data_9BXK
# 
_entry.id   9BXK 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.402 
_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   9BXK         pdb_00009bxk 10.2210/pdb9bxk/pdb 
WWPDB D_1000280439 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
_pdbx_audit_revision_history.part_number 
1 'Structure model' 1 0 2025-01-08 ? 
2 'Structure model' 1 1 2025-02-05 ? 
3 'Structure model' 1 2 2025-03-19 ? 
# 
_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             ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1 2 'Structure model' 'Database references' 
2 3 'Structure model' 'Database references' 
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 2 'Structure model' citation        
2 2 'Structure model' citation_author 
3 3 'Structure model' citation        
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1 2 'Structure model' '_citation.pdbx_database_id_DOI'    
2 2 'Structure model' '_citation.pdbx_database_id_PubMed' 
3 2 'Structure model' '_citation.title'                   
4 2 'Structure model' '_citation.year'                    
5 2 'Structure model' '_citation_author.identifier_ORCID' 
6 3 'Structure model' '_citation.journal_volume'          
7 3 'Structure model' '_citation.page_first'              
8 3 'Structure model' '_citation.page_last'               
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9BXK 
_pdbx_database_status.recvd_initial_deposition_date   2024-05-22 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           N 
# 
_pdbx_contact_author.id                 3 
_pdbx_contact_author.email              katherine.davis@emory.edu 
_pdbx_contact_author.name_first         Katherine 
_pdbx_contact_author.name_last          Davis 
_pdbx_contact_author.name_mi            M 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-0258-8907 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Ireland, K.A.' 1 0000-0003-0986-5142 
'Davis, K.M.'   2 0000-0002-0258-8907 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   UK 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            Structure 
_citation.journal_id_ASTM           STRUE6 
_citation.journal_id_CSD            2005 
_citation.journal_id_ISSN           0969-2126 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            33 
_citation.language                  ? 
_citation.page_first                528 
_citation.page_last                 538.e5 
_citation.title                     
'Structural and functional analysis of SAM-dependent N-methyltransferases involved in ovoselenol and ovothiol biosynthesis.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1016/j.str.2024.12.020 
_citation.pdbx_database_id_PubMed   39862859 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Ireland, K.A.'        1 ? 
primary 'Kayrouz, C.M.'        2 ? 
primary 'Abbott, M.L.'         3 ? 
primary 'Seyedsayamdost, M.R.' 4 ? 
primary 'Davis, K.M.'          5 ? 
# 
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 '5-selenohistidine N-methyltransferase OvsM' 29997.824 1   ? ? ? ? 
2 non-polymer syn S-ADENOSYL-L-HOMOCYSTEINE                    384.411   1   ? ? ? ? 
3 non-polymer syn 5-selanyl-L-histidine                        234.115   1   ? ? ? ? 
4 non-polymer syn 1,2-ETHANEDIOL                               62.068    1   ? ? ? ? 
5 water       nat water                                        18.015    282 ? ? ? ? 
# 
_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       
;MGSSHHHHHHSSGLVPRGSHMTDNPYETDELLGQYLDFHYGPGHFDVPNYPKACIEQALAHHTGTTGRALDLGCAVGRSS
FELARRFDEVIGIDLSRRFIDSATRLAEQGQLQYQVTLEGELIERRTADLAALELSNTAGRTRFQVGDACALDDTLGRFD
LIFAGNLIDRLPDPAAFLAQLPALVRPGGLLMITSPYTLLPEFTPRERWIGGFERNGQPVRMLDGLRHHLEPDFVLLEPT
RDIPFVIRETTRKYQHTVAEASLWRRA
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MGSSHHHHHHSSGLVPRGSHMTDNPYETDELLGQYLDFHYGPGHFDVPNYPKACIEQALAHHTGTTGRALDLGCAVGRSS
FELARRFDEVIGIDLSRRFIDSATRLAEQGQLQYQVTLEGELIERRTADLAALELSNTAGRTRFQVGDACALDDTLGRFD
LIFAGNLIDRLPDPAAFLAQLPALVRPGGLLMITSPYTLLPEFTPRERWIGGFERNGQPVRMLDGLRHHLEPDFVLLEPT
RDIPFVIRETTRKYQHTVAEASLWRRA
;
_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 S-ADENOSYL-L-HOMOCYSTEINE SAH   
3 5-selanyl-L-histidine     A1AS0 
4 1,2-ETHANEDIOL            EDO   
5 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   GLY n 
1 3   SER n 
1 4   SER n 
1 5   HIS n 
1 6   HIS n 
1 7   HIS n 
1 8   HIS n 
1 9   HIS n 
1 10  HIS n 
1 11  SER n 
1 12  SER n 
1 13  GLY n 
1 14  LEU n 
1 15  VAL n 
1 16  PRO n 
1 17  ARG n 
1 18  GLY n 
1 19  SER n 
1 20  HIS n 
1 21  MET n 
1 22  THR n 
1 23  ASP n 
1 24  ASN n 
1 25  PRO n 
1 26  TYR n 
1 27  GLU n 
1 28  THR n 
1 29  ASP n 
1 30  GLU n 
1 31  LEU n 
1 32  LEU n 
1 33  GLY n 
1 34  GLN n 
1 35  TYR n 
1 36  LEU n 
1 37  ASP n 
1 38  PHE n 
1 39  HIS n 
1 40  TYR n 
1 41  GLY n 
1 42  PRO n 
1 43  GLY n 
1 44  HIS n 
1 45  PHE n 
1 46  ASP n 
1 47  VAL n 
1 48  PRO n 
1 49  ASN n 
1 50  TYR n 
1 51  PRO n 
1 52  LYS n 
1 53  ALA n 
1 54  CYS n 
1 55  ILE n 
1 56  GLU n 
1 57  GLN n 
1 58  ALA n 
1 59  LEU n 
1 60  ALA n 
1 61  HIS n 
1 62  HIS n 
1 63  THR n 
1 64  GLY n 
1 65  THR n 
1 66  THR n 
1 67  GLY n 
1 68  ARG n 
1 69  ALA n 
1 70  LEU n 
1 71  ASP n 
1 72  LEU n 
1 73  GLY n 
1 74  CYS n 
1 75  ALA n 
1 76  VAL n 
1 77  GLY n 
1 78  ARG n 
1 79  SER n 
1 80  SER n 
1 81  PHE n 
1 82  GLU n 
1 83  LEU n 
1 84  ALA n 
1 85  ARG n 
1 86  ARG n 
1 87  PHE n 
1 88  ASP n 
1 89  GLU n 
1 90  VAL n 
1 91  ILE n 
1 92  GLY n 
1 93  ILE n 
1 94  ASP n 
1 95  LEU n 
1 96  SER n 
1 97  ARG n 
1 98  ARG n 
1 99  PHE n 
1 100 ILE n 
1 101 ASP n 
1 102 SER n 
1 103 ALA n 
1 104 THR n 
1 105 ARG n 
1 106 LEU n 
1 107 ALA n 
1 108 GLU n 
1 109 GLN n 
1 110 GLY n 
1 111 GLN n 
1 112 LEU n 
1 113 GLN n 
1 114 TYR n 
1 115 GLN n 
1 116 VAL n 
1 117 THR n 
1 118 LEU n 
1 119 GLU n 
1 120 GLY n 
1 121 GLU n 
1 122 LEU n 
1 123 ILE n 
1 124 GLU n 
1 125 ARG n 
1 126 ARG n 
1 127 THR n 
1 128 ALA n 
1 129 ASP n 
1 130 LEU n 
1 131 ALA n 
1 132 ALA n 
1 133 LEU n 
1 134 GLU n 
1 135 LEU n 
1 136 SER n 
1 137 ASN n 
1 138 THR n 
1 139 ALA n 
1 140 GLY n 
1 141 ARG n 
1 142 THR n 
1 143 ARG n 
1 144 PHE n 
1 145 GLN n 
1 146 VAL n 
1 147 GLY n 
1 148 ASP n 
1 149 ALA n 
1 150 CYS n 
1 151 ALA n 
1 152 LEU n 
1 153 ASP n 
1 154 ASP n 
1 155 THR n 
1 156 LEU n 
1 157 GLY n 
1 158 ARG n 
1 159 PHE n 
1 160 ASP n 
1 161 LEU n 
1 162 ILE n 
1 163 PHE n 
1 164 ALA n 
1 165 GLY n 
1 166 ASN n 
1 167 LEU n 
1 168 ILE n 
1 169 ASP n 
1 170 ARG n 
1 171 LEU n 
1 172 PRO n 
1 173 ASP n 
1 174 PRO n 
1 175 ALA n 
1 176 ALA n 
1 177 PHE n 
1 178 LEU n 
1 179 ALA n 
1 180 GLN n 
1 181 LEU n 
1 182 PRO n 
1 183 ALA n 
1 184 LEU n 
1 185 VAL n 
1 186 ARG n 
1 187 PRO n 
1 188 GLY n 
1 189 GLY n 
1 190 LEU n 
1 191 LEU n 
1 192 MET n 
1 193 ILE n 
1 194 THR n 
1 195 SER n 
1 196 PRO n 
1 197 TYR n 
1 198 THR n 
1 199 LEU n 
1 200 LEU n 
1 201 PRO n 
1 202 GLU n 
1 203 PHE n 
1 204 THR n 
1 205 PRO n 
1 206 ARG n 
1 207 GLU n 
1 208 ARG n 
1 209 TRP n 
1 210 ILE n 
1 211 GLY n 
1 212 GLY n 
1 213 PHE n 
1 214 GLU n 
1 215 ARG n 
1 216 ASN n 
1 217 GLY n 
1 218 GLN n 
1 219 PRO n 
1 220 VAL n 
1 221 ARG n 
1 222 MET n 
1 223 LEU n 
1 224 ASP n 
1 225 GLY n 
1 226 LEU n 
1 227 ARG n 
1 228 HIS n 
1 229 HIS n 
1 230 LEU n 
1 231 GLU n 
1 232 PRO n 
1 233 ASP n 
1 234 PHE n 
1 235 VAL n 
1 236 LEU n 
1 237 LEU n 
1 238 GLU n 
1 239 PRO n 
1 240 THR n 
1 241 ARG n 
1 242 ASP n 
1 243 ILE n 
1 244 PRO n 
1 245 PHE n 
1 246 VAL n 
1 247 ILE n 
1 248 ARG n 
1 249 GLU n 
1 250 THR n 
1 251 THR n 
1 252 ARG n 
1 253 LYS n 
1 254 TYR n 
1 255 GLN n 
1 256 HIS n 
1 257 THR n 
1 258 VAL n 
1 259 ALA n 
1 260 GLU n 
1 261 ALA n 
1 262 SER n 
1 263 LEU n 
1 264 TRP n 
1 265 ARG n 
1 266 ARG n 
1 267 ALA 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                   267 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 EDC38_1804 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    'DSM 16974' 
_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      'Marinimicrobium koreense' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     306545 
_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          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_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 
A1AS0 'L-peptide linking' n 5-selanyl-L-histidine     ?                 'C6 H9 N3 O2 Se'  234.115 
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 
CYS   'L-peptide linking' y CYSTEINE                  ?                 'C3 H7 N O2 S'    121.158 
EDO   non-polymer         . 1,2-ETHANEDIOL            'ETHYLENE GLYCOL' 'C2 H6 O2'        62.068  
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 
SAH   non-polymer         . S-ADENOSYL-L-HOMOCYSTEINE ?                 'C14 H20 N6 O5 S' 384.411 
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   -19 ?   ?   ?   A . n 
A 1 2   GLY 2   -18 ?   ?   ?   A . n 
A 1 3   SER 3   -17 ?   ?   ?   A . n 
A 1 4   SER 4   -16 ?   ?   ?   A . n 
A 1 5   HIS 5   -15 ?   ?   ?   A . n 
A 1 6   HIS 6   -14 ?   ?   ?   A . n 
A 1 7   HIS 7   -13 ?   ?   ?   A . n 
A 1 8   HIS 8   -12 ?   ?   ?   A . n 
A 1 9   HIS 9   -11 ?   ?   ?   A . n 
A 1 10  HIS 10  -10 ?   ?   ?   A . n 
A 1 11  SER 11  -9  ?   ?   ?   A . n 
A 1 12  SER 12  -8  ?   ?   ?   A . n 
A 1 13  GLY 13  -7  ?   ?   ?   A . n 
A 1 14  LEU 14  -6  ?   ?   ?   A . n 
A 1 15  VAL 15  -5  ?   ?   ?   A . n 
A 1 16  PRO 16  -4  ?   ?   ?   A . n 
A 1 17  ARG 17  -3  ?   ?   ?   A . n 
A 1 18  GLY 18  -2  ?   ?   ?   A . n 
A 1 19  SER 19  -1  ?   ?   ?   A . n 
A 1 20  HIS 20  0   ?   ?   ?   A . n 
A 1 21  MET 21  1   ?   ?   ?   A . n 
A 1 22  THR 22  2   ?   ?   ?   A . n 
A 1 23  ASP 23  3   3   ASP ASP A . n 
A 1 24  ASN 24  4   4   ASN ASN A . n 
A 1 25  PRO 25  5   5   PRO PRO A . n 
A 1 26  TYR 26  6   6   TYR TYR A . n 
A 1 27  GLU 27  7   7   GLU GLU A . n 
A 1 28  THR 28  8   8   THR THR A . n 
A 1 29  ASP 29  9   9   ASP ASP A . n 
A 1 30  GLU 30  10  10  GLU GLU A . n 
A 1 31  LEU 31  11  11  LEU LEU A . n 
A 1 32  LEU 32  12  12  LEU LEU A . n 
A 1 33  GLY 33  13  13  GLY GLY A . n 
A 1 34  GLN 34  14  14  GLN GLN A . n 
A 1 35  TYR 35  15  15  TYR TYR A . n 
A 1 36  LEU 36  16  16  LEU LEU A . n 
A 1 37  ASP 37  17  17  ASP ASP A . n 
A 1 38  PHE 38  18  18  PHE PHE A . n 
A 1 39  HIS 39  19  19  HIS HIS A . n 
A 1 40  TYR 40  20  20  TYR TYR A . n 
A 1 41  GLY 41  21  21  GLY GLY A . n 
A 1 42  PRO 42  22  22  PRO PRO A . n 
A 1 43  GLY 43  23  23  GLY GLY A . n 
A 1 44  HIS 44  24  24  HIS HIS A . n 
A 1 45  PHE 45  25  25  PHE PHE A . n 
A 1 46  ASP 46  26  26  ASP ASP A . n 
A 1 47  VAL 47  27  27  VAL VAL A . n 
A 1 48  PRO 48  28  28  PRO PRO A . n 
A 1 49  ASN 49  29  29  ASN ASN A . n 
A 1 50  TYR 50  30  30  TYR TYR A . n 
A 1 51  PRO 51  31  31  PRO PRO A . n 
A 1 52  LYS 52  32  32  LYS LYS A . n 
A 1 53  ALA 53  33  33  ALA ALA A . n 
A 1 54  CYS 54  34  34  CYS CYS A . n 
A 1 55  ILE 55  35  35  ILE ILE A . n 
A 1 56  GLU 56  36  36  GLU GLU A . n 
A 1 57  GLN 57  37  37  GLN GLN A . n 
A 1 58  ALA 58  38  38  ALA ALA A . n 
A 1 59  LEU 59  39  39  LEU LEU A . n 
A 1 60  ALA 60  40  40  ALA ALA A . n 
A 1 61  HIS 61  41  41  HIS HIS A . n 
A 1 62  HIS 62  42  42  HIS HIS A . n 
A 1 63  THR 63  43  43  THR THR A . n 
A 1 64  GLY 64  44  44  GLY GLY A . n 
A 1 65  THR 65  45  45  THR THR A . n 
A 1 66  THR 66  46  46  THR THR A . n 
A 1 67  GLY 67  47  47  GLY GLY A . n 
A 1 68  ARG 68  48  48  ARG ARG A . n 
A 1 69  ALA 69  49  49  ALA ALA A . n 
A 1 70  LEU 70  50  50  LEU LEU A . n 
A 1 71  ASP 71  51  51  ASP ASP A . n 
A 1 72  LEU 72  52  52  LEU LEU A . n 
A 1 73  GLY 73  53  53  GLY GLY A . n 
A 1 74  CYS 74  54  54  CYS CYS A . n 
A 1 75  ALA 75  55  55  ALA ALA A . n 
A 1 76  VAL 76  56  56  VAL VAL A . n 
A 1 77  GLY 77  57  57  GLY GLY A . n 
A 1 78  ARG 78  58  58  ARG ARG A . n 
A 1 79  SER 79  59  59  SER SER A . n 
A 1 80  SER 80  60  60  SER SER A . n 
A 1 81  PHE 81  61  61  PHE PHE A . n 
A 1 82  GLU 82  62  62  GLU GLU A . n 
A 1 83  LEU 83  63  63  LEU LEU A . n 
A 1 84  ALA 84  64  64  ALA ALA A . n 
A 1 85  ARG 85  65  65  ARG ARG A . n 
A 1 86  ARG 86  66  66  ARG ARG A . n 
A 1 87  PHE 87  67  67  PHE PHE A . n 
A 1 88  ASP 88  68  68  ASP ASP A . n 
A 1 89  GLU 89  69  69  GLU GLU A . n 
A 1 90  VAL 90  70  70  VAL VAL A . n 
A 1 91  ILE 91  71  71  ILE ILE A . n 
A 1 92  GLY 92  72  72  GLY GLY A . n 
A 1 93  ILE 93  73  73  ILE ILE A . n 
A 1 94  ASP 94  74  74  ASP ASP A . n 
A 1 95  LEU 95  75  75  LEU LEU A . n 
A 1 96  SER 96  76  76  SER SER A . n 
A 1 97  ARG 97  77  77  ARG ARG A . n 
A 1 98  ARG 98  78  78  ARG ARG A . n 
A 1 99  PHE 99  79  79  PHE PHE A . n 
A 1 100 ILE 100 80  80  ILE ILE A . n 
A 1 101 ASP 101 81  81  ASP ASP A . n 
A 1 102 SER 102 82  82  SER SER A . n 
A 1 103 ALA 103 83  83  ALA ALA A . n 
A 1 104 THR 104 84  84  THR THR A . n 
A 1 105 ARG 105 85  85  ARG ARG A . n 
A 1 106 LEU 106 86  86  LEU LEU A . n 
A 1 107 ALA 107 87  87  ALA ALA A . n 
A 1 108 GLU 108 88  88  GLU GLU A . n 
A 1 109 GLN 109 89  89  GLN GLN A . n 
A 1 110 GLY 110 90  90  GLY GLY A . n 
A 1 111 GLN 111 91  91  GLN GLN A . n 
A 1 112 LEU 112 92  92  LEU LEU A . n 
A 1 113 GLN 113 93  93  GLN GLN A . n 
A 1 114 TYR 114 94  94  TYR TYR A . n 
A 1 115 GLN 115 95  95  GLN GLN A . n 
A 1 116 VAL 116 96  96  VAL VAL A . n 
A 1 117 THR 117 97  97  THR THR A . n 
A 1 118 LEU 118 98  98  LEU LEU A . n 
A 1 119 GLU 119 99  99  GLU GLU A . n 
A 1 120 GLY 120 100 100 GLY GLY A . n 
A 1 121 GLU 121 101 101 GLU GLU A . n 
A 1 122 LEU 122 102 102 LEU LEU A . n 
A 1 123 ILE 123 103 103 ILE ILE A . n 
A 1 124 GLU 124 104 104 GLU GLU A . n 
A 1 125 ARG 125 105 105 ARG ARG A . n 
A 1 126 ARG 126 106 106 ARG ARG A . n 
A 1 127 THR 127 107 107 THR THR A . n 
A 1 128 ALA 128 108 108 ALA ALA A . n 
A 1 129 ASP 129 109 109 ASP ASP A . n 
A 1 130 LEU 130 110 110 LEU LEU A . n 
A 1 131 ALA 131 111 111 ALA ALA A . n 
A 1 132 ALA 132 112 112 ALA ALA A . n 
A 1 133 LEU 133 113 113 LEU LEU A . n 
A 1 134 GLU 134 114 114 GLU GLU A . n 
A 1 135 LEU 135 115 115 LEU LEU A . n 
A 1 136 SER 136 116 116 SER SER A . n 
A 1 137 ASN 137 117 117 ASN ASN A . n 
A 1 138 THR 138 118 118 THR THR A . n 
A 1 139 ALA 139 119 119 ALA ALA A . n 
A 1 140 GLY 140 120 120 GLY GLY A . n 
A 1 141 ARG 141 121 121 ARG ARG A . n 
A 1 142 THR 142 122 122 THR THR A . n 
A 1 143 ARG 143 123 123 ARG ARG A . n 
A 1 144 PHE 144 124 124 PHE PHE A . n 
A 1 145 GLN 145 125 125 GLN GLN A . n 
A 1 146 VAL 146 126 126 VAL VAL A . n 
A 1 147 GLY 147 127 127 GLY GLY A . n 
A 1 148 ASP 148 128 128 ASP ASP A . n 
A 1 149 ALA 149 129 129 ALA ALA A . n 
A 1 150 CYS 150 130 130 CYS CYS A . n 
A 1 151 ALA 151 131 131 ALA ALA A . n 
A 1 152 LEU 152 132 132 LEU LEU A . n 
A 1 153 ASP 153 133 133 ASP ASP A . n 
A 1 154 ASP 154 134 134 ASP ASP A . n 
A 1 155 THR 155 135 135 THR THR A . n 
A 1 156 LEU 156 136 136 LEU LEU A . n 
A 1 157 GLY 157 137 137 GLY GLY A . n 
A 1 158 ARG 158 138 138 ARG ARG A . n 
A 1 159 PHE 159 139 139 PHE PHE A . n 
A 1 160 ASP 160 140 140 ASP ASP A . n 
A 1 161 LEU 161 141 141 LEU LEU A . n 
A 1 162 ILE 162 142 142 ILE ILE A . n 
A 1 163 PHE 163 143 143 PHE PHE A . n 
A 1 164 ALA 164 144 144 ALA ALA A . n 
A 1 165 GLY 165 145 145 GLY GLY A . n 
A 1 166 ASN 166 146 146 ASN ASN A . n 
A 1 167 LEU 167 147 147 LEU LEU A . n 
A 1 168 ILE 168 148 148 ILE ILE A . n 
A 1 169 ASP 169 149 149 ASP ASP A . n 
A 1 170 ARG 170 150 150 ARG ARG A . n 
A 1 171 LEU 171 151 151 LEU LEU A . n 
A 1 172 PRO 172 152 152 PRO PRO A . n 
A 1 173 ASP 173 153 153 ASP ASP A . n 
A 1 174 PRO 174 154 154 PRO PRO A . n 
A 1 175 ALA 175 155 155 ALA ALA A . n 
A 1 176 ALA 176 156 156 ALA ALA A . n 
A 1 177 PHE 177 157 157 PHE PHE A . n 
A 1 178 LEU 178 158 158 LEU LEU A . n 
A 1 179 ALA 179 159 159 ALA ALA A . n 
A 1 180 GLN 180 160 160 GLN GLN A . n 
A 1 181 LEU 181 161 161 LEU LEU A . n 
A 1 182 PRO 182 162 162 PRO PRO A . n 
A 1 183 ALA 183 163 163 ALA ALA A . n 
A 1 184 LEU 184 164 164 LEU LEU A . n 
A 1 185 VAL 185 165 165 VAL VAL A . n 
A 1 186 ARG 186 166 166 ARG ARG A . n 
A 1 187 PRO 187 167 167 PRO PRO A . n 
A 1 188 GLY 188 168 168 GLY GLY A . n 
A 1 189 GLY 189 169 169 GLY GLY A . n 
A 1 190 LEU 190 170 170 LEU LEU A . n 
A 1 191 LEU 191 171 171 LEU LEU A . n 
A 1 192 MET 192 172 172 MET MET A . n 
A 1 193 ILE 193 173 173 ILE ILE A . n 
A 1 194 THR 194 174 174 THR THR A . n 
A 1 195 SER 195 175 175 SER SER A . n 
A 1 196 PRO 196 176 176 PRO PRO A . n 
A 1 197 TYR 197 177 177 TYR TYR A . n 
A 1 198 THR 198 178 178 THR THR A . n 
A 1 199 LEU 199 179 179 LEU LEU A . n 
A 1 200 LEU 200 180 180 LEU LEU A . n 
A 1 201 PRO 201 181 181 PRO PRO A . n 
A 1 202 GLU 202 182 182 GLU GLU A . n 
A 1 203 PHE 203 183 183 PHE PHE A . n 
A 1 204 THR 204 184 184 THR THR A . n 
A 1 205 PRO 205 185 185 PRO PRO A . n 
A 1 206 ARG 206 186 186 ARG ARG A . n 
A 1 207 GLU 207 187 187 GLU GLU A . n 
A 1 208 ARG 208 188 188 ARG ARG A . n 
A 1 209 TRP 209 189 189 TRP TRP A . n 
A 1 210 ILE 210 190 190 ILE ILE A . n 
A 1 211 GLY 211 191 191 GLY GLY A . n 
A 1 212 GLY 212 192 192 GLY GLY A . n 
A 1 213 PHE 213 193 193 PHE PHE A . n 
A 1 214 GLU 214 194 194 GLU GLU A . n 
A 1 215 ARG 215 195 195 ARG ARG A . n 
A 1 216 ASN 216 196 196 ASN ASN A . n 
A 1 217 GLY 217 197 197 GLY GLY A . n 
A 1 218 GLN 218 198 198 GLN GLN A . n 
A 1 219 PRO 219 199 199 PRO PRO A . n 
A 1 220 VAL 220 200 200 VAL VAL A . n 
A 1 221 ARG 221 201 201 ARG ARG A . n 
A 1 222 MET 222 202 202 MET MET A . n 
A 1 223 LEU 223 203 203 LEU LEU A . n 
A 1 224 ASP 224 204 204 ASP ASP A . n 
A 1 225 GLY 225 205 205 GLY GLY A . n 
A 1 226 LEU 226 206 206 LEU LEU A . n 
A 1 227 ARG 227 207 207 ARG ARG A . n 
A 1 228 HIS 228 208 208 HIS HIS A . n 
A 1 229 HIS 229 209 209 HIS HIS A . n 
A 1 230 LEU 230 210 210 LEU LEU A . n 
A 1 231 GLU 231 211 211 GLU GLU A . n 
A 1 232 PRO 232 212 212 PRO PRO A . n 
A 1 233 ASP 233 213 213 ASP ASP A . n 
A 1 234 PHE 234 214 214 PHE PHE A . n 
A 1 235 VAL 235 215 215 VAL VAL A . n 
A 1 236 LEU 236 216 216 LEU LEU A . n 
A 1 237 LEU 237 217 217 LEU LEU A . n 
A 1 238 GLU 238 218 218 GLU GLU A . n 
A 1 239 PRO 239 219 219 PRO PRO A . n 
A 1 240 THR 240 220 220 THR THR A . n 
A 1 241 ARG 241 221 221 ARG ARG A . n 
A 1 242 ASP 242 222 222 ASP ASP A . n 
A 1 243 ILE 243 223 223 ILE ILE A . n 
A 1 244 PRO 244 224 224 PRO PRO A . n 
A 1 245 PHE 245 225 225 PHE PHE A . n 
A 1 246 VAL 246 226 226 VAL VAL A . n 
A 1 247 ILE 247 227 227 ILE ILE A . n 
A 1 248 ARG 248 228 228 ARG ARG A . n 
A 1 249 GLU 249 229 229 GLU GLU A . n 
A 1 250 THR 250 230 230 THR THR A . n 
A 1 251 THR 251 231 231 THR THR A . n 
A 1 252 ARG 252 232 232 ARG ARG A . n 
A 1 253 LYS 253 233 233 LYS LYS A . n 
A 1 254 TYR 254 234 234 TYR TYR A . n 
A 1 255 GLN 255 235 235 GLN GLN A . n 
A 1 256 HIS 256 236 236 HIS HIS A . n 
A 1 257 THR 257 237 237 THR THR A . n 
A 1 258 VAL 258 238 238 VAL VAL A . n 
A 1 259 ALA 259 239 239 ALA ALA A . n 
A 1 260 GLU 260 240 240 GLU GLU A . n 
A 1 261 ALA 261 241 241 ALA ALA A . n 
A 1 262 SER 262 242 242 SER SER A . n 
A 1 263 LEU 263 243 243 LEU LEU A . n 
A 1 264 TRP 264 244 244 TRP TRP A . n 
A 1 265 ARG 265 245 245 ARG ARG A . n 
A 1 266 ARG 266 246 246 ARG ARG A . n 
A 1 267 ALA 267 247 247 ALA ALA A . n 
# 
loop_
_pdbx_entity_instance_feature.ordinal 
_pdbx_entity_instance_feature.comp_id 
_pdbx_entity_instance_feature.asym_id 
_pdbx_entity_instance_feature.seq_num 
_pdbx_entity_instance_feature.auth_comp_id 
_pdbx_entity_instance_feature.auth_asym_id 
_pdbx_entity_instance_feature.auth_seq_num 
_pdbx_entity_instance_feature.feature_type 
_pdbx_entity_instance_feature.details 
1 A1AS0 ? ? A1AS0 ? ? 'SUBJECT OF INVESTIGATION' ? 
2 SAH   ? ? SAH   ? ? 'SUBJECT OF INVESTIGATION' ? 
# 
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 SAH   1   301 301 SAH   SAH A . 
C 3 A1AS0 1   302 302 A1AS0 S4H A . 
D 4 EDO   1   303 401 EDO   EDO A . 
E 5 HOH   1   401 57  HOH   HOH A . 
E 5 HOH   2   402 9   HOH   HOH A . 
E 5 HOH   3   403 52  HOH   HOH A . 
E 5 HOH   4   404 127 HOH   HOH A . 
E 5 HOH   5   405 31  HOH   HOH A . 
E 5 HOH   6   406 59  HOH   HOH A . 
E 5 HOH   7   407 36  HOH   HOH A . 
E 5 HOH   8   408 230 HOH   HOH A . 
E 5 HOH   9   409 128 HOH   HOH A . 
E 5 HOH   10  410 143 HOH   HOH A . 
E 5 HOH   11  411 155 HOH   HOH A . 
E 5 HOH   12  412 51  HOH   HOH A . 
E 5 HOH   13  413 33  HOH   HOH A . 
E 5 HOH   14  414 42  HOH   HOH A . 
E 5 HOH   15  415 186 HOH   HOH A . 
E 5 HOH   16  416 212 HOH   HOH A . 
E 5 HOH   17  417 88  HOH   HOH A . 
E 5 HOH   18  418 100 HOH   HOH A . 
E 5 HOH   19  419 153 HOH   HOH A . 
E 5 HOH   20  420 157 HOH   HOH A . 
E 5 HOH   21  421 28  HOH   HOH A . 
E 5 HOH   22  422 289 HOH   HOH A . 
E 5 HOH   23  423 71  HOH   HOH A . 
E 5 HOH   24  424 118 HOH   HOH A . 
E 5 HOH   25  425 229 HOH   HOH A . 
E 5 HOH   26  426 41  HOH   HOH A . 
E 5 HOH   27  427 282 HOH   HOH A . 
E 5 HOH   28  428 53  HOH   HOH A . 
E 5 HOH   29  429 108 HOH   HOH A . 
E 5 HOH   30  430 141 HOH   HOH A . 
E 5 HOH   31  431 35  HOH   HOH A . 
E 5 HOH   32  432 219 HOH   HOH A . 
E 5 HOH   33  433 256 HOH   HOH A . 
E 5 HOH   34  434 182 HOH   HOH A . 
E 5 HOH   35  435 104 HOH   HOH A . 
E 5 HOH   36  436 112 HOH   HOH A . 
E 5 HOH   37  437 8   HOH   HOH A . 
E 5 HOH   38  438 45  HOH   HOH A . 
E 5 HOH   39  439 13  HOH   HOH A . 
E 5 HOH   40  440 7   HOH   HOH A . 
E 5 HOH   41  441 226 HOH   HOH A . 
E 5 HOH   42  442 115 HOH   HOH A . 
E 5 HOH   43  443 103 HOH   HOH A . 
E 5 HOH   44  444 90  HOH   HOH A . 
E 5 HOH   45  445 142 HOH   HOH A . 
E 5 HOH   46  446 69  HOH   HOH A . 
E 5 HOH   47  447 11  HOH   HOH A . 
E 5 HOH   48  448 168 HOH   HOH A . 
E 5 HOH   49  449 129 HOH   HOH A . 
E 5 HOH   50  450 87  HOH   HOH A . 
E 5 HOH   51  451 2   HOH   HOH A . 
E 5 HOH   52  452 172 HOH   HOH A . 
E 5 HOH   53  453 18  HOH   HOH A . 
E 5 HOH   54  454 223 HOH   HOH A . 
E 5 HOH   55  455 232 HOH   HOH A . 
E 5 HOH   56  456 81  HOH   HOH A . 
E 5 HOH   57  457 75  HOH   HOH A . 
E 5 HOH   58  458 160 HOH   HOH A . 
E 5 HOH   59  459 70  HOH   HOH A . 
E 5 HOH   60  460 39  HOH   HOH A . 
E 5 HOH   61  461 4   HOH   HOH A . 
E 5 HOH   62  462 225 HOH   HOH A . 
E 5 HOH   63  463 63  HOH   HOH A . 
E 5 HOH   64  464 43  HOH   HOH A . 
E 5 HOH   65  465 62  HOH   HOH A . 
E 5 HOH   66  466 101 HOH   HOH A . 
E 5 HOH   67  467 307 HOH   HOH A . 
E 5 HOH   68  468 107 HOH   HOH A . 
E 5 HOH   69  469 61  HOH   HOH A . 
E 5 HOH   70  470 292 HOH   HOH A . 
E 5 HOH   71  471 10  HOH   HOH A . 
E 5 HOH   72  472 6   HOH   HOH A . 
E 5 HOH   73  473 34  HOH   HOH A . 
E 5 HOH   74  474 80  HOH   HOH A . 
E 5 HOH   75  475 21  HOH   HOH A . 
E 5 HOH   76  476 213 HOH   HOH A . 
E 5 HOH   77  477 136 HOH   HOH A . 
E 5 HOH   78  478 38  HOH   HOH A . 
E 5 HOH   79  479 310 HOH   HOH A . 
E 5 HOH   80  480 22  HOH   HOH A . 
E 5 HOH   81  481 89  HOH   HOH A . 
E 5 HOH   82  482 68  HOH   HOH A . 
E 5 HOH   83  483 96  HOH   HOH A . 
E 5 HOH   84  484 228 HOH   HOH A . 
E 5 HOH   85  485 308 HOH   HOH A . 
E 5 HOH   86  486 12  HOH   HOH A . 
E 5 HOH   87  487 146 HOH   HOH A . 
E 5 HOH   88  488 3   HOH   HOH A . 
E 5 HOH   89  489 110 HOH   HOH A . 
E 5 HOH   90  490 247 HOH   HOH A . 
E 5 HOH   91  491 281 HOH   HOH A . 
E 5 HOH   92  492 29  HOH   HOH A . 
E 5 HOH   93  493 158 HOH   HOH A . 
E 5 HOH   94  494 102 HOH   HOH A . 
E 5 HOH   95  495 167 HOH   HOH A . 
E 5 HOH   96  496 37  HOH   HOH A . 
E 5 HOH   97  497 185 HOH   HOH A . 
E 5 HOH   98  498 176 HOH   HOH A . 
E 5 HOH   99  499 14  HOH   HOH A . 
E 5 HOH   100 500 196 HOH   HOH A . 
E 5 HOH   101 501 98  HOH   HOH A . 
E 5 HOH   102 502 309 HOH   HOH A . 
E 5 HOH   103 503 137 HOH   HOH A . 
E 5 HOH   104 504 262 HOH   HOH A . 
E 5 HOH   105 505 54  HOH   HOH A . 
E 5 HOH   106 506 50  HOH   HOH A . 
E 5 HOH   107 507 264 HOH   HOH A . 
E 5 HOH   108 508 82  HOH   HOH A . 
E 5 HOH   109 509 20  HOH   HOH A . 
E 5 HOH   110 510 15  HOH   HOH A . 
E 5 HOH   111 511 119 HOH   HOH A . 
E 5 HOH   112 512 79  HOH   HOH A . 
E 5 HOH   113 513 74  HOH   HOH A . 
E 5 HOH   114 514 221 HOH   HOH A . 
E 5 HOH   115 515 16  HOH   HOH A . 
E 5 HOH   116 516 73  HOH   HOH A . 
E 5 HOH   117 517 48  HOH   HOH A . 
E 5 HOH   118 518 122 HOH   HOH A . 
E 5 HOH   119 519 91  HOH   HOH A . 
E 5 HOH   120 520 23  HOH   HOH A . 
E 5 HOH   121 521 84  HOH   HOH A . 
E 5 HOH   122 522 17  HOH   HOH A . 
E 5 HOH   123 523 302 HOH   HOH A . 
E 5 HOH   124 524 124 HOH   HOH A . 
E 5 HOH   125 525 144 HOH   HOH A . 
E 5 HOH   126 526 192 HOH   HOH A . 
E 5 HOH   127 527 317 HOH   HOH A . 
E 5 HOH   128 528 27  HOH   HOH A . 
E 5 HOH   129 529 147 HOH   HOH A . 
E 5 HOH   130 530 93  HOH   HOH A . 
E 5 HOH   131 531 5   HOH   HOH A . 
E 5 HOH   132 532 235 HOH   HOH A . 
E 5 HOH   133 533 32  HOH   HOH A . 
E 5 HOH   134 534 240 HOH   HOH A . 
E 5 HOH   135 535 145 HOH   HOH A . 
E 5 HOH   136 536 297 HOH   HOH A . 
E 5 HOH   137 537 133 HOH   HOH A . 
E 5 HOH   138 538 175 HOH   HOH A . 
E 5 HOH   139 539 184 HOH   HOH A . 
E 5 HOH   140 540 238 HOH   HOH A . 
E 5 HOH   141 541 231 HOH   HOH A . 
E 5 HOH   142 542 26  HOH   HOH A . 
E 5 HOH   143 543 85  HOH   HOH A . 
E 5 HOH   144 544 178 HOH   HOH A . 
E 5 HOH   145 545 60  HOH   HOH A . 
E 5 HOH   146 546 120 HOH   HOH A . 
E 5 HOH   147 547 207 HOH   HOH A . 
E 5 HOH   148 548 86  HOH   HOH A . 
E 5 HOH   149 549 30  HOH   HOH A . 
E 5 HOH   150 550 106 HOH   HOH A . 
E 5 HOH   151 551 170 HOH   HOH A . 
E 5 HOH   152 552 65  HOH   HOH A . 
E 5 HOH   153 553 151 HOH   HOH A . 
E 5 HOH   154 554 105 HOH   HOH A . 
E 5 HOH   155 555 19  HOH   HOH A . 
E 5 HOH   156 556 149 HOH   HOH A . 
E 5 HOH   157 557 165 HOH   HOH A . 
E 5 HOH   158 558 195 HOH   HOH A . 
E 5 HOH   159 559 46  HOH   HOH A . 
E 5 HOH   160 560 169 HOH   HOH A . 
E 5 HOH   161 561 72  HOH   HOH A . 
E 5 HOH   162 562 161 HOH   HOH A . 
E 5 HOH   163 563 123 HOH   HOH A . 
E 5 HOH   164 564 64  HOH   HOH A . 
E 5 HOH   165 565 275 HOH   HOH A . 
E 5 HOH   166 566 95  HOH   HOH A . 
E 5 HOH   167 567 117 HOH   HOH A . 
E 5 HOH   168 568 181 HOH   HOH A . 
E 5 HOH   169 569 24  HOH   HOH A . 
E 5 HOH   170 570 250 HOH   HOH A . 
E 5 HOH   171 571 174 HOH   HOH A . 
E 5 HOH   172 572 171 HOH   HOH A . 
E 5 HOH   173 573 56  HOH   HOH A . 
E 5 HOH   174 574 249 HOH   HOH A . 
E 5 HOH   175 575 40  HOH   HOH A . 
E 5 HOH   176 576 138 HOH   HOH A . 
E 5 HOH   177 577 47  HOH   HOH A . 
E 5 HOH   178 578 67  HOH   HOH A . 
E 5 HOH   179 579 77  HOH   HOH A . 
E 5 HOH   180 580 92  HOH   HOH A . 
E 5 HOH   181 581 255 HOH   HOH A . 
E 5 HOH   182 582 113 HOH   HOH A . 
E 5 HOH   183 583 159 HOH   HOH A . 
E 5 HOH   184 584 154 HOH   HOH A . 
E 5 HOH   185 585 166 HOH   HOH A . 
E 5 HOH   186 586 162 HOH   HOH A . 
E 5 HOH   187 587 163 HOH   HOH A . 
E 5 HOH   188 588 135 HOH   HOH A . 
E 5 HOH   189 589 217 HOH   HOH A . 
E 5 HOH   190 590 311 HOH   HOH A . 
E 5 HOH   191 591 78  HOH   HOH A . 
E 5 HOH   192 592 216 HOH   HOH A . 
E 5 HOH   193 593 156 HOH   HOH A . 
E 5 HOH   194 594 224 HOH   HOH A . 
E 5 HOH   195 595 198 HOH   HOH A . 
E 5 HOH   196 596 251 HOH   HOH A . 
E 5 HOH   197 597 152 HOH   HOH A . 
E 5 HOH   198 598 209 HOH   HOH A . 
E 5 HOH   199 599 76  HOH   HOH A . 
E 5 HOH   200 600 301 HOH   HOH A . 
E 5 HOH   201 601 265 HOH   HOH A . 
E 5 HOH   202 602 243 HOH   HOH A . 
E 5 HOH   203 603 199 HOH   HOH A . 
E 5 HOH   204 604 293 HOH   HOH A . 
E 5 HOH   205 605 111 HOH   HOH A . 
E 5 HOH   206 606 239 HOH   HOH A . 
E 5 HOH   207 607 193 HOH   HOH A . 
E 5 HOH   208 608 197 HOH   HOH A . 
E 5 HOH   209 609 268 HOH   HOH A . 
E 5 HOH   210 610 300 HOH   HOH A . 
E 5 HOH   211 611 237 HOH   HOH A . 
E 5 HOH   212 612 200 HOH   HOH A . 
E 5 HOH   213 613 66  HOH   HOH A . 
E 5 HOH   214 614 179 HOH   HOH A . 
E 5 HOH   215 615 242 HOH   HOH A . 
E 5 HOH   216 616 208 HOH   HOH A . 
E 5 HOH   217 617 253 HOH   HOH A . 
E 5 HOH   218 618 140 HOH   HOH A . 
E 5 HOH   219 619 257 HOH   HOH A . 
E 5 HOH   220 620 304 HOH   HOH A . 
E 5 HOH   221 621 164 HOH   HOH A . 
E 5 HOH   222 622 220 HOH   HOH A . 
E 5 HOH   223 623 49  HOH   HOH A . 
E 5 HOH   224 624 180 HOH   HOH A . 
E 5 HOH   225 625 285 HOH   HOH A . 
E 5 HOH   226 626 191 HOH   HOH A . 
E 5 HOH   227 627 234 HOH   HOH A . 
E 5 HOH   228 628 177 HOH   HOH A . 
E 5 HOH   229 629 187 HOH   HOH A . 
E 5 HOH   230 630 305 HOH   HOH A . 
E 5 HOH   231 631 258 HOH   HOH A . 
E 5 HOH   232 632 210 HOH   HOH A . 
E 5 HOH   233 633 272 HOH   HOH A . 
E 5 HOH   234 634 121 HOH   HOH A . 
E 5 HOH   235 635 132 HOH   HOH A . 
E 5 HOH   236 636 222 HOH   HOH A . 
E 5 HOH   237 637 148 HOH   HOH A . 
E 5 HOH   238 638 274 HOH   HOH A . 
E 5 HOH   239 639 214 HOH   HOH A . 
E 5 HOH   240 640 58  HOH   HOH A . 
E 5 HOH   241 641 316 HOH   HOH A . 
E 5 HOH   242 642 313 HOH   HOH A . 
E 5 HOH   243 643 315 HOH   HOH A . 
E 5 HOH   244 644 273 HOH   HOH A . 
E 5 HOH   245 645 130 HOH   HOH A . 
E 5 HOH   246 646 267 HOH   HOH A . 
E 5 HOH   247 647 306 HOH   HOH A . 
E 5 HOH   248 648 314 HOH   HOH A . 
E 5 HOH   249 649 277 HOH   HOH A . 
E 5 HOH   250 650 246 HOH   HOH A . 
E 5 HOH   251 651 131 HOH   HOH A . 
E 5 HOH   252 652 252 HOH   HOH A . 
E 5 HOH   253 653 312 HOH   HOH A . 
E 5 HOH   254 654 83  HOH   HOH A . 
E 5 HOH   255 655 116 HOH   HOH A . 
E 5 HOH   256 656 269 HOH   HOH A . 
E 5 HOH   257 657 126 HOH   HOH A . 
E 5 HOH   258 658 194 HOH   HOH A . 
E 5 HOH   259 659 44  HOH   HOH A . 
E 5 HOH   260 660 202 HOH   HOH A . 
E 5 HOH   261 661 25  HOH   HOH A . 
E 5 HOH   262 662 125 HOH   HOH A . 
E 5 HOH   263 663 245 HOH   HOH A . 
E 5 HOH   264 664 173 HOH   HOH A . 
E 5 HOH   265 665 188 HOH   HOH A . 
E 5 HOH   266 666 266 HOH   HOH A . 
E 5 HOH   267 667 109 HOH   HOH A . 
E 5 HOH   268 668 201 HOH   HOH A . 
E 5 HOH   269 669 303 HOH   HOH A . 
E 5 HOH   270 670 114 HOH   HOH A . 
E 5 HOH   271 671 94  HOH   HOH A . 
E 5 HOH   272 672 248 HOH   HOH A . 
E 5 HOH   273 673 134 HOH   HOH A . 
E 5 HOH   274 674 99  HOH   HOH A . 
E 5 HOH   275 675 189 HOH   HOH A . 
E 5 HOH   276 676 261 HOH   HOH A . 
E 5 HOH   277 677 288 HOH   HOH A . 
E 5 HOH   278 678 55  HOH   HOH A . 
E 5 HOH   279 679 263 HOH   HOH A . 
E 5 HOH   280 680 233 HOH   HOH A . 
E 5 HOH   281 681 190 HOH   HOH A . 
E 5 HOH   282 682 139 HOH   HOH A . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A ASP 3   ? CG  ? A ASP 23  CG  
2  1 Y 1 A ASP 3   ? OD1 ? A ASP 23  OD1 
3  1 Y 1 A ASP 3   ? OD2 ? A ASP 23  OD2 
4  1 Y 1 A LYS 32  ? NZ  ? A LYS 52  NZ  
5  1 Y 1 A ARG 65  ? NH1 ? A ARG 85  NH1 
6  1 Y 1 A ARG 65  ? NH2 ? A ARG 85  NH2 
7  1 Y 1 A ARG 66  ? CG  ? A ARG 86  CG  
8  1 Y 1 A ARG 66  ? CD  ? A ARG 86  CD  
9  1 Y 1 A ARG 66  ? NE  ? A ARG 86  NE  
10 1 Y 1 A ARG 66  ? CZ  ? A ARG 86  CZ  
11 1 Y 1 A ARG 66  ? NH1 ? A ARG 86  NH1 
12 1 Y 1 A ARG 66  ? NH2 ? A ARG 86  NH2 
13 1 Y 1 A GLU 114 ? CD  ? A GLU 134 CD  
14 1 Y 1 A GLU 114 ? OE1 ? A GLU 134 OE1 
15 1 Y 1 A GLU 114 ? OE2 ? A GLU 134 OE2 
16 1 Y 1 A ASN 117 ? CG  ? A ASN 137 CG  
17 1 Y 1 A ASN 117 ? OD1 ? A ASN 137 OD1 
18 1 Y 1 A ASN 117 ? ND2 ? A ASN 137 ND2 
19 1 Y 1 A ARG 188 ? CZ  ? A ARG 208 CZ  
20 1 Y 1 A ARG 188 ? NH1 ? A ARG 208 NH1 
21 1 Y 1 A ARG 188 ? NH2 ? A ARG 208 NH2 
22 1 Y 1 A ASN 196 ? ND2 ? A ASN 216 ND2 
23 1 Y 1 A GLN 198 ? CG  ? A GLN 218 CG  
24 1 Y 1 A GLN 198 ? CD  ? A GLN 218 CD  
25 1 Y 1 A GLN 198 ? OE1 ? A GLN 218 OE1 
26 1 Y 1 A GLN 198 ? NE2 ? A GLN 218 NE2 
27 1 Y 1 A GLU 218 ? OE1 ? A GLU 238 OE1 
28 1 Y 1 A GLU 218 ? OE2 ? A GLU 238 OE2 
29 1 Y 1 A ARG 221 ? CG  ? A ARG 241 CG  
30 1 Y 1 A ARG 221 ? CD  ? A ARG 241 CD  
31 1 Y 1 A ARG 221 ? NE  ? A ARG 241 NE  
32 1 Y 1 A ARG 221 ? CZ  ? A ARG 241 CZ  
33 1 Y 1 A ARG 221 ? NH1 ? A ARG 241 NH1 
34 1 Y 1 A ARG 221 ? NH2 ? A ARG 241 NH2 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? XDS-Apple_M1 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? XDS-Apple_M1 2 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER ? ? ? 1.20.1_4487  3 
? 'model building' ? ? ? ? ? ? ? ? ? ? ? Coot   ? ? ? 0.9.8.7      4 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX ? ? ? 1.20.1_4487  5 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.000 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9BXK 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     83.838 
_cell.length_a_esd                 ? 
_cell.length_b                     90.058 
_cell.length_b_esd                 ? 
_cell.length_c                     80.321 
_cell.length_c_esd                 ? 
_cell.volume                       606446.249 
_cell.volume_esd                   ? 
_cell.Z_PDB                        8 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9BXK 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                20 
_symmetry.space_group_name_Hall            'C 2c 2' 
_symmetry.space_group_name_H-M             'C 2 2 21' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9BXK 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.5 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          50.8 
_exptl_crystal.description                  Plates 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              8.5 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '0.1 M Tris-HCl, pH 8.5, 0.2 M tri-sodium citrate, 30% v/v PEG400' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER2 S 16M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2023-10-19 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.9686 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'CHESS BEAMLINE 7B2' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.9686 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   7B2 
_diffrn_source.pdbx_synchrotron_site       CHESS 
# 
_reflns.B_iso_Wilson_estimate                          20.26 
_reflns.entry_id                                       9BXK 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.66 
_reflns.d_resolution_low                               29 
_reflns.details                                        ? 
_reflns.limit_h_max                                    ? 
_reflns.limit_h_min                                    ? 
_reflns.limit_k_max                                    ? 
_reflns.limit_k_min                                    ? 
_reflns.limit_l_max                                    ? 
_reflns.limit_l_min                                    ? 
_reflns.number_all                                     ? 
_reflns.number_obs                                     35794 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           98.75 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                1.9 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          9.95 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.07543 
_reflns.pdbx_Rpim_I_all                                0.05334 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.997 
_reflns.pdbx_CC_star                                   0.999 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.05334 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.66 
_reflns_shell.d_res_low                                     1.719 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           1.20 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             3373 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               1.9 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               0.985 
_reflns_shell.pdbx_Rpim_I_all                               0.6965 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.521 
_reflns_shell.pdbx_CC_star                                  0.827 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          95.33 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  0.6965 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               24.79 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9BXK 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            1.66 
_refine.ls_d_res_low                             29.00 
_refine.ls_extinction_coef                       ? 
_refine.ls_extinction_coef_esd                   ? 
_refine.ls_extinction_expression                 ? 
_refine.ls_extinction_method                     ? 
_refine.ls_goodness_of_fit_all                   ? 
_refine.ls_goodness_of_fit_all_esd               ? 
_refine.ls_goodness_of_fit_obs                   ? 
_refine.ls_goodness_of_fit_obs_esd               ? 
_refine.ls_hydrogen_treatment                    ? 
_refine.ls_matrix_type                           ? 
_refine.ls_number_constraints                    ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_reflns_all                     ? 
_refine.ls_number_reflns_obs                     35767 
_refine.ls_number_reflns_R_free                  1362 
_refine.ls_number_reflns_R_work                  34405 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    98.79 
_refine.ls_percent_reflns_R_free                 3.81 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1787 
_refine.ls_R_factor_R_free                       0.2051 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1777 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.34 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          SIR 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'GeoStd + Monomer Library + CDL v1.2' 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.1000 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 23.4549 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.2028 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.66 
_refine_hist.d_res_low                        29.00 
_refine_hist.number_atoms_solvent             282 
_refine_hist.number_atoms_total               2236 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        1912 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         42 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.0113  ? 2000 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.2066  ? 2719 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0714  ? 302  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0349  ? 356  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 14.0392 ? 734  ? f_dihedral_angle_d ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 1.66 1.72  . . 130 3237 95.36 . . . . 0.3070 . . . . . . . . . . . 0.3582 
'X-RAY DIFFRACTION' 1.72 1.79  . . 131 3429 98.94 . . . . 0.2727 . . . . . . . . . . . 0.3164 
'X-RAY DIFFRACTION' 1.79 1.87  . . 133 3424 99.08 . . . . 0.2244 . . . . . . . . . . . 0.2509 
'X-RAY DIFFRACTION' 1.87 1.97  . . 136 3397 99.02 . . . . 0.2025 . . . . . . . . . . . 0.2385 
'X-RAY DIFFRACTION' 1.97 2.09  . . 128 3449 99.47 . . . . 0.1764 . . . . . . . . . . . 0.2074 
'X-RAY DIFFRACTION' 2.09 2.25  . . 147 3442 99.64 . . . . 0.1782 . . . . . . . . . . . 0.2047 
'X-RAY DIFFRACTION' 2.25 2.48  . . 139 3477 99.70 . . . . 0.1768 . . . . . . . . . . . 0.2015 
'X-RAY DIFFRACTION' 2.48 2.84  . . 136 3486 99.86 . . . . 0.1759 . . . . . . . . . . . 0.2173 
'X-RAY DIFFRACTION' 2.84 3.57  . . 142 3519 99.84 . . . . 0.1682 . . . . . . . . . . . 0.1882 
'X-RAY DIFFRACTION' 3.57 29.00 . . 140 3545 96.97 . . . . 0.1489 . . . . . . . . . . . 0.1697 
# 
_struct.entry_id                     9BXK 
_struct.title                        
'OvsM from Marinimicrobium koreense, an ovoselenol-biosynthetic N-methyltransferase in complex with 5-selenohistidine and SAH' 
_struct.pdbx_model_details           ? 
_struct.pdbx_formula_weight          ? 
_struct.pdbx_formula_weight_method   ? 
_struct.pdbx_model_type_details      ? 
_struct.pdbx_CASP_flag               N 
# 
_struct_keywords.entry_id        9BXK 
_struct_keywords.text            'ovoselenol, 5-selenohistidine, S-adenosyl-L-methionine, N-methyltransferase, TRANSFERASE' 
_struct_keywords.pdbx_keywords   TRANSFERASE 
# 
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 ? 
D N N 4 ? 
E N N 5 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    A0A3N1P0S2_9GAMM 
_struct_ref.pdbx_db_accession          A0A3N1P0S2 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MTDNPYETDELLGQYLDFHYGPGHFDVPNYPKACIEQALAHHTGTTGRALDLGCAVGRSSFELARRFDEVIGIDLSRRFI
DSATRLAEQGQLQYQVTLEGELIERRTADLAALELSNTAGRTRFQVGDACALDDTLGRFDLIFAGNLIDRLPDPAAFLAQ
LPALVRPGGLLMITSPYTLLPEFTPRERWIGGFERNGQPVRMLDGLRHHLEPDFVLLEPTRDIPFVIRETTRKYQHTVAE
ASLWRRA
;
_struct_ref.pdbx_align_begin           1 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              9BXK 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 21 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 267 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             A0A3N1P0S2 
_struct_ref_seq.db_align_beg                  1 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  247 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       1 
_struct_ref_seq.pdbx_auth_seq_align_end       247 
# 
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 9BXK MET A 1  ? UNP A0A3N1P0S2 ? ? 'expression tag' -19 1  
1 9BXK GLY A 2  ? UNP A0A3N1P0S2 ? ? 'expression tag' -18 2  
1 9BXK SER A 3  ? UNP A0A3N1P0S2 ? ? 'expression tag' -17 3  
1 9BXK SER A 4  ? UNP A0A3N1P0S2 ? ? 'expression tag' -16 4  
1 9BXK HIS A 5  ? UNP A0A3N1P0S2 ? ? 'expression tag' -15 5  
1 9BXK HIS A 6  ? UNP A0A3N1P0S2 ? ? 'expression tag' -14 6  
1 9BXK HIS A 7  ? UNP A0A3N1P0S2 ? ? 'expression tag' -13 7  
1 9BXK HIS A 8  ? UNP A0A3N1P0S2 ? ? 'expression tag' -12 8  
1 9BXK HIS A 9  ? UNP A0A3N1P0S2 ? ? 'expression tag' -11 9  
1 9BXK HIS A 10 ? UNP A0A3N1P0S2 ? ? 'expression tag' -10 10 
1 9BXK SER A 11 ? UNP A0A3N1P0S2 ? ? 'expression tag' -9  11 
1 9BXK SER A 12 ? UNP A0A3N1P0S2 ? ? 'expression tag' -8  12 
1 9BXK GLY A 13 ? UNP A0A3N1P0S2 ? ? 'expression tag' -7  13 
1 9BXK LEU A 14 ? UNP A0A3N1P0S2 ? ? 'expression tag' -6  14 
1 9BXK VAL A 15 ? UNP A0A3N1P0S2 ? ? 'expression tag' -5  15 
1 9BXK PRO A 16 ? UNP A0A3N1P0S2 ? ? 'expression tag' -4  16 
1 9BXK ARG A 17 ? UNP A0A3N1P0S2 ? ? 'expression tag' -3  17 
1 9BXK GLY A 18 ? UNP A0A3N1P0S2 ? ? 'expression tag' -2  18 
1 9BXK SER A 19 ? UNP A0A3N1P0S2 ? ? 'expression tag' -1  19 
1 9BXK HIS A 20 ? UNP A0A3N1P0S2 ? ? 'expression tag' 0   20 
# 
_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 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 590   ? 
1 MORE         4     ? 
1 'SSA (A^2)'  11310 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   none 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_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 ASN A 24  ? GLU A 27  ? ASN A 4   GLU A 7   5 ? 4  
HELX_P HELX_P2  AA2 THR A 28  ? GLY A 41  ? THR A 8   GLY A 21  1 ? 14 
HELX_P HELX_P3  AA3 ASN A 49  ? HIS A 62  ? ASN A 29  HIS A 42  1 ? 14 
HELX_P HELX_P4  AA4 GLY A 77  ? ALA A 84  ? GLY A 57  ALA A 64  1 ? 8  
HELX_P HELX_P5  AA5 SER A 96  ? GLY A 110 ? SER A 76  GLY A 90  1 ? 15 
HELX_P HELX_P6  AA6 ALA A 131 ? GLU A 134 ? ALA A 111 GLU A 114 5 ? 4  
HELX_P HELX_P7  AA7 THR A 138 ? GLY A 140 ? THR A 118 GLY A 120 5 ? 3  
HELX_P HELX_P8  AA8 LEU A 167 ? LEU A 171 ? LEU A 147 LEU A 151 5 ? 5  
HELX_P HELX_P9  AA9 ASP A 173 ? ALA A 179 ? ASP A 153 ALA A 159 1 ? 7  
HELX_P HELX_P10 AB1 GLN A 180 ? LEU A 184 ? GLN A 160 LEU A 164 1 ? 5  
HELX_P HELX_P11 AB2 PRO A 205 ? TRP A 209 ? PRO A 185 TRP A 189 5 ? 5  
HELX_P HELX_P12 AB3 ARG A 221 ? GLU A 231 ? ARG A 201 GLU A 211 1 ? 11 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 GLU 231 A . ? GLU 211 A PRO 232 A ? PRO 212 A 1 -2.44 
2 GLU 238 A . ? GLU 218 A PRO 239 A ? PRO 219 A 1 0.02  
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 7 ? 
AA2 ? 2 ? 
AA3 ? 2 ? 
# 
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 ? parallel      
AA1 2 3 ? parallel      
AA1 3 4 ? parallel      
AA1 4 5 ? parallel      
AA1 5 6 ? anti-parallel 
AA1 6 7 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA3 1 2 ? anti-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 THR A 142 ? VAL A 146 ? THR A 122 VAL A 126 
AA1 2 GLU A 89  ? ASP A 94  ? GLU A 69  ASP A 74  
AA1 3 ARG A 68  ? LEU A 72  ? ARG A 48  LEU A 52  
AA1 4 PHE A 159 ? GLY A 165 ? PHE A 139 GLY A 145 
AA1 5 VAL A 185 ? SER A 195 ? VAL A 165 SER A 175 
AA1 6 TYR A 254 ? ARG A 266 ? TYR A 234 ARG A 246 
AA1 7 PHE A 234 ? ARG A 248 ? PHE A 214 ARG A 228 
AA2 1 GLN A 111 ? GLU A 119 ? GLN A 91  GLU A 99  
AA2 2 LEU A 122 ? ASP A 129 ? LEU A 102 ASP A 109 
AA3 1 PHE A 213 ? ARG A 215 ? PHE A 193 ARG A 195 
AA3 2 GLN A 218 ? VAL A 220 ? GLN A 198 VAL A 200 
# 
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 O ARG A 143 ? O ARG A 123 N GLY A 92  ? N GLY A 72  
AA1 2 3 O ILE A 91  ? O ILE A 71  N ASP A 71  ? N ASP A 51  
AA1 3 4 N LEU A 70  ? N LEU A 50  O PHE A 163 ? O PHE A 143 
AA1 4 5 N ILE A 162 ? N ILE A 142 O MET A 192 ? O MET A 172 
AA1 5 6 N ILE A 193 ? N ILE A 173 O SER A 262 ? O SER A 242 
AA1 6 7 O ALA A 261 ? O ALA A 241 N ARG A 241 ? N ARG A 221 
AA2 1 2 N TYR A 114 ? N TYR A 94  O ARG A 126 ? O ARG A 106 
AA3 1 2 N PHE A 213 ? N PHE A 193 O VAL A 220 ? O VAL A 200 
# 
_pdbx_entry_details.entry_id                   9BXK 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
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 ALA A 55  ? ? 52.38   -128.54 
2 1 ALA A 131 ? ? -150.06 73.00   
# 
loop_
_pdbx_validate_planes.id 
_pdbx_validate_planes.PDB_model_num 
_pdbx_validate_planes.auth_comp_id 
_pdbx_validate_planes.auth_asym_id 
_pdbx_validate_planes.auth_seq_id 
_pdbx_validate_planes.PDB_ins_code 
_pdbx_validate_planes.label_alt_id 
_pdbx_validate_planes.rmsd 
_pdbx_validate_planes.type 
1 1 ARG A 78  ? ? 0.225 'SIDE CHAIN' 
2 1 ARG A 121 ? ? 0.238 'SIDE CHAIN' 
3 1 ARG A 207 ? ? 0.152 'SIDE CHAIN' 
# 
_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     622 
_pdbx_struct_special_symmetry.PDB_ins_code    ? 
_pdbx_struct_special_symmetry.label_asym_id   E 
_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+1/2         
4 -x,-y,z+1/2         
5 x+1/2,y+1/2,z       
6 x+1/2,-y+1/2,-z     
7 -x+1/2,y+1/2,-z+1/2 
8 -x+1/2,-y+1/2,z+1/2 
# 
loop_
_pdbx_distant_solvent_atoms.id 
_pdbx_distant_solvent_atoms.PDB_model_num 
_pdbx_distant_solvent_atoms.auth_atom_id 
_pdbx_distant_solvent_atoms.label_alt_id 
_pdbx_distant_solvent_atoms.auth_asym_id 
_pdbx_distant_solvent_atoms.auth_comp_id 
_pdbx_distant_solvent_atoms.auth_seq_id 
_pdbx_distant_solvent_atoms.PDB_ins_code 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance 
1 1 O ? A HOH 681 ? 6.18 . 
2 1 O ? A HOH 682 ? 6.50 . 
# 
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 -19 ? A MET 1  
2  1 Y 1 A GLY -18 ? A GLY 2  
3  1 Y 1 A SER -17 ? A SER 3  
4  1 Y 1 A SER -16 ? A SER 4  
5  1 Y 1 A HIS -15 ? A HIS 5  
6  1 Y 1 A HIS -14 ? A HIS 6  
7  1 Y 1 A HIS -13 ? A HIS 7  
8  1 Y 1 A HIS -12 ? A HIS 8  
9  1 Y 1 A HIS -11 ? A HIS 9  
10 1 Y 1 A HIS -10 ? A HIS 10 
11 1 Y 1 A SER -9  ? A SER 11 
12 1 Y 1 A SER -8  ? A SER 12 
13 1 Y 1 A GLY -7  ? A GLY 13 
14 1 Y 1 A LEU -6  ? A LEU 14 
15 1 Y 1 A VAL -5  ? A VAL 15 
16 1 Y 1 A PRO -4  ? A PRO 16 
17 1 Y 1 A ARG -3  ? A ARG 17 
18 1 Y 1 A GLY -2  ? A GLY 18 
19 1 Y 1 A SER -1  ? A SER 19 
20 1 Y 1 A HIS 0   ? A HIS 20 
21 1 Y 1 A MET 1   ? A MET 21 
22 1 Y 1 A THR 2   ? A THR 22 
# 
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 
A1AS0 N      N  N N 1   
A1AS0 CA     C  N S 2   
A1AS0 C      C  N N 3   
A1AS0 O      O  N N 4   
A1AS0 CB     C  N N 5   
A1AS0 CG     C  Y N 6   
A1AS0 ND1    N  Y N 7   
A1AS0 CD2    C  Y N 8   
A1AS0 CE1    C  Y N 9   
A1AS0 NE2    N  Y N 10  
A1AS0 SE2    SE N N 11  
A1AS0 OXT    O  N N 12  
A1AS0 H      H  N N 13  
A1AS0 H2     H  N N 14  
A1AS0 HA     H  N N 15  
A1AS0 HB2    H  N N 16  
A1AS0 HB3    H  N N 17  
A1AS0 HD1    H  N N 18  
A1AS0 HE1    H  N N 19  
A1AS0 H10    H  N N 20  
A1AS0 HXT    H  N N 21  
ALA   N      N  N N 22  
ALA   CA     C  N S 23  
ALA   C      C  N N 24  
ALA   O      O  N N 25  
ALA   CB     C  N N 26  
ALA   OXT    O  N N 27  
ALA   H      H  N N 28  
ALA   H2     H  N N 29  
ALA   HA     H  N N 30  
ALA   HB1    H  N N 31  
ALA   HB2    H  N N 32  
ALA   HB3    H  N N 33  
ALA   HXT    H  N N 34  
ARG   N      N  N N 35  
ARG   CA     C  N S 36  
ARG   C      C  N N 37  
ARG   O      O  N N 38  
ARG   CB     C  N N 39  
ARG   CG     C  N N 40  
ARG   CD     C  N N 41  
ARG   NE     N  N N 42  
ARG   CZ     C  N N 43  
ARG   NH1    N  N N 44  
ARG   NH2    N  N N 45  
ARG   OXT    O  N N 46  
ARG   H      H  N N 47  
ARG   H2     H  N N 48  
ARG   HA     H  N N 49  
ARG   HB2    H  N N 50  
ARG   HB3    H  N N 51  
ARG   HG2    H  N N 52  
ARG   HG3    H  N N 53  
ARG   HD2    H  N N 54  
ARG   HD3    H  N N 55  
ARG   HE     H  N N 56  
ARG   HH11   H  N N 57  
ARG   HH12   H  N N 58  
ARG   HH21   H  N N 59  
ARG   HH22   H  N N 60  
ARG   HXT    H  N N 61  
ASN   N      N  N N 62  
ASN   CA     C  N S 63  
ASN   C      C  N N 64  
ASN   O      O  N N 65  
ASN   CB     C  N N 66  
ASN   CG     C  N N 67  
ASN   OD1    O  N N 68  
ASN   ND2    N  N N 69  
ASN   OXT    O  N N 70  
ASN   H      H  N N 71  
ASN   H2     H  N N 72  
ASN   HA     H  N N 73  
ASN   HB2    H  N N 74  
ASN   HB3    H  N N 75  
ASN   HD21   H  N N 76  
ASN   HD22   H  N N 77  
ASN   HXT    H  N N 78  
ASP   N      N  N N 79  
ASP   CA     C  N S 80  
ASP   C      C  N N 81  
ASP   O      O  N N 82  
ASP   CB     C  N N 83  
ASP   CG     C  N N 84  
ASP   OD1    O  N N 85  
ASP   OD2    O  N N 86  
ASP   OXT    O  N N 87  
ASP   H      H  N N 88  
ASP   H2     H  N N 89  
ASP   HA     H  N N 90  
ASP   HB2    H  N N 91  
ASP   HB3    H  N N 92  
ASP   HD2    H  N N 93  
ASP   HXT    H  N N 94  
CYS   N      N  N N 95  
CYS   CA     C  N R 96  
CYS   C      C  N N 97  
CYS   O      O  N N 98  
CYS   CB     C  N N 99  
CYS   SG     S  N N 100 
CYS   OXT    O  N N 101 
CYS   H      H  N N 102 
CYS   H2     H  N N 103 
CYS   HA     H  N N 104 
CYS   HB2    H  N N 105 
CYS   HB3    H  N N 106 
CYS   HG     H  N N 107 
CYS   HXT    H  N N 108 
EDO   C1     C  N N 109 
EDO   O1     O  N N 110 
EDO   C2     C  N N 111 
EDO   O2     O  N N 112 
EDO   H11    H  N N 113 
EDO   H12    H  N N 114 
EDO   HO1    H  N N 115 
EDO   H21    H  N N 116 
EDO   H22    H  N N 117 
EDO   HO2    H  N N 118 
GLN   N      N  N N 119 
GLN   CA     C  N S 120 
GLN   C      C  N N 121 
GLN   O      O  N N 122 
GLN   CB     C  N N 123 
GLN   CG     C  N N 124 
GLN   CD     C  N N 125 
GLN   OE1    O  N N 126 
GLN   NE2    N  N N 127 
GLN   OXT    O  N N 128 
GLN   H      H  N N 129 
GLN   H2     H  N N 130 
GLN   HA     H  N N 131 
GLN   HB2    H  N N 132 
GLN   HB3    H  N N 133 
GLN   HG2    H  N N 134 
GLN   HG3    H  N N 135 
GLN   HE21   H  N N 136 
GLN   HE22   H  N N 137 
GLN   HXT    H  N N 138 
GLU   N      N  N N 139 
GLU   CA     C  N S 140 
GLU   C      C  N N 141 
GLU   O      O  N N 142 
GLU   CB     C  N N 143 
GLU   CG     C  N N 144 
GLU   CD     C  N N 145 
GLU   OE1    O  N N 146 
GLU   OE2    O  N N 147 
GLU   OXT    O  N N 148 
GLU   H      H  N N 149 
GLU   H2     H  N N 150 
GLU   HA     H  N N 151 
GLU   HB2    H  N N 152 
GLU   HB3    H  N N 153 
GLU   HG2    H  N N 154 
GLU   HG3    H  N N 155 
GLU   HE2    H  N N 156 
GLU   HXT    H  N N 157 
GLY   N      N  N N 158 
GLY   CA     C  N N 159 
GLY   C      C  N N 160 
GLY   O      O  N N 161 
GLY   OXT    O  N N 162 
GLY   H      H  N N 163 
GLY   H2     H  N N 164 
GLY   HA2    H  N N 165 
GLY   HA3    H  N N 166 
GLY   HXT    H  N N 167 
HIS   N      N  N N 168 
HIS   CA     C  N S 169 
HIS   C      C  N N 170 
HIS   O      O  N N 171 
HIS   CB     C  N N 172 
HIS   CG     C  Y N 173 
HIS   ND1    N  Y N 174 
HIS   CD2    C  Y N 175 
HIS   CE1    C  Y N 176 
HIS   NE2    N  Y N 177 
HIS   OXT    O  N N 178 
HIS   H      H  N N 179 
HIS   H2     H  N N 180 
HIS   HA     H  N N 181 
HIS   HB2    H  N N 182 
HIS   HB3    H  N N 183 
HIS   HD1    H  N N 184 
HIS   HD2    H  N N 185 
HIS   HE1    H  N N 186 
HIS   HE2    H  N N 187 
HIS   HXT    H  N N 188 
HOH   O      O  N N 189 
HOH   H1     H  N N 190 
HOH   H2     H  N N 191 
ILE   N      N  N N 192 
ILE   CA     C  N S 193 
ILE   C      C  N N 194 
ILE   O      O  N N 195 
ILE   CB     C  N S 196 
ILE   CG1    C  N N 197 
ILE   CG2    C  N N 198 
ILE   CD1    C  N N 199 
ILE   OXT    O  N N 200 
ILE   H      H  N N 201 
ILE   H2     H  N N 202 
ILE   HA     H  N N 203 
ILE   HB     H  N N 204 
ILE   HG12   H  N N 205 
ILE   HG13   H  N N 206 
ILE   HG21   H  N N 207 
ILE   HG22   H  N N 208 
ILE   HG23   H  N N 209 
ILE   HD11   H  N N 210 
ILE   HD12   H  N N 211 
ILE   HD13   H  N N 212 
ILE   HXT    H  N N 213 
LEU   N      N  N N 214 
LEU   CA     C  N S 215 
LEU   C      C  N N 216 
LEU   O      O  N N 217 
LEU   CB     C  N N 218 
LEU   CG     C  N N 219 
LEU   CD1    C  N N 220 
LEU   CD2    C  N N 221 
LEU   OXT    O  N N 222 
LEU   H      H  N N 223 
LEU   H2     H  N N 224 
LEU   HA     H  N N 225 
LEU   HB2    H  N N 226 
LEU   HB3    H  N N 227 
LEU   HG     H  N N 228 
LEU   HD11   H  N N 229 
LEU   HD12   H  N N 230 
LEU   HD13   H  N N 231 
LEU   HD21   H  N N 232 
LEU   HD22   H  N N 233 
LEU   HD23   H  N N 234 
LEU   HXT    H  N N 235 
LYS   N      N  N N 236 
LYS   CA     C  N S 237 
LYS   C      C  N N 238 
LYS   O      O  N N 239 
LYS   CB     C  N N 240 
LYS   CG     C  N N 241 
LYS   CD     C  N N 242 
LYS   CE     C  N N 243 
LYS   NZ     N  N N 244 
LYS   OXT    O  N N 245 
LYS   H      H  N N 246 
LYS   H2     H  N N 247 
LYS   HA     H  N N 248 
LYS   HB2    H  N N 249 
LYS   HB3    H  N N 250 
LYS   HG2    H  N N 251 
LYS   HG3    H  N N 252 
LYS   HD2    H  N N 253 
LYS   HD3    H  N N 254 
LYS   HE2    H  N N 255 
LYS   HE3    H  N N 256 
LYS   HZ1    H  N N 257 
LYS   HZ2    H  N N 258 
LYS   HZ3    H  N N 259 
LYS   HXT    H  N N 260 
MET   N      N  N N 261 
MET   CA     C  N S 262 
MET   C      C  N N 263 
MET   O      O  N N 264 
MET   CB     C  N N 265 
MET   CG     C  N N 266 
MET   SD     S  N N 267 
MET   CE     C  N N 268 
MET   OXT    O  N N 269 
MET   H      H  N N 270 
MET   H2     H  N N 271 
MET   HA     H  N N 272 
MET   HB2    H  N N 273 
MET   HB3    H  N N 274 
MET   HG2    H  N N 275 
MET   HG3    H  N N 276 
MET   HE1    H  N N 277 
MET   HE2    H  N N 278 
MET   HE3    H  N N 279 
MET   HXT    H  N N 280 
PHE   N      N  N N 281 
PHE   CA     C  N S 282 
PHE   C      C  N N 283 
PHE   O      O  N N 284 
PHE   CB     C  N N 285 
PHE   CG     C  Y N 286 
PHE   CD1    C  Y N 287 
PHE   CD2    C  Y N 288 
PHE   CE1    C  Y N 289 
PHE   CE2    C  Y N 290 
PHE   CZ     C  Y N 291 
PHE   OXT    O  N N 292 
PHE   H      H  N N 293 
PHE   H2     H  N N 294 
PHE   HA     H  N N 295 
PHE   HB2    H  N N 296 
PHE   HB3    H  N N 297 
PHE   HD1    H  N N 298 
PHE   HD2    H  N N 299 
PHE   HE1    H  N N 300 
PHE   HE2    H  N N 301 
PHE   HZ     H  N N 302 
PHE   HXT    H  N N 303 
PRO   N      N  N N 304 
PRO   CA     C  N S 305 
PRO   C      C  N N 306 
PRO   O      O  N N 307 
PRO   CB     C  N N 308 
PRO   CG     C  N N 309 
PRO   CD     C  N N 310 
PRO   OXT    O  N N 311 
PRO   H      H  N N 312 
PRO   HA     H  N N 313 
PRO   HB2    H  N N 314 
PRO   HB3    H  N N 315 
PRO   HG2    H  N N 316 
PRO   HG3    H  N N 317 
PRO   HD2    H  N N 318 
PRO   HD3    H  N N 319 
PRO   HXT    H  N N 320 
SAH   N      N  N N 321 
SAH   CA     C  N S 322 
SAH   CB     C  N N 323 
SAH   CG     C  N N 324 
SAH   SD     S  N N 325 
SAH   C      C  N N 326 
SAH   O      O  N N 327 
SAH   OXT    O  N N 328 
SAH   "C5'"  C  N N 329 
SAH   "C4'"  C  N S 330 
SAH   "O4'"  O  N N 331 
SAH   "C3'"  C  N S 332 
SAH   "O3'"  O  N N 333 
SAH   "C2'"  C  N R 334 
SAH   "O2'"  O  N N 335 
SAH   "C1'"  C  N R 336 
SAH   N9     N  Y N 337 
SAH   C8     C  Y N 338 
SAH   N7     N  Y N 339 
SAH   C5     C  Y N 340 
SAH   C6     C  Y N 341 
SAH   N6     N  N N 342 
SAH   N1     N  Y N 343 
SAH   C2     C  Y N 344 
SAH   N3     N  Y N 345 
SAH   C4     C  Y N 346 
SAH   HN1    H  N N 347 
SAH   HN2    H  N N 348 
SAH   HA     H  N N 349 
SAH   HB1    H  N N 350 
SAH   HB2    H  N N 351 
SAH   HG1    H  N N 352 
SAH   HG2    H  N N 353 
SAH   HXT    H  N N 354 
SAH   "H5'1" H  N N 355 
SAH   "H5'2" H  N N 356 
SAH   "H4'"  H  N N 357 
SAH   "H3'"  H  N N 358 
SAH   "HO3'" H  N N 359 
SAH   "H2'"  H  N N 360 
SAH   "HO2'" H  N N 361 
SAH   "H1'"  H  N N 362 
SAH   H8     H  N N 363 
SAH   HN61   H  N N 364 
SAH   HN62   H  N N 365 
SAH   H2     H  N N 366 
SER   N      N  N N 367 
SER   CA     C  N S 368 
SER   C      C  N N 369 
SER   O      O  N N 370 
SER   CB     C  N N 371 
SER   OG     O  N N 372 
SER   OXT    O  N N 373 
SER   H      H  N N 374 
SER   H2     H  N N 375 
SER   HA     H  N N 376 
SER   HB2    H  N N 377 
SER   HB3    H  N N 378 
SER   HG     H  N N 379 
SER   HXT    H  N N 380 
THR   N      N  N N 381 
THR   CA     C  N S 382 
THR   C      C  N N 383 
THR   O      O  N N 384 
THR   CB     C  N R 385 
THR   OG1    O  N N 386 
THR   CG2    C  N N 387 
THR   OXT    O  N N 388 
THR   H      H  N N 389 
THR   H2     H  N N 390 
THR   HA     H  N N 391 
THR   HB     H  N N 392 
THR   HG1    H  N N 393 
THR   HG21   H  N N 394 
THR   HG22   H  N N 395 
THR   HG23   H  N N 396 
THR   HXT    H  N N 397 
TRP   N      N  N N 398 
TRP   CA     C  N S 399 
TRP   C      C  N N 400 
TRP   O      O  N N 401 
TRP   CB     C  N N 402 
TRP   CG     C  Y N 403 
TRP   CD1    C  Y N 404 
TRP   CD2    C  Y N 405 
TRP   NE1    N  Y N 406 
TRP   CE2    C  Y N 407 
TRP   CE3    C  Y N 408 
TRP   CZ2    C  Y N 409 
TRP   CZ3    C  Y N 410 
TRP   CH2    C  Y N 411 
TRP   OXT    O  N N 412 
TRP   H      H  N N 413 
TRP   H2     H  N N 414 
TRP   HA     H  N N 415 
TRP   HB2    H  N N 416 
TRP   HB3    H  N N 417 
TRP   HD1    H  N N 418 
TRP   HE1    H  N N 419 
TRP   HE3    H  N N 420 
TRP   HZ2    H  N N 421 
TRP   HZ3    H  N N 422 
TRP   HH2    H  N N 423 
TRP   HXT    H  N N 424 
TYR   N      N  N N 425 
TYR   CA     C  N S 426 
TYR   C      C  N N 427 
TYR   O      O  N N 428 
TYR   CB     C  N N 429 
TYR   CG     C  Y N 430 
TYR   CD1    C  Y N 431 
TYR   CD2    C  Y N 432 
TYR   CE1    C  Y N 433 
TYR   CE2    C  Y N 434 
TYR   CZ     C  Y N 435 
TYR   OH     O  N N 436 
TYR   OXT    O  N N 437 
TYR   H      H  N N 438 
TYR   H2     H  N N 439 
TYR   HA     H  N N 440 
TYR   HB2    H  N N 441 
TYR   HB3    H  N N 442 
TYR   HD1    H  N N 443 
TYR   HD2    H  N N 444 
TYR   HE1    H  N N 445 
TYR   HE2    H  N N 446 
TYR   HH     H  N N 447 
TYR   HXT    H  N N 448 
VAL   N      N  N N 449 
VAL   CA     C  N S 450 
VAL   C      C  N N 451 
VAL   O      O  N N 452 
VAL   CB     C  N N 453 
VAL   CG1    C  N N 454 
VAL   CG2    C  N N 455 
VAL   OXT    O  N N 456 
VAL   H      H  N N 457 
VAL   H2     H  N N 458 
VAL   HA     H  N N 459 
VAL   HB     H  N N 460 
VAL   HG11   H  N N 461 
VAL   HG12   H  N N 462 
VAL   HG13   H  N N 463 
VAL   HG21   H  N N 464 
VAL   HG22   H  N N 465 
VAL   HG23   H  N N 466 
VAL   HXT    H  N N 467 
# 
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 
A1AS0 N     CA     sing N N 1   
A1AS0 CA    C      sing N N 2   
A1AS0 CA    CB     sing N N 3   
A1AS0 O     C      doub N N 4   
A1AS0 C     OXT    sing N N 5   
A1AS0 CB    CG     sing N N 6   
A1AS0 CG    ND1    sing Y N 7   
A1AS0 CG    CD2    doub Y N 8   
A1AS0 SE2   CD2    sing N N 9   
A1AS0 ND1   CE1    sing Y N 10  
A1AS0 CD2   NE2    sing Y N 11  
A1AS0 CE1   NE2    doub Y N 12  
A1AS0 N     H      sing N N 13  
A1AS0 N     H2     sing N N 14  
A1AS0 CA    HA     sing N N 15  
A1AS0 CB    HB2    sing N N 16  
A1AS0 CB    HB3    sing N N 17  
A1AS0 ND1   HD1    sing N N 18  
A1AS0 CE1   HE1    sing N N 19  
A1AS0 SE2   H10    sing N N 20  
A1AS0 OXT   HXT    sing N N 21  
ALA   N     CA     sing N N 22  
ALA   N     H      sing N N 23  
ALA   N     H2     sing N N 24  
ALA   CA    C      sing N N 25  
ALA   CA    CB     sing N N 26  
ALA   CA    HA     sing N N 27  
ALA   C     O      doub N N 28  
ALA   C     OXT    sing N N 29  
ALA   CB    HB1    sing N N 30  
ALA   CB    HB2    sing N N 31  
ALA   CB    HB3    sing N N 32  
ALA   OXT   HXT    sing N N 33  
ARG   N     CA     sing N N 34  
ARG   N     H      sing N N 35  
ARG   N     H2     sing N N 36  
ARG   CA    C      sing N N 37  
ARG   CA    CB     sing N N 38  
ARG   CA    HA     sing N N 39  
ARG   C     O      doub N N 40  
ARG   C     OXT    sing N N 41  
ARG   CB    CG     sing N N 42  
ARG   CB    HB2    sing N N 43  
ARG   CB    HB3    sing N N 44  
ARG   CG    CD     sing N N 45  
ARG   CG    HG2    sing N N 46  
ARG   CG    HG3    sing N N 47  
ARG   CD    NE     sing N N 48  
ARG   CD    HD2    sing N N 49  
ARG   CD    HD3    sing N N 50  
ARG   NE    CZ     sing N N 51  
ARG   NE    HE     sing N N 52  
ARG   CZ    NH1    sing N N 53  
ARG   CZ    NH2    doub N N 54  
ARG   NH1   HH11   sing N N 55  
ARG   NH1   HH12   sing N N 56  
ARG   NH2   HH21   sing N N 57  
ARG   NH2   HH22   sing N N 58  
ARG   OXT   HXT    sing N N 59  
ASN   N     CA     sing N N 60  
ASN   N     H      sing N N 61  
ASN   N     H2     sing N N 62  
ASN   CA    C      sing N N 63  
ASN   CA    CB     sing N N 64  
ASN   CA    HA     sing N N 65  
ASN   C     O      doub N N 66  
ASN   C     OXT    sing N N 67  
ASN   CB    CG     sing N N 68  
ASN   CB    HB2    sing N N 69  
ASN   CB    HB3    sing N N 70  
ASN   CG    OD1    doub N N 71  
ASN   CG    ND2    sing N N 72  
ASN   ND2   HD21   sing N N 73  
ASN   ND2   HD22   sing N N 74  
ASN   OXT   HXT    sing N N 75  
ASP   N     CA     sing N N 76  
ASP   N     H      sing N N 77  
ASP   N     H2     sing N N 78  
ASP   CA    C      sing N N 79  
ASP   CA    CB     sing N N 80  
ASP   CA    HA     sing N N 81  
ASP   C     O      doub N N 82  
ASP   C     OXT    sing N N 83  
ASP   CB    CG     sing N N 84  
ASP   CB    HB2    sing N N 85  
ASP   CB    HB3    sing N N 86  
ASP   CG    OD1    doub N N 87  
ASP   CG    OD2    sing N N 88  
ASP   OD2   HD2    sing N N 89  
ASP   OXT   HXT    sing N N 90  
CYS   N     CA     sing N N 91  
CYS   N     H      sing N N 92  
CYS   N     H2     sing N N 93  
CYS   CA    C      sing N N 94  
CYS   CA    CB     sing N N 95  
CYS   CA    HA     sing N N 96  
CYS   C     O      doub N N 97  
CYS   C     OXT    sing N N 98  
CYS   CB    SG     sing N N 99  
CYS   CB    HB2    sing N N 100 
CYS   CB    HB3    sing N N 101 
CYS   SG    HG     sing N N 102 
CYS   OXT   HXT    sing N N 103 
EDO   C1    O1     sing N N 104 
EDO   C1    C2     sing N N 105 
EDO   C1    H11    sing N N 106 
EDO   C1    H12    sing N N 107 
EDO   O1    HO1    sing N N 108 
EDO   C2    O2     sing N N 109 
EDO   C2    H21    sing N N 110 
EDO   C2    H22    sing N N 111 
EDO   O2    HO2    sing N N 112 
GLN   N     CA     sing N N 113 
GLN   N     H      sing N N 114 
GLN   N     H2     sing N N 115 
GLN   CA    C      sing N N 116 
GLN   CA    CB     sing N N 117 
GLN   CA    HA     sing N N 118 
GLN   C     O      doub N N 119 
GLN   C     OXT    sing N N 120 
GLN   CB    CG     sing N N 121 
GLN   CB    HB2    sing N N 122 
GLN   CB    HB3    sing N N 123 
GLN   CG    CD     sing N N 124 
GLN   CG    HG2    sing N N 125 
GLN   CG    HG3    sing N N 126 
GLN   CD    OE1    doub N N 127 
GLN   CD    NE2    sing N N 128 
GLN   NE2   HE21   sing N N 129 
GLN   NE2   HE22   sing N N 130 
GLN   OXT   HXT    sing N N 131 
GLU   N     CA     sing N N 132 
GLU   N     H      sing N N 133 
GLU   N     H2     sing N N 134 
GLU   CA    C      sing N N 135 
GLU   CA    CB     sing N N 136 
GLU   CA    HA     sing N N 137 
GLU   C     O      doub N N 138 
GLU   C     OXT    sing N N 139 
GLU   CB    CG     sing N N 140 
GLU   CB    HB2    sing N N 141 
GLU   CB    HB3    sing N N 142 
GLU   CG    CD     sing N N 143 
GLU   CG    HG2    sing N N 144 
GLU   CG    HG3    sing N N 145 
GLU   CD    OE1    doub N N 146 
GLU   CD    OE2    sing N N 147 
GLU   OE2   HE2    sing N N 148 
GLU   OXT   HXT    sing N N 149 
GLY   N     CA     sing N N 150 
GLY   N     H      sing N N 151 
GLY   N     H2     sing N N 152 
GLY   CA    C      sing N N 153 
GLY   CA    HA2    sing N N 154 
GLY   CA    HA3    sing N N 155 
GLY   C     O      doub N N 156 
GLY   C     OXT    sing N N 157 
GLY   OXT   HXT    sing N N 158 
HIS   N     CA     sing N N 159 
HIS   N     H      sing N N 160 
HIS   N     H2     sing N N 161 
HIS   CA    C      sing N N 162 
HIS   CA    CB     sing N N 163 
HIS   CA    HA     sing N N 164 
HIS   C     O      doub N N 165 
HIS   C     OXT    sing N N 166 
HIS   CB    CG     sing N N 167 
HIS   CB    HB2    sing N N 168 
HIS   CB    HB3    sing N N 169 
HIS   CG    ND1    sing Y N 170 
HIS   CG    CD2    doub Y N 171 
HIS   ND1   CE1    doub Y N 172 
HIS   ND1   HD1    sing N N 173 
HIS   CD2   NE2    sing Y N 174 
HIS   CD2   HD2    sing N N 175 
HIS   CE1   NE2    sing Y N 176 
HIS   CE1   HE1    sing N N 177 
HIS   NE2   HE2    sing N N 178 
HIS   OXT   HXT    sing N N 179 
HOH   O     H1     sing N N 180 
HOH   O     H2     sing N N 181 
ILE   N     CA     sing N N 182 
ILE   N     H      sing N N 183 
ILE   N     H2     sing N N 184 
ILE   CA    C      sing N N 185 
ILE   CA    CB     sing N N 186 
ILE   CA    HA     sing N N 187 
ILE   C     O      doub N N 188 
ILE   C     OXT    sing N N 189 
ILE   CB    CG1    sing N N 190 
ILE   CB    CG2    sing N N 191 
ILE   CB    HB     sing N N 192 
ILE   CG1   CD1    sing N N 193 
ILE   CG1   HG12   sing N N 194 
ILE   CG1   HG13   sing N N 195 
ILE   CG2   HG21   sing N N 196 
ILE   CG2   HG22   sing N N 197 
ILE   CG2   HG23   sing N N 198 
ILE   CD1   HD11   sing N N 199 
ILE   CD1   HD12   sing N N 200 
ILE   CD1   HD13   sing N N 201 
ILE   OXT   HXT    sing N N 202 
LEU   N     CA     sing N N 203 
LEU   N     H      sing N N 204 
LEU   N     H2     sing N N 205 
LEU   CA    C      sing N N 206 
LEU   CA    CB     sing N N 207 
LEU   CA    HA     sing N N 208 
LEU   C     O      doub N N 209 
LEU   C     OXT    sing N N 210 
LEU   CB    CG     sing N N 211 
LEU   CB    HB2    sing N N 212 
LEU   CB    HB3    sing N N 213 
LEU   CG    CD1    sing N N 214 
LEU   CG    CD2    sing N N 215 
LEU   CG    HG     sing N N 216 
LEU   CD1   HD11   sing N N 217 
LEU   CD1   HD12   sing N N 218 
LEU   CD1   HD13   sing N N 219 
LEU   CD2   HD21   sing N N 220 
LEU   CD2   HD22   sing N N 221 
LEU   CD2   HD23   sing N N 222 
LEU   OXT   HXT    sing N N 223 
LYS   N     CA     sing N N 224 
LYS   N     H      sing N N 225 
LYS   N     H2     sing N N 226 
LYS   CA    C      sing N N 227 
LYS   CA    CB     sing N N 228 
LYS   CA    HA     sing N N 229 
LYS   C     O      doub N N 230 
LYS   C     OXT    sing N N 231 
LYS   CB    CG     sing N N 232 
LYS   CB    HB2    sing N N 233 
LYS   CB    HB3    sing N N 234 
LYS   CG    CD     sing N N 235 
LYS   CG    HG2    sing N N 236 
LYS   CG    HG3    sing N N 237 
LYS   CD    CE     sing N N 238 
LYS   CD    HD2    sing N N 239 
LYS   CD    HD3    sing N N 240 
LYS   CE    NZ     sing N N 241 
LYS   CE    HE2    sing N N 242 
LYS   CE    HE3    sing N N 243 
LYS   NZ    HZ1    sing N N 244 
LYS   NZ    HZ2    sing N N 245 
LYS   NZ    HZ3    sing N N 246 
LYS   OXT   HXT    sing N N 247 
MET   N     CA     sing N N 248 
MET   N     H      sing N N 249 
MET   N     H2     sing N N 250 
MET   CA    C      sing N N 251 
MET   CA    CB     sing N N 252 
MET   CA    HA     sing N N 253 
MET   C     O      doub N N 254 
MET   C     OXT    sing N N 255 
MET   CB    CG     sing N N 256 
MET   CB    HB2    sing N N 257 
MET   CB    HB3    sing N N 258 
MET   CG    SD     sing N N 259 
MET   CG    HG2    sing N N 260 
MET   CG    HG3    sing N N 261 
MET   SD    CE     sing N N 262 
MET   CE    HE1    sing N N 263 
MET   CE    HE2    sing N N 264 
MET   CE    HE3    sing N N 265 
MET   OXT   HXT    sing N N 266 
PHE   N     CA     sing N N 267 
PHE   N     H      sing N N 268 
PHE   N     H2     sing N N 269 
PHE   CA    C      sing N N 270 
PHE   CA    CB     sing N N 271 
PHE   CA    HA     sing N N 272 
PHE   C     O      doub N N 273 
PHE   C     OXT    sing N N 274 
PHE   CB    CG     sing N N 275 
PHE   CB    HB2    sing N N 276 
PHE   CB    HB3    sing N N 277 
PHE   CG    CD1    doub Y N 278 
PHE   CG    CD2    sing Y N 279 
PHE   CD1   CE1    sing Y N 280 
PHE   CD1   HD1    sing N N 281 
PHE   CD2   CE2    doub Y N 282 
PHE   CD2   HD2    sing N N 283 
PHE   CE1   CZ     doub Y N 284 
PHE   CE1   HE1    sing N N 285 
PHE   CE2   CZ     sing Y N 286 
PHE   CE2   HE2    sing N N 287 
PHE   CZ    HZ     sing N N 288 
PHE   OXT   HXT    sing N N 289 
PRO   N     CA     sing N N 290 
PRO   N     CD     sing N N 291 
PRO   N     H      sing N N 292 
PRO   CA    C      sing N N 293 
PRO   CA    CB     sing N N 294 
PRO   CA    HA     sing N N 295 
PRO   C     O      doub N N 296 
PRO   C     OXT    sing N N 297 
PRO   CB    CG     sing N N 298 
PRO   CB    HB2    sing N N 299 
PRO   CB    HB3    sing N N 300 
PRO   CG    CD     sing N N 301 
PRO   CG    HG2    sing N N 302 
PRO   CG    HG3    sing N N 303 
PRO   CD    HD2    sing N N 304 
PRO   CD    HD3    sing N N 305 
PRO   OXT   HXT    sing N N 306 
SAH   N     CA     sing N N 307 
SAH   N     HN1    sing N N 308 
SAH   N     HN2    sing N N 309 
SAH   CA    CB     sing N N 310 
SAH   CA    C      sing N N 311 
SAH   CA    HA     sing N N 312 
SAH   CB    CG     sing N N 313 
SAH   CB    HB1    sing N N 314 
SAH   CB    HB2    sing N N 315 
SAH   CG    SD     sing N N 316 
SAH   CG    HG1    sing N N 317 
SAH   CG    HG2    sing N N 318 
SAH   SD    "C5'"  sing N N 319 
SAH   C     O      doub N N 320 
SAH   C     OXT    sing N N 321 
SAH   OXT   HXT    sing N N 322 
SAH   "C5'" "C4'"  sing N N 323 
SAH   "C5'" "H5'1" sing N N 324 
SAH   "C5'" "H5'2" sing N N 325 
SAH   "C4'" "O4'"  sing N N 326 
SAH   "C4'" "C3'"  sing N N 327 
SAH   "C4'" "H4'"  sing N N 328 
SAH   "O4'" "C1'"  sing N N 329 
SAH   "C3'" "O3'"  sing N N 330 
SAH   "C3'" "C2'"  sing N N 331 
SAH   "C3'" "H3'"  sing N N 332 
SAH   "O3'" "HO3'" sing N N 333 
SAH   "C2'" "O2'"  sing N N 334 
SAH   "C2'" "C1'"  sing N N 335 
SAH   "C2'" "H2'"  sing N N 336 
SAH   "O2'" "HO2'" sing N N 337 
SAH   "C1'" N9     sing N N 338 
SAH   "C1'" "H1'"  sing N N 339 
SAH   N9    C8     sing Y N 340 
SAH   N9    C4     sing Y N 341 
SAH   C8    N7     doub Y N 342 
SAH   C8    H8     sing N N 343 
SAH   N7    C5     sing Y N 344 
SAH   C5    C6     sing Y N 345 
SAH   C5    C4     doub Y N 346 
SAH   C6    N6     sing N N 347 
SAH   C6    N1     doub Y N 348 
SAH   N6    HN61   sing N N 349 
SAH   N6    HN62   sing N N 350 
SAH   N1    C2     sing Y N 351 
SAH   C2    N3     doub Y N 352 
SAH   C2    H2     sing N N 353 
SAH   N3    C4     sing Y N 354 
SER   N     CA     sing N N 355 
SER   N     H      sing N N 356 
SER   N     H2     sing N N 357 
SER   CA    C      sing N N 358 
SER   CA    CB     sing N N 359 
SER   CA    HA     sing N N 360 
SER   C     O      doub N N 361 
SER   C     OXT    sing N N 362 
SER   CB    OG     sing N N 363 
SER   CB    HB2    sing N N 364 
SER   CB    HB3    sing N N 365 
SER   OG    HG     sing N N 366 
SER   OXT   HXT    sing N N 367 
THR   N     CA     sing N N 368 
THR   N     H      sing N N 369 
THR   N     H2     sing N N 370 
THR   CA    C      sing N N 371 
THR   CA    CB     sing N N 372 
THR   CA    HA     sing N N 373 
THR   C     O      doub N N 374 
THR   C     OXT    sing N N 375 
THR   CB    OG1    sing N N 376 
THR   CB    CG2    sing N N 377 
THR   CB    HB     sing N N 378 
THR   OG1   HG1    sing N N 379 
THR   CG2   HG21   sing N N 380 
THR   CG2   HG22   sing N N 381 
THR   CG2   HG23   sing N N 382 
THR   OXT   HXT    sing N N 383 
TRP   N     CA     sing N N 384 
TRP   N     H      sing N N 385 
TRP   N     H2     sing N N 386 
TRP   CA    C      sing N N 387 
TRP   CA    CB     sing N N 388 
TRP   CA    HA     sing N N 389 
TRP   C     O      doub N N 390 
TRP   C     OXT    sing N N 391 
TRP   CB    CG     sing N N 392 
TRP   CB    HB2    sing N N 393 
TRP   CB    HB3    sing N N 394 
TRP   CG    CD1    doub Y N 395 
TRP   CG    CD2    sing Y N 396 
TRP   CD1   NE1    sing Y N 397 
TRP   CD1   HD1    sing N N 398 
TRP   CD2   CE2    doub Y N 399 
TRP   CD2   CE3    sing Y N 400 
TRP   NE1   CE2    sing Y N 401 
TRP   NE1   HE1    sing N N 402 
TRP   CE2   CZ2    sing Y N 403 
TRP   CE3   CZ3    doub Y N 404 
TRP   CE3   HE3    sing N N 405 
TRP   CZ2   CH2    doub Y N 406 
TRP   CZ2   HZ2    sing N N 407 
TRP   CZ3   CH2    sing Y N 408 
TRP   CZ3   HZ3    sing N N 409 
TRP   CH2   HH2    sing N N 410 
TRP   OXT   HXT    sing N N 411 
TYR   N     CA     sing N N 412 
TYR   N     H      sing N N 413 
TYR   N     H2     sing N N 414 
TYR   CA    C      sing N N 415 
TYR   CA    CB     sing N N 416 
TYR   CA    HA     sing N N 417 
TYR   C     O      doub N N 418 
TYR   C     OXT    sing N N 419 
TYR   CB    CG     sing N N 420 
TYR   CB    HB2    sing N N 421 
TYR   CB    HB3    sing N N 422 
TYR   CG    CD1    doub Y N 423 
TYR   CG    CD2    sing Y N 424 
TYR   CD1   CE1    sing Y N 425 
TYR   CD1   HD1    sing N N 426 
TYR   CD2   CE2    doub Y N 427 
TYR   CD2   HD2    sing N N 428 
TYR   CE1   CZ     doub Y N 429 
TYR   CE1   HE1    sing N N 430 
TYR   CE2   CZ     sing Y N 431 
TYR   CE2   HE2    sing N N 432 
TYR   CZ    OH     sing N N 433 
TYR   OH    HH     sing N N 434 
TYR   OXT   HXT    sing N N 435 
VAL   N     CA     sing N N 436 
VAL   N     H      sing N N 437 
VAL   N     H2     sing N N 438 
VAL   CA    C      sing N N 439 
VAL   CA    CB     sing N N 440 
VAL   CA    HA     sing N N 441 
VAL   C     O      doub N N 442 
VAL   C     OXT    sing N N 443 
VAL   CB    CG1    sing N N 444 
VAL   CB    CG2    sing N N 445 
VAL   CB    HB     sing N N 446 
VAL   CG1   HG11   sing N N 447 
VAL   CG1   HG12   sing N N 448 
VAL   CG1   HG13   sing N N 449 
VAL   CG2   HG21   sing N N 450 
VAL   CG2   HG22   sing N N 451 
VAL   CG2   HG23   sing N N 452 
VAL   OXT   HXT    sing N N 453 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'National Science Foundation (NSF, United States)'                                         'United States' 1937971  1 
'National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)' 'United States' GM147557 2 
# 
_space_group.name_H-M_alt     'C 2 2 21' 
_space_group.name_Hall        'C 2c 2' 
_space_group.IT_number        20 
_space_group.crystal_system   orthorhombic 
_space_group.id               1 
# 
_atom_sites.entry_id                    9BXK 
_atom_sites.Cartn_transf_matrix[1][1]   ? 
_atom_sites.Cartn_transf_matrix[1][2]   ? 
_atom_sites.Cartn_transf_matrix[1][3]   ? 
_atom_sites.Cartn_transf_matrix[2][1]   ? 
_atom_sites.Cartn_transf_matrix[2][2]   ? 
_atom_sites.Cartn_transf_matrix[2][3]   ? 
_atom_sites.Cartn_transf_matrix[3][1]   ? 
_atom_sites.Cartn_transf_matrix[3][2]   ? 
_atom_sites.Cartn_transf_matrix[3][3]   ? 
_atom_sites.Cartn_transf_vector[1]      ? 
_atom_sites.Cartn_transf_vector[2]      ? 
_atom_sites.Cartn_transf_vector[3]      ? 
_atom_sites.Cartn_transform_axes        ? 
_atom_sites.fract_transf_matrix[1][1]   0.011928 
_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]   0.011104 
_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]   0.012450 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
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.
;
? 
O1- ? ? 5.12366  3.84317 ? ? 3.49406  27.47979 ? ? 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.
;
? 
SE  ? ? 26.02326 7.89457 ? ? 1.54240  29.12501 ? ? 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     . ASP   A 1 23  ? -34.52700 -11.61300 -0.22600  1.000 51.57093 ?  3   ASP   A N     1 
ATOM   2    C  CA    . ASP   A 1 23  ? -34.26900 -10.63900 0.86100   1.000 46.89278 ?  3   ASP   A CA    1 
ATOM   3    C  C     . ASP   A 1 23  ? -32.80300 -10.73900 1.28900   1.000 44.71567 ?  3   ASP   A C     1 
ATOM   4    O  O     . ASP   A 1 23  ? -32.25200 -9.71200  1.68400   1.000 43.54635 ?  3   ASP   A O     1 
ATOM   5    C  CB    . ASP   A 1 23  ? -35.21800 -10.88000 2.03500   1.000 50.01108 ?  3   ASP   A CB    1 
ATOM   6    N  N     . ASN   A 1 24  ? -32.20900 -11.93300 1.21200   1.000 38.43083 ?  4   ASN   A N     1 
ATOM   7    C  CA    . ASN   A 1 24  ? -30.81700 -12.14300 1.69000   1.000 29.31393 ?  4   ASN   A CA    1 
ATOM   8    C  C     . ASN   A 1 24  ? -29.81000 -11.75200 0.61400   1.000 31.14035 ?  4   ASN   A C     1 
ATOM   9    O  O     . ASN   A 1 24  ? -29.71500 -12.44900 -0.39000  1.000 26.25603 ?  4   ASN   A O     1 
ATOM   10   C  CB    . ASN   A 1 24  ? -30.57700 -13.58600 2.13100   1.000 27.06689 ?  4   ASN   A CB    1 
ATOM   11   C  CG    . ASN   A 1 24  ? -29.25400 -13.78800 2.83700   1.000 28.29405 ?  4   ASN   A CG    1 
ATOM   12   O  OD1   . ASN   A 1 24  ? -28.49500 -12.84400 3.03300   1.000 25.89698 ?  4   ASN   A OD1   1 
ATOM   13   N  ND2   . ASN   A 1 24  ? -28.97200 -15.01900 3.22900   1.000 27.39619 ?  4   ASN   A ND2   1 
ATOM   14   N  N     . PRO   A 1 25  ? -29.01100 -10.69200 0.84100   1.000 23.22095 ?  5   PRO   A N     1 
ATOM   15   C  CA    . PRO   A 1 25  ? -28.00100 -10.27000 -0.11200  1.000 21.45795 ?  5   PRO   A CA    1 
ATOM   16   C  C     . PRO   A 1 25  ? -26.99400 -11.39000 -0.39500  1.000 23.65459 ?  5   PRO   A C     1 
ATOM   17   O  O     . PRO   A 1 25  ? -26.48100 -11.43900 -1.47000  1.000 23.83953 ?  5   PRO   A O     1 
ATOM   18   C  CB    . PRO   A 1 25  ? -27.29300 -9.12200  0.63200   1.000 26.12083 ?  5   PRO   A CB    1 
ATOM   19   C  CG    . PRO   A 1 25  ? -27.65800 -9.29100  2.08000   1.000 27.36107 ?  5   PRO   A CG    1 
ATOM   20   C  CD    . PRO   A 1 25  ? -29.06100 -9.84300  2.03100   1.000 30.02826 ?  5   PRO   A CD    1 
ATOM   21   N  N     . TYR   A 1 26  ? -26.77800 -12.26000 0.58400   1.000 20.37905 ?  6   TYR   A N     1 
ATOM   22   C  CA    . TYR   A 1 26  ? -25.75000 -13.32800 0.45800   1.000 18.34623 ?  6   TYR   A CA    1 
ATOM   23   C  C     . TYR   A 1 26  ? -26.24400 -14.46600 -0.45600  1.000 20.25731 ?  6   TYR   A C     1 
ATOM   24   O  O     . TYR   A 1 26  ? -25.48400 -15.37600 -0.70200  1.000 20.76382 ?  6   TYR   A O     1 
ATOM   25   C  CB    . TYR   A 1 26  ? -25.30800 -13.74100 1.86900   1.000 17.60150 ?  6   TYR   A CB    1 
ATOM   26   C  CG    . TYR   A 1 26  ? -24.56600 -12.67800 2.64000   1.000 20.47104 ?  6   TYR   A CG    1 
ATOM   27   C  CD1   . TYR   A 1 26  ? -23.30100 -12.26900 2.25800   1.000 20.48228 ?  6   TYR   A CD1   1 
ATOM   28   C  CD2   . TYR   A 1 26  ? -25.11900 -12.09100 3.76400   1.000 18.70421 ?  6   TYR   A CD2   1 
ATOM   29   C  CE1   . TYR   A 1 26  ? -22.60600 -11.30700 2.97000   1.000 17.87999 ?  6   TYR   A CE1   1 
ATOM   30   C  CE2   . TYR   A 1 26  ? -24.43800 -11.12900 4.48900   1.000 21.04986 ?  6   TYR   A CE2   1 
ATOM   31   C  CZ    . TYR   A 1 26  ? -23.17500 -10.73400 4.09200   1.000 21.26310 ?  6   TYR   A CZ    1 
ATOM   32   O  OH    . TYR   A 1 26  ? -22.49800 -9.78000  4.80600   1.000 20.26512 ?  6   TYR   A OH    1 
ATOM   33   N  N     . GLU   A 1 27  ? -27.48100 -14.38400 -0.94400  1.000 21.67026 ?  7   GLU   A N     1 
ATOM   34   C  CA    . GLU   A 1 27  ? -28.00200 -15.37600 -1.92500  1.000 21.10573 ?  7   GLU   A CA    1 
ATOM   35   C  C     . GLU   A 1 27  ? -27.99000 -14.79900 -3.34900  1.000 25.38130 ?  7   GLU   A C     1 
ATOM   36   O  O     . GLU   A 1 27  ? -28.48900 -15.48100 -4.23600  1.000 26.46547 ?  7   GLU   A O     1 
ATOM   37   C  CB    . GLU   A 1 27  ? -29.41500 -15.80900 -1.53100  1.000 25.01492 ?  7   GLU   A CB    1 
ATOM   38   C  CG    . GLU   A 1 27  ? -29.48600 -16.50600 -0.18800  1.000 22.98547 ?  7   GLU   A CG    1 
ATOM   39   C  CD    . GLU   A 1 27  ? -29.34600 -18.01800 -0.23300  1.000 28.30545 ?  7   GLU   A CD    1 
ATOM   40   O  OE1   . GLU   A 1 27  ? -28.86200 -18.53300 -1.25100  1.000 25.96958 ?  7   GLU   A OE1   1 
ATOM   41   O  OE2   . GLU   A 1 27  ? -29.71500 -18.66800 0.75500   1.000 25.42732 -1 7   GLU   A OE2   1 
ATOM   42   N  N     . THR   A 1 28  ? -27.40800 -13.61900 -3.54700  1.000 24.90675 ?  8   THR   A N     1 
ATOM   43   C  CA    . THR   A 1 28  ? -27.39800 -12.94000 -4.87200  1.000 24.08562 ?  8   THR   A CA    1 
ATOM   44   C  C     . THR   A 1 28  ? -26.13800 -13.25800 -5.69200  1.000 30.28451 ?  8   THR   A C     1 
ATOM   45   O  O     . THR   A 1 28  ? -25.13000 -13.64000 -5.11200  1.000 22.25559 ?  8   THR   A O     1 
ATOM   46   C  CB    . THR   A 1 28  ? -27.53800 -11.42100 -4.71100  1.000 22.72486 ?  8   THR   A CB    1 
ATOM   47   O  OG1   . THR   A 1 28  ? -26.37800 -10.90800 -4.06000  1.000 24.98635 ?  8   THR   A OG1   1 
ATOM   48   C  CG2   . THR   A 1 28  ? -28.78800 -11.03500 -3.95200  1.000 26.58325 ?  8   THR   A CG2   1 
ATOM   49   N  N     . ASP   A 1 29  ? -26.22900 -13.09500 -7.01700  1.000 27.82838 ?  9   ASP   A N     1 
ATOM   50   C  CA    . ASP   A 1 29  ? -25.06300 -13.30900 -7.90900  1.000 23.70908 ?  9   ASP   A CA    1 
ATOM   51   C  C     . ASP   A 1 29  ? -24.02900 -12.22700 -7.64300  1.000 25.39107 ?  9   ASP   A C     1 
ATOM   52   O  O     . ASP   A 1 29  ? -22.84200 -12.49100 -7.78600  1.000 27.98583 ?  9   ASP   A O     1 
ATOM   53   C  CB    . ASP   A 1 29  ? -25.49800 -13.24400 -9.37400  1.000 30.42371 ?  9   ASP   A CB    1 
ATOM   54   C  CG    . ASP   A 1 29  ? -26.06800 -14.55600 -9.87900  1.000 39.20816 ?  9   ASP   A CG    1 
ATOM   55   O  OD1   . ASP   A 1 29  ? -25.75200 -15.59500 -9.27700  1.000 46.63728 ?  9   ASP   A OD1   1 
ATOM   56   O  OD2   . ASP   A 1 29  ? -26.81200 -14.52500 -10.86900 1.000 46.39628 -1 9   ASP   A OD2   1 
ATOM   57   N  N     . GLU   A 1 30  ? -24.50700 -11.03700 -7.31200  1.000 21.81755 ?  10  GLU   A N     1 
ATOM   58   C  CA    . GLU   A 1 30  ? -23.60300 -9.91500  -7.00300  1.000 30.39651 ?  10  GLU   A CA    1 
ATOM   59   C  C     . GLU   A 1 30  ? -22.68400 -10.37300 -5.86600  1.000 28.86792 ?  10  GLU   A C     1 
ATOM   60   O  O     . GLU   A 1 30  ? -21.46900 -10.26300 -6.01200  1.000 23.83721 ?  10  GLU   A O     1 
ATOM   61   C  CB    . GLU   A 1 30  ? -24.44200 -8.68800  -6.64800  1.000 27.70950 ?  10  GLU   A CB    1 
ATOM   62   C  CG    . GLU   A 1 30  ? -23.62800 -7.45900  -6.31300  1.000 34.76744 ?  10  GLU   A CG    1 
ATOM   63   C  CD    . GLU   A 1 30  ? -24.46700 -6.25600  -5.91700  1.000 45.78758 ?  10  GLU   A CD    1 
ATOM   64   O  OE1   . GLU   A 1 30  ? -25.66800 -6.43500  -5.65200  1.000 43.19619 ?  10  GLU   A OE1   1 
ATOM   65   O  OE2   . GLU   A 1 30  ? -23.91600 -5.14600  -5.86900  1.000 42.17240 -1 10  GLU   A OE2   1 
ATOM   66   N  N     . LEU   A 1 31  ? -23.27600 -10.87300 -4.78000  1.000 24.66526 ?  11  LEU   A N     1 
ATOM   67   C  CA    . LEU   A 1 31  ? -22.43500 -11.27400 -3.65800  1.000 22.29946 ?  11  LEU   A CA    1 
ATOM   68   C  C     . LEU   A 1 31  ? -21.61700 -12.52000 -3.98300  1.000 23.10068 ?  11  LEU   A C     1 
ATOM   69   O  O     . LEU   A 1 31  ? -20.48700 -12.66000 -3.49700  1.000 23.33772 ?  11  LEU   A O     1 
ATOM   70   C  CB    . LEU   A 1 31  ? -23.30400 -11.49600 -2.40500  1.000 19.93866 ?  11  LEU   A CB    1 
ATOM   71   C  CG    . LEU   A 1 31  ? -23.35800 -10.28700 -1.46000  1.000 24.44685 ?  11  LEU   A CG    1 
ATOM   72   C  CD1   . LEU   A 1 31  ? -21.99700 -9.93900  -0.82300  1.000 21.63457 ?  11  LEU   A CD1   1 
ATOM   73   C  CD2   . LEU   A 1 31  ? -23.90300 -9.08900  -2.24200  1.000 29.27818 ?  11  LEU   A CD2   1 
ATOM   74   N  N     . LEU   A 1 32  ? -22.15200 -13.44000 -4.79500  1.000 24.20574 ?  12  LEU   A N     1 
ATOM   75   C  CA    . LEU   A 1 32  ? -21.38700 -14.64400 -5.11500  1.000 20.45982 ?  12  LEU   A CA    1 
ATOM   76   C  C     . LEU   A 1 32  ? -20.10100 -14.29700 -5.82800  1.000 27.31363 ?  12  LEU   A C     1 
ATOM   77   O  O     . LEU   A 1 32  ? -19.04700 -14.86200 -5.51800  1.000 23.14840 ?  12  LEU   A O     1 
ATOM   78   C  CB    . LEU   A 1 32  ? -22.20900 -15.60700 -5.96400  1.000 25.47704 ?  12  LEU   A CB    1 
ATOM   79   C  CG    . LEU   A 1 32  ? -21.52000 -16.96800 -6.17200  1.000 26.35687 ?  12  LEU   A CG    1 
ATOM   80   C  CD1   . LEU   A 1 32  ? -21.23700 -17.71500 -4.84000  1.000 23.67413 ?  12  LEU   A CD1   1 
ATOM   81   C  CD2   . LEU   A 1 32  ? -22.33600 -17.80900 -7.10500  1.000 29.19319 ?  12  LEU   A CD2   1 
ATOM   82   N  N     . GLY   A 1 33  ? -20.16500 -13.37000 -6.79300  1.000 30.10942 ?  13  GLY   A N     1 
ATOM   83   C  CA    . GLY   A 1 33  ? -18.97100 -12.99600 -7.52700  1.000 24.49655 ?  13  GLY   A CA    1 
ATOM   84   C  C     . GLY   A 1 33  ? -17.97700 -12.22800 -6.68000  1.000 27.99141 ?  13  GLY   A C     1 
ATOM   85   O  O     . GLY   A 1 33  ? -16.76300 -12.42400 -6.80500  1.000 26.84911 ?  13  GLY   A O     1 
ATOM   86   N  N     . GLN   A 1 34  ? -18.46800 -11.32900 -5.81700  1.000 24.36777 ?  14  GLN   A N     1 
ATOM   87   C  CA    . GLN   A 1 34  ? -17.57600 -10.70000 -4.84600  1.000 24.19894 ?  14  GLN   A CA    1 
ATOM   88   C  C     . GLN   A 1 34  ? -16.87400 -11.76200 -4.00600  1.000 20.46034 ?  14  GLN   A C     1 
ATOM   89   O  O     . GLN   A 1 34  ? -15.65500 -11.70200 -3.81600  1.000 18.12216 ?  14  GLN   A O     1 
ATOM   90   C  CB    . GLN   A 1 34  ? -18.32700 -9.73400  -3.91800  1.000 22.39345 ?  14  GLN   A CB    1 
ATOM   91   C  CG    . GLN   A 1 34  ? -18.67000 -8.38400  -4.52100  1.000 25.94850 ?  14  GLN   A CG    1 
ATOM   92   C  CD    . GLN   A 1 34  ? -19.54300 -7.57300  -3.57800  1.000 24.21777 ?  14  GLN   A CD    1 
ATOM   93   O  OE1   . GLN   A 1 34  ? -19.53200 -7.78900  -2.35200  1.000 29.13322 ?  14  GLN   A OE1   1 
ATOM   94   N  NE2   . GLN   A 1 34  ? -20.31900 -6.65900  -4.13800  1.000 31.87606 ?  14  GLN   A NE2   1 
ATOM   95   N  N     . TYR   A 1 35  ? -17.63200 -12.72400 -3.47400  1.000 19.91471 ?  15  TYR   A N     1 
ATOM   96   C  CA    . TYR   A 1 35  ? -17.05300 -13.59900 -2.44900  1.000 16.89094 ?  15  TYR   A CA    1 
ATOM   97   C  C     . TYR   A 1 35  ? -16.21500 -14.72700 -3.04100  1.000 16.62248 ?  15  TYR   A C     1 
ATOM   98   O  O     . TYR   A 1 35  ? -15.23600 -15.16200 -2.42000  1.000 17.93268 ?  15  TYR   A O     1 
ATOM   99   C  CB    . TYR   A 1 35  ? -18.14500 -14.14000 -1.51100  1.000 18.22579 ?  15  TYR   A CB    1 
ATOM   100  C  CG    . TYR   A 1 35  ? -18.20400 -13.22600 -0.28800  1.000 19.79461 ?  15  TYR   A CG    1 
ATOM   101  C  CD1   . TYR   A 1 35  ? -18.98900 -12.08400 -0.31100  1.000 19.86521 ?  15  TYR   A CD1   1 
ATOM   102  C  CD2   . TYR   A 1 35  ? -17.40700 -13.46400 0.83800   1.000 19.59299 ?  15  TYR   A CD2   1 
ATOM   103  C  CE1   . TYR   A 1 35  ? -19.00800 -11.20600 0.75800   1.000 20.24587 ?  15  TYR   A CE1   1 
ATOM   104  C  CE2   . TYR   A 1 35  ? -17.43200 -12.57500 1.94700   1.000 15.77291 ?  15  TYR   A CE2   1 
ATOM   105  C  CZ    . TYR   A 1 35  ? -18.23400 -11.46500 1.88500   1.000 17.12242 ?  15  TYR   A CZ    1 
ATOM   106  O  OH    . TYR   A 1 35  ? -18.24400 -10.57000 2.93100   1.000 17.77001 ?  15  TYR   A OH    1 
ATOM   107  N  N     . LEU   A 1 36  ? -16.54200 -15.19500 -4.24100  1.000 19.45466 ?  16  LEU   A N     1 
ATOM   108  C  CA    . LEU   A 1 36  ? -15.65400 -16.17500 -4.85700  1.000 17.06980 ?  16  LEU   A CA    1 
ATOM   109  C  C     . LEU   A 1 36  ? -14.33000 -15.51800 -5.23300  1.000 18.91771 ?  16  LEU   A C     1 
ATOM   110  O  O     . LEU   A 1 36  ? -13.26900 -16.12400 -5.06800  1.000 18.58855 ?  16  LEU   A O     1 
ATOM   111  C  CB    . LEU   A 1 36  ? -16.33200 -16.84000 -6.08000  1.000 17.62568 ?  16  LEU   A CB    1 
ATOM   112  C  CG    . LEU   A 1 36  ? -17.43200 -17.86600 -5.75900  1.000 18.42248 ?  16  LEU   A CG    1 
ATOM   113  C  CD1   . LEU   A 1 36  ? -18.27000 -18.25900 -6.99800  1.000 18.38866 ?  16  LEU   A CD1   1 
ATOM   114  C  CD2   . LEU   A 1 36  ? -16.88800 -19.16900 -5.06100  1.000 19.62600 ?  16  LEU   A CD2   1 
ATOM   115  N  N     . ASP   A 1 37  ? -14.35100 -14.26200 -5.71200  1.000 18.04446 ?  17  ASP   A N     1 
ATOM   116  C  CA    . ASP   A 1 37  ? -13.07500 -13.56700 -5.93300  1.000 18.67892 ?  17  ASP   A CA    1 
ATOM   117  C  C     . ASP   A 1 37  ? -12.34200 -13.29800 -4.63200  1.000 21.45345 ?  17  ASP   A C     1 
ATOM   118  O  O     . ASP   A 1 37  ? -11.11000 -13.39600 -4.57900  1.000 22.58497 ?  17  ASP   A O     1 
ATOM   119  C  CB    . ASP   A 1 37  ? -13.27400 -12.24500 -6.69200  1.000 25.49488 ?  17  ASP   A CB    1 
ATOM   120  C  CG    . ASP   A 1 37  ? -11.96000 -11.45100 -6.83100  1.000 29.00046 ?  17  ASP   A CG    1 
ATOM   121  O  OD1   . ASP   A 1 37  ? -11.18400 -11.71000 -7.77200  1.000 30.55338 ?  17  ASP   A OD1   1 
ATOM   122  O  OD2   . ASP   A 1 37  ? -11.66200 -10.58800 -5.96300  1.000 33.41491 -1 17  ASP   A OD2   1 
ATOM   123  N  N     . PHE   A 1 38  ? -13.07900 -12.90800 -3.58100  1.000 19.74640 ?  18  PHE   A N     1 
ATOM   124  C  CA    . PHE   A 1 38  ? -12.47300 -12.60100 -2.29100  1.000 18.72929 ?  18  PHE   A CA    1 
ATOM   125  C  C     . PHE   A 1 38  ? -11.81500 -13.84000 -1.69800  1.000 19.96321 ?  18  PHE   A C     1 
ATOM   126  O  O     . PHE   A 1 38  ? -10.69800 -13.77300 -1.16800  1.000 21.57162 ?  18  PHE   A O     1 
ATOM   127  C  CB    . PHE   A 1 38  ? -13.56300 -12.07600 -1.34700  1.000 19.98972 ?  18  PHE   A CB    1 
ATOM   128  C  CG    . PHE   A 1 38  ? -13.07300 -11.59800 0.00500   1.000 21.56982 ?  18  PHE   A CG    1 
ATOM   129  C  CD1   . PHE   A 1 38  ? -11.99800 -10.73800 0.12600   1.000 19.90958 ?  18  PHE   A CD1   1 
ATOM   130  C  CD2   . PHE   A 1 38  ? -13.75100 -11.98400 1.16300   1.000 20.20411 ?  18  PHE   A CD2   1 
ATOM   131  C  CE1   . PHE   A 1 38  ? -11.58400 -10.28200 1.38100   1.000 18.94742 ?  18  PHE   A CE1   1 
ATOM   132  C  CE2   . PHE   A 1 38  ? -13.35100 -11.52500 2.42800   1.000 19.03108 ?  18  PHE   A CE2   1 
ATOM   133  C  CZ    . PHE   A 1 38  ? -12.27100 -10.68500 2.54800   1.000 18.04803 ?  18  PHE   A CZ    1 
ATOM   134  N  N     . HIS   A 1 39  ? -12.49100 -14.98500 -1.79200  1.000 17.81768 ?  19  HIS   A N     1 
ATOM   135  C  CA    . HIS   A 1 39  ? -11.97600 -16.19100 -1.15300  1.000 16.05294 ?  19  HIS   A CA    1 
ATOM   136  C  C     . HIS   A 1 39  ? -10.95600 -16.93800 -2.00400  1.000 17.66084 ?  19  HIS   A C     1 
ATOM   137  O  O     . HIS   A 1 39  ? -10.03200 -17.54500 -1.43200  1.000 18.31218 ?  19  HIS   A O     1 
ATOM   138  C  CB    . HIS   A 1 39  ? -13.13400 -17.13000 -0.77600  1.000 16.96260 ?  19  HIS   A CB    1 
ATOM   139  C  CG    . HIS   A 1 39  ? -13.76800 -16.77900 0.53800   1.000 18.40982 ?  19  HIS   A CG    1 
ATOM   140  N  ND1   . HIS   A 1 39  ? -14.14500 -17.73300 1.47000   1.000 21.69560 ?  19  HIS   A ND1   1 
ATOM   141  C  CD2   . HIS   A 1 39  ? -14.07000 -15.57600 1.09000   1.000 20.12203 ?  19  HIS   A CD2   1 
ATOM   142  C  CE1   . HIS   A 1 39  ? -14.64500 -17.12800 2.53700   1.000 20.11436 ?  19  HIS   A CE1   1 
ATOM   143  N  NE2   . HIS   A 1 39  ? -14.61800 -15.82300 2.33300   1.000 19.20487 ?  19  HIS   A NE2   1 
ATOM   144  N  N     . TYR   A 1 40  ? -11.07400 -16.89100 -3.35000  1.000 16.51639 ?  20  TYR   A N     1 
ATOM   145  C  CA    . TYR   A 1 40  ? -10.24500 -17.72200 -4.23800  1.000 18.63337 ?  20  TYR   A CA    1 
ATOM   146  C  C     . TYR   A 1 40  ? -9.55000  -16.94400 -5.36200  1.000 23.16283 ?  20  TYR   A C     1 
ATOM   147  O  O     . TYR   A 1 40  ? -8.81300  -17.54700 -6.16100  1.000 21.50363 ?  20  TYR   A O     1 
ATOM   148  C  CB    . TYR   A 1 40  ? -11.08700 -18.85000 -4.86300  1.000 19.03599 ?  20  TYR   A CB    1 
ATOM   149  C  CG    . TYR   A 1 40  ? -11.75100 -19.71300 -3.81400  1.000 19.67430 ?  20  TYR   A CG    1 
ATOM   150  C  CD1   . TYR   A 1 40  ? -11.00000 -20.61300 -3.04000  1.000 23.27643 ?  20  TYR   A CD1   1 
ATOM   151  C  CD2   . TYR   A 1 40  ? -13.12100 -19.63100 -3.57600  1.000 19.56947 ?  20  TYR   A CD2   1 
ATOM   152  C  CE1   . TYR   A 1 40  ? -11.60200 -21.39800 -2.04300  1.000 22.28036 ?  20  TYR   A CE1   1 
ATOM   153  C  CE2   . TYR   A 1 40  ? -13.73400 -20.42500 -2.58800  1.000 20.00503 ?  20  TYR   A CE2   1 
ATOM   154  C  CZ    . TYR   A 1 40  ? -12.96000 -21.30900 -1.82800  1.000 20.99304 ?  20  TYR   A CZ    1 
ATOM   155  O  OH    . TYR   A 1 40  ? -13.57200 -22.08800 -0.86300  1.000 18.81971 ?  20  TYR   A OH    1 
ATOM   156  N  N     . GLY   A 1 41  ? -9.76200  -15.63600 -5.46400  1.000 24.03676 ?  21  GLY   A N     1 
ATOM   157  C  CA    . GLY   A 1 41  ? -9.17000  -14.87400 -6.54000  1.000 26.80249 ?  21  GLY   A CA    1 
ATOM   158  C  C     . GLY   A 1 41  ? -7.79700  -14.32700 -6.21200  1.000 27.16055 ?  21  GLY   A C     1 
ATOM   159  O  O     . GLY   A 1 41  ? -7.24800  -14.53500 -5.12800  1.000 28.10322 ?  21  GLY   A O     1 
ATOM   160  N  N     . PRO   A 1 42  ? -7.21700  -13.60600 -7.16300  1.000 30.13475 ?  22  PRO   A N     1 
ATOM   161  C  CA    . PRO   A 1 42  ? -5.94200  -12.94300 -6.90600  1.000 32.37131 ?  22  PRO   A CA    1 
ATOM   162  C  C     . PRO   A 1 42  ? -6.13100  -11.78700 -5.93400  1.000 31.54296 ?  22  PRO   A C     1 
ATOM   163  O  O     . PRO   A 1 42  ? -7.23200  -11.26100 -5.75400  1.000 34.94206 ?  22  PRO   A O     1 
ATOM   164  C  CB    . PRO   A 1 42  ? -5.53400  -12.44400 -8.29200  1.000 38.12650 ?  22  PRO   A CB    1 
ATOM   165  C  CG    . PRO   A 1 42  ? -6.85800  -12.08000 -8.90000  1.000 35.17095 ?  22  PRO   A CG    1 
ATOM   166  C  CD    . PRO   A 1 42  ? -7.75600  -13.24800 -8.48600  1.000 35.21676 ?  22  PRO   A CD    1 
ATOM   167  N  N     . GLY   A 1 43  ? -5.03300  -11.40400 -5.30700  1.000 32.11699 ?  23  GLY   A N     1 
ATOM   168  C  CA    . GLY   A 1 43  ? -5.06200  -10.35100 -4.32000  1.000 29.18630 ?  23  GLY   A CA    1 
ATOM   169  C  C     . GLY   A 1 43  ? -5.13500  -8.97800  -4.95900  1.000 21.76963 ?  23  GLY   A C     1 
ATOM   170  O  O     . GLY   A 1 43  ? -4.97300  -8.80700  -6.16700  1.000 27.98758 ?  23  GLY   A O     1 
ATOM   171  N  N     . HIS   A 1 44  ? -5.43500  -7.98800  -4.11500  1.000 18.72696 ?  24  HIS   A N     1 
ATOM   172  C  CA    . HIS   A 1 44  ? -5.54000  -6.60200  -4.52800  1.000 23.59094 ?  24  HIS   A CA    1 
ATOM   173  C  C     . HIS   A 1 44  ? -4.74900  -5.73600  -3.56600  1.000 22.44449 ?  24  HIS   A C     1 
ATOM   174  O  O     . HIS   A 1 44  ? -4.68600  -6.03200  -2.36700  1.000 23.04234 ?  24  HIS   A O     1 
ATOM   175  C  CB    . HIS   A 1 44  ? -7.01900  -6.15800  -4.59400  1.000 21.59400 ?  24  HIS   A CB    1 
ATOM   176  C  CG    . HIS   A 1 44  ? -7.89300  -7.11700  -5.34800  1.000 23.36697 ?  24  HIS   A CG    1 
ATOM   177  N  ND1   . HIS   A 1 44  ? -7.88400  -7.19800  -6.72100  1.000 25.58401 ?  24  HIS   A ND1   1 
ATOM   178  C  CD2   . HIS   A 1 44  ? -8.81400  -8.01700  -4.92400  1.000 25.23440 ?  24  HIS   A CD2   1 
ATOM   179  C  CE1   . HIS   A 1 44  ? -8.74700  -8.11400  -7.11700  1.000 21.06196 ?  24  HIS   A CE1   1 
ATOM   180  N  NE2   . HIS   A 1 44  ? -9.32400  -8.63100  -6.04300  1.000 27.82860 ?  24  HIS   A NE2   1 
ATOM   181  N  N     . PHE   A 1 45  ? -4.12700  -4.67400  -4.10700  1.000 19.66069 ?  25  PHE   A N     1 
ATOM   182  C  CA    . PHE   A 1 45  ? -3.37000  -3.69700  -3.30700  1.000 23.09677 ?  25  PHE   A CA    1 
ATOM   183  C  C     . PHE   A 1 45  ? -2.31100  -4.37000  -2.42800  1.000 20.68888 ?  25  PHE   A C     1 
ATOM   184  O  O     . PHE   A 1 45  ? -1.96900  -3.86800  -1.34700  1.000 25.05698 ?  25  PHE   A O     1 
ATOM   185  C  CB    . PHE   A 1 45  ? -4.30400  -2.83400  -2.43900  1.000 23.86234 ?  25  PHE   A CB    1 
ATOM   186  C  CG    . PHE   A 1 45  ? -5.35400  -2.10300  -3.21600  1.000 20.56273 ?  25  PHE   A CG    1 
ATOM   187  C  CD1   . PHE   A 1 45  ? -4.99800  -1.10500  -4.11900  1.000 24.28515 ?  25  PHE   A CD1   1 
ATOM   188  C  CD2   . PHE   A 1 45  ? -6.69700  -2.41900  -3.07700  1.000 22.86440 ?  25  PHE   A CD2   1 
ATOM   189  C  CE1   . PHE   A 1 45  ? -5.95800  -0.43700  -4.87100  1.000 23.89557 ?  25  PHE   A CE1   1 
ATOM   190  C  CE2   . PHE   A 1 45  ? -7.67000  -1.73000  -3.82500  1.000 21.01748 ?  25  PHE   A CE2   1 
ATOM   191  C  CZ    . PHE   A 1 45  ? -7.29600  -0.75100  -4.72700  1.000 22.82068 ?  25  PHE   A CZ    1 
ATOM   192  N  N     . ASP   A 1 46  ? -1.80200  -5.52200  -2.87600  1.000 23.87794 ?  26  ASP   A N     1 
ATOM   193  C  CA    . ASP   A 1 46  ? -0.82400  -6.31100  -2.11400  1.000 25.48998 ?  26  ASP   A CA    1 
ATOM   194  C  C     . ASP   A 1 46  ? -1.32600  -6.71600  -0.72200  1.000 28.64203 ?  26  ASP   A C     1 
ATOM   195  O  O     . ASP   A 1 46  ? -0.52400  -7.00800  0.16300   1.000 27.99221 ?  26  ASP   A O     1 
ATOM   196  C  CB    . ASP   A 1 46  ? 0.51800   -5.58000  -1.99800  1.000 29.25716 ?  26  ASP   A CB    1 
ATOM   197  C  CG    . ASP   A 1 46  ? 1.14900   -5.30500  -3.36100  1.000 36.02497 ?  26  ASP   A CG    1 
ATOM   198  O  OD1   . ASP   A 1 46  ? 1.12300   -6.21200  -4.21200  1.000 43.10428 ?  26  ASP   A OD1   1 
ATOM   199  O  OD2   . ASP   A 1 46  ? 1.66300   -4.19600  -3.58600  1.000 42.63772 -1 26  ASP   A OD2   1 
ATOM   200  N  N     . VAL   A 1 47  ? -2.63700  -6.78400  -0.51200  1.000 22.60104 ?  27  VAL   A N     1 
ATOM   201  C  CA    . VAL   A 1 47  ? -3.17700  -7.29000  0.75400   1.000 22.64206 ?  27  VAL   A CA    1 
ATOM   202  C  C     . VAL   A 1 47  ? -3.30900  -8.81200  0.67300   1.000 22.48283 ?  27  VAL   A C     1 
ATOM   203  O  O     . VAL   A 1 47  ? -3.91300  -9.32800  -0.28300  1.000 22.04898 ?  27  VAL   A O     1 
ATOM   204  C  CB    . VAL   A 1 47  ? -4.52700  -6.62700  1.06900   1.000 21.31850 ?  27  VAL   A CB    1 
ATOM   205  C  CG1   . VAL   A 1 47  ? -5.12100  -7.19500  2.37600   1.000 19.91651 ?  27  VAL   A CG1   1 
ATOM   206  C  CG2   . VAL   A 1 47  ? -4.35000  -5.11300  1.17500   1.000 21.98935 ?  27  VAL   A CG2   1 
ATOM   207  N  N     . PRO   A 1 48  ? -2.78600  -9.57200  1.64500   1.000 22.75289 ?  28  PRO   A N     1 
ATOM   208  C  CA    . PRO   A 1 48  ? -2.90100  -11.03700 1.59000   1.000 19.44746 ?  28  PRO   A CA    1 
ATOM   209  C  C     . PRO   A 1 48  ? -4.35200  -11.50700 1.62900   1.000 19.39010 ?  28  PRO   A C     1 
ATOM   210  O  O     . PRO   A 1 48  ? -5.24000  -10.83300 2.16200   1.000 20.41044 ?  28  PRO   A O     1 
ATOM   211  C  CB    . PRO   A 1 48  ? -2.15100  -11.49800 2.84800   1.000 23.31526 ?  28  PRO   A CB    1 
ATOM   212  C  CG    . PRO   A 1 48  ? -1.19300  -10.35800 3.15300   1.000 23.34470 ?  28  PRO   A CG    1 
ATOM   213  C  CD    . PRO   A 1 48  ? -1.95500  -9.11500  2.78400   1.000 23.58337 ?  28  PRO   A CD    1 
ATOM   214  N  N     . ASN   A 1 49  ? -4.58400  -12.69300 1.06200   1.000 19.81525 ?  29  ASN   A N     1 
ATOM   215  C  CA    . ASN   A 1 49  ? -5.90300  -13.32500 1.13300   1.000 18.08570 ?  29  ASN   A CA    1 
ATOM   216  C  C     . ASN   A 1 49  ? -6.38700  -13.38800 2.57900   1.000 20.46393 ?  29  ASN   A C     1 
ATOM   217  O  O     . ASN   A 1 49  ? -5.67000  -13.86100 3.45700   1.000 19.12116 ?  29  ASN   A O     1 
ATOM   218  C  CB    . ASN   A 1 49  ? -5.84100  -14.73300 0.54600   1.000 20.03660 ?  29  ASN   A CB    1 
ATOM   219  C  CG    . ASN   A 1 49  ? -7.17800  -15.43600 0.58900   1.000 19.82783 ?  29  ASN   A CG    1 
ATOM   220  O  OD1   . ASN   A 1 49  ? -7.49600  -16.14300 1.56200   1.000 20.90717 ?  29  ASN   A OD1   1 
ATOM   221  N  ND2   . ASN   A 1 49  ? -7.99000  -15.23600 -0.45600  1.000 21.24226 ?  29  ASN   A ND2   1 
ATOM   222  N  N     . TYR   A 1 50  ? -7.61200  -12.91800 2.82200   1.000 19.46915 ?  30  TYR   A N     1 
ATOM   223  C  CA    . TYR   A 1 50  ? -8.07400  -12.70000 4.19800   1.000 16.88178 ?  30  TYR   A CA    1 
ATOM   224  C  C     . TYR   A 1 50  ? -8.45000  -14.00100 4.91800   1.000 18.12376 ?  30  TYR   A C     1 
ATOM   225  O  O     . TYR   A 1 50  ? -7.99500  -14.22300 6.04900   1.000 18.20377 ?  30  TYR   A O     1 
ATOM   226  C  CB    . TYR   A 1 50  ? -9.25600  -11.72600 4.20700   1.000 16.57370 ?  30  TYR   A CB    1 
ATOM   227  C  CG    . TYR   A 1 50  ? -9.89900  -11.47000 5.57500   1.000 16.08024 ?  30  TYR   A CG    1 
ATOM   228  C  CD1   . TYR   A 1 50  ? -9.19600  -10.84200 6.61400   1.000 15.73781 ?  30  TYR   A CD1   1 
ATOM   229  C  CD2   . TYR   A 1 50  ? -11.22400 -11.81000 5.80100   1.000 17.47501 ?  30  TYR   A CD2   1 
ATOM   230  C  CE1   . TYR   A 1 50  ? -9.80700  -10.56400 7.83200   1.000 16.28503 ?  30  TYR   A CE1   1 
ATOM   231  C  CE2   . TYR   A 1 50  ? -11.84400 -11.54400 7.03100   1.000 12.39141 ?  30  TYR   A CE2   1 
ATOM   232  C  CZ    . TYR   A 1 50  ? -11.12100 -10.92200 8.03300   1.000 17.16279 ?  30  TYR   A CZ    1 
ATOM   233  O  OH    . TYR   A 1 50  ? -11.72700 -10.65100 9.26000   1.000 16.80053 ?  30  TYR   A OH    1 
ATOM   234  N  N     . PRO   A 1 51  ? -9.27300  -14.88000 4.32900   1.000 18.55850 ?  31  PRO   A N     1 
ATOM   235  C  CA    . PRO   A 1 51  ? -9.56000  -16.14200 5.02600   1.000 18.93999 ?  31  PRO   A CA    1 
ATOM   236  C  C     . PRO   A 1 51  ? -8.29100  -16.89800 5.37500   1.000 18.62458 ?  31  PRO   A C     1 
ATOM   237  O  O     . PRO   A 1 51  ? -8.15800  -17.38800 6.50400   1.000 21.10310 ?  31  PRO   A O     1 
ATOM   238  C  CB    . PRO   A 1 51  ? -10.44000 -16.90500 4.02300   1.000 18.38062 ?  31  PRO   A CB    1 
ATOM   239  C  CG    . PRO   A 1 51  ? -11.14400 -15.77300 3.26900   1.000 20.72078 ?  31  PRO   A CG    1 
ATOM   240  C  CD    . PRO   A 1 51  ? -10.06300 -14.74100 3.08700   1.000 20.37195 ?  31  PRO   A CD    1 
ATOM   241  N  N     . LYS   A 1 52  ? -7.33100  -16.95800 4.44700   1.000 19.23862 ?  32  LYS   A N     1 
ATOM   242  C  CA    . LYS   A 1 52  ? -6.06800  -17.63100 4.73700   1.000 20.21373 ?  32  LYS   A CA    1 
ATOM   243  C  C     . LYS   A 1 52  ? -5.30100  -16.93500 5.86200   1.000 18.89612 ?  32  LYS   A C     1 
ATOM   244  O  O     . LYS   A 1 52  ? -4.76200  -17.60400 6.75300   1.000 21.58661 ?  32  LYS   A O     1 
ATOM   245  C  CB    . LYS   A 1 52  ? -5.21600  -17.72400 3.46400   1.000 20.80032 ?  32  LYS   A CB    1 
ATOM   246  C  CG    . LYS   A 1 52  ? -3.82700  -18.30900 3.68700   1.000 25.22849 ?  32  LYS   A CG    1 
ATOM   247  C  CD    . LYS   A 1 52  ? -3.00800  -18.30700 2.39500   1.000 25.37892 ?  32  LYS   A CD    1 
ATOM   248  C  CE    . LYS   A 1 52  ? -1.80100  -19.22000 2.50200   1.000 35.35498 ?  32  LYS   A CE    1 
ATOM   249  N  N     . ALA   A 1 53  ? -5.21500  -15.59600 5.82600   1.000 19.60727 ?  33  ALA   A N     1 
ATOM   250  C  CA    . ALA   A 1 53  ? -4.52900  -14.85500 6.88800   1.000 17.92149 ?  33  ALA   A CA    1 
ATOM   251  C  C     . ALA   A 1 53  ? -5.17000  -15.11100 8.24500   1.000 21.26619 ?  33  ALA   A C     1 
ATOM   252  O  O     . ALA   A 1 53  ? -4.47400  -15.20000 9.26600   1.000 18.77047 ?  33  ALA   A O     1 
ATOM   253  C  CB    . ALA   A 1 53  ? -4.54200  -13.35500 6.60000   1.000 19.89111 ?  33  ALA   A CB    1 
ATOM   254  N  N     . CYS   A 1 54  ? -6.50200  -15.17500 8.28900   1.000 18.53878 ?  34  CYS   A N     1 
ATOM   255  C  CA    . CYS   A 1 54  ? -7.16900  -15.43500 9.55900   1.000 18.78940 ?  34  CYS   A CA    1 
ATOM   256  C  C     . CYS   A 1 54  ? -6.77500  -16.80300 10.10900  1.000 18.26798 ?  34  CYS   A C     1 
ATOM   257  O  O     . CYS   A 1 54  ? -6.42900  -16.93500 11.29200  1.000 18.84954 ?  34  CYS   A O     1 
ATOM   258  C  CB    . CYS   A 1 54  ? -8.68200  -15.36700 9.38900   1.000 16.53131 ?  34  CYS   A CB    1 
ATOM   259  S  SG    . CYS   A 1 54  ? -9.31700  -13.70700 9.14900   1.000 18.49368 ?  34  CYS   A SG    1 
ATOM   260  N  N     . ILE   A 1 55  ? -6.84200  -17.83000 9.26500   1.000 19.91154 ?  35  ILE   A N     1 
ATOM   261  C  CA    . ILE   A 1 55  ? -6.55600  -19.18100 9.74700   1.000 19.66061 ?  35  ILE   A CA    1 
ATOM   262  C  C     . ILE   A 1 55  ? -5.07200  -19.33000 10.08600  1.000 19.93905 ?  35  ILE   A C     1 
ATOM   263  O  O     . ILE   A 1 55  ? -4.71000  -20.08200 11.00600  1.000 20.32584 ?  35  ILE   A O     1 
ATOM   264  C  CB    . ILE   A 1 55  ? -7.04800  -20.21700 8.71600   1.000 19.82272 ?  35  ILE   A CB    1 
ATOM   265  C  CG1   . ILE   A 1 55  ? -8.58000  -20.16100 8.60500   1.000 18.69986 ?  35  ILE   A CG1   1 
ATOM   266  C  CG2   . ILE   A 1 55  ? -6.56900  -21.65100 9.08400   1.000 20.45958 ?  35  ILE   A CG2   1 
ATOM   267  C  CD1   . ILE   A 1 55  ? -9.32400  -20.00000 9.96300   1.000 17.22706 ?  35  ILE   A CD1   1 
ATOM   268  N  N     . GLU   A 1 56  ? -4.17900  -18.63700 9.37200   1.000 21.51186 ?  36  GLU   A N     1 
ATOM   269  C  CA    . GLU   A 1 56  ? -2.78500  -18.66400 9.80100   1.000 20.59758 ?  36  GLU   A CA    1 
ATOM   270  C  C     . GLU   A 1 56  ? -2.66200  -18.21000 11.25400  1.000 20.48622 ?  36  GLU   A C     1 
ATOM   271  O  O     . GLU   A 1 56  ? -1.94600  -18.82900 12.04300  1.000 22.02608 ?  36  GLU   A O     1 
ATOM   272  C  CB    . GLU   A 1 56  ? -1.90800  -17.80300 8.89100   1.000 24.45702 ?  36  GLU   A CB    1 
ATOM   273  C  CG    . GLU   A 1 56  ? -1.66700  -18.43000 7.52500   1.000 23.39869 ?  36  GLU   A CG    1 
ATOM   274  C  CD    . GLU   A 1 56  ? -0.87600  -17.51700 6.60900   1.000 31.46032 ?  36  GLU   A CD    1 
ATOM   275  O  OE1   . GLU   A 1 56  ? -0.72500  -16.31700 6.94400   1.000 30.78267 ?  36  GLU   A OE1   1 
ATOM   276  O  OE2   . GLU   A 1 56  ? -0.44400  -17.99900 5.54300   1.000 30.65875 -1 36  GLU   A OE2   1 
ATOM   277  N  N     . GLN   A 1 57  ? -3.39700  -17.16300 11.64100  1.000 20.42785 ?  37  GLN   A N     1 
ATOM   278  C  CA    . GLN   A 1 57  ? -3.31800  -16.69600 13.02900  1.000 20.16405 ?  37  GLN   A CA    1 
ATOM   279  C  C     . GLN   A 1 57  ? -3.91000  -17.70100 14.01300  1.000 25.09727 ?  37  GLN   A C     1 
ATOM   280  O  O     . GLN   A 1 57  ? -3.37100  -17.89900 15.11300  1.000 23.10372 ?  37  GLN   A O     1 
ATOM   281  C  CB    . GLN   A 1 57  ? -4.02800  -15.35900 13.17900  1.000 26.02066 ?  37  GLN   A CB    1 
ATOM   282  C  CG    . GLN   A 1 57  ? -3.22300  -14.22400 12.64700  1.000 29.60234 ?  37  GLN   A CG    1 
ATOM   283  C  CD    . GLN   A 1 57  ? -1.95100  -14.00700 13.43000  1.000 38.04537 ?  37  GLN   A CD    1 
ATOM   284  O  OE1   . GLN   A 1 57  ? -1.92200  -14.18800 14.63800  1.000 34.94972 ?  37  GLN   A OE1   1 
ATOM   285  N  NE2   . GLN   A 1 57  ? -0.89000  -13.58800 12.73900  1.000 51.86576 ?  37  GLN   A NE2   1 
ATOM   286  N  N     . ALA   A 1 58  ? -5.04100  -18.31100 13.66100  1.000 21.37497 ?  38  ALA   A N     1 
ATOM   287  C  CA    . ALA   A 1 58  ? -5.62400  -19.32200 14.53400  1.000 18.17675 ?  38  ALA   A CA    1 
ATOM   288  C  C     . ALA   A 1 58  ? -4.66300  -20.48600 14.74500  1.000 22.71817 ?  38  ALA   A C     1 
ATOM   289  O  O     . ALA   A 1 58  ? -4.48900  -20.96500 15.87800  1.000 22.40091 ?  38  ALA   A O     1 
ATOM   290  C  CB    . ALA   A 1 58  ? -6.94000  -19.82100 13.94800  1.000 19.06042 ?  38  ALA   A CB    1 
ATOM   291  N  N     . LEU   A 1 59  ? -4.03700  -20.96400 13.66300  1.000 23.48942 ?  39  LEU   A N     1 
ATOM   292  C  CA    . LEU   A 1 59  ? -3.13300  -22.11000 13.77800  1.000 23.70075 ?  39  LEU   A CA    1 
ATOM   293  C  C     . LEU   A 1 59  ? -1.88200  -21.75100 14.57500  1.000 21.30703 ?  39  LEU   A C     1 
ATOM   294  O  O     . LEU   A 1 59  ? -1.29300  -22.61900 15.22700  1.000 27.15369 ?  39  LEU   A O     1 
ATOM   295  C  CB    . LEU   A 1 59  ? -2.76400  -22.62200 12.37900  1.000 22.97191 ?  39  LEU   A CB    1 
ATOM   296  C  CG    . LEU   A 1 59  ? -3.95500  -23.26600 11.66600  1.000 22.14449 ?  39  LEU   A CG    1 
ATOM   297  C  CD1   . LEU   A 1 59  ? -3.64800  -23.75700 10.22200  1.000 27.25427 ?  39  LEU   A CD1   1 
ATOM   298  C  CD2   . LEU   A 1 59  ? -4.49400  -24.41000 12.49600  1.000 26.85008 ?  39  LEU   A CD2   1 
ATOM   299  N  N     . ALA   A 1 60  ? -1.47300  -20.48100 14.56300  1.000 20.99527 ?  40  ALA   A N     1 
ATOM   300  C  CA    . ALA   A 1 60  ? -0.29100  -20.07400 15.31400  1.000 20.24894 ?  40  ALA   A CA    1 
ATOM   301  C  C     . ALA   A 1 60  ? -0.53500  -20.05900 16.82300  1.000 24.82987 ?  40  ALA   A C     1 
ATOM   302  O  O     . ALA   A 1 60  ? 0.42500   -20.00300 17.59700  1.000 23.05646 ?  40  ALA   A O     1 
ATOM   303  C  CB    . ALA   A 1 60  ? 0.17600   -18.68800 14.85100  1.000 23.49046 ?  40  ALA   A CB    1 
ATOM   304  N  N     . HIS   A 1 61  ? -1.79000  -20.10800 17.25600  1.000 21.56516 ?  41  HIS   A N     1 
ATOM   305  C  CA    . HIS   A 1 61  ? -2.13300  -19.98300 18.67000  1.000 20.54239 ?  41  HIS   A CA    1 
ATOM   306  C  C     . HIS   A 1 61  ? -2.85100  -21.19400 19.25200  1.000 23.83527 ?  41  HIS   A C     1 
ATOM   307  O  O     . HIS   A 1 61  ? -3.01800  -21.26200 20.47600  1.000 27.25184 ?  41  HIS   A O     1 
ATOM   308  C  CB    . HIS   A 1 61  ? -3.01500  -18.74000 18.88900  1.000 23.14262 ?  41  HIS   A CB    1 
ATOM   309  C  CG    . HIS   A 1 61  ? -2.29200  -17.45700 18.66200  1.000 25.57302 ?  41  HIS   A CG    1 
ATOM   310  N  ND1   . HIS   A 1 61  ? -2.23500  -16.85200 17.42300  1.000 26.86526 ?  41  HIS   A ND1   1 
ATOM   311  C  CD2   . HIS   A 1 61  ? -1.60400  -16.65100 19.51000  1.000 26.62106 ?  41  HIS   A CD2   1 
ATOM   312  C  CE1   . HIS   A 1 61  ? -1.52200  -15.74300 17.51200  1.000 26.43702 ?  41  HIS   A CE1   1 
ATOM   313  N  NE2   . HIS   A 1 61  ? -1.12900  -15.59800 18.76400  1.000 32.86745 ?  41  HIS   A NE2   1 
ATOM   314  N  N     . HIS   A 1 62  ? -3.27100  -22.14500 18.43000  1.000 22.72573 ?  42  HIS   A N     1 
ATOM   315  C  CA    . HIS   A 1 62  ? -3.99100  -23.30900 18.93400  1.000 23.90469 ?  42  HIS   A CA    1 
ATOM   316  C  C     . HIS   A 1 62  ? -3.00500  -24.29200 19.55200  1.000 25.89392 ?  42  HIS   A C     1 
ATOM   317  O  O     . HIS   A 1 62  ? -2.11200  -24.79000 18.86300  1.000 24.42564 ?  42  HIS   A O     1 
ATOM   318  C  CB    . HIS   A 1 62  ? -4.77300  -23.97600 17.80300  1.000 22.86718 ?  42  HIS   A CB    1 
ATOM   319  C  CG    . HIS   A 1 62  ? -5.57000  -25.17500 18.23200  1.000 22.59384 ?  42  HIS   A CG    1 
ATOM   320  N  ND1   . HIS   A 1 62  ? -6.49700  -25.13300 19.25100  1.000 22.10579 ?  42  HIS   A ND1   1 
ATOM   321  C  CD2   . HIS   A 1 62  ? -5.59700  -26.44100 17.75300  1.000 22.66544 ?  42  HIS   A CD2   1 
ATOM   322  C  CE1   . HIS   A 1 62  ? -7.05100  -26.32600 19.39300  1.000 22.04568 ?  42  HIS   A CE1   1 
ATOM   323  N  NE2   . HIS   A 1 62  ? -6.51600  -27.14200 18.50400  1.000 21.56475 ?  42  HIS   A NE2   1 
ATOM   324  N  N     . THR   A 1 63  ? -3.15100  -24.55100 20.85200  1.000 25.40557 ?  43  THR   A N     1 
ATOM   325  C  CA    . THR   A 1 63  ? -2.27300  -25.46900 21.56200  1.000 25.92577 ?  43  THR   A CA    1 
ATOM   326  C  C     . THR   A 1 63  ? -2.97400  -26.76800 21.91900  1.000 28.19914 ?  43  THR   A C     1 
ATOM   327  O  O     . THR   A 1 63  ? -2.38700  -27.60900 22.61200  1.000 28.47752 ?  43  THR   A O     1 
ATOM   328  C  CB    . THR   A 1 63  ? -1.71700  -24.79800 22.81900  1.000 26.57807 ?  43  THR   A CB    1 
ATOM   329  O  OG1   . THR   A 1 63  ? -2.80300  -24.41400 23.67100  1.000 24.07090 ?  43  THR   A OG1   1 
ATOM   330  C  CG2   . THR   A 1 63  ? -0.90400  -23.54600 22.45400  1.000 23.86397 ?  43  THR   A CG2   1 
ATOM   331  N  N     . GLY   A 1 64  ? -4.21300  -26.94800 21.46800  1.000 23.46028 ?  44  GLY   A N     1 
ATOM   332  C  CA    . GLY   A 1 64  ? -4.96100  -28.15900 21.72400  1.000 25.52123 ?  44  GLY   A CA    1 
ATOM   333  C  C     . GLY   A 1 64  ? -4.76700  -29.21900 20.65300  1.000 26.52152 ?  44  GLY   A C     1 
ATOM   334  O  O     . GLY   A 1 64  ? -3.85000  -29.17200 19.83000  1.000 28.52706 ?  44  GLY   A O     1 
ATOM   335  N  N     . THR   A 1 65  ? -5.64800  -30.21400 20.69400  1.000 30.49641 ?  45  THR   A N     1 
ATOM   336  C  CA    . THR   A 1 65  ? -5.63100  -31.28400 19.70700  1.000 26.40792 ?  45  THR   A CA    1 
ATOM   337  C  C     . THR   A 1 65  ? -6.30700  -30.82200 18.41600  1.000 26.50751 ?  45  THR   A C     1 
ATOM   338  O  O     . THR   A 1 65  ? -6.96200  -29.77900 18.36600  1.000 26.35495 ?  45  THR   A O     1 
ATOM   339  C  CB    . THR   A 1 65  ? -6.29300  -32.53800 20.28100  1.000 29.54606 ?  45  THR   A CB    1 
ATOM   340  O  OG1   . THR   A 1 65  ? -7.53500  -32.19500 20.91400  1.000 32.20621 ?  45  THR   A OG1   1 
ATOM   341  C  CG2   . THR   A 1 65  ? -5.38200  -33.18700 21.32700  1.000 34.47825 ?  45  THR   A CG2   1 
ATOM   342  N  N     . THR   A 1 66  ? -6.11800  -31.59400 17.35100  1.000 25.21733 ?  46  THR   A N     1 
ATOM   343  C  CA    . THR   A 1 66  ? -6.51000  -31.15300 16.01800  1.000 25.93364 ?  46  THR   A CA    1 
ATOM   344  C  C     . THR   A 1 66  ? -7.50800  -32.11000 15.37900  1.000 24.23471 ?  46  THR   A C     1 
ATOM   345  O  O     . THR   A 1 66  ? -7.43500  -32.39200 14.18100  1.000 23.95151 ?  46  THR   A O     1 
ATOM   346  C  CB    . THR   A 1 66  ? -5.28700  -30.98400 15.12000  1.000 27.32760 ?  46  THR   A CB    1 
ATOM   347  O  OG1   . THR   A 1 66  ? -4.51700  -32.19500 15.12300  1.000 30.70809 ?  46  THR   A OG1   1 
ATOM   348  C  CG2   . THR   A 1 66  ? -4.43400  -29.79900 15.58800  1.000 30.03308 ?  46  THR   A CG2   1 
ATOM   349  N  N     . GLY   A 1 67  ? -8.46500  -32.60800 16.17100  1.000 23.03683 ?  47  GLY   A N     1 
ATOM   350  C  CA    . GLY   A 1 67  ? -9.48900  -33.50400 15.66300  1.000 24.22287 ?  47  GLY   A CA    1 
ATOM   351  C  C     . GLY   A 1 67  ? -10.63200 -32.82100 14.93100  1.000 24.82030 ?  47  GLY   A C     1 
ATOM   352  O  O     . GLY   A 1 67  ? -11.09800 -33.32200 13.90800  1.000 23.65508 ?  47  GLY   A O     1 
ATOM   353  N  N     . ARG   A 1 68  ? -11.10200 -31.67800 15.42700  1.000 22.08650 ?  48  ARG   A N     1 
ATOM   354  C  CA    . ARG   A 1 68  ? -12.33400 -31.11100 14.88900  1.000 22.16751 ?  48  ARG   A CA    1 
ATOM   355  C  C     . ARG   A 1 68  ? -12.35900 -29.59300 14.98500  1.000 18.30649 ?  48  ARG   A C     1 
ATOM   356  O  O     . ARG   A 1 68  ? -12.12300 -29.04700 16.06500  1.000 22.33435 ?  48  ARG   A O     1 
ATOM   357  C  CB    . ARG   A 1 68  ? -13.50900 -31.69100 15.66400  1.000 21.63257 ?  48  ARG   A CB    1 
ATOM   358  C  CG    . ARG   A 1 68  ? -14.70900 -31.93600 14.83000  1.000 27.95679 ?  48  ARG   A CG    1 
ATOM   359  C  CD    . ARG   A 1 68  ? -15.70200 -32.73400 15.66600  1.000 28.70987 ?  48  ARG   A CD    1 
ATOM   360  N  NE    . ARG   A 1 68  ? -16.96300 -32.83700 14.95000  1.000 26.22880 ?  48  ARG   A NE    1 
ATOM   361  C  CZ    . ARG   A 1 68  ? -18.13500 -32.48200 15.45200  1.000 23.34869 ?  48  ARG   A CZ    1 
ATOM   362  N  NH1   . ARG   A 1 68  ? -18.25100 -32.07800 16.70600  1.000 20.49228 ?  48  ARG   A NH1   1 
ATOM   363  N  NH2   . ARG   A 1 68  ? -19.21400 -32.51900 14.66800  1.000 26.07868 ?  48  ARG   A NH2   1 
ATOM   364  N  N     . ALA   A 1 69  ? -12.69100 -28.92000 13.86700  1.000 18.27044 ?  49  ALA   A N     1 
ATOM   365  C  CA    . ALA   A 1 69  ? -12.89100 -27.47100 13.85900  1.000 17.81687 ?  49  ALA   A CA    1 
ATOM   366  C  C     . ALA   A 1 69  ? -14.22300 -27.13300 13.20400  1.000 18.82999 ?  49  ALA   A C     1 
ATOM   367  O  O     . ALA   A 1 69  ? -14.74300 -27.87300 12.35400  1.000 19.25143 ?  49  ALA   A O     1 
ATOM   368  C  CB    . ALA   A 1 69  ? -11.77300 -26.72200 13.12400  1.000 17.76004 ?  49  ALA   A CB    1 
ATOM   369  N  N     . LEU   A 1 70  ? -14.74300 -25.96900 13.58700  1.000 19.87592 ?  50  LEU   A N     1 
ATOM   370  C  CA    . LEU   A 1 70  ? -16.03500 -25.45100 13.14400  1.000 16.61439 ?  50  LEU   A CA    1 
ATOM   371  C  C     . LEU   A 1 70  ? -15.80400 -24.05400 12.58300  1.000 15.90872 ?  50  LEU   A C     1 
ATOM   372  O  O     . LEU   A 1 70  ? -15.16100 -23.23600 13.24000  1.000 17.66084 ?  50  LEU   A O     1 
ATOM   373  C  CB    . LEU   A 1 70  ? -17.03000 -25.38400 14.32400  1.000 17.94664 ?  50  LEU   A CB    1 
ATOM   374  C  CG    . LEU   A 1 70  ? -18.44900 -24.88000 14.04000  1.000 20.22013 ?  50  LEU   A CG    1 
ATOM   375  C  CD1   . LEU   A 1 70  ? -19.15000 -25.84000 13.06900  1.000 19.78082 ?  50  LEU   A CD1   1 
ATOM   376  C  CD2   . LEU   A 1 70  ? -19.29100 -24.66200 15.30000  1.000 21.13035 ?  50  LEU   A CD2   1 
ATOM   377  N  N     . ASP   A 1 71  ? -16.30600 -23.80000 11.36000  1.000 17.91207 ?  51  ASP   A N     1 
ATOM   378  C  CA    . ASP   A 1 71  ? -16.15500 -22.53000 10.64400  1.000 20.27455 ?  51  ASP   A CA    1 
ATOM   379  C  C     . ASP   A 1 71  ? -17.55200 -21.95400 10.46700  1.000 17.40210 ?  51  ASP   A C     1 
ATOM   380  O  O     . ASP   A 1 71  ? -18.30200 -22.41500 9.59700   1.000 18.71801 ?  51  ASP   A O     1 
ATOM   381  C  CB    . ASP   A 1 71  ? -15.45000 -22.75500 9.29800   1.000 16.96124 ?  51  ASP   A CB    1 
ATOM   382  C  CG    . ASP   A 1 71  ? -15.14300 -21.45800 8.55200   1.000 23.28114 ?  51  ASP   A CG    1 
ATOM   383  O  OD1   . ASP   A 1 71  ? -15.55900 -20.38100 9.02300   1.000 21.06787 ?  51  ASP   A OD1   1 
ATOM   384  O  OD2   . ASP   A 1 71  ? -14.50900 -21.52000 7.46400   1.000 19.78773 -1 51  ASP   A OD2   1 
ATOM   385  N  N     . LEU   A 1 72  ? -17.90200 -20.96400 11.30400  1.000 16.54237 ?  52  LEU   A N     1 
ATOM   386  C  CA    . LEU   A 1 72  ? -19.24900 -20.39900 11.33900  1.000 15.99297 ?  52  LEU   A CA    1 
ATOM   387  C  C     . LEU   A 1 72  ? -19.32700 -19.15800 10.44300  1.000 18.62955 ?  52  LEU   A C     1 
ATOM   388  O  O     . LEU   A 1 72  ? -18.46300 -18.27200 10.52000  1.000 18.39127 ?  52  LEU   A O     1 
ATOM   389  C  CB    . LEU   A 1 72  ? -19.62900 -20.03300 12.77800  1.000 15.56605 ?  52  LEU   A CB    1 
ATOM   390  C  CG    . LEU   A 1 72  ? -19.81200 -21.24400 13.69800  1.000 20.33443 ?  52  LEU   A CG    1 
ATOM   391  C  CD1   . LEU   A 1 72  ? -20.13900 -20.82900 15.14400  1.000 18.48917 ?  52  LEU   A CD1   1 
ATOM   392  C  CD2   . LEU   A 1 72  ? -20.89200 -22.16300 13.11300  1.000 19.31580 ?  52  LEU   A CD2   1 
ATOM   393  N  N     . GLY   A 1 73  ? -20.37300 -19.07800 9.62200   1.000 16.01603 ?  53  GLY   A N     1 
ATOM   394  C  CA    . GLY   A 1 73  ? -20.41700 -18.02300 8.59900   1.000 17.78411 ?  53  GLY   A CA    1 
ATOM   395  C  C     . GLY   A 1 73  ? -19.33300 -18.20400 7.55200   1.000 21.74595 ?  53  GLY   A C     1 
ATOM   396  O  O     . GLY   A 1 73  ? -18.69300 -17.22500 7.14100   1.000 20.64039 ?  53  GLY   A O     1 
ATOM   397  N  N     . CYS   A 1 74  ? -19.09600 -19.44600 7.12700   1.000 18.24315 ?  54  CYS   A N     1 
ATOM   398  C  CA    . CYS   A 1 74  ? -17.95100 -19.78700 6.30200   1.000 16.98636 ?  54  CYS   A CA    1 
ATOM   399  C  C     . CYS   A 1 74  ? -18.04300 -19.24800 4.87500   1.000 21.07142 ?  54  CYS   A C     1 
ATOM   400  O  O     . CYS   A 1 74  ? -17.04300 -19.32400 4.15300   1.000 19.66548 ?  54  CYS   A O     1 
ATOM   401  C  CB    . CYS   A 1 74  ? -17.79200 -21.30900 6.24700   1.000 20.25312 ?  54  CYS   A CB    1 
ATOM   402  S  SG    . CYS   A 1 74  ? -19.20500 -22.15800 5.43800   1.000 21.26791 ?  54  CYS   A SG    1 
ATOM   403  N  N     . ALA   A 1 75  ? -19.19400 -18.72600 4.44100   1.000 16.06545 ?  55  ALA   A N     1 
ATOM   404  C  CA    . ALA   A 1 75  ? -19.38200 -18.23900 3.03200   1.000 17.53402 ?  55  ALA   A CA    1 
ATOM   405  C  C     . ALA   A 1 75  ? -18.97100 -19.33700 2.04700   1.000 18.90359 ?  55  ALA   A C     1 
ATOM   406  O  O     . ALA   A 1 75  ? -19.45600 -20.47000 2.16400   1.000 20.35483 ?  55  ALA   A O     1 
ATOM   407  C  CB    . ALA   A 1 75  ? -18.65300 -16.91600 2.84800   1.000 16.60678 ?  55  ALA   A CB    1 
ATOM   408  N  N     . VAL   A 1 76  ? -18.10400 -19.05600 1.05800   1.000 17.10229 ?  56  VAL   A N     1 
ATOM   409  C  CA    . VAL   A 1 76  ? -17.79400 -20.02900 0.01100   1.000 18.29308 ?  56  VAL   A CA    1 
ATOM   410  C  C     . VAL   A 1 76  ? -16.56400 -20.86400 0.36400   1.000 22.18420 ?  56  VAL   A C     1 
ATOM   411  O  O     . VAL   A 1 76  ? -16.05200 -21.61700 -0.47500  1.000 21.08479 ?  56  VAL   A O     1 
ATOM   412  C  CB    . VAL   A 1 76  ? -17.60700 -19.33800 -1.35300  1.000 17.07858 ?  56  VAL   A CB    1 
ATOM   413  C  CG1   . VAL   A 1 76  ? -18.95600 -18.75100 -1.82800  1.000 18.23105 ?  56  VAL   A CG1   1 
ATOM   414  C  CG2   . VAL   A 1 76  ? -16.53100 -18.27000 -1.25300  1.000 17.20915 ?  56  VAL   A CG2   1 
ATOM   415  N  N     . GLY   A 1 77  ? -16.07900 -20.74500 1.59600   1.000 17.84408 ?  57  GLY   A N     1 
ATOM   416  C  CA    . GLY   A 1 77  ? -15.33900 -21.84000 2.20600   1.000 20.01779 ?  57  GLY   A CA    1 
ATOM   417  C  C     . GLY   A 1 77  ? -13.82300 -21.78300 2.27700   1.000 17.54208 ?  57  GLY   A C     1 
ATOM   418  O  O     . GLY   A 1 77  ? -13.22500 -22.77700 2.71300   1.000 19.11708 ?  57  GLY   A O     1 
ATOM   419  N  N     . ARG   A 1 78  ? -13.16900 -20.66300 1.91300   1.000 15.88519 ?  58  ARG   A N     1 
ATOM   420  C  CA    . ARG   A 1 78  ? -11.70000 -20.65800 1.91700   1.000 18.03655 ?  58  ARG   A CA    1 
ATOM   421  C  C     . ARG   A 1 78  ? -11.11800 -20.95600 3.30600   1.000 17.82081 ?  58  ARG   A C     1 
ATOM   422  O  O     . ARG   A 1 78  ? -10.11900 -21.67500 3.41600   1.000 18.05761 ?  58  ARG   A O     1 
ATOM   423  C  CB    . ARG   A 1 78  ? -11.15200 -19.32000 1.39500   1.000 18.46765 ?  58  ARG   A CB    1 
ATOM   424  C  CG    . ARG   A 1 78  ? -9.60300  -19.20500 1.39000   1.000 20.88666 ?  58  ARG   A CG    1 
ATOM   425  C  CD    . ARG   A 1 78  ? -8.91200  -20.18600 0.40700   1.000 21.10898 ?  58  ARG   A CD    1 
ATOM   426  N  NE    . ARG   A 1 78  ? -7.45700  -20.04500 0.39900   1.000 22.39930 ?  58  ARG   A NE    1 
ATOM   427  C  CZ    . ARG   A 1 78  ? -6.79400  -19.24200 -0.42200  1.000 22.10045 ?  58  ARG   A CZ    1 
ATOM   428  N  NH1   . ARG   A 1 78  ? -7.42600  -18.45700 -1.28000  1.000 22.97519 ?  58  ARG   A NH1   1 
ATOM   429  N  NH2   . ARG   A 1 78  ? -5.46400  -19.21300 -0.37700  1.000 19.05356 ?  58  ARG   A NH2   1 
ATOM   430  N  N     . SER   A 1 79  ? -11.68500 -20.37400 4.36800   1.000 18.68800 ?  59  SER   A N     1 
ATOM   431  C  CA    . SER   A 1 79  ? -11.12800 -20.64100 5.69900   1.000 18.66990 ?  59  SER   A CA    1 
ATOM   432  C  C     . SER   A 1 79  ? -11.35400 -22.09900 6.10300   1.000 19.84176 ?  59  SER   A C     1 
ATOM   433  O  O     . SER   A 1 79  ? -10.55600 -22.66900 6.85900   1.000 19.28457 ?  59  SER   A O     1 
ATOM   434  C  CB    . SER   A 1 79  ? -11.72200 -19.68600 6.73900   1.000 19.42553 ?  59  SER   A CB    1 
ATOM   435  O  OG    . SER   A 1 79  ? -13.12200 -19.54700 6.56500   1.000 24.46052 ?  59  SER   A OG    1 
ATOM   436  N  N     . SER   A 1 80  ? -12.42700 -22.72100 5.61400   1.000 18.17013 ?  60  SER   A N     1 
ATOM   437  C  CA    . SER   A 1 80  ? -12.66700 -24.11400 5.95500   1.000 19.45445 ?  60  SER   A CA    1 
ATOM   438  C  C     . SER   A 1 80  ? -11.63400 -25.01600 5.29200   1.000 18.83294 ?  60  SER   A C     1 
ATOM   439  O  O     . SER   A 1 80  ? -11.10500 -25.93500 5.93200   1.000 19.64438 ?  60  SER   A O     1 
ATOM   440  C  CB    . SER   A 1 80  ? -14.08500 -24.52700 5.54800   1.000 27.09987 ?  60  SER   A CB    1 
ATOM   441  O  OG    . SER   A 1 80  ? -15.06700 -23.75400 6.21900   1.000 23.09845 ?  60  SER   A OG    1 
ATOM   442  N  N     . PHE   A 1 81  ? -11.33800 -24.76600 4.01200   1.000 18.58999 ?  61  PHE   A N     1 
ATOM   443  C  CA    . PHE   A 1 81  ? -10.30100 -25.53900 3.33700   1.000 16.75345 ?  61  PHE   A CA    1 
ATOM   444  C  C     . PHE   A 1 81  ? -8.93100  -25.29000 3.95400   1.000 19.83948 ?  61  PHE   A C     1 
ATOM   445  O  O     . PHE   A 1 81  ? -8.10600  -26.20900 4.01100   1.000 21.55787 ?  61  PHE   A O     1 
ATOM   446  C  CB    . PHE   A 1 81  ? -10.28800 -25.21600 1.83600   1.000 18.45508 ?  61  PHE   A CB    1 
ATOM   447  C  CG    . PHE   A 1 81  ? -11.51000 -25.72900 1.09300   1.000 20.28468 ?  61  PHE   A CG    1 
ATOM   448  C  CD1   . PHE   A 1 81  ? -11.83800 -27.08600 1.09700   1.000 22.30654 ?  61  PHE   A CD1   1 
ATOM   449  C  CD2   . PHE   A 1 81  ? -12.33500 -24.84600 0.40400   1.000 20.62507 ?  61  PHE   A CD2   1 
ATOM   450  C  CE1   . PHE   A 1 81  ? -12.97100 -27.56600 0.42300   1.000 21.38246 ?  61  PHE   A CE1   1 
ATOM   451  C  CE2   . PHE   A 1 81  ? -13.46000 -25.30400 -0.28400  1.000 19.18313 ?  61  PHE   A CE2   1 
ATOM   452  C  CZ    . PHE   A 1 81  ? -13.78000 -26.66700 -0.27900  1.000 24.75517 ?  61  PHE   A CZ    1 
ATOM   453  N  N     . GLU   A 1 82  ? -8.65900  -24.06800 4.42300   1.000 19.36267 ?  62  GLU   A N     1 
ATOM   454  C  CA    . GLU   A 1 82  ? -7.37400  -23.81800 5.07500   1.000 19.70340 ?  62  GLU   A CA    1 
ATOM   455  C  C     . GLU   A 1 82  ? -7.28900  -24.57300 6.40100   1.000 24.65469 ?  62  GLU   A C     1 
ATOM   456  O  O     . GLU   A 1 82  ? -6.23600  -25.12400 6.74600   1.000 23.42381 ?  62  GLU   A O     1 
ATOM   457  C  CB    . GLU   A 1 82  ? -7.16900  -22.31400 5.30600   1.000 20.40829 ?  62  GLU   A CB    1 
ATOM   458  C  CG    . GLU   A 1 82  ? -7.04300  -21.47700 3.99400   1.000 17.82898 ?  62  GLU   A CG    1 
ATOM   459  C  CD    . GLU   A 1 82  ? -5.69600  -21.64800 3.32500   1.000 27.56038 ?  62  GLU   A CD    1 
ATOM   460  O  OE1   . GLU   A 1 82  ? -4.75100  -22.12700 3.98900   1.000 23.92828 ?  62  GLU   A OE1   1 
ATOM   461  O  OE2   . GLU   A 1 82  ? -5.58400  -21.32900 2.11800   1.000 24.01604 -1 62  GLU   A OE2   1 
ATOM   462  N  N     . LEU   A 1 83  ? -8.38500  -24.59900 7.16600   1.000 18.14412 ?  63  LEU   A N     1 
ATOM   463  C  CA    . LEU   A 1 83  ? -8.37600  -25.32700 8.43400   1.000 18.86137 ?  63  LEU   A CA    1 
ATOM   464  C  C     . LEU   A 1 83  ? -8.18100  -26.81500 8.19500   1.000 22.91344 ?  63  LEU   A C     1 
ATOM   465  O  O     . LEU   A 1 83  ? -7.59000  -27.51000 9.03200   1.000 23.44171 ?  63  LEU   A O     1 
ATOM   466  C  CB    . LEU   A 1 83  ? -9.68300  -25.11600 9.18600   1.000 18.75212 ?  63  LEU   A CB    1 
ATOM   467  C  CG    . LEU   A 1 83  ? -9.80300  -23.80800 9.96900   1.000 19.69645 ?  63  LEU   A CG    1 
ATOM   468  C  CD1   . LEU   A 1 83  ? -11.26800 -23.61500 10.34300  1.000 18.24309 ?  63  LEU   A CD1   1 
ATOM   469  C  CD2   . LEU   A 1 83  ? -8.93100  -23.79000 11.25000  1.000 20.35538 ?  63  LEU   A CD2   1 
ATOM   470  N  N     . ALA   A 1 84  ? -8.69000  -27.31800 7.07000   1.000 21.81694 ?  64  ALA   A N     1 
ATOM   471  C  CA    . ALA   A 1 84  ? -8.59800  -28.74100 6.76600   1.000 20.69620 ?  64  ALA   A CA    1 
ATOM   472  C  C     . ALA   A 1 84  ? -7.17100  -29.18100 6.46200   1.000 26.33295 ?  64  ALA   A C     1 
ATOM   473  O  O     . ALA   A 1 84  ? -6.89500  -30.39400 6.46500   1.000 25.72200 ?  64  ALA   A O     1 
ATOM   474  C  CB    . ALA   A 1 84  ? -9.51400  -29.08000 5.60000   1.000 23.80878 ?  64  ALA   A CB    1 
ATOM   475  N  N     . ARG   A 1 85  ? -6.25300  -28.24300 6.20900   1.000 22.01264 ?  65  ARG   A N     1 
ATOM   476  C  CA    . ARG   A 1 85  ? -4.86400  -28.66800 6.09800   1.000 28.05771 ?  65  ARG   A CA    1 
ATOM   477  C  C     . ARG   A 1 85  ? -4.33100  -29.21800 7.41200   1.000 28.49570 ?  65  ARG   A C     1 
ATOM   478  O  O     . ARG   A 1 85  ? -3.34000  -29.95300 7.39300   1.000 29.41425 ?  65  ARG   A O     1 
ATOM   479  C  CB    . ARG   A 1 85  ? -3.96200  -27.53300 5.61700   1.000 30.75325 ?  65  ARG   A CB    1 
ATOM   480  C  CG    . ARG   A 1 85  ? -4.37900  -26.93100 4.28300   1.000 34.14664 ?  65  ARG   A CG    1 
ATOM   481  C  CD    . ARG   A 1 85  ? -3.42400  -25.80900 3.83200   1.000 42.75242 ?  65  ARG   A CD    1 
ATOM   482  N  NE    . ARG   A 1 85  ? -2.07400  -26.31200 3.59900   1.000 50.30363 ?  65  ARG   A NE    1 
ATOM   483  C  CZ    . ARG   A 1 85  ? -1.70900  -27.00500 2.52800   1.000 48.78448 ?  65  ARG   A CZ    1 
ATOM   484  N  N     . ARG   A 1 86  ? -4.95800  -28.88700 8.55200   1.000 21.22059 ?  66  ARG   A N     1 
ATOM   485  C  CA    . ARG   A 1 86  ? -4.44500  -29.31700 9.85300   1.000 24.66914 ?  66  ARG   A CA    1 
ATOM   486  C  C     . ARG   A 1 86  ? -5.43000  -30.12400 10.69900  1.000 27.25069 ?  66  ARG   A C     1 
ATOM   487  O  O     . ARG   A 1 86  ? -4.98900  -30.97100 11.48200  1.000 31.11277 ?  66  ARG   A O     1 
ATOM   488  C  CB    . ARG   A 1 86  ? -3.96900  -28.09300 10.66000  1.000 25.10657 ?  66  ARG   A CB    1 
ATOM   489  N  N     . PHE   A 1 87  ? -6.73800  -29.90600 10.56500  1.000 22.33021 ?  67  PHE   A N     1 
ATOM   490  C  CA    . PHE   A 1 87  ? -7.73500  -30.59400 11.37700  1.000 19.73864 ?  67  PHE   A CA    1 
ATOM   491  C  C     . PHE   A 1 87  ? -8.28100  -31.82700 10.65000  1.000 24.80073 ?  67  PHE   A C     1 
ATOM   492  O  O     . PHE   A 1 87  ? -8.42500  -31.82900 9.42700   1.000 23.17409 ?  67  PHE   A O     1 
ATOM   493  C  CB    . PHE   A 1 87  ? -8.86900  -29.62600 11.72400  1.000 20.31888 ?  67  PHE   A CB    1 
ATOM   494  C  CG    . PHE   A 1 87  ? -8.50000  -28.66400 12.82800  1.000 21.95814 ?  67  PHE   A CG    1 
ATOM   495  C  CD1   . PHE   A 1 87  ? -7.81400  -27.48400 12.53900  1.000 20.81748 ?  67  PHE   A CD1   1 
ATOM   496  C  CD2   . PHE   A 1 87  ? -8.76500  -28.97800 14.16600  1.000 22.24711 ?  67  PHE   A CD2   1 
ATOM   497  C  CE1   . PHE   A 1 87  ? -7.44500  -26.60300 13.57300  1.000 20.54620 ?  67  PHE   A CE1   1 
ATOM   498  C  CE2   . PHE   A 1 87  ? -8.40400  -28.11900 15.20000  1.000 19.53818 ?  67  PHE   A CE2   1 
ATOM   499  C  CZ    . PHE   A 1 87  ? -7.73700  -26.92400 14.90600  1.000 21.32184 ?  67  PHE   A CZ    1 
ATOM   500  N  N     . ASP   A 1 88  ? -8.59600  -32.88600 11.41500  1.000 22.41831 ?  68  ASP   A N     1 
ATOM   501  C  CA    . ASP   A 1 88  ? -9.06400  -34.12000 10.77600  1.000 22.97688 ?  68  ASP   A CA    1 
ATOM   502  C  C     . ASP   A 1 88  ? -10.44300 -33.95400 10.15100  1.000 22.26115 ?  68  ASP   A C     1 
ATOM   503  O  O     . ASP   A 1 88  ? -10.75800 -34.63100 9.16800   1.000 21.47792 ?  68  ASP   A O     1 
ATOM   504  C  CB    . ASP   A 1 88  ? -9.09700  -35.28900 11.77800  1.000 26.61889 ?  68  ASP   A CB    1 
ATOM   505  C  CG    . ASP   A 1 88  ? -7.73700  -35.56400 12.42000  1.000 27.62291 ?  68  ASP   A CG    1 
ATOM   506  O  OD1   . ASP   A 1 88  ? -6.69400  -35.28800 11.79000  1.000 30.56350 ?  68  ASP   A OD1   1 
ATOM   507  O  OD2   . ASP   A 1 88  ? -7.71500  -36.08200 13.55800  1.000 32.17165 -1 68  ASP   A OD2   1 
ATOM   508  N  N     . GLU   A 1 89  ? -11.27100 -33.07600 10.72000  1.000 23.25212 ?  69  GLU   A N     1 
ATOM   509  C  CA    . GLU   A 1 89  ? -12.63500 -32.81600 10.27900  1.000 23.76055 ?  69  GLU   A CA    1 
ATOM   510  C  C     . GLU   A 1 89  ? -12.92000 -31.33000 10.44800  1.000 23.05430 ?  69  GLU   A C     1 
ATOM   511  O  O     . GLU   A 1 89  ? -12.65800 -30.76600 11.51700  1.000 19.50977 ?  69  GLU   A O     1 
ATOM   512  C  CB    . GLU   A 1 89  ? -13.66200 -33.61300 11.09600  1.000 19.72828 ?  69  GLU   A CB    1 
ATOM   513  C  CG    . GLU   A 1 89  ? -15.08000 -33.34100 10.65500  1.000 23.62767 ?  69  GLU   A CG    1 
ATOM   514  C  CD    . GLU   A 1 89  ? -16.12600 -34.14600 11.40600  1.000 28.19511 ?  69  GLU   A CD    1 
ATOM   515  O  OE1   . GLU   A 1 89  ? -16.04700 -34.27000 12.64200  1.000 27.34849 ?  69  GLU   A OE1   1 
ATOM   516  O  OE2   . GLU   A 1 89  ? -17.02300 -34.69500 10.73300  1.000 29.99808 -1 69  GLU   A OE2   1 
ATOM   517  N  N     . VAL   A 1 90  ? -13.47200 -30.70800 9.41000   1.000 21.36727 ?  70  VAL   A N     1 
ATOM   518  C  CA    . VAL   A 1 90  ? -13.84100 -29.29900 9.43600   1.000 17.98491 ?  70  VAL   A CA    1 
ATOM   519  C  C     . VAL   A 1 90  ? -15.28200 -29.19600 8.97900   1.000 18.26283 ?  70  VAL   A C     1 
ATOM   520  O  O     . VAL   A 1 90  ? -15.61700 -29.67400 7.88800   1.000 19.87907 ?  70  VAL   A O     1 
ATOM   521  C  CB    . VAL   A 1 90  ? -12.93500 -28.44500 8.53900   1.000 22.00634 ?  70  VAL   A CB    1 
ATOM   522  C  CG1   . VAL   A 1 90  ? -13.40000 -26.96700 8.58900   1.000 20.44426 ?  70  VAL   A CG1   1 
ATOM   523  C  CG2   . VAL   A 1 90  ? -11.50100 -28.56900 9.00500   1.000 21.94720 ?  70  VAL   A CG2   1 
ATOM   524  N  N     . ILE   A 1 91  ? -16.12900 -28.59500 9.81000   1.000 19.56429 ?  71  ILE   A N     1 
ATOM   525  C  CA    . ILE   A 1 91  ? -17.53100 -28.33900 9.48300   1.000 20.21616 ?  71  ILE   A CA    1 
ATOM   526  C  C     . ILE   A 1 91  ? -17.66700 -26.85300 9.19200   1.000 19.63684 ?  71  ILE   A C     1 
ATOM   527  O  O     . ILE   A 1 91  ? -17.34600 -26.03400 10.05300  1.000 18.58307 ?  71  ILE   A O     1 
ATOM   528  C  CB    . ILE   A 1 91  ? -18.48100 -28.72500 10.62500  1.000 21.74340 ?  71  ILE   A CB    1 
ATOM   529  C  CG1   . ILE   A 1 91  ? -18.24000 -30.16400 11.10500  1.000 27.93759 ?  71  ILE   A CG1   1 
ATOM   530  C  CG2   . ILE   A 1 91  ? -19.93300 -28.48900 10.20500  1.000 25.06765 ?  71  ILE   A CG2   1 
ATOM   531  C  CD1   . ILE   A 1 91  ? -18.47900 -31.15000 10.04700  1.000 29.79629 ?  71  ILE   A CD1   1 
ATOM   532  N  N     . GLY   A 1 92  ? -18.16600 -26.50400 8.00600   1.000 19.73130 ?  72  GLY   A N     1 
ATOM   533  C  CA    . GLY   A 1 92  ? -18.46400 -25.11100 7.66100   1.000 16.55663 ?  72  GLY   A CA    1 
ATOM   534  C  C     . GLY   A 1 92  ? -19.96500 -24.90100 7.53400   1.000 20.34377 ?  72  GLY   A C     1 
ATOM   535  O  O     . GLY   A 1 92  ? -20.64800 -25.64500 6.82900   1.000 21.76077 ?  72  GLY   A O     1 
ATOM   536  N  N     . ILE   A 1 93  ? -20.47200 -23.90100 8.25100   1.000 19.71944 ?  73  ILE   A N     1 
ATOM   537  C  CA    . ILE   A 1 93  ? -21.90300 -23.60200 8.30900   1.000 18.84116 ?  73  ILE   A CA    1 
ATOM   538  C  C     . ILE   A 1 93  ? -22.11800 -22.16700 7.84700   1.000 18.78674 ?  73  ILE   A C     1 
ATOM   539  O  O     . ILE   A 1 93  ? -21.41500 -21.25500 8.29100   1.000 17.80018 ?  73  ILE   A O     1 
ATOM   540  C  CB    . ILE   A 1 93  ? -22.47400 -23.81600 9.72800   1.000 19.13289 ?  73  ILE   A CB    1 
ATOM   541  C  CG1   . ILE   A 1 93  ? -22.29000 -25.27800 10.13900  1.000 20.00180 ?  73  ILE   A CG1   1 
ATOM   542  C  CG2   . ILE   A 1 93  ? -23.94600 -23.44900 9.79400   1.000 22.37265 ?  73  ILE   A CG2   1 
ATOM   543  C  CD1   . ILE   A 1 93  ? -22.65400 -25.59700 11.58300  1.000 24.41729 ?  73  ILE   A CD1   1 
ATOM   544  N  N     . ASP   A 1 94  ? -23.06800 -21.98100 6.93200   1.000 18.79712 ?  74  ASP   A N     1 
ATOM   545  C  CA    . ASP   A 1 94  ? -23.45700 -20.65800 6.47700   1.000 21.17863 ?  74  ASP   A CA    1 
ATOM   546  C  C     . ASP   A 1 94  ? -24.94100 -20.71300 6.19800   1.000 20.84196 ?  74  ASP   A C     1 
ATOM   547  O  O     . ASP   A 1 94  ? -25.47000 -21.76400 5.81900   1.000 20.92042 ?  74  ASP   A O     1 
ATOM   548  C  CB    . ASP   A 1 94  ? -22.71000 -20.21300 5.20300   1.000 16.13719 ?  74  ASP   A CB    1 
ATOM   549  C  CG    . ASP   A 1 94  ? -22.67200 -18.69900 5.04700   1.000 20.53656 ?  74  ASP   A CG    1 
ATOM   550  O  OD1   . ASP   A 1 94  ? -23.62700 -18.12400 4.46700   1.000 21.00373 ?  74  ASP   A OD1   1 
ATOM   551  O  OD2   . ASP   A 1 94  ? -21.68900 -18.08600 5.52300   1.000 18.90087 -1 74  ASP   A OD2   1 
ATOM   552  N  N     . LEU   A 1 95  ? -25.59600 -19.57100 6.37300   1.000 20.26780 ?  75  LEU   A N     1 
ATOM   553  C  CA    . LEU   A 1 95  ? -27.01900 -19.44000 6.09000   1.000 21.69261 ?  75  LEU   A CA    1 
ATOM   554  C  C     . LEU   A 1 95  ? -27.32500 -19.32900 4.59400   1.000 22.88426 ?  75  LEU   A C     1 
ATOM   555  O  O     . LEU   A 1 95  ? -28.46000 -19.60300 4.18700   1.000 22.55801 ?  75  LEU   A O     1 
ATOM   556  C  CB    . LEU   A 1 95  ? -27.56700 -18.21700 6.83700   1.000 21.03581 ?  75  LEU   A CB    1 
ATOM   557  C  CG    . LEU   A 1 95  ? -29.08600 -18.07800 6.93400   1.000 24.99553 ?  75  LEU   A CG    1 
ATOM   558  C  CD1   . LEU   A 1 95  ? -29.66000 -19.14100 7.82400   1.000 28.79293 ?  75  LEU   A CD1   1 
ATOM   559  C  CD2   . LEU   A 1 95  ? -29.48900 -16.68700 7.41600   1.000 28.66034 ?  75  LEU   A CD2   1 
ATOM   560  N  N     . SER   A 1 96  ? -26.35100 -18.97000 3.76300   1.000 20.60768 ?  76  SER   A N     1 
ATOM   561  C  CA    . SER   A 1 96  ? -26.58300 -18.79500 2.32200   1.000 19.70390 ?  76  SER   A CA    1 
ATOM   562  C  C     . SER   A 1 96  ? -26.44900 -20.12400 1.58800   1.000 24.58818 ?  76  SER   A C     1 
ATOM   563  O  O     . SER   A 1 96  ? -25.36400 -20.71400 1.55700   1.000 21.43638 ?  76  SER   A O     1 
ATOM   564  C  CB    . SER   A 1 96  ? -25.60600 -17.78900 1.73100   1.000 17.38640 ?  76  SER   A CB    1 
ATOM   565  O  OG    . SER   A 1 96  ? -25.68900 -17.81800 0.30200   1.000 21.67982 ?  76  SER   A OG    1 
ATOM   566  N  N     . ARG   A 1 97  ? -27.55000 -20.59200 0.99600   1.000 22.41416 ?  77  ARG   A N     1 
ATOM   567  C  CA    . ARG   A 1 97  ? -27.50000 -21.83700 0.23400   1.000 22.73606 ?  77  ARG   A CA    1 
ATOM   568  C  C     . ARG   A 1 97  ? -26.66400 -21.66600 -1.03200  1.000 20.47863 ?  77  ARG   A C     1 
ATOM   569  O  O     . ARG   A 1 97  ? -25.90200 -22.57000 -1.40600  1.000 25.35414 ?  77  ARG   A O     1 
ATOM   570  C  CB    . ARG   A 1 97  ? -28.91200 -22.31100 -0.11600  1.000 27.24538 ?  77  ARG   A CB    1 
ATOM   571  C  CG    . ARG   A 1 97  ? -28.88000 -23.67300 -0.82200  1.000 30.58488 ?  77  ARG   A CG    1 
ATOM   572  C  CD    . ARG   A 1 97  ? -30.18200 -24.46000 -0.72000  1.000 34.70631 ?  77  ARG   A CD    1 
ATOM   573  N  NE    . ARG   A 1 97  ? -30.59800 -24.78000 0.64000   1.000 39.32062 ?  77  ARG   A NE    1 
ATOM   574  C  CZ    . ARG   A 1 97  ? -30.20000 -25.84600 1.31900   1.000 37.17987 ?  77  ARG   A CZ    1 
ATOM   575  N  NH1   . ARG   A 1 97  ? -29.22400 -26.62100 0.87800   1.000 42.41142 ?  77  ARG   A NH1   1 
ATOM   576  N  NH2   . ARG   A 1 97  ? -30.78100 -26.12700 2.48200   1.000 36.54013 ?  77  ARG   A NH2   1 
ATOM   577  N  N     . ARG   A 1 98  ? -26.75700 -20.51400 -1.67600  1.000 23.58582 ?  78  ARG   A N     1 
ATOM   578  C  CA    . ARG   A 1 98  ? -25.92300 -20.28000 -2.88200  1.000 21.63040 ?  78  ARG   A CA    1 
ATOM   579  C  C     . ARG   A 1 98  ? -24.44300 -20.36700 -2.50100  1.000 28.53834 ?  78  ARG   A C     1 
ATOM   580  O  O     . ARG   A 1 98  ? -23.67300 -20.94900 -3.27000  1.000 22.66775 ?  78  ARG   A O     1 
ATOM   581  C  CB    . ARG   A 1 98  ? -26.25500 -18.94700 -3.55900  1.000 24.09395 ?  78  ARG   A CB    1 
ATOM   582  C  CG    . ARG   A 1 98  ? -25.91000 -18.89000 -5.03800  1.000 29.58527 ?  78  ARG   A CG    1 
ATOM   583  C  CD    . ARG   A 1 98  ? -26.42100 -17.59800 -5.63600  1.000 23.97177 ?  78  ARG   A CD    1 
ATOM   584  N  NE    . ARG   A 1 98  ? -26.89000 -17.72200 -7.00300  1.000 41.89977 ?  78  ARG   A NE    1 
ATOM   585  C  CZ    . ARG   A 1 98  ? -27.83800 -18.55300 -7.41500  1.000 27.53352 ?  78  ARG   A CZ    1 
ATOM   586  N  NH1   . ARG   A 1 98  ? -29.02300 -18.55700 -6.83600  1.000 30.84767 ?  78  ARG   A NH1   1 
ATOM   587  N  NH2   . ARG   A 1 98  ? -27.60500 -19.35800 -8.43300  1.000 30.63091 ?  78  ARG   A NH2   1 
ATOM   588  N  N     . PHE   A 1 99  ? -24.06300 -19.77500 -1.36900  1.000 23.19107 ?  79  PHE   A N     1 
ATOM   589  C  CA    . PHE   A 1 99  ? -22.67400 -19.88000 -0.91400  1.000 21.54912 ?  79  PHE   A CA    1 
ATOM   590  C  C     . PHE   A 1 99  ? -22.29900 -21.33000 -0.65800  1.000 23.28180 ?  79  PHE   A C     1 
ATOM   591  O  O     . PHE   A 1 99  ? -21.24800 -21.80400 -1.11100  1.000 21.19309 ?  79  PHE   A O     1 
ATOM   592  C  CB    . PHE   A 1 99  ? -22.43900 -19.07300 0.37700   1.000 19.53329 ?  79  PHE   A CB    1 
ATOM   593  C  CG    . PHE   A 1 99  ? -22.26900 -17.58900 0.17000   1.000 20.56892 ?  79  PHE   A CG    1 
ATOM   594  C  CD1   . PHE   A 1 99  ? -22.28100 -17.03500 -1.09200  1.000 19.62073 ?  79  PHE   A CD1   1 
ATOM   595  C  CD2   . PHE   A 1 99  ? -22.08800 -16.73500 1.28800   1.000 18.61753 ?  79  PHE   A CD2   1 
ATOM   596  C  CE1   . PHE   A 1 99  ? -22.11600 -15.67200 -1.27600  1.000 20.49905 ?  79  PHE   A CE1   1 
ATOM   597  C  CE2   . PHE   A 1 99  ? -21.91100 -15.37700 1.11800   1.000 20.09815 ?  79  PHE   A CE2   1 
ATOM   598  C  CZ    . PHE   A 1 99  ? -21.92100 -14.83800 -0.18000  1.000 22.19174 ?  79  PHE   A CZ    1 
ATOM   599  N  N     . ILE   A 1 100 ? -23.14600 -22.04800 0.08600   1.000 18.74647 ?  80  ILE   A N     1 
ATOM   600  C  CA    . ILE   A 1 100 ? -22.79300 -23.40300 0.47300   1.000 20.32605 ?  80  ILE   A CA    1 
ATOM   601  C  C     . ILE   A 1 100 ? -22.75700 -24.31100 -0.75100  1.000 24.18132 ?  80  ILE   A C     1 
ATOM   602  O  O     . ILE   A 1 100 ? -21.94700 -25.24500 -0.81100  1.000 22.35056 ?  80  ILE   A O     1 
ATOM   603  C  CB    . ILE   A 1 100 ? -23.75700 -23.93400 1.55200   1.000 19.47901 ?  80  ILE   A CB    1 
ATOM   604  C  CG1   . ILE   A 1 100 ? -23.54300 -23.20900 2.90300   1.000 19.48327 ?  80  ILE   A CG1   1 
ATOM   605  C  CG2   . ILE   A 1 100 ? -23.69400 -25.46100 1.65500   1.000 22.89359 ?  80  ILE   A CG2   1 
ATOM   606  C  CD1   . ILE   A 1 100 ? -22.17300 -23.42400 3.56100   1.000 24.15601 ?  80  ILE   A CD1   1 
ATOM   607  N  N     . ASP   A 1 101 ? -23.58600 -24.04000 -1.76700  1.000 24.55308 ?  81  ASP   A N     1 
ATOM   608  C  CA    . ASP   A 1 101 ? -23.50900 -24.88400 -2.96100  1.000 27.51596 ?  81  ASP   A CA    1 
ATOM   609  C  C     . ASP   A 1 101 ? -22.18800 -24.67300 -3.69100  1.000 24.34685 ?  81  ASP   A C     1 
ATOM   610  O  O     . ASP   A 1 101 ? -21.63700 -25.62100 -4.25300  1.000 23.95190 ?  81  ASP   A O     1 
ATOM   611  C  CB    . ASP   A 1 101 ? -24.68500 -24.62000 -3.91800  1.000 28.37238 ?  81  ASP   A CB    1 
ATOM   612  C  CG    . ASP   A 1 101 ? -26.00700 -25.25400 -3.45400  1.000 25.23458 ?  81  ASP   A CG    1 
ATOM   613  O  OD1   . ASP   A 1 101 ? -25.99600 -26.18700 -2.63600  1.000 27.10405 ?  81  ASP   A OD1   1 
ATOM   614  O  OD2   . ASP   A 1 101 ? -27.07300 -24.80900 -3.93800  1.000 30.09080 -1 81  ASP   A OD2   1 
ATOM   615  N  N     . SER   A 1 102 ? -21.65100 -23.45200 -3.66700  1.000 21.66757 ?  82  SER   A N     1 
ATOM   616  C  CA    . SER   A 1 102 ? -20.33600 -23.21300 -4.25500  1.000 20.82308 ?  82  SER   A CA    1 
ATOM   617  C  C     . SER   A 1 102 ? -19.24100 -23.92600 -3.46600  1.000 21.08448 ?  82  SER   A C     1 
ATOM   618  O  O     . SER   A 1 102 ? -18.36100 -24.57300 -4.05600  1.000 21.84705 ?  82  SER   A O     1 
ATOM   619  C  CB    . SER   A 1 102 ? -20.05900 -21.71100 -4.34000  1.000 23.24631 ?  82  SER   A CB    1 
ATOM   620  O  OG    . SER   A 1 102 ? -20.62900 -21.15600 -5.51600  1.000 30.27412 ?  82  SER   A OG    1 
ATOM   621  N  N     . ALA   A 1 103 ? -19.26400 -23.80400 -2.12900  1.000 20.44475 ?  83  ALA   A N     1 
ATOM   622  C  CA    . ALA   A 1 103 ? -18.25200 -24.46700 -1.30600  1.000 18.15351 ?  83  ALA   A CA    1 
ATOM   623  C  C     . ALA   A 1 103 ? -18.25300 -25.98000 -1.53500  1.000 21.42791 ?  83  ALA   A C     1 
ATOM   624  O  O     . ALA   A 1 103 ? -17.19300 -26.59400 -1.71500  1.000 21.51357 ?  83  ALA   A O     1 
ATOM   625  C  CB    . ALA   A 1 103 ? -18.47800 -24.13500 0.17700   1.000 19.79217 ?  83  ALA   A CB    1 
ATOM   626  N  N     . THR   A 1 104 ? -19.43600 -26.60100 -1.52500  1.000 20.94351 ?  84  THR   A N     1 
ATOM   627  C  CA    . THR   A 1 104 ? -19.53200 -28.04000 -1.78200  1.000 19.83090 ?  84  THR   A CA    1 
ATOM   628  C  C     . THR   A 1 104 ? -19.01600 -28.41700 -3.17700  1.000 23.51167 ?  84  THR   A C     1 
ATOM   629  O  O     . THR   A 1 104 ? -18.31200 -29.41700 -3.32100  1.000 22.16768 ?  84  THR   A O     1 
ATOM   630  C  CB    . THR   A 1 104 ? -20.97700 -28.50800 -1.57500  1.000 27.98478 ?  84  THR   A CB    1 
ATOM   631  O  OG1   . THR   A 1 104 ? -21.41000 -28.16300 -0.24500  1.000 27.01711 ?  84  THR   A OG1   1 
ATOM   632  C  CG2   . THR   A 1 104 ? -21.10800 -30.00500 -1.75900  1.000 23.91407 ?  84  THR   A CG2   1 
ATOM   633  N  N     . ARG   A 1 105 ? -19.33700 -27.63100 -4.21100  1.000 21.83993 ?  85  ARG   A N     1 
ATOM   634  C  CA    . ARG   A 1 105 ? -18.83200 -27.94600 -5.55400  1.000 17.22715 ?  85  ARG   A CA    1 
ATOM   635  C  C     . ARG   A 1 105 ? -17.31400 -27.91200 -5.58500  1.000 21.64244 ?  85  ARG   A C     1 
ATOM   636  O  O     . ARG   A 1 105 ? -16.66900 -28.76300 -6.21600  1.000 22.00359 ?  85  ARG   A O     1 
ATOM   637  C  CB    . ARG   A 1 105 ? -19.39800 -26.96600 -6.59200  1.000 19.56858 ?  85  ARG   A CB    1 
ATOM   638  C  CG    . ARG   A 1 105 ? -18.82000 -27.18500 -7.98900  1.000 19.67461 ?  85  ARG   A CG    1 
ATOM   639  C  CD    . ARG   A 1 105 ? -19.46200 -26.26400 -9.05500  1.000 20.75367 ?  85  ARG   A CD    1 
ATOM   640  N  NE    . ARG   A 1 105 ? -20.77900 -26.73500 -9.47400  1.000 24.29057 ?  85  ARG   A NE    1 
ATOM   641  C  CZ    . ARG   A 1 105 ? -20.99400 -27.68500 -10.37500 1.000 26.88462 ?  85  ARG   A CZ    1 
ATOM   642  N  NH1   . ARG   A 1 105 ? -19.99800 -28.25100 -11.04700 1.000 23.52653 ?  85  ARG   A NH1   1 
ATOM   643  N  NH2   . ARG   A 1 105 ? -22.24200 -28.07900 -10.60800 1.000 25.16115 ?  85  ARG   A NH2   1 
ATOM   644  N  N     . LEU   A 1 106 ? -16.71800 -26.93900 -4.89100  1.000 18.46265 ?  86  LEU   A N     1 
ATOM   645  C  CA    . LEU   A 1 106 ? -15.26700 -26.90200 -4.78700  1.000 20.16943 ?  86  LEU   A CA    1 
ATOM   646  C  C     . LEU   A 1 106 ? -14.75400 -28.14300 -4.06600  1.000 22.19613 ?  86  LEU   A C     1 
ATOM   647  O  O     . LEU   A 1 106 ? -13.78600 -28.77100 -4.50700  1.000 24.64743 ?  86  LEU   A O     1 
ATOM   648  C  CB    . LEU   A 1 106 ? -14.84000 -25.61600 -4.07100  1.000 21.65324 ?  86  LEU   A CB    1 
ATOM   649  C  CG    . LEU   A 1 106 ? -14.68900 -24.41400 -4.99400  1.000 21.59401 ?  86  LEU   A CG    1 
ATOM   650  C  CD1   . LEU   A 1 106 ? -14.66500 -23.07900 -4.18900  1.000 24.25889 ?  86  LEU   A CD1   1 
ATOM   651  C  CD2   . LEU   A 1 106 ? -13.42900 -24.59100 -5.86000  1.000 23.75394 ?  86  LEU   A CD2   1 
ATOM   652  N  N     . ALA   A 1 107 ? -15.41400 -28.53100 -2.97500  1.000 21.42253 ?  87  ALA   A N     1 
ATOM   653  C  CA    . ALA   A 1 107 ? -14.97400 -29.70300 -2.22200  1.000 22.16636 ?  87  ALA   A CA    1 
ATOM   654  C  C     . ALA   A 1 107 ? -15.02300 -30.95700 -3.08100  1.000 28.19377 ?  87  ALA   A C     1 
ATOM   655  O  O     . ALA   A 1 107 ? -14.12200 -31.79600 -3.01800  1.000 28.78736 ?  87  ALA   A O     1 
ATOM   656  C  CB    . ALA   A 1 107 ? -15.83400 -29.89900 -0.97200  1.000 25.18006 ?  87  ALA   A CB    1 
ATOM   657  N  N     . GLU   A 1 108 ? -16.07200 -31.10600 -3.88300  1.000 24.71873 ?  88  GLU   A N     1 
ATOM   658  C  CA    . GLU   A 1 108 ? -16.27500 -32.33800 -4.63400  1.000 25.35664 ?  88  GLU   A CA    1 
ATOM   659  C  C     . GLU   A 1 108 ? -15.59500 -32.33600 -6.00700  1.000 28.29141 ?  88  GLU   A C     1 
ATOM   660  O  O     . GLU   A 1 108 ? -15.08200 -33.38200 -6.42200  1.000 28.57862 ?  88  GLU   A O     1 
ATOM   661  C  CB    . GLU   A 1 108 ? -17.77900 -32.60200 -4.75300  1.000 27.93221 ?  88  GLU   A CB    1 
ATOM   662  C  CG    . GLU   A 1 108 ? -18.40700 -32.89700 -3.40300  1.000 31.10209 ?  88  GLU   A CG    1 
ATOM   663  C  CD    . GLU   A 1 108 ? -19.91600 -33.03500 -3.42600  1.000 37.04205 ?  88  GLU   A CD    1 
ATOM   664  O  OE1   . GLU   A 1 108 ? -20.53500 -32.76800 -4.48600  1.000 42.68372 ?  88  GLU   A OE1   1 
ATOM   665  O  OE2   . GLU   A 1 108 ? -20.47700 -33.39500 -2.36200  1.000 37.27931 -1 88  GLU   A OE2   1 
ATOM   666  N  N     . GLN   A 1 109 ? -15.57100 -31.20800 -6.73200  1.000 25.01767 ?  89  GLN   A N     1 
ATOM   667  C  CA    . GLN   A 1 109 ? -14.96500 -31.16700 -8.06100  1.000 26.50936 ?  89  GLN   A CA    1 
ATOM   668  C  C     . GLN   A 1 109 ? -13.59500 -30.51000 -8.08700  1.000 22.64458 ?  89  GLN   A C     1 
ATOM   669  O  O     . GLN   A 1 109 ? -12.87900 -30.65800 -9.07900  1.000 26.52943 ?  89  GLN   A O     1 
ATOM   670  C  CB    . GLN   A 1 109 ? -15.85900 -30.41600 -9.05900  1.000 24.39715 ?  89  GLN   A CB    1 
ATOM   671  C  CG    . GLN   A 1 109 ? -17.26900 -30.85800 -8.99600  1.000 28.45068 ?  89  GLN   A CG    1 
ATOM   672  C  CD    . GLN   A 1 109 ? -17.49500 -32.13300 -9.76700  1.000 40.47026 ?  89  GLN   A CD    1 
ATOM   673  O  OE1   . GLN   A 1 109 ? -16.68700 -32.50900 -10.61500 1.000 39.97331 ?  89  GLN   A OE1   1 
ATOM   674  N  NE2   . GLN   A 1 109 ? -18.58700 -32.82000 -9.46100  1.000 40.94995 ?  89  GLN   A NE2   1 
ATOM   675  N  N     . GLY   A 1 110 ? -13.22100 -29.77500 -7.03600  1.000 24.84291 ?  90  GLY   A N     1 
ATOM   676  C  CA    . GLY   A 1 110 ? -11.92800 -29.12700 -6.97500  1.000 23.32651 ?  90  GLY   A CA    1 
ATOM   677  C  C     . GLY   A 1 110 ? -11.82700 -27.80200 -7.69900  1.000 23.45662 ?  90  GLY   A C     1 
ATOM   678  O  O     . GLY   A 1 110 ? -10.78800 -27.14100 -7.59800  1.000 22.68198 ?  90  GLY   A O     1 
ATOM   679  N  N     . GLN   A 1 111 ? -12.86100 -27.40300 -8.43400  1.000 22.54789 ?  91  GLN   A N     1 
ATOM   680  C  CA    . GLN   A 1 111 ? -12.84000 -26.14700 -9.17700  1.000 22.86006 ?  91  GLN   A CA    1 
ATOM   681  C  C     . GLN   A 1 111 ? -14.26700 -25.72000 -9.47600  1.000 20.44848 ?  91  GLN   A C     1 
ATOM   682  O  O     . GLN   A 1 111 ? -15.19700 -26.52000 -9.41400  1.000 23.87302 ?  91  GLN   A O     1 
ATOM   683  C  CB    . GLN   A 1 111 ? -12.02700 -26.28700 -10.47600 1.000 24.03901 ?  91  GLN   A CB    1 
ATOM   684  C  CG    . GLN   A 1 111 ? -12.66000 -27.25000 -11.43200 1.000 28.21005 ?  91  GLN   A CG    1 
ATOM   685  C  CD    . GLN   A 1 111 ? -12.21500 -27.03900 -12.86600 1.000 38.91200 ?  91  GLN   A CD    1 
ATOM   686  O  OE1   . GLN   A 1 111 ? -11.20100 -26.37800 -13.13300 1.000 41.92995 ?  91  GLN   A OE1   1 
ATOM   687  N  NE2   . GLN   A 1 111 ? -12.94100 -27.65500 -13.79700 1.000 48.62345 ?  91  GLN   A NE2   1 
ATOM   688  N  N     . LEU   A 1 112 ? -14.43600 -24.42800 -9.77400  1.000 20.47804 ?  92  LEU   A N     1 
ATOM   689  C  CA    . LEU   A 1 112 ? -15.70200 -23.95300 -10.30900 1.000 19.52618 ?  92  LEU   A CA    1 
ATOM   690  C  C     . LEU   A 1 112 ? -15.38300 -22.70100 -11.11600 1.000 22.35617 ?  92  LEU   A C     1 
ATOM   691  O  O     . LEU   A 1 112 ? -14.26000 -22.19500 -11.08000 1.000 22.02472 ?  92  LEU   A O     1 
ATOM   692  C  CB    . LEU   A 1 112 ? -16.74700 -23.69900 -9.20000  1.000 25.01382 ?  92  LEU   A CB    1 
ATOM   693  C  CG    . LEU   A 1 112 ? -16.40500 -22.69100 -8.09800  1.000 23.92424 ?  92  LEU   A CG    1 
ATOM   694  C  CD1   . LEU   A 1 112 ? -16.43500 -21.25300 -8.64200  1.000 20.80751 ?  92  LEU   A CD1   1 
ATOM   695  C  CD2   . LEU   A 1 112 ? -17.40000 -22.82200 -6.92200  1.000 23.45598 ?  92  LEU   A CD2   1 
ATOM   696  N  N     . GLN   A 1 113 ? -16.35900 -22.23000 -11.87700 1.000 19.26483 ?  93  GLN   A N     1 
ATOM   697  C  CA    . GLN   A 1 113 ? -16.18900 -20.98000 -12.61300 1.000 19.21056 ?  93  GLN   A CA    1 
ATOM   698  C  C     . GLN   A 1 113 ? -17.28600 -20.02400 -12.18300 1.000 20.31674 ?  93  GLN   A C     1 
ATOM   699  O  O     . GLN   A 1 113 ? -18.34400 -20.43700 -11.69800 1.000 20.75948 ?  93  GLN   A O     1 
ATOM   700  C  CB    . GLN   A 1 113 ? -16.21900 -21.19500 -14.14000 1.000 20.97326 ?  93  GLN   A CB    1 
ATOM   701  C  CG    . GLN   A 1 113 ? -15.03000 -22.04400 -14.64800 1.000 20.60072 ?  93  GLN   A CG    1 
ATOM   702  C  CD    . GLN   A 1 113 ? -14.94200 -22.15500 -16.17200 1.000 23.39441 ?  93  GLN   A CD    1 
ATOM   703  O  OE1   . GLN   A 1 113 ? -15.58800 -21.41000 -16.91000 1.000 26.04001 ?  93  GLN   A OE1   1 
ATOM   704  N  NE2   . GLN   A 1 113 ? -14.12600 -23.09200 -16.64100 1.000 28.75509 ?  93  GLN   A NE2   1 
ATOM   705  N  N     . TYR   A 1 114 ? -17.01900 -18.73700 -12.36400 1.000 16.47190 ?  94  TYR   A N     1 
ATOM   706  C  CA    . TYR   A 1 114 ? -17.94100 -17.69900 -11.91900 1.000 18.22294 ?  94  TYR   A CA    1 
ATOM   707  C  C     . TYR   A 1 114 ? -17.68400 -16.44400 -12.73800 1.000 19.22437 ?  94  TYR   A C     1 
ATOM   708  O  O     . TYR   A 1 114 ? -16.67300 -16.33700 -13.43700 1.000 20.10259 ?  94  TYR   A O     1 
ATOM   709  C  CB    . TYR   A 1 114 ? -17.78500 -17.41000 -10.40500 1.000 19.02220 ?  94  TYR   A CB    1 
ATOM   710  C  CG    . TYR   A 1 114 ? -16.41300 -16.90800 -9.99100  1.000 19.17137 ?  94  TYR   A CG    1 
ATOM   711  C  CD1   . TYR   A 1 114 ? -15.35900 -17.79800 -9.82300  1.000 17.76556 ?  94  TYR   A CD1   1 
ATOM   712  C  CD2   . TYR   A 1 114 ? -16.17300 -15.53400 -9.74800  1.000 16.86319 ?  94  TYR   A CD2   1 
ATOM   713  C  CE1   . TYR   A 1 114 ? -14.11100 -17.37500 -9.45600  1.000 19.17459 ?  94  TYR   A CE1   1 
ATOM   714  C  CE2   . TYR   A 1 114 ? -14.92400 -15.10300 -9.32100  1.000 20.88580 ?  94  TYR   A CE2   1 
ATOM   715  C  CZ    . TYR   A 1 114 ? -13.88900 -16.02800 -9.18800  1.000 20.74161 ?  94  TYR   A CZ    1 
ATOM   716  O  OH    . TYR   A 1 114 ? -12.63900 -15.61900 -8.78400  1.000 19.81052 ?  94  TYR   A OH    1 
ATOM   717  N  N     . GLN   A 1 115 ? -18.62200 -15.49500 -12.65400 1.000 18.66704 ?  95  GLN   A N     1 
ATOM   718  C  CA    . GLN   A 1 115 ? -18.48700 -14.19800 -13.31200 1.000 14.64615 ?  95  GLN   A CA    1 
ATOM   719  C  C     . GLN   A 1 115 ? -18.19300 -13.09800 -12.29600 1.000 21.23443 ?  95  GLN   A C     1 
ATOM   720  O  O     . GLN   A 1 115 ? -18.71600 -13.11400 -11.17300 1.000 19.83144 ?  95  GLN   A O     1 
ATOM   721  C  CB    . GLN   A 1 115 ? -19.75000 -13.81100 -14.05900 1.000 16.11470 ?  95  GLN   A CB    1 
ATOM   722  C  CG    . GLN   A 1 115 ? -20.28600 -14.89100 -15.00800 1.000 16.93342 ?  95  GLN   A CG    1 
ATOM   723  C  CD    . GLN   A 1 115 ? -19.59500 -14.93300 -16.34700 1.000 18.85167 ?  95  GLN   A CD    1 
ATOM   724  O  OE1   . GLN   A 1 115 ? -18.74900 -14.09800 -16.65300 1.000 21.84340 ?  95  GLN   A OE1   1 
ATOM   725  N  NE2   . GLN   A 1 115 ? -19.95000 -15.92300 -17.15800 1.000 17.37240 ?  95  GLN   A NE2   1 
ATOM   726  N  N     . VAL   A 1 116 ? -17.38500 -12.11600 -12.72400 1.000 18.50501 ?  96  VAL   A N     1 
ATOM   727  C  CA    . VAL   A 1 116 ? -17.17900 -10.89400 -11.95500 1.000 16.18540 ?  96  VAL   A CA    1 
ATOM   728  C  C     . VAL   A 1 116 ? -17.55000 -9.71500  -12.84500 1.000 17.97350 ?  96  VAL   A C     1 
ATOM   729  O  O     . VAL   A 1 116 ? -17.49000 -9.78700  -14.07500 1.000 19.01983 ?  96  VAL   A O     1 
ATOM   730  C  CB    . VAL   A 1 116 ? -15.73000 -10.72400 -11.43500 1.000 16.87203 ?  96  VAL   A CB    1 
ATOM   731  C  CG1   . VAL   A 1 116 ? -15.35700 -11.87000 -10.44900 1.000 18.54224 ?  96  VAL   A CG1   1 
ATOM   732  C  CG2   . VAL   A 1 116 ? -14.72400 -10.56300 -12.55300 1.000 18.74021 ?  96  VAL   A CG2   1 
ATOM   733  N  N     . THR   A 1 117 ? -17.93200 -8.61900  -12.21200 1.000 18.25015 ?  97  THR   A N     1 
ATOM   734  C  CA    . THR   A 1 117 ? -18.29000 -7.42700  -12.97400 1.000 17.16939 ?  97  THR   A CA    1 
ATOM   735  C  C     . THR   A 1 117 ? -17.02900 -6.68500  -13.38200 1.000 18.97743 ?  97  THR   A C     1 
ATOM   736  O  O     . THR   A 1 117 ? -16.15100 -6.44000  -12.55100 1.000 19.56668 ?  97  THR   A O     1 
ATOM   737  C  CB    . THR   A 1 117 ? -19.20900 -6.52800  -12.14400 1.000 22.48110 ?  97  THR   A CB    1 
ATOM   738  O  OG1   . THR   A 1 117 ? -20.48300 -7.17600  -11.96900 1.000 19.85916 ?  97  THR   A OG1   1 
ATOM   739  C  CG2   . THR   A 1 117 ? -19.38300 -5.16600  -12.82600 1.000 21.34681 ?  97  THR   A CG2   1 
ATOM   740  N  N     . LEU   A 1 118 ? -16.94400 -6.31100  -14.66700 1.000 17.61779 ?  98  LEU   A N     1 
ATOM   741  C  CA    . LEU   A 1 118 ? -15.91500 -5.36400  -15.09100 1.000 18.00698 ?  98  LEU   A CA    1 
ATOM   742  C  C     . LEU   A 1 118 ? -16.41700 -3.93300  -14.95000 1.000 18.64338 ?  98  LEU   A C     1 
ATOM   743  O  O     . LEU   A 1 118 ? -15.86000 -3.13400  -14.18900 1.000 18.77627 ?  98  LEU   A O     1 
ATOM   744  C  CB    . LEU   A 1 118 ? -15.49900 -5.62200  -16.55400 1.000 18.19884 ?  98  LEU   A CB    1 
ATOM   745  C  CG    . LEU   A 1 118 ? -14.88800 -7.00100  -16.85900 1.000 18.87816 ?  98  LEU   A CG    1 
ATOM   746  C  CD1   . LEU   A 1 118 ? -14.56800 -7.16000  -18.37700 1.000 21.62321 ?  98  LEU   A CD1   1 
ATOM   747  C  CD2   . LEU   A 1 118 ? -13.66000 -7.27400  -16.00800 1.000 21.82755 ?  98  LEU   A CD2   1 
ATOM   748  N  N     . GLU   A 1 119 ? -17.47700 -3.60900  -15.68000 1.000 21.23472 ?  99  GLU   A N     1 
ATOM   749  C  CA    . GLU   A 1 119 ? -18.01700 -2.25600  -15.74600 1.000 17.37867 ?  99  GLU   A CA    1 
ATOM   750  C  C     . GLU   A 1 119 ? -19.45000 -2.37200  -16.22900 1.000 17.97118 ?  99  GLU   A C     1 
ATOM   751  O  O     . GLU   A 1 119 ? -19.67900 -2.89000  -17.33000 1.000 20.20073 ?  99  GLU   A O     1 
ATOM   752  C  CB    . GLU   A 1 119 ? -17.17900 -1.40100  -16.68900 1.000 19.97380 ?  99  GLU   A CB    1 
ATOM   753  C  CG    . GLU   A 1 119 ? -17.73400 0.02700   -16.92100 1.000 20.49789 ?  99  GLU   A CG    1 
ATOM   754  C  CD    . GLU   A 1 119 ? -16.96600 0.75000   -18.02800 1.000 27.14277 ?  99  GLU   A CD    1 
ATOM   755  O  OE1   . GLU   A 1 119 ? -15.74700 0.94900   -17.89100 1.000 25.43001 ?  99  GLU   A OE1   1 
ATOM   756  O  OE2   . GLU   A 1 119 ? -17.57300 1.08900   -19.06100 1.000 25.37018 -1 99  GLU   A OE2   1 
ATOM   757  N  N     . GLY   A 1 120 ? -20.40900 -1.93800  -15.40100 1.000 19.59753 ?  100 GLY   A N     1 
ATOM   758  C  CA    . GLY   A 1 120 ? -21.81100 -2.02100  -15.80100 1.000 20.86834 ?  100 GLY   A CA    1 
ATOM   759  C  C     . GLY   A 1 120 ? -22.23500 -3.46600  -16.02800 1.000 24.45055 ?  100 GLY   A C     1 
ATOM   760  O  O     . GLY   A 1 120 ? -22.14600 -4.30600  -15.12300 1.000 22.50769 ?  100 GLY   A O     1 
ATOM   761  N  N     . GLU   A 1 121 ? -22.70100 -3.76500  -17.25600 1.000 20.98987 ?  101 GLU   A N     1 
ATOM   762  C  CA    . GLU   A 1 121 ? -23.09200 -5.11500  -17.66800 1.000 21.32266 ?  101 GLU   A CA    1 
ATOM   763  C  C     . GLU   A 1 121 ? -21.94000 -5.91200  -18.26500 1.000 22.46892 ?  101 GLU   A C     1 
ATOM   764  O  O     . GLU   A 1 121 ? -22.13600 -7.08000  -18.63400 1.000 23.51402 ?  101 GLU   A O     1 
ATOM   765  C  CB    . GLU   A 1 121 ? -24.24300 -5.05700  -18.69400 1.000 22.25033 ?  101 GLU   A CB    1 
ATOM   766  C  CG    . GLU   A 1 121 ? -25.57900 -4.65600  -18.06800 1.000 26.30502 ?  101 GLU   A CG    1 
ATOM   767  C  CD    . GLU   A 1 121 ? -26.67000 -4.39300  -19.08800 1.000 30.30184 ?  101 GLU   A CD    1 
ATOM   768  O  OE1   . GLU   A 1 121 ? -26.42000 -4.52600  -20.31600 1.000 28.51904 ?  101 GLU   A OE1   1 
ATOM   769  O  OE2   . GLU   A 1 121 ? -27.78300 -4.04000  -18.64400 1.000 33.07324 -1 101 GLU   A OE2   1 
ATOM   770  N  N     . LEU   A 1 122 ? -20.75700 -5.32300  -18.39600 1.000 20.11583 ?  102 LEU   A N     1 
ATOM   771  C  CA    . LEU   A 1 122 ? -19.63000 -6.04700  -18.96500 1.000 17.72576 ?  102 LEU   A CA    1 
ATOM   772  C  C     . LEU   A 1 122 ? -19.03500 -6.92400  -17.87200 1.000 19.67221 ?  102 LEU   A C     1 
ATOM   773  O  O     . LEU   A 1 122 ? -18.68900 -6.42900  -16.78900 1.000 18.36678 ?  102 LEU   A O     1 
ATOM   774  C  CB    . LEU   A 1 122 ? -18.58700 -5.08500  -19.53000 1.000 20.16495 ?  102 LEU   A CB    1 
ATOM   775  C  CG    . LEU   A 1 122 ? -19.08900 -4.17400  -20.66200 1.000 18.23281 ?  102 LEU   A CG    1 
ATOM   776  C  CD1   . LEU   A 1 122 ? -18.04800 -3.13800  -21.05500 1.000 21.54846 ?  102 LEU   A CD1   1 
ATOM   777  C  CD2   . LEU   A 1 122 ? -19.51800 -5.01500  -21.87200 1.000 21.95561 ?  102 LEU   A CD2   1 
ATOM   778  N  N     . ILE   A 1 123 ? -18.94200 -8.22300  -18.13200 1.000 21.90755 ?  103 ILE   A N     1 
ATOM   779  C  CA    . ILE   A 1 123 ? -18.51700 -9.17500  -17.10800 1.000 18.94716 ?  103 ILE   A CA    1 
ATOM   780  C  C     . ILE   A 1 123 ? -17.40500 -10.04200 -17.67200 1.000 20.14172 ?  103 ILE   A C     1 
ATOM   781  O  O     . ILE   A 1 123 ? -17.14700 -10.07300 -18.88100 1.000 21.36558 ?  103 ILE   A O     1 
ATOM   782  C  CB    . ILE   A 1 123 ? -19.67900 -10.05300 -16.58900 1.000 22.65085 ?  103 ILE   A CB    1 
ATOM   783  C  CG1   . ILE   A 1 123 ? -20.29700 -10.87300 -17.72700 1.000 18.85702 ?  103 ILE   A CG1   1 
ATOM   784  C  CG2   . ILE   A 1 123 ? -20.75300 -9.18500  -15.95000 1.000 21.59619 ?  103 ILE   A CG2   1 
ATOM   785  C  CD1   . ILE   A 1 123 ? -21.40100 -11.84500 -17.24400 1.000 18.12875 ?  103 ILE   A CD1   1 
ATOM   786  N  N     . GLU   A 1 124 ? -16.74500 -10.76400 -16.77100 1.000 17.28250 ?  104 GLU   A N     1 
ATOM   787  C  CA    . GLU   A 1 124 ? -15.62500 -11.61700 -17.14800 1.000 17.96446 ?  104 GLU   A CA    1 
ATOM   788  C  C     . GLU   A 1 124 ? -15.66100 -12.90700 -16.34900 1.000 21.07340 ?  104 GLU   A C     1 
ATOM   789  O  O     . GLU   A 1 124 ? -15.89500 -12.87700 -15.13400 1.000 16.45820 ?  104 GLU   A O     1 
ATOM   790  C  CB    . GLU   A 1 124 ? -14.30400 -10.88900 -16.91900 1.000 22.84620 ?  104 GLU   A CB    1 
ATOM   791  C  CG    . GLU   A 1 124 ? -13.03400 -11.70200 -17.17300 1.000 23.64098 ?  104 GLU   A CG    1 
ATOM   792  C  CD    . GLU   A 1 124 ? -11.80500 -10.86600 -16.89500 1.000 28.59806 ?  104 GLU   A CD    1 
ATOM   793  O  OE1   . GLU   A 1 124 ? -11.52600 -9.96300  -17.70800 1.000 30.45451 ?  104 GLU   A OE1   1 
ATOM   794  O  OE2   . GLU   A 1 124 ? -11.15800 -11.07800 -15.84500 1.000 27.03950 -1 104 GLU   A OE2   1 
ATOM   795  N  N     . ARG   A 1 125 ? -15.44400 -14.04500 -17.03600 1.000 16.63605 ?  105 ARG   A N     1 
ATOM   796  C  CA    . ARG   A 1 125 ? -15.53300 -15.34600 -16.37300 1.000 15.43389 ?  105 ARG   A CA    1 
ATOM   797  C  C     . ARG   A 1 125 ? -14.18900 -15.72900 -15.78300 1.000 20.81109 ?  105 ARG   A C     1 
ATOM   798  O  O     . ARG   A 1 125 ? -13.14600 -15.46200 -16.37900 1.000 20.88907 ?  105 ARG   A O     1 
ATOM   799  C  CB    . ARG   A 1 125 ? -16.01200 -16.41900 -17.35400 1.000 17.87389 ?  105 ARG   A CB    1 
ATOM   800  C  CG    . ARG   A 1 125 ? -16.68800 -17.60700 -16.65600 1.000 20.12041 ?  105 ARG   A CG    1 
ATOM   801  C  CD    . ARG   A 1 125 ? -17.32200 -18.56900 -17.70700 1.000 20.14364 ?  105 ARG   A CD    1 
ATOM   802  N  NE    . ARG   A 1 125 ? -16.30000 -19.28800 -18.46600 1.000 21.80799 ?  105 ARG   A NE    1 
ATOM   803  C  CZ    . ARG   A 1 125 ? -15.95400 -19.01300 -19.72500 1.000 23.81037 ?  105 ARG   A CZ    1 
ATOM   804  N  NH1   . ARG   A 1 125 ? -16.54600 -18.05700 -20.42100 1.000 19.66864 ?  105 ARG   A NH1   1 
ATOM   805  N  NH2   . ARG   A 1 125 ? -14.97800 -19.71000 -20.29700 1.000 21.69640 ?  105 ARG   A NH2   1 
ATOM   806  N  N     . ARG   A 1 126 ? -14.21900 -16.37100 -14.60700 1.000 17.55237 ?  106 ARG   A N     1 
ATOM   807  C  CA    . ARG   A 1 126 ? -13.02200 -16.67700 -13.83800 1.000 19.81299 ?  106 ARG   A CA    1 
ATOM   808  C  C     . ARG   A 1 126 ? -13.15100 -18.07300 -13.24400 1.000 20.02014 ?  106 ARG   A C     1 
ATOM   809  O  O     . ARG   A 1 126 ? -14.24200 -18.64400 -13.19900 1.000 18.54636 ?  106 ARG   A O     1 
ATOM   810  C  CB    . ARG   A 1 126 ? -12.81200 -15.64600 -12.71600 1.000 23.54282 ?  106 ARG   A CB    1 
ATOM   811  C  CG    . ARG   A 1 126 ? -12.74300 -14.21500 -13.27800 1.000 23.39482 ?  106 ARG   A CG    1 
ATOM   812  C  CD    . ARG   A 1 126 ? -11.53000 -13.49100 -12.78700 1.000 37.45077 ?  106 ARG   A CD    1 
ATOM   813  N  NE    . ARG   A 1 126 ? -11.44700 -12.11500 -13.26800 1.000 25.97810 ?  106 ARG   A NE    1 
ATOM   814  C  CZ    . ARG   A 1 126 ? -11.00800 -11.11500 -12.51500 1.000 27.79692 ?  106 ARG   A CZ    1 
ATOM   815  N  NH1   . ARG   A 1 126 ? -10.85000 -11.25300 -11.20700 1.000 25.50706 ?  106 ARG   A NH1   1 
ATOM   816  N  NH2   . ARG   A 1 126 ? -10.73500 -9.94500  -13.08400 1.000 22.38118 ?  106 ARG   A NH2   1 
ATOM   817  N  N     . THR   A 1 127 ? -12.02900 -18.61700 -12.77300 1.000 23.82204 ?  107 THR   A N     1 
ATOM   818  C  CA    . THR   A 1 127 ? -12.00100 -19.97000 -12.20900 1.000 20.05106 ?  107 THR   A CA    1 
ATOM   819  C  C     . THR   A 1 127 ? -11.47800 -19.94500 -10.76800 1.000 18.98481 ?  107 THR   A C     1 
ATOM   820  O  O     . THR   A 1 127 ? -10.49600 -19.26000 -10.46600 1.000 21.04477 ?  107 THR   A O     1 
ATOM   821  C  CB    . THR   A 1 127 ? -11.11600 -20.89100 -13.06500 1.000 22.17289 ?  107 THR   A CB    1 
ATOM   822  O  OG1   . THR   A 1 127 ? -11.67000 -21.00700 -14.39500 1.000 23.60626 ?  107 THR   A OG1   1 
ATOM   823  C  CG2   . THR   A 1 127 ? -11.05700 -22.29400 -12.44000 1.000 24.06542 ?  107 THR   A CG2   1 
ATOM   824  N  N     . ALA   A 1 128 ? -12.14200 -20.68100 -9.87100  1.000 19.94451 ?  108 ALA   A N     1 
ATOM   825  C  CA    . ALA   A 1 128 ? -11.58800 -21.00400 -8.55500  1.000 22.94268 ?  108 ALA   A CA    1 
ATOM   826  C  C     . ALA   A 1 128 ? -11.07500 -22.43800 -8.61800  1.000 22.05684 ?  108 ALA   A C     1 
ATOM   827  O  O     . ALA   A 1 128 ? -11.77500 -23.31300 -9.13100  1.000 23.57011 ?  108 ALA   A O     1 
ATOM   828  C  CB    . ALA   A 1 128 ? -12.64200 -20.86800 -7.45700  1.000 21.60165 ?  108 ALA   A CB    1 
ATOM   829  N  N     . ASP   A 1 129 ? -9.86800  -22.67600 -8.09200  1.000 21.56164 ?  109 ASP   A N     1 
ATOM   830  C  CA    . ASP   A 1 129 ? -9.18700  -23.96100 -8.26900  1.000 25.68677 ?  109 ASP   A CA    1 
ATOM   831  C  C     . ASP   A 1 129 ? -8.42600  -24.32300 -6.99300  1.000 23.28367 ?  109 ASP   A C     1 
ATOM   832  O  O     . ASP   A 1 129 ? -7.42200  -23.67700 -6.66300  1.000 25.06252 ?  109 ASP   A O     1 
ATOM   833  C  CB    . ASP   A 1 129 ? -8.23700  -23.89600 -9.46100  1.000 30.96502 ?  109 ASP   A CB    1 
ATOM   834  C  CG    . ASP   A 1 129 ? -7.69800  -25.25600 -9.84100  1.000 35.99434 ?  109 ASP   A CG    1 
ATOM   835  O  OD1   . ASP   A 1 129 ? -6.86400  -25.80300 -9.09100  1.000 32.95352 ?  109 ASP   A OD1   1 
ATOM   836  O  OD2   . ASP   A 1 129 ? -8.11200  -25.78500 -10.88800 1.000 41.22128 -1 109 ASP   A OD2   1 
ATOM   837  N  N     . LEU   A 1 130 ? -8.89400  -25.36100 -6.28400  1.000 23.68811 ?  110 LEU   A N     1 
ATOM   838  C  CA    . LEU   A 1 130 ? -8.25900  -25.73000 -5.01400  1.000 23.39943 ?  110 LEU   A CA    1 
ATOM   839  C  C     . LEU   A 1 130 ? -6.84300  -26.23900 -5.23400  1.000 24.85167 ?  110 LEU   A C     1 
ATOM   840  O  O     . LEU   A 1 130 ? -5.94500  -25.95200 -4.43400  1.000 22.85346 ?  110 LEU   A O     1 
ATOM   841  C  CB    . LEU   A 1 130 ? -9.08700  -26.78300 -4.28300  1.000 22.97503 ?  110 LEU   A CB    1 
ATOM   842  C  CG    . LEU   A 1 130 ? -10.50000 -26.43800 -3.83100  1.000 25.26639 ?  110 LEU   A CG    1 
ATOM   843  C  CD1   . LEU   A 1 130 ? -11.00600 -27.57800 -2.91300  1.000 24.36949 ?  110 LEU   A CD1   1 
ATOM   844  C  CD2   . LEU   A 1 130 ? -10.52700 -25.07700 -3.10500  1.000 24.47744 ?  110 LEU   A CD2   1 
ATOM   845  N  N     . ALA   A 1 131 ? -6.62000  -26.98000 -6.33100  1.000 23.89863 ?  111 ALA   A N     1 
ATOM   846  C  CA    . ALA   A 1 131 ? -5.28700  -27.49600 -6.62800  1.000 27.82084 ?  111 ALA   A CA    1 
ATOM   847  C  C     . ALA   A 1 131 ? -4.26000  -26.37200 -6.71000  1.000 26.96773 ?  111 ALA   A C     1 
ATOM   848  O  O     . ALA   A 1 131 ? -3.17900  -26.45200 -6.11400  1.000 31.10728 ?  111 ALA   A O     1 
ATOM   849  C  CB    . ALA   A 1 131 ? -5.32400  -28.29400 -7.93300  1.000 32.76382 ?  111 ALA   A CB    1 
ATOM   850  N  N     . ALA   A 1 132 ? -4.58400  -25.30500 -7.43600  1.000 27.77011 ?  112 ALA   A N     1 
ATOM   851  C  CA    . ALA   A 1 132 ? -3.66900  -24.18100 -7.54100  1.000 27.08993 ?  112 ALA   A CA    1 
ATOM   852  C  C     . ALA   A 1 132 ? -3.34400  -23.55800 -6.18800  1.000 32.55255 ?  112 ALA   A C     1 
ATOM   853  O  O     . ALA   A 1 132 ? -2.29700  -22.91900 -6.05000  1.000 36.49717 ?  112 ALA   A O     1 
ATOM   854  C  CB    . ALA   A 1 132 ? -4.26400  -23.11300 -8.45700  1.000 24.57469 ?  112 ALA   A CB    1 
ATOM   855  N  N     . LEU   A 1 133 ? -4.21900  -23.70200 -5.19500  1.000 25.59358 ?  113 LEU   A N     1 
ATOM   856  C  CA    . LEU   A 1 133 ? -4.00300  -23.10200 -3.88100  1.000 25.66711 ?  113 LEU   A CA    1 
ATOM   857  C  C     . LEU   A 1 133 ? -3.41200  -24.10100 -2.90000  1.000 28.57019 ?  113 LEU   A C     1 
ATOM   858  O  O     . LEU   A 1 133 ? -3.29100  -23.79200 -1.70700  1.000 27.15783 ?  113 LEU   A O     1 
ATOM   859  C  CB    . LEU   A 1 133 ? -5.32600  -22.55800 -3.33700  1.000 23.66434 ?  113 LEU   A CB    1 
ATOM   860  C  CG    . LEU   A 1 133 ? -5.90700  -21.46500 -4.22600  1.000 25.05651 ?  113 LEU   A CG    1 
ATOM   861  C  CD1   . LEU   A 1 133 ? -7.36000  -21.23100 -3.85400  1.000 22.23911 ?  113 LEU   A CD1   1 
ATOM   862  C  CD2   . LEU   A 1 133 ? -5.08100  -20.19400 -4.06800  1.000 26.39432 ?  113 LEU   A CD2   1 
ATOM   863  N  N     . GLU   A 1 134 ? -3.08400  -25.30700 -3.37700  1.000 31.44922 ?  114 GLU   A N     1 
ATOM   864  C  CA    . GLU   A 1 134 ? -2.57800  -26.38600 -2.53900  1.000 29.23094 ?  114 GLU   A CA    1 
ATOM   865  C  C     . GLU   A 1 134 ? -3.60000  -26.82700 -1.49100  1.000 30.39104 ?  114 GLU   A C     1 
ATOM   866  O  O     . GLU   A 1 134 ? -3.23100  -27.22600 -0.38800  1.000 29.78558 ?  114 GLU   A O     1 
ATOM   867  C  CB    . GLU   A 1 134 ? -1.26200  -25.99000 -1.86200  1.000 33.07286 ?  114 GLU   A CB    1 
ATOM   868  C  CG    . GLU   A 1 134 ? -0.17200  -25.51200 -2.81300  1.000 36.19291 ?  114 GLU   A CG    1 
ATOM   869  N  N     . LEU   A 1 135 ? -4.89400  -26.80300 -1.84600  1.000 24.75995 ?  115 LEU   A N     1 
ATOM   870  C  CA    . LEU   A 1 135 ? -5.97900  -27.16000 -0.92800  1.000 21.20886 ?  115 LEU   A CA    1 
ATOM   871  C  C     . LEU   A 1 135 ? -6.74400  -28.41200 -1.33600  1.000 25.12775 ?  115 LEU   A C     1 
ATOM   872  O  O     . LEU   A 1 135 ? -7.71100  -28.78300 -0.65100  1.000 25.46629 ?  115 LEU   A O     1 
ATOM   873  C  CB    . LEU   A 1 135 ? -6.98700  -26.00300 -0.82800  1.000 22.22970 ?  115 LEU   A CB    1 
ATOM   874  C  CG    . LEU   A 1 135 ? -6.47700  -24.70900 -0.19400  1.000 21.40285 ?  115 LEU   A CG    1 
ATOM   875  C  CD1   . LEU   A 1 135 ? -7.49400  -23.58400 -0.38300  1.000 24.29894 ?  115 LEU   A CD1   1 
ATOM   876  C  CD2   . LEU   A 1 135 ? -6.14000  -24.93700 1.31100   1.000 24.84679 ?  115 LEU   A CD2   1 
ATOM   877  N  N     . SER   A 1 136 ? -6.38500  -29.05300 -2.45200  1.000 26.31573 ?  116 SER   A N     1 
ATOM   878  C  CA    . SER   A 1 136 ? -7.25300  -30.11800 -2.93100  1.000 23.66838 ?  116 SER   A CA    1 
ATOM   879  C  C     . SER   A 1 136 ? -7.06600  -31.40300 -2.13700  1.000 24.61009 ?  116 SER   A C     1 
ATOM   880  O  O     . SER   A 1 136 ? -8.03500  -32.14500 -1.94000  1.000 28.58613 ?  116 SER   A O     1 
ATOM   881  C  CB    . SER   A 1 136 ? -7.01500  -30.36700 -4.42300  1.000 32.46303 ?  116 SER   A CB    1 
ATOM   882  O  OG    . SER   A 1 136 ? -5.63700  -30.26700 -4.73400  1.000 30.58977 ?  116 SER   A OG    1 
ATOM   883  N  N     . ASN   A 1 137 ? -5.85700  -31.64100 -1.62200  1.000 26.40485 ?  117 ASN   A N     1 
ATOM   884  C  CA    . ASN   A 1 137 ? -5.55700  -32.92000 -0.98500  1.000 29.84732 ?  117 ASN   A CA    1 
ATOM   885  C  C     . ASN   A 1 137 ? -6.36800  -33.13800 0.28100   1.000 35.47864 ?  117 ASN   A C     1 
ATOM   886  O  O     . ASN   A 1 137 ? -6.63600  -34.29000 0.64200   1.000 31.11514 ?  117 ASN   A O     1 
ATOM   887  C  CB    . ASN   A 1 137 ? -4.07100  -33.01200 -0.66100  1.000 34.93729 ?  117 ASN   A CB    1 
ATOM   888  N  N     . THR   A 1 138 ? -6.77300  -32.06400 0.96300   1.000 32.51629 ?  118 THR   A N     1 
ATOM   889  C  CA    . THR   A 1 138 ? -7.52200  -32.17800 2.21400   1.000 33.14842 ?  118 THR   A CA    1 
ATOM   890  C  C     . THR   A 1 138 ? -8.98100  -31.74600 2.08100   1.000 33.77614 ?  118 THR   A C     1 
ATOM   891  O  O     . THR   A 1 138 ? -9.69000  -31.69800 3.09000   1.000 27.19772 ?  118 THR   A O     1 
ATOM   892  C  CB    . THR   A 1 138 ? -6.85900  -31.34900 3.32000   1.000 34.13896 ?  118 THR   A CB    1 
ATOM   893  O  OG1   . THR   A 1 138 ? -6.52200  -30.04400 2.81600   1.000 32.98336 ?  118 THR   A OG1   1 
ATOM   894  C  CG2   . THR   A 1 138 ? -5.59700  -32.04600 3.83600   1.000 35.23380 ?  118 THR   A CG2   1 
ATOM   895  N  N     . ALA   A 1 139 ? -9.44600  -31.43000 0.86200   1.000 26.57453 ?  119 ALA   A N     1 
ATOM   896  C  CA    . ALA   A 1 139 ? -10.84500 -31.06400 0.65800   1.000 24.00989 ?  119 ALA   A CA    1 
ATOM   897  C  C     . ALA   A 1 139 ? -11.80000 -32.13100 1.15700   1.000 29.37906 ?  119 ALA   A C     1 
ATOM   898  O  O     . ALA   A 1 139 ? -12.92800 -31.81400 1.54100   1.000 28.00635 ?  119 ALA   A O     1 
ATOM   899  C  CB    . ALA   A 1 139 ? -11.11700 -30.79900 -0.82700  1.000 26.62333 ?  119 ALA   A CB    1 
ATOM   900  N  N     . GLY   A 1 140 ? -11.38800 -33.40200 1.13600   1.000 25.87270 ?  120 GLY   A N     1 
ATOM   901  C  CA    . GLY   A 1 140 ? -12.24200 -34.44900 1.66600   1.000 25.49601 ?  120 GLY   A CA    1 
ATOM   902  C  C     . GLY   A 1 140 ? -12.51100 -34.35700 3.16000   1.000 26.83847 ?  120 GLY   A C     1 
ATOM   903  O  O     . GLY   A 1 140 ? -13.43400 -35.01200 3.65300   1.000 30.59576 ?  120 GLY   A O     1 
ATOM   904  N  N     . ARG   A 1 141 ? -11.74200 -33.55300 3.88300   1.000 22.38935 ?  121 ARG   A N     1 
ATOM   905  C  CA    . ARG   A 1 141 ? -11.92900 -33.42600 5.35400   1.000 27.02937 ?  121 ARG   A CA    1 
ATOM   906  C  C     . ARG   A 1 141 ? -12.98800 -32.36300 5.68400   1.000 26.20649 ?  121 ARG   A C     1 
ATOM   907  O  O     . ARG   A 1 141 ? -13.28200 -32.18900 6.86500   1.000 26.32306 ?  121 ARG   A O     1 
ATOM   908  C  CB    . ARG   A 1 141 ? -10.58600 -33.12600 6.01900   1.000 25.15344 ?  121 ARG   A CB    1 
ATOM   909  C  CG    . ARG   A 1 141 ? -9.44100  -33.98000 5.50300   1.000 32.39105 ?  121 ARG   A CG    1 
ATOM   910  C  CD    . ARG   A 1 141 ? -8.41100  -34.25100 6.57200   1.000 26.82682 ?  121 ARG   A CD    1 
ATOM   911  N  NE    . ARG   A 1 141 ? -7.28900  -33.33700 6.52500   1.000 38.70970 ?  121 ARG   A NE    1 
ATOM   912  C  CZ    . ARG   A 1 141 ? -6.21500  -33.45000 7.29300   1.000 39.29919 ?  121 ARG   A CZ    1 
ATOM   913  N  NH1   . ARG   A 1 141 ? -5.54100  -34.58400 7.32100   1.000 50.06412 ?  121 ARG   A NH1   1 
ATOM   914  N  NH2   . ARG   A 1 141 ? -5.82500  -32.43500 8.04200   1.000 44.66009 ?  121 ARG   A NH2   1 
ATOM   915  N  N     . THR   A 1 142 ? -13.55200 -31.70000 4.67400   1.000 21.23886 ?  122 THR   A N     1 
ATOM   916  C  CA    . THR   A 1 142 ? -14.57500 -30.68400 4.90200   1.000 24.15087 ?  122 THR   A CA    1 
ATOM   917  C  C     . THR   A 1 142 ? -15.97500 -31.22300 4.66700   1.000 29.19626 ?  122 THR   A C     1 
ATOM   918  O  O     . THR   A 1 142 ? -16.19200 -32.11300 3.84400   1.000 31.49128 ?  122 THR   A O     1 
ATOM   919  C  CB    . THR   A 1 142 ? -14.37500 -29.47200 3.99900   1.000 27.67503 ?  122 THR   A CB    1 
ATOM   920  O  OG1   . THR   A 1 142 ? -14.80600 -29.81300 2.66600   1.000 30.71876 ?  122 THR   A OG1   1 
ATOM   921  C  CG2   . THR   A 1 142 ? -12.94700 -28.98300 4.03000   1.000 22.82104 ?  122 THR   A CG2   1 
ATOM   922  N  N     . ARG   A 1 143 ? -16.92800 -30.67700 5.41500   1.000 23.17495 ?  123 ARG   A N     1 
ATOM   923  C  CA    . ARG   A 1 143 ? -18.34400 -30.85300 5.12900   1.000 25.18387 ?  123 ARG   A CA    1 
ATOM   924  C  C     . ARG   A 1 143 ? -19.00100 -29.49300 5.32800   1.000 28.34736 ?  123 ARG   A C     1 
ATOM   925  O  O     . ARG   A 1 143 ? -18.75000 -28.82600 6.33400   1.000 24.92120 ?  123 ARG   A O     1 
ATOM   926  C  CB    . ARG   A 1 143 ? -18.97900 -31.90300 6.04200   1.000 30.56314 ?  123 ARG   A CB    1 
ATOM   927  C  CG    . ARG   A 1 143 ? -20.50700 -31.90900 6.03800   1.000 41.53718 ?  123 ARG   A CG    1 
ATOM   928  C  CD    . ARG   A 1 143 ? -21.03500 -33.04200 6.92300   1.000 49.84452 ?  123 ARG   A CD    1 
ATOM   929  N  NE    . ARG   A 1 143 ? -21.66400 -32.55300 8.14500   1.000 51.82172 ?  123 ARG   A NE    1 
ATOM   930  C  CZ    . ARG   A 1 143 ? -21.37300 -32.98500 9.36700   1.000 48.73604 ?  123 ARG   A CZ    1 
ATOM   931  N  NH1   . ARG   A 1 143 ? -20.41800 -33.87800 9.57500   1.000 48.32307 ?  123 ARG   A NH1   1 
ATOM   932  N  NH2   . ARG   A 1 143 ? -22.05400 -32.50300 10.40700  1.000 40.32590 ?  123 ARG   A NH2   1 
ATOM   933  N  N     . PHE   A 1 144 ? -19.83300 -29.08600 4.37800   1.000 19.60262 ?  124 PHE   A N     1 
ATOM   934  C  CA    . PHE   A 1 144 ? -20.48400 -27.78300 4.37900   1.000 19.73596 ?  124 PHE   A CA    1 
ATOM   935  C  C     . PHE   A 1 144 ? -21.98200 -27.99300 4.53400   1.000 26.59400 ?  124 PHE   A C     1 
ATOM   936  O  O     . PHE   A 1 144 ? -22.54700 -28.90600 3.92500   1.000 22.46654 ?  124 PHE   A O     1 
ATOM   937  C  CB    . PHE   A 1 144 ? -20.17700 -27.03800 3.07200   1.000 20.53119 ?  124 PHE   A CB    1 
ATOM   938  C  CG    . PHE   A 1 144 ? -18.74600 -26.63600 2.93400   1.000 20.22694 ?  124 PHE   A CG    1 
ATOM   939  C  CD1   . PHE   A 1 144 ? -18.26600 -25.53000 3.62100   1.000 20.09388 ?  124 PHE   A CD1   1 
ATOM   940  C  CD2   . PHE   A 1 144 ? -17.87700 -27.36600 2.15000   1.000 20.13695 ?  124 PHE   A CD2   1 
ATOM   941  C  CE1   . PHE   A 1 144 ? -16.93100 -25.15300 3.51600   1.000 18.99500 ?  124 PHE   A CE1   1 
ATOM   942  C  CE2   . PHE   A 1 144 ? -16.54300 -26.99900 2.03600   1.000 20.48629 ?  124 PHE   A CE2   1 
ATOM   943  C  CZ    . PHE   A 1 144 ? -16.06800 -25.89500 2.72700   1.000 22.15570 ?  124 PHE   A CZ    1 
ATOM   944  N  N     . GLN   A 1 145 ? -22.63000 -27.17600 5.36700   1.000 23.08203 ?  125 GLN   A N     1 
ATOM   945  C  CA    . GLN   A 1 145 ? -24.07400 -27.29100 5.52300   1.000 23.17757 ?  125 GLN   A CA    1 
ATOM   946  C  C     . GLN   A 1 145 ? -24.67800 -25.91300 5.70000   1.000 26.35343 ?  125 GLN   A C     1 
ATOM   947  O  O     . GLN   A 1 145 ? -24.03300 -24.99900 6.22600   1.000 23.77563 ?  125 GLN   A O     1 
ATOM   948  C  CB    . GLN   A 1 145 ? -24.48500 -28.15200 6.71800   1.000 30.38632 ?  125 GLN   A CB    1 
ATOM   949  C  CG    . GLN   A 1 145 ? -23.63700 -27.94700 7.93500   1.000 30.01727 ?  125 GLN   A CG    1 
ATOM   950  C  CD    . GLN   A 1 145 ? -23.86600 -29.03800 8.96600   1.000 32.40706 ?  125 GLN   A CD    1 
ATOM   951  O  OE1   . GLN   A 1 145 ? -23.26600 -30.11400 8.88700   1.000 34.20784 ?  125 GLN   A OE1   1 
ATOM   952  N  NE2   . GLN   A 1 145 ? -24.72000 -28.75900 9.94800   1.000 32.57634 ?  125 GLN   A NE2   1 
ATOM   953  N  N     . VAL   A 1 146 ? -25.93000 -25.78000 5.26100   1.000 26.70647 ?  126 VAL   A N     1 
ATOM   954  C  CA    . VAL   A 1 146 ? -26.72700 -24.58500 5.54100   1.000 24.54668 ?  126 VAL   A CA    1 
ATOM   955  C  C     . VAL   A 1 146 ? -27.19300 -24.61900 6.99300   1.000 29.37348 ?  126 VAL   A C     1 
ATOM   956  O  O     . VAL   A 1 146 ? -27.63300 -25.66000 7.50000   1.000 32.45803 ?  126 VAL   A O     1 
ATOM   957  C  CB    . VAL   A 1 146 ? -27.91600 -24.49600 4.55600   1.000 28.62826 ?  126 VAL   A CB    1 
ATOM   958  C  CG1   . VAL   A 1 146 ? -28.79100 -23.29300 4.86300   1.000 26.92619 ?  126 VAL   A CG1   1 
ATOM   959  C  CG2   . VAL   A 1 146 ? -27.40300 -24.41400 3.12800   1.000 30.22560 ?  126 VAL   A CG2   1 
ATOM   960  N  N     . GLY   A 1 147 ? -27.07200 -23.49200 7.68600   1.000 25.64299 ?  127 GLY   A N     1 
ATOM   961  C  CA    . GLY   A 1 147 ? -27.50800 -23.44300 9.06900   1.000 22.79232 ?  127 GLY   A CA    1 
ATOM   962  C  C     . GLY   A 1 147 ? -27.41700 -22.03100 9.60400   1.000 24.71254 ?  127 GLY   A C     1 
ATOM   963  O  O     . GLY   A 1 147 ? -26.83700 -21.13700 8.97800   1.000 20.95705 ?  127 GLY   A O     1 
ATOM   964  N  N     . ASP   A 1 148 ? -28.02400 -21.85100 10.77600  1.000 21.80129 ?  128 ASP   A N     1 
ATOM   965  C  CA    . ASP   A 1 148 ? -28.18000 -20.55600 11.43700  1.000 21.99706 ?  128 ASP   A CA    1 
ATOM   966  C  C     . ASP   A 1 148 ? -27.29300 -20.52300 12.67400  1.000 24.94692 ?  128 ASP   A C     1 
ATOM   967  O  O     . ASP   A 1 148 ? -27.53200 -21.24500 13.65900  1.000 23.33447 ?  128 ASP   A O     1 
ATOM   968  C  CB    . ASP   A 1 148 ? -29.64100 -20.32000 11.79700  1.000 25.33780 ?  128 ASP   A CB    1 
ATOM   969  C  CG    . ASP   A 1 148 ? -29.87500 -19.00500 12.50800  1.000 28.59340 ?  128 ASP   A CG    1 
ATOM   970  O  OD1   . ASP   A 1 148 ? -28.92000 -18.21300 12.71300  1.000 24.34542 ?  128 ASP   A OD1   1 
ATOM   971  O  OD2   . ASP   A 1 148 ? -31.03600 -18.78300 12.90300  1.000 31.66507 -1 128 ASP   A OD2   1 
ATOM   972  N  N     . ALA   A 1 149 ? -26.28400 -19.65700 12.63400  1.000 21.89878 ?  129 ALA   A N     1 
ATOM   973  C  CA    . ALA   A 1 149 ? -25.31300 -19.60000 13.70800  1.000 21.56282 ?  129 ALA   A CA    1 
ATOM   974  C  C     . ALA   A 1 149 ? -25.90700 -19.09300 15.00900  1.000 24.55763 ?  129 ALA   A C     1 
ATOM   975  O  O     . ALA   A 1 149 ? -25.27000 -19.22600 16.06000  1.000 26.33159 ?  129 ALA   A O     1 
ATOM   976  C  CB    . ALA   A 1 149 ? -24.14000 -18.71100 13.30600  1.000 21.12761 ?  129 ALA   A CB    1 
ATOM   977  N  N     . CYS   A 1 150 ? -27.08200 -18.48100 14.97000  1.000 21.14114 ?  130 CYS   A N     1 
ATOM   978  C  CA    . CYS   A 1 150 ? -27.71400 -18.07500 16.21600  1.000 20.95454 ?  130 CYS   A CA    1 
ATOM   979  C  C     . CYS   A 1 150 ? -28.56000 -19.19100 16.81200  1.000 24.85985 ?  130 CYS   A C     1 
ATOM   980  O  O     . CYS   A 1 150 ? -29.05400 -19.04200 17.93200  1.000 26.62626 ?  130 CYS   A O     1 
ATOM   981  C  CB    . CYS   A 1 150 ? -28.59200 -16.84600 16.00200  1.000 24.81872 ?  130 CYS   A CB    1 
ATOM   982  S  SG    . CYS   A 1 150 ? -27.68900 -15.28000 15.52000  1.000 26.84825 ?  130 CYS   A SG    1 
ATOM   983  N  N     . ALA   A 1 151 ? -28.75700 -20.29000 16.08800  1.000 20.73073 ?  131 ALA   A N     1 
ATOM   984  C  CA    . ALA   A 1 151 ? -29.54500 -21.41600 16.59300  1.000 22.97188 ?  131 ALA   A CA    1 
ATOM   985  C  C     . ALA   A 1 151 ? -28.99600 -22.70100 15.96000  1.000 24.61678 ?  131 ALA   A C     1 
ATOM   986  O  O     . ALA   A 1 151 ? -29.58800 -23.31800 15.07900  1.000 22.60930 ?  131 ALA   A O     1 
ATOM   987  C  CB    . ALA   A 1 151 ? -31.03300 -21.21200 16.29800  1.000 26.30218 ?  131 ALA   A CB    1 
ATOM   988  N  N     . LEU   A 1 152 ? -27.82000 -23.12400 16.41600  1.000 20.71461 ?  132 LEU   A N     1 
ATOM   989  C  CA    . LEU   A 1 152 ? -27.14200 -24.28500 15.84800  1.000 22.58063 ?  132 LEU   A CA    1 
ATOM   990  C  C     . LEU   A 1 152 ? -27.78400 -25.59000 16.31800  1.000 22.72206 ?  132 LEU   A C     1 
ATOM   991  O  O     . LEU   A 1 152 ? -28.32000 -25.66500 17.42400  1.000 27.37189 ?  132 LEU   A O     1 
ATOM   992  C  CB    . LEU   A 1 152 ? -25.66600 -24.25500 16.23700  1.000 22.52585 ?  132 LEU   A CB    1 
ATOM   993  C  CG    . LEU   A 1 152 ? -24.87900 -23.09400 15.62600  1.000 23.27801 ?  132 LEU   A CG    1 
ATOM   994  C  CD1   . LEU   A 1 152 ? -23.56800 -22.92500 16.38500  1.000 21.42949 ?  132 LEU   A CD1   1 
ATOM   995  C  CD2   . LEU   A 1 152 ? -24.60900 -23.38700 14.14000  1.000 21.04741 ?  132 LEU   A CD2   1 
ATOM   996  N  N     . ASP   A 1 153 ? -27.74600 -26.62000 15.46100  1.000 21.34116 ?  133 ASP   A N     1 
ATOM   997  C  CA    . ASP   A 1 153 ? -28.34600 -27.90700 15.83300  1.000 22.73143 ?  133 ASP   A CA    1 
ATOM   998  C  C     . ASP   A 1 153 ? -27.75800 -28.43100 17.14800  1.000 22.20238 ?  133 ASP   A C     1 
ATOM   999  O  O     . ASP   A 1 153 ? -26.56000 -28.30500 17.39900  1.000 21.81345 ?  133 ASP   A O     1 
ATOM   1000 C  CB    . ASP   A 1 153 ? -28.12600 -28.94400 14.73400  1.000 29.82854 ?  133 ASP   A CB    1 
ATOM   1001 C  CG    . ASP   A 1 153 ? -28.92900 -28.64100 13.48400  1.000 41.38364 ?  133 ASP   A CG    1 
ATOM   1002 O  OD1   . ASP   A 1 153 ? -29.88000 -27.82300 13.57300  1.000 35.01175 ?  133 ASP   A OD1   1 
ATOM   1003 O  OD2   . ASP   A 1 153 ? -28.59600 -29.20200 12.41800  1.000 38.93031 -1 133 ASP   A OD2   1 
ATOM   1004 N  N     . ASP   A 1 154 ? -28.59000 -29.07500 17.96900  1.000 24.73448 ?  134 ASP   A N     1 
ATOM   1005 C  CA    . ASP   A 1 154 ? -28.06300 -29.60700 19.23000  1.000 21.68015 ?  134 ASP   A CA    1 
ATOM   1006 C  C     . ASP   A 1 154 ? -27.29300 -30.91100 19.06300  1.000 23.55085 ?  134 ASP   A C     1 
ATOM   1007 O  O     . ASP   A 1 154 ? -26.77300 -31.42400 20.06100  1.000 20.79666 ?  134 ASP   A O     1 
ATOM   1008 C  CB    . ASP   A 1 154 ? -29.18500 -29.78800 20.27200  1.000 21.38699 ?  134 ASP   A CB    1 
ATOM   1009 C  CG    . ASP   A 1 154 ? -30.17100 -30.89000 19.91500  1.000 29.45199 ?  134 ASP   A CG    1 
ATOM   1010 O  OD1   . ASP   A 1 154 ? -29.98900 -31.58600 18.88700  1.000 28.27046 ?  134 ASP   A OD1   1 
ATOM   1011 O  OD2   . ASP   A 1 154 ? -31.14700 -31.05700 20.67000  1.000 31.11251 -1 134 ASP   A OD2   1 
ATOM   1012 N  N     . THR   A 1 155 ? -27.17100 -31.42400 17.82800  1.000 21.26846 ?  135 THR   A N     1 
ATOM   1013 C  CA    . THR   A 1 155 ? -26.40200 -32.61600 17.49000  1.000 22.38737 ?  135 THR   A CA    1 
ATOM   1014 C  C     . THR   A 1 155 ? -24.98100 -32.30500 17.03800  1.000 22.51051 ?  135 THR   A C     1 
ATOM   1015 O  O     . THR   A 1 155 ? -24.25200 -33.21500 16.65600  1.000 20.78394 ?  135 THR   A O     1 
ATOM   1016 C  CB    . THR   A 1 155 ? -27.12300 -33.39200 16.37800  1.000 25.87591 ?  135 THR   A CB    1 
ATOM   1017 O  OG1   . THR   A 1 155 ? -27.31500 -32.51200 15.25700  1.000 29.70589 ?  135 THR   A OG1   1 
ATOM   1018 C  CG2   . THR   A 1 155 ? -28.46900 -33.80600 16.84500  1.000 26.43108 ?  135 THR   A CG2   1 
ATOM   1019 N  N     . LEU   A 1 156 ? -24.56100 -31.04300 17.09500  1.000 21.41295 ?  136 LEU   A N     1 
ATOM   1020 C  CA    . LEU   A 1 156 ? -23.31300 -30.64000 16.46000  1.000 20.33966 ?  136 LEU   A CA    1 
ATOM   1021 C  C     . LEU   A 1 156 ? -22.07100 -31.09400 17.21600  1.000 26.38472 ?  136 LEU   A C     1 
ATOM   1022 O  O     . LEU   A 1 156 ? -20.98000 -31.08400 16.64000  1.000 22.27070 ?  136 LEU   A O     1 
ATOM   1023 C  CB    . LEU   A 1 156 ? -23.31700 -29.12000 16.31600  1.000 24.65805 ?  136 LEU   A CB    1 
ATOM   1024 C  CG    . LEU   A 1 156 ? -22.49800 -28.42000 15.24100  1.000 29.72561 ?  136 LEU   A CG    1 
ATOM   1025 C  CD1   . LEU   A 1 156 ? -22.71100 -29.05900 13.88400  1.000 23.05120 ?  136 LEU   A CD1   1 
ATOM   1026 C  CD2   . LEU   A 1 156 ? -22.90400 -26.93600 15.23300  1.000 27.99237 ?  136 LEU   A CD2   1 
ATOM   1027 N  N     . GLY   A 1 157 ? -22.18900 -31.47600 18.49200  1.000 19.98350 ?  137 GLY   A N     1 
ATOM   1028 C  CA    . GLY   A 1 157 ? -21.00100 -31.88400 19.21400  1.000 19.30644 ?  137 GLY   A CA    1 
ATOM   1029 C  C     . GLY   A 1 157 ? -20.18500 -30.68700 19.67000  1.000 19.49811 ?  137 GLY   A C     1 
ATOM   1030 O  O     . GLY   A 1 157 ? -20.67000 -29.55200 19.72200  1.000 21.92304 ?  137 GLY   A O     1 
ATOM   1031 N  N     . ARG   A 1 158 ? -18.93100 -30.94900 20.03500  1.000 20.03155 ?  138 ARG   A N     1 
ATOM   1032 C  CA    . ARG   A 1 158 ? -18.03000 -29.86300 20.40600  1.000 25.77453 ?  138 ARG   A CA    1 
ATOM   1033 C  C     . ARG   A 1 158 ? -16.71500 -29.97900 19.64000  1.000 22.88288 ?  138 ARG   A C     1 
ATOM   1034 O  O     . ARG   A 1 158 ? -16.45600 -30.94800 18.92300  1.000 22.70884 ?  138 ARG   A O     1 
ATOM   1035 C  CB    . ARG   A 1 158 ? -17.80900 -29.78600 21.93400  1.000 23.20163 ?  138 ARG   A CB    1 
ATOM   1036 C  CG    . ARG   A 1 158 ? -17.46700 -31.06700 22.59500  1.000 30.65065 ?  138 ARG   A CG    1 
ATOM   1037 C  CD    . ARG   A 1 158 ? -17.59400 -30.87600 24.13000  1.000 30.97346 ?  138 ARG   A CD    1 
ATOM   1038 N  NE    . ARG   A 1 158 ? -16.56700 -31.64300 24.81300  1.000 39.78135 ?  138 ARG   A NE    1 
ATOM   1039 C  CZ    . ARG   A 1 158 ? -16.15700 -31.43200 26.05400  1.000 43.46133 ?  138 ARG   A CZ    1 
ATOM   1040 N  NH1   . ARG   A 1 158 ? -16.58200 -30.38900 26.75700  1.000 32.63645 ?  138 ARG   A NH1   1 
ATOM   1041 N  NH2   . ARG   A 1 158 ? -15.28600 -32.28100 26.59700  1.000 40.04068 ?  138 ARG   A NH2   1 
ATOM   1042 N  N     . PHE   A 1 159 ? -15.89100 -28.94700 19.77400  1.000 18.92109 ?  139 PHE   A N     1 
ATOM   1043 C  CA    . PHE   A 1 159 ? -14.81900 -28.71300 18.83200  1.000 19.00757 ?  139 PHE   A CA    1 
ATOM   1044 C  C     . PHE   A 1 159 ? -13.54800 -28.30400 19.55300  1.000 18.28745 ?  139 PHE   A C     1 
ATOM   1045 O  O     . PHE   A 1 159 ? -13.59400 -27.72500 20.63500  1.000 20.10652 ?  139 PHE   A O     1 
ATOM   1046 C  CB    . PHE   A 1 159 ? -15.23000 -27.62400 17.82800  1.000 17.89602 ?  139 PHE   A CB    1 
ATOM   1047 C  CG    . PHE   A 1 159 ? -16.39700 -28.03300 16.97600  1.000 17.66606 ?  139 PHE   A CG    1 
ATOM   1048 C  CD1   . PHE   A 1 159 ? -17.70100 -27.81800 17.40900  1.000 18.06018 ?  139 PHE   A CD1   1 
ATOM   1049 C  CD2   . PHE   A 1 159 ? -16.18100 -28.67700 15.77100  1.000 18.66534 ?  139 PHE   A CD2   1 
ATOM   1050 C  CE1   . PHE   A 1 159 ? -18.80100 -28.23400 16.64100  1.000 19.27275 ?  139 PHE   A CE1   1 
ATOM   1051 C  CE2   . PHE   A 1 159 ? -17.25500 -29.08200 14.97800  1.000 18.90510 ?  139 PHE   A CE2   1 
ATOM   1052 C  CZ    . PHE   A 1 159 ? -18.57600 -28.87000 15.42200  1.000 19.68167 ?  139 PHE   A CZ    1 
ATOM   1053 N  N     . ASP   A 1 160 ? -12.41800 -28.60400 18.92200  1.000 19.98560 ?  140 ASP   A N     1 
ATOM   1054 C  CA    . ASP   A 1 160 ? -11.12500 -28.12900 19.40000  1.000 17.47034 ?  140 ASP   A CA    1 
ATOM   1055 C  C     . ASP   A 1 160 ? -10.90700 -26.66700 19.03700  1.000 19.54573 ?  140 ASP   A C     1 
ATOM   1056 O  O     . ASP   A 1 160 ? -10.17600 -25.95900 19.74400  1.000 18.20666 ?  140 ASP   A O     1 
ATOM   1057 C  CB    . ASP   A 1 160 ? -10.00300 -28.94400 18.76700  1.000 21.51887 ?  140 ASP   A CB    1 
ATOM   1058 C  CG    . ASP   A 1 160 ? -10.04800 -30.41300 19.17300  1.000 23.50225 ?  140 ASP   A CG    1 
ATOM   1059 O  OD1   . ASP   A 1 160 ? -9.88200  -30.69800 20.38000  1.000 22.86796 ?  140 ASP   A OD1   1 
ATOM   1060 O  OD2   . ASP   A 1 160 ? -10.26800 -31.25500 18.27700  1.000 22.21442 -1 140 ASP   A OD2   1 
ATOM   1061 N  N     . LEU   A 1 161 ? -11.50200 -26.21600 17.93200  1.000 17.52544 ?  141 LEU   A N     1 
ATOM   1062 C  CA    . LEU   A 1 161 ? -11.28500 -24.86500 17.43400  1.000 15.30328 ?  141 LEU   A CA    1 
ATOM   1063 C  C     . LEU   A 1 161 ? -12.55400 -24.39200 16.74700  1.000 17.09424 ?  141 LEU   A C     1 
ATOM   1064 O  O     . LEU   A 1 161 ? -13.15400 -25.14100 15.96700  1.000 17.70033 ?  141 LEU   A O     1 
ATOM   1065 C  CB    . LEU   A 1 161 ? -10.12800 -24.81000 16.43600  1.000 19.70757 ?  141 LEU   A CB    1 
ATOM   1066 C  CG    . LEU   A 1 161 ? -9.70300  -23.38400 16.01800  1.000 17.74270 ?  141 LEU   A CG    1 
ATOM   1067 C  CD1   . LEU   A 1 161 ? -8.20400  -23.34400 15.79900  1.000 20.44766 ?  141 LEU   A CD1   1 
ATOM   1068 C  CD2   . LEU   A 1 161 ? -10.40600 -22.93100 14.71600  1.000 20.11813 ?  141 LEU   A CD2   1 
ATOM   1069 N  N     . ILE   A 1 162 ? -12.93600 -23.13900 17.00200  1.000 17.54997 ?  142 ILE   A N     1 
ATOM   1070 C  CA    . ILE   A 1 162 ? -14.05800 -22.52100 16.30300  1.000 15.69906 ?  142 ILE   A CA    1 
ATOM   1071 C  C     . ILE   A 1 162 ? -13.58700 -21.20500 15.72100  1.000 17.29760 ?  142 ILE   A C     1 
ATOM   1072 O  O     . ILE   A 1 162 ? -12.98100 -20.40100 16.43400  1.000 17.73886 ?  142 ILE   A O     1 
ATOM   1073 C  CB    . ILE   A 1 162 ? -15.25600 -22.27400 17.23500  1.000 19.44772 ?  142 ILE   A CB    1 
ATOM   1074 C  CG1   . ILE   A 1 162 ? -15.75500 -23.61000 17.75300  1.000 16.10269 ?  142 ILE   A CG1   1 
ATOM   1075 C  CG2   . ILE   A 1 162 ? -16.38200 -21.53100 16.44200  1.000 20.14744 ?  142 ILE   A CG2   1 
ATOM   1076 C  CD1   . ILE   A 1 162 ? -17.06300 -23.48000 18.54200  1.000 21.39128 ?  142 ILE   A CD1   1 
ATOM   1077 N  N     . PHE   A 1 163 ? -13.87500 -20.99600 14.43700  1.000 18.83893 ?  143 PHE   A N     1 
ATOM   1078 C  CA    . PHE   A 1 163 ? -13.55600 -19.76700 13.72600  1.000 14.93960 ?  143 PHE   A CA    1 
ATOM   1079 C  C     . PHE   A 1 163 ? -14.85500 -19.10400 13.30600  1.000 17.08020 ?  143 PHE   A C     1 
ATOM   1080 O  O     . PHE   A 1 163 ? -15.71600 -19.75800 12.70000  1.000 17.55789 ?  143 PHE   A O     1 
ATOM   1081 C  CB    . PHE   A 1 163 ? -12.73300 -20.05300 12.46800  1.000 15.25223 ?  143 PHE   A CB    1 
ATOM   1082 C  CG    . PHE   A 1 163 ? -12.43000 -18.81100 11.65700  1.000 15.40819 ?  143 PHE   A CG    1 
ATOM   1083 C  CD1   . PHE   A 1 163 ? -11.66700 -17.79100 12.21300  1.000 20.15072 ?  143 PHE   A CD1   1 
ATOM   1084 C  CD2   . PHE   A 1 163 ? -12.92600 -18.65400 10.37800  1.000 17.88380 ?  143 PHE   A CD2   1 
ATOM   1085 C  CE1   . PHE   A 1 163 ? -11.38200 -16.65400 11.46500  1.000 18.70059 ?  143 PHE   A CE1   1 
ATOM   1086 C  CE2   . PHE   A 1 163 ? -12.64500 -17.51300 9.62400   1.000 18.42437 ?  143 PHE   A CE2   1 
ATOM   1087 C  CZ    . PHE   A 1 163 ? -11.88000 -16.50800 10.18700  1.000 18.26234 ?  143 PHE   A CZ    1 
ATOM   1088 N  N     . ALA   A 1 164 ? -14.97600 -17.80000 13.56300  1.000 16.86239 ?  144 ALA   A N     1 
ATOM   1089 C  CA    . ALA   A 1 164 ? -16.12000 -17.02400 13.07200  1.000 17.07711 ?  144 ALA   A CA    1 
ATOM   1090 C  C     . ALA   A 1 164 ? -15.57900 -15.75100 12.43600  1.000 18.66058 ?  144 ALA   A C     1 
ATOM   1091 O  O     . ALA   A 1 164 ? -15.33800 -14.75800 13.13100  1.000 18.91088 ?  144 ALA   A O     1 
ATOM   1092 C  CB    . ALA   A 1 164 ? -17.10400 -16.71900 14.19000  1.000 17.49794 ?  144 ALA   A CB    1 
ATOM   1093 N  N     . GLY   A 1 165 ? -15.39300 -15.78700 11.11300  1.000 15.95336 ?  145 GLY   A N     1 
ATOM   1094 C  CA    . GLY   A 1 165 ? -14.80400 -14.66200 10.40700  1.000 16.90026 ?  145 GLY   A CA    1 
ATOM   1095 C  C     . GLY   A 1 165 ? -15.81700 -13.65900 9.89000   1.000 17.36319 ?  145 GLY   A C     1 
ATOM   1096 O  O     . GLY   A 1 165 ? -16.74700 -14.01300 9.15400   1.000 16.54468 ?  145 GLY   A O     1 
ATOM   1097 N  N     . ASN   A 1 166 ? -15.66600 -12.39900 10.29500  1.000 14.91514 ?  146 ASN   A N     1 
ATOM   1098 C  CA    . ASN   A 1 166 ? -16.51800 -11.32700 9.78500   1.000 15.47740 ?  146 ASN   A CA    1 
ATOM   1099 C  C     . ASN   A 1 166 ? -17.99900 -11.64500 9.92200   1.000 15.60324 ?  146 ASN   A C     1 
ATOM   1100 O  O     . ASN   A 1 166 ? -18.79800 -11.32900 9.03600   1.000 16.67325 ?  146 ASN   A O     1 
ATOM   1101 C  CB    . ASN   A 1 166 ? -16.17200 -11.02000 8.32400   1.000 15.37486 ?  146 ASN   A CB    1 
ATOM   1102 C  CG    . ASN   A 1 166 ? -14.96000 -10.11600 8.19800   1.000 18.23399 ?  146 ASN   A CG    1 
ATOM   1103 O  OD1   . ASN   A 1 166 ? -14.27000 -9.84500  9.18700   1.000 17.75949 ?  146 ASN   A OD1   1 
ATOM   1104 N  ND2   . ASN   A 1 166 ? -14.67400 -9.67500  6.97600   1.000 17.57018 ?  146 ASN   A ND2   1 
ATOM   1105 N  N     . LEU   A 1 167 ? -18.38200 -12.25400 11.05300  1.000 15.13506 ?  147 LEU   A N     1 
ATOM   1106 C  CA    . LEU   A 1 167 ? -19.73400 -12.76500 11.25500  1.000 17.52545 ?  147 LEU   A CA    1 
ATOM   1107 C  C     . LEU   A 1 167 ? -20.55100 -11.97400 12.25900  1.000 17.92424 ?  147 LEU   A C     1 
ATOM   1108 O  O     . LEU   A 1 167 ? -21.74600 -11.77800 12.03900  1.000 17.10106 ?  147 LEU   A O     1 
ATOM   1109 C  CB    . LEU   A 1 167 ? -19.68800 -14.23000 11.71900  1.000 17.99732 ?  147 LEU   A CB    1 
ATOM   1110 C  CG    . LEU   A 1 167 ? -21.05100 -14.87300 11.98600  1.000 16.14707 ?  147 LEU   A CG    1 
ATOM   1111 C  CD1   . LEU   A 1 167 ? -21.84200 -14.91900 10.67300  1.000 17.91946 ?  147 LEU   A CD1   1 
ATOM   1112 C  CD2   . LEU   A 1 167 ? -20.84800 -16.28400 12.49700  1.000 19.26311 ?  147 LEU   A CD2   1 
ATOM   1113 N  N     . ILE   A 1 168 ? -19.94800 -11.55000 13.38000  1.000 18.50056 ?  148 ILE   A N     1 
ATOM   1114 C  CA    . ILE   A 1 168 ? -20.74400 -11.06800 14.50600  1.000 18.39991 ?  148 ILE   A CA    1 
ATOM   1115 C  C     . ILE   A 1 168 ? -21.51000 -9.79500  14.14100  1.000 20.93821 ?  148 ILE   A C     1 
ATOM   1116 O  O     . ILE   A 1 168 ? -22.61100 -9.56100  14.66100  1.000 19.47647 ?  148 ILE   A O     1 
ATOM   1117 C  CB    . ILE   A 1 168 ? -19.84600 -10.88800 15.75700  1.000 21.58583 ?  148 ILE   A CB    1 
ATOM   1118 C  CG1   . ILE   A 1 168 ? -20.67500 -10.78500 17.03900  1.000 30.99918 ?  148 ILE   A CG1   1 
ATOM   1119 C  CG2   . ILE   A 1 168 ? -18.92500 -9.73600  15.63600  1.000 20.08979 ?  148 ILE   A CG2   1 
ATOM   1120 C  CD1   . ILE   A 1 168 ? -20.99600 -12.12200 17.62900  1.000 35.15460 ?  148 ILE   A CD1   1 
ATOM   1121 N  N     . ASP   A 1 169 ? -20.98100 -8.98200  13.22200  1.000 17.27383 ?  149 ASP   A N     1 
ATOM   1122 C  CA    . ASP   A 1 169 ? -21.67000 -7.76600  12.79100  1.000 18.35052 ?  149 ASP   A CA    1 
ATOM   1123 C  C     . ASP   A 1 169 ? -22.66200 -8.03400  11.66400  1.000 17.67732 ?  149 ASP   A C     1 
ATOM   1124 O  O     . ASP   A 1 169 ? -23.24300 -7.08500  11.10000  1.000 17.71943 ?  149 ASP   A O     1 
ATOM   1125 C  CB    . ASP   A 1 169 ? -20.66300 -6.67300  12.39300  1.000 17.54415 ?  149 ASP   A CB    1 
ATOM   1126 C  CG    . ASP   A 1 169 ? -19.70900 -7.09400  11.27000  1.000 20.79340 ?  149 ASP   A CG    1 
ATOM   1127 O  OD1   . ASP   A 1 169 ? -19.44100 -8.29700  11.06900  1.000 22.92712 ?  149 ASP   A OD1   1 
ATOM   1128 O  OD2   . ASP   A 1 169 ? -19.15900 -6.18200  10.61600  1.000 18.29354 -1 149 ASP   A OD2   1 
ATOM   1129 N  N     . ARG   A 1 170 ? -22.92900 -9.30200  11.37500  1.000 16.10045 ?  150 ARG   A N     1 
ATOM   1130 C  CA    . ARG   A 1 170 ? -23.95100 -9.65800  10.39500  1.000 18.37606 ?  150 ARG   A CA    1 
ATOM   1131 C  C     . ARG   A 1 170 ? -25.03500 -10.55300 10.98700  1.000 22.41204 ?  150 ARG   A C     1 
ATOM   1132 O  O     . ARG   A 1 170 ? -25.80100 -11.15900 10.22600  1.000 21.61409 ?  150 ARG   A O     1 
ATOM   1133 C  CB    . ARG   A 1 170 ? -23.31000 -10.34500 9.17100   1.000 19.44743 ?  150 ARG   A CB    1 
ATOM   1134 C  CG    . ARG   A 1 170 ? -22.36600 -9.40700  8.34500   1.000 20.93934 ?  150 ARG   A CG    1 
ATOM   1135 C  CD    . ARG   A 1 170 ? -23.17000 -8.28900  7.69400   1.000 22.12455 ?  150 ARG   A CD    1 
ATOM   1136 N  NE    . ARG   A 1 170 ? -22.34600 -7.33200  6.95600   1.000 18.90446 ?  150 ARG   A NE    1 
ATOM   1137 C  CZ    . ARG   A 1 170 ? -22.04100 -6.12100  7.40500   1.000 18.70257 ?  150 ARG   A CZ    1 
ATOM   1138 N  NH1   . ARG   A 1 170 ? -22.32500 -5.75100  8.64800   1.000 19.04117 ?  150 ARG   A NH1   1 
ATOM   1139 N  NH2   . ARG   A 1 170 ? -21.44600 -5.25500  6.58400   1.000 19.38188 ?  150 ARG   A NH2   1 
ATOM   1140 N  N     . LEU   A 1 171 ? -25.11200 -10.67400 12.35400  1.000 20.26537 ?  151 LEU   A N     1 
ATOM   1141 C  CA    . LEU   A 1 171 ? -26.04800 -11.56900 13.03600  1.000 20.83498 ?  151 LEU   A CA    1 
ATOM   1142 C  C     . LEU   A 1 171 ? -27.15000 -10.77600 13.70600  1.000 20.25133 ?  151 LEU   A C     1 
ATOM   1143 O  O     . LEU   A 1 171 ? -26.88300 -9.72200  14.28400  1.000 19.36538 ?  151 LEU   A O     1 
ATOM   1144 C  CB    . LEU   A 1 171 ? -25.34200 -12.39100 14.11300  1.000 18.04553 ?  151 LEU   A CB    1 
ATOM   1145 C  CG    . LEU   A 1 171 ? -24.34100 -13.40900 13.60800  1.000 21.36025 ?  151 LEU   A CG    1 
ATOM   1146 C  CD1   . LEU   A 1 171 ? -23.70600 -14.14800 14.80600  1.000 21.67744 ?  151 LEU   A CD1   1 
ATOM   1147 C  CD2   . LEU   A 1 171 ? -25.04100 -14.34200 12.65100  1.000 23.97022 ?  151 LEU   A CD2   1 
ATOM   1148 N  N     . PRO   A 1 172 ? -28.38800 -11.25600 13.68000  1.000 21.31708 ?  152 PRO   A N     1 
ATOM   1149 C  CA    . PRO   A 1 172 ? -29.46200 -10.50400 14.33000  1.000 23.84116 ?  152 PRO   A CA    1 
ATOM   1150 C  C     . PRO   A 1 172 ? -29.48400 -10.63000 15.83900  1.000 24.27466 ?  152 PRO   A C     1 
ATOM   1151 O  O     . PRO   A 1 172 ? -30.05600 -9.75700  16.49900  1.000 23.34884 ?  152 PRO   A O     1 
ATOM   1152 C  CB    . PRO   A 1 172 ? -30.72100 -11.09700 13.68900  1.000 23.92390 ?  152 PRO   A CB    1 
ATOM   1153 C  CG    . PRO   A 1 172 ? -30.34800 -12.48200 13.42700  1.000 26.81246 ?  152 PRO   A CG    1 
ATOM   1154 C  CD    . PRO   A 1 172 ? -28.91700 -12.42600 12.95300  1.000 25.91175 ?  152 PRO   A CD    1 
ATOM   1155 N  N     . ASP   A 1 173 ? -28.85200 -11.65200 16.41300  1.000 23.59996 ?  153 ASP   A N     1 
ATOM   1156 C  CA    . ASP   A 1 173 ? -28.84700 -11.86700 17.86200  1.000 24.58616 ?  153 ASP   A CA    1 
ATOM   1157 C  C     . ASP   A 1 173 ? -27.44500 -12.29000 18.28000  1.000 24.49283 ?  153 ASP   A C     1 
ATOM   1158 O  O     . ASP   A 1 173 ? -27.17700 -13.47200 18.52100  1.000 22.79817 ?  153 ASP   A O     1 
ATOM   1159 C  CB    . ASP   A 1 173 ? -29.89400 -12.90900 18.25600  1.000 28.04616 ?  153 ASP   A CB    1 
ATOM   1160 C  CG    . ASP   A 1 173 ? -30.25800 -12.85400 19.73800  1.000 34.21908 ?  153 ASP   A CG    1 
ATOM   1161 O  OD1   . ASP   A 1 173 ? -29.52100 -12.21500 20.52200  1.000 31.62610 ?  153 ASP   A OD1   1 
ATOM   1162 O  OD2   . ASP   A 1 173 ? -31.28400 -13.46100 20.11300  1.000 36.90621 -1 153 ASP   A OD2   1 
ATOM   1163 N  N     . PRO   A 1 174 ? -26.51500 -11.33700 18.36700  1.000 22.24480 ?  154 PRO   A N     1 
ATOM   1164 C  CA    . PRO   A 1 174 ? -25.14000 -11.68100 18.75900  1.000 20.90881 ?  154 PRO   A CA    1 
ATOM   1165 C  C     . PRO   A 1 174 ? -25.06000 -12.37900 20.11000  1.000 21.37415 ?  154 PRO   A C     1 
ATOM   1166 O  O     . PRO   A 1 174 ? -24.24400 -13.28900 20.28300  1.000 22.65470 ?  154 PRO   A O     1 
ATOM   1167 C  CB    . PRO   A 1 174 ? -24.44600 -10.31000 18.83200  1.000 23.81176 ?  154 PRO   A CB    1 
ATOM   1168 C  CG    . PRO   A 1 174 ? -25.26100 -9.42300  18.03800  1.000 22.71793 ?  154 PRO   A CG    1 
ATOM   1169 C  CD    . PRO   A 1 174 ? -26.66700 -9.89000  18.12700  1.000 25.72670 ?  154 PRO   A CD    1 
ATOM   1170 N  N     . ALA   A 1 175 ? -25.85200 -11.94700 21.09300  1.000 20.26617 ?  155 ALA   A N     1 
ATOM   1171 C  CA    . ALA   A 1 175 ? -25.76000 -12.58800 22.40300  1.000 23.64292 ?  155 ALA   A CA    1 
ATOM   1172 C  C     . ALA   A 1 175 ? -26.19100 -14.04900 22.32200  1.000 20.68733 ?  155 ALA   A C     1 
ATOM   1173 O  O     . ALA   A 1 175 ? -25.61800 -14.91000 22.99800  1.000 22.50929 ?  155 ALA   A O     1 
ATOM   1174 C  CB    . ALA   A 1 175 ? -26.59200 -11.82000 23.43400  1.000 23.08126 ?  155 ALA   A CB    1 
ATOM   1175 N  N     . ALA   A 1 176 ? -27.18600 -14.35100 21.49300  1.000 23.39203 ?  156 ALA   A N     1 
ATOM   1176 C  CA    . ALA   A 1 176 ? -27.63500 -15.73100 21.38900  1.000 25.67011 ?  156 ALA   A CA    1 
ATOM   1177 C  C     . ALA   A 1 176 ? -26.58300 -16.59200 20.70000  1.000 25.88663 ?  156 ALA   A C     1 
ATOM   1178 O  O     . ALA   A 1 176 ? -26.39000 -17.76100 21.05100  1.000 21.07447 ?  156 ALA   A O     1 
ATOM   1179 C  CB    . ALA   A 1 176 ? -28.97500 -15.78400 20.65700  1.000 26.02505 ?  156 ALA   A CB    1 
ATOM   1180 N  N     . PHE   A 1 177 ? -25.89000 -16.02600 19.71200  1.000 22.37915 ?  157 PHE   A N     1 
ATOM   1181 C  CA    . PHE   A 1 177 ? -24.75800 -16.70900 19.10300  1.000 22.60993 ?  157 PHE   A CA    1 
ATOM   1182 C  C     . PHE   A 1 177 ? -23.67400 -17.00200 20.15800  1.000 19.28353 ?  157 PHE   A C     1 
ATOM   1183 O  O     . PHE   A 1 177 ? -23.23000 -18.14600 20.31300  1.000 19.75087 ?  157 PHE   A O     1 
ATOM   1184 C  CB    . PHE   A 1 177 ? -24.24700 -15.82600 17.95300  1.000 21.31704 ?  157 PHE   A CB    1 
ATOM   1185 C  CG    . PHE   A 1 177 ? -22.85200 -16.10400 17.52200  1.000 19.86600 ?  157 PHE   A CG    1 
ATOM   1186 C  CD1   . PHE   A 1 177 ? -22.58400 -17.20300 16.71500  1.000 25.11882 ?  157 PHE   A CD1   1 
ATOM   1187 C  CD2   . PHE   A 1 177 ? -21.81500 -15.25400 17.86300  1.000 25.04602 ?  157 PHE   A CD2   1 
ATOM   1188 C  CE1   . PHE   A 1 177 ? -21.30700 -17.46000 16.27600  1.000 21.68468 ?  157 PHE   A CE1   1 
ATOM   1189 C  CE2   . PHE   A 1 177 ? -20.52100 -15.51500 17.42000  1.000 24.46242 ?  157 PHE   A CE2   1 
ATOM   1190 C  CZ    . PHE   A 1 177 ? -20.27600 -16.63100 16.63400  1.000 21.86172 ?  157 PHE   A CZ    1 
ATOM   1191 N  N     . LEU   A 1 178 ? -23.27200 -15.98200 20.92700  1.000 17.32131 ?  158 LEU   A N     1 
ATOM   1192 C  CA    . LEU   A 1 178 ? -22.17600 -16.15400 21.87900  1.000 18.26407 ?  158 LEU   A CA    1 
ATOM   1193 C  C     . LEU   A 1 178 ? -22.53800 -17.14200 22.98400  1.000 18.54246 ?  158 LEU   A C     1 
ATOM   1194 O  O     . LEU   A 1 178 ? -21.66100 -17.82500 23.53100  1.000 18.14779 ?  158 LEU   A O     1 
ATOM   1195 C  CB    . LEU   A 1 178 ? -21.80300 -14.80200 22.49700  1.000 17.95770 ?  158 LEU   A CB    1 
ATOM   1196 C  CG    . LEU   A 1 178 ? -21.21300 -13.78100 21.49200  1.000 17.82461 ?  158 LEU   A CG    1 
ATOM   1197 C  CD1   . LEU   A 1 178 ? -21.05400 -12.38900 22.14400  1.000 21.36295 ?  158 LEU   A CD1   1 
ATOM   1198 C  CD2   . LEU   A 1 178 ? -19.89600 -14.22900 20.85300  1.000 19.63620 ?  158 LEU   A CD2   1 
ATOM   1199 N  N     . ALA   A 1 179 ? -23.81600 -17.22300 23.34100  1.000 19.35197 ?  159 ALA   A N     1 
ATOM   1200 C  CA    . ALA   A 1 179 ? -24.20600 -18.04900 24.48000  1.000 20.19738 ?  159 ALA   A CA    1 
ATOM   1201 C  C     . ALA   A 1 179 ? -23.97500 -19.53200 24.22000  1.000 24.93391 ?  159 ALA   A C     1 
ATOM   1202 O  O     . ALA   A 1 179 ? -23.97400 -20.32700 25.16800  1.000 20.57048 ?  159 ALA   A O     1 
ATOM   1203 C  CB    . ALA   A 1 179 ? -25.68100 -17.81700 24.81100  1.000 21.49502 ?  159 ALA   A CB    1 
ATOM   1204 N  N     . GLN   A 1 180 ? -23.78400 -19.91600 22.95700  1.000 17.46720 ?  160 GLN   A N     1 
ATOM   1205 C  CA    . GLN   A 1 180 ? -23.56900 -21.30800 22.58900  1.000 17.96730 ?  160 GLN   A CA    1 
ATOM   1206 C  C     . GLN   A 1 180 ? -22.11100 -21.70800 22.71800  1.000 20.85369 ?  160 GLN   A C     1 
ATOM   1207 O  O     . GLN   A 1 180 ? -21.80600 -22.90900 22.82600  1.000 20.26518 ?  160 GLN   A O     1 
ATOM   1208 C  CB    . GLN   A 1 180 ? -24.02700 -21.54900 21.12800  1.000 17.80353 ?  160 GLN   A CB    1 
ATOM   1209 C  CG    . GLN   A 1 180 ? -25.42800 -21.03400 20.80300  1.000 22.75817 ?  160 GLN   A CG    1 
ATOM   1210 C  CD    . GLN   A 1 180 ? -25.72200 -20.99600 19.29800  1.000 20.21544 ?  160 GLN   A CD    1 
ATOM   1211 O  OE1   . GLN   A 1 180 ? -26.51400 -21.78800 18.77600  1.000 23.30849 ?  160 GLN   A OE1   1 
ATOM   1212 N  NE2   . GLN   A 1 180 ? -25.02400 -20.13000 18.58800  1.000 20.28839 ?  160 GLN   A NE2   1 
ATOM   1213 N  N     . LEU   A 1 181 ? -21.21200 -20.73200 22.72800  1.000 17.08949 ?  161 LEU   A N     1 
ATOM   1214 C  CA    . LEU   A 1 181 ? -19.82200 -21.04100 22.43800  1.000 19.82012 ?  161 LEU   A CA    1 
ATOM   1215 C  C     . LEU   A 1 181 ? -19.13800 -21.74600 23.60700  1.000 21.78369 ?  161 LEU   A C     1 
ATOM   1216 O  O     . LEU   A 1 181 ? -18.35800 -22.66200 23.33400  1.000 17.76549 ?  161 LEU   A O     1 
ATOM   1217 C  CB    . LEU   A 1 181 ? -19.05700 -19.77800 21.98700  1.000 17.02674 ?  161 LEU   A CB    1 
ATOM   1218 C  CG    . LEU   A 1 181 ? -19.63400 -19.14100 20.71100  1.000 17.44660 ?  161 LEU   A CG    1 
ATOM   1219 C  CD1   . LEU   A 1 181 ? -18.89700 -17.83700 20.33000  1.000 20.64835 ?  161 LEU   A CD1   1 
ATOM   1220 C  CD2   . LEU   A 1 181 ? -19.54300 -20.14400 19.55600  1.000 17.75152 ?  161 LEU   A CD2   1 
ATOM   1221 N  N     . PRO   A 1 182 ? -19.38900 -21.41200 24.89400  1.000 19.16955 ?  162 PRO   A N     1 
ATOM   1222 C  CA    . PRO   A 1 182 ? -18.71900 -22.19700 25.95800  1.000 18.51622 ?  162 PRO   A CA    1 
ATOM   1223 C  C     . PRO   A 1 182 ? -18.99500 -23.67500 25.83700  1.000 19.71128 ?  162 PRO   A C     1 
ATOM   1224 O  O     . PRO   A 1 182 ? -18.09200 -24.50200 26.02800  1.000 21.65168 ?  162 PRO   A O     1 
ATOM   1225 C  CB    . PRO   A 1 182 ? -19.29300 -21.61600 27.26000  1.000 18.91659 ?  162 PRO   A CB    1 
ATOM   1226 C  CG    . PRO   A 1 182 ? -19.65200 -20.17900 26.91300  1.000 19.22778 ?  162 PRO   A CG    1 
ATOM   1227 C  CD    . PRO   A 1 182 ? -20.13300 -20.25300 25.44400  1.000 16.81221 ?  162 PRO   A CD    1 
ATOM   1228 N  N     . ALA   A 1 183 ? -20.22800 -24.03400 25.49100  1.000 18.19969 ?  163 ALA   A N     1 
ATOM   1229 C  CA    . ALA   A 1 183 ? -20.57700 -25.44300 25.37000  1.000 20.17308 ?  163 ALA   A CA    1 
ATOM   1230 C  C     . ALA   A 1 183 ? -20.01900 -26.07900 24.10400  1.000 20.37229 ?  163 ALA   A C     1 
ATOM   1231 O  O     . ALA   A 1 183 ? -19.88800 -27.30500 24.05200  1.000 20.01148 ?  163 ALA   A O     1 
ATOM   1232 C  CB    . ALA   A 1 183 ? -22.10700 -25.61000 25.39300  1.000 19.30192 ?  163 ALA   A CB    1 
ATOM   1233 N  N     . LEU   A 1 184 ? -19.66700 -25.27200 23.09900  1.000 17.73755 ?  164 LEU   A N     1 
ATOM   1234 C  CA    . LEU   A 1 184 ? -19.18200 -25.79900 21.82800  1.000 17.73954 ?  164 LEU   A CA    1 
ATOM   1235 C  C     . LEU   A 1 184 ? -17.67600 -26.00100 21.77900  1.000 19.77317 ?  164 LEU   A C     1 
ATOM   1236 O  O     . LEU   A 1 184 ? -17.20000 -26.66900 20.86000  1.000 21.01501 ?  164 LEU   A O     1 
ATOM   1237 C  CB    . LEU   A 1 184 ? -19.58000 -24.86000 20.67800  1.000 18.39019 ?  164 LEU   A CB    1 
ATOM   1238 C  CG    . LEU   A 1 184 ? -21.04300 -24.91500 20.22700  1.000 19.17202 ?  164 LEU   A CG    1 
ATOM   1239 C  CD1   . LEU   A 1 184 ? -21.33800 -23.81300 19.18500  1.000 17.35912 ?  164 LEU   A CD1   1 
ATOM   1240 C  CD2   . LEU   A 1 184 ? -21.36900 -26.29600 19.62500  1.000 22.13520 ?  164 LEU   A CD2   1 
ATOM   1241 N  N     . VAL   A 1 185 ? -16.90400 -25.43500 22.71100  1.000 20.04888 ?  165 VAL   A N     1 
ATOM   1242 C  CA    . VAL   A 1 185 ? -15.44600 -25.53600 22.65700  1.000 22.56980 ?  165 VAL   A CA    1 
ATOM   1243 C  C     . VAL   A 1 185 ? -14.97900 -26.38100 23.83600  1.000 19.74217 ?  165 VAL   A C     1 
ATOM   1244 O  O     . VAL   A 1 185 ? -15.33500 -26.09100 24.98000  1.000 21.19517 ?  165 VAL   A O     1 
ATOM   1245 C  CB    . VAL   A 1 185 ? -14.76500 -24.15000 22.67900  1.000 18.97070 ?  165 VAL   A CB    1 
ATOM   1246 C  CG1   . VAL   A 1 185 ? -13.25600 -24.32700 22.49700  1.000 20.99495 ?  165 VAL   A CG1   1 
ATOM   1247 C  CG2   . VAL   A 1 185 ? -15.29300 -23.25100 21.55200  1.000 21.66238 ?  165 VAL   A CG2   1 
ATOM   1248 N  N     . ARG   A 1 186 ? -14.15700 -27.39700 23.55400  1.000 21.85266 ?  166 ARG   A N     1 
ATOM   1249 C  CA    . ARG   A 1 186 ? -13.58100 -28.22000 24.60700  1.000 25.78920 ?  166 ARG   A CA    1 
ATOM   1250 C  C     . ARG   A 1 186 ? -12.63300 -27.37400 25.44400  1.000 25.58002 ?  166 ARG   A C     1 
ATOM   1251 O  O     . ARG   A 1 186 ? -11.97400 -26.47800 24.90900  1.000 22.65026 ?  166 ARG   A O     1 
ATOM   1252 C  CB    . ARG   A 1 186 ? -12.78900 -29.38800 24.01500  1.000 25.50621 ?  166 ARG   A CB    1 
ATOM   1253 C  CG    . ARG   A 1 186 ? -13.50400 -30.15600 22.92800  1.000 34.16184 ?  166 ARG   A CG    1 
ATOM   1254 C  CD    . ARG   A 1 186 ? -12.61600 -31.26100 22.34300  1.000 38.47399 ?  166 ARG   A CD    1 
ATOM   1255 N  NE    . ARG   A 1 186 ? -12.68200 -32.44800 23.18100  1.000 53.77562 ?  166 ARG   A NE    1 
ATOM   1256 C  CZ    . ARG   A 1 186 ? -13.67200 -33.32800 23.12300  1.000 55.46746 ?  166 ARG   A CZ    1 
ATOM   1257 N  NH1   . ARG   A 1 186 ? -14.60700 -33.25000 22.19000  1.000 48.47127 ?  166 ARG   A NH1   1 
ATOM   1258 N  NH2   . ARG   A 1 186 ? -13.73400 -34.30000 24.03000  1.000 59.26751 ?  166 ARG   A NH2   1 
ATOM   1259 N  N     . PRO   A 1 187 ? -12.50100 -27.66200 26.74200  1.000 23.06253 ?  167 PRO   A N     1 
ATOM   1260 C  CA    . PRO   A 1 187 ? -11.51000 -26.93000 27.53900  1.000 22.32011 ?  167 PRO   A CA    1 
ATOM   1261 C  C     . PRO   A 1 187 ? -10.12300 -27.09500 26.94100  1.000 22.82157 ?  167 PRO   A C     1 
ATOM   1262 O  O     . PRO   A 1 187 ? -9.73400  -28.19200 26.54100  1.000 24.11028 ?  167 PRO   A O     1 
ATOM   1263 C  CB    . PRO   A 1 187 ? -11.61500 -27.58600 28.92700  1.000 26.32474 ?  167 PRO   A CB    1 
ATOM   1264 C  CG    . PRO   A 1 187 ? -13.05200 -27.98900 29.00200  1.000 25.90521 ?  167 PRO   A CG    1 
ATOM   1265 C  CD    . PRO   A 1 187 ? -13.36700 -28.49500 27.59800  1.000 25.11034 ?  167 PRO   A CD    1 
ATOM   1266 N  N     . GLY   A 1 188 ? -9.37800  -25.98500 26.88500  1.000 24.61755 ?  168 GLY   A N     1 
ATOM   1267 C  CA    . GLY   A 1 188 ? -8.09900  -25.95700 26.21400  1.000 23.62582 ?  168 GLY   A CA    1 
ATOM   1268 C  C     . GLY   A 1 188 ? -8.16700  -25.62700 24.73300  1.000 22.62218 ?  168 GLY   A C     1 
ATOM   1269 O  O     . GLY   A 1 188 ? -7.11200  -25.42800 24.10600  1.000 21.98380 ?  168 GLY   A O     1 
ATOM   1270 N  N     . GLY   A 1 189 ? -9.36400  -25.59500 24.14900  1.000 18.46950 ?  169 GLY   A N     1 
ATOM   1271 C  CA    . GLY   A 1 189 ? -9.51300  -25.25800 22.74000  1.000 16.64687 ?  169 GLY   A CA    1 
ATOM   1272 C  C     . GLY   A 1 189 ? -9.48200  -23.76600 22.52500  1.000 18.54841 ?  169 GLY   A C     1 
ATOM   1273 O  O     . GLY   A 1 189 ? -9.36900  -22.96600 23.46300  1.000 19.24474 ?  169 GLY   A O     1 
ATOM   1274 N  N     . LEU   A 1 190 ? -9.62300  -23.38000 21.24800  1.000 18.01805 ?  170 LEU   A N     1 
ATOM   1275 C  CA    . LEU   A 1 190 ? -9.44200  -21.99600 20.81700  1.000 16.53915 ?  170 LEU   A CA    1 
ATOM   1276 C  C     . LEU   A 1 190 ? -10.68400 -21.51000 20.07200  1.000 17.02238 ?  170 LEU   A C     1 
ATOM   1277 O  O     . LEU   A 1 190 ? -11.20500 -22.21800 19.19600  1.000 19.08432 ?  170 LEU   A O     1 
ATOM   1278 C  CB    . LEU   A 1 190 ? -8.21000  -21.88000 19.89900  1.000 21.98113 ?  170 LEU   A CB    1 
ATOM   1279 C  CG    . LEU   A 1 190 ? -7.91300  -20.42800 19.47000  1.000 20.44658 ?  170 LEU   A CG    1 
ATOM   1280 C  CD1   . LEU   A 1 190 ? -7.35800  -19.63000 20.60800  1.000 23.11486 ?  170 LEU   A CD1   1 
ATOM   1281 C  CD2   . LEU   A 1 190 ? -7.00700  -20.37000 18.22800  1.000 22.75177 ?  170 LEU   A CD2   1 
ATOM   1282 N  N     . LEU   A 1 191 ? -11.12800 -20.29900 20.40000  1.000 19.16980 ?  171 LEU   A N     1 
ATOM   1283 C  CA    . LEU   A 1 191 ? -12.16900 -19.59600 19.65900  1.000 16.82787 ?  171 LEU   A CA    1 
ATOM   1284 C  C     . LEU   A 1 191 ? -11.53000 -18.36300 19.03300  1.000 16.94724 ?  171 LEU   A C     1 
ATOM   1285 O  O     . LEU   A 1 191 ? -10.80600 -17.63000 19.71800  1.000 17.71241 ?  171 LEU   A O     1 
ATOM   1286 C  CB    . LEU   A 1 191 ? -13.32600 -19.17600 20.59800  1.000 16.95373 ?  171 LEU   A CB    1 
ATOM   1287 C  CG    . LEU   A 1 191 ? -14.30300 -18.09600 20.10500  1.000 19.73421 ?  171 LEU   A CG    1 
ATOM   1288 C  CD1   . LEU   A 1 191 ? -15.14000 -18.64500 18.92000  1.000 20.78740 ?  171 LEU   A CD1   1 
ATOM   1289 C  CD2   . LEU   A 1 191 ? -15.21300 -17.59200 21.28800  1.000 20.64155 ?  171 LEU   A CD2   1 
ATOM   1290 N  N     . MET   A 1 192 ? -11.75500 -18.15200 17.73200  1.000 17.78183 ?  172 MET   A N     1 
ATOM   1291 C  CA    . MET   A 1 192 ? -11.26200 -16.95200 17.05800  1.000 16.68673 ?  172 MET   A CA    1 
ATOM   1292 C  C     . MET   A 1 192 ? -12.41600 -16.23700 16.37800  1.000 16.64207 ?  172 MET   A C     1 
ATOM   1293 O  O     . MET   A 1 192 ? -13.11600 -16.81900 15.54500  1.000 19.00618 ?  172 MET   A O     1 
ATOM   1294 C  CB    . MET   A 1 192 ? -10.14400 -17.26800 16.06200  1.000 16.17809 ?  172 MET   A CB    1 
ATOM   1295 C  CG    . MET   A 1 192 ? -9.65100  -16.02800 15.25700  1.000 16.47260 ?  172 MET   A CG    1 
ATOM   1296 S  SD    . MET   A 1 192 ? -8.33000  -16.48300 14.12200  1.000 20.46318 ?  172 MET   A SD    1 
ATOM   1297 C  CE    . MET   A 1 192 ? -7.78900  -14.86600 13.55200  1.000 18.88659 ?  172 MET   A CE    1 
ATOM   1298 N  N     . ILE   A 1 193 ? -12.60600 -14.98100 16.75100  1.000 16.30516 ?  173 ILE   A N     1 
ATOM   1299 C  CA    . ILE   A 1 193 ? -13.64000 -14.11600 16.20200  1.000 15.10783 ?  173 ILE   A CA    1 
ATOM   1300 C  C     . ILE   A 1 193 ? -12.93400 -12.96100 15.50400  1.000 17.41205 ?  173 ILE   A C     1 
ATOM   1301 O  O     . ILE   A 1 193 ? -12.01600 -12.36600 16.07200  1.000 17.40365 ?  173 ILE   A O     1 
ATOM   1302 C  CB    . ILE   A 1 193 ? -14.57200 -13.59500 17.32100  1.000 18.54818 ?  173 ILE   A CB    1 
ATOM   1303 C  CG1   . ILE   A 1 193 ? -15.48400 -14.71200 17.83700  1.000 18.04455 ?  173 ILE   A CG1   1 
ATOM   1304 C  CG2   . ILE   A 1 193 ? -15.37500 -12.37800 16.88900  1.000 18.07562 ?  173 ILE   A CG2   1 
ATOM   1305 C  CD1   . ILE   A 1 193 ? -16.09600 -14.39400 19.18100  1.000 17.33982 ?  173 ILE   A CD1   1 
ATOM   1306 N  N     . THR   A 1 194 ? -13.33200 -12.65600 14.26900  1.000 16.71182 ?  174 THR   A N     1 
ATOM   1307 C  CA    . THR   A 1 194 ? -12.84200 -11.44000 13.63200  1.000 14.75341 ?  174 THR   A CA    1 
ATOM   1308 C  C     . THR   A 1 194 ? -14.03000 -10.61100 13.17500  1.000 17.82576 ?  174 THR   A C     1 
ATOM   1309 O  O     . THR   A 1 194 ? -15.07700 -11.14800 12.82400  1.000 17.80112 ?  174 THR   A O     1 
ATOM   1310 C  CB    . THR   A 1 194 ? -11.92000 -11.70500 12.40700  1.000 17.27592 ?  174 THR   A CB    1 
ATOM   1311 O  OG1   . THR   A 1 194 ? -12.71000 -12.19100 11.30400  1.000 17.10833 ?  174 THR   A OG1   1 
ATOM   1312 C  CG2   . THR   A 1 194 ? -10.85400 -12.73900 12.73300  1.000 18.46311 ?  174 THR   A CG2   1 
ATOM   1313 N  N     . SER   A 1 195 ? -13.86500 -9.30600  13.20900  1.000 15.85399 ?  175 SER   A N     1 
ATOM   1314 C  CA    . SER   A 1 195 ? -14.92900 -8.44000  12.71000  1.000 17.21895 ?  175 SER   A CA    1 
ATOM   1315 C  C     . SER   A 1 195 ? -14.42100 -7.01800  12.57300  1.000 15.96957 ?  175 SER   A C     1 
ATOM   1316 O  O     . SER   A 1 195 ? -13.64600 -6.54600  13.41900  1.000 18.95543 ?  175 SER   A O     1 
ATOM   1317 C  CB    . SER   A 1 195 ? -16.13300 -8.44000  13.66000  1.000 23.37246 ?  175 SER   A CB    1 
ATOM   1318 O  OG    . SER   A 1 195 ? -17.17600 -7.60200  13.16200  1.000 18.82088 ?  175 SER   A OG    1 
ATOM   1319 N  N     . PRO   A 1 196 ? -14.91600 -6.26900  11.55700  1.000 17.59314 ?  176 PRO   A N     1 
ATOM   1320 C  CA    . PRO   A 1 196 ? -14.66500 -4.83500  11.48100  1.000 14.44213 ?  176 PRO   A CA    1 
ATOM   1321 C  C     . PRO   A 1 196 ? -15.73400 -4.04100  12.24500  1.000 18.34285 ?  176 PRO   A C     1 
ATOM   1322 O  O     . PRO   A 1 196 ? -15.65100 -2.85100  12.26200  1.000 19.03568 ?  176 PRO   A O     1 
ATOM   1323 C  CB    . PRO   A 1 196 ? -14.83600 -4.52300  9.99900   1.000 21.53743 ?  176 PRO   A CB    1 
ATOM   1324 C  CG    . PRO   A 1 196 ? -15.88700 -5.47700  9.53600   1.000 21.82184 ?  176 PRO   A CG    1 
ATOM   1325 C  CD    . PRO   A 1 196 ? -15.58400 -6.73200  10.31500  1.000 19.11077 ?  176 PRO   A CD    1 
ATOM   1326 N  N     . TYR   A 1 197 ? -16.68800 -4.73900  12.85400  1.000 16.69110 ?  177 TYR   A N     1 
ATOM   1327 C  CA    . TYR   A 1 197 ? -17.72000 -4.08000  13.70300  1.000 15.19501 ?  177 TYR   A CA    1 
ATOM   1328 C  C     . TYR   A 1 197 ? -18.55400 -3.10000  12.86900  1.000 20.27023 ?  177 TYR   A C     1 
ATOM   1329 O  O     . TYR   A 1 197 ? -18.85200 -2.00700  13.34900  1.000 17.80293 ?  177 TYR   A O     1 
ATOM   1330 C  CB    . TYR   A 1 197 ? -17.06700 -3.46700  14.94700  1.000 17.09810 ?  177 TYR   A CB    1 
ATOM   1331 C  CG    . TYR   A 1 197 ? -16.16800 -4.38100  15.74000  1.000 20.48962 ?  177 TYR   A CG    1 
ATOM   1332 C  CD1   . TYR   A 1 197 ? -16.57200 -5.65100  16.11200  1.000 20.65620 ?  177 TYR   A CD1   1 
ATOM   1333 C  CD2   . TYR   A 1 197 ? -14.91700 -3.95900  16.14700  1.000 17.34176 ?  177 TYR   A CD2   1 
ATOM   1334 C  CE1   . TYR   A 1 197 ? -15.74900 -6.48100  16.85600  1.000 19.15521 ?  177 TYR   A CE1   1 
ATOM   1335 C  CE2   . TYR   A 1 197 ? -14.08200 -4.77400  16.88800  1.000 20.71775 ?  177 TYR   A CE2   1 
ATOM   1336 C  CZ    . TYR   A 1 197 ? -14.49700 -6.04200  17.24400  1.000 18.59826 ?  177 TYR   A CZ    1 
ATOM   1337 O  OH    . TYR   A 1 197 ? -13.66100 -6.84100  17.98200  1.000 19.74205 ?  177 TYR   A OH    1 
ATOM   1338 N  N     . THR   A 1 198 ? -18.93000 -3.52600  11.66400  1.000 17.64607 ?  178 THR   A N     1 
ATOM   1339 C  CA    . THR   A 1 198 ? -19.79600 -2.68900  10.79500  1.000 17.16724 ?  178 THR   A CA    1 
ATOM   1340 C  C     . THR   A 1 198 ? -21.23600 -2.90000  11.25400  1.000 17.58269 ?  178 THR   A C     1 
ATOM   1341 O  O     . THR   A 1 198 ? -21.97000 -3.62500  10.60100  1.000 18.34392 ?  178 THR   A O     1 
ATOM   1342 C  CB    . THR   A 1 198 ? -19.52800 -2.97200  9.31500   1.000 17.14685 ?  178 THR   A CB    1 
ATOM   1343 O  OG1   . THR   A 1 198 ? -18.13000 -2.78100  9.10600   1.000 28.53188 ?  178 THR   A OG1   1 
ATOM   1344 C  CG2   . THR   A 1 198 ? -20.30600 -2.06600  8.38800   1.000 18.29685 ?  178 THR   A CG2   1 
ATOM   1345 N  N     . LEU   A 1 199 ? -21.57500 -2.25900  12.36700  1.000 18.51184 ?  179 LEU   A N     1 
ATOM   1346 C  CA    . LEU   A 1 199 ? -22.92500 -2.42100  12.95600  1.000 18.45722 ?  179 LEU   A CA    1 
ATOM   1347 C  C     . LEU   A 1 199 ? -23.96700 -1.66800  12.13100  1.000 22.83612 ?  179 LEU   A C     1 
ATOM   1348 O  O     . LEU   A 1 199 ? -23.81400 -0.46700  11.90500  1.000 21.02351 ?  179 LEU   A O     1 
ATOM   1349 C  CB    . LEU   A 1 199 ? -22.90100 -1.95200  14.40900  1.000 22.05241 ?  179 LEU   A CB    1 
ATOM   1350 C  CG    . LEU   A 1 199 ? -21.90200 -2.67400  15.30600  1.000 19.77377 ?  179 LEU   A CG    1 
ATOM   1351 C  CD1   . LEU   A 1 199 ? -21.93800 -2.10600  16.71400  1.000 22.71055 ?  179 LEU   A CD1   1 
ATOM   1352 C  CD2   . LEU   A 1 199 ? -22.18300 -4.16500  15.32300  1.000 26.94923 ?  179 LEU   A CD2   1 
ATOM   1353 N  N     . LEU   A 1 200 ? -24.99300 -2.39100  11.74700  1.000 20.33484 ?  180 LEU   A N     1 
ATOM   1354 C  CA    . LEU   A 1 200 ? -26.05300 -1.84500  10.83800  1.000 22.50169 ?  180 LEU   A CA    1 
ATOM   1355 C  C     . LEU   A 1 200 ? -27.42400 -2.37400  11.24400  1.000 23.13783 ?  180 LEU   A C     1 
ATOM   1356 O  O     . LEU   A 1 200 ? -27.56700 -3.58800  11.42400  1.000 22.58311 ?  180 LEU   A O     1 
ATOM   1357 C  CB    . LEU   A 1 200 ? -25.77100 -2.25000  9.39200   1.000 22.23169 ?  180 LEU   A CB    1 
ATOM   1358 C  CG    . LEU   A 1 200 ? -24.49900 -1.70600  8.74200   1.000 21.31553 ?  180 LEU   A CG    1 
ATOM   1359 C  CD1   . LEU   A 1 200 ? -24.25000 -2.46100  7.41600   1.000 24.88668 ?  180 LEU   A CD1   1 
ATOM   1360 C  CD2   . LEU   A 1 200 ? -24.56500 -0.19000  8.55800   1.000 25.81735 ?  180 LEU   A CD2   1 
ATOM   1361 N  N     . PRO   A 1 201 ? -28.45300 -1.53100  11.37300  1.000 24.24819 ?  181 PRO   A N     1 
ATOM   1362 C  CA    . PRO   A 1 201 ? -29.77700 -2.07200  11.72500  1.000 23.83328 ?  181 PRO   A CA    1 
ATOM   1363 C  C     . PRO   A 1 201 ? -30.30200 -3.08100  10.72500  1.000 25.95500 ?  181 PRO   A C     1 
ATOM   1364 O  O     . PRO   A 1 201 ? -31.11900 -3.92400  11.12400  1.000 29.04876 ?  181 PRO   A O     1 
ATOM   1365 C  CB    . PRO   A 1 201 ? -30.66800 -0.82300  11.79400  1.000 30.83204 ?  181 PRO   A CB    1 
ATOM   1366 C  CG    . PRO   A 1 201 ? -29.71200 0.29600   12.00200  1.000 35.15657 ?  181 PRO   A CG    1 
ATOM   1367 C  CD    . PRO   A 1 201 ? -28.49500 -0.06500  11.21700  1.000 26.76564 ?  181 PRO   A CD    1 
ATOM   1368 N  N     . GLU   A 1 202 ? -29.86200 -3.01500  9.44600   1.000 23.86192 ?  182 GLU   A N     1 
ATOM   1369 C  CA    . GLU   A 1 202 ? -30.24700 -4.00600  8.44400   1.000 26.23070 ?  182 GLU   A CA    1 
ATOM   1370 C  C     . GLU   A 1 202 ? -29.91900 -5.41200  8.92000   1.000 24.96293 ?  182 GLU   A C     1 
ATOM   1371 O  O     . GLU   A 1 202 ? -30.61000 -6.37600  8.55900   1.000 26.58969 ?  182 GLU   A O     1 
ATOM   1372 C  CB    . GLU   A 1 202 ? -29.51500 -3.77600  7.10400   1.000 26.70295 ?  182 GLU   A CB    1 
ATOM   1373 C  CG    . GLU   A 1 202 ? -29.05000 -2.36300  6.80800   1.000 40.17166 ?  182 GLU   A CG    1 
ATOM   1374 C  CD    . GLU   A 1 202 ? -28.06100 -2.31400  5.62800   1.000 50.80943 ?  182 GLU   A CD    1 
ATOM   1375 O  OE1   . GLU   A 1 202 ? -27.93500 -3.32500  4.87800   1.000 44.35644 ?  182 GLU   A OE1   1 
ATOM   1376 O  OE2   . GLU   A 1 202 ? -27.42100 -1.25200  5.44400   1.000 48.96392 -1 182 GLU   A OE2   1 
ATOM   1377 N  N     . PHE   A 1 203 ? -28.85200 -5.55300  9.71300   1.000 25.58356 ?  183 PHE   A N     1 
ATOM   1378 C  CA    . PHE   A 1 203 ? -28.37200 -6.86500  10.11900  1.000 23.76536 ?  183 PHE   A CA    1 
ATOM   1379 C  C     . PHE   A 1 203 ? -28.54900 -7.15800  11.59700  1.000 22.38102 ?  183 PHE   A C     1 
ATOM   1380 O  O     . PHE   A 1 203 ? -28.77700 -8.31700  11.95100  1.000 22.87552 ?  183 PHE   A O     1 
ATOM   1381 C  CB    . PHE   A 1 203 ? -26.89100 -7.01900  9.75800   1.000 20.02667 ?  183 PHE   A CB    1 
ATOM   1382 C  CG    . PHE   A 1 203 ? -26.65300 -7.08300  8.28100   1.000 21.09050 ?  183 PHE   A CG    1 
ATOM   1383 C  CD1   . PHE   A 1 203 ? -27.03900 -8.19800  7.54600   1.000 27.01325 ?  183 PHE   A CD1   1 
ATOM   1384 C  CD2   . PHE   A 1 203 ? -26.06600 -6.01800  7.61800   1.000 26.06654 ?  183 PHE   A CD2   1 
ATOM   1385 C  CE1   . PHE   A 1 203 ? -26.83700 -8.24700  6.17800   1.000 27.84966 ?  183 PHE   A CE1   1 
ATOM   1386 C  CE2   . PHE   A 1 203 ? -25.86700 -6.07800  6.24600   1.000 27.23906 ?  183 PHE   A CE2   1 
ATOM   1387 C  CZ    . PHE   A 1 203 ? -26.25500 -7.19200  5.53900   1.000 29.30718 ?  183 PHE   A CZ    1 
ATOM   1388 N  N     . THR   A 1 204 ? -28.44800 -6.15000  12.46600  1.000 19.79815 ?  184 THR   A N     1 
ATOM   1389 C  CA    . THR   A 1 204 ? -28.65400 -6.33300  13.91000  1.000 21.62809 ?  184 THR   A CA    1 
ATOM   1390 C  C     . THR   A 1 204 ? -29.57200 -5.23300  14.42100  1.000 21.05656 ?  184 THR   A C     1 
ATOM   1391 O  O     . THR   A 1 204 ? -29.17300 -4.04900  14.40300  1.000 21.75932 ?  184 THR   A O     1 
ATOM   1392 C  CB    . THR   A 1 204 ? -27.34300 -6.27700  14.70100  1.000 22.76464 ?  184 THR   A CB    1 
ATOM   1393 O  OG1   . THR   A 1 204 ? -26.33400 -7.06000  14.05200  1.000 21.39330 ?  184 THR   A OG1   1 
ATOM   1394 C  CG2   . THR   A 1 204 ? -27.56100 -6.75500  16.17000  1.000 19.18692 ?  184 THR   A CG2   1 
ATOM   1395 N  N     . PRO   A 1 205 ? -30.76800 -5.56500  14.96200  1.000 23.81989 ?  185 PRO   A N     1 
ATOM   1396 C  CA    . PRO   A 1 205 ? -31.58000 -4.54900  15.61300  1.000 27.92527 ?  185 PRO   A CA    1 
ATOM   1397 C  C     . PRO   A 1 205 ? -30.78300 -3.85700  16.72800  1.000 24.60481 ?  185 PRO   A C     1 
ATOM   1398 O  O     . PRO   A 1 205 ? -30.10100 -4.51600  17.44500  1.000 24.26796 ?  185 PRO   A O     1 
ATOM   1399 C  CB    . PRO   A 1 205 ? -32.74300 -5.34900  16.18200  1.000 27.87902 ?  185 PRO   A CB    1 
ATOM   1400 C  CG    . PRO   A 1 205 ? -32.88100 -6.52700  15.27200  1.000 34.12406 ?  185 PRO   A CG    1 
ATOM   1401 C  CD    . PRO   A 1 205 ? -31.44900 -6.87800  14.95600  1.000 26.36942 ?  185 PRO   A CD    1 
ATOM   1402 N  N     . ARG   A 1 206 ? -30.93800 -2.53800  16.85800  1.000 24.29197 ?  186 ARG   A N     1 
ATOM   1403 C  CA    . ARG   A 1 206 ? -30.13200 -1.75100  17.82400  1.000 23.98328 ?  186 ARG   A CA    1 
ATOM   1404 C  C     . ARG   A 1 206 ? -30.23100 -2.31500  19.25300  1.000 22.99985 ?  186 ARG   A C     1 
ATOM   1405 O  O     . ARG   A 1 206 ? -29.22600 -2.33100  19.94500  1.000 23.84924 ?  186 ARG   A O     1 
ATOM   1406 C  CB    . ARG   A 1 206 ? -30.54000 -0.27400  17.71800  1.000 27.68053 ?  186 ARG   A CB    1 
ATOM   1407 C  CG    . ARG   A 1 206 ? -29.99900 0.61900   18.82200  1.000 27.16369 ?  186 ARG   A CG    1 
ATOM   1408 C  CD    . ARG   A 1 206 ? -28.48900 0.67400   18.77400  1.000 28.28323 ?  186 ARG   A CD    1 
ATOM   1409 N  NE    . ARG   A 1 206 ? -27.91100 1.44600   19.85700  1.000 31.72216 ?  186 ARG   A NE    1 
ATOM   1410 C  CZ    . ARG   A 1 206 ? -27.85800 1.05900   21.12400  1.000 30.46333 ?  186 ARG   A CZ    1 
ATOM   1411 N  NH1   . ARG   A 1 206 ? -28.15900 -0.18100  21.45900  1.000 25.21797 ?  186 ARG   A NH1   1 
ATOM   1412 N  NH2   . ARG   A 1 206 ? -27.50300 1.92200   22.05600  1.000 36.85398 ?  186 ARG   A NH2   1 
ATOM   1413 N  N     . GLU   A 1 207 ? -31.40700 -2.77600  19.66300  1.000 25.74588 ?  187 GLU   A N     1 
ATOM   1414 C  CA    . GLU   A 1 207 ? -31.60000 -3.26300  21.05600  1.000 27.34151 ?  187 GLU   A CA    1 
ATOM   1415 C  C     . GLU   A 1 207 ? -30.76700 -4.52700  21.30100  1.000 32.49205 ?  187 GLU   A C     1 
ATOM   1416 O  O     . GLU   A 1 207 ? -30.62100 -4.91300  22.46600  1.000 29.34903 ?  187 GLU   A O     1 
ATOM   1417 C  CB    . GLU   A 1 207 ? -33.08400 -3.55900  21.29600  1.000 32.11420 ?  187 GLU   A CB    1 
ATOM   1418 C  CG    . GLU   A 1 207 ? -33.69000 -4.47700  20.24800  1.000 38.22676 ?  187 GLU   A CG    1 
ATOM   1419 C  CD    . GLU   A 1 207 ? -34.41600 -3.81300  19.08800  1.000 41.92820 ?  187 GLU   A CD    1 
ATOM   1420 O  OE1   . GLU   A 1 207 ? -33.97300 -2.74200  18.64000  1.000 42.26526 ?  187 GLU   A OE1   1 
ATOM   1421 O  OE2   . GLU   A 1 207 ? -35.42000 -4.38300  18.62600  1.000 58.17277 ?  187 GLU   A OE2   1 
ATOM   1422 N  N     . ARG   A 1 208 ? -30.25700 -5.13800  20.23800  1.000 24.54783 ?  188 ARG   A N     1 
ATOM   1423 C  CA    . ARG   A 1 208 ? -29.49400 -6.40500  20.36900  1.000 23.48249 ?  188 ARG   A CA    1 
ATOM   1424 C  C     . ARG   A 1 208 ? -27.99100 -6.15800  20.18400  1.000 23.77941 ?  188 ARG   A C     1 
ATOM   1425 O  O     . ARG   A 1 208 ? -27.24600 -7.12100  20.21700  1.000 24.55375 ?  188 ARG   A O     1 
ATOM   1426 C  CB    . ARG   A 1 208 ? -29.99700 -7.41500  19.33800  1.000 23.88263 ?  188 ARG   A CB    1 
ATOM   1427 C  CG    . ARG   A 1 208 ? -31.49400 -7.67600  19.39100  1.000 33.33259 ?  188 ARG   A CG    1 
ATOM   1428 C  CD    . ARG   A 1 208 ? -31.78900 -9.13400  19.66600  1.000 39.38343 ?  188 ARG   A CD    1 
ATOM   1429 N  NE    . ARG   A 1 208 ? -33.20600 -9.44700  19.57800  1.000 47.00635 ?  188 ARG   A NE    1 
ATOM   1430 N  N     . TRP   A 1 209 ? -27.58400 -4.90600  19.99200  1.000 24.37440 ?  189 TRP   A N     1 
ATOM   1431 C  CA    . TRP   A 1 209 ? -26.15300 -4.64900  19.88900  1.000 23.78557 ?  189 TRP   A CA    1 
ATOM   1432 C  C     . TRP   A 1 209 ? -25.47300 -4.97900  21.21500  1.000 19.67553 ?  189 TRP   A C     1 
ATOM   1433 O  O     . TRP   A 1 209 ? -25.98900 -4.67000  22.29300  1.000 21.75672 ?  189 TRP   A O     1 
ATOM   1434 C  CB    . TRP   A 1 209 ? -25.90100 -3.17700  19.51500  1.000 19.61211 ?  189 TRP   A CB    1 
ATOM   1435 C  CG    . TRP   A 1 209 ? -26.27600 -2.76100  18.10700  1.000 20.62928 ?  189 TRP   A CG    1 
ATOM   1436 C  CD1   . TRP   A 1 209 ? -27.01300 -3.47700  17.17800  1.000 21.54554 ?  189 TRP   A CD1   1 
ATOM   1437 C  CD2   . TRP   A 1 209 ? -25.93700 -1.51400  17.47100  1.000 20.53912 ?  189 TRP   A CD2   1 
ATOM   1438 N  NE1   . TRP   A 1 209 ? -27.13200 -2.73300  16.00000  1.000 20.74398 ?  189 TRP   A NE1   1 
ATOM   1439 C  CE2   . TRP   A 1 209 ? -26.49800 -1.52900  16.17600  1.000 23.83900 ?  189 TRP   A CE2   1 
ATOM   1440 C  CE3   . TRP   A 1 209 ? -25.21100 -0.38300  17.87800  1.000 22.21034 ?  189 TRP   A CE3   1 
ATOM   1441 C  CZ2   . TRP   A 1 209 ? -26.34600 -0.46200  15.28100  1.000 24.02414 ?  189 TRP   A CZ2   1 
ATOM   1442 C  CZ3   . TRP   A 1 209 ? -25.07400 0.69500   16.97600  1.000 19.18835 ?  189 TRP   A CZ3   1 
ATOM   1443 C  CH2   . TRP   A 1 209 ? -25.64000 0.63100   15.69700  1.000 21.62232 ?  189 TRP   A CH2   1 
ATOM   1444 N  N     . ILE   A 1 210 ? -24.29300 -5.60400  21.15200  1.000 20.59024 ?  190 ILE   A N     1 
ATOM   1445 C  CA    . ILE   A 1 210 ? -23.54000 -5.88200  22.37600  1.000 23.99714 ?  190 ILE   A CA    1 
ATOM   1446 C  C     . ILE   A 1 210 ? -22.45000 -4.85800  22.62600  1.000 23.37460 ?  190 ILE   A C     1 
ATOM   1447 O  O     . ILE   A 1 210 ? -21.74900 -4.94300  23.64000  1.000 21.61384 ?  190 ILE   A O     1 
ATOM   1448 C  CB    . ILE   A 1 210 ? -22.94600 -7.31100  22.37500  1.000 23.00849 ?  190 ILE   A CB    1 
ATOM   1449 C  CG1   . ILE   A 1 210 ? -22.04400 -7.55000  21.15600  1.000 21.29412 ?  190 ILE   A CG1   1 
ATOM   1450 C  CG2   . ILE   A 1 210 ? -24.05000 -8.35200  22.45800  1.000 21.80523 ?  190 ILE   A CG2   1 
ATOM   1451 C  CD1   . ILE   A 1 210 ? -21.10600 -8.74000  21.34500  1.000 23.52020 ?  190 ILE   A CD1   1 
ATOM   1452 N  N     . GLY   A 1 211 ? -22.29700 -3.88400  21.73500  1.000 21.40368 ?  191 GLY   A N     1 
ATOM   1453 C  CA    . GLY   A 1 211 ? -21.26700 -2.86400  21.84200  1.000 19.68880 ?  191 GLY   A CA    1 
ATOM   1454 C  C     . GLY   A 1 211 ? -21.53600 -1.81100  20.78100  1.000 18.35521 ?  191 GLY   A C     1 
ATOM   1455 O  O     . GLY   A 1 211 ? -22.51900 -1.89100  20.03600  1.000 22.70993 ?  191 GLY   A O     1 
ATOM   1456 N  N     . GLY   A 1 212 ? -20.63900 -0.82000  20.72000  1.000 18.23278 ?  192 GLY   A N     1 
ATOM   1457 C  CA    . GLY   A 1 212 ? -20.83700 0.29600   19.81000  1.000 20.26721 ?  192 GLY   A CA    1 
ATOM   1458 C  C     . GLY   A 1 212 ? -21.79800 1.35200   20.30100  1.000 18.70367 ?  192 GLY   A C     1 
ATOM   1459 O  O     . GLY   A 1 212 ? -22.51000 1.96300   19.49000  1.000 19.19530 ?  192 GLY   A O     1 
ATOM   1460 N  N     . PHE   A 1 213 ? -21.84000 1.60300   21.61200  1.000 19.30653 ?  193 PHE   A N     1 
ATOM   1461 C  CA    . PHE   A 1 213 ? -22.73600 2.60500   22.17000  1.000 20.23994 ?  193 PHE   A CA    1 
ATOM   1462 C  C     . PHE   A 1 213 ? -22.22200 3.01800   23.54000  1.000 24.19588 ?  193 PHE   A C     1 
ATOM   1463 O  O     . PHE   A 1 213 ? -21.27600 2.43500   24.08600  1.000 22.08824 ?  193 PHE   A O     1 
ATOM   1464 C  CB    . PHE   A 1 213 ? -24.17500 2.09000   22.27800  1.000 22.44143 ?  193 PHE   A CB    1 
ATOM   1465 C  CG    . PHE   A 1 213 ? -24.28800 0.79800   23.03900  1.000 25.99901 ?  193 PHE   A CG    1 
ATOM   1466 C  CD1   . PHE   A 1 213 ? -24.18200 0.76300   24.42000  1.000 26.73955 ?  193 PHE   A CD1   1 
ATOM   1467 C  CD2   . PHE   A 1 213 ? -24.46600 -0.39000  22.35600  1.000 22.82348 ?  193 PHE   A CD2   1 
ATOM   1468 C  CE1   . PHE   A 1 213 ? -24.26400 -0.45000  25.10900  1.000 26.85932 ?  193 PHE   A CE1   1 
ATOM   1469 C  CE2   . PHE   A 1 213 ? -24.56500 -1.60800  23.04100  1.000 23.18338 ?  193 PHE   A CE2   1 
ATOM   1470 C  CZ    . PHE   A 1 213 ? -24.45000 -1.63700  24.39900  1.000 25.69172 ?  193 PHE   A CZ    1 
ATOM   1471 N  N     . GLU   A 1 214 ? -22.87100 4.04300   24.08800  1.000 22.54305 ?  194 GLU   A N     1 
ATOM   1472 C  CA    . GLU   A 1 214 ? -22.60100 4.53400   25.42800  1.000 28.14991 ?  194 GLU   A CA    1 
ATOM   1473 C  C     . GLU   A 1 214 ? -23.65200 3.98200   26.37700  1.000 29.46258 ?  194 GLU   A C     1 
ATOM   1474 O  O     . GLU   A 1 214 ? -24.83400 3.89200   26.03000  1.000 31.17543 ?  194 GLU   A O     1 
ATOM   1475 C  CB    . GLU   A 1 214 ? -22.62200 6.06300   25.43500  1.000 27.29415 ?  194 GLU   A CB    1 
ATOM   1476 C  CG    . GLU   A 1 214 ? -21.23900 6.63600   25.20600  1.000 28.74947 ?  194 GLU   A CG    1 
ATOM   1477 C  CD    . GLU   A 1 214 ? -21.13000 8.09300   25.59400  1.000 40.22979 ?  194 GLU   A CD    1 
ATOM   1478 O  OE1   . GLU   A 1 214 ? -22.10700 8.66300   26.13900  1.000 34.88827 ?  194 GLU   A OE1   1 
ATOM   1479 O  OE2   . GLU   A 1 214 ? -20.06000 8.66700   25.33300  1.000 33.47314 -1 194 GLU   A OE2   1 
ATOM   1480 N  N     . ARG   A 1 215 ? -23.21000 3.58500   27.56800  1.000 29.09137 ?  195 ARG   A N     1 
ATOM   1481 C  CA    . ARG   A 1 215 ? -24.09600 3.09100   28.61300  1.000 39.10272 ?  195 ARG   A CA    1 
ATOM   1482 C  C     . ARG   A 1 215 ? -23.71300 3.78400   29.91000  1.000 32.96683 ?  195 ARG   A C     1 
ATOM   1483 O  O     . ARG   A 1 215 ? -22.52500 3.84300   30.24900  1.000 37.14639 ?  195 ARG   A O     1 
ATOM   1484 C  CB    . ARG   A 1 215 ? -23.98600 1.57700   28.78100  1.000 38.51527 ?  195 ARG   A CB    1 
ATOM   1485 C  CG    . ARG   A 1 215 ? -25.05100 0.98400   29.69300  1.000 32.91459 ?  195 ARG   A CG    1 
ATOM   1486 C  CD    . ARG   A 1 215 ? -24.67800 -0.41600  30.10200  1.000 38.66437 ?  195 ARG   A CD    1 
ATOM   1487 N  NE    . ARG   A 1 215 ? -24.85400 -1.35200  29.00300  1.000 42.46058 ?  195 ARG   A NE    1 
ATOM   1488 C  CZ    . ARG   A 1 215 ? -23.97100 -2.28600  28.68000  1.000 44.19329 ?  195 ARG   A CZ    1 
ATOM   1489 N  NH1   . ARG   A 1 215 ? -22.84100 -2.42700  29.35600  1.000 50.03034 ?  195 ARG   A NH1   1 
ATOM   1490 N  NH2   . ARG   A 1 215 ? -24.23100 -3.10100  27.65900  1.000 40.00057 ?  195 ARG   A NH2   1 
ATOM   1491 N  N     . ASN   A 1 216 ? -24.71300 4.31700   30.61900  1.000 38.26761 ?  196 ASN   A N     1 
ATOM   1492 C  CA    . ASN   A 1 216 ? -24.46800 5.17700   31.77700  1.000 46.17538 ?  196 ASN   A CA    1 
ATOM   1493 C  C     . ASN   A 1 216 ? -23.37300 6.18700   31.46500  1.000 38.44536 ?  196 ASN   A C     1 
ATOM   1494 O  O     . ASN   A 1 216 ? -22.51200 6.45000   32.31000  1.000 35.81645 ?  196 ASN   A O     1 
ATOM   1495 C  CB    . ASN   A 1 216 ? -24.07000 4.36400   33.02100  1.000 42.77211 ?  196 ASN   A CB    1 
ATOM   1496 C  CG    . ASN   A 1 216 ? -24.96500 3.15400   33.25400  1.000 48.04098 ?  196 ASN   A CG    1 
ATOM   1497 O  OD1   . ASN   A 1 216 ? -26.19000 3.23100   33.14300  1.000 55.07484 ?  196 ASN   A OD1   1 
ATOM   1498 N  N     . GLY   A 1 217 ? -23.36400 6.72400   30.24600  1.000 38.09981 ?  197 GLY   A N     1 
ATOM   1499 C  CA    . GLY   A 1 217 ? -22.40700 7.76000   29.89300  1.000 34.74193 ?  197 GLY   A CA    1 
ATOM   1500 C  C     . GLY   A 1 217 ? -20.98000 7.31400   29.65700  1.000 38.38175 ?  197 GLY   A C     1 
ATOM   1501 O  O     . GLY   A 1 217 ? -20.10200 8.17000   29.53900  1.000 35.38406 ?  197 GLY   A O     1 
ATOM   1502 N  N     . GLN   A 1 218 ? -20.70700 6.00600   29.57500  1.000 33.05094 ?  198 GLN   A N     1 
ATOM   1503 C  CA    . GLN   A 1 218 ? -19.37000 5.54800   29.23000  1.000 29.75464 ?  198 GLN   A CA    1 
ATOM   1504 C  C     . GLN   A 1 218 ? -19.43600 4.68000   27.96900  1.000 27.34728 ?  198 GLN   A C     1 
ATOM   1505 O  O     . GLN   A 1 218 ? -20.46600 4.04400   27.70900  1.000 28.51869 ?  198 GLN   A O     1 
ATOM   1506 C  CB    . GLN   A 1 218 ? -18.72700 4.73900   30.36400  1.000 35.02762 ?  198 GLN   A CB    1 
ATOM   1507 N  N     . PRO   A 1 219 ? -18.36100 4.62900   27.18000  1.000 26.46450 ?  199 PRO   A N     1 
ATOM   1508 C  CA    . PRO   A 1 219 ? -18.39100 3.83200   25.94200  1.000 23.48146 ?  199 PRO   A CA    1 
ATOM   1509 C  C     . PRO   A 1 219 ? -18.34200 2.34300   26.25100  1.000 24.05685 ?  199 PRO   A C     1 
ATOM   1510 O  O     . PRO   A 1 219 ? -17.60000 1.89000   27.12600  1.000 25.06725 ?  199 PRO   A O     1 
ATOM   1511 C  CB    . PRO   A 1 219 ? -17.11400 4.26100   25.19900  1.000 26.55266 ?  199 PRO   A CB    1 
ATOM   1512 C  CG    . PRO   A 1 219 ? -16.61700 5.49300   25.95200  1.000 35.77019 ?  199 PRO   A CG    1 
ATOM   1513 C  CD    . PRO   A 1 219 ? -17.05800 5.28300   27.35800  1.000 34.17706 ?  199 PRO   A CD    1 
ATOM   1514 N  N     . VAL   A 1 220 ? -19.11300 1.57800   25.49700  1.000 22.43665 ?  200 VAL   A N     1 
ATOM   1515 C  CA    . VAL   A 1 220 ? -19.05300 0.12600   25.53400  1.000 18.96548 ?  200 VAL   A CA    1 
ATOM   1516 C  C     . VAL   A 1 220 ? -18.65600 -0.28900  24.12400  1.000 20.40120 ?  200 VAL   A C     1 
ATOM   1517 O  O     . VAL   A 1 220 ? -19.46600 -0.17900  23.20300  1.000 22.86632 ?  200 VAL   A O     1 
ATOM   1518 C  CB    . VAL   A 1 220 ? -20.40100 -0.48800  25.93000  1.000 21.02677 ?  200 VAL   A CB    1 
ATOM   1519 C  CG1   . VAL   A 1 220 ? -20.33100 -2.02000  25.95500  1.000 23.20549 ?  200 VAL   A CG1   1 
ATOM   1520 C  CG2   . VAL   A 1 220 ? -20.85600 0.07900   27.27100  1.000 28.04614 ?  200 VAL   A CG2   1 
ATOM   1521 N  N     . ARG   A 1 221 ? -17.40900 -0.71100  23.94400  1.000 22.55643 ?  201 ARG   A N     1 
ATOM   1522 C  CA    . ARG   A 1 221 ? -16.95000 -1.17700  22.63600  1.000 22.67649 ?  201 ARG   A CA    1 
ATOM   1523 C  C     . ARG   A 1 221 ? -17.45800 -2.59000  22.34900  1.000 23.64261 ?  201 ARG   A C     1 
ATOM   1524 O  O     . ARG   A 1 221 ? -17.78400 -3.35800  23.25400  1.000 20.91291 ?  201 ARG   A O     1 
ATOM   1525 C  CB    . ARG   A 1 221 ? -15.42300 -1.14900  22.59300  1.000 23.71746 ?  201 ARG   A CB    1 
ATOM   1526 C  CG    . ARG   A 1 221 ? -14.87700 0.25300   22.63500  1.000 29.68964 ?  201 ARG   A CG    1 
ATOM   1527 C  CD    . ARG   A 1 221 ? -15.27700 0.91500   21.32300  1.000 39.05755 ?  201 ARG   A CD    1 
ATOM   1528 N  NE    . ARG   A 1 221 ? -14.44500 2.06300   20.99100  1.000 45.44731 ?  201 ARG   A NE    1 
ATOM   1529 C  CZ    . ARG   A 1 221 ? -14.09200 2.41000   19.76300  1.000 43.48652 ?  201 ARG   A CZ    1 
ATOM   1530 N  NH1   . ARG   A 1 221 ? -14.30000 1.60800   18.72900  1.000 38.98728 ?  201 ARG   A NH1   1 
ATOM   1531 N  NH2   . ARG   A 1 221 ? -13.50300 3.58800   19.57200  1.000 43.88384 ?  201 ARG   A NH2   1 
ATOM   1532 N  N     . MET   A 1 222 ? -17.49600 -2.94900  21.06200  1.000 21.53746 ?  202 MET   A N     1 
ATOM   1533 C  CA    . MET   A 1 222 ? -17.86800 -4.32200  20.73400  1.000 22.71664 ?  202 MET   A CA    1 
ATOM   1534 C  C     . MET   A 1 222 ? -16.98000 -5.31400  21.47300  1.000 22.36568 ?  202 MET   A C     1 
ATOM   1535 O  O     . MET   A 1 222 ? -17.43600 -6.38600  21.89900  1.000 20.98700 ?  202 MET   A O     1 
ATOM   1536 C  CB    . MET   A 1 222 ? -17.76500 -4.57500  19.23000  1.000 23.74075 ?  202 MET   A CB    1 
ATOM   1537 C  CG    . MET   A 1 222 ? -18.95600 -4.07300  18.49700  1.000 22.13567 ?  202 MET   A CG    1 
ATOM   1538 S  SD    . MET   A 1 222 ? -20.38900 -5.03100  18.93400  1.000 23.05563 ?  202 MET   A SD    1 
ATOM   1539 C  CE    . MET   A 1 222 ? -20.28200 -6.50000  17.85100  1.000 25.79388 ?  202 MET   A CE    1 
ATOM   1540 N  N     . LEU   A 1 223 ? -15.69300 -5.00500  21.59000  1.000 19.26201 ?  203 LEU   A N     1 
ATOM   1541 C  CA    . LEU   A 1 223 ? -14.80400 -5.92900  22.28600  1.000 18.84962 ?  203 LEU   A CA    1 
ATOM   1542 C  C     . LEU   A 1 223 ? -15.18300 -6.05500  23.76200  1.000 22.09220 ?  203 LEU   A C     1 
ATOM   1543 O  O     . LEU   A 1 223 ? -15.09700 -7.14700  24.33900  1.000 21.65970 ?  203 LEU   A O     1 
ATOM   1544 C  CB    . LEU   A 1 223 ? -13.35100 -5.48000  22.12900  1.000 22.38773 ?  203 LEU   A CB    1 
ATOM   1545 C  CG    . LEU   A 1 223 ? -12.33900 -6.43800  22.76600  1.000 27.43359 ?  203 LEU   A CG    1 
ATOM   1546 C  CD1   . LEU   A 1 223 ? -12.42800 -7.87300  22.12500  1.000 20.54636 ?  203 LEU   A CD1   1 
ATOM   1547 C  CD2   . LEU   A 1 223 ? -10.91500 -5.87300  22.66000  1.000 22.33893 ?  203 LEU   A CD2   1 
ATOM   1548 N  N     . ASP   A 1 224 ? -15.62500 -4.95300  24.38600  1.000 23.99331 ?  204 ASP   A N     1 
ATOM   1549 C  CA    . ASP   A 1 224 ? -16.15400 -5.04000  25.75500  1.000 22.10875 ?  204 ASP   A CA    1 
ATOM   1550 C  C     . ASP   A 1 224 ? -17.35700 -5.96400  25.81900  1.000 21.21149 ?  204 ASP   A C     1 
ATOM   1551 O  O     . ASP   A 1 224 ? -17.53300 -6.71200  26.79200  1.000 24.22744 ?  204 ASP   A O     1 
ATOM   1552 C  CB    . ASP   A 1 224 ? -16.56600 -3.65400  26.28100  1.000 20.24097 ?  204 ASP   A CB    1 
ATOM   1553 C  CG    . ASP   A 1 224 ? -15.41200 -2.68600  26.37700  1.000 30.36353 ?  204 ASP   A CG    1 
ATOM   1554 O  OD1   . ASP   A 1 224 ? -14.30500 -3.07700  26.79000  1.000 28.96490 ?  204 ASP   A OD1   1 
ATOM   1555 O  OD2   . ASP   A 1 224 ? -15.62600 -1.51100  26.03500  1.000 29.39509 -1 204 ASP   A OD2   1 
ATOM   1556 N  N     . GLY   A 1 225 ? -18.23100 -5.88700  24.81400  1.000 19.04678 ?  205 GLY   A N     1 
ATOM   1557 C  CA    . GLY   A 1 225 ? -19.37300 -6.78000  24.78600  1.000 20.35623 ?  205 GLY   A CA    1 
ATOM   1558 C  C     . GLY   A 1 225 ? -18.96100 -8.23400  24.64000  1.000 22.21946 ?  205 GLY   A C     1 
ATOM   1559 O  O     . GLY   A 1 225 ? -19.53000 -9.11500  25.28800  1.000 22.89484 ?  205 GLY   A O     1 
ATOM   1560 N  N     . LEU   A 1 226 ? -17.97800 -8.50800  23.76700  1.000 18.51746 ?  206 LEU   A N     1 
ATOM   1561 C  CA    . LEU   A 1 226 ? -17.44200 -9.87000  23.66000  1.000 19.53014 ?  206 LEU   A CA    1 
ATOM   1562 C  C     . LEU   A 1 226 ? -16.92700 -10.37800 25.00700  1.000 18.72469 ?  206 LEU   A C     1 
ATOM   1563 O  O     . LEU   A 1 226 ? -17.21300 -11.51600 25.40200  1.000 19.28601 ?  206 LEU   A O     1 
ATOM   1564 C  CB    . LEU   A 1 226 ? -16.32300 -9.91100  22.62900  1.000 16.19979 ?  206 LEU   A CB    1 
ATOM   1565 C  CG    . LEU   A 1 226 ? -16.80500 -9.74400  21.17900  1.000 16.47791 ?  206 LEU   A CG    1 
ATOM   1566 C  CD1   . LEU   A 1 226 ? -15.59400 -9.67800  20.27400  1.000 20.86488 ?  206 LEU   A CD1   1 
ATOM   1567 C  CD2   . LEU   A 1 226 ? -17.73200 -10.91100 20.73300  1.000 17.76839 ?  206 LEU   A CD2   1 
ATOM   1568 N  N     . ARG   A 1 227 ? -16.17300 -9.54800  25.72000  1.000 18.29667 ?  207 ARG   A N     1 
ATOM   1569 C  CA    . ARG   A 1 227 ? -15.59600 -9.97700  27.01800  1.000 20.41090 ?  207 ARG   A CA    1 
ATOM   1570 C  C     . ARG   A 1 227 ? -16.71500 -10.24400 28.02700  1.000 21.86448 ?  207 ARG   A C     1 
ATOM   1571 O  O     . ARG   A 1 227 ? -16.64800 -11.23900 28.74100  1.000 23.34207 ?  207 ARG   A O     1 
ATOM   1572 C  CB    . ARG   A 1 227 ? -14.68000 -8.89200  27.58000  1.000 20.83053 ?  207 ARG   A CB    1 
ATOM   1573 C  CG    . ARG   A 1 227 ? -13.34400 -8.74100  26.87700  1.000 22.31760 ?  207 ARG   A CG    1 
ATOM   1574 C  CD    . ARG   A 1 227 ? -12.62900 -7.62600  27.60800  1.000 31.28761 ?  207 ARG   A CD    1 
ATOM   1575 N  NE    . ARG   A 1 227 ? -11.25400 -7.46700  27.18000  1.000 39.81633 ?  207 ARG   A NE    1 
ATOM   1576 C  CZ    . ARG   A 1 227 ? -10.20000 -7.72400  27.94200  1.000 39.52461 ?  207 ARG   A CZ    1 
ATOM   1577 N  NH1   . ARG   A 1 227 ? -10.25600 -8.68600  28.84400  1.000 33.73904 ?  207 ARG   A NH1   1 
ATOM   1578 N  NH2   . ARG   A 1 227 ? -9.09400  -7.02100  27.78800  1.000 36.84240 ?  207 ARG   A NH2   1 
ATOM   1579 N  N     . HIS   A 1 228 ? -17.68700 -9.34500  28.08400  1.000 21.01938 ?  208 HIS   A N     1 
ATOM   1580 C  CA    . HIS   A 1 228 ? -18.78300 -9.51800  29.03200  1.000 25.11667 ?  208 HIS   A CA    1 
ATOM   1581 C  C     . HIS   A 1 228 ? -19.47600 -10.86000 28.83300  1.000 28.22570 ?  208 HIS   A C     1 
ATOM   1582 O  O     . HIS   A 1 228 ? -19.82300 -11.54100 29.80800  1.000 26.35650 ?  208 HIS   A O     1 
ATOM   1583 C  CB    . HIS   A 1 228 ? -19.77900 -8.36800  28.87800  1.000 23.30860 ?  208 HIS   A CB    1 
ATOM   1584 C  CG    . HIS   A 1 228 ? -21.09100 -8.60400  29.56500  1.000 28.26131 ?  208 HIS   A CG    1 
ATOM   1585 N  ND1   . HIS   A 1 228 ? -21.24300 -8.49500  30.93200  1.000 37.47710 ?  208 HIS   A ND1   1 
ATOM   1586 C  CD2   . HIS   A 1 228 ? -22.31200 -8.93400  29.07700  1.000 29.33480 ?  208 HIS   A CD2   1 
ATOM   1587 C  CE1   . HIS   A 1 228 ? -22.50000 -8.74700  31.25700  1.000 34.75274 ?  208 HIS   A CE1   1 
ATOM   1588 N  NE2   . HIS   A 1 228 ? -23.17000 -9.01700  30.15000  1.000 35.02714 ?  208 HIS   A NE2   1 
ATOM   1589 N  N     . HIS   A 1 229 ? -19.66900 -11.26700 27.57300  1.000 20.84483 ?  209 HIS   A N     1 
ATOM   1590 C  CA    . HIS   A 1 229 ? -20.40800 -12.48800 27.27800  1.000 20.08012 ?  209 HIS   A CA    1 
ATOM   1591 C  C     . HIS   A 1 229 ? -19.53300 -13.73200 27.34000  1.000 19.50056 ?  209 HIS   A C     1 
ATOM   1592 O  O     . HIS   A 1 229 ? -20.04500 -14.81700 27.62700  1.000 24.98905 ?  209 HIS   A O     1 
ATOM   1593 C  CB    . HIS   A 1 229 ? -21.07500 -12.36900 25.90400  1.000 22.43146 ?  209 HIS   A CB    1 
ATOM   1594 C  CG    . HIS   A 1 229 ? -22.25800 -11.45900 25.89700  1.000 25.53573 ?  209 HIS   A CG    1 
ATOM   1595 N  ND1   . HIS   A 1 229 ? -23.52600 -11.88700 26.23600  1.000 31.83153 ?  209 HIS   A ND1   1 
ATOM   1596 C  CD2   . HIS   A 1 229 ? -22.36400 -10.13100 25.63700  1.000 21.85514 ?  209 HIS   A CD2   1 
ATOM   1597 C  CE1   . HIS   A 1 229 ? -24.36600 -10.86900 26.15400  1.000 35.51570 ?  209 HIS   A CE1   1 
ATOM   1598 N  NE2   . HIS   A 1 229 ? -23.68700 -9.79300  25.79100  1.000 24.49128 ?  209 HIS   A NE2   1 
ATOM   1599 N  N     . LEU   A 1 230 ? -18.23300 -13.61700 27.10400  1.000 19.65921 ?  210 LEU   A N     1 
ATOM   1600 C  CA    . LEU   A 1 230 ? -17.39900 -14.81600 26.98200  1.000 19.31158 ?  210 LEU   A CA    1 
ATOM   1601 C  C     . LEU   A 1 230 ? -16.59800 -15.14600 28.24700  1.000 23.68148 ?  210 LEU   A C     1 
ATOM   1602 O  O     . LEU   A 1 230 ? -16.32100 -16.32600 28.50700  1.000 20.43260 ?  210 LEU   A O     1 
ATOM   1603 C  CB    . LEU   A 1 230 ? -16.45200 -14.65500 25.78400  1.000 17.76482 ?  210 LEU   A CB    1 
ATOM   1604 C  CG    . LEU   A 1 230 ? -17.15200 -14.63200 24.40600  1.000 19.08806 ?  210 LEU   A CG    1 
ATOM   1605 C  CD1   . LEU   A 1 230 ? -16.15300 -14.36700 23.29300  1.000 18.76347 ?  210 LEU   A CD1   1 
ATOM   1606 C  CD2   . LEU   A 1 230 ? -17.87900 -15.97000 24.12500  1.000 19.95786 ?  210 LEU   A CD2   1 
ATOM   1607 N  N     . GLU   A 1 231 ? -16.22500 -14.14900 29.04500  1.000 19.58819 ?  211 GLU   A N     1 
ATOM   1608 C  CA    . GLU   A 1 231 ? -15.42600 -14.36600 30.24800  1.000 21.20805 ?  211 GLU   A CA    1 
ATOM   1609 C  C     . GLU   A 1 231 ? -16.31400 -14.79500 31.41700  1.000 24.54778 ?  211 GLU   A C     1 
ATOM   1610 O  O     . GLU   A 1 231 ? -17.46900 -14.37100 31.51300  1.000 24.32119 ?  211 GLU   A O     1 
ATOM   1611 C  CB    . GLU   A 1 231 ? -14.69900 -13.07400 30.63400  1.000 23.52074 ?  211 GLU   A CB    1 
ATOM   1612 C  CG    . GLU   A 1 231 ? -13.69600 -12.59500 29.58700  1.000 21.35841 ?  211 GLU   A CG    1 
ATOM   1613 C  CD    . GLU   A 1 231 ? -13.04500 -11.26000 29.94200  1.000 28.20173 ?  211 GLU   A CD    1 
ATOM   1614 O  OE1   . GLU   A 1 231 ? -13.59000 -10.51800 30.79400  1.000 28.50533 ?  211 GLU   A OE1   1 
ATOM   1615 O  OE2   . GLU   A 1 231 ? -11.97800 -10.96200 29.35600  1.000 27.39082 -1 211 GLU   A OE2   1 
ATOM   1616 N  N     . PRO   A 1 232 ? -15.77900 -15.61000 32.35900  1.000 21.50568 ?  212 PRO   A N     1 
ATOM   1617 C  CA    . PRO   A 1 232 ? -14.43800 -16.19800 32.39500  1.000 21.05101 ?  212 PRO   A CA    1 
ATOM   1618 C  C     . PRO   A 1 232 ? -14.36800 -17.57300 31.75600  1.000 20.48240 ?  212 PRO   A C     1 
ATOM   1619 O  O     . PRO   A 1 232 ? -13.32000 -18.23100 31.83800  1.000 21.02784 ?  212 PRO   A O     1 
ATOM   1620 C  CB    . PRO   A 1 232 ? -14.16400 -16.27100 33.91400  1.000 22.18576 ?  212 PRO   A CB    1 
ATOM   1621 C  CG    . PRO   A 1 232 ? -15.51000 -16.69300 34.45200  1.000 22.99845 ?  212 PRO   A CG    1 
ATOM   1622 C  CD    . PRO   A 1 232 ? -16.52800 -15.93200 33.59100  1.000 25.59193 ?  212 PRO   A CD    1 
ATOM   1623 N  N     . ASP   A 1 233 ? -15.45900 -18.05600 31.14900  1.000 20.24247 ?  213 ASP   A N     1 
ATOM   1624 C  CA    . ASP   A 1 233 ? -15.43000 -19.34700 30.46500  1.000 22.24278 ?  213 ASP   A CA    1 
ATOM   1625 C  C     . ASP   A 1 233 ? -14.32600 -19.40000 29.42500  1.000 21.86952 ?  213 ASP   A C     1 
ATOM   1626 O  O     . ASP   A 1 233 ? -13.70200 -20.44800 29.21800  1.000 19.56869 ?  213 ASP   A O     1 
ATOM   1627 C  CB    . ASP   A 1 233 ? -16.77400 -19.61300 29.78200  1.000 20.01531 ?  213 ASP   A CB    1 
ATOM   1628 C  CG    . ASP   A 1 233 ? -17.91300 -19.69600 30.74900  1.000 26.62392 ?  213 ASP   A CG    1 
ATOM   1629 O  OD1   . ASP   A 1 233 ? -18.29500 -18.66000 31.35800  1.000 27.45272 ?  213 ASP   A OD1   1 
ATOM   1630 O  OD2   . ASP   A 1 233 ? -18.44100 -20.82800 30.85700  1.000 36.79521 -1 213 ASP   A OD2   1 
ATOM   1631 N  N     . PHE   A 1 234 ? -14.12300 -18.28800 28.70600  1.000 19.04863 ?  214 PHE   A N     1 
ATOM   1632 C  CA    . PHE   A 1 234 ? -12.99300 -18.09900 27.81300  1.000 18.35754 ?  214 PHE   A CA    1 
ATOM   1633 C  C     . PHE   A 1 234 ? -12.07000 -17.06200 28.43200  1.000 19.86357 ?  214 PHE   A C     1 
ATOM   1634 O  O     . PHE   A 1 234 ? -12.52900 -16.16900 29.14600  1.000 21.79696 ?  214 PHE   A O     1 
ATOM   1635 C  CB    . PHE   A 1 234 ? -13.44100 -17.60500 26.41600  1.000 15.44046 ?  214 PHE   A CB    1 
ATOM   1636 C  CG    . PHE   A 1 234 ? -14.16700 -18.64100 25.59600  1.000 19.38384 ?  214 PHE   A CG    1 
ATOM   1637 C  CD1   . PHE   A 1 234 ? -13.47700 -19.52500 24.77600  1.000 18.21751 ?  214 PHE   A CD1   1 
ATOM   1638 C  CD2   . PHE   A 1 234 ? -15.55000 -18.73700 25.66700  1.000 17.97945 ?  214 PHE   A CD2   1 
ATOM   1639 C  CE1   . PHE   A 1 234 ? -14.15200 -20.45400 24.00700  1.000 18.38079 ?  214 PHE   A CE1   1 
ATOM   1640 C  CE2   . PHE   A 1 234 ? -16.23500 -19.68800 24.89700  1.000 17.60901 ?  214 PHE   A CE2   1 
ATOM   1641 C  CZ    . PHE   A 1 234 ? -15.52900 -20.54800 24.07500  1.000 19.36245 ?  214 PHE   A CZ    1 
ATOM   1642 N  N     . VAL   A 1 235 ? -10.77400 -17.15600 28.11700  1.000 17.58948 ?  215 VAL   A N     1 
ATOM   1643 C  CA    . VAL   A 1 235 ? -9.78400  -16.17000 28.53900  1.000 21.54519 ?  215 VAL   A CA    1 
ATOM   1644 C  C     . VAL   A 1 235 ? -9.20700  -15.53100 27.27800  1.000 22.33663 ?  215 VAL   A C     1 
ATOM   1645 O  O     . VAL   A 1 235 ? -8.66200  -16.23200 26.41700  1.000 21.66561 ?  215 VAL   A O     1 
ATOM   1646 C  CB    . VAL   A 1 235 ? -8.67900  -16.81300 29.38900  1.000 25.68563 ?  215 VAL   A CB    1 
ATOM   1647 C  CG1   . VAL   A 1 235 ? -7.61200  -15.79000 29.74200  1.000 27.61682 ?  215 VAL   A CG1   1 
ATOM   1648 C  CG2   . VAL   A 1 235 ? -9.28800  -17.45000 30.64200  1.000 25.69305 ?  215 VAL   A CG2   1 
ATOM   1649 N  N     . LEU   A 1 236 ? -9.31000  -14.21500 27.19800  1.000 19.13857 ?  216 LEU   A N     1 
ATOM   1650 C  CA    . LEU   A 1 236 ? -8.81600  -13.49800 26.00000  1.000 19.64770 ?  216 LEU   A CA    1 
ATOM   1651 C  C     . LEU   A 1 236 ? -7.29100  -13.55400 25.94600  1.000 24.47767 ?  216 LEU   A C     1 
ATOM   1652 O  O     . LEU   A 1 236 ? -6.66500  -13.22100 26.94800  1.000 23.24074 ?  216 LEU   A O     1 
ATOM   1653 C  CB    . LEU   A 1 236 ? -9.31200  -12.05200 26.04300  1.000 18.95594 ?  216 LEU   A CB    1 
ATOM   1654 C  CG    . LEU   A 1 236 ? -8.84100  -11.15700 24.89800  1.000 17.60335 ?  216 LEU   A CG    1 
ATOM   1655 C  CD1   . LEU   A 1 236 ? -9.37300  -11.65300 23.56400  1.000 18.65060 ?  216 LEU   A CD1   1 
ATOM   1656 C  CD2   . LEU   A 1 236 ? -9.25600  -9.71600  25.13600  1.000 21.89235 ?  216 LEU   A CD2   1 
ATOM   1657 N  N     . LEU   A 1 237 ? -6.74600  -14.00200 24.81900  1.000 21.43763 ?  217 LEU   A N     1 
ATOM   1658 C  CA    . LEU   A 1 237 ? -5.28600  -13.96000 24.61200  1.000 26.61488 ?  217 LEU   A CA    1 
ATOM   1659 C  C     . LEU   A 1 237 ? -4.95900  -12.53600 24.17400  1.000 30.08169 ?  217 LEU   A C     1 
ATOM   1660 O  O     . LEU   A 1 237 ? -5.39200  -12.13300 23.09300  1.000 31.90917 ?  217 LEU   A O     1 
ATOM   1661 C  CB    . LEU   A 1 237 ? -4.90400  -14.99400 23.55100  1.000 26.41733 ?  217 LEU   A CB    1 
ATOM   1662 C  CG    . LEU   A 1 237 ? -5.39900  -16.41000 23.83100  1.000 26.17756 ?  217 LEU   A CG    1 
ATOM   1663 C  CD1   . LEU   A 1 237 ? -5.01600  -17.34800 22.70100  1.000 29.75324 ?  217 LEU   A CD1   1 
ATOM   1664 C  CD2   . LEU   A 1 237 ? -4.85400  -16.92200 25.15000  1.000 33.00802 ?  217 LEU   A CD2   1 
ATOM   1665 N  N     . GLU   A 1 238 ? -4.21800  -11.81100 24.99300  1.000 28.67856 ?  218 GLU   A N     1 
ATOM   1666 C  CA    . GLU   A 1 238 ? -3.96100  -10.38300 24.71300  1.000 29.22619 ?  218 GLU   A CA    1 
ATOM   1667 C  C     . GLU   A 1 238 ? -2.60500  -10.22600 24.01500  1.000 38.38421 ?  218 GLU   A C     1 
ATOM   1668 O  O     . GLU   A 1 238 ? -1.68900  -10.98400 24.32600  1.000 36.94782 ?  218 GLU   A O     1 
ATOM   1669 C  CB    . GLU   A 1 238 ? -4.03000  -9.62100  26.03700  1.000 33.19500 ?  218 GLU   A CB    1 
ATOM   1670 C  CG    . GLU   A 1 238 ? -5.38000  -9.70900  26.71800  1.000 33.75133 ?  218 GLU   A CG    1 
ATOM   1671 C  CD    . GLU   A 1 238 ? -5.76200  -8.41100  27.39800  1.000 33.07152 ?  218 GLU   A CD    1 
ATOM   1672 N  N     . PRO   A 1 239 ? -2.46000  -9.27400  23.07200  1.000 33.28825 ?  219 PRO   A N     1 
ATOM   1673 C  CA    . PRO   A 1 239 ? -3.55400  -8.39400  22.70100  1.000 33.81616 ?  219 PRO   A CA    1 
ATOM   1674 C  C     . PRO   A 1 239 ? -4.35200  -8.81800  21.46500  1.000 20.35346 ?  219 PRO   A C     1 
ATOM   1675 O  O     . PRO   A 1 239 ? -3.98500  -9.74300  20.82200  1.000 25.51942 ?  219 PRO   A O     1 
ATOM   1676 C  CB    . PRO   A 1 239 ? -2.77200  -7.16500  22.24800  1.000 32.72567 ?  219 PRO   A CB    1 
ATOM   1677 C  CG    . PRO   A 1 239 ? -1.57200  -7.74200  21.53900  1.000 31.92248 ?  219 PRO   A CG    1 
ATOM   1678 C  CD    . PRO   A 1 239 ? -1.22400  -8.97500  22.34900  1.000 38.88891 ?  219 PRO   A CD    1 
ATOM   1679 N  N     . THR   A 1 240 ? -5.44000  -8.10700  21.20000  1.000 21.93385 ?  220 THR   A N     1 
ATOM   1680 C  CA    . THR   A 1 240 ? -6.16200  -8.33100  19.92800  1.000 19.49615 ?  220 THR   A CA    1 
ATOM   1681 C  C     . THR   A 1 240 ? -5.27000  -7.87200  18.76900  1.000 25.19950 ?  220 THR   A C     1 
ATOM   1682 O  O     . THR   A 1 240 ? -4.33100  -7.12300  19.01800  1.000 22.43183 ?  220 THR   A O     1 
ATOM   1683 C  CB    . THR   A 1 240 ? -7.51700  -7.61800  19.93700  1.000 21.77663 ?  220 THR   A CB    1 
ATOM   1684 O  OG1   . THR   A 1 240 ? -7.29800  -6.22800  20.16200  1.000 25.72725 ?  220 THR   A OG1   1 
ATOM   1685 C  CG2   . THR   A 1 240 ? -8.44900  -8.19000  20.98400  1.000 19.57848 ?  220 THR   A CG2   1 
ATOM   1686 N  N     . ARG   A 1 241 ? -5.60000  -8.28500  17.54500  1.000 21.40132 ?  221 ARG   A N     1 
ATOM   1687 C  CA    . ARG   A 1 241 ? -4.77000  -8.00700  16.36800  1.000 23.23348 ?  221 ARG   A CA    1 
ATOM   1688 C  C     . ARG   A 1 241 ? -5.63100  -7.50100  15.21300  1.000 24.72447 ?  221 ARG   A C     1 
ATOM   1689 O  O     . ARG   A 1 241 ? -6.72000  -8.02200  14.98100  1.000 21.35804 ?  221 ARG   A O     1 
ATOM   1690 C  CB    . ARG   A 1 241 ? -4.02800  -9.28800  15.90800  1.000 26.46367 ?  221 ARG   A CB    1 
ATOM   1691 N  N     . ASP   A 1 242 ? -5.11800  -6.52700  14.44800  1.000 20.69201 ?  222 ASP   A N     1 
ATOM   1692 C  CA    . ASP   A 1 242 ? -5.77900  -6.06700  13.23400  1.000 20.78060 ?  222 ASP   A CA    1 
ATOM   1693 C  C     . ASP   A 1 242 ? -5.37300  -6.93300  12.03700  1.000 20.31743 ?  222 ASP   A C     1 
ATOM   1694 O  O     . ASP   A 1 242 ? -4.18700  -7.21900  11.84800  1.000 20.17654 ?  222 ASP   A O     1 
ATOM   1695 C  CB    . ASP   A 1 242 ? -5.39600  -4.61000  12.96100  1.000 23.22982 ?  222 ASP   A CB    1 
ATOM   1696 C  CG    . ASP   A 1 242 ? -6.13200  -3.62100  13.86100  1.000 27.63768 ?  222 ASP   A CG    1 
ATOM   1697 O  OD1   . ASP   A 1 242 ? -7.10200  -4.00400  14.54400  1.000 25.02016 ?  222 ASP   A OD1   1 
ATOM   1698 O  OD2   . ASP   A 1 242 ? -5.71300  -2.44300  13.91300  1.000 39.58732 -1 222 ASP   A OD2   1 
ATOM   1699 N  N     . ILE   A 1 243 ? -6.35700  -7.33700  11.22900  1.000 17.69504 ?  223 ILE   A N     1 
ATOM   1700 C  CA    . ILE   A 1 243 ? -6.12400  -8.09600  10.00200  1.000 15.67511 ?  223 ILE   A CA    1 
ATOM   1701 C  C     . ILE   A 1 243 ? -6.88600  -7.38800  8.88300   1.000 21.61690 ?  223 ILE   A C     1 
ATOM   1702 O  O     . ILE   A 1 243 ? -8.11700  -7.33300  8.91400   1.000 19.49644 ?  223 ILE   A O     1 
ATOM   1703 C  CB    . ILE   A 1 243 ? -6.58900  -9.55800  10.11200  1.000 20.00896 ?  223 ILE   A CB    1 
ATOM   1704 C  CG1   . ILE   A 1 243 ? -6.00800  -10.23700 11.36500  1.000 18.77208 ?  223 ILE   A CG1   1 
ATOM   1705 C  CG2   . ILE   A 1 243 ? -6.20700  -10.35100 8.82400   1.000 19.58636 ?  223 ILE   A CG2   1 
ATOM   1706 C  CD1   . ILE   A 1 243 ? -6.35600  -11.73100 11.48800  1.000 21.30618 ?  223 ILE   A CD1   1 
ATOM   1707 N  N     . PRO   A 1 244 ? -6.21400  -6.83700  7.87900   1.000 19.35937 ?  224 PRO   A N     1 
ATOM   1708 C  CA    . PRO   A 1 244 ? -6.91300  -6.11400  6.79700   1.000 17.99188 ?  224 PRO   A CA    1 
ATOM   1709 C  C     . PRO   A 1 244 ? -7.41000  -7.04900  5.69700   1.000 20.19819 ?  224 PRO   A C     1 
ATOM   1710 O  O     . PRO   A 1 244 ? -6.97700  -8.19700  5.58000   1.000 20.31643 ?  224 PRO   A O     1 
ATOM   1711 C  CB    . PRO   A 1 244 ? -5.83100  -5.17600  6.24800   1.000 20.54952 ?  224 PRO   A CB    1 
ATOM   1712 C  CG    . PRO   A 1 244 ? -4.56900  -5.98800  6.40300   1.000 22.97621 ?  224 PRO   A CG    1 
ATOM   1713 C  CD    . PRO   A 1 244 ? -4.75000  -6.78800  7.73000   1.000 21.28755 ?  224 PRO   A CD    1 
ATOM   1714 N  N     . PHE   A 1 245 ? -8.34100  -6.53400  4.88000   1.000 19.72501 ?  225 PHE   A N     1 
ATOM   1715 C  CA    . PHE   A 1 245 ? -8.86400  -7.31500  3.75800   1.000 16.81692 ?  225 PHE   A CA    1 
ATOM   1716 C  C     . PHE   A 1 245 ? -9.40100  -6.39200  2.66200   1.000 20.51159 ?  225 PHE   A C     1 
ATOM   1717 O  O     . PHE   A 1 245 ? -9.78300  -5.24900  2.93200   1.000 17.57005 ?  225 PHE   A O     1 
ATOM   1718 C  CB    . PHE   A 1 245 ? -9.94000  -8.31500  4.23500   1.000 16.26227 ?  225 PHE   A CB    1 
ATOM   1719 C  CG    . PHE   A 1 245 ? -11.23900 -7.69100  4.73400   1.000 17.19208 ?  225 PHE   A CG    1 
ATOM   1720 C  CD1   . PHE   A 1 245 ? -12.26500 -7.39400  3.85600   1.000 17.49890 ?  225 PHE   A CD1   1 
ATOM   1721 C  CD2   . PHE   A 1 245 ? -11.44500 -7.49200  6.10800   1.000 18.57543 ?  225 PHE   A CD2   1 
ATOM   1722 C  CE1   . PHE   A 1 245 ? -13.47200 -6.84600  4.29700   1.000 15.29371 ?  225 PHE   A CE1   1 
ATOM   1723 C  CE2   . PHE   A 1 245 ? -12.64200 -6.97000  6.58700   1.000 20.02709 ?  225 PHE   A CE2   1 
ATOM   1724 C  CZ    . PHE   A 1 245 ? -13.66500 -6.64100  5.67900   1.000 18.42886 ?  225 PHE   A CZ    1 
ATOM   1725 N  N     . VAL   A 1 246 ? -9.41500  -6.89600  1.41900   1.000 17.72181 ?  226 VAL   A N     1 
ATOM   1726 C  CA    . VAL   A 1 246 ? -9.88900  -6.14400  0.25100   1.000 17.22685 ?  226 VAL   A CA    1 
ATOM   1727 C  C     . VAL   A 1 246 ? -10.92800 -6.98300  -0.48600  1.000 17.67236 ?  226 VAL   A C     1 
ATOM   1728 O  O     . VAL   A 1 246 ? -10.63300 -8.11300  -0.91300  1.000 17.13722 ?  226 VAL   A O     1 
ATOM   1729 C  CB    . VAL   A 1 246 ? -8.73300  -5.77300  -0.69600  1.000 17.18932 ?  226 VAL   A CB    1 
ATOM   1730 C  CG1   . VAL   A 1 246 ? -9.23500  -5.07500  -2.04400  1.000 15.74333 ?  226 VAL   A CG1   1 
ATOM   1731 C  CG2   . VAL   A 1 246 ? -7.71300  -4.89300  0.02800   1.000 17.39830 ?  226 VAL   A CG2   1 
ATOM   1732 N  N     . ILE   A 1 247 ? -12.12800 -6.42100  -0.68300  1.000 16.74723 ?  227 ILE   A N     1 
ATOM   1733 C  CA    . ILE   A 1 247 ? -13.17800 -7.06300  -1.49000  1.000 17.32166 ?  227 ILE   A CA    1 
ATOM   1734 C  C     . ILE   A 1 247 ? -13.33700 -6.30000  -2.80300  1.000 18.70763 ?  227 ILE   A C     1 
ATOM   1735 O  O     . ILE   A 1 247 ? -13.59700 -5.08900  -2.79200  1.000 18.12846 ?  227 ILE   A O     1 
ATOM   1736 C  CB    . ILE   A 1 247 ? -14.51800 -7.12700  -0.74200  1.000 18.34076 ?  227 ILE   A CB    1 
ATOM   1737 C  CG1   . ILE   A 1 247 ? -14.35400 -7.95700  0.54400   1.000 18.35830 ?  227 ILE   A CG1   1 
ATOM   1738 C  CG2   . ILE   A 1 247 ? -15.61900 -7.70200  -1.67900  1.000 17.05684 ?  227 ILE   A CG2   1 
ATOM   1739 C  CD1   . ILE   A 1 247 ? -15.62100 -8.09400  1.41900   1.000 20.57686 ?  227 ILE   A CD1   1 
ATOM   1740 N  N     . ARG   A 1 248 ? -13.19400 -7.02000  -3.92600  1.000 16.04849 ?  228 ARG   A N     1 
ATOM   1741 C  CA    . ARG   A 1 248 ? -13.35000 -6.44600  -5.26600  1.000 15.25635 ?  228 ARG   A CA    1 
ATOM   1742 C  C     . ARG   A 1 248 ? -14.83100 -6.39500  -5.64100  1.000 17.90216 ?  228 ARG   A C     1 
ATOM   1743 O  O     . ARG   A 1 248 ? -15.53000 -7.41200  -5.59300  1.000 18.05059 ?  228 ARG   A O     1 
ATOM   1744 C  CB    . ARG   A 1 248 ? -12.56200 -7.28300  -6.29300  1.000 17.09004 ?  228 ARG   A CB    1 
ATOM   1745 C  CG    . ARG   A 1 248 ? -12.69900 -6.83600  -7.78000  1.000 15.79841 ?  228 ARG   A CG    1 
ATOM   1746 C  CD    . ARG   A 1 248 ? -12.34900 -8.01200  -8.75700  1.000 17.09181 ?  228 ARG   A CD    1 
ATOM   1747 N  NE    . ARG   A 1 248 ? -12.34200 -7.59000  -10.16900 1.000 17.73149 ?  228 ARG   A NE    1 
ATOM   1748 C  CZ    . ARG   A 1 248 ? -13.44500 -7.36900  -10.87700 1.000 17.80321 ?  228 ARG   A CZ    1 
ATOM   1749 N  NH1   . ARG   A 1 248 ? -14.64600 -7.53800  -10.34900 1.000 16.93262 ?  228 ARG   A NH1   1 
ATOM   1750 N  NH2   . ARG   A 1 248 ? -13.34000 -6.97200  -12.16000 1.000 16.79876 ?  228 ARG   A NH2   1 
ATOM   1751 N  N     . GLU   A 1 249 ? -15.31200 -5.22200  -6.04800  1.000 15.86918 ?  229 GLU   A N     1 
ATOM   1752 C  CA    . GLU   A 1 249 ? -16.68200 -5.10800  -6.56300  1.000 16.57923 ?  229 GLU   A CA    1 
ATOM   1753 C  C     . GLU   A 1 249 ? -16.75600 -4.95100  -8.08500  1.000 16.67128 ?  229 GLU   A C     1 
ATOM   1754 O  O     . GLU   A 1 249 ? -17.65800 -5.50900  -8.73500  1.000 19.15919 ?  229 GLU   A O     1 
ATOM   1755 C  CB    . GLU   A 1 249 ? -17.39300 -3.93000  -5.89400  1.000 18.39423 ?  229 GLU   A CB    1 
ATOM   1756 C  CG    . GLU   A 1 249 ? -17.46300 -4.05700  -4.37300  1.000 18.64129 ?  229 GLU   A CG    1 
ATOM   1757 C  CD    . GLU   A 1 249 ? -18.34200 -2.99100  -3.71400  1.000 27.57424 ?  229 GLU   A CD    1 
ATOM   1758 O  OE1   . GLU   A 1 249 ? -18.79500 -2.03000  -4.40900  1.000 23.58409 ?  229 GLU   A OE1   1 
ATOM   1759 O  OE2   . GLU   A 1 249 ? -18.55400 -3.09200  -2.48100  1.000 24.09055 -1 229 GLU   A OE2   1 
ATOM   1760 N  N     . THR   A 1 250 ? -15.87400 -4.15400  -8.66300  1.000 15.94039 ?  230 THR   A N     1 
ATOM   1761 C  CA    . THR   A 1 250 ? -15.77300 -3.98000  -10.11500 1.000 16.70733 ?  230 THR   A CA    1 
ATOM   1762 C  C     . THR   A 1 250 ? -14.29500 -3.93900  -10.45200 1.000 17.93533 ?  230 THR   A C     1 
ATOM   1763 O  O     . THR   A 1 250 ? -13.45300 -4.04600  -9.56500  1.000 17.33179 ?  230 THR   A O     1 
ATOM   1764 C  CB    . THR   A 1 250 ? -16.46200 -2.69200  -10.60500 1.000 16.60539 ?  230 THR   A CB    1 
ATOM   1765 O  OG1   . THR   A 1 250 ? -15.68400 -1.55300  -10.19100 1.000 16.72439 ?  230 THR   A OG1   1 
ATOM   1766 C  CG2   . THR   A 1 250 ? -17.88300 -2.56300  -10.05600 1.000 19.47013 ?  230 THR   A CG2   1 
ATOM   1767 N  N     . THR   A 1 251 ? -13.95700 -3.75100  -11.74000 1.000 16.77002 ?  231 THR   A N     1 
ATOM   1768 C  CA    . THR   A 1 251 ? -12.54900 -3.55100  -12.05400 1.000 17.78871 ?  231 THR   A CA    1 
ATOM   1769 C  C     . THR   A 1 251 ? -11.94100 -2.41800  -11.22000 1.000 20.36202 ?  231 THR   A C     1 
ATOM   1770 O  O     . THR   A 1 251 ? -10.76700 -2.48700  -10.82200 1.000 18.99023 ?  231 THR   A O     1 
ATOM   1771 C  CB    . THR   A 1 251 ? -12.38000 -3.25700  -13.54300 1.000 20.04301 ?  231 THR   A CB    1 
ATOM   1772 O  OG1   . THR   A 1 251 ? -12.65700 -4.44200  -14.30500 1.000 20.85028 ?  231 THR   A OG1   1 
ATOM   1773 C  CG2   . THR   A 1 251 ? -10.96300 -2.78700  -13.83200 1.000 21.91042 ?  231 THR   A CG2   1 
ATOM   1774 N  N     . ARG   A 1 252 ? -12.72200 -1.37900  -10.92600 1.000 16.72096 ?  232 ARG   A N     1 
ATOM   1775 C  CA    . ARG   A 1 252 ? -12.19300 -0.17600  -10.28700 1.000 15.74286 ?  232 ARG   A CA    1 
ATOM   1776 C  C     . ARG   A 1 252 ? -12.57900 0.00900   -8.81500  1.000 14.49083 ?  232 ARG   A C     1 
ATOM   1777 O  O     . ARG   A 1 252 ? -11.82700 0.66200   -8.07600  1.000 17.45751 ?  232 ARG   A O     1 
ATOM   1778 C  CB    . ARG   A 1 252 ? -12.63300 1.06400   -11.09200 1.000 17.00354 ?  232 ARG   A CB    1 
ATOM   1779 C  CG    . ARG   A 1 252 ? -12.07200 1.05500   -12.52700 1.000 17.83097 ?  232 ARG   A CG    1 
ATOM   1780 C  CD    . ARG   A 1 252 ? -12.44600 2.29000   -13.37200 1.000 16.84917 ?  232 ARG   A CD    1 
ATOM   1781 N  NE    . ARG   A 1 252 ? -11.65700 2.31300   -14.61000 1.000 18.29323 ?  232 ARG   A NE    1 
ATOM   1782 C  CZ    . ARG   A 1 252 ? -10.39100 2.70600   -14.67800 1.000 18.50690 ?  232 ARG   A CZ    1 
ATOM   1783 N  NH1   . ARG   A 1 252 ? -9.76800  3.22100   -13.63000 1.000 18.48271 ?  232 ARG   A NH1   1 
ATOM   1784 N  NH2   . ARG   A 1 252 ? -9.74400  2.62200   -15.84300 1.000 23.12294 ?  232 ARG   A NH2   1 
ATOM   1785 N  N     . LYS   A 1 253 ? -13.68100 -0.57900  -8.34300  1.000 16.73899 ?  233 LYS   A N     1 
ATOM   1786 C  CA    . LYS   A 1 253 ? -14.20100 -0.30300  -6.99400  1.000 17.07138 ?  233 LYS   A CA    1 
ATOM   1787 C  C     . LYS   A 1 253 ? -13.95800 -1.48000  -6.04300  1.000 17.51339 ?  233 LYS   A C     1 
ATOM   1788 O  O     . LYS   A 1 253 ? -14.30700 -2.62300  -6.36900  1.000 16.24658 ?  233 LYS   A O     1 
ATOM   1789 C  CB    . LYS   A 1 253 ? -15.70200 0.00600   -7.06000  1.000 15.76413 ?  233 LYS   A CB    1 
ATOM   1790 C  CG    . LYS   A 1 253 ? -16.32900 0.43300   -5.71400  1.000 17.66733 ?  233 LYS   A CG    1 
ATOM   1791 C  CD    . LYS   A 1 253 ? -17.80800 0.74400   -5.88000  1.000 23.00622 ?  233 LYS   A CD    1 
ATOM   1792 C  CE    . LYS   A 1 253 ? -18.33800 1.51100   -4.66800  1.000 21.47962 ?  233 LYS   A CE    1 
ATOM   1793 N  NZ    . LYS   A 1 253 ? -18.49000 0.61200   -3.46500  1.000 22.62741 ?  233 LYS   A NZ    1 
ATOM   1794 N  N     . TYR   A 1 254 ? -13.39500 -1.18900  -4.84900  1.000 18.16892 ?  234 TYR   A N     1 
ATOM   1795 C  CA    . TYR   A 1 254 ? -13.04700 -2.18300  -3.82700  1.000 16.43413 ?  234 TYR   A CA    1 
ATOM   1796 C  C     . TYR   A 1 254 ? -13.44900 -1.70300  -2.42900  1.000 16.47828 ?  234 TYR   A C     1 
ATOM   1797 O  O     . TYR   A 1 254 ? -13.56200 -0.49700  -2.16900  1.000 17.62242 ?  234 TYR   A O     1 
ATOM   1798 C  CB    . TYR   A 1 254 ? -11.51900 -2.46900  -3.79700  1.000 15.71490 ?  234 TYR   A CB    1 
ATOM   1799 C  CG    . TYR   A 1 254 ? -10.97900 -2.87900  -5.16300  1.000 16.69746 ?  234 TYR   A CG    1 
ATOM   1800 C  CD1   . TYR   A 1 254 ? -10.73800 -1.92600  -6.16400  1.000 17.61377 ?  234 TYR   A CD1   1 
ATOM   1801 C  CD2   . TYR   A 1 254 ? -10.73000 -4.20200  -5.44500  1.000 19.80859 ?  234 TYR   A CD2   1 
ATOM   1802 C  CE1   . TYR   A 1 254 ? -10.26700 -2.31400  -7.43300  1.000 18.33777 ?  234 TYR   A CE1   1 
ATOM   1803 C  CE2   . TYR   A 1 254 ? -10.25100 -4.59900  -6.69300  1.000 19.86597 ?  234 TYR   A CE2   1 
ATOM   1804 C  CZ    . TYR   A 1 254 ? -10.03900 -3.66600  -7.68500  1.000 18.81660 ?  234 TYR   A CZ    1 
ATOM   1805 O  OH    . TYR   A 1 254 ? -9.58500  -4.12500  -8.91500  1.000 18.79728 ?  234 TYR   A OH    1 
ATOM   1806 N  N     . GLN   A 1 255 ? -13.67400 -2.66300  -1.52800  1.000 17.49090 ?  235 GLN   A N     1 
ATOM   1807 C  CA    . GLN   A 1 255 ? -13.70600 -2.40600  -0.09500  1.000 17.10741 ?  235 GLN   A CA    1 
ATOM   1808 C  C     . GLN   A 1 255 ? -12.32300 -2.70400  0.45400   1.000 14.69678 ?  235 GLN   A C     1 
ATOM   1809 O  O     . GLN   A 1 255 ? -11.69500 -3.68700  0.05100   1.000 17.54954 ?  235 GLN   A O     1 
ATOM   1810 C  CB    . GLN   A 1 255 ? -14.71200 -3.32700  0.60900   1.000 18.13737 ?  235 GLN   A CB    1 
ATOM   1811 C  CG    . GLN   A 1 255 ? -16.10400 -3.23300  0.03800   1.000 20.26407 ?  235 GLN   A CG    1 
ATOM   1812 C  CD    . GLN   A 1 255 ? -17.01700 -4.27700  0.61500   1.000 20.67211 ?  235 GLN   A CD    1 
ATOM   1813 O  OE1   . GLN   A 1 255 ? -16.84400 -4.70900  1.76700   1.000 18.92208 ?  235 GLN   A OE1   1 
ATOM   1814 N  NE2   . GLN   A 1 255 ? -18.01900 -4.66800  -0.16100  1.000 21.56383 ?  235 GLN   A NE2   1 
ATOM   1815 N  N     . HIS   A 1 256 ? -11.84900 -1.86200  1.37000   1.000 14.75699 ?  236 HIS   A N     1 
ATOM   1816 C  CA    . HIS   A 1 256 ? -10.54300 -2.06600  2.00500   1.000 16.86338 ?  236 HIS   A CA    1 
ATOM   1817 C  C     . HIS   A 1 256 ? -10.70200 -1.75600  3.49300   1.000 18.55788 ?  236 HIS   A C     1 
ATOM   1818 O  O     . HIS   A 1 256 ? -10.86800 -0.59200  3.87800   1.000 17.54056 ?  236 HIS   A O     1 
ATOM   1819 C  CB    . HIS   A 1 256 ? -9.48000  -1.19200  1.33000   1.000 20.18063 ?  236 HIS   A CB    1 
ATOM   1820 C  CG    . HIS   A 1 256 ? -8.07200  -1.50300  1.73600   1.000 18.79109 ?  236 HIS   A CG    1 
ATOM   1821 N  ND1   . HIS   A 1 256 ? -6.98100  -0.91000  1.12800   1.000 19.51145 ?  236 HIS   A ND1   1 
ATOM   1822 C  CD2   . HIS   A 1 256 ? -7.57200  -2.30700  2.70900   1.000 18.15287 ?  236 HIS   A CD2   1 
ATOM   1823 C  CE1   . HIS   A 1 256 ? -5.87200  -1.33300  1.71400   1.000 23.14895 ?  236 HIS   A CE1   1 
ATOM   1824 N  NE2   . HIS   A 1 256 ? -6.20100  -2.19600  2.66500   1.000 19.22017 ?  236 HIS   A NE2   1 
ATOM   1825 N  N     . THR   A 1 257 ? -10.67600 -2.79800  4.32500   1.000 15.44254 ?  237 THR   A N     1 
ATOM   1826 C  CA    . THR   A 1 257 ? -11.20800 -2.71900  5.68600   1.000 15.53543 ?  237 THR   A CA    1 
ATOM   1827 C  C     . THR   A 1 257 ? -10.29500 -3.46400  6.65600   1.000 18.00281 ?  237 THR   A C     1 
ATOM   1828 O  O     . THR   A 1 257 ? -9.59600  -4.40900  6.28500   1.000 18.36856 ?  237 THR   A O     1 
ATOM   1829 C  CB    . THR   A 1 257 ? -12.65200 -3.28400  5.68600   1.000 19.62158 ?  237 THR   A CB    1 
ATOM   1830 O  OG1   . THR   A 1 257 ? -13.47600 -2.45300  4.84500   1.000 19.48225 ?  237 THR   A OG1   1 
ATOM   1831 C  CG2   . THR   A 1 257 ? -13.28200 -3.43400  7.12700   1.000 19.03623 ?  237 THR   A CG2   1 
ATOM   1832 N  N     . VAL   A 1 258 ? -10.30700 -3.03500  7.91700   1.000 17.93809 ?  238 VAL   A N     1 
ATOM   1833 C  CA    . VAL   A 1 258 ? -9.40000  -3.57500  8.93100   1.000 18.77696 ?  238 VAL   A CA    1 
ATOM   1834 C  C     . VAL   A 1 258 ? -10.21900 -4.26300  10.00600  1.000 19.34168 ?  238 VAL   A C     1 
ATOM   1835 O  O     . VAL   A 1 258 ? -10.80800 -3.59400  10.86100  1.000 18.81063 ?  238 VAL   A O     1 
ATOM   1836 C  CB    . VAL   A 1 258 ? -8.52300  -2.49200  9.56100   1.000 17.06646 ?  238 VAL   A CB    1 
ATOM   1837 C  CG1   . VAL   A 1 258 ? -7.51800  -3.14000  10.52500  1.000 22.00821 ?  238 VAL   A CG1   1 
ATOM   1838 C  CG2   . VAL   A 1 258 ? -7.78400  -1.65800  8.49600   1.000 17.79594 ?  238 VAL   A CG2   1 
ATOM   1839 N  N     . ALA   A 1 259 ? -10.18600 -5.59500  10.03400  1.000 17.63326 ?  239 ALA   A N     1 
ATOM   1840 C  CA    . ALA   A 1 259 ? -10.93000 -6.33500  11.04800  1.000 19.17506 ?  239 ALA   A CA    1 
ATOM   1841 C  C     . ALA   A 1 259 ? -10.12900 -6.44300  12.34600  1.000 18.43409 ?  239 ALA   A C     1 
ATOM   1842 O  O     . ALA   A 1 259 ? -8.89900  -6.44700  12.33100  1.000 17.25422 ?  239 ALA   A O     1 
ATOM   1843 C  CB    . ALA   A 1 259 ? -11.25700 -7.73800  10.51900  1.000 16.45717 ?  239 ALA   A CB    1 
ATOM   1844 N  N     . GLU   A 1 260 ? -10.82700 -6.56400  13.47200  1.000 16.63295 ?  240 GLU   A N     1 
ATOM   1845 C  CA    . GLU   A 1 260 ? -10.16300 -6.89500  14.73500  1.000 16.79261 ?  240 GLU   A CA    1 
ATOM   1846 C  C     . GLU   A 1 260 ? -10.32200 -8.38600  14.98300  1.000 19.01235 ?  240 GLU   A C     1 
ATOM   1847 O  O     . GLU   A 1 260 ? -11.44500 -8.90100  14.94500  1.000 17.67713 ?  240 GLU   A O     1 
ATOM   1848 C  CB    . GLU   A 1 260 ? -10.72500 -6.10000  15.91800  1.000 17.43659 ?  240 GLU   A CB    1 
ATOM   1849 C  CG    . GLU   A 1 260 ? -10.09300 -6.54500  17.26000  1.000 16.45165 ?  240 GLU   A CG    1 
ATOM   1850 C  CD    . GLU   A 1 260 ? -10.36500 -5.58300  18.39100  1.000 24.83887 ?  240 GLU   A CD    1 
ATOM   1851 O  OE1   . GLU   A 1 260 ? -11.54700 -5.44200  18.77300  1.000 19.53348 ?  240 GLU   A OE1   1 
ATOM   1852 O  OE2   . GLU   A 1 260 ? -9.39200  -4.98600  18.90800  1.000 23.23813 -1 240 GLU   A OE2   1 
ATOM   1853 N  N     . ALA   A 1 261 ? -9.19900  -9.07400  15.20000  1.000 17.09513 ?  241 ALA   A N     1 
ATOM   1854 C  CA    . ALA   A 1 261 ? -9.17900  -10.49500 15.52600  1.000 17.99879 ?  241 ALA   A CA    1 
ATOM   1855 C  C     . ALA   A 1 261 ? -8.96700  -10.67500 17.03100  1.000 17.44413 ?  241 ALA   A C     1 
ATOM   1856 O  O     . ALA   A 1 261 ? -8.01100  -10.13100 17.60600  1.000 19.00129 ?  241 ALA   A O     1 
ATOM   1857 C  CB    . ALA   A 1 261 ? -8.06500  -11.19900 14.74700  1.000 15.30199 ?  241 ALA   A CB    1 
ATOM   1858 N  N     . SER   A 1 262 ? -9.83800  -11.45500 17.66800  1.000 18.20961 ?  242 SER   A N     1 
ATOM   1859 C  CA    . SER   A 1 262 ? -9.70800  -11.74200 19.08600  1.000 15.34675 ?  242 SER   A CA    1 
ATOM   1860 C  C     . SER   A 1 262 ? -9.66700  -13.25600 19.26600  1.000 19.32446 ?  242 SER   A C     1 
ATOM   1861 O  O     . SER   A 1 262 ? -10.48200 -13.99000 18.68500  1.000 16.96837 ?  242 SER   A O     1 
ATOM   1862 C  CB    . SER   A 1 262 ? -10.84900 -11.10900 19.91200  1.000 18.96615 ?  242 SER   A CB    1 
ATOM   1863 O  OG    . SER   A 1 262 ? -12.12900 -11.46100 19.40300  1.000 18.07169 ?  242 SER   A OG    1 
ATOM   1864 N  N     . LEU   A 1 263 ? -8.69100  -13.71200 20.03800  1.000 18.20724 ?  243 LEU   A N     1 
ATOM   1865 C  CA    . LEU   A 1 263 ? -8.42400  -15.12300 20.24800  1.000 17.76141 ?  243 LEU   A CA    1 
ATOM   1866 C  C     . LEU   A 1 263 ? -8.70800  -15.45300 21.70800  1.000 18.13265 ?  243 LEU   A C     1 
ATOM   1867 O  O     . LEU   A 1 263 ? -8.24300  -14.74600 22.60500  1.000 19.43685 ?  243 LEU   A O     1 
ATOM   1868 C  CB    . LEU   A 1 263 ? -6.97200  -15.44600 19.90500  1.000 17.65608 ?  243 LEU   A CB    1 
ATOM   1869 C  CG    . LEU   A 1 263 ? -6.61700  -15.37300 18.41900  1.000 25.05211 ?  243 LEU   A CG    1 
ATOM   1870 C  CD1   . LEU   A 1 263 ? -5.09900  -15.47800 18.24800  1.000 29.80821 ?  243 LEU   A CD1   1 
ATOM   1871 C  CD2   . LEU   A 1 263 ? -7.30800  -16.44400 17.69300  1.000 27.43683 ?  243 LEU   A CD2   1 
ATOM   1872 N  N     . TRP   A 1 264 ? -9.44200  -16.54500 21.94300  1.000 19.48704 ?  244 TRP   A N     1 
ATOM   1873 C  CA    . TRP   A 1 264 ? -10.02200 -16.83500 23.25800  1.000 17.06705 ?  244 TRP   A CA    1 
ATOM   1874 C  C     . TRP   A 1 264 ? -9.75900  -18.29400 23.60000  1.000 19.73694 ?  244 TRP   A C     1 
ATOM   1875 O  O     . TRP   A 1 264 ? -10.18400 -19.17800 22.85700  1.000 19.69786 ?  244 TRP   A O     1 
ATOM   1876 C  CB    . TRP   A 1 264 ? -11.53600 -16.60100 23.24300  1.000 18.43617 ?  244 TRP   A CB    1 
ATOM   1877 C  CG    . TRP   A 1 264 ? -11.95900 -15.26800 22.70400  1.000 18.49411 ?  244 TRP   A CG    1 
ATOM   1878 C  CD1   . TRP   A 1 264 ? -12.05400 -14.90100 21.38400  1.000 19.03524 ?  244 TRP   A CD1   1 
ATOM   1879 C  CD2   . TRP   A 1 264 ? -12.35600 -14.13400 23.47500  1.000 18.18703 ?  244 TRP   A CD2   1 
ATOM   1880 N  NE1   . TRP   A 1 264 ? -12.49300 -13.60400 21.29000  1.000 17.70750 ?  244 TRP   A NE1   1 
ATOM   1881 C  CE2   . TRP   A 1 264 ? -12.68000 -13.10300 22.56400  1.000 20.24233 ?  244 TRP   A CE2   1 
ATOM   1882 C  CE3   . TRP   A 1 264 ? -12.48000 -13.88900 24.86400  1.000 17.74831 ?  244 TRP   A CE3   1 
ATOM   1883 C  CZ2   . TRP   A 1 264 ? -13.12200 -11.84900 22.99300  1.000 19.78887 ?  244 TRP   A CZ2   1 
ATOM   1884 C  CZ3   . TRP   A 1 264 ? -12.91000 -12.64200 25.28900  1.000 20.85695 ?  244 TRP   A CZ3   1 
ATOM   1885 C  CH2   . TRP   A 1 264 ? -13.22700 -11.63600 24.35700  1.000 17.55962 ?  244 TRP   A CH2   1 
ATOM   1886 N  N     . ARG   A 1 265 ? -9.10500  -18.55400 24.73400  1.000 20.06392 ?  245 ARG   A N     1 
ATOM   1887 C  CA    . ARG   A 1 265 ? -8.85900  -19.93200 25.17300  1.000 20.28237 ?  245 ARG   A CA    1 
ATOM   1888 C  C     . ARG   A 1 265 ? -9.99500  -20.40000 26.07600  1.000 18.64896 ?  245 ARG   A C     1 
ATOM   1889 O  O     . ARG   A 1 265 ? -10.36100 -19.69900 27.01500  1.000 20.18129 ?  245 ARG   A O     1 
ATOM   1890 C  CB    . ARG   A 1 265 ? -7.52100  -20.03900 25.93200  1.000 20.75606 ?  245 ARG   A CB    1 
ATOM   1891 C  CG    . ARG   A 1 265 ? -7.06800  -21.48100 26.19100  1.000 22.02681 ?  245 ARG   A CG    1 
ATOM   1892 C  CD    . ARG   A 1 265 ? -6.23700  -22.03800 25.02600  1.000 24.58896 ?  245 ARG   A CD    1 
ATOM   1893 N  NE    . ARG   A 1 265 ? -5.00300  -21.26900 24.90200  1.000 25.54503 ?  245 ARG   A NE    1 
ATOM   1894 C  CZ    . ARG   A 1 265 ? -4.29100  -21.12900 23.79200  1.000 25.23732 ?  245 ARG   A CZ    1 
ATOM   1895 N  NH1   . ARG   A 1 265 ? -4.67100  -21.67400 22.64700  1.000 23.72649 ?  245 ARG   A NH1   1 
ATOM   1896 N  NH2   . ARG   A 1 265 ? -3.16800  -20.41800 23.83400  1.000 25.30116 ?  245 ARG   A NH2   1 
ATOM   1897 N  N     . ARG   A 1 266 ? -10.51300 -21.60400 25.82400  1.000 19.26601 ?  246 ARG   A N     1 
ATOM   1898 C  CA    . ARG   A 1 266 ? -11.54700 -22.16300 26.69100  1.000 19.80783 ?  246 ARG   A CA    1 
ATOM   1899 C  C     . ARG   A 1 266 ? -10.93500 -22.65400 28.00900  1.000 20.37532 ?  246 ARG   A C     1 
ATOM   1900 O  O     . ARG   A 1 266 ? -10.01100 -23.47000 28.00300  1.000 20.11645 ?  246 ARG   A O     1 
ATOM   1901 C  CB    . ARG   A 1 266 ? -12.25700 -23.31400 25.97500  1.000 20.55854 ?  246 ARG   A CB    1 
ATOM   1902 C  CG    . ARG   A 1 266 ? -13.43500 -23.92300 26.75600  1.000 19.67964 ?  246 ARG   A CG    1 
ATOM   1903 C  CD    . ARG   A 1 266 ? -14.65000 -22.97600 26.88100  1.000 19.06252 ?  246 ARG   A CD    1 
ATOM   1904 N  NE    . ARG   A 1 266 ? -15.83000 -23.66900 27.43000  1.000 19.72791 ?  246 ARG   A NE    1 
ATOM   1905 C  CZ    . ARG   A 1 266 ? -16.13000 -23.75600 28.72900  1.000 24.96294 ?  246 ARG   A CZ    1 
ATOM   1906 N  NH1   . ARG   A 1 266 ? -15.39200 -23.17000 29.66300  1.000 20.07381 ?  246 ARG   A NH1   1 
ATOM   1907 N  NH2   . ARG   A 1 266 ? -17.20200 -24.44800 29.10500  1.000 24.93814 ?  246 ARG   A NH2   1 
ATOM   1908 N  N     . ALA   A 1 267 ? -11.45900 -22.15800 29.12700  1.000 18.97592 ?  247 ALA   A N     1 
ATOM   1909 C  CA    . ALA   A 1 267 ? -10.98900 -22.54400 30.49100  1.000 22.32418 ?  247 ALA   A CA    1 
ATOM   1910 C  C     . ALA   A 1 267 ? -11.63400 -23.84300 30.98300  1.000 27.98975 ?  247 ALA   A C     1 
ATOM   1911 O  O     . ALA   A 1 267 ? -12.54000 -24.36300 30.32000  1.000 23.85281 ?  247 ALA   A O     1 
ATOM   1912 C  CB    . ALA   A 1 267 ? -11.27300 -21.42400 31.48300  1.000 21.88367 ?  247 ALA   A CB    1 
HETATM 1913 N  N     . SAH   B 2 .   ? -16.41900 -15.71000 6.84600   1.000 16.64751 ?  301 SAH   A N     1 
HETATM 1914 C  CA    . SAH   B 2 .   ? -16.50100 -15.08200 5.50100   1.000 18.45913 ?  301 SAH   A CA    1 
HETATM 1915 C  CB    . SAH   B 2 .   ? -17.84500 -14.38700 5.29400   1.000 18.53304 ?  301 SAH   A CB    1 
HETATM 1916 C  CG    . SAH   B 2 .   ? -18.08100 -13.16200 6.14800   1.000 15.93282 ?  301 SAH   A CG    1 
HETATM 1917 S  SD    . SAH   B 2 .   ? -19.48900 -12.16800 5.57600   1.000 18.13255 ?  301 SAH   A SD    1 
HETATM 1918 C  C     . SAH   B 2 .   ? -15.35100 -14.08500 5.32500   1.000 21.64965 ?  301 SAH   A C     1 
HETATM 1919 O  O     . SAH   B 2 .   ? -15.11700 -13.68100 4.19300   1.000 18.01048 ?  301 SAH   A O     1 
HETATM 1920 O  OXT   . SAH   B 2 .   ? -14.73100 -13.79900 6.32900   1.000 19.65435 ?  301 SAH   A OXT   1 
HETATM 1921 C  "C5'" . SAH   B 2 .   ? -20.83600 -12.74000 6.64500   1.000 20.72988 ?  301 SAH   A "C5'" 1 
HETATM 1922 C  "C4'" . SAH   B 2 .   ? -21.23900 -14.17500 6.40200   1.000 15.76899 ?  301 SAH   A "C4'" 1 
HETATM 1923 O  "O4'" . SAH   B 2 .   ? -22.14300 -14.59700 7.44600   1.000 17.06523 ?  301 SAH   A "O4'" 1 
HETATM 1924 C  "C3'" . SAH   B 2 .   ? -21.96900 -14.43700 5.08100   1.000 16.96377 ?  301 SAH   A "C3'" 1 
HETATM 1925 O  "O3'" . SAH   B 2 .   ? -21.41400 -15.56700 4.42400   1.000 17.87789 ?  301 SAH   A "O3'" 1 
HETATM 1926 C  "C2'" . SAH   B 2 .   ? -23.41600 -14.69600 5.51600   1.000 19.88112 ?  301 SAH   A "C2'" 1 
HETATM 1927 O  "O2'" . SAH   B 2 .   ? -24.11300 -15.55200 4.64000   1.000 18.88947 ?  301 SAH   A "O2'" 1 
HETATM 1928 C  "C1'" . SAH   B 2 .   ? -23.18400 -15.34600 6.87100   1.000 16.42609 ?  301 SAH   A "C1'" 1 
HETATM 1929 N  N9    . SAH   B 2 .   ? -24.32000 -15.30600 7.78300   1.000 17.98437 ?  301 SAH   A N9    1 
HETATM 1930 C  C8    . SAH   B 2 .   ? -25.12600 -14.23400 8.06200   1.000 23.19713 ?  301 SAH   A C8    1 
HETATM 1931 N  N7    . SAH   B 2 .   ? -26.05100 -14.49700 8.94900   1.000 21.13066 ?  301 SAH   A N7    1 
HETATM 1932 C  C5    . SAH   B 2 .   ? -25.83000 -15.82200 9.29200   1.000 19.33759 ?  301 SAH   A C5    1 
HETATM 1933 C  C6    . SAH   B 2 .   ? -26.47200 -16.68900 10.19700  1.000 20.81781 ?  301 SAH   A C6    1 
HETATM 1934 N  N6    . SAH   B 2 .   ? -27.51500 -16.34100 10.94300  1.000 21.58456 ?  301 SAH   A N6    1 
HETATM 1935 N  N1    . SAH   B 2 .   ? -25.99800 -17.95100 10.29400  1.000 18.86921 ?  301 SAH   A N1    1 
HETATM 1936 C  C2    . SAH   B 2 .   ? -24.95200 -18.30100 9.53800   1.000 18.42315 ?  301 SAH   A C2    1 
HETATM 1937 N  N3    . SAH   B 2 .   ? -24.27600 -17.57700 8.65600   1.000 18.90697 ?  301 SAH   A N3    1 
HETATM 1938 C  C4    . SAH   B 2 .   ? -24.76400 -16.33100 8.57900   1.000 17.12987 ?  301 SAH   A C4    1 
HETATM 1939 N  N     . A1AS0 C 3 .   ? -18.97200 -5.74000  3.37700   1.000 17.33055 ?  302 A1AS0 A N     1 
HETATM 1940 C  CA    . A1AS0 C 3 .   ? -18.78300 -7.21300  3.44600   1.000 19.26490 ?  302 A1AS0 A CA    1 
HETATM 1941 C  C     . A1AS0 C 3 .   ? -20.10000 -7.87700  3.84200   1.000 17.57187 ?  302 A1AS0 A C     1 
HETATM 1942 O  O     . A1AS0 C 3 .   ? -20.16100 -9.12700  3.75500   1.000 19.16285 ?  302 A1AS0 A O     1 
HETATM 1943 C  CB    . A1AS0 C 3 .   ? -17.69800 -7.59700  4.46300   1.000 16.03570 ?  302 A1AS0 A CB    1 
HETATM 1944 C  CG    . A1AS0 C 3 .   ? -18.15200 -7.62700  5.89200   1.000 17.51176 ?  302 A1AS0 A CG    1 
HETATM 1945 N  ND1   . A1AS0 C 3 .   ? -18.54200 -8.76600  6.55400   1.000 17.61882 ?  302 A1AS0 A ND1   1 
HETATM 1946 C  CD2   . A1AS0 C 3 .   ? -18.22500 -6.58700  6.81100   1.000 17.22152 ?  302 A1AS0 A CD2   1 
HETATM 1947 C  CE1   . A1AS0 C 3 .   ? -18.85300 -8.40800  7.81600   1.000 16.36852 ?  302 A1AS0 A CE1   1 
HETATM 1948 N  NE2   . A1AS0 C 3 .   ? -18.65500 -7.07300  7.97000   1.000 19.78114 ?  302 A1AS0 A NE2   1 
HETATM 1949 SE SE2   . A1AS0 C 3 .   ? -17.81600 -4.74700  6.52900   1.000 21.94716 ?  302 A1AS0 A SE2   1 
HETATM 1950 O  OXT   . A1AS0 C 3 .   ? -20.99800 -7.12400  4.26000   1.000 19.04540 -1 302 A1AS0 A OXT   1 
HETATM 1951 C  C1    . EDO   D 4 .   ? -12.41800 -19.11800 -16.91500 1.000 26.93174 ?  303 EDO   A C1    1 
HETATM 1952 O  O1    . EDO   D 4 .   ? -11.23000 -18.97900 -16.13600 1.000 32.75200 ?  303 EDO   A O1    1 
HETATM 1953 C  C2    . EDO   D 4 .   ? -12.06900 -19.23600 -18.38600 1.000 38.70062 ?  303 EDO   A C2    1 
HETATM 1954 O  O2    . EDO   D 4 .   ? -11.13300 -18.22500 -18.75500 1.000 37.72538 ?  303 EDO   A O2    1 
HETATM 1955 O  O     . HOH   E 5 .   ? -14.64400 -20.28400 4.81600   1.000 31.19331 ?  401 HOH   A O     1 
HETATM 1956 O  O     . HOH   E 5 .   ? -8.35500  -28.51300 2.04800   1.000 24.15193 ?  402 HOH   A O     1 
HETATM 1957 O  O     . HOH   E 5 .   ? -19.77900 -1.37800  -1.05600  1.000 26.63539 ?  403 HOH   A O     1 
HETATM 1958 O  O     . HOH   E 5 .   ? -20.14200 11.18800  24.93100  1.000 35.03406 ?  404 HOH   A O     1 
HETATM 1959 O  O     . HOH   E 5 .   ? -6.73500  -11.79400 20.91700  1.000 23.70080 ?  405 HOH   A O     1 
HETATM 1960 O  O     . HOH   E 5 .   ? -9.10700  -2.96500  20.49600  1.000 37.08509 ?  406 HOH   A O     1 
HETATM 1961 O  O     . HOH   E 5 .   ? -11.09300 -6.44700  -13.83300 1.000 26.49054 ?  407 HOH   A O     1 
HETATM 1962 O  O     . HOH   E 5 .   ? -31.378   -33.770   19.049    1.000 39.72658 ?  408 HOH   A O     1 
HETATM 1963 O  O     . HOH   E 5 .   ? -30.69900 -17.65900 2.93400   1.000 33.02996 ?  409 HOH   A O     1 
HETATM 1964 O  O     . HOH   E 5 .   ? -23.22900 -29.37300 1.17100   1.000 39.37429 ?  410 HOH   A O     1 
HETATM 1965 O  O     . HOH   E 5 .   ? -24.50600 -28.32300 -2.71200  1.000 39.09914 ?  411 HOH   A O     1 
HETATM 1966 O  O     . HOH   E 5 .   ? -10.61800 -15.07300 -16.93800 1.000 29.40115 ?  412 HOH   A O     1 
HETATM 1967 O  O     . HOH   E 5 .   ? -13.89600 -17.07800 6.15100   1.000 19.32313 ?  413 HOH   A O     1 
HETATM 1968 O  O     . HOH   E 5 .   ? -27.57300 -9.51000  21.24900  1.000 28.87724 ?  414 HOH   A O     1 
HETATM 1969 O  O     . HOH   E 5 .   ? -23.35200 -31.32700 4.54500   1.000 36.57386 ?  415 HOH   A O     1 
HETATM 1970 O  O     . HOH   E 5 .   ? -30.25300 -19.86500 20.12300  1.000 34.66691 ?  416 HOH   A O     1 
HETATM 1971 O  O     . HOH   E 5 .   ? -0.67500  -20.61500 5.35900   1.000 37.03812 ?  417 HOH   A O     1 
HETATM 1972 O  O     . HOH   E 5 .   ? -26.70400 -27.03500 10.12200  1.000 37.76402 ?  418 HOH   A O     1 
HETATM 1973 O  O     . HOH   E 5 .   ? -2.37000  -9.96300  -2.32200  1.000 38.71071 ?  419 HOH   A O     1 
HETATM 1974 O  O     . HOH   E 5 .   ? -26.07400 -29.95100 12.25300  1.000 44.91737 ?  420 HOH   A O     1 
HETATM 1975 O  O     . HOH   E 5 .   ? -13.01500 -9.73700  -3.86400  1.000 22.22846 ?  421 HOH   A O     1 
HETATM 1976 O  O     . HOH   E 5 .   ? -32.28100 -17.62600 14.92300  1.000 47.23396 ?  422 HOH   A O     1 
HETATM 1977 O  O     . HOH   E 5 .   ? -15.99000 0.53800   -2.03900  1.000 28.96524 ?  423 HOH   A O     1 
HETATM 1978 O  O     . HOH   E 5 .   ? -7.72100  -23.75900 29.29000  1.000 32.58012 ?  424 HOH   A O     1 
HETATM 1979 O  O     . HOH   E 5 .   ? -9.66900  -16.85700 -15.90400 1.000 45.00887 ?  425 HOH   A O     1 
HETATM 1980 O  O     . HOH   E 5 .   ? -8.88100  -10.01600 -1.46400  1.000 26.83550 ?  426 HOH   A O     1 
HETATM 1981 O  O     . HOH   E 5 .   ? -12.30800 -4.66900  26.09000  1.000 43.51907 ?  427 HOH   A O     1 
HETATM 1982 O  O     . HOH   E 5 .   ? -22.53000 10.71400  27.77600  1.000 28.82194 ?  428 HOH   A O     1 
HETATM 1983 O  O     . HOH   E 5 .   ? 0.12300   -14.91300 9.03700   1.000 40.03814 ?  429 HOH   A O     1 
HETATM 1984 O  O     . HOH   E 5 .   ? -29.48200 -25.92500 -4.13700  1.000 32.40876 ?  430 HOH   A O     1 
HETATM 1985 O  O     . HOH   E 5 .   ? -10.11800 -12.85700 29.57400  1.000 22.46714 ?  431 HOH   A O     1 
HETATM 1986 O  O     . HOH   E 5 .   ? -4.01200  -23.74700 6.22800   1.000 37.38790 ?  432 HOH   A O     1 
HETATM 1987 O  O     . HOH   E 5 .   ? -9.28500  -33.61500 19.04200  1.000 36.94034 ?  433 HOH   A O     1 
HETATM 1988 O  O     . HOH   E 5 .   ? -17.05000 -36.34200 14.00600  1.000 34.11752 ?  434 HOH   A O     1 
HETATM 1989 O  O     . HOH   E 5 .   ? -20.79600 -22.07300 30.58400  1.000 35.68017 ?  435 HOH   A O     1 
HETATM 1990 O  O     . HOH   E 5 .   ? -18.10800 -11.80100 31.91800  1.000 30.86886 ?  436 HOH   A O     1 
HETATM 1991 O  O     . HOH   E 5 .   ? -15.62400 -3.98200  4.04200   1.000 22.66843 ?  437 HOH   A O     1 
HETATM 1992 O  O     . HOH   E 5 .   ? -16.59900 0.94100   -10.59800 1.000 19.86009 ?  438 HOH   A O     1 
HETATM 1993 O  O     . HOH   E 5 .   ? -5.27500  -10.21200 5.04100   1.000 19.97302 ?  439 HOH   A O     1 
HETATM 1994 O  O     . HOH   E 5 .   ? -11.31900 -18.44200 33.62700  1.000 22.24628 ?  440 HOH   A O     1 
HETATM 1995 O  O     . HOH   E 5 .   ? -30.30300 -24.42000 18.75400  1.000 37.21424 ?  441 HOH   A O     1 
HETATM 1996 O  O     . HOH   E 5 .   ? -10.33700 -30.69700 27.33000  1.000 34.05736 ?  442 HOH   A O     1 
HETATM 1997 O  O     . HOH   E 5 .   ? -25.19000 1.83900   12.13100  1.000 28.61621 ?  443 HOH   A O     1 
HETATM 1998 O  O     . HOH   E 5 .   ? -2.04100  -25.17000 15.67900  1.000 35.71470 ?  444 HOH   A O     1 
HETATM 1999 O  O     . HOH   E 5 .   ? -18.51900 -28.54900 26.38600  1.000 34.11362 ?  445 HOH   A O     1 
HETATM 2000 O  O     . HOH   E 5 .   ? -28.25100 -13.04800 9.53300   1.000 33.88840 ?  446 HOH   A O     1 
HETATM 2001 O  O     . HOH   E 5 .   ? -12.39100 -14.94500 7.03400   1.000 21.67140 ?  447 HOH   A O     1 
HETATM 2002 O  O     . HOH   E 5 .   ? -10.47100 -17.22800 -8.66500  1.000 36.03077 ?  448 HOH   A O     1 
HETATM 2003 O  O     . HOH   E 5 .   ? -20.86900 -1.58500  -6.08400  1.000 34.03252 ?  449 HOH   A O     1 
HETATM 2004 O  O     . HOH   E 5 .   ? -30.84700 -20.77900 4.66400   1.000 30.59680 ?  450 HOH   A O     1 
HETATM 2005 O  O     . HOH   E 5 .   ? -17.10700 -12.69000 13.74400  1.000 18.39313 ?  451 HOH   A O     1 
HETATM 2006 O  O     . HOH   E 5 .   ? -31.92400 -20.24000 0.84200   1.000 41.54962 ?  452 HOH   A O     1 
HETATM 2007 O  O     . HOH   E 5 .   ? -21.09200 -4.26300  2.54600   1.000 23.12916 ?  453 HOH   A O     1 
HETATM 2008 O  O     . HOH   E 5 .   ? -12.093   -27.646   -16.380   1.000 41.42601 ?  454 HOH   A O     1 
HETATM 2009 O  O     . HOH   E 5 .   ? -10.09600 -4.89000  26.42700  1.000 44.97319 ?  455 HOH   A O     1 
HETATM 2010 O  O     . HOH   E 5 .   ? -9.16800  -11.42500 -3.84400  1.000 30.13314 ?  456 HOH   A O     1 
HETATM 2011 O  O     . HOH   E 5 .   ? -1.92800  -23.28500 25.99300  1.000 33.67137 ?  457 HOH   A O     1 
HETATM 2012 O  O     . HOH   E 5 .   ? -15.60200 -32.94900 1.31600   1.000 34.77516 ?  458 HOH   A O     1 
HETATM 2013 O  O     . HOH   E 5 .   ? -28.423   -22.826   20.429    1.000 28.76630 ?  459 HOH   A O     1 
HETATM 2014 O  O     . HOH   E 5 .   ? -22.59200 -22.48700 26.10900  1.000 23.24869 ?  460 HOH   A O     1 
HETATM 2015 O  O     . HOH   E 5 .   ? -16.11400 -17.70800 9.13400   1.000 17.76393 ?  461 HOH   A O     1 
HETATM 2016 O  O     . HOH   E 5 .   ? -20.930   -20.199   -10.848   1.000 39.84897 ?  462 HOH   A O     1 
HETATM 2017 O  O     . HOH   E 5 .   ? -12.31800 -9.82200  -20.32300 1.000 35.83764 ?  463 HOH   A O     1 
HETATM 2018 O  O     . HOH   E 5 .   ? -12.561   3.665     17.004    1.000 25.71854 ?  464 HOH   A O     1 
HETATM 2019 O  O     . HOH   E 5 .   ? -9.51400  -6.29400  -10.58200 1.000 28.11563 ?  465 HOH   A O     1 
HETATM 2020 O  O     . HOH   E 5 .   ? -4.68000  -33.58200 12.51300  1.000 37.46849 ?  466 HOH   A O     1 
HETATM 2021 O  O     . HOH   E 5 .   ? -14.538   4.167     22.740    1.000 49.76861 ?  467 HOH   A O     1 
HETATM 2022 O  O     . HOH   E 5 .   ? -3.54800  -21.72100 0.33000   1.000 31.22202 ?  468 HOH   A O     1 
HETATM 2023 O  O     . HOH   E 5 .   ? -15.20900 -9.82600  -20.80000 1.000 28.00372 ?  469 HOH   A O     1 
HETATM 2024 O  O     . HOH   E 5 .   ? -34.91800 -1.54800  16.35700  1.000 45.41049 ?  470 HOH   A O     1 
HETATM 2025 O  O     . HOH   E 5 .   ? -24.85600 -5.29300  12.41200  1.000 21.65220 ?  471 HOH   A O     1 
HETATM 2026 O  O     . HOH   E 5 .   ? -23.29800 -28.85300 20.14100  1.000 19.99337 ?  472 HOH   A O     1 
HETATM 2027 O  O     . HOH   E 5 .   ? -24.56500 -15.75200 -3.44000  1.000 23.77320 ?  473 HOH   A O     1 
HETATM 2028 O  O     . HOH   E 5 .   ? -1.17900  -14.40800 5.01100   1.000 31.42780 ?  474 HOH   A O     1 
HETATM 2029 O  O     . HOH   E 5 .   ? -12.83300 -9.52200  17.57400  1.000 19.85983 ?  475 HOH   A O     1 
HETATM 2030 O  O     . HOH   E 5 .   ? -20.48000 -9.19500  -8.35500  1.000 35.98553 ?  476 HOH   A O     1 
HETATM 2031 O  O     . HOH   E 5 .   ? -23.87000 -9.19000  -18.24500 1.000 33.50814 ?  477 HOH   A O     1 
HETATM 2032 O  O     . HOH   E 5 .   ? -4.58100  -26.04700 25.02300  1.000 27.66579 ?  478 HOH   A O     1 
HETATM 2033 O  O     . HOH   E 5 .   ? -4.09300  -11.88700 19.08100  1.000 37.91795 ?  479 HOH   A O     1 
HETATM 2034 O  O     . HOH   E 5 .   ? -13.96600 0.42000   -15.84400 1.000 19.75489 ?  480 HOH   A O     1 
HETATM 2035 O  O     . HOH   E 5 .   ? -29.11700 -10.29000 10.04000  1.000 28.11664 ?  481 HOH   A O     1 
HETATM 2036 O  O     . HOH   E 5 .   ? -12.07100 -2.91100  19.76800  1.000 28.72830 ?  482 HOH   A O     1 
HETATM 2037 O  O     . HOH   E 5 .   ? -22.51300 -6.81600  -14.00200 1.000 29.67928 ?  483 HOH   A O     1 
HETATM 2038 O  O     . HOH   E 5 .   ? -31.76100 -12.64000 -2.25500  1.000 38.07416 ?  484 HOH   A O     1 
HETATM 2039 O  O     . HOH   E 5 .   ? -33.574   -32.401   20.758    1.000 46.00455 ?  485 HOH   A O     1 
HETATM 2040 O  O     . HOH   E 5 .   ? -26.84200 -15.27000 5.07000   1.000 22.89076 ?  486 HOH   A O     1 
HETATM 2041 O  O     . HOH   E 5 .   ? -33.09000 -20.62000 12.52600  1.000 36.92696 ?  487 HOH   A O     1 
HETATM 2042 O  O     . HOH   E 5 .   ? -6.07000  -23.98000 21.96300  1.000 20.44824 ?  488 HOH   A O     1 
HETATM 2043 O  O     . HOH   E 5 .   ? -2.53800  -5.46100  10.45100  1.000 35.99029 ?  489 HOH   A O     1 
HETATM 2044 O  O     . HOH   E 5 .   ? -12.39300 -8.19800  31.76800  1.000 42.83154 ?  490 HOH   A O     1 
HETATM 2045 O  O     . HOH   E 5 .   ? -14.66200 -34.12000 -1.56200  1.000 41.92368 ?  491 HOH   A O     1 
HETATM 2046 O  O     . HOH   E 5 .   ? -20.00600 2.05100   -1.60800  1.000 27.18643 ?  492 HOH   A O     1 
HETATM 2047 O  O     . HOH   E 5 .   ? -6.82200  -4.37000  17.30400  1.000 33.39746 ?  493 HOH   A O     1 
HETATM 2048 O  O     . HOH   E 5 .   ? -7.29500  -12.04000 29.40700  1.000 30.76069 ?  494 HOH   A O     1 
HETATM 2049 O  O     . HOH   E 5 .   ? -4.95600  -8.64400  -8.96300  1.000 35.71461 ?  495 HOH   A O     1 
HETATM 2050 O  O     . HOH   E 5 .   ? -3.04900  -14.83300 3.25400   1.000 22.43193 ?  496 HOH   A O     1 
HETATM 2051 O  O     . HOH   E 5 .   ? -22.30900 -5.65200  -10.48600 1.000 38.70350 ?  497 HOH   A O     1 
HETATM 2052 O  O     . HOH   E 5 .   ? -12.94800 -35.96600 8.02600   1.000 39.54013 ?  498 HOH   A O     1 
HETATM 2053 O  O     . HOH   E 5 .   ? -19.663   0.653     12.957    1.000 19.90105 ?  499 HOH   A O     1 
HETATM 2054 O  O     . HOH   E 5 .   ? -6.11000  -17.21200 -6.87100  1.000 40.81798 ?  500 HOH   A O     1 
HETATM 2055 O  O     . HOH   E 5 .   ? -31.37700 -28.98800 17.57500  1.000 34.41995 ?  501 HOH   A O     1 
HETATM 2056 O  O     . HOH   E 5 .   ? -33.23800 -10.54600 16.98300  1.000 49.19167 ?  502 HOH   A O     1 
HETATM 2057 O  O     . HOH   E 5 .   ? -16.72000 -27.10500 27.22000  1.000 34.70731 ?  503 HOH   A O     1 
HETATM 2058 O  O     . HOH   E 5 .   ? -10.53900 -22.85500 -16.21000 1.000 43.55624 ?  504 HOH   A O     1 
HETATM 2059 O  O     . HOH   E 5 .   ? -23.31000 -19.39900 27.75700  1.000 31.14118 ?  505 HOH   A O     1 
HETATM 2060 O  O     . HOH   E 5 .   ? -21.56600 1.01900   11.03900  1.000 25.79208 ?  506 HOH   A O     1 
HETATM 2061 O  O     . HOH   E 5 .   ? -1.01300  -2.67300  1.04300   1.000 41.57065 ?  507 HOH   A O     1 
HETATM 2062 O  O     . HOH   E 5 .   ? -22.63400 -5.48700  26.28300  1.000 31.52471 ?  508 HOH   A O     1 
HETATM 2063 O  O     . HOH   E 5 .   ? -15.11700 -0.50500  -13.40700 1.000 20.03784 ?  509 HOH   A O     1 
HETATM 2064 O  O     . HOH   E 5 .   ? -17.981   -13.506   -19.330   1.000 22.27137 ?  510 HOH   A O     1 
HETATM 2065 O  O     . HOH   E 5 .   ? -28.60700 -19.15900 22.16700  1.000 35.59994 ?  511 HOH   A O     1 
HETATM 2066 O  O     . HOH   E 5 .   ? -6.45200  -8.99100  -1.53000  1.000 27.97206 ?  512 HOH   A O     1 
HETATM 2067 O  O     . HOH   E 5 .   ? 0.14400   -20.44900 10.98100  1.000 31.84333 ?  513 HOH   A O     1 
HETATM 2068 O  O     . HOH   E 5 .   ? -24.604   -14.506   25.900    1.000 34.74852 ?  514 HOH   A O     1 
HETATM 2069 O  O     . HOH   E 5 .   ? -8.23100  -28.95100 21.91700  1.000 26.49699 ?  515 HOH   A O     1 
HETATM 2070 O  O     . HOH   E 5 .   ? -24.73400 -7.13900  25.96500  1.000 32.94472 ?  516 HOH   A O     1 
HETATM 2071 O  O     . HOH   E 5 .   ? -17.06900 -27.76600 -11.18000 1.000 26.70948 ?  517 HOH   A O     1 
HETATM 2072 O  O     . HOH   E 5 .   ? -30.29300 -15.71500 12.95600  1.000 34.33105 ?  518 HOH   A O     1 
HETATM 2073 O  O     . HOH   E 5 .   ? -17.02700 -5.82400  29.46500  1.000 33.92766 ?  519 HOH   A O     1 
HETATM 2074 O  O     . HOH   E 5 .   ? -8.97100  -12.13300 0.42800   1.000 21.41042 ?  520 HOH   A O     1 
HETATM 2075 O  O     . HOH   E 5 .   ? -22.65700 -3.48100  -12.42800 1.000 26.84812 ?  521 HOH   A O     1 
HETATM 2076 O  O     . HOH   E 5 .   ? -3.95400  -3.06700  4.21400   1.000 23.63253 ?  522 HOH   A O     1 
HETATM 2077 O  O     . HOH   E 5 .   ? -22.71300 -28.25100 -4.62500  1.000 37.77885 ?  523 HOH   A O     1 
HETATM 2078 O  O     . HOH   E 5 .   ? -29.97000 -18.74100 -3.88600  1.000 35.60894 ?  524 HOH   A O     1 
HETATM 2079 O  O     . HOH   E 5 .   ? -16.12200 -9.73300  31.88500  1.000 35.95598 ?  525 HOH   A O     1 
HETATM 2080 O  O     . HOH   E 5 .   ? -9.17900  -34.57700 -0.65900  1.000 41.80527 ?  526 HOH   A O     1 
HETATM 2081 O  O     . HOH   E 5 .   ? -30.201   -4.606    -20.085   1.000 49.60480 ?  527 HOH   A O     1 
HETATM 2082 O  O     . HOH   E 5 .   ? -23.96000 -7.29800  15.80400  1.000 20.49013 ?  528 HOH   A O     1 
HETATM 2083 O  O     . HOH   E 5 .   ? -21.11500 -16.47100 -11.60700 1.000 35.03406 ?  529 HOH   A O     1 
HETATM 2084 O  O     . HOH   E 5 .   ? -2.11800  -13.56800 9.50400   1.000 32.09920 ?  530 HOH   A O     1 
HETATM 2085 O  O     . HOH   E 5 .   ? -15.98000 -10.94300 4.74100   1.000 18.79042 ?  531 HOH   A O     1 
HETATM 2086 O  O     . HOH   E 5 .   ? -4.36300  -29.86000 0.90900   1.000 35.43265 ?  532 HOH   A O     1 
HETATM 2087 O  O     . HOH   E 5 .   ? -28.98600 -24.13500 12.37600  1.000 27.42815 ?  533 HOH   A O     1 
HETATM 2088 O  O     . HOH   E 5 .   ? -12.44300 -35.88200 13.93800  1.000 35.24148 ?  534 HOH   A O     1 
HETATM 2089 O  O     . HOH   E 5 .   ? 1.14600   -11.44300 23.97700  1.000 44.92381 ?  535 HOH   A O     1 
HETATM 2090 O  O     . HOH   E 5 .   ? -2.28600  -31.75400 12.17200  1.000 46.82405 ?  536 HOH   A O     1 
HETATM 2091 O  O     . HOH   E 5 .   ? -2.78000  -5.11200  15.41300  1.000 38.62737 ?  537 HOH   A O     1 
HETATM 2092 O  O     . HOH   E 5 .   ? 3.80700   -3.70600  -5.48500  1.000 56.38627 ?  538 HOH   A O     1 
HETATM 2093 O  O     . HOH   E 5 .   ? -9.02100  -36.83500 8.41200   1.000 37.74457 ?  539 HOH   A O     1 
HETATM 2094 O  O     . HOH   E 5 .   ? -25.440   6.681     28.212    1.000 38.86206 ?  540 HOH   A O     1 
HETATM 2095 O  O     . HOH   E 5 .   ? -8.34000  -28.64200 -8.05000  1.000 35.12825 ?  541 HOH   A O     1 
HETATM 2096 O  O     . HOH   E 5 .   ? -8.27100  -20.14600 -7.34500  1.000 25.97963 ?  542 HOH   A O     1 
HETATM 2097 O  O     . HOH   E 5 .   ? -14.68100 2.85200   -19.82000 1.000 26.90122 ?  543 HOH   A O     1 
HETATM 2098 O  O     . HOH   E 5 .   ? -14.21800 -4.86500  29.09000  1.000 36.74852 ?  544 HOH   A O     1 
HETATM 2099 O  O     . HOH   E 5 .   ? -32.72100 -1.24200  14.94200  1.000 31.44711 ?  545 HOH   A O     1 
HETATM 2100 O  O     . HOH   E 5 .   ? -22.68000 -7.35700  -21.49200 1.000 30.82030 ?  546 HOH   A O     1 
HETATM 2101 O  O     . HOH   E 5 .   ? -21.63700 -4.91700  28.40700  1.000 42.36606 ?  547 HOH   A O     1 
HETATM 2102 O  O     . HOH   E 5 .   ? -2.18900  -7.33700  -5.13800  1.000 32.93836 ?  548 HOH   A O     1 
HETATM 2103 O  O     . HOH   E 5 .   ? -19.92000 -6.81500  0.43800   1.000 23.54452 ?  549 HOH   A O     1 
HETATM 2104 O  O     . HOH   E 5 .   ? -24.544   5.630     22.280    1.000 31.31788 ?  550 HOH   A O     1 
HETATM 2105 O  O     . HOH   E 5 .   ? -9.55000  -17.13700 -13.28000 1.000 32.15736 ?  551 HOH   A O     1 
HETATM 2106 O  O     . HOH   E 5 .   ? -27.03000 -28.21100 4.04600   1.000 29.60643 ?  552 HOH   A O     1 
HETATM 2107 O  O     . HOH   E 5 .   ? -26.68600 -26.03800 12.79000  1.000 34.13830 ?  553 HOH   A O     1 
HETATM 2108 O  O     . HOH   E 5 .   ? -11.34600 -14.56800 31.29900  1.000 30.35234 ?  554 HOH   A O     1 
HETATM 2109 O  O     . HOH   E 5 .   ? -15.52500 -9.14100  -7.97000  1.000 20.01387 ?  555 HOH   A O     1 
HETATM 2110 O  O     . HOH   E 5 .   ? -10.08800 -8.03000  -16.02400 1.000 36.36193 ?  556 HOH   A O     1 
HETATM 2111 O  O     . HOH   E 5 .   ? -11.56900 1.15400   -17.64800 1.000 31.90175 ?  557 HOH   A O     1 
HETATM 2112 O  O     . HOH   E 5 .   ? -3.77500  -33.39400 17.73300  1.000 43.61237 ?  558 HOH   A O     1 
HETATM 2113 O  O     . HOH   E 5 .   ? -19.51100 -9.03200  -20.93900 1.000 26.88395 ?  559 HOH   A O     1 
HETATM 2114 O  O     . HOH   E 5 .   ? -3.39600  -4.20500  -6.95600  1.000 37.91347 ?  560 HOH   A O     1 
HETATM 2115 O  O     . HOH   E 5 .   ? -19.85400 -30.67300 1.85400   1.000 28.06060 ?  561 HOH   A O     1 
HETATM 2116 O  O     . HOH   E 5 .   ? -3.25800  -12.67300 27.68600  1.000 38.51741 ?  562 HOH   A O     1 
HETATM 2117 O  O     . HOH   E 5 .   ? -3.51700  -29.97600 -2.45000  1.000 37.62665 ?  563 HOH   A O     1 
HETATM 2118 O  O     . HOH   E 5 .   ? -27.24000 -10.07600 -8.05500  1.000 29.65844 ?  564 HOH   A O     1 
HETATM 2119 O  O     . HOH   E 5 .   ? -25.32300 0.83400   4.98400   1.000 41.41864 ?  565 HOH   A O     1 
HETATM 2120 O  O     . HOH   E 5 .   ? -6.14800  -16.68400 -3.35700  1.000 30.11527 ?  566 HOH   A O     1 
HETATM 2121 O  O     . HOH   E 5 .   ? -27.41900 -22.30500 -5.54700  1.000 33.16582 ?  567 HOH   A O     1 
HETATM 2122 O  O     . HOH   E 5 .   ? -3.74400  -17.25300 -1.86700  1.000 37.36805 ?  568 HOH   A O     1 
HETATM 2123 O  O     . HOH   E 5 .   ? -7.88000  -9.57200  1.46800   1.000 21.69169 ?  569 HOH   A O     1 
HETATM 2124 O  O     . HOH   E 5 .   ? -7.62800  -30.91900 23.64000  1.000 43.46525 ?  570 HOH   A O     1 
HETATM 2125 O  O     . HOH   E 5 .   ? -1.52700  -27.74900 18.54400  1.000 45.01013 ?  571 HOH   A O     1 
HETATM 2126 O  O     . HOH   E 5 .   ? -33.54600 -3.33100  12.81600  1.000 36.29869 ?  572 HOH   A O     1 
HETATM 2127 O  O     . HOH   E 5 .   ? -6.87500  -13.19200 -2.38200  1.000 32.82134 ?  573 HOH   A O     1 
HETATM 2128 O  O     . HOH   E 5 .   ? -10.23100 -33.41500 21.69700  1.000 46.77386 ?  574 HOH   A O     1 
HETATM 2129 O  O     . HOH   E 5 .   ? -23.61600 -5.99000  18.23000  1.000 23.65396 ?  575 HOH   A O     1 
HETATM 2130 O  O     . HOH   E 5 .   ? -19.98000 -15.16300 33.01100  1.000 37.81376 ?  576 HOH   A O     1 
HETATM 2131 O  O     . HOH   E 5 .   ? -18.27100 -33.90500 19.95700  1.000 27.69419 ?  577 HOH   A O     1 
HETATM 2132 O  O     . HOH   E 5 .   ? -17.93300 -8.58000  -9.18000  1.000 26.62452 ?  578 HOH   A O     1 
HETATM 2133 O  O     . HOH   E 5 .   ? -19.13700 -23.48300 -11.69700 1.000 30.65387 ?  579 HOH   A O     1 
HETATM 2134 O  O     . HOH   E 5 .   ? -22.05200 -2.94600  4.68000   1.000 30.31424 ?  580 HOH   A O     1 
HETATM 2135 O  O     . HOH   E 5 .   ? -4.92100  -4.40700  20.79300  1.000 37.48587 ?  581 HOH   A O     1 
HETATM 2136 O  O     . HOH   E 5 .   ? -20.40900 -31.60500 -7.31600  1.000 36.55194 ?  582 HOH   A O     1 
HETATM 2137 O  O     . HOH   E 5 .   ? -16.60100 -22.70500 32.45700  1.000 32.23642 ?  583 HOH   A O     1 
HETATM 2138 O  O     . HOH   E 5 .   ? -9.17800  -8.71100  -10.68100 1.000 30.30860 ?  584 HOH   A O     1 
HETATM 2139 O  O     . HOH   E 5 .   ? -6.28100  -5.95500  23.28300  1.000 35.55631 ?  585 HOH   A O     1 
HETATM 2140 O  O     . HOH   E 5 .   ? -3.11500  -19.79500 26.90500  1.000 43.12998 ?  586 HOH   A O     1 
HETATM 2141 O  O     . HOH   E 5 .   ? -19.31900 -26.74100 28.93400  1.000 33.54162 ?  587 HOH   A O     1 
HETATM 2142 O  O     . HOH   E 5 .   ? -4.43000  -1.42500  11.24900  1.000 33.99293 ?  588 HOH   A O     1 
HETATM 2143 O  O     . HOH   E 5 .   ? -3.10600  -33.64100 9.13300   1.000 53.40131 ?  589 HOH   A O     1 
HETATM 2144 O  O     . HOH   E 5 .   ? -21.85500 -4.55700  -2.32700  1.000 42.74278 ?  590 HOH   A O     1 
HETATM 2145 O  O     . HOH   E 5 .   ? -23.77300 -7.02600  2.72500   1.000 35.58859 ?  591 HOH   A O     1 
HETATM 2146 O  O     . HOH   E 5 .   ? -21.04600 -14.88400 -9.94500  1.000 37.79883 ?  592 HOH   A O     1 
HETATM 2147 O  O     . HOH   E 5 .   ? -7.52900  -20.09500 -9.70900  1.000 39.68340 ?  593 HOH   A O     1 
HETATM 2148 O  O     . HOH   E 5 .   ? -8.24900  -0.70700  -11.58800 1.000 36.59842 ?  594 HOH   A O     1 
HETATM 2149 O  O     . HOH   E 5 .   ? -0.00600  -5.26700  2.77300   1.000 46.10228 ?  595 HOH   A O     1 
HETATM 2150 O  O     . HOH   E 5 .   ? -31.50600 -31.33400 16.09500  1.000 45.34439 ?  596 HOH   A O     1 
HETATM 2151 O  O     . HOH   E 5 .   ? -24.88200 -32.17700 13.22200  1.000 38.80857 ?  597 HOH   A O     1 
HETATM 2152 O  O     . HOH   E 5 .   ? -8.84800  -13.26800 -15.42000 1.000 37.30445 ?  598 HOH   A O     1 
HETATM 2153 O  O     . HOH   E 5 .   ? -28.06800 -12.87700 6.24600   1.000 30.26405 ?  599 HOH   A O     1 
HETATM 2154 O  O     . HOH   E 5 .   ? -11.28600 -31.68000 -4.58700  1.000 41.03587 ?  600 HOH   A O     1 
HETATM 2155 O  O     . HOH   E 5 .   ? -7.777    0.068     13.765    1.000 40.64667 ?  601 HOH   A O     1 
HETATM 2156 O  O     . HOH   E 5 .   ? -12.49200 -30.26700 -15.75000 1.000 46.72893 ?  602 HOH   A O     1 
HETATM 2157 O  O     . HOH   E 5 .   ? 1.02600   -16.03800 11.59200  1.000 43.37424 ?  603 HOH   A O     1 
HETATM 2158 O  O     . HOH   E 5 .   ? -5.79600  -34.89500 17.33800  1.000 41.85804 ?  604 HOH   A O     1 
HETATM 2159 O  O     . HOH   E 5 .   ? -21.29100 -10.40200 -11.95200 1.000 40.14735 ?  605 HOH   A O     1 
HETATM 2160 O  O     . HOH   E 5 .   ? -30.64700 -9.61100  7.73200   1.000 40.43006 ?  606 HOH   A O     1 
HETATM 2161 O  O     . HOH   E 5 .   ? -11.75400 -2.31700  24.77000  1.000 44.45723 ?  607 HOH   A O     1 
HETATM 2162 O  O     . HOH   E 5 .   ? -15.48900 -34.24400 19.10200  1.000 42.85258 ?  608 HOH   A O     1 
HETATM 2163 O  O     . HOH   E 5 .   ? -6.88900  -5.48000  29.85300  1.000 51.91208 ?  609 HOH   A O     1 
HETATM 2164 O  O     . HOH   E 5 .   ? -3.71700  -13.35700 -2.83700  1.000 39.29755 ?  610 HOH   A O     1 
HETATM 2165 O  O     . HOH   E 5 .   ? -30.37900 -14.60500 10.27800  1.000 38.86529 ?  611 HOH   A O     1 
HETATM 2166 O  O     . HOH   E 5 .   ? -4.14600  -15.06700 28.33000  1.000 40.18883 ?  612 HOH   A O     1 
HETATM 2167 O  O     . HOH   E 5 .   ? -2.82500  -13.02300 20.68200  1.000 35.58935 ?  613 HOH   A O     1 
HETATM 2168 O  O     . HOH   E 5 .   ? -2.12400  -11.33800 10.36900  1.000 50.83566 ?  614 HOH   A O     1 
HETATM 2169 O  O     . HOH   E 5 .   ? -24.71000 -5.20100  30.41300  1.000 45.20044 ?  615 HOH   A O     1 
HETATM 2170 O  O     . HOH   E 5 .   ? -2.32900  -6.85900  -7.39300  1.000 46.61426 ?  616 HOH   A O     1 
HETATM 2171 O  O     . HOH   E 5 .   ? -31.90200 -16.39100 10.47800  1.000 46.06348 ?  617 HOH   A O     1 
HETATM 2172 O  O     . HOH   E 5 .   ? -15.81900 -29.80200 -12.72500 1.000 35.07907 ?  618 HOH   A O     1 
HETATM 2173 O  O     . HOH   E 5 .   ? -24.64800 -3.57300  3.57600   1.000 42.21518 ?  619 HOH   A O     1 
HETATM 2174 O  O     . HOH   E 5 .   ? -25.22500 -33.75600 9.33300   1.000 52.86162 ?  620 HOH   A O     1 
HETATM 2175 O  O     . HOH   E 5 .   ? -8.05700  -13.23600 -12.83000 1.000 37.77554 ?  621 HOH   A O     1 
HETATM 2176 O  O     . HOH   E 5 .   ? -17.64900 0.00000   0.00000   0.50  40.51619 ?  622 HOH   A O     1 
HETATM 2177 O  O     . HOH   E 5 .   ? -5.67900  -4.01000  -7.31400  1.000 32.08049 ?  623 HOH   A O     1 
HETATM 2178 O  O     . HOH   E 5 .   ? -21.78700 -0.13300  -2.14300  1.000 32.29754 ?  624 HOH   A O     1 
HETATM 2179 O  O     . HOH   E 5 .   ? -8.09200  -20.53800 29.77900  1.000 36.56585 ?  625 HOH   A O     1 
HETATM 2180 O  O     . HOH   E 5 .   ? -7.73100  -8.80100  -14.88000 1.000 45.22908 ?  626 HOH   A O     1 
HETATM 2181 O  O     . HOH   E 5 .   ? -26.12600 -28.72600 1.29500   1.000 45.71792 ?  627 HOH   A O     1 
HETATM 2182 O  O     . HOH   E 5 .   ? -22.64200 -6.35800  0.95100   1.000 39.44471 ?  628 HOH   A O     1 
HETATM 2183 O  O     . HOH   E 5 .   ? -15.327   -36.845   21.149    1.000 44.29717 ?  629 HOH   A O     1 
HETATM 2184 O  O     . HOH   E 5 .   ? -1.015    -0.939    -3.633    1.000 39.80650 ?  630 HOH   A O     1 
HETATM 2185 O  O     . HOH   E 5 .   ? -32.57400 -7.99400  11.49900  1.000 47.13413 ?  631 HOH   A O     1 
HETATM 2186 O  O     . HOH   E 5 .   ? -18.948   -33.489   27.190    1.000 38.92956 ?  632 HOH   A O     1 
HETATM 2187 O  O     . HOH   E 5 .   ? -30.77300 -8.41400  -1.73200  1.000 41.43183 ?  633 HOH   A O     1 
HETATM 2188 O  O     . HOH   E 5 .   ? -21.735   9.663     21.994    1.000 39.07325 ?  634 HOH   A O     1 
HETATM 2189 O  O     . HOH   E 5 .   ? -16.76000 -7.49000  31.37000  1.000 38.74204 ?  635 HOH   A O     1 
HETATM 2190 O  O     . HOH   E 5 .   ? -30.72700 -8.71400  5.44100   1.000 45.01406 ?  636 HOH   A O     1 
HETATM 2191 O  O     . HOH   E 5 .   ? -12.338   6.876     21.331    1.000 46.76845 ?  637 HOH   A O     1 
HETATM 2192 O  O     . HOH   E 5 .   ? -25.22100 -6.46600  -14.04100 1.000 48.99109 ?  638 HOH   A O     1 
HETATM 2193 O  O     . HOH   E 5 .   ? -4.99800  -28.37300 25.60100  1.000 40.77178 ?  639 HOH   A O     1 
HETATM 2194 O  O     . HOH   E 5 .   ? -22.20000 0.31100   -4.73000  1.000 29.66204 ?  640 HOH   A O     1 
HETATM 2195 O  O     . HOH   E 5 .   ? -31.38300 2.62400   22.10400  1.000 45.20555 ?  641 HOH   A O     1 
HETATM 2196 O  O     . HOH   E 5 .   ? -7.61200  -27.71800 30.01300  1.000 48.26332 ?  642 HOH   A O     1 
HETATM 2197 O  O     . HOH   E 5 .   ? -0.57500  -21.04000 -2.68600  1.000 50.63315 ?  643 HOH   A O     1 
HETATM 2198 O  O     . HOH   E 5 .   ? -8.73600  -35.92700 18.40600  1.000 44.30325 ?  644 HOH   A O     1 
HETATM 2199 O  O     . HOH   E 5 .   ? -18.96900 -4.07500  29.51300  1.000 40.29638 ?  645 HOH   A O     1 
HETATM 2200 O  O     . HOH   E 5 .   ? -2.12900  -4.12100  20.67200  1.000 49.78270 ?  646 HOH   A O     1 
HETATM 2201 O  O     . HOH   E 5 .   ? -2.64800  -0.77300  1.21500   1.000 46.93288 ?  647 HOH   A O     1 
HETATM 2202 O  O     . HOH   E 5 .   ? -6.20100  -29.12700 28.35900  1.000 49.73729 ?  648 HOH   A O     1 
HETATM 2203 O  O     . HOH   E 5 .   ? -17.50600 -1.34200  29.67500  1.000 48.49463 ?  649 HOH   A O     1 
HETATM 2204 O  O     . HOH   E 5 .   ? -5.92800  0.65100   11.17400  1.000 41.14553 ?  650 HOH   A O     1 
HETATM 2205 O  O     . HOH   E 5 .   ? -5.98900  -2.07000  -8.59400  1.000 38.52733 ?  651 HOH   A O     1 
HETATM 2206 O  O     . HOH   E 5 .   ? -30.61800 -6.50900  3.84400   1.000 47.49946 ?  652 HOH   A O     1 
HETATM 2207 O  O     . HOH   E 5 .   ? -27.79600 1.95400   8.12300   1.000 40.85779 ?  653 HOH   A O     1 
HETATM 2208 O  O     . HOH   E 5 .   ? -10.54900 -15.67700 33.69400  1.000 30.20469 ?  654 HOH   A O     1 
HETATM 2209 O  O     . HOH   E 5 .   ? -8.84400  -15.39400 -11.13300 1.000 41.80632 ?  655 HOH   A O     1 
HETATM 2210 O  O     . HOH   E 5 .   ? -10.206   5.791     18.023    1.000 46.97981 ?  656 HOH   A O     1 
HETATM 2211 O  O     . HOH   E 5 .   ? -4.09800  -3.39400  9.25100   1.000 29.02568 ?  657 HOH   A O     1 
HETATM 2212 O  O     . HOH   E 5 .   ? -32.48200 -18.46300 5.08000   1.000 42.76065 ?  658 HOH   A O     1 
HETATM 2213 O  O     . HOH   E 5 .   ? -1.22200  -12.04900 6.68800   1.000 30.55074 ?  659 HOH   A O     1 
HETATM 2214 O  O     . HOH   E 5 .   ? -31.78300 -15.07700 15.12700  1.000 45.55183 ?  660 HOH   A O     1 
HETATM 2215 O  O     . HOH   E 5 .   ? -2.96900  -9.89300  6.43900   1.000 21.36948 ?  661 HOH   A O     1 
HETATM 2216 O  O     . HOH   E 5 .   ? -1.89700  -5.48000  4.11100   1.000 33.32492 ?  662 HOH   A O     1 
HETATM 2217 O  O     . HOH   E 5 .   ? -24.85900 -30.50600 -2.83200  1.000 40.06493 ?  663 HOH   A O     1 
HETATM 2218 O  O     . HOH   E 5 .   ? 0.84700   -14.15500 3.35100   1.000 40.29272 ?  664 HOH   A O     1 
HETATM 2219 O  O     . HOH   E 5 .   ? -10.95900 -2.02100  21.91800  1.000 40.70696 ?  665 HOH   A O     1 
HETATM 2220 O  O     . HOH   E 5 .   ? -29.731   -2.311    -14.948   1.000 45.29555 ?  666 HOH   A O     1 
HETATM 2221 O  O     . HOH   E 5 .   ? -8.45000  -5.79300  -12.97900 1.000 30.56194 ?  667 HOH   A O     1 
HETATM 2222 O  O     . HOH   E 5 .   ? -0.33400  -22.18900 9.36400   1.000 41.88885 ?  668 HOH   A O     1 
HETATM 2223 O  O     . HOH   E 5 .   ? -8.816    -24.027   32.992    1.000 37.42794 ?  669 HOH   A O     1 
HETATM 2224 O  O     . HOH   E 5 .   ? -1.19600  -6.00900  8.43800   1.000 39.01255 ?  670 HOH   A O     1 
HETATM 2225 O  O     . HOH   E 5 .   ? -21.273   2.028     8.611     1.000 31.59890 ?  671 HOH   A O     1 
HETATM 2226 O  O     . HOH   E 5 .   ? -32.33700 1.37000   14.24000  1.000 43.06361 ?  672 HOH   A O     1 
HETATM 2227 O  O     . HOH   E 5 .   ? -4.42700  -14.70100 31.08200  1.000 41.38769 ?  673 HOH   A O     1 
HETATM 2228 O  O     . HOH   E 5 .   ? -3.57000  -2.19900  6.86100   1.000 32.46763 ?  674 HOH   A O     1 
HETATM 2229 O  O     . HOH   E 5 .   ? -6.30600  -13.30200 31.88700  1.000 42.80616 ?  675 HOH   A O     1 
HETATM 2230 O  O     . HOH   E 5 .   ? -6.14600  -19.13500 29.60000  1.000 39.10015 ?  676 HOH   A O     1 
HETATM 2231 O  O     . HOH   E 5 .   ? -34.23700 -9.50500  13.78100  1.000 48.31978 ?  677 HOH   A O     1 
HETATM 2232 O  O     . HOH   E 5 .   ? -1.43900  -7.64500  6.05900   1.000 28.06535 ?  678 HOH   A O     1 
HETATM 2233 O  O     . HOH   E 5 .   ? 1.12000   -7.92700  5.18000   1.000 44.15241 ?  679 HOH   A O     1 
HETATM 2234 O  O     . HOH   E 5 .   ? -3.354    -0.352    -7.581    1.000 41.94694 ?  680 HOH   A O     1 
HETATM 2235 O  O     . HOH   E 5 .   ? -1.10700  -3.65200  6.48500   1.000 43.57150 ?  681 HOH   A O     1 
HETATM 2236 O  O     . HOH   E 5 .   ? -7.77500  -15.47100 33.80200  1.000 43.33031 ?  682 HOH   A O     1 
# 
