  C CZ  . TYR A 135 ? 0.20131 0.19790 0.20982 0.02787  -0.00517 -0.00561 142 TYR A CZ  
980  O OH  . TYR A 135 ? 0.17636 0.16429 0.18683 0.02582  -0.00596 -0.00950 142 TYR A OH  
981  N N   . LEU A 136 ? 0.21220 0.25536 0.19479 0.04256  0.00046  0.01249  143 LEU A N   
982  C CA  . LEU A 136 ? 0.17417 0.22832 0.14855 0.05016  0.00228  0.01883  143 LEU A CA  
983  C C   . LEU A 136 ? 0.20765 0.25196 0.18438 0.05443  0.00772  0.03267  143 LEU A C   
984  O O   . LEU A 136 ? 0.20541 0.25766 0.17628 0.06335  0.00979  0.04178  143 LEU A O   
985  C CB  . LEU A 136 ? 0.18165 0.24210 0.15061 0.04748  0.00281  0.01273  143 LEU A CB  
986  C CG  . LEU A 136 ? 0.16100 0.23274 0.12757 0.04387  -0.00205 -0.00107 143 LEU A CG  
987  C CD1 . LEU A 136 ? 0.20175 0.27304 0.16506 0.04052  -0.00022 -0.00699 143 LEU A CD1 
988  C CD2 . LEU A 136 ? 0.20066 0.29235 0.16038 0.05118  -0.00617 -0.00291 143 LEU A CD2 
989  N N   . VAL A 137 ? 0.18140 0.20918 0.16737 0.04830  0.01013  0.03469  144 VAL A N   
990  C CA  . VAL A 137 ? 0.19636 0.21395 0.18803 0.05023  0.01569  0.04710  144 VAL A CA  
991  C C   . VAL A 137 ? 0.22023 0.22097 0.22300 0.04733  0.01559  0.04878  144 VAL A C   
992  O O   . VAL A 137 ? 0.23899 0.23042 0.24824 0.04961  0.02010  0.05938  144 VAL A O   
993  C CB  . VAL A 137 ? 0.20018 0.21584 0.19429 0.04587  0.01970  0.04904  144 VAL A CB  
994  C CG1 . VAL A 137 ? 0.25061 0.28273 0.23250 0.05085  0.02089  0.04826  144 VAL A CG1 
995  C CG2 . VAL A 137 ? 0.16799 0.17571 0.16875 0.03630  0.01697  0.03925  144 VAL A CG2 
996  N N   . ALA A 138 ? 0.21354 0.20961 0.21919 0.04262  0.01107  0.03888  145 ALA A N   
997  C CA  . ALA A 138 ? 0.18749 0.16780 0.20271 0.03972  0.01049  0.03807  145 ALA A CA  
998  C C   . ALA A 138 ? 0.20226 0.18318 0.21563 0.04556  0.00819  0.03639  145 ALA A C   
999  O O   . ALA A 138 ? 0.25040 0.24378 0.25737 0.04731  0.00493  0.03028  145 ALA A O   
1000 C CB  . ALA A 138 ? 0.18562 0.16078 0.20481 0.03094  0.00746  0.02829  145 ALA A CB  
1001 N N   . GLU A 139 ? 0.19210 0.15969 0.21237 0.04868  0.01020  0.04178  146 GLU A N   
1002 C CA  . GLU A 139 ? 0.19954 0.16546 0.21940 0.05423  0.00815  0.03881  146 GLU A CA  
1003 C C   . GLU A 139 ? 0.23067 0.18980 0.25354 0.04853  0.00446  0.02707  146 GLU A C   
1004 O O   . GLU A 139 ? 0.26765 0.23051 0.28814 0.05237  0.00233  0.02200  146 GLU A O   
1005 C CB  . GLU A 139 ? 0.24522 0.19807 0.27121 0.06105  0.01218  0.04885  146 GLU A CB  
1006 C CG  . GLU A 139 ? 0.35349 0.28698 0.39152 0.05500  0.01498  0.05129  146 GLU A CG  
1007 C CD  . GLU A 139 ? 0.72861 0.64856 0.77404 0.06165  0.02043  0.06338  146 GLU A CD  
1008 O OE1 . GLU A 139 ? 0.52112 0.44977 0.56021 0.07153  0.02307  0.07335  146 GLU A OE1 
1009 O OE2 . GLU A 139 ? 0.63722 0.53807 0.69527 0.05716  0.02202  0.06287  146 GLU A OE2 
1010 N N   . LYS A 140 ? 0.20367 0.15456 0.23160 0.04022  0.00383  0.02305  147 LYS A N   
1011 C CA  . LYS A 140 ? 0.20063 0.14658 0.22999 0.03544  0.00024  0.01239  147 LYS A CA  
1012 C C   . LYS A 140 ? 0.18890 0.13708 0.21905 0.02725  -0.00087 0.00921  147 LYS A C   
1013 O O   . LYS A 140 ? 0.19776 0.14421 0.23217 0.02452  0.00154  0.01512  147 LYS A O   
1014 C CB  . LYS A 140 ? 0.19322 0.12173 0.23090 0.03588  0.00016  0.01050  147 LYS A CB  
1015 C CG  . LYS A 140 ? 0.20797 0.13197 0.24598 0.03196  -0.00389 -0.00116 147 LYS A CG  
1016 C CD  . LYS A 140 ? 0.35150 0.25840 0.39731 0.03409  -0.00388 -0.00366 147 LYS A CD  
1017 C CE  . LYS A 140 ? 0.45181 0.34877 0.50580 0.02649  -0.00675 -0.01040 147 LYS A CE  
1018 N NZ  . LYS A 140 ? 0.49062 0.36882 0.55648 0.02732  -0.00521 -0.00959 147 LYS A NZ  
1019 N N   . VAL A 141 ? 0.15252 0.10547 0.17871 0.02411  -0.00386 0.00092  148 VAL A N   
1020 C CA  . VAL A 141 ? 0.15814 0.11285 0.18508 0.01744  -0.00493 -0.00188 148 VAL A CA  
1021 C C   . VAL A 141 ? 0.22734 0.17692 0.25529 0.01493  -0.00838 -0.00992 148 VAL A C   
1022 O O   . VAL A 141 ? 0.16283 0.11471 0.18597 0.01789  -0.00964 -0.01490 148 VAL A O   
1023 C CB  . VAL A 141 ? 0.17417 0.14137 0.19430 0.01640  -0.00450 -0.00297 148 VAL A CB  
1024 C CG1 . VAL A 141 ? 0.15817 0.12535 0.17970 0.01056  -0.00507 -0.00518 148 VAL A CG1 
1025 C CG2 . VAL A 141 ? 0.14661 0.12124 0.16388 0.01984  -0.00188 0.00333  148 VAL A CG2 
1026 N N   . THR A 142 ? 0.17639 0.12065 0.21069 0.01001  -0.00990 -0.01118 149 THR A N   
1027 C CA  . THR A 142 ? 0.17805 0.12010 0.21257 0.00768  -0.01401 -0.01913 149 THR A CA  
1028 C C   . THR A 142 ? 0.19698 0.14643 0.22980 0.00383  -0.01471 -0.01922 149 THR A C   
1029 O O   . THR A 142 ? 0.22602 0.17682 0.26386 0.00100  -0.01299 -0.01425 149 THR A O   
1030 C CB  . THR A 142 ? 0.20183 0.13279 0.24686 0.00521  -0.01627 -0.02178 149 THR A CB  
1031 O OG1 . THR A 142 ? 0.25377 0.17542 0.30187 0.00922  -0.01438 -0.01999 149 THR A OG1 
1032 C CG2 . THR A 142 ? 0.23480 0.16547 0.27781 0.00428  -0.02159 -0.03206 149 THR A CG2 
1033 N N   . VAL A 143 ? 0.16314 0.11762 0.18894 0.00450  -0.01650 -0.02399 150 VAL A N   
1034 C CA  . VAL A 143 ? 0.17221 0.13263 0.19638 0.00198  -0.01679 -0.02332 150 VAL A CA  
1035 C C   . VAL A 143 ? 0.23492 0.19559 0.25855 0.00176  -0.02152 -0.02932 150 VAL A C   
1036 O O   . VAL A 143 ? 0.21169 0.17337 0.22855 0.00500  -0.02294 -0.03424 150 VAL A O   
1037 C CB  . VAL A 143 ? 0.15915 0.12627 0.17576 0.00320  -0.01379 -0.02198 150 VAL A CB  
1038 C CG1 . VAL A 143 ? 0.15779 0.12867 0.17347 0.00130  -0.01347 -0.02059 150 VAL A CG1 
1039 C CG2 . VAL A 143 ? 0.19734 0.16638 0.21404 0.00369  -0.01035 -0.01803 150 VAL A CG2 
1040 N N   . ILE A 144 ? 0.16231 0.12383 0.19295 -0.00147 -0.02402 -0.02912 151 ILE A N   
1041 C CA  . ILE A 144 ? 0.16967 0.13463 0.19992 -0.00146 -0.02954 -0.03510 151 ILE A CA  
1042 C C   . ILE A 144 ? 0.23610 0.20926 0.26258 -0.00093 -0.02871 -0.03125 151 ILE A C   
1043 O O   . ILE A 144 ? 0.17368 0.14811 0.20537 -0.00300 -0.02591 -0.02548 151 ILE A O   
1044 C CB  . ILE A 144 ? 0.18038 0.14226 0.22374 -0.00567 -0.03380 -0.03830 151 ILE A CB  
1045 C CG1 . ILE A 144 ? 0.31614 0.26713 0.36727 -0.00711 -0.03212 -0.03813 151 ILE A CG1 
1046 C CG2 . ILE A 144 ? 0.22325 0.19027 0.26497 -0.00493 -0.04113 -0.04739 151 ILE A CG2 
1047 C CD1 . ILE A 144 ? 0.26792 0.21251 0.31438 -0.00387 -0.03433 -0.04584 151 ILE A CD1 
1048 N N   . THR A 145 ? 0.13932 0.11807 0.15681 0.00258  -0.03073 -0.03399 152 THR A N   
1049 C CA  . THR A 145 ? 0.16116 0.14616 0.17457 0.00417  -0.02847 -0.02848 152 THR A CA  
1050 C C   . THR A 145 ? 0.20378 0.19687 0.21099 0.00800  -0.03318 -0.03156 152 THR A C   
1051 O O   . THR A 145 ? 0.20609 0.20049 0.20738 0.01062  -0.03675 -0.03835 152 THR A O   
1052 C CB  . THR A 145 ? 0.20420 0.18785 0.21100 0.00544  -0.02193 -0.02396 152 THR A CB  
1053 O OG1 . THR A 145 ? 0.19966 0.18552 0.20650 0.00565  -0.01849 -0.01781 152 THR A OG1 
1054 C CG2 . THR A 145 ? 0.20180 0.18812 0.19859 0.00945  -0.02145 -0.02669 152 THR A CG2 
1055 N N   . LYS A 146 ? 0.16677 0.16591 0.17501 0.00920  -0.03312 -0.02654 153 LYS A N   
1056 C CA  . LYS A 146 ? 0.19695 0.20623 0.19868 0.01418  -0.03733 -0.02730 153 LYS A CA  
1057 C C   . LYS A 146 ? 0.20789 0.21972 0.20613 0.01747  -0.03201 -0.01756 153 LYS A C   
1058 O O   . LYS A 146 ? 0.19639 0.20763 0.20273 0.01581  -0.03024 -0.01277 153 LYS A O   
1059 C CB  . LYS A 146 ? 0.18052 0.19679 0.19133 0.01251  -0.04541 -0.03256 153 LYS A CB  
1060 C CG  . LYS A 146 ? 0.21493 0.24509 0.21858 0.01874  -0.05092 -0.03342 153 LYS A CG  
1061 C CD  . LYS A 146 ? 0.24237 0.27641 0.23311 0.02338  -0.05480 -0.04132 153 LYS A CD  
1062 C CE  . LYS A 146 ? 0.20290 0.25321 0.18532 0.03056  -0.06105 -0.04251 153 LYS A CE  
1063 N NZ  . LYS A 146 ? 0.18527 0.24074 0.15960 0.03702  -0.05532 -0.02989 153 LYS A NZ  
1064 N N   . HIS A 147 ? 0.18422 0.19878 0.17098 0.02256  -0.02899 -0.01436 154 HIS A N   
1065 C CA  . HIS A 147 ? 0.18988 0.20572 0.17307 0.02647  -0.02329 -0.00439 154 HIS A CA  
1066 C C   . HIS A 147 ? 0.25550 0.28396 0.23104 0.03390  -0.02801 -0.00298 154 HIS A C   
1067 O O   . HIS A 147 ? 0.23563 0.27132 0.20433 0.03654  -0.03398 -0.01027 154 HIS A O   
1068 C CB  . HIS A 147 ? 0.18482 0.19501 0.16224 0.02650  -0.01534 -0.00048 154 HIS A CB  
1069 C CG  . HIS A 147 ? 0.20775 0.21575 0.18394 0.02917  -0.00786 0.01008  154 HIS A CG  
1070 N ND1 . HIS A 147 ? 0.22806 0.24341 0.19585 0.03662  -0.00678 0.01684  154 HIS A ND1 
1071 C CD2 . HIS A 147 ? 0.22249 0.22116 0.20472 0.02561  -0.00064 0.01485  154 HIS A CD2 
1072 C CE1 . HIS A 147 ? 0.27010 0.27924 0.24012 0.03737  0.00132  0.02645  154 HIS A CE1 
1073 N NE2 . HIS A 147 ? 0.26990 0.26849 0.24908 0.03032  0.00494  0.02450  154 HIS A NE2 
1074 N N   . ASN A 148 ? 0.20482 0.23654 0.18131 0.03804  -0.02568 0.00593  155 ASN A N   
1075 C CA  . ASN A 148 ? 0.23439 0.28039 0.20311 0.04647  -0.03052 0.00838  155 ASN A CA  
1076 C C   . ASN A 148 ? 0.23776 0.28979 0.19080 0.05270  -0.02960 0.00862  155 ASN A C   
1077 O O   . ASN A 148 ? 0.25177 0.31797 0.19621 0.05925  -0.03655 0.00529  155 ASN A O   
1078 C CB  . ASN A 148 ? 0.23773 0.28471 0.20852 0.05170  -0.02585 0.02057  155 ASN A CB  
1079 C CG  . ASN A 148 ? 0.23989 0.28789 0.22450 0.04888  -0.02888 0.01993  155 ASN A CG  
1080 O OD1 . ASN A 148 ? 0.28916 0.34334 0.28090 0.04492  -0.03683 0.01098  155 ASN A OD1 
1081 N ND2 . ASN A 148 ? 0.27928 0.32120 0.26882 0.05102  -0.02212 0.02946  155 ASN A ND2 
1082 N N   . ASP A 149 ? 0.25538 0.29874 0.20460 0.05134  -0.02107 0.01265  156 ASP A N   
1083 C CA  . ASP A 149 ? 0.28032 0.33006 0.21527 0.05788  -0.01784 0.01541  156 ASP A CA  
1084 C C   . ASP A 149 ? 0.35791 0.40886 0.28770 0.05628  -0.02137 0.00368  156 ASP A C   
1085 O O   . ASP A 149 ? 0.31508 0.37147 0.23317 0.06172  -0.01771 0.00545  156 ASP A O   
1086 C CB  . ASP A 149 ? 0.28628 0.32751 0.22165 0.05753  -0.00553 0.02746  156 ASP A CB  
1087 C CG  . ASP A 149 ? 0.39547 0.43447 0.33407 0.06126  -0.00061 0.04025  156 ASP A CG  
1088 O OD1 . ASP A 149 ? 0.32232 0.37058 0.25884 0.06708  -0.00648 0.04171  156 ASP A OD1 
1089 O OD2 . ASP A 149 ? 0.41068 0.43859 0.35498 0.05832  0.00910  0.04844  156 ASP A OD2 
1090 N N   . ASP A 150 ? 0.24915 0.29500 0.18749 0.04963  -0.02750 -0.00750 157 ASP A N   
1091 C CA  . ASP A 150 ? 0.21802 0.26276 0.15253 0.04867  -0.03027 -0.01850 157 ASP A CA  
1092 C C   . ASP A 150 ? 0.31738 0.36217 0.25904 0.04496  -0.04061 -0.03112 157 ASP A C   
1093 O O   . ASP A 150 ? 0.28315 0.33087 0.23300 0.04293  -0.04554 -0.03105 157 ASP A O   
1094 C CB  . ASP A 150 ? 0.24915 0.28247 0.18938 0.04297  -0.02280 -0.01684 157 ASP A CB  
1095 C CG  . ASP A 150 ? 0.31527 0.35053 0.24725 0.04601  -0.02150 -0.02282 157 ASP A CG  
1096 O OD1 . ASP A 150 ? 0.31486 0.35737 0.23787 0.05129  -0.02756 -0.03144 157 ASP A OD1 
1097 O OD2 . ASP A 150 ? 0.34847 0.37875 0.28346 0.04333  -0.01451 -0.01953 157 ASP A OD2 
1098 N N   . GLU A 151 ? 0.30369 0.34537 0.24340 0.04420  -0.04354 -0.04194 158 GLU A N   
1099 C CA  . GLU A 151 ? 0.24780 0.28638 0.19621 0.03975  -0.05222 -0.05445 158 GLU A CA  
1100 C C   . GLU A 151 ? 0.19215 0.21652 0.15554 0.03102  -0.04925 -0.05333 158 GLU A C   
1101 O O   . GLU A 151 ? 0.22926 0.24742 0.19446 0.02900  -0.04141 -0.04487 158 GLU A O   
1102 C CB  . GLU A 151 ? 0.29564 0.33611 0.23449 0.04417  -0.05633 -0.06704 158 GLU A CB  
1103 C CG  . GLU A 151 ? 0.48077 0.53766 0.40393 0.05351  -0.06166 -0.07149 158 GLU A CG  
1104 C CD  . GLU A 151 ? 0.78117 0.84994 0.70708 0.05442  -0.06806 -0.06908 158 GLU A CD  
1105 O OE1 . GLU A 151 ? 0.82135 0.88816 0.76195 0.04769  -0.07480 -0.07502 158 GLU A OE1 
1106 O OE2 . GLU A 151 ? 0.86968 0.95076 0.78353 0.06239  -0.06610 -0.06066 158 GLU A OE2 
1107 N N   . GLN A 152 ? 0.24557 0.26539 0.22006 0.02593  -0.05558 -0.06214 159 GLN A N   
1108 C CA  . GLN A 152 ? 0.22032 0.22760 0.20860 0.01859  -0.05273 -0.06042 159 GLN A CA  
1109 C C   . GLN A 152 ? 0.24147 0.23895 0.22723 0.01912  -0.04946 -0.06425 159 GLN A C   
1110 O O   . GLN A 152 ? 0.25734 0.25374 0.23888 0.02190  -0.05357 -0.07463 159 GLN A O   
1111 C CB  . GLN A 152 ? 0.24888 0.25502 0.25221 0.01269  -0.05959 -0.06664 159 GLN A CB  
1112 C CG  . GLN A 152 ? 0.26200 0.25744 0.28003 0.00568  -0.05549 -0.06149 159 GLN A CG  
1113 C CD  . GLN A 152 ? 0.30287 0.30108 0.33760 -0.00029 -0.06056 -0.06351 159 GLN A CD  
1114 O OE1 . GLN A 152 ? 0.30893 0.31851 0.34564 0.00041  -0.06337 -0.06098 159 GLN A OE1 
1115 N NE2 . GLN A 152 ? 0.29009 0.27840 0.33790 -0.00590 -0.06136 -0.06749 159 GLN A NE2 
1116 N N   . TYR A 153 ? 0.19370 0.18463 0.18237 0.01692  -0.04238 -0.05651 160 TYR A N   
1117 C CA  . TYR A 153 ? 0.20762 0.19173 0.19399 0.01843  -0.03858 -0.05809 160 TYR A CA  
1118 C C   . TYR A 153 ? 0.23156 0.20575 0.22968 0.01334  -0.03615 -0.05470 160 TYR A C   
1119 O O   . TYR A 153 ? 0.20249 0.17646 0.20781 0.00914  -0.03456 -0.04822 160 TYR A O   
1120 C CB  . TYR A 153 ? 0.16739 0.15693 0.14419 0.02218  -0.03182 -0.05151 160 TYR A CB  
1121 C CG  . TYR A 153 ? 0.21221 0.21097 0.17571 0.02907  -0.03254 -0.05465 160 TYR A CG  
1122 C CD1 . TYR A 153 ? 0.29219 0.29076 0.24908 0.03409  -0.03307 -0.06231 160 TYR A CD1 
1123 C CD2 . TYR A 153 ? 0.30888 0.31688 0.26595 0.03162  -0.03217 -0.04942 160 TYR A CD2 
1124 C CE1 . TYR A 153 ? 0.27902 0.28752 0.22221 0.04152  -0.03322 -0.06527 160 TYR A CE1 
1125 C CE2 . TYR A 153 ? 0.33644 0.35434 0.27982 0.03916  -0.03232 -0.05122 160 TYR A CE2 
1126 C CZ  . TYR A 153 ? 0.42894 0.44749 0.36513 0.04399  -0.03281 -0.05936 160 TYR A CZ  
1127 O OH  . TYR A 153 ? 0.47468 0.50425 0.39610 0.05239  -0.03237 -0.06120 160 TYR A OH  
1128 N N   . ALA A 154 ? 0.18959 0.15623 0.18872 0.01488  -0.03524 -0.05847 161 ALA A N   
1129 C CA  . ALA A 154 ? 0.19229 0.15042 0.20021 0.01222  -0.03202 -0.05397 161 ALA A CA  
1130 C C   . ALA A 154 ? 0.22683 0.18639 0.22897 0.01622  -0.02681 -0.05076 161 ALA A C   
1131 O O   . ALA A 154 ? 0.20076 0.16039 0.19697 0.02137  -0.02683 -0.05604 161 ALA A O   
1132 C CB  . ALA A 154 ? 0.23810 0.18498 0.25528 0.01079  -0.03539 -0.06022 161 ALA A CB  
1133 N N   . TRP A 155 ? 0.18900 0.15070 0.19342 0.01412  -0.02260 -0.04286 162 TRP A N   
1134 C CA  . TRP A 155 ? 0.20203 0.16663 0.20426 0.01678  -0.01833 -0.03955 162 TRP A CA  
1135 C C   . TRP A 155 ? 0.19863 0.15591 0.20789 0.01684  -0.01752 -0.03669 162 TRP A C   
1136 O O   . TRP A 155 ? 0.21509 0.16731 0.23129 0.01310  -0.01817 -0.03375 162 TRP A O   
1137 C CB  . TRP A 155 ? 0.17427 0.14680 0.17483 0.01419  -0.01484 -0.03385 162 TRP A CB  
1138 C CG  . TRP A 155 ? 0.17085 0.14942 0.17106 0.01526  -0.01107 -0.03092 162 TRP A CG  
1139 C CD1 . TRP A 155 ? 0.16735 0.15452 0.16398 0.01655  -0.00819 -0.03088 162 TRP A CD1 
1140 C CD2 . TRP A 155 ? 0.17678 0.15551 0.18106 0.01479  -0.00979 -0.02736 162 TRP A CD2 
1141 N NE1 . TRP A 155 ? 0.18577 0.17871 0.18538 0.01629  -0.00598 -0.02874 162 TRP A NE1 
1142 C CE2 . TRP A 155 ? 0.17382 0.16218 0.17696 0.01578  -0.00724 -0.02676 162 TRP A CE2 
1143 C CE3 . TRP A 155 ? 0.16321 0.13609 0.17214 0.01402  -0.01033 -0.02423 162 TRP A CE3 
1144 C CZ2 . TRP A 155 ? 0.17568 0.16905 0.18121 0.01640  -0.00637 -0.02437 162 TRP A CZ2 
1145 C CZ3 . TRP A 155 ? 0.16151 0.13880 0.17134 0.01550  -0.00854 -0.02052 162 TRP A CZ3 
1146 C CH2 . TRP A 155 ? 0.16857 0.15652 0.17623 0.01683  -0.00715 -0.02121 162 TRP A CH2 
1147 N N   . GLU A 156 ? 0.16481 0.12226 0.17278 0.02173  -0.01567 -0.03669 163 GLU A N   
1148 C CA  . GLU A 156 ? 0.16996 0.12121 0.18381 0.02316  -0.01431 -0.03212 163 GLU A CA  
1149 C C   . GLU A 156 ? 0.15979 0.11843 0.17098 0.02851  -0.01161 -0.02938 163 GLU A C   
1150 O O   . GLU A 156 ? 0.18364 0.14741 0.19059 0.03268  -0.01119 -0.03332 163 GLU A O   
1151 C CB  . GLU A 156 ? 0.22229 0.15991 0.24156 0.02473  -0.01631 -0.03621 163 GLU A CB  
1152 C CG  . GLU A 156 ? 0.27865 0.20721 0.30629 0.02492  -0.01429 -0.02955 163 GLU A CG  
1153 C CD  . GLU A 156 ? 0.46760 0.38072 0.50383 0.02379  -0.01634 -0.03428 163 GLU A CD  
1154 O OE1 . GLU A 156 ? 0.39270 0.29898 0.42789 0.02908  -0.01688 -0.04006 163 GLU A OE1 
1155 O OE2 . GLU A 156 ? 0.37161 0.27960 0.41664 0.01763  -0.01725 -0.03267 163 GLU A OE2 
1156 N N   . SER A 157 ? 0.19265 0.15327 0.20646 0.02906  -0.00979 -0.02259 164 SER A N   
1157 C CA  . SER A 157 ? 0.16860 0.13794 0.18083 0.03493  -0.00813 -0.01994 164 SER A CA  
1158 C C   . SER A 157 ? 0.16464 0.13134 0.17996 0.03796  -0.00664 -0.01214 164 SER A C   
1159 O O   . SER A 157 ? 0.17965 0.14525 0.19647 0.03415  -0.00594 -0.00763 164 SER A O   
1160 C CB  . SER A 157 ? 0.16253 0.14752 0.17161 0.03269  -0.00746 -0.02045 164 SER A CB  
1161 O OG  . SER A 157 ? 0.17021 0.16589 0.17935 0.03847  -0.00669 -0.01875 164 SER A OG  
1162 N N   . SER A 158 ? 0.18445 0.15093 0.20040 0.04582  -0.00566 -0.00990 165 SER A N   
1163 C CA  . SER A 158 ? 0.19477 0.16325 0.21178 0.05111  -0.00380 -0.00102 165 SER A CA  
1164 C C   . SER A 158 ? 0.20495 0.19312 0.21801 0.05533  -0.00426 0.00004  165 SER A C   
1165 O O   . SER A 158 ? 0.25970 0.25283 0.27254 0.06321  -0.00334 0.00629  165 SER A O   
1166 C CB  . SER A 158 ? 0.27712 0.23130 0.29870 0.05807  -0.00213 0.00206  165 SER A CB  
1167 O OG  . SER A 158 ? 0.27810 0.21456 0.30580 0.05299  -0.00190 0.00118  165 SER A OG  
1168 N N   . ALA A 159 ? 0.19159 0.19152 0.20246 0.05025  -0.00566 -0.00577 166 ALA A N   
1169 C CA  . ALA A 159 ? 0.19894 0.21895 0.20881 0.05247  -0.00663 -0.00713 166 ALA A CA  
1170 C C   . ALA A 159 ? 0.21697 0.24043 0.22858 0.06087  -0.00620 -0.00790 166 ALA A C   
1171 O O   . ALA A 159 ? 0.26992 0.28267 0.28208 0.06184  -0.00537 -0.01157 166 ALA A O   
1172 C CB  . ALA A 159 ? 0.21556 0.24580 0.22323 0.05421  -0.00726 -0.00202 166 ALA A CB  
1173 N N   . GLY A 160 ? 0.23021 0.26984 0.24262 0.06752  -0.00693 -0.00539 167 GLY A N   
1174 C CA  . GLY A 160 ? 0.24070 0.28486 0.25557 0.07597  -0.00612 -0.00635 167 GLY A CA  
1175 C C   . GLY A 160 ? 0.26633 0.31917 0.28318 0.07280  -0.00552 -0.01361 167 GLY A C   
1176 O O   . GLY A 160 ? 0.25198 0.30719 0.27051 0.08000  -0.00406 -0.01513 167 GLY A O   
1177 N N   . GLY A 161 ? 0.16912 0.22642 0.18599 0.06286  -0.00588 -0.01755 168 GLY A N   
1178 C CA  . GLY A 161 ? 0.19440 0.26298 0.21425 0.05954  -0.00437 -0.02243 168 GLY A CA  
1179 C C   . GLY A 161 ? 0.20802 0.26404 0.22444 0.05658  -0.00229 -0.02606 168 GLY A C   
1180 O O   . GLY A 161 ? 0.17920 0.24471 0.19743 0.05445  0.00001  -0.02874 168 GLY A O   
1181 N N   . SER A 162 ? 0.18786 0.22422 0.19991 0.05647  -0.00295 -0.02609 169 SER A N   
1182 C CA  . SER A 162 ? 0.15072 0.17712 0.15868 0.05503  -0.00202 -0.03061 169 SER A CA  
1183 C C   . SER A 162 ? 0.19041 0.20112 0.19603 0.04893  -0.00394 -0.03055 169 SER A C   
1184 O O   . SER A 162 ? 0.18060 0.18470 0.18794 0.04788  -0.00522 -0.02667 169 SER A O   
1185 C CB  . SER A 162 ? 0.23557 0.25573 0.24178 0.06445  -0.00111 -0.03380 169 SER A CB  
1186 O OG  . SER A 162 ? 0.21220 0.21581 0.21916 0.06803  -0.00258 -0.03234 169 SER A OG  
1187 N N   . PHE A 163 ? 0.15570 0.16240 0.15752 0.04539  -0.00385 -0.03427 170 PHE A N   
1188 C CA  . PHE A 163 ? 0.15586 0.14924 0.15616 0.04052  -0.00615 -0.03523 170 PHE A CA  
1189 C C   . PHE A 163 ? 0.20093 0.18812 0.19619 0.04320  -0.00713 -0.04171 170 PHE A C   
1190 O O   . PHE A 163 ? 0.20686 0.20158 0.19836 0.04787  -0.00514 -0.04465 170 PHE A O   
1191 C CB  . PHE A 163 ? 0.15500 0.15229 0.15555 0.03244  -0.00589 -0.03267 170 PHE A CB  
1192 C CG  . PHE A 163 ? 0.14021 0.14720 0.13825 0.03037  -0.00336 -0.03354 170 PHE A CG  
1193 C CD1 . PHE A 163 ? 0.17453 0.19515 0.17612 0.02934  -0.00051 -0.03178 170 PHE A CD1 
1194 C CD2 . PHE A 163 ? 0.17686 0.18015 0.16985 0.02940  -0.00373 -0.03563 170 PHE A CD2 
1195 C CE1 . PHE A 163 ? 0.16374 0.19244 0.16509 0.02683  0.00299  -0.03120 170 PHE A CE1 
1196 C CE2 . PHE A 163 ? 0.15204 0.16391 0.14256 0.02827  -0.00038 -0.03440 170 PHE A CE2 
1197 C CZ  . PHE A 163 ? 0.19857 0.22231 0.19389 0.02659  0.00354  -0.03166 170 PHE A CZ  
1198 N N   . THR A 164 ? 0.16383 0.13836 0.15935 0.04062  -0.01030 -0.04440 171 THR A N   
1199 C CA  . THR A 164 ? 0.17320 0.14319 0.16346 0.04260  -0.01258 -0.05212 171 THR A CA  
1200 C C   . THR A 164 ? 0.20273 0.17337 0.19091 0.03650  -0.01483 -0.05221 171 THR A C   
1201 O O   . THR A 164 ? 0.18143 0.15080 0.17425 0.03061  -0.01513 -0.04708 171 THR A O   
1202 C CB  . THR A 164 ? 0.21777 0.17245 0.21150 0.04563  -0.01535 -0.05783 171 THR A CB  
1203 O OG1 . THR A 164 ? 0.22582 0.17083 0.22734 0.03944  -0.01737 -0.05458 171 THR A OG1 
1204 C CG2 . THR A 164 ? 0.23381 0.18642 0.22965 0.05341  -0.01274 -0.05721 171 THR A CG2 
1205 N N   . VAL A 165 ? 0.21991 0.19388 0.20039 0.03906  -0.01618 -0.05788 172 VAL A N   
1206 C CA  . VAL A 165 ? 0.21194 0.18757 0.18939 0.03532  -0.01906 -0.05860 172 VAL A CA  
1207 C C   . VAL A 165 ? 0.30946 0.28120 0.28189 0.03904  -0.02395 -0.06907 172 VAL A C   
1208 O O   . VAL A 165 ? 0.23250 0.20681 0.19790 0.04599  -0.02303 -0.07483 172 VAL A O   
1209 C CB  . VAL A 165 ? 0.20796 0.19596 0.17936 0.03507  -0.01515 -0.05307 172 VAL A CB  
1210 C CG1 . VAL A 165 ? 0.26427 0.25402 0.23187 0.03306  -0.01843 -0.05335 172 VAL A CG1 
1211 C CG2 . VAL A 165 ? 0.19183 0.18318 0.16949 0.03055  -0.01089 -0.04479 172 VAL A CG2 
1212 N N   . ARG A 166 ? 0.21329 0.18000 0.18973 0.03463  -0.02929 -0.07228 173 ARG A N   
1213 C CA  . ARG A 166 ? 0.21951 0.18389 0.19217 0.03724  -0.03531 -0.08401 173 ARG A CA  
1214 C C   . ARG A 166 ? 0.26849 0.23775 0.24216 0.03279  -0.04026 -0.08424 173 ARG A C   
1215 O O   . ARG A 166 ? 0.21902 0.18853 0.19989 0.02699  -0.03925 -0.07613 173 ARG A O   
1216 C CB  . ARG A 166 ? 0.27430 0.22337 0.25620 0.03672  -0.03808 -0.09153 173 ARG A CB  
1217 C CG  . ARG A 166 ? 0.32533 0.26511 0.32218 0.02840  -0.04004 -0.08788 173 ARG A CG  
1218 C CD  . ARG A 166 ? 0.38643 0.30968 0.39381 0.02845  -0.03958 -0.09082 173 ARG A CD  
1219 N NE  . ARG A 166 ? 0.40925 0.33109 0.41667 0.03194  -0.03309 -0.08187 173 ARG A NE  
1220 C CZ  . ARG A 166 ? 0.52581 0.43564 0.53875 0.03553  -0.03089 -0.08226 173 ARG A CZ  
1221 N NH1 . ARG A 166 ? 0.43952 0.33492 0.45931 0.03565  -0.03400 -0.09154 173 ARG A NH1 
1222 N NH2 . ARG A 166 ? 0.56820 0.48074 0.58041 0.03934  -0.02555 -0.07333 173 ARG A NH2 
1223 N N   . THR A 167 ? 0.27795 0.25251 0.24382 0.03642  -0.04574 -0.09391 174 THR A N   
1224 C CA  . THR A 167 ? 0.24829 0.22803 0.21718 0.03258  -0.05212 -0.09598 174 THR A CA  
1225 C C   . THR A 167 ? 0.31207 0.28019 0.29836 0.02474  -0.05605 -0.09912 174 THR A C   
1226 O O   . THR A 167 ? 0.36602 0.32201 0.35859 0.02436  -0.05725 -0.10658 174 THR A O   
1227 C CB  . THR A 167 ? 0.37928 0.36836 0.33595 0.03885  -0.05830 -0.10753 174 THR A CB  
1228 O OG1 . THR A 167 ? 0.41885 0.42054 0.35978 0.04608  -0.05335 -0.10135 174 THR A OG1 
1229 C CG2 . THR A 167 ? 0.51168 0.50723 0.47357 0.03493  -0.06638 -0.11138 174 THR A CG2 
1230 N N   . ASP A 168 ? 0.25395 0.22539 0.24905 0.01873  -0.05722 -0.09263 175 ASP A N   
1231 C CA  . ASP A 168 ? 0.31324 0.27545 0.32645 0.01088  -0.05948 -0.09322 175 ASP A CA  
1232 C C   . ASP A 168 ? 0.46226 0.42823 0.48175 0.00817  -0.06900 -0.10535 175 ASP A C   
1233 O O   . ASP A 168 ? 0.41828 0.39838 0.43281 0.00948  -0.07342 -0.10612 175 ASP A O   
1234 C CB  . ASP A 168 ? 0.29213 0.25697 0.31262 0.00615  -0.05518 -0.08008 175 ASP A CB  
1235 C CG  . ASP A 168 ? 0.42418 0.38030 0.46343 -0.00137 -0.05552 -0.07839 175 ASP A CG  
1236 O OD1 . ASP A 168 ? 0.55180 0.49498 0.59779 -0.00245 -0.05407 -0.08085 175 ASP A OD1 
1237 O OD2 . ASP A 168 ? 0.37423 0.33672 0.42206 -0.00573 -0.05670 -0.07392 175 ASP A OD2 
1238 N N   . THR A 169 ? 0.54295 0.49788 0.57381 0.00455  -0.07054 -0.11200 176 THR A N   
1239 C CA  . THR A 169 ? 0.78663 0.74587 0.82645 0.00044  -0.07682 -0.11995 176 THR A CA  
1240 C C   . THR A 169 ? 0.66776 0.62445 0.72858 -0.00903 -0.07711 -0.11499 176 THR A C   
1241 O O   . THR A 169 ? 0.69940 0.66037 0.77043 -0.01354 -0.08215 -0.12111 176 THR A O   
1242 C CB  . THR A 169 ? 0.75712 0.70682 0.79675 0.00214  -0.07722 -0.12949 176 THR A CB  
1243 O OG1 . THR A 169 ? 0.64660 0.57982 0.69081 0.00203  -0.07042 -0.12446 176 THR A OG1 
1244 C CG2 . THR A 169 ? 0.51938 0.47819 0.53918 0.01141  -0.07933 -0.13709 176 THR A CG2 
1245 N N   . GLY A 170 ? 0.66647 0.61725 0.73411 -0.01191 -0.07152 -0.10398 177 GLY A N   
1246 C CA  . GLY A 170 ? 0.65353 0.60285 0.74082 -0.02014 -0.07012 -0.09734 177 GLY A CA  
1247 C C   . GLY A 170 ? 0.44881 0.41473 0.54173 -0.02305 -0.07544 -0.09695 177 GLY A C   
1248 O O   . GLY A 170 ? 0.42677 0.40578 0.50887 -0.01881 -0.08151 -0.10325 177 GLY A O   
1249 N N   . GLU A 171 ? 0.54485 0.51149 0.65463 -0.02949 -0.07273 -0.08871 178 GLU A N   
1250 C CA  . GLU A 171 ? 0.41836 0.40155 0.53679 -0.03233 -0.07698 -0.08688 178 GLU A CA  
1251 C C   . GLU A 171 ? 0.42049 0.41563 0.52103 -0.02491 -0.07691 -0.08211 178 GLU A C   
1252 O O   . GLU A 171 ? 0.28526 0.27526 0.37539 -0.02126 -0.06874 -0.07187 178 GLU A O   
1253 C CB  . GLU A 171 ? 0.43739 0.41822 0.57494 -0.03895 -0.07090 -0.07570 178 GLU A CB  
1254 C CG  . GLU A 171 ? 0.47250 0.46855 0.62643 -0.04395 -0.07450 -0.07499 178 GLU A CG  
1255 C CD  . GLU A 171 ? 0.43130 0.43112 0.59152 -0.04712 -0.08117 -0.08647 178 GLU A CD  
1256 O OE1 . GLU A 171 ? 0.45461 0.44109 0.62146 -0.05072 -0.07897 -0.08967 178 GLU A OE1 
1257 O OE2 . GLU A 171 ? 0.57440 0.59094 0.73265 -0.04554 -0.08876 -0.09226 178 GLU A OE2 
1258 N N   . PRO A 172 ? 0.36978 0.38102 0.46492 -0.02169 -0.08455 -0.08791 179 PRO A N   
1259 C CA  . PRO A 172 ? 0.39010 0.41192 0.46787 -0.01369 -0.08220 -0.08010 179 PRO A CA  
1260 C C   . PRO A 172 ? 0.47752 0.50195 0.56158 -0.01478 -0.07512 -0.06592 179 PRO A C   
1261 O O   . PRO A 172 ? 0.47197 0.50025 0.57457 -0.02067 -0.07562 -0.06361 179 PRO A O   
1262 C CB  . PRO A 172 ? 0.37841 0.41839 0.45376 -0.01065 -0.09277 -0.08912 179 PRO A CB  
1263 C CG  . PRO A 172 ? 0.51765 0.55170 0.59727 -0.01400 -0.09897 -0.10419 179 PRO A CG  
1264 C CD  . PRO A 172 ? 0.47973 0.49912 0.57947 -0.02326 -0.09376 -0.10086 179 PRO A CD  
1265 N N   . MET A 173 ? 0.25557 0.27820 0.32483 -0.00903 -0.06818 -0.05675 180 MET A N   
1266 C CA  . MET A 173 ? 0.25909 0.28178 0.33268 -0.00942 -0.06076 -0.04462 180 MET A CA  
1267 C C   . MET A 173 ? 0.36860 0.40461 0.43823 -0.00406 -0.06126 -0.03869 180 MET A C   
1268 O O   . MET A 173 ? 0.42466 0.46196 0.50068 -0.00437 -0.05602 -0.03011 180 MET A O   
1269 C CB  . MET A 173 ? 0.33102 0.34167 0.39375 -0.00745 -0.05194 -0.03822 180 MET A CB  
1270 C CG  . MET A 173 ? 0.61224 0.60984 0.68003 -0.01166 -0.04900 -0.03970 180 MET A CG  
1271 S SD  . MET A 173 ? 0.54230 0.53170 0.59358 -0.00721 -0.04148 -0.03491 180 MET A SD  
1272 C CE  . MET A 173 ? 0.37710 0.37241 0.42635 -0.00503 -0.03609 -0.02503 180 MET A CE  
1273 N N   . GLY A 174 ? 0.28111 0.32642 0.33900 0.00201  -0.06635 -0.04210 181 GLY A N   
1274 C CA  . GLY A 174 ? 0.27824 0.33534 0.33188 0.00843  -0.06595 -0.03464 181 GLY A CA  
1275 C C   . GLY A 174 ? 0.24215 0.29146 0.28146 0.01369  -0.05709 -0.02546 181 GLY A C   
1276 O O   . GLY A 174 ? 0.21770 0.27136 0.24273 0.02052  -0.05737 -0.02394 181 GLY A O   
1277 N N   . ARG A 175 ? 0.16813 0.20637 0.21158 0.01048  -0.04902 -0.01947 182 ARG A N   
1278 C CA  . ARG A 175 ? 0.15708 0.18623 0.18997 0.01345  -0.04049 -0.01247 182 ARG A CA  
1279 C C   . ARG A 175 ? 0.21246 0.23076 0.25186 0.00839  -0.03407 -0.01002 182 ARG A C   
1280 O O   . ARG A 175 ? 0.21817 0.23865 0.26971 0.00551  -0.03366 -0.00832 182 ARG A O   
1281 C CB  . ARG A 175 ? 0.14390 0.17855 0.17342 0.02003  -0.03744 -0.00370 182 ARG A CB  
1282 C CG  . ARG A 175 ? 0.16036 0.18475 0.17972 0.02267  -0.02869 0.00274  182 ARG A CG  
1283 C CD  . ARG A 175 ? 0.15453 0.17944 0.17571 0.02769  -0.02367 0.01206  182 ARG A CD  
1284 N NE  . ARG A 175 ? 0.17412 0.19824 0.20778 0.02490  -0.02200 0.01310  182 ARG A NE  
1285 C CZ  . ARG A 175 ? 0.17078 0.20582 0.21328 0.02766  -0.02519 0.01539  182 ARG A CZ  
1286 N NH1 . ARG A 175 ? 0.17760 0.22599 0.21803 0.03317  -0.03133 0.01628  182 ARG A NH1 
1287 N NH2 . ARG A 175 ? 0.14463 0.17911 0.19838 0.02535  -0.02231 0.01674  182 ARG A NH2 
1288 N N   . GLY A 176 ? 0.19841 0.24314 0.12142 0.03771  -0.02536 -0.00697 183 GLY A N   
1289 C CA  . GLY A 176 ? 0.18161 0.22326 0.12102 0.03161  -0.02212 -0.00628 183 GLY A CA  
1290 C C   . GLY A 176 ? 0.20872 0.24549 0.15180 0.02689  -0.01756 -0.00944 183 GLY A C   
1291 O O   . GLY A 176 ? 0.22324 0.25721 0.15633 0.02950  -0.01413 -0.01032 183 GLY A O   
1292 N N   . THR A 177 ? 0.16247 0.19867 0.11927 0.02106  -0.01714 -0.01079 184 THR A N   
1293 C CA  . THR A 177 ? 0.18304 0.21534 0.14462 0.01782  -0.01312 -0.01236 184 THR A CA  
1294 C C   . THR A 177 ? 0.22766 0.26067 0.19905 0.01218  -0.01670 -0.01705 184 THR A C   
1295 O O   . THR A 177 ? 0.17876 0.21597 0.15745 0.00962  -0.01951 -0.01668 184 THR A O   
1296 C CB  . THR A 177 ? 0.19221 0.22242 0.16011 0.01664  -0.00680 -0.00570 184 THR A CB  
1297 O OG1 . THR A 177 ? 0.21670 0.24557 0.17577 0.02086  -0.00217 -0.00005 184 THR A OG1 
1298 C CG2 . THR A 177 ? 0.21251 0.24253 0.18737 0.01443  -0.00348 -0.00659 184 THR A CG2 
1299 N N   . LYS A 178 ? 0.15223 0.18042 0.12296 0.01105  -0.01578 -0.02093 185 LYS A N   
1300 C CA  . LYS A 178 ? 0.19907 0.22463 0.17775 0.00577  -0.01782 -0.02386 185 LYS A CA  
1301 C C   . LYS A 178 ? 0.20553 0.22706 0.18878 0.00661  -0.01294 -0.02101 185 LYS A C   
1302 O O   . LYS A 178 ? 0.20497 0.22280 0.18274 0.01120  -0.00939 -0.02181 185 LYS A O   
1303 C CB  . LYS A 178 ? 0.25781 0.27829 0.23008 0.00410  -0.02215 -0.03150 185 LYS A CB  
1304 C CG  . LYS A 178 ? 0.42961 0.44477 0.40877 -0.00233 -0.02418 -0.03413 185 LYS A CG  
1305 C CD  . LYS A 178 ? 0.43888 0.44769 0.41158 -0.00584 -0.02949 -0.04263 185 LYS A CD  
1306 C CE  . LYS A 178 ? 0.59583 0.61642 0.56600 -0.00670 -0.03579 -0.04541 185 LYS A CE  
1307 N NZ  . LYS A 178 ? 0.73938 0.75595 0.69288 -0.00103 -0.03741 -0.05079 185 LYS A NZ  
1308 N N   . VAL A 179 ? 0.16532 0.18904 0.15806 0.00316  -0.01274 -0.01764 186 VAL A N   
1309 C CA  . VAL A 179 ? 0.13772 0.16020 0.13574 0.00417  -0.00979 -0.01462 186 VAL A CA  
1310 C C   . VAL A 179 ? 0.19891 0.21480 0.19889 0.00144  -0.01173 -0.01617 186 VAL A C   
1311 O O   . VAL A 179 ? 0.16432 0.18213 0.16801 -0.00346 -0.01407 -0.01552 186 VAL A O   
1312 C CB  . VAL A 179 ? 0.15657 0.18583 0.16177 0.00227  -0.00897 -0.00973 186 VAL A CB  
1313 C CG1 . VAL A 179 ? 0.14486 0.17630 0.15659 0.00341  -0.00763 -0.00658 186 VAL A CG1 
1314 C CG2 . VAL A 179 ? 0.18876 0.22126 0.19214 0.00374  -0.00641 -0.00736 186 VAL A CG2 
1315 N N   . ILE A 180 ? 0.15914 0.16625 0.15587 0.00504  -0.01008 -0.01798 187 ILE A N   
1316 C CA  . ILE A 180 ? 0.15928 0.15549 0.15642 0.00289  -0.01122 -0.01871 187 ILE A CA  
1317 C C   . ILE A 180 ? 0.15322 0.15028 0.15570 0.00680  -0.00900 -0.01271 187 ILE A C   
1318 O O   . ILE A 180 ? 0.18777 0.18578 0.19038 0.01400  -0.00581 -0.01170 187 ILE A O   
1319 C CB  . ILE A 180 ? 0.19165 0.17337 0.17978 0.00494  -0.01135 -0.02553 187 ILE A CB  
1320 C CG1 . ILE A 180 ? 0.21101 0.19540 0.19322 0.00148  -0.01504 -0.03171 187 ILE A CG1 
1321 C CG2 . ILE A 180 ? 0.22044 0.18678 0.20907 0.00138  -0.01232 -0.02562 187 ILE A CG2 
1322 C CD1 . ILE A 180 ? 0.26372 0.23560 0.23341 0.00490  -0.01549 -0.03998 187 ILE A CD1 
1323 N N   . LEU A 181 ? 0.15158 0.15043 0.15842 0.00275  -0.01059 -0.00833 188 LEU A N   
1324 C CA  . LEU A 181 ? 0.15189 0.15313 0.16271 0.00656  -0.01003 -0.00209 188 LEU A CA  
1325 C C   . LEU A 181 ? 0.21101 0.19608 0.21856 0.00807  -0.00944 -0.00040 188 LEU A C   
1326 O O   . LEU A 181 ? 0.20106 0.17955 0.20727 0.00161  -0.01044 0.00058  188 LEU A O   
1327 C CB  . LEU A 181 ? 0.13864 0.15055 0.15277 0.00214  -0.01220 0.00174  188 LEU A CB  
1328 C CG  . LEU A 181 ? 0.18260 0.20582 0.19878 -0.00035 -0.01291 -0.00027 188 LEU A CG  
1329 C CD1 . LEU A 181 ? 0.24130 0.27123 0.25793 -0.00403 -0.01501 0.00196  188 LEU A CD1 
1330 C CD2 . LEU A 181 ? 0.18114 0.21179 0.20161 0.00393  -0.01146 0.00064  188 LEU A CD2 
1331 N N   . HIS A 182 ? 0.17853 0.15701 0.18523 0.01685  -0.00720 0.00062  189 HIS A N   
1332 C CA  . HIS A 182 ? 0.22845 0.18854 0.23142 0.02019  -0.00628 0.00358  189 HIS A CA  
1333 C C   . HIS A 182 ? 0.19513 0.16342 0.20223 0.02324  -0.00756 0.01302  189 HIS A C   
1334 O O   . HIS A 182 ? 0.21091 0.19065 0.22314 0.03151  -0.00742 0.01658  189 HIS A O   
1335 C CB  . HIS A 182 ? 0.21097 0.15877 0.20965 0.03034  -0.00291 -0.00014 189 HIS A CB  
1336 C CG  . HIS A 182 ? 0.28869 0.23190 0.28096 0.02855  -0.00214 -0.00997 189 HIS A CG  
1337 N ND1 . HIS A 182 ? 0.36434 0.28581 0.34757 0.02495  -0.00288 -0.01712 189 HIS A ND1 
1338 C CD2 . HIS A 182 ? 0.26575 0.22310 0.25826 0.02952  -0.00112 -0.01360 189 HIS A CD2 
1339 C CE1 . HIS A 182 ? 0.32348 0.24741 0.30078 0.02440  -0.00312 -0.02533 189 HIS A CE1 
1340 N NE2 . HIS A 182 ? 0.31969 0.26492 0.30201 0.02772  -0.00152 -0.02262 189 HIS A NE2 
1341 N N   . LEU A 183 ? 0.21002 0.17513 0.21515 0.01643  -0.00893 0.01730  190 LEU A N   
1342 C CA  . LEU A 183 ? 0.20798 0.18528 0.21458 0.01776  -0.01113 0.02524  190 LEU A CA  
1343 C C   . LEU A 183 ? 0.30753 0.27708 0.31254 0.02786  -0.01092 0.03322  190 LEU A C   
1344 O O   . LEU A 183 ? 0.26362 0.21129 0.26399 0.03107  -0.00830 0.03435  190 LEU A O   
1345 C CB  . LEU A 183 ? 0.19942 0.17623 0.20246 0.00840  -0.01132 0.02780  190 LEU A CB  
1346 C CG  . LEU A 183 ? 0.18557 0.17400 0.19088 0.00017  -0.01187 0.02151  190 LEU A CG  
1347 C CD1 . LEU A 183 ? 0.22766 0.21751 0.23007 -0.00706 -0.01066 0.02524  190 LEU A CD1 
1348 C CD2 . LEU A 183 ? 0.21215 0.21832 0.22100 0.00239  -0.01438 0.01943  190 LEU A CD2 
1349 N N   . LYS A 184 ? 0.21081 0.19795 0.21937 0.03291  -0.01425 0.03872  191 LYS A N   
1350 C CA  . LYS A 184 ? 0.24842 0.23242 0.25519 0.04309  -0.01543 0.04831  191 LYS A CA  
1351 C C   . LYS A 184 ? 0.27049 0.23709 0.26708 0.03955  -0.01417 0.05555  191 LYS A C   
1352 O O   . LYS A 184 ? 0.29707 0.26442 0.28996 0.02901  -0.01363 0.05444  191 LYS A O   
1353 C CB  . LYS A 184 ? 0.23452 0.24474 0.24702 0.04679  -0.02114 0.05224  191 LYS A CB  
1354 C CG  . LYS A 184 ? 0.27904 0.30890 0.30436 0.05006  -0.02197 0.04737  191 LYS A CG  
1355 C CD  . LYS A 184 ? 0.35711 0.41345 0.38843 0.04679  -0.02882 0.04840  191 LYS A CD  
1356 C CE  . LYS A 184 ? 0.46223 0.53928 0.50869 0.04819  -0.02919 0.04494  191 LYS A CE  
1357 N NZ  . LYS A 184 ? 0.41029 0.51339 0.46499 0.04393  -0.03681 0.04550  191 LYS A NZ  
1358 N N   . GLU A 185 ? 0.33498 0.28620 0.32730 0.04925  -0.01306 0.06390  192 GLU A N   
1359 C CA  . GLU A 185 ? 0.41044 0.34036 0.39260 0.04631  -0.01047 0.07252  192 GLU A CA  
1360 C C   . GLU A 185 ? 0.36658 0.31047 0.34284 0.04070  -0.01267 0.07902  192 GLU A C   
1361 O O   . GLU A 185 ? 0.41668 0.34895 0.38628 0.03220  -0.00904 0.08306  192 GLU A O   
1362 C CB  . GLU A 185 ? 0.41040 0.32281 0.38843 0.06053  -0.00950 0.08200  192 GLU A CB  
1363 C CG  . GLU A 185 ? 0.70445 0.58153 0.67352 0.05727  -0.00432 0.08686  192 GLU A CG  
1364 C CD  . GLU A 185 ? 0.98930 0.84772 0.95244 0.07304  -0.00346 0.09829  192 GLU A CD  
1365 O OE1 . GLU A 185 ? 1.00751 0.88511 0.97448 0.08680  -0.00751 0.10298  192 GLU A OE1 
1366 O OE2 . GLU A 185 ? 0.99407 0.81879 0.94929 0.07156  0.00107  0.10292  192 GLU A OE2 
1367 N N   . ASP A 186 ? 0.33173 0.30070 0.30995 0.04522  -0.01842 0.08015  193 ASP A N   
1368 C CA  . ASP A 186 ? 0.36582 0.34760 0.33524 0.04163  -0.02108 0.08534  193 ASP A CA  
1369 C C   . ASP A 186 ? 0.27898 0.27651 0.25058 0.03082  -0.02188 0.07536  193 ASP A C   
1370 O O   . ASP A 186 ? 0.28456 0.29510 0.24841 0.02885  -0.02466 0.07700  193 ASP A O   
1371 C CB  . ASP A 186 ? 0.42300 0.42171 0.39060 0.05286  -0.02829 0.09255  193 ASP A CB  
1372 C CG  . ASP A 186 ? 0.43225 0.45420 0.41350 0.05571  -0.03400 0.08467  193 ASP A CG  
1373 O OD1 . ASP A 186 ? 0.48468 0.50635 0.47584 0.05122  -0.03131 0.07495  193 ASP A OD1 
1374 O OD2 . ASP A 186 ? 0.50933 0.55075 0.49157 0.06240  -0.04138 0.08886  193 ASP A OD2 
1375 N N   . GLN A 187 ? 0.22487 0.22013 0.20502 0.02464  -0.01940 0.06514  194 GLN A N   
1376 C CA  . GLN A 187 ? 0.22618 0.23430 0.20875 0.01614  -0.01990 0.05606  194 GLN A CA  
1377 C C   . GLN A 187 ? 0.23383 0.23124 0.21647 0.00680  -0.01420 0.05272  194 GLN A C   
1378 O O   . GLN A 187 ? 0.26050 0.26475 0.24798 0.00126  -0.01385 0.04418  194 GLN A O   
1379 C CB  . GLN A 187 ? 0.24017 0.25983 0.23348 0.01745  -0.02285 0.04755  194 GLN A CB  
1380 C CG  . GLN A 187 ? 0.22270 0.25849 0.21993 0.02496  -0.02906 0.05043  194 GLN A CG  
1381 C CD  . GLN A 187 ? 0.29210 0.34142 0.28117 0.02348  -0.03445 0.05256  194 GLN A CD  
1382 O OE1 . GLN A 187 ? 0.29119 0.34321 0.27489 0.01627  -0.03394 0.04741  194 GLN A OE1 
1383 N NE2 . GLN A 187 ? 0.26963 0.32789 0.25688 0.03129  -0.03993 0.05980  194 GLN A NE2 
1384 N N   . THR A 188 ? 0.29678 0.27787 0.27482 0.00470  -0.00987 0.05990  195 THR A N   
1385 C CA  . THR A 188 ? 0.28049 0.25400 0.26168 -0.00563 -0.00509 0.05675  195 THR A CA  
1386 C C   . THR A 188 ? 0.22326 0.21061 0.20177 -0.01214 -0.00260 0.05688  195 THR A C   
1387 O O   . THR A 188 ? 0.29571 0.28227 0.27941 -0.02073 0.00121  0.05445  195 THR A O   
1388 C CB  . THR A 188 ? 0.32202 0.27176 0.30078 -0.00795 -0.00095 0.06413  195 THR A CB  
1389 O OG1 . THR A 188 ? 0.37201 0.31873 0.34072 -0.00538 0.00114  0.07697  195 THR A OG1 
1390 C CG2 . THR A 188 ? 0.36878 0.30184 0.34947 -0.00046 -0.00252 0.06192  195 THR A CG2 
1391 N N   . GLU A 189 ? 0.24369 0.24470 0.21440 -0.00807 -0.00479 0.05898  196 GLU A N   
1392 C CA  . GLU A 189 ? 0.27354 0.28771 0.24068 -0.01249 -0.00191 0.05680  196 GLU A CA  
1393 C C   . GLU A 189 ? 0.22863 0.25084 0.20525 -0.01633 -0.00240 0.04542  196 GLU A C   
1394 O O   . GLU A 189 ? 0.21271 0.24313 0.19041 -0.02058 0.00165  0.04343  196 GLU A O   
1395 C CB  . GLU A 189 ? 0.24542 0.27111 0.20017 -0.00674 -0.00548 0.05843  196 GLU A CB  
1396 C CG  . GLU A 189 ? 0.23625 0.27121 0.19398 -0.00317 -0.01290 0.04951  196 GLU A CG  
1397 C CD  . GLU A 189 ? 0.41098 0.45571 0.35602 0.00175  -0.01827 0.05137  196 GLU A CD  
1398 O OE1 . GLU A 189 ? 0.37467 0.41797 0.31612 0.00751  -0.02208 0.05896  196 GLU A OE1 
1399 O OE2 . GLU A 189 ? 0.31570 0.36908 0.25354 0.00048  -0.01899 0.04512  196 GLU A OE2 
1400 N N   . TYR A 190 ? 0.25138 0.27246 0.23464 -0.01394 -0.00679 0.03870  197 TYR A N   
1401 C CA  . TYR A 190 ? 0.21763 0.24530 0.20798 -0.01644 -0.00743 0.02922  197 TYR A CA  
1402 C C   . TYR A 190 ? 0.23674 0.25900 0.23544 -0.02237 -0.00477 0.02682  197 TYR A C   
1403 O O   . TYR A 190 ? 0.24354 0.27074 0.24786 -0.02348 -0.00594 0.01963  197 TYR A O   
1404 C CB  . TYR A 190 ? 0.18911 0.21894 0.18254 -0.01204 -0.01244 0.02403  197 TYR A CB  
1405 C CG  . TYR A 190 ? 0.17772 0.21555 0.16453 -0.00828 -0.01636 0.02533  197 TYR A CG  
1406 C CD1 . TYR A 190 ? 0.24657 0.29236 0.22707 -0.00940 -0.01663 0.02163  197 TYR A CD1 
1407 C CD2 . TYR A 190 ? 0.19266 0.23040 0.17884 -0.00315 -0.02012 0.03009  197 TYR A CD2 
1408 C CE1 . TYR A 190 ? 0.20453 0.25680 0.17710 -0.00695 -0.02137 0.02136  197 TYR A CE1 
1409 C CE2 . TYR A 190 ? 0.22849 0.27626 0.20885 -0.00052 -0.02535 0.03091  197 TYR A CE2 
1410 C CZ  . TYR A 190 ? 0.25774 0.31203 0.23071 -0.00322 -0.02629 0.02592  197 TYR A CZ  
1411 O OH  . TYR A 190 ? 0.25117 0.31428 0.21654 -0.00159 -0.03248 0.02513  197 TYR A OH  
1412 N N   . LEU A 191 ? 0.21138 0.22315 0.21052 -0.02653 -0.00167 0.03287  198 LEU A N   
1413 C CA  . LEU A 191 ? 0.23949 0.24804 0.24689 -0.03482 0.00045  0.03070  198 LEU A CA  
1414 C C   . LEU A 191 ? 0.23372 0.25274 0.24359 -0.04130 0.00589  0.03536  198 LEU A C   
1415 O O   . LEU A 191 ? 0.22904 0.25043 0.24857 -0.04958 0.00744  0.03379  198 LEU A O   
1416 C CB  . LEU A 191 ? 0.22355 0.21091 0.23086 -0.03699 0.00054  0.03359  198 LEU A CB  
1417 C CG  . LEU A 191 ? 0.22579 0.20259 0.23109 -0.02954 -0.00332 0.02913  198 LEU A CG  
1418 C CD1 . LEU A 191 ? 0.31269 0.26516 0.31575 -0.03034 -0.00226 0.03201  198 LEU A CD1 
1419 C CD2 . LEU A 191 ? 0.29061 0.27476 0.30084 -0.02968 -0.00638 0.01861  198 LEU A CD2 
1420 N N   . GLU A 192 ? 0.22980 0.25605 0.23112 -0.03790 0.00891  0.04122  199 GLU A N   
1421 C CA  . GLU A 192 ? 0.20758 0.24488 0.20988 -0.04284 0.01589  0.04686  199 GLU A CA  
1422 C C   . GLU A 192 ? 0.26773 0.32426 0.27433 -0.04097 0.01676  0.03970  199 GLU A C   
1423 O O   . GLU A 192 ? 0.22592 0.28620 0.22614 -0.03363 0.01336  0.03390  199 GLU A O   
1424 C CB  . GLU A 192 ? 0.31729 0.35296 0.30527 -0.03894 0.01945  0.05685  199 GLU A CB  
1425 C CG  . GLU A 192 ? 0.38909 0.40453 0.37178 -0.03867 0.01872  0.06555  199 GLU A CG  
1426 C CD  . GLU A 192 ? 0.78726 0.80207 0.75375 -0.03310 0.02111  0.07624  199 GLU A CD  
1427 O OE1 . GLU A 192 ? 0.96952 0.99915 0.92872 -0.03177 0.02517  0.07759  199 GLU A OE1 
1428 O OE2 . GLU A 192 ? 0.86814 0.86773 0.82804 -0.02886 0.01884  0.08321  199 GLU A OE2 
1429 N N   . GLU A 193 ? 0.22305 0.29152 0.24135 -0.04775 0.02129  0.04036  200 GLU A N   
1430 C CA  . GLU A 193 ? 0.19738 0.28462 0.22226 -0.04490 0.02223  0.03391  200 GLU A CA  
1431 C C   . GLU A 193 ? 0.19310 0.28797 0.20474 -0.03585 0.02536  0.03334  200 GLU A C   
1432 O O   . GLU A 193 ? 0.22176 0.32042 0.23110 -0.02903 0.02246  0.02544  200 GLU A O   
1433 C CB  . GLU A 193 ? 0.26623 0.36892 0.30720 -0.05382 0.02751  0.03712  200 GLU A CB  
1434 C CG  . GLU A 193 ? 0.35941 0.48508 0.40712 -0.04893 0.03069  0.03317  200 GLU A CG  
1435 C CD  . GLU A 193 ? 0.67761 0.82313 0.74634 -0.05787 0.03374  0.03498  200 GLU A CD  
1436 O OE1 . GLU A 193 ? 0.46677 0.61162 0.54215 -0.06878 0.03810  0.04282  200 GLU A OE1 
1437 O OE2 . GLU A 193 ? 0.50796 0.67022 0.58708 -0.05409 0.03170  0.02913  200 GLU A OE2 
1438 N N   . ARG A 194 ? 0.22937 0.32470 0.23034 -0.03546 0.03117  0.04149  201 ARG A N   
1439 C CA  . ARG A 194 ? 0.25381 0.35728 0.24057 -0.02691 0.03437  0.03943  201 ARG A CA  
1440 C C   . ARG A 194 ? 0.22881 0.32116 0.20229 -0.02007 0.02634  0.03305  201 ARG A C   
1441 O O   . ARG A 194 ? 0.22638 0.32265 0.19114 -0.01336 0.02591  0.02606  201 ARG A O   
1442 C CB  . ARG A 194 ? 0.26596 0.37386 0.24197 -0.02757 0.04291  0.05001  201 ARG A CB  
1443 C CG  . ARG A 194 ? 0.30500 0.39734 0.27385 -0.03097 0.04128  0.05953  201 ARG A CG  
1444 C CD  . ARG A 194 ? 0.43298 0.53087 0.38851 -0.03040 0.05066  0.07094  201 ARG A CD  
1445 N NE  . ARG A 194 ? 0.52774 0.61020 0.46890 -0.02892 0.04794  0.07999  201 ARG A NE  
1446 C CZ  . ARG A 194 ? 0.50786 0.59123 0.43398 -0.02768 0.05493  0.09189  201 ARG A CZ  
1447 N NH1 . ARG A 194 ? 0.51645 0.61582 0.44041 -0.02851 0.06611  0.09625  201 ARG A NH1 
1448 N NH2 . ARG A 194 ? 0.53816 0.60708 0.45095 -0.02467 0.05107  0.10035  201 ARG A NH2 
1449 N N   . ARG A 195 ? 0.18517 0.26374 0.15767 -0.02176 0.02013  0.03522  202 ARG A N   
1450 C CA  . ARG A 195 ? 0.20908 0.28042 0.17302 -0.01661 0.01214  0.02981  202 ARG A CA  
1451 C C   . ARG A 195 ? 0.18278 0.25382 0.15538 -0.01550 0.00772  0.01985  202 ARG A C   
1452 O O   . ARG A 195 ? 0.18922 0.25960 0.15479 -0.01128 0.00410  0.01312  202 ARG A O   
1453 C CB  . ARG A 195 ? 0.20713 0.26679 0.17025 -0.01748 0.00775  0.03595  202 ARG A CB  
1454 C CG  . ARG A 195 ? 0.18310 0.23929 0.14101 -0.01282 -0.00068 0.03174  202 ARG A CG  
1455 C CD  . ARG A 195 ? 0.23767 0.29900 0.17812 -0.00835 -0.00223 0.03244  202 ARG A CD  
1456 N NE  . ARG A 195 ? 0.22939 0.28975 0.16672 -0.00536 -0.01120 0.03012  202 ARG A NE  
1457 C CZ  . ARG A 195 ? 0.24385 0.30798 0.17596 -0.00406 -0.01676 0.02148  202 ARG A CZ  
1458 N NH1 . ARG A 195 ? 0.24262 0.30878 0.16917 -0.00385 -0.01410 0.01379  202 ARG A NH1 
1459 N NH2 . ARG A 195 ? 0.24110 0.30686 0.17450 -0.00296 -0.02516 0.02042  202 ARG A NH2 
1460 N N   . ILE A 196 ? 0.16170 0.23226 0.14856 -0.01960 0.00772  0.01886  203 ILE A N   
1461 C CA  . ILE A 196 ? 0.17297 0.24328 0.16631 -0.01777 0.00392  0.01084  203 ILE A CA  
1462 C C   . ILE A 196 ? 0.17697 0.25641 0.16858 -0.01325 0.00706  0.00585  203 ILE A C   
1463 O O   . ILE A 196 ? 0.18689 0.26215 0.17436 -0.00901 0.00392  -0.00045 203 ILE A O   
1464 C CB  . ILE A 196 ? 0.19245 0.26113 0.19883 -0.02248 0.00262  0.01044  203 ILE A CB  
1465 C CG1 . ILE A 196 ? 0.17721 0.23319 0.18354 -0.02491 -0.00036 0.01375  203 ILE A CG1 
1466 C CG2 . ILE A 196 ? 0.17112 0.24110 0.18189 -0.01930 -0.00072 0.00320  203 ILE A CG2 
1467 C CD1 . ILE A 196 ? 0.20626 0.25845 0.22257 -0.03111 -0.00050 0.01380  203 ILE A CD1 
1468 N N   . LYS A 197 ? 0.17980 0.27144 0.17465 -0.01375 0.01386  0.00891  204 LYS A N   
1469 C CA  . LYS A 197 ? 0.15441 0.25518 0.14710 -0.00700 0.01778  0.00413  204 LYS A CA  
1470 C C   . LYS A 197 ? 0.23068 0.32428 0.20526 -0.00089 0.01705  -0.00040 204 LYS A C   
1471 O O   . LYS A 197 ? 0.20467 0.29514 0.17509 0.00525  0.01638  -0.00762 204 LYS A O   
1472 C CB  . LYS A 197 ? 0.19178 0.31052 0.19104 -0.00745 0.02664  0.00882  204 LYS A CB  
1473 C CG  . LYS A 197 ? 0.35185 0.48334 0.37098 -0.01383 0.02801  0.01209  204 LYS A CG  
1474 C CD  . LYS A 197 ? 0.35815 0.50630 0.38182 -0.01708 0.03771  0.01972  204 LYS A CD  
1475 C CE  . LYS A 197 ? 0.53757 0.69863 0.58256 -0.02705 0.03859  0.02394  204 LYS A CE  
1476 N NZ  . LYS A 197 ? 0.61414 0.79415 0.66648 -0.03147 0.04918  0.03238  204 LYS A NZ  
1477 N N   . GLU A 198 ? 0.17360 0.26413 0.13626 -0.00222 0.01716  0.00376  205 GLU A N   
1478 C CA  . GLU A 198 ? 0.19449 0.27879 0.13840 0.00258  0.01473  -0.00141 205 GLU A CA  
1479 C C   . GLU A 198 ? 0.22456 0.29680 0.16804 0.00255  0.00622  -0.00889 205 GLU A C   
1480 O O   . GLU A 198 ? 0.20619 0.27225 0.13947 0.00671  0.00471  -0.01710 205 GLU A O   
1481 C CB  . GLU A 198 ? 0.19814 0.28194 0.12996 0.00088  0.01422  0.00565  205 GLU A CB  
1482 C CG  . GLU A 198 ? 0.25631 0.33461 0.16790 0.00466  0.00896  0.00005  205 GLU A CG  
1483 C CD  . GLU A 198 ? 0.30904 0.38804 0.20938 0.00375  0.00677  0.00840  205 GLU A CD  
1484 O OE1 . GLU A 198 ? 0.28563 0.36186 0.19584 -0.00016 0.00377  0.01555  205 GLU A OE1 
1485 O OE2 . GLU A 198 ? 0.27936 0.36101 0.15975 0.00793  0.00809  0.00791  205 GLU A OE2 
1486 N N   . ILE A 199 ? 0.16949 0.23742 0.12345 -0.00227 0.00109  -0.00615 206 ILE A N   
1487 C CA  . ILE A 199 ? 0.19002 0.24884 0.14517 -0.00333 -0.00603 -0.01146 206 ILE A CA  
1488 C C   . ILE A 199 ? 0.23599 0.29084 0.19649 -0.00080 -0.00507 -0.01725 206 ILE A C   
1489 O O   . ILE A 199 ? 0.20687 0.25259 0.16184 0.00018  -0.00833 -0.02362 206 ILE A O   
1490 C CB  . ILE A 199 ? 0.17880 0.23591 0.14369 -0.00755 -0.01014 -0.00638 206 ILE A CB  
1491 C CG1 . ILE A 199 ? 0.17345 0.23265 0.13132 -0.00811 -0.01184 -0.00011 206 ILE A CG1 
1492 C CG2 . ILE A 199 ? 0.22473 0.27573 0.19422 -0.00898 -0.01566 -0.01075 206 ILE A CG2 
1493 C CD1 . ILE A 199 ? 0.20608 0.26312 0.17359 -0.01022 -0.01324 0.00640  206 ILE A CD1 
1494 N N   . VAL A 200 ? 0.18800 0.24929 0.15930 0.00004  -0.00105 -0.01487 207 VAL A N   
1495 C CA  . VAL A 200 ? 0.17092 0.22977 0.14668 0.00425  -0.00032 -0.01905 207 VAL A CA  
1496 C C   . VAL A 200 ? 0.22296 0.27883 0.18760 0.01137  0.00306  -0.02492 207 VAL A C   
1497 O O   . VAL A 200 ? 0.22526 0.26935 0.18592 0.01472  0.00138  -0.03029 207 VAL A O   
1498 C CB  . VAL A 200 ? 0.18721 0.25744 0.17674 0.00391  0.00224  -0.01528 207 VAL A CB  
1499 C CG1 . VAL A 200 ? 0.17920 0.25050 0.17217 0.01095  0.00345  -0.01862 207 VAL A CG1 
1500 C CG2 . VAL A 200 ? 0.16067 0.22837 0.15836 -0.00229 -0.00192 -0.01198 207 VAL A CG2 
1501 N N   . LYS A 201 ? 0.18565 0.25049 0.14379 0.01406  0.00844  -0.02386 208 LYS A N   
1502 C CA  . LYS A 201 ? 0.20066 0.26239 0.14603 0.02252  0.01272  -0.03035 208 LYS A CA  
1503 C C   . LYS A 201 ? 0.26532 0.31004 0.19424 0.02173  0.00729  -0.03781 208 LYS A C   
1504 O O   . LYS A 201 ? 0.31428 0.34632 0.23423 0.02738  0.00762  -0.04569 208 LYS A O   
1505 C CB  . LYS A 201 ? 0.24690 0.32418 0.18836 0.02562  0.02089  -0.02670 208 LYS A CB  
1506 C CG  . LYS A 201 ? 0.35944 0.43541 0.28621 0.03634  0.02716  -0.03359 208 LYS A CG  
1507 C CD  . LYS A 201 ? 0.41213 0.50531 0.33406 0.03860  0.03619  -0.02846 208 LYS A CD  
1508 C CE  . LYS A 201 ? 0.50272 0.59394 0.40601 0.05019  0.04297  -0.03602 208 LYS A CE  
1509 N NZ  . LYS A 201 ? 0.64488 0.75781 0.54782 0.05309  0.05421  -0.02902 208 LYS A NZ  
1510 N N   . LYS A 202 ? 0.28251 0.32622 0.20803 0.01462  0.00165  -0.03556 209 LYS A N   
1511 C CA  . LYS A 202 ? 0.31060 0.34216 0.22161 0.01244  -0.00489 -0.04277 209 LYS A CA  
1512 C C   . LYS A 202 ? 0.32262 0.33970 0.23935 0.00856  -0.01070 -0.04729 209 LYS A C   
1513 O O   . LYS A 202 ? 0.28852 0.29074 0.19390 0.00901  -0.01353 -0.05623 209 LYS A O   
1514 C CB  . LYS A 202 ? 0.28057 0.31916 0.18810 0.00699  -0.00973 -0.03767 209 LYS A CB  
1515 C CG  . LYS A 202 ? 0.35513 0.38539 0.25214 0.00268  -0.01915 -0.04441 209 LYS A CG  
1516 C CD  . LYS A 202 ? 0.50313 0.54225 0.38751 0.00241  -0.02207 -0.04099 209 LYS A CD  
1517 C CE  . LYS A 202 ? 0.68157 0.72431 0.57221 -0.00410 -0.03193 -0.03809 209 LYS A CE  
1518 N NZ  . LYS A 202 ? 0.65284 0.69888 0.52527 -0.00435 -0.03930 -0.04137 209 LYS A NZ  
1519 N N   . HIS A 203 ? 0.24916 0.26911 0.18241 0.00453  -0.01210 -0.04135 210 HIS A N   
1520 C CA  . HIS A 203 ? 0.29328 0.30238 0.23267 -0.00077 -0.01723 -0.04311 210 HIS A CA  
1521 C C   . HIS A 203 ? 0.31210 0.31511 0.26030 0.00232  -0.01416 -0.04166 210 HIS A C   
1522 O O   . HIS A 203 ? 0.31524 0.30678 0.26621 -0.00150 -0.01699 -0.04289 210 HIS A O   
1523 C CB  . HIS A 203 ? 0.29272 0.31032 0.24244 -0.00783 -0.02198 -0.03702 210 HIS A CB  
1524 C CG  . HIS A 203 ? 0.28342 0.30642 0.22531 -0.01101 -0.02724 -0.03777 210 HIS A CG  
1525 N ND1 . HIS A 203 ? 0.34827 0.36389 0.28043 -0.01463 -0.03330 -0.04539 210 HIS A ND1 
1526 C CD2 . HIS A 203 ? 0.37877 0.41338 0.32014 -0.01087 -0.02787 -0.03168 210 HIS A CD2 
1527 C CE1 . HIS A 203 ? 0.38078 0.40586 0.30689 -0.01619 -0.03818 -0.04401 210 HIS A CE1 
1528 N NE2 . HIS A 203 ? 0.37123 0.40727 0.30239 -0.01329 -0.03455 -0.03506 210 HIS A NE2 
1529 N N   . SER A 204 ? 0.32068 0.22606 0.20258 -0.03166 -0.07178 -0.05380 211 SER A N   
1530 C CA  . SER A 204 ? 0.31454 0.22285 0.21811 -0.02502 -0.05865 -0.05291 211 SER A CA  
1531 C C   . SER A 204 ? 0.34912 0.24691 0.23213 -0.01367 -0.04385 -0.06091 211 SER A C   
1532 O O   . SER A 204 ? 0.33499 0.24248 0.23241 -0.00508 -0.03177 -0.05766 211 SER A O   
1533 C CB  . SER A 204 ? 0.28965 0.22220 0.22176 -0.02226 -0.05351 -0.04136 211 SER A CB  
1534 O OG  . SER A 204 ? 0.34378 0.28700 0.29787 -0.02999 -0.06609 -0.03456 211 SER A OG  
1535 N N   . GLN A 205 ? 0.38645 0.26508 0.23592 -0.01271 -0.04503 -0.07215 212 GLN A N   
1536 C CA  . GLN A 205 ? 0.44371 0.31689 0.27444 0.00051  -0.02928 -0.07995 212 GLN A CA  
1537 C C   . GLN A 205 ? 0.48608 0.34353 0.32614 0.00902  -0.02234 -0.08519 212 GLN A C   
1538 O O   . GLN A 205 ? 0.52392 0.38496 0.36150 0.02295  -0.00835 -0.08803 212 GLN A O   
1539 C CB  . GLN A 205 ? 0.49353 0.34993 0.28199 0.00073  -0.03053 -0.09214 212 GLN A CB  
1540 C CG  . GLN A 205 ? 0.71310 0.53788 0.48176 -0.00703 -0.04431 -0.10520 212 GLN A CG  
1541 C CD  . GLN A 205 ? 0.86569 0.69182 0.63441 -0.02365 -0.06603 -0.10129 212 GLN A CD  
1542 O OE1 . GLN A 205 ? 0.55080 0.39851 0.34928 -0.02979 -0.07275 -0.08740 212 GLN A OE1 
1543 N NE2 . GLN A 205 ? 0.74946 0.56065 0.49413 -0.02937 -0.07484 -0.11159 212 GLN A NE2 
1544 N N   . PHE A 206 ? 0.40514 0.24641 0.25752 0.00107  -0.03168 -0.08519 213 PHE A N   
1545 C CA  . PHE A 206 ? 0.49352 0.31550 0.35304 0.00802  -0.02608 -0.08743 213 PHE A CA  
1546 C C   . PHE A 206 ? 0.40710 0.24452 0.29962 0.00605  -0.02452 -0.07372 213 PHE A C   
1547 O O   . PHE A 206 ? 0.51333 0.33247 0.41312 0.00595  -0.02410 -0.07205 213 PHE A O   
1548 C CB  . PHE A 206 ? 0.49528 0.28017 0.33895 -0.00041 -0.03625 -0.09859 213 PHE A CB  
1549 C CG  . PHE A 206 ? 0.58208 0.34700 0.38728 0.00281  -0.03723 -0.11519 213 PHE A CG  
1550 C CD1 . PHE A 206 ? 0.53214 0.29498 0.32402 0.02032  -0.02188 -0.12215 213 PHE A CD1 
1551 C CD2 . PHE A 206 ? 0.59513 0.35831 0.38842 -0.01168 -0.05121 -0.11952 213 PHE A CD2 
1552 C CE1 . PHE A 206 ? 0.61927 0.37657 0.38536 0.02266  -0.01905 -0.13408 213 PHE A CE1 
1553 C CE2 . PHE A 206 ? 0.73273 0.48895 0.49700 -0.00893 -0.04949 -0.13128 213 PHE A CE2 
1554 C CZ  . PHE A 206 ? 0.61329 0.36571 0.36314 0.00800  -0.03271 -0.13904 213 PHE A CZ  
1555 N N   . ILE A 207 ? 0.29456 0.16291 0.20516 0.00403  -0.02356 -0.06384 214 ILE A N   
1556 C CA  . ILE A 207 ? 0.27214 0.15621 0.20917 0.00479  -0.01957 -0.05288 214 ILE A CA  
1557 C C   . ILE A 207 ? 0.35931 0.24666 0.29599 0.02040  -0.00801 -0.05182 214 ILE A C   
1558 O O   . ILE A 207 ? 0.30751 0.20758 0.23725 0.02951  -0.00144 -0.05475 214 ILE A O   
1559 C CB  . ILE A 207 ? 0.25615 0.16879 0.21051 -0.00068 -0.02213 -0.04524 214 ILE A CB  
1560 C CG1 . ILE A 207 ? 0.26170 0.17287 0.22247 -0.01463 -0.03524 -0.04452 214 ILE A CG1 
1561 C CG2 . ILE A 207 ? 0.22635 0.15632 0.20279 0.00246  -0.01587 -0.03659 214 ILE A CG2 
1562 C CD1 . ILE A 207 ? 0.33728 0.23970 0.31451 -0.02351 -0.03890 -0.04163 214 ILE A CD1 
1563 N N   . GLY A 208 ? 0.28281 0.16056 0.22800 0.02330  -0.00568 -0.04636 215 GLY A N   
1564 C CA  . GLY A 208 ? 0.30147 0.17743 0.24456 0.03938  0.00230  -0.04505 215 GLY A CA  
1565 C C   . GLY A 208 ? 0.31301 0.21972 0.27137 0.04539  0.00691  -0.03690 215 GLY A C   
1566 O O   . GLY A 208 ? 0.29308 0.19928 0.25429 0.05562  0.01012  -0.03158 215 GLY A O   
1567 N N   . TYR A 209 ? 0.25436 0.18612 0.22126 0.03927  0.00614  -0.03598 216 TYR A N   
1568 C CA  . TYR A 209 ? 0.25239 0.21182 0.23286 0.04248  0.00904  -0.03068 216 TYR A CA  
1569 C C   . TYR A 209 ? 0.23726 0.21577 0.21876 0.04093  0.01058  -0.03408 216 TYR A C   
1570 O O   . TYR A 209 ? 0.25614 0.22854 0.22980 0.03360  0.00762  -0.03728 216 TYR A O   
1571 C CB  . TYR A 209 ? 0.18499 0.15199 0.17817 0.03334  0.00656  -0.02411 216 TYR A CB  
1572 C CG  . TYR A 209 ? 0.24790 0.19776 0.23985 0.03273  0.00693  -0.01828 216 TYR A CG  
1573 C CD1 . TYR A 209 ? 0.23814 0.19026 0.22841 0.04200  0.01012  -0.01214 216 TYR A CD1 
1574 C CD2 . TYR A 209 ? 0.25787 0.18910 0.24998 0.02213  0.00338  -0.01786 216 TYR A CD2 
1575 C CE1 . TYR A 209 ? 0.24695 0.18059 0.23315 0.04103  0.01114  -0.00432 216 TYR A CE1 
1576 C CE2 . TYR A 209 ? 0.22956 0.14327 0.22114 0.01942  0.00481  -0.01081 216 TYR A CE2 
1577 C CZ  . TYR A 209 ? 0.23742 0.15128 0.22472 0.02916  0.00939  -0.00338 216 TYR A CZ  
1578 O OH  . TYR A 209 ? 0.29729 0.19183 0.28143 0.02614  0.01138  0.00598  216 TYR A OH  
1579 N N   . PRO A 210 ? 0.22433 0.22611 0.21495 0.04656  0.01440  -0.03267 217 PRO A N   
1580 C CA  . PRO A 210 ? 0.21583 0.23565 0.20934 0.04250  0.01672  -0.03404 217 PRO A CA  
1581 C C   . PRO A 210 ? 0.25581 0.27753 0.25514 0.02991  0.01140  -0.03107 217 PRO A C   
1582 O O   . PRO A 210 ? 0.25478 0.28019 0.26488 0.02685  0.00850  -0.02820 217 PRO A O   
1583 C CB  . PRO A 210 ? 0.23243 0.27769 0.23958 0.04935  0.02013  -0.03256 217 PRO A CB  
1584 C CG  . PRO A 210 ? 0.27051 0.31263 0.28140 0.05474  0.01697  -0.02910 217 PRO A CG  
1585 C CD  . PRO A 210 ? 0.22239 0.23496 0.22065 0.05622  0.01579  -0.02904 217 PRO A CD  
1586 N N   . ILE A 211 ? 0.21111 0.22928 0.20167 0.02377  0.01029  -0.03166 218 ILE A N   
1587 C CA  . ILE A 211 ? 0.15359 0.17253 0.14958 0.01380  0.00438  -0.02764 218 ILE A CA  
1588 C C   . ILE A 211 ? 0.17921 0.21271 0.17761 0.01052  0.00835  -0.02497 218 ILE A C   
1589 O O   . ILE A 211 ? 0.23374 0.26858 0.21865 0.01091  0.01329  -0.02555 218 ILE A O   
1590 C CB  . ILE A 211 ? 0.21602 0.21810 0.19871 0.00832  -0.00273 -0.02807 218 ILE A CB  
1591 C CG1 . ILE A 211 ? 0.20597 0.19295 0.18803 0.00897  -0.00656 -0.03086 218 ILE A CG1 
1592 C CG2 . ILE A 211 ? 0.20005 0.20446 0.19049 0.00052  -0.00989 -0.02231 218 ILE A CG2 
1593 C CD1 . ILE A 211 ? 0.22616 0.19636 0.19328 0.00268  -0.01523 -0.03364 218 ILE A CD1 
1594 N N   . THR A 212 ? 0.16034 0.20392 0.17483 0.00675  0.00706  -0.02243 219 THR A N   
1595 C CA  . THR A 212 ? 0.15085 0.20745 0.17119 0.00139  0.01062  -0.01949 219 THR A CA  
1596 C C   . THR A 212 ? 0.14015 0.18688 0.16259 -0.00720 0.00450  -0.01393 219 THR A C   
1597 O O   . THR A 212 ? 0.15102 0.19260 0.18463 -0.00771 -0.00090 -0.01450 219 THR A O   
1598 C CB  . THR A 212 ? 0.18682 0.26073 0.22383 0.00289  0.01234  -0.02204 219 THR A CB  
1599 O OG1 . THR A 212 ? 0.15461 0.23819 0.19061 0.01295  0.01661  -0.02546 219 THR A OG1 
1600 C CG2 . THR A 212 ? 0.17941 0.26649 0.22590 -0.00619 0.01504  -0.01893 219 THR A CG2 
1601 N N   . LEU A 213 ? 0.16330 0.20703 0.17414 -0.01282 0.00587  -0.00813 220 LEU A N   
1602 C CA  . LEU A 213 ? 0.15076 0.18336 0.16244 -0.02033 -0.00050 -0.00020 220 LEU A CA  
1603 C C   . LEU A 213 ? 0.15020 0.19063 0.17526 -0.02776 0.00330  0.00296  220 LEU A C   
1604 O O   . LEU A 213 ? 0.18262 0.23442 0.20372 -0.03255 0.01142  0.00625  220 LEU A O   
1605 C CB  . LEU A 213 ? 0.17617 0.19952 0.16396 -0.02344 -0.00195 0.00634  220 LEU A CB  
1606 C CG  . LEU A 213 ? 0.23783 0.24837 0.22232 -0.03062 -0.00918 0.01797  220 LEU A CG  
1607 C CD1 . LEU A 213 ? 0.20122 0.20201 0.20413 -0.02809 -0.02016 0.01821  220 LEU A CD1 
1608 C CD2 . LEU A 213 ? 0.23371 0.23538 0.18845 -0.03192 -0.01272 0.02319  220 LEU A CD2 
1609 N N   . PHE A 214 ? 0.17077 0.20568 0.21228 -0.02908 -0.00188 0.00106  221 PHE A N   
1610 C CA  . PHE A 214 ? 0.17841 0.21539 0.23281 -0.03791 -0.00059 0.00250  221 PHE A CA  
1611 C C   . PHE A 214 ? 0.21648 0.23931 0.26339 -0.04716 -0.00187 0.01514  221 PHE A C   
1612 O O   . PHE A 214 ? 0.22106 0.22827 0.25732 -0.04479 -0.00818 0.02171  221 PHE A O   
1613 C CB  . PHE A 214 ? 0.14103 0.16972 0.21044 -0.03583 -0.00632 -0.00465 221 PHE A CB  
1614 C CG  . PHE A 214 ? 0.14870 0.19209 0.22440 -0.02954 -0.00462 -0.01580 221 PHE A CG  
1615 C CD1 . PHE A 214 ? 0.12793 0.18250 0.19611 -0.02143 -0.00138 -0.01818 221 PHE A CD1 
1616 C CD2 . PHE A 214 ? 0.15220 0.19444 0.23881 -0.03135 -0.00719 -0.02389 221 PHE A CD2 
1617 C CE1 . PHE A 214 ? 0.11787 0.18320 0.18936 -0.01520 -0.00072 -0.02567 221 PHE A CE1 
1618 C CE2 . PHE A 214 ? 0.14061 0.19573 0.22838 -0.02542 -0.00667 -0.03309 221 PHE A CE2 
1619 C CZ  . PHE A 214 ? 0.17212 0.23938 0.25243 -0.01724 -0.00347 -0.03263 221 PHE A CZ  
1620 N N   . VAL A 215 ? 0.19575 0.22435 0.24905 -0.05845 0.00324  0.01962  222 VAL A N   
1621 C CA  . VAL A 215 ? 0.21240 0.22472 0.25884 -0.06925 0.00262  0.03393  222 VAL A CA  
1622 C C   . VAL A 215 ? 0.28205 0.27585 0.34578 -0.07584 -0.00371 0.03343  222 VAL A C   
1623 O O   . VAL A 215 ? 0.21190 0.20990 0.29123 -0.07366 -0.00589 0.02080  222 VAL A O   
1624 C CB  . VAL A 215 ? 0.39906 0.42905 0.43885 -0.07952 0.01481  0.04198  222 VAL A CB  
1625 C CG1 . VAL A 215 ? 0.45551 0.49499 0.47122 -0.07165 0.02079  0.04285  222 VAL A CG1 
1626 C CG2 . VAL A 215 ? 0.22618 0.28188 0.28696 -0.08362 0.02094  0.03346  222 VAL A CG2 
1627 N N   . GLU A 216 ? 0.28114 0.25143 0.33967 -0.08342 -0.00723 0.04713  223 GLU A N   
1628 C CA  . GLU A 216 ? 0.33518 0.28082 0.40886 -0.08850 -0.01381 0.04635  223 GLU A CA  
1629 C C   . GLU A 216 ? 0.36818 0.30860 0.44685 -0.10788 -0.00896 0.05635  223 GLU A C   
1630 O O   . GLU A 216 ? 0.39475 0.34186 0.46013 -0.11653 -0.00172 0.07080  223 GLU A O   
1631 C CB  . GLU A 216 ? 0.43527 0.35119 0.50435 -0.07967 -0.02442 0.05405  223 GLU A CB  
1632 C CG  . GLU A 216 ? 0.41933 0.34339 0.48602 -0.06287 -0.02914 0.04662  223 GLU A CG  
1633 C CD  . GLU A 216 ? 0.53742 0.43825 0.60364 -0.05398 -0.04054 0.05573  223 GLU A CD  
1634 O OE1 . GLU A 216 ? 0.44036 0.34525 0.49159 -0.04924 -0.04511 0.06398  223 GLU A OE1 
1635 O OE2 . GLU A 216 ? 0.39986 0.27786 0.48074 -0.05170 -0.04560 0.05439  223 GLU A OE2 
1636 N N   . LYS A 217 ? 0.37949 0.30736 0.47660 -0.11536 -0.01268 0.04805  224 LYS A N   
1637 C CA  . LYS A 217 ? 0.56158 0.47740 0.66809 -0.13623 -0.01063 0.05648  224 LYS A CA  
1638 C C   . LYS A 217 ? 0.73946 0.63280 0.82988 -0.14416 -0.00923 0.08087  224 LYS A C   
1639 O O   . LYS A 217 ? 0.66246 0.52776 0.74185 -0.13387 -0.01742 0.08895  224 LYS A O   
1640 C CB  . LYS A 217 ? 0.54645 0.43346 0.66893 -0.13938 -0.01956 0.04446  224 LYS A CB  
1641 C CG  . LYS A 217 ? 0.80609 0.69307 0.93987 -0.16015 -0.01574 0.04382  224 LYS A CG  
1642 C CD  . LYS A 217 ? 0.72984 0.57930 0.86673 -0.16152 -0.02226 0.03382  224 LYS A CD  
1643 C CE  . LYS A 217 ? 0.85901 0.68497 0.99179 -0.17583 -0.01789 0.05017  224 LYS A CE  
1644 N NZ  . LYS A 217 ? 0.60632 0.38997 0.73946 -0.17672 -0.02378 0.04317  224 LYS A NZ  
# 
